data_7PA8
# 
_entry.id   7PA8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.366 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7PA8         pdb_00007pa8 10.2210/pdb7pa8/pdb 
WWPDB D_1292115683 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7PA8 
_pdbx_database_status.recvd_initial_deposition_date   2021-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stroeh, L.J.'  1 0000-0002-2781-2303 
'Harprecht, C.' 2 0000-0001-9516-251X 
'Freytag, J.'   3 0000-0003-3754-6587 
'Stehle, T.'    4 0000-0002-4571-8548 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural characterization of human neutralizing antibodies against JC and BK polyomavirus' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Harprecht, C.'   1  0000-0001-9516-251X 
primary 'Stroeh, L.J.'    2  0000-0002-2781-2303 
primary 'Senn, L.'        3  ?                   
primary 
;O'Hara, B.A.
;
4  0000-0002-6158-5159 
primary 'Nagel, F.'       5  0000-0003-3456-7075 
primary 'Freytag, J.'     6  0000-0003-3754-6587 
primary 'Stiehrof, Y.D.'  7  0000-0002-1784-1768 
primary 'Atwood, W.J.'    8  0000-0002-3763-9073 
primary 'Combaluzier, B.' 9  0000-0002-1012-8142 
primary 'Stehle, T.'      10 0000-0002-4571-8548 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.115 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7PA8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     137.070 
_cell.length_a_esd                 ? 
_cell.length_b                     110.440 
_cell.length_b_esd                 ? 
_cell.length_c                     158.210 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        10 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7PA8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Major capsid protein VP1' 30075.861 5 ? ? 'UNP residues 23-290' ? 
2 polymer man 'Fab 27C2 light chain'     22227.623 5 ? ? ?                     ? 
3 polymer man 'Fab 27C2 heavy chain'     43524.938 5 ? ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Major structural protein VP1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSHMGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCG
NILMWEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQ
SQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVD
VCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKN
;
;GSHMGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCG
NILMWEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQ
SQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVD
VCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKN
;
AAA,BBB,CCC,DDD,EEE ? 
2 'polypeptide(L)' no no 
;QSVLTQPPSASGTPGQRVTISCSGGSSNIGSNPVNWFQQFPGTAPKLLIYANTQRPSGVPDRFSGSKSGTSVSLAISGLQ
SEDEGDYHCAAWDDSLKGWVFGGGTKLTVLGAPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVK
AGVETTKPSKQSNNKTAASSYLSLTPEQWKSHRSYSCQVTHEGTTVEKTVAP
;
;QSVLTQPPSASGTPGQRVTISCSGGSSNIGSNPVNWFQQFPGTAPKLLIYANTQRPSGVPDRFSGSKSGTSVSLAISGLQ
SEDEGDYHCAAWDDSLKGWVFGGGTKLTVLGAPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVK
AGVETTKPSKQSNNKTAASSYLSLTPEQWKSHRSYSCQVTHEGTTVEKTVAP
;
FFF,GGG,III,KKK,MMM ? 
3 'polypeptide(L)' no no 
;EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYTMNWVRQAPGKGLQWVSSISSSSTYMYYGDSVKGRFTISRDNARNSLY
LQMNSLRVEDTAVYYCARYAHDWNVDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWN
SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPS
VFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEY
KCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV
;
;EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYTMNWVRQAPGKGLQWVSSISSSSTYMYYGDSVKGRFTISRDNARNSLY
LQMNSLRVEDTAVYYCARYAHDWNVDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWN
SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPS
VFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEY
KCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV
;
HHH,JJJ,LLL,NNN,YYY ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   GLY n 
1 6   GLY n 
1 7   VAL n 
1 8   GLU n 
1 9   VAL n 
1 10  LEU n 
1 11  GLU n 
1 12  VAL n 
1 13  LYS n 
1 14  THR n 
1 15  GLY n 
1 16  VAL n 
1 17  ASP n 
1 18  SER n 
1 19  ILE n 
1 20  THR n 
1 21  GLU n 
1 22  VAL n 
1 23  GLU n 
1 24  CYS n 
1 25  PHE n 
1 26  LEU n 
1 27  THR n 
1 28  PRO n 
1 29  GLU n 
1 30  MET n 
1 31  GLY n 
1 32  ASP n 
1 33  PRO n 
1 34  ASP n 
1 35  GLU n 
1 36  HIS n 
1 37  LEU n 
1 38  ARG n 
1 39  GLY n 
1 40  PHE n 
1 41  SER n 
1 42  LYS n 
1 43  SER n 
1 44  ILE n 
1 45  SER n 
1 46  ILE n 
1 47  SER n 
1 48  ASP n 
1 49  THR n 
1 50  PHE n 
1 51  GLU n 
1 52  SER n 
1 53  ASP n 
1 54  SER n 
1 55  PRO n 
1 56  ASN n 
1 57  ARG n 
1 58  ASP n 
1 59  MET n 
1 60  LEU n 
1 61  PRO n 
1 62  CYS n 
1 63  TYR n 
1 64  SER n 
1 65  VAL n 
1 66  ALA n 
1 67  ARG n 
1 68  ILE n 
1 69  PRO n 
1 70  LEU n 
1 71  PRO n 
1 72  ASN n 
1 73  LEU n 
1 74  ASN n 
1 75  GLU n 
1 76  ASP n 
1 77  LEU n 
1 78  THR n 
1 79  CYS n 
1 80  GLY n 
1 81  ASN n 
1 82  ILE n 
1 83  LEU n 
1 84  MET n 
1 85  TRP n 
1 86  GLU n 
1 87  ALA n 
1 88  VAL n 
1 89  THR n 
1 90  LEU n 
1 91  LYS n 
1 92  THR n 
1 93  GLU n 
1 94  VAL n 
1 95  ILE n 
1 96  GLY n 
1 97  VAL n 
1 98  THR n 
1 99  SER n 
1 100 LEU n 
1 101 MET n 
1 102 ASN n 
1 103 VAL n 
1 104 HIS n 
1 105 SER n 
1 106 ASN n 
1 107 GLY n 
1 108 GLN n 
1 109 ALA n 
1 110 THR n 
1 111 HIS n 
1 112 ASP n 
1 113 ASN n 
1 114 GLY n 
1 115 ALA n 
1 116 GLY n 
1 117 LYS n 
1 118 PRO n 
1 119 VAL n 
1 120 GLN n 
1 121 GLY n 
1 122 THR n 
1 123 SER n 
1 124 PHE n 
1 125 HIS n 
1 126 PHE n 
1 127 PHE n 
1 128 SER n 
1 129 VAL n 
1 130 GLY n 
1 131 GLY n 
1 132 GLU n 
1 133 ALA n 
1 134 LEU n 
1 135 GLU n 
1 136 LEU n 
1 137 GLN n 
1 138 GLY n 
1 139 VAL n 
1 140 LEU n 
1 141 PHE n 
1 142 ASN n 
1 143 TYR n 
1 144 ARG n 
1 145 THR n 
1 146 LYS n 
1 147 TYR n 
1 148 PRO n 
1 149 ASP n 
1 150 GLY n 
1 151 THR n 
1 152 ILE n 
1 153 PHE n 
1 154 PRO n 
1 155 LYS n 
1 156 ASN n 
1 157 ALA n 
1 158 THR n 
1 159 VAL n 
1 160 GLN n 
1 161 SER n 
1 162 GLN n 
1 163 VAL n 
1 164 MET n 
1 165 ASN n 
1 166 THR n 
1 167 GLU n 
1 168 HIS n 
1 169 LYS n 
1 170 ALA n 
1 171 TYR n 
1 172 LEU n 
1 173 ASP n 
1 174 LYS n 
1 175 ASN n 
1 176 LYS n 
1 177 ALA n 
1 178 TYR n 
1 179 PRO n 
1 180 VAL n 
1 181 GLU n 
1 182 CYS n 
1 183 TRP n 
1 184 VAL n 
1 185 PRO n 
1 186 ASP n 
1 187 PRO n 
1 188 THR n 
1 189 ARG n 
1 190 ASN n 
1 191 GLU n 
1 192 ASN n 
1 193 THR n 
1 194 ARG n 
1 195 TYR n 
1 196 PHE n 
1 197 GLY n 
1 198 THR n 
1 199 LEU n 
1 200 THR n 
1 201 GLY n 
1 202 GLY n 
1 203 GLU n 
1 204 ASN n 
1 205 VAL n 
1 206 PRO n 
1 207 PRO n 
1 208 VAL n 
1 209 LEU n 
1 210 HIS n 
1 211 ILE n 
1 212 THR n 
1 213 ASN n 
1 214 THR n 
1 215 ALA n 
1 216 THR n 
1 217 THR n 
1 218 VAL n 
1 219 LEU n 
1 220 LEU n 
1 221 ASP n 
1 222 GLU n 
1 223 PHE n 
1 224 GLY n 
1 225 VAL n 
1 226 GLY n 
1 227 PRO n 
1 228 LEU n 
1 229 CYS n 
1 230 LYS n 
1 231 GLY n 
1 232 ASP n 
1 233 ASN n 
1 234 LEU n 
1 235 TYR n 
1 236 LEU n 
1 237 SER n 
1 238 ALA n 
1 239 VAL n 
1 240 ASP n 
1 241 VAL n 
1 242 CYS n 
1 243 GLY n 
1 244 MET n 
1 245 PHE n 
1 246 THR n 
1 247 ASN n 
1 248 ARG n 
1 249 SER n 
1 250 GLY n 
1 251 SER n 
1 252 GLN n 
1 253 GLN n 
1 254 TRP n 
1 255 ARG n 
1 256 GLY n 
1 257 LEU n 
1 258 SER n 
1 259 ARG n 
1 260 TYR n 
1 261 PHE n 
1 262 LYS n 
1 263 VAL n 
1 264 GLN n 
1 265 LEU n 
1 266 ARG n 
1 267 LYS n 
1 268 ARG n 
1 269 ARG n 
1 270 VAL n 
1 271 LYS n 
1 272 ASN n 
2 1   GLN n 
2 2   SER n 
2 3   VAL n 
2 4   LEU n 
2 5   THR n 
2 6   GLN n 
2 7   PRO n 
2 8   PRO n 
2 9   SER n 
2 10  ALA n 
2 11  SER n 
2 12  GLY n 
2 13  THR n 
2 14  PRO n 
2 15  GLY n 
2 16  GLN n 
2 17  ARG n 
2 18  VAL n 
2 19  THR n 
2 20  ILE n 
2 21  SER n 
2 22  CYS n 
2 23  SER n 
2 24  GLY n 
2 25  GLY n 
2 26  SER n 
2 27  SER n 
2 28  ASN n 
2 29  ILE n 
2 30  GLY n 
2 31  SER n 
2 32  ASN n 
2 33  PRO n 
2 34  VAL n 
2 35  ASN n 
2 36  TRP n 
2 37  PHE n 
2 38  GLN n 
2 39  GLN n 
2 40  PHE n 
2 41  PRO n 
2 42  GLY n 
2 43  THR n 
2 44  ALA n 
2 45  PRO n 
2 46  LYS n 
2 47  LEU n 
2 48  LEU n 
2 49  ILE n 
2 50  TYR n 
2 51  ALA n 
2 52  ASN n 
2 53  THR n 
2 54  GLN n 
2 55  ARG n 
2 56  PRO n 
2 57  SER n 
2 58  GLY n 
2 59  VAL n 
2 60  PRO n 
2 61  ASP n 
2 62  ARG n 
2 63  PHE n 
2 64  SER n 
2 65  GLY n 
2 66  SER n 
2 67  LYS n 
2 68  SER n 
2 69  GLY n 
2 70  THR n 
2 71  SER n 
2 72  VAL n 
2 73  SER n 
2 74  LEU n 
2 75  ALA n 
2 76  ILE n 
2 77  SER n 
2 78  GLY n 
2 79  LEU n 
2 80  GLN n 
2 81  SER n 
2 82  GLU n 
2 83  ASP n 
2 84  GLU n 
2 85  GLY n 
2 86  ASP n 
2 87  TYR n 
2 88  HIS n 
2 89  CYS n 
2 90  ALA n 
2 91  ALA n 
2 92  TRP n 
2 93  ASP n 
2 94  ASP n 
2 95  SER n 
2 96  LEU n 
2 97  LYS n 
2 98  GLY n 
2 99  TRP n 
2 100 VAL n 
2 101 PHE n 
2 102 GLY n 
2 103 GLY n 
2 104 GLY n 
2 105 THR n 
2 106 LYS n 
2 107 LEU n 
2 108 THR n 
2 109 VAL n 
2 110 LEU n 
2 111 GLY n 
2 112 ALA n 
2 113 PRO n 
2 114 LYS n 
2 115 ALA n 
2 116 ASN n 
2 117 PRO n 
2 118 THR n 
2 119 VAL n 
2 120 THR n 
2 121 LEU n 
2 122 PHE n 
2 123 PRO n 
2 124 PRO n 
2 125 SER n 
2 126 SER n 
2 127 GLU n 
2 128 GLU n 
2 129 LEU n 
2 130 GLN n 
2 131 ALA n 
2 132 ASN n 
2 133 LYS n 
2 134 ALA n 
2 135 THR n 
2 136 LEU n 
2 137 VAL n 
2 138 CYS n 
2 139 LEU n 
2 140 ILE n 
2 141 SER n 
2 142 ASP n 
2 143 PHE n 
2 144 TYR n 
2 145 PRO n 
2 146 GLY n 
2 147 ALA n 
2 148 VAL n 
2 149 THR n 
2 150 VAL n 
2 151 ALA n 
2 152 TRP n 
2 153 LYS n 
2 154 ALA n 
2 155 ASP n 
2 156 GLY n 
2 157 SER n 
2 158 PRO n 
2 159 VAL n 
2 160 LYS n 
2 161 ALA n 
2 162 GLY n 
2 163 VAL n 
2 164 GLU n 
2 165 THR n 
2 166 THR n 
2 167 LYS n 
2 168 PRO n 
2 169 SER n 
2 170 LYS n 
2 171 GLN n 
2 172 SER n 
2 173 ASN n 
2 174 ASN n 
2 175 LYS n 
2 176 THR n 
2 177 ALA n 
2 178 ALA n 
2 179 SER n 
2 180 SER n 
2 181 TYR n 
2 182 LEU n 
2 183 SER n 
2 184 LEU n 
2 185 THR n 
2 186 PRO n 
2 187 GLU n 
2 188 GLN n 
2 189 TRP n 
2 190 LYS n 
2 191 SER n 
2 192 HIS n 
2 193 ARG n 
2 194 SER n 
2 195 TYR n 
2 196 SER n 
2 197 CYS n 
2 198 GLN n 
2 199 VAL n 
2 200 THR n 
2 201 HIS n 
2 202 GLU n 
2 203 GLY n 
2 204 THR n 
2 205 THR n 
2 206 VAL n 
2 207 GLU n 
2 208 LYS n 
2 209 THR n 
2 210 VAL n 
2 211 ALA n 
2 212 PRO n 
3 1   GLU n 
3 2   VAL n 
3 3   GLN n 
3 4   LEU n 
3 5   VAL n 
3 6   GLU n 
3 7   SER n 
3 8   GLY n 
3 9   GLY n 
3 10  GLY n 
3 11  LEU n 
3 12  VAL n 
3 13  LYS n 
3 14  PRO n 
3 15  GLY n 
3 16  GLY n 
3 17  SER n 
3 18  LEU n 
3 19  ARG n 
3 20  LEU n 
3 21  SER n 
3 22  CYS n 
3 23  ALA n 
3 24  ALA n 
3 25  SER n 
3 26  GLY n 
3 27  PHE n 
3 28  THR n 
3 29  PHE n 
3 30  SER n 
3 31  SER n 
3 32  TYR n 
3 33  THR n 
3 34  MET n 
3 35  ASN n 
3 36  TRP n 
3 37  VAL n 
3 38  ARG n 
3 39  GLN n 
3 40  ALA n 
3 41  PRO n 
3 42  GLY n 
3 43  LYS n 
3 44  GLY n 
3 45  LEU n 
3 46  GLN n 
3 47  TRP n 
3 48  VAL n 
3 49  SER n 
3 50  SER n 
3 51  ILE n 
3 52  SER n 
3 53  SER n 
3 54  SER n 
3 55  SER n 
3 56  THR n 
3 57  TYR n 
3 58  MET n 
3 59  TYR n 
3 60  TYR n 
3 61  GLY n 
3 62  ASP n 
3 63  SER n 
3 64  VAL n 
3 65  LYS n 
3 66  GLY n 
3 67  ARG n 
3 68  PHE n 
3 69  THR n 
3 70  ILE n 
3 71  SER n 
3 72  ARG n 
3 73  ASP n 
3 74  ASN n 
3 75  ALA n 
3 76  ARG n 
3 77  ASN n 
3 78  SER n 
3 79  LEU n 
3 80  TYR n 
3 81  LEU n 
3 82  GLN n 
3 83  MET n 
3 84  ASN n 
3 85  SER n 
3 86  LEU n 
3 87  ARG n 
3 88  VAL n 
3 89  GLU n 
3 90  ASP n 
3 91  THR n 
3 92  ALA n 
3 93  VAL n 
3 94  TYR n 
3 95  TYR n 
3 96  CYS n 
3 97  ALA n 
3 98  ARG n 
3 99  TYR n 
3 100 ALA n 
3 101 HIS n 
3 102 ASP n 
3 103 TRP n 
3 104 ASN n 
3 105 VAL n 
3 106 ASP n 
3 107 TYR n 
3 108 TRP n 
3 109 GLY n 
3 110 GLN n 
3 111 GLY n 
3 112 THR n 
3 113 LEU n 
3 114 VAL n 
3 115 THR n 
3 116 VAL n 
3 117 SER n 
3 118 SER n 
3 119 ALA n 
3 120 SER n 
3 121 THR n 
3 122 LYS n 
3 123 GLY n 
3 124 PRO n 
3 125 SER n 
3 126 VAL n 
3 127 PHE n 
3 128 PRO n 
3 129 LEU n 
3 130 ALA n 
3 131 PRO n 
3 132 SER n 
3 133 SER n 
3 134 LYS n 
3 135 SER n 
3 136 THR n 
3 137 SER n 
3 138 GLY n 
3 139 GLY n 
3 140 THR n 
3 141 ALA n 
3 142 ALA n 
3 143 LEU n 
3 144 GLY n 
3 145 CYS n 
3 146 LEU n 
3 147 VAL n 
3 148 LYS n 
3 149 ASP n 
3 150 TYR n 
3 151 PHE n 
3 152 PRO n 
3 153 GLU n 
3 154 PRO n 
3 155 VAL n 
3 156 THR n 
3 157 VAL n 
3 158 SER n 
3 159 TRP n 
3 160 ASN n 
3 161 SER n 
3 162 GLY n 
3 163 ALA n 
3 164 LEU n 
3 165 THR n 
3 166 SER n 
3 167 GLY n 
3 168 VAL n 
3 169 HIS n 
3 170 THR n 
3 171 PHE n 
3 172 PRO n 
3 173 ALA n 
3 174 VAL n 
3 175 LEU n 
3 176 GLN n 
3 177 SER n 
3 178 SER n 
3 179 GLY n 
3 180 LEU n 
3 181 TYR n 
3 182 SER n 
3 183 LEU n 
3 184 SER n 
3 185 SER n 
3 186 VAL n 
3 187 VAL n 
3 188 THR n 
3 189 VAL n 
3 190 PRO n 
3 191 SER n 
3 192 SER n 
3 193 SER n 
3 194 LEU n 
3 195 GLY n 
3 196 THR n 
3 197 GLN n 
3 198 THR n 
3 199 TYR n 
3 200 ILE n 
3 201 CYS n 
3 202 ASN n 
3 203 VAL n 
3 204 ASN n 
3 205 HIS n 
3 206 LYS n 
3 207 PRO n 
3 208 SER n 
3 209 ASN n 
3 210 THR n 
3 211 LYS n 
3 212 VAL n 
3 213 ASP n 
3 214 LYS n 
3 215 LYS n 
3 216 VAL n 
3 217 GLU n 
3 218 PRO n 
3 219 LYS n 
3 220 SER n 
3 221 CYS n 
3 222 ASP n 
3 223 LYS n 
3 224 THR n 
3 225 HIS n 
3 226 THR n 
3 227 CYS n 
3 228 PRO n 
3 229 PRO n 
3 230 CYS n 
3 231 PRO n 
3 232 ALA n 
3 233 PRO n 
3 234 GLU n 
3 235 LEU n 
3 236 LEU n 
3 237 GLY n 
3 238 GLY n 
3 239 PRO n 
3 240 SER n 
3 241 VAL n 
3 242 PHE n 
3 243 LEU n 
3 244 PHE n 
3 245 PRO n 
3 246 PRO n 
3 247 LYS n 
3 248 PRO n 
3 249 LYS n 
3 250 ASP n 
3 251 THR n 
3 252 LEU n 
3 253 MET n 
3 254 ILE n 
3 255 SER n 
3 256 ARG n 
3 257 THR n 
3 258 PRO n 
3 259 GLU n 
3 260 VAL n 
3 261 THR n 
3 262 CYS n 
3 263 VAL n 
3 264 VAL n 
3 265 VAL n 
3 266 ASP n 
3 267 VAL n 
3 268 SER n 
3 269 HIS n 
3 270 GLU n 
3 271 ASP n 
3 272 PRO n 
3 273 GLU n 
3 274 VAL n 
3 275 LYS n 
3 276 PHE n 
3 277 ASN n 
3 278 TRP n 
3 279 TYR n 
3 280 VAL n 
3 281 ASP n 
3 282 GLY n 
3 283 VAL n 
3 284 GLU n 
3 285 VAL n 
3 286 HIS n 
3 287 ASN n 
3 288 ALA n 
3 289 LYS n 
3 290 THR n 
3 291 LYS n 
3 292 PRO n 
3 293 ARG n 
3 294 GLU n 
3 295 GLU n 
3 296 GLN n 
3 297 TYR n 
3 298 ASN n 
3 299 SER n 
3 300 THR n 
3 301 TYR n 
3 302 ARG n 
3 303 VAL n 
3 304 VAL n 
3 305 SER n 
3 306 VAL n 
3 307 LEU n 
3 308 THR n 
3 309 VAL n 
3 310 LEU n 
3 311 HIS n 
3 312 GLN n 
3 313 ASP n 
3 314 TRP n 
3 315 LEU n 
3 316 ASN n 
3 317 GLY n 
3 318 LYS n 
3 319 GLU n 
3 320 TYR n 
3 321 LYS n 
3 322 CYS n 
3 323 LYS n 
3 324 VAL n 
3 325 SER n 
3 326 ASN n 
3 327 LYS n 
3 328 ALA n 
3 329 LEU n 
3 330 PRO n 
3 331 ALA n 
3 332 PRO n 
3 333 ILE n 
3 334 GLU n 
3 335 LYS n 
3 336 THR n 
3 337 ILE n 
3 338 SER n 
3 339 LYS n 
3 340 ALA n 
3 341 LYS n 
3 342 GLY n 
3 343 GLN n 
3 344 PRO n 
3 345 ARG n 
3 346 GLU n 
3 347 PRO n 
3 348 GLN n 
3 349 VAL n 
3 350 TYR n 
3 351 THR n 
3 352 LEU n 
3 353 PRO n 
3 354 PRO n 
3 355 SER n 
3 356 ARG n 
3 357 ASP n 
3 358 GLU n 
3 359 LEU n 
3 360 THR n 
3 361 LYS n 
3 362 ASN n 
3 363 GLN n 
3 364 VAL n 
3 365 SER n 
3 366 LEU n 
3 367 THR n 
3 368 CYS n 
3 369 LEU n 
3 370 VAL n 
3 371 LYS n 
3 372 GLY n 
3 373 PHE n 
3 374 TYR n 
3 375 PRO n 
3 376 SER n 
3 377 ASP n 
3 378 ILE n 
3 379 ALA n 
3 380 VAL n 
3 381 GLU n 
3 382 TRP n 
3 383 GLU n 
3 384 SER n 
3 385 ASN n 
3 386 GLY n 
3 387 GLN n 
3 388 PRO n 
3 389 GLU n 
3 390 ASN n 
3 391 ASN n 
3 392 TYR n 
3 393 LYS n 
3 394 THR n 
3 395 THR n 
3 396 PRO n 
3 397 PRO n 
3 398 VAL n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 272 JCPyV ? ? ? ? ? ? ? ? 'JC polyomavirus' 10632 ? ? ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 212 ?     ? ? ? ? ? ? ? ? 'Homo sapiens'    9606  ? ? ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 398 ?     ? ? ? ? ? ? ? ? 'Homo sapiens'    9606  ? ? ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP VP1_POVJC P03089 ? 1 
;GGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNRDMLPCYSVARIPLPNLNEDLTCGNILM
WEAVTLKTEVIGVTSLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVLFNYRTKYPDGTIFPKNATVQSQVM
NTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVDVCGM
FTNRSGSQQWRGLSRYFKVQLRKRRVKN
;
23 
2 PDB 7PA8      7PA8   ? 2 ? 1  
3 PDB 7PA8      7PA8   ? 3 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 7PA8 AAA 5 ? 272 ? P03089 23 ? 290 ? 22 289 
2  1 7PA8 BBB 5 ? 272 ? P03089 23 ? 290 ? 22 289 
3  1 7PA8 CCC 5 ? 272 ? P03089 23 ? 290 ? 22 289 
4  1 7PA8 DDD 5 ? 272 ? P03089 23 ? 290 ? 22 289 
5  1 7PA8 EEE 5 ? 272 ? P03089 23 ? 290 ? 22 289 
6  2 7PA8 FFF 1 ? 212 ? 7PA8   1  ? 212 ? 1  212 
7  2 7PA8 GGG 1 ? 212 ? 7PA8   1  ? 212 ? 1  212 
8  3 7PA8 HHH 1 ? 398 ? 7PA8   1  ? 403 ? 1  403 
9  2 7PA8 III 1 ? 212 ? 7PA8   1  ? 212 ? 1  212 
10 3 7PA8 JJJ 1 ? 398 ? 7PA8   1  ? 403 ? 1  403 
11 2 7PA8 KKK 1 ? 212 ? 7PA8   1  ? 212 ? 1  212 
12 3 7PA8 LLL 1 ? 398 ? 7PA8   1  ? 403 ? 1  403 
13 2 7PA8 MMM 1 ? 212 ? 7PA8   1  ? 212 ? 1  212 
14 3 7PA8 NNN 1 ? 398 ? 7PA8   1  ? 398 ? 1  398 
15 3 7PA8 YYY 1 ? 398 ? 7PA8   1  ? 403 ? 1  403 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7PA8 GLY AAA 1 ? UNP P03089 ? ? 'expression tag' 18 1  
1 7PA8 SER AAA 2 ? UNP P03089 ? ? 'expression tag' 19 2  
1 7PA8 HIS AAA 3 ? UNP P03089 ? ? 'expression tag' 20 3  
1 7PA8 MET AAA 4 ? UNP P03089 ? ? 'expression tag' 21 4  
2 7PA8 GLY BBB 1 ? UNP P03089 ? ? 'expression tag' 18 5  
2 7PA8 SER BBB 2 ? UNP P03089 ? ? 'expression tag' 19 6  
2 7PA8 HIS BBB 3 ? UNP P03089 ? ? 'expression tag' 20 7  
2 7PA8 MET BBB 4 ? UNP P03089 ? ? 'expression tag' 21 8  
3 7PA8 GLY CCC 1 ? UNP P03089 ? ? 'expression tag' 18 9  
3 7PA8 SER CCC 2 ? UNP P03089 ? ? 'expression tag' 19 10 
3 7PA8 HIS CCC 3 ? UNP P03089 ? ? 'expression tag' 20 11 
3 7PA8 MET CCC 4 ? UNP P03089 ? ? 'expression tag' 21 12 
4 7PA8 GLY DDD 1 ? UNP P03089 ? ? 'expression tag' 18 13 
4 7PA8 SER DDD 2 ? UNP P03089 ? ? 'expression tag' 19 14 
4 7PA8 HIS DDD 3 ? UNP P03089 ? ? 'expression tag' 20 15 
4 7PA8 MET DDD 4 ? UNP P03089 ? ? 'expression tag' 21 16 
5 7PA8 GLY EEE 1 ? UNP P03089 ? ? 'expression tag' 18 17 
5 7PA8 SER EEE 2 ? UNP P03089 ? ? 'expression tag' 19 18 
5 7PA8 HIS EEE 3 ? UNP P03089 ? ? 'expression tag' 20 19 
5 7PA8 MET EEE 4 ? UNP P03089 ? ? 'expression tag' 21 20 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7PA8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.38 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         63.64 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            277.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Ammonium citrate tribasic pH 7.0, 12% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-02-14 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7PA8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.15 
_reflns.d_resolution_low                               49.007 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     81593 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.03 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.49 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.32 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.98 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.15 
_reflns_shell.d_res_low                                     3.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12843 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.05 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.53 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            6.326 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            0.325 
_refine.aniso_B[2][2]                            -2.023 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -4.313 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.462 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.903 
_refine.correlation_coeff_Fo_to_Fc_free          0.872 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7PA8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.150 
_refine.ls_d_res_low                             49.007 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     81570 
_refine.ls_number_reflns_R_free                  4079 
_refine.ls_number_reflns_R_work                  77491 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.682 
_refine.ls_percent_reflns_R_free                 5.001 
_refine.ls_R_factor_all                          0.213 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2407 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2120 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      0.217 
_refine.ls_wR_factor_R_work                      0.193 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      '3NXG, 5BVJ' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.405 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    0.9052 
_refine.pdbx_average_fsc_free                    0.8945 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.150 
_refine_hist.d_res_low                        49.007 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               21270 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        21270 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.013  21774 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.037  0.017  19268 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.604  1.642  29671 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 2.444  1.569  44756 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.859  5.000  2803  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 33.411 22.653 965   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.348 15.000 3202  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 17.891 15.000 104   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.069  0.200  2872  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  24617 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4507  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.207  0.200  3734  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.224  0.200  17795 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  10335 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200  9343  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.154  0.200  401   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.050  0.200  18    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.273  0.200  13    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.293  0.200  30    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.204  0.200  5     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 4.689  5.036  11341 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.689  5.036  11340 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 7.403  7.525  14101 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 7.403  7.525  14102 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 4.628  4.923  10433 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.628  4.924  10434 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 7.285  7.379  15570 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 7.285  7.379  15571 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 11.549 90.886 84636 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 11.549 90.886 84637 ? r_lrange_other                 ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 3.150  3.232  5984 . 288 5475 96.3068  . 0.331 . 0.350 . 0.330 . . . . . 0.312 . 20 . 0.762 0.746 
'X-RAY DIFFRACTION' 3.232  3.320  5869 . 293 5572 99.9318  . 0.280 . 0.327 . 0.278 . . . . . 0.262 . 20 . 0.825 0.798 
'X-RAY DIFFRACTION' 3.320  3.415  5638 . 282 5356 100.0000 . 0.263 . 0.301 . 0.261 . . . . . 0.241 . 20 . 0.851 0.841 
'X-RAY DIFFRACTION' 3.415  3.520  5579 . 279 5300 100.0000 . 0.244 . 0.265 . 0.243 . . . . . 0.223 . 20 . 0.882 0.873 
'X-RAY DIFFRACTION' 3.520  3.635  5335 . 267 5067 99.9813  . 0.217 . 0.236 . 0.216 . . . . . 0.194 . 20 . 0.916 0.914 
'X-RAY DIFFRACTION' 3.635  3.762  5172 . 259 4913 100.0000 . 0.216 . 0.254 . 0.214 . . . . . 0.192 . 20 . 0.913 0.901 
'X-RAY DIFFRACTION' 3.762  3.903  5013 . 250 4763 100.0000 . 0.197 . 0.234 . 0.195 . . . . . 0.174 . 20 . 0.935 0.916 
'X-RAY DIFFRACTION' 3.903  4.061  4833 . 242 4591 100.0000 . 0.191 . 0.226 . 0.189 . . . . . 0.167 . 20 . 0.935 0.923 
'X-RAY DIFFRACTION' 4.061  4.240  4613 . 230 4382 99.9783  . 0.171 . 0.198 . 0.169 . . . . . 0.150 . 20 . 0.951 0.945 
'X-RAY DIFFRACTION' 4.240  4.446  4427 . 222 4205 100.0000 . 0.161 . 0.178 . 0.160 . . . . . 0.141 . 20 . 0.958 0.957 
'X-RAY DIFFRACTION' 4.446  4.684  4217 . 211 4006 100.0000 . 0.156 . 0.187 . 0.155 . . . . . 0.137 . 20 . 0.963 0.955 
'X-RAY DIFFRACTION' 4.684  4.965  3995 . 199 3796 100.0000 . 0.159 . 0.183 . 0.158 . . . . . 0.139 . 20 . 0.958 0.952 
'X-RAY DIFFRACTION' 4.965  5.304  3769 . 189 3580 100.0000 . 0.173 . 0.201 . 0.171 . . . . . 0.151 . 20 . 0.954 0.940 
'X-RAY DIFFRACTION' 5.304  5.724  3504 . 175 3329 100.0000 . 0.208 . 0.278 . 0.204 . . . . . 0.180 . 20 . 0.924 0.895 
'X-RAY DIFFRACTION' 5.724  6.261  3249 . 162 3085 99.9384  . 0.228 . 0.248 . 0.227 . . . . . 0.200 . 20 . 0.917 0.921 
'X-RAY DIFFRACTION' 6.261  6.986  2945 . 148 2797 100.0000 . 0.225 . 0.281 . 0.222 . . . . . 0.198 . 20 . 0.923 0.903 
'X-RAY DIFFRACTION' 6.986  8.040  2608 . 130 2478 100.0000 . 0.221 . 0.229 . 0.221 . . . . . 0.199 . 20 . 0.929 0.925 
'X-RAY DIFFRACTION' 8.040  9.781  2231 . 112 2119 100.0000 . 0.229 . 0.231 . 0.229 . . . . . 0.215 . 20 . 0.933 0.930 
'X-RAY DIFFRACTION' 9.781  13.565 1761 . 88  1672 99.9432  . 0.246 . 0.242 . 0.246 . . . . . 0.239 . 20 . 0.927 0.937 
'X-RAY DIFFRACTION' 13.565 49.007 1062 . 53  1006 99.7175  . 0.362 . 0.337 . 0.363 . . . . . 0.361 . 20 . 0.860 0.850 
# 
_struct.entry_id                     7PA8 
_struct.title                        'JC polyomavirus VP1 in complex with Fab 27C2' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7PA8 
_struct_keywords.text            'antibody, polyomavirus, VP1, neutralization, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 1 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 2 ? 
N N N 3 ? 
O N N 3 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 56  ? LEU A 60  ? ASN AAA 73  LEU AAA 77  5 ? 5 
HELX_P HELX_P2  AA2 GLY A 96  ? ASN A 102 ? GLY AAA 113 ASN AAA 119 5 ? 7 
HELX_P HELX_P3  AA3 THR A 158 ? VAL A 163 ? THR AAA 175 VAL AAA 180 5 ? 6 
HELX_P HELX_P4  AA4 PRO A 179 ? GLU A 181 ? PRO AAA 196 GLU AAA 198 5 ? 3 
HELX_P HELX_P5  AA5 CYS A 229 ? GLY A 231 ? CYS AAA 246 GLY AAA 248 5 ? 3 
HELX_P HELX_P6  AA6 THR B 49  ? ASP B 53  ? THR BBB 66  ASP BBB 70  5 ? 5 
HELX_P HELX_P7  AA7 ASN B 56  ? LEU B 60  ? ASN BBB 73  LEU BBB 77  5 ? 5 
HELX_P HELX_P8  AA8 GLY B 96  ? ASN B 102 ? GLY BBB 113 ASN BBB 119 5 ? 7 
HELX_P HELX_P9  AA9 THR B 158 ? VAL B 163 ? THR BBB 175 VAL BBB 180 5 ? 6 
HELX_P HELX_P10 AB1 PRO B 179 ? GLU B 181 ? PRO BBB 196 GLU BBB 198 5 ? 3 
HELX_P HELX_P11 AB2 CYS B 229 ? GLY B 231 ? CYS BBB 246 GLY BBB 248 5 ? 3 
HELX_P HELX_P12 AB3 THR C 49  ? ASP C 53  ? THR CCC 66  ASP CCC 70  5 ? 5 
HELX_P HELX_P13 AB4 ASN C 56  ? LEU C 60  ? ASN CCC 73  LEU CCC 77  5 ? 5 
HELX_P HELX_P14 AB5 GLY C 96  ? ASN C 102 ? GLY CCC 113 ASN CCC 119 5 ? 7 
HELX_P HELX_P15 AB6 THR C 158 ? VAL C 163 ? THR CCC 175 VAL CCC 180 5 ? 6 
HELX_P HELX_P16 AB7 PRO C 179 ? GLU C 181 ? PRO CCC 196 GLU CCC 198 5 ? 3 
HELX_P HELX_P17 AB8 CYS C 229 ? GLY C 231 ? CYS CCC 246 GLY CCC 248 5 ? 3 
HELX_P HELX_P18 AB9 THR D 49  ? ASP D 53  ? THR DDD 66  ASP DDD 70  5 ? 5 
HELX_P HELX_P19 AC1 ASN D 56  ? LEU D 60  ? ASN DDD 73  LEU DDD 77  5 ? 5 
HELX_P HELX_P20 AC2 GLY D 96  ? ASN D 102 ? GLY DDD 113 ASN DDD 119 5 ? 7 
HELX_P HELX_P21 AC3 THR D 158 ? VAL D 163 ? THR DDD 175 VAL DDD 180 5 ? 6 
HELX_P HELX_P22 AC4 PRO D 179 ? GLU D 181 ? PRO DDD 196 GLU DDD 198 5 ? 3 
HELX_P HELX_P23 AC5 CYS D 229 ? GLY D 231 ? CYS DDD 246 GLY DDD 248 5 ? 3 
HELX_P HELX_P24 AC6 THR E 49  ? ASP E 53  ? THR EEE 66  ASP EEE 70  5 ? 5 
HELX_P HELX_P25 AC7 ASN E 56  ? LEU E 60  ? ASN EEE 73  LEU EEE 77  5 ? 5 
HELX_P HELX_P26 AC8 GLY E 96  ? ASN E 102 ? GLY EEE 113 ASN EEE 119 5 ? 7 
HELX_P HELX_P27 AC9 THR E 158 ? VAL E 163 ? THR EEE 175 VAL EEE 180 5 ? 6 
HELX_P HELX_P28 AD1 PRO E 179 ? GLU E 181 ? PRO EEE 196 GLU EEE 198 5 ? 3 
HELX_P HELX_P29 AD2 CYS E 229 ? GLY E 231 ? CYS EEE 246 GLY EEE 248 5 ? 3 
HELX_P HELX_P30 AD3 GLN F 80  ? GLU F 84  ? GLN FFF 80  GLU FFF 84  5 ? 5 
HELX_P HELX_P31 AD4 GLN G 80  ? GLU G 84  ? GLN GGG 80  GLU GGG 84  5 ? 5 
HELX_P HELX_P32 AD5 THR H 28  ? TYR H 32  ? THR HHH 28  TYR HHH 32  5 ? 5 
HELX_P HELX_P33 AD6 GLN I 80  ? GLU I 84  ? GLN III 80  GLU III 84  5 ? 5 
HELX_P HELX_P34 AD7 THR J 28  ? TYR J 32  ? THR JJJ 28  TYR JJJ 32  5 ? 5 
HELX_P HELX_P35 AD8 ASP J 62  ? LYS J 65  ? ASP JJJ 62  LYS JJJ 65  5 ? 4 
HELX_P HELX_P36 AD9 HIS J 205 ? ASN J 209 ? HIS JJJ 210 ASN JJJ 214 5 ? 5 
HELX_P HELX_P37 AE1 GLN K 80  ? GLU K 84  ? GLN KKK 80  GLU KKK 84  5 ? 5 
HELX_P HELX_P38 AE2 THR L 28  ? TYR L 32  ? THR LLL 28  TYR LLL 32  5 ? 5 
HELX_P HELX_P39 AE3 ASP L 62  ? LYS L 65  ? ASP LLL 62  LYS LLL 65  5 ? 4 
HELX_P HELX_P40 AE4 ARG L 87  ? THR L 91  ? ARG LLL 87  THR LLL 91  5 ? 5 
HELX_P HELX_P41 AE5 HIS L 205 ? ASN L 209 ? HIS LLL 210 ASN LLL 214 5 ? 5 
HELX_P HELX_P42 AE6 GLN M 80  ? GLU M 84  ? GLN MMM 80  GLU MMM 84  5 ? 5 
HELX_P HELX_P43 AE7 THR N 28  ? TYR N 32  ? THR NNN 28  TYR NNN 32  5 ? 5 
HELX_P HELX_P44 AE8 ASP N 62  ? LYS N 65  ? ASP NNN 62  LYS NNN 65  5 ? 4 
HELX_P HELX_P45 AE9 ARG N 87  ? THR N 91  ? ARG NNN 87  THR NNN 91  5 ? 5 
HELX_P HELX_P46 AF1 THR O 28  ? TYR O 32  ? THR YYY 28  TYR YYY 32  5 ? 5 
HELX_P HELX_P47 AF2 ASP O 62  ? LYS O 65  ? ASP YYY 62  LYS YYY 65  5 ? 4 
HELX_P HELX_P48 AF3 ARG O 87  ? THR O 91  ? ARG YYY 87  THR YYY 91  5 ? 5 
HELX_P HELX_P49 AF4 HIS O 205 ? ASN O 209 ? HIS YYY 210 ASN YYY 214 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? F CYS 22  SG ? ? ? 1_555 F CYS 89  SG ? ? FFF CYS 22  FFF CYS 89  1_555 ? ? ? ? ? ? ? 2.114 ? ? 
disulf2  disulf ? ? F CYS 138 SG ? ? ? 1_555 F CYS 197 SG ? ? FFF CYS 138 FFF CYS 197 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf3  disulf ? ? G CYS 22  SG ? ? ? 1_555 G CYS 89  SG ? ? GGG CYS 22  GGG CYS 89  1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf4  disulf ? ? G CYS 138 SG ? ? ? 1_555 G CYS 197 SG ? ? GGG CYS 138 GGG CYS 197 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf5  disulf ? ? H CYS 22  SG ? ? ? 1_555 H CYS 96  SG ? ? HHH CYS 22  HHH CYS 96  1_555 ? ? ? ? ? ? ? 2.260 ? ? 
disulf6  disulf ? ? I CYS 22  SG ? ? ? 1_555 I CYS 89  SG ? ? III CYS 22  III CYS 89  1_555 ? ? ? ? ? ? ? 2.214 ? ? 
disulf7  disulf ? ? J CYS 22  SG ? ? ? 1_555 J CYS 96  SG ? ? JJJ CYS 22  JJJ CYS 96  1_555 ? ? ? ? ? ? ? 2.250 ? ? 
disulf8  disulf ? ? J CYS 145 SG ? ? ? 1_555 J CYS 201 SG ? ? JJJ CYS 150 JJJ CYS 206 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf9  disulf ? ? K CYS 22  SG ? ? ? 1_555 K CYS 89  SG ? ? KKK CYS 22  KKK CYS 89  1_555 ? ? ? ? ? ? ? 2.101 ? ? 
disulf10 disulf ? ? L CYS 22  SG ? ? ? 1_555 L CYS 96  SG ? ? LLL CYS 22  LLL CYS 96  1_555 ? ? ? ? ? ? ? 2.252 ? ? 
disulf11 disulf ? ? M CYS 22  SG ? ? ? 1_555 M CYS 89  SG ? ? MMM CYS 22  MMM CYS 89  1_555 ? ? ? ? ? ? ? 2.131 ? ? 
disulf12 disulf ? ? N CYS 22  SG ? ? ? 1_555 N CYS 96  SG ? ? NNN CYS 22  NNN CYS 96  1_555 ? ? ? ? ? ? ? 2.145 ? ? 
disulf13 disulf ? ? O CYS 22  SG ? ? ? 1_555 O CYS 96  SG ? ? YYY CYS 22  YYY CYS 96  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf14 disulf ? ? O CYS 145 SG ? ? ? 1_555 O CYS 201 SG ? ? YYY CYS 150 YYY CYS 206 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 151 J . ? PHE 156 JJJ PRO 152 J ? PRO 157 JJJ 1 -9.89  
2 PHE 151 L . ? PHE 156 LLL PRO 152 L ? PRO 157 LLL 1 -10.44 
3 PHE 151 O . ? PHE 156 YYY PRO 152 O ? PRO 157 YYY 1 -9.28  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 5 ? 
AA8 ? 3 ? 
AA9 ? 4 ? 
AB1 ? 3 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
AB4 ? 3 ? 
AB5 ? 4 ? 
AB6 ? 3 ? 
AB7 ? 5 ? 
AB8 ? 5 ? 
AB9 ? 3 ? 
AC1 ? 4 ? 
AC2 ? 3 ? 
AC3 ? 5 ? 
AC4 ? 5 ? 
AC5 ? 3 ? 
AC6 ? 4 ? 
AC7 ? 3 ? 
AC8 ? 5 ? 
AC9 ? 4 ? 
AD1 ? 3 ? 
AD2 ? 4 ? 
AD3 ? 4 ? 
AD4 ? 2 ? 
AD5 ? 5 ? 
AD6 ? 4 ? 
AD7 ? 3 ? 
AD8 ? 4 ? 
AD9 ? 4 ? 
AE1 ? 2 ? 
AE2 ? 4 ? 
AE3 ? 6 ? 
AE4 ? 4 ? 
AE5 ? 2 ? 
AE6 ? 5 ? 
AE7 ? 4 ? 
AE8 ? 3 ? 
AE9 ? 2 ? 
AF1 ? 4 ? 
AF2 ? 6 ? 
AF3 ? 4 ? 
AF4 ? 4 ? 
AF5 ? 2 ? 
AF6 ? 5 ? 
AF7 ? 4 ? 
AF8 ? 3 ? 
AF9 ? 4 ? 
AG1 ? 6 ? 
AG2 ? 4 ? 
AG3 ? 3 ? 
AG4 ? 5 ? 
AG5 ? 4 ? 
AG6 ? 3 ? 
AG7 ? 4 ? 
AG8 ? 6 ? 
AG9 ? 4 ? 
AH1 ? 4 ? 
AH2 ? 6 ? 
AH3 ? 4 ? 
AH4 ? 4 ? 
AH5 ? 4 ? 
AH6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC3 4 5 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC4 4 5 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC8 1 2 ? parallel      
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD5 1 2 ? parallel      
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD5 4 5 ? anti-parallel 
AD6 1 2 ? parallel      
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE3 1 2 ? parallel      
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE3 4 5 ? anti-parallel 
AE3 5 6 ? anti-parallel 
AE4 1 2 ? parallel      
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE6 1 2 ? parallel      
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE6 4 5 ? anti-parallel 
AE7 1 2 ? parallel      
AE7 2 3 ? anti-parallel 
AE7 3 4 ? anti-parallel 
AE8 1 2 ? anti-parallel 
AE8 2 3 ? anti-parallel 
AE9 1 2 ? anti-parallel 
AF1 1 2 ? anti-parallel 
AF1 2 3 ? anti-parallel 
AF1 3 4 ? anti-parallel 
AF2 1 2 ? parallel      
AF2 2 3 ? anti-parallel 
AF2 3 4 ? anti-parallel 
AF2 4 5 ? anti-parallel 
AF2 5 6 ? anti-parallel 
AF3 1 2 ? parallel      
AF3 2 3 ? anti-parallel 
AF3 3 4 ? anti-parallel 
AF4 1 2 ? anti-parallel 
AF4 2 3 ? anti-parallel 
AF4 3 4 ? anti-parallel 
AF5 1 2 ? anti-parallel 
AF6 1 2 ? parallel      
AF6 2 3 ? anti-parallel 
AF6 3 4 ? anti-parallel 
AF6 4 5 ? anti-parallel 
AF7 1 2 ? parallel      
AF7 2 3 ? anti-parallel 
AF7 3 4 ? anti-parallel 
AF8 1 2 ? anti-parallel 
AF8 2 3 ? anti-parallel 
AF9 1 2 ? anti-parallel 
AF9 2 3 ? anti-parallel 
AF9 3 4 ? anti-parallel 
AG1 1 2 ? parallel      
AG1 2 3 ? anti-parallel 
AG1 3 4 ? anti-parallel 
AG1 4 5 ? anti-parallel 
AG1 5 6 ? anti-parallel 
AG2 1 2 ? parallel      
AG2 2 3 ? anti-parallel 
AG2 3 4 ? anti-parallel 
AG3 1 2 ? anti-parallel 
AG3 2 3 ? anti-parallel 
AG4 1 2 ? parallel      
AG4 2 3 ? anti-parallel 
AG4 3 4 ? anti-parallel 
AG4 4 5 ? anti-parallel 
AG5 1 2 ? parallel      
AG5 2 3 ? anti-parallel 
AG5 3 4 ? anti-parallel 
AG6 1 2 ? anti-parallel 
AG6 2 3 ? anti-parallel 
AG7 1 2 ? anti-parallel 
AG7 2 3 ? anti-parallel 
AG7 3 4 ? anti-parallel 
AG8 1 2 ? parallel      
AG8 2 3 ? anti-parallel 
AG8 3 4 ? anti-parallel 
AG8 4 5 ? anti-parallel 
AG8 5 6 ? anti-parallel 
AG9 1 2 ? parallel      
AG9 2 3 ? anti-parallel 
AG9 3 4 ? anti-parallel 
AH1 1 2 ? anti-parallel 
AH1 2 3 ? anti-parallel 
AH1 3 4 ? anti-parallel 
AH2 1 2 ? parallel      
AH2 2 3 ? anti-parallel 
AH2 3 4 ? anti-parallel 
AH2 4 5 ? anti-parallel 
AH2 5 6 ? anti-parallel 
AH3 1 2 ? parallel      
AH3 2 3 ? anti-parallel 
AH3 3 4 ? anti-parallel 
AH4 1 2 ? anti-parallel 
AH4 2 3 ? anti-parallel 
AH4 3 4 ? anti-parallel 
AH5 1 2 ? anti-parallel 
AH5 2 3 ? anti-parallel 
AH5 3 4 ? anti-parallel 
AH6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 8   ? LYS A 13  ? GLU AAA 25  LYS AAA 30  
AA1 2 SER A 258 ? LYS A 271 ? SER AAA 275 LYS AAA 288 
AA1 3 ILE A 19  ? LEU A 26  ? ILE AAA 36  LEU AAA 43  
AA2 1 GLU A 8   ? LYS A 13  ? GLU AAA 25  LYS AAA 30  
AA2 2 SER A 258 ? LYS A 271 ? SER AAA 275 LYS AAA 288 
AA2 3 ILE A 82  ? ILE A 95  ? ILE AAA 99  ILE AAA 112 
AA2 4 THR A 217 ? VAL A 218 ? THR AAA 234 VAL AAA 235 
AA3 1 SER A 64  ? PRO A 69  ? SER AAA 81  PRO AAA 86  
AA3 2 ASN A 233 ? THR A 246 ? ASN AAA 250 THR AAA 263 
AA3 3 GLN A 252 ? GLY A 256 ? GLN AAA 269 GLY AAA 273 
AA4 1 SER A 64  ? PRO A 69  ? SER AAA 81  PRO AAA 86  
AA4 2 ASN A 233 ? THR A 246 ? ASN AAA 250 THR AAA 263 
AA4 3 SER A 123 ? GLY A 130 ? SER AAA 140 GLY AAA 147 
AA4 4 THR A 193 ? THR A 200 ? THR AAA 210 THR AAA 217 
AA4 5 VAL E 208 ? THR E 212 ? VAL EEE 225 THR EEE 229 
AA5 1 LYS A 169 ? LEU A 172 ? LYS AAA 186 LEU AAA 189 
AA5 2 LEU A 134 ? GLY A 138 ? LEU AAA 151 GLY AAA 155 
AA5 3 TRP A 183 ? PRO A 185 ? TRP AAA 200 PRO AAA 202 
AA6 1 VAL A 208 ? THR A 212 ? VAL AAA 225 THR AAA 229 
AA6 2 THR B 193 ? THR B 200 ? THR BBB 210 THR BBB 217 
AA6 3 SER B 123 ? GLY B 130 ? SER BBB 140 GLY BBB 147 
AA6 4 ASN B 233 ? THR B 246 ? ASN BBB 250 THR BBB 263 
AA6 5 SER B 64  ? PRO B 69  ? SER BBB 81  PRO BBB 86  
AA7 1 VAL A 208 ? THR A 212 ? VAL AAA 225 THR AAA 229 
AA7 2 THR B 193 ? THR B 200 ? THR BBB 210 THR BBB 217 
AA7 3 SER B 123 ? GLY B 130 ? SER BBB 140 GLY BBB 147 
AA7 4 ASN B 233 ? THR B 246 ? ASN BBB 250 THR BBB 263 
AA7 5 GLN B 252 ? GLY B 256 ? GLN BBB 269 GLY BBB 273 
AA8 1 VAL B 9   ? LYS B 13  ? VAL BBB 26  LYS BBB 30  
AA8 2 SER B 258 ? VAL B 270 ? SER BBB 275 VAL BBB 287 
AA8 3 ILE B 19  ? LEU B 26  ? ILE BBB 36  LEU BBB 43  
AA9 1 VAL B 9   ? LYS B 13  ? VAL BBB 26  LYS BBB 30  
AA9 2 SER B 258 ? VAL B 270 ? SER BBB 275 VAL BBB 287 
AA9 3 LEU B 83  ? ILE B 95  ? LEU BBB 100 ILE BBB 112 
AA9 4 THR B 217 ? VAL B 218 ? THR BBB 234 VAL BBB 235 
AB1 1 LYS B 169 ? LEU B 172 ? LYS BBB 186 LEU BBB 189 
AB1 2 LEU B 134 ? GLY B 138 ? LEU BBB 151 GLY BBB 155 
AB1 3 TRP B 183 ? PRO B 185 ? TRP BBB 200 PRO BBB 202 
AB2 1 VAL B 208 ? THR B 212 ? VAL BBB 225 THR BBB 229 
AB2 2 THR C 193 ? THR C 200 ? THR CCC 210 THR CCC 217 
AB2 3 SER C 123 ? GLY C 130 ? SER CCC 140 GLY CCC 147 
AB2 4 ASN C 233 ? THR C 246 ? ASN CCC 250 THR CCC 263 
AB2 5 SER C 64  ? PRO C 69  ? SER CCC 81  PRO CCC 86  
AB3 1 VAL B 208 ? THR B 212 ? VAL BBB 225 THR BBB 229 
AB3 2 THR C 193 ? THR C 200 ? THR CCC 210 THR CCC 217 
AB3 3 SER C 123 ? GLY C 130 ? SER CCC 140 GLY CCC 147 
AB3 4 ASN C 233 ? THR C 246 ? ASN CCC 250 THR CCC 263 
AB3 5 GLN C 252 ? GLY C 256 ? GLN CCC 269 GLY CCC 273 
AB4 1 VAL C 9   ? LYS C 13  ? VAL CCC 26  LYS CCC 30  
AB4 2 SER C 258 ? VAL C 270 ? SER CCC 275 VAL CCC 287 
AB4 3 ILE C 19  ? LEU C 26  ? ILE CCC 36  LEU CCC 43  
AB5 1 VAL C 9   ? LYS C 13  ? VAL CCC 26  LYS CCC 30  
AB5 2 SER C 258 ? VAL C 270 ? SER CCC 275 VAL CCC 287 
AB5 3 LEU C 83  ? ILE C 95  ? LEU CCC 100 ILE CCC 112 
AB5 4 THR C 217 ? VAL C 218 ? THR CCC 234 VAL CCC 235 
AB6 1 LYS C 169 ? TYR C 171 ? LYS CCC 186 TYR CCC 188 
AB6 2 GLU C 135 ? GLY C 138 ? GLU CCC 152 GLY CCC 155 
AB6 3 TRP C 183 ? PRO C 185 ? TRP CCC 200 PRO CCC 202 
AB7 1 VAL C 208 ? THR C 212 ? VAL CCC 225 THR CCC 229 
AB7 2 THR D 193 ? THR D 200 ? THR DDD 210 THR DDD 217 
AB7 3 SER D 123 ? GLY D 130 ? SER DDD 140 GLY DDD 147 
AB7 4 ASN D 233 ? THR D 246 ? ASN DDD 250 THR DDD 263 
AB7 5 SER D 64  ? PRO D 69  ? SER DDD 81  PRO DDD 86  
AB8 1 VAL C 208 ? THR C 212 ? VAL CCC 225 THR CCC 229 
AB8 2 THR D 193 ? THR D 200 ? THR DDD 210 THR DDD 217 
AB8 3 SER D 123 ? GLY D 130 ? SER DDD 140 GLY DDD 147 
AB8 4 ASN D 233 ? THR D 246 ? ASN DDD 250 THR DDD 263 
AB8 5 GLN D 252 ? GLY D 256 ? GLN DDD 269 GLY DDD 273 
AB9 1 GLU D 8   ? LYS D 13  ? GLU DDD 25  LYS DDD 30  
AB9 2 SER D 258 ? LYS D 271 ? SER DDD 275 LYS DDD 288 
AB9 3 ILE D 19  ? LEU D 26  ? ILE DDD 36  LEU DDD 43  
AC1 1 GLU D 8   ? LYS D 13  ? GLU DDD 25  LYS DDD 30  
AC1 2 SER D 258 ? LYS D 271 ? SER DDD 275 LYS DDD 288 
AC1 3 ASN D 81  ? ILE D 95  ? ASN DDD 98  ILE DDD 112 
AC1 4 THR D 217 ? VAL D 218 ? THR DDD 234 VAL DDD 235 
AC2 1 LYS D 169 ? LEU D 172 ? LYS DDD 186 LEU DDD 189 
AC2 2 LEU D 134 ? GLY D 138 ? LEU DDD 151 GLY DDD 155 
AC2 3 TRP D 183 ? PRO D 185 ? TRP DDD 200 PRO DDD 202 
AC3 1 VAL D 208 ? THR D 212 ? VAL DDD 225 THR DDD 229 
AC3 2 THR E 193 ? THR E 200 ? THR EEE 210 THR EEE 217 
AC3 3 SER E 123 ? GLY E 130 ? SER EEE 140 GLY EEE 147 
AC3 4 ASN E 233 ? THR E 246 ? ASN EEE 250 THR EEE 263 
AC3 5 SER E 64  ? PRO E 69  ? SER EEE 81  PRO EEE 86  
AC4 1 VAL D 208 ? THR D 212 ? VAL DDD 225 THR DDD 229 
AC4 2 THR E 193 ? THR E 200 ? THR EEE 210 THR EEE 217 
AC4 3 SER E 123 ? GLY E 130 ? SER EEE 140 GLY EEE 147 
AC4 4 ASN E 233 ? THR E 246 ? ASN EEE 250 THR EEE 263 
AC4 5 GLN E 252 ? GLY E 256 ? GLN EEE 269 GLY EEE 273 
AC5 1 GLU E 8   ? LYS E 13  ? GLU EEE 25  LYS EEE 30  
AC5 2 SER E 258 ? LYS E 271 ? SER EEE 275 LYS EEE 288 
AC5 3 ILE E 19  ? LEU E 26  ? ILE EEE 36  LEU EEE 43  
AC6 1 GLU E 8   ? LYS E 13  ? GLU EEE 25  LYS EEE 30  
AC6 2 SER E 258 ? LYS E 271 ? SER EEE 275 LYS EEE 288 
AC6 3 LEU E 83  ? ILE E 95  ? LEU EEE 100 ILE EEE 112 
AC6 4 THR E 217 ? VAL E 218 ? THR EEE 234 VAL EEE 235 
AC7 1 LYS E 169 ? LEU E 172 ? LYS EEE 186 LEU EEE 189 
AC7 2 LEU E 134 ? GLY E 138 ? LEU EEE 151 GLY EEE 155 
AC7 3 TRP E 183 ? PRO E 185 ? TRP EEE 200 PRO EEE 202 
AC8 1 SER F 9   ? GLY F 12  ? SER FFF 9   GLY FFF 12  
AC8 2 THR F 105 ? VAL F 109 ? THR FFF 105 VAL FFF 109 
AC8 3 GLY F 85  ? ASP F 93  ? GLY FFF 85  ASP FFF 93  
AC8 4 VAL F 34  ? GLN F 39  ? VAL FFF 34  GLN FFF 39  
AC8 5 LYS F 46  ? ILE F 49  ? LYS FFF 46  ILE FFF 49  
AC9 1 SER F 9   ? GLY F 12  ? SER FFF 9   GLY FFF 12  
AC9 2 THR F 105 ? VAL F 109 ? THR FFF 105 VAL FFF 109 
AC9 3 GLY F 85  ? ASP F 93  ? GLY FFF 85  ASP FFF 93  
AC9 4 GLY F 98  ? PHE F 101 ? GLY FFF 98  PHE FFF 101 
AD1 1 VAL F 18  ? SER F 23  ? VAL FFF 18  SER FFF 23  
AD1 2 SER F 71  ? ILE F 76  ? SER FFF 71  ILE FFF 76  
AD1 3 PHE F 63  ? SER F 68  ? PHE FFF 63  SER FFF 68  
AD2 1 THR F 118 ? PHE F 122 ? THR FFF 118 PHE FFF 122 
AD2 2 ALA F 134 ? PHE F 143 ? ALA FFF 134 PHE FFF 143 
AD2 3 THR F 176 ? LEU F 184 ? THR FFF 176 LEU FFF 184 
AD2 4 VAL F 163 ? THR F 165 ? VAL FFF 163 THR FFF 165 
AD3 1 THR F 118 ? PHE F 122 ? THR FFF 118 PHE FFF 122 
AD3 2 ALA F 134 ? PHE F 143 ? ALA FFF 134 PHE FFF 143 
AD3 3 THR F 176 ? LEU F 184 ? THR FFF 176 LEU FFF 184 
AD3 4 SER F 169 ? LYS F 170 ? SER FFF 169 LYS FFF 170 
AD4 1 SER F 196 ? CYS F 197 ? SER FFF 196 CYS FFF 197 
AD4 2 LYS F 208 ? THR F 209 ? LYS FFF 208 THR FFF 209 
AD5 1 SER G 9   ? GLY G 12  ? SER GGG 9   GLY GGG 12  
AD5 2 THR G 105 ? VAL G 109 ? THR GGG 105 VAL GGG 109 
AD5 3 GLY G 85  ? ASP G 93  ? GLY GGG 85  ASP GGG 93  
AD5 4 VAL G 34  ? GLN G 39  ? VAL GGG 34  GLN GGG 39  
AD5 5 LYS G 46  ? ILE G 49  ? LYS GGG 46  ILE GGG 49  
AD6 1 SER G 9   ? GLY G 12  ? SER GGG 9   GLY GGG 12  
AD6 2 THR G 105 ? VAL G 109 ? THR GGG 105 VAL GGG 109 
AD6 3 GLY G 85  ? ASP G 93  ? GLY GGG 85  ASP GGG 93  
AD6 4 GLY G 98  ? PHE G 101 ? GLY GGG 98  PHE GGG 101 
AD7 1 VAL G 18  ? SER G 23  ? VAL GGG 18  SER GGG 23  
AD7 2 SER G 71  ? ILE G 76  ? SER GGG 71  ILE GGG 76  
AD7 3 PHE G 63  ? SER G 68  ? PHE GGG 63  SER GGG 68  
AD8 1 THR G 118 ? VAL G 119 ? THR GGG 118 VAL GGG 119 
AD8 2 LEU G 136 ? PHE G 143 ? LEU GGG 136 PHE GGG 143 
AD8 3 THR G 176 ? LEU G 182 ? THR GGG 176 LEU GGG 182 
AD8 4 GLU G 164 ? THR G 165 ? GLU GGG 164 THR GGG 165 
AD9 1 THR G 118 ? VAL G 119 ? THR GGG 118 VAL GGG 119 
AD9 2 LEU G 136 ? PHE G 143 ? LEU GGG 136 PHE GGG 143 
AD9 3 THR G 176 ? LEU G 182 ? THR GGG 176 LEU GGG 182 
AD9 4 SER G 169 ? LYS G 170 ? SER GGG 169 LYS GGG 170 
AE1 1 SER G 196 ? CYS G 197 ? SER GGG 196 CYS GGG 197 
AE1 2 LYS G 208 ? THR G 209 ? LYS GGG 208 THR GGG 209 
AE2 1 GLN H 3   ? SER H 7   ? GLN HHH 3   SER HHH 7   
AE2 2 LEU H 18  ? SER H 25  ? LEU HHH 18  SER HHH 25  
AE2 3 SER H 78  ? MET H 83  ? SER HHH 78  MET HHH 83  
AE2 4 PHE H 68  ? ASP H 73  ? PHE HHH 68  ASP HHH 73  
AE3 1 LEU H 11  ? VAL H 12  ? LEU HHH 11  VAL HHH 12  
AE3 2 THR H 112 ? VAL H 116 ? THR HHH 112 VAL HHH 116 
AE3 3 ALA H 92  ? ALA H 100 ? ALA HHH 92  ALA HHH 100 
AE3 4 THR H 33  ? GLN H 39  ? THR HHH 33  GLN HHH 39  
AE3 5 LEU H 45  ? ILE H 51  ? LEU HHH 45  ILE HHH 51  
AE3 6 MET H 58  ? TYR H 60  ? MET HHH 58  TYR HHH 60  
AE4 1 LEU H 11  ? VAL H 12  ? LEU HHH 11  VAL HHH 12  
AE4 2 THR H 112 ? VAL H 116 ? THR HHH 112 VAL HHH 116 
AE4 3 ALA H 92  ? ALA H 100 ? ALA HHH 92  ALA HHH 100 
AE4 4 ASN H 104 ? TRP H 108 ? ASN HHH 104 TRP HHH 108 
AE5 1 PHE H 171 ? LEU H 175 ? PHE HHH 176 LEU HHH 180 
AE5 2 TYR H 181 ? SER H 184 ? TYR HHH 186 SER HHH 189 
AE6 1 SER I 9   ? GLY I 12  ? SER III 9   GLY III 12  
AE6 2 THR I 105 ? VAL I 109 ? THR III 105 VAL III 109 
AE6 3 GLY I 85  ? ASP I 93  ? GLY III 85  ASP III 93  
AE6 4 VAL I 34  ? GLN I 39  ? VAL III 34  GLN III 39  
AE6 5 LYS I 46  ? ILE I 49  ? LYS III 46  ILE III 49  
AE7 1 SER I 9   ? GLY I 12  ? SER III 9   GLY III 12  
AE7 2 THR I 105 ? VAL I 109 ? THR III 105 VAL III 109 
AE7 3 GLY I 85  ? ASP I 93  ? GLY III 85  ASP III 93  
AE7 4 GLY I 98  ? PHE I 101 ? GLY III 98  PHE III 101 
AE8 1 VAL I 18  ? SER I 23  ? VAL III 18  SER III 23  
AE8 2 SER I 71  ? ILE I 76  ? SER III 71  ILE III 76  
AE8 3 PHE I 63  ? SER I 68  ? PHE III 63  SER III 68  
AE9 1 THR I 166 ? LYS I 167 ? THR III 166 LYS III 167 
AE9 2 SER I 179 ? SER I 180 ? SER III 179 SER III 180 
AF1 1 GLN J 3   ? SER J 7   ? GLN JJJ 3   SER JJJ 7   
AF1 2 LEU J 18  ? SER J 25  ? LEU JJJ 18  SER JJJ 25  
AF1 3 SER J 78  ? MET J 83  ? SER JJJ 78  MET JJJ 83  
AF1 4 PHE J 68  ? ASP J 73  ? PHE JJJ 68  ASP JJJ 73  
AF2 1 LEU J 11  ? VAL J 12  ? LEU JJJ 11  VAL JJJ 12  
AF2 2 THR J 112 ? VAL J 116 ? THR JJJ 112 VAL JJJ 116 
AF2 3 ALA J 92  ? ALA J 100 ? ALA JJJ 92  ALA JJJ 100 
AF2 4 THR J 33  ? GLN J 39  ? THR JJJ 33  GLN JJJ 39  
AF2 5 GLN J 46  ? ILE J 51  ? GLN JJJ 46  ILE JJJ 51  
AF2 6 MET J 58  ? TYR J 60  ? MET JJJ 58  TYR JJJ 60  
AF3 1 LEU J 11  ? VAL J 12  ? LEU JJJ 11  VAL JJJ 12  
AF3 2 THR J 112 ? VAL J 116 ? THR JJJ 112 VAL JJJ 116 
AF3 3 ALA J 92  ? ALA J 100 ? ALA JJJ 92  ALA JJJ 100 
AF3 4 ASN J 104 ? TRP J 108 ? ASN JJJ 104 TRP JJJ 108 
AF4 1 SER J 125 ? VAL J 126 ? SER JJJ 125 VAL JJJ 126 
AF4 2 CYS J 145 ? TYR J 150 ? CYS JJJ 150 TYR JJJ 155 
AF4 3 TYR J 181 ? SER J 185 ? TYR JJJ 186 SER JJJ 190 
AF4 4 VAL J 174 ? LEU J 175 ? VAL JJJ 179 LEU JJJ 180 
AF5 1 THR J 156 ? SER J 158 ? THR JJJ 161 SER JJJ 163 
AF5 2 ASN J 202 ? ASN J 204 ? ASN JJJ 207 ASN JJJ 209 
AF6 1 SER K 9   ? GLY K 12  ? SER KKK 9   GLY KKK 12  
AF6 2 THR K 105 ? VAL K 109 ? THR KKK 105 VAL KKK 109 
AF6 3 GLY K 85  ? ASP K 93  ? GLY KKK 85  ASP KKK 93  
AF6 4 ASN K 35  ? GLN K 39  ? ASN KKK 35  GLN KKK 39  
AF6 5 LYS K 46  ? ILE K 49  ? LYS KKK 46  ILE KKK 49  
AF7 1 SER K 9   ? GLY K 12  ? SER KKK 9   GLY KKK 12  
AF7 2 THR K 105 ? VAL K 109 ? THR KKK 105 VAL KKK 109 
AF7 3 GLY K 85  ? ASP K 93  ? GLY KKK 85  ASP KKK 93  
AF7 4 GLY K 98  ? PHE K 101 ? GLY KKK 98  PHE KKK 101 
AF8 1 VAL K 18  ? SER K 23  ? VAL KKK 18  SER KKK 23  
AF8 2 SER K 71  ? ILE K 76  ? SER KKK 71  ILE KKK 76  
AF8 3 PHE K 63  ? SER K 68  ? PHE KKK 63  SER KKK 68  
AF9 1 GLN L 3   ? SER L 7   ? GLN LLL 3   SER LLL 7   
AF9 2 LEU L 18  ? SER L 25  ? LEU LLL 18  SER LLL 25  
AF9 3 SER L 78  ? MET L 83  ? SER LLL 78  MET LLL 83  
AF9 4 PHE L 68  ? ASP L 73  ? PHE LLL 68  ASP LLL 73  
AG1 1 LEU L 11  ? VAL L 12  ? LEU LLL 11  VAL LLL 12  
AG1 2 THR L 112 ? VAL L 116 ? THR LLL 112 VAL LLL 116 
AG1 3 ALA L 92  ? ALA L 100 ? ALA LLL 92  ALA LLL 100 
AG1 4 THR L 33  ? GLN L 39  ? THR LLL 33  GLN LLL 39  
AG1 5 GLN L 46  ? ILE L 51  ? GLN LLL 46  ILE LLL 51  
AG1 6 MET L 58  ? TYR L 60  ? MET LLL 58  TYR LLL 60  
AG2 1 LEU L 11  ? VAL L 12  ? LEU LLL 11  VAL LLL 12  
AG2 2 THR L 112 ? VAL L 116 ? THR LLL 112 VAL LLL 116 
AG2 3 ALA L 92  ? ALA L 100 ? ALA LLL 92  ALA LLL 100 
AG2 4 ASN L 104 ? TRP L 108 ? ASN LLL 104 TRP LLL 108 
AG3 1 LEU L 146 ? TYR L 150 ? LEU LLL 151 TYR LLL 155 
AG3 2 TYR L 181 ? SER L 184 ? TYR LLL 186 SER LLL 189 
AG3 3 VAL L 174 ? LEU L 175 ? VAL LLL 179 LEU LLL 180 
AG4 1 SER M 9   ? SER M 11  ? SER MMM 9   SER MMM 11  
AG4 2 THR M 105 ? THR M 108 ? THR MMM 105 THR MMM 108 
AG4 3 GLY M 85  ? ASP M 93  ? GLY MMM 85  ASP MMM 93  
AG4 4 VAL M 34  ? GLN M 39  ? VAL MMM 34  GLN MMM 39  
AG4 5 LYS M 46  ? ILE M 49  ? LYS MMM 46  ILE MMM 49  
AG5 1 SER M 9   ? SER M 11  ? SER MMM 9   SER MMM 11  
AG5 2 THR M 105 ? THR M 108 ? THR MMM 105 THR MMM 108 
AG5 3 GLY M 85  ? ASP M 93  ? GLY MMM 85  ASP MMM 93  
AG5 4 GLY M 98  ? PHE M 101 ? GLY MMM 98  PHE MMM 101 
AG6 1 VAL M 18  ? SER M 23  ? VAL MMM 18  SER MMM 23  
AG6 2 SER M 71  ? ILE M 76  ? SER MMM 71  ILE MMM 76  
AG6 3 PHE M 63  ? SER M 68  ? PHE MMM 63  SER MMM 68  
AG7 1 GLN N 3   ? SER N 7   ? GLN NNN 3   SER NNN 7   
AG7 2 LEU N 18  ? SER N 25  ? LEU NNN 18  SER NNN 25  
AG7 3 SER N 78  ? MET N 83  ? SER NNN 78  MET NNN 83  
AG7 4 PHE N 68  ? ASP N 73  ? PHE NNN 68  ASP NNN 73  
AG8 1 LEU N 11  ? VAL N 12  ? LEU NNN 11  VAL NNN 12  
AG8 2 THR N 112 ? VAL N 116 ? THR NNN 112 VAL NNN 116 
AG8 3 ALA N 92  ? ALA N 100 ? ALA NNN 92  ALA NNN 100 
AG8 4 MET N 34  ? GLN N 39  ? MET NNN 34  GLN NNN 39  
AG8 5 GLN N 46  ? ILE N 51  ? GLN NNN 46  ILE NNN 51  
AG8 6 MET N 58  ? TYR N 60  ? MET NNN 58  TYR NNN 60  
AG9 1 LEU N 11  ? VAL N 12  ? LEU NNN 11  VAL NNN 12  
AG9 2 THR N 112 ? VAL N 116 ? THR NNN 112 VAL NNN 116 
AG9 3 ALA N 92  ? ALA N 100 ? ALA NNN 92  ALA NNN 100 
AG9 4 ASN N 104 ? TRP N 108 ? ASN NNN 104 TRP NNN 108 
AH1 1 GLN O 3   ? SER O 7   ? GLN YYY 3   SER YYY 7   
AH1 2 LEU O 18  ? SER O 25  ? LEU YYY 18  SER YYY 25  
AH1 3 SER O 78  ? MET O 83  ? SER YYY 78  MET YYY 83  
AH1 4 PHE O 68  ? ASP O 73  ? PHE YYY 68  ASP YYY 73  
AH2 1 LEU O 11  ? VAL O 12  ? LEU YYY 11  VAL YYY 12  
AH2 2 THR O 112 ? VAL O 116 ? THR YYY 112 VAL YYY 116 
AH2 3 ALA O 92  ? ALA O 100 ? ALA YYY 92  ALA YYY 100 
AH2 4 THR O 33  ? GLN O 39  ? THR YYY 33  GLN YYY 39  
AH2 5 LEU O 45  ? ILE O 51  ? LEU YYY 45  ILE YYY 51  
AH2 6 MET O 58  ? TYR O 60  ? MET YYY 58  TYR YYY 60  
AH3 1 LEU O 11  ? VAL O 12  ? LEU YYY 11  VAL YYY 12  
AH3 2 THR O 112 ? VAL O 116 ? THR YYY 112 VAL YYY 116 
AH3 3 ALA O 92  ? ALA O 100 ? ALA YYY 92  ALA YYY 100 
AH3 4 ASN O 104 ? TRP O 108 ? ASN YYY 104 TRP YYY 108 
AH4 1 SER O 125 ? LEU O 129 ? SER YYY 125 LEU YYY 129 
AH4 2 GLY O 144 ? TYR O 150 ? GLY YYY 149 TYR YYY 155 
AH4 3 TYR O 181 ? VAL O 186 ? TYR YYY 186 VAL YYY 191 
AH4 4 HIS O 169 ? THR O 170 ? HIS YYY 174 THR YYY 175 
AH5 1 SER O 125 ? LEU O 129 ? SER YYY 125 LEU YYY 129 
AH5 2 GLY O 144 ? TYR O 150 ? GLY YYY 149 TYR YYY 155 
AH5 3 TYR O 181 ? VAL O 186 ? TYR YYY 186 VAL YYY 191 
AH5 4 VAL O 174 ? LEU O 175 ? VAL YYY 179 LEU YYY 180 
AH6 1 THR O 156 ? SER O 158 ? THR YYY 161 SER YYY 163 
AH6 2 ASN O 202 ? ASN O 204 ? ASN YYY 207 ASN YYY 209 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 11  ? N GLU AAA 28  O ARG A 269 ? O ARG AAA 286 
AA1 2 3 O PHE A 261 ? O PHE AAA 278 N CYS A 24  ? N CYS AAA 41  
AA2 1 2 N GLU A 11  ? N GLU AAA 28  O ARG A 269 ? O ARG AAA 286 
AA2 2 3 O ARG A 266 ? O ARG AAA 283 N GLU A 86  ? N GLU AAA 103 
AA2 3 4 N LEU A 90  ? N LEU AAA 107 O THR A 217 ? O THR AAA 234 
AA3 1 2 N ILE A 68  ? N ILE AAA 85  O LEU A 234 ? O LEU AAA 251 
AA3 2 3 N PHE A 245 ? N PHE AAA 262 O GLN A 253 ? O GLN AAA 270 
AA4 1 2 N ILE A 68  ? N ILE AAA 85  O LEU A 234 ? O LEU AAA 251 
AA4 2 3 O TYR A 235 ? O TYR AAA 252 N GLY A 130 ? N GLY AAA 147 
AA4 3 4 N PHE A 127 ? N PHE AAA 144 O PHE A 196 ? O PHE AAA 213 
AA4 4 5 N LEU A 199 ? N LEU AAA 216 O LEU E 209 ? O LEU EEE 226 
AA5 1 2 O ALA A 170 ? O ALA AAA 187 N LEU A 136 ? N LEU AAA 153 
AA5 2 3 N GLN A 137 ? N GLN AAA 154 O VAL A 184 ? O VAL AAA 201 
AA6 1 2 N ILE A 211 ? N ILE AAA 228 O GLY B 197 ? O GLY BBB 214 
AA6 2 3 O PHE B 196 ? O PHE BBB 213 N PHE B 127 ? N PHE BBB 144 
AA6 3 4 N GLY B 130 ? N GLY BBB 147 O TYR B 235 ? O TYR BBB 252 
AA6 4 5 O LEU B 234 ? O LEU BBB 251 N ILE B 68  ? N ILE BBB 85  
AA7 1 2 N ILE A 211 ? N ILE AAA 228 O GLY B 197 ? O GLY BBB 214 
AA7 2 3 O PHE B 196 ? O PHE BBB 213 N PHE B 127 ? N PHE BBB 144 
AA7 3 4 N GLY B 130 ? N GLY BBB 147 O TYR B 235 ? O TYR BBB 252 
AA7 4 5 N PHE B 245 ? N PHE BBB 262 O GLN B 253 ? O GLN BBB 270 
AA8 1 2 N GLU B 11  ? N GLU BBB 28  O ARG B 269 ? O ARG BBB 286 
AA8 2 3 O PHE B 261 ? O PHE BBB 278 N CYS B 24  ? N CYS BBB 41  
AA9 1 2 N GLU B 11  ? N GLU BBB 28  O ARG B 269 ? O ARG BBB 286 
AA9 2 3 O ARG B 266 ? O ARG BBB 283 N GLU B 86  ? N GLU BBB 103 
AA9 3 4 N LEU B 90  ? N LEU BBB 107 O THR B 217 ? O THR BBB 234 
AB1 1 2 O ALA B 170 ? O ALA BBB 187 N LEU B 136 ? N LEU BBB 153 
AB1 2 3 N GLN B 137 ? N GLN BBB 154 O VAL B 184 ? O VAL BBB 201 
AB2 1 2 N LEU B 209 ? N LEU BBB 226 O LEU C 199 ? O LEU CCC 216 
AB2 2 3 O THR C 198 ? O THR CCC 215 N HIS C 125 ? N HIS CCC 142 
AB2 3 4 N GLY C 130 ? N GLY CCC 147 O TYR C 235 ? O TYR CCC 252 
AB2 4 5 O LEU C 234 ? O LEU CCC 251 N ILE C 68  ? N ILE CCC 85  
AB3 1 2 N LEU B 209 ? N LEU BBB 226 O LEU C 199 ? O LEU CCC 216 
AB3 2 3 O THR C 198 ? O THR CCC 215 N HIS C 125 ? N HIS CCC 142 
AB3 3 4 N GLY C 130 ? N GLY CCC 147 O TYR C 235 ? O TYR CCC 252 
AB3 4 5 N PHE C 245 ? N PHE CCC 262 O GLN C 253 ? O GLN CCC 270 
AB4 1 2 N GLU C 11  ? N GLU CCC 28  O ARG C 269 ? O ARG CCC 286 
AB4 2 3 O PHE C 261 ? O PHE CCC 278 N CYS C 24  ? N CYS CCC 41  
AB5 1 2 N GLU C 11  ? N GLU CCC 28  O ARG C 269 ? O ARG CCC 286 
AB5 2 3 O ARG C 266 ? O ARG CCC 283 N GLU C 86  ? N GLU CCC 103 
AB5 3 4 N LEU C 90  ? N LEU CCC 107 O THR C 217 ? O THR CCC 234 
AB6 1 2 O ALA C 170 ? O ALA CCC 187 N LEU C 136 ? N LEU CCC 153 
AB6 2 3 N GLN C 137 ? N GLN CCC 154 O VAL C 184 ? O VAL CCC 201 
AB7 1 2 N ILE C 211 ? N ILE CCC 228 O GLY D 197 ? O GLY DDD 214 
AB7 2 3 O PHE D 196 ? O PHE DDD 213 N PHE D 127 ? N PHE DDD 144 
AB7 3 4 N GLY D 130 ? N GLY DDD 147 O TYR D 235 ? O TYR DDD 252 
AB7 4 5 O LEU D 234 ? O LEU DDD 251 N ILE D 68  ? N ILE DDD 85  
AB8 1 2 N ILE C 211 ? N ILE CCC 228 O GLY D 197 ? O GLY DDD 214 
AB8 2 3 O PHE D 196 ? O PHE DDD 213 N PHE D 127 ? N PHE DDD 144 
AB8 3 4 N GLY D 130 ? N GLY DDD 147 O TYR D 235 ? O TYR DDD 252 
AB8 4 5 N PHE D 245 ? N PHE DDD 262 O GLN D 253 ? O GLN DDD 270 
AB9 1 2 N GLU D 11  ? N GLU DDD 28  O ARG D 269 ? O ARG DDD 286 
AB9 2 3 O PHE D 261 ? O PHE DDD 278 N CYS D 24  ? N CYS DDD 41  
AC1 1 2 N GLU D 11  ? N GLU DDD 28  O ARG D 269 ? O ARG DDD 286 
AC1 2 3 O ARG D 266 ? O ARG DDD 283 N GLU D 86  ? N GLU DDD 103 
AC1 3 4 N LEU D 90  ? N LEU DDD 107 O THR D 217 ? O THR DDD 234 
AC2 1 2 O ALA D 170 ? O ALA DDD 187 N LEU D 136 ? N LEU DDD 153 
AC2 2 3 N GLN D 137 ? N GLN DDD 154 O VAL D 184 ? O VAL DDD 201 
AC3 1 2 N LEU D 209 ? N LEU DDD 226 O LEU E 199 ? O LEU EEE 216 
AC3 2 3 O PHE E 196 ? O PHE EEE 213 N PHE E 127 ? N PHE EEE 144 
AC3 3 4 N GLY E 130 ? N GLY EEE 147 O TYR E 235 ? O TYR EEE 252 
AC3 4 5 O LEU E 234 ? O LEU EEE 251 N ILE E 68  ? N ILE EEE 85  
AC4 1 2 N LEU D 209 ? N LEU DDD 226 O LEU E 199 ? O LEU EEE 216 
AC4 2 3 O PHE E 196 ? O PHE EEE 213 N PHE E 127 ? N PHE EEE 144 
AC4 3 4 N GLY E 130 ? N GLY EEE 147 O TYR E 235 ? O TYR EEE 252 
AC4 4 5 N PHE E 245 ? N PHE EEE 262 O GLN E 253 ? O GLN EEE 270 
AC5 1 2 N LEU E 10  ? N LEU EEE 27  O ARG E 269 ? O ARG EEE 286 
AC5 2 3 O PHE E 261 ? O PHE EEE 278 N CYS E 24  ? N CYS EEE 41  
AC6 1 2 N LEU E 10  ? N LEU EEE 27  O ARG E 269 ? O ARG EEE 286 
AC6 2 3 O ARG E 266 ? O ARG EEE 283 N GLU E 86  ? N GLU EEE 103 
AC6 3 4 N LEU E 90  ? N LEU EEE 107 O THR E 217 ? O THR EEE 234 
AC7 1 2 O ALA E 170 ? O ALA EEE 187 N LEU E 136 ? N LEU EEE 153 
AC7 2 3 N GLN E 137 ? N GLN EEE 154 O VAL E 184 ? O VAL EEE 201 
AC8 1 2 N ALA F 10  ? N ALA FFF 10  O THR F 108 ? O THR FFF 108 
AC8 2 3 O LEU F 107 ? O LEU FFF 107 N GLY F 85  ? N GLY FFF 85  
AC8 3 4 O HIS F 88  ? O HIS FFF 88  N PHE F 37  ? N PHE FFF 37  
AC8 4 5 N TRP F 36  ? N TRP FFF 36  O ILE F 49  ? O ILE FFF 49  
AC9 1 2 N ALA F 10  ? N ALA FFF 10  O THR F 108 ? O THR FFF 108 
AC9 2 3 O LEU F 107 ? O LEU FFF 107 N GLY F 85  ? N GLY FFF 85  
AC9 3 4 N ASP F 93  ? N ASP FFF 93  O GLY F 98  ? O GLY FFF 98  
AD1 1 2 N CYS F 22  ? N CYS FFF 22  O VAL F 72  ? O VAL FFF 72  
AD1 2 3 O ALA F 75  ? O ALA FFF 75  N SER F 64  ? N SER FFF 64  
AD2 1 2 N PHE F 122 ? N PHE FFF 122 O VAL F 137 ? O VAL FFF 137 
AD2 2 3 N ALA F 134 ? N ALA FFF 134 O LEU F 184 ? O LEU FFF 184 
AD2 3 4 O TYR F 181 ? O TYR FFF 181 N GLU F 164 ? N GLU FFF 164 
AD3 1 2 N PHE F 122 ? N PHE FFF 122 O VAL F 137 ? O VAL FFF 137 
AD3 2 3 N ALA F 134 ? N ALA FFF 134 O LEU F 184 ? O LEU FFF 184 
AD3 3 4 O ALA F 177 ? O ALA FFF 177 N SER F 169 ? N SER FFF 169 
AD4 1 2 N CYS F 197 ? N CYS FFF 197 O LYS F 208 ? O LYS FFF 208 
AD5 1 2 N ALA G 10  ? N ALA GGG 10  O THR G 108 ? O THR GGG 108 
AD5 2 3 O LEU G 107 ? O LEU GGG 107 N GLY G 85  ? N GLY GGG 85  
AD5 3 4 O HIS G 88  ? O HIS GGG 88  N PHE G 37  ? N PHE GGG 37  
AD5 4 5 N TRP G 36  ? N TRP GGG 36  O ILE G 49  ? O ILE GGG 49  
AD6 1 2 N ALA G 10  ? N ALA GGG 10  O THR G 108 ? O THR GGG 108 
AD6 2 3 O LEU G 107 ? O LEU GGG 107 N GLY G 85  ? N GLY GGG 85  
AD6 3 4 N ASP G 93  ? N ASP GGG 93  O GLY G 98  ? O GLY GGG 98  
AD7 1 2 N CYS G 22  ? N CYS GGG 22  O VAL G 72  ? O VAL GGG 72  
AD7 2 3 O ALA G 75  ? O ALA GGG 75  N SER G 64  ? N SER GGG 64  
AD8 1 2 N THR G 118 ? N THR GGG 118 O SER G 141 ? O SER GGG 141 
AD8 2 3 N PHE G 143 ? N PHE GGG 143 O THR G 176 ? O THR GGG 176 
AD8 3 4 O TYR G 181 ? O TYR GGG 181 N GLU G 164 ? N GLU GGG 164 
AD9 1 2 N THR G 118 ? N THR GGG 118 O SER G 141 ? O SER GGG 141 
AD9 2 3 N PHE G 143 ? N PHE GGG 143 O THR G 176 ? O THR GGG 176 
AD9 3 4 O ALA G 177 ? O ALA GGG 177 N SER G 169 ? N SER GGG 169 
AE1 1 2 N CYS G 197 ? N CYS GGG 197 O LYS G 208 ? O LYS GGG 208 
AE2 1 2 N SER H 7   ? N SER HHH 7   O SER H 21  ? O SER HHH 21  
AE2 2 3 N LEU H 18  ? N LEU HHH 18  O MET H 83  ? O MET HHH 83  
AE2 3 4 O TYR H 80  ? O TYR HHH 80  N SER H 71  ? N SER HHH 71  
AE3 1 2 N VAL H 12  ? N VAL HHH 12  O THR H 115 ? O THR HHH 115 
AE3 2 3 O THR H 112 ? O THR HHH 112 N TYR H 94  ? N TYR HHH 94  
AE3 3 4 O ALA H 97  ? O ALA HHH 97  N ASN H 35  ? N ASN HHH 35  
AE3 4 5 N ARG H 38  ? N ARG HHH 38  O GLN H 46  ? O GLN HHH 46  
AE3 5 6 N SER H 50  ? N SER HHH 50  O TYR H 59  ? O TYR HHH 59  
AE4 1 2 N VAL H 12  ? N VAL HHH 12  O THR H 115 ? O THR HHH 115 
AE4 2 3 O THR H 112 ? O THR HHH 112 N TYR H 94  ? N TYR HHH 94  
AE4 3 4 N ALA H 100 ? N ALA HHH 100 O ASN H 104 ? O ASN HHH 104 
AE5 1 2 N PHE H 171 ? N PHE HHH 176 O SER H 184 ? O SER HHH 189 
AE6 1 2 N ALA I 10  ? N ALA III 10  O THR I 108 ? O THR III 108 
AE6 2 3 O LEU I 107 ? O LEU III 107 N GLY I 85  ? N GLY III 85  
AE6 3 4 O HIS I 88  ? O HIS III 88  N PHE I 37  ? N PHE III 37  
AE6 4 5 N TRP I 36  ? N TRP III 36  O ILE I 49  ? O ILE III 49  
AE7 1 2 N ALA I 10  ? N ALA III 10  O THR I 108 ? O THR III 108 
AE7 2 3 O LEU I 107 ? O LEU III 107 N GLY I 85  ? N GLY III 85  
AE7 3 4 N ASP I 93  ? N ASP III 93  O GLY I 98  ? O GLY III 98  
AE8 1 2 N CYS I 22  ? N CYS III 22  O VAL I 72  ? O VAL III 72  
AE8 2 3 O ALA I 75  ? O ALA III 75  N SER I 64  ? N SER III 64  
AE9 1 2 N LYS I 167 ? N LYS III 167 O SER I 179 ? O SER III 179 
AF1 1 2 N SER J 7   ? N SER JJJ 7   O SER J 21  ? O SER JJJ 21  
AF1 2 3 N LEU J 18  ? N LEU JJJ 18  O MET J 83  ? O MET JJJ 83  
AF1 3 4 O TYR J 80  ? O TYR JJJ 80  N SER J 71  ? N SER JJJ 71  
AF2 1 2 N VAL J 12  ? N VAL JJJ 12  O THR J 115 ? O THR JJJ 115 
AF2 2 3 O THR J 112 ? O THR JJJ 112 N TYR J 94  ? N TYR JJJ 94  
AF2 3 4 O TYR J 95  ? O TYR JJJ 95  N VAL J 37  ? N VAL JJJ 37  
AF2 4 5 N ARG J 38  ? N ARG JJJ 38  O GLN J 46  ? O GLN JJJ 46  
AF2 5 6 N SER J 50  ? N SER JJJ 50  O TYR J 59  ? O TYR JJJ 59  
AF3 1 2 N VAL J 12  ? N VAL JJJ 12  O THR J 115 ? O THR JJJ 115 
AF3 2 3 O THR J 112 ? O THR JJJ 112 N TYR J 94  ? N TYR JJJ 94  
AF3 3 4 N ALA J 100 ? N ALA JJJ 100 O ASN J 104 ? O ASN JJJ 104 
AF4 1 2 N SER J 125 ? N SER JJJ 125 O LYS J 148 ? O LYS JJJ 153 
AF4 2 3 N VAL J 147 ? N VAL JJJ 152 O LEU J 183 ? O LEU JJJ 188 
AF4 3 4 O SER J 182 ? O SER JJJ 187 N VAL J 174 ? N VAL JJJ 179 
AF5 1 2 N SER J 158 ? N SER JJJ 163 O ASN J 202 ? O ASN JJJ 207 
AF6 1 2 N ALA K 10  ? N ALA KKK 10  O THR K 108 ? O THR KKK 108 
AF6 2 3 O LEU K 107 ? O LEU KKK 107 N GLY K 85  ? N GLY KKK 85  
AF6 3 4 O HIS K 88  ? O HIS KKK 88  N PHE K 37  ? N PHE KKK 37  
AF6 4 5 N TRP K 36  ? N TRP KKK 36  O ILE K 49  ? O ILE KKK 49  
AF7 1 2 N ALA K 10  ? N ALA KKK 10  O THR K 108 ? O THR KKK 108 
AF7 2 3 O LEU K 107 ? O LEU KKK 107 N GLY K 85  ? N GLY KKK 85  
AF7 3 4 N ASP K 93  ? N ASP KKK 93  O GLY K 98  ? O GLY KKK 98  
AF8 1 2 N CYS K 22  ? N CYS KKK 22  O VAL K 72  ? O VAL KKK 72  
AF8 2 3 O ALA K 75  ? O ALA KKK 75  N SER K 64  ? N SER KKK 64  
AF9 1 2 N SER L 7   ? N SER LLL 7   O SER L 21  ? O SER LLL 21  
AF9 2 3 N LEU L 18  ? N LEU LLL 18  O MET L 83  ? O MET LLL 83  
AF9 3 4 O TYR L 80  ? O TYR LLL 80  N SER L 71  ? N SER LLL 71  
AG1 1 2 N VAL L 12  ? N VAL LLL 12  O THR L 115 ? O THR LLL 115 
AG1 2 3 O THR L 112 ? O THR LLL 112 N TYR L 94  ? N TYR LLL 94  
AG1 3 4 O ALA L 97  ? O ALA LLL 97  N ASN L 35  ? N ASN LLL 35  
AG1 4 5 N ARG L 38  ? N ARG LLL 38  O GLN L 46  ? O GLN LLL 46  
AG1 5 6 N SER L 50  ? N SER LLL 50  O TYR L 59  ? O TYR LLL 59  
AG2 1 2 N VAL L 12  ? N VAL LLL 12  O THR L 115 ? O THR LLL 115 
AG2 2 3 O THR L 112 ? O THR LLL 112 N TYR L 94  ? N TYR LLL 94  
AG2 3 4 N ALA L 100 ? N ALA LLL 100 O ASN L 104 ? O ASN LLL 104 
AG3 1 2 N TYR L 150 ? N TYR LLL 155 O TYR L 181 ? O TYR LLL 186 
AG3 2 3 O SER L 182 ? O SER LLL 187 N VAL L 174 ? N VAL LLL 179 
AG4 1 2 N ALA M 10  ? N ALA MMM 10  O THR M 108 ? O THR MMM 108 
AG4 2 3 O LEU M 107 ? O LEU MMM 107 N GLY M 85  ? N GLY MMM 85  
AG4 3 4 O HIS M 88  ? O HIS MMM 88  N PHE M 37  ? N PHE MMM 37  
AG4 4 5 N TRP M 36  ? N TRP MMM 36  O ILE M 49  ? O ILE MMM 49  
AG5 1 2 N ALA M 10  ? N ALA MMM 10  O THR M 108 ? O THR MMM 108 
AG5 2 3 O LEU M 107 ? O LEU MMM 107 N GLY M 85  ? N GLY MMM 85  
AG5 3 4 N ASP M 93  ? N ASP MMM 93  O GLY M 98  ? O GLY MMM 98  
AG6 1 2 N CYS M 22  ? N CYS MMM 22  O VAL M 72  ? O VAL MMM 72  
AG6 2 3 O ALA M 75  ? O ALA MMM 75  N SER M 64  ? N SER MMM 64  
AG7 1 2 N SER N 7   ? N SER NNN 7   O SER N 21  ? O SER NNN 21  
AG7 2 3 N LEU N 18  ? N LEU NNN 18  O MET N 83  ? O MET NNN 83  
AG7 3 4 O TYR N 80  ? O TYR NNN 80  N SER N 71  ? N SER NNN 71  
AG8 1 2 N VAL N 12  ? N VAL NNN 12  O THR N 115 ? O THR NNN 115 
AG8 2 3 O THR N 112 ? O THR NNN 112 N TYR N 94  ? N TYR NNN 94  
AG8 3 4 O ALA N 97  ? O ALA NNN 97  N ASN N 35  ? N ASN NNN 35  
AG8 4 5 N ARG N 38  ? N ARG NNN 38  O GLN N 46  ? O GLN NNN 46  
AG8 5 6 N SER N 50  ? N SER NNN 50  O TYR N 59  ? O TYR NNN 59  
AG9 1 2 N VAL N 12  ? N VAL NNN 12  O THR N 115 ? O THR NNN 115 
AG9 2 3 O THR N 112 ? O THR NNN 112 N TYR N 94  ? N TYR NNN 94  
AG9 3 4 N ALA N 100 ? N ALA NNN 100 O ASN N 104 ? O ASN NNN 104 
AH1 1 2 N SER O 7   ? N SER YYY 7   O SER O 21  ? O SER YYY 21  
AH1 2 3 N LEU O 18  ? N LEU YYY 18  O MET O 83  ? O MET YYY 83  
AH1 3 4 O TYR O 80  ? O TYR YYY 80  N SER O 71  ? N SER YYY 71  
AH2 1 2 N VAL O 12  ? N VAL YYY 12  O THR O 115 ? O THR YYY 115 
AH2 2 3 O THR O 112 ? O THR YYY 112 N TYR O 94  ? N TYR YYY 94  
AH2 3 4 O ALA O 97  ? O ALA YYY 97  N ASN O 35  ? N ASN YYY 35  
AH2 4 5 N ARG O 38  ? N ARG YYY 38  O GLN O 46  ? O GLN YYY 46  
AH2 5 6 N SER O 50  ? N SER YYY 50  O TYR O 59  ? O TYR YYY 59  
AH3 1 2 N VAL O 12  ? N VAL YYY 12  O THR O 115 ? O THR YYY 115 
AH3 2 3 O THR O 112 ? O THR YYY 112 N TYR O 94  ? N TYR YYY 94  
AH3 3 4 N ALA O 100 ? N ALA YYY 100 O ASN O 104 ? O ASN YYY 104 
AH4 1 2 N SER O 125 ? N SER YYY 125 O LYS O 148 ? O LYS YYY 153 
AH4 2 3 N TYR O 150 ? N TYR YYY 155 O TYR O 181 ? O TYR YYY 186 
AH4 3 4 O VAL O 186 ? O VAL YYY 191 N HIS O 169 ? N HIS YYY 174 
AH5 1 2 N SER O 125 ? N SER YYY 125 O LYS O 148 ? O LYS YYY 153 
AH5 2 3 N TYR O 150 ? N TYR YYY 155 O TYR O 181 ? O TYR YYY 186 
AH5 3 4 O SER O 182 ? O SER YYY 187 N VAL O 174 ? N VAL YYY 179 
AH6 1 2 N SER O 158 ? N SER YYY 163 O ASN O 202 ? O ASN YYY 207 
# 
_atom_sites.entry_id                    7PA8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.007296 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000397 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009055 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006330 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 6  6  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 1  1  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 7  7  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 8  8  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S 16 16 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.056   
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1     N N   . VAL A 1 7   ? 179.803 -16.737 18.752  1.000 64.360  ? 24  VAL AAA N   1 
ATOM 2     C CA  . VAL A 1 7   ? 180.715 -15.568 18.940  1.000 61.260  ? 24  VAL AAA CA  1 
ATOM 3     C C   . VAL A 1 7   ? 181.213 -15.553 20.401  1.000 60.470  ? 24  VAL AAA C   1 
ATOM 4     O O   . VAL A 1 7   ? 180.404 -15.429 21.347  1.000 61.010  ? 24  VAL AAA O   1 
ATOM 5     C CB  . VAL A 1 7   ? 180.020 -14.283 18.514  1.000 51.200  ? 24  VAL AAA CB  1 
ATOM 6     N N   . GLU A 1 8   ? 182.520 -15.732 20.589  1.000 64.530  ? 25  GLU AAA N   1 
ATOM 7     C CA  . GLU A 1 8   ? 183.257 -15.454 21.850  1.000 72.920  ? 25  GLU AAA CA  1 
ATOM 8     C C   . GLU A 1 8   ? 183.272 -13.935 22.090  1.000 70.490  ? 25  GLU AAA C   1 
ATOM 9     O O   . GLU A 1 8   ? 183.712 -13.200 21.203  1.000 82.510  ? 25  GLU AAA O   1 
ATOM 10    C CB  . GLU A 1 8   ? 184.671 -16.027 21.803  1.000 71.760  ? 25  GLU AAA CB  1 
ATOM 11    N N   . VAL A 1 9   ? 182.840 -13.490 23.265  1.000 61.580  ? 26  VAL AAA N   1 
ATOM 12    C CA  . VAL A 1 9   ? 182.752 -12.050 23.634  1.000 56.990  ? 26  VAL AAA CA  1 
ATOM 13    C C   . VAL A 1 9   ? 184.013 -11.690 24.415  1.000 57.190  ? 26  VAL AAA C   1 
ATOM 14    O O   . VAL A 1 9   ? 184.201 -12.220 25.511  1.000 55.350  ? 26  VAL AAA O   1 
ATOM 15    C CB  . VAL A 1 9   ? 181.492 -11.762 24.473  1.000 54.100  ? 26  VAL AAA CB  1 
ATOM 16    C CG1 . VAL A 1 9   ? 181.421 -10.306 24.940  1.000 48.680  ? 26  VAL AAA CG1 1 
ATOM 17    C CG2 . VAL A 1 9   ? 180.226 -12.194 23.740  1.000 54.260  ? 26  VAL AAA CG2 1 
ATOM 18    N N   . LEU A 1 10  ? 184.827 -10.797 23.865  1.000 63.880  ? 27  LEU AAA N   1 
ATOM 19    C CA  . LEU A 1 10  ? 186.086 -10.317 24.491  1.000 71.140  ? 27  LEU AAA CA  1 
ATOM 20    C C   . LEU A 1 10  ? 185.771 -9.009  25.217  1.000 72.320  ? 27  LEU AAA C   1 
ATOM 21    O O   . LEU A 1 10  ? 184.598 -8.796  25.523  1.000 84.930  ? 27  LEU AAA O   1 
ATOM 22    C CB  . LEU A 1 10  ? 187.164 -10.176 23.412  1.000 80.680  ? 27  LEU AAA CB  1 
ATOM 23    C CG  . LEU A 1 10  ? 187.999 -11.439 23.167  1.000 88.880  ? 27  LEU AAA CG  1 
ATOM 24    C CD1 . LEU A 1 10  ? 187.175 -12.517 22.463  1.000 86.190  ? 27  LEU AAA CD1 1 
ATOM 25    C CD2 . LEU A 1 10  ? 189.256 -11.109 22.371  1.000 94.670  ? 27  LEU AAA CD2 1 
ATOM 26    N N   . GLU A 1 11  ? 186.781 -8.193  25.503  1.000 74.970  ? 28  GLU AAA N   1 
ATOM 27    C CA  . GLU A 1 11  ? 186.682 -7.047  26.447  1.000 74.540  ? 28  GLU AAA CA  1 
ATOM 28    C C   . GLU A 1 11  ? 186.043 -5.843  25.726  1.000 63.180  ? 28  GLU AAA C   1 
ATOM 29    O O   . GLU A 1 11  ? 185.917 -5.850  24.480  1.000 50.680  ? 28  GLU AAA O   1 
ATOM 30    C CB  . GLU A 1 11  ? 188.063 -6.784  27.068  1.000 86.180  ? 28  GLU AAA CB  1 
ATOM 31    N N   . VAL A 1 12  ? 185.592 -4.865  26.508  1.000 58.350  ? 29  VAL AAA N   1 
ATOM 32    C CA  . VAL A 1 12  ? 184.925 -3.627  26.010  1.000 61.780  ? 29  VAL AAA CA  1 
ATOM 33    C C   . VAL A 1 12  ? 186.026 -2.672  25.541  1.000 63.580  ? 29  VAL AAA C   1 
ATOM 34    O O   . VAL A 1 12  ? 186.851 -2.314  26.380  1.000 67.500  ? 29  VAL AAA O   1 
ATOM 35    C CB  . VAL A 1 12  ? 184.073 -2.965  27.113  1.000 60.600  ? 29  VAL AAA CB  1 
ATOM 36    C CG1 . VAL A 1 12  ? 183.419 -1.688  26.633  1.000 63.580  ? 29  VAL AAA CG1 1 
ATOM 37    C CG2 . VAL A 1 12  ? 183.022 -3.880  27.697  1.000 56.520  ? 29  VAL AAA CG2 1 
ATOM 38    N N   . LYS A 1 13  ? 186.028 -2.250  24.276  1.000 66.160  ? 30  LYS AAA N   1 
ATOM 39    C CA  . LYS A 1 13  ? 186.915 -1.148  23.806  1.000 67.860  ? 30  LYS AAA CA  1 
ATOM 40    C C   . LYS A 1 13  ? 186.420 0.165   24.430  1.000 71.750  ? 30  LYS AAA C   1 
ATOM 41    O O   . LYS A 1 13  ? 185.213 0.410   24.335  1.000 77.480  ? 30  LYS AAA O   1 
ATOM 42    C CB  . LYS A 1 13  ? 186.953 -1.070  22.275  1.000 73.650  ? 30  LYS AAA CB  1 
ATOM 43    C CG  . LYS A 1 13  ? 188.095 -0.203  21.741  1.000 82.190  ? 30  LYS AAA CG  1 
ATOM 44    C CD  . LYS A 1 13  ? 188.196 0.019   20.237  1.000 83.370  ? 30  LYS AAA CD  1 
ATOM 45    C CE  . LYS A 1 13  ? 189.523 0.658   19.866  1.000 82.190  ? 30  LYS AAA CE  1 
ATOM 46    N NZ  . LYS A 1 13  ? 189.878 0.477   18.438  1.000 84.360  ? 30  LYS AAA NZ  1 
ATOM 47    N N   . THR A 1 14  ? 187.298 0.933   25.089  1.000 79.030  ? 31  THR AAA N   1 
ATOM 48    C CA  . THR A 1 14  ? 187.033 2.322   25.591  1.000 81.020  ? 31  THR AAA CA  1 
ATOM 49    C C   . THR A 1 14  ? 187.801 3.330   24.726  1.000 80.020  ? 31  THR AAA C   1 
ATOM 50    O O   . THR A 1 14  ? 188.512 2.893   23.824  1.000 75.760  ? 31  THR AAA O   1 
ATOM 51    C CB  . THR A 1 14  ? 187.405 2.498   27.079  1.000 73.620  ? 31  THR AAA CB  1 
ATOM 52    O OG1 . THR A 1 14  ? 188.812 2.300   27.215  1.000 72.200  ? 31  THR AAA OG1 1 
ATOM 53    C CG2 . THR A 1 14  ? 186.672 1.560   28.020  1.000 66.710  ? 31  THR AAA CG2 1 
ATOM 54    N N   . GLY A 1 15  ? 187.587 4.625   24.961  1.000 82.130  ? 32  GLY AAA N   1 
ATOM 55    C CA  . GLY A 1 15  ? 188.194 5.734   24.195  1.000 87.500  ? 32  GLY AAA CA  1 
ATOM 56    C C   . GLY A 1 15  ? 187.170 6.815   23.901  1.000 93.620  ? 32  GLY AAA C   1 
ATOM 57    O O   . GLY A 1 15  ? 186.006 6.677   24.315  1.000 98.820  ? 32  GLY AAA O   1 
ATOM 58    N N   . VAL A 1 16  ? 187.561 7.867   23.175  1.000 106.370 ? 33  VAL AAA N   1 
ATOM 59    C CA  . VAL A 1 16  ? 186.687 9.039   22.854  1.000 112.310 ? 33  VAL AAA CA  1 
ATOM 60    C C   . VAL A 1 16  ? 185.609 8.625   21.840  1.000 105.980 ? 33  VAL AAA C   1 
ATOM 61    O O   . VAL A 1 16  ? 184.547 9.264   21.856  1.000 106.060 ? 33  VAL AAA O   1 
ATOM 62    C CB  . VAL A 1 16  ? 187.519 10.249  22.381  1.000 125.730 ? 33  VAL AAA CB  1 
ATOM 63    C CG1 . VAL A 1 16  ? 186.666 11.444  21.963  1.000 118.510 ? 33  VAL AAA CG1 1 
ATOM 64    C CG2 . VAL A 1 16  ? 188.506 10.678  23.462  1.000 128.540 ? 33  VAL AAA CG2 1 
ATOM 65    N N   . ASP A 1 17  ? 185.820 7.570   21.041  1.000 88.130  ? 34  ASP AAA N   1 
ATOM 66    C CA  . ASP A 1 17  ? 184.857 7.154   19.987  1.000 82.390  ? 34  ASP AAA CA  1 
ATOM 67    C C   . ASP A 1 17  ? 184.450 5.674   20.126  1.000 78.020  ? 34  ASP AAA C   1 
ATOM 68    O O   . ASP A 1 17  ? 184.357 4.984   19.104  1.000 69.680  ? 34  ASP AAA O   1 
ATOM 69    C CB  . ASP A 1 17  ? 185.461 7.464   18.624  1.000 69.580  ? 34  ASP AAA CB  1 
ATOM 70    N N   . SER A 1 18  ? 184.130 5.240   21.342  1.000 75.620  ? 35  SER AAA N   1 
ATOM 71    C CA  . SER A 1 18  ? 183.693 3.867   21.672  1.000 75.070  ? 35  SER AAA CA  1 
ATOM 72    C C   . SER A 1 18  ? 182.178 3.824   21.931  1.000 70.470  ? 35  SER AAA C   1 
ATOM 73    O O   . SER A 1 18  ? 181.651 2.703   21.954  1.000 66.540  ? 35  SER AAA O   1 
ATOM 74    C CB  . SER A 1 18  ? 184.493 3.342   22.848  1.000 75.750  ? 35  SER AAA CB  1 
ATOM 75    O OG  . SER A 1 18  ? 184.629 4.328   23.861  1.000 82.260  ? 35  SER AAA OG  1 
ATOM 76    N N   . ILE A 1 19  ? 181.512 4.962   22.147  1.000 67.490  ? 36  ILE AAA N   1 
ATOM 77    C CA  . ILE A 1 19  ? 180.060 5.007   22.494  1.000 72.590  ? 36  ILE AAA CA  1 
ATOM 78    C C   . ILE A 1 19  ? 179.306 5.682   21.330  1.000 76.630  ? 36  ILE AAA C   1 
ATOM 79    O O   . ILE A 1 19  ? 179.949 6.424   20.573  1.000 74.480  ? 36  ILE AAA O   1 
ATOM 80    C CB  . ILE A 1 19  ? 179.821 5.679   23.875  1.000 68.830  ? 36  ILE AAA CB  1 
ATOM 81    C CG1 . ILE A 1 19  ? 178.416 5.373   24.437  1.000 75.660  ? 36  ILE AAA CG1 1 
ATOM 82    C CG2 . ILE A 1 19  ? 180.082 7.180   23.797  1.000 60.610  ? 36  ILE AAA CG2 1 
ATOM 83    C CD1 . ILE A 1 19  ? 178.321 5.111   25.936  1.000 73.880  ? 36  ILE AAA CD1 1 
ATOM 84    N N   . THR A 1 20  ? 178.014 5.366   21.159  1.000 71.660  ? 37  THR AAA N   1 
ATOM 85    C CA  . THR A 1 20  ? 177.067 6.036   20.221  1.000 61.040  ? 37  THR AAA CA  1 
ATOM 86    C C   . THR A 1 20  ? 175.642 5.909   20.774  1.000 61.080  ? 37  THR AAA C   1 
ATOM 87    O O   . THR A 1 20  ? 175.453 5.123   21.738  1.000 67.110  ? 37  THR AAA O   1 
ATOM 88    C CB  . THR A 1 20  ? 177.167 5.446   18.809  1.000 61.060  ? 37  THR AAA CB  1 
ATOM 89    O OG1 . THR A 1 20  ? 176.438 6.287   17.907  1.000 60.860  ? 37  THR AAA OG1 1 
ATOM 90    C CG2 . THR A 1 20  ? 176.645 4.028   18.727  1.000 60.650  ? 37  THR AAA CG2 1 
ATOM 91    N N   . GLU A 1 21  ? 174.688 6.656   20.191  1.000 56.400  ? 38  GLU AAA N   1 
ATOM 92    C CA  . GLU A 1 21  ? 173.261 6.738   20.637  1.000 49.370  ? 38  GLU AAA CA  1 
ATOM 93    C C   . GLU A 1 21  ? 172.315 6.616   19.451  1.000 49.050  ? 38  GLU AAA C   1 
ATOM 94    O O   . GLU A 1 21  ? 172.458 7.372   18.506  1.000 63.620  ? 38  GLU AAA O   1 
ATOM 95    C CB  . GLU A 1 21  ? 172.925 8.083   21.265  1.000 45.260  ? 38  GLU AAA CB  1 
ATOM 96    C CG  . GLU A 1 21  ? 173.446 8.224   22.674  1.000 49.680  ? 38  GLU AAA CG  1 
ATOM 97    C CD  . GLU A 1 21  ? 172.862 9.411   23.411  1.000 52.560  ? 38  GLU AAA CD  1 
ATOM 98    O OE1 . GLU A 1 21  ? 172.113 10.192  22.788  1.000 50.070  ? 38  GLU AAA OE1 1 
ATOM 99    O OE2 . GLU A 1 21  ? 173.144 9.529   24.612  1.000 54.480  ? 38  GLU AAA OE2 1 
ATOM 100   N N   . VAL A 1 22  ? 171.379 5.685   19.526  1.000 47.730  ? 39  VAL AAA N   1 
ATOM 101   C CA  . VAL A 1 22  ? 170.151 5.657   18.694  1.000 42.560  ? 39  VAL AAA CA  1 
ATOM 102   C C   . VAL A 1 22  ? 169.028 6.256   19.537  1.000 38.640  ? 39  VAL AAA C   1 
ATOM 103   O O   . VAL A 1 22  ? 168.964 5.991   20.748  1.000 39.080  ? 39  VAL AAA O   1 
ATOM 104   C CB  . VAL A 1 22  ? 169.830 4.220   18.264  1.000 43.210  ? 39  VAL AAA CB  1 
ATOM 105   C CG1 . VAL A 1 22  ? 168.464 4.119   17.603  1.000 48.920  ? 39  VAL AAA CG1 1 
ATOM 106   C CG2 . VAL A 1 22  ? 170.904 3.674   17.355  1.000 43.360  ? 39  VAL AAA CG2 1 
ATOM 107   N N   . GLU A 1 23  ? 168.183 7.045   18.901  1.000 39.060  ? 40  GLU AAA N   1 
ATOM 108   C CA  . GLU A 1 23  ? 166.986 7.675   19.505  1.000 41.340  ? 40  GLU AAA CA  1 
ATOM 109   C C   . GLU A 1 23  ? 165.936 7.712   18.400  1.000 39.610  ? 40  GLU AAA C   1 
ATOM 110   O O   . GLU A 1 23  ? 166.115 8.480   17.477  1.000 41.770  ? 40  GLU AAA O   1 
ATOM 111   C CB  . GLU A 1 23  ? 167.353 9.069   20.015  1.000 43.870  ? 40  GLU AAA CB  1 
ATOM 112   C CG  . GLU A 1 23  ? 166.307 9.736   20.875  1.000 50.840  ? 40  GLU AAA CG  1 
ATOM 113   C CD  . GLU A 1 23  ? 166.692 11.159  21.295  1.000 58.590  ? 40  GLU AAA CD  1 
ATOM 114   O OE1 . GLU A 1 23  ? 166.838 12.014  20.385  1.000 66.200  ? 40  GLU AAA OE1 1 
ATOM 115   O OE2 . GLU A 1 23  ? 166.898 11.430  22.516  1.000 61.330  ? 40  GLU AAA OE2 1 
ATOM 116   N N   . CYS A 1 24  ? 164.921 6.867   18.437  1.000 37.090  ? 41  CYS AAA N   1 
ATOM 117   C CA  . CYS A 1 24  ? 163.806 6.976   17.475  1.000 38.480  ? 41  CYS AAA CA  1 
ATOM 118   C C   . CYS A 1 24  ? 162.463 6.740   18.175  1.000 38.610  ? 41  CYS AAA C   1 
ATOM 119   O O   . CYS A 1 24  ? 162.458 6.531   19.407  1.000 40.700  ? 41  CYS AAA O   1 
ATOM 120   C CB  . CYS A 1 24  ? 164.045 6.010   16.335  1.000 42.610  ? 41  CYS AAA CB  1 
ATOM 121   S SG  . CYS A 1 24  ? 163.827 4.303   16.877  1.000 54.300  ? 41  CYS AAA SG  1 
ATOM 122   N N   . PHE A 1 25  ? 161.371 6.840   17.417  1.000 39.020  ? 42  PHE AAA N   1 
ATOM 123   C CA  . PHE A 1 25  ? 159.983 6.519   17.843  1.000 40.780  ? 42  PHE AAA CA  1 
ATOM 124   C C   . PHE A 1 25  ? 159.516 5.402   16.914  1.000 34.210  ? 42  PHE AAA C   1 
ATOM 125   O O   . PHE A 1 25  ? 159.985 5.394   15.790  1.000 32.840  ? 42  PHE AAA O   1 
ATOM 126   C CB  . PHE A 1 25  ? 159.077 7.760   17.795  1.000 46.800  ? 42  PHE AAA CB  1 
ATOM 127   C CG  . PHE A 1 25  ? 159.024 8.365   16.418  1.000 61.060  ? 42  PHE AAA CG  1 
ATOM 128   C CD1 . PHE A 1 25  ? 160.053 9.180   15.963  1.000 75.470  ? 42  PHE AAA CD1 1 
ATOM 129   C CD2 . PHE A 1 25  ? 158.029 7.996   15.516  1.000 68.370  ? 42  PHE AAA CD2 1 
ATOM 130   C CE1 . PHE A 1 25  ? 160.067 9.645   14.654  1.000 79.730  ? 42  PHE AAA CE1 1 
ATOM 131   C CE2 . PHE A 1 25  ? 158.028 8.483   14.216  1.000 68.120  ? 42  PHE AAA CE2 1 
ATOM 132   C CZ  . PHE A 1 25  ? 159.043 9.310   13.790  1.000 78.810  ? 42  PHE AAA CZ  1 
ATOM 133   N N   . LEU A 1 26  ? 158.691 4.460   17.404  1.000 32.080  ? 43  LEU AAA N   1 
ATOM 134   C CA  . LEU A 1 26  ? 158.020 3.404   16.608  1.000 29.000  ? 43  LEU AAA CA  1 
ATOM 135   C C   . LEU A 1 26  ? 156.535 3.712   16.636  1.000 29.390  ? 43  LEU AAA C   1 
ATOM 136   O O   . LEU A 1 26  ? 156.015 4.005   17.689  1.000 30.690  ? 43  LEU AAA O   1 
ATOM 137   C CB  . LEU A 1 26  ? 158.255 2.018   17.190  1.000 27.710  ? 43  LEU AAA CB  1 
ATOM 138   C CG  . LEU A 1 26  ? 159.426 1.268   16.573  1.000 30.700  ? 43  LEU AAA CG  1 
ATOM 139   C CD1 . LEU A 1 26  ? 160.744 1.916   16.988  1.000 31.440  ? 43  LEU AAA CD1 1 
ATOM 140   C CD2 . LEU A 1 26  ? 159.377 -0.223  16.946  1.000 33.830  ? 43  LEU AAA CD2 1 
ATOM 141   N N   . THR A 1 27  ? 155.874 3.670   15.500  1.000 30.030  ? 44  THR AAA N   1 
ATOM 142   C CA  . THR A 1 27  ? 154.435 3.962   15.417  1.000 28.800  ? 44  THR AAA CA  1 
ATOM 143   C C   . THR A 1 27  ? 153.688 2.653   15.655  1.000 26.130  ? 44  THR AAA C   1 
ATOM 144   O O   . THR A 1 27  ? 154.226 1.563   15.563  1.000 24.400  ? 44  THR AAA O   1 
ATOM 145   C CB  . THR A 1 27  ? 154.103 4.669   14.100  1.000 30.560  ? 44  THR AAA CB  1 
ATOM 146   O OG1 . THR A 1 27  ? 154.060 3.699   13.057  1.000 32.500  ? 44  THR AAA OG1 1 
ATOM 147   C CG2 . THR A 1 27  ? 155.110 5.731   13.735  1.000 30.840  ? 44  THR AAA CG2 1 
ATOM 148   N N   . PRO A 1 28  ? 152.430 2.747   16.082  1.000 26.200  ? 45  PRO AAA N   1 
ATOM 149   C CA  . PRO A 1 28  ? 151.611 1.562   16.273  1.000 28.640  ? 45  PRO AAA CA  1 
ATOM 150   C C   . PRO A 1 28  ? 150.862 1.111   15.019  1.000 29.660  ? 45  PRO AAA C   1 
ATOM 151   O O   . PRO A 1 28  ? 150.207 1.943   14.408  1.000 28.880  ? 45  PRO AAA O   1 
ATOM 152   C CB  . PRO A 1 28  ? 150.613 2.072   17.332  1.000 30.200  ? 45  PRO AAA CB  1 
ATOM 153   C CG  . PRO A 1 28  ? 150.456 3.558   17.059  1.000 27.750  ? 45  PRO AAA CG  1 
ATOM 154   C CD  . PRO A 1 28  ? 151.792 4.003   16.519  1.000 26.910  ? 45  PRO AAA CD  1 
ATOM 155   N N   . GLU A 1 29  ? 150.929 -0.176  14.680  1.000 33.590  ? 46  GLU AAA N   1 
ATOM 156   C CA  . GLU A 1 29  ? 150.086 -0.741  13.590  1.000 39.200  ? 46  GLU AAA CA  1 
ATOM 157   C C   . GLU A 1 29  ? 148.897 -1.447  14.232  1.000 38.180  ? 46  GLU AAA C   1 
ATOM 158   O O   . GLU A 1 29  ? 149.050 -2.596  14.659  1.000 38.030  ? 46  GLU AAA O   1 
ATOM 159   C CB  . GLU A 1 29  ? 150.883 -1.655  12.663  1.000 43.480  ? 46  GLU AAA CB  1 
ATOM 160   C CG  . GLU A 1 29  ? 152.116 -0.996  12.087  1.000 45.220  ? 46  GLU AAA CG  1 
ATOM 161   C CD  . GLU A 1 29  ? 151.872 0.212   11.204  1.000 45.530  ? 46  GLU AAA CD  1 
ATOM 162   O OE1 . GLU A 1 29  ? 152.884 0.800   10.771  1.000 44.390  ? 46  GLU AAA OE1 1 
ATOM 163   O OE2 . GLU A 1 29  ? 150.664 0.565   10.971  1.000 44.910  ? 46  GLU AAA OE2 1 
ATOM 164   N N   . MET A 1 30  ? 147.779 -0.736  14.343  1.000 37.410  ? 47  MET AAA N   1 
ATOM 165   C CA  . MET A 1 30  ? 146.583 -1.205  15.082  1.000 34.200  ? 47  MET AAA CA  1 
ATOM 166   C C   . MET A 1 30  ? 145.566 -1.773  14.105  1.000 33.730  ? 47  MET AAA C   1 
ATOM 167   O O   . MET A 1 30  ? 144.548 -2.240  14.583  1.000 33.960  ? 47  MET AAA O   1 
ATOM 168   C CB  . MET A 1 30  ? 145.931 -0.055  15.856  1.000 35.170  ? 47  MET AAA CB  1 
ATOM 169   C CG  . MET A 1 30  ? 146.699 0.382   17.087  1.000 33.570  ? 47  MET AAA CG  1 
ATOM 170   S SD  . MET A 1 30  ? 147.005 -0.979  18.217  1.000 31.230  ? 47  MET AAA SD  1 
ATOM 171   C CE  . MET A 1 30  ? 148.781 -1.125  18.101  1.000 33.800  ? 47  MET AAA CE  1 
ATOM 172   N N   . GLY A 1 31  ? 145.817 -1.710  12.793  1.000 40.310  ? 48  GLY AAA N   1 
ATOM 173   C CA  . GLY A 1 31  ? 144.896 -2.248  11.764  1.000 47.050  ? 48  GLY AAA CA  1 
ATOM 174   C C   . GLY A 1 31  ? 144.517 -1.223  10.709  1.000 48.840  ? 48  GLY AAA C   1 
ATOM 175   O O   . GLY A 1 31  ? 144.172 -1.661  9.597   1.000 53.360  ? 48  GLY AAA O   1 
ATOM 176   N N   . ASP A 1 32  ? 144.538 0.073   11.073  1.000 45.700  ? 49  ASP AAA N   1 
ATOM 177   C CA  . ASP A 1 32  ? 144.502 1.277   10.193  1.000 38.680  ? 49  ASP AAA CA  1 
ATOM 178   C C   . ASP A 1 32  ? 143.418 1.064   9.144   1.000 36.870  ? 49  ASP AAA C   1 
ATOM 179   O O   . ASP A 1 32  ? 143.695 0.947   7.944   1.000 34.950  ? 49  ASP AAA O   1 
ATOM 180   C CB  . ASP A 1 32  ? 145.874 1.583   9.585   1.000 40.790  ? 49  ASP AAA CB  1 
ATOM 181   C CG  . ASP A 1 32  ? 146.988 2.030   10.531  1.000 48.140  ? 49  ASP AAA CG  1 
ATOM 182   O OD1 . ASP A 1 32  ? 146.825 1.918   11.781  1.000 69.370  ? 49  ASP AAA OD1 1 
ATOM 183   O OD2 . ASP A 1 32  ? 148.033 2.503   10.018  1.000 50.310  ? 49  ASP AAA OD2 1 
ATOM 184   N N   . PRO A 1 33  ? 142.141 1.011   9.584   1.000 36.970  ? 50  PRO AAA N   1 
ATOM 185   C CA  . PRO A 1 33  ? 141.019 0.736   8.695   1.000 41.700  ? 50  PRO AAA CA  1 
ATOM 186   C C   . PRO A 1 33  ? 141.121 1.556   7.401   1.000 44.840  ? 50  PRO AAA C   1 
ATOM 187   O O   . PRO A 1 33  ? 141.345 0.974   6.379   1.000 64.990  ? 50  PRO AAA O   1 
ATOM 188   C CB  . PRO A 1 33  ? 139.777 1.143   9.496   1.000 41.080  ? 50  PRO AAA CB  1 
ATOM 189   C CG  . PRO A 1 33  ? 140.200 1.029   10.921  1.000 39.920  ? 50  PRO AAA CG  1 
ATOM 190   C CD  . PRO A 1 33  ? 141.694 1.291   10.953  1.000 39.490  ? 50  PRO AAA CD  1 
ATOM 191   N N   . ASP A 1 34  ? 141.052 2.876   7.510   1.000 40.930  ? 51  ASP AAA N   1 
ATOM 192   C CA  . ASP A 1 34  ? 140.886 3.792   6.363   1.000 40.480  ? 51  ASP AAA CA  1 
ATOM 193   C C   . ASP A 1 34  ? 141.905 4.936   6.509   1.000 40.900  ? 51  ASP AAA C   1 
ATOM 194   O O   . ASP A 1 34  ? 142.667 4.939   7.489   1.000 41.910  ? 51  ASP AAA O   1 
ATOM 195   C CB  . ASP A 1 34  ? 139.405 4.187   6.272   1.000 40.860  ? 51  ASP AAA CB  1 
ATOM 196   C CG  . ASP A 1 34  ? 138.978 5.408   7.088   1.000 40.620  ? 51  ASP AAA CG  1 
ATOM 197   O OD1 . ASP A 1 34  ? 139.813 5.997   7.806   1.000 34.670  ? 51  ASP AAA OD1 1 
ATOM 198   O OD2 . ASP A 1 34  ? 137.802 5.784   6.989   1.000 44.140  ? 51  ASP AAA OD2 1 
ATOM 199   N N   . GLU A 1 35  ? 141.891 5.882   5.570   1.000 38.450  ? 52  GLU AAA N   1 
ATOM 200   C CA  . GLU A 1 35  ? 142.890 6.968   5.407   1.000 35.070  ? 52  GLU AAA CA  1 
ATOM 201   C C   . GLU A 1 35  ? 142.919 7.897   6.628   1.000 32.920  ? 52  GLU AAA C   1 
ATOM 202   O O   . GLU A 1 35  ? 143.894 8.641   6.749   1.000 34.200  ? 52  GLU AAA O   1 
ATOM 203   C CB  . GLU A 1 35  ? 142.612 7.743   4.114   1.000 37.350  ? 52  GLU AAA CB  1 
ATOM 204   C CG  . GLU A 1 35  ? 141.256 8.407   4.011   1.000 39.440  ? 52  GLU AAA CG  1 
ATOM 205   C CD  . GLU A 1 35  ? 140.983 9.029   2.645   1.000 45.480  ? 52  GLU AAA CD  1 
ATOM 206   O OE1 . GLU A 1 35  ? 141.942 9.421   1.959   1.000 52.580  ? 52  GLU AAA OE1 1 
ATOM 207   O OE2 . GLU A 1 35  ? 139.813 9.145   2.267   1.000 47.430  ? 52  GLU AAA OE2 1 
ATOM 208   N N   . HIS A 1 36  ? 141.936 7.828   7.518   1.000 31.950  ? 53  HIS AAA N   1 
ATOM 209   C CA  . HIS A 1 36  ? 141.661 8.853   8.557   1.000 32.120  ? 53  HIS AAA CA  1 
ATOM 210   C C   . HIS A 1 36  ? 141.837 8.318   9.989   1.000 31.510  ? 53  HIS AAA C   1 
ATOM 211   O O   . HIS A 1 36  ? 141.626 9.125   10.956  1.000 26.190  ? 53  HIS AAA O   1 
ATOM 212   C CB  . HIS A 1 36  ? 140.223 9.331   8.383   1.000 34.670  ? 53  HIS AAA CB  1 
ATOM 213   C CG  . HIS A 1 36  ? 139.967 10.159  7.175   1.000 35.910  ? 53  HIS AAA CG  1 
ATOM 214   N ND1 . HIS A 1 36  ? 140.556 11.370  6.973   1.000 36.880  ? 53  HIS AAA ND1 1 
ATOM 215   C CD2 . HIS A 1 36  ? 139.099 9.997   6.158   1.000 40.190  ? 53  HIS AAA CD2 1 
ATOM 216   C CE1 . HIS A 1 36  ? 140.102 11.903  5.858   1.000 41.770  ? 53  HIS AAA CE1 1 
ATOM 217   N NE2 . HIS A 1 36  ? 139.203 11.086  5.338   1.000 39.120  ? 53  HIS AAA NE2 1 
ATOM 218   N N   . LEU A 1 37  ? 142.155 7.020   10.142  1.000 31.350  ? 54  LEU AAA N   1 
ATOM 219   C CA  . LEU A 1 37  ? 142.032 6.296   11.439  1.000 31.710  ? 54  LEU AAA CA  1 
ATOM 220   C C   . LEU A 1 37  ? 143.331 5.568   11.792  1.000 33.550  ? 54  LEU AAA C   1 
ATOM 221   O O   . LEU A 1 37  ? 143.278 4.530   12.483  1.000 30.840  ? 54  LEU AAA O   1 
ATOM 222   C CB  . LEU A 1 37  ? 140.862 5.320   11.333  1.000 31.560  ? 54  LEU AAA CB  1 
ATOM 223   C CG  . LEU A 1 37  ? 139.482 5.982   11.283  1.000 31.630  ? 54  LEU AAA CG  1 
ATOM 224   C CD1 . LEU A 1 37  ? 138.415 4.936   11.128  1.000 32.420  ? 54  LEU AAA CD1 1 
ATOM 225   C CD2 . LEU A 1 37  ? 139.167 6.818   12.514  1.000 31.530  ? 54  LEU AAA CD2 1 
ATOM 226   N N   . ARG A 1 38  ? 144.464 6.112   11.358  1.000 35.950  ? 55  ARG AAA N   1 
ATOM 227   C CA  . ARG A 1 38  ? 145.804 5.602   11.719  1.000 35.540  ? 55  ARG AAA CA  1 
ATOM 228   C C   . ARG A 1 38  ? 145.907 5.552   13.251  1.000 34.520  ? 55  ARG AAA C   1 
ATOM 229   O O   . ARG A 1 38  ? 145.627 6.578   13.906  1.000 31.430  ? 55  ARG AAA O   1 
ATOM 230   C CB  . ARG A 1 38  ? 146.848 6.513   11.087  1.000 36.440  ? 55  ARG AAA CB  1 
ATOM 231   C CG  . ARG A 1 38  ? 148.281 6.096   11.349  1.000 37.000  ? 55  ARG AAA CG  1 
ATOM 232   C CD  . ARG A 1 38  ? 148.948 5.620   10.099  1.000 40.830  ? 55  ARG AAA CD  1 
ATOM 233   N NE  . ARG A 1 38  ? 150.365 5.538   10.401  1.000 50.880  ? 55  ARG AAA NE  1 
ATOM 234   C CZ  . ARG A 1 38  ? 150.953 4.562   11.104  1.000 56.550  ? 55  ARG AAA CZ  1 
ATOM 235   N NH1 . ARG A 1 38  ? 150.260 3.541   11.591  1.000 53.800  ? 55  ARG AAA NH1 1 
ATOM 236   N NH2 . ARG A 1 38  ? 152.256 4.618   11.305  1.000 57.880  ? 55  ARG AAA NH2 1 
ATOM 237   N N   . GLY A 1 39  ? 146.258 4.387   13.801  1.000 33.650  ? 56  GLY AAA N   1 
ATOM 238   C CA  . GLY A 1 39  ? 146.394 4.192   15.254  1.000 34.650  ? 56  GLY AAA CA  1 
ATOM 239   C C   . GLY A 1 39  ? 145.121 3.637   15.864  1.000 35.140  ? 56  GLY AAA C   1 
ATOM 240   O O   . GLY A 1 39  ? 145.098 3.421   17.077  1.000 36.520  ? 56  GLY AAA O   1 
ATOM 241   N N   . PHE A 1 40  ? 144.102 3.384   15.048  1.000 31.080  ? 57  PHE AAA N   1 
ATOM 242   C CA  . PHE A 1 40  ? 142.901 2.632   15.460  1.000 29.420  ? 57  PHE AAA CA  1 
ATOM 243   C C   . PHE A 1 40  ? 142.891 1.301   14.716  1.000 26.880  ? 57  PHE AAA C   1 
ATOM 244   O O   . PHE A 1 40  ? 143.620 1.135   13.755  1.000 22.770  ? 57  PHE AAA O   1 
ATOM 245   C CB  . PHE A 1 40  ? 141.619 3.422   15.185  1.000 29.700  ? 57  PHE AAA CB  1 
ATOM 246   C CG  . PHE A 1 40  ? 141.518 4.734   15.920  1.000 29.040  ? 57  PHE AAA CG  1 
ATOM 247   C CD1 . PHE A 1 40  ? 142.280 5.827   15.536  1.000 31.330  ? 57  PHE AAA CD1 1 
ATOM 248   C CD2 . PHE A 1 40  ? 140.650 4.887   16.985  1.000 29.410  ? 57  PHE AAA CD2 1 
ATOM 249   C CE1 . PHE A 1 40  ? 142.185 7.042   16.202  1.000 33.020  ? 57  PHE AAA CE1 1 
ATOM 250   C CE2 . PHE A 1 40  ? 140.548 6.097   17.658  1.000 32.280  ? 57  PHE AAA CE2 1 
ATOM 251   C CZ  . PHE A 1 40  ? 141.318 7.177   17.261  1.000 32.810  ? 57  PHE AAA CZ  1 
ATOM 252   N N   . SER A 1 41  ? 142.080 0.372   15.203  1.000 28.240  ? 58  SER AAA N   1 
ATOM 253   C CA  . SER A 1 41  ? 141.622 -0.821  14.458  1.000 27.450  ? 58  SER AAA CA  1 
ATOM 254   C C   . SER A 1 41  ? 140.242 -0.502  13.918  1.000 25.240  ? 58  SER AAA C   1 
ATOM 255   O O   . SER A 1 41  ? 139.693 0.570   14.270  1.000 21.770  ? 58  SER AAA O   1 
ATOM 256   C CB  . SER A 1 41  ? 141.564 -2.053  15.310  1.000 27.970  ? 58  SER AAA CB  1 
ATOM 257   O OG  . SER A 1 41  ? 140.436 -2.018  16.169  1.000 28.740  ? 58  SER AAA OG  1 
ATOM 258   N N   . LYS A 1 42  ? 139.742 -1.406  13.086  1.000 25.710  ? 59  LYS AAA N   1 
ATOM 259   C CA  . LYS A 1 42  ? 138.361 -1.356  12.579  1.000 27.770  ? 59  LYS AAA CA  1 
ATOM 260   C C   . LYS A 1 42  ? 137.484 -1.765  13.744  1.000 26.400  ? 59  LYS AAA C   1 
ATOM 261   O O   . LYS A 1 42  ? 137.950 -2.584  14.575  1.000 26.320  ? 59  LYS AAA O   1 
ATOM 262   C CB  . LYS A 1 42  ? 138.174 -2.279  11.368  1.000 29.510  ? 59  LYS AAA CB  1 
ATOM 263   C CG  . LYS A 1 42  ? 136.769 -2.332  10.788  1.000 31.410  ? 59  LYS AAA CG  1 
ATOM 264   C CD  . LYS A 1 42  ? 136.672 -3.294  9.633   1.000 32.790  ? 59  LYS AAA CD  1 
ATOM 265   C CE  . LYS A 1 42  ? 135.354 -3.259  8.902   1.000 34.750  ? 59  LYS AAA CE  1 
ATOM 266   N NZ  . LYS A 1 42  ? 135.430 -4.138  7.708   1.000 36.830  ? 59  LYS AAA NZ  1 
ATOM 267   N N   . SER A 1 43  ? 136.281 -1.213  13.803  1.000 26.100  ? 60  SER AAA N   1 
ATOM 268   C CA  . SER A 1 43  ? 135.303 -1.602  14.839  1.000 28.390  ? 60  SER AAA CA  1 
ATOM 269   C C   . SER A 1 43  ? 135.177 -3.135  14.848  1.000 28.680  ? 60  SER AAA C   1 
ATOM 270   O O   . SER A 1 43  ? 134.893 -3.718  13.805  1.000 28.430  ? 60  SER AAA O   1 
ATOM 271   C CB  . SER A 1 43  ? 134.003 -0.880  14.663  1.000 30.070  ? 60  SER AAA CB  1 
ATOM 272   O OG  . SER A 1 43  ? 134.131 0.450   15.161  1.000 29.660  ? 60  SER AAA OG  1 
ATOM 273   N N   . ILE A 1 44  ? 135.432 -3.726  16.016  1.000 28.380  ? 61  ILE AAA N   1 
ATOM 274   C CA  . ILE A 1 44  ? 135.577 -5.183  16.266  1.000 26.180  ? 61  ILE AAA CA  1 
ATOM 275   C C   . ILE A 1 44  ? 134.230 -5.869  16.089  1.000 24.960  ? 61  ILE AAA C   1 
ATOM 276   O O   . ILE A 1 44  ? 133.249 -5.367  16.619  1.000 24.920  ? 61  ILE AAA O   1 
ATOM 277   C CB  . ILE A 1 44  ? 136.112 -5.404  17.682  1.000 25.520  ? 61  ILE AAA CB  1 
ATOM 278   C CG1 . ILE A 1 44  ? 137.500 -4.776  17.808  1.000 24.930  ? 61  ILE AAA CG1 1 
ATOM 279   C CG2 . ILE A 1 44  ? 136.116 -6.886  17.986  1.000 26.840  ? 61  ILE AAA CG2 1 
ATOM 280   C CD1 . ILE A 1 44  ? 138.153 -4.949  19.148  1.000 25.210  ? 61  ILE AAA CD1 1 
ATOM 281   N N   . SER A 1 45  ? 134.194 -6.972  15.357  1.000 23.990  ? 62  SER AAA N   1 
ATOM 282   C CA  . SER A 1 45  ? 132.976 -7.813  15.214  1.000 24.480  ? 62  SER AAA CA  1 
ATOM 283   C C   . SER A 1 45  ? 133.315 -9.189  15.766  1.000 22.860  ? 62  SER AAA C   1 
ATOM 284   O O   . SER A 1 45  ? 134.511 -9.456  15.936  1.000 23.210  ? 62  SER AAA O   1 
ATOM 285   C CB  . SER A 1 45  ? 132.489 -7.902  13.774  1.000 26.120  ? 62  SER AAA CB  1 
ATOM 286   O OG  . SER A 1 45  ? 132.989 -6.833  12.960  1.000 26.240  ? 62  SER AAA OG  1 
ATOM 287   N N   . ILE A 1 46  ? 132.307 -10.015 16.020  1.000 21.870  ? 63  ILE AAA N   1 
ATOM 288   C CA  . ILE A 1 46  ? 132.458 -11.344 16.669  1.000 21.760  ? 63  ILE AAA CA  1 
ATOM 289   C C   . ILE A 1 46  ? 131.908 -12.435 15.744  1.000 21.370  ? 63  ILE AAA C   1 
ATOM 290   O O   . ILE A 1 46  ? 130.739 -12.322 15.273  1.000 22.580  ? 63  ILE AAA O   1 
ATOM 291   C CB  . ILE A 1 46  ? 131.728 -11.340 18.023  1.000 23.110  ? 63  ILE AAA CB  1 
ATOM 292   C CG1 . ILE A 1 46  ? 132.386 -10.365 19.005  1.000 24.540  ? 63  ILE AAA CG1 1 
ATOM 293   C CG2 . ILE A 1 46  ? 131.693 -12.745 18.582  1.000 24.850  ? 63  ILE AAA CG2 1 
ATOM 294   C CD1 . ILE A 1 46  ? 131.683 -10.225 20.342  1.000 26.110  ? 63  ILE AAA CD1 1 
ATOM 295   N N   . SER A 1 47  ? 132.666 -13.514 15.558  1.000 19.880  ? 64  SER AAA N   1 
ATOM 296   C CA  . SER A 1 47  ? 132.284 -14.606 14.629  1.000 21.390  ? 64  SER AAA CA  1 
ATOM 297   C C   . SER A 1 47  ? 130.880 -15.129 14.944  1.000 23.770  ? 64  SER AAA C   1 
ATOM 298   O O   . SER A 1 47  ? 130.468 -15.081 16.116  1.000 26.760  ? 64  SER AAA O   1 
ATOM 299   C CB  . SER A 1 47  ? 133.303 -15.703 14.624  1.000 21.190  ? 64  SER AAA CB  1 
ATOM 300   O OG  . SER A 1 47  ? 133.677 -16.054 15.933  1.000 24.520  ? 64  SER AAA OG  1 
ATOM 301   N N   . ASP A 1 48  ? 130.169 -15.591 13.924  1.000 26.620  ? 65  ASP AAA N   1 
ATOM 302   C CA  . ASP A 1 48  ? 128.850 -16.273 14.043  1.000 29.690  ? 65  ASP AAA CA  1 
ATOM 303   C C   . ASP A 1 48  ? 129.022 -17.527 14.931  1.000 26.340  ? 65  ASP AAA C   1 
ATOM 304   O O   . ASP A 1 48  ? 128.074 -17.877 15.645  1.000 23.470  ? 65  ASP AAA O   1 
ATOM 305   C CB  . ASP A 1 48  ? 128.213 -16.527 12.656  1.000 36.320  ? 65  ASP AAA CB  1 
ATOM 306   C CG  . ASP A 1 48  ? 129.045 -17.399 11.694  1.000 49.240  ? 65  ASP AAA CG  1 
ATOM 307   O OD1 . ASP A 1 48  ? 130.172 -16.963 11.280  1.000 60.080  ? 65  ASP AAA OD1 1 
ATOM 308   O OD2 . ASP A 1 48  ? 128.571 -18.524 11.339  1.000 54.470  ? 65  ASP AAA OD2 1 
ATOM 309   N N   . THR A 1 49  ? 130.191 -18.175 14.904  1.000 26.390  ? 66  THR AAA N   1 
ATOM 310   C CA  . THR A 1 49  ? 130.453 -19.488 15.568  1.000 25.530  ? 66  THR AAA CA  1 
ATOM 311   C C   . THR A 1 49  ? 131.925 -19.612 15.954  1.000 24.610  ? 66  THR AAA C   1 
ATOM 312   O O   . THR A 1 49  ? 132.767 -18.935 15.364  1.000 22.490  ? 66  THR AAA O   1 
ATOM 313   C CB  . THR A 1 49  ? 130.145 -20.687 14.670  1.000 25.980  ? 66  THR AAA CB  1 
ATOM 314   O OG1 . THR A 1 49  ? 131.106 -20.671 13.599  1.000 24.930  ? 66  THR AAA OG1 1 
ATOM 315   C CG2 . THR A 1 49  ? 128.698 -20.696 14.206  1.000 26.550  ? 66  THR AAA CG2 1 
ATOM 316   N N   . PHE A 1 50  ? 132.229 -20.495 16.893  1.000 25.370  ? 67  PHE AAA N   1 
ATOM 317   C CA  . PHE A 1 50  ? 133.598 -20.615 17.426  1.000 25.930  ? 67  PHE AAA CA  1 
ATOM 318   C C   . PHE A 1 50  ? 134.523 -21.099 16.313  1.000 25.340  ? 67  PHE AAA C   1 
ATOM 319   O O   . PHE A 1 50  ? 135.720 -20.803 16.317  1.000 29.000  ? 67  PHE AAA O   1 
ATOM 320   C CB  . PHE A 1 50  ? 133.627 -21.573 18.615  1.000 26.870  ? 67  PHE AAA CB  1 
ATOM 321   C CG  . PHE A 1 50  ? 134.921 -21.569 19.375  1.000 25.550  ? 67  PHE AAA CG  1 
ATOM 322   C CD1 . PHE A 1 50  ? 135.290 -20.471 20.131  1.000 24.830  ? 67  PHE AAA CD1 1 
ATOM 323   C CD2 . PHE A 1 50  ? 135.749 -22.670 19.343  1.000 26.320  ? 67  PHE AAA CD2 1 
ATOM 324   C CE1 . PHE A 1 50  ? 136.466 -20.473 20.850  1.000 25.170  ? 67  PHE AAA CE1 1 
ATOM 325   C CE2 . PHE A 1 50  ? 136.934 -22.677 20.054  1.000 26.990  ? 67  PHE AAA CE2 1 
ATOM 326   C CZ  . PHE A 1 50  ? 137.282 -21.580 20.818  1.000 27.480  ? 67  PHE AAA CZ  1 
ATOM 327   N N   . GLU A 1 51  ? 133.928 -21.861 15.400  1.000 25.460  ? 68  GLU AAA N   1 
ATOM 328   C CA  . GLU A 1 51  ? 134.606 -22.625 14.325  1.000 25.680  ? 68  GLU AAA CA  1 
ATOM 329   C C   . GLU A 1 51  ? 134.952 -21.671 13.195  1.000 26.070  ? 68  GLU AAA C   1 
ATOM 330   O O   . GLU A 1 51  ? 135.976 -21.907 12.575  1.000 35.820  ? 68  GLU AAA O   1 
ATOM 331   C CB  . GLU A 1 51  ? 133.707 -23.779 13.865  1.000 23.390  ? 68  GLU AAA CB  1 
ATOM 332   C CG  . GLU A 1 51  ? 133.524 -24.834 14.944  1.000 22.080  ? 68  GLU AAA CG  1 
ATOM 333   C CD  . GLU A 1 51  ? 132.278 -24.754 15.809  1.000 22.450  ? 68  GLU AAA CD  1 
ATOM 334   O OE1 . GLU A 1 51  ? 131.843 -25.817 16.277  1.000 23.220  ? 68  GLU AAA OE1 1 
ATOM 335   O OE2 . GLU A 1 51  ? 131.753 -23.635 16.060  1.000 24.480  ? 68  GLU AAA OE2 1 
ATOM 336   N N   . SER A 1 52  ? 134.163 -20.622 12.992  1.000 24.400  ? 69  SER AAA N   1 
ATOM 337   C CA  . SER A 1 52  ? 134.250 -19.705 11.826  1.000 23.110  ? 69  SER AAA CA  1 
ATOM 338   C C   . SER A 1 52  ? 134.979 -18.398 12.162  1.000 23.310  ? 69  SER AAA C   1 
ATOM 339   O O   . SER A 1 52  ? 134.887 -17.467 11.387  1.000 22.700  ? 69  SER AAA O   1 
ATOM 340   C CB  . SER A 1 52  ? 132.868 -19.434 11.292  1.000 23.730  ? 69  SER AAA CB  1 
ATOM 341   O OG  . SER A 1 52  ? 132.033 -18.736 12.209  1.000 22.850  ? 69  SER AAA OG  1 
ATOM 342   N N   . ASP A 1 53  ? 135.660 -18.312 13.300  1.000 27.490  ? 70  ASP AAA N   1 
ATOM 343   C CA  . ASP A 1 53  ? 136.470 -17.120 13.680  1.000 29.340  ? 70  ASP AAA CA  1 
ATOM 344   C C   . ASP A 1 53  ? 137.394 -16.799 12.506  1.000 32.770  ? 70  ASP AAA C   1 
ATOM 345   O O   . ASP A 1 53  ? 138.159 -17.724 12.119  1.000 43.180  ? 70  ASP AAA O   1 
ATOM 346   C CB  . ASP A 1 53  ? 137.326 -17.368 14.925  1.000 27.610  ? 70  ASP AAA CB  1 
ATOM 347   C CG  . ASP A 1 53  ? 137.926 -16.108 15.510  1.000 27.260  ? 70  ASP AAA CG  1 
ATOM 348   O OD1 . ASP A 1 53  ? 137.184 -15.113 15.641  1.000 25.030  ? 70  ASP AAA OD1 1 
ATOM 349   O OD2 . ASP A 1 53  ? 139.109 -16.144 15.859  1.000 28.470  ? 70  ASP AAA OD2 1 
ATOM 350   N N   . SER A 1 54  ? 137.290 -15.600 11.916  1.000 29.430  ? 71  SER AAA N   1 
ATOM 351   C CA  . SER A 1 54  ? 138.219 -15.178 10.836  1.000 28.190  ? 71  SER AAA CA  1 
ATOM 352   C C   . SER A 1 54  ? 138.292 -13.660 10.757  1.000 25.980  ? 71  SER AAA C   1 
ATOM 353   O O   . SER A 1 54  ? 137.758 -13.046 9.844   1.000 26.280  ? 71  SER AAA O   1 
ATOM 354   C CB  . SER A 1 54  ? 137.885 -15.807 9.501   1.000 29.830  ? 71  SER AAA CB  1 
ATOM 355   O OG  . SER A 1 54  ? 136.513 -15.755 9.217   1.000 33.270  ? 71  SER AAA OG  1 
ATOM 356   N N   . PRO A 1 55  ? 139.059 -13.026 11.658  1.000 24.160  ? 72  PRO AAA N   1 
ATOM 357   C CA  . PRO A 1 55  ? 139.168 -11.579 11.705  1.000 24.930  ? 72  PRO AAA CA  1 
ATOM 358   C C   . PRO A 1 55  ? 139.741 -10.969 10.420  1.000 27.110  ? 72  PRO AAA C   1 
ATOM 359   O O   . PRO A 1 55  ? 140.732 -11.520 9.935   1.000 27.920  ? 72  PRO AAA O   1 
ATOM 360   C CB  . PRO A 1 55  ? 140.198 -11.391 12.826  1.000 25.170  ? 72  PRO AAA CB  1 
ATOM 361   C CG  . PRO A 1 55  ? 141.043 -12.626 12.774  1.000 24.750  ? 72  PRO AAA CG  1 
ATOM 362   C CD  . PRO A 1 55  ? 139.981 -13.679 12.596  1.000 24.750  ? 72  PRO AAA CD  1 
ATOM 363   N N   . ASN A 1 56  ? 139.149 -9.862  9.943   1.000 30.350  ? 73  ASN AAA N   1 
ATOM 364   C CA  . ASN A 1 56  ? 139.687 -9.023  8.838   1.000 32.010  ? 73  ASN AAA CA  1 
ATOM 365   C C   . ASN A 1 56  ? 141.042 -8.466  9.248   1.000 29.970  ? 73  ASN AAA C   1 
ATOM 366   O O   . ASN A 1 56  ? 141.218 -8.242  10.432  1.000 28.110  ? 73  ASN AAA O   1 
ATOM 367   C CB  . ASN A 1 56  ? 138.757 -7.862  8.486   1.000 36.550  ? 73  ASN AAA CB  1 
ATOM 368   C CG  . ASN A 1 56  ? 137.464 -8.307  7.842   1.000 40.520  ? 73  ASN AAA CG  1 
ATOM 369   O OD1 . ASN A 1 56  ? 137.292 -9.487  7.542   1.000 46.320  ? 73  ASN AAA OD1 1 
ATOM 370   N ND2 . ASN A 1 56  ? 136.571 -7.363  7.616   1.000 41.510  ? 73  ASN AAA ND2 1 
ATOM 371   N N   . ARG A 1 57  ? 141.930 -8.190  8.301   1.000 31.660  ? 74  ARG AAA N   1 
ATOM 372   C CA  . ARG A 1 57  ? 143.316 -7.752  8.620   1.000 32.500  ? 74  ARG AAA CA  1 
ATOM 373   C C   . ARG A 1 57  ? 143.314 -6.404  9.356   1.000 31.660  ? 74  ARG AAA C   1 
ATOM 374   O O   . ARG A 1 57  ? 144.267 -6.142  10.142  1.000 32.330  ? 74  ARG AAA O   1 
ATOM 375   C CB  . ARG A 1 57  ? 144.141 -7.657  7.339   1.000 33.540  ? 74  ARG AAA CB  1 
ATOM 376   C CG  . ARG A 1 57  ? 145.596 -7.282  7.560   1.000 33.840  ? 74  ARG AAA CG  1 
ATOM 377   C CD  . ARG A 1 57  ? 146.294 -7.062  6.240   1.000 35.400  ? 74  ARG AAA CD  1 
ATOM 378   N NE  . ARG A 1 57  ? 147.678 -6.731  6.458   1.000 38.240  ? 74  ARG AAA NE  1 
ATOM 379   C CZ  . ARG A 1 57  ? 148.469 -6.144  5.564   1.000 41.780  ? 74  ARG AAA CZ  1 
ATOM 380   N NH1 . ARG A 1 57  ? 147.987 -5.826  4.375   1.000 41.660  ? 74  ARG AAA NH1 1 
ATOM 381   N NH2 . ARG A 1 57  ? 149.727 -5.856  5.865   1.000 43.490  ? 74  ARG AAA NH2 1 
ATOM 382   N N   . ASP A 1 58  ? 142.305 -5.567  9.107   1.000 29.930  ? 75  ASP AAA N   1 
ATOM 383   C CA  . ASP A 1 58  ? 142.225 -4.201  9.688   1.000 33.100  ? 75  ASP AAA CA  1 
ATOM 384   C C   . ASP A 1 58  ? 141.583 -4.244  11.081  1.000 30.550  ? 75  ASP AAA C   1 
ATOM 385   O O   . ASP A 1 58  ? 141.397 -3.172  11.679  1.000 31.370  ? 75  ASP AAA O   1 
ATOM 386   C CB  . ASP A 1 58  ? 141.514 -3.244  8.727   1.000 37.970  ? 75  ASP AAA CB  1 
ATOM 387   C CG  . ASP A 1 58  ? 140.205 -3.726  8.160   1.000 41.320  ? 75  ASP AAA CG  1 
ATOM 388   O OD1 . ASP A 1 58  ? 139.729 -4.794  8.596   1.000 50.640  ? 75  ASP AAA OD1 1 
ATOM 389   O OD2 . ASP A 1 58  ? 139.638 -2.977  7.347   1.000 40.500  ? 75  ASP AAA OD2 1 
ATOM 390   N N   . MET A 1 59  ? 141.279 -5.431  11.602  1.000 28.390  ? 76  MET AAA N   1 
ATOM 391   C CA  . MET A 1 59  ? 140.788 -5.620  12.994  1.000 26.370  ? 76  MET AAA CA  1 
ATOM 392   C C   . MET A 1 59  ? 141.899 -6.190  13.889  1.000 27.110  ? 76  MET AAA C   1 
ATOM 393   O O   . MET A 1 59  ? 141.620 -6.452  15.097  1.000 29.320  ? 76  MET AAA O   1 
ATOM 394   C CB  . MET A 1 59  ? 139.613 -6.587  12.995  1.000 24.620  ? 76  MET AAA CB  1 
ATOM 395   C CG  . MET A 1 59  ? 138.721 -6.417  14.178  1.000 25.470  ? 76  MET AAA CG  1 
ATOM 396   S SD  . MET A 1 59  ? 137.421 -7.650  14.209  1.000 28.360  ? 76  MET AAA SD  1 
ATOM 397   C CE  . MET A 1 59  ? 138.316 -9.081  14.791  1.000 28.520  ? 76  MET AAA CE  1 
ATOM 398   N N   . LEU A 1 60  ? 143.102 -6.393  13.341  1.000 25.840  ? 77  LEU AAA N   1 
ATOM 399   C CA  . LEU A 1 60  ? 144.211 -7.107  14.022  1.000 25.770  ? 77  LEU AAA CA  1 
ATOM 400   C C   . LEU A 1 60  ? 145.401 -6.176  14.213  1.000 27.080  ? 77  LEU AAA C   1 
ATOM 401   O O   . LEU A 1 60  ? 146.172 -5.914  13.285  1.000 30.580  ? 77  LEU AAA O   1 
ATOM 402   C CB  . LEU A 1 60  ? 144.635 -8.323  13.203  1.000 25.290  ? 77  LEU AAA CB  1 
ATOM 403   C CG  . LEU A 1 60  ? 143.639 -9.473  13.144  1.000 28.450  ? 77  LEU AAA CG  1 
ATOM 404   C CD1 . LEU A 1 60  ? 144.204 -10.616 12.306  1.000 30.730  ? 77  LEU AAA CD1 1 
ATOM 405   C CD2 . LEU A 1 60  ? 143.289 -9.981  14.542  1.000 30.750  ? 77  LEU AAA CD2 1 
ATOM 406   N N   . PRO A 1 61  ? 145.599 -5.646  15.432  1.000 25.680  ? 78  PRO AAA N   1 
ATOM 407   C CA  . PRO A 1 61  ? 146.883 -5.058  15.798  1.000 26.110  ? 78  PRO AAA CA  1 
ATOM 408   C C   . PRO A 1 61  ? 148.043 -6.013  15.514  1.000 24.890  ? 78  PRO AAA C   1 
ATOM 409   O O   . PRO A 1 61  ? 147.836 -7.203  15.658  1.000 24.560  ? 78  PRO AAA O   1 
ATOM 410   C CB  . PRO A 1 61  ? 146.750 -4.815  17.307  1.000 26.870  ? 78  PRO AAA CB  1 
ATOM 411   C CG  . PRO A 1 61  ? 145.251 -4.704  17.565  1.000 25.400  ? 78  PRO AAA CG  1 
ATOM 412   C CD  . PRO A 1 61  ? 144.583 -5.516  16.478  1.000 25.340  ? 78  PRO AAA CD  1 
ATOM 413   N N   . CYS A 1 62  ? 149.209 -5.454  15.186  1.000 25.590  ? 79  CYS AAA N   1 
ATOM 414   C CA  . CYS A 1 62  ? 150.460 -6.187  14.858  1.000 26.770  ? 79  CYS AAA CA  1 
ATOM 415   C C   . CYS A 1 62  ? 151.665 -5.600  15.580  1.000 25.680  ? 79  CYS AAA C   1 
ATOM 416   O O   . CYS A 1 62  ? 151.711 -4.360  15.800  1.000 25.020  ? 79  CYS AAA O   1 
ATOM 417   C CB  . CYS A 1 62  ? 150.763 -6.112  13.369  1.000 29.900  ? 79  CYS AAA CB  1 
ATOM 418   S SG  . CYS A 1 62  ? 149.452 -6.810  12.327  1.000 29.230  ? 79  CYS AAA SG  1 
ATOM 419   N N   . TYR A 1 63  ? 152.646 -6.451  15.851  1.000 25.760  ? 80  TYR AAA N   1 
ATOM 420   C CA  . TYR A 1 63  ? 153.975 -6.027  16.362  1.000 27.500  ? 80  TYR AAA CA  1 
ATOM 421   C C   . TYR A 1 63  ? 154.577 -5.024  15.376  1.000 28.220  ? 80  TYR AAA C   1 
ATOM 422   O O   . TYR A 1 63  ? 154.462 -5.206  14.131  1.000 35.730  ? 80  TYR AAA O   1 
ATOM 423   C CB  . TYR A 1 63  ? 154.919 -7.222  16.535  1.000 27.690  ? 80  TYR AAA CB  1 
ATOM 424   C CG  . TYR A 1 63  ? 154.611 -8.145  17.691  1.000 25.560  ? 80  TYR AAA CG  1 
ATOM 425   C CD1 . TYR A 1 63  ? 153.646 -9.129  17.586  1.000 26.720  ? 80  TYR AAA CD1 1 
ATOM 426   C CD2 . TYR A 1 63  ? 155.321 -8.054  18.869  1.000 24.570  ? 80  TYR AAA CD2 1 
ATOM 427   C CE1 . TYR A 1 63  ? 153.383 -9.991  18.636  1.000 28.670  ? 80  TYR AAA CE1 1 
ATOM 428   C CE2 . TYR A 1 63  ? 155.069 -8.897  19.936  1.000 26.330  ? 80  TYR AAA CE2 1 
ATOM 429   C CZ  . TYR A 1 63  ? 154.107 -9.885  19.812  1.000 27.980  ? 80  TYR AAA CZ  1 
ATOM 430   O OH  . TYR A 1 63  ? 153.832 -10.731 20.844  1.000 27.250  ? 80  TYR AAA OH  1 
ATOM 431   N N   . SER A 1 64  ? 155.168 -3.970  15.922  1.000 27.550  ? 81  SER AAA N   1 
ATOM 432   C CA  . SER A 1 64  ? 155.953 -2.955  15.184  1.000 27.660  ? 81  SER AAA CA  1 
ATOM 433   C C   . SER A 1 64  ? 157.428 -3.322  15.378  1.000 27.770  ? 81  SER AAA C   1 
ATOM 434   O O   . SER A 1 64  ? 157.792 -3.751  16.488  1.000 28.540  ? 81  SER AAA O   1 
ATOM 435   C CB  . SER A 1 64  ? 155.625 -1.546  15.662  1.000 27.770  ? 81  SER AAA CB  1 
ATOM 436   O OG  . SER A 1 64  ? 154.215 -1.374  15.872  1.000 29.060  ? 81  SER AAA OG  1 
ATOM 437   N N   . VAL A 1 65  ? 158.227 -3.207  14.321  1.000 29.200  ? 82  VAL AAA N   1 
ATOM 438   C CA  . VAL A 1 65  ? 159.695 -3.466  14.350  1.000 29.940  ? 82  VAL AAA CA  1 
ATOM 439   C C   . VAL A 1 65  ? 160.414 -2.381  13.560  1.000 30.000  ? 82  VAL AAA C   1 
ATOM 440   O O   . VAL A 1 65  ? 159.839 -1.884  12.613  1.000 28.210  ? 82  VAL AAA O   1 
ATOM 441   C CB  . VAL A 1 65  ? 160.037 -4.846  13.771  1.000 31.410  ? 82  VAL AAA CB  1 
ATOM 442   C CG1 . VAL A 1 65  ? 159.416 -5.063  12.394  1.000 31.390  ? 82  VAL AAA CG1 1 
ATOM 443   C CG2 . VAL A 1 65  ? 161.551 -5.088  13.758  1.000 32.060  ? 82  VAL AAA CG2 1 
ATOM 444   N N   . ALA A 1 66  ? 161.644 -2.077  13.944  1.000 32.510  ? 83  ALA AAA N   1 
ATOM 445   C CA  . ALA A 1 66  ? 162.493 -1.062  13.290  1.000 36.490  ? 83  ALA AAA CA  1 
ATOM 446   C C   . ALA A 1 66  ? 163.939 -1.540  13.306  1.000 40.310  ? 83  ALA AAA C   1 
ATOM 447   O O   . ALA A 1 66  ? 164.447 -1.776  14.406  1.000 43.830  ? 83  ALA AAA O   1 
ATOM 448   C CB  . ALA A 1 66  ? 162.358 0.245   14.002  1.000 35.340  ? 83  ALA AAA CB  1 
ATOM 449   N N   . ARG A 1 67  ? 164.553 -1.690  12.127  1.000 42.660  ? 84  ARG AAA N   1 
ATOM 450   C CA  . ARG A 1 67  ? 165.994 -2.013  11.979  1.000 43.560  ? 84  ARG AAA CA  1 
ATOM 451   C C   . ARG A 1 67  ? 166.746 -0.683  11.877  1.000 46.050  ? 84  ARG AAA C   1 
ATOM 452   O O   . ARG A 1 67  ? 166.410 0.087   10.997  1.000 47.730  ? 84  ARG AAA O   1 
ATOM 453   C CB  . ARG A 1 67  ? 166.201 -2.928  10.771  1.000 44.720  ? 84  ARG AAA CB  1 
ATOM 454   C CG  . ARG A 1 67  ? 167.561 -3.606  10.774  1.000 52.860  ? 84  ARG AAA CG  1 
ATOM 455   C CD  . ARG A 1 67  ? 167.790 -4.649  9.694   1.000 57.740  ? 84  ARG AAA CD  1 
ATOM 456   N NE  . ARG A 1 67  ? 167.332 -4.242  8.388   1.000 62.910  ? 84  ARG AAA NE  1 
ATOM 457   C CZ  . ARG A 1 67  ? 167.946 -3.369  7.603   1.000 78.850  ? 84  ARG AAA CZ  1 
ATOM 458   N NH1 . ARG A 1 67  ? 169.065 -2.768  7.980   1.000 80.200  ? 84  ARG AAA NH1 1 
ATOM 459   N NH2 . ARG A 1 67  ? 167.428 -3.089  6.417   1.000 97.100  ? 84  ARG AAA NH2 1 
ATOM 460   N N   . ILE A 1 68  ? 167.673 -0.388  12.787  1.000 51.150  ? 85  ILE AAA N   1 
ATOM 461   C CA  . ILE A 1 68  ? 168.434 0.900   12.797  1.000 55.620  ? 85  ILE AAA CA  1 
ATOM 462   C C   . ILE A 1 68  ? 169.869 0.606   12.375  1.000 62.420  ? 85  ILE AAA C   1 
ATOM 463   O O   . ILE A 1 68  ? 170.566 -0.130  13.071  1.000 64.870  ? 85  ILE AAA O   1 
ATOM 464   C CB  . ILE A 1 68  ? 168.404 1.596   14.178  1.000 58.670  ? 85  ILE AAA CB  1 
ATOM 465   C CG1 . ILE A 1 68  ? 167.029 1.574   14.852  1.000 62.130  ? 85  ILE AAA CG1 1 
ATOM 466   C CG2 . ILE A 1 68  ? 168.940 3.011   14.070  1.000 60.100  ? 85  ILE AAA CG2 1 
ATOM 467   C CD1 . ILE A 1 68  ? 165.917 2.230   14.076  1.000 63.930  ? 85  ILE AAA CD1 1 
ATOM 468   N N   . PRO A 1 69  ? 170.382 1.195   11.269  1.000 67.680  ? 86  PRO AAA N   1 
ATOM 469   C CA  . PRO A 1 69  ? 171.768 0.984   10.877  1.000 66.980  ? 86  PRO AAA CA  1 
ATOM 470   C C   . PRO A 1 69  ? 172.664 1.826   11.797  1.000 58.810  ? 86  PRO AAA C   1 
ATOM 471   O O   . PRO A 1 69  ? 172.351 2.987   12.025  1.000 47.780  ? 86  PRO AAA O   1 
ATOM 472   C CB  . PRO A 1 69  ? 171.814 1.512   9.433   1.000 71.020  ? 86  PRO AAA CB  1 
ATOM 473   C CG  . PRO A 1 69  ? 170.382 1.839   9.060   1.000 65.820  ? 86  PRO AAA CG  1 
ATOM 474   C CD  . PRO A 1 69  ? 169.700 2.135   10.366  1.000 65.840  ? 86  PRO AAA CD  1 
ATOM 475   N N   . LEU A 1 70  ? 173.729 1.217   12.315  1.000 54.740  ? 87  LEU AAA N   1 
ATOM 476   C CA  . LEU A 1 70  ? 174.703 1.882   13.214  1.000 57.240  ? 87  LEU AAA CA  1 
ATOM 477   C C   . LEU A 1 70  ? 175.971 2.224   12.437  1.000 60.200  ? 87  LEU AAA C   1 
ATOM 478   O O   . LEU A 1 70  ? 176.205 1.694   11.357  1.000 67.270  ? 87  LEU AAA O   1 
ATOM 479   C CB  . LEU A 1 70  ? 175.007 0.920   14.365  1.000 56.180  ? 87  LEU AAA CB  1 
ATOM 480   C CG  . LEU A 1 70  ? 173.784 0.448   15.145  1.000 51.760  ? 87  LEU AAA CG  1 
ATOM 481   C CD1 . LEU A 1 70  ? 174.154 -0.612  16.161  1.000 51.250  ? 87  LEU AAA CD1 1 
ATOM 482   C CD2 . LEU A 1 70  ? 173.118 1.605   15.844  1.000 49.960  ? 87  LEU AAA CD2 1 
ATOM 483   N N   . PRO A 1 71  ? 176.826 3.129   12.955  1.000 57.450  ? 88  PRO AAA N   1 
ATOM 484   C CA  . PRO A 1 71  ? 178.130 3.398   12.355  1.000 57.070  ? 88  PRO AAA CA  1 
ATOM 485   C C   . PRO A 1 71  ? 178.953 2.148   12.016  1.000 55.000  ? 88  PRO AAA C   1 
ATOM 486   O O   . PRO A 1 71  ? 179.074 1.291   12.839  1.000 47.600  ? 88  PRO AAA O   1 
ATOM 487   C CB  . PRO A 1 71  ? 178.839 4.198   13.441  1.000 58.130  ? 88  PRO AAA CB  1 
ATOM 488   C CG  . PRO A 1 71  ? 177.723 4.951   14.108  1.000 60.490  ? 88  PRO AAA CG  1 
ATOM 489   C CD  . PRO A 1 71  ? 176.558 3.985   14.111  1.000 59.220  ? 88  PRO AAA CD  1 
ATOM 490   N N   . ASN A 1 72  ? 179.519 2.132   10.815  1.000 61.210  ? 89  ASN AAA N   1 
ATOM 491   C CA  . ASN A 1 72  ? 180.334 1.031   10.253  1.000 67.430  ? 89  ASN AAA CA  1 
ATOM 492   C C   . ASN A 1 72  ? 181.593 0.770   11.096  1.000 72.500  ? 89  ASN AAA C   1 
ATOM 493   O O   . ASN A 1 72  ? 182.176 1.750   11.564  1.000 75.540  ? 89  ASN AAA O   1 
ATOM 494   C CB  . ASN A 1 72  ? 180.730 1.348   8.816   1.000 64.720  ? 89  ASN AAA CB  1 
ATOM 495   C CG  . ASN A 1 72  ? 181.116 0.107   8.055   1.000 68.060  ? 89  ASN AAA CG  1 
ATOM 496   O OD1 . ASN A 1 72  ? 181.476 -0.924  8.629   1.000 74.930  ? 89  ASN AAA OD1 1 
ATOM 497   N ND2 . ASN A 1 72  ? 181.000 0.207   6.747   1.000 72.240  ? 89  ASN AAA ND2 1 
ATOM 498   N N   . LEU A 1 73  ? 182.000 -0.499  11.230  1.000 71.640  ? 90  LEU AAA N   1 
ATOM 499   C CA  . LEU A 1 73  ? 183.198 -0.970  11.987  1.000 64.680  ? 90  LEU AAA CA  1 
ATOM 500   C C   . LEU A 1 73  ? 183.967 -2.083  11.200  1.000 68.520  ? 90  LEU AAA C   1 
ATOM 501   O O   . LEU A 1 73  ? 184.431 -3.090  11.838  1.000 57.050  ? 90  LEU AAA O   1 
ATOM 502   C CB  . LEU A 1 73  ? 182.731 -1.507  13.352  1.000 64.100  ? 90  LEU AAA CB  1 
ATOM 503   C CG  . LEU A 1 73  ? 181.746 -0.656  14.153  1.000 59.780  ? 90  LEU AAA CG  1 
ATOM 504   C CD1 . LEU A 1 73  ? 181.199 -1.421  15.350  1.000 60.120  ? 90  LEU AAA CD1 1 
ATOM 505   C CD2 . LEU A 1 73  ? 182.390 0.631   14.635  1.000 62.640  ? 90  LEU AAA CD2 1 
ATOM 506   N N   . ASN A 1 74  ? 184.154 -1.990  9.862   1.000 78.000  ? 91  ASN AAA N   1 
ATOM 507   C CA  . ASN A 1 74  ? 184.860 -3.016  9.021   1.000 69.390  ? 91  ASN AAA CA  1 
ATOM 508   C C   . ASN A 1 74  ? 186.365 -2.874  9.232   1.000 63.930  ? 91  ASN AAA C   1 
ATOM 509   O O   . ASN A 1 74  ? 186.884 -1.909  8.663   1.000 61.980  ? 91  ASN AAA O   1 
ATOM 510   C CB  . ASN A 1 74  ? 184.548 -2.939  7.522   1.000 55.590  ? 91  ASN AAA CB  1 
ATOM 511   N N   . ASN A 1 81  ? 188.103 -11.722 14.807  1.000 63.490  ? 98  ASN AAA N   1 
ATOM 512   C CA  . ASN A 1 81  ? 188.580 -10.812 15.884  1.000 66.230  ? 98  ASN AAA CA  1 
ATOM 513   C C   . ASN A 1 81  ? 188.225 -9.352  15.517  1.000 66.590  ? 98  ASN AAA C   1 
ATOM 514   O O   . ASN A 1 81  ? 189.146 -8.518  15.420  1.000 66.890  ? 98  ASN AAA O   1 
ATOM 515   C CB  . ASN A 1 81  ? 190.065 -11.032 16.160  1.000 58.830  ? 98  ASN AAA CB  1 
ATOM 516   N N   . ILE A 1 82  ? 186.916 -9.058  15.392  1.000 67.620  ? 99  ILE AAA N   1 
ATOM 517   C CA  . ILE A 1 82  ? 186.303 -7.764  14.942  1.000 68.850  ? 99  ILE AAA CA  1 
ATOM 518   C C   . ILE A 1 82  ? 185.573 -7.035  16.100  1.000 65.100  ? 99  ILE AAA C   1 
ATOM 519   O O   . ILE A 1 82  ? 185.533 -7.551  17.236  1.000 69.900  ? 99  ILE AAA O   1 
ATOM 520   C CB  . ILE A 1 82  ? 185.348 -8.032  13.753  1.000 65.960  ? 99  ILE AAA CB  1 
ATOM 521   C CG1 . ILE A 1 82  ? 184.723 -6.761  13.146  1.000 74.090  ? 99  ILE AAA CG1 1 
ATOM 522   C CG2 . ILE A 1 82  ? 184.250 -9.011  14.149  1.000 56.570  ? 99  ILE AAA CG2 1 
ATOM 523   C CD1 . ILE A 1 82  ? 185.683 -5.643  12.752  1.000 71.320  ? 99  ILE AAA CD1 1 
ATOM 524   N N   . LEU A 1 83  ? 184.983 -5.867  15.815  1.000 55.490  ? 100 LEU AAA N   1 
ATOM 525   C CA  . LEU A 1 83  ? 184.156 -5.061  16.751  1.000 55.900  ? 100 LEU AAA CA  1 
ATOM 526   C C   . LEU A 1 83  ? 182.668 -5.172  16.404  1.000 58.680  ? 100 LEU AAA C   1 
ATOM 527   O O   . LEU A 1 83  ? 182.348 -5.138  15.201  1.000 62.950  ? 100 LEU AAA O   1 
ATOM 528   C CB  . LEU A 1 83  ? 184.576 -3.595  16.649  1.000 52.640  ? 100 LEU AAA CB  1 
ATOM 529   C CG  . LEU A 1 83  ? 185.965 -3.271  17.153  1.000 51.020  ? 100 LEU AAA CG  1 
ATOM 530   C CD1 . LEU A 1 83  ? 186.133 -1.764  17.285  1.000 51.060  ? 100 LEU AAA CD1 1 
ATOM 531   C CD2 . LEU A 1 83  ? 186.238 -3.972  18.481  1.000 51.860  ? 100 LEU AAA CD2 1 
ATOM 532   N N   . MET A 1 84  ? 181.796 -5.242  17.426  1.000 60.340  ? 101 MET AAA N   1 
ATOM 533   C CA  . MET A 1 84  ? 180.312 -5.147  17.304  1.000 57.760  ? 101 MET AAA CA  1 
ATOM 534   C C   . MET A 1 84  ? 179.790 -4.098  18.300  1.000 59.370  ? 101 MET AAA C   1 
ATOM 535   O O   . MET A 1 84  ? 180.400 -3.925  19.396  1.000 55.570  ? 101 MET AAA O   1 
ATOM 536   C CB  . MET A 1 84  ? 179.617 -6.475  17.610  1.000 52.940  ? 101 MET AAA CB  1 
ATOM 537   C CG  . MET A 1 84  ? 180.133 -7.632  16.811  1.000 54.640  ? 101 MET AAA CG  1 
ATOM 538   S SD  . MET A 1 84  ? 179.199 -9.144  17.196  1.000 61.170  ? 101 MET AAA SD  1 
ATOM 539   C CE  . MET A 1 84  ? 177.701 -8.828  16.284  1.000 59.580  ? 101 MET AAA CE  1 
ATOM 540   N N   . TRP A 1 85  ? 178.672 -3.459  17.961  1.000 50.860  ? 102 TRP AAA N   1 
ATOM 541   C CA  . TRP A 1 85  ? 177.966 -2.532  18.874  1.000 47.870  ? 102 TRP AAA CA  1 
ATOM 542   C C   . TRP A 1 85  ? 177.203 -3.315  19.955  1.000 48.980  ? 102 TRP AAA C   1 
ATOM 543   O O   . TRP A 1 85  ? 176.394 -4.203  19.614  1.000 49.570  ? 102 TRP AAA O   1 
ATOM 544   C CB  . TRP A 1 85  ? 177.040 -1.629  18.076  1.000 48.540  ? 102 TRP AAA CB  1 
ATOM 545   C CG  . TRP A 1 85  ? 177.725 -0.549  17.299  1.000 46.210  ? 102 TRP AAA CG  1 
ATOM 546   C CD1 . TRP A 1 85  ? 177.730 -0.379  15.949  1.000 47.880  ? 102 TRP AAA CD1 1 
ATOM 547   C CD2 . TRP A 1 85  ? 178.455 0.562   17.834  1.000 45.880  ? 102 TRP AAA CD2 1 
ATOM 548   N NE1 . TRP A 1 85  ? 178.419 0.747   15.612  1.000 46.070  ? 102 TRP AAA NE1 1 
ATOM 549   C CE2 . TRP A 1 85  ? 178.879 1.346   16.746  1.000 45.920  ? 102 TRP AAA CE2 1 
ATOM 550   C CE3 . TRP A 1 85  ? 178.799 0.967   19.126  1.000 52.550  ? 102 TRP AAA CE3 1 
ATOM 551   C CZ2 . TRP A 1 85  ? 179.627 2.504   16.910  1.000 48.260  ? 102 TRP AAA CZ2 1 
ATOM 552   C CZ3 . TRP A 1 85  ? 179.522 2.124   19.287  1.000 51.430  ? 102 TRP AAA CZ3 1 
ATOM 553   C CH2 . TRP A 1 85  ? 179.925 2.881   18.190  1.000 49.400  ? 102 TRP AAA CH2 1 
ATOM 554   N N   . GLU A 1 86  ? 177.463 -2.973  21.216  1.000 50.110  ? 103 GLU AAA N   1 
ATOM 555   C CA  . GLU A 1 86  ? 176.804 -3.524  22.432  1.000 50.240  ? 103 GLU AAA CA  1 
ATOM 556   C C   . GLU A 1 86  ? 175.771 -2.503  22.936  1.000 50.390  ? 103 GLU AAA C   1 
ATOM 557   O O   . GLU A 1 86  ? 176.165 -1.388  23.311  1.000 47.260  ? 103 GLU AAA O   1 
ATOM 558   C CB  . GLU A 1 86  ? 177.856 -3.813  23.507  1.000 46.490  ? 103 GLU AAA CB  1 
ATOM 559   C CG  . GLU A 1 86  ? 177.376 -4.723  24.626  1.000 44.920  ? 103 GLU AAA CG  1 
ATOM 560   C CD  . GLU A 1 86  ? 178.334 -4.866  25.797  1.000 46.710  ? 103 GLU AAA CD  1 
ATOM 561   O OE1 . GLU A 1 86  ? 179.277 -4.045  25.889  1.000 49.850  ? 103 GLU AAA OE1 1 
ATOM 562   O OE2 . GLU A 1 86  ? 178.145 -5.791  26.636  1.000 46.960  ? 103 GLU AAA OE2 1 
ATOM 563   N N   . ALA A 1 87  ? 174.489 -2.863  22.921  1.000 50.200  ? 104 ALA AAA N   1 
ATOM 564   C CA  . ALA A 1 87  ? 173.393 -2.059  23.502  1.000 45.950  ? 104 ALA AAA CA  1 
ATOM 565   C C   . ALA A 1 87  ? 173.465 -2.177  25.026  1.000 40.800  ? 104 ALA AAA C   1 
ATOM 566   O O   . ALA A 1 87  ? 173.372 -3.294  25.540  1.000 35.390  ? 104 ALA AAA O   1 
ATOM 567   C CB  . ALA A 1 87  ? 172.065 -2.519  22.952  1.000 47.480  ? 104 ALA AAA CB  1 
ATOM 568   N N   . VAL A 1 88  ? 173.629 -1.048  25.707  1.000 40.480  ? 105 VAL AAA N   1 
ATOM 569   C CA  . VAL A 1 88  ? 173.958 -1.011  27.159  1.000 41.920  ? 105 VAL AAA CA  1 
ATOM 570   C C   . VAL A 1 88  ? 172.757 -0.531  27.977  1.000 39.170  ? 105 VAL AAA C   1 
ATOM 571   O O   . VAL A 1 88  ? 172.447 -1.171  28.999  1.000 41.040  ? 105 VAL AAA O   1 
ATOM 572   C CB  . VAL A 1 88  ? 175.208 -0.147  27.377  1.000 44.250  ? 105 VAL AAA CB  1 
ATOM 573   C CG1 . VAL A 1 88  ? 175.539 0.014   28.853  1.000 45.310  ? 105 VAL AAA CG1 1 
ATOM 574   C CG2 . VAL A 1 88  ? 176.378 -0.732  26.600  1.000 43.450  ? 105 VAL AAA CG2 1 
ATOM 575   N N   . THR A 1 89  ? 172.106 0.555   27.582  1.000 38.080  ? 106 THR AAA N   1 
ATOM 576   C CA  . THR A 1 89  ? 170.938 1.121   28.323  1.000 40.970  ? 106 THR AAA CA  1 
ATOM 577   C C   . THR A 1 89  ? 169.810 1.469   27.366  1.000 40.350  ? 106 THR AAA C   1 
ATOM 578   O O   . THR A 1 89  ? 170.074 1.756   26.193  1.000 41.920  ? 106 THR AAA O   1 
ATOM 579   C CB  . THR A 1 89  ? 171.327 2.377   29.105  1.000 45.470  ? 106 THR AAA CB  1 
ATOM 580   O OG1 . THR A 1 89  ? 171.213 3.520   28.250  1.000 50.640  ? 106 THR AAA OG1 1 
ATOM 581   C CG2 . THR A 1 89  ? 172.730 2.313   29.667  1.000 46.800  ? 106 THR AAA CG2 1 
ATOM 582   N N   . LEU A 1 90  ? 168.589 1.444   27.879  1.000 40.300  ? 107 LEU AAA N   1 
ATOM 583   C CA  . LEU A 1 90  ? 167.366 1.841   27.151  1.000 39.820  ? 107 LEU AAA CA  1 
ATOM 584   C C   . LEU A 1 90  ? 166.626 2.855   28.012  1.000 37.190  ? 107 LEU AAA C   1 
ATOM 585   O O   . LEU A 1 90  ? 166.600 2.690   29.241  1.000 35.040  ? 107 LEU AAA O   1 
ATOM 586   C CB  . LEU A 1 90  ? 166.489 0.612   26.911  1.000 41.870  ? 107 LEU AAA CB  1 
ATOM 587   C CG  . LEU A 1 90  ? 165.066 0.925   26.462  1.000 42.040  ? 107 LEU AAA CG  1 
ATOM 588   C CD1 . LEU A 1 90  ? 165.089 1.525   25.062  1.000 41.770  ? 107 LEU AAA CD1 1 
ATOM 589   C CD2 . LEU A 1 90  ? 164.189 -0.321  26.518  1.000 41.910  ? 107 LEU AAA CD2 1 
ATOM 590   N N   . LYS A 1 91  ? 166.068 3.876   27.379  1.000 37.220  ? 108 LYS AAA N   1 
ATOM 591   C CA  . LYS A 1 91  ? 164.979 4.717   27.925  1.000 35.820  ? 108 LYS AAA CA  1 
ATOM 592   C C   . LYS A 1 91  ? 163.829 4.583   26.943  1.000 36.190  ? 108 LYS AAA C   1 
ATOM 593   O O   . LYS A 1 91  ? 164.073 4.661   25.730  1.000 41.760  ? 108 LYS AAA O   1 
ATOM 594   C CB  . LYS A 1 91  ? 165.391 6.183   28.019  1.000 34.430  ? 108 LYS AAA CB  1 
ATOM 595   C CG  . LYS A 1 91  ? 166.335 6.509   29.155  1.000 38.170  ? 108 LYS AAA CG  1 
ATOM 596   C CD  . LYS A 1 91  ? 167.112 7.789   29.017  1.000 43.870  ? 108 LYS AAA CD  1 
ATOM 597   C CE  . LYS A 1 91  ? 166.573 8.903   29.888  1.000 44.890  ? 108 LYS AAA CE  1 
ATOM 598   N NZ  . LYS A 1 91  ? 167.488 10.063  29.859  1.000 45.630  ? 108 LYS AAA NZ  1 
ATOM 599   N N   . THR A 1 92  ? 162.620 4.369   27.433  1.000 31.670  ? 109 THR AAA N   1 
ATOM 600   C CA  . THR A 1 92  ? 161.425 4.288   26.569  1.000 28.530  ? 109 THR AAA CA  1 
ATOM 601   C C   . THR A 1 92  ? 160.260 4.898   27.324  1.000 27.170  ? 109 THR AAA C   1 
ATOM 602   O O   . THR A 1 92  ? 160.317 4.900   28.531  1.000 27.320  ? 109 THR AAA O   1 
ATOM 603   C CB  . THR A 1 92  ? 161.187 2.840   26.120  1.000 27.920  ? 109 THR AAA CB  1 
ATOM 604   O OG1 . THR A 1 92  ? 160.040 2.863   25.272  1.000 26.720  ? 109 THR AAA OG1 1 
ATOM 605   C CG2 . THR A 1 92  ? 160.986 1.866   27.265  1.000 27.250  ? 109 THR AAA CG2 1 
ATOM 606   N N   . GLU A 1 93  ? 159.278 5.437   26.624  1.000 29.270  ? 110 GLU AAA N   1 
ATOM 607   C CA  . GLU A 1 93  ? 157.960 5.776   27.214  1.000 34.770  ? 110 GLU AAA CA  1 
ATOM 608   C C   . GLU A 1 93  ? 156.948 5.844   26.070  1.000 35.160  ? 110 GLU AAA C   1 
ATOM 609   O O   . GLU A 1 93  ? 157.372 5.897   24.908  1.000 35.470  ? 110 GLU AAA O   1 
ATOM 610   C CB  . GLU A 1 93  ? 158.025 7.067   28.054  1.000 40.970  ? 110 GLU AAA CB  1 
ATOM 611   C CG  . GLU A 1 93  ? 157.863 8.369   27.277  1.000 41.900  ? 110 GLU AAA CG  1 
ATOM 612   C CD  . GLU A 1 93  ? 158.221 9.627   28.041  1.000 43.080  ? 110 GLU AAA CD  1 
ATOM 613   O OE1 . GLU A 1 93  ? 159.112 9.539   28.902  1.000 39.540  ? 110 GLU AAA OE1 1 
ATOM 614   O OE2 . GLU A 1 93  ? 157.605 10.708  27.758  1.000 52.700  ? 110 GLU AAA OE2 1 
ATOM 615   N N   . VAL A 1 94  ? 155.663 5.812   26.399  1.000 34.620  ? 111 VAL AAA N   1 
ATOM 616   C CA  . VAL A 1 94  ? 154.584 5.951   25.394  1.000 34.510  ? 111 VAL AAA CA  1 
ATOM 617   C C   . VAL A 1 94  ? 154.419 7.433   25.068  1.000 35.860  ? 111 VAL AAA C   1 
ATOM 618   O O   . VAL A 1 94  ? 154.306 8.263   26.004  1.000 38.250  ? 111 VAL AAA O   1 
ATOM 619   C CB  . VAL A 1 94  ? 153.289 5.308   25.898  1.000 33.060  ? 111 VAL AAA CB  1 
ATOM 620   C CG1 . VAL A 1 94  ? 152.120 5.583   24.964  1.000 33.550  ? 111 VAL AAA CG1 1 
ATOM 621   C CG2 . VAL A 1 94  ? 153.496 3.822   26.103  1.000 32.510  ? 111 VAL AAA CG2 1 
ATOM 622   N N   . ILE A 1 95  ? 154.379 7.753   23.775  1.000 36.880  ? 112 ILE AAA N   1 
ATOM 623   C CA  . ILE A 1 95  ? 154.224 9.157   23.304  1.000 36.540  ? 112 ILE AAA CA  1 
ATOM 624   C C   . ILE A 1 95  ? 152.752 9.463   23.011  1.000 32.700  ? 112 ILE AAA C   1 
ATOM 625   O O   . ILE A 1 95  ? 152.152 8.818   22.116  1.000 32.690  ? 112 ILE AAA O   1 
ATOM 626   C CB  . ILE A 1 95  ? 155.108 9.431   22.086  1.000 36.430  ? 112 ILE AAA CB  1 
ATOM 627   C CG1 . ILE A 1 95  ? 156.546 8.988   22.322  1.000 40.620  ? 112 ILE AAA CG1 1 
ATOM 628   C CG2 . ILE A 1 95  ? 155.033 10.902  21.725  1.000 36.730  ? 112 ILE AAA CG2 1 
ATOM 629   C CD1 . ILE A 1 95  ? 157.358 8.909   21.035  1.000 46.600  ? 112 ILE AAA CD1 1 
ATOM 630   N N   . GLY A 1 96  ? 152.211 10.438  23.733  1.000 29.560  ? 113 GLY AAA N   1 
ATOM 631   C CA  . GLY A 1 96  ? 150.870 10.979  23.470  1.000 30.050  ? 113 GLY AAA CA  1 
ATOM 632   C C   . GLY A 1 96  ? 149.827 10.363  24.383  1.000 28.900  ? 113 GLY AAA C   1 
ATOM 633   O O   . GLY A 1 96  ? 148.706 10.122  23.906  1.000 27.970  ? 113 GLY AAA O   1 
ATOM 634   N N   . VAL A 1 97  ? 150.180 10.142  25.654  1.000 26.710  ? 114 VAL AAA N   1 
ATOM 635   C CA  . VAL A 1 97  ? 149.293 9.506   26.668  1.000 25.180  ? 114 VAL AAA CA  1 
ATOM 636   C C   . VAL A 1 97  ? 148.070 10.396  26.875  1.000 24.430  ? 114 VAL AAA C   1 
ATOM 637   O O   . VAL A 1 97  ? 146.987 9.871   27.006  1.000 23.990  ? 114 VAL AAA O   1 
ATOM 638   C CB  . VAL A 1 97  ? 150.031 9.222   27.991  1.000 27.180  ? 114 VAL AAA CB  1 
ATOM 639   C CG1 . VAL A 1 97  ? 151.244 8.342   27.790  1.000 25.360  ? 114 VAL AAA CG1 1 
ATOM 640   C CG2 . VAL A 1 97  ? 150.433 10.494  28.731  1.000 29.500  ? 114 VAL AAA CG2 1 
ATOM 641   N N   . THR A 1 98  ? 148.253 11.711  26.898  1.000 25.960  ? 115 THR AAA N   1 
ATOM 642   C CA  . THR A 1 98  ? 147.193 12.713  27.195  1.000 28.700  ? 115 THR AAA CA  1 
ATOM 643   C C   . THR A 1 98  ? 146.080 12.639  26.150  1.000 30.380  ? 115 THR AAA C   1 
ATOM 644   O O   . THR A 1 98  ? 144.954 13.045  26.467  1.000 30.930  ? 115 THR AAA O   1 
ATOM 645   C CB  . THR A 1 98  ? 147.748 14.136  27.215  1.000 31.810  ? 115 THR AAA CB  1 
ATOM 646   O OG1 . THR A 1 98  ? 148.346 14.378  25.936  1.000 39.700  ? 115 THR AAA OG1 1 
ATOM 647   C CG2 . THR A 1 98  ? 148.754 14.365  28.322  1.000 32.960  ? 115 THR AAA CG2 1 
ATOM 648   N N   . SER A 1 99  ? 146.381 12.157  24.942  1.000 31.890  ? 116 SER AAA N   1 
ATOM 649   C CA  . SER A 1 99  ? 145.401 12.062  23.826  1.000 29.650  ? 116 SER AAA CA  1 
ATOM 650   C C   . SER A 1 99  ? 144.230 11.192  24.248  1.000 25.610  ? 116 SER AAA C   1 
ATOM 651   O O   . SER A 1 99  ? 143.196 11.273  23.592  1.000 22.930  ? 116 SER AAA O   1 
ATOM 652   C CB  . SER A 1 99  ? 146.011 11.496  22.594  1.000 31.970  ? 116 SER AAA CB  1 
ATOM 653   O OG  . SER A 1 99  ? 146.302 10.128  22.786  1.000 33.490  ? 116 SER AAA OG  1 
ATOM 654   N N   . LEU A 1 100 ? 144.427 10.375  25.282  1.000 25.160  ? 117 LEU AAA N   1 
ATOM 655   C CA  . LEU A 1 100 ? 143.437 9.387   25.766  1.000 26.810  ? 117 LEU AAA CA  1 
ATOM 656   C C   . LEU A 1 100 ? 142.401 10.080  26.639  1.000 27.120  ? 117 LEU AAA C   1 
ATOM 657   O O   . LEU A 1 100 ? 141.367 9.424   26.914  1.000 33.320  ? 117 LEU AAA O   1 
ATOM 658   C CB  . LEU A 1 100 ? 144.161 8.254   26.502  1.000 28.020  ? 117 LEU AAA CB  1 
ATOM 659   C CG  . LEU A 1 100 ? 145.037 7.388   25.591  1.000 28.180  ? 117 LEU AAA CG  1 
ATOM 660   C CD1 . LEU A 1 100 ? 145.631 6.213   26.350  1.000 29.160  ? 117 LEU AAA CD1 1 
ATOM 661   C CD2 . LEU A 1 100 ? 144.234 6.903   24.386  1.000 27.300  ? 117 LEU AAA CD2 1 
ATOM 662   N N   . MET A 1 101 ? 142.615 11.353  26.963  1.000 25.670  ? 118 MET AAA N   1 
ATOM 663   C CA  . MET A 1 101 ? 141.624 12.188  27.686  1.000 26.410  ? 118 MET AAA CA  1 
ATOM 664   C C   . MET A 1 101 ? 140.613 12.800  26.711  1.000 26.030  ? 118 MET AAA C   1 
ATOM 665   O O   . MET A 1 101 ? 139.785 13.606  27.174  1.000 26.940  ? 118 MET AAA O   1 
ATOM 666   C CB  . MET A 1 101 ? 142.321 13.333  28.420  1.000 27.880  ? 118 MET AAA CB  1 
ATOM 667   C CG  . MET A 1 101 ? 143.409 12.870  29.327  1.000 29.150  ? 118 MET AAA CG  1 
ATOM 668   S SD  . MET A 1 101 ? 144.133 14.234  30.228  1.000 30.710  ? 118 MET AAA SD  1 
ATOM 669   C CE  . MET A 1 101 ? 142.826 14.546  31.425  1.000 32.190  ? 118 MET AAA CE  1 
ATOM 670   N N   . ASN A 1 102 ? 140.683 12.520  25.409  1.000 27.180  ? 119 ASN AAA N   1 
ATOM 671   C CA  . ASN A 1 102 ? 139.685 13.059  24.444  1.000 28.730  ? 119 ASN AAA CA  1 
ATOM 672   C C   . ASN A 1 102 ? 138.389 12.278  24.603  1.000 27.110  ? 119 ASN AAA C   1 
ATOM 673   O O   . ASN A 1 102 ? 138.160 11.329  23.838  1.000 28.030  ? 119 ASN AAA O   1 
ATOM 674   C CB  . ASN A 1 102 ? 140.107 13.063  22.974  1.000 31.180  ? 119 ASN AAA CB  1 
ATOM 675   C CG  . ASN A 1 102 ? 139.051 13.722  22.098  1.000 33.360  ? 119 ASN AAA CG  1 
ATOM 676   O OD1 . ASN A 1 102 ? 137.878 13.802  22.477  1.000 31.140  ? 119 ASN AAA OD1 1 
ATOM 677   N ND2 . ASN A 1 102 ? 139.451 14.206  20.924  1.000 38.290  ? 119 ASN AAA ND2 1 
ATOM 678   N N   . VAL A 1 103 ? 137.529 12.767  25.483  1.000 27.230  ? 120 VAL AAA N   1 
ATOM 679   C CA  . VAL A 1 103 ? 136.276 12.099  25.902  1.000 29.380  ? 120 VAL AAA CA  1 
ATOM 680   C C   . VAL A 1 103 ? 135.054 12.787  25.252  1.000 28.620  ? 120 VAL AAA C   1 
ATOM 681   O O   . VAL A 1 103 ? 133.943 12.559  25.711  1.000 28.100  ? 120 VAL AAA O   1 
ATOM 682   C CB  . VAL A 1 103 ? 136.281 12.056  27.440  1.000 28.770  ? 120 VAL AAA CB  1 
ATOM 683   C CG1 . VAL A 1 103 ? 136.598 13.379  28.090  1.000 25.940  ? 120 VAL AAA CG1 1 
ATOM 684   C CG2 . VAL A 1 103 ? 135.025 11.488  27.995  1.000 34.500  ? 120 VAL AAA CG2 1 
ATOM 685   N N   . HIS A 1 104 ? 135.247 13.511  24.147  1.000 29.560  ? 121 HIS AAA N   1 
ATOM 686   C CA  . HIS A 1 104 ? 134.206 14.359  23.492  1.000 29.070  ? 121 HIS AAA CA  1 
ATOM 687   C C   . HIS A 1 104 ? 134.020 14.067  21.990  1.000 27.950  ? 121 HIS AAA C   1 
ATOM 688   O O   . HIS A 1 104 ? 133.154 14.726  21.380  1.000 25.400  ? 121 HIS AAA O   1 
ATOM 689   C CB  . HIS A 1 104 ? 134.537 15.848  23.690  1.000 29.290  ? 121 HIS AAA CB  1 
ATOM 690   C CG  . HIS A 1 104 ? 135.972 16.191  23.465  1.000 30.270  ? 121 HIS AAA CG  1 
ATOM 691   N ND1 . HIS A 1 104 ? 136.440 16.560  22.243  1.000 31.250  ? 121 HIS AAA ND1 1 
ATOM 692   C CD2 . HIS A 1 104 ? 137.037 16.230  24.308  1.000 29.860  ? 121 HIS AAA CD2 1 
ATOM 693   C CE1 . HIS A 1 104 ? 137.739 16.818  22.347  1.000 32.040  ? 121 HIS AAA CE1 1 
ATOM 694   N NE2 . HIS A 1 104 ? 138.131 16.614  23.605  1.000 27.170  ? 121 HIS AAA NE2 1 
ATOM 695   N N   . SER A 1 105 ? 134.777 13.144  21.393  1.000 29.240  ? 122 SER AAA N   1 
ATOM 696   C CA  . SER A 1 105 ? 134.845 12.938  19.914  1.000 28.840  ? 122 SER AAA CA  1 
ATOM 697   C C   . SER A 1 105 ? 133.941 11.776  19.499  1.000 26.520  ? 122 SER AAA C   1 
ATOM 698   O O   . SER A 1 105 ? 134.488 10.670  19.198  1.000 24.370  ? 122 SER AAA O   1 
ATOM 699   C CB  . SER A 1 105 ? 136.276 12.717  19.458  1.000 31.160  ? 122 SER AAA CB  1 
ATOM 700   O OG  . SER A 1 105 ? 136.351 12.514  18.050  1.000 32.530  ? 122 SER AAA OG  1 
ATOM 701   N N   . ASN A 1 106 ? 132.623 12.000  19.524  1.000 26.060  ? 123 ASN AAA N   1 
ATOM 702   C CA  . ASN A 1 106 ? 131.606 10.994  19.136  1.000 28.480  ? 123 ASN AAA CA  1 
ATOM 703   C C   . ASN A 1 106 ? 131.792 9.696   19.934  1.000 29.830  ? 123 ASN AAA C   1 
ATOM 704   O O   . ASN A 1 106 ? 131.686 8.619   19.337  1.000 25.390  ? 123 ASN AAA O   1 
ATOM 705   C CB  . ASN A 1 106 ? 131.712 10.691  17.648  1.000 33.010  ? 123 ASN AAA CB  1 
ATOM 706   C CG  . ASN A 1 106 ? 130.417 10.221  17.051  1.000 37.190  ? 123 ASN AAA CG  1 
ATOM 707   O OD1 . ASN A 1 106 ? 129.429 10.929  17.122  1.000 39.260  ? 123 ASN AAA OD1 1 
ATOM 708   N ND2 . ASN A 1 106 ? 130.409 9.039   16.456  1.000 44.140  ? 123 ASN AAA ND2 1 
ATOM 709   N N   . GLY A 1 107 ? 132.094 9.792   21.233  1.000 33.420  ? 124 GLY AAA N   1 
ATOM 710   C CA  . GLY A 1 107 ? 132.209 8.614   22.121  1.000 32.330  ? 124 GLY AAA CA  1 
ATOM 711   C C   . GLY A 1 107 ? 130.918 8.003   22.611  1.000 30.510  ? 124 GLY AAA C   1 
ATOM 712   O O   . GLY A 1 107 ? 129.864 8.455   22.163  1.000 27.890  ? 124 GLY AAA O   1 
ATOM 713   N N   . GLN A 1 108 ? 130.980 7.172   23.650  1.000 31.660  ? 125 GLN AAA N   1 
ATOM 714   C CA  . GLN A 1 108 ? 129.733 6.652   24.255  1.000 33.460  ? 125 GLN AAA CA  1 
ATOM 715   C C   . GLN A 1 108 ? 129.514 7.252   25.644  1.000 33.870  ? 125 GLN AAA C   1 
ATOM 716   O O   . GLN A 1 108 ? 130.220 6.829   26.559  1.000 29.650  ? 125 GLN AAA O   1 
ATOM 717   C CB  . GLN A 1 108 ? 129.731 5.130   24.324  1.000 30.980  ? 125 GLN AAA CB  1 
ATOM 718   C CG  . GLN A 1 108 ? 128.361 4.530   24.589  1.000 29.000  ? 125 GLN AAA CG  1 
ATOM 719   C CD  . GLN A 1 108 ? 128.458 3.150   25.185  1.000 25.610  ? 125 GLN AAA CD  1 
ATOM 720   O OE1 . GLN A 1 108 ? 127.801 2.218   24.737  1.000 23.420  ? 125 GLN AAA OE1 1 
ATOM 721   N NE2 . GLN A 1 108 ? 129.281 3.009   26.209  1.000 22.360  ? 125 GLN AAA NE2 1 
ATOM 722   N N   . ALA A 1 109 ? 128.593 8.204   25.785  1.000 36.480  ? 126 ALA AAA N   1 
ATOM 723   C CA  . ALA A 1 109 ? 128.174 8.815   27.069  1.000 39.120  ? 126 ALA AAA CA  1 
ATOM 724   C C   . ALA A 1 109 ? 128.082 7.618   28.019  1.000 38.990  ? 126 ALA AAA C   1 
ATOM 725   O O   . ALA A 1 109 ? 127.322 6.698   27.709  1.000 42.230  ? 126 ALA AAA O   1 
ATOM 726   C CB  . ALA A 1 109 ? 126.889 9.591   27.057  1.000 37.940  ? 126 ALA AAA CB  1 
ATOM 727   N N   . THR A 1 110 ? 128.824 7.640   29.114  1.000 37.280  ? 127 THR AAA N   1 
ATOM 728   C CA  . THR A 1 110 ? 128.746 6.667   30.225  1.000 35.400  ? 127 THR AAA CA  1 
ATOM 729   C C   . THR A 1 110 ? 127.336 6.674   30.835  1.000 33.540  ? 127 THR AAA C   1 
ATOM 730   O O   . THR A 1 110 ? 126.948 5.649   31.375  1.000 38.290  ? 127 THR AAA O   1 
ATOM 731   C CB  . THR A 1 110 ? 129.828 6.969   31.273  1.000 38.320  ? 127 THR AAA CB  1 
ATOM 732   O OG1 . THR A 1 110 ? 129.832 8.359   31.612  1.000 36.710  ? 127 THR AAA OG1 1 
ATOM 733   C CG2 . THR A 1 110 ? 131.217 6.587   30.807  1.000 40.010  ? 127 THR AAA CG2 1 
ATOM 734   N N   . HIS A 1 111 ? 126.587 7.773   30.743  1.000 30.860  ? 128 HIS AAA N   1 
ATOM 735   C CA  . HIS A 1 111 ? 125.224 7.919   31.324  1.000 29.340  ? 128 HIS AAA CA  1 
ATOM 736   C C   . HIS A 1 111 ? 124.579 9.220   30.839  1.000 29.290  ? 128 HIS AAA C   1 
ATOM 737   O O   . HIS A 1 111 ? 125.286 10.001  30.216  1.000 28.760  ? 128 HIS AAA O   1 
ATOM 738   C CB  . HIS A 1 111 ? 125.317 7.920   32.851  1.000 29.110  ? 128 HIS AAA CB  1 
ATOM 739   C CG  . HIS A 1 111 ? 126.184 9.012   33.354  1.000 28.600  ? 128 HIS AAA CG  1 
ATOM 740   N ND1 . HIS A 1 111 ? 127.526 8.833   33.547  1.000 28.790  ? 128 HIS AAA ND1 1 
ATOM 741   C CD2 . HIS A 1 111 ? 125.919 10.299  33.655  1.000 30.120  ? 128 HIS AAA CD2 1 
ATOM 742   C CE1 . HIS A 1 111 ? 128.056 9.954   33.988  1.000 29.170  ? 128 HIS AAA CE1 1 
ATOM 743   N NE2 . HIS A 1 111 ? 127.093 10.875  34.051  1.000 28.900  ? 128 HIS AAA NE2 1 
ATOM 744   N N   . ASP A 1 112 ? 123.307 9.476   31.148  1.000 30.270  ? 129 ASP AAA N   1 
ATOM 745   C CA  . ASP A 1 112 ? 122.627 10.716  30.680  1.000 33.080  ? 129 ASP AAA CA  1 
ATOM 746   C C   . ASP A 1 112 ? 123.490 11.936  31.044  1.000 31.660  ? 129 ASP AAA C   1 
ATOM 747   O O   . ASP A 1 112 ? 123.735 12.148  32.269  1.000 29.480  ? 129 ASP AAA O   1 
ATOM 748   C CB  . ASP A 1 112 ? 121.236 10.863  31.287  1.000 36.400  ? 129 ASP AAA CB  1 
ATOM 749   C CG  . ASP A 1 112 ? 120.171 10.034  30.612  1.000 38.150  ? 129 ASP AAA CG  1 
ATOM 750   O OD1 . ASP A 1 112 ? 120.470 9.396   29.617  1.000 42.300  ? 129 ASP AAA OD1 1 
ATOM 751   O OD2 . ASP A 1 112 ? 119.025 10.093  31.066  1.000 39.550  ? 129 ASP AAA OD2 1 
ATOM 752   N N   . ASN A 1 113 ? 123.943 12.689  30.031  1.000 29.910  ? 130 ASN AAA N   1 
ATOM 753   C CA  . ASN A 1 113 ? 124.749 13.934  30.169  1.000 30.730  ? 130 ASN AAA CA  1 
ATOM 754   C C   . ASN A 1 113 ? 126.164 13.573  30.636  1.000 29.300  ? 130 ASN AAA C   1 
ATOM 755   O O   . ASN A 1 113 ? 126.946 14.462  31.027  1.000 32.420  ? 130 ASN AAA O   1 
ATOM 756   C CB  . ASN A 1 113 ? 124.116 14.961  31.117  1.000 33.650  ? 130 ASN AAA CB  1 
ATOM 757   C CG  . ASN A 1 113 ? 122.697 15.338  30.744  1.000 37.110  ? 130 ASN AAA CG  1 
ATOM 758   O OD1 . ASN A 1 113 ? 122.413 15.594  29.576  1.000 34.380  ? 130 ASN AAA OD1 1 
ATOM 759   N ND2 . ASN A 1 113 ? 121.812 15.425  31.734  1.000 39.990  ? 130 ASN AAA ND2 1 
ATOM 760   N N   . GLY A 1 114 ? 126.507 12.300  30.584  1.000 26.230  ? 131 GLY AAA N   1 
ATOM 761   C CA  . GLY A 1 114 ? 127.890 11.865  30.831  1.000 24.360  ? 131 GLY AAA CA  1 
ATOM 762   C C   . GLY A 1 114 ? 128.826 12.325  29.721  1.000 21.320  ? 131 GLY AAA C   1 
ATOM 763   O O   . GLY A 1 114 ? 128.395 12.502  28.568  1.000 18.550  ? 131 GLY AAA O   1 
ATOM 764   N N   . ALA A 1 115 ? 130.093 12.495  30.067  1.000 20.540  ? 132 ALA AAA N   1 
ATOM 765   C CA  . ALA A 1 115 ? 131.184 12.597  29.083  1.000 21.550  ? 132 ALA AAA CA  1 
ATOM 766   C C   . ALA A 1 115 ? 131.278 11.250  28.380  1.000 21.870  ? 132 ALA AAA C   1 
ATOM 767   O O   . ALA A 1 115 ? 130.585 10.340  28.789  1.000 26.610  ? 132 ALA AAA O   1 
ATOM 768   C CB  . ALA A 1 115 ? 132.474 12.960  29.757  1.000 21.500  ? 132 ALA AAA CB  1 
ATOM 769   N N   . GLY A 1 116 ? 132.068 11.134  27.333  1.000 21.960  ? 133 GLY AAA N   1 
ATOM 770   C CA  . GLY A 1 116 ? 132.250 9.850   26.657  1.000 23.370  ? 133 GLY AAA CA  1 
ATOM 771   C C   . GLY A 1 116 ? 133.020 8.881   27.520  1.000 24.740  ? 133 GLY AAA C   1 
ATOM 772   O O   . GLY A 1 116 ? 133.880 9.331   28.291  1.000 24.430  ? 133 GLY AAA O   1 
ATOM 773   N N   . LYS A 1 117 ? 132.733 7.586   27.390  1.000 27.650  ? 134 LYS AAA N   1 
ATOM 774   C CA  . LYS A 1 117 ? 133.571 6.533   28.021  1.000 31.930  ? 134 LYS AAA CA  1 
ATOM 775   C C   . LYS A 1 117 ? 134.974 6.667   27.447  1.000 30.400  ? 134 LYS AAA C   1 
ATOM 776   O O   . LYS A 1 117 ? 135.143 6.607   26.236  1.000 31.940  ? 134 LYS AAA O   1 
ATOM 777   C CB  . LYS A 1 117 ? 133.014 5.136   27.753  1.000 36.020  ? 134 LYS AAA CB  1 
ATOM 778   C CG  . LYS A 1 117 ? 133.974 4.006   28.091  1.000 38.970  ? 134 LYS AAA CG  1 
ATOM 779   C CD  . LYS A 1 117 ? 133.366 2.629   27.948  1.000 40.260  ? 134 LYS AAA CD  1 
ATOM 780   C CE  . LYS A 1 117 ? 132.478 2.290   29.139  1.000 41.740  ? 134 LYS AAA CE  1 
ATOM 781   N NZ  . LYS A 1 117 ? 132.569 0.860   29.509  1.000 45.550  ? 134 LYS AAA NZ  1 
ATOM 782   N N   . PRO A 1 118 ? 136.007 6.830   28.286  1.000 27.820  ? 135 PRO AAA N   1 
ATOM 783   C CA  . PRO A 1 118 ? 137.363 7.043   27.814  1.000 27.870  ? 135 PRO AAA CA  1 
ATOM 784   C C   . PRO A 1 118 ? 137.950 5.741   27.285  1.000 25.000  ? 135 PRO AAA C   1 
ATOM 785   O O   . PRO A 1 118 ? 137.455 4.740   27.638  1.000 21.630  ? 135 PRO AAA O   1 
ATOM 786   C CB  . PRO A 1 118 ? 138.130 7.470   29.063  1.000 29.070  ? 135 PRO AAA CB  1 
ATOM 787   C CG  . PRO A 1 118 ? 137.402 6.782   30.168  1.000 30.420  ? 135 PRO AAA CG  1 
ATOM 788   C CD  . PRO A 1 118 ? 135.943 6.739   29.742  1.000 30.540  ? 135 PRO AAA CD  1 
ATOM 789   N N   . VAL A 1 119 ? 139.019 5.829   26.497  1.000 27.970  ? 136 VAL AAA N   1 
ATOM 790   C CA  . VAL A 1 119 ? 139.823 4.634   26.094  1.000 27.870  ? 136 VAL AAA CA  1 
ATOM 791   C C   . VAL A 1 119 ? 140.151 3.895   27.388  1.000 25.160  ? 136 VAL AAA C   1 
ATOM 792   O O   . VAL A 1 119 ? 140.628 4.549   28.332  1.000 22.310  ? 136 VAL AAA O   1 
ATOM 793   C CB  . VAL A 1 119 ? 141.106 4.969   25.301  1.000 28.020  ? 136 VAL AAA CB  1 
ATOM 794   C CG1 . VAL A 1 119 ? 141.985 3.743   25.154  1.000 27.290  ? 136 VAL AAA CG1 1 
ATOM 795   C CG2 . VAL A 1 119 ? 140.806 5.558   23.930  1.000 27.970  ? 136 VAL AAA CG2 1 
ATOM 796   N N   . GLN A 1 120 ? 139.871 2.594   27.400  1.000 25.590  ? 137 GLN AAA N   1 
ATOM 797   C CA  . GLN A 1 120 ? 140.120 1.667   28.528  1.000 27.010  ? 137 GLN AAA CA  1 
ATOM 798   C C   . GLN A 1 120 ? 140.061 0.224   28.024  1.000 26.280  ? 137 GLN AAA C   1 
ATOM 799   O O   . GLN A 1 120 ? 139.623 0.004   26.890  1.000 28.460  ? 137 GLN AAA O   1 
ATOM 800   C CB  . GLN A 1 120 ? 139.101 1.865   29.651  1.000 28.500  ? 137 GLN AAA CB  1 
ATOM 801   C CG  . GLN A 1 120 ? 137.668 1.508   29.258  1.000 30.710  ? 137 GLN AAA CG  1 
ATOM 802   C CD  . GLN A 1 120 ? 136.654 2.036   30.251  1.000 32.700  ? 137 GLN AAA CD  1 
ATOM 803   O OE1 . GLN A 1 120 ? 136.253 1.364   31.196  1.000 38.180  ? 137 GLN AAA OE1 1 
ATOM 804   N NE2 . GLN A 1 120 ? 136.275 3.282   30.089  1.000 31.640  ? 137 GLN AAA NE2 1 
ATOM 805   N N   . GLY A 1 121 ? 140.409 -0.722  28.878  1.000 24.490  ? 138 GLY AAA N   1 
ATOM 806   C CA  . GLY A 1 121 ? 140.220 -2.154  28.607  1.000 23.430  ? 138 GLY AAA CA  1 
ATOM 807   C C   . GLY A 1 121 ? 141.516 -2.837  28.228  1.000 23.790  ? 138 GLY AAA C   1 
ATOM 808   O O   . GLY A 1 121 ? 142.604 -2.245  28.405  1.000 25.400  ? 138 GLY AAA O   1 
ATOM 809   N N   . THR A 1 122 ? 141.391 -4.053  27.708  1.000 24.440  ? 139 THR AAA N   1 
ATOM 810   C CA  . THR A 1 122 ? 142.487 -4.997  27.373  1.000 23.550  ? 139 THR AAA CA  1 
ATOM 811   C C   . THR A 1 122 ? 143.639 -4.226  26.739  1.000 22.740  ? 139 THR AAA C   1 
ATOM 812   O O   . THR A 1 122 ? 143.402 -3.484  25.810  1.000 22.730  ? 139 THR AAA O   1 
ATOM 813   C CB  . THR A 1 122 ? 141.971 -6.128  26.477  1.000 22.860  ? 139 THR AAA CB  1 
ATOM 814   O OG1 . THR A 1 122 ? 140.802 -6.689  27.090  1.000 26.990  ? 139 THR AAA OG1 1 
ATOM 815   C CG2 . THR A 1 122 ? 143.015 -7.195  26.260  1.000 22.280  ? 139 THR AAA CG2 1 
ATOM 816   N N   . SER A 1 123 ? 144.842 -4.415  27.252  1.000 23.370  ? 140 SER AAA N   1 
ATOM 817   C CA  . SER A 1 123 ? 146.052 -3.639  26.894  1.000 25.880  ? 140 SER AAA CA  1 
ATOM 818   C C   . SER A 1 123 ? 147.222 -4.606  26.764  1.000 26.610  ? 140 SER AAA C   1 
ATOM 819   O O   . SER A 1 123 ? 147.339 -5.471  27.656  1.000 30.860  ? 140 SER AAA O   1 
ATOM 820   C CB  . SER A 1 123 ? 146.357 -2.607  27.954  1.000 27.880  ? 140 SER AAA CB  1 
ATOM 821   O OG  . SER A 1 123 ? 147.093 -3.200  29.019  1.000 29.720  ? 140 SER AAA OG  1 
ATOM 822   N N   . PHE A 1 124 ? 148.076 -4.437  25.754  1.000 25.290  ? 141 PHE AAA N   1 
ATOM 823   C CA  . PHE A 1 124 ? 149.417 -5.079  25.697  1.000 25.750  ? 141 PHE AAA CA  1 
ATOM 824   C C   . PHE A 1 124 ? 150.469 -3.981  25.474  1.000 26.110  ? 141 PHE AAA C   1 
ATOM 825   O O   . PHE A 1 124 ? 150.461 -3.334  24.419  1.000 29.150  ? 141 PHE AAA O   1 
ATOM 826   C CB  . PHE A 1 124 ? 149.431 -6.201  24.652  1.000 25.000  ? 141 PHE AAA CB  1 
ATOM 827   C CG  . PHE A 1 124 ? 150.683 -7.048  24.667  1.000 25.310  ? 141 PHE AAA CG  1 
ATOM 828   C CD1 . PHE A 1 124 ? 151.144 -7.630  25.833  1.000 26.190  ? 141 PHE AAA CD1 1 
ATOM 829   C CD2 . PHE A 1 124 ? 151.402 -7.275  23.518  1.000 24.980  ? 141 PHE AAA CD2 1 
ATOM 830   C CE1 . PHE A 1 124 ? 152.292 -8.405  25.845  1.000 25.760  ? 141 PHE AAA CE1 1 
ATOM 831   C CE2 . PHE A 1 124 ? 152.551 -8.047  23.530  1.000 24.590  ? 141 PHE AAA CE2 1 
ATOM 832   C CZ  . PHE A 1 124 ? 152.980 -8.633  24.687  1.000 24.200  ? 141 PHE AAA CZ  1 
ATOM 833   N N   . HIS A 1 125 ? 151.304 -3.721  26.476  1.000 23.990  ? 142 HIS AAA N   1 
ATOM 834   C CA  . HIS A 1 125 ? 152.485 -2.832  26.364  1.000 23.760  ? 142 HIS AAA CA  1 
ATOM 835   C C   . HIS A 1 125 ? 153.705 -3.737  26.414  1.000 23.770  ? 142 HIS AAA C   1 
ATOM 836   O O   . HIS A 1 125 ? 153.842 -4.490  27.378  1.000 26.130  ? 142 HIS AAA O   1 
ATOM 837   C CB  . HIS A 1 125 ? 152.474 -1.707  27.413  1.000 24.770  ? 142 HIS AAA CB  1 
ATOM 838   C CG  . HIS A 1 125 ? 151.293 -0.820  27.259  1.000 28.390  ? 142 HIS AAA CG  1 
ATOM 839   N ND1 . HIS A 1 125 ? 151.230 0.135   26.271  1.000 30.450  ? 142 HIS AAA ND1 1 
ATOM 840   C CD2 . HIS A 1 125 ? 150.087 -0.812  27.882  1.000 31.730  ? 142 HIS AAA CD2 1 
ATOM 841   C CE1 . HIS A 1 125 ? 150.041 0.713   26.314  1.000 34.310  ? 142 HIS AAA CE1 1 
ATOM 842   N NE2 . HIS A 1 125 ? 149.307 0.161   27.312  1.000 31.790  ? 142 HIS AAA NE2 1 
ATOM 843   N N   . PHE A 1 126 ? 154.507 -3.694  25.360  1.000 25.810  ? 143 PHE AAA N   1 
ATOM 844   C CA  . PHE A 1 126 ? 155.665 -4.579  25.091  1.000 26.630  ? 143 PHE AAA CA  1 
ATOM 845   C C   . PHE A 1 126 ? 156.726 -3.790  24.332  1.000 25.290  ? 143 PHE AAA C   1 
ATOM 846   O O   . PHE A 1 126 ? 156.371 -2.970  23.461  1.000 27.250  ? 143 PHE AAA O   1 
ATOM 847   C CB  . PHE A 1 126 ? 155.226 -5.781  24.250  1.000 28.990  ? 143 PHE AAA CB  1 
ATOM 848   C CG  . PHE A 1 126 ? 156.387 -6.537  23.668  1.000 28.630  ? 143 PHE AAA CG  1 
ATOM 849   C CD1 . PHE A 1 126 ? 157.103 -7.421  24.448  1.000 27.450  ? 143 PHE AAA CD1 1 
ATOM 850   C CD2 . PHE A 1 126 ? 156.793 -6.304  22.372  1.000 29.940  ? 143 PHE AAA CD2 1 
ATOM 851   C CE1 . PHE A 1 126 ? 158.193 -8.084  23.928  1.000 28.250  ? 143 PHE AAA CE1 1 
ATOM 852   C CE2 . PHE A 1 126 ? 157.899 -6.957  21.860  1.000 32.250  ? 143 PHE AAA CE2 1 
ATOM 853   C CZ  . PHE A 1 126 ? 158.593 -7.849  22.638  1.000 30.840  ? 143 PHE AAA CZ  1 
ATOM 854   N N   . PHE A 1 127 ? 157.990 -4.051  24.630  1.000 25.540  ? 144 PHE AAA N   1 
ATOM 855   C CA  . PHE A 1 127 ? 159.135 -3.449  23.896  1.000 27.910  ? 144 PHE AAA CA  1 
ATOM 856   C C   . PHE A 1 127 ? 160.401 -4.282  24.122  1.000 29.320  ? 144 PHE AAA C   1 
ATOM 857   O O   . PHE A 1 127 ? 160.608 -4.801  25.245  1.000 28.670  ? 144 PHE AAA O   1 
ATOM 858   C CB  . PHE A 1 127 ? 159.348 -2.013  24.348  1.000 26.560  ? 144 PHE AAA CB  1 
ATOM 859   C CG  . PHE A 1 127 ? 159.678 -1.906  25.812  1.000 26.100  ? 144 PHE AAA CG  1 
ATOM 860   C CD1 . PHE A 1 127 ? 160.992 -2.062  26.242  1.000 24.750  ? 144 PHE AAA CD1 1 
ATOM 861   C CD2 . PHE A 1 127 ? 158.685 -1.657  26.746  1.000 23.810  ? 144 PHE AAA CD2 1 
ATOM 862   C CE1 . PHE A 1 127 ? 161.312 -1.954  27.575  1.000 23.460  ? 144 PHE AAA CE1 1 
ATOM 863   C CE2 . PHE A 1 127 ? 159.012 -1.564  28.079  1.000 23.540  ? 144 PHE AAA CE2 1 
ATOM 864   C CZ  . PHE A 1 127 ? 160.306 -1.717  28.483  1.000 24.170  ? 144 PHE AAA CZ  1 
ATOM 865   N N   . SER A 1 128 ? 161.210 -4.393  23.068  1.000 30.680  ? 145 SER AAA N   1 
ATOM 866   C CA  . SER A 1 128 ? 162.423 -5.240  23.007  1.000 32.820  ? 145 SER AAA CA  1 
ATOM 867   C C   . SER A 1 128 ? 163.571 -4.430  22.401  1.000 32.540  ? 145 SER AAA C   1 
ATOM 868   O O   . SER A 1 128 ? 163.287 -3.556  21.551  1.000 35.290  ? 145 SER AAA O   1 
ATOM 869   C CB  . SER A 1 128 ? 162.145 -6.492  22.215  1.000 34.390  ? 145 SER AAA CB  1 
ATOM 870   O OG  . SER A 1 128 ? 162.427 -6.298  20.831  1.000 37.820  ? 145 SER AAA OG  1 
ATOM 871   N N   . VAL A 1 129 ? 164.804 -4.717  22.822  1.000 31.560  ? 146 VAL AAA N   1 
ATOM 872   C CA  . VAL A 1 129 ? 166.054 -4.200  22.186  1.000 35.360  ? 146 VAL AAA CA  1 
ATOM 873   C C   . VAL A 1 129 ? 166.965 -5.401  21.879  1.000 43.420  ? 146 VAL AAA C   1 
ATOM 874   O O   . VAL A 1 129 ? 167.292 -6.166  22.809  1.000 43.660  ? 146 VAL AAA O   1 
ATOM 875   C CB  . VAL A 1 129 ? 166.738 -3.153  23.073  1.000 31.980  ? 146 VAL AAA CB  1 
ATOM 876   C CG1 . VAL A 1 129 ? 168.044 -2.674  22.486  1.000 30.940  ? 146 VAL AAA CG1 1 
ATOM 877   C CG2 . VAL A 1 129 ? 165.807 -1.983  23.322  1.000 33.870  ? 146 VAL AAA CG2 1 
ATOM 878   N N   . GLY A 1 130 ? 167.328 -5.569  20.605  1.000 47.310  ? 147 GLY AAA N   1 
ATOM 879   C CA  . GLY A 1 130 ? 168.000 -6.774  20.090  1.000 47.090  ? 147 GLY AAA CA  1 
ATOM 880   C C   . GLY A 1 130 ? 169.098 -6.446  19.095  1.000 49.050  ? 147 GLY AAA C   1 
ATOM 881   O O   . GLY A 1 130 ? 168.956 -5.433  18.364  1.000 50.650  ? 147 GLY AAA O   1 
ATOM 882   N N   . GLY A 1 131 ? 170.147 -7.281  19.073  1.000 46.960  ? 148 GLY AAA N   1 
ATOM 883   C CA  . GLY A 1 131 ? 171.204 -7.321  18.041  1.000 48.670  ? 148 GLY AAA CA  1 
ATOM 884   C C   . GLY A 1 131 ? 170.764 -8.053  16.775  1.000 47.420  ? 148 GLY AAA C   1 
ATOM 885   O O   . GLY A 1 131 ? 171.557 -8.136  15.800  1.000 48.100  ? 148 GLY AAA O   1 
ATOM 886   N N   . GLU A 1 132 ? 169.532 -8.561  16.775  1.000 41.730  ? 149 GLU AAA N   1 
ATOM 887   C CA  . GLU A 1 132 ? 168.900 -9.250  15.625  1.000 37.410  ? 149 GLU AAA CA  1 
ATOM 888   C C   . GLU A 1 132 ? 167.391 -9.215  15.839  1.000 38.030  ? 149 GLU AAA C   1 
ATOM 889   O O   . GLU A 1 132 ? 166.958 -8.747  16.917  1.000 42.260  ? 149 GLU AAA O   1 
ATOM 890   C CB  . GLU A 1 132 ? 169.382 -10.693 15.536  1.000 34.280  ? 149 GLU AAA CB  1 
ATOM 891   C CG  . GLU A 1 132 ? 169.863 -11.255 16.857  1.000 31.640  ? 149 GLU AAA CG  1 
ATOM 892   C CD  . GLU A 1 132 ? 170.171 -12.737 16.829  1.000 31.060  ? 149 GLU AAA CD  1 
ATOM 893   O OE1 . GLU A 1 132 ? 169.344 -13.512 16.314  1.000 30.340  ? 149 GLU AAA OE1 1 
ATOM 894   O OE2 . GLU A 1 132 ? 171.261 -13.100 17.296  1.000 30.770  ? 149 GLU AAA OE2 1 
ATOM 895   N N   . ALA A 1 133 ? 166.624 -9.710  14.881  1.000 37.760  ? 150 ALA AAA N   1 
ATOM 896   C CA  . ALA A 1 133 ? 165.149 -9.732  14.978  1.000 43.170  ? 150 ALA AAA CA  1 
ATOM 897   C C   . ALA A 1 133 ? 164.710 -10.379 16.302  1.000 42.810  ? 150 ALA AAA C   1 
ATOM 898   O O   . ALA A 1 133 ? 165.338 -11.372 16.744  1.000 36.320  ? 150 ALA AAA O   1 
ATOM 899   C CB  . ALA A 1 133 ? 164.562 -10.492 13.818  1.000 48.810  ? 150 ALA AAA CB  1 
ATOM 900   N N   . LEU A 1 134 ? 163.649 -9.843  16.897  1.000 39.280  ? 151 LEU AAA N   1 
ATOM 901   C CA  . LEU A 1 134 ? 162.860 -10.578 17.916  1.000 39.450  ? 151 LEU AAA CA  1 
ATOM 902   C C   . LEU A 1 134 ? 162.434 -11.928 17.337  1.000 34.320  ? 151 LEU AAA C   1 
ATOM 903   O O   . LEU A 1 134 ? 161.930 -11.960 16.210  1.000 31.390  ? 151 LEU AAA O   1 
ATOM 904   C CB  . LEU A 1 134 ? 161.634 -9.755  18.310  1.000 44.540  ? 151 LEU AAA CB  1 
ATOM 905   C CG  . LEU A 1 134 ? 160.791 -10.307 19.458  1.000 39.830  ? 151 LEU AAA CG  1 
ATOM 906   C CD1 . LEU A 1 134 ? 161.599 -10.343 20.730  1.000 36.890  ? 151 LEU AAA CD1 1 
ATOM 907   C CD2 . LEU A 1 134 ? 159.559 -9.452  19.653  1.000 39.450  ? 151 LEU AAA CD2 1 
ATOM 908   N N   . GLU A 1 135 ? 162.619 -12.994 18.104  1.000 32.440  ? 152 GLU AAA N   1 
ATOM 909   C CA  . GLU A 1 135 ? 162.195 -14.368 17.737  1.000 32.910  ? 152 GLU AAA CA  1 
ATOM 910   C C   . GLU A 1 135 ? 160.835 -14.666 18.367  1.000 30.920  ? 152 GLU AAA C   1 
ATOM 911   O O   . GLU A 1 135 ? 160.714 -14.487 19.584  1.000 32.210  ? 152 GLU AAA O   1 
ATOM 912   C CB  . GLU A 1 135 ? 163.287 -15.350 18.150  1.000 33.140  ? 152 GLU AAA CB  1 
ATOM 913   C CG  . GLU A 1 135 ? 164.551 -15.143 17.343  1.000 36.050  ? 152 GLU AAA CG  1 
ATOM 914   C CD  . GLU A 1 135 ? 165.653 -16.125 17.653  1.000 37.270  ? 152 GLU AAA CD  1 
ATOM 915   O OE1 . GLU A 1 135 ? 166.450 -15.876 18.588  1.000 37.650  ? 152 GLU AAA OE1 1 
ATOM 916   O OE2 . GLU A 1 135 ? 165.682 -17.146 16.982  1.000 43.680  ? 152 GLU AAA OE2 1 
ATOM 917   N N   . LEU A 1 136 ? 159.873 -15.106 17.556  1.000 29.650  ? 153 LEU AAA N   1 
ATOM 918   C CA  . LEU A 1 136 ? 158.463 -15.333 17.962  1.000 31.970  ? 153 LEU AAA CA  1 
ATOM 919   C C   . LEU A 1 136 ? 158.136 -16.833 18.054  1.000 34.600  ? 153 LEU AAA C   1 
ATOM 920   O O   . LEU A 1 136 ? 158.567 -17.623 17.182  1.000 32.840  ? 153 LEU AAA O   1 
ATOM 921   C CB  . LEU A 1 136 ? 157.528 -14.689 16.952  1.000 33.970  ? 153 LEU AAA CB  1 
ATOM 922   C CG  . LEU A 1 136 ? 157.733 -13.204 16.677  1.000 40.150  ? 153 LEU AAA CG  1 
ATOM 923   C CD1 . LEU A 1 136 ? 156.786 -12.726 15.570  1.000 38.710  ? 153 LEU AAA CD1 1 
ATOM 924   C CD2 . LEU A 1 136 ? 157.551 -12.383 17.958  1.000 44.710  ? 153 LEU AAA CD2 1 
ATOM 925   N N   . GLN A 1 137 ? 157.344 -17.191 19.070  1.000 34.640  ? 154 GLN AAA N   1 
ATOM 926   C CA  . GLN A 1 137 ? 156.597 -18.468 19.198  1.000 31.110  ? 154 GLN AAA CA  1 
ATOM 927   C C   . GLN A 1 137 ? 155.122 -18.172 18.914  1.000 30.320  ? 154 GLN AAA C   1 
ATOM 928   O O   . GLN A 1 137 ? 154.587 -17.204 19.454  1.000 29.620  ? 154 GLN AAA O   1 
ATOM 929   C CB  . GLN A 1 137 ? 156.771 -19.039 20.607  1.000 30.120  ? 154 GLN AAA CB  1 
ATOM 930   C CG  . GLN A 1 137 ? 155.846 -20.207 20.912  1.000 29.230  ? 154 GLN AAA CG  1 
ATOM 931   C CD  . GLN A 1 137 ? 156.181 -21.364 20.015  1.000 33.540  ? 154 GLN AAA CD  1 
ATOM 932   O OE1 . GLN A 1 137 ? 157.350 -21.667 19.801  1.000 34.390  ? 154 GLN AAA OE1 1 
ATOM 933   N NE2 . GLN A 1 137 ? 155.159 -22.023 19.482  1.000 40.110  ? 154 GLN AAA NE2 1 
ATOM 934   N N   . GLY A 1 138 ? 154.483 -18.970 18.077  1.000 29.390  ? 155 GLY AAA N   1 
ATOM 935   C CA  . GLY A 1 138 ? 153.036 -18.873 17.853  1.000 26.710  ? 155 GLY AAA CA  1 
ATOM 936   C C   . GLY A 1 138 ? 152.288 -19.570 18.959  1.000 26.420  ? 155 GLY AAA C   1 
ATOM 937   O O   . GLY A 1 138 ? 152.652 -20.721 19.333  1.000 25.210  ? 155 GLY AAA O   1 
ATOM 938   N N   . VAL A 1 139 ? 151.257 -18.908 19.468  1.000 29.000  ? 156 VAL AAA N   1 
ATOM 939   C CA  . VAL A 1 139 ? 150.242 -19.537 20.363  1.000 31.830  ? 156 VAL AAA CA  1 
ATOM 940   C C   . VAL A 1 139 ? 148.886 -18.984 19.964  1.000 31.850  ? 156 VAL AAA C   1 
ATOM 941   O O   . VAL A 1 139 ? 148.779 -17.746 19.822  1.000 35.270  ? 156 VAL AAA O   1 
ATOM 942   C CB  . VAL A 1 139 ? 150.489 -19.272 21.855  1.000 32.960  ? 156 VAL AAA CB  1 
ATOM 943   C CG1 . VAL A 1 139 ? 149.519 -20.082 22.695  1.000 32.190  ? 156 VAL AAA CG1 1 
ATOM 944   C CG2 . VAL A 1 139 ? 151.935 -19.523 22.267  1.000 34.680  ? 156 VAL AAA CG2 1 
ATOM 945   N N   . LEU A 1 140 ? 147.904 -19.871 19.830  1.000 31.120  ? 157 LEU AAA N   1 
ATOM 946   C CA  . LEU A 1 140 ? 146.567 -19.532 19.291  1.000 32.780  ? 157 LEU AAA CA  1 
ATOM 947   C C   . LEU A 1 140 ? 145.532 -19.611 20.415  1.000 30.850  ? 157 LEU AAA C   1 
ATOM 948   O O   . LEU A 1 140 ? 145.566 -20.560 21.186  1.000 28.540  ? 157 LEU AAA O   1 
ATOM 949   C CB  . LEU A 1 140 ? 146.231 -20.481 18.134  1.000 31.460  ? 157 LEU AAA CB  1 
ATOM 950   C CG  . LEU A 1 140 ? 147.166 -20.397 16.917  1.000 29.390  ? 157 LEU AAA CG  1 
ATOM 951   C CD1 . LEU A 1 140 ? 146.694 -21.328 15.811  1.000 30.030  ? 157 LEU AAA CD1 1 
ATOM 952   C CD2 . LEU A 1 140 ? 147.283 -18.968 16.401  1.000 26.960  ? 157 LEU AAA CD2 1 
ATOM 953   N N   . PHE A 1 141 ? 144.635 -18.634 20.496  1.000 31.340  ? 158 PHE AAA N   1 
ATOM 954   C CA  . PHE A 1 141 ? 143.466 -18.735 21.396  1.000 28.540  ? 158 PHE AAA CA  1 
ATOM 955   C C   . PHE A 1 141 ? 142.581 -19.859 20.858  1.000 26.160  ? 158 PHE AAA C   1 
ATOM 956   O O   . PHE A 1 141 ? 142.167 -20.726 21.631  1.000 24.480  ? 158 PHE AAA O   1 
ATOM 957   C CB  . PHE A 1 141 ? 142.712 -17.413 21.509  1.000 27.810  ? 158 PHE AAA CB  1 
ATOM 958   C CG  . PHE A 1 141 ? 141.490 -17.526 22.373  1.000 27.700  ? 158 PHE AAA CG  1 
ATOM 959   C CD1 . PHE A 1 141 ? 141.609 -17.648 23.754  1.000 27.950  ? 158 PHE AAA CD1 1 
ATOM 960   C CD2 . PHE A 1 141 ? 140.228 -17.591 21.806  1.000 27.980  ? 158 PHE AAA CD2 1 
ATOM 961   C CE1 . PHE A 1 141 ? 140.484 -17.790 24.554  1.000 25.890  ? 158 PHE AAA CE1 1 
ATOM 962   C CE2 . PHE A 1 141 ? 139.101 -17.691 22.612  1.000 28.600  ? 158 PHE AAA CE2 1 
ATOM 963   C CZ  . PHE A 1 141 ? 139.235 -17.808 23.981  1.000 26.660  ? 158 PHE AAA CZ  1 
ATOM 964   N N   . ASN A 1 142 ? 142.341 -19.852 19.554  1.000 24.800  ? 159 ASN AAA N   1 
ATOM 965   C CA  . ASN A 1 142 ? 141.494 -20.858 18.864  1.000 27.260  ? 159 ASN AAA CA  1 
ATOM 966   C C   . ASN A 1 142 ? 142.241 -21.301 17.613  1.000 29.780  ? 159 ASN AAA C   1 
ATOM 967   O O   . ASN A 1 142 ? 142.463 -20.426 16.779  1.000 36.590  ? 159 ASN AAA O   1 
ATOM 968   C CB  . ASN A 1 142 ? 140.133 -20.250 18.503  1.000 26.500  ? 159 ASN AAA CB  1 
ATOM 969   C CG  . ASN A 1 142 ? 139.220 -21.176 17.736  1.000 23.620  ? 159 ASN AAA CG  1 
ATOM 970   O OD1 . ASN A 1 142 ? 139.509 -22.357 17.619  1.000 22.520  ? 159 ASN AAA OD1 1 
ATOM 971   N ND2 . ASN A 1 142 ? 138.102 -20.656 17.270  1.000 22.860  ? 159 ASN AAA ND2 1 
ATOM 972   N N   . TYR A 1 143 ? 142.661 -22.567 17.501  1.000 30.010  ? 160 TYR AAA N   1 
ATOM 973   C CA  . TYR A 1 143 ? 143.520 -23.040 16.368  1.000 31.730  ? 160 TYR AAA CA  1 
ATOM 974   C C   . TYR A 1 143 ? 142.771 -23.002 15.023  1.000 32.040  ? 160 TYR AAA C   1 
ATOM 975   O O   . TYR A 1 143 ? 143.475 -22.846 13.994  1.000 35.210  ? 160 TYR AAA O   1 
ATOM 976   C CB  . TYR A 1 143 ? 144.169 -24.407 16.640  1.000 33.840  ? 160 TYR AAA CB  1 
ATOM 977   C CG  . TYR A 1 143 ? 143.347 -25.609 16.240  1.000 37.170  ? 160 TYR AAA CG  1 
ATOM 978   C CD1 . TYR A 1 143 ? 142.261 -26.000 17.008  1.000 39.240  ? 160 TYR AAA CD1 1 
ATOM 979   C CD2 . TYR A 1 143 ? 143.630 -26.354 15.108  1.000 36.610  ? 160 TYR AAA CD2 1 
ATOM 980   C CE1 . TYR A 1 143 ? 141.479 -27.082 16.667  1.000 36.780  ? 160 TYR AAA CE1 1 
ATOM 981   C CE2 . TYR A 1 143 ? 142.852 -27.447 14.757  1.000 35.420  ? 160 TYR AAA CE2 1 
ATOM 982   C CZ  . TYR A 1 143 ? 141.794 -27.826 15.559  1.000 34.900  ? 160 TYR AAA CZ  1 
ATOM 983   O OH  . TYR A 1 143 ? 140.968 -28.868 15.301  1.000 37.880  ? 160 TYR AAA OH  1 
ATOM 984   N N   . ARG A 1 144 ? 141.434 -22.962 15.030  1.000 30.430  ? 161 ARG AAA N   1 
ATOM 985   C CA  . ARG A 1 144 ? 140.614 -22.934 13.789  1.000 30.010  ? 161 ARG AAA CA  1 
ATOM 986   C C   . ARG A 1 144 ? 140.351 -21.483 13.360  1.000 27.030  ? 161 ARG AAA C   1 
ATOM 987   O O   . ARG A 1 144 ? 139.638 -21.275 12.376  1.000 23.300  ? 161 ARG AAA O   1 
ATOM 988   C CB  . ARG A 1 144 ? 139.285 -23.643 14.029  1.000 33.080  ? 161 ARG AAA CB  1 
ATOM 989   C CG  . ARG A 1 144 ? 139.393 -25.149 14.213  1.000 37.950  ? 161 ARG AAA CG  1 
ATOM 990   C CD  . ARG A 1 144 ? 138.024 -25.789 14.124  1.000 40.030  ? 161 ARG AAA CD  1 
ATOM 991   N NE  . ARG A 1 144 ? 137.218 -25.277 15.217  1.000 44.370  ? 161 ARG AAA NE  1 
ATOM 992   C CZ  . ARG A 1 144 ? 137.192 -25.778 16.443  1.000 46.390  ? 161 ARG AAA CZ  1 
ATOM 993   N NH1 . ARG A 1 144 ? 136.409 -25.227 17.355  1.000 50.230  ? 161 ARG AAA NH1 1 
ATOM 994   N NH2 . ARG A 1 144 ? 137.941 -26.819 16.753  1.000 38.960  ? 161 ARG AAA NH2 1 
ATOM 995   N N   . THR A 1 145 ? 140.868 -20.523 14.117  1.000 30.360  ? 162 THR AAA N   1 
ATOM 996   C CA  . THR A 1 145 ? 140.813 -19.074 13.720  1.000 30.720  ? 162 THR AAA CA  1 
ATOM 997   C C   . THR A 1 145 ? 141.547 -19.006 12.382  1.000 27.660  ? 162 THR AAA C   1 
ATOM 998   O O   . THR A 1 145 ? 142.690 -19.485 12.375  1.000 28.620  ? 162 THR AAA O   1 
ATOM 999   C CB  . THR A 1 145 ? 141.559 -18.108 14.662  1.000 30.460  ? 162 THR AAA CB  1 
ATOM 1000  O OG1 . THR A 1 145 ? 141.037 -18.015 15.988  1.000 29.170  ? 162 THR AAA OG1 1 
ATOM 1001  C CG2 . THR A 1 145 ? 141.593 -16.707 14.105  1.000 30.180  ? 162 THR AAA CG2 1 
ATOM 1002  N N   . LYS A 1 146 ? 140.938 -18.450 11.332  1.000 25.970  ? 163 LYS AAA N   1 
ATOM 1003  C CA  . LYS A 1 146 ? 141.595 -18.228 10.022  1.000 27.990  ? 163 LYS AAA CA  1 
ATOM 1004  C C   . LYS A 1 146 ? 142.203 -16.827 9.978   1.000 28.580  ? 163 LYS AAA C   1 
ATOM 1005  O O   . LYS A 1 146 ? 141.436 -15.853 9.782   1.000 27.460  ? 163 LYS AAA O   1 
ATOM 1006  C CB  . LYS A 1 146 ? 140.610 -18.359 8.862   1.000 32.220  ? 163 LYS AAA CB  1 
ATOM 1007  C CG  . LYS A 1 146 ? 141.237 -18.101 7.490   1.000 37.760  ? 163 LYS AAA CG  1 
ATOM 1008  C CD  . LYS A 1 146 ? 140.313 -18.323 6.308   1.000 41.390  ? 163 LYS AAA CD  1 
ATOM 1009  C CE  . LYS A 1 146 ? 139.094 -17.412 6.315   1.000 49.610  ? 163 LYS AAA CE  1 
ATOM 1010  N NZ  . LYS A 1 146 ? 139.139 -16.370 5.252   1.000 52.290  ? 163 LYS AAA NZ  1 
ATOM 1011  N N   . TYR A 1 147 ? 143.528 -16.714 10.107  1.000 30.580  ? 164 TYR AAA N   1 
ATOM 1012  C CA  . TYR A 1 147 ? 144.211 -15.390 10.122  1.000 31.120  ? 164 TYR AAA CA  1 
ATOM 1013  C C   . TYR A 1 147 ? 144.204 -14.860 8.699   1.000 32.770  ? 164 TYR AAA C   1 
ATOM 1014  O O   . TYR A 1 147 ? 144.403 -15.617 7.762   1.000 31.970  ? 164 TYR AAA O   1 
ATOM 1015  C CB  . TYR A 1 147 ? 145.552 -15.452 10.863  1.000 29.210  ? 164 TYR AAA CB  1 
ATOM 1016  C CG  . TYR A 1 147 ? 145.350 -15.481 12.363  1.000 29.460  ? 164 TYR AAA CG  1 
ATOM 1017  C CD1 . TYR A 1 147 ? 145.154 -16.673 13.018  1.000 27.970  ? 164 TYR AAA CD1 1 
ATOM 1018  C CD2 . TYR A 1 147 ? 145.227 -14.318 13.119  1.000 29.900  ? 164 TYR AAA CD2 1 
ATOM 1019  C CE1 . TYR A 1 147 ? 144.914 -16.717 14.380  1.000 30.320  ? 164 TYR AAA CE1 1 
ATOM 1020  C CE2 . TYR A 1 147 ? 144.984 -14.349 14.486  1.000 28.550  ? 164 TYR AAA CE2 1 
ATOM 1021  C CZ  . TYR A 1 147 ? 144.825 -15.558 15.128  1.000 29.590  ? 164 TYR AAA CZ  1 
ATOM 1022  O OH  . TYR A 1 147 ? 144.572 -15.665 16.474  1.000 32.570  ? 164 TYR AAA OH  1 
ATOM 1023  N N   . PRO A 1 148 ? 143.946 -13.550 8.496   1.000 42.320  ? 165 PRO AAA N   1 
ATOM 1024  C CA  . PRO A 1 148 ? 143.560 -13.038 7.189   1.000 42.980  ? 165 PRO AAA CA  1 
ATOM 1025  C C   . PRO A 1 148 ? 144.793 -12.881 6.287   1.000 43.660  ? 165 PRO AAA C   1 
ATOM 1026  O O   . PRO A 1 148 ? 145.897 -12.568 6.751   1.000 37.150  ? 165 PRO AAA O   1 
ATOM 1027  C CB  . PRO A 1 148 ? 142.975 -11.657 7.516   1.000 44.460  ? 165 PRO AAA CB  1 
ATOM 1028  C CG  . PRO A 1 148 ? 143.850 -11.186 8.668   1.000 45.580  ? 165 PRO AAA CG  1 
ATOM 1029  C CD  . PRO A 1 148 ? 144.158 -12.455 9.458   1.000 46.760  ? 165 PRO AAA CD  1 
ATOM 1030  N N   . ASP A 1 149 ? 144.567 -13.135 5.010   1.000 43.830  ? 166 ASP AAA N   1 
ATOM 1031  C CA  . ASP A 1 149 ? 145.453 -12.824 3.865   1.000 45.360  ? 166 ASP AAA CA  1 
ATOM 1032  C C   . ASP A 1 149 ? 146.203 -11.507 4.116   1.000 33.440  ? 166 ASP AAA C   1 
ATOM 1033  O O   . ASP A 1 149 ? 145.556 -10.458 4.268   1.000 25.910  ? 166 ASP AAA O   1 
ATOM 1034  C CB  . ASP A 1 149 ? 144.560 -12.776 2.623   1.000 57.580  ? 166 ASP AAA CB  1 
ATOM 1035  C CG  . ASP A 1 149 ? 145.281 -13.122 1.349   1.000 63.360  ? 166 ASP AAA CG  1 
ATOM 1036  O OD1 . ASP A 1 149 ? 146.362 -12.532 1.115   1.000 66.080  ? 166 ASP AAA OD1 1 
ATOM 1037  O OD2 . ASP A 1 149 ? 144.756 -13.987 0.624   1.000 71.250  ? 166 ASP AAA OD2 1 
ATOM 1038  N N   . GLY A 1 150 ? 147.529 -11.551 4.152   1.000 30.820  ? 167 GLY AAA N   1 
ATOM 1039  C CA  . GLY A 1 150 ? 148.357 -10.329 4.235   1.000 30.830  ? 167 GLY AAA CA  1 
ATOM 1040  C C   . GLY A 1 150 ? 149.096 -10.193 5.548   1.000 29.250  ? 167 GLY AAA C   1 
ATOM 1041  O O   . GLY A 1 150 ? 149.894 -9.268  5.667   1.000 27.870  ? 167 GLY AAA O   1 
ATOM 1042  N N   . THR A 1 151 ? 148.791 -11.095 6.491   1.000 29.070  ? 168 THR AAA N   1 
ATOM 1043  C CA  . THR A 1 151 ? 149.457 -11.229 7.809   1.000 27.590  ? 168 THR AAA CA  1 
ATOM 1044  C C   . THR A 1 151 ? 150.263 -12.513 7.781   1.000 27.980  ? 168 THR AAA C   1 
ATOM 1045  O O   . THR A 1 151 ? 149.828 -13.432 7.115   1.000 32.380  ? 168 THR AAA O   1 
ATOM 1046  C CB  . THR A 1 151 ? 148.436 -11.294 8.945   1.000 27.810  ? 168 THR AAA CB  1 
ATOM 1047  O OG1 . THR A 1 151 ? 147.598 -12.436 8.773   1.000 26.940  ? 168 THR AAA OG1 1 
ATOM 1048  C CG2 . THR A 1 151 ? 147.531 -10.086 8.964   1.000 31.570  ? 168 THR AAA CG2 1 
ATOM 1049  N N   . ILE A 1 152 ? 151.381 -12.567 8.491   1.000 29.140  ? 169 ILE AAA N   1 
ATOM 1050  C CA  . ILE A 1 152 ? 152.177 -13.810 8.690   1.000 28.690  ? 169 ILE AAA CA  1 
ATOM 1051  C C   . ILE A 1 152 ? 151.684 -14.455 9.985   1.000 27.840  ? 169 ILE AAA C   1 
ATOM 1052  O O   . ILE A 1 152 ? 151.791 -13.847 11.046  1.000 24.760  ? 169 ILE AAA O   1 
ATOM 1053  C CB  . ILE A 1 152 ? 153.668 -13.446 8.696   1.000 31.740  ? 169 ILE AAA CB  1 
ATOM 1054  C CG1 . ILE A 1 152 ? 154.108 -12.989 7.311   1.000 34.840  ? 169 ILE AAA CG1 1 
ATOM 1055  C CG2 . ILE A 1 152 ? 154.562 -14.561 9.184   1.000 32.000  ? 169 ILE AAA CG2 1 
ATOM 1056  C CD1 . ILE A 1 152 ? 155.382 -12.164 7.358   1.000 40.220  ? 169 ILE AAA CD1 1 
ATOM 1057  N N   . PHE A 1 153 ? 151.126 -15.652 9.890   1.000 30.310  ? 170 PHE AAA N   1 
ATOM 1058  C CA  . PHE A 1 153 ? 150.490 -16.339 11.038  1.000 31.660  ? 170 PHE AAA CA  1 
ATOM 1059  C C   . PHE A 1 153 ? 151.038 -17.749 11.175  1.000 30.240  ? 170 PHE AAA C   1 
ATOM 1060  O O   . PHE A 1 153 ? 151.658 -18.265 10.256  1.000 30.230  ? 170 PHE AAA O   1 
ATOM 1061  C CB  . PHE A 1 153 ? 148.979 -16.372 10.836  1.000 33.040  ? 170 PHE AAA CB  1 
ATOM 1062  C CG  . PHE A 1 153 ? 148.535 -16.892 9.498   1.000 33.980  ? 170 PHE AAA CG  1 
ATOM 1063  C CD1 . PHE A 1 153 ? 148.489 -16.059 8.397   1.000 34.050  ? 170 PHE AAA CD1 1 
ATOM 1064  C CD2 . PHE A 1 153 ? 148.116 -18.198 9.353   1.000 36.730  ? 170 PHE AAA CD2 1 
ATOM 1065  C CE1 . PHE A 1 153 ? 148.037 -16.520 7.169   1.000 33.920  ? 170 PHE AAA CE1 1 
ATOM 1066  C CE2 . PHE A 1 153 ? 147.683 -18.663 8.120   1.000 37.630  ? 170 PHE AAA CE2 1 
ATOM 1067  C CZ  . PHE A 1 153 ? 147.631 -17.816 7.033   1.000 34.960  ? 170 PHE AAA CZ  1 
ATOM 1068  N N   . PRO A 1 154 ? 150.845 -18.397 12.340  1.000 29.220  ? 171 PRO AAA N   1 
ATOM 1069  C CA  . PRO A 1 154 ? 151.154 -19.808 12.512  1.000 31.960  ? 171 PRO AAA CA  1 
ATOM 1070  C C   . PRO A 1 154 ? 150.528 -20.679 11.424  1.000 35.290  ? 171 PRO AAA C   1 
ATOM 1071  O O   . PRO A 1 154 ? 149.324 -20.610 11.258  1.000 34.390  ? 171 PRO AAA O   1 
ATOM 1072  C CB  . PRO A 1 154 ? 150.528 -20.160 13.851  1.000 30.160  ? 171 PRO AAA CB  1 
ATOM 1073  C CG  . PRO A 1 154 ? 150.693 -18.872 14.595  1.000 31.340  ? 171 PRO AAA CG  1 
ATOM 1074  C CD  . PRO A 1 154 ? 150.360 -17.803 13.578  1.000 29.720  ? 171 PRO AAA CD  1 
ATOM 1075  N N   . LYS A 1 155 ? 151.382 -21.429 10.720  1.000 35.680  ? 172 LYS AAA N   1 
ATOM 1076  C CA  . LYS A 1 155 ? 150.984 -22.327 9.623   1.000 38.170  ? 172 LYS AAA CA  1 
ATOM 1077  C C   . LYS A 1 155 ? 150.913 -23.736 10.196  1.000 36.330  ? 172 LYS AAA C   1 
ATOM 1078  O O   . LYS A 1 155 ? 151.675 -24.024 11.106  1.000 34.740  ? 172 LYS AAA O   1 
ATOM 1079  C CB  . LYS A 1 155 ? 151.974 -22.192 8.465   1.000 41.310  ? 172 LYS AAA CB  1 
ATOM 1080  C CG  . LYS A 1 155 ? 151.880 -20.865 7.719   1.000 42.940  ? 172 LYS AAA CG  1 
ATOM 1081  C CD  . LYS A 1 155 ? 152.855 -20.743 6.578   1.000 47.460  ? 172 LYS AAA CD  1 
ATOM 1082  C CE  . LYS A 1 155 ? 154.313 -20.558 6.983   1.000 52.820  ? 172 LYS AAA CE  1 
ATOM 1083  N NZ  . LYS A 1 155 ? 154.627 -19.163 7.389   1.000 58.490  ? 172 LYS AAA NZ  1 
ATOM 1084  N N   . ASN A 1 156 ? 150.011 -24.555 9.666   1.000 39.970  ? 173 ASN AAA N   1 
ATOM 1085  C CA  . ASN A 1 156 ? 149.821 -25.987 10.026  1.000 39.410  ? 173 ASN AAA CA  1 
ATOM 1086  C C   . ASN A 1 156 ? 149.348 -26.065 11.471  1.000 38.880  ? 173 ASN AAA C   1 
ATOM 1087  O O   . ASN A 1 156 ? 149.853 -26.901 12.228  1.000 41.640  ? 173 ASN AAA O   1 
ATOM 1088  C CB  . ASN A 1 156 ? 151.085 -26.794 9.794   1.000 39.760  ? 173 ASN AAA CB  1 
ATOM 1089  C CG  . ASN A 1 156 ? 151.511 -26.766 8.350   1.000 40.630  ? 173 ASN AAA CG  1 
ATOM 1090  O OD1 . ASN A 1 156 ? 150.696 -26.984 7.461   1.000 43.300  ? 173 ASN AAA OD1 1 
ATOM 1091  N ND2 . ASN A 1 156 ? 152.774 -26.460 8.115   1.000 44.000  ? 173 ASN AAA ND2 1 
ATOM 1092  N N   . ALA A 1 157 ? 148.402 -25.199 11.819  1.000 39.830  ? 174 ALA AAA N   1 
ATOM 1093  C CA  . ALA A 1 157 ? 147.776 -25.142 13.150  1.000 39.360  ? 174 ALA AAA CA  1 
ATOM 1094  C C   . ALA A 1 157 ? 147.168 -26.506 13.437  1.000 33.360  ? 174 ALA AAA C   1 
ATOM 1095  O O   . ALA A 1 157 ? 146.473 -27.037 12.581  1.000 30.380  ? 174 ALA AAA O   1 
ATOM 1096  C CB  . ALA A 1 157 ? 146.729 -24.057 13.206  1.000 44.290  ? 174 ALA AAA CB  1 
ATOM 1097  N N   . THR A 1 158 ? 147.461 -27.027 14.617  1.000 31.700  ? 175 THR AAA N   1 
ATOM 1098  C CA  . THR A 1 158 ? 146.810 -28.211 15.206  1.000 32.310  ? 175 THR AAA CA  1 
ATOM 1099  C C   . THR A 1 158 ? 146.162 -27.753 16.521  1.000 31.840  ? 175 THR AAA C   1 
ATOM 1100  O O   . THR A 1 158 ? 146.433 -26.621 16.978  1.000 29.700  ? 175 THR AAA O   1 
ATOM 1101  C CB  . THR A 1 158 ? 147.856 -29.330 15.289  1.000 32.320  ? 175 THR AAA CB  1 
ATOM 1102  O OG1 . THR A 1 158 ? 148.770 -29.126 16.373  1.000 36.650  ? 175 THR AAA OG1 1 
ATOM 1103  C CG2 . THR A 1 158 ? 148.658 -29.427 14.014  1.000 29.720  ? 175 THR AAA CG2 1 
ATOM 1104  N N   . VAL A 1 159 ? 145.320 -28.585 17.122  1.000 30.920  ? 176 VAL AAA N   1 
ATOM 1105  C CA  . VAL A 1 159 ? 144.751 -28.260 18.455  1.000 30.490  ? 176 VAL AAA CA  1 
ATOM 1106  C C   . VAL A 1 159 ? 145.919 -27.946 19.388  1.000 29.610  ? 176 VAL AAA C   1 
ATOM 1107  O O   . VAL A 1 159 ? 145.777 -27.017 20.172  1.000 30.480  ? 176 VAL AAA O   1 
ATOM 1108  C CB  . VAL A 1 159 ? 143.837 -29.377 18.991  1.000 32.250  ? 176 VAL AAA CB  1 
ATOM 1109  C CG1 . VAL A 1 159 ? 144.603 -30.474 19.664  1.000 33.770  ? 176 VAL AAA CG1 1 
ATOM 1110  C CG2 . VAL A 1 159 ? 142.795 -28.842 19.949  1.000 32.900  ? 176 VAL AAA CG2 1 
ATOM 1111  N N   . GLN A 1 160 ? 147.055 -28.644 19.276  1.000 30.010  ? 177 GLN AAA N   1 
ATOM 1112  C CA  . GLN A 1 160 ? 148.221 -28.405 20.178  1.000 29.440  ? 177 GLN AAA CA  1 
ATOM 1113  C C   . GLN A 1 160 ? 148.674 -26.950 20.041  1.000 25.710  ? 177 GLN AAA C   1 
ATOM 1114  O O   . GLN A 1 160 ? 149.213 -26.426 21.010  1.000 23.420  ? 177 GLN AAA O   1 
ATOM 1115  C CB  . GLN A 1 160 ? 149.396 -29.350 19.928  1.000 32.860  ? 177 GLN AAA CB  1 
ATOM 1116  C CG  . GLN A 1 160 ? 149.065 -30.804 20.200  1.000 40.110  ? 177 GLN AAA CG  1 
ATOM 1117  C CD  . GLN A 1 160 ? 148.468 -31.111 21.566  1.000 47.720  ? 177 GLN AAA CD  1 
ATOM 1118  O OE1 . GLN A 1 160 ? 148.908 -30.625 22.625  1.000 48.100  ? 177 GLN AAA OE1 1 
ATOM 1119  N NE2 . GLN A 1 160 ? 147.458 -31.975 21.548  1.000 44.780  ? 177 GLN AAA NE2 1 
ATOM 1120  N N   . SER A 1 161 ? 148.440 -26.314 18.894  1.000 25.250  ? 178 SER AAA N   1 
ATOM 1121  C CA  . SER A 1 161 ? 148.818 -24.899 18.657  1.000 27.550  ? 178 SER AAA CA  1 
ATOM 1122  C C   . SER A 1 161 ? 148.211 -24.003 19.755  1.000 31.000  ? 178 SER AAA C   1 
ATOM 1123  O O   . SER A 1 161 ? 148.900 -23.015 20.135  1.000 35.200  ? 178 SER AAA O   1 
ATOM 1124  C CB  . SER A 1 161 ? 148.432 -24.457 17.270  1.000 27.240  ? 178 SER AAA CB  1 
ATOM 1125  O OG  . SER A 1 161 ? 149.169 -25.197 16.293  1.000 25.060  ? 178 SER AAA OG  1 
ATOM 1126  N N   . GLN A 1 162 ? 147.011 -24.365 20.266  1.000 28.530  ? 179 GLN AAA N   1 
ATOM 1127  C CA  . GLN A 1 162 ? 146.247 -23.654 21.334  1.000 24.630  ? 179 GLN AAA CA  1 
ATOM 1128  C C   . GLN A 1 162 ? 147.025 -23.595 22.659  1.000 25.000  ? 179 GLN AAA C   1 
ATOM 1129  O O   . GLN A 1 162 ? 146.713 -22.703 23.456  1.000 25.140  ? 179 GLN AAA O   1 
ATOM 1130  C CB  . GLN A 1 162 ? 144.890 -24.318 21.586  1.000 22.300  ? 179 GLN AAA CB  1 
ATOM 1131  C CG  . GLN A 1 162 ? 143.735 -23.683 20.829  1.000 22.250  ? 179 GLN AAA CG  1 
ATOM 1132  C CD  . GLN A 1 162 ? 142.525 -24.573 20.635  1.000 21.470  ? 179 GLN AAA CD  1 
ATOM 1133  O OE1 . GLN A 1 162 ? 141.719 -24.367 19.721  1.000 20.200  ? 179 GLN AAA OE1 1 
ATOM 1134  N NE2 . GLN A 1 162 ? 142.375 -25.568 21.498  1.000 20.320  ? 179 GLN AAA NE2 1 
ATOM 1135  N N   . VAL A 1 163 ? 147.950 -24.518 22.943  1.000 25.060  ? 180 VAL AAA N   1 
ATOM 1136  C CA  . VAL A 1 163 ? 148.678 -24.515 24.251  1.000 27.010  ? 180 VAL AAA CA  1 
ATOM 1137  C C   . VAL A 1 163 ? 150.176 -24.352 24.016  1.000 28.630  ? 180 VAL AAA C   1 
ATOM 1138  O O   . VAL A 1 163 ? 150.799 -23.493 24.720  1.000 27.970  ? 180 VAL AAA O   1 
ATOM 1139  C CB  . VAL A 1 163 ? 148.393 -25.755 25.117  1.000 27.700  ? 180 VAL AAA CB  1 
ATOM 1140  C CG1 . VAL A 1 163 ? 146.950 -25.769 25.598  1.000 27.750  ? 180 VAL AAA CG1 1 
ATOM 1141  C CG2 . VAL A 1 163 ? 148.737 -27.057 24.425  1.000 28.380  ? 180 VAL AAA CG2 1 
ATOM 1142  N N   . MET A 1 164 ? 150.708 -25.120 23.064  1.000 30.480  ? 181 MET AAA N   1 
ATOM 1143  C CA  . MET A 1 164 ? 152.113 -25.034 22.614  1.000 33.590  ? 181 MET AAA CA  1 
ATOM 1144  C C   . MET A 1 164 ? 152.358 -25.975 21.422  1.000 34.730  ? 181 MET AAA C   1 
ATOM 1145  O O   . MET A 1 164 ? 151.977 -27.165 21.486  1.000 30.530  ? 181 MET AAA O   1 
ATOM 1146  C CB  . MET A 1 164 ? 153.049 -25.418 23.758  1.000 35.310  ? 181 MET AAA CB  1 
ATOM 1147  C CG  . MET A 1 164 ? 154.494 -25.139 23.432  1.000 38.210  ? 181 MET AAA CG  1 
ATOM 1148  S SD  . MET A 1 164 ? 154.795 -23.407 23.048  1.000 38.370  ? 181 MET AAA SD  1 
ATOM 1149  C CE  . MET A 1 164 ? 156.422 -23.603 22.325  1.000 38.120  ? 181 MET AAA CE  1 
ATOM 1150  N N   . ASN A 1 165 ? 153.024 -25.467 20.381  1.000 38.800  ? 182 ASN AAA N   1 
ATOM 1151  C CA  . ASN A 1 165 ? 153.388 -26.255 19.174  1.000 34.510  ? 182 ASN AAA CA  1 
ATOM 1152  C C   . ASN A 1 165 ? 154.679 -25.682 18.570  1.000 34.490  ? 182 ASN AAA C   1 
ATOM 1153  O O   . ASN A 1 165 ? 154.601 -24.618 17.942  1.000 31.950  ? 182 ASN AAA O   1 
ATOM 1154  C CB  . ASN A 1 165 ? 152.199 -26.246 18.212  1.000 31.640  ? 182 ASN AAA CB  1 
ATOM 1155  C CG  . ASN A 1 165 ? 152.515 -26.837 16.867  1.000 28.480  ? 182 ASN AAA CG  1 
ATOM 1156  O OD1 . ASN A 1 165 ? 153.688 -26.977 16.511  1.000 28.660  ? 182 ASN AAA OD1 1 
ATOM 1157  N ND2 . ASN A 1 165 ? 151.473 -27.159 16.129  1.000 26.000  ? 182 ASN AAA ND2 1 
ATOM 1158  N N   . THR A 1 166 ? 155.817 -26.357 18.742  1.000 35.200  ? 183 THR AAA N   1 
ATOM 1159  C CA  . THR A 1 166 ? 157.158 -25.819 18.394  1.000 37.780  ? 183 THR AAA CA  1 
ATOM 1160  C C   . THR A 1 166 ? 157.335 -25.617 16.879  1.000 39.880  ? 183 THR AAA C   1 
ATOM 1161  O O   . THR A 1 166 ? 158.364 -25.003 16.481  1.000 37.180  ? 183 THR AAA O   1 
ATOM 1162  C CB  . THR A 1 166 ? 158.291 -26.723 18.881  1.000 37.590  ? 183 THR AAA CB  1 
ATOM 1163  O OG1 . THR A 1 166 ? 157.761 -28.035 18.758  1.000 40.870  ? 183 THR AAA OG1 1 
ATOM 1164  C CG2 . THR A 1 166 ? 158.740 -26.454 20.299  1.000 38.840  ? 183 THR AAA CG2 1 
ATOM 1165  N N   . GLU A 1 167 ? 156.393 -26.074 16.047  1.000 39.350  ? 184 GLU AAA N   1 
ATOM 1166  C CA  . GLU A 1 167 ? 156.435 -25.752 14.596  1.000 38.470  ? 184 GLU AAA CA  1 
ATOM 1167  C C   . GLU A 1 167 ? 156.406 -24.230 14.425  1.000 37.320  ? 184 GLU AAA C   1 
ATOM 1168  O O   . GLU A 1 167 ? 157.204 -23.749 13.621  1.000 37.370  ? 184 GLU AAA O   1 
ATOM 1169  C CB  . GLU A 1 167 ? 155.308 -26.405 13.802  1.000 45.010  ? 184 GLU AAA CB  1 
ATOM 1170  C CG  . GLU A 1 167 ? 155.720 -26.740 12.368  1.000 52.450  ? 184 GLU AAA CG  1 
ATOM 1171  C CD  . GLU A 1 167 ? 154.593 -26.855 11.339  1.000 58.820  ? 184 GLU AAA CD  1 
ATOM 1172  O OE1 . GLU A 1 167 ? 154.456 -25.927 10.515  1.000 59.240  ? 184 GLU AAA OE1 1 
ATOM 1173  O OE2 . GLU A 1 167 ? 153.861 -27.876 11.346  1.000 63.480  ? 184 GLU AAA OE2 1 
ATOM 1174  N N   . HIS A 1 168 ? 155.583 -23.507 15.201  1.000 38.190  ? 185 HIS AAA N   1 
ATOM 1175  C CA  . HIS A 1 168 ? 155.273 -22.056 15.027  1.000 32.400  ? 185 HIS AAA CA  1 
ATOM 1176  C C   . HIS A 1 168 ? 156.416 -21.173 15.507  1.000 29.360  ? 185 HIS AAA C   1 
ATOM 1177  O O   . HIS A 1 168 ? 156.209 -20.419 16.476  1.000 29.500  ? 185 HIS AAA O   1 
ATOM 1178  C CB  . HIS A 1 168 ? 153.983 -21.685 15.759  1.000 30.530  ? 185 HIS AAA CB  1 
ATOM 1179  C CG  . HIS A 1 168 ? 152.852 -22.574 15.404  1.000 29.250  ? 185 HIS AAA CG  1 
ATOM 1180  N ND1 . HIS A 1 168 ? 152.572 -22.902 14.109  1.000 29.630  ? 185 HIS AAA ND1 1 
ATOM 1181  C CD2 . HIS A 1 168 ? 151.945 -23.207 16.165  1.000 30.380  ? 185 HIS AAA CD2 1 
ATOM 1182  C CE1 . HIS A 1 168 ? 151.522 -23.696 14.085  1.000 31.070  ? 185 HIS AAA CE1 1 
ATOM 1183  N NE2 . HIS A 1 168 ? 151.124 -23.906 15.322  1.000 30.800  ? 185 HIS AAA NE2 1 
ATOM 1184  N N   . LYS A 1 169 ? 157.555 -21.211 14.812  1.000 28.250  ? 186 LYS AAA N   1 
ATOM 1185  C CA  . LYS A 1 169 ? 158.655 -20.231 15.000  1.000 27.520  ? 186 LYS AAA CA  1 
ATOM 1186  C C   . LYS A 1 169 ? 158.619 -19.216 13.865  1.000 26.780  ? 186 LYS AAA C   1 
ATOM 1187  O O   . LYS A 1 169 ? 158.015 -19.514 12.828  1.000 30.510  ? 186 LYS AAA O   1 
ATOM 1188  C CB  . LYS A 1 169 ? 159.986 -20.964 15.100  1.000 27.230  ? 186 LYS AAA CB  1 
ATOM 1189  C CG  . LYS A 1 169 ? 159.972 -22.135 16.066  1.000 30.170  ? 186 LYS AAA CG  1 
ATOM 1190  C CD  . LYS A 1 169 ? 159.895 -21.746 17.524  1.000 32.300  ? 186 LYS AAA CD  1 
ATOM 1191  C CE  . LYS A 1 169 ? 160.125 -22.932 18.433  1.000 36.280  ? 186 LYS AAA CE  1 
ATOM 1192  N NZ  . LYS A 1 169 ? 160.088 -22.567 19.869  1.000 38.740  ? 186 LYS AAA NZ  1 
ATOM 1193  N N   . ALA A 1 170 ? 159.194 -18.036 14.086  1.000 26.500  ? 187 ALA AAA N   1 
ATOM 1194  C CA  . ALA A 1 170 ? 159.151 -16.899 13.144  1.000 27.630  ? 187 ALA AAA CA  1 
ATOM 1195  C C   . ALA A 1 170 ? 160.029 -15.749 13.630  1.000 29.490  ? 187 ALA AAA C   1 
ATOM 1196  O O   . ALA A 1 170 ? 160.282 -15.665 14.832  1.000 30.850  ? 187 ALA AAA O   1 
ATOM 1197  C CB  . ALA A 1 170 ? 157.728 -16.454 12.979  1.000 26.930  ? 187 ALA AAA CB  1 
ATOM 1198  N N   . TYR A 1 171 ? 160.436 -14.871 12.717  1.000 32.490  ? 188 TYR AAA N   1 
ATOM 1199  C CA  . TYR A 1 171 ? 161.242 -13.668 13.021  1.000 37.390  ? 188 TYR AAA CA  1 
ATOM 1200  C C   . TYR A 1 171 ? 160.351 -12.438 12.840  1.000 39.930  ? 188 TYR AAA C   1 
ATOM 1201  O O   . TYR A 1 171 ? 159.682 -12.328 11.795  1.000 42.430  ? 188 TYR AAA O   1 
ATOM 1202  C CB  . TYR A 1 171 ? 162.486 -13.619 12.127  1.000 41.090  ? 188 TYR AAA CB  1 
ATOM 1203  C CG  . TYR A 1 171 ? 163.481 -14.731 12.350  1.000 43.660  ? 188 TYR AAA CG  1 
ATOM 1204  C CD1 . TYR A 1 171 ? 164.407 -14.634 13.373  1.000 47.850  ? 188 TYR AAA CD1 1 
ATOM 1205  C CD2 . TYR A 1 171 ? 163.516 -15.863 11.551  1.000 40.530  ? 188 TYR AAA CD2 1 
ATOM 1206  C CE1 . TYR A 1 171 ? 165.337 -15.632 13.601  1.000 46.170  ? 188 TYR AAA CE1 1 
ATOM 1207  C CE2 . TYR A 1 171 ? 164.428 -16.875 11.776  1.000 38.960  ? 188 TYR AAA CE2 1 
ATOM 1208  C CZ  . TYR A 1 171 ? 165.348 -16.758 12.798  1.000 41.810  ? 188 TYR AAA CZ  1 
ATOM 1209  O OH  . TYR A 1 171 ? 166.279 -17.732 13.018  1.000 39.350  ? 188 TYR AAA OH  1 
ATOM 1210  N N   . LEU A 1 172 ? 160.352 -11.535 13.828  1.000 42.070  ? 189 LEU AAA N   1 
ATOM 1211  C CA  . LEU A 1 172 ? 159.729 -10.199 13.673  1.000 41.490  ? 189 LEU AAA CA  1 
ATOM 1212  C C   . LEU A 1 172 ? 160.634 -9.360  12.772  1.000 39.240  ? 189 LEU AAA C   1 
ATOM 1213  O O   . LEU A 1 172 ? 161.493 -8.580  13.295  1.000 34.860  ? 189 LEU AAA O   1 
ATOM 1214  C CB  . LEU A 1 172 ? 159.531 -9.529  15.032  1.000 44.560  ? 189 LEU AAA CB  1 
ATOM 1215  C CG  . LEU A 1 172 ? 158.729 -8.231  14.975  1.000 45.320  ? 189 LEU AAA CG  1 
ATOM 1216  C CD1 . LEU A 1 172 ? 157.454 -8.376  14.126  1.000 43.510  ? 189 LEU AAA CD1 1 
ATOM 1217  C CD2 . LEU A 1 172 ? 158.405 -7.758  16.385  1.000 47.610  ? 189 LEU AAA CD2 1 
ATOM 1218  N N   . ASP A 1 173 ? 160.425 -9.543  11.471  1.000 40.910  ? 190 ASP AAA N   1 
ATOM 1219  C CA  . ASP A 1 173 ? 161.287 -9.026  10.379  1.000 46.970  ? 190 ASP AAA CA  1 
ATOM 1220  C C   . ASP A 1 173 ? 160.462 -8.141  9.435   1.000 46.430  ? 190 ASP AAA C   1 
ATOM 1221  O O   . ASP A 1 173 ? 161.030 -7.706  8.438   1.000 54.370  ? 190 ASP AAA O   1 
ATOM 1222  C CB  . ASP A 1 173 ? 161.918 -10.187 9.597   1.000 46.190  ? 190 ASP AAA CB  1 
ATOM 1223  C CG  . ASP A 1 173 ? 160.908 -11.201 9.078   1.000 48.780  ? 190 ASP AAA CG  1 
ATOM 1224  O OD1 . ASP A 1 173 ? 159.691 -10.885 9.024   1.000 50.940  ? 190 ASP AAA OD1 1 
ATOM 1225  O OD2 . ASP A 1 173 ? 161.338 -12.312 8.730   1.000 48.590  ? 190 ASP AAA OD2 1 
ATOM 1226  N N   . LYS A 1 174 ? 159.185 -7.881  9.727   1.000 40.550  ? 191 LYS AAA N   1 
ATOM 1227  C CA  . LYS A 1 174 ? 158.280 -7.157  8.797   1.000 39.830  ? 191 LYS AAA CA  1 
ATOM 1228  C C   . LYS A 1 174 ? 157.172 -6.429  9.573   1.000 38.740  ? 191 LYS AAA C   1 
ATOM 1229  O O   . LYS A 1 174 ? 156.618 -6.991  10.566  1.000 46.830  ? 191 LYS AAA O   1 
ATOM 1230  C CB  . LYS A 1 174 ? 157.724 -8.145  7.772   1.000 40.230  ? 191 LYS AAA CB  1 
ATOM 1231  C CG  . LYS A 1 174 ? 157.040 -7.511  6.572   1.000 43.990  ? 191 LYS AAA CG  1 
ATOM 1232  C CD  . LYS A 1 174 ? 156.406 -8.542  5.662   1.000 49.140  ? 191 LYS AAA CD  1 
ATOM 1233  C CE  . LYS A 1 174 ? 156.053 -8.038  4.277   1.000 51.480  ? 191 LYS AAA CE  1 
ATOM 1234  N NZ  . LYS A 1 174 ? 156.153 -9.141  3.292   1.000 54.060  ? 191 LYS AAA NZ  1 
ATOM 1235  N N   . ASN A 1 175 ? 156.839 -5.219  9.134   1.000 33.880  ? 192 ASN AAA N   1 
ATOM 1236  C CA  . ASN A 1 175 ? 155.789 -4.410  9.787   1.000 36.580  ? 192 ASN AAA CA  1 
ATOM 1237  C C   . ASN A 1 175 ? 154.421 -4.750  9.210   1.000 39.390  ? 192 ASN AAA C   1 
ATOM 1238  O O   . ASN A 1 175 ? 154.344 -5.302  8.108   1.000 37.620  ? 192 ASN AAA O   1 
ATOM 1239  C CB  . ASN A 1 175 ? 156.100 -2.925  9.676   1.000 37.470  ? 192 ASN AAA CB  1 
ATOM 1240  C CG  . ASN A 1 175 ? 156.651 -2.395  10.978  1.000 37.930  ? 192 ASN AAA CG  1 
ATOM 1241  O OD1 . ASN A 1 175 ? 155.890 -2.059  11.888  1.000 42.370  ? 192 ASN AAA OD1 1 
ATOM 1242  N ND2 . ASN A 1 175 ? 157.965 -2.399  11.102  1.000 34.390  ? 192 ASN AAA ND2 1 
ATOM 1243  N N   . LYS A 1 176 ? 153.381 -4.411  9.963   1.000 45.310  ? 193 LYS AAA N   1 
ATOM 1244  C CA  . LYS A 1 176 ? 151.969 -4.571  9.533   1.000 46.940  ? 193 LYS AAA CA  1 
ATOM 1245  C C   . LYS A 1 176 ? 151.751 -6.035  9.163   1.000 48.450  ? 193 LYS AAA C   1 
ATOM 1246  O O   . LYS A 1 176 ? 150.796 -6.317  8.417   1.000 51.710  ? 193 LYS AAA O   1 
ATOM 1247  C CB  . LYS A 1 176 ? 151.649 -3.612  8.381   1.000 48.570  ? 193 LYS AAA CB  1 
ATOM 1248  C CG  . LYS A 1 176 ? 151.921 -2.145  8.711   1.000 54.310  ? 193 LYS AAA CG  1 
ATOM 1249  C CD  . LYS A 1 176 ? 152.004 -1.195  7.543   1.000 57.940  ? 193 LYS AAA CD  1 
ATOM 1250  C CE  . LYS A 1 176 ? 150.627 -0.769  7.108   1.000 65.630  ? 193 LYS AAA CE  1 
ATOM 1251  N NZ  . LYS A 1 176 ? 150.699 0.511   6.359   1.000 76.900  ? 193 LYS AAA NZ  1 
ATOM 1252  N N   . ALA A 1 177 ? 152.565 -6.930  9.731   1.000 47.570  ? 194 ALA AAA N   1 
ATOM 1253  C CA  . ALA A 1 177 ? 152.675 -8.341  9.290   1.000 48.870  ? 194 ALA AAA CA  1 
ATOM 1254  C C   . ALA A 1 177 ? 152.202 -9.312  10.383  1.000 43.480  ? 194 ALA AAA C   1 
ATOM 1255  O O   . ALA A 1 177 ? 151.300 -10.115 10.105  1.000 36.960  ? 194 ALA AAA O   1 
ATOM 1256  C CB  . ALA A 1 177 ? 154.096 -8.629  8.868   1.000 52.260  ? 194 ALA AAA CB  1 
ATOM 1257  N N   . TYR A 1 178 ? 152.826 -9.274  11.559  1.000 40.840  ? 195 TYR AAA N   1 
ATOM 1258  C CA  . TYR A 1 178 ? 152.678 -10.322 12.602  1.000 35.180  ? 195 TYR AAA CA  1 
ATOM 1259  C C   . TYR A 1 178 ? 151.615 -9.895  13.606  1.000 32.650  ? 195 TYR AAA C   1 
ATOM 1260  O O   . TYR A 1 178 ? 151.879 -9.078  14.489  1.000 33.620  ? 195 TYR AAA O   1 
ATOM 1261  C CB  . TYR A 1 178 ? 154.018 -10.598 13.282  1.000 35.630  ? 195 TYR AAA CB  1 
ATOM 1262  C CG  . TYR A 1 178 ? 155.050 -11.211 12.369  1.000 36.100  ? 195 TYR AAA CG  1 
ATOM 1263  C CD1 . TYR A 1 178 ? 155.852 -10.426 11.556  1.000 36.370  ? 195 TYR AAA CD1 1 
ATOM 1264  C CD2 . TYR A 1 178 ? 155.226 -12.577 12.316  1.000 36.140  ? 195 TYR AAA CD2 1 
ATOM 1265  C CE1 . TYR A 1 178 ? 156.785 -10.986 10.696  1.000 34.410  ? 195 TYR AAA CE1 1 
ATOM 1266  C CE2 . TYR A 1 178 ? 156.166 -13.147 11.480  1.000 36.310  ? 195 TYR AAA CE2 1 
ATOM 1267  C CZ  . TYR A 1 178 ? 156.941 -12.352 10.654  1.000 35.050  ? 195 TYR AAA CZ  1 
ATOM 1268  O OH  . TYR A 1 178 ? 157.881 -12.916 9.842   1.000 35.580  ? 195 TYR AAA OH  1 
ATOM 1269  N N   . PRO A 1 179 ? 150.381 -10.447 13.529  1.000 28.500  ? 196 PRO AAA N   1 
ATOM 1270  C CA  . PRO A 1 179 ? 149.330 -10.097 14.472  1.000 27.750  ? 196 PRO AAA CA  1 
ATOM 1271  C C   . PRO A 1 179 ? 149.825 -10.272 15.910  1.000 28.500  ? 196 PRO AAA C   1 
ATOM 1272  O O   . PRO A 1 179 ? 150.560 -11.196 16.121  1.000 31.350  ? 196 PRO AAA O   1 
ATOM 1273  C CB  . PRO A 1 179 ? 148.213 -11.081 14.138  1.000 26.710  ? 196 PRO AAA CB  1 
ATOM 1274  C CG  . PRO A 1 179 ? 148.434 -11.411 12.706  1.000 27.480  ? 196 PRO AAA CG  1 
ATOM 1275  C CD  . PRO A 1 179 ? 149.932 -11.459 12.572  1.000 29.220  ? 196 PRO AAA CD  1 
ATOM 1276  N N   . VAL A 1 180 ? 149.380 -9.423  16.842  1.000 26.030  ? 197 VAL AAA N   1 
ATOM 1277  C CA  . VAL A 1 180 ? 149.806 -9.470  18.265  1.000 25.440  ? 197 VAL AAA CA  1 
ATOM 1278  C C   . VAL A 1 180 ? 149.239 -10.746 18.905  1.000 25.550  ? 197 VAL AAA C   1 
ATOM 1279  O O   . VAL A 1 180 ? 149.936 -11.347 19.740  1.000 22.710  ? 197 VAL AAA O   1 
ATOM 1280  C CB  . VAL A 1 180 ? 149.361 -8.204  19.025  1.000 25.450  ? 197 VAL AAA CB  1 
ATOM 1281  C CG1 . VAL A 1 180 ? 149.687 -8.285  20.508  1.000 24.370  ? 197 VAL AAA CG1 1 
ATOM 1282  C CG2 . VAL A 1 180 ? 149.966 -6.948  18.414  1.000 25.940  ? 197 VAL AAA CG2 1 
ATOM 1283  N N   . GLU A 1 181 ? 148.027 -11.153 18.495  1.000 26.130  ? 198 GLU AAA N   1 
ATOM 1284  C CA  . GLU A 1 181 ? 147.197 -12.125 19.239  1.000 25.810  ? 198 GLU AAA CA  1 
ATOM 1285  C C   . GLU A 1 181 ? 147.616 -13.570 18.957  1.000 29.100  ? 198 GLU AAA C   1 
ATOM 1286  O O   . GLU A 1 181 ? 146.964 -14.491 19.503  1.000 32.880  ? 198 GLU AAA O   1 
ATOM 1287  C CB  . GLU A 1 181 ? 145.724 -11.873 18.914  1.000 24.920  ? 198 GLU AAA CB  1 
ATOM 1288  C CG  . GLU A 1 181 ? 145.192 -12.447 17.627  1.000 24.480  ? 198 GLU AAA CG  1 
ATOM 1289  C CD  . GLU A 1 181 ? 143.661 -12.356 17.520  1.000 24.300  ? 198 GLU AAA CD  1 
ATOM 1290  O OE1 . GLU A 1 181 ? 143.075 -11.357 17.994  1.000 26.850  ? 198 GLU AAA OE1 1 
ATOM 1291  O OE2 . GLU A 1 181 ? 143.067 -13.254 16.934  1.000 23.170  ? 198 GLU AAA OE2 1 
ATOM 1292  N N   . CYS A 1 182 ? 148.611 -13.805 18.108  1.000 31.130  ? 199 CYS AAA N   1 
ATOM 1293  C CA  . CYS A 1 182 ? 149.013 -15.192 17.754  1.000 33.330  ? 199 CYS AAA CA  1 
ATOM 1294  C C   . CYS A 1 182 ? 150.535 -15.345 17.797  1.000 32.720  ? 199 CYS AAA C   1 
ATOM 1295  O O   . CYS A 1 182 ? 151.012 -16.458 17.499  1.000 33.290  ? 199 CYS AAA O   1 
ATOM 1296  C CB  . CYS A 1 182 ? 148.408 -15.651 16.430  1.000 33.870  ? 199 CYS AAA CB  1 
ATOM 1297  S SG  . CYS A 1 182 ? 148.719 -14.556 15.026  1.000 34.610  ? 199 CYS AAA SG  1 
ATOM 1298  N N   . TRP A 1 183 ? 151.260 -14.322 18.247  1.000 31.760  ? 200 TRP AAA N   1 
ATOM 1299  C CA  . TRP A 1 183 ? 152.740 -14.371 18.396  1.000 31.340  ? 200 TRP AAA CA  1 
ATOM 1300  C C   . TRP A 1 183 ? 153.161 -13.798 19.751  1.000 29.400  ? 200 TRP AAA C   1 
ATOM 1301  O O   . TRP A 1 183 ? 152.610 -12.772 20.159  1.000 30.240  ? 200 TRP AAA O   1 
ATOM 1302  C CB  . TRP A 1 183 ? 153.427 -13.605 17.255  1.000 32.920  ? 200 TRP AAA CB  1 
ATOM 1303  C CG  . TRP A 1 183 ? 153.200 -14.156 15.883  1.000 32.360  ? 200 TRP AAA CG  1 
ATOM 1304  C CD1 . TRP A 1 183 ? 152.429 -13.627 14.899  1.000 31.680  ? 200 TRP AAA CD1 1 
ATOM 1305  C CD2 . TRP A 1 183 ? 153.762 -15.358 15.338  1.000 33.820  ? 200 TRP AAA CD2 1 
ATOM 1306  N NE1 . TRP A 1 183 ? 152.464 -14.409 13.778  1.000 31.550  ? 200 TRP AAA NE1 1 
ATOM 1307  C CE2 . TRP A 1 183 ? 153.278 -15.477 14.017  1.000 33.110  ? 200 TRP AAA CE2 1 
ATOM 1308  C CE3 . TRP A 1 183 ? 154.593 -16.358 15.858  1.000 33.400  ? 200 TRP AAA CE3 1 
ATOM 1309  C CZ2 . TRP A 1 183 ? 153.598 -16.562 13.212  1.000 33.310  ? 200 TRP AAA CZ2 1 
ATOM 1310  C CZ3 . TRP A 1 183 ? 154.912 -17.429 15.061  1.000 31.500  ? 200 TRP AAA CZ3 1 
ATOM 1311  C CH2 . TRP A 1 183 ? 154.429 -17.516 13.755  1.000 33.620  ? 200 TRP AAA CH2 1 
ATOM 1312  N N   . VAL A 1 184 ? 154.141 -14.420 20.389  1.000 29.150  ? 201 VAL AAA N   1 
ATOM 1313  C CA  . VAL A 1 184 ? 154.796 -13.900 21.624  1.000 31.480  ? 201 VAL AAA CA  1 
ATOM 1314  C C   . VAL A 1 184 ? 156.296 -14.083 21.482  1.000 31.480  ? 201 VAL AAA C   1 
ATOM 1315  O O   . VAL A 1 184 ? 156.744 -14.910 20.710  1.000 29.320  ? 201 VAL AAA O   1 
ATOM 1316  C CB  . VAL A 1 184 ? 154.270 -14.621 22.868  1.000 31.500  ? 201 VAL AAA CB  1 
ATOM 1317  C CG1 . VAL A 1 184 ? 152.765 -14.437 22.975  1.000 32.140  ? 201 VAL AAA CG1 1 
ATOM 1318  C CG2 . VAL A 1 184 ? 154.643 -16.089 22.857  1.000 30.470  ? 201 VAL AAA CG2 1 
ATOM 1319  N N   . PRO A 1 185 ? 157.114 -13.311 22.213  1.000 33.930  ? 202 PRO AAA N   1 
ATOM 1320  C CA  . PRO A 1 185 ? 158.546 -13.570 22.240  1.000 35.930  ? 202 PRO AAA CA  1 
ATOM 1321  C C   . PRO A 1 185 ? 158.737 -15.040 22.635  1.000 37.690  ? 202 PRO AAA C   1 
ATOM 1322  O O   . PRO A 1 185 ? 158.043 -15.494 23.566  1.000 39.830  ? 202 PRO AAA O   1 
ATOM 1323  C CB  . PRO A 1 185 ? 159.075 -12.585 23.294  1.000 38.050  ? 202 PRO AAA CB  1 
ATOM 1324  C CG  . PRO A 1 185 ? 158.060 -11.462 23.280  1.000 36.380  ? 202 PRO AAA CG  1 
ATOM 1325  C CD  . PRO A 1 185 ? 156.726 -12.144 23.024  1.000 36.370  ? 202 PRO AAA CD  1 
ATOM 1326  N N   . ASP A 1 186 ? 159.623 -15.728 21.910  1.000 36.840  ? 203 ASP AAA N   1 
ATOM 1327  C CA  . ASP A 1 186 ? 159.964 -17.160 22.101  1.000 35.760  ? 203 ASP AAA CA  1 
ATOM 1328  C C   . ASP A 1 186 ? 161.030 -17.230 23.186  1.000 33.520  ? 203 ASP AAA C   1 
ATOM 1329  O O   . ASP A 1 186 ? 162.174 -16.842 22.973  1.000 31.130  ? 203 ASP AAA O   1 
ATOM 1330  C CB  . ASP A 1 186 ? 160.463 -17.799 20.803  1.000 37.190  ? 203 ASP AAA CB  1 
ATOM 1331  C CG  . ASP A 1 186 ? 160.866 -19.259 20.897  1.000 37.480  ? 203 ASP AAA CG  1 
ATOM 1332  O OD1 . ASP A 1 186 ? 160.866 -19.789 21.998  1.000 39.590  ? 203 ASP AAA OD1 1 
ATOM 1333  O OD2 . ASP A 1 186 ? 161.185 -19.852 19.854  1.000 40.130  ? 203 ASP AAA OD2 1 
ATOM 1334  N N   . PRO A 1 187 ? 160.685 -17.734 24.383  1.000 29.860  ? 204 PRO AAA N   1 
ATOM 1335  C CA  . PRO A 1 187 ? 161.573 -17.634 25.526  1.000 32.120  ? 204 PRO AAA CA  1 
ATOM 1336  C C   . PRO A 1 187 ? 162.712 -18.648 25.412  1.000 33.240  ? 204 PRO AAA C   1 
ATOM 1337  O O   . PRO A 1 187 ? 163.643 -18.544 26.168  1.000 36.810  ? 204 PRO AAA O   1 
ATOM 1338  C CB  . PRO A 1 187 ? 160.653 -17.993 26.692  1.000 32.640  ? 204 PRO AAA CB  1 
ATOM 1339  C CG  . PRO A 1 187 ? 159.689 -18.986 26.078  1.000 31.530  ? 204 PRO AAA CG  1 
ATOM 1340  C CD  . PRO A 1 187 ? 159.447 -18.456 24.688  1.000 29.780  ? 204 PRO AAA CD  1 
ATOM 1341  N N   . THR A 1 188 ? 162.583 -19.599 24.487  1.000 33.730  ? 205 THR AAA N   1 
ATOM 1342  C CA  . THR A 1 188 ? 163.584 -20.662 24.210  1.000 36.130  ? 205 THR AAA CA  1 
ATOM 1343  C C   . THR A 1 188 ? 164.692 -20.107 23.307  1.000 38.070  ? 205 THR AAA C   1 
ATOM 1344  O O   . THR A 1 188 ? 165.673 -20.832 23.071  1.000 38.050  ? 205 THR AAA O   1 
ATOM 1345  C CB  . THR A 1 188 ? 162.962 -21.893 23.539  1.000 32.850  ? 205 THR AAA CB  1 
ATOM 1346  O OG1 . THR A 1 188 ? 162.739 -21.534 22.172  1.000 34.850  ? 205 THR AAA OG1 1 
ATOM 1347  C CG2 . THR A 1 188 ? 161.690 -22.362 24.209  1.000 29.710  ? 205 THR AAA CG2 1 
ATOM 1348  N N   . ARG A 1 189 ? 164.513 -18.893 22.783  1.000 37.910  ? 206 ARG AAA N   1 
ATOM 1349  C CA  . ARG A 1 189 ? 165.505 -18.219 21.915  1.000 39.410  ? 206 ARG AAA CA  1 
ATOM 1350  C C   . ARG A 1 189 ? 165.728 -16.809 22.473  1.000 36.130  ? 206 ARG AAA C   1 
ATOM 1351  O O   . ARG A 1 189 ? 165.634 -16.642 23.679  1.000 39.710  ? 206 ARG AAA O   1 
ATOM 1352  C CB  . ARG A 1 189 ? 164.978 -18.317 20.479  1.000 40.590  ? 206 ARG AAA CB  1 
ATOM 1353  C CG  . ARG A 1 189 ? 165.094 -19.712 19.871  1.000 39.740  ? 206 ARG AAA CG  1 
ATOM 1354  C CD  . ARG A 1 189 ? 164.388 -19.877 18.523  1.000 37.520  ? 206 ARG AAA CD  1 
ATOM 1355  N N   . ASN A 1 190 ? 166.054 -15.843 21.627  1.000 34.290  ? 207 ASN AAA N   1 
ATOM 1356  C CA  . ASN A 1 190 ? 166.190 -14.410 21.996  1.000 34.720  ? 207 ASN AAA CA  1 
ATOM 1357  C C   . ASN A 1 190 ? 167.342 -14.240 22.998  1.000 34.420  ? 207 ASN AAA C   1 
ATOM 1358  O O   . ASN A 1 190 ? 167.266 -13.311 23.831  1.000 35.980  ? 207 ASN AAA O   1 
ATOM 1359  C CB  . ASN A 1 190 ? 164.875 -13.816 22.532  1.000 35.730  ? 207 ASN AAA CB  1 
ATOM 1360  C CG  . ASN A 1 190 ? 163.838 -13.573 21.458  1.000 35.410  ? 207 ASN AAA CG  1 
ATOM 1361  O OD1 . ASN A 1 190 ? 164.121 -12.855 20.497  1.000 36.400  ? 207 ASN AAA OD1 1 
ATOM 1362  N ND2 . ASN A 1 190 ? 162.660 -14.181 21.598  1.000 32.700  ? 207 ASN AAA ND2 1 
ATOM 1363  N N   . GLU A 1 191 ? 168.389 -15.066 22.897  1.000 35.030  ? 208 GLU AAA N   1 
ATOM 1364  C CA  . GLU A 1 191 ? 169.671 -14.876 23.638  1.000 33.480  ? 208 GLU AAA CA  1 
ATOM 1365  C C   . GLU A 1 191 ? 170.135 -13.420 23.437  1.000 34.950  ? 208 GLU AAA C   1 
ATOM 1366  O O   . GLU A 1 191 ? 170.563 -12.785 24.416  1.000 32.520  ? 208 GLU AAA O   1 
ATOM 1367  C CB  . GLU A 1 191 ? 170.736 -15.883 23.170  1.000 30.750  ? 208 GLU AAA CB  1 
ATOM 1368  N N   . ASN A 1 192 ? 169.998 -12.895 22.213  1.000 36.300  ? 209 ASN AAA N   1 
ATOM 1369  C CA  . ASN A 1 192 ? 170.630 -11.629 21.758  1.000 35.700  ? 209 ASN AAA CA  1 
ATOM 1370  C C   . ASN A 1 192 ? 169.618 -10.475 21.802  1.000 34.550  ? 209 ASN AAA C   1 
ATOM 1371  O O   . ASN A 1 192 ? 169.890 -9.425  21.210  1.000 34.120  ? 209 ASN AAA O   1 
ATOM 1372  C CB  . ASN A 1 192 ? 171.218 -11.811 20.358  1.000 37.130  ? 209 ASN AAA CB  1 
ATOM 1373  C CG  . ASN A 1 192 ? 172.221 -10.736 20.003  1.000 40.560  ? 209 ASN AAA CG  1 
ATOM 1374  O OD1 . ASN A 1 192 ? 172.797 -10.085 20.881  1.000 35.380  ? 209 ASN AAA OD1 1 
ATOM 1375  N ND2 . ASN A 1 192 ? 172.415 -10.530 18.707  1.000 43.170  ? 209 ASN AAA ND2 1 
ATOM 1376  N N   . THR A 1 193 ? 168.501 -10.642 22.504  1.000 36.480  ? 210 THR AAA N   1 
ATOM 1377  C CA  . THR A 1 193 ? 167.458 -9.601  22.671  1.000 38.020  ? 210 THR AAA CA  1 
ATOM 1378  C C   . THR A 1 193 ? 167.111 -9.479  24.165  1.000 41.190  ? 210 THR AAA C   1 
ATOM 1379  O O   . THR A 1 193 ? 167.288 -10.471 24.908  1.000 44.440  ? 210 THR AAA O   1 
ATOM 1380  C CB  . THR A 1 193 ? 166.244 -9.929  21.800  1.000 38.250  ? 210 THR AAA CB  1 
ATOM 1381  O OG1 . THR A 1 193 ? 166.552 -9.752  20.418  1.000 38.990  ? 210 THR AAA OG1 1 
ATOM 1382  C CG2 . THR A 1 193 ? 165.065 -9.048  22.126  1.000 41.220  ? 210 THR AAA CG2 1 
ATOM 1383  N N   . ARG A 1 194 ? 166.691 -8.292  24.602  1.000 38.660  ? 211 ARG AAA N   1 
ATOM 1384  C CA  . ARG A 1 194 ? 166.107 -8.056  25.946  1.000 37.000  ? 211 ARG AAA CA  1 
ATOM 1385  C C   . ARG A 1 194 ? 164.672 -7.605  25.715  1.000 38.100  ? 211 ARG AAA C   1 
ATOM 1386  O O   . ARG A 1 194 ? 164.503 -6.556  25.091  1.000 41.350  ? 211 ARG AAA O   1 
ATOM 1387  C CB  . ARG A 1 194 ? 166.871 -6.975  26.710  1.000 36.950  ? 211 ARG AAA CB  1 
ATOM 1388  C CG  . ARG A 1 194 ? 168.369 -7.202  26.764  1.000 37.920  ? 211 ARG AAA CG  1 
ATOM 1389  C CD  . ARG A 1 194 ? 168.693 -8.417  27.585  1.000 41.350  ? 211 ARG AAA CD  1 
ATOM 1390  N NE  . ARG A 1 194 ? 170.135 -8.587  27.641  1.000 42.730  ? 211 ARG AAA NE  1 
ATOM 1391  C CZ  . ARG A 1 194 ? 170.837 -9.307  26.787  1.000 42.570  ? 211 ARG AAA CZ  1 
ATOM 1392  N NH1 . ARG A 1 194 ? 170.249 -9.973  25.813  1.000 42.660  ? 211 ARG AAA NH1 1 
ATOM 1393  N NH2 . ARG A 1 194 ? 172.140 -9.376  26.928  1.000 44.680  ? 211 ARG AAA NH2 1 
ATOM 1394  N N   . TYR A 1 195 ? 163.684 -8.403  26.113  1.000 38.130  ? 212 TYR AAA N   1 
ATOM 1395  C CA  . TYR A 1 195 ? 162.254 -8.110  25.851  1.000 35.230  ? 212 TYR AAA CA  1 
ATOM 1396  C C   . TYR A 1 195 ? 161.533 -7.982  27.187  1.000 33.510  ? 212 TYR AAA C   1 
ATOM 1397  O O   . TYR A 1 195 ? 161.907 -8.646  28.155  1.000 38.300  ? 212 TYR AAA O   1 
ATOM 1398  C CB  . TYR A 1 195 ? 161.648 -9.156  24.913  1.000 33.620  ? 212 TYR AAA CB  1 
ATOM 1399  C CG  . TYR A 1 195 ? 161.420 -10.530 25.485  1.000 33.700  ? 212 TYR AAA CG  1 
ATOM 1400  C CD1 . TYR A 1 195 ? 160.300 -10.826 26.237  1.000 33.950  ? 212 TYR AAA CD1 1 
ATOM 1401  C CD2 . TYR A 1 195 ? 162.318 -11.549 25.254  1.000 35.280  ? 212 TYR AAA CD2 1 
ATOM 1402  C CE1 . TYR A 1 195 ? 160.077 -12.092 26.753  1.000 34.470  ? 212 TYR AAA CE1 1 
ATOM 1403  C CE2 . TYR A 1 195 ? 162.113 -12.820 25.766  1.000 38.090  ? 212 TYR AAA CE2 1 
ATOM 1404  C CZ  . TYR A 1 195 ? 160.987 -13.101 26.517  1.000 36.760  ? 212 TYR AAA CZ  1 
ATOM 1405  O OH  . TYR A 1 195 ? 160.795 -14.374 26.991  1.000 40.640  ? 212 TYR AAA OH  1 
ATOM 1406  N N   . PHE A 1 196 ? 160.542 -7.104  27.217  1.000 30.020  ? 213 PHE AAA N   1 
ATOM 1407  C CA  . PHE A 1 196 ? 159.688 -6.795  28.394  1.000 27.010  ? 213 PHE AAA CA  1 
ATOM 1408  C C   . PHE A 1 196 ? 158.303 -6.469  27.895  1.000 27.420  ? 213 PHE AAA C   1 
ATOM 1409  O O   . PHE A 1 196 ? 158.174 -5.611  27.003  1.000 32.000  ? 213 PHE AAA O   1 
ATOM 1410  C CB  . PHE A 1 196 ? 160.216 -5.575  29.148  1.000 25.200  ? 213 PHE AAA CB  1 
ATOM 1411  C CG  . PHE A 1 196 ? 161.706 -5.518  29.342  1.000 24.550  ? 213 PHE AAA CG  1 
ATOM 1412  C CD1 . PHE A 1 196 ? 162.538 -5.021  28.343  1.000 25.530  ? 213 PHE AAA CD1 1 
ATOM 1413  C CD2 . PHE A 1 196 ? 162.285 -5.914  30.530  1.000 22.700  ? 213 PHE AAA CD2 1 
ATOM 1414  C CE1 . PHE A 1 196 ? 163.906 -4.929  28.531  1.000 24.360  ? 213 PHE AAA CE1 1 
ATOM 1415  C CE2 . PHE A 1 196 ? 163.655 -5.843  30.704  1.000 23.440  ? 213 PHE AAA CE2 1 
ATOM 1416  C CZ  . PHE A 1 196 ? 164.457 -5.322  29.718  1.000 23.640  ? 213 PHE AAA CZ  1 
ATOM 1417  N N   . GLY A 1 197 ? 157.288 -7.118  28.449  1.000 26.500  ? 214 GLY AAA N   1 
ATOM 1418  C CA  . GLY A 1 197 ? 155.900 -6.808  28.103  1.000 26.090  ? 214 GLY AAA CA  1 
ATOM 1419  C C   . GLY A 1 197 ? 154.939 -7.174  29.217  1.000 26.130  ? 214 GLY AAA C   1 
ATOM 1420  O O   . GLY A 1 197 ? 155.308 -7.960  30.102  1.000 26.310  ? 214 GLY AAA O   1 
ATOM 1421  N N   . THR A 1 198 ? 153.732 -6.632  29.148  1.000 24.840  ? 215 THR AAA N   1 
ATOM 1422  C CA  . THR A 1 198 ? 152.655 -6.906  30.115  1.000 23.660  ? 215 THR AAA CA  1 
ATOM 1423  C C   . THR A 1 198 ? 151.329 -6.946  29.387  1.000 23.950  ? 215 THR AAA C   1 
ATOM 1424  O O   . THR A 1 198 ? 151.042 -6.002  28.684  1.000 22.950  ? 215 THR AAA O   1 
ATOM 1425  C CB  . THR A 1 198 ? 152.591 -5.830  31.189  1.000 22.870  ? 215 THR AAA CB  1 
ATOM 1426  O OG1 . THR A 1 198 ? 153.863 -5.823  31.831  1.000 22.790  ? 215 THR AAA OG1 1 
ATOM 1427  C CG2 . THR A 1 198 ? 151.472 -6.114  32.158  1.000 23.080  ? 215 THR AAA CG2 1 
ATOM 1428  N N   . LEU A 1 199 ? 150.582 -8.029  29.566  1.000 25.920  ? 216 LEU AAA N   1 
ATOM 1429  C CA  . LEU A 1 199 ? 149.159 -8.123  29.159  1.000 25.960  ? 216 LEU AAA CA  1 
ATOM 1430  C C   . LEU A 1 199 ? 148.308 -7.865  30.396  1.000 26.230  ? 216 LEU AAA C   1 
ATOM 1431  O O   . LEU A 1 199 ? 148.491 -8.589  31.369  1.000 27.280  ? 216 LEU AAA O   1 
ATOM 1432  C CB  . LEU A 1 199 ? 148.945 -9.544  28.620  1.000 25.730  ? 216 LEU AAA CB  1 
ATOM 1433  C CG  . LEU A 1 199 ? 147.555 -9.934  28.156  1.000 24.570  ? 216 LEU AAA CG  1 
ATOM 1434  C CD1 . LEU A 1 199 ? 146.664 -10.525 29.255  1.000 24.810  ? 216 LEU AAA CD1 1 
ATOM 1435  C CD2 . LEU A 1 199 ? 146.875 -8.777  27.466  1.000 24.450  ? 216 LEU AAA CD2 1 
ATOM 1436  N N   . THR A 1 200 ? 147.449 -6.853  30.347  1.000 26.080  ? 217 THR AAA N   1 
ATOM 1437  C CA  . THR A 1 200 ? 146.319 -6.659  31.289  1.000 25.180  ? 217 THR AAA CA  1 
ATOM 1438  C C   . THR A 1 200 ? 145.003 -6.852  30.531  1.000 25.110  ? 217 THR AAA C   1 
ATOM 1439  O O   . THR A 1 200 ? 144.717 -6.034  29.640  1.000 26.320  ? 217 THR AAA O   1 
ATOM 1440  C CB  . THR A 1 200 ? 146.387 -5.275  31.939  1.000 25.100  ? 217 THR AAA CB  1 
ATOM 1441  O OG1 . THR A 1 200 ? 147.710 -5.118  32.431  1.000 26.630  ? 217 THR AAA OG1 1 
ATOM 1442  C CG2 . THR A 1 200 ? 145.403 -5.134  33.067  1.000 25.580  ? 217 THR AAA CG2 1 
ATOM 1443  N N   . GLY A 1 201 ? 144.247 -7.897  30.867  1.000 25.760  ? 218 GLY AAA N   1 
ATOM 1444  C CA  . GLY A 1 201 ? 142.965 -8.231  30.215  1.000 26.430  ? 218 GLY AAA CA  1 
ATOM 1445  C C   . GLY A 1 201 ? 141.791 -7.742  31.047  1.000 26.000  ? 218 GLY AAA C   1 
ATOM 1446  O O   . GLY A 1 201 ? 141.929 -7.677  32.261  1.000 26.750  ? 218 GLY AAA O   1 
ATOM 1447  N N   . GLY A 1 202 ? 140.669 -7.417  30.406  1.000 26.540  ? 219 GLY AAA N   1 
ATOM 1448  C CA  . GLY A 1 202 ? 139.450 -6.944  31.084  1.000 26.960  ? 219 GLY AAA CA  1 
ATOM 1449  C C   . GLY A 1 202 ? 138.908 -5.710  30.386  1.000 28.650  ? 219 GLY AAA C   1 
ATOM 1450  O O   . GLY A 1 202 ? 139.714 -4.803  30.056  1.000 25.980  ? 219 GLY AAA O   1 
ATOM 1451  N N   . GLU A 1 203 ? 137.585 -5.655  30.201  1.000 30.420  ? 220 GLU AAA N   1 
ATOM 1452  C CA  . GLU A 1 203 ? 136.918 -4.606  29.394  1.000 30.600  ? 220 GLU AAA CA  1 
ATOM 1453  C C   . GLU A 1 203 ? 137.025 -3.264  30.122  1.000 30.530  ? 220 GLU AAA C   1 
ATOM 1454  O O   . GLU A 1 203 ? 136.995 -2.243  29.425  1.000 36.730  ? 220 GLU AAA O   1 
ATOM 1455  C CB  . GLU A 1 203 ? 135.480 -4.995  29.023  1.000 31.170  ? 220 GLU AAA CB  1 
ATOM 1456  C CG  . GLU A 1 203 ? 134.540 -5.262  30.178  1.000 32.900  ? 220 GLU AAA CG  1 
ATOM 1457  C CD  . GLU A 1 203 ? 134.410 -6.723  30.569  1.000 34.680  ? 220 GLU AAA CD  1 
ATOM 1458  O OE1 . GLU A 1 203 ? 135.453 -7.392  30.579  1.000 36.070  ? 220 GLU AAA OE1 1 
ATOM 1459  O OE2 . GLU A 1 203 ? 133.265 -7.191  30.864  1.000 34.020  ? 220 GLU AAA OE2 1 
ATOM 1460  N N   . ASN A 1 204 ? 137.213 -3.260  31.446  1.000 28.160  ? 221 ASN AAA N   1 
ATOM 1461  C CA  . ASN A 1 204 ? 137.162 -2.019  32.264  1.000 26.200  ? 221 ASN AAA CA  1 
ATOM 1462  C C   . ASN A 1 204 ? 138.553 -1.676  32.817  1.000 25.140  ? 221 ASN AAA C   1 
ATOM 1463  O O   . ASN A 1 204 ? 138.683 -0.699  33.578  1.000 22.060  ? 221 ASN AAA O   1 
ATOM 1464  C CB  . ASN A 1 204 ? 136.112 -2.179  33.357  1.000 26.210  ? 221 ASN AAA CB  1 
ATOM 1465  C CG  . ASN A 1 204 ? 134.741 -2.320  32.752  1.000 26.250  ? 221 ASN AAA CG  1 
ATOM 1466  O OD1 . ASN A 1 204 ? 134.400 -1.552  31.857  1.000 25.470  ? 221 ASN AAA OD1 1 
ATOM 1467  N ND2 . ASN A 1 204 ? 133.989 -3.323  33.183  1.000 26.750  ? 221 ASN AAA ND2 1 
ATOM 1468  N N   . VAL A 1 205 ? 139.582 -2.419  32.423  1.000 24.090  ? 222 VAL AAA N   1 
ATOM 1469  C CA  . VAL A 1 205 ? 140.949 -2.154  32.942  1.000 23.200  ? 222 VAL AAA CA  1 
ATOM 1470  C C   . VAL A 1 205 ? 141.286 -0.701  32.624  1.000 22.170  ? 222 VAL AAA C   1 
ATOM 1471  O O   . VAL A 1 205 ? 141.338 -0.312  31.453  1.000 24.190  ? 222 VAL AAA O   1 
ATOM 1472  C CB  . VAL A 1 205 ? 142.001 -3.094  32.328  1.000 25.470  ? 222 VAL AAA CB  1 
ATOM 1473  C CG1 . VAL A 1 205 ? 143.391 -2.740  32.831  1.000 26.560  ? 222 VAL AAA CG1 1 
ATOM 1474  C CG2 . VAL A 1 205 ? 141.709 -4.562  32.608  1.000 26.300  ? 222 VAL AAA CG2 1 
ATOM 1475  N N   . PRO A 1 206 ? 141.576 0.136   33.640  1.000 20.580  ? 223 PRO AAA N   1 
ATOM 1476  C CA  . PRO A 1 206 ? 142.053 1.493   33.421  1.000 20.450  ? 223 PRO AAA CA  1 
ATOM 1477  C C   . PRO A 1 206 ? 143.475 1.535   32.889  1.000 19.790  ? 223 PRO AAA C   1 
ATOM 1478  O O   . PRO A 1 206 ? 144.353 0.905   33.467  1.000 18.550  ? 223 PRO AAA O   1 
ATOM 1479  C CB  . PRO A 1 206 ? 142.040 2.109   34.818  1.000 21.390  ? 223 PRO AAA CB  1 
ATOM 1480  C CG  . PRO A 1 206 ? 142.334 0.936   35.691  1.000 22.680  ? 223 PRO AAA CG  1 
ATOM 1481  C CD  . PRO A 1 206 ? 141.529 -0.181  35.062  1.000 22.380  ? 223 PRO AAA CD  1 
ATOM 1482  N N   . PRO A 1 207 ? 143.720 2.294   31.792  1.000 21.040  ? 224 PRO AAA N   1 
ATOM 1483  C CA  . PRO A 1 207 ? 145.066 2.624   31.350  1.000 21.670  ? 224 PRO AAA CA  1 
ATOM 1484  C C   . PRO A 1 207 ? 145.813 3.332   32.477  1.000 22.030  ? 224 PRO AAA C   1 
ATOM 1485  O O   . PRO A 1 207 ? 145.233 4.155   33.147  1.000 22.680  ? 224 PRO AAA O   1 
ATOM 1486  C CB  . PRO A 1 207 ? 144.894 3.606   30.179  1.000 21.870  ? 224 PRO AAA CB  1 
ATOM 1487  C CG  . PRO A 1 207 ? 143.471 3.361   29.698  1.000 22.400  ? 224 PRO AAA CG  1 
ATOM 1488  C CD  . PRO A 1 207 ? 142.710 2.943   30.940  1.000 22.090  ? 224 PRO AAA CD  1 
ATOM 1489  N N   . VAL A 1 208 ? 147.071 2.951   32.667  1.000 21.930  ? 225 VAL AAA N   1 
ATOM 1490  C CA  . VAL A 1 208 ? 148.001 3.591   33.627  1.000 20.630  ? 225 VAL AAA CA  1 
ATOM 1491  C C   . VAL A 1 208 ? 149.340 3.730   32.933  1.000 21.930  ? 225 VAL AAA C   1 
ATOM 1492  O O   . VAL A 1 208 ? 150.089 2.763   32.905  1.000 22.690  ? 225 VAL AAA O   1 
ATOM 1493  C CB  . VAL A 1 208 ? 148.122 2.750   34.887  1.000 20.000  ? 225 VAL AAA CB  1 
ATOM 1494  C CG1 . VAL A 1 208 ? 149.229 3.264   35.785  1.000 20.210  ? 225 VAL AAA CG1 1 
ATOM 1495  C CG2 . VAL A 1 208 ? 146.779 2.708   35.594  1.000 20.720  ? 225 VAL AAA CG2 1 
ATOM 1496  N N   . LEU A 1 209 ? 149.608 4.913   32.402  1.000 24.270  ? 226 LEU AAA N   1 
ATOM 1497  C CA  . LEU A 1 209 ? 150.802 5.192   31.579  1.000 23.930  ? 226 LEU AAA CA  1 
ATOM 1498  C C   . LEU A 1 209 ? 151.633 6.256   32.284  1.000 25.280  ? 226 LEU AAA C   1 
ATOM 1499  O O   . LEU A 1 209 ? 151.142 7.379   32.440  1.000 25.620  ? 226 LEU AAA O   1 
ATOM 1500  C CB  . LEU A 1 209 ? 150.267 5.623   30.218  1.000 23.180  ? 226 LEU AAA CB  1 
ATOM 1501  C CG  . LEU A 1 209 ? 149.328 4.593   29.593  1.000 23.330  ? 226 LEU AAA CG  1 
ATOM 1502  C CD1 . LEU A 1 209 ? 148.716 5.112   28.310  1.000 24.450  ? 226 LEU AAA CD1 1 
ATOM 1503  C CD2 . LEU A 1 209 ? 150.075 3.293   29.348  1.000 22.520  ? 226 LEU AAA CD2 1 
ATOM 1504  N N   . HIS A 1 210 ? 152.817 5.869   32.760  1.000 27.600  ? 227 HIS AAA N   1 
ATOM 1505  C CA  . HIS A 1 210 ? 153.805 6.790   33.378  1.000 30.350  ? 227 HIS AAA CA  1 
ATOM 1506  C C   . HIS A 1 210 ? 154.735 7.316   32.285  1.000 28.290  ? 227 HIS AAA C   1 
ATOM 1507  O O   . HIS A 1 210 ? 155.072 6.563   31.364  1.000 28.920  ? 227 HIS AAA O   1 
ATOM 1508  C CB  . HIS A 1 210 ? 154.567 6.107   34.525  1.000 33.930  ? 227 HIS AAA CB  1 
ATOM 1509  C CG  . HIS A 1 210 ? 153.673 5.438   35.525  1.000 37.610  ? 227 HIS AAA CG  1 
ATOM 1510  N ND1 . HIS A 1 210 ? 152.907 6.143   36.438  1.000 35.670  ? 227 HIS AAA ND1 1 
ATOM 1511  C CD2 . HIS A 1 210 ? 153.414 4.125   35.752  1.000 40.370  ? 227 HIS AAA CD2 1 
ATOM 1512  C CE1 . HIS A 1 210 ? 152.235 5.294   37.197  1.000 36.080  ? 227 HIS AAA CE1 1 
ATOM 1513  N NE2 . HIS A 1 210 ? 152.527 4.040   36.795  1.000 35.950  ? 227 HIS AAA NE2 1 
ATOM 1514  N N   . ILE A 1 211 ? 155.118 8.579   32.376  1.000 29.410  ? 228 ILE AAA N   1 
ATOM 1515  C CA  . ILE A 1 211 ? 156.102 9.211   31.458  1.000 30.690  ? 228 ILE AAA CA  1 
ATOM 1516  C C   . ILE A 1 211 ? 157.186 9.868   32.318  1.000 30.430  ? 228 ILE AAA C   1 
ATOM 1517  O O   . ILE A 1 211 ? 156.853 10.439  33.383  1.000 28.050  ? 228 ILE AAA O   1 
ATOM 1518  C CB  . ILE A 1 211 ? 155.382 10.196  30.520  1.000 32.120  ? 228 ILE AAA CB  1 
ATOM 1519  C CG1 . ILE A 1 211 ? 154.816 11.412  31.261  1.000 32.620  ? 228 ILE AAA CG1 1 
ATOM 1520  C CG2 . ILE A 1 211 ? 154.284 9.484   29.734  1.000 33.000  ? 228 ILE AAA CG2 1 
ATOM 1521  C CD1 . ILE A 1 211 ? 154.162 12.425  30.357  1.000 34.080  ? 228 ILE AAA CD1 1 
ATOM 1522  N N   . THR A 1 212 ? 158.444 9.760   31.907  1.000 30.710  ? 229 THR AAA N   1 
ATOM 1523  C CA  . THR A 1 212 ? 159.565 10.454  32.586  1.000 32.430  ? 229 THR AAA CA  1 
ATOM 1524  C C   . THR A 1 212 ? 160.830 10.328  31.755  1.000 32.390  ? 229 THR AAA C   1 
ATOM 1525  O O   . THR A 1 212 ? 161.041 9.249   31.148  1.000 39.200  ? 229 THR AAA O   1 
ATOM 1526  C CB  . THR A 1 212 ? 159.800 9.887   33.993  1.000 35.170  ? 229 THR AAA CB  1 
ATOM 1527  O OG1 . THR A 1 212 ? 160.725 10.747  34.670  1.000 39.210  ? 229 THR AAA OG1 1 
ATOM 1528  C CG2 . THR A 1 212 ? 160.343 8.474   33.973  1.000 34.190  ? 229 THR AAA CG2 1 
ATOM 1529  N N   . ASN A 1 213 ? 161.666 11.359  31.762  1.000 31.150  ? 230 ASN AAA N   1 
ATOM 1530  C CA  . ASN A 1 213 ? 162.984 11.270  31.089  1.000 32.060  ? 230 ASN AAA CA  1 
ATOM 1531  C C   . ASN A 1 213 ? 164.072 10.911  32.116  1.000 31.300  ? 230 ASN AAA C   1 
ATOM 1532  O O   . ASN A 1 213 ? 165.237 11.162  31.830  1.000 30.880  ? 230 ASN AAA O   1 
ATOM 1533  C CB  . ASN A 1 213 ? 163.267 12.544  30.289  1.000 31.080  ? 230 ASN AAA CB  1 
ATOM 1534  C CG  . ASN A 1 213 ? 163.282 13.786  31.146  1.000 29.660  ? 230 ASN AAA CG  1 
ATOM 1535  O OD1 . ASN A 1 213 ? 163.005 13.723  32.337  1.000 30.020  ? 230 ASN AAA OD1 1 
ATOM 1536  N ND2 . ASN A 1 213 ? 163.542 14.927  30.529  1.000 28.350  ? 230 ASN AAA ND2 1 
ATOM 1537  N N   . THR A 1 214 ? 163.721 10.335  33.266  1.000 31.290  ? 231 THR AAA N   1 
ATOM 1538  C CA  . THR A 1 214 ? 164.667 10.088  34.393  1.000 28.280  ? 231 THR AAA CA  1 
ATOM 1539  C C   . THR A 1 214 ? 164.906 8.593   34.608  1.000 28.910  ? 231 THR AAA C   1 
ATOM 1540  O O   . THR A 1 214 ? 165.724 8.254   35.444  1.000 27.820  ? 231 THR AAA O   1 
ATOM 1541  C CB  . THR A 1 214 ? 164.140 10.692  35.692  1.000 27.730  ? 231 THR AAA CB  1 
ATOM 1542  O OG1 . THR A 1 214 ? 162.906 10.047  35.983  1.000 29.150  ? 231 THR AAA OG1 1 
ATOM 1543  C CG2 . THR A 1 214 ? 163.903 12.174  35.604  1.000 28.980  ? 231 THR AAA CG2 1 
ATOM 1544  N N   . ALA A 1 215 ? 164.214 7.727   33.877  1.000 32.830  ? 232 ALA AAA N   1 
ATOM 1545  C CA  . ALA A 1 215 ? 164.205 6.271   34.134  1.000 33.130  ? 232 ALA AAA CA  1 
ATOM 1546  C C   . ALA A 1 215 ? 165.023 5.554   33.071  1.000 31.990  ? 232 ALA AAA C   1 
ATOM 1547  O O   . ALA A 1 215 ? 164.527 5.485   31.937  1.000 38.120  ? 232 ALA AAA O   1 
ATOM 1548  C CB  . ALA A 1 215 ? 162.781 5.785   34.128  1.000 35.750  ? 232 ALA AAA CB  1 
ATOM 1549  N N   . THR A 1 216 ? 166.198 5.040   33.422  1.000 29.730  ? 233 THR AAA N   1 
ATOM 1550  C CA  . THR A 1 216 ? 167.042 4.216   32.515  1.000 31.940  ? 233 THR AAA CA  1 
ATOM 1551  C C   . THR A 1 216 ? 166.865 2.740   32.866  1.000 30.580  ? 233 THR AAA C   1 
ATOM 1552  O O   . THR A 1 216 ? 166.745 2.466   34.042  1.000 35.650  ? 233 THR AAA O   1 
ATOM 1553  C CB  . THR A 1 216 ? 168.511 4.643   32.597  1.000 34.210  ? 233 THR AAA CB  1 
ATOM 1554  O OG1 . THR A 1 216 ? 168.542 6.061   32.428  1.000 39.270  ? 233 THR AAA OG1 1 
ATOM 1555  C CG2 . THR A 1 216 ? 169.389 3.977   31.560  1.000 32.680  ? 233 THR AAA CG2 1 
ATOM 1556  N N   . THR A 1 217 ? 166.824 1.851   31.872  1.000 31.230  ? 234 THR AAA N   1 
ATOM 1557  C CA  . THR A 1 217 ? 166.769 0.369   32.031  1.000 31.530  ? 234 THR AAA CA  1 
ATOM 1558  C C   . THR A 1 217 ? 168.047 -0.238  31.453  1.000 32.040  ? 234 THR AAA C   1 
ATOM 1559  O O   . THR A 1 217 ? 168.375 0.089   30.302  1.000 33.870  ? 234 THR AAA O   1 
ATOM 1560  C CB  . THR A 1 217 ? 165.588 -0.239  31.271  1.000 29.960  ? 234 THR AAA CB  1 
ATOM 1561  O OG1 . THR A 1 217 ? 164.387 0.396   31.708  1.000 26.020  ? 234 THR AAA OG1 1 
ATOM 1562  C CG2 . THR A 1 217 ? 165.483 -1.736  31.459  1.000 29.930  ? 234 THR AAA CG2 1 
ATOM 1563  N N   . VAL A 1 218 ? 168.753 -1.081  32.202  1.000 31.760  ? 235 VAL AAA N   1 
ATOM 1564  C CA  . VAL A 1 218 ? 170.071 -1.614  31.749  1.000 32.540  ? 235 VAL AAA CA  1 
ATOM 1565  C C   . VAL A 1 218 ? 169.820 -2.868  30.912  1.000 32.880  ? 235 VAL AAA C   1 
ATOM 1566  O O   . VAL A 1 218 ? 168.927 -3.627  31.273  1.000 36.420  ? 235 VAL AAA O   1 
ATOM 1567  C CB  . VAL A 1 218 ? 170.985 -1.877  32.954  1.000 32.840  ? 235 VAL AAA CB  1 
ATOM 1568  C CG1 . VAL A 1 218 ? 172.134 -2.808  32.618  1.000 34.180  ? 235 VAL AAA CG1 1 
ATOM 1569  C CG2 . VAL A 1 218 ? 171.512 -0.570  33.507  1.000 33.170  ? 235 VAL AAA CG2 1 
ATOM 1570  N N   . LEU A 1 219 ? 170.579 -3.071  29.839  1.000 32.420  ? 236 LEU AAA N   1 
ATOM 1571  C CA  . LEU A 1 219 ? 170.336 -4.170  28.867  1.000 34.330  ? 236 LEU AAA CA  1 
ATOM 1572  C C   . LEU A 1 219 ? 171.398 -5.263  29.004  1.000 36.270  ? 236 LEU AAA C   1 
ATOM 1573  O O   . LEU A 1 219 ? 171.330 -6.252  28.255  1.000 35.900  ? 236 LEU AAA O   1 
ATOM 1574  C CB  . LEU A 1 219 ? 170.327 -3.571  27.461  1.000 33.100  ? 236 LEU AAA CB  1 
ATOM 1575  C CG  . LEU A 1 219 ? 169.237 -2.529  27.232  1.000 32.290  ? 236 LEU AAA CG  1 
ATOM 1576  C CD1 . LEU A 1 219 ? 169.415 -1.840  25.903  1.000 33.110  ? 236 LEU AAA CD1 1 
ATOM 1577  C CD2 . LEU A 1 219 ? 167.872 -3.160  27.294  1.000 31.720  ? 236 LEU AAA CD2 1 
ATOM 1578  N N   . LEU A 1 220 ? 172.310 -5.132  29.966  1.000 38.900  ? 237 LEU AAA N   1 
ATOM 1579  C CA  . LEU A 1 220 ? 173.367 -6.138  30.253  1.000 42.840  ? 237 LEU AAA CA  1 
ATOM 1580  C C   . LEU A 1 220 ? 172.735 -7.355  30.928  1.000 41.500  ? 237 LEU AAA C   1 
ATOM 1581  O O   . LEU A 1 220 ? 171.801 -7.168  31.721  1.000 40.670  ? 237 LEU AAA O   1 
ATOM 1582  C CB  . LEU A 1 220 ? 174.444 -5.529  31.157  1.000 44.720  ? 237 LEU AAA CB  1 
ATOM 1583  C CG  . LEU A 1 220 ? 175.083 -4.231  30.672  1.000 45.670  ? 237 LEU AAA CG  1 
ATOM 1584  C CD1 . LEU A 1 220 ? 176.153 -3.786  31.648  1.000 48.430  ? 237 LEU AAA CD1 1 
ATOM 1585  C CD2 . LEU A 1 220 ? 175.673 -4.394  29.279  1.000 47.420  ? 237 LEU AAA CD2 1 
ATOM 1586  N N   . ASP A 1 221 ? 173.259 -8.544  30.633  1.000 41.670  ? 238 ASP AAA N   1 
ATOM 1587  C CA  . ASP A 1 221 ? 172.783 -9.836  31.188  1.000 43.910  ? 238 ASP AAA CA  1 
ATOM 1588  C C   . ASP A 1 221 ? 173.596 -10.159 32.442  1.000 43.460  ? 238 ASP AAA C   1 
ATOM 1589  O O   . ASP A 1 221 ? 174.414 -9.306  32.837  1.000 43.240  ? 238 ASP AAA O   1 
ATOM 1590  C CB  . ASP A 1 221 ? 172.874 -10.948 30.137  1.000 44.720  ? 238 ASP AAA CB  1 
ATOM 1591  C CG  . ASP A 1 221 ? 174.273 -11.328 29.702  1.000 42.410  ? 238 ASP AAA CG  1 
ATOM 1592  O OD1 . ASP A 1 221 ? 175.238 -10.743 30.220  1.000 43.540  ? 238 ASP AAA OD1 1 
ATOM 1593  O OD2 . ASP A 1 221 ? 174.369 -12.211 28.851  1.000 42.350  ? 238 ASP AAA OD2 1 
ATOM 1594  N N   . GLU A 1 222 ? 173.378 -11.343 33.025  1.000 46.600  ? 239 GLU AAA N   1 
ATOM 1595  C CA  . GLU A 1 222 ? 174.049 -11.801 34.280  1.000 50.980  ? 239 GLU AAA CA  1 
ATOM 1596  C C   . GLU A 1 222 ? 175.575 -11.717 34.106  1.000 51.850  ? 239 GLU AAA C   1 
ATOM 1597  O O   . GLU A 1 222 ? 176.234 -11.589 35.130  1.000 57.920  ? 239 GLU AAA O   1 
ATOM 1598  C CB  . GLU A 1 222 ? 173.563 -13.177 34.763  1.000 52.620  ? 239 GLU AAA CB  1 
ATOM 1599  C CG  . GLU A 1 222 ? 173.338 -14.231 33.682  1.000 58.970  ? 239 GLU AAA CG  1 
ATOM 1600  C CD  . GLU A 1 222 ? 171.923 -14.284 33.100  1.000 61.270  ? 239 GLU AAA CD  1 
ATOM 1601  O OE1 . GLU A 1 222 ? 171.142 -15.191 33.469  1.000 74.500  ? 239 GLU AAA OE1 1 
ATOM 1602  O OE2 . GLU A 1 222 ? 171.598 -13.426 32.269  1.000 49.340  ? 239 GLU AAA OE2 1 
ATOM 1603  N N   . PHE A 1 223 ? 176.106 -11.747 32.875  1.000 54.140  ? 240 PHE AAA N   1 
ATOM 1604  C CA  . PHE A 1 223 ? 177.558 -11.710 32.556  1.000 54.590  ? 240 PHE AAA CA  1 
ATOM 1605  C C   . PHE A 1 223 ? 178.011 -10.321 32.083  1.000 55.240  ? 240 PHE AAA C   1 
ATOM 1606  O O   . PHE A 1 223 ? 179.100 -10.226 31.534  1.000 66.370  ? 240 PHE AAA O   1 
ATOM 1607  C CB  . PHE A 1 223 ? 177.888 -12.717 31.450  1.000 58.370  ? 240 PHE AAA CB  1 
ATOM 1608  C CG  . PHE A 1 223 ? 177.523 -14.154 31.734  1.000 69.690  ? 240 PHE AAA CG  1 
ATOM 1609  C CD1 . PHE A 1 223 ? 176.215 -14.601 31.592  1.000 76.070  ? 240 PHE AAA CD1 1 
ATOM 1610  C CD2 . PHE A 1 223 ? 178.498 -15.076 32.099  1.000 80.130  ? 240 PHE AAA CD2 1 
ATOM 1611  C CE1 . PHE A 1 223 ? 175.884 -15.924 31.858  1.000 78.000  ? 240 PHE AAA CE1 1 
ATOM 1612  C CE2 . PHE A 1 223 ? 178.170 -16.401 32.341  1.000 85.270  ? 240 PHE AAA CE2 1 
ATOM 1613  C CZ  . PHE A 1 223 ? 176.863 -16.823 32.220  1.000 85.740  ? 240 PHE AAA CZ  1 
ATOM 1614  N N   . GLY A 1 224 ? 177.203 -9.276  32.240  1.000 56.190  ? 241 GLY AAA N   1 
ATOM 1615  C CA  . GLY A 1 224 ? 177.594 -7.888  31.903  1.000 53.380  ? 241 GLY AAA CA  1 
ATOM 1616  C C   . GLY A 1 224 ? 177.748 -7.634  30.407  1.000 50.460  ? 241 GLY AAA C   1 
ATOM 1617  O O   . GLY A 1 224 ? 178.425 -6.641  30.034  1.000 53.600  ? 241 GLY AAA O   1 
ATOM 1618  N N   . VAL A 1 225 ? 177.116 -8.466  29.574  1.000 49.220  ? 242 VAL AAA N   1 
ATOM 1619  C CA  . VAL A 1 225 ? 177.066 -8.326  28.089  1.000 48.690  ? 242 VAL AAA CA  1 
ATOM 1620  C C   . VAL A 1 225 ? 175.651 -7.912  27.671  1.000 47.560  ? 242 VAL AAA C   1 
ATOM 1621  O O   . VAL A 1 225 ? 174.696 -8.637  28.019  1.000 49.290  ? 242 VAL AAA O   1 
ATOM 1622  C CB  . VAL A 1 225 ? 177.443 -9.644  27.391  1.000 49.420  ? 242 VAL AAA CB  1 
ATOM 1623  C CG1 . VAL A 1 225 ? 177.537 -9.460  25.883  1.000 49.690  ? 242 VAL AAA CG1 1 
ATOM 1624  C CG2 . VAL A 1 225 ? 178.721 -10.237 27.955  1.000 48.060  ? 242 VAL AAA CG2 1 
ATOM 1625  N N   . GLY A 1 226 ? 175.528 -6.816  26.922  1.000 46.780  ? 243 GLY AAA N   1 
ATOM 1626  C CA  . GLY A 1 226 ? 174.264 -6.375  26.306  1.000 44.690  ? 243 GLY AAA CA  1 
ATOM 1627  C C   . GLY A 1 226 ? 174.026 -7.102  24.994  1.000 43.940  ? 243 GLY AAA C   1 
ATOM 1628  O O   . GLY A 1 226 ? 174.843 -7.912  24.584  1.000 45.820  ? 243 GLY AAA O   1 
ATOM 1629  N N   . PRO A 1 227 ? 172.887 -6.871  24.315  1.000 46.030  ? 244 PRO AAA N   1 
ATOM 1630  C CA  . PRO A 1 227 ? 172.708 -7.352  22.948  1.000 48.170  ? 244 PRO AAA CA  1 
ATOM 1631  C C   . PRO A 1 227 ? 173.851 -6.875  22.044  1.000 48.780  ? 244 PRO AAA C   1 
ATOM 1632  O O   . PRO A 1 227 ? 174.331 -5.771  22.239  1.000 44.350  ? 244 PRO AAA O   1 
ATOM 1633  C CB  . PRO A 1 227 ? 171.368 -6.741  22.517  1.000 51.040  ? 244 PRO AAA CB  1 
ATOM 1634  C CG  . PRO A 1 227 ? 170.622 -6.542  23.822  1.000 49.160  ? 244 PRO AAA CG  1 
ATOM 1635  C CD  . PRO A 1 227 ? 171.694 -6.188  24.831  1.000 47.230  ? 244 PRO AAA CD  1 
ATOM 1636  N N   . LEU A 1 228 ? 174.281 -7.742  21.127  1.000 50.620  ? 245 LEU AAA N   1 
ATOM 1637  C CA  . LEU A 1 228 ? 175.370 -7.472  20.143  1.000 46.930  ? 245 LEU AAA CA  1 
ATOM 1638  C C   . LEU A 1 228 ? 174.757 -7.360  18.747  1.000 42.490  ? 245 LEU AAA C   1 
ATOM 1639  O O   . LEU A 1 228 ? 174.078 -8.299  18.315  1.000 38.080  ? 245 LEU AAA O   1 
ATOM 1640  C CB  . LEU A 1 228 ? 176.422 -8.586  20.199  1.000 46.240  ? 245 LEU AAA CB  1 
ATOM 1641  C CG  . LEU A 1 228 ? 177.160 -8.727  21.526  1.000 46.480  ? 245 LEU AAA CG  1 
ATOM 1642  C CD1 . LEU A 1 228 ? 178.174 -9.851  21.440  1.000 45.610  ? 245 LEU AAA CD1 1 
ATOM 1643  C CD2 . LEU A 1 228 ? 177.810 -7.402  21.906  1.000 48.480  ? 245 LEU AAA CD2 1 
ATOM 1644  N N   . CYS A 1 229 ? 174.975 -6.229  18.091  1.000 42.470  ? 246 CYS AAA N   1 
ATOM 1645  C CA  . CYS A 1 229 ? 174.288 -5.834  16.847  1.000 42.420  ? 246 CYS AAA CA  1 
ATOM 1646  C C   . CYS A 1 229 ? 174.953 -6.468  15.623  1.000 43.320  ? 246 CYS AAA C   1 
ATOM 1647  O O   . CYS A 1 229 ? 175.795 -5.797  14.999  1.000 44.950  ? 246 CYS AAA O   1 
ATOM 1648  C CB  . CYS A 1 229 ? 174.279 -4.320  16.751  1.000 42.280  ? 246 CYS AAA CB  1 
ATOM 1649  S SG  . CYS A 1 229 ? 173.268 -3.582  18.063  1.000 35.900  ? 246 CYS AAA SG  1 
ATOM 1650  N N   . LYS A 1 230 ? 174.550 -7.697  15.288  1.000 44.170  ? 247 LYS AAA N   1 
ATOM 1651  C CA  . LYS A 1 230 ? 174.921 -8.403  14.031  1.000 41.410  ? 247 LYS AAA CA  1 
ATOM 1652  C C   . LYS A 1 230 ? 174.623 -7.504  12.831  1.000 42.940  ? 247 LYS AAA C   1 
ATOM 1653  O O   . LYS A 1 230 ? 173.535 -6.941  12.781  1.000 49.480  ? 247 LYS AAA O   1 
ATOM 1654  C CB  . LYS A 1 230 ? 174.163 -9.725  13.934  1.000 41.390  ? 247 LYS AAA CB  1 
ATOM 1655  C CG  . LYS A 1 230 ? 174.658 -10.790 14.897  1.000 45.250  ? 247 LYS AAA CG  1 
ATOM 1656  C CD  . LYS A 1 230 ? 173.895 -12.096 14.836  1.000 49.420  ? 247 LYS AAA CD  1 
ATOM 1657  C CE  . LYS A 1 230 ? 174.363 -13.091 15.874  1.000 50.670  ? 247 LYS AAA CE  1 
ATOM 1658  N NZ  . LYS A 1 230 ? 173.705 -14.393 15.657  1.000 52.630  ? 247 LYS AAA NZ  1 
ATOM 1659  N N   . GLY A 1 231 ? 175.575 -7.371  11.909  1.000 47.330  ? 248 GLY AAA N   1 
ATOM 1660  C CA  . GLY A 1 231 ? 175.422 -6.610  10.653  1.000 47.010  ? 248 GLY AAA CA  1 
ATOM 1661  C C   . GLY A 1 231 ? 175.368 -5.118  10.904  1.000 48.390  ? 248 GLY AAA C   1 
ATOM 1662  O O   . GLY A 1 231 ? 174.861 -4.406  10.032  1.000 47.200  ? 248 GLY AAA O   1 
ATOM 1663  N N   . ASP A 1 232 ? 175.888 -4.657  12.049  1.000 52.240  ? 249 ASP AAA N   1 
ATOM 1664  C CA  . ASP A 1 232 ? 175.853 -3.228  12.452  1.000 57.740  ? 249 ASP AAA CA  1 
ATOM 1665  C C   . ASP A 1 232 ? 174.392 -2.734  12.451  1.000 56.720  ? 249 ASP AAA C   1 
ATOM 1666  O O   . ASP A 1 232 ? 174.144 -1.556  12.047  1.000 48.060  ? 249 ASP AAA O   1 
ATOM 1667  C CB  . ASP A 1 232 ? 176.738 -2.374  11.528  1.000 62.160  ? 249 ASP AAA CB  1 
ATOM 1668  C CG  . ASP A 1 232 ? 178.212 -2.633  11.679  1.000 70.190  ? 249 ASP AAA CG  1 
ATOM 1669  O OD1 . ASP A 1 232 ? 178.593 -3.257  12.712  1.000 72.270  ? 249 ASP AAA OD1 1 
ATOM 1670  O OD2 . ASP A 1 232 ? 178.944 -2.225  10.752  1.000 67.720  ? 249 ASP AAA OD2 1 
ATOM 1671  N N   . ASN A 1 233 ? 173.467 -3.588  12.921  1.000 55.670  ? 250 ASN AAA N   1 
ATOM 1672  C CA  . ASN A 1 233 ? 172.015 -3.287  13.010  1.000 54.040  ? 250 ASN AAA CA  1 
ATOM 1673  C C   . ASN A 1 233 ? 171.496 -3.473  14.438  1.000 49.460  ? 250 ASN AAA C   1 
ATOM 1674  O O   . ASN A 1 233 ? 171.815 -4.498  15.090  1.000 49.910  ? 250 ASN AAA O   1 
ATOM 1675  C CB  . ASN A 1 233 ? 171.207 -4.171  12.063  1.000 53.540  ? 250 ASN AAA CB  1 
ATOM 1676  C CG  . ASN A 1 233 ? 171.389 -3.784  10.616  1.000 52.340  ? 250 ASN AAA CG  1 
ATOM 1677  O OD1 . ASN A 1 233 ? 171.658 -2.616  10.303  1.000 52.970  ? 250 ASN AAA OD1 1 
ATOM 1678  N ND2 . ASN A 1 233 ? 171.211 -4.763  9.744   1.000 50.980  ? 250 ASN AAA ND2 1 
ATOM 1679  N N   . LEU A 1 234 ? 170.660 -2.537  14.877  1.000 47.100  ? 251 LEU AAA N   1 
ATOM 1680  C CA  . LEU A 1 234 ? 169.927 -2.596  16.167  1.000 47.950  ? 251 LEU AAA CA  1 
ATOM 1681  C C   . LEU A 1 234 ? 168.454 -2.804  15.847  1.000 48.580  ? 251 LEU AAA C   1 
ATOM 1682  O O   . LEU A 1 234 ? 167.963 -2.115  14.935  1.000 41.280  ? 251 LEU AAA O   1 
ATOM 1683  C CB  . LEU A 1 234 ? 170.135 -1.271  16.895  1.000 48.330  ? 251 LEU AAA CB  1 
ATOM 1684  C CG  . LEU A 1 234 ? 169.469 -1.138  18.255  1.000 43.580  ? 251 LEU AAA CG  1 
ATOM 1685  C CD1 . LEU A 1 234 ? 170.078 -2.131  19.218  1.000 42.340  ? 251 LEU AAA CD1 1 
ATOM 1686  C CD2 . LEU A 1 234 ? 169.638 0.291   18.772  1.000 45.490  ? 251 LEU AAA CD2 1 
ATOM 1687  N N   . TYR A 1 235 ? 167.796 -3.717  16.563  1.000 50.010  ? 252 TYR AAA N   1 
ATOM 1688  C CA  . TYR A 1 235 ? 166.385 -4.116  16.319  1.000 47.850  ? 252 TYR AAA CA  1 
ATOM 1689  C C   . TYR A 1 235 ? 165.484 -3.686  17.489  1.000 41.030  ? 252 TYR AAA C   1 
ATOM 1690  O O   . TYR A 1 235 ? 165.492 -4.312  18.573  1.000 38.660  ? 252 TYR AAA O   1 
ATOM 1691  C CB  . TYR A 1 235 ? 166.304 -5.621  16.071  1.000 53.570  ? 252 TYR AAA CB  1 
ATOM 1692  C CG  . TYR A 1 235 ? 166.670 -6.072  14.684  1.000 54.240  ? 252 TYR AAA CG  1 
ATOM 1693  C CD1 . TYR A 1 235 ? 167.994 -6.221  14.318  1.000 55.670  ? 252 TYR AAA CD1 1 
ATOM 1694  C CD2 . TYR A 1 235 ? 165.690 -6.388  13.755  1.000 58.590  ? 252 TYR AAA CD2 1 
ATOM 1695  C CE1 . TYR A 1 235 ? 168.343 -6.643  13.045  1.000 64.880  ? 252 TYR AAA CE1 1 
ATOM 1696  C CE2 . TYR A 1 235 ? 166.019 -6.824  12.483  1.000 65.400  ? 252 TYR AAA CE2 1 
ATOM 1697  C CZ  . TYR A 1 235 ? 167.353 -6.947  12.121  1.000 68.160  ? 252 TYR AAA CZ  1 
ATOM 1698  O OH  . TYR A 1 235 ? 167.691 -7.384  10.867  1.000 60.260  ? 252 TYR AAA OH  1 
ATOM 1699  N N   . LEU A 1 236 ? 164.688 -2.647  17.248  1.000 37.890  ? 253 LEU AAA N   1 
ATOM 1700  C CA  . LEU A 1 236 ? 163.652 -2.170  18.190  1.000 39.770  ? 253 LEU AAA CA  1 
ATOM 1701  C C   . LEU A 1 236 ? 162.326 -2.781  17.758  1.000 40.980  ? 253 LEU AAA C   1 
ATOM 1702  O O   . LEU A 1 236 ? 161.948 -2.615  16.580  1.000 43.420  ? 253 LEU AAA O   1 
ATOM 1703  C CB  . LEU A 1 236 ? 163.611 -0.642  18.195  1.000 37.520  ? 253 LEU AAA CB  1 
ATOM 1704  C CG  . LEU A 1 236 ? 164.974 0.021   18.337  1.000 39.400  ? 253 LEU AAA CG  1 
ATOM 1705  C CD1 . LEU A 1 236 ? 164.826 1.520   18.457  1.000 37.880  ? 253 LEU AAA CD1 1 
ATOM 1706  C CD2 . LEU A 1 236 ? 165.758 -0.547  19.514  1.000 39.480  ? 253 LEU AAA CD2 1 
ATOM 1707  N N   . SER A 1 237 ? 161.706 -3.511  18.679  1.000 40.500  ? 254 SER AAA N   1 
ATOM 1708  C CA  . SER A 1 237 ? 160.337 -4.062  18.542  1.000 40.790  ? 254 SER AAA CA  1 
ATOM 1709  C C   . SER A 1 237 ? 159.480 -3.475  19.670  1.000 37.650  ? 254 SER AAA C   1 
ATOM 1710  O O   . SER A 1 237 ? 160.061 -3.107  20.741  1.000 38.380  ? 254 SER AAA O   1 
ATOM 1711  C CB  . SER A 1 237 ? 160.389 -5.563  18.553  1.000 42.570  ? 254 SER AAA CB  1 
ATOM 1712  O OG  . SER A 1 237 ? 161.572 -6.015  17.896  1.000 46.560  ? 254 SER AAA OG  1 
ATOM 1713  N N   . ALA A 1 238 ? 158.176 -3.329  19.424  1.000 31.920  ? 255 ALA AAA N   1 
ATOM 1714  C CA  . ALA A 1 238 ? 157.243 -2.691  20.374  1.000 30.880  ? 255 ALA AAA CA  1 
ATOM 1715  C C   . ALA A 1 238 ? 155.804 -3.021  20.011  1.000 28.140  ? 255 ALA AAA C   1 
ATOM 1716  O O   . ALA A 1 238 ? 155.524 -3.171  18.826  1.000 28.200  ? 255 ALA AAA O   1 
ATOM 1717  C CB  . ALA A 1 238 ? 157.447 -1.196  20.365  1.000 32.330  ? 255 ALA AAA CB  1 
ATOM 1718  N N   . VAL A 1 239 ? 154.938 -3.105  21.020  1.000 26.550  ? 256 VAL AAA N   1 
ATOM 1719  C CA  . VAL A 1 239 ? 153.458 -3.057  20.865  1.000 26.590  ? 256 VAL AAA CA  1 
ATOM 1720  C C   . VAL A 1 239 ? 152.928 -2.222  22.010  1.000 28.500  ? 256 VAL AAA C   1 
ATOM 1721  O O   . VAL A 1 239 ? 153.397 -2.448  23.122  1.000 27.660  ? 256 VAL AAA O   1 
ATOM 1722  C CB  . VAL A 1 239 ? 152.810 -4.438  20.943  1.000 26.510  ? 256 VAL AAA CB  1 
ATOM 1723  C CG1 . VAL A 1 239 ? 151.310 -4.340  20.749  1.000 26.190  ? 256 VAL AAA CG1 1 
ATOM 1724  C CG2 . VAL A 1 239 ? 153.428 -5.418  19.966  1.000 28.550  ? 256 VAL AAA CG2 1 
ATOM 1725  N N   . ASP A 1 240 ? 151.963 -1.342  21.755  1.000 31.300  ? 257 ASP AAA N   1 
ATOM 1726  C CA  . ASP A 1 240 ? 151.330 -0.539  22.833  1.000 29.370  ? 257 ASP AAA CA  1 
ATOM 1727  C C   . ASP A 1 240 ? 149.844 -0.388  22.538  1.000 28.650  ? 257 ASP AAA C   1 
ATOM 1728  O O   . ASP A 1 240 ? 149.397 0.747   22.315  1.000 31.870  ? 257 ASP AAA O   1 
ATOM 1729  C CB  . ASP A 1 240 ? 152.039 0.804   22.969  1.000 29.030  ? 257 ASP AAA CB  1 
ATOM 1730  C CG  . ASP A 1 240 ? 153.406 0.673   23.591  1.000 28.390  ? 257 ASP AAA CG  1 
ATOM 1731  O OD1 . ASP A 1 240 ? 153.447 0.455   24.810  1.000 25.860  ? 257 ASP AAA OD1 1 
ATOM 1732  O OD2 . ASP A 1 240 ? 154.403 0.776   22.842  1.000 30.470  ? 257 ASP AAA OD2 1 
ATOM 1733  N N   . VAL A 1 241 ? 149.122 -1.506  22.497  1.000 25.390  ? 258 VAL AAA N   1 
ATOM 1734  C CA  . VAL A 1 241 ? 147.635 -1.509  22.421  1.000 23.960  ? 258 VAL AAA CA  1 
ATOM 1735  C C   . VAL A 1 241 ? 147.175 -0.962  23.767  1.000 25.600  ? 258 VAL AAA C   1 
ATOM 1736  O O   . VAL A 1 241 ? 147.449 -1.642  24.790  1.000 29.570  ? 258 VAL AAA O   1 
ATOM 1737  C CB  . VAL A 1 241 ? 147.095 -2.921  22.156  1.000 22.190  ? 258 VAL AAA CB  1 
ATOM 1738  C CG1 . VAL A 1 241 ? 145.579 -2.969  22.226  1.000 22.680  ? 258 VAL AAA CG1 1 
ATOM 1739  C CG2 . VAL A 1 241 ? 147.595 -3.473  20.840  1.000 21.260  ? 258 VAL AAA CG2 1 
ATOM 1740  N N   . CYS A 1 242 ? 146.612 0.249   23.790  1.000 24.240  ? 259 CYS AAA N   1 
ATOM 1741  C CA  . CYS A 1 242 ? 146.399 1.017   25.045  1.000 23.750  ? 259 CYS AAA CA  1 
ATOM 1742  C C   . CYS A 1 242 ? 145.081 0.621   25.674  1.000 23.790  ? 259 CYS AAA C   1 
ATOM 1743  O O   . CYS A 1 242 ? 144.931 0.823   26.903  1.000 26.810  ? 259 CYS AAA O   1 
ATOM 1744  C CB  . CYS A 1 242 ? 146.398 2.505   24.769  1.000 23.650  ? 259 CYS AAA CB  1 
ATOM 1745  S SG  . CYS A 1 242 ? 148.079 3.130   24.502  1.000 22.350  ? 259 CYS AAA SG  1 
ATOM 1746  N N   . GLY A 1 243 ? 144.189 0.060   24.853  1.000 21.440  ? 260 GLY AAA N   1 
ATOM 1747  C CA  . GLY A 1 243 ? 142.796 -0.250  25.219  1.000 21.100  ? 260 GLY AAA CA  1 
ATOM 1748  C C   . GLY A 1 243 ? 141.924 -0.146  23.985  1.000 20.560  ? 260 GLY AAA C   1 
ATOM 1749  O O   . GLY A 1 243 ? 142.458 -0.255  22.864  1.000 20.600  ? 260 GLY AAA O   1 
ATOM 1750  N N   . MET A 1 244 ? 140.624 0.037   24.189  1.000 20.870  ? 261 MET AAA N   1 
ATOM 1751  C CA  . MET A 1 244 ? 139.658 0.239   23.085  1.000 22.370  ? 261 MET AAA CA  1 
ATOM 1752  C C   . MET A 1 244 ? 139.022 1.621   23.223  1.000 23.590  ? 261 MET AAA C   1 
ATOM 1753  O O   . MET A 1 244 ? 138.749 2.054   24.369  1.000 23.710  ? 261 MET AAA O   1 
ATOM 1754  C CB  . MET A 1 244 ? 138.545 -0.809  23.109  1.000 22.760  ? 261 MET AAA CB  1 
ATOM 1755  C CG  . MET A 1 244 ? 139.055 -2.209  23.019  1.000 22.260  ? 261 MET AAA CG  1 
ATOM 1756  S SD  . MET A 1 244 ? 137.680 -3.348  23.019  1.000 21.240  ? 261 MET AAA SD  1 
ATOM 1757  C CE  . MET A 1 244 ? 138.579 -4.865  22.700  1.000 20.860  ? 261 MET AAA CE  1 
ATOM 1758  N N   . PHE A 1 245 ? 138.794 2.262   22.077  1.000 23.190  ? 262 PHE AAA N   1 
ATOM 1759  C CA  . PHE A 1 245 ? 137.931 3.454   21.929  1.000 22.280  ? 262 PHE AAA CA  1 
ATOM 1760  C C   . PHE A 1 245 ? 136.515 2.933   21.774  1.000 21.520  ? 262 PHE AAA C   1 
ATOM 1761  O O   . PHE A 1 245 ? 136.343 2.082   20.913  1.000 21.170  ? 262 PHE AAA O   1 
ATOM 1762  C CB  . PHE A 1 245 ? 138.329 4.284   20.705  1.000 22.160  ? 262 PHE AAA CB  1 
ATOM 1763  C CG  . PHE A 1 245 ? 137.365 5.389   20.393  1.000 23.160  ? 262 PHE AAA CG  1 
ATOM 1764  C CD1 . PHE A 1 245 ? 137.071 6.365   21.329  1.000 24.720  ? 262 PHE AAA CD1 1 
ATOM 1765  C CD2 . PHE A 1 245 ? 136.736 5.439   19.173  1.000 25.080  ? 262 PHE AAA CD2 1 
ATOM 1766  C CE1 . PHE A 1 245 ? 136.170 7.384   21.053  1.000 25.940  ? 262 PHE AAA CE1 1 
ATOM 1767  C CE2 . PHE A 1 245 ? 135.846 6.463   18.885  1.000 27.710  ? 262 PHE AAA CE2 1 
ATOM 1768  C CZ  . PHE A 1 245 ? 135.545 7.427   19.835  1.000 27.220  ? 262 PHE AAA CZ  1 
ATOM 1769  N N   . THR A 1 246 ? 135.576 3.389   22.598  1.000 21.880  ? 263 THR AAA N   1 
ATOM 1770  C CA  . THR A 1 246 ? 134.136 3.064   22.448  1.000 22.540  ? 263 THR AAA CA  1 
ATOM 1771  C C   . THR A 1 246 ? 133.447 4.199   21.685  1.000 22.270  ? 263 THR AAA C   1 
ATOM 1772  O O   . THR A 1 246 ? 133.318 5.305   22.231  1.000 24.690  ? 263 THR AAA O   1 
ATOM 1773  C CB  . THR A 1 246 ? 133.489 2.740   23.801  1.000 23.210  ? 263 THR AAA CB  1 
ATOM 1774  O OG1 . THR A 1 246 ? 134.248 1.709   24.448  1.000 22.780  ? 263 THR AAA OG1 1 
ATOM 1775  C CG2 . THR A 1 246 ? 132.050 2.300   23.629  1.000 23.450  ? 263 THR AAA CG2 1 
ATOM 1776  N N   . ASN A 1 247 ? 133.058 3.919   20.445  1.000 22.670  ? 264 ASN AAA N   1 
ATOM 1777  C CA  . ASN A 1 247 ? 132.244 4.799   19.565  1.000 22.060  ? 264 ASN AAA CA  1 
ATOM 1778  C C   . ASN A 1 247 ? 130.835 4.965   20.157  1.000 23.280  ? 264 ASN AAA C   1 
ATOM 1779  O O   . ASN A 1 247 ? 130.458 4.181   21.020  1.000 26.820  ? 264 ASN AAA O   1 
ATOM 1780  C CB  . ASN A 1 247 ? 132.170 4.245   18.147  1.000 21.880  ? 264 ASN AAA CB  1 
ATOM 1781  C CG  . ASN A 1 247 ? 133.388 4.602   17.324  1.000 23.880  ? 264 ASN AAA CG  1 
ATOM 1782  O OD1 . ASN A 1 247 ? 134.369 3.848   17.351  1.000 23.690  ? 264 ASN AAA OD1 1 
ATOM 1783  N ND2 . ASN A 1 247 ? 133.334 5.724   16.593  1.000 23.630  ? 264 ASN AAA ND2 1 
ATOM 1784  N N   . ARG A 1 248 ? 130.112 5.993   19.727  1.000 22.830  ? 265 ARG AAA N   1 
ATOM 1785  C CA  . ARG A 1 248 ? 128.737 6.351   20.161  1.000 22.770  ? 265 ARG AAA CA  1 
ATOM 1786  C C   . ARG A 1 248 ? 127.825 5.134   20.101  1.000 21.770  ? 265 ARG AAA C   1 
ATOM 1787  O O   . ARG A 1 248 ? 127.028 4.978   21.013  1.000 22.690  ? 265 ARG AAA O   1 
ATOM 1788  C CB  . ARG A 1 248 ? 128.222 7.503   19.295  1.000 23.840  ? 265 ARG AAA CB  1 
ATOM 1789  C CG  . ARG A 1 248 ? 126.713 7.551   19.134  1.000 24.780  ? 265 ARG AAA CG  1 
ATOM 1790  C CD  . ARG A 1 248 ? 126.185 8.767   18.368  1.000 24.260  ? 265 ARG AAA CD  1 
ATOM 1791  N NE  . ARG A 1 248 ? 125.841 9.925   19.184  1.000 22.410  ? 265 ARG AAA NE  1 
ATOM 1792  C CZ  . ARG A 1 248 ? 126.571 11.033  19.261  1.000 24.500  ? 265 ARG AAA CZ  1 
ATOM 1793  N NH1 . ARG A 1 248 ? 127.684 11.148  18.574  1.000 25.340  ? 265 ARG AAA NH1 1 
ATOM 1794  N NH2 . ARG A 1 248 ? 126.217 12.050  20.026  1.000 28.360  ? 265 ARG AAA NH2 1 
ATOM 1795  N N   . SER A 1 249 ? 127.953 4.302   19.080  1.000 22.200  ? 266 SER AAA N   1 
ATOM 1796  C CA  . SER A 1 249 ? 127.082 3.116   18.855  1.000 25.160  ? 266 SER AAA CA  1 
ATOM 1797  C C   . SER A 1 249 ? 127.363 2.022   19.884  1.000 26.570  ? 266 SER AAA C   1 
ATOM 1798  O O   . SER A 1 249 ? 126.604 1.030   19.908  1.000 27.280  ? 266 SER AAA O   1 
ATOM 1799  C CB  . SER A 1 249 ? 127.322 2.522   17.497  1.000 26.030  ? 266 SER AAA CB  1 
ATOM 1800  O OG  . SER A 1 249 ? 128.598 1.911   17.456  1.000 26.040  ? 266 SER AAA OG  1 
ATOM 1801  N N   . GLY A 1 250 ? 128.496 2.128   20.574  1.000 26.870  ? 267 GLY AAA N   1 
ATOM 1802  C CA  . GLY A 1 250 ? 129.038 1.065   21.437  1.000 27.410  ? 267 GLY AAA CA  1 
ATOM 1803  C C   . GLY A 1 250 ? 130.142 0.276   20.755  1.000 25.980  ? 267 GLY AAA C   1 
ATOM 1804  O O   . GLY A 1 250 ? 130.879 -0.421  21.481  1.000 32.590  ? 267 GLY AAA O   1 
ATOM 1805  N N   . SER A 1 251 ? 130.244 0.341   19.426  1.000 22.740  ? 268 SER AAA N   1 
ATOM 1806  C CA  . SER A 1 251 ? 131.263 -0.395  18.633  1.000 22.430  ? 268 SER AAA CA  1 
ATOM 1807  C C   . SER A 1 251 ? 132.668 0.022   19.088  1.000 21.200  ? 268 SER AAA C   1 
ATOM 1808  O O   . SER A 1 251 ? 132.882 1.192   19.379  1.000 19.980  ? 268 SER AAA O   1 
ATOM 1809  C CB  . SER A 1 251 ? 131.042 -0.190  17.154  1.000 23.390  ? 268 SER AAA CB  1 
ATOM 1810  O OG  . SER A 1 251 ? 129.662 -0.206  16.832  1.000 23.080  ? 268 SER AAA OG  1 
ATOM 1811  N N   . GLN A 1 252 ? 133.596 -0.921  19.171  1.000 21.320  ? 269 GLN AAA N   1 
ATOM 1812  C CA  . GLN A 1 252 ? 134.915 -0.678  19.809  1.000 22.520  ? 269 GLN AAA CA  1 
ATOM 1813  C C   . GLN A 1 252 ? 136.059 -0.865  18.814  1.000 22.450  ? 269 GLN AAA C   1 
ATOM 1814  O O   . GLN A 1 252 ? 136.040 -1.852  18.096  1.000 25.110  ? 269 GLN AAA O   1 
ATOM 1815  C CB  . GLN A 1 252 ? 135.088 -1.627  20.995  1.000 23.700  ? 269 GLN AAA CB  1 
ATOM 1816  C CG  . GLN A 1 252 ? 134.301 -1.163  22.221  1.000 23.570  ? 269 GLN AAA CG  1 
ATOM 1817  C CD  . GLN A 1 252 ? 134.251 -2.173  23.328  1.000 21.680  ? 269 GLN AAA CD  1 
ATOM 1818  O OE1 . GLN A 1 252 ? 134.277 -3.386  23.118  1.000 19.670  ? 269 GLN AAA OE1 1 
ATOM 1819  N NE2 . GLN A 1 252 ? 134.171 -1.648  24.526  1.000 22.070  ? 269 GLN AAA NE2 1 
ATOM 1820  N N   . GLN A 1 253 ? 137.032 0.043   18.836  1.000 21.170  ? 270 GLN AAA N   1 
ATOM 1821  C CA  . GLN A 1 253 ? 138.279 0.006   18.033  1.000 20.810  ? 270 GLN AAA CA  1 
ATOM 1822  C C   . GLN A 1 253 ? 139.468 0.007   18.984  1.000 20.410  ? 270 GLN AAA C   1 
ATOM 1823  O O   . GLN A 1 253 ? 139.514 0.840   19.868  1.000 18.660  ? 270 GLN AAA O   1 
ATOM 1824  C CB  . GLN A 1 253 ? 138.379 1.236   17.126  1.000 22.350  ? 270 GLN AAA CB  1 
ATOM 1825  C CG  . GLN A 1 253 ? 137.263 1.329   16.091  1.000 23.350  ? 270 GLN AAA CG  1 
ATOM 1826  C CD  . GLN A 1 253 ? 137.167 2.712   15.502  1.000 21.950  ? 270 GLN AAA CD  1 
ATOM 1827  O OE1 . GLN A 1 253 ? 137.926 3.082   14.598  1.000 22.640  ? 270 GLN AAA OE1 1 
ATOM 1828  N NE2 . GLN A 1 253 ? 136.242 3.479   16.050  1.000 18.760  ? 270 GLN AAA NE2 1 
ATOM 1829  N N   . TRP A 1 254 ? 140.387 -0.927  18.820  1.000 22.400  ? 271 TRP AAA N   1 
ATOM 1830  C CA  . TRP A 1 254 ? 141.713 -0.863  19.480  1.000 22.750  ? 271 TRP AAA CA  1 
ATOM 1831  C C   . TRP A 1 254 ? 142.300 0.518   19.225  1.000 22.270  ? 271 TRP AAA C   1 
ATOM 1832  O O   . TRP A 1 254 ? 142.117 0.982   18.118  1.000 24.250  ? 271 TRP AAA O   1 
ATOM 1833  C CB  . TRP A 1 254 ? 142.629 -1.938  18.905  1.000 22.480  ? 271 TRP AAA CB  1 
ATOM 1834  C CG  . TRP A 1 254 ? 142.174 -3.346  19.127  1.000 22.000  ? 271 TRP AAA CG  1 
ATOM 1835  C CD1 . TRP A 1 254 ? 141.754 -4.228  18.182  1.000 22.020  ? 271 TRP AAA CD1 1 
ATOM 1836  C CD2 . TRP A 1 254 ? 142.162 -4.054  20.366  1.000 21.500  ? 271 TRP AAA CD2 1 
ATOM 1837  N NE1 . TRP A 1 254 ? 141.477 -5.432  18.752  1.000 22.330  ? 271 TRP AAA NE1 1 
ATOM 1838  C CE2 . TRP A 1 254 ? 141.706 -5.347  20.093  1.000 20.870  ? 271 TRP AAA CE2 1 
ATOM 1839  C CE3 . TRP A 1 254 ? 142.441 -3.696  21.683  1.000 23.700  ? 271 TRP AAA CE3 1 
ATOM 1840  C CZ2 . TRP A 1 254 ? 141.561 -6.306  21.079  1.000 21.150  ? 271 TRP AAA CZ2 1 
ATOM 1841  C CZ3 . TRP A 1 254 ? 142.301 -4.642  22.669  1.000 24.710  ? 271 TRP AAA CZ3 1 
ATOM 1842  C CH2 . TRP A 1 254 ? 141.870 -5.933  22.361  1.000 23.730  ? 271 TRP AAA CH2 1 
ATOM 1843  N N   . ARG A 1 255 ? 142.977 1.136   20.191  1.000 21.810  ? 272 ARG AAA N   1 
ATOM 1844  C CA  . ARG A 1 255 ? 143.711 2.407   19.973  1.000 21.360  ? 272 ARG AAA CA  1 
ATOM 1845  C C   . ARG A 1 255 ? 145.140 2.236   20.457  1.000 23.570  ? 272 ARG AAA C   1 
ATOM 1846  O O   . ARG A 1 255 ? 145.344 1.780   21.596  1.000 24.950  ? 272 ARG AAA O   1 
ATOM 1847  C CB  . ARG A 1 255 ? 143.089 3.572   20.725  1.000 21.470  ? 272 ARG AAA CB  1 
ATOM 1848  C CG  . ARG A 1 255 ? 143.836 4.881   20.532  1.000 23.590  ? 272 ARG AAA CG  1 
ATOM 1849  C CD  . ARG A 1 255 ? 143.734 5.342   19.099  1.000 26.160  ? 272 ARG AAA CD  1 
ATOM 1850  N NE  . ARG A 1 255 ? 143.980 6.769   18.870  1.000 26.530  ? 272 ARG AAA NE  1 
ATOM 1851  C CZ  . ARG A 1 255 ? 145.166 7.312   18.579  1.000 26.980  ? 272 ARG AAA CZ  1 
ATOM 1852  N NH1 . ARG A 1 255 ? 146.260 6.574   18.478  1.000 26.650  ? 272 ARG AAA NH1 1 
ATOM 1853  N NH2 . ARG A 1 255 ? 145.251 8.609   18.358  1.000 28.160  ? 272 ARG AAA NH2 1 
ATOM 1854  N N   . GLY A 1 256 ? 146.096 2.598   19.613  1.000 26.530  ? 273 GLY AAA N   1 
ATOM 1855  C CA  . GLY A 1 256 ? 147.534 2.384   19.869  1.000 27.390  ? 273 GLY AAA CA  1 
ATOM 1856  C C   . GLY A 1 256 ? 148.252 3.703   20.020  1.000 25.280  ? 273 GLY AAA C   1 
ATOM 1857  O O   . GLY A 1 256 ? 147.659 4.719   19.663  1.000 24.540  ? 273 GLY AAA O   1 
ATOM 1858  N N   . LEU A 1 257 ? 149.471 3.678   20.541  1.000 24.600  ? 274 LEU AAA N   1 
ATOM 1859  C CA  . LEU A 1 257 ? 150.329 4.877   20.644  1.000 28.440  ? 274 LEU AAA CA  1 
ATOM 1860  C C   . LEU A 1 257 ? 151.776 4.514   20.309  1.000 32.200  ? 274 LEU AAA C   1 
ATOM 1861  O O   . LEU A 1 257 ? 152.223 3.355   20.556  1.000 34.420  ? 274 LEU AAA O   1 
ATOM 1862  C CB  . LEU A 1 257 ? 150.235 5.482   22.044  1.000 29.130  ? 274 LEU AAA CB  1 
ATOM 1863  C CG  . LEU A 1 257 ? 148.918 6.167   22.380  1.000 30.290  ? 274 LEU AAA CG  1 
ATOM 1864  C CD1 . LEU A 1 257 ? 148.900 6.591   23.826  1.000 31.000  ? 274 LEU AAA CD1 1 
ATOM 1865  C CD2 . LEU A 1 257 ? 148.680 7.354   21.470  1.000 32.550  ? 274 LEU AAA CD2 1 
ATOM 1866  N N   . SER A 1 258 ? 152.488 5.503   19.776  1.000 34.550  ? 275 SER AAA N   1 
ATOM 1867  C CA  . SER A 1 258 ? 153.917 5.391   19.432  1.000 34.740  ? 275 SER AAA CA  1 
ATOM 1868  C C   . SER A 1 258 ? 154.730 5.160   20.712  1.000 34.950  ? 275 SER AAA C   1 
ATOM 1869  O O   . SER A 1 258 ? 154.292 5.592   21.793  1.000 34.690  ? 275 SER AAA O   1 
ATOM 1870  C CB  . SER A 1 258 ? 154.346 6.621   18.686  1.000 36.730  ? 275 SER AAA CB  1 
ATOM 1871  O OG  . SER A 1 258 ? 153.530 6.804   17.541  1.000 36.090  ? 275 SER AAA OG  1 
ATOM 1872  N N   . ARG A 1 259 ? 155.883 4.505   20.584  1.000 36.220  ? 276 ARG AAA N   1 
ATOM 1873  C CA  . ARG A 1 259 ? 156.857 4.307   21.688  1.000 33.900  ? 276 ARG AAA CA  1 
ATOM 1874  C C   . ARG A 1 259 ? 158.196 4.950   21.324  1.000 30.130  ? 276 ARG AAA C   1 
ATOM 1875  O O   . ARG A 1 259 ? 158.740 4.609   20.286  1.000 28.220  ? 276 ARG AAA O   1 
ATOM 1876  C CB  . ARG A 1 259 ? 157.035 2.816   21.966  1.000 33.150  ? 276 ARG AAA CB  1 
ATOM 1877  C CG  . ARG A 1 259 ? 158.131 2.517   22.978  1.000 34.860  ? 276 ARG AAA CG  1 
ATOM 1878  C CD  . ARG A 1 259 ? 158.053 1.095   23.503  1.000 34.400  ? 276 ARG AAA CD  1 
ATOM 1879  N NE  . ARG A 1 259 ? 156.853 0.916   24.301  1.000 33.640  ? 276 ARG AAA NE  1 
ATOM 1880  C CZ  . ARG A 1 259 ? 156.762 1.094   25.611  1.000 32.250  ? 276 ARG AAA CZ  1 
ATOM 1881  N NH1 . ARG A 1 259 ? 157.803 1.449   26.339  1.000 32.330  ? 276 ARG AAA NH1 1 
ATOM 1882  N NH2 . ARG A 1 259 ? 155.604 0.913   26.194  1.000 35.720  ? 276 ARG AAA NH2 1 
ATOM 1883  N N   . TYR A 1 260 ? 158.711 5.812   22.187  1.000 30.470  ? 277 TYR AAA N   1 
ATOM 1884  C CA  . TYR A 1 260 ? 160.076 6.392   22.106  1.000 34.080  ? 277 TYR AAA CA  1 
ATOM 1885  C C   . TYR A 1 260 ? 161.097 5.369   22.608  1.000 34.950  ? 277 TYR AAA C   1 
ATOM 1886  O O   . TYR A 1 260 ? 160.834 4.696   23.618  1.000 30.630  ? 277 TYR AAA O   1 
ATOM 1887  C CB  . TYR A 1 260 ? 160.147 7.656   22.963  1.000 34.970  ? 277 TYR AAA CB  1 
ATOM 1888  C CG  . TYR A 1 260 ? 161.505 8.260   23.194  1.000 34.220  ? 277 TYR AAA CG  1 
ATOM 1889  C CD1 . TYR A 1 260 ? 162.065 9.136   22.287  1.000 35.060  ? 277 TYR AAA CD1 1 
ATOM 1890  C CD2 . TYR A 1 260 ? 162.197 8.021   24.363  1.000 35.170  ? 277 TYR AAA CD2 1 
ATOM 1891  C CE1 . TYR A 1 260 ? 163.285 9.753   22.527  1.000 35.400  ? 277 TYR AAA CE1 1 
ATOM 1892  C CE2 . TYR A 1 260 ? 163.425 8.610   24.611  1.000 33.830  ? 277 TYR AAA CE2 1 
ATOM 1893  C CZ  . TYR A 1 260 ? 163.965 9.489   23.699  1.000 33.150  ? 277 TYR AAA CZ  1 
ATOM 1894  O OH  . TYR A 1 260 ? 165.173 10.063  23.952  1.000 33.040  ? 277 TYR AAA OH  1 
ATOM 1895  N N   . PHE A 1 261 ? 162.232 5.271   21.921  1.000 35.300  ? 278 PHE AAA N   1 
ATOM 1896  C CA  . PHE A 1 261 ? 163.432 4.512   22.360  1.000 32.570  ? 278 PHE AAA CA  1 
ATOM 1897  C C   . PHE A 1 261 ? 164.648 5.435   22.333  1.000 31.080  ? 278 PHE AAA C   1 
ATOM 1898  O O   . PHE A 1 261 ? 164.784 6.240   21.414  1.000 29.740  ? 278 PHE AAA O   1 
ATOM 1899  C CB  . PHE A 1 261 ? 163.709 3.341   21.422  1.000 32.650  ? 278 PHE AAA CB  1 
ATOM 1900  C CG  . PHE A 1 261 ? 162.678 2.244   21.391  1.000 34.690  ? 278 PHE AAA CG  1 
ATOM 1901  C CD1 . PHE A 1 261 ? 161.479 2.414   20.707  1.000 34.170  ? 278 PHE AAA CD1 1 
ATOM 1902  C CD2 . PHE A 1 261 ? 162.944 1.011   21.978  1.000 34.910  ? 278 PHE AAA CD2 1 
ATOM 1903  C CE1 . PHE A 1 261 ? 160.559 1.374   20.621  1.000 35.870  ? 278 PHE AAA CE1 1 
ATOM 1904  C CE2 . PHE A 1 261 ? 162.011 -0.013  21.906  1.000 37.090  ? 278 PHE AAA CE2 1 
ATOM 1905  C CZ  . PHE A 1 261 ? 160.827 0.160   21.218  1.000 36.300  ? 278 PHE AAA CZ  1 
ATOM 1906  N N   . LYS A 1 262 ? 165.521 5.307   23.314  1.000 33.340  ? 279 LYS AAA N   1 
ATOM 1907  C CA  . LYS A 1 262 ? 166.873 5.919   23.281  1.000 37.620  ? 279 LYS AAA CA  1 
ATOM 1908  C C   . LYS A 1 262 ? 167.832 4.859   23.804  1.000 35.430  ? 279 LYS AAA C   1 
ATOM 1909  O O   . LYS A 1 262 ? 167.729 4.517   24.998  1.000 36.450  ? 279 LYS AAA O   1 
ATOM 1910  C CB  . LYS A 1 262 ? 166.926 7.207   24.109  1.000 40.330  ? 279 LYS AAA CB  1 
ATOM 1911  C CG  . LYS A 1 262 ? 168.258 7.936   24.103  1.000 44.110  ? 279 LYS AAA CG  1 
ATOM 1912  C CD  . LYS A 1 262 ? 168.233 9.195   24.956  1.000 49.360  ? 279 LYS AAA CD  1 
ATOM 1913  C CE  . LYS A 1 262 ? 169.621 9.755   25.250  1.000 54.350  ? 279 LYS AAA CE  1 
ATOM 1914  N NZ  . LYS A 1 262 ? 169.730 10.207  26.670  1.000 54.420  ? 279 LYS AAA NZ  1 
ATOM 1915  N N   . VAL A 1 263 ? 168.694 4.339   22.941  1.000 34.490  ? 280 VAL AAA N   1 
ATOM 1916  C CA  . VAL A 1 263 ? 169.608 3.231   23.315  1.000 36.620  ? 280 VAL AAA CA  1 
ATOM 1917  C C   . VAL A 1 263 ? 171.052 3.735   23.282  1.000 37.710  ? 280 VAL AAA C   1 
ATOM 1918  O O   . VAL A 1 263 ? 171.493 4.189   22.245  1.000 37.250  ? 280 VAL AAA O   1 
ATOM 1919  C CB  . VAL A 1 263 ? 169.368 2.004   22.423  1.000 35.170  ? 280 VAL AAA CB  1 
ATOM 1920  C CG1 . VAL A 1 263 ? 170.260 0.847   22.825  1.000 34.890  ? 280 VAL AAA CG1 1 
ATOM 1921  C CG2 . VAL A 1 263 ? 167.904 1.584   22.456  1.000 34.340  ? 280 VAL AAA CG2 1 
ATOM 1922  N N   . GLN A 1 264 ? 171.724 3.708   24.429  1.000 45.030  ? 281 GLN AAA N   1 
ATOM 1923  C CA  . GLN A 1 264 ? 173.197 3.840   24.545  1.000 52.570  ? 281 GLN AAA CA  1 
ATOM 1924  C C   . GLN A 1 264 ? 173.822 2.562   23.987  1.000 50.260  ? 281 GLN AAA C   1 
ATOM 1925  O O   . GLN A 1 264 ? 173.348 1.468   24.331  1.000 48.760  ? 281 GLN AAA O   1 
ATOM 1926  C CB  . GLN A 1 264 ? 173.644 4.009   26.006  1.000 65.920  ? 281 GLN AAA CB  1 
ATOM 1927  C CG  . GLN A 1 264 ? 173.078 5.228   26.739  1.000 66.490  ? 281 GLN AAA CG  1 
ATOM 1928  C CD  . GLN A 1 264 ? 173.655 6.504   26.195  1.000 73.180  ? 281 GLN AAA CD  1 
ATOM 1929  O OE1 . GLN A 1 264 ? 174.726 6.506   25.571  1.000 87.610  ? 281 GLN AAA OE1 1 
ATOM 1930  N NE2 . GLN A 1 264 ? 172.921 7.581   26.412  1.000 68.150  ? 281 GLN AAA NE2 1 
ATOM 1931  N N   . LEU A 1 265 ? 174.857 2.695   23.171  1.000 51.330  ? 282 LEU AAA N   1 
ATOM 1932  C CA  . LEU A 1 265 ? 175.608 1.536   22.636  1.000 53.480  ? 282 LEU AAA CA  1 
ATOM 1933  C C   . LEU A 1 265 ? 177.099 1.783   22.875  1.000 55.610  ? 282 LEU AAA C   1 
ATOM 1934  O O   . LEU A 1 265 ? 177.486 2.952   22.924  1.000 58.480  ? 282 LEU AAA O   1 
ATOM 1935  C CB  . LEU A 1 265 ? 175.283 1.428   21.147  1.000 54.440  ? 282 LEU AAA CB  1 
ATOM 1936  C CG  . LEU A 1 265 ? 173.846 1.043   20.810  1.000 56.640  ? 282 LEU AAA CG  1 
ATOM 1937  C CD1 . LEU A 1 265 ? 173.321 1.854   19.649  1.000 58.900  ? 282 LEU AAA CD1 1 
ATOM 1938  C CD2 . LEU A 1 265 ? 173.736 -0.436  20.486  1.000 57.900  ? 282 LEU AAA CD2 1 
ATOM 1939  N N   . ARG A 1 266 ? 177.894 0.724   23.039  1.000 54.620  ? 283 ARG AAA N   1 
ATOM 1940  C CA  . ARG A 1 266 ? 179.379 0.800   23.098  1.000 52.060  ? 283 ARG AAA CA  1 
ATOM 1941  C C   . ARG A 1 266 ? 179.965 -0.312  22.212  1.000 50.520  ? 283 ARG AAA C   1 
ATOM 1942  O O   . ARG A 1 266 ? 179.192 -1.151  21.736  1.000 44.650  ? 283 ARG AAA O   1 
ATOM 1943  C CB  . ARG A 1 266 ? 179.860 0.713   24.551  1.000 48.540  ? 283 ARG AAA CB  1 
ATOM 1944  C CG  . ARG A 1 266 ? 179.765 -0.685  25.139  1.000 50.250  ? 283 ARG AAA CG  1 
ATOM 1945  C CD  . ARG A 1 266 ? 179.943 -0.697  26.642  1.000 52.610  ? 283 ARG AAA CD  1 
ATOM 1946  N NE  . ARG A 1 266 ? 179.754 -2.044  27.165  1.000 53.510  ? 283 ARG AAA NE  1 
ATOM 1947  C CZ  . ARG A 1 266 ? 179.527 -2.339  28.436  1.000 55.070  ? 283 ARG AAA CZ  1 
ATOM 1948  N NH1 . ARG A 1 266 ? 179.419 -1.362  29.319  1.000 61.230  ? 283 ARG AAA NH1 1 
ATOM 1949  N NH2 . ARG A 1 266 ? 179.361 -3.596  28.829  1.000 53.490  ? 283 ARG AAA NH2 1 
ATOM 1950  N N   . LYS A 1 267 ? 181.279 -0.317  21.998  1.000 52.030  ? 284 LYS AAA N   1 
ATOM 1951  C CA  . LYS A 1 267 ? 181.974 -1.283  21.106  1.000 50.940  ? 284 LYS AAA CA  1 
ATOM 1952  C C   . LYS A 1 267 ? 182.551 -2.406  21.978  1.000 53.440  ? 284 LYS AAA C   1 
ATOM 1953  O O   . LYS A 1 267 ? 183.367 -2.062  22.878  1.000 56.260  ? 284 LYS AAA O   1 
ATOM 1954  C CB  . LYS A 1 267 ? 183.101 -0.549  20.380  1.000 46.320  ? 284 LYS AAA CB  1 
ATOM 1955  C CG  . LYS A 1 267 ? 182.620 0.531   19.432  1.000 48.220  ? 284 LYS AAA CG  1 
ATOM 1956  C CD  . LYS A 1 267 ? 183.739 1.194   18.687  1.000 53.750  ? 284 LYS AAA CD  1 
ATOM 1957  C CE  . LYS A 1 267 ? 183.234 2.273   17.756  1.000 56.930  ? 284 LYS AAA CE  1 
ATOM 1958  N NZ  . LYS A 1 267 ? 184.336 3.086   17.200  1.000 58.110  ? 284 LYS AAA NZ  1 
ATOM 1959  N N   . ARG A 1 268 ? 182.280 -3.656  21.592  1.000 53.130  ? 285 ARG AAA N   1 
ATOM 1960  C CA  . ARG A 1 268 ? 182.822 -4.833  22.309  1.000 57.680  ? 285 ARG AAA CA  1 
ATOM 1961  C C   . ARG A 1 268 ? 183.650 -5.668  21.331  1.000 61.270  ? 285 ARG AAA C   1 
ATOM 1962  O O   . ARG A 1 268 ? 183.132 -5.957  20.250  1.000 59.500  ? 285 ARG AAA O   1 
ATOM 1963  C CB  . ARG A 1 268 ? 181.672 -5.679  22.856  1.000 57.520  ? 285 ARG AAA CB  1 
ATOM 1964  C CG  . ARG A 1 268 ? 182.101 -6.729  23.867  1.000 58.680  ? 285 ARG AAA CG  1 
ATOM 1965  C CD  . ARG A 1 268 ? 181.671 -6.330  25.259  1.000 60.800  ? 285 ARG AAA CD  1 
ATOM 1966  N NE  . ARG A 1 268 ? 182.139 -7.263  26.269  1.000 61.600  ? 285 ARG AAA NE  1 
ATOM 1967  C CZ  . ARG A 1 268 ? 181.611 -7.387  27.478  1.000 63.500  ? 285 ARG AAA CZ  1 
ATOM 1968  N NH1 . ARG A 1 268 ? 180.597 -6.622  27.837  1.000 63.950  ? 285 ARG AAA NH1 1 
ATOM 1969  N NH2 . ARG A 1 268 ? 182.103 -8.268  28.327  1.000 64.320  ? 285 ARG AAA NH2 1 
ATOM 1970  N N   . ARG A 1 269 ? 184.895 -5.998  21.679  1.000 66.280  ? 286 ARG AAA N   1 
ATOM 1971  C CA  . ARG A 1 269 ? 185.743 -6.894  20.854  1.000 73.000  ? 286 ARG AAA CA  1 
ATOM 1972  C C   . ARG A 1 269 ? 185.142 -8.310  20.899  1.000 68.080  ? 286 ARG AAA C   1 
ATOM 1973  O O   . ARG A 1 269 ? 184.605 -8.691  21.954  1.000 67.230  ? 286 ARG AAA O   1 
ATOM 1974  C CB  . ARG A 1 269 ? 187.170 -6.767  21.408  1.000 86.310  ? 286 ARG AAA CB  1 
ATOM 1975  C CG  . ARG A 1 269 ? 188.277 -7.238  20.461  1.000 92.940  ? 286 ARG AAA CG  1 
ATOM 1976  C CD  . ARG A 1 269 ? 189.170 -6.119  19.943  1.000 91.560  ? 286 ARG AAA CD  1 
ATOM 1977  N NE  . ARG A 1 269 ? 189.454 -5.189  21.036  1.000 85.580  ? 286 ARG AAA NE  1 
ATOM 1978  C CZ  . ARG A 1 269 ? 189.647 -3.875  20.923  1.000 87.530  ? 286 ARG AAA CZ  1 
ATOM 1979  N NH1 . ARG A 1 269 ? 189.879 -3.170  22.015  1.000 93.170  ? 286 ARG AAA NH1 1 
ATOM 1980  N NH2 . ARG A 1 269 ? 189.608 -3.256  19.751  1.000 85.710  ? 286 ARG AAA NH2 1 
ATOM 1981  N N   . VAL A 1 270 ? 185.166 -9.023  19.768  1.000 67.670  ? 287 VAL AAA N   1 
ATOM 1982  C CA  . VAL A 1 270 ? 184.490 -10.332 19.530  1.000 72.360  ? 287 VAL AAA CA  1 
ATOM 1983  C C   . VAL A 1 270 ? 185.401 -11.187 18.631  1.000 80.150  ? 287 VAL AAA C   1 
ATOM 1984  O O   . VAL A 1 270 ? 185.977 -10.598 17.698  1.000 97.470  ? 287 VAL AAA O   1 
ATOM 1985  C CB  . VAL A 1 270 ? 183.105 -10.090 18.892  1.000 70.130  ? 287 VAL AAA CB  1 
ATOM 1986  C CG1 . VAL A 1 270 ? 182.347 -11.385 18.617  1.000 73.450  ? 287 VAL AAA CG1 1 
ATOM 1987  C CG2 . VAL A 1 270 ? 182.252 -9.166  19.751  1.000 69.610  ? 287 VAL AAA CG2 1 
ATOM 1988  N N   . LYS A 1 271 ? 185.546 -12.501 18.890  1.000 81.630  ? 288 LYS AAA N   1 
ATOM 1989  C CA  . LYS A 1 271 ? 186.175 -13.483 17.948  1.000 83.280  ? 288 LYS AAA CA  1 
ATOM 1990  C C   . LYS A 1 271 ? 185.049 -14.195 17.165  1.000 93.500  ? 288 LYS AAA C   1 
ATOM 1991  O O   . LYS A 1 271 ? 184.140 -14.746 17.826  1.000 97.020  ? 288 LYS AAA O   1 
ATOM 1992  C CB  . LYS A 1 271 ? 187.112 -14.460 18.672  1.000 66.960  ? 288 LYS AAA CB  1 
ATOM 1993  N N   . ASN A 1 272 ? 185.126 -14.169 15.817  1.000 93.350  ? 289 ASN AAA N   1 
ATOM 1994  C CA  . ASN A 1 272 ? 184.026 -14.451 14.853  1.000 79.280  ? 289 ASN AAA CA  1 
ATOM 1995  C C   . ASN A 1 272 ? 183.617 -15.928 14.911  1.000 78.990  ? 289 ASN AAA C   1 
ATOM 1996  O O   . ASN A 1 272 ? 184.168 -16.787 14.237  1.000 76.060  ? 289 ASN AAA O   1 
ATOM 1997  C CB  . ASN A 1 272 ? 184.450 -14.054 13.463  1.000 70.040  ? 289 ASN AAA CB  1 
ATOM 1998  N N   . VAL B 1 7   ? 177.180 25.214  28.158  1.000 64.840  ? 24  VAL BBB N   1 
ATOM 1999  C CA  . VAL B 1 7   ? 177.105 23.883  27.475  1.000 75.700  ? 24  VAL BBB CA  1 
ATOM 2000  C C   . VAL B 1 7   ? 178.076 22.900  28.149  1.000 88.090  ? 24  VAL BBB C   1 
ATOM 2001  O O   . VAL B 1 7   ? 177.601 21.807  28.518  1.000 96.500  ? 24  VAL BBB O   1 
ATOM 2002  C CB  . VAL B 1 7   ? 177.351 24.013  25.980  1.000 70.710  ? 24  VAL BBB CB  1 
ATOM 2003  N N   . GLU B 1 8   ? 179.360 23.251  28.283  1.000 90.960  ? 25  GLU BBB N   1 
ATOM 2004  C CA  . GLU B 1 8   ? 180.344 22.450  29.056  1.000 93.170  ? 25  GLU BBB CA  1 
ATOM 2005  C C   . GLU B 1 8   ? 180.089 22.688  30.549  1.000 84.110  ? 25  GLU BBB C   1 
ATOM 2006  O O   . GLU B 1 8   ? 180.070 23.857  30.951  1.000 84.910  ? 25  GLU BBB O   1 
ATOM 2007  C CB  . GLU B 1 8   ? 181.788 22.811  28.685  1.000 107.300 ? 25  GLU BBB CB  1 
ATOM 2008  C CG  . GLU B 1 8   ? 182.810 21.790  29.177  1.000 110.790 ? 25  GLU BBB CG  1 
ATOM 2009  C CD  . GLU B 1 8   ? 184.270 22.227  29.231  1.000 104.680 ? 25  GLU BBB CD  1 
ATOM 2010  O OE1 . GLU B 1 8   ? 184.591 23.358  28.787  1.000 103.590 ? 25  GLU BBB OE1 1 
ATOM 2011  O OE2 . GLU B 1 8   ? 185.085 21.429  29.733  1.000 96.420  ? 25  GLU BBB OE2 1 
ATOM 2012  N N   . VAL B 1 9   ? 179.894 21.633  31.338  1.000 75.040  ? 26  VAL BBB N   1 
ATOM 2013  C CA  . VAL B 1 9   ? 179.548 21.759  32.784  1.000 71.730  ? 26  VAL BBB CA  1 
ATOM 2014  C C   . VAL B 1 9   ? 180.822 21.565  33.602  1.000 71.110  ? 26  VAL BBB C   1 
ATOM 2015  O O   . VAL B 1 9   ? 181.347 20.457  33.576  1.000 69.740  ? 26  VAL BBB O   1 
ATOM 2016  C CB  . VAL B 1 9   ? 178.458 20.762  33.219  1.000 63.990  ? 26  VAL BBB CB  1 
ATOM 2017  C CG1 . VAL B 1 9   ? 178.132 20.958  34.686  1.000 64.020  ? 26  VAL BBB CG1 1 
ATOM 2018  C CG2 . VAL B 1 9   ? 177.207 20.880  32.370  1.000 59.210  ? 26  VAL BBB CG2 1 
ATOM 2019  N N   . LEU B 1 10  ? 181.279 22.595  34.311  1.000 77.070  ? 27  LEU BBB N   1 
ATOM 2020  C CA  . LEU B 1 10  ? 182.474 22.527  35.197  1.000 79.570  ? 27  LEU BBB CA  1 
ATOM 2021  C C   . LEU B 1 10  ? 181.998 22.222  36.625  1.000 75.730  ? 27  LEU BBB C   1 
ATOM 2022  O O   . LEU B 1 10  ? 180.907 21.718  36.753  1.000 65.210  ? 27  LEU BBB O   1 
ATOM 2023  C CB  . LEU B 1 10  ? 183.265 23.839  35.077  1.000 81.070  ? 27  LEU BBB CB  1 
ATOM 2024  C CG  . LEU B 1 10  ? 184.455 23.840  34.107  1.000 77.790  ? 27  LEU BBB CG  1 
ATOM 2025  C CD1 . LEU B 1 10  ? 185.574 22.916  34.601  1.000 74.440  ? 27  LEU BBB CD1 1 
ATOM 2026  C CD2 . LEU B 1 10  ? 184.024 23.462  32.695  1.000 74.760  ? 27  LEU BBB CD2 1 
ATOM 2027  N N   . GLU B 1 11  ? 182.811 22.501  37.638  1.000 87.430  ? 28  GLU BBB N   1 
ATOM 2028  C CA  . GLU B 1 11  ? 182.629 22.001  39.030  1.000 90.380  ? 28  GLU BBB CA  1 
ATOM 2029  C C   . GLU B 1 11  ? 181.598 22.883  39.766  1.000 82.890  ? 28  GLU BBB C   1 
ATOM 2030  O O   . GLU B 1 11  ? 181.259 23.986  39.263  1.000 69.670  ? 28  GLU BBB O   1 
ATOM 2031  C CB  . GLU B 1 11  ? 183.999 21.881  39.710  1.000 91.260  ? 28  GLU BBB CB  1 
ATOM 2032  C CG  . GLU B 1 11  ? 184.523 23.171  40.322  1.000 101.670 ? 28  GLU BBB CG  1 
ATOM 2033  C CD  . GLU B 1 11  ? 184.678 24.416  39.443  1.000 115.620 ? 28  GLU BBB CD  1 
ATOM 2034  O OE1 . GLU B 1 11  ? 184.523 24.345  38.200  1.000 121.140 ? 28  GLU BBB OE1 1 
ATOM 2035  O OE2 . GLU B 1 11  ? 184.979 25.486  40.013  1.000 132.740 ? 28  GLU BBB OE2 1 
ATOM 2036  N N   . VAL B 1 12  ? 181.069 22.372  40.884  1.000 76.160  ? 29  VAL BBB N   1 
ATOM 2037  C CA  . VAL B 1 12  ? 180.028 23.035  41.723  1.000 71.030  ? 29  VAL BBB CA  1 
ATOM 2038  C C   . VAL B 1 12  ? 180.719 24.093  42.583  1.000 68.370  ? 29  VAL BBB C   1 
ATOM 2039  O O   . VAL B 1 12  ? 181.583 23.704  43.360  1.000 67.250  ? 29  VAL BBB O   1 
ATOM 2040  C CB  . VAL B 1 12  ? 179.292 22.016  42.620  1.000 69.420  ? 29  VAL BBB CB  1 
ATOM 2041  C CG1 . VAL B 1 12  ? 178.265 22.696  43.524  1.000 72.490  ? 29  VAL BBB CG1 1 
ATOM 2042  C CG2 . VAL B 1 12  ? 178.640 20.886  41.827  1.000 64.140  ? 29  VAL BBB CG2 1 
ATOM 2043  N N   . LYS B 1 13  ? 180.345 25.366  42.469  1.000 75.020  ? 30  LYS BBB N   1 
ATOM 2044  C CA  . LYS B 1 13  ? 180.819 26.433  43.395  1.000 87.060  ? 30  LYS BBB CA  1 
ATOM 2045  C C   . LYS B 1 13  ? 180.166 26.193  44.762  1.000 91.460  ? 30  LYS BBB C   1 
ATOM 2046  O O   . LYS B 1 13  ? 178.931 26.029  44.786  1.000 99.570  ? 30  LYS BBB O   1 
ATOM 2047  C CB  . LYS B 1 13  ? 180.482 27.830  42.862  1.000 96.370  ? 30  LYS BBB CB  1 
ATOM 2048  C CG  . LYS B 1 13  ? 181.209 28.980  43.549  1.000 101.790 ? 30  LYS BBB CG  1 
ATOM 2049  C CD  . LYS B 1 13  ? 182.697 29.067  43.218  1.000 107.450 ? 30  LYS BBB CD  1 
ATOM 2050  C CE  . LYS B 1 13  ? 182.968 29.484  41.783  1.000 100.680 ? 30  LYS BBB CE  1 
ATOM 2051  N NZ  . LYS B 1 13  ? 184.395 29.344  41.423  1.000 87.970  ? 30  LYS BBB NZ  1 
ATOM 2052  N N   . THR B 1 14  ? 180.966 26.110  45.837  1.000 96.740  ? 31  THR BBB N   1 
ATOM 2053  C CA  . THR B 1 14  ? 180.514 26.128  47.263  1.000 92.490  ? 31  THR BBB CA  1 
ATOM 2054  C C   . THR B 1 14  ? 180.916 27.473  47.884  1.000 84.930  ? 31  THR BBB C   1 
ATOM 2055  O O   . THR B 1 14  ? 181.615 28.248  47.193  1.000 90.700  ? 31  THR BBB O   1 
ATOM 2056  C CB  . THR B 1 14  ? 181.073 24.957  48.092  1.000 91.440  ? 31  THR BBB CB  1 
ATOM 2057  O OG1 . THR B 1 14  ? 182.496 25.071  48.130  1.000 80.170  ? 31  THR BBB OG1 1 
ATOM 2058  C CG2 . THR B 1 14  ? 180.667 23.591  47.574  1.000 88.000  ? 31  THR BBB CG2 1 
ATOM 2059  N N   . GLY B 1 15  ? 180.499 27.734  49.125  1.000 78.440  ? 32  GLY BBB N   1 
ATOM 2060  C CA  . GLY B 1 15  ? 180.781 28.994  49.835  1.000 89.700  ? 32  GLY BBB CA  1 
ATOM 2061  C C   . GLY B 1 15  ? 179.537 29.611  50.453  1.000 97.270  ? 32  GLY BBB C   1 
ATOM 2062  O O   . GLY B 1 15  ? 178.514 28.917  50.511  1.000 85.610  ? 32  GLY BBB O   1 
ATOM 2063  N N   . VAL B 1 16  ? 179.638 30.881  50.865  1.000 106.690 ? 33  VAL BBB N   1 
ATOM 2064  C CA  . VAL B 1 16  ? 178.646 31.576  51.750  1.000 98.090  ? 33  VAL BBB CA  1 
ATOM 2065  C C   . VAL B 1 16  ? 177.360 31.827  50.973  1.000 87.340  ? 33  VAL BBB C   1 
ATOM 2066  O O   . VAL B 1 16  ? 176.289 31.857  51.622  1.000 96.130  ? 33  VAL BBB O   1 
ATOM 2067  C CB  . VAL B 1 16  ? 179.221 32.885  52.334  1.000 81.240  ? 33  VAL BBB CB  1 
ATOM 2068  N N   . ASP B 1 17  ? 177.417 31.996  49.648  1.000 72.720  ? 34  ASP BBB N   1 
ATOM 2069  C CA  . ASP B 1 17  ? 176.216 32.376  48.857  1.000 74.960  ? 34  ASP BBB CA  1 
ATOM 2070  C C   . ASP B 1 17  ? 176.091 31.476  47.628  1.000 75.890  ? 34  ASP BBB C   1 
ATOM 2071  O O   . ASP B 1 17  ? 175.905 32.030  46.538  1.000 80.220  ? 34  ASP BBB O   1 
ATOM 2072  C CB  . ASP B 1 17  ? 176.250 33.864  48.498  1.000 72.390  ? 34  ASP BBB CB  1 
ATOM 2073  C CG  . ASP B 1 17  ? 175.298 34.706  49.326  1.000 71.080  ? 34  ASP BBB CG  1 
ATOM 2074  O OD1 . ASP B 1 17  ? 174.735 34.175  50.293  1.000 69.120  ? 34  ASP BBB OD1 1 
ATOM 2075  O OD2 . ASP B 1 17  ? 175.115 35.882  48.980  1.000 71.670  ? 34  ASP BBB OD2 1 
ATOM 2076  N N   . SER B 1 18  ? 176.164 30.155  47.808  1.000 70.510  ? 35  SER BBB N   1 
ATOM 2077  C CA  . SER B 1 18  ? 176.197 29.184  46.684  1.000 65.280  ? 35  SER BBB CA  1 
ATOM 2078  C C   . SER B 1 18  ? 174.856 28.461  46.509  1.000 65.130  ? 35  SER BBB C   1 
ATOM 2079  O O   . SER B 1 18  ? 174.656 27.919  45.407  1.000 76.280  ? 35  SER BBB O   1 
ATOM 2080  C CB  . SER B 1 18  ? 177.334 28.218  46.815  1.000 62.450  ? 35  SER BBB CB  1 
ATOM 2081  O OG  . SER B 1 18  ? 177.488 27.808  48.154  1.000 62.310  ? 35  SER BBB OG  1 
ATOM 2082  N N   . ILE B 1 19  ? 173.973 28.472  47.510  1.000 59.640  ? 36  ILE BBB N   1 
ATOM 2083  C CA  . ILE B 1 19  ? 172.652 27.766  47.432  1.000 53.720  ? 36  ILE BBB CA  1 
ATOM 2084  C C   . ILE B 1 19  ? 171.540 28.831  47.476  1.000 43.750  ? 36  ILE BBB C   1 
ATOM 2085  O O   . ILE B 1 19  ? 171.808 29.931  47.980  1.000 33.460  ? 36  ILE BBB O   1 
ATOM 2086  C CB  . ILE B 1 19  ? 172.528 26.668  48.522  1.000 57.750  ? 36  ILE BBB CB  1 
ATOM 2087  C CG1 . ILE B 1 19  ? 171.387 25.674  48.230  1.000 69.950  ? 36  ILE BBB CG1 1 
ATOM 2088  C CG2 . ILE B 1 19  ? 172.386 27.296  49.900  1.000 57.270  ? 36  ILE BBB CG2 1 
ATOM 2089  C CD1 . ILE B 1 19  ? 171.668 24.192  48.546  1.000 69.830  ? 36  ILE BBB CD1 1 
ATOM 2090  N N   . THR B 1 20  ? 170.369 28.530  46.904  1.000 41.570  ? 37  THR BBB N   1 
ATOM 2091  C CA  . THR B 1 20  ? 169.118 29.337  46.993  1.000 42.050  ? 37  THR BBB CA  1 
ATOM 2092  C C   . THR B 1 20  ? 167.900 28.410  46.838  1.000 42.830  ? 37  THR BBB C   1 
ATOM 2093  O O   . THR B 1 20  ? 168.107 27.230  46.493  1.000 42.940  ? 37  THR BBB O   1 
ATOM 2094  C CB  . THR B 1 20  ? 169.094 30.458  45.952  1.000 41.120  ? 37  THR BBB CB  1 
ATOM 2095  O OG1 . THR B 1 20  ? 168.013 31.347  46.226  1.000 42.150  ? 37  THR BBB OG1 1 
ATOM 2096  C CG2 . THR B 1 20  ? 168.932 29.932  44.548  1.000 40.720  ? 37  THR BBB CG2 1 
ATOM 2097  N N   . GLU B 1 21  ? 166.688 28.916  47.114  1.000 44.140  ? 38  GLU BBB N   1 
ATOM 2098  C CA  . GLU B 1 21  ? 165.407 28.151  47.136  1.000 43.350  ? 38  GLU BBB CA  1 
ATOM 2099  C C   . GLU B 1 21  ? 164.302 28.928  46.438  1.000 37.910  ? 38  GLU BBB C   1 
ATOM 2100  O O   . GLU B 1 21  ? 164.079 30.070  46.809  1.000 38.730  ? 38  GLU BBB O   1 
ATOM 2101  C CB  . GLU B 1 21  ? 164.873 27.905  48.549  1.000 48.420  ? 38  GLU BBB CB  1 
ATOM 2102  C CG  . GLU B 1 21  ? 165.630 26.834  49.310  1.000 53.120  ? 38  GLU BBB CG  1 
ATOM 2103  C CD  . GLU B 1 21  ? 164.949 26.427  50.589  1.000 54.430  ? 38  GLU BBB CD  1 
ATOM 2104  O OE1 . GLU B 1 21  ? 163.938 27.089  50.949  1.000 59.480  ? 38  GLU BBB OE1 1 
ATOM 2105  O OE2 . GLU B 1 21  ? 165.407 25.444  51.197  1.000 56.360  ? 38  GLU BBB OE2 1 
ATOM 2106  N N   . VAL B 1 22  ? 163.629 28.295  45.485  1.000 37.540  ? 39  VAL BBB N   1 
ATOM 2107  C CA  . VAL B 1 22  ? 162.286 28.718  45.014  1.000 36.550  ? 39  VAL BBB CA  1 
ATOM 2108  C C   . VAL B 1 22  ? 161.256 27.838  45.719  1.000 41.720  ? 39  VAL BBB C   1 
ATOM 2109  O O   . VAL B 1 22  ? 161.507 26.629  45.891  1.000 42.160  ? 39  VAL BBB O   1 
ATOM 2110  C CB  . VAL B 1 22  ? 162.157 28.612  43.495  1.000 34.690  ? 39  VAL BBB CB  1 
ATOM 2111  C CG1 . VAL B 1 22  ? 160.738 28.922  43.056  1.000 34.830  ? 39  VAL BBB CG1 1 
ATOM 2112  C CG2 . VAL B 1 22  ? 163.162 29.507  42.792  1.000 35.270  ? 39  VAL BBB CG2 1 
ATOM 2113  N N   . GLU B 1 23  ? 160.150 28.451  46.133  1.000 43.400  ? 40  GLU BBB N   1 
ATOM 2114  C CA  . GLU B 1 23  ? 158.988 27.777  46.751  1.000 39.320  ? 40  GLU BBB CA  1 
ATOM 2115  C C   . GLU B 1 23  ? 157.752 28.501  46.234  1.000 34.530  ? 40  GLU BBB C   1 
ATOM 2116  O O   . GLU B 1 23  ? 157.568 29.630  46.606  1.000 35.350  ? 40  GLU BBB O   1 
ATOM 2117  C CB  . GLU B 1 23  ? 159.129 27.851  48.270  1.000 41.810  ? 40  GLU BBB CB  1 
ATOM 2118  C CG  . GLU B 1 23  ? 158.138 27.007  49.047  1.000 46.810  ? 40  GLU BBB CG  1 
ATOM 2119  C CD  . GLU B 1 23  ? 158.207 27.189  50.558  1.000 48.900  ? 40  GLU BBB CD  1 
ATOM 2120  O OE1 . GLU B 1 23  ? 157.850 28.286  51.015  1.000 56.740  ? 40  GLU BBB OE1 1 
ATOM 2121  O OE2 . GLU B 1 23  ? 158.596 26.244  51.277  1.000 47.750  ? 40  GLU BBB OE2 1 
ATOM 2122  N N   . CYS B 1 24  ? 156.981 27.913  45.340  1.000 33.480  ? 41  CYS BBB N   1 
ATOM 2123  C CA  . CYS B 1 24  ? 155.704 28.521  44.917  1.000 37.970  ? 41  CYS BBB CA  1 
ATOM 2124  C C   . CYS B 1 24  ? 154.635 27.438  44.744  1.000 39.140  ? 41  CYS BBB C   1 
ATOM 2125  O O   . CYS B 1 24  ? 154.943 26.252  44.979  1.000 36.750  ? 41  CYS BBB O   1 
ATOM 2126  C CB  . CYS B 1 24  ? 155.919 29.310  43.637  1.000 40.670  ? 41  CYS BBB CB  1 
ATOM 2127  S SG  . CYS B 1 24  ? 156.263 28.218  42.241  1.000 40.930  ? 41  CYS BBB SG  1 
ATOM 2128  N N   . PHE B 1 25  ? 153.411 27.856  44.399  1.000 38.820  ? 42  PHE BBB N   1 
ATOM 2129  C CA  . PHE B 1 25  ? 152.276 26.976  44.021  1.000 38.180  ? 42  PHE BBB CA  1 
ATOM 2130  C C   . PHE B 1 25  ? 151.904 27.335  42.586  1.000 37.180  ? 42  PHE BBB C   1 
ATOM 2131  O O   . PHE B 1 25  ? 152.119 28.489  42.240  1.000 36.170  ? 42  PHE BBB O   1 
ATOM 2132  C CB  . PHE B 1 25  ? 151.101 27.126  44.994  1.000 42.280  ? 42  PHE BBB CB  1 
ATOM 2133  C CG  . PHE B 1 25  ? 150.547 28.517  45.039  1.000 48.590  ? 42  PHE BBB CG  1 
ATOM 2134  C CD1 . PHE B 1 25  ? 149.694 28.979  44.048  1.000 54.690  ? 42  PHE BBB CD1 1 
ATOM 2135  C CD2 . PHE B 1 25  ? 150.905 29.382  46.054  1.000 56.250  ? 42  PHE BBB CD2 1 
ATOM 2136  C CE1 . PHE B 1 25  ? 149.213 30.283  44.067  1.000 58.290  ? 42  PHE BBB CE1 1 
ATOM 2137  C CE2 . PHE B 1 25  ? 150.413 30.682  46.084  1.000 59.990  ? 42  PHE BBB CE2 1 
ATOM 2138  C CZ  . PHE B 1 25  ? 149.571 31.132  45.087  1.000 60.830  ? 42  PHE BBB CZ  1 
ATOM 2139  N N   . LEU B 1 26  ? 151.461 26.367  41.773  1.000 41.120  ? 43  LEU BBB N   1 
ATOM 2140  C CA  . LEU B 1 26  ? 150.883 26.581  40.415  1.000 36.040  ? 43  LEU BBB CA  1 
ATOM 2141  C C   . LEU B 1 26  ? 149.395 26.238  40.490  1.000 31.300  ? 43  LEU BBB C   1 
ATOM 2142  O O   . LEU B 1 26  ? 149.064 25.212  41.062  1.000 31.210  ? 43  LEU BBB O   1 
ATOM 2143  C CB  . LEU B 1 26  ? 151.570 25.695  39.374  1.000 34.700  ? 43  LEU BBB CB  1 
ATOM 2144  C CG  . LEU B 1 26  ? 152.756 26.332  38.659  1.000 34.580  ? 43  LEU BBB CG  1 
ATOM 2145  C CD1 . LEU B 1 26  ? 153.936 26.506  39.606  1.000 35.320  ? 43  LEU BBB CD1 1 
ATOM 2146  C CD2 . LEU B 1 26  ? 153.168 25.499  37.463  1.000 36.470  ? 43  LEU BBB CD2 1 
ATOM 2147  N N   . THR B 1 27  ? 148.546 27.086  39.966  1.000 29.940  ? 44  THR BBB N   1 
ATOM 2148  C CA  . THR B 1 27  ? 147.090 26.843  40.007  1.000 32.450  ? 44  THR BBB CA  1 
ATOM 2149  C C   . THR B 1 27  ? 146.733 26.037  38.770  1.000 33.520  ? 44  THR BBB C   1 
ATOM 2150  O O   . THR B 1 27  ? 147.484 25.971  37.802  1.000 33.830  ? 44  THR BBB O   1 
ATOM 2151  C CB  . THR B 1 27  ? 146.298 28.143  40.164  1.000 33.240  ? 44  THR BBB CB  1 
ATOM 2152  O OG1 . THR B 1 27  ? 146.262 28.811  38.912  1.000 36.400  ? 44  THR BBB OG1 1 
ATOM 2153  C CG2 . THR B 1 27  ? 146.894 29.052  41.199  1.000 35.320  ? 44  THR BBB CG2 1 
ATOM 2154  N N   . PRO B 1 28  ? 145.611 25.312  38.821  1.000 36.090  ? 45  PRO BBB N   1 
ATOM 2155  C CA  . PRO B 1 28  ? 145.157 24.550  37.668  1.000 43.190  ? 45  PRO BBB CA  1 
ATOM 2156  C C   . PRO B 1 28  ? 144.287 25.368  36.704  1.000 48.710  ? 45  PRO BBB C   1 
ATOM 2157  O O   . PRO B 1 28  ? 143.331 25.968  37.156  1.000 48.970  ? 45  PRO BBB O   1 
ATOM 2158  C CB  . PRO B 1 28  ? 144.357 23.436  38.361  1.000 41.120  ? 45  PRO BBB CB  1 
ATOM 2159  C CG  . PRO B 1 28  ? 143.775 24.089  39.594  1.000 37.820  ? 45  PRO BBB CG  1 
ATOM 2160  C CD  . PRO B 1 28  ? 144.814 25.087  40.029  1.000 35.620  ? 45  PRO BBB CD  1 
ATOM 2161  N N   . GLU B 1 29  ? 144.590 25.315  35.402  1.000 52.010  ? 46  GLU BBB N   1 
ATOM 2162  C CA  . GLU B 1 29  ? 143.703 25.897  34.357  1.000 52.060  ? 46  GLU BBB CA  1 
ATOM 2163  C C   . GLU B 1 29  ? 142.904 24.746  33.761  1.000 43.680  ? 46  GLU BBB C   1 
ATOM 2164  O O   . GLU B 1 29  ? 143.422 24.045  32.899  1.000 40.210  ? 46  GLU BBB O   1 
ATOM 2165  C CB  . GLU B 1 29  ? 144.499 26.684  33.318  1.000 59.490  ? 46  GLU BBB CB  1 
ATOM 2166  C CG  . GLU B 1 29  ? 145.365 27.780  33.944  1.000 69.430  ? 46  GLU BBB CG  1 
ATOM 2167  C CD  . GLU B 1 29  ? 144.567 28.871  34.643  1.000 69.550  ? 46  GLU BBB CD  1 
ATOM 2168  O OE1 . GLU B 1 29  ? 145.148 29.576  35.491  1.000 61.870  ? 46  GLU BBB OE1 1 
ATOM 2169  O OE2 . GLU B 1 29  ? 143.362 28.999  34.318  1.000 69.890  ? 46  GLU BBB OE2 1 
ATOM 2170  N N   . MET B 1 30  ? 141.698 24.545  34.269  1.000 38.840  ? 47  MET BBB N   1 
ATOM 2171  C CA  . MET B 1 30  ? 140.829 23.406  33.920  1.000 36.520  ? 47  MET BBB CA  1 
ATOM 2172  C C   . MET B 1 30  ? 139.807 23.835  32.879  1.000 35.150  ? 47  MET BBB C   1 
ATOM 2173  O O   . MET B 1 30  ? 139.052 22.972  32.476  1.000 34.760  ? 47  MET BBB O   1 
ATOM 2174  C CB  . MET B 1 30  ? 140.086 22.903  35.163  1.000 37.880  ? 47  MET BBB CB  1 
ATOM 2175  C CG  . MET B 1 30  ? 140.952 22.113  36.114  1.000 36.590  ? 47  MET BBB CG  1 
ATOM 2176  S SD  . MET B 1 30  ? 141.785 20.718  35.311  1.000 35.110  ? 47  MET BBB SD  1 
ATOM 2177  C CE  . MET B 1 30  ? 143.489 21.271  35.416  1.000 38.520  ? 47  MET BBB CE  1 
ATOM 2178  N N   . GLY B 1 31  ? 139.766 25.107  32.475  1.000 38.590  ? 48  GLY BBB N   1 
ATOM 2179  C CA  . GLY B 1 31  ? 138.793 25.606  31.470  1.000 43.030  ? 48  GLY BBB CA  1 
ATOM 2180  C C   . GLY B 1 31  ? 137.988 26.798  31.961  1.000 45.090  ? 48  GLY BBB C   1 
ATOM 2181  O O   . GLY B 1 31  ? 137.553 27.583  31.102  1.000 44.700  ? 48  GLY BBB O   1 
ATOM 2182  N N   . ASP B 1 32  ? 137.784 26.886  33.286  1.000 49.710  ? 49  ASP BBB N   1 
ATOM 2183  C CA  . ASP B 1 32  ? 137.321 28.068  34.066  1.000 48.860  ? 49  ASP BBB CA  1 
ATOM 2184  C C   . ASP B 1 32  ? 136.154 28.700  33.331  1.000 45.040  ? 49  ASP BBB C   1 
ATOM 2185  O O   . ASP B 1 32  ? 136.244 29.837  32.843  1.000 38.360  ? 49  ASP BBB O   1 
ATOM 2186  C CB  . ASP B 1 32  ? 138.475 29.045  34.329  1.000 55.450  ? 49  ASP BBB CB  1 
ATOM 2187  C CG  . ASP B 1 32  ? 139.553 28.581  35.311  1.000 63.130  ? 49  ASP BBB CG  1 
ATOM 2188  O OD1 . ASP B 1 32  ? 139.627 27.378  35.656  1.000 63.570  ? 49  ASP BBB OD1 1 
ATOM 2189  O OD2 . ASP B 1 32  ? 140.332 29.447  35.732  1.000 75.990  ? 49  ASP BBB OD2 1 
ATOM 2190  N N   . PRO B 1 33  ? 135.016 27.967  33.257  1.000 45.320  ? 50  PRO BBB N   1 
ATOM 2191  C CA  . PRO B 1 33  ? 133.841 28.432  32.519  1.000 48.230  ? 50  PRO BBB CA  1 
ATOM 2192  C C   . PRO B 1 33  ? 133.556 29.906  32.848  1.000 50.890  ? 50  PRO BBB C   1 
ATOM 2193  O O   . PRO B 1 33  ? 133.747 30.743  31.991  1.000 60.340  ? 50  PRO BBB O   1 
ATOM 2194  C CB  . PRO B 1 33  ? 132.695 27.532  33.008  1.000 43.460  ? 50  PRO BBB CB  1 
ATOM 2195  C CG  . PRO B 1 33  ? 133.390 26.270  33.497  1.000 42.590  ? 50  PRO BBB CG  1 
ATOM 2196  C CD  . PRO B 1 33  ? 134.779 26.684  33.940  1.000 43.490  ? 50  PRO BBB CD  1 
ATOM 2197  N N   . ASP B 1 34  ? 133.204 30.190  34.099  1.000 44.790  ? 51  ASP BBB N   1 
ATOM 2198  C CA  . ASP B 1 34  ? 132.577 31.463  34.511  1.000 40.280  ? 51  ASP BBB CA  1 
ATOM 2199  C C   . ASP B 1 34  ? 133.248 31.927  35.810  1.000 41.520  ? 51  ASP BBB C   1 
ATOM 2200  O O   . ASP B 1 34  ? 134.152 31.231  36.290  1.000 37.780  ? 51  ASP BBB O   1 
ATOM 2201  C CB  . ASP B 1 34  ? 131.051 31.263  34.553  1.000 34.590  ? 51  ASP BBB CB  1 
ATOM 2202  C CG  . ASP B 1 34  ? 130.467 30.747  35.856  1.000 30.170  ? 51  ASP BBB CG  1 
ATOM 2203  O OD1 . ASP B 1 34  ? 131.219 30.484  36.812  1.000 25.840  ? 51  ASP BBB OD1 1 
ATOM 2204  O OD2 . ASP B 1 34  ? 129.250 30.628  35.902  1.000 29.440  ? 51  ASP BBB OD2 1 
ATOM 2205  N N   . GLU B 1 35  ? 132.778 33.048  36.370  1.000 44.660  ? 52  GLU BBB N   1 
ATOM 2206  C CA  . GLU B 1 35  ? 133.413 33.781  37.503  1.000 41.230  ? 52  GLU BBB CA  1 
ATOM 2207  C C   . GLU B 1 35  ? 133.423 32.932  38.779  1.000 38.420  ? 52  GLU BBB C   1 
ATOM 2208  O O   . GLU B 1 35  ? 134.177 33.291  39.689  1.000 32.850  ? 52  GLU BBB O   1 
ATOM 2209  C CB  . GLU B 1 35  ? 132.722 35.133  37.736  1.000 45.190  ? 52  GLU BBB CB  1 
ATOM 2210  C CG  . GLU B 1 35  ? 131.229 35.051  38.037  1.000 45.990  ? 52  GLU BBB CG  1 
ATOM 2211  C CD  . GLU B 1 35  ? 130.501 36.380  37.992  1.000 46.470  ? 52  GLU BBB CD  1 
ATOM 2212  O OE1 . GLU B 1 35  ? 131.137 37.431  38.254  1.000 43.690  ? 52  GLU BBB OE1 1 
ATOM 2213  O OE2 . GLU B 1 35  ? 129.311 36.357  37.668  1.000 48.850  ? 52  GLU BBB OE2 1 
ATOM 2214  N N   . HIS B 1 36  ? 132.665 31.836  38.822  1.000 39.690  ? 53  HIS BBB N   1 
ATOM 2215  C CA  . HIS B 1 36  ? 132.322 31.094  40.061  1.000 41.380  ? 53  HIS BBB CA  1 
ATOM 2216  C C   . HIS B 1 36  ? 132.898 29.664  40.087  1.000 45.100  ? 53  HIS BBB C   1 
ATOM 2217  O O   . HIS B 1 36  ? 132.657 28.944  41.112  1.000 45.250  ? 53  HIS BBB O   1 
ATOM 2218  C CB  . HIS B 1 36  ? 130.808 31.000  40.148  1.000 45.090  ? 53  HIS BBB CB  1 
ATOM 2219  C CG  . HIS B 1 36  ? 130.104 32.277  40.449  1.000 53.170  ? 53  HIS BBB CG  1 
ATOM 2220  N ND1 . HIS B 1 36  ? 130.290 32.952  41.632  1.000 54.770  ? 53  HIS BBB ND1 1 
ATOM 2221  C CD2 . HIS B 1 36  ? 129.152 32.938  39.772  1.000 65.460  ? 53  HIS BBB CD2 1 
ATOM 2222  C CE1 . HIS B 1 36  ? 129.508 34.011  41.653  1.000 67.820  ? 53  HIS BBB CE1 1 
ATOM 2223  N NE2 . HIS B 1 36  ? 128.792 34.035  40.510  1.000 72.020  ? 53  HIS BBB NE2 1 
ATOM 2224  N N   . LEU B 1 37  ? 133.583 29.240  39.009  1.000 40.740  ? 54  LEU BBB N   1 
ATOM 2225  C CA  . LEU B 1 37  ? 133.919 27.817  38.747  1.000 33.530  ? 54  LEU BBB CA  1 
ATOM 2226  C C   . LEU B 1 37  ? 135.405 27.657  38.420  1.000 33.050  ? 54  LEU BBB C   1 
ATOM 2227  O O   . LEU B 1 37  ? 135.782 26.706  37.697  1.000 32.580  ? 54  LEU BBB O   1 
ATOM 2228  C CB  . LEU B 1 37  ? 133.041 27.302  37.607  1.000 30.160  ? 54  LEU BBB CB  1 
ATOM 2229  C CG  . LEU B 1 37  ? 131.565 27.157  37.951  1.000 29.060  ? 54  LEU BBB CG  1 
ATOM 2230  C CD1 . LEU B 1 37  ? 130.771 26.740  36.746  1.000 30.180  ? 54  LEU BBB CD1 1 
ATOM 2231  C CD2 . LEU B 1 37  ? 131.352 26.145  39.061  1.000 29.320  ? 54  LEU BBB CD2 1 
ATOM 2232  N N   . ARG B 1 38  ? 136.241 28.524  38.971  1.000 34.120  ? 55  ARG BBB N   1 
ATOM 2233  C CA  . ARG B 1 38  ? 137.715 28.411  38.839  1.000 37.030  ? 55  ARG BBB CA  1 
ATOM 2234  C C   . ARG B 1 38  ? 138.132 27.043  39.386  1.000 33.830  ? 55  ARG BBB C   1 
ATOM 2235  O O   . ARG B 1 38  ? 137.730 26.711  40.508  1.000 34.670  ? 55  ARG BBB O   1 
ATOM 2236  C CB  . ARG B 1 38  ? 138.342 29.572  39.603  1.000 41.530  ? 55  ARG BBB CB  1 
ATOM 2237  C CG  . ARG B 1 38  ? 139.849 29.615  39.545  1.000 45.480  ? 55  ARG BBB CG  1 
ATOM 2238  C CD  . ARG B 1 38  ? 140.368 30.767  38.709  1.000 49.890  ? 55  ARG BBB CD  1 
ATOM 2239  N NE  . ARG B 1 38  ? 141.794 30.848  38.983  1.000 57.300  ? 55  ARG BBB NE  1 
ATOM 2240  C CZ  . ARG B 1 38  ? 142.723 30.002  38.507  1.000 62.920  ? 55  ARG BBB CZ  1 
ATOM 2241  N NH1 . ARG B 1 38  ? 142.409 29.005  37.692  1.000 57.790  ? 55  ARG BBB NH1 1 
ATOM 2242  N NH2 . ARG B 1 38  ? 143.986 30.177  38.842  1.000 67.620  ? 55  ARG BBB NH2 1 
ATOM 2243  N N   . GLY B 1 39  ? 138.864 26.259  38.604  1.000 34.580  ? 56  GLY BBB N   1 
ATOM 2244  C CA  . GLY B 1 39  ? 139.310 24.910  39.008  1.000 33.070  ? 56  GLY BBB CA  1 
ATOM 2245  C C   . GLY B 1 39  ? 138.408 23.838  38.443  1.000 31.050  ? 56  GLY BBB C   1 
ATOM 2246  O O   . GLY B 1 39  ? 138.692 22.649  38.657  1.000 33.880  ? 56  GLY BBB O   1 
ATOM 2247  N N   . PHE B 1 40  ? 137.350 24.230  37.736  1.000 27.920  ? 57  PHE BBB N   1 
ATOM 2248  C CA  . PHE B 1 40  ? 136.483 23.285  36.995  1.000 26.280  ? 57  PHE BBB CA  1 
ATOM 2249  C C   . PHE B 1 40  ? 136.647 23.535  35.502  1.000 23.010  ? 57  PHE BBB C   1 
ATOM 2250  O O   . PHE B 1 40  ? 137.191 24.560  35.124  1.000 22.650  ? 57  PHE BBB O   1 
ATOM 2251  C CB  . PHE B 1 40  ? 135.018 23.448  37.406  1.000 27.340  ? 57  PHE BBB CB  1 
ATOM 2252  C CG  . PHE B 1 40  ? 134.732 23.152  38.855  1.000 26.350  ? 57  PHE BBB CG  1 
ATOM 2253  C CD1 . PHE B 1 40  ? 135.101 24.042  39.842  1.000 26.960  ? 57  PHE BBB CD1 1 
ATOM 2254  C CD2 . PHE B 1 40  ? 134.106 21.976  39.229  1.000 27.420  ? 57  PHE BBB CD2 1 
ATOM 2255  C CE1 . PHE B 1 40  ? 134.826 23.776  41.176  1.000 29.520  ? 57  PHE BBB CE1 1 
ATOM 2256  C CE2 . PHE B 1 40  ? 133.822 21.706  40.561  1.000 29.860  ? 57  PHE BBB CE2 1 
ATOM 2257  C CZ  . PHE B 1 40  ? 134.187 22.606  41.536  1.000 31.100  ? 57  PHE BBB CZ  1 
ATOM 2258  N N   . SER B 1 41  ? 136.194 22.586  34.692  1.000 19.990  ? 58  SER BBB N   1 
ATOM 2259  C CA  . SER B 1 41  ? 135.895 22.793  33.258  1.000 20.130  ? 58  SER BBB CA  1 
ATOM 2260  C C   . SER B 1 41  ? 134.406 23.049  33.128  1.000 20.710  ? 58  SER BBB C   1 
ATOM 2261  O O   . SER B 1 41  ? 133.698 22.912  34.146  1.000 19.480  ? 58  SER BBB O   1 
ATOM 2262  C CB  . SER B 1 41  ? 136.294 21.626  32.425  1.000 19.660  ? 58  SER BBB CB  1 
ATOM 2263  O OG  . SER B 1 41  ? 135.387 20.565  32.577  1.000 19.720  ? 58  SER BBB OG  1 
ATOM 2264  N N   . LYS B 1 42  ? 133.978 23.416  31.928  1.000 21.700  ? 59  LYS BBB N   1 
ATOM 2265  C CA  . LYS B 1 42  ? 132.547 23.534  31.593  1.000 25.490  ? 59  LYS BBB CA  1 
ATOM 2266  C C   . LYS B 1 42  ? 132.057 22.102  31.448  1.000 27.010  ? 59  LYS BBB C   1 
ATOM 2267  O O   . LYS B 1 42  ? 132.858 21.221  31.039  1.000 25.920  ? 59  LYS BBB O   1 
ATOM 2268  C CB  . LYS B 1 42  ? 132.318 24.339  30.309  1.000 31.150  ? 59  LYS BBB CB  1 
ATOM 2269  C CG  . LYS B 1 42  ? 130.848 24.487  29.902  1.000 33.340  ? 59  LYS BBB CG  1 
ATOM 2270  C CD  . LYS B 1 42  ? 130.557 25.654  28.945  1.000 36.370  ? 59  LYS BBB CD  1 
ATOM 2271  C CE  . LYS B 1 42  ? 130.569 25.277  27.474  1.000 41.750  ? 59  LYS BBB CE  1 
ATOM 2272  N NZ  . LYS B 1 42  ? 129.722 26.198  26.670  1.000 44.880  ? 59  LYS BBB NZ  1 
ATOM 2273  N N   . SER B 1 43  ? 130.797 21.881  31.782  1.000 29.360  ? 60  SER BBB N   1 
ATOM 2274  C CA  . SER B 1 43  ? 130.155 20.561  31.634  1.000 29.650  ? 60  SER BBB CA  1 
ATOM 2275  C C   . SER B 1 43  ? 130.397 20.066  30.208  1.000 26.790  ? 60  SER BBB C   1 
ATOM 2276  O O   . SER B 1 43  ? 130.057 20.793  29.255  1.000 25.810  ? 60  SER BBB O   1 
ATOM 2277  C CB  . SER B 1 43  ? 128.703 20.605  32.028  1.000 33.470  ? 60  SER BBB CB  1 
ATOM 2278  O OG  . SER B 1 43  ? 128.578 20.689  33.455  1.000 36.250  ? 60  SER BBB OG  1 
ATOM 2279  N N   . ILE B 1 44  ? 131.007 18.880  30.112  1.000 25.270  ? 61  ILE BBB N   1 
ATOM 2280  C CA  . ILE B 1 44  ? 131.531 18.261  28.865  1.000 23.400  ? 61  ILE BBB CA  1 
ATOM 2281  C C   . ILE B 1 44  ? 130.393 17.875  27.937  1.000 21.930  ? 61  ILE BBB C   1 
ATOM 2282  O O   . ILE B 1 44  ? 129.446 17.313  28.415  1.000 21.210  ? 61  ILE BBB O   1 
ATOM 2283  C CB  . ILE B 1 44  ? 132.395 17.053  29.220  1.000 22.400  ? 61  ILE BBB CB  1 
ATOM 2284  C CG1 . ILE B 1 44  ? 133.589 17.483  30.072  1.000 22.850  ? 61  ILE BBB CG1 1 
ATOM 2285  C CG2 . ILE B 1 44  ? 132.833 16.370  27.939  1.000 22.680  ? 61  ILE BBB CG2 1 
ATOM 2286  C CD1 . ILE B 1 44  ? 134.549 16.378  30.446  1.000 23.350  ? 61  ILE BBB CD1 1 
ATOM 2287  N N   . SER B 1 45  ? 130.481 18.215  26.662  1.000 22.070  ? 62  SER BBB N   1 
ATOM 2288  C CA  . SER B 1 45  ? 129.533 17.783  25.607  1.000 25.070  ? 62  SER BBB CA  1 
ATOM 2289  C C   . SER B 1 45  ? 130.321 16.973  24.581  1.000 25.420  ? 62  SER BBB C   1 
ATOM 2290  O O   . SER B 1 45  ? 131.541 17.081  24.592  1.000 26.820  ? 62  SER BBB O   1 
ATOM 2291  C CB  . SER B 1 45  ? 128.814 18.957  24.952  1.000 25.470  ? 62  SER BBB CB  1 
ATOM 2292  O OG  . SER B 1 45  ? 128.776 20.113  25.793  1.000 23.130  ? 62  SER BBB OG  1 
ATOM 2293  N N   . ILE B 1 46  ? 129.652 16.214  23.718  1.000 26.090  ? 63  ILE BBB N   1 
ATOM 2294  C CA  . ILE B 1 46  ? 130.279 15.247  22.768  1.000 28.100  ? 63  ILE BBB CA  1 
ATOM 2295  C C   . ILE B 1 46  ? 129.874 15.588  21.328  1.000 29.930  ? 63  ILE BBB C   1 
ATOM 2296  O O   . ILE B 1 46  ? 128.660 15.748  21.052  1.000 35.050  ? 63  ILE BBB O   1 
ATOM 2297  C CB  . ILE B 1 46  ? 129.837 13.820  23.123  1.000 31.750  ? 63  ILE BBB CB  1 
ATOM 2298  C CG1 . ILE B 1 46  ? 130.338 13.395  24.506  1.000 34.980  ? 63  ILE BBB CG1 1 
ATOM 2299  C CG2 . ILE B 1 46  ? 130.267 12.847  22.036  1.000 33.620  ? 63  ILE BBB CG2 1 
ATOM 2300  C CD1 . ILE B 1 46  ? 129.816 12.037  24.974  1.000 35.500  ? 63  ILE BBB CD1 1 
ATOM 2301  N N   . SER B 1 47  ? 130.823 15.612  20.399  1.000 29.900  ? 64  SER BBB N   1 
ATOM 2302  C CA  . SER B 1 47  ? 130.562 16.006  18.991  1.000 31.600  ? 64  SER BBB CA  1 
ATOM 2303  C C   . SER B 1 47  ? 129.404 15.206  18.393  1.000 30.410  ? 64  SER BBB C   1 
ATOM 2304  O O   . SER B 1 47  ? 129.193 14.048  18.797  1.000 35.790  ? 64  SER BBB O   1 
ATOM 2305  C CB  . SER B 1 47  ? 131.802 15.897  18.142  1.000 32.740  ? 64  SER BBB CB  1 
ATOM 2306  O OG  . SER B 1 47  ? 132.467 14.670  18.369  1.000 36.810  ? 64  SER BBB OG  1 
ATOM 2307  N N   . ASP B 1 48  ? 128.672 15.834  17.484  1.000 32.070  ? 65  ASP BBB N   1 
ATOM 2308  C CA  . ASP B 1 48  ? 127.585 15.215  16.688  1.000 35.030  ? 65  ASP BBB CA  1 
ATOM 2309  C C   . ASP B 1 48  ? 128.177 14.044  15.877  1.000 26.730  ? 65  ASP BBB C   1 
ATOM 2310  O O   . ASP B 1 48  ? 127.455 13.057  15.653  1.000 22.000  ? 65  ASP BBB O   1 
ATOM 2311  C CB  . ASP B 1 48  ? 126.816 16.273  15.866  1.000 44.260  ? 65  ASP BBB CB  1 
ATOM 2312  C CG  . ASP B 1 48  ? 127.667 17.084  14.865  1.000 61.960  ? 65  ASP BBB CG  1 
ATOM 2313  O OD1 . ASP B 1 48  ? 128.571 17.855  15.316  1.000 76.270  ? 65  ASP BBB OD1 1 
ATOM 2314  O OD2 . ASP B 1 48  ? 127.435 16.971  13.621  1.000 64.640  ? 65  ASP BBB OD2 1 
ATOM 2315  N N   . THR B 1 49  ? 129.446 14.125  15.475  1.000 24.310  ? 66  THR BBB N   1 
ATOM 2316  C CA  . THR B 1 49  ? 130.112 13.139  14.569  1.000 25.880  ? 66  THR BBB CA  1 
ATOM 2317  C C   . THR B 1 49  ? 131.619 13.089  14.829  1.000 25.140  ? 66  THR BBB C   1 
ATOM 2318  O O   . THR B 1 49  ? 132.171 14.074  15.363  1.000 24.760  ? 66  THR BBB O   1 
ATOM 2319  C CB  . THR B 1 49  ? 129.960 13.498  13.087  1.000 26.930  ? 66  THR BBB CB  1 
ATOM 2320  O OG1 . THR B 1 49  ? 130.691 14.708  12.862  1.000 25.890  ? 66  THR BBB OG1 1 
ATOM 2321  C CG2 . THR B 1 49  ? 128.519 13.657  12.652  1.000 27.720  ? 66  THR BBB CG2 1 
ATOM 2322  N N   . PHE B 1 50  ? 132.276 12.008  14.419  1.000 23.750  ? 67  PHE BBB N   1 
ATOM 2323  C CA  . PHE B 1 50  ? 133.718 11.826  14.720  1.000 25.590  ? 67  PHE BBB CA  1 
ATOM 2324  C C   . PHE B 1 50  ? 134.519 12.907  14.006  1.000 25.380  ? 67  PHE BBB C   1 
ATOM 2325  O O   . PHE B 1 50  ? 135.592 13.316  14.485  1.000 26.270  ? 67  PHE BBB O   1 
ATOM 2326  C CB  . PHE B 1 50  ? 134.213 10.446  14.291  1.000 26.560  ? 67  PHE BBB CB  1 
ATOM 2327  C CG  . PHE B 1 50  ? 135.579 10.094  14.819  1.000 24.660  ? 67  PHE BBB CG  1 
ATOM 2328  C CD1 . PHE B 1 50  ? 135.787 9.854   16.157  1.000 26.620  ? 67  PHE BBB CD1 1 
ATOM 2329  C CD2 . PHE B 1 50  ? 136.646 9.980   13.972  1.000 24.160  ? 67  PHE BBB CD2 1 
ATOM 2330  C CE1 . PHE B 1 50  ? 137.048 9.517   16.622  1.000 27.410  ? 67  PHE BBB CE1 1 
ATOM 2331  C CE2 . PHE B 1 50  ? 137.906 9.658   14.435  1.000 25.300  ? 67  PHE BBB CE2 1 
ATOM 2332  C CZ  . PHE B 1 50  ? 138.107 9.416   15.756  1.000 25.510  ? 67  PHE BBB CZ  1 
ATOM 2333  N N   . GLU B 1 51  ? 133.974 13.338  12.876  1.000 27.250  ? 68  GLU BBB N   1 
ATOM 2334  C CA  . GLU B 1 51  ? 134.607 14.242  11.890  1.000 27.740  ? 68  GLU BBB CA  1 
ATOM 2335  C C   . GLU B 1 51  ? 134.526 15.677  12.405  1.000 27.140  ? 68  GLU BBB C   1 
ATOM 2336  O O   . GLU B 1 51  ? 135.426 16.420  12.105  1.000 31.020  ? 68  GLU BBB O   1 
ATOM 2337  C CB  . GLU B 1 51  ? 133.919 14.068  10.533  1.000 29.180  ? 68  GLU BBB CB  1 
ATOM 2338  C CG  . GLU B 1 51  ? 134.161 12.689  9.925   1.000 30.590  ? 68  GLU BBB CG  1 
ATOM 2339  C CD  . GLU B 1 51  ? 133.090 11.624  10.106  1.000 30.960  ? 68  GLU BBB CD  1 
ATOM 2340  O OE1 . GLU B 1 51  ? 132.951 10.815  9.171   1.000 29.390  ? 68  GLU BBB OE1 1 
ATOM 2341  O OE2 . GLU B 1 51  ? 132.403 11.584  11.175  1.000 37.370  ? 68  GLU BBB OE2 1 
ATOM 2342  N N   . SER B 1 52  ? 133.502 16.017  13.187  1.000 27.660  ? 69  SER BBB N   1 
ATOM 2343  C CA  . SER B 1 52  ? 133.161 17.410  13.588  1.000 27.560  ? 69  SER BBB CA  1 
ATOM 2344  C C   . SER B 1 52  ? 133.606 17.725  15.022  1.000 31.040  ? 69  SER BBB C   1 
ATOM 2345  O O   . SER B 1 52  ? 133.120 18.732  15.573  1.000 30.300  ? 69  SER BBB O   1 
ATOM 2346  C CB  . SER B 1 52  ? 131.678 17.649  13.421  1.000 26.410  ? 69  SER BBB CB  1 
ATOM 2347  O OG  . SER B 1 52  ? 130.895 16.830  14.264  1.000 23.890  ? 69  SER BBB OG  1 
ATOM 2348  N N   . ASP B 1 53  ? 134.441 16.883  15.639  1.000 34.060  ? 70  ASP BBB N   1 
ATOM 2349  C CA  . ASP B 1 53  ? 134.952 17.136  17.019  1.000 33.820  ? 70  ASP BBB CA  1 
ATOM 2350  C C   . ASP B 1 53  ? 135.503 18.557  17.074  1.000 32.160  ? 70  ASP BBB C   1 
ATOM 2351  O O   . ASP B 1 53  ? 136.375 18.844  16.243  1.000 32.440  ? 70  ASP BBB O   1 
ATOM 2352  C CB  . ASP B 1 53  ? 136.020 16.127  17.406  1.000 33.390  ? 70  ASP BBB CB  1 
ATOM 2353  C CG  . ASP B 1 53  ? 136.396 16.146  18.878  1.000 33.030  ? 70  ASP BBB CG  1 
ATOM 2354  O OD1 . ASP B 1 53  ? 135.496 16.197  19.743  1.000 35.100  ? 70  ASP BBB OD1 1 
ATOM 2355  O OD2 . ASP B 1 53  ? 137.588 16.082  19.148  1.000 28.900  ? 70  ASP BBB OD2 1 
ATOM 2356  N N   . SER B 1 54  ? 134.979 19.420  17.949  1.000 30.320  ? 71  SER BBB N   1 
ATOM 2357  C CA  . SER B 1 54  ? 135.533 20.787  18.129  1.000 33.210  ? 71  SER BBB CA  1 
ATOM 2358  C C   . SER B 1 54  ? 135.237 21.339  19.518  1.000 31.530  ? 71  SER BBB C   1 
ATOM 2359  O O   . SER B 1 54  ? 134.403 22.218  19.675  1.000 30.930  ? 71  SER BBB O   1 
ATOM 2360  C CB  . SER B 1 54  ? 135.088 21.726  17.032  1.000 38.170  ? 71  SER BBB CB  1 
ATOM 2361  O OG  . SER B 1 54  ? 133.693 21.608  16.807  1.000 42.670  ? 71  SER BBB OG  1 
ATOM 2362  N N   . PRO B 1 55  ? 135.989 20.908  20.540  1.000 32.990  ? 72  PRO BBB N   1 
ATOM 2363  C CA  . PRO B 1 55  ? 135.721 21.288  21.926  1.000 34.000  ? 72  PRO BBB CA  1 
ATOM 2364  C C   . PRO B 1 55  ? 135.884 22.790  22.163  1.000 35.910  ? 72  PRO BBB C   1 
ATOM 2365  O O   . PRO B 1 55  ? 136.880 23.325  21.656  1.000 35.900  ? 72  PRO BBB O   1 
ATOM 2366  C CB  . PRO B 1 55  ? 136.834 20.571  22.704  1.000 34.820  ? 72  PRO BBB CB  1 
ATOM 2367  C CG  . PRO B 1 55  ? 137.947 20.458  21.685  1.000 34.470  ? 72  PRO BBB CG  1 
ATOM 2368  C CD  . PRO B 1 55  ? 137.206 20.096  20.415  1.000 36.080  ? 72  PRO BBB CD  1 
ATOM 2369  N N   . ASN B 1 56  ? 134.953 23.408  22.911  1.000 34.980  ? 73  ASN BBB N   1 
ATOM 2370  C CA  . ASN B 1 56  ? 135.039 24.839  23.311  1.000 38.400  ? 73  ASN BBB CA  1 
ATOM 2371  C C   . ASN B 1 56  ? 136.254 25.010  24.215  1.000 36.970  ? 73  ASN BBB C   1 
ATOM 2372  O O   . ASN B 1 56  ? 136.610 24.050  24.871  1.000 34.250  ? 73  ASN BBB O   1 
ATOM 2373  C CB  . ASN B 1 56  ? 133.793 25.329  24.046  1.000 43.890  ? 73  ASN BBB CB  1 
ATOM 2374  C CG  . ASN B 1 56  ? 132.537 25.359  23.203  1.000 48.990  ? 73  ASN BBB CG  1 
ATOM 2375  O OD1 . ASN B 1 56  ? 131.454 25.606  23.733  1.000 60.170  ? 73  ASN BBB OD1 1 
ATOM 2376  N ND2 . ASN B 1 56  ? 132.660 25.127  21.904  1.000 48.270  ? 73  ASN BBB ND2 1 
ATOM 2377  N N   . ARG B 1 57  ? 136.831 26.202  24.287  1.000 40.780  ? 74  ARG BBB N   1 
ATOM 2378  C CA  . ARG B 1 57  ? 138.087 26.433  25.052  1.000 43.040  ? 74  ARG BBB CA  1 
ATOM 2379  C C   . ARG B 1 57  ? 137.871 26.186  26.556  1.000 38.940  ? 74  ARG BBB C   1 
ATOM 2380  O O   . ARG B 1 57  ? 138.859 25.803  27.248  1.000 37.440  ? 74  ARG BBB O   1 
ATOM 2381  C CB  . ARG B 1 57  ? 138.588 27.858  24.822  1.000 46.930  ? 74  ARG BBB CB  1 
ATOM 2382  C CG  . ARG B 1 57  ? 139.893 28.196  25.523  1.000 46.840  ? 74  ARG BBB CG  1 
ATOM 2383  C CD  . ARG B 1 57  ? 140.253 29.649  25.309  1.000 46.620  ? 74  ARG BBB CD  1 
ATOM 2384  N NE  . ARG B 1 57  ? 141.544 29.934  25.904  1.000 46.620  ? 74  ARG BBB NE  1 
ATOM 2385  C CZ  . ARG B 1 57  ? 141.975 31.137  26.218  1.000 42.490  ? 74  ARG BBB CZ  1 
ATOM 2386  N NH1 . ARG B 1 57  ? 141.239 32.196  25.952  1.000 42.140  ? 74  ARG BBB NH1 1 
ATOM 2387  N NH2 . ARG B 1 57  ? 143.146 31.281  26.804  1.000 49.700  ? 74  ARG BBB NH2 1 
ATOM 2388  N N   . ASP B 1 58  ? 136.653 26.390  27.047  1.000 36.250  ? 75  ASP BBB N   1 
ATOM 2389  C CA  . ASP B 1 58  ? 136.319 26.254  28.493  1.000 41.540  ? 75  ASP BBB CA  1 
ATOM 2390  C C   . ASP B 1 58  ? 135.994 24.787  28.841  1.000 42.410  ? 75  ASP BBB C   1 
ATOM 2391  O O   . ASP B 1 58  ? 135.665 24.517  30.013  1.000 49.160  ? 75  ASP BBB O   1 
ATOM 2392  C CB  . ASP B 1 58  ? 135.165 27.191  28.907  1.000 45.220  ? 75  ASP BBB CB  1 
ATOM 2393  C CG  . ASP B 1 58  ? 133.984 27.210  27.948  1.000 46.390  ? 75  ASP BBB CG  1 
ATOM 2394  O OD1 . ASP B 1 58  ? 133.888 26.310  27.104  1.000 49.940  ? 75  ASP BBB OD1 1 
ATOM 2395  O OD2 . ASP B 1 58  ? 133.162 28.161  28.028  1.000 49.530  ? 75  ASP BBB OD2 1 
ATOM 2396  N N   . MET B 1 59  ? 136.151 23.867  27.891  1.000 37.240  ? 76  MET BBB N   1 
ATOM 2397  C CA  . MET B 1 59  ? 136.007 22.414  28.136  1.000 34.640  ? 76  MET BBB CA  1 
ATOM 2398  C C   . MET B 1 59  ? 137.377 21.717  28.118  1.000 34.040  ? 76  MET BBB C   1 
ATOM 2399  O O   . MET B 1 59  ? 137.415 20.462  28.257  1.000 36.950  ? 76  MET BBB O   1 
ATOM 2400  C CB  . MET B 1 59  ? 135.126 21.807  27.046  1.000 34.950  ? 76  MET BBB CB  1 
ATOM 2401  C CG  . MET B 1 59  ? 134.464 20.551  27.461  1.000 35.070  ? 76  MET BBB CG  1 
ATOM 2402  S SD  . MET B 1 59  ? 133.396 20.006  26.144  1.000 37.440  ? 76  MET BBB SD  1 
ATOM 2403  C CE  . MET B 1 59  ? 134.554 19.136  25.090  1.000 40.260  ? 76  MET BBB CE  1 
ATOM 2404  N N   . LEU B 1 60  ? 138.458 22.478  27.938  1.000 31.030  ? 77  LEU BBB N   1 
ATOM 2405  C CA  . LEU B 1 60  ? 139.822 21.938  27.705  1.000 28.980  ? 77  LEU BBB CA  1 
ATOM 2406  C C   . LEU B 1 60  ? 140.745 22.376  28.823  1.000 29.490  ? 77  LEU BBB C   1 
ATOM 2407  O O   . LEU B 1 60  ? 141.235 23.499  28.832  1.000 34.480  ? 77  LEU BBB O   1 
ATOM 2408  C CB  . LEU B 1 60  ? 140.355 22.430  26.362  1.000 28.860  ? 77  LEU BBB CB  1 
ATOM 2409  C CG  . LEU B 1 60  ? 139.698 21.848  25.119  1.000 29.980  ? 77  LEU BBB CG  1 
ATOM 2410  C CD1 . LEU B 1 60  ? 140.320 22.441  23.855  1.000 31.080  ? 77  LEU BBB CD1 1 
ATOM 2411  C CD2 . LEU B 1 60  ? 139.810 20.343  25.105  1.000 30.340  ? 77  LEU BBB CD2 1 
ATOM 2412  N N   . PRO B 1 61  ? 141.042 21.495  29.785  1.000 29.770  ? 78  PRO BBB N   1 
ATOM 2413  C CA  . PRO B 1 61  ? 142.185 21.687  30.667  1.000 31.180  ? 78  PRO BBB CA  1 
ATOM 2414  C C   . PRO B 1 61  ? 143.462 21.976  29.883  1.000 31.120  ? 78  PRO BBB C   1 
ATOM 2415  O O   . PRO B 1 61  ? 143.588 21.435  28.787  1.000 34.080  ? 78  PRO BBB O   1 
ATOM 2416  C CB  . PRO B 1 61  ? 142.318 20.346  31.407  1.000 34.580  ? 78  PRO BBB CB  1 
ATOM 2417  C CG  . PRO B 1 61  ? 140.928 19.727  31.353  1.000 35.190  ? 78  PRO BBB CG  1 
ATOM 2418  C CD  . PRO B 1 61  ? 140.259 20.300  30.113  1.000 34.150  ? 78  PRO BBB CD  1 
ATOM 2419  N N   . CYS B 1 62  ? 144.365 22.761  30.480  1.000 29.150  ? 79  CYS BBB N   1 
ATOM 2420  C CA  . CYS B 1 62  ? 145.664 23.175  29.890  1.000 28.750  ? 79  CYS BBB CA  1 
ATOM 2421  C C   . CYS B 1 62  ? 146.815 22.999  30.876  1.000 27.020  ? 79  CYS BBB C   1 
ATOM 2422  O O   . CYS B 1 62  ? 146.606 23.179  32.096  1.000 29.140  ? 79  CYS BBB O   1 
ATOM 2423  C CB  . CYS B 1 62  ? 145.647 24.644  29.502  1.000 29.050  ? 79  CYS BBB CB  1 
ATOM 2424  S SG  . CYS B 1 62  ? 144.382 25.034  28.307  1.000 28.020  ? 79  CYS BBB SG  1 
ATOM 2425  N N   . TYR B 1 63  ? 148.003 22.766  30.340  1.000 26.790  ? 80  TYR BBB N   1 
ATOM 2426  C CA  . TYR B 1 63  ? 149.273 22.818  31.099  1.000 30.010  ? 80  TYR BBB CA  1 
ATOM 2427  C C   . TYR B 1 63  ? 149.386 24.199  31.759  1.000 35.100  ? 80  TYR BBB C   1 
ATOM 2428  O O   . TYR B 1 63  ? 149.036 25.260  31.160  1.000 38.500  ? 80  TYR BBB O   1 
ATOM 2429  C CB  . TYR B 1 63  ? 150.485 22.547  30.205  1.000 29.700  ? 80  TYR BBB CB  1 
ATOM 2430  C CG  . TYR B 1 63  ? 150.650 21.124  29.720  1.000 27.550  ? 80  TYR BBB CG  1 
ATOM 2431  C CD1 . TYR B 1 63  ? 149.960 20.647  28.628  1.000 26.250  ? 80  TYR BBB CD1 1 
ATOM 2432  C CD2 . TYR B 1 63  ? 151.528 20.258  30.340  1.000 25.440  ? 80  TYR BBB CD2 1 
ATOM 2433  C CE1 . TYR B 1 63  ? 150.119 19.347  28.177  1.000 24.760  ? 80  TYR BBB CE1 1 
ATOM 2434  C CE2 . TYR B 1 63  ? 151.693 18.954  29.905  1.000 24.620  ? 80  TYR BBB CE2 1 
ATOM 2435  C CZ  . TYR B 1 63  ? 150.983 18.497  28.816  1.000 23.490  ? 80  TYR BBB CZ  1 
ATOM 2436  O OH  . TYR B 1 63  ? 151.156 17.227  28.370  1.000 21.390  ? 80  TYR BBB OH  1 
ATOM 2437  N N   . SER B 1 64  ? 149.824 24.181  33.015  1.000 37.660  ? 81  SER BBB N   1 
ATOM 2438  C CA  . SER B 1 64  ? 150.184 25.370  33.815  1.000 37.610  ? 81  SER BBB CA  1 
ATOM 2439  C C   . SER B 1 64  ? 151.707 25.467  33.763  1.000 36.560  ? 81  SER BBB C   1 
ATOM 2440  O O   . SER B 1 64  ? 152.373 24.404  33.814  1.000 36.670  ? 81  SER BBB O   1 
ATOM 2441  C CB  . SER B 1 64  ? 149.634 25.261  35.237  1.000 41.300  ? 81  SER BBB CB  1 
ATOM 2442  O OG  . SER B 1 64  ? 148.278 24.777  35.230  1.000 45.950  ? 81  SER BBB OG  1 
ATOM 2443  N N   . VAL B 1 65  ? 152.238 26.681  33.627  1.000 36.180  ? 82  VAL BBB N   1 
ATOM 2444  C CA  . VAL B 1 65  ? 153.709 26.964  33.627  1.000 35.220  ? 82  VAL BBB CA  1 
ATOM 2445  C C   . VAL B 1 65  ? 153.976 28.210  34.460  1.000 33.310  ? 82  VAL BBB C   1 
ATOM 2446  O O   . VAL B 1 65  ? 153.120 29.060  34.507  1.000 29.660  ? 82  VAL BBB O   1 
ATOM 2447  C CB  . VAL B 1 65  ? 154.262 27.153  32.208  1.000 33.550  ? 82  VAL BBB CB  1 
ATOM 2448  C CG1 . VAL B 1 65  ? 153.480 28.182  31.434  1.000 33.300  ? 82  VAL BBB CG1 1 
ATOM 2449  C CG2 . VAL B 1 65  ? 155.737 27.495  32.211  1.000 31.480  ? 82  VAL BBB CG2 1 
ATOM 2450  N N   . ALA B 1 66  ? 155.150 28.290  35.062  1.000 35.360  ? 83  ALA BBB N   1 
ATOM 2451  C CA  . ALA B 1 66  ? 155.610 29.442  35.856  1.000 36.760  ? 83  ALA BBB CA  1 
ATOM 2452  C C   . ALA B 1 66  ? 157.101 29.638  35.597  1.000 40.430  ? 83  ALA BBB C   1 
ATOM 2453  O O   . ALA B 1 66  ? 157.866 28.703  35.868  1.000 38.130  ? 83  ALA BBB O   1 
ATOM 2454  C CB  . ALA B 1 66  ? 155.344 29.154  37.299  1.000 36.630  ? 83  ALA BBB CB  1 
ATOM 2455  N N   . ARG B 1 67  ? 157.484 30.805  35.078  1.000 46.100  ? 84  ARG BBB N   1 
ATOM 2456  C CA  . ARG B 1 67  ? 158.905 31.225  34.959  1.000 51.690  ? 84  ARG BBB CA  1 
ATOM 2457  C C   . ARG B 1 67  ? 159.264 31.985  36.242  1.000 48.550  ? 84  ARG BBB C   1 
ATOM 2458  O O   . ARG B 1 67  ? 158.593 32.961  36.535  1.000 49.150  ? 84  ARG BBB O   1 
ATOM 2459  C CB  . ARG B 1 67  ? 159.098 32.046  33.682  1.000 58.770  ? 84  ARG BBB CB  1 
ATOM 2460  C CG  . ARG B 1 67  ? 160.557 32.255  33.308  1.000 65.890  ? 84  ARG BBB CG  1 
ATOM 2461  C CD  . ARG B 1 67  ? 160.796 32.991  31.988  1.000 65.610  ? 84  ARG BBB CD  1 
ATOM 2462  N NE  . ARG B 1 67  ? 159.981 34.180  31.870  1.000 71.560  ? 84  ARG BBB NE  1 
ATOM 2463  C CZ  . ARG B 1 67  ? 160.168 35.315  32.549  1.000 72.530  ? 84  ARG BBB CZ  1 
ATOM 2464  N NH1 . ARG B 1 67  ? 161.194 35.455  33.381  1.000 68.850  ? 84  ARG BBB NH1 1 
ATOM 2465  N NH2 . ARG B 1 67  ? 159.307 36.304  32.388  1.000 73.690  ? 84  ARG BBB NH2 1 
ATOM 2466  N N   . ILE B 1 68  ? 160.244 31.516  37.010  1.000 47.970  ? 85  ILE BBB N   1 
ATOM 2467  C CA  . ILE B 1 68  ? 160.668 32.170  38.286  1.000 47.310  ? 85  ILE BBB CA  1 
ATOM 2468  C C   . ILE B 1 68  ? 162.034 32.812  38.053  1.000 48.600  ? 85  ILE BBB C   1 
ATOM 2469  O O   . ILE B 1 68  ? 163.006 32.111  37.759  1.000 46.180  ? 85  ILE BBB O   1 
ATOM 2470  C CB  . ILE B 1 68  ? 160.729 31.172  39.464  1.000 48.380  ? 85  ILE BBB CB  1 
ATOM 2471  C CG1 . ILE B 1 68  ? 159.543 30.201  39.503  1.000 49.580  ? 85  ILE BBB CG1 1 
ATOM 2472  C CG2 . ILE B 1 68  ? 160.885 31.906  40.778  1.000 45.050  ? 85  ILE BBB CG2 1 
ATOM 2473  C CD1 . ILE B 1 68  ? 158.193 30.854  39.664  1.000 49.670  ? 85  ILE BBB CD1 1 
ATOM 2474  N N   . PRO B 1 69  ? 162.185 34.151  38.209  1.000 48.390  ? 86  PRO BBB N   1 
ATOM 2475  C CA  . PRO B 1 69  ? 163.488 34.789  38.071  1.000 42.260  ? 86  PRO BBB CA  1 
ATOM 2476  C C   . PRO B 1 69  ? 164.298 34.486  39.332  1.000 39.550  ? 86  PRO BBB C   1 
ATOM 2477  O O   . PRO B 1 69  ? 163.748 34.615  40.409  1.000 37.420  ? 86  PRO BBB O   1 
ATOM 2478  C CB  . PRO B 1 69  ? 163.163 36.277  37.937  1.000 43.200  ? 86  PRO BBB CB  1 
ATOM 2479  C CG  . PRO B 1 69  ? 161.657 36.342  37.818  1.000 44.270  ? 86  PRO BBB CG  1 
ATOM 2480  C CD  . PRO B 1 69  ? 161.150 35.129  38.563  1.000 46.920  ? 86  PRO BBB CD  1 
ATOM 2481  N N   . LEU B 1 70  ? 165.550 34.083  39.154  1.000 41.800  ? 87  LEU BBB N   1 
ATOM 2482  C CA  . LEU B 1 70  ? 166.461 33.743  40.260  1.000 50.220  ? 87  LEU BBB CA  1 
ATOM 2483  C C   . LEU B 1 70  ? 167.425 34.902  40.493  1.000 53.040  ? 87  LEU BBB C   1 
ATOM 2484  O O   . LEU B 1 70  ? 167.614 35.750  39.625  1.000 48.620  ? 87  LEU BBB O   1 
ATOM 2485  C CB  . LEU B 1 70  ? 167.220 32.466  39.875  1.000 55.240  ? 87  LEU BBB CB  1 
ATOM 2486  C CG  . LEU B 1 70  ? 166.332 31.277  39.544  1.000 57.170  ? 87  LEU BBB CG  1 
ATOM 2487  C CD1 . LEU B 1 70  ? 167.161 30.111  39.031  1.000 57.850  ? 87  LEU BBB CD1 1 
ATOM 2488  C CD2 . LEU B 1 70  ? 165.518 30.857  40.761  1.000 58.820  ? 87  LEU BBB CD2 1 
ATOM 2489  N N   . PRO B 1 71  ? 168.081 34.964  41.671  1.000 59.230  ? 88  PRO BBB N   1 
ATOM 2490  C CA  . PRO B 1 71  ? 169.128 35.946  41.929  1.000 57.530  ? 88  PRO BBB CA  1 
ATOM 2491  C C   . PRO B 1 71  ? 170.163 36.072  40.805  1.000 56.300  ? 88  PRO BBB C   1 
ATOM 2492  O O   . PRO B 1 71  ? 170.641 35.051  40.331  1.000 51.560  ? 88  PRO BBB O   1 
ATOM 2493  C CB  . PRO B 1 71  ? 169.824 35.355  43.158  1.000 61.970  ? 88  PRO BBB CB  1 
ATOM 2494  C CG  . PRO B 1 71  ? 168.708 34.679  43.915  1.000 63.100  ? 88  PRO BBB CG  1 
ATOM 2495  C CD  . PRO B 1 71  ? 167.826 34.100  42.834  1.000 64.390  ? 88  PRO BBB CD  1 
ATOM 2496  N N   . ASN B 1 72  ? 170.455 37.313  40.405  1.000 54.730  ? 89  ASN BBB N   1 
ATOM 2497  C CA  . ASN B 1 72  ? 171.245 37.608  39.173  1.000 57.570  ? 89  ASN BBB CA  1 
ATOM 2498  C C   . ASN B 1 72  ? 172.701 37.164  39.342  1.000 62.330  ? 89  ASN BBB C   1 
ATOM 2499  O O   . ASN B 1 72  ? 173.198 37.299  40.441  1.000 59.300  ? 89  ASN BBB O   1 
ATOM 2500  C CB  . ASN B 1 72  ? 171.175 39.087  38.838  1.000 56.260  ? 89  ASN BBB CB  1 
ATOM 2501  C CG  . ASN B 1 72  ? 171.443 39.304  37.374  1.000 59.980  ? 89  ASN BBB CG  1 
ATOM 2502  O OD1 . ASN B 1 72  ? 172.373 38.730  36.809  1.000 59.840  ? 89  ASN BBB OD1 1 
ATOM 2503  N ND2 . ASN B 1 72  ? 170.574 40.085  36.743  1.000 63.200  ? 89  ASN BBB ND2 1 
ATOM 2504  N N   . LEU B 1 73  ? 173.346 36.684  38.274  1.000 74.490  ? 90  LEU BBB N   1 
ATOM 2505  C CA  . LEU B 1 73  ? 174.750 36.191  38.266  1.000 84.060  ? 90  LEU BBB CA  1 
ATOM 2506  C C   . LEU B 1 73  ? 175.444 36.640  36.969  1.000 97.360  ? 90  LEU BBB C   1 
ATOM 2507  O O   . LEU B 1 73  ? 174.841 36.449  35.877  1.000 105.550 ? 90  LEU BBB O   1 
ATOM 2508  C CB  . LEU B 1 73  ? 174.778 34.660  38.317  1.000 80.200  ? 90  LEU BBB CB  1 
ATOM 2509  C CG  . LEU B 1 73  ? 173.868 33.965  39.315  1.000 78.130  ? 90  LEU BBB CG  1 
ATOM 2510  C CD1 . LEU B 1 73  ? 173.884 32.460  39.065  1.000 81.160  ? 90  LEU BBB CD1 1 
ATOM 2511  C CD2 . LEU B 1 73  ? 174.286 34.227  40.736  1.000 78.040  ? 90  LEU BBB CD2 1 
ATOM 2512  N N   . ASN B 1 74  ? 176.682 37.136  37.072  1.000 88.920  ? 91  ASN BBB N   1 
ATOM 2513  C CA  . ASN B 1 74  ? 177.663 37.142  35.961  1.000 81.480  ? 91  ASN BBB CA  1 
ATOM 2514  C C   . ASN B 1 74  ? 177.314 38.259  34.955  1.000 73.010  ? 91  ASN BBB C   1 
ATOM 2515  O O   . ASN B 1 74  ? 177.430 39.447  35.344  1.000 56.730  ? 91  ASN BBB O   1 
ATOM 2516  C CB  . ASN B 1 74  ? 177.706 35.745  35.346  1.000 68.110  ? 91  ASN BBB CB  1 
ATOM 2517  N N   . ILE B 1 82  ? 181.905 31.635  34.194  1.000 63.670  ? 99  ILE BBB N   1 
ATOM 2518  C CA  . ILE B 1 82  ? 180.458 32.004  34.031  1.000 66.930  ? 99  ILE BBB CA  1 
ATOM 2519  C C   . ILE B 1 82  ? 179.599 31.063  34.902  1.000 70.890  ? 99  ILE BBB C   1 
ATOM 2520  O O   . ILE B 1 82  ? 179.853 29.853  34.821  1.000 74.350  ? 99  ILE BBB O   1 
ATOM 2521  C CB  . ILE B 1 82  ? 180.075 31.950  32.532  1.000 66.600  ? 99  ILE BBB CB  1 
ATOM 2522  C CG1 . ILE B 1 82  ? 181.137 32.581  31.599  1.000 66.540  ? 99  ILE BBB CG1 1 
ATOM 2523  C CG2 . ILE B 1 82  ? 178.686 32.555  32.342  1.000 59.590  ? 99  ILE BBB CG2 1 
ATOM 2524  C CD1 . ILE B 1 82  ? 182.224 31.637  31.024  1.000 58.420  ? 99  ILE BBB CD1 1 
ATOM 2525  N N   . LEU B 1 83  ? 178.706 31.580  35.772  1.000 68.840  ? 100 LEU BBB N   1 
ATOM 2526  C CA  . LEU B 1 83  ? 177.921 30.775  36.756  1.000 61.410  ? 100 LEU BBB CA  1 
ATOM 2527  C C   . LEU B 1 83  ? 176.456 30.654  36.327  1.000 57.800  ? 100 LEU BBB C   1 
ATOM 2528  O O   . LEU B 1 83  ? 175.919 31.661  35.852  1.000 50.550  ? 100 LEU BBB O   1 
ATOM 2529  C CB  . LEU B 1 83  ? 177.972 31.455  38.125  1.000 57.290  ? 100 LEU BBB CB  1 
ATOM 2530  C CG  . LEU B 1 83  ? 179.326 31.462  38.817  1.000 55.140  ? 100 LEU BBB CG  1 
ATOM 2531  C CD1 . LEU B 1 83  ? 179.149 31.806  40.284  1.000 53.610  ? 100 LEU BBB CD1 1 
ATOM 2532  C CD2 . LEU B 1 83  ? 180.040 30.128  38.675  1.000 57.580  ? 100 LEU BBB CD2 1 
ATOM 2533  N N   . MET B 1 84  ? 175.861 29.467  36.498  1.000 55.740  ? 101 MET BBB N   1 
ATOM 2534  C CA  . MET B 1 84  ? 174.410 29.201  36.289  1.000 56.160  ? 101 MET BBB CA  1 
ATOM 2535  C C   . MET B 1 84  ? 173.822 28.501  37.520  1.000 53.870  ? 101 MET BBB C   1 
ATOM 2536  O O   . MET B 1 84  ? 174.559 27.724  38.177  1.000 52.030  ? 101 MET BBB O   1 
ATOM 2537  C CB  . MET B 1 84  ? 174.171 28.303  35.070  1.000 55.150  ? 101 MET BBB CB  1 
ATOM 2538  C CG  . MET B 1 84  ? 174.705 28.869  33.792  1.000 52.990  ? 101 MET BBB CG  1 
ATOM 2539  S SD  . MET B 1 84  ? 174.244 27.822  32.413  1.000 52.470  ? 101 MET BBB SD  1 
ATOM 2540  C CE  . MET B 1 84  ? 172.543 28.324  32.140  1.000 50.350  ? 101 MET BBB CE  1 
ATOM 2541  N N   . TRP B 1 85  ? 172.538 28.743  37.796  1.000 49.670  ? 102 TRP BBB N   1 
ATOM 2542  C CA  . TRP B 1 85  ? 171.795 28.034  38.867  1.000 47.030  ? 102 TRP BBB CA  1 
ATOM 2543  C C   . TRP B 1 85  ? 171.456 26.595  38.441  1.000 45.890  ? 102 TRP BBB C   1 
ATOM 2544  O O   . TRP B 1 85  ? 170.836 26.398  37.374  1.000 43.750  ? 102 TRP BBB O   1 
ATOM 2545  C CB  . TRP B 1 85  ? 170.537 28.809  39.246  1.000 46.050  ? 102 TRP BBB CB  1 
ATOM 2546  C CG  . TRP B 1 85  ? 170.765 30.046  40.053  1.000 43.030  ? 102 TRP BBB CG  1 
ATOM 2547  C CD1 . TRP B 1 85  ? 170.441 31.322  39.707  1.000 42.110  ? 102 TRP BBB CD1 1 
ATOM 2548  C CD2 . TRP B 1 85  ? 171.315 30.120  41.373  1.000 40.690  ? 102 TRP BBB CD2 1 
ATOM 2549  N NE1 . TRP B 1 85  ? 170.724 32.186  40.727  1.000 41.220  ? 102 TRP BBB NE1 1 
ATOM 2550  C CE2 . TRP B 1 85  ? 171.297 31.478  41.746  1.000 41.460  ? 102 TRP BBB CE2 1 
ATOM 2551  C CE3 . TRP B 1 85  ? 171.810 29.174  42.274  1.000 40.180  ? 102 TRP BBB CE3 1 
ATOM 2552  C CZ2 . TRP B 1 85  ? 171.770 31.916  42.977  1.000 43.360  ? 102 TRP BBB CZ2 1 
ATOM 2553  C CZ3 . TRP B 1 85  ? 172.262 29.608  43.501  1.000 43.510  ? 102 TRP BBB CZ3 1 
ATOM 2554  C CH2 . TRP B 1 85  ? 172.250 30.960  43.844  1.000 43.420  ? 102 TRP BBB CH2 1 
ATOM 2555  N N   . GLU B 1 86  ? 171.862 25.626  39.260  1.000 46.370  ? 103 GLU BBB N   1 
ATOM 2556  C CA  . GLU B 1 86  ? 171.616 24.170  39.099  1.000 44.390  ? 103 GLU BBB CA  1 
ATOM 2557  C C   . GLU B 1 86  ? 170.483 23.764  40.053  1.000 46.060  ? 103 GLU BBB C   1 
ATOM 2558  O O   . GLU B 1 86  ? 170.660 23.881  41.277  1.000 46.300  ? 103 GLU BBB O   1 
ATOM 2559  C CB  . GLU B 1 86  ? 172.892 23.387  39.410  1.000 40.760  ? 103 GLU BBB CB  1 
ATOM 2560  C CG  . GLU B 1 86  ? 172.873 21.941  38.914  1.000 42.160  ? 103 GLU BBB CG  1 
ATOM 2561  C CD  . GLU B 1 86  ? 174.026 21.075  39.413  1.000 42.250  ? 103 GLU BBB CD  1 
ATOM 2562  O OE1 . GLU B 1 86  ? 174.698 21.489  40.339  1.000 46.840  ? 103 GLU BBB OE1 1 
ATOM 2563  O OE2 . GLU B 1 86  ? 174.244 19.987  38.865  1.000 42.640  ? 103 GLU BBB OE2 1 
ATOM 2564  N N   . ALA B 1 87  ? 169.341 23.321  39.512  1.000 44.990  ? 104 ALA BBB N   1 
ATOM 2565  C CA  . ALA B 1 87  ? 168.217 22.755  40.288  1.000 37.800  ? 104 ALA BBB CA  1 
ATOM 2566  C C   . ALA B 1 87  ? 168.612 21.350  40.758  1.000 38.380  ? 104 ALA BBB C   1 
ATOM 2567  O O   . ALA B 1 87  ? 168.922 20.492  39.903  1.000 39.510  ? 104 ALA BBB O   1 
ATOM 2568  C CB  . ALA B 1 87  ? 166.972 22.739  39.446  1.000 33.360  ? 104 ALA BBB CB  1 
ATOM 2569  N N   . VAL B 1 88  ? 168.622 21.124  42.068  1.000 37.120  ? 105 VAL BBB N   1 
ATOM 2570  C CA  . VAL B 1 88  ? 169.214 19.902  42.676  1.000 40.510  ? 105 VAL BBB CA  1 
ATOM 2571  C C   . VAL B 1 88  ? 168.127 18.972  43.221  1.000 39.360  ? 105 VAL BBB C   1 
ATOM 2572  O O   . VAL B 1 88  ? 168.197 17.746  42.957  1.000 41.870  ? 105 VAL BBB O   1 
ATOM 2573  C CB  . VAL B 1 88  ? 170.233 20.297  43.753  1.000 43.260  ? 105 VAL BBB CB  1 
ATOM 2574  C CG1 . VAL B 1 88  ? 170.828 19.077  44.452  1.000 42.340  ? 105 VAL BBB CG1 1 
ATOM 2575  C CG2 . VAL B 1 88  ? 171.326 21.168  43.138  1.000 47.060  ? 105 VAL BBB CG2 1 
ATOM 2576  N N   . THR B 1 89  ? 167.170 19.505  43.973  1.000 38.310  ? 106 THR BBB N   1 
ATOM 2577  C CA  . THR B 1 89  ? 166.076 18.700  44.580  1.000 37.930  ? 106 THR BBB CA  1 
ATOM 2578  C C   . THR B 1 89  ? 164.730 19.386  44.363  1.000 33.840  ? 106 THR BBB C   1 
ATOM 2579  O O   . THR B 1 89  ? 164.684 20.616  44.245  1.000 29.400  ? 106 THR BBB O   1 
ATOM 2580  C CB  . THR B 1 89  ? 166.293 18.478  46.080  1.000 40.860  ? 106 THR BBB CB  1 
ATOM 2581  O OG1 . THR B 1 89  ? 165.756 19.599  46.791  1.000 47.910  ? 106 THR BBB OG1 1 
ATOM 2582  C CG2 . THR B 1 89  ? 167.749 18.267  46.436  1.000 41.010  ? 106 THR BBB CG2 1 
ATOM 2583  N N   . LEU B 1 90  ? 163.675 18.588  44.335  1.000 35.570  ? 107 LEU BBB N   1 
ATOM 2584  C CA  . LEU B 1 90  ? 162.273 19.057  44.239  1.000 38.020  ? 107 LEU BBB CA  1 
ATOM 2585  C C   . LEU B 1 90  ? 161.491 18.397  45.366  1.000 38.080  ? 107 LEU BBB C   1 
ATOM 2586  O O   . LEU B 1 90  ? 161.758 17.227  45.656  1.000 38.570  ? 107 LEU BBB O   1 
ATOM 2587  C CB  . LEU B 1 90  ? 161.686 18.666  42.883  1.000 39.120  ? 107 LEU BBB CB  1 
ATOM 2588  C CG  . LEU B 1 90  ? 160.170 18.791  42.795  1.000 39.380  ? 107 LEU BBB CG  1 
ATOM 2589  C CD1 . LEU B 1 90  ? 159.773 20.245  42.836  1.000 40.290  ? 107 LEU BBB CD1 1 
ATOM 2590  C CD2 . LEU B 1 90  ? 159.623 18.103  41.560  1.000 40.880  ? 107 LEU BBB CD2 1 
ATOM 2591  N N   . LYS B 1 91  ? 160.597 19.150  45.992  1.000 38.240  ? 108 LYS BBB N   1 
ATOM 2592  C CA  . LYS B 1 91  ? 159.473 18.623  46.796  1.000 37.500  ? 108 LYS BBB CA  1 
ATOM 2593  C C   . LYS B 1 91  ? 158.219 19.169  46.138  1.000 36.770  ? 108 LYS BBB C   1 
ATOM 2594  O O   . LYS B 1 91  ? 158.192 20.365  45.837  1.000 40.140  ? 108 LYS BBB O   1 
ATOM 2595  C CB  . LYS B 1 91  ? 159.538 19.109  48.240  1.000 40.560  ? 108 LYS BBB CB  1 
ATOM 2596  C CG  . LYS B 1 91  ? 160.582 18.421  49.102  1.000 45.090  ? 108 LYS BBB CG  1 
ATOM 2597  C CD  . LYS B 1 91  ? 160.806 19.035  50.462  1.000 48.940  ? 108 LYS BBB CD  1 
ATOM 2598  C CE  . LYS B 1 91  ? 160.700 18.031  51.595  1.000 50.600  ? 108 LYS BBB CE  1 
ATOM 2599  N NZ  . LYS B 1 91  ? 161.311 18.589  52.817  1.000 54.890  ? 108 LYS BBB NZ  1 
ATOM 2600  N N   . THR B 1 92  ? 157.230 18.324  45.913  1.000 34.070  ? 109 THR BBB N   1 
ATOM 2601  C CA  . THR B 1 92  ? 155.927 18.760  45.373  1.000 30.510  ? 109 THR BBB CA  1 
ATOM 2602  C C   . THR B 1 92  ? 154.835 17.953  46.051  1.000 28.690  ? 109 THR BBB C   1 
ATOM 2603  O O   . THR B 1 92  ? 155.134 16.837  46.478  1.000 30.580  ? 109 THR BBB O   1 
ATOM 2604  C CB  . THR B 1 92  ? 155.928 18.647  43.848  1.000 29.690  ? 109 THR BBB CB  1 
ATOM 2605  O OG1 . THR B 1 92  ? 154.645 19.070  43.401  1.000 28.930  ? 109 THR BBB OG1 1 
ATOM 2606  C CG2 . THR B 1 92  ? 156.191 17.254  43.331  1.000 29.920  ? 109 THR BBB CG2 1 
ATOM 2607  N N   . GLU B 1 93  ? 153.650 18.527  46.195  1.000 28.940  ? 110 GLU BBB N   1 
ATOM 2608  C CA  . GLU B 1 93  ? 152.434 17.741  46.526  1.000 33.660  ? 110 GLU BBB CA  1 
ATOM 2609  C C   . GLU B 1 93  ? 151.215 18.488  46.012  1.000 29.620  ? 110 GLU BBB C   1 
ATOM 2610  O O   . GLU B 1 93  ? 151.361 19.664  45.688  1.000 31.560  ? 110 GLU BBB O   1 
ATOM 2611  C CB  . GLU B 1 93  ? 152.373 17.392  48.017  1.000 41.930  ? 110 GLU BBB CB  1 
ATOM 2612  C CG  . GLU B 1 93  ? 151.716 18.433  48.908  1.000 47.890  ? 110 GLU BBB CG  1 
ATOM 2613  C CD  . GLU B 1 93  ? 151.851 18.151  50.403  1.000 48.810  ? 110 GLU BBB CD  1 
ATOM 2614  O OE1 . GLU B 1 93  ? 152.889 17.556  50.778  1.000 41.740  ? 110 GLU BBB OE1 1 
ATOM 2615  O OE2 . GLU B 1 93  ? 150.925 18.593  51.189  1.000 54.280  ? 110 GLU BBB OE2 1 
ATOM 2616  N N   . VAL B 1 94  ? 150.088 17.795  45.887  1.000 25.880  ? 111 VAL BBB N   1 
ATOM 2617  C CA  . VAL B 1 94  ? 148.819 18.429  45.462  1.000 26.500  ? 111 VAL BBB CA  1 
ATOM 2618  C C   . VAL B 1 94  ? 148.206 19.137  46.663  1.000 27.070  ? 111 VAL BBB C   1 
ATOM 2619  O O   . VAL B 1 94  ? 148.090 18.514  47.739  1.000 27.970  ? 111 VAL BBB O   1 
ATOM 2620  C CB  . VAL B 1 94  ? 147.869 17.404  44.834  1.000 27.090  ? 111 VAL BBB CB  1 
ATOM 2621  C CG1 . VAL B 1 94  ? 146.478 17.997  44.548  1.000 26.840  ? 111 VAL BBB CG1 1 
ATOM 2622  C CG2 . VAL B 1 94  ? 148.518 16.843  43.572  1.000 27.040  ? 111 VAL BBB CG2 1 
ATOM 2623  N N   . ILE B 1 95  ? 147.813 20.397  46.483  1.000 29.360  ? 112 ILE BBB N   1 
ATOM 2624  C CA  . ILE B 1 95  ? 147.250 21.226  47.584  1.000 32.870  ? 112 ILE BBB CA  1 
ATOM 2625  C C   . ILE B 1 95  ? 145.722 21.176  47.544  1.000 30.730  ? 112 ILE BBB C   1 
ATOM 2626  O O   . ILE B 1 95  ? 145.113 21.639  46.517  1.000 31.190  ? 112 ILE BBB O   1 
ATOM 2627  C CB  . ILE B 1 95  ? 147.767 22.664  47.514  1.000 36.240  ? 112 ILE BBB CB  1 
ATOM 2628  C CG1 . ILE B 1 95  ? 149.293 22.710  47.435  1.000 44.130  ? 112 ILE BBB CG1 1 
ATOM 2629  C CG2 . ILE B 1 95  ? 147.246 23.467  48.692  1.000 36.180  ? 112 ILE BBB CG2 1 
ATOM 2630  C CD1 . ILE B 1 95  ? 149.827 24.086  47.013  1.000 51.920  ? 112 ILE BBB CD1 1 
ATOM 2631  N N   . GLY B 1 96  ? 145.127 20.667  48.623  1.000 28.440  ? 113 GLY BBB N   1 
ATOM 2632  C CA  . GLY B 1 96  ? 143.663 20.730  48.788  1.000 32.260  ? 113 GLY BBB CA  1 
ATOM 2633  C C   . GLY B 1 96  ? 142.990 19.418  48.408  1.000 32.640  ? 113 GLY BBB C   1 
ATOM 2634  O O   . GLY B 1 96  ? 141.875 19.465  47.842  1.000 28.680  ? 113 GLY BBB O   1 
ATOM 2635  N N   . VAL B 1 97  ? 143.636 18.290  48.750  1.000 30.060  ? 114 VAL BBB N   1 
ATOM 2636  C CA  . VAL B 1 97  ? 143.153 16.929  48.394  1.000 27.140  ? 114 VAL BBB CA  1 
ATOM 2637  C C   . VAL B 1 97  ? 141.832 16.695  49.121  1.000 27.650  ? 114 VAL BBB C   1 
ATOM 2638  O O   . VAL B 1 97  ? 140.943 16.097  48.514  1.000 34.750  ? 114 VAL BBB O   1 
ATOM 2639  C CB  . VAL B 1 97  ? 144.189 15.831  48.703  1.000 27.200  ? 114 VAL BBB CB  1 
ATOM 2640  C CG1 . VAL B 1 97  ? 145.504 16.073  47.983  1.000 25.750  ? 114 VAL BBB CG1 1 
ATOM 2641  C CG2 . VAL B 1 97  ? 144.435 15.647  50.197  1.000 29.490  ? 114 VAL BBB CG2 1 
ATOM 2642  N N   . THR B 1 98  ? 141.712 17.143  50.369  1.000 25.980  ? 115 THR BBB N   1 
ATOM 2643  C CA  . THR B 1 98  ? 140.537 16.859  51.237  1.000 27.580  ? 115 THR BBB CA  1 
ATOM 2644  C C   . THR B 1 98  ? 139.266 17.470  50.627  1.000 27.740  ? 115 THR BBB C   1 
ATOM 2645  O O   . THR B 1 98  ? 138.159 17.005  50.970  1.000 26.850  ? 115 THR BBB O   1 
ATOM 2646  C CB  . THR B 1 98  ? 140.707 17.398  52.657  1.000 27.840  ? 115 THR BBB CB  1 
ATOM 2647  O OG1 . THR B 1 98  ? 140.936 18.807  52.532  1.000 33.650  ? 115 THR BBB OG1 1 
ATOM 2648  C CG2 . THR B 1 98  ? 141.820 16.700  53.401  1.000 26.580  ? 115 THR BBB CG2 1 
ATOM 2649  N N   . SER B 1 99  ? 139.406 18.496  49.781  1.000 25.630  ? 116 SER BBB N   1 
ATOM 2650  C CA  . SER B 1 99  ? 138.260 19.193  49.145  1.000 24.370  ? 116 SER BBB CA  1 
ATOM 2651  C C   . SER B 1 99  ? 137.421 18.193  48.359  1.000 23.380  ? 116 SER BBB C   1 
ATOM 2652  O O   . SER B 1 99  ? 136.280 18.518  48.031  1.000 22.970  ? 116 SER BBB O   1 
ATOM 2653  C CB  . SER B 1 99  ? 138.712 20.281  48.250  1.000 25.920  ? 116 SER BBB CB  1 
ATOM 2654  O OG  . SER B 1 99  ? 139.348 19.724  47.105  1.000 28.330  ? 116 SER BBB OG  1 
ATOM 2655  N N   . LEU B 1 100 ? 138.006 17.041  48.029  1.000 23.750  ? 117 LEU BBB N   1 
ATOM 2656  C CA  . LEU B 1 100 ? 137.381 15.993  47.182  1.000 24.280  ? 117 LEU BBB CA  1 
ATOM 2657  C C   . LEU B 1 100 ? 136.427 15.146  48.016  1.000 26.520  ? 117 LEU BBB C   1 
ATOM 2658  O O   . LEU B 1 100 ? 135.663 14.360  47.401  1.000 32.150  ? 117 LEU BBB O   1 
ATOM 2659  C CB  . LEU B 1 100 ? 138.471 15.151  46.515  1.000 22.140  ? 117 LEU BBB CB  1 
ATOM 2660  C CG  . LEU B 1 100 ? 139.278 15.920  45.479  1.000 22.630  ? 117 LEU BBB CG  1 
ATOM 2661  C CD1 . LEU B 1 100 ? 140.224 15.002  44.754  1.000 24.190  ? 117 LEU BBB CD1 1 
ATOM 2662  C CD2 . LEU B 1 100 ? 138.371 16.638  44.487  1.000 23.070  ? 117 LEU BBB CD2 1 
ATOM 2663  N N   . MET B 1 101 ? 136.411 15.353  49.330  1.000 26.610  ? 118 MET BBB N   1 
ATOM 2664  C CA  . MET B 1 101 ? 135.420 14.713  50.231  1.000 28.540  ? 118 MET BBB CA  1 
ATOM 2665  C C   . MET B 1 101 ? 134.087 15.471  50.230  1.000 28.040  ? 118 MET BBB C   1 
ATOM 2666  O O   . MET B 1 101 ? 133.171 14.977  50.887  1.000 26.520  ? 118 MET BBB O   1 
ATOM 2667  C CB  . MET B 1 101 ? 135.941 14.657  51.667  1.000 30.040  ? 118 MET BBB CB  1 
ATOM 2668  C CG  . MET B 1 101 ? 137.281 13.999  51.756  1.000 31.090  ? 118 MET BBB CG  1 
ATOM 2669  S SD  . MET B 1 101 ? 137.617 13.546  53.431  1.000 35.290  ? 118 MET BBB SD  1 
ATOM 2670  C CE  . MET B 1 101 ? 136.774 11.971  53.418  1.000 41.080  ? 118 MET BBB CE  1 
ATOM 2671  N N   . ASN B 1 102 ? 133.974 16.603  49.521  1.000 27.830  ? 119 ASN BBB N   1 
ATOM 2672  C CA  . ASN B 1 102 ? 132.706 17.375  49.486  1.000 26.770  ? 119 ASN BBB CA  1 
ATOM 2673  C C   . ASN B 1 102 ? 131.714 16.645  48.588  1.000 24.870  ? 119 ASN BBB C   1 
ATOM 2674  O O   . ASN B 1 102 ? 131.631 16.977  47.410  1.000 25.910  ? 119 ASN BBB O   1 
ATOM 2675  C CB  . ASN B 1 102 ? 132.846 18.829  49.033  1.000 27.730  ? 119 ASN BBB CB  1 
ATOM 2676  C CG  . ASN B 1 102 ? 131.522 19.567  49.100  1.000 28.950  ? 119 ASN BBB CG  1 
ATOM 2677  O OD1 . ASN B 1 102 ? 130.459 18.950  49.113  1.000 29.160  ? 119 ASN BBB OD1 1 
ATOM 2678  N ND2 . ASN B 1 102 ? 131.555 20.890  49.151  1.000 33.100  ? 119 ASN BBB ND2 1 
ATOM 2679  N N   . VAL B 1 103 ? 130.922 15.770  49.188  1.000 23.970  ? 120 VAL BBB N   1 
ATOM 2680  C CA  . VAL B 1 103 ? 129.954 14.884  48.489  1.000 26.280  ? 120 VAL BBB CA  1 
ATOM 2681  C C   . VAL B 1 103 ? 128.521 15.397  48.671  1.000 27.070  ? 120 VAL BBB C   1 
ATOM 2682  O O   . VAL B 1 103 ? 127.602 14.638  48.407  1.000 28.750  ? 120 VAL BBB O   1 
ATOM 2683  C CB  . VAL B 1 103 ? 130.147 13.461  49.016  1.000 27.500  ? 120 VAL BBB CB  1 
ATOM 2684  C CG1 . VAL B 1 103 ? 131.576 13.019  48.802  1.000 29.540  ? 120 VAL BBB CG1 1 
ATOM 2685  C CG2 . VAL B 1 103 ? 129.777 13.353  50.480  1.000 29.530  ? 120 VAL BBB CG2 1 
ATOM 2686  N N   . HIS B 1 104 ? 128.332 16.671  49.005  1.000 28.660  ? 121 HIS BBB N   1 
ATOM 2687  C CA  . HIS B 1 104 ? 127.009 17.251  49.381  1.000 30.470  ? 121 HIS BBB CA  1 
ATOM 2688  C C   . HIS B 1 104 ? 126.615 18.485  48.543  1.000 34.050  ? 121 HIS BBB C   1 
ATOM 2689  O O   . HIS B 1 104 ? 125.498 19.010  48.783  1.000 33.020  ? 121 HIS BBB O   1 
ATOM 2690  C CB  . HIS B 1 104 ? 127.006 17.602  50.870  1.000 29.170  ? 121 HIS BBB CB  1 
ATOM 2691  C CG  . HIS B 1 104 ? 128.233 18.312  51.333  1.000 28.090  ? 121 HIS BBB CG  1 
ATOM 2692  N ND1 . HIS B 1 104 ? 128.353 19.686  51.298  1.000 28.580  ? 121 HIS BBB ND1 1 
ATOM 2693  C CD2 . HIS B 1 104 ? 129.371 17.844  51.862  1.000 27.420  ? 121 HIS BBB CD2 1 
ATOM 2694  C CE1 . HIS B 1 104 ? 129.518 20.027  51.782  1.000 28.210  ? 121 HIS BBB CE1 1 
ATOM 2695  N NE2 . HIS B 1 104 ? 130.163 18.918  52.145  1.000 26.520  ? 121 HIS BBB NE2 1 
ATOM 2696  N N   . SER B 1 105 ? 127.453 18.920  47.591  1.000 34.470  ? 122 SER BBB N   1 
ATOM 2697  C CA  . SER B 1 105 ? 127.311 20.207  46.858  1.000 32.680  ? 122 SER BBB CA  1 
ATOM 2698  C C   . SER B 1 105 ? 126.639 19.955  45.509  1.000 30.810  ? 122 SER BBB C   1 
ATOM 2699  O O   . SER B 1 105 ? 127.331 20.018  44.481  1.000 31.310  ? 122 SER BBB O   1 
ATOM 2700  C CB  . SER B 1 105 ? 128.667 20.883  46.695  1.000 33.920  ? 122 SER BBB CB  1 
ATOM 2701  O OG  . SER B 1 105 ? 128.588 22.094  45.963  1.000 31.480  ? 122 SER BBB OG  1 
ATOM 2702  N N   . ASN B 1 106 ? 125.348 19.648  45.530  1.000 30.630  ? 123 ASN BBB N   1 
ATOM 2703  C CA  . ASN B 1 106 ? 124.511 19.421  44.331  1.000 33.680  ? 123 ASN BBB CA  1 
ATOM 2704  C C   . ASN B 1 106 ? 125.144 18.369  43.421  1.000 33.120  ? 123 ASN BBB C   1 
ATOM 2705  O O   . ASN B 1 106 ? 125.144 18.580  42.195  1.000 34.760  ? 123 ASN BBB O   1 
ATOM 2706  C CB  . ASN B 1 106 ? 124.337 20.718  43.554  1.000 39.320  ? 123 ASN BBB CB  1 
ATOM 2707  C CG  . ASN B 1 106 ? 123.035 20.750  42.786  1.000 43.590  ? 123 ASN BBB CG  1 
ATOM 2708  O OD1 . ASN B 1 106 ? 121.964 20.614  43.374  1.000 42.250  ? 123 ASN BBB OD1 1 
ATOM 2709  N ND2 . ASN B 1 106 ? 123.120 20.949  41.479  1.000 55.580  ? 123 ASN BBB ND2 1 
ATOM 2710  N N   . GLY B 1 107 ? 125.700 17.293  43.991  1.000 34.680  ? 124 GLY BBB N   1 
ATOM 2711  C CA  . GLY B 1 107 ? 126.275 16.166  43.225  1.000 33.010  ? 124 GLY BBB CA  1 
ATOM 2712  C C   . GLY B 1 107 ? 125.256 15.188  42.681  1.000 31.010  ? 124 GLY BBB C   1 
ATOM 2713  O O   . GLY B 1 107 ? 124.022 15.490  42.809  1.000 29.190  ? 124 GLY BBB O   1 
ATOM 2714  N N   . GLN B 1 108 ? 125.693 13.987  42.299  1.000 29.400  ? 125 GLN BBB N   1 
ATOM 2715  C CA  . GLN B 1 108 ? 124.730 12.944  41.870  1.000 33.160  ? 125 GLN BBB CA  1 
ATOM 2716  C C   . GLN B 1 108 ? 124.616 11.825  42.906  1.000 32.660  ? 125 GLN BBB C   1 
ATOM 2717  O O   . GLN B 1 108 ? 125.537 11.008  42.957  1.000 36.700  ? 125 GLN BBB O   1 
ATOM 2718  C CB  . GLN B 1 108 ? 125.113 12.338  40.526  1.000 32.020  ? 125 GLN BBB CB  1 
ATOM 2719  C CG  . GLN B 1 108 ? 123.936 11.905  39.685  1.000 31.480  ? 125 GLN BBB CG  1 
ATOM 2720  C CD  . GLN B 1 108 ? 124.365 10.956  38.596  1.000 32.550  ? 125 GLN BBB CD  1 
ATOM 2721  O OE1 . GLN B 1 108 ? 125.367 10.259  38.715  1.000 28.910  ? 125 GLN BBB OE1 1 
ATOM 2722  N NE2 . GLN B 1 108 ? 123.601 10.926  37.518  1.000 32.390  ? 125 GLN BBB NE2 1 
ATOM 2723  N N   . ALA B 1 109 ? 123.541 11.793  43.691  1.000 28.820  ? 126 ALA BBB N   1 
ATOM 2724  C CA  . ALA B 1 109 ? 123.227 10.714  44.642  1.000 29.640  ? 126 ALA BBB CA  1 
ATOM 2725  C C   . ALA B 1 109 ? 123.557 9.427   43.905  1.000 28.170  ? 126 ALA BBB C   1 
ATOM 2726  O O   . ALA B 1 109 ? 122.962 9.218   42.857  1.000 28.860  ? 126 ALA BBB O   1 
ATOM 2727  C CB  . ALA B 1 109 ? 121.811 10.665  45.148  1.000 32.160  ? 126 ALA BBB CB  1 
ATOM 2728  N N   . THR B 1 110 ? 124.457 8.621   44.467  1.000 26.870  ? 127 THR BBB N   1 
ATOM 2729  C CA  . THR B 1 110 ? 124.817 7.280   43.970  1.000 27.960  ? 127 THR BBB CA  1 
ATOM 2730  C C   . THR B 1 110 ? 123.584 6.370   43.980  1.000 30.390  ? 127 THR BBB C   1 
ATOM 2731  O O   . THR B 1 110 ? 123.545 5.440   43.164  1.000 34.490  ? 127 THR BBB O   1 
ATOM 2732  C CB  . THR B 1 110 ? 125.982 6.701   44.770  1.000 28.690  ? 127 THR BBB CB  1 
ATOM 2733  O OG1 . THR B 1 110 ? 125.730 6.834   46.162  1.000 29.430  ? 127 THR BBB OG1 1 
ATOM 2734  C CG2 . THR B 1 110 ? 127.292 7.399   44.468  1.000 31.680  ? 127 THR BBB CG2 1 
ATOM 2735  N N   . HIS B 1 111 ? 122.604 6.623   44.851  1.000 30.870  ? 128 HIS BBB N   1 
ATOM 2736  C CA  . HIS B 1 111 ? 121.374 5.789   44.998  1.000 29.750  ? 128 HIS BBB CA  1 
ATOM 2737  C C   . HIS B 1 111 ? 120.401 6.485   45.955  1.000 31.690  ? 128 HIS BBB C   1 
ATOM 2738  O O   . HIS B 1 111 ? 120.811 7.489   46.556  1.000 39.950  ? 128 HIS BBB O   1 
ATOM 2739  C CB  . HIS B 1 111 ? 121.733 4.412   45.554  1.000 26.860  ? 128 HIS BBB CB  1 
ATOM 2740  C CG  . HIS B 1 111 ? 122.423 4.505   46.867  1.000 23.400  ? 128 HIS BBB CG  1 
ATOM 2741  N ND1 . HIS B 1 111 ? 123.777 4.587   46.958  1.000 24.260  ? 128 HIS BBB ND1 1 
ATOM 2742  C CD2 . HIS B 1 111 ? 121.949 4.563   48.124  1.000 22.670  ? 128 HIS BBB CD2 1 
ATOM 2743  C CE1 . HIS B 1 111 ? 124.109 4.677   48.229  1.000 24.660  ? 128 HIS BBB CE1 1 
ATOM 2744  N NE2 . HIS B 1 111 ? 123.009 4.658   48.960  1.000 22.570  ? 128 HIS BBB NE2 1 
ATOM 2745  N N   . ASP B 1 112 ? 119.183 5.979   46.124  1.000 29.230  ? 129 ASP BBB N   1 
ATOM 2746  C CA  . ASP B 1 112 ? 118.193 6.627   47.013  1.000 30.630  ? 129 ASP BBB CA  1 
ATOM 2747  C C   . ASP B 1 112 ? 118.829 6.894   48.383  1.000 30.960  ? 129 ASP BBB C   1 
ATOM 2748  O O   . ASP B 1 112 ? 119.228 5.909   49.056  1.000 28.750  ? 129 ASP BBB O   1 
ATOM 2749  C CB  . ASP B 1 112 ? 116.931 5.776   47.141  1.000 34.760  ? 129 ASP BBB CB  1 
ATOM 2750  C CG  . ASP B 1 112 ? 116.047 5.848   45.918  1.000 35.270  ? 129 ASP BBB CG  1 
ATOM 2751  O OD1 . ASP B 1 112 ? 116.091 6.904   45.280  1.000 36.260  ? 129 ASP BBB OD1 1 
ATOM 2752  O OD2 . ASP B 1 112 ? 115.367 4.828   45.599  1.000 39.900  ? 129 ASP BBB OD2 1 
ATOM 2753  N N   . ASN B 1 113 ? 118.895 8.184   48.763  1.000 29.570  ? 130 ASN BBB N   1 
ATOM 2754  C CA  . ASN B 1 113 ? 119.408 8.692   50.068  1.000 28.750  ? 130 ASN BBB CA  1 
ATOM 2755  C C   . ASN B 1 113 ? 120.934 8.512   50.115  1.000 28.700  ? 130 ASN BBB C   1 
ATOM 2756  O O   . ASN B 1 113 ? 121.554 8.717   51.168  1.000 29.600  ? 130 ASN BBB O   1 
ATOM 2757  C CB  . ASN B 1 113 ? 118.743 8.022   51.269  1.000 29.030  ? 130 ASN BBB CB  1 
ATOM 2758  C CG  . ASN B 1 113 ? 117.225 8.067   51.257  1.000 29.360  ? 130 ASN BBB CG  1 
ATOM 2759  O OD1 . ASN B 1 113 ? 116.618 9.093   50.937  1.000 26.600  ? 130 ASN BBB OD1 1 
ATOM 2760  N ND2 . ASN B 1 113 ? 116.590 6.952   51.629  1.000 30.110  ? 130 ASN BBB ND2 1 
ATOM 2761  N N   . GLY B 1 114 ? 121.547 8.171   48.990  1.000 27.470  ? 131 GLY BBB N   1 
ATOM 2762  C CA  . GLY B 1 114 ? 123.010 8.142   48.869  1.000 24.750  ? 131 GLY BBB CA  1 
ATOM 2763  C C   . GLY B 1 114 ? 123.586 9.554   48.920  1.000 22.520  ? 131 GLY BBB C   1 
ATOM 2764  O O   . GLY B 1 114 ? 122.902 10.541  48.573  1.000 18.430  ? 131 GLY BBB O   1 
ATOM 2765  N N   . ALA B 1 115 ? 124.823 9.640   49.377  1.000 22.940  ? 132 ALA BBB N   1 
ATOM 2766  C CA  . ALA B 1 115 ? 125.664 10.841  49.276  1.000 23.610  ? 132 ALA BBB CA  1 
ATOM 2767  C C   . ALA B 1 115 ? 125.898 11.088  47.797  1.000 24.700  ? 132 ALA BBB C   1 
ATOM 2768  O O   . ALA B 1 115 ? 125.533 10.240  47.000  1.000 25.740  ? 132 ALA BBB O   1 
ATOM 2769  C CB  . ALA B 1 115 ? 126.957 10.611  50.025  1.000 24.040  ? 132 ALA BBB CB  1 
ATOM 2770  N N   . GLY B 1 116 ? 126.512 12.201  47.444  1.000 25.860  ? 133 GLY BBB N   1 
ATOM 2771  C CA  . GLY B 1 116 ? 126.834 12.470  46.035  1.000 26.770  ? 133 GLY BBB CA  1 
ATOM 2772  C C   . GLY B 1 116 ? 127.965 11.591  45.582  1.000 28.270  ? 133 GLY BBB C   1 
ATOM 2773  O O   . GLY B 1 116 ? 128.843 11.281  46.426  1.000 26.910  ? 133 GLY BBB O   1 
ATOM 2774  N N   . LYS B 1 117 ? 127.973 11.201  44.307  1.000 32.140  ? 134 LYS BBB N   1 
ATOM 2775  C CA  . LYS B 1 117 ? 129.133 10.484  43.725  1.000 36.410  ? 134 LYS BBB CA  1 
ATOM 2776  C C   . LYS B 1 117 ? 130.319 11.431  43.815  1.000 33.600  ? 134 LYS BBB C   1 
ATOM 2777  O O   . LYS B 1 117 ? 130.229 12.541  43.310  1.000 40.230  ? 134 LYS BBB O   1 
ATOM 2778  C CB  . LYS B 1 117 ? 128.902 10.085  42.261  1.000 43.580  ? 134 LYS BBB CB  1 
ATOM 2779  C CG  . LYS B 1 117 ? 130.162 9.550   41.579  1.000 50.340  ? 134 LYS BBB CG  1 
ATOM 2780  C CD  . LYS B 1 117 ? 130.189 9.630   40.089  1.000 53.800  ? 134 LYS BBB CD  1 
ATOM 2781  C CE  . LYS B 1 117 ? 129.410 8.546   39.405  1.000 57.970  ? 134 LYS BBB CE  1 
ATOM 2782  N NZ  . LYS B 1 117 ? 129.196 8.943   37.990  1.000 60.340  ? 134 LYS BBB NZ  1 
ATOM 2783  N N   . PRO B 1 118 ? 131.448 11.039  44.434  1.000 27.440  ? 135 PRO BBB N   1 
ATOM 2784  C CA  . PRO B 1 118 ? 132.565 11.946  44.634  1.000 26.660  ? 135 PRO BBB CA  1 
ATOM 2785  C C   . PRO B 1 118 ? 133.311 12.144  43.320  1.000 25.860  ? 135 PRO BBB C   1 
ATOM 2786  O O   . PRO B 1 118 ? 133.166 11.320  42.466  1.000 24.890  ? 135 PRO BBB O   1 
ATOM 2787  C CB  . PRO B 1 118 ? 133.489 11.205  45.603  1.000 27.590  ? 135 PRO BBB CB  1 
ATOM 2788  C CG  . PRO B 1 118 ? 133.205 9.759   45.308  1.000 28.650  ? 135 PRO BBB CG  1 
ATOM 2789  C CD  . PRO B 1 118 ? 131.739 9.694   44.917  1.000 27.950  ? 135 PRO BBB CD  1 
ATOM 2790  N N   . VAL B 1 119 ? 134.120 13.198  43.233  1.000 27.440  ? 136 VAL BBB N   1 
ATOM 2791  C CA  . VAL B 1 119 ? 135.086 13.396  42.120  1.000 26.140  ? 136 VAL BBB CA  1 
ATOM 2792  C C   . VAL B 1 119 ? 135.831 12.078  41.951  1.000 23.160  ? 136 VAL BBB C   1 
ATOM 2793  O O   . VAL B 1 119 ? 136.338 11.555  42.963  1.000 22.410  ? 136 VAL BBB O   1 
ATOM 2794  C CB  . VAL B 1 119 ? 136.081 14.555  42.361  1.000 27.740  ? 136 VAL BBB CB  1 
ATOM 2795  C CG1 . VAL B 1 119 ? 137.197 14.551  41.320  1.000 28.320  ? 136 VAL BBB CG1 1 
ATOM 2796  C CG2 . VAL B 1 119 ? 135.398 15.919  42.383  1.000 28.830  ? 136 VAL BBB CG2 1 
ATOM 2797  N N   . GLN B 1 120 ? 135.863 11.585  40.714  1.000 22.010  ? 137 GLN BBB N   1 
ATOM 2798  C CA  . GLN B 1 120 ? 136.605 10.363  40.307  1.000 23.210  ? 137 GLN BBB CA  1 
ATOM 2799  C C   . GLN B 1 120 ? 136.784 10.349  38.795  1.000 25.350  ? 137 GLN BBB C   1 
ATOM 2800  O O   . GLN B 1 120 ? 136.187 11.183  38.117  1.000 26.970  ? 137 GLN BBB O   1 
ATOM 2801  C CB  . GLN B 1 120 ? 135.845 9.106   40.736  1.000 22.660  ? 137 GLN BBB CB  1 
ATOM 2802  C CG  . GLN B 1 120 ? 134.515 8.904   40.088  1.000 22.740  ? 137 GLN BBB CG  1 
ATOM 2803  C CD  . GLN B 1 120 ? 133.697 7.874   40.863  1.000 22.580  ? 137 GLN BBB CD  1 
ATOM 2804  O OE1 . GLN B 1 120 ? 133.598 6.719   40.443  1.000 23.420  ? 137 GLN BBB OE1 1 
ATOM 2805  N NE2 . GLN B 1 120 ? 133.056 8.305   41.952  1.000 20.490  ? 137 GLN BBB NE2 1 
ATOM 2806  N N   . GLY B 1 121 ? 137.552 9.396   38.290  1.000 27.370  ? 138 GLY BBB N   1 
ATOM 2807  C CA  . GLY B 1 121 ? 137.678 9.162   36.837  1.000 25.100  ? 138 GLY BBB CA  1 
ATOM 2808  C C   . GLY B 1 121 ? 138.998 9.642   36.279  1.000 21.880  ? 138 GLY BBB C   1 
ATOM 2809  O O   . GLY B 1 121 ? 139.895 9.940   37.051  1.000 22.270  ? 138 GLY BBB O   1 
ATOM 2810  N N   . THR B 1 122 ? 139.082 9.707   34.958  1.000 21.990  ? 139 THR BBB N   1 
ATOM 2811  C CA  . THR B 1 122 ? 140.303 9.986   34.156  1.000 21.450  ? 139 THR BBB CA  1 
ATOM 2812  C C   . THR B 1 122 ? 141.092 11.118  34.815  1.000 21.190  ? 139 THR BBB C   1 
ATOM 2813  O O   . THR B 1 122 ? 140.505 12.136  35.118  1.000 19.700  ? 139 THR BBB O   1 
ATOM 2814  C CB  . THR B 1 122 ? 139.933 10.300  32.706  1.000 20.740  ? 139 THR BBB CB  1 
ATOM 2815  O OG1 . THR B 1 122 ? 139.098 9.248   32.212  1.000 21.260  ? 139 THR BBB OG1 1 
ATOM 2816  C CG2 . THR B 1 122 ? 141.159 10.425  31.837  1.000 21.910  ? 139 THR BBB CG2 1 
ATOM 2817  N N   . SER B 1 123 ? 142.379 10.898  35.040  1.000 21.570  ? 140 SER BBB N   1 
ATOM 2818  C CA  . SER B 1 123 ? 143.269 11.770  35.836  1.000 21.630  ? 140 SER BBB CA  1 
ATOM 2819  C C   . SER B 1 123 ? 144.600 11.875  35.112  1.000 22.630  ? 140 SER BBB C   1 
ATOM 2820  O O   . SER B 1 123 ? 145.096 10.828  34.683  1.000 24.290  ? 140 SER BBB O   1 
ATOM 2821  C CB  . SER B 1 123 ? 143.495 11.197  37.211  1.000 22.530  ? 140 SER BBB CB  1 
ATOM 2822  O OG  . SER B 1 123 ? 144.542 10.233  37.205  1.000 22.760  ? 140 SER BBB OG  1 
ATOM 2823  N N   . PHE B 1 124 ? 145.173 13.072  35.025  1.000 23.980  ? 141 PHE BBB N   1 
ATOM 2824  C CA  . PHE B 1 124 ? 146.579 13.301  34.596  1.000 25.490  ? 141 PHE BBB CA  1 
ATOM 2825  C C   . PHE B 1 124 ? 147.282 14.141  35.669  1.000 24.830  ? 141 PHE BBB C   1 
ATOM 2826  O O   . PHE B 1 124 ? 146.905 15.296  35.881  1.000 26.630  ? 141 PHE BBB O   1 
ATOM 2827  C CB  . PHE B 1 124 ? 146.620 13.895  33.176  1.000 26.230  ? 141 PHE BBB CB  1 
ATOM 2828  C CG  . PHE B 1 124 ? 148.000 13.960  32.566  1.000 25.700  ? 141 PHE BBB CG  1 
ATOM 2829  C CD1 . PHE B 1 124 ? 148.820 12.836  32.526  1.000 26.470  ? 141 PHE BBB CD1 1 
ATOM 2830  C CD2 . PHE B 1 124 ? 148.494 15.143  32.052  1.000 24.750  ? 141 PHE BBB CD2 1 
ATOM 2831  C CE1 . PHE B 1 124 ? 150.098 12.896  31.992  1.000 24.640  ? 141 PHE BBB CE1 1 
ATOM 2832  C CE2 . PHE B 1 124 ? 149.784 15.205  31.543  1.000 25.160  ? 141 PHE BBB CE2 1 
ATOM 2833  C CZ  . PHE B 1 124 ? 150.577 14.078  31.493  1.000 24.270  ? 141 PHE BBB CZ  1 
ATOM 2834  N N   . HIS B 1 125 ? 148.212 13.538  36.395  1.000 25.600  ? 142 HIS BBB N   1 
ATOM 2835  C CA  . HIS B 1 125 ? 149.088 14.232  37.374  1.000 28.680  ? 142 HIS BBB CA  1 
ATOM 2836  C C   . HIS B 1 125 ? 150.491 14.239  36.764  1.000 30.070  ? 142 HIS BBB C   1 
ATOM 2837  O O   . HIS B 1 125 ? 151.009 13.144  36.460  1.000 29.560  ? 142 HIS BBB O   1 
ATOM 2838  C CB  . HIS B 1 125 ? 148.997 13.607  38.774  1.000 29.240  ? 142 HIS BBB CB  1 
ATOM 2839  C CG  . HIS B 1 125 ? 147.624 13.718  39.339  1.000 31.920  ? 142 HIS BBB CG  1 
ATOM 2840  N ND1 . HIS B 1 125 ? 147.133 14.895  39.854  1.000 33.350  ? 142 HIS BBB ND1 1 
ATOM 2841  C CD2 . HIS B 1 125 ? 146.608 12.835  39.394  1.000 32.400  ? 142 HIS BBB CD2 1 
ATOM 2842  C CE1 . HIS B 1 125 ? 145.870 14.716  40.243  1.000 33.500  ? 142 HIS BBB CE1 1 
ATOM 2843  N NE2 . HIS B 1 125 ? 145.527 13.458  39.978  1.000 31.380  ? 142 HIS BBB NE2 1 
ATOM 2844  N N   . PHE B 1 126 ? 151.024 15.441  36.534  1.000 29.650  ? 143 PHE BBB N   1 
ATOM 2845  C CA  . PHE B 1 126 ? 152.271 15.725  35.788  1.000 29.380  ? 143 PHE BBB CA  1 
ATOM 2846  C C   . PHE B 1 126 ? 152.944 16.953  36.407  1.000 29.120  ? 143 PHE BBB C   1 
ATOM 2847  O O   . PHE B 1 126 ? 152.236 17.903  36.786  1.000 29.000  ? 143 PHE BBB O   1 
ATOM 2848  C CB  . PHE B 1 126 ? 151.961 15.991  34.308  1.000 32.100  ? 143 PHE BBB CB  1 
ATOM 2849  C CG  . PHE B 1 126 ? 153.120 16.609  33.578  1.000 31.760  ? 143 PHE BBB CG  1 
ATOM 2850  C CD1 . PHE B 1 126 ? 154.173 15.829  33.158  1.000 32.670  ? 143 PHE BBB CD1 1 
ATOM 2851  C CD2 . PHE B 1 126 ? 153.206 17.975  33.402  1.000 33.680  ? 143 PHE BBB CD2 1 
ATOM 2852  C CE1 . PHE B 1 126 ? 155.282 16.394  32.554  1.000 34.850  ? 143 PHE BBB CE1 1 
ATOM 2853  C CE2 . PHE B 1 126 ? 154.313 18.547  32.794  1.000 34.780  ? 143 PHE BBB CE2 1 
ATOM 2854  C CZ  . PHE B 1 126 ? 155.349 17.755  32.376  1.000 36.250  ? 143 PHE BBB CZ  1 
ATOM 2855  N N   . PHE B 1 127 ? 154.271 16.953  36.463  1.000 29.320  ? 144 PHE BBB N   1 
ATOM 2856  C CA  . PHE B 1 127 ? 155.071 18.114  36.925  1.000 28.920  ? 144 PHE BBB CA  1 
ATOM 2857  C C   . PHE B 1 127 ? 156.518 17.985  36.434  1.000 30.940  ? 144 PHE BBB C   1 
ATOM 2858  O O   . PHE B 1 127 ? 157.070 16.853  36.407  1.000 29.950  ? 144 PHE BBB O   1 
ATOM 2859  C CB  . PHE B 1 127 ? 155.028 18.205  38.445  1.000 27.290  ? 144 PHE BBB CB  1 
ATOM 2860  C CG  . PHE B 1 127 ? 155.618 17.004  39.126  1.000 27.850  ? 144 PHE BBB CG  1 
ATOM 2861  C CD1 . PHE B 1 127 ? 156.984 16.924  39.346  1.000 27.440  ? 144 PHE BBB CD1 1 
ATOM 2862  C CD2 . PHE B 1 127 ? 154.816 15.953  39.544  1.000 26.870  ? 144 PHE BBB CD2 1 
ATOM 2863  C CE1 . PHE B 1 127 ? 157.537 15.831  39.994  1.000 25.630  ? 144 PHE BBB CE1 1 
ATOM 2864  C CE2 . PHE B 1 127 ? 155.371 14.860  40.185  1.000 25.870  ? 144 PHE BBB CE2 1 
ATOM 2865  C CZ  . PHE B 1 127 ? 156.721 14.805  40.404  1.000 25.380  ? 144 PHE BBB CZ  1 
ATOM 2866  N N   . SER B 1 128 ? 157.111 19.123  36.071  1.000 30.510  ? 145 SER BBB N   1 
ATOM 2867  C CA  . SER B 1 128 ? 158.461 19.236  35.478  1.000 29.610  ? 145 SER BBB CA  1 
ATOM 2868  C C   . SER B 1 128 ? 159.239 20.349  36.192  1.000 29.720  ? 145 SER BBB C   1 
ATOM 2869  O O   . SER B 1 128 ? 158.598 21.322  36.644  1.000 28.210  ? 145 SER BBB O   1 
ATOM 2870  C CB  . SER B 1 128 ? 158.351 19.493  34.005  1.000 30.450  ? 145 SER BBB CB  1 
ATOM 2871  O OG  . SER B 1 128 ? 158.299 20.900  33.737  1.000 34.550  ? 145 SER BBB OG  1 
ATOM 2872  N N   . VAL B 1 129 ? 160.566 20.201  36.271  1.000 31.260  ? 146 VAL BBB N   1 
ATOM 2873  C CA  . VAL B 1 129 ? 161.513 21.269  36.697  1.000 35.310  ? 146 VAL BBB CA  1 
ATOM 2874  C C   . VAL B 1 129 ? 162.591 21.421  35.623  1.000 35.910  ? 146 VAL BBB C   1 
ATOM 2875  O O   . VAL B 1 129 ? 163.275 20.425  35.320  1.000 33.040  ? 146 VAL BBB O   1 
ATOM 2876  C CB  . VAL B 1 129 ? 162.108 20.961  38.080  1.000 39.680  ? 146 VAL BBB CB  1 
ATOM 2877  C CG1 . VAL B 1 129 ? 163.114 22.018  38.520  1.000 39.920  ? 146 VAL BBB CG1 1 
ATOM 2878  C CG2 . VAL B 1 129 ? 161.008 20.832  39.114  1.000 45.100  ? 146 VAL BBB CG2 1 
ATOM 2879  N N   . GLY B 1 130 ? 162.716 22.628  35.068  1.000 39.250  ? 147 GLY BBB N   1 
ATOM 2880  C CA  . GLY B 1 130 ? 163.568 22.901  33.901  1.000 41.860  ? 147 GLY BBB CA  1 
ATOM 2881  C C   . GLY B 1 130 ? 164.330 24.207  34.025  1.000 41.660  ? 147 GLY BBB C   1 
ATOM 2882  O O   . GLY B 1 130 ? 163.789 25.158  34.656  1.000 33.570  ? 147 GLY BBB O   1 
ATOM 2883  N N   . GLY B 1 131 ? 165.530 24.239  33.417  1.000 43.720  ? 148 GLY BBB N   1 
ATOM 2884  C CA  . GLY B 1 131 ? 166.345 25.446  33.155  1.000 43.700  ? 148 GLY BBB CA  1 
ATOM 2885  C C   . GLY B 1 131 ? 165.836 26.248  31.960  1.000 40.780  ? 148 GLY BBB C   1 
ATOM 2886  O O   . GLY B 1 131 ? 166.408 27.298  31.656  1.000 37.720  ? 148 GLY BBB O   1 
ATOM 2887  N N   . GLU B 1 132 ? 164.777 25.773  31.312  1.000 41.640  ? 149 GLU BBB N   1 
ATOM 2888  C CA  . GLU B 1 132 ? 164.116 26.425  30.154  1.000 40.470  ? 149 GLU BBB CA  1 
ATOM 2889  C C   . GLU B 1 132 ? 162.715 25.841  30.033  1.000 40.490  ? 149 GLU BBB C   1 
ATOM 2890  O O   . GLU B 1 132 ? 162.403 24.893  30.795  1.000 42.450  ? 149 GLU BBB O   1 
ATOM 2891  C CB  . GLU B 1 132 ? 164.897 26.186  28.863  1.000 38.820  ? 149 GLU BBB CB  1 
ATOM 2892  C CG  . GLU B 1 132 ? 165.737 24.925  28.894  1.000 37.650  ? 149 GLU BBB CG  1 
ATOM 2893  C CD  . GLU B 1 132 ? 166.331 24.541  27.548  1.000 36.740  ? 149 GLU BBB CD  1 
ATOM 2894  O OE1 . GLU B 1 132 ? 165.597 24.640  26.523  1.000 31.330  ? 149 GLU BBB OE1 1 
ATOM 2895  O OE2 . GLU B 1 132 ? 167.539 24.198  27.518  1.000 38.260  ? 149 GLU BBB OE2 1 
ATOM 2896  N N   . ALA B 1 133 ? 161.917 26.348  29.100  1.000 39.530  ? 150 ALA BBB N   1 
ATOM 2897  C CA  . ALA B 1 133 ? 160.538 25.865  28.902  1.000 43.500  ? 150 ALA BBB CA  1 
ATOM 2898  C C   . ALA B 1 133 ? 160.544 24.343  28.734  1.000 47.920  ? 150 ALA BBB C   1 
ATOM 2899  O O   . ALA B 1 133 ? 161.469 23.800  28.099  1.000 50.760  ? 150 ALA BBB O   1 
ATOM 2900  C CB  . ALA B 1 133 ? 159.929 26.527  27.708  1.000 44.050  ? 150 ALA BBB CB  1 
ATOM 2901  N N   . LEU B 1 134 ? 159.523 23.673  29.277  1.000 50.310  ? 151 LEU BBB N   1 
ATOM 2902  C CA  . LEU B 1 134 ? 159.175 22.293  28.854  1.000 44.930  ? 151 LEU BBB CA  1 
ATOM 2903  C C   . LEU B 1 134 ? 158.997 22.289  27.335  1.000 41.920  ? 151 LEU BBB C   1 
ATOM 2904  O O   . LEU B 1 134 ? 158.291 23.171  26.814  1.000 41.970  ? 151 LEU BBB O   1 
ATOM 2905  C CB  . LEU B 1 134 ? 157.882 21.871  29.552  1.000 43.600  ? 151 LEU BBB CB  1 
ATOM 2906  C CG  . LEU B 1 134 ? 157.427 20.438  29.317  1.000 39.560  ? 151 LEU BBB CG  1 
ATOM 2907  C CD1 . LEU B 1 134 ? 158.455 19.452  29.845  1.000 39.370  ? 151 LEU BBB CD1 1 
ATOM 2908  C CD2 . LEU B 1 134 ? 156.083 20.222  29.984  1.000 38.140  ? 151 LEU BBB CD2 1 
ATOM 2909  N N   . GLU B 1 135 ? 159.588 21.315  26.659  1.000 41.960  ? 152 GLU BBB N   1 
ATOM 2910  C CA  . GLU B 1 135 ? 159.442 21.119  25.195  1.000 42.440  ? 152 GLU BBB CA  1 
ATOM 2911  C C   . GLU B 1 135 ? 158.343 20.076  24.940  1.000 36.040  ? 152 GLU BBB C   1 
ATOM 2912  O O   . GLU B 1 135 ? 158.406 18.984  25.522  1.000 36.870  ? 152 GLU BBB O   1 
ATOM 2913  C CB  . GLU B 1 135 ? 160.800 20.732  24.613  1.000 49.060  ? 152 GLU BBB CB  1 
ATOM 2914  C CG  . GLU B 1 135 ? 161.835 21.830  24.764  1.000 50.930  ? 152 GLU BBB CG  1 
ATOM 2915  C CD  . GLU B 1 135 ? 163.181 21.502  24.149  1.000 53.070  ? 152 GLU BBB CD  1 
ATOM 2916  O OE1 . GLU B 1 135 ? 164.027 20.909  24.832  1.000 47.920  ? 152 GLU BBB OE1 1 
ATOM 2917  O OE2 . GLU B 1 135 ? 163.356 21.797  22.962  1.000 62.290  ? 152 GLU BBB OE2 1 
ATOM 2918  N N   . LEU B 1 136 ? 157.369 20.423  24.106  1.000 32.490  ? 153 LEU BBB N   1 
ATOM 2919  C CA  . LEU B 1 136 ? 156.159 19.608  23.833  1.000 32.320  ? 153 LEU BBB CA  1 
ATOM 2920  C C   . LEU B 1 136 ? 156.212 18.977  22.431  1.000 31.750  ? 153 LEU BBB C   1 
ATOM 2921  O O   . LEU B 1 136 ? 156.627 19.637  21.468  1.000 30.120  ? 153 LEU BBB O   1 
ATOM 2922  C CB  . LEU B 1 136 ? 154.914 20.489  23.932  1.000 34.160  ? 153 LEU BBB CB  1 
ATOM 2923  C CG  . LEU B 1 136 ? 154.716 21.263  25.226  1.000 35.860  ? 153 LEU BBB CG  1 
ATOM 2924  C CD1 . LEU B 1 136 ? 153.482 22.159  25.142  1.000 36.620  ? 153 LEU BBB CD1 1 
ATOM 2925  C CD2 . LEU B 1 136 ? 154.585 20.303  26.372  1.000 38.580  ? 153 LEU BBB CD2 1 
ATOM 2926  N N   . GLN B 1 137 ? 155.750 17.734  22.344  1.000 31.960  ? 154 GLN BBB N   1 
ATOM 2927  C CA  . GLN B 1 137 ? 155.370 17.027  21.098  1.000 30.950  ? 154 GLN BBB CA  1 
ATOM 2928  C C   . GLN B 1 137 ? 153.841 16.980  21.036  1.000 30.460  ? 154 GLN BBB C   1 
ATOM 2929  O O   . GLN B 1 137 ? 153.202 16.618  22.041  1.000 27.260  ? 154 GLN BBB O   1 
ATOM 2930  C CB  . GLN B 1 137 ? 155.935 15.604  21.097  1.000 30.690  ? 154 GLN BBB CB  1 
ATOM 2931  C CG  . GLN B 1 137 ? 155.408 14.734  19.972  1.000 28.320  ? 154 GLN BBB CG  1 
ATOM 2932  C CD  . GLN B 1 137 ? 155.838 15.297  18.649  1.000 28.780  ? 154 GLN BBB CD  1 
ATOM 2933  O OE1 . GLN B 1 137 ? 156.972 15.723  18.485  1.000 29.210  ? 154 GLN BBB OE1 1 
ATOM 2934  N NE2 . GLN B 1 137 ? 154.932 15.307  17.689  1.000 31.780  ? 154 GLN BBB NE2 1 
ATOM 2935  N N   . GLY B 1 138 ? 153.272 17.345  19.900  1.000 30.920  ? 155 GLY BBB N   1 
ATOM 2936  C CA  . GLY B 1 138 ? 151.833 17.190  19.679  1.000 30.830  ? 155 GLY BBB CA  1 
ATOM 2937  C C   . GLY B 1 138 ? 151.502 15.761  19.298  1.000 29.670  ? 155 GLY BBB C   1 
ATOM 2938  O O   . GLY B 1 138 ? 152.193 15.180  18.418  1.000 28.870  ? 155 GLY BBB O   1 
ATOM 2939  N N   . VAL B 1 139 ? 150.467 15.212  19.932  1.000 27.670  ? 156 VAL BBB N   1 
ATOM 2940  C CA  . VAL B 1 139 ? 149.824 13.953  19.478  1.000 29.730  ? 156 VAL BBB CA  1 
ATOM 2941  C C   . VAL B 1 139 ? 148.328 14.151  19.628  1.000 34.130  ? 156 VAL BBB C   1 
ATOM 2942  O O   . VAL B 1 139 ? 147.901 14.632  20.709  1.000 38.990  ? 156 VAL BBB O   1 
ATOM 2943  C CB  . VAL B 1 139 ? 150.286 12.726  20.274  1.000 29.390  ? 156 VAL BBB CB  1 
ATOM 2944  C CG1 . VAL B 1 139 ? 149.669 11.456  19.711  1.000 28.840  ? 156 VAL BBB CG1 1 
ATOM 2945  C CG2 . VAL B 1 139 ? 151.809 12.604  20.331  1.000 28.630  ? 156 VAL BBB CG2 1 
ATOM 2946  N N   . LEU B 1 140 ? 147.577 13.751  18.602  1.000 35.160  ? 157 LEU BBB N   1 
ATOM 2947  C CA  . LEU B 1 140 ? 146.118 13.999  18.522  1.000 35.180  ? 157 LEU BBB CA  1 
ATOM 2948  C C   . LEU B 1 140 ? 145.377 12.666  18.669  1.000 34.060  ? 157 LEU BBB C   1 
ATOM 2949  O O   . LEU B 1 140 ? 145.799 11.669  18.055  1.000 32.400  ? 157 LEU BBB O   1 
ATOM 2950  C CB  . LEU B 1 140 ? 145.826 14.660  17.175  1.000 34.310  ? 157 LEU BBB CB  1 
ATOM 2951  C CG  . LEU B 1 140 ? 146.451 16.034  16.945  1.000 34.020  ? 157 LEU BBB CG  1 
ATOM 2952  C CD1 . LEU B 1 140 ? 145.992 16.615  15.619  1.000 34.290  ? 157 LEU BBB CD1 1 
ATOM 2953  C CD2 . LEU B 1 140 ? 146.112 16.981  18.088  1.000 35.860  ? 157 LEU BBB CD2 1 
ATOM 2954  N N   . PHE B 1 141 ? 144.306 12.639  19.457  1.000 33.260  ? 158 PHE BBB N   1 
ATOM 2955  C CA  . PHE B 1 141 ? 143.420 11.455  19.505  1.000 31.330  ? 158 PHE BBB CA  1 
ATOM 2956  C C   . PHE B 1 141 ? 142.741 11.353  18.146  1.000 32.520  ? 158 PHE BBB C   1 
ATOM 2957  O O   . PHE B 1 141 ? 142.720 10.260  17.563  1.000 38.750  ? 158 PHE BBB O   1 
ATOM 2958  C CB  . PHE B 1 141 ? 142.414 11.542  20.641  1.000 29.680  ? 158 PHE BBB CB  1 
ATOM 2959  C CG  . PHE B 1 141 ? 141.422 10.417  20.648  1.000 26.930  ? 158 PHE BBB CG  1 
ATOM 2960  C CD1 . PHE B 1 141 ? 141.791 9.139   21.027  1.000 26.870  ? 158 PHE BBB CD1 1 
ATOM 2961  C CD2 . PHE B 1 141 ? 140.130 10.637  20.224  1.000 26.440  ? 158 PHE BBB CD2 1 
ATOM 2962  C CE1 . PHE B 1 141 ? 140.869 8.106   21.018  1.000 25.640  ? 158 PHE BBB CE1 1 
ATOM 2963  C CE2 . PHE B 1 141 ? 139.189 9.618   20.277  1.000 26.600  ? 158 PHE BBB CE2 1 
ATOM 2964  C CZ  . PHE B 1 141 ? 139.568 8.352   20.661  1.000 25.370  ? 158 PHE BBB CZ  1 
ATOM 2965  N N   . ASN B 1 142 ? 142.236 12.477  17.645  1.000 32.060  ? 159 ASN BBB N   1 
ATOM 2966  C CA  . ASN B 1 142 ? 141.552 12.554  16.333  1.000 32.750  ? 159 ASN BBB CA  1 
ATOM 2967  C C   . ASN B 1 142 ? 142.127 13.751  15.592  1.000 34.360  ? 159 ASN BBB C   1 
ATOM 2968  O O   . ASN B 1 142 ? 141.954 14.836  16.132  1.000 39.730  ? 159 ASN BBB O   1 
ATOM 2969  C CB  . ASN B 1 142 ? 140.048 12.702  16.554  1.000 31.440  ? 159 ASN BBB CB  1 
ATOM 2970  C CG  . ASN B 1 142 ? 139.256 12.869  15.280  1.000 30.250  ? 159 ASN BBB CG  1 
ATOM 2971  O OD1 . ASN B 1 142 ? 139.786 12.692  14.191  1.000 32.540  ? 159 ASN BBB OD1 1 
ATOM 2972  N ND2 . ASN B 1 142 ? 137.975 13.151  15.411  1.000 28.230  ? 159 ASN BBB ND2 1 
ATOM 2973  N N   . TYR B 1 143 ? 142.800 13.575  14.451  1.000 34.860  ? 160 TYR BBB N   1 
ATOM 2974  C CA  . TYR B 1 143 ? 143.511 14.691  13.756  1.000 37.050  ? 160 TYR BBB CA  1 
ATOM 2975  C C   . TYR B 1 143 ? 142.548 15.756  13.200  1.000 34.790  ? 160 TYR BBB C   1 
ATOM 2976  O O   . TYR B 1 143 ? 142.986 16.927  13.103  1.000 34.330  ? 160 TYR BBB O   1 
ATOM 2977  C CB  . TYR B 1 143 ? 144.505 14.191  12.694  1.000 40.570  ? 160 TYR BBB CB  1 
ATOM 2978  C CG  . TYR B 1 143 ? 143.927 13.981  11.318  1.000 41.700  ? 160 TYR BBB CG  1 
ATOM 2979  C CD1 . TYR B 1 143 ? 143.133 12.882  11.054  1.000 45.290  ? 160 TYR BBB CD1 1 
ATOM 2980  C CD2 . TYR B 1 143 ? 144.159 14.872  10.288  1.000 41.680  ? 160 TYR BBB CD2 1 
ATOM 2981  C CE1 . TYR B 1 143 ? 142.564 12.681  9.812   1.000 47.240  ? 160 TYR BBB CE1 1 
ATOM 2982  C CE2 . TYR B 1 143 ? 143.594 14.689  9.040   1.000 44.670  ? 160 TYR BBB CE2 1 
ATOM 2983  C CZ  . TYR B 1 143 ? 142.773 13.601  8.811   1.000 43.910  ? 160 TYR BBB CZ  1 
ATOM 2984  O OH  . TYR B 1 143 ? 142.188 13.380  7.607   1.000 41.930  ? 160 TYR BBB OH  1 
ATOM 2985  N N   . ARG B 1 144 ? 141.277 15.411  12.988  1.000 32.860  ? 161 ARG BBB N   1 
ATOM 2986  C CA  . ARG B 1 144 ? 140.264 16.350  12.439  1.000 35.060  ? 161 ARG BBB CA  1 
ATOM 2987  C C   . ARG B 1 144 ? 139.610 17.139  13.582  1.000 35.360  ? 161 ARG BBB C   1 
ATOM 2988  O O   . ARG B 1 144 ? 138.742 17.971  13.304  1.000 35.830  ? 161 ARG BBB O   1 
ATOM 2989  C CB  . ARG B 1 144 ? 139.199 15.566  11.679  1.000 40.720  ? 161 ARG BBB CB  1 
ATOM 2990  C CG  . ARG B 1 144 ? 139.678 14.936  10.380  1.000 55.300  ? 161 ARG BBB CG  1 
ATOM 2991  C CD  . ARG B 1 144 ? 138.493 14.467  9.564   1.000 59.020  ? 161 ARG BBB CD  1 
ATOM 2992  N NE  . ARG B 1 144 ? 137.795 13.435  10.310  1.000 67.890  ? 161 ARG BBB NE  1 
ATOM 2993  C CZ  . ARG B 1 144 ? 138.098 12.145  10.293  1.000 66.340  ? 161 ARG BBB CZ  1 
ATOM 2994  N NH1 . ARG B 1 144 ? 137.391 11.298  11.018  1.000 59.430  ? 161 ARG BBB NH1 1 
ATOM 2995  N NH2 . ARG B 1 144 ? 139.105 11.708  9.560   1.000 66.020  ? 161 ARG BBB NH2 1 
ATOM 2996  N N   . THR B 1 145 ? 139.974 16.841  14.821  1.000 35.890  ? 162 THR BBB N   1 
ATOM 2997  C CA  . THR B 1 145 ? 139.526 17.644  15.999  1.000 33.970  ? 162 THR BBB CA  1 
ATOM 2998  C C   . THR B 1 145 ? 139.965 19.072  15.693  1.000 33.580  ? 162 THR BBB C   1 
ATOM 2999  O O   . THR B 1 145 ? 141.154 19.224  15.445  1.000 36.810  ? 162 THR BBB O   1 
ATOM 3000  C CB  . THR B 1 145 ? 140.173 17.266  17.337  1.000 33.910  ? 162 THR BBB CB  1 
ATOM 3001  O OG1 . THR B 1 145 ? 139.903 15.950  17.819  1.000 32.850  ? 162 THR BBB OG1 1 
ATOM 3002  C CG2 . THR B 1 145 ? 139.739 18.206  18.437  1.000 35.730  ? 162 THR BBB CG2 1 
ATOM 3003  N N   . LYS B 1 146 ? 139.057 20.055  15.733  1.000 32.060  ? 163 LYS BBB N   1 
ATOM 3004  C CA  . LYS B 1 146 ? 139.367 21.498  15.561  1.000 30.760  ? 163 LYS BBB CA  1 
ATOM 3005  C C   . LYS B 1 146 ? 139.569 22.113  16.935  1.000 31.030  ? 163 LYS BBB C   1 
ATOM 3006  O O   . LYS B 1 146 ? 138.537 22.375  17.625  1.000 32.020  ? 163 LYS BBB O   1 
ATOM 3007  C CB  . LYS B 1 146 ? 138.213 22.254  14.899  1.000 35.390  ? 163 LYS BBB CB  1 
ATOM 3008  C CG  . LYS B 1 146 ? 138.405 23.759  14.775  1.000 41.190  ? 163 LYS BBB CG  1 
ATOM 3009  C CD  . LYS B 1 146 ? 137.168 24.522  14.371  1.000 47.150  ? 163 LYS BBB CD  1 
ATOM 3010  C CE  . LYS B 1 146 ? 137.488 25.994  14.165  1.000 57.230  ? 163 LYS BBB CE  1 
ATOM 3011  N NZ  . LYS B 1 146 ? 136.358 26.759  13.578  1.000 60.990  ? 163 LYS BBB NZ  1 
ATOM 3012  N N   . TYR B 1 147 ? 140.805 22.385  17.330  1.000 32.300  ? 164 TYR BBB N   1 
ATOM 3013  C CA  . TYR B 1 147 ? 141.082 22.962  18.679  1.000 32.920  ? 164 TYR BBB CA  1 
ATOM 3014  C C   . TYR B 1 147 ? 140.660 24.431  18.651  1.000 32.530  ? 164 TYR BBB C   1 
ATOM 3015  O O   . TYR B 1 147 ? 140.856 25.110  17.658  1.000 29.160  ? 164 TYR BBB O   1 
ATOM 3016  C CB  . TYR B 1 147 ? 142.494 22.614  19.159  1.000 30.630  ? 164 TYR BBB CB  1 
ATOM 3017  C CG  . TYR B 1 147 ? 142.589 21.182  19.617  1.000 30.140  ? 164 TYR BBB CG  1 
ATOM 3018  C CD1 . TYR B 1 147 ? 142.857 20.172  18.720  1.000 30.810  ? 164 TYR BBB CD1 1 
ATOM 3019  C CD2 . TYR B 1 147 ? 142.343 20.809  20.923  1.000 31.370  ? 164 TYR BBB CD2 1 
ATOM 3020  C CE1 . TYR B 1 147 ? 142.921 18.847  19.112  1.000 30.490  ? 164 TYR BBB CE1 1 
ATOM 3021  C CE2 . TYR B 1 147 ? 142.415 19.483  21.337  1.000 31.670  ? 164 TYR BBB CE2 1 
ATOM 3022  C CZ  . TYR B 1 147 ? 142.690 18.488  20.424  1.000 30.460  ? 164 TYR BBB CZ  1 
ATOM 3023  O OH  . TYR B 1 147 ? 142.746 17.166  20.777  1.000 33.470  ? 164 TYR BBB OH  1 
ATOM 3024  N N   . PRO B 1 148 ? 140.043 24.949  19.735  1.000 35.170  ? 165 PRO BBB N   1 
ATOM 3025  C CA  . PRO B 1 148 ? 139.314 26.201  19.689  1.000 34.970  ? 165 PRO BBB CA  1 
ATOM 3026  C C   . PRO B 1 148 ? 140.269 27.402  19.710  1.000 38.170  ? 165 PRO BBB C   1 
ATOM 3027  O O   . PRO B 1 148 ? 141.315 27.368  20.342  1.000 35.950  ? 165 PRO BBB O   1 
ATOM 3028  C CB  . PRO B 1 148 ? 138.497 26.160  20.991  1.000 36.710  ? 165 PRO BBB CB  1 
ATOM 3029  C CG  . PRO B 1 148 ? 139.425 25.498  21.969  1.000 37.410  ? 165 PRO BBB CG  1 
ATOM 3030  C CD  . PRO B 1 148 ? 140.167 24.471  21.128  1.000 40.710  ? 165 PRO BBB CD  1 
ATOM 3031  N N   . ASP B 1 149 ? 139.859 28.433  18.983  1.000 44.440  ? 166 ASP BBB N   1 
ATOM 3032  C CA  . ASP B 1 149 ? 140.398 29.812  19.012  1.000 44.930  ? 166 ASP BBB CA  1 
ATOM 3033  C C   . ASP B 1 149 ? 140.823 30.183  20.442  1.000 40.470  ? 166 ASP BBB C   1 
ATOM 3034  O O   . ASP B 1 149 ? 139.974 30.198  21.341  1.000 35.160  ? 166 ASP BBB O   1 
ATOM 3035  C CB  . ASP B 1 149 ? 139.309 30.732  18.470  1.000 51.820  ? 166 ASP BBB CB  1 
ATOM 3036  C CG  . ASP B 1 149 ? 139.848 31.987  17.833  1.000 59.400  ? 166 ASP BBB CG  1 
ATOM 3037  O OD1 . ASP B 1 149 ? 140.741 32.622  18.437  1.000 63.920  ? 166 ASP BBB OD1 1 
ATOM 3038  O OD2 . ASP B 1 149 ? 139.365 32.324  16.754  1.000 70.970  ? 166 ASP BBB OD2 1 
ATOM 3039  N N   . GLY B 1 150 ? 142.101 30.479  20.655  1.000 41.570  ? 167 GLY BBB N   1 
ATOM 3040  C CA  . GLY B 1 150 ? 142.591 30.986  21.951  1.000 41.510  ? 167 GLY BBB CA  1 
ATOM 3041  C C   . GLY B 1 150 ? 143.544 30.023  22.626  1.000 38.740  ? 167 GLY BBB C   1 
ATOM 3042  O O   . GLY B 1 150 ? 144.158 30.417  23.644  1.000 35.980  ? 167 GLY BBB O   1 
ATOM 3043  N N   . THR B 1 151 ? 143.640 28.805  22.092  1.000 37.610  ? 168 THR BBB N   1 
ATOM 3044  C CA  . THR B 1 151 ? 144.570 27.736  22.536  1.000 38.850  ? 168 THR BBB CA  1 
ATOM 3045  C C   . THR B 1 151 ? 145.645 27.564  21.471  1.000 34.050  ? 168 THR BBB C   1 
ATOM 3046  O O   . THR B 1 151 ? 145.334 27.772  20.312  1.000 39.410  ? 168 THR BBB O   1 
ATOM 3047  C CB  . THR B 1 151 ? 143.817 26.417  22.743  1.000 39.940  ? 168 THR BBB CB  1 
ATOM 3048  O OG1 . THR B 1 151 ? 143.291 25.977  21.491  1.000 46.550  ? 168 THR BBB OG1 1 
ATOM 3049  C CG2 . THR B 1 151 ? 142.671 26.549  23.718  1.000 39.160  ? 168 THR BBB CG2 1 
ATOM 3050  N N   . ILE B 1 152 ? 146.851 27.197  21.861  1.000 30.130  ? 169 ILE BBB N   1 
ATOM 3051  C CA  . ILE B 1 152 ? 147.968 26.863  20.940  1.000 29.680  ? 169 ILE BBB CA  1 
ATOM 3052  C C   . ILE B 1 152 ? 147.915 25.351  20.714  1.000 33.850  ? 169 ILE BBB C   1 
ATOM 3053  O O   . ILE B 1 152 ? 148.075 24.597  21.675  1.000 38.970  ? 169 ILE BBB O   1 
ATOM 3054  C CB  . ILE B 1 152 ? 149.289 27.358  21.558  1.000 27.300  ? 169 ILE BBB CB  1 
ATOM 3055  C CG1 . ILE B 1 152 ? 149.312 28.883  21.604  1.000 27.420  ? 169 ILE BBB CG1 1 
ATOM 3056  C CG2 . ILE B 1 152 ? 150.509 26.824  20.849  1.000 25.880  ? 169 ILE BBB CG2 1 
ATOM 3057  C CD1 . ILE B 1 152 ? 150.352 29.416  22.551  1.000 28.670  ? 169 ILE BBB CD1 1 
ATOM 3058  N N   . PHE B 1 153 ? 147.668 24.917  19.487  1.000 37.310  ? 170 PHE BBB N   1 
ATOM 3059  C CA  . PHE B 1 153 ? 147.467 23.489  19.159  1.000 38.650  ? 170 PHE BBB CA  1 
ATOM 3060  C C   . PHE B 1 153 ? 148.356 23.096  17.988  1.000 40.010  ? 170 PHE BBB C   1 
ATOM 3061  O O   . PHE B 1 153 ? 148.859 23.950  17.278  1.000 45.810  ? 170 PHE BBB O   1 
ATOM 3062  C CB  . PHE B 1 153 ? 145.990 23.243  18.842  1.000 42.100  ? 170 PHE BBB CB  1 
ATOM 3063  C CG  . PHE B 1 153 ? 145.411 24.168  17.812  1.000 43.800  ? 170 PHE BBB CG  1 
ATOM 3064  C CD1 . PHE B 1 153 ? 144.956 25.426  18.165  1.000 44.430  ? 170 PHE BBB CD1 1 
ATOM 3065  C CD2 . PHE B 1 153 ? 145.302 23.766  16.496  1.000 46.850  ? 170 PHE BBB CD2 1 
ATOM 3066  C CE1 . PHE B 1 153 ? 144.418 26.274  17.215  1.000 46.410  ? 170 PHE BBB CE1 1 
ATOM 3067  C CE2 . PHE B 1 153 ? 144.731 24.611  15.554  1.000 50.400  ? 170 PHE BBB CE2 1 
ATOM 3068  C CZ  . PHE B 1 153 ? 144.311 25.868  15.909  1.000 47.640  ? 170 PHE BBB CZ  1 
ATOM 3069  N N   . PRO B 1 154 ? 148.580 21.787  17.763  1.000 44.090  ? 171 PRO BBB N   1 
ATOM 3070  C CA  . PRO B 1 154 ? 149.264 21.287  16.570  1.000 42.800  ? 171 PRO BBB CA  1 
ATOM 3071  C C   . PRO B 1 154 ? 148.663 21.847  15.282  1.000 42.260  ? 171 PRO BBB C   1 
ATOM 3072  O O   . PRO B 1 154 ? 147.476 21.687  15.091  1.000 41.690  ? 171 PRO BBB O   1 
ATOM 3073  C CB  . PRO B 1 154 ? 148.979 19.782  16.635  1.000 41.860  ? 171 PRO BBB CB  1 
ATOM 3074  C CG  . PRO B 1 154 ? 148.982 19.519  18.095  1.000 45.490  ? 171 PRO BBB CG  1 
ATOM 3075  C CD  . PRO B 1 154 ? 148.214 20.691  18.667  1.000 49.540  ? 171 PRO BBB CD  1 
ATOM 3076  N N   . LYS B 1 155 ? 149.505 22.470  14.463  1.000 41.760  ? 172 LYS BBB N   1 
ATOM 3077  C CA  . LYS B 1 155 ? 149.113 23.084  13.169  1.000 44.510  ? 172 LYS BBB CA  1 
ATOM 3078  C C   . LYS B 1 155 ? 149.499 22.106  12.055  1.000 44.240  ? 172 LYS BBB C   1 
ATOM 3079  O O   . LYS B 1 155 ? 150.483 21.379  12.254  1.000 43.660  ? 172 LYS BBB O   1 
ATOM 3080  C CB  . LYS B 1 155 ? 149.791 24.445  13.002  1.000 47.760  ? 172 LYS BBB CB  1 
ATOM 3081  C CG  . LYS B 1 155 ? 149.375 25.516  13.997  1.000 54.390  ? 172 LYS BBB CG  1 
ATOM 3082  C CD  . LYS B 1 155 ? 150.240 26.775  13.866  1.000 63.840  ? 172 LYS BBB CD  1 
ATOM 3083  C CE  . LYS B 1 155 ? 151.641 26.688  14.463  1.000 69.420  ? 172 LYS BBB CE  1 
ATOM 3084  N NZ  . LYS B 1 155 ? 151.649 26.804  15.952  1.000 69.970  ? 172 LYS BBB NZ  1 
ATOM 3085  N N   . ASN B 1 156 ? 148.735 22.084  10.954  1.000 41.270  ? 173 ASN BBB N   1 
ATOM 3086  C CA  . ASN B 1 156 ? 148.977 21.229  9.762   1.000 37.830  ? 173 ASN BBB CA  1 
ATOM 3087  C C   . ASN B 1 156 ? 148.817 19.769  10.162  1.000 37.550  ? 173 ASN BBB C   1 
ATOM 3088  O O   . ASN B 1 156 ? 149.665 18.929  9.771   1.000 38.280  ? 173 ASN BBB O   1 
ATOM 3089  C CB  . ASN B 1 156 ? 150.351 21.475  9.139   1.000 36.780  ? 173 ASN BBB CB  1 
ATOM 3090  C CG  . ASN B 1 156 ? 150.467 22.892  8.649   1.000 38.380  ? 173 ASN BBB CG  1 
ATOM 3091  O OD1 . ASN B 1 156 ? 149.582 23.382  7.952   1.000 37.900  ? 173 ASN BBB OD1 1 
ATOM 3092  N ND2 . ASN B 1 156 ? 151.536 23.561  9.032   1.000 39.390  ? 173 ASN BBB ND2 1 
ATOM 3093  N N   . ALA B 1 157 ? 147.763 19.489  10.919  1.000 36.060  ? 174 ALA BBB N   1 
ATOM 3094  C CA  . ALA B 1 157 ? 147.397 18.124  11.339  1.000 35.910  ? 174 ALA BBB CA  1 
ATOM 3095  C C   . ALA B 1 157 ? 147.211 17.270  10.089  1.000 31.720  ? 174 ALA BBB C   1 
ATOM 3096  O O   . ALA B 1 157 ? 146.528 17.694  9.181   1.000 26.420  ? 174 ALA BBB O   1 
ATOM 3097  C CB  . ALA B 1 157 ? 146.141 18.142  12.166  1.000 39.280  ? 174 ALA BBB CB  1 
ATOM 3098  N N   . THR B 1 158 ? 147.843 16.109  10.083  1.000 32.640  ? 175 THR BBB N   1 
ATOM 3099  C CA  . THR B 1 158 ? 147.637 15.032  9.099   1.000 31.900  ? 175 THR BBB CA  1 
ATOM 3100  C C   . THR B 1 158 ? 147.170 13.803  9.885   1.000 32.210  ? 175 THR BBB C   1 
ATOM 3101  O O   . THR B 1 158 ? 147.254 13.803  11.130  1.000 31.020  ? 175 THR BBB O   1 
ATOM 3102  C CB  . THR B 1 158 ? 148.917 14.879  8.275   1.000 32.670  ? 175 THR BBB CB  1 
ATOM 3103  O OG1 . THR B 1 158 ? 149.938 14.212  9.020   1.000 32.720  ? 175 THR BBB OG1 1 
ATOM 3104  C CG2 . THR B 1 158 ? 149.459 16.231  7.865   1.000 34.470  ? 175 THR BBB CG2 1 
ATOM 3105  N N   . VAL B 1 159 ? 146.670 12.791  9.193   1.000 30.920  ? 176 VAL BBB N   1 
ATOM 3106  C CA  . VAL B 1 159 ? 146.328 11.518  9.864   1.000 30.710  ? 176 VAL BBB CA  1 
ATOM 3107  C C   . VAL B 1 159 ? 147.548 11.058  10.682  1.000 32.720  ? 176 VAL BBB C   1 
ATOM 3108  O O   . VAL B 1 159 ? 147.347 10.576  11.790  1.000 34.360  ? 176 VAL BBB O   1 
ATOM 3109  C CB  . VAL B 1 159 ? 145.841 10.470  8.856   1.000 30.770  ? 176 VAL BBB CB  1 
ATOM 3110  C CG1 . VAL B 1 159 ? 146.994 9.738   8.198   1.000 30.340  ? 176 VAL BBB CG1 1 
ATOM 3111  C CG2 . VAL B 1 159 ? 144.888 9.487   9.524   1.000 33.630  ? 176 VAL BBB CG2 1 
ATOM 3112  N N   . GLN B 1 160 ? 148.776 11.247  10.198  1.000 35.580  ? 177 GLN BBB N   1 
ATOM 3113  C CA  . GLN B 1 160 ? 150.000 10.810  10.935  1.000 36.010  ? 177 GLN BBB CA  1 
ATOM 3114  C C   . GLN B 1 160 ? 150.059 11.508  12.285  1.000 33.140  ? 177 GLN BBB C   1 
ATOM 3115  O O   . GLN B 1 160 ? 150.629 10.917  13.199  1.000 37.130  ? 177 GLN BBB O   1 
ATOM 3116  C CB  . GLN B 1 160 ? 151.287 11.055  10.152  1.000 43.400  ? 177 GLN BBB CB  1 
ATOM 3117  C CG  . GLN B 1 160 ? 151.354 10.219  8.866   1.000 53.220  ? 177 GLN BBB CG  1 
ATOM 3118  C CD  . GLN B 1 160 ? 151.198 8.721   9.069   1.000 60.280  ? 177 GLN BBB CD  1 
ATOM 3119  O OE1 . GLN B 1 160 ? 151.833 8.109   9.949   1.000 56.080  ? 177 GLN BBB OE1 1 
ATOM 3120  N NE2 . GLN B 1 160 ? 150.382 8.102   8.213   1.000 58.250  ? 177 GLN BBB NE2 1 
ATOM 3121  N N   . SER B 1 161 ? 149.452 12.685  12.427  1.000 31.720  ? 178 SER BBB N   1 
ATOM 3122  C CA  . SER B 1 161 ? 149.420 13.436  13.712  1.000 30.140  ? 178 SER BBB CA  1 
ATOM 3123  C C   . SER B 1 161 ? 148.845 12.543  14.826  1.000 29.610  ? 178 SER BBB C   1 
ATOM 3124  O O   . SER B 1 161 ? 149.330 12.684  15.979  1.000 32.570  ? 178 SER BBB O   1 
ATOM 3125  C CB  . SER B 1 161 ? 148.672 14.739  13.569  1.000 28.110  ? 178 SER BBB CB  1 
ATOM 3126  O OG  . SER B 1 161 ? 149.334 15.606  12.673  1.000 26.210  ? 178 SER BBB OG  1 
ATOM 3127  N N   . GLN B 1 162 ? 147.903 11.652  14.476  1.000 27.120  ? 179 GLN BBB N   1 
ATOM 3128  C CA  . GLN B 1 162 ? 147.211 10.698  15.389  1.000 28.170  ? 179 GLN BBB CA  1 
ATOM 3129  C C   . GLN B 1 162 ? 148.191 9.704   16.041  1.000 26.280  ? 179 GLN BBB C   1 
ATOM 3130  O O   . GLN B 1 162 ? 147.827 9.171   17.114  1.000 23.090  ? 179 GLN BBB O   1 
ATOM 3131  C CB  . GLN B 1 162 ? 146.122 9.904   14.656  1.000 29.630  ? 179 GLN BBB CB  1 
ATOM 3132  C CG  . GLN B 1 162 ? 144.731 10.500  14.782  1.000 30.060  ? 179 GLN BBB CG  1 
ATOM 3133  C CD  . GLN B 1 162 ? 143.754 10.070  13.708  1.000 31.910  ? 179 GLN BBB CD  1 
ATOM 3134  O OE1 . GLN B 1 162 ? 142.763 10.755  13.446  1.000 32.480  ? 179 GLN BBB OE1 1 
ATOM 3135  N NE2 . GLN B 1 162 ? 144.016 8.937   13.064  1.000 29.600  ? 179 GLN BBB NE2 1 
ATOM 3136  N N   . VAL B 1 163 ? 149.349 9.411   15.434  1.000 24.860  ? 180 VAL BBB N   1 
ATOM 3137  C CA  . VAL B 1 163 ? 150.299 8.434   16.042  1.000 29.730  ? 180 VAL BBB CA  1 
ATOM 3138  C C   . VAL B 1 163 ? 151.624 9.117   16.359  1.000 30.680  ? 180 VAL BBB C   1 
ATOM 3139  O O   . VAL B 1 163 ? 152.123 8.928   17.517  1.000 32.470  ? 180 VAL BBB O   1 
ATOM 3140  C CB  . VAL B 1 163 ? 150.523 7.174   15.190  1.000 31.450  ? 180 VAL BBB CB  1 
ATOM 3141  C CG1 . VAL B 1 163 ? 149.262 6.327   15.128  1.000 32.740  ? 180 VAL BBB CG1 1 
ATOM 3142  C CG2 . VAL B 1 163 ? 151.049 7.478   13.809  1.000 32.220  ? 180 VAL BBB CG2 1 
ATOM 3143  N N   . MET B 1 164 ? 152.135 9.864   15.389  1.000 30.700  ? 181 MET BBB N   1 
ATOM 3144  C CA  . MET B 1 164 ? 153.345 10.691  15.545  1.000 37.350  ? 181 MET BBB CA  1 
ATOM 3145  C C   . MET B 1 164 ? 153.586 11.542  14.289  1.000 37.790  ? 181 MET BBB C   1 
ATOM 3146  O O   . MET B 1 164 ? 153.535 11.004  13.149  1.000 36.590  ? 181 MET BBB O   1 
ATOM 3147  C CB  . MET B 1 164 ? 154.556 9.790   15.781  1.000 43.270  ? 181 MET BBB CB  1 
ATOM 3148  C CG  . MET B 1 164 ? 155.792 10.565  16.163  1.000 46.270  ? 181 MET BBB CG  1 
ATOM 3149  S SD  . MET B 1 164 ? 155.549 11.519  17.648  1.000 42.610  ? 181 MET BBB SD  1 
ATOM 3150  C CE  . MET B 1 164 ? 157.048 12.499  17.554  1.000 52.440  ? 181 MET BBB CE  1 
ATOM 3151  N N   . ASN B 1 165 ? 153.882 12.825  14.492  1.000 36.760  ? 182 ASN BBB N   1 
ATOM 3152  C CA  . ASN B 1 165 ? 154.170 13.779  13.390  1.000 34.550  ? 182 ASN BBB CA  1 
ATOM 3153  C C   . ASN B 1 165 ? 155.148 14.840  13.913  1.000 33.590  ? 182 ASN BBB C   1 
ATOM 3154  O O   . ASN B 1 165 ? 154.711 15.719  14.655  1.000 38.150  ? 182 ASN BBB O   1 
ATOM 3155  C CB  . ASN B 1 165 ? 152.854 14.350  12.864  1.000 31.460  ? 182 ASN BBB CB  1 
ATOM 3156  C CG  . ASN B 1 165 ? 153.036 15.495  11.898  1.000 28.680  ? 182 ASN BBB CG  1 
ATOM 3157  O OD1 . ASN B 1 165 ? 154.106 16.070  11.826  1.000 26.360  ? 182 ASN BBB OD1 1 
ATOM 3158  N ND2 . ASN B 1 165 ? 151.996 15.834  11.151  1.000 31.030  ? 182 ASN BBB ND2 1 
ATOM 3159  N N   . THR B 1 166 ? 156.418 14.765  13.528  1.000 30.810  ? 183 THR BBB N   1 
ATOM 3160  C CA  . THR B 1 166 ? 157.507 15.584  14.111  1.000 31.030  ? 183 THR BBB CA  1 
ATOM 3161  C C   . THR B 1 166 ? 157.337 17.073  13.788  1.000 31.300  ? 183 THR BBB C   1 
ATOM 3162  O O   . THR B 1 166 ? 158.086 17.875  14.382  1.000 31.640  ? 183 THR BBB O   1 
ATOM 3163  C CB  . THR B 1 166 ? 158.879 15.119  13.629  1.000 31.250  ? 183 THR BBB CB  1 
ATOM 3164  O OG1 . THR B 1 166 ? 158.666 14.680  12.304  1.000 31.210  ? 183 THR BBB OG1 1 
ATOM 3165  C CG2 . THR B 1 166 ? 159.444 13.966  14.414  1.000 33.750  ? 183 THR BBB CG2 1 
ATOM 3166  N N   . GLU B 1 167 ? 156.398 17.454  12.927  1.000 33.580  ? 184 GLU BBB N   1 
ATOM 3167  C CA  . GLU B 1 167 ? 156.069 18.893  12.716  1.000 38.700  ? 184 GLU BBB CA  1 
ATOM 3168  C C   . GLU B 1 167 ? 155.648 19.515  14.051  1.000 37.960  ? 184 GLU BBB C   1 
ATOM 3169  O O   . GLU B 1 167 ? 156.131 20.604  14.336  1.000 45.070  ? 184 GLU BBB O   1 
ATOM 3170  C CB  . GLU B 1 167 ? 154.994 19.134  11.646  1.000 42.360  ? 184 GLU BBB CB  1 
ATOM 3171  C CG  . GLU B 1 167 ? 155.211 20.439  10.886  1.000 44.170  ? 184 GLU BBB CG  1 
ATOM 3172  C CD  . GLU B 1 167 ? 154.002 21.054  10.194  1.000 43.530  ? 184 GLU BBB CD  1 
ATOM 3173  O OE1 . GLU B 1 167 ? 153.468 22.059  10.726  1.000 42.760  ? 184 GLU BBB OE1 1 
ATOM 3174  O OE2 . GLU B 1 167 ? 153.619 20.561  9.107   1.000 40.400  ? 184 GLU BBB OE2 1 
ATOM 3175  N N   . HIS B 1 168 ? 154.833 18.825  14.856  1.000 37.750  ? 185 HIS BBB N   1 
ATOM 3176  C CA  . HIS B 1 168 ? 154.160 19.359  16.078  1.000 32.840  ? 185 HIS BBB CA  1 
ATOM 3177  C C   . HIS B 1 168 ? 155.132 19.486  17.252  1.000 29.470  ? 185 HIS BBB C   1 
ATOM 3178  O O   . HIS B 1 168 ? 154.935 18.795  18.259  1.000 29.660  ? 185 HIS BBB O   1 
ATOM 3179  C CB  . HIS B 1 168 ? 152.987 18.464  16.469  1.000 31.480  ? 185 HIS BBB CB  1 
ATOM 3180  C CG  . HIS B 1 168 ? 152.057 18.207  15.349  1.000 31.170  ? 185 HIS BBB CG  1 
ATOM 3181  N ND1 . HIS B 1 168 ? 151.619 19.211  14.533  1.000 33.510  ? 185 HIS BBB ND1 1 
ATOM 3182  C CD2 . HIS B 1 168 ? 151.480 17.076  14.903  1.000 34.120  ? 185 HIS BBB CD2 1 
ATOM 3183  C CE1 . HIS B 1 168 ? 150.784 18.715  13.642  1.000 33.890  ? 185 HIS BBB CE1 1 
ATOM 3184  N NE2 . HIS B 1 168 ? 150.685 17.407  13.839  1.000 34.400  ? 185 HIS BBB NE2 1 
ATOM 3185  N N   . LYS B 1 169 ? 156.096 20.389  17.156  1.000 26.940  ? 186 LYS BBB N   1 
ATOM 3186  C CA  . LYS B 1 169 ? 156.930 20.814  18.305  1.000 27.070  ? 186 LYS BBB CA  1 
ATOM 3187  C C   . LYS B 1 169 ? 156.430 22.179  18.805  1.000 28.930  ? 186 LYS BBB C   1 
ATOM 3188  O O   . LYS B 1 169 ? 155.748 22.891  18.039  1.000 28.450  ? 186 LYS BBB O   1 
ATOM 3189  C CB  . LYS B 1 169 ? 158.401 20.833  17.910  1.000 25.950  ? 186 LYS BBB CB  1 
ATOM 3190  C CG  . LYS B 1 169 ? 158.845 19.604  17.133  1.000 28.180  ? 186 LYS BBB CG  1 
ATOM 3191  C CD  . LYS B 1 169 ? 158.994 18.382  17.979  1.000 29.190  ? 186 LYS BBB CD  1 
ATOM 3192  C CE  . LYS B 1 169 ? 159.720 17.256  17.259  1.000 29.670  ? 186 LYS BBB CE  1 
ATOM 3193  N NZ  . LYS B 1 169 ? 159.840 16.041  18.106  1.000 31.840  ? 186 LYS BBB NZ  1 
ATOM 3194  N N   . ALA B 1 170 ? 156.709 22.495  20.069  1.000 28.850  ? 187 ALA BBB N   1 
ATOM 3195  C CA  . ALA B 1 170 ? 156.248 23.720  20.741  1.000 30.300  ? 187 ALA BBB CA  1 
ATOM 3196  C C   . ALA B 1 170 ? 156.898 23.864  22.123  1.000 33.830  ? 187 ALA BBB C   1 
ATOM 3197  O O   . ALA B 1 170 ? 157.348 22.854  22.674  1.000 33.090  ? 187 ALA BBB O   1 
ATOM 3198  C CB  . ALA B 1 170 ? 154.754 23.684  20.831  1.000 29.560  ? 187 ALA BBB CB  1 
ATOM 3199  N N   . TYR B 1 171 ? 156.896 25.084  22.668  1.000 39.080  ? 188 TYR BBB N   1 
ATOM 3200  C CA  . TYR B 1 171 ? 157.434 25.391  24.013  1.000 43.510  ? 188 TYR BBB CA  1 
ATOM 3201  C C   . TYR B 1 171 ? 156.272 25.701  24.962  1.000 47.250  ? 188 TYR BBB C   1 
ATOM 3202  O O   . TYR B 1 171 ? 155.394 26.499  24.590  1.000 48.780  ? 188 TYR BBB O   1 
ATOM 3203  C CB  . TYR B 1 171 ? 158.425 26.551  23.915  1.000 45.700  ? 188 TYR BBB CB  1 
ATOM 3204  C CG  . TYR B 1 171 ? 159.693 26.247  23.155  1.000 47.720  ? 188 TYR BBB CG  1 
ATOM 3205  C CD1 . TYR B 1 171 ? 160.726 25.546  23.756  1.000 49.750  ? 188 TYR BBB CD1 1 
ATOM 3206  C CD2 . TYR B 1 171 ? 159.863 26.658  21.844  1.000 43.400  ? 188 TYR BBB CD2 1 
ATOM 3207  C CE1 . TYR B 1 171 ? 161.889 25.256  23.074  1.000 51.550  ? 188 TYR BBB CE1 1 
ATOM 3208  C CE2 . TYR B 1 171 ? 161.035 26.406  21.159  1.000 44.250  ? 188 TYR BBB CE2 1 
ATOM 3209  C CZ  . TYR B 1 171 ? 162.052 25.696  21.775  1.000 50.510  ? 188 TYR BBB CZ  1 
ATOM 3210  O OH  . TYR B 1 171 ? 163.237 25.399  21.154  1.000 52.270  ? 188 TYR BBB OH  1 
ATOM 3211  N N   . LEU B 1 172 ? 156.249 25.086  26.146  1.000 48.930  ? 189 LEU BBB N   1 
ATOM 3212  C CA  . LEU B 1 172 ? 155.290 25.458  27.216  1.000 48.270  ? 189 LEU BBB CA  1 
ATOM 3213  C C   . LEU B 1 172 ? 155.753 26.782  27.822  1.000 47.820  ? 189 LEU BBB C   1 
ATOM 3214  O O   . LEU B 1 172 ? 156.463 26.774  28.865  1.000 44.670  ? 189 LEU BBB O   1 
ATOM 3215  C CB  . LEU B 1 172 ? 155.191 24.370  28.287  1.000 49.490  ? 189 LEU BBB CB  1 
ATOM 3216  C CG  . LEU B 1 172 ? 154.092 24.622  29.336  1.000 49.610  ? 189 LEU BBB CG  1 
ATOM 3217  C CD1 . LEU B 1 172 ? 152.756 24.997  28.706  1.000 48.850  ? 189 LEU BBB CD1 1 
ATOM 3218  C CD2 . LEU B 1 172 ? 153.910 23.405  30.199  1.000 53.860  ? 189 LEU BBB CD2 1 
ATOM 3219  N N   . ASP B 1 173 ? 155.348 27.862  27.152  1.000 47.260  ? 190 ASP BBB N   1 
ATOM 3220  C CA  . ASP B 1 173 ? 155.819 29.253  27.376  1.000 45.900  ? 190 ASP BBB CA  1 
ATOM 3221  C C   . ASP B 1 173 ? 154.636 30.170  27.712  1.000 40.620  ? 190 ASP BBB C   1 
ATOM 3222  O O   . ASP B 1 173 ? 154.859 31.363  27.833  1.000 41.380  ? 190 ASP BBB O   1 
ATOM 3223  C CB  . ASP B 1 173 ? 156.548 29.771  26.131  1.000 43.780  ? 190 ASP BBB CB  1 
ATOM 3224  C CG  . ASP B 1 173 ? 155.740 29.656  24.853  1.000 46.740  ? 190 ASP BBB CG  1 
ATOM 3225  O OD1 . ASP B 1 173 ? 154.496 29.471  24.926  1.000 48.890  ? 190 ASP BBB OD1 1 
ATOM 3226  O OD2 . ASP B 1 173 ? 156.355 29.752  23.785  1.000 57.480  ? 190 ASP BBB OD2 1 
ATOM 3227  N N   . LYS B 1 174 ? 153.426 29.639  27.861  1.000 38.290  ? 191 LYS BBB N   1 
ATOM 3228  C CA  . LYS B 1 174 ? 152.203 30.453  28.050  1.000 39.850  ? 191 LYS BBB CA  1 
ATOM 3229  C C   . LYS B 1 174 ? 151.124 29.661  28.827  1.000 40.750  ? 191 LYS BBB C   1 
ATOM 3230  O O   . LYS B 1 174 ? 150.930 28.435  28.586  1.000 45.220  ? 191 LYS BBB O   1 
ATOM 3231  C CB  . LYS B 1 174 ? 151.712 30.932  26.683  1.000 44.250  ? 191 LYS BBB CB  1 
ATOM 3232  C CG  . LYS B 1 174 ? 150.701 32.067  26.780  1.000 51.970  ? 191 LYS BBB CG  1 
ATOM 3233  C CD  . LYS B 1 174 ? 150.020 32.501  25.517  1.000 52.330  ? 191 LYS BBB CD  1 
ATOM 3234  C CE  . LYS B 1 174 ? 149.112 33.671  25.829  1.000 54.800  ? 191 LYS BBB CE  1 
ATOM 3235  N NZ  . LYS B 1 174 ? 148.643 34.321  24.591  1.000 65.160  ? 191 LYS BBB NZ  1 
ATOM 3236  N N   . ASN B 1 175 ? 150.415 30.345  29.718  1.000 37.330  ? 192 ASN BBB N   1 
ATOM 3237  C CA  . ASN B 1 175 ? 149.351 29.723  30.531  1.000 38.700  ? 192 ASN BBB CA  1 
ATOM 3238  C C   . ASN B 1 175 ? 148.022 29.796  29.794  1.000 36.610  ? 192 ASN BBB C   1 
ATOM 3239  O O   . ASN B 1 175 ? 147.884 30.607  28.874  1.000 30.540  ? 192 ASN BBB O   1 
ATOM 3240  C CB  . ASN B 1 175 ? 149.254 30.384  31.900  1.000 42.410  ? 192 ASN BBB CB  1 
ATOM 3241  C CG  . ASN B 1 175 ? 149.900 29.522  32.949  1.000 43.400  ? 192 ASN BBB CG  1 
ATOM 3242  O OD1 . ASN B 1 175 ? 149.251 28.633  33.499  1.000 58.290  ? 192 ASN BBB OD1 1 
ATOM 3243  N ND2 . ASN B 1 175 ? 151.171 29.755  33.184  1.000 35.420  ? 192 ASN BBB ND2 1 
ATOM 3244  N N   . LYS B 1 176 ? 147.083 28.956  30.210  1.000 39.550  ? 193 LYS BBB N   1 
ATOM 3245  C CA  . LYS B 1 176 ? 145.701 28.950  29.672  1.000 40.040  ? 193 LYS BBB CA  1 
ATOM 3246  C C   . LYS B 1 176 ? 145.787 28.777  28.160  1.000 37.630  ? 193 LYS BBB C   1 
ATOM 3247  O O   . LYS B 1 176 ? 144.796 29.091  27.495  1.000 38.510  ? 193 LYS BBB O   1 
ATOM 3248  C CB  . LYS B 1 176 ? 144.964 30.227  30.086  1.000 40.550  ? 193 LYS BBB CB  1 
ATOM 3249  C CG  . LYS B 1 176 ? 144.903 30.447  31.599  1.000 45.260  ? 193 LYS BBB CG  1 
ATOM 3250  C CD  . LYS B 1 176 ? 144.507 31.836  32.038  1.000 55.910  ? 193 LYS BBB CD  1 
ATOM 3251  C CE  . LYS B 1 176 ? 143.050 32.166  31.753  1.000 69.850  ? 193 LYS BBB CE  1 
ATOM 3252  N NZ  . LYS B 1 176 ? 142.791 33.633  31.790  1.000 76.080  ? 193 LYS BBB NZ  1 
ATOM 3253  N N   . ALA B 1 177 ? 146.883 28.187  27.671  1.000 38.180  ? 194 ALA BBB N   1 
ATOM 3254  C CA  . ALA B 1 177 ? 147.249 28.179  26.236  1.000 39.840  ? 194 ALA BBB CA  1 
ATOM 3255  C C   . ALA B 1 177 ? 147.248 26.760  25.669  1.000 37.690  ? 194 ALA BBB C   1 
ATOM 3256  O O   . ALA B 1 177 ? 146.511 26.517  24.694  1.000 35.380  ? 194 ALA BBB O   1 
ATOM 3257  C CB  . ALA B 1 177 ? 148.601 28.829  26.065  1.000 44.650  ? 194 ALA BBB CB  1 
ATOM 3258  N N   . TYR B 1 178 ? 148.055 25.864  26.237  1.000 38.800  ? 195 TYR BBB N   1 
ATOM 3259  C CA  . TYR B 1 178 ? 148.359 24.546  25.629  1.000 39.530  ? 195 TYR BBB CA  1 
ATOM 3260  C C   . TYR B 1 178 ? 147.418 23.498  26.209  1.000 35.410  ? 195 TYR BBB C   1 
ATOM 3261  O O   . TYR B 1 178 ? 147.625 23.018  27.316  1.000 36.910  ? 195 TYR BBB O   1 
ATOM 3262  C CB  . TYR B 1 178 ? 149.831 24.185  25.846  1.000 41.880  ? 195 TYR BBB CB  1 
ATOM 3263  C CG  . TYR B 1 178 ? 150.797 25.082  25.116  1.000 42.500  ? 195 TYR BBB CG  1 
ATOM 3264  C CD1 . TYR B 1 178 ? 151.215 26.279  25.666  1.000 44.690  ? 195 TYR BBB CD1 1 
ATOM 3265  C CD2 . TYR B 1 178 ? 151.287 24.740  23.871  1.000 43.390  ? 195 TYR BBB CD2 1 
ATOM 3266  C CE1 . TYR B 1 178 ? 152.095 27.116  24.999  1.000 45.700  ? 195 TYR BBB CE1 1 
ATOM 3267  C CE2 . TYR B 1 178 ? 152.167 25.565  23.192  1.000 47.930  ? 195 TYR BBB CE2 1 
ATOM 3268  C CZ  . TYR B 1 178 ? 152.567 26.766  23.750  1.000 46.450  ? 195 TYR BBB CZ  1 
ATOM 3269  O OH  . TYR B 1 178 ? 153.440 27.576  23.076  1.000 42.680  ? 195 TYR BBB OH  1 
ATOM 3270  N N   . PRO B 1 179 ? 146.385 23.065  25.462  1.000 32.530  ? 196 PRO BBB N   1 
ATOM 3271  C CA  . PRO B 1 179 ? 145.481 22.032  25.948  1.000 34.160  ? 196 PRO BBB CA  1 
ATOM 3272  C C   . PRO B 1 179 ? 146.286 20.800  26.377  1.000 32.970  ? 196 PRO BBB C   1 
ATOM 3273  O O   . PRO B 1 179 ? 147.256 20.515  25.704  1.000 32.120  ? 196 PRO BBB O   1 
ATOM 3274  C CB  . PRO B 1 179 ? 144.609 21.706  24.725  1.000 33.230  ? 196 PRO BBB CB  1 
ATOM 3275  C CG  . PRO B 1 179 ? 144.628 22.974  23.949  1.000 33.600  ? 196 PRO BBB CG  1 
ATOM 3276  C CD  . PRO B 1 179 ? 146.045 23.492  24.102  1.000 32.130  ? 196 PRO BBB CD  1 
ATOM 3277  N N   . VAL B 1 180 ? 145.835 20.085  27.412  1.000 30.730  ? 197 VAL BBB N   1 
ATOM 3278  C CA  . VAL B 1 180 ? 146.533 18.886  27.939  1.000 31.590  ? 197 VAL BBB CA  1 
ATOM 3279  C C   . VAL B 1 180 ? 146.434 17.775  26.896  1.000 32.170  ? 197 VAL BBB C   1 
ATOM 3280  O O   . VAL B 1 180 ? 147.411 17.021  26.761  1.000 32.900  ? 197 VAL BBB O   1 
ATOM 3281  C CB  . VAL B 1 180 ? 145.928 18.453  29.294  1.000 34.070  ? 197 VAL BBB CB  1 
ATOM 3282  C CG1 . VAL B 1 180 ? 146.501 17.124  29.793  1.000 33.560  ? 197 VAL BBB CG1 1 
ATOM 3283  C CG2 . VAL B 1 180 ? 146.100 19.557  30.342  1.000 34.510  ? 197 VAL BBB CG2 1 
ATOM 3284  N N   . GLU B 1 181 ? 145.312 17.699  26.167  1.000 31.200  ? 198 GLU BBB N   1 
ATOM 3285  C CA  . GLU B 1 181 ? 144.927 16.470  25.428  1.000 30.500  ? 198 GLU BBB CA  1 
ATOM 3286  C C   . GLU B 1 181 ? 145.616 16.397  24.071  1.000 30.780  ? 198 GLU BBB C   1 
ATOM 3287  O O   . GLU B 1 181 ? 145.346 15.422  23.332  1.000 42.610  ? 198 GLU BBB O   1 
ATOM 3288  C CB  . GLU B 1 181 ? 143.403 16.385  25.309  1.000 30.880  ? 198 GLU BBB CB  1 
ATOM 3289  C CG  . GLU B 1 181 ? 142.769 17.246  24.233  1.000 29.420  ? 198 GLU BBB CG  1 
ATOM 3290  C CD  . GLU B 1 181 ? 141.283 16.984  24.046  1.000 27.540  ? 198 GLU BBB CD  1 
ATOM 3291  O OE1 . GLU B 1 181 ? 140.581 16.732  25.058  1.000 29.920  ? 198 GLU BBB OE1 1 
ATOM 3292  O OE2 . GLU B 1 181 ? 140.831 17.051  22.911  1.000 24.950  ? 198 GLU BBB OE2 1 
ATOM 3293  N N   . CYS B 1 182 ? 146.444 17.372  23.709  1.000 27.770  ? 199 CYS BBB N   1 
ATOM 3294  C CA  . CYS B 1 182 ? 147.104 17.359  22.372  1.000 28.370  ? 199 CYS BBB CA  1 
ATOM 3295  C C   . CYS B 1 182 ? 148.604 17.663  22.491  1.000 27.420  ? 199 CYS BBB C   1 
ATOM 3296  O O   . CYS B 1 182 ? 149.272 17.730  21.445  1.000 24.740  ? 199 CYS BBB O   1 
ATOM 3297  C CB  . CYS B 1 182 ? 146.377 18.261  21.370  1.000 27.480  ? 199 CYS BBB CB  1 
ATOM 3298  S SG  . CYS B 1 182 ? 146.140 19.974  21.904  1.000 24.360  ? 199 CYS BBB SG  1 
ATOM 3299  N N   . TRP B 1 183 ? 149.119 17.757  23.716  1.000 27.040  ? 200 TRP BBB N   1 
ATOM 3300  C CA  . TRP B 1 183 ? 150.562 18.007  23.976  1.000 27.350  ? 200 TRP BBB CA  1 
ATOM 3301  C C   . TRP B 1 183 ? 151.071 17.057  25.058  1.000 27.380  ? 200 TRP BBB C   1 
ATOM 3302  O O   . TRP B 1 183 ? 150.364 16.863  26.058  1.000 27.460  ? 200 TRP BBB O   1 
ATOM 3303  C CB  . TRP B 1 183 ? 150.816 19.467  24.386  1.000 27.030  ? 200 TRP BBB CB  1 
ATOM 3304  C CG  . TRP B 1 183 ? 150.460 20.485  23.350  1.000 27.640  ? 200 TRP BBB CG  1 
ATOM 3305  C CD1 . TRP B 1 183 ? 149.395 21.338  23.362  1.000 29.380  ? 200 TRP BBB CD1 1 
ATOM 3306  C CD2 . TRP B 1 183 ? 151.184 20.759  22.144  1.000 29.860  ? 200 TRP BBB CD2 1 
ATOM 3307  N NE1 . TRP B 1 183 ? 149.403 22.113  22.234  1.000 31.810  ? 200 TRP BBB NE1 1 
ATOM 3308  C CE2 . TRP B 1 183 ? 150.485 21.782  21.470  1.000 31.420  ? 200 TRP BBB CE2 1 
ATOM 3309  C CE3 . TRP B 1 183 ? 152.318 20.191  21.546  1.000 30.730  ? 200 TRP BBB CE3 1 
ATOM 3310  C CZ2 . TRP B 1 183 ? 150.895 22.267  20.231  1.000 32.420  ? 200 TRP BBB CZ2 1 
ATOM 3311  C CZ3 . TRP B 1 183 ? 152.740 20.680  20.333  1.000 30.400  ? 200 TRP BBB CZ3 1 
ATOM 3312  C CH2 . TRP B 1 183 ? 152.031 21.699  19.687  1.000 32.630  ? 200 TRP BBB CH2 1 
ATOM 3313  N N   . VAL B 1 184 ? 152.281 16.535  24.874  1.000 28.110  ? 201 VAL BBB N   1 
ATOM 3314  C CA  . VAL B 1 184 ? 153.019 15.772  25.916  1.000 28.790  ? 201 VAL BBB CA  1 
ATOM 3315  C C   . VAL B 1 184 ? 154.458 16.245  25.918  1.000 28.790  ? 201 VAL BBB C   1 
ATOM 3316  O O   . VAL B 1 184 ? 154.937 16.787  24.939  1.000 29.130  ? 201 VAL BBB O   1 
ATOM 3317  C CB  . VAL B 1 184 ? 152.938 14.268  25.641  1.000 30.790  ? 201 VAL BBB CB  1 
ATOM 3318  C CG1 . VAL B 1 184 ? 151.483 13.815  25.622  1.000 32.100  ? 201 VAL BBB CG1 1 
ATOM 3319  C CG2 . VAL B 1 184 ? 153.633 13.908  24.338  1.000 31.050  ? 201 VAL BBB CG2 1 
ATOM 3320  N N   . PRO B 1 185 ? 155.194 16.065  27.019  1.000 31.570  ? 202 PRO BBB N   1 
ATOM 3321  C CA  . PRO B 1 185 ? 156.633 16.285  27.009  1.000 33.140  ? 202 PRO BBB CA  1 
ATOM 3322  C C   . PRO B 1 185 ? 157.232 15.505  25.837  1.000 33.390  ? 202 PRO BBB C   1 
ATOM 3323  O O   . PRO B 1 185 ? 156.863 14.344  25.672  1.000 38.670  ? 202 PRO BBB O   1 
ATOM 3324  C CB  . PRO B 1 185 ? 157.087 15.740  28.369  1.000 34.310  ? 202 PRO BBB CB  1 
ATOM 3325  C CG  . PRO B 1 185 ? 155.862 15.848  29.252  1.000 34.460  ? 202 PRO BBB CG  1 
ATOM 3326  C CD  . PRO B 1 185 ? 154.691 15.645  28.331  1.000 34.900  ? 202 PRO BBB CD  1 
ATOM 3327  N N   . ASP B 1 186 ? 158.099 16.169  25.070  1.000 33.720  ? 203 ASP BBB N   1 
ATOM 3328  C CA  . ASP B 1 186 ? 158.793 15.623  23.875  1.000 35.610  ? 203 ASP BBB CA  1 
ATOM 3329  C C   . ASP B 1 186 ? 160.019 14.870  24.364  1.000 34.030  ? 203 ASP BBB C   1 
ATOM 3330  O O   . ASP B 1 186 ? 160.977 15.477  24.824  1.000 35.940  ? 203 ASP BBB O   1 
ATOM 3331  C CB  . ASP B 1 186 ? 159.182 16.743  22.902  1.000 39.550  ? 203 ASP BBB CB  1 
ATOM 3332  C CG  . ASP B 1 186 ? 159.929 16.292  21.655  1.000 40.370  ? 203 ASP BBB CG  1 
ATOM 3333  O OD1 . ASP B 1 186 ? 160.242 15.075  21.549  1.000 41.110  ? 203 ASP BBB OD1 1 
ATOM 3334  O OD2 . ASP B 1 186 ? 160.183 17.170  20.795  1.000 37.570  ? 203 ASP BBB OD2 1 
ATOM 3335  N N   . PRO B 1 187 ? 160.026 13.531  24.280  1.000 33.100  ? 204 PRO BBB N   1 
ATOM 3336  C CA  . PRO B 1 187 ? 161.054 12.730  24.923  1.000 36.900  ? 204 PRO BBB CA  1 
ATOM 3337  C C   . PRO B 1 187 ? 162.362 12.799  24.142  1.000 40.570  ? 204 PRO BBB C   1 
ATOM 3338  O O   . PRO B 1 187 ? 163.361 12.380  24.675  1.000 43.910  ? 204 PRO BBB O   1 
ATOM 3339  C CB  . PRO B 1 187 ? 160.494 11.314  24.875  1.000 36.720  ? 204 PRO BBB CB  1 
ATOM 3340  C CG  . PRO B 1 187 ? 159.671 11.323  23.617  1.000 36.650  ? 204 PRO BBB CG  1 
ATOM 3341  C CD  . PRO B 1 187 ? 159.065 12.712  23.548  1.000 35.630  ? 204 PRO BBB CD  1 
ATOM 3342  N N   . THR B 1 188 ? 162.299 13.316  22.911  1.000 43.340  ? 205 THR BBB N   1 
ATOM 3343  C CA  . THR B 1 188 ? 163.466 13.486  21.999  1.000 43.520  ? 205 THR BBB CA  1 
ATOM 3344  C C   . THR B 1 188 ? 164.217 14.770  22.354  1.000 42.410  ? 205 THR BBB C   1 
ATOM 3345  O O   . THR B 1 188 ? 165.258 15.020  21.748  1.000 42.040  ? 205 THR BBB O   1 
ATOM 3346  C CB  . THR B 1 188 ? 163.040 13.553  20.530  1.000 44.180  ? 205 THR BBB CB  1 
ATOM 3347  O OG1 . THR B 1 188 ? 162.466 14.851  20.332  1.000 47.040  ? 205 THR BBB OG1 1 
ATOM 3348  C CG2 . THR B 1 188 ? 162.077 12.457  20.129  1.000 45.060  ? 205 THR BBB CG2 1 
ATOM 3349  N N   . ARG B 1 189 ? 163.671 15.582  23.252  1.000 45.410  ? 206 ARG BBB N   1 
ATOM 3350  C CA  . ARG B 1 189 ? 164.286 16.860  23.690  1.000 51.500  ? 206 ARG BBB CA  1 
ATOM 3351  C C   . ARG B 1 189 ? 164.275 16.860  25.223  1.000 50.770  ? 206 ARG BBB C   1 
ATOM 3352  O O   . ARG B 1 189 ? 164.370 15.778  25.819  1.000 48.740  ? 206 ARG BBB O   1 
ATOM 3353  C CB  . ARG B 1 189 ? 163.551 18.035  23.028  1.000 55.000  ? 206 ARG BBB CB  1 
ATOM 3354  C CG  . ARG B 1 189 ? 163.607 18.022  21.509  1.000 60.010  ? 206 ARG BBB CG  1 
ATOM 3355  C CD  . ARG B 1 189 ? 162.980 19.219  20.816  1.000 63.880  ? 206 ARG BBB CD  1 
ATOM 3356  N NE  . ARG B 1 189 ? 163.135 19.035  19.367  1.000 70.800  ? 206 ARG BBB NE  1 
ATOM 3357  C CZ  . ARG B 1 189 ? 162.637 19.827  18.421  1.000 68.050  ? 206 ARG BBB CZ  1 
ATOM 3358  N NH1 . ARG B 1 189 ? 161.962 20.911  18.755  1.000 78.000  ? 206 ARG BBB NH1 1 
ATOM 3359  N NH2 . ARG B 1 189 ? 162.822 19.542  17.144  1.000 62.230  ? 206 ARG BBB NH2 1 
ATOM 3360  N N   . ASN B 1 190 ? 164.187 18.033  25.844  1.000 49.220  ? 207 ASN BBB N   1 
ATOM 3361  C CA  . ASN B 1 190 ? 164.038 18.199  27.313  1.000 45.870  ? 207 ASN BBB CA  1 
ATOM 3362  C C   . ASN B 1 190 ? 165.284 17.666  28.021  1.000 49.210  ? 207 ASN BBB C   1 
ATOM 3363  O O   . ASN B 1 190 ? 165.144 17.220  29.154  1.000 56.890  ? 207 ASN BBB O   1 
ATOM 3364  C CB  . ASN B 1 190 ? 162.747 17.566  27.832  1.000 43.320  ? 207 ASN BBB CB  1 
ATOM 3365  C CG  . ASN B 1 190 ? 161.520 18.374  27.485  1.000 40.710  ? 207 ASN BBB CG  1 
ATOM 3366  O OD1 . ASN B 1 190 ? 161.442 19.548  27.858  1.000 44.140  ? 207 ASN BBB OD1 1 
ATOM 3367  N ND2 . ASN B 1 190 ? 160.574 17.754  26.790  1.000 32.180  ? 207 ASN BBB ND2 1 
ATOM 3368  N N   . GLU B 1 191 ? 166.452 17.766  27.381  1.000 53.520  ? 208 GLU BBB N   1 
ATOM 3369  C CA  . GLU B 1 191 ? 167.768 17.510  28.017  1.000 53.320  ? 208 GLU BBB CA  1 
ATOM 3370  C C   . GLU B 1 191 ? 167.831 18.318  29.323  1.000 42.850  ? 208 GLU BBB C   1 
ATOM 3371  O O   . GLU B 1 191 ? 168.302 17.748  30.322  1.000 40.160  ? 208 GLU BBB O   1 
ATOM 3372  C CB  . GLU B 1 191 ? 168.894 17.831  27.021  1.000 63.890  ? 208 GLU BBB CB  1 
ATOM 3373  C CG  . GLU B 1 191 ? 170.297 17.940  27.637  1.000 72.560  ? 208 GLU BBB CG  1 
ATOM 3374  C CD  . GLU B 1 191 ? 171.175 19.046  27.050  1.000 79.240  ? 208 GLU BBB CD  1 
ATOM 3375  O OE1 . GLU B 1 191 ? 171.289 19.078  25.809  1.000 86.470  ? 208 GLU BBB OE1 1 
ATOM 3376  O OE2 . GLU B 1 191 ? 171.703 19.907  27.826  1.000 79.890  ? 208 GLU BBB OE2 1 
ATOM 3377  N N   . ASN B 1 192 ? 167.335 19.562  29.325  1.000 36.100  ? 209 ASN BBB N   1 
ATOM 3378  C CA  . ASN B 1 192 ? 167.557 20.539  30.423  1.000 37.330  ? 209 ASN BBB CA  1 
ATOM 3379  C C   . ASN B 1 192 ? 166.337 20.590  31.361  1.000 38.590  ? 209 ASN BBB C   1 
ATOM 3380  O O   . ASN B 1 192 ? 166.220 21.546  32.156  1.000 50.460  ? 209 ASN BBB O   1 
ATOM 3381  C CB  . ASN B 1 192 ? 167.873 21.917  29.849  1.000 39.180  ? 209 ASN BBB CB  1 
ATOM 3382  C CG  . ASN B 1 192 ? 168.495 22.861  30.860  1.000 39.300  ? 209 ASN BBB CG  1 
ATOM 3383  O OD1 . ASN B 1 192 ? 169.085 22.428  31.855  1.000 38.000  ? 209 ASN BBB OD1 1 
ATOM 3384  N ND2 . ASN B 1 192 ? 168.363 24.155  30.609  1.000 35.950  ? 209 ASN BBB ND2 1 
ATOM 3385  N N   . THR B 1 193 ? 165.454 19.603  31.302  1.000 35.840  ? 210 THR BBB N   1 
ATOM 3386  C CA  . THR B 1 193 ? 164.252 19.513  32.158  1.000 37.170  ? 210 THR BBB CA  1 
ATOM 3387  C C   . THR B 1 193 ? 164.184 18.101  32.757  1.000 38.210  ? 210 THR BBB C   1 
ATOM 3388  O O   . THR B 1 193 ? 164.724 17.159  32.146  1.000 38.050  ? 210 THR BBB O   1 
ATOM 3389  C CB  . THR B 1 193 ? 163.001 19.888  31.347  1.000 43.640  ? 210 THR BBB CB  1 
ATOM 3390  O OG1 . THR B 1 193 ? 162.976 21.289  31.044  1.000 42.250  ? 210 THR BBB OG1 1 
ATOM 3391  C CG2 . THR B 1 193 ? 161.724 19.540  32.074  1.000 47.910  ? 210 THR BBB CG2 1 
ATOM 3392  N N   . ARG B 1 194 ? 163.588 17.964  33.940  1.000 36.930  ? 211 ARG BBB N   1 
ATOM 3393  C CA  . ARG B 1 194 ? 163.230 16.658  34.551  1.000 34.800  ? 211 ARG BBB CA  1 
ATOM 3394  C C   . ARG B 1 194 ? 161.711 16.628  34.649  1.000 33.800  ? 211 ARG BBB C   1 
ATOM 3395  O O   . ARG B 1 194 ? 161.175 17.480  35.348  1.000 38.430  ? 211 ARG BBB O   1 
ATOM 3396  C CB  . ARG B 1 194 ? 163.852 16.503  35.937  1.000 33.110  ? 211 ARG BBB CB  1 
ATOM 3397  C CG  . ARG B 1 194 ? 165.347 16.758  35.971  1.000 34.040  ? 211 ARG BBB CG  1 
ATOM 3398  C CD  . ARG B 1 194 ? 166.104 15.711  35.197  1.000 36.410  ? 211 ARG BBB CD  1 
ATOM 3399  N NE  . ARG B 1 194 ? 167.525 15.978  35.297  1.000 37.920  ? 211 ARG BBB NE  1 
ATOM 3400  C CZ  . ARG B 1 194 ? 168.213 16.729  34.447  1.000 40.000  ? 211 ARG BBB CZ  1 
ATOM 3401  N NH1 . ARG B 1 194 ? 167.611 17.255  33.382  1.000 39.790  ? 211 ARG BBB NH1 1 
ATOM 3402  N NH2 . ARG B 1 194 ? 169.511 16.915  34.657  1.000 43.240  ? 211 ARG BBB NH2 1 
ATOM 3403  N N   . TYR B 1 195 ? 161.041 15.754  33.908  1.000 31.620  ? 212 TYR BBB N   1 
ATOM 3404  C CA  . TYR B 1 195 ? 159.560 15.708  33.857  1.000 30.090  ? 212 TYR BBB CA  1 
ATOM 3405  C C   . TYR B 1 195 ? 159.112 14.340  34.346  1.000 30.270  ? 212 TYR BBB C   1 
ATOM 3406  O O   . TYR B 1 195 ? 159.834 13.344  34.152  1.000 32.240  ? 212 TYR BBB O   1 
ATOM 3407  C CB  . TYR B 1 195 ? 159.031 16.058  32.463  1.000 30.600  ? 212 TYR BBB CB  1 
ATOM 3408  C CG  . TYR B 1 195 ? 159.281 15.036  31.377  1.000 31.160  ? 212 TYR BBB CG  1 
ATOM 3409  C CD1 . TYR B 1 195 ? 158.441 13.947  31.207  1.000 30.920  ? 212 TYR BBB CD1 1 
ATOM 3410  C CD2 . TYR B 1 195 ? 160.328 15.172  30.484  1.000 30.540  ? 212 TYR BBB CD2 1 
ATOM 3411  C CE1 . TYR B 1 195 ? 158.639 13.019  30.200  1.000 29.270  ? 212 TYR BBB CE1 1 
ATOM 3412  C CE2 . TYR B 1 195 ? 160.539 14.250  29.471  1.000 29.370  ? 212 TYR BBB CE2 1 
ATOM 3413  C CZ  . TYR B 1 195 ? 159.694 13.166  29.323  1.000 28.940  ? 212 TYR BBB CZ  1 
ATOM 3414  O OH  . TYR B 1 195 ? 159.923 12.254  28.326  1.000 27.360  ? 212 TYR BBB OH  1 
ATOM 3415  N N   . PHE B 1 196 ? 157.959 14.327  35.006  1.000 29.870  ? 213 PHE BBB N   1 
ATOM 3416  C CA  . PHE B 1 196 ? 157.313 13.121  35.565  1.000 27.660  ? 213 PHE BBB CA  1 
ATOM 3417  C C   . PHE B 1 196 ? 155.805 13.310  35.438  1.000 26.560  ? 213 PHE BBB C   1 
ATOM 3418  O O   . PHE B 1 196 ? 155.288 14.351  35.905  1.000 27.030  ? 213 PHE BBB O   1 
ATOM 3419  C CB  . PHE B 1 196 ? 157.660 12.967  37.047  1.000 28.170  ? 213 PHE BBB CB  1 
ATOM 3420  C CG  . PHE B 1 196 ? 159.104 13.196  37.413  1.000 27.270  ? 213 PHE BBB CG  1 
ATOM 3421  C CD1 . PHE B 1 196 ? 159.576 14.484  37.641  1.000 27.720  ? 213 PHE BBB CD1 1 
ATOM 3422  C CD2 . PHE B 1 196 ? 159.976 12.135  37.577  1.000 24.510  ? 213 PHE BBB CD2 1 
ATOM 3423  C CE1 . PHE B 1 196 ? 160.890 14.703  38.016  1.000 24.310  ? 213 PHE BBB CE1 1 
ATOM 3424  C CE2 . PHE B 1 196 ? 161.288 12.361  37.951  1.000 24.480  ? 213 PHE BBB CE2 1 
ATOM 3425  C CZ  . PHE B 1 196 ? 161.740 13.644  38.169  1.000 24.210  ? 213 PHE BBB CZ  1 
ATOM 3426  N N   . GLY B 1 197 ? 155.115 12.337  34.858  1.000 23.650  ? 214 GLY BBB N   1 
ATOM 3427  C CA  . GLY B 1 197 ? 153.646 12.362  34.846  1.000 23.400  ? 214 GLY BBB CA  1 
ATOM 3428  C C   . GLY B 1 197 ? 153.059 10.977  34.757  1.000 23.540  ? 214 GLY BBB C   1 
ATOM 3429  O O   . GLY B 1 197 ? 153.760 10.053  34.367  1.000 23.240  ? 214 GLY BBB O   1 
ATOM 3430  N N   . THR B 1 198 ? 151.773 10.866  35.057  1.000 24.760  ? 215 THR BBB N   1 
ATOM 3431  C CA  . THR B 1 198 ? 151.015 9.605   34.990  1.000 25.110  ? 215 THR BBB CA  1 
ATOM 3432  C C   . THR B 1 198 ? 149.605 9.890   34.506  1.000 25.480  ? 215 THR BBB C   1 
ATOM 3433  O O   . THR B 1 198 ? 148.970 10.758  35.080  1.000 24.070  ? 215 THR BBB O   1 
ATOM 3434  C CB  . THR B 1 198 ? 150.958 8.950   36.363  1.000 26.160  ? 215 THR BBB CB  1 
ATOM 3435  O OG1 . THR B 1 198 ? 152.307 8.597   36.661  1.000 28.030  ? 215 THR BBB OG1 1 
ATOM 3436  C CG2 . THR B 1 198 ? 150.077 7.732   36.399  1.000 27.630  ? 215 THR BBB CG2 1 
ATOM 3437  N N   . LEU B 1 199 ? 149.168 9.172   33.481  1.000 28.090  ? 216 LEU BBB N   1 
ATOM 3438  C CA  . LEU B 1 199 ? 147.737 9.109   33.107  1.000 29.260  ? 216 LEU BBB CA  1 
ATOM 3439  C C   . LEU B 1 199 ? 147.150 7.823   33.696  1.000 29.550  ? 216 LEU BBB C   1 
ATOM 3440  O O   . LEU B 1 199 ? 147.703 6.739   33.416  1.000 25.860  ? 216 LEU BBB O   1 
ATOM 3441  C CB  . LEU B 1 199 ? 147.543 9.131   31.592  1.000 28.460  ? 216 LEU BBB CB  1 
ATOM 3442  C CG  . LEU B 1 199 ? 146.073 9.006   31.204  1.000 27.200  ? 216 LEU BBB CG  1 
ATOM 3443  C CD1 . LEU B 1 199 ? 145.660 10.099  30.268  1.000 27.670  ? 216 LEU BBB CD1 1 
ATOM 3444  C CD2 . LEU B 1 199 ? 145.804 7.659   30.589  1.000 28.400  ? 216 LEU BBB CD2 1 
ATOM 3445  N N   . THR B 1 200 ? 146.080 7.971   34.475  1.000 28.450  ? 217 THR BBB N   1 
ATOM 3446  C CA  . THR B 1 200 ? 145.123 6.883   34.787  1.000 26.750  ? 217 THR BBB CA  1 
ATOM 3447  C C   . THR B 1 200 ? 143.780 7.165   34.102  1.000 27.780  ? 217 THR BBB C   1 
ATOM 3448  O O   . THR B 1 200 ? 143.133 8.159   34.457  1.000 26.910  ? 217 THR BBB O   1 
ATOM 3449  C CB  . THR B 1 200 ? 144.988 6.724   36.298  1.000 24.100  ? 217 THR BBB CB  1 
ATOM 3450  O OG1 . THR B 1 200 ? 146.307 6.645   36.843  1.000 21.070  ? 217 THR BBB OG1 1 
ATOM 3451  C CG2 . THR B 1 200 ? 144.214 5.480   36.641  1.000 24.530  ? 217 THR BBB CG2 1 
ATOM 3452  N N   . GLY B 1 201 ? 143.387 6.329   33.138  1.000 29.220  ? 218 GLY BBB N   1 
ATOM 3453  C CA  . GLY B 1 201 ? 142.148 6.499   32.346  1.000 29.930  ? 218 GLY BBB CA  1 
ATOM 3454  C C   . GLY B 1 201 ? 141.047 5.592   32.853  1.000 29.180  ? 218 GLY BBB C   1 
ATOM 3455  O O   . GLY B 1 201 ? 141.383 4.527   33.370  1.000 27.840  ? 218 GLY BBB O   1 
ATOM 3456  N N   . GLY B 1 202 ? 139.776 5.989   32.709  1.000 29.950  ? 219 GLY BBB N   1 
ATOM 3457  C CA  . GLY B 1 202 ? 138.608 5.206   33.172  1.000 28.590  ? 219 GLY BBB CA  1 
ATOM 3458  C C   . GLY B 1 202 ? 137.659 6.077   33.980  1.000 27.990  ? 219 GLY BBB C   1 
ATOM 3459  O O   . GLY B 1 202 ? 138.141 6.870   34.830  1.000 28.690  ? 219 GLY BBB O   1 
ATOM 3460  N N   . GLU B 1 203 ? 136.352 5.946   33.734  1.000 25.740  ? 220 GLU BBB N   1 
ATOM 3461  C CA  . GLU B 1 203 ? 135.317 6.832   34.315  1.000 25.000  ? 220 GLU BBB CA  1 
ATOM 3462  C C   . GLU B 1 203 ? 135.225 6.607   35.829  1.000 26.310  ? 220 GLU BBB C   1 
ATOM 3463  O O   . GLU B 1 203 ? 134.810 7.531   36.520  1.000 30.590  ? 220 GLU BBB O   1 
ATOM 3464  C CB  . GLU B 1 203 ? 133.983 6.683   33.576  1.000 24.850  ? 220 GLU BBB CB  1 
ATOM 3465  C CG  . GLU B 1 203 ? 133.351 5.312   33.608  1.000 27.110  ? 220 GLU BBB CG  1 
ATOM 3466  C CD  . GLU B 1 203 ? 133.633 4.451   32.402  1.000 28.440  ? 220 GLU BBB CD  1 
ATOM 3467  O OE1 . GLU B 1 203 ? 134.795 4.464   31.979  1.000 28.830  ? 220 GLU BBB OE1 1 
ATOM 3468  O OE2 . GLU B 1 203 ? 132.682 3.745   31.923  1.000 30.510  ? 220 GLU BBB OE2 1 
ATOM 3469  N N   . ASN B 1 204 ? 135.656 5.455   36.336  1.000 28.690  ? 221 ASN BBB N   1 
ATOM 3470  C CA  . ASN B 1 204 ? 135.464 5.046   37.750  1.000 30.370  ? 221 ASN BBB CA  1 
ATOM 3471  C C   . ASN B 1 204 ? 136.800 5.007   38.481  1.000 32.970  ? 221 ASN BBB C   1 
ATOM 3472  O O   . ASN B 1 204 ? 136.827 4.615   39.656  1.000 33.370  ? 221 ASN BBB O   1 
ATOM 3473  C CB  . ASN B 1 204 ? 134.719 3.713   37.804  1.000 30.310  ? 221 ASN BBB CB  1 
ATOM 3474  C CG  . ASN B 1 204 ? 133.323 3.875   37.262  1.000 32.510  ? 221 ASN BBB CG  1 
ATOM 3475  O OD1 . ASN B 1 204 ? 132.641 4.844   37.595  1.000 36.240  ? 221 ASN BBB OD1 1 
ATOM 3476  N ND2 . ASN B 1 204 ? 132.922 2.988   36.372  1.000 35.850  ? 221 ASN BBB ND2 1 
ATOM 3477  N N   . VAL B 1 205 ? 137.880 5.433   37.844  1.000 37.350  ? 222 VAL BBB N   1 
ATOM 3478  C CA  . VAL B 1 205 ? 139.213 5.405   38.509  1.000 37.790  ? 222 VAL BBB CA  1 
ATOM 3479  C C   . VAL B 1 205 ? 139.097 6.215   39.795  1.000 33.460  ? 222 VAL BBB C   1 
ATOM 3480  O O   . VAL B 1 205 ? 138.836 7.420   39.745  1.000 31.660  ? 222 VAL BBB O   1 
ATOM 3481  C CB  . VAL B 1 205 ? 140.334 5.964   37.613  1.000 41.920  ? 222 VAL BBB CB  1 
ATOM 3482  C CG1 . VAL B 1 205 ? 141.650 5.990   38.376  1.000 46.850  ? 222 VAL BBB CG1 1 
ATOM 3483  C CG2 . VAL B 1 205 ? 140.487 5.194   36.308  1.000 40.020  ? 222 VAL BBB CG2 1 
ATOM 3484  N N   . PRO B 1 206 ? 139.327 5.599   40.973  1.000 30.250  ? 223 PRO BBB N   1 
ATOM 3485  C CA  . PRO B 1 206 ? 139.356 6.334   42.236  1.000 28.590  ? 223 PRO BBB CA  1 
ATOM 3486  C C   . PRO B 1 206 ? 140.615 7.185   42.357  1.000 25.480  ? 223 PRO BBB C   1 
ATOM 3487  O O   . PRO B 1 206 ? 141.719 6.672   42.146  1.000 24.080  ? 223 PRO BBB O   1 
ATOM 3488  C CB  . PRO B 1 206 ? 139.360 5.229   43.289  1.000 28.320  ? 223 PRO BBB CB  1 
ATOM 3489  C CG  . PRO B 1 206 ? 140.133 4.147   42.608  1.000 31.480  ? 223 PRO BBB CG  1 
ATOM 3490  C CD  . PRO B 1 206 ? 139.648 4.181   41.165  1.000 32.340  ? 223 PRO BBB CD  1 
ATOM 3491  N N   . PRO B 1 207 ? 140.461 8.487   42.699  1.000 23.110  ? 224 PRO BBB N   1 
ATOM 3492  C CA  . PRO B 1 207 ? 141.591 9.346   43.018  1.000 23.000  ? 224 PRO BBB CA  1 
ATOM 3493  C C   . PRO B 1 207 ? 142.342 8.754   44.211  1.000 21.520  ? 224 PRO BBB C   1 
ATOM 3494  O O   . PRO B 1 207 ? 141.738 8.265   45.119  1.000 22.550  ? 224 PRO BBB O   1 
ATOM 3495  C CB  . PRO B 1 207 ? 140.978 10.696  43.415  1.000 23.510  ? 224 PRO BBB CB  1 
ATOM 3496  C CG  . PRO B 1 207 ? 139.593 10.673  42.807  1.000 23.370  ? 224 PRO BBB CG  1 
ATOM 3497  C CD  . PRO B 1 207 ? 139.190 9.213   42.817  1.000 22.880  ? 224 PRO BBB CD  1 
ATOM 3498  N N   . VAL B 1 208 ? 143.655 8.812   44.140  1.000 20.250  ? 225 VAL BBB N   1 
ATOM 3499  C CA  . VAL B 1 208 ? 144.585 8.389   45.210  1.000 19.790  ? 225 VAL BBB CA  1 
ATOM 3500  C C   . VAL B 1 208 ? 145.671 9.446   45.277  1.000 21.800  ? 225 VAL BBB C   1 
ATOM 3501  O O   . VAL B 1 208 ? 146.596 9.388   44.472  1.000 26.920  ? 225 VAL BBB O   1 
ATOM 3502  C CB  . VAL B 1 208 ? 145.170 7.016   44.898  1.000 18.060  ? 225 VAL BBB CB  1 
ATOM 3503  C CG1 . VAL B 1 208 ? 146.303 6.674   45.853  1.000 17.850  ? 225 VAL BBB CG1 1 
ATOM 3504  C CG2 . VAL B 1 208 ? 144.060 5.987   44.911  1.000 17.830  ? 225 VAL BBB CG2 1 
ATOM 3505  N N   . LEU B 1 209 ? 145.546 10.352  46.230  1.000 22.190  ? 226 LEU BBB N   1 
ATOM 3506  C CA  . LEU B 1 209 ? 146.452 11.495  46.395  1.000 21.750  ? 226 LEU BBB CA  1 
ATOM 3507  C C   . LEU B 1 209 ? 147.144 11.367  47.747  1.000 23.350  ? 226 LEU BBB C   1 
ATOM 3508  O O   . LEU B 1 209 ? 146.471 11.412  48.765  1.000 21.760  ? 226 LEU BBB O   1 
ATOM 3509  C CB  . LEU B 1 209 ? 145.580 12.735  46.249  1.000 21.390  ? 226 LEU BBB CB  1 
ATOM 3510  C CG  . LEU B 1 209 ? 144.807 12.774  44.934  1.000 20.810  ? 226 LEU BBB CG  1 
ATOM 3511  C CD1 . LEU B 1 209 ? 143.830 13.935  44.881  1.000 19.320  ? 226 LEU BBB CD1 1 
ATOM 3512  C CD2 . LEU B 1 209 ? 145.784 12.817  43.758  1.000 21.090  ? 226 LEU BBB CD2 1 
ATOM 3513  N N   . HIS B 1 210 ? 148.459 11.152  47.717  1.000 28.120  ? 227 HIS BBB N   1 
ATOM 3514  C CA  . HIS B 1 210 ? 149.347 11.154  48.902  1.000 33.080  ? 227 HIS BBB CA  1 
ATOM 3515  C C   . HIS B 1 210 ? 149.850 12.587  49.124  1.000 32.210  ? 227 HIS BBB C   1 
ATOM 3516  O O   . HIS B 1 210 ? 150.134 13.305  48.144  1.000 31.090  ? 227 HIS BBB O   1 
ATOM 3517  C CB  . HIS B 1 210 ? 150.488 10.146  48.712  1.000 39.180  ? 227 HIS BBB CB  1 
ATOM 3518  C CG  . HIS B 1 210 ? 150.032 8.779   48.303  1.000 45.520  ? 227 HIS BBB CG  1 
ATOM 3519  N ND1 . HIS B 1 210 ? 149.421 7.902   49.180  1.000 49.080  ? 227 HIS BBB ND1 1 
ATOM 3520  C CD2 . HIS B 1 210 ? 150.094 8.126   47.121  1.000 50.760  ? 227 HIS BBB CD2 1 
ATOM 3521  C CE1 . HIS B 1 210 ? 149.131 6.771   48.560  1.000 47.860  ? 227 HIS BBB CE1 1 
ATOM 3522  N NE2 . HIS B 1 210 ? 149.537 6.881   47.296  1.000 49.280  ? 227 HIS BBB NE2 1 
ATOM 3523  N N   . ILE B 1 211 ? 149.969 12.996  50.377  1.000 32.410  ? 228 ILE BBB N   1 
ATOM 3524  C CA  . ILE B 1 211 ? 150.612 14.286  50.770  1.000 32.200  ? 228 ILE BBB CA  1 
ATOM 3525  C C   . ILE B 1 211 ? 151.654 13.952  51.830  1.000 31.400  ? 228 ILE BBB C   1 
ATOM 3526  O O   . ILE B 1 211 ? 151.413 13.065  52.673  1.000 31.060  ? 228 ILE BBB O   1 
ATOM 3527  C CB  . ILE B 1 211 ? 149.535 15.270  51.271  1.000 33.330  ? 228 ILE BBB CB  1 
ATOM 3528  C CG1 . ILE B 1 211 ? 148.847 14.811  52.565  1.000 33.100  ? 228 ILE BBB CG1 1 
ATOM 3529  C CG2 . ILE B 1 211 ? 148.509 15.515  50.186  1.000 34.070  ? 228 ILE BBB CG2 1 
ATOM 3530  C CD1 . ILE B 1 211 ? 147.844 15.792  53.090  1.000 34.000  ? 228 ILE BBB CD1 1 
ATOM 3531  N N   . THR B 1 212 ? 152.800 14.616  51.781  1.000 30.250  ? 229 THR BBB N   1 
ATOM 3532  C CA  . THR B 1 212 ? 153.828 14.497  52.839  1.000 31.300  ? 229 THR BBB CA  1 
ATOM 3533  C C   . THR B 1 212 ? 154.900 15.558  52.597  1.000 34.010  ? 229 THR BBB C   1 
ATOM 3534  O O   . THR B 1 212 ? 155.240 15.829  51.415  1.000 42.390  ? 229 THR BBB O   1 
ATOM 3535  C CB  . THR B 1 212 ? 154.456 13.099  52.886  1.000 28.880  ? 229 THR BBB CB  1 
ATOM 3536  O OG1 . THR B 1 212 ? 155.269 13.018  54.059  1.000 28.140  ? 229 THR BBB OG1 1 
ATOM 3537  C CG2 . THR B 1 212 ? 155.321 12.812  51.682  1.000 29.410  ? 229 THR BBB CG2 1 
ATOM 3538  N N   . ASN B 1 213 ? 155.431 16.131  53.667  1.000 30.600  ? 230 ASN BBB N   1 
ATOM 3539  C CA  . ASN B 1 213 ? 156.551 17.085  53.542  1.000 30.730  ? 230 ASN BBB CA  1 
ATOM 3540  C C   . ASN B 1 213 ? 157.875 16.347  53.776  1.000 28.830  ? 230 ASN BBB C   1 
ATOM 3541  O O   . ASN B 1 213 ? 158.847 17.017  54.095  1.000 28.630  ? 230 ASN BBB O   1 
ATOM 3542  C CB  . ASN B 1 213 ? 156.329 18.291  54.465  1.000 33.990  ? 230 ASN BBB CB  1 
ATOM 3543  C CG  . ASN B 1 213 ? 156.228 17.914  55.926  1.000 30.460  ? 230 ASN BBB CG  1 
ATOM 3544  O OD1 . ASN B 1 213 ? 156.156 16.745  56.252  1.000 30.610  ? 230 ASN BBB OD1 1 
ATOM 3545  N ND2 . ASN B 1 213 ? 156.276 18.892  56.801  1.000 28.870  ? 230 ASN BBB ND2 1 
ATOM 3546  N N   . THR B 1 214 ? 157.914 15.020  53.625  1.000 29.450  ? 231 THR BBB N   1 
ATOM 3547  C CA  . THR B 1 214 ? 159.102 14.186  53.959  1.000 32.380  ? 231 THR BBB CA  1 
ATOM 3548  C C   . THR B 1 214 ? 159.750 13.598  52.709  1.000 33.440  ? 231 THR BBB C   1 
ATOM 3549  O O   . THR B 1 214 ? 160.800 12.985  52.831  1.000 32.870  ? 231 THR BBB O   1 
ATOM 3550  C CB  . THR B 1 214 ? 158.723 13.047  54.903  1.000 35.140  ? 231 THR BBB CB  1 
ATOM 3551  O OG1 . THR B 1 214 ? 157.796 12.219  54.208  1.000 35.320  ? 231 THR BBB OG1 1 
ATOM 3552  C CG2 . THR B 1 214 ? 158.111 13.536  56.197  1.000 38.300  ? 231 THR BBB CG2 1 
ATOM 3553  N N   . ALA B 1 215 ? 159.152 13.799  51.539  1.000 36.980  ? 232 ALA BBB N   1 
ATOM 3554  C CA  . ALA B 1 215 ? 159.564 13.149  50.282  1.000 37.610  ? 232 ALA BBB CA  1 
ATOM 3555  C C   . ALA B 1 215 ? 160.287 14.165  49.407  1.000 40.030  ? 232 ALA BBB C   1 
ATOM 3556  O O   . ALA B 1 215 ? 159.603 15.082  48.884  1.000 45.980  ? 232 ALA BBB O   1 
ATOM 3557  C CB  . ALA B 1 215 ? 158.328 12.626  49.610  1.000 37.310  ? 232 ALA BBB CB  1 
ATOM 3558  N N   . THR B 1 216 ? 161.600 14.002  49.244  1.000 40.980  ? 233 THR BBB N   1 
ATOM 3559  C CA  . THR B 1 216 ? 162.422 14.818  48.309  1.000 42.050  ? 233 THR BBB CA  1 
ATOM 3560  C C   . THR B 1 216 ? 162.683 13.997  47.053  1.000 37.270  ? 233 THR BBB C   1 
ATOM 3561  O O   . THR B 1 216 ? 162.859 12.812  47.203  1.000 33.970  ? 233 THR BBB O   1 
ATOM 3562  C CB  . THR B 1 216 ? 163.716 15.284  48.983  1.000 45.550  ? 233 THR BBB CB  1 
ATOM 3563  O OG1 . THR B 1 216 ? 163.374 15.884  50.232  1.000 51.690  ? 233 THR BBB OG1 1 
ATOM 3564  C CG2 . THR B 1 216 ? 164.485 16.283  48.155  1.000 45.730  ? 233 THR BBB CG2 1 
ATOM 3565  N N   . THR B 1 217 ? 162.672 14.619  45.873  1.000 40.550  ? 234 THR BBB N   1 
ATOM 3566  C CA  . THR B 1 217 ? 162.995 14.000  44.557  1.000 44.880  ? 234 THR BBB CA  1 
ATOM 3567  C C   . THR B 1 217 ? 164.257 14.657  44.005  1.000 46.210  ? 234 THR BBB C   1 
ATOM 3568  O O   . THR B 1 217 ? 164.271 15.901  43.935  1.000 50.000  ? 234 THR BBB O   1 
ATOM 3569  C CB  . THR B 1 217 ? 161.878 14.226  43.535  1.000 45.600  ? 234 THR BBB CB  1 
ATOM 3570  O OG1 . THR B 1 217 ? 160.660 13.714  44.073  1.000 47.300  ? 234 THR BBB OG1 1 
ATOM 3571  C CG2 . THR B 1 217 ? 162.164 13.557  42.214  1.000 45.700  ? 234 THR BBB CG2 1 
ATOM 3572  N N   . VAL B 1 218 ? 165.269 13.880  43.625  1.000 43.450  ? 235 VAL BBB N   1 
ATOM 3573  C CA  . VAL B 1 218 ? 166.576 14.458  43.187  1.000 41.900  ? 235 VAL BBB CA  1 
ATOM 3574  C C   . VAL B 1 218 ? 166.486 14.755  41.689  1.000 38.550  ? 235 VAL BBB C   1 
ATOM 3575  O O   . VAL B 1 218 ? 165.884 13.953  40.985  1.000 39.800  ? 235 VAL BBB O   1 
ATOM 3576  C CB  . VAL B 1 218 ? 167.730 13.501  43.520  1.000 43.090  ? 235 VAL BBB CB  1 
ATOM 3577  C CG1 . VAL B 1 218 ? 168.992 13.848  42.761  1.000 42.720  ? 235 VAL BBB CG1 1 
ATOM 3578  C CG2 . VAL B 1 218 ? 167.989 13.447  45.016  1.000 43.460  ? 235 VAL BBB CG2 1 
ATOM 3579  N N   . LEU B 1 219 ? 167.051 15.871  41.225  1.000 35.520  ? 236 LEU BBB N   1 
ATOM 3580  C CA  . LEU B 1 219 ? 166.911 16.341  39.824  1.000 32.630  ? 236 LEU BBB CA  1 
ATOM 3581  C C   . LEU B 1 219 ? 168.209 16.133  39.037  1.000 32.900  ? 236 LEU BBB C   1 
ATOM 3582  O O   . LEU B 1 219 ? 168.228 16.482  37.854  1.000 34.440  ? 236 LEU BBB O   1 
ATOM 3583  C CB  . LEU B 1 219 ? 166.490 17.808  39.855  1.000 31.080  ? 236 LEU BBB CB  1 
ATOM 3584  C CG  . LEU B 1 219 ? 165.143 18.064  40.549  1.000 32.680  ? 236 LEU BBB CG  1 
ATOM 3585  C CD1 . LEU B 1 219 ? 164.885 19.544  40.729  1.000 35.030  ? 236 LEU BBB CD1 1 
ATOM 3586  C CD2 . LEU B 1 219 ? 164.005 17.435  39.794  1.000 31.420  ? 236 LEU BBB CD2 1 
ATOM 3587  N N   . LEU B 1 220 ? 169.228 15.542  39.654  1.000 37.100  ? 237 LEU BBB N   1 
ATOM 3588  C CA  . LEU B 1 220 ? 170.547 15.269  39.021  1.000 40.010  ? 237 LEU BBB CA  1 
ATOM 3589  C C   . LEU B 1 220 ? 170.410 14.099  38.043  1.000 39.970  ? 237 LEU BBB C   1 
ATOM 3590  O O   . LEU B 1 220 ? 169.639 13.189  38.319  1.000 37.700  ? 237 LEU BBB O   1 
ATOM 3591  C CB  . LEU B 1 220 ? 171.581 14.936  40.093  1.000 41.270  ? 237 LEU BBB CB  1 
ATOM 3592  C CG  . LEU B 1 220 ? 171.752 15.956  41.210  1.000 45.700  ? 237 LEU BBB CG  1 
ATOM 3593  C CD1 . LEU B 1 220 ? 172.851 15.473  42.148  1.000 53.070  ? 237 LEU BBB CD1 1 
ATOM 3594  C CD2 . LEU B 1 220 ? 172.058 17.350  40.659  1.000 46.830  ? 237 LEU BBB CD2 1 
ATOM 3595  N N   . ASP B 1 221 ? 171.163 14.143  36.945  1.000 41.360  ? 238 ASP BBB N   1 
ATOM 3596  C CA  . ASP B 1 221 ? 171.187 13.106  35.881  1.000 44.220  ? 238 ASP BBB CA  1 
ATOM 3597  C C   . ASP B 1 221 ? 172.294 12.099  36.201  1.000 47.490  ? 238 ASP BBB C   1 
ATOM 3598  O O   . ASP B 1 221 ? 172.911 12.240  37.269  1.000 49.940  ? 238 ASP BBB O   1 
ATOM 3599  C CB  . ASP B 1 221 ? 171.345 13.748  34.502  1.000 45.880  ? 238 ASP BBB CB  1 
ATOM 3600  C CG  . ASP B 1 221 ? 172.678 14.431  34.254  1.000 49.570  ? 238 ASP BBB CG  1 
ATOM 3601  O OD1 . ASP B 1 221 ? 173.542 14.395  35.147  1.000 51.340  ? 238 ASP BBB OD1 1 
ATOM 3602  O OD2 . ASP B 1 221 ? 172.842 15.026  33.168  1.000 59.650  ? 238 ASP BBB OD2 1 
ATOM 3603  N N   . GLU B 1 222 ? 172.542 11.147  35.293  1.000 54.300  ? 239 GLU BBB N   1 
ATOM 3604  C CA  . GLU B 1 222 ? 173.564 10.069  35.464  1.000 56.250  ? 239 GLU BBB CA  1 
ATOM 3605  C C   . GLU B 1 222 ? 174.940 10.693  35.751  1.000 52.030  ? 239 GLU BBB C   1 
ATOM 3606  O O   . GLU B 1 222 ? 175.730 9.995   36.392  1.000 46.390  ? 239 GLU BBB O   1 
ATOM 3607  C CB  . GLU B 1 222 ? 173.595 9.069   34.296  1.000 61.850  ? 239 GLU BBB CB  1 
ATOM 3608  C CG  . GLU B 1 222 ? 173.499 9.661   32.890  1.000 67.330  ? 239 GLU BBB CG  1 
ATOM 3609  C CD  . GLU B 1 222 ? 172.087 9.770   32.329  1.000 67.950  ? 239 GLU BBB CD  1 
ATOM 3610  O OE1 . GLU B 1 222 ? 171.762 8.977   31.421  1.000 69.030  ? 239 GLU BBB OE1 1 
ATOM 3611  O OE2 . GLU B 1 222 ? 171.320 10.665  32.775  1.000 67.110  ? 239 GLU BBB OE2 1 
ATOM 3612  N N   . PHE B 1 223 ? 175.186 11.953  35.376  1.000 56.500  ? 240 PHE BBB N   1 
ATOM 3613  C CA  . PHE B 1 223 ? 176.482 12.658  35.556  1.000 66.990  ? 240 PHE BBB CA  1 
ATOM 3614  C C   . PHE B 1 223 ? 176.433 13.642  36.738  1.000 62.220  ? 240 PHE BBB C   1 
ATOM 3615  O O   . PHE B 1 223 ? 177.327 14.493  36.817  1.000 63.580  ? 240 PHE BBB O   1 
ATOM 3616  C CB  . PHE B 1 223 ? 176.842 13.477  34.313  1.000 81.880  ? 240 PHE BBB CB  1 
ATOM 3617  C CG  . PHE B 1 223 ? 176.862 12.754  32.991  1.000 82.480  ? 240 PHE BBB CG  1 
ATOM 3618  C CD1 . PHE B 1 223 ? 175.695 12.409  32.328  1.000 84.190  ? 240 PHE BBB CD1 1 
ATOM 3619  C CD2 . PHE B 1 223 ? 178.065 12.501  32.369  1.000 80.220  ? 240 PHE BBB CD2 1 
ATOM 3620  C CE1 . PHE B 1 223 ? 175.730 11.797  31.087  1.000 80.820  ? 240 PHE BBB CE1 1 
ATOM 3621  C CE2 . PHE B 1 223 ? 178.105 11.893  31.122  1.000 83.740  ? 240 PHE BBB CE2 1 
ATOM 3622  C CZ  . PHE B 1 223 ? 176.936 11.541  30.486  1.000 82.920  ? 240 PHE BBB CZ  1 
ATOM 3623  N N   . GLY B 1 224 ? 175.413 13.588  37.592  1.000 57.050  ? 241 GLY BBB N   1 
ATOM 3624  C CA  . GLY B 1 224 ? 175.334 14.441  38.793  1.000 54.500  ? 241 GLY BBB CA  1 
ATOM 3625  C C   . GLY B 1 224 ? 175.103 15.918  38.486  1.000 49.040  ? 241 GLY BBB C   1 
ATOM 3626  O O   . GLY B 1 224 ? 175.391 16.744  39.371  1.000 50.750  ? 241 GLY BBB O   1 
ATOM 3627  N N   . VAL B 1 225 ? 174.566 16.230  37.305  1.000 42.320  ? 242 VAL BBB N   1 
ATOM 3628  C CA  . VAL B 1 225 ? 174.154 17.600  36.871  1.000 39.220  ? 242 VAL BBB CA  1 
ATOM 3629  C C   . VAL B 1 225 ? 172.621 17.708  36.847  1.000 39.530  ? 242 VAL BBB C   1 
ATOM 3630  O O   . VAL B 1 225 ? 171.974 16.905  36.156  1.000 41.030  ? 242 VAL BBB O   1 
ATOM 3631  C CB  . VAL B 1 225 ? 174.701 17.934  35.481  1.000 36.710  ? 242 VAL BBB CB  1 
ATOM 3632  C CG1 . VAL B 1 225 ? 174.435 19.383  35.123  1.000 34.690  ? 242 VAL BBB CG1 1 
ATOM 3633  C CG2 . VAL B 1 225 ? 176.167 17.573  35.362  1.000 41.130  ? 242 VAL BBB CG2 1 
ATOM 3634  N N   . GLY B 1 226 ? 172.068 18.691  37.554  1.000 41.250  ? 243 GLY BBB N   1 
ATOM 3635  C CA  . GLY B 1 226 ? 170.643 19.039  37.505  1.000 36.670  ? 243 GLY BBB CA  1 
ATOM 3636  C C   . GLY B 1 226 ? 170.351 19.942  36.315  1.000 34.510  ? 243 GLY BBB C   1 
ATOM 3637  O O   . GLY B 1 226 ? 171.245 20.282  35.567  1.000 32.360  ? 243 GLY BBB O   1 
ATOM 3638  N N   . PRO B 1 227 ? 169.081 20.319  36.079  1.000 36.320  ? 244 PRO BBB N   1 
ATOM 3639  C CA  . PRO B 1 227 ? 168.762 21.372  35.114  1.000 38.470  ? 244 PRO BBB CA  1 
ATOM 3640  C C   . PRO B 1 227 ? 169.555 22.652  35.405  1.000 39.390  ? 244 PRO BBB C   1 
ATOM 3641  O O   . PRO B 1 227 ? 169.787 22.948  36.570  1.000 38.690  ? 244 PRO BBB O   1 
ATOM 3642  C CB  . PRO B 1 227 ? 167.252 21.596  35.303  1.000 37.890  ? 244 PRO BBB CB  1 
ATOM 3643  C CG  . PRO B 1 227 ? 166.754 20.261  35.839  1.000 37.400  ? 244 PRO BBB CG  1 
ATOM 3644  C CD  . PRO B 1 227 ? 167.881 19.739  36.705  1.000 36.210  ? 244 PRO BBB CD  1 
ATOM 3645  N N   . LEU B 1 228 ? 169.992 23.332  34.342  1.000 40.810  ? 245 LEU BBB N   1 
ATOM 3646  C CA  . LEU B 1 228 ? 170.775 24.605  34.401  1.000 39.380  ? 245 LEU BBB CA  1 
ATOM 3647  C C   . LEU B 1 228 ? 169.884 25.745  33.906  1.000 40.910  ? 245 LEU BBB C   1 
ATOM 3648  O O   . LEU B 1 228 ? 169.372 25.656  32.775  1.000 41.050  ? 245 LEU BBB O   1 
ATOM 3649  C CB  . LEU B 1 228 ? 172.057 24.493  33.569  1.000 36.790  ? 245 LEU BBB CB  1 
ATOM 3650  C CG  . LEU B 1 228 ? 173.040 23.424  34.065  1.000 37.900  ? 245 LEU BBB CG  1 
ATOM 3651  C CD1 . LEU B 1 228 ? 174.256 23.296  33.177  1.000 38.070  ? 245 LEU BBB CD1 1 
ATOM 3652  C CD2 . LEU B 1 228 ? 173.426 23.678  35.522  1.000 40.670  ? 245 LEU BBB CD2 1 
ATOM 3653  N N   . CYS B 1 229 ? 169.691 26.761  34.742  1.000 41.060  ? 246 CYS BBB N   1 
ATOM 3654  C CA  . CYS B 1 229 ? 168.689 27.833  34.537  1.000 43.840  ? 246 CYS BBB CA  1 
ATOM 3655  C C   . CYS B 1 229 ? 169.221 28.915  33.598  1.000 47.630  ? 246 CYS BBB C   1 
ATOM 3656  O O   . CYS B 1 229 ? 169.734 29.928  34.103  1.000 53.000  ? 246 CYS BBB O   1 
ATOM 3657  C CB  . CYS B 1 229 ? 168.291 28.414  35.878  1.000 46.580  ? 246 CYS BBB CB  1 
ATOM 3658  S SG  . CYS B 1 229 ? 167.420 27.190  36.891  1.000 55.930  ? 246 CYS BBB SG  1 
ATOM 3659  N N   . LYS B 1 230 ? 169.068 28.704  32.285  1.000 46.860  ? 247 LYS BBB N   1 
ATOM 3660  C CA  . LYS B 1 230 ? 169.320 29.708  31.218  1.000 43.460  ? 247 LYS BBB CA  1 
ATOM 3661  C C   . LYS B 1 230 ? 168.580 31.006  31.550  1.000 41.640  ? 247 LYS BBB C   1 
ATOM 3662  O O   . LYS B 1 230 ? 167.403 30.944  31.880  1.000 45.110  ? 247 LYS BBB O   1 
ATOM 3663  C CB  . LYS B 1 230 ? 168.868 29.153  29.864  1.000 44.400  ? 247 LYS BBB CB  1 
ATOM 3664  C CG  . LYS B 1 230 ? 169.786 28.070  29.320  1.000 53.870  ? 247 LYS BBB CG  1 
ATOM 3665  C CD  . LYS B 1 230 ? 169.322 27.423  28.032  1.000 58.300  ? 247 LYS BBB CD  1 
ATOM 3666  C CE  . LYS B 1 230 ? 170.222 26.272  27.625  1.000 63.150  ? 247 LYS BBB CE  1 
ATOM 3667  N NZ  . LYS B 1 230 ? 169.940 25.845  26.236  1.000 71.680  ? 247 LYS BBB NZ  1 
ATOM 3668  N N   . GLY B 1 231 ? 169.258 32.144  31.458  1.000 44.840  ? 248 GLY BBB N   1 
ATOM 3669  C CA  . GLY B 1 231 ? 168.657 33.479  31.651  1.000 48.430  ? 248 GLY BBB CA  1 
ATOM 3670  C C   . GLY B 1 231 ? 168.338 33.737  33.112  1.000 53.750  ? 248 GLY BBB C   1 
ATOM 3671  O O   . GLY B 1 231 ? 167.539 34.628  33.377  1.000 58.790  ? 248 GLY BBB O   1 
ATOM 3672  N N   . ASP B 1 232 ? 168.938 32.979  34.029  1.000 52.740  ? 249 ASP BBB N   1 
ATOM 3673  C CA  . ASP B 1 232 ? 168.666 33.055  35.487  1.000 52.190  ? 249 ASP BBB CA  1 
ATOM 3674  C C   . ASP B 1 232 ? 167.167 32.848  35.728  1.000 52.780  ? 249 ASP BBB C   1 
ATOM 3675  O O   . ASP B 1 232 ? 166.586 33.520  36.606  1.000 52.300  ? 249 ASP BBB O   1 
ATOM 3676  C CB  . ASP B 1 232 ? 169.239 34.357  36.045  1.000 52.880  ? 249 ASP BBB CB  1 
ATOM 3677  C CG  . ASP B 1 232 ? 170.760 34.329  36.090  1.000 58.470  ? 249 ASP BBB CG  1 
ATOM 3678  O OD1 . ASP B 1 232 ? 171.348 33.231  35.929  1.000 61.130  ? 249 ASP BBB OD1 1 
ATOM 3679  O OD2 . ASP B 1 232 ? 171.352 35.394  36.300  1.000 63.470  ? 249 ASP BBB OD2 1 
ATOM 3680  N N   . ASN B 1 233 ? 166.574 31.900  34.996  1.000 53.980  ? 250 ASN BBB N   1 
ATOM 3681  C CA  . ASN B 1 233 ? 165.136 31.528  35.083  1.000 49.540  ? 250 ASN BBB CA  1 
ATOM 3682  C C   . ASN B 1 233 ? 164.967 30.028  35.375  1.000 50.580  ? 250 ASN BBB C   1 
ATOM 3683  O O   . ASN B 1 233 ? 165.653 29.195  34.743  1.000 48.280  ? 250 ASN BBB O   1 
ATOM 3684  C CB  . ASN B 1 233 ? 164.398 31.882  33.801  1.000 43.000  ? 250 ASN BBB CB  1 
ATOM 3685  C CG  . ASN B 1 233 ? 164.210 33.366  33.626  1.000 39.660  ? 250 ASN BBB CG  1 
ATOM 3686  O OD1 . ASN B 1 233 ? 164.155 34.111  34.595  1.000 41.170  ? 250 ASN BBB OD1 1 
ATOM 3687  N ND2 . ASN B 1 233 ? 164.079 33.795  32.391  1.000 39.540  ? 250 ASN BBB ND2 1 
ATOM 3688  N N   . LEU B 1 234 ? 164.045 29.707  36.281  1.000 47.640  ? 251 LEU BBB N   1 
ATOM 3689  C CA  . LEU B 1 234 ? 163.618 28.326  36.600  1.000 45.790  ? 251 LEU BBB CA  1 
ATOM 3690  C C   . LEU B 1 234 ? 162.196 28.156  36.069  1.000 47.500  ? 251 LEU BBB C   1 
ATOM 3691  O O   . LEU B 1 234 ? 161.372 29.075  36.301  1.000 40.830  ? 251 LEU BBB O   1 
ATOM 3692  C CB  . LEU B 1 234 ? 163.651 28.151  38.113  1.000 46.500  ? 251 LEU BBB CB  1 
ATOM 3693  C CG  . LEU B 1 234 ? 163.260 26.766  38.619  1.000 49.620  ? 251 LEU BBB CG  1 
ATOM 3694  C CD1 . LEU B 1 234 ? 164.271 25.727  38.157  1.000 50.040  ? 251 LEU BBB CD1 1 
ATOM 3695  C CD2 . LEU B 1 234 ? 163.146 26.760  40.131  1.000 48.170  ? 251 LEU BBB CD2 1 
ATOM 3696  N N   . TYR B 1 235 ? 161.930 27.034  35.388  1.000 49.020  ? 252 TYR BBB N   1 
ATOM 3697  C CA  . TYR B 1 235 ? 160.632 26.759  34.718  1.000 50.060  ? 252 TYR BBB CA  1 
ATOM 3698  C C   . TYR B 1 235 ? 159.916 25.578  35.396  1.000 47.420  ? 252 TYR BBB C   1 
ATOM 3699  O O   . TYR B 1 235 ? 160.289 24.384  35.217  1.000 47.170  ? 252 TYR BBB O   1 
ATOM 3700  C CB  . TYR B 1 235 ? 160.851 26.499  33.232  1.000 52.630  ? 252 TYR BBB CB  1 
ATOM 3701  C CG  . TYR B 1 235 ? 161.052 27.721  32.373  1.000 50.230  ? 252 TYR BBB CG  1 
ATOM 3702  C CD1 . TYR B 1 235 ? 162.281 28.346  32.307  1.000 48.890  ? 252 TYR BBB CD1 1 
ATOM 3703  C CD2 . TYR B 1 235 ? 160.029 28.219  31.585  1.000 49.050  ? 252 TYR BBB CD2 1 
ATOM 3704  C CE1 . TYR B 1 235 ? 162.480 29.451  31.494  1.000 50.190  ? 252 TYR BBB CE1 1 
ATOM 3705  C CE2 . TYR B 1 235 ? 160.213 29.308  30.754  1.000 48.490  ? 252 TYR BBB CE2 1 
ATOM 3706  C CZ  . TYR B 1 235 ? 161.448 29.935  30.716  1.000 50.620  ? 252 TYR BBB CZ  1 
ATOM 3707  O OH  . TYR B 1 235 ? 161.702 31.034  29.941  1.000 57.470  ? 252 TYR BBB OH  1 
ATOM 3708  N N   . LEU B 1 236 ? 158.876 25.905  36.152  1.000 41.430  ? 253 LEU BBB N   1 
ATOM 3709  C CA  . LEU B 1 236 ? 157.968 24.918  36.766  1.000 38.790  ? 253 LEU BBB CA  1 
ATOM 3710  C C   . LEU B 1 236 ? 156.754 24.769  35.854  1.000 36.690  ? 253 LEU BBB C   1 
ATOM 3711  O O   . LEU B 1 236 ? 156.103 25.788  35.537  1.000 30.550  ? 253 LEU BBB O   1 
ATOM 3712  C CB  . LEU B 1 236 ? 157.581 25.398  38.168  1.000 37.680  ? 253 LEU BBB CB  1 
ATOM 3713  C CG  . LEU B 1 236 ? 158.755 25.818  39.038  1.000 36.320  ? 253 LEU BBB CG  1 
ATOM 3714  C CD1 . LEU B 1 236 ? 158.256 26.143  40.436  1.000 35.190  ? 253 LEU BBB CD1 1 
ATOM 3715  C CD2 . LEU B 1 236 ? 159.838 24.739  39.051  1.000 36.070  ? 253 LEU BBB CD2 1 
ATOM 3716  N N   . SER B 1 237 ? 156.517 23.534  35.415  1.000 36.970  ? 254 SER BBB N   1 
ATOM 3717  C CA  . SER B 1 237 ? 155.318 23.121  34.649  1.000 38.150  ? 254 SER BBB CA  1 
ATOM 3718  C C   . SER B 1 237 ? 154.573 22.044  35.451  1.000 37.560  ? 254 SER BBB C   1 
ATOM 3719  O O   . SER B 1 237 ? 155.252 21.333  36.249  1.000 36.470  ? 254 SER BBB O   1 
ATOM 3720  C CB  . SER B 1 237 ? 155.734 22.662  33.289  1.000 38.280  ? 254 SER BBB CB  1 
ATOM 3721  O OG  . SER B 1 237 ? 156.835 23.443  32.814  1.000 41.000  ? 254 SER BBB OG  1 
ATOM 3722  N N   . ALA B 1 238 ? 153.243 21.971  35.306  1.000 35.730  ? 255 ALA BBB N   1 
ATOM 3723  C CA  . ALA B 1 238 ? 152.391 21.044  36.083  1.000 34.830  ? 255 ALA BBB CA  1 
ATOM 3724  C C   . ALA B 1 238 ? 151.018 20.887  35.435  1.000 33.980  ? 255 ALA BBB C   1 
ATOM 3725  O O   . ALA B 1 238 ? 150.544 21.864  34.838  1.000 32.940  ? 255 ALA BBB O   1 
ATOM 3726  C CB  . ALA B 1 238 ? 152.229 21.569  37.480  1.000 35.740  ? 255 ALA BBB CB  1 
ATOM 3727  N N   . VAL B 1 239 ? 150.414 19.703  35.576  1.000 32.720  ? 256 VAL BBB N   1 
ATOM 3728  C CA  . VAL B 1 239 ? 148.961 19.460  35.345  1.000 31.630  ? 256 VAL BBB CA  1 
ATOM 3729  C C   . VAL B 1 239 ? 148.490 18.517  36.439  1.000 30.030  ? 256 VAL BBB C   1 
ATOM 3730  O O   . VAL B 1 239 ? 149.210 17.558  36.691  1.000 28.020  ? 256 VAL BBB O   1 
ATOM 3731  C CB  . VAL B 1 239 ? 148.692 18.795  33.990  1.000 33.500  ? 256 VAL BBB CB  1 
ATOM 3732  C CG1 . VAL B 1 239 ? 147.204 18.579  33.775  1.000 33.000  ? 256 VAL BBB CG1 1 
ATOM 3733  C CG2 . VAL B 1 239 ? 149.292 19.585  32.848  1.000 35.780  ? 256 VAL BBB CG2 1 
ATOM 3734  N N   . ASP B 1 240 ? 147.316 18.751  37.011  1.000 30.820  ? 257 ASP BBB N   1 
ATOM 3735  C CA  . ASP B 1 240 ? 146.737 17.842  38.031  1.000 31.200  ? 257 ASP BBB CA  1 
ATOM 3736  C C   . ASP B 1 240 ? 145.224 17.759  37.837  1.000 32.570  ? 257 ASP BBB C   1 
ATOM 3737  O O   . ASP B 1 240 ? 144.471 18.183  38.750  1.000 33.320  ? 257 ASP BBB O   1 
ATOM 3738  C CB  . ASP B 1 240 ? 147.114 18.320  39.425  1.000 32.300  ? 257 ASP BBB CB  1 
ATOM 3739  C CG  . ASP B 1 240 ? 148.570 18.092  39.745  1.000 30.750  ? 257 ASP BBB CG  1 
ATOM 3740  O OD1 . ASP B 1 240 ? 148.905 16.916  39.990  1.000 28.610  ? 257 ASP BBB OD1 1 
ATOM 3741  O OD2 . ASP B 1 240 ? 149.345 19.093  39.729  1.000 27.970  ? 257 ASP BBB OD2 1 
ATOM 3742  N N   . VAL B 1 241 ? 144.800 17.254  36.679  1.000 32.400  ? 258 VAL BBB N   1 
ATOM 3743  C CA  . VAL B 1 241 ? 143.379 16.900  36.415  1.000 31.060  ? 258 VAL BBB CA  1 
ATOM 3744  C C   . VAL B 1 241 ? 143.076 15.719  37.331  1.000 32.830  ? 258 VAL BBB C   1 
ATOM 3745  O O   . VAL B 1 241 ? 143.695 14.668  37.123  1.000 39.430  ? 258 VAL BBB O   1 
ATOM 3746  C CB  . VAL B 1 241 ? 143.149 16.566  34.935  1.000 29.860  ? 258 VAL BBB CB  1 
ATOM 3747  C CG1 . VAL B 1 241 ? 141.730 16.091  34.674  1.000 30.820  ? 258 VAL BBB CG1 1 
ATOM 3748  C CG2 . VAL B 1 241 ? 143.482 17.749  34.042  1.000 30.800  ? 258 VAL BBB CG2 1 
ATOM 3749  N N   . CYS B 1 242 ? 142.248 15.914  38.356  1.000 31.060  ? 259 CYS BBB N   1 
ATOM 3750  C CA  . CYS B 1 242 ? 142.090 14.949  39.470  1.000 29.900  ? 259 CYS BBB CA  1 
ATOM 3751  C C   . CYS B 1 242 ? 141.051 13.902  39.099  1.000 29.420  ? 259 CYS BBB C   1 
ATOM 3752  O O   . CYS B 1 242 ? 141.091 12.792  39.700  1.000 30.700  ? 259 CYS BBB O   1 
ATOM 3753  C CB  . CYS B 1 242 ? 141.619 15.650  40.732  1.000 30.120  ? 259 CYS BBB CB  1 
ATOM 3754  S SG  . CYS B 1 242 ? 142.964 16.570  41.491  1.000 29.900  ? 259 CYS BBB SG  1 
ATOM 3755  N N   . GLY B 1 243 ? 140.170 14.259  38.166  1.000 26.920  ? 260 GLY BBB N   1 
ATOM 3756  C CA  . GLY B 1 243 ? 138.971 13.472  37.815  1.000 26.570  ? 260 GLY BBB CA  1 
ATOM 3757  C C   . GLY B 1 243 ? 137.876 14.377  37.297  1.000 24.720  ? 260 GLY BBB C   1 
ATOM 3758  O O   . GLY B 1 243 ? 138.202 15.510  36.887  1.000 26.560  ? 260 GLY BBB O   1 
ATOM 3759  N N   . MET B 1 244 ? 136.635 13.917  37.324  1.000 22.920  ? 261 MET BBB N   1 
ATOM 3760  C CA  . MET B 1 244 ? 135.459 14.753  36.977  1.000 24.110  ? 261 MET BBB CA  1 
ATOM 3761  C C   . MET B 1 244 ? 134.543 14.883  38.191  1.000 24.690  ? 261 MET BBB C   1 
ATOM 3762  O O   . MET B 1 244 ? 134.389 13.889  38.945  1.000 25.720  ? 261 MET BBB O   1 
ATOM 3763  C CB  . MET B 1 244 ? 134.646 14.135  35.841  1.000 24.590  ? 261 MET BBB CB  1 
ATOM 3764  C CG  . MET B 1 244 ? 135.432 14.027  34.576  1.000 24.710  ? 261 MET BBB CG  1 
ATOM 3765  S SD  . MET B 1 244 ? 134.402 13.312  33.304  1.000 22.650  ? 261 MET BBB SD  1 
ATOM 3766  C CE  . MET B 1 244 ? 135.592 13.298  31.963  1.000 22.660  ? 261 MET BBB CE  1 
ATOM 3767  N N   . PHE B 1 245 ? 133.968 16.069  38.355  1.000 24.140  ? 262 PHE BBB N   1 
ATOM 3768  C CA  . PHE B 1 245 ? 132.824 16.316  39.254  1.000 25.570  ? 262 PHE BBB CA  1 
ATOM 3769  C C   . PHE B 1 245 ? 131.560 15.945  38.487  1.000 25.330  ? 262 PHE BBB C   1 
ATOM 3770  O O   . PHE B 1 245 ? 131.421 16.453  37.387  1.000 23.220  ? 262 PHE BBB O   1 
ATOM 3771  C CB  . PHE B 1 245 ? 132.767 17.774  39.698  1.000 26.180  ? 262 PHE BBB CB  1 
ATOM 3772  C CG  . PHE B 1 245 ? 131.515 18.098  40.489  1.000 27.230  ? 262 PHE BBB CG  1 
ATOM 3773  C CD1 . PHE B 1 245 ? 131.219 17.421  41.665  1.000 28.240  ? 262 PHE BBB CD1 1 
ATOM 3774  C CD2 . PHE B 1 245 ? 130.643 19.058  40.042  1.000 28.880  ? 262 PHE BBB CD2 1 
ATOM 3775  C CE1 . PHE B 1 245 ? 130.079 17.712  42.395  1.000 28.860  ? 262 PHE BBB CE1 1 
ATOM 3776  C CE2 . PHE B 1 245 ? 129.488 19.345  40.765  1.000 30.050  ? 262 PHE BBB CE2 1 
ATOM 3777  C CZ  . PHE B 1 245 ? 129.218 18.679  41.940  1.000 30.650  ? 262 PHE BBB CZ  1 
ATOM 3778  N N   . THR B 1 246 ? 130.726 15.059  39.031  1.000 26.450  ? 263 THR BBB N   1 
ATOM 3779  C CA  . THR B 1 246 ? 129.413 14.712  38.443  1.000 27.120  ? 263 THR BBB CA  1 
ATOM 3780  C C   . THR B 1 246 ? 128.339 15.531  39.149  1.000 27.890  ? 263 THR BBB C   1 
ATOM 3781  O O   . THR B 1 246 ? 128.076 15.308  40.364  1.000 30.980  ? 263 THR BBB O   1 
ATOM 3782  C CB  . THR B 1 246 ? 129.144 13.207  38.482  1.000 28.470  ? 263 THR BBB CB  1 
ATOM 3783  O OG1 . THR B 1 246 ? 130.253 12.520  37.884  1.000 31.290  ? 263 THR BBB OG1 1 
ATOM 3784  C CG2 . THR B 1 246 ? 127.846 12.843  37.797  1.000 27.190  ? 263 THR BBB CG2 1 
ATOM 3785  N N   . ASN B 1 247 ? 127.766 16.477  38.403  1.000 30.080  ? 264 ASN BBB N   1 
ATOM 3786  C CA  . ASN B 1 247 ? 126.614 17.320  38.813  1.000 29.270  ? 264 ASN BBB CA  1 
ATOM 3787  C C   . ASN B 1 247 ? 125.369 16.442  38.992  1.000 26.440  ? 264 ASN BBB C   1 
ATOM 3788  O O   . ASN B 1 247 ? 125.362 15.315  38.492  1.000 25.280  ? 264 ASN BBB O   1 
ATOM 3789  C CB  . ASN B 1 247 ? 126.408 18.451  37.807  1.000 30.600  ? 264 ASN BBB CB  1 
ATOM 3790  C CG  . ASN B 1 247 ? 127.313 19.636  38.096  1.000 32.170  ? 264 ASN BBB CG  1 
ATOM 3791  O OD1 . ASN B 1 247 ? 126.968 20.480  38.939  1.000 39.970  ? 264 ASN BBB OD1 1 
ATOM 3792  N ND2 . ASN B 1 247 ? 128.465 19.692  37.439  1.000 25.240  ? 264 ASN BBB ND2 1 
ATOM 3793  N N   . ARG B 1 248 ? 124.361 16.959  39.688  1.000 23.570  ? 265 ARG BBB N   1 
ATOM 3794  C CA  . ARG B 1 248 ? 123.056 16.304  39.965  1.000 22.890  ? 265 ARG BBB CA  1 
ATOM 3795  C C   . ARG B 1 248 ? 122.452 15.783  38.669  1.000 23.060  ? 265 ARG BBB C   1 
ATOM 3796  O O   . ARG B 1 248 ? 121.898 14.703  38.692  1.000 22.720  ? 265 ARG BBB O   1 
ATOM 3797  C CB  . ARG B 1 248 ? 122.107 17.301  40.653  1.000 23.260  ? 265 ARG BBB CB  1 
ATOM 3798  C CG  . ARG B 1 248 ? 120.625 17.085  40.386  1.000 22.500  ? 265 ARG BBB CG  1 
ATOM 3799  C CD  . ARG B 1 248 ? 119.701 17.987  41.193  1.000 22.220  ? 265 ARG BBB CD  1 
ATOM 3800  N NE  . ARG B 1 248 ? 119.272 17.428  42.480  1.000 20.240  ? 265 ARG BBB NE  1 
ATOM 3801  C CZ  . ARG B 1 248 ? 119.711 17.838  43.659  1.000 21.560  ? 265 ARG BBB CZ  1 
ATOM 3802  N NH1 . ARG B 1 248 ? 120.600 18.805  43.760  1.000 22.880  ? 265 ARG BBB NH1 1 
ATOM 3803  N NH2 . ARG B 1 248 ? 119.290 17.258  44.758  1.000 24.820  ? 265 ARG BBB NH2 1 
ATOM 3804  N N   . SER B 1 249 ? 122.573 16.538  37.578  1.000 27.030  ? 266 SER BBB N   1 
ATOM 3805  C CA  . SER B 1 249 ? 121.986 16.220  36.247  1.000 28.770  ? 266 SER BBB CA  1 
ATOM 3806  C C   . SER B 1 249 ? 122.699 15.038  35.603  1.000 31.470  ? 266 SER BBB C   1 
ATOM 3807  O O   . SER B 1 249 ? 122.200 14.564  34.568  1.000 34.830  ? 266 SER BBB O   1 
ATOM 3808  C CB  . SER B 1 249 ? 122.114 17.378  35.325  1.000 27.310  ? 266 SER BBB CB  1 
ATOM 3809  O OG  . SER B 1 249 ? 123.486 17.564  34.988  1.000 25.580  ? 266 SER BBB OG  1 
ATOM 3810  N N   . GLY B 1 250 ? 123.888 14.697  36.107  1.000 32.640  ? 267 GLY BBB N   1 
ATOM 3811  C CA  . GLY B 1 250 ? 124.813 13.734  35.484  1.000 31.550  ? 267 GLY BBB CA  1 
ATOM 3812  C C   . GLY B 1 250 ? 125.910 14.418  34.688  1.000 30.080  ? 267 GLY BBB C   1 
ATOM 3813  O O   . GLY B 1 250 ? 126.906 13.733  34.381  1.000 29.450  ? 267 GLY BBB O   1 
ATOM 3814  N N   . SER B 1 251 ? 125.744 15.701  34.345  1.000 28.260  ? 268 SER BBB N   1 
ATOM 3815  C CA  . SER B 1 251 ? 126.717 16.473  33.524  1.000 25.920  ? 268 SER BBB CA  1 
ATOM 3816  C C   . SER B 1 251 ? 128.058 16.524  34.273  1.000 24.780  ? 268 SER BBB C   1 
ATOM 3817  O O   . SER B 1 251 ? 128.035 16.652  35.496  1.000 24.120  ? 268 SER BBB O   1 
ATOM 3818  C CB  . SER B 1 251 ? 126.180 17.855  33.207  1.000 25.420  ? 268 SER BBB CB  1 
ATOM 3819  O OG  . SER B 1 251 ? 124.797 17.838  32.925  1.000 22.110  ? 268 SER BBB OG  1 
ATOM 3820  N N   . GLN B 1 252 ? 129.179 16.410  33.573  1.000 24.270  ? 269 GLN BBB N   1 
ATOM 3821  C CA  . GLN B 1 252 ? 130.500 16.234  34.225  1.000 22.990  ? 269 GLN BBB CA  1 
ATOM 3822  C C   . GLN B 1 252 ? 131.443 17.377  33.864  1.000 22.340  ? 269 GLN BBB C   1 
ATOM 3823  O O   . GLN B 1 252 ? 131.551 17.703  32.671  1.000 25.370  ? 269 GLN BBB O   1 
ATOM 3824  C CB  . GLN B 1 252 ? 131.122 14.911  33.794  1.000 24.090  ? 269 GLN BBB CB  1 
ATOM 3825  C CG  . GLN B 1 252 ? 130.491 13.718  34.486  1.000 25.550  ? 269 GLN BBB CG  1 
ATOM 3826  C CD  . GLN B 1 252 ? 130.961 12.394  33.939  1.000 27.160  ? 269 GLN BBB CD  1 
ATOM 3827  O OE1 . GLN B 1 252 ? 131.231 12.226  32.747  1.000 26.130  ? 269 GLN BBB OE1 1 
ATOM 3828  N NE2 . GLN B 1 252 ? 131.050 11.426  34.836  1.000 33.680  ? 269 GLN BBB NE2 1 
ATOM 3829  N N   . GLN B 1 253 ? 132.156 17.899  34.865  1.000 22.460  ? 270 GLN BBB N   1 
ATOM 3830  C CA  . GLN B 1 253 ? 133.212 18.938  34.751  1.000 20.560  ? 270 GLN BBB CA  1 
ATOM 3831  C C   . GLN B 1 253 ? 134.523 18.367  35.269  1.000 18.430  ? 270 GLN BBB C   1 
ATOM 3832  O O   . GLN B 1 253 ? 134.525 17.847  36.359  1.000 18.010  ? 270 GLN BBB O   1 
ATOM 3833  C CB  . GLN B 1 253 ? 132.833 20.170  35.572  1.000 21.400  ? 270 GLN BBB CB  1 
ATOM 3834  C CG  . GLN B 1 253 ? 131.546 20.854  35.098  1.000 23.090  ? 270 GLN BBB CG  1 
ATOM 3835  C CD  . GLN B 1 253 ? 131.019 21.816  36.146  1.000 24.500  ? 270 GLN BBB CD  1 
ATOM 3836  O OE1 . GLN B 1 253 ? 130.238 21.431  37.029  1.000 24.830  ? 270 GLN BBB OE1 1 
ATOM 3837  N NE2 . GLN B 1 253 ? 131.477 23.066  36.081  1.000 22.000  ? 270 GLN BBB NE2 1 
ATOM 3838  N N   . TRP B 1 254 ? 135.587 18.433  34.494  1.000 19.100  ? 271 TRP BBB N   1 
ATOM 3839  C CA  . TRP B 1 254 ? 136.957 18.193  35.007  1.000 21.660  ? 271 TRP BBB CA  1 
ATOM 3840  C C   . TRP B 1 254 ? 137.143 19.007  36.292  1.000 23.850  ? 271 TRP BBB C   1 
ATOM 3841  O O   . TRP B 1 254 ? 136.639 20.142  36.313  1.000 29.370  ? 271 TRP BBB O   1 
ATOM 3842  C CB  . TRP B 1 254 ? 137.985 18.643  33.969  1.000 22.180  ? 271 TRP BBB CB  1 
ATOM 3843  C CG  . TRP B 1 254 ? 137.957 17.911  32.670  1.000 22.190  ? 271 TRP BBB CG  1 
ATOM 3844  C CD1 . TRP B 1 254 ? 137.599 18.402  31.453  1.000 22.610  ? 271 TRP BBB CD1 1 
ATOM 3845  C CD2 . TRP B 1 254 ? 138.361 16.558  32.457  1.000 22.560  ? 271 TRP BBB CD2 1 
ATOM 3846  N NE1 . TRP B 1 254 ? 137.744 17.439  30.497  1.000 23.350  ? 271 TRP BBB NE1 1 
ATOM 3847  C CE2 . TRP B 1 254 ? 138.207 16.300  31.090  1.000 22.880  ? 271 TRP BBB CE2 1 
ATOM 3848  C CE3 . TRP B 1 254 ? 138.811 15.539  33.295  1.000 24.240  ? 271 TRP BBB CE3 1 
ATOM 3849  C CZ2 . TRP B 1 254 ? 138.499 15.059  30.542  1.000 23.570  ? 271 TRP BBB CZ2 1 
ATOM 3850  C CZ3 . TRP B 1 254 ? 139.086 14.308  32.753  1.000 24.450  ? 271 TRP BBB CZ3 1 
ATOM 3851  C CH2 . TRP B 1 254 ? 138.939 14.078  31.392  1.000 23.490  ? 271 TRP BBB CH2 1 
ATOM 3852  N N   . ARG B 1 255 ? 137.848 18.499  37.303  1.000 22.970  ? 272 ARG BBB N   1 
ATOM 3853  C CA  . ARG B 1 255 ? 138.212 19.301  38.503  1.000 24.170  ? 272 ARG BBB CA  1 
ATOM 3854  C C   . ARG B 1 255 ? 139.715 19.204  38.743  1.000 24.660  ? 272 ARG BBB C   1 
ATOM 3855  O O   . ARG B 1 255 ? 140.249 18.083  38.738  1.000 25.190  ? 272 ARG BBB O   1 
ATOM 3856  C CB  . ARG B 1 255 ? 137.498 18.808  39.760  1.000 26.080  ? 272 ARG BBB CB  1 
ATOM 3857  C CG  . ARG B 1 255 ? 137.839 19.595  41.013  1.000 27.220  ? 272 ARG BBB CG  1 
ATOM 3858  C CD  . ARG B 1 255 ? 137.317 21.015  40.904  1.000 28.070  ? 272 ARG BBB CD  1 
ATOM 3859  N NE  . ARG B 1 255 ? 137.141 21.746  42.168  1.000 27.410  ? 272 ARG BBB NE  1 
ATOM 3860  C CZ  . ARG B 1 255 ? 138.068 22.504  42.758  1.000 27.940  ? 272 ARG BBB CZ  1 
ATOM 3861  N NH1 . ARG B 1 255 ? 139.289 22.625  42.257  1.000 30.460  ? 272 ARG BBB NH1 1 
ATOM 3862  N NH2 . ARG B 1 255 ? 137.771 23.142  43.867  1.000 28.200  ? 272 ARG BBB NH2 1 
ATOM 3863  N N   . GLY B 1 256 ? 140.361 20.343  38.956  1.000 25.020  ? 273 GLY BBB N   1 
ATOM 3864  C CA  . GLY B 1 256 ? 141.823 20.427  39.087  1.000 25.290  ? 273 GLY BBB CA  1 
ATOM 3865  C C   . GLY B 1 256 ? 142.204 20.884  40.473  1.000 25.350  ? 273 GLY BBB C   1 
ATOM 3866  O O   . GLY B 1 256 ? 141.324 21.383  41.186  1.000 24.390  ? 273 GLY BBB O   1 
ATOM 3867  N N   . LEU B 1 257 ? 143.471 20.714  40.836  1.000 25.600  ? 274 LEU BBB N   1 
ATOM 3868  C CA  . LEU B 1 257 ? 144.029 21.226  42.112  1.000 25.750  ? 274 LEU BBB CA  1 
ATOM 3869  C C   . LEU B 1 257 ? 145.427 21.796  41.882  1.000 26.980  ? 274 LEU BBB C   1 
ATOM 3870  O O   . LEU B 1 257 ? 146.168 21.317  40.995  1.000 27.680  ? 274 LEU BBB O   1 
ATOM 3871  C CB  . LEU B 1 257 ? 144.082 20.105  43.145  1.000 26.060  ? 274 LEU BBB CB  1 
ATOM 3872  C CG  . LEU B 1 257 ? 142.738 19.651  43.692  1.000 27.640  ? 274 LEU BBB CG  1 
ATOM 3873  C CD1 . LEU B 1 257 ? 142.933 18.451  44.605  1.000 27.240  ? 274 LEU BBB CD1 1 
ATOM 3874  C CD2 . LEU B 1 257 ? 142.021 20.788  44.414  1.000 29.590  ? 274 LEU BBB CD2 1 
ATOM 3875  N N   . SER B 1 258 ? 145.764 22.795  42.686  1.000 28.310  ? 275 SER BBB N   1 
ATOM 3876  C CA  . SER B 1 258 ? 147.081 23.470  42.668  1.000 29.480  ? 275 SER BBB CA  1 
ATOM 3877  C C   . SER B 1 258 ? 148.179 22.471  43.057  1.000 28.930  ? 275 SER BBB C   1 
ATOM 3878  O O   . SER B 1 258 ? 147.885 21.495  43.771  1.000 29.230  ? 275 SER BBB O   1 
ATOM 3879  C CB  . SER B 1 258 ? 147.053 24.661  43.573  1.000 31.330  ? 275 SER BBB CB  1 
ATOM 3880  O OG  . SER B 1 258 ? 145.979 25.514  43.232  1.000 31.090  ? 275 SER BBB OG  1 
ATOM 3881  N N   . ARG B 1 259 ? 149.400 22.712  42.593  1.000 28.640  ? 276 ARG BBB N   1 
ATOM 3882  C CA  . ARG B 1 259 ? 150.597 21.915  42.961  1.000 29.160  ? 276 ARG BBB CA  1 
ATOM 3883  C C   . ARG B 1 259 ? 151.638 22.828  43.605  1.000 28.630  ? 276 ARG BBB C   1 
ATOM 3884  O O   . ARG B 1 259 ? 152.025 23.812  42.981  1.000 28.450  ? 276 ARG BBB O   1 
ATOM 3885  C CB  . ARG B 1 259 ? 151.181 21.233  41.723  1.000 31.270  ? 276 ARG BBB CB  1 
ATOM 3886  C CG  . ARG B 1 259 ? 152.498 20.527  41.974  1.000 31.530  ? 276 ARG BBB CG  1 
ATOM 3887  C CD  . ARG B 1 259 ? 152.859 19.595  40.815  1.000 33.280  ? 276 ARG BBB CD  1 
ATOM 3888  N NE  . ARG B 1 259 ? 151.933 18.478  40.712  1.000 33.440  ? 276 ARG BBB NE  1 
ATOM 3889  C CZ  . ARG B 1 259 ? 152.079 17.309  41.318  1.000 33.740  ? 276 ARG BBB CZ  1 
ATOM 3890  N NH1 . ARG B 1 259 ? 153.123 17.051  42.093  1.000 32.840  ? 276 ARG BBB NH1 1 
ATOM 3891  N NH2 . ARG B 1 259 ? 151.150 16.393  41.150  1.000 36.170  ? 276 ARG BBB NH2 1 
ATOM 3892  N N   . TYR B 1 260 ? 152.104 22.471  44.795  1.000 29.750  ? 277 TYR BBB N   1 
ATOM 3893  C CA  . TYR B 1 260 ? 153.244 23.116  45.496  1.000 30.200  ? 277 TYR BBB CA  1 
ATOM 3894  C C   . TYR B 1 260 ? 154.558 22.614  44.896  1.000 29.930  ? 277 TYR BBB C   1 
ATOM 3895  O O   . TYR B 1 260 ? 154.675 21.414  44.614  1.000 33.600  ? 277 TYR BBB O   1 
ATOM 3896  C CB  . TYR B 1 260 ? 153.182 22.764  46.978  1.000 31.480  ? 277 TYR BBB CB  1 
ATOM 3897  C CG  . TYR B 1 260 ? 154.384 23.123  47.814  1.000 33.720  ? 277 TYR BBB CG  1 
ATOM 3898  C CD1 . TYR B 1 260 ? 154.527 24.387  48.363  1.000 34.160  ? 277 TYR BBB CD1 1 
ATOM 3899  C CD2 . TYR B 1 260 ? 155.332 22.165  48.138  1.000 34.010  ? 277 TYR BBB CD2 1 
ATOM 3900  C CE1 . TYR B 1 260 ? 155.591 24.700  49.190  1.000 32.280  ? 277 TYR BBB CE1 1 
ATOM 3901  C CE2 . TYR B 1 260 ? 156.406 22.464  48.959  1.000 33.040  ? 277 TYR BBB CE2 1 
ATOM 3902  C CZ  . TYR B 1 260 ? 156.529 23.732  49.491  1.000 32.760  ? 277 TYR BBB CZ  1 
ATOM 3903  O OH  . TYR B 1 260 ? 157.584 24.025  50.303  1.000 36.670  ? 277 TYR BBB OH  1 
ATOM 3904  N N   . PHE B 1 261 ? 155.517 23.515  44.727  1.000 29.340  ? 278 PHE BBB N   1 
ATOM 3905  C CA  . PHE B 1 261 ? 156.925 23.199  44.376  1.000 30.310  ? 278 PHE BBB CA  1 
ATOM 3906  C C   . PHE B 1 261 ? 157.866 23.854  45.391  1.000 31.140  ? 278 PHE BBB C   1 
ATOM 3907  O O   . PHE B 1 261 ? 157.625 24.986  45.788  1.000 31.330  ? 278 PHE BBB O   1 
ATOM 3908  C CB  . PHE B 1 261 ? 157.284 23.734  42.990  1.000 30.720  ? 278 PHE BBB CB  1 
ATOM 3909  C CG  . PHE B 1 261 ? 156.544 23.139  41.811  1.000 28.210  ? 278 PHE BBB CG  1 
ATOM 3910  C CD1 . PHE B 1 261 ? 155.229 23.493  41.537  1.000 24.830  ? 278 PHE BBB CD1 1 
ATOM 3911  C CD2 . PHE B 1 261 ? 157.198 22.285  40.933  1.000 26.000  ? 278 PHE BBB CD2 1 
ATOM 3912  C CE1 . PHE B 1 261 ? 154.578 22.987  40.425  1.000 22.890  ? 278 PHE BBB CE1 1 
ATOM 3913  C CE2 . PHE B 1 261 ? 156.553 21.788  39.822  1.000 25.150  ? 278 PHE BBB CE2 1 
ATOM 3914  C CZ  . PHE B 1 261 ? 155.250 22.145  39.564  1.000 23.610  ? 278 PHE BBB CZ  1 
ATOM 3915  N N   . LYS B 1 262 ? 158.926 23.163  45.781  1.000 34.170  ? 279 LYS BBB N   1 
ATOM 3916  C CA  . LYS B 1 262 ? 160.064 23.761  46.515  1.000 36.940  ? 279 LYS BBB CA  1 
ATOM 3917  C C   . LYS B 1 262 ? 161.330 23.190  45.891  1.000 36.900  ? 279 LYS BBB C   1 
ATOM 3918  O O   . LYS B 1 262 ? 161.547 21.965  46.000  1.000 35.720  ? 279 LYS BBB O   1 
ATOM 3919  C CB  . LYS B 1 262 ? 159.976 23.446  48.006  1.000 41.140  ? 279 LYS BBB CB  1 
ATOM 3920  C CG  . LYS B 1 262 ? 161.061 24.070  48.870  1.000 46.150  ? 279 LYS BBB CG  1 
ATOM 3921  C CD  . LYS B 1 262 ? 160.894 23.721  50.329  1.000 53.610  ? 279 LYS BBB CD  1 
ATOM 3922  C CE  . LYS B 1 262 ? 162.043 24.174  51.201  1.000 59.810  ? 279 LYS BBB CE  1 
ATOM 3923  N NZ  . LYS B 1 262 ? 162.174 23.280  52.373  1.000 65.230  ? 279 LYS BBB NZ  1 
ATOM 3924  N N   . VAL B 1 263 ? 162.110 24.032  45.224  1.000 36.730  ? 280 VAL BBB N   1 
ATOM 3925  C CA  . VAL B 1 263 ? 163.312 23.571  44.485  1.000 37.990  ? 280 VAL BBB CA  1 
ATOM 3926  C C   . VAL B 1 263 ? 164.553 24.154  45.155  1.000 37.370  ? 280 VAL BBB C   1 
ATOM 3927  O O   . VAL B 1 263 ? 164.656 25.374  45.238  1.000 34.840  ? 280 VAL BBB O   1 
ATOM 3928  C CB  . VAL B 1 263 ? 163.204 23.931  42.995  1.000 40.450  ? 280 VAL BBB CB  1 
ATOM 3929  C CG1 . VAL B 1 263 ? 164.409 23.437  42.210  1.000 42.720  ? 280 VAL BBB CG1 1 
ATOM 3930  C CG2 . VAL B 1 263 ? 161.918 23.394  42.387  1.000 41.340  ? 280 VAL BBB CG2 1 
ATOM 3931  N N   . GLN B 1 264 ? 165.428 23.282  45.650  1.000 42.000  ? 281 GLN BBB N   1 
ATOM 3932  C CA  . GLN B 1 264 ? 166.821 23.623  46.036  1.000 47.540  ? 281 GLN BBB CA  1 
ATOM 3933  C C   . GLN B 1 264 ? 167.607 23.897  44.759  1.000 43.520  ? 281 GLN BBB C   1 
ATOM 3934  O O   . GLN B 1 264 ? 167.499 23.108  43.824  1.000 37.750  ? 281 GLN BBB O   1 
ATOM 3935  C CB  . GLN B 1 264 ? 167.497 22.463  46.796  1.000 59.480  ? 281 GLN BBB CB  1 
ATOM 3936  C CG  . GLN B 1 264 ? 166.828 22.034  48.103  1.000 65.310  ? 281 GLN BBB CG  1 
ATOM 3937  C CD  . GLN B 1 264 ? 166.932 23.122  49.151  1.000 77.770  ? 281 GLN BBB CD  1 
ATOM 3938  O OE1 . GLN B 1 264 ? 167.831 23.978  49.083  1.000 101.760 ? 281 GLN BBB OE1 1 
ATOM 3939  N NE2 . GLN B 1 264 ? 165.995 23.104  50.093  1.000 68.450  ? 281 GLN BBB NE2 1 
ATOM 3940  N N   . LEU B 1 265 ? 168.391 24.962  44.739  1.000 49.530  ? 282 LEU BBB N   1 
ATOM 3941  C CA  . LEU B 1 265 ? 169.286 25.296  43.606  1.000 50.310  ? 282 LEU BBB CA  1 
ATOM 3942  C C   . LEU B 1 265 ? 170.693 25.542  44.166  1.000 47.050  ? 282 LEU BBB C   1 
ATOM 3943  O O   . LEU B 1 265 ? 170.788 25.971  45.315  1.000 45.400  ? 282 LEU BBB O   1 
ATOM 3944  C CB  . LEU B 1 265 ? 168.717 26.530  42.901  1.000 46.930  ? 282 LEU BBB CB  1 
ATOM 3945  C CG  . LEU B 1 265 ? 167.362 26.329  42.219  1.000 45.470  ? 282 LEU BBB CG  1 
ATOM 3946  C CD1 . LEU B 1 265 ? 166.431 27.510  42.439  1.000 42.030  ? 282 LEU BBB CD1 1 
ATOM 3947  C CD2 . LEU B 1 265 ? 167.543 26.093  40.730  1.000 49.120  ? 282 LEU BBB CD2 1 
ATOM 3948  N N   . ARG B 1 266 ? 171.735 25.282  43.384  1.000 47.310  ? 283 ARG BBB N   1 
ATOM 3949  C CA  . ARG B 1 266 ? 173.132 25.663  43.714  1.000 49.660  ? 283 ARG BBB CA  1 
ATOM 3950  C C   . ARG B 1 266 ? 173.784 26.264  42.466  1.000 50.200  ? 283 ARG BBB C   1 
ATOM 3951  O O   . ARG B 1 266 ? 173.168 26.211  41.396  1.000 60.670  ? 283 ARG BBB O   1 
ATOM 3952  C CB  . ARG B 1 266 ? 173.905 24.446  44.238  1.000 48.860  ? 283 ARG BBB CB  1 
ATOM 3953  C CG  . ARG B 1 266 ? 174.262 23.429  43.166  1.000 44.860  ? 283 ARG BBB CG  1 
ATOM 3954  C CD  . ARG B 1 266 ? 174.715 22.120  43.776  1.000 44.330  ? 283 ARG BBB CD  1 
ATOM 3955  N NE  . ARG B 1 266 ? 174.953 21.145  42.728  1.000 46.440  ? 283 ARG BBB NE  1 
ATOM 3956  C CZ  . ARG B 1 266 ? 175.055 19.838  42.912  1.000 49.980  ? 283 ARG BBB CZ  1 
ATOM 3957  N NH1 . ARG B 1 266 ? 174.933 19.346  44.125  1.000 53.080  ? 283 ARG BBB NH1 1 
ATOM 3958  N NH2 . ARG B 1 266 ? 175.261 19.021  41.890  1.000 54.230  ? 283 ARG BBB NH2 1 
ATOM 3959  N N   . LYS B 1 267 ? 174.997 26.799  42.599  1.000 50.510  ? 284 LYS BBB N   1 
ATOM 3960  C CA  . LYS B 1 267 ? 175.734 27.466  41.499  1.000 53.150  ? 284 LYS BBB CA  1 
ATOM 3961  C C   . LYS B 1 267 ? 176.714 26.452  40.905  1.000 52.890  ? 284 LYS BBB C   1 
ATOM 3962  O O   . LYS B 1 267 ? 177.513 25.908  41.684  1.000 49.170  ? 284 LYS BBB O   1 
ATOM 3963  C CB  . LYS B 1 267 ? 176.507 28.648  42.076  1.000 54.230  ? 284 LYS BBB CB  1 
ATOM 3964  C CG  . LYS B 1 267 ? 175.620 29.749  42.621  1.000 57.010  ? 284 LYS BBB CG  1 
ATOM 3965  C CD  . LYS B 1 267 ? 176.377 30.949  43.080  1.000 58.110  ? 284 LYS BBB CD  1 
ATOM 3966  C CE  . LYS B 1 267 ? 175.437 32.095  43.390  1.000 63.950  ? 284 LYS BBB CE  1 
ATOM 3967  N NZ  . LYS B 1 267 ? 176.099 33.200  44.124  1.000 71.740  ? 284 LYS BBB NZ  1 
ATOM 3968  N N   . ARG B 1 268 ? 176.746 26.397  39.578  1.000 55.830  ? 285 ARG BBB N   1 
ATOM 3969  C CA  . ARG B 1 268 ? 177.674 25.502  38.867  1.000 59.960  ? 285 ARG BBB CA  1 
ATOM 3970  C C   . ARG B 1 268 ? 178.473 26.350  37.883  1.000 71.340  ? 285 ARG BBB C   1 
ATOM 3971  O O   . ARG B 1 268 ? 177.858 27.182  37.204  1.000 62.680  ? 285 ARG BBB O   1 
ATOM 3972  C CB  . ARG B 1 268 ? 176.888 24.425  38.119  1.000 55.720  ? 285 ARG BBB CB  1 
ATOM 3973  C CG  . ARG B 1 268 ? 177.733 23.261  37.635  1.000 54.730  ? 285 ARG BBB CG  1 
ATOM 3974  C CD  . ARG B 1 268 ? 177.438 22.019  38.441  1.000 56.710  ? 285 ARG BBB CD  1 
ATOM 3975  N NE  . ARG B 1 268 ? 178.330 20.934  38.079  1.000 63.150  ? 285 ARG BBB NE  1 
ATOM 3976  C CZ  . ARG B 1 268 ? 178.107 19.657  38.352  1.000 67.760  ? 285 ARG BBB CZ  1 
ATOM 3977  N NH1 . ARG B 1 268 ? 177.016 19.303  39.004  1.000 64.490  ? 285 ARG BBB NH1 1 
ATOM 3978  N NH2 . ARG B 1 268 ? 178.980 18.740  37.978  1.000 75.470  ? 285 ARG BBB NH2 1 
ATOM 3979  N N   . ARG B 1 269 ? 179.793 26.206  37.881  1.000 84.390  ? 286 ARG BBB N   1 
ATOM 3980  C CA  . ARG B 1 269 ? 180.656 26.863  36.867  1.000 86.420  ? 286 ARG BBB CA  1 
ATOM 3981  C C   . ARG B 1 269 ? 180.411 26.194  35.501  1.000 73.840  ? 286 ARG BBB C   1 
ATOM 3982  O O   . ARG B 1 269 ? 180.203 24.974  35.486  1.000 70.960  ? 286 ARG BBB O   1 
ATOM 3983  C CB  . ARG B 1 269 ? 182.080 26.758  37.429  1.000 107.110 ? 286 ARG BBB CB  1 
ATOM 3984  C CG  . ARG B 1 269 ? 183.065 27.753  36.836  1.000 123.010 ? 286 ARG BBB CG  1 
ATOM 3985  C CD  . ARG B 1 269 ? 184.249 27.961  37.767  1.000 120.890 ? 286 ARG BBB CD  1 
ATOM 3986  N NE  . ARG B 1 269 ? 185.497 27.347  37.310  1.000 114.060 ? 286 ARG BBB NE  1 
ATOM 3987  C CZ  . ARG B 1 269 ? 186.446 27.964  36.604  1.000 110.630 ? 286 ARG BBB CZ  1 
ATOM 3988  N NH1 . ARG B 1 269 ? 186.299 29.225  36.225  1.000 106.140 ? 286 ARG BBB NH1 1 
ATOM 3989  N NH2 . ARG B 1 269 ? 187.543 27.309  36.269  1.000 111.040 ? 286 ARG BBB NH2 1 
ATOM 3990  N N   . VAL B 1 270 ? 180.366 26.975  34.419  1.000 70.080  ? 287 VAL BBB N   1 
ATOM 3991  C CA  . VAL B 1 270 ? 179.933 26.560  33.047  1.000 74.010  ? 287 VAL BBB CA  1 
ATOM 3992  C C   . VAL B 1 270 ? 180.787 27.322  32.014  1.000 83.020  ? 287 VAL BBB C   1 
ATOM 3993  O O   . VAL B 1 270 ? 181.021 28.520  32.252  1.000 92.040  ? 287 VAL BBB O   1 
ATOM 3994  C CB  . VAL B 1 270 ? 178.425 26.858  32.860  1.000 74.170  ? 287 VAL BBB CB  1 
ATOM 3995  C CG1 . VAL B 1 270 ? 177.892 26.452  31.502  1.000 79.500  ? 287 VAL BBB CG1 1 
ATOM 3996  C CG2 . VAL B 1 270 ? 177.584 26.189  33.909  1.000 75.370  ? 287 VAL BBB CG2 1 
ATOM 3997  N N   . LYS B 1 271 ? 181.218 26.680  30.912  1.000 91.890  ? 288 LYS BBB N   1 
ATOM 3998  C CA  . LYS B 1 271 ? 181.736 27.353  29.677  1.000 86.030  ? 288 LYS BBB CA  1 
ATOM 3999  C C   . LYS B 1 271 ? 180.609 27.507  28.643  1.000 79.100  ? 288 LYS BBB C   1 
ATOM 4000  O O   . LYS B 1 271 ? 180.572 28.389  27.782  1.000 70.810  ? 288 LYS BBB O   1 
ATOM 4001  C CB  . LYS B 1 271 ? 182.873 26.550  29.047  1.000 77.870  ? 288 LYS BBB CB  1 
ATOM 4002  N N   . GLU C 1 8   ? 168.727 27.349  66.212  1.000 38.620  ? 25  GLU CCC N   1 
ATOM 4003  C CA  . GLU C 1 8   ? 170.020 26.765  65.654  1.000 44.600  ? 25  GLU CCC CA  1 
ATOM 4004  C C   . GLU C 1 8   ? 170.336 25.457  66.397  1.000 49.190  ? 25  GLU CCC C   1 
ATOM 4005  O O   . GLU C 1 8   ? 170.409 25.487  67.642  1.000 53.700  ? 25  GLU CCC O   1 
ATOM 4006  C CB  . GLU C 1 8   ? 171.182 27.734  65.761  1.000 43.740  ? 25  GLU CCC CB  1 
ATOM 4007  N N   . VAL C 1 9   ? 170.457 24.347  65.665  1.000 45.430  ? 26  VAL CCC N   1 
ATOM 4008  C CA  . VAL C 1 9   ? 170.392 22.972  66.237  1.000 44.040  ? 26  VAL CCC CA  1 
ATOM 4009  C C   . VAL C 1 9   ? 171.812 22.460  66.444  1.000 43.410  ? 26  VAL CCC C   1 
ATOM 4010  O O   . VAL C 1 9   ? 172.519 22.297  65.472  1.000 40.470  ? 26  VAL CCC O   1 
ATOM 4011  C CB  . VAL C 1 9   ? 169.589 22.034  65.317  1.000 44.250  ? 26  VAL CCC CB  1 
ATOM 4012  C CG1 . VAL C 1 9   ? 169.576 20.597  65.824  1.000 43.140  ? 26  VAL CCC CG1 1 
ATOM 4013  C CG2 . VAL C 1 9   ? 168.171 22.542  65.100  1.000 42.830  ? 26  VAL CCC CG2 1 
ATOM 4014  N N   . LEU C 1 10  ? 172.185 22.204  67.689  1.000 50.910  ? 27  LEU CCC N   1 
ATOM 4015  C CA  . LEU C 1 10  ? 173.515 21.673  68.085  1.000 55.980  ? 27  LEU CCC CA  1 
ATOM 4016  C C   . LEU C 1 10  ? 173.403 20.161  68.230  1.000 51.530  ? 27  LEU CCC C   1 
ATOM 4017  O O   . LEU C 1 10  ? 172.482 19.603  67.614  1.000 49.650  ? 27  LEU CCC O   1 
ATOM 4018  C CB  . LEU C 1 10  ? 173.961 22.372  69.374  1.000 64.680  ? 27  LEU CCC CB  1 
ATOM 4019  C CG  . LEU C 1 10  ? 173.817 23.897  69.320  1.000 69.800  ? 27  LEU CCC CG  1 
ATOM 4020  C CD1 . LEU C 1 10  ? 174.226 24.549  70.636  1.000 76.240  ? 27  LEU CCC CD1 1 
ATOM 4021  C CD2 . LEU C 1 10  ? 174.597 24.507  68.165  1.000 65.680  ? 27  LEU CCC CD2 1 
ATOM 4022  N N   . GLU C 1 11  ? 174.311 19.529  68.980  1.000 52.260  ? 28  GLU CCC N   1 
ATOM 4023  C CA  . GLU C 1 11  ? 174.519 18.057  68.944  1.000 59.350  ? 28  GLU CCC CA  1 
ATOM 4024  C C   . GLU C 1 11  ? 173.468 17.369  69.834  1.000 52.850  ? 28  GLU CCC C   1 
ATOM 4025  O O   . GLU C 1 11  ? 172.802 18.049  70.630  1.000 45.540  ? 28  GLU CCC O   1 
ATOM 4026  C CB  . GLU C 1 11  ? 175.985 17.729  69.280  1.000 67.690  ? 28  GLU CCC CB  1 
ATOM 4027  C CG  . GLU C 1 11  ? 176.313 17.642  70.770  1.000 71.370  ? 28  GLU CCC CG  1 
ATOM 4028  C CD  . GLU C 1 11  ? 176.010 18.855  71.645  1.000 75.480  ? 28  GLU CCC CD  1 
ATOM 4029  O OE1 . GLU C 1 11  ? 175.415 18.650  72.741  1.000 84.540  ? 28  GLU CCC OE1 1 
ATOM 4030  O OE2 . GLU C 1 11  ? 176.374 20.001  71.254  1.000 66.220  ? 28  GLU CCC OE2 1 
ATOM 4031  N N   . VAL C 1 12  ? 173.301 16.059  69.645  1.000 48.550  ? 29  VAL CCC N   1 
ATOM 4032  C CA  . VAL C 1 12  ? 172.324 15.207  70.378  1.000 48.950  ? 29  VAL CCC CA  1 
ATOM 4033  C C   . VAL C 1 12  ? 172.930 14.896  71.740  1.000 51.990  ? 29  VAL CCC C   1 
ATOM 4034  O O   . VAL C 1 12  ? 174.002 14.286  71.745  1.000 57.180  ? 29  VAL CCC O   1 
ATOM 4035  C CB  . VAL C 1 12  ? 172.013 13.900  69.617  1.000 46.540  ? 29  VAL CCC CB  1 
ATOM 4036  C CG1 . VAL C 1 12  ? 171.073 12.997  70.395  1.000 44.100  ? 29  VAL CCC CG1 1 
ATOM 4037  C CG2 . VAL C 1 12  ? 171.469 14.145  68.225  1.000 45.960  ? 29  VAL CCC CG2 1 
ATOM 4038  N N   . LYS C 1 13  ? 172.265 15.261  72.841  1.000 57.400  ? 30  LYS CCC N   1 
ATOM 4039  C CA  . LYS C 1 13  ? 172.675 14.826  74.203  1.000 60.510  ? 30  LYS CCC CA  1 
ATOM 4040  C C   . LYS C 1 13  ? 172.387 13.329  74.325  1.000 56.830  ? 30  LYS CCC C   1 
ATOM 4041  O O   . LYS C 1 13  ? 171.251 12.951  74.014  1.000 51.890  ? 30  LYS CCC O   1 
ATOM 4042  C CB  . LYS C 1 13  ? 171.952 15.636  75.296  1.000 64.820  ? 30  LYS CCC CB  1 
ATOM 4043  C CG  . LYS C 1 13  ? 172.575 15.500  76.684  1.000 74.170  ? 30  LYS CCC CG  1 
ATOM 4044  C CD  . LYS C 1 13  ? 173.968 16.141  76.850  1.000 84.590  ? 30  LYS CCC CD  1 
ATOM 4045  C CE  . LYS C 1 13  ? 174.031 17.647  76.645  1.000 86.560  ? 30  LYS CCC CE  1 
ATOM 4046  N NZ  . LYS C 1 13  ? 175.199 18.244  77.336  1.000 80.100  ? 30  LYS CCC NZ  1 
ATOM 4047  N N   . THR C 1 14  ? 173.393 12.522  74.684  1.000 60.240  ? 31  THR CCC N   1 
ATOM 4048  C CA  . THR C 1 14  ? 173.263 11.075  75.040  1.000 66.300  ? 31  THR CCC CA  1 
ATOM 4049  C C   . THR C 1 14  ? 173.517 10.939  76.545  1.000 62.350  ? 31  THR CCC C   1 
ATOM 4050  O O   . THR C 1 14  ? 173.887 11.971  77.174  1.000 70.140  ? 31  THR CCC O   1 
ATOM 4051  C CB  . THR C 1 14  ? 174.223 10.159  74.244  1.000 66.700  ? 31  THR CCC CB  1 
ATOM 4052  O OG1 . THR C 1 14  ? 175.559 10.538  74.540  1.000 66.820  ? 31  THR CCC OG1 1 
ATOM 4053  C CG2 . THR C 1 14  ? 174.009 10.204  72.745  1.000 66.690  ? 31  THR CCC CG2 1 
ATOM 4054  N N   . GLY C 1 15  ? 173.341 9.733   77.095  1.000 53.030  ? 32  GLY CCC N   1 
ATOM 4055  C CA  . GLY C 1 15  ? 173.490 9.466   78.536  1.000 54.660  ? 32  GLY CCC CA  1 
ATOM 4056  C C   . GLY C 1 15  ? 172.310 8.690   79.098  1.000 56.280  ? 32  GLY CCC C   1 
ATOM 4057  O O   . GLY C 1 15  ? 171.507 8.201   78.292  1.000 56.100  ? 32  GLY CCC O   1 
ATOM 4058  N N   . VAL C 1 16  ? 172.221 8.582   80.431  1.000 56.470  ? 33  VAL CCC N   1 
ATOM 4059  C CA  . VAL C 1 16  ? 171.345 7.631   81.161  1.000 54.630  ? 33  VAL CCC CA  1 
ATOM 4060  C C   . VAL C 1 16  ? 169.867 8.017   80.982  1.000 55.010  ? 33  VAL CCC C   1 
ATOM 4061  O O   . VAL C 1 16  ? 169.023 7.101   81.000  1.000 67.270  ? 33  VAL CCC O   1 
ATOM 4062  C CB  . VAL C 1 16  ? 171.730 7.523   82.631  1.000 49.360  ? 33  VAL CCC CB  1 
ATOM 4063  N N   . ASP C 1 17  ? 169.552 9.297   80.803  1.000 49.830  ? 34  ASP CCC N   1 
ATOM 4064  C CA  . ASP C 1 17  ? 168.144 9.772   80.746  1.000 52.560  ? 34  ASP CCC CA  1 
ATOM 4065  C C   . ASP C 1 17  ? 168.010 10.771  79.604  1.000 55.120  ? 34  ASP CCC C   1 
ATOM 4066  O O   . ASP C 1 17  ? 167.559 11.911  79.852  1.000 60.300  ? 34  ASP CCC O   1 
ATOM 4067  C CB  . ASP C 1 17  ? 167.701 10.384  82.080  1.000 58.340  ? 34  ASP CCC CB  1 
ATOM 4068  C CG  . ASP C 1 17  ? 166.809 9.471   82.893  1.000 60.690  ? 34  ASP CCC CG  1 
ATOM 4069  O OD1 . ASP C 1 17  ? 166.558 8.324   82.437  1.000 58.720  ? 34  ASP CCC OD1 1 
ATOM 4070  O OD2 . ASP C 1 17  ? 166.443 9.884   83.996  1.000 64.580  ? 34  ASP CCC OD2 1 
ATOM 4071  N N   . SER C 1 18  ? 168.378 10.360  78.388  1.000 53.030  ? 35  SER CCC N   1 
ATOM 4072  C CA  . SER C 1 18  ? 168.381 11.242  77.189  1.000 49.260  ? 35  SER CCC CA  1 
ATOM 4073  C C   . SER C 1 18  ? 167.194 10.894  76.288  1.000 46.180  ? 35  SER CCC C   1 
ATOM 4074  O O   . SER C 1 18  ? 166.867 11.710  75.390  1.000 46.720  ? 35  SER CCC O   1 
ATOM 4075  C CB  . SER C 1 18  ? 169.698 11.173  76.456  1.000 48.360  ? 35  SER CCC CB  1 
ATOM 4076  O OG  . SER C 1 18  ? 170.210 9.861   76.459  1.000 46.490  ? 35  SER CCC OG  1 
ATOM 4077  N N   . ILE C 1 19  ? 166.524 9.787   76.613  1.000 44.970  ? 36  ILE CCC N   1 
ATOM 4078  C CA  . ILE C 1 19  ? 165.401 9.285   75.774  1.000 45.300  ? 36  ILE CCC CA  1 
ATOM 4079  C C   . ILE C 1 19  ? 164.097 9.218   76.566  1.000 39.560  ? 36  ILE CCC C   1 
ATOM 4080  O O   . ILE C 1 19  ? 164.169 9.064   77.792  1.000 37.620  ? 36  ILE CCC O   1 
ATOM 4081  C CB  . ILE C 1 19  ? 165.803 7.901   75.212  1.000 43.930  ? 36  ILE CCC CB  1 
ATOM 4082  C CG1 . ILE C 1 19  ? 164.875 7.389   74.116  1.000 50.960  ? 36  ILE CCC CG1 1 
ATOM 4083  C CG2 . ILE C 1 19  ? 165.988 6.874   76.317  1.000 42.210  ? 36  ILE CCC CG2 1 
ATOM 4084  C CD1 . ILE C 1 19  ? 164.909 8.211   72.849  1.000 51.430  ? 36  ILE CCC CD1 1 
ATOM 4085  N N   . THR C 1 20  ? 162.963 9.419   75.903  1.000 38.730  ? 37  THR CCC N   1 
ATOM 4086  C CA  . THR C 1 20  ? 161.605 9.276   76.512  1.000 41.710  ? 37  THR CCC CA  1 
ATOM 4087  C C   . THR C 1 20  ? 160.611 8.822   75.432  1.000 39.290  ? 37  THR CCC C   1 
ATOM 4088  O O   . THR C 1 20  ? 160.996 8.879   74.241  1.000 40.680  ? 37  THR CCC O   1 
ATOM 4089  C CB  . THR C 1 20  ? 161.122 10.562  77.195  1.000 41.860  ? 37  THR CCC CB  1 
ATOM 4090  O OG1 . THR C 1 20  ? 159.940 10.308  77.951  1.000 42.640  ? 37  THR CCC OG1 1 
ATOM 4091  C CG2 . THR C 1 20  ? 160.794 11.662  76.216  1.000 40.170  ? 37  THR CCC CG2 1 
ATOM 4092  N N   . GLU C 1 21  ? 159.413 8.388   75.841  1.000 37.060  ? 38  GLU CCC N   1 
ATOM 4093  C CA  . GLU C 1 21  ? 158.349 7.822   74.962  1.000 36.640  ? 38  GLU CCC CA  1 
ATOM 4094  C C   . GLU C 1 21  ? 156.992 8.412   75.339  1.000 34.920  ? 38  GLU CCC C   1 
ATOM 4095  O O   . GLU C 1 21  ? 156.607 8.338   76.496  1.000 42.160  ? 38  GLU CCC O   1 
ATOM 4096  C CB  . GLU C 1 21  ? 158.173 6.314   75.110  1.000 37.450  ? 38  GLU CCC CB  1 
ATOM 4097  C CG  . GLU C 1 21  ? 159.308 5.484   74.528  1.000 42.770  ? 38  GLU CCC CG  1 
ATOM 4098  C CD  . GLU C 1 21  ? 158.946 4.018   74.400  1.000 49.500  ? 38  GLU CCC CD  1 
ATOM 4099  O OE1 . GLU C 1 21  ? 157.888 3.632   74.960  1.000 63.030  ? 38  GLU CCC OE1 1 
ATOM 4100  O OE2 . GLU C 1 21  ? 159.688 3.271   73.730  1.000 49.590  ? 38  GLU CCC OE2 1 
ATOM 4101  N N   . VAL C 1 22  ? 156.295 8.961   74.367  1.000 31.060  ? 39  VAL CCC N   1 
ATOM 4102  C CA  . VAL C 1 22  ? 154.843 9.222   74.417  1.000 27.600  ? 39  VAL CCC CA  1 
ATOM 4103  C C   . VAL C 1 22  ? 154.160 8.066   73.683  1.000 27.750  ? 39  VAL CCC C   1 
ATOM 4104  O O   . VAL C 1 22  ? 154.686 7.589   72.657  1.000 31.250  ? 39  VAL CCC O   1 
ATOM 4105  C CB  . VAL C 1 22  ? 154.527 10.571  73.759  1.000 27.300  ? 39  VAL CCC CB  1 
ATOM 4106  C CG1 . VAL C 1 22  ? 153.028 10.776  73.565  1.000 28.200  ? 39  VAL CCC CG1 1 
ATOM 4107  C CG2 . VAL C 1 22  ? 155.132 11.713  74.539  1.000 28.070  ? 39  VAL CCC CG2 1 
ATOM 4108  N N   . GLU C 1 23  ? 153.023 7.637   74.203  1.000 28.170  ? 40  GLU CCC N   1 
ATOM 4109  C CA  . GLU C 1 23  ? 152.178 6.562   73.643  1.000 28.970  ? 40  GLU CCC CA  1 
ATOM 4110  C C   . GLU C 1 23  ? 150.744 6.949   73.965  1.000 29.770  ? 40  GLU CCC C   1 
ATOM 4111  O O   . GLU C 1 23  ? 150.378 6.885   75.123  1.000 38.130  ? 40  GLU CCC O   1 
ATOM 4112  C CB  . GLU C 1 23  ? 152.557 5.226   74.282  1.000 30.650  ? 40  GLU CCC CB  1 
ATOM 4113  C CG  . GLU C 1 23  ? 151.950 4.010   73.619  1.000 33.840  ? 40  GLU CCC CG  1 
ATOM 4114  C CD  . GLU C 1 23  ? 152.248 2.701   74.334  1.000 34.980  ? 40  GLU CCC CD  1 
ATOM 4115  O OE1 . GLU C 1 23  ? 151.720 2.525   75.441  1.000 38.400  ? 40  GLU CCC OE1 1 
ATOM 4116  O OE2 . GLU C 1 23  ? 152.987 1.858   73.766  1.000 37.560  ? 40  GLU CCC OE2 1 
ATOM 4117  N N   . CYS C 1 24  ? 149.965 7.423   73.007  1.000 30.070  ? 41  CYS CCC N   1 
ATOM 4118  C CA  . CYS C 1 24  ? 148.533 7.666   73.254  1.000 33.580  ? 41  CYS CCC CA  1 
ATOM 4119  C C   . CYS C 1 24  ? 147.702 7.232   72.047  1.000 36.570  ? 41  CYS CCC C   1 
ATOM 4120  O O   . CYS C 1 24  ? 148.294 6.734   71.064  1.000 38.110  ? 41  CYS CCC O   1 
ATOM 4121  C CB  . CYS C 1 24  ? 148.322 9.128   73.591  1.000 36.620  ? 41  CYS CCC CB  1 
ATOM 4122  S SG  . CYS C 1 24  ? 148.544 10.185  72.152  1.000 37.500  ? 41  CYS CCC SG  1 
ATOM 4123  N N   . PHE C 1 25  ? 146.370 7.339   72.173  1.000 38.100  ? 42  PHE CCC N   1 
ATOM 4124  C CA  . PHE C 1 25  ? 145.399 7.140   71.072  1.000 39.080  ? 42  PHE CCC CA  1 
ATOM 4125  C C   . PHE C 1 25  ? 144.678 8.469   70.867  1.000 34.680  ? 42  PHE CCC C   1 
ATOM 4126  O O   . PHE C 1 25  ? 144.551 9.178   71.857  1.000 37.140  ? 42  PHE CCC O   1 
ATOM 4127  C CB  . PHE C 1 25  ? 144.450 5.982   71.383  1.000 45.330  ? 42  PHE CCC CB  1 
ATOM 4128  C CG  . PHE C 1 25  ? 143.607 6.204   72.601  1.000 50.450  ? 42  PHE CCC CG  1 
ATOM 4129  C CD1 . PHE C 1 25  ? 142.484 7.015   72.552  1.000 51.740  ? 42  PHE CCC CD1 1 
ATOM 4130  C CD2 . PHE C 1 25  ? 143.950 5.604   73.796  1.000 61.270  ? 42  PHE CCC CD2 1 
ATOM 4131  C CE1 . PHE C 1 25  ? 141.712 7.217   73.684  1.000 56.470  ? 42  PHE CCC CE1 1 
ATOM 4132  C CE2 . PHE C 1 25  ? 143.155 5.791   74.930  1.000 64.760  ? 42  PHE CCC CE2 1 
ATOM 4133  C CZ  . PHE C 1 25  ? 142.041 6.605   74.871  1.000 62.620  ? 42  PHE CCC CZ  1 
ATOM 4134  N N   . LEU C 1 26  ? 144.299 8.805   69.626  1.000 29.870  ? 43  LEU CCC N   1 
ATOM 4135  C CA  . LEU C 1 26  ? 143.416 9.950   69.282  1.000 28.870  ? 43  LEU CCC CA  1 
ATOM 4136  C C   . LEU C 1 26  ? 142.077 9.385   68.819  1.000 27.390  ? 43  LEU CCC C   1 
ATOM 4137  O O   . LEU C 1 26  ? 142.092 8.456   68.032  1.000 30.320  ? 43  LEU CCC O   1 
ATOM 4138  C CB  . LEU C 1 26  ? 144.051 10.791  68.172  1.000 28.380  ? 43  LEU CCC CB  1 
ATOM 4139  C CG  . LEU C 1 26  ? 144.921 11.948  68.647  1.000 28.110  ? 43  LEU CCC CG  1 
ATOM 4140  C CD1 . LEU C 1 26  ? 146.201 11.442  69.299  1.000 28.050  ? 43  LEU CCC CD1 1 
ATOM 4141  C CD2 . LEU C 1 26  ? 145.248 12.905  67.515  1.000 29.800  ? 43  LEU CCC CD2 1 
ATOM 4142  N N   . THR C 1 27  ? 140.966 9.923   69.274  1.000 28.340  ? 44  THR CCC N   1 
ATOM 4143  C CA  . THR C 1 27  ? 139.633 9.454   68.833  1.000 32.720  ? 44  THR CCC CA  1 
ATOM 4144  C C   . THR C 1 27  ? 139.252 10.237  67.584  1.000 32.120  ? 44  THR CCC C   1 
ATOM 4145  O O   . THR C 1 27  ? 139.812 11.282  67.279  1.000 34.500  ? 44  THR CCC O   1 
ATOM 4146  C CB  . THR C 1 27  ? 138.602 9.525   69.968  1.000 34.710  ? 44  THR CCC CB  1 
ATOM 4147  O OG1 . THR C 1 27  ? 138.165 10.873  70.124  1.000 35.710  ? 44  THR CCC OG1 1 
ATOM 4148  C CG2 . THR C 1 27  ? 139.164 9.017   71.277  1.000 36.400  ? 44  THR CCC CG2 1 
ATOM 4149  N N   . PRO C 1 28  ? 138.345 9.684   66.772  1.000 32.020  ? 45  PRO CCC N   1 
ATOM 4150  C CA  . PRO C 1 28  ? 137.850 10.388  65.598  1.000 33.530  ? 45  PRO CCC CA  1 
ATOM 4151  C C   . PRO C 1 28  ? 136.656 11.304  65.883  1.000 31.770  ? 45  PRO CCC C   1 
ATOM 4152  O O   . PRO C 1 28  ? 135.711 10.833  66.459  1.000 30.490  ? 45  PRO CCC O   1 
ATOM 4153  C CB  . PRO C 1 28  ? 137.464 9.204   64.688  1.000 34.590  ? 45  PRO CCC CB  1 
ATOM 4154  C CG  . PRO C 1 28  ? 137.012 8.120   65.636  1.000 32.370  ? 45  PRO CCC CG  1 
ATOM 4155  C CD  . PRO C 1 28  ? 137.862 8.303   66.870  1.000 31.700  ? 45  PRO CCC CD  1 
ATOM 4156  N N   . GLU C 1 29  ? 136.693 12.537  65.388  1.000 34.750  ? 46  GLU CCC N   1 
ATOM 4157  C CA  . GLU C 1 29  ? 135.507 13.415  65.507  1.000 40.190  ? 46  GLU CCC CA  1 
ATOM 4158  C C   . GLU C 1 29  ? 134.858 13.447  64.128  1.000 39.720  ? 46  GLU CCC C   1 
ATOM 4159  O O   . GLU C 1 29  ? 135.402 14.115  63.251  1.000 36.650  ? 46  GLU CCC O   1 
ATOM 4160  C CB  . GLU C 1 29  ? 135.900 14.774  66.078  1.000 44.580  ? 46  GLU CCC CB  1 
ATOM 4161  C CG  . GLU C 1 29  ? 136.814 14.683  67.283  1.000 47.790  ? 46  GLU CCC CG  1 
ATOM 4162  C CD  . GLU C 1 29  ? 136.134 14.249  68.569  1.000 49.340  ? 46  GLU CCC CD  1 
ATOM 4163  O OE1 . GLU C 1 29  ? 136.852 13.868  69.509  1.000 50.930  ? 46  GLU CCC OE1 1 
ATOM 4164  O OE2 . GLU C 1 29  ? 134.892 14.301  68.632  1.000 48.890  ? 46  GLU CCC OE2 1 
ATOM 4165  N N   . MET C 1 30  ? 133.752 12.724  63.946  1.000 39.650  ? 47  MET CCC N   1 
ATOM 4166  C CA  . MET C 1 30  ? 133.173 12.594  62.589  1.000 38.520  ? 47  MET CCC CA  1 
ATOM 4167  C C   . MET C 1 30  ? 131.839 13.321  62.457  1.000 36.540  ? 47  MET CCC C   1 
ATOM 4168  O O   . MET C 1 30  ? 131.266 13.256  61.385  1.000 31.200  ? 47  MET CCC O   1 
ATOM 4169  C CB  . MET C 1 30  ? 132.987 11.126  62.211  1.000 36.810  ? 47  MET CCC CB  1 
ATOM 4170  C CG  . MET C 1 30  ? 134.241 10.312  62.306  1.000 34.460  ? 47  MET CCC CG  1 
ATOM 4171  S SD  . MET C 1 30  ? 135.190 10.452  60.794  1.000 28.530  ? 47  MET CCC SD  1 
ATOM 4172  C CE  . MET C 1 30  ? 136.736 11.080  61.444  1.000 31.650  ? 47  MET CCC CE  1 
ATOM 4173  N N   . GLY C 1 31  ? 131.393 14.025  63.491  1.000 38.740  ? 48  GLY CCC N   1 
ATOM 4174  C CA  . GLY C 1 31  ? 130.091 14.708  63.459  1.000 42.850  ? 48  GLY CCC CA  1 
ATOM 4175  C C   . GLY C 1 31  ? 129.311 14.390  64.710  1.000 47.880  ? 48  GLY CCC C   1 
ATOM 4176  O O   . GLY C 1 31  ? 128.644 15.293  65.217  1.000 47.190  ? 48  GLY CCC O   1 
ATOM 4177  N N   . ASP C 1 32  ? 129.424 13.156  65.197  1.000 54.200  ? 49  ASP CCC N   1 
ATOM 4178  C CA  . ASP C 1 32  ? 128.745 12.704  66.440  1.000 49.370  ? 49  ASP CCC CA  1 
ATOM 4179  C C   . ASP C 1 32  ? 127.316 13.220  66.476  1.000 41.230  ? 49  ASP CCC C   1 
ATOM 4180  O O   . ASP C 1 32  ? 127.016 14.101  67.295  1.000 32.670  ? 49  ASP CCC O   1 
ATOM 4181  C CB  . ASP C 1 32  ? 129.599 12.948  67.685  1.000 57.550  ? 49  ASP CCC CB  1 
ATOM 4182  C CG  . ASP C 1 32  ? 131.006 12.384  67.580  1.000 63.650  ? 49  ASP CCC CG  1 
ATOM 4183  O OD1 . ASP C 1 32  ? 131.249 11.560  66.679  1.000 62.270  ? 49  ASP CCC OD1 1 
ATOM 4184  O OD2 . ASP C 1 32  ? 131.848 12.774  68.404  1.000 56.870  ? 49  ASP CCC OD2 1 
ATOM 4185  N N   . PRO C 1 33  ? 126.415 12.628  65.674  1.000 43.930  ? 50  PRO CCC N   1 
ATOM 4186  C CA  . PRO C 1 33  ? 125.052 13.107  65.597  1.000 47.610  ? 50  PRO CCC CA  1 
ATOM 4187  C C   . PRO C 1 33  ? 124.316 13.151  66.939  1.000 51.350  ? 50  PRO CCC C   1 
ATOM 4188  O O   . PRO C 1 33  ? 123.920 14.217  67.345  1.000 64.280  ? 50  PRO CCC O   1 
ATOM 4189  C CB  . PRO C 1 33  ? 124.361 12.116  64.665  1.000 44.530  ? 50  PRO CCC CB  1 
ATOM 4190  C CG  . PRO C 1 33  ? 125.444 11.309  64.015  1.000 42.400  ? 50  PRO CCC CG  1 
ATOM 4191  C CD  . PRO C 1 33  ? 126.671 11.441  64.878  1.000 40.960  ? 50  PRO CCC CD  1 
ATOM 4192  N N   . ASP C 1 34  ? 124.162 12.001  67.595  1.000 45.540  ? 51  ASP CCC N   1 
ATOM 4193  C CA  . ASP C 1 34  ? 123.411 11.948  68.861  1.000 38.710  ? 51  ASP CCC CA  1 
ATOM 4194  C C   . ASP C 1 34  ? 124.185 11.152  69.896  1.000 35.500  ? 51  ASP CCC C   1 
ATOM 4195  O O   . ASP C 1 34  ? 125.288 10.716  69.553  1.000 31.910  ? 51  ASP CCC O   1 
ATOM 4196  C CB  . ASP C 1 34  ? 121.920 11.675  68.637  1.000 36.780  ? 51  ASP CCC CB  1 
ATOM 4197  C CG  . ASP C 1 34  ? 121.563 10.324  68.061  1.000 35.990  ? 51  ASP CCC CG  1 
ATOM 4198  O OD1 . ASP C 1 34  ? 122.452 9.492   67.974  1.000 32.540  ? 51  ASP CCC OD1 1 
ATOM 4199  O OD2 . ASP C 1 34  ? 120.395 10.139  67.684  1.000 38.310  ? 51  ASP CCC OD2 1 
ATOM 4200  N N   . GLU C 1 35  ? 123.668 11.039  71.120  1.000 32.990  ? 52  GLU CCC N   1 
ATOM 4201  C CA  . GLU C 1 35  ? 124.340 10.297  72.221  1.000 31.420  ? 52  GLU CCC CA  1 
ATOM 4202  C C   . GLU C 1 35  ? 124.849 8.887   71.904  1.000 29.660  ? 52  GLU CCC C   1 
ATOM 4203  O O   . GLU C 1 35  ? 125.676 8.370   72.678  1.000 28.330  ? 52  GLU CCC O   1 
ATOM 4204  C CB  . GLU C 1 35  ? 123.453 10.321  73.466  1.000 31.670  ? 52  GLU CCC CB  1 
ATOM 4205  C CG  . GLU C 1 35  ? 122.162 9.544   73.392  1.000 33.670  ? 52  GLU CCC CG  1 
ATOM 4206  C CD  . GLU C 1 35  ? 121.355 9.585   74.702  1.000 35.670  ? 52  GLU CCC CD  1 
ATOM 4207  O OE1 . GLU C 1 35  ? 121.961 9.688   75.783  1.000 33.890  ? 52  GLU CCC OE1 1 
ATOM 4208  O OE2 . GLU C 1 35  ? 120.125 9.490   74.641  1.000 39.170  ? 52  GLU CCC OE2 1 
ATOM 4209  N N   . HIS C 1 36  ? 124.402 8.302   70.797  1.000 30.120  ? 53  HIS CCC N   1 
ATOM 4210  C CA  . HIS C 1 36  ? 124.516 6.851   70.504  1.000 29.950  ? 53  HIS CCC CA  1 
ATOM 4211  C C   . HIS C 1 36  ? 125.402 6.536   69.288  1.000 28.970  ? 53  HIS CCC C   1 
ATOM 4212  O O   . HIS C 1 36  ? 125.544 5.328   68.958  1.000 26.440  ? 53  HIS CCC O   1 
ATOM 4213  C CB  . HIS C 1 36  ? 123.104 6.340   70.249  1.000 32.450  ? 53  HIS CCC CB  1 
ATOM 4214  C CG  . HIS C 1 36  ? 122.264 6.212   71.472  1.000 34.360  ? 53  HIS CCC CG  1 
ATOM 4215  N ND1 . HIS C 1 36  ? 122.614 5.382   72.526  1.000 33.140  ? 53  HIS CCC ND1 1 
ATOM 4216  C CD2 . HIS C 1 36  ? 121.051 6.742   71.763  1.000 37.770  ? 53  HIS CCC CD2 1 
ATOM 4217  C CE1 . HIS C 1 36  ? 121.650 5.425   73.422  1.000 39.510  ? 53  HIS CCC CE1 1 
ATOM 4218  N NE2 . HIS C 1 36  ? 120.669 6.249   72.975  1.000 39.230  ? 53  HIS CCC NE2 1 
ATOM 4219  N N   . LEU C 1 37  ? 125.943 7.563   68.626  1.000 30.170  ? 54  LEU CCC N   1 
ATOM 4220  C CA  . LEU C 1 37  ? 126.555 7.448   67.273  1.000 30.440  ? 54  LEU CCC CA  1 
ATOM 4221  C C   . LEU C 1 37  ? 127.944 8.088   67.247  1.000 31.090  ? 54  LEU CCC C   1 
ATOM 4222  O O   . LEU C 1 37  ? 128.374 8.542   66.165  1.000 29.720  ? 54  LEU CCC O   1 
ATOM 4223  C CB  . LEU C 1 37  ? 125.630 8.106   66.250  1.000 30.610  ? 54  LEU CCC CB  1 
ATOM 4224  C CG  . LEU C 1 37  ? 124.313 7.372   66.004  1.000 31.610  ? 54  LEU CCC CG  1 
ATOM 4225  C CD1 . LEU C 1 37  ? 123.444 8.195   65.061  1.000 32.600  ? 54  LEU CCC CD1 1 
ATOM 4226  C CD2 . LEU C 1 37  ? 124.538 5.961   65.456  1.000 29.830  ? 54  LEU CCC CD2 1 
ATOM 4227  N N   . ARG C 1 38  ? 128.646 8.070   68.377  1.000 33.020  ? 55  ARG CCC N   1 
ATOM 4228  C CA  . ARG C 1 38  ? 130.058 8.520   68.454  1.000 34.570  ? 55  ARG CCC CA  1 
ATOM 4229  C C   . ARG C 1 38  ? 130.870 7.706   67.441  1.000 31.630  ? 55  ARG CCC C   1 
ATOM 4230  O O   . ARG C 1 38  ? 130.780 6.481   67.466  1.000 29.770  ? 55  ARG CCC O   1 
ATOM 4231  C CB  . ARG C 1 38  ? 130.557 8.335   69.885  1.000 38.570  ? 55  ARG CCC CB  1 
ATOM 4232  C CG  . ARG C 1 38  ? 131.979 8.806   70.112  1.000 42.420  ? 55  ARG CCC CG  1 
ATOM 4233  C CD  . ARG C 1 38  ? 132.050 10.049  70.972  1.000 45.710  ? 55  ARG CCC CD  1 
ATOM 4234  N NE  . ARG C 1 38  ? 133.442 10.223  71.364  1.000 51.420  ? 55  ARG CCC NE  1 
ATOM 4235  C CZ  . ARG C 1 38  ? 134.425 10.662  70.556  1.000 53.200  ? 55  ARG CCC CZ  1 
ATOM 4236  N NH1 . ARG C 1 38  ? 134.185 11.021  69.296  1.000 44.520  ? 55  ARG CCC NH1 1 
ATOM 4237  N NH2 . ARG C 1 38  ? 135.655 10.768  71.039  1.000 57.110  ? 55  ARG CCC NH2 1 
ATOM 4238  N N   . GLY C 1 39  ? 131.599 8.373   66.551  1.000 34.040  ? 56  GLY CCC N   1 
ATOM 4239  C CA  . GLY C 1 39  ? 132.415 7.716   65.513  1.000 33.660  ? 56  GLY CCC CA  1 
ATOM 4240  C C   . GLY C 1 39  ? 131.690 7.678   64.179  1.000 33.410  ? 56  GLY CCC C   1 
ATOM 4241  O O   . GLY C 1 39  ? 132.279 7.199   63.192  1.000 32.290  ? 56  GLY CCC O   1 
ATOM 4242  N N   . PHE C 1 40  ? 130.448 8.160   64.133  1.000 31.080  ? 57  PHE CCC N   1 
ATOM 4243  C CA  . PHE C 1 40  ? 129.705 8.326   62.870  1.000 29.210  ? 57  PHE CCC CA  1 
ATOM 4244  C C   . PHE C 1 40  ? 129.509 9.813   62.608  1.000 26.420  ? 57  PHE CCC C   1 
ATOM 4245  O O   . PHE C 1 40  ? 129.704 10.617  63.502  1.000 25.450  ? 57  PHE CCC O   1 
ATOM 4246  C CB  . PHE C 1 40  ? 128.355 7.611   62.931  1.000 30.070  ? 57  PHE CCC CB  1 
ATOM 4247  C CG  . PHE C 1 40  ? 128.431 6.117   63.122  1.000 31.730  ? 57  PHE CCC CG  1 
ATOM 4248  C CD1 . PHE C 1 40  ? 128.774 5.580   64.357  1.000 32.460  ? 57  PHE CCC CD1 1 
ATOM 4249  C CD2 . PHE C 1 40  ? 128.180 5.241   62.074  1.000 29.930  ? 57  PHE CCC CD2 1 
ATOM 4250  C CE1 . PHE C 1 40  ? 128.846 4.204   64.539  1.000 30.710  ? 57  PHE CCC CE1 1 
ATOM 4251  C CE2 . PHE C 1 40  ? 128.248 3.869   62.266  1.000 28.390  ? 57  PHE CCC CE2 1 
ATOM 4252  C CZ  . PHE C 1 40  ? 128.575 3.351   63.493  1.000 28.810  ? 57  PHE CCC CZ  1 
ATOM 4253  N N   . SER C 1 41  ? 129.137 10.139  61.381  1.000 26.150  ? 58  SER CCC N   1 
ATOM 4254  C CA  . SER C 1 41  ? 128.534 11.439  61.010  1.000 25.610  ? 58  SER CCC CA  1 
ATOM 4255  C C   . SER C 1 41  ? 127.040 11.247  60.961  1.000 23.310  ? 58  SER CCC C   1 
ATOM 4256  O O   . SER C 1 41  ? 126.599 10.102  61.083  1.000 22.120  ? 58  SER CCC O   1 
ATOM 4257  C CB  . SER C 1 41  ? 129.039 11.953  59.679  1.000 25.080  ? 58  SER CCC CB  1 
ATOM 4258  O OG  . SER C 1 41  ? 128.444 11.265  58.604  1.000 22.420  ? 58  SER CCC OG  1 
ATOM 4259  N N   . LYS C 1 42  ? 126.324 12.342  60.786  1.000 24.410  ? 59  LYS CCC N   1 
ATOM 4260  C CA  . LYS C 1 42  ? 124.871 12.329  60.547  1.000 26.550  ? 59  LYS CCC CA  1 
ATOM 4261  C C   . LYS C 1 42  ? 124.710 11.878  59.107  1.000 26.250  ? 59  LYS CCC C   1 
ATOM 4262  O O   . LYS C 1 42  ? 125.600 12.150  58.282  1.000 22.740  ? 59  LYS CCC O   1 
ATOM 4263  C CB  . LYS C 1 42  ? 124.237 13.696  60.789  1.000 30.550  ? 59  LYS CCC CB  1 
ATOM 4264  C CG  . LYS C 1 42  ? 122.728 13.744  60.565  1.000 37.840  ? 59  LYS CCC CG  1 
ATOM 4265  C CD  . LYS C 1 42  ? 121.946 14.835  61.319  1.000 40.310  ? 59  LYS CCC CD  1 
ATOM 4266  C CE  . LYS C 1 42  ? 121.717 16.089  60.501  1.000 43.480  ? 59  LYS CCC CE  1 
ATOM 4267  N NZ  . LYS C 1 42  ? 120.538 16.842  60.993  1.000 44.840  ? 59  LYS CCC NZ  1 
ATOM 4268  N N   . SER C 1 43  ? 123.622 11.177  58.836  1.000 27.800  ? 60  SER CCC N   1 
ATOM 4269  C CA  . SER C 1 43  ? 123.280 10.740  57.470  1.000 29.100  ? 60  SER CCC CA  1 
ATOM 4270  C C   . SER C 1 43  ? 123.371 11.949  56.536  1.000 24.310  ? 60  SER CCC C   1 
ATOM 4271  O O   . SER C 1 43  ? 122.706 12.975  56.797  1.000 23.590  ? 60  SER CCC O   1 
ATOM 4272  C CB  . SER C 1 43  ? 121.940 10.047  57.448  1.000 35.160  ? 60  SER CCC CB  1 
ATOM 4273  O OG  . SER C 1 43  ? 122.036 8.737   58.028  1.000 40.040  ? 60  SER CCC OG  1 
ATOM 4274  N N   . ILE C 1 44  ? 124.208 11.809  55.506  1.000 20.340  ? 61  ILE CCC N   1 
ATOM 4275  C CA  . ILE C 1 44  ? 124.642 12.871  54.560  1.000 17.930  ? 61  ILE CCC CA  1 
ATOM 4276  C C   . ILE C 1 44  ? 123.478 13.294  53.695  1.000 16.600  ? 61  ILE CCC C   1 
ATOM 4277  O O   . ILE C 1 44  ? 122.799 12.423  53.225  1.000 15.810  ? 61  ILE CCC O   1 
ATOM 4278  C CB  . ILE C 1 44  ? 125.810 12.361  53.717  1.000 17.050  ? 61  ILE CCC CB  1 
ATOM 4279  C CG1 . ILE C 1 44  ? 127.009 12.062  54.620  1.000 17.990  ? 61  ILE CCC CG1 1 
ATOM 4280  C CG2 . ILE C 1 44  ? 126.136 13.349  52.619  1.000 16.810  ? 61  ILE CCC CG2 1 
ATOM 4281  C CD1 . ILE C 1 44  ? 128.235 11.566  53.904  1.000 19.120  ? 61  ILE CCC CD1 1 
ATOM 4282  N N   . SER C 1 45  ? 123.262 14.590  53.526  1.000 18.230  ? 62  SER CCC N   1 
ATOM 4283  C CA  . SER C 1 45  ? 122.225 15.128  52.602  1.000 20.700  ? 62  SER CCC CA  1 
ATOM 4284  C C   . SER C 1 45  ? 122.959 15.932  51.540  1.000 23.420  ? 62  SER CCC C   1 
ATOM 4285  O O   . SER C 1 45  ? 124.121 16.299  51.804  1.000 25.550  ? 62  SER CCC O   1 
ATOM 4286  C CB  . SER C 1 45  ? 121.156 15.958  53.291  1.000 19.980  ? 62  SER CCC CB  1 
ATOM 4287  O OG  . SER C 1 45  ? 121.105 15.705  54.689  1.000 20.150  ? 62  SER CCC OG  1 
ATOM 4288  N N   . ILE C 1 46  ? 122.289 16.214  50.427  1.000 26.760  ? 63  ILE CCC N   1 
ATOM 4289  C CA  . ILE C 1 46  ? 122.890 16.959  49.282  1.000 30.030  ? 63  ILE CCC CA  1 
ATOM 4290  C C   . ILE C 1 46  ? 122.121 18.259  49.036  1.000 33.630  ? 63  ILE CCC C   1 
ATOM 4291  O O   . ILE C 1 46  ? 120.878 18.229  48.920  1.000 37.490  ? 63  ILE CCC O   1 
ATOM 4292  C CB  . ILE C 1 46  ? 122.888 16.077  48.033  1.000 30.900  ? 63  ILE CCC CB  1 
ATOM 4293  C CG1 . ILE C 1 46  ? 123.727 14.809  48.220  1.000 31.430  ? 63  ILE CCC CG1 1 
ATOM 4294  C CG2 . ILE C 1 46  ? 123.333 16.898  46.836  1.000 32.700  ? 63  ILE CCC CG2 1 
ATOM 4295  C CD1 . ILE C 1 46  ? 123.668 13.842  47.041  1.000 31.410  ? 63  ILE CCC CD1 1 
ATOM 4296  N N   . SER C 1 47  ? 122.834 19.371  48.891  1.000 35.670  ? 64  SER CCC N   1 
ATOM 4297  C CA  . SER C 1 47  ? 122.206 20.703  48.716  1.000 36.720  ? 64  SER CCC CA  1 
ATOM 4298  C C   . SER C 1 47  ? 121.192 20.677  47.565  1.000 35.780  ? 64  SER CCC C   1 
ATOM 4299  O O   . SER C 1 47  ? 121.358 19.924  46.596  1.000 29.090  ? 64  SER CCC O   1 
ATOM 4300  C CB  . SER C 1 47  ? 123.238 21.780  48.525  1.000 36.870  ? 64  SER CCC CB  1 
ATOM 4301  O OG  . SER C 1 47  ? 124.223 21.381  47.586  1.000 38.790  ? 64  SER CCC OG  1 
ATOM 4302  N N   . ASP C 1 48  ? 120.144 21.481  47.730  1.000 43.260  ? 65  ASP CCC N   1 
ATOM 4303  C CA  . ASP C 1 48  ? 119.069 21.730  46.738  1.000 43.890  ? 65  ASP CCC CA  1 
ATOM 4304  C C   . ASP C 1 48  ? 119.732 22.303  45.473  1.000 38.910  ? 65  ASP CCC C   1 
ATOM 4305  O O   . ASP C 1 48  ? 119.207 22.039  44.385  1.000 41.140  ? 65  ASP CCC O   1 
ATOM 4306  C CB  . ASP C 1 48  ? 117.948 22.596  47.353  1.000 52.130  ? 65  ASP CCC CB  1 
ATOM 4307  C CG  . ASP C 1 48  ? 118.377 23.975  47.912  1.000 63.960  ? 65  ASP CCC CG  1 
ATOM 4308  O OD1 . ASP C 1 48  ? 119.165 24.025  48.907  1.000 60.000  ? 65  ASP CCC OD1 1 
ATOM 4309  O OD2 . ASP C 1 48  ? 117.931 25.024  47.364  1.000 65.350  ? 65  ASP CCC OD2 1 
ATOM 4310  N N   . THR C 1 49  ? 120.850 23.032  45.591  1.000 33.550  ? 66  THR CCC N   1 
ATOM 4311  C CA  . THR C 1 49  ? 121.543 23.726  44.472  1.000 32.720  ? 66  THR CCC CA  1 
ATOM 4312  C C   . THR C 1 49  ? 123.035 23.873  44.764  1.000 31.140  ? 66  THR CCC C   1 
ATOM 4313  O O   . THR C 1 49  ? 123.428 23.839  45.932  1.000 27.920  ? 66  THR CCC O   1 
ATOM 4314  C CB  . THR C 1 49  ? 121.017 25.157  44.267  1.000 34.900  ? 66  THR CCC CB  1 
ATOM 4315  O OG1 . THR C 1 49  ? 121.382 25.937  45.409  1.000 31.440  ? 66  THR CCC OG1 1 
ATOM 4316  C CG2 . THR C 1 49  ? 119.515 25.254  44.104  1.000 35.610  ? 66  THR CCC CG2 1 
ATOM 4317  N N   . PHE C 1 50  ? 123.844 24.087  43.737  1.000 32.420  ? 67  PHE CCC N   1 
ATOM 4318  C CA  . PHE C 1 50  ? 125.325 24.144  43.891  1.000 31.590  ? 67  PHE CCC CA  1 
ATOM 4319  C C   . PHE C 1 50  ? 125.675 25.352  44.754  1.000 31.330  ? 67  PHE CCC C   1 
ATOM 4320  O O   . PHE C 1 50  ? 126.699 25.337  45.455  1.000 31.350  ? 67  PHE CCC O   1 
ATOM 4321  C CB  . PHE C 1 50  ? 126.015 24.242  42.527  1.000 31.110  ? 67  PHE CCC CB  1 
ATOM 4322  C CG  . PHE C 1 50  ? 127.511 24.103  42.562  1.000 27.450  ? 67  PHE CCC CG  1 
ATOM 4323  C CD1 . PHE C 1 50  ? 128.087 22.888  42.822  1.000 28.030  ? 67  PHE CCC CD1 1 
ATOM 4324  C CD2 . PHE C 1 50  ? 128.341 25.176  42.325  1.000 27.380  ? 67  PHE CCC CD2 1 
ATOM 4325  C CE1 . PHE C 1 50  ? 129.468 22.747  42.843  1.000 28.660  ? 67  PHE CCC CE1 1 
ATOM 4326  C CE2 . PHE C 1 50  ? 129.718 25.041  42.358  1.000 26.450  ? 67  PHE CCC CE2 1 
ATOM 4327  C CZ  . PHE C 1 50  ? 130.280 23.827  42.604  1.000 26.550  ? 67  PHE CCC CZ  1 
ATOM 4328  N N   . GLU C 1 51  ? 124.825 26.373  44.667  1.000 32.710  ? 68  GLU CCC N   1 
ATOM 4329  C CA  . GLU C 1 51  ? 125.036 27.720  45.241  1.000 33.650  ? 68  GLU CCC CA  1 
ATOM 4330  C C   . GLU C 1 51  ? 124.723 27.668  46.737  1.000 33.960  ? 68  GLU CCC C   1 
ATOM 4331  O O   . GLU C 1 51  ? 125.348 28.420  47.460  1.000 35.650  ? 68  GLU CCC O   1 
ATOM 4332  C CB  . GLU C 1 51  ? 124.157 28.730  44.503  1.000 32.880  ? 68  GLU CCC CB  1 
ATOM 4333  C CG  . GLU C 1 51  ? 124.572 28.935  43.062  1.000 32.220  ? 68  GLU CCC CG  1 
ATOM 4334  C CD  . GLU C 1 51  ? 123.832 28.160  41.988  1.000 34.390  ? 68  GLU CCC CD  1 
ATOM 4335  O OE1 . GLU C 1 51  ? 123.723 28.730  40.891  1.000 33.280  ? 68  GLU CCC OE1 1 
ATOM 4336  O OE2 . GLU C 1 51  ? 123.407 26.971  42.217  1.000 40.610  ? 68  GLU CCC OE2 1 
ATOM 4337  N N   . SER C 1 52  ? 123.816 26.785  47.161  1.000 32.940  ? 69  SER CCC N   1 
ATOM 4338  C CA  . SER C 1 52  ? 123.244 26.756  48.528  1.000 34.970  ? 69  SER CCC CA  1 
ATOM 4339  C C   . SER C 1 52  ? 123.877 25.662  49.394  1.000 36.030  ? 69  SER CCC C   1 
ATOM 4340  O O   . SER C 1 52  ? 123.300 25.336  50.436  1.000 37.490  ? 69  SER CCC O   1 
ATOM 4341  C CB  . SER C 1 52  ? 121.736 26.594  48.456  1.000 37.350  ? 69  SER CCC CB  1 
ATOM 4342  O OG  . SER C 1 52  ? 121.359 25.350  47.894  1.000 39.500  ? 69  SER CCC OG  1 
ATOM 4343  N N   . ASP C 1 53  ? 124.994 25.072  48.977  1.000 37.850  ? 70  ASP CCC N   1 
ATOM 4344  C CA  . ASP C 1 53  ? 125.709 24.043  49.789  1.000 34.930  ? 70  ASP CCC CA  1 
ATOM 4345  C C   . ASP C 1 53  ? 125.911 24.614  51.189  1.000 35.510  ? 70  ASP CCC C   1 
ATOM 4346  O O   . ASP C 1 53  ? 126.489 25.702  51.267  1.000 39.010  ? 70  ASP CCC O   1 
ATOM 4347  C CB  . ASP C 1 53  ? 127.054 23.677  49.163  1.000 33.200  ? 70  ASP CCC CB  1 
ATOM 4348  C CG  . ASP C 1 53  ? 127.703 22.456  49.792  1.000 32.060  ? 70  ASP CCC CG  1 
ATOM 4349  O OD1 . ASP C 1 53  ? 126.994 21.451  50.008  1.000 29.720  ? 70  ASP CCC OD1 1 
ATOM 4350  O OD2 . ASP C 1 53  ? 128.915 22.514  50.039  1.000 31.770  ? 70  ASP CCC OD2 1 
ATOM 4351  N N   . SER C 1 54  ? 125.385 23.961  52.232  1.000 39.360  ? 71  SER CCC N   1 
ATOM 4352  C CA  . SER C 1 54  ? 125.612 24.387  53.640  1.000 44.490  ? 71  SER CCC CA  1 
ATOM 4353  C C   . SER C 1 54  ? 125.468 23.220  54.612  1.000 42.390  ? 71  SER CCC C   1 
ATOM 4354  O O   . SER C 1 54  ? 124.501 23.135  55.356  1.000 37.890  ? 71  SER CCC O   1 
ATOM 4355  C CB  . SER C 1 54  ? 124.721 25.547  54.013  1.000 49.690  ? 71  SER CCC CB  1 
ATOM 4356  O OG  . SER C 1 54  ? 123.377 25.309  53.584  1.000 48.130  ? 71  SER CCC OG  1 
ATOM 4357  N N   . PRO C 1 55  ? 126.493 22.353  54.705  1.000 42.410  ? 72  PRO CCC N   1 
ATOM 4358  C CA  . PRO C 1 55  ? 126.434 21.176  55.566  1.000 43.260  ? 72  PRO CCC CA  1 
ATOM 4359  C C   . PRO C 1 55  ? 126.273 21.516  57.053  1.000 43.700  ? 72  PRO CCC C   1 
ATOM 4360  O O   . PRO C 1 55  ? 126.976 22.410  57.492  1.000 40.330  ? 72  PRO CCC O   1 
ATOM 4361  C CB  . PRO C 1 55  ? 127.830 20.566  55.369  1.000 44.210  ? 72  PRO CCC CB  1 
ATOM 4362  C CG  . PRO C 1 55  ? 128.694 21.760  55.048  1.000 42.410  ? 72  PRO CCC CG  1 
ATOM 4363  C CD  . PRO C 1 55  ? 127.819 22.535  54.088  1.000 42.450  ? 72  PRO CCC CD  1 
ATOM 4364  N N   . ASN C 1 56  ? 125.389 20.797  57.768  1.000 45.660  ? 73  ASN CCC N   1 
ATOM 4365  C CA  . ASN C 1 56  ? 125.246 20.877  59.251  1.000 46.160  ? 73  ASN CCC CA  1 
ATOM 4366  C C   . ASN C 1 56  ? 126.556 20.427  59.896  1.000 38.770  ? 73  ASN CCC C   1 
ATOM 4367  O O   . ASN C 1 56  ? 127.251 19.635  59.303  1.000 35.320  ? 73  ASN CCC O   1 
ATOM 4368  C CB  . ASN C 1 56  ? 124.114 20.011  59.801  1.000 48.160  ? 73  ASN CCC CB  1 
ATOM 4369  C CG  . ASN C 1 56  ? 122.731 20.507  59.442  1.000 53.240  ? 73  ASN CCC CG  1 
ATOM 4370  O OD1 . ASN C 1 56  ? 122.575 21.384  58.579  1.000 50.870  ? 73  ASN CCC OD1 1 
ATOM 4371  N ND2 . ASN C 1 56  ? 121.722 19.953  60.120  1.000 50.530  ? 73  ASN CCC ND2 1 
ATOM 4372  N N   . ARG C 1 57  ? 126.854 20.895  61.095  1.000 37.950  ? 74  ARG CCC N   1 
ATOM 4373  C CA  . ARG C 1 57  ? 128.151 20.625  61.767  1.000 40.660  ? 74  ARG CCC CA  1 
ATOM 4374  C C   . ARG C 1 57  ? 128.323 19.126  62.050  1.000 41.590  ? 74  ARG CCC C   1 
ATOM 4375  O O   . ARG C 1 57  ? 129.494 18.657  62.103  1.000 40.790  ? 74  ARG CCC O   1 
ATOM 4376  C CB  . ARG C 1 57  ? 128.215 21.424  63.066  1.000 42.530  ? 74  ARG CCC CB  1 
ATOM 4377  C CG  . ARG C 1 57  ? 129.510 21.240  63.837  1.000 42.040  ? 74  ARG CCC CG  1 
ATOM 4378  C CD  . ARG C 1 57  ? 129.489 22.032  65.119  1.000 45.350  ? 74  ARG CCC CD  1 
ATOM 4379  N NE  . ARG C 1 57  ? 130.771 21.837  65.784  1.000 50.430  ? 74  ARG CCC NE  1 
ATOM 4380  C CZ  . ARG C 1 57  ? 130.976 21.999  67.077  1.000 51.970  ? 74  ARG CCC CZ  1 
ATOM 4381  N NH1 . ARG C 1 57  ? 129.972 22.311  67.867  1.000 55.580  ? 74  ARG CCC NH1 1 
ATOM 4382  N NH2 . ARG C 1 57  ? 132.176 21.820  67.580  1.000 57.610  ? 74  ARG CCC NH2 1 
ATOM 4383  N N   . ASP C 1 58  ? 127.219 18.400  62.239  1.000 44.250  ? 75  ASP CCC N   1 
ATOM 4384  C CA  . ASP C 1 58  ? 127.235 16.954  62.597  1.000 44.570  ? 75  ASP CCC CA  1 
ATOM 4385  C C   . ASP C 1 58  ? 127.352 16.094  61.329  1.000 39.550  ? 75  ASP CCC C   1 
ATOM 4386  O O   . ASP C 1 58  ? 127.337 14.861  61.452  1.000 42.940  ? 75  ASP CCC O   1 
ATOM 4387  C CB  . ASP C 1 58  ? 126.011 16.577  63.457  1.000 49.520  ? 75  ASP CCC CB  1 
ATOM 4388  C CG  . ASP C 1 58  ? 124.680 17.083  62.950  1.000 56.890  ? 75  ASP CCC CG  1 
ATOM 4389  O OD1 . ASP C 1 58  ? 124.616 17.563  61.790  1.000 55.950  ? 75  ASP CCC OD1 1 
ATOM 4390  O OD2 . ASP C 1 58  ? 123.699 17.027  63.749  1.000 67.180  ? 75  ASP CCC OD2 1 
ATOM 4391  N N   . MET C 1 59  ? 127.496 16.707  60.158  1.000 32.730  ? 76  MET CCC N   1 
ATOM 4392  C CA  . MET C 1 59  ? 127.739 15.998  58.879  1.000 28.160  ? 76  MET CCC CA  1 
ATOM 4393  C C   . MET C 1 59  ? 129.201 16.157  58.443  1.000 25.870  ? 76  MET CCC C   1 
ATOM 4394  O O   . MET C 1 59  ? 129.560 15.644  57.358  1.000 27.540  ? 76  MET CCC O   1 
ATOM 4395  C CB  . MET C 1 59  ? 126.827 16.563  57.794  1.000 27.130  ? 76  MET CCC CB  1 
ATOM 4396  C CG  . MET C 1 59  ? 126.579 15.600  56.685  1.000 26.410  ? 76  MET CCC CG  1 
ATOM 4397  S SD  . MET C 1 59  ? 125.753 16.349  55.301  1.000 28.700  ? 76  MET CCC SD  1 
ATOM 4398  C CE  . MET C 1 59  ? 127.149 17.129  54.502  1.000 30.530  ? 76  MET CCC CE  1 
ATOM 4399  N N   . LEU C 1 60  ? 130.015 16.842  59.238  1.000 26.070  ? 77  LEU CCC N   1 
ATOM 4400  C CA  . LEU C 1 60  ? 131.388 17.255  58.865  1.000 29.250  ? 77  LEU CCC CA  1 
ATOM 4401  C C   . LEU C 1 60  ? 132.399 16.618  59.810  1.000 29.900  ? 77  LEU CCC C   1 
ATOM 4402  O O   . LEU C 1 60  ? 132.603 17.064  60.941  1.000 27.040  ? 77  LEU CCC O   1 
ATOM 4403  C CB  . LEU C 1 60  ? 131.510 18.779  58.914  1.000 31.450  ? 77  LEU CCC CB  1 
ATOM 4404  C CG  . LEU C 1 60  ? 130.767 19.549  57.818  1.000 33.160  ? 77  LEU CCC CG  1 
ATOM 4405  C CD1 . LEU C 1 60  ? 131.004 21.053  57.954  1.000 34.680  ? 77  LEU CCC CD1 1 
ATOM 4406  C CD2 . LEU C 1 60  ? 131.192 19.102  56.428  1.000 34.050  ? 77  LEU CCC CD2 1 
ATOM 4407  N N   . PRO C 1 61  ? 133.079 15.547  59.357  1.000 29.940  ? 78  PRO CCC N   1 
ATOM 4408  C CA  . PRO C 1 61  ? 134.302 15.094  60.015  1.000 29.480  ? 78  PRO CCC CA  1 
ATOM 4409  C C   . PRO C 1 61  ? 135.295 16.241  60.185  1.000 27.390  ? 78  PRO CCC C   1 
ATOM 4410  O O   . PRO C 1 61  ? 135.321 17.093  59.311  1.000 27.710  ? 78  PRO CCC O   1 
ATOM 4411  C CB  . PRO C 1 61  ? 134.878 14.055  59.049  1.000 29.180  ? 78  PRO CCC CB  1 
ATOM 4412  C CG  . PRO C 1 61  ? 133.662 13.540  58.282  1.000 29.900  ? 78  PRO CCC CG  1 
ATOM 4413  C CD  . PRO C 1 61  ? 132.667 14.680  58.247  1.000 28.960  ? 78  PRO CCC CD  1 
ATOM 4414  N N   . CYS C 1 62  ? 136.089 16.187  61.256  1.000 26.530  ? 79  CYS CCC N   1 
ATOM 4415  C CA  . CYS C 1 62  ? 137.116 17.199  61.608  1.000 26.850  ? 79  CYS CCC CA  1 
ATOM 4416  C C   . CYS C 1 62  ? 138.454 16.556  61.976  1.000 24.890  ? 79  CYS CCC C   1 
ATOM 4417  O O   . CYS C 1 62  ? 138.468 15.438  62.540  1.000 28.150  ? 79  CYS CCC O   1 
ATOM 4418  C CB  . CYS C 1 62  ? 136.679 18.001  62.822  1.000 28.700  ? 79  CYS CCC CB  1 
ATOM 4419  S SG  . CYS C 1 62  ? 135.128 18.869  62.555  1.000 36.410  ? 79  CYS CCC SG  1 
ATOM 4420  N N   . TYR C 1 63  ? 139.534 17.287  61.732  1.000 21.600  ? 80  TYR CCC N   1 
ATOM 4421  C CA  . TYR C 1 63  ? 140.888 16.924  62.192  1.000 21.880  ? 80  TYR CCC CA  1 
ATOM 4422  C C   . TYR C 1 63  ? 140.841 16.777  63.709  1.000 25.410  ? 80  TYR CCC C   1 
ATOM 4423  O O   . TYR C 1 63  ? 140.178 17.595  64.413  1.000 31.000  ? 80  TYR CCC O   1 
ATOM 4424  C CB  . TYR C 1 63  ? 141.911 17.984  61.788  1.000 22.210  ? 80  TYR CCC CB  1 
ATOM 4425  C CG  . TYR C 1 63  ? 142.292 18.034  60.328  1.000 20.670  ? 80  TYR CCC CG  1 
ATOM 4426  C CD1 . TYR C 1 63  ? 141.504 18.686  59.401  1.000 19.350  ? 80  TYR CCC CD1 1 
ATOM 4427  C CD2 . TYR C 1 63  ? 143.454 17.438  59.882  1.000 20.660  ? 80  TYR CCC CD2 1 
ATOM 4428  C CE1 . TYR C 1 63  ? 141.853 18.725  58.068  1.000 19.350  ? 80  TYR CCC CE1 1 
ATOM 4429  C CE2 . TYR C 1 63  ? 143.804 17.439  58.544  1.000 20.470  ? 80  TYR CCC CE2 1 
ATOM 4430  C CZ  . TYR C 1 63  ? 143.001 18.096  57.635  1.000 19.770  ? 80  TYR CCC CZ  1 
ATOM 4431  O OH  . TYR C 1 63  ? 143.378 18.167  56.327  1.000 19.980  ? 80  TYR CCC OH  1 
ATOM 4432  N N   . SER C 1 64  ? 141.499 15.735  64.202  1.000 29.800  ? 81  SER CCC N   1 
ATOM 4433  C CA  . SER C 1 64  ? 141.710 15.463  65.645  1.000 30.170  ? 81  SER CCC CA  1 
ATOM 4434  C C   . SER C 1 64  ? 143.140 15.916  65.959  1.000 29.040  ? 81  SER CCC C   1 
ATOM 4435  O O   . SER C 1 64  ? 144.024 15.702  65.105  1.000 25.620  ? 81  SER CCC O   1 
ATOM 4436  C CB  . SER C 1 64  ? 141.463 13.989  65.986  1.000 31.520  ? 81  SER CCC CB  1 
ATOM 4437  O OG  . SER C 1 64  ? 140.311 13.465  65.309  1.000 33.630  ? 81  SER CCC OG  1 
ATOM 4438  N N   . VAL C 1 65  ? 143.343 16.553  67.116  1.000 29.080  ? 82  VAL CCC N   1 
ATOM 4439  C CA  . VAL C 1 65  ? 144.678 17.024  67.592  1.000 28.630  ? 82  VAL CCC CA  1 
ATOM 4440  C C   . VAL C 1 65  ? 144.825 16.729  69.078  1.000 24.760  ? 82  VAL CCC C   1 
ATOM 4441  O O   . VAL C 1 65  ? 143.811 16.728  69.744  1.000 21.930  ? 82  VAL CCC O   1 
ATOM 4442  C CB  . VAL C 1 65  ? 144.857 18.529  67.333  1.000 32.760  ? 82  VAL CCC CB  1 
ATOM 4443  C CG1 . VAL C 1 65  ? 143.703 19.363  67.894  1.000 30.000  ? 82  VAL CCC CG1 1 
ATOM 4444  C CG2 . VAL C 1 65  ? 146.204 19.020  67.852  1.000 37.070  ? 82  VAL CCC CG2 1 
ATOM 4445  N N   . ALA C 1 66  ? 146.055 16.527  69.546  1.000 24.650  ? 83  ALA CCC N   1 
ATOM 4446  C CA  . ALA C 1 66  ? 146.381 16.234  70.954  1.000 26.470  ? 83  ALA CCC CA  1 
ATOM 4447  C C   . ALA C 1 66  ? 147.732 16.852  71.317  1.000 30.880  ? 83  ALA CCC C   1 
ATOM 4448  O O   . ALA C 1 66  ? 148.725 16.511  70.637  1.000 35.740  ? 83  ALA CCC O   1 
ATOM 4449  C CB  . ALA C 1 66  ? 146.448 14.749  71.151  1.000 26.530  ? 83  ALA CCC CB  1 
ATOM 4450  N N   . ARG C 1 67  ? 147.766 17.742  72.318  1.000 31.330  ? 84  ARG CCC N   1 
ATOM 4451  C CA  . ARG C 1 67  ? 149.022 18.345  72.839  1.000 30.910  ? 84  ARG CCC CA  1 
ATOM 4452  C C   . ARG C 1 67  ? 149.498 17.495  74.014  1.000 29.220  ? 84  ARG CCC C   1 
ATOM 4453  O O   . ARG C 1 67  ? 148.712 17.329  74.930  1.000 28.420  ? 84  ARG CCC O   1 
ATOM 4454  C CB  . ARG C 1 67  ? 148.790 19.812  73.204  1.000 33.700  ? 84  ARG CCC CB  1 
ATOM 4455  C CG  . ARG C 1 67  ? 150.077 20.595  73.429  1.000 39.830  ? 84  ARG CCC CG  1 
ATOM 4456  C CD  . ARG C 1 67  ? 149.869 22.063  73.740  1.000 45.870  ? 84  ARG CCC CD  1 
ATOM 4457  N NE  . ARG C 1 67  ? 149.257 21.994  75.074  1.000 52.260  ? 84  ARG CCC NE  1 
ATOM 4458  C CZ  . ARG C 1 67  ? 148.115 22.563  75.437  1.000 57.930  ? 84  ARG CCC CZ  1 
ATOM 4459  N NH1 . ARG C 1 67  ? 147.462 23.355  74.613  1.000 66.600  ? 84  ARG CCC NH1 1 
ATOM 4460  N NH2 . ARG C 1 67  ? 147.627 22.335  76.638  1.000 59.350  ? 84  ARG CCC NH2 1 
ATOM 4461  N N   . ILE C 1 68  ? 150.690 16.908  73.949  1.000 31.430  ? 85  ILE CCC N   1 
ATOM 4462  C CA  . ILE C 1 68  ? 151.225 16.036  75.037  1.000 34.360  ? 85  ILE CCC CA  1 
ATOM 4463  C C   . ILE C 1 68  ? 152.357 16.782  75.752  1.000 36.830  ? 85  ILE CCC C   1 
ATOM 4464  O O   . ILE C 1 68  ? 153.374 17.105  75.140  1.000 40.150  ? 85  ILE CCC O   1 
ATOM 4465  C CB  . ILE C 1 68  ? 151.734 14.681  74.499  1.000 35.410  ? 85  ILE CCC CB  1 
ATOM 4466  C CG1 . ILE C 1 68  ? 150.817 14.069  73.431  1.000 37.930  ? 85  ILE CCC CG1 1 
ATOM 4467  C CG2 . ILE C 1 68  ? 151.981 13.727  75.659  1.000 34.210  ? 85  ILE CCC CG2 1 
ATOM 4468  C CD1 . ILE C 1 68  ? 149.407 13.770  73.878  1.000 38.030  ? 85  ILE CCC CD1 1 
ATOM 4469  N N   . PRO C 1 69  ? 152.249 17.063  77.074  1.000 35.410  ? 86  PRO CCC N   1 
ATOM 4470  C CA  . PRO C 1 69  ? 153.319 17.740  77.795  1.000 33.000  ? 86  PRO CCC CA  1 
ATOM 4471  C C   . PRO C 1 69  ? 154.426 16.732  78.089  1.000 33.470  ? 86  PRO CCC C   1 
ATOM 4472  O O   . PRO C 1 69  ? 154.111 15.639  78.495  1.000 33.830  ? 86  PRO CCC O   1 
ATOM 4473  C CB  . PRO C 1 69  ? 152.654 18.223  79.080  1.000 35.320  ? 86  PRO CCC CB  1 
ATOM 4474  C CG  . PRO C 1 69  ? 151.172 17.937  78.876  1.000 38.450  ? 86  PRO CCC CG  1 
ATOM 4475  C CD  . PRO C 1 69  ? 151.129 16.734  77.967  1.000 36.200  ? 86  PRO CCC CD  1 
ATOM 4476  N N   . LEU C 1 70  ? 155.673 17.109  77.832  1.000 35.450  ? 87  LEU CCC N   1 
ATOM 4477  C CA  . LEU C 1 70  ? 156.867 16.251  78.042  1.000 36.120  ? 87  LEU CCC CA  1 
ATOM 4478  C C   . LEU C 1 70  ? 157.599 16.680  79.309  1.000 35.650  ? 87  LEU CCC C   1 
ATOM 4479  O O   . LEU C 1 70  ? 157.393 17.778  79.813  1.000 34.440  ? 87  LEU CCC O   1 
ATOM 4480  C CB  . LEU C 1 70  ? 157.769 16.403  76.815  1.000 40.210  ? 87  LEU CCC CB  1 
ATOM 4481  C CG  . LEU C 1 70  ? 157.089 16.094  75.482  1.000 43.380  ? 87  LEU CCC CG  1 
ATOM 4482  C CD1 . LEU C 1 70  ? 157.997 16.467  74.318  1.000 45.640  ? 87  LEU CCC CD1 1 
ATOM 4483  C CD2 . LEU C 1 70  ? 156.687 14.632  75.406  1.000 42.920  ? 87  LEU CCC CD2 1 
ATOM 4484  N N   . PRO C 1 71  ? 158.482 15.826  79.861  1.000 35.880  ? 88  PRO CCC N   1 
ATOM 4485  C CA  . PRO C 1 71  ? 159.365 16.216  80.960  1.000 37.790  ? 88  PRO CCC CA  1 
ATOM 4486  C C   . PRO C 1 71  ? 160.100 17.547  80.746  1.000 38.720  ? 88  PRO CCC C   1 
ATOM 4487  O O   . PRO C 1 71  ? 160.700 17.714  79.727  1.000 33.740  ? 88  PRO CCC O   1 
ATOM 4488  C CB  . PRO C 1 71  ? 160.381 15.068  80.987  1.000 36.960  ? 88  PRO CCC CB  1 
ATOM 4489  C CG  . PRO C 1 71  ? 159.572 13.874  80.561  1.000 38.140  ? 88  PRO CCC CG  1 
ATOM 4490  C CD  . PRO C 1 71  ? 158.635 14.416  79.498  1.000 36.280  ? 88  PRO CCC CD  1 
ATOM 4491  N N   . ASN C 1 72  ? 160.089 18.414  81.758  1.000 42.270  ? 89  ASN CCC N   1 
ATOM 4492  C CA  . ASN C 1 72  ? 160.784 19.727  81.766  1.000 45.560  ? 89  ASN CCC CA  1 
ATOM 4493  C C   . ASN C 1 72  ? 162.302 19.538  81.657  1.000 45.100  ? 89  ASN CCC C   1 
ATOM 4494  O O   . ASN C 1 72  ? 162.799 18.569  82.217  1.000 46.180  ? 89  ASN CCC O   1 
ATOM 4495  C CB  . ASN C 1 72  ? 160.473 20.518  83.030  1.000 45.530  ? 89  ASN CCC CB  1 
ATOM 4496  C CG  . ASN C 1 72  ? 160.776 21.990  82.864  1.000 44.740  ? 89  ASN CCC CG  1 
ATOM 4497  O OD1 . ASN C 1 72  ? 161.546 22.408  82.004  1.000 48.750  ? 89  ASN CCC OD1 1 
ATOM 4498  N ND2 . ASN C 1 72  ? 160.192 22.799  83.710  1.000 49.370  ? 89  ASN CCC ND2 1 
ATOM 4499  N N   . LEU C 1 73  ? 163.017 20.463  81.003  1.000 45.550  ? 90  LEU CCC N   1 
ATOM 4500  C CA  . LEU C 1 73  ? 164.500 20.388  80.817  1.000 45.670  ? 90  LEU CCC CA  1 
ATOM 4501  C C   . LEU C 1 73  ? 165.260 21.649  81.277  1.000 39.040  ? 90  LEU CCC C   1 
ATOM 4502  O O   . LEU C 1 73  ? 164.854 22.746  80.896  1.000 36.030  ? 90  LEU CCC O   1 
ATOM 4503  C CB  . LEU C 1 73  ? 164.696 20.079  79.331  1.000 49.430  ? 90  LEU CCC CB  1 
ATOM 4504  C CG  . LEU C 1 73  ? 163.979 18.813  78.835  1.000 47.600  ? 90  LEU CCC CG  1 
ATOM 4505  C CD1 . LEU C 1 73  ? 164.103 18.652  77.331  1.000 45.500  ? 90  LEU CCC CD1 1 
ATOM 4506  C CD2 . LEU C 1 73  ? 164.517 17.580  79.551  1.000 49.070  ? 90  LEU CCC CD2 1 
ATOM 4507  N N   . ILE C 1 82  ? 170.605 25.222  76.235  1.000 39.940  ? 99  ILE CCC N   1 
ATOM 4508  C CA  . ILE C 1 82  ? 169.113 25.062  76.176  1.000 40.130  ? 99  ILE CCC CA  1 
ATOM 4509  C C   . ILE C 1 82  ? 168.784 23.727  75.477  1.000 38.600  ? 99  ILE CCC C   1 
ATOM 4510  O O   . ILE C 1 82  ? 169.365 23.493  74.411  1.000 39.450  ? 99  ILE CCC O   1 
ATOM 4511  C CB  . ILE C 1 82  ? 168.478 26.278  75.463  1.000 41.090  ? 99  ILE CCC CB  1 
ATOM 4512  C CG1 . ILE C 1 82  ? 169.071 27.625  75.939  1.000 48.440  ? 99  ILE CCC CG1 1 
ATOM 4513  C CG2 . ILE C 1 82  ? 166.953 26.228  75.574  1.000 35.750  ? 99  ILE CCC CG2 1 
ATOM 4514  C CD1 . ILE C 1 82  ? 170.278 28.204  75.133  1.000 47.150  ? 99  ILE CCC CD1 1 
ATOM 4515  N N   . LEU C 1 83  ? 167.997 22.839  76.105  1.000 37.490  ? 100 LEU CCC N   1 
ATOM 4516  C CA  . LEU C 1 83  ? 167.635 21.490  75.583  1.000 35.240  ? 100 LEU CCC CA  1 
ATOM 4517  C C   . LEU C 1 83  ? 166.176 21.477  75.114  1.000 36.740  ? 100 LEU CCC C   1 
ATOM 4518  O O   . LEU C 1 83  ? 165.330 22.044  75.825  1.000 41.550  ? 100 LEU CCC O   1 
ATOM 4519  C CB  . LEU C 1 83  ? 167.801 20.450  76.689  1.000 33.840  ? 100 LEU CCC CB  1 
ATOM 4520  C CG  . LEU C 1 83  ? 169.225 20.214  77.162  1.000 35.260  ? 100 LEU CCC CG  1 
ATOM 4521  C CD1 . LEU C 1 83  ? 169.275 18.976  78.053  1.000 35.940  ? 100 LEU CCC CD1 1 
ATOM 4522  C CD2 . LEU C 1 83  ? 170.165 20.086  75.972  1.000 36.110  ? 100 LEU CCC CD2 1 
ATOM 4523  N N   . MET C 1 84  ? 165.907 20.812  73.988  1.000 35.090  ? 101 MET CCC N   1 
ATOM 4524  C CA  . MET C 1 84  ? 164.541 20.548  73.465  1.000 36.190  ? 101 MET CCC CA  1 
ATOM 4525  C C   . MET C 1 84  ? 164.380 19.051  73.173  1.000 39.910  ? 101 MET CCC C   1 
ATOM 4526  O O   . MET C 1 84  ? 165.391 18.396  72.798  1.000 41.880  ? 101 MET CCC O   1 
ATOM 4527  C CB  . MET C 1 84  ? 164.282 21.323  72.175  1.000 33.340  ? 101 MET CCC CB  1 
ATOM 4528  C CG  . MET C 1 84  ? 164.408 22.798  72.337  1.000 32.750  ? 101 MET CCC CG  1 
ATOM 4529  S SD  . MET C 1 84  ? 163.928 23.627  70.808  1.000 34.750  ? 101 MET CCC SD  1 
ATOM 4530  C CE  . MET C 1 84  ? 162.149 23.601  70.975  1.000 33.290  ? 101 MET CCC CE  1 
ATOM 4531  N N   . TRP C 1 85  ? 163.152 18.537  73.301  1.000 37.700  ? 102 TRP CCC N   1 
ATOM 4532  C CA  . TRP C 1 85  ? 162.830 17.141  72.908  1.000 35.790  ? 102 TRP CCC CA  1 
ATOM 4533  C C   . TRP C 1 85  ? 162.737 17.041  71.380  1.000 32.460  ? 102 TRP CCC C   1 
ATOM 4534  O O   . TRP C 1 85  ? 161.975 17.816  70.765  1.000 31.390  ? 102 TRP CCC O   1 
ATOM 4535  C CB  . TRP C 1 85  ? 161.541 16.676  73.579  1.000 37.770  ? 102 TRP CCC CB  1 
ATOM 4536  C CG  . TRP C 1 85  ? 161.664 16.347  75.034  1.000 35.900  ? 102 TRP CCC CG  1 
ATOM 4537  C CD1 . TRP C 1 85  ? 161.049 16.978  76.071  1.000 34.610  ? 102 TRP CCC CD1 1 
ATOM 4538  C CD2 . TRP C 1 85  ? 162.412 15.270  75.614  1.000 34.060  ? 102 TRP CCC CD2 1 
ATOM 4539  N NE1 . TRP C 1 85  ? 161.372 16.374  77.248  1.000 34.240  ? 102 TRP CCC NE1 1 
ATOM 4540  C CE2 . TRP C 1 85  ? 162.204 15.317  77.000  1.000 32.290  ? 102 TRP CCC CE2 1 
ATOM 4541  C CE3 . TRP C 1 85  ? 163.249 14.280  75.108  1.000 37.030  ? 102 TRP CCC CE3 1 
ATOM 4542  C CZ2 . TRP C 1 85  ? 162.806 14.419  77.879  1.000 31.200  ? 102 TRP CCC CZ2 1 
ATOM 4543  C CZ3 . TRP C 1 85  ? 163.826 13.372  75.971  1.000 35.090  ? 102 TRP CCC CZ3 1 
ATOM 4544  C CH2 . TRP C 1 85  ? 163.603 13.447  77.339  1.000 31.340  ? 102 TRP CCC CH2 1 
ATOM 4545  N N   . GLU C 1 86  ? 163.490 16.096  70.816  1.000 32.010  ? 103 GLU CCC N   1 
ATOM 4546  C CA  . GLU C 1 86  ? 163.520 15.745  69.374  1.000 31.240  ? 103 GLU CCC CA  1 
ATOM 4547  C C   . GLU C 1 86  ? 162.701 14.466  69.167  1.000 30.610  ? 103 GLU CCC C   1 
ATOM 4548  O O   . GLU C 1 86  ? 163.094 13.417  69.724  1.000 34.960  ? 103 GLU CCC O   1 
ATOM 4549  C CB  . GLU C 1 86  ? 164.975 15.547  68.934  1.000 30.830  ? 103 GLU CCC CB  1 
ATOM 4550  C CG  . GLU C 1 86  ? 165.172 15.569  67.428  1.000 31.010  ? 103 GLU CCC CG  1 
ATOM 4551  C CD  . GLU C 1 86  ? 166.565 15.181  66.949  1.000 30.390  ? 103 GLU CCC CD  1 
ATOM 4552  O OE1 . GLU C 1 86  ? 167.339 14.629  67.761  1.000 29.260  ? 103 GLU CCC OE1 1 
ATOM 4553  O OE2 . GLU C 1 86  ? 166.885 15.435  65.764  1.000 28.620  ? 103 GLU CCC OE2 1 
ATOM 4554  N N   . ALA C 1 87  ? 161.605 14.542  68.413  1.000 27.020  ? 104 ALA CCC N   1 
ATOM 4555  C CA  . ALA C 1 87  ? 160.800 13.364  68.013  1.000 24.910  ? 104 ALA CCC CA  1 
ATOM 4556  C C   . ALA C 1 87  ? 161.565 12.612  66.925  1.000 23.760  ? 104 ALA CCC C   1 
ATOM 4557  O O   . ALA C 1 87  ? 161.844 13.212  65.878  1.000 22.360  ? 104 ALA CCC O   1 
ATOM 4558  C CB  . ALA C 1 87  ? 159.431 13.791  67.551  1.000 25.040  ? 104 ALA CCC CB  1 
ATOM 4559  N N   . VAL C 1 88  ? 161.890 11.348  67.174  1.000 24.540  ? 105 VAL CCC N   1 
ATOM 4560  C CA  . VAL C 1 88  ? 162.843 10.572  66.339  1.000 26.710  ? 105 VAL CCC CA  1 
ATOM 4561  C C   . VAL C 1 88  ? 162.105 9.504   65.524  1.000 26.380  ? 105 VAL CCC C   1 
ATOM 4562  O O   . VAL C 1 88  ? 162.376 9.400   64.311  1.000 28.530  ? 105 VAL CCC O   1 
ATOM 4563  C CB  . VAL C 1 88  ? 163.954 9.986   67.224  1.000 27.050  ? 105 VAL CCC CB  1 
ATOM 4564  C CG1 . VAL C 1 88  ? 164.916 9.104   66.433  1.000 28.430  ? 105 VAL CCC CG1 1 
ATOM 4565  C CG2 . VAL C 1 88  ? 164.713 11.110  67.889  1.000 26.230  ? 105 VAL CCC CG2 1 
ATOM 4566  N N   . THR C 1 89  ? 161.235 8.723   66.155  1.000 25.050  ? 106 THR CCC N   1 
ATOM 4567  C CA  . THR C 1 89  ? 160.486 7.640   65.473  1.000 24.920  ? 106 THR CCC CA  1 
ATOM 4568  C C   . THR C 1 89  ? 159.006 7.695   65.844  1.000 25.160  ? 106 THR CCC C   1 
ATOM 4569  O O   . THR C 1 89  ? 158.663 8.148   66.928  1.000 24.660  ? 106 THR CCC O   1 
ATOM 4570  C CB  . THR C 1 89  ? 161.045 6.258   65.824  1.000 24.530  ? 106 THR CCC CB  1 
ATOM 4571  O OG1 . THR C 1 89  ? 160.408 5.781   67.016  1.000 23.090  ? 106 THR CCC OG1 1 
ATOM 4572  C CG2 . THR C 1 89  ? 162.547 6.259   65.996  1.000 25.440  ? 106 THR CCC CG2 1 
ATOM 4573  N N   . LEU C 1 90  ? 158.170 7.209   64.943  1.000 26.800  ? 107 LEU CCC N   1 
ATOM 4574  C CA  . LEU C 1 90  ? 156.713 7.045   65.137  1.000 28.280  ? 107 LEU CCC CA  1 
ATOM 4575  C C   . LEU C 1 90  ? 156.341 5.597   64.815  1.000 27.810  ? 107 LEU CCC C   1 
ATOM 4576  O O   . LEU C 1 90  ? 156.943 5.032   63.929  1.000 25.260  ? 107 LEU CCC O   1 
ATOM 4577  C CB  . LEU C 1 90  ? 155.983 8.006   64.200  1.000 27.590  ? 107 LEU CCC CB  1 
ATOM 4578  C CG  . LEU C 1 90  ? 154.494 7.730   64.059  1.000 28.340  ? 107 LEU CCC CG  1 
ATOM 4579  C CD1 . LEU C 1 90  ? 153.799 8.042   65.369  1.000 29.870  ? 107 LEU CCC CD1 1 
ATOM 4580  C CD2 . LEU C 1 90  ? 153.935 8.559   62.920  1.000 30.460  ? 107 LEU CCC CD2 1 
ATOM 4581  N N   . LYS C 1 91  ? 155.434 5.025   65.586  1.000 30.320  ? 108 LYS CCC N   1 
ATOM 4582  C CA  . LYS C 1 91  ? 154.628 3.841   65.220  1.000 31.600  ? 108 LYS CCC CA  1 
ATOM 4583  C C   . LYS C 1 91  ? 153.187 4.288   65.332  1.000 31.390  ? 108 LYS CCC C   1 
ATOM 4584  O O   . LYS C 1 91  ? 152.840 4.933   66.337  1.000 35.880  ? 108 LYS CCC O   1 
ATOM 4585  C CB  . LYS C 1 91  ? 154.855 2.671   66.181  1.000 35.500  ? 108 LYS CCC CB  1 
ATOM 4586  C CG  . LYS C 1 91  ? 156.193 1.941   66.039  1.000 39.500  ? 108 LYS CCC CG  1 
ATOM 4587  C CD  . LYS C 1 91  ? 156.359 0.908   67.132  1.000 41.690  ? 108 LYS CCC CD  1 
ATOM 4588  C CE  . LYS C 1 91  ? 157.104 -0.325  66.706  1.000 44.730  ? 108 LYS CCC CE  1 
ATOM 4589  N NZ  . LYS C 1 91  ? 157.631 -1.048  67.891  1.000 47.240  ? 108 LYS CCC NZ  1 
ATOM 4590  N N   . THR C 1 92  ? 152.377 3.997   64.334  1.000 30.860  ? 109 THR CCC N   1 
ATOM 4591  C CA  . THR C 1 92  ? 150.936 4.331   64.369  1.000 30.640  ? 109 THR CCC CA  1 
ATOM 4592  C C   . THR C 1 92  ? 150.177 3.212   63.679  1.000 31.240  ? 109 THR CCC C   1 
ATOM 4593  O O   . THR C 1 92  ? 150.785 2.555   62.824  1.000 38.100  ? 109 THR CCC O   1 
ATOM 4594  C CB  . THR C 1 92  ? 150.693 5.710   63.760  1.000 29.370  ? 109 THR CCC CB  1 
ATOM 4595  O OG1 . THR C 1 92  ? 149.293 5.941   63.846  1.000 31.270  ? 109 THR CCC OG1 1 
ATOM 4596  C CG2 . THR C 1 92  ? 151.140 5.822   62.323  1.000 29.790  ? 109 THR CCC CG2 1 
ATOM 4597  N N   . GLU C 1 93  ? 148.942 2.973   64.090  1.000 32.580  ? 110 GLU CCC N   1 
ATOM 4598  C CA  . GLU C 1 93  ? 148.015 2.097   63.337  1.000 36.690  ? 110 GLU CCC CA  1 
ATOM 4599  C C   . GLU C 1 93  ? 146.593 2.504   63.694  1.000 33.740  ? 110 GLU CCC C   1 
ATOM 4600  O O   . GLU C 1 93  ? 146.417 3.205   64.687  1.000 36.220  ? 110 GLU CCC O   1 
ATOM 4601  C CB  . GLU C 1 93  ? 148.329 0.609   63.575  1.000 41.130  ? 110 GLU CCC CB  1 
ATOM 4602  C CG  . GLU C 1 93  ? 147.678 -0.015  64.794  1.000 43.740  ? 110 GLU CCC CG  1 
ATOM 4603  C CD  . GLU C 1 93  ? 148.223 -1.397  65.161  1.000 48.370  ? 110 GLU CCC CD  1 
ATOM 4604  O OE1 . GLU C 1 93  ? 149.445 -1.648  64.899  1.000 39.310  ? 110 GLU CCC OE1 1 
ATOM 4605  O OE2 . GLU C 1 93  ? 147.418 -2.226  65.740  1.000 57.750  ? 110 GLU CCC OE2 1 
ATOM 4606  N N   . VAL C 1 94  ? 145.636 2.093   62.886  1.000 29.600  ? 111 VAL CCC N   1 
ATOM 4607  C CA  . VAL C 1 94  ? 144.195 2.334   63.173  1.000 27.010  ? 111 VAL CCC CA  1 
ATOM 4608  C C   . VAL C 1 94  ? 143.741 1.284   64.179  1.000 27.840  ? 111 VAL CCC C   1 
ATOM 4609  O O   . VAL C 1 94  ? 144.003 0.071   63.983  1.000 27.430  ? 111 VAL CCC O   1 
ATOM 4610  C CB  . VAL C 1 94  ? 143.376 2.316   61.891  1.000 26.700  ? 111 VAL CCC CB  1 
ATOM 4611  C CG1 . VAL C 1 94  ? 141.887 2.371   62.176  1.000 26.560  ? 111 VAL CCC CG1 1 
ATOM 4612  C CG2 . VAL C 1 94  ? 143.798 3.461   61.002  1.000 27.680  ? 111 VAL CCC CG2 1 
ATOM 4613  N N   . ILE C 1 95  ? 143.053 1.738   65.225  1.000 30.520  ? 112 ILE CCC N   1 
ATOM 4614  C CA  . ILE C 1 95  ? 142.542 0.834   66.290  1.000 33.040  ? 112 ILE CCC CA  1 
ATOM 4615  C C   . ILE C 1 95  ? 141.085 0.456   66.006  1.000 34.230  ? 112 ILE CCC C   1 
ATOM 4616  O O   . ILE C 1 95  ? 140.201 1.368   65.973  1.000 35.560  ? 112 ILE CCC O   1 
ATOM 4617  C CB  . ILE C 1 95  ? 142.710 1.463   67.671  1.000 31.830  ? 112 ILE CCC CB  1 
ATOM 4618  C CG1 . ILE C 1 95  ? 144.135 1.974   67.889  1.000 35.140  ? 112 ILE CCC CG1 1 
ATOM 4619  C CG2 . ILE C 1 95  ? 142.310 0.453   68.725  1.000 31.310  ? 112 ILE CCC CG2 1 
ATOM 4620  C CD1 . ILE C 1 95  ? 144.240 2.947   69.048  1.000 38.370  ? 112 ILE CCC CD1 1 
ATOM 4621  N N   . GLY C 1 96  ? 140.855 -0.849  65.829  1.000 30.760  ? 113 GLY CCC N   1 
ATOM 4622  C CA  . GLY C 1 96  ? 139.501 -1.400  65.717  1.000 29.990  ? 113 GLY CCC CA  1 
ATOM 4623  C C   . GLY C 1 96  ? 139.105 -1.608  64.273  1.000 27.840  ? 113 GLY CCC C   1 
ATOM 4624  O O   . GLY C 1 96  ? 137.925 -1.376  63.950  1.000 25.830  ? 113 GLY CCC O   1 
ATOM 4625  N N   . VAL C 1 97  ? 140.050 -2.094  63.461  1.000 27.150  ? 114 VAL CCC N   1 
ATOM 4626  C CA  . VAL C 1 97  ? 139.857 -2.321  61.999  1.000 26.010  ? 114 VAL CCC CA  1 
ATOM 4627  C C   . VAL C 1 97  ? 138.791 -3.399  61.830  1.000 24.030  ? 114 VAL CCC C   1 
ATOM 4628  O O   . VAL C 1 97  ? 137.965 -3.236  60.926  1.000 24.210  ? 114 VAL CCC O   1 
ATOM 4629  C CB  . VAL C 1 97  ? 141.159 -2.704  61.266  1.000 26.770  ? 114 VAL CCC CB  1 
ATOM 4630  C CG1 . VAL C 1 97  ? 142.215 -1.626  61.429  1.000 27.110  ? 114 VAL CCC CG1 1 
ATOM 4631  C CG2 . VAL C 1 97  ? 141.715 -4.057  61.706  1.000 27.140  ? 114 VAL CCC CG2 1 
ATOM 4632  N N   . THR C 1 98  ? 138.805 -4.439  62.668  1.000 22.920  ? 115 THR CCC N   1 
ATOM 4633  C CA  . THR C 1 98  ? 137.919 -5.619  62.534  1.000 24.600  ? 115 THR CCC CA  1 
ATOM 4634  C C   . THR C 1 98  ? 136.450 -5.200  62.672  1.000 25.160  ? 115 THR CCC C   1 
ATOM 4635  O O   . THR C 1 98  ? 135.591 -5.934  62.152  1.000 26.560  ? 115 THR CCC O   1 
ATOM 4636  C CB  . THR C 1 98  ? 138.203 -6.696  63.581  1.000 27.100  ? 115 THR CCC CB  1 
ATOM 4637  O OG1 . THR C 1 98  ? 138.035 -6.087  64.872  1.000 31.940  ? 115 THR CCC OG1 1 
ATOM 4638  C CG2 . THR C 1 98  ? 139.567 -7.332  63.393  1.000 26.890  ? 115 THR CCC CG2 1 
ATOM 4639  N N   . SER C 1 99  ? 136.172 -4.089  63.364  1.000 24.710  ? 116 SER CCC N   1 
ATOM 4640  C CA  . SER C 1 99  ? 134.796 -3.605  63.619  1.000 24.150  ? 116 SER CCC CA  1 
ATOM 4641  C C   . SER C 1 99  ? 134.095 -3.378  62.299  1.000 24.070  ? 116 SER CCC C   1 
ATOM 4642  O O   . SER C 1 99  ? 132.868 -3.281  62.331  1.000 24.670  ? 116 SER CCC O   1 
ATOM 4643  C CB  . SER C 1 99  ? 134.806 -2.342  64.398  1.000 27.000  ? 116 SER CCC CB  1 
ATOM 4644  O OG  . SER C 1 99  ? 135.299 -1.279  63.603  1.000 28.900  ? 116 SER CCC OG  1 
ATOM 4645  N N   . LEU C 1 100 ? 134.858 -3.243  61.206  1.000 24.500  ? 117 LEU CCC N   1 
ATOM 4646  C CA  . LEU C 1 100 ? 134.345 -2.909  59.855  1.000 25.010  ? 117 LEU CCC CA  1 
ATOM 4647  C C   . LEU C 1 100 ? 133.802 -4.169  59.187  1.000 25.600  ? 117 LEU CCC C   1 
ATOM 4648  O O   . LEU C 1 100 ? 133.186 -4.041  58.097  1.000 29.270  ? 117 LEU CCC O   1 
ATOM 4649  C CB  . LEU C 1 100 ? 135.454 -2.248  59.034  1.000 24.490  ? 117 LEU CCC CB  1 
ATOM 4650  C CG  . LEU C 1 100 ? 135.841 -0.859  59.536  1.000 23.440  ? 117 LEU CCC CG  1 
ATOM 4651  C CD1 . LEU C 1 100 ? 136.827 -0.170  58.608  1.000 22.530  ? 117 LEU CCC CD1 1 
ATOM 4652  C CD2 . LEU C 1 100 ? 134.609 0.006   59.714  1.000 23.650  ? 117 LEU CCC CD2 1 
ATOM 4653  N N   . MET C 1 101 ? 133.970 -5.331  59.826  1.000 23.910  ? 118 MET CCC N   1 
ATOM 4654  C CA  . MET C 1 101 ? 133.348 -6.601  59.373  1.000 26.560  ? 118 MET CCC CA  1 
ATOM 4655  C C   . MET C 1 101 ? 131.888 -6.711  59.845  1.000 25.530  ? 118 MET CCC C   1 
ATOM 4656  O O   . MET C 1 101 ? 131.261 -7.740  59.531  1.000 22.730  ? 118 MET CCC O   1 
ATOM 4657  C CB  . MET C 1 101 ? 134.140 -7.794  59.888  1.000 28.850  ? 118 MET CCC CB  1 
ATOM 4658  C CG  . MET C 1 101 ? 135.583 -7.724  59.420  1.000 29.930  ? 118 MET CCC CG  1 
ATOM 4659  S SD  . MET C 1 101 ? 136.608 -9.135  59.885  1.000 33.300  ? 118 MET CCC SD  1 
ATOM 4660  C CE  . MET C 1 101 ? 135.830 -10.475 58.986  1.000 36.150  ? 118 MET CCC CE  1 
ATOM 4661  N N   . ASN C 1 102 ? 131.367 -5.725  60.589  1.000 25.570  ? 119 ASN CCC N   1 
ATOM 4662  C CA  . ASN C 1 102 ? 129.978 -5.786  61.101  1.000 25.960  ? 119 ASN CCC CA  1 
ATOM 4663  C C   . ASN C 1 102 ? 129.007 -5.498  59.958  1.000 25.240  ? 119 ASN CCC C   1 
ATOM 4664  O O   . ASN C 1 102 ? 128.588 -4.353  59.808  1.000 24.910  ? 119 ASN CCC O   1 
ATOM 4665  C CB  . ASN C 1 102 ? 129.692 -4.872  62.286  1.000 26.310  ? 119 ASN CCC CB  1 
ATOM 4666  C CG  . ASN C 1 102 ? 128.290 -5.075  62.822  1.000 30.260  ? 119 ASN CCC CG  1 
ATOM 4667  O OD1 . ASN C 1 102 ? 127.413 -5.568  62.113  1.000 30.500  ? 119 ASN CCC OD1 1 
ATOM 4668  N ND2 . ASN C 1 102 ? 128.051 -4.709  64.082  1.000 38.470  ? 119 ASN CCC ND2 1 
ATOM 4669  N N   . VAL C 1 103 ? 128.575 -6.557  59.283  1.000 24.350  ? 120 VAL CCC N   1 
ATOM 4670  C CA  . VAL C 1 103 ? 127.700 -6.506  58.084  1.000 23.530  ? 120 VAL CCC CA  1 
ATOM 4671  C C   . VAL C 1 103 ? 126.246 -6.871  58.433  1.000 22.860  ? 120 VAL CCC C   1 
ATOM 4672  O O   . VAL C 1 103 ? 125.481 -7.159  57.518  1.000 20.010  ? 120 VAL CCC O   1 
ATOM 4673  C CB  . VAL C 1 103 ? 128.314 -7.442  57.046  1.000 23.990  ? 120 VAL CCC CB  1 
ATOM 4674  C CG1 . VAL C 1 103 ? 129.734 -7.033  56.740  1.000 25.710  ? 120 VAL CCC CG1 1 
ATOM 4675  C CG2 . VAL C 1 103 ? 128.273 -8.883  57.493  1.000 25.450  ? 120 VAL CCC CG2 1 
ATOM 4676  N N   . HIS C 1 104 ? 125.852 -6.789  59.704  1.000 24.460  ? 121 HIS CCC N   1 
ATOM 4677  C CA  . HIS C 1 104 ? 124.542 -7.286  60.212  1.000 26.010  ? 121 HIS CCC CA  1 
ATOM 4678  C C   . HIS C 1 104 ? 123.740 -6.229  60.997  1.000 27.880  ? 121 HIS CCC C   1 
ATOM 4679  O O   . HIS C 1 104 ? 122.628 -6.562  61.455  1.000 28.250  ? 121 HIS CCC O   1 
ATOM 4680  C CB  . HIS C 1 104 ? 124.764 -8.526  61.092  1.000 25.160  ? 121 HIS CCC CB  1 
ATOM 4681  C CG  . HIS C 1 104 ? 125.892 -8.399  62.057  1.000 24.720  ? 121 HIS CCC CG  1 
ATOM 4682  N ND1 . HIS C 1 104 ? 125.696 -7.905  63.327  1.000 25.560  ? 121 HIS CCC ND1 1 
ATOM 4683  C CD2 . HIS C 1 104 ? 127.204 -8.717  61.951  1.000 24.120  ? 121 HIS CCC CD2 1 
ATOM 4684  C CE1 . HIS C 1 104 ? 126.845 -7.923  63.971  1.000 25.420  ? 121 HIS CCC CE1 1 
ATOM 4685  N NE2 . HIS C 1 104 ? 127.782 -8.417  63.142  1.000 25.190  ? 121 HIS CCC NE2 1 
ATOM 4686  N N   . SER C 1 105 ? 124.250 -5.007  61.162  1.000 30.830  ? 122 SER CCC N   1 
ATOM 4687  C CA  . SER C 1 105 ? 123.680 -3.972  62.075  1.000 30.030  ? 122 SER CCC CA  1 
ATOM 4688  C C   . SER C 1 105 ? 122.795 -2.992  61.290  1.000 28.100  ? 122 SER CCC C   1 
ATOM 4689  O O   . SER C 1 105 ? 123.196 -1.854  61.123  1.000 26.460  ? 122 SER CCC O   1 
ATOM 4690  C CB  . SER C 1 105 ? 124.774 -3.260  62.860  1.000 28.800  ? 122 SER CCC CB  1 
ATOM 4691  O OG  . SER C 1 105 ? 124.193 -2.348  63.788  1.000 28.400  ? 122 SER CCC OG  1 
ATOM 4692  N N   . ASN C 1 106 ? 121.634 -3.449  60.834  1.000 27.540  ? 123 ASN CCC N   1 
ATOM 4693  C CA  . ASN C 1 106 ? 120.645 -2.641  60.080  1.000 30.120  ? 123 ASN CCC CA  1 
ATOM 4694  C C   . ASN C 1 106 ? 121.308 -1.991  58.866  1.000 31.950  ? 123 ASN CCC C   1 
ATOM 4695  O O   . ASN C 1 106 ? 121.018 -0.815  58.613  1.000 32.710  ? 123 ASN CCC O   1 
ATOM 4696  C CB  . ASN C 1 106 ? 120.031 -1.564  60.966  1.000 32.050  ? 123 ASN CCC CB  1 
ATOM 4697  C CG  . ASN C 1 106 ? 118.638 -1.186  60.514  1.000 34.620  ? 123 ASN CCC CG  1 
ATOM 4698  O OD1 . ASN C 1 106 ? 117.763 -2.051  60.449  1.000 35.930  ? 123 ASN CCC OD1 1 
ATOM 4699  N ND2 . ASN C 1 106 ? 118.417 0.092   60.226  1.000 35.360  ? 123 ASN CCC ND2 1 
ATOM 4700  N N   . GLY C 1 107 ? 122.179 -2.724  58.160  1.000 36.980  ? 124 GLY CCC N   1 
ATOM 4701  C CA  . GLY C 1 107 ? 122.842 -2.240  56.931  1.000 38.780  ? 124 GLY CCC CA  1 
ATOM 4702  C C   . GLY C 1 107 ? 121.983 -2.272  55.683  1.000 38.270  ? 124 GLY CCC C   1 
ATOM 4703  O O   . GLY C 1 107 ? 120.760 -2.609  55.806  1.000 33.840  ? 124 GLY CCC O   1 
ATOM 4704  N N   . GLN C 1 108 ? 122.626 -2.180  54.515  1.000 36.240  ? 125 GLN CCC N   1 
ATOM 4705  C CA  . GLN C 1 108 ? 121.882 -2.332  53.242  1.000 35.440  ? 125 GLN CCC CA  1 
ATOM 4706  C C   . GLN C 1 108 ? 122.279 -3.632  52.539  1.000 34.840  ? 125 GLN CCC C   1 
ATOM 4707  O O   . GLN C 1 108 ? 123.373 -3.650  51.964  1.000 32.150  ? 125 GLN CCC O   1 
ATOM 4708  C CB  . GLN C 1 108 ? 122.127 -1.152  52.312  1.000 32.710  ? 125 GLN CCC CB  1 
ATOM 4709  C CG  . GLN C 1 108 ? 121.009 -0.895  51.331  1.000 33.720  ? 125 GLN CCC CG  1 
ATOM 4710  C CD  . GLN C 1 108 ? 121.476 -0.041  50.180  1.000 33.740  ? 125 GLN CCC CD  1 
ATOM 4711  O OE1 . GLN C 1 108 ? 122.635 -0.088  49.778  1.000 27.540  ? 125 GLN CCC OE1 1 
ATOM 4712  N NE2 . GLN C 1 108 ? 120.569 0.751   49.639  1.000 30.870  ? 125 GLN CCC NE2 1 
ATOM 4713  N N   . ALA C 1 109 ? 121.449 -4.673  52.609  1.000 31.560  ? 126 ALA CCC N   1 
ATOM 4714  C CA  . ALA C 1 109 ? 121.621 -5.942  51.874  1.000 30.780  ? 126 ALA CCC CA  1 
ATOM 4715  C C   . ALA C 1 109 ? 122.116 -5.529  50.489  1.000 28.860  ? 126 ALA CCC C   1 
ATOM 4716  O O   . ALA C 1 109 ? 121.411 -4.766  49.839  1.000 27.630  ? 126 ALA CCC O   1 
ATOM 4717  C CB  . ALA C 1 109 ? 120.386 -6.796  51.761  1.000 34.510  ? 126 ALA CCC CB  1 
ATOM 4718  N N   . THR C 1 110 ? 123.267 -6.040  50.077  1.000 29.130  ? 127 THR CCC N   1 
ATOM 4719  C CA  . THR C 1 110 ? 123.826 -5.888  48.712  1.000 28.710  ? 127 THR CCC CA  1 
ATOM 4720  C C   . THR C 1 110 ? 122.872 -6.509  47.681  1.000 26.820  ? 127 THR CCC C   1 
ATOM 4721  O O   . THR C 1 110 ? 122.891 -6.049  46.536  1.000 25.190  ? 127 THR CCC O   1 
ATOM 4722  C CB  . THR C 1 110 ? 125.236 -6.478  48.643  1.000 29.610  ? 127 THR CCC CB  1 
ATOM 4723  O OG1 . THR C 1 110 ? 125.243 -7.794  49.195  1.000 30.530  ? 127 THR CCC OG1 1 
ATOM 4724  C CG2 . THR C 1 110 ? 126.251 -5.627  49.382  1.000 29.480  ? 127 THR CCC CG2 1 
ATOM 4725  N N   . HIS C 1 111 ? 122.058 -7.493  48.062  1.000 26.360  ? 128 HIS CCC N   1 
ATOM 4726  C CA  . HIS C 1 111 ? 121.117 -8.195  47.137  1.000 27.740  ? 128 HIS CCC CA  1 
ATOM 4727  C C   . HIS C 1 111 ? 120.188 -9.120  47.924  1.000 27.270  ? 128 HIS CCC C   1 
ATOM 4728  O O   . HIS C 1 111 ? 120.426 -9.269  49.121  1.000 30.220  ? 128 HIS CCC O   1 
ATOM 4729  C CB  . HIS C 1 111 ? 121.893 -9.024  46.109  1.000 28.270  ? 128 HIS CCC CB  1 
ATOM 4730  C CG  . HIS C 1 111 ? 122.789 -10.012 46.760  1.000 25.740  ? 128 HIS CCC CG  1 
ATOM 4731  N ND1 . HIS C 1 111 ? 124.075 -9.706  47.107  1.000 25.950  ? 128 HIS CCC ND1 1 
ATOM 4732  C CD2 . HIS C 1 111 ? 122.566 -11.273 47.167  1.000 25.260  ? 128 HIS CCC CD2 1 
ATOM 4733  C CE1 . HIS C 1 111 ? 124.624 -10.758 47.676  1.000 27.150  ? 128 HIS CCC CE1 1 
ATOM 4734  N NE2 . HIS C 1 111 ? 123.712 -11.728 47.746  1.000 25.410  ? 128 HIS CCC NE2 1 
ATOM 4735  N N   . ASP C 1 112 ? 119.199 -9.754  47.291  1.000 25.130  ? 129 ASP CCC N   1 
ATOM 4736  C CA  . ASP C 1 112 ? 118.266 -10.636 48.035  1.000 24.990  ? 129 ASP CCC CA  1 
ATOM 4737  C C   . ASP C 1 112 ? 119.064 -11.674 48.827  1.000 23.950  ? 129 ASP CCC C   1 
ATOM 4738  O O   . ASP C 1 112 ? 119.806 -12.437 48.213  1.000 23.950  ? 129 ASP CCC O   1 
ATOM 4739  C CB  . ASP C 1 112 ? 117.246 -11.283 47.110  1.000 26.380  ? 129 ASP CCC CB  1 
ATOM 4740  C CG  . ASP C 1 112 ? 116.135 -10.334 46.700  1.000 26.250  ? 129 ASP CCC CG  1 
ATOM 4741  O OD1 . ASP C 1 112 ? 115.950 -9.320  47.377  1.000 25.350  ? 129 ASP CCC OD1 1 
ATOM 4742  O OD2 . ASP C 1 112 ? 115.463 -10.632 45.710  1.000 28.410  ? 129 ASP CCC OD2 1 
ATOM 4743  N N   . ASN C 1 113 ? 118.900 -11.663 50.149  1.000 24.610  ? 130 ASN CCC N   1 
ATOM 4744  C CA  . ASN C 1 113 ? 119.537 -12.577 51.140  1.000 25.530  ? 130 ASN CCC CA  1 
ATOM 4745  C C   . ASN C 1 113 ? 121.018 -12.219 51.274  1.000 27.050  ? 130 ASN CCC C   1 
ATOM 4746  O O   . ASN C 1 113 ? 121.766 -12.968 51.916  1.000 31.100  ? 130 ASN CCC O   1 
ATOM 4747  C CB  . ASN C 1 113 ? 119.364 -14.056 50.790  1.000 24.170  ? 130 ASN CCC CB  1 
ATOM 4748  C CG  . ASN C 1 113 ? 117.927 -14.479 50.587  1.000 24.440  ? 130 ASN CCC CG  1 
ATOM 4749  O OD1 . ASN C 1 113 ? 117.008 -14.067 51.318  1.000 21.730  ? 130 ASN CCC OD1 1 
ATOM 4750  N ND2 . ASN C 1 113 ? 117.755 -15.339 49.592  1.000 24.790  ? 130 ASN CCC ND2 1 
ATOM 4751  N N   . GLY C 1 114 ? 121.430 -11.099 50.713  1.000 27.090  ? 131 GLY CCC N   1 
ATOM 4752  C CA  . GLY C 1 114 ? 122.809 -10.614 50.881  1.000 25.490  ? 131 GLY CCC CA  1 
ATOM 4753  C C   . GLY C 1 114 ? 123.057 -10.137 52.287  1.000 22.900  ? 131 GLY CCC C   1 
ATOM 4754  O O   . GLY C 1 114 ? 122.085 -9.717  52.987  1.000 20.330  ? 131 GLY CCC O   1 
ATOM 4755  N N   . ALA C 1 115 ? 124.322 -10.217 52.689  1.000 22.310  ? 132 ALA CCC N   1 
ATOM 4756  C CA  . ALA C 1 115 ? 124.802 -9.588  53.935  1.000 23.300  ? 132 ALA CCC CA  1 
ATOM 4757  C C   . ALA C 1 115 ? 124.666 -8.087  53.725  1.000 23.460  ? 132 ALA CCC C   1 
ATOM 4758  O O   . ALA C 1 115 ? 124.376 -7.682  52.591  1.000 25.530  ? 132 ALA CCC O   1 
ATOM 4759  C CB  . ALA C 1 115 ? 126.223 -9.995  54.229  1.000 22.970  ? 132 ALA CCC CB  1 
ATOM 4760  N N   . GLY C 1 116 ? 124.878 -7.283  54.751  1.000 21.790  ? 133 GLY CCC N   1 
ATOM 4761  C CA  . GLY C 1 116 ? 124.861 -5.828  54.557  1.000 23.130  ? 133 GLY CCC CA  1 
ATOM 4762  C C   . GLY C 1 116 ? 126.075 -5.370  53.780  1.000 22.960  ? 133 GLY CCC C   1 
ATOM 4763  O O   . GLY C 1 116 ? 127.133 -5.988  53.931  1.000 21.020  ? 133 GLY CCC O   1 
ATOM 4764  N N   . LYS C 1 117 ? 125.936 -4.305  52.997  1.000 24.460  ? 134 LYS CCC N   1 
ATOM 4765  C CA  . LYS C 1 117 ? 127.105 -3.654  52.363  1.000 26.250  ? 134 LYS CCC CA  1 
ATOM 4766  C C   . LYS C 1 117 ? 128.018 -3.176  53.480  1.000 24.880  ? 134 LYS CCC C   1 
ATOM 4767  O O   . LYS C 1 117 ? 127.576 -2.418  54.334  1.000 26.640  ? 134 LYS CCC O   1 
ATOM 4768  C CB  . LYS C 1 117 ? 126.690 -2.472  51.492  1.000 29.740  ? 134 LYS CCC CB  1 
ATOM 4769  C CG  . LYS C 1 117 ? 127.845 -1.628  50.997  1.000 33.400  ? 134 LYS CCC CG  1 
ATOM 4770  C CD  . LYS C 1 117 ? 127.429 -0.406  50.239  1.000 38.770  ? 134 LYS CCC CD  1 
ATOM 4771  C CE  . LYS C 1 117 ? 127.032 -0.725  48.820  1.000 45.540  ? 134 LYS CCC CE  1 
ATOM 4772  N NZ  . LYS C 1 117 ? 126.997 0.522   48.031  1.000 54.430  ? 134 LYS CCC NZ  1 
ATOM 4773  N N   . PRO C 1 118 ? 129.304 -3.574  53.501  1.000 23.900  ? 135 PRO CCC N   1 
ATOM 4774  C CA  . PRO C 1 118 ? 130.216 -3.196  54.574  1.000 25.010  ? 135 PRO CCC CA  1 
ATOM 4775  C C   . PRO C 1 118 ? 130.625 -1.730  54.435  1.000 26.230  ? 135 PRO CCC C   1 
ATOM 4776  O O   . PRO C 1 118 ? 130.497 -1.221  53.362  1.000 26.630  ? 135 PRO CCC O   1 
ATOM 4777  C CB  . PRO C 1 118 ? 131.450 -4.062  54.343  1.000 24.050  ? 135 PRO CCC CB  1 
ATOM 4778  C CG  . PRO C 1 118 ? 131.445 -4.272  52.855  1.000 23.840  ? 135 PRO CCC CG  1 
ATOM 4779  C CD  . PRO C 1 118 ? 129.989 -4.314  52.447  1.000 23.760  ? 135 PRO CCC CD  1 
ATOM 4780  N N   . VAL C 1 119 ? 131.133 -1.124  55.503  1.000 27.520  ? 136 VAL CCC N   1 
ATOM 4781  C CA  . VAL C 1 119 ? 131.766 0.223   55.425  1.000 29.120  ? 136 VAL CCC CA  1 
ATOM 4782  C C   . VAL C 1 119 ? 132.778 0.175   54.280  1.000 27.530  ? 136 VAL CCC C   1 
ATOM 4783  O O   . VAL C 1 119 ? 133.599 -0.778  54.281  1.000 27.040  ? 136 VAL CCC O   1 
ATOM 4784  C CB  . VAL C 1 119 ? 132.453 0.662   56.733  1.000 30.740  ? 136 VAL CCC CB  1 
ATOM 4785  C CG1 . VAL C 1 119 ? 133.272 1.925   56.524  1.000 30.790  ? 136 VAL CCC CG1 1 
ATOM 4786  C CG2 . VAL C 1 119 ? 131.468 0.876   57.874  1.000 33.300  ? 136 VAL CCC CG2 1 
ATOM 4787  N N   . GLN C 1 120 ? 132.683 1.150   53.371  1.000 26.490  ? 137 GLN CCC N   1 
ATOM 4788  C CA  . GLN C 1 120 ? 133.562 1.322   52.189  1.000 26.100  ? 137 GLN CCC CA  1 
ATOM 4789  C C   . GLN C 1 120 ? 133.397 2.731   51.622  1.000 25.750  ? 137 GLN CCC C   1 
ATOM 4790  O O   . GLN C 1 120 ? 132.473 3.450   52.059  1.000 24.550  ? 137 GLN CCC O   1 
ATOM 4791  C CB  . GLN C 1 120 ? 133.218 0.320   51.091  1.000 26.760  ? 137 GLN CCC CB  1 
ATOM 4792  C CG  . GLN C 1 120 ? 131.832 0.505   50.484  1.000 28.070  ? 137 GLN CCC CG  1 
ATOM 4793  C CD  . GLN C 1 120 ? 131.437 -0.669  49.623  1.000 28.910  ? 137 GLN CCC CD  1 
ATOM 4794  O OE1 . GLN C 1 120 ? 130.808 -1.633  50.056  1.000 30.370  ? 137 GLN CCC OE1 1 
ATOM 4795  N NE2 . GLN C 1 120 ? 131.857 -0.611  48.371  1.000 29.310  ? 137 GLN CCC NE2 1 
ATOM 4796  N N   . GLY C 1 121 ? 134.235 3.092   50.655  1.000 26.730  ? 138 GLY CCC N   1 
ATOM 4797  C CA  . GLY C 1 121 ? 134.092 4.358   49.915  1.000 29.150  ? 138 GLY CCC CA  1 
ATOM 4798  C C   . GLY C 1 121 ? 135.110 5.394   50.361  1.000 28.230  ? 138 GLY CCC C   1 
ATOM 4799  O O   . GLY C 1 121 ? 136.071 5.024   51.047  1.000 25.860  ? 138 GLY CCC O   1 
ATOM 4800  N N   . THR C 1 122 ? 134.893 6.649   49.961  1.000 29.250  ? 139 THR CCC N   1 
ATOM 4801  C CA  . THR C 1 122 ? 135.846 7.779   50.092  1.000 28.930  ? 139 THR CCC CA  1 
ATOM 4802  C C   . THR C 1 122 ? 136.472 7.743   51.480  1.000 27.270  ? 139 THR CCC C   1 
ATOM 4803  O O   . THR C 1 122 ? 135.735 7.634   52.459  1.000 29.130  ? 139 THR CCC O   1 
ATOM 4804  C CB  . THR C 1 122 ? 135.127 9.104   49.819  1.000 30.890  ? 139 THR CCC CB  1 
ATOM 4805  O OG1 . THR C 1 122 ? 134.437 9.007   48.570  1.000 30.240  ? 139 THR CCC OG1 1 
ATOM 4806  C CG2 . THR C 1 122 ? 136.079 10.280  49.809  1.000 32.290  ? 139 THR CCC CG2 1 
ATOM 4807  N N   . SER C 1 123 ? 137.795 7.804   51.543  1.000 26.430  ? 140 SER CCC N   1 
ATOM 4808  C CA  . SER C 1 123 ? 138.594 7.603   52.768  1.000 26.870  ? 140 SER CCC CA  1 
ATOM 4809  C C   . SER C 1 123 ? 139.680 8.675   52.812  1.000 28.590  ? 140 SER CCC C   1 
ATOM 4810  O O   . SER C 1 123 ? 140.306 8.884   51.761  1.000 32.930  ? 140 SER CCC O   1 
ATOM 4811  C CB  . SER C 1 123 ? 139.226 6.237   52.758  1.000 26.910  ? 140 SER CCC CB  1 
ATOM 4812  O OG  . SER C 1 123 ? 140.461 6.246   52.006  1.000 24.890  ? 140 SER CCC OG  1 
ATOM 4813  N N   . PHE C 1 124 ? 139.927 9.275   53.978  1.000 28.180  ? 141 PHE CCC N   1 
ATOM 4814  C CA  . PHE C 1 124 ? 141.149 10.081  54.251  1.000 27.590  ? 141 PHE CCC CA  1 
ATOM 4815  C C   . PHE C 1 124 ? 141.825 9.537   55.514  1.000 25.080  ? 141 PHE CCC C   1 
ATOM 4816  O O   . PHE C 1 124 ? 141.245 9.608   56.605  1.000 24.890  ? 141 PHE CCC O   1 
ATOM 4817  C CB  . PHE C 1 124 ? 140.808 11.576  54.313  1.000 29.790  ? 141 PHE CCC CB  1 
ATOM 4818  C CG  . PHE C 1 124 ? 142.011 12.492  54.364  1.000 29.220  ? 141 PHE CCC CG  1 
ATOM 4819  C CD1 . PHE C 1 124 ? 143.033 12.384  53.432  1.000 29.070  ? 141 PHE CCC CD1 1 
ATOM 4820  C CD2 . PHE C 1 124 ? 142.127 13.455  55.347  1.000 28.940  ? 141 PHE CCC CD2 1 
ATOM 4821  C CE1 . PHE C 1 124 ? 144.127 13.222  53.471  1.000 27.100  ? 141 PHE CCC CE1 1 
ATOM 4822  C CE2 . PHE C 1 124 ? 143.245 14.273  55.402  1.000 28.600  ? 141 PHE CCC CE2 1 
ATOM 4823  C CZ  . PHE C 1 124 ? 144.235 14.160  54.464  1.000 27.570  ? 141 PHE CCC CZ  1 
ATOM 4824  N N   . HIS C 1 125 ? 142.993 8.924   55.351  1.000 24.770  ? 142 HIS CCC N   1 
ATOM 4825  C CA  . HIS C 1 125 ? 143.870 8.481   56.466  1.000 26.230  ? 142 HIS CCC CA  1 
ATOM 4826  C C   . HIS C 1 125 ? 145.078 9.411   56.459  1.000 28.110  ? 142 HIS CCC C   1 
ATOM 4827  O O   . HIS C 1 125 ? 145.730 9.516   55.409  1.000 28.300  ? 142 HIS CCC O   1 
ATOM 4828  C CB  . HIS C 1 125 ? 144.205 6.991   56.394  1.000 25.380  ? 142 HIS CCC CB  1 
ATOM 4829  C CG  . HIS C 1 125 ? 142.979 6.151   56.481  1.000 26.580  ? 142 HIS CCC CG  1 
ATOM 4830  N ND1 . HIS C 1 125 ? 142.340 5.927   57.672  1.000 31.420  ? 142 HIS CCC ND1 1 
ATOM 4831  C CD2 . HIS C 1 125 ? 142.221 5.569   55.529  1.000 27.500  ? 142 HIS CCC CD2 1 
ATOM 4832  C CE1 . HIS C 1 125 ? 141.262 5.203   57.452  1.000 33.530  ? 142 HIS CCC CE1 1 
ATOM 4833  N NE2 . HIS C 1 125 ? 141.160 4.971   56.139  1.000 29.790  ? 142 HIS CCC NE2 1 
ATOM 4834  N N   . PHE C 1 126 ? 145.277 10.119  57.579  1.000 27.430  ? 143 PHE CCC N   1 
ATOM 4835  C CA  . PHE C 1 126 ? 146.248 11.217  57.773  1.000 24.280  ? 143 PHE CCC CA  1 
ATOM 4836  C C   . PHE C 1 126 ? 146.728 11.190  59.215  1.000 23.770  ? 143 PHE CCC C   1 
ATOM 4837  O O   . PHE C 1 126 ? 145.919 10.922  60.119  1.000 22.630  ? 143 PHE CCC O   1 
ATOM 4838  C CB  . PHE C 1 126 ? 145.606 12.571  57.478  1.000 25.350  ? 143 PHE CCC CB  1 
ATOM 4839  C CG  . PHE C 1 126 ? 146.438 13.731  57.964  1.000 26.330  ? 143 PHE CCC CG  1 
ATOM 4840  C CD1 . PHE C 1 126 ? 147.545 14.154  57.248  1.000 26.990  ? 143 PHE CCC CD1 1 
ATOM 4841  C CD2 . PHE C 1 126 ? 146.177 14.341  59.170  1.000 24.910  ? 143 PHE CCC CD2 1 
ATOM 4842  C CE1 . PHE C 1 126 ? 148.336 15.189  57.706  1.000 26.670  ? 143 PHE CCC CE1 1 
ATOM 4843  C CE2 . PHE C 1 126 ? 146.974 15.375  59.631  1.000 25.140  ? 143 PHE CCC CE2 1 
ATOM 4844  C CZ  . PHE C 1 126 ? 148.038 15.812  58.888  1.000 25.980  ? 143 PHE CCC CZ  1 
ATOM 4845  N N   . PHE C 1 127 ? 148.004 11.493  59.432  1.000 25.420  ? 144 PHE CCC N   1 
ATOM 4846  C CA  . PHE C 1 127 ? 148.603 11.627  60.785  1.000 26.010  ? 144 PHE CCC CA  1 
ATOM 4847  C C   . PHE C 1 127 ? 149.911 12.422  60.697  1.000 27.200  ? 144 PHE CCC C   1 
ATOM 4848  O O   . PHE C 1 127 ? 150.678 12.251  59.722  1.000 26.380  ? 144 PHE CCC O   1 
ATOM 4849  C CB  . PHE C 1 127 ? 148.828 10.249  61.393  1.000 24.400  ? 144 PHE CCC CB  1 
ATOM 4850  C CG  . PHE C 1 127 ? 149.784 9.413   60.598  1.000 25.170  ? 144 PHE CCC CG  1 
ATOM 4851  C CD1 . PHE C 1 127 ? 151.147 9.546   60.775  1.000 25.490  ? 144 PHE CCC CD1 1 
ATOM 4852  C CD2 . PHE C 1 127 ? 149.311 8.500   59.664  1.000 25.600  ? 144 PHE CCC CD2 1 
ATOM 4853  C CE1 . PHE C 1 127 ? 152.021 8.764   60.037  1.000 25.480  ? 144 PHE CCC CE1 1 
ATOM 4854  C CE2 . PHE C 1 127 ? 150.193 7.743   58.917  1.000 23.160  ? 144 PHE CCC CE2 1 
ATOM 4855  C CZ  . PHE C 1 127 ? 151.539 7.886   59.102  1.000 23.630  ? 144 PHE CCC CZ  1 
ATOM 4856  N N   . SER C 1 128 ? 150.145 13.258  61.709  1.000 26.900  ? 145 SER CCC N   1 
ATOM 4857  C CA  . SER C 1 128 ? 151.279 14.211  61.797  1.000 27.020  ? 145 SER CCC CA  1 
ATOM 4858  C C   . SER C 1 128 ? 151.898 14.125  63.191  1.000 27.180  ? 145 SER CCC C   1 
ATOM 4859  O O   . SER C 1 128 ? 151.171 13.829  64.149  1.000 24.080  ? 145 SER CCC O   1 
ATOM 4860  C CB  . SER C 1 128 ? 150.823 15.609  61.494  1.000 28.190  ? 145 SER CCC CB  1 
ATOM 4861  O OG  . SER C 1 128 ? 150.389 16.267  62.686  1.000 32.570  ? 145 SER CCC OG  1 
ATOM 4862  N N   . VAL C 1 129 ? 153.211 14.365  63.275  1.000 28.270  ? 146 VAL CCC N   1 
ATOM 4863  C CA  . VAL C 1 129 ? 153.986 14.491  64.541  1.000 28.100  ? 146 VAL CCC CA  1 
ATOM 4864  C C   . VAL C 1 129 ? 154.791 15.790  64.460  1.000 29.680  ? 146 VAL CCC C   1 
ATOM 4865  O O   . VAL C 1 129 ? 155.591 15.959  63.529  1.000 27.200  ? 146 VAL CCC O   1 
ATOM 4866  C CB  . VAL C 1 129 ? 154.876 13.264  64.793  1.000 26.980  ? 146 VAL CCC CB  1 
ATOM 4867  C CG1 . VAL C 1 129 ? 155.674 13.414  66.074  1.000 26.970  ? 146 VAL CCC CG1 1 
ATOM 4868  C CG2 . VAL C 1 129 ? 154.048 11.995  64.839  1.000 28.680  ? 146 VAL CCC CG2 1 
ATOM 4869  N N   . GLY C 1 130 ? 154.552 16.701  65.408  1.000 34.610  ? 147 GLY CCC N   1 
ATOM 4870  C CA  . GLY C 1 130 ? 155.030 18.096  65.353  1.000 36.150  ? 147 GLY CCC CA  1 
ATOM 4871  C C   . GLY C 1 130 ? 155.513 18.585  66.704  1.000 36.500  ? 147 GLY CCC C   1 
ATOM 4872  O O   . GLY C 1 130 ? 154.942 18.141  67.723  1.000 34.220  ? 147 GLY CCC O   1 
ATOM 4873  N N   . GLY C 1 131 ? 156.530 19.467  66.685  1.000 37.310  ? 148 GLY CCC N   1 
ATOM 4874  C CA  . GLY C 1 131 ? 157.003 20.278  67.824  1.000 34.420  ? 148 GLY CCC CA  1 
ATOM 4875  C C   . GLY C 1 131 ? 156.117 21.489  68.079  1.000 32.180  ? 148 GLY CCC C   1 
ATOM 4876  O O   . GLY C 1 131 ? 156.395 22.246  69.040  1.000 32.800  ? 148 GLY CCC O   1 
ATOM 4877  N N   . GLU C 1 132 ? 155.075 21.663  67.263  1.000 28.590  ? 149 GLU CCC N   1 
ATOM 4878  C CA  . GLU C 1 132 ? 154.058 22.733  67.390  1.000 27.380  ? 149 GLU CCC CA  1 
ATOM 4879  C C   . GLU C 1 132 ? 152.829 22.307  66.613  1.000 24.720  ? 149 GLU CCC C   1 
ATOM 4880  O O   . GLU C 1 132 ? 152.890 21.268  65.958  1.000 24.380  ? 149 GLU CCC O   1 
ATOM 4881  C CB  . GLU C 1 132 ? 154.589 24.053  66.838  1.000 28.690  ? 149 GLU CCC CB  1 
ATOM 4882  C CG  . GLU C 1 132 ? 155.691 23.879  65.812  1.000 28.950  ? 149 GLU CCC CG  1 
ATOM 4883  C CD  . GLU C 1 132 ? 156.061 25.137  65.066  1.000 27.690  ? 149 GLU CCC CD  1 
ATOM 4884  O OE1 . GLU C 1 132 ? 155.135 25.816  64.594  1.000 25.800  ? 149 GLU CCC OE1 1 
ATOM 4885  O OE2 . GLU C 1 132 ? 157.248 25.367  64.907  1.000 29.610  ? 149 GLU CCC OE2 1 
ATOM 4886  N N   . ALA C 1 133 ? 151.767 23.093  66.666  1.000 27.150  ? 150 ALA CCC N   1 
ATOM 4887  C CA  . ALA C 1 133 ? 150.513 22.778  65.948  1.000 31.640  ? 150 ALA CCC CA  1 
ATOM 4888  C C   . ALA C 1 133 ? 150.804 22.512  64.470  1.000 32.230  ? 150 ALA CCC C   1 
ATOM 4889  O O   . ALA C 1 133 ? 151.651 23.194  63.895  1.000 29.330  ? 150 ALA CCC O   1 
ATOM 4890  C CB  . ALA C 1 133 ? 149.516 23.895  66.086  1.000 35.180  ? 150 ALA CCC CB  1 
ATOM 4891  N N   . LEU C 1 134 ? 150.101 21.541  63.893  1.000 37.380  ? 151 LEU CCC N   1 
ATOM 4892  C CA  . LEU C 1 134 ? 149.958 21.428  62.421  1.000 37.460  ? 151 LEU CCC CA  1 
ATOM 4893  C C   . LEU C 1 134 ? 149.462 22.767  61.868  1.000 37.460  ? 151 LEU CCC C   1 
ATOM 4894  O O   . LEU C 1 134 ? 148.505 23.330  62.422  1.000 38.890  ? 151 LEU CCC O   1 
ATOM 4895  C CB  . LEU C 1 134 ? 148.960 20.319  62.092  1.000 34.670  ? 151 LEU CCC CB  1 
ATOM 4896  C CG  . LEU C 1 134 ? 148.797 19.983  60.617  1.000 30.010  ? 151 LEU CCC CG  1 
ATOM 4897  C CD1 . LEU C 1 134 ? 150.115 19.467  60.052  1.000 29.230  ? 151 LEU CCC CD1 1 
ATOM 4898  C CD2 . LEU C 1 134 ? 147.692 18.942  60.455  1.000 30.450  ? 151 LEU CCC CD2 1 
ATOM 4899  N N   . GLU C 1 135 ? 150.097 23.247  60.806  1.000 36.310  ? 152 GLU CCC N   1 
ATOM 4900  C CA  . GLU C 1 135 ? 149.703 24.491  60.102  1.000 34.590  ? 152 GLU CCC CA  1 
ATOM 4901  C C   . GLU C 1 135 ? 148.838 24.118  58.890  1.000 32.630  ? 152 GLU CCC C   1 
ATOM 4902  O O   . GLU C 1 135 ? 149.275 23.251  58.087  1.000 31.310  ? 152 GLU CCC O   1 
ATOM 4903  C CB  . GLU C 1 135 ? 150.968 25.265  59.746  1.000 35.970  ? 152 GLU CCC CB  1 
ATOM 4904  C CG  . GLU C 1 135 ? 151.728 25.743  60.965  1.000 37.860  ? 152 GLU CCC CG  1 
ATOM 4905  C CD  . GLU C 1 135 ? 152.953 26.563  60.624  1.000 42.300  ? 152 GLU CCC CD  1 
ATOM 4906  O OE1 . GLU C 1 135 ? 154.047 25.985  60.466  1.000 38.410  ? 152 GLU CCC OE1 1 
ATOM 4907  O OE2 . GLU C 1 135 ? 152.795 27.780  60.485  1.000 56.000  ? 152 GLU CCC OE2 1 
ATOM 4908  N N   . LEU C 1 136 ? 147.663 24.742  58.773  1.000 29.890  ? 153 LEU CCC N   1 
ATOM 4909  C CA  . LEU C 1 136 ? 146.651 24.423  57.729  1.000 32.340  ? 153 LEU CCC CA  1 
ATOM 4910  C C   . LEU C 1 136 ? 146.569 25.515  56.657  1.000 31.890  ? 153 LEU CCC C   1 
ATOM 4911  O O   . LEU C 1 136 ? 146.618 26.718  57.000  1.000 34.220  ? 153 LEU CCC O   1 
ATOM 4912  C CB  . LEU C 1 136 ? 145.273 24.278  58.378  1.000 35.430  ? 153 LEU CCC CB  1 
ATOM 4913  C CG  . LEU C 1 136 ? 145.154 23.264  59.506  1.000 37.150  ? 153 LEU CCC CG  1 
ATOM 4914  C CD1 . LEU C 1 136 ? 143.752 23.292  60.089  1.000 37.720  ? 153 LEU CCC CD1 1 
ATOM 4915  C CD2 . LEU C 1 136 ? 145.495 21.871  59.012  1.000 38.160  ? 153 LEU CCC CD2 1 
ATOM 4916  N N   . GLN C 1 137 ? 146.391 25.088  55.408  1.000 31.090  ? 154 GLN CCC N   1 
ATOM 4917  C CA  . GLN C 1 137 ? 145.956 25.917  54.257  1.000 32.540  ? 154 GLN CCC CA  1 
ATOM 4918  C C   . GLN C 1 137 ? 144.504 25.552  53.954  1.000 33.270  ? 154 GLN CCC C   1 
ATOM 4919  O O   . GLN C 1 137 ? 144.185 24.353  53.886  1.000 39.950  ? 154 GLN CCC O   1 
ATOM 4920  C CB  . GLN C 1 137 ? 146.834 25.629  53.035  1.000 33.870  ? 154 GLN CCC CB  1 
ATOM 4921  C CG  . GLN C 1 137 ? 146.317 26.236  51.738  1.000 33.440  ? 154 GLN CCC CG  1 
ATOM 4922  C CD  . GLN C 1 137 ? 146.317 27.741  51.833  1.000 34.410  ? 154 GLN CCC CD  1 
ATOM 4923  O OE1 . GLN C 1 137 ? 147.265 28.334  52.340  1.000 38.890  ? 154 GLN CCC OE1 1 
ATOM 4924  N NE2 . GLN C 1 137 ? 145.268 28.370  51.352  1.000 30.380  ? 154 GLN CCC NE2 1 
ATOM 4925  N N   . GLY C 1 138 ? 143.645 26.542  53.788  1.000 32.490  ? 155 GLY CCC N   1 
ATOM 4926  C CA  . GLY C 1 138 ? 142.270 26.306  53.333  1.000 31.230  ? 155 GLY CCC CA  1 
ATOM 4927  C C   . GLY C 1 138 ? 142.222 26.110  51.828  1.000 30.920  ? 155 GLY CCC C   1 
ATOM 4928  O O   . GLY C 1 138 ? 142.848 26.907  51.081  1.000 30.990  ? 155 GLY CCC O   1 
ATOM 4929  N N   . VAL C 1 139 ? 141.510 25.085  51.388  1.000 30.990  ? 156 VAL CCC N   1 
ATOM 4930  C CA  . VAL C 1 139 ? 141.120 24.906  49.962  1.000 30.020  ? 156 VAL CCC CA  1 
ATOM 4931  C C   . VAL C 1 139 ? 139.680 24.410  49.957  1.000 29.810  ? 156 VAL CCC C   1 
ATOM 4932  O O   . VAL C 1 139 ? 139.376 23.461  50.716  1.000 31.930  ? 156 VAL CCC O   1 
ATOM 4933  C CB  . VAL C 1 139 ? 142.020 23.915  49.205  1.000 28.490  ? 156 VAL CCC CB  1 
ATOM 4934  C CG1 . VAL C 1 139 ? 141.657 23.877  47.738  1.000 28.580  ? 156 VAL CCC CG1 1 
ATOM 4935  C CG2 . VAL C 1 139 ? 143.494 24.215  49.378  1.000 27.520  ? 156 VAL CCC CG2 1 
ATOM 4936  N N   . LEU C 1 140 ? 138.860 25.010  49.108  1.000 29.620  ? 157 LEU CCC N   1 
ATOM 4937  C CA  . LEU C 1 140 ? 137.396 24.780  49.088  1.000 32.350  ? 157 LEU CCC CA  1 
ATOM 4938  C C   . LEU C 1 140 ? 137.026 24.022  47.810  1.000 30.900  ? 157 LEU CCC C   1 
ATOM 4939  O O   . LEU C 1 140 ? 137.542 24.380  46.732  1.000 29.310  ? 157 LEU CCC O   1 
ATOM 4940  C CB  . LEU C 1 140 ? 136.664 26.130  49.164  1.000 32.330  ? 157 LEU CCC CB  1 
ATOM 4941  C CG  . LEU C 1 140 ? 136.890 26.935  50.441  1.000 32.670  ? 157 LEU CCC CG  1 
ATOM 4942  C CD1 . LEU C 1 140 ? 136.001 28.167  50.447  1.000 34.050  ? 157 LEU CCC CD1 1 
ATOM 4943  C CD2 . LEU C 1 140 ? 136.617 26.106  51.688  1.000 33.280  ? 157 LEU CCC CD2 1 
ATOM 4944  N N   . PHE C 1 141 ? 136.147 23.033  47.924  1.000 30.510  ? 158 PHE CCC N   1 
ATOM 4945  C CA  . PHE C 1 141 ? 135.577 22.383  46.724  1.000 30.300  ? 158 PHE CCC CA  1 
ATOM 4946  C C   . PHE C 1 141 ? 134.720 23.420  46.006  1.000 27.910  ? 158 PHE CCC C   1 
ATOM 4947  O O   . PHE C 1 141 ? 134.844 23.587  44.799  1.000 27.680  ? 158 PHE CCC O   1 
ATOM 4948  C CB  . PHE C 1 141 ? 134.786 21.122  47.077  1.000 30.240  ? 158 PHE CCC CB  1 
ATOM 4949  C CG  . PHE C 1 141 ? 134.153 20.489  45.875  1.000 27.980  ? 158 PHE CCC CG  1 
ATOM 4950  C CD1 . PHE C 1 141 ? 134.921 19.811  44.951  1.000 29.390  ? 158 PHE CCC CD1 1 
ATOM 4951  C CD2 . PHE C 1 141 ? 132.801 20.632  45.643  1.000 29.500  ? 158 PHE CCC CD2 1 
ATOM 4952  C CE1 . PHE C 1 141 ? 134.343 19.264  43.819  1.000 31.960  ? 158 PHE CCC CE1 1 
ATOM 4953  C CE2 . PHE C 1 141 ? 132.210 20.073  44.518  1.000 31.950  ? 158 PHE CCC CE2 1 
ATOM 4954  C CZ  . PHE C 1 141 ? 132.985 19.393  43.608  1.000 33.180  ? 158 PHE CCC CZ  1 
ATOM 4955  N N   . ASN C 1 142 ? 133.885 24.112  46.770  1.000 28.400  ? 159 ASN CCC N   1 
ATOM 4956  C CA  . ASN C 1 142 ? 132.920 25.123  46.269  1.000 28.600  ? 159 ASN CCC CA  1 
ATOM 4957  C C   . ASN C 1 142 ? 133.019 26.321  47.199  1.000 30.770  ? 159 ASN CCC C   1 
ATOM 4958  O O   . ASN C 1 142 ? 132.702 26.117  48.367  1.000 38.600  ? 159 ASN CCC O   1 
ATOM 4959  C CB  . ASN C 1 142 ? 131.504 24.550  46.257  1.000 27.110  ? 159 ASN CCC CB  1 
ATOM 4960  C CG  . ASN C 1 142 ? 130.452 25.540  45.838  1.000 26.970  ? 159 ASN CCC CG  1 
ATOM 4961  O OD1 . ASN C 1 142 ? 130.771 26.628  45.382  1.000 30.380  ? 159 ASN CCC OD1 1 
ATOM 4962  N ND2 . ASN C 1 142 ? 129.197 25.149  45.960  1.000 28.980  ? 159 ASN CCC ND2 1 
ATOM 4963  N N   . TYR C 1 143 ? 133.467 27.491  46.736  1.000 31.280  ? 160 TYR CCC N   1 
ATOM 4964  C CA  . TYR C 1 143 ? 133.743 28.653  47.628  1.000 35.070  ? 160 TYR CCC CA  1 
ATOM 4965  C C   . TYR C 1 143 ? 132.424 29.200  48.203  1.000 34.700  ? 160 TYR CCC C   1 
ATOM 4966  O O   . TYR C 1 143 ? 132.497 29.792  49.312  1.000 34.690  ? 160 TYR CCC O   1 
ATOM 4967  C CB  . TYR C 1 143 ? 134.602 29.731  46.946  1.000 38.220  ? 160 TYR CCC CB  1 
ATOM 4968  C CG  . TYR C 1 143 ? 133.837 30.775  46.165  1.000 36.240  ? 160 TYR CCC CG  1 
ATOM 4969  C CD1 . TYR C 1 143 ? 133.297 30.464  44.934  1.000 35.140  ? 160 TYR CCC CD1 1 
ATOM 4970  C CD2 . TYR C 1 143 ? 133.648 32.057  46.649  1.000 33.600  ? 160 TYR CCC CD2 1 
ATOM 4971  C CE1 . TYR C 1 143 ? 132.583 31.382  44.203  1.000 34.560  ? 160 TYR CCC CE1 1 
ATOM 4972  C CE2 . TYR C 1 143 ? 132.937 32.994  45.920  1.000 33.690  ? 160 TYR CCC CE2 1 
ATOM 4973  C CZ  . TYR C 1 143 ? 132.395 32.650  44.697  1.000 33.480  ? 160 TYR CCC CZ  1 
ATOM 4974  O OH  . TYR C 1 143 ? 131.672 33.527  43.951  1.000 34.940  ? 160 TYR CCC OH  1 
ATOM 4975  N N   . ARG C 1 144 ? 131.283 28.954  47.536  1.000 32.340  ? 161 ARG CCC N   1 
ATOM 4976  C CA  . ARG C 1 144 ? 129.944 29.398  48.000  1.000 34.520  ? 161 ARG CCC CA  1 
ATOM 4977  C C   . ARG C 1 144 ? 129.375 28.435  49.059  1.000 36.130  ? 161 ARG CCC C   1 
ATOM 4978  O O   . ARG C 1 144 ? 128.322 28.786  49.636  1.000 39.700  ? 161 ARG CCC O   1 
ATOM 4979  C CB  . ARG C 1 144 ? 129.013 29.641  46.809  1.000 41.150  ? 161 ARG CCC CB  1 
ATOM 4980  C CG  . ARG C 1 144 ? 128.980 31.096  46.308  1.000 49.850  ? 161 ARG CCC CG  1 
ATOM 4981  C CD  . ARG C 1 144 ? 128.674 31.416  44.841  1.000 53.420  ? 161 ARG CCC CD  1 
ATOM 4982  N NE  . ARG C 1 144 ? 129.207 30.344  44.007  1.000 62.040  ? 161 ARG CCC NE  1 
ATOM 4983  C CZ  . ARG C 1 144 ? 128.689 29.883  42.861  1.000 62.380  ? 161 ARG CCC CZ  1 
ATOM 4984  N NH1 . ARG C 1 144 ? 127.618 30.440  42.314  1.000 62.480  ? 161 ARG CCC NH1 1 
ATOM 4985  N NH2 . ARG C 1 144 ? 129.295 28.869  42.258  1.000 58.960  ? 161 ARG CCC NH2 1 
ATOM 4986  N N   . THR C 1 145 ? 130.054 27.322  49.385  1.000 38.670  ? 162 THR CCC N   1 
ATOM 4987  C CA  . THR C 1 145 ? 129.706 26.433  50.544  1.000 35.480  ? 162 THR CCC CA  1 
ATOM 4988  C C   . THR C 1 145 ? 129.702 27.268  51.824  1.000 32.490  ? 162 THR CCC C   1 
ATOM 4989  O O   . THR C 1 145 ? 130.735 27.873  52.060  1.000 37.290  ? 162 THR CCC O   1 
ATOM 4990  C CB  . THR C 1 145 ? 130.706 25.282  50.784  1.000 36.500  ? 162 THR CCC CB  1 
ATOM 4991  O OG1 . THR C 1 145 ? 130.859 24.368  49.688  1.000 36.760  ? 162 THR CCC OG1 1 
ATOM 4992  C CG2 . THR C 1 145 ? 130.300 24.463  51.997  1.000 39.990  ? 162 THR CCC CG2 1 
ATOM 4993  N N   . LYS C 1 146 ? 128.615 27.290  52.600  1.000 31.910  ? 163 LYS CCC N   1 
ATOM 4994  C CA  . LYS C 1 146 ? 128.535 27.965  53.923  1.000 32.950  ? 163 LYS CCC CA  1 
ATOM 4995  C C   . LYS C 1 146 ? 128.879 26.964  55.026  1.000 32.010  ? 163 LYS CCC C   1 
ATOM 4996  O O   . LYS C 1 146 ? 127.993 26.154  55.377  1.000 28.010  ? 163 LYS CCC O   1 
ATOM 4997  C CB  . LYS C 1 146 ? 127.135 28.505  54.217  1.000 37.790  ? 163 LYS CCC CB  1 
ATOM 4998  C CG  . LYS C 1 146 ? 127.048 29.207  55.570  1.000 43.550  ? 163 LYS CCC CG  1 
ATOM 4999  C CD  . LYS C 1 146 ? 125.696 29.725  56.000  1.000 48.750  ? 163 LYS CCC CD  1 
ATOM 5000  C CE  . LYS C 1 146 ? 125.828 30.447  57.328  1.000 53.020  ? 163 LYS CCC CE  1 
ATOM 5001  N NZ  . LYS C 1 146 ? 124.631 31.267  57.637  1.000 62.720  ? 163 LYS CCC NZ  1 
ATOM 5002  N N   . TYR C 1 147 ? 130.087 27.040  55.590  1.000 34.680  ? 164 TYR CCC N   1 
ATOM 5003  C CA  . TYR C 1 147 ? 130.522 26.093  56.653  1.000 36.250  ? 164 TYR CCC CA  1 
ATOM 5004  C C   . TYR C 1 147 ? 129.798 26.466  57.936  1.000 34.320  ? 164 TYR CCC C   1 
ATOM 5005  O O   . TYR C 1 147 ? 129.627 27.639  58.220  1.000 33.930  ? 164 TYR CCC O   1 
ATOM 5006  C CB  . TYR C 1 147 ? 132.050 25.980  56.717  1.000 35.840  ? 164 TYR CCC CB  1 
ATOM 5007  C CG  . TYR C 1 147 ? 132.594 25.146  55.585  1.000 36.010  ? 164 TYR CCC CG  1 
ATOM 5008  C CD1 . TYR C 1 147 ? 132.873 25.709  54.365  1.000 36.080  ? 164 TYR CCC CD1 1 
ATOM 5009  C CD2 . TYR C 1 147 ? 132.719 23.774  55.690  1.000 38.700  ? 164 TYR CCC CD2 1 
ATOM 5010  C CE1 . TYR C 1 147 ? 133.312 24.949  53.295  1.000 38.120  ? 164 TYR CCC CE1 1 
ATOM 5011  C CE2 . TYR C 1 147 ? 133.156 23.000  54.627  1.000 38.630  ? 164 TYR CCC CE2 1 
ATOM 5012  C CZ  . TYR C 1 147 ? 133.455 23.586  53.415  1.000 39.260  ? 164 TYR CCC CZ  1 
ATOM 5013  O OH  . TYR C 1 147 ? 133.880 22.859  52.329  1.000 47.950  ? 164 TYR CCC OH  1 
ATOM 5014  N N   . PRO C 1 148 ? 129.319 25.481  58.722  1.000 38.500  ? 165 PRO CCC N   1 
ATOM 5015  C CA  . PRO C 1 148 ? 128.310 25.724  59.738  1.000 39.120  ? 165 PRO CCC CA  1 
ATOM 5016  C C   . PRO C 1 148 ? 128.939 26.343  60.995  1.000 40.240  ? 165 PRO CCC C   1 
ATOM 5017  O O   . PRO C 1 148 ? 130.063 26.031  61.360  1.000 35.050  ? 165 PRO CCC O   1 
ATOM 5018  C CB  . PRO C 1 148 ? 127.790 24.319  60.062  1.000 40.920  ? 165 PRO CCC CB  1 
ATOM 5019  C CG  . PRO C 1 148 ? 129.026 23.463  59.946  1.000 41.170  ? 165 PRO CCC CG  1 
ATOM 5020  C CD  . PRO C 1 148 ? 129.820 24.099  58.805  1.000 44.210  ? 165 PRO CCC CD  1 
ATOM 5021  N N   . ASP C 1 149 ? 128.170 27.236  61.598  1.000 41.670  ? 166 ASP CCC N   1 
ATOM 5022  C CA  . ASP C 1 149 ? 128.389 27.826  62.932  1.000 42.180  ? 166 ASP CCC CA  1 
ATOM 5023  C C   . ASP C 1 149 ? 128.922 26.758  63.902  1.000 36.790  ? 166 ASP CCC C   1 
ATOM 5024  O O   . ASP C 1 149 ? 128.260 25.747  64.112  1.000 31.950  ? 166 ASP CCC O   1 
ATOM 5025  C CB  . ASP C 1 149 ? 127.057 28.430  63.366  1.000 49.510  ? 166 ASP CCC CB  1 
ATOM 5026  C CG  . ASP C 1 149 ? 127.242 29.616  64.270  1.000 55.900  ? 166 ASP CCC CG  1 
ATOM 5027  O OD1 . ASP C 1 149 ? 127.919 29.414  65.310  1.000 62.450  ? 166 ASP CCC OD1 1 
ATOM 5028  O OD2 . ASP C 1 149 ? 126.764 30.735  63.884  1.000 56.300  ? 166 ASP CCC OD2 1 
ATOM 5029  N N   . GLY C 1 150 ? 130.101 26.965  64.475  1.000 34.050  ? 167 GLY CCC N   1 
ATOM 5030  C CA  . GLY C 1 150 ? 130.677 26.057  65.482  1.000 32.820  ? 167 GLY CCC CA  1 
ATOM 5031  C C   . GLY C 1 150 ? 131.949 25.390  65.002  1.000 31.090  ? 167 GLY CCC C   1 
ATOM 5032  O O   . GLY C 1 150 ? 132.638 24.740  65.830  1.000 27.640  ? 167 GLY CCC O   1 
ATOM 5033  N N   . THR C 1 151 ? 132.241 25.522  63.710  1.000 34.590  ? 168 THR CCC N   1 
ATOM 5034  C CA  . THR C 1 151 ? 133.477 25.009  63.037  1.000 37.460  ? 168 THR CCC CA  1 
ATOM 5035  C C   . THR C 1 151 ? 134.342 26.209  62.666  1.000 35.790  ? 168 THR CCC C   1 
ATOM 5036  O O   . THR C 1 151 ? 133.769 27.266  62.396  1.000 41.120  ? 168 THR CCC O   1 
ATOM 5037  C CB  . THR C 1 151 ? 133.125 24.221  61.768  1.000 36.430  ? 168 THR CCC CB  1 
ATOM 5038  O OG1 . THR C 1 151 ? 132.485 25.089  60.829  1.000 36.910  ? 168 THR CCC OG1 1 
ATOM 5039  C CG2 . THR C 1 151 ? 132.194 23.071  62.057  1.000 37.550  ? 168 THR CCC CG2 1 
ATOM 5040  N N   . ILE C 1 152 ? 135.654 26.040  62.640  1.000 31.330  ? 169 ILE CCC N   1 
ATOM 5041  C CA  . ILE C 1 152 ? 136.605 27.065  62.145  1.000 29.780  ? 169 ILE CCC CA  1 
ATOM 5042  C C   . ILE C 1 152 ? 136.841 26.777  60.661  1.000 29.490  ? 169 ILE CCC C   1 
ATOM 5043  O O   . ILE C 1 152 ? 137.356 25.710  60.331  1.000 24.550  ? 169 ILE CCC O   1 
ATOM 5044  C CB  . ILE C 1 152 ? 137.867 27.020  63.009  1.000 30.800  ? 169 ILE CCC CB  1 
ATOM 5045  C CG1 . ILE C 1 152 ? 137.560 27.457  64.438  1.000 31.500  ? 169 ILE CCC CG1 1 
ATOM 5046  C CG2 . ILE C 1 152 ? 139.012 27.836  62.429  1.000 31.530  ? 169 ILE CCC CG2 1 
ATOM 5047  C CD1 . ILE C 1 152 ? 138.618 27.027  65.412  1.000 32.920  ? 169 ILE CCC CD1 1 
ATOM 5048  N N   . PHE C 1 153 ? 136.458 27.704  59.790  1.000 32.660  ? 170 PHE CCC N   1 
ATOM 5049  C CA  . PHE C 1 153 ? 136.525 27.517  58.327  1.000 34.310  ? 170 PHE CCC CA  1 
ATOM 5050  C C   . PHE C 1 153 ? 137.237 28.689  57.670  1.000 35.820  ? 170 PHE CCC C   1 
ATOM 5051  O O   . PHE C 1 153 ? 137.402 29.731  58.279  1.000 44.380  ? 170 PHE CCC O   1 
ATOM 5052  C CB  . PHE C 1 153 ? 135.112 27.367  57.784  1.000 35.060  ? 170 PHE CCC CB  1 
ATOM 5053  C CG  . PHE C 1 153 ? 134.156 28.449  58.190  1.000 36.920  ? 170 PHE CCC CG  1 
ATOM 5054  C CD1 . PHE C 1 153 ? 133.508 28.391  59.406  1.000 38.740  ? 170 PHE CCC CD1 1 
ATOM 5055  C CD2 . PHE C 1 153 ? 133.877 29.503  57.336  1.000 38.360  ? 170 PHE CCC CD2 1 
ATOM 5056  C CE1 . PHE C 1 153 ? 132.611 29.383  59.774  1.000 43.470  ? 170 PHE CCC CE1 1 
ATOM 5057  C CE2 . PHE C 1 153 ? 132.965 30.482  57.694  1.000 40.200  ? 170 PHE CCC CE2 1 
ATOM 5058  C CZ  . PHE C 1 153 ? 132.342 30.429  58.917  1.000 43.020  ? 170 PHE CCC CZ  1 
ATOM 5059  N N   . PRO C 1 154 ? 137.696 28.543  56.414  1.000 38.110  ? 171 PRO CCC N   1 
ATOM 5060  C CA  . PRO C 1 154 ? 138.215 29.656  55.625  1.000 40.640  ? 171 PRO CCC CA  1 
ATOM 5061  C C   . PRO C 1 154 ? 137.256 30.842  55.587  1.000 38.040  ? 171 PRO CCC C   1 
ATOM 5062  O O   . PRO C 1 154 ? 136.133 30.655  55.197  1.000 35.720  ? 171 PRO CCC O   1 
ATOM 5063  C CB  . PRO C 1 154 ? 138.329 29.064  54.217  1.000 44.950  ? 171 PRO CCC CB  1 
ATOM 5064  C CG  . PRO C 1 154 ? 138.664 27.629  54.511  1.000 45.970  ? 171 PRO CCC CG  1 
ATOM 5065  C CD  . PRO C 1 154 ? 137.772 27.283  55.679  1.000 42.110  ? 171 PRO CCC CD  1 
ATOM 5066  N N   . LYS C 1 155 ? 137.749 32.000  56.008  1.000 39.930  ? 172 LYS CCC N   1 
ATOM 5067  C CA  . LYS C 1 155 ? 136.984 33.266  56.079  1.000 42.340  ? 172 LYS CCC CA  1 
ATOM 5068  C C   . LYS C 1 155 ? 137.343 34.080  54.836  1.000 38.100  ? 172 LYS CCC C   1 
ATOM 5069  O O   . LYS C 1 155 ? 138.478 33.953  54.369  1.000 36.090  ? 172 LYS CCC O   1 
ATOM 5070  C CB  . LYS C 1 155 ? 137.303 34.007  57.379  1.000 46.770  ? 172 LYS CCC CB  1 
ATOM 5071  C CG  . LYS C 1 155 ? 136.879 33.299  58.660  1.000 49.920  ? 172 LYS CCC CG  1 
ATOM 5072  C CD  . LYS C 1 155 ? 137.359 33.993  59.910  1.000 57.660  ? 172 LYS CCC CD  1 
ATOM 5073  C CE  . LYS C 1 155 ? 138.814 33.731  60.253  1.000 62.630  ? 172 LYS CCC CE  1 
ATOM 5074  N NZ  . LYS C 1 155 ? 138.996 32.480  61.034  1.000 64.920  ? 172 LYS CCC NZ  1 
ATOM 5075  N N   . ASN C 1 156 ? 136.388 34.855  54.328  1.000 38.610  ? 173 ASN CCC N   1 
ATOM 5076  C CA  . ASN C 1 156 ? 136.557 35.765  53.163  1.000 39.120  ? 173 ASN CCC CA  1 
ATOM 5077  C C   . ASN C 1 156 ? 136.822 34.933  51.911  1.000 36.480  ? 173 ASN CCC C   1 
ATOM 5078  O O   . ASN C 1 156 ? 137.722 35.296  51.132  1.000 34.680  ? 173 ASN CCC O   1 
ATOM 5079  C CB  . ASN C 1 156 ? 137.662 36.791  53.410  1.000 41.150  ? 173 ASN CCC CB  1 
ATOM 5080  C CG  . ASN C 1 156 ? 137.346 37.666  54.600  1.000 40.700  ? 173 ASN CCC CG  1 
ATOM 5081  O OD1 . ASN C 1 156 ? 136.233 38.180  54.719  1.000 43.310  ? 173 ASN CCC OD1 1 
ATOM 5082  N ND2 . ASN C 1 156 ? 138.302 37.797  55.498  1.000 38.640  ? 173 ASN CCC ND2 1 
ATOM 5083  N N   . ALA C 1 157 ? 136.071 33.850  51.751  1.000 35.700  ? 174 ALA CCC N   1 
ATOM 5084  C CA  . ALA C 1 157 ? 136.164 32.945  50.588  1.000 34.260  ? 174 ALA CCC CA  1 
ATOM 5085  C C   . ALA C 1 157 ? 135.943 33.752  49.317  1.000 33.280  ? 174 ALA CCC C   1 
ATOM 5086  O O   . ALA C 1 157 ? 134.982 34.523  49.267  1.000 36.050  ? 174 ALA CCC O   1 
ATOM 5087  C CB  . ALA C 1 157 ? 135.147 31.843  50.700  1.000 35.100  ? 174 ALA CCC CB  1 
ATOM 5088  N N   . THR C 1 158 ? 136.831 33.579  48.352  1.000 31.760  ? 175 THR CCC N   1 
ATOM 5089  C CA  . THR C 1 158 ? 136.690 34.094  46.975  1.000 32.120  ? 175 THR CCC CA  1 
ATOM 5090  C C   . THR C 1 158 ? 136.701 32.884  46.036  1.000 32.810  ? 175 THR CCC C   1 
ATOM 5091  O O   . THR C 1 158 ? 137.022 31.757  46.491  1.000 30.800  ? 175 THR CCC O   1 
ATOM 5092  C CB  . THR C 1 158 ? 137.768 35.153  46.744  1.000 33.570  ? 175 THR CCC CB  1 
ATOM 5093  O OG1 . THR C 1 158 ? 139.053 34.557  46.554  1.000 34.210  ? 175 THR CCC OG1 1 
ATOM 5094  C CG2 . THR C 1 158 ? 137.847 36.100  47.919  1.000 36.640  ? 175 THR CCC CG2 1 
ATOM 5095  N N   . VAL C 1 159 ? 136.347 33.080  44.771  1.000 31.010  ? 176 VAL CCC N   1 
ATOM 5096  C CA  . VAL C 1 159 ? 136.455 31.978  43.788  1.000 29.790  ? 176 VAL CCC CA  1 
ATOM 5097  C C   . VAL C 1 159 ? 137.886 31.430  43.852  1.000 27.780  ? 176 VAL CCC C   1 
ATOM 5098  O O   . VAL C 1 159 ? 138.031 30.206  43.767  1.000 27.850  ? 176 VAL CCC O   1 
ATOM 5099  C CB  . VAL C 1 159 ? 136.051 32.428  42.378  1.000 32.390  ? 176 VAL CCC CB  1 
ATOM 5100  C CG1 . VAL C 1 159 ? 137.198 33.138  41.655  1.000 30.830  ? 176 VAL CCC CG1 1 
ATOM 5101  C CG2 . VAL C 1 159 ? 135.506 31.244  41.572  1.000 32.710  ? 176 VAL CCC CG2 1 
ATOM 5102  N N   . GLN C 1 160 ? 138.908 32.270  44.047  1.000 26.680  ? 177 GLN CCC N   1 
ATOM 5103  C CA  . GLN C 1 160 ? 140.320 31.796  44.100  1.000 28.230  ? 177 GLN CCC CA  1 
ATOM 5104  C C   . GLN C 1 160 ? 140.472 30.768  45.212  1.000 29.950  ? 177 GLN CCC C   1 
ATOM 5105  O O   . GLN C 1 160 ? 141.343 29.906  45.066  1.000 30.260  ? 177 GLN CCC O   1 
ATOM 5106  C CB  . GLN C 1 160 ? 141.334 32.926  44.268  1.000 28.500  ? 177 GLN CCC CB  1 
ATOM 5107  C CG  . GLN C 1 160 ? 141.377 33.866  43.073  1.000 31.850  ? 177 GLN CCC CG  1 
ATOM 5108  C CD  . GLN C 1 160 ? 141.587 33.205  41.721  1.000 37.100  ? 177 GLN CCC CD  1 
ATOM 5109  O OE1 . GLN C 1 160 ? 142.492 32.375  41.565  1.000 40.940  ? 177 GLN CCC OE1 1 
ATOM 5110  N NE2 . GLN C 1 160 ? 140.795 33.597  40.711  1.000 34.730  ? 177 GLN CCC NE2 1 
ATOM 5111  N N   . SER C 1 161 ? 139.647 30.836  46.259  1.000 34.280  ? 178 SER CCC N   1 
ATOM 5112  C CA  . SER C 1 161 ? 139.693 29.880  47.401  1.000 35.480  ? 178 SER CCC CA  1 
ATOM 5113  C C   . SER C 1 161 ? 139.594 28.433  46.880  1.000 35.930  ? 178 SER CCC C   1 
ATOM 5114  O O   . SER C 1 161 ? 140.272 27.556  47.490  1.000 39.980  ? 178 SER CCC O   1 
ATOM 5115  C CB  . SER C 1 161 ? 138.635 30.192  48.435  1.000 32.650  ? 178 SER CCC CB  1 
ATOM 5116  O OG  . SER C 1 161 ? 138.881 31.465  49.018  1.000 31.430  ? 178 SER CCC OG  1 
ATOM 5117  N N   . GLN C 1 162 ? 138.840 28.224  45.782  1.000 29.640  ? 179 GLN CCC N   1 
ATOM 5118  C CA  . GLN C 1 162 ? 138.588 26.914  45.121  1.000 25.870  ? 179 GLN CCC CA  1 
ATOM 5119  C C   . GLN C 1 162 ? 139.879 26.272  44.597  1.000 25.390  ? 179 GLN CCC C   1 
ATOM 5120  O O   . GLN C 1 162 ? 139.876 25.044  44.431  1.000 23.620  ? 179 GLN CCC O   1 
ATOM 5121  C CB  . GLN C 1 162 ? 137.595 27.062  43.967  1.000 24.680  ? 179 GLN CCC CB  1 
ATOM 5122  C CG  . GLN C 1 162 ? 136.149 26.776  44.371  1.000 24.860  ? 179 GLN CCC CG  1 
ATOM 5123  C CD  . GLN C 1 162 ? 135.117 27.336  43.415  1.000 24.920  ? 179 GLN CCC CD  1 
ATOM 5124  O OE1 . GLN C 1 162 ? 133.954 27.511  43.772  1.000 29.080  ? 179 GLN CCC OE1 1 
ATOM 5125  N NE2 . GLN C 1 162 ? 135.513 27.639  42.189  1.000 23.390  ? 179 GLN CCC NE2 1 
ATOM 5126  N N   . VAL C 1 163 ? 140.928 27.039  44.286  1.000 26.650  ? 180 VAL CCC N   1 
ATOM 5127  C CA  . VAL C 1 163 ? 142.183 26.453  43.716  1.000 27.110  ? 180 VAL CCC CA  1 
ATOM 5128  C C   . VAL C 1 163 ? 143.359 26.753  44.634  1.000 28.710  ? 180 VAL CCC C   1 
ATOM 5129  O O   . VAL C 1 163 ? 144.133 25.793  44.919  1.000 29.320  ? 180 VAL CCC O   1 
ATOM 5130  C CB  . VAL C 1 163 ? 142.480 26.919  42.280  1.000 26.760  ? 180 VAL CCC CB  1 
ATOM 5131  C CG1 . VAL C 1 163 ? 141.466 26.359  41.302  1.000 27.050  ? 180 VAL CCC CG1 1 
ATOM 5132  C CG2 . VAL C 1 163 ? 142.596 28.424  42.144  1.000 26.200  ? 180 VAL CCC CG2 1 
ATOM 5133  N N   . MET C 1 164 ? 143.470 28.007  45.073  1.000 32.210  ? 181 MET CCC N   1 
ATOM 5134  C CA  . MET C 1 164 ? 144.456 28.450  46.094  1.000 37.360  ? 181 MET CCC CA  1 
ATOM 5135  C C   . MET C 1 164 ? 144.213 29.918  46.488  1.000 36.330  ? 181 MET CCC C   1 
ATOM 5136  O O   . MET C 1 164 ? 144.067 30.772  45.577  1.000 37.620  ? 181 MET CCC O   1 
ATOM 5137  C CB  . MET C 1 164 ? 145.875 28.295  45.544  1.000 39.390  ? 181 MET CCC CB  1 
ATOM 5138  C CG  . MET C 1 164 ? 146.933 28.538  46.576  1.000 42.540  ? 181 MET CCC CG  1 
ATOM 5139  S SD  . MET C 1 164 ? 146.807 27.412  47.962  1.000 46.830  ? 181 MET CCC SD  1 
ATOM 5140  C CE  . MET C 1 164 ? 147.967 28.196  49.080  1.000 51.510  ? 181 MET CCC CE  1 
ATOM 5141  N N   . ASN C 1 165 ? 144.216 30.215  47.788  1.000 33.390  ? 182 ASN CCC N   1 
ATOM 5142  C CA  . ASN C 1 165 ? 144.042 31.601  48.309  1.000 30.540  ? 182 ASN CCC CA  1 
ATOM 5143  C C   . ASN C 1 165 ? 144.812 31.747  49.628  1.000 29.620  ? 182 ASN CCC C   1 
ATOM 5144  O O   . ASN C 1 165 ? 144.338 31.215  50.643  1.000 28.080  ? 182 ASN CCC O   1 
ATOM 5145  C CB  . ASN C 1 165 ? 142.554 31.901  48.440  1.000 29.910  ? 182 ASN CCC CB  1 
ATOM 5146  C CG  . ASN C 1 165 ? 142.250 33.190  49.161  1.000 29.410  ? 182 ASN CCC CG  1 
ATOM 5147  O OD1 . ASN C 1 165 ? 143.116 33.743  49.831  1.000 28.470  ? 182 ASN CCC OD1 1 
ATOM 5148  N ND2 . ASN C 1 165 ? 141.020 33.653  49.043  1.000 27.940  ? 182 ASN CCC ND2 1 
ATOM 5149  N N   . THR C 1 166 ? 145.951 32.447  49.614  1.000 29.540  ? 183 THR CCC N   1 
ATOM 5150  C CA  . THR C 1 166 ? 146.911 32.473  50.748  1.000 31.280  ? 183 THR CCC CA  1 
ATOM 5151  C C   . THR C 1 166 ? 146.310 33.136  51.994  1.000 31.280  ? 183 THR CCC C   1 
ATOM 5152  O O   . THR C 1 166 ? 146.959 32.992  53.061  1.000 29.360  ? 183 THR CCC O   1 
ATOM 5153  C CB  . THR C 1 166 ? 148.211 33.178  50.371  1.000 31.850  ? 183 THR CCC CB  1 
ATOM 5154  O OG1 . THR C 1 166 ? 147.785 34.222  49.509  1.000 32.770  ? 183 THR CCC OG1 1 
ATOM 5155  C CG2 . THR C 1 166 ? 149.214 32.281  49.675  1.000 32.860  ? 183 THR CCC CG2 1 
ATOM 5156  N N   . GLU C 1 167 ? 145.142 33.785  51.892  1.000 32.810  ? 184 GLU CCC N   1 
ATOM 5157  C CA  . GLU C 1 167 ? 144.445 34.324  53.089  1.000 34.670  ? 184 GLU CCC CA  1 
ATOM 5158  C C   . GLU C 1 167 ? 144.182 33.179  54.080  1.000 32.630  ? 184 GLU CCC C   1 
ATOM 5159  O O   . GLU C 1 167 ? 144.439 33.379  55.261  1.000 32.320  ? 184 GLU CCC O   1 
ATOM 5160  C CB  . GLU C 1 167 ? 143.149 35.072  52.760  1.000 38.220  ? 184 GLU CCC CB  1 
ATOM 5161  C CG  . GLU C 1 167 ? 142.895 36.220  53.730  1.000 42.950  ? 184 GLU CCC CG  1 
ATOM 5162  C CD  . GLU C 1 167 ? 141.463 36.718  53.884  1.000 48.710  ? 184 GLU CCC CD  1 
ATOM 5163  O OE1 . GLU C 1 167 ? 140.844 36.385  54.920  1.000 56.060  ? 184 GLU CCC OE1 1 
ATOM 5164  O OE2 . GLU C 1 167 ? 140.985 37.485  53.013  1.000 50.760  ? 184 GLU CCC OE2 1 
ATOM 5165  N N   . HIS C 1 168 ? 143.751 32.010  53.601  1.000 31.240  ? 185 HIS CCC N   1 
ATOM 5166  C CA  . HIS C 1 168 ? 143.239 30.883  54.428  1.000 29.410  ? 185 HIS CCC CA  1 
ATOM 5167  C C   . HIS C 1 168 ? 144.366 30.122  55.136  1.000 25.580  ? 185 HIS CCC C   1 
ATOM 5168  O O   . HIS C 1 168 ? 144.558 28.927  54.823  1.000 24.480  ? 185 HIS CCC O   1 
ATOM 5169  C CB  . HIS C 1 168 ? 142.420 29.924  53.561  1.000 29.080  ? 185 HIS CCC CB  1 
ATOM 5170  C CG  . HIS C 1 168 ? 141.363 30.613  52.788  1.000 29.170  ? 185 HIS CCC CG  1 
ATOM 5171  N ND1 . HIS C 1 168 ? 140.537 31.535  53.362  1.000 30.880  ? 185 HIS CCC ND1 1 
ATOM 5172  C CD2 . HIS C 1 168 ? 141.016 30.522  51.492  1.000 31.530  ? 185 HIS CCC CD2 1 
ATOM 5173  C CE1 . HIS C 1 168 ? 139.684 31.970  52.448  1.000 32.900  ? 185 HIS CCC CE1 1 
ATOM 5174  N NE2 . HIS C 1 168 ? 139.965 31.359  51.288  1.000 30.290  ? 185 HIS CCC NE2 1 
ATOM 5175  N N   . LYS C 1 169 ? 145.038 30.763  56.085  1.000 24.390  ? 186 LYS CCC N   1 
ATOM 5176  C CA  . LYS C 1 169 ? 145.971 30.067  57.013  1.000 28.540  ? 186 LYS CCC CA  1 
ATOM 5177  C C   . LYS C 1 169 ? 145.291 29.888  58.374  1.000 28.130  ? 186 LYS CCC C   1 
ATOM 5178  O O   . LYS C 1 169 ? 144.284 30.589  58.639  1.000 27.810  ? 186 LYS CCC O   1 
ATOM 5179  C CB  . LYS C 1 169 ? 147.289 30.832  57.117  1.000 32.230  ? 186 LYS CCC CB  1 
ATOM 5180  C CG  . LYS C 1 169 ? 147.854 31.270  55.768  1.000 37.790  ? 186 LYS CCC CG  1 
ATOM 5181  C CD  . LYS C 1 169 ? 148.446 30.134  54.965  1.000 38.370  ? 186 LYS CCC CD  1 
ATOM 5182  C CE  . LYS C 1 169 ? 149.241 30.641  53.787  1.000 39.790  ? 186 LYS CCC CE  1 
ATOM 5183  N NZ  . LYS C 1 169 ? 149.834 29.536  53.006  1.000 45.290  ? 186 LYS CCC NZ  1 
ATOM 5184  N N   . ALA C 1 170 ? 145.781 28.942  59.174  1.000 27.750  ? 187 ALA CCC N   1 
ATOM 5185  C CA  . ALA C 1 170 ? 145.158 28.522  60.448  1.000 29.420  ? 187 ALA CCC CA  1 
ATOM 5186  C C   . ALA C 1 170 ? 146.027 27.481  61.160  1.000 27.880  ? 187 ALA CCC C   1 
ATOM 5187  O O   . ALA C 1 170 ? 146.788 26.775  60.489  1.000 28.520  ? 187 ALA CCC O   1 
ATOM 5188  C CB  . ALA C 1 170 ? 143.784 27.962  60.167  1.000 31.130  ? 187 ALA CCC CB  1 
ATOM 5189  N N   . TYR C 1 171 ? 145.872 27.357  62.473  1.000 26.790  ? 188 TYR CCC N   1 
ATOM 5190  C CA  . TYR C 1 171 ? 146.577 26.362  63.303  1.000 31.980  ? 188 TYR CCC CA  1 
ATOM 5191  C C   . TYR C 1 171 ? 145.590 25.273  63.746  1.000 33.460  ? 188 TYR CCC C   1 
ATOM 5192  O O   . TYR C 1 171 ? 144.484 25.612  64.199  1.000 34.900  ? 188 TYR CCC O   1 
ATOM 5193  C CB  . TYR C 1 171 ? 147.229 27.072  64.493  1.000 36.440  ? 188 TYR CCC CB  1 
ATOM 5194  C CG  . TYR C 1 171 ? 148.346 28.018  64.132  1.000 39.720  ? 188 TYR CCC CG  1 
ATOM 5195  C CD1 . TYR C 1 171 ? 149.622 27.532  63.893  1.000 44.780  ? 188 TYR CCC CD1 1 
ATOM 5196  C CD2 . TYR C 1 171 ? 148.142 29.385  64.038  1.000 40.810  ? 188 TYR CCC CD2 1 
ATOM 5197  C CE1 . TYR C 1 171 ? 150.661 28.374  63.540  1.000 47.880  ? 188 TYR CCC CE1 1 
ATOM 5198  C CE2 . TYR C 1 171 ? 149.165 30.239  63.670  1.000 43.250  ? 188 TYR CCC CE2 1 
ATOM 5199  C CZ  . TYR C 1 171 ? 150.429 29.733  63.428  1.000 45.590  ? 188 TYR CCC CZ  1 
ATOM 5200  O OH  . TYR C 1 171 ? 151.467 30.553  63.093  1.000 45.120  ? 188 TYR CCC OH  1 
ATOM 5201  N N   . LEU C 1 172 ? 145.955 23.999  63.600  1.000 33.950  ? 189 LEU CCC N   1 
ATOM 5202  C CA  . LEU C 1 172 ? 145.171 22.877  64.171  1.000 35.030  ? 189 LEU CCC CA  1 
ATOM 5203  C C   . LEU C 1 172 ? 145.429 22.865  65.677  1.000 36.270  ? 189 LEU CCC C   1 
ATOM 5204  O O   . LEU C 1 172 ? 146.323 22.096  66.148  1.000 36.600  ? 189 LEU CCC O   1 
ATOM 5205  C CB  . LEU C 1 172 ? 145.538 21.539  63.530  1.000 34.380  ? 189 LEU CCC CB  1 
ATOM 5206  C CG  . LEU C 1 172 ? 144.652 20.370  63.972  1.000 34.020  ? 189 LEU CCC CG  1 
ATOM 5207  C CD1 . LEU C 1 172 ? 143.168 20.706  63.904  1.000 31.920  ? 189 LEU CCC CD1 1 
ATOM 5208  C CD2 . LEU C 1 172 ? 144.937 19.140  63.136  1.000 37.200  ? 189 LEU CCC CD2 1 
ATOM 5209  N N   . ASP C 1 173 ? 144.658 23.702  66.374  1.000 35.740  ? 190 ASP CCC N   1 
ATOM 5210  C CA  . ASP C 1 173 ? 144.834 24.067  67.800  1.000 35.720  ? 190 ASP CCC CA  1 
ATOM 5211  C C   . ASP C 1 173 ? 143.569 23.724  68.590  1.000 36.330  ? 190 ASP CCC C   1 
ATOM 5212  O O   . ASP C 1 173 ? 143.535 24.065  69.774  1.000 39.220  ? 190 ASP CCC O   1 
ATOM 5213  C CB  . ASP C 1 173 ? 145.132 25.561  67.925  1.000 36.140  ? 190 ASP CCC CB  1 
ATOM 5214  C CG  . ASP C 1 173 ? 144.106 26.463  67.238  1.000 39.490  ? 190 ASP CCC CG  1 
ATOM 5215  O OD1 . ASP C 1 173 ? 142.990 25.991  66.912  1.000 37.450  ? 190 ASP CCC OD1 1 
ATOM 5216  O OD2 . ASP C 1 173 ? 144.424 27.641  67.025  1.000 46.230  ? 190 ASP CCC OD2 1 
ATOM 5217  N N   . LYS C 1 174 ? 142.567 23.081  67.977  1.000 37.030  ? 191 LYS CCC N   1 
ATOM 5218  C CA  . LYS C 1 174 ? 141.257 22.835  68.629  1.000 37.980  ? 191 LYS CCC CA  1 
ATOM 5219  C C   . LYS C 1 174 ? 140.571 21.609  68.014  1.000 38.120  ? 191 LYS CCC C   1 
ATOM 5220  O O   . LYS C 1 174 ? 140.623 21.400  66.775  1.000 44.030  ? 191 LYS CCC O   1 
ATOM 5221  C CB  . LYS C 1 174 ? 140.397 24.095  68.515  1.000 43.660  ? 191 LYS CCC CB  1 
ATOM 5222  C CG  . LYS C 1 174 ? 139.167 24.129  69.404  1.000 50.890  ? 191 LYS CCC CG  1 
ATOM 5223  C CD  . LYS C 1 174 ? 138.338 25.362  69.171  1.000 57.650  ? 191 LYS CCC CD  1 
ATOM 5224  C CE  . LYS C 1 174 ? 137.013 25.369  69.901  1.000 62.800  ? 191 LYS CCC CE  1 
ATOM 5225  N NZ  . LYS C 1 174 ? 136.067 26.300  69.235  1.000 66.120  ? 191 LYS CCC NZ  1 
ATOM 5226  N N   . ASN C 1 175 ? 139.928 20.812  68.861  1.000 35.170  ? 192 ASN CCC N   1 
ATOM 5227  C CA  . ASN C 1 175 ? 139.215 19.593  68.428  1.000 33.480  ? 192 ASN CCC CA  1 
ATOM 5228  C C   . ASN C 1 175 ? 137.777 19.937  68.047  1.000 33.800  ? 192 ASN CCC C   1 
ATOM 5229  O O   . ASN C 1 175 ? 137.272 20.995  68.442  1.000 28.550  ? 192 ASN CCC O   1 
ATOM 5230  C CB  . ASN C 1 175 ? 139.284 18.528  69.507  1.000 34.960  ? 192 ASN CCC CB  1 
ATOM 5231  C CG  . ASN C 1 175 ? 140.312 17.486  69.156  1.000 37.660  ? 192 ASN CCC CG  1 
ATOM 5232  O OD1 . ASN C 1 175 ? 140.014 16.552  68.400  1.000 58.830  ? 192 ASN CCC OD1 1 
ATOM 5233  N ND2 . ASN C 1 175 ? 141.521 17.672  69.647  1.000 28.570  ? 192 ASN CCC ND2 1 
ATOM 5234  N N   . LYS C 1 176 ? 137.153 19.042  67.293  1.000 37.080  ? 193 LYS CCC N   1 
ATOM 5235  C CA  . LYS C 1 176 ? 135.730 19.169  66.881  1.000 36.570  ? 193 LYS CCC CA  1 
ATOM 5236  C C   . LYS C 1 176 ? 135.547 20.511  66.175  1.000 34.790  ? 193 LYS CCC C   1 
ATOM 5237  O O   . LYS C 1 176 ? 134.390 20.975  66.085  1.000 31.750  ? 193 LYS CCC O   1 
ATOM 5238  C CB  . LYS C 1 176 ? 134.805 19.012  68.091  1.000 35.860  ? 193 LYS CCC CB  1 
ATOM 5239  C CG  . LYS C 1 176 ? 134.969 17.685  68.815  1.000 39.040  ? 193 LYS CCC CG  1 
ATOM 5240  C CD  . LYS C 1 176 ? 134.477 17.612  70.268  1.000 44.080  ? 193 LYS CCC CD  1 
ATOM 5241  C CE  . LYS C 1 176 ? 132.981 17.793  70.450  1.000 48.020  ? 193 LYS CCC CE  1 
ATOM 5242  N NZ  . LYS C 1 176 ? 132.208 16.858  69.597  1.000 57.280  ? 193 LYS CCC NZ  1 
ATOM 5243  N N   . ALA C 1 177 ? 136.638 21.059  65.624  1.000 35.530  ? 194 ALA CCC N   1 
ATOM 5244  C CA  . ALA C 1 177 ? 136.698 22.457  65.145  1.000 37.580  ? 194 ALA CCC CA  1 
ATOM 5245  C C   . ALA C 1 177 ? 136.888 22.515  63.619  1.000 38.540  ? 194 ALA CCC C   1 
ATOM 5246  O O   . ALA C 1 177 ? 136.019 23.133  62.940  1.000 36.160  ? 194 ALA CCC O   1 
ATOM 5247  C CB  . ALA C 1 177 ? 137.791 23.187  65.883  1.000 36.380  ? 194 ALA CCC CB  1 
ATOM 5248  N N   . TYR C 1 178 ? 137.981 21.931  63.108  1.000 37.380  ? 195 TYR CCC N   1 
ATOM 5249  C CA  . TYR C 1 178 ? 138.454 22.178  61.718  1.000 35.890  ? 195 TYR CCC CA  1 
ATOM 5250  C C   . TYR C 1 178 ? 137.924 21.087  60.798  1.000 32.920  ? 195 TYR CCC C   1 
ATOM 5251  O O   . TYR C 1 178 ? 138.470 19.987  60.765  1.000 33.400  ? 195 TYR CCC O   1 
ATOM 5252  C CB  . TYR C 1 178 ? 139.981 22.272  61.674  1.000 35.640  ? 195 TYR CCC CB  1 
ATOM 5253  C CG  . TYR C 1 178 ? 140.544 23.467  62.390  1.000 35.070  ? 195 TYR CCC CG  1 
ATOM 5254  C CD1 . TYR C 1 178 ? 140.780 23.440  63.747  1.000 37.230  ? 195 TYR CCC CD1 1 
ATOM 5255  C CD2 . TYR C 1 178 ? 140.824 24.634  61.708  1.000 37.340  ? 195 TYR CCC CD2 1 
ATOM 5256  C CE1 . TYR C 1 178 ? 141.293 24.546  64.412  1.000 38.030  ? 195 TYR CCC CE1 1 
ATOM 5257  C CE2 . TYR C 1 178 ? 141.339 25.749  62.357  1.000 37.090  ? 195 TYR CCC CE2 1 
ATOM 5258  C CZ  . TYR C 1 178 ? 141.555 25.711  63.714  1.000 37.060  ? 195 TYR CCC CZ  1 
ATOM 5259  O OH  . TYR C 1 178 ? 142.062 26.810  64.332  1.000 37.940  ? 195 TYR CCC OH  1 
ATOM 5260  N N   . PRO C 1 179 ? 136.873 21.349  59.997  1.000 28.950  ? 196 PRO CCC N   1 
ATOM 5261  C CA  . PRO C 1 179 ? 136.357 20.358  59.070  1.000 29.450  ? 196 PRO CCC CA  1 
ATOM 5262  C C   . PRO C 1 179 ? 137.483 19.813  58.180  1.000 30.020  ? 196 PRO CCC C   1 
ATOM 5263  O O   . PRO C 1 179 ? 138.342 20.579  57.836  1.000 28.070  ? 196 PRO CCC O   1 
ATOM 5264  C CB  . PRO C 1 179 ? 135.350 21.143  58.220  1.000 27.770  ? 196 PRO CCC CB  1 
ATOM 5265  C CG  . PRO C 1 179 ? 134.907 22.226  59.124  1.000 28.100  ? 196 PRO CCC CG  1 
ATOM 5266  C CD  . PRO C 1 179 ? 136.164 22.617  59.868  1.000 29.110  ? 196 PRO CCC CD  1 
ATOM 5267  N N   . VAL C 1 180 ? 137.429 18.522  57.832  1.000 31.300  ? 197 VAL CCC N   1 
ATOM 5268  C CA  . VAL C 1 180 ? 138.494 17.860  57.031  1.000 32.280  ? 197 VAL CCC CA  1 
ATOM 5269  C C   . VAL C 1 180 ? 138.465 18.420  55.607  1.000 33.770  ? 197 VAL CCC C   1 
ATOM 5270  O O   . VAL C 1 180 ? 139.540 18.582  55.009  1.000 33.150  ? 197 VAL CCC O   1 
ATOM 5271  C CB  . VAL C 1 180 ? 138.357 16.332  57.063  1.000 32.960  ? 197 VAL CCC CB  1 
ATOM 5272  C CG1 . VAL C 1 180 ? 139.415 15.671  56.191  1.000 33.390  ? 197 VAL CCC CG1 1 
ATOM 5273  C CG2 . VAL C 1 180 ? 138.449 15.792  58.489  1.000 34.290  ? 197 VAL CCC CG2 1 
ATOM 5274  N N   . GLU C 1 181 ? 137.278 18.739  55.102  1.000 34.060  ? 198 GLU CCC N   1 
ATOM 5275  C CA  . GLU C 1 181 ? 137.036 18.954  53.649  1.000 32.820  ? 198 GLU CCC CA  1 
ATOM 5276  C C   . GLU C 1 181 ? 137.430 20.361  53.206  1.000 34.220  ? 198 GLU CCC C   1 
ATOM 5277  O O   . GLU C 1 181 ? 137.250 20.664  52.021  1.000 42.600  ? 198 GLU CCC O   1 
ATOM 5278  C CB  . GLU C 1 181 ? 135.570 18.658  53.321  1.000 32.910  ? 198 GLU CCC CB  1 
ATOM 5279  C CG  . GLU C 1 181 ? 134.561 19.743  53.686  1.000 29.920  ? 198 GLU CCC CG  1 
ATOM 5280  C CD  . GLU C 1 181 ? 133.161 19.449  53.178  1.000 28.310  ? 198 GLU CCC CD  1 
ATOM 5281  O OE1 . GLU C 1 181 ? 132.745 18.262  53.212  1.000 32.120  ? 198 GLU CCC OE1 1 
ATOM 5282  O OE2 . GLU C 1 181 ? 132.493 20.393  52.756  1.000 24.160  ? 198 GLU CCC OE2 1 
ATOM 5283  N N   . CYS C 1 182 ? 137.923 21.214  54.094  1.000 36.280  ? 199 CYS CCC N   1 
ATOM 5284  C CA  . CYS C 1 182 ? 138.287 22.607  53.704  1.000 37.550  ? 199 CYS CCC CA  1 
ATOM 5285  C C   . CYS C 1 182 ? 139.659 22.992  54.263  1.000 35.310  ? 199 CYS CCC C   1 
ATOM 5286  O O   . CYS C 1 182 ? 140.068 24.135  54.049  1.000 35.420  ? 199 CYS CCC O   1 
ATOM 5287  C CB  . CYS C 1 182 ? 137.194 23.604  54.092  1.000 38.400  ? 199 CYS CCC CB  1 
ATOM 5288  S SG  . CYS C 1 182 ? 136.672 23.565  55.833  1.000 35.210  ? 199 CYS CCC SG  1 
ATOM 5289  N N   . TRP C 1 183 ? 140.372 22.046  54.870  1.000 33.550  ? 200 TRP CCC N   1 
ATOM 5290  C CA  . TRP C 1 183 ? 141.730 22.282  55.416  1.000 34.400  ? 200 TRP CCC CA  1 
ATOM 5291  C C   . TRP C 1 183 ? 142.665 21.142  55.021  1.000 32.830  ? 200 TRP CCC C   1 
ATOM 5292  O O   . TRP C 1 183 ? 142.238 19.982  55.087  1.000 32.590  ? 200 TRP CCC O   1 
ATOM 5293  C CB  . TRP C 1 183 ? 141.695 22.426  56.942  1.000 36.350  ? 200 TRP CCC CB  1 
ATOM 5294  C CG  . TRP C 1 183 ? 140.902 23.586  57.454  1.000 33.450  ? 200 TRP CCC CG  1 
ATOM 5295  C CD1 . TRP C 1 183 ? 139.700 23.545  58.094  1.000 33.330  ? 200 TRP CCC CD1 1 
ATOM 5296  C CD2 . TRP C 1 183 ? 141.286 24.959  57.396  1.000 33.920  ? 200 TRP CCC CD2 1 
ATOM 5297  N NE1 . TRP C 1 183 ? 139.302 24.802  58.432  1.000 32.960  ? 200 TRP CCC NE1 1 
ATOM 5298  C CE2 . TRP C 1 183 ? 140.253 25.690  58.013  1.000 35.310  ? 200 TRP CCC CE2 1 
ATOM 5299  C CE3 . TRP C 1 183 ? 142.374 25.637  56.840  1.000 36.610  ? 200 TRP CCC CE3 1 
ATOM 5300  C CZ2 . TRP C 1 183 ? 140.285 27.079  58.094  1.000 36.770  ? 200 TRP CCC CZ2 1 
ATOM 5301  C CZ3 . TRP C 1 183 ? 142.407 27.011  56.923  1.000 38.590  ? 200 TRP CCC CZ3 1 
ATOM 5302  C CH2 . TRP C 1 183 ? 141.377 27.715  57.551  1.000 38.680  ? 200 TRP CCC CH2 1 
ATOM 5303  N N   . VAL C 1 184 ? 143.906 21.482  54.673  1.000 30.990  ? 201 VAL CCC N   1 
ATOM 5304  C CA  . VAL C 1 184 ? 144.994 20.500  54.435  1.000 31.270  ? 201 VAL CCC CA  1 
ATOM 5305  C C   . VAL C 1 184 ? 146.254 21.019  55.087  1.000 28.770  ? 201 VAL CCC C   1 
ATOM 5306  O O   . VAL C 1 184 ? 146.373 22.210  55.329  1.000 28.340  ? 201 VAL CCC O   1 
ATOM 5307  C CB  . VAL C 1 184 ? 145.202 20.278  52.932  1.000 34.320  ? 201 VAL CCC CB  1 
ATOM 5308  C CG1 . VAL C 1 184 ? 143.934 19.734  52.290  1.000 34.860  ? 201 VAL CCC CG1 1 
ATOM 5309  C CG2 . VAL C 1 184 ? 145.665 21.552  52.249  1.000 35.960  ? 201 VAL CCC CG2 1 
ATOM 5310  N N   . PRO C 1 185 ? 147.228 20.150  55.385  1.000 30.460  ? 202 PRO CCC N   1 
ATOM 5311  C CA  . PRO C 1 185 ? 148.546 20.607  55.809  1.000 34.730  ? 202 PRO CCC CA  1 
ATOM 5312  C C   . PRO C 1 185 ? 149.050 21.625  54.786  1.000 37.820  ? 202 PRO CCC C   1 
ATOM 5313  O O   . PRO C 1 185 ? 148.928 21.333  53.592  1.000 43.810  ? 202 PRO CCC O   1 
ATOM 5314  C CB  . PRO C 1 185 ? 149.415 19.337  55.837  1.000 34.570  ? 202 PRO CCC CB  1 
ATOM 5315  C CG  . PRO C 1 185 ? 148.391 18.228  56.076  1.000 35.940  ? 202 PRO CCC CG  1 
ATOM 5316  C CD  . PRO C 1 185 ? 147.113 18.694  55.383  1.000 33.050  ? 202 PRO CCC CD  1 
ATOM 5317  N N   . ASP C 1 186 ? 149.552 22.766  55.275  1.000 37.540  ? 203 ASP CCC N   1 
ATOM 5318  C CA  . ASP C 1 186 ? 150.102 23.880  54.463  1.000 37.370  ? 203 ASP CCC CA  1 
ATOM 5319  C C   . ASP C 1 186 ? 151.548 23.538  54.128  1.000 36.330  ? 203 ASP CCC C   1 
ATOM 5320  O O   . ASP C 1 186 ? 152.415 23.568  54.998  1.000 34.590  ? 203 ASP CCC O   1 
ATOM 5321  C CB  . ASP C 1 186 ? 150.012 25.211  55.216  1.000 40.970  ? 203 ASP CCC CB  1 
ATOM 5322  C CG  . ASP C 1 186 ? 150.599 26.416  54.493  1.000 40.370  ? 203 ASP CCC CG  1 
ATOM 5323  O OD1 . ASP C 1 186 ? 151.156 26.234  53.396  1.000 41.130  ? 203 ASP CCC OD1 1 
ATOM 5324  O OD2 . ASP C 1 186 ? 150.476 27.531  55.039  1.000 45.160  ? 203 ASP CCC OD2 1 
ATOM 5325  N N   . PRO C 1 187 ? 151.848 23.211  52.857  1.000 33.830  ? 204 PRO CCC N   1 
ATOM 5326  C CA  . PRO C 1 187 ? 153.141 22.653  52.501  1.000 32.790  ? 204 PRO CCC CA  1 
ATOM 5327  C C   . PRO C 1 187 ? 154.208 23.736  52.476  1.000 33.430  ? 204 PRO CCC C   1 
ATOM 5328  O O   . PRO C 1 187 ? 155.361 23.381  52.427  1.000 36.650  ? 204 PRO CCC O   1 
ATOM 5329  C CB  . PRO C 1 187 ? 152.926 22.085  51.111  1.000 33.380  ? 204 PRO CCC CB  1 
ATOM 5330  C CG  . PRO C 1 187 ? 151.890 23.025  50.536  1.000 36.170  ? 204 PRO CCC CG  1 
ATOM 5331  C CD  . PRO C 1 187 ? 150.986 23.386  51.695  1.000 36.260  ? 204 PRO CCC CD  1 
ATOM 5332  N N   . THR C 1 188 ? 153.781 25.000  52.512  1.000 35.710  ? 205 THR CCC N   1 
ATOM 5333  C CA  . THR C 1 188 ? 154.668 26.198  52.522  1.000 36.830  ? 205 THR CCC CA  1 
ATOM 5334  C C   . THR C 1 188 ? 155.179 26.450  53.942  1.000 38.630  ? 205 THR CCC C   1 
ATOM 5335  O O   . THR C 1 188 ? 156.019 27.331  54.100  1.000 42.140  ? 205 THR CCC O   1 
ATOM 5336  C CB  . THR C 1 188 ? 153.950 27.457  52.022  1.000 34.520  ? 205 THR CCC CB  1 
ATOM 5337  O OG1 . THR C 1 188 ? 153.086 27.887  53.077  1.000 34.150  ? 205 THR CCC OG1 1 
ATOM 5338  C CG2 . THR C 1 188 ? 153.195 27.244  50.736  1.000 34.140  ? 205 THR CCC CG2 1 
ATOM 5339  N N   . ARG C 1 189 ? 154.650 25.736  54.936  1.000 41.830  ? 206 ARG CCC N   1 
ATOM 5340  C CA  . ARG C 1 189 ? 155.049 25.882  56.358  1.000 42.950  ? 206 ARG CCC CA  1 
ATOM 5341  C C   . ARG C 1 189 ? 155.321 24.477  56.899  1.000 38.760  ? 206 ARG CCC C   1 
ATOM 5342  O O   . ARG C 1 189 ? 155.773 23.627  56.123  1.000 37.860  ? 206 ARG CCC O   1 
ATOM 5343  C CB  . ARG C 1 189 ? 153.968 26.674  57.100  1.000 49.790  ? 206 ARG CCC CB  1 
ATOM 5344  C CG  . ARG C 1 189 ? 153.726 28.073  56.553  1.000 55.640  ? 206 ARG CCC CG  1 
ATOM 5345  C CD  . ARG C 1 189 ? 152.720 28.911  57.309  1.000 62.170  ? 206 ARG CCC CD  1 
ATOM 5346  N NE  . ARG C 1 189 ? 152.589 30.205  56.622  1.000 68.360  ? 206 ARG CCC NE  1 
ATOM 5347  C CZ  . ARG C 1 189 ? 151.708 31.156  56.937  1.000 70.920  ? 206 ARG CCC CZ  1 
ATOM 5348  N NH1 . ARG C 1 189 ? 150.877 30.991  57.952  1.000 86.480  ? 206 ARG CCC NH1 1 
ATOM 5349  N NH2 . ARG C 1 189 ? 151.671 32.281  56.251  1.000 64.710  ? 206 ARG CCC NH2 1 
ATOM 5350  N N   . ASN C 1 190 ? 155.101 24.245  58.186  1.000 38.410  ? 207 ASN CCC N   1 
ATOM 5351  C CA  . ASN C 1 190 ? 155.206 22.907  58.825  1.000 40.590  ? 207 ASN CCC CA  1 
ATOM 5352  C C   . ASN C 1 190 ? 156.648 22.409  58.747  1.000 39.770  ? 207 ASN CCC C   1 
ATOM 5353  O O   . ASN C 1 190 ? 156.839 21.188  58.703  1.000 41.950  ? 207 ASN CCC O   1 
ATOM 5354  C CB  . ASN C 1 190 ? 154.214 21.897  58.234  1.000 40.530  ? 207 ASN CCC CB  1 
ATOM 5355  C CG  . ASN C 1 190 ? 152.790 22.128  58.678  1.000 38.240  ? 207 ASN CCC CG  1 
ATOM 5356  O OD1 . ASN C 1 190 ? 152.522 22.117  59.878  1.000 37.230  ? 207 ASN CCC OD1 1 
ATOM 5357  N ND2 . ASN C 1 190 ? 151.892 22.326  57.723  1.000 33.200  ? 207 ASN CCC ND2 1 
ATOM 5358  N N   . GLU C 1 191 ? 157.626 23.320  58.783  1.000 42.760  ? 208 GLU CCC N   1 
ATOM 5359  C CA  . GLU C 1 191 ? 159.066 22.987  58.938  1.000 44.090  ? 208 GLU CCC CA  1 
ATOM 5360  C C   . GLU C 1 191 ? 159.197 22.023  60.126  1.000 39.370  ? 208 GLU CCC C   1 
ATOM 5361  O O   . GLU C 1 191 ? 159.950 21.034  59.989  1.000 37.790  ? 208 GLU CCC O   1 
ATOM 5362  C CB  . GLU C 1 191 ? 159.901 24.264  59.087  1.000 52.200  ? 208 GLU CCC CB  1 
ATOM 5363  C CG  . GLU C 1 191 ? 161.317 24.032  59.616  1.000 63.910  ? 208 GLU CCC CG  1 
ATOM 5364  C CD  . GLU C 1 191 ? 162.281 25.193  59.499  1.000 76.720  ? 208 GLU CCC CD  1 
ATOM 5365  O OE1 . GLU C 1 191 ? 162.432 25.700  58.364  1.000 86.290  ? 208 GLU CCC OE1 1 
ATOM 5366  O OE2 . GLU C 1 191 ? 162.902 25.576  60.543  1.000 84.360  ? 208 GLU CCC OE2 1 
ATOM 5367  N N   . ASN C 1 192 ? 158.459 22.278  61.217  1.000 37.260  ? 209 ASN CCC N   1 
ATOM 5368  C CA  . ASN C 1 192 ? 158.665 21.617  62.532  1.000 37.460  ? 209 ASN CCC CA  1 
ATOM 5369  C C   . ASN C 1 192 ? 157.671 20.455  62.737  1.000 38.330  ? 209 ASN CCC C   1 
ATOM 5370  O O   . ASN C 1 192 ? 157.520 19.983  63.865  1.000 33.400  ? 209 ASN CCC O   1 
ATOM 5371  C CB  . ASN C 1 192 ? 158.555 22.644  63.655  1.000 32.570  ? 209 ASN CCC CB  1 
ATOM 5372  C CG  . ASN C 1 192 ? 159.172 22.169  64.949  1.000 30.240  ? 209 ASN CCC CG  1 
ATOM 5373  O OD1 . ASN C 1 192 ? 160.034 21.279  64.957  1.000 29.600  ? 209 ASN CCC OD1 1 
ATOM 5374  N ND2 . ASN C 1 192 ? 158.727 22.758  66.044  1.000 27.550  ? 209 ASN CCC ND2 1 
ATOM 5375  N N   . THR C 1 193 ? 157.034 19.985  61.670  1.000 39.200  ? 210 THR CCC N   1 
ATOM 5376  C CA  . THR C 1 193 ? 156.074 18.859  61.707  1.000 37.430  ? 210 THR CCC CA  1 
ATOM 5377  C C   . THR C 1 193 ? 156.440 17.865  60.596  1.000 36.910  ? 210 THR CCC C   1 
ATOM 5378  O O   . THR C 1 193 ? 157.033 18.288  59.583  1.000 36.930  ? 210 THR CCC O   1 
ATOM 5379  C CB  . THR C 1 193 ? 154.638 19.386  61.594  1.000 38.650  ? 210 THR CCC CB  1 
ATOM 5380  O OG1 . THR C 1 193 ? 154.257 20.090  62.773  1.000 37.760  ? 210 THR CCC OG1 1 
ATOM 5381  C CG2 . THR C 1 193 ? 153.648 18.267  61.386  1.000 43.780  ? 210 THR CCC CG2 1 
ATOM 5382  N N   . ARG C 1 194 ? 156.146 16.581  60.806  1.000 33.700  ? 211 ARG CCC N   1 
ATOM 5383  C CA  . ARG C 1 194 ? 156.217 15.526  59.765  1.000 32.340  ? 211 ARG CCC CA  1 
ATOM 5384  C C   . ARG C 1 194 ? 154.799 15.019  59.565  1.000 33.010  ? 211 ARG CCC C   1 
ATOM 5385  O O   . ARG C 1 194 ? 154.234 14.501  60.514  1.000 37.040  ? 211 ARG CCC O   1 
ATOM 5386  C CB  . ARG C 1 194 ? 157.121 14.372  60.187  1.000 31.400  ? 211 ARG CCC CB  1 
ATOM 5387  C CG  . ARG C 1 194 ? 158.499 14.815  60.626  1.000 32.520  ? 211 ARG CCC CG  1 
ATOM 5388  C CD  . ARG C 1 194 ? 159.283 15.423  59.478  1.000 35.350  ? 211 ARG CCC CD  1 
ATOM 5389  N NE  . ARG C 1 194 ? 160.602 15.783  59.974  1.000 37.330  ? 211 ARG CCC NE  1 
ATOM 5390  C CZ  . ARG C 1 194 ? 160.924 16.967  60.473  1.000 34.310  ? 211 ARG CCC CZ  1 
ATOM 5391  N NH1 . ARG C 1 194 ? 160.024 17.940  60.512  1.000 34.120  ? 211 ARG CCC NH1 1 
ATOM 5392  N NH2 . ARG C 1 194 ? 162.154 17.170  60.908  1.000 30.790  ? 211 ARG CCC NH2 1 
ATOM 5393  N N   . TYR C 1 195 ? 154.221 15.236  58.398  1.000 34.060  ? 212 TYR CCC N   1 
ATOM 5394  C CA  . TYR C 1 195 ? 152.803 14.898  58.118  1.000 33.760  ? 212 TYR CCC CA  1 
ATOM 5395  C C   . TYR C 1 195 ? 152.781 13.921  56.953  1.000 31.960  ? 212 TYR CCC C   1 
ATOM 5396  O O   . TYR C 1 195 ? 153.663 13.980  56.077  1.000 34.310  ? 212 TYR CCC O   1 
ATOM 5397  C CB  . TYR C 1 195 ? 151.952 16.150  57.883  1.000 33.970  ? 212 TYR CCC CB  1 
ATOM 5398  C CG  . TYR C 1 195 ? 152.246 16.914  56.618  1.000 35.890  ? 212 TYR CCC CG  1 
ATOM 5399  C CD1 . TYR C 1 195 ? 151.692 16.550  55.402  1.000 36.450  ? 212 TYR CCC CD1 1 
ATOM 5400  C CD2 . TYR C 1 195 ? 153.049 18.042  56.650  1.000 36.010  ? 212 TYR CCC CD2 1 
ATOM 5401  C CE1 . TYR C 1 195 ? 151.944 17.283  54.258  1.000 39.300  ? 212 TYR CCC CE1 1 
ATOM 5402  C CE2 . TYR C 1 195 ? 153.304 18.786  55.517  1.000 35.050  ? 212 TYR CCC CE2 1 
ATOM 5403  C CZ  . TYR C 1 195 ? 152.762 18.404  54.311  1.000 39.330  ? 212 TYR CCC CZ  1 
ATOM 5404  O OH  . TYR C 1 195 ? 153.072 19.127  53.188  1.000 46.170  ? 212 TYR CCC OH  1 
ATOM 5405  N N   . PHE C 1 196 ? 151.815 13.016  57.004  1.000 28.770  ? 213 PHE CCC N   1 
ATOM 5406  C CA  . PHE C 1 196 ? 151.581 11.958  56.000  1.000 25.830  ? 213 PHE CCC CA  1 
ATOM 5407  C C   . PHE C 1 196 ? 150.078 11.711  55.921  1.000 24.270  ? 213 PHE CCC C   1 
ATOM 5408  O O   . PHE C 1 196 ? 149.454 11.483  56.972  1.000 25.310  ? 213 PHE CCC O   1 
ATOM 5409  C CB  . PHE C 1 196 ? 152.254 10.657  56.416  1.000 25.610  ? 213 PHE CCC CB  1 
ATOM 5410  C CG  . PHE C 1 196 ? 153.638 10.777  56.994  1.000 24.840  ? 213 PHE CCC CG  1 
ATOM 5411  C CD1 . PHE C 1 196 ? 153.818 11.069  58.329  1.000 25.790  ? 213 PHE CCC CD1 1 
ATOM 5412  C CD2 . PHE C 1 196 ? 154.747 10.516  56.222  1.000 25.030  ? 213 PHE CCC CD2 1 
ATOM 5413  C CE1 . PHE C 1 196 ? 155.083 11.123  58.878  1.000 27.680  ? 213 PHE CCC CE1 1 
ATOM 5414  C CE2 . PHE C 1 196 ? 156.015 10.548  56.768  1.000 26.300  ? 213 PHE CCC CE2 1 
ATOM 5415  C CZ  . PHE C 1 196 ? 156.182 10.863  58.093  1.000 28.340  ? 213 PHE CCC CZ  1 
ATOM 5416  N N   . GLY C 1 197 ? 149.519 11.749  54.722  1.000 21.600  ? 214 GLY CCC N   1 
ATOM 5417  C CA  . GLY C 1 197 ? 148.106 11.437  54.512  1.000 21.230  ? 214 GLY CCC CA  1 
ATOM 5418  C C   . GLY C 1 197 ? 147.862 10.921  53.113  1.000 23.110  ? 214 GLY CCC C   1 
ATOM 5419  O O   . GLY C 1 197 ? 148.690 11.168  52.210  1.000 22.930  ? 214 GLY CCC O   1 
ATOM 5420  N N   . THR C 1 198 ? 146.737 10.242  52.932  1.000 24.810  ? 215 THR CCC N   1 
ATOM 5421  C CA  . THR C 1 198 ? 146.298 9.726   51.623  1.000 24.810  ? 215 THR CCC CA  1 
ATOM 5422  C C   . THR C 1 198 ? 144.802 9.866   51.497  1.000 26.060  ? 215 THR CCC C   1 
ATOM 5423  O O   . THR C 1 198 ? 144.094 9.424   52.408  1.000 25.460  ? 215 THR CCC O   1 
ATOM 5424  C CB  . THR C 1 198 ? 146.675 8.264   51.464  1.000 23.620  ? 215 THR CCC CB  1 
ATOM 5425  O OG1 . THR C 1 198 ? 148.098 8.223   51.548  1.000 23.530  ? 215 THR CCC OG1 1 
ATOM 5426  C CG2 . THR C 1 198 ? 146.177 7.701   50.159  1.000 24.580  ? 215 THR CCC CG2 1 
ATOM 5427  N N   . LEU C 1 199 ? 144.349 10.496  50.415  1.000 27.760  ? 216 LEU CCC N   1 
ATOM 5428  C CA  . LEU C 1 199 ? 142.929 10.471  50.019  1.000 26.380  ? 216 LEU CCC CA  1 
ATOM 5429  C C   . LEU C 1 199 ? 142.774 9.406   48.936  1.000 27.640  ? 216 LEU CCC C   1 
ATOM 5430  O O   . LEU C 1 199 ? 143.485 9.493   47.916  1.000 27.850  ? 216 LEU CCC O   1 
ATOM 5431  C CB  . LEU C 1 199 ? 142.455 11.821  49.496  1.000 24.270  ? 216 LEU CCC CB  1 
ATOM 5432  C CG  . LEU C 1 199 ? 140.997 11.764  49.051  1.000 24.320  ? 216 LEU CCC CG  1 
ATOM 5433  C CD1 . LEU C 1 199 ? 140.194 12.846  49.703  1.000 25.610  ? 216 LEU CCC CD1 1 
ATOM 5434  C CD2 . LEU C 1 199 ? 140.873 11.842  47.547  1.000 25.780  ? 216 LEU CCC CD2 1 
ATOM 5435  N N   . THR C 1 200 ? 141.876 8.456   49.174  1.000 27.350  ? 217 THR CCC N   1 
ATOM 5436  C CA  . THR C 1 200 ? 141.281 7.592   48.135  1.000 26.090  ? 217 THR CCC CA  1 
ATOM 5437  C C   . THR C 1 200 ? 139.799 7.938   47.971  1.000 25.890  ? 217 THR CCC C   1 
ATOM 5438  O O   . THR C 1 200 ? 139.032 7.729   48.922  1.000 26.610  ? 217 THR CCC O   1 
ATOM 5439  C CB  . THR C 1 200 ? 141.512 6.128   48.496  1.000 25.560  ? 217 THR CCC CB  1 
ATOM 5440  O OG1 . THR C 1 200 ? 142.896 5.955   48.796  1.000 24.940  ? 217 THR CCC OG1 1 
ATOM 5441  C CG2 . THR C 1 200 ? 141.129 5.221   47.357  1.000 25.370  ? 217 THR CCC CG2 1 
ATOM 5442  N N   . GLY C 1 201 ? 139.406 8.451   46.811  1.000 27.620  ? 218 GLY CCC N   1 
ATOM 5443  C CA  . GLY C 1 201 ? 138.016 8.875   46.532  1.000 31.900  ? 218 GLY CCC CA  1 
ATOM 5444  C C   . GLY C 1 201 ? 137.270 7.847   45.708  1.000 33.080  ? 218 GLY CCC C   1 
ATOM 5445  O O   . GLY C 1 201 ? 137.951 7.134   44.941  1.000 37.510  ? 218 GLY CCC O   1 
ATOM 5446  N N   . GLY C 1 202 ? 135.942 7.755   45.854  1.000 30.100  ? 219 GLY CCC N   1 
ATOM 5447  C CA  . GLY C 1 202 ? 135.118 6.776   45.126  1.000 30.460  ? 219 GLY CCC CA  1 
ATOM 5448  C C   . GLY C 1 202 ? 134.193 6.019   46.060  1.000 31.450  ? 219 GLY CCC C   1 
ATOM 5449  O O   . GLY C 1 202 ? 134.639 5.626   47.156  1.000 32.070  ? 219 GLY CCC O   1 
ATOM 5450  N N   . GLU C 1 203 ? 132.949 5.812   45.631  1.000 31.940  ? 220 GLU CCC N   1 
ATOM 5451  C CA  . GLU C 1 203 ? 131.868 5.259   46.488  1.000 32.590  ? 220 GLU CCC CA  1 
ATOM 5452  C C   . GLU C 1 203 ? 132.164 3.785   46.809  1.000 30.960  ? 220 GLU CCC C   1 
ATOM 5453  O O   . GLU C 1 203 ? 131.706 3.327   47.858  1.000 30.540  ? 220 GLU CCC O   1 
ATOM 5454  C CB  . GLU C 1 203 ? 130.478 5.500   45.870  1.000 32.220  ? 220 GLU CCC CB  1 
ATOM 5455  C CG  . GLU C 1 203 ? 130.241 4.885   44.501  1.000 32.010  ? 220 GLU CCC CG  1 
ATOM 5456  C CD  . GLU C 1 203 ? 130.500 5.822   43.330  1.000 31.160  ? 220 GLU CCC CD  1 
ATOM 5457  O OE1 . GLU C 1 203 ? 131.438 6.609   43.435  1.000 32.850  ? 220 GLU CCC OE1 1 
ATOM 5458  O OE2 . GLU C 1 203 ? 129.788 5.756   42.316  1.000 29.990  ? 220 GLU CCC OE2 1 
ATOM 5459  N N   . ASN C 1 204 ? 132.956 3.096   45.987  1.000 31.040  ? 221 ASN CCC N   1 
ATOM 5460  C CA  . ASN C 1 204 ? 133.177 1.627   46.110  1.000 31.510  ? 221 ASN CCC CA  1 
ATOM 5461  C C   . ASN C 1 204 ? 134.628 1.338   46.526  1.000 31.420  ? 221 ASN CCC C   1 
ATOM 5462  O O   . ASN C 1 204 ? 135.041 0.157   46.564  1.000 26.740  ? 221 ASN CCC O   1 
ATOM 5463  C CB  . ASN C 1 204 ? 132.783 0.921   44.813  1.000 30.040  ? 221 ASN CCC CB  1 
ATOM 5464  C CG  . ASN C 1 204 ? 131.310 1.104   44.536  1.000 28.670  ? 221 ASN CCC CG  1 
ATOM 5465  O OD1 . ASN C 1 204 ? 130.501 0.922   45.429  1.000 27.540  ? 221 ASN CCC OD1 1 
ATOM 5466  N ND2 . ASN C 1 204 ? 130.954 1.518   43.332  1.000 28.670  ? 221 ASN CCC ND2 1 
ATOM 5467  N N   . VAL C 1 205 ? 135.391 2.365   46.877  1.000 30.610  ? 222 VAL CCC N   1 
ATOM 5468  C CA  . VAL C 1 205 ? 136.794 2.140   47.302  1.000 32.130  ? 222 VAL CCC CA  1 
ATOM 5469  C C   . VAL C 1 205 ? 136.771 1.187   48.497  1.000 34.090  ? 222 VAL CCC C   1 
ATOM 5470  O O   . VAL C 1 205 ? 136.211 1.516   49.544  1.000 33.490  ? 222 VAL CCC O   1 
ATOM 5471  C CB  . VAL C 1 205 ? 137.514 3.447   47.658  1.000 33.990  ? 222 VAL CCC CB  1 
ATOM 5472  C CG1 . VAL C 1 205 ? 138.917 3.152   48.151  1.000 36.750  ? 222 VAL CCC CG1 1 
ATOM 5473  C CG2 . VAL C 1 205 ? 137.559 4.434   46.508  1.000 34.910  ? 222 VAL CCC CG2 1 
ATOM 5474  N N   . PRO C 1 206 ? 137.422 0.006   48.403  1.000 33.190  ? 223 PRO CCC N   1 
ATOM 5475  C CA  . PRO C 1 206 ? 137.573 -0.885  49.545  1.000 30.800  ? 223 PRO CCC CA  1 
ATOM 5476  C C   . PRO C 1 206 ? 138.569 -0.352  50.570  1.000 25.270  ? 223 PRO CCC C   1 
ATOM 5477  O O   . PRO C 1 206 ? 139.686 0.011   50.207  1.000 19.790  ? 223 PRO CCC O   1 
ATOM 5478  C CB  . PRO C 1 206 ? 138.133 -2.165  48.920  1.000 33.570  ? 223 PRO CCC CB  1 
ATOM 5479  C CG  . PRO C 1 206 ? 138.964 -1.638  47.797  1.000 37.530  ? 223 PRO CCC CG  1 
ATOM 5480  C CD  . PRO C 1 206 ? 138.122 -0.511  47.224  1.000 37.340  ? 223 PRO CCC CD  1 
ATOM 5481  N N   . PRO C 1 207 ? 138.174 -0.339  51.867  1.000 23.430  ? 224 PRO CCC N   1 
ATOM 5482  C CA  . PRO C 1 207 ? 139.103 -0.128  52.962  1.000 23.140  ? 224 PRO CCC CA  1 
ATOM 5483  C C   . PRO C 1 207 ? 140.204 -1.185  52.910  1.000 23.770  ? 224 PRO CCC C   1 
ATOM 5484  O O   . PRO C 1 207 ? 139.921 -2.322  52.635  1.000 23.380  ? 224 PRO CCC O   1 
ATOM 5485  C CB  . PRO C 1 207 ? 138.276 -0.325  54.243  1.000 22.480  ? 224 PRO CCC CB  1 
ATOM 5486  C CG  . PRO C 1 207 ? 136.859 -0.090  53.818  1.000 22.850  ? 224 PRO CCC CG  1 
ATOM 5487  C CD  . PRO C 1 207 ? 136.820 -0.586  52.384  1.000 24.190  ? 224 PRO CCC CD  1 
ATOM 5488  N N   . VAL C 1 208 ? 141.429 -0.748  53.151  1.000 24.930  ? 225 VAL CCC N   1 
ATOM 5489  C CA  . VAL C 1 208 ? 142.623 -1.617  53.284  1.000 24.970  ? 225 VAL CCC CA  1 
ATOM 5490  C C   . VAL C 1 208 ? 143.442 -1.073  54.445  1.000 28.390  ? 225 VAL CCC C   1 
ATOM 5491  O O   . VAL C 1 208 ? 144.190 -0.097  54.235  1.000 33.510  ? 225 VAL CCC O   1 
ATOM 5492  C CB  . VAL C 1 208 ? 143.453 -1.604  52.005  1.000 22.090  ? 225 VAL CCC CB  1 
ATOM 5493  C CG1 . VAL C 1 208 ? 144.767 -2.335  52.215  1.000 20.980  ? 225 VAL CCC CG1 1 
ATOM 5494  C CG2 . VAL C 1 208 ? 142.643 -2.159  50.863  1.000 22.870  ? 225 VAL CCC CG2 1 
ATOM 5495  N N   . LEU C 1 209 ? 143.301 -1.672  55.617  1.000 28.360  ? 226 LEU CCC N   1 
ATOM 5496  C CA  . LEU C 1 209 ? 143.944 -1.178  56.846  1.000 27.820  ? 226 LEU CCC CA  1 
ATOM 5497  C C   . LEU C 1 209 ? 144.898 -2.256  57.363  1.000 25.290  ? 226 LEU CCC C   1 
ATOM 5498  O O   . LEU C 1 209 ? 144.417 -3.335  57.701  1.000 23.050  ? 226 LEU CCC O   1 
ATOM 5499  C CB  . LEU C 1 209 ? 142.808 -0.845  57.808  1.000 32.660  ? 226 LEU CCC CB  1 
ATOM 5500  C CG  . LEU C 1 209 ? 141.739 0.072   57.220  1.000 36.330  ? 226 LEU CCC CG  1 
ATOM 5501  C CD1 . LEU C 1 209 ? 140.583 0.273   58.191  1.000 40.270  ? 226 LEU CCC CD1 1 
ATOM 5502  C CD2 . LEU C 1 209 ? 142.332 1.416   56.884  1.000 38.100  ? 226 LEU CCC CD2 1 
ATOM 5503  N N   . HIS C 1 210 ? 146.197 -1.978  57.349  1.000 26.100  ? 227 HIS CCC N   1 
ATOM 5504  C CA  . HIS C 1 210 ? 147.251 -2.873  57.900  1.000 28.160  ? 227 HIS CCC CA  1 
ATOM 5505  C C   . HIS C 1 210 ? 147.484 -2.547  59.376  1.000 25.160  ? 227 HIS CCC C   1 
ATOM 5506  O O   . HIS C 1 210 ? 147.462 -1.359  59.739  1.000 25.290  ? 227 HIS CCC O   1 
ATOM 5507  C CB  . HIS C 1 210 ? 148.555 -2.775  57.082  1.000 32.450  ? 227 HIS CCC CB  1 
ATOM 5508  C CG  . HIS C 1 210 ? 148.342 -2.931  55.610  1.000 36.270  ? 227 HIS CCC CG  1 
ATOM 5509  N ND1 . HIS C 1 210 ? 148.080 -4.162  55.036  1.000 39.000  ? 227 HIS CCC ND1 1 
ATOM 5510  C CD2 . HIS C 1 210 ? 148.340 -2.035  54.598  1.000 38.770  ? 227 HIS CCC CD2 1 
ATOM 5511  C CE1 . HIS C 1 210 ? 147.920 -4.025  53.738  1.000 39.680  ? 227 HIS CCC CE1 1 
ATOM 5512  N NE2 . HIS C 1 210 ? 148.057 -2.725  53.447  1.000 40.790  ? 227 HIS CCC NE2 1 
ATOM 5513  N N   . ILE C 1 211 ? 147.694 -3.567  60.195  1.000 23.880  ? 228 ILE CCC N   1 
ATOM 5514  C CA  . ILE C 1 211 ? 148.039 -3.395  61.633  1.000 24.590  ? 228 ILE CCC CA  1 
ATOM 5515  C C   . ILE C 1 211 ? 149.296 -4.214  61.910  1.000 24.160  ? 228 ILE CCC C   1 
ATOM 5516  O O   . ILE C 1 211 ? 149.427 -5.303  61.363  1.000 27.380  ? 228 ILE CCC O   1 
ATOM 5517  C CB  . ILE C 1 211 ? 146.847 -3.775  62.540  1.000 24.980  ? 228 ILE CCC CB  1 
ATOM 5518  C CG1 . ILE C 1 211 ? 146.518 -5.266  62.487  1.000 23.930  ? 228 ILE CCC CG1 1 
ATOM 5519  C CG2 . ILE C 1 211 ? 145.627 -2.948  62.178  1.000 25.470  ? 228 ILE CCC CG2 1 
ATOM 5520  C CD1 . ILE C 1 211 ? 145.344 -5.659  63.353  1.000 22.880  ? 228 ILE CCC CD1 1 
ATOM 5521  N N   . THR C 1 212 ? 150.219 -3.660  62.675  1.000 23.870  ? 229 THR CCC N   1 
ATOM 5522  C CA  . THR C 1 212 ? 151.452 -4.364  63.095  1.000 24.640  ? 229 THR CCC CA  1 
ATOM 5523  C C   . THR C 1 212 ? 152.176 -3.499  64.114  1.000 29.490  ? 229 THR CCC C   1 
ATOM 5524  O O   . THR C 1 212 ? 152.194 -2.259  63.969  1.000 39.210  ? 229 THR CCC O   1 
ATOM 5525  C CB  . THR C 1 212 ? 152.363 -4.698  61.917  1.000 21.630  ? 229 THR CCC CB  1 
ATOM 5526  O OG1 . THR C 1 212 ? 153.371 -5.584  62.402  1.000 22.000  ? 229 THR CCC OG1 1 
ATOM 5527  C CG2 . THR C 1 212 ? 153.008 -3.470  61.325  1.000 21.290  ? 229 THR CCC CG2 1 
ATOM 5528  N N   . ASN C 1 213 ? 152.770 -4.133  65.113  1.000 28.900  ? 230 ASN CCC N   1 
ATOM 5529  C CA  . ASN C 1 213 ? 153.623 -3.422  66.086  1.000 29.320  ? 230 ASN CCC CA  1 
ATOM 5530  C C   . ASN C 1 213 ? 155.092 -3.544  65.661  1.000 28.140  ? 230 ASN CCC C   1 
ATOM 5531  O O   . ASN C 1 213 ? 155.938 -3.365  66.520  1.000 29.150  ? 230 ASN CCC O   1 
ATOM 5532  C CB  . ASN C 1 213 ? 153.330 -3.921  67.501  1.000 31.510  ? 230 ASN CCC CB  1 
ATOM 5533  C CG  . ASN C 1 213 ? 153.560 -5.408  67.666  1.000 30.470  ? 230 ASN CCC CG  1 
ATOM 5534  O OD1 . ASN C 1 213 ? 153.838 -6.109  66.705  1.000 27.180  ? 230 ASN CCC OD1 1 
ATOM 5535  N ND2 . ASN C 1 213 ? 153.415 -5.897  68.886  1.000 33.100  ? 230 ASN CCC ND2 1 
ATOM 5536  N N   . THR C 1 214 ? 155.389 -3.837  64.394  1.000 27.960  ? 231 THR CCC N   1 
ATOM 5537  C CA  . THR C 1 214 ? 156.772 -4.126  63.913  1.000 29.090  ? 231 THR CCC CA  1 
ATOM 5538  C C   . THR C 1 214 ? 157.290 -3.027  62.976  1.000 29.340  ? 231 THR CCC C   1 
ATOM 5539  O O   . THR C 1 214 ? 158.450 -3.075  62.605  1.000 30.550  ? 231 THR CCC O   1 
ATOM 5540  C CB  . THR C 1 214 ? 156.839 -5.466  63.181  1.000 29.190  ? 231 THR CCC CB  1 
ATOM 5541  O OG1 . THR C 1 214 ? 156.000 -5.364  62.042  1.000 31.730  ? 231 THR CCC OG1 1 
ATOM 5542  C CG2 . THR C 1 214 ? 156.385 -6.629  64.026  1.000 28.230  ? 231 THR CCC CG2 1 
ATOM 5543  N N   . ALA C 1 215 ? 156.451 -2.065  62.621  1.000 29.600  ? 232 ALA CCC N   1 
ATOM 5544  C CA  . ALA C 1 215 ? 156.743 -1.072  61.568  1.000 30.220  ? 232 ALA CCC CA  1 
ATOM 5545  C C   . ALA C 1 215 ? 156.999 0.279   62.221  1.000 30.980  ? 232 ALA CCC C   1 
ATOM 5546  O O   . ALA C 1 215 ? 156.033 0.888   62.719  1.000 32.500  ? 232 ALA CCC O   1 
ATOM 5547  C CB  . ALA C 1 215 ? 155.572 -0.994  60.621  1.000 30.980  ? 232 ALA CCC CB  1 
ATOM 5548  N N   . THR C 1 216 ? 158.242 0.741   62.191  1.000 33.060  ? 233 THR CCC N   1 
ATOM 5549  C CA  . THR C 1 216 ? 158.634 2.084   62.693  1.000 34.850  ? 233 THR CCC CA  1 
ATOM 5550  C C   . THR C 1 216 ? 158.783 3.049   61.505  1.000 32.440  ? 233 THR CCC C   1 
ATOM 5551  O O   . THR C 1 216 ? 159.190 2.601   60.469  1.000 35.290  ? 233 THR CCC O   1 
ATOM 5552  C CB  . THR C 1 216 ? 159.931 1.960   63.495  1.000 37.770  ? 233 THR CCC CB  1 
ATOM 5553  O OG1 . THR C 1 216 ? 159.732 0.951   64.481  1.000 41.440  ? 233 THR CCC OG1 1 
ATOM 5554  C CG2 . THR C 1 216 ? 160.337 3.238   64.183  1.000 38.120  ? 233 THR CCC CG2 1 
ATOM 5555  N N   . THR C 1 217 ? 158.414 4.313   61.669  1.000 31.170  ? 234 THR CCC N   1 
ATOM 5556  C CA  . THR C 1 217 ? 158.583 5.427   60.693  1.000 29.140  ? 234 THR CCC CA  1 
ATOM 5557  C C   . THR C 1 217 ? 159.544 6.456   61.279  1.000 31.260  ? 234 THR CCC C   1 
ATOM 5558  O O   . THR C 1 217 ? 159.298 6.893   62.413  1.000 44.480  ? 234 THR CCC O   1 
ATOM 5559  C CB  . THR C 1 217 ? 157.265 6.158   60.446  1.000 26.840  ? 234 THR CCC CB  1 
ATOM 5560  O OG1 . THR C 1 217 ? 156.269 5.215   60.054  1.000 30.290  ? 234 THR CCC OG1 1 
ATOM 5561  C CG2 . THR C 1 217 ? 157.408 7.226   59.397  1.000 27.230  ? 234 THR CCC CG2 1 
ATOM 5562  N N   . VAL C 1 218 ? 160.594 6.846   60.571  1.000 29.190  ? 235 VAL CCC N   1 
ATOM 5563  C CA  . VAL C 1 218 ? 161.611 7.781   61.138  1.000 28.440  ? 235 VAL CCC CA  1 
ATOM 5564  C C   . VAL C 1 218 ? 161.158 9.214   60.873  1.000 27.310  ? 235 VAL CCC C   1 
ATOM 5565  O O   . VAL C 1 218 ? 160.629 9.448   59.812  1.000 30.510  ? 235 VAL CCC O   1 
ATOM 5566  C CB  . VAL C 1 218 ? 162.998 7.479   60.556  1.000 30.150  ? 235 VAL CCC CB  1 
ATOM 5567  C CG1 . VAL C 1 218 ? 163.961 8.630   60.749  1.000 32.790  ? 235 VAL CCC CG1 1 
ATOM 5568  C CG2 . VAL C 1 218 ? 163.567 6.197   61.133  1.000 30.390  ? 235 VAL CCC CG2 1 
ATOM 5569  N N   . LEU C 1 219 ? 161.355 10.131  61.814  1.000 28.870  ? 236 LEU CCC N   1 
ATOM 5570  C CA  . LEU C 1 219 ? 160.819 11.518  61.735  1.000 30.770  ? 236 LEU CCC CA  1 
ATOM 5571  C C   . LEU C 1 219 ? 161.939 12.530  61.448  1.000 31.570  ? 236 LEU CCC C   1 
ATOM 5572  O O   . LEU C 1 219 ? 161.647 13.744  61.393  1.000 29.230  ? 236 LEU CCC O   1 
ATOM 5573  C CB  . LEU C 1 219 ? 160.090 11.813  63.054  1.000 31.630  ? 236 LEU CCC CB  1 
ATOM 5574  C CG  . LEU C 1 219 ? 158.907 10.892  63.350  1.000 31.450  ? 236 LEU CCC CG  1 
ATOM 5575  C CD1 . LEU C 1 219 ? 158.381 11.107  64.752  1.000 32.380  ? 236 LEU CCC CD1 1 
ATOM 5576  C CD2 . LEU C 1 219 ? 157.809 11.123  62.342  1.000 32.200  ? 236 LEU CCC CD2 1 
ATOM 5577  N N   . LEU C 1 220 ? 163.174 12.053  61.259  1.000 32.990  ? 237 LEU CCC N   1 
ATOM 5578  C CA  . LEU C 1 220 ? 164.353 12.914  60.961  1.000 34.920  ? 237 LEU CCC CA  1 
ATOM 5579  C C   . LEU C 1 220 ? 164.260 13.440  59.521  1.000 35.770  ? 237 LEU CCC C   1 
ATOM 5580  O O   . LEU C 1 220 ? 163.777 12.702  58.656  1.000 33.160  ? 237 LEU CCC O   1 
ATOM 5581  C CB  . LEU C 1 220 ? 165.633 12.101  61.144  1.000 35.970  ? 237 LEU CCC CB  1 
ATOM 5582  C CG  . LEU C 1 220 ? 165.818 11.430  62.505  1.000 38.180  ? 237 LEU CCC CG  1 
ATOM 5583  C CD1 . LEU C 1 220 ? 167.151 10.706  62.555  1.000 40.720  ? 237 LEU CCC CD1 1 
ATOM 5584  C CD2 . LEU C 1 220 ? 165.717 12.428  63.644  1.000 41.870  ? 237 LEU CCC CD2 1 
ATOM 5585  N N   . ASP C 1 221 ? 164.733 14.664  59.288  1.000 36.080  ? 238 ASP CCC N   1 
ATOM 5586  C CA  . ASP C 1 221 ? 164.730 15.348  57.970  1.000 36.850  ? 238 ASP CCC CA  1 
ATOM 5587  C C   . ASP C 1 221 ? 166.060 15.059  57.262  1.000 39.700  ? 238 ASP CCC C   1 
ATOM 5588  O O   . ASP C 1 221 ? 166.859 14.274  57.827  1.000 40.380  ? 238 ASP CCC O   1 
ATOM 5589  C CB  . ASP C 1 221 ? 164.481 16.851  58.127  1.000 36.760  ? 238 ASP CCC CB  1 
ATOM 5590  C CG  . ASP C 1 221 ? 165.577 17.632  58.838  1.000 37.310  ? 238 ASP CCC CG  1 
ATOM 5591  O OD1 . ASP C 1 221 ? 166.593 17.023  59.217  1.000 38.990  ? 238 ASP CCC OD1 1 
ATOM 5592  O OD2 . ASP C 1 221 ? 165.401 18.842  59.020  1.000 37.470  ? 238 ASP CCC OD2 1 
ATOM 5593  N N   . GLU C 1 222 ? 166.281 15.682  56.094  1.000 41.550  ? 239 GLU CCC N   1 
ATOM 5594  C CA  . GLU C 1 222 ? 167.501 15.527  55.253  1.000 42.930  ? 239 GLU CCC CA  1 
ATOM 5595  C C   . GLU C 1 222 ? 168.764 15.762  56.104  1.000 47.650  ? 239 GLU CCC C   1 
ATOM 5596  O O   . GLU C 1 222 ? 169.787 15.201  55.736  1.000 46.700  ? 239 GLU CCC O   1 
ATOM 5597  C CB  . GLU C 1 222 ? 167.461 16.382  53.975  1.000 44.340  ? 239 GLU CCC CB  1 
ATOM 5598  C CG  . GLU C 1 222 ? 166.944 17.798  54.125  1.000 48.160  ? 239 GLU CCC CG  1 
ATOM 5599  C CD  . GLU C 1 222 ? 165.446 18.004  53.909  1.000 62.760  ? 239 GLU CCC CD  1 
ATOM 5600  O OE1 . GLU C 1 222 ? 165.116 18.719  52.973  1.000 75.850  ? 239 GLU CCC OE1 1 
ATOM 5601  O OE2 . GLU C 1 222 ? 164.590 17.485  54.674  1.000 70.160  ? 239 GLU CCC OE2 1 
ATOM 5602  N N   . PHE C 1 223 ? 168.693 16.517  57.206  1.000 54.720  ? 240 PHE CCC N   1 
ATOM 5603  C CA  . PHE C 1 223 ? 169.842 16.885  58.080  1.000 51.240  ? 240 PHE CCC CA  1 
ATOM 5604  C C   . PHE C 1 223 ? 169.839 16.067  59.378  1.000 45.240  ? 240 PHE CCC C   1 
ATOM 5605  O O   . PHE C 1 223 ? 170.538 16.466  60.303  1.000 47.420  ? 240 PHE CCC O   1 
ATOM 5606  C CB  . PHE C 1 223 ? 169.771 18.356  58.491  1.000 57.580  ? 240 PHE CCC CB  1 
ATOM 5607  C CG  . PHE C 1 223 ? 169.688 19.377  57.391  1.000 63.560  ? 240 PHE CCC CG  1 
ATOM 5608  C CD1 . PHE C 1 223 ? 168.519 19.592  56.679  1.000 63.830  ? 240 PHE CCC CD1 1 
ATOM 5609  C CD2 . PHE C 1 223 ? 170.752 20.241  57.189  1.000 69.300  ? 240 PHE CCC CD2 1 
ATOM 5610  C CE1 . PHE C 1 223 ? 168.453 20.577  55.707  1.000 68.760  ? 240 PHE CCC CE1 1 
ATOM 5611  C CE2 . PHE C 1 223 ? 170.676 21.256  56.244  1.000 69.550  ? 240 PHE CCC CE2 1 
ATOM 5612  C CZ  . PHE C 1 223 ? 169.529 21.414  55.497  1.000 74.520  ? 240 PHE CCC CZ  1 
ATOM 5613  N N   . GLY C 1 224 ? 169.046 15.003  59.488  1.000 44.350  ? 241 GLY CCC N   1 
ATOM 5614  C CA  . GLY C 1 224 ? 169.048 14.129  60.685  1.000 45.740  ? 241 GLY CCC CA  1 
ATOM 5615  C C   . GLY C 1 224 ? 168.482 14.783  61.941  1.000 44.000  ? 241 GLY CCC C   1 
ATOM 5616  O O   . GLY C 1 224 ? 168.780 14.288  63.050  1.000 38.630  ? 241 GLY CCC O   1 
ATOM 5617  N N   . VAL C 1 225 ? 167.656 15.824  61.769  1.000 45.930  ? 242 VAL CCC N   1 
ATOM 5618  C CA  . VAL C 1 225 ? 166.894 16.527  62.854  1.000 41.660  ? 242 VAL CCC CA  1 
ATOM 5619  C C   . VAL C 1 225 ? 165.406 16.186  62.762  1.000 36.920  ? 242 VAL CCC C   1 
ATOM 5620  O O   . VAL C 1 225 ? 164.815 16.429  61.697  1.000 37.170  ? 242 VAL CCC O   1 
ATOM 5621  C CB  . VAL C 1 225 ? 167.083 18.046  62.758  1.000 44.180  ? 242 VAL CCC CB  1 
ATOM 5622  C CG1 . VAL C 1 225 ? 166.463 18.744  63.959  1.000 47.400  ? 242 VAL CCC CG1 1 
ATOM 5623  C CG2 . VAL C 1 225 ? 168.540 18.429  62.582  1.000 48.540  ? 242 VAL CCC CG2 1 
ATOM 5624  N N   . GLY C 1 226 ? 164.819 15.684  63.851  1.000 32.330  ? 243 GLY CCC N   1 
ATOM 5625  C CA  . GLY C 1 226 ? 163.368 15.443  63.973  1.000 30.630  ? 243 GLY CCC CA  1 
ATOM 5626  C C   . GLY C 1 226 ? 162.656 16.722  64.371  1.000 29.430  ? 243 GLY CCC C   1 
ATOM 5627  O O   . GLY C 1 226 ? 163.300 17.752  64.556  1.000 27.190  ? 243 GLY CCC O   1 
ATOM 5628  N N   . PRO C 1 227 ? 161.312 16.719  64.475  1.000 31.720  ? 244 PRO CCC N   1 
ATOM 5629  C CA  . PRO C 1 227 ? 160.586 17.857  65.047  1.000 32.420  ? 244 PRO CCC CA  1 
ATOM 5630  C C   . PRO C 1 227 ? 161.141 18.183  66.441  1.000 31.370  ? 244 PRO CCC C   1 
ATOM 5631  O O   . PRO C 1 227 ? 161.516 17.250  67.167  1.000 28.500  ? 244 PRO CCC O   1 
ATOM 5632  C CB  . PRO C 1 227 ? 159.131 17.379  65.129  1.000 32.420  ? 244 PRO CCC CB  1 
ATOM 5633  C CG  . PRO C 1 227 ? 159.042 16.350  64.021  1.000 33.650  ? 244 PRO CCC CG  1 
ATOM 5634  C CD  . PRO C 1 227 ? 160.408 15.669  63.987  1.000 32.780  ? 244 PRO CCC CD  1 
ATOM 5635  N N   . LEU C 1 228 ? 161.212 19.480  66.758  1.000 32.310  ? 245 LEU CCC N   1 
ATOM 5636  C CA  . LEU C 1 228 ? 161.677 19.980  68.072  1.000 35.010  ? 245 LEU CCC CA  1 
ATOM 5637  C C   . LEU C 1 228 ? 160.469 20.532  68.831  1.000 39.480  ? 245 LEU CCC C   1 
ATOM 5638  O O   . LEU C 1 228 ? 159.783 21.427  68.299  1.000 51.170  ? 245 LEU CCC O   1 
ATOM 5639  C CB  . LEU C 1 228 ? 162.755 21.043  67.852  1.000 33.690  ? 245 LEU CCC CB  1 
ATOM 5640  C CG  . LEU C 1 228 ? 164.075 20.552  67.264  1.000 33.190  ? 245 LEU CCC CG  1 
ATOM 5641  C CD1 . LEU C 1 228 ? 165.098 21.682  67.332  1.000 32.440  ? 245 LEU CCC CD1 1 
ATOM 5642  C CD2 . LEU C 1 228 ? 164.642 19.354  67.994  1.000 32.270  ? 245 LEU CCC CD2 1 
ATOM 5643  N N   . CYS C 1 229 ? 160.227 20.010  70.032  1.000 35.630  ? 246 CYS CCC N   1 
ATOM 5644  C CA  . CYS C 1 229 ? 159.005 20.274  70.821  1.000 30.920  ? 246 CYS CCC CA  1 
ATOM 5645  C C   . CYS C 1 229 ? 159.115 21.600  71.579  1.000 30.510  ? 246 CYS CCC C   1 
ATOM 5646  O O   . CYS C 1 229 ? 159.515 21.570  72.746  1.000 29.810  ? 246 CYS CCC O   1 
ATOM 5647  C CB  . CYS C 1 229 ? 158.805 19.125  71.788  1.000 31.800  ? 246 CYS CCC CB  1 
ATOM 5648  S SG  . CYS C 1 229 ? 158.457 17.580  70.940  1.000 28.620  ? 246 CYS CCC SG  1 
ATOM 5649  N N   . LYS C 1 230 ? 158.754 22.707  70.928  1.000 31.800  ? 247 LYS CCC N   1 
ATOM 5650  C CA  . LYS C 1 230 ? 158.611 24.055  71.540  1.000 32.970  ? 247 LYS CCC CA  1 
ATOM 5651  C C   . LYS C 1 230 ? 157.706 23.950  72.769  1.000 32.750  ? 247 LYS CCC C   1 
ATOM 5652  O O   . LYS C 1 230 ? 156.641 23.316  72.664  1.000 34.350  ? 247 LYS CCC O   1 
ATOM 5653  C CB  . LYS C 1 230 ? 158.045 25.050  70.527  1.000 35.610  ? 247 LYS CCC CB  1 
ATOM 5654  C CG  . LYS C 1 230 ? 159.063 25.452  69.480  1.000 43.990  ? 247 LYS CCC CG  1 
ATOM 5655  C CD  . LYS C 1 230 ? 158.574 26.204  68.256  1.000 50.790  ? 247 LYS CCC CD  1 
ATOM 5656  C CE  . LYS C 1 230 ? 159.637 26.178  67.170  1.000 56.700  ? 247 LYS CCC CE  1 
ATOM 5657  N NZ  . LYS C 1 230 ? 159.436 27.247  66.170  1.000 69.980  ? 247 LYS CCC NZ  1 
ATOM 5658  N N   . GLY C 1 231 ? 158.128 24.546  73.886  1.000 31.510  ? 248 GLY CCC N   1 
ATOM 5659  C CA  . GLY C 1 231 ? 157.338 24.606  75.132  1.000 31.620  ? 248 GLY CCC CA  1 
ATOM 5660  C C   . GLY C 1 231 ? 157.224 23.255  75.804  1.000 30.980  ? 248 GLY CCC C   1 
ATOM 5661  O O   . GLY C 1 231 ? 156.285 23.073  76.599  1.000 37.090  ? 248 GLY CCC O   1 
ATOM 5662  N N   . ASP C 1 232 ? 158.121 22.334  75.485  1.000 29.840  ? 249 ASP CCC N   1 
ATOM 5663  C CA  . ASP C 1 232 ? 158.113 20.945  75.998  1.000 33.430  ? 249 ASP CCC CA  1 
ATOM 5664  C C   . ASP C 1 232 ? 156.761 20.289  75.680  1.000 34.310  ? 249 ASP CCC C   1 
ATOM 5665  O O   . ASP C 1 232 ? 156.244 19.533  76.525  1.000 38.050  ? 249 ASP CCC O   1 
ATOM 5666  C CB  . ASP C 1 232 ? 158.530 20.971  77.461  1.000 37.560  ? 249 ASP CCC CB  1 
ATOM 5667  C CG  . ASP C 1 232 ? 160.021 21.250  77.615  1.000 45.850  ? 249 ASP CCC CG  1 
ATOM 5668  O OD1 . ASP C 1 232 ? 160.733 21.070  76.620  1.000 51.270  ? 249 ASP CCC OD1 1 
ATOM 5669  O OD2 . ASP C 1 232 ? 160.485 21.643  78.732  1.000 64.910  ? 249 ASP CCC OD2 1 
ATOM 5670  N N   . ASN C 1 233 ? 156.252 20.540  74.477  1.000 33.470  ? 250 ASN CCC N   1 
ATOM 5671  C CA  . ASN C 1 233 ? 154.974 19.977  73.965  1.000 35.110  ? 250 ASN CCC CA  1 
ATOM 5672  C C   . ASN C 1 233 ? 155.171 19.241  72.631  1.000 33.400  ? 250 ASN CCC C   1 
ATOM 5673  O O   . ASN C 1 233 ? 155.862 19.750  71.734  1.000 32.350  ? 250 ASN CCC O   1 
ATOM 5674  C CB  . ASN C 1 233 ? 153.927 21.069  73.769  1.000 37.230  ? 250 ASN CCC CB  1 
ATOM 5675  C CG  . ASN C 1 233 ? 153.383 21.600  75.074  1.000 37.790  ? 250 ASN CCC CG  1 
ATOM 5676  O OD1 . ASN C 1 233 ? 153.372 20.899  76.079  1.000 44.320  ? 250 ASN CCC OD1 1 
ATOM 5677  N ND2 . ASN C 1 233 ? 152.918 22.832  75.056  1.000 39.390  ? 250 ASN CCC ND2 1 
ATOM 5678  N N   . LEU C 1 234 ? 154.532 18.086  72.509  1.000 33.330  ? 251 LEU CCC N   1 
ATOM 5679  C CA  . LEU C 1 234 ? 154.490 17.255  71.287  1.000 33.040  ? 251 LEU CCC CA  1 
ATOM 5680  C C   . LEU C 1 234 ? 153.059 17.310  70.762  1.000 31.530  ? 251 LEU CCC C   1 
ATOM 5681  O O   . LEU C 1 234 ? 152.128 17.151  71.582  1.000 28.880  ? 251 LEU CCC O   1 
ATOM 5682  C CB  . LEU C 1 234 ? 154.872 15.823  71.664  1.000 36.080  ? 251 LEU CCC CB  1 
ATOM 5683  C CG  . LEU C 1 234 ? 154.911 14.831  70.516  1.000 39.540  ? 251 LEU CCC CG  1 
ATOM 5684  C CD1 . LEU C 1 234 ? 155.990 15.214  69.512  1.000 38.300  ? 251 LEU CCC CD1 1 
ATOM 5685  C CD2 . LEU C 1 234 ? 155.102 13.409  71.058  1.000 40.430  ? 251 LEU CCC CD2 1 
ATOM 5686  N N   . TYR C 1 235 ? 152.899 17.518  69.459  1.000 31.870  ? 252 TYR CCC N   1 
ATOM 5687  C CA  . TYR C 1 235 ? 151.586 17.726  68.800  1.000 34.550  ? 252 TYR CCC CA  1 
ATOM 5688  C C   . TYR C 1 235 ? 151.280 16.568  67.841  1.000 38.520  ? 252 TYR CCC C   1 
ATOM 5689  O O   . TYR C 1 235 ? 151.851 16.475  66.728  1.000 43.740  ? 252 TYR CCC O   1 
ATOM 5690  C CB  . TYR C 1 235 ? 151.575 19.066  68.063  1.000 34.710  ? 252 TYR CCC CB  1 
ATOM 5691  C CG  . TYR C 1 235 ? 151.313 20.271  68.923  1.000 32.350  ? 252 TYR CCC CG  1 
ATOM 5692  C CD1 . TYR C 1 235 ? 152.327 20.849  69.668  1.000 31.290  ? 252 TYR CCC CD1 1 
ATOM 5693  C CD2 . TYR C 1 235 ? 150.052 20.853  68.949  1.000 32.190  ? 252 TYR CCC CD2 1 
ATOM 5694  C CE1 . TYR C 1 235 ? 152.084 21.968  70.450  1.000 33.870  ? 252 TYR CCC CE1 1 
ATOM 5695  C CE2 . TYR C 1 235 ? 149.791 21.964  69.733  1.000 35.030  ? 252 TYR CCC CE2 1 
ATOM 5696  C CZ  . TYR C 1 235 ? 150.807 22.522  70.492  1.000 36.760  ? 252 TYR CCC CZ  1 
ATOM 5697  O OH  . TYR C 1 235 ? 150.496 23.616  71.254  1.000 37.830  ? 252 TYR CCC OH  1 
ATOM 5698  N N   . LEU C 1 236 ? 150.360 15.705  68.265  1.000 37.440  ? 253 LEU CCC N   1 
ATOM 5699  C CA  . LEU C 1 236 ? 149.829 14.603  67.441  1.000 33.000  ? 253 LEU CCC CA  1 
ATOM 5700  C C   . LEU C 1 236 ? 148.519 15.089  66.820  1.000 31.990  ? 253 LEU CCC C   1 
ATOM 5701  O O   . LEU C 1 236 ? 147.617 15.539  67.561  1.000 26.990  ? 253 LEU CCC O   1 
ATOM 5702  C CB  . LEU C 1 236 ? 149.648 13.369  68.328  1.000 31.340  ? 253 LEU CCC CB  1 
ATOM 5703  C CG  . LEU C 1 236 ? 150.877 13.020  69.178  1.000 28.840  ? 253 LEU CCC CG  1 
ATOM 5704  C CD1 . LEU C 1 236 ? 150.663 11.702  69.896  1.000 28.990  ? 253 LEU CCC CD1 1 
ATOM 5705  C CD2 . LEU C 1 236 ? 152.156 12.971  68.352  1.000 27.910  ? 253 LEU CCC CD2 1 
ATOM 5706  N N   . SER C 1 237 ? 148.469 15.049  65.494  1.000 34.000  ? 254 SER CCC N   1 
ATOM 5707  C CA  . SER C 1 237 ? 147.255 15.293  64.678  1.000 35.980  ? 254 SER CCC CA  1 
ATOM 5708  C C   . SER C 1 237 ? 146.955 14.025  63.863  1.000 34.050  ? 254 SER CCC C   1 
ATOM 5709  O O   . SER C 1 237 ? 147.913 13.264  63.570  1.000 30.660  ? 254 SER CCC O   1 
ATOM 5710  C CB  . SER C 1 237 ? 147.461 16.520  63.817  1.000 38.260  ? 254 SER CCC CB  1 
ATOM 5711  O OG  . SER C 1 237 ? 148.229 17.490  64.526  1.000 46.230  ? 254 SER CCC OG  1 
ATOM 5712  N N   . ALA C 1 238 ? 145.685 13.793  63.520  1.000 31.500  ? 255 ALA CCC N   1 
ATOM 5713  C CA  . ALA C 1 238 ? 145.243 12.580  62.800  1.000 29.850  ? 255 ALA CCC CA  1 
ATOM 5714  C C   . ALA C 1 238 ? 143.847 12.779  62.219  1.000 27.850  ? 255 ALA CCC C   1 
ATOM 5715  O O   . ALA C 1 238 ? 143.068 13.536  62.817  1.000 31.680  ? 255 ALA CCC O   1 
ATOM 5716  C CB  . ALA C 1 238 ? 145.236 11.417  63.744  1.000 32.190  ? 255 ALA CCC CB  1 
ATOM 5717  N N   . VAL C 1 239 ? 143.558 12.125  61.099  1.000 26.220  ? 256 VAL CCC N   1 
ATOM 5718  C CA  . VAL C 1 239 ? 142.182 11.919  60.564  1.000 28.340  ? 256 VAL CCC CA  1 
ATOM 5719  C C   . VAL C 1 239 ? 142.137 10.507  60.010  1.000 29.890  ? 256 VAL CCC C   1 
ATOM 5720  O O   . VAL C 1 239 ? 143.092 10.157  59.322  1.000 29.800  ? 256 VAL CCC O   1 
ATOM 5721  C CB  . VAL C 1 239 ? 141.816 12.883  59.429  1.000 28.240  ? 256 VAL CCC CB  1 
ATOM 5722  C CG1 . VAL C 1 239 ? 140.409 12.635  58.922  1.000 27.710  ? 256 VAL CCC CG1 1 
ATOM 5723  C CG2 . VAL C 1 239 ? 141.984 14.323  59.850  1.000 30.410  ? 256 VAL CCC CG2 1 
ATOM 5724  N N   . ASP C 1 240 ? 141.065 9.757   60.265  1.000 30.830  ? 257 ASP CCC N   1 
ATOM 5725  C CA  . ASP C 1 240 ? 140.923 8.388   59.707  1.000 28.990  ? 257 ASP CCC CA  1 
ATOM 5726  C C   . ASP C 1 240 ? 139.463 8.141   59.336  1.000 31.090  ? 257 ASP CCC C   1 
ATOM 5727  O O   . ASP C 1 240 ? 138.828 7.243   59.932  1.000 30.110  ? 257 ASP CCC O   1 
ATOM 5728  C CB  . ASP C 1 240 ? 141.449 7.364   60.699  1.000 26.930  ? 257 ASP CCC CB  1 
ATOM 5729  C CG  . ASP C 1 240 ? 142.952 7.383   60.800  1.000 24.580  ? 257 ASP CCC CG  1 
ATOM 5730  O OD1 . ASP C 1 240 ? 143.575 6.878   59.863  1.000 22.800  ? 257 ASP CCC OD1 1 
ATOM 5731  O OD2 . ASP C 1 240 ? 143.471 7.896   61.822  1.000 23.230  ? 257 ASP CCC OD2 1 
ATOM 5732  N N   . VAL C 1 241 ? 138.951 8.937   58.399  1.000 30.790  ? 258 VAL CCC N   1 
ATOM 5733  C CA  . VAL C 1 241 ? 137.625 8.700   57.771  1.000 29.280  ? 258 VAL CCC CA  1 
ATOM 5734  C C   . VAL C 1 241 ? 137.787 7.419   56.952  1.000 30.960  ? 258 VAL CCC C   1 
ATOM 5735  O O   . VAL C 1 241 ? 138.564 7.456   55.981  1.000 37.920  ? 258 VAL CCC O   1 
ATOM 5736  C CB  . VAL C 1 241 ? 137.202 9.900   56.910  1.000 26.920  ? 258 VAL CCC CB  1 
ATOM 5737  C CG1 . VAL C 1 241 ? 135.901 9.620   56.195  1.000 27.070  ? 258 VAL CCC CG1 1 
ATOM 5738  C CG2 . VAL C 1 241 ? 137.087 11.164  57.739  1.000 26.630  ? 258 VAL CCC CG2 1 
ATOM 5739  N N   . CYS C 1 242 ? 137.176 6.316   57.383  1.000 29.560  ? 259 CYS CCC N   1 
ATOM 5740  C CA  . CYS C 1 242 ? 137.463 4.957   56.860  1.000 27.130  ? 259 CYS CCC CA  1 
ATOM 5741  C C   . CYS C 1 242 ? 136.639 4.698   55.607  1.000 27.440  ? 259 CYS CCC C   1 
ATOM 5742  O O   . CYS C 1 242 ? 137.045 3.824   54.809  1.000 28.550  ? 259 CYS CCC O   1 
ATOM 5743  C CB  . CYS C 1 242 ? 137.132 3.896   57.889  1.000 25.580  ? 259 CYS CCC CB  1 
ATOM 5744  S SG  . CYS C 1 242 ? 138.363 3.824   59.199  1.000 24.480  ? 259 CYS CCC SG  1 
ATOM 5745  N N   . GLY C 1 243 ? 135.530 5.427   55.483  1.000 25.460  ? 260 GLY CCC N   1 
ATOM 5746  C CA  . GLY C 1 243 ? 134.502 5.209   54.456  1.000 25.460  ? 260 GLY CCC CA  1 
ATOM 5747  C C   . GLY C 1 243 ? 133.148 5.665   54.955  1.000 24.210  ? 260 GLY CCC C   1 
ATOM 5748  O O   . GLY C 1 243 ? 133.112 6.454   55.907  1.000 24.370  ? 260 GLY CCC O   1 
ATOM 5749  N N   . MET C 1 244 ? 132.076 5.159   54.353  1.000 23.000  ? 261 MET CCC N   1 
ATOM 5750  C CA  . MET C 1 244 ? 130.693 5.427   54.806  1.000 23.230  ? 261 MET CCC CA  1 
ATOM 5751  C C   . MET C 1 244 ? 130.044 4.116   55.230  1.000 24.240  ? 261 MET CCC C   1 
ATOM 5752  O O   . MET C 1 244 ? 130.298 3.053   54.574  1.000 23.210  ? 261 MET CCC O   1 
ATOM 5753  C CB  . MET C 1 244 ? 129.842 6.042   53.702  1.000 22.360  ? 261 MET CCC CB  1 
ATOM 5754  C CG  . MET C 1 244 ? 130.375 7.364   53.250  1.000 22.780  ? 261 MET CCC CG  1 
ATOM 5755  S SD  . MET C 1 244 ? 129.325 8.028   51.940  1.000 22.780  ? 261 MET CCC SD  1 
ATOM 5756  C CE  . MET C 1 244 ? 130.216 9.567   51.684  1.000 22.290  ? 261 MET CCC CE  1 
ATOM 5757  N N   . PHE C 1 245 ? 129.238 4.202   56.291  1.000 25.090  ? 262 PHE CCC N   1 
ATOM 5758  C CA  . PHE C 1 245 ? 128.279 3.148   56.685  1.000 25.380  ? 262 PHE CCC CA  1 
ATOM 5759  C C   . PHE C 1 245 ? 127.022 3.407   55.881  1.000 24.120  ? 262 PHE CCC C   1 
ATOM 5760  O O   . PHE C 1 245 ? 126.563 4.543   55.934  1.000 23.620  ? 262 PHE CCC O   1 
ATOM 5761  C CB  . PHE C 1 245 ? 127.966 3.186   58.174  1.000 26.480  ? 262 PHE CCC CB  1 
ATOM 5762  C CG  . PHE C 1 245 ? 126.853 2.256   58.568  1.000 28.470  ? 262 PHE CCC CG  1 
ATOM 5763  C CD1 . PHE C 1 245 ? 126.956 0.892   58.328  1.000 28.250  ? 262 PHE CCC CD1 1 
ATOM 5764  C CD2 . PHE C 1 245 ? 125.700 2.742   59.162  1.000 29.120  ? 262 PHE CCC CD2 1 
ATOM 5765  C CE1 . PHE C 1 245 ? 125.936 0.023   58.684  1.000 26.720  ? 262 PHE CCC CE1 1 
ATOM 5766  C CE2 . PHE C 1 245 ? 124.686 1.868   59.521  1.000 29.250  ? 262 PHE CCC CE2 1 
ATOM 5767  C CZ  . PHE C 1 245 ? 124.804 0.514   59.270  1.000 27.390  ? 262 PHE CCC CZ  1 
ATOM 5768  N N   . THR C 1 246 ? 126.542 2.412   55.131  1.000 24.360  ? 263 THR CCC N   1 
ATOM 5769  C CA  . THR C 1 246 ? 125.262 2.514   54.396  1.000 24.960  ? 263 THR CCC CA  1 
ATOM 5770  C C   . THR C 1 246 ? 124.170 1.857   55.243  1.000 27.150  ? 263 THR CCC C   1 
ATOM 5771  O O   . THR C 1 246 ? 124.199 0.618   55.428  1.000 32.990  ? 263 THR CCC O   1 
ATOM 5772  C CB  . THR C 1 246 ? 125.375 1.950   52.981  1.000 24.510  ? 263 THR CCC CB  1 
ATOM 5773  O OG1 . THR C 1 246 ? 126.509 2.523   52.321  1.000 22.750  ? 263 THR CCC OG1 1 
ATOM 5774  C CG2 . THR C 1 246 ? 124.099 2.220   52.213  1.000 25.280  ? 263 THR CCC CG2 1 
ATOM 5775  N N   . ASN C 1 247 ? 123.264 2.683   55.765  1.000 28.510  ? 264 ASN CCC N   1 
ATOM 5776  C CA  . ASN C 1 247 ? 122.045 2.265   56.501  1.000 29.470  ? 264 ASN CCC CA  1 
ATOM 5777  C C   . ASN C 1 247 ? 121.093 1.528   55.555  1.000 27.660  ? 264 ASN CCC C   1 
ATOM 5778  O O   . ASN C 1 247 ? 121.258 1.646   54.327  1.000 29.850  ? 264 ASN CCC O   1 
ATOM 5779  C CB  . ASN C 1 247 ? 121.381 3.473   57.154  1.000 32.210  ? 264 ASN CCC CB  1 
ATOM 5780  C CG  . ASN C 1 247 ? 122.012 3.801   58.500  1.000 36.600  ? 264 ASN CCC CG  1 
ATOM 5781  O OD1 . ASN C 1 247 ? 121.649 3.186   59.542  1.000 33.060  ? 264 ASN CCC OD1 1 
ATOM 5782  N ND2 . ASN C 1 247 ? 122.965 4.740   58.471  1.000 33.190  ? 264 ASN CCC ND2 1 
ATOM 5783  N N   . ARG C 1 248 ? 120.147 0.787   56.123  1.000 25.240  ? 265 ARG CCC N   1 
ATOM 5784  C CA  . ARG C 1 248 ? 119.107 0.005   55.411  1.000 25.200  ? 265 ARG CCC CA  1 
ATOM 5785  C C   . ARG C 1 248 ? 118.407 0.885   54.373  1.000 25.010  ? 265 ARG CCC C   1 
ATOM 5786  O O   . ARG C 1 248 ? 118.135 0.384   53.282  1.000 27.460  ? 265 ARG CCC O   1 
ATOM 5787  C CB  . ARG C 1 248 ? 118.107 -0.548  56.432  1.000 24.630  ? 265 ARG CCC CB  1 
ATOM 5788  C CG  . ARG C 1 248 ? 116.672 -0.703  55.945  1.000 23.230  ? 265 ARG CCC CG  1 
ATOM 5789  C CD  . ARG C 1 248 ? 115.760 -1.334  56.988  1.000 21.920  ? 265 ARG CCC CD  1 
ATOM 5790  N NE  . ARG C 1 248 ? 115.610 -2.789  56.879  1.000 20.320  ? 265 ARG CCC NE  1 
ATOM 5791  C CZ  . ARG C 1 248 ? 116.166 -3.684  57.679  1.000 21.390  ? 265 ARG CCC CZ  1 
ATOM 5792  N NH1 . ARG C 1 248 ? 116.951 -3.318  58.679  1.000 23.870  ? 265 ARG CCC NH1 1 
ATOM 5793  N NH2 . ARG C 1 248 ? 115.959 -4.963  57.465  1.000 22.970  ? 265 ARG CCC NH2 1 
ATOM 5794  N N   . SER C 1 249 ? 118.150 2.148   54.687  1.000 25.460  ? 266 SER CCC N   1 
ATOM 5795  C CA  . SER C 1 249 ? 117.400 3.092   53.817  1.000 26.860  ? 266 SER CCC CA  1 
ATOM 5796  C C   . SER C 1 249 ? 118.228 3.495   52.609  1.000 27.630  ? 266 SER CCC C   1 
ATOM 5797  O O   . SER C 1 249 ? 117.659 4.171   51.715  1.000 30.430  ? 266 SER CCC O   1 
ATOM 5798  C CB  . SER C 1 249 ? 117.051 4.345   54.558  1.000 27.960  ? 266 SER CCC CB  1 
ATOM 5799  O OG  . SER C 1 249 ? 118.242 5.069   54.834  1.000 28.750  ? 266 SER CCC OG  1 
ATOM 5800  N N   . GLY C 1 250 ? 119.540 3.243   52.669  1.000 27.960  ? 267 GLY CCC N   1 
ATOM 5801  C CA  . GLY C 1 250 ? 120.527 3.758   51.698  1.000 27.710  ? 267 GLY CCC CA  1 
ATOM 5802  C C   . GLY C 1 250 ? 121.240 4.995   52.201  1.000 27.340  ? 267 GLY CCC C   1 
ATOM 5803  O O   . GLY C 1 250 ? 122.275 5.342   51.615  1.000 32.940  ? 267 GLY CCC O   1 
ATOM 5804  N N   . SER C 1 251 ? 120.723 5.658   53.235  1.000 25.690  ? 268 SER CCC N   1 
ATOM 5805  C CA  . SER C 1 251 ? 121.324 6.877   53.838  1.000 25.090  ? 268 SER CCC CA  1 
ATOM 5806  C C   . SER C 1 251 ? 122.731 6.538   54.341  1.000 24.250  ? 268 SER CCC C   1 
ATOM 5807  O O   . SER C 1 251 ? 122.913 5.443   54.899  1.000 23.270  ? 268 SER CCC O   1 
ATOM 5808  C CB  . SER C 1 251 ? 120.437 7.424   54.936  1.000 25.480  ? 268 SER CCC CB  1 
ATOM 5809  O OG  . SER C 1 251 ? 119.065 7.382   54.545  1.000 23.780  ? 268 SER CCC OG  1 
ATOM 5810  N N   . GLN C 1 252 ? 123.694 7.434   54.144  1.000 23.540  ? 269 GLN CCC N   1 
ATOM 5811  C CA  . GLN C 1 252 ? 125.111 7.118   54.433  1.000 25.690  ? 269 GLN CCC CA  1 
ATOM 5812  C C   . GLN C 1 252 ? 125.678 8.048   55.511  1.000 25.440  ? 269 GLN CCC C   1 
ATOM 5813  O O   . GLN C 1 252 ? 125.460 9.246   55.421  1.000 26.870  ? 269 GLN CCC O   1 
ATOM 5814  C CB  . GLN C 1 252 ? 125.924 7.238   53.151  1.000 28.110  ? 269 GLN CCC CB  1 
ATOM 5815  C CG  . GLN C 1 252 ? 125.737 6.051   52.224  1.000 28.930  ? 269 GLN CCC CG  1 
ATOM 5816  C CD  . GLN C 1 252 ? 126.327 6.268   50.845  1.000 30.420  ? 269 GLN CCC CD  1 
ATOM 5817  O OE1 . GLN C 1 252 ? 126.406 7.387   50.315  1.000 29.870  ? 269 GLN CCC OE1 1 
ATOM 5818  N NE2 . GLN C 1 252 ? 126.730 5.161   50.246  1.000 31.760  ? 269 GLN CCC NE2 1 
ATOM 5819  N N   . GLN C 1 253 ? 126.425 7.493   56.461  1.000 25.060  ? 270 GLN CCC N   1 
ATOM 5820  C CA  . GLN C 1 253 ? 127.159 8.206   57.542  1.000 22.460  ? 270 GLN CCC CA  1 
ATOM 5821  C C   . GLN C 1 253 ? 128.647 7.882   57.414  1.000 20.220  ? 270 GLN CCC C   1 
ATOM 5822  O O   . GLN C 1 253 ? 128.984 6.710   57.326  1.000 20.300  ? 270 GLN CCC O   1 
ATOM 5823  C CB  . GLN C 1 253 ? 126.671 7.745   58.917  1.000 22.280  ? 270 GLN CCC CB  1 
ATOM 5824  C CG  . GLN C 1 253 ? 125.193 8.039   59.173  1.000 21.860  ? 270 GLN CCC CG  1 
ATOM 5825  C CD  . GLN C 1 253 ? 124.669 7.249   60.342  1.000 21.720  ? 270 GLN CCC CD  1 
ATOM 5826  O OE1 . GLN C 1 253 ? 124.176 6.140   60.184  1.000 25.380  ? 270 GLN CCC OE1 1 
ATOM 5827  N NE2 . GLN C 1 253 ? 124.801 7.795   61.528  1.000 19.840  ? 270 GLN CCC NE2 1 
ATOM 5828  N N   . TRP C 1 254 ? 129.501 8.891   57.365  1.000 19.290  ? 271 TRP CCC N   1 
ATOM 5829  C CA  . TRP C 1 254 ? 130.954 8.698   57.530  1.000 19.810  ? 271 TRP CCC CA  1 
ATOM 5830  C C   . TRP C 1 254 ? 131.187 7.831   58.764  1.000 21.760  ? 271 TRP CCC C   1 
ATOM 5831  O O   . TRP C 1 254 ? 130.448 8.035   59.735  1.000 26.660  ? 271 TRP CCC O   1 
ATOM 5832  C CB  . TRP C 1 254 ? 131.628 10.052  57.723  1.000 20.080  ? 271 TRP CCC CB  1 
ATOM 5833  C CG  . TRP C 1 254 ? 131.532 11.001  56.578  1.000 18.930  ? 271 TRP CCC CG  1 
ATOM 5834  C CD1 . TRP C 1 254 ? 130.857 12.174  56.546  1.000 18.690  ? 271 TRP CCC CD1 1 
ATOM 5835  C CD2 . TRP C 1 254 ? 132.194 10.875  55.318  1.000 19.260  ? 271 TRP CCC CD2 1 
ATOM 5836  N NE1 . TRP C 1 254 ? 131.050 12.792  55.343  1.000 19.540  ? 271 TRP CCC NE1 1 
ATOM 5837  C CE2 . TRP C 1 254 ? 131.858 12.007  54.566  1.000 19.370  ? 271 TRP CCC CE2 1 
ATOM 5838  C CE3 . TRP C 1 254 ? 133.003 9.891   54.740  1.000 20.300  ? 271 TRP CCC CE3 1 
ATOM 5839  C CZ2 . TRP C 1 254 ? 132.295 12.179  53.258  1.000 19.580  ? 271 TRP CCC CZ2 1 
ATOM 5840  C CZ3 . TRP C 1 254 ? 133.446 10.063  53.454  1.000 19.900  ? 271 TRP CCC CZ3 1 
ATOM 5841  C CH2 . TRP C 1 254 ? 133.101 11.204  52.730  1.000 20.030  ? 271 TRP CCC CH2 1 
ATOM 5842  N N   . ARG C 1 255 ? 132.171 6.927   58.760  1.000 22.490  ? 272 ARG CCC N   1 
ATOM 5843  C CA  . ARG C 1 255 ? 132.573 6.172   59.982  1.000 22.620  ? 272 ARG CCC CA  1 
ATOM 5844  C C   . ARG C 1 255 ? 134.078 6.320   60.195  1.000 23.800  ? 272 ARG CCC C   1 
ATOM 5845  O O   . ARG C 1 255 ? 134.847 6.096   59.232  1.000 24.910  ? 272 ARG CCC O   1 
ATOM 5846  C CB  . ARG C 1 255 ? 132.245 4.689   59.869  1.000 22.160  ? 272 ARG CCC CB  1 
ATOM 5847  C CG  . ARG C 1 255 ? 132.660 3.883   61.087  1.000 22.900  ? 272 ARG CCC CG  1 
ATOM 5848  C CD  . ARG C 1 255 ? 131.817 4.293   62.283  1.000 23.610  ? 272 ARG CCC CD  1 
ATOM 5849  N NE  . ARG C 1 255 ? 131.724 3.317   63.374  1.000 23.180  ? 272 ARG CCC NE  1 
ATOM 5850  C CZ  . ARG C 1 255 ? 132.546 3.249   64.412  1.000 24.450  ? 272 ARG CCC CZ  1 
ATOM 5851  N NH1 . ARG C 1 255 ? 133.580 4.070   64.527  1.000 25.570  ? 272 ARG CCC NH1 1 
ATOM 5852  N NH2 . ARG C 1 255 ? 132.341 2.333   65.340  1.000 25.580  ? 272 ARG CCC NH2 1 
ATOM 5853  N N   . GLY C 1 256 ? 134.476 6.661   61.416  1.000 24.490  ? 273 GLY CCC N   1 
ATOM 5854  C CA  . GLY C 1 256 ? 135.878 6.954   61.750  1.000 24.810  ? 273 GLY CCC CA  1 
ATOM 5855  C C   . GLY C 1 256 ? 136.420 5.930   62.726  1.000 26.150  ? 273 GLY CCC C   1 
ATOM 5856  O O   . GLY C 1 256 ? 135.596 5.196   63.315  1.000 26.430  ? 273 GLY CCC O   1 
ATOM 5857  N N   . LEU C 1 257 ? 137.737 5.880   62.887  1.000 27.370  ? 274 LEU CCC N   1 
ATOM 5858  C CA  . LEU C 1 257 ? 138.391 5.017   63.892  1.000 29.780  ? 274 LEU CCC CA  1 
ATOM 5859  C C   . LEU C 1 257 ? 139.556 5.762   64.546  1.000 28.850  ? 274 LEU CCC C   1 
ATOM 5860  O O   . LEU C 1 257 ? 140.200 6.613   63.898  1.000 24.790  ? 274 LEU CCC O   1 
ATOM 5861  C CB  . LEU C 1 257 ? 138.884 3.725   63.233  1.000 32.400  ? 274 LEU CCC CB  1 
ATOM 5862  C CG  . LEU C 1 257 ? 137.800 2.735   62.815  1.000 31.550  ? 274 LEU CCC CG  1 
ATOM 5863  C CD1 . LEU C 1 257 ? 138.418 1.566   62.066  1.000 33.180  ? 274 LEU CCC CD1 1 
ATOM 5864  C CD2 . LEU C 1 257 ? 137.015 2.239   64.019  1.000 30.530  ? 274 LEU CCC CD2 1 
ATOM 5865  N N   . SER C 1 258 ? 139.809 5.410   65.807  1.000 29.820  ? 275 SER CCC N   1 
ATOM 5866  C CA  . SER C 1 258 ? 140.910 5.965   66.633  1.000 28.160  ? 275 SER CCC CA  1 
ATOM 5867  C C   . SER C 1 258 ? 142.260 5.596   66.017  1.000 26.700  ? 275 SER CCC C   1 
ATOM 5868  O O   . SER C 1 258 ? 142.334 4.572   65.305  1.000 28.830  ? 275 SER CCC O   1 
ATOM 5869  C CB  . SER C 1 258 ? 140.784 5.487   68.034  1.000 28.110  ? 275 SER CCC CB  1 
ATOM 5870  O OG  . SER C 1 258 ? 139.494 5.807   68.546  1.000 29.760  ? 275 SER CCC OG  1 
ATOM 5871  N N   . ARG C 1 259 ? 143.270 6.422   66.249  1.000 24.730  ? 276 ARG CCC N   1 
ATOM 5872  C CA  . ARG C 1 259 ? 144.653 6.180   65.779  1.000 25.930  ? 276 ARG CCC CA  1 
ATOM 5873  C C   . ARG C 1 259 ? 145.606 6.127   66.975  1.000 24.720  ? 276 ARG CCC C   1 
ATOM 5874  O O   . ARG C 1 259 ? 145.652 7.094   67.735  1.000 26.090  ? 276 ARG CCC O   1 
ATOM 5875  C CB  . ARG C 1 259 ? 145.109 7.268   64.798  1.000 27.280  ? 276 ARG CCC CB  1 
ATOM 5876  C CG  . ARG C 1 259 ? 146.583 7.141   64.406  1.000 28.330  ? 276 ARG CCC CG  1 
ATOM 5877  C CD  . ARG C 1 259 ? 146.942 7.935   63.178  1.000 29.270  ? 276 ARG CCC CD  1 
ATOM 5878  N NE  . ARG C 1 259 ? 146.265 7.402   62.005  1.000 29.770  ? 276 ARG CCC NE  1 
ATOM 5879  C CZ  . ARG C 1 259 ? 146.766 6.507   61.171  1.000 31.370  ? 276 ARG CCC CZ  1 
ATOM 5880  N NH1 . ARG C 1 259 ? 147.985 6.025   61.329  1.000 35.610  ? 276 ARG CCC NH1 1 
ATOM 5881  N NH2 . ARG C 1 259 ? 146.048 6.120   60.145  1.000 31.830  ? 276 ARG CCC NH2 1 
ATOM 5882  N N   . TYR C 1 260 ? 146.362 5.042   67.098  1.000 23.180  ? 277 TYR CCC N   1 
ATOM 5883  C CA  . TYR C 1 260 ? 147.455 4.875   68.086  1.000 23.070  ? 277 TYR CCC CA  1 
ATOM 5884  C C   . TYR C 1 260 ? 148.702 5.603   67.600  1.000 24.330  ? 277 TYR CCC C   1 
ATOM 5885  O O   . TYR C 1 260 ? 149.011 5.541   66.407  1.000 26.160  ? 277 TYR CCC O   1 
ATOM 5886  C CB  . TYR C 1 260 ? 147.758 3.394   68.251  1.000 22.650  ? 277 TYR CCC CB  1 
ATOM 5887  C CG  . TYR C 1 260 ? 148.973 3.034   69.053  1.000 22.770  ? 277 TYR CCC CG  1 
ATOM 5888  C CD1 . TYR C 1 260 ? 148.926 2.939   70.434  1.000 23.910  ? 277 TYR CCC CD1 1 
ATOM 5889  C CD2 . TYR C 1 260 ? 150.146 2.682   68.420  1.000 23.580  ? 277 TYR CCC CD2 1 
ATOM 5890  C CE1 . TYR C 1 260 ? 150.026 2.531   71.175  1.000 23.350  ? 277 TYR CCC CE1 1 
ATOM 5891  C CE2 . TYR C 1 260 ? 151.256 2.281   69.141  1.000 24.620  ? 277 TYR CCC CE2 1 
ATOM 5892  C CZ  . TYR C 1 260 ? 151.194 2.203   70.522  1.000 23.880  ? 277 TYR CCC CZ  1 
ATOM 5893  O OH  . TYR C 1 260 ? 152.291 1.818   71.229  1.000 24.390  ? 277 TYR CCC OH  1 
ATOM 5894  N N   . PHE C 1 261 ? 149.395 6.272   68.515  1.000 25.600  ? 278 PHE CCC N   1 
ATOM 5895  C CA  . PHE C 1 261 ? 150.745 6.855   68.304  1.000 24.700  ? 278 PHE CCC CA  1 
ATOM 5896  C C   . PHE C 1 261 ? 151.694 6.337   69.387  1.000 25.910  ? 278 PHE CCC C   1 
ATOM 5897  O O   . PHE C 1 261 ? 151.297 6.255   70.547  1.000 27.600  ? 278 PHE CCC O   1 
ATOM 5898  C CB  . PHE C 1 261 ? 150.700 8.383   68.413  1.000 22.210  ? 278 PHE CCC CB  1 
ATOM 5899  C CG  . PHE C 1 261 ? 149.927 9.106   67.343  1.000 19.600  ? 278 PHE CCC CG  1 
ATOM 5900  C CD1 . PHE C 1 261 ? 148.541 9.121   67.368  1.000 19.550  ? 278 PHE CCC CD1 1 
ATOM 5901  C CD2 . PHE C 1 261 ? 150.581 9.818   66.352  1.000 17.540  ? 278 PHE CCC CD2 1 
ATOM 5902  C CE1 . PHE C 1 261 ? 147.810 9.804   66.410  1.000 18.760  ? 278 PHE CCC CE1 1 
ATOM 5903  C CE2 . PHE C 1 261 ? 149.850 10.506  65.404  1.000 18.450  ? 278 PHE CCC CE2 1 
ATOM 5904  C CZ  . PHE C 1 261 ? 148.465 10.496  65.435  1.000 18.520  ? 278 PHE CCC CZ  1 
ATOM 5905  N N   . LYS C 1 262 ? 152.921 6.015   69.012  1.000 25.980  ? 279 LYS CCC N   1 
ATOM 5906  C CA  . LYS C 1 262 ? 154.025 5.814   69.975  1.000 26.790  ? 279 LYS CCC CA  1 
ATOM 5907  C C   . LYS C 1 262 ? 155.230 6.551   69.400  1.000 28.140  ? 279 LYS CCC C   1 
ATOM 5908  O O   . LYS C 1 262 ? 155.728 6.135   68.332  1.000 24.990  ? 279 LYS CCC O   1 
ATOM 5909  C CB  . LYS C 1 262 ? 154.291 4.327   70.192  1.000 25.700  ? 279 LYS CCC CB  1 
ATOM 5910  C CG  . LYS C 1 262 ? 155.371 3.995   71.204  1.000 26.510  ? 279 LYS CCC CG  1 
ATOM 5911  C CD  . LYS C 1 262 ? 155.517 2.493   71.368  1.000 29.980  ? 279 LYS CCC CD  1 
ATOM 5912  C CE  . LYS C 1 262 ? 156.739 2.022   72.125  1.000 33.250  ? 279 LYS CCC CE  1 
ATOM 5913  N NZ  . LYS C 1 262 ? 157.318 0.810   71.473  1.000 35.540  ? 279 LYS CCC NZ  1 
ATOM 5914  N N   . VAL C 1 263 ? 155.640 7.631   70.061  1.000 28.980  ? 280 VAL CCC N   1 
ATOM 5915  C CA  . VAL C 1 263 ? 156.751 8.477   69.558  1.000 31.830  ? 280 VAL CCC CA  1 
ATOM 5916  C C   . VAL C 1 263 ? 157.955 8.354   70.496  1.000 34.510  ? 280 VAL CCC C   1 
ATOM 5917  O O   . VAL C 1 263 ? 157.815 8.659   71.658  1.000 39.120  ? 280 VAL CCC O   1 
ATOM 5918  C CB  . VAL C 1 263 ? 156.271 9.919   69.366  1.000 33.000  ? 280 VAL CCC CB  1 
ATOM 5919  C CG1 . VAL C 1 263 ? 157.382 10.803  68.811  1.000 35.090  ? 280 VAL CCC CG1 1 
ATOM 5920  C CG2 . VAL C 1 263 ? 155.045 9.967   68.456  1.000 33.730  ? 280 VAL CCC CG2 1 
ATOM 5921  N N   . GLN C 1 264 ? 159.077 7.847   69.989  1.000 40.630  ? 281 GLN CCC N   1 
ATOM 5922  C CA  . GLN C 1 264 ? 160.420 7.951   70.616  1.000 45.260  ? 281 GLN CCC CA  1 
ATOM 5923  C C   . GLN C 1 264 ? 160.860 9.416   70.518  1.000 41.440  ? 281 GLN CCC C   1 
ATOM 5924  O O   . GLN C 1 264 ? 160.730 10.019  69.453  1.000 47.190  ? 281 GLN CCC O   1 
ATOM 5925  C CB  . GLN C 1 264 ? 161.469 7.087   69.907  1.000 60.270  ? 281 GLN CCC CB  1 
ATOM 5926  C CG  . GLN C 1 264 ? 161.169 5.591   69.852  1.000 68.760  ? 281 GLN CCC CG  1 
ATOM 5927  C CD  . GLN C 1 264 ? 161.320 4.950   71.201  1.000 74.930  ? 281 GLN CCC CD  1 
ATOM 5928  O OE1 . GLN C 1 264 ? 161.976 5.478   72.096  1.000 74.900  ? 281 GLN CCC OE1 1 
ATOM 5929  N NE2 . GLN C 1 264 ? 160.698 3.794   71.356  1.000 74.250  ? 281 GLN CCC NE2 1 
ATOM 5930  N N   . LEU C 1 265 ? 161.383 9.969   71.597  1.000 38.410  ? 282 LEU CCC N   1 
ATOM 5931  C CA  . LEU C 1 265 ? 161.944 11.335  71.624  1.000 36.870  ? 282 LEU CCC CA  1 
ATOM 5932  C C   . LEU C 1 265 ? 163.339 11.266  72.249  1.000 38.070  ? 282 LEU CCC C   1 
ATOM 5933  O O   . LEU C 1 265 ? 163.565 10.375  73.070  1.000 40.090  ? 282 LEU CCC O   1 
ATOM 5934  C CB  . LEU C 1 265 ? 160.996 12.191  72.456  1.000 39.350  ? 282 LEU CCC CB  1 
ATOM 5935  C CG  . LEU C 1 265 ? 159.613 12.429  71.859  1.000 41.190  ? 282 LEU CCC CG  1 
ATOM 5936  C CD1 . LEU C 1 265 ? 158.538 12.334  72.930  1.000 42.750  ? 282 LEU CCC CD1 1 
ATOM 5937  C CD2 . LEU C 1 265 ? 159.548 13.784  71.175  1.000 39.860  ? 282 LEU CCC CD2 1 
ATOM 5938  N N   . ARG C 1 266 ? 164.252 12.152  71.857  1.000 37.620  ? 283 ARG CCC N   1 
ATOM 5939  C CA  . ARG C 1 266 ? 165.584 12.303  72.510  1.000 38.660  ? 283 ARG CCC CA  1 
ATOM 5940  C C   . ARG C 1 266 ? 165.835 13.801  72.742  1.000 40.400  ? 283 ARG CCC C   1 
ATOM 5941  O O   . ARG C 1 266 ? 165.040 14.621  72.246  1.000 47.580  ? 283 ARG CCC O   1 
ATOM 5942  C CB  . ARG C 1 266 ? 166.672 11.642  71.665  1.000 38.200  ? 283 ARG CCC CB  1 
ATOM 5943  C CG  . ARG C 1 266 ? 167.030 12.429  70.417  1.000 39.850  ? 283 ARG CCC CG  1 
ATOM 5944  C CD  . ARG C 1 266 ? 167.893 11.623  69.464  1.000 41.250  ? 283 ARG CCC CD  1 
ATOM 5945  N NE  . ARG C 1 266 ? 168.114 12.392  68.239  1.000 42.010  ? 283 ARG CCC NE  1 
ATOM 5946  C CZ  . ARG C 1 266 ? 168.537 11.880  67.096  1.000 42.420  ? 283 ARG CCC CZ  1 
ATOM 5947  N NH1 . ARG C 1 266 ? 168.820 10.590  67.038  1.000 44.820  ? 283 ARG CCC NH1 1 
ATOM 5948  N NH2 . ARG C 1 266 ? 168.688 12.644  66.023  1.000 40.130  ? 283 ARG CCC NH2 1 
ATOM 5949  N N   . LYS C 1 267 ? 166.895 14.150  73.464  1.000 37.870  ? 284 LYS CCC N   1 
ATOM 5950  C CA  . LYS C 1 267 ? 167.211 15.557  73.821  1.000 38.210  ? 284 LYS CCC CA  1 
ATOM 5951  C C   . LYS C 1 267 ? 168.253 16.082  72.817  1.000 40.110  ? 284 LYS CCC C   1 
ATOM 5952  O O   . LYS C 1 267 ? 169.295 15.419  72.685  1.000 39.550  ? 284 LYS CCC O   1 
ATOM 5953  C CB  . LYS C 1 267 ? 167.786 15.571  75.232  1.000 39.050  ? 284 LYS CCC CB  1 
ATOM 5954  C CG  . LYS C 1 267 ? 166.836 15.095  76.315  1.000 36.420  ? 284 LYS CCC CG  1 
ATOM 5955  C CD  . LYS C 1 267 ? 167.437 15.119  77.688  1.000 35.120  ? 284 LYS CCC CD  1 
ATOM 5956  C CE  . LYS C 1 267 ? 166.443 14.653  78.718  1.000 37.290  ? 284 LYS CCC CE  1 
ATOM 5957  N NZ  . LYS C 1 267 ? 167.067 14.528  80.052  1.000 41.380  ? 284 LYS CCC NZ  1 
ATOM 5958  N N   . ARG C 1 268 ? 168.019 17.283  72.290  1.000 41.420  ? 285 ARG CCC N   1 
ATOM 5959  C CA  . ARG C 1 268 ? 168.978 17.922  71.365  1.000 44.890  ? 285 ARG CCC CA  1 
ATOM 5960  C C   . ARG C 1 268 ? 169.366 19.289  71.919  1.000 46.450  ? 285 ARG CCC C   1 
ATOM 5961  O O   . ARG C 1 268 ? 168.459 20.033  72.291  1.000 50.440  ? 285 ARG CCC O   1 
ATOM 5962  C CB  . ARG C 1 268 ? 168.338 18.102  69.991  1.000 50.680  ? 285 ARG CCC CB  1 
ATOM 5963  C CG  . ARG C 1 268 ? 169.323 18.439  68.885  1.000 56.640  ? 285 ARG CCC CG  1 
ATOM 5964  C CD  . ARG C 1 268 ? 169.506 17.264  67.951  1.000 61.060  ? 285 ARG CCC CD  1 
ATOM 5965  N NE  . ARG C 1 268 ? 170.514 17.521  66.939  1.000 58.300  ? 285 ARG CCC NE  1 
ATOM 5966  C CZ  . ARG C 1 268 ? 170.551 16.927  65.757  1.000 58.600  ? 285 ARG CCC CZ  1 
ATOM 5967  N NH1 . ARG C 1 268 ? 169.635 16.029  65.445  1.000 61.090  ? 285 ARG CCC NH1 1 
ATOM 5968  N NH2 . ARG C 1 268 ? 171.503 17.225  64.893  1.000 64.400  ? 285 ARG CCC NH2 1 
ATOM 5969  N N   . ARG C 1 269 ? 170.660 19.579  72.015  1.000 49.720  ? 286 ARG CCC N   1 
ATOM 5970  C CA  . ARG C 1 269 ? 171.153 20.922  72.425  1.000 49.220  ? 286 ARG CCC CA  1 
ATOM 5971  C C   . ARG C 1 269 ? 170.815 21.922  71.306  1.000 50.270  ? 286 ARG CCC C   1 
ATOM 5972  O O   . ARG C 1 269 ? 170.851 21.540  70.127  1.000 49.830  ? 286 ARG CCC O   1 
ATOM 5973  C CB  . ARG C 1 269 ? 172.643 20.756  72.748  1.000 46.810  ? 286 ARG CCC CB  1 
ATOM 5974  N N   . VAL C 1 270 ? 170.438 23.148  71.675  1.000 49.280  ? 287 VAL CCC N   1 
ATOM 5975  C CA  . VAL C 1 270 ? 169.919 24.231  70.781  1.000 46.010  ? 287 VAL CCC CA  1 
ATOM 5976  C C   . VAL C 1 270 ? 170.445 25.579  71.312  1.000 46.210  ? 287 VAL CCC C   1 
ATOM 5977  O O   . VAL C 1 270 ? 170.478 25.728  72.540  1.000 49.820  ? 287 VAL CCC O   1 
ATOM 5978  C CB  . VAL C 1 270 ? 168.374 24.182  70.768  1.000 44.410  ? 287 VAL CCC CB  1 
ATOM 5979  C CG1 . VAL C 1 270 ? 167.769 25.238  69.860  1.000 45.280  ? 287 VAL CCC CG1 1 
ATOM 5980  C CG2 . VAL C 1 270 ? 167.840 22.793  70.419  1.000 44.530  ? 287 VAL CCC CG2 1 
ATOM 5981  N N   . LYS C 1 271 ? 170.848 26.529  70.457  1.000 50.680  ? 288 LYS CCC N   1 
ATOM 5982  C CA  . LYS C 1 271 ? 171.105 27.959  70.832  1.000 53.840  ? 288 LYS CCC CA  1 
ATOM 5983  C C   . LYS C 1 271 ? 169.868 28.780  70.436  1.000 61.660  ? 288 LYS CCC C   1 
ATOM 5984  O O   . LYS C 1 271 ? 169.489 28.695  69.241  1.000 60.700  ? 288 LYS CCC O   1 
ATOM 5985  C CB  . LYS C 1 271 ? 172.396 28.514  70.200  1.000 50.770  ? 288 LYS CCC CB  1 
ATOM 5986  N N   . ASN C 1 272 ? 169.243 29.493  71.402  1.000 72.450  ? 289 ASN CCC N   1 
ATOM 5987  C CA  . ASN C 1 272 ? 167.959 30.246  71.272  1.000 72.550  ? 289 ASN CCC CA  1 
ATOM 5988  C C   . ASN C 1 272 ? 168.148 31.682  71.778  1.000 72.910  ? 289 ASN CCC C   1 
ATOM 5989  O O   . ASN C 1 272 ? 168.942 32.458  71.262  1.000 70.360  ? 289 ASN CCC O   1 
ATOM 5990  C CB  . ASN C 1 272 ? 166.824 29.573  72.026  1.000 66.530  ? 289 ASN CCC CB  1 
ATOM 5991  N N   . VAL D 1 7   ? 162.386 -8.226  83.203  1.000 49.420  ? 24  VAL DDD N   1 
ATOM 5992  C CA  . VAL D 1 7   ? 163.385 -9.153  82.567  1.000 49.930  ? 24  VAL DDD CA  1 
ATOM 5993  C C   . VAL D 1 7   ? 164.466 -8.329  81.861  1.000 48.100  ? 24  VAL DDD C   1 
ATOM 5994  O O   . VAL D 1 7   ? 164.191 -7.833  80.763  1.000 51.930  ? 24  VAL DDD O   1 
ATOM 5995  C CB  . VAL D 1 7   ? 162.717 -10.112 81.590  1.000 46.270  ? 24  VAL DDD CB  1 
ATOM 5996  N N   . GLU D 1 8   ? 165.667 -8.232  82.441  1.000 47.640  ? 25  GLU DDD N   1 
ATOM 5997  C CA  . GLU D 1 8   ? 166.910 -7.820  81.732  1.000 48.340  ? 25  GLU DDD CA  1 
ATOM 5998  C C   . GLU D 1 8   ? 167.321 -8.960  80.789  1.000 42.870  ? 25  GLU DDD C   1 
ATOM 5999  O O   . GLU D 1 8   ? 167.451 -10.098 81.245  1.000 41.120  ? 25  GLU DDD O   1 
ATOM 6000  C CB  . GLU D 1 8   ? 168.038 -7.460  82.697  1.000 48.370  ? 25  GLU DDD CB  1 
ATOM 6001  N N   . VAL D 1 9   ? 167.503 -8.664  79.504  1.000 40.200  ? 26  VAL DDD N   1 
ATOM 6002  C CA  . VAL D 1 9   ? 167.826 -9.673  78.461  1.000 41.440  ? 26  VAL DDD CA  1 
ATOM 6003  C C   . VAL D 1 9   ? 169.336 -9.679  78.250  1.000 41.950  ? 26  VAL DDD C   1 
ATOM 6004  O O   . VAL D 1 9   ? 169.869 -8.681  77.794  1.000 44.670  ? 26  VAL DDD O   1 
ATOM 6005  C CB  . VAL D 1 9   ? 167.068 -9.387  77.157  1.000 44.540  ? 26  VAL DDD CB  1 
ATOM 6006  C CG1 . VAL D 1 9   ? 167.476 -10.328 76.026  1.000 44.530  ? 26  VAL DDD CG1 1 
ATOM 6007  C CG2 . VAL D 1 9   ? 165.558 -9.435  77.398  1.000 44.920  ? 26  VAL DDD CG2 1 
ATOM 6008  N N   . LEU D 1 10  ? 169.969 -10.805 78.551  1.000 49.060  ? 27  LEU DDD N   1 
ATOM 6009  C CA  . LEU D 1 10  ? 171.435 -11.016 78.478  1.000 50.960  ? 27  LEU DDD CA  1 
ATOM 6010  C C   . LEU D 1 10  ? 171.717 -11.671 77.121  1.000 48.810  ? 27  LEU DDD C   1 
ATOM 6011  O O   . LEU D 1 10  ? 170.865 -11.527 76.223  1.000 43.020  ? 27  LEU DDD O   1 
ATOM 6012  C CB  . LEU D 1 10  ? 171.871 -11.904 79.657  1.000 58.370  ? 27  LEU DDD CB  1 
ATOM 6013  C CG  . LEU D 1 10  ? 172.372 -11.243 80.939  1.000 57.600  ? 27  LEU DDD CG  1 
ATOM 6014  C CD1 . LEU D 1 10  ? 173.737 -10.608 80.686  1.000 61.540  ? 27  LEU DDD CD1 1 
ATOM 6015  C CD2 . LEU D 1 10  ? 171.361 -10.247 81.489  1.000 53.310  ? 27  LEU DDD CD2 1 
ATOM 6016  N N   . GLU D 1 11  ? 172.848 -12.374 76.990  1.000 57.690  ? 28  GLU DDD N   1 
ATOM 6017  C CA  . GLU D 1 11  ? 173.418 -12.789 75.684  1.000 65.340  ? 28  GLU DDD CA  1 
ATOM 6018  C C   . GLU D 1 11  ? 172.708 -14.055 75.187  1.000 55.760  ? 28  GLU DDD C   1 
ATOM 6019  O O   . GLU D 1 11  ? 172.020 -14.713 75.982  1.000 52.830  ? 28  GLU DDD O   1 
ATOM 6020  C CB  . GLU D 1 11  ? 174.944 -12.898 75.818  1.000 80.040  ? 28  GLU DDD CB  1 
ATOM 6021  C CG  . GLU D 1 11  ? 175.687 -11.551 75.658  1.000 94.210  ? 28  GLU DDD CG  1 
ATOM 6022  C CD  . GLU D 1 11  ? 175.297 -10.379 76.567  1.000 97.400  ? 28  GLU DDD CD  1 
ATOM 6023  O OE1 . GLU D 1 11  ? 174.720 -10.627 77.650  1.000 93.650  ? 28  GLU DDD OE1 1 
ATOM 6024  O OE2 . GLU D 1 11  ? 175.542 -9.216  76.179  1.000 97.610  ? 28  GLU DDD OE2 1 
ATOM 6025  N N   . VAL D 1 12  ? 172.840 -14.341 73.891  1.000 56.300  ? 29  VAL DDD N   1 
ATOM 6026  C CA  . VAL D 1 12  ? 172.223 -15.527 73.225  1.000 56.780  ? 29  VAL DDD CA  1 
ATOM 6027  C C   . VAL D 1 12  ? 173.098 -16.740 73.542  1.000 55.910  ? 29  VAL DDD C   1 
ATOM 6028  O O   . VAL D 1 12  ? 174.271 -16.699 73.163  1.000 59.130  ? 29  VAL DDD O   1 
ATOM 6029  C CB  . VAL D 1 12  ? 172.112 -15.328 71.694  1.000 55.680  ? 29  VAL DDD CB  1 
ATOM 6030  C CG1 . VAL D 1 12  ? 171.552 -16.564 71.000  1.000 54.990  ? 29  VAL DDD CG1 1 
ATOM 6031  C CG2 . VAL D 1 12  ? 171.296 -14.098 71.317  1.000 57.090  ? 29  VAL DDD CG2 1 
ATOM 6032  N N   . LYS D 1 13  ? 172.558 -17.780 74.176  1.000 58.930  ? 30  LYS DDD N   1 
ATOM 6033  C CA  . LYS D 1 13  ? 173.269 -19.078 74.351  1.000 65.230  ? 30  LYS DDD CA  1 
ATOM 6034  C C   . LYS D 1 13  ? 173.359 -19.748 72.975  1.000 60.980  ? 30  LYS DDD C   1 
ATOM 6035  O O   . LYS D 1 13  ? 172.311 -19.862 72.322  1.000 58.560  ? 30  LYS DDD O   1 
ATOM 6036  C CB  . LYS D 1 13  ? 172.571 -19.991 75.380  1.000 68.220  ? 30  LYS DDD CB  1 
ATOM 6037  C CG  . LYS D 1 13  ? 172.693 -19.566 76.844  1.000 78.130  ? 30  LYS DDD CG  1 
ATOM 6038  C CD  . LYS D 1 13  ? 174.132 -19.537 77.436  1.000 80.410  ? 30  LYS DDD CD  1 
ATOM 6039  C CE  . LYS D 1 13  ? 174.295 -18.629 78.646  1.000 70.470  ? 30  LYS DDD CE  1 
ATOM 6040  N NZ  . LYS D 1 13  ? 175.302 -19.164 79.594  1.000 65.890  ? 30  LYS DDD NZ  1 
ATOM 6041  N N   . THR D 1 14  ? 174.581 -20.108 72.544  1.000 60.000  ? 31  THR DDD N   1 
ATOM 6042  C CA  . THR D 1 14  ? 174.878 -20.980 71.377  1.000 59.470  ? 31  THR DDD CA  1 
ATOM 6043  C C   . THR D 1 14  ? 175.387 -22.318 71.920  1.000 57.810  ? 31  THR DDD C   1 
ATOM 6044  O O   . THR D 1 14  ? 175.585 -22.426 73.162  1.000 63.310  ? 31  THR DDD O   1 
ATOM 6045  C CB  . THR D 1 14  ? 175.883 -20.366 70.391  1.000 60.610  ? 31  THR DDD CB  1 
ATOM 6046  O OG1 . THR D 1 14  ? 177.122 -20.180 71.073  1.000 58.110  ? 31  THR DDD OG1 1 
ATOM 6047  C CG2 . THR D 1 14  ? 175.432 -19.048 69.793  1.000 59.730  ? 31  THR DDD CG2 1 
ATOM 6048  N N   . GLY D 1 15  ? 175.604 -23.293 71.034  1.000 55.610  ? 32  GLY DDD N   1 
ATOM 6049  C CA  . GLY D 1 15  ? 176.039 -24.650 71.419  1.000 62.260  ? 32  GLY DDD CA  1 
ATOM 6050  C C   . GLY D 1 15  ? 175.181 -25.729 70.782  1.000 63.040  ? 32  GLY DDD C   1 
ATOM 6051  O O   . GLY D 1 15  ? 174.452 -25.380 69.841  1.000 59.340  ? 32  GLY DDD O   1 
ATOM 6052  N N   . VAL D 1 16  ? 175.245 -26.955 71.313  1.000 65.690  ? 33  VAL DDD N   1 
ATOM 6053  C CA  . VAL D 1 16  ? 174.852 -28.194 70.580  1.000 69.880  ? 33  VAL DDD CA  1 
ATOM 6054  C C   . VAL D 1 16  ? 173.323 -28.257 70.452  1.000 70.870  ? 33  VAL DDD C   1 
ATOM 6055  O O   . VAL D 1 16  ? 172.841 -28.814 69.437  1.000 84.010  ? 33  VAL DDD O   1 
ATOM 6056  C CB  . VAL D 1 16  ? 175.407 -29.477 71.229  1.000 73.830  ? 33  VAL DDD CB  1 
ATOM 6057  C CG1 . VAL D 1 16  ? 175.159 -30.669 70.307  1.000 74.710  ? 33  VAL DDD CG1 1 
ATOM 6058  C CG2 . VAL D 1 16  ? 176.881 -29.374 71.615  1.000 76.140  ? 33  VAL DDD CG2 1 
ATOM 6059  N N   . ASP D 1 17  ? 172.587 -27.719 71.420  1.000 59.280  ? 34  ASP DDD N   1 
ATOM 6060  C CA  . ASP D 1 17  ? 171.104 -27.817 71.444  1.000 57.690  ? 34  ASP DDD CA  1 
ATOM 6061  C C   . ASP D 1 17  ? 170.560 -26.467 71.872  1.000 56.170  ? 34  ASP DDD C   1 
ATOM 6062  O O   . ASP D 1 17  ? 169.867 -26.413 72.904  1.000 56.860  ? 34  ASP DDD O   1 
ATOM 6063  C CB  . ASP D 1 17  ? 170.613 -28.931 72.381  1.000 63.380  ? 34  ASP DDD CB  1 
ATOM 6064  C CG  . ASP D 1 17  ? 170.147 -30.171 71.649  1.000 64.800  ? 34  ASP DDD CG  1 
ATOM 6065  O OD1 . ASP D 1 17  ? 170.283 -30.212 70.419  1.000 65.070  ? 34  ASP DDD OD1 1 
ATOM 6066  O OD2 . ASP D 1 17  ? 169.722 -31.103 72.311  1.000 67.520  ? 34  ASP DDD OD2 1 
ATOM 6067  N N   . SER D 1 18  ? 170.876 -25.409 71.124  1.000 56.370  ? 35  SER DDD N   1 
ATOM 6068  C CA  . SER D 1 18  ? 170.499 -24.008 71.484  1.000 54.210  ? 35  SER DDD CA  1 
ATOM 6069  C C   . SER D 1 18  ? 169.348 -23.499 70.613  1.000 50.170  ? 35  SER DDD C   1 
ATOM 6070  O O   . SER D 1 18  ? 168.723 -22.493 71.003  1.000 52.620  ? 35  SER DDD O   1 
ATOM 6071  C CB  . SER D 1 18  ? 171.677 -23.076 71.425  1.000 54.660  ? 35  SER DDD CB  1 
ATOM 6072  O OG  . SER D 1 18  ? 172.515 -23.405 70.338  1.000 55.940  ? 35  SER DDD OG  1 
ATOM 6073  N N   . ILE D 1 19  ? 169.055 -24.173 69.498  1.000 46.520  ? 36  ILE DDD N   1 
ATOM 6074  C CA  . ILE D 1 19  ? 167.922 -23.830 68.592  1.000 44.290  ? 36  ILE DDD CA  1 
ATOM 6075  C C   . ILE D 1 19  ? 166.886 -24.959 68.674  1.000 39.620  ? 36  ILE DDD C   1 
ATOM 6076  O O   . ILE D 1 19  ? 167.259 -26.070 69.046  1.000 42.560  ? 36  ILE DDD O   1 
ATOM 6077  C CB  . ILE D 1 19  ? 168.436 -23.538 67.162  1.000 47.910  ? 36  ILE DDD CB  1 
ATOM 6078  C CG1 . ILE D 1 19  ? 167.395 -22.789 66.314  1.000 60.700  ? 36  ILE DDD CG1 1 
ATOM 6079  C CG2 . ILE D 1 19  ? 168.892 -24.807 66.468  1.000 46.680  ? 36  ILE DDD CG2 1 
ATOM 6080  C CD1 . ILE D 1 19  ? 167.919 -21.658 65.399  1.000 62.470  ? 36  ILE DDD CD1 1 
ATOM 6081  N N   . THR D 1 20  ? 165.618 -24.654 68.391  1.000 38.860  ? 37  THR DDD N   1 
ATOM 6082  C CA  . THR D 1 20  ? 164.496 -25.627 68.244  1.000 41.790  ? 37  THR DDD CA  1 
ATOM 6083  C C   . THR D 1 20  ? 163.454 -25.044 67.276  1.000 43.250  ? 37  THR DDD C   1 
ATOM 6084  O O   . THR D 1 20  ? 163.572 -23.851 66.956  1.000 38.940  ? 37  THR DDD O   1 
ATOM 6085  C CB  . THR D 1 20  ? 163.872 -25.982 69.600  1.000 39.200  ? 37  THR DDD CB  1 
ATOM 6086  O OG1 . THR D 1 20  ? 162.958 -27.060 69.468  1.000 35.090  ? 37  THR DDD OG1 1 
ATOM 6087  C CG2 . THR D 1 20  ? 163.098 -24.833 70.202  1.000 41.290  ? 37  THR DDD CG2 1 
ATOM 6088  N N   . GLU D 1 21  ? 162.487 -25.864 66.841  1.000 47.020  ? 38  GLU DDD N   1 
ATOM 6089  C CA  . GLU D 1 21  ? 161.439 -25.524 65.836  1.000 43.030  ? 38  GLU DDD CA  1 
ATOM 6090  C C   . GLU D 1 21  ? 160.071 -26.015 66.307  1.000 38.450  ? 38  GLU DDD C   1 
ATOM 6091  O O   . GLU D 1 21  ? 159.940 -27.190 66.637  1.000 38.470  ? 38  GLU DDD O   1 
ATOM 6092  C CB  . GLU D 1 21  ? 161.667 -26.210 64.492  1.000 44.680  ? 38  GLU DDD CB  1 
ATOM 6093  C CG  . GLU D 1 21  ? 162.742 -25.572 63.650  1.000 48.940  ? 38  GLU DDD CG  1 
ATOM 6094  C CD  . GLU D 1 21  ? 162.680 -26.007 62.184  1.000 52.880  ? 38  GLU DDD CD  1 
ATOM 6095  O OE1 . GLU D 1 21  ? 161.807 -26.861 61.843  1.000 49.080  ? 38  GLU DDD OE1 1 
ATOM 6096  O OE2 . GLU D 1 21  ? 163.493 -25.495 61.380  1.000 57.210  ? 38  GLU DDD OE2 1 
ATOM 6097  N N   . VAL D 1 22  ? 159.086 -25.131 66.302  1.000 34.250  ? 39  VAL DDD N   1 
ATOM 6098  C CA  . VAL D 1 22  ? 157.643 -25.481 66.301  1.000 29.970  ? 39  VAL DDD CA  1 
ATOM 6099  C C   . VAL D 1 22  ? 157.150 -25.358 64.857  1.000 34.360  ? 39  VAL DDD C   1 
ATOM 6100  O O   . VAL D 1 22  ? 157.582 -24.407 64.140  1.000 38.910  ? 39  VAL DDD O   1 
ATOM 6101  C CB  . VAL D 1 22  ? 156.870 -24.548 67.236  1.000 26.310  ? 39  VAL DDD CB  1 
ATOM 6102  C CG1 . VAL D 1 22  ? 155.389 -24.764 67.114  1.000 27.750  ? 39  VAL DDD CG1 1 
ATOM 6103  C CG2 . VAL D 1 22  ? 157.319 -24.692 68.673  1.000 26.020  ? 39  VAL DDD CG2 1 
ATOM 6104  N N   . GLU D 1 23  ? 156.285 -26.276 64.432  1.000 35.710  ? 40  GLU DDD N   1 
ATOM 6105  C CA  . GLU D 1 23  ? 155.651 -26.287 63.087  1.000 35.490  ? 40  GLU DDD CA  1 
ATOM 6106  C C   . GLU D 1 23  ? 154.242 -26.823 63.296  1.000 37.570  ? 40  GLU DDD C   1 
ATOM 6107  O O   . GLU D 1 23  ? 154.124 -28.003 63.581  1.000 47.120  ? 40  GLU DDD O   1 
ATOM 6108  C CB  . GLU D 1 23  ? 156.471 -27.159 62.123  1.000 34.440  ? 40  GLU DDD CB  1 
ATOM 6109  C CG  . GLU D 1 23  ? 156.022 -27.119 60.667  1.000 36.200  ? 40  GLU DDD CG  1 
ATOM 6110  C CD  . GLU D 1 23  ? 156.706 -28.137 59.768  1.000 39.950  ? 40  GLU DDD CD  1 
ATOM 6111  O OE1 . GLU D 1 23  ? 156.448 -29.357 59.982  1.000 45.360  ? 40  GLU DDD OE1 1 
ATOM 6112  O OE2 . GLU D 1 23  ? 157.517 -27.717 58.879  1.000 35.890  ? 40  GLU DDD OE2 1 
ATOM 6113  N N   . CYS D 1 24  ? 153.209 -25.995 63.244  1.000 39.380  ? 41  CYS DDD N   1 
ATOM 6114  C CA  . CYS D 1 24  ? 151.824 -26.514 63.298  1.000 41.180  ? 41  CYS DDD CA  1 
ATOM 6115  C C   . CYS D 1 24  ? 150.941 -25.756 62.315  1.000 40.100  ? 41  CYS DDD C   1 
ATOM 6116  O O   . CYS D 1 24  ? 151.445 -24.860 61.606  1.000 43.760  ? 41  CYS DDD O   1 
ATOM 6117  C CB  . CYS D 1 24  ? 151.312 -26.426 64.718  1.000 44.090  ? 41  CYS DDD CB  1 
ATOM 6118  S SG  . CYS D 1 24  ? 151.059 -24.706 65.197  1.000 52.740  ? 41  CYS DDD SG  1 
ATOM 6119  N N   . PHE D 1 25  ? 149.677 -26.166 62.238  1.000 39.780  ? 42  PHE DDD N   1 
ATOM 6120  C CA  . PHE D 1 25  ? 148.594 -25.482 61.481  1.000 41.250  ? 42  PHE DDD CA  1 
ATOM 6121  C C   . PHE D 1 25  ? 147.540 -25.065 62.504  1.000 36.760  ? 42  PHE DDD C   1 
ATOM 6122  O O   . PHE D 1 25  ? 147.416 -25.772 63.507  1.000 37.520  ? 42  PHE DDD O   1 
ATOM 6123  C CB  . PHE D 1 25  ? 148.017 -26.379 60.384  1.000 46.060  ? 42  PHE DDD CB  1 
ATOM 6124  C CG  . PHE D 1 25  ? 147.434 -27.658 60.911  1.000 52.960  ? 42  PHE DDD CG  1 
ATOM 6125  C CD1 . PHE D 1 25  ? 146.167 -27.675 61.471  1.000 58.630  ? 42  PHE DDD CD1 1 
ATOM 6126  C CD2 . PHE D 1 25  ? 148.168 -28.836 60.895  1.000 60.140  ? 42  PHE DDD CD2 1 
ATOM 6127  C CE1 . PHE D 1 25  ? 145.632 -28.853 61.984  1.000 59.290  ? 42  PHE DDD CE1 1 
ATOM 6128  C CE2 . PHE D 1 25  ? 147.642 -30.008 61.426  1.000 58.720  ? 42  PHE DDD CE2 1 
ATOM 6129  C CZ  . PHE D 1 25  ? 146.371 -30.015 61.961  1.000 56.310  ? 42  PHE DDD CZ  1 
ATOM 6130  N N   . LEU D 1 26  ? 146.895 -23.914 62.307  1.000 34.270  ? 43  LEU DDD N   1 
ATOM 6131  C CA  . LEU D 1 26  ? 145.732 -23.436 63.110  1.000 32.830  ? 43  LEU DDD CA  1 
ATOM 6132  C C   . LEU D 1 26  ? 144.514 -23.488 62.208  1.000 30.810  ? 43  LEU DDD C   1 
ATOM 6133  O O   . LEU D 1 26  ? 144.598 -23.040 61.082  1.000 32.590  ? 43  LEU DDD O   1 
ATOM 6134  C CB  . LEU D 1 26  ? 145.949 -22.012 63.619  1.000 31.190  ? 43  LEU DDD CB  1 
ATOM 6135  C CG  . LEU D 1 26  ? 146.565 -21.913 65.012  1.000 31.460  ? 43  LEU DDD CG  1 
ATOM 6136  C CD1 . LEU D 1 26  ? 148.013 -22.361 64.984  1.000 31.390  ? 43  LEU DDD CD1 1 
ATOM 6137  C CD2 . LEU D 1 26  ? 146.460 -20.492 65.554  1.000 32.260  ? 43  LEU DDD CD2 1 
ATOM 6138  N N   . THR D 1 27  ? 143.424 -24.044 62.698  1.000 30.200  ? 44  THR DDD N   1 
ATOM 6139  C CA  . THR D 1 27  ? 142.192 -24.165 61.901  1.000 31.410  ? 44  THR DDD CA  1 
ATOM 6140  C C   . THR D 1 27  ? 141.394 -22.888 62.109  1.000 30.520  ? 44  THR DDD C   1 
ATOM 6141  O O   . THR D 1 27  ? 141.618 -22.123 63.040  1.000 30.830  ? 44  THR DDD O   1 
ATOM 6142  C CB  . THR D 1 27  ? 141.447 -25.457 62.244  1.000 31.650  ? 44  THR DDD CB  1 
ATOM 6143  O OG1 . THR D 1 27  ? 140.716 -25.272 63.472  1.000 31.720  ? 44  THR DDD OG1 1 
ATOM 6144  C CG2 . THR D 1 27  ? 142.376 -26.650 62.345  1.000 30.430  ? 44  THR DDD CG2 1 
ATOM 6145  N N   . PRO D 1 28  ? 140.502 -22.573 61.166  1.000 31.300  ? 45  PRO DDD N   1 
ATOM 6146  C CA  . PRO D 1 28  ? 139.633 -21.411 61.322  1.000 35.810  ? 45  PRO DDD CA  1 
ATOM 6147  C C   . PRO D 1 28  ? 138.339 -21.703 62.090  1.000 35.740  ? 45  PRO DDD C   1 
ATOM 6148  O O   . PRO D 1 28  ? 137.655 -22.639 61.718  1.000 32.920  ? 45  PRO DDD O   1 
ATOM 6149  C CB  . PRO D 1 28  ? 139.340 -21.069 59.848  1.000 36.370  ? 45  PRO DDD CB  1 
ATOM 6150  C CG  . PRO D 1 28  ? 139.392 -22.396 59.119  1.000 32.650  ? 45  PRO DDD CG  1 
ATOM 6151  C CD  . PRO D 1 28  ? 140.399 -23.239 59.863  1.000 29.050  ? 45  PRO DDD CD  1 
ATOM 6152  N N   . GLU D 1 29  ? 137.987 -20.866 63.078  1.000 37.620  ? 46  GLU DDD N   1 
ATOM 6153  C CA  . GLU D 1 29  ? 136.634 -20.930 63.708  1.000 40.220  ? 46  GLU DDD CA  1 
ATOM 6154  C C   . GLU D 1 29  ? 135.783 -19.833 63.088  1.000 32.860  ? 46  GLU DDD C   1 
ATOM 6155  O O   . GLU D 1 29  ? 135.901 -18.675 63.516  1.000 33.430  ? 46  GLU DDD O   1 
ATOM 6156  C CB  . GLU D 1 29  ? 136.704 -20.845 65.237  1.000 50.300  ? 46  GLU DDD CB  1 
ATOM 6157  C CG  . GLU D 1 29  ? 137.659 -21.851 65.863  1.000 56.640  ? 46  GLU DDD CG  1 
ATOM 6158  C CD  . GLU D 1 29  ? 137.263 -23.307 65.674  1.000 59.700  ? 46  GLU DDD CD  1 
ATOM 6159  O OE1 . GLU D 1 29  ? 138.008 -24.183 66.142  1.000 58.400  ? 46  GLU DDD OE1 1 
ATOM 6160  O OE2 . GLU D 1 29  ? 136.211 -23.570 65.066  1.000 73.490  ? 46  GLU DDD OE2 1 
ATOM 6161  N N   . MET D 1 30  ? 135.008 -20.185 62.072  1.000 28.910  ? 47  MET DDD N   1 
ATOM 6162  C CA  . MET D 1 30  ? 134.208 -19.222 61.279  1.000 28.250  ? 47  MET DDD CA  1 
ATOM 6163  C C   . MET D 1 30  ? 132.764 -19.196 61.774  1.000 28.240  ? 47  MET DDD C   1 
ATOM 6164  O O   . MET D 1 30  ? 132.005 -18.412 61.216  1.000 25.110  ? 47  MET DDD O   1 
ATOM 6165  C CB  . MET D 1 30  ? 134.193 -19.597 59.800  1.000 29.990  ? 47  MET DDD CB  1 
ATOM 6166  C CG  . MET D 1 30  ? 135.510 -19.321 59.093  1.000 30.080  ? 47  MET DDD CG  1 
ATOM 6167  S SD  . MET D 1 30  ? 136.039 -17.594 59.228  1.000 27.040  ? 47  MET DDD SD  1 
ATOM 6168  C CE  . MET D 1 30  ? 137.505 -17.800 60.234  1.000 29.540  ? 47  MET DDD CE  1 
ATOM 6169  N N   . GLY D 1 31  ? 132.396 -20.021 62.763  1.000 30.380  ? 48  GLY DDD N   1 
ATOM 6170  C CA  . GLY D 1 31  ? 131.006 -20.070 63.309  1.000 29.860  ? 48  GLY DDD CA  1 
ATOM 6171  C C   . GLY D 1 31  ? 130.403 -21.462 63.300  1.000 30.600  ? 48  GLY DDD C   1 
ATOM 6172  O O   . GLY D 1 31  ? 129.522 -21.704 64.127  1.000 31.080  ? 48  GLY DDD O   1 
ATOM 6173  N N   . ASP D 1 32  ? 130.839 -22.302 62.352  1.000 36.100  ? 49  ASP DDD N   1 
ATOM 6174  C CA  . ASP D 1 32  ? 130.649 -23.780 62.264  1.000 36.250  ? 49  ASP DDD CA  1 
ATOM 6175  C C   . ASP D 1 32  ? 129.195 -24.099 62.570  1.000 33.530  ? 49  ASP DDD C   1 
ATOM 6176  O O   . ASP D 1 32  ? 128.892 -24.772 63.555  1.000 30.080  ? 49  ASP DDD O   1 
ATOM 6177  C CB  . ASP D 1 32  ? 131.629 -24.538 63.156  1.000 43.110  ? 49  ASP DDD CB  1 
ATOM 6178  C CG  . ASP D 1 32  ? 133.129 -24.474 62.768  1.000 53.560  ? 49  ASP DDD CG  1 
ATOM 6179  O OD1 . ASP D 1 32  ? 133.533 -23.639 61.899  1.000 54.910  ? 49  ASP DDD OD1 1 
ATOM 6180  O OD2 . ASP D 1 32  ? 133.890 -25.290 63.328  1.000 68.150  ? 49  ASP DDD OD2 1 
ATOM 6181  N N   . PRO D 1 33  ? 128.260 -23.631 61.709  1.000 36.880  ? 50  PRO DDD N   1 
ATOM 6182  C CA  . PRO D 1 33  ? 126.825 -23.796 61.920  1.000 40.340  ? 50  PRO DDD CA  1 
ATOM 6183  C C   . PRO D 1 33  ? 126.483 -25.207 62.407  1.000 45.480  ? 50  PRO DDD C   1 
ATOM 6184  O O   . PRO D 1 33  ? 126.117 -25.361 63.538  1.000 63.220  ? 50  PRO DDD O   1 
ATOM 6185  C CB  . PRO D 1 33  ? 126.180 -23.551 60.537  1.000 37.890  ? 50  PRO DDD CB  1 
ATOM 6186  C CG  . PRO D 1 33  ? 127.170 -22.671 59.827  1.000 39.260  ? 50  PRO DDD CG  1 
ATOM 6187  C CD  . PRO D 1 33  ? 128.533 -22.999 60.412  1.000 39.090  ? 50  PRO DDD CD  1 
ATOM 6188  N N   . ASP D 1 34  ? 126.700 -26.206 61.556  1.000 42.710  ? 51  ASP DDD N   1 
ATOM 6189  C CA  . ASP D 1 34  ? 126.141 -27.570 61.712  1.000 39.360  ? 51  ASP DDD CA  1 
ATOM 6190  C C   . ASP D 1 34  ? 127.261 -28.576 61.431  1.000 36.550  ? 51  ASP DDD C   1 
ATOM 6191  O O   . ASP D 1 34  ? 128.397 -28.115 61.159  1.000 38.650  ? 51  ASP DDD O   1 
ATOM 6192  C CB  . ASP D 1 34  ? 124.886 -27.682 60.842  1.000 42.030  ? 51  ASP DDD CB  1 
ATOM 6193  C CG  . ASP D 1 34  ? 125.095 -28.136 59.401  1.000 41.400  ? 51  ASP DDD CG  1 
ATOM 6194  O OD1 . ASP D 1 34  ? 126.279 -28.326 58.978  1.000 41.660  ? 51  ASP DDD OD1 1 
ATOM 6195  O OD2 . ASP D 1 34  ? 124.060 -28.313 58.714  1.000 39.310  ? 51  ASP DDD OD2 1 
ATOM 6196  N N   . GLU D 1 35  ? 126.947 -29.880 61.466  1.000 32.440  ? 52  GLU DDD N   1 
ATOM 6197  C CA  . GLU D 1 35  ? 127.963 -30.974 61.472  1.000 31.650  ? 52  GLU DDD CA  1 
ATOM 6198  C C   . GLU D 1 35  ? 128.756 -31.019 60.169  1.000 28.150  ? 52  GLU DDD C   1 
ATOM 6199  O O   . GLU D 1 35  ? 129.796 -31.676 60.149  1.000 26.090  ? 52  GLU DDD O   1 
ATOM 6200  C CB  . GLU D 1 35  ? 127.323 -32.328 61.786  1.000 34.730  ? 52  GLU DDD CB  1 
ATOM 6201  C CG  . GLU D 1 35  ? 126.226 -32.763 60.849  1.000 35.600  ? 52  GLU DDD CG  1 
ATOM 6202  C CD  . GLU D 1 35  ? 125.610 -34.107 61.216  1.000 35.340  ? 52  GLU DDD CD  1 
ATOM 6203  O OE1 . GLU D 1 35  ? 126.325 -34.962 61.745  1.000 31.030  ? 52  GLU DDD OE1 1 
ATOM 6204  O OE2 . GLU D 1 35  ? 124.413 -34.292 60.941  1.000 40.730  ? 52  GLU DDD OE2 1 
ATOM 6205  N N   . HIS D 1 36  ? 128.316 -30.295 59.149  1.000 30.560  ? 53  HIS DDD N   1 
ATOM 6206  C CA  . HIS D 1 36  ? 128.749 -30.462 57.735  1.000 32.170  ? 53  HIS DDD CA  1 
ATOM 6207  C C   . HIS D 1 36  ? 129.489 -29.222 57.192  1.000 33.750  ? 53  HIS DDD C   1 
ATOM 6208  O O   . HIS D 1 36  ? 129.893 -29.271 55.990  1.000 40.390  ? 53  HIS DDD O   1 
ATOM 6209  C CB  . HIS D 1 36  ? 127.503 -30.710 56.891  1.000 31.780  ? 53  HIS DDD CB  1 
ATOM 6210  C CG  . HIS D 1 36  ? 126.807 -32.009 57.121  1.000 31.280  ? 53  HIS DDD CG  1 
ATOM 6211  N ND1 . HIS D 1 36  ? 127.397 -33.193 56.806  1.000 30.100  ? 53  HIS DDD ND1 1 
ATOM 6212  C CD2 . HIS D 1 36  ? 125.543 -32.302 57.531  1.000 32.190  ? 53  HIS DDD CD2 1 
ATOM 6213  C CE1 . HIS D 1 36  ? 126.529 -34.167 56.997  1.000 33.960  ? 53  HIS DDD CE1 1 
ATOM 6214  N NE2 . HIS D 1 36  ? 125.372 -33.642 57.440  1.000 31.420  ? 53  HIS DDD NE2 1 
ATOM 6215  N N   . LEU D 1 37  ? 129.620 -28.143 57.981  1.000 32.460  ? 54  LEU DDD N   1 
ATOM 6216  C CA  . LEU D 1 37  ? 129.984 -26.788 57.454  1.000 30.040  ? 54  LEU DDD CA  1 
ATOM 6217  C C   . LEU D 1 37  ? 131.148 -26.167 58.228  1.000 27.390  ? 54  LEU DDD C   1 
ATOM 6218  O O   . LEU D 1 37  ? 131.226 -24.934 58.311  1.000 24.650  ? 54  LEU DDD O   1 
ATOM 6219  C CB  . LEU D 1 37  ? 128.745 -25.891 57.523  1.000 29.470  ? 54  LEU DDD CB  1 
ATOM 6220  C CG  . LEU D 1 37  ? 127.640 -26.242 56.540  1.000 29.990  ? 54  LEU DDD CG  1 
ATOM 6221  C CD1 . LEU D 1 37  ? 126.462 -25.321 56.760  1.000 30.930  ? 54  LEU DDD CD1 1 
ATOM 6222  C CD2 . LEU D 1 37  ? 128.111 -26.145 55.104  1.000 31.050  ? 54  LEU DDD CD2 1 
ATOM 6223  N N   . ARG D 1 38  ? 132.038 -26.998 58.745  1.000 26.640  ? 55  ARG DDD N   1 
ATOM 6224  C CA  . ARG D 1 38  ? 133.276 -26.551 59.420  1.000 26.180  ? 55  ARG DDD CA  1 
ATOM 6225  C C   . ARG D 1 38  ? 134.050 -25.653 58.456  1.000 24.230  ? 55  ARG DDD C   1 
ATOM 6226  O O   . ARG D 1 38  ? 134.293 -26.081 57.321  1.000 26.330  ? 55  ARG DDD O   1 
ATOM 6227  C CB  . ARG D 1 38  ? 134.071 -27.787 59.823  1.000 30.070  ? 55  ARG DDD CB  1 
ATOM 6228  C CG  . ARG D 1 38  ? 135.366 -27.504 60.554  1.000 34.510  ? 55  ARG DDD CG  1 
ATOM 6229  C CD  . ARG D 1 38  ? 135.288 -27.913 62.003  1.000 39.760  ? 55  ARG DDD CD  1 
ATOM 6230  N NE  . ARG D 1 38  ? 136.652 -27.860 62.500  1.000 45.820  ? 55  ARG DDD NE  1 
ATOM 6231  C CZ  . ARG D 1 38  ? 137.306 -26.743 62.834  1.000 55.670  ? 55  ARG DDD CZ  1 
ATOM 6232  N NH1 . ARG D 1 38  ? 136.725 -25.550 62.747  1.000 54.380  ? 55  ARG DDD NH1 1 
ATOM 6233  N NH2 . ARG D 1 38  ? 138.548 -26.836 63.263  1.000 61.760  ? 55  ARG DDD NH2 1 
ATOM 6234  N N   . GLY D 1 39  ? 134.384 -24.436 58.872  1.000 23.380  ? 56  GLY DDD N   1 
ATOM 6235  C CA  . GLY D 1 39  ? 135.117 -23.472 58.031  1.000 22.780  ? 56  GLY DDD CA  1 
ATOM 6236  C C   . GLY D 1 39  ? 134.184 -22.491 57.356  1.000 21.760  ? 56  GLY DDD C   1 
ATOM 6237  O O   . GLY D 1 39  ? 134.666 -21.596 56.652  1.000 21.980  ? 56  GLY DDD O   1 
ATOM 6238  N N   . PHE D 1 40  ? 132.889 -22.631 57.576  1.000 22.710  ? 57  PHE DDD N   1 
ATOM 6239  C CA  . PHE D 1 40  ? 131.875 -21.635 57.145  1.000 24.610  ? 57  PHE DDD CA  1 
ATOM 6240  C C   . PHE D 1 40  ? 131.270 -20.988 58.385  1.000 22.010  ? 57  PHE DDD C   1 
ATOM 6241  O O   . PHE D 1 40  ? 131.441 -21.506 59.479  1.000 19.450  ? 57  PHE DDD O   1 
ATOM 6242  C CB  . PHE D 1 40  ? 130.776 -22.276 56.286  1.000 27.400  ? 57  PHE DDD CB  1 
ATOM 6243  C CG  . PHE D 1 40  ? 131.277 -22.887 54.999  1.000 28.810  ? 57  PHE DDD CG  1 
ATOM 6244  C CD1 . PHE D 1 40  ? 131.975 -24.089 55.007  1.000 28.960  ? 57  PHE DDD CD1 1 
ATOM 6245  C CD2 . PHE D 1 40  ? 131.050 -22.261 53.778  1.000 29.520  ? 57  PHE DDD CD2 1 
ATOM 6246  C CE1 . PHE D 1 40  ? 132.417 -24.647 53.813  1.000 28.150  ? 57  PHE DDD CE1 1 
ATOM 6247  C CE2 . PHE D 1 40  ? 131.490 -22.829 52.592  1.000 27.160  ? 57  PHE DDD CE2 1 
ATOM 6248  C CZ  . PHE D 1 40  ? 132.171 -24.020 52.612  1.000 26.680  ? 57  PHE DDD CZ  1 
ATOM 6249  N N   . SER D 1 41  ? 130.611 -19.859 58.189  1.000 21.990  ? 58  SER DDD N   1 
ATOM 6250  C CA  . SER D 1 41  ? 129.642 -19.278 59.144  1.000 22.310  ? 58  SER DDD CA  1 
ATOM 6251  C C   . SER D 1 41  ? 128.251 -19.687 58.685  1.000 22.610  ? 58  SER DDD C   1 
ATOM 6252  O O   . SER D 1 41  ? 128.132 -20.277 57.591  1.000 20.820  ? 58  SER DDD O   1 
ATOM 6253  C CB  . SER D 1 41  ? 129.733 -17.791 59.229  1.000 21.690  ? 58  SER DDD CB  1 
ATOM 6254  O OG  . SER D 1 41  ? 129.141 -17.187 58.093  1.000 21.650  ? 58  SER DDD OG  1 
ATOM 6255  N N   . LYS D 1 42  ? 127.263 -19.386 59.518  1.000 24.000  ? 59  LYS DDD N   1 
ATOM 6256  C CA  . LYS D 1 42  ? 125.841 -19.563 59.181  1.000 26.960  ? 59  LYS DDD CA  1 
ATOM 6257  C C   . LYS D 1 42  ? 125.519 -18.441 58.212  1.000 27.990  ? 59  LYS DDD C   1 
ATOM 6258  O O   . LYS D 1 42  ? 126.139 -17.360 58.323  1.000 28.510  ? 59  LYS DDD O   1 
ATOM 6259  C CB  . LYS D 1 42  ? 124.954 -19.521 60.431  1.000 29.850  ? 59  LYS DDD CB  1 
ATOM 6260  C CG  . LYS D 1 42  ? 123.464 -19.718 60.146  1.000 33.760  ? 59  LYS DDD CG  1 
ATOM 6261  C CD  . LYS D 1 42  ? 122.593 -20.180 61.326  1.000 37.440  ? 59  LYS DDD CD  1 
ATOM 6262  C CE  . LYS D 1 42  ? 121.964 -19.064 62.155  1.000 41.300  ? 59  LYS DDD CE  1 
ATOM 6263  N NZ  . LYS D 1 42  ? 120.748 -19.532 62.867  1.000 39.970  ? 59  LYS DDD NZ  1 
ATOM 6264  N N   . SER D 1 43  ? 124.599 -18.692 57.292  1.000 28.910  ? 60  SER DDD N   1 
ATOM 6265  C CA  . SER D 1 43  ? 124.131 -17.652 56.344  1.000 28.510  ? 60  SER DDD CA  1 
ATOM 6266  C C   . SER D 1 43  ? 123.729 -16.416 57.149  1.000 24.690  ? 60  SER DDD C   1 
ATOM 6267  O O   . SER D 1 43  ? 122.901 -16.539 58.087  1.000 21.300  ? 60  SER DDD O   1 
ATOM 6268  C CB  . SER D 1 43  ? 123.034 -18.165 55.458  1.000 32.740  ? 60  SER DDD CB  1 
ATOM 6269  O OG  . SER D 1 43  ? 123.570 -19.031 54.461  1.000 34.920  ? 60  SER DDD OG  1 
ATOM 6270  N N   . ILE D 1 44  ? 124.353 -15.292 56.798  1.000 23.790  ? 61  ILE DDD N   1 
ATOM 6271  C CA  . ILE D 1 44  ? 124.327 -14.003 57.549  1.000 24.470  ? 61  ILE DDD CA  1 
ATOM 6272  C C   . ILE D 1 44  ? 122.928 -13.401 57.480  1.000 25.050  ? 61  ILE DDD C   1 
ATOM 6273  O O   . ILE D 1 44  ? 122.346 -13.411 56.407  1.000 26.980  ? 61  ILE DDD O   1 
ATOM 6274  C CB  . ILE D 1 44  ? 125.374 -13.056 56.958  1.000 22.220  ? 61  ILE DDD CB  1 
ATOM 6275  C CG1 . ILE D 1 44  ? 126.770 -13.645 57.190  1.000 23.490  ? 61  ILE DDD CG1 1 
ATOM 6276  C CG2 . ILE D 1 44  ? 125.218 -11.676 57.538  1.000 20.370  ? 61  ILE DDD CG2 1 
ATOM 6277  C CD1 . ILE D 1 44  ? 127.928 -12.792 56.700  1.000 24.500  ? 61  ILE DDD CD1 1 
ATOM 6278  N N   . SER D 1 45  ? 122.402 -12.923 58.595  1.000 24.190  ? 62  SER DDD N   1 
ATOM 6279  C CA  . SER D 1 45  ? 121.100 -12.213 58.645  1.000 23.320  ? 62  SER DDD CA  1 
ATOM 6280  C C   . SER D 1 45  ? 121.383 -10.800 59.136  1.000 21.530  ? 62  SER DDD C   1 
ATOM 6281  O O   . SER D 1 45  ? 122.470 -10.597 59.694  1.000 20.450  ? 62  SER DDD O   1 
ATOM 6282  C CB  . SER D 1 45  ? 120.079 -12.922 59.533  1.000 25.450  ? 62  SER DDD CB  1 
ATOM 6283  O OG  . SER D 1 45  ? 120.436 -14.283 59.793  1.000 27.610  ? 62  SER DDD OG  1 
ATOM 6284  N N   . ILE D 1 46  ? 120.428 -9.896  58.963  1.000 21.720  ? 63  ILE DDD N   1 
ATOM 6285  C CA  . ILE D 1 46  ? 120.583 -8.456  59.290  1.000 24.740  ? 63  ILE DDD CA  1 
ATOM 6286  C C   . ILE D 1 46  ? 119.523 -8.033  60.309  1.000 26.770  ? 63  ILE DDD C   1 
ATOM 6287  O O   . ILE D 1 46  ? 118.340 -8.281  60.101  1.000 28.880  ? 63  ILE DDD O   1 
ATOM 6288  C CB  . ILE D 1 46  ? 120.482 -7.622  58.007  1.000 26.790  ? 63  ILE DDD CB  1 
ATOM 6289  C CG1 . ILE D 1 46  ? 121.597 -7.937  57.016  1.000 29.530  ? 63  ILE DDD CG1 1 
ATOM 6290  C CG2 . ILE D 1 46  ? 120.476 -6.159  58.357  1.000 28.850  ? 63  ILE DDD CG2 1 
ATOM 6291  C CD1 . ILE D 1 46  ? 121.367 -7.332  55.636  1.000 31.120  ? 63  ILE DDD CD1 1 
ATOM 6292  N N   . SER D 1 47  ? 119.922 -7.325  61.353  1.000 31.040  ? 64  SER DDD N   1 
ATOM 6293  C CA  . SER D 1 47  ? 119.003 -6.907  62.436  1.000 36.610  ? 64  SER DDD CA  1 
ATOM 6294  C C   . SER D 1 47  ? 117.806 -6.135  61.873  1.000 36.540  ? 64  SER DDD C   1 
ATOM 6295  O O   . SER D 1 47  ? 117.926 -5.452  60.849  1.000 30.100  ? 64  SER DDD O   1 
ATOM 6296  C CB  . SER D 1 47  ? 119.709 -6.140  63.493  1.000 43.720  ? 64  SER DDD CB  1 
ATOM 6297  O OG  . SER D 1 47  ? 120.558 -5.143  62.939  1.000 50.430  ? 64  SER DDD OG  1 
ATOM 6298  N N   . ASP D 1 48  ? 116.670 -6.309  62.546  1.000 44.240  ? 65  ASP DDD N   1 
ATOM 6299  C CA  . ASP D 1 48  ? 115.380 -5.619  62.276  1.000 47.790  ? 65  ASP DDD CA  1 
ATOM 6300  C C   . ASP D 1 48  ? 115.609 -4.111  62.454  1.000 43.810  ? 65  ASP DDD C   1 
ATOM 6301  O O   . ASP D 1 48  ? 114.930 -3.334  61.772  1.000 38.890  ? 65  ASP DDD O   1 
ATOM 6302  C CB  . ASP D 1 48  ? 114.229 -6.216  63.123  1.000 49.780  ? 65  ASP DDD CB  1 
ATOM 6303  C CG  . ASP D 1 48  ? 114.424 -6.200  64.642  1.000 55.740  ? 65  ASP DDD CG  1 
ATOM 6304  O OD1 . ASP D 1 48  ? 115.373 -6.882  65.141  1.000 49.680  ? 65  ASP DDD OD1 1 
ATOM 6305  O OD2 . ASP D 1 48  ? 113.637 -5.495  65.341  1.000 66.060  ? 65  ASP DDD OD2 1 
ATOM 6306  N N   . THR D 1 49  ? 116.528 -3.711  63.334  1.000 41.870  ? 66  THR DDD N   1 
ATOM 6307  C CA  . THR D 1 49  ? 116.797 -2.290  63.710  1.000 38.560  ? 66  THR DDD CA  1 
ATOM 6308  C C   . THR D 1 49  ? 118.257 -2.132  64.132  1.000 35.030  ? 66  THR DDD C   1 
ATOM 6309  O O   . THR D 1 49  ? 118.875 -3.120  64.553  1.000 32.640  ? 66  THR DDD O   1 
ATOM 6310  C CB  . THR D 1 49  ? 115.939 -1.818  64.893  1.000 36.840  ? 66  THR DDD CB  1 
ATOM 6311  O OG1 . THR D 1 49  ? 116.366 -2.549  66.043  1.000 34.630  ? 66  THR DDD OG1 1 
ATOM 6312  C CG2 . THR D 1 49  ? 114.453 -2.039  64.717  1.000 34.740  ? 66  THR DDD CG2 1 
ATOM 6313  N N   . PHE D 1 50  ? 118.777 -0.911  64.092  1.000 33.410  ? 67  PHE DDD N   1 
ATOM 6314  C CA  . PHE D 1 50  ? 120.208 -0.657  64.398  1.000 34.350  ? 67  PHE DDD CA  1 
ATOM 6315  C C   . PHE D 1 50  ? 120.465 -1.035  65.858  1.000 38.760  ? 67  PHE DDD C   1 
ATOM 6316  O O   . PHE D 1 50  ? 121.596 -1.427  66.207  1.000 38.070  ? 67  PHE DDD O   1 
ATOM 6317  C CB  . PHE D 1 50  ? 120.567 0.810   64.158  1.000 31.910  ? 67  PHE DDD CB  1 
ATOM 6318  C CG  . PHE D 1 50  ? 122.039 1.116   64.258  1.000 28.050  ? 67  PHE DDD CG  1 
ATOM 6319  C CD1 . PHE D 1 50  ? 122.911 0.673   63.286  1.000 28.090  ? 67  PHE DDD CD1 1 
ATOM 6320  C CD2 . PHE D 1 50  ? 122.540 1.852   65.306  1.000 25.250  ? 67  PHE DDD CD2 1 
ATOM 6321  C CE1 . PHE D 1 50  ? 124.257 0.956   63.371  1.000 27.740  ? 67  PHE DDD CE1 1 
ATOM 6322  C CE2 . PHE D 1 50  ? 123.886 2.134   65.385  1.000 26.050  ? 67  PHE DDD CE2 1 
ATOM 6323  C CZ  . PHE D 1 50  ? 124.744 1.690   64.421  1.000 26.940  ? 67  PHE DDD CZ  1 
ATOM 6324  N N   . GLU D 1 51  ? 119.420 -0.867  66.674  1.000 40.950  ? 68  GLU DDD N   1 
ATOM 6325  C CA  . GLU D 1 51  ? 119.459 -0.933  68.151  1.000 36.570  ? 68  GLU DDD CA  1 
ATOM 6326  C C   . GLU D 1 51  ? 119.461 -2.399  68.567  1.000 34.040  ? 68  GLU DDD C   1 
ATOM 6327  O O   . GLU D 1 51  ? 120.041 -2.681  69.598  1.000 40.050  ? 68  GLU DDD O   1 
ATOM 6328  C CB  . GLU D 1 51  ? 118.265 -0.166  68.723  1.000 36.110  ? 68  GLU DDD CB  1 
ATOM 6329  C CG  . GLU D 1 51  ? 118.342 1.323   68.476  1.000 36.780  ? 68  GLU DDD CG  1 
ATOM 6330  C CD  . GLU D 1 51  ? 117.646 1.906   67.255  1.000 41.270  ? 68  GLU DDD CD  1 
ATOM 6331  O OE1 . GLU D 1 51  ? 117.335 3.087   67.325  1.000 49.440  ? 68  GLU DDD OE1 1 
ATOM 6332  O OE2 . GLU D 1 51  ? 117.454 1.208   66.221  1.000 44.940  ? 68  GLU DDD OE2 1 
ATOM 6333  N N   . SER D 1 52  ? 118.867 -3.284  67.764  1.000 28.740  ? 69  SER DDD N   1 
ATOM 6334  C CA  . SER D 1 52  ? 118.599 -4.698  68.121  1.000 27.560  ? 69  SER DDD CA  1 
ATOM 6335  C C   . SER D 1 52  ? 119.614 -5.646  67.477  1.000 27.400  ? 69  SER DDD C   1 
ATOM 6336  O O   . SER D 1 52  ? 119.355 -6.854  67.432  1.000 26.970  ? 69  SER DDD O   1 
ATOM 6337  C CB  . SER D 1 52  ? 117.183 -5.073  67.736  1.000 26.850  ? 69  SER DDD CB  1 
ATOM 6338  O OG  . SER D 1 52  ? 116.972 -5.011  66.336  1.000 25.370  ? 69  SER DDD OG  1 
ATOM 6339  N N   . ASP D 1 53  ? 120.719 -5.138  66.945  1.000 28.620  ? 70  ASP DDD N   1 
ATOM 6340  C CA  . ASP D 1 53  ? 121.811 -5.984  66.394  1.000 28.830  ? 70  ASP DDD CA  1 
ATOM 6341  C C   . ASP D 1 53  ? 122.166 -7.015  67.461  1.000 28.510  ? 70  ASP DDD C   1 
ATOM 6342  O O   . ASP D 1 53  ? 122.472 -6.593  68.596  1.000 30.950  ? 70  ASP DDD O   1 
ATOM 6343  C CB  . ASP D 1 53  ? 123.061 -5.169  66.062  1.000 28.620  ? 70  ASP DDD CB  1 
ATOM 6344  C CG  . ASP D 1 53  ? 124.090 -5.912  65.251  1.000 28.090  ? 70  ASP DDD CG  1 
ATOM 6345  O OD1 . ASP D 1 53  ? 123.683 -6.553  64.254  1.000 30.480  ? 70  ASP DDD OD1 1 
ATOM 6346  O OD2 . ASP D 1 53  ? 125.263 -5.802  65.590  1.000 27.120  ? 70  ASP DDD OD2 1 
ATOM 6347  N N   . SER D 1 54  ? 122.048 -8.305  67.146  1.000 28.910  ? 71  SER DDD N   1 
ATOM 6348  C CA  . SER D 1 54  ? 122.447 -9.397  68.068  1.000 29.790  ? 71  SER DDD CA  1 
ATOM 6349  C C   . SER D 1 54  ? 122.753 -10.655 67.279  1.000 28.890  ? 71  SER DDD C   1 
ATOM 6350  O O   . SER D 1 54  ? 121.978 -11.601 67.279  1.000 29.410  ? 71  SER DDD O   1 
ATOM 6351  C CB  . SER D 1 54  ? 121.435 -9.635  69.162  1.000 30.700  ? 71  SER DDD CB  1 
ATOM 6352  O OG  . SER D 1 54  ? 120.128 -9.673  68.653  1.000 35.010  ? 71  SER DDD OG  1 
ATOM 6353  N N   . PRO D 1 55  ? 123.953 -10.738 66.679  1.000 29.190  ? 72  PRO DDD N   1 
ATOM 6354  C CA  . PRO D 1 55  ? 124.342 -11.901 65.896  1.000 29.980  ? 72  PRO DDD CA  1 
ATOM 6355  C C   . PRO D 1 55  ? 124.383 -13.195 66.718  1.000 29.700  ? 72  PRO DDD C   1 
ATOM 6356  O O   . PRO D 1 55  ? 124.914 -13.138 67.810  1.000 27.050  ? 72  PRO DDD O   1 
ATOM 6357  C CB  . PRO D 1 55  ? 125.770 -11.538 65.484  1.000 30.930  ? 72  PRO DDD CB  1 
ATOM 6358  C CG  . PRO D 1 55  ? 126.249 -10.673 66.614  1.000 31.360  ? 72  PRO DDD CG  1 
ATOM 6359  C CD  . PRO D 1 55  ? 125.053 -9.779  66.831  1.000 30.940  ? 72  PRO DDD CD  1 
ATOM 6360  N N   . ASN D 1 56  ? 123.850 -14.298 66.166  1.000 30.630  ? 73  ASN DDD N   1 
ATOM 6361  C CA  . ASN D 1 56  ? 123.942 -15.656 66.763  1.000 31.670  ? 73  ASN DDD CA  1 
ATOM 6362  C C   . ASN D 1 56  ? 125.409 -16.068 66.749  1.000 30.210  ? 73  ASN DDD C   1 
ATOM 6363  O O   . ASN D 1 56  ? 126.150 -15.587 65.911  1.000 28.440  ? 73  ASN DDD O   1 
ATOM 6364  C CB  . ASN D 1 56  ? 123.134 -16.699 65.999  1.000 37.750  ? 73  ASN DDD CB  1 
ATOM 6365  C CG  . ASN D 1 56  ? 121.635 -16.469 66.014  1.000 41.200  ? 73  ASN DDD CG  1 
ATOM 6366  O OD1 . ASN D 1 56  ? 120.912 -17.146 65.282  1.000 48.130  ? 73  ASN DDD OD1 1 
ATOM 6367  N ND2 . ASN D 1 56  ? 121.157 -15.541 66.830  1.000 38.150  ? 73  ASN DDD ND2 1 
ATOM 6368  N N   . ARG D 1 57  ? 125.813 -16.955 67.644  1.000 32.990  ? 74  ARG DDD N   1 
ATOM 6369  C CA  . ARG D 1 57  ? 127.241 -17.336 67.831  1.000 34.760  ? 74  ARG DDD CA  1 
ATOM 6370  C C   . ARG D 1 57  ? 127.809 -17.991 66.561  1.000 35.550  ? 74  ARG DDD C   1 
ATOM 6371  O O   . ARG D 1 57  ? 129.042 -17.875 66.323  1.000 33.810  ? 74  ARG DDD O   1 
ATOM 6372  C CB  . ARG D 1 57  ? 127.362 -18.279 69.031  1.000 34.740  ? 74  ARG DDD CB  1 
ATOM 6373  C CG  . ARG D 1 57  ? 128.793 -18.665 69.357  1.000 35.480  ? 74  ARG DDD CG  1 
ATOM 6374  C CD  . ARG D 1 57  ? 128.860 -19.659 70.497  1.000 35.010  ? 74  ARG DDD CD  1 
ATOM 6375  N NE  . ARG D 1 57  ? 130.253 -19.953 70.804  1.000 35.530  ? 74  ARG DDD NE  1 
ATOM 6376  C CZ  . ARG D 1 57  ? 130.667 -21.025 71.452  1.000 32.830  ? 74  ARG DDD CZ  1 
ATOM 6377  N NH1 . ARG D 1 57  ? 129.804 -21.921 71.879  1.000 30.590  ? 74  ARG DDD NH1 1 
ATOM 6378  N NH2 . ARG D 1 57  ? 131.950 -21.211 71.660  1.000 36.730  ? 74  ARG DDD NH2 1 
ATOM 6379  N N   . ASP D 1 58  ? 126.959 -18.669 65.786  1.000 35.860  ? 75  ASP DDD N   1 
ATOM 6380  C CA  . ASP D 1 58  ? 127.366 -19.421 64.573  1.000 35.020  ? 75  ASP DDD CA  1 
ATOM 6381  C C   . ASP D 1 58  ? 127.426 -18.487 63.353  1.000 34.710  ? 75  ASP DDD C   1 
ATOM 6382  O O   . ASP D 1 58  ? 127.728 -18.985 62.245  1.000 39.430  ? 75  ASP DDD O   1 
ATOM 6383  C CB  . ASP D 1 58  ? 126.460 -20.632 64.345  1.000 35.880  ? 75  ASP DDD CB  1 
ATOM 6384  C CG  . ASP D 1 58  ? 124.960 -20.346 64.410  1.000 38.410  ? 75  ASP DDD CG  1 
ATOM 6385  O OD1 . ASP D 1 58  ? 124.574 -19.158 64.451  1.000 38.850  ? 75  ASP DDD OD1 1 
ATOM 6386  O OD2 . ASP D 1 58  ? 124.188 -21.325 64.460  1.000 42.190  ? 75  ASP DDD OD2 1 
ATOM 6387  N N   . MET D 1 59  ? 127.211 -17.184 63.542  1.000 29.430  ? 76  MET DDD N   1 
ATOM 6388  C CA  . MET D 1 59  ? 127.378 -16.173 62.474  1.000 26.690  ? 76  MET DDD CA  1 
ATOM 6389  C C   . MET D 1 59  ? 128.662 -15.351 62.696  1.000 26.380  ? 76  MET DDD C   1 
ATOM 6390  O O   . MET D 1 59  ? 128.911 -14.397 61.883  1.000 25.960  ? 76  MET DDD O   1 
ATOM 6391  C CB  . MET D 1 59  ? 126.165 -15.248 62.464  1.000 24.600  ? 76  MET DDD CB  1 
ATOM 6392  C CG  . MET D 1 59  ? 125.961 -14.604 61.132  1.000 24.240  ? 76  MET DDD CG  1 
ATOM 6393  S SD  . MET D 1 59  ? 124.730 -13.314 61.210  1.000 25.670  ? 76  MET DDD SD  1 
ATOM 6394  C CE  . MET D 1 59  ? 125.701 -11.984 61.897  1.000 25.960  ? 76  MET DDD CE  1 
ATOM 6395  N N   . LEU D 1 60  ? 129.420 -15.672 63.745  1.000 23.330  ? 77  LEU DDD N   1 
ATOM 6396  C CA  . LEU D 1 60  ? 130.560 -14.843 64.200  1.000 24.690  ? 77  LEU DDD CA  1 
ATOM 6397  C C   . LEU D 1 60  ? 131.868 -15.610 64.105  1.000 23.780  ? 77  LEU DDD C   1 
ATOM 6398  O O   . LEU D 1 60  ? 132.184 -16.441 64.949  1.000 24.100  ? 77  LEU DDD O   1 
ATOM 6399  C CB  . LEU D 1 60  ? 130.330 -14.391 65.642  1.000 26.160  ? 77  LEU DDD CB  1 
ATOM 6400  C CG  . LEU D 1 60  ? 129.253 -13.335 65.848  1.000 27.900  ? 77  LEU DDD CG  1 
ATOM 6401  C CD1 . LEU D 1 60  ? 129.163 -12.979 67.322  1.000 29.290  ? 77  LEU DDD CD1 1 
ATOM 6402  C CD2 . LEU D 1 60  ? 129.517 -12.075 65.016  1.000 28.780  ? 77  LEU DDD CD2 1 
ATOM 6403  N N   . PRO D 1 61  ? 132.680 -15.338 63.071  1.000 23.800  ? 78  PRO DDD N   1 
ATOM 6404  C CA  . PRO D 1 61  ? 134.080 -15.748 63.087  1.000 24.760  ? 78  PRO DDD CA  1 
ATOM 6405  C C   . PRO D 1 61  ? 134.785 -15.292 64.363  1.000 24.970  ? 78  PRO DDD C   1 
ATOM 6406  O O   . PRO D 1 61  ? 134.436 -14.224 64.848  1.000 27.100  ? 78  PRO DDD O   1 
ATOM 6407  C CB  . PRO D 1 61  ? 134.698 -15.028 61.877  1.000 25.210  ? 78  PRO DDD CB  1 
ATOM 6408  C CG  . PRO D 1 61  ? 133.513 -14.784 60.927  1.000 25.160  ? 78  PRO DDD CG  1 
ATOM 6409  C CD  . PRO D 1 61  ? 132.283 -14.694 61.808  1.000 24.550  ? 78  PRO DDD CD  1 
ATOM 6410  N N   . CYS D 1 62  ? 135.770 -16.075 64.815  1.000 25.220  ? 79  CYS DDD N   1 
ATOM 6411  C CA  . CYS D 1 62  ? 136.574 -15.824 66.036  1.000 25.560  ? 79  CYS DDD CA  1 
ATOM 6412  C C   . CYS D 1 62  ? 138.068 -16.018 65.771  1.000 24.610  ? 79  CYS DDD C   1 
ATOM 6413  O O   . CYS D 1 62  ? 138.455 -16.882 64.938  1.000 25.550  ? 79  CYS DDD O   1 
ATOM 6414  C CB  . CYS D 1 62  ? 136.201 -16.793 67.148  1.000 27.600  ? 79  CYS DDD CB  1 
ATOM 6415  S SG  . CYS D 1 62  ? 134.463 -16.675 67.636  1.000 32.820  ? 79  CYS DDD SG  1 
ATOM 6416  N N   . TYR D 1 63  ? 138.882 -15.290 66.530  1.000 23.910  ? 80  TYR DDD N   1 
ATOM 6417  C CA  . TYR D 1 63  ? 140.344 -15.493 66.610  1.000 23.890  ? 80  TYR DDD CA  1 
ATOM 6418  C C   . TYR D 1 63  ? 140.618 -16.948 66.994  1.000 27.940  ? 80  TYR DDD C   1 
ATOM 6419  O O   . TYR D 1 63  ? 139.914 -17.520 67.874  1.000 34.400  ? 80  TYR DDD O   1 
ATOM 6420  C CB  . TYR D 1 63  ? 140.983 -14.542 67.629  1.000 22.200  ? 80  TYR DDD CB  1 
ATOM 6421  C CG  . TYR D 1 63  ? 141.074 -13.092 67.225  1.000 20.180  ? 80  TYR DDD CG  1 
ATOM 6422  C CD1 . TYR D 1 63  ? 140.011 -12.239 67.412  1.000 19.640  ? 80  TYR DDD CD1 1 
ATOM 6423  C CD2 . TYR D 1 63  ? 142.244 -12.573 66.686  1.000 19.620  ? 80  TYR DDD CD2 1 
ATOM 6424  C CE1 . TYR D 1 63  ? 140.090 -10.914 67.034  1.000 20.960  ? 80  TYR DDD CE1 1 
ATOM 6425  C CE2 . TYR D 1 63  ? 142.348 -11.251 66.310  1.000 20.390  ? 80  TYR DDD CE2 1 
ATOM 6426  C CZ  . TYR D 1 63  ? 141.267 -10.414 66.497  1.000 21.960  ? 80  TYR DDD CZ  1 
ATOM 6427  O OH  . TYR D 1 63  ? 141.357 -9.107  66.109  1.000 23.280  ? 80  TYR DDD OH  1 
ATOM 6428  N N   . SER D 1 64  ? 141.603 -17.543 66.330  1.000 30.720  ? 81  SER DDD N   1 
ATOM 6429  C CA  . SER D 1 64  ? 142.149 -18.893 66.628  1.000 31.590  ? 81  SER DDD CA  1 
ATOM 6430  C C   . SER D 1 64  ? 143.444 -18.676 67.395  1.000 30.150  ? 81  SER DDD C   1 
ATOM 6431  O O   . SER D 1 64  ? 144.165 -17.723 67.049  1.000 34.150  ? 81  SER DDD O   1 
ATOM 6432  C CB  . SER D 1 64  ? 142.354 -19.713 65.352  1.000 36.570  ? 81  SER DDD CB  1 
ATOM 6433  O OG  . SER D 1 64  ? 141.252 -19.557 64.431  1.000 52.880  ? 81  SER DDD OG  1 
ATOM 6434  N N   . VAL D 1 65  ? 143.710 -19.482 68.423  1.000 30.420  ? 82  VAL DDD N   1 
ATOM 6435  C CA  . VAL D 1 65  ? 144.958 -19.419 69.257  1.000 28.100  ? 82  VAL DDD CA  1 
ATOM 6436  C C   . VAL D 1 65  ? 145.450 -20.830 69.550  1.000 24.930  ? 82  VAL DDD C   1 
ATOM 6437  O O   . VAL D 1 65  ? 144.611 -21.713 69.631  1.000 22.710  ? 82  VAL DDD O   1 
ATOM 6438  C CB  . VAL D 1 65  ? 144.728 -18.665 70.575  1.000 27.580  ? 82  VAL DDD CB  1 
ATOM 6439  C CG1 . VAL D 1 65  ? 143.544 -19.218 71.346  1.000 27.430  ? 82  VAL DDD CG1 1 
ATOM 6440  C CG2 . VAL D 1 65  ? 145.983 -18.641 71.427  1.000 27.230  ? 82  VAL DDD CG2 1 
ATOM 6441  N N   . ALA D 1 66  ? 146.756 -20.997 69.719  1.000 24.380  ? 83  ALA DDD N   1 
ATOM 6442  C CA  . ALA D 1 66  ? 147.415 -22.283 70.016  1.000 25.160  ? 83  ALA DDD CA  1 
ATOM 6443  C C   . ALA D 1 66  ? 148.601 -22.062 70.949  1.000 26.720  ? 83  ALA DDD C   1 
ATOM 6444  O O   . ALA D 1 66  ? 149.486 -21.325 70.549  1.000 25.300  ? 83  ALA DDD O   1 
ATOM 6445  C CB  . ALA D 1 66  ? 147.872 -22.894 68.733  1.000 24.650  ? 83  ALA DDD CB  1 
ATOM 6446  N N   . ARG D 1 67  ? 148.572 -22.634 72.154  1.000 32.040  ? 84  ARG DDD N   1 
ATOM 6447  C CA  . ARG D 1 67  ? 149.695 -22.620 73.128  1.000 32.610  ? 84  ARG DDD CA  1 
ATOM 6448  C C   . ARG D 1 67  ? 150.558 -23.867 72.879  1.000 31.610  ? 84  ARG DDD C   1 
ATOM 6449  O O   . ARG D 1 67  ? 150.019 -24.959 72.966  1.000 34.280  ? 84  ARG DDD O   1 
ATOM 6450  C CB  . ARG D 1 67  ? 149.149 -22.529 74.556  1.000 32.720  ? 84  ARG DDD CB  1 
ATOM 6451  C CG  . ARG D 1 67  ? 150.214 -22.210 75.587  1.000 39.940  ? 84  ARG DDD CG  1 
ATOM 6452  C CD  . ARG D 1 67  ? 149.715 -22.052 77.011  1.000 48.580  ? 84  ARG DDD CD  1 
ATOM 6453  N NE  . ARG D 1 67  ? 148.844 -23.144 77.403  1.000 57.860  ? 84  ARG DDD NE  1 
ATOM 6454  C CZ  . ARG D 1 67  ? 149.226 -24.393 77.667  1.000 69.110  ? 84  ARG DDD CZ  1 
ATOM 6455  N NH1 . ARG D 1 67  ? 150.505 -24.736 77.633  1.000 75.170  ? 84  ARG DDD NH1 1 
ATOM 6456  N NH2 . ARG D 1 67  ? 148.310 -25.299 77.958  1.000 73.700  ? 84  ARG DDD NH2 1 
ATOM 6457  N N   . ILE D 1 68  ? 151.832 -23.711 72.517  1.000 29.900  ? 85  ILE DDD N   1 
ATOM 6458  C CA  . ILE D 1 68  ? 152.751 -24.852 72.224  1.000 30.630  ? 85  ILE DDD CA  1 
ATOM 6459  C C   . ILE D 1 68  ? 153.764 -24.970 73.358  1.000 33.260  ? 85  ILE DDD C   1 
ATOM 6460  O O   . ILE D 1 68  ? 154.541 -24.042 73.580  1.000 34.330  ? 85  ILE DDD O   1 
ATOM 6461  C CB  . ILE D 1 68  ? 153.463 -24.691 70.865  1.000 30.860  ? 85  ILE DDD CB  1 
ATOM 6462  C CG1 . ILE D 1 68  ? 152.534 -24.191 69.751  1.000 33.710  ? 85  ILE DDD CG1 1 
ATOM 6463  C CG2 . ILE D 1 68  ? 154.165 -25.985 70.475  1.000 30.180  ? 85  ILE DDD CG2 1 
ATOM 6464  C CD1 . ILE D 1 68  ? 151.375 -25.105 69.426  1.000 34.370  ? 85  ILE DDD CD1 1 
ATOM 6465  N N   . PRO D 1 69  ? 153.838 -26.105 74.092  1.000 36.840  ? 86  PRO DDD N   1 
ATOM 6466  C CA  . PRO D 1 69  ? 154.817 -26.264 75.151  1.000 36.820  ? 86  PRO DDD CA  1 
ATOM 6467  C C   . PRO D 1 69  ? 156.185 -26.549 74.511  1.000 37.410  ? 86  PRO DDD C   1 
ATOM 6468  O O   . PRO D 1 69  ? 156.232 -27.373 73.610  1.000 39.510  ? 86  PRO DDD O   1 
ATOM 6469  C CB  . PRO D 1 69  ? 154.326 -27.466 75.957  1.000 41.050  ? 86  PRO DDD CB  1 
ATOM 6470  C CG  . PRO D 1 69  ? 152.964 -27.819 75.367  1.000 42.530  ? 86  PRO DDD CG  1 
ATOM 6471  C CD  . PRO D 1 69  ? 153.019 -27.313 73.946  1.000 39.970  ? 86  PRO DDD CD  1 
ATOM 6472  N N   . LEU D 1 70  ? 157.215 -25.845 74.953  1.000 34.910  ? 87  LEU DDD N   1 
ATOM 6473  C CA  . LEU D 1 70  ? 158.613 -26.010 74.454  1.000 34.200  ? 87  LEU DDD CA  1 
ATOM 6474  C C   . LEU D 1 70  ? 159.421 -26.809 75.456  1.000 35.470  ? 87  LEU DDD C   1 
ATOM 6475  O O   . LEU D 1 70  ? 159.039 -26.968 76.607  1.000 43.180  ? 87  LEU DDD O   1 
ATOM 6476  C CB  . LEU D 1 70  ? 159.203 -24.627 74.257  1.000 34.810  ? 87  LEU DDD CB  1 
ATOM 6477  C CG  . LEU D 1 70  ? 158.398 -23.715 73.334  1.000 39.390  ? 87  LEU DDD CG  1 
ATOM 6478  C CD1 . LEU D 1 70  ? 158.953 -22.289 73.367  1.000 40.510  ? 87  LEU DDD CD1 1 
ATOM 6479  C CD2 . LEU D 1 70  ? 158.388 -24.276 71.908  1.000 37.270  ? 87  LEU DDD CD2 1 
ATOM 6480  N N   . PRO D 1 71  ? 160.549 -27.407 75.036  1.000 35.390  ? 88  PRO DDD N   1 
ATOM 6481  C CA  . PRO D 1 71  ? 161.473 -28.070 75.954  1.000 38.950  ? 88  PRO DDD CA  1 
ATOM 6482  C C   . PRO D 1 71  ? 161.806 -27.261 77.212  1.000 39.760  ? 88  PRO DDD C   1 
ATOM 6483  O O   . PRO D 1 71  ? 162.146 -26.117 77.082  1.000 41.640  ? 88  PRO DDD O   1 
ATOM 6484  C CB  . PRO D 1 71  ? 162.729 -28.221 75.089  1.000 39.970  ? 88  PRO DDD CB  1 
ATOM 6485  C CG  . PRO D 1 71  ? 162.168 -28.468 73.726  1.000 41.410  ? 88  PRO DDD CG  1 
ATOM 6486  C CD  . PRO D 1 71  ? 160.982 -27.529 73.640  1.000 38.030  ? 88  PRO DDD CD  1 
ATOM 6487  N N   . ASN D 1 72  ? 161.770 -27.914 78.375  1.000 40.430  ? 89  ASN DDD N   1 
ATOM 6488  C CA  . ASN D 1 72  ? 162.127 -27.352 79.701  1.000 42.600  ? 89  ASN DDD CA  1 
ATOM 6489  C C   . ASN D 1 72  ? 163.596 -26.905 79.710  1.000 44.400  ? 89  ASN DDD C   1 
ATOM 6490  O O   . ASN D 1 72  ? 164.430 -27.596 79.071  1.000 44.520  ? 89  ASN DDD O   1 
ATOM 6491  C CB  . ASN D 1 72  ? 161.936 -28.401 80.800  1.000 45.930  ? 89  ASN DDD CB  1 
ATOM 6492  C CG  . ASN D 1 72  ? 162.016 -27.824 82.196  1.000 46.270  ? 89  ASN DDD CG  1 
ATOM 6493  O OD1 . ASN D 1 72  ? 161.340 -26.842 82.471  1.000 46.200  ? 89  ASN DDD OD1 1 
ATOM 6494  N ND2 . ASN D 1 72  ? 162.971 -28.303 82.984  1.000 48.670  ? 89  ASN DDD ND2 1 
ATOM 6495  N N   . LEU D 1 73  ? 163.907 -25.823 80.440  1.000 44.970  ? 90  LEU DDD N   1 
ATOM 6496  C CA  . LEU D 1 73  ? 165.278 -25.252 80.534  1.000 44.210  ? 90  LEU DDD CA  1 
ATOM 6497  C C   . LEU D 1 73  ? 165.700 -24.897 81.957  1.000 46.700  ? 90  LEU DDD C   1 
ATOM 6498  O O   . LEU D 1 73  ? 166.908 -24.770 82.155  1.000 55.180  ? 90  LEU DDD O   1 
ATOM 6499  C CB  . LEU D 1 73  ? 165.302 -23.976 79.693  1.000 45.070  ? 90  LEU DDD CB  1 
ATOM 6500  C CG  . LEU D 1 73  ? 164.832 -24.120 78.253  1.000 47.070  ? 90  LEU DDD CG  1 
ATOM 6501  C CD1 . LEU D 1 73  ? 164.716 -22.762 77.590  1.000 48.170  ? 90  LEU DDD CD1 1 
ATOM 6502  C CD2 . LEU D 1 73  ? 165.773 -25.034 77.505  1.000 47.920  ? 90  LEU DDD CD2 1 
ATOM 6503  N N   . ASN D 1 74  ? 164.765 -24.615 82.856  1.000 47.140  ? 91  ASN DDD N   1 
ATOM 6504  C CA  . ASN D 1 74  ? 165.031 -23.817 84.074  1.000 45.000  ? 91  ASN DDD CA  1 
ATOM 6505  C C   . ASN D 1 74  ? 164.207 -24.412 85.247  1.000 46.030  ? 91  ASN DDD C   1 
ATOM 6506  O O   . ASN D 1 74  ? 164.089 -25.688 85.349  1.000 34.240  ? 91  ASN DDD O   1 
ATOM 6507  C CB  . ASN D 1 74  ? 164.784 -22.331 83.747  1.000 36.990  ? 91  ASN DDD CB  1 
ATOM 6508  N N   . GLY D 1 80  ? 165.859 -15.913 88.723  1.000 112.350 ? 97  GLY DDD N   1 
ATOM 6509  C CA  . GLY D 1 80  ? 167.171 -15.224 88.845  1.000 117.210 ? 97  GLY DDD CA  1 
ATOM 6510  C C   . GLY D 1 80  ? 167.889 -15.219 87.482  1.000 113.200 ? 97  GLY DDD C   1 
ATOM 6511  O O   . GLY D 1 80  ? 167.390 -14.498 86.604  1.000 121.300 ? 97  GLY DDD O   1 
ATOM 6512  N N   . ASN D 1 81  ? 168.997 -15.966 87.305  1.000 101.220 ? 98  ASN DDD N   1 
ATOM 6513  C CA  . ASN D 1 81  ? 169.808 -16.035 86.055  1.000 84.920  ? 98  ASN DDD CA  1 
ATOM 6514  C C   . ASN D 1 81  ? 169.443 -17.299 85.234  1.000 80.880  ? 98  ASN DDD C   1 
ATOM 6515  O O   . ASN D 1 81  ? 170.221 -18.310 85.260  1.000 74.790  ? 98  ASN DDD O   1 
ATOM 6516  C CB  . ASN D 1 81  ? 171.286 -15.952 86.400  1.000 71.480  ? 98  ASN DDD CB  1 
ATOM 6517  N N   . ILE D 1 82  ? 168.314 -17.230 84.493  1.000 65.620  ? 99  ILE DDD N   1 
ATOM 6518  C CA  . ILE D 1 82  ? 167.613 -18.382 83.834  1.000 55.110  ? 99  ILE DDD CA  1 
ATOM 6519  C C   . ILE D 1 82  ? 167.655 -18.264 82.294  1.000 47.970  ? 99  ILE DDD C   1 
ATOM 6520  O O   . ILE D 1 82  ? 168.038 -17.206 81.777  1.000 43.450  ? 99  ILE DDD O   1 
ATOM 6521  C CB  . ILE D 1 82  ? 166.163 -18.497 84.358  1.000 53.640  ? 99  ILE DDD CB  1 
ATOM 6522  C CG1 . ILE D 1 82  ? 165.264 -17.385 83.820  1.000 53.640  ? 99  ILE DDD CG1 1 
ATOM 6523  C CG2 . ILE D 1 82  ? 166.139 -18.521 85.880  1.000 55.450  ? 99  ILE DDD CG2 1 
ATOM 6524  C CD1 . ILE D 1 82  ? 163.830 -17.450 84.304  1.000 54.940  ? 99  ILE DDD CD1 1 
ATOM 6525  N N   . LEU D 1 83  ? 167.224 -19.318 81.590  1.000 42.760  ? 100 LEU DDD N   1 
ATOM 6526  C CA  . LEU D 1 83  ? 167.094 -19.367 80.105  1.000 37.420  ? 100 LEU DDD CA  1 
ATOM 6527  C C   . LEU D 1 83  ? 165.620 -19.306 79.694  1.000 37.820  ? 100 LEU DDD C   1 
ATOM 6528  O O   . LEU D 1 83  ? 164.801 -19.985 80.348  1.000 40.600  ? 100 LEU DDD O   1 
ATOM 6529  C CB  . LEU D 1 83  ? 167.686 -20.670 79.572  1.000 37.350  ? 100 LEU DDD CB  1 
ATOM 6530  C CG  . LEU D 1 83  ? 169.184 -20.841 79.743  1.000 40.200  ? 100 LEU DDD CG  1 
ATOM 6531  C CD1 . LEU D 1 83  ? 169.674 -22.044 78.941  1.000 40.670  ? 100 LEU DDD CD1 1 
ATOM 6532  C CD2 . LEU D 1 83  ? 169.906 -19.567 79.345  1.000 42.430  ? 100 LEU DDD CD2 1 
ATOM 6533  N N   . MET D 1 84  ? 165.313 -18.563 78.623  1.000 36.470  ? 101 MET DDD N   1 
ATOM 6534  C CA  . MET D 1 84  ? 163.984 -18.531 77.954  1.000 37.570  ? 101 MET DDD CA  1 
ATOM 6535  C C   . MET D 1 84  ? 164.146 -18.778 76.451  1.000 37.850  ? 101 MET DDD C   1 
ATOM 6536  O O   . MET D 1 84  ? 165.199 -18.381 75.879  1.000 39.350  ? 101 MET DDD O   1 
ATOM 6537  C CB  . MET D 1 84  ? 163.311 -17.174 78.135  1.000 36.590  ? 101 MET DDD CB  1 
ATOM 6538  C CG  . MET D 1 84  ? 163.152 -16.763 79.564  1.000 37.520  ? 101 MET DDD CG  1 
ATOM 6539  S SD  . MET D 1 84  ? 162.208 -15.253 79.656  1.000 41.570  ? 101 MET DDD SD  1 
ATOM 6540  C CE  . MET D 1 84  ? 160.558 -15.912 79.408  1.000 40.910  ? 101 MET DDD CE  1 
ATOM 6541  N N   . TRP D 1 85  ? 163.133 -19.379 75.826  1.000 36.080  ? 102 TRP DDD N   1 
ATOM 6542  C CA  . TRP D 1 85  ? 163.114 -19.560 74.355  1.000 37.010  ? 102 TRP DDD CA  1 
ATOM 6543  C C   . TRP D 1 85  ? 162.762 -18.224 73.676  1.000 37.420  ? 102 TRP DDD C   1 
ATOM 6544  O O   . TRP D 1 85  ? 161.725 -17.608 74.030  1.000 33.970  ? 102 TRP DDD O   1 
ATOM 6545  C CB  . TRP D 1 85  ? 162.126 -20.652 73.971  1.000 35.970  ? 102 TRP DDD CB  1 
ATOM 6546  C CG  . TRP D 1 85  ? 162.594 -22.045 74.229  1.000 32.380  ? 102 TRP DDD CG  1 
ATOM 6547  C CD1 . TRP D 1 85  ? 162.023 -22.942 75.083  1.000 33.230  ? 102 TRP DDD CD1 1 
ATOM 6548  C CD2 . TRP D 1 85  ? 163.660 -22.733 73.573  1.000 31.790  ? 102 TRP DDD CD2 1 
ATOM 6549  N NE1 . TRP D 1 85  ? 162.683 -24.135 75.016  1.000 32.580  ? 102 TRP DDD NE1 1 
ATOM 6550  C CE2 . TRP D 1 85  ? 163.683 -24.047 74.085  1.000 31.130  ? 102 TRP DDD CE2 1 
ATOM 6551  C CE3 . TRP D 1 85  ? 164.603 -22.372 72.610  1.000 34.850  ? 102 TRP DDD CE3 1 
ATOM 6552  C CZ2 . TRP D 1 85  ? 164.617 -24.996 73.676  1.000 31.930  ? 102 TRP DDD CZ2 1 
ATOM 6553  C CZ3 . TRP D 1 85  ? 165.530 -23.308 72.196  1.000 35.770  ? 102 TRP DDD CZ3 1 
ATOM 6554  C CH2 . TRP D 1 85  ? 165.537 -24.603 72.729  1.000 34.490  ? 102 TRP DDD CH2 1 
ATOM 6555  N N   . GLU D 1 86  ? 163.610 -17.819 72.723  1.000 35.420  ? 103 GLU DDD N   1 
ATOM 6556  C CA  . GLU D 1 86  ? 163.472 -16.606 71.888  1.000 35.350  ? 103 GLU DDD CA  1 
ATOM 6557  C C   . GLU D 1 86  ? 162.970 -17.022 70.507  1.000 33.440  ? 103 GLU DDD C   1 
ATOM 6558  O O   . GLU D 1 86  ? 163.695 -17.754 69.822  1.000 32.810  ? 103 GLU DDD O   1 
ATOM 6559  C CB  . GLU D 1 86  ? 164.825 -15.894 71.809  1.000 37.490  ? 103 GLU DDD CB  1 
ATOM 6560  C CG  . GLU D 1 86  ? 164.743 -14.453 71.331  1.000 38.800  ? 103 GLU DDD CG  1 
ATOM 6561  C CD  . GLU D 1 86  ? 166.083 -13.792 71.034  1.000 40.080  ? 103 GLU DDD CD  1 
ATOM 6562  O OE1 . GLU D 1 86  ? 167.088 -14.518 70.940  1.000 41.160  ? 103 GLU DDD OE1 1 
ATOM 6563  O OE2 . GLU D 1 86  ? 166.124 -12.556 70.886  1.000 38.640  ? 103 GLU DDD OE2 1 
ATOM 6564  N N   . ALA D 1 87  ? 161.771 -16.579 70.119  1.000 33.070  ? 104 ALA DDD N   1 
ATOM 6565  C CA  . ALA D 1 87  ? 161.216 -16.786 68.758  1.000 32.420  ? 104 ALA DDD CA  1 
ATOM 6566  C C   . ALA D 1 87  ? 161.939 -15.840 67.794  1.000 30.800  ? 104 ALA DDD C   1 
ATOM 6567  O O   . ALA D 1 87  ? 161.879 -14.624 68.002  1.000 28.580  ? 104 ALA DDD O   1 
ATOM 6568  C CB  . ALA D 1 87  ? 159.722 -16.575 68.761  1.000 30.990  ? 104 ALA DDD CB  1 
ATOM 6569  N N   . VAL D 1 88  ? 162.599 -16.397 66.786  1.000 31.340  ? 105 VAL DDD N   1 
ATOM 6570  C CA  . VAL D 1 88  ? 163.550 -15.656 65.916  1.000 35.170  ? 105 VAL DDD CA  1 
ATOM 6571  C C   . VAL D 1 88  ? 162.960 -15.444 64.516  1.000 35.770  ? 105 VAL DDD C   1 
ATOM 6572  O O   . VAL D 1 88  ? 163.038 -14.311 64.022  1.000 40.650  ? 105 VAL DDD O   1 
ATOM 6573  C CB  . VAL D 1 88  ? 164.892 -16.400 65.890  1.000 35.850  ? 105 VAL DDD CB  1 
ATOM 6574  C CG1 . VAL D 1 88  ? 165.889 -15.785 64.930  1.000 38.070  ? 105 VAL DDD CG1 1 
ATOM 6575  C CG2 . VAL D 1 88  ? 165.475 -16.412 67.293  1.000 38.360  ? 105 VAL DDD CG2 1 
ATOM 6576  N N   . THR D 1 89  ? 162.413 -16.471 63.883  1.000 33.550  ? 106 THR DDD N   1 
ATOM 6577  C CA  . THR D 1 89  ? 161.859 -16.376 62.516  1.000 34.510  ? 106 THR DDD CA  1 
ATOM 6578  C C   . THR D 1 89  ? 160.500 -17.066 62.453  1.000 33.900  ? 106 THR DDD C   1 
ATOM 6579  O O   . THR D 1 89  ? 160.242 -18.004 63.216  1.000 34.490  ? 106 THR DDD O   1 
ATOM 6580  C CB  . THR D 1 89  ? 162.783 -16.999 61.461  1.000 39.140  ? 106 THR DDD CB  1 
ATOM 6581  O OG1 . THR D 1 89  ? 162.490 -18.400 61.356  1.000 40.180  ? 106 THR DDD OG1 1 
ATOM 6582  C CG2 . THR D 1 89  ? 164.252 -16.783 61.771  1.000 40.040  ? 106 THR DDD CG2 1 
ATOM 6583  N N   . LEU D 1 90  ? 159.660 -16.608 61.533  1.000 32.990  ? 107 LEU DDD N   1 
ATOM 6584  C CA  . LEU D 1 90  ? 158.339 -17.205 61.227  1.000 31.300  ? 107 LEU DDD CA  1 
ATOM 6585  C C   . LEU D 1 90  ? 158.279 -17.469 59.730  1.000 29.200  ? 107 LEU DDD C   1 
ATOM 6586  O O   . LEU D 1 90  ? 158.806 -16.666 58.989  1.000 29.380  ? 107 LEU DDD O   1 
ATOM 6587  C CB  . LEU D 1 90  ? 157.238 -16.233 61.646  1.000 29.480  ? 107 LEU DDD CB  1 
ATOM 6588  C CG  . LEU D 1 90  ? 155.856 -16.583 61.113  1.000 29.440  ? 107 LEU DDD CG  1 
ATOM 6589  C CD1 . LEU D 1 90  ? 155.363 -17.869 61.751  1.000 30.830  ? 107 LEU DDD CD1 1 
ATOM 6590  C CD2 . LEU D 1 90  ? 154.879 -15.447 61.370  1.000 29.860  ? 107 LEU DDD CD2 1 
ATOM 6591  N N   . LYS D 1 91  ? 157.705 -18.596 59.340  1.000 29.890  ? 108 LYS DDD N   1 
ATOM 6592  C CA  . LYS D 1 91  ? 157.157 -18.830 57.989  1.000 31.720  ? 108 LYS DDD CA  1 
ATOM 6593  C C   . LYS D 1 91  ? 155.684 -19.136 58.175  1.000 31.130  ? 108 LYS DDD C   1 
ATOM 6594  O O   . LYS D 1 91  ? 155.371 -19.933 59.077  1.000 31.580  ? 108 LYS DDD O   1 
ATOM 6595  C CB  . LYS D 1 91  ? 157.823 -20.026 57.316  1.000 34.490  ? 108 LYS DDD CB  1 
ATOM 6596  C CG  . LYS D 1 91  ? 159.235 -19.806 56.813  1.000 36.050  ? 108 LYS DDD CG  1 
ATOM 6597  C CD  . LYS D 1 91  ? 159.761 -21.092 56.172  1.000 36.150  ? 108 LYS DDD CD  1 
ATOM 6598  C CE  . LYS D 1 91  ? 160.565 -20.855 54.921  1.000 37.620  ? 108 LYS DDD CE  1 
ATOM 6599  N NZ  . LYS D 1 91  ? 161.541 -21.951 54.746  1.000 41.100  ? 108 LYS DDD NZ  1 
ATOM 6600  N N   . THR D 1 92  ? 154.826 -18.520 57.385  1.000 32.200  ? 109 THR DDD N   1 
ATOM 6601  C CA  . THR D 1 92  ? 153.378 -18.811 57.441  1.000 32.710  ? 109 THR DDD CA  1 
ATOM 6602  C C   . THR D 1 92  ? 152.828 -18.724 56.023  1.000 32.900  ? 109 THR DDD C   1 
ATOM 6603  O O   . THR D 1 92  ? 153.396 -17.955 55.219  1.000 31.160  ? 109 THR DDD O   1 
ATOM 6604  C CB  . THR D 1 92  ? 152.678 -17.879 58.435  1.000 30.050  ? 109 THR DDD CB  1 
ATOM 6605  O OG1 . THR D 1 92  ? 151.300 -18.237 58.430  1.000 29.740  ? 109 THR DDD OG1 1 
ATOM 6606  C CG2 . THR D 1 92  ? 152.820 -16.417 58.102  1.000 29.590  ? 109 THR DDD CG2 1 
ATOM 6607  N N   . GLU D 1 93  ? 151.797 -19.508 55.726  1.000 33.180  ? 110 GLU DDD N   1 
ATOM 6608  C CA  . GLU D 1 93  ? 150.975 -19.294 54.507  1.000 34.650  ? 110 GLU DDD CA  1 
ATOM 6609  C C   . GLU D 1 93  ? 149.575 -19.852 54.770  1.000 31.700  ? 110 GLU DDD C   1 
ATOM 6610  O O   . GLU D 1 93  ? 149.419 -20.602 55.748  1.000 34.280  ? 110 GLU DDD O   1 
ATOM 6611  C CB  . GLU D 1 93  ? 151.676 -19.869 53.271  1.000 35.750  ? 110 GLU DDD CB  1 
ATOM 6612  C CG  . GLU D 1 93  ? 151.374 -21.332 52.982  1.000 36.730  ? 110 GLU DDD CG  1 
ATOM 6613  C CD  . GLU D 1 93  ? 152.235 -21.960 51.896  1.000 38.820  ? 110 GLU DDD CD  1 
ATOM 6614  O OE1 . GLU D 1 93  ? 153.418 -21.532 51.751  1.000 36.350  ? 110 GLU DDD OE1 1 
ATOM 6615  O OE2 . GLU D 1 93  ? 151.725 -22.902 51.203  1.000 46.230  ? 110 GLU DDD OE2 1 
ATOM 6616  N N   . VAL D 1 94  ? 148.598 -19.456 53.965  1.000 26.630  ? 111 VAL DDD N   1 
ATOM 6617  C CA  . VAL D 1 94  ? 147.223 -19.996 54.084  1.000 26.110  ? 111 VAL DDD CA  1 
ATOM 6618  C C   . VAL D 1 94  ? 147.184 -21.366 53.402  1.000 26.210  ? 111 VAL DDD C   1 
ATOM 6619  O O   . VAL D 1 94  ? 147.657 -21.493 52.233  1.000 25.810  ? 111 VAL DDD O   1 
ATOM 6620  C CB  . VAL D 1 94  ? 146.205 -19.024 53.484  1.000 26.270  ? 111 VAL DDD CB  1 
ATOM 6621  C CG1 . VAL D 1 94  ? 144.801 -19.621 53.429  1.000 26.380  ? 111 VAL DDD CG1 1 
ATOM 6622  C CG2 . VAL D 1 94  ? 146.212 -17.736 54.269  1.000 27.730  ? 111 VAL DDD CG2 1 
ATOM 6623  N N   . ILE D 1 95  ? 146.620 -22.358 54.089  1.000 25.670  ? 112 ILE DDD N   1 
ATOM 6624  C CA  . ILE D 1 95  ? 146.534 -23.741 53.547  1.000 26.470  ? 112 ILE DDD CA  1 
ATOM 6625  C C   . ILE D 1 95  ? 145.172 -23.975 52.880  1.000 28.520  ? 112 ILE DDD C   1 
ATOM 6626  O O   . ILE D 1 95  ? 144.116 -23.925 53.569  1.000 31.430  ? 112 ILE DDD O   1 
ATOM 6627  C CB  . ILE D 1 95  ? 146.816 -24.776 54.631  1.000 24.610  ? 112 ILE DDD CB  1 
ATOM 6628  C CG1 . ILE D 1 95  ? 148.084 -24.463 55.409  1.000 26.680  ? 112 ILE DDD CG1 1 
ATOM 6629  C CG2 . ILE D 1 95  ? 146.912 -26.137 53.994  1.000 24.160  ? 112 ILE DDD CG2 1 
ATOM 6630  C CD1 . ILE D 1 95  ? 148.171 -25.232 56.722  1.000 30.030  ? 112 ILE DDD CD1 1 
ATOM 6631  N N   . GLY D 1 96  ? 145.205 -24.259 51.583  1.000 27.460  ? 113 GLY DDD N   1 
ATOM 6632  C CA  . GLY D 1 96  ? 144.014 -24.676 50.843  1.000 26.780  ? 113 GLY DDD CA  1 
ATOM 6633  C C   . GLY D 1 96  ? 143.453 -23.540 50.033  1.000 26.260  ? 113 GLY DDD C   1 
ATOM 6634  O O   . GLY D 1 96  ? 142.216 -23.484 49.937  1.000 25.570  ? 113 GLY DDD O   1 
ATOM 6635  N N   . VAL D 1 97  ? 144.320 -22.704 49.443  1.000 26.030  ? 114 VAL DDD N   1 
ATOM 6636  C CA  . VAL D 1 97  ? 143.891 -21.500 48.665  1.000 24.700  ? 114 VAL DDD CA  1 
ATOM 6637  C C   . VAL D 1 97  ? 143.106 -21.959 47.435  1.000 23.430  ? 114 VAL DDD C   1 
ATOM 6638  O O   . VAL D 1 97  ? 142.114 -21.316 47.114  1.000 22.170  ? 114 VAL DDD O   1 
ATOM 6639  C CB  . VAL D 1 97  ? 145.069 -20.595 48.269  1.000 24.100  ? 114 VAL DDD CB  1 
ATOM 6640  C CG1 . VAL D 1 97  ? 145.802 -20.099 49.505  1.000 25.750  ? 114 VAL DDD CG1 1 
ATOM 6641  C CG2 . VAL D 1 97  ? 146.022 -21.266 47.294  1.000 23.590  ? 114 VAL DDD CG2 1 
ATOM 6642  N N   . THR D 1 98  ? 143.535 -23.044 46.795  1.000 23.860  ? 115 THR DDD N   1 
ATOM 6643  C CA  . THR D 1 98  ? 142.956 -23.561 45.534  1.000 25.240  ? 115 THR DDD CA  1 
ATOM 6644  C C   . THR D 1 98  ? 141.484 -23.932 45.739  1.000 25.780  ? 115 THR DDD C   1 
ATOM 6645  O O   . THR D 1 98  ? 140.735 -23.954 44.741  1.000 30.660  ? 115 THR DDD O   1 
ATOM 6646  C CB  . THR D 1 98  ? 143.694 -24.815 45.038  1.000 26.720  ? 115 THR DDD CB  1 
ATOM 6647  O OG1 . THR D 1 98  ? 143.625 -25.811 46.069  1.000 31.090  ? 115 THR DDD OG1 1 
ATOM 6648  C CG2 . THR D 1 98  ? 145.126 -24.562 44.633  1.000 24.810  ? 115 THR DDD CG2 1 
ATOM 6649  N N   . SER D 1 99  ? 141.083 -24.252 46.968  1.000 24.480  ? 116 SER DDD N   1 
ATOM 6650  C CA  . SER D 1 99  ? 139.710 -24.699 47.285  1.000 25.000  ? 116 SER DDD CA  1 
ATOM 6651  C C   . SER D 1 99  ? 138.722 -23.610 46.888  1.000 23.670  ? 116 SER DDD C   1 
ATOM 6652  O O   . SER D 1 99  ? 137.533 -23.950 46.751  1.000 24.460  ? 116 SER DDD O   1 
ATOM 6653  C CB  . SER D 1 99  ? 139.563 -25.031 48.725  1.000 26.320  ? 116 SER DDD CB  1 
ATOM 6654  O OG  . SER D 1 99  ? 139.638 -23.851 49.486  1.000 27.340  ? 116 SER DDD OG  1 
ATOM 6655  N N   . LEU D 1 100 ? 139.211 -22.378 46.737  1.000 22.800  ? 117 LEU DDD N   1 
ATOM 6656  C CA  . LEU D 1 100 ? 138.378 -21.185 46.438  1.000 23.080  ? 117 LEU DDD CA  1 
ATOM 6657  C C   . LEU D 1 100 ? 138.012 -21.146 44.956  1.000 24.760  ? 117 LEU DDD C   1 
ATOM 6658  O O   . LEU D 1 100 ? 137.078 -20.373 44.628  1.000 28.360  ? 117 LEU DDD O   1 
ATOM 6659  C CB  . LEU D 1 100 ? 139.112 -19.914 46.872  1.000 21.950  ? 117 LEU DDD CB  1 
ATOM 6660  C CG  . LEU D 1 100 ? 139.273 -19.786 48.379  1.000 21.550  ? 117 LEU DDD CG  1 
ATOM 6661  C CD1 . LEU D 1 100 ? 139.874 -18.436 48.742  1.000 21.320  ? 117 LEU DDD CD1 1 
ATOM 6662  C CD2 . LEU D 1 100 ? 137.945 -20.004 49.088  1.000 21.350  ? 117 LEU DDD CD2 1 
ATOM 6663  N N   . MET D 1 101 ? 138.622 -22.011 44.148  1.000 26.530  ? 118 MET DDD N   1 
ATOM 6664  C CA  . MET D 1 101 ? 138.275 -22.164 42.716  1.000 27.950  ? 118 MET DDD CA  1 
ATOM 6665  C C   . MET D 1 101 ? 137.027 -23.045 42.530  1.000 29.730  ? 118 MET DDD C   1 
ATOM 6666  O O   . MET D 1 101 ? 136.617 -23.179 41.375  1.000 35.130  ? 118 MET DDD O   1 
ATOM 6667  C CB  . MET D 1 101 ? 139.431 -22.785 41.934  1.000 28.090  ? 118 MET DDD CB  1 
ATOM 6668  C CG  . MET D 1 101 ? 140.716 -22.052 42.126  1.000 30.410  ? 118 MET DDD CG  1 
ATOM 6669  S SD  . MET D 1 101 ? 141.958 -22.582 40.913  1.000 34.830  ? 118 MET DDD SD  1 
ATOM 6670  C CE  . MET D 1 101 ? 141.463 -21.504 39.574  1.000 35.810  ? 118 MET DDD CE  1 
ATOM 6671  N N   . ASN D 1 102 ? 136.452 -23.624 43.596  1.000 29.550  ? 119 ASN DDD N   1 
ATOM 6672  C CA  . ASN D 1 102 ? 135.233 -24.458 43.463  1.000 29.060  ? 119 ASN DDD CA  1 
ATOM 6673  C C   . ASN D 1 102 ? 134.027 -23.547 43.208  1.000 27.000  ? 119 ASN DDD C   1 
ATOM 6674  O O   . ASN D 1 102 ? 133.323 -23.198 44.159  1.000 27.430  ? 119 ASN DDD O   1 
ATOM 6675  C CB  . ASN D 1 102 ? 134.961 -25.374 44.652  1.000 30.710  ? 119 ASN DDD CB  1 
ATOM 6676  C CG  . ASN D 1 102 ? 133.745 -26.257 44.413  1.000 34.750  ? 119 ASN DDD CG  1 
ATOM 6677  O OD1 . ASN D 1 102 ? 132.901 -25.948 43.578  1.000 36.920  ? 119 ASN DDD OD1 1 
ATOM 6678  N ND2 . ASN D 1 102 ? 133.641 -27.368 45.133  1.000 43.250  ? 119 ASN DDD ND2 1 
ATOM 6679  N N   . VAL D 1 103 ? 133.739 -23.308 41.938  1.000 25.680  ? 120 VAL DDD N   1 
ATOM 6680  C CA  . VAL D 1 103 ? 132.672 -22.382 41.467  1.000 25.790  ? 120 VAL DDD CA  1 
ATOM 6681  C C   . VAL D 1 103 ? 131.437 -23.160 40.980  1.000 24.460  ? 120 VAL DDD C   1 
ATOM 6682  O O   . VAL D 1 103 ? 130.600 -22.563 40.313  1.000 21.400  ? 120 VAL DDD O   1 
ATOM 6683  C CB  . VAL D 1 103 ? 133.276 -21.500 40.368  1.000 26.640  ? 120 VAL DDD CB  1 
ATOM 6684  C CG1 . VAL D 1 103 ? 134.472 -20.753 40.892  1.000 29.370  ? 120 VAL DDD CG1 1 
ATOM 6685  C CG2 . VAL D 1 103 ? 133.687 -22.301 39.150  1.000 26.630  ? 120 VAL DDD CG2 1 
ATOM 6686  N N   . HIS D 1 104 ? 131.273 -24.419 41.393  1.000 24.730  ? 121 HIS DDD N   1 
ATOM 6687  C CA  . HIS D 1 104 ? 130.222 -25.340 40.880  1.000 24.890  ? 121 HIS DDD CA  1 
ATOM 6688  C C   . HIS D 1 104 ? 129.347 -25.951 41.993  1.000 25.220  ? 121 HIS DDD C   1 
ATOM 6689  O O   . HIS D 1 104 ? 128.424 -26.721 41.638  1.000 28.630  ? 121 HIS DDD O   1 
ATOM 6690  C CB  . HIS D 1 104 ? 130.890 -26.449 40.042  1.000 23.240  ? 121 HIS DDD CB  1 
ATOM 6691  C CG  . HIS D 1 104 ? 132.084 -27.057 40.664  1.000 21.320  ? 121 HIS DDD CG  1 
ATOM 6692  N ND1 . HIS D 1 104 ? 132.006 -28.137 41.514  1.000 21.800  ? 121 HIS DDD ND1 1 
ATOM 6693  C CD2 . HIS D 1 104 ? 133.393 -26.749 40.557  1.000 21.570  ? 121 HIS DDD CD2 1 
ATOM 6694  C CE1 . HIS D 1 104 ? 133.217 -28.472 41.916  1.000 22.420  ? 121 HIS DDD CE1 1 
ATOM 6695  N NE2 . HIS D 1 104 ? 134.092 -27.640 41.335  1.000 22.400  ? 121 HIS DDD NE2 1 
ATOM 6696  N N   . SER D 1 105 ? 129.592 -25.635 43.267  1.000 22.610  ? 122 SER DDD N   1 
ATOM 6697  C CA  . SER D 1 105 ? 128.952 -26.297 44.433  1.000 22.550  ? 122 SER DDD CA  1 
ATOM 6698  C C   . SER D 1 105 ? 127.771 -25.456 44.929  1.000 21.190  ? 122 SER DDD C   1 
ATOM 6699  O O   . SER D 1 105 ? 127.887 -24.832 45.973  1.000 19.770  ? 122 SER DDD O   1 
ATOM 6700  C CB  . SER D 1 105 ? 129.963 -26.567 45.527  1.000 23.470  ? 122 SER DDD CB  1 
ATOM 6701  O OG  . SER D 1 105 ? 129.365 -27.199 46.650  1.000 23.760  ? 122 SER DDD OG  1 
ATOM 6702  N N   . ASN D 1 106 ? 126.670 -25.470 44.184  1.000 22.390  ? 123 ASN DDD N   1 
ATOM 6703  C CA  . ASN D 1 106 ? 125.402 -24.790 44.541  1.000 24.010  ? 123 ASN DDD CA  1 
ATOM 6704  C C   . ASN D 1 106 ? 125.654 -23.307 44.799  1.000 24.940  ? 123 ASN DDD C   1 
ATOM 6705  O O   . ASN D 1 106 ? 125.070 -22.788 45.740  1.000 22.780  ? 123 ASN DDD O   1 
ATOM 6706  C CB  . ASN D 1 106 ? 124.766 -25.430 45.765  1.000 25.350  ? 123 ASN DDD CB  1 
ATOM 6707  C CG  . ASN D 1 106 ? 123.266 -25.266 45.783  1.000 27.730  ? 123 ASN DDD CG  1 
ATOM 6708  O OD1 . ASN D 1 106 ? 122.606 -25.733 44.872  1.000 28.280  ? 123 ASN DDD OD1 1 
ATOM 6709  N ND2 . ASN D 1 106 ? 122.711 -24.638 46.810  1.000 34.550  ? 123 ASN DDD ND2 1 
ATOM 6710  N N   . GLY D 1 107 ? 126.518 -22.659 44.004  1.000 29.440  ? 124 GLY DDD N   1 
ATOM 6711  C CA  . GLY D 1 107 ? 126.805 -21.217 44.128  1.000 33.060  ? 124 GLY DDD CA  1 
ATOM 6712  C C   . GLY D 1 107 ? 125.789 -20.263 43.527  1.000 35.080  ? 124 GLY DDD C   1 
ATOM 6713  O O   . GLY D 1 107 ? 124.722 -20.762 43.033  1.000 32.970  ? 124 GLY DDD O   1 
ATOM 6714  N N   . GLN D 1 108 ? 126.166 -18.999 43.327  1.000 32.120  ? 125 GLN DDD N   1 
ATOM 6715  C CA  . GLN D 1 108 ? 125.250 -18.075 42.616  1.000 30.200  ? 125 GLN DDD CA  1 
ATOM 6716  C C   . GLN D 1 108 ? 125.771 -17.737 41.221  1.000 30.340  ? 125 GLN DDD C   1 
ATOM 6717  O O   . GLN D 1 108 ? 126.703 -16.940 41.151  1.000 31.020  ? 125 GLN DDD O   1 
ATOM 6718  C CB  . GLN D 1 108 ? 125.025 -16.783 43.385  1.000 28.190  ? 125 GLN DDD CB  1 
ATOM 6719  C CG  . GLN D 1 108 ? 123.736 -16.068 43.019  1.000 26.060  ? 125 GLN DDD CG  1 
ATOM 6720  C CD  . GLN D 1 108 ? 123.762 -14.625 43.451  1.000 23.240  ? 125 GLN DDD CD  1 
ATOM 6721  O OE1 . GLN D 1 108 ? 124.812 -13.993 43.509  1.000 20.130  ? 125 GLN DDD OE1 1 
ATOM 6722  N NE2 . GLN D 1 108 ? 122.594 -14.089 43.756  1.000 22.920  ? 125 GLN DDD NE2 1 
ATOM 6723  N N   . ALA D 1 109 ? 125.220 -18.325 40.169  1.000 29.850  ? 126 ALA DDD N   1 
ATOM 6724  C CA  . ALA D 1 109 ? 125.511 -18.028 38.755  1.000 30.870  ? 126 ALA DDD CA  1 
ATOM 6725  C C   . ALA D 1 109 ? 125.601 -16.509 38.730  1.000 30.140  ? 126 ALA DDD C   1 
ATOM 6726  O O   . ALA D 1 109 ? 124.625 -15.872 39.085  1.000 33.020  ? 126 ALA DDD O   1 
ATOM 6727  C CB  . ALA D 1 109 ? 124.519 -18.513 37.739  1.000 32.050  ? 126 ALA DDD CB  1 
ATOM 6728  N N   . THR D 1 110 ? 126.745 -15.973 38.331  1.000 31.640  ? 127 THR DDD N   1 
ATOM 6729  C CA  . THR D 1 110 ? 126.997 -14.526 38.143  1.000 32.060  ? 127 THR DDD CA  1 
ATOM 6730  C C   . THR D 1 110 ? 126.059 -13.994 37.061  1.000 32.400  ? 127 THR DDD C   1 
ATOM 6731  O O   . THR D 1 110 ? 125.779 -12.809 37.091  1.000 40.350  ? 127 THR DDD O   1 
ATOM 6732  C CB  . THR D 1 110 ? 128.477 -14.303 37.792  1.000 37.170  ? 127 THR DDD CB  1 
ATOM 6733  O OG1 . THR D 1 110 ? 128.920 -15.205 36.773  1.000 35.370  ? 127 THR DDD OG1 1 
ATOM 6734  C CG2 . THR D 1 110 ? 129.393 -14.501 38.982  1.000 41.500  ? 127 THR DDD CG2 1 
ATOM 6735  N N   . HIS D 1 111 ? 125.577 -14.834 36.144  1.000 30.410  ? 128 HIS DDD N   1 
ATOM 6736  C CA  . HIS D 1 111 ? 124.682 -14.449 35.023  1.000 29.140  ? 128 HIS DDD CA  1 
ATOM 6737  C C   . HIS D 1 111 ? 124.171 -15.712 34.315  1.000 30.310  ? 128 HIS DDD C   1 
ATOM 6738  O O   . HIS D 1 111 ? 124.663 -16.798 34.642  1.000 33.950  ? 128 HIS DDD O   1 
ATOM 6739  C CB  . HIS D 1 111 ? 125.448 -13.585 34.032  1.000 28.410  ? 128 HIS DDD CB  1 
ATOM 6740  C CG  . HIS D 1 111 ? 126.650 -14.281 33.491  1.000 28.390  ? 128 HIS DDD CG  1 
ATOM 6741  N ND1 . HIS D 1 111 ? 127.877 -14.177 34.097  1.000 29.230  ? 128 HIS DDD ND1 1 
ATOM 6742  C CD2 . HIS D 1 111 ? 126.810 -15.120 32.443  1.000 27.320  ? 128 HIS DDD CD2 1 
ATOM 6743  C CE1 . HIS D 1 111 ? 128.752 -14.891 33.418  1.000 28.630  ? 128 HIS DDD CE1 1 
ATOM 6744  N NE2 . HIS D 1 111 ? 128.118 -15.499 32.417  1.000 26.350  ? 128 HIS DDD NE2 1 
ATOM 6745  N N   . ASP D 1 112 ? 123.249 -15.592 33.353  1.000 28.050  ? 129 ASP DDD N   1 
ATOM 6746  C CA  . ASP D 1 112 ? 122.698 -16.779 32.667  1.000 27.580  ? 129 ASP DDD CA  1 
ATOM 6747  C C   . ASP D 1 112 ? 123.853 -17.643 32.137  1.000 29.730  ? 129 ASP DDD C   1 
ATOM 6748  O O   . ASP D 1 112 ? 124.654 -17.144 31.319  1.000 30.950  ? 129 ASP DDD O   1 
ATOM 6749  C CB  . ASP D 1 112 ? 121.730 -16.365 31.574  1.000 27.940  ? 129 ASP DDD CB  1 
ATOM 6750  C CG  . ASP D 1 112 ? 120.358 -16.021 32.102  1.000 27.540  ? 129 ASP DDD CG  1 
ATOM 6751  O OD1 . ASP D 1 112 ? 120.039 -16.465 33.193  1.000 25.780  ? 129 ASP DDD OD1 1 
ATOM 6752  O OD2 . ASP D 1 112 ? 119.612 -15.331 31.389  1.000 32.470  ? 129 ASP DDD OD2 1 
ATOM 6753  N N   . ASN D 1 113 ? 123.904 -18.894 32.607  1.000 29.330  ? 130 ASN DDD N   1 
ATOM 6754  C CA  . ASN D 1 113 ? 124.874 -19.952 32.219  1.000 28.570  ? 130 ASN DDD CA  1 
ATOM 6755  C C   . ASN D 1 113 ? 126.241 -19.611 32.812  1.000 26.790  ? 130 ASN DDD C   1 
ATOM 6756  O O   . ASN D 1 113 ? 127.243 -20.293 32.467  1.000 30.800  ? 130 ASN DDD O   1 
ATOM 6757  C CB  . ASN D 1 113 ? 124.977 -20.164 30.700  1.000 28.630  ? 130 ASN DDD CB  1 
ATOM 6758  C CG  . ASN D 1 113 ? 123.660 -20.414 30.000  1.000 28.710  ? 130 ASN DDD CG  1 
ATOM 6759  O OD1 . ASN D 1 113 ? 122.777 -21.126 30.483  1.000 28.330  ? 130 ASN DDD OD1 1 
ATOM 6760  N ND2 . ASN D 1 113 ? 123.533 -19.816 28.833  1.000 28.880  ? 130 ASN DDD ND2 1 
ATOM 6761  N N   . GLY D 1 114 ? 126.307 -18.615 33.684  1.000 24.840  ? 131 GLY DDD N   1 
ATOM 6762  C CA  . GLY D 1 114 ? 127.559 -18.266 34.373  1.000 24.450  ? 131 GLY DDD CA  1 
ATOM 6763  C C   . GLY D 1 114 ? 127.969 -19.351 35.347  1.000 22.850  ? 131 GLY DDD C   1 
ATOM 6764  O O   . GLY D 1 114 ? 127.101 -20.145 35.835  1.000 20.680  ? 131 GLY DDD O   1 
ATOM 6765  N N   . ALA D 1 115 ? 129.267 -19.410 35.604  1.000 23.460  ? 132 ALA DDD N   1 
ATOM 6766  C CA  . ALA D 1 115 ? 129.831 -20.216 36.701  1.000 24.700  ? 132 ALA DDD CA  1 
ATOM 6767  C C   . ALA D 1 115 ? 129.302 -19.590 37.989  1.000 26.130  ? 132 ALA DDD C   1 
ATOM 6768  O O   . ALA D 1 115 ? 128.704 -18.503 37.920  1.000 26.250  ? 132 ALA DDD O   1 
ATOM 6769  C CB  . ALA D 1 115 ? 131.341 -20.195 36.634  1.000 24.650  ? 132 ALA DDD CB  1 
ATOM 6770  N N   . GLY D 1 116 ? 129.534 -20.217 39.123  1.000 26.920  ? 133 GLY DDD N   1 
ATOM 6771  C CA  . GLY D 1 116 ? 129.085 -19.610 40.383  1.000 28.240  ? 133 GLY DDD CA  1 
ATOM 6772  C C   . GLY D 1 116 ? 129.979 -18.448 40.739  1.000 27.040  ? 133 GLY DDD C   1 
ATOM 6773  O O   . GLY D 1 116 ? 131.183 -18.497 40.394  1.000 22.870  ? 133 GLY DDD O   1 
ATOM 6774  N N   . LYS D 1 117 ? 129.423 -17.466 41.449  1.000 29.470  ? 134 LYS DDD N   1 
ATOM 6775  C CA  . LYS D 1 117 ? 130.235 -16.365 42.023  1.000 28.970  ? 134 LYS DDD CA  1 
ATOM 6776  C C   . LYS D 1 117 ? 131.227 -16.994 42.985  1.000 25.760  ? 134 LYS DDD C   1 
ATOM 6777  O O   . LYS D 1 117 ? 130.813 -17.690 43.902  1.000 27.530  ? 134 LYS DDD O   1 
ATOM 6778  C CB  . LYS D 1 117 ? 129.356 -15.336 42.731  1.000 30.710  ? 134 LYS DDD CB  1 
ATOM 6779  C CG  . LYS D 1 117 ? 130.130 -14.341 43.575  1.000 34.640  ? 134 LYS DDD CG  1 
ATOM 6780  C CD  . LYS D 1 117 ? 129.280 -13.261 44.189  1.000 38.250  ? 134 LYS DDD CD  1 
ATOM 6781  C CE  . LYS D 1 117 ? 129.057 -12.159 43.182  1.000 42.020  ? 134 LYS DDD CE  1 
ATOM 6782  N NZ  . LYS D 1 117 ? 127.979 -11.260 43.617  1.000 48.670  ? 134 LYS DDD NZ  1 
ATOM 6783  N N   . PRO D 1 118 ? 132.540 -16.756 42.824  1.000 23.280  ? 135 PRO DDD N   1 
ATOM 6784  C CA  . PRO D 1 118 ? 133.548 -17.381 43.675  1.000 23.530  ? 135 PRO DDD CA  1 
ATOM 6785  C C   . PRO D 1 118 ? 133.552 -16.712 45.045  1.000 24.220  ? 135 PRO DDD C   1 
ATOM 6786  O O   . PRO D 1 118 ? 133.075 -15.614 45.138  1.000 23.350  ? 135 PRO DDD O   1 
ATOM 6787  C CB  . PRO D 1 118 ? 134.886 -17.066 43.002  1.000 23.320  ? 135 PRO DDD CB  1 
ATOM 6788  C CG  . PRO D 1 118 ? 134.599 -15.767 42.285  1.000 23.980  ? 135 PRO DDD CG  1 
ATOM 6789  C CD  . PRO D 1 118 ? 133.133 -15.812 41.875  1.000 23.560  ? 135 PRO DDD CD  1 
ATOM 6790  N N   . VAL D 1 119 ? 134.115 -17.379 46.054  1.000 24.890  ? 136 VAL DDD N   1 
ATOM 6791  C CA  . VAL D 1 119 ? 134.361 -16.733 47.379  1.000 24.080  ? 136 VAL DDD CA  1 
ATOM 6792  C C   . VAL D 1 119 ? 135.089 -15.422 47.099  1.000 22.340  ? 136 VAL DDD C   1 
ATOM 6793  O O   . VAL D 1 119 ? 136.077 -15.466 46.370  1.000 22.040  ? 136 VAL DDD O   1 
ATOM 6794  C CB  . VAL D 1 119 ? 135.159 -17.620 48.349  1.000 23.430  ? 136 VAL DDD CB  1 
ATOM 6795  C CG1 . VAL D 1 119 ? 135.607 -16.839 49.572  1.000 24.110  ? 136 VAL DDD CG1 1 
ATOM 6796  C CG2 . VAL D 1 119 ? 134.393 -18.856 48.778  1.000 23.500  ? 136 VAL DDD CG2 1 
ATOM 6797  N N   . GLN D 1 120 ? 134.584 -14.333 47.665  1.000 23.220  ? 137 GLN DDD N   1 
ATOM 6798  C CA  . GLN D 1 120 ? 135.150 -12.964 47.554  1.000 27.380  ? 137 GLN DDD CA  1 
ATOM 6799  C C   . GLN D 1 120 ? 134.578 -12.067 48.641  1.000 26.490  ? 137 GLN DDD C   1 
ATOM 6800  O O   . GLN D 1 120 ? 133.653 -12.490 49.314  1.000 30.830  ? 137 GLN DDD O   1 
ATOM 6801  C CB  . GLN D 1 120 ? 134.822 -12.344 46.188  1.000 30.430  ? 137 GLN DDD CB  1 
ATOM 6802  C CG  . GLN D 1 120 ? 133.338 -12.095 45.952  1.000 30.730  ? 137 GLN DDD CG  1 
ATOM 6803  C CD  . GLN D 1 120 ? 133.033 -11.810 44.511  1.000 30.830  ? 137 GLN DDD CD  1 
ATOM 6804  O OE1 . GLN D 1 120 ? 132.970 -10.678 44.060  1.000 32.900  ? 137 GLN DDD OE1 1 
ATOM 6805  N NE2 . GLN D 1 120 ? 132.885 -12.873 43.757  1.000 35.410  ? 137 GLN DDD NE2 1 
ATOM 6806  N N   . GLY D 1 121 ? 135.097 -10.854 48.767  1.000 24.940  ? 138 GLY DDD N   1 
ATOM 6807  C CA  . GLY D 1 121 ? 134.527 -9.824  49.650  1.000 24.940  ? 138 GLY DDD CA  1 
ATOM 6808  C C   . GLY D 1 121 ? 135.327 -9.654  50.923  1.000 23.700  ? 138 GLY DDD C   1 
ATOM 6809  O O   . GLY D 1 121 ? 136.445 -10.155 50.985  1.000 28.010  ? 138 GLY DDD O   1 
ATOM 6810  N N   . THR D 1 122 ? 134.741 -8.952  51.892  1.000 22.760  ? 139 THR DDD N   1 
ATOM 6811  C CA  . THR D 1 122 ? 135.388 -8.490  53.143  1.000 22.660  ? 139 THR DDD CA  1 
ATOM 6812  C C   . THR D 1 122 ? 136.256 -9.616  53.708  1.000 21.450  ? 139 THR DDD C   1 
ATOM 6813  O O   . THR D 1 122 ? 135.774 -10.735 53.810  1.000 20.560  ? 139 THR DDD O   1 
ATOM 6814  C CB  . THR D 1 122 ? 134.327 -8.018  54.140  1.000 24.350  ? 139 THR DDD CB  1 
ATOM 6815  O OG1 . THR D 1 122 ? 133.467 -7.075  53.488  1.000 23.980  ? 139 THR DDD OG1 1 
ATOM 6816  C CG2 . THR D 1 122 ? 134.933 -7.422  55.391  1.000 24.790  ? 139 THR DDD CG2 1 
ATOM 6817  N N   . SER D 1 123 ? 137.507 -9.311  54.022  1.000 21.390  ? 140 SER DDD N   1 
ATOM 6818  C CA  . SER D 1 123 ? 138.561 -10.287 54.376  1.000 23.080  ? 140 SER DDD CA  1 
ATOM 6819  C C   . SER D 1 123 ? 139.365 -9.731  55.541  1.000 24.120  ? 140 SER DDD C   1 
ATOM 6820  O O   . SER D 1 123 ? 139.696 -8.537  55.471  1.000 25.360  ? 140 SER DDD O   1 
ATOM 6821  C CB  . SER D 1 123 ? 139.478 -10.538 53.209  1.000 24.800  ? 140 SER DDD CB  1 
ATOM 6822  O OG  . SER D 1 123 ? 140.482 -9.532  53.134  1.000 27.490  ? 140 SER DDD OG  1 
ATOM 6823  N N   . PHE D 1 124 ? 139.703 -10.560 56.536  1.000 24.760  ? 141 PHE DDD N   1 
ATOM 6824  C CA  . PHE D 1 124 ? 140.717 -10.239 57.573  1.000 24.380  ? 141 PHE DDD CA  1 
ATOM 6825  C C   . PHE D 1 124 ? 141.736 -11.385 57.623  1.000 24.940  ? 141 PHE DDD C   1 
ATOM 6826  O O   . PHE D 1 124 ? 141.380 -12.521 57.984  1.000 26.720  ? 141 PHE DDD O   1 
ATOM 6827  C CB  . PHE D 1 124 ? 140.040 -9.928  58.913  1.000 25.470  ? 141 PHE DDD CB  1 
ATOM 6828  C CG  . PHE D 1 124 ? 140.969 -9.370  59.969  1.000 26.740  ? 141 PHE DDD CG  1 
ATOM 6829  C CD1 . PHE D 1 124 ? 141.778 -8.281  59.704  1.000 26.100  ? 141 PHE DDD CD1 1 
ATOM 6830  C CD2 . PHE D 1 124 ? 141.073 -9.953  61.222  1.000 27.500  ? 141 PHE DDD CD2 1 
ATOM 6831  C CE1 . PHE D 1 124 ? 142.635 -7.772  60.661  1.000 24.830  ? 141 PHE DDD CE1 1 
ATOM 6832  C CE2 . PHE D 1 124 ? 141.953 -9.461  62.166  1.000 25.910  ? 141 PHE DDD CE2 1 
ATOM 6833  C CZ  . PHE D 1 124 ? 142.740 -8.383  61.877  1.000 25.610  ? 141 PHE DDD CZ  1 
ATOM 6834  N N   . HIS D 1 125 ? 142.964 -11.120 57.187  1.000 25.380  ? 142 HIS DDD N   1 
ATOM 6835  C CA  . HIS D 1 125 ? 144.115 -12.057 57.303  1.000 26.830  ? 142 HIS DDD CA  1 
ATOM 6836  C C   . HIS D 1 125 ? 145.050 -11.461 58.341  1.000 27.380  ? 142 HIS DDD C   1 
ATOM 6837  O O   . HIS D 1 125 ? 145.449 -10.296 58.158  1.000 28.780  ? 142 HIS DDD O   1 
ATOM 6838  C CB  . HIS D 1 125 ? 144.778 -12.360 55.949  1.000 27.030  ? 142 HIS DDD CB  1 
ATOM 6839  C CG  . HIS D 1 125 ? 143.825 -13.017 55.011  1.000 28.950  ? 142 HIS DDD CG  1 
ATOM 6840  N ND1 . HIS D 1 125 ? 143.517 -14.348 55.122  1.000 30.320  ? 142 HIS DDD ND1 1 
ATOM 6841  C CD2 . HIS D 1 125 ? 143.041 -12.508 54.022  1.000 30.170  ? 142 HIS DDD CD2 1 
ATOM 6842  C CE1 . HIS D 1 125 ? 142.616 -14.651 54.201  1.000 34.080  ? 142 HIS DDD CE1 1 
ATOM 6843  N NE2 . HIS D 1 125 ? 142.306 -13.525 53.497  1.000 30.590  ? 142 HIS DDD NE2 1 
ATOM 6844  N N   . PHE D 1 126 ? 145.289 -12.219 59.416  1.000 27.540  ? 143 PHE DDD N   1 
ATOM 6845  C CA  . PHE D 1 126 ? 146.006 -11.800 60.642  1.000 26.450  ? 143 PHE DDD CA  1 
ATOM 6846  C C   . PHE D 1 126 ? 146.742 -13.009 61.222  1.000 23.880  ? 143 PHE DDD C   1 
ATOM 6847  O O   . PHE D 1 126 ? 146.197 -14.129 61.188  1.000 22.920  ? 143 PHE DDD O   1 
ATOM 6848  C CB  . PHE D 1 126 ? 145.015 -11.248 61.672  1.000 29.930  ? 143 PHE DDD CB  1 
ATOM 6849  C CG  . PHE D 1 126 ? 145.611 -11.128 63.046  1.000 33.390  ? 143 PHE DDD CG  1 
ATOM 6850  C CD1 . PHE D 1 126 ? 146.434 -10.058 63.351  1.000 34.600  ? 143 PHE DDD CD1 1 
ATOM 6851  C CD2 . PHE D 1 126 ? 145.429 -12.123 63.997  1.000 32.090  ? 143 PHE DDD CD2 1 
ATOM 6852  C CE1 . PHE D 1 126 ? 147.027 -9.975  64.596  1.000 33.230  ? 143 PHE DDD CE1 1 
ATOM 6853  C CE2 . PHE D 1 126 ? 146.037 -12.034 65.231  1.000 31.010  ? 143 PHE DDD CE2 1 
ATOM 6854  C CZ  . PHE D 1 126 ? 146.825 -10.958 65.529  1.000 32.160  ? 143 PHE DDD CZ  1 
ATOM 6855  N N   . PHE D 1 127 ? 147.928 -12.782 61.774  1.000 23.350  ? 144 PHE DDD N   1 
ATOM 6856  C CA  . PHE D 1 127 ? 148.711 -13.823 62.484  1.000 25.720  ? 144 PHE DDD CA  1 
ATOM 6857  C C   . PHE D 1 127 ? 149.751 -13.176 63.385  1.000 29.320  ? 144 PHE DDD C   1 
ATOM 6858  O O   . PHE D 1 127 ? 150.344 -12.137 62.999  1.000 29.620  ? 144 PHE DDD O   1 
ATOM 6859  C CB  . PHE D 1 127 ? 149.379 -14.746 61.475  1.000 25.550  ? 144 PHE DDD CB  1 
ATOM 6860  C CG  . PHE D 1 127 ? 150.343 -14.030 60.562  1.000 24.900  ? 144 PHE DDD CG  1 
ATOM 6861  C CD1 . PHE D 1 127 ? 151.645 -13.809 60.965  1.000 24.490  ? 144 PHE DDD CD1 1 
ATOM 6862  C CD2 . PHE D 1 127 ? 149.952 -13.575 59.316  1.000 22.600  ? 144 PHE DDD CD2 1 
ATOM 6863  C CE1 . PHE D 1 127 ? 152.549 -13.188 60.129  1.000 22.090  ? 144 PHE DDD CE1 1 
ATOM 6864  C CE2 . PHE D 1 127 ? 150.846 -12.915 58.505  1.000 20.890  ? 144 PHE DDD CE2 1 
ATOM 6865  C CZ  . PHE D 1 127 ? 152.138 -12.732 58.913  1.000 21.080  ? 144 PHE DDD CZ  1 
ATOM 6866  N N   . SER D 1 128 ? 149.964 -13.787 64.555  1.000 31.830  ? 145 SER DDD N   1 
ATOM 6867  C CA  . SER D 1 128 ? 150.829 -13.272 65.646  1.000 31.020  ? 145 SER DDD CA  1 
ATOM 6868  C C   . SER D 1 128 ? 151.710 -14.411 66.171  1.000 28.020  ? 145 SER DDD C   1 
ATOM 6869  O O   . SER D 1 128 ? 151.252 -15.570 66.142  1.000 26.440  ? 145 SER DDD O   1 
ATOM 6870  C CB  . SER D 1 128 ? 149.989 -12.679 66.753  1.000 32.630  ? 145 SER DDD CB  1 
ATOM 6871  O OG  . SER D 1 128 ? 149.646 -13.674 67.726  1.000 36.640  ? 145 SER DDD OG  1 
ATOM 6872  N N   . VAL D 1 129 ? 152.916 -14.080 66.634  1.000 26.280  ? 146 VAL DDD N   1 
ATOM 6873  C CA  . VAL D 1 129 ? 153.830 -14.999 67.371  1.000 26.220  ? 146 VAL DDD CA  1 
ATOM 6874  C C   . VAL D 1 129 ? 154.255 -14.312 68.672  1.000 26.820  ? 146 VAL DDD C   1 
ATOM 6875  O O   . VAL D 1 129 ? 154.812 -13.194 68.613  1.000 26.420  ? 146 VAL DDD O   1 
ATOM 6876  C CB  . VAL D 1 129 ? 155.025 -15.427 66.506  1.000 24.720  ? 146 VAL DDD CB  1 
ATOM 6877  C CG1 . VAL D 1 129 ? 155.985 -16.314 67.268  1.000 23.620  ? 146 VAL DDD CG1 1 
ATOM 6878  C CG2 . VAL D 1 129 ? 154.547 -16.136 65.248  1.000 25.280  ? 146 VAL DDD CG2 1 
ATOM 6879  N N   . GLY D 1 130 ? 153.970 -14.956 69.804  1.000 29.610  ? 147 GLY DDD N   1 
ATOM 6880  C CA  . GLY D 1 130 ? 154.091 -14.349 71.141  1.000 31.220  ? 147 GLY DDD CA  1 
ATOM 6881  C C   . GLY D 1 130 ? 154.669 -15.313 72.165  1.000 29.710  ? 147 GLY DDD C   1 
ATOM 6882  O O   . GLY D 1 130 ? 154.418 -16.541 72.048  1.000 27.340  ? 147 GLY DDD O   1 
ATOM 6883  N N   . GLY D 1 131 ? 155.407 -14.755 73.131  1.000 30.510  ? 148 GLY DDD N   1 
ATOM 6884  C CA  . GLY D 1 131 ? 155.864 -15.417 74.364  1.000 31.530  ? 148 GLY DDD CA  1 
ATOM 6885  C C   . GLY D 1 131 ? 154.757 -15.507 75.425  1.000 31.520  ? 148 GLY DDD C   1 
ATOM 6886  O O   . GLY D 1 131 ? 155.001 -16.077 76.516  1.000 32.920  ? 148 GLY DDD O   1 
ATOM 6887  N N   . GLU D 1 132 ? 153.580 -14.975 75.118  1.000 28.830  ? 149 GLU DDD N   1 
ATOM 6888  C CA  . GLU D 1 132 ? 152.383 -15.010 75.991  1.000 29.460  ? 149 GLU DDD CA  1 
ATOM 6889  C C   . GLU D 1 132 ? 151.165 -14.762 75.111  1.000 30.880  ? 149 GLU DDD C   1 
ATOM 6890  O O   . GLU D 1 132 ? 151.368 -14.471 73.892  1.000 36.660  ? 149 GLU DDD O   1 
ATOM 6891  C CB  . GLU D 1 132 ? 152.473 -13.927 77.060  1.000 28.670  ? 149 GLU DDD CB  1 
ATOM 6892  C CG  . GLU D 1 132 ? 153.366 -12.761 76.679  1.000 27.580  ? 149 GLU DDD CG  1 
ATOM 6893  C CD  . GLU D 1 132 ? 153.304 -11.601 77.653  1.000 29.290  ? 149 GLU DDD CD  1 
ATOM 6894  O OE1 . GLU D 1 132 ? 152.169 -11.204 78.054  1.000 30.000  ? 149 GLU DDD OE1 1 
ATOM 6895  O OE2 . GLU D 1 132 ? 154.361 -11.092 77.996  1.000 31.500  ? 149 GLU DDD OE2 1 
ATOM 6896  N N   . ALA D 1 133 ? 149.973 -14.828 75.694  1.000 28.780  ? 150 ALA DDD N   1 
ATOM 6897  C CA  . ALA D 1 133 ? 148.725 -14.600 74.944  1.000 31.920  ? 150 ALA DDD CA  1 
ATOM 6898  C C   . ALA D 1 133 ? 148.810 -13.273 74.188  1.000 30.880  ? 150 ALA DDD C   1 
ATOM 6899  O O   . ALA D 1 133 ? 149.357 -12.306 74.730  1.000 29.390  ? 150 ALA DDD O   1 
ATOM 6900  C CB  . ALA D 1 133 ? 147.542 -14.613 75.866  1.000 35.130  ? 150 ALA DDD CB  1 
ATOM 6901  N N   . LEU D 1 134 ? 148.251 -13.241 72.977  1.000 30.820  ? 151 LEU DDD N   1 
ATOM 6902  C CA  . LEU D 1 134 ? 147.925 -11.965 72.300  1.000 31.310  ? 151 LEU DDD CA  1 
ATOM 6903  C C   . LEU D 1 134 ? 147.032 -11.149 73.235  1.000 32.170  ? 151 LEU DDD C   1 
ATOM 6904  O O   . LEU D 1 134 ? 146.067 -11.716 73.789  1.000 32.590  ? 151 LEU DDD O   1 
ATOM 6905  C CB  . LEU D 1 134 ? 147.195 -12.265 70.993  1.000 31.730  ? 151 LEU DDD CB  1 
ATOM 6906  C CG  . LEU D 1 134 ? 146.859 -11.059 70.118  1.000 28.910  ? 151 LEU DDD CG  1 
ATOM 6907  C CD1 . LEU D 1 134 ? 148.120 -10.355 69.665  1.000 28.490  ? 151 LEU DDD CD1 1 
ATOM 6908  C CD2 . LEU D 1 134 ? 146.036 -11.495 68.921  1.000 27.930  ? 151 LEU DDD CD2 1 
ATOM 6909  N N   . GLU D 1 135 ? 147.341 -9.866  73.393  1.000 32.330  ? 152 GLU DDD N   1 
ATOM 6910  C CA  . GLU D 1 135 ? 146.540 -8.931  74.215  1.000 30.450  ? 152 GLU DDD CA  1 
ATOM 6911  C C   . GLU D 1 135 ? 145.591 -8.151  73.314  1.000 25.470  ? 152 GLU DDD C   1 
ATOM 6912  O O   . GLU D 1 135 ? 146.059 -7.567  72.332  1.000 22.290  ? 152 GLU DDD O   1 
ATOM 6913  C CB  . GLU D 1 135 ? 147.483 -8.035  75.005  1.000 34.030  ? 152 GLU DDD CB  1 
ATOM 6914  C CG  . GLU D 1 135 ? 148.324 -8.799  76.009  1.000 33.410  ? 152 GLU DDD CG  1 
ATOM 6915  C CD  . GLU D 1 135 ? 149.207 -7.898  76.831  1.000 33.220  ? 152 GLU DDD CD  1 
ATOM 6916  O OE1 . GLU D 1 135 ? 150.353 -7.642  76.416  1.000 32.180  ? 152 GLU DDD OE1 1 
ATOM 6917  O OE2 . GLU D 1 135 ? 148.715 -7.441  77.869  1.000 35.670  ? 152 GLU DDD OE2 1 
ATOM 6918  N N   . LEU D 1 136 ? 144.304 -8.160  73.659  1.000 26.480  ? 153 LEU DDD N   1 
ATOM 6919  C CA  . LEU D 1 136 ? 143.215 -7.575  72.834  1.000 29.890  ? 153 LEU DDD CA  1 
ATOM 6920  C C   . LEU D 1 136 ? 142.682 -6.274  73.451  1.000 29.600  ? 153 LEU DDD C   1 
ATOM 6921  O O   . LEU D 1 136 ? 142.516 -6.203  74.683  1.000 29.750  ? 153 LEU DDD O   1 
ATOM 6922  C CB  . LEU D 1 136 ? 142.063 -8.573  72.711  1.000 32.080  ? 153 LEU DDD CB  1 
ATOM 6923  C CG  . LEU D 1 136 ? 142.416 -9.955  72.176  1.000 34.940  ? 153 LEU DDD CG  1 
ATOM 6924  C CD1 . LEU D 1 136 ? 141.185 -10.857 72.217  1.000 36.850  ? 153 LEU DDD CD1 1 
ATOM 6925  C CD2 . LEU D 1 136 ? 142.987 -9.852  70.776  1.000 36.130  ? 153 LEU DDD CD2 1 
ATOM 6926  N N   . GLN D 1 137 ? 142.389 -5.308  72.576  1.000 26.720  ? 154 GLN DDD N   1 
ATOM 6927  C CA  . GLN D 1 137 ? 141.549 -4.121  72.847  1.000 25.050  ? 154 GLN DDD CA  1 
ATOM 6928  C C   . GLN D 1 137 ? 140.192 -4.339  72.177  1.000 25.400  ? 154 GLN DDD C   1 
ATOM 6929  O O   . GLN D 1 137 ? 140.158 -4.735  71.011  1.000 24.700  ? 154 GLN DDD O   1 
ATOM 6930  C CB  . GLN D 1 137 ? 142.218 -2.871  72.288  1.000 24.870  ? 154 GLN DDD CB  1 
ATOM 6931  C CG  . GLN D 1 137 ? 141.331 -1.641  72.309  1.000 24.390  ? 154 GLN DDD CG  1 
ATOM 6932  C CD  . GLN D 1 137 ? 141.013 -1.259  73.723  1.000 24.480  ? 154 GLN DDD CD  1 
ATOM 6933  O OE1 . GLN D 1 137 ? 141.866 -1.296  74.602  1.000 25.810  ? 154 GLN DDD OE1 1 
ATOM 6934  N NE2 . GLN D 1 137 ? 139.767 -0.899  73.948  1.000 24.180  ? 154 GLN DDD NE2 1 
ATOM 6935  N N   . GLY D 1 138 ? 139.109 -4.100  72.898  1.000 26.400  ? 155 GLY DDD N   1 
ATOM 6936  C CA  . GLY D 1 138 ? 137.764 -4.128  72.314  1.000 27.880  ? 155 GLY DDD CA  1 
ATOM 6937  C C   . GLY D 1 138 ? 137.468 -2.833  71.590  1.000 30.120  ? 155 GLY DDD C   1 
ATOM 6938  O O   . GLY D 1 138 ? 137.733 -1.741  72.149  1.000 37.990  ? 155 GLY DDD O   1 
ATOM 6939  N N   . VAL D 1 139 ? 136.919 -2.942  70.388  1.000 29.910  ? 156 VAL DDD N   1 
ATOM 6940  C CA  . VAL D 1 139 ? 136.306 -1.806  69.649  1.000 29.800  ? 156 VAL DDD CA  1 
ATOM 6941  C C   . VAL D 1 139 ? 135.048 -2.325  68.967  1.000 28.510  ? 156 VAL DDD C   1 
ATOM 6942  O O   . VAL D 1 139 ? 135.125 -3.385  68.336  1.000 30.460  ? 156 VAL DDD O   1 
ATOM 6943  C CB  . VAL D 1 139 ? 137.251 -1.198  68.597  1.000 32.620  ? 156 VAL DDD CB  1 
ATOM 6944  C CG1 . VAL D 1 139 ? 136.632 0.057   67.991  1.000 32.150  ? 156 VAL DDD CG1 1 
ATOM 6945  C CG2 . VAL D 1 139 ? 138.655 -0.929  69.132  1.000 32.000  ? 156 VAL DDD CG2 1 
ATOM 6946  N N   . LEU D 1 140 ? 133.958 -1.576  69.073  1.000 27.590  ? 157 LEU DDD N   1 
ATOM 6947  C CA  . LEU D 1 140 ? 132.610 -2.016  68.634  1.000 28.840  ? 157 LEU DDD CA  1 
ATOM 6948  C C   . LEU D 1 140 ? 132.184 -1.192  67.422  1.000 26.210  ? 157 LEU DDD C   1 
ATOM 6949  O O   . LEU D 1 140 ? 132.374 0.041   67.452  1.000 25.950  ? 157 LEU DDD O   1 
ATOM 6950  C CB  . LEU D 1 140 ? 131.621 -1.844  69.803  1.000 30.640  ? 157 LEU DDD CB  1 
ATOM 6951  C CG  . LEU D 1 140 ? 131.898 -2.721  71.027  1.000 32.950  ? 157 LEU DDD CG  1 
ATOM 6952  C CD1 . LEU D 1 140 ? 130.801 -2.562  72.059  1.000 36.140  ? 157 LEU DDD CD1 1 
ATOM 6953  C CD2 . LEU D 1 140 ? 132.057 -4.193  70.660  1.000 31.900  ? 157 LEU DDD CD2 1 
ATOM 6954  N N   . PHE D 1 141 ? 131.601 -1.830  66.416  1.000 25.360  ? 158 PHE DDD N   1 
ATOM 6955  C CA  . PHE D 1 141 ? 130.960 -1.080  65.312  1.000 26.910  ? 158 PHE DDD CA  1 
ATOM 6956  C C   . PHE D 1 141 ? 129.756 -0.339  65.897  1.000 27.000  ? 158 PHE DDD C   1 
ATOM 6957  O O   . PHE D 1 141 ? 129.580 0.847   65.657  1.000 28.900  ? 158 PHE DDD O   1 
ATOM 6958  C CB  . PHE D 1 141 ? 130.560 -1.986  64.145  1.000 26.350  ? 158 PHE DDD CB  1 
ATOM 6959  C CG  . PHE D 1 141 ? 129.858 -1.244  63.054  1.000 24.710  ? 158 PHE DDD CG  1 
ATOM 6960  C CD1 . PHE D 1 141 ? 130.569 -0.408  62.211  1.000 26.560  ? 158 PHE DDD CD1 1 
ATOM 6961  C CD2 . PHE D 1 141 ? 128.475 -1.314  62.918  1.000 24.640  ? 158 PHE DDD CD2 1 
ATOM 6962  C CE1 . PHE D 1 141 ? 129.927 0.315   61.213  1.000 26.960  ? 158 PHE DDD CE1 1 
ATOM 6963  C CE2 . PHE D 1 141 ? 127.834 -0.585  61.936  1.000 26.890  ? 158 PHE DDD CE2 1 
ATOM 6964  C CZ  . PHE D 1 141 ? 128.557 0.229   61.083  1.000 27.490  ? 158 PHE DDD CZ  1 
ATOM 6965  N N   . ASN D 1 142 ? 128.957 -1.049  66.681  1.000 28.970  ? 159 ASN DDD N   1 
ATOM 6966  C CA  . ASN D 1 142 ? 127.713 -0.534  67.309  1.000 29.190  ? 159 ASN DDD CA  1 
ATOM 6967  C C   . ASN D 1 142 ? 127.722 -0.988  68.762  1.000 29.250  ? 159 ASN DDD C   1 
ATOM 6968  O O   . ASN D 1 142 ? 127.711 -2.186  68.943  1.000 32.840  ? 159 ASN DDD O   1 
ATOM 6969  C CB  . ASN D 1 142 ? 126.490 -1.074  66.566  1.000 28.350  ? 159 ASN DDD CB  1 
ATOM 6970  C CG  . ASN D 1 142 ? 125.175 -0.678  67.170  1.000 28.200  ? 159 ASN DDD CG  1 
ATOM 6971  O OD1 . ASN D 1 142 ? 125.126 0.160   68.073  1.000 33.000  ? 159 ASN DDD OD1 1 
ATOM 6972  N ND2 . ASN D 1 142 ? 124.115 -1.249  66.621  1.000 28.050  ? 159 ASN DDD ND2 1 
ATOM 6973  N N   . TYR D 1 143 ? 127.783 -0.088  69.741  1.000 31.720  ? 160 TYR DDD N   1 
ATOM 6974  C CA  . TYR D 1 143 ? 127.950 -0.458  71.179  1.000 34.190  ? 160 TYR DDD CA  1 
ATOM 6975  C C   . TYR D 1 143 ? 126.681 -1.154  71.693  1.000 30.480  ? 160 TYR DDD C   1 
ATOM 6976  O O   . TYR D 1 143 ? 126.840 -1.972  72.641  1.000 29.200  ? 160 TYR DDD O   1 
ATOM 6977  C CB  . TYR D 1 143 ? 128.385 0.727   72.062  1.000 37.940  ? 160 TYR DDD CB  1 
ATOM 6978  C CG  . TYR D 1 143 ? 127.260 1.561   72.624  1.000 38.860  ? 160 TYR DDD CG  1 
ATOM 6979  C CD1 . TYR D 1 143 ? 126.574 2.450   71.813  1.000 40.490  ? 160 TYR DDD CD1 1 
ATOM 6980  C CD2 . TYR D 1 143 ? 126.878 1.469   73.952  1.000 36.550  ? 160 TYR DDD CD2 1 
ATOM 6981  C CE1 . TYR D 1 143 ? 125.530 3.214   72.296  1.000 38.010  ? 160 TYR DDD CE1 1 
ATOM 6982  C CE2 . TYR D 1 143 ? 125.833 2.224   74.453  1.000 34.000  ? 160 TYR DDD CE2 1 
ATOM 6983  C CZ  . TYR D 1 143 ? 125.145 3.077   73.611  1.000 35.410  ? 160 TYR DDD CZ  1 
ATOM 6984  O OH  . TYR D 1 143 ? 124.100 3.837   74.024  1.000 37.760  ? 160 TYR DDD OH  1 
ATOM 6985  N N   . ARG D 1 144 ? 125.525 -0.929  71.049  1.000 29.180  ? 161 ARG DDD N   1 
ATOM 6986  C CA  . ARG D 1 144 ? 124.239 -1.592  71.411  1.000 33.760  ? 161 ARG DDD CA  1 
ATOM 6987  C C   . ARG D 1 144 ? 124.142 -3.015  70.813  1.000 32.060  ? 161 ARG DDD C   1 
ATOM 6988  O O   . ARG D 1 144 ? 123.203 -3.723  71.201  1.000 29.630  ? 161 ARG DDD O   1 
ATOM 6989  C CB  . ARG D 1 144 ? 123.048 -0.674  71.111  1.000 37.490  ? 161 ARG DDD CB  1 
ATOM 6990  C CG  . ARG D 1 144 ? 122.764 0.324   72.255  1.000 44.400  ? 161 ARG DDD CG  1 
ATOM 6991  C CD  . ARG D 1 144 ? 121.921 1.573   71.971  1.000 46.770  ? 161 ARG DDD CD  1 
ATOM 6992  N NE  . ARG D 1 144 ? 122.522 2.148   70.768  1.000 60.520  ? 161 ARG DDD NE  1 
ATOM 6993  C CZ  . ARG D 1 144 ? 121.949 2.946   69.867  1.000 65.010  ? 161 ARG DDD CZ  1 
ATOM 6994  N NH1 . ARG D 1 144 ? 120.694 3.355   70.009  1.000 66.560  ? 161 ARG DDD NH1 1 
ATOM 6995  N NH2 . ARG D 1 144 ? 122.674 3.329   68.826  1.000 61.480  ? 161 ARG DDD NH2 1 
ATOM 6996  N N   . THR D 1 145 ? 125.110 -3.466  69.998  1.000 31.020  ? 162 THR DDD N   1 
ATOM 6997  C CA  . THR D 1 145 ? 125.218 -4.875  69.508  1.000 30.010  ? 162 THR DDD CA  1 
ATOM 6998  C C   . THR D 1 145 ? 125.309 -5.799  70.720  1.000 27.910  ? 162 THR DDD C   1 
ATOM 6999  O O   . THR D 1 145 ? 126.219 -5.555  71.516  1.000 32.320  ? 162 THR DDD O   1 
ATOM 7000  C CB  . THR D 1 145 ? 126.482 -5.185  68.679  1.000 33.300  ? 162 THR DDD CB  1 
ATOM 7001  O OG1 . THR D 1 145 ? 126.621 -4.427  67.472  1.000 38.840  ? 162 THR DDD OG1 1 
ATOM 7002  C CG2 . THR D 1 145 ? 126.544 -6.646  68.278  1.000 34.560  ? 162 THR DDD CG2 1 
ATOM 7003  N N   . LYS D 1 146 ? 124.430 -6.800  70.840  1.000 26.030  ? 163 LYS DDD N   1 
ATOM 7004  C CA  . LYS D 1 146 ? 124.479 -7.822  71.908  1.000 27.090  ? 163 LYS DDD CA  1 
ATOM 7005  C C   . LYS D 1 146 ? 125.236 -9.042  71.414  1.000 27.440  ? 163 LYS DDD C   1 
ATOM 7006  O O   . LYS D 1 146 ? 124.655 -9.833  70.659  1.000 31.820  ? 163 LYS DDD O   1 
ATOM 7007  C CB  . LYS D 1 146 ? 123.075 -8.268  72.321  1.000 31.190  ? 163 LYS DDD CB  1 
ATOM 7008  C CG  . LYS D 1 146 ? 123.060 -9.348  73.402  1.000 33.710  ? 163 LYS DDD CG  1 
ATOM 7009  C CD  . LYS D 1 146 ? 121.682 -9.731  73.852  1.000 37.920  ? 163 LYS DDD CD  1 
ATOM 7010  C CE  . LYS D 1 146 ? 121.636 -11.070 74.558  1.000 44.330  ? 163 LYS DDD CE  1 
ATOM 7011  N NZ  . LYS D 1 146 ? 120.241 -11.584 74.607  1.000 51.180  ? 163 LYS DDD NZ  1 
ATOM 7012  N N   . TYR D 1 147 ? 126.476 -9.235  71.844  1.000 30.370  ? 164 TYR DDD N   1 
ATOM 7013  C CA  . TYR D 1 147 ? 127.307 -10.396 71.401  1.000 30.220  ? 164 TYR DDD CA  1 
ATOM 7014  C C   . TYR D 1 147 ? 126.760 -11.635 72.101  1.000 33.620  ? 164 TYR DDD C   1 
ATOM 7015  O O   . TYR D 1 147 ? 126.369 -11.589 73.258  1.000 42.710  ? 164 TYR DDD O   1 
ATOM 7016  C CB  . TYR D 1 147 ? 128.808 -10.111 71.546  1.000 27.860  ? 164 TYR DDD CB  1 
ATOM 7017  C CG  . TYR D 1 147 ? 129.294 -9.171  70.470  1.000 27.900  ? 164 TYR DDD CG  1 
ATOM 7018  C CD1 . TYR D 1 147 ? 129.199 -7.804  70.626  1.000 30.040  ? 164 TYR DDD CD1 1 
ATOM 7019  C CD2 . TYR D 1 147 ? 129.729 -9.628  69.249  1.000 29.500  ? 164 TYR DDD CD2 1 
ATOM 7020  C CE1 . TYR D 1 147 ? 129.565 -6.927  69.626  1.000 32.520  ? 164 TYR DDD CE1 1 
ATOM 7021  C CE2 . TYR D 1 147 ? 130.108 -8.761  68.235  1.000 33.280  ? 164 TYR DDD CE2 1 
ATOM 7022  C CZ  . TYR D 1 147 ? 130.022 -7.395  68.415  1.000 34.040  ? 164 TYR DDD CZ  1 
ATOM 7023  O OH  . TYR D 1 147 ? 130.381 -6.491  67.441  1.000 42.520  ? 164 TYR DDD OH  1 
ATOM 7024  N N   . PRO D 1 148 ? 126.675 -12.783 71.407  1.000 37.360  ? 165 PRO DDD N   1 
ATOM 7025  C CA  . PRO D 1 148 ? 125.845 -13.895 71.841  1.000 36.210  ? 165 PRO DDD CA  1 
ATOM 7026  C C   . PRO D 1 148 ? 126.522 -14.694 72.955  1.000 36.010  ? 165 PRO DDD C   1 
ATOM 7027  O O   . PRO D 1 148 ? 127.739 -14.818 72.992  1.000 37.790  ? 165 PRO DDD O   1 
ATOM 7028  C CB  . PRO D 1 148 ? 125.735 -14.755 70.588  1.000 37.220  ? 165 PRO DDD CB  1 
ATOM 7029  C CG  . PRO D 1 148 ? 127.100 -14.597 69.950  1.000 38.930  ? 165 PRO DDD CG  1 
ATOM 7030  C CD  . PRO D 1 148 ? 127.487 -13.158 70.242  1.000 41.180  ? 165 PRO DDD CD  1 
ATOM 7031  N N   . ASP D 1 149 ? 125.679 -15.189 73.843  1.000 36.960  ? 166 ASP DDD N   1 
ATOM 7032  C CA  . ASP D 1 149 ? 125.970 -16.226 74.859  1.000 38.150  ? 166 ASP DDD CA  1 
ATOM 7033  C C   . ASP D 1 149 ? 126.991 -17.249 74.326  1.000 30.030  ? 166 ASP DDD C   1 
ATOM 7034  O O   . ASP D 1 149 ? 126.681 -17.903 73.351  1.000 28.820  ? 166 ASP DDD O   1 
ATOM 7035  C CB  . ASP D 1 149 ? 124.641 -16.854 75.270  1.000 44.750  ? 166 ASP DDD CB  1 
ATOM 7036  C CG  . ASP D 1 149 ? 124.648 -17.305 76.703  1.000 51.020  ? 166 ASP DDD CG  1 
ATOM 7037  O OD1 . ASP D 1 149 ? 125.578 -18.092 77.034  1.000 56.800  ? 166 ASP DDD OD1 1 
ATOM 7038  O OD2 . ASP D 1 149 ? 123.752 -16.819 77.470  1.000 56.500  ? 166 ASP DDD OD2 1 
ATOM 7039  N N   . GLY D 1 150 ? 128.149 -17.370 74.944  1.000 27.520  ? 167 GLY DDD N   1 
ATOM 7040  C CA  . GLY D 1 150 ? 129.148 -18.398 74.571  1.000 28.670  ? 167 GLY DDD CA  1 
ATOM 7041  C C   . GLY D 1 150 ? 130.425 -17.825 73.974  1.000 28.360  ? 167 GLY DDD C   1 
ATOM 7042  O O   . GLY D 1 150 ? 131.389 -18.595 73.773  1.000 24.900  ? 167 GLY DDD O   1 
ATOM 7043  N N   . THR D 1 151 ? 130.417 -16.528 73.678  1.000 29.290  ? 168 THR DDD N   1 
ATOM 7044  C CA  . THR D 1 151 ? 131.575 -15.742 73.185  1.000 28.940  ? 168 THR DDD CA  1 
ATOM 7045  C C   . THR D 1 151 ? 132.019 -14.797 74.298  1.000 31.430  ? 168 THR DDD C   1 
ATOM 7046  O O   . THR D 1 151 ? 131.148 -14.376 75.087  1.000 33.160  ? 168 THR DDD O   1 
ATOM 7047  C CB  . THR D 1 151 ? 131.179 -14.919 71.956  1.000 29.290  ? 168 THR DDD CB  1 
ATOM 7048  O OG1 . THR D 1 151 ? 130.174 -13.978 72.324  1.000 28.090  ? 168 THR DDD OG1 1 
ATOM 7049  C CG2 . THR D 1 151 ? 130.628 -15.784 70.843  1.000 31.160  ? 168 THR DDD CG2 1 
ATOM 7050  N N   . ILE D 1 152 ? 133.307 -14.480 74.359  1.000 30.990  ? 169 ILE DDD N   1 
ATOM 7051  C CA  . ILE D 1 152 ? 133.857 -13.469 75.304  1.000 27.460  ? 169 ILE DDD CA  1 
ATOM 7052  C C   . ILE D 1 152 ? 133.891 -12.122 74.564  1.000 28.200  ? 169 ILE DDD C   1 
ATOM 7053  O O   . ILE D 1 152 ? 134.581 -12.004 73.543  1.000 27.460  ? 169 ILE DDD O   1 
ATOM 7054  C CB  . ILE D 1 152 ? 135.240 -13.958 75.757  1.000 23.790  ? 169 ILE DDD CB  1 
ATOM 7055  C CG1 . ILE D 1 152 ? 135.121 -15.227 76.583  1.000 22.760  ? 169 ILE DDD CG1 1 
ATOM 7056  C CG2 . ILE D 1 152 ? 136.007 -12.906 76.508  1.000 24.670  ? 169 ILE DDD CG2 1 
ATOM 7057  C CD1 . ILE D 1 152 ? 136.406 -15.979 76.700  1.000 24.070  ? 169 ILE DDD CD1 1 
ATOM 7058  N N   . PHE D 1 153 ? 133.121 -11.146 75.033  1.000 29.370  ? 170 PHE DDD N   1 
ATOM 7059  C CA  . PHE D 1 153 ? 132.968 -9.845  74.343  1.000 31.770  ? 170 PHE DDD CA  1 
ATOM 7060  C C   . PHE D 1 153 ? 133.216 -8.687  75.301  1.000 33.200  ? 170 PHE DDD C   1 
ATOM 7061  O O   . PHE D 1 153 ? 133.236 -8.876  76.503  1.000 30.720  ? 170 PHE DDD O   1 
ATOM 7062  C CB  . PHE D 1 153 ? 131.570 -9.764  73.754  1.000 32.620  ? 170 PHE DDD CB  1 
ATOM 7063  C CG  . PHE D 1 153 ? 130.452 -10.051 74.728  1.000 33.860  ? 170 PHE DDD CG  1 
ATOM 7064  C CD1 . PHE D 1 153 ? 130.077 -11.353 75.013  1.000 34.560  ? 170 PHE DDD CD1 1 
ATOM 7065  C CD2 . PHE D 1 153 ? 129.759 -9.014  75.321  1.000 35.850  ? 170 PHE DDD CD2 1 
ATOM 7066  C CE1 . PHE D 1 153 ? 129.043 -11.612 75.899  1.000 36.170  ? 170 PHE DDD CE1 1 
ATOM 7067  C CE2 . PHE D 1 153 ? 128.696 -9.280  76.174  1.000 36.840  ? 170 PHE DDD CE2 1 
ATOM 7068  C CZ  . PHE D 1 153 ? 128.364 -10.575 76.494  1.000 35.540  ? 170 PHE DDD CZ  1 
ATOM 7069  N N   . PRO D 1 154 ? 133.452 -7.460  74.789  1.000 35.870  ? 171 PRO DDD N   1 
ATOM 7070  C CA  . PRO D 1 154 ? 133.543 -6.264  75.619  1.000 36.180  ? 171 PRO DDD CA  1 
ATOM 7071  C C   . PRO D 1 154 ? 132.347 -6.114  76.546  1.000 37.470  ? 171 PRO DDD C   1 
ATOM 7072  O O   . PRO D 1 154 ? 131.234 -6.117  76.053  1.000 38.420  ? 171 PRO DDD O   1 
ATOM 7073  C CB  . PRO D 1 154 ? 133.539 -5.127  74.599  1.000 38.840  ? 171 PRO DDD CB  1 
ATOM 7074  C CG  . PRO D 1 154 ? 134.246 -5.745  73.416  1.000 39.270  ? 171 PRO DDD CG  1 
ATOM 7075  C CD  . PRO D 1 154 ? 133.700 -7.156  73.370  1.000 39.290  ? 171 PRO DDD CD  1 
ATOM 7076  N N   . LYS D 1 155 ? 132.628 -6.011  77.845  1.000 39.940  ? 172 LYS DDD N   1 
ATOM 7077  C CA  . LYS D 1 155 ? 131.603 -5.870  78.906  1.000 42.380  ? 172 LYS DDD CA  1 
ATOM 7078  C C   . LYS D 1 155 ? 131.531 -4.392  79.280  1.000 38.380  ? 172 LYS DDD C   1 
ATOM 7079  O O   . LYS D 1 155 ? 132.553 -3.729  79.166  1.000 37.820  ? 172 LYS DDD O   1 
ATOM 7080  C CB  . LYS D 1 155 ? 131.942 -6.762  80.105  1.000 47.560  ? 172 LYS DDD CB  1 
ATOM 7081  C CG  . LYS D 1 155 ? 131.918 -8.260  79.835  1.000 57.220  ? 172 LYS DDD CG  1 
ATOM 7082  C CD  . LYS D 1 155 ? 131.322 -9.126  80.963  1.000 73.740  ? 172 LYS DDD CD  1 
ATOM 7083  C CE  . LYS D 1 155 ? 130.569 -10.352 80.470  1.000 83.090  ? 172 LYS DDD CE  1 
ATOM 7084  N NZ  . LYS D 1 155 ? 131.488 -11.476 80.160  1.000 93.850  ? 172 LYS DDD NZ  1 
ATOM 7085  N N   . ASN D 1 156 ? 130.347 -3.917  79.666  1.000 38.360  ? 173 ASN DDD N   1 
ATOM 7086  C CA  . ASN D 1 156 ? 130.077 -2.524  80.103  1.000 37.060  ? 173 ASN DDD CA  1 
ATOM 7087  C C   . ASN D 1 156 ? 130.300 -1.584  78.931  1.000 34.310  ? 173 ASN DDD C   1 
ATOM 7088  O O   . ASN D 1 156 ? 130.936 -0.526  79.124  1.000 36.490  ? 173 ASN DDD O   1 
ATOM 7089  C CB  . ASN D 1 156 ? 130.938 -2.126  81.303  1.000 37.920  ? 173 ASN DDD CB  1 
ATOM 7090  C CG  . ASN D 1 156 ? 130.640 -2.997  82.494  1.000 37.180  ? 173 ASN DDD CG  1 
ATOM 7091  O OD1 . ASN D 1 156 ? 129.469 -3.200  82.831  1.000 35.270  ? 173 ASN DDD OD1 1 
ATOM 7092  N ND2 . ASN D 1 156 ? 131.687 -3.537  83.091  1.000 37.240  ? 173 ASN DDD ND2 1 
ATOM 7093  N N   . ALA D 1 157 ? 129.789 -1.968  77.771  1.000 33.010  ? 174 ALA DDD N   1 
ATOM 7094  C CA  . ALA D 1 157 ? 129.866 -1.161  76.537  1.000 34.930  ? 174 ALA DDD CA  1 
ATOM 7095  C C   . ALA D 1 157 ? 129.209 0.185   76.799  1.000 32.630  ? 174 ALA DDD C   1 
ATOM 7096  O O   . ALA D 1 157 ? 128.111 0.216   77.361  1.000 36.220  ? 174 ALA DDD O   1 
ATOM 7097  C CB  . ALA D 1 157 ? 129.182 -1.867  75.395  1.000 42.080  ? 174 ALA DDD CB  1 
ATOM 7098  N N   . THR D 1 158 ? 129.897 1.249   76.426  1.000 29.310  ? 175 THR DDD N   1 
ATOM 7099  C CA  . THR D 1 158 ? 129.370 2.627   76.385  1.000 27.940  ? 175 THR DDD CA  1 
ATOM 7100  C C   . THR D 1 158 ? 129.475 3.105   74.931  1.000 27.290  ? 175 THR DDD C   1 
ATOM 7101  O O   . THR D 1 158 ? 130.146 2.424   74.108  1.000 25.230  ? 175 THR DDD O   1 
ATOM 7102  C CB  . THR D 1 158 ? 130.109 3.454   77.437  1.000 27.320  ? 175 THR DDD CB  1 
ATOM 7103  O OG1 . THR D 1 158 ? 131.433 3.779   77.022  1.000 26.380  ? 175 THR DDD OG1 1 
ATOM 7104  C CG2 . THR D 1 158 ? 130.212 2.695   78.735  1.000 29.110  ? 175 THR DDD CG2 1 
ATOM 7105  N N   . VAL D 1 159 ? 128.848 4.219   74.597  1.000 26.100  ? 176 VAL DDD N   1 
ATOM 7106  C CA  . VAL D 1 159 ? 129.028 4.792   73.246  1.000 28.240  ? 176 VAL DDD CA  1 
ATOM 7107  C C   . VAL D 1 159 ? 130.534 4.941   72.990  1.000 30.520  ? 176 VAL DDD C   1 
ATOM 7108  O O   . VAL D 1 159 ? 130.943 4.676   71.851  1.000 37.990  ? 176 VAL DDD O   1 
ATOM 7109  C CB  . VAL D 1 159 ? 128.267 6.113   73.078  1.000 30.700  ? 176 VAL DDD CB  1 
ATOM 7110  C CG1 . VAL D 1 159 ? 129.050 7.304   73.609  1.000 31.910  ? 176 VAL DDD CG1 1 
ATOM 7111  C CG2 . VAL D 1 159 ? 127.876 6.339   71.625  1.000 32.680  ? 176 VAL DDD CG2 1 
ATOM 7112  N N   . GLN D 1 160 ? 131.351 5.301   73.990  1.000 29.270  ? 177 GLN DDD N   1 
ATOM 7113  C CA  . GLN D 1 160 ? 132.816 5.484   73.790  1.000 30.640  ? 177 GLN DDD CA  1 
ATOM 7114  C C   . GLN D 1 160 ? 133.415 4.176   73.267  1.000 31.030  ? 177 GLN DDD C   1 
ATOM 7115  O O   . GLN D 1 160 ? 134.422 4.246   72.567  1.000 33.300  ? 177 GLN DDD O   1 
ATOM 7116  C CB  . GLN D 1 160 ? 133.538 5.933   75.057  1.000 32.840  ? 177 GLN DDD CB  1 
ATOM 7117  C CG  . GLN D 1 160 ? 133.113 7.318   75.541  1.000 38.550  ? 177 GLN DDD CG  1 
ATOM 7118  C CD  . GLN D 1 160 ? 133.227 8.429   74.501  1.000 44.950  ? 177 GLN DDD CD  1 
ATOM 7119  O OE1 . GLN D 1 160 ? 134.259 8.581   73.806  1.000 43.830  ? 177 GLN DDD OE1 1 
ATOM 7120  N NE2 . GLN D 1 160 ? 132.181 9.251   74.393  1.000 38.690  ? 177 GLN DDD NE2 1 
ATOM 7121  N N   . SER D 1 161 ? 132.810 3.024   73.573  1.000 29.770  ? 178 SER DDD N   1 
ATOM 7122  C CA  . SER D 1 161 ? 133.306 1.699   73.122  1.000 30.820  ? 178 SER DDD CA  1 
ATOM 7123  C C   . SER D 1 161 ? 133.440 1.684   71.590  1.000 31.740  ? 178 SER DDD C   1 
ATOM 7124  O O   . SER D 1 161 ? 134.387 1.022   71.100  1.000 34.650  ? 178 SER DDD O   1 
ATOM 7125  C CB  . SER D 1 161 ? 132.434 0.586   73.633  1.000 32.750  ? 178 SER DDD CB  1 
ATOM 7126  O OG  . SER D 1 161 ? 132.482 0.523   75.055  1.000 33.670  ? 178 SER DDD OG  1 
ATOM 7127  N N   . GLN D 1 162 ? 132.564 2.424   70.882  1.000 27.450  ? 179 GLN DDD N   1 
ATOM 7128  C CA  . GLN D 1 162 ? 132.500 2.553   69.395  1.000 22.340  ? 179 GLN DDD CA  1 
ATOM 7129  C C   . GLN D 1 162 ? 133.777 3.176   68.829  1.000 20.940  ? 179 GLN DDD C   1 
ATOM 7130  O O   . GLN D 1 162 ? 134.019 2.973   67.651  1.000 21.020  ? 179 GLN DDD O   1 
ATOM 7131  C CB  . GLN D 1 162 ? 131.288 3.388   68.961  1.000 20.940  ? 179 GLN DDD CB  1 
ATOM 7132  C CG  . GLN D 1 162 ? 130.052 2.560   68.618  1.000 20.540  ? 179 GLN DDD CG  1 
ATOM 7133  C CD  . GLN D 1 162 ? 128.746 3.326   68.661  1.000 20.330  ? 179 GLN DDD CD  1 
ATOM 7134  O OE1 . GLN D 1 162 ? 127.649 2.754   68.784  1.000 17.900  ? 179 GLN DDD OE1 1 
ATOM 7135  N NE2 . GLN D 1 162 ? 128.851 4.646   68.529  1.000 21.380  ? 179 GLN DDD NE2 1 
ATOM 7136  N N   . VAL D 1 163 ? 134.540 3.965   69.590  1.000 21.530  ? 180 VAL DDD N   1 
ATOM 7137  C CA  . VAL D 1 163 ? 135.766 4.646   69.053  1.000 21.920  ? 180 VAL DDD CA  1 
ATOM 7138  C C   . VAL D 1 163 ? 136.999 4.183   69.816  1.000 22.710  ? 180 VAL DDD C   1 
ATOM 7139  O O   . VAL D 1 163 ? 137.987 3.804   69.159  1.000 24.070  ? 180 VAL DDD O   1 
ATOM 7140  C CB  . VAL D 1 163 ? 135.667 6.181   69.062  1.000 21.650  ? 180 VAL DDD CB  1 
ATOM 7141  C CG1 . VAL D 1 163 ? 134.607 6.666   68.087  1.000 23.360  ? 180 VAL DDD CG1 1 
ATOM 7142  C CG2 . VAL D 1 163 ? 135.412 6.771   70.425  1.000 21.270  ? 180 VAL DDD CG2 1 
ATOM 7143  N N   . MET D 1 164 ? 136.906 4.176   71.140  1.000 24.810  ? 181 MET DDD N   1 
ATOM 7144  C CA  . MET D 1 164 ? 137.948 3.658   72.056  1.000 28.720  ? 181 MET DDD CA  1 
ATOM 7145  C C   . MET D 1 164 ? 137.444 3.696   73.506  1.000 30.390  ? 181 MET DDD C   1 
ATOM 7146  O O   . MET D 1 164 ? 136.910 4.757   73.951  1.000 31.170  ? 181 MET DDD O   1 
ATOM 7147  C CB  . MET D 1 164 ? 139.220 4.502   71.950  1.000 30.540  ? 181 MET DDD CB  1 
ATOM 7148  C CG  . MET D 1 164 ? 140.383 3.927   72.735  1.000 31.420  ? 181 MET DDD CG  1 
ATOM 7149  S SD  . MET D 1 164 ? 140.827 2.307   72.076  1.000 32.430  ? 181 MET DDD SD  1 
ATOM 7150  C CE  . MET D 1 164 ? 142.032 1.798   73.292  1.000 38.630  ? 181 MET DDD CE  1 
ATOM 7151  N N   . ASN D 1 165 ? 137.644 2.607   74.241  1.000 30.410  ? 182 ASN DDD N   1 
ATOM 7152  C CA  . ASN D 1 165 ? 137.247 2.516   75.675  1.000 31.580  ? 182 ASN DDD CA  1 
ATOM 7153  C C   . ASN D 1 165 ? 138.200 1.549   76.387  1.000 32.230  ? 182 ASN DDD C   1 
ATOM 7154  O O   . ASN D 1 165 ? 138.057 0.355   76.198  1.000 37.850  ? 182 ASN DDD O   1 
ATOM 7155  C CB  . ASN D 1 165 ? 135.776 2.118   75.781  1.000 31.260  ? 182 ASN DDD CB  1 
ATOM 7156  C CG  . ASN D 1 165 ? 135.334 1.786   77.183  1.000 29.260  ? 182 ASN DDD CG  1 
ATOM 7157  O OD1 . ASN D 1 165 ? 136.167 1.544   78.047  1.000 27.090  ? 182 ASN DDD OD1 1 
ATOM 7158  N ND2 . ASN D 1 165 ? 134.030 1.736   77.396  1.000 27.550  ? 182 ASN DDD ND2 1 
ATOM 7159  N N   . THR D 1 166 ? 139.153 2.046   77.167  1.000 30.680  ? 183 THR DDD N   1 
ATOM 7160  C CA  . THR D 1 166 ? 140.272 1.247   77.727  1.000 29.790  ? 183 THR DDD CA  1 
ATOM 7161  C C   . THR D 1 166 ? 139.774 0.206   78.731  1.000 31.500  ? 183 THR DDD C   1 
ATOM 7162  O O   . THR D 1 166 ? 140.604 -0.627  79.138  1.000 32.750  ? 183 THR DDD O   1 
ATOM 7163  C CB  . THR D 1 166 ? 141.303 2.146   78.408  1.000 30.160  ? 183 THR DDD CB  1 
ATOM 7164  O OG1 . THR D 1 166 ? 140.543 3.198   78.993  1.000 31.260  ? 183 THR DDD OG1 1 
ATOM 7165  C CG2 . THR D 1 166 ? 142.338 2.701   77.453  1.000 32.730  ? 183 THR DDD CG2 1 
ATOM 7166  N N   . GLU D 1 167 ? 138.490 0.216   79.116  1.000 32.630  ? 184 GLU DDD N   1 
ATOM 7167  C CA  . GLU D 1 167 ? 137.919 -0.881  79.951  1.000 34.580  ? 184 GLU DDD CA  1 
ATOM 7168  C C   . GLU D 1 167 ? 138.118 -2.212  79.212  1.000 33.730  ? 184 GLU DDD C   1 
ATOM 7169  O O   . GLU D 1 167 ? 138.524 -3.160  79.854  1.000 37.570  ? 184 GLU DDD O   1 
ATOM 7170  C CB  . GLU D 1 167 ? 136.443 -0.685  80.316  1.000 36.380  ? 184 GLU DDD CB  1 
ATOM 7171  C CG  . GLU D 1 167 ? 136.111 -1.267  81.675  1.000 41.980  ? 184 GLU DDD CG  1 
ATOM 7172  C CD  . GLU D 1 167 ? 134.670 -1.641  81.982  1.000 45.590  ? 184 GLU DDD CD  1 
ATOM 7173  O OE1 . GLU D 1 167 ? 134.356 -2.863  81.979  1.000 46.530  ? 184 GLU DDD OE1 1 
ATOM 7174  O OE2 . GLU D 1 167 ? 133.878 -0.724  82.275  1.000 50.690  ? 184 GLU DDD OE2 1 
ATOM 7175  N N   . HIS D 1 168 ? 137.891 -2.254  77.894  1.000 30.760  ? 185 HIS DDD N   1 
ATOM 7176  C CA  . HIS D 1 168 ? 137.828 -3.483  77.056  1.000 26.130  ? 185 HIS DDD CA  1 
ATOM 7177  C C   . HIS D 1 168 ? 139.220 -4.044  76.774  1.000 25.310  ? 185 HIS DDD C   1 
ATOM 7178  O O   . HIS D 1 168 ? 139.615 -4.070  75.601  1.000 25.260  ? 185 HIS DDD O   1 
ATOM 7179  C CB  . HIS D 1 168 ? 137.105 -3.185  75.746  1.000 23.900  ? 185 HIS DDD CB  1 
ATOM 7180  C CG  . HIS D 1 168 ? 135.784 -2.543  75.959  1.000 22.230  ? 185 HIS DDD CG  1 
ATOM 7181  N ND1 . HIS D 1 168 ? 134.895 -3.006  76.905  1.000 22.120  ? 185 HIS DDD ND1 1 
ATOM 7182  C CD2 . HIS D 1 168 ? 135.214 -1.485  75.358  1.000 21.480  ? 185 HIS DDD CD2 1 
ATOM 7183  C CE1 . HIS D 1 168 ? 133.821 -2.256  76.860  1.000 22.950  ? 185 HIS DDD CE1 1 
ATOM 7184  N NE2 . HIS D 1 168 ? 133.997 -1.308  75.926  1.000 21.830  ? 185 HIS DDD NE2 1 
ATOM 7185  N N   . LYS D 1 169 ? 139.905 -4.536  77.797  1.000 25.000  ? 186 LYS DDD N   1 
ATOM 7186  C CA  . LYS D 1 169 ? 141.130 -5.360  77.650  1.000 24.660  ? 186 LYS DDD CA  1 
ATOM 7187  C C   . LYS D 1 169 ? 140.782 -6.832  77.879  1.000 24.660  ? 186 LYS DDD C   1 
ATOM 7188  O O   . LYS D 1 169 ? 139.755 -7.114  78.515  1.000 22.460  ? 186 LYS DDD O   1 
ATOM 7189  C CB  . LYS D 1 169 ? 142.200 -4.869  78.614  1.000 25.230  ? 186 LYS DDD CB  1 
ATOM 7190  C CG  . LYS D 1 169 ? 142.371 -3.356  78.618  1.000 27.140  ? 186 LYS DDD CG  1 
ATOM 7191  C CD  . LYS D 1 169 ? 143.063 -2.822  77.388  1.000 28.690  ? 186 LYS DDD CD  1 
ATOM 7192  C CE  . LYS D 1 169 ? 143.493 -1.386  77.569  1.000 30.640  ? 186 LYS DDD CE  1 
ATOM 7193  N NZ  . LYS D 1 169 ? 144.134 -0.834  76.355  1.000 31.490  ? 186 LYS DDD NZ  1 
ATOM 7194  N N   . ALA D 1 170 ? 141.591 -7.733  77.326  1.000 26.850  ? 187 ALA DDD N   1 
ATOM 7195  C CA  . ALA D 1 170 ? 141.350 -9.192  77.343  1.000 29.210  ? 187 ALA DDD CA  1 
ATOM 7196  C C   . ALA D 1 170 ? 142.544 -9.954  76.773  1.000 29.370  ? 187 ALA DDD C   1 
ATOM 7197  O O   . ALA D 1 170 ? 143.294 -9.367  75.991  1.000 29.310  ? 187 ALA DDD O   1 
ATOM 7198  C CB  . ALA D 1 170 ? 140.098 -9.481  76.557  1.000 32.000  ? 187 ALA DDD CB  1 
ATOM 7199  N N   . TYR D 1 171 ? 142.666 -11.234 77.115  1.000 30.920  ? 188 TYR DDD N   1 
ATOM 7200  C CA  . TYR D 1 171 ? 143.741 -12.126 76.605  1.000 34.970  ? 188 TYR DDD CA  1 
ATOM 7201  C C   . TYR D 1 171 ? 143.135 -13.130 75.621  1.000 37.020  ? 188 TYR DDD C   1 
ATOM 7202  O O   . TYR D 1 171 ? 142.096 -13.733 75.932  1.000 38.750  ? 188 TYR DDD O   1 
ATOM 7203  C CB  . TYR D 1 171 ? 144.441 -12.827 77.773  1.000 36.180  ? 188 TYR DDD CB  1 
ATOM 7204  C CG  . TYR D 1 171 ? 145.216 -11.908 78.686  1.000 35.830  ? 188 TYR DDD CG  1 
ATOM 7205  C CD1 . TYR D 1 171 ? 146.483 -11.479 78.347  1.000 39.930  ? 188 TYR DDD CD1 1 
ATOM 7206  C CD2 . TYR D 1 171 ? 144.698 -11.475 79.889  1.000 33.880  ? 188 TYR DDD CD2 1 
ATOM 7207  C CE1 . TYR D 1 171 ? 147.209 -10.638 79.172  1.000 41.100  ? 188 TYR DDD CE1 1 
ATOM 7208  C CE2 . TYR D 1 171 ? 145.408 -10.637 80.728  1.000 32.880  ? 188 TYR DDD CE2 1 
ATOM 7209  C CZ  . TYR D 1 171 ? 146.673 -10.230 80.376  1.000 35.630  ? 188 TYR DDD CZ  1 
ATOM 7210  O OH  . TYR D 1 171 ? 147.411 -9.399  81.167  1.000 36.120  ? 188 TYR DDD OH  1 
ATOM 7211  N N   . LEU D 1 172 ? 143.755 -13.285 74.446  1.000 39.490  ? 189 LEU DDD N   1 
ATOM 7212  C CA  . LEU D 1 172 ? 143.375 -14.361 73.495  1.000 39.780  ? 189 LEU DDD CA  1 
ATOM 7213  C C   . LEU D 1 172 ? 143.926 -15.672 74.052  1.000 38.000  ? 189 LEU DDD C   1 
ATOM 7214  O O   . LEU D 1 172 ? 145.051 -16.094 73.653  1.000 40.550  ? 189 LEU DDD O   1 
ATOM 7215  C CB  . LEU D 1 172 ? 143.909 -14.074 72.091  1.000 42.140  ? 189 LEU DDD CB  1 
ATOM 7216  C CG  . LEU D 1 172 ? 143.448 -15.072 71.026  1.000 41.620  ? 189 LEU DDD CG  1 
ATOM 7217  C CD1 . LEU D 1 172 ? 141.946 -15.300 71.074  1.000 38.910  ? 189 LEU DDD CD1 1 
ATOM 7218  C CD2 . LEU D 1 172 ? 143.877 -14.609 69.649  1.000 40.190  ? 189 LEU DDD CD2 1 
ATOM 7219  N N   . ASP D 1 173 ? 143.130 -16.256 74.952  1.000 35.300  ? 190 ASP DDD N   1 
ATOM 7220  C CA  . ASP D 1 173 ? 143.498 -17.406 75.814  1.000 36.910  ? 190 ASP DDD CA  1 
ATOM 7221  C C   . ASP D 1 173 ? 142.533 -18.575 75.573  1.000 37.150  ? 190 ASP DDD C   1 
ATOM 7222  O O   . ASP D 1 173 ? 142.663 -19.557 76.289  1.000 34.990  ? 190 ASP DDD O   1 
ATOM 7223  C CB  . ASP D 1 173 ? 143.453 -16.984 77.285  1.000 39.100  ? 190 ASP DDD CB  1 
ATOM 7224  C CG  . ASP D 1 173 ? 142.118 -16.361 77.723  1.000 40.060  ? 190 ASP DDD CG  1 
ATOM 7225  O OD1 . ASP D 1 173 ? 141.109 -16.496 76.998  1.000 38.090  ? 190 ASP DDD OD1 1 
ATOM 7226  O OD2 . ASP D 1 173 ? 142.093 -15.729 78.787  1.000 37.320  ? 190 ASP DDD OD2 1 
ATOM 7227  N N   . LYS D 1 174 ? 141.609 -18.470 74.617  1.000 37.740  ? 191 LYS DDD N   1 
ATOM 7228  C CA  . LYS D 1 174 ? 140.543 -19.479 74.408  1.000 37.990  ? 191 LYS DDD CA  1 
ATOM 7229  C C   . LYS D 1 174 ? 140.065 -19.466 72.944  1.000 37.310  ? 191 LYS DDD C   1 
ATOM 7230  O O   . LYS D 1 174 ? 139.922 -18.385 72.324  1.000 38.670  ? 191 LYS DDD O   1 
ATOM 7231  C CB  . LYS D 1 174 ? 139.401 -19.221 75.403  1.000 42.660  ? 191 LYS DDD CB  1 
ATOM 7232  C CG  . LYS D 1 174 ? 138.399 -20.357 75.537  1.000 51.170  ? 191 LYS DDD CG  1 
ATOM 7233  C CD  . LYS D 1 174 ? 137.194 -20.022 76.394  1.000 57.080  ? 191 LYS DDD CD  1 
ATOM 7234  C CE  . LYS D 1 174 ? 136.067 -21.027 76.239  1.000 58.440  ? 191 LYS DDD CE  1 
ATOM 7235  N NZ  . LYS D 1 174 ? 134.755 -20.410 76.549  1.000 59.770  ? 191 LYS DDD NZ  1 
ATOM 7236  N N   . ASN D 1 175 ? 139.794 -20.646 72.400  1.000 37.980  ? 192 ASN DDD N   1 
ATOM 7237  C CA  . ASN D 1 175 ? 139.317 -20.807 71.007  1.000 36.430  ? 192 ASN DDD CA  1 
ATOM 7238  C C   . ASN D 1 175 ? 137.794 -20.738 70.959  1.000 35.600  ? 192 ASN DDD C   1 
ATOM 7239  O O   . ASN D 1 175 ? 137.141 -20.902 71.991  1.000 34.710  ? 192 ASN DDD O   1 
ATOM 7240  C CB  . ASN D 1 175 ? 139.827 -22.105 70.401  1.000 36.640  ? 192 ASN DDD CB  1 
ATOM 7241  C CG  . ASN D 1 175 ? 140.991 -21.835 69.488  1.000 37.190  ? 192 ASN DDD CG  1 
ATOM 7242  O OD1 . ASN D 1 175 ? 140.788 -21.518 68.317  1.000 44.730  ? 192 ASN DDD OD1 1 
ATOM 7243  N ND2 . ASN D 1 175 ? 142.188 -21.912 70.034  1.000 31.550  ? 192 ASN DDD ND2 1 
ATOM 7244  N N   . LYS D 1 176 ? 137.262 -20.498 69.774  1.000 39.620  ? 193 LYS DDD N   1 
ATOM 7245  C CA  . LYS D 1 176 ? 135.808 -20.435 69.518  1.000 45.740  ? 193 LYS DDD CA  1 
ATOM 7246  C C   . LYS D 1 176 ? 135.188 -19.415 70.471  1.000 43.680  ? 193 LYS DDD C   1 
ATOM 7247  O O   . LYS D 1 176 ? 133.958 -19.487 70.684  1.000 40.700  ? 193 LYS DDD O   1 
ATOM 7248  C CB  . LYS D 1 176 ? 135.202 -21.829 69.673  1.000 52.930  ? 193 LYS DDD CB  1 
ATOM 7249  C CG  . LYS D 1 176 ? 135.799 -22.888 68.752  1.000 65.440  ? 193 LYS DDD CG  1 
ATOM 7250  C CD  . LYS D 1 176 ? 135.137 -24.251 68.855  1.000 77.250  ? 193 LYS DDD CD  1 
ATOM 7251  C CE  . LYS D 1 176 ? 133.770 -24.269 68.189  1.000 97.340  ? 193 LYS DDD CE  1 
ATOM 7252  N NZ  . LYS D 1 176 ? 132.936 -25.409 68.627  1.000 111.400 ? 193 LYS DDD NZ  1 
ATOM 7253  N N   . ALA D 1 177 ? 135.998 -18.459 70.952  1.000 43.870  ? 194 ALA DDD N   1 
ATOM 7254  C CA  . ALA D 1 177 ? 135.644 -17.575 72.085  1.000 42.270  ? 194 ALA DDD CA  1 
ATOM 7255  C C   . ALA D 1 177 ? 135.521 -16.103 71.650  1.000 36.430  ? 194 ALA DDD C   1 
ATOM 7256  O O   . ALA D 1 177 ? 134.439 -15.506 71.864  1.000 28.230  ? 194 ALA DDD O   1 
ATOM 7257  C CB  . ALA D 1 177 ? 136.654 -17.756 73.186  1.000 41.560  ? 194 ALA DDD CB  1 
ATOM 7258  N N   . TYR D 1 178 ? 136.597 -15.530 71.110  1.000 31.980  ? 195 TYR DDD N   1 
ATOM 7259  C CA  . TYR D 1 178 ? 136.715 -14.061 70.919  1.000 31.460  ? 195 TYR DDD CA  1 
ATOM 7260  C C   . TYR D 1 178 ? 136.298 -13.688 69.501  1.000 29.570  ? 195 TYR DDD C   1 
ATOM 7261  O O   . TYR D 1 178 ? 137.061 -13.858 68.557  1.000 28.990  ? 195 TYR DDD O   1 
ATOM 7262  C CB  . TYR D 1 178 ? 138.140 -13.600 71.235  1.000 32.440  ? 195 TYR DDD CB  1 
ATOM 7263  C CG  . TYR D 1 178 ? 138.523 -13.746 72.686  1.000 30.820  ? 195 TYR DDD CG  1 
ATOM 7264  C CD1 . TYR D 1 178 ? 139.016 -14.939 73.179  1.000 29.090  ? 195 TYR DDD CD1 1 
ATOM 7265  C CD2 . TYR D 1 178 ? 138.384 -12.689 73.572  1.000 30.720  ? 195 TYR DDD CD2 1 
ATOM 7266  C CE1 . TYR D 1 178 ? 139.366 -15.085 74.511  1.000 28.340  ? 195 TYR DDD CE1 1 
ATOM 7267  C CE2 . TYR D 1 178 ? 138.715 -12.819 74.907  1.000 30.720  ? 195 TYR DDD CE2 1 
ATOM 7268  C CZ  . TYR D 1 178 ? 139.194 -14.025 75.382  1.000 29.680  ? 195 TYR DDD CZ  1 
ATOM 7269  O OH  . TYR D 1 178 ? 139.532 -14.128 76.698  1.000 31.080  ? 195 TYR DDD OH  1 
ATOM 7270  N N   . PRO D 1 179 ? 135.086 -13.141 69.297  1.000 29.650  ? 196 PRO DDD N   1 
ATOM 7271  C CA  . PRO D 1 179 ? 134.649 -12.743 67.964  1.000 30.780  ? 196 PRO DDD CA  1 
ATOM 7272  C C   . PRO D 1 179 ? 135.679 -11.809 67.320  1.000 29.430  ? 196 PRO DDD C   1 
ATOM 7273  O O   . PRO D 1 179 ? 136.244 -11.034 68.041  1.000 28.970  ? 196 PRO DDD O   1 
ATOM 7274  C CB  . PRO D 1 179 ? 133.323 -12.003 68.213  1.000 29.900  ? 196 PRO DDD CB  1 
ATOM 7275  C CG  . PRO D 1 179 ? 132.827 -12.593 69.498  1.000 29.880  ? 196 PRO DDD CG  1 
ATOM 7276  C CD  . PRO D 1 179 ? 134.081 -12.826 70.317  1.000 30.310  ? 196 PRO DDD CD  1 
ATOM 7277  N N   . VAL D 1 180 ? 135.878 -11.903 66.001  1.000 28.470  ? 197 VAL DDD N   1 
ATOM 7278  C CA  . VAL D 1 180 ? 136.910 -11.103 65.283  1.000 27.280  ? 197 VAL DDD CA  1 
ATOM 7279  C C   . VAL D 1 180 ? 136.474 -9.632  65.271  1.000 27.450  ? 197 VAL DDD C   1 
ATOM 7280  O O   . VAL D 1 180 ? 137.343 -8.767  65.383  1.000 25.760  ? 197 VAL DDD O   1 
ATOM 7281  C CB  . VAL D 1 180 ? 137.131 -11.635 63.861  1.000 27.920  ? 197 VAL DDD CB  1 
ATOM 7282  C CG1 . VAL D 1 180 ? 138.121 -10.772 63.103  1.000 28.220  ? 197 VAL DDD CG1 1 
ATOM 7283  C CG2 . VAL D 1 180 ? 137.588 -13.079 63.846  1.000 28.430  ? 197 VAL DDD CG2 1 
ATOM 7284  N N   . GLU D 1 181 ? 135.171 -9.368  65.180  1.000 28.750  ? 198 GLU DDD N   1 
ATOM 7285  C CA  . GLU D 1 181 ? 134.619 -8.041  64.810  1.000 28.490  ? 198 GLU DDD CA  1 
ATOM 7286  C C   . GLU D 1 181 ? 134.558 -7.100  66.018  1.000 34.610  ? 198 GLU DDD C   1 
ATOM 7287  O O   . GLU D 1 181 ? 134.054 -5.959  65.854  1.000 38.380  ? 198 GLU DDD O   1 
ATOM 7288  C CB  . GLU D 1 181 ? 133.235 -8.218  64.179  1.000 28.210  ? 198 GLU DDD CB  1 
ATOM 7289  C CG  . GLU D 1 181 ? 132.073 -8.452  65.128  1.000 27.750  ? 198 GLU DDD CG  1 
ATOM 7290  C CD  . GLU D 1 181 ? 130.720 -8.465  64.451  1.000 27.850  ? 198 GLU DDD CD  1 
ATOM 7291  O OE1 . GLU D 1 181 ? 130.645 -9.002  63.308  1.000 35.440  ? 198 GLU DDD OE1 1 
ATOM 7292  O OE2 . GLU D 1 181 ? 129.754 -7.978  65.065  1.000 23.850  ? 198 GLU DDD OE2 1 
ATOM 7293  N N   . CYS D 1 182 ? 134.984 -7.532  67.207  1.000 38.600  ? 199 CYS DDD N   1 
ATOM 7294  C CA  . CYS D 1 182 ? 134.919 -6.661  68.411  1.000 37.080  ? 199 CYS DDD CA  1 
ATOM 7295  C C   . CYS D 1 182 ? 136.239 -6.692  69.186  1.000 31.060  ? 199 CYS DDD C   1 
ATOM 7296  O O   . CYS D 1 182 ? 136.308 -6.035  70.233  1.000 27.920  ? 199 CYS DDD O   1 
ATOM 7297  C CB  . CYS D 1 182 ? 133.705 -6.993  69.281  1.000 40.400  ? 199 CYS DDD CB  1 
ATOM 7298  S SG  . CYS D 1 182 ? 133.566 -8.725  69.783  1.000 40.680  ? 199 CYS DDD SG  1 
ATOM 7299  N N   . TRP D 1 183 ? 137.263 -7.349  68.652  1.000 28.510  ? 200 TRP DDD N   1 
ATOM 7300  C CA  . TRP D 1 183 ? 138.605 -7.418  69.283  1.000 29.820  ? 200 TRP DDD CA  1 
ATOM 7301  C C   . TRP D 1 183 ? 139.695 -7.159  68.240  1.000 28.410  ? 200 TRP DDD C   1 
ATOM 7302  O O   . TRP D 1 183 ? 139.581 -7.691  67.126  1.000 29.020  ? 200 TRP DDD O   1 
ATOM 7303  C CB  . TRP D 1 183 ? 138.832 -8.776  69.963  1.000 31.430  ? 200 TRP DDD CB  1 
ATOM 7304  C CG  . TRP D 1 183 ? 137.901 -9.097  71.087  1.000 27.820  ? 200 TRP DDD CG  1 
ATOM 7305  C CD1 . TRP D 1 183 ? 136.888 -10.005 71.091  1.000 27.060  ? 200 TRP DDD CD1 1 
ATOM 7306  C CD2 . TRP D 1 183 ? 137.922 -8.513  72.389  1.000 27.080  ? 200 TRP DDD CD2 1 
ATOM 7307  N NE1 . TRP D 1 183 ? 136.275 -10.031 72.310  1.000 27.250  ? 200 TRP DDD NE1 1 
ATOM 7308  C CE2 . TRP D 1 183 ? 136.889 -9.125  73.129  1.000 27.230  ? 200 TRP DDD CE2 1 
ATOM 7309  C CE3 . TRP D 1 183 ? 138.697 -7.510  72.983  1.000 28.170  ? 200 TRP DDD CE3 1 
ATOM 7310  C CZ2 . TRP D 1 183 ? 136.605 -8.759  74.440  1.000 26.460  ? 200 TRP DDD CZ2 1 
ATOM 7311  C CZ3 . TRP D 1 183 ? 138.427 -7.155  74.285  1.000 28.320  ? 200 TRP DDD CZ3 1 
ATOM 7312  C CH2 . TRP D 1 183 ? 137.380 -7.774  74.994  1.000 28.090  ? 200 TRP DDD CH2 1 
ATOM 7313  N N   . VAL D 1 184 ? 140.737 -6.427  68.625  1.000 26.690  ? 201 VAL DDD N   1 
ATOM 7314  C CA  . VAL D 1 184 ? 141.952 -6.215  67.795  1.000 27.080  ? 201 VAL DDD CA  1 
ATOM 7315  C C   . VAL D 1 184 ? 143.151 -6.328  68.706  1.000 26.100  ? 201 VAL DDD C   1 
ATOM 7316  O O   . VAL D 1 184 ? 143.032 -6.143  69.902  1.000 26.320  ? 201 VAL DDD O   1 
ATOM 7317  C CB  . VAL D 1 184 ? 141.928 -4.852  67.092  1.000 29.830  ? 201 VAL DDD CB  1 
ATOM 7318  C CG1 . VAL D 1 184 ? 140.723 -4.749  66.183  1.000 33.570  ? 201 VAL DDD CG1 1 
ATOM 7319  C CG2 . VAL D 1 184 ? 141.956 -3.711  68.089  1.000 30.300  ? 201 VAL DDD CG2 1 
ATOM 7320  N N   . PRO D 1 185 ? 144.343 -6.635  68.165  1.000 26.650  ? 202 PRO DDD N   1 
ATOM 7321  C CA  . PRO D 1 185 ? 145.558 -6.556  68.960  1.000 27.660  ? 202 PRO DDD CA  1 
ATOM 7322  C C   . PRO D 1 185 ? 145.617 -5.154  69.580  1.000 29.920  ? 202 PRO DDD C   1 
ATOM 7323  O O   . PRO D 1 185 ? 145.357 -4.182  68.847  1.000 35.900  ? 202 PRO DDD O   1 
ATOM 7324  C CB  . PRO D 1 185 ? 146.665 -6.797  67.928  1.000 29.080  ? 202 PRO DDD CB  1 
ATOM 7325  C CG  . PRO D 1 185 ? 145.999 -7.598  66.836  1.000 27.760  ? 202 PRO DDD CG  1 
ATOM 7326  C CD  . PRO D 1 185 ? 144.581 -7.078  66.782  1.000 27.520  ? 202 PRO DDD CD  1 
ATOM 7327  N N   . ASP D 1 186 ? 145.925 -5.100  70.881  1.000 28.660  ? 203 ASP DDD N   1 
ATOM 7328  C CA  . ASP D 1 186 ? 146.021 -3.858  71.695  1.000 27.370  ? 203 ASP DDD CA  1 
ATOM 7329  C C   . ASP D 1 186 ? 147.404 -3.272  71.484  1.000 25.220  ? 203 ASP DDD C   1 
ATOM 7330  O O   . ASP D 1 186 ? 148.384 -3.827  71.953  1.000 25.010  ? 203 ASP DDD O   1 
ATOM 7331  C CB  . ASP D 1 186 ? 145.765 -4.151  73.179  1.000 29.550  ? 203 ASP DDD CB  1 
ATOM 7332  C CG  . ASP D 1 186 ? 145.882 -2.958  74.116  1.000 28.140  ? 203 ASP DDD CG  1 
ATOM 7333  O OD1 . ASP D 1 186 ? 146.224 -1.872  73.627  1.000 26.410  ? 203 ASP DDD OD1 1 
ATOM 7334  O OD2 . ASP D 1 186 ? 145.599 -3.142  75.331  1.000 25.420  ? 203 ASP DDD OD2 1 
ATOM 7335  N N   . PRO D 1 187 ? 147.519 -2.140  70.775  1.000 26.420  ? 204 PRO DDD N   1 
ATOM 7336  C CA  . PRO D 1 187 ? 148.814 -1.642  70.332  1.000 28.880  ? 204 PRO DDD CA  1 
ATOM 7337  C C   . PRO D 1 187 ? 149.559 -0.993  71.494  1.000 32.870  ? 204 PRO DDD C   1 
ATOM 7338  O O   . PRO D 1 187 ? 150.742 -0.765  71.342  1.000 36.070  ? 204 PRO DDD O   1 
ATOM 7339  C CB  . PRO D 1 187 ? 148.475 -0.596  69.277  1.000 27.110  ? 204 PRO DDD CB  1 
ATOM 7340  C CG  . PRO D 1 187 ? 147.144 -0.073  69.746  1.000 27.630  ? 204 PRO DDD CG  1 
ATOM 7341  C CD  . PRO D 1 187 ? 146.419 -1.257  70.373  1.000 28.270  ? 204 PRO DDD CD  1 
ATOM 7342  N N   . THR D 1 188 ? 148.849 -0.740  72.600  1.000 34.940  ? 205 THR DDD N   1 
ATOM 7343  C CA  . THR D 1 188 ? 149.399 -0.150  73.849  1.000 35.600  ? 205 THR DDD CA  1 
ATOM 7344  C C   . THR D 1 188 ? 150.088 -1.236  74.681  1.000 38.580  ? 205 THR DDD C   1 
ATOM 7345  O O   . THR D 1 188 ? 150.689 -0.889  75.693  1.000 46.900  ? 205 THR DDD O   1 
ATOM 7346  C CB  . THR D 1 188 ? 148.294 0.502   74.700  1.000 32.520  ? 205 THR DDD CB  1 
ATOM 7347  O OG1 . THR D 1 188 ? 147.591 -0.557  75.351  1.000 31.560  ? 205 THR DDD OG1 1 
ATOM 7348  C CG2 . THR D 1 188 ? 147.341 1.370   73.913  1.000 32.220  ? 205 THR DDD CG2 1 
ATOM 7349  N N   . ARG D 1 189 ? 149.969 -2.502  74.300  1.000 38.590  ? 206 ARG DDD N   1 
ATOM 7350  C CA  . ARG D 1 189 ? 150.566 -3.652  75.011  1.000 38.470  ? 206 ARG DDD CA  1 
ATOM 7351  C C   . ARG D 1 189 ? 151.267 -4.519  73.949  1.000 37.530  ? 206 ARG DDD C   1 
ATOM 7352  O O   . ARG D 1 189 ? 151.757 -3.951  72.973  1.000 41.680  ? 206 ARG DDD O   1 
ATOM 7353  C CB  . ARG D 1 189 ? 149.499 -4.376  75.839  1.000 40.830  ? 206 ARG DDD CB  1 
ATOM 7354  C CG  . ARG D 1 189 ? 148.829 -3.510  76.888  1.000 49.780  ? 206 ARG DDD CG  1 
ATOM 7355  C CD  . ARG D 1 189 ? 147.815 -4.218  77.764  1.000 61.530  ? 206 ARG DDD CD  1 
ATOM 7356  N NE  . ARG D 1 189 ? 147.238 -3.290  78.738  1.000 69.000  ? 206 ARG DDD NE  1 
ATOM 7357  C CZ  . ARG D 1 189 ? 146.250 -3.577  79.594  1.000 64.630  ? 206 ARG DDD CZ  1 
ATOM 7358  N NH1 . ARG D 1 189 ? 145.708 -4.783  79.628  1.000 67.600  ? 206 ARG DDD NH1 1 
ATOM 7359  N NH2 . ARG D 1 189 ? 145.794 -2.654  80.420  1.000 58.360  ? 206 ARG DDD NH2 1 
ATOM 7360  N N   . ASN D 1 190 ? 151.353 -5.827  74.149  1.000 35.700  ? 207 ASN DDD N   1 
ATOM 7361  C CA  . ASN D 1 190 ? 151.909 -6.792  73.174  1.000 36.360  ? 207 ASN DDD CA  1 
ATOM 7362  C C   . ASN D 1 190 ? 153.389 -6.491  72.919  1.000 37.580  ? 207 ASN DDD C   1 
ATOM 7363  O O   . ASN D 1 190 ? 153.867 -6.790  71.819  1.000 39.840  ? 207 ASN DDD O   1 
ATOM 7364  C CB  . ASN D 1 190 ? 151.098 -6.835  71.876  1.000 36.650  ? 207 ASN DDD CB  1 
ATOM 7365  C CG  . ASN D 1 190 ? 149.784 -7.569  72.028  1.000 37.140  ? 207 ASN DDD CG  1 
ATOM 7366  O OD1 . ASN D 1 190 ? 149.758 -8.750  72.430  1.000 33.500  ? 207 ASN DDD OD1 1 
ATOM 7367  N ND2 . ASN D 1 190 ? 148.701 -6.869  71.707  1.000 35.940  ? 207 ASN DDD ND2 1 
ATOM 7368  N N   . GLU D 1 191 ? 154.099 -5.985  73.930  1.000 39.180  ? 208 GLU DDD N   1 
ATOM 7369  C CA  . GLU D 1 191 ? 155.578 -5.879  73.938  1.000 42.640  ? 208 GLU DDD CA  1 
ATOM 7370  C C   . GLU D 1 191 ? 156.164 -7.237  73.521  1.000 38.080  ? 208 GLU DDD C   1 
ATOM 7371  O O   . GLU D 1 191 ? 157.103 -7.232  72.701  1.000 41.180  ? 208 GLU DDD O   1 
ATOM 7372  C CB  . GLU D 1 191 ? 156.040 -5.419  75.328  1.000 50.140  ? 208 GLU DDD CB  1 
ATOM 7373  C CG  . GLU D 1 191 ? 157.541 -5.519  75.567  1.000 60.620  ? 208 GLU DDD CG  1 
ATOM 7374  C CD  . GLU D 1 191 ? 157.972 -6.013  76.954  1.000 73.750  ? 208 GLU DDD CD  1 
ATOM 7375  O OE1 . GLU D 1 191 ? 157.250 -5.751  77.968  1.000 73.530  ? 208 GLU DDD OE1 1 
ATOM 7376  O OE2 . GLU D 1 191 ? 159.020 -6.698  77.014  1.000 86.340  ? 208 GLU DDD OE2 1 
ATOM 7377  N N   . ASN D 1 192 ? 155.602 -8.346  74.020  1.000 32.040  ? 209 ASN DDD N   1 
ATOM 7378  C CA  . ASN D 1 192 ? 156.199 -9.703  73.927  1.000 29.700  ? 209 ASN DDD CA  1 
ATOM 7379  C C   . ASN D 1 192 ? 155.572 -10.504 72.768  1.000 31.700  ? 209 ASN DDD C   1 
ATOM 7380  O O   . ASN D 1 192 ? 155.747 -11.746 72.720  1.000 28.220  ? 209 ASN DDD O   1 
ATOM 7381  C CB  . ASN D 1 192 ? 156.024 -10.435 75.252  1.000 28.510  ? 209 ASN DDD CB  1 
ATOM 7382  C CG  . ASN D 1 192 ? 156.942 -11.632 75.386  1.000 29.600  ? 209 ASN DDD CG  1 
ATOM 7383  O OD1 . ASN D 1 192 ? 157.974 -11.710 74.719  1.000 27.840  ? 209 ASN DDD OD1 1 
ATOM 7384  N ND2 . ASN D 1 192 ? 156.573 -12.564 76.254  1.000 29.860  ? 209 ASN DDD ND2 1 
ATOM 7385  N N   . THR D 1 193 ? 154.869 -9.838  71.849  1.000 32.820  ? 210 THR DDD N   1 
ATOM 7386  C CA  . THR D 1 193 ? 154.228 -10.484 70.677  1.000 32.580  ? 210 THR DDD CA  1 
ATOM 7387  C C   . THR D 1 193 ? 154.593 -9.686  69.419  1.000 32.160  ? 210 THR DDD C   1 
ATOM 7388  O O   . THR D 1 193 ? 154.877 -8.486  69.536  1.000 32.790  ? 210 THR DDD O   1 
ATOM 7389  C CB  . THR D 1 193 ? 152.716 -10.610 70.894  1.000 33.130  ? 210 THR DDD CB  1 
ATOM 7390  O OG1 . THR D 1 193 ? 152.419 -11.580 71.912  1.000 30.060  ? 210 THR DDD OG1 1 
ATOM 7391  C CG2 . THR D 1 193 ? 152.004 -11.010 69.622  1.000 34.410  ? 210 THR DDD CG2 1 
ATOM 7392  N N   . ARG D 1 194 ? 154.658 -10.355 68.271  1.000 31.490  ? 211 ARG DDD N   1 
ATOM 7393  C CA  . ARG D 1 194 ? 154.805 -9.723  66.938  1.000 30.410  ? 211 ARG DDD CA  1 
ATOM 7394  C C   . ARG D 1 194 ? 153.546 -10.065 66.162  1.000 28.270  ? 211 ARG DDD C   1 
ATOM 7395  O O   . ARG D 1 194 ? 153.315 -11.243 65.933  1.000 31.350  ? 211 ARG DDD O   1 
ATOM 7396  C CB  . ARG D 1 194 ? 156.028 -10.267 66.190  1.000 31.330  ? 211 ARG DDD CB  1 
ATOM 7397  C CG  . ARG D 1 194 ? 157.317 -10.192 66.989  1.000 31.190  ? 211 ARG DDD CG  1 
ATOM 7398  C CD  . ARG D 1 194 ? 157.717 -8.758  67.257  1.000 31.020  ? 211 ARG DDD CD  1 
ATOM 7399  N NE  . ARG D 1 194 ? 158.979 -8.762  67.965  1.000 32.030  ? 211 ARG DDD NE  1 
ATOM 7400  C CZ  . ARG D 1 194 ? 159.093 -8.735  69.288  1.000 31.300  ? 211 ARG DDD CZ  1 
ATOM 7401  N NH1 . ARG D 1 194 ? 157.998 -8.673  70.040  1.000 29.780  ? 211 ARG DDD NH1 1 
ATOM 7402  N NH2 . ARG D 1 194 ? 160.301 -8.759  69.838  1.000 29.970  ? 211 ARG DDD NH2 1 
ATOM 7403  N N   . TYR D 1 195 ? 152.729 -9.079  65.843  1.000 27.570  ? 212 TYR DDD N   1 
ATOM 7404  C CA  . TYR D 1 195 ? 151.417 -9.300  65.194  1.000 28.280  ? 212 TYR DDD CA  1 
ATOM 7405  C C   . TYR D 1 195 ? 151.414 -8.544  63.870  1.000 27.270  ? 212 TYR DDD C   1 
ATOM 7406  O O   . TYR D 1 195 ? 152.053 -7.492  63.751  1.000 26.570  ? 212 TYR DDD O   1 
ATOM 7407  C CB  . TYR D 1 195 ? 150.264 -8.916  66.128  1.000 28.210  ? 212 TYR DDD CB  1 
ATOM 7408  C CG  . TYR D 1 195 ? 150.087 -7.445  66.404  1.000 25.440  ? 212 TYR DDD CG  1 
ATOM 7409  C CD1 . TYR D 1 195 ? 149.385 -6.638  65.537  1.000 26.070  ? 212 TYR DDD CD1 1 
ATOM 7410  C CD2 . TYR D 1 195 ? 150.575 -6.878  67.560  1.000 24.370  ? 212 TYR DDD CD2 1 
ATOM 7411  C CE1 . TYR D 1 195 ? 149.195 -5.294  65.806  1.000 28.100  ? 212 TYR DDD CE1 1 
ATOM 7412  C CE2 . TYR D 1 195 ? 150.383 -5.544  67.853  1.000 25.340  ? 212 TYR DDD CE2 1 
ATOM 7413  C CZ  . TYR D 1 195 ? 149.699 -4.736  66.970  1.000 27.510  ? 212 TYR DDD CZ  1 
ATOM 7414  O OH  . TYR D 1 195 ? 149.546 -3.396  67.238  1.000 30.730  ? 212 TYR DDD OH  1 
ATOM 7415  N N   . PHE D 1 196 ? 150.729 -9.123  62.898  1.000 25.990  ? 213 PHE DDD N   1 
ATOM 7416  C CA  . PHE D 1 196 ? 150.600 -8.606  61.519  1.000 25.100  ? 213 PHE DDD CA  1 
ATOM 7417  C C   . PHE D 1 196 ? 149.218 -8.988  61.008  1.000 24.330  ? 213 PHE DDD C   1 
ATOM 7418  O O   . PHE D 1 196 ? 148.867 -10.178 61.092  1.000 27.500  ? 213 PHE DDD O   1 
ATOM 7419  C CB  . PHE D 1 196 ? 151.640 -9.230  60.594  1.000 24.360  ? 213 PHE DDD CB  1 
ATOM 7420  C CG  . PHE D 1 196 ? 153.034 -9.358  61.150  1.000 23.800  ? 213 PHE DDD CG  1 
ATOM 7421  C CD1 . PHE D 1 196 ? 153.378 -10.430 61.935  1.000 24.560  ? 213 PHE DDD CD1 1 
ATOM 7422  C CD2 . PHE D 1 196 ? 154.017 -8.445  60.832  1.000 24.270  ? 213 PHE DDD CD2 1 
ATOM 7423  C CE1 . PHE D 1 196 ? 154.670 -10.589 62.396  1.000 25.470  ? 213 PHE DDD CE1 1 
ATOM 7424  C CE2 . PHE D 1 196 ? 155.314 -8.605  61.280  1.000 24.540  ? 213 PHE DDD CE2 1 
ATOM 7425  C CZ  . PHE D 1 196 ? 155.640 -9.685  62.051  1.000 25.820  ? 213 PHE DDD CZ  1 
ATOM 7426  N N   . GLY D 1 197 ? 148.470 -8.024  60.500  1.000 21.890  ? 214 GLY DDD N   1 
ATOM 7427  C CA  . GLY D 1 197 ? 147.136 -8.276  59.949  1.000 20.410  ? 214 GLY DDD CA  1 
ATOM 7428  C C   . GLY D 1 197 ? 146.718 -7.202  58.971  1.000 19.130  ? 214 GLY DDD C   1 
ATOM 7429  O O   . GLY D 1 197 ? 147.268 -6.108  58.992  1.000 17.650  ? 214 GLY DDD O   1 
ATOM 7430  N N   . THR D 1 198 ? 145.738 -7.524  58.142  1.000 18.810  ? 215 THR DDD N   1 
ATOM 7431  C CA  . THR D 1 198 ? 145.205 -6.621  57.109  1.000 18.940  ? 215 THR DDD CA  1 
ATOM 7432  C C   . THR D 1 198 ? 143.713 -6.844  56.978  1.000 19.700  ? 215 THR DDD C   1 
ATOM 7433  O O   . THR D 1 198 ? 143.325 -7.992  56.795  1.000 20.730  ? 215 THR DDD O   1 
ATOM 7434  C CB  . THR D 1 198 ? 145.857 -6.882  55.754  1.000 18.780  ? 215 THR DDD CB  1 
ATOM 7435  O OG1 . THR D 1 198 ? 147.272 -6.738  55.926  1.000 17.660  ? 215 THR DDD OG1 1 
ATOM 7436  C CG2 . THR D 1 198 ? 145.264 -5.977  54.695  1.000 19.400  ? 215 THR DDD CG2 1 
ATOM 7437  N N   . LEU D 1 199 ? 142.931 -5.775  57.093  1.000 20.900  ? 216 LEU DDD N   1 
ATOM 7438  C CA  . LEU D 1 199 ? 141.503 -5.785  56.727  1.000 21.750  ? 216 LEU DDD CA  1 
ATOM 7439  C C   . LEU D 1 199 ? 141.393 -5.158  55.349  1.000 23.550  ? 216 LEU DDD C   1 
ATOM 7440  O O   . LEU D 1 199 ? 141.861 -4.020  55.181  1.000 23.110  ? 216 LEU DDD O   1 
ATOM 7441  C CB  . LEU D 1 199 ? 140.644 -5.014  57.717  1.000 22.810  ? 216 LEU DDD CB  1 
ATOM 7442  C CG  . LEU D 1 199 ? 139.175 -4.978  57.291  1.000 25.490  ? 216 LEU DDD CG  1 
ATOM 7443  C CD1 . LEU D 1 199 ? 138.276 -5.437  58.410  1.000 27.210  ? 216 LEU DDD CD1 1 
ATOM 7444  C CD2 . LEU D 1 199 ? 138.756 -3.595  56.807  1.000 25.460  ? 216 LEU DDD CD2 1 
ATOM 7445  N N   . THR D 1 200 ? 140.796 -5.899  54.418  1.000 25.770  ? 217 THR DDD N   1 
ATOM 7446  C CA  . THR D 1 200 ? 140.224 -5.363  53.163  1.000 25.740  ? 217 THR DDD CA  1 
ATOM 7447  C C   . THR D 1 200 ? 138.691 -5.482  53.208  1.000 26.760  ? 217 THR DDD C   1 
ATOM 7448  O O   . THR D 1 200 ? 138.192 -6.607  53.247  1.000 29.150  ? 217 THR DDD O   1 
ATOM 7449  C CB  . THR D 1 200 ? 140.834 -6.090  51.973  1.000 23.290  ? 217 THR DDD CB  1 
ATOM 7450  O OG1 . THR D 1 200 ? 142.245 -6.077  52.142  1.000 21.180  ? 217 THR DDD OG1 1 
ATOM 7451  C CG2 . THR D 1 200 ? 140.482 -5.406  50.682  1.000 24.570  ? 217 THR DDD CG2 1 
ATOM 7452  N N   . GLY D 1 201 ? 137.973 -4.368  53.204  1.000 26.570  ? 218 GLY DDD N   1 
ATOM 7453  C CA  . GLY D 1 201 ? 136.498 -4.350  53.238  1.000 28.790  ? 218 GLY DDD CA  1 
ATOM 7454  C C   . GLY D 1 201 ? 135.907 -4.094  51.869  1.000 29.740  ? 218 GLY DDD C   1 
ATOM 7455  O O   . GLY D 1 201 ? 136.583 -3.434  51.081  1.000 29.590  ? 218 GLY DDD O   1 
ATOM 7456  N N   . GLY D 1 202 ? 134.699 -4.585  51.603  1.000 31.040  ? 219 GLY DDD N   1 
ATOM 7457  C CA  . GLY D 1 202 ? 134.010 -4.430  50.307  1.000 32.320  ? 219 GLY DDD CA  1 
ATOM 7458  C C   . GLY D 1 202 ? 133.478 -5.769  49.807  1.000 34.510  ? 219 GLY DDD C   1 
ATOM 7459  O O   . GLY D 1 202 ? 134.209 -6.784  49.913  1.000 32.930  ? 219 GLY DDD O   1 
ATOM 7460  N N   . GLU D 1 203 ? 132.244 -5.783  49.285  1.000 34.570  ? 220 GLU DDD N   1 
ATOM 7461  C CA  . GLU D 1 203 ? 131.518 -7.034  48.931  1.000 32.630  ? 220 GLU DDD CA  1 
ATOM 7462  C C   . GLU D 1 203 ? 132.199 -7.698  47.724  1.000 31.040  ? 220 GLU DDD C   1 
ATOM 7463  O O   . GLU D 1 203 ? 132.082 -8.914  47.605  1.000 30.070  ? 220 GLU DDD O   1 
ATOM 7464  C CB  . GLU D 1 203 ? 130.008 -6.801  48.743  1.000 30.540  ? 220 GLU DDD CB  1 
ATOM 7465  C CG  . GLU D 1 203 ? 129.626 -5.812  47.665  1.000 31.300  ? 220 GLU DDD CG  1 
ATOM 7466  C CD  . GLU D 1 203 ? 129.378 -4.405  48.188  1.000 33.320  ? 220 GLU DDD CD  1 
ATOM 7467  O OE1 . GLU D 1 203 ? 130.153 -3.981  49.066  1.000 32.730  ? 220 GLU DDD OE1 1 
ATOM 7468  O OE2 . GLU D 1 203 ? 128.434 -3.718  47.703  1.000 38.800  ? 220 GLU DDD OE2 1 
ATOM 7469  N N   . ASN D 1 204 ? 132.941 -6.947  46.916  1.000 31.680  ? 221 ASN DDD N   1 
ATOM 7470  C CA  . ASN D 1 204 ? 133.521 -7.436  45.637  1.000 32.280  ? 221 ASN DDD CA  1 
ATOM 7471  C C   . ASN D 1 204 ? 135.051 -7.538  45.743  1.000 32.810  ? 221 ASN DDD C   1 
ATOM 7472  O O   . ASN D 1 204 ? 135.703 -7.875  44.744  1.000 31.380  ? 221 ASN DDD O   1 
ATOM 7473  C CB  . ASN D 1 204 ? 133.043 -6.554  44.485  1.000 32.600  ? 221 ASN DDD CB  1 
ATOM 7474  C CG  . ASN D 1 204 ? 131.536 -6.654  44.326  1.000 31.850  ? 221 ASN DDD CG  1 
ATOM 7475  O OD1 . ASN D 1 204 ? 130.994 -7.748  44.336  1.000 32.480  ? 221 ASN DDD OD1 1 
ATOM 7476  N ND2 . ASN D 1 204 ? 130.829 -5.541  44.244  1.000 29.570  ? 221 ASN DDD ND2 1 
ATOM 7477  N N   . VAL D 1 205 ? 135.615 -7.328  46.926  1.000 32.930  ? 222 VAL DDD N   1 
ATOM 7478  C CA  . VAL D 1 205 ? 137.088 -7.421  47.095  1.000 33.810  ? 222 VAL DDD CA  1 
ATOM 7479  C C   . VAL D 1 205 ? 137.532 -8.805  46.632  1.000 33.010  ? 222 VAL DDD C   1 
ATOM 7480  O O   . VAL D 1 205 ? 137.131 -9.808  47.223  1.000 36.030  ? 222 VAL DDD O   1 
ATOM 7481  C CB  . VAL D 1 205 ? 137.536 -7.161  48.542  1.000 34.620  ? 222 VAL DDD CB  1 
ATOM 7482  C CG1 . VAL D 1 205 ? 139.029 -7.360  48.688  1.000 36.900  ? 222 VAL DDD CG1 1 
ATOM 7483  C CG2 . VAL D 1 205 ? 137.141 -5.786  49.035  1.000 35.860  ? 222 VAL DDD CG2 1 
ATOM 7484  N N   . PRO D 1 206 ? 138.411 -8.899  45.613  1.000 29.580  ? 223 PRO DDD N   1 
ATOM 7485  C CA  . PRO D 1 206 ? 138.983 -10.176 45.201  1.000 28.090  ? 223 PRO DDD CA  1 
ATOM 7486  C C   . PRO D 1 206 ? 139.998 -10.701 46.210  1.000 25.480  ? 223 PRO DDD C   1 
ATOM 7487  O O   . PRO D 1 206 ? 140.913 -9.965  46.593  1.000 26.430  ? 223 PRO DDD O   1 
ATOM 7488  C CB  . PRO D 1 206 ? 139.708 -9.841  43.895  1.000 27.660  ? 223 PRO DDD CB  1 
ATOM 7489  C CG  . PRO D 1 206 ? 140.148 -8.432  44.128  1.000 30.530  ? 223 PRO DDD CG  1 
ATOM 7490  C CD  . PRO D 1 206 ? 138.967 -7.787  44.841  1.000 30.590  ? 223 PRO DDD CD  1 
ATOM 7491  N N   . PRO D 1 207 ? 139.873 -11.986 46.625  1.000 21.600  ? 224 PRO DDD N   1 
ATOM 7492  C CA  . PRO D 1 207 ? 140.926 -12.683 47.346  1.000 20.650  ? 224 PRO DDD CA  1 
ATOM 7493  C C   . PRO D 1 207 ? 142.215 -12.668 46.531  1.000 19.550  ? 224 PRO DDD C   1 
ATOM 7494  O O   . PRO D 1 207 ? 142.149 -12.857 45.351  1.000 18.990  ? 224 PRO DDD O   1 
ATOM 7495  C CB  . PRO D 1 207 ? 140.429 -14.127 47.490  1.000 20.260  ? 224 PRO DDD CB  1 
ATOM 7496  C CG  . PRO D 1 207 ? 138.935 -14.011 47.350  1.000 20.550  ? 224 PRO DDD CG  1 
ATOM 7497  C CD  . PRO D 1 207 ? 138.739 -12.876 46.368  1.000 20.930  ? 224 PRO DDD CD  1 
ATOM 7498  N N   . VAL D 1 208 ? 143.331 -12.411 47.197  1.000 19.720  ? 225 VAL DDD N   1 
ATOM 7499  C CA  . VAL D 1 208 ? 144.691 -12.500 46.606  1.000 19.580  ? 225 VAL DDD CA  1 
ATOM 7500  C C   . VAL D 1 208 ? 145.589 -13.180 47.624  1.000 20.730  ? 225 VAL DDD C   1 
ATOM 7501  O O   . VAL D 1 208 ? 146.044 -12.491 48.552  1.000 24.010  ? 225 VAL DDD O   1 
ATOM 7502  C CB  . VAL D 1 208 ? 145.228 -11.113 46.269  1.000 19.160  ? 225 VAL DDD CB  1 
ATOM 7503  C CG1 . VAL D 1 208 ? 146.692 -11.190 45.850  1.000 19.220  ? 225 VAL DDD CG1 1 
ATOM 7504  C CG2 . VAL D 1 208 ? 144.330 -10.439 45.244  1.000 19.550  ? 225 VAL DDD CG2 1 
ATOM 7505  N N   . LEU D 1 209 ? 145.809 -14.476 47.467  1.000 20.340  ? 226 LEU DDD N   1 
ATOM 7506  C CA  . LEU D 1 209 ? 146.537 -15.290 48.455  1.000 19.690  ? 226 LEU DDD CA  1 
ATOM 7507  C C   . LEU D 1 209 ? 147.815 -15.837 47.810  1.000 21.320  ? 226 LEU DDD C   1 
ATOM 7508  O O   . LEU D 1 209 ? 147.690 -16.625 46.854  1.000 21.060  ? 226 LEU DDD O   1 
ATOM 7509  C CB  . LEU D 1 209 ? 145.546 -16.367 48.890  1.000 17.960  ? 226 LEU DDD CB  1 
ATOM 7510  C CG  . LEU D 1 209 ? 144.235 -15.797 49.416  1.000 16.760  ? 226 LEU DDD CG  1 
ATOM 7511  C CD1 . LEU D 1 209 ? 143.230 -16.908 49.694  1.000 16.720  ? 226 LEU DDD CD1 1 
ATOM 7512  C CD2 . LEU D 1 209 ? 144.479 -14.944 50.659  1.000 16.410  ? 226 LEU DDD CD2 1 
ATOM 7513  N N   . HIS D 1 210 ? 148.976 -15.383 48.279  1.000 23.120  ? 227 HIS DDD N   1 
ATOM 7514  C CA  . HIS D 1 210 ? 150.304 -15.891 47.846  1.000 26.420  ? 227 HIS DDD CA  1 
ATOM 7515  C C   . HIS D 1 210 ? 150.715 -17.058 48.751  1.000 27.160  ? 227 HIS DDD C   1 
ATOM 7516  O O   . HIS D 1 210 ? 150.443 -17.026 49.975  1.000 28.340  ? 227 HIS DDD O   1 
ATOM 7517  C CB  . HIS D 1 210 ? 151.368 -14.779 47.834  1.000 29.710  ? 227 HIS DDD CB  1 
ATOM 7518  C CG  . HIS D 1 210 ? 150.932 -13.536 47.130  1.000 33.900  ? 227 HIS DDD CG  1 
ATOM 7519  N ND1 . HIS D 1 210 ? 150.836 -13.457 45.751  1.000 37.460  ? 227 HIS DDD ND1 1 
ATOM 7520  C CD2 . HIS D 1 210 ? 150.558 -12.326 47.596  1.000 37.910  ? 227 HIS DDD CD2 1 
ATOM 7521  C CE1 . HIS D 1 210 ? 150.421 -12.258 45.397  1.000 38.170  ? 227 HIS DDD CE1 1 
ATOM 7522  N NE2 . HIS D 1 210 ? 150.213 -11.548 46.511  1.000 39.830  ? 227 HIS DDD NE2 1 
ATOM 7523  N N   . ILE D 1 211 ? 151.330 -18.081 48.161  1.000 26.160  ? 228 ILE DDD N   1 
ATOM 7524  C CA  . ILE D 1 211 ? 151.868 -19.260 48.890  1.000 22.210  ? 228 ILE DDD CA  1 
ATOM 7525  C C   . ILE D 1 211 ? 153.305 -19.450 48.413  1.000 22.120  ? 228 ILE DDD C   1 
ATOM 7526  O O   . ILE D 1 211 ? 153.580 -19.245 47.224  1.000 19.930  ? 228 ILE DDD O   1 
ATOM 7527  C CB  . ILE D 1 211 ? 150.966 -20.486 48.641  1.000 19.470  ? 228 ILE DDD CB  1 
ATOM 7528  C CG1 . ILE D 1 211 ? 150.986 -20.981 47.201  1.000 18.050  ? 228 ILE DDD CG1 1 
ATOM 7529  C CG2 . ILE D 1 211 ? 149.543 -20.203 49.056  1.000 18.450  ? 228 ILE DDD CG2 1 
ATOM 7530  C CD1 . ILE D 1 211 ? 150.283 -22.304 47.045  1.000 17.220  ? 228 ILE DDD CD1 1 
ATOM 7531  N N   . THR D 1 212 ? 154.206 -19.792 49.323  1.000 25.310  ? 229 THR DDD N   1 
ATOM 7532  C CA  . THR D 1 212 ? 155.632 -20.069 49.005  1.000 27.340  ? 229 THR DDD CA  1 
ATOM 7533  C C   . THR D 1 212 ? 156.332 -20.587 50.261  1.000 29.300  ? 229 THR DDD C   1 
ATOM 7534  O O   . THR D 1 212 ? 156.033 -20.089 51.364  1.000 32.840  ? 229 THR DDD O   1 
ATOM 7535  C CB  . THR D 1 212 ? 156.353 -18.831 48.454  1.000 24.550  ? 229 THR DDD CB  1 
ATOM 7536  O OG1 . THR D 1 212 ? 157.621 -19.250 47.965  1.000 26.780  ? 229 THR DDD OG1 1 
ATOM 7537  C CG2 . THR D 1 212 ? 156.572 -17.770 49.492  1.000 23.180  ? 229 THR DDD CG2 1 
ATOM 7538  N N   . ASN D 1 213 ? 157.235 -21.539 50.101  1.000 31.220  ? 230 ASN DDD N   1 
ATOM 7539  C CA  . ASN D 1 213 ? 158.064 -22.016 51.235  1.000 32.020  ? 230 ASN DDD CA  1 
ATOM 7540  C C   . ASN D 1 213 ? 159.424 -21.295 51.203  1.000 30.030  ? 230 ASN DDD C   1 
ATOM 7541  O O   . ASN D 1 213 ? 160.348 -21.818 51.794  1.000 30.300  ? 230 ASN DDD O   1 
ATOM 7542  C CB  . ASN D 1 213 ? 158.186 -23.543 51.234  1.000 32.370  ? 230 ASN DDD CB  1 
ATOM 7543  C CG  . ASN D 1 213 ? 158.780 -24.088 49.957  1.000 31.000  ? 230 ASN DDD CG  1 
ATOM 7544  O OD1 . ASN D 1 213 ? 159.054 -23.345 49.032  1.000 34.970  ? 230 ASN DDD OD1 1 
ATOM 7545  N ND2 . ASN D 1 213 ? 158.944 -25.389 49.879  1.000 32.760  ? 230 ASN DDD ND2 1 
ATOM 7546  N N   . THR D 1 214 ? 159.530 -20.132 50.557  1.000 28.390  ? 231 THR DDD N   1 
ATOM 7547  C CA  . THR D 1 214 ? 160.815 -19.404 50.376  1.000 28.590  ? 231 THR DDD CA  1 
ATOM 7548  C C   . THR D 1 214 ? 160.831 -18.100 51.182  1.000 27.940  ? 231 THR DDD C   1 
ATOM 7549  O O   . THR D 1 214 ? 161.865 -17.443 51.204  1.000 28.180  ? 231 THR DDD O   1 
ATOM 7550  C CB  . THR D 1 214 ? 161.060 -19.087 48.900  1.000 29.860  ? 231 THR DDD CB  1 
ATOM 7551  O OG1 . THR D 1 214 ? 160.014 -18.225 48.472  1.000 31.900  ? 231 THR DDD OG1 1 
ATOM 7552  C CG2 . THR D 1 214 ? 161.050 -20.311 48.021  1.000 31.500  ? 231 THR DDD CG2 1 
ATOM 7553  N N   . ALA D 1 215 ? 159.728 -17.742 51.834  1.000 28.490  ? 232 ALA DDD N   1 
ATOM 7554  C CA  . ALA D 1 215 ? 159.552 -16.435 52.493  1.000 29.400  ? 232 ALA DDD CA  1 
ATOM 7555  C C   . ALA D 1 215 ? 159.629 -16.613 54.004  1.000 31.270  ? 232 ALA DDD C   1 
ATOM 7556  O O   . ALA D 1 215 ? 158.680 -17.161 54.583  1.000 31.340  ? 232 ALA DDD O   1 
ATOM 7557  C CB  . ALA D 1 215 ? 158.229 -15.839 52.087  1.000 31.030  ? 232 ALA DDD CB  1 
ATOM 7558  N N   . THR D 1 216 ? 160.711 -16.136 54.612  1.000 34.080  ? 233 THR DDD N   1 
ATOM 7559  C CA  . THR D 1 216 ? 160.900 -16.099 56.085  1.000 35.190  ? 233 THR DDD CA  1 
ATOM 7560  C C   . THR D 1 216 ? 160.636 -14.675 56.569  1.000 31.950  ? 233 THR DDD C   1 
ATOM 7561  O O   . THR D 1 216 ? 160.994 -13.784 55.859  1.000 33.310  ? 233 THR DDD O   1 
ATOM 7562  C CB  . THR D 1 216 ? 162.303 -16.596 56.459  1.000 37.280  ? 233 THR DDD CB  1 
ATOM 7563  O OG1 . THR D 1 216 ? 162.525 -17.846 55.810  1.000 43.700  ? 233 THR DDD OG1 1 
ATOM 7564  C CG2 . THR D 1 216 ? 162.486 -16.783 57.942  1.000 36.540  ? 233 THR DDD CG2 1 
ATOM 7565  N N   . THR D 1 217 ? 160.018 -14.497 57.735  1.000 33.130  ? 234 THR DDD N   1 
ATOM 7566  C CA  . THR D 1 217 ? 159.763 -13.201 58.423  1.000 31.760  ? 234 THR DDD CA  1 
ATOM 7567  C C   . THR D 1 217 ? 160.530 -13.181 59.741  1.000 34.320  ? 234 THR DDD C   1 
ATOM 7568  O O   . THR D 1 217 ? 160.351 -14.127 60.511  1.000 35.230  ? 234 THR DDD O   1 
ATOM 7569  C CB  . THR D 1 217 ? 158.284 -13.020 58.766  1.000 29.560  ? 234 THR DDD CB  1 
ATOM 7570  O OG1 . THR D 1 217 ? 157.512 -13.171 57.584  1.000 31.210  ? 234 THR DDD OG1 1 
ATOM 7571  C CG2 . THR D 1 217 ? 157.995 -11.669 59.364  1.000 31.020  ? 234 THR DDD CG2 1 
ATOM 7572  N N   . VAL D 1 218 ? 161.324 -12.152 60.019  1.000 36.620  ? 235 VAL DDD N   1 
ATOM 7573  C CA  . VAL D 1 218 ? 162.161 -12.111 61.253  1.000 34.370  ? 235 VAL DDD CA  1 
ATOM 7574  C C   . VAL D 1 218 ? 161.319 -11.537 62.395  1.000 33.800  ? 235 VAL DDD C   1 
ATOM 7575  O O   . VAL D 1 218 ? 160.567 -10.616 62.132  1.000 40.330  ? 235 VAL DDD O   1 
ATOM 7576  C CB  . VAL D 1 218 ? 163.444 -11.306 61.003  1.000 32.560  ? 235 VAL DDD CB  1 
ATOM 7577  C CG1 . VAL D 1 218 ? 164.120 -10.902 62.303  1.000 35.990  ? 235 VAL DDD CG1 1 
ATOM 7578  C CG2 . VAL D 1 218 ? 164.403 -12.070 60.117  1.000 30.740  ? 235 VAL DDD CG2 1 
ATOM 7579  N N   . LEU D 1 219 ? 161.431 -12.064 63.610  1.000 31.990  ? 236 LEU DDD N   1 
ATOM 7580  C CA  . LEU D 1 219 ? 160.575 -11.683 64.766  1.000 32.210  ? 236 LEU DDD CA  1 
ATOM 7581  C C   . LEU D 1 219 ? 161.351 -10.838 65.788  1.000 31.450  ? 236 LEU DDD C   1 
ATOM 7582  O O   . LEU D 1 219 ? 160.750 -10.441 66.813  1.000 27.480  ? 236 LEU DDD O   1 
ATOM 7583  C CB  . LEU D 1 219 ? 160.035 -12.963 65.399  1.000 31.980  ? 236 LEU DDD CB  1 
ATOM 7584  C CG  . LEU D 1 219 ? 159.182 -13.813 64.461  1.000 31.600  ? 236 LEU DDD CG  1 
ATOM 7585  C CD1 . LEU D 1 219 ? 158.871 -15.156 65.094  1.000 31.180  ? 236 LEU DDD CD1 1 
ATOM 7586  C CD2 . LEU D 1 219 ? 157.898 -13.086 64.101  1.000 33.500  ? 236 LEU DDD CD2 1 
ATOM 7587  N N   . LEU D 1 220 ? 162.620 -10.527 65.493  1.000 31.720  ? 237 LEU DDD N   1 
ATOM 7588  C CA  . LEU D 1 220 ? 163.485 -9.685  66.360  1.000 33.750  ? 237 LEU DDD CA  1 
ATOM 7589  C C   . LEU D 1 220 ? 163.035 -8.226  66.272  1.000 38.340  ? 237 LEU DDD C   1 
ATOM 7590  O O   . LEU D 1 220 ? 162.626 -7.811  65.179  1.000 37.920  ? 237 LEU DDD O   1 
ATOM 7591  C CB  . LEU D 1 220 ? 164.944 -9.811  65.921  1.000 33.830  ? 237 LEU DDD CB  1 
ATOM 7592  C CG  . LEU D 1 220 ? 165.500 -11.233 65.842  1.000 34.380  ? 237 LEU DDD CG  1 
ATOM 7593  C CD1 . LEU D 1 220 ? 166.951 -11.216 65.440  1.000 37.860  ? 237 LEU DDD CD1 1 
ATOM 7594  C CD2 . LEU D 1 220 ? 165.380 -11.935 67.164  1.000 35.540  ? 237 LEU DDD CD2 1 
ATOM 7595  N N   . ASP D 1 221 ? 163.139 -7.487  67.380  1.000 43.090  ? 238 ASP DDD N   1 
ATOM 7596  C CA  . ASP D 1 221 ? 162.731 -6.060  67.487  1.000 44.160  ? 238 ASP DDD CA  1 
ATOM 7597  C C   . ASP D 1 221 ? 163.942 -5.179  67.187  1.000 42.790  ? 238 ASP DDD C   1 
ATOM 7598  O O   . ASP D 1 221 ? 164.994 -5.742  66.840  1.000 32.210  ? 238 ASP DDD O   1 
ATOM 7599  C CB  . ASP D 1 221 ? 162.132 -5.759  68.871  1.000 46.470  ? 238 ASP DDD CB  1 
ATOM 7600  C CG  . ASP D 1 221 ? 163.086 -5.874  70.047  1.000 41.550  ? 238 ASP DDD CG  1 
ATOM 7601  O OD1 . ASP D 1 221 ? 164.265 -6.155  69.828  1.000 45.660  ? 238 ASP DDD OD1 1 
ATOM 7602  O OD2 . ASP D 1 221 ? 162.632 -5.679  71.166  1.000 38.920  ? 238 ASP DDD OD2 1 
ATOM 7603  N N   . GLU D 1 222 ? 163.775 -3.857  67.344  1.000 50.000  ? 239 GLU DDD N   1 
ATOM 7604  C CA  . GLU D 1 222 ? 164.803 -2.784  67.198  1.000 56.550  ? 239 GLU DDD CA  1 
ATOM 7605  C C   . GLU D 1 222 ? 166.118 -3.203  67.859  1.000 50.970  ? 239 GLU DDD C   1 
ATOM 7606  O O   . GLU D 1 222 ? 167.173 -2.799  67.349  1.000 46.050  ? 239 GLU DDD O   1 
ATOM 7607  C CB  . GLU D 1 222 ? 164.379 -1.470  67.890  1.000 62.640  ? 239 GLU DDD CB  1 
ATOM 7608  C CG  . GLU D 1 222 ? 163.000 -0.947  67.506  1.000 70.750  ? 239 GLU DDD CG  1 
ATOM 7609  C CD  . GLU D 1 222 ? 161.807 -1.457  68.306  1.000 71.040  ? 239 GLU DDD CD  1 
ATOM 7610  O OE1 . GLU D 1 222 ? 161.030 -2.278  67.745  1.000 59.250  ? 239 GLU DDD OE1 1 
ATOM 7611  O OE2 . GLU D 1 222 ? 161.683 -1.067  69.481  1.000 75.800  ? 239 GLU DDD OE2 1 
ATOM 7612  N N   . PHE D 1 223 ? 166.038 -3.960  68.965  1.000 46.200  ? 240 PHE DDD N   1 
ATOM 7613  C CA  . PHE D 1 223 ? 167.179 -4.329  69.845  1.000 40.650  ? 240 PHE DDD CA  1 
ATOM 7614  C C   . PHE D 1 223 ? 167.607 -5.781  69.618  1.000 39.110  ? 240 PHE DDD C   1 
ATOM 7615  O O   . PHE D 1 223 ? 168.331 -6.312  70.457  1.000 39.630  ? 240 PHE DDD O   1 
ATOM 7616  C CB  . PHE D 1 223 ? 166.805 -4.174  71.322  1.000 41.570  ? 240 PHE DDD CB  1 
ATOM 7617  C CG  . PHE D 1 223 ? 166.287 -2.820  71.738  1.000 45.980  ? 240 PHE DDD CG  1 
ATOM 7618  C CD1 . PHE D 1 223 ? 164.961 -2.503  71.521  1.000 51.450  ? 240 PHE DDD CD1 1 
ATOM 7619  C CD2 . PHE D 1 223 ? 167.105 -1.859  72.324  1.000 51.700  ? 240 PHE DDD CD2 1 
ATOM 7620  C CE1 . PHE D 1 223 ? 164.448 -1.270  71.894  1.000 55.810  ? 240 PHE DDD CE1 1 
ATOM 7621  C CE2 . PHE D 1 223 ? 166.601 -0.613  72.654  1.000 57.520  ? 240 PHE DDD CE2 1 
ATOM 7622  C CZ  . PHE D 1 223 ? 165.268 -0.326  72.455  1.000 57.580  ? 240 PHE DDD CZ  1 
ATOM 7623  N N   . GLY D 1 224 ? 167.153 -6.438  68.552  1.000 37.850  ? 241 GLY DDD N   1 
ATOM 7624  C CA  . GLY D 1 224 ? 167.602 -7.801  68.191  1.000 40.480  ? 241 GLY DDD CA  1 
ATOM 7625  C C   . GLY D 1 224 ? 167.117 -8.881  69.145  1.000 40.170  ? 241 GLY DDD C   1 
ATOM 7626  O O   . GLY D 1 224 ? 167.722 -9.973  69.141  1.000 39.900  ? 241 GLY DDD O   1 
ATOM 7627  N N   . VAL D 1 225 ? 166.047 -8.597  69.898  1.000 38.870  ? 242 VAL DDD N   1 
ATOM 7628  C CA  . VAL D 1 225 ? 165.348 -9.554  70.805  1.000 35.590  ? 242 VAL DDD CA  1 
ATOM 7629  C C   . VAL D 1 225 ? 163.994 -9.957  70.200  1.000 33.140  ? 242 VAL DDD C   1 
ATOM 7630  O O   . VAL D 1 225 ? 163.169 -9.055  69.909  1.000 33.840  ? 242 VAL DDD O   1 
ATOM 7631  C CB  . VAL D 1 225 ? 165.138 -8.928  72.188  1.000 34.760  ? 242 VAL DDD CB  1 
ATOM 7632  C CG1 . VAL D 1 225 ? 164.589 -9.954  73.161  1.000 37.640  ? 242 VAL DDD CG1 1 
ATOM 7633  C CG2 . VAL D 1 225 ? 166.410 -8.319  72.729  1.000 33.950  ? 242 VAL DDD CG2 1 
ATOM 7634  N N   . GLY D 1 226 ? 163.753 -11.259 70.057  1.000 29.380  ? 243 GLY DDD N   1 
ATOM 7635  C CA  . GLY D 1 226 ? 162.453 -11.807 69.625  1.000 31.530  ? 243 GLY DDD CA  1 
ATOM 7636  C C   . GLY D 1 226 ? 161.519 -11.930 70.812  1.000 33.020  ? 243 GLY DDD C   1 
ATOM 7637  O O   . GLY D 1 226 ? 161.903 -11.595 71.936  1.000 35.780  ? 243 GLY DDD O   1 
ATOM 7638  N N   . PRO D 1 227 ? 160.255 -12.362 70.612  1.000 33.940  ? 244 PRO DDD N   1 
ATOM 7639  C CA  . PRO D 1 227 ? 159.387 -12.710 71.735  1.000 34.180  ? 244 PRO DDD CA  1 
ATOM 7640  C C   . PRO D 1 227 ? 160.088 -13.733 72.642  1.000 33.760  ? 244 PRO DDD C   1 
ATOM 7641  O O   . PRO D 1 227 ? 160.807 -14.599 72.117  1.000 30.970  ? 244 PRO DDD O   1 
ATOM 7642  C CB  . PRO D 1 227 ? 158.135 -13.308 71.074  1.000 34.260  ? 244 PRO DDD CB  1 
ATOM 7643  C CG  . PRO D 1 227 ? 158.107 -12.631 69.724  1.000 34.080  ? 244 PRO DDD CG  1 
ATOM 7644  C CD  . PRO D 1 227 ? 159.567 -12.481 69.322  1.000 34.340  ? 244 PRO DDD CD  1 
ATOM 7645  N N   . LEU D 1 228 ? 159.889 -13.591 73.959  1.000 32.160  ? 245 LEU DDD N   1 
ATOM 7646  C CA  . LEU D 1 228 ? 160.419 -14.519 74.978  1.000 33.640  ? 245 LEU DDD CA  1 
ATOM 7647  C C   . LEU D 1 228 ? 159.265 -15.360 75.545  1.000 29.820  ? 245 LEU DDD C   1 
ATOM 7648  O O   . LEU D 1 228 ? 158.296 -14.776 76.045  1.000 25.350  ? 245 LEU DDD O   1 
ATOM 7649  C CB  . LEU D 1 228 ? 161.136 -13.681 76.043  1.000 33.900  ? 245 LEU DDD CB  1 
ATOM 7650  C CG  . LEU D 1 228 ? 162.436 -13.005 75.596  1.000 33.010  ? 245 LEU DDD CG  1 
ATOM 7651  C CD1 . LEU D 1 228 ? 163.186 -12.446 76.789  1.000 31.520  ? 245 LEU DDD CD1 1 
ATOM 7652  C CD2 . LEU D 1 228 ? 163.399 -13.933 74.882  1.000 31.780  ? 245 LEU DDD CD2 1 
ATOM 7653  N N   . CYS D 1 229 ? 159.388 -16.677 75.467  1.000 27.770  ? 246 CYS DDD N   1 
ATOM 7654  C CA  . CYS D 1 229 ? 158.314 -17.639 75.803  1.000 28.910  ? 246 CYS DDD CA  1 
ATOM 7655  C C   . CYS D 1 229 ? 158.241 -17.877 77.316  1.000 28.600  ? 246 CYS DDD C   1 
ATOM 7656  O O   . CYS D 1 229 ? 158.853 -18.856 77.801  1.000 25.000  ? 246 CYS DDD O   1 
ATOM 7657  C CB  . CYS D 1 229 ? 158.573 -18.949 75.079  1.000 29.540  ? 246 CYS DDD CB  1 
ATOM 7658  S SG  . CYS D 1 229 ? 158.437 -18.742 73.298  1.000 30.050  ? 246 CYS DDD SG  1 
ATOM 7659  N N   . LYS D 1 230 ? 157.509 -17.012 78.022  1.000 29.310  ? 247 LYS DDD N   1 
ATOM 7660  C CA  . LYS D 1 230 ? 157.164 -17.160 79.451  1.000 31.170  ? 247 LYS DDD CA  1 
ATOM 7661  C C   . LYS D 1 230 ? 156.523 -18.535 79.656  1.000 30.230  ? 247 LYS DDD C   1 
ATOM 7662  O O   . LYS D 1 230 ? 155.643 -18.918 78.867  1.000 30.270  ? 247 LYS DDD O   1 
ATOM 7663  C CB  . LYS D 1 230 ? 156.245 -16.012 79.871  1.000 35.230  ? 247 LYS DDD CB  1 
ATOM 7664  C CG  . LYS D 1 230 ? 156.987 -14.697 80.056  1.000 40.850  ? 247 LYS DDD CG  1 
ATOM 7665  C CD  . LYS D 1 230 ? 156.167 -13.438 80.223  1.000 48.660  ? 247 LYS DDD CD  1 
ATOM 7666  C CE  . LYS D 1 230 ? 156.969 -12.182 79.901  1.000 50.370  ? 247 LYS DDD CE  1 
ATOM 7667  N NZ  . LYS D 1 230 ? 156.327 -10.963 80.450  1.000 51.550  ? 247 LYS DDD NZ  1 
ATOM 7668  N N   . GLY D 1 231 ? 156.958 -19.252 80.690  1.000 31.310  ? 248 GLY DDD N   1 
ATOM 7669  C CA  . GLY D 1 231 ? 156.415 -20.562 81.087  1.000 31.960  ? 248 GLY DDD CA  1 
ATOM 7670  C C   . GLY D 1 231 ? 156.778 -21.644 80.091  1.000 32.930  ? 248 GLY DDD C   1 
ATOM 7671  O O   . GLY D 1 231 ? 156.087 -22.662 80.065  1.000 42.230  ? 248 GLY DDD O   1 
ATOM 7672  N N   . ASP D 1 232 ? 157.819 -21.432 79.294  1.000 31.320  ? 249 ASP DDD N   1 
ATOM 7673  C CA  . ASP D 1 232 ? 158.247 -22.364 78.226  1.000 32.550  ? 249 ASP DDD CA  1 
ATOM 7674  C C   . ASP D 1 232 ? 157.081 -22.617 77.262  1.000 32.120  ? 249 ASP DDD C   1 
ATOM 7675  O O   . ASP D 1 232 ? 156.946 -23.743 76.782  1.000 38.790  ? 249 ASP DDD O   1 
ATOM 7676  C CB  . ASP D 1 232 ? 158.869 -23.587 78.888  1.000 35.780  ? 249 ASP DDD CB  1 
ATOM 7677  C CG  . ASP D 1 232 ? 160.250 -23.279 79.455  1.000 42.080  ? 249 ASP DDD CG  1 
ATOM 7678  O OD1 . ASP D 1 232 ? 160.844 -22.255 78.994  1.000 45.710  ? 249 ASP DDD OD1 1 
ATOM 7679  O OD2 . ASP D 1 232 ? 160.752 -24.079 80.321  1.000 45.330  ? 249 ASP DDD OD2 1 
ATOM 7680  N N   . ASN D 1 233 ? 156.299 -21.589 76.947  1.000 32.490  ? 250 ASN DDD N   1 
ATOM 7681  C CA  . ASN D 1 233 ? 155.135 -21.649 76.022  1.000 34.490  ? 250 ASN DDD CA  1 
ATOM 7682  C C   . ASN D 1 233 ? 155.249 -20.629 74.877  1.000 36.090  ? 250 ASN DDD C   1 
ATOM 7683  O O   . ASN D 1 233 ? 155.615 -19.456 75.127  1.000 36.640  ? 250 ASN DDD O   1 
ATOM 7684  C CB  . ASN D 1 233 ? 153.834 -21.387 76.771  1.000 37.500  ? 250 ASN DDD CB  1 
ATOM 7685  C CG  . ASN D 1 233 ? 153.436 -22.538 77.659  1.000 38.480  ? 250 ASN DDD CG  1 
ATOM 7686  O OD1 . ASN D 1 233 ? 153.799 -23.690 77.414  1.000 38.380  ? 250 ASN DDD OD1 1 
ATOM 7687  N ND2 . ASN D 1 233 ? 152.677 -22.227 78.692  1.000 43.760  ? 250 ASN DDD ND2 1 
ATOM 7688  N N   . LEU D 1 234 ? 154.924 -21.063 73.665  1.000 33.920  ? 251 LEU DDD N   1 
ATOM 7689  C CA  . LEU D 1 234 ? 154.853 -20.221 72.447  1.000 32.230  ? 251 LEU DDD CA  1 
ATOM 7690  C C   . LEU D 1 234 ? 153.385 -20.079 72.076  1.000 33.340  ? 251 LEU DDD C   1 
ATOM 7691  O O   . LEU D 1 234 ? 152.702 -21.121 72.065  1.000 30.030  ? 251 LEU DDD O   1 
ATOM 7692  C CB  . LEU D 1 234 ? 155.628 -20.911 71.325  1.000 30.720  ? 251 LEU DDD CB  1 
ATOM 7693  C CG  . LEU D 1 234 ? 155.675 -20.155 70.000  1.000 31.740  ? 251 LEU DDD CG  1 
ATOM 7694  C CD1 . LEU D 1 234 ? 156.449 -18.856 70.172  1.000 33.240  ? 251 LEU DDD CD1 1 
ATOM 7695  C CD2 . LEU D 1 234 ? 156.277 -21.012 68.906  1.000 31.550  ? 251 LEU DDD CD2 1 
ATOM 7696  N N   . TYR D 1 235 ? 152.945 -18.857 71.770  1.000 36.400  ? 252 TYR DDD N   1 
ATOM 7697  C CA  . TYR D 1 235 ? 151.527 -18.525 71.473  1.000 38.680  ? 252 TYR DDD CA  1 
ATOM 7698  C C   . TYR D 1 235 ? 151.382 -18.115 69.997  1.000 39.210  ? 252 TYR DDD C   1 
ATOM 7699  O O   . TYR D 1 235 ? 151.768 -16.997 69.601  1.000 51.930  ? 252 TYR DDD O   1 
ATOM 7700  C CB  . TYR D 1 235 ? 151.036 -17.433 72.424  1.000 41.330  ? 252 TYR DDD CB  1 
ATOM 7701  C CG  . TYR D 1 235 ? 150.650 -17.891 73.805  1.000 42.830  ? 252 TYR DDD CG  1 
ATOM 7702  C CD1 . TYR D 1 235 ? 151.613 -18.131 74.770  1.000 49.580  ? 252 TYR DDD CD1 1 
ATOM 7703  C CD2 . TYR D 1 235 ? 149.321 -18.059 74.159  1.000 43.270  ? 252 TYR DDD CD2 1 
ATOM 7704  C CE1 . TYR D 1 235 ? 151.263 -18.552 76.046  1.000 51.960  ? 252 TYR DDD CE1 1 
ATOM 7705  C CE2 . TYR D 1 235 ? 148.947 -18.481 75.430  1.000 47.630  ? 252 TYR DDD CE2 1 
ATOM 7706  C CZ  . TYR D 1 235 ? 149.928 -18.731 76.377  1.000 51.450  ? 252 TYR DDD CZ  1 
ATOM 7707  O OH  . TYR D 1 235 ? 149.576 -19.138 77.632  1.000 53.220  ? 252 TYR DDD OH  1 
ATOM 7708  N N   . LEU D 1 236 ? 150.790 -18.999 69.206  1.000 35.280  ? 253 LEU DDD N   1 
ATOM 7709  C CA  . LEU D 1 236 ? 150.386 -18.715 67.810  1.000 34.350  ? 253 LEU DDD CA  1 
ATOM 7710  C C   . LEU D 1 236 ? 148.914 -18.311 67.818  1.000 37.690  ? 253 LEU DDD C   1 
ATOM 7711  O O   . LEU D 1 236 ? 148.087 -19.081 68.338  1.000 41.610  ? 253 LEU DDD O   1 
ATOM 7712  C CB  . LEU D 1 236 ? 150.639 -19.951 66.943  1.000 32.180  ? 253 LEU DDD CB  1 
ATOM 7713  C CG  . LEU D 1 236 ? 152.019 -20.572 67.124  1.000 31.910  ? 253 LEU DDD CG  1 
ATOM 7714  C CD1 . LEU D 1 236 ? 152.236 -21.672 66.124  1.000 32.650  ? 253 LEU DDD CD1 1 
ATOM 7715  C CD2 . LEU D 1 236 ? 153.106 -19.534 66.979  1.000 32.920  ? 253 LEU DDD CD2 1 
ATOM 7716  N N   . SER D 1 237 ? 148.632 -17.113 67.308  1.000 37.060  ? 254 SER DDD N   1 
ATOM 7717  C CA  . SER D 1 237 ? 147.267 -16.592 67.053  1.000 33.350  ? 254 SER DDD CA  1 
ATOM 7718  C C   . SER D 1 237 ? 147.126 -16.300 65.553  1.000 30.040  ? 254 SER DDD C   1 
ATOM 7719  O O   . SER D 1 237 ? 148.162 -16.019 64.902  1.000 28.800  ? 254 SER DDD O   1 
ATOM 7720  C CB  . SER D 1 237 ? 147.022 -15.386 67.910  1.000 34.410  ? 254 SER DDD CB  1 
ATOM 7721  O OG  . SER D 1 237 ? 147.667 -15.543 69.173  1.000 38.590  ? 254 SER DDD OG  1 
ATOM 7722  N N   . ALA D 1 238 ? 145.911 -16.419 65.008  1.000 26.180  ? 255 ALA DDD N   1 
ATOM 7723  C CA  . ALA D 1 238 ? 145.638 -16.251 63.561  1.000 25.780  ? 255 ALA DDD CA  1 
ATOM 7724  C C   . ALA D 1 238 ? 144.155 -16.018 63.306  1.000 25.370  ? 255 ALA DDD C   1 
ATOM 7725  O O   . ALA D 1 238 ? 143.355 -16.526 64.088  1.000 26.910  ? 255 ALA DDD O   1 
ATOM 7726  C CB  . ALA D 1 238 ? 146.097 -17.481 62.837  1.000 25.140  ? 255 ALA DDD CB  1 
ATOM 7727  N N   . VAL D 1 239 ? 143.840 -15.276 62.249  1.000 24.290  ? 256 VAL DDD N   1 
ATOM 7728  C CA  . VAL D 1 239 ? 142.481 -15.208 61.647  1.000 25.430  ? 256 VAL DDD CA  1 
ATOM 7729  C C   . VAL D 1 239 ? 142.677 -15.158 60.149  1.000 26.950  ? 256 VAL DDD C   1 
ATOM 7730  O O   . VAL D 1 239 ? 143.534 -14.367 59.735  1.000 33.140  ? 256 VAL DDD O   1 
ATOM 7731  C CB  . VAL D 1 239 ? 141.705 -13.948 62.065  1.000 27.040  ? 256 VAL DDD CB  1 
ATOM 7732  C CG1 . VAL D 1 239 ? 140.315 -13.924 61.430  1.000 26.790  ? 256 VAL DDD CG1 1 
ATOM 7733  C CG2 . VAL D 1 239 ? 141.598 -13.823 63.572  1.000 28.600  ? 256 VAL DDD CG2 1 
ATOM 7734  N N   . ASP D 1 240 ? 141.888 -15.899 59.374  1.000 27.080  ? 257 ASP DDD N   1 
ATOM 7735  C CA  . ASP D 1 240 ? 141.964 -15.823 57.890  1.000 26.340  ? 257 ASP DDD CA  1 
ATOM 7736  C C   . ASP D 1 240 ? 140.560 -15.921 57.295  1.000 26.860  ? 257 ASP DDD C   1 
ATOM 7737  O O   . ASP D 1 240 ? 140.275 -16.910 56.583  1.000 28.940  ? 257 ASP DDD O   1 
ATOM 7738  C CB  . ASP D 1 240 ? 142.896 -16.908 57.376  1.000 25.620  ? 257 ASP DDD CB  1 
ATOM 7739  C CG  . ASP D 1 240 ? 144.351 -16.599 57.662  1.000 24.270  ? 257 ASP DDD CG  1 
ATOM 7740  O OD1 . ASP D 1 240 ? 144.899 -15.716 56.976  1.000 20.840  ? 257 ASP DDD OD1 1 
ATOM 7741  O OD2 . ASP D 1 240 ? 144.907 -17.248 58.573  1.000 25.370  ? 257 ASP DDD OD2 1 
ATOM 7742  N N   . VAL D 1 241 ? 139.706 -14.954 57.615  1.000 25.700  ? 258 VAL DDD N   1 
ATOM 7743  C CA  . VAL D 1 241 ? 138.377 -14.803 56.966  1.000 26.210  ? 258 VAL DDD CA  1 
ATOM 7744  C C   . VAL D 1 241 ? 138.674 -14.396 55.523  1.000 26.370  ? 258 VAL DDD C   1 
ATOM 7745  O O   . VAL D 1 241 ? 139.215 -13.292 55.350  1.000 25.900  ? 258 VAL DDD O   1 
ATOM 7746  C CB  . VAL D 1 241 ? 137.504 -13.769 57.694  1.000 26.740  ? 258 VAL DDD CB  1 
ATOM 7747  C CG1 . VAL D 1 241 ? 136.182 -13.551 56.980  1.000 27.390  ? 258 VAL DDD CG1 1 
ATOM 7748  C CG2 . VAL D 1 241 ? 137.260 -14.168 59.136  1.000 27.500  ? 258 VAL DDD CG2 1 
ATOM 7749  N N   . CYS D 1 242 ? 138.427 -15.286 54.554  1.000 25.060  ? 259 CYS DDD N   1 
ATOM 7750  C CA  . CYS D 1 242 ? 138.924 -15.150 53.166  1.000 23.770  ? 259 CYS DDD CA  1 
ATOM 7751  C C   . CYS D 1 242 ? 137.974 -14.293 52.355  1.000 23.370  ? 259 CYS DDD C   1 
ATOM 7752  O O   . CYS D 1 242 ? 138.442 -13.712 51.341  1.000 23.960  ? 259 CYS DDD O   1 
ATOM 7753  C CB  . CYS D 1 242 ? 139.041 -16.499 52.496  1.000 25.150  ? 259 CYS DDD CB  1 
ATOM 7754  S SG  . CYS D 1 242 ? 140.463 -17.409 53.121  1.000 28.780  ? 259 CYS DDD SG  1 
ATOM 7755  N N   . GLY D 1 243 ? 136.723 -14.233 52.809  1.000 22.770  ? 260 GLY DDD N   1 
ATOM 7756  C CA  . GLY D 1 243 ? 135.601 -13.626 52.078  1.000 23.500  ? 260 GLY DDD CA  1 
ATOM 7757  C C   . GLY D 1 243 ? 134.303 -14.309 52.450  1.000 23.650  ? 260 GLY DDD C   1 
ATOM 7758  O O   . GLY D 1 243 ? 134.257 -14.959 53.515  1.000 21.780  ? 260 GLY DDD O   1 
ATOM 7759  N N   . MET D 1 244 ? 133.296 -14.176 51.603  1.000 23.510  ? 261 MET DDD N   1 
ATOM 7760  C CA  . MET D 1 244 ? 131.989 -14.867 51.775  1.000 25.630  ? 261 MET DDD CA  1 
ATOM 7761  C C   . MET D 1 244 ? 131.764 -15.812 50.601  1.000 26.950  ? 261 MET DDD C   1 
ATOM 7762  O O   . MET D 1 244 ? 132.121 -15.460 49.453  1.000 28.250  ? 261 MET DDD O   1 
ATOM 7763  C CB  . MET D 1 244 ? 130.827 -13.885 51.828  1.000 25.190  ? 261 MET DDD CB  1 
ATOM 7764  C CG  . MET D 1 244 ? 130.961 -12.890 52.924  1.000 26.260  ? 261 MET DDD CG  1 
ATOM 7765  S SD  . MET D 1 244 ? 129.541 -11.807 52.918  1.000 29.100  ? 261 MET DDD SD  1 
ATOM 7766  C CE  . MET D 1 244 ? 129.904 -10.871 54.405  1.000 28.070  ? 261 MET DDD CE  1 
ATOM 7767  N N   . PHE D 1 245 ? 131.201 -16.980 50.908  1.000 26.600  ? 262 PHE DDD N   1 
ATOM 7768  C CA  . PHE D 1 245 ? 130.612 -17.920 49.931  1.000 25.440  ? 262 PHE DDD CA  1 
ATOM 7769  C C   . PHE D 1 245 ? 129.197 -17.440 49.666  1.000 23.910  ? 262 PHE DDD C   1 
ATOM 7770  O O   . PHE D 1 245 ? 128.494 -17.259 50.641  1.000 22.840  ? 262 PHE DDD O   1 
ATOM 7771  C CB  . PHE D 1 245 ? 130.594 -19.354 50.461  1.000 26.210  ? 262 PHE DDD CB  1 
ATOM 7772  C CG  . PHE D 1 245 ? 129.852 -20.307 49.564  1.000 25.710  ? 262 PHE DDD CG  1 
ATOM 7773  C CD1 . PHE D 1 245 ? 130.255 -20.487 48.254  1.000 24.310  ? 262 PHE DDD CD1 1 
ATOM 7774  C CD2 . PHE D 1 245 ? 128.741 -20.995 50.017  1.000 26.560  ? 262 PHE DDD CD2 1 
ATOM 7775  C CE1 . PHE D 1 245 ? 129.575 -21.349 47.410  1.000 24.460  ? 262 PHE DDD CE1 1 
ATOM 7776  C CE2 . PHE D 1 245 ? 128.061 -21.853 49.163  1.000 27.110  ? 262 PHE DDD CE2 1 
ATOM 7777  C CZ  . PHE D 1 245 ? 128.473 -22.024 47.859  1.000 25.130  ? 262 PHE DDD CZ  1 
ATOM 7778  N N   . THR D 1 246 ? 128.839 -17.189 48.412  1.000 24.300  ? 263 THR DDD N   1 
ATOM 7779  C CA  . THR D 1 246 ? 127.458 -16.811 48.030  1.000 24.230  ? 263 THR DDD CA  1 
ATOM 7780  C C   . THR D 1 246 ? 126.748 -18.081 47.539  1.000 26.480  ? 263 THR DDD C   1 
ATOM 7781  O O   . THR D 1 246 ? 127.133 -18.648 46.463  1.000 31.160  ? 263 THR DDD O   1 
ATOM 7782  C CB  . THR D 1 246 ? 127.433 -15.668 47.012  1.000 23.130  ? 263 THR DDD CB  1 
ATOM 7783  O OG1 . THR D 1 246 ? 128.227 -14.578 47.489  1.000 24.690  ? 263 THR DDD OG1 1 
ATOM 7784  C CG2 . THR D 1 246 ? 126.019 -15.222 46.755  1.000 21.710  ? 263 THR DDD CG2 1 
ATOM 7785  N N   . ASN D 1 247 ? 125.787 -18.544 48.336  1.000 24.550  ? 264 ASN DDD N   1 
ATOM 7786  C CA  . ASN D 1 247 ? 124.874 -19.655 48.006  1.000 23.710  ? 264 ASN DDD CA  1 
ATOM 7787  C C   . ASN D 1 247 ? 123.970 -19.264 46.830  1.000 23.870  ? 264 ASN DDD C   1 
ATOM 7788  O O   . ASN D 1 247 ? 123.860 -18.078 46.540  1.000 23.710  ? 264 ASN DDD O   1 
ATOM 7789  C CB  . ASN D 1 247 ? 124.075 -20.052 49.246  1.000 23.510  ? 264 ASN DDD CB  1 
ATOM 7790  C CG  . ASN D 1 247 ? 124.832 -21.028 50.117  1.000 22.790  ? 264 ASN DDD CG  1 
ATOM 7791  O OD1 . ASN D 1 247 ? 124.814 -22.257 49.841  1.000 22.100  ? 264 ASN DDD OD1 1 
ATOM 7792  N ND2 . ASN D 1 247 ? 125.500 -20.480 51.128  1.000 19.420  ? 264 ASN DDD ND2 1 
ATOM 7793  N N   . ARG D 1 248 ? 123.355 -20.261 46.190  1.000 24.870  ? 265 ARG DDD N   1 
ATOM 7794  C CA  . ARG D 1 248 ? 122.414 -20.136 45.048  1.000 23.230  ? 265 ARG DDD CA  1 
ATOM 7795  C C   . ARG D 1 248 ? 121.333 -19.107 45.376  1.000 22.300  ? 265 ARG DDD C   1 
ATOM 7796  O O   . ARG D 1 248 ? 121.002 -18.331 44.475  1.000 22.170  ? 265 ARG DDD O   1 
ATOM 7797  C CB  . ARG D 1 248 ? 121.823 -21.514 44.726  1.000 23.180  ? 265 ARG DDD CB  1 
ATOM 7798  C CG  . ARG D 1 248 ? 120.448 -21.476 44.095  1.000 24.150  ? 265 ARG DDD CG  1 
ATOM 7799  C CD  . ARG D 1 248 ? 119.907 -22.872 43.779  1.000 24.050  ? 265 ARG DDD CD  1 
ATOM 7800  N NE  . ARG D 1 248 ? 120.108 -23.344 42.415  1.000 21.250  ? 265 ARG DDD NE  1 
ATOM 7801  C CZ  . ARG D 1 248 ? 120.977 -24.268 42.055  1.000 23.390  ? 265 ARG DDD CZ  1 
ATOM 7802  N NH1 . ARG D 1 248 ? 121.747 -24.846 42.940  1.000 24.470  ? 265 ARG DDD NH1 1 
ATOM 7803  N NH2 . ARG D 1 248 ? 121.101 -24.654 40.797  1.000 28.290  ? 265 ARG DDD NH2 1 
ATOM 7804  N N   . SER D 1 249 ? 120.833 -19.078 46.610  1.000 21.940  ? 266 SER DDD N   1 
ATOM 7805  C CA  . SER D 1 249 ? 119.733 -18.170 47.041  1.000 23.050  ? 266 SER DDD CA  1 
ATOM 7806  C C   . SER D 1 249 ? 120.206 -16.720 47.112  1.000 24.170  ? 266 SER DDD C   1 
ATOM 7807  O O   . SER D 1 249 ? 119.347 -15.829 47.311  1.000 24.890  ? 266 SER DDD O   1 
ATOM 7808  C CB  . SER D 1 249 ? 119.222 -18.520 48.399  1.000 23.460  ? 266 SER DDD CB  1 
ATOM 7809  O OG  . SER D 1 249 ? 120.217 -18.231 49.365  1.000 25.530  ? 266 SER DDD OG  1 
ATOM 7810  N N   . GLY D 1 250 ? 121.527 -16.516 47.123  1.000 24.010  ? 267 GLY DDD N   1 
ATOM 7811  C CA  . GLY D 1 250 ? 122.165 -15.215 47.395  1.000 22.730  ? 267 GLY DDD CA  1 
ATOM 7812  C C   . GLY D 1 250 ? 122.635 -15.091 48.838  1.000 21.830  ? 267 GLY DDD C   1 
ATOM 7813  O O   . GLY D 1 250 ? 123.421 -14.160 49.119  1.000 22.090  ? 267 GLY DDD O   1 
ATOM 7814  N N   . SER D 1 251 ? 122.176 -15.971 49.736  1.000 21.040  ? 268 SER DDD N   1 
ATOM 7815  C CA  . SER D 1 251 ? 122.567 -15.986 51.173  1.000 19.160  ? 268 SER DDD CA  1 
ATOM 7816  C C   . SER D 1 251 ? 124.082 -16.197 51.275  1.000 19.010  ? 268 SER DDD C   1 
ATOM 7817  O O   . SER D 1 251 ? 124.611 -16.993 50.518  1.000 17.660  ? 268 SER DDD O   1 
ATOM 7818  C CB  . SER D 1 251 ? 121.763 -17.012 51.943  1.000 17.860  ? 268 SER DDD CB  1 
ATOM 7819  O OG  . SER D 1 251 ? 120.412 -17.029 51.529  1.000 17.270  ? 268 SER DDD OG  1 
ATOM 7820  N N   . GLN D 1 252 ? 124.744 -15.491 52.172  1.000 21.460  ? 269 GLN DDD N   1 
ATOM 7821  C CA  . GLN D 1 252 ? 126.224 -15.480 52.232  1.000 24.130  ? 269 GLN DDD CA  1 
ATOM 7822  C C   . GLN D 1 252 ? 126.727 -16.028 53.572  1.000 25.800  ? 269 GLN DDD C   1 
ATOM 7823  O O   . GLN D 1 252 ? 126.194 -15.637 54.624  1.000 33.880  ? 269 GLN DDD O   1 
ATOM 7824  C CB  . GLN D 1 252 ? 126.713 -14.050 52.040  1.000 27.500  ? 269 GLN DDD CB  1 
ATOM 7825  C CG  . GLN D 1 252 ? 126.661 -13.603 50.593  1.000 28.690  ? 269 GLN DDD CG  1 
ATOM 7826  C CD  . GLN D 1 252 ? 126.905 -12.127 50.402  1.000 29.500  ? 269 GLN DDD CD  1 
ATOM 7827  O OE1 . GLN D 1 252 ? 126.690 -11.273 51.277  1.000 27.580  ? 269 GLN DDD OE1 1 
ATOM 7828  N NE2 . GLN D 1 252 ? 127.288 -11.824 49.175  1.000 32.730  ? 269 GLN DDD NE2 1 
ATOM 7829  N N   . GLN D 1 253 ? 127.764 -16.862 53.519  1.000 25.090  ? 270 GLN DDD N   1 
ATOM 7830  C CA  . GLN D 1 253 ? 128.475 -17.469 54.677  1.000 24.310  ? 270 GLN DDD CA  1 
ATOM 7831  C C   . GLN D 1 253 ? 129.942 -17.054 54.595  1.000 21.990  ? 270 GLN DDD C   1 
ATOM 7832  O O   . GLN D 1 253 ? 130.533 -17.226 53.549  1.000 23.250  ? 270 GLN DDD O   1 
ATOM 7833  C CB  . GLN D 1 253 ? 128.375 -18.997 54.653  1.000 25.310  ? 270 GLN DDD CB  1 
ATOM 7834  C CG  . GLN D 1 253 ? 126.946 -19.514 54.779  1.000 27.050  ? 270 GLN DDD CG  1 
ATOM 7835  C CD  . GLN D 1 253 ? 126.830 -20.964 54.390  1.000 29.400  ? 270 GLN DDD CD  1 
ATOM 7836  O OE1 . GLN D 1 253 ? 126.612 -21.307 53.229  1.000 32.340  ? 270 GLN DDD OE1 1 
ATOM 7837  N NE2 . GLN D 1 253 ? 127.001 -21.828 55.368  1.000 30.970  ? 270 GLN DDD NE2 1 
ATOM 7838  N N   . TRP D 1 254 ? 130.499 -16.511 55.662  1.000 19.780  ? 271 TRP DDD N   1 
ATOM 7839  C CA  . TRP D 1 254 ? 131.959 -16.334 55.782  1.000 19.640  ? 271 TRP DDD CA  1 
ATOM 7840  C C   . TRP D 1 254 ? 132.629 -17.668 55.449  1.000 20.570  ? 271 TRP DDD C   1 
ATOM 7841  O O   . TRP D 1 254 ? 132.056 -18.687 55.858  1.000 23.050  ? 271 TRP DDD O   1 
ATOM 7842  C CB  . TRP D 1 254 ? 132.300 -15.915 57.203  1.000 19.030  ? 271 TRP DDD CB  1 
ATOM 7843  C CG  . TRP D 1 254 ? 131.747 -14.604 57.644  1.000 17.590  ? 271 TRP DDD CG  1 
ATOM 7844  C CD1 . TRP D 1 254 ? 130.805 -14.398 58.595  1.000 18.030  ? 271 TRP DDD CD1 1 
ATOM 7845  C CD2 . TRP D 1 254 ? 132.160 -13.317 57.194  1.000 17.890  ? 271 TRP DDD CD2 1 
ATOM 7846  N NE1 . TRP D 1 254 ? 130.587 -13.068 58.755  1.000 19.380  ? 271 TRP DDD NE1 1 
ATOM 7847  C CE2 . TRP D 1 254 ? 131.395 -12.379 57.897  1.000 18.760  ? 271 TRP DDD CE2 1 
ATOM 7848  C CE3 . TRP D 1 254 ? 133.071 -12.867 56.240  1.000 19.040  ? 271 TRP DDD CE3 1 
ATOM 7849  C CZ2 . TRP D 1 254 ? 131.531 -11.010 57.697  1.000 19.550  ? 271 TRP DDD CZ2 1 
ATOM 7850  C CZ3 . TRP D 1 254 ? 133.203 -11.512 56.034  1.000 19.620  ? 271 TRP DDD CZ3 1 
ATOM 7851  C CH2 . TRP D 1 254 ? 132.439 -10.598 56.754  1.000 19.650  ? 271 TRP DDD CH2 1 
ATOM 7852  N N   . ARG D 1 255 ? 133.784 -17.675 54.775  1.000 19.860  ? 272 ARG DDD N   1 
ATOM 7853  C CA  . ARG D 1 255 ? 134.585 -18.915 54.583  1.000 20.340  ? 272 ARG DDD CA  1 
ATOM 7854  C C   . ARG D 1 255 ? 136.018 -18.674 55.041  1.000 19.590  ? 272 ARG DDD C   1 
ATOM 7855  O O   . ARG D 1 255 ? 136.620 -17.666 54.615  1.000 21.490  ? 272 ARG DDD O   1 
ATOM 7856  C CB  . ARG D 1 255 ? 134.622 -19.365 53.123  1.000 21.190  ? 272 ARG DDD CB  1 
ATOM 7857  C CG  . ARG D 1 255 ? 135.452 -20.619 52.887  1.000 22.260  ? 272 ARG DDD CG  1 
ATOM 7858  C CD  . ARG D 1 255 ? 134.779 -21.808 53.555  1.000 24.230  ? 272 ARG DDD CD  1 
ATOM 7859  N NE  . ARG D 1 255 ? 135.149 -23.135 53.056  1.000 23.530  ? 272 ARG DDD NE  1 
ATOM 7860  C CZ  . ARG D 1 255 ? 136.149 -23.884 53.507  1.000 24.470  ? 272 ARG DDD CZ  1 
ATOM 7861  N NH1 . ARG D 1 255 ? 136.939 -23.468 54.483  1.000 26.330  ? 272 ARG DDD NH1 1 
ATOM 7862  N NH2 . ARG D 1 255 ? 136.353 -25.075 52.984  1.000 25.150  ? 272 ARG DDD NH2 1 
ATOM 7863  N N   . GLY D 1 256 ? 136.542 -19.581 55.858  1.000 18.410  ? 273 GLY DDD N   1 
ATOM 7864  C CA  . GLY D 1 256 ? 137.868 -19.440 56.475  1.000 18.000  ? 273 GLY DDD CA  1 
ATOM 7865  C C   . GLY D 1 256 ? 138.804 -20.503 55.990  1.000 17.210  ? 273 GLY DDD C   1 
ATOM 7866  O O   . GLY D 1 256 ? 138.323 -21.456 55.414  1.000 16.400  ? 273 GLY DDD O   1 
ATOM 7867  N N   . LEU D 1 257 ? 140.100 -20.329 56.223  1.000 18.600  ? 274 LEU DDD N   1 
ATOM 7868  C CA  . LEU D 1 257 ? 141.136 -21.338 55.882  1.000 21.030  ? 274 LEU DDD CA  1 
ATOM 7869  C C   . LEU D 1 257 ? 142.173 -21.427 56.995  1.000 22.090  ? 274 LEU DDD C   1 
ATOM 7870  O O   . LEU D 1 257 ? 142.454 -20.399 57.665  1.000 22.430  ? 274 LEU DDD O   1 
ATOM 7871  C CB  . LEU D 1 257 ? 141.800 -20.980 54.545  1.000 21.010  ? 274 LEU DDD CB  1 
ATOM 7872  C CG  . LEU D 1 257 ? 140.934 -21.173 53.303  1.000 20.630  ? 274 LEU DDD CG  1 
ATOM 7873  C CD1 . LEU D 1 257 ? 141.690 -20.700 52.082  1.000 20.670  ? 274 LEU DDD CD1 1 
ATOM 7874  C CD2 . LEU D 1 257 ? 140.526 -22.629 53.131  1.000 21.480  ? 274 LEU DDD CD2 1 
ATOM 7875  N N   . SER D 1 258 ? 142.741 -22.620 57.146  1.000 23.950  ? 275 SER DDD N   1 
ATOM 7876  C CA  . SER D 1 258 ? 143.827 -22.903 58.111  1.000 25.420  ? 275 SER DDD CA  1 
ATOM 7877  C C   . SER D 1 258 ? 145.066 -22.075 57.764  1.000 24.860  ? 275 SER DDD C   1 
ATOM 7878  O O   . SER D 1 258 ? 145.255 -21.742 56.586  1.000 23.470  ? 275 SER DDD O   1 
ATOM 7879  C CB  . SER D 1 258 ? 144.113 -24.366 58.132  1.000 27.360  ? 275 SER DDD CB  1 
ATOM 7880  O OG  . SER D 1 258 ? 142.918 -25.084 58.419  1.000 33.390  ? 275 SER DDD OG  1 
ATOM 7881  N N   . ARG D 1 259 ? 145.877 -21.750 58.762  1.000 26.700  ? 276 ARG DDD N   1 
ATOM 7882  C CA  . ARG D 1 259 ? 147.186 -21.072 58.583  1.000 28.720  ? 276 ARG DDD CA  1 
ATOM 7883  C C   . ARG D 1 259 ? 148.309 -21.970 59.119  1.000 29.830  ? 276 ARG DDD C   1 
ATOM 7884  O O   . ARG D 1 259 ? 148.254 -22.370 60.293  1.000 33.650  ? 276 ARG DDD O   1 
ATOM 7885  C CB  . ARG D 1 259 ? 147.190 -19.739 59.329  1.000 27.900  ? 276 ARG DDD CB  1 
ATOM 7886  C CG  . ARG D 1 259 ? 148.549 -19.051 59.314  1.000 28.670  ? 276 ARG DDD CG  1 
ATOM 7887  C CD  . ARG D 1 259 ? 148.455 -17.587 59.698  1.000 30.130  ? 276 ARG DDD CD  1 
ATOM 7888  N NE  . ARG D 1 259 ? 147.724 -16.830 58.687  1.000 30.160  ? 276 ARG DDD NE  1 
ATOM 7889  C CZ  . ARG D 1 259 ? 148.266 -16.214 57.653  1.000 29.740  ? 276 ARG DDD CZ  1 
ATOM 7890  N NH1 . ARG D 1 259 ? 149.572 -16.215 57.450  1.000 29.290  ? 276 ARG DDD NH1 1 
ATOM 7891  N NH2 . ARG D 1 259 ? 147.481 -15.574 56.821  1.000 32.010  ? 276 ARG DDD NH2 1 
ATOM 7892  N N   . TYR D 1 260 ? 149.313 -22.241 58.297  1.000 27.350  ? 277 TYR DDD N   1 
ATOM 7893  C CA  . TYR D 1 260 ? 150.565 -22.926 58.700  1.000 27.510  ? 277 TYR DDD CA  1 
ATOM 7894  C C   . TYR D 1 260 ? 151.491 -21.930 59.400  1.000 25.900  ? 277 TYR DDD C   1 
ATOM 7895  O O   . TYR D 1 260 ? 151.589 -20.777 58.957  1.000 25.790  ? 277 TYR DDD O   1 
ATOM 7896  C CB  . TYR D 1 260 ? 151.246 -23.476 57.454  1.000 30.020  ? 277 TYR DDD CB  1 
ATOM 7897  C CG  . TYR D 1 260 ? 152.645 -24.001 57.609  1.000 30.070  ? 277 TYR DDD CG  1 
ATOM 7898  C CD1 . TYR D 1 260 ? 152.861 -25.305 57.999  1.000 31.500  ? 277 TYR DDD CD1 1 
ATOM 7899  C CD2 . TYR D 1 260 ? 153.743 -23.227 57.269  1.000 29.610  ? 277 TYR DDD CD2 1 
ATOM 7900  C CE1 . TYR D 1 260 ? 154.141 -25.826 58.072  1.000 33.960  ? 277 TYR DDD CE1 1 
ATOM 7901  C CE2 . TYR D 1 260 ? 155.027 -23.723 57.355  1.000 30.260  ? 277 TYR DDD CE2 1 
ATOM 7902  C CZ  . TYR D 1 260 ? 155.226 -25.032 57.744  1.000 33.970  ? 277 TYR DDD CZ  1 
ATOM 7903  O OH  . TYR D 1 260 ? 156.486 -25.542 57.845  1.000 40.560  ? 277 TYR DDD OH  1 
ATOM 7904  N N   . PHE D 1 261 ? 152.150 -22.379 60.459  1.000 24.710  ? 278 PHE DDD N   1 
ATOM 7905  C CA  . PHE D 1 261 ? 153.253 -21.659 61.136  1.000 25.320  ? 278 PHE DDD CA  1 
ATOM 7906  C C   . PHE D 1 261 ? 154.478 -22.572 61.233  1.000 26.650  ? 278 PHE DDD C   1 
ATOM 7907  O O   . PHE D 1 261 ? 154.325 -23.769 61.487  1.000 29.670  ? 278 PHE DDD O   1 
ATOM 7908  C CB  . PHE D 1 261 ? 152.855 -21.280 62.561  1.000 24.730  ? 278 PHE DDD CB  1 
ATOM 7909  C CG  . PHE D 1 261 ? 151.736 -20.289 62.712  1.000 22.900  ? 278 PHE DDD CG  1 
ATOM 7910  C CD1 . PHE D 1 261 ? 150.423 -20.676 62.525  1.000 22.430  ? 278 PHE DDD CD1 1 
ATOM 7911  C CD2 . PHE D 1 261 ? 151.988 -18.989 63.115  1.000 22.620  ? 278 PHE DDD CD2 1 
ATOM 7912  C CE1 . PHE D 1 261 ? 149.387 -19.775 62.714  1.000 22.240  ? 278 PHE DDD CE1 1 
ATOM 7913  C CE2 . PHE D 1 261 ? 150.949 -18.091 63.293  1.000 22.270  ? 278 PHE DDD CE2 1 
ATOM 7914  C CZ  . PHE D 1 261 ? 149.648 -18.487 63.102  1.000 21.340  ? 278 PHE DDD CZ  1 
ATOM 7915  N N   . LYS D 1 262 ? 155.666 -22.022 61.053  1.000 28.460  ? 279 LYS DDD N   1 
ATOM 7916  C CA  . LYS D 1 262 ? 156.933 -22.709 61.405  1.000 33.250  ? 279 LYS DDD CA  1 
ATOM 7917  C C   . LYS D 1 262 ? 157.821 -21.668 62.074  1.000 36.150  ? 279 LYS DDD C   1 
ATOM 7918  O O   . LYS D 1 262 ? 158.209 -20.688 61.387  1.000 42.300  ? 279 LYS DDD O   1 
ATOM 7919  C CB  . LYS D 1 262 ? 157.583 -23.315 60.159  1.000 34.130  ? 279 LYS DDD CB  1 
ATOM 7920  C CG  . LYS D 1 262 ? 158.856 -24.100 60.400  1.000 35.730  ? 279 LYS DDD CG  1 
ATOM 7921  C CD  . LYS D 1 262 ? 159.387 -24.675 59.085  1.000 43.500  ? 279 LYS DDD CD  1 
ATOM 7922  C CE  . LYS D 1 262 ? 160.869 -25.025 59.055  1.000 49.810  ? 279 LYS DDD CE  1 
ATOM 7923  N NZ  . LYS D 1 262 ? 161.596 -24.485 57.870  1.000 47.590  ? 279 LYS DDD NZ  1 
ATOM 7924  N N   . VAL D 1 263 ? 158.078 -21.828 63.364  1.000 33.230  ? 280 VAL DDD N   1 
ATOM 7925  C CA  . VAL D 1 263 ? 158.826 -20.800 64.138  1.000 34.000  ? 280 VAL DDD CA  1 
ATOM 7926  C C   . VAL D 1 263 ? 160.168 -21.390 64.574  1.000 34.550  ? 280 VAL DDD C   1 
ATOM 7927  O O   . VAL D 1 263 ? 160.163 -22.398 65.266  1.000 31.360  ? 280 VAL DDD O   1 
ATOM 7928  C CB  . VAL D 1 263 ? 157.983 -20.282 65.317  1.000 34.420  ? 280 VAL DDD CB  1 
ATOM 7929  C CG1 . VAL D 1 263 ? 158.714 -19.219 66.121  1.000 33.320  ? 280 VAL DDD CG1 1 
ATOM 7930  C CG2 . VAL D 1 263 ? 156.644 -19.758 64.827  1.000 35.960  ? 280 VAL DDD CG2 1 
ATOM 7931  N N   . GLN D 1 264 ? 161.265 -20.786 64.116  1.000 37.290  ? 281 GLN DDD N   1 
ATOM 7932  C CA  . GLN D 1 264 ? 162.626 -20.982 64.670  1.000 42.730  ? 281 GLN DDD CA  1 
ATOM 7933  C C   . GLN D 1 264 ? 162.663 -20.317 66.053  1.000 38.940  ? 281 GLN DDD C   1 
ATOM 7934  O O   . GLN D 1 264 ? 162.188 -19.195 66.205  1.000 39.030  ? 281 GLN DDD O   1 
ATOM 7935  C CB  . GLN D 1 264 ? 163.710 -20.352 63.790  1.000 55.090  ? 281 GLN DDD CB  1 
ATOM 7936  C CG  . GLN D 1 264 ? 163.786 -20.856 62.351  1.000 63.630  ? 281 GLN DDD CG  1 
ATOM 7937  C CD  . GLN D 1 264 ? 164.314 -22.259 62.268  1.000 74.790  ? 281 GLN DDD CD  1 
ATOM 7938  O OE1 . GLN D 1 264 ? 164.930 -22.762 63.191  1.000 92.820  ? 281 GLN DDD OE1 1 
ATOM 7939  N NE2 . GLN D 1 264 ? 164.039 -22.921 61.157  1.000 69.000  ? 281 GLN DDD NE2 1 
ATOM 7940  N N   . LEU D 1 265 ? 163.228 -20.990 67.039  1.000 36.320  ? 282 LEU DDD N   1 
ATOM 7941  C CA  . LEU D 1 265 ? 163.434 -20.444 68.402  1.000 32.880  ? 282 LEU DDD CA  1 
ATOM 7942  C C   . LEU D 1 265 ? 164.895 -20.674 68.792  1.000 34.400  ? 282 LEU DDD C   1 
ATOM 7943  O O   . LEU D 1 265 ? 165.468 -21.631 68.291  1.000 37.320  ? 282 LEU DDD O   1 
ATOM 7944  C CB  . LEU D 1 265 ? 162.474 -21.172 69.342  1.000 30.500  ? 282 LEU DDD CB  1 
ATOM 7945  C CG  . LEU D 1 265 ? 160.986 -20.911 69.098  1.000 29.310  ? 282 LEU DDD CG  1 
ATOM 7946  C CD1 . LEU D 1 265 ? 160.165 -22.179 69.212  1.000 27.860  ? 282 LEU DDD CD1 1 
ATOM 7947  C CD2 . LEU D 1 265 ? 160.475 -19.870 70.072  1.000 30.450  ? 282 LEU DDD CD2 1 
ATOM 7948  N N   . ARG D 1 266 ? 165.484 -19.815 69.621  1.000 35.220  ? 283 ARG DDD N   1 
ATOM 7949  C CA  . ARG D 1 266 ? 166.824 -20.031 70.231  1.000 36.090  ? 283 ARG DDD CA  1 
ATOM 7950  C C   . ARG D 1 266 ? 166.746 -19.706 71.734  1.000 36.740  ? 283 ARG DDD C   1 
ATOM 7951  O O   . ARG D 1 266 ? 165.708 -19.193 72.174  1.000 36.740  ? 283 ARG DDD O   1 
ATOM 7952  C CB  . ARG D 1 266 ? 167.868 -19.187 69.501  1.000 35.730  ? 283 ARG DDD CB  1 
ATOM 7953  C CG  . ARG D 1 266 ? 167.803 -17.709 69.842  1.000 34.680  ? 283 ARG DDD CG  1 
ATOM 7954  C CD  . ARG D 1 266 ? 168.644 -16.884 68.907  1.000 35.750  ? 283 ARG DDD CD  1 
ATOM 7955  N NE  . ARG D 1 266 ? 168.463 -15.473 69.208  1.000 37.330  ? 283 ARG DDD NE  1 
ATOM 7956  C CZ  . ARG D 1 266 ? 168.774 -14.483 68.379  1.000 39.530  ? 283 ARG DDD CZ  1 
ATOM 7957  N NH1 . ARG D 1 266 ? 169.281 -14.755 67.194  1.000 44.430  ? 283 ARG DDD NH1 1 
ATOM 7958  N NH2 . ARG D 1 266 ? 168.576 -13.227 68.724  1.000 37.950  ? 283 ARG DDD NH2 1 
ATOM 7959  N N   . LYS D 1 267 ? 167.802 -19.986 72.491  1.000 37.130  ? 284 LYS DDD N   1 
ATOM 7960  C CA  . LYS D 1 267 ? 167.830 -19.794 73.967  1.000 37.910  ? 284 LYS DDD CA  1 
ATOM 7961  C C   . LYS D 1 267 ? 168.490 -18.448 74.302  1.000 36.540  ? 284 LYS DDD C   1 
ATOM 7962  O O   . LYS D 1 267 ? 169.617 -18.252 73.852  1.000 36.020  ? 284 LYS DDD O   1 
ATOM 7963  C CB  . LYS D 1 267 ? 168.632 -20.939 74.588  1.000 37.920  ? 284 LYS DDD CB  1 
ATOM 7964  C CG  . LYS D 1 267 ? 168.036 -22.314 74.387  1.000 35.110  ? 284 LYS DDD CG  1 
ATOM 7965  C CD  . LYS D 1 267 ? 168.794 -23.388 75.059  1.000 35.200  ? 284 LYS DDD CD  1 
ATOM 7966  C CE  . LYS D 1 267 ? 168.142 -24.737 74.897  1.000 37.280  ? 284 LYS DDD CE  1 
ATOM 7967  N NZ  . LYS D 1 267 ? 169.032 -25.818 75.399  1.000 38.640  ? 284 LYS DDD NZ  1 
ATOM 7968  N N   . ARG D 1 268 ? 167.855 -17.659 75.168  1.000 37.910  ? 285 ARG DDD N   1 
ATOM 7969  C CA  . ARG D 1 268 ? 168.403 -16.343 75.556  1.000 43.700  ? 285 ARG DDD CA  1 
ATOM 7970  C C   . ARG D 1 268 ? 168.570 -16.294 77.072  1.000 49.780  ? 285 ARG DDD C   1 
ATOM 7971  O O   . ARG D 1 268 ? 167.593 -16.589 77.761  1.000 57.000  ? 285 ARG DDD O   1 
ATOM 7972  C CB  . ARG D 1 268 ? 167.447 -15.248 75.093  1.000 47.440  ? 285 ARG DDD CB  1 
ATOM 7973  C CG  . ARG D 1 268 ? 167.947 -13.834 75.327  1.000 52.620  ? 285 ARG DDD CG  1 
ATOM 7974  C CD  . ARG D 1 268 ? 169.038 -13.501 74.327  1.000 53.930  ? 285 ARG DDD CD  1 
ATOM 7975  N NE  . ARG D 1 268 ? 168.549 -12.788 73.161  1.000 51.210  ? 285 ARG DDD NE  1 
ATOM 7976  C CZ  . ARG D 1 268 ? 169.033 -11.629 72.742  1.000 46.840  ? 285 ARG DDD CZ  1 
ATOM 7977  N NH1 . ARG D 1 268 ? 170.015 -11.044 73.402  1.000 44.530  ? 285 ARG DDD NH1 1 
ATOM 7978  N NH2 . ARG D 1 268 ? 168.538 -11.060 71.662  1.000 53.630  ? 285 ARG DDD NH2 1 
ATOM 7979  N N   . ARG D 1 269 ? 169.769 -15.982 77.560  1.000 51.620  ? 286 ARG DDD N   1 
ATOM 7980  C CA  . ARG D 1 269 ? 170.035 -15.797 79.011  1.000 45.960  ? 286 ARG DDD CA  1 
ATOM 7981  C C   . ARG D 1 269 ? 169.276 -14.533 79.450  1.000 46.010  ? 286 ARG DDD C   1 
ATOM 7982  O O   . ARG D 1 269 ? 169.228 -13.575 78.656  1.000 46.870  ? 286 ARG DDD O   1 
ATOM 7983  C CB  . ARG D 1 269 ? 171.557 -15.797 79.224  1.000 42.300  ? 286 ARG DDD CB  1 
ATOM 7984  N N   . VAL D 1 270 ? 168.661 -14.564 80.634  1.000 52.690  ? 287 VAL DDD N   1 
ATOM 7985  C CA  . VAL D 1 270 ? 167.747 -13.513 81.187  1.000 56.700  ? 287 VAL DDD CA  1 
ATOM 7986  C C   . VAL D 1 270 ? 167.966 -13.432 82.710  1.000 54.960  ? 287 VAL DDD C   1 
ATOM 7987  O O   . VAL D 1 270 ? 168.114 -14.501 83.315  1.000 55.860  ? 287 VAL DDD O   1 
ATOM 7988  C CB  . VAL D 1 270 ? 166.279 -13.857 80.843  1.000 59.580  ? 287 VAL DDD CB  1 
ATOM 7989  C CG1 . VAL D 1 270 ? 165.304 -12.802 81.336  1.000 64.420  ? 287 VAL DDD CG1 1 
ATOM 7990  C CG2 . VAL D 1 270 ? 166.064 -14.109 79.357  1.000 57.090  ? 287 VAL DDD CG2 1 
ATOM 7991  N N   . LYS D 1 271 ? 168.015 -12.225 83.301  1.000 54.690  ? 288 LYS DDD N   1 
ATOM 7992  C CA  . LYS D 1 271 ? 168.033 -11.993 84.777  1.000 58.780  ? 288 LYS DDD CA  1 
ATOM 7993  C C   . LYS D 1 271 ? 166.597 -11.673 85.249  1.000 63.760  ? 288 LYS DDD C   1 
ATOM 7994  O O   . LYS D 1 271 ? 165.936 -10.817 84.608  1.000 51.490  ? 288 LYS DDD O   1 
ATOM 7995  C CB  . LYS D 1 271 ? 169.032 -10.889 85.156  1.000 53.710  ? 288 LYS DDD CB  1 
ATOM 7996  N N   . ASN D 1 272 ? 166.131 -12.392 86.290  1.000 76.410  ? 289 ASN DDD N   1 
ATOM 7997  C CA  . ASN D 1 272 ? 164.913 -12.139 87.121  1.000 81.010  ? 289 ASN DDD CA  1 
ATOM 7998  C C   . ASN D 1 272 ? 163.643 -12.390 86.292  1.000 80.950  ? 289 ASN DDD C   1 
ATOM 7999  O O   . ASN D 1 272 ? 163.102 -13.504 86.255  1.000 64.550  ? 289 ASN DDD O   1 
ATOM 8000  C CB  . ASN D 1 272 ? 164.933 -10.742 87.730  1.000 73.650  ? 289 ASN DDD CB  1 
ATOM 8001  N N   . MET E 1 4   ? 167.046 -28.284 50.922  1.000 68.610  ? 21  MET EEE N   1 
ATOM 8002  C CA  . MET E 1 4   ? 167.145 -29.636 50.332  1.000 80.780  ? 21  MET EEE CA  1 
ATOM 8003  C C   . MET E 1 4   ? 167.538 -30.647 51.410  1.000 94.180  ? 21  MET EEE C   1 
ATOM 8004  O O   . MET E 1 4   ? 166.710 -31.517 51.725  1.000 112.750 ? 21  MET EEE O   1 
ATOM 8005  C CB  . MET E 1 4   ? 168.153 -29.585 49.244  1.000 77.830  ? 21  MET EEE CB  1 
ATOM 8006  N N   . GLY E 1 5   ? 168.764 -30.573 51.908  1.000 98.350  ? 22  GLY EEE N   1 
ATOM 8007  C CA  . GLY E 1 5   ? 169.226 -31.422 53.035  1.000 107.400 ? 22  GLY EEE CA  1 
ATOM 8008  C C   . GLY E 1 5   ? 168.879 -32.907 52.920  1.000 116.620 ? 22  GLY EEE C   1 
ATOM 8009  O O   . GLY E 1 5   ? 169.076 -33.438 51.806  1.000 114.670 ? 22  GLY EEE O   1 
ATOM 8010  N N   . GLY E 1 6   ? 168.474 -33.545 54.034  1.000 118.680 ? 23  GLY EEE N   1 
ATOM 8011  C CA  . GLY E 1 6   ? 168.204 -35.007 54.119  1.000 111.180 ? 23  GLY EEE CA  1 
ATOM 8012  C C   . GLY E 1 6   ? 169.532 -35.768 54.184  1.000 113.740 ? 23  GLY EEE C   1 
ATOM 8013  O O   . GLY E 1 6   ? 169.640 -36.691 55.013  1.000 97.550  ? 23  GLY EEE O   1 
ATOM 8014  N N   . VAL E 1 7   ? 170.505 -35.387 53.354  1.000 117.720 ? 24  VAL EEE N   1 
ATOM 8015  C CA  . VAL E 1 7   ? 171.848 -36.004 53.382  1.000 100.370 ? 24  VAL EEE CA  1 
ATOM 8016  C C   . VAL E 1 7   ? 172.857 -34.903 53.707  1.000 97.550  ? 24  VAL EEE C   1 
ATOM 8017  O O   . VAL E 1 7   ? 172.437 -33.737 53.800  1.000 94.560  ? 24  VAL EEE O   1 
ATOM 8018  C CB  . VAL E 1 7   ? 172.133 -36.625 52.045  1.000 88.000  ? 24  VAL EEE CB  1 
ATOM 8019  N N   . GLU E 1 8   ? 174.129 -35.258 53.878  1.000 91.820  ? 25  GLU EEE N   1 
ATOM 8020  C CA  . GLU E 1 8   ? 175.130 -34.243 54.285  1.000 86.690  ? 25  GLU EEE CA  1 
ATOM 8021  C C   . GLU E 1 8   ? 175.507 -33.433 53.054  1.000 81.140  ? 25  GLU EEE C   1 
ATOM 8022  O O   . GLU E 1 8   ? 176.088 -34.006 52.138  1.000 85.630  ? 25  GLU EEE O   1 
ATOM 8023  C CB  . GLU E 1 8   ? 176.365 -34.906 54.885  1.000 92.590  ? 25  GLU EEE CB  1 
ATOM 8024  C CG  . GLU E 1 8   ? 176.841 -34.240 56.159  1.000 94.590  ? 25  GLU EEE CG  1 
ATOM 8025  C CD  . GLU E 1 8   ? 178.321 -34.417 56.439  1.000 95.510  ? 25  GLU EEE CD  1 
ATOM 8026  O OE1 . GLU E 1 8   ? 178.857 -35.492 56.108  1.000 93.200  ? 25  GLU EEE OE1 1 
ATOM 8027  O OE2 . GLU E 1 8   ? 178.934 -33.479 56.982  1.000 82.770  ? 25  GLU EEE OE2 1 
ATOM 8028  N N   . VAL E 1 9   ? 175.153 -32.154 53.039  1.000 69.940  ? 26  VAL EEE N   1 
ATOM 8029  C CA  . VAL E 1 9   ? 175.437 -31.330 51.836  1.000 65.660  ? 26  VAL EEE CA  1 
ATOM 8030  C C   . VAL E 1 9   ? 176.848 -30.810 52.003  1.000 66.200  ? 26  VAL EEE C   1 
ATOM 8031  O O   . VAL E 1 9   ? 177.083 -30.045 52.945  1.000 65.770  ? 26  VAL EEE O   1 
ATOM 8032  C CB  . VAL E 1 9   ? 174.414 -30.197 51.648  1.000 65.820  ? 26  VAL EEE CB  1 
ATOM 8033  C CG1 . VAL E 1 9   ? 174.230 -29.888 50.179  1.000 66.830  ? 26  VAL EEE CG1 1 
ATOM 8034  C CG2 . VAL E 1 9   ? 173.079 -30.529 52.294  1.000 67.820  ? 26  VAL EEE CG2 1 
ATOM 8035  N N   . LEU E 1 10  ? 177.762 -31.243 51.131  1.000 73.900  ? 27  LEU EEE N   1 
ATOM 8036  C CA  . LEU E 1 10  ? 179.173 -30.861 51.298  1.000 68.400  ? 27  LEU EEE CA  1 
ATOM 8037  C C   . LEU E 1 10  ? 179.486 -29.663 50.412  1.000 62.970  ? 27  LEU EEE C   1 
ATOM 8038  O O   . LEU E 1 10  ? 178.637 -28.771 50.332  1.000 67.290  ? 27  LEU EEE O   1 
ATOM 8039  C CB  . LEU E 1 10  ? 180.068 -32.069 51.003  1.000 70.570  ? 27  LEU EEE CB  1 
ATOM 8040  C CG  . LEU E 1 10  ? 179.720 -33.325 51.803  1.000 68.960  ? 27  LEU EEE CG  1 
ATOM 8041  C CD1 . LEU E 1 10  ? 180.545 -34.513 51.322  1.000 74.470  ? 27  LEU EEE CD1 1 
ATOM 8042  C CD2 . LEU E 1 10  ? 179.941 -33.097 53.287  1.000 57.030  ? 27  LEU EEE CD2 1 
ATOM 8043  N N   . GLU E 1 11  ? 180.652 -29.642 49.774  1.000 66.110  ? 28  GLU EEE N   1 
ATOM 8044  C CA  . GLU E 1 11  ? 181.031 -28.404 49.040  1.000 70.420  ? 28  GLU EEE CA  1 
ATOM 8045  C C   . GLU E 1 11  ? 180.546 -28.504 47.581  1.000 71.440  ? 28  GLU EEE C   1 
ATOM 8046  O O   . GLU E 1 11  ? 180.190 -29.623 47.126  1.000 62.280  ? 28  GLU EEE O   1 
ATOM 8047  C CB  . GLU E 1 11  ? 182.544 -28.175 49.190  1.000 62.990  ? 28  GLU EEE CB  1 
ATOM 8048  N N   . VAL E 1 12  ? 180.486 -27.368 46.883  1.000 78.180  ? 29  VAL EEE N   1 
ATOM 8049  C CA  . VAL E 1 12  ? 180.071 -27.285 45.450  1.000 83.420  ? 29  VAL EEE CA  1 
ATOM 8050  C C   . VAL E 1 12  ? 181.268 -27.710 44.594  1.000 87.750  ? 29  VAL EEE C   1 
ATOM 8051  O O   . VAL E 1 12  ? 182.297 -27.044 44.693  1.000 90.780  ? 29  VAL EEE O   1 
ATOM 8052  C CB  . VAL E 1 12  ? 179.613 -25.863 45.065  1.000 82.390  ? 29  VAL EEE CB  1 
ATOM 8053  C CG1 . VAL E 1 12  ? 179.244 -25.766 43.588  1.000 80.170  ? 29  VAL EEE CG1 1 
ATOM 8054  C CG2 . VAL E 1 12  ? 178.456 -25.370 45.930  1.000 81.540  ? 29  VAL EEE CG2 1 
ATOM 8055  N N   . LYS E 1 13  ? 181.138 -28.765 43.780  1.000 90.820  ? 30  LYS EEE N   1 
ATOM 8056  C CA  . LYS E 1 13  ? 182.180 -29.169 42.797  1.000 84.000  ? 30  LYS EEE CA  1 
ATOM 8057  C C   . LYS E 1 13  ? 182.192 -28.113 41.688  1.000 86.460  ? 30  LYS EEE C   1 
ATOM 8058  O O   . LYS E 1 13  ? 181.074 -27.796 41.187  1.000 100.680 ? 30  LYS EEE O   1 
ATOM 8059  C CB  . LYS E 1 13  ? 181.877 -30.574 42.261  1.000 80.810  ? 30  LYS EEE CB  1 
ATOM 8060  C CG  . LYS E 1 13  ? 182.880 -31.210 41.306  1.000 83.520  ? 30  LYS EEE CG  1 
ATOM 8061  C CD  . LYS E 1 13  ? 182.336 -32.483 40.638  1.000 84.070  ? 30  LYS EEE CD  1 
ATOM 8062  C CE  . LYS E 1 13  ? 183.029 -32.874 39.335  1.000 87.060  ? 30  LYS EEE CE  1 
ATOM 8063  N NZ  . LYS E 1 13  ? 184.460 -33.236 39.522  1.000 88.890  ? 30  LYS EEE NZ  1 
ATOM 8064  N N   . THR E 1 14  ? 183.370 -27.555 41.369  1.000 86.080  ? 31  THR EEE N   1 
ATOM 8065  C CA  . THR E 1 14  ? 183.624 -26.696 40.166  1.000 91.740  ? 31  THR EEE CA  1 
ATOM 8066  C C   . THR E 1 14  ? 184.464 -27.479 39.148  1.000 89.110  ? 31  THR EEE C   1 
ATOM 8067  O O   . THR E 1 14  ? 184.869 -28.594 39.475  1.000 76.210  ? 31  THR EEE O   1 
ATOM 8068  C CB  . THR E 1 14  ? 184.265 -25.342 40.484  1.000 92.650  ? 31  THR EEE CB  1 
ATOM 8069  O OG1 . THR E 1 14  ? 185.548 -25.620 41.050  1.000 92.560  ? 31  THR EEE OG1 1 
ATOM 8070  C CG2 . THR E 1 14  ? 183.414 -24.461 41.377  1.000 87.480  ? 31  THR EEE CG2 1 
ATOM 8071  N N   . GLY E 1 15  ? 184.695 -26.908 37.963  1.000 103.370 ? 32  GLY EEE N   1 
ATOM 8072  C CA  . GLY E 1 15  ? 185.413 -27.557 36.848  1.000 120.630 ? 32  GLY EEE CA  1 
ATOM 8073  C C   . GLY E 1 15  ? 184.716 -27.318 35.523  1.000 124.040 ? 32  GLY EEE C   1 
ATOM 8074  O O   . GLY E 1 15  ? 183.720 -26.574 35.499  1.000 130.420 ? 32  GLY EEE O   1 
ATOM 8075  N N   . VAL E 1 16  ? 185.204 -27.948 34.448  1.000 129.310 ? 33  VAL EEE N   1 
ATOM 8076  C CA  . VAL E 1 16  ? 184.737 -27.722 33.045  1.000 136.110 ? 33  VAL EEE CA  1 
ATOM 8077  C C   . VAL E 1 16  ? 183.321 -28.292 32.867  1.000 123.620 ? 33  VAL EEE C   1 
ATOM 8078  O O   . VAL E 1 16  ? 182.595 -27.766 32.013  1.000 120.440 ? 33  VAL EEE O   1 
ATOM 8079  C CB  . VAL E 1 16  ? 185.732 -28.305 32.017  1.000 141.830 ? 33  VAL EEE CB  1 
ATOM 8080  C CG1 . VAL E 1 16  ? 185.267 -28.147 30.568  1.000 129.910 ? 33  VAL EEE CG1 1 
ATOM 8081  C CG2 . VAL E 1 16  ? 187.117 -27.693 32.188  1.000 136.050 ? 33  VAL EEE CG2 1 
ATOM 8082  N N   . ASP E 1 17  ? 182.920 -29.298 33.647  1.000 114.480 ? 34  ASP EEE N   1 
ATOM 8083  C CA  . ASP E 1 17  ? 181.592 -29.945 33.485  1.000 115.700 ? 34  ASP EEE CA  1 
ATOM 8084  C C   . ASP E 1 17  ? 180.893 -30.063 34.839  1.000 109.210 ? 34  ASP EEE C   1 
ATOM 8085  O O   . ASP E 1 17  ? 180.453 -31.164 35.195  1.000 99.790  ? 34  ASP EEE O   1 
ATOM 8086  C CB  . ASP E 1 17  ? 181.728 -31.297 32.781  1.000 119.650 ? 34  ASP EEE CB  1 
ATOM 8087  C CG  . ASP E 1 17  ? 181.181 -31.273 31.367  1.000 119.070 ? 34  ASP EEE CG  1 
ATOM 8088  O OD1 . ASP E 1 17  ? 181.172 -30.200 30.765  1.000 120.160 ? 34  ASP EEE OD1 1 
ATOM 8089  O OD2 . ASP E 1 17  ? 180.650 -32.335 30.932  1.000 119.630 ? 34  ASP EEE OD2 1 
ATOM 8090  N N   . SER E 1 18  ? 180.764 -28.944 35.546  1.000 95.320  ? 35  SER EEE N   1 
ATOM 8091  C CA  . SER E 1 18  ? 180.102 -28.869 36.873  1.000 87.070  ? 35  SER EEE CA  1 
ATOM 8092  C C   . SER E 1 18  ? 178.712 -28.234 36.764  1.000 77.470  ? 35  SER EEE C   1 
ATOM 8093  O O   . SER E 1 18  ? 177.938 -28.414 37.698  1.000 72.690  ? 35  SER EEE O   1 
ATOM 8094  C CB  . SER E 1 18  ? 180.959 -28.134 37.852  1.000 86.540  ? 35  SER EEE CB  1 
ATOM 8095  O OG  . SER E 1 18  ? 181.604 -27.021 37.254  1.000 79.760  ? 35  SER EEE OG  1 
ATOM 8096  N N   . ILE E 1 19  ? 178.397 -27.548 35.664  1.000 70.870  ? 36  ILE EEE N   1 
ATOM 8097  C CA  . ILE E 1 19  ? 177.078 -26.879 35.458  1.000 72.780  ? 36  ILE EEE CA  1 
ATOM 8098  C C   . ILE E 1 19  ? 176.356 -27.589 34.299  1.000 63.060  ? 36  ILE EEE C   1 
ATOM 8099  O O   . ILE E 1 19  ? 177.037 -28.236 33.503  1.000 60.110  ? 36  ILE EEE O   1 
ATOM 8100  C CB  . ILE E 1 19  ? 177.240 -25.349 35.258  1.000 76.940  ? 36  ILE EEE CB  1 
ATOM 8101  C CG1 . ILE E 1 19  ? 175.910 -24.592 35.454  1.000 90.450  ? 36  ILE EEE CG1 1 
ATOM 8102  C CG2 . ILE E 1 19  ? 177.876 -25.047 33.909  1.000 70.350  ? 36  ILE EEE CG2 1 
ATOM 8103  C CD1 . ILE E 1 19  ? 175.993 -23.250 36.178  1.000 93.660  ? 36  ILE EEE CD1 1 
ATOM 8104  N N   . THR E 1 20  ? 175.019 -27.544 34.279  1.000 56.150  ? 37  THR EEE N   1 
ATOM 8105  C CA  . THR E 1 20  ? 174.145 -27.995 33.164  1.000 51.970  ? 37  THR EEE CA  1 
ATOM 8106  C C   . THR E 1 20  ? 172.835 -27.192 33.198  1.000 54.240  ? 37  THR EEE C   1 
ATOM 8107  O O   . THR E 1 20  ? 172.600 -26.483 34.204  1.000 56.880  ? 37  THR EEE O   1 
ATOM 8108  C CB  . THR E 1 20  ? 173.879 -29.502 33.246  1.000 51.710  ? 37  THR EEE CB  1 
ATOM 8109  O OG1 . THR E 1 20  ? 173.254 -29.952 32.048  1.000 51.830  ? 37  THR EEE OG1 1 
ATOM 8110  C CG2 . THR E 1 20  ? 172.994 -29.876 34.408  1.000 55.110  ? 37  THR EEE CG2 1 
ATOM 8111  N N   . GLU E 1 21  ? 172.010 -27.310 32.143  1.000 51.900  ? 38  GLU EEE N   1 
ATOM 8112  C CA  . GLU E 1 21  ? 170.729 -26.573 31.962  1.000 47.860  ? 38  GLU EEE CA  1 
ATOM 8113  C C   . GLU E 1 21  ? 169.619 -27.521 31.511  1.000 45.420  ? 38  GLU EEE C   1 
ATOM 8114  O O   . GLU E 1 21  ? 169.813 -28.228 30.531  1.000 45.820  ? 38  GLU EEE O   1 
ATOM 8115  C CB  . GLU E 1 21  ? 170.835 -25.524 30.861  1.000 51.780  ? 38  GLU EEE CB  1 
ATOM 8116  C CG  . GLU E 1 21  ? 171.547 -24.268 31.302  1.000 57.420  ? 38  GLU EEE CG  1 
ATOM 8117  C CD  . GLU E 1 21  ? 171.353 -23.113 30.340  1.000 61.580  ? 38  GLU EEE CD  1 
ATOM 8118  O OE1 . GLU E 1 21  ? 170.665 -23.312 29.297  1.000 55.460  ? 38  GLU EEE OE1 1 
ATOM 8119  O OE2 . GLU E 1 21  ? 171.854 -22.015 30.655  1.000 71.480  ? 38  GLU EEE OE2 1 
ATOM 8120  N N   . VAL E 1 22  ? 168.483 -27.482 32.192  1.000 43.060  ? 39  VAL EEE N   1 
ATOM 8121  C CA  . VAL E 1 22  ? 167.181 -27.937 31.653  1.000 39.470  ? 39  VAL EEE CA  1 
ATOM 8122  C C   . VAL E 1 22  ? 166.433 -26.692 31.174  1.000 44.770  ? 39  VAL EEE C   1 
ATOM 8123  O O   . VAL E 1 22  ? 166.498 -25.625 31.844  1.000 48.530  ? 39  VAL EEE O   1 
ATOM 8124  C CB  . VAL E 1 22  ? 166.387 -28.685 32.724  1.000 39.520  ? 39  VAL EEE CB  1 
ATOM 8125  C CG1 . VAL E 1 22  ? 164.983 -29.003 32.249  1.000 45.410  ? 39  VAL EEE CG1 1 
ATOM 8126  C CG2 . VAL E 1 22  ? 167.095 -29.944 33.160  1.000 37.830  ? 39  VAL EEE CG2 1 
ATOM 8127  N N   . GLU E 1 23  ? 165.753 -26.823 30.040  1.000 47.140  ? 40  GLU EEE N   1 
ATOM 8128  C CA  . GLU E 1 23  ? 164.882 -25.776 29.457  1.000 49.320  ? 40  GLU EEE CA  1 
ATOM 8129  C C   . GLU E 1 23  ? 163.715 -26.512 28.815  1.000 49.700  ? 40  GLU EEE C   1 
ATOM 8130  O O   . GLU E 1 23  ? 163.962 -27.193 27.832  1.000 53.200  ? 40  GLU EEE O   1 
ATOM 8131  C CB  . GLU E 1 23  ? 165.697 -24.954 28.444  1.000 51.640  ? 40  GLU EEE CB  1 
ATOM 8132  C CG  . GLU E 1 23  ? 165.000 -23.699 27.932  1.000 52.030  ? 40  GLU EEE CG  1 
ATOM 8133  C CD  . GLU E 1 23  ? 165.760 -22.995 26.814  1.000 56.550  ? 40  GLU EEE CD  1 
ATOM 8134  O OE1 . GLU E 1 23  ? 165.888 -23.610 25.714  1.000 54.800  ? 40  GLU EEE OE1 1 
ATOM 8135  O OE2 . GLU E 1 23  ? 166.270 -21.855 27.052  1.000 61.750  ? 40  GLU EEE OE2 1 
ATOM 8136  N N   . CYS E 1 24  ? 162.522 -26.460 29.382  1.000 52.160  ? 41  CYS EEE N   1 
ATOM 8137  C CA  . CYS E 1 24  ? 161.332 -27.017 28.701  1.000 52.680  ? 41  CYS EEE CA  1 
ATOM 8138  C C   . CYS E 1 24  ? 160.120 -26.106 28.928  1.000 51.220  ? 41  CYS EEE C   1 
ATOM 8139  O O   . CYS E 1 24  ? 160.256 -25.052 29.571  1.000 51.750  ? 41  CYS EEE O   1 
ATOM 8140  C CB  . CYS E 1 24  ? 161.083 -28.425 29.215  1.000 58.170  ? 41  CYS EEE CB  1 
ATOM 8141  S SG  . CYS E 1 24  ? 160.535 -28.428 30.939  1.000 59.780  ? 41  CYS EEE SG  1 
ATOM 8142  N N   . PHE E 1 25  ? 158.994 -26.481 28.357  1.000 50.410  ? 42  PHE EEE N   1 
ATOM 8143  C CA  . PHE E 1 25  ? 157.659 -25.859 28.540  1.000 48.270  ? 42  PHE EEE CA  1 
ATOM 8144  C C   . PHE E 1 25  ? 156.745 -26.949 29.130  1.000 40.480  ? 42  PHE EEE C   1 
ATOM 8145  O O   . PHE E 1 25  ? 156.988 -28.106 28.819  1.000 38.470  ? 42  PHE EEE O   1 
ATOM 8146  C CB  . PHE E 1 25  ? 157.122 -25.314 27.209  1.000 54.210  ? 42  PHE EEE CB  1 
ATOM 8147  C CG  . PHE E 1 25  ? 157.029 -26.376 26.144  1.000 66.770  ? 42  PHE EEE CG  1 
ATOM 8148  C CD1 . PHE E 1 25  ? 158.164 -26.734 25.428  1.000 72.670  ? 42  PHE EEE CD1 1 
ATOM 8149  C CD2 . PHE E 1 25  ? 155.868 -27.120 25.951  1.000 78.830  ? 42  PHE EEE CD2 1 
ATOM 8150  C CE1 . PHE E 1 25  ? 158.132 -27.773 24.508  1.000 75.870  ? 42  PHE EEE CE1 1 
ATOM 8151  C CE2 . PHE E 1 25  ? 155.829 -28.152 25.021  1.000 77.230  ? 42  PHE EEE CE2 1 
ATOM 8152  C CZ  . PHE E 1 25  ? 156.962 -28.476 24.301  1.000 79.350  ? 42  PHE EEE CZ  1 
ATOM 8153  N N   . LEU E 1 26  ? 155.812 -26.592 30.009  1.000 38.500  ? 43  LEU EEE N   1 
ATOM 8154  C CA  . LEU E 1 26  ? 154.761 -27.490 30.564  1.000 36.560  ? 43  LEU EEE CA  1 
ATOM 8155  C C   . LEU E 1 26  ? 153.432 -27.022 30.017  1.000 35.280  ? 43  LEU EEE C   1 
ATOM 8156  O O   . LEU E 1 26  ? 153.186 -25.827 30.058  1.000 35.960  ? 43  LEU EEE O   1 
ATOM 8157  C CB  . LEU E 1 26  ? 154.722 -27.435 32.093  1.000 39.080  ? 43  LEU EEE CB  1 
ATOM 8158  C CG  . LEU E 1 26  ? 155.543 -28.505 32.795  1.000 42.320  ? 43  LEU EEE CG  1 
ATOM 8159  C CD1 . LEU E 1 26  ? 157.027 -28.252 32.592  1.000 44.540  ? 43  LEU EEE CD1 1 
ATOM 8160  C CD2 . LEU E 1 26  ? 155.181 -28.559 34.273  1.000 43.020  ? 43  LEU EEE CD2 1 
ATOM 8161  N N   . THR E 1 27  ? 152.635 -27.933 29.493  1.000 36.620  ? 44  THR EEE N   1 
ATOM 8162  C CA  . THR E 1 27  ? 151.334 -27.566 28.904  1.000 37.250  ? 44  THR EEE CA  1 
ATOM 8163  C C   . THR E 1 27  ? 150.306 -27.590 30.026  1.000 33.880  ? 44  THR EEE C   1 
ATOM 8164  O O   . THR E 1 27  ? 150.506 -28.180 31.086  1.000 31.470  ? 44  THR EEE O   1 
ATOM 8165  C CB  . THR E 1 27  ? 151.009 -28.452 27.705  1.000 39.910  ? 44  THR EEE CB  1 
ATOM 8166  O OG1 . THR E 1 27  ? 150.563 -29.718 28.188  1.000 43.890  ? 44  THR EEE OG1 1 
ATOM 8167  C CG2 . THR E 1 27  ? 152.187 -28.646 26.783  1.000 42.610  ? 44  THR EEE CG2 1 
ATOM 8168  N N   . PRO E 1 28  ? 149.207 -26.851 29.846  1.000 31.050  ? 45  PRO EEE N   1 
ATOM 8169  C CA  . PRO E 1 28  ? 148.141 -26.838 30.832  1.000 32.680  ? 45  PRO EEE CA  1 
ATOM 8170  C C   . PRO E 1 28  ? 147.117 -27.955 30.636  1.000 33.250  ? 45  PRO EEE C   1 
ATOM 8171  O O   . PRO E 1 28  ? 146.608 -28.074 29.529  1.000 31.390  ? 45  PRO EEE O   1 
ATOM 8172  C CB  . PRO E 1 28  ? 147.521 -25.456 30.587  1.000 33.380  ? 45  PRO EEE CB  1 
ATOM 8173  C CG  . PRO E 1 28  ? 147.717 -25.196 29.111  1.000 32.150  ? 45  PRO EEE CG  1 
ATOM 8174  C CD  . PRO E 1 28  ? 149.021 -25.883 28.759  1.000 30.990  ? 45  PRO EEE CD  1 
ATOM 8175  N N   . GLU E 1 29  ? 146.783 -28.689 31.710  1.000 36.660  ? 46  GLU EEE N   1 
ATOM 8176  C CA  . GLU E 1 29  ? 145.635 -29.635 31.662  1.000 37.850  ? 46  GLU EEE CA  1 
ATOM 8177  C C   . GLU E 1 29  ? 144.446 -28.938 32.312  1.000 36.660  ? 46  GLU EEE C   1 
ATOM 8178  O O   . GLU E 1 29  ? 144.363 -28.932 33.559  1.000 39.590  ? 46  GLU EEE O   1 
ATOM 8179  C CB  . GLU E 1 29  ? 145.965 -30.981 32.293  1.000 38.200  ? 46  GLU EEE CB  1 
ATOM 8180  C CG  . GLU E 1 29  ? 147.194 -31.632 31.703  1.000 42.480  ? 46  GLU EEE CG  1 
ATOM 8181  C CD  . GLU E 1 29  ? 147.099 -32.004 30.231  1.000 47.150  ? 46  GLU EEE CD  1 
ATOM 8182  O OE1 . GLU E 1 29  ? 148.082 -32.540 29.695  1.000 51.560  ? 46  GLU EEE OE1 1 
ATOM 8183  O OE2 . GLU E 1 29  ? 146.060 -31.765 29.608  1.000 52.770  ? 46  GLU EEE OE2 1 
ATOM 8184  N N   . MET E 1 30  ? 143.600 -28.325 31.477  1.000 32.020  ? 47  MET EEE N   1 
ATOM 8185  C CA  . MET E 1 30  ? 142.450 -27.527 31.954  1.000 29.160  ? 47  MET EEE CA  1 
ATOM 8186  C C   . MET E 1 30  ? 141.179 -28.378 31.904  1.000 28.870  ? 47  MET EEE C   1 
ATOM 8187  O O   . MET E 1 30  ? 140.147 -27.854 32.305  1.000 29.620  ? 47  MET EEE O   1 
ATOM 8188  C CB  . MET E 1 30  ? 142.240 -26.291 31.086  1.000 30.340  ? 47  MET EEE CB  1 
ATOM 8189  C CG  . MET E 1 30  ? 143.266 -25.213 31.296  1.000 30.190  ? 47  MET EEE CG  1 
ATOM 8190  S SD  . MET E 1 30  ? 143.416 -24.694 33.012  1.000 30.820  ? 47  MET EEE SD  1 
ATOM 8191  C CE  . MET E 1 30  ? 145.056 -25.283 33.434  1.000 32.550  ? 47  MET EEE CE  1 
ATOM 8192  N N   . GLY E 1 31  ? 141.251 -29.620 31.404  1.000 29.810  ? 48  GLY EEE N   1 
ATOM 8193  C CA  . GLY E 1 31  ? 140.095 -30.535 31.342  1.000 31.480  ? 48  GLY EEE CA  1 
ATOM 8194  C C   . GLY E 1 31  ? 139.834 -31.092 29.963  1.000 32.360  ? 48  GLY EEE C   1 
ATOM 8195  O O   . GLY E 1 31  ? 139.203 -32.149 29.899  1.000 35.700  ? 48  GLY EEE O   1 
ATOM 8196  N N   . ASP E 1 32  ? 140.240 -30.355 28.921  1.000 33.800  ? 49  ASP EEE N   1 
ATOM 8197  C CA  . ASP E 1 32  ? 140.372 -30.766 27.494  1.000 30.110  ? 49  ASP EEE CA  1 
ATOM 8198  C C   . ASP E 1 32  ? 139.115 -31.522 27.099  1.000 29.470  ? 49  ASP EEE C   1 
ATOM 8199  O O   . ASP E 1 32  ? 139.174 -32.703 26.785  1.000 30.360  ? 49  ASP EEE O   1 
ATOM 8200  C CB  . ASP E 1 32  ? 141.664 -31.540 27.240  1.000 33.200  ? 49  ASP EEE CB  1 
ATOM 8201  C CG  . ASP E 1 32  ? 142.985 -30.767 27.360  1.000 38.540  ? 49  ASP EEE CG  1 
ATOM 8202  O OD1 . ASP E 1 32  ? 143.004 -29.623 27.921  1.000 46.300  ? 49  ASP EEE OD1 1 
ATOM 8203  O OD2 . ASP E 1 32  ? 144.021 -31.315 26.921  1.000 40.560  ? 49  ASP EEE OD2 1 
ATOM 8204  N N   . PRO E 1 33  ? 137.949 -30.835 27.090  1.000 32.090  ? 50  PRO EEE N   1 
ATOM 8205  C CA  . PRO E 1 33  ? 136.664 -31.457 26.793  1.000 33.330  ? 50  PRO EEE CA  1 
ATOM 8206  C C   . PRO E 1 33  ? 136.758 -32.371 25.565  1.000 36.760  ? 50  PRO EEE C   1 
ATOM 8207  O O   . PRO E 1 33  ? 136.642 -33.560 25.761  1.000 50.320  ? 50  PRO EEE O   1 
ATOM 8208  C CB  . PRO E 1 33  ? 135.714 -30.288 26.496  1.000 32.930  ? 50  PRO EEE CB  1 
ATOM 8209  C CG  . PRO E 1 33  ? 136.324 -29.121 27.197  1.000 31.970  ? 50  PRO EEE CG  1 
ATOM 8210  C CD  . PRO E 1 33  ? 137.814 -29.383 27.269  1.000 33.270  ? 50  PRO EEE CD  1 
ATOM 8211  N N   . ASP E 1 34  ? 137.053 -31.810 24.389  1.000 32.570  ? 51  ASP EEE N   1 
ATOM 8212  C CA  . ASP E 1 34  ? 136.938 -32.538 23.102  1.000 33.780  ? 51  ASP EEE CA  1 
ATOM 8213  C C   . ASP E 1 34  ? 138.209 -32.295 22.272  1.000 32.620  ? 51  ASP EEE C   1 
ATOM 8214  O O   . ASP E 1 34  ? 139.095 -31.599 22.788  1.000 30.010  ? 51  ASP EEE O   1 
ATOM 8215  C CB  . ASP E 1 34  ? 135.609 -32.179 22.431  1.000 33.670  ? 51  ASP EEE CB  1 
ATOM 8216  C CG  . ASP E 1 34  ? 135.624 -30.949 21.540  1.000 34.110  ? 51  ASP EEE CG  1 
ATOM 8217  O OD1 . ASP E 1 34  ? 136.696 -30.278 21.407  1.000 31.070  ? 51  ASP EEE OD1 1 
ATOM 8218  O OD2 . ASP E 1 34  ? 134.542 -30.668 20.982  1.000 38.510  ? 51  ASP EEE OD2 1 
ATOM 8219  N N   . GLU E 1 35  ? 138.271 -32.818 21.036  1.000 29.980  ? 52  GLU EEE N   1 
ATOM 8220  C CA  . GLU E 1 35  ? 139.496 -32.879 20.197  1.000 31.310  ? 52  GLU EEE CA  1 
ATOM 8221  C C   . GLU E 1 35  ? 139.989 -31.474 19.837  1.000 35.240  ? 52  GLU EEE C   1 
ATOM 8222  O O   . GLU E 1 35  ? 141.166 -31.361 19.412  1.000 35.340  ? 52  GLU EEE O   1 
ATOM 8223  C CB  . GLU E 1 35  ? 139.274 -33.717 18.930  1.000 33.370  ? 52  GLU EEE CB  1 
ATOM 8224  C CG  . GLU E 1 35  ? 138.160 -33.249 18.025  1.000 36.750  ? 52  GLU EEE CG  1 
ATOM 8225  C CD  . GLU E 1 35  ? 137.677 -34.253 16.999  1.000 41.230  ? 52  GLU EEE CD  1 
ATOM 8226  O OE1 . GLU E 1 35  ? 138.494 -35.103 16.585  1.000 41.210  ? 52  GLU EEE OE1 1 
ATOM 8227  O OE2 . GLU E 1 35  ? 136.481 -34.215 16.659  1.000 45.130  ? 52  GLU EEE OE2 1 
ATOM 8228  N N   . HIS E 1 36  ? 139.160 -30.441 20.048  1.000 37.090  ? 53  HIS EEE N   1 
ATOM 8229  C CA  . HIS E 1 36  ? 139.342 -29.089 19.469  1.000 35.980  ? 53  HIS EEE CA  1 
ATOM 8230  C C   . HIS E 1 36  ? 139.582 -28.015 20.540  1.000 36.360  ? 53  HIS EEE C   1 
ATOM 8231  O O   . HIS E 1 36  ? 139.713 -26.807 20.145  1.000 44.240  ? 53  HIS EEE O   1 
ATOM 8232  C CB  . HIS E 1 36  ? 138.076 -28.732 18.709  1.000 36.360  ? 53  HIS EEE CB  1 
ATOM 8233  C CG  . HIS E 1 36  ? 137.844 -29.479 17.442  1.000 34.280  ? 53  HIS EEE CG  1 
ATOM 8234  N ND1 . HIS E 1 36  ? 138.702 -29.392 16.369  1.000 30.750  ? 53  HIS EEE ND1 1 
ATOM 8235  C CD2 . HIS E 1 36  ? 136.798 -30.240 17.057  1.000 33.030  ? 53  HIS EEE CD2 1 
ATOM 8236  C CE1 . HIS E 1 36  ? 138.202 -30.097 15.377  1.000 32.300  ? 53  HIS EEE CE1 1 
ATOM 8237  N NE2 . HIS E 1 36  ? 137.039 -30.650 15.784  1.000 33.160  ? 53  HIS EEE NE2 1 
ATOM 8238  N N   . LEU E 1 37  ? 139.604 -28.392 21.825  1.000 32.000  ? 54  LEU EEE N   1 
ATOM 8239  C CA  . LEU E 1 37  ? 139.526 -27.446 22.961  1.000 31.550  ? 54  LEU EEE CA  1 
ATOM 8240  C C   . LEU E 1 37  ? 140.660 -27.672 23.965  1.000 34.090  ? 54  LEU EEE C   1 
ATOM 8241  O O   . LEU E 1 37  ? 140.453 -27.367 25.166  1.000 36.380  ? 54  LEU EEE O   1 
ATOM 8242  C CB  . LEU E 1 37  ? 138.159 -27.608 23.612  1.000 29.400  ? 54  LEU EEE CB  1 
ATOM 8243  C CG  . LEU E 1 37  ? 136.988 -27.088 22.791  1.000 30.960  ? 54  LEU EEE CG  1 
ATOM 8244  C CD1 . LEU E 1 37  ? 135.695 -27.358 23.523  1.000 30.920  ? 54  LEU EEE CD1 1 
ATOM 8245  C CD2 . LEU E 1 37  ? 137.107 -25.599 22.484  1.000 33.180  ? 54  LEU EEE CD2 1 
ATOM 8246  N N   . ARG E 1 38  ? 141.822 -28.113 23.487  1.000 33.310  ? 55  ARG EEE N   1 
ATOM 8247  C CA  . ARG E 1 38  ? 143.023 -28.257 24.337  1.000 34.420  ? 55  ARG EEE CA  1 
ATOM 8248  C C   . ARG E 1 38  ? 143.324 -26.902 24.981  1.000 33.510  ? 55  ARG EEE C   1 
ATOM 8249  O O   . ARG E 1 38  ? 143.415 -25.921 24.244  1.000 33.990  ? 55  ARG EEE O   1 
ATOM 8250  C CB  . ARG E 1 38  ? 144.188 -28.767 23.489  1.000 38.310  ? 55  ARG EEE CB  1 
ATOM 8251  C CG  . ARG E 1 38  ? 145.492 -28.983 24.243  1.000 38.680  ? 55  ARG EEE CG  1 
ATOM 8252  C CD  . ARG E 1 38  ? 145.799 -30.454 24.328  1.000 42.970  ? 55  ARG EEE CD  1 
ATOM 8253  N NE  . ARG E 1 38  ? 147.161 -30.602 24.805  1.000 43.920  ? 55  ARG EEE NE  1 
ATOM 8254  C CZ  . ARG E 1 38  ? 147.538 -30.447 26.078  1.000 47.820  ? 55  ARG EEE CZ  1 
ATOM 8255  N NH1 . ARG E 1 38  ? 146.677 -30.146 27.045  1.000 42.940  ? 55  ARG EEE NH1 1 
ATOM 8256  N NH2 . ARG E 1 38  ? 148.813 -30.603 26.380  1.000 53.790  ? 55  ARG EEE NH2 1 
ATOM 8257  N N   . GLY E 1 39  ? 143.441 -26.854 26.311  1.000 33.400  ? 56  GLY EEE N   1 
ATOM 8258  C CA  . GLY E 1 39  ? 143.739 -25.620 27.058  1.000 32.330  ? 56  GLY EEE CA  1 
ATOM 8259  C C   . GLY E 1 39  ? 142.477 -24.944 27.555  1.000 29.130  ? 56  GLY EEE C   1 
ATOM 8260  O O   . GLY E 1 39  ? 142.584 -23.903 28.198  1.000 28.260  ? 56  GLY EEE O   1 
ATOM 8261  N N   . PHE E 1 40  ? 141.319 -25.529 27.291  1.000 26.980  ? 57  PHE EEE N   1 
ATOM 8262  C CA  . PHE E 1 40  ? 140.040 -25.093 27.885  1.000 26.000  ? 57  PHE EEE CA  1 
ATOM 8263  C C   . PHE E 1 40  ? 139.541 -26.188 28.820  1.000 25.050  ? 57  PHE EEE C   1 
ATOM 8264  O O   . PHE E 1 40  ? 140.049 -27.319 28.757  1.000 23.760  ? 57  PHE EEE O   1 
ATOM 8265  C CB  . PHE E 1 40  ? 138.988 -24.809 26.815  1.000 27.390  ? 57  PHE EEE CB  1 
ATOM 8266  C CG  . PHE E 1 40  ? 139.346 -23.707 25.854  1.000 29.190  ? 57  PHE EEE CG  1 
ATOM 8267  C CD1 . PHE E 1 40  ? 140.302 -23.896 24.877  1.000 29.500  ? 57  PHE EEE CD1 1 
ATOM 8268  C CD2 . PHE E 1 40  ? 138.711 -22.480 25.914  1.000 31.100  ? 57  PHE EEE CD2 1 
ATOM 8269  C CE1 . PHE E 1 40  ? 140.610 -22.884 23.980  1.000 31.120  ? 57  PHE EEE CE1 1 
ATOM 8270  C CE2 . PHE E 1 40  ? 139.033 -21.459 25.029  1.000 31.260  ? 57  PHE EEE CE2 1 
ATOM 8271  C CZ  . PHE E 1 40  ? 139.983 -21.665 24.061  1.000 31.030  ? 57  PHE EEE CZ  1 
ATOM 8272  N N   . SER E 1 41  ? 138.594 -25.828 29.678  1.000 24.470  ? 58  SER EEE N   1 
ATOM 8273  C CA  . SER E 1 41  ? 137.732 -26.775 30.407  1.000 22.670  ? 58  SER EEE CA  1 
ATOM 8274  C C   . SER E 1 41  ? 136.423 -26.848 29.648  1.000 21.870  ? 58  SER EEE C   1 
ATOM 8275  O O   . SER E 1 41  ? 136.240 -26.077 28.697  1.000 19.350  ? 58  SER EEE O   1 
ATOM 8276  C CB  . SER E 1 41  ? 137.488 -26.361 31.823  1.000 22.790  ? 58  SER EEE CB  1 
ATOM 8277  O OG  . SER E 1 41  ? 136.548 -25.295 31.884  1.000 23.470  ? 58  SER EEE OG  1 
ATOM 8278  N N   . LYS E 1 42  ? 135.577 -27.775 30.081  1.000 24.470  ? 59  LYS EEE N   1 
ATOM 8279  C CA  . LYS E 1 42  ? 134.191 -27.891 29.599  1.000 25.060  ? 59  LYS EEE CA  1 
ATOM 8280  C C   . LYS E 1 42  ? 133.437 -26.734 30.219  1.000 24.010  ? 59  LYS EEE C   1 
ATOM 8281  O O   . LYS E 1 42  ? 133.790 -26.332 31.342  1.000 21.020  ? 59  LYS EEE O   1 
ATOM 8282  C CB  . LYS E 1 42  ? 133.583 -29.240 29.988  1.000 26.840  ? 59  LYS EEE CB  1 
ATOM 8283  C CG  . LYS E 1 42  ? 132.152 -29.458 29.508  1.000 29.510  ? 59  LYS EEE CG  1 
ATOM 8284  C CD  . LYS E 1 42  ? 131.624 -30.830 29.879  1.000 32.410  ? 59  LYS EEE CD  1 
ATOM 8285  C CE  . LYS E 1 42  ? 130.211 -31.097 29.423  1.000 33.130  ? 59  LYS EEE CE  1 
ATOM 8286  N NZ  . LYS E 1 42  ? 129.781 -32.427 29.910  1.000 34.290  ? 59  LYS EEE NZ  1 
ATOM 8287  N N   . SER E 1 43  ? 132.452 -26.215 29.505  1.000 26.440  ? 60  SER EEE N   1 
ATOM 8288  C CA  . SER E 1 43  ? 131.563 -25.159 30.040  1.000 27.700  ? 60  SER EEE CA  1 
ATOM 8289  C C   . SER E 1 43  ? 131.045 -25.604 31.418  1.000 28.330  ? 60  SER EEE C   1 
ATOM 8290  O O   . SER E 1 43  ? 130.458 -26.694 31.525  1.000 30.570  ? 60  SER EEE O   1 
ATOM 8291  C CB  . SER E 1 43  ? 130.471 -24.802 29.077  1.000 29.930  ? 60  SER EEE CB  1 
ATOM 8292  O OG  . SER E 1 43  ? 131.012 -24.005 28.022  1.000 30.450  ? 60  SER EEE OG  1 
ATOM 8293  N N   . ILE E 1 44  ? 131.315 -24.775 32.428  1.000 26.190  ? 61  ILE EEE N   1 
ATOM 8294  C CA  . ILE E 1 44  ? 131.127 -25.044 33.877  1.000 23.700  ? 61  ILE EEE CA  1 
ATOM 8295  C C   . ILE E 1 44  ? 129.644 -25.116 34.177  1.000 24.040  ? 61  ILE EEE C   1 
ATOM 8296  O O   . ILE E 1 44  ? 128.921 -24.243 33.698  1.000 25.990  ? 61  ILE EEE O   1 
ATOM 8297  C CB  . ILE E 1 44  ? 131.793 -23.931 34.694  1.000 21.930  ? 61  ILE EEE CB  1 
ATOM 8298  C CG1 . ILE E 1 44  ? 133.298 -23.919 34.430  1.000 22.900  ? 61  ILE EEE CG1 1 
ATOM 8299  C CG2 . ILE E 1 44  ? 131.475 -24.140 36.151  1.000 21.350  ? 61  ILE EEE CG2 1 
ATOM 8300  C CD1 . ILE E 1 44  ? 134.087 -22.923 35.232  1.000 22.730  ? 61  ILE EEE CD1 1 
ATOM 8301  N N   . SER E 1 45  ? 129.208 -26.123 34.924  1.000 24.440  ? 62  SER EEE N   1 
ATOM 8302  C CA  . SER E 1 45  ? 127.804 -26.224 35.396  1.000 26.310  ? 62  SER EEE CA  1 
ATOM 8303  C C   . SER E 1 45  ? 127.842 -26.176 36.922  1.000 27.000  ? 62  SER EEE C   1 
ATOM 8304  O O   . SER E 1 45  ? 128.948 -26.396 37.482  1.000 27.860  ? 62  SER EEE O   1 
ATOM 8305  C CB  . SER E 1 45  ? 127.113 -27.484 34.885  1.000 27.080  ? 62  SER EEE CB  1 
ATOM 8306  O OG  . SER E 1 45  ? 127.763 -28.040 33.738  1.000 26.110  ? 62  SER EEE OG  1 
ATOM 8307  N N   . ILE E 1 46  ? 126.689 -25.968 37.561  1.000 25.170  ? 63  ILE EEE N   1 
ATOM 8308  C CA  . ILE E 1 46  ? 126.587 -25.844 39.039  1.000 24.740  ? 63  ILE EEE CA  1 
ATOM 8309  C C   . ILE E 1 46  ? 125.663 -26.940 39.597  1.000 25.180  ? 63  ILE EEE C   1 
ATOM 8310  O O   . ILE E 1 46  ? 124.522 -27.115 39.075  1.000 25.230  ? 63  ILE EEE O   1 
ATOM 8311  C CB  . ILE E 1 46  ? 126.062 -24.445 39.376  1.000 26.610  ? 63  ILE EEE CB  1 
ATOM 8312  C CG1 . ILE E 1 46  ? 127.046 -23.349 38.968  1.000 26.800  ? 63  ILE EEE CG1 1 
ATOM 8313  C CG2 . ILE E 1 46  ? 125.713 -24.359 40.850  1.000 29.880  ? 63  ILE EEE CG2 1 
ATOM 8314  C CD1 . ILE E 1 46  ? 126.542 -21.919 39.185  1.000 25.810  ? 63  ILE EEE CD1 1 
ATOM 8315  N N   . SER E 1 47  ? 126.063 -27.603 40.674  1.000 24.000  ? 64  SER EEE N   1 
ATOM 8316  C CA  . SER E 1 47  ? 125.277 -28.713 41.270  1.000 24.790  ? 64  SER EEE CA  1 
ATOM 8317  C C   . SER E 1 47  ? 123.850 -28.270 41.588  1.000 24.470  ? 64  SER EEE C   1 
ATOM 8318  O O   . SER E 1 47  ? 123.628 -27.090 41.893  1.000 23.550  ? 64  SER EEE O   1 
ATOM 8319  C CB  . SER E 1 47  ? 125.946 -29.297 42.480  1.000 26.960  ? 64  SER EEE CB  1 
ATOM 8320  O OG  . SER E 1 47  ? 126.405 -28.274 43.342  1.000 30.510  ? 64  SER EEE OG  1 
ATOM 8321  N N   . ASP E 1 48  ? 122.919 -29.216 41.497  1.000 26.180  ? 65  ASP EEE N   1 
ATOM 8322  C CA  . ASP E 1 48  ? 121.495 -29.044 41.887  1.000 29.060  ? 65  ASP EEE CA  1 
ATOM 8323  C C   . ASP E 1 48  ? 121.430 -28.655 43.375  1.000 27.980  ? 65  ASP EEE C   1 
ATOM 8324  O O   . ASP E 1 48  ? 120.508 -27.917 43.738  1.000 30.100  ? 65  ASP EEE O   1 
ATOM 8325  C CB  . ASP E 1 48  ? 120.656 -30.280 41.501  1.000 30.380  ? 65  ASP EEE CB  1 
ATOM 8326  C CG  . ASP E 1 48  ? 121.098 -31.611 42.104  1.000 32.470  ? 65  ASP EEE CG  1 
ATOM 8327  O OD1 . ASP E 1 48  ? 122.235 -32.078 41.779  1.000 32.110  ? 65  ASP EEE OD1 1 
ATOM 8328  O OD2 . ASP E 1 48  ? 120.290 -32.192 42.885  1.000 36.130  ? 65  ASP EEE OD2 1 
ATOM 8329  N N   . THR E 1 49  ? 122.372 -29.125 44.198  1.000 26.960  ? 66  THR EEE N   1 
ATOM 8330  C CA  . THR E 1 49  ? 122.358 -28.980 45.679  1.000 27.520  ? 66  THR EEE CA  1 
ATOM 8331  C C   . THR E 1 49  ? 123.783 -28.986 46.229  1.000 25.880  ? 66  THR EEE C   1 
ATOM 8332  O O   . THR E 1 49  ? 124.673 -29.525 45.574  1.000 23.060  ? 66  THR EEE O   1 
ATOM 8333  C CB  . THR E 1 49  ? 121.612 -30.116 46.394  1.000 27.380  ? 66  THR EEE CB  1 
ATOM 8334  O OG1 . THR E 1 49  ? 122.382 -31.307 46.198  1.000 28.750  ? 66  THR EEE OG1 1 
ATOM 8335  C CG2 . THR E 1 49  ? 120.182 -30.281 45.938  1.000 25.360  ? 66  THR EEE CG2 1 
ATOM 8336  N N   . PHE E 1 50  ? 123.968 -28.460 47.434  1.000 26.890  ? 67  PHE EEE N   1 
ATOM 8337  C CA  . PHE E 1 50  ? 125.323 -28.327 48.014  1.000 29.250  ? 67  PHE EEE CA  1 
ATOM 8338  C C   . PHE E 1 50  ? 125.907 -29.719 48.242  1.000 30.910  ? 67  PHE EEE C   1 
ATOM 8339  O O   . PHE E 1 50  ? 127.138 -29.894 48.191  1.000 30.530  ? 67  PHE EEE O   1 
ATOM 8340  C CB  . PHE E 1 50  ? 125.281 -27.531 49.317  1.000 29.180  ? 67  PHE EEE CB  1 
ATOM 8341  C CG  . PHE E 1 50  ? 126.639 -27.128 49.818  1.000 27.800  ? 67  PHE EEE CG  1 
ATOM 8342  C CD1 . PHE E 1 50  ? 127.383 -26.174 49.149  1.000 28.070  ? 67  PHE EEE CD1 1 
ATOM 8343  C CD2 . PHE E 1 50  ? 127.157 -27.682 50.961  1.000 28.180  ? 67  PHE EEE CD2 1 
ATOM 8344  C CE1 . PHE E 1 50  ? 128.629 -25.797 49.609  1.000 28.590  ? 67  PHE EEE CE1 1 
ATOM 8345  C CE2 . PHE E 1 50  ? 128.405 -27.305 51.423  1.000 30.160  ? 67  PHE EEE CE2 1 
ATOM 8346  C CZ  . PHE E 1 50  ? 129.138 -26.356 50.753  1.000 28.830  ? 67  PHE EEE CZ  1 
ATOM 8347  N N   . GLU E 1 51  ? 125.005 -30.665 48.495  1.000 32.300  ? 68  GLU EEE N   1 
ATOM 8348  C CA  . GLU E 1 51  ? 125.299 -32.046 48.949  1.000 31.130  ? 68  GLU EEE CA  1 
ATOM 8349  C C   . GLU E 1 51  ? 125.726 -32.867 47.743  1.000 32.810  ? 68  GLU EEE C   1 
ATOM 8350  O O   . GLU E 1 51  ? 126.545 -33.756 47.943  1.000 37.410  ? 68  GLU EEE O   1 
ATOM 8351  C CB  . GLU E 1 51  ? 124.070 -32.645 49.633  1.000 29.790  ? 68  GLU EEE CB  1 
ATOM 8352  C CG  . GLU E 1 51  ? 123.709 -31.931 50.923  1.000 30.860  ? 68  GLU EEE CG  1 
ATOM 8353  C CD  . GLU E 1 51  ? 122.649 -30.833 50.885  1.000 29.370  ? 68  GLU EEE CD  1 
ATOM 8354  O OE1 . GLU E 1 51  ? 121.925 -30.690 51.883  1.000 31.050  ? 68  GLU EEE OE1 1 
ATOM 8355  O OE2 . GLU E 1 51  ? 122.552 -30.096 49.897  1.000 28.480  ? 68  GLU EEE OE2 1 
ATOM 8356  N N   . SER E 1 52  ? 125.226 -32.537 46.546  1.000 31.840  ? 69  SER EEE N   1 
ATOM 8357  C CA  . SER E 1 52  ? 125.363 -33.363 45.318  1.000 30.170  ? 69  SER EEE CA  1 
ATOM 8358  C C   . SER E 1 52  ? 126.439 -32.823 44.374  1.000 28.370  ? 69  SER EEE C   1 
ATOM 8359  O O   . SER E 1 52  ? 126.458 -33.232 43.215  1.000 23.980  ? 69  SER EEE O   1 
ATOM 8360  C CB  . SER E 1 52  ? 124.032 -33.457 44.620  1.000 30.600  ? 69  SER EEE CB  1 
ATOM 8361  O OG  . SER E 1 52  ? 123.581 -32.196 44.141  1.000 26.690  ? 69  SER EEE OG  1 
ATOM 8362  N N   . ASP E 1 53  ? 127.289 -31.903 44.826  1.000 32.290  ? 70  ASP EEE N   1 
ATOM 8363  C CA  . ASP E 1 53  ? 128.410 -31.375 43.997  1.000 31.090  ? 70  ASP EEE CA  1 
ATOM 8364  C C   . ASP E 1 53  ? 129.179 -32.583 43.459  1.000 32.910  ? 70  ASP EEE C   1 
ATOM 8365  O O   . ASP E 1 53  ? 129.606 -33.415 44.303  1.000 42.770  ? 70  ASP EEE O   1 
ATOM 8366  C CB  . ASP E 1 53  ? 129.340 -30.481 44.818  1.000 28.460  ? 70  ASP EEE CB  1 
ATOM 8367  C CG  . ASP E 1 53  ? 130.340 -29.714 43.980  1.000 25.910  ? 70  ASP EEE CG  1 
ATOM 8368  O OD1 . ASP E 1 53  ? 129.933 -29.127 42.980  1.000 22.440  ? 70  ASP EEE OD1 1 
ATOM 8369  O OD2 . ASP E 1 53  ? 131.511 -29.674 44.375  1.000 25.400  ? 70  ASP EEE OD2 1 
ATOM 8370  N N   . SER E 1 54  ? 129.298 -32.732 42.139  1.000 28.750  ? 71  SER EEE N   1 
ATOM 8371  C CA  . SER E 1 54  ? 130.118 -33.817 41.537  1.000 27.640  ? 71  SER EEE CA  1 
ATOM 8372  C C   . SER E 1 54  ? 130.580 -33.437 40.138  1.000 27.090  ? 71  SER EEE C   1 
ATOM 8373  O O   . SER E 1 54  ? 130.098 -33.953 39.139  1.000 26.900  ? 71  SER EEE O   1 
ATOM 8374  C CB  . SER E 1 54  ? 129.407 -35.141 41.552  1.000 28.390  ? 71  SER EEE CB  1 
ATOM 8375  O OG  . SER E 1 54  ? 128.072 -35.035 41.130  1.000 28.360  ? 71  SER EEE OG  1 
ATOM 8376  N N   . PRO E 1 55  ? 131.627 -32.581 40.039  1.000 25.090  ? 72  PRO EEE N   1 
ATOM 8377  C CA  . PRO E 1 55  ? 132.117 -32.100 38.755  1.000 26.230  ? 72  PRO EEE CA  1 
ATOM 8378  C C   . PRO E 1 55  ? 132.655 -33.219 37.854  1.000 28.800  ? 72  PRO EEE C   1 
ATOM 8379  O O   . PRO E 1 55  ? 133.374 -34.056 38.378  1.000 31.310  ? 72  PRO EEE O   1 
ATOM 8380  C CB  . PRO E 1 55  ? 133.300 -31.239 39.195  1.000 26.310  ? 72  PRO EEE CB  1 
ATOM 8381  C CG  . PRO E 1 55  ? 133.759 -31.867 40.461  1.000 25.190  ? 72  PRO EEE CG  1 
ATOM 8382  C CD  . PRO E 1 55  ? 132.454 -32.135 41.151  1.000 24.610  ? 72  PRO EEE CD  1 
ATOM 8383  N N   . ASN E 1 56  ? 132.312 -33.187 36.559  1.000 29.780  ? 73  ASN EEE N   1 
ATOM 8384  C CA  . ASN E 1 56  ? 132.847 -34.097 35.511  1.000 30.740  ? 73  ASN EEE CA  1 
ATOM 8385  C C   . ASN E 1 56  ? 134.348 -33.852 35.392  1.000 31.430  ? 73  ASN EEE C   1 
ATOM 8386  O O   . ASN E 1 56  ? 134.778 -32.720 35.669  1.000 33.940  ? 73  ASN EEE O   1 
ATOM 8387  C CB  . ASN E 1 56  ? 132.217 -33.839 34.143  1.000 34.830  ? 73  ASN EEE CB  1 
ATOM 8388  C CG  . ASN E 1 56  ? 130.745 -34.192 34.059  1.000 38.230  ? 73  ASN EEE CG  1 
ATOM 8389  O OD1 . ASN E 1 56  ? 130.127 -34.587 35.054  1.000 40.200  ? 73  ASN EEE OD1 1 
ATOM 8390  N ND2 . ASN E 1 56  ? 130.194 -34.093 32.856  1.000 36.760  ? 73  ASN EEE ND2 1 
ATOM 8391  N N   . ARG E 1 57  ? 135.116 -34.851 34.964  1.000 32.490  ? 74  ARG EEE N   1 
ATOM 8392  C CA  . ARG E 1 57  ? 136.604 -34.750 34.948  1.000 33.680  ? 74  ARG EEE CA  1 
ATOM 8393  C C   . ARG E 1 57  ? 137.100 -33.626 34.017  1.000 31.470  ? 74  ARG EEE C   1 
ATOM 8394  O O   . ARG E 1 57  ? 138.185 -33.053 34.286  1.000 25.570  ? 74  ARG EEE O   1 
ATOM 8395  C CB  . ARG E 1 57  ? 137.195 -36.099 34.545  1.000 34.770  ? 74  ARG EEE CB  1 
ATOM 8396  C CG  . ARG E 1 57  ? 138.711 -36.138 34.556  1.000 37.310  ? 74  ARG EEE CG  1 
ATOM 8397  C CD  . ARG E 1 57  ? 139.223 -37.451 34.025  1.000 40.970  ? 74  ARG EEE CD  1 
ATOM 8398  N NE  . ARG E 1 57  ? 140.673 -37.472 34.092  1.000 45.650  ? 74  ARG EEE NE  1 
ATOM 8399  C CZ  . ARG E 1 57  ? 141.443 -38.301 33.416  1.000 45.480  ? 74  ARG EEE CZ  1 
ATOM 8400  N NH1 . ARG E 1 57  ? 140.897 -39.210 32.633  1.000 51.370  ? 74  ARG EEE NH1 1 
ATOM 8401  N NH2 . ARG E 1 57  ? 142.753 -38.233 33.536  1.000 44.490  ? 74  ARG EEE NH2 1 
ATOM 8402  N N   . ASP E 1 58  ? 136.342 -33.348 32.955  1.000 31.680  ? 75  ASP EEE N   1 
ATOM 8403  C CA  . ASP E 1 58  ? 136.721 -32.381 31.894  1.000 31.560  ? 75  ASP EEE CA  1 
ATOM 8404  C C   . ASP E 1 58  ? 136.315 -30.956 32.308  1.000 27.720  ? 75  ASP EEE C   1 
ATOM 8405  O O   . ASP E 1 58  ? 136.508 -30.024 31.491  1.000 24.710  ? 75  ASP EEE O   1 
ATOM 8406  C CB  . ASP E 1 58  ? 136.121 -32.797 30.541  1.000 36.580  ? 75  ASP EEE CB  1 
ATOM 8407  C CG  . ASP E 1 58  ? 134.639 -33.141 30.542  1.000 39.730  ? 75  ASP EEE CG  1 
ATOM 8408  O OD1 . ASP E 1 58  ? 133.974 -32.931 31.575  1.000 50.350  ? 75  ASP EEE OD1 1 
ATOM 8409  O OD2 . ASP E 1 58  ? 134.149 -33.573 29.506  1.000 39.620  ? 75  ASP EEE OD2 1 
ATOM 8410  N N   . MET E 1 59  ? 135.781 -30.780 33.525  1.000 24.890  ? 76  MET EEE N   1 
ATOM 8411  C CA  . MET E 1 59  ? 135.446 -29.450 34.083  1.000 25.240  ? 76  MET EEE CA  1 
ATOM 8412  C C   . MET E 1 59  ? 136.482 -29.040 35.140  1.000 27.300  ? 76  MET EEE C   1 
ATOM 8413  O O   . MET E 1 59  ? 136.324 -27.937 35.745  1.000 29.990  ? 76  MET EEE O   1 
ATOM 8414  C CB  . MET E 1 59  ? 134.063 -29.497 34.720  1.000 23.910  ? 76  MET EEE CB  1 
ATOM 8415  C CG  . MET E 1 59  ? 133.426 -28.153 34.815  1.000 24.730  ? 76  MET EEE CG  1 
ATOM 8416  S SD  . MET E 1 59  ? 131.912 -28.177 35.765  1.000 27.200  ? 76  MET EEE SD  1 
ATOM 8417  C CE  . MET E 1 59  ? 132.552 -28.219 37.427  1.000 27.890  ? 76  MET EEE CE  1 
ATOM 8418  N N   . LEU E 1 60  ? 137.489 -29.886 35.383  1.000 27.400  ? 77  LEU EEE N   1 
ATOM 8419  C CA  . LEU E 1 60  ? 138.453 -29.722 36.504  1.000 26.480  ? 77  LEU EEE CA  1 
ATOM 8420  C C   . LEU E 1 60  ? 139.862 -29.557 35.956  1.000 26.500  ? 77  LEU EEE C   1 
ATOM 8421  O O   . LEU E 1 60  ? 140.516 -30.521 35.563  1.000 30.070  ? 77  LEU EEE O   1 
ATOM 8422  C CB  . LEU E 1 60  ? 138.399 -30.940 37.425  1.000 27.090  ? 77  LEU EEE CB  1 
ATOM 8423  C CG  . LEU E 1 60  ? 137.122 -31.131 38.234  1.000 27.550  ? 77  LEU EEE CG  1 
ATOM 8424  C CD1 . LEU E 1 60  ? 137.216 -32.413 39.059  1.000 29.270  ? 77  LEU EEE CD1 1 
ATOM 8425  C CD2 . LEU E 1 60  ? 136.872 -29.935 39.123  1.000 27.280  ? 77  LEU EEE CD2 1 
ATOM 8426  N N   . PRO E 1 61  ? 140.383 -28.322 35.920  1.000 24.170  ? 78  PRO EEE N   1 
ATOM 8427  C CA  . PRO E 1 61  ? 141.823 -28.108 35.781  1.000 24.160  ? 78  PRO EEE CA  1 
ATOM 8428  C C   . PRO E 1 61  ? 142.631 -28.931 36.789  1.000 21.830  ? 78  PRO EEE C   1 
ATOM 8429  O O   . PRO E 1 61  ? 142.138 -29.119 37.890  1.000 19.420  ? 78  PRO EEE O   1 
ATOM 8430  C CB  . PRO E 1 61  ? 142.005 -26.618 36.109  1.000 24.710  ? 78  PRO EEE CB  1 
ATOM 8431  C CG  . PRO E 1 61  ? 140.642 -25.997 35.775  1.000 24.400  ? 78  PRO EEE CG  1 
ATOM 8432  C CD  . PRO E 1 61  ? 139.609 -27.084 35.982  1.000 23.330  ? 78  PRO EEE CD  1 
ATOM 8433  N N   . CYS E 1 62  ? 143.838 -29.338 36.388  1.000 22.060  ? 79  CYS EEE N   1 
ATOM 8434  C CA  . CYS E 1 62  ? 144.782 -30.165 37.189  1.000 23.820  ? 79  CYS EEE CA  1 
ATOM 8435  C C   . CYS E 1 62  ? 146.198 -29.601 37.165  1.000 23.900  ? 79  CYS EEE C   1 
ATOM 8436  O O   . CYS E 1 62  ? 146.611 -29.005 36.131  1.000 26.040  ? 79  CYS EEE O   1 
ATOM 8437  C CB  . CYS E 1 62  ? 144.867 -31.581 36.643  1.000 25.740  ? 79  CYS EEE CB  1 
ATOM 8438  S SG  . CYS E 1 62  ? 143.272 -32.436 36.604  1.000 27.830  ? 79  CYS EEE SG  1 
ATOM 8439  N N   . TYR E 1 63  ? 146.942 -29.863 38.232  1.000 24.720  ? 80  TYR EEE N   1 
ATOM 8440  C CA  . TYR E 1 63  ? 148.402 -29.602 38.299  1.000 27.310  ? 80  TYR EEE CA  1 
ATOM 8441  C C   . TYR E 1 63  ? 149.079 -30.321 37.135  1.000 29.860  ? 80  TYR EEE C   1 
ATOM 8442  O O   . TYR E 1 63  ? 148.723 -31.494 36.828  1.000 38.740  ? 80  TYR EEE O   1 
ATOM 8443  C CB  . TYR E 1 63  ? 149.007 -30.066 39.633  1.000 27.360  ? 80  TYR EEE CB  1 
ATOM 8444  C CG  . TYR E 1 63  ? 148.651 -29.236 40.842  1.000 25.860  ? 80  TYR EEE CG  1 
ATOM 8445  C CD1 . TYR E 1 63  ? 147.454 -29.413 41.516  1.000 25.740  ? 80  TYR EEE CD1 1 
ATOM 8446  C CD2 . TYR E 1 63  ? 149.531 -28.279 41.313  1.000 25.350  ? 80  TYR EEE CD2 1 
ATOM 8447  C CE1 . TYR E 1 63  ? 147.133 -28.634 42.611  1.000 26.870  ? 80  TYR EEE CE1 1 
ATOM 8448  C CE2 . TYR E 1 63  ? 149.223 -27.489 42.406  1.000 26.730  ? 80  TYR EEE CE2 1 
ATOM 8449  C CZ  . TYR E 1 63  ? 148.021 -27.675 43.062  1.000 27.450  ? 80  TYR EEE CZ  1 
ATOM 8450  O OH  . TYR E 1 63  ? 147.713 -26.913 44.152  1.000 29.720  ? 80  TYR EEE OH  1 
ATOM 8451  N N   . SER E 1 64  ? 150.021 -29.630 36.501  1.000 30.900  ? 81  SER EEE N   1 
ATOM 8452  C CA  . SER E 1 64  ? 150.920 -30.180 35.456  1.000 32.500  ? 81  SER EEE CA  1 
ATOM 8453  C C   . SER E 1 64  ? 152.250 -30.489 36.139  1.000 30.690  ? 81  SER EEE C   1 
ATOM 8454  O O   . SER E 1 64  ? 152.647 -29.703 37.022  1.000 30.980  ? 81  SER EEE O   1 
ATOM 8455  C CB  . SER E 1 64  ? 151.067 -29.210 34.285  1.000 35.390  ? 81  SER EEE CB  1 
ATOM 8456  O OG  . SER E 1 64  ? 149.815 -28.598 33.927  1.000 41.890  ? 81  SER EEE OG  1 
ATOM 8457  N N   . VAL E 1 65  ? 152.878 -31.613 35.795  1.000 30.440  ? 82  VAL EEE N   1 
ATOM 8458  C CA  . VAL E 1 65  ? 154.203 -32.034 36.345  1.000 30.550  ? 82  VAL EEE CA  1 
ATOM 8459  C C   . VAL E 1 65  ? 155.037 -32.624 35.223  1.000 26.820  ? 82  VAL EEE C   1 
ATOM 8460  O O   . VAL E 1 65  ? 154.468 -33.209 34.341  1.000 22.910  ? 82  VAL EEE O   1 
ATOM 8461  C CB  . VAL E 1 65  ? 154.064 -33.059 37.486  1.000 34.250  ? 82  VAL EEE CB  1 
ATOM 8462  C CG1 . VAL E 1 65  ? 153.194 -34.248 37.071  1.000 36.450  ? 82  VAL EEE CG1 1 
ATOM 8463  C CG2 . VAL E 1 65  ? 155.428 -33.501 38.008  1.000 33.560  ? 82  VAL EEE CG2 1 
ATOM 8464  N N   . ALA E 1 66  ? 156.352 -32.511 35.322  1.000 30.480  ? 83  ALA EEE N   1 
ATOM 8465  C CA  . ALA E 1 66  ? 157.313 -33.027 34.325  1.000 33.400  ? 83  ALA EEE CA  1 
ATOM 8466  C C   . ALA E 1 66  ? 158.561 -33.495 35.060  1.000 35.590  ? 83  ALA EEE C   1 
ATOM 8467  O O   . ALA E 1 66  ? 159.178 -32.641 35.726  1.000 32.920  ? 83  ALA EEE O   1 
ATOM 8468  C CB  . ALA E 1 66  ? 157.641 -31.945 33.330  1.000 33.690  ? 83  ALA EEE CB  1 
ATOM 8469  N N   . ARG E 1 67  ? 158.889 -34.789 34.935  1.000 38.930  ? 84  ARG EEE N   1 
ATOM 8470  C CA  . ARG E 1 67  ? 160.144 -35.381 35.464  1.000 40.800  ? 84  ARG EEE CA  1 
ATOM 8471  C C   . ARG E 1 67  ? 161.200 -35.276 34.362  1.000 37.810  ? 84  ARG EEE C   1 
ATOM 8472  O O   . ARG E 1 67  ? 160.941 -35.801 33.289  1.000 41.450  ? 84  ARG EEE O   1 
ATOM 8473  C CB  . ARG E 1 67  ? 159.904 -36.832 35.912  1.000 46.040  ? 84  ARG EEE CB  1 
ATOM 8474  C CG  . ARG E 1 67  ? 161.021 -37.354 36.811  1.000 57.140  ? 84  ARG EEE CG  1 
ATOM 8475  C CD  . ARG E 1 67  ? 160.791 -38.711 37.451  1.000 59.630  ? 84  ARG EEE CD  1 
ATOM 8476  N NE  . ARG E 1 67  ? 160.283 -39.706 36.539  1.000 65.280  ? 84  ARG EEE NE  1 
ATOM 8477  C CZ  . ARG E 1 67  ? 160.987 -40.310 35.596  1.000 75.040  ? 84  ARG EEE CZ  1 
ATOM 8478  N NH1 . ARG E 1 67  ? 162.265 -40.023 35.390  1.000 72.190  ? 84  ARG EEE NH1 1 
ATOM 8479  N NH2 . ARG E 1 67  ? 160.387 -41.215 34.841  1.000 87.980  ? 84  ARG EEE NH2 1 
ATOM 8480  N N   . ILE E 1 68  ? 162.306 -34.567 34.578  1.000 36.790  ? 85  ILE EEE N   1 
ATOM 8481  C CA  . ILE E 1 68  ? 163.374 -34.389 33.547  1.000 40.290  ? 85  ILE EEE CA  1 
ATOM 8482  C C   . ILE E 1 68  ? 164.594 -35.195 33.989  1.000 48.080  ? 85  ILE EEE C   1 
ATOM 8483  O O   . ILE E 1 68  ? 165.177 -34.912 35.041  1.000 53.600  ? 85  ILE EEE O   1 
ATOM 8484  C CB  . ILE E 1 68  ? 163.753 -32.909 33.342  1.000 41.300  ? 85  ILE EEE CB  1 
ATOM 8485  C CG1 . ILE E 1 68  ? 162.545 -31.964 33.313  1.000 44.000  ? 85  ILE EEE CG1 1 
ATOM 8486  C CG2 . ILE E 1 68  ? 164.625 -32.748 32.116  1.000 40.630  ? 85  ILE EEE CG2 1 
ATOM 8487  C CD1 . ILE E 1 68  ? 161.552 -32.217 32.219  1.000 44.750  ? 85  ILE EEE CD1 1 
ATOM 8488  N N   . PRO E 1 69  ? 165.063 -36.196 33.199  1.000 50.500  ? 86  PRO EEE N   1 
ATOM 8489  C CA  . PRO E 1 69  ? 166.254 -36.950 33.562  1.000 46.330  ? 86  PRO EEE CA  1 
ATOM 8490  C C   . PRO E 1 69  ? 167.472 -36.072 33.252  1.000 46.830  ? 86  PRO EEE C   1 
ATOM 8491  O O   . PRO E 1 69  ? 167.507 -35.479 32.188  1.000 40.150  ? 86  PRO EEE O   1 
ATOM 8492  C CB  . PRO E 1 69  ? 166.192 -38.200 32.688  1.000 44.770  ? 86  PRO EEE CB  1 
ATOM 8493  C CG  . PRO E 1 69  ? 164.842 -38.139 32.014  1.000 44.490  ? 86  PRO EEE CG  1 
ATOM 8494  C CD  . PRO E 1 69  ? 164.518 -36.661 31.919  1.000 49.040  ? 86  PRO EEE CD  1 
ATOM 8495  N N   . LEU E 1 70  ? 168.408 -36.001 34.196  1.000 49.520  ? 87  LEU EEE N   1 
ATOM 8496  C CA  . LEU E 1 70  ? 169.646 -35.197 34.070  1.000 52.180  ? 87  LEU EEE CA  1 
ATOM 8497  C C   . LEU E 1 70  ? 170.822 -36.101 33.716  1.000 53.580  ? 87  LEU EEE C   1 
ATOM 8498  O O   . LEU E 1 70  ? 170.753 -37.312 33.909  1.000 55.990  ? 87  LEU EEE O   1 
ATOM 8499  C CB  . LEU E 1 70  ? 169.882 -34.493 35.404  1.000 51.970  ? 87  LEU EEE CB  1 
ATOM 8500  C CG  . LEU E 1 70  ? 168.733 -33.610 35.856  1.000 54.180  ? 87  LEU EEE CG  1 
ATOM 8501  C CD1 . LEU E 1 70  ? 168.982 -33.079 37.264  1.000 56.720  ? 87  LEU EEE CD1 1 
ATOM 8502  C CD2 . LEU E 1 70  ? 168.526 -32.469 34.876  1.000 52.880  ? 87  LEU EEE CD2 1 
ATOM 8503  N N   . PRO E 1 71  ? 171.933 -35.542 33.200  1.000 50.420  ? 88  PRO EEE N   1 
ATOM 8504  C CA  . PRO E 1 71  ? 173.158 -36.300 32.982  1.000 53.600  ? 88  PRO EEE CA  1 
ATOM 8505  C C   . PRO E 1 71  ? 173.582 -37.166 34.167  1.000 59.560  ? 88  PRO EEE C   1 
ATOM 8506  O O   . PRO E 1 71  ? 173.606 -36.663 35.261  1.000 64.860  ? 88  PRO EEE O   1 
ATOM 8507  C CB  . PRO E 1 71  ? 174.193 -35.196 32.777  1.000 57.110  ? 88  PRO EEE CB  1 
ATOM 8508  C CG  . PRO E 1 71  ? 173.412 -34.098 32.087  1.000 57.190  ? 88  PRO EEE CG  1 
ATOM 8509  C CD  . PRO E 1 71  ? 172.049 -34.152 32.745  1.000 58.060  ? 88  PRO EEE CD  1 
ATOM 8510  N N   . ASN E 1 72  ? 173.898 -38.439 33.910  1.000 69.850  ? 89  ASN EEE N   1 
ATOM 8511  C CA  . ASN E 1 72  ? 174.102 -39.471 34.961  1.000 72.070  ? 89  ASN EEE CA  1 
ATOM 8512  C C   . ASN E 1 72  ? 175.376 -39.151 35.749  1.000 77.090  ? 89  ASN EEE C   1 
ATOM 8513  O O   . ASN E 1 72  ? 176.339 -38.677 35.128  1.000 80.470  ? 89  ASN EEE O   1 
ATOM 8514  C CB  . ASN E 1 72  ? 174.214 -40.849 34.331  1.000 76.620  ? 89  ASN EEE CB  1 
ATOM 8515  C CG  . ASN E 1 72  ? 174.008 -41.957 35.327  1.000 83.800  ? 89  ASN EEE CG  1 
ATOM 8516  O OD1 . ASN E 1 72  ? 174.241 -41.812 36.515  1.000 84.000  ? 89  ASN EEE OD1 1 
ATOM 8517  N ND2 . ASN E 1 72  ? 173.542 -43.086 34.833  1.000 99.200  ? 89  ASN EEE ND2 1 
ATOM 8518  N N   . LEU E 1 73  ? 175.381 -39.430 37.058  1.000 80.680  ? 90  LEU EEE N   1 
ATOM 8519  C CA  . LEU E 1 73  ? 176.541 -39.213 37.973  1.000 85.130  ? 90  LEU EEE CA  1 
ATOM 8520  C C   . LEU E 1 73  ? 176.612 -40.415 38.931  1.000 90.490  ? 90  LEU EEE C   1 
ATOM 8521  O O   . LEU E 1 73  ? 175.558 -40.725 39.556  1.000 116.230 ? 90  LEU EEE O   1 
ATOM 8522  C CB  . LEU E 1 73  ? 176.343 -37.931 38.787  1.000 85.460  ? 90  LEU EEE CB  1 
ATOM 8523  C CG  . LEU E 1 73  ? 175.800 -36.702 38.065  1.000 84.220  ? 90  LEU EEE CG  1 
ATOM 8524  C CD1 . LEU E 1 73  ? 175.379 -35.650 39.087  1.000 87.430  ? 90  LEU EEE CD1 1 
ATOM 8525  C CD2 . LEU E 1 73  ? 176.839 -36.126 37.128  1.000 83.630  ? 90  LEU EEE CD2 1 
ATOM 8526  N N   . ASN E 1 74  ? 177.736 -41.131 39.016  1.000 80.750  ? 91  ASN EEE N   1 
ATOM 8527  C CA  . ASN E 1 74  ? 177.828 -42.345 39.879  1.000 76.680  ? 91  ASN EEE CA  1 
ATOM 8528  C C   . ASN E 1 74  ? 177.149 -43.540 39.174  1.000 70.850  ? 91  ASN EEE C   1 
ATOM 8529  O O   . ASN E 1 74  ? 177.639 -43.979 38.107  1.000 55.760  ? 91  ASN EEE O   1 
ATOM 8530  C CB  . ASN E 1 74  ? 177.159 -42.107 41.255  1.000 68.450  ? 91  ASN EEE CB  1 
ATOM 8531  C CG  . ASN E 1 74  ? 177.388 -40.729 41.867  1.000 61.680  ? 91  ASN EEE CG  1 
ATOM 8532  O OD1 . ASN E 1 74  ? 177.078 -39.692 41.287  1.000 52.540  ? 91  ASN EEE OD1 1 
ATOM 8533  N ND2 . ASN E 1 74  ? 177.901 -40.693 43.082  1.000 61.590  ? 91  ASN EEE ND2 1 
ATOM 8534  N N   . ILE E 1 82  ? 178.822 -39.436 47.008  1.000 59.350  ? 99  ILE EEE N   1 
ATOM 8535  C CA  . ILE E 1 82  ? 178.032 -39.201 45.773  1.000 57.780  ? 99  ILE EEE CA  1 
ATOM 8536  C C   . ILE E 1 82  ? 178.110 -37.731 45.326  1.000 63.680  ? 99  ILE EEE C   1 
ATOM 8537  O O   . ILE E 1 82  ? 178.316 -36.828 46.167  1.000 71.920  ? 99  ILE EEE O   1 
ATOM 8538  C CB  . ILE E 1 82  ? 176.588 -39.595 45.971  1.000 48.830  ? 99  ILE EEE CB  1 
ATOM 8539  N N   . LEU E 1 83  ? 177.845 -37.501 44.036  1.000 64.230  ? 100 LEU EEE N   1 
ATOM 8540  C CA  . LEU E 1 83  ? 177.446 -36.180 43.462  1.000 63.560  ? 100 LEU EEE CA  1 
ATOM 8541  C C   . LEU E 1 83  ? 175.941 -36.162 43.182  1.000 61.560  ? 100 LEU EEE C   1 
ATOM 8542  O O   . LEU E 1 83  ? 175.440 -37.189 42.674  1.000 62.780  ? 100 LEU EEE O   1 
ATOM 8543  C CB  . LEU E 1 83  ? 178.203 -35.935 42.156  1.000 61.110  ? 100 LEU EEE CB  1 
ATOM 8544  C CG  . LEU E 1 83  ? 179.705 -35.726 42.309  1.000 61.110  ? 100 LEU EEE CG  1 
ATOM 8545  C CD1 . LEU E 1 83  ? 180.305 -35.180 41.026  1.000 58.890  ? 100 LEU EEE CD1 1 
ATOM 8546  C CD2 . LEU E 1 83  ? 180.023 -34.795 43.475  1.000 68.350  ? 100 LEU EEE CD2 1 
ATOM 8547  N N   . MET E 1 84  ? 175.275 -35.029 43.449  1.000 57.090  ? 101 MET EEE N   1 
ATOM 8548  C CA  . MET E 1 84  ? 173.867 -34.761 43.042  1.000 59.480  ? 101 MET EEE CA  1 
ATOM 8549  C C   . MET E 1 84  ? 173.789 -33.414 42.311  1.000 64.980  ? 101 MET EEE C   1 
ATOM 8550  O O   . MET E 1 84  ? 174.597 -32.495 42.631  1.000 70.430  ? 101 MET EEE O   1 
ATOM 8551  C CB  . MET E 1 84  ? 172.916 -34.715 44.243  1.000 57.030  ? 101 MET EEE CB  1 
ATOM 8552  C CG  . MET E 1 84  ? 172.927 -35.966 45.073  1.000 51.320  ? 101 MET EEE CG  1 
ATOM 8553  S SD  . MET E 1 84  ? 171.729 -35.836 46.414  1.000 45.630  ? 101 MET EEE SD  1 
ATOM 8554  C CE  . MET E 1 84  ? 170.213 -36.221 45.524  1.000 45.780  ? 101 MET EEE CE  1 
ATOM 8555  N N   . TRP E 1 85  ? 172.829 -33.287 41.389  1.000 59.420  ? 102 TRP EEE N   1 
ATOM 8556  C CA  . TRP E 1 85  ? 172.532 -32.001 40.708  1.000 51.190  ? 102 TRP EEE CA  1 
ATOM 8557  C C   . TRP E 1 85  ? 171.774 -31.057 41.650  1.000 43.880  ? 102 TRP EEE C   1 
ATOM 8558  O O   . TRP E 1 85  ? 170.722 -31.456 42.192  1.000 40.740  ? 102 TRP EEE O   1 
ATOM 8559  C CB  . TRP E 1 85  ? 171.765 -32.259 39.421  1.000 54.610  ? 102 TRP EEE CB  1 
ATOM 8560  C CG  . TRP E 1 85  ? 172.575 -32.810 38.288  1.000 55.150  ? 102 TRP EEE CG  1 
ATOM 8561  C CD1 . TRP E 1 85  ? 172.403 -34.010 37.662  1.000 53.740  ? 102 TRP EEE CD1 1 
ATOM 8562  C CD2 . TRP E 1 85  ? 173.659 -32.155 37.607  1.000 52.760  ? 102 TRP EEE CD2 1 
ATOM 8563  N NE1 . TRP E 1 85  ? 173.288 -34.135 36.623  1.000 50.030  ? 102 TRP EEE NE1 1 
ATOM 8564  C CE2 . TRP E 1 85  ? 174.089 -33.030 36.587  1.000 48.980  ? 102 TRP EEE CE2 1 
ATOM 8565  C CE3 . TRP E 1 85  ? 174.307 -30.921 37.762  1.000 54.140  ? 102 TRP EEE CE3 1 
ATOM 8566  C CZ2 . TRP E 1 85  ? 175.134 -32.717 35.732  1.000 49.430  ? 102 TRP EEE CZ2 1 
ATOM 8567  C CZ3 . TRP E 1 85  ? 175.335 -30.603 36.903  1.000 53.830  ? 102 TRP EEE CZ3 1 
ATOM 8568  C CH2 . TRP E 1 85  ? 175.745 -31.492 35.908  1.000 53.240  ? 102 TRP EEE CH2 1 
ATOM 8569  N N   . GLU E 1 86  ? 172.306 -29.849 41.822  1.000 42.130  ? 103 GLU EEE N   1 
ATOM 8570  C CA  . GLU E 1 86  ? 171.734 -28.740 42.632  1.000 41.230  ? 103 GLU EEE CA  1 
ATOM 8571  C C   . GLU E 1 86  ? 171.097 -27.722 41.677  1.000 41.410  ? 103 GLU EEE C   1 
ATOM 8572  O O   . GLU E 1 86  ? 171.828 -27.127 40.864  1.000 35.750  ? 103 GLU EEE O   1 
ATOM 8573  C CB  . GLU E 1 86  ? 172.835 -28.080 43.466  1.000 42.620  ? 103 GLU EEE CB  1 
ATOM 8574  C CG  . GLU E 1 86  ? 172.333 -27.206 44.602  1.000 43.280  ? 103 GLU EEE CG  1 
ATOM 8575  C CD  . GLU E 1 86  ? 173.395 -26.375 45.313  1.000 41.210  ? 103 GLU EEE CD  1 
ATOM 8576  O OE1 . GLU E 1 86  ? 174.501 -26.251 44.771  1.000 37.690  ? 103 GLU EEE OE1 1 
ATOM 8577  O OE2 . GLU E 1 86  ? 173.115 -25.842 46.413  1.000 41.650  ? 103 GLU EEE OE2 1 
ATOM 8578  N N   . ALA E 1 87  ? 169.775 -27.543 41.756  1.000 43.690  ? 104 ALA EEE N   1 
ATOM 8579  C CA  . ALA E 1 87  ? 169.024 -26.515 40.999  1.000 41.050  ? 104 ALA EEE CA  1 
ATOM 8580  C C   . ALA E 1 87  ? 169.297 -25.159 41.644  1.000 40.320  ? 104 ALA EEE C   1 
ATOM 8581  O O   . ALA E 1 87  ? 168.981 -24.993 42.819  1.000 38.500  ? 104 ALA EEE O   1 
ATOM 8582  C CB  . ALA E 1 87  ? 167.556 -26.844 40.983  1.000 40.890  ? 104 ALA EEE CB  1 
ATOM 8583  N N   . VAL E 1 88  ? 169.861 -24.224 40.885  1.000 41.110  ? 105 VAL EEE N   1 
ATOM 8584  C CA  . VAL E 1 88  ? 170.424 -22.960 41.435  1.000 43.130  ? 105 VAL EEE CA  1 
ATOM 8585  C C   . VAL E 1 88  ? 169.541 -21.765 41.055  1.000 43.320  ? 105 VAL EEE C   1 
ATOM 8586  O O   . VAL E 1 88  ? 169.251 -20.938 41.952  1.000 42.570  ? 105 VAL EEE O   1 
ATOM 8587  C CB  . VAL E 1 88  ? 171.874 -22.797 40.956  1.000 44.560  ? 105 VAL EEE CB  1 
ATOM 8588  C CG1 . VAL E 1 88  ? 172.493 -21.467 41.369  1.000 44.180  ? 105 VAL EEE CG1 1 
ATOM 8589  C CG2 . VAL E 1 88  ? 172.702 -23.955 41.462  1.000 46.620  ? 105 VAL EEE CG2 1 
ATOM 8590  N N   . THR E 1 89  ? 169.165 -21.655 39.783  1.000 39.370  ? 106 THR EEE N   1 
ATOM 8591  C CA  . THR E 1 89  ? 168.341 -20.522 39.300  1.000 41.220  ? 106 THR EEE CA  1 
ATOM 8592  C C   . THR E 1 89  ? 167.192 -21.033 38.436  1.000 41.350  ? 106 THR EEE C   1 
ATOM 8593  O O   . THR E 1 89  ? 167.325 -22.084 37.812  1.000 45.560  ? 106 THR EEE O   1 
ATOM 8594  C CB  . THR E 1 89  ? 169.165 -19.511 38.502  1.000 40.500  ? 106 THR EEE CB  1 
ATOM 8595  O OG1 . THR E 1 89  ? 169.205 -19.933 37.141  1.000 47.140  ? 106 THR EEE OG1 1 
ATOM 8596  C CG2 . THR E 1 89  ? 170.566 -19.336 39.032  1.000 40.520  ? 106 THR EEE CG2 1 
ATOM 8597  N N   . LEU E 1 90  ? 166.109 -20.272 38.408  1.000 41.810  ? 107 LEU EEE N   1 
ATOM 8598  C CA  . LEU E 1 90  ? 164.924 -20.526 37.566  1.000 40.540  ? 107 LEU EEE CA  1 
ATOM 8599  C C   . LEU E 1 90  ? 164.637 -19.248 36.786  1.000 41.460  ? 107 LEU EEE C   1 
ATOM 8600  O O   . LEU E 1 90  ? 164.817 -18.166 37.341  1.000 46.030  ? 107 LEU EEE O   1 
ATOM 8601  C CB  . LEU E 1 90  ? 163.734 -20.884 38.449  1.000 40.230  ? 107 LEU EEE CB  1 
ATOM 8602  C CG  . LEU E 1 90  ? 162.388 -20.847 37.742  1.000 45.900  ? 107 LEU EEE CG  1 
ATOM 8603  C CD1 . LEU E 1 90  ? 162.316 -21.959 36.708  1.000 49.250  ? 107 LEU EEE CD1 1 
ATOM 8604  C CD2 . LEU E 1 90  ? 161.251 -20.967 38.750  1.000 47.510  ? 107 LEU EEE CD2 1 
ATOM 8605  N N   . LYS E 1 91  ? 164.269 -19.396 35.520  1.000 40.760  ? 108 LYS EEE N   1 
ATOM 8606  C CA  . LYS E 1 91  ? 163.559 -18.375 34.726  1.000 37.610  ? 108 LYS EEE CA  1 
ATOM 8607  C C   . LYS E 1 91  ? 162.264 -19.034 34.294  1.000 36.960  ? 108 LYS EEE C   1 
ATOM 8608  O O   . LYS E 1 91  ? 162.325 -20.191 33.841  1.000 37.600  ? 108 LYS EEE O   1 
ATOM 8609  C CB  . LYS E 1 91  ? 164.360 -17.962 33.492  1.000 37.450  ? 108 LYS EEE CB  1 
ATOM 8610  C CG  . LYS E 1 91  ? 165.550 -17.055 33.752  1.000 38.630  ? 108 LYS EEE CG  1 
ATOM 8611  C CD  . LYS E 1 91  ? 166.291 -16.691 32.473  1.000 39.920  ? 108 LYS EEE CD  1 
ATOM 8612  C CE  . LYS E 1 91  ? 166.650 -15.216 32.358  1.000 41.500  ? 108 LYS EEE CE  1 
ATOM 8613  N NZ  . LYS E 1 91  ? 167.948 -14.995 31.662  1.000 43.280  ? 108 LYS EEE NZ  1 
ATOM 8614  N N   . THR E 1 92  ? 161.148 -18.348 34.467  1.000 36.860  ? 109 THR EEE N   1 
ATOM 8615  C CA  . THR E 1 92  ? 159.843 -18.864 34.009  1.000 35.760  ? 109 THR EEE CA  1 
ATOM 8616  C C   . THR E 1 92  ? 159.018 -17.698 33.491  1.000 35.280  ? 109 THR EEE C   1 
ATOM 8617  O O   . THR E 1 92  ? 159.228 -16.588 33.964  1.000 34.440  ? 109 THR EEE O   1 
ATOM 8618  C CB  . THR E 1 92  ? 159.170 -19.659 35.122  1.000 33.090  ? 109 THR EEE CB  1 
ATOM 8619  O OG1 . THR E 1 92  ? 157.956 -20.150 34.566  1.000 39.020  ? 109 THR EEE OG1 1 
ATOM 8620  C CG2 . THR E 1 92  ? 158.888 -18.849 36.363  1.000 31.210  ? 109 THR EEE CG2 1 
ATOM 8621  N N   . GLU E 1 93  ? 158.158 -17.950 32.512  1.000 37.430  ? 110 GLU EEE N   1 
ATOM 8622  C CA  . GLU E 1 93  ? 157.093 -16.985 32.135  1.000 41.470  ? 110 GLU EEE CA  1 
ATOM 8623  C C   . GLU E 1 93  ? 155.947 -17.761 31.495  1.000 36.220  ? 110 GLU EEE C   1 
ATOM 8624  O O   . GLU E 1 93  ? 156.165 -18.915 31.142  1.000 31.700  ? 110 GLU EEE O   1 
ATOM 8625  C CB  . GLU E 1 93  ? 157.653 -15.843 31.269  1.000 45.870  ? 110 GLU EEE CB  1 
ATOM 8626  C CG  . GLU E 1 93  ? 157.694 -16.109 29.769  1.000 45.110  ? 110 GLU EEE CG  1 
ATOM 8627  C CD  . GLU E 1 93  ? 158.515 -15.091 28.973  1.000 45.070  ? 110 GLU EEE CD  1 
ATOM 8628  O OE1 . GLU E 1 93  ? 159.486 -14.527 29.551  1.000 48.790  ? 110 GLU EEE OE1 1 
ATOM 8629  O OE2 . GLU E 1 93  ? 158.224 -14.858 27.765  1.000 45.230  ? 110 GLU EEE OE2 1 
ATOM 8630  N N   . VAL E 1 94  ? 154.777 -17.147 31.399  1.000 34.070  ? 111 VAL EEE N   1 
ATOM 8631  C CA  . VAL E 1 94  ? 153.620 -17.775 30.715  1.000 38.580  ? 111 VAL EEE CA  1 
ATOM 8632  C C   . VAL E 1 94  ? 153.794 -17.585 29.202  1.000 43.600  ? 111 VAL EEE C   1 
ATOM 8633  O O   . VAL E 1 94  ? 154.074 -16.450 28.742  1.000 44.130  ? 111 VAL EEE O   1 
ATOM 8634  C CB  . VAL E 1 94  ? 152.301 -17.193 31.236  1.000 37.930  ? 111 VAL EEE CB  1 
ATOM 8635  C CG1 . VAL E 1 94  ? 151.114 -17.701 30.437  1.000 39.300  ? 111 VAL EEE CG1 1 
ATOM 8636  C CG2 . VAL E 1 94  ? 152.126 -17.515 32.704  1.000 36.850  ? 111 VAL EEE CG2 1 
ATOM 8637  N N   . ILE E 1 95  ? 153.637 -18.662 28.439  1.000 42.830  ? 112 ILE EEE N   1 
ATOM 8638  C CA  . ILE E 1 95  ? 153.795 -18.622 26.959  1.000 42.340  ? 112 ILE EEE CA  1 
ATOM 8639  C C   . ILE E 1 95  ? 152.428 -18.450 26.291  1.000 40.030  ? 112 ILE EEE C   1 
ATOM 8640  O O   . ILE E 1 95  ? 151.532 -19.323 26.439  1.000 35.570  ? 112 ILE EEE O   1 
ATOM 8641  C CB  . ILE E 1 95  ? 154.511 -19.874 26.451  1.000 47.930  ? 112 ILE EEE CB  1 
ATOM 8642  C CG1 . ILE E 1 95  ? 155.804 -20.136 27.221  1.000 54.660  ? 112 ILE EEE CG1 1 
ATOM 8643  C CG2 . ILE E 1 95  ? 154.757 -19.759 24.961  1.000 50.030  ? 112 ILE EEE CG2 1 
ATOM 8644  C CD1 . ILE E 1 95  ? 156.349 -21.550 26.997  1.000 61.370  ? 112 ILE EEE CD1 1 
ATOM 8645  N N   . GLY E 1 96  ? 152.293 -17.359 25.545  1.000 40.150  ? 113 GLY EEE N   1 
ATOM 8646  C CA  . GLY E 1 96  ? 151.122 -17.114 24.685  1.000 37.270  ? 113 GLY EEE CA  1 
ATOM 8647  C C   . GLY E 1 96  ? 150.136 -16.181 25.359  1.000 34.020  ? 113 GLY EEE C   1 
ATOM 8648  O O   . GLY E 1 96  ? 148.927 -16.407 25.196  1.000 34.050  ? 113 GLY EEE O   1 
ATOM 8649  N N   . VAL E 1 97  ? 150.636 -15.168 26.074  1.000 29.200  ? 114 VAL EEE N   1 
ATOM 8650  C CA  . VAL E 1 97  ? 149.804 -14.204 26.842  1.000 26.730  ? 114 VAL EEE CA  1 
ATOM 8651  C C   . VAL E 1 97  ? 148.911 -13.437 25.863  1.000 25.310  ? 114 VAL EEE C   1 
ATOM 8652  O O   . VAL E 1 97  ? 147.745 -13.219 26.208  1.000 24.770  ? 114 VAL EEE O   1 
ATOM 8653  C CB  . VAL E 1 97  ? 150.661 -13.252 27.700  1.000 26.660  ? 114 VAL EEE CB  1 
ATOM 8654  C CG1 . VAL E 1 97  ? 151.491 -14.012 28.710  1.000 26.140  ? 114 VAL EEE CG1 1 
ATOM 8655  C CG2 . VAL E 1 97  ? 151.531 -12.313 26.875  1.000 26.340  ? 114 VAL EEE CG2 1 
ATOM 8656  N N   . THR E 1 98  ? 149.431 -13.061 24.696  1.000 24.540  ? 115 THR EEE N   1 
ATOM 8657  C CA  . THR E 1 98  ? 148.721 -12.192 23.714  1.000 23.520  ? 115 THR EEE CA  1 
ATOM 8658  C C   . THR E 1 98  ? 147.463 -12.895 23.202  1.000 21.170  ? 115 THR EEE C   1 
ATOM 8659  O O   . THR E 1 98  ? 146.551 -12.206 22.733  1.000 17.340  ? 115 THR EEE O   1 
ATOM 8660  C CB  . THR E 1 98  ? 149.602 -11.823 22.514  1.000 24.930  ? 115 THR EEE CB  1 
ATOM 8661  O OG1 . THR E 1 98  ? 149.999 -13.041 21.880  1.000 28.000  ? 115 THR EEE OG1 1 
ATOM 8662  C CG2 . THR E 1 98  ? 150.820 -11.010 22.900  1.000 25.510  ? 115 THR EEE CG2 1 
ATOM 8663  N N   . SER E 1 99  ? 147.428 -14.225 23.262  1.000 22.250  ? 116 SER EEE N   1 
ATOM 8664  C CA  . SER E 1 99  ? 146.303 -15.039 22.744  1.000 23.270  ? 116 SER EEE CA  1 
ATOM 8665  C C   . SER E 1 99  ? 145.028 -14.636 23.462  1.000 24.910  ? 116 SER EEE C   1 
ATOM 8666  O O   . SER E 1 99  ? 143.948 -14.967 22.937  1.000 24.630  ? 116 SER EEE O   1 
ATOM 8667  C CB  . SER E 1 99  ? 146.549 -16.489 22.932  1.000 24.220  ? 116 SER EEE CB  1 
ATOM 8668  O OG  . SER E 1 99  ? 146.491 -16.808 24.314  1.000 25.790  ? 116 SER EEE OG  1 
ATOM 8669  N N   . LEU E 1 100 ? 145.161 -13.993 24.632  1.000 26.000  ? 117 LEU EEE N   1 
ATOM 8670  C CA  . LEU E 1 100 ? 144.024 -13.603 25.509  1.000 24.050  ? 117 LEU EEE CA  1 
ATOM 8671  C C   . LEU E 1 100 ? 143.389 -12.314 24.989  1.000 23.890  ? 117 LEU EEE C   1 
ATOM 8672  O O   . LEU E 1 100 ? 142.326 -11.939 25.510  1.000 27.510  ? 117 LEU EEE O   1 
ATOM 8673  C CB  . LEU E 1 100 ? 144.509 -13.469 26.954  1.000 22.640  ? 117 LEU EEE CB  1 
ATOM 8674  C CG  . LEU E 1 100 ? 144.940 -14.792 27.579  1.000 21.810  ? 117 LEU EEE CG  1 
ATOM 8675  C CD1 . LEU E 1 100 ? 145.292 -14.637 29.042  1.000 21.160  ? 117 LEU EEE CD1 1 
ATOM 8676  C CD2 . LEU E 1 100 ? 143.847 -15.808 27.426  1.000 21.400  ? 117 LEU EEE CD2 1 
ATOM 8677  N N   . MET E 1 101 ? 143.986 -11.691 23.974  1.000 21.680  ? 118 MET EEE N   1 
ATOM 8678  C CA  . MET E 1 101 ? 143.391 -10.531 23.274  1.000 23.750  ? 118 MET EEE CA  1 
ATOM 8679  C C   . MET E 1 101 ? 142.417 -11.003 22.185  1.000 25.920  ? 118 MET EEE C   1 
ATOM 8680  O O   . MET E 1 101 ? 141.874 -10.126 21.493  1.000 28.190  ? 118 MET EEE O   1 
ATOM 8681  C CB  . MET E 1 101 ? 144.471 -9.651  22.644  1.000 24.250  ? 118 MET EEE CB  1 
ATOM 8682  C CG  . MET E 1 101 ? 145.534 -9.250  23.613  1.000 24.650  ? 118 MET EEE CG  1 
ATOM 8683  S SD  . MET E 1 101 ? 146.748 -8.161  22.878  1.000 26.790  ? 118 MET EEE SD  1 
ATOM 8684  C CE  . MET E 1 101 ? 145.838 -6.630  23.027  1.000 29.480  ? 118 MET EEE CE  1 
ATOM 8685  N N   . ASN E 1 102 ? 142.211 -12.303 21.972  1.000 28.360  ? 119 ASN EEE N   1 
ATOM 8686  C CA  . ASN E 1 102 ? 141.251 -12.778 20.927  1.000 30.800  ? 119 ASN EEE CA  1 
ATOM 8687  C C   . ASN E 1 102 ? 139.840 -12.609 21.493  1.000 30.820  ? 119 ASN EEE C   1 
ATOM 8688  O O   . ASN E 1 102 ? 139.282 -13.583 22.054  1.000 32.740  ? 119 ASN EEE O   1 
ATOM 8689  C CB  . ASN E 1 102 ? 141.436 -14.216 20.436  1.000 32.130  ? 119 ASN EEE CB  1 
ATOM 8690  C CG  . ASN E 1 102 ? 140.421 -14.584 19.356  1.000 30.710  ? 119 ASN EEE CG  1 
ATOM 8691  O OD1 . ASN E 1 102 ? 139.379 -13.949 19.225  1.000 26.060  ? 119 ASN EEE OD1 1 
ATOM 8692  N ND2 . ASN E 1 102 ? 140.701 -15.604 18.555  1.000 31.980  ? 119 ASN EEE ND2 1 
ATOM 8693  N N   . VAL E 1 103 ? 139.258 -11.446 21.233  1.000 27.560  ? 120 VAL EEE N   1 
ATOM 8694  C CA  . VAL E 1 103 ? 137.959 -11.005 21.786  1.000 27.160  ? 120 VAL EEE CA  1 
ATOM 8695  C C   . VAL E 1 103 ? 136.856 -11.115 20.711  1.000 26.550  ? 120 VAL EEE C   1 
ATOM 8696  O O   . VAL E 1 103 ? 135.805 -10.522 20.885  1.000 27.380  ? 120 VAL EEE O   1 
ATOM 8697  C CB  . VAL E 1 103 ? 138.171 -9.593  22.356  1.000 28.510  ? 120 VAL EEE CB  1 
ATOM 8698  C CG1 . VAL E 1 103 ? 138.906 -8.654  21.434  1.000 27.570  ? 120 VAL EEE CG1 1 
ATOM 8699  C CG2 . VAL E 1 103 ? 136.908 -8.919  22.782  1.000 34.550  ? 120 VAL EEE CG2 1 
ATOM 8700  N N   . HIS E 1 104 ? 137.050 -11.925 19.668  1.000 25.530  ? 121 HIS EEE N   1 
ATOM 8701  C CA  . HIS E 1 104 ? 136.153 -11.994 18.480  1.000 25.620  ? 121 HIS EEE CA  1 
ATOM 8702  C C   . HIS E 1 104 ? 135.665 -13.417 18.153  1.000 25.120  ? 121 HIS EEE C   1 
ATOM 8703  O O   . HIS E 1 104 ? 134.918 -13.562 17.149  1.000 25.140  ? 121 HIS EEE O   1 
ATOM 8704  C CB  . HIS E 1 104 ? 136.871 -11.388 17.255  1.000 26.020  ? 121 HIS EEE CB  1 
ATOM 8705  C CG  . HIS E 1 104 ? 138.286 -11.825 17.089  1.000 24.780  ? 121 HIS EEE CG  1 
ATOM 8706  N ND1 . HIS E 1 104 ? 138.635 -12.929 16.359  1.000 24.500  ? 121 HIS EEE ND1 1 
ATOM 8707  C CD2 . HIS E 1 104 ? 139.443 -11.298 17.535  1.000 24.570  ? 121 HIS EEE CD2 1 
ATOM 8708  C CE1 . HIS E 1 104 ? 139.944 -13.071 16.367  1.000 24.310  ? 121 HIS EEE CE1 1 
ATOM 8709  N NE2 . HIS E 1 104 ? 140.462 -12.082 17.075  1.000 24.080  ? 121 HIS EEE NE2 1 
ATOM 8710  N N   . SER E 1 105 ? 136.060 -14.433 18.920  1.000 24.410  ? 122 SER EEE N   1 
ATOM 8711  C CA  . SER E 1 105 ? 135.849 -15.870 18.580  1.000 24.890  ? 122 SER EEE CA  1 
ATOM 8712  C C   . SER E 1 105 ? 134.609 -16.401 19.306  1.000 24.090  ? 122 SER EEE C   1 
ATOM 8713  O O   . SER E 1 105 ? 134.750 -17.140 20.265  1.000 25.520  ? 122 SER EEE O   1 
ATOM 8714  C CB  . SER E 1 105 ? 137.091 -16.696 18.887  1.000 26.350  ? 122 SER EEE CB  1 
ATOM 8715  O OG  . SER E 1 105 ? 136.895 -18.092 18.631  1.000 25.740  ? 122 SER EEE OG  1 
ATOM 8716  N N   . ASN E 1 106 ? 133.435 -16.003 18.852  1.000 25.170  ? 123 ASN EEE N   1 
ATOM 8717  C CA  . ASN E 1 106 ? 132.123 -16.397 19.416  1.000 27.180  ? 123 ASN EEE CA  1 
ATOM 8718  C C   . ASN E 1 106 ? 132.087 -16.104 20.919  1.000 28.370  ? 123 ASN EEE C   1 
ATOM 8719  O O   . ASN E 1 106 ? 131.569 -16.931 21.649  1.000 27.860  ? 123 ASN EEE O   1 
ATOM 8720  C CB  . ASN E 1 106 ? 131.857 -17.871 19.161  1.000 28.710  ? 123 ASN EEE CB  1 
ATOM 8721  C CG  . ASN E 1 106 ? 130.375 -18.165 19.094  1.000 32.110  ? 123 ASN EEE CG  1 
ATOM 8722  O OD1 . ASN E 1 106 ? 129.667 -17.581 18.278  1.000 32.410  ? 123 ASN EEE OD1 1 
ATOM 8723  N ND2 . ASN E 1 106 ? 129.897 -19.070 19.939  1.000 38.240  ? 123 ASN EEE ND2 1 
ATOM 8724  N N   . GLY E 1 107 ? 132.615 -14.958 21.347  1.000 31.700  ? 124 GLY EEE N   1 
ATOM 8725  C CA  . GLY E 1 107 ? 132.565 -14.517 22.753  1.000 32.280  ? 124 GLY EEE CA  1 
ATOM 8726  C C   . GLY E 1 107 ? 131.252 -13.916 23.203  1.000 30.200  ? 124 GLY EEE C   1 
ATOM 8727  O O   . GLY E 1 107 ? 130.298 -13.931 22.399  1.000 25.260  ? 124 GLY EEE O   1 
ATOM 8728  N N   . GLN E 1 108 ? 131.209 -13.380 24.431  1.000 30.370  ? 125 GLN EEE N   1 
ATOM 8729  C CA  . GLN E 1 108 ? 130.082 -12.485 24.850  1.000 30.540  ? 125 GLN EEE CA  1 
ATOM 8730  C C   . GLN E 1 108 ? 130.309 -10.987 24.651  1.000 31.110  ? 125 GLN EEE C   1 
ATOM 8731  O O   . GLN E 1 108 ? 131.203 -10.400 25.327  1.000 31.550  ? 125 GLN EEE O   1 
ATOM 8732  C CB  . GLN E 1 108 ? 129.690 -12.810 26.302  1.000 28.930  ? 125 GLN EEE CB  1 
ATOM 8733  C CG  . GLN E 1 108 ? 128.427 -12.148 26.831  1.000 28.260  ? 125 GLN EEE CG  1 
ATOM 8734  C CD  . GLN E 1 108 ? 128.060 -12.673 28.193  1.000 27.020  ? 125 GLN EEE CD  1 
ATOM 8735  O OE1 . GLN E 1 108 ? 128.686 -13.595 28.709  1.000 23.240  ? 125 GLN EEE OE1 1 
ATOM 8736  N NE2 . GLN E 1 108 ? 127.025 -12.079 28.784  1.000 29.620  ? 125 GLN EEE NE2 1 
ATOM 8737  N N   . ALA E 1 109 ? 129.580 -10.399 23.705  1.000 29.220  ? 126 ALA EEE N   1 
ATOM 8738  C CA  . ALA E 1 109 ? 129.505 -8.940  23.556  1.000 31.570  ? 126 ALA EEE CA  1 
ATOM 8739  C C   . ALA E 1 109 ? 129.233 -8.420  24.960  1.000 31.720  ? 126 ALA EEE C   1 
ATOM 8740  O O   . ALA E 1 109 ? 128.215 -8.808  25.526  1.000 30.200  ? 126 ALA EEE O   1 
ATOM 8741  C CB  . ALA E 1 109 ? 128.465 -8.432  22.605  1.000 36.790  ? 126 ALA EEE CB  1 
ATOM 8742  N N   . THR E 1 110 ? 130.126 -7.575  25.478  1.000 33.120  ? 127 THR EEE N   1 
ATOM 8743  C CA  . THR E 1 110 ? 129.977 -6.882  26.779  1.000 32.140  ? 127 THR EEE CA  1 
ATOM 8744  C C   . THR E 1 110 ? 128.742 -5.974  26.728  1.000 30.100  ? 127 THR EEE C   1 
ATOM 8745  O O   . THR E 1 110 ? 128.186 -5.708  27.788  1.000 32.790  ? 127 THR EEE O   1 
ATOM 8746  C CB  . THR E 1 110 ? 131.251 -6.095  27.115  1.000 33.240  ? 127 THR EEE CB  1 
ATOM 8747  O OG1 . THR E 1 110 ? 131.706 -5.376  25.977  1.000 35.640  ? 127 THR EEE OG1 1 
ATOM 8748  C CG2 . THR E 1 110 ? 132.423 -6.945  27.513  1.000 33.880  ? 127 THR EEE CG2 1 
ATOM 8749  N N   . HIS E 1 111 ? 128.314 -5.523  25.546  1.000 28.140  ? 128 HIS EEE N   1 
ATOM 8750  C CA  . HIS E 1 111 ? 127.166 -4.585  25.370  1.000 28.660  ? 128 HIS EEE CA  1 
ATOM 8751  C C   . HIS E 1 111 ? 126.820 -4.458  23.885  1.000 28.150  ? 128 HIS EEE C   1 
ATOM 8752  O O   . HIS E 1 111 ? 127.609 -4.987  23.081  1.000 28.370  ? 128 HIS EEE O   1 
ATOM 8753  C CB  . HIS E 1 111 ? 127.511 -3.208  25.934  1.000 25.770  ? 128 HIS EEE CB  1 
ATOM 8754  C CG  . HIS E 1 111 ? 128.726 -2.645  25.298  1.000 24.030  ? 128 HIS EEE CG  1 
ATOM 8755  N ND1 . HIS E 1 111 ? 129.979 -2.865  25.800  1.000 21.850  ? 128 HIS EEE ND1 1 
ATOM 8756  C CD2 . HIS E 1 111 ? 128.884 -1.901  24.182  1.000 24.620  ? 128 HIS EEE CD2 1 
ATOM 8757  C CE1 . HIS E 1 111 ? 130.868 -2.262  25.036  1.000 22.940  ? 128 HIS EEE CE1 1 
ATOM 8758  N NE2 . HIS E 1 111 ? 130.231 -1.676  24.028  1.000 23.250  ? 128 HIS EEE NE2 1 
ATOM 8759  N N   . ASP E 1 112 ? 125.735 -3.768  23.513  1.000 25.940  ? 129 ASP EEE N   1 
ATOM 8760  C CA  . ASP E 1 112 ? 125.371 -3.674  22.077  1.000 28.410  ? 129 ASP EEE CA  1 
ATOM 8761  C C   . ASP E 1 112 ? 126.585 -3.173  21.287  1.000 29.150  ? 129 ASP EEE C   1 
ATOM 8762  O O   . ASP E 1 112 ? 127.078 -2.045  21.586  1.000 30.450  ? 129 ASP EEE O   1 
ATOM 8763  C CB  . ASP E 1 112 ? 124.176 -2.766  21.832  1.000 32.300  ? 129 ASP EEE CB  1 
ATOM 8764  C CG  . ASP E 1 112 ? 122.857 -3.394  22.196  1.000 36.980  ? 129 ASP EEE CG  1 
ATOM 8765  O OD1 . ASP E 1 112 ? 122.809 -4.616  22.272  1.000 42.110  ? 129 ASP EEE OD1 1 
ATOM 8766  O OD2 . ASP E 1 112 ? 121.891 -2.641  22.401  1.000 44.760  ? 129 ASP EEE OD2 1 
ATOM 8767  N N   . ASN E 1 113 ? 127.043 -3.981  20.318  1.000 29.140  ? 130 ASN EEE N   1 
ATOM 8768  C CA  . ASN E 1 113 ? 128.156 -3.682  19.374  1.000 28.050  ? 130 ASN EEE CA  1 
ATOM 8769  C C   . ASN E 1 113 ? 129.482 -3.734  20.138  1.000 26.780  ? 130 ASN EEE C   1 
ATOM 8770  O O   . ASN E 1 113 ? 130.535 -3.314  19.610  1.000 25.690  ? 130 ASN EEE O   1 
ATOM 8771  C CB  . ASN E 1 113 ? 127.982 -2.338  18.662  1.000 28.800  ? 130 ASN EEE CB  1 
ATOM 8772  C CG  . ASN E 1 113 ? 126.662 -2.193  17.939  1.000 29.750  ? 130 ASN EEE CG  1 
ATOM 8773  O OD1 . ASN E 1 113 ? 126.216 -3.112  17.259  1.000 27.200  ? 130 ASN EEE OD1 1 
ATOM 8774  N ND2 . ASN E 1 113 ? 126.054 -1.017  18.050  1.000 36.160  ? 130 ASN EEE ND2 1 
ATOM 8775  N N   . GLY E 1 114 ? 129.453 -4.255  21.353  1.000 26.510  ? 131 GLY EEE N   1 
ATOM 8776  C CA  . GLY E 1 114 ? 130.691 -4.487  22.114  1.000 25.270  ? 131 GLY EEE CA  1 
ATOM 8777  C C   . GLY E 1 114 ? 131.511 -5.601  21.501  1.000 22.490  ? 131 GLY EEE C   1 
ATOM 8778  O O   . GLY E 1 114 ? 130.941 -6.506  20.808  1.000 19.940  ? 131 GLY EEE O   1 
ATOM 8779  N N   . ALA E 1 115 ? 132.815 -5.536  21.732  1.000 20.680  ? 132 ALA EEE N   1 
ATOM 8780  C CA  . ALA E 1 115 ? 133.722 -6.660  21.446  1.000 21.820  ? 132 ALA EEE CA  1 
ATOM 8781  C C   . ALA E 1 115 ? 133.323 -7.770  22.405  1.000 21.900  ? 132 ALA EEE C   1 
ATOM 8782  O O   . ALA E 1 115 ? 132.486 -7.505  23.278  1.000 25.550  ? 132 ALA EEE O   1 
ATOM 8783  C CB  . ALA E 1 115 ? 135.154 -6.223  21.630  1.000 22.950  ? 132 ALA EEE CB  1 
ATOM 8784  N N   . GLY E 1 116 ? 133.901 -8.948  22.294  1.000 20.490  ? 133 GLY EEE N   1 
ATOM 8785  C CA  . GLY E 1 116 ? 133.643 -9.987  23.293  1.000 21.280  ? 133 GLY EEE CA  1 
ATOM 8786  C C   . GLY E 1 116 ? 134.249 -9.650  24.633  1.000 21.090  ? 133 GLY EEE C   1 
ATOM 8787  O O   . GLY E 1 116 ? 135.287 -9.002  24.670  1.000 20.910  ? 133 GLY EEE O   1 
ATOM 8788  N N   . LYS E 1 117 ? 133.636 -10.129 25.701  1.000 23.590  ? 134 LYS EEE N   1 
ATOM 8789  C CA  . LYS E 1 117 ? 134.254 -10.054 27.051  1.000 25.780  ? 134 LYS EEE CA  1 
ATOM 8790  C C   . LYS E 1 117 ? 135.532 -10.864 26.987  1.000 24.500  ? 134 LYS EEE C   1 
ATOM 8791  O O   . LYS E 1 117 ? 135.473 -12.034 26.637  1.000 28.120  ? 134 LYS EEE O   1 
ATOM 8792  C CB  . LYS E 1 117 ? 133.314 -10.604 28.125  1.000 29.640  ? 134 LYS EEE CB  1 
ATOM 8793  C CG  . LYS E 1 117 ? 133.971 -10.778 29.474  1.000 33.810  ? 134 LYS EEE CG  1 
ATOM 8794  C CD  . LYS E 1 117 ? 133.098 -11.392 30.524  1.000 36.570  ? 134 LYS EEE CD  1 
ATOM 8795  C CE  . LYS E 1 117 ? 132.107 -10.428 31.119  1.000 38.170  ? 134 LYS EEE CE  1 
ATOM 8796  N NZ  . LYS E 1 117 ? 131.170 -11.233 31.933  1.000 44.770  ? 134 LYS EEE NZ  1 
ATOM 8797  N N   . PRO E 1 118 ? 136.697 -10.297 27.339  1.000 22.970  ? 135 PRO EEE N   1 
ATOM 8798  C CA  . PRO E 1 118 ? 137.967 -11.000 27.224  1.000 24.040  ? 135 PRO EEE CA  1 
ATOM 8799  C C   . PRO E 1 118 ? 138.094 -12.054 28.318  1.000 24.380  ? 135 PRO EEE C   1 
ATOM 8800  O O   . PRO E 1 118 ? 137.387 -11.926 29.288  1.000 23.310  ? 135 PRO EEE O   1 
ATOM 8801  C CB  . PRO E 1 118 ? 139.027 -9.924  27.480  1.000 23.760  ? 135 PRO EEE CB  1 
ATOM 8802  C CG  . PRO E 1 118 ? 138.327 -8.955  28.370  1.000 23.280  ? 135 PRO EEE CG  1 
ATOM 8803  C CD  . PRO E 1 118 ? 136.862 -8.987  27.953  1.000 23.470  ? 135 PRO EEE CD  1 
ATOM 8804  N N   . VAL E 1 119 ? 138.990 -13.027 28.143  1.000 26.140  ? 136 VAL EEE N   1 
ATOM 8805  C CA  . VAL E 1 119 ? 139.321 -13.984 29.238  1.000 27.650  ? 136 VAL EEE CA  1 
ATOM 8806  C C   . VAL E 1 119 ? 139.647 -13.140 30.465  1.000 24.270  ? 136 VAL EEE C   1 
ATOM 8807  O O   . VAL E 1 119 ? 140.457 -12.211 30.308  1.000 22.190  ? 136 VAL EEE O   1 
ATOM 8808  C CB  . VAL E 1 119 ? 140.492 -14.934 28.896  1.000 29.940  ? 136 VAL EEE CB  1 
ATOM 8809  C CG1 . VAL E 1 119 ? 140.974 -15.692 30.126  1.000 29.780  ? 136 VAL EEE CG1 1 
ATOM 8810  C CG2 . VAL E 1 119 ? 140.140 -15.920 27.794  1.000 30.930  ? 136 VAL EEE CG2 1 
ATOM 8811  N N   . GLN E 1 120 ? 139.026 -13.467 31.595  1.000 25.100  ? 137 GLN EEE N   1 
ATOM 8812  C CA  . GLN E 1 120 ? 139.222 -12.795 32.906  1.000 29.160  ? 137 GLN EEE CA  1 
ATOM 8813  C C   . GLN E 1 120 ? 138.657 -13.667 34.026  1.000 29.960  ? 137 GLN EEE C   1 
ATOM 8814  O O   . GLN E 1 120 ? 137.991 -14.663 33.723  1.000 33.980  ? 137 GLN EEE O   1 
ATOM 8815  C CB  . GLN E 1 120 ? 138.503 -11.440 32.943  1.000 30.000  ? 137 GLN EEE CB  1 
ATOM 8816  C CG  . GLN E 1 120 ? 136.976 -11.534 32.862  1.000 30.190  ? 137 GLN EEE CG  1 
ATOM 8817  C CD  . GLN E 1 120 ? 136.365 -10.190 32.570  1.000 30.070  ? 137 GLN EEE CD  1 
ATOM 8818  O OE1 . GLN E 1 120 ? 135.944 -9.446  33.445  1.000 32.940  ? 137 GLN EEE OE1 1 
ATOM 8819  N NE2 . GLN E 1 120 ? 136.337 -9.850  31.303  1.000 32.220  ? 137 GLN EEE NE2 1 
ATOM 8820  N N   . GLY E 1 121 ? 138.894 -13.276 35.271  1.000 29.500  ? 138 GLY EEE N   1 
ATOM 8821  C CA  . GLY E 1 121 ? 138.276 -13.915 36.443  1.000 30.160  ? 138 GLY EEE CA  1 
ATOM 8822  C C   . GLY E 1 121 ? 139.250 -14.808 37.188  1.000 30.440  ? 138 GLY EEE C   1 
ATOM 8823  O O   . GLY E 1 121 ? 140.458 -14.725 36.916  1.000 34.270  ? 138 GLY EEE O   1 
ATOM 8824  N N   . THR E 1 122 ? 138.728 -15.633 38.099  1.000 28.400  ? 139 THR EEE N   1 
ATOM 8825  C CA  . THR E 1 122 ? 139.484 -16.457 39.072  1.000 26.010  ? 139 THR EEE CA  1 
ATOM 8826  C C   . THR E 1 122 ? 140.689 -17.081 38.379  1.000 24.600  ? 139 THR EEE C   1 
ATOM 8827  O O   . THR E 1 122 ? 140.515 -17.657 37.304  1.000 25.690  ? 139 THR EEE O   1 
ATOM 8828  C CB  . THR E 1 122 ? 138.564 -17.501 39.703  1.000 25.880  ? 139 THR EEE CB  1 
ATOM 8829  O OG1 . THR E 1 122 ? 137.403 -16.831 40.230  1.000 25.170  ? 139 THR EEE OG1 1 
ATOM 8830  C CG2 . THR E 1 122 ? 139.238 -18.292 40.792  1.000 25.680  ? 139 THR EEE CG2 1 
ATOM 8831  N N   . SER E 1 123 ? 141.866 -16.925 38.969  1.000 23.430  ? 140 SER EEE N   1 
ATOM 8832  C CA  . SER E 1 123 ? 143.166 -17.298 38.366  1.000 24.820  ? 140 SER EEE CA  1 
ATOM 8833  C C   . SER E 1 123 ? 144.006 -17.982 39.434  1.000 24.460  ? 140 SER EEE C   1 
ATOM 8834  O O   . SER E 1 123 ? 144.014 -17.456 40.572  1.000 30.170  ? 140 SER EEE O   1 
ATOM 8835  C CB  . SER E 1 123 ? 143.891 -16.074 37.861  1.000 28.180  ? 140 SER EEE CB  1 
ATOM 8836  O OG  . SER E 1 123 ? 144.599 -15.430 38.930  1.000 31.040  ? 140 SER EEE OG  1 
ATOM 8837  N N   . PHE E 1 124 ? 144.712 -19.056 39.089  1.000 22.060  ? 141 PHE EEE N   1 
ATOM 8838  C CA  . PHE E 1 124 ? 145.800 -19.627 39.924  1.000 21.170  ? 141 PHE EEE CA  1 
ATOM 8839  C C   . PHE E 1 124 ? 147.055 -19.757 39.057  1.000 20.990  ? 141 PHE EEE C   1 
ATOM 8840  O O   . PHE E 1 124 ? 147.049 -20.522 38.086  1.000 23.860  ? 141 PHE EEE O   1 
ATOM 8841  C CB  . PHE E 1 124 ? 145.327 -20.933 40.576  1.000 21.680  ? 141 PHE EEE CB  1 
ATOM 8842  C CG  . PHE E 1 124 ? 146.273 -21.474 41.616  1.000 22.080  ? 141 PHE EEE CG  1 
ATOM 8843  C CD1 . PHE E 1 124 ? 146.704 -20.682 42.664  1.000 22.010  ? 141 PHE EEE CD1 1 
ATOM 8844  C CD2 . PHE E 1 124 ? 146.736 -22.775 41.544  1.000 23.030  ? 141 PHE EEE CD2 1 
ATOM 8845  C CE1 . PHE E 1 124 ? 147.569 -21.182 43.623  1.000 23.040  ? 141 PHE EEE CE1 1 
ATOM 8846  C CE2 . PHE E 1 124 ? 147.633 -23.264 42.479  1.000 24.800  ? 141 PHE EEE CE2 1 
ATOM 8847  C CZ  . PHE E 1 124 ? 148.067 -22.459 43.508  1.000 24.540  ? 141 PHE EEE CZ  1 
ATOM 8848  N N   . HIS E 1 125 ? 148.076 -18.960 39.337  1.000 21.610  ? 142 HIS EEE N   1 
ATOM 8849  C CA  . HIS E 1 125 ? 149.416 -19.066 38.712  1.000 22.450  ? 142 HIS EEE CA  1 
ATOM 8850  C C   . HIS E 1 125 ? 150.357 -19.583 39.790  1.000 23.260  ? 142 HIS EEE C   1 
ATOM 8851  O O   . HIS E 1 125 ? 150.434 -18.943 40.855  1.000 22.620  ? 142 HIS EEE O   1 
ATOM 8852  C CB  . HIS E 1 125 ? 149.857 -17.747 38.066  1.000 23.890  ? 142 HIS EEE CB  1 
ATOM 8853  C CG  . HIS E 1 125 ? 148.954 -17.338 36.963  1.000 24.770  ? 142 HIS EEE CG  1 
ATOM 8854  N ND1 . HIS E 1 125 ? 149.013 -17.925 35.728  1.000 25.990  ? 142 HIS EEE ND1 1 
ATOM 8855  C CD2 . HIS E 1 125 ? 147.922 -16.466 36.944  1.000 27.670  ? 142 HIS EEE CD2 1 
ATOM 8856  C CE1 . HIS E 1 125 ? 148.061 -17.419 34.965  1.000 30.490  ? 142 HIS EEE CE1 1 
ATOM 8857  N NE2 . HIS E 1 125 ? 147.372 -16.494 35.688  1.000 30.460  ? 142 HIS EEE NE2 1 
ATOM 8858  N N   . PHE E 1 126 ? 150.957 -20.740 39.518  1.000 26.220  ? 143 PHE EEE N   1 
ATOM 8859  C CA  . PHE E 1 126 ? 151.758 -21.554 40.453  1.000 28.490  ? 143 PHE EEE CA  1 
ATOM 8860  C C   . PHE E 1 126 ? 152.875 -22.260 39.664  1.000 26.880  ? 143 PHE EEE C   1 
ATOM 8861  O O   . PHE E 1 126 ? 152.608 -22.708 38.534  1.000 26.560  ? 143 PHE EEE O   1 
ATOM 8862  C CB  . PHE E 1 126 ? 150.887 -22.591 41.166  1.000 29.870  ? 143 PHE EEE CB  1 
ATOM 8863  C CG  . PHE E 1 126 ? 151.705 -23.639 41.870  1.000 31.990  ? 143 PHE EEE CG  1 
ATOM 8864  C CD1 . PHE E 1 126 ? 152.301 -23.370 43.090  1.000 32.200  ? 143 PHE EEE CD1 1 
ATOM 8865  C CD2 . PHE E 1 126 ? 151.955 -24.862 41.271  1.000 31.600  ? 143 PHE EEE CD2 1 
ATOM 8866  C CE1 . PHE E 1 126 ? 153.088 -24.323 43.710  1.000 32.810  ? 143 PHE EEE CE1 1 
ATOM 8867  C CE2 . PHE E 1 126 ? 152.747 -25.809 41.892  1.000 29.320  ? 143 PHE EEE CE2 1 
ATOM 8868  C CZ  . PHE E 1 126 ? 153.303 -25.540 43.111  1.000 30.960  ? 143 PHE EEE CZ  1 
ATOM 8869  N N   . PHE E 1 127 ? 154.049 -22.385 40.251  1.000 25.600  ? 144 PHE EEE N   1 
ATOM 8870  C CA  . PHE E 1 127 ? 155.188 -23.142 39.657  1.000 26.170  ? 144 PHE EEE CA  1 
ATOM 8871  C C   . PHE E 1 127 ? 156.189 -23.500 40.738  1.000 29.700  ? 144 PHE EEE C   1 
ATOM 8872  O O   . PHE E 1 127 ? 156.442 -22.666 41.654  1.000 34.730  ? 144 PHE EEE O   1 
ATOM 8873  C CB  . PHE E 1 127 ? 155.851 -22.326 38.552  1.000 24.020  ? 144 PHE EEE CB  1 
ATOM 8874  C CG  . PHE E 1 127 ? 156.432 -21.030 39.039  1.000 22.020  ? 144 PHE EEE CG  1 
ATOM 8875  C CD1 . PHE E 1 127 ? 157.697 -21.000 39.597  1.000 21.770  ? 144 PHE EEE CD1 1 
ATOM 8876  C CD2 . PHE E 1 127 ? 155.707 -19.854 38.954  1.000 21.110  ? 144 PHE EEE CD2 1 
ATOM 8877  C CE1 . PHE E 1 127 ? 158.241 -19.804 40.037  1.000 21.530  ? 144 PHE EEE CE1 1 
ATOM 8878  C CE2 . PHE E 1 127 ? 156.239 -18.667 39.425  1.000 20.450  ? 144 PHE EEE CE2 1 
ATOM 8879  C CZ  . PHE E 1 127 ? 157.503 -18.645 39.958  1.000 20.590  ? 144 PHE EEE CZ  1 
ATOM 8880  N N   . SER E 1 128 ? 156.749 -24.706 40.620  1.000 30.790  ? 145 SER EEE N   1 
ATOM 8881  C CA  . SER E 1 128 ? 157.673 -25.316 41.607  1.000 31.740  ? 145 SER EEE CA  1 
ATOM 8882  C C   . SER E 1 128 ? 158.881 -25.903 40.868  1.000 31.460  ? 145 SER EEE C   1 
ATOM 8883  O O   . SER E 1 128 ? 158.722 -26.351 39.717  1.000 34.460  ? 145 SER EEE O   1 
ATOM 8884  C CB  . SER E 1 128 ? 156.965 -26.362 42.417  1.000 32.420  ? 145 SER EEE CB  1 
ATOM 8885  O OG  . SER E 1 128 ? 157.064 -27.647 41.784  1.000 34.350  ? 145 SER EEE OG  1 
ATOM 8886  N N   . VAL E 1 129 ? 160.047 -25.898 41.516  1.000 29.170  ? 146 VAL EEE N   1 
ATOM 8887  C CA  . VAL E 1 129 ? 161.268 -26.620 41.067  1.000 30.080  ? 146 VAL EEE CA  1 
ATOM 8888  C C   . VAL E 1 129 ? 161.754 -27.498 42.228  1.000 31.580  ? 146 VAL EEE C   1 
ATOM 8889  O O   . VAL E 1 129 ? 162.015 -26.965 43.318  1.000 35.690  ? 146 VAL EEE O   1 
ATOM 8890  C CB  . VAL E 1 129 ? 162.342 -25.638 40.563  1.000 29.110  ? 146 VAL EEE CB  1 
ATOM 8891  C CG1 . VAL E 1 129 ? 163.634 -26.354 40.173  1.000 29.510  ? 146 VAL EEE CG1 1 
ATOM 8892  C CG2 . VAL E 1 129 ? 161.824 -24.816 39.406  1.000 28.020  ? 146 VAL EEE CG2 1 
ATOM 8893  N N   . GLY E 1 130 ? 161.844 -28.804 42.000  1.000 30.710  ? 147 GLY EEE N   1 
ATOM 8894  C CA  . GLY E 1 130 ? 162.103 -29.795 43.054  1.000 32.630  ? 147 GLY EEE CA  1 
ATOM 8895  C C   . GLY E 1 130 ? 163.076 -30.872 42.615  1.000 32.300  ? 147 GLY EEE C   1 
ATOM 8896  O O   . GLY E 1 130 ? 163.075 -31.211 41.413  1.000 31.660  ? 147 GLY EEE O   1 
ATOM 8897  N N   . GLY E 1 131 ? 163.854 -31.385 43.581  1.000 33.940  ? 148 GLY EEE N   1 
ATOM 8898  C CA  . GLY E 1 131 ? 164.693 -32.598 43.471  1.000 36.470  ? 148 GLY EEE CA  1 
ATOM 8899  C C   . GLY E 1 131 ? 163.865 -33.869 43.602  1.000 39.330  ? 148 GLY EEE C   1 
ATOM 8900  O O   . GLY E 1 131 ? 164.439 -34.962 43.493  1.000 42.460  ? 148 GLY EEE O   1 
ATOM 8901  N N   . GLU E 1 132 ? 162.554 -33.731 43.820  1.000 41.350  ? 149 GLU EEE N   1 
ATOM 8902  C CA  . GLU E 1 132 ? 161.577 -34.841 43.923  1.000 41.450  ? 149 GLU EEE CA  1 
ATOM 8903  C C   . GLU E 1 132 ? 160.191 -34.277 43.659  1.000 40.430  ? 149 GLU EEE C   1 
ATOM 8904  O O   . GLU E 1 132 ? 160.068 -33.046 43.521  1.000 47.350  ? 149 GLU EEE O   1 
ATOM 8905  C CB  . GLU E 1 132 ? 161.630 -35.462 45.316  1.000 40.940  ? 149 GLU EEE CB  1 
ATOM 8906  C CG  . GLU E 1 132 ? 162.156 -34.528 46.382  1.000 41.050  ? 149 GLU EEE CG  1 
ATOM 8907  C CD  . GLU E 1 132 ? 162.040 -35.086 47.787  1.000 45.090  ? 149 GLU EEE CD  1 
ATOM 8908  O OE1 . GLU E 1 132 ? 160.948 -35.597 48.149  1.000 47.880  ? 149 GLU EEE OE1 1 
ATOM 8909  O OE2 . GLU E 1 132 ? 163.052 -35.030 48.518  1.000 47.460  ? 149 GLU EEE OE2 1 
ATOM 8910  N N   . ALA E 1 133 ? 159.181 -35.136 43.629  1.000 39.530  ? 150 ALA EEE N   1 
ATOM 8911  C CA  . ALA E 1 133 ? 157.785 -34.716 43.382  1.000 40.590  ? 150 ALA EEE CA  1 
ATOM 8912  C C   . ALA E 1 133 ? 157.412 -33.600 44.358  1.000 41.890  ? 150 ALA EEE C   1 
ATOM 8913  O O   . ALA E 1 133 ? 157.827 -33.654 45.540  1.000 36.830  ? 150 ALA EEE O   1 
ATOM 8914  C CB  . ALA E 1 133 ? 156.838 -35.870 43.526  1.000 39.380  ? 150 ALA EEE CB  1 
ATOM 8915  N N   . LEU E 1 134 ? 156.638 -32.628 43.877  1.000 43.180  ? 151 LEU EEE N   1 
ATOM 8916  C CA  . LEU E 1 134 ? 155.890 -31.714 44.768  1.000 41.690  ? 151 LEU EEE CA  1 
ATOM 8917  C C   . LEU E 1 134 ? 155.041 -32.560 45.714  1.000 37.970  ? 151 LEU EEE C   1 
ATOM 8918  O O   . LEU E 1 134 ? 154.357 -33.488 45.234  1.000 37.500  ? 151 LEU EEE O   1 
ATOM 8919  C CB  . LEU E 1 134 ? 155.001 -30.811 43.907  1.000 41.110  ? 151 LEU EEE CB  1 
ATOM 8920  C CG  . LEU E 1 134 ? 154.243 -29.724 44.662  1.000 35.950  ? 151 LEU EEE CG  1 
ATOM 8921  C CD1 . LEU E 1 134 ? 155.205 -28.763 45.334  1.000 33.990  ? 151 LEU EEE CD1 1 
ATOM 8922  C CD2 . LEU E 1 134 ? 153.335 -28.992 43.703  1.000 36.800  ? 151 LEU EEE CD2 1 
ATOM 8923  N N   . GLU E 1 135 ? 155.070 -32.233 47.001  1.000 36.000  ? 152 GLU EEE N   1 
ATOM 8924  C CA  . GLU E 1 135 ? 154.252 -32.920 48.031  1.000 36.250  ? 152 GLU EEE CA  1 
ATOM 8925  C C   . GLU E 1 135 ? 152.975 -32.120 48.280  1.000 32.200  ? 152 GLU EEE C   1 
ATOM 8926  O O   . GLU E 1 135 ? 153.093 -30.909 48.537  1.000 30.020  ? 152 GLU EEE O   1 
ATOM 8927  C CB  . GLU E 1 135 ? 155.105 -33.126 49.281  1.000 38.510  ? 152 GLU EEE CB  1 
ATOM 8928  C CG  . GLU E 1 135 ? 156.246 -34.108 49.047  1.000 39.170  ? 152 GLU EEE CG  1 
ATOM 8929  C CD  . GLU E 1 135 ? 157.029 -34.414 50.302  1.000 38.360  ? 152 GLU EEE CD  1 
ATOM 8930  O OE1 . GLU E 1 135 ? 157.995 -33.673 50.596  1.000 35.330  ? 152 GLU EEE OE1 1 
ATOM 8931  O OE2 . GLU E 1 135 ? 156.642 -35.375 50.979  1.000 43.330  ? 152 GLU EEE OE2 1 
ATOM 8932  N N   . LEU E 1 136 ? 151.816 -32.783 48.185  1.000 29.430  ? 153 LEU EEE N   1 
ATOM 8933  C CA  . LEU E 1 136 ? 150.478 -32.144 48.257  1.000 28.440  ? 153 LEU EEE CA  1 
ATOM 8934  C C   . LEU E 1 136 ? 149.769 -32.445 49.587  1.000 27.860  ? 153 LEU EEE C   1 
ATOM 8935  O O   . LEU E 1 136 ? 149.824 -33.592 50.068  1.000 26.720  ? 153 LEU EEE O   1 
ATOM 8936  C CB  . LEU E 1 136 ? 149.608 -32.655 47.112  1.000 28.010  ? 153 LEU EEE CB  1 
ATOM 8937  C CG  . LEU E 1 136 ? 150.158 -32.482 45.709  1.000 28.870  ? 153 LEU EEE CG  1 
ATOM 8938  C CD1 . LEU E 1 136 ? 149.175 -33.060 44.699  1.000 29.710  ? 153 LEU EEE CD1 1 
ATOM 8939  C CD2 . LEU E 1 136 ? 150.410 -31.011 45.405  1.000 31.060  ? 153 LEU EEE CD2 1 
ATOM 8940  N N   . GLN E 1 137 ? 149.081 -31.433 50.116  1.000 26.600  ? 154 GLN EEE N   1 
ATOM 8941  C CA  . GLN E 1 137 ? 148.048 -31.539 51.171  1.000 25.800  ? 154 GLN EEE CA  1 
ATOM 8942  C C   . GLN E 1 137 ? 146.683 -31.340 50.514  1.000 24.120  ? 154 GLN EEE C   1 
ATOM 8943  O O   . GLN E 1 137 ? 146.517 -30.415 49.727  1.000 25.560  ? 154 GLN EEE O   1 
ATOM 8944  C CB  . GLN E 1 137 ? 148.267 -30.468 52.236  1.000 27.970  ? 154 GLN EEE CB  1 
ATOM 8945  C CG  . GLN E 1 137 ? 147.127 -30.334 53.233  1.000 28.530  ? 154 GLN EEE CG  1 
ATOM 8946  C CD  . GLN E 1 137 ? 146.996 -31.600 54.032  1.000 30.620  ? 154 GLN EEE CD  1 
ATOM 8947  O OE1 . GLN E 1 137 ? 147.996 -32.173 54.453  1.000 30.810  ? 154 GLN EEE OE1 1 
ATOM 8948  N NE2 . GLN E 1 137 ? 145.764 -32.045 54.245  1.000 32.460  ? 154 GLN EEE NE2 1 
ATOM 8949  N N   . GLY E 1 138 ? 145.734 -32.200 50.809  1.000 24.550  ? 155 GLY EEE N   1 
ATOM 8950  C CA  . GLY E 1 138 ? 144.347 -32.015 50.364  1.000 24.320  ? 155 GLY EEE CA  1 
ATOM 8951  C C   . GLY E 1 138 ? 143.614 -31.043 51.259  1.000 23.540  ? 155 GLY EEE C   1 
ATOM 8952  O O   . GLY E 1 138 ? 143.696 -31.159 52.507  1.000 21.700  ? 155 GLY EEE O   1 
ATOM 8953  N N   . VAL E 1 139 ? 142.897 -30.116 50.643  1.000 26.440  ? 156 VAL EEE N   1 
ATOM 8954  C CA  . VAL E 1 139 ? 141.915 -29.232 51.335  1.000 28.390  ? 156 VAL EEE CA  1 
ATOM 8955  C C   . VAL E 1 139 ? 140.717 -29.077 50.418  1.000 27.770  ? 156 VAL EEE C   1 
ATOM 8956  O O   . VAL E 1 139 ? 140.926 -28.784 49.217  1.000 33.880  ? 156 VAL EEE O   1 
ATOM 8957  C CB  . VAL E 1 139 ? 142.467 -27.844 51.674  1.000 31.580  ? 156 VAL EEE CB  1 
ATOM 8958  C CG1 . VAL E 1 139 ? 141.466 -27.073 52.519  1.000 34.670  ? 156 VAL EEE CG1 1 
ATOM 8959  C CG2 . VAL E 1 139 ? 143.827 -27.904 52.352  1.000 31.780  ? 156 VAL EEE CG2 1 
ATOM 8960  N N   . LEU E 1 140 ? 139.528 -29.246 50.977  1.000 26.720  ? 157 LEU EEE N   1 
ATOM 8961  C CA  . LEU E 1 140 ? 138.266 -29.317 50.198  1.000 27.310  ? 157 LEU EEE CA  1 
ATOM 8962  C C   . LEU E 1 140 ? 137.432 -28.071 50.490  1.000 26.860  ? 157 LEU EEE C   1 
ATOM 8963  O O   . LEU E 1 140 ? 137.306 -27.710 51.648  1.000 25.280  ? 157 LEU EEE O   1 
ATOM 8964  C CB  . LEU E 1 140 ? 137.502 -30.601 50.559  1.000 25.350  ? 157 LEU EEE CB  1 
ATOM 8965  C CG  . LEU E 1 140 ? 138.214 -31.907 50.243  1.000 24.140  ? 157 LEU EEE CG  1 
ATOM 8966  C CD1 . LEU E 1 140 ? 137.335 -33.091 50.577  1.000 24.790  ? 157 LEU EEE CD1 1 
ATOM 8967  C CD2 . LEU E 1 140 ? 138.629 -31.958 48.788  1.000 24.010  ? 157 LEU EEE CD2 1 
ATOM 8968  N N   . PHE E 1 141 ? 136.871 -27.440 49.460  1.000 26.960  ? 158 PHE EEE N   1 
ATOM 8969  C CA  . PHE E 1 141 ? 135.850 -26.387 49.670  1.000 24.770  ? 158 PHE EEE CA  1 
ATOM 8970  C C   . PHE E 1 141 ? 134.622 -27.037 50.316  1.000 24.000  ? 158 PHE EEE C   1 
ATOM 8971  O O   . PHE E 1 141 ? 134.124 -26.511 51.296  1.000 23.600  ? 158 PHE EEE O   1 
ATOM 8972  C CB  . PHE E 1 141 ? 135.504 -25.681 48.364  1.000 23.930  ? 158 PHE EEE CB  1 
ATOM 8973  C CG  . PHE E 1 141 ? 134.432 -24.649 48.536  1.000 21.870  ? 158 PHE EEE CG  1 
ATOM 8974  C CD1 . PHE E 1 141 ? 134.742 -23.445 49.143  1.000 21.140  ? 158 PHE EEE CD1 1 
ATOM 8975  C CD2 . PHE E 1 141 ? 133.119 -24.910 48.151  1.000 21.530  ? 158 PHE EEE CD2 1 
ATOM 8976  C CE1 . PHE E 1 141 ? 133.763 -22.476 49.319  1.000 22.710  ? 158 PHE EEE CE1 1 
ATOM 8977  C CE2 . PHE E 1 141 ? 132.136 -23.957 48.347  1.000 23.110  ? 158 PHE EEE CE2 1 
ATOM 8978  C CZ  . PHE E 1 141 ? 132.461 -22.731 48.918  1.000 23.900  ? 158 PHE EEE CZ  1 
ATOM 8979  N N   . ASN E 1 142 ? 134.186 -28.170 49.778  1.000 24.570  ? 159 ASN EEE N   1 
ATOM 8980  C CA  . ASN E 1 142 ? 132.999 -28.929 50.252  1.000 23.060  ? 159 ASN EEE CA  1 
ATOM 8981  C C   . ASN E 1 142 ? 133.399 -30.395 50.338  1.000 23.090  ? 159 ASN EEE C   1 
ATOM 8982  O O   . ASN E 1 142 ? 133.709 -30.934 49.278  1.000 24.840  ? 159 ASN EEE O   1 
ATOM 8983  C CB  . ASN E 1 142 ? 131.828 -28.743 49.286  1.000 21.970  ? 159 ASN EEE CB  1 
ATOM 8984  C CG  . ASN E 1 142 ? 130.593 -29.532 49.668  1.000 20.800  ? 159 ASN EEE CG  1 
ATOM 8985  O OD1 . ASN E 1 142 ? 130.527 -30.101 50.747  1.000 24.980  ? 159 ASN EEE OD1 1 
ATOM 8986  N ND2 . ASN E 1 142 ? 129.585 -29.535 48.824  1.000 19.700  ? 159 ASN EEE ND2 1 
ATOM 8987  N N   . TYR E 1 143 ? 133.441 -30.995 51.529  1.000 24.350  ? 160 TYR EEE N   1 
ATOM 8988  C CA  . TYR E 1 143 ? 133.946 -32.386 51.719  1.000 26.640  ? 160 TYR EEE CA  1 
ATOM 8989  C C   . TYR E 1 143 ? 133.034 -33.405 51.036  1.000 25.550  ? 160 TYR EEE C   1 
ATOM 8990  O O   . TYR E 1 143 ? 133.558 -34.467 50.650  1.000 22.000  ? 160 TYR EEE O   1 
ATOM 8991  C CB  . TYR E 1 143 ? 134.220 -32.725 53.196  1.000 28.970  ? 160 TYR EEE CB  1 
ATOM 8992  C CG  . TYR E 1 143 ? 133.041 -33.264 53.971  1.000 30.760  ? 160 TYR EEE CG  1 
ATOM 8993  C CD1 . TYR E 1 143 ? 132.020 -32.421 54.379  1.000 31.570  ? 160 TYR EEE CD1 1 
ATOM 8994  C CD2 . TYR E 1 143 ? 132.930 -34.601 54.296  1.000 31.530  ? 160 TYR EEE CD2 1 
ATOM 8995  C CE1 . TYR E 1 143 ? 130.925 -32.880 55.082  1.000 28.280  ? 160 TYR EEE CE1 1 
ATOM 8996  C CE2 . TYR E 1 143 ? 131.831 -35.080 54.998  1.000 29.960  ? 160 TYR EEE CE2 1 
ATOM 8997  C CZ  . TYR E 1 143 ? 130.822 -34.215 55.366  1.000 27.450  ? 160 TYR EEE CZ  1 
ATOM 8998  O OH  . TYR E 1 143 ? 129.719 -34.621 56.036  1.000 28.930  ? 160 TYR EEE OH  1 
ATOM 8999  N N   . ARG E 1 144 ? 131.776 -33.033 50.783  1.000 28.560  ? 161 ARG EEE N   1 
ATOM 9000  C CA  . ARG E 1 144 ? 130.770 -33.929 50.155  1.000 33.020  ? 161 ARG EEE CA  1 
ATOM 9001  C C   . ARG E 1 144 ? 130.868 -33.858 48.632  1.000 31.940  ? 161 ARG EEE C   1 
ATOM 9002  O O   . ARG E 1 144 ? 130.103 -34.559 47.978  1.000 34.060  ? 161 ARG EEE O   1 
ATOM 9003  C CB  . ARG E 1 144 ? 129.382 -33.598 50.692  1.000 40.310  ? 161 ARG EEE CB  1 
ATOM 9004  C CG  . ARG E 1 144 ? 128.892 -34.533 51.790  1.000 48.810  ? 161 ARG EEE CG  1 
ATOM 9005  C CD  . ARG E 1 144 ? 127.787 -33.887 52.606  1.000 53.850  ? 161 ARG EEE CD  1 
ATOM 9006  N NE  . ARG E 1 144 ? 128.014 -32.457 52.725  1.000 67.370  ? 161 ARG EEE NE  1 
ATOM 9007  C CZ  . ARG E 1 144 ? 127.135 -31.600 53.223  1.000 64.600  ? 161 ARG EEE CZ  1 
ATOM 9008  N NH1 . ARG E 1 144 ? 125.964 -32.033 53.653  1.000 59.970  ? 161 ARG EEE NH1 1 
ATOM 9009  N NH2 . ARG E 1 144 ? 127.430 -30.317 53.295  1.000 58.700  ? 161 ARG EEE NH2 1 
ATOM 9010  N N   . THR E 1 145 ? 131.716 -32.998 48.090  1.000 33.140  ? 162 THR EEE N   1 
ATOM 9011  C CA  . THR E 1 145 ? 132.025 -32.969 46.625  1.000 32.560  ? 162 THR EEE CA  1 
ATOM 9012  C C   . THR E 1 145 ? 132.545 -34.354 46.222  1.000 31.840  ? 162 THR EEE C   1 
ATOM 9013  O O   . THR E 1 145 ? 133.513 -34.777 46.877  1.000 29.880  ? 162 THR EEE O   1 
ATOM 9014  C CB  . THR E 1 145 ? 133.128 -31.970 46.237  1.000 32.200  ? 162 THR EEE CB  1 
ATOM 9015  O OG1 . THR E 1 145 ? 132.853 -30.596 46.529  1.000 29.810  ? 162 THR EEE OG1 1 
ATOM 9016  C CG2 . THR E 1 145 ? 133.451 -32.059 44.762  1.000 33.470  ? 162 THR EEE CG2 1 
ATOM 9017  N N   . LYS E 1 146 ? 131.949 -35.008 45.215  1.000 32.610  ? 163 LYS EEE N   1 
ATOM 9018  C CA  . LYS E 1 146 ? 132.413 -36.315 44.675  1.000 36.700  ? 163 LYS EEE CA  1 
ATOM 9019  C C   . LYS E 1 146 ? 133.352 -36.051 43.507  1.000 36.260  ? 163 LYS EEE C   1 
ATOM 9020  O O   . LYS E 1 146 ? 132.835 -35.754 42.393  1.000 43.830  ? 163 LYS EEE O   1 
ATOM 9021  C CB  . LYS E 1 146 ? 131.280 -37.186 44.117  1.000 42.720  ? 163 LYS EEE CB  1 
ATOM 9022  C CG  . LYS E 1 146 ? 130.456 -38.000 45.098  1.000 58.830  ? 163 LYS EEE CG  1 
ATOM 9023  C CD  . LYS E 1 146 ? 129.664 -37.173 46.112  1.000 66.570  ? 163 LYS EEE CD  1 
ATOM 9024  C CE  . LYS E 1 146 ? 129.089 -38.012 47.240  1.000 61.760  ? 163 LYS EEE CE  1 
ATOM 9025  N NZ  . LYS E 1 146 ? 128.834 -37.181 48.443  1.000 57.710  ? 163 LYS EEE NZ  1 
ATOM 9026  N N   . TYR E 1 147 ? 134.672 -36.181 43.702  1.000 34.470  ? 164 TYR EEE N   1 
ATOM 9027  C CA  . TYR E 1 147 ? 135.655 -35.900 42.626  1.000 31.520  ? 164 TYR EEE CA  1 
ATOM 9028  C C   . TYR E 1 147 ? 135.575 -37.054 41.640  1.000 31.670  ? 164 TYR EEE C   1 
ATOM 9029  O O   . TYR E 1 147 ? 135.429 -38.200 42.032  1.000 28.110  ? 164 TYR EEE O   1 
ATOM 9030  C CB  . TYR E 1 147 ? 137.030 -35.538 43.196  1.000 30.440  ? 164 TYR EEE CB  1 
ATOM 9031  C CG  . TYR E 1 147 ? 137.058 -34.121 43.723  1.000 29.580  ? 164 TYR EEE CG  1 
ATOM 9032  C CD1 . TYR E 1 147 ? 136.689 -33.856 45.017  1.000 31.860  ? 164 TYR EEE CD1 1 
ATOM 9033  C CD2 . TYR E 1 147 ? 137.370 -33.039 42.931  1.000 29.430  ? 164 TYR EEE CD2 1 
ATOM 9034  C CE1 . TYR E 1 147 ? 136.658 -32.572 45.524  1.000 34.220  ? 164 TYR EEE CE1 1 
ATOM 9035  C CE2 . TYR E 1 147 ? 137.349 -31.745 43.419  1.000 33.630  ? 164 TYR EEE CE2 1 
ATOM 9036  C CZ  . TYR E 1 147 ? 136.975 -31.495 44.727  1.000 35.620  ? 164 TYR EEE CZ  1 
ATOM 9037  O OH  . TYR E 1 147 ? 136.911 -30.223 45.270  1.000 39.290  ? 164 TYR EEE OH  1 
ATOM 9038  N N   . PRO E 1 148 ? 135.645 -36.779 40.320  1.000 40.470  ? 165 PRO EEE N   1 
ATOM 9039  C CA  . PRO E 1 148 ? 135.207 -37.732 39.316  1.000 41.730  ? 165 PRO EEE CA  1 
ATOM 9040  C C   . PRO E 1 148 ? 136.263 -38.808 39.087  1.000 41.800  ? 165 PRO EEE C   1 
ATOM 9041  O O   . PRO E 1 148 ? 137.474 -38.533 39.178  1.000 42.280  ? 165 PRO EEE O   1 
ATOM 9042  C CB  . PRO E 1 148 ? 135.081 -36.870 38.060  1.000 46.680  ? 165 PRO EEE CB  1 
ATOM 9043  C CG  . PRO E 1 148 ? 136.209 -35.867 38.205  1.000 46.220  ? 165 PRO EEE CG  1 
ATOM 9044  C CD  . PRO E 1 148 ? 136.282 -35.602 39.698  1.000 46.740  ? 165 PRO EEE CD  1 
ATOM 9045  N N   . ASP E 1 149 ? 135.759 -40.008 38.813  1.000 40.590  ? 166 ASP EEE N   1 
ATOM 9046  C CA  . ASP E 1 149 ? 136.521 -41.181 38.324  1.000 41.370  ? 166 ASP EEE CA  1 
ATOM 9047  C C   . ASP E 1 149 ? 137.629 -40.720 37.359  1.000 34.650  ? 166 ASP EEE C   1 
ATOM 9048  O O   . ASP E 1 149 ? 137.303 -40.105 36.316  1.000 34.920  ? 166 ASP EEE O   1 
ATOM 9049  C CB  . ASP E 1 149 ? 135.502 -42.095 37.657  1.000 50.830  ? 166 ASP EEE CB  1 
ATOM 9050  C CG  . ASP E 1 149 ? 135.897 -43.539 37.580  1.000 56.340  ? 166 ASP EEE CG  1 
ATOM 9051  O OD1 . ASP E 1 149 ? 137.093 -43.831 37.403  1.000 60.270  ? 166 ASP EEE OD1 1 
ATOM 9052  O OD2 . ASP E 1 149 ? 134.983 -44.331 37.628  1.000 75.440  ? 166 ASP EEE OD2 1 
ATOM 9053  N N   . GLY E 1 150 ? 138.891 -41.001 37.664  1.000 31.440  ? 167 GLY EEE N   1 
ATOM 9054  C CA  . GLY E 1 150 ? 139.998 -40.728 36.718  1.000 31.260  ? 167 GLY EEE CA  1 
ATOM 9055  C C   . GLY E 1 150 ? 140.954 -39.660 37.212  1.000 29.930  ? 167 GLY EEE C   1 
ATOM 9056  O O   . GLY E 1 150 ? 142.002 -39.487 36.601  1.000 27.380  ? 167 GLY EEE O   1 
ATOM 9057  N N   . THR E 1 151 ? 140.573 -38.966 38.278  1.000 31.400  ? 168 THR EEE N   1 
ATOM 9058  C CA  . THR E 1 151 ? 141.381 -37.975 39.024  1.000 31.650  ? 168 THR EEE CA  1 
ATOM 9059  C C   . THR E 1 151 ? 141.776 -38.592 40.363  1.000 32.480  ? 168 THR EEE C   1 
ATOM 9060  O O   . THR E 1 151 ? 141.018 -39.385 40.887  1.000 37.200  ? 168 THR EEE O   1 
ATOM 9061  C CB  . THR E 1 151 ? 140.557 -36.709 39.273  1.000 32.340  ? 168 THR EEE CB  1 
ATOM 9062  O OG1 . THR E 1 151 ? 139.436 -37.024 40.102  1.000 28.940  ? 168 THR EEE OG1 1 
ATOM 9063  C CG2 . THR E 1 151 ? 140.030 -36.111 37.994  1.000 33.510  ? 168 THR EEE CG2 1 
ATOM 9064  N N   . ILE E 1 152 ? 142.934 -38.235 40.880  1.000 31.630  ? 169 ILE EEE N   1 
ATOM 9065  C CA  . ILE E 1 152 ? 143.418 -38.622 42.230  1.000 30.930  ? 169 ILE EEE CA  1 
ATOM 9066  C C   . ILE E 1 152 ? 142.975 -37.508 43.191  1.000 34.440  ? 169 ILE EEE C   1 
ATOM 9067  O O   . ILE E 1 152 ? 143.405 -36.368 43.050  1.000 34.630  ? 169 ILE EEE O   1 
ATOM 9068  C CB  . ILE E 1 152 ? 144.942 -38.810 42.165  1.000 29.770  ? 169 ILE EEE CB  1 
ATOM 9069  C CG1 . ILE E 1 152 ? 145.284 -40.000 41.281  1.000 31.110  ? 169 ILE EEE CG1 1 
ATOM 9070  C CG2 . ILE E 1 152 ? 145.569 -38.957 43.531  1.000 30.260  ? 169 ILE EEE CG2 1 
ATOM 9071  C CD1 . ILE E 1 152 ? 146.730 -40.016 40.863  1.000 33.800  ? 169 ILE EEE CD1 1 
ATOM 9072  N N   . PHE E 1 153 ? 142.114 -37.830 44.145  1.000 38.400  ? 170 PHE EEE N   1 
ATOM 9073  C CA  . PHE E 1 153 ? 141.513 -36.843 45.071  1.000 39.160  ? 170 PHE EEE CA  1 
ATOM 9074  C C   . PHE E 1 153 ? 141.689 -37.295 46.510  1.000 36.300  ? 170 PHE EEE C   1 
ATOM 9075  O O   . PHE E 1 153 ? 141.995 -38.449 46.763  1.000 42.110  ? 170 PHE EEE O   1 
ATOM 9076  C CB  . PHE E 1 153 ? 140.039 -36.664 44.727  1.000 41.990  ? 170 PHE EEE CB  1 
ATOM 9077  C CG  . PHE E 1 153 ? 139.260 -37.945 44.637  1.000 43.230  ? 170 PHE EEE CG  1 
ATOM 9078  C CD1 . PHE E 1 153 ? 139.265 -38.694 43.474  1.000 45.830  ? 170 PHE EEE CD1 1 
ATOM 9079  C CD2 . PHE E 1 153 ? 138.483 -38.371 45.696  1.000 43.750  ? 170 PHE EEE CD2 1 
ATOM 9080  C CE1 . PHE E 1 153 ? 138.527 -39.866 43.384  1.000 49.920  ? 170 PHE EEE CE1 1 
ATOM 9081  C CE2 . PHE E 1 153 ? 137.736 -39.534 45.601  1.000 46.690  ? 170 PHE EEE CE2 1 
ATOM 9082  C CZ  . PHE E 1 153 ? 137.762 -40.283 44.447  1.000 49.760  ? 170 PHE EEE CZ  1 
ATOM 9083  N N   . PRO E 1 154 ? 141.525 -36.395 47.491  1.000 36.180  ? 171 PRO EEE N   1 
ATOM 9084  C CA  . PRO E 1 154 ? 141.485 -36.772 48.899  1.000 41.240  ? 171 PRO EEE CA  1 
ATOM 9085  C C   . PRO E 1 154 ? 140.477 -37.890 49.169  1.000 39.290  ? 171 PRO EEE C   1 
ATOM 9086  O O   . PRO E 1 154 ? 139.325 -37.720 48.825  1.000 36.440  ? 171 PRO EEE O   1 
ATOM 9087  C CB  . PRO E 1 154 ? 141.013 -35.486 49.585  1.000 42.720  ? 171 PRO EEE CB  1 
ATOM 9088  C CG  . PRO E 1 154 ? 141.599 -34.422 48.719  1.000 41.070  ? 171 PRO EEE CG  1 
ATOM 9089  C CD  . PRO E 1 154 ? 141.397 -34.946 47.313  1.000 39.550  ? 171 PRO EEE CD  1 
ATOM 9090  N N   . LYS E 1 155 ? 140.959 -38.978 49.760  1.000 39.070  ? 172 LYS EEE N   1 
ATOM 9091  C CA  . LYS E 1 155 ? 140.148 -40.170 50.090  1.000 45.370  ? 172 LYS EEE CA  1 
ATOM 9092  C C   . LYS E 1 155 ? 139.794 -40.080 51.571  1.000 44.600  ? 172 LYS EEE C   1 
ATOM 9093  O O   . LYS E 1 155 ? 140.589 -39.508 52.325  1.000 39.420  ? 172 LYS EEE O   1 
ATOM 9094  C CB  . LYS E 1 155 ? 140.925 -41.445 49.744  1.000 49.090  ? 172 LYS EEE CB  1 
ATOM 9095  C CG  . LYS E 1 155 ? 141.106 -41.684 48.250  1.000 55.590  ? 172 LYS EEE CG  1 
ATOM 9096  C CD  . LYS E 1 155 ? 142.336 -42.521 47.920  1.000 63.640  ? 172 LYS EEE CD  1 
ATOM 9097  C CE  . LYS E 1 155 ? 143.598 -41.675 47.913  1.000 70.760  ? 172 LYS EEE CE  1 
ATOM 9098  N NZ  . LYS E 1 155 ? 144.788 -42.450 47.493  1.000 76.720  ? 172 LYS EEE NZ  1 
ATOM 9099  N N   . ASN E 1 156 ? 138.613 -40.609 51.943  1.000 42.270  ? 173 ASN EEE N   1 
ATOM 9100  C CA  . ASN E 1 156 ? 138.123 -40.676 53.346  1.000 41.000  ? 173 ASN EEE CA  1 
ATOM 9101  C C   . ASN E 1 156 ? 137.868 -39.259 53.842  1.000 37.490  ? 173 ASN EEE C   1 
ATOM 9102  O O   . ASN E 1 156 ? 138.233 -38.952 54.978  1.000 38.010  ? 173 ASN EEE O   1 
ATOM 9103  C CB  . ASN E 1 156 ? 139.086 -41.438 54.255  1.000 44.430  ? 173 ASN EEE CB  1 
ATOM 9104  C CG  . ASN E 1 156 ? 139.264 -42.863 53.780  1.000 46.170  ? 173 ASN EEE CG  1 
ATOM 9105  O OD1 . ASN E 1 156 ? 138.277 -43.548 53.503  1.000 48.080  ? 173 ASN EEE OD1 1 
ATOM 9106  N ND2 . ASN E 1 156 ? 140.510 -43.291 53.632  1.000 47.510  ? 173 ASN EEE ND2 1 
ATOM 9107  N N   . ALA E 1 157 ? 137.258 -38.444 52.993  1.000 37.410  ? 174 ALA EEE N   1 
ATOM 9108  C CA  . ALA E 1 157 ? 136.903 -37.045 53.295  1.000 36.590  ? 174 ALA EEE CA  1 
ATOM 9109  C C   . ALA E 1 157 ? 135.979 -37.044 54.500  1.000 33.670  ? 174 ALA EEE C   1 
ATOM 9110  O O   . ALA E 1 157 ? 135.034 -37.826 54.533  1.000 29.720  ? 174 ALA EEE O   1 
ATOM 9111  C CB  . ALA E 1 157 ? 136.231 -36.392 52.115  1.000 43.140  ? 174 ALA EEE CB  1 
ATOM 9112  N N   . THR E 1 158 ? 136.300 -36.198 55.464  1.000 35.470  ? 175 THR EEE N   1 
ATOM 9113  C CA  . THR E 1 158 ? 135.455 -35.866 56.627  1.000 33.770  ? 175 THR EEE CA  1 
ATOM 9114  C C   . THR E 1 158 ? 135.192 -34.356 56.574  1.000 31.380  ? 175 THR EEE C   1 
ATOM 9115  O O   . THR E 1 158 ? 135.834 -33.646 55.779  1.000 30.880  ? 175 THR EEE O   1 
ATOM 9116  C CB  . THR E 1 158 ? 136.154 -36.397 57.882  1.000 36.760  ? 175 THR EEE CB  1 
ATOM 9117  O OG1 . THR E 1 158 ? 137.272 -35.579 58.252  1.000 35.280  ? 175 THR EEE OG1 1 
ATOM 9118  C CG2 . THR E 1 158 ? 136.642 -37.813 57.668  1.000 38.260  ? 175 THR EEE CG2 1 
ATOM 9119  N N   . VAL E 1 159 ? 134.264 -33.861 57.370  1.000 29.550  ? 176 VAL EEE N   1 
ATOM 9120  C CA  . VAL E 1 159 ? 134.045 -32.395 57.464  1.000 27.470  ? 176 VAL EEE CA  1 
ATOM 9121  C C   . VAL E 1 159 ? 135.393 -31.736 57.780  1.000 26.700  ? 176 VAL EEE C   1 
ATOM 9122  O O   . VAL E 1 159 ? 135.639 -30.672 57.221  1.000 26.510  ? 176 VAL EEE O   1 
ATOM 9123  C CB  . VAL E 1 159 ? 132.966 -32.050 58.503  1.000 27.200  ? 176 VAL EEE CB  1 
ATOM 9124  C CG1 . VAL E 1 159 ? 133.514 -32.013 59.914  1.000 25.990  ? 176 VAL EEE CG1 1 
ATOM 9125  C CG2 . VAL E 1 159 ? 132.263 -30.750 58.143  1.000 28.160  ? 176 VAL EEE CG2 1 
ATOM 9126  N N   . GLN E 1 160 ? 136.266 -32.354 58.583  1.000 28.190  ? 177 GLN EEE N   1 
ATOM 9127  C CA  . GLN E 1 160 ? 137.591 -31.754 58.925  1.000 29.890  ? 177 GLN EEE CA  1 
ATOM 9128  C C   . GLN E 1 160 ? 138.387 -31.513 57.646  1.000 27.480  ? 177 GLN EEE C   1 
ATOM 9129  O O   . GLN E 1 160 ? 139.190 -30.587 57.638  1.000 24.730  ? 177 GLN EEE O   1 
ATOM 9130  C CB  . GLN E 1 160 ? 138.433 -32.592 59.899  1.000 31.430  ? 177 GLN EEE CB  1 
ATOM 9131  C CG  . GLN E 1 160 ? 137.808 -32.749 61.276  1.000 34.820  ? 177 GLN EEE CG  1 
ATOM 9132  C CD  . GLN E 1 160 ? 137.364 -31.467 61.957  1.000 37.510  ? 177 GLN EEE CD  1 
ATOM 9133  O OE1 . GLN E 1 160 ? 138.071 -30.427 61.971  1.000 39.480  ? 177 GLN EEE OE1 1 
ATOM 9134  N NE2 . GLN E 1 160 ? 136.168 -31.558 62.541  1.000 32.820  ? 177 GLN EEE NE2 1 
ATOM 9135  N N   . SER E 1 161 ? 138.144 -32.300 56.596  1.000 29.040  ? 178 SER EEE N   1 
ATOM 9136  C CA  . SER E 1 161 ? 138.846 -32.158 55.293  1.000 30.940  ? 178 SER EEE CA  1 
ATOM 9137  C C   . SER E 1 161 ? 138.690 -30.722 54.766  1.000 31.800  ? 178 SER EEE C   1 
ATOM 9138  O O   . SER E 1 161 ? 139.683 -30.229 54.152  1.000 38.660  ? 178 SER EEE O   1 
ATOM 9139  C CB  . SER E 1 161 ? 138.377 -33.188 54.300  1.000 30.640  ? 178 SER EEE CB  1 
ATOM 9140  O OG  . SER E 1 161 ? 138.709 -34.501 54.754  1.000 30.430  ? 178 SER EEE OG  1 
ATOM 9141  N N   . GLN E 1 162 ? 137.543 -30.076 55.055  1.000 27.080  ? 179 GLN EEE N   1 
ATOM 9142  C CA  . GLN E 1 162 ? 137.171 -28.698 54.643  1.000 24.450  ? 179 GLN EEE CA  1 
ATOM 9143  C C   . GLN E 1 162 ? 138.135 -27.656 55.224  1.000 24.670  ? 179 GLN EEE C   1 
ATOM 9144  O O   . GLN E 1 162 ? 138.212 -26.560 54.631  1.000 24.730  ? 179 GLN EEE O   1 
ATOM 9145  C CB  . GLN E 1 162 ? 135.738 -28.347 55.074  1.000 24.200  ? 179 GLN EEE CB  1 
ATOM 9146  C CG  . GLN E 1 162 ? 134.692 -28.584 53.987  1.000 24.130  ? 179 GLN EEE CG  1 
ATOM 9147  C CD  . GLN E 1 162 ? 133.270 -28.721 54.482  1.000 22.730  ? 179 GLN EEE CD  1 
ATOM 9148  O OE1 . GLN E 1 162 ? 132.407 -29.287 53.785  1.000 20.450  ? 179 GLN EEE OE1 1 
ATOM 9149  N NE2 . GLN E 1 162 ? 133.014 -28.171 55.667  1.000 20.700  ? 179 GLN EEE NE2 1 
ATOM 9150  N N   . VAL E 1 163 ? 138.808 -27.915 56.352  1.000 24.370  ? 180 VAL EEE N   1 
ATOM 9151  C CA  . VAL E 1 163 ? 139.714 -26.894 56.969  1.000 25.480  ? 180 VAL EEE CA  1 
ATOM 9152  C C   . VAL E 1 163 ? 141.139 -27.425 57.026  1.000 27.140  ? 180 VAL EEE C   1 
ATOM 9153  O O   . VAL E 1 163 ? 142.062 -26.684 56.599  1.000 29.550  ? 180 VAL EEE O   1 
ATOM 9154  C CB  . VAL E 1 163 ? 139.246 -26.418 58.354  1.000 25.020  ? 180 VAL EEE CB  1 
ATOM 9155  C CG1 . VAL E 1 163 ? 137.956 -25.616 58.253  1.000 25.840  ? 180 VAL EEE CG1 1 
ATOM 9156  C CG2 . VAL E 1 163 ? 139.076 -27.551 59.342  1.000 26.320  ? 180 VAL EEE CG2 1 
ATOM 9157  N N   . MET E 1 164 ? 141.289 -28.657 57.504  1.000 29.580  ? 181 MET EEE N   1 
ATOM 9158  C CA  . MET E 1 164 ? 142.578 -29.389 57.554  1.000 31.810  ? 181 MET EEE CA  1 
ATOM 9159  C C   . MET E 1 164 ? 142.376 -30.833 58.042  1.000 32.810  ? 181 MET EEE C   1 
ATOM 9160  O O   . MET E 1 164 ? 141.696 -31.043 59.049  1.000 32.860  ? 181 MET EEE O   1 
ATOM 9161  C CB  . MET E 1 164 ? 143.554 -28.679 58.484  1.000 33.320  ? 181 MET EEE CB  1 
ATOM 9162  C CG  . MET E 1 164 ? 144.945 -29.231 58.361  1.000 37.170  ? 181 MET EEE CG  1 
ATOM 9163  S SD  . MET E 1 164 ? 145.597 -29.101 56.677  1.000 37.720  ? 181 MET EEE SD  1 
ATOM 9164  C CE  . MET E 1 164 ? 147.076 -30.088 56.886  1.000 40.280  ? 181 MET EEE CE  1 
ATOM 9165  N N   . ASN E 1 165 ? 142.981 -31.797 57.351  1.000 33.590  ? 182 ASN EEE N   1 
ATOM 9166  C CA  . ASN E 1 165 ? 142.883 -33.247 57.667  1.000 30.180  ? 182 ASN EEE CA  1 
ATOM 9167  C C   . ASN E 1 165 ? 144.166 -33.928 57.165  1.000 29.840  ? 182 ASN EEE C   1 
ATOM 9168  O O   . ASN E 1 165 ? 144.290 -34.140 55.943  1.000 32.250  ? 182 ASN EEE O   1 
ATOM 9169  C CB  . ASN E 1 165 ? 141.615 -33.825 57.035  1.000 28.660  ? 182 ASN EEE CB  1 
ATOM 9170  C CG  . ASN E 1 165 ? 141.539 -35.333 57.125  1.000 28.180  ? 182 ASN EEE CG  1 
ATOM 9171  O OD1 . ASN E 1 165 ? 142.547 -35.985 57.359  1.000 29.270  ? 182 ASN EEE OD1 1 
ATOM 9172  N ND2 . ASN E 1 165 ? 140.351 -35.893 56.943  1.000 28.680  ? 182 ASN EEE ND2 1 
ATOM 9173  N N   . THR E 1 166 ? 145.091 -34.266 58.059  1.000 27.310  ? 183 THR EEE N   1 
ATOM 9174  C CA  . THR E 1 166 ? 146.456 -34.701 57.685  1.000 27.940  ? 183 THR EEE CA  1 
ATOM 9175  C C   . THR E 1 166 ? 146.440 -36.063 56.997  1.000 28.410  ? 183 THR EEE C   1 
ATOM 9176  O O   . THR E 1 166 ? 147.513 -36.460 56.500  1.000 31.690  ? 183 THR EEE O   1 
ATOM 9177  C CB  . THR E 1 166 ? 147.385 -34.754 58.896  1.000 30.090  ? 183 THR EEE CB  1 
ATOM 9178  O OG1 . THR E 1 166 ? 146.545 -35.158 59.963  1.000 32.340  ? 183 THR EEE OG1 1 
ATOM 9179  C CG2 . THR E 1 166 ? 148.039 -33.433 59.235  1.000 33.330  ? 183 THR EEE CG2 1 
ATOM 9180  N N   . GLU E 1 167 ? 145.305 -36.759 56.931  1.000 30.160  ? 184 GLU EEE N   1 
ATOM 9181  C CA  . GLU E 1 167 ? 145.197 -37.999 56.100  1.000 32.190  ? 184 GLU EEE CA  1 
ATOM 9182  C C   . GLU E 1 167 ? 145.562 -37.658 54.649  1.000 30.830  ? 184 GLU EEE C   1 
ATOM 9183  O O   . GLU E 1 167 ? 146.318 -38.420 54.075  1.000 32.080  ? 184 GLU EEE O   1 
ATOM 9184  C CB  . GLU E 1 167 ? 143.823 -38.679 56.156  1.000 36.290  ? 184 GLU EEE CB  1 
ATOM 9185  C CG  . GLU E 1 167 ? 143.925 -40.196 56.002  1.000 41.110  ? 184 GLU EEE CG  1 
ATOM 9186  C CD  . GLU E 1 167 ? 142.675 -40.935 55.530  1.000 49.040  ? 184 GLU EEE CD  1 
ATOM 9187  O OE1 . GLU E 1 167 ? 142.657 -41.354 54.341  1.000 52.860  ? 184 GLU EEE OE1 1 
ATOM 9188  O OE2 . GLU E 1 167 ? 141.723 -41.120 56.350  1.000 51.430  ? 184 GLU EEE OE2 1 
ATOM 9189  N N   . HIS E 1 168 ? 145.090 -36.525 54.111  1.000 30.360  ? 185 HIS EEE N   1 
ATOM 9190  C CA  . HIS E 1 168 ? 145.156 -36.154 52.671  1.000 28.250  ? 185 HIS EEE CA  1 
ATOM 9191  C C   . HIS E 1 168 ? 146.561 -35.701 52.268  1.000 28.430  ? 185 HIS EEE C   1 
ATOM 9192  O O   . HIS E 1 168 ? 146.718 -34.532 51.881  1.000 27.840  ? 185 HIS EEE O   1 
ATOM 9193  C CB  . HIS E 1 168 ? 144.147 -35.061 52.352  1.000 27.280  ? 185 HIS EEE CB  1 
ATOM 9194  C CG  . HIS E 1 168 ? 142.783 -35.406 52.811  1.000 28.930  ? 185 HIS EEE CG  1 
ATOM 9195  N ND1 . HIS E 1 168 ? 142.228 -36.637 52.575  1.000 31.670  ? 185 HIS EEE ND1 1 
ATOM 9196  C CD2 . HIS E 1 168 ? 141.864 -34.678 53.474  1.000 30.800  ? 185 HIS EEE CD2 1 
ATOM 9197  C CE1 . HIS E 1 168 ? 140.998 -36.641 53.065  1.000 34.140  ? 185 HIS EEE CE1 1 
ATOM 9198  N NE2 . HIS E 1 168 ? 140.757 -35.454 53.626  1.000 30.660  ? 185 HIS EEE NE2 1 
ATOM 9199  N N   . LYS E 1 169 ? 147.533 -36.619 52.293  1.000 26.070  ? 186 LYS EEE N   1 
ATOM 9200  C CA  . LYS E 1 169 ? 148.871 -36.413 51.684  1.000 24.600  ? 186 LYS EEE CA  1 
ATOM 9201  C C   . LYS E 1 169 ? 148.940 -37.156 50.346  1.000 24.340  ? 186 LYS EEE C   1 
ATOM 9202  O O   . LYS E 1 169 ? 148.099 -38.057 50.121  1.000 21.280  ? 186 LYS EEE O   1 
ATOM 9203  C CB  . LYS E 1 169 ? 149.941 -36.860 52.662  1.000 23.310  ? 186 LYS EEE CB  1 
ATOM 9204  C CG  . LYS E 1 169 ? 149.745 -36.333 54.069  1.000 24.650  ? 186 LYS EEE CG  1 
ATOM 9205  C CD  . LYS E 1 169 ? 150.032 -34.866 54.236  1.000 25.890  ? 186 LYS EEE CD  1 
ATOM 9206  C CE  . LYS E 1 169 ? 150.097 -34.467 55.695  1.000 27.350  ? 186 LYS EEE CE  1 
ATOM 9207  N NZ  . LYS E 1 169 ? 150.366 -33.022 55.878  1.000 28.650  ? 186 LYS EEE NZ  1 
ATOM 9208  N N   . ALA E 1 170 ? 149.870 -36.755 49.476  1.000 25.370  ? 187 ALA EEE N   1 
ATOM 9209  C CA  . ALA E 1 170 ? 149.970 -37.235 48.084  1.000 28.250  ? 187 ALA EEE CA  1 
ATOM 9210  C C   . ALA E 1 170 ? 151.203 -36.640 47.401  1.000 32.950  ? 187 ALA EEE C   1 
ATOM 9211  O O   . ALA E 1 170 ? 151.647 -35.552 47.798  1.000 34.960  ? 187 ALA EEE O   1 
ATOM 9212  C CB  . ALA E 1 170 ? 148.710 -36.861 47.342  1.000 28.000  ? 187 ALA EEE CB  1 
ATOM 9213  N N   . TYR E 1 171 ? 151.686 -37.293 46.348  1.000 37.840  ? 188 TYR EEE N   1 
ATOM 9214  C CA  . TYR E 1 171 ? 152.818 -36.817 45.512  1.000 38.840  ? 188 TYR EEE CA  1 
ATOM 9215  C C   . TYR E 1 171 ? 152.279 -36.398 44.141  1.000 39.350  ? 188 TYR EEE C   1 
ATOM 9216  O O   . TYR E 1 171 ? 151.473 -37.138 43.538  1.000 36.270  ? 188 TYR EEE O   1 
ATOM 9217  C CB  . TYR E 1 171 ? 153.858 -37.928 45.382  1.000 42.630  ? 188 TYR EEE CB  1 
ATOM 9218  C CG  . TYR E 1 171 ? 154.557 -38.307 46.667  1.000 42.070  ? 188 TYR EEE CG  1 
ATOM 9219  C CD1 . TYR E 1 171 ? 155.630 -37.566 47.119  1.000 44.720  ? 188 TYR EEE CD1 1 
ATOM 9220  C CD2 . TYR E 1 171 ? 154.182 -39.423 47.393  1.000 36.760  ? 188 TYR EEE CD2 1 
ATOM 9221  C CE1 . TYR E 1 171 ? 156.302 -37.905 48.273  1.000 47.420  ? 188 TYR EEE CE1 1 
ATOM 9222  C CE2 . TYR E 1 171 ? 154.855 -39.791 48.540  1.000 38.790  ? 188 TYR EEE CE2 1 
ATOM 9223  C CZ  . TYR E 1 171 ? 155.910 -39.022 48.990  1.000 45.930  ? 188 TYR EEE CZ  1 
ATOM 9224  O OH  . TYR E 1 171 ? 156.564 -39.343 50.149  1.000 48.510  ? 188 TYR EEE OH  1 
ATOM 9225  N N   . LEU E 1 172 ? 152.676 -35.216 43.665  1.000 45.200  ? 189 LEU EEE N   1 
ATOM 9226  C CA  . LEU E 1 172 ? 152.361 -34.769 42.279  1.000 44.310  ? 189 LEU EEE CA  1 
ATOM 9227  C C   . LEU E 1 172 ? 153.277 -35.545 41.330  1.000 39.330  ? 189 LEU EEE C   1 
ATOM 9228  O O   . LEU E 1 172 ? 154.367 -35.032 40.964  1.000 39.170  ? 189 LEU EEE O   1 
ATOM 9229  C CB  . LEU E 1 172 ? 152.532 -33.257 42.135  1.000 45.170  ? 189 LEU EEE CB  1 
ATOM 9230  C CG  . LEU E 1 172 ? 152.101 -32.709 40.780  1.000 51.090  ? 189 LEU EEE CG  1 
ATOM 9231  C CD1 . LEU E 1 172 ? 150.720 -33.216 40.365  1.000 47.700  ? 189 LEU EEE CD1 1 
ATOM 9232  C CD2 . LEU E 1 172 ? 152.149 -31.189 40.782  1.000 55.040  ? 189 LEU EEE CD2 1 
ATOM 9233  N N   . ASP E 1 173 ? 152.830 -36.748 40.998  1.000 36.060  ? 190 ASP EEE N   1 
ATOM 9234  C CA  . ASP E 1 173 ? 153.597 -37.800 40.292  1.000 39.170  ? 190 ASP EEE CA  1 
ATOM 9235  C C   . ASP E 1 173 ? 152.892 -38.199 38.998  1.000 43.290  ? 190 ASP EEE C   1 
ATOM 9236  O O   . ASP E 1 173 ? 153.372 -39.130 38.357  1.000 47.040  ? 190 ASP EEE O   1 
ATOM 9237  C CB  . ASP E 1 173 ? 153.750 -39.030 41.188  1.000 41.820  ? 190 ASP EEE CB  1 
ATOM 9238  C CG  . ASP E 1 173 ? 152.439 -39.578 41.745  1.000 40.910  ? 190 ASP EEE CG  1 
ATOM 9239  O OD1 . ASP E 1 173 ? 151.361 -39.226 41.215  1.000 40.350  ? 190 ASP EEE OD1 1 
ATOM 9240  O OD2 . ASP E 1 173 ? 152.513 -40.349 42.716  1.000 39.400  ? 190 ASP EEE OD2 1 
ATOM 9241  N N   . LYS E 1 174 ? 151.802 -37.520 38.621  1.000 47.570  ? 191 LYS EEE N   1 
ATOM 9242  C CA  . LYS E 1 174 ? 150.971 -37.910 37.455  1.000 45.800  ? 191 LYS EEE CA  1 
ATOM 9243  C C   . LYS E 1 174 ? 150.244 -36.689 36.861  1.000 44.840  ? 191 LYS EEE C   1 
ATOM 9244  O O   . LYS E 1 174 ? 149.745 -35.816 37.615  1.000 46.780  ? 191 LYS EEE O   1 
ATOM 9245  C CB  . LYS E 1 174 ? 150.017 -39.024 37.881  1.000 47.730  ? 191 LYS EEE CB  1 
ATOM 9246  C CG  . LYS E 1 174 ? 149.378 -39.767 36.722  1.000 55.660  ? 191 LYS EEE CG  1 
ATOM 9247  C CD  . LYS E 1 174 ? 148.355 -40.805 37.175  1.000 58.830  ? 191 LYS EEE CD  1 
ATOM 9248  C CE  . LYS E 1 174 ? 147.811 -41.660 36.053  1.000 56.800  ? 191 LYS EEE CE  1 
ATOM 9249  N NZ  . LYS E 1 174 ? 146.372 -41.949 36.261  1.000 60.570  ? 191 LYS EEE NZ  1 
ATOM 9250  N N   . ASN E 1 175 ? 150.160 -36.637 35.539  1.000 43.210  ? 192 ASN EEE N   1 
ATOM 9251  C CA  . ASN E 1 175 ? 149.486 -35.537 34.811  1.000 41.680  ? 192 ASN EEE CA  1 
ATOM 9252  C C   . ASN E 1 175 ? 148.013 -35.862 34.611  1.000 36.480  ? 192 ASN EEE C   1 
ATOM 9253  O O   . ASN E 1 175 ? 147.636 -37.033 34.724  1.000 34.850  ? 192 ASN EEE O   1 
ATOM 9254  C CB  . ASN E 1 175 ? 150.164 -35.253 33.479  1.000 45.190  ? 192 ASN EEE CB  1 
ATOM 9255  C CG  . ASN E 1 175 ? 151.034 -34.030 33.585  1.000 49.490  ? 192 ASN EEE CG  1 
ATOM 9256  O OD1 . ASN E 1 175 ? 150.548 -32.900 33.429  1.000 51.850  ? 192 ASN EEE OD1 1 
ATOM 9257  N ND2 . ASN E 1 175 ? 152.295 -34.265 33.910  1.000 46.890  ? 192 ASN EEE ND2 1 
ATOM 9258  N N   . LYS E 1 176 ? 147.219 -34.836 34.332  1.000 35.120  ? 193 LYS EEE N   1 
ATOM 9259  C CA  . LYS E 1 176 ? 145.770 -34.963 34.072  1.000 37.240  ? 193 LYS EEE CA  1 
ATOM 9260  C C   . LYS E 1 176 ? 145.128 -35.681 35.255  1.000 35.360  ? 193 LYS EEE C   1 
ATOM 9261  O O   . LYS E 1 176 ? 144.025 -36.224 35.066  1.000 35.250  ? 193 LYS EEE O   1 
ATOM 9262  C CB  . LYS E 1 176 ? 145.539 -35.710 32.762  1.000 42.040  ? 193 LYS EEE CB  1 
ATOM 9263  C CG  . LYS E 1 176 ? 146.107 -35.031 31.536  1.000 52.050  ? 193 LYS EEE CG  1 
ATOM 9264  C CD  . LYS E 1 176 ? 145.849 -35.735 30.175  1.000 63.390  ? 193 LYS EEE CD  1 
ATOM 9265  C CE  . LYS E 1 176 ? 144.431 -36.201 29.829  1.000 71.260  ? 193 LYS EEE CE  1 
ATOM 9266  N NZ  . LYS E 1 176 ? 143.415 -35.117 29.832  1.000 75.580  ? 193 LYS EEE NZ  1 
ATOM 9267  N N   . ALA E 1 177 ? 145.760 -35.625 36.432  1.000 35.950  ? 194 ALA EEE N   1 
ATOM 9268  C CA  . ALA E 1 177 ? 145.432 -36.498 37.587  1.000 33.530  ? 194 ALA EEE CA  1 
ATOM 9269  C C   . ALA E 1 177 ? 144.913 -35.689 38.778  1.000 31.700  ? 194 ALA EEE C   1 
ATOM 9270  O O   . ALA E 1 177 ? 143.780 -35.959 39.207  1.000 30.450  ? 194 ALA EEE O   1 
ATOM 9271  C CB  . ALA E 1 177 ? 146.644 -37.301 37.986  1.000 34.650  ? 194 ALA EEE CB  1 
ATOM 9272  N N   . TYR E 1 178 ? 145.705 -34.748 39.298  1.000 29.140  ? 195 TYR EEE N   1 
ATOM 9273  C CA  . TYR E 1 178 ? 145.421 -34.071 40.588  1.000 27.460  ? 195 TYR EEE CA  1 
ATOM 9274  C C   . TYR E 1 178 ? 144.678 -32.765 40.337  1.000 27.520  ? 195 TYR EEE C   1 
ATOM 9275  O O   . TYR E 1 178 ? 145.281 -31.764 39.960  1.000 29.580  ? 195 TYR EEE O   1 
ATOM 9276  C CB  . TYR E 1 178 ? 146.722 -33.846 41.352  1.000 29.520  ? 195 TYR EEE CB  1 
ATOM 9277  C CG  . TYR E 1 178 ? 147.406 -35.110 41.803  1.000 32.140  ? 195 TYR EEE CG  1 
ATOM 9278  C CD1 . TYR E 1 178 ? 148.250 -35.809 40.959  1.000 34.650  ? 195 TYR EEE CD1 1 
ATOM 9279  C CD2 . TYR E 1 178 ? 147.220 -35.611 43.073  1.000 34.740  ? 195 TYR EEE CD2 1 
ATOM 9280  C CE1 . TYR E 1 178 ? 148.884 -36.970 41.361  1.000 33.830  ? 195 TYR EEE CE1 1 
ATOM 9281  C CE2 . TYR E 1 178 ? 147.840 -36.779 43.491  1.000 34.800  ? 195 TYR EEE CE2 1 
ATOM 9282  C CZ  . TYR E 1 178 ? 148.670 -37.468 42.633  1.000 34.120  ? 195 TYR EEE CZ  1 
ATOM 9283  O OH  . TYR E 1 178 ? 149.263 -38.624 43.060  1.000 33.160  ? 195 TYR EEE OH  1 
ATOM 9284  N N   . PRO E 1 179 ? 143.348 -32.713 40.564  1.000 26.570  ? 196 PRO EEE N   1 
ATOM 9285  C CA  . PRO E 1 179 ? 142.590 -31.485 40.379  1.000 26.540  ? 196 PRO EEE CA  1 
ATOM 9286  C C   . PRO E 1 179 ? 143.229 -30.339 41.175  1.000 26.210  ? 196 PRO EEE C   1 
ATOM 9287  O O   . PRO E 1 179 ? 143.712 -30.613 42.238  1.000 26.440  ? 196 PRO EEE O   1 
ATOM 9288  C CB  . PRO E 1 179 ? 141.198 -31.827 40.923  1.000 27.490  ? 196 PRO EEE CB  1 
ATOM 9289  C CG  . PRO E 1 179 ? 141.106 -33.300 40.747  1.000 28.590  ? 196 PRO EEE CG  1 
ATOM 9290  C CD  . PRO E 1 179 ? 142.501 -33.801 41.060  1.000 28.940  ? 196 PRO EEE CD  1 
ATOM 9291  N N   . VAL E 1 180 ? 143.177 -29.105 40.660  1.000 25.040  ? 197 VAL EEE N   1 
ATOM 9292  C CA  . VAL E 1 180 ? 143.815 -27.926 41.304  1.000 23.480  ? 197 VAL EEE CA  1 
ATOM 9293  C C   . VAL E 1 180 ? 143.048 -27.592 42.583  1.000 22.370  ? 197 VAL EEE C   1 
ATOM 9294  O O   . VAL E 1 180 ? 143.685 -27.203 43.562  1.000 20.970  ? 197 VAL EEE O   1 
ATOM 9295  C CB  . VAL E 1 180 ? 143.872 -26.727 40.343  1.000 24.940  ? 197 VAL EEE CB  1 
ATOM 9296  C CG1 . VAL E 1 180 ? 144.429 -25.489 41.029  1.000 26.040  ? 197 VAL EEE CG1 1 
ATOM 9297  C CG2 . VAL E 1 180 ? 144.673 -27.038 39.088  1.000 24.640  ? 197 VAL EEE CG2 1 
ATOM 9298  N N   . GLU E 1 181 ? 141.733 -27.779 42.577  1.000 24.350  ? 198 GLU EEE N   1 
ATOM 9299  C CA  . GLU E 1 181 ? 140.803 -27.187 43.574  1.000 26.480  ? 198 GLU EEE CA  1 
ATOM 9300  C C   . GLU E 1 181 ? 140.766 -28.000 44.870  1.000 30.570  ? 198 GLU EEE C   1 
ATOM 9301  O O   . GLU E 1 181 ? 139.990 -27.626 45.773  1.000 33.430  ? 198 GLU EEE O   1 
ATOM 9302  C CB  . GLU E 1 181 ? 139.405 -27.063 42.955  1.000 27.220  ? 198 GLU EEE CB  1 
ATOM 9303  C CG  . GLU E 1 181 ? 138.572 -28.337 42.850  1.000 25.450  ? 198 GLU EEE CG  1 
ATOM 9304  C CD  . GLU E 1 181 ? 137.120 -28.044 42.432  1.000 24.650  ? 198 GLU EEE CD  1 
ATOM 9305  O OE1 . GLU E 1 181 ? 136.915 -27.162 41.584  1.000 27.080  ? 198 GLU EEE OE1 1 
ATOM 9306  O OE2 . GLU E 1 181 ? 136.176 -28.688 42.953  1.000 21.270  ? 198 GLU EEE OE2 1 
ATOM 9307  N N   . CYS E 1 182 ? 141.511 -29.103 44.972  1.000 34.260  ? 199 CYS EEE N   1 
ATOM 9308  C CA  . CYS E 1 182 ? 141.468 -29.956 46.187  1.000 35.980  ? 199 CYS EEE CA  1 
ATOM 9309  C C   . CYS E 1 182 ? 142.877 -30.334 46.642  1.000 33.320  ? 199 CYS EEE C   1 
ATOM 9310  O O   . CYS E 1 182 ? 142.990 -31.077 47.639  1.000 32.450  ? 199 CYS EEE O   1 
ATOM 9311  C CB  . CYS E 1 182 ? 140.560 -31.168 45.993  1.000 38.460  ? 199 CYS EEE CB  1 
ATOM 9312  S SG  . CYS E 1 182 ? 140.933 -32.197 44.549  1.000 44.590  ? 199 CYS EEE SG  1 
ATOM 9313  N N   . TRP E 1 183 ? 143.908 -29.772 46.015  1.000 31.850  ? 200 TRP EEE N   1 
ATOM 9314  C CA  . TRP E 1 183 ? 145.325 -30.018 46.398  1.000 32.090  ? 200 TRP EEE CA  1 
ATOM 9315  C C   . TRP E 1 183 ? 146.099 -28.707 46.440  1.000 28.660  ? 200 TRP EEE C   1 
ATOM 9316  O O   . TRP E 1 183 ? 145.903 -27.879 45.542  1.000 27.810  ? 200 TRP EEE O   1 
ATOM 9317  C CB  . TRP E 1 183 ? 146.003 -30.995 45.428  1.000 33.170  ? 200 TRP EEE CB  1 
ATOM 9318  C CG  . TRP E 1 183 ? 145.405 -32.365 45.383  1.000 31.500  ? 200 TRP EEE CG  1 
ATOM 9319  C CD1 . TRP E 1 183 ? 144.646 -32.915 44.390  1.000 31.160  ? 200 TRP EEE CD1 1 
ATOM 9320  C CD2 . TRP E 1 183 ? 145.547 -33.371 46.388  1.000 30.540  ? 200 TRP EEE CD2 1 
ATOM 9321  N NE1 . TRP E 1 183 ? 144.308 -34.196 44.706  1.000 30.530  ? 200 TRP EEE NE1 1 
ATOM 9322  C CE2 . TRP E 1 183 ? 144.855 -34.507 45.919  1.000 31.370  ? 200 TRP EEE CE2 1 
ATOM 9323  C CE3 . TRP E 1 183 ? 146.170 -33.410 47.637  1.000 30.540  ? 200 TRP EEE CE3 1 
ATOM 9324  C CZ2 . TRP E 1 183 ? 144.765 -35.673 46.667  1.000 32.690  ? 200 TRP EEE CZ2 1 
ATOM 9325  C CZ3 . TRP E 1 183 ? 146.087 -34.563 48.381  1.000 31.330  ? 200 TRP EEE CZ3 1 
ATOM 9326  C CH2 . TRP E 1 183 ? 145.389 -35.672 47.897  1.000 33.940  ? 200 TRP EEE CH2 1 
ATOM 9327  N N   . VAL E 1 184 ? 146.980 -28.564 47.423  1.000 28.290  ? 201 VAL EEE N   1 
ATOM 9328  C CA  . VAL E 1 184 ? 147.942 -27.434 47.518  1.000 28.570  ? 201 VAL EEE CA  1 
ATOM 9329  C C   . VAL E 1 184 ? 149.288 -27.991 47.938  1.000 26.570  ? 201 VAL EEE C   1 
ATOM 9330  O O   . VAL E 1 184 ? 149.369 -29.069 48.510  1.000 23.410  ? 201 VAL EEE O   1 
ATOM 9331  C CB  . VAL E 1 184 ? 147.447 -26.392 48.523  1.000 31.780  ? 201 VAL EEE CB  1 
ATOM 9332  C CG1 . VAL E 1 184 ? 146.083 -25.852 48.109  1.000 33.640  ? 201 VAL EEE CG1 1 
ATOM 9333  C CG2 . VAL E 1 184 ? 147.392 -26.960 49.932  1.000 32.340  ? 201 VAL EEE CG2 1 
ATOM 9334  N N   . PRO E 1 185 ? 150.390 -27.277 47.659  1.000 28.200  ? 202 PRO EEE N   1 
ATOM 9335  C CA  . PRO E 1 185 ? 151.687 -27.654 48.207  1.000 32.320  ? 202 PRO EEE CA  1 
ATOM 9336  C C   . PRO E 1 185 ? 151.526 -27.812 49.724  1.000 35.150  ? 202 PRO EEE C   1 
ATOM 9337  O O   . PRO E 1 185 ? 150.889 -26.935 50.331  1.000 42.700  ? 202 PRO EEE O   1 
ATOM 9338  C CB  . PRO E 1 185 ? 152.611 -26.487 47.810  1.000 31.000  ? 202 PRO EEE CB  1 
ATOM 9339  C CG  . PRO E 1 185 ? 151.970 -25.933 46.564  1.000 29.070  ? 202 PRO EEE CG  1 
ATOM 9340  C CD  . PRO E 1 185 ? 150.473 -26.106 46.784  1.000 28.800  ? 202 PRO EEE CD  1 
ATOM 9341  N N   . ASP E 1 186 ? 152.073 -28.904 50.270  1.000 31.200  ? 203 ASP EEE N   1 
ATOM 9342  C CA  . ASP E 1 186 ? 152.026 -29.246 51.715  1.000 30.040  ? 203 ASP EEE CA  1 
ATOM 9343  C C   . ASP E 1 186 ? 153.187 -28.529 52.376  1.000 28.440  ? 203 ASP EEE C   1 
ATOM 9344  O O   . ASP E 1 186 ? 154.328 -28.898 52.174  1.000 28.230  ? 203 ASP EEE O   1 
ATOM 9345  C CB  . ASP E 1 186 ? 152.120 -30.756 51.945  1.000 30.750  ? 203 ASP EEE CB  1 
ATOM 9346  C CG  . ASP E 1 186 ? 152.119 -31.198 53.406  1.000 29.390  ? 203 ASP EEE CG  1 
ATOM 9347  O OD1 . ASP E 1 186 ? 152.133 -30.328 54.288  1.000 28.520  ? 203 ASP EEE OD1 1 
ATOM 9348  O OD2 . ASP E 1 186 ? 152.133 -32.417 53.639  1.000 30.050  ? 203 ASP EEE OD2 1 
ATOM 9349  N N   . PRO E 1 187 ? 152.934 -27.486 53.181  1.000 29.190  ? 204 PRO EEE N   1 
ATOM 9350  C CA  . PRO E 1 187 ? 154.000 -26.616 53.655  1.000 32.170  ? 204 PRO EEE CA  1 
ATOM 9351  C C   . PRO E 1 187 ? 154.797 -27.297 54.761  1.000 35.120  ? 204 PRO EEE C   1 
ATOM 9352  O O   . PRO E 1 187 ? 155.843 -26.797 55.086  1.000 37.360  ? 204 PRO EEE O   1 
ATOM 9353  C CB  . PRO E 1 187 ? 153.237 -25.424 54.231  1.000 34.960  ? 204 PRO EEE CB  1 
ATOM 9354  C CG  . PRO E 1 187 ? 151.938 -26.043 54.727  1.000 33.020  ? 204 PRO EEE CG  1 
ATOM 9355  C CD  . PRO E 1 187 ? 151.614 -27.107 53.703  1.000 30.830  ? 204 PRO EEE CD  1 
ATOM 9356  N N   . THR E 1 188 ? 154.264 -28.397 55.301  1.000 41.320  ? 205 THR EEE N   1 
ATOM 9357  C CA  . THR E 1 188 ? 154.882 -29.211 56.383  1.000 40.960  ? 205 THR EEE CA  1 
ATOM 9358  C C   . THR E 1 188 ? 155.913 -30.169 55.769  1.000 40.290  ? 205 THR EEE C   1 
ATOM 9359  O O   . THR E 1 188 ? 156.587 -30.843 56.560  1.000 40.960  ? 205 THR EEE O   1 
ATOM 9360  C CB  . THR E 1 188 ? 153.838 -30.029 57.161  1.000 37.090  ? 205 THR EEE CB  1 
ATOM 9361  O OG1 . THR E 1 188 ? 153.462 -31.130 56.336  1.000 38.930  ? 205 THR EEE OG1 1 
ATOM 9362  C CG2 . THR E 1 188 ? 152.604 -29.246 57.549  1.000 35.950  ? 205 THR EEE CG2 1 
ATOM 9363  N N   . ARG E 1 189 ? 155.984 -30.189 54.442  1.000 37.360  ? 206 ARG EEE N   1 
ATOM 9364  C CA  . ARG E 1 189 ? 156.981 -31.060 53.812  1.000 43.940  ? 206 ARG EEE CA  1 
ATOM 9365  C C   . ARG E 1 189 ? 157.272 -30.774 52.352  1.000 48.430  ? 206 ARG EEE C   1 
ATOM 9366  O O   . ARG E 1 189 ? 156.706 -31.469 51.545  1.000 74.240  ? 206 ARG EEE O   1 
ATOM 9367  C CB  . ARG E 1 189 ? 156.625 -32.544 53.929  1.000 51.190  ? 206 ARG EEE CB  1 
ATOM 9368  C CG  . ARG E 1 189 ? 155.154 -32.917 53.891  1.000 55.530  ? 206 ARG EEE CG  1 
ATOM 9369  C CD  . ARG E 1 189 ? 154.967 -34.419 53.828  1.000 62.600  ? 206 ARG EEE CD  1 
ATOM 9370  N NE  . ARG E 1 189 ? 154.364 -34.950 55.040  1.000 67.310  ? 206 ARG EEE NE  1 
ATOM 9371  C CZ  . ARG E 1 189 ? 153.736 -36.115 55.117  1.000 64.500  ? 206 ARG EEE CZ  1 
ATOM 9372  N NH1 . ARG E 1 189 ? 153.217 -36.513 56.265  1.000 61.890  ? 206 ARG EEE NH1 1 
ATOM 9373  N NH2 . ARG E 1 189 ? 153.627 -36.879 54.046  1.000 63.440  ? 206 ARG EEE NH2 1 
ATOM 9374  N N   . ASN E 1 190 ? 158.024 -29.728 52.013  1.000 42.900  ? 207 ASN EEE N   1 
ATOM 9375  C CA  . ASN E 1 190 ? 158.592 -29.661 50.638  1.000 43.530  ? 207 ASN EEE CA  1 
ATOM 9376  C C   . ASN E 1 190 ? 160.007 -29.143 50.805  1.000 48.380  ? 207 ASN EEE C   1 
ATOM 9377  O O   . ASN E 1 190 ? 160.316 -28.141 50.197  1.000 49.250  ? 207 ASN EEE O   1 
ATOM 9378  C CB  . ASN E 1 190 ? 157.655 -28.841 49.763  1.000 41.410  ? 207 ASN EEE CB  1 
ATOM 9379  C CG  . ASN E 1 190 ? 156.604 -29.645 49.012  1.000 40.550  ? 207 ASN EEE CG  1 
ATOM 9380  O OD1 . ASN E 1 190 ? 156.930 -30.397 48.080  1.000 37.090  ? 207 ASN EEE OD1 1 
ATOM 9381  N ND2 . ASN E 1 190 ? 155.330 -29.430 49.361  1.000 37.490  ? 207 ASN EEE ND2 1 
ATOM 9382  N N   . GLU E 1 191 ? 160.757 -29.743 51.722  1.000 54.840  ? 208 GLU EEE N   1 
ATOM 9383  C CA  . GLU E 1 191 ? 162.139 -29.315 52.058  1.000 56.000  ? 208 GLU EEE CA  1 
ATOM 9384  C C   . GLU E 1 191 ? 162.955 -29.207 50.752  1.000 47.190  ? 208 GLU EEE C   1 
ATOM 9385  O O   . GLU E 1 191 ? 163.682 -28.228 50.590  1.000 47.420  ? 208 GLU EEE O   1 
ATOM 9386  C CB  . GLU E 1 191 ? 162.767 -30.280 53.069  1.000 67.780  ? 208 GLU EEE CB  1 
ATOM 9387  C CG  . GLU E 1 191 ? 164.216 -29.927 53.374  1.000 78.380  ? 208 GLU EEE CG  1 
ATOM 9388  C CD  . GLU E 1 191 ? 164.872 -30.710 54.498  1.000 81.510  ? 208 GLU EEE CD  1 
ATOM 9389  O OE1 . GLU E 1 191 ? 164.831 -31.966 54.428  1.000 82.730  ? 208 GLU EEE OE1 1 
ATOM 9390  O OE2 . GLU E 1 191 ? 165.442 -30.066 55.433  1.000 76.330  ? 208 GLU EEE OE2 1 
ATOM 9391  N N   . ASN E 1 192 ? 162.780 -30.156 49.833  1.000 44.420  ? 209 ASN EEE N   1 
ATOM 9392  C CA  . ASN E 1 192 ? 163.624 -30.347 48.622  1.000 40.680  ? 209 ASN EEE CA  1 
ATOM 9393  C C   . ASN E 1 192 ? 162.968 -29.722 47.372  1.000 37.540  ? 209 ASN EEE C   1 
ATOM 9394  O O   . ASN E 1 192 ? 163.402 -30.009 46.253  1.000 30.520  ? 209 ASN EEE O   1 
ATOM 9395  C CB  . ASN E 1 192 ? 163.911 -31.837 48.424  1.000 41.140  ? 209 ASN EEE CB  1 
ATOM 9396  C CG  . ASN E 1 192 ? 165.079 -32.086 47.493  1.000 43.660  ? 209 ASN EEE CG  1 
ATOM 9397  O OD1 . ASN E 1 192 ? 165.948 -31.229 47.325  1.000 42.140  ? 209 ASN EEE OD1 1 
ATOM 9398  N ND2 . ASN E 1 192 ? 165.101 -33.259 46.881  1.000 46.750  ? 209 ASN EEE ND2 1 
ATOM 9399  N N   . THR E 1 193 ? 161.970 -28.867 47.551  1.000 40.710  ? 210 THR EEE N   1 
ATOM 9400  C CA  . THR E 1 193 ? 161.263 -28.160 46.451  1.000 40.410  ? 210 THR EEE CA  1 
ATOM 9401  C C   . THR E 1 193 ? 161.196 -26.663 46.789  1.000 40.180  ? 210 THR EEE C   1 
ATOM 9402  O O   . THR E 1 193 ? 161.220 -26.316 47.987  1.000 44.110  ? 210 THR EEE O   1 
ATOM 9403  C CB  . THR E 1 193 ? 159.882 -28.779 46.217  1.000 41.030  ? 210 THR EEE CB  1 
ATOM 9404  O OG1 . THR E 1 193 ? 160.007 -30.090 45.660  1.000 42.850  ? 210 THR EEE OG1 1 
ATOM 9405  C CG2 . THR E 1 193 ? 159.051 -27.930 45.288  1.000 43.300  ? 210 THR EEE CG2 1 
ATOM 9406  N N   . ARG E 1 194 ? 161.189 -25.805 45.772  1.000 35.670  ? 211 ARG EEE N   1 
ATOM 9407  C CA  . ARG E 1 194 ? 160.921 -24.352 45.904  1.000 34.800  ? 211 ARG EEE CA  1 
ATOM 9408  C C   . ARG E 1 194 ? 159.631 -24.075 45.146  1.000 35.490  ? 211 ARG EEE C   1 
ATOM 9409  O O   . ARG E 1 194 ? 159.635 -24.283 43.940  1.000 40.940  ? 211 ARG EEE O   1 
ATOM 9410  C CB  . ARG E 1 194 ? 162.058 -23.520 45.322  1.000 33.180  ? 211 ARG EEE CB  1 
ATOM 9411  C CG  . ARG E 1 194 ? 163.423 -23.889 45.865  1.000 34.570  ? 211 ARG EEE CG  1 
ATOM 9412  C CD  . ARG E 1 194 ? 163.533 -23.578 47.340  1.000 38.560  ? 211 ARG EEE CD  1 
ATOM 9413  N NE  . ARG E 1 194 ? 164.868 -23.909 47.798  1.000 39.210  ? 211 ARG EEE NE  1 
ATOM 9414  C CZ  . ARG E 1 194 ? 165.226 -25.076 48.291  1.000 38.330  ? 211 ARG EEE CZ  1 
ATOM 9415  N NH1 . ARG E 1 194 ? 164.329 -26.029 48.431  1.000 36.840  ? 211 ARG EEE NH1 1 
ATOM 9416  N NH2 . ARG E 1 194 ? 166.479 -25.275 48.662  1.000 41.740  ? 211 ARG EEE NH2 1 
ATOM 9417  N N   . TYR E 1 195 ? 158.554 -23.716 45.835  1.000 33.270  ? 212 TYR EEE N   1 
ATOM 9418  C CA  . TYR E 1 195 ? 157.225 -23.531 45.212  1.000 30.440  ? 212 TYR EEE CA  1 
ATOM 9419  C C   . TYR E 1 195 ? 156.787 -22.087 45.450  1.000 27.670  ? 212 TYR EEE C   1 
ATOM 9420  O O   . TYR E 1 195 ? 157.124 -21.498 46.473  1.000 25.310  ? 212 TYR EEE O   1 
ATOM 9421  C CB  . TYR E 1 195 ? 156.231 -24.577 45.720  1.000 30.340  ? 212 TYR EEE CB  1 
ATOM 9422  C CG  . TYR E 1 195 ? 155.762 -24.427 47.143  1.000 30.570  ? 212 TYR EEE CG  1 
ATOM 9423  C CD1 . TYR E 1 195 ? 154.737 -23.562 47.479  1.000 32.030  ? 212 TYR EEE CD1 1 
ATOM 9424  C CD2 . TYR E 1 195 ? 156.319 -25.183 48.154  1.000 30.030  ? 212 TYR EEE CD2 1 
ATOM 9425  C CE1 . TYR E 1 195 ? 154.294 -23.435 48.789  1.000 32.520  ? 212 TYR EEE CE1 1 
ATOM 9426  C CE2 . TYR E 1 195 ? 155.875 -25.079 49.462  1.000 32.190  ? 212 TYR EEE CE2 1 
ATOM 9427  C CZ  . TYR E 1 195 ? 154.862 -24.196 49.791  1.000 31.770  ? 212 TYR EEE CZ  1 
ATOM 9428  O OH  . TYR E 1 195 ? 154.430 -24.091 51.085  1.000 29.970  ? 212 TYR EEE OH  1 
ATOM 9429  N N   . PHE E 1 196 ? 156.085 -21.546 44.466  1.000 26.790  ? 213 PHE EEE N   1 
ATOM 9430  C CA  . PHE E 1 196 ? 155.547 -20.173 44.435  1.000 24.860  ? 213 PHE EEE CA  1 
ATOM 9431  C C   . PHE E 1 196 ? 154.228 -20.183 43.672  1.000 24.110  ? 213 PHE EEE C   1 
ATOM 9432  O O   . PHE E 1 196 ? 154.188 -20.705 42.552  1.000 24.020  ? 213 PHE EEE O   1 
ATOM 9433  C CB  . PHE E 1 196 ? 156.494 -19.241 43.699  1.000 24.360  ? 213 PHE EEE CB  1 
ATOM 9434  C CG  . PHE E 1 196 ? 157.953 -19.394 44.011  1.000 24.680  ? 213 PHE EEE CG  1 
ATOM 9435  C CD1 . PHE E 1 196 ? 158.704 -20.344 43.352  1.000 26.480  ? 213 PHE EEE CD1 1 
ATOM 9436  C CD2 . PHE E 1 196 ? 158.582 -18.549 44.911  1.000 24.470  ? 213 PHE EEE CD2 1 
ATOM 9437  C CE1 . PHE E 1 196 ? 160.065 -20.454 43.600  1.000 28.210  ? 213 PHE EEE CE1 1 
ATOM 9438  C CE2 . PHE E 1 196 ? 159.938 -18.660 45.158  1.000 25.290  ? 213 PHE EEE CE2 1 
ATOM 9439  C CZ  . PHE E 1 196 ? 160.687 -19.584 44.476  1.000 27.030  ? 213 PHE EEE CZ  1 
ATOM 9440  N N   . GLY E 1 197 ? 153.183 -19.641 44.278  1.000 23.690  ? 214 GLY EEE N   1 
ATOM 9441  C CA  . GLY E 1 197 ? 151.863 -19.555 43.645  1.000 23.530  ? 214 GLY EEE CA  1 
ATOM 9442  C C   . GLY E 1 197 ? 151.060 -18.394 44.193  1.000 23.570  ? 214 GLY EEE C   1 
ATOM 9443  O O   . GLY E 1 197 ? 151.403 -17.859 45.279  1.000 22.850  ? 214 GLY EEE O   1 
ATOM 9444  N N   . THR E 1 198 ? 150.031 -18.006 43.445  1.000 22.620  ? 215 THR EEE N   1 
ATOM 9445  C CA  . THR E 1 198 ? 149.118 -16.916 43.833  1.000 21.760  ? 215 THR EEE CA  1 
ATOM 9446  C C   . THR E 1 198 ? 147.725 -17.258 43.357  1.000 20.860  ? 215 THR EEE C   1 
ATOM 9447  O O   . THR E 1 198 ? 147.588 -17.543 42.155  1.000 20.480  ? 215 THR EEE O   1 
ATOM 9448  C CB  . THR E 1 198 ? 149.520 -15.581 43.206  1.000 21.140  ? 215 THR EEE CB  1 
ATOM 9449  O OG1 . THR E 1 198 ? 150.875 -15.313 43.573  1.000 20.080  ? 215 THR EEE OG1 1 
ATOM 9450  C CG2 . THR E 1 198 ? 148.549 -14.494 43.607  1.000 20.330  ? 215 THR EEE CG2 1 
ATOM 9451  N N   . LEU E 1 199 ? 146.748 -17.227 44.264  1.000 21.260  ? 216 LEU EEE N   1 
ATOM 9452  C CA  . LEU E 1 199 ? 145.319 -17.258 43.876  1.000 21.180  ? 216 LEU EEE CA  1 
ATOM 9453  C C   . LEU E 1 199 ? 144.793 -15.844 43.923  1.000 21.180  ? 216 LEU EEE C   1 
ATOM 9454  O O   . LEU E 1 199 ? 144.915 -15.220 44.993  1.000 20.650  ? 216 LEU EEE O   1 
ATOM 9455  C CB  . LEU E 1 199 ? 144.485 -18.131 44.801  1.000 20.430  ? 216 LEU EEE CB  1 
ATOM 9456  C CG  . LEU E 1 199 ? 143.021 -18.147 44.409  1.000 20.180  ? 216 LEU EEE CG  1 
ATOM 9457  C CD1 . LEU E 1 199 ? 142.543 -19.554 44.256  1.000 22.330  ? 216 LEU EEE CD1 1 
ATOM 9458  C CD2 . LEU E 1 199 ? 142.196 -17.416 45.433  1.000 20.790  ? 216 LEU EEE CD2 1 
ATOM 9459  N N   . THR E 1 200 ? 144.236 -15.387 42.797  1.000 21.260  ? 217 THR EEE N   1 
ATOM 9460  C CA  . THR E 1 200 ? 143.332 -14.218 42.733  1.000 20.440  ? 217 THR EEE CA  1 
ATOM 9461  C C   . THR E 1 200 ? 141.917 -14.691 42.406  1.000 21.800  ? 217 THR EEE C   1 
ATOM 9462  O O   . THR E 1 200 ? 141.719 -15.197 41.285  1.000 23.690  ? 217 THR EEE O   1 
ATOM 9463  C CB  . THR E 1 200 ? 143.872 -13.209 41.734  1.000 18.480  ? 217 THR EEE CB  1 
ATOM 9464  O OG1 . THR E 1 200 ? 145.250 -13.006 42.038  1.000 18.470  ? 217 THR EEE OG1 1 
ATOM 9465  C CG2 . THR E 1 200 ? 143.132 -11.906 41.827  1.000 17.730  ? 217 THR EEE CG2 1 
ATOM 9466  N N   . GLY E 1 201 ? 140.973 -14.536 43.340  1.000 23.490  ? 218 GLY EEE N   1 
ATOM 9467  C CA  . GLY E 1 201 ? 139.566 -14.961 43.164  1.000 26.400  ? 218 GLY EEE CA  1 
ATOM 9468  C C   . GLY E 1 201 ? 138.677 -13.785 42.788  1.000 28.600  ? 218 GLY EEE C   1 
ATOM 9469  O O   . GLY E 1 201 ? 139.002 -12.674 43.195  1.000 31.400  ? 218 GLY EEE O   1 
ATOM 9470  N N   . GLY E 1 202 ? 137.603 -14.014 42.034  1.000 30.650  ? 219 GLY EEE N   1 
ATOM 9471  C CA  . GLY E 1 202 ? 136.676 -12.952 41.591  1.000 32.660  ? 219 GLY EEE CA  1 
ATOM 9472  C C   . GLY E 1 202 ? 136.393 -13.063 40.106  1.000 33.640  ? 219 GLY EEE C   1 
ATOM 9473  O O   . GLY E 1 202 ? 137.348 -13.289 39.324  1.000 30.080  ? 219 GLY EEE O   1 
ATOM 9474  N N   . GLU E 1 203 ? 135.118 -12.905 39.725  1.000 33.390  ? 220 GLU EEE N   1 
ATOM 9475  C CA  . GLU E 1 203 ? 134.642 -13.157 38.342  1.000 31.530  ? 220 GLU EEE CA  1 
ATOM 9476  C C   . GLU E 1 203 ? 135.219 -12.098 37.399  1.000 29.960  ? 220 GLU EEE C   1 
ATOM 9477  O O   . GLU E 1 203 ? 135.355 -12.404 36.219  1.000 34.080  ? 220 GLU EEE O   1 
ATOM 9478  C CB  . GLU E 1 203 ? 133.110 -13.277 38.294  1.000 33.300  ? 220 GLU EEE CB  1 
ATOM 9479  C CG  . GLU E 1 203 ? 132.319 -12.056 38.714  1.000 33.820  ? 220 GLU EEE CG  1 
ATOM 9480  C CD  . GLU E 1 203 ? 131.898 -12.009 40.166  1.000 34.120  ? 220 GLU EEE CD  1 
ATOM 9481  O OE1 . GLU E 1 203 ? 132.676 -12.493 40.999  1.000 36.400  ? 220 GLU EEE OE1 1 
ATOM 9482  O OE2 . GLU E 1 203 ? 130.788 -11.488 40.451  1.000 31.160  ? 220 GLU EEE OE2 1 
ATOM 9483  N N   . ASN E 1 204 ? 135.616 -10.935 37.910  1.000 30.220  ? 221 ASN EEE N   1 
ATOM 9484  C CA  . ASN E 1 204 ? 136.040 -9.775  37.089  1.000 29.630  ? 221 ASN EEE CA  1 
ATOM 9485  C C   . ASN E 1 204 ? 137.538 -9.510  37.253  1.000 28.080  ? 221 ASN EEE C   1 
ATOM 9486  O O   . ASN E 1 204 ? 138.041 -8.517  36.693  1.000 30.310  ? 221 ASN EEE O   1 
ATOM 9487  C CB  . ASN E 1 204 ? 135.180 -8.566  37.437  1.000 31.080  ? 221 ASN EEE CB  1 
ATOM 9488  C CG  . ASN E 1 204 ? 133.744 -8.813  37.060  1.000 32.710  ? 221 ASN EEE CG  1 
ATOM 9489  O OD1 . ASN E 1 204 ? 133.496 -9.280  35.958  1.000 34.440  ? 221 ASN EEE OD1 1 
ATOM 9490  N ND2 . ASN E 1 204 ? 132.818 -8.571  37.981  1.000 35.510  ? 221 ASN EEE ND2 1 
ATOM 9491  N N   . VAL E 1 205 ? 138.258 -10.374 37.946  1.000 25.120  ? 222 VAL EEE N   1 
ATOM 9492  C CA  . VAL E 1 205 ? 139.712 -10.159 38.150  1.000 23.570  ? 222 VAL EEE CA  1 
ATOM 9493  C C   . VAL E 1 205 ? 140.358 -10.058 36.780  1.000 21.840  ? 222 VAL EEE C   1 
ATOM 9494  O O   . VAL E 1 205 ? 140.324 -11.015 36.009  1.000 20.600  ? 222 VAL EEE O   1 
ATOM 9495  C CB  . VAL E 1 205 ? 140.365 -11.276 38.982  1.000 25.630  ? 222 VAL EEE CB  1 
ATOM 9496  C CG1 . VAL E 1 205 ? 141.860 -11.044 39.092  1.000 26.640  ? 222 VAL EEE CG1 1 
ATOM 9497  C CG2 . VAL E 1 205 ? 139.739 -11.435 40.368  1.000 26.010  ? 222 VAL EEE CG2 1 
ATOM 9498  N N   . PRO E 1 206 ? 141.010 -8.920  36.458  1.000 22.890  ? 223 PRO EEE N   1 
ATOM 9499  C CA  . PRO E 1 206 ? 141.774 -8.783  35.225  1.000 23.500  ? 223 PRO EEE CA  1 
ATOM 9500  C C   . PRO E 1 206 ? 143.056 -9.594  35.250  1.000 21.200  ? 223 PRO EEE C   1 
ATOM 9501  O O   . PRO E 1 206 ? 143.816 -9.477  36.202  1.000 22.730  ? 223 PRO EEE O   1 
ATOM 9502  C CB  . PRO E 1 206 ? 142.124 -7.295  35.163  1.000 23.240  ? 223 PRO EEE CB  1 
ATOM 9503  C CG  . PRO E 1 206 ? 142.244 -6.949  36.596  1.000 25.560  ? 223 PRO EEE CG  1 
ATOM 9504  C CD  . PRO E 1 206 ? 141.115 -7.708  37.270  1.000 25.050  ? 223 PRO EEE CD  1 
ATOM 9505  N N   . PRO E 1 207 ? 143.318 -10.401 34.197  1.000 19.840  ? 224 PRO EEE N   1 
ATOM 9506  C CA  . PRO E 1 207 ? 144.615 -11.021 33.986  1.000 20.470  ? 224 PRO EEE CA  1 
ATOM 9507  C C   . PRO E 1 207 ? 145.700 -9.957  33.925  1.000 19.350  ? 224 PRO EEE C   1 
ATOM 9508  O O   . PRO E 1 207 ? 145.465 -8.929  33.328  1.000 20.470  ? 224 PRO EEE O   1 
ATOM 9509  C CB  . PRO E 1 207 ? 144.525 -11.735 32.633  1.000 20.800  ? 224 PRO EEE CB  1 
ATOM 9510  C CG  . PRO E 1 207 ? 143.040 -11.939 32.447  1.000 21.330  ? 224 PRO EEE CG  1 
ATOM 9511  C CD  . PRO E 1 207 ? 142.397 -10.743 33.113  1.000 20.320  ? 224 PRO EEE CD  1 
ATOM 9512  N N   . VAL E 1 208 ? 146.820 -10.229 34.585  1.000 19.000  ? 225 VAL EEE N   1 
ATOM 9513  C CA  . VAL E 1 208 ? 148.022 -9.364  34.532  1.000 20.000  ? 225 VAL EEE CA  1 
ATOM 9514  C C   . VAL E 1 208 ? 149.228 -10.268 34.409  1.000 21.170  ? 225 VAL EEE C   1 
ATOM 9515  O O   . VAL E 1 208 ? 149.671 -10.769 35.417  1.000 23.750  ? 225 VAL EEE O   1 
ATOM 9516  C CB  . VAL E 1 208 ? 148.146 -8.467  35.761  1.000 19.120  ? 225 VAL EEE CB  1 
ATOM 9517  C CG1 . VAL E 1 208 ? 149.437 -7.678  35.693  1.000 19.040  ? 225 VAL EEE CG1 1 
ATOM 9518  C CG2 . VAL E 1 208 ? 146.943 -7.573  35.892  1.000 19.430  ? 225 VAL EEE CG2 1 
ATOM 9519  N N   . LEU E 1 209 ? 149.721 -10.444 33.195  1.000 23.320  ? 226 LEU EEE N   1 
ATOM 9520  C CA  . LEU E 1 209 ? 150.793 -11.396 32.880  1.000 24.440  ? 226 LEU EEE CA  1 
ATOM 9521  C C   . LEU E 1 209 ? 151.991 -10.606 32.349  1.000 25.490  ? 226 LEU EEE C   1 
ATOM 9522  O O   . LEU E 1 209 ? 151.871 -9.933  31.312  1.000 23.330  ? 226 LEU EEE O   1 
ATOM 9523  C CB  . LEU E 1 209 ? 150.189 -12.372 31.874  1.000 24.540  ? 226 LEU EEE CB  1 
ATOM 9524  C CG  . LEU E 1 209 ? 148.901 -13.028 32.364  1.000 23.550  ? 226 LEU EEE CG  1 
ATOM 9525  C CD1 . LEU E 1 209 ? 148.280 -13.918 31.301  1.000 24.120  ? 226 LEU EEE CD1 1 
ATOM 9526  C CD2 . LEU E 1 209 ? 149.161 -13.843 33.612  1.000 24.260  ? 226 LEU EEE CD2 1 
ATOM 9527  N N   . HIS E 1 210 ? 153.086 -10.638 33.104  1.000 27.540  ? 227 HIS EEE N   1 
ATOM 9528  C CA  . HIS E 1 210 ? 154.394 -10.069 32.702  1.000 32.710  ? 227 HIS EEE CA  1 
ATOM 9529  C C   . HIS E 1 210 ? 155.199 -11.145 31.981  1.000 31.750  ? 227 HIS EEE C   1 
ATOM 9530  O O   . HIS E 1 210 ? 155.154 -12.297 32.374  1.000 35.050  ? 227 HIS EEE O   1 
ATOM 9531  C CB  . HIS E 1 210 ? 155.128 -9.454  33.915  1.000 37.450  ? 227 HIS EEE CB  1 
ATOM 9532  C CG  . HIS E 1 210 ? 154.285 -8.473  34.664  1.000 41.890  ? 227 HIS EEE CG  1 
ATOM 9533  N ND1 . HIS E 1 210 ? 153.946 -7.224  34.149  1.000 44.180  ? 227 HIS EEE ND1 1 
ATOM 9534  C CD2 . HIS E 1 210 ? 153.657 -8.576  35.861  1.000 46.280  ? 227 HIS EEE CD2 1 
ATOM 9535  C CE1 . HIS E 1 210 ? 153.137 -6.613  34.994  1.000 48.480  ? 227 HIS EEE CE1 1 
ATOM 9536  N NE2 . HIS E 1 210 ? 152.944 -7.425  36.060  1.000 46.330  ? 227 HIS EEE NE2 1 
ATOM 9537  N N   . ILE E 1 211 ? 155.942 -10.745 30.965  1.000 32.200  ? 228 ILE EEE N   1 
ATOM 9538  C CA  . ILE E 1 211 ? 156.912 -11.605 30.231  1.000 32.280  ? 228 ILE EEE CA  1 
ATOM 9539  C C   . ILE E 1 211 ? 158.238 -10.847 30.187  1.000 31.040  ? 228 ILE EEE C   1 
ATOM 9540  O O   . ILE E 1 211 ? 158.217 -9.613  30.041  1.000 33.460  ? 228 ILE EEE O   1 
ATOM 9541  C CB  . ILE E 1 211 ? 156.358 -11.961 28.834  1.000 32.930  ? 228 ILE EEE CB  1 
ATOM 9542  C CG1 . ILE E 1 211 ? 156.218 -10.720 27.937  1.000 31.400  ? 228 ILE EEE CG1 1 
ATOM 9543  C CG2 . ILE E 1 211 ? 155.035 -12.701 28.982  1.000 35.830  ? 228 ILE EEE CG2 1 
ATOM 9544  C CD1 . ILE E 1 211 ? 155.504 -10.950 26.630  1.000 30.340  ? 228 ILE EEE CD1 1 
ATOM 9545  N N   . THR E 1 212 ? 159.355 -11.539 30.330  1.000 31.660  ? 229 THR EEE N   1 
ATOM 9546  C CA  . THR E 1 212 ? 160.705 -10.941 30.167  1.000 34.070  ? 229 THR EEE CA  1 
ATOM 9547  C C   . THR E 1 212 ? 161.760 -12.047 30.206  1.000 39.830  ? 229 THR EEE C   1 
ATOM 9548  O O   . THR E 1 212 ? 161.601 -13.013 31.002  1.000 44.940  ? 229 THR EEE O   1 
ATOM 9549  C CB  . THR E 1 212 ? 160.998 -9.888  31.244  1.000 28.910  ? 229 THR EEE CB  1 
ATOM 9550  O OG1 . THR E 1 212 ? 162.202 -9.213  30.926  1.000 25.820  ? 229 THR EEE OG1 1 
ATOM 9551  C CG2 . THR E 1 212 ? 161.169 -10.490 32.611  1.000 29.700  ? 229 THR EEE CG2 1 
ATOM 9552  N N   . ASN E 1 213 ? 162.818 -11.899 29.414  1.000 39.800  ? 230 ASN EEE N   1 
ATOM 9553  C CA  . ASN E 1 213 ? 163.951 -12.849 29.482  1.000 41.060  ? 230 ASN EEE CA  1 
ATOM 9554  C C   . ASN E 1 213 ? 165.057 -12.261 30.372  1.000 39.100  ? 230 ASN EEE C   1 
ATOM 9555  O O   . ASN E 1 213 ? 166.194 -12.716 30.250  1.000 36.770  ? 230 ASN EEE O   1 
ATOM 9556  C CB  . ASN E 1 213 ? 164.430 -13.232 28.077  1.000 41.690  ? 230 ASN EEE CB  1 
ATOM 9557  C CG  . ASN E 1 213 ? 164.919 -12.050 27.275  1.000 41.460  ? 230 ASN EEE CG  1 
ATOM 9558  O OD1 . ASN E 1 213 ? 164.760 -10.912 27.703  1.000 44.100  ? 230 ASN EEE OD1 1 
ATOM 9559  N ND2 . ASN E 1 213 ? 165.583 -12.323 26.164  1.000 44.150  ? 230 ASN EEE ND2 1 
ATOM 9560  N N   . THR E 1 214 ? 164.745 -11.323 31.267  1.000 39.810  ? 231 THR EEE N   1 
ATOM 9561  C CA  . THR E 1 214 ? 165.750 -10.612 32.101  1.000 39.590  ? 231 THR EEE CA  1 
ATOM 9562  C C   . THR E 1 214 ? 165.629 -11.004 33.577  1.000 36.920  ? 231 THR EEE C   1 
ATOM 9563  O O   . THR E 1 214 ? 166.483 -10.587 34.343  1.000 38.420  ? 231 THR EEE O   1 
ATOM 9564  C CB  . THR E 1 214 ? 165.600 -9.097  31.965  1.000 40.300  ? 231 THR EEE CB  1 
ATOM 9565  O OG1 . THR E 1 214 ? 164.315 -8.757  32.479  1.000 41.280  ? 231 THR EEE OG1 1 
ATOM 9566  C CG2 . THR E 1 214 ? 165.727 -8.625  30.534  1.000 41.690  ? 231 THR EEE CG2 1 
ATOM 9567  N N   . ALA E 1 215 ? 164.631 -11.788 33.951  1.000 36.810  ? 232 ALA EEE N   1 
ATOM 9568  C CA  . ALA E 1 215 ? 164.259 -11.992 35.364  1.000 39.940  ? 232 ALA EEE CA  1 
ATOM 9569  C C   . ALA E 1 215 ? 164.658 -13.399 35.787  1.000 42.730  ? 232 ALA EEE C   1 
ATOM 9570  O O   . ALA E 1 215 ? 163.972 -14.357 35.353  1.000 46.950  ? 232 ALA EEE O   1 
ATOM 9571  C CB  . ALA E 1 215 ? 162.779 -11.785 35.552  1.000 40.400  ? 232 ALA EEE CB  1 
ATOM 9572  N N   . THR E 1 216 ? 165.698 -13.513 36.618  1.000 40.380  ? 233 THR EEE N   1 
ATOM 9573  C CA  . THR E 1 216 ? 166.152 -14.803 37.197  1.000 36.110  ? 233 THR EEE CA  1 
ATOM 9574  C C   . THR E 1 216 ? 165.653 -14.878 38.635  1.000 32.190  ? 233 THR EEE C   1 
ATOM 9575  O O   . THR E 1 216 ? 165.650 -13.847 39.273  1.000 36.120  ? 233 THR EEE O   1 
ATOM 9576  C CB  . THR E 1 216 ? 167.671 -14.933 37.095  1.000 36.640  ? 233 THR EEE CB  1 
ATOM 9577  O OG1 . THR E 1 216 ? 168.047 -14.690 35.740  1.000 35.960  ? 233 THR EEE OG1 1 
ATOM 9578  C CG2 . THR E 1 216 ? 168.158 -16.304 37.489  1.000 39.880  ? 233 THR EEE CG2 1 
ATOM 9579  N N   . THR E 1 217 ? 165.220 -16.051 39.093  1.000 31.070  ? 234 THR EEE N   1 
ATOM 9580  C CA  . THR E 1 217 ? 164.775 -16.339 40.490  1.000 32.370  ? 234 THR EEE CA  1 
ATOM 9581  C C   . THR E 1 217 ? 165.741 -17.349 41.098  1.000 35.900  ? 234 THR EEE C   1 
ATOM 9582  O O   . THR E 1 217 ? 165.978 -18.390 40.466  1.000 44.550  ? 234 THR EEE O   1 
ATOM 9583  C CB  . THR E 1 217 ? 163.396 -16.976 40.533  1.000 32.330  ? 234 THR EEE CB  1 
ATOM 9584  O OG1 . THR E 1 217 ? 162.478 -16.133 39.833  1.000 33.780  ? 234 THR EEE OG1 1 
ATOM 9585  C CG2 . THR E 1 217 ? 162.905 -17.218 41.946  1.000 33.320  ? 234 THR EEE CG2 1 
ATOM 9586  N N   . VAL E 1 218 ? 166.317 -17.065 42.262  1.000 38.040  ? 235 VAL EEE N   1 
ATOM 9587  C CA  . VAL E 1 218 ? 167.354 -17.961 42.853  1.000 37.750  ? 235 VAL EEE CA  1 
ATOM 9588  C C   . VAL E 1 218 ? 166.644 -19.034 43.682  1.000 35.710  ? 235 VAL EEE C   1 
ATOM 9589  O O   . VAL E 1 218 ? 165.670 -18.699 44.330  1.000 34.020  ? 235 VAL EEE O   1 
ATOM 9590  C CB  . VAL E 1 218 ? 168.371 -17.148 43.665  1.000 38.700  ? 235 VAL EEE CB  1 
ATOM 9591  C CG1 . VAL E 1 218 ? 169.152 -18.014 44.640  1.000 43.670  ? 235 VAL EEE CG1 1 
ATOM 9592  C CG2 . VAL E 1 218 ? 169.307 -16.394 42.737  1.000 35.780  ? 235 VAL EEE CG2 1 
ATOM 9593  N N   . LEU E 1 219 ? 167.122 -20.277 43.644  1.000 34.700  ? 236 LEU EEE N   1 
ATOM 9594  C CA  . LEU E 1 219 ? 166.430 -21.430 44.266  1.000 36.490  ? 236 LEU EEE CA  1 
ATOM 9595  C C   . LEU E 1 219 ? 167.168 -21.890 45.528  1.000 39.330  ? 236 LEU EEE C   1 
ATOM 9596  O O   . LEU E 1 219 ? 166.717 -22.882 46.136  1.000 39.120  ? 236 LEU EEE O   1 
ATOM 9597  C CB  . LEU E 1 219 ? 166.356 -22.539 43.217  1.000 38.880  ? 236 LEU EEE CB  1 
ATOM 9598  C CG  . LEU E 1 219 ? 165.556 -22.184 41.967  1.000 39.750  ? 236 LEU EEE CG  1 
ATOM 9599  C CD1 . LEU E 1 219 ? 165.695 -23.268 40.906  1.000 40.190  ? 236 LEU EEE CD1 1 
ATOM 9600  C CD2 . LEU E 1 219 ? 164.089 -21.945 42.301  1.000 39.320  ? 236 LEU EEE CD2 1 
ATOM 9601  N N   . LEU E 1 220 ? 168.233 -21.188 45.927  1.000 44.960  ? 237 LEU EEE N   1 
ATOM 9602  C CA  . LEU E 1 220 ? 169.022 -21.506 47.150  1.000 48.670  ? 237 LEU EEE CA  1 
ATOM 9603  C C   . LEU E 1 220 ? 168.216 -21.129 48.397  1.000 45.730  ? 237 LEU EEE C   1 
ATOM 9604  O O   . LEU E 1 220 ? 167.504 -20.127 48.352  1.000 41.010  ? 237 LEU EEE O   1 
ATOM 9605  C CB  . LEU E 1 220 ? 170.348 -20.740 47.132  1.000 52.740  ? 237 LEU EEE CB  1 
ATOM 9606  C CG  . LEU E 1 220 ? 171.227 -20.930 45.901  1.000 55.230  ? 237 LEU EEE CG  1 
ATOM 9607  C CD1 . LEU E 1 220 ? 172.513 -20.134 46.073  1.000 55.310  ? 237 LEU EEE CD1 1 
ATOM 9608  C CD2 . LEU E 1 220 ? 171.528 -22.400 45.644  1.000 55.810  ? 237 LEU EEE CD2 1 
ATOM 9609  N N   . ASP E 1 221 ? 168.368 -21.903 49.471  1.000 46.470  ? 238 ASP EEE N   1 
ATOM 9610  C CA  . ASP E 1 221 ? 167.674 -21.698 50.767  1.000 47.670  ? 238 ASP EEE CA  1 
ATOM 9611  C C   . ASP E 1 221 ? 168.553 -20.843 51.671  1.000 50.580  ? 238 ASP EEE C   1 
ATOM 9612  O O   . ASP E 1 221 ? 169.628 -20.405 51.192  1.000 45.220  ? 238 ASP EEE O   1 
ATOM 9613  C CB  . ASP E 1 221 ? 167.308 -23.036 51.422  1.000 49.470  ? 238 ASP EEE CB  1 
ATOM 9614  C CG  . ASP E 1 221 ? 168.485 -23.891 51.858  1.000 49.130  ? 238 ASP EEE CG  1 
ATOM 9615  O OD1 . ASP E 1 221 ? 169.628 -23.449 51.701  1.000 48.850  ? 238 ASP EEE OD1 1 
ATOM 9616  O OD2 . ASP E 1 221 ? 168.245 -24.999 52.352  1.000 51.380  ? 238 ASP EEE OD2 1 
ATOM 9617  N N   . GLU E 1 222 ? 168.117 -20.639 52.929  1.000 59.420  ? 239 GLU EEE N   1 
ATOM 9618  C CA  . GLU E 1 222 ? 168.825 -19.874 53.999  1.000 63.760  ? 239 GLU EEE CA  1 
ATOM 9619  C C   . GLU E 1 222 ? 170.307 -20.267 54.050  1.000 59.540  ? 239 GLU EEE C   1 
ATOM 9620  O O   . GLU E 1 222 ? 171.115 -19.435 54.436  1.000 57.820  ? 239 GLU EEE O   1 
ATOM 9621  C CB  . GLU E 1 222 ? 168.221 -20.160 55.385  1.000 70.410  ? 239 GLU EEE CB  1 
ATOM 9622  C CG  . GLU E 1 222 ? 166.737 -19.861 55.493  1.000 76.100  ? 239 GLU EEE CG  1 
ATOM 9623  C CD  . GLU E 1 222 ? 165.790 -21.025 55.234  1.000 81.200  ? 239 GLU EEE CD  1 
ATOM 9624  O OE1 . GLU E 1 222 ? 165.211 -21.549 56.197  1.000 82.380  ? 239 GLU EEE OE1 1 
ATOM 9625  O OE2 . GLU E 1 222 ? 165.602 -21.379 54.064  1.000 89.540  ? 239 GLU EEE OE2 1 
ATOM 9626  N N   . PHE E 1 223 ? 170.624 -21.527 53.722  1.000 56.480  ? 240 PHE EEE N   1 
ATOM 9627  C CA  . PHE E 1 223 ? 171.959 -22.160 53.870  1.000 60.130  ? 240 PHE EEE CA  1 
ATOM 9628  C C   . PHE E 1 223 ? 172.668 -22.271 52.511  1.000 63.610  ? 240 PHE EEE C   1 
ATOM 9629  O O   . PHE E 1 223 ? 173.646 -23.018 52.424  1.000 69.990  ? 240 PHE EEE O   1 
ATOM 9630  C CB  . PHE E 1 223 ? 171.829 -23.565 54.468  1.000 65.820  ? 240 PHE EEE CB  1 
ATOM 9631  C CG  . PHE E 1 223 ? 171.079 -23.676 55.777  1.000 71.420  ? 240 PHE EEE CG  1 
ATOM 9632  C CD1 . PHE E 1 223 ? 169.691 -23.662 55.800  1.000 75.620  ? 240 PHE EEE CD1 1 
ATOM 9633  C CD2 . PHE E 1 223 ? 171.750 -23.823 56.986  1.000 75.320  ? 240 PHE EEE CD2 1 
ATOM 9634  C CE1 . PHE E 1 223 ? 168.994 -23.745 56.995  1.000 71.850  ? 240 PHE EEE CE1 1 
ATOM 9635  C CE2 . PHE E 1 223 ? 171.051 -23.927 58.178  1.000 72.790  ? 240 PHE EEE CE2 1 
ATOM 9636  C CZ  . PHE E 1 223 ? 169.676 -23.888 58.180  1.000 72.260  ? 240 PHE EEE CZ  1 
ATOM 9637  N N   . GLY E 1 224 ? 172.197 -21.600 51.461  1.000 62.220  ? 241 GLY EEE N   1 
ATOM 9638  C CA  . GLY E 1 224 ? 172.879 -21.556 50.145  1.000 58.130  ? 241 GLY EEE CA  1 
ATOM 9639  C C   . GLY E 1 224 ? 172.859 -22.884 49.391  1.000 50.620  ? 241 GLY EEE C   1 
ATOM 9640  O O   . GLY E 1 224 ? 173.701 -23.063 48.476  1.000 49.030  ? 241 GLY EEE O   1 
ATOM 9641  N N   . VAL E 1 225 ? 171.917 -23.765 49.728  1.000 47.330  ? 242 VAL EEE N   1 
ATOM 9642  C CA  . VAL E 1 225 ? 171.659 -25.065 49.042  1.000 47.400  ? 242 VAL EEE CA  1 
ATOM 9643  C C   . VAL E 1 225 ? 170.342 -24.979 48.254  1.000 46.500  ? 242 VAL EEE C   1 
ATOM 9644  O O   . VAL E 1 225 ? 169.293 -24.670 48.862  1.000 46.480  ? 242 VAL EEE O   1 
ATOM 9645  C CB  . VAL E 1 225 ? 171.576 -26.215 50.058  1.000 48.730  ? 242 VAL EEE CB  1 
ATOM 9646  C CG1 . VAL E 1 225 ? 171.487 -27.558 49.360  1.000 49.700  ? 242 VAL EEE CG1 1 
ATOM 9647  C CG2 . VAL E 1 225 ? 172.744 -26.197 51.017  1.000 48.770  ? 242 VAL EEE CG2 1 
ATOM 9648  N N   . GLY E 1 226 ? 170.386 -25.282 46.957  1.000 43.350  ? 243 GLY EEE N   1 
ATOM 9649  C CA  . GLY E 1 226 ? 169.193 -25.411 46.095  1.000 44.000  ? 243 GLY EEE CA  1 
ATOM 9650  C C   . GLY E 1 226 ? 168.570 -26.796 46.246  1.000 45.920  ? 243 GLY EEE C   1 
ATOM 9651  O O   . GLY E 1 226 ? 169.075 -27.619 47.009  1.000 49.000  ? 243 GLY EEE O   1 
ATOM 9652  N N   . PRO E 1 227 ? 167.435 -27.086 45.574  1.000 41.950  ? 244 PRO EEE N   1 
ATOM 9653  C CA  . PRO E 1 227 ? 166.917 -28.450 45.506  1.000 41.330  ? 244 PRO EEE CA  1 
ATOM 9654  C C   . PRO E 1 227 ? 167.995 -29.411 44.997  1.000 39.090  ? 244 PRO EEE C   1 
ATOM 9655  O O   . PRO E 1 227 ? 168.775 -29.009 44.154  1.000 35.010  ? 244 PRO EEE O   1 
ATOM 9656  C CB  . PRO E 1 227 ? 165.727 -28.359 44.539  1.000 41.570  ? 244 PRO EEE CB  1 
ATOM 9657  C CG  . PRO E 1 227 ? 165.282 -26.918 44.673  1.000 41.770  ? 244 PRO EEE CG  1 
ATOM 9658  C CD  . PRO E 1 227 ? 166.552 -26.119 44.915  1.000 40.120  ? 244 PRO EEE CD  1 
ATOM 9659  N N   . LEU E 1 228 ? 168.028 -30.625 45.558  1.000 40.890  ? 245 LEU EEE N   1 
ATOM 9660  C CA  . LEU E 1 228 ? 168.978 -31.710 45.182  1.000 41.620  ? 245 LEU EEE CA  1 
ATOM 9661  C C   . LEU E 1 228 ? 168.193 -32.806 44.464  1.000 41.710  ? 245 LEU EEE C   1 
ATOM 9662  O O   . LEU E 1 228 ? 167.220 -33.319 45.031  1.000 42.940  ? 245 LEU EEE O   1 
ATOM 9663  C CB  . LEU E 1 228 ? 169.696 -32.244 46.425  1.000 41.100  ? 245 LEU EEE CB  1 
ATOM 9664  C CG  . LEU E 1 228 ? 170.583 -31.221 47.137  1.000 42.170  ? 245 LEU EEE CG  1 
ATOM 9665  C CD1 . LEU E 1 228 ? 171.202 -31.783 48.392  1.000 44.150  ? 245 LEU EEE CD1 1 
ATOM 9666  C CD2 . LEU E 1 228 ? 171.623 -30.646 46.183  1.000 43.600  ? 245 LEU EEE CD2 1 
ATOM 9667  N N   . CYS E 1 229 ? 168.595 -33.125 43.240  1.000 41.870  ? 246 CYS EEE N   1 
ATOM 9668  C CA  . CYS E 1 229 ? 167.829 -33.992 42.320  1.000 49.440  ? 246 CYS EEE CA  1 
ATOM 9669  C C   . CYS E 1 229 ? 168.076 -35.475 42.619  1.000 50.680  ? 246 CYS EEE C   1 
ATOM 9670  O O   . CYS E 1 229 ? 168.944 -36.065 41.965  1.000 56.330  ? 246 CYS EEE O   1 
ATOM 9671  C CB  . CYS E 1 229 ? 168.204 -33.636 40.895  1.000 55.920  ? 246 CYS EEE CB  1 
ATOM 9672  S SG  . CYS E 1 229 ? 167.645 -31.968 40.474  1.000 57.610  ? 246 CYS EEE SG  1 
ATOM 9673  N N   . LYS E 1 230 ? 167.311 -36.039 43.556  1.000 48.550  ? 247 LYS EEE N   1 
ATOM 9674  C CA  . LYS E 1 230 ? 167.259 -37.494 43.846  1.000 50.960  ? 247 LYS EEE CA  1 
ATOM 9675  C C   . LYS E 1 230 ? 166.987 -38.261 42.546  1.000 55.380  ? 247 LYS EEE C   1 
ATOM 9676  O O   . LYS E 1 230 ? 166.097 -37.866 41.787  1.000 59.970  ? 247 LYS EEE O   1 
ATOM 9677  C CB  . LYS E 1 230 ? 166.166 -37.789 44.874  1.000 51.840  ? 247 LYS EEE CB  1 
ATOM 9678  C CG  . LYS E 1 230 ? 166.479 -37.318 46.287  1.000 57.250  ? 247 LYS EEE CG  1 
ATOM 9679  C CD  . LYS E 1 230 ? 165.347 -37.633 47.256  1.000 59.710  ? 247 LYS EEE CD  1 
ATOM 9680  C CE  . LYS E 1 230 ? 165.642 -37.219 48.681  1.000 63.200  ? 247 LYS EEE CE  1 
ATOM 9681  N NZ  . LYS E 1 230 ? 164.565 -37.676 49.585  1.000 61.530  ? 247 LYS EEE NZ  1 
ATOM 9682  N N   . GLY E 1 231 ? 167.746 -39.325 42.295  1.000 61.770  ? 248 GLY EEE N   1 
ATOM 9683  C CA  . GLY E 1 231 ? 167.568 -40.212 41.128  1.000 59.560  ? 248 GLY EEE CA  1 
ATOM 9684  C C   . GLY E 1 231 ? 168.031 -39.543 39.844  1.000 59.180  ? 248 GLY EEE C   1 
ATOM 9685  O O   . GLY E 1 231 ? 167.609 -40.012 38.793  1.000 56.700  ? 248 GLY EEE O   1 
ATOM 9686  N N   . ASP E 1 232 ? 168.839 -38.483 39.927  1.000 59.070  ? 249 ASP EEE N   1 
ATOM 9687  C CA  . ASP E 1 232 ? 169.253 -37.667 38.760  1.000 58.870  ? 249 ASP EEE CA  1 
ATOM 9688  C C   . ASP E 1 232 ? 168.009 -37.186 37.990  1.000 60.560  ? 249 ASP EEE C   1 
ATOM 9689  O O   . ASP E 1 232 ? 168.034 -37.154 36.734  1.000 61.290  ? 249 ASP EEE O   1 
ATOM 9690  C CB  . ASP E 1 232 ? 170.267 -38.465 37.951  1.000 57.140  ? 249 ASP EEE CB  1 
ATOM 9691  C CG  . ASP E 1 232 ? 171.626 -38.491 38.629  1.000 60.240  ? 249 ASP EEE CG  1 
ATOM 9692  O OD1 . ASP E 1 232 ? 171.834 -37.667 39.554  1.000 60.460  ? 249 ASP EEE OD1 1 
ATOM 9693  O OD2 . ASP E 1 232 ? 172.494 -39.276 38.187  1.000 55.930  ? 249 ASP EEE OD2 1 
ATOM 9694  N N   . ASN E 1 233 ? 166.984 -36.765 38.744  1.000 53.110  ? 250 ASN EEE N   1 
ATOM 9695  C CA  . ASN E 1 233 ? 165.702 -36.238 38.208  1.000 46.320  ? 250 ASN EEE CA  1 
ATOM 9696  C C   . ASN E 1 233 ? 165.407 -34.842 38.769  1.000 42.200  ? 250 ASN EEE C   1 
ATOM 9697  O O   . ASN E 1 233 ? 165.556 -34.613 39.979  1.000 38.480  ? 250 ASN EEE O   1 
ATOM 9698  C CB  . ASN E 1 233 ? 164.534 -37.163 38.533  1.000 44.930  ? 250 ASN EEE CB  1 
ATOM 9699  C CG  . ASN E 1 233 ? 164.578 -38.443 37.747  1.000 44.780  ? 250 ASN EEE CG  1 
ATOM 9700  O OD1 . ASN E 1 233 ? 165.101 -38.475 36.631  1.000 46.400  ? 250 ASN EEE OD1 1 
ATOM 9701  N ND2 . ASN E 1 233 ? 164.003 -39.482 38.325  1.000 50.010  ? 250 ASN EEE ND2 1 
ATOM 9702  N N   . LEU E 1 234 ? 164.948 -33.954 37.896  1.000 40.290  ? 251 LEU EEE N   1 
ATOM 9703  C CA  . LEU E 1 234 ? 164.436 -32.607 38.236  1.000 37.560  ? 251 LEU EEE CA  1 
ATOM 9704  C C   . LEU E 1 234 ? 162.928 -32.618 38.009  1.000 37.660  ? 251 LEU EEE C   1 
ATOM 9705  O O   . LEU E 1 234 ? 162.495 -33.140 36.959  1.000 37.080  ? 251 LEU EEE O   1 
ATOM 9706  C CB  . LEU E 1 234 ? 165.112 -31.594 37.313  1.000 35.190  ? 251 LEU EEE CB  1 
ATOM 9707  C CG  . LEU E 1 234 ? 164.737 -30.143 37.548  1.000 33.610  ? 251 LEU EEE CG  1 
ATOM 9708  C CD1 . LEU E 1 234 ? 165.193 -29.684 38.919  1.000 33.310  ? 251 LEU EEE CD1 1 
ATOM 9709  C CD2 . LEU E 1 234 ? 165.357 -29.267 36.490  1.000 33.480  ? 251 LEU EEE CD2 1 
ATOM 9710  N N   . TYR E 1 235 ? 162.167 -32.069 38.954  1.000 39.760  ? 252 TYR EEE N   1 
ATOM 9711  C CA  . TYR E 1 235 ? 160.684 -32.070 38.941  1.000 42.540  ? 252 TYR EEE CA  1 
ATOM 9712  C C   . TYR E 1 235 ? 160.163 -30.636 38.775  1.000 41.690  ? 252 TYR EEE C   1 
ATOM 9713  O O   . TYR E 1 235 ? 160.181 -29.829 39.734  1.000 46.290  ? 252 TYR EEE O   1 
ATOM 9714  C CB  . TYR E 1 235 ? 160.148 -32.722 40.217  1.000 48.240  ? 252 TYR EEE CB  1 
ATOM 9715  C CG  . TYR E 1 235 ? 160.154 -34.225 40.229  1.000 48.010  ? 252 TYR EEE CG  1 
ATOM 9716  C CD1 . TYR E 1 235 ? 161.301 -34.938 40.508  1.000 49.580  ? 252 TYR EEE CD1 1 
ATOM 9717  C CD2 . TYR E 1 235 ? 158.984 -34.929 39.996  1.000 48.290  ? 252 TYR EEE CD2 1 
ATOM 9718  C CE1 . TYR E 1 235 ? 161.291 -36.324 40.527  1.000 57.500  ? 252 TYR EEE CE1 1 
ATOM 9719  C CE2 . TYR E 1 235 ? 158.959 -36.313 40.008  1.000 50.080  ? 252 TYR EEE CE2 1 
ATOM 9720  C CZ  . TYR E 1 235 ? 160.106 -37.015 40.283  1.000 55.540  ? 252 TYR EEE CZ  1 
ATOM 9721  O OH  . TYR E 1 235 ? 160.058 -38.379 40.327  1.000 55.540  ? 252 TYR EEE OH  1 
ATOM 9722  N N   . LEU E 1 236 ? 159.661 -30.343 37.579  1.000 39.800  ? 253 LEU EEE N   1 
ATOM 9723  C CA  . LEU E 1 236 ? 158.951 -29.079 37.282  1.000 39.110  ? 253 LEU EEE CA  1 
ATOM 9724  C C   . LEU E 1 236 ? 157.453 -29.340 37.416  1.000 39.210  ? 253 LEU EEE C   1 
ATOM 9725  O O   . LEU E 1 236 ? 156.942 -30.276 36.766  1.000 36.990  ? 253 LEU EEE O   1 
ATOM 9726  C CB  . LEU E 1 236 ? 159.340 -28.599 35.885  1.000 36.900  ? 253 LEU EEE CB  1 
ATOM 9727  C CG  . LEU E 1 236 ? 160.846 -28.594 35.620  1.000 35.160  ? 253 LEU EEE CG  1 
ATOM 9728  C CD1 . LEU E 1 236 ? 161.152 -27.982 34.277  1.000 37.220  ? 253 LEU EEE CD1 1 
ATOM 9729  C CD2 . LEU E 1 236 ? 161.590 -27.856 36.703  1.000 34.410  ? 253 LEU EEE CD2 1 
ATOM 9730  N N   . SER E 1 237 ? 156.814 -28.575 38.293  1.000 40.550  ? 254 SER EEE N   1 
ATOM 9731  C CA  . SER E 1 237 ? 155.349 -28.540 38.486  1.000 41.210  ? 254 SER EEE CA  1 
ATOM 9732  C C   . SER E 1 237 ? 154.869 -27.111 38.192  1.000 37.170  ? 254 SER EEE C   1 
ATOM 9733  O O   . SER E 1 237 ? 155.668 -26.155 38.373  1.000 31.810  ? 254 SER EEE O   1 
ATOM 9734  C CB  . SER E 1 237 ? 155.002 -29.021 39.880  1.000 43.540  ? 254 SER EEE CB  1 
ATOM 9735  O OG  . SER E 1 237 ? 155.898 -30.047 40.286  1.000 46.200  ? 254 SER EEE OG  1 
ATOM 9736  N N   . ALA E 1 238 ? 153.621 -26.961 37.742  1.000 32.130  ? 255 ALA EEE N   1 
ATOM 9737  C CA  . ALA E 1 238 ? 153.040 -25.662 37.329  1.000 28.610  ? 255 ALA EEE CA  1 
ATOM 9738  C C   . ALA E 1 238 ? 151.525 -25.756 37.236  1.000 25.140  ? 255 ALA EEE C   1 
ATOM 9739  O O   . ALA E 1 238 ? 151.040 -26.821 36.917  1.000 24.000  ? 255 ALA EEE O   1 
ATOM 9740  C CB  . ALA E 1 238 ? 153.616 -25.235 36.009  1.000 29.660  ? 255 ALA EEE CB  1 
ATOM 9741  N N   . VAL E 1 239 ? 150.833 -24.655 37.523  1.000 24.130  ? 256 VAL EEE N   1 
ATOM 9742  C CA  . VAL E 1 239 ? 149.412 -24.425 37.137  1.000 25.130  ? 256 VAL EEE CA  1 
ATOM 9743  C C   . VAL E 1 239 ? 149.307 -22.988 36.676  1.000 25.590  ? 256 VAL EEE C   1 
ATOM 9744  O O   . VAL E 1 239 ? 149.865 -22.152 37.379  1.000 27.860  ? 256 VAL EEE O   1 
ATOM 9745  C CB  . VAL E 1 239 ? 148.436 -24.640 38.294  1.000 24.810  ? 256 VAL EEE CB  1 
ATOM 9746  C CG1 . VAL E 1 239 ? 146.999 -24.409 37.844  1.000 23.780  ? 256 VAL EEE CG1 1 
ATOM 9747  C CG2 . VAL E 1 239 ? 148.604 -26.007 38.924  1.000 25.380  ? 256 VAL EEE CG2 1 
ATOM 9748  N N   . ASP E 1 240 ? 148.594 -22.715 35.589  1.000 25.010  ? 257 ASP EEE N   1 
ATOM 9749  C CA  . ASP E 1 240 ? 148.384 -21.319 35.125  1.000 24.650  ? 257 ASP EEE CA  1 
ATOM 9750  C C   . ASP E 1 240 ? 146.970 -21.174 34.580  1.000 23.650  ? 257 ASP EEE C   1 
ATOM 9751  O O   . ASP E 1 240 ? 146.808 -20.928 33.360  1.000 23.330  ? 257 ASP EEE O   1 
ATOM 9752  C CB  . ASP E 1 240 ? 149.442 -20.955 34.093  1.000 26.430  ? 257 ASP EEE CB  1 
ATOM 9753  C CG  . ASP E 1 240 ? 150.802 -20.743 34.725  1.000 25.820  ? 257 ASP EEE CG  1 
ATOM 9754  O OD1 . ASP E 1 240 ? 150.986 -19.703 35.369  1.000 22.240  ? 257 ASP EEE OD1 1 
ATOM 9755  O OD2 . ASP E 1 240 ? 151.655 -21.632 34.545  1.000 29.090  ? 257 ASP EEE OD2 1 
ATOM 9756  N N   . VAL E 1 241 ? 145.980 -21.380 35.446  1.000 22.450  ? 258 VAL EEE N   1 
ATOM 9757  C CA  . VAL E 1 241 ? 144.561 -21.091 35.124  1.000 22.220  ? 258 VAL EEE CA  1 
ATOM 9758  C C   . VAL E 1 241 ? 144.487 -19.567 35.025  1.000 22.490  ? 258 VAL EEE C   1 
ATOM 9759  O O   . VAL E 1 241 ? 144.712 -18.911 36.061  1.000 20.820  ? 258 VAL EEE O   1 
ATOM 9760  C CB  . VAL E 1 241 ? 143.612 -21.659 36.188  1.000 22.480  ? 258 VAL EEE CB  1 
ATOM 9761  C CG1 . VAL E 1 241 ? 142.164 -21.257 35.935  1.000 22.180  ? 258 VAL EEE CG1 1 
ATOM 9762  C CG2 . VAL E 1 241 ? 143.738 -23.166 36.292  1.000 22.830  ? 258 VAL EEE CG2 1 
ATOM 9763  N N   . CYS E 1 242 ? 144.277 -19.033 33.816  1.000 22.010  ? 259 CYS EEE N   1 
ATOM 9764  C CA  . CYS E 1 242 ? 144.453 -17.599 33.516  1.000 22.000  ? 259 CYS EEE CA  1 
ATOM 9765  C C   . CYS E 1 242 ? 143.181 -16.842 33.853  1.000 24.410  ? 259 CYS EEE C   1 
ATOM 9766  O O   . CYS E 1 242 ? 143.286 -15.605 34.085  1.000 32.400  ? 259 CYS EEE O   1 
ATOM 9767  C CB  . CYS E 1 242 ? 144.753 -17.401 32.057  1.000 21.620  ? 259 CYS EEE CB  1 
ATOM 9768  S SG  . CYS E 1 242 ? 146.463 -17.842 31.708  1.000 28.190  ? 259 CYS EEE SG  1 
ATOM 9769  N N   . GLY E 1 243 ? 142.060 -17.565 33.897  1.000 22.730  ? 260 GLY EEE N   1 
ATOM 9770  C CA  . GLY E 1 243 ? 140.707 -17.004 33.990  1.000 22.590  ? 260 GLY EEE CA  1 
ATOM 9771  C C   . GLY E 1 243 ? 139.715 -17.905 33.290  1.000 22.790  ? 260 GLY EEE C   1 
ATOM 9772  O O   . GLY E 1 243 ? 140.025 -19.090 33.114  1.000 23.330  ? 260 GLY EEE O   1 
ATOM 9773  N N   . MET E 1 244 ? 138.559 -17.378 32.915  1.000 22.260  ? 261 MET EEE N   1 
ATOM 9774  C CA  . MET E 1 244 ? 137.530 -18.113 32.145  1.000 23.530  ? 261 MET EEE CA  1 
ATOM 9775  C C   . MET E 1 244 ? 137.301 -17.402 30.818  1.000 24.340  ? 261 MET EEE C   1 
ATOM 9776  O O   . MET E 1 244 ? 137.337 -16.146 30.788  1.000 28.600  ? 261 MET EEE O   1 
ATOM 9777  C CB  . MET E 1 244 ? 136.193 -18.172 32.880  1.000 25.640  ? 261 MET EEE CB  1 
ATOM 9778  C CG  . MET E 1 244 ? 136.286 -18.807 34.225  1.000 27.500  ? 261 MET EEE CG  1 
ATOM 9779  S SD  . MET E 1 244 ? 134.667 -18.775 35.015  1.000 32.870  ? 261 MET EEE SD  1 
ATOM 9780  C CE  . MET E 1 244 ? 135.090 -19.744 36.468  1.000 33.780  ? 261 MET EEE CE  1 
ATOM 9781  N N   . PHE E 1 245 ? 137.070 -18.182 29.766  1.000 23.650  ? 262 PHE EEE N   1 
ATOM 9782  C CA  . PHE E 1 245 ? 136.554 -17.719 28.465  1.000 23.060  ? 262 PHE EEE CA  1 
ATOM 9783  C C   . PHE E 1 245 ? 135.039 -17.694 28.605  1.000 21.880  ? 262 PHE EEE C   1 
ATOM 9784  O O   . PHE E 1 245 ? 134.496 -18.716 29.023  1.000 19.830  ? 262 PHE EEE O   1 
ATOM 9785  C CB  . PHE E 1 245 ? 136.957 -18.656 27.329  1.000 23.730  ? 262 PHE EEE CB  1 
ATOM 9786  C CG  . PHE E 1 245 ? 136.283 -18.335 26.025  1.000 25.100  ? 262 PHE EEE CG  1 
ATOM 9787  C CD1 . PHE E 1 245 ? 136.444 -17.081 25.444  1.000 26.630  ? 262 PHE EEE CD1 1 
ATOM 9788  C CD2 . PHE E 1 245 ? 135.483 -19.264 25.390  1.000 25.160  ? 262 PHE EEE CD2 1 
ATOM 9789  C CE1 . PHE E 1 245 ? 135.838 -16.763 24.239  1.000 26.250  ? 262 PHE EEE CE1 1 
ATOM 9790  C CE2 . PHE E 1 245 ? 134.871 -18.943 24.192  1.000 26.970  ? 262 PHE EEE CE2 1 
ATOM 9791  C CZ  . PHE E 1 245 ? 135.044 -17.696 23.625  1.000 27.800  ? 262 PHE EEE CZ  1 
ATOM 9792  N N   . THR E 1 246 ? 134.399 -16.559 28.325  1.000 21.610  ? 263 THR EEE N   1 
ATOM 9793  C CA  . THR E 1 246 ? 132.922 -16.450 28.308  1.000 21.130  ? 263 THR EEE CA  1 
ATOM 9794  C C   . THR E 1 246 ? 132.448 -16.602 26.859  1.000 23.000  ? 263 THR EEE C   1 
ATOM 9795  O O   . THR E 1 246 ? 132.726 -15.717 26.019  1.000 27.230  ? 263 THR EEE O   1 
ATOM 9796  C CB  . THR E 1 246 ? 132.432 -15.163 28.976  1.000 20.240  ? 263 THR EEE CB  1 
ATOM 9797  O OG1 . THR E 1 246 ? 132.980 -15.082 30.293  1.000 20.660  ? 263 THR EEE OG1 1 
ATOM 9798  C CG2 . THR E 1 246 ? 130.929 -15.106 29.050  1.000 19.500  ? 263 THR EEE CG2 1 
ATOM 9799  N N   . ASN E 1 247 ? 131.786 -17.720 26.584  1.000 23.350  ? 264 ASN EEE N   1 
ATOM 9800  C CA  . ASN E 1 247 ? 131.093 -18.018 25.310  1.000 22.000  ? 264 ASN EEE CA  1 
ATOM 9801  C C   . ASN E 1 247 ? 129.922 -17.049 25.109  1.000 20.830  ? 264 ASN EEE C   1 
ATOM 9802  O O   . ASN E 1 247 ? 129.502 -16.445 26.065  1.000 21.440  ? 264 ASN EEE O   1 
ATOM 9803  C CB  . ASN E 1 247 ? 130.653 -19.484 25.278  1.000 22.540  ? 264 ASN EEE CB  1 
ATOM 9804  C CG  . ASN E 1 247 ? 131.779 -20.383 24.811  1.000 24.710  ? 264 ASN EEE CG  1 
ATOM 9805  O OD1 . ASN E 1 247 ? 131.990 -20.540 23.594  1.000 27.300  ? 264 ASN EEE OD1 1 
ATOM 9806  N ND2 . ASN E 1 247 ? 132.506 -20.957 25.758  1.000 22.810  ? 264 ASN EEE ND2 1 
ATOM 9807  N N   . ARG E 1 248 ? 129.439 -16.939 23.878  1.000 20.530  ? 265 ARG EEE N   1 
ATOM 9808  C CA  . ARG E 1 248 ? 128.302 -16.101 23.441  1.000 21.330  ? 265 ARG EEE CA  1 
ATOM 9809  C C   . ARG E 1 248 ? 127.100 -16.309 24.362  1.000 23.040  ? 265 ARG EEE C   1 
ATOM 9810  O O   . ARG E 1 248 ? 126.441 -15.332 24.682  1.000 25.770  ? 265 ARG EEE O   1 
ATOM 9811  C CB  . ARG E 1 248 ? 127.963 -16.413 21.984  1.000 21.910  ? 265 ARG EEE CB  1 
ATOM 9812  C CG  . ARG E 1 248 ? 126.504 -16.181 21.617  1.000 23.180  ? 265 ARG EEE CG  1 
ATOM 9813  C CD  . ARG E 1 248 ? 126.230 -16.493 20.152  1.000 24.180  ? 265 ARG EEE CD  1 
ATOM 9814  N NE  . ARG E 1 248 ? 126.213 -15.338 19.260  1.000 21.680  ? 265 ARG EEE NE  1 
ATOM 9815  C CZ  . ARG E 1 248 ? 127.168 -15.030 18.407  1.000 22.260  ? 265 ARG EEE CZ  1 
ATOM 9816  N NH1 . ARG E 1 248 ? 128.286 -15.745 18.333  1.000 23.640  ? 265 ARG EEE NH1 1 
ATOM 9817  N NH2 . ARG E 1 248 ? 127.017 -13.965 17.640  1.000 24.620  ? 265 ARG EEE NH2 1 
ATOM 9818  N N   . SER E 1 249 ? 126.825 -17.540 24.775  1.000 25.060  ? 266 SER EEE N   1 
ATOM 9819  C CA  . SER E 1 249 ? 125.650 -17.912 25.613  1.000 25.380  ? 266 SER EEE CA  1 
ATOM 9820  C C   . SER E 1 249 ? 125.808 -17.390 27.037  1.000 26.970  ? 266 SER EEE C   1 
ATOM 9821  O O   . SER E 1 249 ? 124.837 -17.485 27.805  1.000 28.670  ? 266 SER EEE O   1 
ATOM 9822  C CB  . SER E 1 249 ? 125.497 -19.388 25.701  1.000 25.300  ? 266 SER EEE CB  1 
ATOM 9823  O OG  . SER E 1 249 ? 126.582 -19.927 26.434  1.000 24.170  ? 266 SER EEE OG  1 
ATOM 9824  N N   . GLY E 1 250 ? 127.027 -17.010 27.408  1.000 28.380  ? 267 GLY EEE N   1 
ATOM 9825  C CA  . GLY E 1 250 ? 127.398 -16.718 28.803  1.000 28.260  ? 267 GLY EEE CA  1 
ATOM 9826  C C   . GLY E 1 250 ? 128.108 -17.885 29.474  1.000 27.080  ? 267 GLY EEE C   1 
ATOM 9827  O O   . GLY E 1 250 ? 128.721 -17.645 30.517  1.000 30.640  ? 267 GLY EEE O   1 
ATOM 9828  N N   . SER E 1 251 ? 128.015 -19.100 28.921  1.000 24.550  ? 268 SER EEE N   1 
ATOM 9829  C CA  . SER E 1 251 ? 128.646 -20.330 29.476  1.000 22.180  ? 268 SER EEE CA  1 
ATOM 9830  C C   . SER E 1 251 ? 130.158 -20.126 29.556  1.000 20.830  ? 268 SER EEE C   1 
ATOM 9831  O O   . SER E 1 251 ? 130.723 -19.537 28.627  1.000 20.800  ? 268 SER EEE O   1 
ATOM 9832  C CB  . SER E 1 251 ? 128.268 -21.552 28.662  1.000 22.050  ? 268 SER EEE CB  1 
ATOM 9833  O OG  . SER E 1 251 ? 126.888 -21.504 28.335  1.000 21.600  ? 268 SER EEE OG  1 
ATOM 9834  N N   . GLN E 1 252 ? 130.795 -20.575 30.634  1.000 20.770  ? 269 GLN EEE N   1 
ATOM 9835  C CA  . GLN E 1 252 ? 132.214 -20.230 30.893  1.000 22.520  ? 269 GLN EEE CA  1 
ATOM 9836  C C   . GLN E 1 252 ? 133.098 -21.469 30.924  1.000 23.240  ? 269 GLN EEE C   1 
ATOM 9837  O O   . GLN E 1 252 ? 132.715 -22.417 31.583  1.000 26.580  ? 269 GLN EEE O   1 
ATOM 9838  C CB  . GLN E 1 252 ? 132.317 -19.473 32.214  1.000 24.590  ? 269 GLN EEE CB  1 
ATOM 9839  C CG  . GLN E 1 252 ? 131.882 -18.024 32.093  1.000 24.650  ? 269 GLN EEE CG  1 
ATOM 9840  C CD  . GLN E 1 252 ? 131.718 -17.318 33.410  1.000 24.840  ? 269 GLN EEE CD  1 
ATOM 9841  O OE1 . GLN E 1 252 ? 131.426 -17.895 34.461  1.000 24.460  ? 269 GLN EEE OE1 1 
ATOM 9842  N NE2 . GLN E 1 252 ? 131.892 -16.017 33.335  1.000 28.890  ? 269 GLN EEE NE2 1 
ATOM 9843  N N   . GLN E 1 253 ? 134.258 -21.412 30.275  1.000 25.310  ? 270 GLN EEE N   1 
ATOM 9844  C CA  . GLN E 1 253 ? 135.315 -22.467 30.265  1.000 25.210  ? 270 GLN EEE CA  1 
ATOM 9845  C C   . GLN E 1 253 ? 136.604 -21.877 30.836  1.000 23.730  ? 270 GLN EEE C   1 
ATOM 9846  O O   . GLN E 1 253 ? 137.015 -20.833 30.364  1.000 22.970  ? 270 GLN EEE O   1 
ATOM 9847  C CB  . GLN E 1 253 ? 135.582 -22.946 28.837  1.000 25.290  ? 270 GLN EEE CB  1 
ATOM 9848  C CG  . GLN E 1 253 ? 134.388 -23.587 28.159  1.000 25.420  ? 270 GLN EEE CG  1 
ATOM 9849  C CD  . GLN E 1 253 ? 134.572 -23.718 26.658  1.000 25.230  ? 270 GLN EEE CD  1 
ATOM 9850  O OE1 . GLN E 1 253 ? 134.144 -22.885 25.862  1.000 22.600  ? 270 GLN EEE OE1 1 
ATOM 9851  N NE2 . GLN E 1 253 ? 135.261 -24.759 26.234  1.000 26.620  ? 270 GLN EEE NE2 1 
ATOM 9852  N N   . TRP E 1 254 ? 137.192 -22.502 31.843  1.000 22.780  ? 271 TRP EEE N   1 
ATOM 9853  C CA  . TRP E 1 254 ? 138.575 -22.182 32.278  1.000 21.920  ? 271 TRP EEE CA  1 
ATOM 9854  C C   . TRP E 1 254 ? 139.472 -22.131 31.044  1.000 19.970  ? 271 TRP EEE C   1 
ATOM 9855  O O   . TRP E 1 254 ? 139.250 -22.955 30.169  1.000 18.770  ? 271 TRP EEE O   1 
ATOM 9856  C CB  . TRP E 1 254 ? 139.075 -23.258 33.234  1.000 22.540  ? 271 TRP EEE CB  1 
ATOM 9857  C CG  . TRP E 1 254 ? 138.306 -23.396 34.510  1.000 23.160  ? 271 TRP EEE CG  1 
ATOM 9858  C CD1 . TRP E 1 254 ? 137.528 -24.442 34.896  1.000 23.320  ? 271 TRP EEE CD1 1 
ATOM 9859  C CD2 . TRP E 1 254 ? 138.320 -22.486 35.607  1.000 23.660  ? 271 TRP EEE CD2 1 
ATOM 9860  N NE1 . TRP E 1 254 ? 137.054 -24.243 36.156  1.000 23.750  ? 271 TRP EEE NE1 1 
ATOM 9861  C CE2 . TRP E 1 254 ? 137.518 -23.046 36.611  1.000 23.460  ? 271 TRP EEE CE2 1 
ATOM 9862  C CE3 . TRP E 1 254 ? 138.910 -21.242 35.821  1.000 25.790  ? 271 TRP EEE CE3 1 
ATOM 9863  C CZ2 . TRP E 1 254 ? 137.284 -22.402 37.818  1.000 25.250  ? 271 TRP EEE CZ2 1 
ATOM 9864  C CZ3 . TRP E 1 254 ? 138.676 -20.601 37.014  1.000 27.480  ? 271 TRP EEE CZ3 1 
ATOM 9865  C CH2 . TRP E 1 254 ? 137.879 -21.181 38.002  1.000 26.680  ? 271 TRP EEE CH2 1 
ATOM 9866  N N   . ARG E 1 255 ? 140.442 -21.222 30.985  1.000 20.450  ? 272 ARG EEE N   1 
ATOM 9867  C CA  . ARG E 1 255 ? 141.463 -21.185 29.903  1.000 21.600  ? 272 ARG EEE CA  1 
ATOM 9868  C C   . ARG E 1 255 ? 142.856 -21.167 30.520  1.000 22.770  ? 272 ARG EEE C   1 
ATOM 9869  O O   . ARG E 1 255 ? 143.117 -20.329 31.393  1.000 23.680  ? 272 ARG EEE O   1 
ATOM 9870  C CB  . ARG E 1 255 ? 141.326 -19.966 28.998  1.000 20.330  ? 272 ARG EEE CB  1 
ATOM 9871  C CG  . ARG E 1 255 ? 142.348 -19.961 27.865  1.000 21.180  ? 272 ARG EEE CG  1 
ATOM 9872  C CD  . ARG E 1 255 ? 142.095 -21.117 26.905  1.000 22.930  ? 272 ARG EEE CD  1 
ATOM 9873  N NE  . ARG E 1 255 ? 142.670 -20.966 25.572  1.000 24.900  ? 272 ARG EEE NE  1 
ATOM 9874  C CZ  . ARG E 1 255 ? 143.894 -21.364 25.187  1.000 25.640  ? 272 ARG EEE CZ  1 
ATOM 9875  N NH1 . ARG E 1 255 ? 144.740 -21.913 26.044  1.000 25.430  ? 272 ARG EEE NH1 1 
ATOM 9876  N NH2 . ARG E 1 255 ? 144.273 -21.197 23.930  1.000 25.850  ? 272 ARG EEE NH2 1 
ATOM 9877  N N   . GLY E 1 256 ? 143.723 -22.066 30.061  1.000 24.040  ? 273 GLY EEE N   1 
ATOM 9878  C CA  . GLY E 1 256 ? 145.074 -22.260 30.625  1.000 24.240  ? 273 GLY EEE CA  1 
ATOM 9879  C C   . GLY E 1 256 ? 146.128 -21.894 29.613  1.000 22.360  ? 273 GLY EEE C   1 
ATOM 9880  O O   . GLY E 1 256 ? 145.778 -21.752 28.445  1.000 20.980  ? 273 GLY EEE O   1 
ATOM 9881  N N   . LEU E 1 257 ? 147.371 -21.724 30.060  1.000 22.280  ? 274 LEU EEE N   1 
ATOM 9882  C CA  . LEU E 1 257 ? 148.525 -21.451 29.166  1.000 23.400  ? 274 LEU EEE CA  1 
ATOM 9883  C C   . LEU E 1 257 ? 149.746 -22.229 29.652  1.000 21.940  ? 274 LEU EEE C   1 
ATOM 9884  O O   . LEU E 1 257 ? 149.908 -22.459 30.897  1.000 20.700  ? 274 LEU EEE O   1 
ATOM 9885  C CB  . LEU E 1 257 ? 148.815 -19.948 29.129  1.000 25.340  ? 274 LEU EEE CB  1 
ATOM 9886  C CG  . LEU E 1 257 ? 147.814 -19.099 28.364  1.000 27.410  ? 274 LEU EEE CG  1 
ATOM 9887  C CD1 . LEU E 1 257 ? 148.163 -17.622 28.461  1.000 28.360  ? 274 LEU EEE CD1 1 
ATOM 9888  C CD2 . LEU E 1 257 ? 147.736 -19.506 26.892  1.000 28.870  ? 274 LEU EEE CD2 1 
ATOM 9889  N N   . SER E 1 258 ? 150.597 -22.588 28.697  1.000 23.000  ? 275 SER EEE N   1 
ATOM 9890  C CA  . SER E 1 258 ? 151.877 -23.284 28.963  1.000 24.830  ? 275 SER EEE CA  1 
ATOM 9891  C C   . SER E 1 258 ? 152.801 -22.370 29.775  1.000 24.740  ? 275 SER EEE C   1 
ATOM 9892  O O   . SER E 1 258 ? 152.669 -21.129 29.691  1.000 25.190  ? 275 SER EEE O   1 
ATOM 9893  C CB  . SER E 1 258 ? 152.521 -23.716 27.679  1.000 26.520  ? 275 SER EEE CB  1 
ATOM 9894  O OG  . SER E 1 258 ? 151.616 -24.510 26.929  1.000 30.320  ? 275 SER EEE OG  1 
ATOM 9895  N N   . ARG E 1 259 ? 153.700 -22.967 30.548  1.000 25.310  ? 276 ARG EEE N   1 
ATOM 9896  C CA  . ARG E 1 259 ? 154.733 -22.235 31.319  1.000 27.200  ? 276 ARG EEE CA  1 
ATOM 9897  C C   . ARG E 1 259 ? 156.119 -22.707 30.880  1.000 26.620  ? 276 ARG EEE C   1 
ATOM 9898  O O   . ARG E 1 259 ? 156.381 -23.911 30.926  1.000 23.810  ? 276 ARG EEE O   1 
ATOM 9899  C CB  . ARG E 1 259 ? 154.542 -22.448 32.821  1.000 29.830  ? 276 ARG EEE CB  1 
ATOM 9900  C CG  . ARG E 1 259 ? 155.676 -21.890 33.673  1.000 31.680  ? 276 ARG EEE CG  1 
ATOM 9901  C CD  . ARG E 1 259 ? 155.320 -21.811 35.149  1.000 30.380  ? 276 ARG EEE CD  1 
ATOM 9902  N NE  . ARG E 1 259 ? 154.257 -20.841 35.369  1.000 27.230  ? 276 ARG EEE NE  1 
ATOM 9903  C CZ  . ARG E 1 259 ? 154.435 -19.565 35.656  1.000 25.550  ? 276 ARG EEE CZ  1 
ATOM 9904  N NH1 . ARG E 1 259 ? 155.638 -19.042 35.801  1.000 24.560  ? 276 ARG EEE NH1 1 
ATOM 9905  N NH2 . ARG E 1 259 ? 153.378 -18.809 35.815  1.000 27.850  ? 276 ARG EEE NH2 1 
ATOM 9906  N N   . TYR E 1 260 ? 156.976 -21.766 30.507  1.000 29.950  ? 277 TYR EEE N   1 
ATOM 9907  C CA  . TYR E 1 260 ? 158.412 -21.993 30.211  1.000 33.830  ? 277 TYR EEE CA  1 
ATOM 9908  C C   . TYR E 1 260 ? 159.190 -22.105 31.523  1.000 34.860  ? 277 TYR EEE C   1 
ATOM 9909  O O   . TYR E 1 260 ? 158.920 -21.325 32.455  1.000 31.660  ? 277 TYR EEE O   1 
ATOM 9910  C CB  . TYR E 1 260 ? 158.951 -20.824 29.388  1.000 32.640  ? 277 TYR EEE CB  1 
ATOM 9911  C CG  . TYR E 1 260 ? 160.435 -20.777 29.174  1.000 33.400  ? 277 TYR EEE CG  1 
ATOM 9912  C CD1 . TYR E 1 260 ? 161.049 -21.496 28.153  1.000 36.140  ? 277 TYR EEE CD1 1 
ATOM 9913  C CD2 . TYR E 1 260 ? 161.231 -19.949 29.942  1.000 34.980  ? 277 TYR EEE CD2 1 
ATOM 9914  C CE1 . TYR E 1 260 ? 162.414 -21.410 27.916  1.000 37.480  ? 277 TYR EEE CE1 1 
ATOM 9915  C CE2 . TYR E 1 260 ? 162.596 -19.839 29.711  1.000 35.480  ? 277 TYR EEE CE2 1 
ATOM 9916  C CZ  . TYR E 1 260 ? 163.183 -20.579 28.701  1.000 35.950  ? 277 TYR EEE CZ  1 
ATOM 9917  O OH  . TYR E 1 260 ? 164.517 -20.486 28.477  1.000 34.300  ? 277 TYR EEE OH  1 
ATOM 9918  N N   . PHE E 1 261 ? 160.124 -23.056 31.568  1.000 35.090  ? 278 PHE EEE N   1 
ATOM 9919  C CA  . PHE E 1 261 ? 161.134 -23.188 32.637  1.000 34.780  ? 278 PHE EEE CA  1 
ATOM 9920  C C   . PHE E 1 261 ? 162.522 -23.235 32.008  1.000 34.030  ? 278 PHE EEE C   1 
ATOM 9921  O O   . PHE E 1 261 ? 162.709 -23.901 31.009  1.000 31.010  ? 278 PHE EEE O   1 
ATOM 9922  C CB  . PHE E 1 261 ? 160.933 -24.472 33.436  1.000 33.970  ? 278 PHE EEE CB  1 
ATOM 9923  C CG  . PHE E 1 261 ? 159.661 -24.572 34.239  1.000 33.250  ? 278 PHE EEE CG  1 
ATOM 9924  C CD1 . PHE E 1 261 ? 158.456 -24.860 33.613  1.000 33.870  ? 278 PHE EEE CD1 1 
ATOM 9925  C CD2 . PHE E 1 261 ? 159.681 -24.450 35.614  1.000 30.520  ? 278 PHE EEE CD2 1 
ATOM 9926  C CE1 . PHE E 1 261 ? 157.288 -25.004 34.346  1.000 32.780  ? 278 PHE EEE CE1 1 
ATOM 9927  C CE2 . PHE E 1 261 ? 158.515 -24.595 36.341  1.000 32.460  ? 278 PHE EEE CE2 1 
ATOM 9928  C CZ  . PHE E 1 261 ? 157.325 -24.877 35.709  1.000 32.120  ? 278 PHE EEE CZ  1 
ATOM 9929  N N   . LYS E 1 262 ? 163.483 -22.569 32.628  1.000 37.790  ? 279 LYS EEE N   1 
ATOM 9930  C CA  . LYS E 1 262 ? 164.918 -22.780 32.351  1.000 38.800  ? 279 LYS EEE CA  1 
ATOM 9931  C C   . LYS E 1 262 ? 165.607 -22.839 33.702  1.000 40.540  ? 279 LYS EEE C   1 
ATOM 9932  O O   . LYS E 1 262 ? 165.609 -21.810 34.419  1.000 44.320  ? 279 LYS EEE O   1 
ATOM 9933  C CB  . LYS E 1 262 ? 165.453 -21.644 31.491  1.000 41.120  ? 279 LYS EEE CB  1 
ATOM 9934  C CG  . LYS E 1 262 ? 166.918 -21.734 31.086  1.000 44.570  ? 279 LYS EEE CG  1 
ATOM 9935  C CD  . LYS E 1 262 ? 167.298 -20.532 30.245  1.000 52.050  ? 279 LYS EEE CD  1 
ATOM 9936  C CE  . LYS E 1 262 ? 168.778 -20.457 29.965  1.000 59.540  ? 279 LYS EEE CE  1 
ATOM 9937  N NZ  . LYS E 1 262 ? 169.184 -19.107 29.541  1.000 64.460  ? 279 LYS EEE NZ  1 
ATOM 9938  N N   . VAL E 1 263 ? 166.137 -24.005 34.054  1.000 40.420  ? 280 VAL EEE N   1 
ATOM 9939  C CA  . VAL E 1 263 ? 166.784 -24.187 35.378  1.000 40.620  ? 280 VAL EEE CA  1 
ATOM 9940  C C   . VAL E 1 263 ? 168.286 -24.413 35.170  1.000 44.610  ? 280 VAL EEE C   1 
ATOM 9941  O O   . VAL E 1 263 ? 168.659 -25.356 34.466  1.000 48.210  ? 280 VAL EEE O   1 
ATOM 9942  C CB  . VAL E 1 263 ? 166.094 -25.315 36.155  1.000 39.210  ? 280 VAL EEE CB  1 
ATOM 9943  C CG1 . VAL E 1 263 ? 166.724 -25.521 37.515  1.000 37.560  ? 280 VAL EEE CG1 1 
ATOM 9944  C CG2 . VAL E 1 263 ? 164.602 -25.041 36.290  1.000 38.520  ? 280 VAL EEE CG2 1 
ATOM 9945  N N   . GLN E 1 264 ? 169.108 -23.517 35.713  1.000 46.990  ? 281 GLN EEE N   1 
ATOM 9946  C CA  . GLN E 1 264 ? 170.563 -23.728 35.906  1.000 50.250  ? 281 GLN EEE CA  1 
ATOM 9947  C C   . GLN E 1 264 ? 170.735 -24.775 37.012  1.000 46.230  ? 281 GLN EEE C   1 
ATOM 9948  O O   . GLN E 1 264 ? 170.066 -24.677 38.045  1.000 43.740  ? 281 GLN EEE O   1 
ATOM 9949  C CB  . GLN E 1 264 ? 171.258 -22.427 36.326  1.000 60.980  ? 281 GLN EEE CB  1 
ATOM 9950  C CG  . GLN E 1 264 ? 171.144 -21.267 35.336  1.000 63.580  ? 281 GLN EEE CG  1 
ATOM 9951  C CD  . GLN E 1 264 ? 171.942 -21.526 34.081  1.000 68.150  ? 281 GLN EEE CD  1 
ATOM 9952  O OE1 . GLN E 1 264 ? 172.858 -22.353 34.064  1.000 79.580  ? 281 GLN EEE OE1 1 
ATOM 9953  N NE2 . GLN E 1 264 ? 171.572 -20.835 33.017  1.000 66.410  ? 281 GLN EEE NE2 1 
ATOM 9954  N N   . LEU E 1 265 ? 171.619 -25.736 36.810  1.000 44.450  ? 282 LEU EEE N   1 
ATOM 9955  C CA  . LEU E 1 265 ? 171.957 -26.751 37.830  1.000 45.700  ? 282 LEU EEE CA  1 
ATOM 9956  C C   . LEU E 1 265 ? 173.482 -26.795 37.975  1.000 45.460  ? 282 LEU EEE C   1 
ATOM 9957  O O   . LEU E 1 265 ? 174.159 -26.479 37.003  1.000 48.150  ? 282 LEU EEE O   1 
ATOM 9958  C CB  . LEU E 1 265 ? 171.392 -28.085 37.345  1.000 47.110  ? 282 LEU EEE CB  1 
ATOM 9959  C CG  . LEU E 1 265 ? 169.867 -28.177 37.289  1.000 45.560  ? 282 LEU EEE CG  1 
ATOM 9960  C CD1 . LEU E 1 265 ? 169.405 -28.898 36.029  1.000 42.870  ? 282 LEU EEE CD1 1 
ATOM 9961  C CD2 . LEU E 1 265 ? 169.327 -28.888 38.531  1.000 47.040  ? 282 LEU EEE CD2 1 
ATOM 9962  N N   . ARG E 1 266 ? 173.990 -27.148 39.154  1.000 48.640  ? 283 ARG EEE N   1 
ATOM 9963  C CA  . ARG E 1 266 ? 175.433 -27.414 39.387  1.000 48.480  ? 283 ARG EEE CA  1 
ATOM 9964  C C   . ARG E 1 266 ? 175.569 -28.698 40.212  1.000 53.770  ? 283 ARG EEE C   1 
ATOM 9965  O O   . ARG E 1 266 ? 174.525 -29.217 40.676  1.000 66.800  ? 283 ARG EEE O   1 
ATOM 9966  C CB  . ARG E 1 266 ? 176.086 -26.215 40.076  1.000 45.410  ? 283 ARG EEE CB  1 
ATOM 9967  C CG  . ARG E 1 266 ? 175.720 -26.067 41.545  1.000 41.710  ? 283 ARG EEE CG  1 
ATOM 9968  C CD  . ARG E 1 266 ? 176.126 -24.714 42.093  1.000 43.700  ? 283 ARG EEE CD  1 
ATOM 9969  N NE  . ARG E 1 266 ? 175.685 -24.587 43.476  1.000 49.230  ? 283 ARG EEE NE  1 
ATOM 9970  C CZ  . ARG E 1 266 ? 175.583 -23.444 44.145  1.000 49.560  ? 283 ARG EEE CZ  1 
ATOM 9971  N NH1 . ARG E 1 266 ? 175.883 -22.310 43.540  1.000 53.800  ? 283 ARG EEE NH1 1 
ATOM 9972  N NH2 . ARG E 1 266 ? 175.169 -23.428 45.403  1.000 46.170  ? 283 ARG EEE NH2 1 
ATOM 9973  N N   . LYS E 1 267 ? 176.785 -29.192 40.394  1.000 53.870  ? 284 LYS EEE N   1 
ATOM 9974  C CA  . LYS E 1 267 ? 177.062 -30.465 41.109  1.000 54.700  ? 284 LYS EEE CA  1 
ATOM 9975  C C   . LYS E 1 267 ? 177.393 -30.190 42.573  1.000 52.560  ? 284 LYS EEE C   1 
ATOM 9976  O O   . LYS E 1 267 ? 178.336 -29.407 42.801  1.000 56.250  ? 284 LYS EEE O   1 
ATOM 9977  C CB  . LYS E 1 267 ? 178.218 -31.176 40.412  1.000 56.020  ? 284 LYS EEE CB  1 
ATOM 9978  C CG  . LYS E 1 267 ? 177.894 -31.645 39.010  1.000 59.870  ? 284 LYS EEE CG  1 
ATOM 9979  C CD  . LYS E 1 267 ? 178.994 -32.449 38.381  1.000 62.800  ? 284 LYS EEE CD  1 
ATOM 9980  C CE  . LYS E 1 267 ? 178.594 -32.978 37.027  1.000 62.380  ? 284 LYS EEE CE  1 
ATOM 9981  N NZ  . LYS E 1 267 ? 179.758 -33.500 36.281  1.000 65.340  ? 284 LYS EEE NZ  1 
ATOM 9982  N N   . ARG E 1 268 ? 176.766 -30.950 43.459  1.000 50.790  ? 285 ARG EEE N   1 
ATOM 9983  C CA  . ARG E 1 268 ? 177.031 -30.789 44.895  1.000 61.330  ? 285 ARG EEE CA  1 
ATOM 9984  C C   . ARG E 1 268 ? 177.539 -32.108 45.455  1.000 69.850  ? 285 ARG EEE C   1 
ATOM 9985  O O   . ARG E 1 268 ? 176.890 -33.126 45.201  1.000 74.810  ? 285 ARG EEE O   1 
ATOM 9986  C CB  . ARG E 1 268 ? 175.751 -30.362 45.612  1.000 63.240  ? 285 ARG EEE CB  1 
ATOM 9987  C CG  . ARG E 1 268 ? 175.986 -29.753 46.985  1.000 62.030  ? 285 ARG EEE CG  1 
ATOM 9988  C CD  . ARG E 1 268 ? 176.201 -28.258 46.916  1.000 59.780  ? 285 ARG EEE CD  1 
ATOM 9989  N NE  . ARG E 1 268 ? 176.596 -27.730 48.210  1.000 53.180  ? 285 ARG EEE NE  1 
ATOM 9990  C CZ  . ARG E 1 268 ? 176.221 -26.557 48.697  1.000 50.400  ? 285 ARG EEE CZ  1 
ATOM 9991  N NH1 . ARG E 1 268 ? 175.443 -25.762 47.988  1.000 57.780  ? 285 ARG EEE NH1 1 
ATOM 9992  N NH2 . ARG E 1 268 ? 176.635 -26.175 49.889  1.000 49.700  ? 285 ARG EEE NH2 1 
ATOM 9993  N N   . ARG E 1 269 ? 178.682 -32.089 46.127  1.000 73.070  ? 286 ARG EEE N   1 
ATOM 9994  C CA  . ARG E 1 269 ? 179.230 -33.268 46.844  1.000 73.870  ? 286 ARG EEE CA  1 
ATOM 9995  C C   . ARG E 1 269 ? 178.292 -33.509 48.045  1.000 69.800  ? 286 ARG EEE C   1 
ATOM 9996  O O   . ARG E 1 269 ? 177.828 -32.523 48.665  1.000 60.780  ? 286 ARG EEE O   1 
ATOM 9997  C CB  . ARG E 1 269 ? 180.710 -32.990 47.151  1.000 82.580  ? 286 ARG EEE CB  1 
ATOM 9998  N N   . VAL E 1 270 ? 177.991 -34.783 48.312  1.000 69.270  ? 287 VAL EEE N   1 
ATOM 9999  C CA  . VAL E 1 270 ? 176.968 -35.264 49.284  1.000 72.200  ? 287 VAL EEE CA  1 
ATOM 10000 C C   . VAL E 1 270 ? 177.515 -36.538 49.959  1.000 75.870  ? 287 VAL EEE C   1 
ATOM 10001 O O   . VAL E 1 270 ? 178.150 -37.341 49.248  1.000 80.400  ? 287 VAL EEE O   1 
ATOM 10002 C CB  . VAL E 1 270 ? 175.644 -35.516 48.532  1.000 74.540  ? 287 VAL EEE CB  1 
ATOM 10003 C CG1 . VAL E 1 270 ? 174.539 -36.079 49.415  1.000 82.490  ? 287 VAL EEE CG1 1 
ATOM 10004 C CG2 . VAL E 1 270 ? 175.149 -34.253 47.844  1.000 74.290  ? 287 VAL EEE CG2 1 
ATOM 10005 N N   . LYS E 1 271 ? 177.307 -36.712 51.275  1.000 76.850  ? 288 LYS EEE N   1 
ATOM 10006 C CA  . LYS E 1 271 ? 177.536 -37.998 52.002  1.000 75.980  ? 288 LYS EEE CA  1 
ATOM 10007 C C   . LYS E 1 271 ? 176.188 -38.725 52.163  1.000 76.190  ? 288 LYS EEE C   1 
ATOM 10008 O O   . LYS E 1 271 ? 175.247 -38.078 52.678  1.000 83.310  ? 288 LYS EEE O   1 
ATOM 10009 C CB  . LYS E 1 271 ? 178.214 -37.762 53.361  1.000 72.610  ? 288 LYS EEE CB  1 
ATOM 10010 N N   . ASN E 1 272 ? 176.097 -39.991 51.706  1.000 74.200  ? 289 ASN EEE N   1 
ATOM 10011 C CA  . ASN E 1 272 ? 175.091 -41.024 52.086  1.000 71.930  ? 289 ASN EEE CA  1 
ATOM 10012 C C   . ASN E 1 272 ? 173.686 -40.630 51.613  1.000 71.070  ? 289 ASN EEE C   1 
ATOM 10013 O O   . ASN E 1 272 ? 173.225 -40.888 50.510  1.000 67.630  ? 289 ASN EEE O   1 
ATOM 10014 C CB  . ASN E 1 272 ? 175.118 -41.251 53.587  1.000 68.040  ? 289 ASN EEE CB  1 
ATOM 10015 N N   . SER F 2 2   ? 118.579 -40.049 32.749  1.000 54.840  ? 2   SER FFF N   1 
ATOM 10016 C CA  . SER F 2 2   ? 119.065 -40.711 31.466  1.000 56.480  ? 2   SER FFF CA  1 
ATOM 10017 C C   . SER F 2 2   ? 118.083 -40.544 30.281  1.000 59.030  ? 2   SER FFF C   1 
ATOM 10018 O O   . SER F 2 2   ? 118.532 -40.745 29.133  1.000 59.140  ? 2   SER FFF O   1 
ATOM 10019 C CB  . SER F 2 2   ? 119.354 -42.162 31.707  1.000 55.330  ? 2   SER FFF CB  1 
ATOM 10020 O OG  . SER F 2 2   ? 120.272 -42.663 30.749  1.000 55.560  ? 2   SER FFF OG  1 
ATOM 10021 N N   . VAL F 2 3   ? 116.801 -40.223 30.524  1.000 59.480  ? 3   VAL FFF N   1 
ATOM 10022 C CA  . VAL F 2 3   ? 115.815 -39.748 29.503  1.000 60.900  ? 3   VAL FFF CA  1 
ATOM 10023 C C   . VAL F 2 3   ? 115.285 -38.378 29.954  1.000 53.720  ? 3   VAL FFF C   1 
ATOM 10024 O O   . VAL F 2 3   ? 115.199 -38.124 31.163  1.000 53.960  ? 3   VAL FFF O   1 
ATOM 10025 C CB  . VAL F 2 3   ? 114.660 -40.752 29.282  1.000 67.380  ? 3   VAL FFF CB  1 
ATOM 10026 C CG1 . VAL F 2 3   ? 113.983 -41.145 30.588  1.000 59.930  ? 3   VAL FFF CG1 1 
ATOM 10027 C CG2 . VAL F 2 3   ? 113.661 -40.247 28.243  1.000 77.020  ? 3   VAL FFF CG2 1 
ATOM 10028 N N   . LEU F 2 4   ? 114.932 -37.507 29.017  1.000 44.910  ? 4   LEU FFF N   1 
ATOM 10029 C CA  . LEU F 2 4   ? 114.351 -36.187 29.354  1.000 42.070  ? 4   LEU FFF CA  1 
ATOM 10030 C C   . LEU F 2 4   ? 112.833 -36.327 29.418  1.000 41.570  ? 4   LEU FFF C   1 
ATOM 10031 O O   . LEU F 2 4   ? 112.253 -36.892 28.482  1.000 50.940  ? 4   LEU FFF O   1 
ATOM 10032 C CB  . LEU F 2 4   ? 114.804 -35.145 28.323  1.000 40.540  ? 4   LEU FFF CB  1 
ATOM 10033 C CG  . LEU F 2 4   ? 116.313 -34.951 28.205  1.000 39.300  ? 4   LEU FFF CG  1 
ATOM 10034 C CD1 . LEU F 2 4   ? 116.640 -33.775 27.310  1.000 40.600  ? 4   LEU FFF CD1 1 
ATOM 10035 C CD2 . LEU F 2 4   ? 116.960 -34.753 29.552  1.000 38.090  ? 4   LEU FFF CD2 1 
ATOM 10036 N N   . THR F 2 5   ? 112.248 -35.857 30.515  1.000 37.670  ? 5   THR FFF N   1 
ATOM 10037 C CA  . THR F 2 5   ? 110.798 -35.936 30.819  1.000 37.280  ? 5   THR FFF CA  1 
ATOM 10038 C C   . THR F 2 5   ? 110.198 -34.546 30.619  1.000 32.310  ? 5   THR FFF C   1 
ATOM 10039 O O   . THR F 2 5   ? 110.587 -33.627 31.359  1.000 29.680  ? 5   THR FFF O   1 
ATOM 10040 C CB  . THR F 2 5   ? 110.611 -36.522 32.229  1.000 39.680  ? 5   THR FFF CB  1 
ATOM 10041 O OG1 . THR F 2 5   ? 111.490 -37.650 32.307  1.000 47.010  ? 5   THR FFF OG1 1 
ATOM 10042 C CG2 . THR F 2 5   ? 109.203 -36.959 32.564  1.000 37.910  ? 5   THR FFF CG2 1 
ATOM 10043 N N   . GLN F 2 6   ? 109.315 -34.390 29.629  1.000 31.910  ? 6   GLN FFF N   1 
ATOM 10044 C CA  . GLN F 2 6   ? 108.501 -33.152 29.445  1.000 33.250  ? 6   GLN FFF CA  1 
ATOM 10045 C C   . GLN F 2 6   ? 107.017 -33.510 29.315  1.000 39.280  ? 6   GLN FFF C   1 
ATOM 10046 O O   . GLN F 2 6   ? 106.663 -34.604 28.874  1.000 37.250  ? 6   GLN FFF O   1 
ATOM 10047 C CB  . GLN F 2 6   ? 109.051 -32.327 28.281  1.000 31.520  ? 6   GLN FFF CB  1 
ATOM 10048 C CG  . GLN F 2 6   ? 108.758 -32.913 26.908  1.000 33.400  ? 6   GLN FFF CG  1 
ATOM 10049 C CD  . GLN F 2 6   ? 109.582 -32.259 25.826  1.000 32.770  ? 6   GLN FFF CD  1 
ATOM 10050 O OE1 . GLN F 2 6   ? 110.799 -32.428 25.766  1.000 31.910  ? 6   GLN FFF OE1 1 
ATOM 10051 N NE2 . GLN F 2 6   ? 108.916 -31.498 24.969  1.000 29.780  ? 6   GLN FFF NE2 1 
ATOM 10052 N N   . PRO F 2 7   ? 106.094 -32.629 29.768  1.000 50.380  ? 7   PRO FFF N   1 
ATOM 10053 C CA  . PRO F 2 7   ? 104.660 -32.894 29.684  1.000 52.890  ? 7   PRO FFF CA  1 
ATOM 10054 C C   . PRO F 2 7   ? 104.252 -33.256 28.271  1.000 49.320  ? 7   PRO FFF C   1 
ATOM 10055 O O   . PRO F 2 7   ? 104.639 -32.559 27.346  1.000 49.770  ? 7   PRO FFF O   1 
ATOM 10056 C CB  . PRO F 2 7   ? 104.025 -31.560 30.118  1.000 57.790  ? 7   PRO FFF CB  1 
ATOM 10057 C CG  . PRO F 2 7   ? 105.054 -30.931 31.048  1.000 57.940  ? 7   PRO FFF CG  1 
ATOM 10058 C CD  . PRO F 2 7   ? 106.375 -31.339 30.423  1.000 60.420  ? 7   PRO FFF CD  1 
ATOM 10059 N N   . PRO F 2 8   ? 103.497 -34.365 28.050  1.000 47.830  ? 8   PRO FFF N   1 
ATOM 10060 C CA  . PRO F 2 8   ? 103.030 -34.731 26.709  1.000 45.700  ? 8   PRO FFF CA  1 
ATOM 10061 C C   . PRO F 2 8   ? 102.162 -33.648 26.068  1.000 41.140  ? 8   PRO FFF C   1 
ATOM 10062 O O   . PRO F 2 8   ? 102.237 -33.491 24.880  1.000 45.230  ? 8   PRO FFF O   1 
ATOM 10063 C CB  . PRO F 2 8   ? 102.237 -36.022 26.915  1.000 45.440  ? 8   PRO FFF CB  1 
ATOM 10064 C CG  . PRO F 2 8   ? 102.892 -36.600 28.148  1.000 49.340  ? 8   PRO FFF CG  1 
ATOM 10065 C CD  . PRO F 2 8   ? 103.119 -35.389 29.037  1.000 47.290  ? 8   PRO FFF CD  1 
ATOM 10066 N N   . SER F 2 9   ? 101.397 -32.916 26.869  1.000 43.070  ? 9   SER FFF N   1 
ATOM 10067 C CA  . SER F 2 9   ? 100.594 -31.766 26.380  1.000 47.570  ? 9   SER FFF CA  1 
ATOM 10068 C C   . SER F 2 9   ? 100.654 -30.593 27.360  1.000 48.140  ? 9   SER FFF C   1 
ATOM 10069 O O   . SER F 2 9   ? 100.927 -30.801 28.553  1.000 54.510  ? 9   SER FFF O   1 
ATOM 10070 C CB  . SER F 2 9   ? 99.172  -32.179 26.099  1.000 50.700  ? 9   SER FFF CB  1 
ATOM 10071 O OG  . SER F 2 9   ? 98.504  -32.537 27.297  1.000 53.300  ? 9   SER FFF OG  1 
ATOM 10072 N N   . ALA F 2 10  ? 100.420 -29.402 26.822  1.000 50.010  ? 10  ALA FFF N   1 
ATOM 10073 C CA  . ALA F 2 10  ? 100.247 -28.129 27.552  1.000 54.680  ? 10  ALA FFF CA  1 
ATOM 10074 C C   . ALA F 2 10  ? 99.307  -27.255 26.736  1.000 58.770  ? 10  ALA FFF C   1 
ATOM 10075 O O   . ALA F 2 10  ? 99.183  -27.505 25.520  1.000 62.250  ? 10  ALA FFF O   1 
ATOM 10076 C CB  . ALA F 2 10  ? 101.561 -27.443 27.769  1.000 53.890  ? 10  ALA FFF CB  1 
ATOM 10077 N N   . SER F 2 11  ? 98.632  -26.313 27.392  1.000 59.870  ? 11  SER FFF N   1 
ATOM 10078 C CA  . SER F 2 11  ? 97.657  -25.399 26.747  1.000 60.900  ? 11  SER FFF CA  1 
ATOM 10079 C C   . SER F 2 11  ? 97.531  -24.104 27.549  1.000 57.550  ? 11  SER FFF C   1 
ATOM 10080 O O   . SER F 2 11  ? 98.027  -24.061 28.701  1.000 54.490  ? 11  SER FFF O   1 
ATOM 10081 C CB  . SER F 2 11  ? 96.321  -26.061 26.589  1.000 62.220  ? 11  SER FFF CB  1 
ATOM 10082 O OG  . SER F 2 11  ? 95.803  -26.394 27.867  1.000 65.590  ? 11  SER FFF OG  1 
ATOM 10083 N N   . GLY F 2 12  ? 96.882  -23.107 26.940  1.000 57.950  ? 12  GLY FFF N   1 
ATOM 10084 C CA  . GLY F 2 12  ? 96.659  -21.769 27.510  1.000 60.510  ? 12  GLY FFF CA  1 
ATOM 10085 C C   . GLY F 2 12  ? 95.682  -20.954 26.681  1.000 62.990  ? 12  GLY FFF C   1 
ATOM 10086 O O   . GLY F 2 12  ? 95.392  -21.325 25.508  1.000 66.620  ? 12  GLY FFF O   1 
ATOM 10087 N N   . THR F 2 13  ? 95.189  -19.866 27.279  1.000 66.670  ? 13  THR FFF N   1 
ATOM 10088 C CA  . THR F 2 13  ? 94.285  -18.862 26.651  1.000 66.100  ? 13  THR FFF CA  1 
ATOM 10089 C C   . THR F 2 13  ? 95.143  -17.741 26.062  1.000 63.880  ? 13  THR FFF C   1 
ATOM 10090 O O   . THR F 2 13  ? 96.139  -17.329 26.663  1.000 57.150  ? 13  THR FFF O   1 
ATOM 10091 C CB  . THR F 2 13  ? 93.250  -18.386 27.674  1.000 65.840  ? 13  THR FFF CB  1 
ATOM 10092 O OG1 . THR F 2 13  ? 93.980  -18.067 28.845  1.000 58.440  ? 13  THR FFF OG1 1 
ATOM 10093 C CG2 . THR F 2 13  ? 92.210  -19.437 28.003  1.000 66.730  ? 13  THR FFF CG2 1 
ATOM 10094 N N   . PRO F 2 14  ? 94.824  -17.234 24.844  1.000 61.340  ? 14  PRO FFF N   1 
ATOM 10095 C CA  . PRO F 2 14  ? 95.670  -16.230 24.192  1.000 60.800  ? 14  PRO FFF CA  1 
ATOM 10096 C C   . PRO F 2 14  ? 96.028  -15.109 25.178  1.000 67.740  ? 14  PRO FFF C   1 
ATOM 10097 O O   . PRO F 2 14  ? 95.153  -14.693 25.908  1.000 79.700  ? 14  PRO FFF O   1 
ATOM 10098 C CB  . PRO F 2 14  ? 94.807  -15.721 23.034  1.000 59.350  ? 14  PRO FFF CB  1 
ATOM 10099 C CG  . PRO F 2 14  ? 93.928  -16.910 22.695  1.000 66.460  ? 14  PRO FFF CG  1 
ATOM 10100 C CD  . PRO F 2 14  ? 93.660  -17.604 24.020  1.000 63.150  ? 14  PRO FFF CD  1 
ATOM 10101 N N   . GLY F 2 15  ? 97.298  -14.695 25.216  1.000 69.780  ? 15  GLY FFF N   1 
ATOM 10102 C CA  . GLY F 2 15  ? 97.796  -13.618 26.094  1.000 64.900  ? 15  GLY FFF CA  1 
ATOM 10103 C C   . GLY F 2 15  ? 98.399  -14.163 27.377  1.000 64.050  ? 15  GLY FFF C   1 
ATOM 10104 O O   . GLY F 2 15  ? 99.153  -13.413 28.024  1.000 58.750  ? 15  GLY FFF O   1 
ATOM 10105 N N   . GLN F 2 16  ? 98.099  -15.420 27.735  1.000 66.210  ? 16  GLN FFF N   1 
ATOM 10106 C CA  . GLN F 2 16  ? 98.623  -16.081 28.959  1.000 72.950  ? 16  GLN FFF CA  1 
ATOM 10107 C C   . GLN F 2 16  ? 100.118 -16.381 28.790  1.000 68.870  ? 16  GLN FFF C   1 
ATOM 10108 O O   . GLN F 2 16  ? 100.642 -16.305 27.650  1.000 74.260  ? 16  GLN FFF O   1 
ATOM 10109 C CB  . GLN F 2 16  ? 97.890  -17.391 29.277  1.000 77.160  ? 16  GLN FFF CB  1 
ATOM 10110 C CG  . GLN F 2 16  ? 96.766  -17.236 30.293  1.000 83.370  ? 16  GLN FFF CG  1 
ATOM 10111 C CD  . GLN F 2 16  ? 96.132  -18.564 30.650  1.000 90.480  ? 16  GLN FFF CD  1 
ATOM 10112 O OE1 . GLN F 2 16  ? 96.009  -19.463 29.819  1.000 82.630  ? 16  GLN FFF OE1 1 
ATOM 10113 N NE2 . GLN F 2 16  ? 95.716  -18.703 31.901  1.000 93.640  ? 16  GLN FFF NE2 1 
ATOM 10114 N N   . ARG F 2 17  ? 100.773 -16.712 29.907  1.000 68.940  ? 17  ARG FFF N   1 
ATOM 10115 C CA  . ARG F 2 17  ? 102.109 -17.363 29.975  1.000 67.030  ? 17  ARG FFF CA  1 
ATOM 10116 C C   . ARG F 2 17  ? 101.883 -18.864 30.198  1.000 66.130  ? 17  ARG FFF C   1 
ATOM 10117 O O   . ARG F 2 17  ? 101.207 -19.224 31.179  1.000 68.040  ? 17  ARG FFF O   1 
ATOM 10118 C CB  . ARG F 2 17  ? 102.981 -16.753 31.078  1.000 57.580  ? 17  ARG FFF CB  1 
ATOM 10119 N N   . VAL F 2 18  ? 102.401 -19.698 29.290  1.000 59.320  ? 18  VAL FFF N   1 
ATOM 10120 C CA  . VAL F 2 18  ? 102.450 -21.180 29.444  1.000 52.880  ? 18  VAL FFF CA  1 
ATOM 10121 C C   . VAL F 2 18  ? 103.889 -21.558 29.773  1.000 50.850  ? 18  VAL FFF C   1 
ATOM 10122 O O   . VAL F 2 18  ? 104.801 -20.877 29.276  1.000 53.260  ? 18  VAL FFF O   1 
ATOM 10123 C CB  . VAL F 2 18  ? 101.985 -21.913 28.187  1.000 51.190  ? 18  VAL FFF CB  1 
ATOM 10124 C CG1 . VAL F 2 18  ? 101.762 -23.383 28.473  1.000 48.740  ? 18  VAL FFF CG1 1 
ATOM 10125 C CG2 . VAL F 2 18  ? 100.736 -21.268 27.618  1.000 56.730  ? 18  VAL FFF CG2 1 
ATOM 10126 N N   . THR F 2 19  ? 104.062 -22.594 30.588  1.000 46.470  ? 19  THR FFF N   1 
ATOM 10127 C CA  . THR F 2 19  ? 105.386 -23.063 31.062  1.000 47.440  ? 19  THR FFF CA  1 
ATOM 10128 C C   . THR F 2 19  ? 105.497 -24.573 30.769  1.000 48.350  ? 19  THR FFF C   1 
ATOM 10129 O O   . THR F 2 19  ? 104.684 -25.337 31.285  1.000 49.810  ? 19  THR FFF O   1 
ATOM 10130 C CB  . THR F 2 19  ? 105.597 -22.626 32.518  1.000 47.690  ? 19  THR FFF CB  1 
ATOM 10131 O OG1 . THR F 2 19  ? 106.997 -22.773 32.798  1.000 52.480  ? 19  THR FFF OG1 1 
ATOM 10132 C CG2 . THR F 2 19  ? 104.738 -23.387 33.512  1.000 49.260  ? 19  THR FFF CG2 1 
ATOM 10133 N N   . ILE F 2 20  ? 106.449 -24.975 29.923  1.000 44.900  ? 20  ILE FFF N   1 
ATOM 10134 C CA  . ILE F 2 20  ? 106.757 -26.406 29.628  1.000 44.480  ? 20  ILE FFF CA  1 
ATOM 10135 C C   . ILE F 2 20  ? 108.070 -26.758 30.330  1.000 41.830  ? 20  ILE FFF C   1 
ATOM 10136 O O   . ILE F 2 20  ? 109.099 -26.120 30.016  1.000 48.970  ? 20  ILE FFF O   1 
ATOM 10137 C CB  . ILE F 2 20  ? 106.875 -26.675 28.112  1.000 44.840  ? 20  ILE FFF CB  1 
ATOM 10138 C CG1 . ILE F 2 20  ? 105.751 -26.021 27.309  1.000 44.820  ? 20  ILE FFF CG1 1 
ATOM 10139 C CG2 . ILE F 2 20  ? 106.959 -28.169 27.865  1.000 47.300  ? 20  ILE FFF CG2 1 
ATOM 10140 C CD1 . ILE F 2 20  ? 105.946 -26.099 25.796  1.000 43.740  ? 20  ILE FFF CD1 1 
ATOM 10141 N N   . SER F 2 21  ? 108.056 -27.763 31.199  1.000 38.220  ? 21  SER FFF N   1 
ATOM 10142 C CA  . SER F 2 21  ? 109.256 -28.207 31.950  1.000 39.490  ? 21  SER FFF CA  1 
ATOM 10143 C C   . SER F 2 21  ? 109.961 -29.330 31.183  1.000 38.380  ? 21  SER FFF C   1 
ATOM 10144 O O   . SER F 2 21  ? 109.306 -30.044 30.416  1.000 39.700  ? 21  SER FFF O   1 
ATOM 10145 C CB  . SER F 2 21  ? 108.902 -28.637 33.346  1.000 42.850  ? 21  SER FFF CB  1 
ATOM 10146 O OG  . SER F 2 21  ? 107.955 -29.708 33.317  1.000 47.860  ? 21  SER FFF OG  1 
ATOM 10147 N N   . CYS F 2 22  ? 111.272 -29.444 31.380  1.000 37.250  ? 22  CYS FFF N   1 
ATOM 10148 C CA  . CYS F 2 22  ? 112.115 -30.572 30.921  1.000 36.670  ? 22  CYS FFF CA  1 
ATOM 10149 C C   . CYS F 2 22  ? 113.034 -31.006 32.060  1.000 34.940  ? 22  CYS FFF C   1 
ATOM 10150 O O   . CYS F 2 22  ? 113.838 -30.192 32.508  1.000 36.700  ? 22  CYS FFF O   1 
ATOM 10151 C CB  . CYS F 2 22  ? 112.925 -30.196 29.691  1.000 40.130  ? 22  CYS FFF CB  1 
ATOM 10152 S SG  . CYS F 2 22  ? 113.237 -31.679 28.706  1.000 46.960  ? 22  CYS FFF SG  1 
ATOM 10153 N N   . SER F 2 23  ? 112.852 -32.224 32.555  1.000 35.370  ? 23  SER FFF N   1 
ATOM 10154 C CA  . SER F 2 23  ? 113.578 -32.780 33.716  1.000 37.410  ? 23  SER FFF CA  1 
ATOM 10155 C C   . SER F 2 23  ? 114.499 -33.897 33.230  1.000 39.050  ? 23  SER FFF C   1 
ATOM 10156 O O   . SER F 2 23  ? 114.016 -34.780 32.494  1.000 43.940  ? 23  SER FFF O   1 
ATOM 10157 C CB  . SER F 2 23  ? 112.607 -33.268 34.752  1.000 39.120  ? 23  SER FFF CB  1 
ATOM 10158 O OG  . SER F 2 23  ? 113.280 -33.956 35.796  1.000 44.570  ? 23  SER FFF OG  1 
ATOM 10159 N N   . GLY F 2 24  ? 115.770 -33.845 33.627  1.000 36.550  ? 24  GLY FFF N   1 
ATOM 10160 C CA  . GLY F 2 24  ? 116.791 -34.860 33.300  1.000 35.230  ? 24  GLY FFF CA  1 
ATOM 10161 C C   . GLY F 2 24  ? 117.544 -35.311 34.532  1.000 34.320  ? 24  GLY FFF C   1 
ATOM 10162 O O   . GLY F 2 24  ? 116.926 -35.332 35.595  1.000 31.340  ? 24  GLY FFF O   1 
ATOM 10163 N N   . GLY F 2 25  ? 118.827 -35.629 34.385  1.000 36.970  ? 25  GLY FFF N   1 
ATOM 10164 C CA  . GLY F 2 25  ? 119.709 -36.023 35.500  1.000 41.550  ? 25  GLY FFF CA  1 
ATOM 10165 C C   . GLY F 2 25  ? 121.151 -35.604 35.272  1.000 40.960  ? 25  GLY FFF C   1 
ATOM 10166 O O   . GLY F 2 25  ? 121.441 -35.015 34.206  1.000 39.680  ? 25  GLY FFF O   1 
ATOM 10167 N N   . SER F 2 26  ? 122.030 -35.903 36.236  1.000 39.020  ? 26  SER FFF N   1 
ATOM 10168 C CA  . SER F 2 26  ? 123.415 -35.365 36.270  1.000 39.650  ? 26  SER FFF CA  1 
ATOM 10169 C C   . SER F 2 26  ? 124.140 -35.692 34.957  1.000 39.130  ? 26  SER FFF C   1 
ATOM 10170 O O   . SER F 2 26  ? 124.912 -34.846 34.482  1.000 35.820  ? 26  SER FFF O   1 
ATOM 10171 C CB  . SER F 2 26  ? 124.163 -35.865 37.480  1.000 38.780  ? 26  SER FFF CB  1 
ATOM 10172 O OG  . SER F 2 26  ? 124.471 -37.238 37.360  1.000 36.810  ? 26  SER FFF OG  1 
ATOM 10173 N N   . SER F 2 27  ? 123.876 -36.867 34.383  1.000 42.940  ? 27  SER FFF N   1 
ATOM 10174 C CA  . SER F 2 27  ? 124.527 -37.387 33.151  1.000 45.000  ? 27  SER FFF CA  1 
ATOM 10175 C C   . SER F 2 27  ? 124.178 -36.532 31.920  1.000 42.470  ? 27  SER FFF C   1 
ATOM 10176 O O   . SER F 2 27  ? 124.995 -36.488 30.984  1.000 42.560  ? 27  SER FFF O   1 
ATOM 10177 C CB  . SER F 2 27  ? 124.150 -38.845 32.946  1.000 47.700  ? 27  SER FFF CB  1 
ATOM 10178 O OG  . SER F 2 27  ? 122.738 -39.022 32.845  1.000 46.070  ? 27  SER FFF OG  1 
ATOM 10179 N N   . ASN F 2 28  ? 123.014 -35.883 31.899  1.000 39.650  ? 28  ASN FFF N   1 
ATOM 10180 C CA  . ASN F 2 28  ? 122.596 -35.036 30.757  1.000 37.910  ? 28  ASN FFF CA  1 
ATOM 10181 C C   . ASN F 2 28  ? 122.530 -33.570 31.227  1.000 36.420  ? 28  ASN FFF C   1 
ATOM 10182 O O   . ASN F 2 28  ? 123.583 -32.880 31.171  1.000 38.180  ? 28  ASN FFF O   1 
ATOM 10183 C CB  . ASN F 2 28  ? 121.332 -35.586 30.080  1.000 36.410  ? 28  ASN FFF CB  1 
ATOM 10184 C CG  . ASN F 2 28  ? 120.220 -35.939 31.033  1.000 33.010  ? 28  ASN FFF CG  1 
ATOM 10185 O OD1 . ASN F 2 28  ? 119.727 -35.072 31.730  1.000 30.920  ? 28  ASN FFF OD1 1 
ATOM 10186 N ND2 . ASN F 2 28  ? 119.807 -37.190 31.052  1.000 32.520  ? 28  ASN FFF ND2 1 
ATOM 10187 N N   . ILE F 2 29  ? 121.353 -33.114 31.669  1.000 31.830  ? 29  ILE FFF N   1 
ATOM 10188 C CA  . ILE F 2 29  ? 121.037 -31.664 31.846  1.000 31.960  ? 29  ILE FFF CA  1 
ATOM 10189 C C   . ILE F 2 29  ? 121.920 -31.072 32.949  1.000 32.390  ? 29  ILE FFF C   1 
ATOM 10190 O O   . ILE F 2 29  ? 122.185 -29.844 32.886  1.000 42.930  ? 29  ILE FFF O   1 
ATOM 10191 C CB  . ILE F 2 29  ? 119.536 -31.425 32.112  1.000 29.320  ? 29  ILE FFF CB  1 
ATOM 10192 C CG1 . ILE F 2 29  ? 118.692 -31.813 30.898  1.000 30.110  ? 29  ILE FFF CG1 1 
ATOM 10193 C CG2 . ILE F 2 29  ? 119.291 -29.994 32.533  1.000 28.360  ? 29  ILE FFF CG2 1 
ATOM 10194 C CD1 . ILE F 2 29  ? 117.229 -31.449 30.969  1.000 31.000  ? 29  ILE FFF CD1 1 
ATOM 10195 N N   . GLY F 2 30  ? 122.359 -31.891 33.902  1.000 29.380  ? 30  GLY FFF N   1 
ATOM 10196 C CA  . GLY F 2 30  ? 123.233 -31.472 35.010  1.000 30.320  ? 30  GLY FFF CA  1 
ATOM 10197 C C   . GLY F 2 30  ? 124.491 -30.837 34.476  1.000 30.950  ? 30  GLY FFF C   1 
ATOM 10198 O O   . GLY F 2 30  ? 124.767 -29.652 34.843  1.000 35.230  ? 30  GLY FFF O   1 
ATOM 10199 N N   . SER F 2 31  ? 125.180 -31.533 33.569  1.000 31.660  ? 31  SER FFF N   1 
ATOM 10200 C CA  . SER F 2 31  ? 126.499 -31.047 33.067  1.000 34.790  ? 31  SER FFF CA  1 
ATOM 10201 C C   . SER F 2 31  ? 126.452 -30.666 31.586  1.000 30.360  ? 31  SER FFF C   1 
ATOM 10202 O O   . SER F 2 31  ? 127.530 -30.297 31.103  1.000 26.440  ? 31  SER FFF O   1 
ATOM 10203 C CB  . SER F 2 31  ? 127.660 -31.987 33.387  1.000 39.850  ? 31  SER FFF CB  1 
ATOM 10204 O OG  . SER F 2 31  ? 127.473 -33.228 32.738  1.000 53.880  ? 31  SER FFF OG  1 
ATOM 10205 N N   . ASN F 2 32  ? 125.285 -30.675 30.920  1.000 29.080  ? 32  ASN FFF N   1 
ATOM 10206 C CA  . ASN F 2 32  ? 125.163 -30.280 29.479  1.000 26.760  ? 32  ASN FFF CA  1 
ATOM 10207 C C   . ASN F 2 32  ? 123.995 -29.321 29.248  1.000 27.570  ? 32  ASN FFF C   1 
ATOM 10208 O O   . ASN F 2 32  ? 122.999 -29.364 29.964  1.000 31.230  ? 32  ASN FFF O   1 
ATOM 10209 C CB  . ASN F 2 32  ? 125.145 -31.510 28.562  1.000 24.440  ? 32  ASN FFF CB  1 
ATOM 10210 C CG  . ASN F 2 32  ? 126.346 -32.397 28.811  1.000 23.070  ? 32  ASN FFF CG  1 
ATOM 10211 O OD1 . ASN F 2 32  ? 126.387 -33.072 29.821  1.000 22.980  ? 32  ASN FFF OD1 1 
ATOM 10212 N ND2 . ASN F 2 32  ? 127.428 -32.201 28.077  1.000 22.380  ? 32  ASN FFF ND2 1 
ATOM 10213 N N   . PRO F 2 33  ? 124.102 -28.408 28.248  1.000 27.270  ? 33  PRO FFF N   1 
ATOM 10214 C CA  . PRO F 2 33  ? 123.054 -27.441 27.942  1.000 27.950  ? 33  PRO FFF CA  1 
ATOM 10215 C C   . PRO F 2 33  ? 121.851 -28.042 27.216  1.000 29.750  ? 33  PRO FFF C   1 
ATOM 10216 O O   . PRO F 2 33  ? 122.045 -28.950 26.420  1.000 35.770  ? 33  PRO FFF O   1 
ATOM 10217 C CB  . PRO F 2 33  ? 123.670 -26.434 26.957  1.000 26.020  ? 33  PRO FFF CB  1 
ATOM 10218 C CG  . PRO F 2 33  ? 125.118 -26.751 26.973  1.000 27.490  ? 33  PRO FFF CG  1 
ATOM 10219 C CD  . PRO F 2 33  ? 125.222 -28.230 27.327  1.000 27.790  ? 33  PRO FFF CD  1 
ATOM 10220 N N   . VAL F 2 34  ? 120.673 -27.465 27.460  1.000 30.070  ? 34  VAL FFF N   1 
ATOM 10221 C CA  . VAL F 2 34  ? 119.391 -27.808 26.783  1.000 30.920  ? 34  VAL FFF CA  1 
ATOM 10222 C C   . VAL F 2 34  ? 119.115 -26.821 25.646  1.000 32.140  ? 34  VAL FFF C   1 
ATOM 10223 O O   . VAL F 2 34  ? 119.046 -25.604 25.945  1.000 31.910  ? 34  VAL FFF O   1 
ATOM 10224 C CB  . VAL F 2 34  ? 118.240 -27.774 27.796  1.000 29.780  ? 34  VAL FFF CB  1 
ATOM 10225 C CG1 . VAL F 2 34  ? 116.901 -28.047 27.118  1.000 29.700  ? 34  VAL FFF CG1 1 
ATOM 10226 C CG2 . VAL F 2 34  ? 118.498 -28.749 28.933  1.000 30.530  ? 34  VAL FFF CG2 1 
ATOM 10227 N N   . ASN F 2 35  ? 118.928 -27.315 24.418  1.000 31.100  ? 35  ASN FFF N   1 
ATOM 10228 C CA  . ASN F 2 35  ? 118.266 -26.535 23.338  1.000 32.090  ? 35  ASN FFF CA  1 
ATOM 10229 C C   . ASN F 2 35  ? 116.788 -26.947 23.280  1.000 33.750  ? 35  ASN FFF C   1 
ATOM 10230 O O   . ASN F 2 35  ? 116.479 -28.132 23.551  1.000 31.860  ? 35  ASN FFF O   1 
ATOM 10231 C CB  . ASN F 2 35  ? 118.932 -26.685 21.970  1.000 33.920  ? 35  ASN FFF CB  1 
ATOM 10232 C CG  . ASN F 2 35  ? 120.361 -26.177 21.914  1.000 34.110  ? 35  ASN FFF CG  1 
ATOM 10233 O OD1 . ASN F 2 35  ? 121.065 -26.213 22.924  1.000 31.260  ? 35  ASN FFF OD1 1 
ATOM 10234 N ND2 . ASN F 2 35  ? 120.811 -25.743 20.738  1.000 28.340  ? 35  ASN FFF ND2 1 
ATOM 10235 N N   . TRP F 2 36  ? 115.907 -25.982 22.985  1.000 34.940  ? 36  TRP FFF N   1 
ATOM 10236 C CA  . TRP F 2 36  ? 114.465 -26.179 22.673  1.000 32.900  ? 36  TRP FFF CA  1 
ATOM 10237 C C   . TRP F 2 36  ? 114.260 -26.012 21.165  1.000 32.990  ? 36  TRP FFF C   1 
ATOM 10238 O O   . TRP F 2 36  ? 114.784 -25.037 20.609  1.000 38.400  ? 36  TRP FFF O   1 
ATOM 10239 C CB  . TRP F 2 36  ? 113.602 -25.189 23.453  1.000 32.530  ? 36  TRP FFF CB  1 
ATOM 10240 C CG  . TRP F 2 36  ? 113.518 -25.469 24.920  1.000 33.810  ? 36  TRP FFF CG  1 
ATOM 10241 C CD1 . TRP F 2 36  ? 114.319 -24.973 25.905  1.000 33.730  ? 36  TRP FFF CD1 1 
ATOM 10242 C CD2 . TRP F 2 36  ? 112.556 -26.311 25.573  1.000 35.670  ? 36  TRP FFF CD2 1 
ATOM 10243 N NE1 . TRP F 2 36  ? 113.923 -25.444 27.127  1.000 33.100  ? 36  TRP FFF NE1 1 
ATOM 10244 C CE2 . TRP F 2 36  ? 112.860 -26.291 26.947  1.000 35.000  ? 36  TRP FFF CE2 1 
ATOM 10245 C CE3 . TRP F 2 36  ? 111.483 -27.092 25.125  1.000 36.560  ? 36  TRP FFF CE3 1 
ATOM 10246 C CZ2 . TRP F 2 36  ? 112.107 -27.005 27.876  1.000 36.250  ? 36  TRP FFF CZ2 1 
ATOM 10247 C CZ3 . TRP F 2 36  ? 110.740 -27.796 26.047  1.000 34.320  ? 36  TRP FFF CZ3 1 
ATOM 10248 C CH2 . TRP F 2 36  ? 111.054 -27.753 27.404  1.000 35.740  ? 36  TRP FFF CH2 1 
ATOM 10249 N N   . PHE F 2 37  ? 113.517 -26.903 20.520  1.000 32.680  ? 37  PHE FFF N   1 
ATOM 10250 C CA  . PHE F 2 37  ? 113.172 -26.815 19.076  1.000 29.640  ? 37  PHE FFF CA  1 
ATOM 10251 C C   . PHE F 2 37  ? 111.652 -26.734 18.942  1.000 29.410  ? 37  PHE FFF C   1 
ATOM 10252 O O   . PHE F 2 37  ? 110.941 -27.479 19.646  1.000 28.710  ? 37  PHE FFF O   1 
ATOM 10253 C CB  . PHE F 2 37  ? 113.753 -27.989 18.286  1.000 27.480  ? 37  PHE FFF CB  1 
ATOM 10254 C CG  . PHE F 2 37  ? 115.230 -28.150 18.478  1.000 26.830  ? 37  PHE FFF CG  1 
ATOM 10255 C CD1 . PHE F 2 37  ? 116.124 -27.379 17.778  1.000 28.530  ? 37  PHE FFF CD1 1 
ATOM 10256 C CD2 . PHE F 2 37  ? 115.726 -29.061 19.385  1.000 28.980  ? 37  PHE FFF CD2 1 
ATOM 10257 C CE1 . PHE F 2 37  ? 117.490 -27.510 17.979  1.000 30.010  ? 37  PHE FFF CE1 1 
ATOM 10258 C CE2 . PHE F 2 37  ? 117.088 -29.206 19.584  1.000 30.570  ? 37  PHE FFF CE2 1 
ATOM 10259 C CZ  . PHE F 2 37  ? 117.968 -28.442 18.861  1.000 31.690  ? 37  PHE FFF CZ  1 
ATOM 10260 N N   . GLN F 2 38  ? 111.189 -25.821 18.087  1.000 28.040  ? 38  GLN FFF N   1 
ATOM 10261 C CA  . GLN F 2 38  ? 109.756 -25.602 17.774  1.000 29.110  ? 38  GLN FFF CA  1 
ATOM 10262 C C   . GLN F 2 38  ? 109.475 -26.326 16.466  1.000 29.960  ? 38  GLN FFF C   1 
ATOM 10263 O O   . GLN F 2 38  ? 110.340 -26.262 15.596  1.000 28.610  ? 38  GLN FFF O   1 
ATOM 10264 C CB  . GLN F 2 38  ? 109.458 -24.112 17.690  1.000 28.980  ? 38  GLN FFF CB  1 
ATOM 10265 C CG  . GLN F 2 38  ? 108.000 -23.793 17.454  1.000 30.080  ? 38  GLN FFF CG  1 
ATOM 10266 C CD  . GLN F 2 38  ? 107.819 -22.318 17.203  1.000 30.640  ? 38  GLN FFF CD  1 
ATOM 10267 O OE1 . GLN F 2 38  ? 108.308 -21.760 16.214  1.000 32.730  ? 38  GLN FFF OE1 1 
ATOM 10268 N NE2 . GLN F 2 38  ? 107.075 -21.683 18.091  1.000 31.150  ? 38  GLN FFF NE2 1 
ATOM 10269 N N   . GLN F 2 39  ? 108.362 -27.061 16.393  1.000 33.980  ? 39  GLN FFF N   1 
ATOM 10270 C CA  . GLN F 2 39  ? 107.988 -27.905 15.227  1.000 39.170  ? 39  GLN FFF CA  1 
ATOM 10271 C C   . GLN F 2 39  ? 106.489 -27.740 14.942  1.000 47.400  ? 39  GLN FFF C   1 
ATOM 10272 O O   . GLN F 2 39  ? 105.642 -28.172 15.762  1.000 53.210  ? 39  GLN FFF O   1 
ATOM 10273 C CB  . GLN F 2 39  ? 108.327 -29.383 15.443  1.000 40.490  ? 39  GLN FFF CB  1 
ATOM 10274 C CG  . GLN F 2 39  ? 108.278 -30.201 14.156  1.000 41.500  ? 39  GLN FFF CG  1 
ATOM 10275 C CD  . GLN F 2 39  ? 108.680 -31.647 14.321  1.000 40.400  ? 39  GLN FFF CD  1 
ATOM 10276 O OE1 . GLN F 2 39  ? 108.513 -32.230 15.385  1.000 39.250  ? 39  GLN FFF OE1 1 
ATOM 10277 N NE2 . GLN F 2 39  ? 109.200 -32.238 13.257  1.000 36.670  ? 39  GLN FFF NE2 1 
ATOM 10278 N N   . PHE F 2 40  ? 106.188 -27.142 13.791  1.000 51.470  ? 40  PHE FFF N   1 
ATOM 10279 C CA  . PHE F 2 40  ? 104.838 -27.016 13.220  1.000 50.930  ? 40  PHE FFF CA  1 
ATOM 10280 C C   . PHE F 2 40  ? 104.539 -28.270 12.424  1.000 57.370  ? 40  PHE FFF C   1 
ATOM 10281 O O   . PHE F 2 40  ? 105.448 -28.844 11.827  1.000 72.590  ? 40  PHE FFF O   1 
ATOM 10282 C CB  . PHE F 2 40  ? 104.801 -25.762 12.351  1.000 46.830  ? 40  PHE FFF CB  1 
ATOM 10283 C CG  . PHE F 2 40  ? 105.020 -24.511 13.152  1.000 42.140  ? 40  PHE FFF CG  1 
ATOM 10284 C CD1 . PHE F 2 40  ? 104.274 -24.256 14.286  1.000 39.440  ? 40  PHE FFF CD1 1 
ATOM 10285 C CD2 . PHE F 2 40  ? 106.010 -23.621 12.786  1.000 41.760  ? 40  PHE FFF CD2 1 
ATOM 10286 C CE1 . PHE F 2 40  ? 104.491 -23.097 15.015  1.000 42.310  ? 40  PHE FFF CE1 1 
ATOM 10287 C CE2 . PHE F 2 40  ? 106.217 -22.463 13.511  1.000 42.050  ? 40  PHE FFF CE2 1 
ATOM 10288 C CZ  . PHE F 2 40  ? 105.459 -22.204 14.627  1.000 41.680  ? 40  PHE FFF CZ  1 
ATOM 10289 N N   . PRO F 2 41  ? 103.254 -28.688 12.341  1.000 58.450  ? 41  PRO FFF N   1 
ATOM 10290 C CA  . PRO F 2 41  ? 102.803 -29.715 11.402  1.000 53.560  ? 41  PRO FFF CA  1 
ATOM 10291 C C   . PRO F 2 41  ? 103.505 -29.657 10.041  1.000 50.980  ? 41  PRO FFF C   1 
ATOM 10292 O O   . PRO F 2 41  ? 103.642 -28.563 9.497   1.000 47.150  ? 41  PRO FFF O   1 
ATOM 10293 C CB  . PRO F 2 41  ? 101.317 -29.368 11.212  1.000 56.380  ? 41  PRO FFF CB  1 
ATOM 10294 C CG  . PRO F 2 41  ? 100.886 -28.747 12.532  1.000 61.240  ? 41  PRO FFF CG  1 
ATOM 10295 C CD  . PRO F 2 41  ? 102.140 -28.165 13.148  1.000 62.160  ? 41  PRO FFF CD  1 
ATOM 10296 N N   . GLY F 2 42  ? 103.987 -30.812 9.573   1.000 48.090  ? 42  GLY FFF N   1 
ATOM 10297 C CA  . GLY F 2 42  ? 104.550 -31.000 8.224   1.000 48.540  ? 42  GLY FFF CA  1 
ATOM 10298 C C   . GLY F 2 42  ? 105.878 -30.292 8.005   1.000 47.350  ? 42  GLY FFF C   1 
ATOM 10299 O O   . GLY F 2 42  ? 106.307 -30.244 6.842   1.000 50.500  ? 42  GLY FFF O   1 
ATOM 10300 N N   . THR F 2 43  ? 106.484 -29.713 9.036   1.000 45.950  ? 43  THR FFF N   1 
ATOM 10301 C CA  . THR F 2 43  ? 107.740 -28.927 8.932   1.000 46.440  ? 43  THR FFF CA  1 
ATOM 10302 C C   . THR F 2 43  ? 108.810 -29.592 9.799   1.000 49.450  ? 43  THR FFF C   1 
ATOM 10303 O O   . THR F 2 43  ? 108.488 -30.462 10.627  1.000 52.250  ? 43  THR FFF O   1 
ATOM 10304 C CB  . THR F 2 43  ? 107.551 -27.463 9.349   1.000 41.270  ? 43  THR FFF CB  1 
ATOM 10305 O OG1 . THR F 2 43  ? 106.654 -26.931 8.394   1.000 42.250  ? 43  THR FFF OG1 1 
ATOM 10306 N N   . ALA F 2 44  ? 110.058 -29.210 9.561   1.000 51.500  ? 44  ALA FFF N   1 
ATOM 10307 C CA  . ALA F 2 44  ? 111.231 -29.656 10.334  1.000 48.510  ? 44  ALA FFF CA  1 
ATOM 10308 C C   . ALA F 2 44  ? 111.161 -29.008 11.708  1.000 43.140  ? 44  ALA FFF C   1 
ATOM 10309 O O   . ALA F 2 44  ? 110.476 -28.007 11.869  1.000 36.010  ? 44  ALA FFF O   1 
ATOM 10310 C CB  . ALA F 2 44  ? 112.491 -29.247 9.612   1.000 55.160  ? 44  ALA FFF CB  1 
ATOM 10311 N N   . PRO F 2 45  ? 111.887 -29.543 12.722  1.000 39.320  ? 45  PRO FFF N   1 
ATOM 10312 C CA  . PRO F 2 45  ? 112.183 -28.798 13.937  1.000 36.220  ? 45  PRO FFF CA  1 
ATOM 10313 C C   . PRO F 2 45  ? 113.029 -27.575 13.576  1.000 36.590  ? 45  PRO FFF C   1 
ATOM 10314 O O   . PRO F 2 45  ? 113.719 -27.618 12.577  1.000 38.510  ? 45  PRO FFF O   1 
ATOM 10315 C CB  . PRO F 2 45  ? 113.036 -29.760 14.776  1.000 36.010  ? 45  PRO FFF CB  1 
ATOM 10316 C CG  . PRO F 2 45  ? 112.737 -31.124 14.217  1.000 35.580  ? 45  PRO FFF CG  1 
ATOM 10317 C CD  . PRO F 2 45  ? 112.496 -30.882 12.747  1.000 38.480  ? 45  PRO FFF CD  1 
ATOM 10318 N N   . LYS F 2 46  ? 112.945 -26.517 14.383  1.000 38.180  ? 46  LYS FFF N   1 
ATOM 10319 C CA  . LYS F 2 46  ? 113.754 -25.281 14.222  1.000 38.080  ? 46  LYS FFF CA  1 
ATOM 10320 C C   . LYS F 2 46  ? 114.198 -24.852 15.610  1.000 32.820  ? 46  LYS FFF C   1 
ATOM 10321 O O   . LYS F 2 46  ? 113.453 -25.126 16.578  1.000 31.210  ? 46  LYS FFF O   1 
ATOM 10322 C CB  . LYS F 2 46  ? 112.966 -24.182 13.490  1.000 41.550  ? 46  LYS FFF CB  1 
ATOM 10323 C CG  . LYS F 2 46  ? 113.696 -22.863 13.266  1.000 42.110  ? 46  LYS FFF CG  1 
ATOM 10324 C CD  . LYS F 2 46  ? 113.159 -22.039 12.104  1.000 42.400  ? 46  LYS FFF CD  1 
ATOM 10325 C CE  . LYS F 2 46  ? 114.081 -20.888 11.765  1.000 41.820  ? 46  LYS FFF CE  1 
ATOM 10326 N NZ  . LYS F 2 46  ? 113.355 -19.780 11.119  1.000 41.310  ? 46  LYS FFF NZ  1 
ATOM 10327 N N   . LEU F 2 47  ? 115.383 -24.255 15.706  1.000 30.090  ? 47  LEU FFF N   1 
ATOM 10328 C CA  . LEU F 2 47  ? 115.947 -23.797 17.006  1.000 28.750  ? 47  LEU FFF CA  1 
ATOM 10329 C C   . LEU F 2 47  ? 115.075 -22.655 17.540  1.000 27.640  ? 47  LEU FFF C   1 
ATOM 10330 O O   . LEU F 2 47  ? 114.863 -21.690 16.780  1.000 30.390  ? 47  LEU FFF O   1 
ATOM 10331 C CB  . LEU F 2 47  ? 117.382 -23.319 16.785  1.000 26.570  ? 47  LEU FFF CB  1 
ATOM 10332 C CG  . LEU F 2 47  ? 118.102 -22.891 18.040  1.000 24.010  ? 47  LEU FFF CG  1 
ATOM 10333 C CD1 . LEU F 2 47  ? 118.230 -24.071 18.995  1.000 26.310  ? 47  LEU FFF CD1 1 
ATOM 10334 C CD2 . LEU F 2 47  ? 119.442 -22.293 17.693  1.000 21.370  ? 47  LEU FFF CD2 1 
ATOM 10335 N N   . LEU F 2 48  ? 114.596 -22.782 18.778  1.000 26.750  ? 48  LEU FFF N   1 
ATOM 10336 C CA  . LEU F 2 48  ? 113.777 -21.754 19.476  1.000 29.430  ? 48  LEU FFF CA  1 
ATOM 10337 C C   . LEU F 2 48  ? 114.577 -21.161 20.641  1.000 29.140  ? 48  LEU FFF C   1 
ATOM 10338 O O   . LEU F 2 48  ? 114.693 -19.938 20.711  1.000 27.460  ? 48  LEU FFF O   1 
ATOM 10339 C CB  . LEU F 2 48  ? 112.505 -22.434 19.984  1.000 32.100  ? 48  LEU FFF CB  1 
ATOM 10340 C CG  . LEU F 2 48  ? 111.513 -21.618 20.810  1.000 35.360  ? 48  LEU FFF CG  1 
ATOM 10341 C CD1 . LEU F 2 48  ? 110.923 -20.467 20.013  1.000 37.940  ? 48  LEU FFF CD1 1 
ATOM 10342 C CD2 . LEU F 2 48  ? 110.412 -22.444 21.454  1.000 34.860  ? 48  LEU FFF CD2 1 
ATOM 10343 N N   . ILE F 2 49  ? 115.110 -22.014 21.516  1.000 28.480  ? 49  ILE FFF N   1 
ATOM 10344 C CA  . ILE F 2 49  ? 116.042 -21.645 22.617  1.000 29.760  ? 49  ILE FFF CA  1 
ATOM 10345 C C   . ILE F 2 49  ? 117.297 -22.503 22.494  1.000 29.300  ? 49  ILE FFF C   1 
ATOM 10346 O O   . ILE F 2 49  ? 117.131 -23.695 22.215  1.000 33.900  ? 49  ILE FFF O   1 
ATOM 10347 C CB  . ILE F 2 49  ? 115.376 -21.835 23.996  1.000 31.800  ? 49  ILE FFF CB  1 
ATOM 10348 C CG1 . ILE F 2 49  ? 114.143 -20.940 24.159  1.000 34.960  ? 49  ILE FFF CG1 1 
ATOM 10349 C CG2 . ILE F 2 49  ? 116.377 -21.627 25.131  1.000 31.040  ? 49  ILE FFF CG2 1 
ATOM 10350 C CD1 . ILE F 2 49  ? 114.467 -19.450 24.188  1.000 36.980  ? 49  ILE FFF CD1 1 
ATOM 10351 N N   . TYR F 2 50  ? 118.486 -21.947 22.745  1.000 28.770  ? 50  TYR FFF N   1 
ATOM 10352 C CA  . TYR F 2 50  ? 119.758 -22.701 22.931  1.000 28.750  ? 50  TYR FFF CA  1 
ATOM 10353 C C   . TYR F 2 50  ? 120.417 -22.336 24.268  1.000 27.950  ? 50  TYR FFF C   1 
ATOM 10354 O O   . TYR F 2 50  ? 120.114 -21.311 24.859  1.000 26.960  ? 50  TYR FFF O   1 
ATOM 10355 C CB  . TYR F 2 50  ? 120.698 -22.439 21.756  1.000 29.630  ? 50  TYR FFF CB  1 
ATOM 10356 C CG  . TYR F 2 50  ? 121.357 -21.084 21.726  1.000 28.280  ? 50  TYR FFF CG  1 
ATOM 10357 C CD1 . TYR F 2 50  ? 120.700 -19.978 21.224  1.000 28.590  ? 50  TYR FFF CD1 1 
ATOM 10358 C CD2 . TYR F 2 50  ? 122.656 -20.924 22.154  1.000 27.520  ? 50  TYR FFF CD2 1 
ATOM 10359 C CE1 . TYR F 2 50  ? 121.309 -18.740 21.161  1.000 29.150  ? 50  TYR FFF CE1 1 
ATOM 10360 C CE2 . TYR F 2 50  ? 123.284 -19.692 22.097  1.000 29.460  ? 50  TYR FFF CE2 1 
ATOM 10361 C CZ  . TYR F 2 50  ? 122.611 -18.590 21.598  1.000 30.570  ? 50  TYR FFF CZ  1 
ATOM 10362 O OH  . TYR F 2 50  ? 123.224 -17.363 21.553  1.000 31.760  ? 50  TYR FFF OH  1 
ATOM 10363 N N   . ALA F 2 51  ? 121.330 -23.179 24.734  1.000 29.210  ? 51  ALA FFF N   1 
ATOM 10364 C CA  . ALA F 2 51  ? 122.123 -22.965 25.972  1.000 27.290  ? 51  ALA FFF CA  1 
ATOM 10365 C C   . ALA F 2 51  ? 121.185 -22.598 27.128  1.000 25.900  ? 51  ALA FFF C   1 
ATOM 10366 O O   . ALA F 2 51  ? 121.479 -21.651 27.855  1.000 25.740  ? 51  ALA FFF O   1 
ATOM 10367 C CB  . ALA F 2 51  ? 123.178 -21.912 25.731  1.000 26.260  ? 51  ALA FFF CB  1 
ATOM 10368 N N   . ASN F 2 52  ? 120.072 -23.321 27.250  1.000 25.940  ? 52  ASN FFF N   1 
ATOM 10369 C CA  . ASN F 2 52  ? 119.130 -23.275 28.404  1.000 24.540  ? 52  ASN FFF CA  1 
ATOM 10370 C C   . ASN F 2 52  ? 118.186 -22.069 28.303  1.000 22.750  ? 52  ASN FFF C   1 
ATOM 10371 O O   . ASN F 2 52  ? 116.976 -22.273 28.598  1.000 20.630  ? 52  ASN FFF O   1 
ATOM 10372 C CB  . ASN F 2 52  ? 119.860 -23.273 29.743  1.000 24.080  ? 52  ASN FFF CB  1 
ATOM 10373 C CG  . ASN F 2 52  ? 120.817 -24.439 29.883  1.000 24.490  ? 52  ASN FFF CG  1 
ATOM 10374 O OD1 . ASN F 2 52  ? 120.424 -25.608 29.903  1.000 23.430  ? 52  ASN FFF OD1 1 
ATOM 10375 N ND2 . ASN F 2 52  ? 122.085 -24.128 30.033  1.000 25.860  ? 52  ASN FFF ND2 1 
ATOM 10376 N N   . THR F 2 53  ? 118.706 -20.896 27.916  1.000 23.340  ? 53  THR FFF N   1 
ATOM 10377 C CA  . THR F 2 53  ? 118.101 -19.566 28.204  1.000 26.690  ? 53  THR FFF CA  1 
ATOM 10378 C C   . THR F 2 53  ? 118.314 -18.525 27.092  1.000 29.380  ? 53  THR FFF C   1 
ATOM 10379 O O   . THR F 2 53  ? 117.953 -17.387 27.323  1.000 36.440  ? 53  THR FFF O   1 
ATOM 10380 C CB  . THR F 2 53  ? 118.658 -18.958 29.499  1.000 27.850  ? 53  THR FFF CB  1 
ATOM 10381 O OG1 . THR F 2 53  ? 120.093 -18.880 29.497  1.000 27.980  ? 53  THR FFF OG1 1 
ATOM 10382 C CG2 . THR F 2 53  ? 118.272 -19.743 30.723  1.000 29.240  ? 53  THR FFF CG2 1 
ATOM 10383 N N   . GLN F 2 54  ? 118.839 -18.864 25.924  1.000 30.350  ? 54  GLN FFF N   1 
ATOM 10384 C CA  . GLN F 2 54  ? 119.268 -17.863 24.908  1.000 30.710  ? 54  GLN FFF CA  1 
ATOM 10385 C C   . GLN F 2 54  ? 118.427 -17.993 23.648  1.000 31.570  ? 54  GLN FFF C   1 
ATOM 10386 O O   . GLN F 2 54  ? 118.107 -19.118 23.274  1.000 27.010  ? 54  GLN FFF O   1 
ATOM 10387 C CB  . GLN F 2 54  ? 120.743 -18.068 24.565  1.000 31.120  ? 54  GLN FFF CB  1 
ATOM 10388 C CG  . GLN F 2 54  ? 121.613 -18.090 25.808  1.000 30.970  ? 54  GLN FFF CG  1 
ATOM 10389 C CD  . GLN F 2 54  ? 121.637 -16.718 26.427  1.000 29.110  ? 54  GLN FFF CD  1 
ATOM 10390 O OE1 . GLN F 2 54  ? 122.022 -15.765 25.770  1.000 29.380  ? 54  GLN FFF OE1 1 
ATOM 10391 N NE2 . GLN F 2 54  ? 121.204 -16.613 27.678  1.000 27.340  ? 54  GLN FFF NE2 1 
ATOM 10392 N N   . ARG F 2 55  ? 118.111 -16.859 23.019  1.000 36.860  ? 55  ARG FFF N   1 
ATOM 10393 C CA  . ARG F 2 55  ? 117.282 -16.791 21.792  1.000 36.790  ? 55  ARG FFF CA  1 
ATOM 10394 C C   . ARG F 2 55  ? 118.183 -16.562 20.593  1.000 36.630  ? 55  ARG FFF C   1 
ATOM 10395 O O   . ARG F 2 55  ? 119.048 -15.703 20.610  1.000 33.560  ? 55  ARG FFF O   1 
ATOM 10396 C CB  . ARG F 2 55  ? 116.241 -15.679 21.914  1.000 38.910  ? 55  ARG FFF CB  1 
ATOM 10397 C CG  . ARG F 2 55  ? 115.095 -16.060 22.841  1.000 42.700  ? 55  ARG FFF CG  1 
ATOM 10398 C CD  . ARG F 2 55  ? 113.989 -15.040 22.850  1.000 48.860  ? 55  ARG FFF CD  1 
ATOM 10399 N NE  . ARG F 2 55  ? 114.482 -13.682 23.044  1.000 54.580  ? 55  ARG FFF NE  1 
ATOM 10400 C CZ  . ARG F 2 55  ? 114.746 -13.109 24.211  1.000 56.030  ? 55  ARG FFF CZ  1 
ATOM 10401 N NH1 . ARG F 2 55  ? 114.588 -13.764 25.350  1.000 58.410  ? 55  ARG FFF NH1 1 
ATOM 10402 N NH2 . ARG F 2 55  ? 115.162 -11.860 24.238  1.000 60.020  ? 55  ARG FFF NH2 1 
ATOM 10403 N N   . PRO F 2 56  ? 118.005 -17.326 19.498  1.000 38.940  ? 56  PRO FFF N   1 
ATOM 10404 C CA  . PRO F 2 56  ? 118.683 -16.992 18.251  1.000 40.680  ? 56  PRO FFF CA  1 
ATOM 10405 C C   . PRO F 2 56  ? 117.964 -15.763 17.681  1.000 43.990  ? 56  PRO FFF C   1 
ATOM 10406 O O   . PRO F 2 56  ? 116.843 -15.498 18.126  1.000 48.210  ? 56  PRO FFF O   1 
ATOM 10407 C CB  . PRO F 2 56  ? 118.505 -18.270 17.426  1.000 40.430  ? 56  PRO FFF CB  1 
ATOM 10408 C CG  . PRO F 2 56  ? 117.232 -18.902 17.947  1.000 36.980  ? 56  PRO FFF CG  1 
ATOM 10409 C CD  . PRO F 2 56  ? 117.138 -18.511 19.398  1.000 37.080  ? 56  PRO FFF CD  1 
ATOM 10410 N N   . SER F 2 57  ? 118.585 -15.059 16.729  1.000 43.920  ? 57  SER FFF N   1 
ATOM 10411 C CA  . SER F 2 57  ? 117.908 -13.954 16.004  1.000 49.220  ? 57  SER FFF CA  1 
ATOM 10412 C C   . SER F 2 57  ? 116.627 -14.491 15.353  1.000 47.480  ? 57  SER FFF C   1 
ATOM 10413 O O   . SER F 2 57  ? 116.691 -15.582 14.742  1.000 43.870  ? 57  SER FFF O   1 
ATOM 10414 C CB  . SER F 2 57  ? 118.830 -13.306 14.996  1.000 57.140  ? 57  SER FFF CB  1 
ATOM 10415 O OG  . SER F 2 57  ? 118.114 -12.475 14.079  1.000 65.650  ? 57  SER FFF OG  1 
ATOM 10416 N N   . GLY F 2 58  ? 115.504 -13.781 15.535  1.000 51.580  ? 58  GLY FFF N   1 
ATOM 10417 C CA  . GLY F 2 58  ? 114.207 -14.106 14.914  1.000 53.960  ? 58  GLY FFF CA  1 
ATOM 10418 C C   . GLY F 2 58  ? 113.181 -14.582 15.931  1.000 57.990  ? 58  GLY FFF C   1 
ATOM 10419 O O   . GLY F 2 58  ? 111.994 -14.663 15.570  1.000 61.570  ? 58  GLY FFF O   1 
ATOM 10420 N N   . VAL F 2 59  ? 113.614 -14.933 17.144  1.000 58.570  ? 59  VAL FFF N   1 
ATOM 10421 C CA  . VAL F 2 59  ? 112.716 -15.443 18.219  1.000 52.700  ? 59  VAL FFF CA  1 
ATOM 10422 C C   . VAL F 2 59  ? 112.346 -14.269 19.118  1.000 54.070  ? 59  VAL FFF C   1 
ATOM 10423 O O   . VAL F 2 59  ? 113.205 -13.646 19.735  1.000 54.820  ? 59  VAL FFF O   1 
ATOM 10424 C CB  . VAL F 2 59  ? 113.352 -16.600 19.008  1.000 53.740  ? 59  VAL FFF CB  1 
ATOM 10425 C CG1 . VAL F 2 59  ? 112.426 -17.112 20.097  1.000 53.540  ? 59  VAL FFF CG1 1 
ATOM 10426 C CG2 . VAL F 2 59  ? 113.715 -17.744 18.087  1.000 55.500  ? 59  VAL FFF CG2 1 
ATOM 10427 N N   . PRO F 2 60  ? 111.041 -13.938 19.201  1.000 52.630  ? 60  PRO FFF N   1 
ATOM 10428 C CA  . PRO F 2 60  ? 110.559 -12.901 20.108  1.000 49.470  ? 60  PRO FFF CA  1 
ATOM 10429 C C   . PRO F 2 60  ? 111.006 -12.996 21.575  1.000 45.020  ? 60  PRO FFF C   1 
ATOM 10430 O O   . PRO F 2 60  ? 111.167 -14.073 22.085  1.000 44.180  ? 60  PRO FFF O   1 
ATOM 10431 C CB  . PRO F 2 60  ? 109.034 -13.124 20.059  1.000 57.250  ? 60  PRO FFF CB  1 
ATOM 10432 C CG  . PRO F 2 60  ? 108.765 -13.688 18.678  1.000 59.720  ? 60  PRO FFF CG  1 
ATOM 10433 C CD  . PRO F 2 60  ? 109.963 -14.557 18.402  1.000 57.700  ? 60  PRO FFF CD  1 
ATOM 10434 N N   . ASP F 2 61  ? 111.138 -11.836 22.221  1.000 49.400  ? 61  ASP FFF N   1 
ATOM 10435 C CA  . ASP F 2 61  ? 111.263 -11.612 23.691  1.000 48.370  ? 61  ASP FFF CA  1 
ATOM 10436 C C   . ASP F 2 61  ? 110.397 -12.554 24.531  1.000 42.930  ? 61  ASP FFF C   1 
ATOM 10437 O O   . ASP F 2 61  ? 110.800 -12.912 25.641  1.000 37.610  ? 61  ASP FFF O   1 
ATOM 10438 C CB  . ASP F 2 61  ? 110.678 -10.234 24.043  1.000 51.180  ? 61  ASP FFF CB  1 
ATOM 10439 C CG  . ASP F 2 61  ? 111.730 -9.195  24.285  1.000 57.670  ? 61  ASP FFF CG  1 
ATOM 10440 O OD1 . ASP F 2 61  ? 112.747 -9.551  24.909  1.000 56.700  ? 61  ASP FFF OD1 1 
ATOM 10441 O OD2 . ASP F 2 61  ? 111.514 -8.024  23.848  1.000 77.340  ? 61  ASP FFF OD2 1 
ATOM 10442 N N   . ARG F 2 62  ? 109.198 -12.858 24.038  1.000 44.150  ? 62  ARG FFF N   1 
ATOM 10443 C CA  . ARG F 2 62  ? 108.138 -13.626 24.738  1.000 47.610  ? 62  ARG FFF CA  1 
ATOM 10444 C C   . ARG F 2 62  ? 108.697 -14.974 25.202  1.000 49.570  ? 62  ARG FFF C   1 
ATOM 10445 O O   . ARG F 2 62  ? 108.470 -15.356 26.384  1.000 53.740  ? 62  ARG FFF O   1 
ATOM 10446 C CB  . ARG F 2 62  ? 106.955 -13.863 23.800  1.000 50.030  ? 62  ARG FFF CB  1 
ATOM 10447 C CG  . ARG F 2 62  ? 106.534 -12.651 22.975  1.000 54.070  ? 62  ARG FFF CG  1 
ATOM 10448 C CD  . ARG F 2 62  ? 105.243 -12.859 22.198  1.000 53.300  ? 62  ARG FFF CD  1 
ATOM 10449 N NE  . ARG F 2 62  ? 104.955 -14.252 21.875  1.000 48.120  ? 62  ARG FFF NE  1 
ATOM 10450 C CZ  . ARG F 2 62  ? 104.805 -14.745 20.648  1.000 49.810  ? 62  ARG FFF CZ  1 
ATOM 10451 N NH1 . ARG F 2 62  ? 104.953 -13.980 19.572  1.000 48.780  ? 62  ARG FFF NH1 1 
ATOM 10452 N NH2 . ARG F 2 62  ? 104.512 -16.027 20.510  1.000 50.080  ? 62  ARG FFF NH2 1 
ATOM 10453 N N   . PHE F 2 63  ? 109.413 -15.655 24.308  1.000 45.080  ? 63  PHE FFF N   1 
ATOM 10454 C CA  . PHE F 2 63  ? 110.087 -16.955 24.556  1.000 40.550  ? 63  PHE FFF CA  1 
ATOM 10455 C C   . PHE F 2 63  ? 111.296 -16.766 25.478  1.000 37.930  ? 63  PHE FFF C   1 
ATOM 10456 O O   . PHE F 2 63  ? 112.175 -15.942 25.207  1.000 33.680  ? 63  PHE FFF O   1 
ATOM 10457 C CB  . PHE F 2 63  ? 110.511 -17.588 23.234  1.000 39.290  ? 63  PHE FFF CB  1 
ATOM 10458 C CG  . PHE F 2 63  ? 109.358 -17.976 22.350  1.000 34.990  ? 63  PHE FFF CG  1 
ATOM 10459 C CD1 . PHE F 2 63  ? 108.676 -19.168 22.555  1.000 32.220  ? 63  PHE FFF CD1 1 
ATOM 10460 C CD2 . PHE F 2 63  ? 108.958 -17.133 21.323  1.000 32.650  ? 63  PHE FFF CD2 1 
ATOM 10461 C CE1 . PHE F 2 63  ? 107.622 -19.520 21.735  1.000 32.090  ? 63  PHE FFF CE1 1 
ATOM 10462 C CE2 . PHE F 2 63  ? 107.896 -17.484 20.514  1.000 32.740  ? 63  PHE FFF CE2 1 
ATOM 10463 C CZ  . PHE F 2 63  ? 107.219 -18.660 20.735  1.000 32.070  ? 63  PHE FFF CZ  1 
ATOM 10464 N N   . SER F 2 64  ? 111.327 -17.538 26.554  1.000 36.960  ? 64  SER FFF N   1 
ATOM 10465 C CA  . SER F 2 64  ? 112.357 -17.440 27.607  1.000 38.010  ? 64  SER FFF CA  1 
ATOM 10466 C C   . SER F 2 64  ? 112.563 -18.817 28.243  1.000 39.880  ? 64  SER FFF C   1 
ATOM 10467 O O   . SER F 2 64  ? 111.683 -19.695 28.093  1.000 41.030  ? 64  SER FFF O   1 
ATOM 10468 C CB  . SER F 2 64  ? 111.934 -16.438 28.622  1.000 36.730  ? 64  SER FFF CB  1 
ATOM 10469 O OG  . SER F 2 64  ? 111.056 -17.033 29.556  1.000 32.550  ? 64  SER FFF OG  1 
ATOM 10470 N N   . GLY F 2 65  ? 113.667 -18.982 28.952  1.000 36.350  ? 65  GLY FFF N   1 
ATOM 10471 C CA  . GLY F 2 65  ? 113.975 -20.227 29.666  1.000 36.690  ? 65  GLY FFF CA  1 
ATOM 10472 C C   . GLY F 2 65  ? 114.476 -19.953 31.058  1.000 36.280  ? 65  GLY FFF C   1 
ATOM 10473 O O   . GLY F 2 65  ? 114.916 -18.843 31.297  1.000 37.830  ? 65  GLY FFF O   1 
ATOM 10474 N N   . SER F 2 66  ? 114.380 -20.944 31.941  1.000 38.270  ? 66  SER FFF N   1 
ATOM 10475 C CA  . SER F 2 66  ? 115.033 -20.964 33.266  1.000 42.350  ? 66  SER FFF CA  1 
ATOM 10476 C C   . SER F 2 66  ? 115.680 -22.335 33.477  1.000 44.540  ? 66  SER FFF C   1 
ATOM 10477 O O   . SER F 2 66  ? 115.086 -23.341 33.012  1.000 47.690  ? 66  SER FFF O   1 
ATOM 10478 C CB  . SER F 2 66  ? 114.035 -20.638 34.335  1.000 46.190  ? 66  SER FFF CB  1 
ATOM 10479 O OG  . SER F 2 66  ? 113.351 -21.806 34.783  1.000 51.120  ? 66  SER FFF OG  1 
ATOM 10480 N N   . LYS F 2 67  ? 116.855 -22.366 34.114  1.000 43.820  ? 67  LYS FFF N   1 
ATOM 10481 C CA  . LYS F 2 67  ? 117.564 -23.605 34.532  1.000 44.820  ? 67  LYS FFF CA  1 
ATOM 10482 C C   . LYS F 2 67  ? 117.623 -23.620 36.060  1.000 46.190  ? 67  LYS FFF C   1 
ATOM 10483 O O   . LYS F 2 67  ? 118.008 -22.605 36.640  1.000 45.820  ? 67  LYS FFF O   1 
ATOM 10484 C CB  . LYS F 2 67  ? 118.977 -23.651 33.931  1.000 46.350  ? 67  LYS FFF CB  1 
ATOM 10485 C CG  . LYS F 2 67  ? 119.780 -24.912 34.227  1.000 47.700  ? 67  LYS FFF CG  1 
ATOM 10486 C CD  . LYS F 2 67  ? 121.243 -24.836 33.815  1.000 48.930  ? 67  LYS FFF CD  1 
ATOM 10487 C CE  . LYS F 2 67  ? 121.818 -26.188 33.410  1.000 57.400  ? 67  LYS FFF CE  1 
ATOM 10488 N NZ  . LYS F 2 67  ? 121.868 -27.168 34.526  1.000 55.210  ? 67  LYS FFF NZ  1 
ATOM 10489 N N   . SER F 2 68  ? 117.259 -24.731 36.685  1.000 53.390  ? 68  SER FFF N   1 
ATOM 10490 C CA  . SER F 2 68  ? 117.590 -25.032 38.102  1.000 53.090  ? 68  SER FFF CA  1 
ATOM 10491 C C   . SER F 2 68  ? 118.164 -26.453 38.180  1.000 47.670  ? 68  SER FFF C   1 
ATOM 10492 O O   . SER F 2 68  ? 117.369 -27.401 38.070  1.000 39.160  ? 68  SER FFF O   1 
ATOM 10493 C CB  . SER F 2 68  ? 116.381 -24.845 38.978  1.000 56.010  ? 68  SER FFF CB  1 
ATOM 10494 O OG  . SER F 2 68  ? 116.738 -24.882 40.347  1.000 57.690  ? 68  SER FFF OG  1 
ATOM 10495 N N   . GLY F 2 69  ? 119.492 -26.576 38.296  1.000 46.490  ? 69  GLY FFF N   1 
ATOM 10496 C CA  . GLY F 2 69  ? 120.211 -27.868 38.306  1.000 49.600  ? 69  GLY FFF CA  1 
ATOM 10497 C C   . GLY F 2 69  ? 119.757 -28.774 37.168  1.000 51.120  ? 69  GLY FFF C   1 
ATOM 10498 O O   . GLY F 2 69  ? 119.816 -28.320 35.993  1.000 48.260  ? 69  GLY FFF O   1 
ATOM 10499 N N   . THR F 2 70  ? 119.253 -29.972 37.490  1.000 50.720  ? 70  THR FFF N   1 
ATOM 10500 C CA  . THR F 2 70  ? 118.970 -31.057 36.502  1.000 51.000  ? 70  THR FFF CA  1 
ATOM 10501 C C   . THR F 2 70  ? 117.638 -30.819 35.761  1.000 47.840  ? 70  THR FFF C   1 
ATOM 10502 O O   . THR F 2 70  ? 117.276 -31.648 34.908  1.000 47.950  ? 70  THR FFF O   1 
ATOM 10503 C CB  . THR F 2 70  ? 119.026 -32.443 37.162  1.000 48.340  ? 70  THR FFF CB  1 
ATOM 10504 O OG1 . THR F 2 70  ? 117.863 -32.599 37.967  1.000 54.550  ? 70  THR FFF OG1 1 
ATOM 10505 C CG2 . THR F 2 70  ? 120.255 -32.640 38.016  1.000 48.190  ? 70  THR FFF CG2 1 
ATOM 10506 N N   . SER F 2 71  ? 116.925 -29.732 36.031  1.000 43.190  ? 71  SER FFF N   1 
ATOM 10507 C CA  . SER F 2 71  ? 115.651 -29.407 35.344  1.000 43.680  ? 71  SER FFF CA  1 
ATOM 10508 C C   . SER F 2 71  ? 115.754 -28.026 34.718  1.000 44.340  ? 71  SER FFF C   1 
ATOM 10509 O O   . SER F 2 71  ? 116.416 -27.148 35.300  1.000 46.140  ? 71  SER FFF O   1 
ATOM 10510 C CB  . SER F 2 71  ? 114.457 -29.466 36.271  1.000 51.360  ? 71  SER FFF CB  1 
ATOM 10511 O OG  . SER F 2 71  ? 114.404 -30.691 36.988  1.000 58.740  ? 71  SER FFF OG  1 
ATOM 10512 N N   . VAL F 2 72  ? 115.095 -27.868 33.574  1.000 43.750  ? 72  VAL FFF N   1 
ATOM 10513 C CA  . VAL F 2 72  ? 114.986 -26.612 32.783  1.000 40.160  ? 72  VAL FFF CA  1 
ATOM 10514 C C   . VAL F 2 72  ? 113.509 -26.428 32.467  1.000 39.950  ? 72  VAL FFF C   1 
ATOM 10515 O O   . VAL F 2 72  ? 112.803 -27.443 32.404  1.000 40.900  ? 72  VAL FFF O   1 
ATOM 10516 C CB  . VAL F 2 72  ? 115.833 -26.699 31.499  1.000 39.470  ? 72  VAL FFF CB  1 
ATOM 10517 C CG1 . VAL F 2 72  ? 115.414 -25.675 30.449  1.000 45.720  ? 72  VAL FFF CG1 1 
ATOM 10518 C CG2 . VAL F 2 72  ? 117.311 -26.552 31.821  1.000 38.700  ? 72  VAL FFF CG2 1 
ATOM 10519 N N   . SER F 2 73  ? 113.067 -25.192 32.254  1.000 39.290  ? 73  SER FFF N   1 
ATOM 10520 C CA  . SER F 2 73  ? 111.718 -24.891 31.720  1.000 40.290  ? 73  SER FFF CA  1 
ATOM 10521 C C   . SER F 2 73  ? 111.826 -23.921 30.545  1.000 38.570  ? 73  SER FFF C   1 
ATOM 10522 O O   . SER F 2 73  ? 112.832 -23.174 30.463  1.000 38.850  ? 73  SER FFF O   1 
ATOM 10523 C CB  . SER F 2 73  ? 110.799 -24.375 32.797  1.000 43.580  ? 73  SER FFF CB  1 
ATOM 10524 O OG  . SER F 2 73  ? 111.300 -23.173 33.320  1.000 46.720  ? 73  SER FFF OG  1 
ATOM 10525 N N   . LEU F 2 74  ? 110.848 -24.022 29.642  1.000 39.630  ? 74  LEU FFF N   1 
ATOM 10526 C CA  . LEU F 2 74  ? 110.581 -23.058 28.556  1.000 40.130  ? 74  LEU FFF CA  1 
ATOM 10527 C C   . LEU F 2 74  ? 109.335 -22.269 28.966  1.000 39.580  ? 74  LEU FFF C   1 
ATOM 10528 O O   . LEU F 2 74  ? 108.370 -22.894 29.446  1.000 38.880  ? 74  LEU FFF O   1 
ATOM 10529 C CB  . LEU F 2 74  ? 110.338 -23.813 27.247  1.000 42.600  ? 74  LEU FFF CB  1 
ATOM 10530 C CG  . LEU F 2 74  ? 109.761 -22.977 26.104  1.000 44.380  ? 74  LEU FFF CG  1 
ATOM 10531 C CD1 . LEU F 2 74  ? 110.744 -21.896 25.684  1.000 46.770  ? 74  LEU FFF CD1 1 
ATOM 10532 C CD2 . LEU F 2 74  ? 109.386 -23.851 24.924  1.000 43.360  ? 74  LEU FFF CD2 1 
ATOM 10533 N N   . ALA F 2 75  ? 109.368 -20.953 28.785  1.000 37.770  ? 75  ALA FFF N   1 
ATOM 10534 C CA  . ALA F 2 75  ? 108.257 -20.032 29.088  1.000 34.580  ? 75  ALA FFF CA  1 
ATOM 10535 C C   . ALA F 2 75  ? 107.854 -19.305 27.809  1.000 34.570  ? 75  ALA FFF C   1 
ATOM 10536 O O   . ALA F 2 75  ? 108.607 -18.440 27.334  1.000 36.920  ? 75  ALA FFF O   1 
ATOM 10537 C CB  . ALA F 2 75  ? 108.703 -19.073 30.157  1.000 35.260  ? 75  ALA FFF CB  1 
ATOM 10538 N N   . ILE F 2 76  ? 106.678 -19.636 27.295  1.000 37.450  ? 76  ILE FFF N   1 
ATOM 10539 C CA  . ILE F 2 76  ? 106.011 -18.864 26.209  1.000 44.100  ? 76  ILE FFF CA  1 
ATOM 10540 C C   . ILE F 2 76  ? 105.054 -17.874 26.866  1.000 48.640  ? 76  ILE FFF C   1 
ATOM 10541 O O   . ILE F 2 76  ? 104.005 -18.323 27.330  1.000 51.220  ? 76  ILE FFF O   1 
ATOM 10542 C CB  . ILE F 2 76  ? 105.258 -19.795 25.242  1.000 46.370  ? 76  ILE FFF CB  1 
ATOM 10543 C CG1 . ILE F 2 76  ? 106.115 -20.978 24.800  1.000 48.540  ? 76  ILE FFF CG1 1 
ATOM 10544 C CG2 . ILE F 2 76  ? 104.751 -18.996 24.056  1.000 46.540  ? 76  ILE FFF CG2 1 
ATOM 10545 C CD1 . ILE F 2 76  ? 105.343 -22.012 24.034  1.000 47.440  ? 76  ILE FFF CD1 1 
ATOM 10546 N N   . SER F 2 77  ? 105.419 -16.595 26.931  1.000 54.460  ? 77  SER FFF N   1 
ATOM 10547 C CA  . SER F 2 77  ? 104.551 -15.510 27.452  1.000 61.770  ? 77  SER FFF CA  1 
ATOM 10548 C C   . SER F 2 77  ? 103.848 -14.852 26.264  1.000 65.360  ? 77  SER FFF C   1 
ATOM 10549 O O   . SER F 2 77  ? 104.306 -15.060 25.117  1.000 79.340  ? 77  SER FFF O   1 
ATOM 10550 C CB  . SER F 2 77  ? 105.330 -14.524 28.283  1.000 64.070  ? 77  SER FFF CB  1 
ATOM 10551 O OG  . SER F 2 77  ? 106.157 -13.711 27.460  1.000 71.600  ? 77  SER FFF OG  1 
ATOM 10552 N N   . GLY F 2 78  ? 102.767 -14.112 26.519  1.000 61.300  ? 78  GLY FFF N   1 
ATOM 10553 C CA  . GLY F 2 78  ? 101.951 -13.477 25.468  1.000 58.740  ? 78  GLY FFF CA  1 
ATOM 10554 C C   . GLY F 2 78  ? 101.544 -14.491 24.417  1.000 51.840  ? 78  GLY FFF C   1 
ATOM 10555 O O   . GLY F 2 78  ? 101.804 -14.257 23.220  1.000 47.200  ? 78  GLY FFF O   1 
ATOM 10556 N N   . LEU F 2 79  ? 100.942 -15.589 24.866  1.000 52.150  ? 79  LEU FFF N   1 
ATOM 10557 C CA  . LEU F 2 79  ? 100.622 -16.751 24.006  1.000 58.000  ? 79  LEU FFF CA  1 
ATOM 10558 C C   . LEU F 2 79  ? 99.780  -16.297 22.807  1.000 55.470  ? 79  LEU FFF C   1 
ATOM 10559 O O   . LEU F 2 79  ? 98.873  -15.499 23.002  1.000 58.550  ? 79  LEU FFF O   1 
ATOM 10560 C CB  . LEU F 2 79  ? 99.881  -17.800 24.839  1.000 61.590  ? 79  LEU FFF CB  1 
ATOM 10561 C CG  . LEU F 2 79  ? 99.649  -19.120 24.106  1.000 70.900  ? 79  LEU FFF CG  1 
ATOM 10562 C CD1 . LEU F 2 79  ? 100.961 -19.837 23.812  1.000 71.240  ? 79  LEU FFF CD1 1 
ATOM 10563 C CD2 . LEU F 2 79  ? 98.718  -20.002 24.908  1.000 76.930  ? 79  LEU FFF CD2 1 
ATOM 10564 N N   . GLN F 2 80  ? 100.088 -16.798 21.613  1.000 59.380  ? 80  GLN FFF N   1 
ATOM 10565 C CA  . GLN F 2 80  ? 99.344  -16.512 20.359  1.000 67.920  ? 80  GLN FFF CA  1 
ATOM 10566 C C   . GLN F 2 80  ? 99.017  -17.837 19.667  1.000 67.640  ? 80  GLN FFF C   1 
ATOM 10567 O O   . GLN F 2 80  ? 99.587  -18.854 20.067  1.000 65.930  ? 80  GLN FFF O   1 
ATOM 10568 C CB  . GLN F 2 80  ? 100.157 -15.604 19.436  1.000 69.020  ? 80  GLN FFF CB  1 
ATOM 10569 C CG  . GLN F 2 80  ? 100.458 -14.247 20.041  1.000 72.530  ? 80  GLN FFF CG  1 
ATOM 10570 C CD  . GLN F 2 80  ? 101.263 -13.380 19.102  1.000 75.420  ? 80  GLN FFF CD  1 
ATOM 10571 O OE1 . GLN F 2 80  ? 101.365 -13.652 17.905  1.000 73.240  ? 80  GLN FFF OE1 1 
ATOM 10572 N NE2 . GLN F 2 80  ? 101.830 -12.310 19.641  1.000 83.490  ? 80  GLN FFF NE2 1 
ATOM 10573 N N   . SER F 2 81  ? 98.112  -17.813 18.681  1.000 65.050  ? 81  SER FFF N   1 
ATOM 10574 C CA  . SER F 2 81  ? 97.635  -19.010 17.950  1.000 60.960  ? 81  SER FFF CA  1 
ATOM 10575 C C   . SER F 2 81  ? 98.768  -19.522 17.054  1.000 61.990  ? 81  SER FFF C   1 
ATOM 10576 O O   . SER F 2 81  ? 98.867  -20.748 16.872  1.000 61.660  ? 81  SER FFF O   1 
ATOM 10577 C CB  . SER F 2 81  ? 96.414  -18.717 17.153  1.000 57.940  ? 81  SER FFF CB  1 
ATOM 10578 O OG  . SER F 2 81  ? 95.860  -19.939 16.710  1.000 64.870  ? 81  SER FFF OG  1 
ATOM 10579 N N   . GLU F 2 82  ? 99.628  -18.612 16.566  1.000 63.150  ? 82  GLU FFF N   1 
ATOM 10580 C CA  . GLU F 2 82  ? 100.798 -18.906 15.697  1.000 65.790  ? 82  GLU FFF CA  1 
ATOM 10581 C C   . GLU F 2 82  ? 101.820 -19.762 16.469  1.000 64.540  ? 82  GLU FFF C   1 
ATOM 10582 O O   . GLU F 2 82  ? 102.763 -20.283 15.815  1.000 74.240  ? 82  GLU FFF O   1 
ATOM 10583 C CB  . GLU F 2 82  ? 101.415 -17.595 15.193  1.000 72.220  ? 82  GLU FFF CB  1 
ATOM 10584 C CG  . GLU F 2 82  ? 100.492 -16.777 14.300  1.000 82.210  ? 82  GLU FFF CG  1 
ATOM 10585 C CD  . GLU F 2 82  ? 99.526  -15.822 14.992  1.000 85.970  ? 82  GLU FFF CD  1 
ATOM 10586 O OE1 . GLU F 2 82  ? 99.497  -15.803 16.227  1.000 86.630  ? 82  GLU FFF OE1 1 
ATOM 10587 O OE2 . GLU F 2 82  ? 98.809  -15.088 14.291  1.000 83.710  ? 82  GLU FFF OE2 1 
ATOM 10588 N N   . ASP F 2 83  ? 101.627 -19.922 17.792  1.000 56.650  ? 83  ASP FFF N   1 
ATOM 10589 C CA  . ASP F 2 83  ? 102.506 -20.701 18.709  1.000 54.010  ? 83  ASP FFF CA  1 
ATOM 10590 C C   . ASP F 2 83  ? 102.029 -22.155 18.821  1.000 48.880  ? 83  ASP FFF C   1 
ATOM 10591 O O   . ASP F 2 83  ? 102.634 -22.917 19.611  1.000 45.590  ? 83  ASP FFF O   1 
ATOM 10592 C CB  . ASP F 2 83  ? 102.542 -20.067 20.109  1.000 54.200  ? 83  ASP FFF CB  1 
ATOM 10593 C CG  . ASP F 2 83  ? 103.260 -18.728 20.152  1.000 55.090  ? 83  ASP FFF CG  1 
ATOM 10594 O OD1 . ASP F 2 83  ? 103.962 -18.416 19.168  1.000 57.650  ? 83  ASP FFF OD1 1 
ATOM 10595 O OD2 . ASP F 2 83  ? 103.129 -18.002 21.165  1.000 50.090  ? 83  ASP FFF OD2 1 
ATOM 10596 N N   . GLU F 2 84  ? 100.977 -22.504 18.088  1.000 45.760  ? 84  GLU FFF N   1 
ATOM 10597 C CA  . GLU F 2 84  ? 100.437 -23.881 18.150  1.000 50.710  ? 84  GLU FFF CA  1 
ATOM 10598 C C   . GLU F 2 84  ? 101.427 -24.799 17.455  1.000 48.080  ? 84  GLU FFF C   1 
ATOM 10599 O O   . GLU F 2 84  ? 101.746 -24.533 16.295  1.000 50.940  ? 84  GLU FFF O   1 
ATOM 10600 C CB  . GLU F 2 84  ? 99.059  -23.977 17.503  1.000 30.000  ? 84  GLU FFF CB  1 
ATOM 10601 C CG  . GLU F 2 84  ? 98.057  -24.770 18.316  1.000 30.000  ? 84  GLU FFF CG  1 
ATOM 10602 C CD  . GLU F 2 84  ? 96.646  -24.215 18.267  1.000 30.000  ? 84  GLU FFF CD  1 
ATOM 10603 O OE1 . GLU F 2 84  ? 96.435  -23.216 17.560  1.000 30.000  ? 84  GLU FFF OE1 1 
ATOM 10604 O OE2 . GLU F 2 84  ? 95.767  -24.780 18.937  1.000 30.000  ? 84  GLU FFF OE2 1 
ATOM 10605 N N   . GLY F 2 85  ? 101.844 -25.860 18.129  1.000 46.050  ? 85  GLY FFF N   1 
ATOM 10606 C CA  . GLY F 2 85  ? 102.889 -26.754 17.596  1.000 46.810  ? 85  GLY FFF CA  1 
ATOM 10607 C C   . GLY F 2 85  ? 103.440 -27.677 18.663  1.000 45.300  ? 85  GLY FFF C   1 
ATOM 10608 O O   . GLY F 2 85  ? 102.942 -27.614 19.793  1.000 41.930  ? 85  GLY FFF O   1 
ATOM 10609 N N   . ASP F 2 86  ? 104.431 -28.499 18.310  1.000 46.390  ? 86  ASP FFF N   1 
ATOM 10610 C CA  . ASP F 2 86  ? 105.192 -29.370 19.240  1.000 44.680  ? 86  ASP FFF CA  1 
ATOM 10611 C C   . ASP F 2 86  ? 106.490 -28.638 19.654  1.000 37.870  ? 86  ASP FFF C   1 
ATOM 10612 O O   . ASP F 2 86  ? 107.137 -27.987 18.793  1.000 34.910  ? 86  ASP FFF O   1 
ATOM 10613 C CB  . ASP F 2 86  ? 105.512 -30.720 18.594  1.000 30.000  ? 86  ASP FFF CB  1 
ATOM 10614 C CG  . ASP F 2 86  ? 104.289 -31.605 18.460  1.000 30.000  ? 86  ASP FFF CG  1 
ATOM 10615 O OD1 . ASP F 2 86  ? 103.264 -31.308 19.108  1.000 30.000  ? 86  ASP FFF OD1 1 
ATOM 10616 O OD2 . ASP F 2 86  ? 104.259 -32.618 17.728  1.000 30.000  ? 86  ASP FFF OD2 1 
ATOM 10617 N N   . TYR F 2 87  ? 106.838 -28.714 20.946  1.000 31.010  ? 87  TYR FFF N   1 
ATOM 10618 C CA  . TYR F 2 87  ? 108.069 -28.131 21.531  1.000 27.670  ? 87  TYR FFF CA  1 
ATOM 10619 C C   . TYR F 2 87  ? 108.943 -29.282 22.031  1.000 27.440  ? 87  TYR FFF C   1 
ATOM 10620 O O   . TYR F 2 87  ? 108.530 -30.036 22.934  1.000 25.770  ? 87  TYR FFF O   1 
ATOM 10621 C CB  . TYR F 2 87  ? 107.702 -27.088 22.592  1.000 27.840  ? 87  TYR FFF CB  1 
ATOM 10622 C CG  . TYR F 2 87  ? 107.067 -25.862 21.987  1.000 27.660  ? 87  TYR FFF CG  1 
ATOM 10623 C CD1 . TYR F 2 87  ? 105.761 -25.895 21.533  1.000 26.440  ? 87  TYR FFF CD1 1 
ATOM 10624 C CD2 . TYR F 2 87  ? 107.805 -24.711 21.749  1.000 28.200  ? 87  TYR FFF CD2 1 
ATOM 10625 C CE1 . TYR F 2 87  ? 105.175 -24.808 20.917  1.000 26.710  ? 87  TYR FFF CE1 1 
ATOM 10626 C CE2 . TYR F 2 87  ? 107.234 -23.605 21.147  1.000 27.740  ? 87  TYR FFF CE2 1 
ATOM 10627 C CZ  . TYR F 2 87  ? 105.916 -23.659 20.716  1.000 27.710  ? 87  TYR FFF CZ  1 
ATOM 10628 O OH  . TYR F 2 87  ? 105.334 -22.593 20.092  1.000 27.030  ? 87  TYR FFF OH  1 
ATOM 10629 N N   . HIS F 2 88  ? 110.112 -29.436 21.412  1.000 28.410  ? 88  HIS FFF N   1 
ATOM 10630 C CA  . HIS F 2 88  ? 111.089 -30.522 21.668  1.000 27.220  ? 88  HIS FFF CA  1 
ATOM 10631 C C   . HIS F 2 88  ? 112.264 -30.067 22.524  1.000 26.240  ? 88  HIS FFF C   1 
ATOM 10632 O O   . HIS F 2 88  ? 112.904 -29.071 22.203  1.000 23.450  ? 88  HIS FFF O   1 
ATOM 10633 C CB  . HIS F 2 88  ? 111.539 -31.140 20.351  1.000 28.510  ? 88  HIS FFF CB  1 
ATOM 10634 C CG  . HIS F 2 88  ? 110.426 -31.739 19.576  1.000 29.750  ? 88  HIS FFF CG  1 
ATOM 10635 N ND1 . HIS F 2 88  ? 109.907 -32.965 19.926  1.000 30.910  ? 88  HIS FFF ND1 1 
ATOM 10636 C CD2 . HIS F 2 88  ? 109.774 -31.305 18.467  1.000 29.950  ? 88  HIS FFF CD2 1 
ATOM 10637 C CE1 . HIS F 2 88  ? 108.955 -33.272 19.052  1.000 36.680  ? 88  HIS FFF CE1 1 
ATOM 10638 N NE2 . HIS F 2 88  ? 108.839 -32.241 18.147  1.000 31.800  ? 88  HIS FFF NE2 1 
ATOM 10639 N N   . CYS F 2 89  ? 112.499 -30.800 23.597  1.000 30.500  ? 89  CYS FFF N   1 
ATOM 10640 C CA  . CYS F 2 89  ? 113.583 -30.582 24.576  1.000 33.100  ? 89  CYS FFF CA  1 
ATOM 10641 C C   . CYS F 2 89  ? 114.742 -31.541 24.304  1.000 29.990  ? 89  CYS FFF C   1 
ATOM 10642 O O   . CYS F 2 89  ? 114.479 -32.734 24.198  1.000 28.650  ? 89  CYS FFF O   1 
ATOM 10643 C CB  . CYS F 2 89  ? 112.974 -30.794 25.961  1.000 35.490  ? 89  CYS FFF CB  1 
ATOM 10644 S SG  . CYS F 2 89  ? 114.158 -30.432 27.269  1.000 47.940  ? 89  CYS FFF SG  1 
ATOM 10645 N N   . ALA F 2 90  ? 115.972 -31.055 24.163  1.000 28.640  ? 90  ALA FFF N   1 
ATOM 10646 C CA  . ALA F 2 90  ? 117.145 -31.905 23.840  1.000 27.750  ? 90  ALA FFF CA  1 
ATOM 10647 C C   . ALA F 2 90  ? 118.381 -31.498 24.634  1.000 28.130  ? 90  ALA FFF C   1 
ATOM 10648 O O   . ALA F 2 90  ? 118.520 -30.295 24.965  1.000 29.560  ? 90  ALA FFF O   1 
ATOM 10649 C CB  . ALA F 2 90  ? 117.463 -31.920 22.373  1.000 28.630  ? 90  ALA FFF CB  1 
ATOM 10650 N N   . ALA F 2 91  ? 119.265 -32.464 24.884  1.000 28.090  ? 91  ALA FFF N   1 
ATOM 10651 C CA  . ALA F 2 91  ? 120.525 -32.252 25.624  1.000 29.220  ? 91  ALA FFF CA  1 
ATOM 10652 C C   . ALA F 2 91  ? 121.422 -33.477 25.457  1.000 28.700  ? 91  ALA FFF C   1 
ATOM 10653 O O   . ALA F 2 91  ? 120.881 -34.595 25.382  1.000 25.050  ? 91  ALA FFF O   1 
ATOM 10654 C CB  . ALA F 2 91  ? 120.214 -32.003 27.075  1.000 30.210  ? 91  ALA FFF CB  1 
ATOM 10655 N N   . TRP F 2 92  ? 122.742 -33.267 25.442  1.000 28.160  ? 92  TRP FFF N   1 
ATOM 10656 C CA  . TRP F 2 92  ? 123.731 -34.374 25.372  1.000 25.650  ? 92  TRP FFF CA  1 
ATOM 10657 C C   . TRP F 2 92  ? 123.728 -35.164 26.674  1.000 25.460  ? 92  TRP FFF C   1 
ATOM 10658 O O   . TRP F 2 92  ? 123.618 -34.530 27.733  1.000 26.310  ? 92  TRP FFF O   1 
ATOM 10659 C CB  . TRP F 2 92  ? 125.126 -33.831 25.101  1.000 24.040  ? 92  TRP FFF CB  1 
ATOM 10660 C CG  . TRP F 2 92  ? 126.178 -34.885 24.970  1.000 22.370  ? 92  TRP FFF CG  1 
ATOM 10661 C CD1 . TRP F 2 92  ? 127.057 -35.295 25.927  1.000 22.330  ? 92  TRP FFF CD1 1 
ATOM 10662 C CD2 . TRP F 2 92  ? 126.469 -35.662 23.793  1.000 21.780  ? 92  TRP FFF CD2 1 
ATOM 10663 N NE1 . TRP F 2 92  ? 127.884 -36.264 25.424  1.000 23.240  ? 92  TRP FFF NE1 1 
ATOM 10664 C CE2 . TRP F 2 92  ? 127.534 -36.518 24.124  1.000 21.420  ? 92  TRP FFF CE2 1 
ATOM 10665 C CE3 . TRP F 2 92  ? 125.912 -35.731 22.511  1.000 22.020  ? 92  TRP FFF CE3 1 
ATOM 10666 C CZ2 . TRP F 2 92  ? 128.074 -37.408 23.212  1.000 21.710  ? 92  TRP FFF CZ2 1 
ATOM 10667 C CZ3 . TRP F 2 92  ? 126.450 -36.614 21.609  1.000 22.720  ? 92  TRP FFF CZ3 1 
ATOM 10668 C CH2 . TRP F 2 92  ? 127.521 -37.435 21.957  1.000 22.970  ? 92  TRP FFF CH2 1 
ATOM 10669 N N   . ASP F 2 93  ? 123.873 -36.487 26.595  1.000 25.970  ? 93  ASP FFF N   1 
ATOM 10670 C CA  . ASP F 2 93  ? 124.011 -37.348 27.796  1.000 27.580  ? 93  ASP FFF CA  1 
ATOM 10671 C C   . ASP F 2 93  ? 125.408 -37.965 27.793  1.000 26.040  ? 93  ASP FFF C   1 
ATOM 10672 O O   . ASP F 2 93  ? 125.719 -38.678 26.848  1.000 24.310  ? 93  ASP FFF O   1 
ATOM 10673 C CB  . ASP F 2 93  ? 122.905 -38.402 27.875  1.000 27.540  ? 93  ASP FFF CB  1 
ATOM 10674 C CG  . ASP F 2 93  ? 122.988 -39.209 29.148  1.000 28.470  ? 93  ASP FFF CG  1 
ATOM 10675 O OD1 . ASP F 2 93  ? 124.074 -39.801 29.361  1.000 28.300  ? 93  ASP FFF OD1 1 
ATOM 10676 O OD2 . ASP F 2 93  ? 122.007 -39.186 29.933  1.000 27.760  ? 93  ASP FFF OD2 1 
ATOM 10677 N N   . ASP F 2 94  ? 126.188 -37.676 28.825  1.000 27.770  ? 94  ASP FFF N   1 
ATOM 10678 C CA  . ASP F 2 94  ? 127.611 -38.083 28.944  1.000 30.680  ? 94  ASP FFF CA  1 
ATOM 10679 C C   . ASP F 2 94  ? 127.733 -39.589 29.100  1.000 31.220  ? 94  ASP FFF C   1 
ATOM 10680 O O   . ASP F 2 94  ? 128.759 -40.125 28.661  1.000 27.740  ? 94  ASP FFF O   1 
ATOM 10681 C CB  . ASP F 2 94  ? 128.300 -37.427 30.138  1.000 32.470  ? 94  ASP FFF CB  1 
ATOM 10682 C CG  . ASP F 2 94  ? 128.600 -35.959 29.911  1.000 34.810  ? 94  ASP FFF CG  1 
ATOM 10683 O OD1 . ASP F 2 94  ? 128.921 -35.615 28.730  1.000 41.780  ? 94  ASP FFF OD1 1 
ATOM 10684 O OD2 . ASP F 2 94  ? 128.510 -35.172 30.900  1.000 32.980  ? 94  ASP FFF OD2 1 
ATOM 10685 N N   . SER F 2 95  ? 126.743 -40.229 29.715  1.000 36.610  ? 95  SER FFF N   1 
ATOM 10686 C CA  . SER F 2 95  ? 126.755 -41.689 29.972  1.000 43.140  ? 95  SER FFF CA  1 
ATOM 10687 C C   . SER F 2 95  ? 126.435 -42.432 28.670  1.000 37.530  ? 95  SER FFF C   1 
ATOM 10688 O O   . SER F 2 95  ? 127.225 -43.329 28.324  1.000 41.230  ? 95  SER FFF O   1 
ATOM 10689 C CB  . SER F 2 95  ? 125.831 -42.067 31.130  1.000 50.140  ? 95  SER FFF CB  1 
ATOM 10690 O OG  . SER F 2 95  ? 124.473 -41.775 30.831  1.000 57.480  ? 95  SER FFF OG  1 
ATOM 10691 N N   . LEU F 2 96  ? 125.415 -42.017 27.932  1.000 33.190  ? 96  LEU FFF N   1 
ATOM 10692 C CA  . LEU F 2 96  ? 124.961 -42.700 26.688  1.000 32.640  ? 96  LEU FFF CA  1 
ATOM 10693 C C   . LEU F 2 96  ? 125.814 -42.262 25.502  1.000 32.040  ? 96  LEU FFF C   1 
ATOM 10694 O O   . LEU F 2 96  ? 125.625 -42.812 24.420  1.000 34.010  ? 96  LEU FFF O   1 
ATOM 10695 C CB  . LEU F 2 96  ? 123.498 -42.386 26.387  1.000 32.970  ? 96  LEU FFF CB  1 
ATOM 10696 C CG  . LEU F 2 96  ? 122.507 -42.642 27.520  1.000 36.670  ? 96  LEU FFF CG  1 
ATOM 10697 C CD1 . LEU F 2 96  ? 121.071 -42.411 27.047  1.000 35.350  ? 96  LEU FFF CD1 1 
ATOM 10698 C CD2 . LEU F 2 96  ? 122.667 -44.060 28.059  1.000 37.750  ? 96  LEU FFF CD2 1 
ATOM 10699 N N   . LYS F 2 97  ? 126.720 -41.303 25.685  1.000 34.190  ? 97  LYS FFF N   1 
ATOM 10700 C CA  . LYS F 2 97  ? 127.493 -40.668 24.581  1.000 36.170  ? 97  LYS FFF CA  1 
ATOM 10701 C C   . LYS F 2 97  ? 126.556 -40.456 23.380  1.000 33.300  ? 97  LYS FFF C   1 
ATOM 10702 O O   . LYS F 2 97  ? 126.842 -40.951 22.282  1.000 34.280  ? 97  LYS FFF O   1 
ATOM 10703 C CB  . LYS F 2 97  ? 128.727 -41.518 24.260  1.000 39.890  ? 97  LYS FFF CB  1 
ATOM 10704 C CG  . LYS F 2 97  ? 129.750 -41.643 25.384  1.000 46.660  ? 97  LYS FFF CG  1 
ATOM 10705 C CD  . LYS F 2 97  ? 130.557 -40.381 25.630  1.000 54.160  ? 97  LYS FFF CD  1 
ATOM 10706 C CE  . LYS F 2 97  ? 131.525 -40.503 26.797  1.000 55.600  ? 97  LYS FFF CE  1 
ATOM 10707 N NZ  . LYS F 2 97  ? 132.096 -39.186 27.173  1.000 54.940  ? 97  LYS FFF NZ  1 
ATOM 10708 N N   . GLY F 2 98  ? 125.469 -39.716 23.582  1.000 30.600  ? 98  GLY FFF N   1 
ATOM 10709 C CA  . GLY F 2 98  ? 124.512 -39.373 22.521  1.000 30.290  ? 98  GLY FFF CA  1 
ATOM 10710 C C   . GLY F 2 98  ? 123.599 -38.230 22.930  1.000 31.600  ? 98  GLY FFF C   1 
ATOM 10711 O O   . GLY F 2 98  ? 123.642 -37.797 24.098  1.000 34.750  ? 98  GLY FFF O   1 
ATOM 10712 N N   . TRP F 2 99  ? 122.795 -37.741 21.998  1.000 29.800  ? 99  TRP FFF N   1 
ATOM 10713 C CA  . TRP F 2 99  ? 121.728 -36.751 22.268  1.000 29.180  ? 99  TRP FFF CA  1 
ATOM 10714 C C   . TRP F 2 99  ? 120.490 -37.489 22.772  1.000 27.720  ? 99  TRP FFF C   1 
ATOM 10715 O O   . TRP F 2 99  ? 120.068 -38.452 22.121  1.000 28.100  ? 99  TRP FFF O   1 
ATOM 10716 C CB  . TRP F 2 99  ? 121.440 -35.921 21.015  1.000 31.500  ? 99  TRP FFF CB  1 
ATOM 10717 C CG  . TRP F 2 99  ? 122.591 -35.043 20.634  1.000 32.610  ? 99  TRP FFF CG  1 
ATOM 10718 C CD1 . TRP F 2 99  ? 123.576 -35.300 19.729  1.000 33.790  ? 99  TRP FFF CD1 1 
ATOM 10719 C CD2 . TRP F 2 99  ? 122.900 -33.761 21.198  1.000 32.470  ? 99  TRP FFF CD2 1 
ATOM 10720 N NE1 . TRP F 2 99  ? 124.464 -34.256 19.674  1.000 33.460  ? 99  TRP FFF NE1 1 
ATOM 10721 C CE2 . TRP F 2 99  ? 124.071 -33.302 20.569  1.000 31.500  ? 99  TRP FFF CE2 1 
ATOM 10722 C CE3 . TRP F 2 99  ? 122.300 -32.965 22.175  1.000 33.540  ? 99  TRP FFF CE3 1 
ATOM 10723 C CZ2 . TRP F 2 99  ? 124.653 -32.084 20.889  1.000 32.580  ? 99  TRP FFF CZ2 1 
ATOM 10724 C CZ3 . TRP F 2 99  ? 122.872 -31.753 22.483  1.000 37.060  ? 99  TRP FFF CZ3 1 
ATOM 10725 C CH2 . TRP F 2 99  ? 124.047 -31.330 21.863  1.000 35.550  ? 99  TRP FFF CH2 1 
ATOM 10726 N N   . VAL F 2 100 ? 119.948 -37.050 23.902  1.000 28.960  ? 100 VAL FFF N   1 
ATOM 10727 C CA  . VAL F 2 100 ? 118.589 -37.437 24.392  1.000 29.070  ? 100 VAL FFF CA  1 
ATOM 10728 C C   . VAL F 2 100 ? 117.608 -36.284 24.133  1.000 28.980  ? 100 VAL FFF C   1 
ATOM 10729 O O   . VAL F 2 100 ? 118.011 -35.100 24.253  1.000 33.490  ? 100 VAL FFF O   1 
ATOM 10730 C CB  . VAL F 2 100 ? 118.625 -37.848 25.873  1.000 29.130  ? 100 VAL FFF CB  1 
ATOM 10731 C CG1 . VAL F 2 100 ? 119.576 -39.008 26.074  1.000 30.960  ? 100 VAL FFF CG1 1 
ATOM 10732 C CG2 . VAL F 2 100 ? 119.014 -36.713 26.798  1.000 31.070  ? 100 VAL FFF CG2 1 
ATOM 10733 N N   . PHE F 2 101 ? 116.388 -36.619 23.713  1.000 27.010  ? 101 PHE FFF N   1 
ATOM 10734 C CA  . PHE F 2 101 ? 115.264 -35.669 23.514  1.000 25.540  ? 101 PHE FFF CA  1 
ATOM 10735 C C   . PHE F 2 101 ? 114.194 -36.017 24.532  1.000 25.260  ? 101 PHE FFF C   1 
ATOM 10736 O O   . PHE F 2 101 ? 114.323 -37.033 25.203  1.000 29.330  ? 101 PHE FFF O   1 
ATOM 10737 C CB  . PHE F 2 101 ? 114.696 -35.728 22.095  1.000 24.650  ? 101 PHE FFF CB  1 
ATOM 10738 C CG  . PHE F 2 101 ? 115.590 -35.112 21.047  1.000 25.300  ? 101 PHE FFF CG  1 
ATOM 10739 C CD1 . PHE F 2 101 ? 116.684 -35.798 20.552  1.000 25.700  ? 101 PHE FFF CD1 1 
ATOM 10740 C CD2 . PHE F 2 101 ? 115.360 -33.832 20.567  1.000 25.770  ? 101 PHE FFF CD2 1 
ATOM 10741 C CE1 . PHE F 2 101 ? 117.528 -35.220 19.616  1.000 26.020  ? 101 PHE FFF CE1 1 
ATOM 10742 C CE2 . PHE F 2 101 ? 116.197 -33.261 19.619  1.000 24.900  ? 101 PHE FFF CE2 1 
ATOM 10743 C CZ  . PHE F 2 101 ? 117.279 -33.959 19.142  1.000 25.230  ? 101 PHE FFF CZ  1 
ATOM 10744 N N   . GLY F 2 102 ? 113.225 -35.134 24.685  1.000 26.430  ? 102 GLY FFF N   1 
ATOM 10745 C CA  . GLY F 2 102 ? 111.998 -35.380 25.448  1.000 28.420  ? 102 GLY FFF CA  1 
ATOM 10746 C C   . GLY F 2 102 ? 110.978 -36.011 24.543  1.000 30.480  ? 102 GLY FFF C   1 
ATOM 10747 O O   . GLY F 2 102 ? 111.332 -36.350 23.391  1.000 31.580  ? 102 GLY FFF O   1 
ATOM 10748 N N   . GLY F 2 103 ? 109.766 -36.199 25.057  1.000 33.170  ? 103 GLY FFF N   1 
ATOM 10749 C CA  . GLY F 2 103 ? 108.663 -36.807 24.300  1.000 33.710  ? 103 GLY FFF CA  1 
ATOM 10750 C C   . GLY F 2 103 ? 108.181 -35.843 23.256  1.000 33.790  ? 103 GLY FFF C   1 
ATOM 10751 O O   . GLY F 2 103 ? 107.685 -36.285 22.219  1.000 37.650  ? 103 GLY FFF O   1 
ATOM 10752 N N   . GLY F 2 104 ? 108.356 -34.561 23.510  1.000 35.750  ? 104 GLY FFF N   1 
ATOM 10753 C CA  . GLY F 2 104 ? 107.601 -33.523 22.791  1.000 43.920  ? 104 GLY FFF CA  1 
ATOM 10754 C C   . GLY F 2 104 ? 106.404 -33.082 23.627  1.000 45.030  ? 104 GLY FFF C   1 
ATOM 10755 O O   . GLY F 2 104 ? 105.906 -33.884 24.470  1.000 43.710  ? 104 GLY FFF O   1 
ATOM 10756 N N   . THR F 2 105 ? 106.005 -31.829 23.439  1.000 40.550  ? 105 THR FFF N   1 
ATOM 10757 C CA  . THR F 2 105 ? 104.895 -31.169 24.152  1.000 37.720  ? 105 THR FFF CA  1 
ATOM 10758 C C   . THR F 2 105 ? 104.041 -30.494 23.096  1.000 37.810  ? 105 THR FFF C   1 
ATOM 10759 O O   . THR F 2 105 ? 104.562 -29.556 22.467  1.000 39.060  ? 105 THR FFF O   1 
ATOM 10760 C CB  . THR F 2 105 ? 105.453 -30.171 25.170  1.000 39.180  ? 105 THR FFF CB  1 
ATOM 10761 O OG1 . THR F 2 105 ? 106.255 -30.895 26.098  1.000 37.460  ? 105 THR FFF OG1 1 
ATOM 10762 C CG2 . THR F 2 105 ? 104.383 -29.409 25.915  1.000 41.500  ? 105 THR FFF CG2 1 
ATOM 10763 N N   . LYS F 2 106 ? 102.839 -31.011 22.847  1.000 42.130  ? 106 LYS FFF N   1 
ATOM 10764 C CA  . LYS F 2 106 ? 101.886 -30.377 21.903  1.000 47.690  ? 106 LYS FFF CA  1 
ATOM 10765 C C   . LYS F 2 106 ? 101.167 -29.269 22.677  1.000 43.750  ? 106 LYS FFF C   1 
ATOM 10766 O O   . LYS F 2 106 ? 100.477 -29.565 23.676  1.000 44.310  ? 106 LYS FFF O   1 
ATOM 10767 C CB  . LYS F 2 106 ? 100.937 -31.406 21.282  1.000 51.930  ? 106 LYS FFF CB  1 
ATOM 10768 C CG  . LYS F 2 106 ? 100.141 -30.908 20.084  1.000 57.930  ? 106 LYS FFF CG  1 
ATOM 10769 C CD  . LYS F 2 106 ? 99.318  -32.024 19.433  1.000 63.590  ? 106 LYS FFF CD  1 
ATOM 10770 C CE  . LYS F 2 106 ? 98.664  -31.605 18.134  1.000 70.390  ? 106 LYS FFF CE  1 
ATOM 10771 N NZ  . LYS F 2 106 ? 97.640  -30.556 18.355  1.000 79.250  ? 106 LYS FFF NZ  1 
ATOM 10772 N N   . LEU F 2 107 ? 101.413 -28.032 22.268  1.000 41.550  ? 107 LEU FFF N   1 
ATOM 10773 C CA  . LEU F 2 107 ? 100.848 -26.812 22.882  1.000 43.450  ? 107 LEU FFF CA  1 
ATOM 10774 C C   . LEU F 2 107 ? 99.600  -26.462 22.100  1.000 45.840  ? 107 LEU FFF C   1 
ATOM 10775 O O   . LEU F 2 107 ? 99.736  -26.142 20.904  1.000 55.600  ? 107 LEU FFF O   1 
ATOM 10776 C CB  . LEU F 2 107 ? 101.868 -25.678 22.817  1.000 48.460  ? 107 LEU FFF CB  1 
ATOM 10777 C CG  . LEU F 2 107 ? 101.511 -24.431 23.605  1.000 53.670  ? 107 LEU FFF CG  1 
ATOM 10778 C CD1 . LEU F 2 107 ? 100.370 -23.665 22.984  1.000 57.480  ? 107 LEU FFF CD1 1 
ATOM 10779 C CD2 . LEU F 2 107 ? 101.186 -24.781 25.047  1.000 56.960  ? 107 LEU FFF CD2 1 
ATOM 10780 N N   . THR F 2 108 ? 98.432  -26.558 22.743  1.000 52.910  ? 108 THR FFF N   1 
ATOM 10781 C CA  . THR F 2 108 ? 97.118  -26.143 22.188  1.000 55.400  ? 108 THR FFF CA  1 
ATOM 10782 C C   . THR F 2 108 ? 96.802  -24.736 22.706  1.000 56.160  ? 108 THR FFF C   1 
ATOM 10783 O O   . THR F 2 108 ? 97.034  -24.487 23.892  1.000 55.260  ? 108 THR FFF O   1 
ATOM 10784 C CB  . THR F 2 108 ? 96.033  -27.177 22.520  1.000 55.070  ? 108 THR FFF CB  1 
ATOM 10785 O OG1 . THR F 2 108 ? 96.512  -28.451 22.098  1.000 56.660  ? 108 THR FFF OG1 1 
ATOM 10786 C CG2 . THR F 2 108 ? 94.710  -26.894 21.848  1.000 54.850  ? 108 THR FFF CG2 1 
ATOM 10787 N N   . VAL F 2 109 ? 96.347  -23.859 21.810  1.000 62.540  ? 109 VAL FFF N   1 
ATOM 10788 C CA  . VAL F 2 109 ? 95.899  -22.468 22.105  1.000 66.780  ? 109 VAL FFF CA  1 
ATOM 10789 C C   . VAL F 2 109 ? 94.378  -22.426 21.955  1.000 72.650  ? 109 VAL FFF C   1 
ATOM 10790 O O   . VAL F 2 109 ? 93.873  -22.768 20.850  1.000 67.060  ? 109 VAL FFF O   1 
ATOM 10791 C CB  . VAL F 2 109 ? 96.554  -21.451 21.160  1.000 69.180  ? 109 VAL FFF CB  1 
ATOM 10792 C CG1 . VAL F 2 109 ? 96.346  -20.034 21.663  1.000 70.500  ? 109 VAL FFF CG1 1 
ATOM 10793 C CG2 . VAL F 2 109 ? 98.027  -21.740 20.953  1.000 73.300  ? 109 VAL FFF CG2 1 
ATOM 10794 N N   . LEU F 2 110 ? 93.686  -21.963 22.997  1.000 81.880  ? 110 LEU FFF N   1 
ATOM 10795 C CA  . LEU F 2 110 ? 92.205  -21.990 23.084  1.000 94.550  ? 110 LEU FFF CA  1 
ATOM 10796 C C   . LEU F 2 110 ? 91.624  -20.634 22.647  1.000 108.140 ? 110 LEU FFF C   1 
ATOM 10797 O O   . LEU F 2 110 ? 92.420  -19.713 22.432  1.000 116.950 ? 110 LEU FFF O   1 
ATOM 10798 C CB  . LEU F 2 110 ? 91.848  -22.396 24.512  1.000 95.410  ? 110 LEU FFF CB  1 
ATOM 10799 C CG  . LEU F 2 110 ? 92.501  -23.708 24.964  1.000 92.510  ? 110 LEU FFF CG  1 
ATOM 10800 C CD1 . LEU F 2 110 ? 92.191  -23.996 26.421  1.000 89.110  ? 110 LEU FFF CD1 1 
ATOM 10801 C CD2 . LEU F 2 110 ? 92.084  -24.897 24.098  1.000 91.110  ? 110 LEU FFF CD2 1 
ATOM 10802 N N   . GLY F 2 111 ? 90.317  -20.582 22.361  1.000 104.830 ? 111 GLY FFF N   1 
ATOM 10803 C CA  . GLY F 2 111 ? 89.675  -19.481 21.611  1.000 96.090  ? 111 GLY FFF CA  1 
ATOM 10804 C C   . GLY F 2 111 ? 88.849  -19.988 20.449  1.000 90.730  ? 111 GLY FFF C   1 
ATOM 10805 O O   . GLY F 2 111 ? 87.814  -19.384 20.194  1.000 88.820  ? 111 GLY FFF O   1 
ATOM 10806 N N   . ALA F 2 112 ? 89.251  -21.099 19.812  1.000 99.240  ? 112 ALA FFF N   1 
ATOM 10807 C CA  . ALA F 2 112 ? 88.509  -21.822 18.743  1.000 107.780 ? 112 ALA FFF CA  1 
ATOM 10808 C C   . ALA F 2 112 ? 87.233  -22.464 19.309  1.000 109.480 ? 112 ALA FFF C   1 
ATOM 10809 O O   . ALA F 2 112 ? 87.312  -23.392 20.112  1.000 108.690 ? 112 ALA FFF O   1 
ATOM 10810 C CB  . ALA F 2 112 ? 89.403  -22.862 18.093  1.000 98.620  ? 112 ALA FFF CB  1 
ATOM 10811 N N   . PRO F 2 113 ? 86.019  -21.992 18.928  1.000 104.260 ? 113 PRO FFF N   1 
ATOM 10812 C CA  . PRO F 2 113 ? 84.788  -22.514 19.520  1.000 92.190  ? 113 PRO FFF CA  1 
ATOM 10813 C C   . PRO F 2 113 ? 84.438  -23.907 18.970  1.000 82.780  ? 113 PRO FFF C   1 
ATOM 10814 O O   . PRO F 2 113 ? 84.922  -24.234 17.894  1.000 74.880  ? 113 PRO FFF O   1 
ATOM 10815 C CB  . PRO F 2 113 ? 83.745  -21.455 19.118  1.000 100.400 ? 113 PRO FFF CB  1 
ATOM 10816 C CG  . PRO F 2 113 ? 84.271  -20.871 17.809  1.000 101.630 ? 113 PRO FFF CG  1 
ATOM 10817 C CD  . PRO F 2 113 ? 85.775  -20.917 17.944  1.000 101.340 ? 113 PRO FFF CD  1 
ATOM 10818 N N   . LYS F 2 114 ? 83.603  -24.661 19.704  1.000 75.780  ? 114 LYS FFF N   1 
ATOM 10819 C CA  . LYS F 2 114 ? 83.055  -26.000 19.328  1.000 71.600  ? 114 LYS FFF CA  1 
ATOM 10820 C C   . LYS F 2 114 ? 82.276  -25.901 18.002  1.000 78.200  ? 114 LYS FFF C   1 
ATOM 10821 O O   . LYS F 2 114 ? 81.501  -24.949 17.842  1.000 70.010  ? 114 LYS FFF O   1 
ATOM 10822 C CB  . LYS F 2 114 ? 82.191  -26.578 20.461  1.000 54.550  ? 114 LYS FFF CB  1 
ATOM 10823 N N   . ALA F 2 115 ? 82.540  -26.829 17.064  1.000 92.200  ? 115 ALA FFF N   1 
ATOM 10824 C CA  . ALA F 2 115 ? 81.901  -26.927 15.727  1.000 89.010  ? 115 ALA FFF CA  1 
ATOM 10825 C C   . ALA F 2 115 ? 81.275  -28.318 15.525  1.000 89.460  ? 115 ALA FFF C   1 
ATOM 10826 O O   . ALA F 2 115 ? 81.678  -29.301 16.202  1.000 69.540  ? 115 ALA FFF O   1 
ATOM 10827 C CB  . ALA F 2 115 ? 82.910  -26.621 14.646  1.000 85.080  ? 115 ALA FFF CB  1 
ATOM 10828 N N   . ASN F 2 116 ? 80.365  -28.411 14.550  1.000 107.800 ? 116 ASN FFF N   1 
ATOM 10829 C CA  . ASN F 2 116 ? 79.464  -29.578 14.305  1.000 114.880 ? 116 ASN FFF CA  1 
ATOM 10830 C C   . ASN F 2 116 ? 80.229  -30.705 13.590  1.000 108.770 ? 116 ASN FFF C   1 
ATOM 10831 O O   . ASN F 2 116 ? 80.634  -30.532 12.440  1.000 124.380 ? 116 ASN FFF O   1 
ATOM 10832 C CB  . ASN F 2 116 ? 78.155  -29.112 13.627  1.000 121.110 ? 116 ASN FFF CB  1 
ATOM 10833 C CG  . ASN F 2 116 ? 78.252  -28.608 12.190  1.000 117.260 ? 116 ASN FFF CG  1 
ATOM 10834 O OD1 . ASN F 2 116 ? 79.118  -27.805 11.837  1.000 115.050 ? 116 ASN FFF OD1 1 
ATOM 10835 N ND2 . ASN F 2 116 ? 77.310  -29.023 11.355  1.000 97.780  ? 116 ASN FFF ND2 1 
ATOM 10836 N N   . PRO F 2 117 ? 80.522  -31.853 14.263  1.000 92.930  ? 117 PRO FFF N   1 
ATOM 10837 C CA  . PRO F 2 117 ? 81.098  -33.021 13.589  1.000 88.740  ? 117 PRO FFF CA  1 
ATOM 10838 C C   . PRO F 2 117 ? 80.064  -33.667 12.651  1.000 89.090  ? 117 PRO FFF C   1 
ATOM 10839 O O   . PRO F 2 117 ? 79.315  -34.499 13.120  1.000 95.180  ? 117 PRO FFF O   1 
ATOM 10840 C CB  . PRO F 2 117 ? 81.516  -33.949 14.742  1.000 86.670  ? 117 PRO FFF CB  1 
ATOM 10841 C CG  . PRO F 2 117 ? 80.607  -33.551 15.883  1.000 87.930  ? 117 PRO FFF CG  1 
ATOM 10842 C CD  . PRO F 2 117 ? 80.378  -32.063 15.716  1.000 84.760  ? 117 PRO FFF CD  1 
ATOM 10843 N N   . THR F 2 118 ? 80.005  -33.199 11.399  1.000 83.810  ? 118 THR FFF N   1 
ATOM 10844 C CA  . THR F 2 118 ? 79.047  -33.649 10.342  1.000 86.590  ? 118 THR FFF CA  1 
ATOM 10845 C C   . THR F 2 118 ? 79.372  -35.098 9.941   1.000 78.520  ? 118 THR FFF C   1 
ATOM 10846 O O   . THR F 2 118 ? 80.567  -35.401 9.872   1.000 82.340  ? 118 THR FFF O   1 
ATOM 10847 C CB  . THR F 2 118 ? 79.091  -32.708 9.127   1.000 91.320  ? 118 THR FFF CB  1 
ATOM 10848 O OG1 . THR F 2 118 ? 80.421  -32.746 8.619   1.000 95.220  ? 118 THR FFF OG1 1 
ATOM 10849 C CG2 . THR F 2 118 ? 78.729  -31.269 9.433   1.000 93.020  ? 118 THR FFF CG2 1 
ATOM 10850 N N   . VAL F 2 119 ? 78.371  -35.961 9.732   1.000 73.140  ? 119 VAL FFF N   1 
ATOM 10851 C CA  . VAL F 2 119 ? 78.567  -37.426 9.501   1.000 79.820  ? 119 VAL FFF CA  1 
ATOM 10852 C C   . VAL F 2 119 ? 77.779  -37.850 8.256   1.000 83.000  ? 119 VAL FFF C   1 
ATOM 10853 O O   . VAL F 2 119 ? 76.596  -37.510 8.163   1.000 102.800 ? 119 VAL FFF O   1 
ATOM 10854 C CB  . VAL F 2 119 ? 78.178  -38.260 10.737  1.000 82.430  ? 119 VAL FFF CB  1 
ATOM 10855 C CG1 . VAL F 2 119 ? 78.089  -39.741 10.400  1.000 86.030  ? 119 VAL FFF CG1 1 
ATOM 10856 C CG2 . VAL F 2 119 ? 79.137  -38.010 11.890  1.000 79.160  ? 119 VAL FFF CG2 1 
ATOM 10857 N N   . THR F 2 120 ? 78.432  -38.587 7.354   1.000 80.160  ? 120 THR FFF N   1 
ATOM 10858 C CA  . THR F 2 120 ? 78.025  -38.837 5.942   1.000 80.960  ? 120 THR FFF CA  1 
ATOM 10859 C C   . THR F 2 120 ? 78.208  -40.336 5.636   1.000 83.530  ? 120 THR FFF C   1 
ATOM 10860 O O   . THR F 2 120 ? 78.887  -40.655 4.633   1.000 82.540  ? 120 THR FFF O   1 
ATOM 10861 C CB  . THR F 2 120 ? 78.860  -37.932 5.004   1.000 79.250  ? 120 THR FFF CB  1 
ATOM 10862 O OG1 . THR F 2 120 ? 78.779  -36.594 5.503   1.000 77.560  ? 120 THR FFF OG1 1 
ATOM 10863 C CG2 . THR F 2 120 ? 78.436  -37.935 3.547   1.000 73.160  ? 120 THR FFF CG2 1 
ATOM 10864 N N   . LEU F 2 121 ? 77.585  -41.219 6.440   1.000 85.860  ? 121 LEU FFF N   1 
ATOM 10865 C CA  . LEU F 2 121 ? 77.762  -42.708 6.367   1.000 86.440  ? 121 LEU FFF CA  1 
ATOM 10866 C C   . LEU F 2 121 ? 77.171  -43.295 5.067   1.000 84.190  ? 121 LEU FFF C   1 
ATOM 10867 O O   . LEU F 2 121 ? 75.926  -43.301 4.914   1.000 88.590  ? 121 LEU FFF O   1 
ATOM 10868 C CB  . LEU F 2 121 ? 77.148  -43.354 7.621   1.000 88.930  ? 121 LEU FFF CB  1 
ATOM 10869 C CG  . LEU F 2 121 ? 77.024  -44.884 7.636   1.000 88.340  ? 121 LEU FFF CG  1 
ATOM 10870 C CD1 . LEU F 2 121 ? 78.379  -45.560 7.794   1.000 90.750  ? 121 LEU FFF CD1 1 
ATOM 10871 C CD2 . LEU F 2 121 ? 76.090  -45.346 8.746   1.000 90.470  ? 121 LEU FFF CD2 1 
ATOM 10872 N N   . PHE F 2 122 ? 78.036  -43.825 4.188   1.000 80.940  ? 122 PHE FFF N   1 
ATOM 10873 C CA  . PHE F 2 122 ? 77.709  -44.450 2.878   1.000 81.000  ? 122 PHE FFF CA  1 
ATOM 10874 C C   . PHE F 2 122 ? 77.592  -45.967 3.052   1.000 86.150  ? 122 PHE FFF C   1 
ATOM 10875 O O   . PHE F 2 122 ? 78.344  -46.574 3.810   1.000 84.320  ? 122 PHE FFF O   1 
ATOM 10876 C CB  . PHE F 2 122 ? 78.782  -44.136 1.826   1.000 70.990  ? 122 PHE FFF CB  1 
ATOM 10877 C CG  . PHE F 2 122 ? 78.876  -42.713 1.339   1.000 66.400  ? 122 PHE FFF CG  1 
ATOM 10878 C CD1 . PHE F 2 122 ? 79.588  -41.771 2.059   1.000 73.660  ? 122 PHE FFF CD1 1 
ATOM 10879 C CD2 . PHE F 2 122 ? 78.341  -42.334 0.117   1.000 65.850  ? 122 PHE FFF CD2 1 
ATOM 10880 C CE1 . PHE F 2 122 ? 79.719  -40.467 1.602   1.000 74.420  ? 122 PHE FFF CE1 1 
ATOM 10881 C CE2 . PHE F 2 122 ? 78.480  -41.033 -0.348  1.000 67.320  ? 122 PHE FFF CE2 1 
ATOM 10882 C CZ  . PHE F 2 122 ? 79.163  -40.099 0.399   1.000 70.650  ? 122 PHE FFF CZ  1 
ATOM 10883 N N   . PRO F 2 123 ? 76.677  -46.652 2.322   1.000 96.670  ? 123 PRO FFF N   1 
ATOM 10884 C CA  . PRO F 2 123 ? 76.670  -48.117 2.295   1.000 91.200  ? 123 PRO FFF CA  1 
ATOM 10885 C C   . PRO F 2 123 ? 77.733  -48.700 1.356   1.000 82.990  ? 123 PRO FFF C   1 
ATOM 10886 O O   . PRO F 2 123 ? 78.422  -47.967 0.656   1.000 85.950  ? 123 PRO FFF O   1 
ATOM 10887 C CB  . PRO F 2 123 ? 75.251  -48.421 1.783   1.000 103.310 ? 123 PRO FFF CB  1 
ATOM 10888 C CG  . PRO F 2 123 ? 74.921  -47.244 0.862   1.000 104.700 ? 123 PRO FFF CG  1 
ATOM 10889 C CD  . PRO F 2 123 ? 75.611  -46.053 1.489   1.000 102.990 ? 123 PRO FFF CD  1 
ATOM 10890 N N   . PRO F 2 124 ? 77.890  -50.041 1.287   1.000 74.800  ? 124 PRO FFF N   1 
ATOM 10891 C CA  . PRO F 2 124 ? 78.587  -50.698 0.173   1.000 74.330  ? 124 PRO FFF CA  1 
ATOM 10892 C C   . PRO F 2 124 ? 78.031  -50.375 -1.228  1.000 71.760  ? 124 PRO FFF C   1 
ATOM 10893 O O   . PRO F 2 124 ? 77.063  -49.696 -1.313  1.000 70.350  ? 124 PRO FFF O   1 
ATOM 10894 C CB  . PRO F 2 124 ? 78.407  -52.203 0.444   1.000 77.330  ? 124 PRO FFF CB  1 
ATOM 10895 C CG  . PRO F 2 124 ? 77.451  -52.329 1.632   1.000 75.710  ? 124 PRO FFF CG  1 
ATOM 10896 C CD  . PRO F 2 124 ? 77.423  -50.981 2.312   1.000 72.820  ? 124 PRO FFF CD  1 
ATOM 10897 N N   . SER F 2 125 ? 78.611  -50.952 -2.287  1.000 75.960  ? 125 SER FFF N   1 
ATOM 10898 C CA  . SER F 2 125 ? 78.325  -50.632 -3.714  1.000 77.330  ? 125 SER FFF CA  1 
ATOM 10899 C C   . SER F 2 125 ? 78.310  -51.886 -4.631  1.000 77.680  ? 125 SER FFF C   1 
ATOM 10900 O O   . SER F 2 125 ? 77.420  -51.962 -5.536  1.000 59.160  ? 125 SER FFF O   1 
ATOM 10901 C CB  . SER F 2 125 ? 79.324  -49.603 -4.168  1.000 79.650  ? 125 SER FFF CB  1 
ATOM 10902 O OG  . SER F 2 125 ? 79.033  -49.189 -5.492  1.000 103.180 ? 125 SER FFF OG  1 
ATOM 10903 N N   . SER F 2 126 ? 79.283  -52.803 -4.466  1.000 86.160  ? 126 SER FFF N   1 
ATOM 10904 C CA  . SER F 2 126 ? 79.414  -54.106 -5.187  1.000 73.530  ? 126 SER FFF CA  1 
ATOM 10905 C C   . SER F 2 126 ? 79.927  -55.194 -4.220  1.000 68.000  ? 126 SER FFF C   1 
ATOM 10906 O O   . SER F 2 126 ? 81.120  -55.110 -3.792  1.000 55.830  ? 126 SER FFF O   1 
ATOM 10907 C CB  . SER F 2 126 ? 80.321  -53.980 -6.416  1.000 64.480  ? 126 SER FFF CB  1 
ATOM 10908 O OG  . SER F 2 126 ? 80.014  -52.816 -7.180  1.000 50.310  ? 126 SER FFF OG  1 
ATOM 10909 N N   . ASN F 2 132 ? 81.925  -60.804 -4.502  1.000 73.870  ? 132 ASN FFF N   1 
ATOM 10910 C CA  . ASN F 2 132 ? 82.700  -59.584 -4.152  1.000 70.660  ? 132 ASN FFF CA  1 
ATOM 10911 C C   . ASN F 2 132 ? 82.654  -59.413 -2.613  1.000 75.440  ? 132 ASN FFF C   1 
ATOM 10912 O O   . ASN F 2 132 ? 82.350  -60.395 -1.885  1.000 61.490  ? 132 ASN FFF O   1 
ATOM 10913 C CB  . ASN F 2 132 ? 82.302  -58.378 -5.042  1.000 71.630  ? 132 ASN FFF CB  1 
ATOM 10914 C CG  . ASN F 2 132 ? 80.823  -58.192 -5.376  1.000 74.440  ? 132 ASN FFF CG  1 
ATOM 10915 O OD1 . ASN F 2 132 ? 79.976  -57.924 -4.511  1.000 69.310  ? 132 ASN FFF OD1 1 
ATOM 10916 N ND2 . ASN F 2 132 ? 80.516  -58.222 -6.661  1.000 61.020  ? 132 ASN FFF ND2 1 
ATOM 10917 N N   . LYS F 2 133 ? 83.001  -58.220 -2.121  1.000 86.470  ? 133 LYS FFF N   1 
ATOM 10918 C CA  . LYS F 2 133 ? 83.214  -57.887 -0.685  1.000 86.910  ? 133 LYS FFF CA  1 
ATOM 10919 C C   . LYS F 2 133 ? 82.496  -56.567 -0.377  1.000 91.610  ? 133 LYS FFF C   1 
ATOM 10920 O O   . LYS F 2 133 ? 81.996  -55.914 -1.332  1.000 87.460  ? 133 LYS FFF O   1 
ATOM 10921 C CB  . LYS F 2 133 ? 84.712  -57.769 -0.385  1.000 73.010  ? 133 LYS FFF CB  1 
ATOM 10922 N N   . ALA F 2 134 ? 82.469  -56.171 0.898   1.000 94.360  ? 134 ALA FFF N   1 
ATOM 10923 C CA  . ALA F 2 134 ? 81.552  -55.127 1.423   1.000 103.880 ? 134 ALA FFF CA  1 
ATOM 10924 C C   . ALA F 2 134 ? 82.232  -54.216 2.456   1.000 103.330 ? 134 ALA FFF C   1 
ATOM 10925 O O   . ALA F 2 134 ? 82.281  -54.608 3.647   1.000 97.010  ? 134 ALA FFF O   1 
ATOM 10926 C CB  . ALA F 2 134 ? 80.342  -55.807 2.017   1.000 105.250 ? 134 ALA FFF CB  1 
ATOM 10927 N N   . THR F 2 135 ? 82.664  -53.019 2.031   1.000 98.980  ? 135 THR FFF N   1 
ATOM 10928 C CA  . THR F 2 135 ? 83.268  -51.963 2.897   1.000 105.150 ? 135 THR FFF CA  1 
ATOM 10929 C C   . THR F 2 135 ? 82.238  -50.856 3.175   1.000 96.770  ? 135 THR FFF C   1 
ATOM 10930 O O   . THR F 2 135 ? 81.496  -50.506 2.248   1.000 97.110  ? 135 THR FFF O   1 
ATOM 10931 C CB  . THR F 2 135 ? 84.546  -51.405 2.251   1.000 116.880 ? 135 THR FFF CB  1 
ATOM 10932 O OG1 . THR F 2 135 ? 85.300  -52.512 1.751   1.000 117.470 ? 135 THR FFF OG1 1 
ATOM 10933 C CG2 . THR F 2 135 ? 85.409  -50.590 3.193   1.000 117.860 ? 135 THR FFF CG2 1 
ATOM 10934 N N   . LEU F 2 136 ? 82.269  -50.254 4.378   1.000 92.690  ? 136 LEU FFF N   1 
ATOM 10935 C CA  . LEU F 2 136 ? 81.392  -49.117 4.802   1.000 87.770  ? 136 LEU FFF CA  1 
ATOM 10936 C C   . LEU F 2 136 ? 82.252  -47.891 5.155   1.000 85.380  ? 136 LEU FFF C   1 
ATOM 10937 O O   . LEU F 2 136 ? 83.359  -48.081 5.716   1.000 98.600  ? 136 LEU FFF O   1 
ATOM 10938 C CB  . LEU F 2 136 ? 80.534  -49.532 6.012   1.000 86.120  ? 136 LEU FFF CB  1 
ATOM 10939 C CG  . LEU F 2 136 ? 79.095  -49.932 5.733   1.000 81.150  ? 136 LEU FFF CG  1 
ATOM 10940 C CD1 . LEU F 2 136 ? 78.980  -51.418 5.430   1.000 75.560  ? 136 LEU FFF CD1 1 
ATOM 10941 C CD2 . LEU F 2 136 ? 78.203  -49.571 6.917   1.000 80.800  ? 136 LEU FFF CD2 1 
ATOM 10942 N N   . VAL F 2 137 ? 81.737  -46.685 4.878   1.000 72.940  ? 137 VAL FFF N   1 
ATOM 10943 C CA  . VAL F 2 137 ? 82.471  -45.380 4.959   1.000 72.380  ? 137 VAL FFF CA  1 
ATOM 10944 C C   . VAL F 2 137 ? 81.667  -44.420 5.849   1.000 76.230  ? 137 VAL FFF C   1 
ATOM 10945 O O   . VAL F 2 137 ? 80.471  -44.299 5.624   1.000 91.510  ? 137 VAL FFF O   1 
ATOM 10946 C CB  . VAL F 2 137 ? 82.695  -44.772 3.562   1.000 65.790  ? 137 VAL FFF CB  1 
ATOM 10947 C CG1 . VAL F 2 137 ? 83.125  -43.314 3.622   1.000 64.620  ? 137 VAL FFF CG1 1 
ATOM 10948 C CG2 . VAL F 2 137 ? 83.690  -45.579 2.744   1.000 68.440  ? 137 VAL FFF CG2 1 
ATOM 10949 N N   . CYS F 2 138 ? 82.328  -43.758 6.805   1.000 79.490  ? 138 CYS FFF N   1 
ATOM 10950 C CA  . CYS F 2 138 ? 81.705  -42.835 7.796   1.000 83.330  ? 138 CYS FFF CA  1 
ATOM 10951 C C   . CYS F 2 138 ? 82.576  -41.578 7.908   1.000 90.080  ? 138 CYS FFF C   1 
ATOM 10952 O O   . CYS F 2 138 ? 83.393  -41.497 8.852   1.000 101.920 ? 138 CYS FFF O   1 
ATOM 10953 C CB  . CYS F 2 138 ? 81.525  -43.530 9.144   1.000 84.230  ? 138 CYS FFF CB  1 
ATOM 10954 S SG  . CYS F 2 138 ? 80.707  -42.533 10.424  1.000 83.450  ? 138 CYS FFF SG  1 
ATOM 10955 N N   . LEU F 2 139 ? 82.414  -40.649 6.958   1.000 83.170  ? 139 LEU FFF N   1 
ATOM 10956 C CA  . LEU F 2 139 ? 83.243  -39.417 6.838   1.000 81.700  ? 139 LEU FFF CA  1 
ATOM 10957 C C   . LEU F 2 139 ? 82.762  -38.371 7.849   1.000 84.790  ? 139 LEU FFF C   1 
ATOM 10958 O O   . LEU F 2 139 ? 81.562  -38.092 7.869   1.000 103.030 ? 139 LEU FFF O   1 
ATOM 10959 C CB  . LEU F 2 139 ? 83.166  -38.899 5.403   1.000 75.800  ? 139 LEU FFF CB  1 
ATOM 10960 C CG  . LEU F 2 139 ? 83.479  -39.951 4.346   1.000 73.610  ? 139 LEU FFF CG  1 
ATOM 10961 C CD1 . LEU F 2 139 ? 83.274  -39.395 2.957   1.000 73.100  ? 139 LEU FFF CD1 1 
ATOM 10962 C CD2 . LEU F 2 139 ? 84.892  -40.483 4.509   1.000 72.360  ? 139 LEU FFF CD2 1 
ATOM 10963 N N   . ILE F 2 140 ? 83.673  -37.849 8.674   1.000 82.730  ? 140 ILE FFF N   1 
ATOM 10964 C CA  . ILE F 2 140 ? 83.408  -36.885 9.782   1.000 82.600  ? 140 ILE FFF CA  1 
ATOM 10965 C C   . ILE F 2 140 ? 84.275  -35.657 9.489   1.000 91.040  ? 140 ILE FFF C   1 
ATOM 10966 O O   . ILE F 2 140 ? 85.432  -35.904 9.131   1.000 103.710 ? 140 ILE FFF O   1 
ATOM 10967 C CB  . ILE F 2 140 ? 83.737  -37.534 11.146  1.000 83.160  ? 140 ILE FFF CB  1 
ATOM 10968 C CG1 . ILE F 2 140 ? 83.461  -39.041 11.144  1.000 84.770  ? 140 ILE FFF CG1 1 
ATOM 10969 C CG2 . ILE F 2 140 ? 83.001  -36.834 12.274  1.000 90.940  ? 140 ILE FFF CG2 1 
ATOM 10970 C CD1 . ILE F 2 140 ? 84.017  -39.765 12.348  1.000 88.530  ? 140 ILE FFF CD1 1 
ATOM 10971 N N   . SER F 2 141 ? 83.758  -34.414 9.583   1.000 98.440  ? 141 SER FFF N   1 
ATOM 10972 C CA  . SER F 2 141 ? 84.532  -33.161 9.303   1.000 96.950  ? 141 SER FFF CA  1 
ATOM 10973 C C   . SER F 2 141 ? 84.125  -31.963 10.190  1.000 97.480  ? 141 SER FFF C   1 
ATOM 10974 O O   . SER F 2 141 ? 83.085  -32.034 10.868  1.000 88.200  ? 141 SER FFF O   1 
ATOM 10975 C CB  . SER F 2 141 ? 84.507  -32.793 7.822   1.000 93.210  ? 141 SER FFF CB  1 
ATOM 10976 O OG  . SER F 2 141 ? 83.282  -32.199 7.443   1.000 98.650  ? 141 SER FFF OG  1 
ATOM 10977 N N   . ASP F 2 142 ? 84.981  -30.926 10.174  1.000 104.210 ? 142 ASP FFF N   1 
ATOM 10978 C CA  . ASP F 2 142 ? 84.839  -29.585 10.812  1.000 97.010  ? 142 ASP FFF CA  1 
ATOM 10979 C C   . ASP F 2 142 ? 84.565  -29.702 12.314  1.000 97.670  ? 142 ASP FFF C   1 
ATOM 10980 O O   . ASP F 2 142 ? 83.434  -29.423 12.712  1.000 105.860 ? 142 ASP FFF O   1 
ATOM 10981 C CB  . ASP F 2 142 ? 83.762  -28.762 10.105  1.000 86.860  ? 142 ASP FFF CB  1 
ATOM 10982 C CG  . ASP F 2 142 ? 84.177  -28.332 8.711   1.000 81.520  ? 142 ASP FFF CG  1 
ATOM 10983 O OD1 . ASP F 2 142 ? 85.243  -27.715 8.591   1.000 88.020  ? 142 ASP FFF OD1 1 
ATOM 10984 O OD2 . ASP F 2 142 ? 83.443  -28.628 7.763   1.000 68.850  ? 142 ASP FFF OD2 1 
ATOM 10985 N N   . PHE F 2 143 ? 85.582  -30.046 13.113  1.000 100.940 ? 143 PHE FFF N   1 
ATOM 10986 C CA  . PHE F 2 143 ? 85.535  -30.103 14.603  1.000 109.540 ? 143 PHE FFF CA  1 
ATOM 10987 C C   . PHE F 2 143 ? 86.688  -29.266 15.204  1.000 125.850 ? 143 PHE FFF C   1 
ATOM 10988 O O   . PHE F 2 143 ? 87.790  -29.830 15.316  1.000 160.530 ? 143 PHE FFF O   1 
ATOM 10989 C CB  . PHE F 2 143 ? 85.568  -31.573 15.044  1.000 106.330 ? 143 PHE FFF CB  1 
ATOM 10990 N N   . TYR F 2 144 ? 86.447  -27.993 15.588  1.000 124.270 ? 144 TYR FFF N   1 
ATOM 10991 C CA  . TYR F 2 144 ? 87.470  -26.975 16.000  1.000 111.880 ? 144 TYR FFF CA  1 
ATOM 10992 C C   . TYR F 2 144 ? 87.898  -27.128 17.463  1.000 105.520 ? 144 TYR FFF C   1 
ATOM 10993 O O   . TYR F 2 144 ? 88.792  -26.403 17.924  1.000 84.840  ? 144 TYR FFF O   1 
ATOM 10994 C CB  . TYR F 2 144 ? 86.962  -25.548 15.745  1.000 107.460 ? 144 TYR FFF CB  1 
ATOM 10995 N N   . PRO F 2 145 ? 87.243  -28.004 18.266  1.000 113.940 ? 145 PRO FFF N   1 
ATOM 10996 C CA  . PRO F 2 145 ? 87.864  -28.586 19.458  1.000 114.090 ? 145 PRO FFF CA  1 
ATOM 10997 C C   . PRO F 2 145 ? 88.874  -29.723 19.226  1.000 112.870 ? 145 PRO FFF C   1 
ATOM 10998 O O   . PRO F 2 145 ? 89.519  -30.055 20.185  1.000 114.820 ? 145 PRO FFF O   1 
ATOM 10999 C CB  . PRO F 2 145 ? 86.697  -29.207 20.243  1.000 118.010 ? 145 PRO FFF CB  1 
ATOM 11000 C CG  . PRO F 2 145 ? 85.447  -28.625 19.619  1.000 124.130 ? 145 PRO FFF CG  1 
ATOM 11001 C CD  . PRO F 2 145 ? 85.818  -28.364 18.174  1.000 118.430 ? 145 PRO FFF CD  1 
ATOM 11002 N N   . GLY F 2 146 ? 88.929  -30.335 18.033  1.000 108.030 ? 146 GLY FFF N   1 
ATOM 11003 C CA  . GLY F 2 146 ? 89.998  -31.275 17.624  1.000 100.300 ? 146 GLY FFF CA  1 
ATOM 11004 C C   . GLY F 2 146 ? 89.513  -32.705 17.397  1.000 99.190  ? 146 GLY FFF C   1 
ATOM 11005 O O   . GLY F 2 146 ? 88.876  -32.948 16.361  1.000 120.600 ? 146 GLY FFF O   1 
ATOM 11006 N N   . ALA F 2 147 ? 89.877  -33.634 18.292  1.000 94.360  ? 147 ALA FFF N   1 
ATOM 11007 C CA  . ALA F 2 147 ? 89.750  -35.107 18.140  1.000 97.930  ? 147 ALA FFF CA  1 
ATOM 11008 C C   . ALA F 2 147 ? 88.363  -35.607 18.594  1.000 95.730  ? 147 ALA FFF C   1 
ATOM 11009 O O   . ALA F 2 147 ? 87.641  -34.861 19.271  1.000 89.290  ? 147 ALA FFF O   1 
ATOM 11010 C CB  . ALA F 2 147 ? 90.869  -35.790 18.904  1.000 100.440 ? 147 ALA FFF CB  1 
ATOM 11011 N N   . VAL F 2 148 ? 87.997  -36.838 18.209  1.000 97.740  ? 148 VAL FFF N   1 
ATOM 11012 C CA  . VAL F 2 148 ? 86.634  -37.433 18.381  1.000 92.850  ? 148 VAL FFF CA  1 
ATOM 11013 C C   . VAL F 2 148 ? 86.768  -38.944 18.672  1.000 84.250  ? 148 VAL FFF C   1 
ATOM 11014 O O   . VAL F 2 148 ? 87.909  -39.434 18.819  1.000 79.930  ? 148 VAL FFF O   1 
ATOM 11015 C CB  . VAL F 2 148 ? 85.744  -37.130 17.154  1.000 106.760 ? 148 VAL FFF CB  1 
ATOM 11016 C CG1 . VAL F 2 148 ? 85.819  -35.668 16.711  1.000 114.310 ? 148 VAL FFF CG1 1 
ATOM 11017 C CG2 . VAL F 2 148 ? 86.043  -38.030 15.962  1.000 112.350 ? 148 VAL FFF CG2 1 
ATOM 11018 N N   . THR F 2 149 ? 85.642  -39.658 18.788  1.000 79.670  ? 149 THR FFF N   1 
ATOM 11019 C CA  . THR F 2 149 ? 85.552  -41.124 19.078  1.000 79.820  ? 149 THR FFF CA  1 
ATOM 11020 C C   . THR F 2 149 ? 84.745  -41.783 17.957  1.000 80.600  ? 149 THR FFF C   1 
ATOM 11021 O O   . THR F 2 149 ? 84.272  -41.028 17.105  1.000 89.790  ? 149 THR FFF O   1 
ATOM 11022 C CB  . THR F 2 149 ? 84.888  -41.401 20.435  1.000 79.720  ? 149 THR FFF CB  1 
ATOM 11023 O OG1 . THR F 2 149 ? 85.392  -40.455 21.381  1.000 81.910  ? 149 THR FFF OG1 1 
ATOM 11024 C CG2 . THR F 2 149 ? 85.107  -42.815 20.934  1.000 74.680  ? 149 THR FFF CG2 1 
ATOM 11025 N N   . VAL F 2 150 ? 84.595  -43.112 17.944  1.000 79.000  ? 150 VAL FFF N   1 
ATOM 11026 C CA  . VAL F 2 150 ? 83.747  -43.836 16.956  1.000 79.520  ? 150 VAL FFF CA  1 
ATOM 11027 C C   . VAL F 2 150 ? 83.320  -45.206 17.507  1.000 90.020  ? 150 VAL FFF C   1 
ATOM 11028 O O   . VAL F 2 150 ? 84.130  -45.850 18.204  1.000 97.080  ? 150 VAL FFF O   1 
ATOM 11029 C CB  . VAL F 2 150 ? 84.472  -44.023 15.615  1.000 79.170  ? 150 VAL FFF CB  1 
ATOM 11030 C CG1 . VAL F 2 150 ? 84.455  -42.765 14.759  1.000 74.920  ? 150 VAL FFF CG1 1 
ATOM 11031 C CG2 . VAL F 2 150 ? 85.895  -44.527 15.837  1.000 83.530  ? 150 VAL FFF CG2 1 
ATOM 11032 N N   . ALA F 2 151 ? 82.119  -45.647 17.150  1.000 92.690  ? 151 ALA FFF N   1 
ATOM 11033 C CA  . ALA F 2 151 ? 81.541  -46.972 17.486  1.000 90.960  ? 151 ALA FFF CA  1 
ATOM 11034 C C   . ALA F 2 151 ? 80.586  -47.366 16.369  1.000 91.500  ? 151 ALA FFF C   1 
ATOM 11035 O O   . ALA F 2 151 ? 80.329  -46.510 15.501  1.000 95.180  ? 151 ALA FFF O   1 
ATOM 11036 C CB  . ALA F 2 151 ? 80.855  -46.931 18.835  1.000 85.340  ? 151 ALA FFF CB  1 
ATOM 11037 N N   . TRP F 2 152 ? 80.086  -48.606 16.392  1.000 94.120  ? 152 TRP FFF N   1 
ATOM 11038 C CA  . TRP F 2 152 ? 79.224  -49.200 15.331  1.000 91.390  ? 152 TRP FFF CA  1 
ATOM 11039 C C   . TRP F 2 152 ? 78.254  -50.208 15.975  1.000 79.230  ? 152 TRP FFF C   1 
ATOM 11040 O O   . TRP F 2 152 ? 77.049  -50.215 15.604  1.000 60.870  ? 152 TRP FFF O   1 
ATOM 11041 C CB  . TRP F 2 152 ? 80.089  -49.862 14.237  1.000 95.120  ? 152 TRP FFF CB  1 
ATOM 11042 C CG  . TRP F 2 152 ? 81.089  -49.004 13.501  1.000 99.220  ? 152 TRP FFF CG  1 
ATOM 11043 C CD1 . TRP F 2 152 ? 82.320  -48.603 13.945  1.000 97.420  ? 152 TRP FFF CD1 1 
ATOM 11044 C CD2 . TRP F 2 152 ? 81.001  -48.530 12.138  1.000 97.130  ? 152 TRP FFF CD2 1 
ATOM 11045 N NE1 . TRP F 2 152 ? 82.980  -47.889 12.978  1.000 89.660  ? 152 TRP FFF NE1 1 
ATOM 11046 C CE2 . TRP F 2 152 ? 82.197  -47.829 11.859  1.000 88.680  ? 152 TRP FFF CE2 1 
ATOM 11047 C CE3 . TRP F 2 152 ? 80.020  -48.603 11.137  1.000 96.860  ? 152 TRP FFF CE3 1 
ATOM 11048 C CZ2 . TRP F 2 152 ? 82.431  -47.214 10.631  1.000 87.820  ? 152 TRP FFF CZ2 1 
ATOM 11049 C CZ3 . TRP F 2 152 ? 80.255  -48.000 9.919   1.000 93.930  ? 152 TRP FFF CZ3 1 
ATOM 11050 C CH2 . TRP F 2 152 ? 81.446  -47.315 9.674   1.000 93.100  ? 152 TRP FFF CH2 1 
ATOM 11051 N N   . ALA F 2 161 ? 85.364  -54.817 15.228  1.000 89.850  ? 161 ALA FFF N   1 
ATOM 11052 C CA  . ALA F 2 161 ? 85.524  -55.994 14.340  1.000 80.340  ? 161 ALA FFF CA  1 
ATOM 11053 C C   . ALA F 2 161 ? 85.466  -55.558 12.878  1.000 77.190  ? 161 ALA FFF C   1 
ATOM 11054 O O   . ALA F 2 161 ? 84.385  -55.647 12.283  1.000 68.310  ? 161 ALA FFF O   1 
ATOM 11055 C CB  . ALA F 2 161 ? 84.474  -57.023 14.648  1.000 30.000  ? 161 ALA FFF CB  1 
ATOM 11056 N N   . GLY F 2 162 ? 86.601  -55.142 12.322  1.000 80.450  ? 162 GLY FFF N   1 
ATOM 11057 C CA  . GLY F 2 162 ? 86.631  -54.617 10.945  1.000 81.340  ? 162 GLY FFF CA  1 
ATOM 11058 C C   . GLY F 2 162 ? 86.772  -53.115 11.002  1.000 81.630  ? 162 GLY FFF C   1 
ATOM 11059 O O   . GLY F 2 162 ? 86.838  -52.485 9.940   1.000 74.730  ? 162 GLY FFF O   1 
ATOM 11060 N N   . VAL F 2 163 ? 86.857  -52.575 12.215  1.000 79.820  ? 163 VAL FFF N   1 
ATOM 11061 C CA  . VAL F 2 163 ? 86.900  -51.100 12.388  1.000 82.120  ? 163 VAL FFF CA  1 
ATOM 11062 C C   . VAL F 2 163 ? 88.309  -50.577 12.111  1.000 80.180  ? 163 VAL FFF C   1 
ATOM 11063 O O   . VAL F 2 163 ? 89.280  -51.233 12.516  1.000 82.740  ? 163 VAL FFF O   1 
ATOM 11064 C CB  . VAL F 2 163 ? 86.371  -50.706 13.777  1.000 85.910  ? 163 VAL FFF CB  1 
ATOM 11065 C CG1 . VAL F 2 163 ? 84.885  -50.990 13.886  1.000 87.020  ? 163 VAL FFF CG1 1 
ATOM 11066 C CG2 . VAL F 2 163 ? 87.113  -51.416 14.898  1.000 82.910  ? 163 VAL FFF CG2 1 
ATOM 11067 N N   . GLU F 2 164 ? 88.401  -49.444 11.417  1.000 75.640  ? 164 GLU FFF N   1 
ATOM 11068 C CA  . GLU F 2 164 ? 89.705  -48.838 11.072  1.000 76.320  ? 164 GLU FFF CA  1 
ATOM 11069 C C   . GLU F 2 164 ? 89.494  -47.327 11.069  1.000 78.150  ? 164 GLU FFF C   1 
ATOM 11070 O O   . GLU F 2 164 ? 88.932  -46.830 10.088  1.000 80.690  ? 164 GLU FFF O   1 
ATOM 11071 C CB  . GLU F 2 164 ? 90.167  -49.365 9.720   1.000 79.310  ? 164 GLU FFF CB  1 
ATOM 11072 C CG  . GLU F 2 164 ? 91.603  -49.846 9.732   1.000 86.140  ? 164 GLU FFF CG  1 
ATOM 11073 C CD  . GLU F 2 164 ? 91.803  -51.293 10.147  1.000 95.480  ? 164 GLU FFF CD  1 
ATOM 11074 O OE1 . GLU F 2 164 ? 91.190  -52.177 9.520   1.000 99.400  ? 164 GLU FFF OE1 1 
ATOM 11075 O OE2 . GLU F 2 164 ? 92.581  -51.532 11.090  1.000 87.990  ? 164 GLU FFF OE2 1 
ATOM 11076 N N   . THR F 2 165 ? 89.939  -46.632 12.115  1.000 82.610  ? 165 THR FFF N   1 
ATOM 11077 C CA  . THR F 2 165 ? 89.675  -45.171 12.282  1.000 83.380  ? 165 THR FFF CA  1 
ATOM 11078 C C   . THR F 2 165 ? 90.976  -44.361 12.104  1.000 82.910  ? 165 THR FFF C   1 
ATOM 11079 O O   . THR F 2 165 ? 92.037  -44.834 12.544  1.000 94.880  ? 165 THR FFF O   1 
ATOM 11080 C CB  . THR F 2 165 ? 89.016  -44.907 13.647  1.000 79.540  ? 165 THR FFF CB  1 
ATOM 11081 O OG1 . THR F 2 165 ? 87.997  -45.883 13.874  1.000 70.150  ? 165 THR FFF OG1 1 
ATOM 11082 C CG2 . THR F 2 165 ? 88.421  -43.520 13.766  1.000 76.390  ? 165 THR FFF CG2 1 
ATOM 11083 N N   . THR F 2 166 ? 90.877  -43.154 11.535  1.000 79.010  ? 166 THR FFF N   1 
ATOM 11084 C CA  . THR F 2 166 ? 91.996  -42.228 11.199  1.000 79.150  ? 166 THR FFF CA  1 
ATOM 11085 C C   . THR F 2 166 ? 92.363  -41.338 12.398  1.000 77.250  ? 166 THR FFF C   1 
ATOM 11086 O O   . THR F 2 166 ? 91.483  -41.067 13.223  1.000 79.640  ? 166 THR FFF O   1 
ATOM 11087 C CB  . THR F 2 166 ? 91.594  -41.351 10.005  1.000 81.630  ? 166 THR FFF CB  1 
ATOM 11088 O OG1 . THR F 2 166 ? 91.289  -42.206 8.901   1.000 77.390  ? 166 THR FFF OG1 1 
ATOM 11089 C CG2 . THR F 2 166 ? 92.651  -40.352 9.592   1.000 85.950  ? 166 THR FFF CG2 1 
ATOM 11090 N N   . LYS F 2 167 ? 93.627  -40.913 12.495  1.000 77.200  ? 167 LYS FFF N   1 
ATOM 11091 C CA  . LYS F 2 167 ? 94.069  -39.815 13.397  1.000 70.870  ? 167 LYS FFF CA  1 
ATOM 11092 C C   . LYS F 2 167 ? 93.476  -38.523 12.839  1.000 80.240  ? 167 LYS FFF C   1 
ATOM 11093 O O   . LYS F 2 167 ? 93.493  -38.311 11.626  1.000 82.840  ? 167 LYS FFF O   1 
ATOM 11094 C CB  . LYS F 2 167 ? 95.596  -39.744 13.505  1.000 57.130  ? 167 LYS FFF CB  1 
ATOM 11095 N N   . PRO F 2 168 ? 92.845  -37.675 13.685  1.000 87.430  ? 168 PRO FFF N   1 
ATOM 11096 C CA  . PRO F 2 168 ? 92.254  -36.413 13.223  1.000 88.980  ? 168 PRO FFF CA  1 
ATOM 11097 C C   . PRO F 2 168 ? 93.196  -35.474 12.447  1.000 81.340  ? 168 PRO FFF C   1 
ATOM 11098 O O   . PRO F 2 168 ? 94.288  -35.267 12.914  1.000 78.800  ? 168 PRO FFF O   1 
ATOM 11099 C CB  . PRO F 2 168 ? 91.771  -35.773 14.540  1.000 93.590  ? 168 PRO FFF CB  1 
ATOM 11100 C CG  . PRO F 2 168 ? 91.501  -36.946 15.462  1.000 87.060  ? 168 PRO FFF CG  1 
ATOM 11101 C CD  . PRO F 2 168 ? 92.577  -37.945 15.110  1.000 86.450  ? 168 PRO FFF CD  1 
ATOM 11102 N N   . SER F 2 169 ? 92.760  -34.941 11.299  1.000 76.890  ? 169 SER FFF N   1 
ATOM 11103 C CA  . SER F 2 169 ? 93.553  -34.045 10.405  1.000 80.660  ? 169 SER FFF CA  1 
ATOM 11104 C C   . SER F 2 169 ? 92.997  -32.618 10.355  1.000 77.250  ? 169 SER FFF C   1 
ATOM 11105 O O   . SER F 2 169 ? 91.816  -32.488 10.021  1.000 90.510  ? 169 SER FFF O   1 
ATOM 11106 C CB  . SER F 2 169 ? 93.585  -34.617 8.992   1.000 80.980  ? 169 SER FFF CB  1 
ATOM 11107 O OG  . SER F 2 169 ? 92.291  -34.642 8.401   1.000 79.080  ? 169 SER FFF OG  1 
ATOM 11108 N N   . LYS F 2 170 ? 93.788  -31.578 10.652  1.000 74.940  ? 170 LYS FFF N   1 
ATOM 11109 C CA  . LYS F 2 170 ? 93.352  -30.157 10.490  1.000 74.590  ? 170 LYS FFF CA  1 
ATOM 11110 C C   . LYS F 2 170 ? 92.893  -30.043 9.029   1.000 82.070  ? 170 LYS FFF C   1 
ATOM 11111 O O   . LYS F 2 170 ? 93.621  -30.519 8.150   1.000 83.740  ? 170 LYS FFF O   1 
ATOM 11112 C CB  . LYS F 2 170 ? 94.423  -29.110 10.838  1.000 58.290  ? 170 LYS FFF CB  1 
ATOM 11113 N N   . GLN F 2 171 ? 91.683  -29.531 8.790   1.000 93.880  ? 171 GLN FFF N   1 
ATOM 11114 C CA  . GLN F 2 171 ? 91.209  -29.060 7.456   1.000 94.590  ? 171 GLN FFF CA  1 
ATOM 11115 C C   . GLN F 2 171 ? 91.769  -27.643 7.241   1.000 94.230  ? 171 GLN FFF C   1 
ATOM 11116 O O   . GLN F 2 171 ? 92.194  -27.020 8.240   1.000 94.690  ? 171 GLN FFF O   1 
ATOM 11117 C CB  . GLN F 2 171 ? 89.679  -29.134 7.367   1.000 92.560  ? 171 GLN FFF CB  1 
ATOM 11118 N N   . SER F 2 172 ? 91.773  -27.165 5.992   1.000 89.580  ? 172 SER FFF N   1 
ATOM 11119 C CA  . SER F 2 172 ? 92.473  -25.926 5.538   1.000 87.860  ? 172 SER FFF CA  1 
ATOM 11120 C C   . SER F 2 172 ? 91.795  -24.670 6.122   1.000 87.390  ? 172 SER FFF C   1 
ATOM 11121 O O   . SER F 2 172 ? 92.378  -23.578 5.996   1.000 91.320  ? 172 SER FFF O   1 
ATOM 11122 C CB  . SER F 2 172 ? 92.510  -25.869 4.035   1.000 88.300  ? 172 SER FFF CB  1 
ATOM 11123 O OG  . SER F 2 172 ? 91.192  -25.807 3.506   1.000 90.970  ? 172 SER FFF OG  1 
ATOM 11124 N N   . ASN F 2 173 ? 90.614  -24.815 6.723   1.000 88.040  ? 173 ASN FFF N   1 
ATOM 11125 C CA  . ASN F 2 173 ? 89.879  -23.732 7.430   1.000 89.540  ? 173 ASN FFF CA  1 
ATOM 11126 C C   . ASN F 2 173 ? 90.209  -23.804 8.930   1.000 92.970  ? 173 ASN FFF C   1 
ATOM 11127 O O   . ASN F 2 173 ? 89.428  -23.264 9.728   1.000 114.010 ? 173 ASN FFF O   1 
ATOM 11128 C CB  . ASN F 2 173 ? 88.375  -23.831 7.145   1.000 82.650  ? 173 ASN FFF CB  1 
ATOM 11129 C CG  . ASN F 2 173 ? 87.820  -25.199 7.474   1.000 75.980  ? 173 ASN FFF CG  1 
ATOM 11130 O OD1 . ASN F 2 173 ? 87.940  -25.666 8.596   1.000 72.290  ? 173 ASN FFF OD1 1 
ATOM 11131 N ND2 . ASN F 2 173 ? 87.259  -25.873 6.486   1.000 75.970  ? 173 ASN FFF ND2 1 
ATOM 11132 N N   . ASN F 2 174 ? 91.341  -24.415 9.287   1.000 89.620  ? 174 ASN FFF N   1 
ATOM 11133 C CA  . ASN F 2 174 ? 91.681  -24.890 10.659  1.000 97.730  ? 174 ASN FFF CA  1 
ATOM 11134 C C   . ASN F 2 174 ? 90.403  -25.302 11.420  1.000 90.030  ? 174 ASN FFF C   1 
ATOM 11135 O O   . ASN F 2 174 ? 90.089  -24.680 12.439  1.000 84.770  ? 174 ASN FFF O   1 
ATOM 11136 C CB  . ASN F 2 174 ? 92.605  -23.918 11.412  1.000 94.320  ? 174 ASN FFF CB  1 
ATOM 11137 C CG  . ASN F 2 174 ? 92.278  -22.452 11.252  1.000 93.520  ? 174 ASN FFF CG  1 
ATOM 11138 O OD1 . ASN F 2 174 ? 92.055  -21.970 10.141  1.000 98.050  ? 174 ASN FFF OD1 1 
ATOM 11139 N ND2 . ASN F 2 174 ? 92.289  -21.737 12.364  1.000 86.540  ? 174 ASN FFF ND2 1 
ATOM 11140 N N   . LYS F 2 175 ? 89.694  -26.318 10.912  1.000 94.180  ? 175 LYS FFF N   1 
ATOM 11141 C CA  . LYS F 2 175 ? 88.752  -27.205 11.661  1.000 100.740 ? 175 LYS FFF CA  1 
ATOM 11142 C C   . LYS F 2 175 ? 89.050  -28.650 11.210  1.000 110.040 ? 175 LYS FFF C   1 
ATOM 11143 O O   . LYS F 2 175 ? 89.445  -28.838 10.048  1.000 135.650 ? 175 LYS FFF O   1 
ATOM 11144 C CB  . LYS F 2 175 ? 87.295  -26.778 11.442  1.000 90.080  ? 175 LYS FFF CB  1 
ATOM 11145 N N   . THR F 2 176 ? 88.930  -29.640 12.098  1.000 108.350 ? 176 THR FFF N   1 
ATOM 11146 C CA  . THR F 2 176 ? 89.662  -30.938 12.007  1.000 107.050 ? 176 THR FFF CA  1 
ATOM 11147 C C   . THR F 2 176 ? 88.718  -32.088 11.580  1.000 109.550 ? 176 THR FFF C   1 
ATOM 11148 O O   . THR F 2 176 ? 87.649  -32.324 12.228  1.000 115.560 ? 176 THR FFF O   1 
ATOM 11149 C CB  . THR F 2 176 ? 90.469  -31.168 13.301  1.000 103.260 ? 176 THR FFF CB  1 
ATOM 11150 O OG1 . THR F 2 176 ? 91.547  -30.231 13.391  1.000 85.610  ? 176 THR FFF OG1 1 
ATOM 11151 C CG2 . THR F 2 176 ? 91.065  -32.554 13.405  1.000 101.070 ? 176 THR FFF CG2 1 
ATOM 11152 N N   . ALA F 2 177 ? 89.167  -32.813 10.545  1.000 105.310 ? 177 ALA FFF N   1 
ATOM 11153 C CA  . ALA F 2 177 ? 88.497  -33.933 9.843   1.000 96.090  ? 177 ALA FFF CA  1 
ATOM 11154 C C   . ALA F 2 177 ? 89.153  -35.303 10.147  1.000 85.340  ? 177 ALA FFF C   1 
ATOM 11155 O O   . ALA F 2 177 ? 90.386  -35.367 10.340  1.000 83.220  ? 177 ALA FFF O   1 
ATOM 11156 C CB  . ALA F 2 177 ? 88.528  -33.620 8.363   1.000 89.110  ? 177 ALA FFF CB  1 
ATOM 11157 N N   . ALA F 2 178 ? 88.348  -36.374 10.160  1.000 81.120  ? 178 ALA FFF N   1 
ATOM 11158 C CA  . ALA F 2 178 ? 88.778  -37.799 10.227  1.000 85.710  ? 178 ALA FFF CA  1 
ATOM 11159 C C   . ALA F 2 178 ? 87.910  -38.657 9.291   1.000 82.700  ? 178 ALA FFF C   1 
ATOM 11160 O O   . ALA F 2 178 ? 87.013  -38.096 8.652   1.000 99.140  ? 178 ALA FFF O   1 
ATOM 11161 C CB  . ALA F 2 178 ? 88.696  -38.306 11.649  1.000 85.280  ? 178 ALA FFF CB  1 
ATOM 11162 N N   . SER F 2 179 ? 88.165  -39.969 9.215   1.000 70.280  ? 179 SER FFF N   1 
ATOM 11163 C CA  . SER F 2 179 ? 87.334  -40.973 8.486   1.000 69.170  ? 179 SER FFF CA  1 
ATOM 11164 C C   . SER F 2 179 ? 87.428  -42.323 9.213   1.000 69.560  ? 179 SER FFF C   1 
ATOM 11165 O O   . SER F 2 179 ? 88.476  -42.576 9.812   1.000 72.360  ? 179 SER FFF O   1 
ATOM 11166 C CB  . SER F 2 179 ? 87.717  -41.084 7.012   1.000 68.930  ? 179 SER FFF CB  1 
ATOM 11167 O OG  . SER F 2 179 ? 89.113  -40.863 6.783   1.000 74.460  ? 179 SER FFF OG  1 
ATOM 11168 N N   . SER F 2 180 ? 86.376  -43.148 9.195   1.000 67.920  ? 180 SER FFF N   1 
ATOM 11169 C CA  . SER F 2 180 ? 86.356  -44.505 9.814   1.000 67.430  ? 180 SER FFF CA  1 
ATOM 11170 C C   . SER F 2 180 ? 85.699  -45.510 8.857   1.000 70.810  ? 180 SER FFF C   1 
ATOM 11171 O O   . SER F 2 180 ? 84.683  -45.131 8.220   1.000 81.020  ? 180 SER FFF O   1 
ATOM 11172 C CB  . SER F 2 180 ? 85.649  -44.473 11.137  1.000 66.880  ? 180 SER FFF CB  1 
ATOM 11173 O OG  . SER F 2 180 ? 85.490  -45.788 11.651  1.000 70.570  ? 180 SER FFF OG  1 
ATOM 11174 N N   . TYR F 2 181 ? 86.241  -46.734 8.765   1.000 65.860  ? 181 TYR FFF N   1 
ATOM 11175 C CA  . TYR F 2 181 ? 85.825  -47.780 7.789   1.000 68.990  ? 181 TYR FFF CA  1 
ATOM 11176 C C   . TYR F 2 181 ? 85.515  -49.070 8.551   1.000 71.730  ? 181 TYR FFF C   1 
ATOM 11177 O O   . TYR F 2 181 ? 86.196  -49.349 9.558   1.000 73.240  ? 181 TYR FFF O   1 
ATOM 11178 C CB  . TYR F 2 181 ? 86.902  -48.021 6.720   1.000 69.830  ? 181 TYR FFF CB  1 
ATOM 11179 C CG  . TYR F 2 181 ? 87.322  -46.813 5.905   1.000 73.820  ? 181 TYR FFF CG  1 
ATOM 11180 C CD1 . TYR F 2 181 ? 88.016  -45.756 6.476   1.000 75.560  ? 181 TYR FFF CD1 1 
ATOM 11181 C CD2 . TYR F 2 181 ? 87.056  -46.721 4.548   1.000 75.520  ? 181 TYR FFF CD2 1 
ATOM 11182 C CE1 . TYR F 2 181 ? 88.408  -44.642 5.740   1.000 73.240  ? 181 TYR FFF CE1 1 
ATOM 11183 C CE2 . TYR F 2 181 ? 87.450  -45.624 3.792   1.000 70.790  ? 181 TYR FFF CE2 1 
ATOM 11184 C CZ  . TYR F 2 181 ? 88.127  -44.577 4.390   1.000 72.560  ? 181 TYR FFF CZ  1 
ATOM 11185 O OH  . TYR F 2 181 ? 88.520  -43.480 3.675   1.000 75.830  ? 181 TYR FFF OH  1 
ATOM 11186 N N   . LEU F 2 182 ? 84.526  -49.833 8.082   1.000 77.240  ? 182 LEU FFF N   1 
ATOM 11187 C CA  . LEU F 2 182 ? 84.099  -51.118 8.702   1.000 83.540  ? 182 LEU FFF CA  1 
ATOM 11188 C C   . LEU F 2 182 ? 83.904  -52.167 7.609   1.000 82.130  ? 182 LEU FFF C   1 
ATOM 11189 O O   . LEU F 2 182 ? 83.162  -51.880 6.658   1.000 85.060  ? 182 LEU FFF O   1 
ATOM 11190 C CB  . LEU F 2 182 ? 82.795  -50.908 9.478   1.000 93.800  ? 182 LEU FFF CB  1 
ATOM 11191 C CG  . LEU F 2 182 ? 82.115  -52.186 9.976   1.000 98.240  ? 182 LEU FFF CG  1 
ATOM 11192 C CD1 . LEU F 2 182 ? 82.916  -52.849 11.093  1.000 105.520 ? 182 LEU FFF CD1 1 
ATOM 11193 C CD2 . LEU F 2 182 ? 80.696  -51.895 10.439  1.000 95.420  ? 182 LEU FFF CD2 1 
ATOM 11194 N N   . SER F 2 183 ? 84.534  -53.333 7.756   1.000 84.280  ? 183 SER FFF N   1 
ATOM 11195 C CA  . SER F 2 183 ? 84.440  -54.464 6.799   1.000 91.270  ? 183 SER FFF CA  1 
ATOM 11196 C C   . SER F 2 183 ? 83.301  -55.382 7.237   1.000 90.510  ? 183 SER FFF C   1 
ATOM 11197 O O   . SER F 2 183 ? 83.108  -55.532 8.462   1.000 88.230  ? 183 SER FFF O   1 
ATOM 11198 C CB  . SER F 2 183 ? 85.740  -55.219 6.705   1.000 101.280 ? 183 SER FFF CB  1 
ATOM 11199 O OG  . SER F 2 183 ? 86.813  -54.347 6.386   1.000 111.690 ? 183 SER FFF OG  1 
ATOM 11200 N N   . LEU F 2 184 ? 82.578  -55.952 6.270   1.000 88.900  ? 184 LEU FFF N   1 
ATOM 11201 C CA  . LEU F 2 184 ? 81.455  -56.895 6.506   1.000 92.510  ? 184 LEU FFF CA  1 
ATOM 11202 C C   . LEU F 2 184 ? 81.498  -58.027 5.470   1.000 86.830  ? 184 LEU FFF C   1 
ATOM 11203 O O   . LEU F 2 184 ? 81.900  -57.783 4.319   1.000 87.060  ? 184 LEU FFF O   1 
ATOM 11204 C CB  . LEU F 2 184 ? 80.123  -56.129 6.437   1.000 96.200  ? 184 LEU FFF CB  1 
ATOM 11205 C CG  . LEU F 2 184 ? 79.541  -55.643 7.771   1.000 94.120  ? 184 LEU FFF CG  1 
ATOM 11206 C CD1 . LEU F 2 184 ? 80.030  -54.243 8.105   1.000 82.880  ? 184 LEU FFF CD1 1 
ATOM 11207 C CD2 . LEU F 2 184 ? 78.005  -55.683 7.778   1.000 101.810 ? 184 LEU FFF CD2 1 
ATOM 11208 N N   . THR F 2 185 ? 81.059  -59.218 5.886   1.000 83.220  ? 185 THR FFF N   1 
ATOM 11209 C CA  . THR F 2 185 ? 80.573  -60.303 5.006   1.000 90.430  ? 185 THR FFF CA  1 
ATOM 11210 C C   . THR F 2 185 ? 79.152  -59.975 4.547   1.000 107.570 ? 185 THR FFF C   1 
ATOM 11211 O O   . THR F 2 185 ? 78.275  -59.676 5.371   1.000 122.720 ? 185 THR FFF O   1 
ATOM 11212 C CB  . THR F 2 185 ? 80.535  -61.649 5.739   1.000 91.610  ? 185 THR FFF CB  1 
ATOM 11213 O OG1 . THR F 2 185 ? 81.734  -61.710 6.503   1.000 105.170 ? 185 THR FFF OG1 1 
ATOM 11214 C CG2 . THR F 2 185 ? 80.434  -62.849 4.821   1.000 87.070  ? 185 THR FFF CG2 1 
ATOM 11215 N N   . PRO F 2 186 ? 78.889  -60.019 3.217   1.000 95.440  ? 186 PRO FFF N   1 
ATOM 11216 C CA  . PRO F 2 186 ? 77.525  -60.185 2.700   1.000 82.840  ? 186 PRO FFF CA  1 
ATOM 11217 C C   . PRO F 2 186 ? 76.845  -61.484 3.182   1.000 71.300  ? 186 PRO FFF C   1 
ATOM 11218 O O   . PRO F 2 186 ? 76.319  -61.483 4.294   1.000 58.830  ? 186 PRO FFF O   1 
ATOM 11219 C CB  . PRO F 2 186 ? 77.721  -60.217 1.173   1.000 79.940  ? 186 PRO FFF CB  1 
ATOM 11220 C CG  . PRO F 2 186 ? 79.073  -59.559 0.923   1.000 78.000  ? 186 PRO FFF CG  1 
ATOM 11221 C CD  . PRO F 2 186 ? 79.896  -59.860 2.153   1.000 83.760  ? 186 PRO FFF CD  1 
ATOM 11222 N N   . SER F 2 194 ? 70.089  -51.954 9.262   1.000 79.040  ? 194 SER FFF N   1 
ATOM 11223 C CA  . SER F 2 194 ? 70.229  -51.904 10.742  1.000 79.460  ? 194 SER FFF CA  1 
ATOM 11224 C C   . SER F 2 194 ? 71.440  -51.034 11.151  1.000 89.900  ? 194 SER FFF C   1 
ATOM 11225 O O   . SER F 2 194 ? 71.220  -50.123 11.991  1.000 94.780  ? 194 SER FFF O   1 
ATOM 11226 C CB  . SER F 2 194 ? 70.288  -53.313 11.320  1.000 75.050  ? 194 SER FFF CB  1 
ATOM 11227 O OG  . SER F 2 194 ? 69.484  -54.223 10.568  1.000 61.090  ? 194 SER FFF OG  1 
ATOM 11228 N N   . TYR F 2 195 ? 72.630  -51.246 10.537  1.000 90.830  ? 195 TYR FFF N   1 
ATOM 11229 C CA  . TYR F 2 195 ? 73.994  -50.806 10.985  1.000 89.750  ? 195 TYR FFF CA  1 
ATOM 11230 C C   . TYR F 2 195 ? 74.147  -49.273 10.948  1.000 88.190  ? 195 TYR FFF C   1 
ATOM 11231 O O   . TYR F 2 195 ? 73.875  -48.663 9.888   1.000 85.210  ? 195 TYR FFF O   1 
ATOM 11232 C CB  . TYR F 2 195 ? 75.092  -51.480 10.146  1.000 74.790  ? 195 TYR FFF CB  1 
ATOM 11233 N N   . SER F 2 196 ? 74.556  -48.675 12.078  1.000 84.780  ? 196 SER FFF N   1 
ATOM 11234 C CA  . SER F 2 196 ? 74.805  -47.218 12.251  1.000 91.320  ? 196 SER FFF CA  1 
ATOM 11235 C C   . SER F 2 196 ? 76.295  -46.941 12.544  1.000 99.860  ? 196 SER FFF C   1 
ATOM 11236 O O   . SER F 2 196 ? 77.069  -47.903 12.719  1.000 96.480  ? 196 SER FFF O   1 
ATOM 11237 C CB  . SER F 2 196 ? 73.919  -46.653 13.340  1.000 88.540  ? 196 SER FFF CB  1 
ATOM 11238 O OG  . SER F 2 196 ? 73.973  -45.228 13.358  1.000 89.480  ? 196 SER FFF OG  1 
ATOM 11239 N N   . CYS F 2 197 ? 76.674  -45.657 12.632  1.000 103.510 ? 197 CYS FFF N   1 
ATOM 11240 C CA  . CYS F 2 197 ? 78.045  -45.150 12.940  1.000 94.190  ? 197 CYS FFF CA  1 
ATOM 11241 C C   . CYS F 2 197 ? 77.948  -43.994 13.956  1.000 93.610  ? 197 CYS FFF C   1 
ATOM 11242 O O   . CYS F 2 197 ? 78.030  -42.811 13.544  1.000 82.800  ? 197 CYS FFF O   1 
ATOM 11243 C CB  . CYS F 2 197 ? 78.763  -44.713 11.663  1.000 94.740  ? 197 CYS FFF CB  1 
ATOM 11244 S SG  . CYS F 2 197 ? 80.372  -43.904 11.936  1.000 96.060  ? 197 CYS FFF SG  1 
ATOM 11245 N N   . GLN F 2 198 ? 77.774  -44.328 15.243  1.000 94.330  ? 198 GLN FFF N   1 
ATOM 11246 C CA  . GLN F 2 198 ? 77.670  -43.357 16.369  1.000 89.870  ? 198 GLN FFF CA  1 
ATOM 11247 C C   . GLN F 2 198 ? 79.067  -42.750 16.616  1.000 80.640  ? 198 GLN FFF C   1 
ATOM 11248 O O   . GLN F 2 198 ? 80.009  -43.533 16.846  1.000 82.250  ? 198 GLN FFF O   1 
ATOM 11249 C CB  . GLN F 2 198 ? 77.050  -44.067 17.590  1.000 73.820  ? 198 GLN FFF CB  1 
ATOM 11250 N N   . VAL F 2 199 ? 79.211  -41.418 16.517  1.000 71.160  ? 199 VAL FFF N   1 
ATOM 11251 C CA  . VAL F 2 199 ? 80.498  -40.679 16.739  1.000 76.400  ? 199 VAL FFF CA  1 
ATOM 11252 C C   . VAL F 2 199 ? 80.285  -39.636 17.852  1.000 83.560  ? 199 VAL FFF C   1 
ATOM 11253 O O   . VAL F 2 199 ? 79.394  -38.784 17.697  1.000 97.540  ? 199 VAL FFF O   1 
ATOM 11254 C CB  . VAL F 2 199 ? 81.080  -40.045 15.446  1.000 74.860  ? 199 VAL FFF CB  1 
ATOM 11255 C CG1 . VAL F 2 199 ? 80.769  -40.854 14.192  1.000 78.990  ? 199 VAL FFF CG1 1 
ATOM 11256 C CG2 . VAL F 2 199 ? 80.696  -38.590 15.223  1.000 74.560  ? 199 VAL FFF CG2 1 
ATOM 11257 N N   . THR F 2 200 ? 81.117  -39.674 18.899  1.000 92.180  ? 200 THR FFF N   1 
ATOM 11258 C CA  . THR F 2 200 ? 81.097  -38.746 20.070  1.000 96.500  ? 200 THR FFF CA  1 
ATOM 11259 C C   . THR F 2 200 ? 82.056  -37.568 19.829  1.000 93.850  ? 200 THR FFF C   1 
ATOM 11260 O O   . THR F 2 200 ? 83.018  -37.736 19.063  1.000 103.010 ? 200 THR FFF O   1 
ATOM 11261 C CB  . THR F 2 200 ? 81.478  -39.489 21.358  1.000 97.640  ? 200 THR FFF CB  1 
ATOM 11262 O OG1 . THR F 2 200 ? 80.906  -40.799 21.320  1.000 94.540  ? 200 THR FFF OG1 1 
ATOM 11263 C CG2 . THR F 2 200 ? 81.039  -38.750 22.602  1.000 96.530  ? 200 THR FFF CG2 1 
ATOM 11264 N N   . HIS F 2 201 ? 81.800  -36.419 20.454  1.000 91.010  ? 201 HIS FFF N   1 
ATOM 11265 C CA  . HIS F 2 201 ? 82.630  -35.191 20.309  1.000 101.900 ? 201 HIS FFF CA  1 
ATOM 11266 C C   . HIS F 2 201 ? 82.303  -34.201 21.434  1.000 107.340 ? 201 HIS FFF C   1 
ATOM 11267 O O   . HIS F 2 201 ? 81.285  -33.485 21.334  1.000 108.520 ? 201 HIS FFF O   1 
ATOM 11268 C CB  . HIS F 2 201 ? 82.441  -34.592 18.909  1.000 106.850 ? 201 HIS FFF CB  1 
ATOM 11269 C CG  . HIS F 2 201 ? 83.041  -33.238 18.728  1.000 113.330 ? 201 HIS FFF CG  1 
ATOM 11270 N ND1 . HIS F 2 201 ? 84.398  -33.051 18.535  1.000 125.140 ? 201 HIS FFF ND1 1 
ATOM 11271 C CD2 . HIS F 2 201 ? 82.477  -32.011 18.639  1.000 119.580 ? 201 HIS FFF CD2 1 
ATOM 11272 C CE1 . HIS F 2 201 ? 84.648  -31.766 18.377  1.000 128.770 ? 201 HIS FFF CE1 1 
ATOM 11273 N NE2 . HIS F 2 201 ? 83.484  -31.106 18.439  1.000 128.870 ? 201 HIS FFF NE2 1 
ATOM 11274 N N   . GLU F 2 202 ? 83.145  -34.168 22.472  1.000 106.790 ? 202 GLU FFF N   1 
ATOM 11275 C CA  . GLU F 2 202 ? 82.904  -33.405 23.724  1.000 98.700  ? 202 GLU FFF CA  1 
ATOM 11276 C C   . GLU F 2 202 ? 81.626  -33.952 24.390  1.000 93.970  ? 202 GLU FFF C   1 
ATOM 11277 O O   . GLU F 2 202 ? 80.703  -33.154 24.635  1.000 92.060  ? 202 GLU FFF O   1 
ATOM 11278 C CB  . GLU F 2 202 ? 82.841  -31.902 23.410  1.000 95.620  ? 202 GLU FFF CB  1 
ATOM 11279 C CG  . GLU F 2 202 ? 83.935  -31.383 22.474  1.000 94.080  ? 202 GLU FFF CG  1 
ATOM 11280 C CD  . GLU F 2 202 ? 85.359  -31.387 23.015  1.000 91.920  ? 202 GLU FFF CD  1 
ATOM 11281 O OE1 . GLU F 2 202 ? 85.601  -32.095 23.994  1.000 101.530 ? 202 GLU FFF OE1 1 
ATOM 11282 O OE2 . GLU F 2 202 ? 86.233  -30.690 22.450  1.000 79.540  ? 202 GLU FFF OE2 1 
ATOM 11283 N N   . GLY F 2 203 ? 81.564  -35.273 24.620  1.000 91.540  ? 203 GLY FFF N   1 
ATOM 11284 C CA  . GLY F 2 203 ? 80.497  -35.971 25.373  1.000 93.830  ? 203 GLY FFF CA  1 
ATOM 11285 C C   . GLY F 2 203 ? 79.158  -36.058 24.629  1.000 95.430  ? 203 GLY FFF C   1 
ATOM 11286 O O   . GLY F 2 203 ? 78.207  -36.559 25.256  1.000 79.980  ? 203 GLY FFF O   1 
ATOM 11287 N N   . THR F 2 204 ? 79.079  -35.658 23.346  1.000 99.200  ? 204 THR FFF N   1 
ATOM 11288 C CA  . THR F 2 204 ? 77.811  -35.440 22.574  1.000 88.490  ? 204 THR FFF CA  1 
ATOM 11289 C C   . THR F 2 204 ? 77.792  -36.168 21.211  1.000 84.480  ? 204 THR FFF C   1 
ATOM 11290 O O   . THR F 2 204 ? 78.483  -35.707 20.285  1.000 73.320  ? 204 THR FFF O   1 
ATOM 11291 C CB  . THR F 2 204 ? 77.547  -33.933 22.389  1.000 80.400  ? 204 THR FFF CB  1 
ATOM 11292 O OG1 . THR F 2 204 ? 78.643  -33.329 21.693  1.000 67.580  ? 204 THR FFF OG1 1 
ATOM 11293 C CG2 . THR F 2 204 ? 77.305  -33.215 23.704  1.000 72.730  ? 204 THR FFF CG2 1 
ATOM 11294 N N   . THR F 2 205 ? 76.934  -37.196 21.084  1.000 91.080  ? 205 THR FFF N   1 
ATOM 11295 C CA  . THR F 2 205 ? 76.851  -38.195 19.967  1.000 95.930  ? 205 THR FFF CA  1 
ATOM 11296 C C   . THR F 2 205 ? 76.041  -37.647 18.767  1.000 90.270  ? 205 THR FFF C   1 
ATOM 11297 O O   . THR F 2 205 ? 75.104  -36.870 19.002  1.000 83.060  ? 205 THR FFF O   1 
ATOM 11298 C CB  . THR F 2 205 ? 76.286  -39.543 20.452  1.000 93.640  ? 205 THR FFF CB  1 
ATOM 11299 O OG1 . THR F 2 205 ? 76.896  -39.852 21.705  1.000 85.930  ? 205 THR FFF OG1 1 
ATOM 11300 C CG2 . THR F 2 205 ? 76.517  -40.682 19.478  1.000 91.870  ? 205 THR FFF CG2 1 
ATOM 11301 N N   . VAL F 2 206 ? 76.392  -38.052 17.532  1.000 83.990  ? 206 VAL FFF N   1 
ATOM 11302 C CA  . VAL F 2 206 ? 75.865  -37.513 16.241  1.000 83.670  ? 206 VAL FFF CA  1 
ATOM 11303 C C   . VAL F 2 206 ? 75.750  -38.658 15.225  1.000 83.720  ? 206 VAL FFF C   1 
ATOM 11304 O O   . VAL F 2 206 ? 76.148  -38.436 14.065  1.000 79.550  ? 206 VAL FFF O   1 
ATOM 11305 C CB  . VAL F 2 206 ? 76.744  -36.370 15.673  1.000 86.630  ? 206 VAL FFF CB  1 
ATOM 11306 C CG1 . VAL F 2 206 ? 76.097  -35.651 14.492  1.000 84.650  ? 206 VAL FFF CG1 1 
ATOM 11307 C CG2 . VAL F 2 206 ? 77.137  -35.353 16.737  1.000 92.580  ? 206 VAL FFF CG2 1 
ATOM 11308 N N   . GLU F 2 207 ? 75.193  -39.814 15.623  1.000 93.090  ? 207 GLU FFF N   1 
ATOM 11309 C CA  . GLU F 2 207 ? 75.039  -41.031 14.757  1.000 94.170  ? 207 GLU FFF CA  1 
ATOM 11310 C C   . GLU F 2 207 ? 74.185  -40.700 13.514  1.000 87.700  ? 207 GLU FFF C   1 
ATOM 11311 O O   . GLU F 2 207 ? 73.080  -40.170 13.688  1.000 83.560  ? 207 GLU FFF O   1 
ATOM 11312 C CB  . GLU F 2 207 ? 74.429  -42.206 15.541  1.000 82.460  ? 207 GLU FFF CB  1 
ATOM 11313 N N   . LYS F 2 208 ? 74.707  -40.963 12.307  1.000 87.580  ? 208 LYS FFF N   1 
ATOM 11314 C CA  . LYS F 2 208 ? 73.927  -41.134 11.043  1.000 87.490  ? 208 LYS FFF CA  1 
ATOM 11315 C C   . LYS F 2 208 ? 73.829  -42.655 10.790  1.000 88.140  ? 208 LYS FFF C   1 
ATOM 11316 O O   . LYS F 2 208 ? 74.701  -43.396 11.302  1.000 75.430  ? 208 LYS FFF O   1 
ATOM 11317 C CB  . LYS F 2 208 ? 74.551  -40.325 9.891   1.000 72.360  ? 208 LYS FFF CB  1 
ATOM 11318 N N   . THR F 2 209 ? 72.781  -43.121 10.093  1.000 87.540  ? 209 THR FFF N   1 
ATOM 11319 C CA  . THR F 2 209 ? 72.471  -44.568 9.873   1.000 84.070  ? 209 THR FFF CA  1 
ATOM 11320 C C   . THR F 2 209 ? 72.304  -44.859 8.372   1.000 83.530  ? 209 THR FFF C   1 
ATOM 11321 O O   . THR F 2 209 ? 72.091  -43.896 7.589   1.000 83.190  ? 209 THR FFF O   1 
ATOM 11322 C CB  . THR F 2 209 ? 71.204  -44.994 10.631  1.000 81.920  ? 209 THR FFF CB  1 
ATOM 11323 O OG1 . THR F 2 209 ? 71.225  -44.376 11.915  1.000 82.240  ? 209 THR FFF OG1 1 
ATOM 11324 C CG2 . THR F 2 209 ? 71.063  -46.494 10.790  1.000 78.750  ? 209 THR FFF CG2 1 
ATOM 11325 N N   . VAL F 2 210 ? 72.409  -46.141 7.997   1.000 76.260  ? 210 VAL FFF N   1 
ATOM 11326 C CA  . VAL F 2 210 ? 72.139  -46.676 6.630   1.000 74.760  ? 210 VAL FFF CA  1 
ATOM 11327 C C   . VAL F 2 210 ? 71.683  -48.134 6.793   1.000 69.440  ? 210 VAL FFF C   1 
ATOM 11328 O O   . VAL F 2 210 ? 71.906  -48.685 7.889   1.000 60.380  ? 210 VAL FFF O   1 
ATOM 11329 C CB  . VAL F 2 210 ? 73.384  -46.531 5.727   1.000 86.710  ? 210 VAL FFF CB  1 
ATOM 11330 C CG1 . VAL F 2 210 ? 74.461  -47.562 6.047   1.000 91.520  ? 210 VAL FFF CG1 1 
ATOM 11331 C CG2 . VAL F 2 210 ? 73.047  -46.558 4.244   1.000 89.090  ? 210 VAL FFF CG2 1 
ATOM 11332 N N   . ALA F 2 211 ? 71.080  -48.719 5.752   1.000 69.060  ? 211 ALA FFF N   1 
ATOM 11333 C CA  . ALA F 2 211 ? 70.581  -50.121 5.710   1.000 70.590  ? 211 ALA FFF CA  1 
ATOM 11334 C C   . ALA F 2 211 ? 70.581  -50.668 4.274   1.000 74.800  ? 211 ALA FFF C   1 
ATOM 11335 O O   . ALA F 2 211 ? 70.719  -49.897 3.319   1.000 80.910  ? 211 ALA FFF O   1 
ATOM 11336 C CB  . ALA F 2 211 ? 69.192  -50.176 6.339   1.000 70.160  ? 211 ALA FFF CB  1 
ATOM 11337 N N   . PRO F 2 212 ? 70.456  -52.012 4.071   1.000 70.690  ? 212 PRO FFF N   1 
ATOM 11338 C CA  . PRO F 2 212 ? 70.353  -52.590 2.720   1.000 63.940  ? 212 PRO FFF CA  1 
ATOM 11339 C C   . PRO F 2 212 ? 69.338  -51.879 1.807   1.000 61.380  ? 212 PRO FFF C   1 
ATOM 11340 O O   . PRO F 2 212 ? 68.953  -52.345 0.737   1.000 54.330  ? 212 PRO FFF O   1 
ATOM 11341 C CB  . PRO F 2 212 ? 69.913  -54.035 3.009   1.000 61.420  ? 212 PRO FFF CB  1 
ATOM 11342 C CG  . PRO F 2 212 ? 70.538  -54.348 4.368   1.000 59.900  ? 212 PRO FFF CG  1 
ATOM 11343 C CD  . PRO F 2 212 ? 70.445  -53.046 5.130   1.000 60.180  ? 212 PRO FFF CD  1 
ATOM 11344 N N   . LEU G 2 4   ? 105.394 21.733  58.432  1.000 55.940  ? 4   LEU GGG N   1 
ATOM 11345 C CA  . LEU G 2 4   ? 105.229 20.975  57.165  1.000 55.200  ? 4   LEU GGG CA  1 
ATOM 11346 C C   . LEU G 2 4   ? 103.852 21.312  56.582  1.000 64.360  ? 4   LEU GGG C   1 
ATOM 11347 O O   . LEU G 2 4   ? 102.835 21.242  57.309  1.000 59.190  ? 4   LEU GGG O   1 
ATOM 11348 C CB  . LEU G 2 4   ? 105.409 19.474  57.391  1.000 49.770  ? 4   LEU GGG CB  1 
ATOM 11349 C CG  . LEU G 2 4   ? 106.750 19.077  58.010  1.000 51.520  ? 4   LEU GGG CG  1 
ATOM 11350 C CD1 . LEU G 2 4   ? 106.947 17.565  58.062  1.000 57.930  ? 4   LEU GGG CD1 1 
ATOM 11351 C CD2 . LEU G 2 4   ? 107.911 19.690  57.259  1.000 51.250  ? 4   LEU GGG CD2 1 
ATOM 11352 N N   . THR G 2 5   ? 103.843 21.713  55.315  1.000 73.590  ? 5   THR GGG N   1 
ATOM 11353 C CA  . THR G 2 5   ? 102.633 22.124  54.563  1.000 69.830  ? 5   THR GGG CA  1 
ATOM 11354 C C   . THR G 2 5   ? 102.286 20.998  53.584  1.000 75.290  ? 5   THR GGG C   1 
ATOM 11355 O O   . THR G 2 5   ? 103.140 20.716  52.696  1.000 74.550  ? 5   THR GGG O   1 
ATOM 11356 C CB  . THR G 2 5   ? 102.872 23.492  53.916  1.000 64.870  ? 5   THR GGG CB  1 
ATOM 11357 O OG1 . THR G 2 5   ? 104.224 23.513  53.449  1.000 73.110  ? 5   THR GGG OG1 1 
ATOM 11358 C CG2 . THR G 2 5   ? 102.616 24.619  54.895  1.000 60.560  ? 5   THR GGG CG2 1 
ATOM 11359 N N   . GLN G 2 6   ? 101.124 20.358  53.770  1.000 73.730  ? 6   GLN GGG N   1 
ATOM 11360 C CA  . GLN G 2 6   ? 100.568 19.383  52.787  1.000 71.680  ? 6   GLN GGG CA  1 
ATOM 11361 C C   . GLN G 2 6   ? 99.111  19.739  52.452  1.000 64.770  ? 6   GLN GGG C   1 
ATOM 11362 O O   . GLN G 2 6   ? 98.394  20.312  53.266  1.000 56.470  ? 6   GLN GGG O   1 
ATOM 11363 C CB  . GLN G 2 6   ? 100.760 17.949  53.297  1.000 71.080  ? 6   GLN GGG CB  1 
ATOM 11364 C CG  . GLN G 2 6   ? 99.833  17.562  54.441  1.000 75.040  ? 6   GLN GGG CG  1 
ATOM 11365 C CD  . GLN G 2 6   ? 100.276 16.286  55.115  1.000 69.340  ? 6   GLN GGG CD  1 
ATOM 11366 O OE1 . GLN G 2 6   ? 101.308 16.219  55.777  1.000 76.650  ? 6   GLN GGG OE1 1 
ATOM 11367 N NE2 . GLN G 2 6   ? 99.486  15.245  54.961  1.000 62.970  ? 6   GLN GGG NE2 1 
ATOM 11368 N N   . PRO G 2 7   ? 98.643  19.436  51.223  1.000 63.790  ? 7   PRO GGG N   1 
ATOM 11369 C CA  . PRO G 2 7   ? 97.266  19.727  50.833  1.000 64.170  ? 7   PRO GGG CA  1 
ATOM 11370 C C   . PRO G 2 7   ? 96.249  19.148  51.823  1.000 64.670  ? 7   PRO GGG C   1 
ATOM 11371 O O   . PRO G 2 7   ? 96.381  17.986  52.199  1.000 65.600  ? 7   PRO GGG O   1 
ATOM 11372 C CB  . PRO G 2 7   ? 97.136  19.020  49.469  1.000 74.330  ? 7   PRO GGG CB  1 
ATOM 11373 C CG  . PRO G 2 7   ? 98.544  19.011  48.910  1.000 69.020  ? 7   PRO GGG CG  1 
ATOM 11374 C CD  . PRO G 2 7   ? 99.408  18.809  50.131  1.000 67.530  ? 7   PRO GGG CD  1 
ATOM 11375 N N   . PRO G 2 8   ? 95.256  19.929  52.308  1.000 69.700  ? 8   PRO GGG N   1 
ATOM 11376 C CA  . PRO G 2 8   ? 94.238  19.416  53.230  1.000 68.610  ? 8   PRO GGG CA  1 
ATOM 11377 C C   . PRO G 2 8   ? 93.441  18.242  52.648  1.000 68.310  ? 8   PRO GGG C   1 
ATOM 11378 O O   . PRO G 2 8   ? 93.066  17.363  53.401  1.000 55.990  ? 8   PRO GGG O   1 
ATOM 11379 C CB  . PRO G 2 8   ? 93.307  20.615  53.480  1.000 68.660  ? 8   PRO GGG CB  1 
ATOM 11380 C CG  . PRO G 2 8   ? 94.181  21.816  53.196  1.000 73.780  ? 8   PRO GGG CG  1 
ATOM 11381 C CD  . PRO G 2 8   ? 95.087  21.368  52.066  1.000 75.400  ? 8   PRO GGG CD  1 
ATOM 11382 N N   . SER G 2 9   ? 93.231  18.238  51.331  1.000 71.970  ? 9   SER GGG N   1 
ATOM 11383 C CA  . SER G 2 9   ? 92.528  17.130  50.640  1.000 69.570  ? 9   SER GGG CA  1 
ATOM 11384 C C   . SER G 2 9   ? 93.175  16.838  49.286  1.000 63.790  ? 9   SER GGG C   1 
ATOM 11385 O O   . SER G 2 9   ? 93.881  17.713  48.727  1.000 54.120  ? 9   SER GGG O   1 
ATOM 11386 C CB  . SER G 2 9   ? 91.056  17.417  50.488  1.000 74.560  ? 9   SER GGG CB  1 
ATOM 11387 O OG  . SER G 2 9   ? 90.848  18.519  49.623  1.000 85.240  ? 9   SER GGG OG  1 
ATOM 11388 N N   . ALA G 2 10  ? 92.959  15.604  48.829  1.000 65.260  ? 10  ALA GGG N   1 
ATOM 11389 C CA  . ALA G 2 10  ? 93.274  15.089  47.485  1.000 61.820  ? 10  ALA GGG CA  1 
ATOM 11390 C C   . ALA G 2 10  ? 92.235  14.013  47.167  1.000 64.600  ? 10  ALA GGG C   1 
ATOM 11391 O O   . ALA G 2 10  ? 91.643  13.450  48.115  1.000 58.030  ? 10  ALA GGG O   1 
ATOM 11392 C CB  . ALA G 2 10  ? 94.672  14.539  47.471  1.000 56.900  ? 10  ALA GGG CB  1 
ATOM 11393 N N   . SER G 2 11  ? 92.031  13.738  45.882  1.000 73.360  ? 11  SER GGG N   1 
ATOM 11394 C CA  . SER G 2 11  ? 91.061  12.723  45.394  1.000 74.410  ? 11  SER GGG CA  1 
ATOM 11395 C C   . SER G 2 11  ? 91.485  12.194  44.024  1.000 76.220  ? 11  SER GGG C   1 
ATOM 11396 O O   . SER G 2 11  ? 92.417  12.781  43.417  1.000 73.550  ? 11  SER GGG O   1 
ATOM 11397 C CB  . SER G 2 11  ? 89.683  13.298  45.339  1.000 76.220  ? 11  SER GGG CB  1 
ATOM 11398 O OG  . SER G 2 11  ? 89.642  14.368  44.411  1.000 75.620  ? 11  SER GGG OG  1 
ATOM 11399 N N   . GLY G 2 12  ? 90.834  11.113  43.585  1.000 83.120  ? 12  GLY GGG N   1 
ATOM 11400 C CA  . GLY G 2 12  ? 91.074  10.470  42.282  1.000 84.020  ? 12  GLY GGG CA  1 
ATOM 11401 C C   . GLY G 2 12  ? 90.064  9.379   41.979  1.000 82.710  ? 12  GLY GGG C   1 
ATOM 11402 O O   . GLY G 2 12  ? 89.329  8.958   42.898  1.000 65.210  ? 12  GLY GGG O   1 
ATOM 11403 N N   . THR G 2 13  ? 90.044  8.949   40.715  1.000 91.460  ? 13  THR GGG N   1 
ATOM 11404 C CA  . THR G 2 13  ? 89.223  7.827   40.189  1.000 88.630  ? 13  THR GGG CA  1 
ATOM 11405 C C   . THR G 2 13  ? 90.054  6.539   40.282  1.000 79.620  ? 13  THR GGG C   1 
ATOM 11406 O O   . THR G 2 13  ? 91.261  6.533   39.998  1.000 76.790  ? 13  THR GGG O   1 
ATOM 11407 C CB  . THR G 2 13  ? 88.759  8.152   38.768  1.000 95.590  ? 13  THR GGG CB  1 
ATOM 11408 O OG1 . THR G 2 13  ? 89.919  8.579   38.055  1.000 92.800  ? 13  THR GGG OG1 1 
ATOM 11409 C CG2 . THR G 2 13  ? 87.694  9.233   38.730  1.000 100.970 ? 13  THR GGG CG2 1 
ATOM 11410 N N   . PRO G 2 14  ? 89.437  5.404   40.704  1.000 74.260  ? 14  PRO GGG N   1 
ATOM 11411 C CA  . PRO G 2 14  ? 90.177  4.147   40.834  1.000 71.250  ? 14  PRO GGG CA  1 
ATOM 11412 C C   . PRO G 2 14  ? 91.072  3.900   39.599  1.000 69.000  ? 14  PRO GGG C   1 
ATOM 11413 O O   . PRO G 2 14  ? 90.604  4.127   38.521  1.000 86.180  ? 14  PRO GGG O   1 
ATOM 11414 C CB  . PRO G 2 14  ? 89.069  3.091   40.984  1.000 68.340  ? 14  PRO GGG CB  1 
ATOM 11415 C CG  . PRO G 2 14  ? 87.906  3.843   41.604  1.000 65.680  ? 14  PRO GGG CG  1 
ATOM 11416 C CD  . PRO G 2 14  ? 88.020  5.267   41.094  1.000 70.160  ? 14  PRO GGG CD  1 
ATOM 11417 N N   . GLY G 2 15  ? 92.330  3.498   39.796  1.000 60.630  ? 15  GLY GGG N   1 
ATOM 11418 C CA  . GLY G 2 15  ? 93.308  3.211   38.729  1.000 57.670  ? 15  GLY GGG CA  1 
ATOM 11419 C C   . GLY G 2 15  ? 94.214  4.394   38.455  1.000 63.480  ? 15  GLY GGG C   1 
ATOM 11420 O O   . GLY G 2 15  ? 95.285  4.166   37.864  1.000 63.930  ? 15  GLY GGG O   1 
ATOM 11421 N N   . GLN G 2 16  ? 93.821  5.609   38.861  1.000 73.350  ? 16  GLN GGG N   1 
ATOM 11422 C CA  . GLN G 2 16  ? 94.622  6.856   38.658  1.000 76.980  ? 16  GLN GGG CA  1 
ATOM 11423 C C   . GLN G 2 16  ? 95.876  6.866   39.550  1.000 78.450  ? 16  GLN GGG C   1 
ATOM 11424 O O   . GLN G 2 16  ? 95.968  6.022   40.477  1.000 70.640  ? 16  GLN GGG O   1 
ATOM 11425 C CB  . GLN G 2 16  ? 93.803  8.116   38.946  1.000 76.480  ? 16  GLN GGG CB  1 
ATOM 11426 C CG  . GLN G 2 16  ? 93.167  8.725   37.703  1.000 82.060  ? 16  GLN GGG CG  1 
ATOM 11427 C CD  . GLN G 2 16  ? 92.415  10.003  37.996  1.000 88.980  ? 16  GLN GGG CD  1 
ATOM 11428 O OE1 . GLN G 2 16  ? 91.813  10.172  39.052  1.000 91.160  ? 16  GLN GGG OE1 1 
ATOM 11429 N NE2 . GLN G 2 16  ? 92.452  10.929  37.051  1.000 91.280  ? 16  GLN GGG NE2 1 
ATOM 11430 N N   . ARG G 2 17  ? 96.798  7.785   39.248  1.000 74.050  ? 17  ARG GGG N   1 
ATOM 11431 C CA  . ARG G 2 17  ? 97.955  8.161   40.113  1.000 74.040  ? 17  ARG GGG CA  1 
ATOM 11432 C C   . ARG G 2 17  ? 97.594  9.486   40.799  1.000 64.820  ? 17  ARG GGG C   1 
ATOM 11433 O O   . ARG G 2 17  ? 97.295  10.446  40.090  1.000 55.860  ? 17  ARG GGG O   1 
ATOM 11434 C CB  . ARG G 2 17  ? 99.250  8.269   39.293  1.000 79.770  ? 17  ARG GGG CB  1 
ATOM 11435 C CG  . ARG G 2 17  ? 100.486 8.643   40.095  1.000 81.890  ? 17  ARG GGG CG  1 
ATOM 11436 C CD  . ARG G 2 17  ? 101.757 8.268   39.360  1.000 83.440  ? 17  ARG GGG CD  1 
ATOM 11437 N NE  . ARG G 2 17  ? 102.819 9.249   39.565  1.000 91.840  ? 17  ARG GGG NE  1 
ATOM 11438 C CZ  . ARG G 2 17  ? 104.131 8.974   39.621  1.000 99.070  ? 17  ARG GGG CZ  1 
ATOM 11439 N NH1 . ARG G 2 17  ? 104.577 7.732   39.504  1.000 90.670  ? 17  ARG GGG NH1 1 
ATOM 11440 N NH2 . ARG G 2 17  ? 105.001 9.954   39.806  1.000 103.430 ? 17  ARG GGG NH2 1 
ATOM 11441 N N   . VAL G 2 18  ? 97.598  9.509   42.131  1.000 66.000  ? 18  VAL GGG N   1 
ATOM 11442 C CA  . VAL G 2 18  ? 97.409  10.731  42.968  1.000 65.570  ? 18  VAL GGG CA  1 
ATOM 11443 C C   . VAL G 2 18  ? 98.757  11.102  43.585  1.000 61.900  ? 18  VAL GGG C   1 
ATOM 11444 O O   . VAL G 2 18  ? 99.552  10.182  43.857  1.000 59.610  ? 18  VAL GGG O   1 
ATOM 11445 C CB  . VAL G 2 18  ? 96.353  10.514  44.066  1.000 64.540  ? 18  VAL GGG CB  1 
ATOM 11446 C CG1 . VAL G 2 18  ? 95.924  11.843  44.651  1.000 65.390  ? 18  VAL GGG CG1 1 
ATOM 11447 C CG2 . VAL G 2 18  ? 95.138  9.768   43.551  1.000 66.580  ? 18  VAL GGG CG2 1 
ATOM 11448 N N   . THR G 2 19  ? 98.997  12.389  43.835  1.000 58.440  ? 19  THR GGG N   1 
ATOM 11449 C CA  . THR G 2 19  ? 100.281 12.917  44.363  1.000 59.530  ? 19  THR GGG CA  1 
ATOM 11450 C C   . THR G 2 19  ? 99.990  13.834  45.563  1.000 59.850  ? 19  THR GGG C   1 
ATOM 11451 O O   . THR G 2 19  ? 99.285  14.821  45.382  1.000 61.300  ? 19  THR GGG O   1 
ATOM 11452 C CB  . THR G 2 19  ? 101.083 13.552  43.213  1.000 60.560  ? 19  THR GGG CB  1 
ATOM 11453 O OG1 . THR G 2 19  ? 102.431 13.661  43.657  1.000 67.340  ? 19  THR GGG OG1 1 
ATOM 11454 C CG2 . THR G 2 19  ? 100.562 14.897  42.746  1.000 60.030  ? 19  THR GGG CG2 1 
ATOM 11455 N N   . ILE G 2 20  ? 100.496 13.513  46.754  1.000 64.110  ? 20  ILE GGG N   1 
ATOM 11456 C CA  . ILE G 2 20  ? 100.426 14.401  47.958  1.000 67.510  ? 20  ILE GGG CA  1 
ATOM 11457 C C   . ILE G 2 20  ? 101.813 15.001  48.210  1.000 67.120  ? 20  ILE GGG C   1 
ATOM 11458 O O   . ILE G 2 20  ? 102.759 14.224  48.430  1.000 65.880  ? 20  ILE GGG O   1 
ATOM 11459 C CB  . ILE G 2 20  ? 99.928  13.651  49.212  1.000 71.490  ? 20  ILE GGG CB  1 
ATOM 11460 C CG1 . ILE G 2 20  ? 98.764  12.698  48.933  1.000 69.400  ? 20  ILE GGG CG1 1 
ATOM 11461 C CG2 . ILE G 2 20  ? 99.571  14.673  50.266  1.000 73.380  ? 20  ILE GGG CG2 1 
ATOM 11462 C CD1 . ILE G 2 20  ? 97.676  13.335  48.134  1.000 72.990  ? 20  ILE GGG CD1 1 
ATOM 11463 N N   . SER G 2 21  ? 101.933 16.326  48.204  1.000 67.510  ? 21  SER GGG N   1 
ATOM 11464 C CA  . SER G 2 21  ? 103.217 17.044  48.443  1.000 68.520  ? 21  SER GGG CA  1 
ATOM 11465 C C   . SER G 2 21  ? 103.344 17.407  49.926  1.000 69.500  ? 21  SER GGG C   1 
ATOM 11466 O O   . SER G 2 21  ? 102.299 17.545  50.593  1.000 57.400  ? 21  SER GGG O   1 
ATOM 11467 C CB  . SER G 2 21  ? 103.318 18.270  47.572  1.000 67.820  ? 21  SER GGG CB  1 
ATOM 11468 O OG  . SER G 2 21  ? 102.229 19.149  47.801  1.000 64.040  ? 21  SER GGG OG  1 
ATOM 11469 N N   . CYS G 2 22  ? 104.586 17.527  50.419  1.000 70.700  ? 22  CYS GGG N   1 
ATOM 11470 C CA  . CYS G 2 22  ? 104.928 17.944  51.805  1.000 65.130  ? 22  CYS GGG CA  1 
ATOM 11471 C C   . CYS G 2 22  ? 106.143 18.880  51.720  1.000 65.170  ? 22  CYS GGG C   1 
ATOM 11472 O O   . CYS G 2 22  ? 107.230 18.434  51.257  1.000 54.540  ? 22  CYS GGG O   1 
ATOM 11473 C CB  . CYS G 2 22  ? 105.213 16.724  52.676  1.000 66.320  ? 22  CYS GGG CB  1 
ATOM 11474 S SG  . CYS G 2 22  ? 105.488 17.009  54.437  1.000 64.260  ? 22  CYS GGG SG  1 
ATOM 11475 N N   . SER G 2 23  ? 105.953 20.131  52.127  1.000 70.740  ? 23  SER GGG N   1 
ATOM 11476 C CA  . SER G 2 23  ? 106.956 21.209  51.951  1.000 77.210  ? 23  SER GGG CA  1 
ATOM 11477 C C   . SER G 2 23  ? 107.384 21.686  53.327  1.000 82.830  ? 23  SER GGG C   1 
ATOM 11478 O O   . SER G 2 23  ? 106.461 22.023  54.128  1.000 75.970  ? 23  SER GGG O   1 
ATOM 11479 C CB  . SER G 2 23  ? 106.429 22.357  51.126  1.000 84.820  ? 23  SER GGG CB  1 
ATOM 11480 O OG  . SER G 2 23  ? 106.606 22.116  49.742  1.000 100.250 ? 23  SER GGG OG  1 
ATOM 11481 N N   . GLY G 2 24  ? 108.705 21.730  53.560  1.000 88.350  ? 24  GLY GGG N   1 
ATOM 11482 C CA  . GLY G 2 24  ? 109.314 22.192  54.823  1.000 88.720  ? 24  GLY GGG CA  1 
ATOM 11483 C C   . GLY G 2 24  ? 110.419 23.205  54.583  1.000 74.580  ? 24  GLY GGG C   1 
ATOM 11484 O O   . GLY G 2 24  ? 110.288 23.961  53.635  1.000 73.330  ? 24  GLY GGG O   1 
ATOM 11485 N N   . GLY G 2 25  ? 111.478 23.185  55.389  1.000 71.060  ? 25  GLY GGG N   1 
ATOM 11486 C CA  . GLY G 2 25  ? 112.629 24.098  55.290  1.000 79.790  ? 25  GLY GGG CA  1 
ATOM 11487 C C   . GLY G 2 25  ? 113.923 23.446  55.751  1.000 82.150  ? 25  GLY GGG C   1 
ATOM 11488 O O   . GLY G 2 25  ? 113.865 22.305  56.242  1.000 90.710  ? 25  GLY GGG O   1 
ATOM 11489 N N   . SER G 2 26  ? 115.054 24.156  55.633  1.000 79.570  ? 26  SER GGG N   1 
ATOM 11490 C CA  . SER G 2 26  ? 116.412 23.629  55.924  1.000 73.500  ? 26  SER GGG CA  1 
ATOM 11491 C C   . SER G 2 26  ? 116.446 22.985  57.316  1.000 64.350  ? 26  SER GGG C   1 
ATOM 11492 O O   . SER G 2 26  ? 117.104 21.944  57.471  1.000 50.360  ? 26  SER GGG O   1 
ATOM 11493 C CB  . SER G 2 26  ? 117.450 24.722  55.818  1.000 73.090  ? 26  SER GGG CB  1 
ATOM 11494 O OG  . SER G 2 26  ? 117.681 25.054  54.471  1.000 74.540  ? 26  SER GGG OG  1 
ATOM 11495 N N   . SER G 2 27  ? 115.635 23.507  58.236  1.000 59.490  ? 27  SER GGG N   1 
ATOM 11496 C CA  . SER G 2 27  ? 115.606 23.003  59.634  1.000 61.590  ? 27  SER GGG CA  1 
ATOM 11497 C C   . SER G 2 27  ? 114.979 21.612  59.720  1.000 63.330  ? 27  SER GGG C   1 
ATOM 11498 O O   . SER G 2 27  ? 115.434 20.828  60.558  1.000 63.090  ? 27  SER GGG O   1 
ATOM 11499 C CB  . SER G 2 27  ? 114.884 23.965  60.497  1.000 56.920  ? 27  SER GGG CB  1 
ATOM 11500 O OG  . SER G 2 27  ? 114.212 24.930  59.704  1.000 60.630  ? 27  SER GGG OG  1 
ATOM 11501 N N   . ASN G 2 28  ? 113.979 21.318  58.886  1.000 62.550  ? 28  ASN GGG N   1 
ATOM 11502 C CA  . ASN G 2 28  ? 113.383 19.958  58.885  1.000 55.710  ? 28  ASN GGG CA  1 
ATOM 11503 C C   . ASN G 2 28  ? 113.762 19.149  57.644  1.000 54.200  ? 28  ASN GGG C   1 
ATOM 11504 O O   . ASN G 2 28  ? 114.847 18.567  57.664  1.000 47.790  ? 28  ASN GGG O   1 
ATOM 11505 C CB  . ASN G 2 28  ? 111.887 19.930  59.203  1.000 52.870  ? 28  ASN GGG CB  1 
ATOM 11506 C CG  . ASN G 2 28  ? 111.132 21.200  58.907  1.000 52.900  ? 28  ASN GGG CG  1 
ATOM 11507 O OD1 . ASN G 2 28  ? 110.475 21.761  59.774  1.000 67.400  ? 28  ASN GGG OD1 1 
ATOM 11508 N ND2 . ASN G 2 28  ? 111.157 21.617  57.663  1.000 61.830  ? 28  ASN GGG ND2 1 
ATOM 11509 N N   . ILE G 2 29  ? 112.911 19.111  56.619  1.000 52.510  ? 29  ILE GGG N   1 
ATOM 11510 C CA  . ILE G 2 29  ? 113.141 18.224  55.436  1.000 54.130  ? 29  ILE GGG CA  1 
ATOM 11511 C C   . ILE G 2 29  ? 114.553 18.385  54.875  1.000 55.720  ? 29  ILE GGG C   1 
ATOM 11512 O O   . ILE G 2 29  ? 115.088 17.397  54.354  1.000 61.620  ? 29  ILE GGG O   1 
ATOM 11513 C CB  . ILE G 2 29  ? 112.044 18.436  54.379  1.000 48.890  ? 29  ILE GGG CB  1 
ATOM 11514 C CG1 . ILE G 2 29  ? 110.655 18.480  55.017  1.000 47.560  ? 29  ILE GGG CG1 1 
ATOM 11515 C CG2 . ILE G 2 29  ? 112.119 17.395  53.278  1.000 48.260  ? 29  ILE GGG CG2 1 
ATOM 11516 C CD1 . ILE G 2 29  ? 109.536 18.154  54.063  1.000 45.800  ? 29  ILE GGG CD1 1 
ATOM 11517 N N   . GLY G 2 30  ? 115.148 19.563  55.004  1.000 60.030  ? 30  GLY GGG N   1 
ATOM 11518 C CA  . GLY G 2 30  ? 116.469 19.804  54.400  1.000 63.540  ? 30  GLY GGG CA  1 
ATOM 11519 C C   . GLY G 2 30  ? 117.496 18.836  54.959  1.000 71.510  ? 30  GLY GGG C   1 
ATOM 11520 O O   . GLY G 2 30  ? 118.150 18.124  54.171  1.000 74.040  ? 30  GLY GGG O   1 
ATOM 11521 N N   . SER G 2 31  ? 117.566 18.756  56.288  1.000 73.480  ? 31  SER GGG N   1 
ATOM 11522 C CA  . SER G 2 31  ? 118.611 18.021  57.040  1.000 68.630  ? 31  SER GGG CA  1 
ATOM 11523 C C   . SER G 2 31  ? 118.068 16.741  57.683  1.000 54.010  ? 31  SER GGG C   1 
ATOM 11524 O O   . SER G 2 31  ? 118.913 16.025  58.241  1.000 49.600  ? 31  SER GGG O   1 
ATOM 11525 C CB  . SER G 2 31  ? 119.207 18.905  58.098  1.000 76.330  ? 31  SER GGG CB  1 
ATOM 11526 O OG  . SER G 2 31  ? 119.963 19.955  57.521  1.000 89.140  ? 31  SER GGG OG  1 
ATOM 11527 N N   . ASN G 2 32  ? 116.753 16.464  57.619  1.000 42.740  ? 32  ASN GGG N   1 
ATOM 11528 C CA  . ASN G 2 32  ? 116.149 15.283  58.298  1.000 39.440  ? 32  ASN GGG CA  1 
ATOM 11529 C C   . ASN G 2 32  ? 115.197 14.536  57.364  1.000 36.080  ? 32  ASN GGG C   1 
ATOM 11530 O O   . ASN G 2 32  ? 114.565 15.134  56.495  1.000 34.400  ? 32  ASN GGG O   1 
ATOM 11531 C CB  . ASN G 2 32  ? 115.512 15.675  59.637  1.000 38.770  ? 32  ASN GGG CB  1 
ATOM 11532 C CG  . ASN G 2 32  ? 116.511 16.366  60.545  1.000 35.690  ? 32  ASN GGG CG  1 
ATOM 11533 O OD1 . ASN G 2 32  ? 117.462 15.744  61.023  1.000 30.760  ? 32  ASN GGG OD1 1 
ATOM 11534 N ND2 . ASN G 2 32  ? 116.310 17.653  60.791  1.000 36.170  ? 32  ASN GGG ND2 1 
ATOM 11535 N N   . PRO G 2 33  ? 115.085 13.192  57.506  1.000 35.530  ? 33  PRO GGG N   1 
ATOM 11536 C CA  . PRO G 2 33  ? 114.224 12.379  56.657  1.000 37.350  ? 33  PRO GGG CA  1 
ATOM 11537 C C   . PRO G 2 33  ? 112.736 12.510  57.009  1.000 39.980  ? 33  PRO GGG C   1 
ATOM 11538 O O   . PRO G 2 33  ? 112.405 12.680  58.194  1.000 42.460  ? 33  PRO GGG O   1 
ATOM 11539 C CB  . PRO G 2 33  ? 114.603 10.928  56.985  1.000 37.120  ? 33  PRO GGG CB  1 
ATOM 11540 C CG  . PRO G 2 33  ? 115.822 11.013  57.831  1.000 35.890  ? 33  PRO GGG CG  1 
ATOM 11541 C CD  . PRO G 2 33  ? 115.750 12.360  58.513  1.000 36.280  ? 33  PRO GGG CD  1 
ATOM 11542 N N   . VAL G 2 34  ? 111.888 12.353  55.990  1.000 39.270  ? 34  VAL GGG N   1 
ATOM 11543 C CA  . VAL G 2 34  ? 110.405 12.368  56.107  1.000 36.890  ? 34  VAL GGG CA  1 
ATOM 11544 C C   . VAL G 2 34  ? 109.900 10.934  56.123  1.000 39.080  ? 34  VAL GGG C   1 
ATOM 11545 O O   . VAL G 2 34  ? 110.215 10.189  55.155  1.000 43.710  ? 34  VAL GGG O   1 
ATOM 11546 C CB  . VAL G 2 34  ? 109.788 13.116  54.922  1.000 37.490  ? 34  VAL GGG CB  1 
ATOM 11547 C CG1 . VAL G 2 34  ? 108.269 13.046  54.935  1.000 38.030  ? 34  VAL GGG CG1 1 
ATOM 11548 C CG2 . VAL G 2 34  ? 110.295 14.552  54.863  1.000 38.380  ? 34  VAL GGG CG2 1 
ATOM 11549 N N   . ASN G 2 35  ? 109.135 10.562  57.160  1.000 37.500  ? 35  ASN GGG N   1 
ATOM 11550 C CA  . ASN G 2 35  ? 108.277 9.351   57.120  1.000 35.880  ? 35  ASN GGG CA  1 
ATOM 11551 C C   . ASN G 2 35  ? 106.863 9.803   56.749  1.000 36.660  ? 35  ASN GGG C   1 
ATOM 11552 O O   . ASN G 2 35  ? 106.447 10.904  57.173  1.000 35.470  ? 35  ASN GGG O   1 
ATOM 11553 C CB  . ASN G 2 35  ? 108.296 8.551   58.425  1.000 35.840  ? 35  ASN GGG CB  1 
ATOM 11554 C CG  . ASN G 2 35  ? 109.652 7.955   58.755  1.000 38.280  ? 35  ASN GGG CG  1 
ATOM 11555 O OD1 . ASN G 2 35  ? 110.686 8.523   58.396  1.000 40.970  ? 35  ASN GGG OD1 1 
ATOM 11556 N ND2 . ASN G 2 35  ? 109.658 6.837   59.471  1.000 35.950  ? 35  ASN GGG ND2 1 
ATOM 11557 N N   . TRP G 2 36  ? 106.162 8.974   55.973  1.000 36.610  ? 36  TRP GGG N   1 
ATOM 11558 C CA  . TRP G 2 36  ? 104.707 9.085   55.689  1.000 36.080  ? 36  TRP GGG CA  1 
ATOM 11559 C C   . TRP G 2 36  ? 103.961 8.038   56.518  1.000 34.040  ? 36  TRP GGG C   1 
ATOM 11560 O O   . TRP G 2 36  ? 104.419 6.880   56.553  1.000 33.450  ? 36  TRP GGG O   1 
ATOM 11561 C CB  . TRP G 2 36  ? 104.447 8.884   54.196  1.000 38.170  ? 36  TRP GGG CB  1 
ATOM 11562 C CG  . TRP G 2 36  ? 104.903 10.016  53.337  1.000 35.690  ? 36  TRP GGG CG  1 
ATOM 11563 C CD1 . TRP G 2 36  ? 106.109 10.159  52.722  1.000 36.840  ? 36  TRP GGG CD1 1 
ATOM 11564 C CD2 . TRP G 2 36  ? 104.117 11.148  52.959  1.000 36.120  ? 36  TRP GGG CD2 1 
ATOM 11565 N NE1 . TRP G 2 36  ? 106.142 11.328  52.013  1.000 38.470  ? 36  TRP GGG NE1 1 
ATOM 11566 C CE2 . TRP G 2 36  ? 104.934 11.964  52.141  1.000 39.420  ? 36  TRP GGG CE2 1 
ATOM 11567 C CE3 . TRP G 2 36  ? 102.824 11.578  53.274  1.000 35.350  ? 36  TRP GGG CE3 1 
ATOM 11568 C CZ2 . TRP G 2 36  ? 104.492 13.181  51.623  1.000 38.220  ? 36  TRP GGG CZ2 1 
ATOM 11569 C CZ3 . TRP G 2 36  ? 102.391 12.789  52.786  1.000 37.670  ? 36  TRP GGG CZ3 1 
ATOM 11570 C CH2 . TRP G 2 36  ? 103.204 13.569  51.958  1.000 38.410  ? 36  TRP GGG CH2 1 
ATOM 11571 N N   . PHE G 2 37  ? 102.851 8.425   57.139  1.000 34.380  ? 37  PHE GGG N   1 
ATOM 11572 C CA  . PHE G 2 37  ? 101.971 7.500   57.899  1.000 37.500  ? 37  PHE GGG CA  1 
ATOM 11573 C C   . PHE G 2 37  ? 100.592 7.490   57.248  1.000 36.790  ? 37  PHE GGG C   1 
ATOM 11574 O O   . PHE G 2 37  ? 100.097 8.569   56.867  1.000 35.870  ? 37  PHE GGG O   1 
ATOM 11575 C CB  . PHE G 2 37  ? 101.920 7.881   59.383  1.000 38.150  ? 37  PHE GGG CB  1 
ATOM 11576 C CG  . PHE G 2 37  ? 103.278 7.955   60.027  1.000 36.740  ? 37  PHE GGG CG  1 
ATOM 11577 C CD1 . PHE G 2 37  ? 104.051 9.085   59.901  1.000 36.430  ? 37  PHE GGG CD1 1 
ATOM 11578 C CD2 . PHE G 2 37  ? 103.819 6.861   60.687  1.000 37.300  ? 37  PHE GGG CD2 1 
ATOM 11579 C CE1 . PHE G 2 37  ? 105.301 9.153   60.496  1.000 36.780  ? 37  PHE GGG CE1 1 
ATOM 11580 C CE2 . PHE G 2 37  ? 105.086 6.916   61.246  1.000 35.030  ? 37  PHE GGG CE2 1 
ATOM 11581 C CZ  . PHE G 2 37  ? 105.826 8.061   61.145  1.000 35.310  ? 37  PHE GGG CZ  1 
ATOM 11582 N N   . GLN G 2 38  ? 100.026 6.293   57.098  1.000 38.930  ? 38  GLN GGG N   1 
ATOM 11583 C CA  . GLN G 2 38  ? 98.656  6.056   56.561  1.000 40.490  ? 38  GLN GGG CA  1 
ATOM 11584 C C   . GLN G 2 38  ? 97.765  5.841   57.782  1.000 41.370  ? 38  GLN GGG C   1 
ATOM 11585 O O   . GLN G 2 38  ? 98.217  5.126   58.681  1.000 38.800  ? 38  GLN GGG O   1 
ATOM 11586 C CB  . GLN G 2 38  ? 98.679  4.891   55.566  1.000 40.560  ? 38  GLN GGG CB  1 
ATOM 11587 C CG  . GLN G 2 38  ? 97.357  4.184   55.308  1.000 43.750  ? 38  GLN GGG CG  1 
ATOM 11588 C CD  . GLN G 2 38  ? 97.454  3.243   54.142  1.000 45.220  ? 38  GLN GGG CD  1 
ATOM 11589 O OE1 . GLN G 2 38  ? 97.522  3.699   53.000  1.000 49.590  ? 38  GLN GGG OE1 1 
ATOM 11590 N NE2 . GLN G 2 38  ? 97.516  1.938   54.426  1.000 43.730  ? 38  GLN GGG NE2 1 
ATOM 11591 N N   . GLN G 2 39  ? 96.575  6.445   57.803  1.000 44.020  ? 39  GLN GGG N   1 
ATOM 11592 C CA  . GLN G 2 39  ? 95.614  6.350   58.936  1.000 46.930  ? 39  GLN GGG CA  1 
ATOM 11593 C C   . GLN G 2 39  ? 94.203  6.153   58.393  1.000 48.100  ? 39  GLN GGG C   1 
ATOM 11594 O O   . GLN G 2 39  ? 93.660  7.098   57.753  1.000 46.180  ? 39  GLN GGG O   1 
ATOM 11595 C CB  . GLN G 2 39  ? 95.662  7.589   59.841  1.000 51.380  ? 39  GLN GGG CB  1 
ATOM 11596 C CG  . GLN G 2 39  ? 94.921  7.409   61.174  1.000 51.000  ? 39  GLN GGG CG  1 
ATOM 11597 C CD  . GLN G 2 39  ? 95.033  8.600   62.087  1.000 48.190  ? 39  GLN GGG CD  1 
ATOM 11598 O OE1 . GLN G 2 39  ? 95.254  9.729   61.653  1.000 41.890  ? 39  GLN GGG OE1 1 
ATOM 11599 N NE2 . GLN G 2 39  ? 94.937  8.329   63.382  1.000 53.070  ? 39  GLN GGG NE2 1 
ATOM 11600 N N   . PHE G 2 40  ? 93.640  4.977   58.677  1.000 53.200  ? 40  PHE GGG N   1 
ATOM 11601 C CA  . PHE G 2 40  ? 92.205  4.676   58.443  1.000 59.130  ? 40  PHE GGG CA  1 
ATOM 11602 C C   . PHE G 2 40  ? 91.422  5.149   59.657  1.000 64.520  ? 40  PHE GGG C   1 
ATOM 11603 O O   . PHE G 2 40  ? 91.903  4.986   60.769  1.000 69.310  ? 40  PHE GGG O   1 
ATOM 11604 C CB  . PHE G 2 40  ? 91.988  3.184   58.181  1.000 50.490  ? 40  PHE GGG CB  1 
ATOM 11605 C CG  . PHE G 2 40  ? 92.813  2.679   57.034  1.000 43.640  ? 40  PHE GGG CG  1 
ATOM 11606 C CD1 . PHE G 2 40  ? 92.703  3.293   55.798  1.000 42.460  ? 40  PHE GGG CD1 1 
ATOM 11607 C CD2 . PHE G 2 40  ? 93.710  1.637   57.185  1.000 41.170  ? 40  PHE GGG CD2 1 
ATOM 11608 C CE1 . PHE G 2 40  ? 93.475  2.886   54.729  1.000 43.060  ? 40  PHE GGG CE1 1 
ATOM 11609 C CE2 . PHE G 2 40  ? 94.488  1.230   56.111  1.000 43.790  ? 40  PHE GGG CE2 1 
ATOM 11610 C CZ  . PHE G 2 40  ? 94.337  1.830   54.875  1.000 44.750  ? 40  PHE GGG CZ  1 
ATOM 11611 N N   . PRO G 2 41  ? 90.227  5.755   59.463  1.000 70.670  ? 41  PRO GGG N   1 
ATOM 11612 C CA  . PRO G 2 41  ? 89.373  6.188   60.573  1.000 68.500  ? 41  PRO GGG CA  1 
ATOM 11613 C C   . PRO G 2 41  ? 89.307  5.176   61.726  1.000 61.590  ? 41  PRO GGG C   1 
ATOM 11614 O O   . PRO G 2 41  ? 89.203  3.988   61.475  1.000 47.580  ? 41  PRO GGG O   1 
ATOM 11615 C CB  . PRO G 2 41  ? 88.001  6.306   59.908  1.000 71.730  ? 41  PRO GGG CB  1 
ATOM 11616 C CG  . PRO G 2 41  ? 88.324  6.742   58.493  1.000 73.640  ? 41  PRO GGG CG  1 
ATOM 11617 C CD  . PRO G 2 41  ? 89.640  6.071   58.149  1.000 73.800  ? 41  PRO GGG CD  1 
ATOM 11618 N N   . GLY G 2 42  ? 89.447  5.681   62.950  1.000 58.430  ? 42  GLY GGG N   1 
ATOM 11619 C CA  . GLY G 2 42  ? 89.275  4.916   64.198  1.000 58.820  ? 42  GLY GGG CA  1 
ATOM 11620 C C   . GLY G 2 42  ? 90.391  3.910   64.440  1.000 59.670  ? 42  GLY GGG C   1 
ATOM 11621 O O   . GLY G 2 42  ? 90.250  3.146   65.397  1.000 63.030  ? 42  GLY GGG O   1 
ATOM 11622 N N   . THR G 2 43  ? 91.455  3.887   63.631  1.000 60.340  ? 43  THR GGG N   1 
ATOM 11623 C CA  . THR G 2 43  ? 92.704  3.130   63.929  1.000 59.530  ? 43  THR GGG CA  1 
ATOM 11624 C C   . THR G 2 43  ? 93.863  4.127   64.114  1.000 63.070  ? 43  THR GGG C   1 
ATOM 11625 O O   . THR G 2 43  ? 93.700  5.360   63.838  1.000 46.320  ? 43  THR GGG O   1 
ATOM 11626 C CB  . THR G 2 43  ? 93.020  2.048   62.879  1.000 49.180  ? 43  THR GGG CB  1 
ATOM 11627 O OG1 . THR G 2 43  ? 93.012  2.627   61.579  1.000 45.150  ? 43  THR GGG OG1 1 
ATOM 11628 N N   . ALA G 2 44  ? 94.996  3.601   64.574  1.000 66.170  ? 44  ALA GGG N   1 
ATOM 11629 C CA  . ALA G 2 44  ? 96.257  4.345   64.745  1.000 64.130  ? 44  ALA GGG CA  1 
ATOM 11630 C C   . ALA G 2 44  ? 96.817  4.701   63.374  1.000 53.370  ? 44  ALA GGG C   1 
ATOM 11631 O O   . ALA G 2 44  ? 96.461  4.066   62.395  1.000 55.720  ? 44  ALA GGG O   1 
ATOM 11632 C CB  . ALA G 2 44  ? 97.225  3.488   65.529  1.000 70.300  ? 44  ALA GGG CB  1 
ATOM 11633 N N   . PRO G 2 45  ? 97.733  5.691   63.279  1.000 46.370  ? 45  PRO GGG N   1 
ATOM 11634 C CA  . PRO G 2 45  ? 98.620  5.833   62.118  1.000 43.900  ? 45  PRO GGG CA  1 
ATOM 11635 C C   . PRO G 2 45  ? 99.519  4.599   62.004  1.000 44.790  ? 45  PRO GGG C   1 
ATOM 11636 O O   . PRO G 2 45  ? 99.756  3.962   62.998  1.000 51.310  ? 45  PRO GGG O   1 
ATOM 11637 C CB  . PRO G 2 45  ? 99.486  7.059   62.418  1.000 45.190  ? 45  PRO GGG CB  1 
ATOM 11638 C CG  . PRO G 2 45  ? 98.748  7.784   63.534  1.000 46.980  ? 45  PRO GGG CG  1 
ATOM 11639 C CD  . PRO G 2 45  ? 98.012  6.706   64.302  1.000 46.900  ? 45  PRO GGG CD  1 
ATOM 11640 N N   . LYS G 2 46  ? 99.971  4.287   60.797  1.000 43.680  ? 46  LYS GGG N   1 
ATOM 11641 C CA  . LYS G 2 46  ? 100.931 3.186   60.521  1.000 39.600  ? 46  LYS GGG CA  1 
ATOM 11642 C C   . LYS G 2 46  ? 101.956 3.718   59.516  1.000 35.700  ? 46  LYS GGG C   1 
ATOM 11643 O O   . LYS G 2 46  ? 101.610 4.596   58.700  1.000 29.580  ? 46  LYS GGG O   1 
ATOM 11644 C CB  . LYS G 2 46  ? 100.197 1.946   60.008  1.000 43.170  ? 46  LYS GGG CB  1 
ATOM 11645 C CG  . LYS G 2 46  ? 101.087 0.724   59.790  1.000 47.570  ? 46  LYS GGG CG  1 
ATOM 11646 C CD  . LYS G 2 46  ? 100.400 -0.490  59.148  1.000 48.580  ? 46  LYS GGG CD  1 
ATOM 11647 C CE  . LYS G 2 46  ? 99.712  -1.421  60.133  1.000 49.610  ? 46  LYS GGG CE  1 
ATOM 11648 N NZ  . LYS G 2 46  ? 99.873  -2.841  59.750  1.000 51.480  ? 46  LYS GGG NZ  1 
ATOM 11649 N N   . LEU G 2 47  ? 103.184 3.228   59.612  1.000 35.310  ? 47  LEU GGG N   1 
ATOM 11650 C CA  . LEU G 2 47  ? 104.285 3.571   58.690  1.000 32.960  ? 47  LEU GGG CA  1 
ATOM 11651 C C   . LEU G 2 47  ? 103.925 3.116   57.275  1.000 32.820  ? 47  LEU GGG C   1 
ATOM 11652 O O   . LEU G 2 47  ? 103.640 1.918   57.088  1.000 29.690  ? 47  LEU GGG O   1 
ATOM 11653 C CB  . LEU G 2 47  ? 105.565 2.885   59.170  1.000 32.440  ? 47  LEU GGG CB  1 
ATOM 11654 C CG  . LEU G 2 47  ? 106.820 3.244   58.391  1.000 31.710  ? 47  LEU GGG CG  1 
ATOM 11655 C CD1 . LEU G 2 47  ? 107.061 4.726   58.474  1.000 33.740  ? 47  LEU GGG CD1 1 
ATOM 11656 C CD2 . LEU G 2 47  ? 108.024 2.512   58.946  1.000 31.140  ? 47  LEU GGG CD2 1 
ATOM 11657 N N   . LEU G 2 48  ? 103.953 4.055   56.328  1.000 34.850  ? 48  LEU GGG N   1 
ATOM 11658 C CA  . LEU G 2 48  ? 103.698 3.817   54.887  1.000 35.410  ? 48  LEU GGG CA  1 
ATOM 11659 C C   . LEU G 2 48  ? 105.017 3.957   54.115  1.000 38.230  ? 48  LEU GGG C   1 
ATOM 11660 O O   . LEU G 2 48  ? 105.410 3.013   53.406  1.000 40.020  ? 48  LEU GGG O   1 
ATOM 11661 C CB  . LEU G 2 48  ? 102.667 4.831   54.403  1.000 33.030  ? 48  LEU GGG CB  1 
ATOM 11662 C CG  . LEU G 2 48  ? 102.249 4.662   52.950  1.000 35.180  ? 48  LEU GGG CG  1 
ATOM 11663 C CD1 . LEU G 2 48  ? 101.465 3.381   52.778  1.000 34.340  ? 48  LEU GGG CD1 1 
ATOM 11664 C CD2 . LEU G 2 48  ? 101.444 5.851   52.462  1.000 36.840  ? 48  LEU GGG CD2 1 
ATOM 11665 N N   . ILE G 2 49  ? 105.669 5.109   54.244  1.000 39.160  ? 49  ILE GGG N   1 
ATOM 11666 C CA  . ILE G 2 49  ? 107.015 5.388   53.669  1.000 39.270  ? 49  ILE GGG CA  1 
ATOM 11667 C C   . ILE G 2 49  ? 107.918 5.858   54.804  1.000 36.050  ? 49  ILE GGG C   1 
ATOM 11668 O O   . ILE G 2 49  ? 107.419 6.617   55.635  1.000 33.990  ? 49  ILE GGG O   1 
ATOM 11669 C CB  . ILE G 2 49  ? 106.930 6.450   52.556  1.000 39.080  ? 49  ILE GGG CB  1 
ATOM 11670 C CG1 . ILE G 2 49  ? 106.070 5.978   51.387  1.000 40.450  ? 49  ILE GGG CG1 1 
ATOM 11671 C CG2 . ILE G 2 49  ? 108.319 6.874   52.103  1.000 36.090  ? 49  ILE GGG CG2 1 
ATOM 11672 C CD1 . ILE G 2 49  ? 106.663 4.812   50.625  1.000 39.360  ? 49  ILE GGG CD1 1 
ATOM 11673 N N   . TYR G 2 50  ? 109.181 5.427   54.817  1.000 32.700  ? 50  TYR GGG N   1 
ATOM 11674 C CA  . TYR G 2 50  ? 110.234 5.966   55.713  1.000 31.930  ? 50  TYR GGG CA  1 
ATOM 11675 C C   . TYR G 2 50  ? 111.433 6.442   54.893  1.000 30.440  ? 50  TYR GGG C   1 
ATOM 11676 O O   . TYR G 2 50  ? 111.603 6.046   53.734  1.000 33.200  ? 50  TYR GGG O   1 
ATOM 11677 C CB  . TYR G 2 50  ? 110.651 4.924   56.745  1.000 33.530  ? 50  TYR GGG CB  1 
ATOM 11678 C CG  . TYR G 2 50  ? 111.447 3.759   56.220  1.000 35.750  ? 50  TYR GGG CG  1 
ATOM 11679 C CD1 . TYR G 2 50  ? 112.817 3.834   56.083  1.000 37.550  ? 50  TYR GGG CD1 1 
ATOM 11680 C CD2 . TYR G 2 50  ? 110.832 2.552   55.909  1.000 36.480  ? 50  TYR GGG CD2 1 
ATOM 11681 C CE1 . TYR G 2 50  ? 113.561 2.753   55.637  1.000 39.630  ? 50  TYR GGG CE1 1 
ATOM 11682 C CE2 . TYR G 2 50  ? 111.554 1.461   55.462  1.000 36.700  ? 50  TYR GGG CE2 1 
ATOM 11683 C CZ  . TYR G 2 50  ? 112.931 1.559   55.325  1.000 40.000  ? 50  TYR GGG CZ  1 
ATOM 11684 O OH  . TYR G 2 50  ? 113.703 0.516   54.883  1.000 39.860  ? 50  TYR GGG OH  1 
ATOM 11685 N N   . ALA G 2 51  ? 112.251 7.302   55.490  1.000 29.320  ? 51  ALA GGG N   1 
ATOM 11686 C CA  . ALA G 2 51  ? 113.486 7.830   54.871  1.000 30.800  ? 51  ALA GGG CA  1 
ATOM 11687 C C   . ALA G 2 51  ? 113.169 8.352   53.461  1.000 31.610  ? 51  ALA GGG C   1 
ATOM 11688 O O   . ALA G 2 51  ? 113.928 8.045   52.518  1.000 29.640  ? 51  ALA GGG O   1 
ATOM 11689 C CB  . ALA G 2 51  ? 114.563 6.766   54.858  1.000 30.230  ? 51  ALA GGG CB  1 
ATOM 11690 N N   . ASN G 2 52  ? 112.069 9.100   53.336  1.000 32.930  ? 52  ASN GGG N   1 
ATOM 11691 C CA  . ASN G 2 52  ? 111.708 9.891   52.127  1.000 35.670  ? 52  ASN GGG CA  1 
ATOM 11692 C C   . ASN G 2 52  ? 111.097 8.997   51.045  1.000 36.240  ? 52  ASN GGG C   1 
ATOM 11693 O O   . ASN G 2 52  ? 110.068 9.484   50.439  1.000 34.860  ? 52  ASN GGG O   1 
ATOM 11694 C CB  . ASN G 2 52  ? 112.907 10.661  51.548  1.000 32.880  ? 52  ASN GGG CB  1 
ATOM 11695 C CG  . ASN G 2 52  ? 113.576 11.529  52.581  1.000 33.180  ? 52  ASN GGG CG  1 
ATOM 11696 O OD1 . ASN G 2 52  ? 112.975 12.490  53.090  1.000 33.710  ? 52  ASN GGG OD1 1 
ATOM 11697 N ND2 . ASN G 2 52  ? 114.840 11.223  52.849  1.000 30.910  ? 52  ASN GGG ND2 1 
ATOM 11698 N N   . THR G 2 53  ? 111.670 7.795   50.816  1.000 33.000  ? 53  THR GGG N   1 
ATOM 11699 C CA  . THR G 2 53  ? 111.518 7.019   49.554  1.000 34.350  ? 53  THR GGG CA  1 
ATOM 11700 C C   . THR G 2 53  ? 111.503 5.500   49.759  1.000 36.840  ? 53  THR GGG C   1 
ATOM 11701 O O   . THR G 2 53  ? 111.541 4.809   48.745  1.000 34.780  ? 53  THR GGG O   1 
ATOM 11702 C CB  . THR G 2 53  ? 112.668 7.324   48.584  1.000 36.970  ? 53  THR GGG CB  1 
ATOM 11703 O OG1 . THR G 2 53  ? 113.960 7.106   49.161  1.000 38.210  ? 53  THR GGG OG1 1 
ATOM 11704 C CG2 . THR G 2 53  ? 112.636 8.750   48.081  1.000 42.990  ? 53  THR GGG CG2 1 
ATOM 11705 N N   . GLN G 2 54  ? 111.432 4.974   50.981  1.000 43.580  ? 54  GLN GGG N   1 
ATOM 11706 C CA  . GLN G 2 54  ? 111.588 3.514   51.234  1.000 45.080  ? 54  GLN GGG CA  1 
ATOM 11707 C C   . GLN G 2 54  ? 110.266 2.929   51.763  1.000 46.930  ? 54  GLN GGG C   1 
ATOM 11708 O O   . GLN G 2 54  ? 109.606 3.598   52.576  1.000 53.280  ? 54  GLN GGG O   1 
ATOM 11709 C CB  . GLN G 2 54  ? 112.700 3.297   52.245  1.000 45.530  ? 54  GLN GGG CB  1 
ATOM 11710 C CG  . GLN G 2 54  ? 113.978 4.009   51.833  1.000 45.890  ? 54  GLN GGG CG  1 
ATOM 11711 C CD  . GLN G 2 54  ? 114.561 3.341   50.612  1.000 47.410  ? 54  GLN GGG CD  1 
ATOM 11712 O OE1 . GLN G 2 54  ? 114.797 2.131   50.606  1.000 41.560  ? 54  GLN GGG OE1 1 
ATOM 11713 N NE2 . GLN G 2 54  ? 114.736 4.131   49.561  1.000 51.110  ? 54  GLN GGG NE2 1 
ATOM 11714 N N   . ARG G 2 55  ? 109.940 1.711   51.337  1.000 47.300  ? 55  ARG GGG N   1 
ATOM 11715 C CA  . ARG G 2 55  ? 108.703 0.990   51.769  1.000 51.640  ? 55  ARG GGG CA  1 
ATOM 11716 C C   . ARG G 2 55  ? 109.067 -0.068  52.792  1.000 47.830  ? 55  ARG GGG C   1 
ATOM 11717 O O   . ARG G 2 55  ? 110.005 -0.819  52.599  1.000 50.160  ? 55  ARG GGG O   1 
ATOM 11718 C CB  . ARG G 2 55  ? 108.020 0.340   50.573  1.000 60.370  ? 55  ARG GGG CB  1 
ATOM 11719 C CG  . ARG G 2 55  ? 107.296 1.350   49.692  1.000 67.600  ? 55  ARG GGG CG  1 
ATOM 11720 C CD  . ARG G 2 55  ? 106.484 0.708   48.591  1.000 73.750  ? 55  ARG GGG CD  1 
ATOM 11721 N NE  . ARG G 2 55  ? 107.266 -0.281  47.848  1.000 75.950  ? 55  ARG GGG NE  1 
ATOM 11722 C CZ  . ARG G 2 55  ? 108.083 -0.013  46.833  1.000 65.690  ? 55  ARG GGG CZ  1 
ATOM 11723 N NH1 . ARG G 2 55  ? 108.263 1.232   46.405  1.000 56.510  ? 55  ARG GGG NH1 1 
ATOM 11724 N NH2 . ARG G 2 55  ? 108.716 -1.013  46.251  1.000 64.510  ? 55  ARG GGG NH2 1 
ATOM 11725 N N   . PRO G 2 56  ? 108.355 -0.163  53.925  1.000 51.960  ? 56  PRO GGG N   1 
ATOM 11726 C CA  . PRO G 2 56  ? 108.536 -1.300  54.824  1.000 58.720  ? 56  PRO GGG CA  1 
ATOM 11727 C C   . PRO G 2 56  ? 107.880 -2.508  54.143  1.000 64.010  ? 56  PRO GGG C   1 
ATOM 11728 O O   . PRO G 2 56  ? 107.098 -2.285  53.239  1.000 67.060  ? 56  PRO GGG O   1 
ATOM 11729 C CB  . PRO G 2 56  ? 107.838 -0.847  56.113  1.000 55.440  ? 56  PRO GGG CB  1 
ATOM 11730 C CG  . PRO G 2 56  ? 106.789 0.154   55.651  1.000 54.080  ? 56  PRO GGG CG  1 
ATOM 11731 C CD  . PRO G 2 56  ? 107.343 0.788   54.392  1.000 50.360  ? 56  PRO GGG CD  1 
ATOM 11732 N N   . SER G 2 57  ? 108.203 -3.733  54.555  1.000 65.320  ? 57  SER GGG N   1 
ATOM 11733 C CA  . SER G 2 57  ? 107.509 -4.955  54.069  1.000 65.250  ? 57  SER GGG CA  1 
ATOM 11734 C C   . SER G 2 57  ? 106.007 -4.819  54.356  1.000 63.780  ? 57  SER GGG C   1 
ATOM 11735 O O   . SER G 2 57  ? 105.644 -4.421  55.479  1.000 63.050  ? 57  SER GGG O   1 
ATOM 11736 C CB  . SER G 2 57  ? 108.092 -6.217  54.680  1.000 67.880  ? 57  SER GGG CB  1 
ATOM 11737 O OG  . SER G 2 57  ? 107.230 -7.342  54.526  1.000 63.760  ? 57  SER GGG OG  1 
ATOM 11738 N N   . GLY G 2 58  ? 105.171 -5.088  53.354  1.000 66.810  ? 58  GLY GGG N   1 
ATOM 11739 C CA  . GLY G 2 58  ? 103.704 -5.022  53.468  1.000 67.970  ? 58  GLY GGG CA  1 
ATOM 11740 C C   . GLY G 2 58  ? 103.123 -3.909  52.619  1.000 67.130  ? 58  GLY GGG C   1 
ATOM 11741 O O   . GLY G 2 58  ? 101.897 -3.957  52.390  1.000 78.580  ? 58  GLY GGG O   1 
ATOM 11742 N N   . VAL G 2 59  ? 103.934 -2.932  52.204  1.000 56.210  ? 59  VAL GGG N   1 
ATOM 11743 C CA  . VAL G 2 59  ? 103.462 -1.765  51.411  1.000 54.720  ? 59  VAL GGG CA  1 
ATOM 11744 C C   . VAL G 2 59  ? 103.714 -2.050  49.935  1.000 58.140  ? 59  VAL GGG C   1 
ATOM 11745 O O   . VAL G 2 59  ? 104.850 -2.232  49.504  1.000 54.560  ? 59  VAL GGG O   1 
ATOM 11746 C CB  . VAL G 2 59  ? 104.095 -0.440  51.857  1.000 51.000  ? 59  VAL GGG CB  1 
ATOM 11747 C CG1 . VAL G 2 59  ? 103.602 0.744   51.039  1.000 51.140  ? 59  VAL GGG CG1 1 
ATOM 11748 C CG2 . VAL G 2 59  ? 103.868 -0.186  53.336  1.000 46.590  ? 59  VAL GGG CG2 1 
ATOM 11749 N N   . PRO G 2 60  ? 102.636 -2.113  49.127  1.000 66.700  ? 60  PRO GGG N   1 
ATOM 11750 C CA  . PRO G 2 60  ? 102.760 -2.308  47.684  1.000 72.810  ? 60  PRO GGG CA  1 
ATOM 11751 C C   . PRO G 2 60  ? 103.705 -1.356  46.934  1.000 66.240  ? 60  PRO GGG C   1 
ATOM 11752 O O   . PRO G 2 60  ? 103.833 -0.218  47.311  1.000 55.620  ? 60  PRO GGG O   1 
ATOM 11753 C CB  . PRO G 2 60  ? 101.321 -2.050  47.197  1.000 78.260  ? 60  PRO GGG CB  1 
ATOM 11754 C CG  . PRO G 2 60  ? 100.444 -2.484  48.361  1.000 70.860  ? 60  PRO GGG CG  1 
ATOM 11755 C CD  . PRO G 2 60  ? 101.233 -2.056  49.575  1.000 66.450  ? 60  PRO GGG CD  1 
ATOM 11756 N N   . ASP G 2 61  ? 104.296 -1.869  45.850  1.000 69.940  ? 61  ASP GGG N   1 
ATOM 11757 C CA  . ASP G 2 61  ? 105.045 -1.154  44.775  1.000 76.640  ? 61  ASP GGG CA  1 
ATOM 11758 C C   . ASP G 2 61  ? 104.399 0.195   44.416  1.000 68.640  ? 61  ASP GGG C   1 
ATOM 11759 O O   . ASP G 2 61  ? 105.128 1.124   44.047  1.000 62.280  ? 61  ASP GGG O   1 
ATOM 11760 C CB  . ASP G 2 61  ? 104.959 -1.969  43.473  1.000 87.210  ? 61  ASP GGG CB  1 
ATOM 11761 N N   . ARG G 2 62  ? 103.066 0.246   44.424  1.000 68.990  ? 62  ARG GGG N   1 
ATOM 11762 C CA  . ARG G 2 62  ? 102.241 1.388   43.947  1.000 78.670  ? 62  ARG GGG CA  1 
ATOM 11763 C C   . ARG G 2 62  ? 102.664 2.669   44.669  1.000 81.090  ? 62  ARG GGG C   1 
ATOM 11764 O O   . ARG G 2 62  ? 102.844 3.717   43.988  1.000 85.720  ? 62  ARG GGG O   1 
ATOM 11765 C CB  . ARG G 2 62  ? 100.757 1.118   44.214  1.000 81.800  ? 62  ARG GGG CB  1 
ATOM 11766 C CG  . ARG G 2 62  ? 100.301 -0.298  43.882  1.000 82.730  ? 62  ARG GGG CG  1 
ATOM 11767 C CD  . ARG G 2 62  ? 98.798  -0.489  43.982  1.000 78.320  ? 62  ARG GGG CD  1 
ATOM 11768 N NE  . ARG G 2 62  ? 98.132  0.411   44.919  1.000 66.770  ? 62  ARG GGG NE  1 
ATOM 11769 C CZ  . ARG G 2 62  ? 97.432  0.030   45.981  1.000 64.870  ? 62  ARG GGG CZ  1 
ATOM 11770 N NH1 . ARG G 2 62  ? 97.305  -1.244  46.319  1.000 73.620  ? 62  ARG GGG NH1 1 
ATOM 11771 N NH2 . ARG G 2 62  ? 96.878  0.948   46.742  1.000 56.910  ? 62  ARG GGG NH2 1 
ATOM 11772 N N   . PHE G 2 63  ? 102.811 2.571   45.999  1.000 73.780  ? 63  PHE GGG N   1 
ATOM 11773 C CA  . PHE G 2 63  ? 103.238 3.671   46.903  1.000 57.510  ? 63  PHE GGG CA  1 
ATOM 11774 C C   . PHE G 2 63  ? 104.725 3.974   46.694  1.000 57.430  ? 63  PHE GGG C   1 
ATOM 11775 O O   . PHE G 2 63  ? 105.581 3.063   46.769  1.000 60.660  ? 63  PHE GGG O   1 
ATOM 11776 C CB  . PHE G 2 63  ? 102.978 3.274   48.352  1.000 49.640  ? 63  PHE GGG CB  1 
ATOM 11777 C CG  . PHE G 2 63  ? 101.526 3.103   48.699  1.000 42.730  ? 63  PHE GGG CG  1 
ATOM 11778 C CD1 . PHE G 2 63  ? 100.749 4.202   49.013  1.000 41.230  ? 63  PHE GGG CD1 1 
ATOM 11779 C CD2 . PHE G 2 63  ? 100.944 1.852   48.727  1.000 37.830  ? 63  PHE GGG CD2 1 
ATOM 11780 C CE1 . PHE G 2 63  ? 99.411  4.064   49.347  1.000 38.440  ? 63  PHE GGG CE1 1 
ATOM 11781 C CE2 . PHE G 2 63  ? 99.614  1.710   49.087  1.000 39.420  ? 63  PHE GGG CE2 1 
ATOM 11782 C CZ  . PHE G 2 63  ? 98.853  2.814   49.407  1.000 39.570  ? 63  PHE GGG CZ  1 
ATOM 11783 N N   . SER G 2 64  ? 105.034 5.238   46.435  1.000 56.220  ? 64  SER GGG N   1 
ATOM 11784 C CA  . SER G 2 64  ? 106.406 5.694   46.107  1.000 56.710  ? 64  SER GGG CA  1 
ATOM 11785 C C   . SER G 2 64  ? 106.583 7.141   46.566  1.000 58.590  ? 64  SER GGG C   1 
ATOM 11786 O O   . SER G 2 64  ? 105.571 7.832   46.781  1.000 56.910  ? 64  SER GGG O   1 
ATOM 11787 C CB  . SER G 2 64  ? 106.653 5.580   44.646  1.000 57.580  ? 64  SER GGG CB  1 
ATOM 11788 O OG  . SER G 2 64  ? 106.120 6.729   43.993  1.000 62.480  ? 64  SER GGG OG  1 
ATOM 11789 N N   . GLY G 2 65  ? 107.830 7.572   46.701  1.000 58.790  ? 65  GLY GGG N   1 
ATOM 11790 C CA  . GLY G 2 65  ? 108.163 8.926   47.187  1.000 59.970  ? 65  GLY GGG CA  1 
ATOM 11791 C C   . GLY G 2 65  ? 109.267 9.537   46.358  1.000 55.280  ? 65  GLY GGG C   1 
ATOM 11792 O O   . GLY G 2 65  ? 110.012 8.779   45.729  1.000 52.660  ? 65  GLY GGG O   1 
ATOM 11793 N N   . SER G 2 66  ? 109.310 10.867  46.315  1.000 52.950  ? 66  SER GGG N   1 
ATOM 11794 C CA  . SER G 2 66  ? 110.426 11.635  45.725  1.000 59.430  ? 66  SER GGG CA  1 
ATOM 11795 C C   . SER G 2 66  ? 110.800 12.759  46.697  1.000 67.310  ? 66  SER GGG C   1 
ATOM 11796 O O   . SER G 2 66  ? 109.880 13.333  47.328  1.000 58.170  ? 66  SER GGG O   1 
ATOM 11797 C CB  . SER G 2 66  ? 110.045 12.150  44.379  1.000 62.080  ? 66  SER GGG CB  1 
ATOM 11798 O OG  . SER G 2 66  ? 109.350 13.382  44.488  1.000 70.390  ? 66  SER GGG OG  1 
ATOM 11799 N N   . LYS G 2 67  ? 112.107 12.994  46.843  1.000 70.730  ? 67  LYS GGG N   1 
ATOM 11800 C CA  . LYS G 2 67  ? 112.688 14.094  47.651  1.000 73.730  ? 67  LYS GGG CA  1 
ATOM 11801 C C   . LYS G 2 67  ? 113.419 15.023  46.686  1.000 81.120  ? 67  LYS GGG C   1 
ATOM 11802 O O   . LYS G 2 67  ? 114.223 14.520  45.878  1.000 77.550  ? 67  LYS GGG O   1 
ATOM 11803 C CB  . LYS G 2 67  ? 113.660 13.574  48.720  1.000 75.760  ? 67  LYS GGG CB  1 
ATOM 11804 C CG  . LYS G 2 67  ? 114.254 14.638  49.646  1.000 76.870  ? 67  LYS GGG CG  1 
ATOM 11805 C CD  . LYS G 2 67  ? 115.525 14.171  50.367  1.000 72.060  ? 67  LYS GGG CD  1 
ATOM 11806 C CE  . LYS G 2 67  ? 116.499 15.262  50.769  1.000 72.500  ? 67  LYS GGG CE  1 
ATOM 11807 N NZ  . LYS G 2 67  ? 115.905 16.374  51.572  1.000 68.220  ? 67  LYS GGG NZ  1 
ATOM 11808 N N   . SER G 2 68  ? 113.132 16.319  46.757  1.000 85.940  ? 68  SER GGG N   1 
ATOM 11809 C CA  . SER G 2 68  ? 113.956 17.368  46.112  1.000 89.470  ? 68  SER GGG CA  1 
ATOM 11810 C C   . SER G 2 68  ? 114.186 18.468  47.143  1.000 86.610  ? 68  SER GGG C   1 
ATOM 11811 O O   . SER G 2 68  ? 113.220 19.227  47.402  1.000 83.740  ? 68  SER GGG O   1 
ATOM 11812 C CB  . SER G 2 68  ? 113.316 17.886  44.849  1.000 97.940  ? 68  SER GGG CB  1 
ATOM 11813 O OG  . SER G 2 68  ? 111.984 18.322  45.095  1.000 109.370 ? 68  SER GGG OG  1 
ATOM 11814 N N   . GLY G 2 69  ? 115.390 18.511  47.735  1.000 80.420  ? 69  GLY GGG N   1 
ATOM 11815 C CA  . GLY G 2 69  ? 115.753 19.484  48.786  1.000 76.780  ? 69  GLY GGG CA  1 
ATOM 11816 C C   . GLY G 2 69  ? 114.703 19.527  49.888  1.000 65.850  ? 69  GLY GGG C   1 
ATOM 11817 O O   . GLY G 2 69  ? 114.383 18.460  50.436  1.000 66.870  ? 69  GLY GGG O   1 
ATOM 11818 N N   . THR G 2 70  ? 114.137 20.708  50.145  1.000 58.660  ? 70  THR GGG N   1 
ATOM 11819 C CA  . THR G 2 70  ? 113.267 20.999  51.317  1.000 61.930  ? 70  THR GGG CA  1 
ATOM 11820 C C   . THR G 2 70  ? 111.832 20.485  51.090  1.000 60.370  ? 70  THR GGG C   1 
ATOM 11821 O O   . THR G 2 70  ? 110.980 20.649  52.003  1.000 61.650  ? 70  THR GGG O   1 
ATOM 11822 C CB  . THR G 2 70  ? 113.292 22.496  51.660  1.000 64.080  ? 70  THR GGG CB  1 
ATOM 11823 O OG1 . THR G 2 70  ? 112.509 23.208  50.710  1.000 62.470  ? 70  THR GGG OG1 1 
ATOM 11824 C CG2 . THR G 2 70  ? 114.693 23.073  51.682  1.000 66.840  ? 70  THR GGG CG2 1 
ATOM 11825 N N   . SER G 2 71  ? 111.526 19.886  49.939  1.000 60.680  ? 71  SER GGG N   1 
ATOM 11826 C CA  . SER G 2 71  ? 110.174 19.350  49.649  1.000 65.500  ? 71  SER GGG CA  1 
ATOM 11827 C C   . SER G 2 71  ? 110.268 17.866  49.313  1.000 67.880  ? 71  SER GGG C   1 
ATOM 11828 O O   . SER G 2 71  ? 111.279 17.452  48.688  1.000 70.840  ? 71  SER GGG O   1 
ATOM 11829 C CB  . SER G 2 71  ? 109.482 20.095  48.550  1.000 71.540  ? 71  SER GGG CB  1 
ATOM 11830 O OG  . SER G 2 71  ? 108.084 19.876  48.676  1.000 74.130  ? 71  SER GGG OG  1 
ATOM 11831 N N   . VAL G 2 72  ? 109.235 17.129  49.727  1.000 68.090  ? 72  VAL GGG N   1 
ATOM 11832 C CA  . VAL G 2 72  ? 109.040 15.687  49.431  1.000 66.150  ? 72  VAL GGG CA  1 
ATOM 11833 C C   . VAL G 2 72  ? 107.623 15.534  48.888  1.000 69.710  ? 72  VAL GGG C   1 
ATOM 11834 O O   . VAL G 2 72  ? 106.773 16.376  49.226  1.000 63.810  ? 72  VAL GGG O   1 
ATOM 11835 C CB  . VAL G 2 72  ? 109.247 14.839  50.691  1.000 68.280  ? 72  VAL GGG CB  1 
ATOM 11836 C CG1 . VAL G 2 72  ? 108.673 13.436  50.535  1.000 77.230  ? 72  VAL GGG CG1 1 
ATOM 11837 C CG2 . VAL G 2 72  ? 110.718 14.757  51.067  1.000 70.610  ? 72  VAL GGG CG2 1 
ATOM 11838 N N   . SER G 2 73  ? 107.388 14.516  48.058  1.000 69.030  ? 73  SER GGG N   1 
ATOM 11839 C CA  . SER G 2 73  ? 106.025 14.113  47.631  1.000 64.560  ? 73  SER GGG CA  1 
ATOM 11840 C C   . SER G 2 73  ? 105.835 12.601  47.829  1.000 60.680  ? 73  SER GGG C   1 
ATOM 11841 O O   . SER G 2 73  ? 106.852 11.853  47.844  1.000 58.830  ? 73  SER GGG O   1 
ATOM 11842 C CB  . SER G 2 73  ? 105.773 14.531  46.218  1.000 62.010  ? 73  SER GGG CB  1 
ATOM 11843 O OG  . SER G 2 73  ? 106.695 13.875  45.353  1.000 69.410  ? 73  SER GGG OG  1 
ATOM 11844 N N   . LEU G 2 74  ? 104.584 12.202  48.073  1.000 54.160  ? 74  LEU GGG N   1 
ATOM 11845 C CA  . LEU G 2 74  ? 104.109 10.798  48.105  1.000 53.700  ? 74  LEU GGG CA  1 
ATOM 11846 C C   . LEU G 2 74  ? 103.281 10.573  46.847  1.000 63.090  ? 74  LEU GGG C   1 
ATOM 11847 O O   . LEU G 2 74  ? 102.467 11.450  46.524  1.000 61.750  ? 74  LEU GGG O   1 
ATOM 11848 C CB  . LEU G 2 74  ? 103.263 10.546  49.356  1.000 49.980  ? 74  LEU GGG CB  1 
ATOM 11849 C CG  . LEU G 2 74  ? 102.498 9.223   49.373  1.000 47.070  ? 74  LEU GGG CG  1 
ATOM 11850 C CD1 . LEU G 2 74  ? 103.448 8.041   49.395  1.000 46.350  ? 74  LEU GGG CD1 1 
ATOM 11851 C CD2 . LEU G 2 74  ? 101.554 9.141   50.557  1.000 48.490  ? 74  LEU GGG CD2 1 
ATOM 11852 N N   . ALA G 2 75  ? 103.492 9.448   46.165  1.000 75.200  ? 75  ALA GGG N   1 
ATOM 11853 C CA  . ALA G 2 75  ? 102.808 9.071   44.905  1.000 74.290  ? 75  ALA GGG CA  1 
ATOM 11854 C C   . ALA G 2 75  ? 102.081 7.742   45.107  1.000 71.580  ? 75  ALA GGG C   1 
ATOM 11855 O O   . ALA G 2 75  ? 102.754 6.694   45.217  1.000 67.910  ? 75  ALA GGG O   1 
ATOM 11856 C CB  . ALA G 2 75  ? 103.816 8.981   43.790  1.000 77.820  ? 75  ALA GGG CB  1 
ATOM 11857 N N   . ILE G 2 76  ? 100.753 7.790   45.183  1.000 69.130  ? 76  ILE GGG N   1 
ATOM 11858 C CA  . ILE G 2 76  ? 99.891  6.575   45.186  1.000 73.210  ? 76  ILE GGG CA  1 
ATOM 11859 C C   . ILE G 2 76  ? 99.453  6.319   43.744  1.000 75.430  ? 76  ILE GGG C   1 
ATOM 11860 O O   . ILE G 2 76  ? 98.582  7.056   43.265  1.000 75.700  ? 76  ILE GGG O   1 
ATOM 11861 C CB  . ILE G 2 76  ? 98.677  6.756   46.110  1.000 76.510  ? 76  ILE GGG CB  1 
ATOM 11862 C CG1 . ILE G 2 76  ? 99.089  7.289   47.481  1.000 83.380  ? 76  ILE GGG CG1 1 
ATOM 11863 C CG2 . ILE G 2 76  ? 97.897  5.454   46.215  1.000 78.160  ? 76  ILE GGG CG2 1 
ATOM 11864 C CD1 . ILE G 2 76  ? 97.928  7.687   48.358  1.000 93.420  ? 76  ILE GGG CD1 1 
ATOM 11865 N N   . SER G 2 77  ? 100.049 5.336   43.071  1.000 75.580  ? 77  SER GGG N   1 
ATOM 11866 C CA  . SER G 2 77  ? 99.653  4.915   41.702  1.000 70.400  ? 77  SER GGG CA  1 
ATOM 11867 C C   . SER G 2 77  ? 98.685  3.732   41.823  1.000 69.700  ? 77  SER GGG C   1 
ATOM 11868 O O   . SER G 2 77  ? 98.634  3.114   42.919  1.000 74.810  ? 77  SER GGG O   1 
ATOM 11869 C CB  . SER G 2 77  ? 100.865 4.572   40.877  1.000 72.410  ? 77  SER GGG CB  1 
ATOM 11870 O OG  . SER G 2 77  ? 101.449 3.349   41.309  1.000 75.140  ? 77  SER GGG OG  1 
ATOM 11871 N N   . GLY G 2 78  ? 97.931  3.456   40.759  1.000 62.630  ? 78  GLY GGG N   1 
ATOM 11872 C CA  . GLY G 2 78  ? 96.939  2.365   40.739  1.000 59.850  ? 78  GLY GGG CA  1 
ATOM 11873 C C   . GLY G 2 78  ? 95.975  2.498   41.898  1.000 55.880  ? 78  GLY GGG C   1 
ATOM 11874 O O   . GLY G 2 78  ? 95.807  1.519   42.657  1.000 60.080  ? 78  GLY GGG O   1 
ATOM 11875 N N   . LEU G 2 79  ? 95.371  3.676   42.028  1.000 52.480  ? 79  LEU GGG N   1 
ATOM 11876 C CA  . LEU G 2 79  ? 94.524  4.044   43.191  1.000 59.020  ? 79  LEU GGG CA  1 
ATOM 11877 C C   . LEU G 2 79  ? 93.418  3.001   43.387  1.000 56.710  ? 79  LEU GGG C   1 
ATOM 11878 O O   . LEU G 2 79  ? 92.843  2.579   42.408  1.000 62.310  ? 79  LEU GGG O   1 
ATOM 11879 C CB  . LEU G 2 79  ? 93.942  5.441   42.972  1.000 57.870  ? 79  LEU GGG CB  1 
ATOM 11880 C CG  . LEU G 2 79  ? 93.199  6.017   44.169  1.000 61.790  ? 79  LEU GGG CG  1 
ATOM 11881 C CD1 . LEU G 2 79  ? 94.167  6.263   45.316  1.000 65.350  ? 79  LEU GGG CD1 1 
ATOM 11882 C CD2 . LEU G 2 79  ? 92.469  7.309   43.815  1.000 67.020  ? 79  LEU GGG CD2 1 
ATOM 11883 N N   . GLN G 2 80  ? 93.151  2.605   44.624  1.000 56.970  ? 80  GLN GGG N   1 
ATOM 11884 C CA  . GLN G 2 80  ? 92.071  1.650   45.001  1.000 64.790  ? 80  GLN GGG CA  1 
ATOM 11885 C C   . GLN G 2 80  ? 91.236  2.273   46.123  1.000 63.580  ? 80  GLN GGG C   1 
ATOM 11886 O O   . GLN G 2 80  ? 91.692  3.266   46.694  1.000 67.120  ? 80  GLN GGG O   1 
ATOM 11887 C CB  . GLN G 2 80  ? 92.648  0.292   45.412  1.000 65.890  ? 80  GLN GGG CB  1 
ATOM 11888 C CG  . GLN G 2 80  ? 93.428  -0.387  44.297  1.000 64.380  ? 80  GLN GGG CG  1 
ATOM 11889 C CD  . GLN G 2 80  ? 93.957  -1.740  44.706  1.000 66.470  ? 80  GLN GGG CD  1 
ATOM 11890 O OE1 . GLN G 2 80  ? 93.541  -2.326  45.701  1.000 66.240  ? 80  GLN GGG OE1 1 
ATOM 11891 N NE2 . GLN G 2 80  ? 94.903  -2.252  43.936  1.000 70.090  ? 80  GLN GGG NE2 1 
ATOM 11892 N N   . SER G 2 81  ? 90.060  1.711   46.406  1.000 68.450  ? 81  SER GGG N   1 
ATOM 11893 C CA  . SER G 2 81  ? 89.103  2.226   47.416  1.000 77.290  ? 81  SER GGG CA  1 
ATOM 11894 C C   . SER G 2 81  ? 89.684  1.993   48.805  1.000 81.700  ? 81  SER GGG C   1 
ATOM 11895 O O   . SER G 2 81  ? 89.443  2.847   49.686  1.000 98.100  ? 81  SER GGG O   1 
ATOM 11896 C CB  . SER G 2 81  ? 87.744  1.588   47.280  1.000 86.880  ? 81  SER GGG CB  1 
ATOM 11897 O OG  . SER G 2 81  ? 87.153  1.933   46.038  1.000 97.950  ? 81  SER GGG OG  1 
ATOM 11898 N N   . GLU G 2 82  ? 90.448  0.899   48.968  1.000 73.470  ? 82  GLU GGG N   1 
ATOM 11899 C CA  . GLU G 2 82  ? 91.098  0.515   50.249  1.000 69.620  ? 82  GLU GGG CA  1 
ATOM 11900 C C   . GLU G 2 82  ? 92.156  1.568   50.642  1.000 56.300  ? 82  GLU GGG C   1 
ATOM 11901 O O   . GLU G 2 82  ? 92.638  1.501   51.789  1.000 52.300  ? 82  GLU GGG O   1 
ATOM 11902 C CB  . GLU G 2 82  ? 91.672  -0.897  50.114  1.000 77.310  ? 82  GLU GGG CB  1 
ATOM 11903 C CG  . GLU G 2 82  ? 92.840  -0.994  49.138  1.000 88.130  ? 82  GLU GGG CG  1 
ATOM 11904 C CD  . GLU G 2 82  ? 93.252  -2.408  48.755  1.000 91.560  ? 82  GLU GGG CD  1 
ATOM 11905 O OE1 . GLU G 2 82  ? 92.346  -3.245  48.682  1.000 87.130  ? 82  GLU GGG OE1 1 
ATOM 11906 O OE2 . GLU G 2 82  ? 94.472  -2.667  48.504  1.000 94.030  ? 82  GLU GGG OE2 1 
ATOM 11907 N N   . ASP G 2 83  ? 92.475  2.503   49.738  1.000 50.410  ? 83  ASP GGG N   1 
ATOM 11908 C CA  . ASP G 2 83  ? 93.459  3.607   49.928  1.000 53.420  ? 83  ASP GGG CA  1 
ATOM 11909 C C   . ASP G 2 83  ? 92.785  4.869   50.472  1.000 52.640  ? 83  ASP GGG C   1 
ATOM 11910 O O   . ASP G 2 83  ? 93.490  5.882   50.667  1.000 53.680  ? 83  ASP GGG O   1 
ATOM 11911 C CB  . ASP G 2 83  ? 94.165  3.979   48.624  1.000 50.810  ? 83  ASP GGG CB  1 
ATOM 11912 C CG  . ASP G 2 83  ? 95.083  2.892   48.100  1.000 55.810  ? 83  ASP GGG CG  1 
ATOM 11913 O OD1 . ASP G 2 83  ? 95.387  1.943   48.884  1.000 57.600  ? 83  ASP GGG OD1 1 
ATOM 11914 O OD2 . ASP G 2 83  ? 95.509  3.009   46.915  1.000 49.880  ? 83  ASP GGG OD2 1 
ATOM 11915 N N   . GLU G 2 84  ? 91.503  4.759   50.799  1.000 54.280  ? 84  GLU GGG N   1 
ATOM 11916 C CA  . GLU G 2 84  ? 90.763  5.898   51.381  1.000 61.130  ? 84  GLU GGG CA  1 
ATOM 11917 C C   . GLU G 2 84  ? 91.152  6.040   52.843  1.000 58.200  ? 84  GLU GGG C   1 
ATOM 11918 O O   . GLU G 2 84  ? 90.950  5.076   53.592  1.000 53.780  ? 84  GLU GGG O   1 
ATOM 11919 C CB  . GLU G 2 84  ? 89.254  5.680   51.263  1.000 30.000  ? 84  GLU GGG CB  1 
ATOM 11920 C CG  . GLU G 2 84  ? 88.456  6.954   51.084  1.000 30.000  ? 84  GLU GGG CG  1 
ATOM 11921 C CD  . GLU G 2 84  ? 87.244  6.776   50.191  1.000 30.000  ? 84  GLU GGG CD  1 
ATOM 11922 O OE1 . GLU G 2 84  ? 86.982  5.630   49.786  1.000 30.000  ? 84  GLU GGG OE1 1 
ATOM 11923 O OE2 . GLU G 2 84  ? 86.572  7.780   49.900  1.000 30.000  ? 84  GLU GGG OE2 1 
ATOM 11924 N N   . GLY G 2 85  ? 91.689  7.193   53.217  1.000 57.770  ? 85  GLY GGG N   1 
ATOM 11925 C CA  . GLY G 2 85  ? 92.085  7.517   54.593  1.000 55.650  ? 85  GLY GGG CA  1 
ATOM 11926 C C   . GLY G 2 85  ? 92.876  8.814   54.630  1.000 55.440  ? 85  GLY GGG C   1 
ATOM 11927 O O   . GLY G 2 85  ? 92.877  9.540   53.611  1.000 53.260  ? 85  GLY GGG O   1 
ATOM 11928 N N   . ASP G 2 86  ? 93.492  9.111   55.783  1.000 55.130  ? 86  ASP GGG N   1 
ATOM 11929 C CA  . ASP G 2 86  ? 94.346  10.307  56.008  1.000 52.940  ? 86  ASP GGG CA  1 
ATOM 11930 C C   . ASP G 2 86  ? 95.828  9.910   55.823  1.000 48.320  ? 86  ASP GGG C   1 
ATOM 11931 O O   . ASP G 2 86  ? 96.218  8.812   56.289  1.000 42.850  ? 86  ASP GGG O   1 
ATOM 11932 C CB  . ASP G 2 86  ? 94.015  10.913  57.376  1.000 54.090  ? 86  ASP GGG CB  1 
ATOM 11933 C CG  . ASP G 2 86  ? 92.725  11.716  57.437  1.000 55.300  ? 86  ASP GGG CG  1 
ATOM 11934 O OD1 . ASP G 2 86  ? 91.875  11.578  56.541  1.000 60.560  ? 86  ASP GGG OD1 1 
ATOM 11935 O OD2 . ASP G 2 86  ? 92.593  12.517  58.376  1.000 59.980  ? 86  ASP GGG OD2 1 
ATOM 11936 N N   . TYR G 2 87  ? 96.610  10.761  55.141  1.000 43.610  ? 87  TYR GGG N   1 
ATOM 11937 C CA  . TYR G 2 87  ? 98.060  10.566  54.875  1.000 43.470  ? 87  TYR GGG CA  1 
ATOM 11938 C C   . TYR G 2 87  ? 98.821  11.680  55.592  1.000 45.800  ? 87  TYR GGG C   1 
ATOM 11939 O O   . TYR G 2 87  ? 98.632  12.865  55.288  1.000 48.840  ? 87  TYR GGG O   1 
ATOM 11940 C CB  . TYR G 2 87  ? 98.336  10.465  53.373  1.000 42.030  ? 87  TYR GGG CB  1 
ATOM 11941 C CG  . TYR G 2 87  ? 97.789  9.189   52.794  1.000 43.780  ? 87  TYR GGG CG  1 
ATOM 11942 C CD1 . TYR G 2 87  ? 96.427  9.030   52.592  1.000 47.470  ? 87  TYR GGG CD1 1 
ATOM 11943 C CD2 . TYR G 2 87  ? 98.608  8.121   52.505  1.000 42.500  ? 87  TYR GGG CD2 1 
ATOM 11944 C CE1 . TYR G 2 87  ? 95.883  7.848   52.117  1.000 44.640  ? 87  TYR GGG CE1 1 
ATOM 11945 C CE2 . TYR G 2 87  ? 98.085  6.927   52.035  1.000 48.300  ? 87  TYR GGG CE2 1 
ATOM 11946 C CZ  . TYR G 2 87  ? 96.718  6.789   51.827  1.000 47.670  ? 87  TYR GGG CZ  1 
ATOM 11947 O OH  . TYR G 2 87  ? 96.184  5.621   51.371  1.000 47.210  ? 87  TYR GGG OH  1 
ATOM 11948 N N   . HIS G 2 88  ? 99.630  11.287  56.575  1.000 47.210  ? 88  HIS GGG N   1 
ATOM 11949 C CA  . HIS G 2 88  ? 100.385 12.184  57.485  1.000 42.650  ? 88  HIS GGG CA  1 
ATOM 11950 C C   . HIS G 2 88  ? 101.863 12.149  57.111  1.000 40.490  ? 88  HIS GGG C   1 
ATOM 11951 O O   . HIS G 2 88  ? 102.442 11.047  57.042  1.000 45.860  ? 88  HIS GGG O   1 
ATOM 11952 C CB  . HIS G 2 88  ? 100.151 11.777  58.941  1.000 46.820  ? 88  HIS GGG CB  1 
ATOM 11953 C CG  . HIS G 2 88  ? 98.712  11.820  59.336  1.000 49.520  ? 88  HIS GGG CG  1 
ATOM 11954 N ND1 . HIS G 2 88  ? 98.027  13.011  59.523  1.000 51.940  ? 88  HIS GGG ND1 1 
ATOM 11955 C CD2 . HIS G 2 88  ? 97.825  10.827  59.571  1.000 50.210  ? 88  HIS GGG CD2 1 
ATOM 11956 C CE1 . HIS G 2 88  ? 96.772  12.740  59.823  1.000 51.740  ? 88  HIS GGG CE1 1 
ATOM 11957 N NE2 . HIS G 2 88  ? 96.633  11.415  59.900  1.000 48.400  ? 88  HIS GGG NE2 1 
ATOM 11958 N N   . CYS G 2 89  ? 102.448 13.316  56.888  1.000 38.430  ? 89  CYS GGG N   1 
ATOM 11959 C CA  . CYS G 2 89  ? 103.901 13.462  56.624  1.000 40.140  ? 89  CYS GGG CA  1 
ATOM 11960 C C   . CYS G 2 89  ? 104.548 14.054  57.869  1.000 38.070  ? 89  CYS GGG C   1 
ATOM 11961 O O   . CYS G 2 89  ? 103.969 14.959  58.441  1.000 40.640  ? 89  CYS GGG O   1 
ATOM 11962 C CB  . CYS G 2 89  ? 104.257 14.253  55.379  1.000 44.300  ? 89  CYS GGG CB  1 
ATOM 11963 S SG  . CYS G 2 89  ? 104.062 16.030  55.524  1.000 53.230  ? 89  CYS GGG SG  1 
ATOM 11964 N N   . ALA G 2 90  ? 105.652 13.471  58.344  1.000 38.930  ? 90  ALA GGG N   1 
ATOM 11965 C CA  . ALA G 2 90  ? 106.367 13.917  59.561  1.000 35.430  ? 90  ALA GGG CA  1 
ATOM 11966 C C   . ALA G 2 90  ? 107.882 13.953  59.327  1.000 36.370  ? 90  ALA GGG C   1 
ATOM 11967 O O   . ALA G 2 90  ? 108.388 13.214  58.461  1.000 44.440  ? 90  ALA GGG O   1 
ATOM 11968 C CB  . ALA G 2 90  ? 106.009 12.983  60.675  1.000 33.310  ? 90  ALA GGG CB  1 
ATOM 11969 N N   . ALA G 2 91  ? 108.591 14.759  60.106  1.000 35.680  ? 91  ALA GGG N   1 
ATOM 11970 C CA  . ALA G 2 91  ? 110.062 14.923  60.026  1.000 36.910  ? 91  ALA GGG CA  1 
ATOM 11971 C C   . ALA G 2 91  ? 110.565 15.693  61.247  1.000 36.110  ? 91  ALA GGG C   1 
ATOM 11972 O O   . ALA G 2 91  ? 109.828 16.583  61.728  1.000 35.530  ? 91  ALA GGG O   1 
ATOM 11973 C CB  . ALA G 2 91  ? 110.409 15.675  58.759  1.000 40.030  ? 91  ALA GGG CB  1 
ATOM 11974 N N   . TRP G 2 92  ? 111.779 15.387  61.709  1.000 35.360  ? 92  TRP GGG N   1 
ATOM 11975 C CA  . TRP G 2 92  ? 112.395 16.120  62.849  1.000 37.340  ? 92  TRP GGG CA  1 
ATOM 11976 C C   . TRP G 2 92  ? 112.776 17.540  62.429  1.000 42.400  ? 92  TRP GGG C   1 
ATOM 11977 O O   . TRP G 2 92  ? 113.234 17.696  61.297  1.000 51.100  ? 92  TRP GGG O   1 
ATOM 11978 C CB  . TRP G 2 92  ? 113.605 15.382  63.355  1.000 34.270  ? 92  TRP GGG CB  1 
ATOM 11979 C CG  . TRP G 2 92  ? 114.255 16.026  64.534  1.000 32.460  ? 92  TRP GGG CG  1 
ATOM 11980 C CD1 . TRP G 2 92  ? 115.363 16.815  64.513  1.000 32.880  ? 92  TRP GGG CD1 1 
ATOM 11981 C CD2 . TRP G 2 92  ? 113.873 15.897  65.914  1.000 32.590  ? 92  TRP GGG CD2 1 
ATOM 11982 N NE1 . TRP G 2 92  ? 115.696 17.186  65.790  1.000 34.630  ? 92  TRP GGG NE1 1 
ATOM 11983 C CE2 . TRP G 2 92  ? 114.785 16.653  66.667  1.000 32.610  ? 92  TRP GGG CE2 1 
ATOM 11984 C CE3 . TRP G 2 92  ? 112.843 15.239  66.582  1.000 34.030  ? 92  TRP GGG CE3 1 
ATOM 11985 C CZ2 . TRP G 2 92  ? 114.706 16.744  68.053  1.000 31.930  ? 92  TRP GGG CZ2 1 
ATOM 11986 C CZ3 . TRP G 2 92  ? 112.762 15.338  67.952  1.000 32.550  ? 92  TRP GGG CZ3 1 
ATOM 11987 C CH2 . TRP G 2 92  ? 113.687 16.069  68.675  1.000 31.190  ? 92  TRP GGG CH2 1 
ATOM 11988 N N   . ASP G 2 93  ? 112.593 18.528  63.310  1.000 42.800  ? 93  ASP GGG N   1 
ATOM 11989 C CA  . ASP G 2 93  ? 113.070 19.916  63.063  1.000 41.720  ? 93  ASP GGG CA  1 
ATOM 11990 C C   . ASP G 2 93  ? 114.181 20.230  64.060  1.000 39.000  ? 93  ASP GGG C   1 
ATOM 11991 O O   . ASP G 2 93  ? 113.914 20.200  65.269  1.000 32.700  ? 93  ASP GGG O   1 
ATOM 11992 C CB  . ASP G 2 93  ? 111.925 20.930  63.126  1.000 43.700  ? 93  ASP GGG CB  1 
ATOM 11993 C CG  . ASP G 2 93  ? 112.426 22.340  62.816  1.000 46.110  ? 93  ASP GGG CG  1 
ATOM 11994 O OD1 . ASP G 2 93  ? 113.356 22.798  63.506  1.000 47.650  ? 93  ASP GGG OD1 1 
ATOM 11995 O OD2 . ASP G 2 93  ? 111.905 22.957  61.871  1.000 48.290  ? 93  ASP GGG OD2 1 
ATOM 11996 N N   . ASP G 2 94  ? 115.382 20.515  63.543  1.000 39.460  ? 94  ASP GGG N   1 
ATOM 11997 C CA  . ASP G 2 94  ? 116.615 20.726  64.340  1.000 39.210  ? 94  ASP GGG CA  1 
ATOM 11998 C C   . ASP G 2 94  ? 116.480 22.002  65.153  1.000 37.820  ? 94  ASP GGG C   1 
ATOM 11999 O O   . ASP G 2 94  ? 117.074 22.051  66.230  1.000 40.390  ? 94  ASP GGG O   1 
ATOM 12000 C CB  . ASP G 2 94  ? 117.851 20.838  63.456  1.000 42.200  ? 94  ASP GGG CB  1 
ATOM 12001 C CG  . ASP G 2 94  ? 118.306 19.506  62.892  1.000 47.100  ? 94  ASP GGG CG  1 
ATOM 12002 O OD1 . ASP G 2 94  ? 118.147 18.479  63.634  1.000 42.300  ? 94  ASP GGG OD1 1 
ATOM 12003 O OD2 . ASP G 2 94  ? 118.815 19.507  61.721  1.000 47.350  ? 94  ASP GGG OD2 1 
ATOM 12004 N N   . SER G 2 95  ? 115.765 22.998  64.631  1.000 37.420  ? 95  SER GGG N   1 
ATOM 12005 C CA  . SER G 2 95  ? 115.608 24.313  65.289  1.000 38.720  ? 95  SER GGG CA  1 
ATOM 12006 C C   . SER G 2 95  ? 114.659 24.157  66.491  1.000 39.930  ? 95  SER GGG C   1 
ATOM 12007 O O   . SER G 2 95  ? 115.066 24.539  67.594  1.000 41.360  ? 95  SER GGG O   1 
ATOM 12008 C CB  . SER G 2 95  ? 115.194 25.370  64.294  1.000 43.170  ? 95  SER GGG CB  1 
ATOM 12009 O OG  . SER G 2 95  ? 116.209 25.597  63.319  1.000 53.450  ? 95  SER GGG OG  1 
ATOM 12010 N N   . LEU G 2 96  ? 113.489 23.534  66.318  1.000 41.600  ? 96  LEU GGG N   1 
ATOM 12011 C CA  . LEU G 2 96  ? 112.458 23.402  67.391  1.000 38.810  ? 96  LEU GGG CA  1 
ATOM 12012 C C   . LEU G 2 96  ? 112.757 22.213  68.309  1.000 37.140  ? 96  LEU GGG C   1 
ATOM 12013 O O   . LEU G 2 96  ? 111.989 22.007  69.251  1.000 33.430  ? 96  LEU GGG O   1 
ATOM 12014 C CB  . LEU G 2 96  ? 111.088 23.181  66.747  1.000 40.060  ? 96  LEU GGG CB  1 
ATOM 12015 C CG  . LEU G 2 96  ? 110.680 24.153  65.657  1.000 38.740  ? 96  LEU GGG CG  1 
ATOM 12016 C CD1 . LEU G 2 96  ? 109.294 23.788  65.119  1.000 38.270  ? 96  LEU GGG CD1 1 
ATOM 12017 C CD2 . LEU G 2 96  ? 110.783 25.567  66.179  1.000 40.540  ? 96  LEU GGG CD2 1 
ATOM 12018 N N   . LYS G 2 97  ? 113.797 21.436  68.024  1.000 40.370  ? 97  LYS GGG N   1 
ATOM 12019 C CA  . LYS G 2 97  ? 114.107 20.189  68.764  1.000 46.620  ? 97  LYS GGG CA  1 
ATOM 12020 C C   . LYS G 2 97  ? 112.802 19.415  69.020  1.000 42.330  ? 97  LYS GGG C   1 
ATOM 12021 O O   . LYS G 2 97  ? 112.475 19.113  70.193  1.000 39.290  ? 97  LYS GGG O   1 
ATOM 12022 C CB  . LYS G 2 97  ? 114.909 20.512  70.032  1.000 52.700  ? 97  LYS GGG CB  1 
ATOM 12023 C CG  . LYS G 2 97  ? 116.317 21.036  69.771  1.000 59.030  ? 97  LYS GGG CG  1 
ATOM 12024 C CD  . LYS G 2 97  ? 117.269 19.976  69.201  1.000 66.590  ? 97  LYS GGG CD  1 
ATOM 12025 C CE  . LYS G 2 97  ? 118.630 20.507  68.797  1.000 66.110  ? 97  LYS GGG CE  1 
ATOM 12026 N NZ  . LYS G 2 97  ? 119.349 19.510  67.970  1.000 63.050  ? 97  LYS GGG NZ  1 
ATOM 12027 N N   . GLY G 2 98  ? 112.094 19.076  67.950  1.000 37.380  ? 98  GLY GGG N   1 
ATOM 12028 C CA  . GLY G 2 98  ? 110.876 18.260  68.040  1.000 37.160  ? 98  GLY GGG CA  1 
ATOM 12029 C C   . GLY G 2 98  ? 110.460 17.711  66.688  1.000 36.840  ? 98  GLY GGG C   1 
ATOM 12030 O O   . GLY G 2 98  ? 111.063 18.084  65.654  1.000 33.080  ? 98  GLY GGG O   1 
ATOM 12031 N N   . TRP G 2 99  ? 109.455 16.840  66.704  1.000 36.940  ? 99  TRP GGG N   1 
ATOM 12032 C CA  . TRP G 2 99  ? 108.822 16.311  65.475  1.000 37.290  ? 99  TRP GGG CA  1 
ATOM 12033 C C   . TRP G 2 99  ? 107.776 17.313  64.996  1.000 36.830  ? 99  TRP GGG C   1 
ATOM 12034 O O   . TRP G 2 99  ? 106.919 17.713  65.804  1.000 35.530  ? 99  TRP GGG O   1 
ATOM 12035 C CB  . TRP G 2 99  ? 108.223 14.924  65.727  1.000 35.060  ? 99  TRP GGG CB  1 
ATOM 12036 C CG  . TRP G 2 99  ? 109.273 13.897  65.983  1.000 32.860  ? 99  TRP GGG CG  1 
ATOM 12037 C CD1 . TRP G 2 99  ? 109.719 13.449  67.191  1.000 33.270  ? 99  TRP GGG CD1 1 
ATOM 12038 C CD2 . TRP G 2 99  ? 110.044 13.210  64.989  1.000 31.330  ? 99  TRP GGG CD2 1 
ATOM 12039 N NE1 . TRP G 2 99  ? 110.702 12.510  67.018  1.000 32.970  ? 99  TRP GGG NE1 1 
ATOM 12040 C CE2 . TRP G 2 99  ? 110.918 12.346  65.674  1.000 32.440  ? 99  TRP GGG CE2 1 
ATOM 12041 C CE3 . TRP G 2 99  ? 110.076 13.232  63.597  1.000 31.570  ? 99  TRP GGG CE3 1 
ATOM 12042 C CZ2 . TRP G 2 99  ? 111.808 11.517  65.001  1.000 33.700  ? 99  TRP GGG CZ2 1 
ATOM 12043 C CZ3 . TRP G 2 99  ? 110.958 12.396  62.937  1.000 33.540  ? 99  TRP GGG CZ3 1 
ATOM 12044 C CH2 . TRP G 2 99  ? 111.815 11.565  63.629  1.000 32.470  ? 99  TRP GGG CH2 1 
ATOM 12045 N N   . VAL G 2 100 ? 107.857 17.684  63.722  1.000 37.050  ? 100 VAL GGG N   1 
ATOM 12046 C CA  . VAL G 2 100 ? 106.786 18.433  63.004  1.000 39.400  ? 100 VAL GGG CA  1 
ATOM 12047 C C   . VAL G 2 100 ? 106.051 17.448  62.091  1.000 43.490  ? 100 VAL GGG C   1 
ATOM 12048 O O   . VAL G 2 100 ? 106.680 16.565  61.505  1.000 37.200  ? 100 VAL GGG O   1 
ATOM 12049 C CB  . VAL G 2 100 ? 107.360 19.661  62.257  1.000 35.970  ? 100 VAL GGG CB  1 
ATOM 12050 C CG1 . VAL G 2 100 ? 108.077 20.592  63.219  1.000 36.680  ? 100 VAL GGG CG1 1 
ATOM 12051 C CG2 . VAL G 2 100 ? 108.306 19.279  61.147  1.000 33.950  ? 100 VAL GGG CG2 1 
ATOM 12052 N N   . PHE G 2 101 ? 104.727 17.577  62.047  1.000 51.240  ? 101 PHE GGG N   1 
ATOM 12053 C CA  . PHE G 2 101 ? 103.812 16.846  61.136  1.000 46.710  ? 101 PHE GGG CA  1 
ATOM 12054 C C   . PHE G 2 101 ? 103.193 17.873  60.201  1.000 44.640  ? 101 PHE GGG C   1 
ATOM 12055 O O   . PHE G 2 101 ? 103.373 19.069  60.438  1.000 44.810  ? 101 PHE GGG O   1 
ATOM 12056 C CB  . PHE G 2 101 ? 102.715 16.094  61.893  1.000 43.740  ? 101 PHE GGG CB  1 
ATOM 12057 C CG  . PHE G 2 101 ? 103.190 14.874  62.632  1.000 43.420  ? 101 PHE GGG CG  1 
ATOM 12058 C CD1 . PHE G 2 101 ? 103.831 14.977  63.845  1.000 44.580  ? 101 PHE GGG CD1 1 
ATOM 12059 C CD2 . PHE G 2 101 ? 103.001 13.611  62.093  1.000 45.750  ? 101 PHE GGG CD2 1 
ATOM 12060 C CE1 . PHE G 2 101 ? 104.265 13.842  64.518  1.000 44.230  ? 101 PHE GGG CE1 1 
ATOM 12061 C CE2 . PHE G 2 101 ? 103.431 12.476  62.770  1.000 44.800  ? 101 PHE GGG CE2 1 
ATOM 12062 C CZ  . PHE G 2 101 ? 104.048 12.594  63.986  1.000 43.910  ? 101 PHE GGG CZ  1 
ATOM 12063 N N   . GLY G 2 102 ? 102.547 17.390  59.147  1.000 45.590  ? 102 GLY GGG N   1 
ATOM 12064 C CA  . GLY G 2 102 ? 101.694 18.197  58.275  1.000 45.290  ? 102 GLY GGG CA  1 
ATOM 12065 C C   . GLY G 2 102 ? 100.297 18.258  58.843  1.000 49.440  ? 102 GLY GGG C   1 
ATOM 12066 O O   . GLY G 2 102 ? 100.091 17.748  59.971  1.000 54.350  ? 102 GLY GGG O   1 
ATOM 12067 N N   . GLY G 2 103 ? 99.378  18.860  58.098  1.000 53.190  ? 103 GLY GGG N   1 
ATOM 12068 C CA  . GLY G 2 103 ? 97.969  18.976  58.511  1.000 59.040  ? 103 GLY GGG CA  1 
ATOM 12069 C C   . GLY G 2 103 ? 97.297  17.630  58.427  1.000 63.450  ? 103 GLY GGG C   1 
ATOM 12070 O O   . GLY G 2 103 ? 96.355  17.374  59.182  1.000 65.290  ? 103 GLY GGG O   1 
ATOM 12071 N N   . GLY G 2 104 ? 97.806  16.778  57.551  1.000 68.100  ? 104 GLY GGG N   1 
ATOM 12072 C CA  . GLY G 2 104 ? 97.066  15.600  57.093  1.000 77.940  ? 104 GLY GGG CA  1 
ATOM 12073 C C   . GLY G 2 104 ? 96.404  15.887  55.768  1.000 80.510  ? 104 GLY GGG C   1 
ATOM 12074 O O   . GLY G 2 104 ? 96.127  17.078  55.470  1.000 80.910  ? 104 GLY GGG O   1 
ATOM 12075 N N   . THR G 2 105 ? 96.221  14.828  54.984  1.000 78.830  ? 105 THR GGG N   1 
ATOM 12076 C CA  . THR G 2 105 ? 95.615  14.859  53.638  1.000 76.180  ? 105 THR GGG CA  1 
ATOM 12077 C C   . THR G 2 105 ? 94.570  13.750  53.627  1.000 78.290  ? 105 THR GGG C   1 
ATOM 12078 O O   . THR G 2 105 ? 94.980  12.582  53.701  1.000 73.390  ? 105 THR GGG O   1 
ATOM 12079 C CB  . THR G 2 105 ? 96.700  14.680  52.574  1.000 70.340  ? 105 THR GGG CB  1 
ATOM 12080 O OG1 . THR G 2 105 ? 97.637  15.747  52.714  1.000 67.200  ? 105 THR GGG OG1 1 
ATOM 12081 C CG2 . THR G 2 105 ? 96.174  14.660  51.165  1.000 72.840  ? 105 THR GGG CG2 1 
ATOM 12082 N N   . LYS G 2 106 ? 93.281  14.094  53.608  1.000 76.090  ? 106 LYS GGG N   1 
ATOM 12083 C CA  . LYS G 2 106 ? 92.205  13.089  53.413  1.000 76.590  ? 106 LYS GGG CA  1 
ATOM 12084 C C   . LYS G 2 106 ? 92.117  12.805  51.910  1.000 79.760  ? 106 LYS GGG C   1 
ATOM 12085 O O   . LYS G 2 106 ? 91.832  13.745  51.125  1.000 83.200  ? 106 LYS GGG O   1 
ATOM 12086 C CB  . LYS G 2 106 ? 90.875  13.548  54.018  1.000 79.910  ? 106 LYS GGG CB  1 
ATOM 12087 C CG  . LYS G 2 106 ? 89.825  12.449  54.155  1.000 82.360  ? 106 LYS GGG CG  1 
ATOM 12088 C CD  . LYS G 2 106 ? 88.524  12.916  54.771  1.000 80.610  ? 106 LYS GGG CD  1 
ATOM 12089 C CE  . LYS G 2 106 ? 87.425  11.888  54.606  1.000 81.410  ? 106 LYS GGG CE  1 
ATOM 12090 N NZ  . LYS G 2 106 ? 86.225  12.216  55.410  1.000 78.940  ? 106 LYS GGG NZ  1 
ATOM 12091 N N   . LEU G 2 107 ? 92.467  11.574  51.527  1.000 75.470  ? 107 LEU GGG N   1 
ATOM 12092 C CA  . LEU G 2 107 ? 92.356  11.063  50.139  1.000 73.540  ? 107 LEU GGG CA  1 
ATOM 12093 C C   . LEU G 2 107 ? 90.971  10.435  49.995  1.000 82.880  ? 107 LEU GGG C   1 
ATOM 12094 O O   . LEU G 2 107 ? 90.722  9.415   50.689  1.000 82.820  ? 107 LEU GGG O   1 
ATOM 12095 C CB  . LEU G 2 107 ? 93.456  10.025  49.910  1.000 68.260  ? 107 LEU GGG CB  1 
ATOM 12096 C CG  . LEU G 2 107 ? 93.550  9.455   48.498  1.000 67.590  ? 107 LEU GGG CG  1 
ATOM 12097 C CD1 . LEU G 2 107 ? 94.071  10.478  47.514  1.000 69.510  ? 107 LEU GGG CD1 1 
ATOM 12098 C CD2 . LEU G 2 107 ? 94.447  8.239   48.475  1.000 69.520  ? 107 LEU GGG CD2 1 
ATOM 12099 N N   . THR G 2 108 ? 90.105  11.031  49.171  1.000 86.010  ? 108 THR GGG N   1 
ATOM 12100 C CA  . THR G 2 108 ? 88.756  10.473  48.837  1.000 80.180  ? 108 THR GGG CA  1 
ATOM 12101 C C   . THR G 2 108 ? 88.867  9.767   47.483  1.000 78.110  ? 108 THR GGG C   1 
ATOM 12102 O O   . THR G 2 108 ? 89.509  10.355  46.570  1.000 78.830  ? 108 THR GGG O   1 
ATOM 12103 C CB  . THR G 2 108 ? 87.655  11.546  48.865  1.000 77.720  ? 108 THR GGG CB  1 
ATOM 12104 O OG1 . THR G 2 108 ? 88.161  12.785  48.364  1.000 79.120  ? 108 THR GGG OG1 1 
ATOM 12105 C CG2 . THR G 2 108 ? 87.077  11.720  50.255  1.000 77.790  ? 108 THR GGG CG2 1 
ATOM 12106 N N   . VAL G 2 109 ? 88.334  8.539   47.392  1.000 74.530  ? 109 VAL GGG N   1 
ATOM 12107 C CA  . VAL G 2 109 ? 88.338  7.705   46.154  1.000 74.830  ? 109 VAL GGG CA  1 
ATOM 12108 C C   . VAL G 2 109 ? 86.913  7.668   45.599  1.000 82.280  ? 109 VAL GGG C   1 
ATOM 12109 O O   . VAL G 2 109 ? 85.995  7.249   46.328  1.000 87.750  ? 109 VAL GGG O   1 
ATOM 12110 C CB  . VAL G 2 109 ? 88.861  6.287   46.422  1.000 71.590  ? 109 VAL GGG CB  1 
ATOM 12111 C CG1 . VAL G 2 109 ? 89.104  5.524   45.131  1.000 73.720  ? 109 VAL GGG CG1 1 
ATOM 12112 C CG2 . VAL G 2 109 ? 90.135  6.320   47.227  1.000 71.520  ? 109 VAL GGG CG2 1 
ATOM 12113 N N   . LEU G 2 110 ? 86.752  8.081   44.342  1.000 81.870  ? 110 LEU GGG N   1 
ATOM 12114 C CA  . LEU G 2 110 ? 85.437  8.343   43.709  1.000 79.960  ? 110 LEU GGG CA  1 
ATOM 12115 C C   . LEU G 2 110 ? 85.036  7.142   42.839  1.000 82.210  ? 110 LEU GGG C   1 
ATOM 12116 O O   . LEU G 2 110 ? 85.512  7.018   41.705  1.000 86.370  ? 110 LEU GGG O   1 
ATOM 12117 C CB  . LEU G 2 110 ? 85.564  9.650   42.921  1.000 83.700  ? 110 LEU GGG CB  1 
ATOM 12118 C CG  . LEU G 2 110 ? 86.105  10.823  43.741  1.000 76.880  ? 110 LEU GGG CG  1 
ATOM 12119 C CD1 . LEU G 2 110 ? 86.387  12.027  42.855  1.000 74.620  ? 110 LEU GGG CD1 1 
ATOM 12120 C CD2 . LEU G 2 110 ? 85.148  11.184  44.874  1.000 68.500  ? 110 LEU GGG CD2 1 
ATOM 12121 N N   . GLY G 2 111 ? 84.157  6.299   43.391  1.000 79.920  ? 111 GLY GGG N   1 
ATOM 12122 C CA  . GLY G 2 111 ? 83.521  5.150   42.725  1.000 81.680  ? 111 GLY GGG CA  1 
ATOM 12123 C C   . GLY G 2 111 ? 82.032  5.199   42.990  1.000 86.330  ? 111 GLY GGG C   1 
ATOM 12124 O O   . GLY G 2 111 ? 81.508  4.278   43.659  1.000 89.030  ? 111 GLY GGG O   1 
ATOM 12125 N N   . ALA G 2 112 ? 81.408  6.302   42.575  1.000 90.470  ? 112 ALA GGG N   1 
ATOM 12126 C CA  . ALA G 2 112 ? 79.952  6.583   42.639  1.000 93.920  ? 112 ALA GGG CA  1 
ATOM 12127 C C   . ALA G 2 112 ? 79.722  7.806   41.752  1.000 103.370 ? 112 ALA GGG C   1 
ATOM 12128 O O   . ALA G 2 112 ? 80.682  8.459   41.350  1.000 96.260  ? 112 ALA GGG O   1 
ATOM 12129 C CB  . ALA G 2 112 ? 79.492  6.791   44.075  1.000 81.450  ? 112 ALA GGG CB  1 
ATOM 12130 N N   . PRO G 2 113 ? 78.468  8.157   41.391  1.000 120.770 ? 113 PRO GGG N   1 
ATOM 12131 C CA  . PRO G 2 113 ? 78.217  9.379   40.621  1.000 115.810 ? 113 PRO GGG CA  1 
ATOM 12132 C C   . PRO G 2 113 ? 78.398  10.640  41.481  1.000 104.300 ? 113 PRO GGG C   1 
ATOM 12133 O O   . PRO G 2 113 ? 78.274  10.525  42.686  1.000 94.360  ? 113 PRO GGG O   1 
ATOM 12134 C CB  . PRO G 2 113 ? 76.759  9.218   40.175  1.000 130.730 ? 113 PRO GGG CB  1 
ATOM 12135 C CG  . PRO G 2 113 ? 76.118  8.330   41.241  1.000 129.600 ? 113 PRO GGG CG  1 
ATOM 12136 C CD  . PRO G 2 113 ? 77.234  7.414   41.703  1.000 127.210 ? 113 PRO GGG CD  1 
ATOM 12137 N N   . LYS G 2 114 ? 78.689  11.792  40.858  1.000 105.470 ? 114 LYS GGG N   1 
ATOM 12138 C CA  . LYS G 2 114 ? 78.817  13.115  41.546  1.000 103.900 ? 114 LYS GGG CA  1 
ATOM 12139 C C   . LYS G 2 114 ? 77.423  13.568  42.000  1.000 106.970 ? 114 LYS GGG C   1 
ATOM 12140 O O   . LYS G 2 114 ? 76.804  14.382  41.280  1.000 103.310 ? 114 LYS GGG O   1 
ATOM 12141 C CB  . LYS G 2 114 ? 79.488  14.174  40.658  1.000 87.560  ? 114 LYS GGG CB  1 
ATOM 12142 N N   . ALA G 2 115 ? 76.972  13.087  43.167  1.000 119.650 ? 115 ALA GGG N   1 
ATOM 12143 C CA  . ALA G 2 115 ? 75.632  13.346  43.758  1.000 130.440 ? 115 ALA GGG CA  1 
ATOM 12144 C C   . ALA G 2 115 ? 75.701  14.507  44.762  1.000 141.250 ? 115 ALA GGG C   1 
ATOM 12145 O O   . ALA G 2 115 ? 76.551  14.422  45.678  1.000 159.500 ? 115 ALA GGG O   1 
ATOM 12146 C CB  . ALA G 2 115 ? 75.126  12.090  44.419  1.000 119.610 ? 115 ALA GGG CB  1 
ATOM 12147 N N   . ASN G 2 116 ? 74.832  15.523  44.600  1.000 130.530 ? 116 ASN GGG N   1 
ATOM 12148 C CA  . ASN G 2 116 ? 74.898  16.839  45.298  1.000 127.440 ? 116 ASN GGG CA  1 
ATOM 12149 C C   . ASN G 2 116 ? 73.913  16.850  46.465  1.000 116.630 ? 116 ASN GGG C   1 
ATOM 12150 O O   . ASN G 2 116 ? 72.963  16.074  46.471  1.000 91.450  ? 116 ASN GGG O   1 
ATOM 12151 C CB  . ASN G 2 116 ? 74.659  18.014  44.340  1.000 134.360 ? 116 ASN GGG CB  1 
ATOM 12152 C CG  . ASN G 2 116 ? 75.921  18.804  44.044  1.000 143.370 ? 116 ASN GGG CG  1 
ATOM 12153 O OD1 . ASN G 2 116 ? 76.427  19.529  44.900  1.000 147.600 ? 116 ASN GGG OD1 1 
ATOM 12154 N ND2 . ASN G 2 116 ? 76.439  18.684  42.831  1.000 145.320 ? 116 ASN GGG ND2 1 
ATOM 12155 N N   . PRO G 2 117 ? 74.093  17.752  47.467  1.000 130.790 ? 117 PRO GGG N   1 
ATOM 12156 C CA  . PRO G 2 117 ? 73.356  17.674  48.733  1.000 135.420 ? 117 PRO GGG CA  1 
ATOM 12157 C C   . PRO G 2 117 ? 71.871  18.083  48.698  1.000 137.800 ? 117 PRO GGG C   1 
ATOM 12158 O O   . PRO G 2 117 ? 71.555  19.224  48.346  1.000 131.090 ? 117 PRO GGG O   1 
ATOM 12159 C CB  . PRO G 2 117 ? 74.113  18.654  49.649  1.000 140.850 ? 117 PRO GGG CB  1 
ATOM 12160 C CG  . PRO G 2 117 ? 74.721  19.673  48.704  1.000 138.870 ? 117 PRO GGG CG  1 
ATOM 12161 C CD  . PRO G 2 117 ? 75.021  18.901  47.437  1.000 134.710 ? 117 PRO GGG CD  1 
ATOM 12162 N N   . THR G 2 118 ? 70.994  17.169  49.143  1.000 137.630 ? 118 THR GGG N   1 
ATOM 12163 C CA  . THR G 2 118 ? 69.574  17.434  49.526  1.000 139.680 ? 118 THR GGG CA  1 
ATOM 12164 C C   . THR G 2 118 ? 69.554  18.384  50.739  1.000 147.120 ? 118 THR GGG C   1 
ATOM 12165 O O   . THR G 2 118 ? 70.406  18.210  51.622  1.000 161.240 ? 118 THR GGG O   1 
ATOM 12166 C CB  . THR G 2 118 ? 68.833  16.111  49.790  1.000 127.890 ? 118 THR GGG CB  1 
ATOM 12167 O OG1 . THR G 2 118 ? 68.750  15.411  48.548  1.000 108.960 ? 118 THR GGG OG1 1 
ATOM 12168 C CG2 . THR G 2 118 ? 67.438  16.278  50.358  1.000 119.890 ? 118 THR GGG CG2 1 
ATOM 12169 N N   . VAL G 2 119 ? 68.614  19.340  50.780  1.000 139.030 ? 119 VAL GGG N   1 
ATOM 12170 C CA  . VAL G 2 119 ? 68.488  20.382  51.849  1.000 130.750 ? 119 VAL GGG CA  1 
ATOM 12171 C C   . VAL G 2 119 ? 67.094  20.292  52.489  1.000 141.450 ? 119 VAL GGG C   1 
ATOM 12172 O O   . VAL G 2 119 ? 66.103  20.302  51.730  1.000 181.540 ? 119 VAL GGG O   1 
ATOM 12173 C CB  . VAL G 2 119 ? 68.795  21.795  51.304  1.000 128.890 ? 119 VAL GGG CB  1 
ATOM 12174 C CG1 . VAL G 2 119 ? 70.221  21.906  50.791  1.000 127.540 ? 119 VAL GGG CG1 1 
ATOM 12175 C CG2 . VAL G 2 119 ? 67.812  22.254  50.230  1.000 129.390 ? 119 VAL GGG CG2 1 
ATOM 12176 N N   . THR G 2 120 ? 67.031  20.206  53.825  1.000 132.880 ? 120 THR GGG N   1 
ATOM 12177 C CA  . THR G 2 120 ? 65.822  19.804  54.609  1.000 118.980 ? 120 THR GGG CA  1 
ATOM 12178 C C   . THR G 2 120 ? 65.635  20.767  55.800  1.000 105.120 ? 120 THR GGG C   1 
ATOM 12179 O O   . THR G 2 120 ? 65.289  20.276  56.877  1.000 97.210  ? 120 THR GGG O   1 
ATOM 12180 C CB  . THR G 2 120 ? 65.922  18.322  55.047  1.000 108.850 ? 120 THR GGG CB  1 
ATOM 12181 O OG1 . THR G 2 120 ? 66.566  17.529  54.041  1.000 89.360  ? 120 THR GGG OG1 1 
ATOM 12182 C CG2 . THR G 2 120 ? 64.580  17.695  55.369  1.000 97.640  ? 120 THR GGG CG2 1 
ATOM 12183 N N   . LEU G 2 121 ? 65.838  22.080  55.617  1.000 110.930 ? 121 LEU GGG N   1 
ATOM 12184 C CA  . LEU G 2 121 ? 65.995  23.075  56.727  1.000 130.990 ? 121 LEU GGG CA  1 
ATOM 12185 C C   . LEU G 2 121 ? 64.658  23.352  57.447  1.000 128.300 ? 121 LEU GGG C   1 
ATOM 12186 O O   . LEU G 2 121 ? 63.760  23.938  56.825  1.000 127.240 ? 121 LEU GGG O   1 
ATOM 12187 C CB  . LEU G 2 121 ? 66.656  24.356  56.191  1.000 139.470 ? 121 LEU GGG CB  1 
ATOM 12188 C CG  . LEU G 2 121 ? 65.789  25.340  55.402  1.000 154.500 ? 121 LEU GGG CG  1 
ATOM 12189 C CD1 . LEU G 2 121 ? 66.551  26.637  55.164  1.000 151.250 ? 121 LEU GGG CD1 1 
ATOM 12190 C CD2 . LEU G 2 121 ? 65.314  24.751  54.075  1.000 157.730 ? 121 LEU GGG CD2 1 
ATOM 12191 N N   . PHE G 2 122 ? 64.561  22.962  58.732  1.000 132.780 ? 122 PHE GGG N   1 
ATOM 12192 C CA  . PHE G 2 122 ? 63.388  23.117  59.648  1.000 130.080 ? 122 PHE GGG CA  1 
ATOM 12193 C C   . PHE G 2 122 ? 63.498  24.447  60.403  1.000 143.080 ? 122 PHE GGG C   1 
ATOM 12194 O O   . PHE G 2 122 ? 64.582  24.834  60.832  1.000 140.450 ? 122 PHE GGG O   1 
ATOM 12195 C CB  . PHE G 2 122 ? 63.323  21.925  60.614  1.000 120.200 ? 122 PHE GGG CB  1 
ATOM 12196 C CG  . PHE G 2 122 ? 62.054  21.727  61.415  1.000 132.540 ? 122 PHE GGG CG  1 
ATOM 12197 C CD1 . PHE G 2 122 ? 60.909  21.186  60.835  1.000 132.620 ? 122 PHE GGG CD1 1 
ATOM 12198 C CD2 . PHE G 2 122 ? 62.017  22.019  62.775  1.000 127.390 ? 122 PHE GGG CD2 1 
ATOM 12199 C CE1 . PHE G 2 122 ? 59.752  20.988  61.582  1.000 124.950 ? 122 PHE GGG CE1 1 
ATOM 12200 C CE2 . PHE G 2 122 ? 60.850  21.812  63.522  1.000 122.220 ? 122 PHE GGG CE2 1 
ATOM 12201 C CZ  . PHE G 2 122 ? 59.730  21.296  62.926  1.000 118.790 ? 122 PHE GGG CZ  1 
ATOM 12202 N N   . PRO G 2 123 ? 62.393  25.212  60.563  1.000 164.160 ? 123 PRO GGG N   1 
ATOM 12203 C CA  . PRO G 2 123 ? 62.439  26.507  61.255  1.000 160.570 ? 123 PRO GGG CA  1 
ATOM 12204 C C   . PRO G 2 123 ? 62.386  26.383  62.781  1.000 156.280 ? 123 PRO GGG C   1 
ATOM 12205 O O   . PRO G 2 123 ? 62.232  25.275  63.301  1.000 142.880 ? 123 PRO GGG O   1 
ATOM 12206 C CB  . PRO G 2 123 ? 61.190  27.201  60.686  1.000 165.900 ? 123 PRO GGG CB  1 
ATOM 12207 C CG  . PRO G 2 123 ? 60.200  26.071  60.467  1.000 165.140 ? 123 PRO GGG CG  1 
ATOM 12208 C CD  . PRO G 2 123 ? 61.047  24.883  60.058  1.000 165.980 ? 123 PRO GGG CD  1 
ATOM 12209 N N   . PRO G 2 124 ? 62.494  27.500  63.548  1.000 144.820 ? 124 PRO GGG N   1 
ATOM 12210 C CA  . PRO G 2 124 ? 62.380  27.455  65.013  1.000 129.780 ? 124 PRO GGG CA  1 
ATOM 12211 C C   . PRO G 2 124 ? 60.998  26.991  65.506  1.000 116.520 ? 124 PRO GGG C   1 
ATOM 12212 O O   . PRO G 2 124 ? 60.925  26.401  66.579  1.000 95.150  ? 124 PRO GGG O   1 
ATOM 12213 C CB  . PRO G 2 124 ? 62.617  28.905  65.476  1.000 120.240 ? 124 PRO GGG CB  1 
ATOM 12214 C CG  . PRO G 2 124 ? 63.268  29.598  64.294  1.000 122.040 ? 124 PRO GGG CG  1 
ATOM 12215 C CD  . PRO G 2 124 ? 62.806  28.857  63.059  1.000 133.880 ? 124 PRO GGG CD  1 
ATOM 12216 N N   . ALA G 2 134 ? 67.054  30.971  70.350  1.000 75.770  ? 134 ALA GGG N   1 
ATOM 12217 C CA  . ALA G 2 134 ? 67.325  31.110  68.897  1.000 84.660  ? 134 ALA GGG CA  1 
ATOM 12218 C C   . ALA G 2 134 ? 67.715  29.732  68.330  1.000 102.440 ? 134 ALA GGG C   1 
ATOM 12219 O O   . ALA G 2 134 ? 68.826  29.593  67.766  1.000 110.380 ? 134 ALA GGG O   1 
ATOM 12220 C CB  . ALA G 2 134 ? 68.383  32.171  68.648  1.000 76.850  ? 134 ALA GGG CB  1 
ATOM 12221 N N   . THR G 2 135 ? 66.792  28.768  68.442  1.000 116.500 ? 135 THR GGG N   1 
ATOM 12222 C CA  . THR G 2 135 ? 67.000  27.292  68.289  1.000 117.810 ? 135 THR GGG CA  1 
ATOM 12223 C C   . THR G 2 135 ? 66.596  26.828  66.869  1.000 118.080 ? 135 THR GGG C   1 
ATOM 12224 O O   . THR G 2 135 ? 65.436  26.381  66.708  1.000 139.870 ? 135 THR GGG O   1 
ATOM 12225 C CB  . THR G 2 135 ? 66.274  26.559  69.440  1.000 108.740 ? 135 THR GGG CB  1 
ATOM 12226 O OG1 . THR G 2 135 ? 66.147  25.168  69.142  1.000 108.560 ? 135 THR GGG OG1 1 
ATOM 12227 C CG2 . THR G 2 135 ? 64.881  27.077  69.749  1.000 94.470  ? 135 THR GGG CG2 1 
ATOM 12228 N N   . LEU G 2 136 ? 67.499  26.942  65.877  1.000 101.820 ? 136 LEU GGG N   1 
ATOM 12229 C CA  . LEU G 2 136 ? 67.202  26.694  64.430  1.000 110.330 ? 136 LEU GGG CA  1 
ATOM 12230 C C   . LEU G 2 136 ? 68.059  25.536  63.890  1.000 114.600 ? 136 LEU GGG C   1 
ATOM 12231 O O   . LEU G 2 136 ? 69.226  25.439  64.293  1.000 133.430 ? 136 LEU GGG O   1 
ATOM 12232 C CB  . LEU G 2 136 ? 67.444  27.976  63.624  1.000 103.230 ? 136 LEU GGG CB  1 
ATOM 12233 N N   . VAL G 2 137 ? 67.500  24.711  62.999  1.000 111.180 ? 137 VAL GGG N   1 
ATOM 12234 C CA  . VAL G 2 137 ? 68.051  23.392  62.539  1.000 105.710 ? 137 VAL GGG CA  1 
ATOM 12235 C C   . VAL G 2 137 ? 68.111  23.386  61.004  1.000 110.980 ? 137 VAL GGG C   1 
ATOM 12236 O O   . VAL G 2 137 ? 67.117  23.769  60.381  1.000 118.780 ? 137 VAL GGG O   1 
ATOM 12237 C CB  . VAL G 2 137 ? 67.179  22.224  63.062  1.000 97.090  ? 137 VAL GGG CB  1 
ATOM 12238 C CG1 . VAL G 2 137 ? 67.503  20.911  62.372  1.000 97.460  ? 137 VAL GGG CG1 1 
ATOM 12239 C CG2 . VAL G 2 137 ? 67.274  22.059  64.567  1.000 90.800  ? 137 VAL GGG CG2 1 
ATOM 12240 N N   . CYS G 2 138 ? 69.226  22.939  60.419  1.000 124.410 ? 138 CYS GGG N   1 
ATOM 12241 C CA  . CYS G 2 138 ? 69.509  22.961  58.955  1.000 126.120 ? 138 CYS GGG CA  1 
ATOM 12242 C C   . CYS G 2 138 ? 70.212  21.651  58.561  1.000 123.370 ? 138 CYS GGG C   1 
ATOM 12243 O O   . CYS G 2 138 ? 71.451  21.668  58.426  1.000 129.180 ? 138 CYS GGG O   1 
ATOM 12244 C CB  . CYS G 2 138 ? 70.343  24.192  58.587  1.000 131.170 ? 138 CYS GGG CB  1 
ATOM 12245 S SG  . CYS G 2 138 ? 70.662  24.377  56.813  1.000 134.130 ? 138 CYS GGG SG  1 
ATOM 12246 N N   . LEU G 2 139 ? 69.456  20.558  58.401  1.000 116.820 ? 139 LEU GGG N   1 
ATOM 12247 C CA  . LEU G 2 139 ? 69.977  19.212  58.015  1.000 119.400 ? 139 LEU GGG CA  1 
ATOM 12248 C C   . LEU G 2 139 ? 70.398  19.184  56.530  1.000 119.940 ? 139 LEU GGG C   1 
ATOM 12249 O O   . LEU G 2 139 ? 69.585  19.572  55.686  1.000 136.300 ? 139 LEU GGG O   1 
ATOM 12250 C CB  . LEU G 2 139 ? 68.903  18.155  58.305  1.000 110.310 ? 139 LEU GGG CB  1 
ATOM 12251 C CG  . LEU G 2 139 ? 68.957  17.522  59.696  1.000 107.260 ? 139 LEU GGG CG  1 
ATOM 12252 C CD1 . LEU G 2 139 ? 68.407  18.475  60.742  1.000 104.490 ? 139 LEU GGG CD1 1 
ATOM 12253 C CD2 . LEU G 2 139 ? 68.213  16.195  59.716  1.000 103.560 ? 139 LEU GGG CD2 1 
ATOM 12254 N N   . ILE G 2 140 ? 71.606  18.678  56.241  1.000 107.280 ? 140 ILE GGG N   1 
ATOM 12255 C CA  . ILE G 2 140 ? 72.142  18.367  54.878  1.000 103.990 ? 140 ILE GGG CA  1 
ATOM 12256 C C   . ILE G 2 140 ? 72.184  16.833  54.695  1.000 110.070 ? 140 ILE GGG C   1 
ATOM 12257 O O   . ILE G 2 140 ? 72.520  16.157  55.690  1.000 115.180 ? 140 ILE GGG O   1 
ATOM 12258 C CB  . ILE G 2 140 ? 73.524  19.032  54.724  1.000 85.710  ? 140 ILE GGG CB  1 
ATOM 12259 N N   . SER G 2 141 ? 71.851  16.291  53.505  1.000 124.430 ? 141 SER GGG N   1 
ATOM 12260 C CA  . SER G 2 141 ? 71.519  14.846  53.291  1.000 128.970 ? 141 SER GGG CA  1 
ATOM 12261 C C   . SER G 2 141 ? 72.225  14.225  52.066  1.000 132.830 ? 141 SER GGG C   1 
ATOM 12262 O O   . SER G 2 141 ? 72.836  14.972  51.259  1.000 138.310 ? 141 SER GGG O   1 
ATOM 12263 C CB  . SER G 2 141 ? 70.019  14.648  53.219  1.000 121.190 ? 141 SER GGG CB  1 
ATOM 12264 O OG  . SER G 2 141 ? 69.469  14.526  54.520  1.000 113.110 ? 141 SER GGG OG  1 
ATOM 12265 N N   . ASP G 2 142 ? 72.152  12.886  51.969  1.000 123.360 ? 142 ASP GGG N   1 
ATOM 12266 C CA  . ASP G 2 142 ? 72.830  11.960  51.000  1.000 123.170 ? 142 ASP GGG CA  1 
ATOM 12267 C C   . ASP G 2 142 ? 73.641  12.677  49.898  1.000 139.800 ? 142 ASP GGG C   1 
ATOM 12268 O O   . ASP G 2 142 ? 73.089  12.939  48.817  1.000 151.180 ? 142 ASP GGG O   1 
ATOM 12269 C CB  . ASP G 2 142 ? 71.791  11.025  50.381  1.000 99.410  ? 142 ASP GGG CB  1 
ATOM 12270 N N   . PHE G 2 143 ? 74.946  12.882  50.124  1.000 138.950 ? 143 PHE GGG N   1 
ATOM 12271 C CA  . PHE G 2 143 ? 75.913  13.526  49.190  1.000 117.570 ? 143 PHE GGG CA  1 
ATOM 12272 C C   . PHE G 2 143 ? 77.177  12.658  48.991  1.000 123.440 ? 143 PHE GGG C   1 
ATOM 12273 O O   . PHE G 2 143 ? 77.308  11.609  49.661  1.000 112.330 ? 143 PHE GGG O   1 
ATOM 12274 C CB  . PHE G 2 143 ? 76.311  14.886  49.767  1.000 92.630  ? 143 PHE GGG CB  1 
ATOM 12275 N N   . TYR G 2 144 ? 78.114  13.086  48.117  1.000 138.110 ? 144 TYR GGG N   1 
ATOM 12276 C CA  . TYR G 2 144 ? 79.579  12.756  48.179  1.000 138.920 ? 144 TYR GGG CA  1 
ATOM 12277 C C   . TYR G 2 144 ? 80.247  13.777  49.113  1.000 163.180 ? 144 TYR GGG C   1 
ATOM 12278 O O   . TYR G 2 144 ? 80.151  14.979  48.873  1.000 186.990 ? 144 TYR GGG O   1 
ATOM 12279 C CB  . TYR G 2 144 ? 80.219  12.781  46.790  1.000 30.000  ? 144 TYR GGG CB  1 
ATOM 12280 N N   . PRO G 2 145 ? 80.900  13.353  50.226  1.000 167.260 ? 145 PRO GGG N   1 
ATOM 12281 C CA  . PRO G 2 145 ? 80.996  14.173  51.448  1.000 137.690 ? 145 PRO GGG CA  1 
ATOM 12282 C C   . PRO G 2 145 ? 81.860  15.436  51.319  1.000 107.060 ? 145 PRO GGG C   1 
ATOM 12283 O O   . PRO G 2 145 ? 82.620  15.498  50.385  1.000 115.480 ? 145 PRO GGG O   1 
ATOM 12284 C CB  . PRO G 2 145 ? 81.607  13.221  52.485  1.000 143.320 ? 145 PRO GGG CB  1 
ATOM 12285 C CG  . PRO G 2 145 ? 82.375  12.213  51.653  1.000 157.170 ? 145 PRO GGG CG  1 
ATOM 12286 C CD  . PRO G 2 145 ? 81.618  12.076  50.353  1.000 170.540 ? 145 PRO GGG CD  1 
ATOM 12287 N N   . GLY G 2 146 ? 81.674  16.413  52.223  1.000 84.960  ? 146 GLY GGG N   1 
ATOM 12288 C CA  . GLY G 2 146 ? 82.403  17.703  52.222  1.000 84.050  ? 146 GLY GGG CA  1 
ATOM 12289 C C   . GLY G 2 146 ? 81.580  18.903  51.732  1.000 89.410  ? 146 GLY GGG C   1 
ATOM 12290 O O   . GLY G 2 146 ? 81.939  19.487  50.673  1.000 91.280  ? 146 GLY GGG O   1 
ATOM 12291 N N   . ALA G 2 147 ? 80.550  19.304  52.491  1.000 93.680  ? 147 ALA GGG N   1 
ATOM 12292 C CA  . ALA G 2 147 ? 79.799  20.581  52.323  1.000 84.300  ? 147 ALA GGG CA  1 
ATOM 12293 C C   . ALA G 2 147 ? 80.531  21.746  53.037  1.000 80.560  ? 147 ALA GGG C   1 
ATOM 12294 O O   . ALA G 2 147 ? 81.482  21.495  53.793  1.000 65.160  ? 147 ALA GGG O   1 
ATOM 12295 C CB  . ALA G 2 147 ? 78.370  20.409  52.806  1.000 68.980  ? 147 ALA GGG CB  1 
ATOM 12296 N N   . VAL G 2 148 ? 80.131  22.991  52.762  1.000 88.020  ? 148 VAL GGG N   1 
ATOM 12297 C CA  . VAL G 2 148 ? 80.610  24.229  53.452  1.000 98.560  ? 148 VAL GGG CA  1 
ATOM 12298 C C   . VAL G 2 148 ? 79.406  25.173  53.619  1.000 115.620 ? 148 VAL GGG C   1 
ATOM 12299 O O   . VAL G 2 148 ? 78.608  25.240  52.677  1.000 131.560 ? 148 VAL GGG O   1 
ATOM 12300 C CB  . VAL G 2 148 ? 81.783  24.892  52.696  1.000 93.780  ? 148 VAL GGG CB  1 
ATOM 12301 C CG1 . VAL G 2 148 ? 81.522  25.045  51.206  1.000 91.150  ? 148 VAL GGG CG1 1 
ATOM 12302 C CG2 . VAL G 2 148 ? 82.176  26.234  53.300  1.000 89.590  ? 148 VAL GGG CG2 1 
ATOM 12303 N N   . THR G 2 149 ? 79.284  25.856  54.773  1.000 124.150 ? 149 THR GGG N   1 
ATOM 12304 C CA  . THR G 2 149 ? 78.137  26.721  55.177  1.000 114.160 ? 149 THR GGG CA  1 
ATOM 12305 C C   . THR G 2 149 ? 78.620  28.174  55.354  1.000 98.980  ? 149 THR GGG C   1 
ATOM 12306 O O   . THR G 2 149 ? 79.228  28.453  56.397  1.000 84.880  ? 149 THR GGG O   1 
ATOM 12307 C CB  . THR G 2 149 ? 77.447  26.097  56.402  1.000 115.290 ? 149 THR GGG CB  1 
ATOM 12308 O OG1 . THR G 2 149 ? 76.989  24.814  55.978  1.000 106.340 ? 149 THR GGG OG1 1 
ATOM 12309 C CG2 . THR G 2 149 ? 76.278  26.890  56.951  1.000 121.920 ? 149 THR GGG CG2 1 
ATOM 12310 N N   . GLY G 2 162 ? 77.037  32.739  64.752  1.000 82.660  ? 162 GLY GGG N   1 
ATOM 12311 C CA  . GLY G 2 162 ? 76.782  31.707  65.780  1.000 93.730  ? 162 GLY GGG CA  1 
ATOM 12312 C C   . GLY G 2 162 ? 76.406  30.347  65.194  1.000 104.960 ? 162 GLY GGG C   1 
ATOM 12313 O O   . GLY G 2 162 ? 75.652  29.607  65.872  1.000 106.620 ? 162 GLY GGG O   1 
ATOM 12314 N N   . VAL G 2 163 ? 76.915  30.005  64.000  1.000 113.790 ? 163 VAL GGG N   1 
ATOM 12315 C CA  . VAL G 2 163 ? 76.696  28.678  63.339  1.000 125.840 ? 163 VAL GGG CA  1 
ATOM 12316 C C   . VAL G 2 163 ? 77.483  27.611  64.108  1.000 124.270 ? 163 VAL GGG C   1 
ATOM 12317 O O   . VAL G 2 163 ? 78.591  27.920  64.576  1.000 129.900 ? 163 VAL GGG O   1 
ATOM 12318 C CB  . VAL G 2 163 ? 77.091  28.662  61.841  1.000 133.480 ? 163 VAL GGG CB  1 
ATOM 12319 C CG1 . VAL G 2 163 ? 76.256  29.642  61.035  1.000 138.420 ? 163 VAL GGG CG1 1 
ATOM 12320 C CG2 . VAL G 2 163 ? 78.581  28.881  61.595  1.000 127.540 ? 163 VAL GGG CG2 1 
ATOM 12321 N N   . GLU G 2 164 ? 76.931  26.400  64.200  1.000 119.080 ? 164 GLU GGG N   1 
ATOM 12322 C CA  . GLU G 2 164 ? 77.584  25.203  64.794  1.000 118.080 ? 164 GLU GGG CA  1 
ATOM 12323 C C   . GLU G 2 164 ? 77.380  24.037  63.816  1.000 114.930 ? 164 GLU GGG C   1 
ATOM 12324 O O   . GLU G 2 164 ? 76.283  23.473  63.827  1.000 128.410 ? 164 GLU GGG O   1 
ATOM 12325 C CB  . GLU G 2 164 ? 76.992  24.970  66.191  1.000 112.300 ? 164 GLU GGG CB  1 
ATOM 12326 C CG  . GLU G 2 164 ? 77.848  24.116  67.113  1.000 103.880 ? 164 GLU GGG CG  1 
ATOM 12327 C CD  . GLU G 2 164 ? 78.369  24.840  68.341  1.000 94.170  ? 164 GLU GGG CD  1 
ATOM 12328 O OE1 . GLU G 2 164 ? 77.550  25.468  69.041  1.000 80.290  ? 164 GLU GGG OE1 1 
ATOM 12329 O OE2 . GLU G 2 164 ? 79.590  24.757  68.605  1.000 89.540  ? 164 GLU GGG OE2 1 
ATOM 12330 N N   . THR G 2 165 ? 78.399  23.711  62.996  1.000 110.230 ? 165 THR GGG N   1 
ATOM 12331 C CA  . THR G 2 165 ? 78.325  22.709  61.884  1.000 111.190 ? 165 THR GGG CA  1 
ATOM 12332 C C   . THR G 2 165 ? 79.077  21.411  62.257  1.000 101.950 ? 165 THR GGG C   1 
ATOM 12333 O O   . THR G 2 165 ? 80.158  21.500  62.872  1.000 91.020  ? 165 THR GGG O   1 
ATOM 12334 C CB  . THR G 2 165 ? 78.852  23.315  60.570  1.000 111.380 ? 165 THR GGG CB  1 
ATOM 12335 O OG1 . THR G 2 165 ? 78.350  24.651  60.443  1.000 106.880 ? 165 THR GGG OG1 1 
ATOM 12336 C CG2 . THR G 2 165 ? 78.498  22.500  59.340  1.000 98.130  ? 165 THR GGG CG2 1 
ATOM 12337 N N   . THR G 2 166 ? 78.539  20.249  61.856  1.000 97.790  ? 166 THR GGG N   1 
ATOM 12338 C CA  . THR G 2 166 ? 79.045  18.891  62.214  1.000 98.110  ? 166 THR GGG CA  1 
ATOM 12339 C C   . THR G 2 166 ? 80.017  18.370  61.140  1.000 98.530  ? 166 THR GGG C   1 
ATOM 12340 O O   . THR G 2 166 ? 80.013  18.901  60.000  1.000 95.620  ? 166 THR GGG O   1 
ATOM 12341 C CB  . THR G 2 166 ? 77.888  17.913  62.470  1.000 92.060  ? 166 THR GGG CB  1 
ATOM 12342 O OG1 . THR G 2 166 ? 78.374  16.962  63.408  1.000 90.960  ? 166 THR GGG OG1 1 
ATOM 12343 C CG2 . THR G 2 166 ? 77.400  17.171  61.246  1.000 95.470  ? 166 THR GGG CG2 1 
ATOM 12344 N N   . LYS G 2 167 ? 80.815  17.358  61.497  1.000 93.530  ? 167 LYS GGG N   1 
ATOM 12345 C CA  . LYS G 2 167 ? 81.605  16.545  60.538  1.000 92.680  ? 167 LYS GGG CA  1 
ATOM 12346 C C   . LYS G 2 167 ? 80.617  15.741  59.691  1.000 96.010  ? 167 LYS GGG C   1 
ATOM 12347 O O   . LYS G 2 167 ? 79.643  15.187  60.215  1.000 87.550  ? 167 LYS GGG O   1 
ATOM 12348 C CB  . LYS G 2 167 ? 82.602  15.645  61.279  1.000 86.160  ? 167 LYS GGG CB  1 
ATOM 12349 N N   . PRO G 2 168 ? 80.815  15.682  58.351  1.000 95.200  ? 168 PRO GGG N   1 
ATOM 12350 C CA  . PRO G 2 168 ? 80.072  14.750  57.495  1.000 93.360  ? 168 PRO GGG CA  1 
ATOM 12351 C C   . PRO G 2 168 ? 80.173  13.289  57.967  1.000 91.530  ? 168 PRO GGG C   1 
ATOM 12352 O O   . PRO G 2 168 ? 81.266  12.878  58.299  1.000 96.730  ? 168 PRO GGG O   1 
ATOM 12353 C CB  . PRO G 2 168 ? 80.756  14.901  56.120  1.000 93.320  ? 168 PRO GGG CB  1 
ATOM 12354 C CG  . PRO G 2 168 ? 81.396  16.281  56.141  1.000 90.910  ? 168 PRO GGG CG  1 
ATOM 12355 C CD  . PRO G 2 168 ? 81.748  16.537  57.590  1.000 92.320  ? 168 PRO GGG CD  1 
ATOM 12356 N N   . SER G 2 169 ? 79.058  12.545  57.996  1.000 91.770  ? 169 SER GGG N   1 
ATOM 12357 C CA  . SER G 2 169 ? 79.023  11.097  58.347  1.000 95.670  ? 169 SER GGG CA  1 
ATOM 12358 C C   . SER G 2 169 ? 78.765  10.217  57.105  1.000 102.030 ? 169 SER GGG C   1 
ATOM 12359 O O   . SER G 2 169 ? 77.793  10.495  56.394  1.000 120.990 ? 169 SER GGG O   1 
ATOM 12360 C CB  . SER G 2 169 ? 78.009  10.833  59.425  1.000 87.380  ? 169 SER GGG CB  1 
ATOM 12361 O OG  . SER G 2 169 ? 77.718  9.443   59.490  1.000 78.910  ? 169 SER GGG OG  1 
ATOM 12362 N N   . LYS G 2 170 ? 79.605  9.195   56.862  1.000 100.830 ? 170 LYS GGG N   1 
ATOM 12363 C CA  . LYS G 2 170 ? 79.341  8.123   55.860  1.000 97.490  ? 170 LYS GGG CA  1 
ATOM 12364 C C   . LYS G 2 170 ? 78.079  7.387   56.331  1.000 109.420 ? 170 LYS GGG C   1 
ATOM 12365 O O   . LYS G 2 170 ? 78.097  6.882   57.480  1.000 97.570  ? 170 LYS GGG O   1 
ATOM 12366 C CB  . LYS G 2 170 ? 80.540  7.179   55.681  1.000 75.980  ? 170 LYS GGG CB  1 
ATOM 12367 N N   . GLN G 2 171 ? 77.003  7.426   55.525  1.000 121.060 ? 171 GLN GGG N   1 
ATOM 12368 C CA  . GLN G 2 171 ? 75.696  6.773   55.823  1.000 109.270 ? 171 GLN GGG CA  1 
ATOM 12369 C C   . GLN G 2 171 ? 75.797  5.335   55.315  1.000 110.250 ? 171 GLN GGG C   1 
ATOM 12370 O O   . GLN G 2 171 ? 76.700  5.068   54.491  1.000 100.830 ? 171 GLN GGG O   1 
ATOM 12371 C CB  . GLN G 2 171 ? 74.514  7.532   55.205  1.000 92.430  ? 171 GLN GGG CB  1 
ATOM 12372 N N   . SER G 2 172 ? 74.928  4.442   55.805  1.000 121.460 ? 172 SER GGG N   1 
ATOM 12373 C CA  . SER G 2 172 ? 74.979  2.973   55.554  1.000 120.470 ? 172 SER GGG CA  1 
ATOM 12374 C C   . SER G 2 172 ? 74.637  2.657   54.090  1.000 121.250 ? 172 SER GGG C   1 
ATOM 12375 O O   . SER G 2 172 ? 74.831  1.497   53.691  1.000 116.070 ? 172 SER GGG O   1 
ATOM 12376 C CB  . SER G 2 172 ? 74.077  2.233   56.504  1.000 110.090 ? 172 SER GGG CB  1 
ATOM 12377 O OG  . SER G 2 172 ? 72.736  2.651   56.331  1.000 102.240 ? 172 SER GGG OG  1 
ATOM 12378 N N   . ASN G 2 173 ? 74.149  3.645   53.329  1.000 122.600 ? 173 ASN GGG N   1 
ATOM 12379 C CA  . ASN G 2 173 ? 73.912  3.554   51.861  1.000 120.830 ? 173 ASN GGG CA  1 
ATOM 12380 C C   . ASN G 2 173 ? 75.161  4.078   51.107  1.000 121.990 ? 173 ASN GGG C   1 
ATOM 12381 O O   . ASN G 2 173 ? 75.020  4.445   49.923  1.000 108.440 ? 173 ASN GGG O   1 
ATOM 12382 C CB  . ASN G 2 173 ? 72.634  4.293   51.471  1.000 119.870 ? 173 ASN GGG CB  1 
ATOM 12383 C CG  . ASN G 2 173 ? 72.630  5.792   51.732  1.000 117.060 ? 173 ASN GGG CG  1 
ATOM 12384 O OD1 . ASN G 2 173 ? 73.550  6.342   52.333  1.000 137.330 ? 173 ASN GGG OD1 1 
ATOM 12385 N ND2 . ASN G 2 173 ? 71.630  6.483   51.242  1.000 99.190  ? 173 ASN GGG ND2 1 
ATOM 12386 N N   . ASN G 2 174 ? 76.327  4.065   51.751  1.000 116.930 ? 174 ASN GGG N   1 
ATOM 12387 C CA  . ASN G 2 174 ? 77.562  4.827   51.366  1.000 106.510 ? 174 ASN GGG CA  1 
ATOM 12388 C C   . ASN G 2 174 ? 77.158  6.153   50.684  1.000 106.800 ? 174 ASN GGG C   1 
ATOM 12389 O O   . ASN G 2 174 ? 77.461  6.325   49.496  1.000 109.130 ? 174 ASN GGG O   1 
ATOM 12390 C CB  . ASN G 2 174 ? 78.532  3.949   50.562  1.000 86.620  ? 174 ASN GGG CB  1 
ATOM 12391 N N   . LYS G 2 175 ? 76.477  7.040   51.421  1.000 118.420 ? 175 LYS GGG N   1 
ATOM 12392 C CA  . LYS G 2 175 ? 76.184  8.464   51.070  1.000 127.920 ? 175 LYS GGG CA  1 
ATOM 12393 C C   . LYS G 2 175 ? 76.396  9.312   52.334  1.000 139.570 ? 175 LYS GGG C   1 
ATOM 12394 O O   . LYS G 2 175 ? 76.158  8.770   53.436  1.000 158.630 ? 175 LYS GGG O   1 
ATOM 12395 C CB  . LYS G 2 175 ? 74.760  8.611   50.507  1.000 125.660 ? 175 LYS GGG CB  1 
ATOM 12396 N N   . THR G 2 176 ? 76.829  10.574  52.207  1.000 137.200 ? 176 THR GGG N   1 
ATOM 12397 C CA  . THR G 2 176 ? 77.378  11.367  53.345  1.000 140.240 ? 176 THR GGG CA  1 
ATOM 12398 C C   . THR G 2 176 ? 76.406  12.475  53.796  1.000 133.870 ? 176 THR GGG C   1 
ATOM 12399 O O   . THR G 2 176 ? 76.111  13.404  53.006  1.000 104.980 ? 176 THR GGG O   1 
ATOM 12400 C CB  . THR G 2 176 ? 78.735  11.985  52.961  1.000 30.000  ? 176 THR GGG CB  1 
ATOM 12401 O OG1 . THR G 2 176 ? 78.570  12.836  51.821  1.000 30.000  ? 176 THR GGG OG1 1 
ATOM 12402 C CG2 . THR G 2 176 ? 79.689  10.911  52.462  1.000 30.000  ? 176 THR GGG CG2 1 
ATOM 12403 N N   . ALA G 2 177 ? 75.990  12.406  55.069  1.000 139.690 ? 177 ALA GGG N   1 
ATOM 12404 C CA  . ALA G 2 177 ? 75.021  13.313  55.739  1.000 149.980 ? 177 ALA GGG CA  1 
ATOM 12405 C C   . ALA G 2 177 ? 75.715  14.160  56.824  1.000 157.400 ? 177 ALA GGG C   1 
ATOM 12406 O O   . ALA G 2 177 ? 76.655  13.661  57.488  1.000 172.210 ? 177 ALA GGG O   1 
ATOM 12407 C CB  . ALA G 2 177 ? 73.885  12.499  56.322  1.000 152.580 ? 177 ALA GGG CB  1 
ATOM 12408 N N   . ALA G 2 178 ? 75.256  15.406  57.001  1.000 146.680 ? 178 ALA GGG N   1 
ATOM 12409 C CA  . ALA G 2 178 ? 75.723  16.392  58.008  1.000 130.000 ? 178 ALA GGG CA  1 
ATOM 12410 C C   . ALA G 2 178 ? 74.514  17.105  58.639  1.000 119.670 ? 178 ALA GGG C   1 
ATOM 12411 O O   . ALA G 2 178 ? 73.376  16.785  58.260  1.000 129.130 ? 178 ALA GGG O   1 
ATOM 12412 C CB  . ALA G 2 178 ? 76.648  17.375  57.334  1.000 118.700 ? 178 ALA GGG CB  1 
ATOM 12413 N N   . SER G 2 179 ? 74.762  18.035  59.566  1.000 105.260 ? 179 SER GGG N   1 
ATOM 12414 C CA  . SER G 2 179 ? 73.766  18.928  60.215  1.000 101.040 ? 179 SER GGG CA  1 
ATOM 12415 C C   . SER G 2 179 ? 74.470  20.222  60.647  1.000 98.090  ? 179 SER GGG C   1 
ATOM 12416 O O   . SER G 2 179 ? 75.648  20.151  60.999  1.000 99.110  ? 179 SER GGG O   1 
ATOM 12417 C CB  . SER G 2 179 ? 73.035  18.259  61.384  1.000 103.740 ? 179 SER GGG CB  1 
ATOM 12418 O OG  . SER G 2 179 ? 73.857  17.364  62.130  1.000 102.500 ? 179 SER GGG OG  1 
ATOM 12419 N N   . SER G 2 180 ? 73.765  21.357  60.599  1.000 101.000 ? 180 SER GGG N   1 
ATOM 12420 C CA  . SER G 2 180 ? 74.228  22.703  61.034  1.000 108.590 ? 180 SER GGG CA  1 
ATOM 12421 C C   . SER G 2 180 ? 73.098  23.423  61.789  1.000 126.340 ? 180 SER GGG C   1 
ATOM 12422 O O   . SER G 2 180 ? 71.939  23.301  61.359  1.000 157.600 ? 180 SER GGG O   1 
ATOM 12423 C CB  . SER G 2 180 ? 74.703  23.503  59.852  1.000 105.030 ? 180 SER GGG CB  1 
ATOM 12424 O OG  . SER G 2 180 ? 75.000  24.844  60.219  1.000 118.910 ? 180 SER GGG OG  1 
ATOM 12425 N N   . TYR G 2 181 ? 73.424  24.151  62.869  1.000 131.800 ? 181 TYR GGG N   1 
ATOM 12426 C CA  . TYR G 2 181 ? 72.449  24.785  63.821  1.000 121.280 ? 181 TYR GGG CA  1 
ATOM 12427 C C   . TYR G 2 181 ? 72.762  26.291  63.910  1.000 120.650 ? 181 TYR GGG C   1 
ATOM 12428 O O   . TYR G 2 181 ? 73.969  26.606  63.988  1.000 115.910 ? 181 TYR GGG O   1 
ATOM 12429 C CB  . TYR G 2 181 ? 72.500  24.065  65.178  1.000 115.660 ? 181 TYR GGG CB  1 
ATOM 12430 C CG  . TYR G 2 181 ? 72.167  22.586  65.164  1.000 114.840 ? 181 TYR GGG CG  1 
ATOM 12431 C CD1 . TYR G 2 181 ? 73.023  21.646  64.607  1.000 111.570 ? 181 TYR GGG CD1 1 
ATOM 12432 C CD2 . TYR G 2 181 ? 71.023  22.098  65.781  1.000 109.250 ? 181 TYR GGG CD2 1 
ATOM 12433 C CE1 . TYR G 2 181 ? 72.723  20.292  64.593  1.000 110.340 ? 181 TYR GGG CE1 1 
ATOM 12434 C CE2 . TYR G 2 181 ? 70.715  20.745  65.795  1.000 107.750 ? 181 TYR GGG CE2 1 
ATOM 12435 C CZ  . TYR G 2 181 ? 71.568  19.832  65.198  1.000 108.040 ? 181 TYR GGG CZ  1 
ATOM 12436 O OH  . TYR G 2 181 ? 71.296  18.491  65.210  1.000 92.230  ? 181 TYR GGG OH  1 
ATOM 12437 N N   . LEU G 2 182 ? 71.735  27.166  63.834  1.000 124.970 ? 182 LEU GGG N   1 
ATOM 12438 C CA  . LEU G 2 182 ? 71.847  28.655  63.673  1.000 118.900 ? 182 LEU GGG CA  1 
ATOM 12439 C C   . LEU G 2 182 ? 70.478  29.302  63.909  1.000 102.750 ? 182 LEU GGG C   1 
ATOM 12440 O O   . LEU G 2 182 ? 69.960  29.107  65.009  1.000 87.500  ? 182 LEU GGG O   1 
ATOM 12441 C CB  . LEU G 2 182 ? 72.413  29.025  62.284  1.000 123.890 ? 182 LEU GGG CB  1 
ATOM 12442 C CG  . LEU G 2 182 ? 71.471  28.945  61.070  1.000 119.820 ? 182 LEU GGG CG  1 
ATOM 12443 C CD1 . LEU G 2 182 ? 70.612  30.200  60.925  1.000 110.740 ? 182 LEU GGG CD1 1 
ATOM 12444 C CD2 . LEU G 2 182 ? 72.261  28.700  59.782  1.000 107.930 ? 182 LEU GGG CD2 1 
ATOM 12445 N N   . TYR G 2 195 ? 67.903  35.098  57.640  1.000 135.560 ? 195 TYR GGG N   1 
ATOM 12446 C CA  . TYR G 2 195 ? 68.952  34.053  57.797  1.000 127.550 ? 195 TYR GGG CA  1 
ATOM 12447 C C   . TYR G 2 195 ? 68.716  32.935  56.769  1.000 133.320 ? 195 TYR GGG C   1 
ATOM 12448 O O   . TYR G 2 195 ? 67.587  32.403  56.698  1.000 131.910 ? 195 TYR GGG O   1 
ATOM 12449 C CB  . TYR G 2 195 ? 68.963  33.508  59.230  1.000 109.150 ? 195 TYR GGG CB  1 
ATOM 12450 N N   . SER G 2 196 ? 69.766  32.577  56.016  1.000 137.600 ? 196 SER GGG N   1 
ATOM 12451 C CA  . SER G 2 196 ? 69.793  31.444  55.047  1.000 145.450 ? 196 SER GGG CA  1 
ATOM 12452 C C   . SER G 2 196 ? 70.777  30.359  55.518  1.000 155.360 ? 196 SER GGG C   1 
ATOM 12453 O O   . SER G 2 196 ? 71.360  30.507  56.623  1.000 141.290 ? 196 SER GGG O   1 
ATOM 12454 C CB  . SER G 2 196 ? 70.141  31.922  53.656  1.000 140.740 ? 196 SER GGG CB  1 
ATOM 12455 O OG  . SER G 2 196 ? 69.328  33.013  53.260  1.000 145.110 ? 196 SER GGG OG  1 
ATOM 12456 N N   . CYS G 2 197 ? 70.934  29.298  54.714  1.000 172.820 ? 197 CYS GGG N   1 
ATOM 12457 C CA  . CYS G 2 197 ? 71.840  28.138  54.956  1.000 170.120 ? 197 CYS GGG CA  1 
ATOM 12458 C C   . CYS G 2 197 ? 72.435  27.668  53.614  1.000 167.300 ? 197 CYS GGG C   1 
ATOM 12459 O O   . CYS G 2 197 ? 71.972  26.634  53.100  1.000 164.490 ? 197 CYS GGG O   1 
ATOM 12460 C CB  . CYS G 2 197 ? 71.051  27.035  55.659  1.000 158.590 ? 197 CYS GGG CB  1 
ATOM 12461 S SG  . CYS G 2 197 ? 72.024  25.888  56.666  1.000 151.820 ? 197 CYS GGG SG  1 
ATOM 12462 N N   . GLN G 2 198 ? 73.392  28.413  53.043  1.000 158.540 ? 198 GLN GGG N   1 
ATOM 12463 C CA  . GLN G 2 198 ? 74.052  28.080  51.746  1.000 151.670 ? 198 GLN GGG CA  1 
ATOM 12464 C C   . GLN G 2 198 ? 75.002  26.893  51.972  1.000 156.010 ? 198 GLN GGG C   1 
ATOM 12465 O O   . GLN G 2 198 ? 75.891  27.048  52.819  1.000 158.490 ? 198 GLN GGG O   1 
ATOM 12466 C CB  . GLN G 2 198 ? 74.786  29.307  51.173  1.000 130.150 ? 198 GLN GGG CB  1 
ATOM 12467 N N   . VAL G 2 199 ? 74.810  25.757  51.280  1.000 161.390 ? 199 VAL GGG N   1 
ATOM 12468 C CA  . VAL G 2 199 ? 75.740  24.581  51.287  1.000 165.750 ? 199 VAL GGG CA  1 
ATOM 12469 C C   . VAL G 2 199 ? 76.201  24.295  49.852  1.000 159.280 ? 199 VAL GGG C   1 
ATOM 12470 O O   . VAL G 2 199 ? 75.352  23.950  49.015  1.000 154.770 ? 199 VAL GGG O   1 
ATOM 12471 C CB  . VAL G 2 199 ? 75.112  23.322  51.934  1.000 173.470 ? 199 VAL GGG CB  1 
ATOM 12472 C CG1 . VAL G 2 199 ? 74.669  23.588  53.362  1.000 171.770 ? 199 VAL GGG CG1 1 
ATOM 12473 C CG2 . VAL G 2 199 ? 73.983  22.733  51.114  1.000 171.090 ? 199 VAL GGG CG2 1 
ATOM 12474 N N   . THR G 2 200 ? 77.510  24.441  49.587  1.000 154.300 ? 200 THR GGG N   1 
ATOM 12475 C CA  . THR G 2 200 ? 78.177  24.207  48.272  1.000 155.620 ? 200 THR GGG CA  1 
ATOM 12476 C C   . THR G 2 200 ? 78.764  22.787  48.244  1.000 153.880 ? 200 THR GGG C   1 
ATOM 12477 O O   . THR G 2 200 ? 78.995  22.226  49.326  1.000 159.580 ? 200 THR GGG O   1 
ATOM 12478 C CB  . THR G 2 200 ? 79.231  25.294  48.004  1.000 147.360 ? 200 THR GGG CB  1 
ATOM 12479 O OG1 . THR G 2 200 ? 78.610  26.553  48.267  1.000 139.060 ? 200 THR GGG OG1 1 
ATOM 12480 C CG2 . THR G 2 200 ? 79.782  25.302  46.592  1.000 135.570 ? 200 THR GGG CG2 1 
ATOM 12481 N N   . HIS G 2 201 ? 79.007  22.228  47.053  1.000 147.040 ? 201 HIS GGG N   1 
ATOM 12482 C CA  . HIS G 2 201 ? 79.642  20.896  46.864  1.000 137.680 ? 201 HIS GGG CA  1 
ATOM 12483 C C   . HIS G 2 201 ? 80.108  20.733  45.409  1.000 137.220 ? 201 HIS GGG C   1 
ATOM 12484 O O   . HIS G 2 201 ? 79.258  20.454  44.540  1.000 143.460 ? 201 HIS GGG O   1 
ATOM 12485 C CB  . HIS G 2 201 ? 78.679  19.787  47.311  1.000 134.370 ? 201 HIS GGG CB  1 
ATOM 12486 C CG  . HIS G 2 201 ? 79.143  18.425  46.920  1.000 138.740 ? 201 HIS GGG CG  1 
ATOM 12487 N ND1 . HIS G 2 201 ? 78.294  17.342  46.827  1.000 125.040 ? 201 HIS GGG ND1 1 
ATOM 12488 C CD2 . HIS G 2 201 ? 80.361  17.993  46.529  1.000 147.380 ? 201 HIS GGG CD2 1 
ATOM 12489 C CE1 . HIS G 2 201 ? 78.979  16.285  46.437  1.000 128.080 ? 201 HIS GGG CE1 1 
ATOM 12490 N NE2 . HIS G 2 201 ? 80.250  16.658  46.251  1.000 152.650 ? 201 HIS GGG NE2 1 
ATOM 12491 N N   . GLU G 2 202 ? 81.415  20.861  45.166  1.000 131.660 ? 202 GLU GGG N   1 
ATOM 12492 C CA  . GLU G 2 202 ? 82.023  20.831  43.809  1.000 129.160 ? 202 GLU GGG CA  1 
ATOM 12493 C C   . GLU G 2 202 ? 81.479  22.026  43.002  1.000 137.620 ? 202 GLU GGG C   1 
ATOM 12494 O O   . GLU G 2 202 ? 80.939  21.800  41.904  1.000 132.830 ? 202 GLU GGG O   1 
ATOM 12495 C CB  . GLU G 2 202 ? 81.760  19.466  43.164  1.000 105.410 ? 202 GLU GGG CB  1 
ATOM 12496 N N   . GLY G 2 203 ? 81.584  23.242  43.565  1.000 145.780 ? 203 GLY GGG N   1 
ATOM 12497 C CA  . GLY G 2 203 ? 81.266  24.542  42.929  1.000 139.250 ? 203 GLY GGG CA  1 
ATOM 12498 C C   . GLY G 2 203 ? 79.777  24.804  42.710  1.000 136.360 ? 203 GLY GGG C   1 
ATOM 12499 O O   . GLY G 2 203 ? 79.477  25.796  42.017  1.000 130.150 ? 203 GLY GGG O   1 
ATOM 12500 N N   . THR G 2 204 ? 78.879  23.983  43.283  1.000 138.500 ? 204 THR GGG N   1 
ATOM 12501 C CA  . THR G 2 204 ? 77.413  23.952  43.008  1.000 129.950 ? 204 THR GGG CA  1 
ATOM 12502 C C   . THR G 2 204 ? 76.598  24.038  44.318  1.000 138.470 ? 204 THR GGG C   1 
ATOM 12503 O O   . THR G 2 204 ? 76.350  22.964  44.940  1.000 124.870 ? 204 THR GGG O   1 
ATOM 12504 C CB  . THR G 2 204 ? 77.035  22.676  42.233  1.000 30.000  ? 204 THR GGG CB  1 
ATOM 12505 O OG1 . THR G 2 204 ? 77.407  21.523  42.995  1.000 30.000  ? 204 THR GGG OG1 1 
ATOM 12506 C CG2 . THR G 2 204 ? 77.877  22.549  40.972  1.000 30.000  ? 204 THR GGG CG2 1 
ATOM 12507 N N   . THR G 2 205 ? 76.174  25.264  44.695  1.000 140.830 ? 205 THR GGG N   1 
ATOM 12508 C CA  . THR G 2 205 ? 75.494  25.653  45.978  1.000 131.260 ? 205 THR GGG CA  1 
ATOM 12509 C C   . THR G 2 205 ? 73.978  25.382  45.894  1.000 123.440 ? 205 THR GGG C   1 
ATOM 12510 O O   . THR G 2 205 ? 73.436  25.450  44.778  1.000 109.440 ? 205 THR GGG O   1 
ATOM 12511 C CB  . THR G 2 205 ? 75.804  27.124  46.317  1.000 120.820 ? 205 THR GGG CB  1 
ATOM 12512 O OG1 . THR G 2 205 ? 77.217  27.303  46.199  1.000 112.660 ? 205 THR GGG OG1 1 
ATOM 12513 C CG2 . THR G 2 205 ? 75.374  27.565  47.702  1.000 111.910 ? 205 THR GGG CG2 1 
ATOM 12514 N N   . VAL G 2 206 ? 73.315  25.101  47.032  1.000 131.490 ? 206 VAL GGG N   1 
ATOM 12515 C CA  . VAL G 2 206 ? 71.878  24.671  47.102  1.000 141.540 ? 206 VAL GGG CA  1 
ATOM 12516 C C   . VAL G 2 206 ? 71.191  25.327  48.316  1.000 145.180 ? 206 VAL GGG C   1 
ATOM 12517 O O   . VAL G 2 206 ? 70.419  24.622  48.999  1.000 146.970 ? 206 VAL GGG O   1 
ATOM 12518 C CB  . VAL G 2 206 ? 71.740  23.130  47.144  1.000 140.330 ? 206 VAL GGG CB  1 
ATOM 12519 C CG1 . VAL G 2 206 ? 70.302  22.678  46.907  1.000 136.330 ? 206 VAL GGG CG1 1 
ATOM 12520 C CG2 . VAL G 2 206 ? 72.672  22.433  46.156  1.000 130.930 ? 206 VAL GGG CG2 1 
ATOM 12521 N N   . GLU G 2 207 ? 71.427  26.629  48.548  1.000 146.980 ? 207 GLU GGG N   1 
ATOM 12522 C CA  . GLU G 2 207 ? 70.881  27.426  49.691  1.000 142.660 ? 207 GLU GGG CA  1 
ATOM 12523 C C   . GLU G 2 207 ? 69.344  27.409  49.668  1.000 141.310 ? 207 GLU GGG C   1 
ATOM 12524 O O   . GLU G 2 207 ? 68.768  27.767  48.620  1.000 152.880 ? 207 GLU GGG O   1 
ATOM 12525 C CB  . GLU G 2 207 ? 71.375  28.880  49.657  1.000 125.740 ? 207 GLU GGG CB  1 
ATOM 12526 N N   . LYS G 2 208 ? 68.711  26.972  50.767  1.000 125.840 ? 208 LYS GGG N   1 
ATOM 12527 C CA  . LYS G 2 208 ? 67.285  27.245  51.102  1.000 114.450 ? 208 LYS GGG CA  1 
ATOM 12528 C C   . LYS G 2 208 ? 67.282  28.358  52.169  1.000 119.430 ? 208 LYS GGG C   1 
ATOM 12529 O O   . LYS G 2 208 ? 68.316  28.487  52.875  1.000 115.040 ? 208 LYS GGG O   1 
ATOM 12530 C CB  . LYS G 2 208 ? 66.565  25.947  51.508  1.000 92.980  ? 208 LYS GGG CB  1 
ATOM 12531 N N   . THR G 2 209 ? 66.216  29.171  52.248  1.000 128.540 ? 209 THR GGG N   1 
ATOM 12532 C CA  . THR G 2 209 ? 66.095  30.341  53.172  1.000 123.380 ? 209 THR GGG CA  1 
ATOM 12533 C C   . THR G 2 209 ? 64.833  30.217  54.046  1.000 123.230 ? 209 THR GGG C   1 
ATOM 12534 O O   . THR G 2 209 ? 63.909  29.456  53.678  1.000 93.230  ? 209 THR GGG O   1 
ATOM 12535 C CB  . THR G 2 209 ? 66.113  31.674  52.406  1.000 110.630 ? 209 THR GGG CB  1 
ATOM 12536 O OG1 . THR G 2 209 ? 67.134  31.590  51.397  1.000 88.750  ? 209 THR GGG OG1 1 
ATOM 12537 C CG2 . THR G 2 209 ? 66.379  32.871  53.299  1.000 105.570 ? 209 THR GGG CG2 1 
ATOM 12538 N N   . VAL G 2 210 ? 64.829  30.923  55.183  1.000 126.040 ? 210 VAL GGG N   1 
ATOM 12539 C CA  . VAL G 2 210 ? 63.700  31.003  56.159  1.000 130.580 ? 210 VAL GGG CA  1 
ATOM 12540 C C   . VAL G 2 210 ? 63.773  32.382  56.831  1.000 143.690 ? 210 VAL GGG C   1 
ATOM 12541 O O   . VAL G 2 210 ? 64.858  33.017  56.723  1.000 133.900 ? 210 VAL GGG O   1 
ATOM 12542 C CB  . VAL G 2 210 ? 63.770  29.840  57.170  1.000 125.850 ? 210 VAL GGG CB  1 
ATOM 12543 C CG1 . VAL G 2 210 ? 62.765  29.983  58.304  1.000 128.560 ? 210 VAL GGG CG1 1 
ATOM 12544 C CG2 . VAL G 2 210 ? 63.600  28.490  56.491  1.000 121.780 ? 210 VAL GGG CG2 1 
ATOM 12545 N N   . ALA G 2 211 ? 62.661  32.847  57.433  1.000 159.990 ? 211 ALA GGG N   1 
ATOM 12546 C CA  . ALA G 2 211 ? 62.537  34.140  58.160  1.000 153.900 ? 211 ALA GGG CA  1 
ATOM 12547 C C   . ALA G 2 211 ? 61.424  34.099  59.218  1.000 157.970 ? 211 ALA GGG C   1 
ATOM 12548 O O   . ALA G 2 211 ? 60.294  34.513  58.940  1.000 142.940 ? 211 ALA GGG O   1 
ATOM 12549 C CB  . ALA G 2 211 ? 62.302  35.268  57.171  1.000 128.890 ? 211 ALA GGG CB  1 
ATOM 12550 N N   . PRO G 2 212 ? 61.694  33.646  60.476  1.000 154.230 ? 212 PRO GGG N   1 
ATOM 12551 C CA  . PRO G 2 212 ? 60.797  33.930  61.606  1.000 137.390 ? 212 PRO GGG CA  1 
ATOM 12552 C C   . PRO G 2 212 ? 60.373  35.411  61.642  1.000 110.630 ? 212 PRO GGG C   1 
ATOM 12553 O O   . PRO G 2 212 ? 59.905  35.962  62.627  1.000 93.510  ? 212 PRO GGG O   1 
ATOM 12554 C CB  . PRO G 2 212 ? 61.641  33.533  62.836  1.000 132.330 ? 212 PRO GGG CB  1 
ATOM 12555 C CG  . PRO G 2 212 ? 62.565  32.443  62.320  1.000 127.770 ? 212 PRO GGG CG  1 
ATOM 12556 C CD  . PRO G 2 212 ? 62.847  32.815  60.876  1.000 135.300 ? 212 PRO GGG CD  1 
ATOM 12557 N N   . GLU H 3 1   ? 105.625 -9.914  66.925  1.000 49.010  ? 1   GLU HHH N   1 
ATOM 12558 C CA  . GLU H 3 1   ? 105.287 -8.537  66.525  1.000 49.640  ? 1   GLU HHH CA  1 
ATOM 12559 C C   . GLU H 3 1   ? 105.899 -7.581  67.557  1.000 48.710  ? 1   GLU HHH C   1 
ATOM 12560 O O   . GLU H 3 1   ? 106.474 -8.013  68.551  1.000 45.140  ? 1   GLU HHH O   1 
ATOM 12561 C CB  . GLU H 3 1   ? 103.766 -8.358  66.372  1.000 48.070  ? 1   GLU HHH CB  1 
ATOM 12562 N N   . VAL H 3 2   ? 105.785 -6.294  67.287  1.000 53.740  ? 2   VAL HHH N   1 
ATOM 12563 C CA  . VAL H 3 2   ? 106.021 -5.186  68.255  1.000 55.820  ? 2   VAL HHH CA  1 
ATOM 12564 C C   . VAL H 3 2   ? 104.636 -4.642  68.592  1.000 57.970  ? 2   VAL HHH C   1 
ATOM 12565 O O   . VAL H 3 2   ? 103.882 -4.319  67.649  1.000 62.590  ? 2   VAL HHH O   1 
ATOM 12566 C CB  . VAL H 3 2   ? 106.918 -4.099  67.625  1.000 58.040  ? 2   VAL HHH CB  1 
ATOM 12567 C CG1 . VAL H 3 2   ? 106.716 -2.731  68.262  1.000 60.400  ? 2   VAL HHH CG1 1 
ATOM 12568 C CG2 . VAL H 3 2   ? 108.383 -4.490  67.676  1.000 55.840  ? 2   VAL HHH CG2 1 
ATOM 12569 N N   . GLN H 3 3   ? 104.290 -4.549  69.867  1.000 57.940  ? 3   GLN HHH N   1 
ATOM 12570 C CA  . GLN H 3 3   ? 102.976 -3.996  70.291  1.000 64.710  ? 3   GLN HHH CA  1 
ATOM 12571 C C   . GLN H 3 3   ? 103.220 -2.949  71.387  1.000 59.050  ? 3   GLN HHH C   1 
ATOM 12572 O O   . GLN H 3 3   ? 103.997 -3.217  72.319  1.000 61.140  ? 3   GLN HHH O   1 
ATOM 12573 C CB  . GLN H 3 3   ? 102.030 -5.149  70.674  1.000 69.860  ? 3   GLN HHH CB  1 
ATOM 12574 C CG  . GLN H 3 3   ? 101.347 -5.795  69.469  1.000 75.760  ? 3   GLN HHH CG  1 
ATOM 12575 C CD  . GLN H 3 3   ? 101.135 -7.280  69.643  1.000 83.690  ? 3   GLN HHH CD  1 
ATOM 12576 O OE1 . GLN H 3 3   ? 101.043 -7.757  70.770  1.000 83.860  ? 3   GLN HHH OE1 1 
ATOM 12577 N NE2 . GLN H 3 3   ? 101.081 -8.007  68.532  1.000 81.960  ? 3   GLN HHH NE2 1 
ATOM 12578 N N   . LEU H 3 4   ? 102.619 -1.773  71.215  1.000 50.950  ? 4   LEU HHH N   1 
ATOM 12579 C CA  . LEU H 3 4   ? 102.515 -0.700  72.225  1.000 42.750  ? 4   LEU HHH CA  1 
ATOM 12580 C C   . LEU H 3 4   ? 101.039 -0.577  72.608  1.000 44.080  ? 4   LEU HHH C   1 
ATOM 12581 O O   . LEU H 3 4   ? 100.187 -0.594  71.688  1.000 40.570  ? 4   LEU HHH O   1 
ATOM 12582 C CB  . LEU H 3 4   ? 103.028 0.605   71.612  1.000 39.540  ? 4   LEU HHH CB  1 
ATOM 12583 C CG  . LEU H 3 4   ? 104.455 0.589   71.080  1.000 36.760  ? 4   LEU HHH CG  1 
ATOM 12584 C CD1 . LEU H 3 4   ? 104.757 1.883   70.339  1.000 34.430  ? 4   LEU HHH CD1 1 
ATOM 12585 C CD2 . LEU H 3 4   ? 105.452 0.371   72.211  1.000 38.140  ? 4   LEU HHH CD2 1 
ATOM 12586 N N   . VAL H 3 5   ? 100.744 -0.467  73.908  1.000 46.800  ? 5   VAL HHH N   1 
ATOM 12587 C CA  . VAL H 3 5   ? 99.348  -0.340  74.424  1.000 45.740  ? 5   VAL HHH CA  1 
ATOM 12588 C C   . VAL H 3 5   ? 99.257  0.823   75.406  1.000 45.630  ? 5   VAL HHH C   1 
ATOM 12589 O O   . VAL H 3 5   ? 99.939  0.773   76.456  1.000 44.260  ? 5   VAL HHH O   1 
ATOM 12590 C CB  . VAL H 3 5   ? 98.837  -1.639  75.071  1.000 45.460  ? 5   VAL HHH CB  1 
ATOM 12591 C CG1 . VAL H 3 5   ? 97.317  -1.645  75.138  1.000 45.140  ? 5   VAL HHH CG1 1 
ATOM 12592 C CG2 . VAL H 3 5   ? 99.362  -2.864  74.324  1.000 47.280  ? 5   VAL HHH CG2 1 
ATOM 12593 N N   . GLU H 3 6   ? 98.448  1.821   75.055  1.000 46.960  ? 6   GLU HHH N   1 
ATOM 12594 C CA  . GLU H 3 6   ? 98.223  3.022   75.889  1.000 51.610  ? 6   GLU HHH CA  1 
ATOM 12595 C C   . GLU H 3 6   ? 97.037  2.762   76.812  1.000 50.450  ? 6   GLU HHH C   1 
ATOM 12596 O O   . GLU H 3 6   ? 96.234  1.860   76.503  1.000 49.210  ? 6   GLU HHH O   1 
ATOM 12597 C CB  . GLU H 3 6   ? 97.974  4.252   75.016  1.000 54.990  ? 6   GLU HHH CB  1 
ATOM 12598 C CG  . GLU H 3 6   ? 99.151  4.590   74.108  1.000 52.030  ? 6   GLU HHH CG  1 
ATOM 12599 C CD  . GLU H 3 6   ? 99.002  4.038   72.705  1.000 48.450  ? 6   GLU HHH CD  1 
ATOM 12600 O OE1 . GLU H 3 6   ? 98.246  3.057   72.535  1.000 48.380  ? 6   GLU HHH OE1 1 
ATOM 12601 O OE2 . GLU H 3 6   ? 99.615  4.605   71.781  1.000 46.520  ? 6   GLU HHH OE2 1 
ATOM 12602 N N   . SER H 3 7   ? 96.961  3.538   77.894  1.000 48.350  ? 7   SER HHH N   1 
ATOM 12603 C CA  . SER H 3 7   ? 95.963  3.415   78.983  1.000 45.700  ? 7   SER HHH CA  1 
ATOM 12604 C C   . SER H 3 7   ? 96.091  4.621   79.908  1.000 48.410  ? 7   SER HHH C   1 
ATOM 12605 O O   . SER H 3 7   ? 97.167  5.279   79.897  1.000 48.520  ? 7   SER HHH O   1 
ATOM 12606 C CB  . SER H 3 7   ? 96.161  2.144   79.729  1.000 43.570  ? 7   SER HHH CB  1 
ATOM 12607 O OG  . SER H 3 7   ? 97.481  2.091   80.227  1.000 39.540  ? 7   SER HHH OG  1 
ATOM 12608 N N   . GLY H 3 8   ? 95.029  4.882   80.672  1.000 53.700  ? 8   GLY HHH N   1 
ATOM 12609 C CA  . GLY H 3 8   ? 94.992  5.944   81.696  1.000 59.860  ? 8   GLY HHH CA  1 
ATOM 12610 C C   . GLY H 3 8   ? 94.190  7.148   81.238  1.000 54.030  ? 8   GLY HHH C   1 
ATOM 12611 O O   . GLY H 3 8   ? 93.861  7.996   82.101  1.000 57.670  ? 8   GLY HHH O   1 
ATOM 12612 N N   . GLY H 3 9   ? 93.886  7.226   79.943  1.000 46.380  ? 9   GLY HHH N   1 
ATOM 12613 C CA  . GLY H 3 9   ? 93.025  8.276   79.374  1.000 49.250  ? 9   GLY HHH CA  1 
ATOM 12614 C C   . GLY H 3 9   ? 91.615  8.224   79.942  1.000 48.540  ? 9   GLY HHH C   1 
ATOM 12615 O O   . GLY H 3 9   ? 91.146  7.133   80.265  1.000 57.410  ? 9   GLY HHH O   1 
ATOM 12616 N N   . GLY H 3 10  ? 90.960  9.369   80.075  1.000 49.980  ? 10  GLY HHH N   1 
ATOM 12617 C CA  . GLY H 3 10  ? 89.528  9.443   80.416  1.000 52.150  ? 10  GLY HHH CA  1 
ATOM 12618 C C   . GLY H 3 10  ? 88.983  10.859  80.396  1.000 55.640  ? 10  GLY HHH C   1 
ATOM 12619 O O   . GLY H 3 10  ? 89.552  11.720  79.668  1.000 48.780  ? 10  GLY HHH O   1 
ATOM 12620 N N   . LEU H 3 11  ? 87.890  11.076  81.136  1.000 60.710  ? 11  LEU HHH N   1 
ATOM 12621 C CA  . LEU H 3 11  ? 87.197  12.387  81.239  1.000 59.890  ? 11  LEU HHH CA  1 
ATOM 12622 C C   . LEU H 3 11  ? 87.686  13.089  82.499  1.000 58.170  ? 11  LEU HHH C   1 
ATOM 12623 O O   . LEU H 3 11  ? 87.661  12.448  83.577  1.000 49.880  ? 11  LEU HHH O   1 
ATOM 12624 C CB  . LEU H 3 11  ? 85.685  12.175  81.284  1.000 59.760  ? 11  LEU HHH CB  1 
ATOM 12625 C CG  . LEU H 3 11  ? 84.836  13.420  81.039  1.000 66.130  ? 11  LEU HHH CG  1 
ATOM 12626 C CD1 . LEU H 3 11  ? 84.968  13.944  79.617  1.000 69.250  ? 11  LEU HHH CD1 1 
ATOM 12627 C CD2 . LEU H 3 11  ? 83.383  13.110  81.343  1.000 73.390  ? 11  LEU HHH CD2 1 
ATOM 12628 N N   . VAL H 3 12  ? 88.151  14.332  82.353  1.000 54.060  ? 12  VAL HHH N   1 
ATOM 12629 C CA  . VAL H 3 12  ? 88.649  15.165  83.476  1.000 52.640  ? 12  VAL HHH CA  1 
ATOM 12630 C C   . VAL H 3 12  ? 88.287  16.618  83.146  1.000 55.140  ? 12  VAL HHH C   1 
ATOM 12631 O O   . VAL H 3 12  ? 88.141  16.943  81.954  1.000 48.510  ? 12  VAL HHH O   1 
ATOM 12632 C CB  . VAL H 3 12  ? 90.157  14.955  83.706  1.000 51.620  ? 12  VAL HHH CB  1 
ATOM 12633 C CG1 . VAL H 3 12  ? 90.959  15.244  82.465  1.000 55.440  ? 12  VAL HHH CG1 1 
ATOM 12634 C CG2 . VAL H 3 12  ? 90.693  15.762  84.865  1.000 53.740  ? 12  VAL HHH CG2 1 
ATOM 12635 N N   . LYS H 3 13  ? 88.103  17.436  84.188  1.000 55.260  ? 13  LYS HHH N   1 
ATOM 12636 C CA  . LYS H 3 13  ? 87.643  18.841  84.086  1.000 52.660  ? 13  LYS HHH CA  1 
ATOM 12637 C C   . LYS H 3 13  ? 88.880  19.705  83.889  1.000 45.890  ? 13  LYS HHH C   1 
ATOM 12638 O O   . LYS H 3 13  ? 89.963  19.351  84.353  1.000 49.060  ? 13  LYS HHH O   1 
ATOM 12639 C CB  . LYS H 3 13  ? 86.840  19.221  85.339  1.000 63.700  ? 13  LYS HHH CB  1 
ATOM 12640 C CG  . LYS H 3 13  ? 85.494  18.527  85.551  1.000 70.060  ? 13  LYS HHH CG  1 
ATOM 12641 C CD  . LYS H 3 13  ? 84.564  19.310  86.508  1.000 74.350  ? 13  LYS HHH CD  1 
ATOM 12642 C CE  . LYS H 3 13  ? 83.576  18.453  87.270  1.000 79.850  ? 13  LYS HHH CE  1 
ATOM 12643 N NZ  . LYS H 3 13  ? 82.559  17.870  86.363  1.000 84.150  ? 13  LYS HHH NZ  1 
ATOM 12644 N N   . PRO H 3 14  ? 88.768  20.844  83.171  1.000 42.100  ? 14  PRO HHH N   1 
ATOM 12645 C CA  . PRO H 3 14  ? 89.861  21.804  83.062  1.000 42.900  ? 14  PRO HHH CA  1 
ATOM 12646 C C   . PRO H 3 14  ? 90.564  21.993  84.406  1.000 45.640  ? 14  PRO HHH C   1 
ATOM 12647 O O   . PRO H 3 14  ? 89.919  21.842  85.420  1.000 44.740  ? 14  PRO HHH O   1 
ATOM 12648 C CB  . PRO H 3 14  ? 89.161  23.097  82.647  1.000 41.450  ? 14  PRO HHH CB  1 
ATOM 12649 C CG  . PRO H 3 14  ? 88.015  22.609  81.808  1.000 40.470  ? 14  PRO HHH CG  1 
ATOM 12650 C CD  . PRO H 3 14  ? 87.592  21.286  82.419  1.000 40.570  ? 14  PRO HHH CD  1 
ATOM 12651 N N   . GLY H 3 15  ? 91.861  22.297  84.359  1.000 51.650  ? 15  GLY HHH N   1 
ATOM 12652 C CA  . GLY H 3 15  ? 92.728  22.389  85.546  1.000 55.030  ? 15  GLY HHH CA  1 
ATOM 12653 C C   . GLY H 3 15  ? 93.004  21.020  86.127  1.000 57.570  ? 15  GLY HHH C   1 
ATOM 12654 O O   . GLY H 3 15  ? 93.833  20.954  87.048  1.000 64.340  ? 15  GLY HHH O   1 
ATOM 12655 N N   . GLY H 3 16  ? 92.396  19.965  85.580  1.000 59.140  ? 16  GLY HHH N   1 
ATOM 12656 C CA  . GLY H 3 16  ? 92.528  18.582  86.071  1.000 60.860  ? 16  GLY HHH CA  1 
ATOM 12657 C C   . GLY H 3 16  ? 93.903  17.979  85.775  1.000 62.420  ? 16  GLY HHH C   1 
ATOM 12658 O O   . GLY H 3 16  ? 94.762  18.695  85.197  1.000 65.750  ? 16  GLY HHH O   1 
ATOM 12659 N N   . SER H 3 17  ? 94.080  16.713  86.161  1.000 57.780  ? 17  SER HHH N   1 
ATOM 12660 C CA  . SER H 3 17  ? 95.366  15.965  86.037  1.000 52.880  ? 17  SER HHH CA  1 
ATOM 12661 C C   . SER H 3 17  ? 95.082  14.547  85.558  1.000 53.470  ? 17  SER HHH C   1 
ATOM 12662 O O   . SER H 3 17  ? 93.894  14.140  85.607  1.000 56.260  ? 17  SER HHH O   1 
ATOM 12663 C CB  . SER H 3 17  ? 96.125  15.962  87.319  1.000 49.160  ? 17  SER HHH CB  1 
ATOM 12664 O OG  . SER H 3 17  ? 96.781  17.195  87.480  1.000 57.270  ? 17  SER HHH OG  1 
ATOM 12665 N N   . LEU H 3 18  ? 96.116  13.849  85.076  1.000 54.560  ? 18  LEU HHH N   1 
ATOM 12666 C CA  . LEU H 3 18  ? 95.974  12.531  84.408  1.000 47.780  ? 18  LEU HHH CA  1 
ATOM 12667 C C   . LEU H 3 18  ? 97.354  11.972  84.064  1.000 43.830  ? 18  LEU HHH C   1 
ATOM 12668 O O   . LEU H 3 18  ? 98.192  12.747  83.552  1.000 39.890  ? 18  LEU HHH O   1 
ATOM 12669 C CB  . LEU H 3 18  ? 95.117  12.697  83.150  1.000 48.410  ? 18  LEU HHH CB  1 
ATOM 12670 C CG  . LEU H 3 18  ? 93.804  11.929  83.238  1.000 50.720  ? 18  LEU HHH CG  1 
ATOM 12671 C CD1 . LEU H 3 18  ? 93.047  12.002  81.921  1.000 51.960  ? 18  LEU HHH CD1 1 
ATOM 12672 C CD2 . LEU H 3 18  ? 94.049  10.483  83.679  1.000 50.680  ? 18  LEU HHH CD2 1 
ATOM 12673 N N   . ARG H 3 19  ? 97.581  10.687  84.358  1.000 41.660  ? 19  ARG HHH N   1 
ATOM 12674 C CA  . ARG H 3 19  ? 98.837  9.968   84.024  1.000 41.480  ? 19  ARG HHH CA  1 
ATOM 12675 C C   . ARG H 3 19  ? 98.517  8.889   82.989  1.000 38.610  ? 19  ARG HHH C   1 
ATOM 12676 O O   . ARG H 3 19  ? 97.649  8.028   83.256  1.000 34.240  ? 19  ARG HHH O   1 
ATOM 12677 C CB  . ARG H 3 19  ? 99.471  9.357   85.277  1.000 45.810  ? 19  ARG HHH CB  1 
ATOM 12678 C CG  . ARG H 3 19  ? 100.734 8.542   85.038  1.000 50.050  ? 19  ARG HHH CG  1 
ATOM 12679 C CD  . ARG H 3 19  ? 101.504 8.456   86.348  1.000 56.580  ? 19  ARG HHH CD  1 
ATOM 12680 N NE  . ARG H 3 19  ? 102.848 7.894   86.278  1.000 57.650  ? 19  ARG HHH NE  1 
ATOM 12681 C CZ  . ARG H 3 19  ? 103.186 6.654   86.648  1.000 59.660  ? 19  ARG HHH CZ  1 
ATOM 12682 N NH1 . ARG H 3 19  ? 102.274 5.799   87.071  1.000 58.980  ? 19  ARG HHH NH1 1 
ATOM 12683 N NH2 . ARG H 3 19  ? 104.438 6.249   86.554  1.000 63.810  ? 19  ARG HHH NH2 1 
ATOM 12684 N N   . LEU H 3 20  ? 99.193  8.960   81.843  1.000 39.090  ? 20  LEU HHH N   1 
ATOM 12685 C CA  . LEU H 3 20  ? 99.031  8.006   80.723  1.000 38.510  ? 20  LEU HHH CA  1 
ATOM 12686 C C   . LEU H 3 20  ? 100.155 6.973   80.825  1.000 39.160  ? 20  LEU HHH C   1 
ATOM 12687 O O   . LEU H 3 20  ? 101.249 7.333   81.347  1.000 34.200  ? 20  LEU HHH O   1 
ATOM 12688 C CB  . LEU H 3 20  ? 99.069  8.780   79.406  1.000 38.080  ? 20  LEU HHH CB  1 
ATOM 12689 C CG  . LEU H 3 20  ? 97.736  9.356   78.946  1.000 39.560  ? 20  LEU HHH CG  1 
ATOM 12690 C CD1 . LEU H 3 20  ? 96.972  9.989   80.086  1.000 42.260  ? 20  LEU HHH CD1 1 
ATOM 12691 C CD2 . LEU H 3 20  ? 97.937  10.358  77.812  1.000 41.250  ? 20  LEU HHH CD2 1 
ATOM 12692 N N   . SER H 3 21  ? 99.848  5.747   80.387  1.000 37.210  ? 21  SER HHH N   1 
ATOM 12693 C CA  . SER H 3 21  ? 100.767 4.586   80.397  1.000 37.200  ? 21  SER HHH CA  1 
ATOM 12694 C C   . SER H 3 21  ? 100.865 3.991   78.993  1.000 41.320  ? 21  SER HHH C   1 
ATOM 12695 O O   . SER H 3 21  ? 99.807  3.754   78.372  1.000 42.880  ? 21  SER HHH O   1 
ATOM 12696 C CB  . SER H 3 21  ? 100.289 3.568   81.354  1.000 35.800  ? 21  SER HHH CB  1 
ATOM 12697 O OG  . SER H 3 21  ? 100.743 3.883   82.649  1.000 38.410  ? 21  SER HHH OG  1 
ATOM 12698 N N   . CYS H 3 22  ? 102.096 3.750   78.526  1.000 41.970  ? 22  CYS HHH N   1 
ATOM 12699 C CA  . CYS H 3 22  ? 102.386 2.898   77.346  1.000 42.430  ? 22  CYS HHH CA  1 
ATOM 12700 C C   . CYS H 3 22  ? 103.057 1.616   77.827  1.000 41.470  ? 22  CYS HHH C   1 
ATOM 12701 O O   . CYS H 3 22  ? 104.063 1.719   78.548  1.000 38.850  ? 22  CYS HHH O   1 
ATOM 12702 C CB  . CYS H 3 22  ? 103.287 3.600   76.337  1.000 45.750  ? 22  CYS HHH CB  1 
ATOM 12703 S SG  . CYS H 3 22  ? 103.164 2.887   74.678  1.000 46.660  ? 22  CYS HHH SG  1 
ATOM 12704 N N   . ALA H 3 23  ? 102.491 0.471   77.457  1.000 45.420  ? 23  ALA HHH N   1 
ATOM 12705 C CA  . ALA H 3 23  ? 103.042 -0.868  77.748  1.000 47.240  ? 23  ALA HHH CA  1 
ATOM 12706 C C   . ALA H 3 23  ? 103.647 -1.423  76.461  1.000 48.870  ? 23  ALA HHH C   1 
ATOM 12707 O O   . ALA H 3 23  ? 102.882 -1.667  75.500  1.000 52.010  ? 23  ALA HHH O   1 
ATOM 12708 C CB  . ALA H 3 23  ? 101.962 -1.771  78.269  1.000 50.410  ? 23  ALA HHH CB  1 
ATOM 12709 N N   . ALA H 3 24  ? 104.970 -1.588  76.458  1.000 44.570  ? 24  ALA HHH N   1 
ATOM 12710 C CA  . ALA H 3 24  ? 105.772 -2.077  75.314  1.000 41.440  ? 24  ALA HHH CA  1 
ATOM 12711 C C   . ALA H 3 24  ? 106.112 -3.563  75.501  1.000 42.820  ? 24  ALA HHH C   1 
ATOM 12712 O O   . ALA H 3 24  ? 106.709 -3.939  76.529  1.000 43.330  ? 24  ALA HHH O   1 
ATOM 12713 C CB  . ALA H 3 24  ? 107.016 -1.241  75.181  1.000 39.630  ? 24  ALA HHH CB  1 
ATOM 12714 N N   . SER H 3 25  ? 105.717 -4.387  74.533  1.000 42.770  ? 25  SER HHH N   1 
ATOM 12715 C CA  . SER H 3 25  ? 106.133 -5.801  74.349  1.000 41.570  ? 25  SER HHH CA  1 
ATOM 12716 C C   . SER H 3 25  ? 106.614 -6.002  72.910  1.000 42.950  ? 25  SER HHH C   1 
ATOM 12717 O O   . SER H 3 25  ? 106.157 -5.265  72.009  1.000 50.200  ? 25  SER HHH O   1 
ATOM 12718 C CB  . SER H 3 25  ? 104.991 -6.730  74.660  1.000 41.550  ? 25  SER HHH CB  1 
ATOM 12719 O OG  . SER H 3 25  ? 103.916 -6.488  73.771  1.000 43.380  ? 25  SER HHH OG  1 
ATOM 12720 N N   . GLY H 3 26  ? 107.526 -6.945  72.689  1.000 41.310  ? 26  GLY HHH N   1 
ATOM 12721 C CA  . GLY H 3 26  ? 107.964 -7.252  71.315  1.000 41.350  ? 26  GLY HHH CA  1 
ATOM 12722 C C   . GLY H 3 26  ? 109.361 -6.769  71.009  1.000 38.810  ? 26  GLY HHH C   1 
ATOM 12723 O O   . GLY H 3 26  ? 109.911 -7.200  69.989  1.000 35.350  ? 26  GLY HHH O   1 
ATOM 12724 N N   . PHE H 3 27  ? 109.905 -5.904  71.862  1.000 36.850  ? 27  PHE HHH N   1 
ATOM 12725 C CA  . PHE H 3 27  ? 111.241 -5.319  71.613  1.000 36.890  ? 27  PHE HHH CA  1 
ATOM 12726 C C   . PHE H 3 27  ? 111.888 -4.942  72.936  1.000 38.910  ? 27  PHE HHH C   1 
ATOM 12727 O O   . PHE H 3 27  ? 111.178 -4.915  73.951  1.000 43.540  ? 27  PHE HHH O   1 
ATOM 12728 C CB  . PHE H 3 27  ? 111.135 -4.097  70.701  1.000 37.440  ? 27  PHE HHH CB  1 
ATOM 12729 C CG  . PHE H 3 27  ? 110.368 -2.912  71.225  1.000 36.850  ? 27  PHE HHH CG  1 
ATOM 12730 C CD1 . PHE H 3 27  ? 108.985 -2.916  71.264  1.000 37.770  ? 27  PHE HHH CD1 1 
ATOM 12731 C CD2 . PHE H 3 27  ? 111.031 -1.767  71.625  1.000 38.470  ? 27  PHE HHH CD2 1 
ATOM 12732 C CE1 . PHE H 3 27  ? 108.287 -1.815  71.725  1.000 37.950  ? 27  PHE HHH CE1 1 
ATOM 12733 C CE2 . PHE H 3 27  ? 110.333 -0.667  72.089  1.000 38.600  ? 27  PHE HHH CE2 1 
ATOM 12734 C CZ  . PHE H 3 27  ? 108.963 -0.692  72.134  1.000 38.140  ? 27  PHE HHH CZ  1 
ATOM 12735 N N   . THR H 3 28  ? 113.193 -4.680  72.917  1.000 38.010  ? 28  THR HHH N   1 
ATOM 12736 C CA  . THR H 3 28  ? 113.895 -4.216  74.133  1.000 39.310  ? 28  THR HHH CA  1 
ATOM 12737 C C   . THR H 3 28  ? 113.597 -2.731  74.282  1.000 42.640  ? 28  THR HHH C   1 
ATOM 12738 O O   . THR H 3 28  ? 114.326 -1.945  73.700  1.000 61.530  ? 28  THR HHH O   1 
ATOM 12739 C CB  . THR H 3 28  ? 115.398 -4.463  74.010  1.000 38.250  ? 28  THR HHH CB  1 
ATOM 12740 O OG1 . THR H 3 28  ? 115.575 -5.646  73.234  1.000 35.690  ? 28  THR HHH OG1 1 
ATOM 12741 C CG2 . THR H 3 28  ? 116.079 -4.610  75.346  1.000 37.880  ? 28  THR HHH CG2 1 
ATOM 12742 N N   . PHE H 3 29  ? 112.570 -2.371  75.054  1.000 37.130  ? 29  PHE HHH N   1 
ATOM 12743 C CA  . PHE H 3 29  ? 112.154 -0.959  75.220  1.000 34.790  ? 29  PHE HHH CA  1 
ATOM 12744 C C   . PHE H 3 29  ? 113.323 -0.120  75.706  1.000 33.750  ? 29  PHE HHH C   1 
ATOM 12745 O O   . PHE H 3 29  ? 113.444 1.026   75.271  1.000 32.850  ? 29  PHE HHH O   1 
ATOM 12746 C CB  . PHE H 3 29  ? 110.962 -0.962  76.175  1.000 32.920  ? 29  PHE HHH CB  1 
ATOM 12747 C CG  . PHE H 3 29  ? 110.485 0.357   76.718  1.000 33.560  ? 29  PHE HHH CG  1 
ATOM 12748 C CD1 . PHE H 3 29  ? 109.693 1.192   75.954  1.000 33.510  ? 29  PHE HHH CD1 1 
ATOM 12749 C CD2 . PHE H 3 29  ? 110.778 0.730   78.017  1.000 33.970  ? 29  PHE HHH CD2 1 
ATOM 12750 C CE1 . PHE H 3 29  ? 109.229 2.388   76.469  1.000 32.540  ? 29  PHE HHH CE1 1 
ATOM 12751 C CE2 . PHE H 3 29  ? 110.322 1.932   78.526  1.000 34.030  ? 29  PHE HHH CE2 1 
ATOM 12752 C CZ  . PHE H 3 29  ? 109.557 2.762   77.747  1.000 33.320  ? 29  PHE HHH CZ  1 
ATOM 12753 N N   . SER H 3 30  ? 114.195 -0.704  76.519  1.000 32.120  ? 30  SER HHH N   1 
ATOM 12754 C CA  . SER H 3 30  ? 115.346 0.021   77.104  1.000 33.920  ? 30  SER HHH CA  1 
ATOM 12755 C C   . SER H 3 30  ? 116.387 0.429   76.062  1.000 38.440  ? 30  SER HHH C   1 
ATOM 12756 O O   . SER H 3 30  ? 117.436 0.930   76.481  1.000 37.770  ? 30  SER HHH O   1 
ATOM 12757 C CB  . SER H 3 30  ? 116.000 -0.877  78.089  1.000 33.010  ? 30  SER HHH CB  1 
ATOM 12758 O OG  . SER H 3 30  ? 116.529 -2.021  77.442  1.000 35.290  ? 30  SER HHH OG  1 
ATOM 12759 N N   . SER H 3 31  ? 116.123 0.234   74.770  1.000 42.000  ? 31  SER HHH N   1 
ATOM 12760 C CA  . SER H 3 31  ? 117.160 0.485   73.730  1.000 37.050  ? 31  SER HHH CA  1 
ATOM 12761 C C   . SER H 3 31  ? 116.652 1.532   72.754  1.000 34.210  ? 31  SER HHH C   1 
ATOM 12762 O O   . SER H 3 31  ? 117.390 1.860   71.825  1.000 36.990  ? 31  SER HHH O   1 
ATOM 12763 C CB  . SER H 3 31  ? 117.514 -0.771  72.998  1.000 35.950  ? 31  SER HHH CB  1 
ATOM 12764 O OG  . SER H 3 31  ? 118.004 -1.762  73.885  1.000 34.760  ? 31  SER HHH OG  1 
ATOM 12765 N N   . TYR H 3 32  ? 115.466 2.081   72.993  1.000 32.550  ? 32  TYR HHH N   1 
ATOM 12766 C CA  . TYR H 3 32  ? 114.882 2.973   71.970  1.000 32.000  ? 32  TYR HHH CA  1 
ATOM 12767 C C   . TYR H 3 32  ? 114.258 4.253   72.521  1.000 30.340  ? 32  TYR HHH C   1 
ATOM 12768 O O   . TYR H 3 32  ? 113.558 4.164   73.530  1.000 29.410  ? 32  TYR HHH O   1 
ATOM 12769 C CB  . TYR H 3 32  ? 113.760 2.229   71.244  1.000 32.740  ? 32  TYR HHH CB  1 
ATOM 12770 C CG  . TYR H 3 32  ? 114.137 0.997   70.468  1.000 33.100  ? 32  TYR HHH CG  1 
ATOM 12771 C CD1 . TYR H 3 32  ? 114.161 -0.242  71.076  1.000 34.680  ? 32  TYR HHH CD1 1 
ATOM 12772 C CD2 . TYR H 3 32  ? 114.415 1.057   69.116  1.000 36.060  ? 32  TYR HHH CD2 1 
ATOM 12773 C CE1 . TYR H 3 32  ? 114.491 -1.388  70.380  1.000 34.570  ? 32  TYR HHH CE1 1 
ATOM 12774 C CE2 . TYR H 3 32  ? 114.732 -0.081  68.397  1.000 35.460  ? 32  TYR HHH CE2 1 
ATOM 12775 C CZ  . TYR H 3 32  ? 114.776 -1.305  69.034  1.000 35.280  ? 32  TYR HHH CZ  1 
ATOM 12776 O OH  . TYR H 3 32  ? 115.089 -2.440  68.355  1.000 39.250  ? 32  TYR HHH OH  1 
ATOM 12777 N N   . THR H 3 33  ? 114.536 5.400   71.903  1.000 29.170  ? 33  THR HHH N   1 
ATOM 12778 C CA  . THR H 3 33  ? 113.834 6.676   72.187  1.000 29.150  ? 33  THR HHH CA  1 
ATOM 12779 C C   . THR H 3 33  ? 112.332 6.452   71.961  1.000 28.320  ? 33  THR HHH C   1 
ATOM 12780 O O   . THR H 3 33  ? 111.993 5.748   70.995  1.000 27.710  ? 33  THR HHH O   1 
ATOM 12781 C CB  . THR H 3 33  ? 114.346 7.787   71.260  1.000 27.120  ? 33  THR HHH CB  1 
ATOM 12782 O OG1 . THR H 3 33  ? 115.580 8.273   71.779  1.000 26.390  ? 33  THR HHH OG1 1 
ATOM 12783 C CG2 . THR H 3 33  ? 113.390 8.946   71.134  1.000 26.780  ? 33  THR HHH CG2 1 
ATOM 12784 N N   . MET H 3 34  ? 111.477 7.023   72.806  1.000 29.170  ? 34  MET HHH N   1 
ATOM 12785 C CA  . MET H 3 34  ? 110.009 6.834   72.738  1.000 31.220  ? 34  MET HHH CA  1 
ATOM 12786 C C   . MET H 3 34  ? 109.323 8.204   72.724  1.000 31.350  ? 34  MET HHH C   1 
ATOM 12787 O O   . MET H 3 34  ? 109.889 9.151   73.291  1.000 33.790  ? 34  MET HHH O   1 
ATOM 12788 C CB  . MET H 3 34  ? 109.520 6.010   73.930  1.000 32.740  ? 34  MET HHH CB  1 
ATOM 12789 C CG  . MET H 3 34  ? 109.992 4.562   73.896  1.000 34.720  ? 34  MET HHH CG  1 
ATOM 12790 S SD  . MET H 3 34  ? 109.255 3.576   72.558  1.000 38.430  ? 34  MET HHH SD  1 
ATOM 12791 C CE  . MET H 3 34  ? 107.502 3.852   72.794  1.000 35.740  ? 34  MET HHH CE  1 
ATOM 12792 N N   . ASN H 3 35  ? 108.155 8.285   72.092  1.000 30.180  ? 35  ASN HHH N   1 
ATOM 12793 C CA  . ASN H 3 35  ? 107.445 9.549   71.800  1.000 31.520  ? 35  ASN HHH CA  1 
ATOM 12794 C C   . ASN H 3 35  ? 105.980 9.452   72.260  1.000 32.880  ? 35  ASN HHH C   1 
ATOM 12795 O O   . ASN H 3 35  ? 105.416 8.336   72.306  1.000 32.070  ? 35  ASN HHH O   1 
ATOM 12796 C CB  . ASN H 3 35  ? 107.546 9.888   70.313  1.000 33.910  ? 35  ASN HHH CB  1 
ATOM 12797 C CG  . ASN H 3 35  ? 108.917 10.399  69.919  1.000 36.530  ? 35  ASN HHH CG  1 
ATOM 12798 O OD1 . ASN H 3 35  ? 109.189 11.598  69.998  1.000 39.660  ? 35  ASN HHH OD1 1 
ATOM 12799 N ND2 . ASN H 3 35  ? 109.792 9.493   69.492  1.000 37.990  ? 35  ASN HHH ND2 1 
ATOM 12800 N N   . TRP H 3 36  ? 105.395 10.598  72.616  1.000 35.610  ? 36  TRP HHH N   1 
ATOM 12801 C CA  . TRP H 3 36  ? 103.932 10.816  72.713  1.000 36.680  ? 36  TRP HHH CA  1 
ATOM 12802 C C   . TRP H 3 36  ? 103.544 11.768  71.583  1.000 42.670  ? 36  TRP HHH C   1 
ATOM 12803 O O   . TRP H 3 36  ? 104.207 12.817  71.439  1.000 45.190  ? 36  TRP HHH O   1 
ATOM 12804 C CB  . TRP H 3 36  ? 103.525 11.390  74.076  1.000 36.340  ? 36  TRP HHH CB  1 
ATOM 12805 C CG  . TRP H 3 36  ? 103.648 10.427  75.216  1.000 35.340  ? 36  TRP HHH CG  1 
ATOM 12806 C CD1 . TRP H 3 36  ? 104.659 10.380  76.127  1.000 35.020  ? 36  TRP HHH CD1 1 
ATOM 12807 C CD2 . TRP H 3 36  ? 102.737 9.379   75.576  1.000 35.570  ? 36  TRP HHH CD2 1 
ATOM 12808 N NE1 . TRP H 3 36  ? 104.454 9.362   77.013  1.000 35.390  ? 36  TRP HHH NE1 1 
ATOM 12809 C CE2 . TRP H 3 36  ? 103.281 8.729   76.701  1.000 35.660  ? 36  TRP HHH CE2 1 
ATOM 12810 C CE3 . TRP H 3 36  ? 101.531 8.913   75.046  1.000 38.430  ? 36  TRP HHH CE3 1 
ATOM 12811 C CZ2 . TRP H 3 36  ? 102.657 7.642   77.308  1.000 35.710  ? 36  TRP HHH CZ2 1 
ATOM 12812 C CZ3 . TRP H 3 36  ? 100.908 7.843   75.648  1.000 37.840  ? 36  TRP HHH CZ3 1 
ATOM 12813 C CH2 . TRP H 3 36  ? 101.470 7.215   76.763  1.000 37.250  ? 36  TRP HHH CH2 1 
ATOM 12814 N N   . VAL H 3 37  ? 102.537 11.396  70.794  1.000 44.000  ? 37  VAL HHH N   1 
ATOM 12815 C CA  . VAL H 3 37  ? 101.950 12.257  69.727  1.000 43.060  ? 37  VAL HHH CA  1 
ATOM 12816 C C   . VAL H 3 37  ? 100.441 12.250  69.946  1.000 38.830  ? 37  VAL HHH C   1 
ATOM 12817 O O   . VAL H 3 37  ? 99.915  11.171  70.278  1.000 38.430  ? 37  VAL HHH O   1 
ATOM 12818 C CB  . VAL H 3 37  ? 102.312 11.725  68.331  1.000 48.050  ? 37  VAL HHH CB  1 
ATOM 12819 C CG1 . VAL H 3 37  ? 101.684 12.554  67.232  1.000 52.090  ? 37  VAL HHH CG1 1 
ATOM 12820 C CG2 . VAL H 3 37  ? 103.815 11.642  68.121  1.000 51.670  ? 37  VAL HHH CG2 1 
ATOM 12821 N N   . ARG H 3 38  ? 99.773  13.390  69.775  1.000 37.820  ? 38  ARG HHH N   1 
ATOM 12822 C CA  . ARG H 3 38  ? 98.310  13.460  70.013  1.000 39.700  ? 38  ARG HHH CA  1 
ATOM 12823 C C   . ARG H 3 38  ? 97.592  13.940  68.761  1.000 38.680  ? 38  ARG HHH C   1 
ATOM 12824 O O   . ARG H 3 38  ? 98.234  14.590  67.919  1.000 34.510  ? 38  ARG HHH O   1 
ATOM 12825 C CB  . ARG H 3 38  ? 97.975  14.385  71.180  1.000 42.120  ? 38  ARG HHH CB  1 
ATOM 12826 C CG  . ARG H 3 38  ? 98.240  15.852  70.895  1.000 42.580  ? 38  ARG HHH CG  1 
ATOM 12827 C CD  . ARG H 3 38  ? 97.843  16.689  72.083  1.000 46.810  ? 38  ARG HHH CD  1 
ATOM 12828 N NE  . ARG H 3 38  ? 98.383  18.029  71.949  1.000 48.350  ? 38  ARG HHH NE  1 
ATOM 12829 C CZ  . ARG H 3 38  ? 98.272  18.966  72.874  1.000 48.150  ? 38  ARG HHH CZ  1 
ATOM 12830 N NH1 . ARG H 3 38  ? 97.595  18.712  73.981  1.000 45.450  ? 38  ARG HHH NH1 1 
ATOM 12831 N NH2 . ARG H 3 38  ? 98.839  20.145  72.682  1.000 48.590  ? 38  ARG HHH NH2 1 
ATOM 12832 N N   . GLN H 3 39  ? 96.297  13.615  68.686  1.000 42.690  ? 39  GLN HHH N   1 
ATOM 12833 C CA  . GLN H 3 39  ? 95.416  13.897  67.527  1.000 43.350  ? 39  GLN HHH CA  1 
ATOM 12834 C C   . GLN H 3 39  ? 94.064  14.418  68.022  1.000 45.620  ? 39  GLN HHH C   1 
ATOM 12835 O O   . GLN H 3 39  ? 93.242  13.613  68.475  1.000 45.410  ? 39  GLN HHH O   1 
ATOM 12836 C CB  . GLN H 3 39  ? 95.253  12.646  66.673  1.000 43.920  ? 39  GLN HHH CB  1 
ATOM 12837 C CG  . GLN H 3 39  ? 94.672  12.956  65.299  1.000 46.030  ? 39  GLN HHH CG  1 
ATOM 12838 C CD  . GLN H 3 39  ? 94.623  11.749  64.399  1.000 42.220  ? 39  GLN HHH CD  1 
ATOM 12839 O OE1 . GLN H 3 39  ? 94.598  10.601  64.860  1.000 41.820  ? 39  GLN HHH OE1 1 
ATOM 12840 N NE2 . GLN H 3 39  ? 94.613  12.020  63.108  1.000 36.390  ? 39  GLN HHH NE2 1 
ATOM 12841 N N   . ALA H 3 40  ? 93.872  15.734  67.936  1.000 51.340  ? 40  ALA HHH N   1 
ATOM 12842 C CA  . ALA H 3 40  ? 92.643  16.429  68.370  1.000 55.870  ? 40  ALA HHH CA  1 
ATOM 12843 C C   . ALA H 3 40  ? 91.532  16.069  67.393  1.000 58.080  ? 40  ALA HHH C   1 
ATOM 12844 O O   . ALA H 3 40  ? 91.793  15.926  66.200  1.000 50.980  ? 40  ALA HHH O   1 
ATOM 12845 C CB  . ALA H 3 40  ? 92.888  17.913  68.450  1.000 58.690  ? 40  ALA HHH CB  1 
ATOM 12846 N N   . PRO H 3 41  ? 90.267  15.915  67.855  1.000 59.030  ? 41  PRO HHH N   1 
ATOM 12847 C CA  . PRO H 3 41  ? 89.208  15.370  67.018  1.000 60.850  ? 41  PRO HHH CA  1 
ATOM 12848 C C   . PRO H 3 41  ? 89.111  16.192  65.729  1.000 60.100  ? 41  PRO HHH C   1 
ATOM 12849 O O   . PRO H 3 41  ? 89.015  17.392  65.836  1.000 57.980  ? 41  PRO HHH O   1 
ATOM 12850 C CB  . PRO H 3 41  ? 87.945  15.477  67.895  1.000 61.790  ? 41  PRO HHH CB  1 
ATOM 12851 C CG  . PRO H 3 41  ? 88.469  15.528  69.303  1.000 57.890  ? 41  PRO HHH CG  1 
ATOM 12852 C CD  . PRO H 3 41  ? 89.757  16.305  69.174  1.000 60.180  ? 41  PRO HHH CD  1 
ATOM 12853 N N   . GLY H 3 42  ? 89.230  15.525  64.575  1.000 61.110  ? 42  GLY HHH N   1 
ATOM 12854 C CA  . GLY H 3 42  ? 89.032  16.115  63.240  1.000 61.340  ? 42  GLY HHH CA  1 
ATOM 12855 C C   . GLY H 3 42  ? 90.304  16.748  62.684  1.000 61.940  ? 42  GLY HHH C   1 
ATOM 12856 O O   . GLY H 3 42  ? 90.347  16.941  61.446  1.000 72.490  ? 42  GLY HHH O   1 
ATOM 12857 N N   . LYS H 3 43  ? 91.260  17.094  63.545  1.000 59.480  ? 43  LYS HHH N   1 
ATOM 12858 C CA  . LYS H 3 43  ? 92.541  17.766  63.167  1.000 58.460  ? 43  LYS HHH CA  1 
ATOM 12859 C C   . LYS H 3 43  ? 93.631  16.690  62.915  1.000 58.310  ? 43  LYS HHH C   1 
ATOM 12860 O O   . LYS H 3 43  ? 93.331  15.456  63.012  1.000 55.760  ? 43  LYS HHH O   1 
ATOM 12861 C CB  . LYS H 3 43  ? 92.876  18.833  64.219  1.000 49.210  ? 43  LYS HHH CB  1 
ATOM 12862 N N   . GLY H 3 44  ? 94.856  17.119  62.540  1.000 54.260  ? 44  GLY HHH N   1 
ATOM 12863 C CA  . GLY H 3 44  ? 95.974  16.225  62.174  1.000 51.310  ? 44  GLY HHH CA  1 
ATOM 12864 C C   . GLY H 3 44  ? 96.723  15.739  63.391  1.000 49.470  ? 44  GLY HHH C   1 
ATOM 12865 O O   . GLY H 3 44  ? 96.175  15.814  64.489  1.000 50.830  ? 44  GLY HHH O   1 
ATOM 12866 N N   . LEU H 3 45  ? 97.965  15.286  63.214  1.000 49.010  ? 45  LEU HHH N   1 
ATOM 12867 C CA  . LEU H 3 45  ? 98.828  14.790  64.330  1.000 43.470  ? 45  LEU HHH CA  1 
ATOM 12868 C C   . LEU H 3 45  ? 99.636  15.962  64.886  1.000 40.440  ? 45  LEU HHH C   1 
ATOM 12869 O O   . LEU H 3 45  ? 99.823  16.926  64.150  1.000 47.530  ? 45  LEU HHH O   1 
ATOM 12870 C CB  . LEU H 3 45  ? 99.765  13.703  63.802  1.000 42.890  ? 45  LEU HHH CB  1 
ATOM 12871 C CG  . LEU H 3 45  ? 99.087  12.419  63.340  1.000 42.110  ? 45  LEU HHH CG  1 
ATOM 12872 C CD1 . LEU H 3 45  ? 100.126 11.460  62.777  1.000 40.350  ? 45  LEU HHH CD1 1 
ATOM 12873 C CD2 . LEU H 3 45  ? 98.286  11.765  64.469  1.000 43.430  ? 45  LEU HHH CD2 1 
ATOM 12874 N N   . GLN H 3 46  ? 100.056 15.896  66.143  1.000 37.760  ? 46  GLN HHH N   1 
ATOM 12875 C CA  . GLN H 3 46  ? 100.893 16.932  66.809  1.000 36.850  ? 46  GLN HHH CA  1 
ATOM 12876 C C   . GLN H 3 46  ? 101.733 16.246  67.888  1.000 40.430  ? 46  GLN HHH C   1 
ATOM 12877 O O   . GLN H 3 46  ? 101.159 15.665  68.846  1.000 44.180  ? 46  GLN HHH O   1 
ATOM 12878 C CB  . GLN H 3 46  ? 100.051 18.049  67.421  1.000 34.810  ? 46  GLN HHH CB  1 
ATOM 12879 C CG  . GLN H 3 46  ? 100.863 19.094  68.180  1.000 34.340  ? 46  GLN HHH CG  1 
ATOM 12880 C CD  . GLN H 3 46  ? 100.025 19.979  69.085  1.000 35.250  ? 46  GLN HHH CD  1 
ATOM 12881 O OE1 . GLN H 3 46  ? 99.164  19.522  69.822  1.000 35.570  ? 46  GLN HHH OE1 1 
ATOM 12882 N NE2 . GLN H 3 46  ? 100.223 21.278  69.020  1.000 36.890  ? 46  GLN HHH NE2 1 
ATOM 12883 N N   . TRP H 3 47  ? 103.052 16.286  67.708  1.000 40.130  ? 47  TRP HHH N   1 
ATOM 12884 C CA  . TRP H 3 47  ? 104.027 15.666  68.634  1.000 39.670  ? 47  TRP HHH CA  1 
ATOM 12885 C C   . TRP H 3 47  ? 103.943 16.373  69.987  1.000 40.100  ? 47  TRP HHH C   1 
ATOM 12886 O O   . TRP H 3 47  ? 103.801 17.612  70.008  1.000 38.440  ? 47  TRP HHH O   1 
ATOM 12887 C CB  . TRP H 3 47  ? 105.429 15.757  68.041  1.000 40.710  ? 47  TRP HHH CB  1 
ATOM 12888 C CG  . TRP H 3 47  ? 106.506 15.362  69.003  1.000 41.300  ? 47  TRP HHH CG  1 
ATOM 12889 C CD1 . TRP H 3 47  ? 106.837 14.098  69.395  1.000 41.730  ? 47  TRP HHH CD1 1 
ATOM 12890 C CD2 . TRP H 3 47  ? 107.396 16.248  69.697  1.000 37.030  ? 47  TRP HHH CD2 1 
ATOM 12891 N NE1 . TRP H 3 47  ? 107.873 14.138  70.282  1.000 39.170  ? 47  TRP HHH NE1 1 
ATOM 12892 C CE2 . TRP H 3 47  ? 108.239 15.441  70.480  1.000 37.610  ? 47  TRP HHH CE2 1 
ATOM 12893 C CE3 . TRP H 3 47  ? 107.572 17.633  69.706  1.000 36.320  ? 47  TRP HHH CE3 1 
ATOM 12894 C CZ2 . TRP H 3 47  ? 109.249 15.977  71.270  1.000 40.940  ? 47  TRP HHH CZ2 1 
ATOM 12895 C CZ3 . TRP H 3 47  ? 108.566 18.166  70.492  1.000 38.400  ? 47  TRP HHH CZ3 1 
ATOM 12896 C CH2 . TRP H 3 47  ? 109.402 17.347  71.256  1.000 41.610  ? 47  TRP HHH CH2 1 
ATOM 12897 N N   . VAL H 3 48  ? 104.026 15.604  71.080  1.000 37.820  ? 48  VAL HHH N   1 
ATOM 12898 C CA  . VAL H 3 48  ? 103.925 16.160  72.462  1.000 37.950  ? 48  VAL HHH CA  1 
ATOM 12899 C C   . VAL H 3 48  ? 105.291 16.104  73.146  1.000 39.040  ? 48  VAL HHH C   1 
ATOM 12900 O O   . VAL H 3 48  ? 105.771 17.161  73.537  1.000 35.500  ? 48  VAL HHH O   1 
ATOM 12901 C CB  . VAL H 3 48  ? 102.870 15.385  73.272  1.000 37.900  ? 48  VAL HHH CB  1 
ATOM 12902 C CG1 . VAL H 3 48  ? 102.900 15.710  74.754  1.000 38.700  ? 48  VAL HHH CG1 1 
ATOM 12903 C CG2 . VAL H 3 48  ? 101.473 15.590  72.722  1.000 37.450  ? 48  VAL HHH CG2 1 
ATOM 12904 N N   . SER H 3 49  ? 105.895 14.919  73.261  1.000 42.020  ? 49  SER HHH N   1 
ATOM 12905 C CA  . SER H 3 49  ? 107.176 14.782  74.003  1.000 38.910  ? 49  SER HHH CA  1 
ATOM 12906 C C   . SER H 3 49  ? 108.050 13.616  73.540  1.000 34.950  ? 49  SER HHH C   1 
ATOM 12907 O O   . SER H 3 49  ? 107.488 12.657  73.027  1.000 31.390  ? 49  SER HHH O   1 
ATOM 12908 C CB  . SER H 3 49  ? 106.918 14.680  75.458  1.000 40.210  ? 49  SER HHH CB  1 
ATOM 12909 O OG  . SER H 3 49  ? 108.144 14.671  76.159  1.000 40.450  ? 49  SER HHH OG  1 
ATOM 12910 N N   . SER H 3 50  ? 109.374 13.705  73.740  1.000 33.560  ? 50  SER HHH N   1 
ATOM 12911 C CA  . SER H 3 50  ? 110.338 12.623  73.393  1.000 33.680  ? 50  SER HHH CA  1 
ATOM 12912 C C   . SER H 3 50  ? 111.180 12.274  74.609  1.000 31.680  ? 50  SER HHH C   1 
ATOM 12913 O O   . SER H 3 50  ? 111.442 13.179  75.387  1.000 29.670  ? 50  SER HHH O   1 
ATOM 12914 C CB  . SER H 3 50  ? 111.245 13.055  72.297  1.000 33.080  ? 50  SER HHH CB  1 
ATOM 12915 O OG  . SER H 3 50  ? 112.182 12.039  71.994  1.000 35.920  ? 50  SER HHH OG  1 
ATOM 12916 N N   . ILE H 3 51  ? 111.558 11.007  74.773  1.000 29.070  ? 51  ILE HHH N   1 
ATOM 12917 C CA  . ILE H 3 51  ? 112.427 10.578  75.905  1.000 28.700  ? 51  ILE HHH CA  1 
ATOM 12918 C C   . ILE H 3 51  ? 113.487 9.631   75.365  1.000 28.680  ? 51  ILE HHH C   1 
ATOM 12919 O O   . ILE H 3 51  ? 113.165 8.808   74.525  1.000 28.690  ? 51  ILE HHH O   1 
ATOM 12920 C CB  . ILE H 3 51  ? 111.669 9.974   77.104  1.000 30.230  ? 51  ILE HHH CB  1 
ATOM 12921 C CG1 . ILE H 3 51  ? 112.585 9.795   78.314  1.000 29.700  ? 51  ILE HHH CG1 1 
ATOM 12922 C CG2 . ILE H 3 51  ? 110.980 8.673   76.742  1.000 30.810  ? 51  ILE HHH CG2 1 
ATOM 12923 C CD1 . ILE H 3 51  ? 111.861 9.702   79.619  1.000 29.650  ? 51  ILE HHH CD1 1 
ATOM 12924 N N   . SER H 3 52  ? 114.715 9.771   75.841  1.000 30.630  ? 52  SER HHH N   1 
ATOM 12925 C CA  . SER H 3 52  ? 115.829 8.943   75.343  1.000 31.960  ? 52  SER HHH CA  1 
ATOM 12926 C C   . SER H 3 52  ? 115.745 7.560   75.959  1.000 30.620  ? 52  SER HHH C   1 
ATOM 12927 O O   . SER H 3 52  ? 115.011 7.397   76.922  1.000 24.210  ? 52  SER HHH O   1 
ATOM 12928 C CB  . SER H 3 52  ? 117.135 9.591   75.650  1.000 33.510  ? 52  SER HHH CB  1 
ATOM 12929 O OG  . SER H 3 52  ? 117.681 9.100   76.859  1.000 31.760  ? 52  SER HHH OG  1 
ATOM 12930 N N   . SER H 3 53  ? 116.482 6.612   75.393  1.000 34.100  ? 53  SER HHH N   1 
ATOM 12931 C CA  . SER H 3 53  ? 116.517 5.244   75.975  1.000 34.800  ? 53  SER HHH CA  1 
ATOM 12932 C C   . SER H 3 53  ? 116.776 5.313   77.489  1.000 33.750  ? 53  SER HHH C   1 
ATOM 12933 O O   . SER H 3 53  ? 116.100 4.590   78.232  1.000 32.760  ? 53  SER HHH O   1 
ATOM 12934 C CB  . SER H 3 53  ? 117.519 4.366   75.255  1.000 34.330  ? 53  SER HHH CB  1 
ATOM 12935 O OG  . SER H 3 53  ? 118.852 4.659   75.650  1.000 35.290  ? 53  SER HHH OG  1 
ATOM 12936 N N   . SER H 3 54  ? 117.704 6.154   77.937  1.000 35.680  ? 54  SER HHH N   1 
ATOM 12937 C CA  . SER H 3 54  ? 118.179 6.173   79.353  1.000 39.510  ? 54  SER HHH CA  1 
ATOM 12938 C C   . SER H 3 54  ? 117.617 7.400   80.082  1.000 38.260  ? 54  SER HHH C   1 
ATOM 12939 O O   . SER H 3 54  ? 118.082 7.712   81.195  1.000 42.550  ? 54  SER HHH O   1 
ATOM 12940 C CB  . SER H 3 54  ? 119.673 6.151   79.407  1.000 39.630  ? 54  SER HHH CB  1 
ATOM 12941 O OG  . SER H 3 54  ? 120.156 7.154   78.536  1.000 48.040  ? 54  SER HHH OG  1 
ATOM 12942 N N   . SER H 3 55  ? 116.676 8.095   79.461  1.000 33.370  ? 55  SER HHH N   1 
ATOM 12943 C CA  . SER H 3 55  ? 116.005 9.272   80.059  1.000 28.570  ? 55  SER HHH CA  1 
ATOM 12944 C C   . SER H 3 55  ? 117.079 10.363  80.212  1.000 26.780  ? 55  SER HHH C   1 
ATOM 12945 O O   . SER H 3 55  ? 116.883 11.263  81.024  1.000 25.150  ? 55  SER HHH O   1 
ATOM 12946 C CB  . SER H 3 55  ? 115.287 8.854   81.323  1.000 26.240  ? 55  SER HHH CB  1 
ATOM 12947 O OG  . SER H 3 55  ? 114.823 7.503   81.237  1.000 22.180  ? 55  SER HHH OG  1 
ATOM 12948 N N   . THR H 3 56  ? 118.044 10.358  79.299  1.000 28.430  ? 56  THR HHH N   1 
ATOM 12949 C CA  . THR H 3 56  ? 119.093 11.401  79.289  1.000 28.390  ? 56  THR HHH CA  1 
ATOM 12950 C C   . THR H 3 56  ? 118.563 12.678  78.616  1.000 30.150  ? 56  THR HHH C   1 
ATOM 12951 O O   . THR H 3 56  ? 118.937 13.772  79.050  1.000 36.840  ? 56  THR HHH O   1 
ATOM 12952 C CB  . THR H 3 56  ? 120.368 10.826  78.676  1.000 25.490  ? 56  THR HHH CB  1 
ATOM 12953 O OG1 . THR H 3 56  ? 120.751 9.718   79.486  1.000 24.720  ? 56  THR HHH OG1 1 
ATOM 12954 N N   . TYR H 3 57  ? 117.710 12.529  77.600  1.000 28.890  ? 57  TYR HHH N   1 
ATOM 12955 C CA  . TYR H 3 57  ? 117.153 13.700  76.878  1.000 28.620  ? 57  TYR HHH CA  1 
ATOM 12956 C C   . TYR H 3 57  ? 115.637 13.596  76.746  1.000 29.810  ? 57  TYR HHH C   1 
ATOM 12957 O O   . TYR H 3 57  ? 115.109 12.737  75.971  1.000 34.040  ? 57  TYR HHH O   1 
ATOM 12958 C CB  . TYR H 3 57  ? 117.824 13.767  75.502  1.000 29.850  ? 57  TYR HHH CB  1 
ATOM 12959 C CG  . TYR H 3 57  ? 119.315 13.950  75.526  1.000 30.840  ? 57  TYR HHH CG  1 
ATOM 12960 C CD1 . TYR H 3 57  ? 120.162 12.894  75.811  1.000 34.440  ? 57  TYR HHH CD1 1 
ATOM 12961 C CD2 . TYR H 3 57  ? 119.875 15.183  75.249  1.000 31.400  ? 57  TYR HHH CD2 1 
ATOM 12962 C CE1 . TYR H 3 57  ? 121.535 13.070  75.832  1.000 39.820  ? 57  TYR HHH CE1 1 
ATOM 12963 C CE2 . TYR H 3 57  ? 121.246 15.380  75.245  1.000 33.700  ? 57  TYR HHH CE2 1 
ATOM 12964 C CZ  . TYR H 3 57  ? 122.080 14.317  75.539  1.000 40.020  ? 57  TYR HHH CZ  1 
ATOM 12965 O OH  . TYR H 3 57  ? 123.437 14.493  75.542  1.000 44.350  ? 57  TYR HHH OH  1 
ATOM 12966 N N   . MET H 3 58  ? 114.942 14.479  77.462  1.000 29.230  ? 58  MET HHH N   1 
ATOM 12967 C CA  . MET H 3 58  ? 113.486 14.694  77.281  1.000 30.480  ? 58  MET HHH CA  1 
ATOM 12968 C C   . MET H 3 58  ? 113.296 15.992  76.488  1.000 32.730  ? 58  MET HHH C   1 
ATOM 12969 O O   . MET H 3 58  ? 114.046 16.930  76.727  1.000 38.730  ? 58  MET HHH O   1 
ATOM 12970 C CB  . MET H 3 58  ? 112.790 14.773  78.639  1.000 30.370  ? 58  MET HHH CB  1 
ATOM 12971 C CG  . MET H 3 58  ? 112.680 13.430  79.360  1.000 31.070  ? 58  MET HHH CG  1 
ATOM 12972 S SD  . MET H 3 58  ? 114.271 12.757  79.981  1.000 32.130  ? 58  MET HHH SD  1 
ATOM 12973 C CE  . MET H 3 58  ? 114.748 13.976  81.195  1.000 34.940  ? 58  MET HHH CE  1 
ATOM 12974 N N   . TYR H 3 59  ? 112.386 16.005  75.523  1.000 33.210  ? 59  TYR HHH N   1 
ATOM 12975 C CA  . TYR H 3 59  ? 112.004 17.190  74.714  1.000 35.090  ? 59  TYR HHH CA  1 
ATOM 12976 C C   . TYR H 3 59  ? 110.481 17.302  74.729  1.000 36.800  ? 59  TYR HHH C   1 
ATOM 12977 O O   . TYR H 3 59  ? 109.792 16.247  74.759  1.000 45.680  ? 59  TYR HHH O   1 
ATOM 12978 C CB  . TYR H 3 59  ? 112.463 17.045  73.262  1.000 38.080  ? 59  TYR HHH CB  1 
ATOM 12979 C CG  . TYR H 3 59  ? 113.948 16.926  73.076  1.000 40.140  ? 59  TYR HHH CG  1 
ATOM 12980 C CD1 . TYR H 3 59  ? 114.754 18.046  73.137  1.000 42.460  ? 59  TYR HHH CD1 1 
ATOM 12981 C CD2 . TYR H 3 59  ? 114.542 15.708  72.822  1.000 41.030  ? 59  TYR HHH CD2 1 
ATOM 12982 C CE1 . TYR H 3 59  ? 116.121 17.968  72.949  1.000 41.970  ? 59  TYR HHH CE1 1 
ATOM 12983 C CE2 . TYR H 3 59  ? 115.907 15.610  72.606  1.000 44.040  ? 59  TYR HHH CE2 1 
ATOM 12984 C CZ  . TYR H 3 59  ? 116.699 16.743  72.695  1.000 43.950  ? 59  TYR HHH CZ  1 
ATOM 12985 O OH  . TYR H 3 59  ? 118.047 16.686  72.536  1.000 47.910  ? 59  TYR HHH OH  1 
ATOM 12986 N N   . TYR H 3 60  ? 109.963 18.522  74.690  1.000 30.390  ? 60  TYR HHH N   1 
ATOM 12987 C CA  . TYR H 3 60  ? 108.506 18.758  74.696  1.000 27.740  ? 60  TYR HHH CA  1 
ATOM 12988 C C   . TYR H 3 60  ? 108.182 19.756  73.596  1.000 28.900  ? 60  TYR HHH C   1 
ATOM 12989 O O   . TYR H 3 60  ? 108.966 20.678  73.367  1.000 25.480  ? 60  TYR HHH O   1 
ATOM 12990 C CB  . TYR H 3 60  ? 108.029 19.255  76.066  1.000 26.210  ? 60  TYR HHH CB  1 
ATOM 12991 C CG  . TYR H 3 60  ? 108.413 18.371  77.221  1.000 24.020  ? 60  TYR HHH CG  1 
ATOM 12992 C CD1 . TYR H 3 60  ? 109.660 18.463  77.794  1.000 23.720  ? 60  TYR HHH CD1 1 
ATOM 12993 C CD2 . TYR H 3 60  ? 107.530 17.451  77.753  1.000 24.460  ? 60  TYR HHH CD2 1 
ATOM 12994 C CE1 . TYR H 3 60  ? 110.030 17.669  78.860  1.000 24.380  ? 60  TYR HHH CE1 1 
ATOM 12995 C CE2 . TYR H 3 60  ? 107.870 16.649  78.831  1.000 24.500  ? 60  TYR HHH CE2 1 
ATOM 12996 C CZ  . TYR H 3 60  ? 109.130 16.767  79.387  1.000 25.300  ? 60  TYR HHH CZ  1 
ATOM 12997 O OH  . TYR H 3 60  ? 109.547 15.992  80.434  1.000 29.730  ? 60  TYR HHH OH  1 
ATOM 12998 N N   . GLY H 3 61  ? 107.036 19.546  72.952  1.000 34.800  ? 61  GLY HHH N   1 
ATOM 12999 C CA  . GLY H 3 61  ? 106.344 20.571  72.151  1.000 38.940  ? 61  GLY HHH CA  1 
ATOM 13000 C C   . GLY H 3 61  ? 106.043 21.783  73.015  1.000 38.450  ? 61  GLY HHH C   1 
ATOM 13001 O O   . GLY H 3 61  ? 105.868 21.614  74.236  1.000 39.540  ? 61  GLY HHH O   1 
ATOM 13002 N N   . ASP H 3 62  ? 106.065 22.976  72.432  1.000 38.070  ? 62  ASP HHH N   1 
ATOM 13003 C CA  . ASP H 3 62  ? 105.912 24.217  73.231  1.000 36.370  ? 62  ASP HHH CA  1 
ATOM 13004 C C   . ASP H 3 62  ? 104.471 24.255  73.720  1.000 35.480  ? 62  ASP HHH C   1 
ATOM 13005 O O   . ASP H 3 62  ? 104.184 25.003  74.658  1.000 33.090  ? 62  ASP HHH O   1 
ATOM 13006 C CB  . ASP H 3 62  ? 106.263 25.436  72.380  1.000 35.880  ? 62  ASP HHH CB  1 
ATOM 13007 C CG  . ASP H 3 62  ? 107.749 25.659  72.189  1.000 38.350  ? 62  ASP HHH CG  1 
ATOM 13008 O OD1 . ASP H 3 62  ? 108.530 24.811  72.646  1.000 43.930  ? 62  ASP HHH OD1 1 
ATOM 13009 O OD2 . ASP H 3 62  ? 108.107 26.680  71.581  1.000 37.120  ? 62  ASP HHH OD2 1 
ATOM 13010 N N   . SER H 3 63  ? 103.599 23.466  73.112  1.000 37.400  ? 63  SER HHH N   1 
ATOM 13011 C CA  . SER H 3 63  ? 102.159 23.521  73.449  1.000 36.750  ? 63  SER HHH CA  1 
ATOM 13012 C C   . SER H 3 63  ? 101.910 22.972  74.852  1.000 36.380  ? 63  SER HHH C   1 
ATOM 13013 O O   . SER H 3 63  ? 100.910 23.344  75.474  1.000 47.700  ? 63  SER HHH O   1 
ATOM 13014 C CB  . SER H 3 63  ? 101.405 22.788  72.401  1.000 40.050  ? 63  SER HHH CB  1 
ATOM 13015 O OG  . SER H 3 63  ? 101.539 23.436  71.147  1.000 42.600  ? 63  SER HHH OG  1 
ATOM 13016 N N   . VAL H 3 64  ? 102.818 22.126  75.324  1.000 34.250  ? 64  VAL HHH N   1 
ATOM 13017 C CA  . VAL H 3 64  ? 102.652 21.466  76.646  1.000 36.270  ? 64  VAL HHH CA  1 
ATOM 13018 C C   . VAL H 3 64  ? 103.824 21.804  77.565  1.000 36.920  ? 64  VAL HHH C   1 
ATOM 13019 O O   . VAL H 3 64  ? 103.881 21.230  78.655  1.000 36.320  ? 64  VAL HHH O   1 
ATOM 13020 C CB  . VAL H 3 64  ? 102.580 19.960  76.359  1.000 38.570  ? 64  VAL HHH CB  1 
ATOM 13021 C CG1 . VAL H 3 64  ? 101.484 19.631  75.361  1.000 39.870  ? 64  VAL HHH CG1 1 
ATOM 13022 C CG2 . VAL H 3 64  ? 103.910 19.403  75.880  1.000 38.280  ? 64  VAL HHH CG2 1 
ATOM 13023 N N   . LYS H 3 65  ? 104.695 22.732  77.150  1.000 37.090  ? 65  LYS HHH N   1 
ATOM 13024 C CA  . LYS H 3 65  ? 105.893 23.095  77.957  1.000 36.590  ? 65  LYS HHH CA  1 
ATOM 13025 C C   . LYS H 3 65  ? 105.421 23.470  79.354  1.000 34.700  ? 65  LYS HHH C   1 
ATOM 13026 O O   . LYS H 3 65  ? 104.481 24.257  79.466  1.000 34.010  ? 65  LYS HHH O   1 
ATOM 13027 C CB  . LYS H 3 65  ? 106.693 24.248  77.350  1.000 38.230  ? 65  LYS HHH CB  1 
ATOM 13028 C CG  . LYS H 3 65  ? 107.895 23.815  76.526  1.000 45.730  ? 65  LYS HHH CG  1 
ATOM 13029 C CD  . LYS H 3 65  ? 108.704 24.965  75.999  1.000 48.990  ? 65  LYS HHH CD  1 
ATOM 13030 C CE  . LYS H 3 65  ? 109.404 25.718  77.112  1.000 50.930  ? 65  LYS HHH CE  1 
ATOM 13031 N NZ  . LYS H 3 65  ? 110.341 26.728  76.564  1.000 54.230  ? 65  LYS HHH NZ  1 
ATOM 13032 N N   . GLY H 3 66  ? 106.008 22.872  80.382  1.000 34.300  ? 66  GLY HHH N   1 
ATOM 13033 C CA  . GLY H 3 66  ? 105.758 23.301  81.766  1.000 36.530  ? 66  GLY HHH CA  1 
ATOM 13034 C C   . GLY H 3 66  ? 104.575 22.602  82.405  1.000 38.480  ? 66  GLY HHH C   1 
ATOM 13035 O O   . GLY H 3 66  ? 104.455 22.745  83.618  1.000 38.180  ? 66  GLY HHH O   1 
ATOM 13036 N N   . ARG H 3 67  ? 103.732 21.889  81.651  1.000 42.330  ? 67  ARG HHH N   1 
ATOM 13037 C CA  . ARG H 3 67  ? 102.499 21.247  82.198  1.000 44.980  ? 67  ARG HHH CA  1 
ATOM 13038 C C   . ARG H 3 67  ? 102.648 19.721  82.180  1.000 41.180  ? 67  ARG HHH C   1 
ATOM 13039 O O   . ARG H 3 67  ? 102.267 19.061  83.178  1.000 38.920  ? 67  ARG HHH O   1 
ATOM 13040 C CB  . ARG H 3 67  ? 101.256 21.701  81.411  1.000 51.740  ? 67  ARG HHH CB  1 
ATOM 13041 C CG  . ARG H 3 67  ? 101.089 23.213  81.349  1.000 51.950  ? 67  ARG HHH CG  1 
ATOM 13042 C CD  . ARG H 3 67  ? 99.762  23.661  80.788  1.000 51.260  ? 67  ARG HHH CD  1 
ATOM 13043 N NE  . ARG H 3 67  ? 99.636  23.374  79.360  1.000 50.100  ? 67  ARG HHH NE  1 
ATOM 13044 C CZ  . ARG H 3 67  ? 98.783  22.490  78.850  1.000 50.910  ? 67  ARG HHH CZ  1 
ATOM 13045 N NH1 . ARG H 3 67  ? 97.963  21.806  79.643  1.000 53.690  ? 67  ARG HHH NH1 1 
ATOM 13046 N NH2 . ARG H 3 67  ? 98.742  22.299  77.543  1.000 49.720  ? 67  ARG HHH NH2 1 
ATOM 13047 N N   . PHE H 3 68  ? 103.146 19.175  81.075  1.000 39.420  ? 68  PHE HHH N   1 
ATOM 13048 C CA  . PHE H 3 68  ? 103.308 17.716  80.858  1.000 39.040  ? 68  PHE HHH CA  1 
ATOM 13049 C C   . PHE H 3 68  ? 104.729 17.288  81.217  1.000 36.970  ? 68  PHE HHH C   1 
ATOM 13050 O O   . PHE H 3 68  ? 105.654 18.096  81.094  1.000 38.980  ? 68  PHE HHH O   1 
ATOM 13051 C CB  . PHE H 3 68  ? 103.009 17.378  79.401  1.000 40.840  ? 68  PHE HHH CB  1 
ATOM 13052 C CG  . PHE H 3 68  ? 101.567 17.518  79.002  1.000 42.570  ? 68  PHE HHH CG  1 
ATOM 13053 C CD1 . PHE H 3 68  ? 100.665 18.210  79.797  1.000 42.160  ? 68  PHE HHH CD1 1 
ATOM 13054 C CD2 . PHE H 3 68  ? 101.124 16.950  77.818  1.000 41.830  ? 68  PHE HHH CD2 1 
ATOM 13055 C CE1 . PHE H 3 68  ? 99.342  18.323  79.415  1.000 42.650  ? 68  PHE HHH CE1 1 
ATOM 13056 C CE2 . PHE H 3 68  ? 99.803  17.065  77.440  1.000 43.310  ? 68  PHE HHH CE2 1 
ATOM 13057 C CZ  . PHE H 3 68  ? 98.917  17.750  78.238  1.000 45.050  ? 68  PHE HHH CZ  1 
ATOM 13058 N N   . THR H 3 69  ? 104.895 16.043  81.655  1.000 35.170  ? 69  THR HHH N   1 
ATOM 13059 C CA  . THR H 3 69  ? 106.223 15.456  81.951  1.000 34.850  ? 69  THR HHH CA  1 
ATOM 13060 C C   . THR H 3 69  ? 106.257 14.015  81.447  1.000 34.090  ? 69  THR HHH C   1 
ATOM 13061 O O   . THR H 3 69  ? 105.400 13.215  81.880  1.000 36.700  ? 69  THR HHH O   1 
ATOM 13062 C CB  . THR H 3 69  ? 106.538 15.559  83.446  1.000 33.130  ? 69  THR HHH CB  1 
ATOM 13063 O OG1 . THR H 3 69  ? 106.180 16.889  83.803  1.000 31.540  ? 69  THR HHH OG1 1 
ATOM 13064 C CG2 . THR H 3 69  ? 107.987 15.289  83.773  1.000 32.190  ? 69  THR HHH CG2 1 
ATOM 13065 N N   . ILE H 3 70  ? 107.207 13.716  80.570  1.000 33.460  ? 70  ILE HHH N   1 
ATOM 13066 C CA  . ILE H 3 70  ? 107.441 12.348  80.032  1.000 36.810  ? 70  ILE HHH CA  1 
ATOM 13067 C C   . ILE H 3 70  ? 108.358 11.615  81.013  1.000 33.250  ? 70  ILE HHH C   1 
ATOM 13068 O O   . ILE H 3 70  ? 109.203 12.278  81.645  1.000 31.350  ? 70  ILE HHH O   1 
ATOM 13069 C CB  . ILE H 3 70  ? 108.033 12.406  78.603  1.000 39.010  ? 70  ILE HHH CB  1 
ATOM 13070 C CG1 . ILE H 3 70  ? 107.839 11.091  77.837  1.000 36.430  ? 70  ILE HHH CG1 1 
ATOM 13071 C CG2 . ILE H 3 70  ? 109.497 12.813  78.636  1.000 39.090  ? 70  ILE HHH CG2 1 
ATOM 13072 C CD1 . ILE H 3 70  ? 108.124 11.211  76.358  1.000 33.720  ? 70  ILE HHH CD1 1 
ATOM 13073 N N   . SER H 3 71  ? 108.182 10.308  81.148  1.000 30.880  ? 71  SER HHH N   1 
ATOM 13074 C CA  . SER H 3 71  ? 109.078 9.452   81.956  1.000 30.450  ? 71  SER HHH CA  1 
ATOM 13075 C C   . SER H 3 71  ? 108.957 8.011   81.480  1.000 30.460  ? 71  SER HHH C   1 
ATOM 13076 O O   . SER H 3 71  ? 107.940 7.661   80.848  1.000 32.870  ? 71  SER HHH O   1 
ATOM 13077 C CB  . SER H 3 71  ? 108.761 9.573   83.421  1.000 32.070  ? 71  SER HHH CB  1 
ATOM 13078 O OG  . SER H 3 71  ? 107.513 8.966   83.753  1.000 32.570  ? 71  SER HHH OG  1 
ATOM 13079 N N   . ARG H 3 72  ? 109.956 7.197   81.783  1.000 30.790  ? 72  ARG HHH N   1 
ATOM 13080 C CA  . ARG H 3 72  ? 109.934 5.758   81.435  1.000 33.250  ? 72  ARG HHH CA  1 
ATOM 13081 C C   . ARG H 3 72  ? 110.441 4.957   82.634  1.000 33.380  ? 72  ARG HHH C   1 
ATOM 13082 O O   . ARG H 3 72  ? 111.204 5.507   83.440  1.000 33.070  ? 72  ARG HHH O   1 
ATOM 13083 C CB  . ARG H 3 72  ? 110.766 5.517   80.172  1.000 36.400  ? 72  ARG HHH CB  1 
ATOM 13084 C CG  . ARG H 3 72  ? 112.228 5.925   80.320  1.000 39.180  ? 72  ARG HHH CG  1 
ATOM 13085 C CD  . ARG H 3 72  ? 112.996 5.896   79.006  1.000 39.330  ? 72  ARG HHH CD  1 
ATOM 13086 N NE  . ARG H 3 72  ? 112.853 4.629   78.301  1.000 37.620  ? 72  ARG HHH NE  1 
ATOM 13087 C CZ  . ARG H 3 72  ? 112.855 4.476   76.982  1.000 35.760  ? 72  ARG HHH CZ  1 
ATOM 13088 N NH1 . ARG H 3 72  ? 112.734 3.266   76.472  1.000 36.940  ? 72  ARG HHH NH1 1 
ATOM 13089 N NH2 . ARG H 3 72  ? 112.968 5.510   76.164  1.000 34.410  ? 72  ARG HHH NH2 1 
ATOM 13090 N N   . ASP H 3 73  ? 109.999 3.705   82.737  1.000 36.350  ? 73  ASP HHH N   1 
ATOM 13091 C CA  . ASP H 3 73  ? 110.511 2.676   83.680  1.000 38.240  ? 73  ASP HHH CA  1 
ATOM 13092 C C   . ASP H 3 73  ? 110.949 1.490   82.827  1.000 36.430  ? 73  ASP HHH C   1 
ATOM 13093 O O   . ASP H 3 73  ? 110.073 0.719   82.383  1.000 36.070  ? 73  ASP HHH O   1 
ATOM 13094 C CB  . ASP H 3 73  ? 109.466 2.296   84.733  1.000 41.660  ? 73  ASP HHH CB  1 
ATOM 13095 C CG  . ASP H 3 73  ? 109.964 1.380   85.848  1.000 45.910  ? 73  ASP HHH CG  1 
ATOM 13096 O OD1 . ASP H 3 73  ? 111.111 0.844   85.738  1.000 50.680  ? 73  ASP HHH OD1 1 
ATOM 13097 O OD2 . ASP H 3 73  ? 109.191 1.193   86.824  1.000 46.830  ? 73  ASP HHH OD2 1 
ATOM 13098 N N   . ASN H 3 74  ? 112.252 1.397   82.567  1.000 37.530  ? 74  ASN HHH N   1 
ATOM 13099 C CA  . ASN H 3 74  ? 112.823 0.419   81.605  1.000 38.730  ? 74  ASN HHH CA  1 
ATOM 13100 C C   . ASN H 3 74  ? 112.701 -0.979  82.204  1.000 40.250  ? 74  ASN HHH C   1 
ATOM 13101 O O   . ASN H 3 74  ? 112.589 -1.927  81.430  1.000 39.420  ? 74  ASN HHH O   1 
ATOM 13102 C CB  . ASN H 3 74  ? 114.271 0.755   81.219  1.000 38.210  ? 74  ASN HHH CB  1 
ATOM 13103 C CG  . ASN H 3 74  ? 114.368 1.800   80.135  1.000 36.740  ? 74  ASN HHH CG  1 
ATOM 13104 O OD1 . ASN H 3 74  ? 113.365 2.146   79.499  1.000 33.640  ? 74  ASN HHH OD1 1 
ATOM 13105 N ND2 . ASN H 3 74  ? 115.583 2.283   79.915  1.000 38.380  ? 74  ASN HHH ND2 1 
ATOM 13106 N N   . ALA H 3 75  ? 112.684 -1.093  83.534  1.000 43.880  ? 75  ALA HHH N   1 
ATOM 13107 C CA  . ALA H 3 75  ? 112.462 -2.378  84.222  1.000 45.720  ? 75  ALA HHH CA  1 
ATOM 13108 C C   . ALA H 3 75  ? 111.011 -2.821  84.047  1.000 42.020  ? 75  ALA HHH C   1 
ATOM 13109 O O   . ALA H 3 75  ? 110.797 -4.009  84.008  1.000 40.630  ? 75  ALA HHH O   1 
ATOM 13110 C CB  . ALA H 3 75  ? 112.840 -2.254  85.673  1.000 53.960  ? 75  ALA HHH CB  1 
ATOM 13111 N N   . ARG H 3 76  ? 110.048 -1.904  83.954  1.000 48.540  ? 76  ARG HHH N   1 
ATOM 13112 C CA  . ARG H 3 76  ? 108.602 -2.253  83.863  1.000 51.900  ? 76  ARG HHH CA  1 
ATOM 13113 C C   . ARG H 3 76  ? 108.139 -2.133  82.398  1.000 46.980  ? 76  ARG HHH C   1 
ATOM 13114 O O   . ARG H 3 76  ? 106.931 -2.255  82.172  1.000 47.070  ? 76  ARG HHH O   1 
ATOM 13115 C CB  . ARG H 3 76  ? 107.761 -1.388  84.822  1.000 58.750  ? 76  ARG HHH CB  1 
ATOM 13116 C CG  . ARG H 3 76  ? 107.735 -1.837  86.288  1.000 64.350  ? 76  ARG HHH CG  1 
ATOM 13117 C CD  . ARG H 3 76  ? 106.847 -1.025  87.246  1.000 68.980  ? 76  ARG HHH CD  1 
ATOM 13118 N NE  . ARG H 3 76  ? 105.444 -1.457  87.397  1.000 68.820  ? 76  ARG HHH NE  1 
ATOM 13119 C CZ  . ARG H 3 76  ? 104.486 -0.759  88.021  1.000 59.930  ? 76  ARG HHH CZ  1 
ATOM 13120 N N   . ASN H 3 77  ? 109.043 -1.931  81.431  1.000 40.100  ? 77  ASN HHH N   1 
ATOM 13121 C CA  . ASN H 3 77  ? 108.734 -1.868  79.975  1.000 41.250  ? 77  ASN HHH CA  1 
ATOM 13122 C C   . ASN H 3 77  ? 107.604 -0.869  79.716  1.000 41.250  ? 77  ASN HHH C   1 
ATOM 13123 O O   . ASN H 3 77  ? 106.694 -1.210  78.942  1.000 43.560  ? 77  ASN HHH O   1 
ATOM 13124 C CB  . ASN H 3 77  ? 108.333 -3.233  79.403  1.000 43.130  ? 77  ASN HHH CB  1 
ATOM 13125 C CG  . ASN H 3 77  ? 109.508 -4.134  79.074  1.000 44.420  ? 77  ASN HHH CG  1 
ATOM 13126 O OD1 . ASN H 3 77  ? 110.383 -3.790  78.277  1.000 50.060  ? 77  ASN HHH OD1 1 
ATOM 13127 N ND2 . ASN H 3 77  ? 109.529 -5.318  79.652  1.000 44.520  ? 77  ASN HHH ND2 1 
ATOM 13128 N N   . SER H 3 78  ? 107.656 0.318   80.327  1.000 40.420  ? 78  SER HHH N   1 
ATOM 13129 C CA  . SER H 3 78  ? 106.540 1.303   80.302  1.000 38.030  ? 78  SER HHH CA  1 
ATOM 13130 C C   . SER H 3 78  ? 107.030 2.734   80.101  1.000 33.770  ? 78  SER HHH C   1 
ATOM 13131 O O   . SER H 3 78  ? 107.978 3.149   80.761  1.000 34.510  ? 78  SER HHH O   1 
ATOM 13132 C CB  . SER H 3 78  ? 105.713 1.195   81.546  1.000 38.650  ? 78  SER HHH CB  1 
ATOM 13133 O OG  . SER H 3 78  ? 104.951 0.006   81.499  1.000 40.430  ? 78  SER HHH OG  1 
ATOM 13134 N N   . LEU H 3 79  ? 106.334 3.456   79.237  1.000 33.910  ? 79  LEU HHH N   1 
ATOM 13135 C CA  . LEU H 3 79  ? 106.489 4.912   79.028  1.000 36.220  ? 79  LEU HHH CA  1 
ATOM 13136 C C   . LEU H 3 79  ? 105.289 5.601   79.682  1.000 39.320  ? 79  LEU HHH C   1 
ATOM 13137 O O   . LEU H 3 79  ? 104.165 5.044   79.582  1.000 41.610  ? 79  LEU HHH O   1 
ATOM 13138 C CB  . LEU H 3 79  ? 106.528 5.167   77.521  1.000 36.720  ? 79  LEU HHH CB  1 
ATOM 13139 C CG  . LEU H 3 79  ? 106.424 6.625   77.105  1.000 38.270  ? 79  LEU HHH CG  1 
ATOM 13140 C CD1 . LEU H 3 79  ? 107.770 7.312   77.258  1.000 41.020  ? 79  LEU HHH CD1 1 
ATOM 13141 C CD2 . LEU H 3 79  ? 105.927 6.731   75.672  1.000 38.900  ? 79  LEU HHH CD2 1 
ATOM 13142 N N   . TYR H 3 80  ? 105.518 6.745   80.330  1.000 38.140  ? 80  TYR HHH N   1 
ATOM 13143 C CA  . TYR H 3 80  ? 104.464 7.518   81.036  1.000 39.420  ? 80  TYR HHH CA  1 
ATOM 13144 C C   . TYR H 3 80  ? 104.466 8.971   80.555  1.000 41.340  ? 80  TYR HHH C   1 
ATOM 13145 O O   . TYR H 3 80  ? 105.538 9.523   80.187  1.000 39.640  ? 80  TYR HHH O   1 
ATOM 13146 C CB  . TYR H 3 80  ? 104.656 7.465   82.553  1.000 38.950  ? 80  TYR HHH CB  1 
ATOM 13147 C CG  . TYR H 3 80  ? 104.805 6.085   83.134  1.000 41.280  ? 80  TYR HHH CG  1 
ATOM 13148 C CD1 . TYR H 3 80  ? 103.736 5.203   83.189  1.000 45.660  ? 80  TYR HHH CD1 1 
ATOM 13149 C CD2 . TYR H 3 80  ? 106.019 5.657   83.636  1.000 42.080  ? 80  TYR HHH CD2 1 
ATOM 13150 C CE1 . TYR H 3 80  ? 103.861 3.944   83.767  1.000 44.830  ? 80  TYR HHH CE1 1 
ATOM 13151 C CE2 . TYR H 3 80  ? 106.170 4.392   84.185  1.000 42.810  ? 80  TYR HHH CE2 1 
ATOM 13152 C CZ  . TYR H 3 80  ? 105.090 3.528   84.247  1.000 45.220  ? 80  TYR HHH CZ  1 
ATOM 13153 O OH  . TYR H 3 80  ? 105.239 2.272   84.768  1.000 52.500  ? 80  TYR HHH OH  1 
ATOM 13154 N N   . LEU H 3 81  ? 103.275 9.574   80.575  1.000 43.090  ? 81  LEU HHH N   1 
ATOM 13155 C CA  . LEU H 3 81  ? 103.075 11.036  80.406  1.000 43.580  ? 81  LEU HHH CA  1 
ATOM 13156 C C   . LEU H 3 81  ? 102.230 11.545  81.575  1.000 43.100  ? 81  LEU HHH C   1 
ATOM 13157 O O   . LEU H 3 81  ? 101.065 11.131  81.683  1.000 48.880  ? 81  LEU HHH O   1 
ATOM 13158 C CB  . LEU H 3 81  ? 102.395 11.328  79.063  1.000 46.160  ? 81  LEU HHH CB  1 
ATOM 13159 C CG  . LEU H 3 81  ? 102.210 12.808  78.740  1.000 45.540  ? 81  LEU HHH CG  1 
ATOM 13160 C CD1 . LEU H 3 81  ? 103.552 13.501  78.638  1.000 46.300  ? 81  LEU HHH CD1 1 
ATOM 13161 C CD2 . LEU H 3 81  ? 101.424 13.003  77.441  1.000 45.760  ? 81  LEU HHH CD2 1 
ATOM 13162 N N   . GLN H 3 82  ? 102.812 12.415  82.401  1.000 43.900  ? 82  GLN HHH N   1 
ATOM 13163 C CA  . GLN H 3 82  ? 102.126 13.135  83.500  1.000 44.800  ? 82  GLN HHH CA  1 
ATOM 13164 C C   . GLN H 3 82  ? 101.522 14.421  82.945  1.000 46.870  ? 82  GLN HHH C   1 
ATOM 13165 O O   . GLN H 3 82  ? 102.309 15.322  82.581  1.000 57.020  ? 82  GLN HHH O   1 
ATOM 13166 C CB  . GLN H 3 82  ? 103.120 13.469  84.618  1.000 45.370  ? 82  GLN HHH CB  1 
ATOM 13167 C CG  . GLN H 3 82  ? 102.463 14.073  85.851  1.000 44.130  ? 82  GLN HHH CG  1 
ATOM 13168 C CD  . GLN H 3 82  ? 101.285 13.226  86.311  1.000 41.630  ? 82  GLN HHH CD  1 
ATOM 13169 O OE1 . GLN H 3 82  ? 101.448 12.044  86.662  1.000 35.460  ? 82  GLN HHH OE1 1 
ATOM 13170 N NE2 . GLN H 3 82  ? 100.099 13.824  86.258  1.000 37.870  ? 82  GLN HHH NE2 1 
ATOM 13171 N N   . MET H 3 83  ? 100.185 14.501  82.875  1.000 45.020  ? 83  MET HHH N   1 
ATOM 13172 C CA  . MET H 3 83  ? 99.457  15.663  82.296  1.000 45.780  ? 83  MET HHH CA  1 
ATOM 13173 C C   . MET H 3 83  ? 98.821  16.459  83.432  1.000 41.800  ? 83  MET HHH C   1 
ATOM 13174 O O   . MET H 3 83  ? 97.821  15.981  83.998  1.000 46.560  ? 83  MET HHH O   1 
ATOM 13175 C CB  . MET H 3 83  ? 98.375  15.207  81.305  1.000 47.800  ? 83  MET HHH CB  1 
ATOM 13176 C CG  . MET H 3 83  ? 98.937  14.388  80.163  1.000 47.510  ? 83  MET HHH CG  1 
ATOM 13177 S SD  . MET H 3 83  ? 97.755  13.436  79.252  1.000 49.720  ? 83  MET HHH SD  1 
ATOM 13178 C CE  . MET H 3 83  ? 97.045  14.695  78.181  1.000 51.560  ? 83  MET HHH CE  1 
ATOM 13179 N N   . ASN H 3 84  ? 99.397  17.623  83.747  1.000 39.880  ? 84  ASN HHH N   1 
ATOM 13180 C CA  . ASN H 3 84  ? 98.879  18.545  84.787  1.000 40.150  ? 84  ASN HHH CA  1 
ATOM 13181 C C   . ASN H 3 84  ? 98.247  19.745  84.098  1.000 42.520  ? 84  ASN HHH C   1 
ATOM 13182 O O   . ASN H 3 84  ? 98.608  19.996  82.936  1.000 49.150  ? 84  ASN HHH O   1 
ATOM 13183 C CB  . ASN H 3 84  ? 99.981  19.001  85.737  1.000 37.160  ? 84  ASN HHH CB  1 
ATOM 13184 C CG  . ASN H 3 84  ? 100.567 17.848  86.505  1.000 37.660  ? 84  ASN HHH CG  1 
ATOM 13185 O OD1 . ASN H 3 84  ? 99.958  16.778  86.637  1.000 34.210  ? 84  ASN HHH OD1 1 
ATOM 13186 N ND2 . ASN H 3 84  ? 101.766 18.063  87.019  1.000 42.850  ? 84  ASN HHH ND2 1 
ATOM 13187 N N   . SER H 3 85  ? 97.347  20.450  84.785  1.000 40.970  ? 85  SER HHH N   1 
ATOM 13188 C CA  . SER H 3 85  ? 96.791  21.748  84.326  1.000 47.020  ? 85  SER HHH CA  1 
ATOM 13189 C C   . SER H 3 85  ? 96.131  21.572  82.962  1.000 49.290  ? 85  SER HHH C   1 
ATOM 13190 O O   . SER H 3 85  ? 96.238  22.494  82.101  1.000 47.930  ? 85  SER HHH O   1 
ATOM 13191 C CB  . SER H 3 85  ? 97.865  22.804  84.277  1.000 50.720  ? 85  SER HHH CB  1 
ATOM 13192 O OG  . SER H 3 85  ? 98.536  22.834  85.531  1.000 50.570  ? 85  SER HHH OG  1 
ATOM 13193 N N   . LEU H 3 86  ? 95.456  20.435  82.789  1.000 49.560  ? 86  LEU HHH N   1 
ATOM 13194 C CA  . LEU H 3 86  ? 94.799  20.056  81.511  1.000 50.180  ? 86  LEU HHH CA  1 
ATOM 13195 C C   . LEU H 3 86  ? 93.860  21.176  81.057  1.000 49.330  ? 86  LEU HHH C   1 
ATOM 13196 O O   . LEU H 3 86  ? 93.209  21.798  81.906  1.000 53.540  ? 86  LEU HHH O   1 
ATOM 13197 C CB  . LEU H 3 86  ? 94.052  18.737  81.723  1.000 49.670  ? 86  LEU HHH CB  1 
ATOM 13198 C CG  . LEU H 3 86  ? 94.912  17.493  81.519  1.000 51.450  ? 86  LEU HHH CG  1 
ATOM 13199 C CD1 . LEU H 3 86  ? 94.238  16.218  82.029  1.000 48.930  ? 86  LEU HHH CD1 1 
ATOM 13200 C CD2 . LEU H 3 86  ? 95.281  17.370  80.045  1.000 54.580  ? 86  LEU HHH CD2 1 
ATOM 13201 N N   . ARG H 3 87  ? 93.804  21.425  79.756  1.000 49.750  ? 87  ARG HHH N   1 
ATOM 13202 C CA  . ARG H 3 87  ? 92.917  22.442  79.141  1.000 50.510  ? 87  ARG HHH CA  1 
ATOM 13203 C C   . ARG H 3 87  ? 92.015  21.766  78.120  1.000 54.280  ? 87  ARG HHH C   1 
ATOM 13204 O O   . ARG H 3 87  ? 92.224  20.583  77.842  1.000 58.270  ? 87  ARG HHH O   1 
ATOM 13205 C CB  . ARG H 3 87  ? 93.757  23.509  78.460  1.000 47.390  ? 87  ARG HHH CB  1 
ATOM 13206 C CG  . ARG H 3 87  ? 94.899  24.008  79.326  1.000 45.250  ? 87  ARG HHH CG  1 
ATOM 13207 C CD  . ARG H 3 87  ? 95.749  24.932  78.493  1.000 43.300  ? 87  ARG HHH CD  1 
ATOM 13208 N NE  . ARG H 3 87  ? 96.873  25.472  79.217  1.000 39.540  ? 87  ARG HHH NE  1 
ATOM 13209 C CZ  . ARG H 3 87  ? 97.885  26.071  78.643  1.000 39.410  ? 87  ARG HHH CZ  1 
ATOM 13210 N NH1 . ARG H 3 87  ? 97.913  26.170  77.331  1.000 43.650  ? 87  ARG HHH NH1 1 
ATOM 13211 N NH2 . ARG H 3 87  ? 98.872  26.549  79.374  1.000 42.110  ? 87  ARG HHH NH2 1 
ATOM 13212 N N   . VAL H 3 88  ? 91.026  22.493  77.616  1.000 59.980  ? 88  VAL HHH N   1 
ATOM 13213 C CA  . VAL H 3 88  ? 90.025  21.965  76.646  1.000 64.360  ? 88  VAL HHH CA  1 
ATOM 13214 C C   . VAL H 3 88  ? 90.772  21.540  75.374  1.000 61.700  ? 88  VAL HHH C   1 
ATOM 13215 O O   . VAL H 3 88  ? 90.482  20.440  74.874  1.000 55.130  ? 88  VAL HHH O   1 
ATOM 13216 C CB  . VAL H 3 88  ? 88.941  23.032  76.396  1.000 70.240  ? 88  VAL HHH CB  1 
ATOM 13217 C CG1 . VAL H 3 88  ? 88.089  22.775  75.150  1.000 69.360  ? 88  VAL HHH CG1 1 
ATOM 13218 C CG2 . VAL H 3 88  ? 88.103  23.192  77.659  1.000 67.220  ? 88  VAL HHH CG2 1 
ATOM 13219 N N   . GLU H 3 89  ? 91.725  22.345  74.904  1.000 61.180  ? 89  GLU HHH N   1 
ATOM 13220 C CA  . GLU H 3 89  ? 92.482  22.067  73.639  1.000 62.510  ? 89  GLU HHH CA  1 
ATOM 13221 C C   . GLU H 3 89  ? 93.273  20.763  73.788  1.000 58.180  ? 89  GLU HHH C   1 
ATOM 13222 O O   . GLU H 3 89  ? 93.477  20.109  72.764  1.000 66.070  ? 89  GLU HHH O   1 
ATOM 13223 C CB  . GLU H 3 89  ? 93.396  23.218  73.204  1.000 66.380  ? 89  GLU HHH CB  1 
ATOM 13224 C CG  . GLU H 3 89  ? 94.062  23.982  74.332  1.000 69.350  ? 89  GLU HHH CG  1 
ATOM 13225 C CD  . GLU H 3 89  ? 93.165  24.923  75.126  1.000 67.260  ? 89  GLU HHH CD  1 
ATOM 13226 O OE1 . GLU H 3 89  ? 91.929  24.948  74.897  1.000 66.580  ? 89  GLU HHH OE1 1 
ATOM 13227 O OE2 . GLU H 3 89  ? 93.699  25.518  76.055  1.000 70.570  ? 89  GLU HHH OE2 1 
ATOM 13228 N N   . ASP H 3 90  ? 93.656  20.369  74.997  1.000 53.730  ? 90  ASP HHH N   1 
ATOM 13229 C CA  . ASP H 3 90  ? 94.416  19.107  75.230  1.000 53.840  ? 90  ASP HHH CA  1 
ATOM 13230 C C   . ASP H 3 90  ? 93.563  17.868  74.910  1.000 55.260  ? 90  ASP HHH C   1 
ATOM 13231 O O   . ASP H 3 90  ? 94.129  16.760  74.922  1.000 51.790  ? 90  ASP HHH O   1 
ATOM 13232 C CB  . ASP H 3 90  ? 94.970  19.005  76.655  1.000 47.090  ? 90  ASP HHH CB  1 
ATOM 13233 C CG  . ASP H 3 90  ? 96.009  20.063  76.981  1.000 42.500  ? 90  ASP HHH CG  1 
ATOM 13234 O OD1 . ASP H 3 90  ? 96.632  20.606  76.017  1.000 37.650  ? 90  ASP HHH OD1 1 
ATOM 13235 O OD2 . ASP H 3 90  ? 96.168  20.359  78.186  1.000 35.790  ? 90  ASP HHH OD2 1 
ATOM 13236 N N   . THR H 3 91  ? 92.273  18.031  74.636  1.000 57.910  ? 91  THR HHH N   1 
ATOM 13237 C CA  . THR H 3 91  ? 91.393  16.922  74.191  1.000 55.300  ? 91  THR HHH CA  1 
ATOM 13238 C C   . THR H 3 91  ? 91.944  16.351  72.892  1.000 48.260  ? 91  THR HHH C   1 
ATOM 13239 O O   . THR H 3 91  ? 92.107  17.131  71.924  1.000 43.880  ? 91  THR HHH O   1 
ATOM 13240 C CB  . THR H 3 91  ? 89.943  17.353  73.975  1.000 59.480  ? 91  THR HHH CB  1 
ATOM 13241 O OG1 . THR H 3 91  ? 89.455  17.781  75.248  1.000 59.530  ? 91  THR HHH OG1 1 
ATOM 13242 C CG2 . THR H 3 91  ? 89.074  16.226  73.471  1.000 65.540  ? 91  THR HHH CG2 1 
ATOM 13243 N N   . ALA H 3 92  ? 92.233  15.053  72.893  1.000 44.830  ? 92  ALA HHH N   1 
ATOM 13244 C CA  . ALA H 3 92  ? 92.801  14.320  71.742  1.000 46.210  ? 92  ALA HHH CA  1 
ATOM 13245 C C   . ALA H 3 92  ? 92.906  12.840  72.094  1.000 48.430  ? 92  ALA HHH C   1 
ATOM 13246 O O   . ALA H 3 92  ? 92.793  12.486  73.297  1.000 56.400  ? 92  ALA HHH O   1 
ATOM 13247 C CB  . ALA H 3 92  ? 94.156  14.868  71.393  1.000 45.000  ? 92  ALA HHH CB  1 
ATOM 13248 N N   . VAL H 3 93  ? 93.119  12.012  71.075  1.000 46.830  ? 93  VAL HHH N   1 
ATOM 13249 C CA  . VAL H 3 93  ? 93.667  10.643  71.249  1.000 48.650  ? 93  VAL HHH CA  1 
ATOM 13250 C C   . VAL H 3 93  ? 95.178  10.813  71.439  1.000 49.960  ? 93  VAL HHH C   1 
ATOM 13251 O O   . VAL H 3 93  ? 95.795  11.556  70.640  1.000 45.580  ? 93  VAL HHH O   1 
ATOM 13252 C CB  . VAL H 3 93  ? 93.346  9.747   70.046  1.000 53.410  ? 93  VAL HHH CB  1 
ATOM 13253 C CG1 . VAL H 3 93  ? 93.915  8.358   70.246  1.000 56.540  ? 93  VAL HHH CG1 1 
ATOM 13254 C CG2 . VAL H 3 93  ? 91.851  9.681   69.781  1.000 58.440  ? 93  VAL HHH CG2 1 
ATOM 13255 N N   . TYR H 3 94  ? 95.739  10.179  72.475  1.000 47.970  ? 94  TYR HHH N   1 
ATOM 13256 C CA  . TYR H 3 94  ? 97.177  10.240  72.825  1.000 42.500  ? 94  TYR HHH CA  1 
ATOM 13257 C C   . TYR H 3 94  ? 97.818  8.922   72.397  1.000 39.410  ? 94  TYR HHH C   1 
ATOM 13258 O O   . TYR H 3 94  ? 97.658  7.908   73.106  1.000 36.080  ? 94  TYR HHH O   1 
ATOM 13259 C CB  . TYR H 3 94  ? 97.360  10.573  74.309  1.000 43.900  ? 94  TYR HHH CB  1 
ATOM 13260 C CG  . TYR H 3 94  ? 97.220  12.047  74.586  1.000 44.430  ? 94  TYR HHH CG  1 
ATOM 13261 C CD1 . TYR H 3 94  ? 96.020  12.687  74.392  1.000 44.610  ? 94  TYR HHH CD1 1 
ATOM 13262 C CD2 . TYR H 3 94  ? 98.307  12.808  74.975  1.000 45.480  ? 94  TYR HHH CD2 1 
ATOM 13263 C CE1 . TYR H 3 94  ? 95.871  14.045  74.601  1.000 46.950  ? 94  TYR HHH CE1 1 
ATOM 13264 C CE2 . TYR H 3 94  ? 98.191  14.176  75.173  1.000 43.850  ? 94  TYR HHH CE2 1 
ATOM 13265 C CZ  . TYR H 3 94  ? 96.970  14.795  74.985  1.000 44.730  ? 94  TYR HHH CZ  1 
ATOM 13266 O OH  . TYR H 3 94  ? 96.846  16.135  75.192  1.000 49.120  ? 94  TYR HHH OH  1 
ATOM 13267 N N   . TYR H 3 95  ? 98.498  8.962   71.244  1.000 38.820  ? 95  TYR HHH N   1 
ATOM 13268 C CA  . TYR H 3 95  ? 99.288  7.843   70.684  1.000 39.300  ? 95  TYR HHH CA  1 
ATOM 13269 C C   . TYR H 3 95  ? 100.691 7.818   71.336  1.000 41.320  ? 95  TYR HHH C   1 
ATOM 13270 O O   . TYR H 3 95  ? 101.277 8.860   71.738  1.000 37.590  ? 95  TYR HHH O   1 
ATOM 13271 C CB  . TYR H 3 95  ? 99.302  7.899   69.151  1.000 34.790  ? 95  TYR HHH CB  1 
ATOM 13272 C CG  . TYR H 3 95  ? 97.966  7.736   68.471  1.000 32.820  ? 95  TYR HHH CG  1 
ATOM 13273 C CD1 . TYR H 3 95  ? 97.340  6.504   68.366  1.000 33.320  ? 95  TYR HHH CD1 1 
ATOM 13274 C CD2 . TYR H 3 95  ? 97.329  8.816   67.877  1.000 34.480  ? 95  TYR HHH CD2 1 
ATOM 13275 C CE1 . TYR H 3 95  ? 96.109  6.363   67.725  1.000 34.910  ? 95  TYR HHH CE1 1 
ATOM 13276 C CE2 . TYR H 3 95  ? 96.098  8.689   67.228  1.000 36.060  ? 95  TYR HHH CE2 1 
ATOM 13277 C CZ  . TYR H 3 95  ? 95.472  7.457   67.151  1.000 34.220  ? 95  TYR HHH CZ  1 
ATOM 13278 N N   . CYS H 3 96  ? 101.202 6.599   71.471  1.000 41.040  ? 96  CYS HHH N   1 
ATOM 13279 C CA  . CYS H 3 96  ? 102.558 6.261   71.955  1.000 39.600  ? 96  CYS HHH CA  1 
ATOM 13280 C C   . CYS H 3 96  ? 103.324 5.648   70.772  1.000 38.920  ? 96  CYS HHH C   1 
ATOM 13281 O O   . CYS H 3 96  ? 102.784 4.706   70.162  1.000 44.270  ? 96  CYS HHH O   1 
ATOM 13282 C CB  . CYS H 3 96  ? 102.397 5.316   73.140  1.000 40.340  ? 96  CYS HHH CB  1 
ATOM 13283 S SG  . CYS H 3 96  ? 103.951 4.869   73.930  1.000 51.170  ? 96  CYS HHH SG  1 
ATOM 13284 N N   . ALA H 3 97  ? 104.495 6.178   70.415  1.000 39.370  ? 97  ALA HHH N   1 
ATOM 13285 C CA  . ALA H 3 97  ? 105.225 5.812   69.171  1.000 39.140  ? 97  ALA HHH CA  1 
ATOM 13286 C C   . ALA H 3 97  ? 106.724 5.619   69.425  1.000 36.910  ? 97  ALA HHH C   1 
ATOM 13287 O O   . ALA H 3 97  ? 107.309 6.414   70.178  1.000 43.960  ? 97  ALA HHH O   1 
ATOM 13288 C CB  . ALA H 3 97  ? 105.001 6.832   68.076  1.000 38.170  ? 97  ALA HHH CB  1 
ATOM 13289 N N   . ARG H 3 98  ? 107.317 4.603   68.798  1.000 34.000  ? 98  ARG HHH N   1 
ATOM 13290 C CA  . ARG H 3 98  ? 108.769 4.317   68.886  1.000 33.540  ? 98  ARG HHH CA  1 
ATOM 13291 C C   . ARG H 3 98  ? 109.531 5.058   67.778  1.000 32.730  ? 98  ARG HHH C   1 
ATOM 13292 O O   . ARG H 3 98  ? 109.007 5.149   66.650  1.000 33.740  ? 98  ARG HHH O   1 
ATOM 13293 C CB  . ARG H 3 98  ? 109.049 2.822   68.744  1.000 32.890  ? 98  ARG HHH CB  1 
ATOM 13294 C CG  . ARG H 3 98  ? 110.492 2.474   69.076  1.000 33.870  ? 98  ARG HHH CG  1 
ATOM 13295 C CD  . ARG H 3 98  ? 110.767 1.003   68.926  1.000 35.180  ? 98  ARG HHH CD  1 
ATOM 13296 N NE  . ARG H 3 98  ? 110.767 0.621   67.518  1.000 34.850  ? 98  ARG HHH NE  1 
ATOM 13297 C CZ  . ARG H 3 98  ? 111.142 -0.557  67.069  1.000 32.430  ? 98  ARG HHH CZ  1 
ATOM 13298 N NH1 . ARG H 3 98  ? 111.538 -1.499  67.903  1.000 32.110  ? 98  ARG HHH NH1 1 
ATOM 13299 N NH2 . ARG H 3 98  ? 111.101 -0.790  65.777  1.000 33.020  ? 98  ARG HHH NH2 1 
ATOM 13300 N N   . TYR H 3 99  ? 110.735 5.545   68.092  1.000 30.880  ? 99  TYR HHH N   1 
ATOM 13301 C CA  . TYR H 3 99  ? 111.756 5.990   67.109  1.000 28.820  ? 99  TYR HHH CA  1 
ATOM 13302 C C   . TYR H 3 99  ? 112.944 5.022   67.164  1.000 26.100  ? 99  TYR HHH C   1 
ATOM 13303 O O   . TYR H 3 99  ? 113.548 4.793   68.230  1.000 22.750  ? 99  TYR HHH O   1 
ATOM 13304 C CB  . TYR H 3 99  ? 112.187 7.448   67.332  1.000 28.240  ? 99  TYR HHH CB  1 
ATOM 13305 C CG  . TYR H 3 99  ? 113.482 7.808   66.636  1.000 27.550  ? 99  TYR HHH CG  1 
ATOM 13306 C CD1 . TYR H 3 99  ? 114.703 7.424   67.175  1.000 28.410  ? 99  TYR HHH CD1 1 
ATOM 13307 C CD2 . TYR H 3 99  ? 113.510 8.528   65.452  1.000 25.670  ? 99  TYR HHH CD2 1 
ATOM 13308 C CE1 . TYR H 3 99  ? 115.904 7.749   66.565  1.000 27.130  ? 99  TYR HHH CE1 1 
ATOM 13309 C CE2 . TYR H 3 99  ? 114.709 8.866   64.830  1.000 25.650  ? 99  TYR HHH CE2 1 
ATOM 13310 C CZ  . TYR H 3 99  ? 115.918 8.478   65.390  1.000 26.700  ? 99  TYR HHH CZ  1 
ATOM 13311 O OH  . TYR H 3 99  ? 117.147 8.702   64.814  1.000 27.800  ? 99  TYR HHH OH  1 
ATOM 13312 N N   . ALA H 3 100 ? 113.262 4.479   66.005  1.000 27.340  ? 100 ALA HHH N   1 
ATOM 13313 C CA  . ALA H 3 100 ? 114.464 3.656   65.764  1.000 29.790  ? 100 ALA HHH CA  1 
ATOM 13314 C C   . ALA H 3 100 ? 115.347 4.387   64.752  1.000 28.210  ? 100 ALA HHH C   1 
ATOM 13315 O O   . ALA H 3 100 ? 114.798 5.099   63.915  1.000 26.580  ? 100 ALA HHH O   1 
ATOM 13316 C CB  . ALA H 3 100 ? 114.078 2.284   65.260  1.000 31.340  ? 100 ALA HHH CB  1 
ATOM 13317 N N   . HIS H 3 101 ? 116.655 4.149   64.774  1.000 27.270  ? 101 HIS HHH N   1 
ATOM 13318 C CA  . HIS H 3 101 ? 117.605 4.802   63.843  1.000 26.430  ? 101 HIS HHH CA  1 
ATOM 13319 C C   . HIS H 3 101 ? 117.317 4.432   62.397  1.000 28.820  ? 101 HIS HHH C   1 
ATOM 13320 O O   . HIS H 3 101 ? 117.097 3.237   62.175  1.000 35.770  ? 101 HIS HHH O   1 
ATOM 13321 C CB  . HIS H 3 101 ? 119.033 4.404   64.208  1.000 24.760  ? 101 HIS HHH CB  1 
ATOM 13322 C CG  . HIS H 3 101 ? 120.079 5.074   63.390  1.000 24.010  ? 101 HIS HHH CG  1 
ATOM 13323 N ND1 . HIS H 3 101 ? 121.034 4.364   62.692  1.000 25.000  ? 101 HIS HHH ND1 1 
ATOM 13324 C CD2 . HIS H 3 101 ? 120.335 6.376   63.159  1.000 23.110  ? 101 HIS HHH CD2 1 
ATOM 13325 C CE1 . HIS H 3 101 ? 121.830 5.199   62.068  1.000 23.150  ? 101 HIS HHH CE1 1 
ATOM 13326 N NE2 . HIS H 3 101 ? 121.425 6.436   62.332  1.000 22.350  ? 101 HIS HHH NE2 1 
ATOM 13327 N N   . ASP H 3 102 ? 117.322 5.407   61.480  1.000 30.190  ? 102 ASP HHH N   1 
ATOM 13328 C CA  . ASP H 3 102 ? 117.102 5.211   60.017  1.000 29.330  ? 102 ASP HHH CA  1 
ATOM 13329 C C   . ASP H 3 102 ? 115.628 4.964   59.713  1.000 28.660  ? 102 ASP HHH C   1 
ATOM 13330 O O   . ASP H 3 102 ? 115.122 5.542   58.748  1.000 27.520  ? 102 ASP HHH O   1 
ATOM 13331 C CB  . ASP H 3 102 ? 118.127 4.257   59.407  1.000 32.020  ? 102 ASP HHH CB  1 
ATOM 13332 C CG  . ASP H 3 102 ? 118.023 3.997   57.918  1.000 35.440  ? 102 ASP HHH CG  1 
ATOM 13333 O OD1 . ASP H 3 102 ? 118.227 4.949   57.177  1.000 35.150  ? 102 ASP HHH OD1 1 
ATOM 13334 O OD2 . ASP H 3 102 ? 117.809 2.836   57.518  1.000 37.170  ? 102 ASP HHH OD2 1 
ATOM 13335 N N   . TRP H 3 103 ? 114.977 4.149   60.530  1.000 30.250  ? 103 TRP HHH N   1 
ATOM 13336 C CA  . TRP H 3 103 ? 113.548 3.829   60.333  1.000 31.670  ? 103 TRP HHH CA  1 
ATOM 13337 C C   . TRP H 3 103 ? 112.771 5.061   60.752  1.000 32.330  ? 103 TRP HHH C   1 
ATOM 13338 O O   . TRP H 3 103 ? 111.717 5.289   60.159  1.000 29.860  ? 103 TRP HHH O   1 
ATOM 13339 C CB  . TRP H 3 103 ? 113.180 2.657   61.230  1.000 32.360  ? 103 TRP HHH CB  1 
ATOM 13340 C CG  . TRP H 3 103 ? 113.510 1.299   60.708  1.000 34.910  ? 103 TRP HHH CG  1 
ATOM 13341 C CD1 . TRP H 3 103 ? 114.604 0.544   61.006  1.000 41.600  ? 103 TRP HHH CD1 1 
ATOM 13342 C CD2 . TRP H 3 103 ? 112.698 0.506   59.831  1.000 35.880  ? 103 TRP HHH CD2 1 
ATOM 13343 N NE1 . TRP H 3 103 ? 114.536 -0.657  60.356  1.000 40.970  ? 103 TRP HHH NE1 1 
ATOM 13344 C CE2 . TRP H 3 103 ? 113.377 -0.709  59.630  1.000 36.620  ? 103 TRP HHH CE2 1 
ATOM 13345 C CE3 . TRP H 3 103 ? 111.472 0.710   59.194  1.000 39.440  ? 103 TRP HHH CE3 1 
ATOM 13346 C CZ2 . TRP H 3 103 ? 112.865 -1.717  58.818  1.000 35.250  ? 103 TRP HHH CZ2 1 
ATOM 13347 C CZ3 . TRP H 3 103 ? 110.970 -0.286  58.390  1.000 38.240  ? 103 TRP HHH CZ3 1 
ATOM 13348 C CH2 . TRP H 3 103 ? 111.664 -1.477  58.197  1.000 36.040  ? 103 TRP HHH CH2 1 
ATOM 13349 N N   . ASN H 3 104 ? 113.281 5.794   61.740  1.000 35.170  ? 104 ASN HHH N   1 
ATOM 13350 C CA  . ASN H 3 104 ? 112.624 7.014   62.273  1.000 37.390  ? 104 ASN HHH CA  1 
ATOM 13351 C C   . ASN H 3 104 ? 111.407 6.583   63.101  1.000 37.180  ? 104 ASN HHH C   1 
ATOM 13352 O O   . ASN H 3 104 ? 111.483 5.516   63.700  1.000 33.470  ? 104 ASN HHH O   1 
ATOM 13353 C CB  . ASN H 3 104 ? 112.476 8.125   61.232  1.000 38.960  ? 104 ASN HHH CB  1 
ATOM 13354 C CG  . ASN H 3 104 ? 113.777 8.501   60.561  1.000 40.430  ? 104 ASN HHH CG  1 
ATOM 13355 O OD1 . ASN H 3 104 ? 113.864 8.506   59.339  1.000 40.830  ? 104 ASN HHH OD1 1 
ATOM 13356 N ND2 . ASN H 3 104 ? 114.789 8.818   61.349  1.000 39.960  ? 104 ASN HHH ND2 1 
ATOM 13357 N N   . VAL H 3 105 ? 110.347 7.383   63.152  1.000 39.610  ? 105 VAL HHH N   1 
ATOM 13358 C CA  . VAL H 3 105 ? 109.133 6.922   63.878  1.000 38.720  ? 105 VAL HHH CA  1 
ATOM 13359 C C   . VAL H 3 105 ? 108.535 5.761   63.094  1.000 38.390  ? 105 VAL HHH C   1 
ATOM 13360 O O   . VAL H 3 105 ? 108.273 5.943   61.906  1.000 34.160  ? 105 VAL HHH O   1 
ATOM 13361 C CB  . VAL H 3 105 ? 108.136 8.055   64.162  1.000 41.000  ? 105 VAL HHH CB  1 
ATOM 13362 C CG1 . VAL H 3 105 ? 106.893 7.538   64.864  1.000 43.590  ? 105 VAL HHH CG1 1 
ATOM 13363 C CG2 . VAL H 3 105 ? 108.773 9.158   64.987  1.000 43.600  ? 105 VAL HHH CG2 1 
ATOM 13364 N N   . ASP H 3 106 ? 108.351 4.607   63.740  1.000 35.370  ? 106 ASP HHH N   1 
ATOM 13365 C CA  . ASP H 3 106 ? 107.890 3.397   63.021  1.000 32.130  ? 106 ASP HHH CA  1 
ATOM 13366 C C   . ASP H 3 106 ? 106.604 2.815   63.606  1.000 32.120  ? 106 ASP HHH C   1 
ATOM 13367 O O   . ASP H 3 106 ? 105.607 2.793   62.890  1.000 36.810  ? 106 ASP HHH O   1 
ATOM 13368 C CB  . ASP H 3 106 ? 108.991 2.325   62.988  1.000 30.720  ? 106 ASP HHH CB  1 
ATOM 13369 C CG  . ASP H 3 106 ? 109.823 2.143   64.235  1.000 30.720  ? 106 ASP HHH CG  1 
ATOM 13370 O OD1 . ASP H 3 106 ? 109.352 2.476   65.323  1.000 30.310  ? 106 ASP HHH OD1 1 
ATOM 13371 O OD2 . ASP H 3 106 ? 110.936 1.624   64.097  1.000 28.380  ? 106 ASP HHH OD2 1 
ATOM 13372 N N   . TYR H 3 107 ? 106.639 2.353   64.851  1.000 32.390  ? 107 TYR HHH N   1 
ATOM 13373 C CA  . TYR H 3 107 ? 105.474 1.636   65.421  1.000 34.140  ? 107 TYR HHH CA  1 
ATOM 13374 C C   . TYR H 3 107 ? 104.645 2.550   66.314  1.000 33.830  ? 107 TYR HHH C   1 
ATOM 13375 O O   . TYR H 3 107 ? 105.231 3.379   66.995  1.000 36.690  ? 107 TYR HHH O   1 
ATOM 13376 C CB  . TYR H 3 107 ? 105.952 0.383   66.152  1.000 36.300  ? 107 TYR HHH CB  1 
ATOM 13377 C CG  . TYR H 3 107 ? 106.356 -0.765  65.268  1.000 40.410  ? 107 TYR HHH CG  1 
ATOM 13378 C CD1 . TYR H 3 107 ? 105.413 -1.642  64.765  1.000 44.360  ? 107 TYR HHH CD1 1 
ATOM 13379 C CD2 . TYR H 3 107 ? 107.683 -0.993  64.955  1.000 43.940  ? 107 TYR HHH CD2 1 
ATOM 13380 C CE1 . TYR H 3 107 ? 105.777 -2.708  63.962  1.000 42.650  ? 107 TYR HHH CE1 1 
ATOM 13381 C CE2 . TYR H 3 107 ? 108.064 -2.053  64.152  1.000 42.240  ? 107 TYR HHH CE2 1 
ATOM 13382 C CZ  . TYR H 3 107 ? 107.107 -2.914  63.654  1.000 38.660  ? 107 TYR HHH CZ  1 
ATOM 13383 O OH  . TYR H 3 107 ? 107.476 -3.963  62.863  1.000 35.720  ? 107 TYR HHH OH  1 
ATOM 13384 N N   . TRP H 3 108 ? 103.323 2.379   66.290  1.000 32.390  ? 108 TRP HHH N   1 
ATOM 13385 C CA  . TRP H 3 108 ? 102.402 3.228   67.082  1.000 33.020  ? 108 TRP HHH CA  1 
ATOM 13386 C C   . TRP H 3 108 ? 101.462 2.331   67.879  1.000 34.920  ? 108 TRP HHH C   1 
ATOM 13387 O O   . TRP H 3 108 ? 101.189 1.222   67.414  1.000 36.660  ? 108 TRP HHH O   1 
ATOM 13388 C CB  . TRP H 3 108 ? 101.567 4.129   66.169  1.000 32.240  ? 108 TRP HHH CB  1 
ATOM 13389 C CG  . TRP H 3 108 ? 102.293 5.159   65.366  1.000 33.070  ? 108 TRP HHH CG  1 
ATOM 13390 C CD1 . TRP H 3 108 ? 103.199 4.942   64.374  1.000 35.620  ? 108 TRP HHH CD1 1 
ATOM 13391 C CD2 . TRP H 3 108 ? 102.116 6.582   65.443  1.000 34.720  ? 108 TRP HHH CD2 1 
ATOM 13392 N NE1 . TRP H 3 108 ? 103.628 6.131   63.862  1.000 36.760  ? 108 TRP HHH NE1 1 
ATOM 13393 C CE2 . TRP H 3 108 ? 102.976 7.156   64.488  1.000 34.910  ? 108 TRP HHH CE2 1 
ATOM 13394 C CE3 . TRP H 3 108 ? 101.334 7.426   66.235  1.000 39.960  ? 108 TRP HHH CE3 1 
ATOM 13395 C CZ2 . TRP H 3 108 ? 103.073 8.532   64.302  1.000 36.240  ? 108 TRP HHH CZ2 1 
ATOM 13396 C CZ3 . TRP H 3 108 ? 101.427 8.785   66.050  1.000 39.280  ? 108 TRP HHH CZ3 1 
ATOM 13397 C CH2 . TRP H 3 108 ? 102.286 9.328   65.097  1.000 37.550  ? 108 TRP HHH CH2 1 
ATOM 13398 N N   . GLY H 3 109 ? 100.997 2.791   69.035  1.000 39.320  ? 109 GLY HHH N   1 
ATOM 13399 C CA  . GLY H 3 109 ? 99.995  2.052   69.817  1.000 43.310  ? 109 GLY HHH CA  1 
ATOM 13400 C C   . GLY H 3 109 ? 98.603  2.328   69.272  1.000 50.330  ? 109 GLY HHH C   1 
ATOM 13401 O O   . GLY H 3 109 ? 98.520  2.981   68.207  1.000 48.630  ? 109 GLY HHH O   1 
ATOM 13402 N N   . GLN H 3 110 ? 97.559  1.855   69.967  1.000 56.540  ? 110 GLN HHH N   1 
ATOM 13403 C CA  . GLN H 3 110 ? 96.143  1.946   69.519  1.000 57.650  ? 110 GLN HHH CA  1 
ATOM 13404 C C   . GLN H 3 110 ? 95.633  3.351   69.817  1.000 51.640  ? 110 GLN HHH C   1 
ATOM 13405 O O   . GLN H 3 110 ? 94.661  3.774   69.191  1.000 46.960  ? 110 GLN HHH O   1 
ATOM 13406 C CB  . GLN H 3 110 ? 95.268  0.896   70.210  1.000 73.470  ? 110 GLN HHH CB  1 
ATOM 13407 C CG  . GLN H 3 110 ? 95.621  -0.552  69.866  1.000 90.030  ? 110 GLN HHH CG  1 
ATOM 13408 C CD  . GLN H 3 110 ? 96.733  -1.118  70.722  1.000 91.570  ? 110 GLN HHH CD  1 
ATOM 13409 O OE1 . GLN H 3 110 ? 97.069  -0.571  71.775  1.000 99.460  ? 110 GLN HHH OE1 1 
ATOM 13410 N NE2 . GLN H 3 110 ? 97.308  -2.225  70.272  1.000 81.360  ? 110 GLN HHH NE2 1 
ATOM 13411 N N   . GLY H 3 111 ? 96.304  4.041   70.740  1.000 60.750  ? 111 GLY HHH N   1 
ATOM 13412 C CA  . GLY H 3 111 ? 95.916  5.368   71.261  1.000 64.480  ? 111 GLY HHH CA  1 
ATOM 13413 C C   . GLY H 3 111 ? 94.936  5.234   72.410  1.000 56.320  ? 111 GLY HHH C   1 
ATOM 13414 O O   . GLY H 3 111 ? 94.247  4.211   72.467  1.000 60.640  ? 111 GLY HHH O   1 
ATOM 13415 N N   . THR H 3 112 ? 94.898  6.226   73.299  1.000 49.530  ? 112 THR HHH N   1 
ATOM 13416 C CA  . THR H 3 112 ? 93.963  6.302   74.448  1.000 48.120  ? 112 THR HHH CA  1 
ATOM 13417 C C   . THR H 3 112 ? 93.321  7.682   74.459  1.000 43.080  ? 112 THR HHH C   1 
ATOM 13418 O O   . THR H 3 112 ? 94.045  8.650   74.257  1.000 42.580  ? 112 THR HHH O   1 
ATOM 13419 C CB  . THR H 3 112 ? 94.643  5.996   75.778  1.000 48.190  ? 112 THR HHH CB  1 
ATOM 13420 O OG1 . THR H 3 112 ? 93.610  5.886   76.755  1.000 56.810  ? 112 THR HHH OG1 1 
ATOM 13421 C CG2 . THR H 3 112 ? 95.616  7.058   76.215  1.000 45.850  ? 112 THR HHH CG2 1 
ATOM 13422 N N   . LEU H 3 113 ? 92.003  7.753   74.667  1.000 42.890  ? 113 LEU HHH N   1 
ATOM 13423 C CA  . LEU H 3 113 ? 91.268  9.032   74.546  1.000 43.480  ? 113 LEU HHH CA  1 
ATOM 13424 C C   . LEU H 3 113 ? 91.363  9.806   75.856  1.000 43.270  ? 113 LEU HHH C   1 
ATOM 13425 O O   . LEU H 3 113 ? 91.042  9.231   76.918  1.000 40.580  ? 113 LEU HHH O   1 
ATOM 13426 C CB  . LEU H 3 113 ? 89.802  8.787   74.199  1.000 41.340  ? 113 LEU HHH CB  1 
ATOM 13427 C CG  . LEU H 3 113 ? 88.987  10.063  74.043  1.000 40.960  ? 113 LEU HHH CG  1 
ATOM 13428 C CD1 . LEU H 3 113 ? 89.641  11.016  73.041  1.000 42.780  ? 113 LEU HHH CD1 1 
ATOM 13429 C CD2 . LEU H 3 113 ? 87.560  9.736   73.631  1.000 42.550  ? 113 LEU HHH CD2 1 
ATOM 13430 N N   . VAL H 3 114 ? 91.789  11.068  75.759  1.000 45.000  ? 114 VAL HHH N   1 
ATOM 13431 C CA  . VAL H 3 114 ? 91.747  12.067  76.862  1.000 47.040  ? 114 VAL HHH CA  1 
ATOM 13432 C C   . VAL H 3 114 ? 90.747  13.145  76.456  1.000 43.940  ? 114 VAL HHH C   1 
ATOM 13433 O O   . VAL H 3 114 ? 91.052  13.895  75.499  1.000 39.340  ? 114 VAL HHH O   1 
ATOM 13434 C CB  . VAL H 3 114 ? 93.141  12.663  77.137  1.000 55.340  ? 114 VAL HHH CB  1 
ATOM 13435 C CG1 . VAL H 3 114 ? 93.055  13.892  78.035  1.000 60.840  ? 114 VAL HHH CG1 1 
ATOM 13436 C CG2 . VAL H 3 114 ? 94.100  11.627  77.731  1.000 54.750  ? 114 VAL HHH CG2 1 
ATOM 13437 N N   . THR H 3 115 ? 89.605  13.209  77.145  1.000 49.530  ? 115 THR HHH N   1 
ATOM 13438 C CA  . THR H 3 115 ? 88.567  14.248  76.930  1.000 55.490  ? 115 THR HHH CA  1 
ATOM 13439 C C   . THR H 3 115 ? 88.562  15.201  78.126  1.000 59.530  ? 115 THR HHH C   1 
ATOM 13440 O O   . THR H 3 115 ? 88.287  14.729  79.261  1.000 53.310  ? 115 THR HHH O   1 
ATOM 13441 C CB  . THR H 3 115 ? 87.184  13.642  76.699  1.000 54.010  ? 115 THR HHH CB  1 
ATOM 13442 O OG1 . THR H 3 115 ? 87.378  12.420  76.006  1.000 58.910  ? 115 THR HHH OG1 1 
ATOM 13443 C CG2 . THR H 3 115 ? 86.290  14.559  75.898  1.000 54.200  ? 115 THR HHH CG2 1 
ATOM 13444 N N   . VAL H 3 116 ? 88.873  16.478  77.868  1.000 56.640  ? 116 VAL HHH N   1 
ATOM 13445 C CA  . VAL H 3 116 ? 88.896  17.557  78.890  1.000 57.050  ? 116 VAL HHH CA  1 
ATOM 13446 C C   . VAL H 3 116 ? 87.711  18.485  78.631  1.000 60.740  ? 116 VAL HHH C   1 
ATOM 13447 O O   . VAL H 3 116 ? 87.779  19.290  77.682  1.000 63.220  ? 116 VAL HHH O   1 
ATOM 13448 C CB  . VAL H 3 116 ? 90.211  18.336  78.850  1.000 58.400  ? 116 VAL HHH CB  1 
ATOM 13449 C CG1 . VAL H 3 116 ? 90.141  19.575  79.723  1.000 63.720  ? 116 VAL HHH CG1 1 
ATOM 13450 C CG2 . VAL H 3 116 ? 91.398  17.479  79.222  1.000 61.030  ? 116 VAL HHH CG2 1 
ATOM 13451 N N   . SER H 3 117 ? 86.685  18.396  79.479  1.000 66.540  ? 117 SER HHH N   1 
ATOM 13452 C CA  . SER H 3 117 ? 85.408  19.140  79.332  1.000 67.930  ? 117 SER HHH CA  1 
ATOM 13453 C C   . SER H 3 117 ? 84.986  19.612  80.718  1.000 68.960  ? 117 SER HHH C   1 
ATOM 13454 O O   . SER H 3 117 ? 85.281  18.857  81.725  1.000 63.040  ? 117 SER HHH O   1 
ATOM 13455 C CB  . SER H 3 117 ? 84.372  18.293  78.651  1.000 69.730  ? 117 SER HHH CB  1 
ATOM 13456 O OG  . SER H 3 117 ? 83.136  18.980  78.480  1.000 70.010  ? 117 SER HHH OG  1 
ATOM 13457 N N   . SER H 3 118 ? 84.435  20.835  80.765  1.000 69.380  ? 118 SER HHH N   1 
ATOM 13458 C CA  . SER H 3 118 ? 83.844  21.459  81.979  1.000 70.770  ? 118 SER HHH CA  1 
ATOM 13459 C C   . SER H 3 118 ? 82.509  20.764  82.257  1.000 73.860  ? 118 SER HHH C   1 
ATOM 13460 O O   . SER H 3 118 ? 82.144  20.592  83.443  1.000 72.420  ? 118 SER HHH O   1 
ATOM 13461 C CB  . SER H 3 118 ? 83.641  22.949  81.802  1.000 68.050  ? 118 SER HHH CB  1 
ATOM 13462 O OG  . SER H 3 118 ? 84.873  23.646  81.787  1.000 70.150  ? 118 SER HHH OG  1 
ATOM 13463 N N   . ALA H 3 119 ? 81.823  20.399  81.167  1.000 78.200  ? 119 ALA HHH N   1 
ATOM 13464 C CA  . ALA H 3 119 ? 80.424  19.924  81.128  1.000 78.640  ? 119 ALA HHH CA  1 
ATOM 13465 C C   . ALA H 3 119 ? 80.249  18.753  82.097  1.000 76.570  ? 119 ALA HHH C   1 
ATOM 13466 O O   . ALA H 3 119 ? 81.133  17.879  82.142  1.000 60.630  ? 119 ALA HHH O   1 
ATOM 13467 C CB  . ALA H 3 119 ? 80.074  19.542  79.716  1.000 80.180  ? 119 ALA HHH CB  1 
ATOM 13468 N N   . SER H 3 120 ? 79.149  18.776  82.865  1.000 82.650  ? 120 SER HHH N   1 
ATOM 13469 C CA  . SER H 3 120 ? 78.629  17.656  83.689  1.000 86.400  ? 120 SER HHH CA  1 
ATOM 13470 C C   . SER H 3 120 ? 77.402  17.076  82.981  1.000 90.800  ? 120 SER HHH C   1 
ATOM 13471 O O   . SER H 3 120 ? 76.897  17.737  82.039  1.000 89.310  ? 120 SER HHH O   1 
ATOM 13472 C CB  . SER H 3 120 ? 78.311  18.123  85.080  1.000 85.930  ? 120 SER HHH CB  1 
ATOM 13473 O OG  . SER H 3 120 ? 79.459  18.725  85.651  1.000 86.290  ? 120 SER HHH OG  1 
ATOM 13474 N N   . THR H 3 121 ? 76.907  15.919  83.450  1.000 88.890  ? 121 THR HHH N   1 
ATOM 13475 C CA  . THR H 3 121 ? 76.011  15.004  82.691  1.000 87.010  ? 121 THR HHH CA  1 
ATOM 13476 C C   . THR H 3 121 ? 74.554  15.503  82.757  1.000 86.330  ? 121 THR HHH C   1 
ATOM 13477 O O   . THR H 3 121 ? 73.784  14.928  83.503  1.000 93.740  ? 121 THR HHH O   1 
ATOM 13478 C CB  . THR H 3 121 ? 76.247  13.560  83.168  1.000 84.550  ? 121 THR HHH CB  1 
ATOM 13479 O OG1 . THR H 3 121 ? 75.928  13.486  84.555  1.000 68.600  ? 121 THR HHH OG1 1 
ATOM 13480 C CG2 . THR H 3 121 ? 77.681  13.100  82.994  1.000 83.060  ? 121 THR HHH CG2 1 
ATOM 13481 N N   . LYS H 3 122 ? 74.187  16.517  81.961  1.000 90.410  ? 122 LYS HHH N   1 
ATOM 13482 C CA  . LYS H 3 122 ? 72.792  17.001  81.760  1.000 85.720  ? 122 LYS HHH CA  1 
ATOM 13483 C C   . LYS H 3 122 ? 72.023  15.958  80.932  1.000 86.140  ? 122 LYS HHH C   1 
ATOM 13484 O O   . LYS H 3 122 ? 72.606  15.338  79.985  1.000 87.150  ? 122 LYS HHH O   1 
ATOM 13485 C CB  . LYS H 3 122 ? 72.745  18.377  81.072  1.000 74.930  ? 122 LYS HHH CB  1 
ATOM 13486 N N   . GLY H 3 123 ? 70.735  15.804  81.242  1.000 83.740  ? 123 GLY HHH N   1 
ATOM 13487 C CA  . GLY H 3 123 ? 69.745  15.125  80.388  1.000 82.170  ? 123 GLY HHH CA  1 
ATOM 13488 C C   . GLY H 3 123 ? 69.342  16.016  79.212  1.000 85.780  ? 123 GLY HHH C   1 
ATOM 13489 O O   . GLY H 3 123 ? 69.537  17.235  79.246  1.000 79.870  ? 123 GLY HHH O   1 
ATOM 13490 N N   . PRO H 3 124 ? 68.797  15.427  78.122  1.000 90.470  ? 124 PRO HHH N   1 
ATOM 13491 C CA  . PRO H 3 124 ? 68.387  16.192  76.942  1.000 97.500  ? 124 PRO HHH CA  1 
ATOM 13492 C C   . PRO H 3 124 ? 67.015  16.815  77.236  1.000 109.440 ? 124 PRO HHH C   1 
ATOM 13493 O O   . PRO H 3 124 ? 66.460  16.535  78.276  1.000 121.920 ? 124 PRO HHH O   1 
ATOM 13494 C CB  . PRO H 3 124 ? 68.246  15.110  75.859  1.000 94.540  ? 124 PRO HHH CB  1 
ATOM 13495 C CG  . PRO H 3 124 ? 67.841  13.868  76.630  1.000 85.780  ? 124 PRO HHH CG  1 
ATOM 13496 C CD  . PRO H 3 124 ? 68.553  13.983  77.961  1.000 88.410  ? 124 PRO HHH CD  1 
ATOM 13497 N N   . SER H 3 125 ? 66.510  17.633  76.309  1.000 117.050 ? 125 SER HHH N   1 
ATOM 13498 C CA  . SER H 3 125 ? 65.194  18.310  76.303  1.000 113.730 ? 125 SER HHH CA  1 
ATOM 13499 C C   . SER H 3 125 ? 64.724  18.444  74.862  1.000 122.510 ? 125 SER HHH C   1 
ATOM 13500 O O   . SER H 3 125 ? 65.608  18.699  74.013  1.000 143.040 ? 125 SER HHH O   1 
ATOM 13501 C CB  . SER H 3 125 ? 65.250  19.643  77.046  1.000 102.320 ? 125 SER HHH CB  1 
ATOM 13502 O OG  . SER H 3 125 ? 66.103  20.544  76.370  1.000 100.520 ? 125 SER HHH OG  1 
ATOM 13503 N N   . VAL H 3 126 ? 63.425  18.289  74.557  1.000 118.590 ? 126 VAL HHH N   1 
ATOM 13504 C CA  . VAL H 3 126 ? 62.825  18.741  73.258  1.000 98.850  ? 126 VAL HHH CA  1 
ATOM 13505 C C   . VAL H 3 126 ? 62.200  20.134  73.413  1.000 85.940  ? 126 VAL HHH C   1 
ATOM 13506 O O   . VAL H 3 126 ? 62.272  20.904  72.439  1.000 75.880  ? 126 VAL HHH O   1 
ATOM 13507 C CB  . VAL H 3 126 ? 61.770  17.701  72.841  1.000 88.690  ? 126 VAL HHH CB  1 
ATOM 13508 C CG1 . VAL H 3 126 ? 62.413  16.398  72.389  1.000 80.860  ? 126 VAL HHH CG1 1 
ATOM 13509 C CG2 . VAL H 3 126 ? 60.750  17.447  73.941  1.000 87.430  ? 126 VAL HHH CG2 1 
ATOM 13510 N N   . VAL H 3 147 ? 68.922  15.908  72.523  1.000 90.540  ? 152 VAL HHH N   1 
ATOM 13511 C CA  . VAL H 3 147 ? 68.282  16.770  71.488  1.000 102.300 ? 152 VAL HHH CA  1 
ATOM 13512 C C   . VAL H 3 147 ? 68.734  18.217  71.705  1.000 109.570 ? 152 VAL HHH C   1 
ATOM 13513 O O   . VAL H 3 147 ? 68.639  19.011  70.752  1.000 124.890 ? 152 VAL HHH O   1 
ATOM 13514 C CB  . VAL H 3 147 ? 66.748  16.639  71.528  1.000 98.360  ? 152 VAL HHH CB  1 
ATOM 13515 C CG1 . VAL H 3 147 ? 66.144  16.527  70.138  1.000 83.310  ? 152 VAL HHH CG1 1 
ATOM 13516 C CG2 . VAL H 3 147 ? 66.309  15.477  72.402  1.000 97.050  ? 152 VAL HHH CG2 1 
ATOM 13517 N N   . LYS H 3 148 ? 69.216  18.539  72.907  1.000 111.960 ? 153 LYS HHH N   1 
ATOM 13518 C CA  . LYS H 3 148 ? 69.621  19.936  73.210  1.000 105.710 ? 153 LYS HHH CA  1 
ATOM 13519 C C   . LYS H 3 148 ? 70.888  19.954  74.070  1.000 111.570 ? 153 LYS HHH C   1 
ATOM 13520 O O   . LYS H 3 148 ? 71.747  20.825  73.840  1.000 108.880 ? 153 LYS HHH O   1 
ATOM 13521 C CB  . LYS H 3 148 ? 68.491  20.660  73.938  1.000 91.650  ? 153 LYS HHH CB  1 
ATOM 13522 N N   . ASP H 3 149 ? 70.969  19.051  75.048  1.000 104.910 ? 154 ASP HHH N   1 
ATOM 13523 C CA  . ASP H 3 149 ? 72.139  19.019  75.960  1.000 99.680  ? 154 ASP HHH CA  1 
ATOM 13524 C C   . ASP H 3 149 ? 72.355  17.586  76.429  1.000 94.700  ? 154 ASP HHH C   1 
ATOM 13525 O O   . ASP H 3 149 ? 71.945  17.287  77.551  1.000 80.810  ? 154 ASP HHH O   1 
ATOM 13526 C CB  . ASP H 3 149 ? 71.917  19.883  77.200  1.000 96.600  ? 154 ASP HHH CB  1 
ATOM 13527 C CG  . ASP H 3 149 ? 70.542  20.518  77.288  1.000 96.150  ? 154 ASP HHH CG  1 
ATOM 13528 O OD1 . ASP H 3 149 ? 69.582  19.798  77.626  1.000 92.200  ? 154 ASP HHH OD1 1 
ATOM 13529 O OD2 . ASP H 3 149 ? 70.445  21.730  77.013  1.000 103.020 ? 154 ASP HHH OD2 1 
ATOM 13530 N N   . TYR H 3 150 ? 73.001  16.744  75.624  1.000 99.270  ? 155 TYR HHH N   1 
ATOM 13531 C CA  . TYR H 3 150 ? 73.111  15.317  76.022  1.000 109.630 ? 155 TYR HHH CA  1 
ATOM 13532 C C   . TYR H 3 150 ? 74.535  14.949  76.454  1.000 107.420 ? 155 TYR HHH C   1 
ATOM 13533 O O   . TYR H 3 150 ? 75.449  15.758  76.220  1.000 98.180  ? 155 TYR HHH O   1 
ATOM 13534 C CB  . TYR H 3 150 ? 72.426  14.420  74.982  1.000 118.920 ? 155 TYR HHH CB  1 
ATOM 13535 C CG  . TYR H 3 150 ? 73.260  13.790  73.887  1.000 114.390 ? 155 TYR HHH CG  1 
ATOM 13536 C CD1 . TYR H 3 150 ? 74.121  12.739  74.143  1.000 108.480 ? 155 TYR HHH CD1 1 
ATOM 13537 C CD2 . TYR H 3 150 ? 73.098  14.172  72.567  1.000 116.730 ? 155 TYR HHH CD2 1 
ATOM 13538 C CE1 . TYR H 3 150 ? 74.868  12.142  73.146  1.000 109.580 ? 155 TYR HHH CE1 1 
ATOM 13539 C CE2 . TYR H 3 150 ? 73.825  13.574  71.552  1.000 109.750 ? 155 TYR HHH CE2 1 
ATOM 13540 C CZ  . TYR H 3 150 ? 74.711  12.552  71.839  1.000 113.380 ? 155 TYR HHH CZ  1 
ATOM 13541 O OH  . TYR H 3 150 ? 75.439  11.942  70.859  1.000 116.580 ? 155 TYR HHH OH  1 
ATOM 13542 N N   . PHE H 3 151 ? 74.700  13.782  77.097  1.000 111.520 ? 156 PHE HHH N   1 
ATOM 13543 C CA  . PHE H 3 151 ? 76.051  13.275  77.455  1.000 117.420 ? 156 PHE HHH CA  1 
ATOM 13544 C C   . PHE H 3 151 ? 76.292  11.914  76.793  1.000 119.100 ? 156 PHE HHH C   1 
ATOM 13545 O O   . PHE H 3 151 ? 75.394  11.066  76.875  1.000 105.410 ? 156 PHE HHH O   1 
ATOM 13546 C CB  . PHE H 3 151 ? 76.297  13.324  78.962  1.000 110.670 ? 156 PHE HHH CB  1 
ATOM 13547 C CG  . PHE H 3 151 ? 77.468  14.214  79.276  1.000 105.030 ? 156 PHE HHH CG  1 
ATOM 13548 C CD1 . PHE H 3 151 ? 77.372  15.583  79.104  1.000 103.000 ? 156 PHE HHH CD1 1 
ATOM 13549 C CD2 . PHE H 3 151 ? 78.688  13.680  79.654  1.000 103.700 ? 156 PHE HHH CD2 1 
ATOM 13550 C CE1 . PHE H 3 151 ? 78.458  16.402  79.353  1.000 104.500 ? 156 PHE HHH CE1 1 
ATOM 13551 C CE2 . PHE H 3 151 ? 79.773  14.502  79.907  1.000 113.260 ? 156 PHE HHH CE2 1 
ATOM 13552 C CZ  . PHE H 3 151 ? 79.655  15.861  79.755  1.000 111.720 ? 156 PHE HHH CZ  1 
ATOM 13553 N N   . PRO H 3 152 ? 77.467  11.659  76.175  1.000 136.020 ? 157 PRO HHH N   1 
ATOM 13554 C CA  . PRO H 3 152 ? 77.797  10.427  75.426  1.000 142.630 ? 157 PRO HHH CA  1 
ATOM 13555 C C   . PRO H 3 152 ? 76.881  9.200   75.328  1.000 141.980 ? 157 PRO HHH C   1 
ATOM 13556 O O   . PRO H 3 152 ? 77.310  8.173   75.821  1.000 130.380 ? 157 PRO HHH O   1 
ATOM 13557 C CB  . PRO H 3 152 ? 79.120  10.077  76.121  1.000 145.740 ? 157 PRO HHH CB  1 
ATOM 13558 C CG  . PRO H 3 152 ? 79.783  11.433  76.332  1.000 143.390 ? 157 PRO HHH CG  1 
ATOM 13559 C CD  . PRO H 3 152 ? 78.679  12.470  76.230  1.000 142.830 ? 157 PRO HHH CD  1 
ATOM 13560 N N   . GLU H 3 153 ? 75.757  9.310   74.622  1.000 142.170 ? 158 GLU HHH N   1 
ATOM 13561 C CA  . GLU H 3 153 ? 74.767  8.214   74.431  1.000 129.460 ? 158 GLU HHH CA  1 
ATOM 13562 C C   . GLU H 3 153 ? 73.509  8.904   73.914  1.000 130.280 ? 158 GLU HHH C   1 
ATOM 13563 O O   . GLU H 3 153 ? 72.972  9.749   74.651  1.000 127.840 ? 158 GLU HHH O   1 
ATOM 13564 C CB  . GLU H 3 153 ? 74.387  7.511   75.737  1.000 121.490 ? 158 GLU HHH CB  1 
ATOM 13565 C CG  . GLU H 3 153 ? 73.158  6.624   75.634  1.000 126.040 ? 158 GLU HHH CG  1 
ATOM 13566 C CD  . GLU H 3 153 ? 73.452  5.145   75.469  1.000 129.870 ? 158 GLU HHH CD  1 
ATOM 13567 O OE1 . GLU H 3 153 ? 74.254  4.614   76.263  1.000 127.800 ? 158 GLU HHH OE1 1 
ATOM 13568 O OE2 . GLU H 3 153 ? 72.883  4.528   74.549  1.000 129.070 ? 158 GLU HHH OE2 1 
ATOM 13569 N N   . PRO H 3 154 ? 73.033  8.624   72.688  1.000 116.640 ? 159 PRO HHH N   1 
ATOM 13570 C CA  . PRO H 3 154 ? 71.890  9.334   72.121  1.000 99.590  ? 159 PRO HHH CA  1 
ATOM 13571 C C   . PRO H 3 154 ? 70.841  9.788   73.141  1.000 88.860  ? 159 PRO HHH C   1 
ATOM 13572 O O   . PRO H 3 154 ? 70.042  10.620  72.765  1.000 69.080  ? 159 PRO HHH O   1 
ATOM 13573 C CB  . PRO H 3 154 ? 71.279  8.238   71.250  1.000 101.890 ? 159 PRO HHH CB  1 
ATOM 13574 C CG  . PRO H 3 154 ? 72.484  7.502   70.702  1.000 108.610 ? 159 PRO HHH CG  1 
ATOM 13575 C CD  . PRO H 3 154 ? 73.543  7.594   71.784  1.000 111.600 ? 159 PRO HHH CD  1 
ATOM 13576 N N   . THR H 3 170 ? 68.646  10.189  64.350  1.000 101.190 ? 175 THR HHH N   1 
ATOM 13577 C CA  . THR H 3 170 ? 69.377  9.485   63.265  1.000 112.590 ? 175 THR HHH CA  1 
ATOM 13578 C C   . THR H 3 170 ? 70.592  10.317  62.834  1.000 112.380 ? 175 THR HHH C   1 
ATOM 13579 O O   . THR H 3 170 ? 71.643  9.720   62.537  1.000 109.160 ? 175 THR HHH O   1 
ATOM 13580 C CB  . THR H 3 170 ? 68.480  9.277   62.049  1.000 118.980 ? 175 THR HHH CB  1 
ATOM 13581 O OG1 . THR H 3 170 ? 67.149  9.598   62.450  1.000 140.870 ? 175 THR HHH OG1 1 
ATOM 13582 C CG2 . THR H 3 170 ? 68.534  7.864   61.510  1.000 108.130 ? 175 THR HHH CG2 1 
ATOM 13583 N N   . PHE H 3 171 ? 70.443  11.639  62.797  1.000 112.380 ? 176 PHE HHH N   1 
ATOM 13584 C CA  . PHE H 3 171 ? 71.551  12.485  62.288  1.000 127.740 ? 176 PHE HHH CA  1 
ATOM 13585 C C   . PHE H 3 171 ? 72.606  12.622  63.372  1.000 138.860 ? 176 PHE HHH C   1 
ATOM 13586 O O   . PHE H 3 171 ? 72.231  12.745  64.542  1.000 140.420 ? 176 PHE HHH O   1 
ATOM 13587 C CB  . PHE H 3 171 ? 71.020  13.798  61.716  1.000 126.230 ? 176 PHE HHH CB  1 
ATOM 13588 C CG  . PHE H 3 171 ? 70.706  13.697  60.248  1.000 134.760 ? 176 PHE HHH CG  1 
ATOM 13589 C CD1 . PHE H 3 171 ? 69.718  12.838  59.794  1.000 135.690 ? 176 PHE HHH CD1 1 
ATOM 13590 C CD2 . PHE H 3 171 ? 71.420  14.429  59.317  1.000 130.630 ? 176 PHE HHH CD2 1 
ATOM 13591 C CE1 . PHE H 3 171 ? 69.433  12.733  58.443  1.000 130.490 ? 176 PHE HHH CE1 1 
ATOM 13592 C CE2 . PHE H 3 171 ? 71.129  14.328  57.967  1.000 130.830 ? 176 PHE HHH CE2 1 
ATOM 13593 C CZ  . PHE H 3 171 ? 70.141  13.479  57.533  1.000 130.720 ? 176 PHE HHH CZ  1 
ATOM 13594 N N   . PRO H 3 172 ? 73.923  12.606  63.031  1.000 145.960 ? 177 PRO HHH N   1 
ATOM 13595 C CA  . PRO H 3 172 ? 74.978  12.625  64.039  1.000 133.820 ? 177 PRO HHH CA  1 
ATOM 13596 C C   . PRO H 3 172 ? 74.939  13.840  64.978  1.000 125.340 ? 177 PRO HHH C   1 
ATOM 13597 O O   . PRO H 3 172 ? 74.435  14.876  64.576  1.000 138.020 ? 177 PRO HHH O   1 
ATOM 13598 C CB  . PRO H 3 172 ? 76.250  12.687  63.183  1.000 140.150 ? 177 PRO HHH CB  1 
ATOM 13599 C CG  . PRO H 3 172 ? 75.801  13.226  61.849  1.000 141.830 ? 177 PRO HHH CG  1 
ATOM 13600 C CD  . PRO H 3 172 ? 74.443  12.589  61.664  1.000 145.490 ? 177 PRO HHH CD  1 
ATOM 13601 N N   . ALA H 3 173 ? 75.499  13.700  66.185  1.000 93.170  ? 178 ALA HHH N   1 
ATOM 13602 C CA  . ALA H 3 173 ? 75.442  14.818  67.158  1.000 88.490  ? 178 ALA HHH CA  1 
ATOM 13603 C C   . ALA H 3 173 ? 76.412  15.938  66.767  1.000 89.900  ? 178 ALA HHH C   1 
ATOM 13604 O O   . ALA H 3 173 ? 77.276  15.703  65.910  1.000 94.620  ? 178 ALA HHH O   1 
ATOM 13605 C CB  . ALA H 3 173 ? 75.721  14.320  68.550  1.000 84.520  ? 178 ALA HHH CB  1 
ATOM 13606 N N   . VAL H 3 174 ? 76.229  17.127  67.345  1.000 98.620  ? 179 VAL HHH N   1 
ATOM 13607 C CA  . VAL H 3 174 ? 77.159  18.288  67.210  1.000 107.160 ? 179 VAL HHH CA  1 
ATOM 13608 C C   . VAL H 3 174 ? 77.615  18.647  68.623  1.000 104.770 ? 179 VAL HHH C   1 
ATOM 13609 O O   . VAL H 3 174 ? 76.762  18.626  69.523  1.000 105.090 ? 179 VAL HHH O   1 
ATOM 13610 C CB  . VAL H 3 174 ? 76.503  19.496  66.501  1.000 116.460 ? 179 VAL HHH CB  1 
ATOM 13611 C CG1 . VAL H 3 174 ? 75.522  20.231  67.397  1.000 120.110 ? 179 VAL HHH CG1 1 
ATOM 13612 C CG2 . VAL H 3 174 ? 77.528  20.467  65.934  1.000 117.810 ? 179 VAL HHH CG2 1 
ATOM 13613 N N   . LEU H 3 175 ? 78.905  18.922  68.813  1.000 99.530  ? 180 LEU HHH N   1 
ATOM 13614 C CA  . LEU H 3 175 ? 79.453  19.385  70.117  1.000 93.100  ? 180 LEU HHH CA  1 
ATOM 13615 C C   . LEU H 3 175 ? 79.433  20.913  70.127  1.000 90.000  ? 180 LEU HHH C   1 
ATOM 13616 O O   . LEU H 3 175 ? 80.326  21.511  69.523  1.000 91.140  ? 180 LEU HHH O   1 
ATOM 13617 C CB  . LEU H 3 175 ? 80.861  18.822  70.357  1.000 91.260  ? 180 LEU HHH CB  1 
ATOM 13618 C CG  . LEU H 3 175 ? 81.260  18.718  71.832  1.000 86.000  ? 180 LEU HHH CG  1 
ATOM 13619 C CD1 . LEU H 3 175 ? 82.055  17.443  72.109  1.000 81.310  ? 180 LEU HHH CD1 1 
ATOM 13620 C CD2 . LEU H 3 175 ? 82.030  19.951  72.284  1.000 85.230  ? 180 LEU HHH CD2 1 
ATOM 13621 N N   . GLN H 3 176 ? 78.407  21.510  70.750  1.000 96.730  ? 181 GLN HHH N   1 
ATOM 13622 C CA  . GLN H 3 176 ? 78.329  22.972  71.036  1.000 97.890  ? 181 GLN HHH CA  1 
ATOM 13623 C C   . GLN H 3 176 ? 79.530  23.379  71.917  1.000 92.230  ? 181 GLN HHH C   1 
ATOM 13624 O O   . GLN H 3 176 ? 80.062  22.512  72.626  1.000 92.790  ? 181 GLN HHH O   1 
ATOM 13625 C CB  . GLN H 3 176 ? 76.955  23.314  71.636  1.000 87.500  ? 181 GLN HHH CB  1 
ATOM 13626 N N   . SER H 3 177 ? 79.964  24.644  71.854  1.000 86.930  ? 182 SER HHH N   1 
ATOM 13627 C CA  . SER H 3 177 ? 81.054  25.232  72.688  1.000 76.640  ? 182 SER HHH CA  1 
ATOM 13628 C C   . SER H 3 177 ? 80.732  25.103  74.183  1.000 74.540  ? 182 SER HHH C   1 
ATOM 13629 O O   . SER H 3 177 ? 81.664  25.136  74.981  1.000 72.320  ? 182 SER HHH O   1 
ATOM 13630 C CB  . SER H 3 177 ? 81.314  26.676  72.342  1.000 70.230  ? 182 SER HHH CB  1 
ATOM 13631 O OG  . SER H 3 177 ? 81.586  26.820  70.961  1.000 72.260  ? 182 SER HHH OG  1 
ATOM 13632 N N   . SER H 3 178 ? 79.447  24.967  74.541  1.000 80.150  ? 183 SER HHH N   1 
ATOM 13633 C CA  . SER H 3 178 ? 78.940  24.724  75.924  1.000 87.050  ? 183 SER HHH CA  1 
ATOM 13634 C C   . SER H 3 178 ? 79.489  23.398  76.482  1.000 89.940  ? 183 SER HHH C   1 
ATOM 13635 O O   . SER H 3 178 ? 79.467  23.214  77.724  1.000 74.780  ? 183 SER HHH O   1 
ATOM 13636 C CB  . SER H 3 178 ? 77.423  24.760  75.956  1.000 91.220  ? 183 SER HHH CB  1 
ATOM 13637 O OG  . SER H 3 178 ? 76.863  24.025  74.877  1.000 87.860  ? 183 SER HHH OG  1 
ATOM 13638 N N   . GLY H 3 179 ? 79.960  22.504  75.607  1.000 93.750  ? 184 GLY HHH N   1 
ATOM 13639 C CA  . GLY H 3 179 ? 80.436  21.155  75.970  1.000 93.600  ? 184 GLY HHH CA  1 
ATOM 13640 C C   . GLY H 3 179 ? 79.295  20.153  75.955  1.000 93.110  ? 184 GLY HHH C   1 
ATOM 13641 O O   . GLY H 3 179 ? 79.541  18.973  76.304  1.000 89.100  ? 184 GLY HHH O   1 
ATOM 13642 N N   . LEU H 3 180 ? 78.090  20.602  75.565  1.000 91.360  ? 185 LEU HHH N   1 
ATOM 13643 C CA  . LEU H 3 180 ? 76.848  19.785  75.493  1.000 91.030  ? 185 LEU HHH CA  1 
ATOM 13644 C C   . LEU H 3 180 ? 76.572  19.464  74.023  1.000 87.390  ? 185 LEU HHH C   1 
ATOM 13645 O O   . LEU H 3 180 ? 76.721  20.382  73.177  1.000 83.420  ? 185 LEU HHH O   1 
ATOM 13646 C CB  . LEU H 3 180 ? 75.681  20.560  76.120  1.000 98.880  ? 185 LEU HHH CB  1 
ATOM 13647 C CG  . LEU H 3 180 ? 75.631  20.657  77.649  1.000 104.450 ? 185 LEU HHH CG  1 
ATOM 13648 C CD1 . LEU H 3 180 ? 75.714  19.290  78.317  1.000 106.280 ? 185 LEU HHH CD1 1 
ATOM 13649 C CD2 . LEU H 3 180 ? 76.723  21.557  78.188  1.000 106.530 ? 185 LEU HHH CD2 1 
ATOM 13650 N N   . TYR H 3 181 ? 76.140  18.227  73.757  1.000 95.720  ? 186 TYR HHH N   1 
ATOM 13651 C CA  . TYR H 3 181 ? 75.823  17.692  72.403  1.000 102.180 ? 186 TYR HHH CA  1 
ATOM 13652 C C   . TYR H 3 181 ? 74.371  18.044  72.047  1.000 97.820  ? 186 TYR HHH C   1 
ATOM 13653 O O   . TYR H 3 181 ? 73.562  18.295  72.927  1.000 95.330  ? 186 TYR HHH O   1 
ATOM 13654 C CB  . TYR H 3 181 ? 76.052  16.171  72.332  1.000 106.820 ? 186 TYR HHH CB  1 
ATOM 13655 C CG  . TYR H 3 181 ? 77.478  15.716  72.547  1.000 101.590 ? 186 TYR HHH CG  1 
ATOM 13656 C CD1 . TYR H 3 181 ? 78.060  15.735  73.807  1.000 95.790  ? 186 TYR HHH CD1 1 
ATOM 13657 C CD2 . TYR H 3 181 ? 78.244  15.237  71.492  1.000 92.760  ? 186 TYR HHH CD2 1 
ATOM 13658 C CE1 . TYR H 3 181 ? 79.364  15.314  74.010  1.000 87.560  ? 186 TYR HHH CE1 1 
ATOM 13659 C CE2 . TYR H 3 181 ? 79.545  14.799  71.682  1.000 88.990  ? 186 TYR HHH CE2 1 
ATOM 13660 C CZ  . TYR H 3 181 ? 80.106  14.838  72.946  1.000 82.490  ? 186 TYR HHH CZ  1 
ATOM 13661 O OH  . TYR H 3 181 ? 81.390  14.436  73.159  1.000 77.320  ? 186 TYR HHH OH  1 
ATOM 13662 N N   . SER H 3 182 ? 74.062  18.072  70.755  1.000 92.310  ? 187 SER HHH N   1 
ATOM 13663 C CA  . SER H 3 182 ? 72.717  18.327  70.175  1.000 90.210  ? 187 SER HHH CA  1 
ATOM 13664 C C   . SER H 3 182 ? 72.576  17.441  68.932  1.000 90.600  ? 187 SER HHH C   1 
ATOM 13665 O O   . SER H 3 182 ? 73.547  17.331  68.171  1.000 96.960  ? 187 SER HHH O   1 
ATOM 13666 C CB  . SER H 3 182 ? 72.551  19.789  69.877  1.000 85.960  ? 187 SER HHH CB  1 
ATOM 13667 O OG  . SER H 3 182 ? 72.566  20.545  71.093  1.000 79.020  ? 187 SER HHH OG  1 
ATOM 13668 N N   . LEU H 3 183 ? 71.430  16.775  68.795  1.000 98.200  ? 188 LEU HHH N   1 
ATOM 13669 C CA  . LEU H 3 183 ? 71.202  15.511  68.031  1.000 102.660 ? 188 LEU HHH CA  1 
ATOM 13670 C C   . LEU H 3 183 ? 69.786  15.586  67.428  1.000 100.430 ? 188 LEU HHH C   1 
ATOM 13671 O O   . LEU H 3 183 ? 68.887  16.143  68.104  1.000 107.480 ? 188 LEU HHH O   1 
ATOM 13672 C CB  . LEU H 3 183 ? 71.393  14.362  69.043  1.000 108.210 ? 188 LEU HHH CB  1 
ATOM 13673 C CG  . LEU H 3 183 ? 71.220  12.911  68.578  1.000 111.210 ? 188 LEU HHH CG  1 
ATOM 13674 C CD1 . LEU H 3 183 ? 72.398  12.462  67.724  1.000 119.250 ? 188 LEU HHH CD1 1 
ATOM 13675 C CD2 . LEU H 3 183 ? 71.081  11.956  69.770  1.000 102.200 ? 188 LEU HHH CD2 1 
ATOM 13676 N N   . SER H 3 184 ? 69.585  15.123  66.185  1.000 107.330 ? 189 SER HHH N   1 
ATOM 13677 C CA  . SER H 3 184 ? 68.324  15.292  65.399  1.000 100.000 ? 189 SER HHH CA  1 
ATOM 13678 C C   . SER H 3 184 ? 67.787  13.943  64.869  1.000 92.510  ? 189 SER HHH C   1 
ATOM 13679 O O   . SER H 3 184 ? 68.390  13.016  64.291  1.000 92.410  ? 189 SER HHH O   1 
ATOM 13680 C CB  . SER H 3 184 ? 68.516  16.314  64.290  1.000 95.270  ? 189 SER HHH CB  1 
ATOM 13681 O OG  . SER H 3 184 ? 69.082  17.514  64.806  1.000 88.860  ? 189 SER HHH OG  1 
ATOM 13682 N N   . SER I 2 2   ? 121.756 29.097  15.314  1.000 75.470  ? 2   SER III N   1 
ATOM 13683 C CA  . SER I 2 2   ? 121.611 30.276  16.243  1.000 82.040  ? 2   SER III CA  1 
ATOM 13684 C C   . SER I 2 2   ? 120.193 30.402  16.851  1.000 91.730  ? 2   SER III C   1 
ATOM 13685 O O   . SER I 2 2   ? 120.061 31.145  17.845  1.000 107.980 ? 2   SER III O   1 
ATOM 13686 C CB  . SER I 2 2   ? 122.009 31.553  15.535  1.000 72.910  ? 2   SER III CB  1 
ATOM 13687 O OG  . SER I 2 2   ? 123.378 31.832  15.750  1.000 63.170  ? 2   SER III OG  1 
ATOM 13688 N N   . VAL I 2 3   ? 119.149 29.788  16.262  1.000 81.550  ? 3   VAL III N   1 
ATOM 13689 C CA  . VAL I 2 3   ? 117.758 29.727  16.808  1.000 73.330  ? 3   VAL III CA  1 
ATOM 13690 C C   . VAL I 2 3   ? 117.388 28.253  17.007  1.000 62.300  ? 3   VAL III C   1 
ATOM 13691 O O   . VAL I 2 3   ? 117.852 27.381  16.278  1.000 49.690  ? 3   VAL III O   1 
ATOM 13692 C CB  . VAL I 2 3   ? 116.740 30.447  15.888  1.000 87.330  ? 3   VAL III CB  1 
ATOM 13693 C CG1 . VAL I 2 3   ? 115.315 30.481  16.437  1.000 84.910  ? 3   VAL III CG1 1 
ATOM 13694 C CG2 . VAL I 2 3   ? 117.181 31.867  15.579  1.000 88.640  ? 3   VAL III CG2 1 
ATOM 13695 N N   . LEU I 2 4   ? 116.546 27.979  17.996  1.000 62.980  ? 4   LEU III N   1 
ATOM 13696 C CA  . LEU I 2 4   ? 116.044 26.614  18.269  1.000 61.670  ? 4   LEU III CA  1 
ATOM 13697 C C   . LEU I 2 4   ? 114.758 26.412  17.466  1.000 63.200  ? 4   LEU III C   1 
ATOM 13698 O O   . LEU I 2 4   ? 113.857 27.291  17.510  1.000 57.510  ? 4   LEU III O   1 
ATOM 13699 C CB  . LEU I 2 4   ? 115.817 26.464  19.777  1.000 58.870  ? 4   LEU III CB  1 
ATOM 13700 C CG  . LEU I 2 4   ? 117.059 26.673  20.643  1.000 54.950  ? 4   LEU III CG  1 
ATOM 13701 C CD1 . LEU I 2 4   ? 116.756 26.338  22.090  1.000 56.870  ? 4   LEU III CD1 1 
ATOM 13702 C CD2 . LEU I 2 4   ? 118.249 25.876  20.113  1.000 57.440  ? 4   LEU III CD2 1 
ATOM 13703 N N   . THR I 2 5   ? 114.722 25.306  16.729  1.000 63.460  ? 5   THR III N   1 
ATOM 13704 C CA  . THR I 2 5   ? 113.595 24.938  15.838  1.000 63.740  ? 5   THR III CA  1 
ATOM 13705 C C   . THR I 2 5   ? 112.801 23.819  16.520  1.000 65.320  ? 5   THR III C   1 
ATOM 13706 O O   . THR I 2 5   ? 113.375 22.719  16.718  1.000 59.470  ? 5   THR III O   1 
ATOM 13707 C CB  . THR I 2 5   ? 114.136 24.563  14.454  1.000 62.830  ? 5   THR III CB  1 
ATOM 13708 O OG1 . THR I 2 5   ? 115.185 25.480  14.151  1.000 69.510  ? 5   THR III OG1 1 
ATOM 13709 C CG2 . THR I 2 5   ? 113.082 24.597  13.372  1.000 62.880  ? 5   THR III CG2 1 
ATOM 13710 N N   . GLN I 2 6   ? 111.550 24.101  16.912  1.000 64.480  ? 6   GLN III N   1 
ATOM 13711 C CA  . GLN I 2 6   ? 110.583 23.067  17.386  1.000 63.810  ? 6   GLN III CA  1 
ATOM 13712 C C   . GLN I 2 6   ? 109.289 23.167  16.589  1.000 67.010  ? 6   GLN III C   1 
ATOM 13713 O O   . GLN I 2 6   ? 108.899 24.239  16.119  1.000 61.080  ? 6   GLN III O   1 
ATOM 13714 C CB  . GLN I 2 6   ? 110.409 23.171  18.900  1.000 58.700  ? 6   GLN III CB  1 
ATOM 13715 C CG  . GLN I 2 6   ? 109.583 24.366  19.365  1.000 60.710  ? 6   GLN III CG  1 
ATOM 13716 C CD  . GLN I 2 6   ? 109.719 24.588  20.856  1.000 63.640  ? 6   GLN III CD  1 
ATOM 13717 O OE1 . GLN I 2 6   ? 110.782 24.978  21.343  1.000 65.500  ? 6   GLN III OE1 1 
ATOM 13718 N NE2 . GLN I 2 6   ? 108.643 24.329  21.590  1.000 58.070  ? 6   GLN III NE2 1 
ATOM 13719 N N   . PRO I 2 7   ? 108.587 22.030  16.372  1.000 71.810  ? 7   PRO III N   1 
ATOM 13720 C CA  . PRO I 2 7   ? 107.314 22.036  15.652  1.000 80.500  ? 7   PRO III CA  1 
ATOM 13721 C C   . PRO I 2 7   ? 106.334 23.049  16.243  1.000 80.310  ? 7   PRO III C   1 
ATOM 13722 O O   . PRO I 2 7   ? 106.152 23.082  17.458  1.000 81.060  ? 7   PRO III O   1 
ATOM 13723 C CB  . PRO I 2 7   ? 106.803 20.598  15.858  1.000 82.320  ? 7   PRO III CB  1 
ATOM 13724 C CG  . PRO I 2 7   ? 108.058 19.773  16.000  1.000 69.650  ? 7   PRO III CG  1 
ATOM 13725 C CD  . PRO I 2 7   ? 108.983 20.673  16.788  1.000 70.410  ? 7   PRO III CD  1 
ATOM 13726 N N   . PRO I 2 8   ? 105.696 23.925  15.430  1.000 76.190  ? 8   PRO III N   1 
ATOM 13727 C CA  . PRO I 2 8   ? 104.712 24.878  15.949  1.000 73.120  ? 8   PRO III CA  1 
ATOM 13728 C C   . PRO I 2 8   ? 103.521 24.185  16.625  1.000 69.150  ? 8   PRO III C   1 
ATOM 13729 O O   . PRO I 2 8   ? 102.989 24.734  17.566  1.000 61.840  ? 8   PRO III O   1 
ATOM 13730 C CB  . PRO I 2 8   ? 104.261 25.666  14.715  1.000 77.480  ? 8   PRO III CB  1 
ATOM 13731 C CG  . PRO I 2 8   ? 105.405 25.502  13.734  1.000 81.320  ? 8   PRO III CG  1 
ATOM 13732 C CD  . PRO I 2 8   ? 105.931 24.102  13.988  1.000 80.210  ? 8   PRO III CD  1 
ATOM 13733 N N   . SER I 2 9   ? 103.134 23.000  16.150  1.000 72.780  ? 9   SER III N   1 
ATOM 13734 C CA  . SER I 2 9   ? 102.065 22.185  16.781  1.000 79.410  ? 9   SER III CA  1 
ATOM 13735 C C   . SER I 2 9   ? 102.425 20.694  16.780  1.000 75.890  ? 9   SER III C   1 
ATOM 13736 O O   . SER I 2 9   ? 103.264 20.266  15.958  1.000 64.630  ? 9   SER III O   1 
ATOM 13737 C CB  . SER I 2 9   ? 100.736 22.430  16.122  1.000 83.340  ? 9   SER III CB  1 
ATOM 13738 O OG  . SER I 2 9   ? 100.753 21.969  14.786  1.000 94.940  ? 9   SER III OG  1 
ATOM 13739 N N   . ALA I 2 10  ? 101.802 19.961  17.713  1.000 76.590  ? 10  ALA III N   1 
ATOM 13740 C CA  . ALA I 2 10  ? 101.841 18.489  17.855  1.000 71.970  ? 10  ALA III CA  1 
ATOM 13741 C C   . ALA I 2 10  ? 100.543 18.055  18.530  1.000 72.990  ? 10  ALA III C   1 
ATOM 13742 O O   . ALA I 2 10  ? 99.909  18.918  19.188  1.000 76.540  ? 10  ALA III O   1 
ATOM 13743 C CB  . ALA I 2 10  ? 103.033 18.064  18.665  1.000 68.730  ? 10  ALA III CB  1 
ATOM 13744 N N   . SER I 2 11  ? 100.152 16.791  18.350  1.000 71.730  ? 11  SER III N   1 
ATOM 13745 C CA  . SER I 2 11  ? 98.896  16.231  18.919  1.000 74.320  ? 11  SER III CA  1 
ATOM 13746 C C   . SER I 2 11  ? 99.009  14.714  19.102  1.000 73.980  ? 11  SER III C   1 
ATOM 13747 O O   . SER I 2 11  ? 99.979  14.123  18.570  1.000 75.190  ? 11  SER III O   1 
ATOM 13748 C CB  . SER I 2 11  ? 97.731  16.578  18.048  1.000 71.940  ? 11  SER III CB  1 
ATOM 13749 O OG  . SER I 2 11  ? 97.905  15.982  16.774  1.000 77.420  ? 11  SER III OG  1 
ATOM 13750 N N   . GLY I 2 12  ? 98.048  14.129  19.828  1.000 68.250  ? 12  GLY III N   1 
ATOM 13751 C CA  . GLY I 2 12  ? 97.935  12.676  20.080  1.000 74.420  ? 12  GLY III CA  1 
ATOM 13752 C C   . GLY I 2 12  ? 96.594  12.299  20.698  1.000 82.280  ? 12  GLY III C   1 
ATOM 13753 O O   . GLY I 2 12  ? 95.858  13.218  21.129  1.000 88.490  ? 12  GLY III O   1 
ATOM 13754 N N   . THR I 2 13  ? 96.286  10.996  20.729  1.000 85.920  ? 13  THR III N   1 
ATOM 13755 C CA  . THR I 2 13  ? 95.082  10.393  21.367  1.000 86.890  ? 13  THR III CA  1 
ATOM 13756 C C   . THR I 2 13  ? 95.423  10.023  22.812  1.000 80.420  ? 13  THR III C   1 
ATOM 13757 O O   . THR I 2 13  ? 96.512  9.509   23.074  1.000 79.720  ? 13  THR III O   1 
ATOM 13758 C CB  . THR I 2 13  ? 94.557  9.203   20.538  1.000 86.900  ? 13  THR III CB  1 
ATOM 13759 O OG1 . THR I 2 13  ? 93.295  8.810   21.075  1.000 94.450  ? 13  THR III OG1 1 
ATOM 13760 C CG2 . THR I 2 13  ? 95.419  7.964   20.548  1.000 79.410  ? 13  THR III CG2 1 
ATOM 13761 N N   . PRO I 2 14  ? 94.511  10.239  23.792  1.000 74.210  ? 14  PRO III N   1 
ATOM 13762 C CA  . PRO I 2 14  ? 94.791  9.903   25.189  1.000 70.890  ? 14  PRO III CA  1 
ATOM 13763 C C   . PRO I 2 14  ? 95.418  8.506   25.301  1.000 73.140  ? 14  PRO III C   1 
ATOM 13764 O O   . PRO I 2 14  ? 94.948  7.618   24.624  1.000 84.850  ? 14  PRO III O   1 
ATOM 13765 C CB  . PRO I 2 14  ? 93.420  9.985   25.876  1.000 64.190  ? 14  PRO III CB  1 
ATOM 13766 C CG  . PRO I 2 14  ? 92.659  10.998  25.048  1.000 64.810  ? 14  PRO III CG  1 
ATOM 13767 C CD  . PRO I 2 14  ? 93.169  10.814  23.633  1.000 67.300  ? 14  PRO III CD  1 
ATOM 13768 N N   . GLY I 2 15  ? 96.491  8.373   26.089  1.000 74.900  ? 15  GLY III N   1 
ATOM 13769 C CA  . GLY I 2 15  ? 97.195  7.097   26.323  1.000 71.120  ? 15  GLY III CA  1 
ATOM 13770 C C   . GLY I 2 15  ? 98.395  6.928   25.407  1.000 67.600  ? 15  GLY III C   1 
ATOM 13771 O O   . GLY I 2 15  ? 99.261  6.102   25.738  1.000 60.970  ? 15  GLY III O   1 
ATOM 13772 N N   . GLN I 2 16  ? 98.460  7.686   24.304  1.000 67.860  ? 16  GLN III N   1 
ATOM 13773 C CA  . GLN I 2 16  ? 99.579  7.624   23.325  1.000 73.650  ? 16  GLN III CA  1 
ATOM 13774 C C   . GLN I 2 16  ? 100.843 8.264   23.917  1.000 72.620  ? 16  GLN III C   1 
ATOM 13775 O O   . GLN I 2 16  ? 100.759 8.937   24.976  1.000 63.620  ? 16  GLN III O   1 
ATOM 13776 C CB  . GLN I 2 16  ? 99.241  8.345   22.021  1.000 80.060  ? 16  GLN III CB  1 
ATOM 13777 C CG  . GLN I 2 16  ? 98.701  7.436   20.930  1.000 88.800  ? 16  GLN III CG  1 
ATOM 13778 C CD  . GLN I 2 16  ? 98.473  8.184   19.632  1.000 103.570 ? 16  GLN III CD  1 
ATOM 13779 O OE1 . GLN I 2 16  ? 98.129  9.371   19.613  1.000 110.510 ? 16  GLN III OE1 1 
ATOM 13780 N NE2 . GLN I 2 16  ? 98.631  7.486   18.520  1.000 100.070 ? 16  GLN III NE2 1 
ATOM 13781 N N   . ARG I 2 17  ? 101.976 8.013   23.251  1.000 69.020  ? 17  ARG III N   1 
ATOM 13782 C CA  . ARG I 2 17  ? 103.265 8.722   23.445  1.000 71.240  ? 17  ARG III CA  1 
ATOM 13783 C C   . ARG I 2 17  ? 103.412 9.753   22.325  1.000 65.600  ? 17  ARG III C   1 
ATOM 13784 O O   . ARG I 2 17  ? 103.358 9.362   21.163  1.000 66.670  ? 17  ARG III O   1 
ATOM 13785 C CB  . ARG I 2 17  ? 104.434 7.727   23.459  1.000 80.160  ? 17  ARG III CB  1 
ATOM 13786 C CG  . ARG I 2 17  ? 105.803 8.353   23.693  1.000 83.610  ? 17  ARG III CG  1 
ATOM 13787 C CD  . ARG I 2 17  ? 106.703 7.458   24.534  1.000 85.280  ? 17  ARG III CD  1 
ATOM 13788 N NE  . ARG I 2 17  ? 108.093 7.648   24.155  1.000 92.230  ? 17  ARG III NE  1 
ATOM 13789 C CZ  . ARG I 2 17  ? 109.078 6.778   24.367  1.000 103.800 ? 17  ARG III CZ  1 
ATOM 13790 N NH1 . ARG I 2 17  ? 108.836 5.628   24.983  1.000 111.130 ? 17  ARG III NH1 1 
ATOM 13791 N NH2 . ARG I 2 17  ? 110.305 7.066   23.955  1.000 96.930  ? 17  ARG III NH2 1 
ATOM 13792 N N   . VAL I 2 18  ? 103.553 11.029  22.678  1.000 70.100  ? 18  VAL III N   1 
ATOM 13793 C CA  . VAL I 2 18  ? 103.842 12.151  21.738  1.000 75.120  ? 18  VAL III CA  1 
ATOM 13794 C C   . VAL I 2 18  ? 105.300 12.566  21.930  1.000 75.490  ? 18  VAL III C   1 
ATOM 13795 O O   . VAL I 2 18  ? 105.794 12.457  23.063  1.000 86.340  ? 18  VAL III O   1 
ATOM 13796 C CB  . VAL I 2 18  ? 102.904 13.347  21.975  1.000 78.660  ? 18  VAL III CB  1 
ATOM 13797 C CG1 . VAL I 2 18  ? 103.021 14.370  20.855  1.000 81.000  ? 18  VAL III CG1 1 
ATOM 13798 C CG2 . VAL I 2 18  ? 101.466 12.893  22.136  1.000 79.130  ? 18  VAL III CG2 1 
ATOM 13799 N N   . THR I 2 19  ? 105.944 13.035  20.864  1.000 73.900  ? 19  THR III N   1 
ATOM 13800 C CA  . THR I 2 19  ? 107.374 13.429  20.851  1.000 69.960  ? 19  THR III CA  1 
ATOM 13801 C C   . THR I 2 19  ? 107.485 14.834  20.242  1.000 64.000  ? 19  THR III C   1 
ATOM 13802 O O   . THR I 2 19  ? 107.106 15.005  19.075  1.000 65.490  ? 19  THR III O   1 
ATOM 13803 C CB  . THR I 2 19  ? 108.211 12.334  20.165  1.000 75.140  ? 19  THR III CB  1 
ATOM 13804 O OG1 . THR I 2 19  ? 109.574 12.561  20.517  1.000 73.280  ? 19  THR III OG1 1 
ATOM 13805 C CG2 . THR I 2 19  ? 108.061 12.273  18.656  1.000 76.490  ? 19  THR III CG2 1 
ATOM 13806 N N   . ILE I 2 20  ? 107.967 15.816  21.009  1.000 58.780  ? 20  ILE III N   1 
ATOM 13807 C CA  . ILE I 2 20  ? 108.274 17.190  20.508  1.000 58.730  ? 20  ILE III CA  1 
ATOM 13808 C C   . ILE I 2 20  ? 109.794 17.337  20.387  1.000 59.650  ? 20  ILE III C   1 
ATOM 13809 O O   . ILE I 2 20  ? 110.480 17.177  21.407  1.000 71.730  ? 20  ILE III O   1 
ATOM 13810 C CB  . ILE I 2 20  ? 107.684 18.290  21.414  1.000 56.400  ? 20  ILE III CB  1 
ATOM 13811 C CG1 . ILE I 2 20  ? 106.229 18.010  21.798  1.000 58.300  ? 20  ILE III CG1 1 
ATOM 13812 C CG2 . ILE I 2 20  ? 107.844 19.651  20.744  1.000 55.300  ? 20  ILE III CG2 1 
ATOM 13813 C CD1 . ILE I 2 20  ? 105.666 18.951  22.847  1.000 58.150  ? 20  ILE III CD1 1 
ATOM 13814 N N   . SER I 2 21  ? 110.291 17.652  19.191  1.000 57.460  ? 21  SER III N   1 
ATOM 13815 C CA  . SER I 2 21  ? 111.741 17.790  18.918  1.000 59.510  ? 21  SER III CA  1 
ATOM 13816 C C   . SER I 2 21  ? 112.168 19.256  19.075  1.000 61.360  ? 21  SER III C   1 
ATOM 13817 O O   . SER I 2 21  ? 111.327 20.148  18.893  1.000 58.580  ? 21  SER III O   1 
ATOM 13818 C CB  . SER I 2 21  ? 112.099 17.236  17.568  1.000 59.530  ? 21  SER III CB  1 
ATOM 13819 O OG  . SER I 2 21  ? 111.390 17.904  16.553  1.000 69.740  ? 21  SER III OG  1 
ATOM 13820 N N   . CYS I 2 22  ? 113.442 19.472  19.413  1.000 66.010  ? 22  CYS III N   1 
ATOM 13821 C CA  . CYS I 2 22  ? 114.120 20.790  19.451  1.000 64.590  ? 22  CYS III CA  1 
ATOM 13822 C C   . CYS I 2 22  ? 115.510 20.660  18.829  1.000 66.590  ? 22  CYS III C   1 
ATOM 13823 O O   . CYS I 2 22  ? 116.329 19.869  19.330  1.000 68.420  ? 22  CYS III O   1 
ATOM 13824 C CB  . CYS I 2 22  ? 114.219 21.339  20.867  1.000 67.280  ? 22  CYS III CB  1 
ATOM 13825 S SG  . CYS I 2 22  ? 114.254 23.149  20.828  1.000 64.700  ? 22  CYS III SG  1 
ATOM 13826 N N   . SER I 2 23  ? 115.733 21.348  17.712  1.000 70.050  ? 23  SER III N   1 
ATOM 13827 C CA  . SER I 2 23  ? 116.980 21.246  16.901  1.000 71.960  ? 23  SER III CA  1 
ATOM 13828 C C   . SER I 2 23  ? 117.710 22.584  16.986  1.000 66.110  ? 23  SER III C   1 
ATOM 13829 O O   . SER I 2 23  ? 117.062 23.643  16.791  1.000 57.830  ? 23  SER III O   1 
ATOM 13830 C CB  . SER I 2 23  ? 116.673 20.861  15.482  1.000 73.500  ? 23  SER III CB  1 
ATOM 13831 O OG  . SER I 2 23  ? 117.849 20.897  14.689  1.000 81.130  ? 23  SER III OG  1 
ATOM 13832 N N   . GLY I 2 24  ? 119.007 22.522  17.296  1.000 62.150  ? 24  GLY III N   1 
ATOM 13833 C CA  . GLY I 2 24  ? 119.876 23.703  17.429  1.000 60.670  ? 24  GLY III CA  1 
ATOM 13834 C C   . GLY I 2 24  ? 121.177 23.508  16.665  1.000 55.860  ? 24  GLY III C   1 
ATOM 13835 O O   . GLY I 2 24  ? 121.176 22.771  15.669  1.000 51.260  ? 24  GLY III O   1 
ATOM 13836 N N   . GLY I 2 25  ? 122.237 24.176  17.115  1.000 56.790  ? 25  GLY III N   1 
ATOM 13837 C CA  . GLY I 2 25  ? 123.565 24.169  16.462  1.000 57.330  ? 25  GLY III CA  1 
ATOM 13838 C C   . GLY I 2 25  ? 124.678 24.179  17.478  1.000 53.180  ? 25  GLY III C   1 
ATOM 13839 O O   . GLY I 2 25  ? 124.386 24.350  18.667  1.000 53.660  ? 25  GLY III O   1 
ATOM 13840 N N   . SER I 2 26  ? 125.925 23.981  17.038  1.000 49.600  ? 26  SER III N   1 
ATOM 13841 C CA  . SER I 2 26  ? 127.099 23.796  17.929  1.000 49.810  ? 26  SER III CA  1 
ATOM 13842 C C   . SER I 2 26  ? 127.194 24.935  18.963  1.000 45.950  ? 26  SER III C   1 
ATOM 13843 O O   . SER I 2 26  ? 127.539 24.661  20.101  1.000 43.490  ? 26  SER III O   1 
ATOM 13844 C CB  . SER I 2 26  ? 128.365 23.647  17.128  1.000 46.790  ? 26  SER III CB  1 
ATOM 13845 O OG  . SER I 2 26  ? 128.684 24.861  16.478  1.000 48.500  ? 26  SER III OG  1 
ATOM 13846 N N   . SER I 2 27  ? 126.866 26.161  18.584  1.000 50.670  ? 27  SER III N   1 
ATOM 13847 C CA  . SER I 2 27  ? 126.959 27.374  19.445  1.000 54.510  ? 27  SER III CA  1 
ATOM 13848 C C   . SER I 2 27  ? 125.937 27.326  20.598  1.000 59.040  ? 27  SER III C   1 
ATOM 13849 O O   . SER I 2 27  ? 126.191 27.957  21.637  1.000 63.170  ? 27  SER III O   1 
ATOM 13850 C CB  . SER I 2 27  ? 126.777 28.632  18.616  1.000 60.870  ? 27  SER III CB  1 
ATOM 13851 O OG  . SER I 2 27  ? 125.540 28.616  17.897  1.000 63.530  ? 27  SER III OG  1 
ATOM 13852 N N   . ASN I 2 28  ? 124.807 26.623  20.443  1.000 54.050  ? 28  ASN III N   1 
ATOM 13853 C CA  . ASN I 2 28  ? 123.765 26.520  21.498  1.000 46.580  ? 28  ASN III CA  1 
ATOM 13854 C C   . ASN I 2 28  ? 123.716 25.068  22.003  1.000 49.490  ? 28  ASN III C   1 
ATOM 13855 O O   . ASN I 2 28  ? 124.526 24.738  22.915  1.000 47.330  ? 28  ASN III O   1 
ATOM 13856 C CB  . ASN I 2 28  ? 122.436 27.090  20.995  1.000 41.870  ? 28  ASN III CB  1 
ATOM 13857 N N   . ILE I 2 29  ? 122.833 24.226  21.435  1.000 52.190  ? 29  ILE III N   1 
ATOM 13858 C CA  . ILE I 2 29  ? 122.467 22.899  22.021  1.000 50.240  ? 29  ILE III CA  1 
ATOM 13859 C C   . ILE I 2 29  ? 123.683 21.968  22.024  1.000 52.020  ? 29  ILE III C   1 
ATOM 13860 O O   . ILE I 2 29  ? 123.732 21.068  22.910  1.000 64.050  ? 29  ILE III O   1 
ATOM 13861 C CB  . ILE I 2 29  ? 121.254 22.258  21.314  1.000 47.170  ? 29  ILE III CB  1 
ATOM 13862 C CG1 . ILE I 2 29  ? 119.993 23.080  21.580  1.000 47.300  ? 29  ILE III CG1 1 
ATOM 13863 C CG2 . ILE I 2 29  ? 121.081 20.808  21.763  1.000 48.490  ? 29  ILE III CG2 1 
ATOM 13864 C CD1 . ILE I 2 29  ? 118.691 22.425  21.131  1.000 48.630  ? 29  ILE III CD1 1 
ATOM 13865 N N   . GLY I 2 30  ? 124.615 22.170  21.088  1.000 49.810  ? 30  GLY III N   1 
ATOM 13866 C CA  . GLY I 2 30  ? 125.846 21.367  20.976  1.000 50.810  ? 30  GLY III CA  1 
ATOM 13867 C C   . GLY I 2 30  ? 126.630 21.403  22.268  1.000 48.290  ? 30  GLY III C   1 
ATOM 13868 O O   . GLY I 2 30  ? 126.923 20.326  22.841  1.000 50.440  ? 30  GLY III O   1 
ATOM 13869 N N   . SER I 2 31  ? 126.870 22.616  22.759  1.000 47.030  ? 31  SER III N   1 
ATOM 13870 C CA  . SER I 2 31  ? 127.760 22.895  23.908  1.000 48.440  ? 31  SER III CA  1 
ATOM 13871 C C   . SER I 2 31  ? 126.975 23.266  25.169  1.000 46.480  ? 31  SER III C   1 
ATOM 13872 O O   . SER I 2 31  ? 127.665 23.398  26.193  1.000 46.230  ? 31  SER III O   1 
ATOM 13873 C CB  . SER I 2 31  ? 128.751 23.965  23.566  1.000 46.080  ? 31  SER III CB  1 
ATOM 13874 O OG  . SER I 2 31  ? 129.677 23.500  22.594  1.000 49.120  ? 31  SER III OG  1 
ATOM 13875 N N   . ASN I 2 32  ? 125.638 23.432  25.114  1.000 41.590  ? 32  ASN III N   1 
ATOM 13876 C CA  . ASN I 2 32  ? 124.835 23.886  26.281  1.000 39.490  ? 32  ASN III CA  1 
ATOM 13877 C C   . ASN I 2 32  ? 123.576 23.040  26.479  1.000 38.690  ? 32  ASN III C   1 
ATOM 13878 O O   . ASN I 2 32  ? 123.016 22.500  25.522  1.000 41.820  ? 32  ASN III O   1 
ATOM 13879 C CB  . ASN I 2 32  ? 124.552 25.377  26.184  1.000 41.340  ? 32  ASN III CB  1 
ATOM 13880 C CG  . ASN I 2 32  ? 125.835 26.175  26.051  1.000 45.690  ? 32  ASN III CG  1 
ATOM 13881 O OD1 . ASN I 2 32  ? 126.634 26.264  26.985  1.000 44.700  ? 32  ASN III OD1 1 
ATOM 13882 N ND2 . ASN I 2 32  ? 126.041 26.789  24.899  1.000 57.050  ? 32  ASN III ND2 1 
ATOM 13883 N N   . PRO I 2 33  ? 123.116 22.860  27.742  1.000 37.460  ? 33  PRO III N   1 
ATOM 13884 C CA  . PRO I 2 33  ? 121.951 22.034  28.050  1.000 38.540  ? 33  PRO III CA  1 
ATOM 13885 C C   . PRO I 2 33  ? 120.624 22.725  27.723  1.000 41.280  ? 33  PRO III C   1 
ATOM 13886 O O   . PRO I 2 33  ? 120.530 23.945  27.883  1.000 46.600  ? 33  PRO III O   1 
ATOM 13887 C CB  . PRO I 2 33  ? 121.955 21.857  29.575  1.000 38.810  ? 33  PRO III CB  1 
ATOM 13888 C CG  . PRO I 2 33  ? 123.281 22.417  30.015  1.000 40.060  ? 33  PRO III CG  1 
ATOM 13889 C CD  . PRO I 2 33  ? 123.673 23.434  28.965  1.000 38.410  ? 33  PRO III CD  1 
ATOM 13890 N N   . VAL I 2 34  ? 119.627 21.919  27.370  1.000 40.460  ? 34  VAL III N   1 
ATOM 13891 C CA  . VAL I 2 34  ? 118.234 22.350  27.073  1.000 39.370  ? 34  VAL III CA  1 
ATOM 13892 C C   . VAL I 2 34  ? 117.352 22.117  28.299  1.000 37.960  ? 34  VAL III C   1 
ATOM 13893 O O   . VAL I 2 34  ? 117.279 20.969  28.749  1.000 35.110  ? 34  VAL III O   1 
ATOM 13894 C CB  . VAL I 2 34  ? 117.683 21.555  25.878  1.000 41.390  ? 34  VAL III CB  1 
ATOM 13895 C CG1 . VAL I 2 34  ? 116.227 21.906  25.605  1.000 42.740  ? 34  VAL III CG1 1 
ATOM 13896 C CG2 . VAL I 2 34  ? 118.564 21.708  24.643  1.000 41.020  ? 34  VAL III CG2 1 
ATOM 13897 N N   . ASN I 2 35  ? 116.661 23.150  28.792  1.000 41.680  ? 35  ASN III N   1 
ATOM 13898 C CA  . ASN I 2 35  ? 115.485 22.990  29.695  1.000 44.910  ? 35  ASN III CA  1 
ATOM 13899 C C   . ASN I 2 35  ? 114.204 23.082  28.856  1.000 41.840  ? 35  ASN III C   1 
ATOM 13900 O O   . ASN I 2 35  ? 114.199 23.833  27.871  1.000 36.810  ? 35  ASN III O   1 
ATOM 13901 C CB  . ASN I 2 35  ? 115.460 24.002  30.848  1.000 47.940  ? 35  ASN III CB  1 
ATOM 13902 C CG  . ASN I 2 35  ? 116.625 23.854  31.810  1.000 49.700  ? 35  ASN III CG  1 
ATOM 13903 O OD1 . ASN I 2 35  ? 117.717 23.461  31.407  1.000 54.870  ? 35  ASN III OD1 1 
ATOM 13904 N ND2 . ASN I 2 35  ? 116.423 24.214  33.071  1.000 47.420  ? 35  ASN III ND2 1 
ATOM 13905 N N   . TRP I 2 36  ? 113.202 22.289  29.224  1.000 46.360  ? 36  TRP III N   1 
ATOM 13906 C CA  . TRP I 2 36  ? 111.821 22.335  28.692  1.000 52.380  ? 36  TRP III CA  1 
ATOM 13907 C C   . TRP I 2 36  ? 110.903 22.972  29.744  1.000 52.970  ? 36  TRP III C   1 
ATOM 13908 O O   . TRP I 2 36  ? 111.000 22.582  30.928  1.000 51.250  ? 36  TRP III O   1 
ATOM 13909 C CB  . TRP I 2 36  ? 111.326 20.929  28.342  1.000 57.970  ? 36  TRP III CB  1 
ATOM 13910 C CG  . TRP I 2 36  ? 111.984 20.326  27.144  1.000 58.140  ? 36  TRP III CG  1 
ATOM 13911 C CD1 . TRP I 2 36  ? 113.103 19.547  27.110  1.000 58.740  ? 36  TRP III CD1 1 
ATOM 13912 C CD2 . TRP I 2 36  ? 111.543 20.463  25.787  1.000 58.370  ? 36  TRP III CD2 1 
ATOM 13913 N NE1 . TRP I 2 36  ? 113.378 19.173  25.825  1.000 59.770  ? 36  TRP III NE1 1 
ATOM 13914 C CE2 . TRP I 2 36  ? 112.443 19.729  24.990  1.000 59.100  ? 36  TRP III CE2 1 
ATOM 13915 C CE3 . TRP I 2 36  ? 110.480 21.132  25.172  1.000 59.820  ? 36  TRP III CE3 1 
ATOM 13916 C CZ2 . TRP I 2 36  ? 112.293 19.631  23.610  1.000 58.620  ? 36  TRP III CZ2 1 
ATOM 13917 C CZ3 . TRP I 2 36  ? 110.342 21.043  23.807  1.000 58.220  ? 36  TRP III CZ3 1 
ATOM 13918 C CH2 . TRP I 2 36  ? 111.239 20.303  23.039  1.000 57.870  ? 36  TRP III CH2 1 
ATOM 13919 N N   . PHE I 2 37  ? 110.050 23.911  29.332  1.000 49.970  ? 37  PHE III N   1 
ATOM 13920 C CA  . PHE I 2 37  ? 109.060 24.570  30.217  1.000 44.510  ? 37  PHE III CA  1 
ATOM 13921 C C   . PHE I 2 37  ? 107.662 24.266  29.693  1.000 45.630  ? 37  PHE III C   1 
ATOM 13922 O O   . PHE I 2 37  ? 107.469 24.331  28.466  1.000 42.150  ? 37  PHE III O   1 
ATOM 13923 C CB  . PHE I 2 37  ? 109.335 26.067  30.326  1.000 41.570  ? 37  PHE III CB  1 
ATOM 13924 C CG  . PHE I 2 37  ? 110.738 26.387  30.755  1.000 43.080  ? 37  PHE III CG  1 
ATOM 13925 C CD1 . PHE I 2 37  ? 111.117 26.323  32.084  1.000 53.140  ? 37  PHE III CD1 1 
ATOM 13926 C CD2 . PHE I 2 37  ? 111.692 26.730  29.824  1.000 45.920  ? 37  PHE III CD2 1 
ATOM 13927 C CE1 . PHE I 2 37  ? 112.427 26.587  32.464  1.000 57.520  ? 37  PHE III CE1 1 
ATOM 13928 C CE2 . PHE I 2 37  ? 112.993 27.030  30.208  1.000 50.760  ? 37  PHE III CE2 1 
ATOM 13929 C CZ  . PHE I 2 37  ? 113.359 26.968  31.528  1.000 52.050  ? 37  PHE III CZ  1 
ATOM 13930 N N   . GLN I 2 38  ? 106.752 23.911  30.605  1.000 56.630  ? 38  GLN III N   1 
ATOM 13931 C CA  . GLN I 2 38  ? 105.312 23.657  30.314  1.000 59.190  ? 38  GLN III CA  1 
ATOM 13932 C C   . GLN I 2 38  ? 104.557 24.936  30.665  1.000 60.060  ? 38  GLN III C   1 
ATOM 13933 O O   . GLN I 2 38  ? 104.900 25.522  31.715  1.000 50.370  ? 38  GLN III O   1 
ATOM 13934 C CB  . GLN I 2 38  ? 104.807 22.458  31.121  1.000 57.650  ? 38  GLN III CB  1 
ATOM 13935 C CG  . GLN I 2 38  ? 103.369 22.081  30.820  1.000 57.450  ? 38  GLN III CG  1 
ATOM 13936 C CD  . GLN I 2 38  ? 102.877 20.988  31.746  1.000 61.620  ? 38  GLN III CD  1 
ATOM 13937 O OE1 . GLN I 2 38  ? 102.706 21.186  32.949  1.000 61.590  ? 38  GLN III OE1 1 
ATOM 13938 N NE2 . GLN I 2 38  ? 102.616 19.816  31.185  1.000 56.150  ? 38  GLN III NE2 1 
ATOM 13939 N N   . GLN I 2 39  ? 103.643 25.376  29.792  1.000 66.330  ? 39  GLN III N   1 
ATOM 13940 C CA  . GLN I 2 39  ? 102.855 26.626  29.975  1.000 74.770  ? 39  GLN III CA  1 
ATOM 13941 C C   . GLN I 2 39  ? 101.390 26.370  29.609  1.000 79.580  ? 39  GLN III C   1 
ATOM 13942 O O   . GLN I 2 39  ? 101.097 26.120  28.423  1.000 83.780  ? 39  GLN III O   1 
ATOM 13943 C CB  . GLN I 2 39  ? 103.417 27.785  29.148  1.000 70.070  ? 39  GLN III CB  1 
ATOM 13944 C CG  . GLN I 2 39  ? 102.887 29.146  29.596  1.000 70.640  ? 39  GLN III CG  1 
ATOM 13945 C CD  . GLN I 2 39  ? 103.506 30.305  28.840  1.000 66.880  ? 39  GLN III CD  1 
ATOM 13946 O OE1 . GLN I 2 39  ? 103.956 30.178  27.704  1.000 59.770  ? 39  GLN III OE1 1 
ATOM 13947 N NE2 . GLN I 2 39  ? 103.531 31.472  29.467  1.000 67.200  ? 39  GLN III NE2 1 
ATOM 13948 N N   . PHE I 2 40  ? 100.515 26.434  30.608  1.000 82.710  ? 40  PHE III N   1 
ATOM 13949 C CA  . PHE I 2 40  ? 99.046  26.465  30.427  1.000 84.430  ? 40  PHE III CA  1 
ATOM 13950 C C   . PHE I 2 40  ? 98.629  27.908  30.187  1.000 93.070  ? 40  PHE III C   1 
ATOM 13951 O O   . PHE I 2 40  ? 99.207  28.809  30.806  1.000 105.350 ? 40  PHE III O   1 
ATOM 13952 C CB  . PHE I 2 40  ? 98.355  25.877  31.651  1.000 82.350  ? 40  PHE III CB  1 
ATOM 13953 C CG  . PHE I 2 40  ? 98.771  24.459  31.925  1.000 71.740  ? 40  PHE III CG  1 
ATOM 13954 C CD1 . PHE I 2 40  ? 98.696  23.497  30.935  1.000 65.470  ? 40  PHE III CD1 1 
ATOM 13955 C CD2 . PHE I 2 40  ? 99.255  24.101  33.164  1.000 70.340  ? 40  PHE III CD2 1 
ATOM 13956 C CE1 . PHE I 2 40  ? 99.079  22.195  31.191  1.000 66.300  ? 40  PHE III CE1 1 
ATOM 13957 C CE2 . PHE I 2 40  ? 99.638  22.794  33.418  1.000 75.470  ? 40  PHE III CE2 1 
ATOM 13958 C CZ  . PHE I 2 40  ? 99.563  21.850  32.427  1.000 71.040  ? 40  PHE III CZ  1 
ATOM 13959 N N   . PRO I 2 41  ? 97.660  28.148  29.269  1.000 96.170  ? 41  PRO III N   1 
ATOM 13960 C CA  . PRO I 2 41  ? 97.178  29.500  28.972  1.000 90.050  ? 41  PRO III CA  1 
ATOM 13961 C C   . PRO I 2 41  ? 97.009  30.379  30.220  1.000 83.120  ? 41  PRO III C   1 
ATOM 13962 O O   . PRO I 2 41  ? 96.478  29.894  31.210  1.000 72.640  ? 41  PRO III O   1 
ATOM 13963 C CB  . PRO I 2 41  ? 95.826  29.242  28.329  1.000 86.560  ? 41  PRO III CB  1 
ATOM 13964 C CG  . PRO I 2 41  ? 95.993  27.902  27.628  1.000 88.930  ? 41  PRO III CG  1 
ATOM 13965 C CD  . PRO I 2 41  ? 96.994  27.121  28.456  1.000 89.690  ? 41  PRO III CD  1 
ATOM 13966 N N   . GLY I 2 42  ? 97.529  31.609  30.160  1.000 77.480  ? 42  GLY III N   1 
ATOM 13967 C CA  . GLY I 2 42  ? 97.342  32.651  31.185  1.000 78.800  ? 42  GLY III CA  1 
ATOM 13968 C C   . GLY I 2 42  ? 98.035  32.356  32.504  1.000 77.420  ? 42  GLY III C   1 
ATOM 13969 O O   . GLY I 2 42  ? 97.802  33.116  33.441  1.000 78.810  ? 42  GLY III O   1 
ATOM 13970 N N   . THR I 2 43  ? 98.885  31.325  32.581  1.000 85.730  ? 43  THR III N   1 
ATOM 13971 C CA  . THR I 2 43  ? 99.832  31.113  33.716  1.000 88.300  ? 43  THR III CA  1 
ATOM 13972 C C   . THR I 2 43  ? 101.272 31.269  33.214  1.000 95.200  ? 43  THR III C   1 
ATOM 13973 O O   . THR I 2 43  ? 101.485 31.385  31.976  1.000 93.820  ? 43  THR III O   1 
ATOM 13974 C CB  . THR I 2 43  ? 99.613  29.779  34.441  1.000 78.970  ? 43  THR III CB  1 
ATOM 13975 O OG1 . THR I 2 43  ? 99.632  28.712  33.492  1.000 83.010  ? 43  THR III OG1 1 
ATOM 13976 N N   . ALA I 2 44  ? 102.211 31.331  34.159  1.000 86.480  ? 44  ALA III N   1 
ATOM 13977 C CA  . ALA I 2 44  ? 103.660 31.418  33.889  1.000 78.090  ? 44  ALA III CA  1 
ATOM 13978 C C   . ALA I 2 44  ? 104.124 30.099  33.279  1.000 71.640  ? 44  ALA III C   1 
ATOM 13979 O O   . ALA I 2 44  ? 103.443 29.085  33.443  1.000 72.010  ? 44  ALA III O   1 
ATOM 13980 C CB  . ALA I 2 44  ? 104.392 31.713  35.171  1.000 77.090  ? 44  ALA III CB  1 
ATOM 13981 N N   . PRO I 2 45  ? 105.288 30.076  32.588  1.000 60.010  ? 45  PRO III N   1 
ATOM 13982 C CA  . PRO I 2 45  ? 105.975 28.828  32.286  1.000 54.980  ? 45  PRO III CA  1 
ATOM 13983 C C   . PRO I 2 45  ? 106.422 28.179  33.598  1.000 56.450  ? 45  PRO III C   1 
ATOM 13984 O O   . PRO I 2 45  ? 106.588 28.886  34.568  1.000 59.790  ? 45  PRO III O   1 
ATOM 13985 C CB  . PRO I 2 45  ? 107.201 29.242  31.467  1.000 57.170  ? 45  PRO III CB  1 
ATOM 13986 C CG  . PRO I 2 45  ? 106.943 30.666  31.031  1.000 56.690  ? 45  PRO III CG  1 
ATOM 13987 C CD  . PRO I 2 45  ? 106.009 31.247  32.072  1.000 58.900  ? 45  PRO III CD  1 
ATOM 13988 N N   . LYS I 2 46  ? 106.595 26.861  33.594  1.000 59.060  ? 46  LYS III N   1 
ATOM 13989 C CA  . LYS I 2 46  ? 107.138 26.096  34.749  1.000 62.020  ? 46  LYS III CA  1 
ATOM 13990 C C   . LYS I 2 46  ? 108.144 25.084  34.202  1.000 60.050  ? 46  LYS III C   1 
ATOM 13991 O O   . LYS I 2 46  ? 107.957 24.621  33.051  1.000 67.330  ? 46  LYS III O   1 
ATOM 13992 C CB  . LYS I 2 46  ? 106.005 25.437  35.547  1.000 63.740  ? 46  LYS III CB  1 
ATOM 13993 C CG  . LYS I 2 46  ? 106.446 24.688  36.796  1.000 63.220  ? 46  LYS III CG  1 
ATOM 13994 C CD  . LYS I 2 46  ? 105.326 24.305  37.759  1.000 58.420  ? 46  LYS III CD  1 
ATOM 13995 C CE  . LYS I 2 46  ? 105.861 23.549  38.963  1.000 57.770  ? 46  LYS III CE  1 
ATOM 13996 N NZ  . LYS I 2 46  ? 105.229 23.962  40.249  1.000 55.120  ? 46  LYS III NZ  1 
ATOM 13997 N N   . LEU I 2 47  ? 109.180 24.788  34.992  1.000 54.510  ? 47  LEU III N   1 
ATOM 13998 C CA  . LEU I 2 47  ? 110.223 23.803  34.616  1.000 51.370  ? 47  LEU III CA  1 
ATOM 13999 C C   . LEU I 2 47  ? 109.585 22.413  34.512  1.000 47.380  ? 47  LEU III C   1 
ATOM 14000 O O   . LEU I 2 47  ? 108.969 21.981  35.500  1.000 47.990  ? 47  LEU III O   1 
ATOM 14001 C CB  . LEU I 2 47  ? 111.334 23.825  35.665  1.000 51.580  ? 47  LEU III CB  1 
ATOM 14002 C CG  . LEU I 2 47  ? 112.505 22.894  35.361  1.000 49.990  ? 47  LEU III CG  1 
ATOM 14003 C CD1 . LEU I 2 47  ? 113.178 23.334  34.073  1.000 49.170  ? 47  LEU III CD1 1 
ATOM 14004 C CD2 . LEU I 2 47  ? 113.464 22.824  36.532  1.000 47.230  ? 47  LEU III CD2 1 
ATOM 14005 N N   . LEU I 2 48  ? 109.746 21.755  33.364  1.000 46.150  ? 48  LEU III N   1 
ATOM 14006 C CA  . LEU I 2 48  ? 109.240 20.382  33.095  1.000 43.810  ? 48  LEU III CA  1 
ATOM 14007 C C   . LEU I 2 48  ? 110.423 19.408  33.020  1.000 42.610  ? 48  LEU III C   1 
ATOM 14008 O O   . LEU I 2 48  ? 110.437 18.423  33.769  1.000 41.040  ? 48  LEU III O   1 
ATOM 14009 C CB  . LEU I 2 48  ? 108.458 20.408  31.779  1.000 44.170  ? 48  LEU III CB  1 
ATOM 14010 C CG  . LEU I 2 48  ? 107.811 19.071  31.418  1.000 46.890  ? 48  LEU III CG  1 
ATOM 14011 C CD1 . LEU I 2 48  ? 106.701 18.738  32.389  1.000 47.190  ? 48  LEU III CD1 1 
ATOM 14012 C CD2 . LEU I 2 48  ? 107.289 19.068  29.994  1.000 47.960  ? 48  LEU III CD2 1 
ATOM 14013 N N   . ILE I 2 49  ? 111.380 19.688  32.131  1.000 41.260  ? 49  ILE III N   1 
ATOM 14014 C CA  . ILE I 2 49  ? 112.667 18.939  32.009  1.000 37.520  ? 49  ILE III CA  1 
ATOM 14015 C C   . ILE I 2 49  ? 113.810 19.944  32.132  1.000 38.570  ? 49  ILE III C   1 
ATOM 14016 O O   . ILE I 2 49  ? 113.664 21.044  31.571  1.000 39.820  ? 49  ILE III O   1 
ATOM 14017 C CB  . ILE I 2 49  ? 112.722 18.196  30.669  1.000 35.710  ? 49  ILE III CB  1 
ATOM 14018 C CG1 . ILE I 2 49  ? 111.633 17.127  30.578  1.000 36.980  ? 49  ILE III CG1 1 
ATOM 14019 C CG2 . ILE I 2 49  ? 114.086 17.596  30.440  1.000 35.420  ? 49  ILE III CG2 1 
ATOM 14020 C CD1 . ILE I 2 49  ? 111.765 15.985  31.564  1.000 38.630  ? 49  ILE III CD1 1 
ATOM 14021 N N   . TYR I 2 50  ? 114.901 19.573  32.815  1.000 38.480  ? 50  TYR III N   1 
ATOM 14022 C CA  . TYR I 2 50  ? 116.180 20.337  32.812  1.000 37.530  ? 50  TYR III CA  1 
ATOM 14023 C C   . TYR I 2 50  ? 117.339 19.440  32.363  1.000 37.490  ? 50  TYR III C   1 
ATOM 14024 O O   . TYR I 2 50  ? 117.227 18.202  32.395  1.000 40.270  ? 50  TYR III O   1 
ATOM 14025 C CB  . TYR I 2 50  ? 116.432 20.932  34.191  1.000 36.590  ? 50  TYR III CB  1 
ATOM 14026 C CG  . TYR I 2 50  ? 116.882 19.959  35.252  1.000 37.900  ? 50  TYR III CG  1 
ATOM 14027 C CD1 . TYR I 2 50  ? 115.974 19.173  35.943  1.000 39.920  ? 50  TYR III CD1 1 
ATOM 14028 C CD2 . TYR I 2 50  ? 118.218 19.856  35.596  1.000 37.500  ? 50  TYR III CD2 1 
ATOM 14029 C CE1 . TYR I 2 50  ? 116.379 18.294  36.933  1.000 40.490  ? 50  TYR III CE1 1 
ATOM 14030 C CE2 . TYR I 2 50  ? 118.642 18.970  36.571  1.000 40.920  ? 50  TYR III CE2 1 
ATOM 14031 C CZ  . TYR I 2 50  ? 117.719 18.198  37.259  1.000 41.770  ? 50  TYR III CZ  1 
ATOM 14032 O OH  . TYR I 2 50  ? 118.117 17.328  38.238  1.000 41.920  ? 50  TYR III OH  1 
ATOM 14033 N N   . ALA I 2 51  ? 118.446 20.052  31.954  1.000 36.640  ? 51  ALA III N   1 
ATOM 14034 C CA  . ALA I 2 51  ? 119.677 19.347  31.538  1.000 37.400  ? 51  ALA III CA  1 
ATOM 14035 C C   . ALA I 2 51  ? 119.312 18.225  30.546  1.000 38.250  ? 51  ALA III C   1 
ATOM 14036 O O   . ALA I 2 51  ? 119.814 17.098  30.693  1.000 37.020  ? 51  ALA III O   1 
ATOM 14037 C CB  . ALA I 2 51  ? 120.398 18.838  32.751  1.000 36.030  ? 51  ALA III CB  1 
ATOM 14038 N N   . ASN I 2 52  ? 118.458 18.548  29.566  1.000 36.150  ? 52  ASN III N   1 
ATOM 14039 C CA  . ASN I 2 52  ? 118.158 17.730  28.368  1.000 34.200  ? 52  ASN III CA  1 
ATOM 14040 C C   . ASN I 2 52  ? 117.150 16.612  28.713  1.000 33.940  ? 52  ASN III C   1 
ATOM 14041 O O   . ASN I 2 52  ? 116.234 16.385  27.888  1.000 32.150  ? 52  ASN III O   1 
ATOM 14042 C CB  . ASN I 2 52  ? 119.416 17.128  27.747  1.000 34.350  ? 52  ASN III CB  1 
ATOM 14043 C CG  . ASN I 2 52  ? 120.489 18.133  27.439  1.000 35.170  ? 52  ASN III CG  1 
ATOM 14044 O OD1 . ASN I 2 52  ? 120.310 18.994  26.594  1.000 36.660  ? 52  ASN III OD1 1 
ATOM 14045 N ND2 . ASN I 2 52  ? 121.628 17.996  28.096  1.000 39.720  ? 52  ASN III ND2 1 
ATOM 14046 N N   . THR I 2 53  ? 117.331 15.942  29.864  1.000 34.450  ? 53  THR III N   1 
ATOM 14047 C CA  . THR I 2 53  ? 116.809 14.571  30.137  1.000 37.460  ? 53  THR III CA  1 
ATOM 14048 C C   . THR I 2 53  ? 116.409 14.355  31.602  1.000 39.190  ? 53  THR III C   1 
ATOM 14049 O O   . THR I 2 53  ? 116.095 13.221  31.915  1.000 43.620  ? 53  THR III O   1 
ATOM 14050 C CB  . THR I 2 53  ? 117.847 13.491  29.784  1.000 38.010  ? 53  THR III CB  1 
ATOM 14051 O OG1 . THR I 2 53  ? 119.108 13.697  30.423  1.000 39.920  ? 53  THR III OG1 1 
ATOM 14052 C CG2 . THR I 2 53  ? 118.128 13.414  28.304  1.000 37.940  ? 53  THR III CG2 1 
ATOM 14053 N N   . GLN I 2 54  ? 116.386 15.368  32.469  1.000 39.100  ? 54  GLN III N   1 
ATOM 14054 C CA  . GLN I 2 54  ? 116.187 15.160  33.930  1.000 36.910  ? 54  GLN III CA  1 
ATOM 14055 C C   . GLN I 2 54  ? 114.866 15.789  34.372  1.000 39.720  ? 54  GLN III C   1 
ATOM 14056 O O   . GLN I 2 54  ? 114.534 16.881  33.872  1.000 46.510  ? 54  GLN III O   1 
ATOM 14057 C CB  . GLN I 2 54  ? 117.347 15.798  34.678  1.000 37.450  ? 54  GLN III CB  1 
ATOM 14058 C CG  . GLN I 2 54  ? 118.695 15.335  34.154  1.000 37.010  ? 54  GLN III CG  1 
ATOM 14059 C CD  . GLN I 2 54  ? 118.909 13.889  34.484  1.000 35.540  ? 54  GLN III CD  1 
ATOM 14060 O OE1 . GLN I 2 54  ? 118.865 13.506  35.650  1.000 35.130  ? 54  GLN III OE1 1 
ATOM 14061 N NE2 . GLN I 2 54  ? 119.116 13.086  33.455  1.000 35.900  ? 54  GLN III NE2 1 
ATOM 14062 N N   . ARG I 2 55  ? 114.168 15.149  35.309  1.000 40.500  ? 55  ARG III N   1 
ATOM 14063 C CA  . ARG I 2 55  ? 112.883 15.638  35.866  1.000 43.780  ? 55  ARG III CA  1 
ATOM 14064 C C   . ARG I 2 55  ? 113.114 16.265  37.233  1.000 44.960  ? 55  ARG III C   1 
ATOM 14065 O O   . ARG I 2 55  ? 113.796 15.701  38.070  1.000 45.210  ? 55  ARG III O   1 
ATOM 14066 C CB  . ARG I 2 55  ? 111.904 14.479  35.998  1.000 46.880  ? 55  ARG III CB  1 
ATOM 14067 C CG  . ARG I 2 55  ? 111.306 14.039  34.681  1.000 52.920  ? 55  ARG III CG  1 
ATOM 14068 C CD  . ARG I 2 55  ? 110.167 13.056  34.856  1.000 61.460  ? 55  ARG III CD  1 
ATOM 14069 N NE  . ARG I 2 55  ? 110.615 11.686  35.063  1.000 63.530  ? 55  ARG III NE  1 
ATOM 14070 C CZ  . ARG I 2 55  ? 110.910 11.147  36.241  1.000 62.670  ? 55  ARG III CZ  1 
ATOM 14071 N NH1 . ARG I 2 55  ? 110.825 11.856  37.352  1.000 59.280  ? 55  ARG III NH1 1 
ATOM 14072 N NH2 . ARG I 2 55  ? 111.356 9.908   36.312  1.000 67.860  ? 55  ARG III NH2 1 
ATOM 14073 N N   . PRO I 2 56  ? 112.550 17.451  37.517  1.000 51.060  ? 56  PRO III N   1 
ATOM 14074 C CA  . PRO I 2 56  ? 112.525 17.942  38.894  1.000 56.610  ? 56  PRO III CA  1 
ATOM 14075 C C   . PRO I 2 56  ? 111.474 17.114  39.642  1.000 60.870  ? 56  PRO III C   1 
ATOM 14076 O O   . PRO I 2 56  ? 110.668 16.527  38.984  1.000 56.390  ? 56  PRO III O   1 
ATOM 14077 C CB  . PRO I 2 56  ? 112.151 19.417  38.738  1.000 63.660  ? 56  PRO III CB  1 
ATOM 14078 C CG  . PRO I 2 56  ? 111.383 19.491  37.394  1.000 60.870  ? 56  PRO III CG  1 
ATOM 14079 C CD  . PRO I 2 56  ? 111.892 18.344  36.545  1.000 54.110  ? 56  PRO III CD  1 
ATOM 14080 N N   . SER I 2 57  ? 111.531 16.982  40.969  1.000 72.400  ? 57  SER III N   1 
ATOM 14081 C CA  . SER I 2 57  ? 110.552 16.106  41.675  1.000 80.620  ? 57  SER III CA  1 
ATOM 14082 C C   . SER I 2 57  ? 109.180 16.770  41.560  1.000 87.510  ? 57  SER III C   1 
ATOM 14083 O O   . SER I 2 57  ? 109.119 17.992  41.709  1.000 92.210  ? 57  SER III O   1 
ATOM 14084 C CB  . SER I 2 57  ? 110.951 15.784  43.079  1.000 80.610  ? 57  SER III CB  1 
ATOM 14085 O OG  . SER I 2 57  ? 111.830 14.668  43.050  1.000 75.590  ? 57  SER III OG  1 
ATOM 14086 N N   . GLY I 2 58  ? 108.136 16.008  41.215  1.000 90.330  ? 58  GLY III N   1 
ATOM 14087 C CA  . GLY I 2 58  ? 106.767 16.531  41.004  1.000 91.750  ? 58  GLY III CA  1 
ATOM 14088 C C   . GLY I 2 58  ? 106.354 16.454  39.546  1.000 90.050  ? 58  GLY III C   1 
ATOM 14089 O O   . GLY I 2 58  ? 105.153 16.561  39.253  1.000 94.580  ? 58  GLY III O   1 
ATOM 14090 N N   . VAL I 2 59  ? 107.300 16.173  38.651  1.000 81.580  ? 59  VAL III N   1 
ATOM 14091 C CA  . VAL I 2 59  ? 107.025 15.808  37.230  1.000 70.510  ? 59  VAL III CA  1 
ATOM 14092 C C   . VAL I 2 59  ? 106.960 14.289  37.143  1.000 61.900  ? 59  VAL III C   1 
ATOM 14093 O O   . VAL I 2 59  ? 107.921 13.592  37.459  1.000 56.010  ? 59  VAL III O   1 
ATOM 14094 C CB  . VAL I 2 59  ? 108.076 16.396  36.278  1.000 71.800  ? 59  VAL III CB  1 
ATOM 14095 C CG1 . VAL I 2 59  ? 107.815 16.005  34.834  1.000 75.550  ? 59  VAL III CG1 1 
ATOM 14096 C CG2 . VAL I 2 59  ? 108.150 17.909  36.424  1.000 74.240  ? 59  VAL III CG2 1 
ATOM 14097 N N   . PRO I 2 60  ? 105.800 13.742  36.734  1.000 64.440  ? 60  PRO III N   1 
ATOM 14098 C CA  . PRO I 2 60  ? 105.650 12.299  36.544  1.000 69.150  ? 60  PRO III CA  1 
ATOM 14099 C C   . PRO I 2 60  ? 106.713 11.606  35.666  1.000 67.580  ? 60  PRO III C   1 
ATOM 14100 O O   . PRO I 2 60  ? 107.197 12.198  34.739  1.000 60.060  ? 60  PRO III O   1 
ATOM 14101 C CB  . PRO I 2 60  ? 104.280 12.193  35.846  1.000 74.300  ? 60  PRO III CB  1 
ATOM 14102 C CG  . PRO I 2 60  ? 103.510 13.409  36.317  1.000 69.980  ? 60  PRO III CG  1 
ATOM 14103 C CD  . PRO I 2 60  ? 104.557 14.491  36.487  1.000 67.400  ? 60  PRO III CD  1 
ATOM 14104 N N   . ASP I 2 61  ? 106.966 10.333  35.973  1.000 64.850  ? 61  ASP III N   1 
ATOM 14105 C CA  . ASP I 2 61  ? 107.681 9.325   35.155  1.000 68.040  ? 61  ASP III CA  1 
ATOM 14106 C C   . ASP I 2 61  ? 107.387 9.420   33.653  1.000 60.020  ? 61  ASP III C   1 
ATOM 14107 O O   . ASP I 2 61  ? 108.296 9.127   32.867  1.000 49.730  ? 61  ASP III O   1 
ATOM 14108 C CB  . ASP I 2 61  ? 107.281 7.931   35.622  1.000 76.610  ? 61  ASP III CB  1 
ATOM 14109 C CG  . ASP I 2 61  ? 108.346 6.882   35.397  1.000 85.690  ? 61  ASP III CG  1 
ATOM 14110 O OD1 . ASP I 2 61  ? 109.534 7.250   35.198  1.000 94.720  ? 61  ASP III OD1 1 
ATOM 14111 O OD2 . ASP I 2 61  ? 107.980 5.696   35.435  1.000 88.930  ? 61  ASP III OD2 1 
ATOM 14112 N N   . ARG I 2 62  ? 106.150 9.751   33.290  1.000 64.820  ? 62  ARG III N   1 
ATOM 14113 C CA  . ARG I 2 62  ? 105.640 9.775   31.884  1.000 70.580  ? 62  ARG III CA  1 
ATOM 14114 C C   . ARG I 2 62  ? 106.546 10.663  31.017  1.000 70.470  ? 62  ARG III C   1 
ATOM 14115 O O   . ARG I 2 62  ? 106.937 10.244  29.891  1.000 63.930  ? 62  ARG III O   1 
ATOM 14116 C CB  . ARG I 2 62  ? 104.203 10.314  31.829  1.000 74.290  ? 62  ARG III CB  1 
ATOM 14117 C CG  . ARG I 2 62  ? 103.289 9.801   32.934  1.000 80.670  ? 62  ARG III CG  1 
ATOM 14118 C CD  . ARG I 2 62  ? 101.817 10.099  32.701  1.000 82.360  ? 62  ARG III CD  1 
ATOM 14119 N NE  . ARG I 2 62  ? 101.597 11.361  31.995  1.000 73.290  ? 62  ARG III NE  1 
ATOM 14120 C CZ  . ARG I 2 62  ? 100.883 12.385  32.451  1.000 70.060  ? 62  ARG III CZ  1 
ATOM 14121 N NH1 . ARG I 2 62  ? 100.199 12.278  33.580  1.000 68.230  ? 62  ARG III NH1 1 
ATOM 14122 N NH2 . ARG I 2 62  ? 100.754 13.470  31.710  1.000 72.110  ? 62  ARG III NH2 1 
ATOM 14123 N N   . PHE I 2 63  ? 106.859 11.852  31.543  1.000 64.560  ? 63  PHE III N   1 
ATOM 14124 C CA  . PHE I 2 63  ? 107.709 12.882  30.894  1.000 59.360  ? 63  PHE III CA  1 
ATOM 14125 C C   . PHE I 2 63  ? 109.171 12.433  30.906  1.000 57.220  ? 63  PHE III C   1 
ATOM 14126 O O   . PHE I 2 63  ? 109.715 12.067  31.959  1.000 60.540  ? 63  PHE III O   1 
ATOM 14127 C CB  . PHE I 2 63  ? 107.534 14.217  31.612  1.000 62.170  ? 63  PHE III CB  1 
ATOM 14128 C CG  . PHE I 2 63  ? 106.148 14.798  31.512  1.000 62.340  ? 63  PHE III CG  1 
ATOM 14129 C CD1 . PHE I 2 63  ? 105.766 15.518  30.392  1.000 64.240  ? 63  PHE III CD1 1 
ATOM 14130 C CD2 . PHE I 2 63  ? 105.235 14.641  32.538  1.000 60.000  ? 63  PHE III CD2 1 
ATOM 14131 C CE1 . PHE I 2 63  ? 104.495 16.061  30.289  1.000 65.420  ? 63  PHE III CE1 1 
ATOM 14132 C CE2 . PHE I 2 63  ? 103.958 15.170  32.432  1.000 63.330  ? 63  PHE III CE2 1 
ATOM 14133 C CZ  . PHE I 2 63  ? 103.594 15.895  31.315  1.000 65.790  ? 63  PHE III CZ  1 
ATOM 14134 N N   . SER I 2 64  ? 109.803 12.479  29.741  1.000 55.970  ? 64  SER III N   1 
ATOM 14135 C CA  . SER I 2 64  ? 111.217 12.079  29.538  1.000 55.370  ? 64  SER III CA  1 
ATOM 14136 C C   . SER I 2 64  ? 111.837 12.895  28.392  1.000 56.370  ? 64  SER III C   1 
ATOM 14137 O O   . SER I 2 64  ? 111.079 13.521  27.623  1.000 56.820  ? 64  SER III O   1 
ATOM 14138 C CB  . SER I 2 64  ? 111.290 10.625  29.236  1.000 51.500  ? 64  SER III CB  1 
ATOM 14139 O OG  . SER I 2 64  ? 111.044 10.419  27.853  1.000 52.680  ? 64  SER III OG  1 
ATOM 14140 N N   . GLY I 2 65  ? 113.163 12.863  28.264  1.000 58.080  ? 65  GLY III N   1 
ATOM 14141 C CA  . GLY I 2 65  ? 113.876 13.485  27.143  1.000 58.430  ? 65  GLY III CA  1 
ATOM 14142 C C   . GLY I 2 65  ? 114.904 12.545  26.558  1.000 58.640  ? 65  GLY III C   1 
ATOM 14143 O O   . GLY I 2 65  ? 115.282 11.566  27.226  1.000 64.200  ? 65  GLY III O   1 
ATOM 14144 N N   . SER I 2 66  ? 115.394 12.885  25.376  1.000 56.650  ? 66  SER III N   1 
ATOM 14145 C CA  . SER I 2 66  ? 116.601 12.298  24.753  1.000 54.390  ? 66  SER III CA  1 
ATOM 14146 C C   . SER I 2 66  ? 117.422 13.434  24.140  1.000 52.150  ? 66  SER III C   1 
ATOM 14147 O O   . SER I 2 66  ? 116.813 14.386  23.598  1.000 54.860  ? 66  SER III O   1 
ATOM 14148 C CB  . SER I 2 66  ? 116.224 11.266  23.733  1.000 57.660  ? 66  SER III CB  1 
ATOM 14149 O OG  . SER I 2 66  ? 115.946 11.869  22.471  1.000 63.080  ? 66  SER III OG  1 
ATOM 14150 N N   . LYS I 2 67  ? 118.749 13.334  24.243  1.000 48.670  ? 67  LYS III N   1 
ATOM 14151 C CA  . LYS I 2 67  ? 119.730 14.219  23.561  1.000 51.110  ? 67  LYS III CA  1 
ATOM 14152 C C   . LYS I 2 67  ? 120.509 13.343  22.586  1.000 53.800  ? 67  LYS III C   1 
ATOM 14153 O O   . LYS I 2 67  ? 120.994 12.288  22.999  1.000 70.950  ? 67  LYS III O   1 
ATOM 14154 C CB  . LYS I 2 67  ? 120.693 14.899  24.546  1.000 49.280  ? 67  LYS III CB  1 
ATOM 14155 C CG  . LYS I 2 67  ? 121.672 15.893  23.930  1.000 49.810  ? 67  LYS III CG  1 
ATOM 14156 C CD  . LYS I 2 67  ? 122.833 16.317  24.803  1.000 50.080  ? 67  LYS III CD  1 
ATOM 14157 C CE  . LYS I 2 67  ? 123.306 17.746  24.566  1.000 53.420  ? 67  LYS III CE  1 
ATOM 14158 N NZ  . LYS I 2 67  ? 123.958 17.924  23.252  1.000 52.910  ? 67  LYS III NZ  1 
ATOM 14159 N N   . SER I 2 68  ? 120.610 13.764  21.331  1.000 54.350  ? 68  SER III N   1 
ATOM 14160 C CA  . SER I 2 68  ? 121.577 13.223  20.350  1.000 52.270  ? 68  SER III CA  1 
ATOM 14161 C C   . SER I 2 68  ? 122.271 14.414  19.688  1.000 52.860  ? 68  SER III C   1 
ATOM 14162 O O   . SER I 2 68  ? 121.624 15.058  18.838  1.000 53.090  ? 68  SER III O   1 
ATOM 14163 C CB  . SER I 2 68  ? 120.871 12.329  19.372  1.000 55.100  ? 68  SER III CB  1 
ATOM 14164 O OG  . SER I 2 68  ? 121.787 11.678  18.510  1.000 61.330  ? 68  SER III OG  1 
ATOM 14165 N N   . GLY I 2 69  ? 123.506 14.721  20.112  1.000 55.340  ? 69  GLY III N   1 
ATOM 14166 C CA  . GLY I 2 69  ? 124.284 15.881  19.638  1.000 58.540  ? 69  GLY III CA  1 
ATOM 14167 C C   . GLY I 2 69  ? 123.446 17.157  19.650  1.000 60.200  ? 69  GLY III C   1 
ATOM 14168 O O   . GLY I 2 69  ? 122.890 17.510  20.719  1.000 49.990  ? 69  GLY III O   1 
ATOM 14169 N N   . THR I 2 70  ? 123.306 17.806  18.491  1.000 59.350  ? 70  THR III N   1 
ATOM 14170 C CA  . THR I 2 70  ? 122.735 19.173  18.350  1.000 63.950  ? 70  THR III CA  1 
ATOM 14171 C C   . THR I 2 70  ? 121.193 19.154  18.410  1.000 60.840  ? 70  THR III C   1 
ATOM 14172 O O   . THR I 2 70  ? 120.584 20.245  18.353  1.000 62.180  ? 70  THR III O   1 
ATOM 14173 C CB  . THR I 2 70  ? 123.280 19.834  17.074  1.000 70.160  ? 70  THR III CB  1 
ATOM 14174 O OG1 . THR I 2 70  ? 122.619 19.267  15.946  1.000 71.060  ? 70  THR III OG1 1 
ATOM 14175 C CG2 . THR I 2 70  ? 124.778 19.673  16.893  1.000 72.590  ? 70  THR III CG2 1 
ATOM 14176 N N   . SER I 2 71  ? 120.565 17.981  18.537  1.000 59.830  ? 71  SER III N   1 
ATOM 14177 C CA  . SER I 2 71  ? 119.089 17.866  18.629  1.000 64.160  ? 71  SER III CA  1 
ATOM 14178 C C   . SER I 2 71  ? 118.716 17.162  19.927  1.000 65.040  ? 71  SER III C   1 
ATOM 14179 O O   . SER I 2 71  ? 119.450 16.252  20.362  1.000 65.750  ? 71  SER III O   1 
ATOM 14180 C CB  . SER I 2 71  ? 118.494 17.144  17.466  1.000 65.080  ? 71  SER III CB  1 
ATOM 14181 O OG  . SER I 2 71  ? 118.848 17.769  16.248  1.000 71.260  ? 71  SER III OG  1 
ATOM 14182 N N   . VAL I 2 72  ? 117.611 17.614  20.508  1.000 62.590  ? 72  VAL III N   1 
ATOM 14183 C CA  . VAL I 2 72  ? 116.996 17.064  21.743  1.000 58.600  ? 72  VAL III CA  1 
ATOM 14184 C C   . VAL I 2 72  ? 115.527 16.833  21.415  1.000 59.990  ? 72  VAL III C   1 
ATOM 14185 O O   . VAL I 2 72  ? 115.005 17.550  20.549  1.000 57.860  ? 72  VAL III O   1 
ATOM 14186 C CB  . VAL I 2 72  ? 117.165 18.044  22.915  1.000 61.780  ? 72  VAL III CB  1 
ATOM 14187 C CG1 . VAL I 2 72  ? 116.192 17.754  24.047  1.000 69.960  ? 72  VAL III CG1 1 
ATOM 14188 C CG2 . VAL I 2 72  ? 118.597 18.066  23.403  1.000 62.930  ? 72  VAL III CG2 1 
ATOM 14189 N N   . SER I 2 73  ? 114.894 15.880  22.086  1.000 63.550  ? 73  SER III N   1 
ATOM 14190 C CA  . SER I 2 73  ? 113.424 15.695  22.049  1.000 62.870  ? 73  SER III CA  1 
ATOM 14191 C C   . SER I 2 73  ? 112.866 15.593  23.476  1.000 60.650  ? 73  SER III C   1 
ATOM 14192 O O   . SER I 2 73  ? 113.626 15.234  24.408  1.000 63.470  ? 73  SER III O   1 
ATOM 14193 C CB  . SER I 2 73  ? 113.063 14.510  21.208  1.000 65.470  ? 73  SER III CB  1 
ATOM 14194 O OG  . SER I 2 73  ? 113.614 13.329  21.765  1.000 72.210  ? 73  SER III OG  1 
ATOM 14195 N N   . LEU I 2 74  ? 111.601 15.986  23.628  1.000 55.040  ? 74  LEU III N   1 
ATOM 14196 C CA  . LEU I 2 74  ? 110.754 15.779  24.827  1.000 52.650  ? 74  LEU III CA  1 
ATOM 14197 C C   . LEU I 2 74  ? 109.749 14.683  24.484  1.000 53.920  ? 74  LEU III C   1 
ATOM 14198 O O   . LEU I 2 74  ? 109.199 14.744  23.379  1.000 56.750  ? 74  LEU III O   1 
ATOM 14199 C CB  . LEU I 2 74  ? 110.043 17.096  25.173  1.000 53.240  ? 74  LEU III CB  1 
ATOM 14200 C CG  . LEU I 2 74  ? 108.903 16.973  26.188  1.000 53.230  ? 74  LEU III CG  1 
ATOM 14201 C CD1 . LEU I 2 74  ? 109.421 16.499  27.534  1.000 55.010  ? 74  LEU III CD1 1 
ATOM 14202 C CD2 . LEU I 2 74  ? 108.169 18.288  26.358  1.000 50.370  ? 74  LEU III CD2 1 
ATOM 14203 N N   . ALA I 2 75  ? 109.531 13.739  25.399  1.000 58.650  ? 75  ALA III N   1 
ATOM 14204 C CA  . ALA I 2 75  ? 108.655 12.560  25.211  1.000 60.080  ? 75  ALA III CA  1 
ATOM 14205 C C   . ALA I 2 75  ? 107.595 12.521  26.313  1.000 67.010  ? 75  ALA III C   1 
ATOM 14206 O O   . ALA I 2 75  ? 107.931 12.176  27.476  1.000 75.380  ? 75  ALA III O   1 
ATOM 14207 C CB  . ALA I 2 75  ? 109.476 11.297  25.209  1.000 60.980  ? 75  ALA III CB  1 
ATOM 14208 N N   . ILE I 2 76  ? 106.359 12.868  25.969  1.000 69.150  ? 76  ILE III N   1 
ATOM 14209 C CA  . ILE I 2 76  ? 105.180 12.747  26.872  1.000 64.520  ? 76  ILE III CA  1 
ATOM 14210 C C   . ILE I 2 76  ? 104.501 11.411  26.577  1.000 64.530  ? 76  ILE III C   1 
ATOM 14211 O O   . ILE I 2 76  ? 103.847 11.321  25.531  1.000 72.460  ? 76  ILE III O   1 
ATOM 14212 C CB  . ILE I 2 76  ? 104.211 13.918  26.654  1.000 65.770  ? 76  ILE III CB  1 
ATOM 14213 C CG1 . ILE I 2 76  ? 104.933 15.266  26.666  1.000 68.920  ? 76  ILE III CG1 1 
ATOM 14214 C CG2 . ILE I 2 76  ? 103.077 13.859  27.670  1.000 73.930  ? 76  ILE III CG2 1 
ATOM 14215 C CD1 . ILE I 2 76  ? 104.068 16.429  26.263  1.000 72.210  ? 76  ILE III CD1 1 
ATOM 14216 N N   . SER I 2 77  ? 104.671 10.416  27.444  1.000 69.150  ? 77  SER III N   1 
ATOM 14217 C CA  . SER I 2 77  ? 103.989 9.100   27.337  1.000 76.080  ? 77  SER III CA  1 
ATOM 14218 C C   . SER I 2 77  ? 102.731 9.127   28.206  1.000 80.270  ? 77  SER III C   1 
ATOM 14219 O O   . SER I 2 77  ? 102.617 10.021  29.065  1.000 81.400  ? 77  SER III O   1 
ATOM 14220 C CB  . SER I 2 77  ? 104.911 7.963   27.705  1.000 77.910  ? 77  SER III CB  1 
ATOM 14221 O OG  . SER I 2 77  ? 105.141 7.933   29.101  1.000 84.790  ? 77  SER III OG  1 
ATOM 14222 N N   . GLY I 2 78  ? 101.807 8.192   27.969  1.000 81.390  ? 78  GLY III N   1 
ATOM 14223 C CA  . GLY I 2 78  ? 100.517 8.108   28.692  1.000 77.500  ? 78  GLY III CA  1 
ATOM 14224 C C   . GLY I 2 78  ? 99.797  9.434   28.638  1.000 73.430  ? 78  GLY III C   1 
ATOM 14225 O O   . GLY I 2 78  ? 99.411  9.961   29.711  1.000 67.900  ? 78  GLY III O   1 
ATOM 14226 N N   . LEU I 2 79  ? 99.627  9.959   27.426  1.000 71.820  ? 79  LEU III N   1 
ATOM 14227 C CA  . LEU I 2 79  ? 99.111  11.330  27.193  1.000 78.160  ? 79  LEU III CA  1 
ATOM 14228 C C   . LEU I 2 79  ? 97.754  11.495  27.879  1.000 70.120  ? 79  LEU III C   1 
ATOM 14229 O O   . LEU I 2 79  ? 96.948  10.578  27.795  1.000 62.920  ? 79  LEU III O   1 
ATOM 14230 C CB  . LEU I 2 79  ? 98.996  11.573  25.687  1.000 83.990  ? 79  LEU III CB  1 
ATOM 14231 C CG  . LEU I 2 79  ? 98.629  13.006  25.303  1.000 83.060  ? 79  LEU III CG  1 
ATOM 14232 C CD1 . LEU I 2 79  ? 99.742  13.966  25.664  1.000 76.650  ? 79  LEU III CD1 1 
ATOM 14233 C CD2 . LEU I 2 79  ? 98.287  13.117  23.829  1.000 91.060  ? 79  LEU III CD2 1 
ATOM 14234 N N   . GLN I 2 80  ? 97.525  12.633  28.539  1.000 75.430  ? 80  GLN III N   1 
ATOM 14235 C CA  . GLN I 2 80  ? 96.229  12.986  29.191  1.000 84.230  ? 80  GLN III CA  1 
ATOM 14236 C C   . GLN I 2 80  ? 95.803  14.380  28.723  1.000 88.340  ? 80  GLN III C   1 
ATOM 14237 O O   . GLN I 2 80  ? 96.639  15.073  28.118  1.000 87.730  ? 80  GLN III O   1 
ATOM 14238 C CB  . GLN I 2 80  ? 96.348  12.908  30.714  1.000 84.370  ? 80  GLN III CB  1 
ATOM 14239 C CG  . GLN I 2 80  ? 96.653  11.497  31.201  1.000 86.940  ? 80  GLN III CG  1 
ATOM 14240 C CD  . GLN I 2 80  ? 96.669  11.375  32.699  1.000 85.250  ? 80  GLN III CD  1 
ATOM 14241 O OE1 . GLN I 2 80  ? 96.210  12.262  33.412  1.000 87.890  ? 80  GLN III OE1 1 
ATOM 14242 N NE2 . GLN I 2 80  ? 97.270  10.297  33.174  1.000 76.180  ? 80  GLN III NE2 1 
ATOM 14243 N N   . SER I 2 81  ? 94.546  14.759  28.982  1.000 87.570  ? 81  SER III N   1 
ATOM 14244 C CA  . SER I 2 81  ? 93.962  16.050  28.546  1.000 83.780  ? 81  SER III CA  1 
ATOM 14245 C C   . SER I 2 81  ? 94.586  17.178  29.360  1.000 85.630  ? 81  SER III C   1 
ATOM 14246 O O   . SER I 2 81  ? 94.732  18.274  28.806  1.000 88.520  ? 81  SER III O   1 
ATOM 14247 C CB  . SER I 2 81  ? 92.461  16.053  28.649  1.000 85.970  ? 81  SER III CB  1 
ATOM 14248 O OG  . SER I 2 81  ? 92.012  15.861  29.988  1.000 89.140  ? 81  SER III OG  1 
ATOM 14249 N N   . GLU I 2 82  ? 94.977  16.893  30.606  1.000 90.060  ? 82  GLU III N   1 
ATOM 14250 C CA  . GLU I 2 82  ? 95.625  17.860  31.539  1.000 90.160  ? 82  GLU III CA  1 
ATOM 14251 C C   . GLU I 2 82  ? 97.002  18.279  30.985  1.000 92.770  ? 82  GLU III C   1 
ATOM 14252 O O   . GLU I 2 82  ? 97.583  19.227  31.537  1.000 84.400  ? 82  GLU III O   1 
ATOM 14253 C CB  . GLU I 2 82  ? 95.728  17.262  32.946  1.000 85.250  ? 82  GLU III CB  1 
ATOM 14254 C CG  . GLU I 2 82  ? 94.385  16.961  33.586  1.000 87.890  ? 82  GLU III CG  1 
ATOM 14255 C CD  . GLU I 2 82  ? 93.790  15.591  33.288  1.000 95.720  ? 82  GLU III CD  1 
ATOM 14256 O OE1 . GLU I 2 82  ? 94.360  14.846  32.456  1.000 103.630 ? 82  GLU III OE1 1 
ATOM 14257 O OE2 . GLU I 2 82  ? 92.744  15.275  33.885  1.000 95.830  ? 82  GLU III OE2 1 
ATOM 14258 N N   . ASP I 2 83  ? 97.489  17.607  29.929  1.000 91.900  ? 83  ASP III N   1 
ATOM 14259 C CA  . ASP I 2 83  ? 98.788  17.874  29.246  1.000 81.190  ? 83  ASP III CA  1 
ATOM 14260 C C   . ASP I 2 83  ? 98.621  18.877  28.097  1.000 74.440  ? 83  ASP III C   1 
ATOM 14261 O O   . ASP I 2 83  ? 99.612  19.176  27.424  1.000 64.750  ? 83  ASP III O   1 
ATOM 14262 C CB  . ASP I 2 83  ? 99.416  16.579  28.709  1.000 78.810  ? 83  ASP III CB  1 
ATOM 14263 C CG  . ASP I 2 83  ? 99.875  15.618  29.795  1.000 78.760  ? 83  ASP III CG  1 
ATOM 14264 O OD1 . ASP I 2 83  ? 99.989  16.063  30.957  1.000 77.470  ? 83  ASP III OD1 1 
ATOM 14265 O OD2 . ASP I 2 83  ? 100.132 14.429  29.477  1.000 73.820  ? 83  ASP III OD2 1 
ATOM 14266 N N   . GLU I 2 84  ? 97.401  19.354  27.856  1.000 78.790  ? 84  GLU III N   1 
ATOM 14267 C CA  . GLU I 2 84  ? 97.117  20.333  26.773  1.000 76.420  ? 84  GLU III CA  1 
ATOM 14268 C C   . GLU I 2 84  ? 97.702  21.671  27.224  1.000 68.950  ? 84  GLU III C   1 
ATOM 14269 O O   . GLU I 2 84  ? 97.344  22.131  28.307  1.000 66.590  ? 84  GLU III O   1 
ATOM 14270 C CB  . GLU I 2 84  ? 95.613  20.418  26.473  1.000 85.750  ? 84  GLU III CB  1 
ATOM 14271 C CG  . GLU I 2 84  ? 95.278  20.614  25.004  1.000 93.220  ? 84  GLU III CG  1 
ATOM 14272 C CD  . GLU I 2 84  ? 93.886  20.212  24.559  1.000 95.910  ? 84  GLU III CD  1 
ATOM 14273 O OE1 . GLU I 2 84  ? 93.178  19.537  25.326  1.000 99.980  ? 84  GLU III OE1 1 
ATOM 14274 O OE2 . GLU I 2 84  ? 93.538  20.549  23.422  1.000 94.860  ? 84  GLU III OE2 1 
ATOM 14275 N N   . GLY I 2 85  ? 98.585  22.244  26.410  1.000 64.570  ? 85  GLY III N   1 
ATOM 14276 C CA  . GLY I 2 85  ? 99.321  23.486  26.719  1.000 64.570  ? 85  GLY III CA  1 
ATOM 14277 C C   . GLY I 2 85  ? 100.437 23.714  25.716  1.000 67.680  ? 85  GLY III C   1 
ATOM 14278 O O   . GLY I 2 85  ? 100.530 22.926  24.745  1.000 68.560  ? 85  GLY III O   1 
ATOM 14279 N N   . ASP I 2 86  ? 101.251 24.747  25.950  1.000 75.190  ? 86  ASP III N   1 
ATOM 14280 C CA  . ASP I 2 86  ? 102.442 25.103  25.130  1.000 74.760  ? 86  ASP III CA  1 
ATOM 14281 C C   . ASP I 2 86  ? 103.695 24.531  25.819  1.000 67.580  ? 86  ASP III C   1 
ATOM 14282 O O   . ASP I 2 86  ? 103.799 24.623  27.072  1.000 69.280  ? 86  ASP III O   1 
ATOM 14283 C CB  . ASP I 2 86  ? 102.520 26.621  24.900  1.000 79.060  ? 86  ASP III CB  1 
ATOM 14284 C CG  . ASP I 2 86  ? 101.472 27.199  23.961  1.000 81.620  ? 86  ASP III CG  1 
ATOM 14285 O OD1 . ASP I 2 86  ? 100.595 26.442  23.502  1.000 86.290  ? 86  ASP III OD1 1 
ATOM 14286 O OD2 . ASP I 2 86  ? 101.548 28.408  23.697  1.000 83.840  ? 86  ASP III OD2 1 
ATOM 14287 N N   . TYR I 2 87  ? 104.604 23.937  25.037  1.000 58.300  ? 87  TYR III N   1 
ATOM 14288 C CA  . TYR I 2 87  ? 105.887 23.361  25.514  1.000 58.660  ? 87  TYR III CA  1 
ATOM 14289 C C   . TYR I 2 87  ? 107.026 24.177  24.899  1.000 59.030  ? 87  TYR III C   1 
ATOM 14290 O O   . TYR I 2 87  ? 107.177 24.202  23.666  1.000 63.890  ? 87  TYR III O   1 
ATOM 14291 C CB  . TYR I 2 87  ? 105.930 21.855  25.245  1.000 57.780  ? 87  TYR III CB  1 
ATOM 14292 C CG  . TYR I 2 87  ? 104.950 21.100  26.106  1.000 58.310  ? 87  TYR III CG  1 
ATOM 14293 C CD1 . TYR I 2 87  ? 103.597 21.128  25.821  1.000 60.690  ? 87  TYR III CD1 1 
ATOM 14294 C CD2 . TYR I 2 87  ? 105.348 20.427  27.244  1.000 59.580  ? 87  TYR III CD2 1 
ATOM 14295 C CE1 . TYR I 2 87  ? 102.669 20.476  26.613  1.000 59.420  ? 87  TYR III CE1 1 
ATOM 14296 C CE2 . TYR I 2 87  ? 104.435 19.752  28.040  1.000 61.930  ? 87  TYR III CE2 1 
ATOM 14297 C CZ  . TYR I 2 87  ? 103.091 19.777  27.726  1.000 62.400  ? 87  TYR III CZ  1 
ATOM 14298 O OH  . TYR I 2 87  ? 102.163 19.136  28.507  1.000 65.510  ? 87  TYR III OH  1 
ATOM 14299 N N   . HIS I 2 88  ? 107.837 24.807  25.757  1.000 60.060  ? 88  HIS III N   1 
ATOM 14300 C CA  . HIS I 2 88  ? 108.932 25.698  25.290  1.000 59.290  ? 88  HIS III CA  1 
ATOM 14301 C C   . HIS I 2 88  ? 110.266 25.050  25.655  1.000 53.640  ? 88  HIS III C   1 
ATOM 14302 O O   . HIS I 2 88  ? 110.417 24.647  26.801  1.000 46.060  ? 88  HIS III O   1 
ATOM 14303 C CB  . HIS I 2 88  ? 108.815 27.064  25.966  1.000 62.810  ? 88  HIS III CB  1 
ATOM 14304 C CG  . HIS I 2 88  ? 107.538 27.775  25.679  1.000 62.520  ? 88  HIS III CG  1 
ATOM 14305 N ND1 . HIS I 2 88  ? 107.384 28.594  24.583  1.000 63.080  ? 88  HIS III ND1 1 
ATOM 14306 C CD2 . HIS I 2 88  ? 106.364 27.801  26.341  1.000 65.690  ? 88  HIS III CD2 1 
ATOM 14307 C CE1 . HIS I 2 88  ? 106.167 29.091  24.577  1.000 70.190  ? 88  HIS III CE1 1 
ATOM 14308 N NE2 . HIS I 2 88  ? 105.522 28.617  25.642  1.000 70.630  ? 88  HIS III NE2 1 
ATOM 14309 N N   . CYS I 2 89  ? 111.199 25.007  24.707  1.000 55.010  ? 89  CYS III N   1 
ATOM 14310 C CA  . CYS I 2 89  ? 112.545 24.425  24.928  1.000 52.520  ? 89  CYS III CA  1 
ATOM 14311 C C   . CYS I 2 89  ? 113.509 25.596  24.888  1.000 46.800  ? 89  CYS III C   1 
ATOM 14312 O O   . CYS I 2 89  ? 113.295 26.472  24.062  1.000 52.340  ? 89  CYS III O   1 
ATOM 14313 C CB  . CYS I 2 89  ? 112.822 23.407  23.831  1.000 53.140  ? 89  CYS III CB  1 
ATOM 14314 S SG  . CYS I 2 89  ? 112.659 23.973  22.123  1.000 61.340  ? 89  CYS III SG  1 
ATOM 14315 N N   . ALA I 2 90  ? 114.494 25.625  25.777  1.000 44.160  ? 90  ALA III N   1 
ATOM 14316 C CA  . ALA I 2 90  ? 115.384 26.796  25.870  1.000 44.780  ? 90  ALA III CA  1 
ATOM 14317 C C   . ALA I 2 90  ? 116.807 26.303  26.084  1.000 41.420  ? 90  ALA III C   1 
ATOM 14318 O O   . ALA I 2 90  ? 116.954 25.241  26.669  1.000 39.930  ? 90  ALA III O   1 
ATOM 14319 C CB  . ALA I 2 90  ? 114.930 27.554  27.072  1.000 47.460  ? 90  ALA III CB  1 
ATOM 14320 N N   . ALA I 2 91  ? 117.791 27.102  25.685  1.000 40.210  ? 91  ALA III N   1 
ATOM 14321 C CA  . ALA I 2 91  ? 119.223 26.730  25.804  1.000 42.810  ? 91  ALA III CA  1 
ATOM 14322 C C   . ALA I 2 91  ? 120.104 27.957  25.590  1.000 41.230  ? 91  ALA III C   1 
ATOM 14323 O O   . ALA I 2 91  ? 119.719 28.813  24.785  1.000 36.070  ? 91  ALA III O   1 
ATOM 14324 C CB  . ALA I 2 91  ? 119.577 25.648  24.814  1.000 44.020  ? 91  ALA III CB  1 
ATOM 14325 N N   . TRP I 2 92  ? 121.242 28.034  26.284  1.000 41.980  ? 92  TRP III N   1 
ATOM 14326 C CA  . TRP I 2 92  ? 122.194 29.166  26.136  1.000 42.770  ? 92  TRP III CA  1 
ATOM 14327 C C   . TRP I 2 92  ? 122.879 29.082  24.778  1.000 45.540  ? 92  TRP III C   1 
ATOM 14328 O O   . TRP I 2 92  ? 123.173 27.963  24.351  1.000 49.570  ? 92  TRP III O   1 
ATOM 14329 C CB  . TRP I 2 92  ? 123.222 29.150  27.251  1.000 43.900  ? 92  TRP III CB  1 
ATOM 14330 C CG  . TRP I 2 92  ? 124.214 30.264  27.186  1.000 47.360  ? 92  TRP III CG  1 
ATOM 14331 C CD1 . TRP I 2 92  ? 125.480 30.215  26.684  1.000 47.960  ? 92  TRP III CD1 1 
ATOM 14332 C CD2 . TRP I 2 92  ? 124.038 31.600  27.685  1.000 48.870  ? 92  TRP III CD2 1 
ATOM 14333 N NE1 . TRP I 2 92  ? 126.104 31.422  26.843  1.000 49.060  ? 92  TRP III NE1 1 
ATOM 14334 C CE2 . TRP I 2 92  ? 125.237 32.299  27.438  1.000 46.570  ? 92  TRP III CE2 1 
ATOM 14335 C CE3 . TRP I 2 92  ? 122.987 32.275  28.306  1.000 48.460  ? 92  TRP III CE3 1 
ATOM 14336 C CZ2 . TRP I 2 92  ? 125.409 33.630  27.805  1.000 43.660  ? 92  TRP III CZ2 1 
ATOM 14337 C CZ3 . TRP I 2 92  ? 123.140 33.594  28.656  1.000 45.810  ? 92  TRP III CZ3 1 
ATOM 14338 C CH2 . TRP I 2 92  ? 124.350 34.257  28.413  1.000 44.960  ? 92  TRP III CH2 1 
ATOM 14339 N N   . ASP I 2 93  ? 123.135 30.221  24.127  1.000 49.530  ? 93  ASP III N   1 
ATOM 14340 C CA  . ASP I 2 93  ? 123.920 30.267  22.861  1.000 46.410  ? 93  ASP III CA  1 
ATOM 14341 C C   . ASP I 2 93  ? 125.224 31.021  23.142  1.000 44.530  ? 93  ASP III C   1 
ATOM 14342 O O   . ASP I 2 93  ? 125.146 32.192  23.512  1.000 38.160  ? 93  ASP III O   1 
ATOM 14343 C CB  . ASP I 2 93  ? 123.132 30.867  21.699  1.000 43.790  ? 93  ASP III CB  1 
ATOM 14344 C CG  . ASP I 2 93  ? 123.942 30.825  20.407  1.000 48.230  ? 93  ASP III CG  1 
ATOM 14345 O OD1 . ASP I 2 93  ? 125.057 31.386  20.419  1.000 56.850  ? 93  ASP III OD1 1 
ATOM 14346 O OD2 . ASP I 2 93  ? 123.485 30.213  19.400  1.000 44.420  ? 93  ASP III OD2 1 
ATOM 14347 N N   . ASP I 2 94  ? 126.365 30.348  22.970  1.000 48.160  ? 94  ASP III N   1 
ATOM 14348 C CA  . ASP I 2 94  ? 127.717 30.870  23.290  1.000 50.430  ? 94  ASP III CA  1 
ATOM 14349 C C   . ASP I 2 94  ? 128.109 32.044  22.407  1.000 49.500  ? 94  ASP III C   1 
ATOM 14350 O O   . ASP I 2 94  ? 128.852 32.886  22.890  1.000 51.490  ? 94  ASP III O   1 
ATOM 14351 C CB  . ASP I 2 94  ? 128.790 29.785  23.163  1.000 52.790  ? 94  ASP III CB  1 
ATOM 14352 C CG  . ASP I 2 94  ? 128.773 28.789  24.299  1.000 49.980  ? 94  ASP III CG  1 
ATOM 14353 O OD1 . ASP I 2 94  ? 128.467 29.220  25.428  1.000 50.910  ? 94  ASP III OD1 1 
ATOM 14354 O OD2 . ASP I 2 94  ? 129.073 27.607  24.041  1.000 48.140  ? 94  ASP III OD2 1 
ATOM 14355 N N   . SER I 2 95  ? 127.656 32.058  21.160  1.000 52.280  ? 95  SER III N   1 
ATOM 14356 C CA  . SER I 2 95  ? 128.002 33.118  20.182  1.000 56.360  ? 95  SER III CA  1 
ATOM 14357 C C   . SER I 2 95  ? 127.161 34.379  20.464  1.000 49.100  ? 95  SER III C   1 
ATOM 14358 O O   . SER I 2 95  ? 127.747 35.454  20.501  1.000 45.330  ? 95  SER III O   1 
ATOM 14359 C CB  . SER I 2 95  ? 127.857 32.636  18.742  1.000 61.880  ? 95  SER III CB  1 
ATOM 14360 O OG  . SER I 2 95  ? 126.512 32.297  18.416  1.000 67.570  ? 95  SER III OG  1 
ATOM 14361 N N   . LEU I 2 96  ? 125.862 34.238  20.749  1.000 43.060  ? 96  LEU III N   1 
ATOM 14362 C CA  . LEU I 2 96  ? 124.938 35.381  20.978  1.000 42.220  ? 96  LEU III CA  1 
ATOM 14363 C C   . LEU I 2 96  ? 125.089 35.851  22.429  1.000 43.430  ? 96  LEU III C   1 
ATOM 14364 O O   . LEU I 2 96  ? 124.485 36.856  22.769  1.000 50.060  ? 96  LEU III O   1 
ATOM 14365 C CB  . LEU I 2 96  ? 123.476 35.019  20.716  1.000 43.240  ? 96  LEU III CB  1 
ATOM 14366 C CG  . LEU I 2 96  ? 123.168 34.395  19.353  1.000 48.000  ? 96  LEU III CG  1 
ATOM 14367 C CD1 . LEU I 2 96  ? 121.659 34.200  19.169  1.000 47.250  ? 96  LEU III CD1 1 
ATOM 14368 C CD2 . LEU I 2 96  ? 123.739 35.222  18.211  1.000 50.170  ? 96  LEU III CD2 1 
ATOM 14369 N N   . LYS I 2 97  ? 125.830 35.136  23.264  1.000 44.230  ? 97  LYS III N   1 
ATOM 14370 C CA  . LYS I 2 97  ? 125.900 35.390  24.726  1.000 44.860  ? 97  LYS III CA  1 
ATOM 14371 C C   . LYS I 2 97  ? 124.494 35.722  25.259  1.000 39.600  ? 97  LYS III C   1 
ATOM 14372 O O   . LYS I 2 97  ? 124.283 36.791  25.856  1.000 37.530  ? 97  LYS III O   1 
ATOM 14373 C CB  . LYS I 2 97  ? 126.954 36.461  25.013  1.000 51.330  ? 97  LYS III CB  1 
ATOM 14374 C CG  . LYS I 2 97  ? 128.380 35.992  24.767  1.000 61.110  ? 97  LYS III CG  1 
ATOM 14375 C CD  . LYS I 2 97  ? 129.465 36.822  25.442  1.000 77.330  ? 97  LYS III CD  1 
ATOM 14376 C CE  . LYS I 2 97  ? 130.871 36.470  24.973  1.000 81.510  ? 97  LYS III CE  1 
ATOM 14377 N NZ  . LYS I 2 97  ? 131.870 37.466  25.438  1.000 79.220  ? 97  LYS III NZ  1 
ATOM 14378 N N   . GLY I 2 98  ? 123.559 34.804  25.071  1.000 38.880  ? 98  GLY III N   1 
ATOM 14379 C CA  . GLY I 2 98  ? 122.191 34.944  25.594  1.000 40.670  ? 98  GLY III CA  1 
ATOM 14380 C C   . GLY I 2 98  ? 121.431 33.635  25.567  1.000 41.870  ? 98  GLY III C   1 
ATOM 14381 O O   . GLY I 2 98  ? 121.952 32.647  25.002  1.000 48.430  ? 98  GLY III O   1 
ATOM 14382 N N   . TRP I 2 99  ? 120.239 33.622  26.162  1.000 40.610  ? 99  TRP III N   1 
ATOM 14383 C CA  . TRP I 2 99  ? 119.316 32.468  26.098  1.000 41.590  ? 99  TRP III CA  1 
ATOM 14384 C C   . TRP I 2 99  ? 118.521 32.551  24.804  1.000 44.310  ? 99  TRP III C   1 
ATOM 14385 O O   . TRP I 2 99  ? 117.949 33.622  24.534  1.000 50.660  ? 99  TRP III O   1 
ATOM 14386 C CB  . TRP I 2 99  ? 118.407 32.451  27.323  1.000 43.890  ? 99  TRP III CB  1 
ATOM 14387 C CG  . TRP I 2 99  ? 119.144 32.140  28.580  1.000 47.350  ? 99  TRP III CG  1 
ATOM 14388 C CD1 . TRP I 2 99  ? 119.616 33.027  29.494  1.000 50.940  ? 99  TRP III CD1 1 
ATOM 14389 C CD2 . TRP I 2 99  ? 119.521 30.838  29.041  1.000 49.400  ? 99  TRP III CD2 1 
ATOM 14390 N NE1 . TRP I 2 99  ? 120.262 32.363  30.501  1.000 54.530  ? 99  TRP III NE1 1 
ATOM 14391 C CE2 . TRP I 2 99  ? 120.217 31.017  30.248  1.000 51.590  ? 99  TRP III CE2 1 
ATOM 14392 C CE3 . TRP I 2 99  ? 119.328 29.543  28.564  1.000 55.020  ? 99  TRP III CE3 1 
ATOM 14393 C CZ2 . TRP I 2 99  ? 120.710 29.946  30.985  1.000 53.880  ? 99  TRP III CZ2 1 
ATOM 14394 C CZ3 . TRP I 2 99  ? 119.824 28.483  29.286  1.000 57.470  ? 99  TRP III CZ3 1 
ATOM 14395 C CH2 . TRP I 2 99  ? 120.509 28.685  30.480  1.000 55.590  ? 99  TRP III CH2 1 
ATOM 14396 N N   . VAL I 2 100 ? 118.500 31.460  24.039  1.000 46.710  ? 100 VAL III N   1 
ATOM 14397 C CA  . VAL I 2 100 ? 117.578 31.268  22.879  1.000 49.590  ? 100 VAL III CA  1 
ATOM 14398 C C   . VAL I 2 100 ? 116.453 30.304  23.282  1.000 44.490  ? 100 VAL III C   1 
ATOM 14399 O O   . VAL I 2 100 ? 116.714 29.363  24.059  1.000 43.020  ? 100 VAL III O   1 
ATOM 14400 C CB  . VAL I 2 100 ? 118.357 30.796  21.634  1.000 54.410  ? 100 VAL III CB  1 
ATOM 14401 C CG1 . VAL I 2 100 ? 119.445 31.802  21.277  1.000 56.530  ? 100 VAL III CG1 1 
ATOM 14402 C CG2 . VAL I 2 100 ? 118.963 29.403  21.801  1.000 54.430  ? 100 VAL III CG2 1 
ATOM 14403 N N   . PHE I 2 101 ? 115.234 30.572  22.822  1.000 43.060  ? 101 PHE III N   1 
ATOM 14404 C CA  . PHE I 2 101 ? 114.048 29.696  22.984  1.000 47.350  ? 101 PHE III CA  1 
ATOM 14405 C C   . PHE I 2 101 ? 113.642 29.193  21.599  1.000 48.620  ? 101 PHE III C   1 
ATOM 14406 O O   . PHE I 2 101 ? 114.190 29.680  20.597  1.000 47.830  ? 101 PHE III O   1 
ATOM 14407 C CB  . PHE I 2 101 ? 112.882 30.433  23.650  1.000 47.670  ? 101 PHE III CB  1 
ATOM 14408 C CG  . PHE I 2 101 ? 113.069 30.698  25.122  1.000 47.350  ? 101 PHE III CG  1 
ATOM 14409 C CD1 . PHE I 2 101 ? 113.874 31.736  25.567  1.000 45.420  ? 101 PHE III CD1 1 
ATOM 14410 C CD2 . PHE I 2 101 ? 112.450 29.895  26.071  1.000 48.450  ? 101 PHE III CD2 1 
ATOM 14411 C CE1 . PHE I 2 101 ? 114.038 31.980  26.920  1.000 44.410  ? 101 PHE III CE1 1 
ATOM 14412 C CE2 . PHE I 2 101 ? 112.629 30.126  27.428  1.000 47.480  ? 101 PHE III CE2 1 
ATOM 14413 C CZ  . PHE I 2 101 ? 113.417 31.172  27.848  1.000 48.000  ? 101 PHE III CZ  1 
ATOM 14414 N N   . GLY I 2 102 ? 112.752 28.206  21.569  1.000 51.010  ? 102 GLY III N   1 
ATOM 14415 C CA  . GLY I 2 102 ? 112.050 27.763  20.358  1.000 53.150  ? 102 GLY III CA  1 
ATOM 14416 C C   . GLY I 2 102 ? 110.799 28.600  20.170  1.000 51.480  ? 102 GLY III C   1 
ATOM 14417 O O   . GLY I 2 102 ? 110.625 29.578  20.927  1.000 48.630  ? 102 GLY III O   1 
ATOM 14418 N N   . GLY I 2 103 ? 109.975 28.245  19.182  1.000 49.940  ? 103 GLY III N   1 
ATOM 14419 C CA  . GLY I 2 103 ? 108.723 28.957  18.891  1.000 51.310  ? 103 GLY III CA  1 
ATOM 14420 C C   . GLY I 2 103 ? 107.704 28.675  19.973  1.000 49.120  ? 103 GLY III C   1 
ATOM 14421 O O   . GLY I 2 103 ? 106.852 29.516  20.263  1.000 44.730  ? 103 GLY III O   1 
ATOM 14422 N N   . GLY I 2 104 ? 107.825 27.519  20.595  1.000 56.650  ? 104 GLY III N   1 
ATOM 14423 C CA  . GLY I 2 104 ? 106.707 26.931  21.346  1.000 62.930  ? 104 GLY III CA  1 
ATOM 14424 C C   . GLY I 2 104 ? 106.005 25.892  20.494  1.000 65.480  ? 104 GLY III C   1 
ATOM 14425 O O   . GLY I 2 104 ? 106.054 25.984  19.249  1.000 60.550  ? 104 GLY III O   1 
ATOM 14426 N N   . THR I 2 105 ? 105.419 24.909  21.165  1.000 75.010  ? 105 THR III N   1 
ATOM 14427 C CA  . THR I 2 105 ? 104.689 23.770  20.571  1.000 73.900  ? 105 THR III CA  1 
ATOM 14428 C C   . THR I 2 105 ? 103.363 23.672  21.317  1.000 78.170  ? 105 THR III C   1 
ATOM 14429 O O   . THR I 2 105 ? 103.427 23.357  22.520  1.000 71.790  ? 105 THR III O   1 
ATOM 14430 C CB  . THR I 2 105 ? 105.528 22.494  20.685  1.000 72.920  ? 105 THR III CB  1 
ATOM 14431 O OG1 . THR I 2 105 ? 106.758 22.711  19.993  1.000 75.440  ? 105 THR III OG1 1 
ATOM 14432 C CG2 . THR I 2 105 ? 104.828 21.272  20.127  1.000 76.030  ? 105 THR III CG2 1 
ATOM 14433 N N   . LYS I 2 106 ? 102.234 23.990  20.672  1.000 87.890  ? 106 LYS III N   1 
ATOM 14434 C CA  . LYS I 2 106 ? 100.898 23.743  21.275  1.000 87.320  ? 106 LYS III CA  1 
ATOM 14435 C C   . LYS I 2 106 ? 100.578 22.260  21.046  1.000 83.990  ? 106 LYS III C   1 
ATOM 14436 O O   . LYS I 2 106 ? 100.457 21.835  19.869  1.000 69.760  ? 106 LYS III O   1 
ATOM 14437 C CB  . LYS I 2 106 ? 99.795  24.685  20.779  1.000 83.740  ? 106 LYS III CB  1 
ATOM 14438 C CG  . LYS I 2 106 ? 98.546  24.680  21.661  1.000 83.580  ? 106 LYS III CG  1 
ATOM 14439 C CD  . LYS I 2 106 ? 97.465  25.672  21.295  1.000 92.310  ? 106 LYS III CD  1 
ATOM 14440 C CE  . LYS I 2 106 ? 97.858  27.080  21.693  1.000 93.110  ? 106 LYS III CE  1 
ATOM 14441 N NZ  . LYS I 2 106 ? 96.771  28.052  21.422  1.000 90.490  ? 106 LYS III NZ  1 
ATOM 14442 N N   . LEU I 2 107 ? 100.503 21.506  22.153  1.000 77.500  ? 107 LEU III N   1 
ATOM 14443 C CA  . LEU I 2 107 ? 100.063 20.099  22.182  1.000 80.650  ? 107 LEU III CA  1 
ATOM 14444 C C   . LEU I 2 107 ? 98.542  20.084  22.331  1.000 84.180  ? 107 LEU III C   1 
ATOM 14445 O O   . LEU I 2 107 ? 98.063  20.557  23.374  1.000 81.670  ? 107 LEU III O   1 
ATOM 14446 C CB  . LEU I 2 107 ? 100.743 19.411  23.366  1.000 81.200  ? 107 LEU III CB  1 
ATOM 14447 C CG  . LEU I 2 107 ? 100.482 17.906  23.506  1.000 82.110  ? 107 LEU III CG  1 
ATOM 14448 C CD1 . LEU I 2 107 ? 101.151 17.108  22.393  1.000 82.170  ? 107 LEU III CD1 1 
ATOM 14449 C CD2 . LEU I 2 107 ? 100.952 17.407  24.862  1.000 86.150  ? 107 LEU III CD2 1 
ATOM 14450 N N   . THR I 2 108 ? 97.834  19.595  21.306  1.000 82.870  ? 108 THR III N   1 
ATOM 14451 C CA  . THR I 2 108 ? 96.369  19.358  21.328  1.000 85.740  ? 108 THR III CA  1 
ATOM 14452 C C   . THR I 2 108 ? 96.139  17.874  21.637  1.000 86.980  ? 108 THR III C   1 
ATOM 14453 O O   . THR I 2 108 ? 96.864  17.028  21.052  1.000 80.900  ? 108 THR III O   1 
ATOM 14454 C CB  . THR I 2 108 ? 95.729  19.818  20.011  1.000 88.120  ? 108 THR III CB  1 
ATOM 14455 O OG1 . THR I 2 108 ? 96.131  21.168  19.783  1.000 79.320  ? 108 THR III OG1 1 
ATOM 14456 C CG2 . THR I 2 108 ? 94.219  19.745  20.014  1.000 87.530  ? 108 THR III CG2 1 
ATOM 14457 N N   . VAL I 2 109 ? 95.206  17.582  22.549  1.000 83.970  ? 109 VAL III N   1 
ATOM 14458 C CA  . VAL I 2 109 ? 94.807  16.197  22.943  1.000 95.180  ? 109 VAL III CA  1 
ATOM 14459 C C   . VAL I 2 109 ? 93.416  15.916  22.377  1.000 92.860  ? 109 VAL III C   1 
ATOM 14460 O O   . VAL I 2 109 ? 92.486  16.672  22.694  1.000 91.340  ? 109 VAL III O   1 
ATOM 14461 C CB  . VAL I 2 109 ? 94.827  16.008  24.471  1.000 111.270 ? 109 VAL III CB  1 
ATOM 14462 C CG1 . VAL I 2 109 ? 94.675  14.547  24.871  1.000 118.080 ? 109 VAL III CG1 1 
ATOM 14463 C CG2 . VAL I 2 109 ? 96.076  16.601  25.088  1.000 115.190 ? 109 VAL III CG2 1 
ATOM 14464 N N   . LEU I 2 110 ? 93.295  14.851  21.586  1.000 95.710  ? 110 LEU III N   1 
ATOM 14465 C CA  . LEU I 2 110 ? 92.087  14.518  20.788  1.000 109.300 ? 110 LEU III CA  1 
ATOM 14466 C C   . LEU I 2 110 ? 91.324  13.409  21.517  1.000 117.150 ? 110 LEU III C   1 
ATOM 14467 O O   . LEU I 2 110 ? 91.943  12.796  22.417  1.000 132.960 ? 110 LEU III O   1 
ATOM 14468 C CB  . LEU I 2 110 ? 92.561  14.082  19.399  1.000 108.740 ? 110 LEU III CB  1 
ATOM 14469 C CG  . LEU I 2 110 ? 93.534  15.048  18.720  1.000 110.380 ? 110 LEU III CG  1 
ATOM 14470 C CD1 . LEU I 2 110 ? 94.080  14.444  17.433  1.000 107.310 ? 110 LEU III CD1 1 
ATOM 14471 C CD2 . LEU I 2 110 ? 92.864  16.392  18.448  1.000 98.320  ? 110 LEU III CD2 1 
ATOM 14472 N N   . GLY I 2 111 ? 90.059  13.162  21.151  1.000 114.590 ? 111 GLY III N   1 
ATOM 14473 C CA  . GLY I 2 111 ? 89.222  12.089  21.718  1.000 105.650 ? 111 GLY III CA  1 
ATOM 14474 C C   . GLY I 2 111 ? 87.875  12.602  22.200  1.000 110.030 ? 111 GLY III C   1 
ATOM 14475 O O   . GLY I 2 111 ? 86.891  11.893  21.969  1.000 100.750 ? 111 GLY III O   1 
ATOM 14476 N N   . ALA I 2 112 ? 87.842  13.786  22.832  1.000 124.400 ? 112 ALA III N   1 
ATOM 14477 C CA  . ALA I 2 112 ? 86.758  14.256  23.738  1.000 125.950 ? 112 ALA III CA  1 
ATOM 14478 C C   . ALA I 2 112 ? 85.511  14.661  22.951  1.000 125.210 ? 112 ALA III C   1 
ATOM 14479 O O   . ALA I 2 112 ? 85.538  15.659  22.239  1.000 132.830 ? 112 ALA III O   1 
ATOM 14480 C CB  . ALA I 2 112 ? 87.257  15.410  24.588  1.000 109.540 ? 112 ALA III CB  1 
ATOM 14481 N N   . PRO I 2 113 ? 84.364  13.943  23.078  1.000 117.440 ? 113 PRO III N   1 
ATOM 14482 C CA  . PRO I 2 113 ? 83.122  14.374  22.427  1.000 104.610 ? 113 PRO III CA  1 
ATOM 14483 C C   . PRO I 2 113 ? 82.505  15.566  23.191  1.000 89.050  ? 113 PRO III C   1 
ATOM 14484 O O   . PRO I 2 113 ? 81.627  16.228  22.672  1.000 73.010  ? 113 PRO III O   1 
ATOM 14485 C CB  . PRO I 2 113 ? 82.266  13.090  22.441  1.000 100.590 ? 113 PRO III CB  1 
ATOM 14486 C CG  . PRO I 2 113 ? 82.727  12.358  23.687  1.000 105.050 ? 113 PRO III CG  1 
ATOM 14487 C CD  . PRO I 2 113 ? 84.193  12.706  23.867  1.000 107.980 ? 113 PRO III CD  1 
ATOM 14488 N N   . ASN I 2 132 ? 72.764  56.349  24.055  1.000 79.790  ? 132 ASN III N   1 
ATOM 14489 C CA  . ASN I 2 132 ? 71.712  55.318  23.841  1.000 85.720  ? 132 ASN III CA  1 
ATOM 14490 C C   . ASN I 2 132 ? 72.343  54.069  23.188  1.000 91.320  ? 132 ASN III C   1 
ATOM 14491 O O   . ASN I 2 132 ? 71.804  53.603  22.165  1.000 99.580  ? 132 ASN III O   1 
ATOM 14492 C CB  . ASN I 2 132 ? 70.540  55.909  23.044  1.000 77.120  ? 132 ASN III CB  1 
ATOM 14493 N N   . LYS I 2 133 ? 73.442  53.547  23.756  1.000 93.340  ? 133 LYS III N   1 
ATOM 14494 C CA  . LYS I 2 133 ? 74.197  52.356  23.252  1.000 91.820  ? 133 LYS III CA  1 
ATOM 14495 C C   . LYS I 2 133 ? 73.454  51.067  23.651  1.000 98.120  ? 133 LYS III C   1 
ATOM 14496 O O   . LYS I 2 133 ? 72.996  50.979  24.815  1.000 114.840 ? 133 LYS III O   1 
ATOM 14497 C CB  . LYS I 2 133 ? 75.647  52.362  23.770  1.000 78.940  ? 133 LYS III CB  1 
ATOM 14498 N N   . ALA I 2 134 ? 73.337  50.102  22.727  1.000 103.560 ? 134 ALA III N   1 
ATOM 14499 C CA  . ALA I 2 134 ? 72.820  48.727  22.965  1.000 110.780 ? 134 ALA III CA  1 
ATOM 14500 C C   . ALA I 2 134 ? 73.808  47.720  22.373  1.000 114.800 ? 134 ALA III C   1 
ATOM 14501 O O   . ALA I 2 134 ? 74.035  47.838  21.153  1.000 119.970 ? 134 ALA III O   1 
ATOM 14502 C CB  . ALA I 2 134 ? 71.454  48.557  22.336  1.000 109.410 ? 134 ALA III CB  1 
ATOM 14503 N N   . THR I 2 135 ? 74.370  46.815  23.197  1.000 107.020 ? 135 THR III N   1 
ATOM 14504 C CA  . THR I 2 135 ? 75.365  45.765  22.819  1.000 106.570 ? 135 THR III CA  1 
ATOM 14505 C C   . THR I 2 135 ? 74.888  44.402  23.347  1.000 99.650  ? 135 THR III C   1 
ATOM 14506 O O   . THR I 2 135 ? 74.620  44.325  24.548  1.000 92.570  ? 135 THR III O   1 
ATOM 14507 C CB  . THR I 2 135 ? 76.770  46.138  23.332  1.000 111.310 ? 135 THR III CB  1 
ATOM 14508 O OG1 . THR I 2 135 ? 76.822  46.000  24.750  1.000 107.450 ? 135 THR III OG1 1 
ATOM 14509 C CG2 . THR I 2 135 ? 77.171  47.554  22.975  1.000 112.380 ? 135 THR III CG2 1 
ATOM 14510 N N   . LEU I 2 136 ? 74.815  43.359  22.502  1.000 107.190 ? 136 LEU III N   1 
ATOM 14511 C CA  . LEU I 2 136 ? 74.204  42.034  22.838  1.000 118.680 ? 136 LEU III CA  1 
ATOM 14512 C C   . LEU I 2 136 ? 75.245  40.898  22.741  1.000 127.990 ? 136 LEU III C   1 
ATOM 14513 O O   . LEU I 2 136 ? 76.176  41.010  21.923  1.000 149.980 ? 136 LEU III O   1 
ATOM 14514 C CB  . LEU I 2 136 ? 72.965  41.792  21.956  1.000 117.780 ? 136 LEU III CB  1 
ATOM 14515 C CG  . LEU I 2 136 ? 73.137  41.839  20.434  1.000 118.850 ? 136 LEU III CG  1 
ATOM 14516 C CD1 . LEU I 2 136 ? 73.606  40.503  19.858  1.000 120.670 ? 136 LEU III CD1 1 
ATOM 14517 C CD2 . LEU I 2 136 ? 71.831  42.255  19.773  1.000 103.830 ? 136 LEU III CD2 1 
ATOM 14518 N N   . VAL I 2 137 ? 75.073  39.846  23.558  1.000 113.940 ? 137 VAL III N   1 
ATOM 14519 C CA  . VAL I 2 137 ? 76.063  38.758  23.834  1.000 102.610 ? 137 VAL III CA  1 
ATOM 14520 C C   . VAL I 2 137 ? 75.368  37.421  23.528  1.000 98.440  ? 137 VAL III C   1 
ATOM 14521 O O   . VAL I 2 137 ? 74.218  37.246  23.971  1.000 109.020 ? 137 VAL III O   1 
ATOM 14522 C CB  . VAL I 2 137 ? 76.532  38.832  25.303  1.000 91.880  ? 137 VAL III CB  1 
ATOM 14523 C CG1 . VAL I 2 137 ? 77.235  37.560  25.773  1.000 89.510  ? 137 VAL III CG1 1 
ATOM 14524 C CG2 . VAL I 2 137 ? 77.407  40.057  25.539  1.000 86.030  ? 137 VAL III CG2 1 
ATOM 14525 N N   . CYS I 2 138 ? 76.053  36.493  22.854  1.000 87.310  ? 138 CYS III N   1 
ATOM 14526 C CA  . CYS I 2 138 ? 75.535  35.128  22.539  1.000 86.830  ? 138 CYS III CA  1 
ATOM 14527 C C   . CYS I 2 138 ? 75.968  34.153  23.660  1.000 100.120 ? 138 CYS III C   1 
ATOM 14528 O O   . CYS I 2 138 ? 76.681  33.161  23.389  1.000 95.750  ? 138 CYS III O   1 
ATOM 14529 C CB  . CYS I 2 138 ? 76.034  34.661  21.175  1.000 83.840  ? 138 CYS III CB  1 
ATOM 14530 S SG  . CYS I 2 138 ? 75.415  35.630  19.772  1.000 84.060  ? 138 CYS III SG  1 
ATOM 14531 N N   . LEU I 2 139 ? 75.503  34.410  24.888  1.000 118.870 ? 139 LEU III N   1 
ATOM 14532 C CA  . LEU I 2 139 ? 75.734  33.609  26.127  1.000 111.340 ? 139 LEU III CA  1 
ATOM 14533 C C   . LEU I 2 139 ? 77.194  33.675  26.605  1.000 88.930  ? 139 LEU III C   1 
ATOM 14534 O O   . LEU I 2 139 ? 78.030  32.937  26.052  1.000 77.880  ? 139 LEU III O   1 
ATOM 14535 C CB  . LEU I 2 139 ? 75.226  32.168  25.911  1.000 114.320 ? 139 LEU III CB  1 
ATOM 14536 C CG  . LEU I 2 139 ? 73.754  32.012  25.504  1.000 100.110 ? 139 LEU III CG  1 
ATOM 14537 C CD1 . LEU I 2 139 ? 73.402  30.552  25.203  1.000 83.470  ? 139 LEU III CD1 1 
ATOM 14538 C CD2 . LEU I 2 139 ? 72.827  32.587  26.570  1.000 94.680  ? 139 LEU III CD2 1 
ATOM 14539 N N   . VAL I 2 163 ? 78.119  45.457  12.226  1.000 84.270  ? 163 VAL III N   1 
ATOM 14540 C CA  . VAL I 2 163 ? 78.765  44.115  12.399  1.000 94.630  ? 163 VAL III CA  1 
ATOM 14541 C C   . VAL I 2 163 ? 79.836  44.201  13.515  1.000 104.500 ? 163 VAL III C   1 
ATOM 14542 O O   . VAL I 2 163 ? 80.560  45.210  13.536  1.000 113.390 ? 163 VAL III O   1 
ATOM 14543 C CB  . VAL I 2 163 ? 79.337  43.588  11.056  1.000 89.230  ? 163 VAL III CB  1 
ATOM 14544 C CG1 . VAL I 2 163 ? 78.246  43.254  10.037  1.000 74.360  ? 163 VAL III CG1 1 
ATOM 14545 C CG2 . VAL I 2 163 ? 80.379  44.518  10.435  1.000 90.640  ? 163 VAL III CG2 1 
ATOM 14546 N N   . GLU I 2 164 ? 79.956  43.178  14.388  1.000 102.370 ? 164 GLU III N   1 
ATOM 14547 C CA  . GLU I 2 164 ? 80.991  43.079  15.467  1.000 97.830  ? 164 GLU III CA  1 
ATOM 14548 C C   . GLU I 2 164 ? 81.772  41.742  15.399  1.000 100.880 ? 164 GLU III C   1 
ATOM 14549 O O   . GLU I 2 164 ? 81.518  40.948  14.463  1.000 81.490  ? 164 GLU III O   1 
ATOM 14550 C CB  . GLU I 2 164 ? 80.304  43.280  16.817  1.000 85.930  ? 164 GLU III CB  1 
ATOM 14551 N N   . THR I 2 165 ? 82.667  41.484  16.376  1.000 113.110 ? 165 THR III N   1 
ATOM 14552 C CA  . THR I 2 165 ? 83.718  40.408  16.382  1.000 110.620 ? 165 THR III CA  1 
ATOM 14553 C C   . THR I 2 165 ? 83.282  39.145  17.173  1.000 95.290  ? 165 THR III C   1 
ATOM 14554 O O   . THR I 2 165 ? 82.239  39.184  17.865  1.000 78.440  ? 165 THR III O   1 
ATOM 14555 C CB  . THR I 2 165 ? 85.040  41.014  16.885  1.000 100.820 ? 165 THR III CB  1 
ATOM 14556 N N   . THR I 2 166 ? 84.026  38.037  17.048  1.000 93.030  ? 166 THR III N   1 
ATOM 14557 C CA  . THR I 2 166 ? 83.835  36.771  17.824  1.000 97.910  ? 166 THR III CA  1 
ATOM 14558 C C   . THR I 2 166 ? 85.221  36.126  18.027  1.000 107.350 ? 166 THR III C   1 
ATOM 14559 O O   . THR I 2 166 ? 85.929  35.978  17.012  1.000 123.860 ? 166 THR III O   1 
ATOM 14560 C CB  . THR I 2 166 ? 82.806  35.869  17.132  1.000 77.640  ? 166 THR III CB  1 
ATOM 14561 N N   . LYS I 2 167 ? 85.627  35.805  19.275  1.000 108.660 ? 167 LYS III N   1 
ATOM 14562 C CA  . LYS I 2 167 ? 86.964  35.248  19.643  1.000 102.290 ? 167 LYS III CA  1 
ATOM 14563 C C   . LYS I 2 167 ? 86.896  33.720  19.713  1.000 111.160 ? 167 LYS III C   1 
ATOM 14564 O O   . LYS I 2 167 ? 85.913  33.177  20.209  1.000 115.130 ? 167 LYS III O   1 
ATOM 14565 C CB  . LYS I 2 167 ? 87.433  35.798  20.999  1.000 81.330  ? 167 LYS III CB  1 
ATOM 14566 N N   . PRO I 2 168 ? 87.915  32.967  19.223  1.000 116.860 ? 168 PRO III N   1 
ATOM 14567 C CA  . PRO I 2 168 ? 87.986  31.516  19.458  1.000 109.450 ? 168 PRO III CA  1 
ATOM 14568 C C   . PRO I 2 168 ? 88.416  31.136  20.887  1.000 95.040  ? 168 PRO III C   1 
ATOM 14569 O O   . PRO I 2 168 ? 88.821  32.021  21.626  1.000 93.060  ? 168 PRO III O   1 
ATOM 14570 C CB  . PRO I 2 168 ? 89.040  31.046  18.441  1.000 107.840 ? 168 PRO III CB  1 
ATOM 14571 C CG  . PRO I 2 168 ? 89.949  32.246  18.274  1.000 107.850 ? 168 PRO III CG  1 
ATOM 14572 C CD  . PRO I 2 168 ? 89.038  33.453  18.402  1.000 111.870 ? 168 PRO III CD  1 
ATOM 14573 N N   . SER I 2 169 ? 88.343  29.847  21.241  1.000 75.800  ? 169 SER III N   1 
ATOM 14574 C CA  . SER I 2 169 ? 88.868  29.308  22.523  1.000 79.210  ? 169 SER III CA  1 
ATOM 14575 C C   . SER I 2 169 ? 88.625  27.799  22.577  1.000 76.570  ? 169 SER III C   1 
ATOM 14576 O O   . SER I 2 169 ? 88.475  27.314  23.723  1.000 76.390  ? 169 SER III O   1 
ATOM 14577 C CB  . SER I 2 169 ? 88.266  29.988  23.752  1.000 80.930  ? 169 SER III CB  1 
ATOM 14578 O OG  . SER I 2 169 ? 88.847  29.494  24.960  1.000 72.130  ? 169 SER III OG  1 
ATOM 14579 N N   . ALA I 2 178 ? 84.033  30.441  23.473  1.000 99.640  ? 178 ALA III N   1 
ATOM 14580 C CA  . ALA I 2 178 ? 83.868  31.533  22.481  1.000 102.090 ? 178 ALA III CA  1 
ATOM 14581 C C   . ALA I 2 178 ? 83.116  32.735  23.098  1.000 100.940 ? 178 ALA III C   1 
ATOM 14582 O O   . ALA I 2 178 ? 82.428  32.564  24.121  1.000 94.930  ? 178 ALA III O   1 
ATOM 14583 C CB  . ALA I 2 178 ? 83.170  30.998  21.247  1.000 93.710  ? 178 ALA III CB  1 
ATOM 14584 N N   . SER I 2 179 ? 83.264  33.921  22.496  1.000 104.930 ? 179 SER III N   1 
ATOM 14585 C CA  . SER I 2 179 ? 82.577  35.192  22.861  1.000 106.510 ? 179 SER III CA  1 
ATOM 14586 C C   . SER I 2 179 ? 82.210  35.954  21.574  1.000 118.960 ? 179 SER III C   1 
ATOM 14587 O O   . SER I 2 179 ? 83.019  35.900  20.621  1.000 139.760 ? 179 SER III O   1 
ATOM 14588 C CB  . SER I 2 179 ? 83.444  36.029  23.784  1.000 95.790  ? 179 SER III CB  1 
ATOM 14589 O OG  . SER I 2 179 ? 83.807  35.301  24.946  1.000 87.110  ? 179 SER III OG  1 
ATOM 14590 N N   . SER I 2 180 ? 81.035  36.606  21.541  1.000 114.230 ? 180 SER III N   1 
ATOM 14591 C CA  . SER I 2 180 ? 80.506  37.425  20.411  1.000 102.940 ? 180 SER III CA  1 
ATOM 14592 C C   . SER I 2 180 ? 79.768  38.667  20.952  1.000 101.580 ? 180 SER III C   1 
ATOM 14593 O O   . SER I 2 180 ? 79.141  38.538  22.016  1.000 101.370 ? 180 SER III O   1 
ATOM 14594 C CB  . SER I 2 180 ? 79.603  36.587  19.534  1.000 85.360  ? 180 SER III CB  1 
ATOM 14595 O OG  . SER I 2 180 ? 79.145  37.344  18.436  1.000 72.460  ? 180 SER III OG  1 
ATOM 14596 N N   . TYR I 2 181 ? 79.864  39.825  20.274  1.000 93.650  ? 181 TYR III N   1 
ATOM 14597 C CA  . TYR I 2 181 ? 79.047  41.054  20.506  1.000 91.550  ? 181 TYR III CA  1 
ATOM 14598 C C   . TYR I 2 181 ? 78.592  41.619  19.142  1.000 103.560 ? 181 TYR III C   1 
ATOM 14599 O O   . TYR I 2 181 ? 79.398  41.513  18.204  1.000 98.540  ? 181 TYR III O   1 
ATOM 14600 C CB  . TYR I 2 181 ? 79.831  42.072  21.347  1.000 70.310  ? 181 TYR III CB  1 
ATOM 14601 N N   . LEU I 2 182 ? 77.373  42.188  19.030  1.000 114.210 ? 182 LEU III N   1 
ATOM 14602 C CA  . LEU I 2 182 ? 76.771  42.709  17.757  1.000 111.170 ? 182 LEU III CA  1 
ATOM 14603 C C   . LEU I 2 182 ? 75.971  44.007  17.997  1.000 111.900 ? 182 LEU III C   1 
ATOM 14604 O O   . LEU I 2 182 ? 74.790  43.895  18.362  1.000 125.130 ? 182 LEU III O   1 
ATOM 14605 C CB  . LEU I 2 182 ? 75.863  41.637  17.155  1.000 93.090  ? 182 LEU III CB  1 
ATOM 14606 N N   . SER I 2 183 ? 76.536  45.185  17.684  1.000 105.440 ? 183 SER III N   1 
ATOM 14607 C CA  . SER I 2 183 ? 76.086  46.535  18.146  1.000 107.600 ? 183 SER III CA  1 
ATOM 14608 C C   . SER I 2 183 ? 75.155  47.240  17.140  1.000 124.700 ? 183 SER III C   1 
ATOM 14609 O O   . SER I 2 183 ? 75.380  47.090  15.919  1.000 134.750 ? 183 SER III O   1 
ATOM 14610 C CB  . SER I 2 183 ? 77.287  47.404  18.439  1.000 97.610  ? 183 SER III CB  1 
ATOM 14611 O OG  . SER I 2 183 ? 78.054  46.896  19.517  1.000 87.650  ? 183 SER III OG  1 
ATOM 14612 N N   . LEU I 2 184 ? 74.169  48.024  17.633  1.000 123.390 ? 184 LEU III N   1 
ATOM 14613 C CA  . LEU I 2 184 ? 73.057  48.614  16.844  1.000 115.560 ? 184 LEU III CA  1 
ATOM 14614 C C   . LEU I 2 184 ? 72.079  49.324  17.820  1.000 131.190 ? 184 LEU III C   1 
ATOM 14615 O O   . LEU I 2 184 ? 72.408  49.317  19.020  1.000 142.290 ? 184 LEU III O   1 
ATOM 14616 C CB  . LEU I 2 184 ? 72.401  47.457  16.070  1.000 104.020 ? 184 LEU III CB  1 
ATOM 14617 C CG  . LEU I 2 184 ? 71.789  46.331  16.916  1.000 90.220  ? 184 LEU III CG  1 
ATOM 14618 C CD1 . LEU I 2 184 ? 70.414  46.726  17.438  1.000 88.080  ? 184 LEU III CD1 1 
ATOM 14619 C CD2 . LEU I 2 184 ? 71.681  45.036  16.131  1.000 88.140  ? 184 LEU III CD2 1 
ATOM 14620 N N   . THR I 2 185 ? 70.980  49.961  17.354  1.000 136.880 ? 185 THR III N   1 
ATOM 14621 C CA  . THR I 2 185 ? 69.756  50.313  18.164  1.000 125.000 ? 185 THR III CA  1 
ATOM 14622 C C   . THR I 2 185 ? 68.500  49.899  17.388  1.000 120.320 ? 185 THR III C   1 
ATOM 14623 O O   . THR I 2 185 ? 68.249  50.431  16.305  1.000 110.870 ? 185 THR III O   1 
ATOM 14624 C CB  . THR I 2 185 ? 69.664  51.801  18.569  1.000 107.100 ? 185 THR III CB  1 
ATOM 14625 O OG1 . THR I 2 185 ? 70.648  52.115  19.552  1.000 95.630  ? 185 THR III OG1 1 
ATOM 14626 C CG2 . THR I 2 185 ? 68.331  52.179  19.174  1.000 93.560  ? 185 THR III CG2 1 
ATOM 14627 N N   . PRO I 2 186 ? 67.641  48.958  17.894  1.000 111.890 ? 186 PRO III N   1 
ATOM 14628 C CA  . PRO I 2 186 ? 66.510  48.432  17.135  1.000 107.290 ? 186 PRO III CA  1 
ATOM 14629 C C   . PRO I 2 186 ? 65.136  49.049  17.515  1.000 100.360 ? 186 PRO III C   1 
ATOM 14630 O O   . PRO I 2 186 ? 64.053  48.689  17.045  1.000 75.880  ? 186 PRO III O   1 
ATOM 14631 C CB  . PRO I 2 186 ? 66.563  46.957  17.557  1.000 98.420  ? 186 PRO III CB  1 
ATOM 14632 C CG  . PRO I 2 186 ? 66.905  47.037  19.042  1.000 100.300 ? 186 PRO III CG  1 
ATOM 14633 C CD  . PRO I 2 186 ? 67.733  48.304  19.212  1.000 102.710 ? 186 PRO III CD  1 
ATOM 14634 N N   . GLU J 3 1   ? 107.735 27.596  48.650  1.000 69.150  ? 1   GLU JJJ N   1 
ATOM 14635 C CA  . GLU J 3 1   ? 109.201 27.395  48.853  1.000 73.520  ? 1   GLU JJJ CA  1 
ATOM 14636 C C   . GLU J 3 1   ? 109.966 28.595  48.263  1.000 71.130  ? 1   GLU JJJ C   1 
ATOM 14637 O O   . GLU J 3 1   ? 110.491 29.357  49.067  1.000 62.620  ? 1   GLU JJJ O   1 
ATOM 14638 C CB  . GLU J 3 1   ? 109.635 26.031  48.290  1.000 71.870  ? 1   GLU JJJ CB  1 
ATOM 14639 N N   . VAL J 3 2   ? 110.107 28.686  46.940  1.000 66.150  ? 2   VAL JJJ N   1 
ATOM 14640 C CA  . VAL J 3 2   ? 110.783 29.811  46.247  1.000 69.800  ? 2   VAL JJJ CA  1 
ATOM 14641 C C   . VAL J 3 2   ? 109.678 30.589  45.541  1.000 74.460  ? 2   VAL JJJ C   1 
ATOM 14642 O O   . VAL J 3 2   ? 108.940 29.962  44.767  1.000 67.980  ? 2   VAL JJJ O   1 
ATOM 14643 C CB  . VAL J 3 2   ? 111.877 29.338  45.257  1.000 70.450  ? 2   VAL JJJ CB  1 
ATOM 14644 C CG1 . VAL J 3 2   ? 112.186 30.360  44.176  1.000 70.120  ? 2   VAL JJJ CG1 1 
ATOM 14645 C CG2 . VAL J 3 2   ? 113.163 28.970  45.969  1.000 67.300  ? 2   VAL JJJ CG2 1 
ATOM 14646 N N   . GLN J 3 3   ? 109.569 31.893  45.785  1.000 79.410  ? 3   GLN JJJ N   1 
ATOM 14647 C CA  . GLN J 3 3   ? 108.612 32.735  45.026  1.000 78.360  ? 3   GLN JJJ CA  1 
ATOM 14648 C C   . GLN J 3 3   ? 109.335 33.980  44.516  1.000 63.710  ? 3   GLN JJJ C   1 
ATOM 14649 O O   . GLN J 3 3   ? 110.118 34.598  45.259  1.000 56.630  ? 3   GLN JJJ O   1 
ATOM 14650 C CB  . GLN J 3 3   ? 107.346 33.043  45.822  1.000 89.530  ? 3   GLN JJJ CB  1 
ATOM 14651 C CG  . GLN J 3 3   ? 107.506 32.900  47.320  1.000 94.350  ? 3   GLN JJJ CG  1 
ATOM 14652 C CD  . GLN J 3 3   ? 106.282 33.389  48.051  1.000 94.840  ? 3   GLN JJJ CD  1 
ATOM 14653 O OE1 . GLN J 3 3   ? 105.450 34.113  47.507  1.000 90.960  ? 3   GLN JJJ OE1 1 
ATOM 14654 N NE2 . GLN J 3 3   ? 106.159 32.998  49.312  1.000 98.690  ? 3   GLN JJJ NE2 1 
ATOM 14655 N N   . LEU J 3 4   ? 109.098 34.287  43.242  1.000 55.590  ? 4   LEU JJJ N   1 
ATOM 14656 C CA  . LEU J 3 4   ? 109.478 35.553  42.578  1.000 59.760  ? 4   LEU JJJ CA  1 
ATOM 14657 C C   . LEU J 3 4   ? 108.186 36.301  42.244  1.000 64.570  ? 4   LEU JJJ C   1 
ATOM 14658 O O   . LEU J 3 4   ? 107.232 35.638  41.777  1.000 58.600  ? 4   LEU JJJ O   1 
ATOM 14659 C CB  . LEU J 3 4   ? 110.269 35.233  41.309  1.000 60.490  ? 4   LEU JJJ CB  1 
ATOM 14660 C CG  . LEU J 3 4   ? 111.525 34.385  41.488  1.000 57.110  ? 4   LEU JJJ CG  1 
ATOM 14661 C CD1 . LEU J 3 4   ? 112.090 33.981  40.137  1.000 59.850  ? 4   LEU JJJ CD1 1 
ATOM 14662 C CD2 . LEU J 3 4   ? 112.584 35.093  42.305  1.000 50.380  ? 4   LEU JJJ CD2 1 
ATOM 14663 N N   . VAL J 3 5   ? 108.149 37.616  42.483  1.000 69.990  ? 5   VAL JJJ N   1 
ATOM 14664 C CA  . VAL J 3 5   ? 106.952 38.462  42.210  1.000 74.730  ? 5   VAL JJJ CA  1 
ATOM 14665 C C   . VAL J 3 5   ? 107.384 39.712  41.449  1.000 70.840  ? 5   VAL JJJ C   1 
ATOM 14666 O O   . VAL J 3 5   ? 108.175 40.502  41.982  1.000 73.330  ? 5   VAL JJJ O   1 
ATOM 14667 C CB  . VAL J 3 5   ? 106.195 38.837  43.497  1.000 82.850  ? 5   VAL JJJ CB  1 
ATOM 14668 C CG1 . VAL J 3 5   ? 104.770 39.252  43.174  1.000 78.830  ? 5   VAL JJJ CG1 1 
ATOM 14669 C CG2 . VAL J 3 5   ? 106.206 37.702  44.510  1.000 88.870  ? 5   VAL JJJ CG2 1 
ATOM 14670 N N   . GLU J 3 6   ? 106.866 39.867  40.242  1.000 73.290  ? 6   GLU JJJ N   1 
ATOM 14671 C CA  . GLU J 3 6   ? 107.125 41.028  39.361  1.000 81.000  ? 6   GLU JJJ CA  1 
ATOM 14672 C C   . GLU J 3 6   ? 106.070 42.100  39.648  1.000 87.780  ? 6   GLU JJJ C   1 
ATOM 14673 O O   . GLU J 3 6   ? 105.003 41.761  40.201  1.000 76.890  ? 6   GLU JJJ O   1 
ATOM 14674 C CB  . GLU J 3 6   ? 107.101 40.610  37.892  1.000 79.730  ? 6   GLU JJJ CB  1 
ATOM 14675 C CG  . GLU J 3 6   ? 108.135 39.558  37.546  1.000 76.500  ? 6   GLU JJJ CG  1 
ATOM 14676 C CD  . GLU J 3 6   ? 107.622 38.130  37.576  1.000 74.400  ? 6   GLU JJJ CD  1 
ATOM 14677 O OE1 . GLU J 3 6   ? 106.604 37.880  38.250  1.000 73.440  ? 6   GLU JJJ OE1 1 
ATOM 14678 O OE2 . GLU J 3 6   ? 108.225 37.277  36.904  1.000 70.460  ? 6   GLU JJJ OE2 1 
ATOM 14679 N N   . SER J 3 7   ? 106.374 43.339  39.263  1.000 99.080  ? 7   SER JJJ N   1 
ATOM 14680 C CA  . SER J 3 7   ? 105.561 44.557  39.503  1.000 91.900  ? 7   SER JJJ CA  1 
ATOM 14681 C C   . SER J 3 7   ? 106.192 45.728  38.744  1.000 102.130 ? 7   SER JJJ C   1 
ATOM 14682 O O   . SER J 3 7   ? 107.389 45.631  38.368  1.000 102.700 ? 7   SER JJJ O   1 
ATOM 14683 C CB  . SER J 3 7   ? 105.475 44.854  40.965  1.000 81.140  ? 7   SER JJJ CB  1 
ATOM 14684 O OG  . SER J 3 7   ? 106.788 45.002  41.484  1.000 81.520  ? 7   SER JJJ OG  1 
ATOM 14685 N N   . GLY J 3 8   ? 105.409 46.788  38.525  1.000 101.720 ? 8   GLY JJJ N   1 
ATOM 14686 C CA  . GLY J 3 8   ? 105.842 48.009  37.821  1.000 92.990  ? 8   GLY JJJ CA  1 
ATOM 14687 C C   . GLY J 3 8   ? 105.300 48.057  36.406  1.000 91.960  ? 8   GLY JJJ C   1 
ATOM 14688 O O   . GLY J 3 8   ? 105.366 49.138  35.795  1.000 109.540 ? 8   GLY JJJ O   1 
ATOM 14689 N N   . GLY J 3 9   ? 104.786 46.930  35.903  1.000 81.430  ? 9   GLY JJJ N   1 
ATOM 14690 C CA  . GLY J 3 9   ? 104.196 46.840  34.554  1.000 81.380  ? 9   GLY JJJ CA  1 
ATOM 14691 C C   . GLY J 3 9   ? 102.933 47.664  34.466  1.000 77.660  ? 9   GLY JJJ C   1 
ATOM 14692 O O   . GLY J 3 9   ? 102.228 47.735  35.471  1.000 66.650  ? 9   GLY JJJ O   1 
ATOM 14693 N N   . GLY J 3 10  ? 102.671 48.270  33.305  1.000 86.030  ? 10  GLY JJJ N   1 
ATOM 14694 C CA  . GLY J 3 10  ? 101.396 48.951  33.016  1.000 92.430  ? 10  GLY JJJ CA  1 
ATOM 14695 C C   . GLY J 3 10  ? 101.323 49.462  31.585  1.000 99.700  ? 10  GLY JJJ C   1 
ATOM 14696 O O   . GLY J 3 10  ? 101.996 48.886  30.701  1.000 86.910  ? 10  GLY JJJ O   1 
ATOM 14697 N N   . LEU J 3 11  ? 100.545 50.532  31.366  1.000 103.860 ? 11  LEU JJJ N   1 
ATOM 14698 C CA  . LEU J 3 11  ? 100.426 51.240  30.066  1.000 95.940  ? 11  LEU JJJ CA  1 
ATOM 14699 C C   . LEU J 3 11  ? 101.424 52.400  30.058  1.000 85.100  ? 11  LEU JJJ C   1 
ATOM 14700 O O   . LEU J 3 11  ? 101.439 53.167  31.037  1.000 72.390  ? 11  LEU JJJ O   1 
ATOM 14701 C CB  . LEU J 3 11  ? 98.988  51.726  29.871  1.000 107.150 ? 11  LEU JJJ CB  1 
ATOM 14702 C CG  . LEU J 3 11  ? 98.657  52.185  28.449  1.000 120.980 ? 11  LEU JJJ CG  1 
ATOM 14703 C CD1 . LEU J 3 11  ? 97.256  51.766  28.028  1.000 128.950 ? 11  LEU JJJ CD1 1 
ATOM 14704 C CD2 . LEU J 3 11  ? 98.843  53.693  28.311  1.000 123.990 ? 11  LEU JJJ CD2 1 
ATOM 14705 N N   . VAL J 3 12  ? 102.227 52.501  29.000  1.000 88.180  ? 12  VAL JJJ N   1 
ATOM 14706 C CA  . VAL J 3 12  ? 103.063 53.706  28.718  1.000 90.350  ? 12  VAL JJJ CA  1 
ATOM 14707 C C   . VAL J 3 12  ? 103.067 53.925  27.201  1.000 86.560  ? 12  VAL JJJ C   1 
ATOM 14708 O O   . VAL J 3 12  ? 102.832 52.915  26.464  1.000 84.050  ? 12  VAL JJJ O   1 
ATOM 14709 C CB  . VAL J 3 12  ? 104.485 53.550  29.283  1.000 79.450  ? 12  VAL JJJ CB  1 
ATOM 14710 C CG1 . VAL J 3 12  ? 105.132 52.287  28.756  1.000 81.730  ? 12  VAL JJJ CG1 1 
ATOM 14711 C CG2 . VAL J 3 12  ? 105.362 54.764  29.014  1.000 73.830  ? 12  VAL JJJ CG2 1 
ATOM 14712 N N   . LYS J 3 13  ? 103.251 55.181  26.770  1.000 81.790  ? 13  LYS JJJ N   1 
ATOM 14713 C CA  . LYS J 3 13  ? 103.162 55.596  25.347  1.000 78.640  ? 13  LYS JJJ CA  1 
ATOM 14714 C C   . LYS J 3 13  ? 104.526 55.353  24.707  1.000 78.050  ? 13  LYS JJJ C   1 
ATOM 14715 O O   . LYS J 3 13  ? 105.553 55.441  25.382  1.000 62.880  ? 13  LYS JJJ O   1 
ATOM 14716 C CB  . LYS J 3 13  ? 102.695 57.053  25.228  1.000 70.930  ? 13  LYS JJJ CB  1 
ATOM 14717 N N   . PRO J 3 14  ? 104.569 54.980  23.405  1.000 80.740  ? 14  PRO JJJ N   1 
ATOM 14718 C CA  . PRO J 3 14  ? 105.830 54.837  22.680  1.000 80.440  ? 14  PRO JJJ CA  1 
ATOM 14719 C C   . PRO J 3 14  ? 106.784 55.978  23.019  1.000 74.050  ? 14  PRO JJJ C   1 
ATOM 14720 O O   . PRO J 3 14  ? 106.306 57.038  23.336  1.000 81.750  ? 14  PRO JJJ O   1 
ATOM 14721 C CB  . PRO J 3 14  ? 105.403 54.894  21.210  1.000 78.190  ? 14  PRO JJJ CB  1 
ATOM 14722 C CG  . PRO J 3 14  ? 104.000 54.295  21.220  1.000 76.970  ? 14  PRO JJJ CG  1 
ATOM 14723 C CD  . PRO J 3 14  ? 103.405 54.649  22.570  1.000 77.000  ? 14  PRO JJJ CD  1 
ATOM 14724 N N   . GLY J 3 15  ? 108.087 55.716  22.957  1.000 75.850  ? 15  GLY JJJ N   1 
ATOM 14725 C CA  . GLY J 3 15  ? 109.139 56.658  23.381  1.000 76.200  ? 15  GLY JJJ CA  1 
ATOM 14726 C C   . GLY J 3 15  ? 109.192 56.771  24.894  1.000 81.730  ? 15  GLY JJJ C   1 
ATOM 14727 O O   . GLY J 3 15  ? 110.153 57.385  25.396  1.000 86.220  ? 15  GLY JJJ O   1 
ATOM 14728 N N   . GLY J 3 16  ? 108.232 56.159  25.600  1.000 81.660  ? 16  GLY JJJ N   1 
ATOM 14729 C CA  . GLY J 3 16  ? 108.095 56.249  27.065  1.000 86.190  ? 16  GLY JJJ CA  1 
ATOM 14730 C C   . GLY J 3 16  ? 109.148 55.420  27.781  1.000 89.700  ? 16  GLY JJJ C   1 
ATOM 14731 O O   . GLY J 3 16  ? 110.046 54.850  27.118  1.000 101.250 ? 16  GLY JJJ O   1 
ATOM 14732 N N   . SER J 3 17  ? 109.037 55.386  29.111  1.000 79.350  ? 17  SER JJJ N   1 
ATOM 14733 C CA  . SER J 3 17  ? 109.981 54.729  30.043  1.000 73.410  ? 17  SER JJJ CA  1 
ATOM 14734 C C   . SER J 3 17  ? 109.178 53.981  31.113  1.000 84.150  ? 17  SER JJJ C   1 
ATOM 14735 O O   . SER J 3 17  ? 107.969 54.220  31.221  1.000 94.400  ? 17  SER JJJ O   1 
ATOM 14736 C CB  . SER J 3 17  ? 110.905 55.753  30.611  1.000 60.640  ? 17  SER JJJ CB  1 
ATOM 14737 O OG  . SER J 3 17  ? 111.599 55.273  31.733  1.000 56.570  ? 17  SER JJJ OG  1 
ATOM 14738 N N   . LEU J 3 18  ? 109.819 53.066  31.838  1.000 93.260  ? 18  LEU JJJ N   1 
ATOM 14739 C CA  . LEU J 3 18  ? 109.157 52.147  32.804  1.000 87.220  ? 18  LEU JJJ CA  1 
ATOM 14740 C C   . LEU J 3 18  ? 110.228 51.333  33.543  1.000 85.910  ? 18  LEU JJJ C   1 
ATOM 14741 O O   . LEU J 3 18  ? 111.161 50.843  32.864  1.000 102.360 ? 18  LEU JJJ O   1 
ATOM 14742 C CB  . LEU J 3 18  ? 108.205 51.241  32.015  1.000 85.610  ? 18  LEU JJJ CB  1 
ATOM 14743 C CG  . LEU J 3 18  ? 107.107 50.550  32.824  1.000 84.600  ? 18  LEU JJJ CG  1 
ATOM 14744 C CD1 . LEU J 3 18  ? 106.597 51.445  33.942  1.000 81.000  ? 18  LEU JJJ CD1 1 
ATOM 14745 C CD2 . LEU J 3 18  ? 105.970 50.081  31.917  1.000 83.100  ? 18  LEU JJJ CD2 1 
ATOM 14746 N N   . ARG J 3 19  ? 110.101 51.192  34.869  1.000 74.910  ? 19  ARG JJJ N   1 
ATOM 14747 C CA  . ARG J 3 19  ? 111.000 50.363  35.714  1.000 76.010  ? 19  ARG JJJ CA  1 
ATOM 14748 C C   . ARG J 3 19  ? 110.208 49.181  36.287  1.000 78.240  ? 19  ARG JJJ C   1 
ATOM 14749 O O   . ARG J 3 19  ? 109.165 49.416  36.937  1.000 79.800  ? 19  ARG JJJ O   1 
ATOM 14750 C CB  . ARG J 3 19  ? 111.603 51.209  36.832  1.000 80.220  ? 19  ARG JJJ CB  1 
ATOM 14751 C CG  . ARG J 3 19  ? 112.514 50.458  37.793  1.000 79.640  ? 19  ARG JJJ CG  1 
ATOM 14752 C CD  . ARG J 3 19  ? 113.023 51.391  38.877  1.000 80.970  ? 19  ARG JJJ CD  1 
ATOM 14753 N NE  . ARG J 3 19  ? 114.137 50.789  39.591  1.000 80.790  ? 19  ARG JJJ NE  1 
ATOM 14754 C CZ  . ARG J 3 19  ? 114.494 51.039  40.841  1.000 80.120  ? 19  ARG JJJ CZ  1 
ATOM 14755 N NH1 . ARG J 3 19  ? 113.875 51.966  41.551  1.000 83.640  ? 19  ARG JJJ NH1 1 
ATOM 14756 N NH2 . ARG J 3 19  ? 115.516 50.387  41.370  1.000 84.010  ? 19  ARG JJJ NH2 1 
ATOM 14757 N N   . LEU J 3 20  ? 110.686 47.959  36.039  1.000 82.500  ? 20  LEU JJJ N   1 
ATOM 14758 C CA  . LEU J 3 20  ? 110.066 46.703  36.531  1.000 81.130  ? 20  LEU JJJ CA  1 
ATOM 14759 C C   . LEU J 3 20  ? 110.832 46.255  37.775  1.000 78.060  ? 20  LEU JJJ C   1 
ATOM 14760 O O   . LEU J 3 20  ? 112.043 46.565  37.861  1.000 76.240  ? 20  LEU JJJ O   1 
ATOM 14761 C CB  . LEU J 3 20  ? 110.104 45.656  35.413  1.000 88.590  ? 20  LEU JJJ CB  1 
ATOM 14762 C CG  . LEU J 3 20  ? 108.942 45.712  34.408  1.000 94.110  ? 20  LEU JJJ CG  1 
ATOM 14763 C CD1 . LEU J 3 20  ? 108.571 47.134  34.023  1.000 96.300  ? 20  LEU JJJ CD1 1 
ATOM 14764 C CD2 . LEU J 3 20  ? 109.251 44.901  33.148  1.000 92.370  ? 20  LEU JJJ CD2 1 
ATOM 14765 N N   . SER J 3 21  ? 110.133 45.584  38.692  1.000 78.030  ? 21  SER JJJ N   1 
ATOM 14766 C CA  . SER J 3 21  ? 110.660 45.068  39.980  1.000 83.000  ? 21  SER JJJ CA  1 
ATOM 14767 C C   . SER J 3 21  ? 110.363 43.572  40.119  1.000 84.640  ? 21  SER JJJ C   1 
ATOM 14768 O O   . SER J 3 21  ? 109.201 43.179  39.896  1.000 84.460  ? 21  SER JJJ O   1 
ATOM 14769 C CB  . SER J 3 21  ? 110.051 45.817  41.116  1.000 84.420  ? 21  SER JJJ CB  1 
ATOM 14770 O OG  . SER J 3 21  ? 110.777 47.004  41.329  1.000 89.380  ? 21  SER JJJ OG  1 
ATOM 14771 N N   . CYS J 3 22  ? 111.365 42.778  40.476  1.000 78.750  ? 22  CYS JJJ N   1 
ATOM 14772 C CA  . CYS J 3 22  ? 111.210 41.373  40.929  1.000 74.590  ? 22  CYS JJJ CA  1 
ATOM 14773 C C   . CYS J 3 22  ? 111.551 41.298  42.412  1.000 70.610  ? 22  CYS JJJ C   1 
ATOM 14774 O O   . CYS J 3 22  ? 112.648 41.758  42.786  1.000 69.500  ? 22  CYS JJJ O   1 
ATOM 14775 C CB  . CYS J 3 22  ? 112.107 40.394  40.168  1.000 79.760  ? 22  CYS JJJ CB  1 
ATOM 14776 S SG  . CYS J 3 22  ? 111.477 38.690  40.236  1.000 74.670  ? 22  CYS JJJ SG  1 
ATOM 14777 N N   . ALA J 3 23  ? 110.624 40.770  43.210  1.000 67.090  ? 23  ALA JJJ N   1 
ATOM 14778 C CA  . ALA J 3 23  ? 110.797 40.543  44.657  1.000 64.960  ? 23  ALA JJJ CA  1 
ATOM 14779 C C   . ALA J 3 23  ? 111.000 39.049  44.874  1.000 74.180  ? 23  ALA JJJ C   1 
ATOM 14780 O O   . ALA J 3 23  ? 110.059 38.270  44.609  1.000 73.120  ? 23  ALA JJJ O   1 
ATOM 14781 C CB  . ALA J 3 23  ? 109.602 41.040  45.406  1.000 64.830  ? 23  ALA JJJ CB  1 
ATOM 14782 N N   . ALA J 3 24  ? 112.198 38.677  45.326  1.000 81.580  ? 24  ALA JJJ N   1 
ATOM 14783 C CA  . ALA J 3 24  ? 112.627 37.282  45.583  1.000 70.330  ? 24  ALA JJJ CA  1 
ATOM 14784 C C   . ALA J 3 24  ? 112.535 36.963  47.079  1.000 65.890  ? 24  ALA JJJ C   1 
ATOM 14785 O O   . ALA J 3 24  ? 113.157 37.677  47.896  1.000 69.450  ? 24  ALA JJJ O   1 
ATOM 14786 C CB  . ALA J 3 24  ? 114.035 37.087  45.065  1.000 70.850  ? 24  ALA JJJ CB  1 
ATOM 14787 N N   . SER J 3 25  ? 111.765 35.932  47.415  1.000 62.560  ? 25  SER JJJ N   1 
ATOM 14788 C CA  . SER J 3 25  ? 111.740 35.269  48.745  1.000 63.620  ? 25  SER JJJ CA  1 
ATOM 14789 C C   . SER J 3 25  ? 111.938 33.761  48.559  1.000 62.130  ? 25  SER JJJ C   1 
ATOM 14790 O O   . SER J 3 25  ? 111.591 33.229  47.477  1.000 60.200  ? 25  SER JJJ O   1 
ATOM 14791 C CB  . SER J 3 25  ? 110.450 35.546  49.465  1.000 67.710  ? 25  SER JJJ CB  1 
ATOM 14792 O OG  . SER J 3 25  ? 109.351 35.028  48.731  1.000 72.700  ? 25  SER JJJ OG  1 
ATOM 14793 N N   . GLY J 3 26  ? 112.479 33.102  49.581  1.000 58.690  ? 26  GLY JJJ N   1 
ATOM 14794 C CA  . GLY J 3 26  ? 112.555 31.634  49.631  1.000 54.870  ? 26  GLY JJJ CA  1 
ATOM 14795 C C   . GLY J 3 26  ? 113.961 31.099  49.443  1.000 48.990  ? 26  GLY JJJ C   1 
ATOM 14796 O O   . GLY J 3 26  ? 114.110 29.871  49.499  1.000 50.490  ? 26  GLY JJJ O   1 
ATOM 14797 N N   . PHE J 3 27  ? 114.953 31.962  49.233  1.000 40.950  ? 27  PHE JJJ N   1 
ATOM 14798 C CA  . PHE J 3 27  ? 116.323 31.538  48.865  1.000 41.610  ? 27  PHE JJJ CA  1 
ATOM 14799 C C   . PHE J 3 27  ? 117.277 32.715  48.956  1.000 40.690  ? 27  PHE JJJ C   1 
ATOM 14800 O O   . PHE J 3 27  ? 116.800 33.824  48.861  1.000 47.250  ? 27  PHE JJJ O   1 
ATOM 14801 C CB  . PHE J 3 27  ? 116.350 30.991  47.439  1.000 41.490  ? 27  PHE JJJ CB  1 
ATOM 14802 C CG  . PHE J 3 27  ? 116.117 31.998  46.343  1.000 39.280  ? 27  PHE JJJ CG  1 
ATOM 14803 C CD1 . PHE J 3 27  ? 114.827 32.421  46.052  1.000 40.360  ? 27  PHE JJJ CD1 1 
ATOM 14804 C CD2 . PHE J 3 27  ? 117.163 32.447  45.550  1.000 38.310  ? 27  PHE JJJ CD2 1 
ATOM 14805 C CE1 . PHE J 3 27  ? 114.583 33.293  45.001  1.000 39.600  ? 27  PHE JJJ CE1 1 
ATOM 14806 C CE2 . PHE J 3 27  ? 116.920 33.332  44.510  1.000 38.490  ? 27  PHE JJJ CE2 1 
ATOM 14807 C CZ  . PHE J 3 27  ? 115.635 33.757  44.240  1.000 40.060  ? 27  PHE JJJ CZ  1 
ATOM 14808 N N   . THR J 3 28  ? 118.577 32.453  49.071  1.000 39.610  ? 28  THR JJJ N   1 
ATOM 14809 C CA  . THR J 3 28  ? 119.649 33.474  49.063  1.000 39.490  ? 28  THR JJJ CA  1 
ATOM 14810 C C   . THR J 3 28  ? 119.730 34.088  47.667  1.000 40.760  ? 28  THR JJJ C   1 
ATOM 14811 O O   . THR J 3 28  ? 120.657 33.798  46.935  1.000 46.190  ? 28  THR JJJ O   1 
ATOM 14812 C CB  . THR J 3 28  ? 121.000 32.900  49.495  1.000 40.060  ? 28  THR JJJ CB  1 
ATOM 14813 O OG1 . THR J 3 28  ? 120.777 32.296  50.770  1.000 39.400  ? 28  THR JJJ OG1 1 
ATOM 14814 C CG2 . THR J 3 28  ? 122.083 33.955  49.596  1.000 39.320  ? 28  THR JJJ CG2 1 
ATOM 14815 N N   . PHE J 3 29  ? 118.754 34.895  47.293  1.000 44.450  ? 29  PHE JJJ N   1 
ATOM 14816 C CA  . PHE J 3 29  ? 118.736 35.741  46.068  1.000 43.230  ? 29  PHE JJJ CA  1 
ATOM 14817 C C   . PHE J 3 29  ? 120.119 36.249  45.669  1.000 42.080  ? 29  PHE JJJ C   1 
ATOM 14818 O O   . PHE J 3 29  ? 120.434 36.254  44.481  1.000 39.030  ? 29  PHE JJJ O   1 
ATOM 14819 C CB  . PHE J 3 29  ? 117.859 36.957  46.315  1.000 41.460  ? 29  PHE JJJ CB  1 
ATOM 14820 C CG  . PHE J 3 29  ? 117.851 37.915  45.155  1.000 43.170  ? 29  PHE JJJ CG  1 
ATOM 14821 C CD1 . PHE J 3 29  ? 117.157 37.610  43.995  1.000 39.540  ? 29  PHE JJJ CD1 1 
ATOM 14822 C CD2 . PHE J 3 29  ? 118.592 39.091  45.206  1.000 44.990  ? 29  PHE JJJ CD2 1 
ATOM 14823 C CE1 . PHE J 3 29  ? 117.154 38.492  42.929  1.000 38.960  ? 29  PHE JJJ CE1 1 
ATOM 14824 C CE2 . PHE J 3 29  ? 118.596 39.967  44.132  1.000 42.280  ? 29  PHE JJJ CE2 1 
ATOM 14825 C CZ  . PHE J 3 29  ? 117.879 39.665  42.997  1.000 42.000  ? 29  PHE JJJ CZ  1 
ATOM 14826 N N   . SER J 3 30  ? 120.889 36.701  46.654  1.000 40.510  ? 30  SER JJJ N   1 
ATOM 14827 C CA  . SER J 3 30  ? 122.222 37.320  46.447  1.000 38.730  ? 30  SER JJJ CA  1 
ATOM 14828 C C   . SER J 3 30  ? 123.241 36.310  45.904  1.000 34.640  ? 30  SER JJJ C   1 
ATOM 14829 O O   . SER J 3 30  ? 124.395 36.717  45.688  1.000 29.650  ? 30  SER JJJ O   1 
ATOM 14830 C CB  . SER J 3 30  ? 122.700 37.925  47.737  1.000 42.750  ? 30  SER JJJ CB  1 
ATOM 14831 O OG  . SER J 3 30  ? 123.039 36.898  48.663  1.000 42.500  ? 30  SER JJJ OG  1 
ATOM 14832 N N   . SER J 3 31  ? 122.856 35.041  45.731  1.000 38.730  ? 31  SER JJJ N   1 
ATOM 14833 C CA  . SER J 3 31  ? 123.772 33.917  45.375  1.000 40.560  ? 31  SER JJJ CA  1 
ATOM 14834 C C   . SER J 3 31  ? 123.626 33.503  43.913  1.000 37.460  ? 31  SER JJJ C   1 
ATOM 14835 O O   . SER J 3 31  ? 124.524 32.822  43.434  1.000 37.300  ? 31  SER JJJ O   1 
ATOM 14836 C CB  . SER J 3 31  ? 123.583 32.725  46.291  1.000 41.720  ? 31  SER JJJ CB  1 
ATOM 14837 O OG  . SER J 3 31  ? 124.145 32.993  47.574  1.000 38.570  ? 31  SER JJJ OG  1 
ATOM 14838 N N   . TYR J 3 32  ? 122.566 33.944  43.238  1.000 38.720  ? 32  TYR JJJ N   1 
ATOM 14839 C CA  . TYR J 3 32  ? 122.111 33.417  41.925  1.000 39.870  ? 32  TYR JJJ CA  1 
ATOM 14840 C C   . TYR J 3 32  ? 122.135 34.498  40.848  1.000 39.060  ? 32  TYR JJJ C   1 
ATOM 14841 O O   . TYR J 3 32  ? 121.741 35.630  41.106  1.000 46.810  ? 32  TYR JJJ O   1 
ATOM 14842 C CB  . TYR J 3 32  ? 120.698 32.862  42.090  1.000 39.490  ? 32  TYR JJJ CB  1 
ATOM 14843 C CG  . TYR J 3 32  ? 120.649 31.683  43.020  1.000 42.310  ? 32  TYR JJJ CG  1 
ATOM 14844 C CD1 . TYR J 3 32  ? 120.636 31.849  44.385  1.000 40.270  ? 32  TYR JJJ CD1 1 
ATOM 14845 C CD2 . TYR J 3 32  ? 120.665 30.389  42.527  1.000 46.820  ? 32  TYR JJJ CD2 1 
ATOM 14846 C CE1 . TYR J 3 32  ? 120.602 30.760  45.239  1.000 43.380  ? 32  TYR JJJ CE1 1 
ATOM 14847 C CE2 . TYR J 3 32  ? 120.637 29.287  43.365  1.000 44.570  ? 32  TYR JJJ CE2 1 
ATOM 14848 C CZ  . TYR J 3 32  ? 120.605 29.474  44.731  1.000 44.530  ? 32  TYR JJJ CZ  1 
ATOM 14849 O OH  . TYR J 3 32  ? 120.588 28.391  45.561  1.000 48.130  ? 32  TYR JJJ OH  1 
ATOM 14850 N N   . THR J 3 33  ? 122.581 34.146  39.648  1.000 40.170  ? 33  THR JJJ N   1 
ATOM 14851 C CA  . THR J 3 33  ? 122.314 34.924  38.407  1.000 40.790  ? 33  THR JJJ CA  1 
ATOM 14852 C C   . THR J 3 33  ? 120.799 35.001  38.199  1.000 42.150  ? 33  THR JJJ C   1 
ATOM 14853 O O   . THR J 3 33  ? 120.128 33.999  38.464  1.000 41.250  ? 33  THR JJJ O   1 
ATOM 14854 C CB  . THR J 3 33  ? 122.975 34.236  37.207  1.000 39.390  ? 33  THR JJJ CB  1 
ATOM 14855 O OG1 . THR J 3 33  ? 124.364 34.570  37.235  1.000 44.540  ? 33  THR JJJ OG1 1 
ATOM 14856 C CG2 . THR J 3 33  ? 122.370 34.618  35.875  1.000 38.210  ? 33  THR JJJ CG2 1 
ATOM 14857 N N   . MET J 3 34  ? 120.285 36.147  37.762  1.000 48.200  ? 34  MET JJJ N   1 
ATOM 14858 C CA  . MET J 3 34  ? 118.827 36.378  37.581  1.000 51.530  ? 34  MET JJJ CA  1 
ATOM 14859 C C   . MET J 3 34  ? 118.574 36.903  36.162  1.000 49.900  ? 34  MET JJJ C   1 
ATOM 14860 O O   . MET J 3 34  ? 119.472 37.552  35.600  1.000 43.130  ? 34  MET JJJ O   1 
ATOM 14861 C CB  . MET J 3 34  ? 118.311 37.374  38.622  1.000 52.260  ? 34  MET JJJ CB  1 
ATOM 14862 C CG  . MET J 3 34  ? 118.338 36.835  40.040  1.000 54.120  ? 34  MET JJJ CG  1 
ATOM 14863 S SD  . MET J 3 34  ? 117.124 35.478  40.356  1.000 63.540  ? 34  MET JJJ SD  1 
ATOM 14864 C CE  . MET J 3 34  ? 115.608 36.185  39.776  1.000 59.940  ? 34  MET JJJ CE  1 
ATOM 14865 N N   . ASN J 3 35  ? 117.398 36.596  35.617  1.000 50.500  ? 35  ASN JJJ N   1 
ATOM 14866 C CA  . ASN J 3 35  ? 117.054 36.820  34.193  1.000 52.300  ? 35  ASN JJJ CA  1 
ATOM 14867 C C   . ASN J 3 35  ? 115.712 37.554  34.081  1.000 55.920  ? 35  ASN JJJ C   1 
ATOM 14868 O O   . ASN J 3 35  ? 114.859 37.425  34.999  1.000 54.660  ? 35  ASN JJJ O   1 
ATOM 14869 C CB  . ASN J 3 35  ? 117.025 35.493  33.430  1.000 50.950  ? 35  ASN JJJ CB  1 
ATOM 14870 C CG  . ASN J 3 35  ? 118.409 34.954  33.146  1.000 53.500  ? 35  ASN JJJ CG  1 
ATOM 14871 O OD1 . ASN J 3 35  ? 119.019 35.277  32.138  1.000 55.260  ? 35  ASN JJJ OD1 1 
ATOM 14872 N ND2 . ASN J 3 35  ? 118.919 34.127  34.029  1.000 60.580  ? 35  ASN JJJ ND2 1 
ATOM 14873 N N   . TRP J 3 36  ? 115.549 38.324  32.998  1.000 61.860  ? 36  TRP JJJ N   1 
ATOM 14874 C CA  . TRP J 3 36  ? 114.240 38.821  32.491  1.000 57.960  ? 36  TRP JJJ CA  1 
ATOM 14875 C C   . TRP J 3 36  ? 113.963 38.119  31.167  1.000 53.980  ? 36  TRP JJJ C   1 
ATOM 14876 O O   . TRP J 3 36  ? 114.867 38.109  30.318  1.000 57.240  ? 36  TRP JJJ O   1 
ATOM 14877 C CB  . TRP J 3 36  ? 114.236 40.352  32.320  1.000 55.140  ? 36  TRP JJJ CB  1 
ATOM 14878 C CG  . TRP J 3 36  ? 114.263 41.117  33.611  1.000 49.610  ? 36  TRP JJJ CG  1 
ATOM 14879 C CD1 . TRP J 3 36  ? 115.344 41.706  34.185  1.000 48.050  ? 36  TRP JJJ CD1 1 
ATOM 14880 C CD2 . TRP J 3 36  ? 113.160 41.363  34.496  1.000 47.640  ? 36  TRP JJJ CD2 1 
ATOM 14881 N NE1 . TRP J 3 36  ? 114.992 42.308  35.362  1.000 49.630  ? 36  TRP JJJ NE1 1 
ATOM 14882 C CE2 . TRP J 3 36  ? 113.657 42.115  35.577  1.000 48.530  ? 36  TRP JJJ CE2 1 
ATOM 14883 C CE3 . TRP J 3 36  ? 111.807 41.020  34.479  1.000 52.790  ? 36  TRP JJJ CE3 1 
ATOM 14884 C CZ2 . TRP J 3 36  ? 112.847 42.539  36.629  1.000 52.190  ? 36  TRP JJJ CZ2 1 
ATOM 14885 C CZ3 . TRP J 3 36  ? 111.001 41.435  35.517  1.000 54.460  ? 36  TRP JJJ CZ3 1 
ATOM 14886 C CH2 . TRP J 3 36  ? 111.517 42.182  36.580  1.000 52.530  ? 36  TRP JJJ CH2 1 
ATOM 14887 N N   . VAL J 3 37  ? 112.779 37.536  31.013  1.000 54.920  ? 37  VAL JJJ N   1 
ATOM 14888 C CA  . VAL J 3 37  ? 112.308 36.900  29.745  1.000 61.450  ? 37  VAL JJJ CA  1 
ATOM 14889 C C   . VAL J 3 37  ? 110.916 37.465  29.476  1.000 65.210  ? 37  VAL JJJ C   1 
ATOM 14890 O O   . VAL J 3 37  ? 110.152 37.593  30.454  1.000 64.810  ? 37  VAL JJJ O   1 
ATOM 14891 C CB  . VAL J 3 37  ? 112.271 35.361  29.861  1.000 62.150  ? 37  VAL JJJ CB  1 
ATOM 14892 C CG1 . VAL J 3 37  ? 111.738 34.701  28.603  1.000 64.330  ? 37  VAL JJJ CG1 1 
ATOM 14893 C CG2 . VAL J 3 37  ? 113.622 34.783  30.218  1.000 61.710  ? 37  VAL JJJ CG2 1 
ATOM 14894 N N   . ARG J 3 38  ? 110.594 37.781  28.224  1.000 66.530  ? 38  ARG JJJ N   1 
ATOM 14895 C CA  . ARG J 3 38  ? 109.267 38.370  27.902  1.000 69.160  ? 38  ARG JJJ CA  1 
ATOM 14896 C C   . ARG J 3 38  ? 108.522 37.502  26.892  1.000 69.310  ? 38  ARG JJJ C   1 
ATOM 14897 O O   . ARG J 3 38  ? 109.180 36.722  26.180  1.000 70.250  ? 38  ARG JJJ O   1 
ATOM 14898 C CB  . ARG J 3 38  ? 109.414 39.786  27.356  1.000 71.520  ? 38  ARG JJJ CB  1 
ATOM 14899 C CG  . ARG J 3 38  ? 110.046 39.855  25.976  1.000 70.720  ? 38  ARG JJJ CG  1 
ATOM 14900 C CD  . ARG J 3 38  ? 110.119 41.294  25.508  1.000 67.430  ? 38  ARG JJJ CD  1 
ATOM 14901 N NE  . ARG J 3 38  ? 111.019 41.406  24.380  1.000 62.460  ? 38  ARG JJJ NE  1 
ATOM 14902 C CZ  . ARG J 3 38  ? 111.355 42.544  23.814  1.000 66.200  ? 38  ARG JJJ CZ  1 
ATOM 14903 N NH1 . ARG J 3 38  ? 110.825 43.679  24.243  1.000 71.980  ? 38  ARG JJJ NH1 1 
ATOM 14904 N NH2 . ARG J 3 38  ? 112.200 42.539  22.800  1.000 72.360  ? 38  ARG JJJ NH2 1 
ATOM 14905 N N   . GLN J 3 39  ? 107.198 37.669  26.848  1.000 71.060  ? 39  GLN JJJ N   1 
ATOM 14906 C CA  . GLN J 3 39  ? 106.267 36.873  26.008  1.000 77.680  ? 39  GLN JJJ CA  1 
ATOM 14907 C C   . GLN J 3 39  ? 105.219 37.803  25.385  1.000 88.980  ? 39  GLN JJJ C   1 
ATOM 14908 O O   . GLN J 3 39  ? 104.269 38.203  26.091  1.000 81.850  ? 39  GLN JJJ O   1 
ATOM 14909 C CB  . GLN J 3 39  ? 105.597 35.778  26.836  1.000 72.630  ? 39  GLN JJJ CB  1 
ATOM 14910 C CG  . GLN J 3 39  ? 104.900 34.731  25.971  1.000 67.160  ? 39  GLN JJJ CG  1 
ATOM 14911 C CD  . GLN J 3 39  ? 104.343 33.600  26.792  1.000 64.860  ? 39  GLN JJJ CD  1 
ATOM 14912 O OE1 . GLN J 3 39  ? 104.077 33.728  27.989  1.000 57.300  ? 39  GLN JJJ OE1 1 
ATOM 14913 N NE2 . GLN J 3 39  ? 104.176 32.469  26.139  1.000 62.860  ? 39  GLN JJJ NE2 1 
ATOM 14914 N N   . ALA J 3 40  ? 105.394 38.130  24.104  1.000 103.740 ? 40  ALA JJJ N   1 
ATOM 14915 C CA  . ALA J 3 40  ? 104.486 39.004  23.331  1.000 99.270  ? 40  ALA JJJ CA  1 
ATOM 14916 C C   . ALA J 3 40  ? 103.183 38.246  23.103  1.000 97.190  ? 40  ALA JJJ C   1 
ATOM 14917 O O   . ALA J 3 40  ? 103.208 37.031  22.911  1.000 79.870  ? 40  ALA JJJ O   1 
ATOM 14918 C CB  . ALA J 3 40  ? 105.141 39.418  22.036  1.000 99.460  ? 40  ALA JJJ CB  1 
ATOM 14919 N N   . PRO J 3 41  ? 102.010 38.927  23.125  1.000 105.140 ? 41  PRO JJJ N   1 
ATOM 14920 C CA  . PRO J 3 41  ? 100.734 38.216  23.195  1.000 100.200 ? 41  PRO JJJ CA  1 
ATOM 14921 C C   . PRO J 3 41  ? 100.642 37.259  21.999  1.000 92.110  ? 41  PRO JJJ C   1 
ATOM 14922 O O   . PRO J 3 41  ? 100.863 37.714  20.890  1.000 87.140  ? 41  PRO JJJ O   1 
ATOM 14923 C CB  . PRO J 3 41  ? 99.678  39.331  23.165  1.000 102.990 ? 41  PRO JJJ CB  1 
ATOM 14924 C CG  . PRO J 3 41  ? 100.437 40.587  23.573  1.000 101.840 ? 41  PRO JJJ CG  1 
ATOM 14925 C CD  . PRO J 3 41  ? 101.841 40.390  23.038  1.000 98.950  ? 41  PRO JJJ CD  1 
ATOM 14926 N N   . GLY J 3 42  ? 100.416 35.966  22.264  1.000 82.890  ? 42  GLY JJJ N   1 
ATOM 14927 C CA  . GLY J 3 42  ? 100.172 34.928  21.243  1.000 77.910  ? 42  GLY JJJ CA  1 
ATOM 14928 C C   . GLY J 3 42  ? 101.448 34.335  20.667  1.000 75.270  ? 42  GLY JJJ C   1 
ATOM 14929 O O   . GLY J 3 42  ? 101.338 33.252  20.064  1.000 72.610  ? 42  GLY JJJ O   1 
ATOM 14930 N N   . LYS J 3 43  ? 102.602 35.006  20.837  1.000 69.250  ? 43  LYS JJJ N   1 
ATOM 14931 C CA  . LYS J 3 43  ? 103.943 34.516  20.407  1.000 62.700  ? 43  LYS JJJ CA  1 
ATOM 14932 C C   . LYS J 3 43  ? 104.599 33.703  21.553  1.000 67.010  ? 43  LYS JJJ C   1 
ATOM 14933 O O   . LYS J 3 43  ? 103.973 33.536  22.650  1.000 64.940  ? 43  LYS JJJ O   1 
ATOM 14934 C CB  . LYS J 3 43  ? 104.765 35.703  19.890  1.000 54.740  ? 43  LYS JJJ CB  1 
ATOM 14935 N N   . GLY J 3 44  ? 105.792 33.144  21.308  1.000 68.230  ? 44  GLY JJJ N   1 
ATOM 14936 C CA  . GLY J 3 44  ? 106.530 32.309  22.282  1.000 72.970  ? 44  GLY JJJ CA  1 
ATOM 14937 C C   . GLY J 3 44  ? 107.326 33.160  23.265  1.000 78.700  ? 44  GLY JJJ C   1 
ATOM 14938 O O   . GLY J 3 44  ? 106.993 34.354  23.423  1.000 74.560  ? 44  GLY JJJ O   1 
ATOM 14939 N N   . LEU J 3 45  ? 108.370 32.593  23.881  1.000 74.280  ? 45  LEU JJJ N   1 
ATOM 14940 C CA  . LEU J 3 45  ? 109.203 33.301  24.897  1.000 69.320  ? 45  LEU JJJ CA  1 
ATOM 14941 C C   . LEU J 3 45  ? 110.381 33.969  24.188  1.000 62.660  ? 45  LEU JJJ C   1 
ATOM 14942 O O   . LEU J 3 45  ? 110.708 33.516  23.077  1.000 55.440  ? 45  LEU JJJ O   1 
ATOM 14943 C CB  . LEU J 3 45  ? 109.694 32.303  25.947  1.000 71.720  ? 45  LEU JJJ CB  1 
ATOM 14944 C CG  . LEU J 3 45  ? 108.607 31.695  26.834  1.000 73.810  ? 45  LEU JJJ CG  1 
ATOM 14945 C CD1 . LEU J 3 45  ? 109.206 30.718  27.826  1.000 76.190  ? 45  LEU JJJ CD1 1 
ATOM 14946 C CD2 . LEU J 3 45  ? 107.822 32.760  27.587  1.000 75.690  ? 45  LEU JJJ CD2 1 
ATOM 14947 N N   . GLN J 3 46  ? 110.988 34.996  24.802  1.000 58.950  ? 46  GLN JJJ N   1 
ATOM 14948 C CA  . GLN J 3 46  ? 112.196 35.692  24.278  1.000 58.440  ? 46  GLN JJJ CA  1 
ATOM 14949 C C   . GLN J 3 46  ? 112.970 36.300  25.451  1.000 56.340  ? 46  GLN JJJ C   1 
ATOM 14950 O O   . GLN J 3 46  ? 112.417 37.182  26.158  1.000 56.160  ? 46  GLN JJJ O   1 
ATOM 14951 C CB  . GLN J 3 46  ? 111.828 36.787  23.269  1.000 65.610  ? 46  GLN JJJ CB  1 
ATOM 14952 C CG  . GLN J 3 46  ? 113.030 37.557  22.735  1.000 65.300  ? 46  GLN JJJ CG  1 
ATOM 14953 C CD  . GLN J 3 46  ? 112.668 38.853  22.046  1.000 58.420  ? 46  GLN JJJ CD  1 
ATOM 14954 O OE1 . GLN J 3 46  ? 111.788 39.619  22.455  1.000 52.060  ? 46  GLN JJJ OE1 1 
ATOM 14955 N NE2 . GLN J 3 46  ? 113.410 39.126  20.994  1.000 54.910  ? 46  GLN JJJ NE2 1 
ATOM 14956 N N   . TRP J 3 47  ? 114.202 35.836  25.653  1.000 57.270  ? 47  TRP JJJ N   1 
ATOM 14957 C CA  . TRP J 3 47  ? 115.101 36.296  26.746  1.000 50.440  ? 47  TRP JJJ CA  1 
ATOM 14958 C C   . TRP J 3 47  ? 115.442 37.764  26.515  1.000 46.000  ? 47  TRP JJJ C   1 
ATOM 14959 O O   . TRP J 3 47  ? 115.671 38.140  25.355  1.000 39.410  ? 47  TRP JJJ O   1 
ATOM 14960 C CB  . TRP J 3 47  ? 116.367 35.438  26.807  1.000 47.170  ? 47  TRP JJJ CB  1 
ATOM 14961 C CG  . TRP J 3 47  ? 117.412 35.970  27.732  1.000 43.000  ? 47  TRP JJJ CG  1 
ATOM 14962 C CD1 . TRP J 3 47  ? 117.405 35.920  29.097  1.000 42.180  ? 47  TRP JJJ CD1 1 
ATOM 14963 C CD2 . TRP J 3 47  ? 118.622 36.636  27.353  1.000 41.320  ? 47  TRP JJJ CD2 1 
ATOM 14964 N NE1 . TRP J 3 47  ? 118.537 36.517  29.590  1.000 42.110  ? 47  TRP JJJ NE1 1 
ATOM 14965 C CE2 . TRP J 3 47  ? 119.310 36.961  28.543  1.000 40.830  ? 47  TRP JJJ CE2 1 
ATOM 14966 C CE3 . TRP J 3 47  ? 119.201 36.973  26.127  1.000 42.310  ? 47  TRP JJJ CE3 1 
ATOM 14967 C CZ2 . TRP J 3 47  ? 120.534 37.612  28.539  1.000 40.450  ? 47  TRP JJJ CZ2 1 
ATOM 14968 C CZ3 . TRP J 3 47  ? 120.417 37.629  26.125  1.000 44.060  ? 47  TRP JJJ CZ3 1 
ATOM 14969 C CH2 . TRP J 3 47  ? 121.079 37.940  27.314  1.000 42.490  ? 47  TRP JJJ CH2 1 
ATOM 14970 N N   . VAL J 3 48  ? 115.469 38.543  27.590  1.000 47.520  ? 48  VAL JJJ N   1 
ATOM 14971 C CA  . VAL J 3 48  ? 115.693 40.014  27.563  1.000 48.150  ? 48  VAL JJJ CA  1 
ATOM 14972 C C   . VAL J 3 48  ? 117.096 40.297  28.085  1.000 50.670  ? 48  VAL JJJ C   1 
ATOM 14973 O O   . VAL J 3 48  ? 117.880 40.921  27.359  1.000 51.370  ? 48  VAL JJJ O   1 
ATOM 14974 C CB  . VAL J 3 48  ? 114.634 40.744  28.407  1.000 48.530  ? 48  VAL JJJ CB  1 
ATOM 14975 C CG1 . VAL J 3 48  ? 115.057 42.161  28.755  1.000 46.430  ? 48  VAL JJJ CG1 1 
ATOM 14976 C CG2 . VAL J 3 48  ? 113.263 40.706  27.725  1.000 46.060  ? 48  VAL JJJ CG2 1 
ATOM 14977 N N   . SER J 3 49  ? 117.385 39.881  29.314  1.000 53.380  ? 49  SER JJJ N   1 
ATOM 14978 C CA  . SER J 3 49  ? 118.649 40.260  29.995  1.000 56.440  ? 49  SER JJJ CA  1 
ATOM 14979 C C   . SER J 3 49  ? 118.942 39.329  31.177  1.000 54.120  ? 49  SER JJJ C   1 
ATOM 14980 O O   . SER J 3 49  ? 117.985 38.828  31.795  1.000 51.860  ? 49  SER JJJ O   1 
ATOM 14981 C CB  . SER J 3 49  ? 118.588 41.705  30.419  1.000 59.460  ? 49  SER JJJ CB  1 
ATOM 14982 O OG  . SER J 3 49  ? 119.817 42.122  30.995  1.000 58.010  ? 49  SER JJJ OG  1 
ATOM 14983 N N   . SER J 3 50  ? 120.252 39.201  31.466  1.000 52.480  ? 50  SER JJJ N   1 
ATOM 14984 C CA  . SER J 3 50  ? 120.770 38.406  32.606  1.000 55.570  ? 50  SER JJJ CA  1 
ATOM 14985 C C   . SER J 3 50  ? 121.681 39.300  33.426  1.000 51.270  ? 50  SER JJJ C   1 
ATOM 14986 O O   . SER J 3 50  ? 122.265 40.212  32.841  1.000 53.170  ? 50  SER JJJ O   1 
ATOM 14987 C CB  . SER J 3 50  ? 121.701 37.334  32.157  1.000 63.370  ? 50  SER JJJ CB  1 
ATOM 14988 O OG  . SER J 3 50  ? 121.103 36.428  31.258  1.000 62.300  ? 50  SER JJJ OG  1 
ATOM 14989 N N   . ILE J 3 51  ? 121.801 39.032  34.715  1.000 49.490  ? 51  ILE JJJ N   1 
ATOM 14990 C CA  . ILE J 3 51  ? 122.780 39.724  35.594  1.000 52.000  ? 51  ILE JJJ CA  1 
ATOM 14991 C C   . ILE J 3 51  ? 123.341 38.701  36.578  1.000 50.590  ? 51  ILE JJJ C   1 
ATOM 14992 O O   . ILE J 3 51  ? 122.538 37.934  37.147  1.000 45.030  ? 51  ILE JJJ O   1 
ATOM 14993 C CB  . ILE J 3 51  ? 122.120 40.913  36.316  1.000 56.160  ? 51  ILE JJJ CB  1 
ATOM 14994 C CG1 . ILE J 3 51  ? 123.140 41.691  37.150  1.000 60.650  ? 51  ILE JJJ CG1 1 
ATOM 14995 C CG2 . ILE J 3 51  ? 120.940 40.468  37.159  1.000 54.910  ? 51  ILE JJJ CG2 1 
ATOM 14996 C CD1 . ILE J 3 51  ? 122.658 43.027  37.628  1.000 59.990  ? 51  ILE JJJ CD1 1 
ATOM 14997 N N   . SER J 3 52  ? 124.664 38.720  36.769  1.000 49.320  ? 52  SER JJJ N   1 
ATOM 14998 C CA  . SER J 3 52  ? 125.399 37.837  37.708  1.000 50.810  ? 52  SER JJJ CA  1 
ATOM 14999 C C   . SER J 3 52  ? 125.016 38.171  39.159  1.000 52.410  ? 52  SER JJJ C   1 
ATOM 15000 O O   . SER J 3 52  ? 124.386 39.213  39.387  1.000 49.850  ? 52  SER JJJ O   1 
ATOM 15001 C CB  . SER J 3 52  ? 126.902 37.883  37.463  1.000 50.010  ? 52  SER JJJ CB  1 
ATOM 15002 O OG  . SER J 3 52  ? 127.525 39.075  37.938  1.000 48.560  ? 52  SER JJJ OG  1 
ATOM 15003 N N   . SER J 3 53  ? 125.353 37.283  40.100  1.000 55.290  ? 53  SER JJJ N   1 
ATOM 15004 C CA  . SER J 3 53  ? 125.050 37.442  41.546  1.000 57.820  ? 53  SER JJJ CA  1 
ATOM 15005 C C   . SER J 3 53  ? 125.547 38.816  42.029  1.000 61.380  ? 53  SER JJJ C   1 
ATOM 15006 O O   . SER J 3 53  ? 124.815 39.480  42.779  1.000 68.840  ? 53  SER JJJ O   1 
ATOM 15007 C CB  . SER J 3 53  ? 125.630 36.302  42.355  1.000 59.050  ? 53  SER JJJ CB  1 
ATOM 15008 O OG  . SER J 3 53  ? 127.039 36.440  42.523  1.000 61.890  ? 53  SER JJJ OG  1 
ATOM 15009 N N   . SER J 3 54  ? 126.744 39.240  41.614  1.000 60.110  ? 54  SER JJJ N   1 
ATOM 15010 C CA  . SER J 3 54  ? 127.426 40.448  42.146  1.000 60.060  ? 54  SER JJJ CA  1 
ATOM 15011 C C   . SER J 3 54  ? 127.356 41.594  41.137  1.000 59.810  ? 54  SER JJJ C   1 
ATOM 15012 O O   . SER J 3 54  ? 128.056 42.612  41.317  1.000 62.100  ? 54  SER JJJ O   1 
ATOM 15013 C CB  . SER J 3 54  ? 128.833 40.143  42.524  1.000 62.830  ? 54  SER JJJ CB  1 
ATOM 15014 O OG  . SER J 3 54  ? 128.865 39.834  43.909  1.000 67.880  ? 54  SER JJJ OG  1 
ATOM 15015 N N   . SER J 3 55  ? 126.562 41.426  40.095  1.000 55.790  ? 55  SER JJJ N   1 
ATOM 15016 C CA  . SER J 3 55  ? 126.334 42.459  39.060  1.000 51.980  ? 55  SER JJJ CA  1 
ATOM 15017 C C   . SER J 3 55  ? 127.649 42.752  38.323  1.000 51.580  ? 55  SER JJJ C   1 
ATOM 15018 O O   . SER J 3 55  ? 127.733 43.832  37.737  1.000 51.620  ? 55  SER JJJ O   1 
ATOM 15019 C CB  . SER J 3 55  ? 125.728 43.674  39.698  1.000 50.580  ? 55  SER JJJ CB  1 
ATOM 15020 O OG  . SER J 3 55  ? 124.885 43.299  40.792  1.000 48.240  ? 55  SER JJJ OG  1 
ATOM 15021 N N   . THR J 3 56  ? 128.521 41.749  38.233  1.000 56.030  ? 56  THR JJJ N   1 
ATOM 15022 C CA  . THR J 3 56  ? 129.779 41.885  37.463  1.000 50.280  ? 56  THR JJJ CA  1 
ATOM 15023 C C   . THR J 3 56  ? 129.493 41.638  35.980  1.000 51.020  ? 56  THR JJJ C   1 
ATOM 15024 O O   . THR J 3 56  ? 130.176 42.264  35.161  1.000 55.520  ? 56  THR JJJ O   1 
ATOM 15025 C CB  . THR J 3 56  ? 130.834 40.931  38.024  1.000 42.570  ? 56  THR JJJ CB  1 
ATOM 15026 O OG1 . THR J 3 56  ? 132.089 41.331  37.478  1.000 47.040  ? 56  THR JJJ OG1 1 
ATOM 15027 N N   . TYR J 3 57  ? 128.516 40.783  35.647  1.000 52.660  ? 57  TYR JJJ N   1 
ATOM 15028 C CA  . TYR J 3 57  ? 128.235 40.427  34.233  1.000 57.870  ? 57  TYR JJJ CA  1 
ATOM 15029 C C   . TYR J 3 57  ? 126.744 40.592  33.929  1.000 62.600  ? 57  TYR JJJ C   1 
ATOM 15030 O O   . TYR J 3 57  ? 125.883 39.768  34.349  1.000 64.120  ? 57  TYR JJJ O   1 
ATOM 15031 C CB  . TYR J 3 57  ? 128.740 39.020  33.908  1.000 55.710  ? 57  TYR JJJ CB  1 
ATOM 15032 C CG  . TYR J 3 57  ? 130.230 38.838  34.038  1.000 56.680  ? 57  TYR JJJ CG  1 
ATOM 15033 C CD1 . TYR J 3 57  ? 130.815 38.655  35.284  1.000 63.130  ? 57  TYR JJJ CD1 1 
ATOM 15034 C CD2 . TYR J 3 57  ? 131.058 38.822  32.929  1.000 53.270  ? 57  TYR JJJ CD2 1 
ATOM 15035 C CE1 . TYR J 3 57  ? 132.187 38.487  35.424  1.000 59.420  ? 57  TYR JJJ CE1 1 
ATOM 15036 C CE2 . TYR J 3 57  ? 132.431 38.645  33.049  1.000 53.320  ? 57  TYR JJJ CE2 1 
ATOM 15037 C CZ  . TYR J 3 57  ? 132.998 38.490  34.302  1.000 54.000  ? 57  TYR JJJ CZ  1 
ATOM 15038 O OH  . TYR J 3 57  ? 134.343 38.336  34.445  1.000 49.110  ? 57  TYR JJJ OH  1 
ATOM 15039 N N   . MET J 3 58  ? 126.439 41.646  33.172  1.000 60.960  ? 58  MET JJJ N   1 
ATOM 15040 C CA  . MET J 3 58  ? 125.099 41.875  32.585  1.000 55.140  ? 58  MET JJJ CA  1 
ATOM 15041 C C   . MET J 3 58  ? 125.178 41.540  31.096  1.000 51.140  ? 58  MET JJJ C   1 
ATOM 15042 O O   . MET J 3 58  ? 126.203 41.829  30.480  1.000 46.540  ? 58  MET JJJ O   1 
ATOM 15043 C CB  . MET J 3 58  ? 124.674 43.326  32.794  1.000 58.510  ? 58  MET JJJ CB  1 
ATOM 15044 C CG  . MET J 3 58  ? 124.281 43.654  34.242  1.000 56.910  ? 58  MET JJJ CG  1 
ATOM 15045 S SD  . MET J 3 58  ? 125.687 43.715  35.408  1.000 54.960  ? 58  MET JJJ SD  1 
ATOM 15046 C CE  . MET J 3 58  ? 126.729 45.011  34.746  1.000 61.810  ? 58  MET JJJ CE  1 
ATOM 15047 N N   . TYR J 3 59  ? 124.164 40.863  30.571  1.000 53.940  ? 59  TYR JJJ N   1 
ATOM 15048 C CA  . TYR J 3 59  ? 124.019 40.501  29.137  1.000 58.740  ? 59  TYR JJJ CA  1 
ATOM 15049 C C   . TYR J 3 59  ? 122.626 40.915  28.686  1.000 59.380  ? 59  TYR JJJ C   1 
ATOM 15050 O O   . TYR J 3 59  ? 121.674 40.827  29.515  1.000 50.600  ? 59  TYR JJJ O   1 
ATOM 15051 C CB  . TYR J 3 59  ? 124.180 38.996  28.904  1.000 59.930  ? 59  TYR JJJ CB  1 
ATOM 15052 C CG  . TYR J 3 59  ? 125.516 38.443  29.310  1.000 57.770  ? 59  TYR JJJ CG  1 
ATOM 15053 C CD1 . TYR J 3 59  ? 126.610 38.593  28.471  1.000 58.980  ? 59  TYR JJJ CD1 1 
ATOM 15054 C CD2 . TYR J 3 59  ? 125.708 37.780  30.512  1.000 53.320  ? 59  TYR JJJ CD2 1 
ATOM 15055 C CE1 . TYR J 3 59  ? 127.844 38.082  28.796  1.000 58.860  ? 59  TYR JJJ CE1 1 
ATOM 15056 C CE2 . TYR J 3 59  ? 126.954 37.315  30.877  1.000 55.300  ? 59  TYR JJJ CE2 1 
ATOM 15057 C CZ  . TYR J 3 59  ? 128.026 37.461  30.014  1.000 57.210  ? 59  TYR JJJ CZ  1 
ATOM 15058 O OH  . TYR J 3 59  ? 129.272 37.015  30.339  1.000 57.980  ? 59  TYR JJJ OH  1 
ATOM 15059 N N   . TYR J 3 60  ? 122.497 41.334  27.426  1.000 58.240  ? 60  TYR JJJ N   1 
ATOM 15060 C CA  . TYR J 3 60  ? 121.187 41.749  26.866  1.000 54.130  ? 60  TYR JJJ CA  1 
ATOM 15061 C C   . TYR J 3 60  ? 120.981 41.054  25.527  1.000 55.540  ? 60  TYR JJJ C   1 
ATOM 15062 O O   . TYR J 3 60  ? 121.954 40.887  24.783  1.000 49.350  ? 60  TYR JJJ O   1 
ATOM 15063 C CB  . TYR J 3 60  ? 121.095 43.270  26.739  1.000 47.500  ? 60  TYR JJJ CB  1 
ATOM 15064 C CG  . TYR J 3 60  ? 121.391 44.022  28.016  1.000 42.850  ? 60  TYR JJJ CG  1 
ATOM 15065 C CD1 . TYR J 3 60  ? 122.702 44.285  28.394  1.000 38.520  ? 60  TYR JJJ CD1 1 
ATOM 15066 C CD2 . TYR J 3 60  ? 120.360 44.468  28.850  1.000 38.760  ? 60  TYR JJJ CD2 1 
ATOM 15067 C CE1 . TYR J 3 60  ? 122.986 44.975  29.555  1.000 36.410  ? 60  TYR JJJ CE1 1 
ATOM 15068 C CE2 . TYR J 3 60  ? 120.641 45.162  30.021  1.000 38.850  ? 60  TYR JJJ CE2 1 
ATOM 15069 C CZ  . TYR J 3 60  ? 121.959 45.407  30.378  1.000 38.490  ? 60  TYR JJJ CZ  1 
ATOM 15070 O OH  . TYR J 3 60  ? 122.265 46.077  31.526  1.000 38.620  ? 60  TYR JJJ OH  1 
ATOM 15071 N N   . GLY J 3 61  ? 119.735 40.655  25.261  1.000 58.200  ? 61  GLY JJJ N   1 
ATOM 15072 C CA  . GLY J 3 61  ? 119.258 40.300  23.912  1.000 63.440  ? 61  GLY JJJ CA  1 
ATOM 15073 C C   . GLY J 3 61  ? 119.449 41.467  22.975  1.000 65.920  ? 61  GLY JJJ C   1 
ATOM 15074 O O   . GLY J 3 61  ? 119.451 42.605  23.461  1.000 69.930  ? 61  GLY JJJ O   1 
ATOM 15075 N N   . ASP J 3 62  ? 119.634 41.190  21.691  1.000 74.310  ? 62  ASP JJJ N   1 
ATOM 15076 C CA  . ASP J 3 62  ? 119.894 42.229  20.663  1.000 83.470  ? 62  ASP JJJ CA  1 
ATOM 15077 C C   . ASP J 3 62  ? 118.712 43.197  20.614  1.000 84.760  ? 62  ASP JJJ C   1 
ATOM 15078 O O   . ASP J 3 62  ? 118.944 44.420  20.633  1.000 92.880  ? 62  ASP JJJ O   1 
ATOM 15079 C CB  . ASP J 3 62  ? 120.218 41.608  19.304  1.000 82.460  ? 62  ASP JJJ CB  1 
ATOM 15080 C CG  . ASP J 3 62  ? 121.668 41.146  19.209  1.000 87.920  ? 62  ASP JJJ CG  1 
ATOM 15081 O OD1 . ASP J 3 62  ? 122.517 41.678  19.969  1.000 92.790  ? 62  ASP JJJ OD1 1 
ATOM 15082 O OD2 . ASP J 3 62  ? 121.948 40.256  18.393  1.000 86.460  ? 62  ASP JJJ OD2 1 
ATOM 15083 N N   . SER J 3 63  ? 117.488 42.673  20.611  1.000 76.590  ? 63  SER JJJ N   1 
ATOM 15084 C CA  . SER J 3 63  ? 116.256 43.478  20.396  1.000 70.180  ? 63  SER JJJ CA  1 
ATOM 15085 C C   . SER J 3 63  ? 116.172 44.645  21.386  1.000 72.640  ? 63  SER JJJ C   1 
ATOM 15086 O O   . SER J 3 63  ? 115.437 45.573  21.080  1.000 76.140  ? 63  SER JJJ O   1 
ATOM 15087 C CB  . SER J 3 63  ? 115.039 42.623  20.489  1.000 64.860  ? 63  SER JJJ CB  1 
ATOM 15088 O OG  . SER J 3 63  ? 114.949 42.120  21.790  1.000 67.370  ? 63  SER JJJ OG  1 
ATOM 15089 N N   . VAL J 3 64  ? 116.885 44.623  22.515  1.000 73.010  ? 64  VAL JJJ N   1 
ATOM 15090 C CA  . VAL J 3 64  ? 116.779 45.717  23.530  1.000 74.900  ? 64  VAL JJJ CA  1 
ATOM 15091 C C   . VAL J 3 64  ? 118.150 46.315  23.842  1.000 69.810  ? 64  VAL JJJ C   1 
ATOM 15092 O O   . VAL J 3 64  ? 118.181 47.145  24.765  1.000 58.270  ? 64  VAL JJJ O   1 
ATOM 15093 C CB  . VAL J 3 64  ? 116.104 45.256  24.838  1.000 80.000  ? 64  VAL JJJ CB  1 
ATOM 15094 C CG1 . VAL J 3 64  ? 114.741 44.639  24.578  1.000 81.930  ? 64  VAL JJJ CG1 1 
ATOM 15095 C CG2 . VAL J 3 64  ? 116.987 44.292  25.621  1.000 80.950  ? 64  VAL JJJ CG2 1 
ATOM 15096 N N   . LYS J 3 65  ? 119.225 45.900  23.156  1.000 80.840  ? 65  LYS JJJ N   1 
ATOM 15097 C CA  . LYS J 3 65  ? 120.602 46.436  23.385  1.000 87.030  ? 65  LYS JJJ CA  1 
ATOM 15098 C C   . LYS J 3 65  ? 120.511 47.961  23.398  1.000 88.810  ? 65  LYS JJJ C   1 
ATOM 15099 O O   . LYS J 3 65  ? 119.882 48.520  22.496  1.000 90.890  ? 65  LYS JJJ O   1 
ATOM 15100 C CB  . LYS J 3 65  ? 121.594 45.973  22.311  1.000 85.410  ? 65  LYS JJJ CB  1 
ATOM 15101 N N   . GLY J 3 66  ? 121.051 48.607  24.423  1.000 92.370  ? 66  GLY JJJ N   1 
ATOM 15102 C CA  . GLY J 3 66  ? 121.162 50.073  24.455  1.000 95.480  ? 66  GLY JJJ CA  1 
ATOM 15103 C C   . GLY J 3 66  ? 119.922 50.781  24.987  1.000 100.610 ? 66  GLY JJJ C   1 
ATOM 15104 O O   . GLY J 3 66  ? 120.043 51.969  25.267  1.000 110.010 ? 66  GLY JJJ O   1 
ATOM 15105 N N   . ARG J 3 67  ? 118.784 50.102  25.155  1.000 96.000  ? 67  ARG JJJ N   1 
ATOM 15106 C CA  . ARG J 3 67  ? 117.514 50.740  25.616  1.000 88.230  ? 67  ARG JJJ CA  1 
ATOM 15107 C C   . ARG J 3 67  ? 117.192 50.293  27.047  1.000 84.220  ? 67  ARG JJJ C   1 
ATOM 15108 O O   . ARG J 3 67  ? 116.818 51.146  27.870  1.000 74.000  ? 67  ARG JJJ O   1 
ATOM 15109 C CB  . ARG J 3 67  ? 116.363 50.415  24.657  1.000 85.320  ? 67  ARG JJJ CB  1 
ATOM 15110 C CG  . ARG J 3 67  ? 116.650 50.809  23.214  1.000 81.030  ? 67  ARG JJJ CG  1 
ATOM 15111 C CD  . ARG J 3 67  ? 115.432 50.761  22.293  1.000 78.390  ? 67  ARG JJJ CD  1 
ATOM 15112 N NE  . ARG J 3 67  ? 114.959 49.403  22.090  1.000 77.430  ? 67  ARG JJJ NE  1 
ATOM 15113 C CZ  . ARG J 3 67  ? 113.812 48.905  22.555  1.000 79.380  ? 67  ARG JJJ CZ  1 
ATOM 15114 N NH1 . ARG J 3 67  ? 112.974 49.663  23.242  1.000 77.610  ? 67  ARG JJJ NH1 1 
ATOM 15115 N NH2 . ARG J 3 67  ? 113.506 47.639  22.320  1.000 75.190  ? 67  ARG JJJ NH2 1 
ATOM 15116 N N   . PHE J 3 68  ? 117.332 48.997  27.327  1.000 82.770  ? 68  PHE JJJ N   1 
ATOM 15117 C CA  . PHE J 3 68  ? 117.013 48.385  28.642  1.000 77.820  ? 68  PHE JJJ CA  1 
ATOM 15118 C C   . PHE J 3 68  ? 118.288 48.313  29.487  1.000 72.530  ? 68  PHE JJJ C   1 
ATOM 15119 O O   . PHE J 3 68  ? 119.389 48.218  28.922  1.000 65.970  ? 68  PHE JJJ O   1 
ATOM 15120 C CB  . PHE J 3 68  ? 116.400 47.008  28.425  1.000 79.280  ? 68  PHE JJJ CB  1 
ATOM 15121 C CG  . PHE J 3 68  ? 115.017 47.023  27.837  1.000 79.280  ? 68  PHE JJJ CG  1 
ATOM 15122 C CD1 . PHE J 3 68  ? 114.502 48.152  27.226  1.000 86.540  ? 68  PHE JJJ CD1 1 
ATOM 15123 C CD2 . PHE J 3 68  ? 114.233 45.883  27.873  1.000 87.120  ? 68  PHE JJJ CD2 1 
ATOM 15124 C CE1 . PHE J 3 68  ? 113.226 48.143  26.680  1.000 96.600  ? 68  PHE JJJ CE1 1 
ATOM 15125 C CE2 . PHE J 3 68  ? 112.958 45.874  27.329  1.000 92.620  ? 68  PHE JJJ CE2 1 
ATOM 15126 C CZ  . PHE J 3 68  ? 112.456 47.005  26.733  1.000 94.120  ? 68  PHE JJJ CZ  1 
ATOM 15127 N N   . THR J 3 69  ? 118.146 48.364  30.808  1.000 69.400  ? 69  THR JJJ N   1 
ATOM 15128 C CA  . THR J 3 69  ? 119.258 48.158  31.761  1.000 74.830  ? 69  THR JJJ CA  1 
ATOM 15129 C C   . THR J 3 69  ? 118.773 47.293  32.920  1.000 80.080  ? 69  THR JJJ C   1 
ATOM 15130 O O   . THR J 3 69  ? 117.793 47.668  33.588  1.000 71.950  ? 69  THR JJJ O   1 
ATOM 15131 C CB  . THR J 3 69  ? 119.822 49.496  32.238  1.000 75.080  ? 69  THR JJJ CB  1 
ATOM 15132 O OG1 . THR J 3 69  ? 119.991 50.254  31.046  1.000 76.510  ? 69  THR JJJ OG1 1 
ATOM 15133 C CG2 . THR J 3 69  ? 121.143 49.384  32.966  1.000 73.410  ? 69  THR JJJ CG2 1 
ATOM 15134 N N   . ILE J 3 70  ? 119.443 46.164  33.137  1.000 78.950  ? 70  ILE JJJ N   1 
ATOM 15135 C CA  . ILE J 3 70  ? 119.158 45.242  34.275  1.000 75.890  ? 70  ILE JJJ CA  1 
ATOM 15136 C C   . ILE J 3 70  ? 119.962 45.741  35.481  1.000 69.590  ? 70  ILE JJJ C   1 
ATOM 15137 O O   . ILE J 3 70  ? 121.058 46.294  35.281  1.000 66.800  ? 70  ILE JJJ O   1 
ATOM 15138 C CB  . ILE J 3 70  ? 119.492 43.789  33.881  1.000 69.840  ? 70  ILE JJJ CB  1 
ATOM 15139 C CG1 . ILE J 3 70  ? 118.799 42.774  34.790  1.000 63.410  ? 70  ILE JJJ CG1 1 
ATOM 15140 C CG2 . ILE J 3 70  ? 120.998 43.578  33.852  1.000 72.780  ? 70  ILE JJJ CG2 1 
ATOM 15141 C CD1 . ILE J 3 70  ? 118.881 41.361  34.273  1.000 62.320  ? 70  ILE JJJ CD1 1 
ATOM 15142 N N   . SER J 3 71  ? 119.430 45.576  36.680  1.000 63.240  ? 71  SER JJJ N   1 
ATOM 15143 C CA  . SER J 3 71  ? 120.161 45.896  37.931  1.000 66.000  ? 71  SER JJJ CA  1 
ATOM 15144 C C   . SER J 3 71  ? 119.559 45.084  39.081  1.000 69.900  ? 71  SER JJJ C   1 
ATOM 15145 O O   . SER J 3 71  ? 118.392 44.624  38.956  1.000 66.660  ? 71  SER JJJ O   1 
ATOM 15146 C CB  . SER J 3 71  ? 120.139 47.363  38.223  1.000 65.650  ? 71  SER JJJ CB  1 
ATOM 15147 O OG  . SER J 3 71  ? 118.828 47.791  38.600  1.000 70.830  ? 71  SER JJJ OG  1 
ATOM 15148 N N   . ARG J 3 72  ? 120.317 44.906  40.152  1.000 64.100  ? 72  ARG JJJ N   1 
ATOM 15149 C CA  . ARG J 3 72  ? 119.819 44.188  41.350  1.000 66.480  ? 72  ARG JJJ CA  1 
ATOM 15150 C C   . ARG J 3 72  ? 120.257 44.950  42.603  1.000 60.360  ? 72  ARG JJJ C   1 
ATOM 15151 O O   . ARG J 3 72  ? 121.264 45.675  42.536  1.000 60.800  ? 72  ARG JJJ O   1 
ATOM 15152 C CB  . ARG J 3 72  ? 120.333 42.743  41.337  1.000 73.680  ? 72  ARG JJJ CB  1 
ATOM 15153 C CG  . ARG J 3 72  ? 121.852 42.640  41.351  1.000 69.670  ? 72  ARG JJJ CG  1 
ATOM 15154 C CD  . ARG J 3 72  ? 122.354 41.233  41.133  1.000 64.610  ? 72  ARG JJJ CD  1 
ATOM 15155 N NE  . ARG J 3 72  ? 121.766 40.273  42.054  1.000 59.590  ? 72  ARG JJJ NE  1 
ATOM 15156 C CZ  . ARG J 3 72  ? 121.519 38.992  41.768  1.000 56.920  ? 72  ARG JJJ CZ  1 
ATOM 15157 N NH1 . ARG J 3 72  ? 120.961 38.221  42.683  1.000 57.670  ? 72  ARG JJJ NH1 1 
ATOM 15158 N NH2 . ARG J 3 72  ? 121.796 38.483  40.577  1.000 55.710  ? 72  ARG JJJ NH2 1 
ATOM 15159 N N   . ASP J 3 73  ? 119.493 44.803  43.685  1.000 60.340  ? 73  ASP JJJ N   1 
ATOM 15160 C CA  . ASP J 3 73  ? 119.835 45.275  45.050  1.000 65.130  ? 73  ASP JJJ CA  1 
ATOM 15161 C C   . ASP J 3 73  ? 119.766 44.050  45.967  1.000 64.620  ? 73  ASP JJJ C   1 
ATOM 15162 O O   . ASP J 3 73  ? 118.642 43.618  46.331  1.000 53.000  ? 73  ASP JJJ O   1 
ATOM 15163 C CB  . ASP J 3 73  ? 118.904 46.405  45.499  1.000 71.060  ? 73  ASP JJJ CB  1 
ATOM 15164 C CG  . ASP J 3 73  ? 119.275 47.076  46.815  1.000 69.530  ? 73  ASP JJJ CG  1 
ATOM 15165 O OD1 . ASP J 3 73  ? 120.162 46.574  47.519  1.000 70.660  ? 73  ASP JJJ OD1 1 
ATOM 15166 O OD2 . ASP J 3 73  ? 118.657 48.103  47.133  1.000 77.610  ? 73  ASP JJJ OD2 1 
ATOM 15167 N N   . ASN J 3 74  ? 120.935 43.488  46.280  1.000 62.460  ? 74  ASN JJJ N   1 
ATOM 15168 C CA  . ASN J 3 74  ? 121.041 42.200  47.015  1.000 62.620  ? 74  ASN JJJ CA  1 
ATOM 15169 C C   . ASN J 3 74  ? 120.616 42.431  48.463  1.000 62.840  ? 74  ASN JJJ C   1 
ATOM 15170 O O   . ASN J 3 74  ? 120.117 41.480  49.065  1.000 66.270  ? 74  ASN JJJ O   1 
ATOM 15171 C CB  . ASN J 3 74  ? 122.433 41.566  46.909  1.000 59.300  ? 74  ASN JJJ CB  1 
ATOM 15172 C CG  . ASN J 3 74  ? 122.664 40.822  45.609  1.000 52.670  ? 74  ASN JJJ CG  1 
ATOM 15173 O OD1 . ASN J 3 74  ? 121.728 40.576  44.832  1.000 44.550  ? 74  ASN JJJ OD1 1 
ATOM 15174 N ND2 . ASN J 3 74  ? 123.918 40.467  45.374  1.000 46.540  ? 74  ASN JJJ ND2 1 
ATOM 15175 N N   . ALA J 3 75  ? 120.763 43.652  48.980  1.000 66.810  ? 75  ALA JJJ N   1 
ATOM 15176 C CA  . ALA J 3 75  ? 120.269 44.021  50.323  1.000 65.810  ? 75  ALA JJJ CA  1 
ATOM 15177 C C   . ALA J 3 75  ? 118.736 44.056  50.329  1.000 68.230  ? 75  ALA JJJ C   1 
ATOM 15178 O O   . ALA J 3 75  ? 118.171 43.740  51.369  1.000 69.660  ? 75  ALA JJJ O   1 
ATOM 15179 C CB  . ALA J 3 75  ? 120.850 45.340  50.757  1.000 63.820  ? 75  ALA JJJ CB  1 
ATOM 15180 N N   . ARG J 3 76  ? 118.082 44.420  49.223  1.000 73.550  ? 76  ARG JJJ N   1 
ATOM 15181 C CA  . ARG J 3 76  ? 116.602 44.560  49.181  1.000 75.830  ? 76  ARG JJJ CA  1 
ATOM 15182 C C   . ARG J 3 76  ? 115.977 43.321  48.515  1.000 68.660  ? 76  ARG JJJ C   1 
ATOM 15183 O O   . ARG J 3 76  ? 114.760 43.358  48.292  1.000 67.420  ? 76  ARG JJJ O   1 
ATOM 15184 C CB  . ARG J 3 76  ? 116.203 45.872  48.476  1.000 82.630  ? 76  ARG JJJ CB  1 
ATOM 15185 C CG  . ARG J 3 76  ? 116.247 47.152  49.315  1.000 80.030  ? 76  ARG JJJ CG  1 
ATOM 15186 C CD  . ARG J 3 76  ? 115.698 48.355  48.515  1.000 77.340  ? 76  ARG JJJ CD  1 
ATOM 15187 N NE  . ARG J 3 76  ? 115.435 49.602  49.236  1.000 74.550  ? 76  ARG JJJ NE  1 
ATOM 15188 C CZ  . ARG J 3 76  ? 114.851 50.680  48.697  1.000 66.180  ? 76  ARG JJJ CZ  1 
ATOM 15189 N N   . ASN J 3 77  ? 116.750 42.262  48.223  1.000 62.780  ? 77  ASN JJJ N   1 
ATOM 15190 C CA  . ASN J 3 77  ? 116.246 40.995  47.607  1.000 57.520  ? 77  ASN JJJ CA  1 
ATOM 15191 C C   . ASN J 3 77  ? 115.425 41.303  46.345  1.000 55.960  ? 77  ASN JJJ C   1 
ATOM 15192 O O   . ASN J 3 77  ? 114.332 40.695  46.193  1.000 46.920  ? 77  ASN JJJ O   1 
ATOM 15193 C CB  . ASN J 3 77  ? 115.358 40.178  48.557  1.000 54.760  ? 77  ASN JJJ CB  1 
ATOM 15194 C CG  . ASN J 3 77  ? 116.132 39.343  49.554  1.000 57.090  ? 77  ASN JJJ CG  1 
ATOM 15195 O OD1 . ASN J 3 77  ? 116.933 38.495  49.183  1.000 67.170  ? 77  ASN JJJ OD1 1 
ATOM 15196 N ND2 . ASN J 3 77  ? 115.879 39.545  50.831  1.000 57.380  ? 77  ASN JJJ ND2 1 
ATOM 15197 N N   . SER J 3 78  ? 115.913 42.201  45.479  1.000 57.300  ? 78  SER JJJ N   1 
ATOM 15198 C CA  . SER J 3 78  ? 115.135 42.711  44.320  1.000 60.730  ? 78  SER JJJ CA  1 
ATOM 15199 C C   . SER J 3 78  ? 115.976 42.813  43.048  1.000 59.010  ? 78  SER JJJ C   1 
ATOM 15200 O O   . SER J 3 78  ? 117.105 43.325  43.097  1.000 53.290  ? 78  SER JJJ O   1 
ATOM 15201 C CB  . SER J 3 78  ? 114.519 44.028  44.648  1.000 62.080  ? 78  SER JJJ CB  1 
ATOM 15202 O OG  . SER J 3 78  ? 113.444 43.836  45.541  1.000 66.770  ? 78  SER JJJ OG  1 
ATOM 15203 N N   . LEU J 3 79  ? 115.388 42.366  41.943  1.000 60.990  ? 79  LEU JJJ N   1 
ATOM 15204 C CA  . LEU J 3 79  ? 115.927 42.523  40.573  1.000 65.040  ? 79  LEU JJJ CA  1 
ATOM 15205 C C   . LEU J 3 79  ? 115.108 43.601  39.876  1.000 69.930  ? 79  LEU JJJ C   1 
ATOM 15206 O O   . LEU J 3 79  ? 113.859 43.620  40.097  1.000 64.200  ? 79  LEU JJJ O   1 
ATOM 15207 C CB  . LEU J 3 79  ? 115.814 41.175  39.862  1.000 63.590  ? 79  LEU JJJ CB  1 
ATOM 15208 C CG  . LEU J 3 79  ? 116.075 41.200  38.364  1.000 63.360  ? 79  LEU JJJ CG  1 
ATOM 15209 C CD1 . LEU J 3 79  ? 117.571 41.226  38.079  1.000 67.350  ? 79  LEU JJJ CD1 1 
ATOM 15210 C CD2 . LEU J 3 79  ? 115.408 40.006  37.693  1.000 66.490  ? 79  LEU JJJ CD2 1 
ATOM 15211 N N   . TYR J 3 80  ? 115.755 44.462  39.083  1.000 75.140  ? 80  TYR JJJ N   1 
ATOM 15212 C CA  . TYR J 3 80  ? 115.091 45.574  38.352  1.000 73.600  ? 80  TYR JJJ CA  1 
ATOM 15213 C C   . TYR J 3 80  ? 115.441 45.510  36.863  1.000 69.860  ? 80  TYR JJJ C   1 
ATOM 15214 O O   . TYR J 3 80  ? 116.566 45.078  36.489  1.000 61.610  ? 80  TYR JJJ O   1 
ATOM 15215 C CB  . TYR J 3 80  ? 115.492 46.934  38.936  1.000 71.200  ? 80  TYR JJJ CB  1 
ATOM 15216 C CG  . TYR J 3 80  ? 115.316 47.062  40.432  1.000 67.700  ? 80  TYR JJJ CG  1 
ATOM 15217 C CD1 . TYR J 3 80  ? 114.058 47.122  41.019  1.000 62.060  ? 80  TYR JJJ CD1 1 
ATOM 15218 C CD2 . TYR J 3 80  ? 116.424 47.141  41.260  1.000 64.660  ? 80  TYR JJJ CD2 1 
ATOM 15219 C CE1 . TYR J 3 80  ? 113.913 47.246  42.394  1.000 65.110  ? 80  TYR JJJ CE1 1 
ATOM 15220 C CE2 . TYR J 3 80  ? 116.297 47.253  42.637  1.000 62.470  ? 80  TYR JJJ CE2 1 
ATOM 15221 C CZ  . TYR J 3 80  ? 115.039 47.301  43.211  1.000 68.900  ? 80  TYR JJJ CZ  1 
ATOM 15222 O OH  . TYR J 3 80  ? 114.940 47.406  44.575  1.000 70.470  ? 80  TYR JJJ OH  1 
ATOM 15223 N N   . LEU J 3 81  ? 114.496 45.963  36.037  1.000 70.980  ? 81  LEU JJJ N   1 
ATOM 15224 C CA  . LEU J 3 81  ? 114.724 46.242  34.593  1.000 75.280  ? 81  LEU JJJ CA  1 
ATOM 15225 C C   . LEU J 3 81  ? 114.267 47.671  34.293  1.000 72.070  ? 81  LEU JJJ C   1 
ATOM 15226 O O   . LEU J 3 81  ? 113.059 47.940  34.431  1.000 73.190  ? 81  LEU JJJ O   1 
ATOM 15227 C CB  . LEU J 3 81  ? 113.952 45.229  33.740  1.000 77.360  ? 81  LEU JJJ CB  1 
ATOM 15228 C CG  . LEU J 3 81  ? 114.176 45.354  32.232  1.000 74.180  ? 81  LEU JJJ CG  1 
ATOM 15229 C CD1 . LEU J 3 81  ? 115.646 45.122  31.880  1.000 67.520  ? 81  LEU JJJ CD1 1 
ATOM 15230 C CD2 . LEU J 3 81  ? 113.263 44.404  31.447  1.000 70.370  ? 81  LEU JJJ CD2 1 
ATOM 15231 N N   . GLN J 3 82  ? 115.210 48.528  33.902  1.000 73.040  ? 82  GLN JJJ N   1 
ATOM 15232 C CA  . GLN J 3 82  ? 114.956 49.906  33.420  1.000 80.720  ? 82  GLN JJJ CA  1 
ATOM 15233 C C   . GLN J 3 82  ? 114.683 49.873  31.914  1.000 79.180  ? 82  GLN JJJ C   1 
ATOM 15234 O O   . GLN J 3 82  ? 115.631 49.605  31.157  1.000 73.060  ? 82  GLN JJJ O   1 
ATOM 15235 C CB  . GLN J 3 82  ? 116.165 50.794  33.734  1.000 80.930  ? 82  GLN JJJ CB  1 
ATOM 15236 C CG  . GLN J 3 82  ? 115.947 52.259  33.411  1.000 78.890  ? 82  GLN JJJ CG  1 
ATOM 15237 C CD  . GLN J 3 82  ? 114.668 52.749  34.046  1.000 82.010  ? 82  GLN JJJ CD  1 
ATOM 15238 O OE1 . GLN J 3 82  ? 114.488 52.703  35.274  1.000 73.130  ? 82  GLN JJJ OE1 1 
ATOM 15239 N NE2 . GLN J 3 82  ? 113.743 53.163  33.190  1.000 74.080  ? 82  GLN JJJ NE2 1 
ATOM 15240 N N   . MET J 3 83  ? 113.445 50.145  31.502  1.000 79.710  ? 83  MET JJJ N   1 
ATOM 15241 C CA  . MET J 3 83  ? 113.014 50.098  30.079  1.000 82.880  ? 83  MET JJJ CA  1 
ATOM 15242 C C   . MET J 3 83  ? 112.845 51.536  29.561  1.000 89.680  ? 83  MET JJJ C   1 
ATOM 15243 O O   . MET J 3 83  ? 111.878 52.199  29.962  1.000 85.900  ? 83  MET JJJ O   1 
ATOM 15244 C CB  . MET J 3 83  ? 111.698 49.329  29.930  1.000 81.670  ? 83  MET JJJ CB  1 
ATOM 15245 C CG  . MET J 3 83  ? 111.761 47.912  30.453  1.000 77.180  ? 83  MET JJJ CG  1 
ATOM 15246 S SD  . MET J 3 83  ? 110.100 47.189  30.713  1.000 84.620  ? 83  MET JJJ SD  1 
ATOM 15247 C CE  . MET J 3 83  ? 109.740 46.642  29.048  1.000 81.570  ? 83  MET JJJ CE  1 
ATOM 15248 N N   . ASN J 3 84  ? 113.779 51.999  28.727  1.000 90.930  ? 84  ASN JJJ N   1 
ATOM 15249 C CA  . ASN J 3 84  ? 113.761 53.341  28.089  1.000 86.330  ? 84  ASN JJJ CA  1 
ATOM 15250 C C   . ASN J 3 84  ? 113.407 53.169  26.610  1.000 85.470  ? 84  ASN JJJ C   1 
ATOM 15251 O O   . ASN J 3 84  ? 113.601 52.057  26.094  1.000 93.250  ? 84  ASN JJJ O   1 
ATOM 15252 C CB  . ASN J 3 84  ? 115.098 54.065  28.244  1.000 75.040  ? 84  ASN JJJ CB  1 
ATOM 15253 C CG  . ASN J 3 84  ? 115.451 54.305  29.693  1.000 72.460  ? 84  ASN JJJ CG  1 
ATOM 15254 O OD1 . ASN J 3 84  ? 114.589 54.303  30.576  1.000 73.170  ? 84  ASN JJJ OD1 1 
ATOM 15255 N ND2 . ASN J 3 84  ? 116.730 54.507  29.957  1.000 69.680  ? 84  ASN JJJ ND2 1 
ATOM 15256 N N   . SER J 3 85  ? 112.932 54.233  25.959  1.000 71.420  ? 85  SER JJJ N   1 
ATOM 15257 C CA  . SER J 3 85  ? 112.704 54.300  24.493  1.000 68.050  ? 85  SER JJJ CA  1 
ATOM 15258 C C   . SER J 3 85  ? 111.768 53.167  24.061  1.000 67.480  ? 85  SER JJJ C   1 
ATOM 15259 O O   . SER J 3 85  ? 111.975 52.572  22.958  1.000 53.940  ? 85  SER JJJ O   1 
ATOM 15260 C CB  . SER J 3 85  ? 114.002 54.230  23.739  1.000 66.360  ? 85  SER JJJ CB  1 
ATOM 15261 O OG  . SER J 3 85  ? 114.974 55.100  24.281  1.000 61.250  ? 85  SER JJJ OG  1 
ATOM 15262 N N   . LEU J 3 86  ? 110.767 52.891  24.895  1.000 69.900  ? 86  LEU JJJ N   1 
ATOM 15263 C CA  . LEU J 3 86  ? 109.824 51.764  24.689  1.000 79.260  ? 86  LEU JJJ CA  1 
ATOM 15264 C C   . LEU J 3 86  ? 109.180 51.856  23.304  1.000 71.260  ? 86  LEU JJJ C   1 
ATOM 15265 O O   . LEU J 3 86  ? 108.888 52.974  22.853  1.000 71.050  ? 86  LEU JJJ O   1 
ATOM 15266 C CB  . LEU J 3 86  ? 108.789 51.793  25.816  1.000 84.210  ? 86  LEU JJJ CB  1 
ATOM 15267 C CG  . LEU J 3 86  ? 109.238 51.049  27.069  1.000 84.170  ? 86  LEU JJJ CG  1 
ATOM 15268 C CD1 . LEU J 3 86  ? 108.342 51.355  28.255  1.000 89.280  ? 86  LEU JJJ CD1 1 
ATOM 15269 C CD2 . LEU J 3 86  ? 109.269 49.554  26.802  1.000 83.930  ? 86  LEU JJJ CD2 1 
ATOM 15270 N N   . ARG J 3 87  ? 108.967 50.707  22.669  1.000 71.540  ? 87  ARG JJJ N   1 
ATOM 15271 C CA  . ARG J 3 87  ? 108.307 50.609  21.343  1.000 73.910  ? 87  ARG JJJ CA  1 
ATOM 15272 C C   . ARG J 3 87  ? 107.067 49.740  21.470  1.000 69.970  ? 87  ARG JJJ C   1 
ATOM 15273 O O   . ARG J 3 87  ? 106.893 49.105  22.519  1.000 67.610  ? 87  ARG JJJ O   1 
ATOM 15274 C CB  . ARG J 3 87  ? 109.270 50.019  20.316  1.000 76.820  ? 87  ARG JJJ CB  1 
ATOM 15275 C CG  . ARG J 3 87  ? 110.647 50.663  20.391  1.000 84.480  ? 87  ARG JJJ CG  1 
ATOM 15276 C CD  . ARG J 3 87  ? 111.592 49.907  19.499  1.000 85.020  ? 87  ARG JJJ CD  1 
ATOM 15277 N NE  . ARG J 3 87  ? 112.930 50.462  19.482  1.000 80.670  ? 87  ARG JJJ NE  1 
ATOM 15278 C CZ  . ARG J 3 87  ? 113.966 49.823  18.980  1.000 71.630  ? 87  ARG JJJ CZ  1 
ATOM 15279 N NH1 . ARG J 3 87  ? 113.807 48.610  18.482  1.000 68.410  ? 87  ARG JJJ NH1 1 
ATOM 15280 N NH2 . ARG J 3 87  ? 115.155 50.387  18.984  1.000 77.470  ? 87  ARG JJJ NH2 1 
ATOM 15281 N N   . VAL J 3 88  ? 106.240 49.741  20.435  1.000 80.230  ? 88  VAL JJJ N   1 
ATOM 15282 C CA  . VAL J 3 88  ? 104.977 48.947  20.383  1.000 93.290  ? 88  VAL JJJ CA  1 
ATOM 15283 C C   . VAL J 3 88  ? 105.336 47.454  20.506  1.000 98.160  ? 88  VAL JJJ C   1 
ATOM 15284 O O   . VAL J 3 88  ? 104.683 46.754  21.287  1.000 91.150  ? 88  VAL JJJ O   1 
ATOM 15285 C CB  . VAL J 3 88  ? 104.174 49.277  19.106  1.000 98.060  ? 88  VAL JJJ CB  1 
ATOM 15286 C CG1 . VAL J 3 88  ? 103.582 50.679  19.190  1.000 91.530  ? 88  VAL JJJ CG1 1 
ATOM 15287 C CG2 . VAL J 3 88  ? 104.979 49.118  17.815  1.000 101.090 ? 88  VAL JJJ CG2 1 
ATOM 15288 N N   . GLU J 3 89  ? 106.386 47.016  19.806  1.000 101.180 ? 89  GLU JJJ N   1 
ATOM 15289 C CA  . GLU J 3 89  ? 106.861 45.604  19.775  1.000 90.450  ? 89  GLU JJJ CA  1 
ATOM 15290 C C   . GLU J 3 89  ? 107.224 45.149  21.197  1.000 84.590  ? 89  GLU JJJ C   1 
ATOM 15291 O O   . GLU J 3 89  ? 107.017 43.958  21.484  1.000 79.680  ? 89  GLU JJJ O   1 
ATOM 15292 C CB  . GLU J 3 89  ? 108.062 45.415  18.844  1.000 89.870  ? 89  GLU JJJ CB  1 
ATOM 15293 C CG  . GLU J 3 89  ? 107.988 46.191  17.536  1.000 91.120  ? 89  GLU JJJ CG  1 
ATOM 15294 C CD  . GLU J 3 89  ? 108.669 47.561  17.510  1.000 99.760  ? 89  GLU JJJ CD  1 
ATOM 15295 O OE1 . GLU J 3 89  ? 109.663 47.762  18.224  1.000 100.450 ? 89  GLU JJJ OE1 1 
ATOM 15296 O OE2 . GLU J 3 89  ? 108.233 48.415  16.722  1.000 101.230 ? 89  GLU JJJ OE2 1 
ATOM 15297 N N   . ASP J 3 90  ? 107.695 46.048  22.070  1.000 77.930  ? 90  ASP JJJ N   1 
ATOM 15298 C CA  . ASP J 3 90  ? 108.100 45.702  23.463  1.000 76.450  ? 90  ASP JJJ CA  1 
ATOM 15299 C C   . ASP J 3 90  ? 106.887 45.265  24.303  1.000 79.560  ? 90  ASP JJJ C   1 
ATOM 15300 O O   . ASP J 3 90  ? 107.110 44.832  25.454  1.000 77.930  ? 90  ASP JJJ O   1 
ATOM 15301 C CB  . ASP J 3 90  ? 108.828 46.864  24.154  1.000 73.900  ? 90  ASP JJJ CB  1 
ATOM 15302 C CG  . ASP J 3 90  ? 110.170 47.201  23.526  1.000 74.520  ? 90  ASP JJJ CG  1 
ATOM 15303 O OD1 . ASP J 3 90  ? 110.750 46.295  22.849  1.000 71.510  ? 90  ASP JJJ OD1 1 
ATOM 15304 O OD2 . ASP J 3 90  ? 110.614 48.367  23.688  1.000 68.710  ? 90  ASP JJJ OD2 1 
ATOM 15305 N N   . THR J 3 91  ? 105.659 45.386  23.789  1.000 89.370  ? 91  THR JJJ N   1 
ATOM 15306 C CA  . THR J 3 91  ? 104.436 44.893  24.481  1.000 98.420  ? 91  THR JJJ CA  1 
ATOM 15307 C C   . THR J 3 91  ? 104.583 43.385  24.713  1.000 102.020 ? 91  THR JJJ C   1 
ATOM 15308 O O   . THR J 3 91  ? 104.789 42.646  23.714  1.000 105.840 ? 91  THR JJJ O   1 
ATOM 15309 C CB  . THR J 3 91  ? 103.144 45.131  23.686  1.000 96.340  ? 91  THR JJJ CB  1 
ATOM 15310 O OG1 . THR J 3 91  ? 103.306 44.531  22.401  1.000 101.050 ? 91  THR JJJ OG1 1 
ATOM 15311 C CG2 . THR J 3 91  ? 102.756 46.575  23.493  1.000 95.500  ? 91  THR JJJ CG2 1 
ATOM 15312 N N   . ALA J 3 92  ? 104.482 42.958  25.973  1.000 100.800 ? 92  ALA JJJ N   1 
ATOM 15313 C CA  . ALA J 3 92  ? 104.603 41.546  26.399  1.000 97.720  ? 92  ALA JJJ CA  1 
ATOM 15314 C C   . ALA J 3 92  ? 104.325 41.432  27.898  1.000 88.400  ? 92  ALA JJJ C   1 
ATOM 15315 O O   . ALA J 3 92  ? 104.299 42.470  28.584  1.000 87.020  ? 92  ALA JJJ O   1 
ATOM 15316 C CB  . ALA J 3 92  ? 105.988 41.039  26.083  1.000 104.470 ? 92  ALA JJJ CB  1 
ATOM 15317 N N   . VAL J 3 93  ? 104.235 40.189  28.378  1.000 73.570  ? 93  VAL JJJ N   1 
ATOM 15318 C CA  . VAL J 3 93  ? 104.152 39.946  29.842  1.000 70.100  ? 93  VAL JJJ CA  1 
ATOM 15319 C C   . VAL J 3 93  ? 105.607 39.681  30.199  1.000 64.580  ? 93  VAL JJJ C   1 
ATOM 15320 O O   . VAL J 3 93  ? 106.205 38.823  29.546  1.000 56.610  ? 93  VAL JJJ O   1 
ATOM 15321 C CB  . VAL J 3 93  ? 103.290 38.719  30.171  1.000 75.610  ? 93  VAL JJJ CB  1 
ATOM 15322 C CG1 . VAL J 3 93  ? 102.730 38.779  31.582  1.000 81.740  ? 93  VAL JJJ CG1 1 
ATOM 15323 C CG2 . VAL J 3 93  ? 102.178 38.520  29.157  1.000 75.160  ? 93  VAL JJJ CG2 1 
ATOM 15324 N N   . TYR J 3 94  ? 106.165 40.427  31.144  1.000 71.310  ? 94  TYR JJJ N   1 
ATOM 15325 C CA  . TYR J 3 94  ? 107.609 40.286  31.444  1.000 78.260  ? 94  TYR JJJ CA  1 
ATOM 15326 C C   . TYR J 3 94  ? 107.803 39.384  32.654  1.000 79.020  ? 94  TYR JJJ C   1 
ATOM 15327 O O   . TYR J 3 94  ? 107.292 39.707  33.730  1.000 81.510  ? 94  TYR JJJ O   1 
ATOM 15328 C CB  . TYR J 3 94  ? 108.269 41.648  31.640  1.000 80.960  ? 94  TYR JJJ CB  1 
ATOM 15329 C CG  . TYR J 3 94  ? 108.653 42.331  30.356  1.000 80.460  ? 94  TYR JJJ CG  1 
ATOM 15330 C CD1 . TYR J 3 94  ? 107.687 42.795  29.482  1.000 80.930  ? 94  TYR JJJ CD1 1 
ATOM 15331 C CD2 . TYR J 3 94  ? 109.981 42.503  30.011  1.000 83.250  ? 94  TYR JJJ CD2 1 
ATOM 15332 C CE1 . TYR J 3 94  ? 108.039 43.416  28.295  1.000 84.360  ? 94  TYR JJJ CE1 1 
ATOM 15333 C CE2 . TYR J 3 94  ? 110.340 43.125  28.829  1.000 84.100  ? 94  TYR JJJ CE2 1 
ATOM 15334 C CZ  . TYR J 3 94  ? 109.370 43.575  27.966  1.000 83.720  ? 94  TYR JJJ CZ  1 
ATOM 15335 O OH  . TYR J 3 94  ? 109.714 44.203  26.805  1.000 81.030  ? 94  TYR JJJ OH  1 
ATOM 15336 N N   . TYR J 3 95  ? 108.541 38.294  32.463  1.000 76.860  ? 95  TYR JJJ N   1 
ATOM 15337 C CA  . TYR J 3 95  ? 108.752 37.312  33.547  1.000 71.820  ? 95  TYR JJJ CA  1 
ATOM 15338 C C   . TYR J 3 95  ? 110.141 37.453  34.175  1.000 73.220  ? 95  TYR JJJ C   1 
ATOM 15339 O O   . TYR J 3 95  ? 111.069 37.872  33.474  1.000 61.220  ? 95  TYR JJJ O   1 
ATOM 15340 C CB  . TYR J 3 95  ? 108.517 35.902  33.009  1.000 63.310  ? 95  TYR JJJ CB  1 
ATOM 15341 C CG  . TYR J 3 95  ? 107.136 35.601  32.485  1.000 58.030  ? 95  TYR JJJ CG  1 
ATOM 15342 C CD1 . TYR J 3 95  ? 106.130 35.174  33.332  1.000 55.790  ? 95  TYR JJJ CD1 1 
ATOM 15343 C CD2 . TYR J 3 95  ? 106.847 35.690  31.135  1.000 60.250  ? 95  TYR JJJ CD2 1 
ATOM 15344 C CE1 . TYR J 3 95  ? 104.861 34.887  32.860  1.000 56.520  ? 95  TYR JJJ CE1 1 
ATOM 15345 C CE2 . TYR J 3 95  ? 105.585 35.402  30.646  1.000 55.690  ? 95  TYR JJJ CE2 1 
ATOM 15346 C CZ  . TYR J 3 95  ? 104.587 34.997  31.510  1.000 50.330  ? 95  TYR JJJ CZ  1 
ATOM 15347 N N   . CYS J 3 96  ? 110.262 37.129  35.460  1.000 74.970  ? 96  CYS JJJ N   1 
ATOM 15348 C CA  . CYS J 3 96  ? 111.553 37.184  36.188  1.000 72.340  ? 96  CYS JJJ CA  1 
ATOM 15349 C C   . CYS J 3 96  ? 111.948 35.759  36.532  1.000 67.760  ? 96  CYS JJJ C   1 
ATOM 15350 O O   . CYS J 3 96  ? 111.108 35.054  37.107  1.000 61.950  ? 96  CYS JJJ O   1 
ATOM 15351 C CB  . CYS J 3 96  ? 111.355 38.028  37.441  1.000 76.650  ? 96  CYS JJJ CB  1 
ATOM 15352 S SG  . CYS J 3 96  ? 112.814 38.347  38.459  1.000 73.640  ? 96  CYS JJJ SG  1 
ATOM 15353 N N   . ALA J 3 97  ? 113.148 35.339  36.146  1.000 62.570  ? 97  ALA JJJ N   1 
ATOM 15354 C CA  . ALA J 3 97  ? 113.507 33.920  36.320  1.000 58.710  ? 97  ALA JJJ CA  1 
ATOM 15355 C C   . ALA J 3 97  ? 114.892 33.734  36.924  1.000 58.560  ? 97  ALA JJJ C   1 
ATOM 15356 O O   . ALA J 3 97  ? 115.776 34.531  36.613  1.000 59.820  ? 97  ALA JJJ O   1 
ATOM 15357 C CB  . ALA J 3 97  ? 113.386 33.178  35.024  1.000 58.350  ? 97  ALA JJJ CB  1 
ATOM 15358 N N   . ARG J 3 98  ? 115.057 32.702  37.746  1.000 56.570  ? 98  ARG JJJ N   1 
ATOM 15359 C CA  . ARG J 3 98  ? 116.363 32.374  38.375  1.000 51.120  ? 98  ARG JJJ CA  1 
ATOM 15360 C C   . ARG J 3 98  ? 117.132 31.364  37.512  1.000 48.370  ? 98  ARG JJJ C   1 
ATOM 15361 O O   . ARG J 3 98  ? 116.489 30.457  36.937  1.000 44.340  ? 98  ARG JJJ O   1 
ATOM 15362 C CB  . ARG J 3 98  ? 116.187 31.757  39.761  1.000 48.790  ? 98  ARG JJJ CB  1 
ATOM 15363 C CG  . ARG J 3 98  ? 117.491 31.622  40.511  1.000 48.530  ? 98  ARG JJJ CG  1 
ATOM 15364 C CD  . ARG J 3 98  ? 117.302 31.017  41.883  1.000 47.110  ? 98  ARG JJJ CD  1 
ATOM 15365 N NE  . ARG J 3 98  ? 116.982 29.606  41.767  1.000 45.230  ? 98  ARG JJJ NE  1 
ATOM 15366 C CZ  . ARG J 3 98  ? 116.952 28.760  42.787  1.000 43.550  ? 98  ARG JJJ CZ  1 
ATOM 15367 N NH1 . ARG J 3 98  ? 117.215 29.169  44.021  1.000 42.740  ? 98  ARG JJJ NH1 1 
ATOM 15368 N NH2 . ARG J 3 98  ? 116.653 27.498  42.562  1.000 42.530  ? 98  ARG JJJ NH2 1 
ATOM 15369 N N   . TYR J 3 99  ? 118.457 31.527  37.427  1.000 43.320  ? 99  TYR JJJ N   1 
ATOM 15370 C CA  . TYR J 3 99  ? 119.403 30.513  36.905  1.000 40.330  ? 99  TYR JJJ CA  1 
ATOM 15371 C C   . TYR J 3 99  ? 120.274 30.024  38.058  1.000 41.690  ? 99  TYR JJJ C   1 
ATOM 15372 O O   . TYR J 3 99  ? 120.948 30.815  38.762  1.000 37.990  ? 99  TYR JJJ O   1 
ATOM 15373 C CB  . TYR J 3 99  ? 120.256 31.038  35.753  1.000 40.310  ? 99  TYR JJJ CB  1 
ATOM 15374 C CG  . TYR J 3 99  ? 121.474 30.199  35.455  1.000 39.580  ? 99  TYR JJJ CG  1 
ATOM 15375 C CD1 . TYR J 3 99  ? 122.613 30.298  36.238  1.000 37.820  ? 99  TYR JJJ CD1 1 
ATOM 15376 C CD2 . TYR J 3 99  ? 121.505 29.314  34.385  1.000 37.900  ? 99  TYR JJJ CD2 1 
ATOM 15377 C CE1 . TYR J 3 99  ? 123.740 29.541  35.967  1.000 37.420  ? 99  TYR JJJ CE1 1 
ATOM 15378 C CE2 . TYR J 3 99  ? 122.628 28.545  34.102  1.000 34.950  ? 99  TYR JJJ CE2 1 
ATOM 15379 C CZ  . TYR J 3 99  ? 123.752 28.654  34.899  1.000 35.690  ? 99  TYR JJJ CZ  1 
ATOM 15380 O OH  . TYR J 3 99  ? 124.852 27.870  34.673  1.000 36.650  ? 99  TYR JJJ OH  1 
ATOM 15381 N N   . ALA J 3 100 ? 120.241 28.711  38.242  1.000 44.680  ? 100 ALA JJJ N   1 
ATOM 15382 C CA  . ALA J 3 100 ? 121.108 27.981  39.182  1.000 45.580  ? 100 ALA JJJ CA  1 
ATOM 15383 C C   . ALA J 3 100 ? 122.007 27.059  38.367  1.000 41.590  ? 100 ALA JJJ C   1 
ATOM 15384 O O   . ALA J 3 100 ? 121.560 26.611  37.305  1.000 37.510  ? 100 ALA JJJ O   1 
ATOM 15385 C CB  . ALA J 3 100 ? 120.264 27.223  40.171  1.000 48.050  ? 100 ALA JJJ CB  1 
ATOM 15386 N N   . HIS J 3 101 ? 123.215 26.797  38.874  1.000 40.240  ? 101 HIS JJJ N   1 
ATOM 15387 C CA  . HIS J 3 101 ? 124.218 25.946  38.189  1.000 38.510  ? 101 HIS JJJ CA  1 
ATOM 15388 C C   . HIS J 3 101 ? 123.603 24.563  38.014  1.000 35.110  ? 101 HIS JJJ C   1 
ATOM 15389 O O   . HIS J 3 101 ? 122.904 24.108  38.954  1.000 33.970  ? 101 HIS JJJ O   1 
ATOM 15390 C CB  . HIS J 3 101 ? 125.532 25.859  38.961  1.000 35.920  ? 101 HIS JJJ CB  1 
ATOM 15391 C CG  . HIS J 3 101 ? 126.519 24.971  38.287  1.000 32.940  ? 101 HIS JJJ CG  1 
ATOM 15392 N ND1 . HIS J 3 101 ? 127.204 25.356  37.162  1.000 30.350  ? 101 HIS JJJ ND1 1 
ATOM 15393 C CD2 . HIS J 3 101 ? 126.894 23.703  38.541  1.000 31.320  ? 101 HIS JJJ CD2 1 
ATOM 15394 C CE1 . HIS J 3 101 ? 128.033 24.396  36.815  1.000 29.250  ? 101 HIS JJJ CE1 1 
ATOM 15395 N NE2 . HIS J 3 101 ? 127.837 23.360  37.622  1.000 28.670  ? 101 HIS JJJ NE2 1 
ATOM 15396 N N   . ASP J 3 102 ? 123.800 24.000  36.829  1.000 30.850  ? 102 ASP JJJ N   1 
ATOM 15397 C CA  . ASP J 3 102 ? 123.423 22.631  36.416  1.000 30.380  ? 102 ASP JJJ CA  1 
ATOM 15398 C C   . ASP J 3 102 ? 121.917 22.530  36.236  1.000 28.550  ? 102 ASP JJJ C   1 
ATOM 15399 O O   . ASP J 3 102 ? 121.540 21.792  35.303  1.000 27.030  ? 102 ASP JJJ O   1 
ATOM 15400 C CB  . ASP J 3 102 ? 124.002 21.552  37.336  1.000 31.370  ? 102 ASP JJJ CB  1 
ATOM 15401 C CG  . ASP J 3 102 ? 123.735 20.137  36.842  1.000 29.710  ? 102 ASP JJJ CG  1 
ATOM 15402 O OD1 . ASP J 3 102 ? 124.400 19.693  35.888  1.000 27.060  ? 102 ASP JJJ OD1 1 
ATOM 15403 O OD2 . ASP J 3 102 ? 122.879 19.478  37.442  1.000 29.910  ? 102 ASP JJJ OD2 1 
ATOM 15404 N N   . TRP J 3 103 ? 121.117 23.224  37.068  1.000 30.660  ? 103 TRP JJJ N   1 
ATOM 15405 C CA  . TRP J 3 103 ? 119.632 23.325  36.953  1.000 34.620  ? 103 TRP JJJ CA  1 
ATOM 15406 C C   . TRP J 3 103 ? 119.252 24.127  35.698  1.000 35.690  ? 103 TRP JJJ C   1 
ATOM 15407 O O   . TRP J 3 103 ? 118.276 23.767  34.987  1.000 31.150  ? 103 TRP JJJ O   1 
ATOM 15408 C CB  . TRP J 3 103 ? 119.014 23.977  38.197  1.000 34.710  ? 103 TRP JJJ CB  1 
ATOM 15409 C CG  . TRP J 3 103 ? 118.901 23.091  39.394  1.000 39.540  ? 103 TRP JJJ CG  1 
ATOM 15410 C CD1 . TRP J 3 103 ? 119.673 23.148  40.499  1.000 44.620  ? 103 TRP JJJ CD1 1 
ATOM 15411 C CD2 . TRP J 3 103 ? 117.955 22.033  39.637  1.000 41.190  ? 103 TRP JJJ CD2 1 
ATOM 15412 N NE1 . TRP J 3 103 ? 119.264 22.226  41.427  1.000 42.880  ? 103 TRP JJJ NE1 1 
ATOM 15413 C CE2 . TRP J 3 103 ? 118.217 21.519  40.917  1.000 40.360  ? 103 TRP JJJ CE2 1 
ATOM 15414 C CE3 . TRP J 3 103 ? 116.921 21.456  38.898  1.000 40.380  ? 103 TRP JJJ CE3 1 
ATOM 15415 C CZ2 . TRP J 3 103 ? 117.500 20.466  41.467  1.000 40.360  ? 103 TRP JJJ CZ2 1 
ATOM 15416 C CZ3 . TRP J 3 103 ? 116.210 20.416  39.438  1.000 38.420  ? 103 TRP JJJ CZ3 1 
ATOM 15417 C CH2 . TRP J 3 103 ? 116.491 19.928  40.706  1.000 40.220  ? 103 TRP JJJ CH2 1 
ATOM 15418 N N   . ASN J 3 104 ? 119.991 25.214  35.479  1.000 38.730  ? 104 ASN JJJ N   1 
ATOM 15419 C CA  . ASN J 3 104 ? 119.768 26.206  34.397  1.000 38.680  ? 104 ASN JJJ CA  1 
ATOM 15420 C C   . ASN J 3 104 ? 118.637 27.135  34.861  1.000 35.880  ? 104 ASN JJJ C   1 
ATOM 15421 O O   . ASN J 3 104 ? 118.559 27.387  36.065  1.000 34.690  ? 104 ASN JJJ O   1 
ATOM 15422 C CB  . ASN J 3 104 ? 119.650 25.487  33.050  1.000 40.040  ? 104 ASN JJJ CB  1 
ATOM 15423 C CG  . ASN J 3 104 ? 120.928 24.736  32.732  1.000 43.060  ? 104 ASN JJJ CG  1 
ATOM 15424 O OD1 . ASN J 3 104 ? 121.994 25.359  32.605  1.000 46.320  ? 104 ASN JJJ OD1 1 
ATOM 15425 N ND2 . ASN J 3 104 ? 120.845 23.412  32.666  1.000 43.060  ? 104 ASN JJJ ND2 1 
ATOM 15426 N N   . VAL J 3 105 ? 117.826 27.680  33.965  1.000 39.140  ? 105 VAL JJJ N   1 
ATOM 15427 C CA  . VAL J 3 105 ? 116.645 28.498  34.365  1.000 42.300  ? 105 VAL JJJ CA  1 
ATOM 15428 C C   . VAL J 3 105 ? 115.618 27.539  34.974  1.000 42.270  ? 105 VAL JJJ C   1 
ATOM 15429 O O   . VAL J 3 105 ? 115.236 26.584  34.261  1.000 42.210  ? 105 VAL JJJ O   1 
ATOM 15430 C CB  . VAL J 3 105 ? 116.092 29.304  33.175  1.000 44.950  ? 105 VAL JJJ CB  1 
ATOM 15431 C CG1 . VAL J 3 105 ? 114.699 29.840  33.440  1.000 45.490  ? 105 VAL JJJ CG1 1 
ATOM 15432 C CG2 . VAL J 3 105 ? 117.036 30.448  32.816  1.000 44.470  ? 105 VAL JJJ CG2 1 
ATOM 15433 N N   . ASP J 3 106 ? 115.230 27.760  36.241  1.000 41.320  ? 106 ASP JJJ N   1 
ATOM 15434 C CA  . ASP J 3 106 ? 114.341 26.841  37.005  1.000 42.300  ? 106 ASP JJJ CA  1 
ATOM 15435 C C   . ASP J 3 106 ? 113.034 27.538  37.432  1.000 45.390  ? 106 ASP JJJ C   1 
ATOM 15436 O O   . ASP J 3 106 ? 111.949 27.132  36.952  1.000 42.220  ? 106 ASP JJJ O   1 
ATOM 15437 C CB  . ASP J 3 106 ? 115.090 26.173  38.162  1.000 43.130  ? 106 ASP JJJ CB  1 
ATOM 15438 C CG  . ASP J 3 106 ? 115.782 27.068  39.176  1.000 45.570  ? 106 ASP JJJ CG  1 
ATOM 15439 O OD1 . ASP J 3 106 ? 115.572 28.288  39.150  1.000 52.560  ? 106 ASP JJJ OD1 1 
ATOM 15440 O OD2 . ASP J 3 106 ? 116.519 26.519  40.001  1.000 47.010  ? 106 ASP JJJ OD2 1 
ATOM 15441 N N   . TYR J 3 107 ? 113.109 28.519  38.326  1.000 50.930  ? 107 TYR JJJ N   1 
ATOM 15442 C CA  . TYR J 3 107 ? 111.919 29.182  38.905  1.000 50.420  ? 107 TYR JJJ CA  1 
ATOM 15443 C C   . TYR J 3 107 ? 111.593 30.450  38.118  1.000 55.420  ? 107 TYR JJJ C   1 
ATOM 15444 O O   . TYR J 3 107 ? 112.531 31.194  37.760  1.000 50.590  ? 107 TYR JJJ O   1 
ATOM 15445 C CB  . TYR J 3 107 ? 112.147 29.511  40.373  1.000 47.920  ? 107 TYR JJJ CB  1 
ATOM 15446 C CG  . TYR J 3 107 ? 112.150 28.303  41.270  1.000 46.430  ? 107 TYR JJJ CG  1 
ATOM 15447 C CD1 . TYR J 3 107 ? 110.964 27.683  41.632  1.000 48.520  ? 107 TYR JJJ CD1 1 
ATOM 15448 C CD2 . TYR J 3 107 ? 113.333 27.776  41.744  1.000 43.510  ? 107 TYR JJJ CD2 1 
ATOM 15449 C CE1 . TYR J 3 107 ? 110.956 26.564  42.443  1.000 48.750  ? 107 TYR JJJ CE1 1 
ATOM 15450 C CE2 . TYR J 3 107 ? 113.344 26.672  42.571  1.000 45.400  ? 107 TYR JJJ CE2 1 
ATOM 15451 C CZ  . TYR J 3 107 ? 112.150 26.068  42.924  1.000 46.800  ? 107 TYR JJJ CZ  1 
ATOM 15452 O OH  . TYR J 3 107 ? 112.121 25.005  43.770  1.000 49.760  ? 107 TYR JJJ OH  1 
ATOM 15453 N N   . TRP J 3 108 ? 110.295 30.664  37.876  1.000 58.510  ? 108 TRP JJJ N   1 
ATOM 15454 C CA  . TRP J 3 108 ? 109.729 31.866  37.215  1.000 62.780  ? 108 TRP JJJ CA  1 
ATOM 15455 C C   . TRP J 3 108 ? 108.786 32.584  38.188  1.000 68.150  ? 108 TRP JJJ C   1 
ATOM 15456 O O   . TRP J 3 108 ? 108.234 31.925  39.082  1.000 59.570  ? 108 TRP JJJ O   1 
ATOM 15457 C CB  . TRP J 3 108 ? 108.991 31.469  35.932  1.000 64.660  ? 108 TRP JJJ CB  1 
ATOM 15458 C CG  . TRP J 3 108 ? 109.837 30.826  34.878  1.000 64.340  ? 108 TRP JJJ CG  1 
ATOM 15459 C CD1 . TRP J 3 108 ? 110.465 29.621  34.973  1.000 63.110  ? 108 TRP JJJ CD1 1 
ATOM 15460 C CD2 . TRP J 3 108 ? 110.108 31.321  33.553  1.000 66.600  ? 108 TRP JJJ CD2 1 
ATOM 15461 N NE1 . TRP J 3 108 ? 111.094 29.333  33.795  1.000 61.320  ? 108 TRP JJJ NE1 1 
ATOM 15462 C CE2 . TRP J 3 108 ? 110.911 30.361  32.913  1.000 64.100  ? 108 TRP JJJ CE2 1 
ATOM 15463 C CE3 . TRP J 3 108 ? 109.777 32.486  32.851  1.000 75.400  ? 108 TRP JJJ CE3 1 
ATOM 15464 C CZ2 . TRP J 3 108 ? 111.396 30.533  31.618  1.000 71.740  ? 108 TRP JJJ CZ2 1 
ATOM 15465 C CZ3 . TRP J 3 108 ? 110.257 32.656  31.567  1.000 74.730  ? 108 TRP JJJ CZ3 1 
ATOM 15466 C CH2 . TRP J 3 108 ? 111.058 31.694  30.961  1.000 76.240  ? 108 TRP JJJ CH2 1 
ATOM 15467 N N   . GLY J 3 109 ? 108.610 33.894  38.014  1.000 71.520  ? 109 GLY JJJ N   1 
ATOM 15468 C CA  . GLY J 3 109 ? 107.555 34.660  38.698  1.000 73.150  ? 109 GLY JJJ CA  1 
ATOM 15469 C C   . GLY J 3 109 ? 106.243 34.540  37.947  1.000 72.940  ? 109 GLY JJJ C   1 
ATOM 15470 O O   . GLY J 3 109 ? 106.191 33.749  36.979  1.000 62.460  ? 109 GLY JJJ O   1 
ATOM 15471 N N   . GLN J 3 110 ? 105.226 35.300  38.368  1.000 78.250  ? 110 GLN JJJ N   1 
ATOM 15472 C CA  . GLN J 3 110 ? 103.846 35.234  37.813  1.000 80.510  ? 110 GLN JJJ CA  1 
ATOM 15473 C C   . GLN J 3 110 ? 103.811 36.029  36.509  1.000 73.710  ? 110 GLN JJJ C   1 
ATOM 15474 O O   . GLN J 3 110 ? 102.902 35.791  35.696  1.000 77.090  ? 110 GLN JJJ O   1 
ATOM 15475 C CB  . GLN J 3 110 ? 102.813 35.785  38.804  1.000 85.490  ? 110 GLN JJJ CB  1 
ATOM 15476 C CG  . GLN J 3 110 ? 102.673 34.986  40.097  1.000 89.120  ? 110 GLN JJJ CG  1 
ATOM 15477 C CD  . GLN J 3 110 ? 103.682 35.383  41.145  1.000 89.790  ? 110 GLN JJJ CD  1 
ATOM 15478 O OE1 . GLN J 3 110 ? 104.317 36.433  41.065  1.000 111.330 ? 110 GLN JJJ OE1 1 
ATOM 15479 N NE2 . GLN J 3 110 ? 103.833 34.548  42.156  1.000 86.210  ? 110 GLN JJJ NE2 1 
ATOM 15480 N N   . GLY J 3 111 ? 104.782 36.925  36.328  1.000 68.500  ? 111 GLY JJJ N   1 
ATOM 15481 C CA  . GLY J 3 111 ? 104.866 37.865  35.192  1.000 73.040  ? 111 GLY JJJ CA  1 
ATOM 15482 C C   . GLY J 3 111 ? 104.083 39.131  35.472  1.000 70.920  ? 111 GLY JJJ C   1 
ATOM 15483 O O   . GLY J 3 111 ? 103.142 39.061  36.282  1.000 77.390  ? 111 GLY JJJ O   1 
ATOM 15484 N N   . THR J 3 112 ? 104.465 40.245  34.843  1.000 67.530  ? 112 THR JJJ N   1 
ATOM 15485 C CA  . THR J 3 112 ? 103.756 41.550  34.936  1.000 66.580  ? 112 THR JJJ CA  1 
ATOM 15486 C C   . THR J 3 112 ? 103.553 42.080  33.520  1.000 72.150  ? 112 THR JJJ C   1 
ATOM 15487 O O   . THR J 3 112 ? 104.510 42.010  32.731  1.000 72.320  ? 112 THR JJJ O   1 
ATOM 15488 C CB  . THR J 3 112 ? 104.521 42.553  35.805  1.000 63.340  ? 112 THR JJJ CB  1 
ATOM 15489 O OG1 . THR J 3 112 ? 103.619 43.638  36.015  1.000 66.140  ? 112 THR JJJ OG1 1 
ATOM 15490 C CG2 . THR J 3 112 ? 105.814 43.040  35.180  1.000 57.860  ? 112 THR JJJ CG2 1 
ATOM 15491 N N   . LEU J 3 113 ? 102.356 42.575  33.203  1.000 78.700  ? 113 LEU JJJ N   1 
ATOM 15492 C CA  . LEU J 3 113 ? 102.027 42.985  31.810  1.000 80.030  ? 113 LEU JJJ CA  1 
ATOM 15493 C C   . LEU J 3 113 ? 102.543 44.406  31.558  1.000 77.460  ? 113 LEU JJJ C   1 
ATOM 15494 O O   . LEU J 3 113 ? 102.219 45.302  32.360  1.000 73.440  ? 113 LEU JJJ O   1 
ATOM 15495 C CB  . LEU J 3 113 ? 100.520 42.911  31.560  1.000 76.590  ? 113 LEU JJJ CB  1 
ATOM 15496 C CG  . LEU J 3 113 ? 100.105 43.353  30.157  1.000 80.110  ? 113 LEU JJJ CG  1 
ATOM 15497 C CD1 . LEU J 3 113 ? 100.841 42.562  29.096  1.000 75.270  ? 113 LEU JJJ CD1 1 
ATOM 15498 C CD2 . LEU J 3 113 ? 98.608  43.224  29.949  1.000 88.970  ? 113 LEU JJJ CD2 1 
ATOM 15499 N N   . VAL J 3 114 ? 103.309 44.573  30.479  1.000 75.850  ? 114 VAL JJJ N   1 
ATOM 15500 C CA  . VAL J 3 114 ? 103.738 45.889  29.936  1.000 85.730  ? 114 VAL JJJ CA  1 
ATOM 15501 C C   . VAL J 3 114 ? 103.073 46.056  28.574  1.000 95.290  ? 114 VAL JJJ C   1 
ATOM 15502 O O   . VAL J 3 114 ? 103.440 45.316  27.636  1.000 94.230  ? 114 VAL JJJ O   1 
ATOM 15503 C CB  . VAL J 3 114 ? 105.270 45.994  29.813  1.000 90.790  ? 114 VAL JJJ CB  1 
ATOM 15504 C CG1 . VAL J 3 114 ? 105.705 47.185  28.965  1.000 89.470  ? 114 VAL JJJ CG1 1 
ATOM 15505 C CG2 . VAL J 3 114 ? 105.937 46.043  31.177  1.000 91.560  ? 114 VAL JJJ CG2 1 
ATOM 15506 N N   . THR J 3 115 ? 102.129 46.994  28.475  1.000 94.000  ? 115 THR JJJ N   1 
ATOM 15507 C CA  . THR J 3 115 ? 101.451 47.369  27.208  1.000 83.880  ? 115 THR JJJ CA  1 
ATOM 15508 C C   . THR J 3 115 ? 101.942 48.749  26.764  1.000 83.340  ? 115 THR JJJ C   1 
ATOM 15509 O O   . THR J 3 115 ? 101.754 49.720  27.522  1.000 97.100  ? 115 THR JJJ O   1 
ATOM 15510 C CB  . THR J 3 115 ? 99.932  47.318  27.367  1.000 76.850  ? 115 THR JJJ CB  1 
ATOM 15511 O OG1 . THR J 3 115 ? 99.633  46.283  28.311  1.000 66.110  ? 115 THR JJJ OG1 1 
ATOM 15512 C CG2 . THR J 3 115 ? 99.253  47.075  26.036  1.000 71.290  ? 115 THR JJJ CG2 1 
ATOM 15513 N N   . VAL J 3 116 ? 102.579 48.810  25.595  1.000 80.170  ? 116 VAL JJJ N   1 
ATOM 15514 C CA  . VAL J 3 116 ? 103.086 50.063  24.963  1.000 91.300  ? 116 VAL JJJ CA  1 
ATOM 15515 C C   . VAL J 3 116 ? 102.194 50.427  23.772  1.000 103.640 ? 116 VAL JJJ C   1 
ATOM 15516 O O   . VAL J 3 116 ? 102.297 49.750  22.719  1.000 97.390  ? 116 VAL JJJ O   1 
ATOM 15517 C CB  . VAL J 3 116 ? 104.547 49.899  24.519  1.000 93.160  ? 116 VAL JJJ CB  1 
ATOM 15518 C CG1 . VAL J 3 116 ? 104.997 51.061  23.654  1.000 96.920  ? 116 VAL JJJ CG1 1 
ATOM 15519 C CG2 . VAL J 3 116 ? 105.485 49.723  25.694  1.000 95.290  ? 116 VAL JJJ CG2 1 
ATOM 15520 N N   . SER J 3 117 ? 101.373 51.466  23.945  1.000 118.070 ? 117 SER JJJ N   1 
ATOM 15521 C CA  . SER J 3 117 ? 100.340 51.940  22.984  1.000 116.020 ? 117 SER JJJ CA  1 
ATOM 15522 C C   . SER J 3 117 ? 100.190 53.458  23.152  1.000 121.050 ? 117 SER JJJ C   1 
ATOM 15523 O O   . SER J 3 117 ? 100.465 53.939  24.268  1.000 115.350 ? 117 SER JJJ O   1 
ATOM 15524 C CB  . SER J 3 117 ? 99.024  51.221  23.207  1.000 110.040 ? 117 SER JJJ CB  1 
ATOM 15525 O OG  . SER J 3 117 ? 98.067  51.598  22.236  1.000 111.080 ? 117 SER JJJ OG  1 
ATOM 15526 N N   . SER J 3 118 ? 99.916  54.197  22.066  1.000 124.330 ? 118 SER JJJ N   1 
ATOM 15527 C CA  . SER J 3 118 ? 99.605  55.656  22.083  1.000 109.700 ? 118 SER JJJ CA  1 
ATOM 15528 C C   . SER J 3 118 ? 98.197  55.867  22.654  1.000 98.530  ? 118 SER JJJ C   1 
ATOM 15529 O O   . SER J 3 118 ? 97.985  56.888  23.345  1.000 96.120  ? 118 SER JJJ O   1 
ATOM 15530 C CB  . SER J 3 118 ? 99.748  56.281  20.718  1.000 98.340  ? 118 SER JJJ CB  1 
ATOM 15531 O OG  . SER J 3 118 ? 101.118 56.421  20.365  1.000 83.680  ? 118 SER JJJ OG  1 
ATOM 15532 N N   . ALA J 3 119 ? 97.302  54.890  22.441  1.000 91.950  ? 119 ALA JJJ N   1 
ATOM 15533 C CA  . ALA J 3 119 ? 95.967  54.770  23.086  1.000 85.780  ? 119 ALA JJJ CA  1 
ATOM 15534 C C   . ALA J 3 119 ? 96.098  54.987  24.602  1.000 83.640  ? 119 ALA JJJ C   1 
ATOM 15535 O O   . ALA J 3 119 ? 97.081  54.506  25.201  1.000 83.520  ? 119 ALA JJJ O   1 
ATOM 15536 C CB  . ALA J 3 119 ? 95.355  53.421  22.777  1.000 77.150  ? 119 ALA JJJ CB  1 
ATOM 15537 N N   . SER J 3 120 ? 95.120  55.672  25.196  1.000 82.930  ? 120 SER JJJ N   1 
ATOM 15538 C CA  . SER J 3 120 ? 95.059  56.040  26.637  1.000 82.500  ? 120 SER JJJ CA  1 
ATOM 15539 C C   . SER J 3 120 ? 94.124  55.083  27.391  1.000 81.590  ? 120 SER JJJ C   1 
ATOM 15540 O O   . SER J 3 120 ? 93.399  54.311  26.740  1.000 68.840  ? 120 SER JJJ O   1 
ATOM 15541 C CB  . SER J 3 120 ? 94.633  57.469  26.797  1.000 80.300  ? 120 SER JJJ CB  1 
ATOM 15542 O OG  . SER J 3 120 ? 95.321  58.314  25.890  1.000 83.460  ? 120 SER JJJ OG  1 
ATOM 15543 N N   . THR J 3 121 ? 94.143  55.162  28.720  1.000 81.240  ? 121 THR JJJ N   1 
ATOM 15544 C CA  . THR J 3 121 ? 93.646  54.146  29.687  1.000 86.120  ? 121 THR JJJ CA  1 
ATOM 15545 C C   . THR J 3 121 ? 92.110  54.233  29.816  1.000 82.090  ? 121 THR JJJ C   1 
ATOM 15546 O O   . THR J 3 121 ? 91.662  54.823  30.819  1.000 76.420  ? 121 THR JJJ O   1 
ATOM 15547 C CB  . THR J 3 121 ? 94.392  54.361  31.023  1.000 88.650  ? 121 THR JJJ CB  1 
ATOM 15548 O OG1 . THR J 3 121 ? 95.808  54.478  30.829  1.000 76.470  ? 121 THR JJJ OG1 1 
ATOM 15549 C CG2 . THR J 3 121 ? 94.118  53.272  32.038  1.000 93.280  ? 121 THR JJJ CG2 1 
ATOM 15550 N N   . LYS J 3 122 ? 91.331  53.699  28.859  1.000 87.510  ? 122 LYS JJJ N   1 
ATOM 15551 C CA  . LYS J 3 122 ? 89.835  53.834  28.829  1.000 101.500 ? 122 LYS JJJ CA  1 
ATOM 15552 C C   . LYS J 3 122 ? 89.206  52.966  29.931  1.000 119.910 ? 122 LYS JJJ C   1 
ATOM 15553 O O   . LYS J 3 122 ? 89.630  51.804  30.067  1.000 129.020 ? 122 LYS JJJ O   1 
ATOM 15554 C CB  . LYS J 3 122 ? 89.248  53.497  27.453  1.000 87.990  ? 122 LYS JJJ CB  1 
ATOM 15555 N N   . GLY J 3 123 ? 88.313  53.542  30.743  1.000 133.060 ? 123 GLY JJJ N   1 
ATOM 15556 C CA  . GLY J 3 123 ? 87.650  52.846  31.863  1.000 116.480 ? 123 GLY JJJ CA  1 
ATOM 15557 C C   . GLY J 3 123 ? 86.495  52.009  31.340  1.000 111.420 ? 123 GLY JJJ C   1 
ATOM 15558 O O   . GLY J 3 123 ? 85.945  52.344  30.299  1.000 106.770 ? 123 GLY JJJ O   1 
ATOM 15559 N N   . PRO J 3 124 ? 86.121  50.894  32.009  1.000 114.490 ? 124 PRO JJJ N   1 
ATOM 15560 C CA  . PRO J 3 124 ? 84.985  50.074  31.581  1.000 119.950 ? 124 PRO JJJ CA  1 
ATOM 15561 C C   . PRO J 3 124 ? 83.637  50.696  31.961  1.000 112.710 ? 124 PRO JJJ C   1 
ATOM 15562 O O   . PRO J 3 124 ? 83.622  51.673  32.691  1.000 114.590 ? 124 PRO JJJ O   1 
ATOM 15563 C CB  . PRO J 3 124 ? 85.163  48.758  32.356  1.000 116.860 ? 124 PRO JJJ CB  1 
ATOM 15564 C CG  . PRO J 3 124 ? 85.889  49.192  33.622  1.000 121.290 ? 124 PRO JJJ CG  1 
ATOM 15565 C CD  . PRO J 3 124 ? 86.777  50.355  33.208  1.000 118.650 ? 124 PRO JJJ CD  1 
ATOM 15566 N N   . SER J 3 125 ? 82.553  50.118  31.440  1.000 98.980  ? 125 SER JJJ N   1 
ATOM 15567 C CA  . SER J 3 125 ? 81.146  50.415  31.803  1.000 103.010 ? 125 SER JJJ CA  1 
ATOM 15568 C C   . SER J 3 125 ? 80.415  49.078  31.995  1.000 114.710 ? 125 SER JJJ C   1 
ATOM 15569 O O   . SER J 3 125 ? 80.562  48.210  31.120  1.000 124.350 ? 125 SER JJJ O   1 
ATOM 15570 C CB  . SER J 3 125 ? 80.480  51.284  30.745  1.000 101.950 ? 125 SER JJJ CB  1 
ATOM 15571 O OG  . SER J 3 125 ? 80.841  52.658  30.874  1.000 89.130  ? 125 SER JJJ OG  1 
ATOM 15572 N N   . VAL J 3 126 ? 79.665  48.907  33.095  1.000 109.010 ? 126 VAL JJJ N   1 
ATOM 15573 C CA  . VAL J 3 126 ? 79.034  47.606  33.488  1.000 101.550 ? 126 VAL JJJ CA  1 
ATOM 15574 C C   . VAL J 3 126 ? 77.537  47.617  33.137  1.000 103.470 ? 126 VAL JJJ C   1 
ATOM 15575 O O   . VAL J 3 126 ? 76.915  48.691  33.192  1.000 98.180  ? 126 VAL JJJ O   1 
ATOM 15576 C CB  . VAL J 3 126 ? 79.275  47.287  34.978  1.000 88.610  ? 126 VAL JJJ CB  1 
ATOM 15577 N N   . PHE J 3 127 ? 77.008  46.437  32.767  1.000 107.140 ? 127 PHE JJJ N   1 
ATOM 15578 C CA  . PHE J 3 127 ? 75.591  46.109  32.414  1.000 106.330 ? 127 PHE JJJ CA  1 
ATOM 15579 C C   . PHE J 3 127 ? 74.866  47.366  31.894  1.000 103.860 ? 127 PHE JJJ C   1 
ATOM 15580 O O   . PHE J 3 127 ? 74.871  47.620  30.657  1.000 76.700  ? 127 PHE JJJ O   1 
ATOM 15581 C CB  . PHE J 3 127 ? 74.879  45.425  33.602  1.000 99.510  ? 127 PHE JJJ CB  1 
ATOM 15582 C CG  . PHE J 3 127 ? 73.846  44.367  33.258  1.000 100.820 ? 127 PHE JJJ CG  1 
ATOM 15583 C CD1 . PHE J 3 127 ? 74.210  43.167  32.648  1.000 97.340  ? 127 PHE JJJ CD1 1 
ATOM 15584 C CD2 . PHE J 3 127 ? 72.502  44.555  33.560  1.000 92.400  ? 127 PHE JJJ CD2 1 
ATOM 15585 C CE1 . PHE J 3 127 ? 73.269  42.192  32.340  1.000 83.750  ? 127 PHE JJJ CE1 1 
ATOM 15586 C CE2 . PHE J 3 127 ? 71.563  43.580  33.249  1.000 88.500  ? 127 PHE JJJ CE2 1 
ATOM 15587 C CZ  . PHE J 3 127 ? 71.948  42.400  32.643  1.000 84.710  ? 127 PHE JJJ CZ  1 
ATOM 15588 N N   . ALA J 3 142 ? 68.999  35.339  30.902  1.000 111.900 ? 147 ALA JJJ N   1 
ATOM 15589 C CA  . ALA J 3 142 ? 70.361  35.841  31.207  1.000 113.430 ? 147 ALA JJJ CA  1 
ATOM 15590 C C   . ALA J 3 142 ? 70.546  35.935  32.732  1.000 125.000 ? 147 ALA JJJ C   1 
ATOM 15591 O O   . ALA J 3 142 ? 69.665  36.530  33.397  1.000 140.090 ? 147 ALA JJJ O   1 
ATOM 15592 C CB  . ALA J 3 142 ? 70.583  37.173  30.523  1.000 104.150 ? 147 ALA JJJ CB  1 
ATOM 15593 N N   . LEU J 3 143 ? 71.633  35.349  33.266  1.000 116.950 ? 148 LEU JJJ N   1 
ATOM 15594 C CA  . LEU J 3 143 ? 72.052  35.432  34.697  1.000 103.830 ? 148 LEU JJJ CA  1 
ATOM 15595 C C   . LEU J 3 143 ? 73.493  35.964  34.790  1.000 112.740 ? 148 LEU JJJ C   1 
ATOM 15596 O O   . LEU J 3 143 ? 74.402  35.113  34.765  1.000 128.290 ? 148 LEU JJJ O   1 
ATOM 15597 C CB  . LEU J 3 143 ? 71.942  34.031  35.312  1.000 82.590  ? 148 LEU JJJ CB  1 
ATOM 15598 N N   . GLY J 3 144 ? 73.688  37.296  34.873  1.000 114.150 ? 149 GLY JJJ N   1 
ATOM 15599 C CA  . GLY J 3 144 ? 75.003  37.952  35.068  1.000 116.460 ? 149 GLY JJJ CA  1 
ATOM 15600 C C   . GLY J 3 144 ? 75.067  39.405  34.582  1.000 123.950 ? 149 GLY JJJ C   1 
ATOM 15601 O O   . GLY J 3 144 ? 74.001  39.974  34.219  1.000 103.020 ? 149 GLY JJJ O   1 
ATOM 15602 N N   . CYS J 3 145 ? 76.286  39.980  34.578  1.000 137.660 ? 150 CYS JJJ N   1 
ATOM 15603 C CA  . CYS J 3 145 ? 76.621  41.394  34.211  1.000 139.790 ? 150 CYS JJJ CA  1 
ATOM 15604 C C   . CYS J 3 145 ? 77.762  41.431  33.173  1.000 138.870 ? 150 CYS JJJ C   1 
ATOM 15605 O O   . CYS J 3 145 ? 78.536  40.466  33.129  1.000 126.720 ? 150 CYS JJJ O   1 
ATOM 15606 C CB  . CYS J 3 145 ? 76.956  42.251  35.436  1.000 139.470 ? 150 CYS JJJ CB  1 
ATOM 15607 S SG  . CYS J 3 145 ? 78.221  41.580  36.555  1.000 155.660 ? 150 CYS JJJ SG  1 
ATOM 15608 N N   . LEU J 3 146 ? 77.846  42.506  32.372  1.000 138.880 ? 151 LEU JJJ N   1 
ATOM 15609 C CA  . LEU J 3 146 ? 78.694  42.654  31.148  1.000 122.020 ? 151 LEU JJJ CA  1 
ATOM 15610 C C   . LEU J 3 146 ? 79.666  43.832  31.325  1.000 121.380 ? 151 LEU JJJ C   1 
ATOM 15611 O O   . LEU J 3 146 ? 79.260  44.818  31.975  1.000 119.440 ? 151 LEU JJJ O   1 
ATOM 15612 C CB  . LEU J 3 146 ? 77.762  42.897  29.952  1.000 120.890 ? 151 LEU JJJ CB  1 
ATOM 15613 C CG  . LEU J 3 146 ? 78.438  43.155  28.592  1.000 120.320 ? 151 LEU JJJ CG  1 
ATOM 15614 C CD1 . LEU J 3 146 ? 77.625  42.534  27.463  1.000 110.910 ? 151 LEU JJJ CD1 1 
ATOM 15615 C CD2 . LEU J 3 146 ? 78.649  44.643  28.325  1.000 111.630 ? 151 LEU JJJ CD2 1 
ATOM 15616 N N   . VAL J 3 147 ? 80.881  43.751  30.761  1.000 117.830 ? 152 VAL JJJ N   1 
ATOM 15617 C CA  . VAL J 3 147 ? 81.912  44.831  30.843  1.000 123.310 ? 152 VAL JJJ CA  1 
ATOM 15618 C C   . VAL J 3 147 ? 82.281  45.296  29.421  1.000 129.610 ? 152 VAL JJJ C   1 
ATOM 15619 O O   . VAL J 3 147 ? 82.887  44.501  28.669  1.000 115.210 ? 152 VAL JJJ O   1 
ATOM 15620 C CB  . VAL J 3 147 ? 83.125  44.388  31.689  1.000 123.330 ? 152 VAL JJJ CB  1 
ATOM 15621 C CG1 . VAL J 3 147 ? 84.194  45.468  31.847  1.000 128.940 ? 152 VAL JJJ CG1 1 
ATOM 15622 C CG2 . VAL J 3 147 ? 82.682  43.943  33.072  1.000 116.120 ? 152 VAL JJJ CG2 1 
ATOM 15623 N N   . LYS J 3 148 ? 81.893  46.535  29.072  1.000 137.080 ? 153 LYS JJJ N   1 
ATOM 15624 C CA  . LYS J 3 148 ? 82.056  47.123  27.715  1.000 129.830 ? 153 LYS JJJ CA  1 
ATOM 15625 C C   . LYS J 3 148 ? 83.187  48.171  27.668  1.000 125.540 ? 153 LYS JJJ C   1 
ATOM 15626 O O   . LYS J 3 148 ? 83.422  48.879  28.682  1.000 99.240  ? 153 LYS JJJ O   1 
ATOM 15627 C CB  . LYS J 3 148 ? 80.730  47.745  27.270  1.000 120.160 ? 153 LYS JJJ CB  1 
ATOM 15628 N N   . ASP J 3 149 ? 83.857  48.210  26.509  1.000 123.750 ? 154 ASP JJJ N   1 
ATOM 15629 C CA  . ASP J 3 149 ? 84.827  49.230  26.022  1.000 115.110 ? 154 ASP JJJ CA  1 
ATOM 15630 C C   . ASP J 3 149 ? 85.781  49.692  27.142  1.000 116.100 ? 154 ASP JJJ C   1 
ATOM 15631 O O   . ASP J 3 149 ? 85.656  50.849  27.596  1.000 109.400 ? 154 ASP JJJ O   1 
ATOM 15632 C CB  . ASP J 3 149 ? 84.072  50.360  25.320  1.000 100.300 ? 154 ASP JJJ CB  1 
ATOM 15633 N N   . TYR J 3 150 ? 86.743  48.833  27.511  1.000 114.530 ? 155 TYR JJJ N   1 
ATOM 15634 C CA  . TYR J 3 150 ? 87.855  49.105  28.470  1.000 111.680 ? 155 TYR JJJ CA  1 
ATOM 15635 C C   . TYR J 3 150 ? 89.211  48.806  27.812  1.000 99.230  ? 155 TYR JJJ C   1 
ATOM 15636 O O   . TYR J 3 150 ? 89.236  48.077  26.806  1.000 87.750  ? 155 TYR JJJ O   1 
ATOM 15637 C CB  . TYR J 3 150 ? 87.684  48.269  29.745  1.000 121.380 ? 155 TYR JJJ CB  1 
ATOM 15638 C CG  . TYR J 3 150 ? 87.956  46.792  29.619  1.000 117.490 ? 155 TYR JJJ CG  1 
ATOM 15639 C CD1 . TYR J 3 150 ? 89.246  46.290  29.676  1.000 115.090 ? 155 TYR JJJ CD1 1 
ATOM 15640 C CD2 . TYR J 3 150 ? 86.917  45.885  29.479  1.000 112.050 ? 155 TYR JJJ CD2 1 
ATOM 15641 C CE1 . TYR J 3 150 ? 89.499  44.930  29.574  1.000 119.180 ? 155 TYR JJJ CE1 1 
ATOM 15642 C CE2 . TYR J 3 150 ? 87.149  44.522  29.376  1.000 110.540 ? 155 TYR JJJ CE2 1 
ATOM 15643 C CZ  . TYR J 3 150 ? 88.447  44.041  29.426  1.000 115.330 ? 155 TYR JJJ CZ  1 
ATOM 15644 O OH  . TYR J 3 150 ? 88.684  42.701  29.333  1.000 108.830 ? 155 TYR JJJ OH  1 
ATOM 15645 N N   . PHE J 3 151 ? 90.307  49.325  28.382  1.000 96.440  ? 156 PHE JJJ N   1 
ATOM 15646 C CA  . PHE J 3 151 ? 91.709  49.167  27.903  1.000 106.670 ? 156 PHE JJJ CA  1 
ATOM 15647 C C   . PHE J 3 151 ? 92.658  49.557  29.026  1.000 121.150 ? 156 PHE JJJ C   1 
ATOM 15648 O O   . PHE J 3 151 ? 92.385  50.528  29.727  1.000 124.760 ? 156 PHE JJJ O   1 
ATOM 15649 C CB  . PHE J 3 151 ? 91.973  50.068  26.697  1.000 100.560 ? 156 PHE JJJ CB  1 
ATOM 15650 C CG  . PHE J 3 151 ? 93.267  49.788  25.980  1.000 107.570 ? 156 PHE JJJ CG  1 
ATOM 15651 C CD1 . PHE J 3 151 ? 93.381  48.669  25.172  1.000 111.410 ? 156 PHE JJJ CD1 1 
ATOM 15652 C CD2 . PHE J 3 151 ? 94.363  50.636  26.089  1.000 102.170 ? 156 PHE JJJ CD2 1 
ATOM 15653 C CE1 . PHE J 3 151 ? 94.536  48.430  24.440  1.000 107.020 ? 156 PHE JJJ CE1 1 
ATOM 15654 C CE2 . PHE J 3 151 ? 95.529  50.382  25.378  1.000 95.350  ? 156 PHE JJJ CE2 1 
ATOM 15655 C CZ  . PHE J 3 151 ? 95.618  49.278  24.560  1.000 95.710  ? 156 PHE JJJ CZ  1 
ATOM 15656 N N   . PRO J 3 152 ? 93.794  48.854  29.286  1.000 131.730 ? 157 PRO JJJ N   1 
ATOM 15657 C CA  . PRO J 3 152 ? 94.133  47.557  28.684  1.000 130.190 ? 157 PRO JJJ CA  1 
ATOM 15658 C C   . PRO J 3 152 ? 93.508  46.326  29.383  1.000 126.560 ? 157 PRO JJJ C   1 
ATOM 15659 O O   . PRO J 3 152 ? 92.595  46.496  30.169  1.000 126.570 ? 157 PRO JJJ O   1 
ATOM 15660 C CB  . PRO J 3 152 ? 95.667  47.477  28.814  1.000 127.100 ? 157 PRO JJJ CB  1 
ATOM 15661 C CG  . PRO J 3 152 ? 96.123  48.733  29.530  1.000 127.270 ? 157 PRO JJJ CG  1 
ATOM 15662 C CD  . PRO J 3 152 ? 94.886  49.362  30.136  1.000 122.120 ? 157 PRO JJJ CD  1 
ATOM 15663 N N   . GLU J 3 153 ? 94.078  45.134  29.152  1.000 128.760 ? 158 GLU JJJ N   1 
ATOM 15664 C CA  . GLU J 3 153 ? 93.419  43.802  29.298  1.000 128.230 ? 158 GLU JJJ CA  1 
ATOM 15665 C C   . GLU J 3 153 ? 93.020  43.468  30.741  1.000 120.200 ? 158 GLU JJJ C   1 
ATOM 15666 O O   . GLU J 3 153 ? 91.886  43.046  30.959  1.000 116.990 ? 158 GLU JJJ O   1 
ATOM 15667 C CB  . GLU J 3 153 ? 94.313  42.704  28.708  1.000 120.710 ? 158 GLU JJJ CB  1 
ATOM 15668 C CG  . GLU J 3 153 ? 93.777  41.289  28.905  1.000 120.550 ? 158 GLU JJJ CG  1 
ATOM 15669 C CD  . GLU J 3 153 ? 92.378  40.986  28.414  1.000 113.630 ? 158 GLU JJJ CD  1 
ATOM 15670 O OE1 . GLU J 3 153 ? 91.415  41.156  29.201  1.000 102.050 ? 158 GLU JJJ OE1 1 
ATOM 15671 O OE2 . GLU J 3 153 ? 92.237  40.523  27.255  1.000 109.110 ? 158 GLU JJJ OE2 1 
ATOM 15672 N N   . PRO J 3 154 ? 93.894  43.623  31.767  1.000 112.260 ? 159 PRO JJJ N   1 
ATOM 15673 C CA  . PRO J 3 154 ? 93.662  42.969  33.063  1.000 100.120 ? 159 PRO JJJ CA  1 
ATOM 15674 C C   . PRO J 3 154 ? 92.417  43.446  33.836  1.000 90.460  ? 159 PRO JJJ C   1 
ATOM 15675 O O   . PRO J 3 154 ? 92.460  44.504  34.425  1.000 87.240  ? 159 PRO JJJ O   1 
ATOM 15676 C CB  . PRO J 3 154 ? 94.964  43.267  33.842  1.000 99.370  ? 159 PRO JJJ CB  1 
ATOM 15677 C CG  . PRO J 3 154 ? 95.538  44.532  33.202  1.000 98.860  ? 159 PRO JJJ CG  1 
ATOM 15678 C CD  . PRO J 3 154 ? 95.111  44.460  31.753  1.000 102.960 ? 159 PRO JJJ CD  1 
ATOM 15679 N N   . VAL J 3 155 ? 91.335  42.652  33.827  1.000 93.110  ? 160 VAL JJJ N   1 
ATOM 15680 C CA  . VAL J 3 155 ? 90.015  42.995  34.453  1.000 103.730 ? 160 VAL JJJ CA  1 
ATOM 15681 C C   . VAL J 3 155 ? 89.511  41.828  35.319  1.000 120.320 ? 160 VAL JJJ C   1 
ATOM 15682 O O   . VAL J 3 155 ? 89.536  40.668  34.838  1.000 120.980 ? 160 VAL JJJ O   1 
ATOM 15683 C CB  . VAL J 3 155 ? 88.962  43.379  33.392  1.000 101.810 ? 160 VAL JJJ CB  1 
ATOM 15684 C CG1 . VAL J 3 155 ? 88.448  42.163  32.629  1.000 94.830  ? 160 VAL JJJ CG1 1 
ATOM 15685 C CG2 . VAL J 3 155 ? 87.822  44.180  34.011  1.000 99.190  ? 160 VAL JJJ CG2 1 
ATOM 15686 N N   . THR J 3 156 ? 89.021  42.144  36.527  1.000 130.880 ? 161 THR JJJ N   1 
ATOM 15687 C CA  . THR J 3 156 ? 88.624  41.178  37.590  1.000 127.350 ? 161 THR JJJ CA  1 
ATOM 15688 C C   . THR J 3 156 ? 87.094  41.144  37.732  1.000 124.450 ? 161 THR JJJ C   1 
ATOM 15689 O O   . THR J 3 156 ? 86.448  42.204  37.669  1.000 111.860 ? 161 THR JJJ O   1 
ATOM 15690 C CB  . THR J 3 156 ? 89.293  41.523  38.928  1.000 126.920 ? 161 THR JJJ CB  1 
ATOM 15691 O OG1 . THR J 3 156 ? 90.711  41.547  38.756  1.000 121.070 ? 161 THR JJJ OG1 1 
ATOM 15692 C CG2 . THR J 3 156 ? 88.930  40.549  40.030  1.000 120.010 ? 161 THR JJJ CG2 1 
ATOM 15693 N N   . VAL J 3 157 ? 86.549  39.941  37.889  1.000 132.310 ? 162 VAL JJJ N   1 
ATOM 15694 C CA  . VAL J 3 157 ? 85.101  39.685  38.143  1.000 144.350 ? 162 VAL JJJ CA  1 
ATOM 15695 C C   . VAL J 3 157 ? 84.991  39.065  39.539  1.000 160.910 ? 162 VAL JJJ C   1 
ATOM 15696 O O   . VAL J 3 157 ? 85.752  38.108  39.815  1.000 183.450 ? 162 VAL JJJ O   1 
ATOM 15697 C CB  . VAL J 3 157 ? 84.486  38.785  37.051  1.000 139.980 ? 162 VAL JJJ CB  1 
ATOM 15698 C CG1 . VAL J 3 157 ? 85.189  37.436  36.913  1.000 124.200 ? 162 VAL JJJ CG1 1 
ATOM 15699 C CG2 . VAL J 3 157 ? 83.000  38.585  37.277  1.000 138.850 ? 162 VAL JJJ CG2 1 
ATOM 15700 N N   . SER J 3 158 ? 84.109  39.600  40.396  1.000 158.190 ? 163 SER JJJ N   1 
ATOM 15701 C CA  . SER J 3 158 ? 83.903  39.069  41.768  1.000 142.850 ? 163 SER JJJ CA  1 
ATOM 15702 C C   . SER J 3 158 ? 82.418  39.138  42.127  1.000 136.740 ? 163 SER JJJ C   1 
ATOM 15703 O O   . SER J 3 158 ? 81.685  39.950  41.516  1.000 140.350 ? 163 SER JJJ O   1 
ATOM 15704 C CB  . SER J 3 158 ? 84.779  39.792  42.774  1.000 135.260 ? 163 SER JJJ CB  1 
ATOM 15705 O OG  . SER J 3 158 ? 86.161  39.646  42.460  1.000 117.680 ? 163 SER JJJ OG  1 
ATOM 15706 N N   . TRP J 3 159 ? 82.013  38.281  43.069  1.000 135.830 ? 164 TRP JJJ N   1 
ATOM 15707 C CA  . TRP J 3 159 ? 80.630  38.135  43.589  1.000 139.930 ? 164 TRP JJJ CA  1 
ATOM 15708 C C   . TRP J 3 159 ? 80.723  37.931  45.113  1.000 134.320 ? 164 TRP JJJ C   1 
ATOM 15709 O O   . TRP J 3 159 ? 80.235  36.894  45.633  1.000 125.580 ? 164 TRP JJJ O   1 
ATOM 15710 C CB  . TRP J 3 159 ? 79.897  37.006  42.848  1.000 139.530 ? 164 TRP JJJ CB  1 
ATOM 15711 C CG  . TRP J 3 159 ? 79.890  37.136  41.349  1.000 141.840 ? 164 TRP JJJ CG  1 
ATOM 15712 C CD1 . TRP J 3 159 ? 80.936  36.896  40.502  1.000 131.890 ? 164 TRP JJJ CD1 1 
ATOM 15713 C CD2 . TRP J 3 159 ? 78.777  37.514  40.508  1.000 138.440 ? 164 TRP JJJ CD2 1 
ATOM 15714 N NE1 . TRP J 3 159 ? 80.567  37.102  39.201  1.000 136.830 ? 164 TRP JJJ NE1 1 
ATOM 15715 C CE2 . TRP J 3 159 ? 79.246  37.472  39.170  1.000 137.860 ? 164 TRP JJJ CE2 1 
ATOM 15716 C CE3 . TRP J 3 159 ? 77.444  37.881  40.747  1.000 119.740 ? 164 TRP JJJ CE3 1 
ATOM 15717 C CZ2 . TRP J 3 159 ? 78.417  37.775  38.086  1.000 126.740 ? 164 TRP JJJ CZ2 1 
ATOM 15718 C CZ3 . TRP J 3 159 ? 76.641  38.183  39.678  1.000 111.630 ? 164 TRP JJJ CZ3 1 
ATOM 15719 C CH2 . TRP J 3 159 ? 77.116  38.127  38.365  1.000 115.520 ? 164 TRP JJJ CH2 1 
ATOM 15720 N N   . ASN J 3 160 ? 81.335  38.922  45.782  1.000 124.690 ? 165 ASN JJJ N   1 
ATOM 15721 C CA  . ASN J 3 160 ? 81.536  39.046  47.256  1.000 108.120 ? 165 ASN JJJ CA  1 
ATOM 15722 C C   . ASN J 3 160 ? 82.702  38.157  47.702  1.000 96.170  ? 165 ASN JJJ C   1 
ATOM 15723 O O   . ASN J 3 160 ? 83.838  38.458  47.280  1.000 80.640  ? 165 ASN JJJ O   1 
ATOM 15724 C CB  . ASN J 3 160 ? 80.264  38.719  48.043  1.000 103.790 ? 165 ASN JJJ CB  1 
ATOM 15725 C CG  . ASN J 3 160 ? 79.055  39.514  47.587  1.000 97.320  ? 165 ASN JJJ CG  1 
ATOM 15726 O OD1 . ASN J 3 160 ? 78.520  39.292  46.501  1.000 81.040  ? 165 ASN JJJ OD1 1 
ATOM 15727 N ND2 . ASN J 3 160 ? 78.592  40.427  48.426  1.000 92.130  ? 165 ASN JJJ ND2 1 
ATOM 15728 N N   . THR J 3 170 ? 82.816  33.279  33.866  1.000 111.910 ? 175 THR JJJ N   1 
ATOM 15729 C CA  . THR J 3 170 ? 83.552  34.432  33.275  1.000 124.000 ? 175 THR JJJ CA  1 
ATOM 15730 C C   . THR J 3 170 ? 84.184  34.004  31.943  1.000 134.100 ? 175 THR JJJ C   1 
ATOM 15731 O O   . THR J 3 170 ? 84.857  32.963  31.921  1.000 144.220 ? 175 THR JJJ O   1 
ATOM 15732 C CB  . THR J 3 170 ? 84.605  34.995  34.245  1.000 124.330 ? 175 THR JJJ CB  1 
ATOM 15733 O OG1 . THR J 3 170 ? 85.222  36.161  33.696  1.000 115.970 ? 175 THR JJJ OG1 1 
ATOM 15734 C CG2 . THR J 3 170 ? 85.704  34.015  34.600  1.000 121.740 ? 175 THR JJJ CG2 1 
ATOM 15735 N N   . PHE J 3 171 ? 83.974  34.780  30.873  1.000 130.910 ? 176 PHE JJJ N   1 
ATOM 15736 C CA  . PHE J 3 171 ? 84.531  34.523  29.512  1.000 122.910 ? 176 PHE JJJ CA  1 
ATOM 15737 C C   . PHE J 3 171 ? 85.797  35.359  29.337  1.000 118.390 ? 176 PHE JJJ C   1 
ATOM 15738 O O   . PHE J 3 171 ? 85.923  36.431  29.933  1.000 106.760 ? 176 PHE JJJ O   1 
ATOM 15739 C CB  . PHE J 3 171 ? 83.488  34.792  28.430  1.000 109.440 ? 176 PHE JJJ CB  1 
ATOM 15740 C CG  . PHE J 3 171 ? 82.448  33.713  28.318  1.000 102.060 ? 176 PHE JJJ CG  1 
ATOM 15741 C CD1 . PHE J 3 171 ? 81.610  33.416  29.394  1.000 105.860 ? 176 PHE JJJ CD1 1 
ATOM 15742 C CD2 . PHE J 3 171 ? 82.309  32.976  27.150  1.000 93.640  ? 176 PHE JJJ CD2 1 
ATOM 15743 C CE1 . PHE J 3 171 ? 80.661  32.405  29.301  1.000 108.210 ? 176 PHE JJJ CE1 1 
ATOM 15744 C CE2 . PHE J 3 171 ? 81.356  31.969  27.056  1.000 94.370  ? 176 PHE JJJ CE2 1 
ATOM 15745 C CZ  . PHE J 3 171 ? 80.540  31.686  28.130  1.000 101.800 ? 176 PHE JJJ CZ  1 
ATOM 15746 N N   . PRO J 3 172 ? 86.775  34.935  28.483  1.000 107.450 ? 177 PRO JJJ N   1 
ATOM 15747 C CA  . PRO J 3 172 ? 87.871  35.812  28.074  1.000 104.010 ? 177 PRO JJJ CA  1 
ATOM 15748 C C   . PRO J 3 172 ? 87.337  36.924  27.158  1.000 104.660 ? 177 PRO JJJ C   1 
ATOM 15749 O O   . PRO J 3 172 ? 86.350  36.712  26.453  1.000 103.790 ? 177 PRO JJJ O   1 
ATOM 15750 C CB  . PRO J 3 172 ? 88.826  34.877  27.320  1.000 104.950 ? 177 PRO JJJ CB  1 
ATOM 15751 C CG  . PRO J 3 172 ? 87.920  33.792  26.770  1.000 103.440 ? 177 PRO JJJ CG  1 
ATOM 15752 C CD  . PRO J 3 172 ? 86.840  33.622  27.822  1.000 100.510 ? 177 PRO JJJ CD  1 
ATOM 15753 N N   . ALA J 3 173 ? 88.005  38.078  27.179  1.000 94.460  ? 178 ALA JJJ N   1 
ATOM 15754 C CA  . ALA J 3 173 ? 87.588  39.313  26.476  1.000 91.480  ? 178 ALA JJJ CA  1 
ATOM 15755 C C   . ALA J 3 173 ? 87.669  39.131  24.954  1.000 91.730  ? 178 ALA JJJ C   1 
ATOM 15756 O O   . ALA J 3 173 ? 88.261  38.135  24.501  1.000 93.480  ? 178 ALA JJJ O   1 
ATOM 15757 C CB  . ALA J 3 173 ? 88.449  40.458  26.937  1.000 88.490  ? 178 ALA JJJ CB  1 
ATOM 15758 N N   . VAL J 3 174 ? 87.086  40.069  24.197  1.000 89.960  ? 179 VAL JJJ N   1 
ATOM 15759 C CA  . VAL J 3 174 ? 87.291  40.217  22.726  1.000 84.360  ? 179 VAL JJJ CA  1 
ATOM 15760 C C   . VAL J 3 174 ? 87.912  41.590  22.498  1.000 83.970  ? 179 VAL JJJ C   1 
ATOM 15761 O O   . VAL J 3 174 ? 87.456  42.539  23.156  1.000 75.270  ? 179 VAL JJJ O   1 
ATOM 15762 C CB  . VAL J 3 174 ? 85.984  40.030  21.928  1.000 84.010  ? 179 VAL JJJ CB  1 
ATOM 15763 C CG1 . VAL J 3 174 ? 86.032  40.652  20.537  1.000 78.820  ? 179 VAL JJJ CG1 1 
ATOM 15764 C CG2 . VAL J 3 174 ? 85.637  38.554  21.795  1.000 85.900  ? 179 VAL JJJ CG2 1 
ATOM 15765 N N   . LEU J 3 175 ? 88.917  41.674  21.614  1.000 91.280  ? 180 LEU JJJ N   1 
ATOM 15766 C CA  . LEU J 3 175 ? 89.524  42.940  21.121  1.000 99.910  ? 180 LEU JJJ CA  1 
ATOM 15767 C C   . LEU J 3 175 ? 88.685  43.428  19.928  1.000 107.110 ? 180 LEU JJJ C   1 
ATOM 15768 O O   . LEU J 3 175 ? 88.892  42.913  18.815  1.000 118.550 ? 180 LEU JJJ O   1 
ATOM 15769 C CB  . LEU J 3 175 ? 90.990  42.674  20.743  1.000 100.120 ? 180 LEU JJJ CB  1 
ATOM 15770 C CG  . LEU J 3 175 ? 91.882  43.894  20.459  1.000 107.220 ? 180 LEU JJJ CG  1 
ATOM 15771 C CD1 . LEU J 3 175 ? 93.336  43.635  20.840  1.000 102.390 ? 180 LEU JJJ CD1 1 
ATOM 15772 C CD2 . LEU J 3 175 ? 91.806  44.328  18.991  1.000 101.230 ? 180 LEU JJJ CD2 1 
ATOM 15773 N N   . GLN J 3 176 ? 87.757  44.363  20.166  1.000 105.810 ? 181 GLN JJJ N   1 
ATOM 15774 C CA  . GLN J 3 176 ? 86.957  45.045  19.110  1.000 99.450  ? 181 GLN JJJ CA  1 
ATOM 15775 C C   . GLN J 3 176 ? 87.933  45.843  18.226  1.000 99.540  ? 181 GLN JJJ C   1 
ATOM 15776 O O   . GLN J 3 176 ? 89.042  46.190  18.719  1.000 94.290  ? 181 GLN JJJ O   1 
ATOM 15777 C CB  . GLN J 3 176 ? 85.849  45.899  19.745  1.000 83.940  ? 181 GLN JJJ CB  1 
ATOM 15778 N N   . SER J 3 177 ? 87.586  46.096  16.959  1.000 95.810  ? 182 SER JJJ N   1 
ATOM 15779 C CA  . SER J 3 177 ? 88.403  46.888  15.993  1.000 89.680  ? 182 SER JJJ CA  1 
ATOM 15780 C C   . SER J 3 177 ? 88.619  48.319  16.515  1.000 94.450  ? 182 SER JJJ C   1 
ATOM 15781 O O   . SER J 3 177 ? 89.575  48.960  16.064  1.000 91.510  ? 182 SER JJJ O   1 
ATOM 15782 C CB  . SER J 3 177 ? 87.783  46.896  14.627  1.000 79.390  ? 182 SER JJJ CB  1 
ATOM 15783 O OG  . SER J 3 177 ? 86.463  47.406  14.687  1.000 80.940  ? 182 SER JJJ OG  1 
ATOM 15784 N N   . SER J 3 178 ? 87.750  48.795  17.428  1.000 100.500 ? 183 SER JJJ N   1 
ATOM 15785 C CA  . SER J 3 178 ? 87.861  50.104  18.130  1.000 99.690  ? 183 SER JJJ CA  1 
ATOM 15786 C C   . SER J 3 178 ? 89.161  50.180  18.950  1.000 104.300 ? 183 SER JJJ C   1 
ATOM 15787 O O   . SER J 3 178 ? 89.579  51.308  19.303  1.000 114.670 ? 183 SER JJJ O   1 
ATOM 15788 C CB  . SER J 3 178 ? 86.642  50.355  18.990  1.000 97.560  ? 183 SER JJJ CB  1 
ATOM 15789 O OG  . SER J 3 178 ? 86.295  49.196  19.735  1.000 100.180 ? 183 SER JJJ OG  1 
ATOM 15790 N N   . GLY J 3 179 ? 89.779  49.033  19.243  1.000 102.880 ? 184 GLY JJJ N   1 
ATOM 15791 C CA  . GLY J 3 179 ? 90.980  48.934  20.093  1.000 105.030 ? 184 GLY JJJ CA  1 
ATOM 15792 C C   . GLY J 3 179 ? 90.600  48.783  21.557  1.000 110.170 ? 184 GLY JJJ C   1 
ATOM 15793 O O   . GLY J 3 179 ? 91.527  48.769  22.402  1.000 98.370  ? 184 GLY JJJ O   1 
ATOM 15794 N N   . LEU J 3 180 ? 89.289  48.693  21.848  1.000 112.700 ? 185 LEU JJJ N   1 
ATOM 15795 C CA  . LEU J 3 180 ? 88.718  48.527  23.215  1.000 107.020 ? 185 LEU JJJ CA  1 
ATOM 15796 C C   . LEU J 3 180 ? 88.266  47.069  23.385  1.000 106.900 ? 185 LEU JJJ C   1 
ATOM 15797 O O   . LEU J 3 180 ? 87.656  46.532  22.441  1.000 99.870  ? 185 LEU JJJ O   1 
ATOM 15798 C CB  . LEU J 3 180 ? 87.540  49.493  23.429  1.000 105.820 ? 185 LEU JJJ CB  1 
ATOM 15799 C CG  . LEU J 3 180 ? 87.871  50.980  23.618  1.000 99.110  ? 185 LEU JJJ CG  1 
ATOM 15800 C CD1 . LEU J 3 180 ? 88.862  51.203  24.759  1.000 100.280 ? 185 LEU JJJ CD1 1 
ATOM 15801 C CD2 . LEU J 3 180 ? 88.383  51.609  22.332  1.000 96.660  ? 185 LEU JJJ CD2 1 
ATOM 15802 N N   . TYR J 3 181 ? 88.517  46.479  24.560  1.000 108.790 ? 186 TYR JJJ N   1 
ATOM 15803 C CA  . TYR J 3 181 ? 88.134  45.089  24.941  1.000 113.670 ? 186 TYR JJJ CA  1 
ATOM 15804 C C   . TYR J 3 181 ? 86.700  45.085  25.492  1.000 108.710 ? 186 TYR JJJ C   1 
ATOM 15805 O O   . TYR J 3 181 ? 86.229  46.150  25.953  1.000 103.100 ? 186 TYR JJJ O   1 
ATOM 15806 C CB  . TYR J 3 181 ? 89.103  44.488  25.974  1.000 117.870 ? 186 TYR JJJ CB  1 
ATOM 15807 C CG  . TYR J 3 181 ? 90.544  44.363  25.531  1.000 118.610 ? 186 TYR JJJ CG  1 
ATOM 15808 C CD1 . TYR J 3 181 ? 90.939  43.400  24.615  1.000 111.790 ? 186 TYR JJJ CD1 1 
ATOM 15809 C CD2 . TYR J 3 181 ? 91.522  45.204  26.045  1.000 118.990 ? 186 TYR JJJ CD2 1 
ATOM 15810 C CE1 . TYR J 3 181 ? 92.256  43.294  24.198  1.000 111.350 ? 186 TYR JJJ CE1 1 
ATOM 15811 C CE2 . TYR J 3 181 ? 92.845  45.110  25.645  1.000 114.100 ? 186 TYR JJJ CE2 1 
ATOM 15812 C CZ  . TYR J 3 181 ? 93.212  44.149  24.721  1.000 116.370 ? 186 TYR JJJ CZ  1 
ATOM 15813 O OH  . TYR J 3 181 ? 94.512  44.065  24.323  1.000 121.060 ? 186 TYR JJJ OH  1 
ATOM 15814 N N   . SER J 3 182 ? 86.029  43.929  25.426  1.000 108.970 ? 187 SER JJJ N   1 
ATOM 15815 C CA  . SER J 3 182 ? 84.703  43.675  26.046  1.000 108.950 ? 187 SER JJJ CA  1 
ATOM 15816 C C   . SER J 3 182 ? 84.657  42.218  26.508  1.000 119.500 ? 187 SER JJJ C   1 
ATOM 15817 O O   . SER J 3 182 ? 85.098  41.352  25.697  1.000 119.420 ? 187 SER JJJ O   1 
ATOM 15818 C CB  . SER J 3 182 ? 83.572  43.971  25.093  1.000 95.540  ? 187 SER JJJ CB  1 
ATOM 15819 O OG  . SER J 3 182 ? 83.559  45.335  24.729  1.000 91.340  ? 187 SER JJJ OG  1 
ATOM 15820 N N   . LEU J 3 183 ? 84.159  41.974  27.732  1.000 128.730 ? 188 LEU JJJ N   1 
ATOM 15821 C CA  . LEU J 3 183 ? 84.030  40.612  28.322  1.000 121.960 ? 188 LEU JJJ CA  1 
ATOM 15822 C C   . LEU J 3 183 ? 82.697  40.496  29.093  1.000 114.920 ? 188 LEU JJJ C   1 
ATOM 15823 O O   . LEU J 3 183 ? 82.241  41.526  29.639  1.000 108.280 ? 188 LEU JJJ O   1 
ATOM 15824 C CB  . LEU J 3 183 ? 85.247  40.301  29.195  1.000 123.860 ? 188 LEU JJJ CB  1 
ATOM 15825 C CG  . LEU J 3 183 ? 85.195  40.597  30.696  1.000 115.090 ? 188 LEU JJJ CG  1 
ATOM 15826 C CD1 . LEU J 3 183 ? 86.175  39.707  31.447  1.000 113.500 ? 188 LEU JJJ CD1 1 
ATOM 15827 C CD2 . LEU J 3 183 ? 85.513  42.047  30.967  1.000 105.020 ? 188 LEU JJJ CD2 1 
ATOM 15828 N N   . SER J 3 184 ? 82.141  39.278  29.141  1.000 106.900 ? 189 SER JJJ N   1 
ATOM 15829 C CA  . SER J 3 184 ? 80.851  38.931  29.796  1.000 109.580 ? 189 SER JJJ CA  1 
ATOM 15830 C C   . SER J 3 184 ? 81.064  37.816  30.834  1.000 117.420 ? 189 SER JJJ C   1 
ATOM 15831 O O   . SER J 3 184 ? 82.056  37.089  30.695  1.000 119.250 ? 189 SER JJJ O   1 
ATOM 15832 C CB  . SER J 3 184 ? 79.848  38.542  28.763  1.000 104.940 ? 189 SER JJJ CB  1 
ATOM 15833 O OG  . SER J 3 184 ? 79.831  39.496  27.712  1.000 115.860 ? 189 SER JJJ OG  1 
ATOM 15834 N N   . SER J 3 185 ? 80.182  37.709  31.838  1.000 126.610 ? 190 SER JJJ N   1 
ATOM 15835 C CA  . SER J 3 185 ? 80.421  36.971  33.115  1.000 125.160 ? 190 SER JJJ CA  1 
ATOM 15836 C C   . SER J 3 185 ? 79.117  36.337  33.629  1.000 131.780 ? 190 SER JJJ C   1 
ATOM 15837 O O   . SER J 3 185 ? 78.095  37.039  33.613  1.000 146.270 ? 190 SER JJJ O   1 
ATOM 15838 C CB  . SER J 3 185 ? 81.030  37.908  34.135  1.000 108.840 ? 190 SER JJJ CB  1 
ATOM 15839 O OG  . SER J 3 185 ? 81.243  37.266  35.382  1.000 102.790 ? 190 SER JJJ OG  1 
ATOM 15840 N N   . VAL J 3 186 ? 79.153  35.069  34.067  1.000 126.540 ? 191 VAL JJJ N   1 
ATOM 15841 C CA  . VAL J 3 186 ? 77.951  34.303  34.538  1.000 119.260 ? 191 VAL JJJ CA  1 
ATOM 15842 C C   . VAL J 3 186 ? 78.290  33.542  35.829  1.000 114.630 ? 191 VAL JJJ C   1 
ATOM 15843 O O   . VAL J 3 186 ? 77.951  34.070  36.925  1.000 99.090  ? 191 VAL JJJ O   1 
ATOM 15844 C CB  . VAL J 3 186 ? 77.402  33.358  33.446  1.000 106.090 ? 191 VAL JJJ CB  1 
ATOM 15845 C CG1 . VAL J 3 186 ? 76.617  34.109  32.383  1.000 91.760  ? 191 VAL JJJ CG1 1 
ATOM 15846 C CG2 . VAL J 3 186 ? 78.498  32.524  32.805  1.000 103.520 ? 191 VAL JJJ CG2 1 
ATOM 15847 N N   . CYS J 3 201 ? 77.400  42.081  41.484  1.000 145.470 ? 206 CYS JJJ N   1 
ATOM 15848 C CA  . CYS J 3 201 ? 78.772  41.707  41.031  1.000 143.710 ? 206 CYS JJJ CA  1 
ATOM 15849 C C   . CYS J 3 201 ? 79.760  42.839  41.347  1.000 137.280 ? 206 CYS JJJ C   1 
ATOM 15850 O O   . CYS J 3 201 ? 79.332  44.016  41.377  1.000 136.030 ? 206 CYS JJJ O   1 
ATOM 15851 C CB  . CYS J 3 201 ? 78.831  41.338  39.547  1.000 147.720 ? 206 CYS JJJ CB  1 
ATOM 15852 S SG  . CYS J 3 201 ? 78.033  42.504  38.397  1.000 155.240 ? 206 CYS JJJ SG  1 
ATOM 15853 N N   . ASN J 3 202 ? 81.029  42.477  41.579  1.000 136.600 ? 207 ASN JJJ N   1 
ATOM 15854 C CA  . ASN J 3 202 ? 82.161  43.396  41.868  1.000 127.000 ? 207 ASN JJJ CA  1 
ATOM 15855 C C   . ASN J 3 202 ? 83.181  43.335  40.716  1.000 122.990 ? 207 ASN JJJ C   1 
ATOM 15856 O O   . ASN J 3 202 ? 83.960  42.356  40.633  1.000 134.990 ? 207 ASN JJJ O   1 
ATOM 15857 C CB  . ASN J 3 202 ? 82.812  43.064  43.214  1.000 125.230 ? 207 ASN JJJ CB  1 
ATOM 15858 C CG  . ASN J 3 202 ? 81.844  43.088  44.381  1.000 112.620 ? 207 ASN JJJ CG  1 
ATOM 15859 O OD1 . ASN J 3 202 ? 81.204  44.098  44.656  1.000 96.520  ? 207 ASN JJJ OD1 1 
ATOM 15860 N ND2 . ASN J 3 202 ? 81.751  41.984  45.103  1.000 95.700  ? 207 ASN JJJ ND2 1 
ATOM 15861 N N   . VAL J 3 203 ? 83.185  44.345  39.844  1.000 109.710 ? 208 VAL JJJ N   1 
ATOM 15862 C CA  . VAL J 3 203 ? 84.116  44.447  38.680  1.000 105.760 ? 208 VAL JJJ CA  1 
ATOM 15863 C C   . VAL J 3 203 ? 85.250  45.417  39.040  1.000 101.780 ? 208 VAL JJJ C   1 
ATOM 15864 O O   . VAL J 3 203 ? 84.977  46.449  39.681  1.000 85.440  ? 208 VAL JJJ O   1 
ATOM 15865 C CB  . VAL J 3 203 ? 83.379  44.840  37.385  1.000 109.370 ? 208 VAL JJJ CB  1 
ATOM 15866 C CG1 . VAL J 3 203 ? 82.776  46.234  37.447  1.000 120.920 ? 208 VAL JJJ CG1 1 
ATOM 15867 C CG2 . VAL J 3 203 ? 84.278  44.696  36.167  1.000 108.260 ? 208 VAL JJJ CG2 1 
ATOM 15868 N N   . ASN J 3 204 ? 86.485  45.067  38.672  1.000 109.610 ? 209 ASN JJJ N   1 
ATOM 15869 C CA  . ASN J 3 204 ? 87.718  45.834  39.010  1.000 118.280 ? 209 ASN JJJ CA  1 
ATOM 15870 C C   . ASN J 3 204 ? 88.609  45.905  37.760  1.000 117.890 ? 209 ASN JJJ C   1 
ATOM 15871 O O   . ASN J 3 204 ? 88.742  44.879  37.064  1.000 119.000 ? 209 ASN JJJ O   1 
ATOM 15872 C CB  . ASN J 3 204 ? 88.423  45.216  40.223  1.000 115.940 ? 209 ASN JJJ CB  1 
ATOM 15873 C CG  . ASN J 3 204 ? 89.303  46.188  40.988  1.000 112.930 ? 209 ASN JJJ CG  1 
ATOM 15874 O OD1 . ASN J 3 204 ? 90.040  46.973  40.394  1.000 107.860 ? 209 ASN JJJ OD1 1 
ATOM 15875 N ND2 . ASN J 3 204 ? 89.225  46.162  42.311  1.000 102.560 ? 209 ASN JJJ ND2 1 
ATOM 15876 N N   . HIS J 3 205 ? 89.186  47.079  37.482  1.000 110.000 ? 210 HIS JJJ N   1 
ATOM 15877 C CA  . HIS J 3 205 ? 90.110  47.333  36.343  1.000 110.660 ? 210 HIS JJJ CA  1 
ATOM 15878 C C   . HIS J 3 205 ? 91.231  48.265  36.824  1.000 111.790 ? 210 HIS JJJ C   1 
ATOM 15879 O O   . HIS J 3 205 ? 91.110  49.486  36.619  1.000 108.080 ? 210 HIS JJJ O   1 
ATOM 15880 C CB  . HIS J 3 205 ? 89.291  47.863  35.158  1.000 113.200 ? 210 HIS JJJ CB  1 
ATOM 15881 C CG  . HIS J 3 205 ? 90.065  48.134  33.912  1.000 120.390 ? 210 HIS JJJ CG  1 
ATOM 15882 N ND1 . HIS J 3 205 ? 90.471  49.408  33.549  1.000 136.640 ? 210 HIS JJJ ND1 1 
ATOM 15883 C CD2 . HIS J 3 205 ? 90.465  47.317  32.913  1.000 113.710 ? 210 HIS JJJ CD2 1 
ATOM 15884 C CE1 . HIS J 3 205 ? 91.100  49.361  32.396  1.000 130.320 ? 210 HIS JJJ CE1 1 
ATOM 15885 N NE2 . HIS J 3 205 ? 91.113  48.088  31.981  1.000 117.900 ? 210 HIS JJJ NE2 1 
ATOM 15886 N N   . LYS J 3 206 ? 92.273  47.697  37.449  1.000 116.800 ? 211 LYS JJJ N   1 
ATOM 15887 C CA  . LYS J 3 206 ? 93.336  48.426  38.204  1.000 123.310 ? 211 LYS JJJ CA  1 
ATOM 15888 C C   . LYS J 3 206 ? 93.919  49.550  37.349  1.000 135.350 ? 211 LYS JJJ C   1 
ATOM 15889 O O   . LYS J 3 206 ? 94.092  50.657  37.851  1.000 134.750 ? 211 LYS JJJ O   1 
ATOM 15890 C CB  . LYS J 3 206 ? 94.448  47.481  38.675  1.000 116.140 ? 211 LYS JJJ CB  1 
ATOM 15891 N N   . PRO J 3 207 ? 94.232  49.333  36.046  1.000 143.990 ? 212 PRO JJJ N   1 
ATOM 15892 C CA  . PRO J 3 207 ? 94.831  50.382  35.211  1.000 140.950 ? 212 PRO JJJ CA  1 
ATOM 15893 C C   . PRO J 3 207 ? 94.048  51.706  35.103  1.000 136.450 ? 212 PRO JJJ C   1 
ATOM 15894 O O   . PRO J 3 207 ? 94.647  52.688  34.681  1.000 113.730 ? 212 PRO JJJ O   1 
ATOM 15895 C CB  . PRO J 3 207 ? 94.895  49.730  33.815  1.000 147.510 ? 212 PRO JJJ CB  1 
ATOM 15896 C CG  . PRO J 3 207 ? 94.963  48.248  34.106  1.000 150.320 ? 212 PRO JJJ CG  1 
ATOM 15897 C CD  . PRO J 3 207 ? 94.060  48.071  35.306  1.000 140.850 ? 212 PRO JJJ CD  1 
ATOM 15898 N N   . SER J 3 208 ? 92.753  51.704  35.458  1.000 144.110 ? 213 SER JJJ N   1 
ATOM 15899 C CA  . SER J 3 208 ? 91.837  52.877  35.378  1.000 133.350 ? 213 SER JJJ CA  1 
ATOM 15900 C C   . SER J 3 208 ? 91.183  53.187  36.738  1.000 123.610 ? 213 SER JJJ C   1 
ATOM 15901 O O   . SER J 3 208 ? 90.247  54.011  36.753  1.000 107.360 ? 213 SER JJJ O   1 
ATOM 15902 C CB  . SER J 3 208 ? 90.793  52.666  34.298  1.000 132.870 ? 213 SER JJJ CB  1 
ATOM 15903 O OG  . SER J 3 208 ? 89.630  52.032  34.810  1.000 131.690 ? 213 SER JJJ OG  1 
ATOM 15904 N N   . ASN J 3 209 ? 91.636  52.558  37.831  1.000 117.710 ? 214 ASN JJJ N   1 
ATOM 15905 C CA  . ASN J 3 209 ? 91.188  52.851  39.222  1.000 108.450 ? 214 ASN JJJ CA  1 
ATOM 15906 C C   . ASN J 3 209 ? 89.677  52.610  39.356  1.000 108.320 ? 214 ASN JJJ C   1 
ATOM 15907 O O   . ASN J 3 209 ? 89.049  53.223  40.255  1.000 114.690 ? 214 ASN JJJ O   1 
ATOM 15908 C CB  . ASN J 3 209 ? 91.570  54.278  39.631  1.000 100.510 ? 214 ASN JJJ CB  1 
ATOM 15909 C CG  . ASN J 3 209 ? 93.069  54.495  39.631  1.000 93.660  ? 214 ASN JJJ CG  1 
ATOM 15910 O OD1 . ASN J 3 209 ? 93.743  54.049  40.545  1.000 92.520  ? 214 ASN JJJ OD1 1 
ATOM 15911 N ND2 . ASN J 3 209 ? 93.593  55.177  38.626  1.000 78.600  ? 214 ASN JJJ ND2 1 
ATOM 15912 N N   . THR J 3 210 ? 89.105  51.753  38.506  1.000 108.000 ? 215 THR JJJ N   1 
ATOM 15913 C CA  . THR J 3 210 ? 87.643  51.479  38.434  1.000 121.750 ? 215 THR JJJ CA  1 
ATOM 15914 C C   . THR J 3 210 ? 87.317  50.291  39.351  1.000 133.970 ? 215 THR JJJ C   1 
ATOM 15915 O O   . THR J 3 210 ? 87.915  49.211  39.133  1.000 151.840 ? 215 THR JJJ O   1 
ATOM 15916 C CB  . THR J 3 210 ? 87.193  51.214  36.988  1.000 117.090 ? 215 THR JJJ CB  1 
ATOM 15917 O OG1 . THR J 3 210 ? 87.536  52.319  36.150  1.000 93.800  ? 215 THR JJJ OG1 1 
ATOM 15918 C CG2 . THR J 3 210 ? 85.705  50.956  36.875  1.000 115.030 ? 215 THR JJJ CG2 1 
ATOM 15919 N N   . LYS J 3 211 ? 86.401  50.479  40.324  1.000 127.750 ? 216 LYS JJJ N   1 
ATOM 15920 C CA  . LYS J 3 211 ? 85.983  49.418  41.285  1.000 128.550 ? 216 LYS JJJ CA  1 
ATOM 15921 C C   . LYS J 3 211 ? 84.464  49.472  41.523  1.000 137.080 ? 216 LYS JJJ C   1 
ATOM 15922 O O   . LYS J 3 211 ? 84.054  49.433  42.703  1.000 143.910 ? 216 LYS JJJ O   1 
ATOM 15923 C CB  . LYS J 3 211 ? 86.767  49.575  42.594  1.000 117.510 ? 216 LYS JJJ CB  1 
ATOM 15924 N N   . VAL J 3 212 ? 83.661  49.505  40.452  1.000 144.990 ? 217 VAL JJJ N   1 
ATOM 15925 C CA  . VAL J 3 212 ? 82.177  49.730  40.510  1.000 141.120 ? 217 VAL JJJ CA  1 
ATOM 15926 C C   . VAL J 3 212 ? 81.426  48.404  40.761  1.000 132.560 ? 217 VAL JJJ C   1 
ATOM 15927 O O   . VAL J 3 212 ? 81.731  47.414  40.067  1.000 125.080 ? 217 VAL JJJ O   1 
ATOM 15928 C CB  . VAL J 3 212 ? 81.678  50.460  39.248  1.000 132.100 ? 217 VAL JJJ CB  1 
ATOM 15929 C CG1 . VAL J 3 212 ? 82.290  51.851  39.125  1.000 124.340 ? 217 VAL JJJ CG1 1 
ATOM 15930 C CG2 . VAL J 3 212 ? 81.891  49.661  37.967  1.000 122.010 ? 217 VAL JJJ CG2 1 
ATOM 15931 N N   . ASP J 3 213 ? 80.512  48.389  41.745  1.000 123.000 ? 218 ASP JJJ N   1 
ATOM 15932 C CA  . ASP J 3 213 ? 79.752  47.197  42.226  1.000 120.780 ? 218 ASP JJJ CA  1 
ATOM 15933 C C   . ASP J 3 213 ? 78.278  47.328  41.802  1.000 111.960 ? 218 ASP JJJ C   1 
ATOM 15934 O O   . ASP J 3 213 ? 77.639  48.294  42.251  1.000 118.220 ? 218 ASP JJJ O   1 
ATOM 15935 C CB  . ASP J 3 213 ? 79.878  47.041  43.754  1.000 119.330 ? 218 ASP JJJ CB  1 
ATOM 15936 C CG  . ASP J 3 213 ? 81.292  47.111  44.337  1.000 113.490 ? 218 ASP JJJ CG  1 
ATOM 15937 O OD1 . ASP J 3 213 ? 82.228  46.623  43.681  1.000 122.420 ? 218 ASP JJJ OD1 1 
ATOM 15938 O OD2 . ASP J 3 213 ? 81.452  47.644  45.454  1.000 91.400  ? 218 ASP JJJ OD2 1 
ATOM 15939 N N   . LYS J 3 214 ? 77.759  46.398  40.982  1.000 105.140 ? 219 LYS JJJ N   1 
ATOM 15940 C CA  . LYS J 3 214 ? 76.349  46.383  40.466  1.000 99.220  ? 219 LYS JJJ CA  1 
ATOM 15941 C C   . LYS J 3 214 ? 75.544  45.250  41.136  1.000 94.330  ? 219 LYS JJJ C   1 
ATOM 15942 O O   . LYS J 3 214 ? 74.321  44.999  40.991  1.000 77.460  ? 219 LYS JJJ O   1 
ATOM 15943 C CB  . LYS J 3 214 ? 76.356  46.235  38.938  1.000 92.450  ? 219 LYS JJJ CB  1 
ATOM 15944 N N   . SER K 2 2   ? 127.262 -12.103 -0.060  1.000 66.470  ? 2   SER KKK N   1 
ATOM 15945 C CA  . SER K 2 2   ? 127.320 -10.978 -1.074  1.000 70.790  ? 2   SER KKK CA  1 
ATOM 15946 C C   . SER K 2 2   ? 125.960 -10.277 -1.270  1.000 74.070  ? 2   SER KKK C   1 
ATOM 15947 O O   . SER K 2 2   ? 125.952 -9.197  -1.921  1.000 67.140  ? 2   SER KKK O   1 
ATOM 15948 C CB  . SER K 2 2   ? 127.867 -11.455 -2.402  1.000 63.540  ? 2   SER KKK CB  1 
ATOM 15949 O OG  . SER K 2 2   ? 129.266 -11.297 -2.423  1.000 58.330  ? 2   SER KKK OG  1 
ATOM 15950 N N   . VAL K 2 3   ? 124.849 -10.891 -0.846  1.000 68.140  ? 3   VAL KKK N   1 
ATOM 15951 C CA  . VAL K 2 3   ? 123.471 -10.329 -0.983  1.000 58.460  ? 3   VAL KKK CA  1 
ATOM 15952 C C   . VAL K 2 3   ? 122.878 -10.240 0.413   1.000 49.640  ? 3   VAL KKK C   1 
ATOM 15953 O O   . VAL K 2 3   ? 123.031 -11.210 1.167   1.000 45.020  ? 3   VAL KKK O   1 
ATOM 15954 C CB  . VAL K 2 3   ? 122.537 -11.186 -1.857  1.000 61.890  ? 3   VAL KKK CB  1 
ATOM 15955 C CG1 . VAL K 2 3   ? 121.317 -10.366 -2.290  1.000 67.680  ? 3   VAL KKK CG1 1 
ATOM 15956 C CG2 . VAL K 2 3   ? 123.249 -11.847 -3.042  1.000 59.230  ? 3   VAL KKK CG2 1 
ATOM 15957 N N   . LEU K 2 4   ? 122.179 -9.151  0.720   1.000 43.970  ? 4   LEU KKK N   1 
ATOM 15958 C CA  . LEU K 2 4   ? 121.362 -9.120  1.955   1.000 43.720  ? 4   LEU KKK CA  1 
ATOM 15959 C C   . LEU K 2 4   ? 119.969 -9.629  1.596   1.000 44.910  ? 4   LEU KKK C   1 
ATOM 15960 O O   . LEU K 2 4   ? 119.376 -9.132  0.618   1.000 51.320  ? 4   LEU KKK O   1 
ATOM 15961 C CB  . LEU K 2 4   ? 121.347 -7.713  2.550   1.000 39.310  ? 4   LEU KKK CB  1 
ATOM 15962 C CG  . LEU K 2 4   ? 122.715 -7.152  2.930   1.000 38.330  ? 4   LEU KKK CG  1 
ATOM 15963 C CD1 . LEU K 2 4   ? 122.578 -5.840  3.702   1.000 38.760  ? 4   LEU KKK CD1 1 
ATOM 15964 C CD2 . LEU K 2 4   ? 123.533 -8.136  3.744   1.000 38.310  ? 4   LEU KKK CD2 1 
ATOM 15965 N N   . THR K 2 5   ? 119.488 -10.603 2.361   1.000 47.470  ? 5   THR KKK N   1 
ATOM 15966 C CA  . THR K 2 5   ? 118.174 -11.263 2.178   1.000 48.580  ? 5   THR KKK CA  1 
ATOM 15967 C C   . THR K 2 5   ? 117.237 -10.736 3.269   1.000 43.110  ? 5   THR KKK C   1 
ATOM 15968 O O   . THR K 2 5   ? 117.512 -10.999 4.466   1.000 39.140  ? 5   THR KKK O   1 
ATOM 15969 C CB  . THR K 2 5   ? 118.364 -12.788 2.186   1.000 47.730  ? 5   THR KKK CB  1 
ATOM 15970 O OG1 . THR K 2 5   ? 119.558 -13.062 1.446   1.000 53.740  ? 5   THR KKK OG1 1 
ATOM 15971 C CG2 . THR K 2 5   ? 117.186 -13.539 1.609   1.000 44.860  ? 5   THR KKK CG2 1 
ATOM 15972 N N   . GLN K 2 6   ? 116.191 -9.997  2.879   1.000 39.800  ? 6   GLN KKK N   1 
ATOM 15973 C CA  . GLN K 2 6   ? 115.084 -9.624  3.801   1.000 44.370  ? 6   GLN KKK CA  1 
ATOM 15974 C C   . GLN K 2 6   ? 113.735 -10.017 3.190   1.000 46.720  ? 6   GLN KKK C   1 
ATOM 15975 O O   . GLN K 2 6   ? 113.590 -10.090 1.974   1.000 45.210  ? 6   GLN KKK O   1 
ATOM 15976 C CB  . GLN K 2 6   ? 115.190 -8.148  4.180   1.000 45.580  ? 6   GLN KKK CB  1 
ATOM 15977 C CG  . GLN K 2 6   ? 114.796 -7.178  3.084   1.000 45.960  ? 6   GLN KKK CG  1 
ATOM 15978 C CD  . GLN K 2 6   ? 115.238 -5.769  3.398   1.000 44.150  ? 6   GLN KKK CD  1 
ATOM 15979 O OE1 . GLN K 2 6   ? 116.443 -5.477  3.427   1.000 39.560  ? 6   GLN KKK OE1 1 
ATOM 15980 N NE2 . GLN K 2 6   ? 114.261 -4.903  3.646   1.000 43.150  ? 6   GLN KKK NE2 1 
ATOM 15981 N N   . PRO K 2 7   ? 112.717 -10.349 4.022   1.000 48.040  ? 7   PRO KKK N   1 
ATOM 15982 C CA  . PRO K 2 7   ? 111.402 -10.723 3.511   1.000 50.220  ? 7   PRO KKK CA  1 
ATOM 15983 C C   . PRO K 2 7   ? 110.852 -9.667  2.562   1.000 49.400  ? 7   PRO KKK C   1 
ATOM 15984 O O   . PRO K 2 7   ? 110.891 -8.490  2.898   1.000 49.100  ? 7   PRO KKK O   1 
ATOM 15985 C CB  . PRO K 2 7   ? 110.552 -10.795 4.785   1.000 57.480  ? 7   PRO KKK CB  1 
ATOM 15986 C CG  . PRO K 2 7   ? 111.527 -11.162 5.879   1.000 57.490  ? 7   PRO KKK CG  1 
ATOM 15987 C CD  . PRO K 2 7   ? 112.781 -10.394 5.494   1.000 51.810  ? 7   PRO KKK CD  1 
ATOM 15988 N N   . PRO K 2 8   ? 110.356 -10.039 1.352   1.000 50.200  ? 8   PRO KKK N   1 
ATOM 15989 C CA  . PRO K 2 8   ? 109.760 -9.073  0.427   1.000 47.700  ? 8   PRO KKK CA  1 
ATOM 15990 C C   . PRO K 2 8   ? 108.565 -8.329  1.029   1.000 45.270  ? 8   PRO KKK C   1 
ATOM 15991 O O   . PRO K 2 8   ? 108.385 -7.174  0.738   1.000 38.930  ? 8   PRO KKK O   1 
ATOM 15992 C CB  . PRO K 2 8   ? 109.322 -9.932  -0.768  1.000 45.540  ? 8   PRO KKK CB  1 
ATOM 15993 C CG  . PRO K 2 8   ? 110.272 -11.104 -0.727  1.000 44.060  ? 8   PRO KKK CG  1 
ATOM 15994 C CD  . PRO K 2 8   ? 110.413 -11.384 0.758   1.000 49.460  ? 8   PRO KKK CD  1 
ATOM 15995 N N   . SER K 2 9   ? 107.794 -8.997  1.883   1.000 50.240  ? 9   SER KKK N   1 
ATOM 15996 C CA  . SER K 2 9   ? 106.647 -8.374  2.593   1.000 59.030  ? 9   SER KKK CA  1 
ATOM 15997 C C   . SER K 2 9   ? 106.572 -8.865  4.041   1.000 55.230  ? 9   SER KKK C   1 
ATOM 15998 O O   . SER K 2 9   ? 107.134 -9.945  4.359   1.000 49.940  ? 9   SER KKK O   1 
ATOM 15999 C CB  . SER K 2 9   ? 105.358 -8.633  1.862   1.000 69.400  ? 9   SER KKK CB  1 
ATOM 16000 O OG  . SER K 2 9   ? 105.058 -10.028 1.856   1.000 79.830  ? 9   SER KKK OG  1 
ATOM 16001 N N   . ALA K 2 10  ? 105.920 -8.052  4.873   1.000 50.630  ? 10  ALA KKK N   1 
ATOM 16002 C CA  . ALA K 2 10  ? 105.550 -8.342  6.276   1.000 54.030  ? 10  ALA KKK CA  1 
ATOM 16003 C C   . ALA K 2 10  ? 104.282 -7.565  6.596   1.000 57.170  ? 10  ALA KKK C   1 
ATOM 16004 O O   . ALA K 2 10  ? 104.019 -6.565  5.884   1.000 62.300  ? 10  ALA KKK O   1 
ATOM 16005 C CB  . ALA K 2 10  ? 106.675 -7.952  7.198   1.000 55.080  ? 10  ALA KKK CB  1 
ATOM 16006 N N   . SER K 2 11  ? 103.551 -7.992  7.627   1.000 58.490  ? 11  SER KKK N   1 
ATOM 16007 C CA  . SER K 2 11  ? 102.319 -7.323  8.109   1.000 59.230  ? 11  SER KKK CA  1 
ATOM 16008 C C   . SER K 2 11  ? 102.087 -7.619  9.597   1.000 61.670  ? 11  SER KKK C   1 
ATOM 16009 O O   . SER K 2 11  ? 102.784 -8.487  10.149  1.000 53.230  ? 11  SER KKK O   1 
ATOM 16010 C CB  . SER K 2 11  ? 101.148 -7.746  7.288   1.000 57.000  ? 11  SER KKK CB  1 
ATOM 16011 O OG  . SER K 2 11  ? 100.921 -9.134  7.448   1.000 62.670  ? 11  SER KKK OG  1 
ATOM 16012 N N   . GLY K 2 12  ? 101.136 -6.898  10.202  1.000 67.020  ? 12  GLY KKK N   1 
ATOM 16013 C CA  . GLY K 2 12  ? 100.687 -7.057  11.600  1.000 68.980  ? 12  GLY KKK CA  1 
ATOM 16014 C C   . GLY K 2 12  ? 99.402  -6.275  11.867  1.000 82.500  ? 12  GLY KKK C   1 
ATOM 16015 O O   . GLY K 2 12  ? 99.006  -5.429  11.017  1.000 92.690  ? 12  GLY KKK O   1 
ATOM 16016 N N   . THR K 2 13  ? 98.765  -6.544  13.010  1.000 87.150  ? 13  THR KKK N   1 
ATOM 16017 C CA  . THR K 2 13  ? 97.554  -5.843  13.518  1.000 86.700  ? 13  THR KKK CA  1 
ATOM 16018 C C   . THR K 2 13  ? 97.992  -4.688  14.424  1.000 76.580  ? 13  THR KKK C   1 
ATOM 16019 O O   . THR K 2 13  ? 98.928  -4.838  15.211  1.000 65.520  ? 13  THR KKK O   1 
ATOM 16020 C CB  . THR K 2 13  ? 96.603  -6.843  14.198  1.000 94.190  ? 13  THR KKK CB  1 
ATOM 16021 O OG1 . THR K 2 13  ? 95.363  -6.165  14.390  1.000 107.050 ? 13  THR KKK OG1 1 
ATOM 16022 C CG2 . THR K 2 13  ? 97.073  -7.378  15.533  1.000 94.890  ? 13  THR KKK CG2 1 
ATOM 16023 N N   . PRO K 2 14  ? 97.333  -3.508  14.364  1.000 66.600  ? 14  PRO KKK N   1 
ATOM 16024 C CA  . PRO K 2 14  ? 97.715  -2.370  15.197  1.000 67.720  ? 14  PRO KKK CA  1 
ATOM 16025 C C   . PRO K 2 14  ? 97.972  -2.798  16.644  1.000 67.360  ? 14  PRO KKK C   1 
ATOM 16026 O O   . PRO K 2 14  ? 97.178  -3.573  17.140  1.000 75.650  ? 14  PRO KKK O   1 
ATOM 16027 C CB  . PRO K 2 14  ? 96.530  -1.401  15.085  1.000 61.200  ? 14  PRO KKK CB  1 
ATOM 16028 C CG  . PRO K 2 14  ? 95.966  -1.694  13.708  1.000 64.830  ? 14  PRO KKK CG  1 
ATOM 16029 C CD  . PRO K 2 14  ? 96.215  -3.173  13.476  1.000 67.620  ? 14  PRO KKK CD  1 
ATOM 16030 N N   . GLY K 2 15  ? 99.074  -2.337  17.237  1.000 67.210  ? 15  GLY KKK N   1 
ATOM 16031 C CA  . GLY K 2 15  ? 99.451  -2.622  18.632  1.000 60.000  ? 15  GLY KKK CA  1 
ATOM 16032 C C   . GLY K 2 15  ? 100.399 -3.806  18.731  1.000 61.580  ? 15  GLY KKK C   1 
ATOM 16033 O O   . GLY K 2 15  ? 101.055 -3.928  19.783  1.000 64.910  ? 15  GLY KKK O   1 
ATOM 16034 N N   . GLN K 2 16  ? 100.482 -4.649  17.692  1.000 61.410  ? 16  GLN KKK N   1 
ATOM 16035 C CA  . GLN K 2 16  ? 101.373 -5.845  17.663  1.000 69.060  ? 16  GLN KKK CA  1 
ATOM 16036 C C   . GLN K 2 16  ? 102.843 -5.421  17.543  1.000 63.710  ? 16  GLN KKK C   1 
ATOM 16037 O O   . GLN K 2 16  ? 103.127 -4.234  17.239  1.000 69.750  ? 16  GLN KKK O   1 
ATOM 16038 C CB  . GLN K 2 16  ? 101.057 -6.782  16.494  1.000 72.140  ? 16  GLN KKK CB  1 
ATOM 16039 C CG  . GLN K 2 16  ? 100.124 -7.927  16.852  1.000 73.640  ? 16  GLN KKK CG  1 
ATOM 16040 C CD  . GLN K 2 16  ? 99.908  -8.868  15.690  1.000 77.870  ? 16  GLN KKK CD  1 
ATOM 16041 O OE1 . GLN K 2 16  ? 99.902  -8.473  14.516  1.000 70.110  ? 16  GLN KKK OE1 1 
ATOM 16042 N NE2 . GLN K 2 16  ? 99.687  -10.131 16.016  1.000 79.900  ? 16  GLN KKK NE2 1 
ATOM 16043 N N   . ARG K 2 17  ? 103.738 -6.378  17.788  1.000 57.640  ? 17  ARG KKK N   1 
ATOM 16044 C CA  . ARG K 2 17  ? 105.183 -6.319  17.457  1.000 62.240  ? 17  ARG KKK CA  1 
ATOM 16045 C C   . ARG K 2 17  ? 105.421 -7.110  16.166  1.000 60.420  ? 17  ARG KKK C   1 
ATOM 16046 O O   . ARG K 2 17  ? 105.056 -8.279  16.127  1.000 69.790  ? 17  ARG KKK O   1 
ATOM 16047 C CB  . ARG K 2 17  ? 106.017 -6.864  18.625  1.000 65.160  ? 17  ARG KKK CB  1 
ATOM 16048 C CG  . ARG K 2 17  ? 107.522 -6.823  18.408  1.000 67.470  ? 17  ARG KKK CG  1 
ATOM 16049 C CD  . ARG K 2 17  ? 108.323 -6.454  19.649  1.000 69.790  ? 17  ARG KKK CD  1 
ATOM 16050 N NE  . ARG K 2 17  ? 109.529 -7.264  19.721  1.000 76.380  ? 17  ARG KKK NE  1 
ATOM 16051 C CZ  . ARG K 2 17  ? 110.555 -7.056  20.531  1.000 76.460  ? 17  ARG KKK CZ  1 
ATOM 16052 N NH1 . ARG K 2 17  ? 110.578 -6.013  21.349  1.000 69.960  ? 17  ARG KKK NH1 1 
ATOM 16053 N NH2 . ARG K 2 17  ? 111.571 -7.906  20.494  1.000 76.460  ? 17  ARG KKK NH2 1 
ATOM 16054 N N   . VAL K 2 18  ? 105.975 -6.467  15.141  1.000 63.950  ? 18  VAL KKK N   1 
ATOM 16055 C CA  . VAL K 2 18  ? 106.415 -7.103  13.864  1.000 64.170  ? 18  VAL KKK CA  1 
ATOM 16056 C C   . VAL K 2 18  ? 107.941 -7.175  13.875  1.000 62.420  ? 18  VAL KKK C   1 
ATOM 16057 O O   . VAL K 2 18  ? 108.569 -6.263  14.462  1.000 68.830  ? 18  VAL KKK O   1 
ATOM 16058 C CB  . VAL K 2 18  ? 105.919 -6.307  12.645  1.000 68.200  ? 18  VAL KKK CB  1 
ATOM 16059 C CG1 . VAL K 2 18  ? 106.128 -7.075  11.354  1.000 74.390  ? 18  VAL KKK CG1 1 
ATOM 16060 C CG2 . VAL K 2 18  ? 104.460 -5.911  12.794  1.000 73.720  ? 18  VAL KKK CG2 1 
ATOM 16061 N N   . THR K 2 19  ? 108.510 -8.196  13.229  1.000 54.910  ? 19  THR KKK N   1 
ATOM 16062 C CA  . THR K 2 19  ? 109.976 -8.409  13.145  1.000 53.320  ? 19  THR KKK CA  1 
ATOM 16063 C C   . THR K 2 19  ? 110.368 -8.575  11.668  1.000 52.230  ? 19  THR KKK C   1 
ATOM 16064 O O   . THR K 2 19  ? 109.880 -9.516  11.034  1.000 52.980  ? 19  THR KKK O   1 
ATOM 16065 C CB  . THR K 2 19  ? 110.388 -9.557  14.079  1.000 53.300  ? 19  THR KKK CB  1 
ATOM 16066 O OG1 . THR K 2 19  ? 111.794 -9.444  14.287  1.000 53.550  ? 19  THR KKK OG1 1 
ATOM 16067 C CG2 . THR K 2 19  ? 110.057 -10.950 13.566  1.000 52.550  ? 19  THR KKK CG2 1 
ATOM 16068 N N   . ILE K 2 20  ? 111.204 -7.680  11.131  1.000 54.930  ? 20  ILE KKK N   1 
ATOM 16069 C CA  . ILE K 2 20  ? 111.800 -7.815  9.765   1.000 57.980  ? 20  ILE KKK CA  1 
ATOM 16070 C C   . ILE K 2 20  ? 113.266 -8.238  9.900   1.000 50.430  ? 20  ILE KKK C   1 
ATOM 16071 O O   . ILE K 2 20  ? 114.034 -7.511  10.541  1.000 49.930  ? 20  ILE KKK O   1 
ATOM 16072 C CB  . ILE K 2 20  ? 111.672 -6.519  8.939   1.000 64.650  ? 20  ILE KKK CB  1 
ATOM 16073 C CG1 . ILE K 2 20  ? 110.263 -5.913  9.025   1.000 67.350  ? 20  ILE KKK CG1 1 
ATOM 16074 C CG2 . ILE K 2 20  ? 112.085 -6.796  7.495   1.000 67.460  ? 20  ILE KKK CG2 1 
ATOM 16075 C CD1 . ILE K 2 20  ? 110.096 -4.550  8.385   1.000 65.420  ? 20  ILE KKK CD1 1 
ATOM 16076 N N   . SER K 2 21  ? 113.635 -9.374  9.317   1.000 45.500  ? 21  SER KKK N   1 
ATOM 16077 C CA  . SER K 2 21  ? 115.000 -9.940  9.401   1.000 47.880  ? 21  SER KKK CA  1 
ATOM 16078 C C   . SER K 2 21  ? 115.824 -9.485  8.191   1.000 46.680  ? 21  SER KKK C   1 
ATOM 16079 O O   . SER K 2 21  ? 115.240 -9.197  7.143   1.000 49.840  ? 21  SER KKK O   1 
ATOM 16080 C CB  . SER K 2 21  ? 114.964 -11.444 9.524   1.000 50.120  ? 21  SER KKK CB  1 
ATOM 16081 O OG  . SER K 2 21  ? 114.290 -12.022 8.425   1.000 52.410  ? 21  SER KKK OG  1 
ATOM 16082 N N   . CYS K 2 22  ? 117.146 -9.428  8.357   1.000 44.730  ? 22  CYS KKK N   1 
ATOM 16083 C CA  . CYS K 2 22  ? 118.152 -9.175  7.299   1.000 43.070  ? 22  CYS KKK CA  1 
ATOM 16084 C C   . CYS K 2 22  ? 119.325 -10.132 7.499   1.000 46.390  ? 22  CYS KKK C   1 
ATOM 16085 O O   . CYS K 2 22  ? 119.959 -10.077 8.551   1.000 54.900  ? 22  CYS KKK O   1 
ATOM 16086 C CB  . CYS K 2 22  ? 118.626 -7.728  7.304   1.000 41.790  ? 22  CYS KKK CB  1 
ATOM 16087 S SG  . CYS K 2 22  ? 119.207 -7.255  5.659   1.000 43.210  ? 22  CYS KKK SG  1 
ATOM 16088 N N   . SER K 2 23  ? 119.550 -11.028 6.545   1.000 47.970  ? 23  SER KKK N   1 
ATOM 16089 C CA  . SER K 2 23  ? 120.565 -12.102 6.619   1.000 48.650  ? 23  SER KKK CA  1 
ATOM 16090 C C   . SER K 2 23  ? 121.636 -11.828 5.559   1.000 46.900  ? 23  SER KKK C   1 
ATOM 16091 O O   . SER K 2 23  ? 121.261 -11.578 4.403   1.000 49.450  ? 23  SER KKK O   1 
ATOM 16092 C CB  . SER K 2 23  ? 119.942 -13.456 6.436   1.000 55.720  ? 23  SER KKK CB  1 
ATOM 16093 O OG  . SER K 2 23  ? 120.940 -14.464 6.373   1.000 66.090  ? 23  SER KKK OG  1 
ATOM 16094 N N   . GLY K 2 24  ? 122.898 -11.860 5.958   1.000 42.400  ? 24  GLY KKK N   1 
ATOM 16095 C CA  . GLY K 2 24  ? 124.070 -11.635 5.075   1.000 39.380  ? 24  GLY KKK CA  1 
ATOM 16096 C C   . GLY K 2 24  ? 125.120 -12.708 5.251   1.000 38.240  ? 24  GLY KKK C   1 
ATOM 16097 O O   . GLY K 2 24  ? 124.741 -13.832 5.565   1.000 41.330  ? 24  GLY KKK O   1 
ATOM 16098 N N   . GLY K 2 25  ? 126.395 -12.361 5.042   1.000 37.410  ? 25  GLY KKK N   1 
ATOM 16099 C CA  . GLY K 2 25  ? 127.550 -13.266 5.195   1.000 37.710  ? 25  GLY KKK CA  1 
ATOM 16100 C C   . GLY K 2 25  ? 128.755 -12.567 5.801   1.000 36.880  ? 25  GLY KKK C   1 
ATOM 16101 O O   . GLY K 2 25  ? 128.697 -11.331 5.980   1.000 37.480  ? 25  GLY KKK O   1 
ATOM 16102 N N   . SER K 2 26  ? 129.821 -13.316 6.069   1.000 35.900  ? 26  SER KKK N   1 
ATOM 16103 C CA  . SER K 2 26  ? 131.021 -12.803 6.781   1.000 36.790  ? 26  SER KKK CA  1 
ATOM 16104 C C   . SER K 2 26  ? 131.569 -11.547 6.085   1.000 39.450  ? 26  SER KKK C   1 
ATOM 16105 O O   . SER K 2 26  ? 132.013 -10.631 6.775   1.000 38.770  ? 26  SER KKK O   1 
ATOM 16106 C CB  . SER K 2 26  ? 132.068 -13.856 6.947   1.000 35.050  ? 26  SER KKK CB  1 
ATOM 16107 O OG  . SER K 2 26  ? 132.687 -14.159 5.720   1.000 37.760  ? 26  SER KKK OG  1 
ATOM 16108 N N   . SER K 2 27  ? 131.522 -11.494 4.756   1.000 44.930  ? 27  SER KKK N   1 
ATOM 16109 C CA  . SER K 2 27  ? 132.046 -10.381 3.913   1.000 45.050  ? 27  SER KKK CA  1 
ATOM 16110 C C   . SER K 2 27  ? 131.279 -9.068  4.166   1.000 39.190  ? 27  SER KKK C   1 
ATOM 16111 O O   . SER K 2 27  ? 131.875 -7.995  3.967   1.000 36.940  ? 27  SER KKK O   1 
ATOM 16112 C CB  . SER K 2 27  ? 131.996 -10.821 2.461   1.000 54.340  ? 27  SER KKK CB  1 
ATOM 16113 O OG  . SER K 2 27  ? 132.242 -9.771  1.533   1.000 67.860  ? 27  SER KKK OG  1 
ATOM 16114 N N   . ASN K 2 28  ? 130.002 -9.133  4.545   1.000 35.620  ? 28  ASN KKK N   1 
ATOM 16115 C CA  . ASN K 2 28  ? 129.191 -7.920  4.802   1.000 35.840  ? 28  ASN KKK CA  1 
ATOM 16116 C C   . ASN K 2 28  ? 128.836 -7.853  6.291   1.000 35.580  ? 28  ASN KKK C   1 
ATOM 16117 O O   . ASN K 2 28  ? 129.656 -7.299  7.050   1.000 34.450  ? 28  ASN KKK O   1 
ATOM 16118 C CB  . ASN K 2 28  ? 127.995 -7.820  3.848   1.000 38.590  ? 28  ASN KKK CB  1 
ATOM 16119 C CG  . ASN K 2 28  ? 127.196 -9.087  3.685   1.000 35.440  ? 28  ASN KKK CG  1 
ATOM 16120 O OD1 . ASN K 2 28  ? 126.630 -9.544  4.665   1.000 40.320  ? 28  ASN KKK OD1 1 
ATOM 16121 N ND2 . ASN K 2 28  ? 127.088 -9.602  2.468   1.000 31.520  ? 28  ASN KKK ND2 1 
ATOM 16122 N N   . ILE K 2 29  ? 127.686 -8.402  6.697   1.000 38.420  ? 29  ILE KKK N   1 
ATOM 16123 C CA  . ILE K 2 29  ? 127.063 -8.162  8.036   1.000 35.560  ? 29  ILE KKK CA  1 
ATOM 16124 C C   . ILE K 2 29  ? 127.967 -8.722  9.137   1.000 35.310  ? 29  ILE KKK C   1 
ATOM 16125 O O   . ILE K 2 29  ? 127.918 -8.166  10.264  1.000 43.820  ? 29  ILE KKK O   1 
ATOM 16126 C CB  . ILE K 2 29  ? 125.630 -8.716  8.121   1.000 31.150  ? 29  ILE KKK CB  1 
ATOM 16127 C CG1 . ILE K 2 29  ? 124.708 -7.946  7.180   1.000 31.910  ? 29  ILE KKK CG1 1 
ATOM 16128 C CG2 . ILE K 2 29  ? 125.137 -8.658  9.552   1.000 31.450  ? 29  ILE KKK CG2 1 
ATOM 16129 C CD1 . ILE K 2 29  ? 123.221 -8.255  7.335   1.000 35.660  ? 29  ILE KKK CD1 1 
ATOM 16130 N N   . GLY K 2 30  ? 128.746 -9.759  8.827   1.000 32.380  ? 30  GLY KKK N   1 
ATOM 16131 C CA  . GLY K 2 30  ? 129.679 -10.379 9.785   1.000 35.340  ? 30  GLY KKK CA  1 
ATOM 16132 C C   . GLY K 2 30  ? 130.655 -9.363  10.333  1.000 33.990  ? 30  GLY KKK C   1 
ATOM 16133 O O   . GLY K 2 30  ? 130.745 -9.222  11.561  1.000 37.820  ? 30  GLY KKK O   1 
ATOM 16134 N N   . SER K 2 31  ? 131.286 -8.617  9.434   1.000 33.400  ? 31  SER KKK N   1 
ATOM 16135 C CA  . SER K 2 31  ? 132.385 -7.674  9.736   1.000 34.370  ? 31  SER KKK CA  1 
ATOM 16136 C C   . SER K 2 31  ? 131.958 -6.208  9.639   1.000 29.900  ? 31  SER KKK C   1 
ATOM 16137 O O   . SER K 2 31  ? 132.809 -5.389  9.985   1.000 26.890  ? 31  SER KKK O   1 
ATOM 16138 C CB  . SER K 2 31  ? 133.554 -7.940  8.837   1.000 39.490  ? 31  SER KKK CB  1 
ATOM 16139 O OG  . SER K 2 31  ? 134.145 -9.205  9.150   1.000 43.600  ? 31  SER KKK OG  1 
ATOM 16140 N N   . ASN K 2 32  ? 130.726 -5.891  9.209   1.000 29.590  ? 32  ASN KKK N   1 
ATOM 16141 C CA  . ASN K 2 32  ? 130.271 -4.483  9.008   1.000 29.110  ? 32  ASN KKK CA  1 
ATOM 16142 C C   . ASN K 2 32  ? 128.877 -4.243  9.587   1.000 30.270  ? 32  ASN KKK C   1 
ATOM 16143 O O   . ASN K 2 32  ? 128.057 -5.160  9.675   1.000 35.830  ? 32  ASN KKK O   1 
ATOM 16144 C CB  . ASN K 2 32  ? 130.376 -4.083  7.541   1.000 29.780  ? 32  ASN KKK CB  1 
ATOM 16145 C CG  . ASN K 2 32  ? 131.781 -4.274  7.012   1.000 29.530  ? 32  ASN KKK CG  1 
ATOM 16146 O OD1 . ASN K 2 32  ? 132.694 -3.551  7.404   1.000 28.400  ? 32  ASN KKK OD1 1 
ATOM 16147 N ND2 . ASN K 2 32  ? 131.967 -5.233  6.111   1.000 27.510  ? 32  ASN KKK ND2 1 
ATOM 16148 N N   . PRO K 2 33  ? 128.580 -3.004  10.060  1.000 29.240  ? 33  PRO KKK N   1 
ATOM 16149 C CA  . PRO K 2 33  ? 127.302 -2.678  10.686  1.000 28.840  ? 33  PRO KKK CA  1 
ATOM 16150 C C   . PRO K 2 33  ? 126.164 -2.498  9.685   1.000 28.170  ? 33  PRO KKK C   1 
ATOM 16151 O O   . PRO K 2 33  ? 126.421 -2.023  8.598   1.000 32.190  ? 33  PRO KKK O   1 
ATOM 16152 C CB  . PRO K 2 33  ? 127.504 -1.303  11.339  1.000 29.890  ? 33  PRO KKK CB  1 
ATOM 16153 C CG  . PRO K 2 33  ? 128.980 -1.089  11.292  1.000 31.030  ? 33  PRO KKK CG  1 
ATOM 16154 C CD  . PRO K 2 33  ? 129.454 -1.833  10.056  1.000 30.690  ? 33  PRO KKK CD  1 
ATOM 16155 N N   . VAL K 2 34  ? 124.946 -2.824  10.116  1.000 27.040  ? 34  VAL KKK N   1 
ATOM 16156 C CA  . VAL K 2 34  ? 123.688 -2.657  9.340   1.000 28.000  ? 34  VAL KKK CA  1 
ATOM 16157 C C   . VAL K 2 34  ? 122.970 -1.382  9.778   1.000 31.380  ? 34  VAL KKK C   1 
ATOM 16158 O O   . VAL K 2 34  ? 122.672 -1.266  10.983  1.000 31.000  ? 34  VAL KKK O   1 
ATOM 16159 C CB  . VAL K 2 34  ? 122.772 -3.859  9.567   1.000 28.960  ? 34  VAL KKK CB  1 
ATOM 16160 C CG1 . VAL K 2 34  ? 121.437 -3.672  8.852   1.000 30.290  ? 34  VAL KKK CG1 1 
ATOM 16161 C CG2 . VAL K 2 34  ? 123.465 -5.149  9.155   1.000 31.140  ? 34  VAL KKK CG2 1 
ATOM 16162 N N   . ASN K 2 35  ? 122.682 -0.478  8.840   1.000 34.180  ? 35  ASN KKK N   1 
ATOM 16163 C CA  . ASN K 2 35  ? 121.675 0.598   9.045   1.000 35.550  ? 35  ASN KKK CA  1 
ATOM 16164 C C   . ASN K 2 35  ? 120.359 0.147   8.404   1.000 37.360  ? 35  ASN KKK C   1 
ATOM 16165 O O   . ASN K 2 35  ? 120.392 -0.557  7.369   1.000 33.400  ? 35  ASN KKK O   1 
ATOM 16166 C CB  . ASN K 2 35  ? 122.108 1.961   8.483   1.000 35.500  ? 35  ASN KKK CB  1 
ATOM 16167 C CG  . ASN K 2 35  ? 123.335 2.533   9.155   1.000 35.090  ? 35  ASN KKK CG  1 
ATOM 16168 O OD1 . ASN K 2 35  ? 124.194 1.788   9.611   1.000 34.280  ? 35  ASN KKK OD1 1 
ATOM 16169 N ND2 . ASN K 2 35  ? 123.441 3.852   9.176   1.000 36.630  ? 35  ASN KKK ND2 1 
ATOM 16170 N N   . TRP K 2 36  ? 119.245 0.526   9.031   1.000 42.680  ? 36  TRP KKK N   1 
ATOM 16171 C CA  . TRP K 2 36  ? 117.859 0.388   8.505   1.000 43.670  ? 36  TRP KKK CA  1 
ATOM 16172 C C   . TRP K 2 36  ? 117.372 1.759   8.048   1.000 42.960  ? 36  TRP KKK C   1 
ATOM 16173 O O   . TRP K 2 36  ? 117.543 2.725   8.810   1.000 40.010  ? 36  TRP KKK O   1 
ATOM 16174 C CB  . TRP K 2 36  ? 116.924 -0.193  9.576   1.000 41.940  ? 36  TRP KKK CB  1 
ATOM 16175 C CG  . TRP K 2 36  ? 117.177 -1.633  9.881   1.000 41.790  ? 36  TRP KKK CG  1 
ATOM 16176 C CD1 . TRP K 2 36  ? 118.007 -2.146  10.839  1.000 46.330  ? 36  TRP KKK CD1 1 
ATOM 16177 C CD2 . TRP K 2 36  ? 116.612 -2.758  9.194   1.000 39.060  ? 36  TRP KKK CD2 1 
ATOM 16178 N NE1 . TRP K 2 36  ? 117.992 -3.512  10.798  1.000 45.250  ? 36  TRP KKK NE1 1 
ATOM 16179 C CE2 . TRP K 2 36  ? 117.140 -3.914  9.801   1.000 41.260  ? 36  TRP KKK CE2 1 
ATOM 16180 C CE3 . TRP K 2 36  ? 115.697 -2.897  8.152   1.000 40.010  ? 36  TRP KKK CE3 1 
ATOM 16181 C CZ2 . TRP K 2 36  ? 116.769 -5.192  9.399   1.000 40.600  ? 36  TRP KKK CZ2 1 
ATOM 16182 C CZ3 . TRP K 2 36  ? 115.328 -4.161  7.756   1.000 41.230  ? 36  TRP KKK CZ3 1 
ATOM 16183 C CH2 . TRP K 2 36  ? 115.861 -5.291  8.372   1.000 41.580  ? 36  TRP KKK CH2 1 
ATOM 16184 N N   . PHE K 2 37  ? 116.766 1.839   6.865   1.000 42.790  ? 37  PHE KKK N   1 
ATOM 16185 C CA  . PHE K 2 37  ? 116.154 3.090   6.341   1.000 39.690  ? 37  PHE KKK CA  1 
ATOM 16186 C C   . PHE K 2 37  ? 114.656 2.850   6.144   1.000 40.120  ? 37  PHE KKK C   1 
ATOM 16187 O O   . PHE K 2 37  ? 114.280 1.759   5.647   1.000 39.420  ? 37  PHE KKK O   1 
ATOM 16188 C CB  . PHE K 2 37  ? 116.860 3.537   5.056   1.000 33.280  ? 37  PHE KKK CB  1 
ATOM 16189 C CG  . PHE K 2 37  ? 118.349 3.682   5.208   1.000 29.670  ? 37  PHE KKK CG  1 
ATOM 16190 C CD1 . PHE K 2 37  ? 118.885 4.815   5.773   1.000 29.690  ? 37  PHE KKK CD1 1 
ATOM 16191 C CD2 . PHE K 2 37  ? 119.203 2.668   4.811   1.000 28.680  ? 37  PHE KKK CD2 1 
ATOM 16192 C CE1 . PHE K 2 37  ? 120.256 4.936   5.931   1.000 29.710  ? 37  PHE KKK CE1 1 
ATOM 16193 C CE2 . PHE K 2 37  ? 120.576 2.800   4.935   1.000 27.900  ? 37  PHE KKK CE2 1 
ATOM 16194 C CZ  . PHE K 2 37  ? 121.109 3.931   5.494   1.000 28.950  ? 37  PHE KKK CZ  1 
ATOM 16195 N N   . GLN K 2 38  ? 113.847 3.820   6.572   1.000 37.460  ? 38  GLN KKK N   1 
ATOM 16196 C CA  . GLN K 2 38  ? 112.373 3.817   6.390   1.000 39.250  ? 38  GLN KKK CA  1 
ATOM 16197 C C   . GLN K 2 38  ? 112.081 4.668   5.164   1.000 39.870  ? 38  GLN KKK C   1 
ATOM 16198 O O   . GLN K 2 38  ? 112.725 5.711   5.037   1.000 43.290  ? 38  GLN KKK O   1 
ATOM 16199 C CB  . GLN K 2 38  ? 111.673 4.347   7.642   1.000 40.170  ? 38  GLN KKK CB  1 
ATOM 16200 C CG  . GLN K 2 38  ? 110.158 4.287   7.578   1.000 39.950  ? 38  GLN KKK CG  1 
ATOM 16201 C CD  . GLN K 2 38  ? 109.541 4.982   8.769   1.000 40.720  ? 38  GLN KKK CD  1 
ATOM 16202 O OE1 . GLN K 2 38  ? 109.671 6.200   8.955   1.000 41.410  ? 38  GLN KKK OE1 1 
ATOM 16203 N NE2 . GLN K 2 38  ? 108.863 4.195   9.590   1.000 39.700  ? 38  GLN KKK NE2 1 
ATOM 16204 N N   . GLN K 2 39  ? 111.193 4.199   4.283   1.000 40.940  ? 39  GLN KKK N   1 
ATOM 16205 C CA  . GLN K 2 39  ? 110.786 4.906   3.047   1.000 42.400  ? 39  GLN KKK CA  1 
ATOM 16206 C C   . GLN K 2 39  ? 109.260 4.860   2.898   1.000 48.410  ? 39  GLN KKK C   1 
ATOM 16207 O O   . GLN K 2 39  ? 108.692 3.769   2.721   1.000 51.650  ? 39  GLN KKK O   1 
ATOM 16208 C CB  . GLN K 2 39  ? 111.460 4.287   1.828   1.000 44.260  ? 39  GLN KKK CB  1 
ATOM 16209 C CG  . GLN K 2 39  ? 111.398 5.193   0.599   1.000 46.750  ? 39  GLN KKK CG  1 
ATOM 16210 C CD  . GLN K 2 39  ? 112.087 4.602   -0.616  1.000 47.040  ? 39  GLN KKK CD  1 
ATOM 16211 O OE1 . GLN K 2 39  ? 112.190 3.373   -0.769  1.000 40.710  ? 39  GLN KKK OE1 1 
ATOM 16212 N NE2 . GLN K 2 39  ? 112.592 5.490   -1.468  1.000 46.750  ? 39  GLN KKK NE2 1 
ATOM 16213 N N   . PHE K 2 40  ? 108.623 6.023   2.971   1.000 50.740  ? 40  PHE KKK N   1 
ATOM 16214 C CA  . PHE K 2 40  ? 107.212 6.218   2.572   1.000 53.850  ? 40  PHE KKK CA  1 
ATOM 16215 C C   . PHE K 2 40  ? 107.169 6.472   1.071   1.000 60.420  ? 40  PHE KKK C   1 
ATOM 16216 O O   . PHE K 2 40  ? 108.055 7.149   0.552   1.000 65.110  ? 40  PHE KKK O   1 
ATOM 16217 C CB  . PHE K 2 40  ? 106.601 7.367   3.360   1.000 57.950  ? 40  PHE KKK CB  1 
ATOM 16218 C CG  . PHE K 2 40  ? 106.641 7.133   4.843   1.000 56.590  ? 40  PHE KKK CG  1 
ATOM 16219 C CD1 . PHE K 2 40  ? 106.124 5.977   5.391   1.000 61.940  ? 40  PHE KKK CD1 1 
ATOM 16220 C CD2 . PHE K 2 40  ? 107.212 8.066   5.685   1.000 58.290  ? 40  PHE KKK CD2 1 
ATOM 16221 C CE1 . PHE K 2 40  ? 106.139 5.781   6.763   1.000 70.070  ? 40  PHE KKK CE1 1 
ATOM 16222 C CE2 . PHE K 2 40  ? 107.246 7.862   7.054   1.000 58.150  ? 40  PHE KKK CE2 1 
ATOM 16223 C CZ  . PHE K 2 40  ? 106.727 6.716   7.589   1.000 65.190  ? 40  PHE KKK CZ  1 
ATOM 16224 N N   . PRO K 2 41  ? 106.170 5.901   0.354   1.000 65.930  ? 41  PRO KKK N   1 
ATOM 16225 C CA  . PRO K 2 41  ? 106.033 6.083   -1.093  1.000 57.410  ? 41  PRO KKK CA  1 
ATOM 16226 C C   . PRO K 2 41  ? 106.293 7.520   -1.556  1.000 52.860  ? 41  PRO KKK C   1 
ATOM 16227 O O   . PRO K 2 41  ? 105.824 8.437   -0.911  1.000 40.380  ? 41  PRO KKK O   1 
ATOM 16228 C CB  . PRO K 2 41  ? 104.575 5.716   -1.339  1.000 60.440  ? 41  PRO KKK CB  1 
ATOM 16229 C CG  . PRO K 2 41  ? 104.304 4.630   -0.316  1.000 67.580  ? 41  PRO KKK CG  1 
ATOM 16230 C CD  . PRO K 2 41  ? 105.127 5.013   0.901   1.000 70.340  ? 41  PRO KKK CD  1 
ATOM 16231 N N   . GLY K 2 42  ? 107.109 7.655   -2.608  1.000 55.640  ? 42  GLY KKK N   1 
ATOM 16232 C CA  . GLY K 2 42  ? 107.388 8.921   -3.309  1.000 52.040  ? 42  GLY KKK CA  1 
ATOM 16233 C C   . GLY K 2 42  ? 108.183 9.916   -2.487  1.000 48.270  ? 42  GLY KKK C   1 
ATOM 16234 O O   . GLY K 2 42  ? 108.306 11.047  -2.948  1.000 49.420  ? 42  GLY KKK O   1 
ATOM 16235 N N   . THR K 2 43  ? 108.728 9.522   -1.331  1.000 48.660  ? 43  THR KKK N   1 
ATOM 16236 C CA  . THR K 2 43  ? 109.770 10.293  -0.596  1.000 49.910  ? 43  THR KKK CA  1 
ATOM 16237 C C   . THR K 2 43  ? 111.083 9.496   -0.603  1.000 57.030  ? 43  THR KKK C   1 
ATOM 16238 O O   . THR K 2 43  ? 111.096 8.325   -1.039  1.000 55.370  ? 43  THR KKK O   1 
ATOM 16239 C CB  . THR K 2 43  ? 109.328 10.692  0.817   1.000 43.890  ? 43  THR KKK CB  1 
ATOM 16240 O OG1 . THR K 2 43  ? 108.890 9.528   1.520   1.000 43.700  ? 43  THR KKK OG1 1 
ATOM 16241 N N   . ALA K 2 44  ? 112.161 10.145  -0.176  1.000 57.830  ? 44  ALA KKK N   1 
ATOM 16242 C CA  . ALA K 2 44  ? 113.504 9.547   -0.031  1.000 48.840  ? 44  ALA KKK CA  1 
ATOM 16243 C C   . ALA K 2 44  ? 113.475 8.558   1.120   1.000 42.920  ? 44  ALA KKK C   1 
ATOM 16244 O O   . ALA K 2 44  ? 112.584 8.646   1.967   1.000 40.180  ? 44  ALA KKK O   1 
ATOM 16245 C CB  . ALA K 2 44  ? 114.518 10.633  0.232   1.000 54.980  ? 44  ALA KKK CB  1 
ATOM 16246 N N   . PRO K 2 45  ? 114.449 7.616   1.187   1.000 39.160  ? 45  PRO KKK N   1 
ATOM 16247 C CA  . PRO K 2 45  ? 114.735 6.875   2.405   1.000 36.380  ? 45  PRO KKK CA  1 
ATOM 16248 C C   . PRO K 2 45  ? 115.191 7.845   3.499   1.000 37.170  ? 45  PRO KKK C   1 
ATOM 16249 O O   . PRO K 2 45  ? 115.697 8.882   3.172   1.000 35.190  ? 45  PRO KKK O   1 
ATOM 16250 C CB  . PRO K 2 45  ? 115.889 5.938   2.031   1.000 33.820  ? 45  PRO KKK CB  1 
ATOM 16251 C CG  . PRO K 2 45  ? 115.836 5.844   0.545   1.000 32.740  ? 45  PRO KKK CG  1 
ATOM 16252 C CD  . PRO K 2 45  ? 115.351 7.207   0.106   1.000 38.560  ? 45  PRO KKK CD  1 
ATOM 16253 N N   . LYS K 2 46  ? 114.988 7.468   4.759   1.000 39.280  ? 46  LYS KKK N   1 
ATOM 16254 C CA  . LYS K 2 46  ? 115.469 8.194   5.954   1.000 39.180  ? 46  LYS KKK CA  1 
ATOM 16255 C C   . LYS K 2 46  ? 116.051 7.166   6.929   1.000 37.380  ? 46  LYS KKK C   1 
ATOM 16256 O O   . LYS K 2 46  ? 115.578 6.011   6.933   1.000 37.290  ? 46  LYS KKK O   1 
ATOM 16257 C CB  . LYS K 2 46  ? 114.338 9.014   6.580   1.000 40.620  ? 46  LYS KKK CB  1 
ATOM 16258 C CG  . LYS K 2 46  ? 114.771 9.890   7.763   1.000 44.530  ? 46  LYS KKK CG  1 
ATOM 16259 C CD  . LYS K 2 46  ? 113.682 10.632  8.484   1.000 50.230  ? 46  LYS KKK CD  1 
ATOM 16260 C CE  . LYS K 2 46  ? 113.450 12.037  7.972   1.000 54.610  ? 46  LYS KKK CE  1 
ATOM 16261 N NZ  . LYS K 2 46  ? 112.189 12.576  8.534   1.000 57.460  ? 46  LYS KKK NZ  1 
ATOM 16262 N N   . LEU K 2 47  ? 117.060 7.562   7.698   1.000 36.630  ? 47  LEU KKK N   1 
ATOM 16263 C CA  . LEU K 2 47  ? 117.708 6.687   8.711   1.000 35.860  ? 47  LEU KKK CA  1 
ATOM 16264 C C   . LEU K 2 47  ? 116.690 6.353   9.800   1.000 35.950  ? 47  LEU KKK C   1 
ATOM 16265 O O   . LEU K 2 47  ? 116.120 7.300   10.387  1.000 39.630  ? 47  LEU KKK O   1 
ATOM 16266 C CB  . LEU K 2 47  ? 118.915 7.409   9.310   1.000 34.270  ? 47  LEU KKK CB  1 
ATOM 16267 C CG  . LEU K 2 47  ? 119.728 6.578   10.291  1.000 32.680  ? 47  LEU KKK CG  1 
ATOM 16268 C CD1 . LEU K 2 47  ? 120.295 5.351   9.610   1.000 33.670  ? 47  LEU KKK CD1 1 
ATOM 16269 C CD2 . LEU K 2 47  ? 120.831 7.394   10.929  1.000 32.470  ? 47  LEU KKK CD2 1 
ATOM 16270 N N   . LEU K 2 48  ? 116.484 5.061   10.060  1.000 36.650  ? 48  LEU KKK N   1 
ATOM 16271 C CA  . LEU K 2 48  ? 115.601 4.546   11.146  1.000 34.340  ? 48  LEU KKK CA  1 
ATOM 16272 C C   . LEU K 2 48  ? 116.452 3.953   12.274  1.000 31.870  ? 48  LEU KKK C   1 
ATOM 16273 O O   . LEU K 2 48  ? 116.304 4.377   13.416  1.000 32.180  ? 48  LEU KKK O   1 
ATOM 16274 C CB  . LEU K 2 48  ? 114.673 3.489   10.544  1.000 31.980  ? 48  LEU KKK CB  1 
ATOM 16275 C CG  . LEU K 2 48  ? 113.635 2.935   11.504  1.000 29.270  ? 48  LEU KKK CG  1 
ATOM 16276 C CD1 . LEU K 2 48  ? 112.639 4.018   11.862  1.000 28.210  ? 48  LEU KKK CD1 1 
ATOM 16277 C CD2 . LEU K 2 48  ? 112.937 1.739   10.889  1.000 29.180  ? 48  LEU KKK CD2 1 
ATOM 16278 N N   . ILE K 2 49  ? 117.304 2.988   11.945  1.000 30.150  ? 49  ILE KKK N   1 
ATOM 16279 C CA  . ILE K 2 49  ? 118.278 2.362   12.882  1.000 31.310  ? 49  ILE KKK CA  1 
ATOM 16280 C C   . ILE K 2 49  ? 119.659 2.464   12.249  1.000 31.440  ? 49  ILE KKK C   1 
ATOM 16281 O O   . ILE K 2 49  ? 119.729 2.267   11.031  1.000 34.510  ? 49  ILE KKK O   1 
ATOM 16282 C CB  . ILE K 2 49  ? 117.902 0.892   13.151  1.000 34.470  ? 49  ILE KKK CB  1 
ATOM 16283 C CG1 . ILE K 2 49  ? 116.540 0.787   13.843  1.000 37.690  ? 49  ILE KKK CG1 1 
ATOM 16284 C CG2 . ILE K 2 49  ? 118.996 0.180   13.946  1.000 33.240  ? 49  ILE KKK CG2 1 
ATOM 16285 C CD1 . ILE K 2 49  ? 116.506 1.370   15.249  1.000 38.420  ? 49  ILE KKK CD1 1 
ATOM 16286 N N   . TYR K 2 50  ? 120.703 2.726   13.049  1.000 29.950  ? 50  TYR KKK N   1 
ATOM 16287 C CA  . TYR K 2 50  ? 122.124 2.636   12.622  1.000 27.950  ? 50  TYR KKK CA  1 
ATOM 16288 C C   . TYR K 2 50  ? 122.898 1.701   13.553  1.000 28.290  ? 50  TYR KKK C   1 
ATOM 16289 O O   . TYR K 2 50  ? 122.468 1.434   14.676  1.000 28.380  ? 50  TYR KKK O   1 
ATOM 16290 C CB  . TYR K 2 50  ? 122.751 4.027   12.559  1.000 27.210  ? 50  TYR KKK CB  1 
ATOM 16291 C CG  . TYR K 2 50  ? 123.060 4.664   13.889  1.000 28.060  ? 50  TYR KKK CG  1 
ATOM 16292 C CD1 . TYR K 2 50  ? 122.083 5.320   14.614  1.000 30.820  ? 50  TYR KKK CD1 1 
ATOM 16293 C CD2 . TYR K 2 50  ? 124.337 4.649   14.408  1.000 28.040  ? 50  TYR KKK CD2 1 
ATOM 16294 C CE1 . TYR K 2 50  ? 122.361 5.930   15.830  1.000 32.120  ? 50  TYR KKK CE1 1 
ATOM 16295 C CE2 . TYR K 2 50  ? 124.632 5.242   15.626  1.000 29.480  ? 50  TYR KKK CE2 1 
ATOM 16296 C CZ  . TYR K 2 50  ? 123.643 5.892   16.347  1.000 30.600  ? 50  TYR KKK CZ  1 
ATOM 16297 O OH  . TYR K 2 50  ? 123.860 6.497   17.557  1.000 28.240  ? 50  TYR KKK OH  1 
ATOM 16298 N N   . ALA K 2 51  ? 124.041 1.215   13.079  1.000 30.110  ? 51  ALA KKK N   1 
ATOM 16299 C CA  . ALA K 2 51  ? 124.976 0.366   13.857  1.000 31.370  ? 51  ALA KKK CA  1 
ATOM 16300 C C   . ALA K 2 51  ? 124.193 -0.787  14.507  1.000 30.370  ? 51  ALA KKK C   1 
ATOM 16301 O O   . ALA K 2 51  ? 124.379 -1.066  15.696  1.000 26.600  ? 51  ALA KKK O   1 
ATOM 16302 C CB  . ALA K 2 51  ? 125.710 1.206   14.879  1.000 31.670  ? 51  ALA KKK CB  1 
ATOM 16303 N N   . ASN K 2 52  ? 123.327 -1.422  13.720  1.000 31.710  ? 52  ASN KKK N   1 
ATOM 16304 C CA  . ASN K 2 52  ? 122.622 -2.691  14.052  1.000 31.210  ? 52  ASN KKK CA  1 
ATOM 16305 C C   . ASN K 2 52  ? 121.412 -2.419  14.965  1.000 31.490  ? 52  ASN KKK C   1 
ATOM 16306 O O   . ASN K 2 52  ? 120.343 -3.023  14.693  1.000 33.900  ? 52  ASN KKK O   1 
ATOM 16307 C CB  . ASN K 2 52  ? 123.562 -3.719  14.667  1.000 29.670  ? 52  ASN KKK CB  1 
ATOM 16308 C CG  . ASN K 2 52  ? 124.792 -3.981  13.825  1.000 33.900  ? 52  ASN KKK CG  1 
ATOM 16309 O OD1 . ASN K 2 52  ? 124.706 -4.491  12.702  1.000 42.460  ? 52  ASN KKK OD1 1 
ATOM 16310 N ND2 . ASN K 2 52  ? 125.959 -3.678  14.369  1.000 33.290  ? 52  ASN KKK ND2 1 
ATOM 16311 N N   . THR K 2 53  ? 121.568 -1.558  15.983  1.000 30.290  ? 53  THR KKK N   1 
ATOM 16312 C CA  . THR K 2 53  ? 120.727 -1.539  17.217  1.000 31.490  ? 53  THR KKK CA  1 
ATOM 16313 C C   . THR K 2 53  ? 120.490 -0.131  17.804  1.000 30.190  ? 53  THR KKK C   1 
ATOM 16314 O O   . THR K 2 53  ? 119.955 -0.068  18.905  1.000 26.310  ? 53  THR KKK O   1 
ATOM 16315 C CB  . THR K 2 53  ? 121.369 -2.391  18.326  1.000 33.210  ? 53  THR KKK CB  1 
ATOM 16316 O OG1 . THR K 2 53  ? 122.720 -2.016  18.619  1.000 35.630  ? 53  THR KKK OG1 1 
ATOM 16317 C CG2 . THR K 2 53  ? 121.377 -3.860  17.985  1.000 32.280  ? 53  THR KKK CG2 1 
ATOM 16318 N N   . GLN K 2 54  ? 120.854 0.957   17.134  1.000 31.470  ? 54  GLN KKK N   1 
ATOM 16319 C CA  . GLN K 2 54  ? 120.840 2.316   17.736  1.000 32.070  ? 54  GLN KKK CA  1 
ATOM 16320 C C   . GLN K 2 54  ? 119.852 3.217   17.014  1.000 34.900  ? 54  GLN KKK C   1 
ATOM 16321 O O   . GLN K 2 54  ? 119.759 3.111   15.784  1.000 38.910  ? 54  GLN KKK O   1 
ATOM 16322 C CB  . GLN K 2 54  ? 122.235 2.917   17.629  1.000 33.270  ? 54  GLN KKK CB  1 
ATOM 16323 C CG  . GLN K 2 54  ? 123.319 2.003   18.176  1.000 33.730  ? 54  GLN KKK CG  1 
ATOM 16324 C CD  . GLN K 2 54  ? 123.171 1.893   19.664  1.000 33.230  ? 54  GLN KKK CD  1 
ATOM 16325 O OE1 . GLN K 2 54  ? 123.154 2.896   20.371  1.000 36.170  ? 54  GLN KKK OE1 1 
ATOM 16326 N NE2 . GLN K 2 54  ? 123.004 0.673   20.134  1.000 34.220  ? 54  GLN KKK NE2 1 
ATOM 16327 N N   . ARG K 2 55  ? 119.157 4.101   17.747  1.000 40.200  ? 55  ARG KKK N   1 
ATOM 16328 C CA  . ARG K 2 55  ? 118.156 5.048   17.203  1.000 42.440  ? 55  ARG KKK CA  1 
ATOM 16329 C C   . ARG K 2 55  ? 118.757 6.442   17.096  1.000 43.960  ? 55  ARG KKK C   1 
ATOM 16330 O O   . ARG K 2 55  ? 119.359 6.934   18.029  1.000 44.440  ? 55  ARG KKK O   1 
ATOM 16331 C CB  . ARG K 2 55  ? 116.918 5.086   18.101  1.000 43.650  ? 55  ARG KKK CB  1 
ATOM 16332 C CG  . ARG K 2 55  ? 116.030 3.865   17.927  1.000 49.290  ? 55  ARG KKK CG  1 
ATOM 16333 C CD  . ARG K 2 55  ? 114.695 3.981   18.658  1.000 53.240  ? 55  ARG KKK CD  1 
ATOM 16334 N NE  . ARG K 2 55  ? 114.850 4.447   20.024  1.000 56.390  ? 55  ARG KKK NE  1 
ATOM 16335 C CZ  . ARG K 2 55  ? 115.179 3.693   21.065  1.000 58.270  ? 55  ARG KKK CZ  1 
ATOM 16336 N NH1 . ARG K 2 55  ? 115.371 2.390   20.931  1.000 58.850  ? 55  ARG KKK NH1 1 
ATOM 16337 N NH2 . ARG K 2 55  ? 115.291 4.266   22.249  1.000 61.030  ? 55  ARG KKK NH2 1 
ATOM 16338 N N   . PRO K 2 56  ? 118.593 7.138   15.959  1.000 48.350  ? 56  PRO KKK N   1 
ATOM 16339 C CA  . PRO K 2 56  ? 118.931 8.557   15.904  1.000 51.220  ? 56  PRO KKK CA  1 
ATOM 16340 C C   . PRO K 2 56  ? 117.839 9.303   16.674  1.000 52.290  ? 56  PRO KKK C   1 
ATOM 16341 O O   . PRO K 2 56  ? 116.788 8.715   16.871  1.000 56.940  ? 56  PRO KKK O   1 
ATOM 16342 C CB  . PRO K 2 56  ? 118.951 8.853   14.399  1.000 52.300  ? 56  PRO KKK CB  1 
ATOM 16343 C CG  . PRO K 2 56  ? 118.007 7.833   13.786  1.000 49.720  ? 56  PRO KKK CG  1 
ATOM 16344 C CD  . PRO K 2 56  ? 118.073 6.615   14.690  1.000 47.590  ? 56  PRO KKK CD  1 
ATOM 16345 N N   . SER K 2 57  ? 118.082 10.548  17.085  1.000 55.590  ? 57  SER KKK N   1 
ATOM 16346 C CA  . SER K 2 57  ? 117.015 11.415  17.673  1.000 62.260  ? 57  SER KKK CA  1 
ATOM 16347 C C   . SER K 2 57  ? 115.867 11.532  16.668  1.000 63.020  ? 57  SER KKK C   1 
ATOM 16348 O O   . SER K 2 57  ? 116.140 11.760  15.477  1.000 66.910  ? 57  SER KKK O   1 
ATOM 16349 C CB  . SER K 2 57  ? 117.547 12.769  18.093  1.000 55.850  ? 57  SER KKK CB  1 
ATOM 16350 N N   . GLY K 2 58  ? 114.627 11.324  17.125  1.000 59.170  ? 58  GLY KKK N   1 
ATOM 16351 C CA  . GLY K 2 58  ? 113.414 11.465  16.302  1.000 58.140  ? 58  GLY KKK CA  1 
ATOM 16352 C C   . GLY K 2 58  ? 112.701 10.141  16.130  1.000 61.530  ? 58  GLY KKK C   1 
ATOM 16353 O O   . GLY K 2 58  ? 111.519 10.150  15.709  1.000 64.680  ? 58  GLY KKK O   1 
ATOM 16354 N N   . VAL K 2 59  ? 113.394 9.032   16.400  1.000 65.410  ? 59  VAL KKK N   1 
ATOM 16355 C CA  . VAL K 2 59  ? 112.837 7.659   16.219  1.000 64.510  ? 59  VAL KKK CA  1 
ATOM 16356 C C   . VAL K 2 59  ? 112.299 7.182   17.567  1.000 71.040  ? 59  VAL KKK C   1 
ATOM 16357 O O   . VAL K 2 59  ? 113.051 7.073   18.531  1.000 72.200  ? 59  VAL KKK O   1 
ATOM 16358 C CB  . VAL K 2 59  ? 113.862 6.685   15.609  1.000 54.900  ? 59  VAL KKK CB  1 
ATOM 16359 C CG1 . VAL K 2 59  ? 113.282 5.297   15.423  1.000 55.730  ? 59  VAL KKK CG1 1 
ATOM 16360 C CG2 . VAL K 2 59  ? 114.375 7.196   14.282  1.000 56.670  ? 59  VAL KKK CG2 1 
ATOM 16361 N N   . PRO K 2 60  ? 110.983 6.902   17.663  1.000 75.410  ? 60  PRO KKK N   1 
ATOM 16362 C CA  . PRO K 2 60  ? 110.390 6.336   18.876  1.000 75.450  ? 60  PRO KKK CA  1 
ATOM 16363 C C   . PRO K 2 60  ? 111.089 5.103   19.479  1.000 79.360  ? 60  PRO KKK C   1 
ATOM 16364 O O   . PRO K 2 60  ? 111.619 4.290   18.740  1.000 77.180  ? 60  PRO KKK O   1 
ATOM 16365 C CB  . PRO K 2 60  ? 108.993 5.899   18.395  1.000 79.390  ? 60  PRO KKK CB  1 
ATOM 16366 C CG  . PRO K 2 60  ? 108.665 6.836   17.244  1.000 76.360  ? 60  PRO KKK CG  1 
ATOM 16367 C CD  . PRO K 2 60  ? 110.007 7.141   16.598  1.000 74.560  ? 60  PRO KKK CD  1 
ATOM 16368 N N   . ASP K 2 61  ? 111.001 4.976   20.810  1.000 76.890  ? 61  ASP KKK N   1 
ATOM 16369 C CA  . ASP K 2 61  ? 111.400 3.789   21.613  1.000 72.740  ? 61  ASP KKK CA  1 
ATOM 16370 C C   . ASP K 2 61  ? 110.918 2.466   20.995  1.000 59.990  ? 61  ASP KKK C   1 
ATOM 16371 O O   . ASP K 2 61  ? 111.590 1.451   21.196  1.000 45.170  ? 61  ASP KKK O   1 
ATOM 16372 C CB  . ASP K 2 61  ? 110.772 3.901   22.997  1.000 77.840  ? 61  ASP KKK CB  1 
ATOM 16373 C CG  . ASP K 2 61  ? 111.508 3.141   24.083  1.000 85.840  ? 61  ASP KKK CG  1 
ATOM 16374 O OD1 . ASP K 2 61  ? 112.693 2.803   23.891  1.000 85.650  ? 61  ASP KKK OD1 1 
ATOM 16375 O OD2 . ASP K 2 61  ? 110.887 2.894   25.128  1.000 90.690  ? 61  ASP KKK OD2 1 
ATOM 16376 N N   . ARG K 2 62  ? 109.762 2.484   20.329  1.000 59.310  ? 62  ARG KKK N   1 
ATOM 16377 C CA  . ARG K 2 62  ? 109.077 1.293   19.751  1.000 62.270  ? 62  ARG KKK CA  1 
ATOM 16378 C C   . ARG K 2 62  ? 110.036 0.534   18.828  1.000 65.640  ? 62  ARG KKK C   1 
ATOM 16379 O O   . ARG K 2 62  ? 110.124 -0.723  18.937  1.000 67.240  ? 62  ARG KKK O   1 
ATOM 16380 C CB  . ARG K 2 62  ? 107.842 1.719   18.952  1.000 64.920  ? 62  ARG KKK CB  1 
ATOM 16381 C CG  . ARG K 2 62  ? 106.988 2.783   19.628  1.000 70.540  ? 62  ARG KKK CG  1 
ATOM 16382 C CD  . ARG K 2 62  ? 105.669 3.049   18.914  1.000 73.890  ? 62  ARG KKK CD  1 
ATOM 16383 N NE  . ARG K 2 62  ? 105.684 2.762   17.477  1.000 71.910  ? 62  ARG KKK NE  1 
ATOM 16384 C CZ  . ARG K 2 62  ? 105.466 3.640   16.505  1.000 64.410  ? 62  ARG KKK CZ  1 
ATOM 16385 N NH1 . ARG K 2 62  ? 105.244 4.919   16.766  1.000 69.460  ? 62  ARG KKK NH1 1 
ATOM 16386 N NH2 . ARG K 2 62  ? 105.489 3.233   15.255  1.000 56.020  ? 62  ARG KKK NH2 1 
ATOM 16387 N N   . PHE K 2 63  ? 110.731 1.283   17.961  1.000 63.420  ? 63  PHE KKK N   1 
ATOM 16388 C CA  . PHE K 2 63  ? 111.742 0.764   16.990  1.000 57.440  ? 63  PHE KKK CA  1 
ATOM 16389 C C   . PHE K 2 63  ? 113.000 0.316   17.725  1.000 56.200  ? 63  PHE KKK C   1 
ATOM 16390 O O   . PHE K 2 63  ? 113.587 1.089   18.519  1.000 52.700  ? 63  PHE KKK O   1 
ATOM 16391 C CB  . PHE K 2 63  ? 112.055 1.836   15.954  1.000 53.630  ? 63  PHE KKK CB  1 
ATOM 16392 C CG  . PHE K 2 63  ? 110.889 2.206   15.076  1.000 49.350  ? 63  PHE KKK CG  1 
ATOM 16393 C CD1 . PHE K 2 63  ? 110.571 1.439   13.962  1.000 44.050  ? 63  PHE KKK CD1 1 
ATOM 16394 C CD2 . PHE K 2 63  ? 110.128 3.331   15.347  1.000 46.280  ? 63  PHE KKK CD2 1 
ATOM 16395 C CE1 . PHE K 2 63  ? 109.502 1.781   13.144  1.000 42.040  ? 63  PHE KKK CE1 1 
ATOM 16396 C CE2 . PHE K 2 63  ? 109.073 3.675   14.514  1.000 46.990  ? 63  PHE KKK CE2 1 
ATOM 16397 C CZ  . PHE K 2 63  ? 108.750 2.895   13.419  1.000 43.620  ? 63  PHE KKK CZ  1 
ATOM 16398 N N   . SER K 2 64  ? 113.417 -0.918  17.457  1.000 49.240  ? 64  SER KKK N   1 
ATOM 16399 C CA  . SER K 2 64  ? 114.615 -1.535  18.066  1.000 47.090  ? 64  SER KKK CA  1 
ATOM 16400 C C   . SER K 2 64  ? 115.250 -2.522  17.076  1.000 48.460  ? 64  SER KKK C   1 
ATOM 16401 O O   . SER K 2 64  ? 114.579 -2.920  16.094  1.000 47.770  ? 64  SER KKK O   1 
ATOM 16402 C CB  . SER K 2 64  ? 114.225 -2.222  19.308  1.000 47.520  ? 64  SER KKK CB  1 
ATOM 16403 O OG  . SER K 2 64  ? 113.711 -3.516  18.994  1.000 57.480  ? 64  SER KKK OG  1 
ATOM 16404 N N   . GLY K 2 65  ? 116.487 -2.929  17.337  1.000 49.880  ? 65  GLY KKK N   1 
ATOM 16405 C CA  . GLY K 2 65  ? 117.172 -3.966  16.537  1.000 52.050  ? 65  GLY KKK CA  1 
ATOM 16406 C C   . GLY K 2 65  ? 117.836 -5.000  17.409  1.000 49.860  ? 65  GLY KKK C   1 
ATOM 16407 O O   . GLY K 2 65  ? 118.008 -4.747  18.618  1.000 47.090  ? 65  GLY KKK O   1 
ATOM 16408 N N   . SER K 2 66  ? 118.240 -6.111  16.799  1.000 48.140  ? 66  SER KKK N   1 
ATOM 16409 C CA  . SER K 2 66  ? 119.106 -7.141  17.396  1.000 45.850  ? 66  SER KKK CA  1 
ATOM 16410 C C   . SER K 2 66  ? 120.076 -7.627  16.309  1.000 43.830  ? 66  SER KKK C   1 
ATOM 16411 O O   . SER K 2 66  ? 119.650 -7.719  15.128  1.000 38.430  ? 66  SER KKK O   1 
ATOM 16412 C CB  . SER K 2 66  ? 118.296 -8.286  17.960  1.000 51.680  ? 66  SER KKK CB  1 
ATOM 16413 O OG  . SER K 2 66  ? 117.968 -9.236  16.949  1.000 57.900  ? 66  SER KKK OG  1 
ATOM 16414 N N   . LYS K 2 67  ? 121.321 -7.922  16.696  1.000 45.680  ? 67  LYS KKK N   1 
ATOM 16415 C CA  . LYS K 2 67  ? 122.354 -8.569  15.841  1.000 44.100  ? 67  LYS KKK CA  1 
ATOM 16416 C C   . LYS K 2 67  ? 122.681 -9.924  16.467  1.000 44.720  ? 67  LYS KKK C   1 
ATOM 16417 O O   . LYS K 2 67  ? 122.929 -9.978  17.674  1.000 44.560  ? 67  LYS KKK O   1 
ATOM 16418 C CB  . LYS K 2 67  ? 123.621 -7.705  15.746  1.000 39.500  ? 67  LYS KKK CB  1 
ATOM 16419 C CG  . LYS K 2 67  ? 124.717 -8.232  14.835  1.000 36.190  ? 67  LYS KKK CG  1 
ATOM 16420 C CD  . LYS K 2 67  ? 126.060 -7.557  15.027  1.000 36.670  ? 67  LYS KKK CD  1 
ATOM 16421 C CE  . LYS K 2 67  ? 126.880 -7.492  13.745  1.000 43.160  ? 67  LYS KKK CE  1 
ATOM 16422 N NZ  . LYS K 2 67  ? 127.344 -8.835  13.291  1.000 39.590  ? 67  LYS KKK NZ  1 
ATOM 16423 N N   . SER K 2 68  ? 122.671 -10.981 15.669  1.000 46.910  ? 68  SER KKK N   1 
ATOM 16424 C CA  . SER K 2 68  ? 123.277 -12.287 16.019  1.000 48.310  ? 68  SER KKK CA  1 
ATOM 16425 C C   . SER K 2 68  ? 124.163 -12.734 14.850  1.000 44.080  ? 68  SER KKK C   1 
ATOM 16426 O O   . SER K 2 68  ? 123.608 -13.171 13.848  1.000 41.500  ? 68  SER KKK O   1 
ATOM 16427 C CB  . SER K 2 68  ? 122.199 -13.274 16.354  1.000 51.550  ? 68  SER KKK CB  1 
ATOM 16428 O OG  . SER K 2 68  ? 122.756 -14.436 16.936  1.000 60.040  ? 68  SER KKK OG  1 
ATOM 16429 N N   . GLY K 2 69  ? 125.481 -12.560 14.972  1.000 45.210  ? 69  GLY KKK N   1 
ATOM 16430 C CA  . GLY K 2 69  ? 126.476 -12.865 13.923  1.000 52.630  ? 69  GLY KKK CA  1 
ATOM 16431 C C   . GLY K 2 69  ? 126.064 -12.277 12.580  1.000 58.350  ? 69  GLY KKK C   1 
ATOM 16432 O O   . GLY K 2 69  ? 125.818 -11.037 12.523  1.000 57.790  ? 69  GLY KKK O   1 
ATOM 16433 N N   . THR K 2 70  ? 125.923 -13.125 11.551  1.000 54.460  ? 70  THR KKK N   1 
ATOM 16434 C CA  . THR K 2 70  ? 125.727 -12.686 10.137  1.000 50.150  ? 70  THR KKK CA  1 
ATOM 16435 C C   . THR K 2 70  ? 124.272 -12.267 9.855   1.000 43.860  ? 70  THR KKK C   1 
ATOM 16436 O O   . THR K 2 70  ? 123.977 -11.887 8.713   1.000 37.900  ? 70  THR KKK O   1 
ATOM 16437 C CB  . THR K 2 70  ? 126.223 -13.752 9.157   1.000 56.330  ? 70  THR KKK CB  1 
ATOM 16438 O OG1 . THR K 2 70  ? 125.294 -14.831 9.160   1.000 60.570  ? 70  THR KKK OG1 1 
ATOM 16439 C CG2 . THR K 2 70  ? 127.619 -14.234 9.481   1.000 64.140  ? 70  THR KKK CG2 1 
ATOM 16440 N N   . SER K 2 71  ? 123.381 -12.314 10.838  1.000 48.650  ? 71  SER KKK N   1 
ATOM 16441 C CA  . SER K 2 71  ? 121.956 -11.909 10.682  1.000 48.450  ? 71  SER KKK CA  1 
ATOM 16442 C C   . SER K 2 71  ? 121.627 -10.812 11.688  1.000 45.970  ? 71  SER KKK C   1 
ATOM 16443 O O   . SER K 2 71  ? 122.159 -10.843 12.810  1.000 47.450  ? 71  SER KKK O   1 
ATOM 16444 C CB  . SER K 2 71  ? 120.997 -13.058 10.839  1.000 49.650  ? 71  SER KKK CB  1 
ATOM 16445 O OG  . SER K 2 71  ? 121.346 -14.135 9.981   1.000 60.130  ? 71  SER KKK OG  1 
ATOM 16446 N N   . VAL K 2 72  ? 120.781 -9.883  11.261  1.000 42.780  ? 72  VAL KKK N   1 
ATOM 16447 C CA  . VAL K 2 72  ? 120.244 -8.750  12.062  1.000 43.130  ? 72  VAL KKK CA  1 
ATOM 16448 C C   . VAL K 2 72  ? 118.734 -8.769  11.885  1.000 40.810  ? 72  VAL KKK C   1 
ATOM 16449 O O   . VAL K 2 72  ? 118.288 -9.251  10.837  1.000 42.150  ? 72  VAL KKK O   1 
ATOM 16450 C CB  . VAL K 2 72  ? 120.846 -7.415  11.593  1.000 46.470  ? 72  VAL KKK CB  1 
ATOM 16451 C CG1 . VAL K 2 72  ? 120.023 -6.213  12.050  1.000 50.760  ? 72  VAL KKK CG1 1 
ATOM 16452 C CG2 . VAL K 2 72  ? 122.287 -7.289  12.056  1.000 48.700  ? 72  VAL KKK CG2 1 
ATOM 16453 N N   . SER K 2 73  ? 117.991 -8.268  12.866  1.000 41.680  ? 73  SER KKK N   1 
ATOM 16454 C CA  . SER K 2 73  ? 116.536 -8.018  12.728  1.000 44.890  ? 73  SER KKK CA  1 
ATOM 16455 C C   . SER K 2 73  ? 116.198 -6.592  13.181  1.000 42.690  ? 73  SER KKK C   1 
ATOM 16456 O O   . SER K 2 73  ? 116.978 -5.993  13.985  1.000 41.380  ? 73  SER KKK O   1 
ATOM 16457 C CB  . SER K 2 73  ? 115.760 -9.046  13.483  1.000 52.520  ? 73  SER KKK CB  1 
ATOM 16458 O OG  . SER K 2 73  ? 116.059 -8.963  14.873  1.000 60.320  ? 73  SER KKK OG  1 
ATOM 16459 N N   . LEU K 2 74  ? 115.122 -6.054  12.602  1.000 38.890  ? 74  LEU KKK N   1 
ATOM 16460 C CA  . LEU K 2 74  ? 114.454 -4.798  13.020  1.000 40.660  ? 74  LEU KKK CA  1 
ATOM 16461 C C   . LEU K 2 74  ? 113.153 -5.199  13.705  1.000 42.330  ? 74  LEU KKK C   1 
ATOM 16462 O O   . LEU K 2 74  ? 112.467 -6.083  13.167  1.000 41.700  ? 74  LEU KKK O   1 
ATOM 16463 C CB  . LEU K 2 74  ? 114.184 -3.935  11.782  1.000 41.060  ? 74  LEU KKK CB  1 
ATOM 16464 C CG  . LEU K 2 74  ? 113.233 -2.758  12.005  1.000 42.900  ? 74  LEU KKK CG  1 
ATOM 16465 C CD1 . LEU K 2 74  ? 113.816 -1.757  12.989  1.000 43.630  ? 74  LEU KKK CD1 1 
ATOM 16466 C CD2 . LEU K 2 74  ? 112.898 -2.067  10.690  1.000 42.800  ? 74  LEU KKK CD2 1 
ATOM 16467 N N   . ALA K 2 75  ? 112.837 -4.569  14.836  1.000 47.680  ? 75  ALA KKK N   1 
ATOM 16468 C CA  . ALA K 2 75  ? 111.643 -4.868  15.663  1.000 51.290  ? 75  ALA KKK CA  1 
ATOM 16469 C C   . ALA K 2 75  ? 110.800 -3.601  15.810  1.000 52.390  ? 75  ALA KKK C   1 
ATOM 16470 O O   . ALA K 2 75  ? 111.214 -2.672  16.572  1.000 56.570  ? 75  ALA KKK O   1 
ATOM 16471 C CB  . ALA K 2 75  ? 112.051 -5.406  17.010  1.000 52.470  ? 75  ALA KKK CB  1 
ATOM 16472 N N   . ILE K 2 76  ? 109.668 -3.562  15.105  1.000 48.590  ? 76  ILE KKK N   1 
ATOM 16473 C CA  . ILE K 2 76  ? 108.657 -2.477  15.236  1.000 47.440  ? 76  ILE KKK CA  1 
ATOM 16474 C C   . ILE K 2 76  ? 107.608 -2.948  16.235  1.000 48.060  ? 76  ILE KKK C   1 
ATOM 16475 O O   . ILE K 2 76  ? 106.801 -3.798  15.850  1.000 55.260  ? 76  ILE KKK O   1 
ATOM 16476 C CB  . ILE K 2 76  ? 108.027 -2.128  13.876  1.000 44.430  ? 76  ILE KKK CB  1 
ATOM 16477 C CG1 . ILE K 2 76  ? 109.101 -1.909  12.802  1.000 42.980  ? 76  ILE KKK CG1 1 
ATOM 16478 C CG2 . ILE K 2 76  ? 107.092 -0.931  14.018  1.000 41.820  ? 76  ILE KKK CG2 1 
ATOM 16479 C CD1 . ILE K 2 76  ? 108.554 -1.728  11.403  1.000 42.870  ? 76  ILE KKK CD1 1 
ATOM 16480 N N   . SER K 2 77  ? 107.627 -2.444  17.472  1.000 51.650  ? 77  SER KKK N   1 
ATOM 16481 C CA  . SER K 2 77  ? 106.614 -2.762  18.511  1.000 57.040  ? 77  SER KKK CA  1 
ATOM 16482 C C   . SER K 2 77  ? 105.566 -1.650  18.508  1.000 60.210  ? 77  SER KKK C   1 
ATOM 16483 O O   . SER K 2 77  ? 105.853 -0.574  17.935  1.000 72.140  ? 77  SER KKK O   1 
ATOM 16484 C CB  . SER K 2 77  ? 107.239 -2.950  19.871  1.000 61.220  ? 77  SER KKK CB  1 
ATOM 16485 O OG  . SER K 2 77  ? 107.672 -1.712  20.411  1.000 69.530  ? 77  SER KKK OG  1 
ATOM 16486 N N   . GLY K 2 78  ? 104.403 -1.903  19.105  1.000 59.460  ? 78  GLY KKK N   1 
ATOM 16487 C CA  . GLY K 2 78  ? 103.288 -0.940  19.153  1.000 64.160  ? 78  GLY KKK CA  1 
ATOM 16488 C C   . GLY K 2 78  ? 102.943 -0.457  17.759  1.000 61.500  ? 78  GLY KKK C   1 
ATOM 16489 O O   . GLY K 2 78  ? 102.907 0.762   17.544  1.000 60.750  ? 78  GLY KKK O   1 
ATOM 16490 N N   . LEU K 2 79  ? 102.729 -1.398  16.843  1.000 56.940  ? 79  LEU KKK N   1 
ATOM 16491 C CA  . LEU K 2 79  ? 102.547 -1.111  15.405  1.000 56.970  ? 79  LEU KKK CA  1 
ATOM 16492 C C   . LEU K 2 79  ? 101.419 -0.096  15.204  1.000 54.670  ? 79  LEU KKK C   1 
ATOM 16493 O O   . LEU K 2 79  ? 100.385 -0.224  15.865  1.000 61.990  ? 79  LEU KKK O   1 
ATOM 16494 C CB  . LEU K 2 79  ? 102.246 -2.414  14.672  1.000 60.480  ? 79  LEU KKK CB  1 
ATOM 16495 C CG  . LEU K 2 79  ? 102.225 -2.284  13.151  1.000 75.360  ? 79  LEU KKK CG  1 
ATOM 16496 C CD1 . LEU K 2 79  ? 103.601 -1.939  12.593  1.000 80.450  ? 79  LEU KKK CD1 1 
ATOM 16497 C CD2 . LEU K 2 79  ? 101.724 -3.553  12.514  1.000 79.740  ? 79  LEU KKK CD2 1 
ATOM 16498 N N   . GLN K 2 80  ? 101.627 0.888   14.328  1.000 60.930  ? 80  GLN KKK N   1 
ATOM 16499 C CA  . GLN K 2 80  ? 100.616 1.921   13.975  1.000 69.440  ? 80  GLN KKK CA  1 
ATOM 16500 C C   . GLN K 2 80  ? 100.488 1.988   12.453  1.000 76.340  ? 80  GLN KKK C   1 
ATOM 16501 O O   . GLN K 2 80  ? 101.367 1.419   11.775  1.000 90.060  ? 80  GLN KKK O   1 
ATOM 16502 C CB  . GLN K 2 80  ? 101.005 3.277   14.553  1.000 68.750  ? 80  GLN KKK CB  1 
ATOM 16503 C CG  . GLN K 2 80  ? 101.094 3.280   16.070  1.000 72.850  ? 80  GLN KKK CG  1 
ATOM 16504 C CD  . GLN K 2 80  ? 101.499 4.628   16.605  1.000 81.970  ? 80  GLN KKK CD  1 
ATOM 16505 O OE1 . GLN K 2 80  ? 101.455 5.636   15.902  1.000 98.950  ? 80  GLN KKK OE1 1 
ATOM 16506 N NE2 . GLN K 2 80  ? 101.870 4.661   17.871  1.000 97.730  ? 80  GLN KKK NE2 1 
ATOM 16507 N N   . SER K 2 81  ? 99.432  2.630   11.941  1.000 77.440  ? 81  SER KKK N   1 
ATOM 16508 C CA  . SER K 2 81  ? 99.155  2.723   10.481  1.000 78.950  ? 81  SER KKK CA  1 
ATOM 16509 C C   . SER K 2 81  ? 100.183 3.654   9.837   1.000 82.140  ? 81  SER KKK C   1 
ATOM 16510 O O   . SER K 2 81  ? 100.536 3.417   8.675   1.000 78.850  ? 81  SER KKK O   1 
ATOM 16511 C CB  . SER K 2 81  ? 97.737  3.135   10.178  1.000 81.210  ? 81  SER KKK CB  1 
ATOM 16512 O OG  . SER K 2 81  ? 97.441  4.411   10.707  1.000 85.740  ? 81  SER KKK OG  1 
ATOM 16513 N N   . GLU K 2 82  ? 100.670 4.640   10.603  1.000 80.270  ? 82  GLU KKK N   1 
ATOM 16514 C CA  . GLU K 2 82  ? 101.713 5.625   10.203  1.000 69.280  ? 82  GLU KKK CA  1 
ATOM 16515 C C   . GLU K 2 82  ? 103.039 4.898   9.881   1.000 66.600  ? 82  GLU KKK C   1 
ATOM 16516 O O   . GLU K 2 82  ? 103.934 5.553   9.309   1.000 66.250  ? 82  GLU KKK O   1 
ATOM 16517 C CB  . GLU K 2 82  ? 101.853 6.679   11.309  1.000 55.400  ? 82  GLU KKK CB  1 
ATOM 16518 N N   . ASP K 2 83  ? 103.154 3.606   10.220  1.000 59.100  ? 83  ASP KKK N   1 
ATOM 16519 C CA  . ASP K 2 83  ? 104.352 2.748   10.003  1.000 57.980  ? 83  ASP KKK CA  1 
ATOM 16520 C C   . ASP K 2 83  ? 104.274 2.020   8.658   1.000 57.620  ? 83  ASP KKK C   1 
ATOM 16521 O O   . ASP K 2 83  ? 105.196 1.222   8.357   1.000 57.810  ? 83  ASP KKK O   1 
ATOM 16522 C CB  . ASP K 2 83  ? 104.506 1.713   11.127  1.000 60.170  ? 83  ASP KKK CB  1 
ATOM 16523 C CG  . ASP K 2 83  ? 104.882 2.322   12.467  1.000 66.090  ? 83  ASP KKK CG  1 
ATOM 16524 O OD1 . ASP K 2 83  ? 105.314 3.494   12.463  1.000 71.140  ? 83  ASP KKK OD1 1 
ATOM 16525 O OD2 . ASP K 2 83  ? 104.755 1.625   13.505  1.000 72.830  ? 83  ASP KKK OD2 1 
ATOM 16526 N N   . GLU K 2 84  ? 103.204 2.231   7.892   1.000 61.620  ? 84  GLU KKK N   1 
ATOM 16527 C CA  . GLU K 2 84  ? 103.025 1.560   6.577   1.000 69.480  ? 84  GLU KKK CA  1 
ATOM 16528 C C   . GLU K 2 84  ? 104.021 2.207   5.615   1.000 65.880  ? 84  GLU KKK C   1 
ATOM 16529 O O   . GLU K 2 84  ? 104.017 3.450   5.503   1.000 75.480  ? 84  GLU KKK O   1 
ATOM 16530 C CB  . GLU K 2 84  ? 101.570 1.660   6.094   1.000 80.200  ? 84  GLU KKK CB  1 
ATOM 16531 C CG  . GLU K 2 84  ? 101.073 0.420   5.376   1.000 83.780  ? 84  GLU KKK CG  1 
ATOM 16532 C CD  . GLU K 2 84  ? 99.564  0.227   5.328   1.000 86.730  ? 84  GLU KKK CD  1 
ATOM 16533 O OE1 . GLU K 2 84  ? 98.819  0.925   6.061   1.000 82.910  ? 84  GLU KKK OE1 1 
ATOM 16534 O OE2 . GLU K 2 84  ? 99.127  -0.661  4.574   1.000 86.820  ? 84  GLU KKK OE2 1 
ATOM 16535 N N   . GLY K 2 85  ? 104.881 1.393   4.992   1.000 59.440  ? 85  GLY KKK N   1 
ATOM 16536 C CA  . GLY K 2 85  ? 105.975 1.846   4.112   1.000 57.990  ? 85  GLY KKK CA  1 
ATOM 16537 C C   . GLY K 2 85  ? 106.963 0.727   3.837   1.000 57.610  ? 85  GLY KKK C   1 
ATOM 16538 O O   . GLY K 2 85  ? 106.674 -0.419  4.242   1.000 58.830  ? 85  GLY KKK O   1 
ATOM 16539 N N   . ASP K 2 86  ? 108.060 1.042   3.142   1.000 58.040  ? 86  ASP KKK N   1 
ATOM 16540 C CA  . ASP K 2 86  ? 109.158 0.102   2.794   1.000 53.730  ? 86  ASP KKK CA  1 
ATOM 16541 C C   . ASP K 2 86  ? 110.304 0.275   3.814   1.000 49.880  ? 86  ASP KKK C   1 
ATOM 16542 O O   . ASP K 2 86  ? 110.627 1.432   4.180   1.000 46.030  ? 86  ASP KKK O   1 
ATOM 16543 C CB  . ASP K 2 86  ? 109.583 0.312   1.332   1.000 56.470  ? 86  ASP KKK CB  1 
ATOM 16544 C CG  . ASP K 2 86  ? 108.627 -0.306  0.307   1.000 56.430  ? 86  ASP KKK CG  1 
ATOM 16545 O OD1 . ASP K 2 86  ? 107.470 -0.571  0.634   1.000 56.080  ? 86  ASP KKK OD1 1 
ATOM 16546 O OD2 . ASP K 2 86  ? 109.069 -0.569  -0.825  1.000 63.140  ? 86  ASP KKK OD2 1 
ATOM 16547 N N   . TYR K 2 87  ? 110.883 -0.835  4.280   1.000 43.330  ? 87  TYR KKK N   1 
ATOM 16548 C CA  . TYR K 2 87  ? 112.015 -0.871  5.243   1.000 38.520  ? 87  TYR KKK CA  1 
ATOM 16549 C C   . TYR K 2 87  ? 113.222 -1.485  4.525   1.000 39.860  ? 87  TYR KKK C   1 
ATOM 16550 O O   . TYR K 2 87  ? 113.172 -2.656  4.112   1.000 36.300  ? 87  TYR KKK O   1 
ATOM 16551 C CB  . TYR K 2 87  ? 111.577 -1.582  6.533   1.000 34.410  ? 87  TYR KKK CB  1 
ATOM 16552 C CG  . TYR K 2 87  ? 110.582 -0.765  7.311   1.000 33.280  ? 87  TYR KKK CG  1 
ATOM 16553 C CD1 . TYR K 2 87  ? 109.263 -0.698  6.906   1.000 33.480  ? 87  TYR KKK CD1 1 
ATOM 16554 C CD2 . TYR K 2 87  ? 110.962 0.019   8.383   1.000 34.550  ? 87  TYR KKK CD2 1 
ATOM 16555 C CE1 . TYR K 2 87  ? 108.331 0.090   7.560   1.000 33.220  ? 87  TYR KKK CE1 1 
ATOM 16556 C CE2 . TYR K 2 87  ? 110.047 0.821   9.047   1.000 36.090  ? 87  TYR KKK CE2 1 
ATOM 16557 C CZ  . TYR K 2 87  ? 108.722 0.850   8.639   1.000 35.460  ? 87  TYR KKK CZ  1 
ATOM 16558 O OH  . TYR K 2 87  ? 107.794 1.621   9.275   1.000 40.150  ? 87  TYR KKK OH  1 
ATOM 16559 N N   . HIS K 2 88  ? 114.304 -0.710  4.430   1.000 41.650  ? 88  HIS KKK N   1 
ATOM 16560 C CA  . HIS K 2 88  ? 115.505 -1.152  3.677   1.000 41.750  ? 88  HIS KKK CA  1 
ATOM 16561 C C   . HIS K 2 88  ? 116.686 -1.477  4.583   1.000 38.370  ? 88  HIS KKK C   1 
ATOM 16562 O O   . HIS K 2 88  ? 116.930 -0.721  5.512   1.000 36.100  ? 88  HIS KKK O   1 
ATOM 16563 C CB  . HIS K 2 88  ? 115.877 -0.106  2.626   1.000 41.650  ? 88  HIS KKK CB  1 
ATOM 16564 C CG  . HIS K 2 88  ? 114.824 0.124   1.599   1.000 41.200  ? 88  HIS KKK CG  1 
ATOM 16565 N ND1 . HIS K 2 88  ? 114.689 -0.684  0.493   1.000 40.620  ? 88  HIS KKK ND1 1 
ATOM 16566 C CD2 . HIS K 2 88  ? 113.868 1.069   1.500   1.000 39.900  ? 88  HIS KKK CD2 1 
ATOM 16567 C CE1 . HIS K 2 88  ? 113.688 -0.251  -0.242  1.000 44.640  ? 88  HIS KKK CE1 1 
ATOM 16568 N NE2 . HIS K 2 88  ? 113.170 0.820   0.355   1.000 39.940  ? 88  HIS KKK NE2 1 
ATOM 16569 N N   . CYS K 2 89  ? 117.394 -2.557  4.278   1.000 36.000  ? 89  CYS KKK N   1 
ATOM 16570 C CA  . CYS K 2 89  ? 118.547 -3.003  5.085   1.000 39.530  ? 89  CYS KKK CA  1 
ATOM 16571 C C   . CYS K 2 89  ? 119.813 -2.709  4.304   1.000 35.930  ? 89  CYS KKK C   1 
ATOM 16572 O O   . CYS K 2 89  ? 119.797 -2.922  3.101   1.000 31.190  ? 89  CYS KKK O   1 
ATOM 16573 C CB  . CYS K 2 89  ? 118.384 -4.496  5.332   1.000 44.310  ? 89  CYS KKK CB  1 
ATOM 16574 S SG  . CYS K 2 89  ? 119.586 -5.320  6.385   1.000 49.810  ? 89  CYS KKK SG  1 
ATOM 16575 N N   . ALA K 2 90  ? 120.843 -2.207  4.974   1.000 36.440  ? 90  ALA KKK N   1 
ATOM 16576 C CA  . ALA K 2 90  ? 122.057 -1.794  4.254   1.000 36.500  ? 90  ALA KKK CA  1 
ATOM 16577 C C   . ALA K 2 90  ? 123.300 -2.077  5.069   1.000 31.530  ? 90  ALA KKK C   1 
ATOM 16578 O O   . ALA K 2 90  ? 123.274 -1.790  6.256   1.000 27.560  ? 90  ALA KKK O   1 
ATOM 16579 C CB  . ALA K 2 90  ? 122.007 -0.339  3.951   1.000 39.380  ? 90  ALA KKK CB  1 
ATOM 16580 N N   . ALA K 2 91  ? 124.346 -2.535  4.400   1.000 30.300  ? 91  ALA KKK N   1 
ATOM 16581 C CA  . ALA K 2 91  ? 125.628 -2.833  5.066   1.000 32.340  ? 91  ALA KKK CA  1 
ATOM 16582 C C   . ALA K 2 91  ? 126.747 -2.873  4.029   1.000 33.150  ? 91  ALA KKK C   1 
ATOM 16583 O O   . ALA K 2 91  ? 126.478 -3.321  2.905   1.000 31.810  ? 91  ALA KKK O   1 
ATOM 16584 C CB  . ALA K 2 91  ? 125.521 -4.139  5.797   1.000 33.220  ? 91  ALA KKK CB  1 
ATOM 16585 N N   . TRP K 2 92  ? 127.956 -2.441  4.403   1.000 33.230  ? 92  TRP KKK N   1 
ATOM 16586 C CA  . TRP K 2 92  ? 129.141 -2.500  3.510   1.000 32.620  ? 92  TRP KKK CA  1 
ATOM 16587 C C   . TRP K 2 92  ? 129.564 -3.957  3.306   1.000 34.750  ? 92  TRP KKK C   1 
ATOM 16588 O O   . TRP K 2 92  ? 129.479 -4.732  4.266   1.000 40.680  ? 92  TRP KKK O   1 
ATOM 16589 C CB  . TRP K 2 92  ? 130.290 -1.705  4.102   1.000 33.200  ? 92  TRP KKK CB  1 
ATOM 16590 C CG  . TRP K 2 92  ? 131.527 -1.694  3.251   1.000 33.450  ? 92  TRP KKK CG  1 
ATOM 16591 C CD1 . TRP K 2 92  ? 132.635 -2.477  3.391   1.000 33.340  ? 92  TRP KKK CD1 1 
ATOM 16592 C CD2 . TRP K 2 92  ? 131.791 -0.828  2.131   1.000 32.380  ? 92  TRP KKK CD2 1 
ATOM 16593 N NE1 . TRP K 2 92  ? 133.565 -2.155  2.436   1.000 32.460  ? 92  TRP KKK NE1 1 
ATOM 16594 C CE2 . TRP K 2 92  ? 133.070 -1.159  1.644   1.000 30.550  ? 92  TRP KKK CE2 1 
ATOM 16595 C CE3 . TRP K 2 92  ? 131.055 0.171   1.482   1.000 30.190  ? 92  TRP KKK CE3 1 
ATOM 16596 C CZ2 . TRP K 2 92  ? 133.641 -0.514  0.557   1.000 30.420  ? 92  TRP KKK CZ2 1 
ATOM 16597 C CZ3 . TRP K 2 92  ? 131.614 0.804   0.402   1.000 30.030  ? 92  TRP KKK CZ3 1 
ATOM 16598 C CH2 . TRP K 2 92  ? 132.895 0.471   -0.047  1.000 31.610  ? 92  TRP KKK CH2 1 
ATOM 16599 N N   . ASP K 2 93  ? 130.009 -4.320  2.103   1.000 34.630  ? 93  ASP KKK N   1 
ATOM 16600 C CA  . ASP K 2 93  ? 130.559 -5.671  1.812   1.000 31.680  ? 93  ASP KKK CA  1 
ATOM 16601 C C   . ASP K 2 93  ? 132.034 -5.517  1.457   1.000 28.290  ? 93  ASP KKK C   1 
ATOM 16602 O O   . ASP K 2 93  ? 132.339 -4.838  0.487   1.000 27.360  ? 93  ASP KKK O   1 
ATOM 16603 C CB  . ASP K 2 93  ? 129.768 -6.397  0.722   1.000 32.930  ? 93  ASP KKK CB  1 
ATOM 16604 C CG  . ASP K 2 93  ? 130.285 -7.796  0.481   1.000 35.350  ? 93  ASP KKK CG  1 
ATOM 16605 O OD1 . ASP K 2 93  ? 131.488 -7.912  0.191   1.000 40.140  ? 93  ASP KKK OD1 1 
ATOM 16606 O OD2 . ASP K 2 93  ? 129.517 -8.759  0.643   1.000 33.240  ? 93  ASP KKK OD2 1 
ATOM 16607 N N   . ASP K 2 94  ? 132.902 -6.134  2.242   1.000 27.910  ? 94  ASP KKK N   1 
ATOM 16608 C CA  . ASP K 2 94  ? 134.378 -6.014  2.123   1.000 28.970  ? 94  ASP KKK CA  1 
ATOM 16609 C C   . ASP K 2 94  ? 134.890 -6.672  0.847   1.000 29.090  ? 94  ASP KKK C   1 
ATOM 16610 O O   . ASP K 2 94  ? 135.913 -6.233  0.365   1.000 29.520  ? 94  ASP KKK O   1 
ATOM 16611 C CB  . ASP K 2 94  ? 135.093 -6.649  3.309   1.000 30.860  ? 94  ASP KKK CB  1 
ATOM 16612 C CG  . ASP K 2 94  ? 134.958 -5.857  4.591   1.000 31.540  ? 94  ASP KKK CG  1 
ATOM 16613 O OD1 . ASP K 2 94  ? 134.975 -4.621  4.500   1.000 28.650  ? 94  ASP KKK OD1 1 
ATOM 16614 O OD2 . ASP K 2 94  ? 134.874 -6.508  5.676   1.000 34.690  ? 94  ASP KKK OD2 1 
ATOM 16615 N N   . SER K 2 95  ? 134.223 -7.702  0.343   1.000 31.600  ? 95  SER KKK N   1 
ATOM 16616 C CA  . SER K 2 95  ? 134.642 -8.431  -0.878  1.000 38.150  ? 95  SER KKK CA  1 
ATOM 16617 C C   . SER K 2 95  ? 134.270 -7.600  -2.118  1.000 42.480  ? 95  SER KKK C   1 
ATOM 16618 O O   . SER K 2 95  ? 135.141 -7.407  -2.978  1.000 55.530  ? 95  SER KKK O   1 
ATOM 16619 C CB  . SER K 2 95  ? 134.096 -9.838  -0.928  1.000 40.510  ? 95  SER KKK CB  1 
ATOM 16620 O OG  . SER K 2 95  ? 132.679 -9.839  -0.994  1.000 51.690  ? 95  SER KKK OG  1 
ATOM 16621 N N   . LEU K 2 96  ? 133.054 -7.048  -2.172  1.000 42.870  ? 96  LEU KKK N   1 
ATOM 16622 C CA  . LEU K 2 96  ? 132.543 -6.280  -3.346  1.000 42.310  ? 96  LEU KKK CA  1 
ATOM 16623 C C   . LEU K 2 96  ? 133.067 -4.845  -3.283  1.000 41.040  ? 96  LEU KKK C   1 
ATOM 16624 O O   . LEU K 2 96  ? 132.816 -4.114  -4.233  1.000 42.150  ? 96  LEU KKK O   1 
ATOM 16625 C CB  . LEU K 2 96  ? 131.010 -6.272  -3.391  1.000 39.870  ? 96  LEU KKK CB  1 
ATOM 16626 C CG  . LEU K 2 96  ? 130.352 -7.652  -3.364  1.000 38.710  ? 96  LEU KKK CG  1 
ATOM 16627 C CD1 . LEU K 2 96  ? 128.838 -7.566  -3.545  1.000 36.760  ? 96  LEU KKK CD1 1 
ATOM 16628 C CD2 . LEU K 2 96  ? 130.958 -8.541  -4.453  1.000 40.250  ? 96  LEU KKK CD2 1 
ATOM 16629 N N   . LYS K 2 97  ? 133.723 -4.447  -2.196  1.000 38.910  ? 97  LYS KKK N   1 
ATOM 16630 C CA  . LYS K 2 97  ? 134.090 -3.032  -1.937  1.000 39.590  ? 97  LYS KKK CA  1 
ATOM 16631 C C   . LYS K 2 97  ? 132.929 -2.124  -2.369  1.000 36.940  ? 97  LYS KKK C   1 
ATOM 16632 O O   . LYS K 2 97  ? 133.121 -1.226  -3.216  1.000 39.520  ? 97  LYS KKK O   1 
ATOM 16633 C CB  . LYS K 2 97  ? 135.426 -2.729  -2.608  1.000 43.260  ? 97  LYS KKK CB  1 
ATOM 16634 C CG  . LYS K 2 97  ? 136.600 -3.420  -1.928  1.000 50.140  ? 97  LYS KKK CG  1 
ATOM 16635 C CD  . LYS K 2 97  ? 137.941 -3.286  -2.629  1.000 57.850  ? 97  LYS KKK CD  1 
ATOM 16636 C CE  . LYS K 2 97  ? 139.025 -4.132  -1.980  1.000 60.510  ? 97  LYS KKK CE  1 
ATOM 16637 N NZ  . LYS K 2 97  ? 140.264 -4.193  -2.794  1.000 62.050  ? 97  LYS KKK NZ  1 
ATOM 16638 N N   . GLY K 2 98  ? 131.762 -2.335  -1.770  1.000 34.170  ? 98  GLY KKK N   1 
ATOM 16639 C CA  . GLY K 2 98  ? 130.579 -1.497  -2.013  1.000 34.950  ? 98  GLY KKK CA  1 
ATOM 16640 C C   . GLY K 2 98  ? 129.515 -1.690  -0.954  1.000 33.250  ? 98  GLY KKK C   1 
ATOM 16641 O O   . GLY K 2 98  ? 129.659 -2.583  -0.115  1.000 33.370  ? 98  GLY KKK O   1 
ATOM 16642 N N   . TRP K 2 99  ? 128.475 -0.872  -0.989  1.000 32.150  ? 99  TRP KKK N   1 
ATOM 16643 C CA  . TRP K 2 99  ? 127.271 -1.040  -0.147  1.000 33.580  ? 99  TRP KKK CA  1 
ATOM 16644 C C   . TRP K 2 99  ? 126.351 -2.060  -0.815  1.000 32.420  ? 99  TRP KKK C   1 
ATOM 16645 O O   . TRP K 2 99  ? 126.052 -1.900  -2.020  1.000 31.520  ? 99  TRP KKK O   1 
ATOM 16646 C CB  . TRP K 2 99  ? 126.575 0.302   0.068   1.000 35.050  ? 99  TRP KKK CB  1 
ATOM 16647 C CG  . TRP K 2 99  ? 127.393 1.239   0.893   1.000 37.020  ? 99  TRP KKK CG  1 
ATOM 16648 C CD1 . TRP K 2 99  ? 128.232 2.222   0.461   1.000 38.830  ? 99  TRP KKK CD1 1 
ATOM 16649 C CD2 . TRP K 2 99  ? 127.470 1.248   2.325   1.000 38.820  ? 99  TRP KKK CD2 1 
ATOM 16650 N NE1 . TRP K 2 99  ? 128.815 2.854   1.528   1.000 41.540  ? 99  TRP KKK NE1 1 
ATOM 16651 C CE2 . TRP K 2 99  ? 128.360 2.279   2.684   1.000 39.850  ? 99  TRP KKK CE2 1 
ATOM 16652 C CE3 . TRP K 2 99  ? 126.859 0.499   3.332   1.000 37.250  ? 99  TRP KKK CE3 1 
ATOM 16653 C CZ2 . TRP K 2 99  ? 128.642 2.579   4.011   1.000 38.380  ? 99  TRP KKK CZ2 1 
ATOM 16654 C CZ3 . TRP K 2 99  ? 127.150 0.789   4.641   1.000 38.670  ? 99  TRP KKK CZ3 1 
ATOM 16655 C CH2 . TRP K 2 99  ? 128.016 1.825   4.974   1.000 39.590  ? 99  TRP KKK CH2 1 
ATOM 16656 N N   . VAL K 2 100 ? 125.930 -3.067  -0.050  1.000 32.110  ? 100 VAL KKK N   1 
ATOM 16657 C CA  . VAL K 2 100 ? 124.816 -3.989  -0.423  1.000 31.600  ? 100 VAL KKK CA  1 
ATOM 16658 C C   . VAL K 2 100 ? 123.558 -3.592  0.366   1.000 29.920  ? 100 VAL KKK C   1 
ATOM 16659 O O   . VAL K 2 100 ? 123.678 -3.179  1.549   1.000 29.220  ? 100 VAL KKK O   1 
ATOM 16660 C CB  . VAL K 2 100 ? 125.222 -5.456  -0.220  1.000 31.990  ? 100 VAL KKK CB  1 
ATOM 16661 C CG1 . VAL K 2 100 ? 126.447 -5.788  -1.042  1.000 31.560  ? 100 VAL KKK CG1 1 
ATOM 16662 C CG2 . VAL K 2 100 ? 125.482 -5.796  1.235   1.000 35.210  ? 100 VAL KKK CG2 1 
ATOM 16663 N N   . PHE K 2 101 ? 122.401 -3.638  -0.297  1.000 29.270  ? 101 PHE KKK N   1 
ATOM 16664 C CA  . PHE K 2 101 ? 121.063 -3.417  0.301   1.000 29.300  ? 101 PHE KKK CA  1 
ATOM 16665 C C   . PHE K 2 101 ? 120.311 -4.732  0.211   1.000 31.600  ? 101 PHE KKK C   1 
ATOM 16666 O O   . PHE K 2 101 ? 120.803 -5.674  -0.451  1.000 34.570  ? 101 PHE KKK O   1 
ATOM 16667 C CB  . PHE K 2 101 ? 120.294 -2.308  -0.411  1.000 29.990  ? 101 PHE KKK CB  1 
ATOM 16668 C CG  . PHE K 2 101 ? 120.804 -0.916  -0.103  1.000 32.670  ? 101 PHE KKK CG  1 
ATOM 16669 C CD1 . PHE K 2 101 ? 121.926 -0.419  -0.739  1.000 32.540  ? 101 PHE KKK CD1 1 
ATOM 16670 C CD2 . PHE K 2 101 ? 120.174 -0.100  0.833   1.000 34.000  ? 101 PHE KKK CD2 1 
ATOM 16671 C CE1 . PHE K 2 101 ? 122.411 0.844   -0.439  1.000 32.980  ? 101 PHE KKK CE1 1 
ATOM 16672 C CE2 . PHE K 2 101 ? 120.655 1.167   1.118   1.000 32.500  ? 101 PHE KKK CE2 1 
ATOM 16673 C CZ  . PHE K 2 101 ? 121.760 1.648   0.462   1.000 31.950  ? 101 PHE KKK CZ  1 
ATOM 16674 N N   . GLY K 2 102 ? 119.198 -4.813  0.926   1.000 35.180  ? 102 GLY KKK N   1 
ATOM 16675 C CA  . GLY K 2 102 ? 118.227 -5.913  0.803   1.000 37.960  ? 102 GLY KKK CA  1 
ATOM 16676 C C   . GLY K 2 102 ? 117.241 -5.586  -0.288  1.000 36.670  ? 102 GLY KKK C   1 
ATOM 16677 O O   . GLY K 2 102 ? 117.459 -4.575  -0.995  1.000 36.300  ? 102 GLY KKK O   1 
ATOM 16678 N N   . GLY K 2 103 ? 116.218 -6.421  -0.439  1.000 37.350  ? 103 GLY KKK N   1 
ATOM 16679 C CA  . GLY K 2 103 ? 115.173 -6.234  -1.454  1.000 39.540  ? 103 GLY KKK CA  1 
ATOM 16680 C C   . GLY K 2 103 ? 114.303 -5.062  -1.082  1.000 37.530  ? 103 GLY KKK C   1 
ATOM 16681 O O   . GLY K 2 103 ? 113.754 -4.403  -1.970  1.000 35.170  ? 103 GLY KKK O   1 
ATOM 16682 N N   . GLY K 2 104 ? 114.211 -4.794  0.208   1.000 42.210  ? 104 GLY KKK N   1 
ATOM 16683 C CA  . GLY K 2 104 ? 113.116 -3.976  0.751   1.000 49.150  ? 104 GLY KKK CA  1 
ATOM 16684 C C   . GLY K 2 104 ? 112.010 -4.861  1.287   1.000 45.720  ? 104 GLY KKK C   1 
ATOM 16685 O O   . GLY K 2 104 ? 111.877 -6.005  0.816   1.000 42.000  ? 104 GLY KKK O   1 
ATOM 16686 N N   . THR K 2 105 ? 111.291 -4.357  2.279   1.000 45.780  ? 105 THR KKK N   1 
ATOM 16687 C CA  . THR K 2 105 ? 110.193 -5.050  2.982   1.000 52.380  ? 105 THR KKK CA  1 
ATOM 16688 C C   . THR K 2 105 ? 109.022 -4.074  3.030   1.000 57.640  ? 105 THR KKK C   1 
ATOM 16689 O O   . THR K 2 105 ? 109.183 -3.052  3.710   1.000 60.200  ? 105 THR KKK O   1 
ATOM 16690 C CB  . THR K 2 105 ? 110.660 -5.499  4.378   1.000 53.540  ? 105 THR KKK CB  1 
ATOM 16691 O OG1 . THR K 2 105 ? 111.776 -6.380  4.224   1.000 48.800  ? 105 THR KKK OG1 1 
ATOM 16692 C CG2 . THR K 2 105 ? 109.570 -6.190  5.172   1.000 53.040  ? 105 THR KKK CG2 1 
ATOM 16693 N N   . LYS K 2 106 ? 107.944 -4.329  2.281   1.000 60.510  ? 106 LYS KKK N   1 
ATOM 16694 C CA  . LYS K 2 106 ? 106.710 -3.508  2.391   1.000 64.960  ? 106 LYS KKK CA  1 
ATOM 16695 C C   . LYS K 2 106 ? 105.920 -4.040  3.591   1.000 65.780  ? 106 LYS KKK C   1 
ATOM 16696 O O   . LYS K 2 106 ? 105.499 -5.223  3.566   1.000 80.030  ? 106 LYS KKK O   1 
ATOM 16697 C CB  . LYS K 2 106 ? 105.894 -3.481  1.095   1.000 69.450  ? 106 LYS KKK CB  1 
ATOM 16698 C CG  . LYS K 2 106 ? 104.830 -2.383  1.042   1.000 70.670  ? 106 LYS KKK CG  1 
ATOM 16699 C CD  . LYS K 2 106 ? 104.005 -2.366  -0.232  1.000 71.670  ? 106 LYS KKK CD  1 
ATOM 16700 C CE  . LYS K 2 106 ? 103.028 -3.524  -0.284  1.000 75.400  ? 106 LYS KKK CE  1 
ATOM 16701 N NZ  . LYS K 2 106 ? 102.334 -3.604  -1.584  1.000 79.740  ? 106 LYS KKK NZ  1 
ATOM 16702 N N   . LEU K 2 107 ? 105.798 -3.205  4.623   1.000 55.570  ? 107 LEU KKK N   1 
ATOM 16703 C CA  . LEU K 2 107 ? 105.021 -3.488  5.856   1.000 59.620  ? 107 LEU KKK CA  1 
ATOM 16704 C C   . LEU K 2 107 ? 103.611 -2.982  5.644   1.000 63.640  ? 107 LEU KKK C   1 
ATOM 16705 O O   . LEU K 2 107 ? 103.453 -1.772  5.481   1.000 63.680  ? 107 LEU KKK O   1 
ATOM 16706 C CB  . LEU K 2 107 ? 105.694 -2.769  7.029   1.000 63.470  ? 107 LEU KKK CB  1 
ATOM 16707 C CG  . LEU K 2 107 ? 105.093 -3.029  8.412   1.000 64.090  ? 107 LEU KKK CG  1 
ATOM 16708 C CD1 . LEU K 2 107 ? 105.394 -4.451  8.874   1.000 63.620  ? 107 LEU KKK CD1 1 
ATOM 16709 C CD2 . LEU K 2 107 ? 105.585 -1.999  9.428   1.000 63.560  ? 107 LEU KKK CD2 1 
ATOM 16710 N N   . THR K 2 108 ? 102.637 -3.892  5.612   1.000 69.910  ? 108 THR KKK N   1 
ATOM 16711 C CA  . THR K 2 108 ? 101.179 -3.599  5.554   1.000 71.220  ? 108 THR KKK CA  1 
ATOM 16712 C C   . THR K 2 108 ? 100.601 -3.676  6.981   1.000 70.410  ? 108 THR KKK C   1 
ATOM 16713 O O   . THR K 2 108 ? 100.997 -4.617  7.720   1.000 55.660  ? 108 THR KKK O   1 
ATOM 16714 C CB  . THR K 2 108 ? 100.494 -4.562  4.573   1.000 67.990  ? 108 THR KKK CB  1 
ATOM 16715 O OG1 . THR K 2 108 ? 101.217 -4.516  3.341   1.000 57.030  ? 108 THR KKK OG1 1 
ATOM 16716 C CG2 . THR K 2 108 ? 99.030  -4.248  4.344   1.000 65.930  ? 108 THR KKK CG2 1 
ATOM 16717 N N   . VAL K 2 109 ? 99.764  -2.703  7.359   1.000 71.280  ? 109 VAL KKK N   1 
ATOM 16718 C CA  . VAL K 2 109 ? 99.080  -2.635  8.687   1.000 75.690  ? 109 VAL KKK CA  1 
ATOM 16719 C C   . VAL K 2 109 ? 97.589  -2.911  8.481   1.000 81.800  ? 109 VAL KKK C   1 
ATOM 16720 O O   . VAL K 2 109 ? 96.959  -2.172  7.697   1.000 87.040  ? 109 VAL KKK O   1 
ATOM 16721 C CB  . VAL K 2 109 ? 99.293  -1.272  9.371   1.000 68.650  ? 109 VAL KKK CB  1 
ATOM 16722 C CG1 . VAL K 2 109 ? 98.846  -1.292  10.825  1.000 65.150  ? 109 VAL KKK CG1 1 
ATOM 16723 C CG2 . VAL K 2 109 ? 100.735 -0.810  9.257   1.000 69.830  ? 109 VAL KKK CG2 1 
ATOM 16724 N N   . LEU K 2 110 ? 97.047  -3.901  9.194   1.000 84.690  ? 110 LEU KKK N   1 
ATOM 16725 C CA  . LEU K 2 110 ? 95.672  -4.433  8.983   1.000 88.210  ? 110 LEU KKK CA  1 
ATOM 16726 C C   . LEU K 2 110 ? 94.682  -3.854  10.018  1.000 93.720  ? 110 LEU KKK C   1 
ATOM 16727 O O   . LEU K 2 110 ? 94.575  -4.430  11.140  1.000 78.270  ? 110 LEU KKK O   1 
ATOM 16728 C CB  . LEU K 2 110 ? 95.767  -5.960  9.046   1.000 83.640  ? 110 LEU KKK CB  1 
ATOM 16729 C CG  . LEU K 2 110 ? 96.831  -6.566  8.134   1.000 80.770  ? 110 LEU KKK CG  1 
ATOM 16730 C CD1 . LEU K 2 110 ? 97.021  -8.049  8.409   1.000 79.810  ? 110 LEU KKK CD1 1 
ATOM 16731 C CD2 . LEU K 2 110 ? 96.498  -6.310  6.671   1.000 79.400  ? 110 LEU KKK CD2 1 
ATOM 16732 N N   . GLY K 2 111 ? 93.956  -2.784  9.658   1.000 87.160  ? 111 GLY KKK N   1 
ATOM 16733 C CA  . GLY K 2 111 ? 93.100  -2.001  10.572  1.000 78.810  ? 111 GLY KKK CA  1 
ATOM 16734 C C   . GLY K 2 111 ? 91.698  -1.751  10.025  1.000 90.360  ? 111 GLY KKK C   1 
ATOM 16735 O O   . GLY K 2 111 ? 91.370  -2.218  8.921   1.000 89.060  ? 111 GLY KKK O   1 
ATOM 16736 N N   . ALA K 2 112 ? 90.881  -1.017  10.791  1.000 103.930 ? 112 ALA KKK N   1 
ATOM 16737 C CA  . ALA K 2 112 ? 89.417  -0.851  10.597  1.000 98.500  ? 112 ALA KKK CA  1 
ATOM 16738 C C   . ALA K 2 112 ? 89.159  0.146   9.471   1.000 94.360  ? 112 ALA KKK C   1 
ATOM 16739 O O   . ALA K 2 112 ? 89.498  1.314   9.608   1.000 81.750  ? 112 ALA KKK O   1 
ATOM 16740 C CB  . ALA K 2 112 ? 88.764  -0.409  11.895  1.000 90.650  ? 112 ALA KKK CB  1 
ATOM 16741 N N   . PRO K 2 113 ? 88.509  -0.248  8.349   1.000 108.640 ? 113 PRO KKK N   1 
ATOM 16742 C CA  . PRO K 2 113 ? 88.041  0.726   7.354   1.000 104.480 ? 113 PRO KKK CA  1 
ATOM 16743 C C   . PRO K 2 113 ? 87.065  1.758   7.945   1.000 92.830  ? 113 PRO KKK C   1 
ATOM 16744 O O   . PRO K 2 113 ? 86.549  2.532   7.166   1.000 79.960  ? 113 PRO KKK O   1 
ATOM 16745 C CB  . PRO K 2 113 ? 87.581  -0.143  6.171   1.000 100.570 ? 113 PRO KKK CB  1 
ATOM 16746 C CG  . PRO K 2 113 ? 87.195  -1.467  6.807   1.000 101.900 ? 113 PRO KKK CG  1 
ATOM 16747 C CD  . PRO K 2 113 ? 88.149  -1.630  7.984   1.000 109.420 ? 113 PRO KKK CD  1 
ATOM 16748 N N   . LEU K 2 139 ? 88.743  10.901  -9.558  1.000 68.370  ? 139 LEU KKK N   1 
ATOM 16749 C CA  . LEU K 2 139 ? 87.899  9.696   -9.348  1.000 77.320  ? 139 LEU KKK CA  1 
ATOM 16750 C C   . LEU K 2 139 ? 88.045  9.194   -7.906  1.000 81.390  ? 139 LEU KKK C   1 
ATOM 16751 O O   . LEU K 2 139 ? 87.768  9.984   -6.990  1.000 77.950  ? 139 LEU KKK O   1 
ATOM 16752 C CB  . LEU K 2 139 ? 88.277  8.625   -10.374 1.000 75.730  ? 139 LEU KKK CB  1 
ATOM 16753 C CG  . LEU K 2 139 ? 87.279  8.439   -11.514 1.000 74.020  ? 139 LEU KKK CG  1 
ATOM 16754 C CD1 . LEU K 2 139 ? 87.655  9.301   -12.707 1.000 67.560  ? 139 LEU KKK CD1 1 
ATOM 16755 C CD2 . LEU K 2 139 ? 87.183  6.977   -11.916 1.000 70.100  ? 139 LEU KKK CD2 1 
ATOM 16756 N N   . ILE K 2 140 ? 88.453  7.936   -7.709  1.000 85.710  ? 140 ILE KKK N   1 
ATOM 16757 C CA  . ILE K 2 140 ? 88.536  7.344   -6.337  1.000 93.790  ? 140 ILE KKK CA  1 
ATOM 16758 C C   . ILE K 2 140 ? 89.476  8.185   -5.474  1.000 108.730 ? 140 ILE KKK C   1 
ATOM 16759 O O   . ILE K 2 140 ? 90.517  8.629   -6.010  1.000 115.570 ? 140 ILE KKK O   1 
ATOM 16760 C CB  . ILE K 2 140 ? 88.942  5.861   -6.419  1.000 88.250  ? 140 ILE KKK CB  1 
ATOM 16761 C CG1 . ILE K 2 140 ? 88.994  5.380   -7.870  1.000 87.330  ? 140 ILE KKK CG1 1 
ATOM 16762 C CG2 . ILE K 2 140 ? 87.989  5.011   -5.588  1.000 83.240  ? 140 ILE KKK CG2 1 
ATOM 16763 C CD1 . ILE K 2 140 ? 88.161  4.155   -8.143  1.000 86.280  ? 140 ILE KKK CD1 1 
ATOM 16764 N N   . SER K 2 141 ? 89.168  8.387   -4.185  1.000 113.160 ? 141 SER KKK N   1 
ATOM 16765 C CA  . SER K 2 141 ? 90.011  9.325   -3.393  1.000 111.330 ? 141 SER KKK CA  1 
ATOM 16766 C C   . SER K 2 141 ? 90.353  8.842   -1.985  1.000 114.360 ? 141 SER KKK C   1 
ATOM 16767 O O   . SER K 2 141 ? 91.502  9.068   -1.565  1.000 114.590 ? 141 SER KKK O   1 
ATOM 16768 C CB  . SER K 2 141 ? 89.382  10.685  -3.325  1.000 108.290 ? 141 SER KKK CB  1 
ATOM 16769 O OG  . SER K 2 141 ? 89.782  11.368  -2.147  1.000 106.380 ? 141 SER KKK OG  1 
ATOM 16770 N N   . ASP K 2 142 ? 89.407  8.263   -1.248  1.000 116.420 ? 142 ASP KKK N   1 
ATOM 16771 C CA  . ASP K 2 142 ? 89.732  7.928   0.163   1.000 105.540 ? 142 ASP KKK CA  1 
ATOM 16772 C C   . ASP K 2 142 ? 89.229  6.535   0.524   1.000 101.470 ? 142 ASP KKK C   1 
ATOM 16773 O O   . ASP K 2 142 ? 88.238  6.450   1.261   1.000 95.600  ? 142 ASP KKK O   1 
ATOM 16774 C CB  . ASP K 2 142 ? 89.173  8.984   1.114   1.000 97.720  ? 142 ASP KKK CB  1 
ATOM 16775 C CG  . ASP K 2 142 ? 90.141  10.122  1.383   1.000 101.330 ? 142 ASP KKK CG  1 
ATOM 16776 O OD1 . ASP K 2 142 ? 91.351  9.848   1.479   1.000 107.890 ? 142 ASP KKK OD1 1 
ATOM 16777 O OD2 . ASP K 2 142 ? 89.677  11.273  1.489   1.000 96.780  ? 142 ASP KKK OD2 1 
ATOM 16778 N N   . PHE K 2 143 ? 89.911  5.490   0.057   1.000 111.700 ? 143 PHE KKK N   1 
ATOM 16779 C CA  . PHE K 2 143 ? 89.507  4.121   0.471   1.000 119.120 ? 143 PHE KKK CA  1 
ATOM 16780 C C   . PHE K 2 143 ? 90.449  3.576   1.543   1.000 119.240 ? 143 PHE KKK C   1 
ATOM 16781 O O   . PHE K 2 143 ? 91.674  3.675   1.381   1.000 128.860 ? 143 PHE KKK O   1 
ATOM 16782 C CB  . PHE K 2 143 ? 89.328  3.164   -0.709  1.000 123.960 ? 143 PHE KKK CB  1 
ATOM 16783 C CG  . PHE K 2 143 ? 90.397  3.174   -1.770  1.000 129.870 ? 143 PHE KKK CG  1 
ATOM 16784 C CD1 . PHE K 2 143 ? 91.499  2.344   -1.674  1.000 127.440 ? 143 PHE KKK CD1 1 
ATOM 16785 C CD2 . PHE K 2 143 ? 90.270  3.975   -2.892  1.000 126.330 ? 143 PHE KKK CD2 1 
ATOM 16786 C CE1 . PHE K 2 143 ? 92.471  2.345   -2.659  1.000 127.070 ? 143 PHE KKK CE1 1 
ATOM 16787 C CE2 . PHE K 2 143 ? 91.238  3.966   -3.880  1.000 118.010 ? 143 PHE KKK CE2 1 
ATOM 16788 C CZ  . PHE K 2 143 ? 92.336  3.152   -3.761  1.000 119.560 ? 143 PHE KKK CZ  1 
ATOM 16789 N N   . TYR K 2 144 ? 89.877  3.031   2.613   1.000 114.930 ? 144 TYR KKK N   1 
ATOM 16790 C CA  . TYR K 2 144 ? 90.686  2.423   3.698   1.000 114.940 ? 144 TYR KKK CA  1 
ATOM 16791 C C   . TYR K 2 144 ? 90.932  0.929   3.458   1.000 113.390 ? 144 TYR KKK C   1 
ATOM 16792 O O   . TYR K 2 144 ? 92.040  0.498   3.821   1.000 94.250  ? 144 TYR KKK O   1 
ATOM 16793 C CB  . TYR K 2 144 ? 90.060  2.697   5.064   1.000 111.610 ? 144 TYR KKK CB  1 
ATOM 16794 N N   . PRO K 2 145 ? 89.988  0.100   2.948   1.000 119.770 ? 145 PRO KKK N   1 
ATOM 16795 C CA  . PRO K 2 145 ? 90.275  -1.294  2.620   1.000 114.040 ? 145 PRO KKK CA  1 
ATOM 16796 C C   . PRO K 2 145 ? 91.702  -1.502  2.106   1.000 101.190 ? 145 PRO KKK C   1 
ATOM 16797 O O   . PRO K 2 145 ? 92.392  -2.335  2.645   1.000 99.940  ? 145 PRO KKK O   1 
ATOM 16798 C CB  . PRO K 2 145 ? 89.311  -1.507  1.452   1.000 120.480 ? 145 PRO KKK CB  1 
ATOM 16799 C CG  . PRO K 2 145 ? 88.057  -0.808  1.899   1.000 121.870 ? 145 PRO KKK CG  1 
ATOM 16800 C CD  . PRO K 2 145 ? 88.552  0.352   2.736   1.000 123.910 ? 145 PRO KKK CD  1 
ATOM 16801 N N   . GLY K 2 146 ? 92.093  -0.759  1.073   1.000 92.060  ? 146 GLY KKK N   1 
ATOM 16802 C CA  . GLY K 2 146 ? 93.472  -0.849  0.566   1.000 91.960  ? 146 GLY KKK CA  1 
ATOM 16803 C C   . GLY K 2 146 ? 93.515  -0.859  -0.946  1.000 96.910  ? 146 GLY KKK C   1 
ATOM 16804 O O   . GLY K 2 146 ? 94.524  -0.400  -1.507  1.000 99.600  ? 146 GLY KKK O   1 
ATOM 16805 N N   . ALA K 2 147 ? 92.458  -1.353  -1.586  1.000 105.200 ? 147 ALA KKK N   1 
ATOM 16806 C CA  . ALA K 2 147 ? 92.482  -1.478  -3.058  1.000 105.810 ? 147 ALA KKK CA  1 
ATOM 16807 C C   . ALA K 2 147 ? 91.072  -1.386  -3.649  1.000 109.070 ? 147 ALA KKK C   1 
ATOM 16808 O O   . ALA K 2 147 ? 90.099  -1.546  -2.889  1.000 99.130  ? 147 ALA KKK O   1 
ATOM 16809 C CB  . ALA K 2 147 ? 93.141  -2.776  -3.429  1.000 98.910  ? 147 ALA KKK CB  1 
ATOM 16810 N N   . VAL K 2 148 ? 90.979  -1.127  -4.957  1.000 105.390 ? 148 VAL KKK N   1 
ATOM 16811 C CA  . VAL K 2 148 ? 89.664  -1.058  -5.656  1.000 98.350  ? 148 VAL KKK CA  1 
ATOM 16812 C C   . VAL K 2 148 ? 89.746  -1.993  -6.863  1.000 94.370  ? 148 VAL KKK C   1 
ATOM 16813 O O   . VAL K 2 148 ? 90.791  -2.655  -6.997  1.000 88.520  ? 148 VAL KKK O   1 
ATOM 16814 C CB  . VAL K 2 148 ? 89.345  0.377   -6.101  1.000 91.940  ? 148 VAL KKK CB  1 
ATOM 16815 C CG1 . VAL K 2 148 ? 88.704  1.186   -4.981  1.000 95.650  ? 148 VAL KKK CG1 1 
ATOM 16816 C CG2 . VAL K 2 148 ? 90.564  1.086   -6.664  1.000 85.730  ? 148 VAL KKK CG2 1 
ATOM 16817 N N   . THR K 2 165 ? 93.413  3.132   -14.735 1.000 87.600  ? 165 THR KKK N   1 
ATOM 16818 C CA  . THR K 2 165 ? 94.108  1.880   -14.336 1.000 93.360  ? 165 THR KKK CA  1 
ATOM 16819 C C   . THR K 2 165 ? 95.303  2.242   -13.448 1.000 91.060  ? 165 THR KKK C   1 
ATOM 16820 O O   . THR K 2 165 ? 96.408  1.734   -13.692 1.000 94.060  ? 165 THR KKK O   1 
ATOM 16821 C CB  . THR K 2 165 ? 94.403  1.022   -15.575 1.000 98.940  ? 165 THR KKK CB  1 
ATOM 16822 O OG1 . THR K 2 165 ? 95.319  -0.036  -15.285 1.000 113.490 ? 165 THR KKK OG1 1 
ATOM 16823 C CG2 . THR K 2 165 ? 94.884  1.833   -16.758 1.000 84.220  ? 165 THR KKK CG2 1 
ATOM 16824 N N   . THR K 2 166 ? 95.079  3.098   -12.451 1.000 92.370  ? 166 THR KKK N   1 
ATOM 16825 C CA  . THR K 2 166 ? 96.167  3.488   -11.523 1.000 93.670  ? 166 THR KKK CA  1 
ATOM 16826 C C   . THR K 2 166 ? 96.216  2.499   -10.369 1.000 95.370  ? 166 THR KKK C   1 
ATOM 16827 O O   . THR K 2 166 ? 95.147  2.142   -9.859  1.000 84.590  ? 166 THR KKK O   1 
ATOM 16828 C CB  . THR K 2 166 ? 95.929  4.862   -10.898 1.000 88.810  ? 166 THR KKK CB  1 
ATOM 16829 O OG1 . THR K 2 166 ? 95.549  5.726   -11.963 1.000 95.170  ? 166 THR KKK OG1 1 
ATOM 16830 C CG2 . THR K 2 166 ? 97.145  5.430   -10.202 1.000 87.610  ? 166 THR KKK CG2 1 
ATOM 16831 N N   . LYS K 2 167 ? 97.417  2.066   -9.999  1.000 95.390  ? 167 LYS KKK N   1 
ATOM 16832 C CA  . LYS K 2 167 ? 97.552  1.194   -8.816  1.000 92.070  ? 167 LYS KKK CA  1 
ATOM 16833 C C   . LYS K 2 167 ? 97.256  2.059   -7.595  1.000 99.020  ? 167 LYS KKK C   1 
ATOM 16834 O O   . LYS K 2 167 ? 97.927  3.091   -7.431  1.000 95.460  ? 167 LYS KKK O   1 
ATOM 16835 C CB  . LYS K 2 167 ? 98.978  0.650   -8.758  1.000 80.710  ? 167 LYS KKK CB  1 
ATOM 16836 N N   . PRO K 2 168 ? 96.272  1.688   -6.753  1.000 108.430 ? 168 PRO KKK N   1 
ATOM 16837 C CA  . PRO K 2 168 ? 95.921  2.455   -5.561  1.000 108.240 ? 168 PRO KKK CA  1 
ATOM 16838 C C   . PRO K 2 168 ? 97.122  3.001   -4.778  1.000 100.260 ? 168 PRO KKK C   1 
ATOM 16839 O O   . PRO K 2 168 ? 98.038  2.252   -4.511  1.000 106.500 ? 168 PRO KKK O   1 
ATOM 16840 C CB  . PRO K 2 168 ? 95.232  1.381   -4.722  1.000 112.410 ? 168 PRO KKK CB  1 
ATOM 16841 C CG  . PRO K 2 168 ? 94.479  0.566   -5.736  1.000 107.980 ? 168 PRO KKK CG  1 
ATOM 16842 C CD  . PRO K 2 168 ? 95.434  0.496   -6.910  1.000 107.330 ? 168 PRO KKK CD  1 
ATOM 16843 N N   . SER K 2 169 ? 97.066  4.274   -4.393  1.000 87.080  ? 169 SER KKK N   1 
ATOM 16844 C CA  . SER K 2 169 ? 98.179  4.913   -3.655  1.000 82.100  ? 169 SER KKK CA  1 
ATOM 16845 C C   . SER K 2 169 ? 97.727  5.233   -2.238  1.000 81.320  ? 169 SER KKK C   1 
ATOM 16846 O O   . SER K 2 169 ? 96.653  4.754   -1.839  1.000 81.090  ? 169 SER KKK O   1 
ATOM 16847 C CB  . SER K 2 169 ? 98.591  6.167   -4.344  1.000 82.910  ? 169 SER KKK CB  1 
ATOM 16848 O OG  . SER K 2 169 ? 97.626  7.187   -4.141  1.000 81.860  ? 169 SER KKK OG  1 
ATOM 16849 N N   . LYS K 2 170 ? 98.518  6.034   -1.525  1.000 79.470  ? 170 LYS KKK N   1 
ATOM 16850 C CA  . LYS K 2 170 ? 98.179  6.407   -0.131  1.000 78.610  ? 170 LYS KKK CA  1 
ATOM 16851 C C   . LYS K 2 170 ? 98.567  7.869   0.102   1.000 72.520  ? 170 LYS KKK C   1 
ATOM 16852 O O   . LYS K 2 170 ? 97.836  8.538   0.853   1.000 72.600  ? 170 LYS KKK O   1 
ATOM 16853 C CB  . LYS K 2 170 ? 98.941  5.501   0.835   1.000 72.830  ? 170 LYS KKK CB  1 
ATOM 16854 N N   . ALA K 2 177 ? 94.100  6.016   -2.648  1.000 102.450 ? 177 ALA KKK N   1 
ATOM 16855 C CA  . ALA K 2 177 ? 93.501  6.766   -3.779  1.000 100.780 ? 177 ALA KKK CA  1 
ATOM 16856 C C   . ALA K 2 177 ? 93.997  6.197   -5.123  1.000 102.040 ? 177 ALA KKK C   1 
ATOM 16857 O O   . ALA K 2 177 ? 95.218  5.957   -5.262  1.000 100.480 ? 177 ALA KKK O   1 
ATOM 16858 C CB  . ALA K 2 177 ? 93.815  8.237   -3.621  1.000 93.610  ? 177 ALA KKK CB  1 
ATOM 16859 N N   . ALA K 2 178 ? 93.086  5.969   -6.067  1.000 103.750 ? 178 ALA KKK N   1 
ATOM 16860 C CA  . ALA K 2 178 ? 93.342  5.430   -7.427  1.000 105.530 ? 178 ALA KKK CA  1 
ATOM 16861 C C   . ALA K 2 178 ? 92.588  6.265   -8.482  1.000 104.410 ? 178 ALA KKK C   1 
ATOM 16862 O O   . ALA K 2 178 ? 91.807  7.150   -8.088  1.000 94.750  ? 178 ALA KKK O   1 
ATOM 16863 C CB  . ALA K 2 178 ? 92.958  3.972   -7.467  1.000 98.660  ? 178 ALA KKK CB  1 
ATOM 16864 N N   . SER K 2 179 ? 92.860  6.049   -9.773  1.000 98.540  ? 179 SER KKK N   1 
ATOM 16865 C CA  . SER K 2 179 ? 92.315  6.829   -10.919 1.000 99.780  ? 179 SER KKK CA  1 
ATOM 16866 C C   . SER K 2 179 ? 92.059  5.888   -12.104 1.000 105.470 ? 179 SER KKK C   1 
ATOM 16867 O O   . SER K 2 179 ? 92.834  4.908   -12.260 1.000 108.980 ? 179 SER KKK O   1 
ATOM 16868 C CB  . SER K 2 179 ? 93.253  7.953   -11.304 1.000 103.590 ? 179 SER KKK CB  1 
ATOM 16869 O OG  . SER K 2 179 ? 93.512  8.814   -10.202 1.000 108.020 ? 179 SER KKK OG  1 
ATOM 16870 N N   . SER K 2 180 ? 91.010  6.161   -12.892 1.000 111.220 ? 180 SER KKK N   1 
ATOM 16871 C CA  . SER K 2 180 ? 90.626  5.396   -14.110 1.000 102.980 ? 180 SER KKK CA  1 
ATOM 16872 C C   . SER K 2 180 ? 90.186  6.359   -15.224 1.000 102.970 ? 180 SER KKK C   1 
ATOM 16873 O O   . SER K 2 180 ? 89.500  7.354   -14.900 1.000 89.000  ? 180 SER KKK O   1 
ATOM 16874 C CB  . SER K 2 180 ? 89.548  4.396   -13.794 1.000 100.980 ? 180 SER KKK CB  1 
ATOM 16875 O OG  . SER K 2 180 ? 89.198  3.674   -14.958 1.000 99.040  ? 180 SER KKK OG  1 
ATOM 16876 N N   . TYR K 2 181 ? 90.604  6.085   -16.468 1.000 104.240 ? 181 TYR KKK N   1 
ATOM 16877 C CA  . TYR K 2 181 ? 90.100  6.693   -17.724 1.000 103.760 ? 181 TYR KKK CA  1 
ATOM 16878 C C   . TYR K 2 181 ? 89.912  5.576   -18.775 1.000 105.340 ? 181 TYR KKK C   1 
ATOM 16879 O O   . TYR K 2 181 ? 90.714  4.609   -18.752 1.000 107.320 ? 181 TYR KKK O   1 
ATOM 16880 C CB  . TYR K 2 181 ? 91.073  7.738   -18.292 1.000 103.060 ? 181 TYR KKK CB  1 
ATOM 16881 C CG  . TYR K 2 181 ? 91.690  8.758   -17.363 1.000 100.120 ? 181 TYR KKK CG  1 
ATOM 16882 C CD1 . TYR K 2 181 ? 92.771  8.438   -16.561 1.000 87.380  ? 181 TYR KKK CD1 1 
ATOM 16883 C CD2 . TYR K 2 181 ? 91.233  10.069  -17.331 1.000 102.140 ? 181 TYR KKK CD2 1 
ATOM 16884 C CE1 . TYR K 2 181 ? 93.373  9.383   -15.738 1.000 77.720  ? 181 TYR KKK CE1 1 
ATOM 16885 C CE2 . TYR K 2 181 ? 91.812  11.023  -16.511 1.000 97.040  ? 181 TYR KKK CE2 1 
ATOM 16886 C CZ  . TYR K 2 181 ? 92.891  10.682  -15.715 1.000 83.040  ? 181 TYR KKK CZ  1 
ATOM 16887 O OH  . TYR K 2 181 ? 93.444  11.648  -14.926 1.000 70.590  ? 181 TYR KKK OH  1 
ATOM 16888 N N   . LEU K 2 182 ? 88.890  5.679   -19.650 1.000 102.060 ? 182 LEU KKK N   1 
ATOM 16889 C CA  . LEU K 2 182 ? 88.776  5.017   -21.002 1.000 96.920  ? 182 LEU KKK CA  1 
ATOM 16890 C C   . LEU K 2 182 ? 87.345  5.197   -21.526 1.000 78.090  ? 182 LEU KKK C   1 
ATOM 16891 O O   . LEU K 2 182 ? 86.850  6.304   -21.436 1.000 63.750  ? 182 LEU KKK O   1 
ATOM 16892 C CB  . LEU K 2 182 ? 89.162  3.524   -20.995 1.000 97.350  ? 182 LEU KKK CB  1 
ATOM 16893 C CG  . LEU K 2 182 ? 88.948  2.750   -22.307 1.000 93.480  ? 182 LEU KKK CG  1 
ATOM 16894 C CD1 . LEU K 2 182 ? 89.518  3.481   -23.525 1.000 84.130  ? 182 LEU KKK CD1 1 
ATOM 16895 C CD2 . LEU K 2 182 ? 89.547  1.355   -22.207 1.000 86.710  ? 182 LEU KKK CD2 1 
ATOM 16896 N N   . GLU L 3 1   ? 118.545 21.081  9.370   1.000 60.420  ? 1   GLU LLL N   1 
ATOM 16897 C CA  . GLU L 3 1   ? 119.969 21.038  9.889   1.000 61.740  ? 1   GLU LLL CA  1 
ATOM 16898 C C   . GLU L 3 1   ? 120.922 20.720  8.720   1.000 48.710  ? 1   GLU LLL C   1 
ATOM 16899 O O   . GLU L 3 1   ? 121.706 21.574  8.373   1.000 34.250  ? 1   GLU LLL O   1 
ATOM 16900 C CB  . GLU L 3 1   ? 120.064 20.058  11.079  1.000 62.410  ? 1   GLU LLL CB  1 
ATOM 16901 N N   . VAL L 3 2   ? 120.905 19.485  8.235   1.000 48.690  ? 2   VAL LLL N   1 
ATOM 16902 C CA  . VAL L 3 2   ? 121.738 18.995  7.109   1.000 49.920  ? 2   VAL LLL CA  1 
ATOM 16903 C C   . VAL L 3 2   ? 120.794 18.805  5.925   1.000 49.900  ? 2   VAL LLL C   1 
ATOM 16904 O O   . VAL L 3 2   ? 119.798 18.094  6.103   1.000 62.180  ? 2   VAL LLL O   1 
ATOM 16905 C CB  . VAL L 3 2   ? 122.469 17.684  7.466   1.000 48.350  ? 2   VAL LLL CB  1 
ATOM 16906 C CG1 . VAL L 3 2   ? 122.876 16.885  6.234   1.000 50.670  ? 2   VAL LLL CG1 1 
ATOM 16907 C CG2 . VAL L 3 2   ? 123.687 17.942  8.329   1.000 51.210  ? 2   VAL LLL CG2 1 
ATOM 16908 N N   . GLN L 3 3   ? 121.094 19.409  4.780   1.000 46.980  ? 3   GLN LLL N   1 
ATOM 16909 C CA  . GLN L 3 3   ? 120.294 19.135  3.564   1.000 47.850  ? 3   GLN LLL CA  1 
ATOM 16910 C C   . GLN L 3 3   ? 121.227 18.855  2.395   1.000 42.230  ? 3   GLN LLL C   1 
ATOM 16911 O O   . GLN L 3 3   ? 122.258 19.547  2.229   1.000 37.410  ? 3   GLN LLL O   1 
ATOM 16912 C CB  . GLN L 3 3   ? 119.280 20.233  3.256   1.000 58.240  ? 3   GLN LLL CB  1 
ATOM 16913 C CG  . GLN L 3 3   ? 119.594 21.566  3.906   1.000 67.790  ? 3   GLN LLL CG  1 
ATOM 16914 C CD  . GLN L 3 3   ? 118.663 22.636  3.393   1.000 71.660  ? 3   GLN LLL CD  1 
ATOM 16915 O OE1 . GLN L 3 3   ? 118.002 22.487  2.351   1.000 63.160  ? 3   GLN LLL OE1 1 
ATOM 16916 N NE2 . GLN L 3 3   ? 118.611 23.740  4.130   1.000 77.590  ? 3   GLN LLL NE2 1 
ATOM 16917 N N   . LEU L 3 4   ? 120.874 17.815  1.643   1.000 39.270  ? 4   LEU LLL N   1 
ATOM 16918 C CA  . LEU L 3 4   ? 121.470 17.456  0.336   1.000 41.570  ? 4   LEU LLL CA  1 
ATOM 16919 C C   . LEU L 3 4   ? 120.398 17.653  -0.739  1.000 39.520  ? 4   LEU LLL C   1 
ATOM 16920 O O   . LEU L 3 4   ? 119.243 17.258  -0.489  1.000 39.750  ? 4   LEU LLL O   1 
ATOM 16921 C CB  . LEU L 3 4   ? 121.922 15.995  0.389   1.000 42.510  ? 4   LEU LLL CB  1 
ATOM 16922 C CG  . LEU L 3 4   ? 122.923 15.641  1.490   1.000 41.790  ? 4   LEU LLL CG  1 
ATOM 16923 C CD1 . LEU L 3 4   ? 123.101 14.143  1.500   1.000 42.270  ? 4   LEU LLL CD1 1 
ATOM 16924 C CD2 . LEU L 3 4   ? 124.265 16.361  1.352   1.000 39.820  ? 4   LEU LLL CD2 1 
ATOM 16925 N N   . VAL L 3 5   ? 120.758 18.243  -1.881  1.000 36.420  ? 5   VAL LLL N   1 
ATOM 16926 C CA  . VAL L 3 5   ? 119.816 18.511  -3.006  1.000 35.110  ? 5   VAL LLL CA  1 
ATOM 16927 C C   . VAL L 3 5   ? 120.450 18.050  -4.313  1.000 34.730  ? 5   VAL LLL C   1 
ATOM 16928 O O   . VAL L 3 5   ? 121.499 18.560  -4.680  1.000 36.410  ? 5   VAL LLL O   1 
ATOM 16929 C CB  . VAL L 3 5   ? 119.404 19.986  -3.091  1.000 35.290  ? 5   VAL LLL CB  1 
ATOM 16930 C CG1 . VAL L 3 5   ? 118.117 20.131  -3.873  1.000 32.980  ? 5   VAL LLL CG1 1 
ATOM 16931 C CG2 . VAL L 3 5   ? 119.260 20.610  -1.709  1.000 38.600  ? 5   VAL LLL CG2 1 
ATOM 16932 N N   . GLU L 3 6   ? 119.804 17.102  -4.974  1.000 37.680  ? 6   GLU LLL N   1 
ATOM 16933 C CA  . GLU L 3 6   ? 120.229 16.549  -6.280  1.000 43.010  ? 6   GLU LLL CA  1 
ATOM 16934 C C   . GLU L 3 6   ? 119.591 17.379  -7.394  1.000 45.510  ? 6   GLU LLL C   1 
ATOM 16935 O O   . GLU L 3 6   ? 118.595 18.074  -7.134  1.000 53.400  ? 6   GLU LLL O   1 
ATOM 16936 C CB  . GLU L 3 6   ? 119.833 15.076  -6.391  1.000 47.850  ? 6   GLU LLL CB  1 
ATOM 16937 C CG  . GLU L 3 6   ? 120.471 14.207  -5.330  1.000 52.020  ? 6   GLU LLL CG  1 
ATOM 16938 C CD  . GLU L 3 6   ? 119.596 13.964  -4.113  1.000 53.840  ? 6   GLU LLL CD  1 
ATOM 16939 O OE1 . GLU L 3 6   ? 118.662 14.764  -3.881  1.000 55.040  ? 6   GLU LLL OE1 1 
ATOM 16940 O OE2 . GLU L 3 6   ? 119.830 12.970  -3.420  1.000 53.820  ? 6   GLU LLL OE2 1 
ATOM 16941 N N   . SER L 3 7   ? 120.148 17.260  -8.598  1.000 43.200  ? 7   SER LLL N   1 
ATOM 16942 C CA  . SER L 3 7   ? 119.760 17.992  -9.824  1.000 43.730  ? 7   SER LLL CA  1 
ATOM 16943 C C   . SER L 3 7   ? 120.551 17.425  -11.001 1.000 43.210  ? 7   SER LLL C   1 
ATOM 16944 O O   . SER L 3 7   ? 121.583 16.754  -10.771 1.000 45.120  ? 7   SER LLL O   1 
ATOM 16945 C CB  . SER L 3 7   ? 120.025 19.457  -9.663  1.000 44.990  ? 7   SER LLL CB  1 
ATOM 16946 O OG  . SER L 3 7   ? 121.391 19.661  -9.338  1.000 45.180  ? 7   SER LLL OG  1 
ATOM 16947 N N   . GLY L 3 8   ? 120.075 17.693  -12.213 1.000 45.910  ? 8   GLY LLL N   1 
ATOM 16948 C CA  . GLY L 3 8   ? 120.720 17.277  -13.471 1.000 48.020  ? 8   GLY LLL CA  1 
ATOM 16949 C C   . GLY L 3 8   ? 119.997 16.108  -14.106 1.000 49.010  ? 8   GLY LLL C   1 
ATOM 16950 O O   . GLY L 3 8   ? 120.275 15.824  -15.284 1.000 54.260  ? 8   GLY LLL O   1 
ATOM 16951 N N   . GLY L 3 9   ? 119.112 15.447  -13.358 1.000 47.610  ? 9   GLY LLL N   1 
ATOM 16952 C CA  . GLY L 3 9   ? 118.306 14.325  -13.867 1.000 49.310  ? 9   GLY LLL CA  1 
ATOM 16953 C C   . GLY L 3 9   ? 117.330 14.785  -14.938 1.000 46.440  ? 9   GLY LLL C   1 
ATOM 16954 O O   . GLY L 3 9   ? 116.846 15.913  -14.834 1.000 41.270  ? 9   GLY LLL O   1 
ATOM 16955 N N   . GLY L 3 10  ? 117.073 13.940  -15.937 1.000 45.410  ? 10  GLY LLL N   1 
ATOM 16956 C CA  . GLY L 3 10  ? 116.018 14.158  -16.940 1.000 52.440  ? 10  GLY LLL CA  1 
ATOM 16957 C C   . GLY L 3 10  ? 115.895 12.984  -17.902 1.000 60.090  ? 10  GLY LLL C   1 
ATOM 16958 O O   . GLY L 3 10  ? 116.246 11.849  -17.518 1.000 56.680  ? 10  GLY LLL O   1 
ATOM 16959 N N   . LEU L 3 11  ? 115.406 13.251  -19.120 1.000 67.980  ? 11  LEU LLL N   1 
ATOM 16960 C CA  . LEU L 3 11  ? 115.277 12.257  -20.214 1.000 65.290  ? 11  LEU LLL CA  1 
ATOM 16961 C C   . LEU L 3 11  ? 116.530 12.326  -21.094 1.000 56.220  ? 11  LEU LLL C   1 
ATOM 16962 O O   . LEU L 3 11  ? 116.901 13.430  -21.493 1.000 57.420  ? 11  LEU LLL O   1 
ATOM 16963 C CB  . LEU L 3 11  ? 114.002 12.540  -21.013 1.000 71.180  ? 11  LEU LLL CB  1 
ATOM 16964 C CG  . LEU L 3 11  ? 113.567 11.411  -21.955 1.000 82.110  ? 11  LEU LLL CG  1 
ATOM 16965 C CD1 . LEU L 3 11  ? 112.069 11.291  -21.997 1.000 93.540  ? 11  LEU LLL CD1 1 
ATOM 16966 C CD2 . LEU L 3 11  ? 114.126 11.597  -23.364 1.000 83.700  ? 11  LEU LLL CD2 1 
ATOM 16967 N N   . VAL L 3 12  ? 117.149 11.182  -21.357 1.000 48.580  ? 12  VAL LLL N   1 
ATOM 16968 C CA  . VAL L 3 12  ? 118.257 11.048  -22.340 1.000 52.070  ? 12  VAL LLL CA  1 
ATOM 16969 C C   . VAL L 3 12  ? 118.096 9.694   -23.032 1.000 51.390  ? 12  VAL LLL C   1 
ATOM 16970 O O   . VAL L 3 12  ? 117.469 8.789   -22.416 1.000 49.940  ? 12  VAL LLL O   1 
ATOM 16971 C CB  . VAL L 3 12  ? 119.631 11.181  -21.658 1.000 60.980  ? 12  VAL LLL CB  1 
ATOM 16972 C CG1 . VAL L 3 12  ? 119.770 10.196  -20.508 1.000 66.520  ? 12  VAL LLL CG1 1 
ATOM 16973 C CG2 . VAL L 3 12  ? 120.792 11.039  -22.639 1.000 60.310  ? 12  VAL LLL CG2 1 
ATOM 16974 N N   . LYS L 3 13  ? 118.587 9.592   -24.275 1.000 50.830  ? 13  LYS LLL N   1 
ATOM 16975 C CA  . LYS L 3 13  ? 118.400 8.415   -25.160 1.000 44.630  ? 13  LYS LLL CA  1 
ATOM 16976 C C   . LYS L 3 13  ? 119.512 7.427   -24.841 1.000 41.620  ? 13  LYS LLL C   1 
ATOM 16977 O O   . LYS L 3 13  ? 120.606 7.836   -24.468 1.000 40.480  ? 13  LYS LLL O   1 
ATOM 16978 C CB  . LYS L 3 13  ? 118.380 8.830   -26.639 1.000 39.900  ? 13  LYS LLL CB  1 
ATOM 16979 N N   . PRO L 3 14  ? 119.245 6.102   -24.910 1.000 40.810  ? 14  PRO LLL N   1 
ATOM 16980 C CA  . PRO L 3 14  ? 120.286 5.088   -24.756 1.000 40.610  ? 14  PRO LLL CA  1 
ATOM 16981 C C   . PRO L 3 14  ? 121.562 5.506   -25.481 1.000 43.260  ? 14  PRO LLL C   1 
ATOM 16982 O O   . PRO L 3 14  ? 121.464 6.214   -26.461 1.000 40.770  ? 14  PRO LLL O   1 
ATOM 16983 C CB  . PRO L 3 14  ? 119.678 3.860   -25.438 1.000 41.610  ? 14  PRO LLL CB  1 
ATOM 16984 C CG  . PRO L 3 14  ? 118.180 4.028   -25.177 1.000 44.180  ? 14  PRO LLL CG  1 
ATOM 16985 C CD  . PRO L 3 14  ? 117.909 5.522   -25.118 1.000 41.130  ? 14  PRO LLL CD  1 
ATOM 16986 N N   . GLY L 3 15  ? 122.715 5.074   -24.971 1.000 49.200  ? 15  GLY LLL N   1 
ATOM 16987 C CA  . GLY L 3 15  ? 124.043 5.488   -25.464 1.000 50.570  ? 15  GLY LLL CA  1 
ATOM 16988 C C   . GLY L 3 15  ? 124.357 6.912   -25.028 1.000 53.420  ? 15  GLY LLL C   1 
ATOM 16989 O O   . GLY L 3 15  ? 125.518 7.344   -25.202 1.000 57.600  ? 15  GLY LLL O   1 
ATOM 16990 N N   . GLY L 3 16  ? 123.386 7.614   -24.440 1.000 52.430  ? 16  GLY LLL N   1 
ATOM 16991 C CA  . GLY L 3 16  ? 123.504 9.036   -24.074 1.000 54.310  ? 16  GLY LLL CA  1 
ATOM 16992 C C   . GLY L 3 16  ? 124.385 9.248   -22.856 1.000 52.340  ? 16  GLY LLL C   1 
ATOM 16993 O O   . GLY L 3 16  ? 124.987 8.260   -22.356 1.000 54.950  ? 16  GLY LLL O   1 
ATOM 16994 N N   . SER L 3 17  ? 124.459 10.513  -22.418 1.000 44.980  ? 17  SER LLL N   1 
ATOM 16995 C CA  . SER L 3 17  ? 125.289 10.984  -21.291 1.000 41.050  ? 17  SER LLL CA  1 
ATOM 16996 C C   . SER L 3 17  ? 124.465 11.924  -20.417 1.000 39.560  ? 17  SER LLL C   1 
ATOM 16997 O O   . SER L 3 17  ? 123.404 12.372  -20.848 1.000 39.830  ? 17  SER LLL O   1 
ATOM 16998 C CB  . SER L 3 17  ? 126.540 11.614  -21.792 1.000 42.370  ? 17  SER LLL CB  1 
ATOM 16999 O OG  . SER L 3 17  ? 127.461 10.615  -22.175 1.000 50.100  ? 17  SER LLL OG  1 
ATOM 17000 N N   . LEU L 3 18  ? 124.918 12.144  -19.189 1.000 43.450  ? 18  LEU LLL N   1 
ATOM 17001 C CA  . LEU L 3 18  ? 124.203 12.939  -18.162 1.000 49.030  ? 18  LEU LLL CA  1 
ATOM 17002 C C   . LEU L 3 18  ? 125.113 13.166  -16.959 1.000 49.320  ? 18  LEU LLL C   1 
ATOM 17003 O O   . LEU L 3 18  ? 125.759 12.195  -16.553 1.000 49.900  ? 18  LEU LLL O   1 
ATOM 17004 C CB  . LEU L 3 18  ? 122.936 12.175  -17.780 1.000 50.460  ? 18  LEU LLL CB  1 
ATOM 17005 C CG  . LEU L 3 18  ? 121.821 12.999  -17.115 1.000 55.360  ? 18  LEU LLL CG  1 
ATOM 17006 C CD1 . LEU L 3 18  ? 121.767 14.415  -17.668 1.000 57.890  ? 18  LEU LLL CD1 1 
ATOM 17007 C CD2 . LEU L 3 18  ? 120.481 12.319  -17.272 1.000 61.010  ? 18  LEU LLL CD2 1 
ATOM 17008 N N   . ARG L 3 19  ? 125.170 14.401  -16.443 1.000 46.110  ? 19  ARG LLL N   1 
ATOM 17009 C CA  . ARG L 3 19  ? 125.920 14.756  -15.217 1.000 50.360  ? 19  ARG LLL CA  1 
ATOM 17010 C C   . ARG L 3 19  ? 124.926 15.145  -14.115 1.000 54.250  ? 19  ARG LLL C   1 
ATOM 17011 O O   . ARG L 3 19  ? 124.116 16.068  -14.340 1.000 57.950  ? 19  ARG LLL O   1 
ATOM 17012 C CB  . ARG L 3 19  ? 126.899 15.896  -15.494 1.000 54.930  ? 19  ARG LLL CB  1 
ATOM 17013 C CG  . ARG L 3 19  ? 127.713 16.348  -14.290 1.000 59.900  ? 19  ARG LLL CG  1 
ATOM 17014 C CD  . ARG L 3 19  ? 128.616 17.482  -14.720 1.000 65.120  ? 19  ARG LLL CD  1 
ATOM 17015 N NE  . ARG L 3 19  ? 129.271 18.254  -13.670 1.000 69.720  ? 19  ARG LLL NE  1 
ATOM 17016 C CZ  . ARG L 3 19  ? 130.550 18.140  -13.306 1.000 69.580  ? 19  ARG LLL CZ  1 
ATOM 17017 N NH1 . ARG L 3 19  ? 131.327 17.221  -13.861 1.000 68.380  ? 19  ARG LLL NH1 1 
ATOM 17018 N NH2 . ARG L 3 19  ? 131.044 18.948  -12.380 1.000 67.630  ? 19  ARG LLL NH2 1 
ATOM 17019 N N   . LEU L 3 20  ? 124.996 14.460  -12.970 1.000 51.620  ? 20  LEU LLL N   1 
ATOM 17020 C CA  . LEU L 3 20  ? 124.139 14.715  -11.788 1.000 47.820  ? 20  LEU LLL CA  1 
ATOM 17021 C C   . LEU L 3 20  ? 124.935 15.568  -10.807 1.000 43.370  ? 20  LEU LLL C   1 
ATOM 17022 O O   . LEU L 3 20  ? 126.177 15.449  -10.804 1.000 37.940  ? 20  LEU LLL O   1 
ATOM 17023 C CB  . LEU L 3 20  ? 123.718 13.366  -11.187 1.000 53.320  ? 20  LEU LLL CB  1 
ATOM 17024 C CG  . LEU L 3 20  ? 122.478 12.708  -11.807 1.000 54.090  ? 20  LEU LLL CG  1 
ATOM 17025 C CD1 . LEU L 3 20  ? 122.441 12.861  -13.312 1.000 59.190  ? 20  LEU LLL CD1 1 
ATOM 17026 C CD2 . LEU L 3 20  ? 122.394 11.241  -11.445 1.000 50.460  ? 20  LEU LLL CD2 1 
ATOM 17027 N N   . SER L 3 21  ? 124.228 16.378  -10.024 1.000 43.710  ? 21  SER LLL N   1 
ATOM 17028 C CA  . SER L 3 21  ? 124.791 17.333  -9.037  1.000 47.770  ? 21  SER LLL CA  1 
ATOM 17029 C C   . SER L 3 21  ? 124.120 17.134  -7.674  1.000 46.920  ? 21  SER LLL C   1 
ATOM 17030 O O   . SER L 3 21  ? 122.881 17.113  -7.638  1.000 44.600  ? 21  SER LLL O   1 
ATOM 17031 C CB  . SER L 3 21  ? 124.606 18.748  -9.534  1.000 48.880  ? 21  SER LLL CB  1 
ATOM 17032 O OG  . SER L 3 21  ? 125.546 19.655  -8.980  1.000 52.110  ? 21  SER LLL OG  1 
ATOM 17033 N N   . CYS L 3 22  ? 124.911 17.009  -6.604  1.000 45.630  ? 22  CYS LLL N   1 
ATOM 17034 C CA  . CYS L 3 22  ? 124.437 17.086  -5.192  1.000 43.150  ? 22  CYS LLL CA  1 
ATOM 17035 C C   . CYS L 3 22  ? 124.980 18.367  -4.568  1.000 37.970  ? 22  CYS LLL C   1 
ATOM 17036 O O   . CYS L 3 22  ? 126.193 18.574  -4.639  1.000 36.270  ? 22  CYS LLL O   1 
ATOM 17037 C CB  . CYS L 3 22  ? 124.880 15.896  -4.348  1.000 45.850  ? 22  CYS LLL CB  1 
ATOM 17038 S SG  . CYS L 3 22  ? 123.877 15.674  -2.850  1.000 46.960  ? 22  CYS LLL SG  1 
ATOM 17039 N N   . ALA L 3 23  ? 124.092 19.187  -4.014  1.000 34.820  ? 23  ALA LLL N   1 
ATOM 17040 C CA  . ALA L 3 23  ? 124.427 20.425  -3.295  1.000 35.670  ? 23  ALA LLL CA  1 
ATOM 17041 C C   . ALA L 3 23  ? 124.249 20.164  -1.806  1.000 38.180  ? 23  ALA LLL C   1 
ATOM 17042 O O   . ALA L 3 23  ? 123.092 19.950  -1.375  1.000 39.770  ? 23  ALA LLL O   1 
ATOM 17043 C CB  . ALA L 3 23  ? 123.542 21.547  -3.760  1.000 35.610  ? 23  ALA LLL CB  1 
ATOM 17044 N N   . ALA L 3 24  ? 125.356 20.210  -1.064  1.000 39.720  ? 24  ALA LLL N   1 
ATOM 17045 C CA  . ALA L 3 24  ? 125.409 20.028  0.404   1.000 38.380  ? 24  ALA LLL CA  1 
ATOM 17046 C C   . ALA L 3 24  ? 125.451 21.381  1.128   1.000 35.430  ? 24  ALA LLL C   1 
ATOM 17047 O O   . ALA L 3 24  ? 126.377 22.208  0.843   1.000 33.650  ? 24  ALA LLL O   1 
ATOM 17048 C CB  . ALA L 3 24  ? 126.606 19.187  0.750   1.000 39.890  ? 24  ALA LLL CB  1 
ATOM 17049 N N   . SER L 3 25  ? 124.490 21.585  2.029   1.000 36.000  ? 25  SER LLL N   1 
ATOM 17050 C CA  . SER L 3 25  ? 124.512 22.632  3.084   1.000 39.260  ? 25  SER LLL CA  1 
ATOM 17051 C C   . SER L 3 25  ? 124.285 21.981  4.458   1.000 41.030  ? 25  SER LLL C   1 
ATOM 17052 O O   . SER L 3 25  ? 123.626 20.912  4.524   1.000 49.190  ? 25  SER LLL O   1 
ATOM 17053 C CB  . SER L 3 25  ? 123.463 23.674  2.810   1.000 39.350  ? 25  SER LLL CB  1 
ATOM 17054 O OG  . SER L 3 25  ? 122.159 23.091  2.842   1.000 39.140  ? 25  SER LLL OG  1 
ATOM 17055 N N   . GLY L 3 26  ? 124.774 22.619  5.519   1.000 36.610  ? 26  GLY LLL N   1 
ATOM 17056 C CA  . GLY L 3 26  ? 124.407 22.256  6.900   1.000 37.300  ? 26  GLY LLL CA  1 
ATOM 17057 C C   . GLY L 3 26  ? 125.545 21.603  7.666   1.000 39.010  ? 26  GLY LLL C   1 
ATOM 17058 O O   . GLY L 3 26  ? 125.356 21.296  8.855   1.000 41.450  ? 26  GLY LLL O   1 
ATOM 17059 N N   . PHE L 3 27  ? 126.701 21.404  7.037   1.000 37.280  ? 27  PHE LLL N   1 
ATOM 17060 C CA  . PHE L 3 27  ? 127.829 20.623  7.615   1.000 32.190  ? 27  PHE LLL CA  1 
ATOM 17061 C C   . PHE L 3 27  ? 129.069 20.814  6.766   1.000 28.560  ? 27  PHE LLL C   1 
ATOM 17062 O O   . PHE L 3 27  ? 128.913 21.150  5.606   1.000 30.180  ? 27  PHE LLL O   1 
ATOM 17063 C CB  . PHE L 3 27  ? 127.481 19.135  7.651   1.000 32.500  ? 27  PHE LLL CB  1 
ATOM 17064 C CG  . PHE L 3 27  ? 127.362 18.447  6.313   1.000 31.010  ? 27  PHE LLL CG  1 
ATOM 17065 C CD1 . PHE L 3 27  ? 126.235 18.604  5.539   1.000 32.750  ? 27  PHE LLL CD1 1 
ATOM 17066 C CD2 . PHE L 3 27  ? 128.356 17.586  5.865   1.000 31.030  ? 27  PHE LLL CD2 1 
ATOM 17067 C CE1 . PHE L 3 27  ? 126.092 17.940  4.325   1.000 35.060  ? 27  PHE LLL CE1 1 
ATOM 17068 C CE2 . PHE L 3 27  ? 128.209 16.922  4.653   1.000 34.270  ? 27  PHE LLL CE2 1 
ATOM 17069 C CZ  . PHE L 3 27  ? 127.081 17.102  3.876   1.000 34.390  ? 27  PHE LLL CZ  1 
ATOM 17070 N N   . THR L 3 28  ? 130.251 20.546  7.310   1.000 27.170  ? 28  THR LLL N   1 
ATOM 17071 C CA  . THR L 3 28  ? 131.537 20.576  6.557   1.000 27.350  ? 28  THR LLL CA  1 
ATOM 17072 C C   . THR L 3 28  ? 131.570 19.423  5.546   1.000 27.440  ? 28  THR LLL C   1 
ATOM 17073 O O   . THR L 3 28  ? 132.212 18.410  5.793   1.000 27.940  ? 28  THR LLL O   1 
ATOM 17074 C CB  . THR L 3 28  ? 132.740 20.506  7.492   1.000 27.480  ? 28  THR LLL CB  1 
ATOM 17075 O OG1 . THR L 3 28  ? 132.604 21.631  8.346   1.000 27.820  ? 28  THR LLL OG1 1 
ATOM 17076 C CG2 . THR L 3 28  ? 134.070 20.616  6.797   1.000 28.190  ? 28  THR LLL CG2 1 
ATOM 17077 N N   . PHE L 3 29  ? 130.809 19.545  4.471   1.000 27.260  ? 29  PHE LLL N   1 
ATOM 17078 C CA  . PHE L 3 29  ? 130.816 18.640  3.289   1.000 25.380  ? 29  PHE LLL CA  1 
ATOM 17079 C C   . PHE L 3 29  ? 132.192 18.054  2.998   1.000 24.610  ? 29  PHE LLL C   1 
ATOM 17080 O O   . PHE L 3 29  ? 132.300 16.883  2.668   1.000 22.090  ? 29  PHE LLL O   1 
ATOM 17081 C CB  . PHE L 3 29  ? 130.405 19.425  2.048   1.000 26.330  ? 29  PHE LLL CB  1 
ATOM 17082 C CG  . PHE L 3 29  ? 130.465 18.608  0.787   1.000 26.080  ? 29  PHE LLL CG  1 
ATOM 17083 C CD1 . PHE L 3 29  ? 129.521 17.623  0.540   1.000 26.210  ? 29  PHE LLL CD1 1 
ATOM 17084 C CD2 . PHE L 3 29  ? 131.498 18.775  -0.110  1.000 26.260  ? 29  PHE LLL CD2 1 
ATOM 17085 C CE1 . PHE L 3 29  ? 129.580 16.841  -0.598  1.000 24.060  ? 29  PHE LLL CE1 1 
ATOM 17086 C CE2 . PHE L 3 29  ? 131.551 18.000  -1.260  1.000 26.990  ? 29  PHE LLL CE2 1 
ATOM 17087 C CZ  . PHE L 3 29  ? 130.593 17.031  -1.494  1.000 25.730  ? 29  PHE LLL CZ  1 
ATOM 17088 N N   . SER L 3 30  ? 133.207 18.904  3.082   1.000 26.480  ? 30  SER LLL N   1 
ATOM 17089 C CA  . SER L 3 30  ? 134.606 18.567  2.732   1.000 28.070  ? 30  SER LLL CA  1 
ATOM 17090 C C   . SER L 3 30  ? 135.210 17.558  3.715   1.000 27.160  ? 30  SER LLL C   1 
ATOM 17091 O O   . SER L 3 30  ? 136.379 17.180  3.501   1.000 27.410  ? 30  SER LLL O   1 
ATOM 17092 C CB  . SER L 3 30  ? 135.421 19.817  2.667   1.000 29.760  ? 30  SER LLL CB  1 
ATOM 17093 O OG  . SER L 3 30  ? 135.598 20.352  3.950   1.000 31.150  ? 30  SER LLL OG  1 
ATOM 17094 N N   . SER L 3 31  ? 134.469 17.130  4.741   1.000 29.250  ? 31  SER LLL N   1 
ATOM 17095 C CA  . SER L 3 31  ? 134.964 16.265  5.858   1.000 29.380  ? 31  SER LLL CA  1 
ATOM 17096 C C   . SER L 3 31  ? 134.470 14.820  5.718   1.000 28.050  ? 31  SER LLL C   1 
ATOM 17097 O O   . SER L 3 31  ? 135.047 13.955  6.393   1.000 27.610  ? 31  SER LLL O   1 
ATOM 17098 C CB  . SER L 3 31  ? 134.587 16.818  7.213   1.000 28.210  ? 31  SER LLL CB  1 
ATOM 17099 O OG  . SER L 3 31  ? 135.398 17.933  7.525   1.000 28.770  ? 31  SER LLL OG  1 
ATOM 17100 N N   . TYR L 3 32  ? 133.492 14.576  4.856   1.000 27.990  ? 32  TYR LLL N   1 
ATOM 17101 C CA  . TYR L 3 32  ? 132.709 13.319  4.807   1.000 27.890  ? 32  TYR LLL CA  1 
ATOM 17102 C C   . TYR L 3 32  ? 132.855 12.612  3.458   1.000 26.770  ? 32  TYR LLL C   1 
ATOM 17103 O O   . TYR L 3 32  ? 132.819 13.252  2.427   1.000 27.510  ? 32  TYR LLL O   1 
ATOM 17104 C CB  . TYR L 3 32  ? 131.248 13.653  5.077   1.000 26.770  ? 32  TYR LLL CB  1 
ATOM 17105 C CG  . TYR L 3 32  ? 131.011 14.190  6.462   1.000 27.560  ? 32  TYR LLL CG  1 
ATOM 17106 C CD1 . TYR L 3 32  ? 131.266 15.509  6.781   1.000 27.680  ? 32  TYR LLL CD1 1 
ATOM 17107 C CD2 . TYR L 3 32  ? 130.591 13.349  7.475   1.000 29.590  ? 32  TYR LLL CD2 1 
ATOM 17108 C CE1 . TYR L 3 32  ? 131.067 15.987  8.065   1.000 30.790  ? 32  TYR LLL CE1 1 
ATOM 17109 C CE2 . TYR L 3 32  ? 130.390 13.803  8.768   1.000 28.520  ? 32  TYR LLL CE2 1 
ATOM 17110 C CZ  . TYR L 3 32  ? 130.630 15.122  9.069   1.000 29.490  ? 32  TYR LLL CZ  1 
ATOM 17111 O OH  . TYR L 3 32  ? 130.407 15.494  10.359  1.000 27.790  ? 32  TYR LLL OH  1 
ATOM 17112 N N   . THR L 3 33  ? 132.986 11.295  3.479   1.000 26.850  ? 33  THR LLL N   1 
ATOM 17113 C CA  . THR L 3 33  ? 132.751 10.409  2.312   1.000 26.070  ? 33  THR LLL CA  1 
ATOM 17114 C C   . THR L 3 33  ? 131.302 10.593  1.857   1.000 25.850  ? 33  THR LLL C   1 
ATOM 17115 O O   . THR L 3 33  ? 130.446 10.729  2.715   1.000 26.810  ? 33  THR LLL O   1 
ATOM 17116 C CB  . THR L 3 33  ? 132.973 8.943   2.711   1.000 25.370  ? 33  THR LLL CB  1 
ATOM 17117 O OG1 . THR L 3 33  ? 134.372 8.690   2.760   1.000 26.960  ? 33  THR LLL OG1 1 
ATOM 17118 C CG2 . THR L 3 33  ? 132.318 7.947   1.783   1.000 25.950  ? 33  THR LLL CG2 1 
ATOM 17119 N N   . MET L 3 34  ? 131.043 10.597  0.555   1.000 27.050  ? 34  MET LLL N   1 
ATOM 17120 C CA  . MET L 3 34  ? 129.691 10.806  -0.019  1.000 26.950  ? 34  MET LLL CA  1 
ATOM 17121 C C   . MET L 3 34  ? 129.383 9.682   -1.005  1.000 27.100  ? 34  MET LLL C   1 
ATOM 17122 O O   . MET L 3 34  ? 130.323 9.134   -1.597  1.000 27.590  ? 34  MET LLL O   1 
ATOM 17123 C CB  . MET L 3 34  ? 129.637 12.164  -0.727  1.000 29.630  ? 34  MET LLL CB  1 
ATOM 17124 C CG  . MET L 3 34  ? 129.758 13.372  0.207   1.000 29.260  ? 34  MET LLL CG  1 
ATOM 17125 S SD  . MET L 3 34  ? 128.318 13.589  1.302   1.000 31.550  ? 34  MET LLL SD  1 
ATOM 17126 C CE  . MET L 3 34  ? 126.971 13.568  0.119   1.000 32.080  ? 34  MET LLL CE  1 
ATOM 17127 N N   . ASN L 3 35  ? 128.107 9.357   -1.165  1.000 29.330  ? 35  ASN LLL N   1 
ATOM 17128 C CA  . ASN L 3 35  ? 127.622 8.185   -1.938  1.000 33.040  ? 35  ASN LLL CA  1 
ATOM 17129 C C   . ASN L 3 35  ? 126.547 8.611   -2.955  1.000 35.230  ? 35  ASN LLL C   1 
ATOM 17130 O O   . ASN L 3 35  ? 125.842 9.623   -2.718  1.000 42.470  ? 35  ASN LLL O   1 
ATOM 17131 C CB  . ASN L 3 35  ? 127.091 7.112   -0.982  1.000 32.810  ? 35  ASN LLL CB  1 
ATOM 17132 C CG  . ASN L 3 35  ? 128.198 6.365   -0.278  1.000 34.100  ? 35  ASN LLL CG  1 
ATOM 17133 O OD1 . ASN L 3 35  ? 128.704 5.378   -0.786  1.000 33.230  ? 35  ASN LLL OD1 1 
ATOM 17134 N ND2 . ASN L 3 35  ? 128.595 6.826   0.887   1.000 36.300  ? 35  ASN LLL ND2 1 
ATOM 17135 N N   . TRP L 3 36  ? 126.426 7.860   -4.048  1.000 33.010  ? 36  TRP LLL N   1 
ATOM 17136 C CA  . TRP L 3 36  ? 125.230 7.841   -4.935  1.000 34.530  ? 36  TRP LLL CA  1 
ATOM 17137 C C   . TRP L 3 36  ? 124.559 6.477   -4.778  1.000 35.080  ? 36  TRP LLL C   1 
ATOM 17138 O O   . TRP L 3 36  ? 125.281 5.471   -4.863  1.000 31.950  ? 36  TRP LLL O   1 
ATOM 17139 C CB  . TRP L 3 36  ? 125.616 8.097   -6.411  1.000 33.300  ? 36  TRP LLL CB  1 
ATOM 17140 C CG  . TRP L 3 36  ? 126.076 9.488   -6.705  1.000 26.580  ? 36  TRP LLL CG  1 
ATOM 17141 C CD1 . TRP L 3 36  ? 127.357 9.920   -6.834  1.000 25.120  ? 36  TRP LLL CD1 1 
ATOM 17142 C CD2 . TRP L 3 36  ? 125.242 10.634  -6.885  1.000 25.310  ? 36  TRP LLL CD2 1 
ATOM 17143 N NE1 . TRP L 3 36  ? 127.379 11.261  -7.069  1.000 24.920  ? 36  TRP LLL NE1 1 
ATOM 17144 C CE2 . TRP L 3 36  ? 126.096 11.725  -7.108  1.000 25.900  ? 36  TRP LLL CE2 1 
ATOM 17145 C CE3 . TRP L 3 36  ? 123.862 10.845  -6.883  1.000 26.790  ? 36  TRP LLL CE3 1 
ATOM 17146 C CZ2 . TRP L 3 36  ? 125.611 13.012  -7.321  1.000 28.700  ? 36  TRP LLL CZ2 1 
ATOM 17147 C CZ3 . TRP L 3 36  ? 123.379 12.117  -7.098  1.000 28.270  ? 36  TRP LLL CZ3 1 
ATOM 17148 C CH2 . TRP L 3 36  ? 124.244 13.189  -7.312  1.000 28.770  ? 36  TRP LLL CH2 1 
ATOM 17149 N N   . VAL L 3 37  ? 123.250 6.460   -4.545  1.000 38.300  ? 37  VAL LLL N   1 
ATOM 17150 C CA  . VAL L 3 37  ? 122.423 5.220   -4.501  1.000 43.050  ? 37  VAL LLL CA  1 
ATOM 17151 C C   . VAL L 3 37  ? 121.225 5.463   -5.412  1.000 42.370  ? 37  VAL LLL C   1 
ATOM 17152 O O   . VAL L 3 37  ? 120.686 6.587   -5.366  1.000 39.400  ? 37  VAL LLL O   1 
ATOM 17153 C CB  . VAL L 3 37  ? 121.971 4.903   -3.063  1.000 47.000  ? 37  VAL LLL CB  1 
ATOM 17154 C CG1 . VAL L 3 37  ? 121.078 3.685   -2.992  1.000 45.960  ? 37  VAL LLL CG1 1 
ATOM 17155 C CG2 . VAL L 3 37  ? 123.146 4.727   -2.126  1.000 50.740  ? 37  VAL LLL CG2 1 
ATOM 17156 N N   . ARG L 3 38  ? 120.821 4.466   -6.191  1.000 42.420  ? 38  ARG LLL N   1 
ATOM 17157 C CA  . ARG L 3 38  ? 119.687 4.646   -7.137  1.000 46.020  ? 38  ARG LLL CA  1 
ATOM 17158 C C   . ARG L 3 38  ? 118.582 3.637   -6.847  1.000 47.220  ? 38  ARG LLL C   1 
ATOM 17159 O O   . ARG L 3 38  ? 118.867 2.615   -6.208  1.000 46.530  ? 38  ARG LLL O   1 
ATOM 17160 C CB  . ARG L 3 38  ? 120.131 4.499   -8.586  1.000 47.460  ? 38  ARG LLL CB  1 
ATOM 17161 C CG  . ARG L 3 38  ? 120.563 3.099   -8.961  1.000 49.840  ? 38  ARG LLL CG  1 
ATOM 17162 C CD  . ARG L 3 38  ? 120.981 3.037   -10.410 1.000 49.990  ? 38  ARG LLL CD  1 
ATOM 17163 N NE  . ARG L 3 38  ? 121.687 1.806   -10.683 1.000 50.600  ? 38  ARG LLL NE  1 
ATOM 17164 C CZ  . ARG L 3 38  ? 122.174 1.482   -11.862 1.000 54.950  ? 38  ARG LLL CZ  1 
ATOM 17165 N NH1 . ARG L 3 38  ? 122.042 2.313   -12.884 1.000 60.200  ? 38  ARG LLL NH1 1 
ATOM 17166 N NH2 . ARG L 3 38  ? 122.797 0.328   -12.013 1.000 57.900  ? 38  ARG LLL NH2 1 
ATOM 17167 N N   . GLN L 3 39  ? 117.373 3.951   -7.311  1.000 50.390  ? 39  GLN LLL N   1 
ATOM 17168 C CA  . GLN L 3 39  ? 116.128 3.187   -7.033  1.000 51.440  ? 39  GLN LLL CA  1 
ATOM 17169 C C   . GLN L 3 39  ? 115.290 3.115   -8.311  1.000 50.880  ? 39  GLN LLL C   1 
ATOM 17170 O O   . GLN L 3 39  ? 114.612 4.109   -8.644  1.000 51.220  ? 39  GLN LLL O   1 
ATOM 17171 C CB  . GLN L 3 39  ? 115.334 3.836   -5.896  1.000 47.030  ? 39  GLN LLL CB  1 
ATOM 17172 C CG  . GLN L 3 39  ? 114.279 2.911   -5.321  1.000 46.770  ? 39  GLN LLL CG  1 
ATOM 17173 C CD  . GLN L 3 39  ? 113.683 3.427   -4.043  1.000 46.940  ? 39  GLN LLL CD  1 
ATOM 17174 O OE1 . GLN L 3 39  ? 113.601 4.635   -3.842  1.000 45.570  ? 39  GLN LLL OE1 1 
ATOM 17175 N NE2 . GLN L 3 39  ? 113.239 2.497   -3.200  1.000 46.810  ? 39  GLN LLL NE2 1 
ATOM 17176 N N   . ALA L 3 40  ? 115.338 1.964   -8.984  1.000 50.410  ? 40  ALA LLL N   1 
ATOM 17177 C CA  . ALA L 3 40  ? 114.604 1.702   -10.239 1.000 55.150  ? 40  ALA LLL CA  1 
ATOM 17178 C C   . ALA L 3 40  ? 113.119 1.610   -9.902  1.000 58.040  ? 40  ALA LLL C   1 
ATOM 17179 O O   . ALA L 3 40  ? 112.752 1.122   -8.834  1.000 52.000  ? 40  ALA LLL O   1 
ATOM 17180 C CB  . ALA L 3 40  ? 115.131 0.451   -10.890 1.000 55.360  ? 40  ALA LLL CB  1 
ATOM 17181 N N   . PRO L 3 41  ? 112.211 2.077   -10.791 1.000 67.700  ? 41  PRO LLL N   1 
ATOM 17182 C CA  . PRO L 3 41  ? 110.810 2.241   -10.408 1.000 66.170  ? 41  PRO LLL CA  1 
ATOM 17183 C C   . PRO L 3 41  ? 110.280 0.871   -9.952  1.000 65.650  ? 41  PRO LLL C   1 
ATOM 17184 O O   . PRO L 3 41  ? 110.486 -0.109  -10.678 1.000 58.090  ? 41  PRO LLL O   1 
ATOM 17185 C CB  . PRO L 3 41  ? 110.124 2.762   -11.677 1.000 67.930  ? 41  PRO LLL CB  1 
ATOM 17186 C CG  . PRO L 3 41  ? 111.263 3.300   -12.536 1.000 71.410  ? 41  PRO LLL CG  1 
ATOM 17187 C CD  . PRO L 3 41  ? 112.456 2.422   -12.208 1.000 69.740  ? 41  PRO LLL CD  1 
ATOM 17188 N N   . GLY L 3 42  ? 109.710 0.824   -8.741  1.000 60.690  ? 42  GLY LLL N   1 
ATOM 17189 C CA  . GLY L 3 42  ? 109.031 -0.365  -8.194  1.000 58.180  ? 42  GLY LLL CA  1 
ATOM 17190 C C   . GLY L 3 42  ? 109.985 -1.303  -7.479  1.000 62.050  ? 42  GLY LLL C   1 
ATOM 17191 O O   . GLY L 3 42  ? 109.472 -2.103  -6.658  1.000 63.890  ? 42  GLY LLL O   1 
ATOM 17192 N N   . LYS L 3 43  ? 111.296 -1.219  -7.767  1.000 60.520  ? 43  LYS LLL N   1 
ATOM 17193 C CA  . LYS L 3 43  ? 112.367 -2.058  -7.152  1.000 54.590  ? 43  LYS LLL CA  1 
ATOM 17194 C C   . LYS L 3 43  ? 112.901 -1.350  -5.880  1.000 53.120  ? 43  LYS LLL C   1 
ATOM 17195 O O   . LYS L 3 43  ? 112.446 -0.229  -5.524  1.000 40.270  ? 43  LYS LLL O   1 
ATOM 17196 C CB  . LYS L 3 43  ? 113.422 -2.422  -8.215  1.000 43.070  ? 43  LYS LLL CB  1 
ATOM 17197 N N   . GLY L 3 44  ? 113.811 -2.017  -5.163  1.000 56.200  ? 44  GLY LLL N   1 
ATOM 17198 C CA  . GLY L 3 44  ? 114.455 -1.493  -3.943  1.000 52.430  ? 44  GLY LLL CA  1 
ATOM 17199 C C   . GLY L 3 44  ? 115.650 -0.625  -4.287  1.000 50.750  ? 44  GLY LLL C   1 
ATOM 17200 O O   . GLY L 3 44  ? 115.697 -0.100  -5.414  1.000 53.240  ? 44  GLY LLL O   1 
ATOM 17201 N N   . LEU L 3 45  ? 116.565 -0.425  -3.333  1.000 48.350  ? 45  LEU LLL N   1 
ATOM 17202 C CA  . LEU L 3 45  ? 117.728 0.489   -3.470  1.000 45.760  ? 45  LEU LLL CA  1 
ATOM 17203 C C   . LEU L 3 45  ? 118.913 -0.270  -4.056  1.000 42.490  ? 45  LEU LLL C   1 
ATOM 17204 O O   . LEU L 3 45  ? 118.924 -1.489  -3.919  1.000 56.460  ? 45  LEU LLL O   1 
ATOM 17205 C CB  . LEU L 3 45  ? 118.056 1.046   -2.084  1.000 46.440  ? 45  LEU LLL CB  1 
ATOM 17206 C CG  . LEU L 3 45  ? 117.041 2.051   -1.552  1.000 48.250  ? 45  LEU LLL CG  1 
ATOM 17207 C CD1 . LEU L 3 45  ? 117.386 2.471   -0.126  1.000 46.100  ? 45  LEU LLL CD1 1 
ATOM 17208 C CD2 . LEU L 3 45  ? 116.977 3.258   -2.490  1.000 53.350  ? 45  LEU LLL CD2 1 
ATOM 17209 N N   . GLN L 3 46  ? 119.862 0.429   -4.675  1.000 35.690  ? 46  GLN LLL N   1 
ATOM 17210 C CA  . GLN L 3 46  ? 121.114 -0.156  -5.227  1.000 33.420  ? 46  GLN LLL CA  1 
ATOM 17211 C C   . GLN L 3 46  ? 122.202 0.918   -5.236  1.000 36.970  ? 46  GLN LLL C   1 
ATOM 17212 O O   . GLN L 3 46  ? 122.058 1.953   -5.934  1.000 39.210  ? 46  GLN LLL O   1 
ATOM 17213 C CB  . GLN L 3 46  ? 120.917 -0.702  -6.641  1.000 29.300  ? 46  GLN LLL CB  1 
ATOM 17214 C CG  . GLN L 3 46  ? 122.178 -1.262  -7.274  1.000 27.510  ? 46  GLN LLL CG  1 
ATOM 17215 C CD  . GLN L 3 46  ? 122.051 -1.477  -8.762  1.000 27.200  ? 46  GLN LLL CD  1 
ATOM 17216 O OE1 . GLN L 3 46  ? 121.524 -0.667  -9.513  1.000 26.570  ? 46  GLN LLL OE1 1 
ATOM 17217 N NE2 . GLN L 3 46  ? 122.579 -2.590  -9.218  1.000 28.380  ? 46  GLN LLL NE2 1 
ATOM 17218 N N   . TRP L 3 47  ? 123.261 0.685   -4.470  1.000 41.620  ? 47  TRP LLL N   1 
ATOM 17219 C CA  . TRP L 3 47  ? 124.419 1.609   -4.353  1.000 40.450  ? 47  TRP LLL CA  1 
ATOM 17220 C C   . TRP L 3 47  ? 125.117 1.717   -5.711  1.000 41.100  ? 47  TRP LLL C   1 
ATOM 17221 O O   . TRP L 3 47  ? 125.278 0.686   -6.385  1.000 41.740  ? 47  TRP LLL O   1 
ATOM 17222 C CB  . TRP L 3 47  ? 125.381 1.129   -3.272  1.000 36.300  ? 47  TRP LLL CB  1 
ATOM 17223 C CG  . TRP L 3 47  ? 126.667 1.883   -3.239  1.000 33.500  ? 47  TRP LLL CG  1 
ATOM 17224 C CD1 . TRP L 3 47  ? 126.875 3.130   -2.727  1.000 33.830  ? 47  TRP LLL CD1 1 
ATOM 17225 C CD2 . TRP L 3 47  ? 127.937 1.423   -3.714  1.000 30.960  ? 47  TRP LLL CD2 1 
ATOM 17226 N NE1 . TRP L 3 47  ? 128.191 3.481   -2.860  1.000 32.650  ? 47  TRP LLL NE1 1 
ATOM 17227 C CE2 . TRP L 3 47  ? 128.870 2.447   -3.453  1.000 32.760  ? 47  TRP LLL CE2 1 
ATOM 17228 C CE3 . TRP L 3 47  ? 128.379 0.248   -4.307  1.000 31.540  ? 47  TRP LLL CE3 1 
ATOM 17229 C CZ2 . TRP L 3 47  ? 130.221 2.328   -3.775  1.000 33.240  ? 47  TRP LLL CZ2 1 
ATOM 17230 C CZ3 . TRP L 3 47  ? 129.716 0.129   -4.620  1.000 34.160  ? 47  TRP LLL CZ3 1 
ATOM 17231 C CH2 . TRP L 3 47  ? 130.624 1.155   -4.360  1.000 33.480  ? 47  TRP LLL CH2 1 
ATOM 17232 N N   . VAL L 3 48  ? 125.540 2.929   -6.064  1.000 39.430  ? 48  VAL LLL N   1 
ATOM 17233 C CA  . VAL L 3 48  ? 126.156 3.257   -7.372  1.000 37.790  ? 48  VAL LLL CA  1 
ATOM 17234 C C   . VAL L 3 48  ? 127.651 3.474   -7.160  1.000 40.110  ? 48  VAL LLL C   1 
ATOM 17235 O O   . VAL L 3 48  ? 128.447 2.782   -7.824  1.000 40.100  ? 48  VAL LLL O   1 
ATOM 17236 C CB  . VAL L 3 48  ? 125.506 4.510   -7.972  1.000 38.500  ? 48  VAL LLL CB  1 
ATOM 17237 C CG1 . VAL L 3 48  ? 126.353 5.093   -9.089  1.000 37.100  ? 48  VAL LLL CG1 1 
ATOM 17238 C CG2 . VAL L 3 48  ? 124.089 4.244   -8.438  1.000 42.570  ? 48  VAL LLL CG2 1 
ATOM 17239 N N   . SER L 3 49  ? 128.017 4.428   -6.298  1.000 36.810  ? 49  SER LLL N   1 
ATOM 17240 C CA  . SER L 3 49  ? 129.420 4.863   -6.151  1.000 34.550  ? 49  SER LLL CA  1 
ATOM 17241 C C   . SER L 3 49  ? 129.660 5.615   -4.839  1.000 36.430  ? 49  SER LLL C   1 
ATOM 17242 O O   . SER L 3 49  ? 128.737 6.303   -4.356  1.000 33.030  ? 49  SER LLL O   1 
ATOM 17243 C CB  . SER L 3 49  ? 129.835 5.669   -7.347  1.000 34.420  ? 49  SER LLL CB  1 
ATOM 17244 O OG  . SER L 3 49  ? 131.201 6.024   -7.281  1.000 32.880  ? 49  SER LLL OG  1 
ATOM 17245 N N   . SER L 3 50  ? 130.869 5.452   -4.287  1.000 36.990  ? 50  SER LLL N   1 
ATOM 17246 C CA  . SER L 3 50  ? 131.402 6.168   -3.100  1.000 34.770  ? 50  SER LLL CA  1 
ATOM 17247 C C   . SER L 3 50  ? 132.612 7.013   -3.469  1.000 33.740  ? 50  SER LLL C   1 
ATOM 17248 O O   . SER L 3 50  ? 133.389 6.603   -4.355  1.000 36.710  ? 50  SER LLL O   1 
ATOM 17249 C CB  . SER L 3 50  ? 131.834 5.197   -2.045  1.000 37.720  ? 50  SER LLL CB  1 
ATOM 17250 O OG  . SER L 3 50  ? 132.366 5.898   -0.917  1.000 42.580  ? 50  SER LLL OG  1 
ATOM 17251 N N   . ILE L 3 51  ? 132.819 8.112   -2.747  1.000 30.720  ? 51  ILE LLL N   1 
ATOM 17252 C CA  . ILE L 3 51  ? 134.049 8.936   -2.885  1.000 29.240  ? 51  ILE LLL CA  1 
ATOM 17253 C C   . ILE L 3 51  ? 134.448 9.432   -1.502  1.000 26.970  ? 51  ILE LLL C   1 
ATOM 17254 O O   . ILE L 3 51  ? 133.570 9.938   -0.800  1.000 24.480  ? 51  ILE LLL O   1 
ATOM 17255 C CB  . ILE L 3 51  ? 133.881 10.086  -3.892  1.000 29.940  ? 51  ILE LLL CB  1 
ATOM 17256 C CG1 . ILE L 3 51  ? 135.211 10.807  -4.120  1.000 29.710  ? 51  ILE LLL CG1 1 
ATOM 17257 C CG2 . ILE L 3 51  ? 132.768 11.035  -3.459  1.000 29.180  ? 51  ILE LLL CG2 1 
ATOM 17258 C CD1 . ILE L 3 51  ? 135.192 11.745  -5.290  1.000 31.180  ? 51  ILE LLL CD1 1 
ATOM 17259 N N   . SER L 3 52  ? 135.737 9.313   -1.167  1.000 26.180  ? 52  SER LLL N   1 
ATOM 17260 C CA  . SER L 3 52  ? 136.327 9.781   0.111   1.000 27.110  ? 52  SER LLL CA  1 
ATOM 17261 C C   . SER L 3 52  ? 136.283 11.315  0.188   1.000 30.370  ? 52  SER LLL C   1 
ATOM 17262 O O   . SER L 3 52  ? 136.018 11.961  -0.838  1.000 29.370  ? 52  SER LLL O   1 
ATOM 17263 C CB  . SER L 3 52  ? 137.724 9.214   0.323   1.000 26.210  ? 52  SER LLL CB  1 
ATOM 17264 O OG  . SER L 3 52  ? 138.741 9.824   -0.473  1.000 26.510  ? 52  SER LLL OG  1 
ATOM 17265 N N   . SER L 3 53  ? 136.502 11.877  1.379   1.000 33.500  ? 53  SER LLL N   1 
ATOM 17266 C CA  . SER L 3 53  ? 136.521 13.341  1.622   1.000 34.010  ? 53  SER LLL CA  1 
ATOM 17267 C C   . SER L 3 53  ? 137.459 14.029  0.616   1.000 33.340  ? 53  SER LLL C   1 
ATOM 17268 O O   . SER L 3 53  ? 137.073 15.082  0.102   1.000 38.940  ? 53  SER LLL O   1 
ATOM 17269 C CB  . SER L 3 53  ? 136.900 13.650  3.068   1.000 36.620  ? 53  SER LLL CB  1 
ATOM 17270 O OG  . SER L 3 53  ? 138.316 13.506  3.299   1.000 36.290  ? 53  SER LLL OG  1 
ATOM 17271 N N   . SER L 3 54  ? 138.639 13.469  0.347   1.000 34.040  ? 54  SER LLL N   1 
ATOM 17272 C CA  . SER L 3 54  ? 139.709 14.120  -0.449  1.000 38.620  ? 54  SER LLL CA  1 
ATOM 17273 C C   . SER L 3 54  ? 139.793 13.511  -1.845  1.000 41.950  ? 54  SER LLL C   1 
ATOM 17274 O O   . SER L 3 54  ? 140.765 13.795  -2.580  1.000 51.750  ? 54  SER LLL O   1 
ATOM 17275 C CB  . SER L 3 54  ? 141.021 14.027  0.250   1.000 43.480  ? 54  SER LLL CB  1 
ATOM 17276 O OG  . SER L 3 54  ? 141.245 15.210  0.988   1.000 53.500  ? 54  SER LLL OG  1 
ATOM 17277 N N   . SER L 3 55  ? 138.828 12.667  -2.191  1.000 40.180  ? 55  SER LLL N   1 
ATOM 17278 C CA  . SER L 3 55  ? 138.741 12.021  -3.522  1.000 34.700  ? 55  SER LLL CA  1 
ATOM 17279 C C   . SER L 3 55  ? 139.951 11.100  -3.724  1.000 33.860  ? 55  SER LLL C   1 
ATOM 17280 O O   . SER L 3 55  ? 140.276 10.817  -4.889  1.000 39.120  ? 55  SER LLL O   1 
ATOM 17281 C CB  . SER L 3 55  ? 138.615 13.093  -4.586  1.000 33.670  ? 55  SER LLL CB  1 
ATOM 17282 O OG  . SER L 3 55  ? 137.908 14.243  -4.077  1.000 31.400  ? 55  SER LLL OG  1 
ATOM 17283 N N   . THR L 3 56  ? 140.568 10.605  -2.637  1.000 30.880  ? 56  THR LLL N   1 
ATOM 17284 C CA  . THR L 3 56  ? 141.622 9.547   -2.681  1.000 30.470  ? 56  THR LLL CA  1 
ATOM 17285 C C   . THR L 3 56  ? 141.013 8.181   -2.991  1.000 31.090  ? 56  THR LLL C   1 
ATOM 17286 O O   . THR L 3 56  ? 141.720 7.380   -3.572  1.000 37.550  ? 56  THR LLL O   1 
ATOM 17287 C CB  . THR L 3 56  ? 142.383 9.336   -1.373  1.000 29.000  ? 56  THR LLL CB  1 
ATOM 17288 O OG1 . THR L 3 56  ? 142.988 10.604  -1.157  1.000 31.960  ? 56  THR LLL OG1 1 
ATOM 17289 N N   . TYR L 3 57  ? 139.789 7.885   -2.562  1.000 29.810  ? 57  TYR LLL N   1 
ATOM 17290 C CA  . TYR L 3 57  ? 139.173 6.549   -2.762  1.000 29.500  ? 57  TYR LLL CA  1 
ATOM 17291 C C   . TYR L 3 57  ? 137.780 6.697   -3.386  1.000 31.530  ? 57  TYR LLL C   1 
ATOM 17292 O O   . TYR L 3 57  ? 136.806 7.093   -2.698  1.000 33.720  ? 57  TYR LLL O   1 
ATOM 17293 C CB  . TYR L 3 57  ? 139.142 5.766   -1.443  1.000 29.810  ? 57  TYR LLL CB  1 
ATOM 17294 C CG  . TYR L 3 57  ? 140.499 5.476   -0.856  1.000 30.310  ? 57  TYR LLL CG  1 
ATOM 17295 C CD1 . TYR L 3 57  ? 141.231 6.438   -0.179  1.000 33.200  ? 57  TYR LLL CD1 1 
ATOM 17296 C CD2 . TYR L 3 57  ? 141.055 4.218   -0.972  1.000 31.690  ? 57  TYR LLL CD2 1 
ATOM 17297 C CE1 . TYR L 3 57  ? 142.491 6.163   0.330   1.000 34.800  ? 57  TYR LLL CE1 1 
ATOM 17298 C CE2 . TYR L 3 57  ? 142.306 3.912   -0.461  1.000 33.200  ? 57  TYR LLL CE2 1 
ATOM 17299 C CZ  . TYR L 3 57  ? 143.025 4.890   0.192   1.000 34.610  ? 57  TYR LLL CZ  1 
ATOM 17300 O OH  . TYR L 3 57  ? 144.270 4.582   0.647   1.000 37.430  ? 57  TYR LLL OH  1 
ATOM 17301 N N   . MET L 3 58  ? 137.682 6.353   -4.665  1.000 33.450  ? 58  MET LLL N   1 
ATOM 17302 C CA  . MET L 3 58  ? 136.388 6.183   -5.362  1.000 35.000  ? 58  MET LLL CA  1 
ATOM 17303 C C   . MET L 3 58  ? 136.137 4.679   -5.512  1.000 36.830  ? 58  MET LLL C   1 
ATOM 17304 O O   . MET L 3 58  ? 137.094 3.949   -5.787  1.000 38.190  ? 58  MET LLL O   1 
ATOM 17305 C CB  . MET L 3 58  ? 136.426 6.866   -6.732  1.000 36.850  ? 58  MET LLL CB  1 
ATOM 17306 C CG  . MET L 3 58  ? 136.318 8.373   -6.641  1.000 35.740  ? 58  MET LLL CG  1 
ATOM 17307 S SD  . MET L 3 58  ? 137.868 9.156   -6.265  1.000 39.590  ? 58  MET LLL SD  1 
ATOM 17308 C CE  . MET L 3 58  ? 138.620 9.062   -7.895  1.000 40.210  ? 58  MET LLL CE  1 
ATOM 17309 N N   . TYR L 3 59  ? 134.905 4.239   -5.284  1.000 38.270  ? 59  TYR LLL N   1 
ATOM 17310 C CA  . TYR L 3 59  ? 134.441 2.845   -5.496  1.000 36.120  ? 59  TYR LLL CA  1 
ATOM 17311 C C   . TYR L 3 59  ? 133.168 2.889   -6.317  1.000 34.760  ? 59  TYR LLL C   1 
ATOM 17312 O O   . TYR L 3 59  ? 132.369 3.848   -6.163  1.000 29.840  ? 59  TYR LLL O   1 
ATOM 17313 C CB  . TYR L 3 59  ? 134.131 2.155   -4.164  1.000 36.860  ? 59  TYR LLL CB  1 
ATOM 17314 C CG  . TYR L 3 59  ? 135.306 2.021   -3.245  1.000 34.650  ? 59  TYR LLL CG  1 
ATOM 17315 C CD1 . TYR L 3 59  ? 136.254 1.042   -3.465  1.000 36.470  ? 59  TYR LLL CD1 1 
ATOM 17316 C CD2 . TYR L 3 59  ? 135.472 2.864   -2.167  1.000 34.890  ? 59  TYR LLL CD2 1 
ATOM 17317 C CE1 . TYR L 3 59  ? 137.360 0.911   -2.647  1.000 35.870  ? 59  TYR LLL CE1 1 
ATOM 17318 C CE2 . TYR L 3 59  ? 136.569 2.735   -1.328  1.000 36.150  ? 59  TYR LLL CE2 1 
ATOM 17319 C CZ  . TYR L 3 59  ? 137.509 1.748   -1.563  1.000 34.330  ? 59  TYR LLL CZ  1 
ATOM 17320 O OH  . TYR L 3 59  ? 138.598 1.590   -0.763  1.000 35.330  ? 59  TYR LLL OH  1 
ATOM 17321 N N   . TYR L 3 60  ? 132.949 1.866   -7.138  1.000 35.030  ? 60  TYR LLL N   1 
ATOM 17322 C CA  . TYR L 3 60  ? 131.733 1.768   -7.981  1.000 34.420  ? 60  TYR LLL CA  1 
ATOM 17323 C C   . TYR L 3 60  ? 131.141 0.375   -7.813  1.000 34.310  ? 60  TYR LLL C   1 
ATOM 17324 O O   . TYR L 3 60  ? 131.905 -0.591  -7.667  1.000 31.900  ? 60  TYR LLL O   1 
ATOM 17325 C CB  . TYR L 3 60  ? 132.050 2.082   -9.447  1.000 30.890  ? 60  TYR LLL CB  1 
ATOM 17326 C CG  . TYR L 3 60  ? 132.739 3.406   -9.667  1.000 28.920  ? 60  TYR LLL CG  1 
ATOM 17327 C CD1 . TYR L 3 60  ? 134.111 3.510   -9.516  1.000 29.290  ? 60  TYR LLL CD1 1 
ATOM 17328 C CD2 . TYR L 3 60  ? 132.041 4.550   -10.011 1.000 26.900  ? 60  TYR LLL CD2 1 
ATOM 17329 C CE1 . TYR L 3 60  ? 134.780 4.707   -9.712  1.000 28.500  ? 60  TYR LLL CE1 1 
ATOM 17330 C CE2 . TYR L 3 60  ? 132.691 5.759   -10.196 1.000 26.920  ? 60  TYR LLL CE2 1 
ATOM 17331 C CZ  . TYR L 3 60  ? 134.065 5.844   -10.037 1.000 27.750  ? 60  TYR LLL CZ  1 
ATOM 17332 O OH  . TYR L 3 60  ? 134.737 7.018   -10.233 1.000 24.620  ? 60  TYR LLL OH  1 
ATOM 17333 N N   . GLY L 3 61  ? 129.810 0.310   -7.822  1.000 34.890  ? 61  GLY LLL N   1 
ATOM 17334 C CA  . GLY L 3 61  ? 129.063 -0.935  -8.055  1.000 37.690  ? 61  GLY LLL CA  1 
ATOM 17335 C C   . GLY L 3 61  ? 129.455 -1.538  -9.381  1.000 37.870  ? 61  GLY LLL C   1 
ATOM 17336 O O   . GLY L 3 61  ? 129.827 -0.774  -10.262 1.000 38.630  ? 61  GLY LLL O   1 
ATOM 17337 N N   . ASP L 3 62  ? 129.374 -2.859  -9.497  1.000 39.270  ? 62  ASP LLL N   1 
ATOM 17338 C CA  . ASP L 3 62  ? 129.694 -3.611  -10.731 1.000 44.700  ? 62  ASP LLL CA  1 
ATOM 17339 C C   . ASP L 3 62  ? 128.738 -3.041  -11.792 1.000 40.080  ? 62  ASP LLL C   1 
ATOM 17340 O O   . ASP L 3 62  ? 129.174 -2.795  -12.923 1.000 42.770  ? 62  ASP LLL O   1 
ATOM 17341 C CB  . ASP L 3 62  ? 129.481 -5.110  -10.478 1.000 50.140  ? 62  ASP LLL CB  1 
ATOM 17342 C CG  . ASP L 3 62  ? 130.380 -6.004  -11.291 1.000 55.400  ? 62  ASP LLL CG  1 
ATOM 17343 O OD1 . ASP L 3 62  ? 131.609 -5.969  -11.029 1.000 67.570  ? 62  ASP LLL OD1 1 
ATOM 17344 O OD2 . ASP L 3 62  ? 129.850 -6.714  -12.183 1.000 59.240  ? 62  ASP LLL OD2 1 
ATOM 17345 N N   . SER L 3 63  ? 127.490 -2.794  -11.405 1.000 36.660  ? 63  SER LLL N   1 
ATOM 17346 C CA  . SER L 3 63  ? 126.396 -2.384  -12.313 1.000 37.650  ? 63  SER LLL CA  1 
ATOM 17347 C C   . SER L 3 63  ? 126.858 -1.287  -13.313 1.000 42.690  ? 63  SER LLL C   1 
ATOM 17348 O O   . SER L 3 63  ? 126.452 -1.295  -14.469 1.000 44.090  ? 63  SER LLL O   1 
ATOM 17349 C CB  . SER L 3 63  ? 125.183 -2.022  -11.527 1.000 34.780  ? 63  SER LLL CB  1 
ATOM 17350 O OG  . SER L 3 63  ? 124.678 -3.153  -10.825 1.000 32.280  ? 63  SER LLL OG  1 
ATOM 17351 N N   . VAL L 3 64  ? 127.705 -0.369  -12.857 1.000 44.560  ? 64  VAL LLL N   1 
ATOM 17352 C CA  . VAL L 3 64  ? 128.165 0.777   -13.699 1.000 39.640  ? 64  VAL LLL CA  1 
ATOM 17353 C C   . VAL L 3 64  ? 129.678 0.896   -13.840 1.000 36.110  ? 64  VAL LLL C   1 
ATOM 17354 O O   . VAL L 3 64  ? 130.085 1.960   -14.292 1.000 35.730  ? 64  VAL LLL O   1 
ATOM 17355 C CB  . VAL L 3 64  ? 127.596 2.030   -12.991 1.000 38.200  ? 64  VAL LLL CB  1 
ATOM 17356 C CG1 . VAL L 3 64  ? 126.093 1.945   -12.806 1.000 39.670  ? 64  VAL LLL CG1 1 
ATOM 17357 C CG2 . VAL L 3 64  ? 128.262 2.276   -11.654 1.000 37.870  ? 64  VAL LLL CG2 1 
ATOM 17358 N N   . LYS L 3 65  ? 130.478 -0.095  -13.428 1.000 37.960  ? 65  LYS LLL N   1 
ATOM 17359 C CA  . LYS L 3 65  ? 131.969 -0.060  -13.542 1.000 39.110  ? 65  LYS LLL CA  1 
ATOM 17360 C C   . LYS L 3 65  ? 132.305 0.368   -14.972 1.000 42.790  ? 65  LYS LLL C   1 
ATOM 17361 O O   . LYS L 3 65  ? 131.714 -0.185  -15.908 1.000 52.140  ? 65  LYS LLL O   1 
ATOM 17362 C CB  . LYS L 3 65  ? 132.624 -1.413  -13.236 1.000 35.610  ? 65  LYS LLL CB  1 
ATOM 17363 N N   . GLY L 3 66  ? 133.156 1.365   -15.144 1.000 41.630  ? 66  GLY LLL N   1 
ATOM 17364 C CA  . GLY L 3 66  ? 133.642 1.730   -16.485 1.000 41.710  ? 66  GLY LLL CA  1 
ATOM 17365 C C   . GLY L 3 66  ? 132.776 2.739   -17.209 1.000 38.490  ? 66  GLY LLL C   1 
ATOM 17366 O O   . GLY L 3 66  ? 133.267 3.294   -18.181 1.000 42.280  ? 66  GLY LLL O   1 
ATOM 17367 N N   . ARG L 3 67  ? 131.540 2.992   -16.762 1.000 36.060  ? 67  ARG LLL N   1 
ATOM 17368 C CA  . ARG L 3 67  ? 130.602 3.903   -17.457 1.000 36.980  ? 67  ARG LLL CA  1 
ATOM 17369 C C   . ARG L 3 67  ? 130.387 5.186   -16.645 1.000 36.930  ? 67  ARG LLL C   1 
ATOM 17370 O O   . ARG L 3 67  ? 130.407 6.292   -17.244 1.000 44.200  ? 67  ARG LLL O   1 
ATOM 17371 C CB  . ARG L 3 67  ? 129.269 3.201   -17.721 1.000 36.760  ? 67  ARG LLL CB  1 
ATOM 17372 C CG  . ARG L 3 67  ? 129.426 1.893   -18.488 1.000 38.800  ? 67  ARG LLL CG  1 
ATOM 17373 C CD  . ARG L 3 67  ? 128.123 1.314   -19.011 1.000 41.950  ? 67  ARG LLL CD  1 
ATOM 17374 N NE  . ARG L 3 67  ? 127.252 0.859   -17.935 1.000 42.750  ? 67  ARG LLL NE  1 
ATOM 17375 C CZ  . ARG L 3 67  ? 126.101 1.424   -17.584 1.000 41.300  ? 67  ARG LLL CZ  1 
ATOM 17376 N NH1 . ARG L 3 67  ? 125.645 2.488   -18.227 1.000 43.180  ? 67  ARG LLL NH1 1 
ATOM 17377 N NH2 . ARG L 3 67  ? 125.402 0.930   -16.569 1.000 40.720  ? 67  ARG LLL NH2 1 
ATOM 17378 N N   . PHE L 3 68  ? 130.204 5.053   -15.334 1.000 34.700  ? 68  PHE LLL N   1 
ATOM 17379 C CA  . PHE L 3 68  ? 129.950 6.187   -14.410 1.000 35.040  ? 68  PHE LLL CA  1 
ATOM 17380 C C   . PHE L 3 68  ? 131.264 6.655   -13.782 1.000 33.470  ? 68  PHE LLL C   1 
ATOM 17381 O O   . PHE L 3 68  ? 132.199 5.857   -13.651 1.000 31.640  ? 68  PHE LLL O   1 
ATOM 17382 C CB  . PHE L 3 68  ? 128.938 5.770   -13.350 1.000 33.750  ? 68  PHE LLL CB  1 
ATOM 17383 C CG  . PHE L 3 68  ? 127.535 5.568   -13.864 1.000 35.450  ? 68  PHE LLL CG  1 
ATOM 17384 C CD1 . PHE L 3 68  ? 127.272 5.423   -15.215 1.000 37.950  ? 68  PHE LLL CD1 1 
ATOM 17385 C CD2 . PHE L 3 68  ? 126.475 5.477   -12.982 1.000 34.710  ? 68  PHE LLL CD2 1 
ATOM 17386 C CE1 . PHE L 3 68  ? 125.976 5.215   -15.661 1.000 38.830  ? 68  PHE LLL CE1 1 
ATOM 17387 C CE2 . PHE L 3 68  ? 125.182 5.275   -13.430 1.000 33.890  ? 68  PHE LLL CE2 1 
ATOM 17388 C CZ  . PHE L 3 68  ? 124.934 5.145   -14.768 1.000 34.930  ? 68  PHE LLL CZ  1 
ATOM 17389 N N   . THR L 3 69  ? 131.339 7.933   -13.425 1.000 34.260  ? 69  THR LLL N   1 
ATOM 17390 C CA  . THR L 3 69  ? 132.490 8.516   -12.692 1.000 34.060  ? 69  THR LLL CA  1 
ATOM 17391 C C   . THR L 3 69  ? 131.964 9.465   -11.621 1.000 34.800  ? 69  THR LLL C   1 
ATOM 17392 O O   . THR L 3 69  ? 131.237 10.416  -11.962 1.000 42.790  ? 69  THR LLL O   1 
ATOM 17393 C CB  . THR L 3 69  ? 133.446 9.213   -13.652 1.000 34.020  ? 69  THR LLL CB  1 
ATOM 17394 O OG1 . THR L 3 69  ? 133.593 8.298   -14.733 1.000 31.340  ? 69  THR LLL OG1 1 
ATOM 17395 C CG2 . THR L 3 69  ? 134.781 9.543   -13.024 1.000 37.490  ? 69  THR LLL CG2 1 
ATOM 17396 N N   . ILE L 3 70  ? 132.317 9.200   -10.368 1.000 32.180  ? 70  ILE LLL N   1 
ATOM 17397 C CA  . ILE L 3 70  ? 131.957 10.065  -9.211  1.000 33.080  ? 70  ILE LLL CA  1 
ATOM 17398 C C   . ILE L 3 70  ? 133.047 11.129  -9.098  1.000 31.300  ? 70  ILE LLL C   1 
ATOM 17399 O O   . ILE L 3 70  ? 134.207 10.837  -9.419  1.000 31.240  ? 70  ILE LLL O   1 
ATOM 17400 C CB  . ILE L 3 70  ? 131.812 9.232   -7.919  1.000 34.500  ? 70  ILE LLL CB  1 
ATOM 17401 C CG1 . ILE L 3 70  ? 131.032 9.969   -6.832  1.000 33.030  ? 70  ILE LLL CG1 1 
ATOM 17402 C CG2 . ILE L 3 70  ? 133.173 8.791   -7.404  1.000 36.150  ? 70  ILE LLL CG2 1 
ATOM 17403 C CD1 . ILE L 3 70  ? 130.626 9.090   -5.691  1.000 34.440  ? 70  ILE LLL CD1 1 
ATOM 17404 N N   . SER L 3 71  ? 132.683 12.327  -8.670  1.000 30.810  ? 71  SER LLL N   1 
ATOM 17405 C CA  . SER L 3 71  ? 133.659 13.399  -8.387  1.000 34.700  ? 71  SER LLL CA  1 
ATOM 17406 C C   . SER L 3 71  ? 133.039 14.365  -7.388  1.000 36.770  ? 71  SER LLL C   1 
ATOM 17407 O O   . SER L 3 71  ? 131.796 14.403  -7.270  1.000 34.270  ? 71  SER LLL O   1 
ATOM 17408 C CB  . SER L 3 71  ? 134.086 14.092  -9.659  1.000 36.350  ? 71  SER LLL CB  1 
ATOM 17409 O OG  . SER L 3 71  ? 133.032 14.870  -10.209 1.000 35.600  ? 71  SER LLL OG  1 
ATOM 17410 N N   . ARG L 3 72  ? 133.882 15.139  -6.717  1.000 37.660  ? 72  ARG LLL N   1 
ATOM 17411 C CA  . ARG L 3 72  ? 133.396 16.193  -5.792  1.000 36.960  ? 72  ARG LLL CA  1 
ATOM 17412 C C   . ARG L 3 72  ? 134.230 17.454  -6.036  1.000 37.200  ? 72  ARG LLL C   1 
ATOM 17413 O O   . ARG L 3 72  ? 135.390 17.334  -6.564  1.000 43.330  ? 72  ARG LLL O   1 
ATOM 17414 C CB  . ARG L 3 72  ? 133.510 15.686  -4.355  1.000 37.960  ? 72  ARG LLL CB  1 
ATOM 17415 C CG  . ARG L 3 72  ? 134.929 15.327  -3.931  1.000 38.910  ? 72  ARG LLL CG  1 
ATOM 17416 C CD  . ARG L 3 72  ? 134.974 14.624  -2.593  1.000 39.600  ? 72  ARG LLL CD  1 
ATOM 17417 N NE  . ARG L 3 72  ? 134.291 15.371  -1.530  1.000 37.330  ? 72  ARG LLL NE  1 
ATOM 17418 C CZ  . ARG L 3 72  ? 133.649 14.818  -0.501  1.000 34.250  ? 72  ARG LLL CZ  1 
ATOM 17419 N NH1 . ARG L 3 72  ? 133.061 15.606  0.384   1.000 33.700  ? 72  ARG LLL NH1 1 
ATOM 17420 N NH2 . ARG L 3 72  ? 133.576 13.496  -0.371  1.000 33.200  ? 72  ARG LLL NH2 1 
ATOM 17421 N N   . ASP L 3 73  ? 133.648 18.606  -5.695  1.000 33.430  ? 73  ASP LLL N   1 
ATOM 17422 C CA  . ASP L 3 73  ? 134.351 19.907  -5.611  1.000 32.810  ? 73  ASP LLL CA  1 
ATOM 17423 C C   . ASP L 3 73  ? 134.117 20.453  -4.206  1.000 31.130  ? 73  ASP LLL C   1 
ATOM 17424 O O   . ASP L 3 73  ? 133.003 20.947  -3.936  1.000 26.120  ? 73  ASP LLL O   1 
ATOM 17425 C CB  . ASP L 3 73  ? 133.888 20.854  -6.714  1.000 33.400  ? 73  ASP LLL CB  1 
ATOM 17426 C CG  . ASP L 3 73  ? 134.694 22.132  -6.859  1.000 32.350  ? 73  ASP LLL CG  1 
ATOM 17427 O OD1 . ASP L 3 73  ? 135.557 22.400  -5.982  1.000 28.090  ? 73  ASP LLL OD1 1 
ATOM 17428 O OD2 . ASP L 3 73  ? 134.436 22.847  -7.854  1.000 32.770  ? 73  ASP LLL OD2 1 
ATOM 17429 N N   . ASN L 3 74  ? 135.120 20.318  -3.338  1.000 32.340  ? 74  ASN LLL N   1 
ATOM 17430 C CA  . ASN L 3 74  ? 135.003 20.681  -1.899  1.000 32.100  ? 74  ASN LLL CA  1 
ATOM 17431 C C   . ASN L 3 74  ? 134.936 22.208  -1.784  1.000 31.780  ? 74  ASN LLL C   1 
ATOM 17432 O O   . ASN L 3 74  ? 134.318 22.690  -0.827  1.000 35.470  ? 74  ASN LLL O   1 
ATOM 17433 C CB  . ASN L 3 74  ? 136.098 20.071  -1.019  1.000 29.440  ? 74  ASN LLL CB  1 
ATOM 17434 C CG  . ASN L 3 74  ? 135.871 18.612  -0.663  1.000 26.130  ? 74  ASN LLL CG  1 
ATOM 17435 O OD1 . ASN L 3 74  ? 134.797 18.044  -0.902  1.000 22.600  ? 74  ASN LLL OD1 1 
ATOM 17436 N ND2 . ASN L 3 74  ? 136.907 17.992  -0.113  1.000 22.450  ? 74  ASN LLL ND2 1 
ATOM 17437 N N   . ALA L 3 75  ? 135.489 22.943  -2.737  1.000 31.540  ? 75  ALA LLL N   1 
ATOM 17438 C CA  . ALA L 3 75  ? 135.334 24.417  -2.796  1.000 33.150  ? 75  ALA LLL CA  1 
ATOM 17439 C C   . ALA L 3 75  ? 133.894 24.787  -3.186  1.000 30.350  ? 75  ALA LLL C   1 
ATOM 17440 O O   . ALA L 3 75  ? 133.462 25.828  -2.752  1.000 28.800  ? 75  ALA LLL O   1 
ATOM 17441 C CB  . ALA L 3 75  ? 136.342 25.040  -3.730  1.000 33.150  ? 75  ALA LLL CB  1 
ATOM 17442 N N   . ARG L 3 76  ? 133.187 23.985  -3.975  1.000 30.850  ? 76  ARG LLL N   1 
ATOM 17443 C CA  . ARG L 3 76  ? 131.809 24.318  -4.437  1.000 35.840  ? 76  ARG LLL CA  1 
ATOM 17444 C C   . ARG L 3 76  ? 130.759 23.551  -3.599  1.000 35.440  ? 76  ARG LLL C   1 
ATOM 17445 O O   . ARG L 3 76  ? 129.570 23.643  -3.951  1.000 30.840  ? 76  ARG LLL O   1 
ATOM 17446 C CB  . ARG L 3 76  ? 131.661 24.077  -5.952  1.000 40.430  ? 76  ARG LLL CB  1 
ATOM 17447 C CG  . ARG L 3 76  ? 132.181 25.183  -6.873  1.000 45.810  ? 76  ARG LLL CG  1 
ATOM 17448 C CD  . ARG L 3 76  ? 131.904 24.923  -8.370  1.000 56.800  ? 76  ARG LLL CD  1 
ATOM 17449 N NE  . ARG L 3 76  ? 131.739 26.107  -9.256  1.000 66.710  ? 76  ARG LLL NE  1 
ATOM 17450 C CZ  . ARG L 3 76  ? 131.696 26.076  -10.600 1.000 55.000  ? 76  ARG LLL CZ  1 
ATOM 17451 N N   . ASN L 3 77  ? 131.153 22.846  -2.529  1.000 37.560  ? 77  ASN LLL N   1 
ATOM 17452 C CA  . ASN L 3 77  ? 130.215 22.066  -1.655  1.000 36.760  ? 77  ASN LLL CA  1 
ATOM 17453 C C   . ASN L 3 77  ? 129.299 21.157  -2.494  1.000 35.630  ? 77  ASN LLL C   1 
ATOM 17454 O O   . ASN L 3 77  ? 128.075 21.098  -2.196  1.000 36.710  ? 77  ASN LLL O   1 
ATOM 17455 C CB  . ASN L 3 77  ? 129.291 22.948  -0.800  1.000 37.570  ? 77  ASN LLL CB  1 
ATOM 17456 C CG  . ASN L 3 77  ? 129.952 23.507  0.433   1.000 39.840  ? 77  ASN LLL CG  1 
ATOM 17457 O OD1 . ASN L 3 77  ? 130.447 22.756  1.271   1.000 50.720  ? 77  ASN LLL OD1 1 
ATOM 17458 N ND2 . ASN L 3 77  ? 129.923 24.817  0.561   1.000 39.980  ? 77  ASN LLL ND2 1 
ATOM 17459 N N   . SER L 3 78  ? 129.849 20.454  -3.490  1.000 33.540  ? 78  SER LLL N   1 
ATOM 17460 C CA  . SER L 3 78  ? 129.049 19.673  -4.462  1.000 34.410  ? 78  SER LLL CA  1 
ATOM 17461 C C   . SER L 3 78  ? 129.672 18.322  -4.797  1.000 32.470  ? 78  SER LLL C   1 
ATOM 17462 O O   . SER L 3 78  ? 130.883 18.243  -5.006  1.000 37.420  ? 78  SER LLL O   1 
ATOM 17463 C CB  . SER L 3 78  ? 128.825 20.472  -5.699  1.000 40.370  ? 78  SER LLL CB  1 
ATOM 17464 O OG  . SER L 3 78  ? 127.905 21.532  -5.449  1.000 48.250  ? 78  SER LLL OG  1 
ATOM 17465 N N   . LEU L 3 79  ? 128.832 17.300  -4.865  1.000 31.440  ? 79  LEU LLL N   1 
ATOM 17466 C CA  . LEU L 3 79  ? 129.166 15.940  -5.336  1.000 32.450  ? 79  LEU LLL CA  1 
ATOM 17467 C C   . LEU L 3 79  ? 128.571 15.774  -6.733  1.000 35.780  ? 79  LEU LLL C   1 
ATOM 17468 O O   . LEU L 3 79  ? 127.441 16.275  -6.948  1.000 37.510  ? 79  LEU LLL O   1 
ATOM 17469 C CB  . LEU L 3 79  ? 128.566 14.938  -4.349  1.000 31.960  ? 79  LEU LLL CB  1 
ATOM 17470 C CG  . LEU L 3 79  ? 128.559 13.482  -4.810  1.000 32.480  ? 79  LEU LLL CG  1 
ATOM 17471 C CD1 . LEU L 3 79  ? 129.917 12.866  -4.593  1.000 33.450  ? 79  LEU LLL CD1 1 
ATOM 17472 C CD2 . LEU L 3 79  ? 127.502 12.686  -4.090  1.000 32.570  ? 79  LEU LLL CD2 1 
ATOM 17473 N N   . TYR L 3 80  ? 129.289 15.116  -7.648  1.000 36.070  ? 80  TYR LLL N   1 
ATOM 17474 C CA  . TYR L 3 80  ? 128.856 14.908  -9.052  1.000 41.980  ? 80  TYR LLL CA  1 
ATOM 17475 C C   . TYR L 3 80  ? 128.932 13.423  -9.424  1.000 44.610  ? 80  TYR LLL C   1 
ATOM 17476 O O   . TYR L 3 80  ? 129.806 12.691  -8.907  1.000 44.720  ? 80  TYR LLL O   1 
ATOM 17477 C CB  . TYR L 3 80  ? 129.702 15.737  -10.024 1.000 45.470  ? 80  TYR LLL CB  1 
ATOM 17478 C CG  . TYR L 3 80  ? 129.806 17.202  -9.684  1.000 43.410  ? 80  TYR LLL CG  1 
ATOM 17479 C CD1 . TYR L 3 80  ? 128.721 18.052  -9.826  1.000 40.020  ? 80  TYR LLL CD1 1 
ATOM 17480 C CD2 . TYR L 3 80  ? 131.001 17.739  -9.235  1.000 46.160  ? 80  TYR LLL CD2 1 
ATOM 17481 C CE1 . TYR L 3 80  ? 128.810 19.396  -9.508  1.000 43.110  ? 80  TYR LLL CE1 1 
ATOM 17482 C CE2 . TYR L 3 80  ? 131.108 19.085  -8.922  1.000 48.820  ? 80  TYR LLL CE2 1 
ATOM 17483 C CZ  . TYR L 3 80  ? 130.008 19.919  -9.041  1.000 47.820  ? 80  TYR LLL CZ  1 
ATOM 17484 O OH  . TYR L 3 80  ? 130.140 21.248  -8.715  1.000 44.720  ? 80  TYR LLL OH  1 
ATOM 17485 N N   . LEU L 3 81  ? 128.029 13.001  -10.314 1.000 43.440  ? 81  LEU LLL N   1 
ATOM 17486 C CA  . LEU L 3 81  ? 128.088 11.686  -11.000 1.000 41.300  ? 81  LEU LLL CA  1 
ATOM 17487 C C   . LEU L 3 81  ? 128.008 11.904  -12.515 1.000 41.540  ? 81  LEU LLL C   1 
ATOM 17488 O O   . LEU L 3 81  ? 126.961 12.382  -12.978 1.000 37.940  ? 81  LEU LLL O   1 
ATOM 17489 C CB  . LEU L 3 81  ? 126.940 10.798  -10.515 1.000 38.160  ? 81  LEU LLL CB  1 
ATOM 17490 C CG  . LEU L 3 81  ? 126.948 9.382   -11.094 1.000 36.840  ? 81  LEU LLL CG  1 
ATOM 17491 C CD1 . LEU L 3 81  ? 128.212 8.638   -10.670 1.000 39.170  ? 81  LEU LLL CD1 1 
ATOM 17492 C CD2 . LEU L 3 81  ? 125.704 8.622   -10.686 1.000 36.150  ? 81  LEU LLL CD2 1 
ATOM 17493 N N   . GLN L 3 82  ? 129.085 11.570  -13.228 1.000 41.450  ? 82  GLN LLL N   1 
ATOM 17494 C CA  . GLN L 3 82  ? 129.161 11.590  -14.707 1.000 47.430  ? 82  GLN LLL CA  1 
ATOM 17495 C C   . GLN L 3 82  ? 128.686 10.229  -15.238 1.000 46.870  ? 82  GLN LLL C   1 
ATOM 17496 O O   . GLN L 3 82  ? 129.403 9.223   -15.037 1.000 42.980  ? 82  GLN LLL O   1 
ATOM 17497 C CB  . GLN L 3 82  ? 130.595 11.883  -15.146 1.000 54.700  ? 82  GLN LLL CB  1 
ATOM 17498 C CG  . GLN L 3 82  ? 130.757 12.023  -16.653 1.000 55.150  ? 82  GLN LLL CG  1 
ATOM 17499 C CD  . GLN L 3 82  ? 129.778 13.022  -17.201 1.000 58.600  ? 82  GLN LLL CD  1 
ATOM 17500 O OE1 . GLN L 3 82  ? 129.764 14.196  -16.832 1.000 60.490  ? 82  GLN LLL OE1 1 
ATOM 17501 N NE2 . GLN L 3 82  ? 128.908 12.541  -18.060 1.000 64.560  ? 82  GLN LLL NE2 1 
ATOM 17502 N N   . MET L 3 83  ? 127.529 10.199  -15.899 1.000 46.410  ? 83  MET LLL N   1 
ATOM 17503 C CA  . MET L 3 83  ? 126.889 8.961   -16.411 1.000 44.240  ? 83  MET LLL CA  1 
ATOM 17504 C C   . MET L 3 83  ? 127.072 8.923   -17.936 1.000 43.740  ? 83  MET LLL C   1 
ATOM 17505 O O   . MET L 3 83  ? 126.401 9.705   -18.625 1.000 42.710  ? 83  MET LLL O   1 
ATOM 17506 C CB  . MET L 3 83  ? 125.401 8.920   -16.048 1.000 43.490  ? 83  MET LLL CB  1 
ATOM 17507 C CG  . MET L 3 83  ? 125.113 9.006   -14.572 1.000 45.760  ? 83  MET LLL CG  1 
ATOM 17508 S SD  . MET L 3 83  ? 123.375 9.467   -14.207 1.000 44.230  ? 83  MET LLL SD  1 
ATOM 17509 C CE  . MET L 3 83  ? 122.646 7.842   -14.281 1.000 48.130  ? 83  MET LLL CE  1 
ATOM 17510 N N   . ASN L 3 84  ? 127.958 8.056   -18.427 1.000 41.600  ? 84  ASN LLL N   1 
ATOM 17511 C CA  . ASN L 3 84  ? 128.203 7.840   -19.872 1.000 39.470  ? 84  ASN LLL CA  1 
ATOM 17512 C C   . ASN L 3 84  ? 127.601 6.495   -20.268 1.000 39.290  ? 84  ASN LLL C   1 
ATOM 17513 O O   . ASN L 3 84  ? 127.377 5.666   -19.366 1.000 39.910  ? 84  ASN LLL O   1 
ATOM 17514 C CB  . ASN L 3 84  ? 129.692 7.858   -20.192 1.000 39.960  ? 84  ASN LLL CB  1 
ATOM 17515 C CG  . ASN L 3 84  ? 130.336 9.184   -19.873 1.000 41.270  ? 84  ASN LLL CG  1 
ATOM 17516 O OD1 . ASN L 3 84  ? 129.666 10.215  -19.752 1.000 39.160  ? 84  ASN LLL OD1 1 
ATOM 17517 N ND2 . ASN L 3 84  ? 131.647 9.146   -19.749 1.000 46.000  ? 84  ASN LLL ND2 1 
ATOM 17518 N N   . SER L 3 85  ? 127.355 6.292   -21.565 1.000 37.820  ? 85  SER LLL N   1 
ATOM 17519 C CA  . SER L 3 85  ? 126.918 4.999   -22.151 1.000 35.350  ? 85  SER LLL CA  1 
ATOM 17520 C C   . SER L 3 85  ? 125.641 4.519   -21.448 1.000 38.480  ? 85  SER LLL C   1 
ATOM 17521 O O   . SER L 3 85  ? 125.492 3.286   -21.213 1.000 37.640  ? 85  SER LLL O   1 
ATOM 17522 C CB  . SER L 3 85  ? 128.002 3.968   -22.043 1.000 32.360  ? 85  SER LLL CB  1 
ATOM 17523 O OG  . SER L 3 85  ? 129.263 4.460   -22.439 1.000 28.900  ? 85  SER LLL OG  1 
ATOM 17524 N N   . LEU L 3 86  ? 124.750 5.458   -21.132 1.000 41.820  ? 86  LEU LLL N   1 
ATOM 17525 C CA  . LEU L 3 86  ? 123.507 5.180   -20.379 1.000 44.950  ? 86  LEU LLL CA  1 
ATOM 17526 C C   . LEU L 3 86  ? 122.707 4.069   -21.067 1.000 46.240  ? 86  LEU LLL C   1 
ATOM 17527 O O   . LEU L 3 86  ? 122.673 4.032   -22.316 1.000 43.300  ? 86  LEU LLL O   1 
ATOM 17528 C CB  . LEU L 3 86  ? 122.704 6.479   -20.282 1.000 49.850  ? 86  LEU LLL CB  1 
ATOM 17529 C CG  . LEU L 3 86  ? 123.097 7.336   -19.089 1.000 54.130  ? 86  LEU LLL CG  1 
ATOM 17530 C CD1 . LEU L 3 86  ? 122.498 8.720   -19.181 1.000 55.780  ? 86  LEU LLL CD1 1 
ATOM 17531 C CD2 . LEU L 3 86  ? 122.668 6.666   -17.792 1.000 58.420  ? 86  LEU LLL CD2 1 
ATOM 17532 N N   . ARG L 3 87  ? 122.080 3.209   -20.264 1.000 46.660  ? 87  ARG LLL N   1 
ATOM 17533 C CA  . ARG L 3 87  ? 121.224 2.112   -20.766 1.000 48.340  ? 87  ARG LLL CA  1 
ATOM 17534 C C   . ARG L 3 87  ? 119.826 2.275   -20.192 1.000 53.970  ? 87  ARG LLL C   1 
ATOM 17535 O O   . ARG L 3 87  ? 119.642 3.126   -19.301 1.000 52.700  ? 87  ARG LLL O   1 
ATOM 17536 C CB  . ARG L 3 87  ? 121.807 0.771   -20.353 1.000 45.570  ? 87  ARG LLL CB  1 
ATOM 17537 C CG  . ARG L 3 87  ? 123.300 0.684   -20.609 1.000 47.370  ? 87  ARG LLL CG  1 
ATOM 17538 C CD  . ARG L 3 87  ? 123.821 -0.600  -20.018 1.000 46.530  ? 87  ARG LLL CD  1 
ATOM 17539 N NE  . ARG L 3 87  ? 125.243 -0.775  -20.246 1.000 44.630  ? 87  ARG LLL NE  1 
ATOM 17540 C CZ  . ARG L 3 87  ? 125.966 -1.677  -19.613 1.000 45.330  ? 87  ARG LLL CZ  1 
ATOM 17541 N NH1 . ARG L 3 87  ? 125.385 -2.448  -18.708 1.000 48.480  ? 87  ARG LLL NH1 1 
ATOM 17542 N NH2 . ARG L 3 87  ? 127.259 -1.800  -19.862 1.000 43.110  ? 87  ARG LLL NH2 1 
ATOM 17543 N N   . VAL L 3 88  ? 118.886 1.490   -20.709 1.000 60.000  ? 88  VAL LLL N   1 
ATOM 17544 C CA  . VAL L 3 88  ? 117.457 1.526   -20.282 1.000 61.040  ? 88  VAL LLL CA  1 
ATOM 17545 C C   . VAL L 3 88  ? 117.397 1.154   -18.792 1.000 60.210  ? 88  VAL LLL C   1 
ATOM 17546 O O   . VAL L 3 88  ? 116.691 1.876   -18.028 1.000 50.940  ? 88  VAL LLL O   1 
ATOM 17547 C CB  . VAL L 3 88  ? 116.588 0.594   -21.145 1.000 62.810  ? 88  VAL LLL CB  1 
ATOM 17548 C CG1 . VAL L 3 88  ? 115.134 0.666   -20.714 1.000 63.330  ? 88  VAL LLL CG1 1 
ATOM 17549 C CG2 . VAL L 3 88  ? 116.720 0.908   -22.630 1.000 66.970  ? 88  VAL LLL CG2 1 
ATOM 17550 N N   . GLU L 3 89  ? 118.168 0.131   -18.384 1.000 55.370  ? 89  GLU LLL N   1 
ATOM 17551 C CA  . GLU L 3 89  ? 118.230 -0.375  -16.989 1.000 55.400  ? 89  GLU LLL CA  1 
ATOM 17552 C C   . GLU L 3 89  ? 118.603 0.762   -16.021 1.000 57.840  ? 89  GLU LLL C   1 
ATOM 17553 O O   . GLU L 3 89  ? 118.113 0.751   -14.884 1.000 60.870  ? 89  GLU LLL O   1 
ATOM 17554 C CB  . GLU L 3 89  ? 119.249 -1.508  -16.848 1.000 54.140  ? 89  GLU LLL CB  1 
ATOM 17555 C CG  . GLU L 3 89  ? 119.212 -2.519  -17.964 1.000 61.150  ? 89  GLU LLL CG  1 
ATOM 17556 C CD  . GLU L 3 89  ? 120.308 -2.328  -18.993 1.000 68.180  ? 89  GLU LLL CD  1 
ATOM 17557 O OE1 . GLU L 3 89  ? 121.474 -2.707  -18.692 1.000 66.510  ? 89  GLU LLL OE1 1 
ATOM 17558 O OE2 . GLU L 3 89  ? 120.004 -1.800  -20.090 1.000 76.200  ? 89  GLU LLL OE2 1 
ATOM 17559 N N   . ASP L 3 90  ? 119.426 1.720   -16.454 1.000 56.630  ? 90  ASP LLL N   1 
ATOM 17560 C CA  . ASP L 3 90  ? 119.936 2.819   -15.591 1.000 52.610  ? 90  ASP LLL CA  1 
ATOM 17561 C C   . ASP L 3 90  ? 118.794 3.760   -15.180 1.000 50.490  ? 90  ASP LLL C   1 
ATOM 17562 O O   . ASP L 3 90  ? 119.056 4.658   -14.355 1.000 54.080  ? 90  ASP LLL O   1 
ATOM 17563 C CB  . ASP L 3 90  ? 121.067 3.592   -16.275 1.000 54.050  ? 90  ASP LLL CB  1 
ATOM 17564 C CG  . ASP L 3 90  ? 122.326 2.760   -16.499 1.000 54.890  ? 90  ASP LLL CG  1 
ATOM 17565 O OD1 . ASP L 3 90  ? 122.512 1.766   -15.759 1.000 52.480  ? 90  ASP LLL OD1 1 
ATOM 17566 O OD2 . ASP L 3 90  ? 123.112 3.108   -17.419 1.000 56.330  ? 90  ASP LLL OD2 1 
ATOM 17567 N N   . THR L 3 91  ? 117.584 3.598   -15.733 1.000 48.290  ? 91  THR LLL N   1 
ATOM 17568 C CA  . THR L 3 91  ? 116.399 4.397   -15.316 1.000 50.520  ? 91  THR LLL CA  1 
ATOM 17569 C C   . THR L 3 91  ? 116.146 4.168   -13.827 1.000 50.520  ? 91  THR LLL C   1 
ATOM 17570 O O   . THR L 3 91  ? 115.972 2.978   -13.431 1.000 54.240  ? 91  THR LLL O   1 
ATOM 17571 C CB  . THR L 3 91  ? 115.140 4.045   -16.113 1.000 49.470  ? 91  THR LLL CB  1 
ATOM 17572 O OG1 . THR L 3 91  ? 115.442 4.382   -17.468 1.000 54.610  ? 91  THR LLL OG1 1 
ATOM 17573 C CG2 . THR L 3 91  ? 113.916 4.806   -15.646 1.000 47.440  ? 91  THR LLL CG2 1 
ATOM 17574 N N   . ALA L 3 92  ? 116.116 5.250   -13.049 1.000 45.500  ? 92  ALA LLL N   1 
ATOM 17575 C CA  . ALA L 3 92  ? 115.896 5.228   -11.581 1.000 47.340  ? 92  ALA LLL CA  1 
ATOM 17576 C C   . ALA L 3 92  ? 115.842 6.657   -11.044 1.000 47.580  ? 92  ALA LLL C   1 
ATOM 17577 O O   . ALA L 3 92  ? 116.231 7.575   -11.777 1.000 57.790  ? 92  ALA LLL O   1 
ATOM 17578 C CB  . ALA L 3 92  ? 117.015 4.470   -10.907 1.000 50.670  ? 92  ALA LLL CB  1 
ATOM 17579 N N   . VAL L 3 93  ? 115.383 6.823   -9.806  1.000 43.720  ? 93  VAL LLL N   1 
ATOM 17580 C CA  . VAL L 3 93  ? 115.667 8.029   -8.980  1.000 42.780  ? 93  VAL LLL CA  1 
ATOM 17581 C C   . VAL L 3 93  ? 117.093 7.866   -8.443  1.000 46.400  ? 93  VAL LLL C   1 
ATOM 17582 O O   . VAL L 3 93  ? 117.409 6.772   -7.927  1.000 53.520  ? 93  VAL LLL O   1 
ATOM 17583 C CB  . VAL L 3 93  ? 114.653 8.195   -7.839  1.000 41.880  ? 93  VAL LLL CB  1 
ATOM 17584 C CG1 . VAL L 3 93  ? 114.954 9.408   -6.990  1.000 40.550  ? 93  VAL LLL CG1 1 
ATOM 17585 C CG2 . VAL L 3 93  ? 113.241 8.285   -8.385  1.000 47.190  ? 93  VAL LLL CG2 1 
ATOM 17586 N N   . TYR L 3 94  ? 117.931 8.895   -8.595  1.000 41.400  ? 94  TYR LLL N   1 
ATOM 17587 C CA  . TYR L 3 94  ? 119.349 8.903   -8.148  1.000 35.940  ? 94  TYR LLL CA  1 
ATOM 17588 C C   . TYR L 3 94  ? 119.429 9.754   -6.874  1.000 39.960  ? 94  TYR LLL C   1 
ATOM 17589 O O   . TYR L 3 94  ? 119.385 10.998  -6.954  1.000 39.230  ? 94  TYR LLL O   1 
ATOM 17590 C CB  . TYR L 3 94  ? 120.270 9.372   -9.271  1.000 33.220  ? 94  TYR LLL CB  1 
ATOM 17591 C CG  . TYR L 3 94  ? 120.564 8.287   -10.266 1.000 33.900  ? 94  TYR LLL CG  1 
ATOM 17592 C CD1 . TYR L 3 94  ? 119.560 7.736   -11.047 1.000 33.510  ? 94  TYR LLL CD1 1 
ATOM 17593 C CD2 . TYR L 3 94  ? 121.841 7.779   -10.405 1.000 37.430  ? 94  TYR LLL CD2 1 
ATOM 17594 C CE1 . TYR L 3 94  ? 119.814 6.708   -11.938 1.000 34.160  ? 94  TYR LLL CE1 1 
ATOM 17595 C CE2 . TYR L 3 94  ? 122.115 6.741   -11.284 1.000 37.960  ? 94  TYR LLL CE2 1 
ATOM 17596 C CZ  . TYR L 3 94  ? 121.095 6.194   -12.043 1.000 36.730  ? 94  TYR LLL CZ  1 
ATOM 17597 O OH  . TYR L 3 94  ? 121.381 5.175   -12.906 1.000 37.920  ? 94  TYR LLL OH  1 
ATOM 17598 N N   . TYR L 3 95  ? 119.495 9.075   -5.721  1.000 41.130  ? 95  TYR LLL N   1 
ATOM 17599 C CA  . TYR L 3 95  ? 119.685 9.681   -4.382  1.000 37.710  ? 95  TYR LLL CA  1 
ATOM 17600 C C   . TYR L 3 95  ? 121.185 9.924   -4.125  1.000 38.460  ? 95  TYR LLL C   1 
ATOM 17601 O O   . TYR L 3 95  ? 122.074 9.198   -4.618  1.000 37.440  ? 95  TYR LLL O   1 
ATOM 17602 C CB  . TYR L 3 95  ? 118.998 8.843   -3.300  1.000 37.060  ? 95  TYR LLL CB  1 
ATOM 17603 C CG  . TYR L 3 95  ? 117.498 8.716   -3.395  1.000 35.460  ? 95  TYR LLL CG  1 
ATOM 17604 C CD1 . TYR L 3 95  ? 116.661 9.746   -3.013  1.000 33.450  ? 95  TYR LLL CD1 1 
ATOM 17605 C CD2 . TYR L 3 95  ? 116.899 7.542   -3.832  1.000 38.000  ? 95  TYR LLL CD2 1 
ATOM 17606 C CE1 . TYR L 3 95  ? 115.274 9.626   -3.096  1.000 35.880  ? 95  TYR LLL CE1 1 
ATOM 17607 C CE2 . TYR L 3 95  ? 115.516 7.413   -3.920  1.000 37.300  ? 95  TYR LLL CE2 1 
ATOM 17608 C CZ  . TYR L 3 95  ? 114.687 8.455   -3.548  1.000 33.910  ? 95  TYR LLL CZ  1 
ATOM 17609 N N   . CYS L 3 96  ? 121.458 10.988  -3.383  1.000 42.340  ? 96  CYS LLL N   1 
ATOM 17610 C CA  . CYS L 3 96  ? 122.786 11.420  -2.887  1.000 45.240  ? 96  CYS LLL CA  1 
ATOM 17611 C C   . CYS L 3 96  ? 122.794 11.270  -1.356  1.000 42.040  ? 96  CYS LLL C   1 
ATOM 17612 O O   . CYS L 3 96  ? 121.851 11.802  -0.719  1.000 45.500  ? 96  CYS LLL O   1 
ATOM 17613 C CB  . CYS L 3 96  ? 122.997 12.861  -3.343  1.000 48.590  ? 96  CYS LLL CB  1 
ATOM 17614 S SG  . CYS L 3 96  ? 124.618 13.548  -2.917  1.000 61.410  ? 96  CYS LLL SG  1 
ATOM 17615 N N   . ALA L 3 97  ? 123.754 10.541  -0.776  1.000 33.970  ? 97  ALA LLL N   1 
ATOM 17616 C CA  . ALA L 3 97  ? 123.745 10.173  0.661   1.000 32.740  ? 97  ALA LLL CA  1 
ATOM 17617 C C   . ALA L 3 97  ? 125.119 10.357  1.308   1.000 32.070  ? 97  ALA LLL C   1 
ATOM 17618 O O   . ALA L 3 97  ? 126.118 9.996   0.667   1.000 33.540  ? 97  ALA LLL O   1 
ATOM 17619 C CB  . ALA L 3 97  ? 123.254 8.765   0.834   1.000 34.650  ? 97  ALA LLL CB  1 
ATOM 17620 N N   . ARG L 3 98  ? 125.158 10.868  2.543   1.000 30.600  ? 98  ARG LLL N   1 
ATOM 17621 C CA  . ARG L 3 98  ? 126.406 11.068  3.327   1.000 29.080  ? 98  ARG LLL CA  1 
ATOM 17622 C C   . ARG L 3 98  ? 126.719 9.813   4.137   1.000 28.540  ? 98  ARG LLL C   1 
ATOM 17623 O O   . ARG L 3 98  ? 125.770 9.175   4.638   1.000 32.040  ? 98  ARG LLL O   1 
ATOM 17624 C CB  . ARG L 3 98  ? 126.289 12.231  4.308   1.000 30.940  ? 98  ARG LLL CB  1 
ATOM 17625 C CG  . ARG L 3 98  ? 127.613 12.590  4.973   1.000 32.350  ? 98  ARG LLL CG  1 
ATOM 17626 C CD  . ARG L 3 98  ? 127.484 13.743  5.950   1.000 30.940  ? 98  ARG LLL CD  1 
ATOM 17627 N NE  . ARG L 3 98  ? 126.778 13.318  7.130   1.000 31.650  ? 98  ARG LLL NE  1 
ATOM 17628 C CZ  . ARG L 3 98  ? 126.665 14.033  8.238   1.000 33.790  ? 98  ARG LLL CZ  1 
ATOM 17629 N NH1 . ARG L 3 98  ? 127.222 15.226  8.334   1.000 35.670  ? 98  ARG LLL NH1 1 
ATOM 17630 N NH2 . ARG L 3 98  ? 125.990 13.543  9.260   1.000 34.020  ? 98  ARG LLL NH2 1 
ATOM 17631 N N   . TYR L 3 99  ? 128.004 9.470   4.255   1.000 26.670  ? 99  TYR LLL N   1 
ATOM 17632 C CA  . TYR L 3 99  ? 128.524 8.471   5.224   1.000 25.400  ? 99  TYR LLL CA  1 
ATOM 17633 C C   . TYR L 3 99  ? 129.378 9.200   6.247   1.000 26.520  ? 99  TYR LLL C   1 
ATOM 17634 O O   . TYR L 3 99  ? 130.352 9.917   5.900   1.000 30.380  ? 99  TYR LLL O   1 
ATOM 17635 C CB  . TYR L 3 99  ? 129.294 7.345   4.547   1.000 22.760  ? 99  TYR LLL CB  1 
ATOM 17636 C CG  . TYR L 3 99  ? 130.156 6.541   5.479   1.000 23.160  ? 99  TYR LLL CG  1 
ATOM 17637 C CD1 . TYR L 3 99  ? 131.384 7.022   5.865   1.000 23.530  ? 99  TYR LLL CD1 1 
ATOM 17638 C CD2 . TYR L 3 99  ? 129.766 5.296   5.962   1.000 23.940  ? 99  TYR LLL CD2 1 
ATOM 17639 C CE1 . TYR L 3 99  ? 132.212 6.296   6.690   1.000 22.610  ? 99  TYR LLL CE1 1 
ATOM 17640 C CE2 . TYR L 3 99  ? 130.592 4.557   6.799   1.000 22.920  ? 99  TYR LLL CE2 1 
ATOM 17641 C CZ  . TYR L 3 99  ? 131.833 5.055   7.158   1.000 22.120  ? 99  TYR LLL CZ  1 
ATOM 17642 O OH  . TYR L 3 99  ? 132.699 4.392   7.993   1.000 21.700  ? 99  TYR LLL OH  1 
ATOM 17643 N N   . ALA L 3 100 ? 129.009 9.015   7.502   1.000 25.830  ? 100 ALA LLL N   1 
ATOM 17644 C CA  . ALA L 3 100 ? 129.793 9.468   8.661   1.000 27.270  ? 100 ALA LLL CA  1 
ATOM 17645 C C   . ALA L 3 100 ? 130.261 8.229   9.410   1.000 24.860  ? 100 ALA LLL C   1 
ATOM 17646 O O   . ALA L 3 100 ? 129.545 7.241   9.395   1.000 23.180  ? 100 ALA LLL O   1 
ATOM 17647 C CB  . ALA L 3 100 ? 128.965 10.376  9.531   1.000 29.490  ? 100 ALA LLL CB  1 
ATOM 17648 N N   . HIS L 3 101 ? 131.421 8.329   10.047  1.000 24.250  ? 101 HIS LLL N   1 
ATOM 17649 C CA  . HIS L 3 101 ? 132.035 7.231   10.825  1.000 23.190  ? 101 HIS LLL CA  1 
ATOM 17650 C C   . HIS L 3 101 ? 131.056 6.872   11.929  1.000 22.190  ? 101 HIS LLL C   1 
ATOM 17651 O O   . HIS L 3 101 ? 130.411 7.808   12.480  1.000 22.390  ? 101 HIS LLL O   1 
ATOM 17652 C CB  . HIS L 3 101 ? 133.384 7.650   11.391  1.000 23.660  ? 101 HIS LLL CB  1 
ATOM 17653 C CG  . HIS L 3 101 ? 133.989 6.617   12.255  1.000 22.900  ? 101 HIS LLL CG  1 
ATOM 17654 N ND1 . HIS L 3 101 ? 134.575 5.524   11.732  1.000 23.770  ? 101 HIS LLL ND1 1 
ATOM 17655 C CD2 . HIS L 3 101 ? 134.034 6.479   13.588  1.000 24.980  ? 101 HIS LLL CD2 1 
ATOM 17656 C CE1 . HIS L 3 101 ? 135.032 4.768   12.715  1.000 25.330  ? 101 HIS LLL CE1 1 
ATOM 17657 N NE2 . HIS L 3 101 ? 134.687 5.313   13.859  1.000 25.130  ? 101 HIS LLL NE2 1 
ATOM 17658 N N   . ASP L 3 102 ? 130.914 5.574   12.150  1.000 21.660  ? 102 ASP LLL N   1 
ATOM 17659 C CA  . ASP L 3 102 ? 130.090 4.928   13.197  1.000 22.680  ? 102 ASP LLL CA  1 
ATOM 17660 C C   . ASP L 3 102 ? 128.601 5.079   12.903  1.000 23.970  ? 102 ASP LLL C   1 
ATOM 17661 O O   . ASP L 3 102 ? 127.894 4.089   13.198  1.000 24.260  ? 102 ASP LLL O   1 
ATOM 17662 C CB  . ASP L 3 102 ? 130.484 5.373   14.598  1.000 22.980  ? 102 ASP LLL CB  1 
ATOM 17663 C CG  . ASP L 3 102 ? 129.742 4.609   15.686  1.000 23.930  ? 102 ASP LLL CG  1 
ATOM 17664 O OD1 . ASP L 3 102 ? 130.090 3.394   15.942  1.000 21.010  ? 102 ASP LLL OD1 1 
ATOM 17665 O OD2 . ASP L 3 102 ? 128.830 5.254   16.280  1.000 25.470  ? 102 ASP LLL OD2 1 
ATOM 17666 N N   . TRP L 3 103 ? 128.154 6.221   12.353  1.000 27.210  ? 103 TRP LLL N   1 
ATOM 17667 C CA  . TRP L 3 103 ? 126.745 6.497   11.926  1.000 27.940  ? 103 TRP LLL CA  1 
ATOM 17668 C C   . TRP L 3 103 ? 126.406 5.636   10.695  1.000 28.220  ? 103 TRP LLL C   1 
ATOM 17669 O O   . TRP L 3 103 ? 125.285 5.103   10.594  1.000 25.660  ? 103 TRP LLL O   1 
ATOM 17670 C CB  . TRP L 3 103 ? 126.545 7.991   11.619  1.000 26.760  ? 103 TRP LLL CB  1 
ATOM 17671 C CG  . TRP L 3 103 ? 126.385 8.867   12.823  1.000 27.040  ? 103 TRP LLL CG  1 
ATOM 17672 C CD1 . TRP L 3 103 ? 127.342 9.653   13.395  1.000 30.090  ? 103 TRP LLL CD1 1 
ATOM 17673 C CD2 . TRP L 3 103 ? 125.202 9.071   13.613  1.000 28.420  ? 103 TRP LLL CD2 1 
ATOM 17674 N NE1 . TRP L 3 103 ? 126.846 10.311  14.491  1.000 29.800  ? 103 TRP LLL NE1 1 
ATOM 17675 C CE2 . TRP L 3 103 ? 125.530 9.984   14.640  1.000 28.750  ? 103 TRP LLL CE2 1 
ATOM 17676 C CE3 . TRP L 3 103 ? 123.907 8.549   13.592  1.000 28.760  ? 103 TRP LLL CE3 1 
ATOM 17677 C CZ2 . TRP L 3 103 ? 124.612 10.397  15.603  1.000 26.920  ? 103 TRP LLL CZ2 1 
ATOM 17678 C CZ3 . TRP L 3 103 ? 122.990 8.984   14.533  1.000 27.120  ? 103 TRP LLL CZ3 1 
ATOM 17679 C CH2 . TRP L 3 103 ? 123.339 9.891   15.525  1.000 24.950  ? 103 TRP LLL CH2 1 
ATOM 17680 N N   . ASN L 3 104 ? 127.360 5.555   9.772   1.000 31.490  ? 104 ASN LLL N   1 
ATOM 17681 C CA  . ASN L 3 104 ? 127.264 4.864   8.460   1.000 34.710  ? 104 ASN LLL CA  1 
ATOM 17682 C C   . ASN L 3 104 ? 126.511 5.815   7.519   1.000 35.610  ? 104 ASN LLL C   1 
ATOM 17683 O O   . ASN L 3 104 ? 126.698 7.032   7.659   1.000 35.480  ? 104 ASN LLL O   1 
ATOM 17684 C CB  . ASN L 3 104 ? 126.752 3.441   8.664   1.000 38.660  ? 104 ASN LLL CB  1 
ATOM 17685 C CG  . ASN L 3 104 ? 127.723 2.647   9.522   1.000 45.580  ? 104 ASN LLL CG  1 
ATOM 17686 O OD1 . ASN L 3 104 ? 128.862 2.417   9.092   1.000 49.500  ? 104 ASN LLL OD1 1 
ATOM 17687 N ND2 . ASN L 3 104 ? 127.322 2.258   10.734  1.000 44.990  ? 104 ASN LLL ND2 1 
ATOM 17688 N N   . VAL L 3 105 ? 125.753 5.312   6.549   1.000 37.650  ? 105 VAL LLL N   1 
ATOM 17689 C CA  . VAL L 3 105 ? 124.982 6.198   5.636   1.000 38.020  ? 105 VAL LLL CA  1 
ATOM 17690 C C   . VAL L 3 105 ? 123.809 6.763   6.456   1.000 34.310  ? 105 VAL LLL C   1 
ATOM 17691 O O   . VAL L 3 105 ? 123.051 5.941   7.003   1.000 41.490  ? 105 VAL LLL O   1 
ATOM 17692 C CB  . VAL L 3 105 ? 124.514 5.422   4.388   1.000 43.670  ? 105 VAL LLL CB  1 
ATOM 17693 C CG1 . VAL L 3 105 ? 123.414 6.158   3.631   1.000 44.710  ? 105 VAL LLL CG1 1 
ATOM 17694 C CG2 . VAL L 3 105 ? 125.681 5.061   3.471   1.000 42.140  ? 105 VAL LLL CG2 1 
ATOM 17695 N N   . ASP L 3 106 ? 123.703 8.088   6.581   1.000 29.830  ? 106 ASP LLL N   1 
ATOM 17696 C CA  . ASP L 3 106 ? 122.730 8.754   7.499   1.000 30.200  ? 106 ASP LLL CA  1 
ATOM 17697 C C   . ASP L 3 106 ? 121.749 9.663   6.733   1.000 30.610  ? 106 ASP LLL C   1 
ATOM 17698 O O   . ASP L 3 106 ? 120.532 9.356   6.706   1.000 32.000  ? 106 ASP LLL O   1 
ATOM 17699 C CB  . ASP L 3 106 ? 123.427 9.468   8.664   1.000 28.590  ? 106 ASP LLL CB  1 
ATOM 17700 C CG  . ASP L 3 106 ? 124.504 10.487  8.323   1.000 27.340  ? 106 ASP LLL CG  1 
ATOM 17701 O OD1 . ASP L 3 106 ? 124.628 10.863  7.147   1.000 27.080  ? 106 ASP LLL OD1 1 
ATOM 17702 O OD2 . ASP L 3 106 ? 125.203 10.908  9.249   1.000 24.350  ? 106 ASP LLL OD2 1 
ATOM 17703 N N   . TYR L 3 107 ? 122.231 10.747  6.136   1.000 29.970  ? 107 TYR LLL N   1 
ATOM 17704 C CA  . TYR L 3 107 ? 121.381 11.750  5.472   1.000 29.390  ? 107 TYR LLL CA  1 
ATOM 17705 C C   . TYR L 3 107 ? 121.309 11.446  3.979   1.000 29.320  ? 107 TYR LLL C   1 
ATOM 17706 O O   . TYR L 3 107 ? 122.352 11.105  3.382   1.000 28.590  ? 107 TYR LLL O   1 
ATOM 17707 C CB  . TYR L 3 107 ? 121.911 13.159  5.705   1.000 30.230  ? 107 TYR LLL CB  1 
ATOM 17708 C CG  . TYR L 3 107 ? 121.725 13.642  7.119   1.000 31.770  ? 107 TYR LLL CG  1 
ATOM 17709 C CD1 . TYR L 3 107 ? 120.497 14.095  7.557   1.000 32.960  ? 107 TYR LLL CD1 1 
ATOM 17710 C CD2 . TYR L 3 107 ? 122.784 13.633  8.021   1.000 32.190  ? 107 TYR LLL CD2 1 
ATOM 17711 C CE1 . TYR L 3 107 ? 120.321 14.534  8.858   1.000 35.690  ? 107 TYR LLL CE1 1 
ATOM 17712 C CE2 . TYR L 3 107 ? 122.629 14.080  9.315   1.000 31.400  ? 107 TYR LLL CE2 1 
ATOM 17713 C CZ  . TYR L 3 107 ? 121.394 14.532  9.729   1.000 34.360  ? 107 TYR LLL CZ  1 
ATOM 17714 O OH  . TYR L 3 107 ? 121.236 15.005  10.989  1.000 41.930  ? 107 TYR LLL OH  1 
ATOM 17715 N N   . TRP L 3 108 ? 120.103 11.576  3.421   1.000 29.410  ? 108 TRP LLL N   1 
ATOM 17716 C CA  . TRP L 3 108 ? 119.793 11.416  1.981   1.000 29.680  ? 108 TRP LLL CA  1 
ATOM 17717 C C   . TRP L 3 108 ? 119.246 12.737  1.428   1.000 29.480  ? 108 TRP LLL C   1 
ATOM 17718 O O   . TRP L 3 108 ? 118.671 13.514  2.183   1.000 24.950  ? 108 TRP LLL O   1 
ATOM 17719 C CB  . TRP L 3 108 ? 118.782 10.278  1.786   1.000 30.300  ? 108 TRP LLL CB  1 
ATOM 17720 C CG  . TRP L 3 108 ? 119.265 8.921   2.191   1.000 26.530  ? 108 TRP LLL CG  1 
ATOM 17721 C CD1 . TRP L 3 108 ? 119.574 8.528   3.453   1.000 26.980  ? 108 TRP LLL CD1 1 
ATOM 17722 C CD2 . TRP L 3 108 ? 119.410 7.757   1.359   1.000 24.110  ? 108 TRP LLL CD2 1 
ATOM 17723 N NE1 . TRP L 3 108 ? 119.928 7.211   3.458   1.000 26.710  ? 108 TRP LLL NE1 1 
ATOM 17724 C CE2 . TRP L 3 108 ? 119.863 6.719   2.188   1.000 24.550  ? 108 TRP LLL CE2 1 
ATOM 17725 C CE3 . TRP L 3 108 ? 119.236 7.494   -0.001  1.000 23.980  ? 108 TRP LLL CE3 1 
ATOM 17726 C CZ2 . TRP L 3 108 ? 120.151 5.445   1.711   1.000 25.270  ? 108 TRP LLL CZ2 1 
ATOM 17727 C CZ3 . TRP L 3 108 ? 119.526 6.238   -0.487  1.000 25.250  ? 108 TRP LLL CZ3 1 
ATOM 17728 C CH2 . TRP L 3 108 ? 119.954 5.221   0.368   1.000 26.430  ? 108 TRP LLL CH2 1 
ATOM 17729 N N   . GLY L 3 109 ? 119.421 12.968  0.134   1.000 35.000  ? 109 GLY LLL N   1 
ATOM 17730 C CA  . GLY L 3 109 ? 118.748 14.061  -0.580  1.000 42.010  ? 109 GLY LLL CA  1 
ATOM 17731 C C   . GLY L 3 109 ? 117.353 13.639  -1.004  1.000 44.790  ? 109 GLY LLL C   1 
ATOM 17732 O O   . GLY L 3 109 ? 116.942 12.540  -0.607  1.000 41.950  ? 109 GLY LLL O   1 
ATOM 17733 N N   . GLN L 3 110 ? 116.665 14.496  -1.773  1.000 45.810  ? 110 GLN LLL N   1 
ATOM 17734 C CA  . GLN L 3 110 ? 115.249 14.303  -2.185  1.000 48.630  ? 110 GLN LLL CA  1 
ATOM 17735 C C   . GLN L 3 110 ? 115.215 13.321  -3.351  1.000 46.340  ? 110 GLN LLL C   1 
ATOM 17736 O O   . GLN L 3 110 ? 114.157 12.723  -3.582  1.000 39.710  ? 110 GLN LLL O   1 
ATOM 17737 C CB  . GLN L 3 110 ? 114.607 15.630  -2.579  1.000 59.440  ? 110 GLN LLL CB  1 
ATOM 17738 C CG  . GLN L 3 110 ? 114.463 16.620  -1.421  1.000 75.350  ? 110 GLN LLL CG  1 
ATOM 17739 C CD  . GLN L 3 110 ? 115.703 17.460  -1.210  1.000 89.260  ? 110 GLN LLL CD  1 
ATOM 17740 O OE1 . GLN L 3 110 ? 116.576 17.528  -2.071  1.000 112.550 ? 110 GLN LLL OE1 1 
ATOM 17741 N NE2 . GLN L 3 110 ? 115.795 18.113  -0.063  1.000 87.600  ? 110 GLN LLL NE2 1 
ATOM 17742 N N   . GLY L 3 111 ? 116.358 13.163  -4.030  1.000 49.600  ? 111 GLY LLL N   1 
ATOM 17743 C CA  . GLY L 3 111 ? 116.520 12.338  -5.246  1.000 47.060  ? 111 GLY LLL CA  1 
ATOM 17744 C C   . GLY L 3 111 ? 116.182 13.123  -6.494  1.000 41.600  ? 111 GLY LLL C   1 
ATOM 17745 O O   . GLY L 3 111 ? 115.407 14.084  -6.365  1.000 40.640  ? 111 GLY LLL O   1 
ATOM 17746 N N   . THR L 3 112 ? 116.755 12.747  -7.641  1.000 40.160  ? 112 THR LLL N   1 
ATOM 17747 C CA  . THR L 3 112 ? 116.467 13.355  -8.968  1.000 42.750  ? 112 THR LLL CA  1 
ATOM 17748 C C   . THR L 3 112 ? 116.215 12.232  -9.972  1.000 40.550  ? 112 THR LLL C   1 
ATOM 17749 O O   . THR L 3 112 ? 116.976 11.255  -9.958  1.000 32.830  ? 112 THR LLL O   1 
ATOM 17750 C CB  . THR L 3 112 ? 117.610 14.267  -9.437  1.000 47.770  ? 112 THR LLL CB  1 
ATOM 17751 O OG1 . THR L 3 112 ? 117.087 14.975  -10.566 1.000 44.680  ? 112 THR LLL OG1 1 
ATOM 17752 C CG2 . THR L 3 112 ? 118.885 13.513  -9.784  1.000 48.480  ? 112 THR LLL CG2 1 
ATOM 17753 N N   . LEU L 3 113 ? 115.183 12.360  -10.804 1.000 46.160  ? 113 LEU LLL N   1 
ATOM 17754 C CA  . LEU L 3 113 ? 114.760 11.254  -11.705 1.000 50.160  ? 113 LEU LLL CA  1 
ATOM 17755 C C   . LEU L 3 113 ? 115.605 11.282  -12.979 1.000 46.300  ? 113 LEU LLL C   1 
ATOM 17756 O O   . LEU L 3 113 ? 115.673 12.347  -13.614 1.000 49.920  ? 113 LEU LLL O   1 
ATOM 17757 C CB  . LEU L 3 113 ? 113.271 11.361  -12.048 1.000 53.920  ? 113 LEU LLL CB  1 
ATOM 17758 C CG  . LEU L 3 113 ? 112.780 10.295  -13.032 1.000 59.670  ? 113 LEU LLL CG  1 
ATOM 17759 C CD1 . LEU L 3 113 ? 113.066 8.901   -12.500 1.000 61.680  ? 113 LEU LLL CD1 1 
ATOM 17760 C CD2 . LEU L 3 113 ? 111.310 10.465  -13.360 1.000 64.490  ? 113 LEU LLL CD2 1 
ATOM 17761 N N   . VAL L 3 114 ? 116.203 10.142  -13.320 1.000 40.870  ? 114 VAL LLL N   1 
ATOM 17762 C CA  . VAL L 3 114 ? 116.891 9.890   -14.613 1.000 43.300  ? 114 VAL LLL CA  1 
ATOM 17763 C C   . VAL L 3 114 ? 116.087 8.834   -15.368 1.000 47.620  ? 114 VAL LLL C   1 
ATOM 17764 O O   . VAL L 3 114 ? 116.043 7.685   -14.916 1.000 52.570  ? 114 VAL LLL O   1 
ATOM 17765 C CB  . VAL L 3 114 ? 118.346 9.430   -14.402 1.000 45.930  ? 114 VAL LLL CB  1 
ATOM 17766 C CG1 . VAL L 3 114 ? 118.969 8.825   -15.658 1.000 45.810  ? 114 VAL LLL CG1 1 
ATOM 17767 C CG2 . VAL L 3 114 ? 119.211 10.550  -13.848 1.000 48.680  ? 114 VAL LLL CG2 1 
ATOM 17768 N N   . THR L 3 115 ? 115.469 9.228   -16.478 1.000 52.670  ? 115 THR LLL N   1 
ATOM 17769 C CA  . THR L 3 115 ? 114.707 8.349   -17.397 1.000 52.040  ? 115 THR LLL CA  1 
ATOM 17770 C C   . THR L 3 115 ? 115.501 8.157   -18.695 1.000 48.070  ? 115 THR LLL C   1 
ATOM 17771 O O   . THR L 3 115 ? 115.776 9.163   -19.378 1.000 51.710  ? 115 THR LLL O   1 
ATOM 17772 C CB  . THR L 3 115 ? 113.339 8.980   -17.652 1.000 53.770  ? 115 THR LLL CB  1 
ATOM 17773 O OG1 . THR L 3 115 ? 112.938 9.685   -16.462 1.000 51.780  ? 115 THR LLL OG1 1 
ATOM 17774 C CG2 . THR L 3 115 ? 112.323 7.937   -18.068 1.000 58.340  ? 115 THR LLL CG2 1 
ATOM 17775 N N   . VAL L 3 116 ? 115.884 6.921   -18.992 1.000 50.730  ? 116 VAL LLL N   1 
ATOM 17776 C CA  . VAL L 3 116 ? 116.670 6.545   -20.208 1.000 63.000  ? 116 VAL LLL CA  1 
ATOM 17777 C C   . VAL L 3 116 ? 115.767 5.754   -21.162 1.000 72.030  ? 116 VAL LLL C   1 
ATOM 17778 O O   . VAL L 3 116 ? 115.512 4.550   -20.896 1.000 71.560  ? 116 VAL LLL O   1 
ATOM 17779 C CB  . VAL L 3 116 ? 117.936 5.733   -19.874 1.000 63.110  ? 116 VAL LLL CB  1 
ATOM 17780 C CG1 . VAL L 3 116 ? 118.580 5.163   -21.124 1.000 67.510  ? 116 VAL LLL CG1 1 
ATOM 17781 C CG2 . VAL L 3 116 ? 118.954 6.546   -19.112 1.000 65.620  ? 116 VAL LLL CG2 1 
ATOM 17782 N N   . SER L 3 117 ? 115.345 6.407   -22.250 1.000 78.990  ? 117 SER LLL N   1 
ATOM 17783 C CA  . SER L 3 117 ? 114.276 5.971   -23.182 1.000 82.570  ? 117 SER LLL CA  1 
ATOM 17784 C C   . SER L 3 117 ? 114.559 6.556   -24.570 1.000 87.510  ? 117 SER LLL C   1 
ATOM 17785 O O   . SER L 3 117 ? 115.205 7.603   -24.617 1.000 87.630  ? 117 SER LLL O   1 
ATOM 17786 C CB  . SER L 3 117 ? 112.914 6.424   -22.642 1.000 79.550  ? 117 SER LLL CB  1 
ATOM 17787 O OG  . SER L 3 117 ? 111.867 5.852   -23.396 1.000 70.480  ? 117 SER LLL OG  1 
ATOM 17788 N N   . SER L 3 118 ? 114.131 5.895   -25.654 1.000 85.660  ? 118 SER LLL N   1 
ATOM 17789 C CA  . SER L 3 118 ? 114.101 6.440   -27.042 1.000 75.310  ? 118 SER LLL CA  1 
ATOM 17790 C C   . SER L 3 118 ? 112.991 7.503   -27.164 1.000 71.620  ? 118 SER LLL C   1 
ATOM 17791 O O   . SER L 3 118 ? 113.163 8.459   -27.935 1.000 75.150  ? 118 SER LLL O   1 
ATOM 17792 C CB  . SER L 3 118 ? 113.935 5.335   -28.052 1.000 72.520  ? 118 SER LLL CB  1 
ATOM 17793 O OG  . SER L 3 118 ? 115.139 4.604   -28.200 1.000 69.990  ? 118 SER LLL OG  1 
ATOM 17794 N N   . ALA L 3 119 ? 111.913 7.330   -26.402 1.000 65.990  ? 119 ALA LLL N   1 
ATOM 17795 C CA  . ALA L 3 119 ? 110.759 8.245   -26.259 1.000 68.480  ? 119 ALA LLL CA  1 
ATOM 17796 C C   . ALA L 3 119 ? 111.207 9.710   -26.155 1.000 68.100  ? 119 ALA LLL C   1 
ATOM 17797 O O   . ALA L 3 119 ? 112.183 10.005  -25.442 1.000 65.380  ? 119 ALA LLL O   1 
ATOM 17798 C CB  . ALA L 3 119 ? 109.919 7.857   -25.057 1.000 72.830  ? 119 ALA LLL CB  1 
ATOM 17799 N N   . SER L 3 120 ? 110.454 10.575  -26.830 1.000 71.490  ? 120 SER LLL N   1 
ATOM 17800 C CA  . SER L 3 120 ? 110.671 12.031  -26.999 1.000 68.830  ? 120 SER LLL CA  1 
ATOM 17801 C C   . SER L 3 120 ? 109.794 12.795  -26.006 1.000 70.100  ? 120 SER LLL C   1 
ATOM 17802 O O   . SER L 3 120 ? 108.809 12.214  -25.500 1.000 67.100  ? 120 SER LLL O   1 
ATOM 17803 C CB  . SER L 3 120 ? 110.376 12.442  -28.420 1.000 65.600  ? 120 SER LLL CB  1 
ATOM 17804 O OG  . SER L 3 120 ? 110.892 11.477  -29.341 1.000 70.620  ? 120 SER LLL OG  1 
ATOM 17805 N N   . THR L 3 121 ? 110.163 14.050  -25.744 1.000 82.070  ? 121 THR LLL N   1 
ATOM 17806 C CA  . THR L 3 121 ? 109.684 14.871  -24.593 1.000 89.630  ? 121 THR LLL CA  1 
ATOM 17807 C C   . THR L 3 121 ? 108.299 15.463  -24.919 1.000 98.050  ? 121 THR LLL C   1 
ATOM 17808 O O   . THR L 3 121 ? 108.266 16.675  -25.271 1.000 108.370 ? 121 THR LLL O   1 
ATOM 17809 C CB  . THR L 3 121 ? 110.745 15.931  -24.235 1.000 82.210  ? 121 THR LLL CB  1 
ATOM 17810 O OG1 . THR L 3 121 ? 112.020 15.317  -24.049 1.000 77.330  ? 121 THR LLL OG1 1 
ATOM 17811 C CG2 . THR L 3 121 ? 110.424 16.715  -22.984 1.000 78.560  ? 121 THR LLL CG2 1 
ATOM 17812 N N   . LYS L 3 122 ? 107.207 14.675  -24.832 1.000 87.420  ? 122 LYS LLL N   1 
ATOM 17813 C CA  . LYS L 3 122 ? 105.837 15.123  -25.219 1.000 84.830  ? 122 LYS LLL CA  1 
ATOM 17814 C C   . LYS L 3 122 ? 105.311 16.125  -24.179 1.000 93.570  ? 122 LYS LLL C   1 
ATOM 17815 O O   . LYS L 3 122 ? 105.461 15.854  -22.965 1.000 100.400 ? 122 LYS LLL O   1 
ATOM 17816 C CB  . LYS L 3 122 ? 104.880 13.939  -25.392 1.000 78.590  ? 122 LYS LLL CB  1 
ATOM 17817 N N   . GLY L 3 123 ? 104.806 17.275  -24.639 1.000 102.410 ? 123 GLY LLL N   1 
ATOM 17818 C CA  . GLY L 3 123 ? 104.233 18.321  -23.775 1.000 98.390  ? 123 GLY LLL CA  1 
ATOM 17819 C C   . GLY L 3 123 ? 102.814 17.926  -23.390 1.000 95.990  ? 123 GLY LLL C   1 
ATOM 17820 O O   . GLY L 3 123 ? 102.169 17.185  -24.129 1.000 85.980  ? 123 GLY LLL O   1 
ATOM 17821 N N   . PRO L 3 124 ? 102.302 18.378  -22.222 1.000 94.230  ? 124 PRO LLL N   1 
ATOM 17822 C CA  . PRO L 3 124 ? 100.926 18.102  -21.824 1.000 93.720  ? 124 PRO LLL CA  1 
ATOM 17823 C C   . PRO L 3 124 ? 99.911  18.991  -22.560 1.000 96.500  ? 124 PRO LLL C   1 
ATOM 17824 O O   . PRO L 3 124 ? 100.320 19.893  -23.267 1.000 110.110 ? 124 PRO LLL O   1 
ATOM 17825 C CB  . PRO L 3 124 ? 100.923 18.455  -20.330 1.000 95.400  ? 124 PRO LLL CB  1 
ATOM 17826 C CG  . PRO L 3 124 ? 101.966 19.535  -20.194 1.000 91.990  ? 124 PRO LLL CG  1 
ATOM 17827 C CD  . PRO L 3 124 ? 103.021 19.189  -21.228 1.000 94.110  ? 124 PRO LLL CD  1 
ATOM 17828 N N   . SER L 3 125 ? 98.617  18.714  -22.354 1.000 93.690  ? 125 SER LLL N   1 
ATOM 17829 C CA  . SER L 3 125 ? 97.480  19.626  -22.649 1.000 93.460  ? 125 SER LLL CA  1 
ATOM 17830 C C   . SER L 3 125 ? 96.606  19.753  -21.394 1.000 90.810  ? 125 SER LLL C   1 
ATOM 17831 O O   . SER L 3 125 ? 96.277  18.689  -20.819 1.000 97.020  ? 125 SER LLL O   1 
ATOM 17832 C CB  . SER L 3 125 ? 96.701  19.137  -23.840 1.000 86.580  ? 125 SER LLL CB  1 
ATOM 17833 O OG  . SER L 3 125 ? 97.307  19.559  -25.050 1.000 81.600  ? 125 SER LLL OG  1 
ATOM 17834 N N   . VAL L 3 126 ? 96.303  20.990  -20.984 1.000 84.920  ? 126 VAL LLL N   1 
ATOM 17835 C CA  . VAL L 3 126 ? 95.569  21.321  -19.728 1.000 93.820  ? 126 VAL LLL CA  1 
ATOM 17836 C C   . VAL L 3 126 ? 94.098  21.612  -20.077 1.000 98.220  ? 126 VAL LLL C   1 
ATOM 17837 O O   . VAL L 3 126 ? 93.218  21.282  -19.248 1.000 93.120  ? 126 VAL LLL O   1 
ATOM 17838 C CB  . VAL L 3 126 ? 96.246  22.478  -18.953 1.000 102.500 ? 126 VAL LLL CB  1 
ATOM 17839 C CG1 . VAL L 3 126 ? 96.296  23.798  -19.728 1.000 107.960 ? 126 VAL LLL CG1 1 
ATOM 17840 C CG2 . VAL L 3 126 ? 95.613  22.686  -17.580 1.000 97.160  ? 126 VAL LLL CG2 1 
ATOM 17841 N N   . CYS L 3 145 ? 91.730  21.102  -12.990 1.000 90.630  ? 150 CYS LLL N   1 
ATOM 17842 C CA  . CYS L 3 145 ? 92.541  20.925  -14.231 1.000 91.960  ? 150 CYS LLL CA  1 
ATOM 17843 C C   . CYS L 3 145 ? 92.685  19.428  -14.545 1.000 87.220  ? 150 CYS LLL C   1 
ATOM 17844 O O   . CYS L 3 145 ? 92.686  18.619  -13.587 1.000 94.540  ? 150 CYS LLL O   1 
ATOM 17845 C CB  . CYS L 3 145 ? 93.944  21.529  -14.111 1.000 89.550  ? 150 CYS LLL CB  1 
ATOM 17846 S SG  . CYS L 3 145 ? 94.005  23.321  -13.827 1.000 80.020  ? 150 CYS LLL SG  1 
ATOM 17847 N N   . LEU L 3 146 ? 92.827  19.084  -15.833 1.000 83.490  ? 151 LEU LLL N   1 
ATOM 17848 C CA  . LEU L 3 146 ? 93.385  17.792  -16.331 1.000 88.820  ? 151 LEU LLL CA  1 
ATOM 17849 C C   . LEU L 3 146 ? 94.757  18.079  -16.958 1.000 95.510  ? 151 LEU LLL C   1 
ATOM 17850 O O   . LEU L 3 146 ? 94.926  19.143  -17.564 1.000 115.870 ? 151 LEU LLL O   1 
ATOM 17851 C CB  . LEU L 3 146 ? 92.435  17.165  -17.361 1.000 87.330  ? 151 LEU LLL CB  1 
ATOM 17852 C CG  . LEU L 3 146 ? 92.930  15.902  -18.099 1.000 82.470  ? 151 LEU LLL CG  1 
ATOM 17853 C CD1 . LEU L 3 146 ? 92.743  14.641  -17.262 1.000 83.340  ? 151 LEU LLL CD1 1 
ATOM 17854 C CD2 . LEU L 3 146 ? 92.244  15.716  -19.445 1.000 74.980  ? 151 LEU LLL CD2 1 
ATOM 17855 N N   . VAL L 3 147 ? 95.696  17.141  -16.841 1.000 95.860  ? 152 VAL LLL N   1 
ATOM 17856 C CA  . VAL L 3 147 ? 97.008  17.149  -17.585 1.000 98.700  ? 152 VAL LLL CA  1 
ATOM 17857 C C   . VAL L 3 147 ? 97.083  15.864  -18.430 1.000 98.430  ? 152 VAL LLL C   1 
ATOM 17858 O O   . VAL L 3 147 ? 97.240  14.773  -17.839 1.000 80.550  ? 152 VAL LLL O   1 
ATOM 17859 C CB  . VAL L 3 147 ? 98.203  17.304  -16.636 1.000 99.280  ? 152 VAL LLL CB  1 
ATOM 17860 C CG1 . VAL L 3 147 ? 99.479  17.586  -17.424 1.000 100.350 ? 152 VAL LLL CG1 1 
ATOM 17861 C CG2 . VAL L 3 147 ? 97.985  18.370  -15.565 1.000 89.050  ? 152 VAL LLL CG2 1 
ATOM 17862 N N   . LYS L 3 148 ? 96.895  15.975  -19.752 1.000 106.820 ? 153 LYS LLL N   1 
ATOM 17863 C CA  . LYS L 3 148 ? 96.684  14.808  -20.666 1.000 107.880 ? 153 LYS LLL CA  1 
ATOM 17864 C C   . LYS L 3 148 ? 97.918  14.606  -21.551 1.000 100.870 ? 153 LYS LLL C   1 
ATOM 17865 O O   . LYS L 3 148 ? 98.525  15.614  -21.950 1.000 92.280  ? 153 LYS LLL O   1 
ATOM 17866 C CB  . LYS L 3 148 ? 95.426  14.960  -21.533 1.000 95.800  ? 153 LYS LLL CB  1 
ATOM 17867 N N   . ASP L 3 149 ? 98.287  13.342  -21.755 1.000 100.400 ? 154 ASP LLL N   1 
ATOM 17868 C CA  . ASP L 3 149 ? 99.353  12.821  -22.653 1.000 109.100 ? 154 ASP LLL CA  1 
ATOM 17869 C C   . ASP L 3 149 ? 100.621 13.698  -22.604 1.000 127.730 ? 154 ASP LLL C   1 
ATOM 17870 O O   . ASP L 3 149 ? 100.910 14.394  -23.593 1.000 148.450 ? 154 ASP LLL O   1 
ATOM 17871 C CB  . ASP L 3 149 ? 98.740  12.570  -24.031 1.000 99.600  ? 154 ASP LLL CB  1 
ATOM 17872 C CG  . ASP L 3 149 ? 97.645  11.504  -24.006 1.000 92.320  ? 154 ASP LLL CG  1 
ATOM 17873 O OD1 . ASP L 3 149 ? 97.886  10.392  -23.477 1.000 89.330  ? 154 ASP LLL OD1 1 
ATOM 17874 O OD2 . ASP L 3 149 ? 96.549  11.781  -24.521 1.000 95.720  ? 154 ASP LLL OD2 1 
ATOM 17875 N N   . TYR L 3 150 ? 101.382 13.587  -21.504 1.000 130.990 ? 155 TYR LLL N   1 
ATOM 17876 C CA  . TYR L 3 150 ? 102.722 14.205  -21.270 1.000 123.080 ? 155 TYR LLL CA  1 
ATOM 17877 C C   . TYR L 3 150 ? 103.768 13.117  -20.966 1.000 117.970 ? 155 TYR LLL C   1 
ATOM 17878 O O   . TYR L 3 150 ? 103.375 11.993  -20.603 1.000 111.250 ? 155 TYR LLL O   1 
ATOM 17879 C CB  . TYR L 3 150 ? 102.656 15.219  -20.122 1.000 117.370 ? 155 TYR LLL CB  1 
ATOM 17880 C CG  . TYR L 3 150 ? 102.539 14.640  -18.729 1.000 112.640 ? 155 TYR LLL CG  1 
ATOM 17881 C CD1 . TYR L 3 150 ? 103.639 14.172  -18.028 1.000 106.390 ? 155 TYR LLL CD1 1 
ATOM 17882 C CD2 . TYR L 3 150 ? 101.312 14.577  -18.097 1.000 119.670 ? 155 TYR LLL CD2 1 
ATOM 17883 C CE1 . TYR L 3 150 ? 103.508 13.650  -16.752 1.000 105.610 ? 155 TYR LLL CE1 1 
ATOM 17884 C CE2 . TYR L 3 150 ? 101.161 14.062  -16.818 1.000 118.800 ? 155 TYR LLL CE2 1 
ATOM 17885 C CZ  . TYR L 3 150 ? 102.269 13.595  -16.141 1.000 108.680 ? 155 TYR LLL CZ  1 
ATOM 17886 O OH  . TYR L 3 150 ? 102.115 13.082  -14.884 1.000 114.900 ? 155 TYR LLL OH  1 
ATOM 17887 N N   . PHE L 3 151 ? 105.062 13.453  -21.075 1.000 109.140 ? 156 PHE LLL N   1 
ATOM 17888 C CA  . PHE L 3 151 ? 106.223 12.548  -20.855 1.000 100.420 ? 156 PHE LLL CA  1 
ATOM 17889 C C   . PHE L 3 151 ? 107.488 13.386  -20.692 1.000 99.360  ? 156 PHE LLL C   1 
ATOM 17890 O O   . PHE L 3 151 ? 107.633 14.375  -21.406 1.000 95.910  ? 156 PHE LLL O   1 
ATOM 17891 C CB  . PHE L 3 151 ? 106.397 11.616  -22.054 1.000 97.040  ? 156 PHE LLL CB  1 
ATOM 17892 C CG  . PHE L 3 151 ? 107.360 10.484  -21.827 1.000 100.150 ? 156 PHE LLL CG  1 
ATOM 17893 C CD1 . PHE L 3 151 ? 107.018 9.414   -21.017 1.000 100.560 ? 156 PHE LLL CD1 1 
ATOM 17894 C CD2 . PHE L 3 151 ? 108.600 10.475  -22.434 1.000 96.210  ? 156 PHE LLL CD2 1 
ATOM 17895 C CE1 . PHE L 3 151 ? 107.883 8.340   -20.849 1.000 96.800  ? 156 PHE LLL CE1 1 
ATOM 17896 C CE2 . PHE L 3 151 ? 109.462 9.398   -22.268 1.000 95.680  ? 156 PHE LLL CE2 1 
ATOM 17897 C CZ  . PHE L 3 151 ? 109.110 8.339   -21.466 1.000 92.070  ? 156 PHE LLL CZ  1 
ATOM 17898 N N   . PRO L 3 152 ? 108.437 13.077  -19.769 1.000 101.650 ? 157 PRO LLL N   1 
ATOM 17899 C CA  . PRO L 3 152 ? 108.262 12.075  -18.707 1.000 96.960  ? 157 PRO LLL CA  1 
ATOM 17900 C C   . PRO L 3 152 ? 107.597 12.602  -17.414 1.000 90.080  ? 157 PRO LLL C   1 
ATOM 17901 O O   . PRO L 3 152 ? 106.983 13.644  -17.469 1.000 87.630  ? 157 PRO LLL O   1 
ATOM 17902 C CB  . PRO L 3 152 ? 109.702 11.624  -18.440 1.000 101.270 ? 157 PRO LLL CB  1 
ATOM 17903 C CG  . PRO L 3 152 ? 110.528 12.870  -18.714 1.000 113.220 ? 157 PRO LLL CG  1 
ATOM 17904 C CD  . PRO L 3 152 ? 109.800 13.639  -19.796 1.000 110.430 ? 157 PRO LLL CD  1 
ATOM 17905 N N   . GLU L 3 153 ? 107.758 11.900  -16.285 1.000 86.100  ? 158 GLU LLL N   1 
ATOM 17906 C CA  . GLU L 3 153 ? 106.809 11.870  -15.127 1.000 94.690  ? 158 GLU LLL CA  1 
ATOM 17907 C C   . GLU L 3 153 ? 106.675 13.221  -14.408 1.000 97.640  ? 158 GLU LLL C   1 
ATOM 17908 O O   . GLU L 3 153 ? 105.558 13.661  -14.158 1.000 123.120 ? 158 GLU LLL O   1 
ATOM 17909 C CB  . GLU L 3 153 ? 107.204 10.750  -14.158 1.000 95.860  ? 158 GLU LLL CB  1 
ATOM 17910 C CG  . GLU L 3 153 ? 106.387 10.711  -12.871 1.000 99.480  ? 158 GLU LLL CG  1 
ATOM 17911 C CD  . GLU L 3 153 ? 104.869 10.627  -12.997 1.000 98.240  ? 158 GLU LLL CD  1 
ATOM 17912 O OE1 . GLU L 3 153 ? 104.218 11.690  -13.030 1.000 85.910  ? 158 GLU LLL OE1 1 
ATOM 17913 O OE2 . GLU L 3 153 ? 104.329 9.493   -12.996 1.000 96.380  ? 158 GLU LLL OE2 1 
ATOM 17914 N N   . PRO L 3 154 ? 107.766 13.921  -14.024 1.000 84.240  ? 159 PRO LLL N   1 
ATOM 17915 C CA  . PRO L 3 154 ? 107.655 14.974  -13.001 1.000 76.080  ? 159 PRO LLL CA  1 
ATOM 17916 C C   . PRO L 3 154 ? 106.845 16.220  -13.420 1.000 79.300  ? 159 PRO LLL C   1 
ATOM 17917 O O   . PRO L 3 154 ? 107.339 17.033  -14.183 1.000 84.820  ? 159 PRO LLL O   1 
ATOM 17918 C CB  . PRO L 3 154 ? 109.122 15.309  -12.695 1.000 80.230  ? 159 PRO LLL CB  1 
ATOM 17919 C CG  . PRO L 3 154 ? 109.894 14.913  -13.955 1.000 86.500  ? 159 PRO LLL CG  1 
ATOM 17920 C CD  . PRO L 3 154 ? 109.128 13.756  -14.559 1.000 81.370  ? 159 PRO LLL CD  1 
ATOM 17921 N N   . VAL L 3 155 ? 105.613 16.356  -12.910 1.000 83.880  ? 160 VAL LLL N   1 
ATOM 17922 C CA  . VAL L 3 155 ? 104.644 17.449  -13.256 1.000 90.670  ? 160 VAL LLL CA  1 
ATOM 17923 C C   . VAL L 3 155 ? 104.059 18.083  -11.976 1.000 90.190  ? 160 VAL LLL C   1 
ATOM 17924 O O   . VAL L 3 155 ? 103.643 17.339  -11.075 1.000 92.660  ? 160 VAL LLL O   1 
ATOM 17925 C CB  . VAL L 3 155 ? 103.524 16.916  -14.176 1.000 99.110  ? 160 VAL LLL CB  1 
ATOM 17926 C CG1 . VAL L 3 155 ? 102.530 16.058  -13.418 1.000 107.500 ? 160 VAL LLL CG1 1 
ATOM 17927 C CG2 . VAL L 3 155 ? 102.799 18.043  -14.894 1.000 96.460  ? 160 VAL LLL CG2 1 
ATOM 17928 N N   . THR L 3 156 ? 103.966 19.420  -11.939 1.000 93.130  ? 161 THR LLL N   1 
ATOM 17929 C CA  . THR L 3 156 ? 103.606 20.278  -10.766 1.000 93.480  ? 161 THR LLL CA  1 
ATOM 17930 C C   . THR L 3 156 ? 102.201 20.889  -10.949 1.000 95.860  ? 161 THR LLL C   1 
ATOM 17931 O O   . THR L 3 156 ? 101.818 21.180  -12.100 1.000 108.960 ? 161 THR LLL O   1 
ATOM 17932 C CB  . THR L 3 156 ? 104.686 21.362  -10.581 1.000 92.890  ? 161 THR LLL CB  1 
ATOM 17933 O OG1 . THR L 3 156 ? 105.905 20.717  -10.199 1.000 84.010  ? 161 THR LLL OG1 1 
ATOM 17934 C CG2 . THR L 3 156 ? 104.350 22.450  -9.579  1.000 85.500  ? 161 THR LLL CG2 1 
ATOM 17935 N N   . VAL L 3 157 ? 101.512 21.187  -9.842  1.000 98.980  ? 162 VAL LLL N   1 
ATOM 17936 C CA  . VAL L 3 157 ? 100.067 21.561  -9.783  1.000 93.800  ? 162 VAL LLL CA  1 
ATOM 17937 C C   . VAL L 3 157 ? 99.898  23.085  -9.610  1.000 89.400  ? 162 VAL LLL C   1 
ATOM 17938 O O   . VAL L 3 157 ? 100.540 23.653  -8.707  1.000 77.310  ? 162 VAL LLL O   1 
ATOM 17939 C CB  . VAL L 3 157 ? 99.364  20.765  -8.663  1.000 92.820  ? 162 VAL LLL CB  1 
ATOM 17940 C CG1 . VAL L 3 157 ? 99.964  20.992  -7.267  1.000 78.230  ? 162 VAL LLL CG1 1 
ATOM 17941 C CG2 . VAL L 3 157 ? 97.865  21.032  -8.672  1.000 96.250  ? 162 VAL LLL CG2 1 
ATOM 17942 N N   . HIS L 3 169 ? 93.945  18.851  -3.346  1.000 85.980  ? 174 HIS LLL N   1 
ATOM 17943 C CA  . HIS L 3 169 ? 94.257  17.394  -3.419  1.000 96.430  ? 174 HIS LLL CA  1 
ATOM 17944 C C   . HIS L 3 169 ? 94.539  16.943  -4.874  1.000 108.060 ? 174 HIS LLL C   1 
ATOM 17945 O O   . HIS L 3 169 ? 93.568  16.850  -5.666  1.000 121.390 ? 174 HIS LLL O   1 
ATOM 17946 C CB  . HIS L 3 169 ? 93.120  16.581  -2.775  1.000 93.290  ? 174 HIS LLL CB  1 
ATOM 17947 C CG  . HIS L 3 169 ? 93.452  15.130  -2.677  1.000 99.360  ? 174 HIS LLL CG  1 
ATOM 17948 N ND1 . HIS L 3 169 ? 93.148  14.221  -3.678  1.000 96.280  ? 174 HIS LLL ND1 1 
ATOM 17949 C CD2 . HIS L 3 169 ? 94.109  14.437  -1.723  1.000 101.300 ? 174 HIS LLL CD2 1 
ATOM 17950 C CE1 . HIS L 3 169 ? 93.585  13.027  -3.334  1.000 92.330  ? 174 HIS LLL CE1 1 
ATOM 17951 N NE2 . HIS L 3 169 ? 94.181  13.135  -2.139  1.000 101.000 ? 174 HIS LLL NE2 1 
ATOM 17952 N N   . THR L 3 170 ? 95.816  16.702  -5.229  1.000 101.380 ? 175 THR LLL N   1 
ATOM 17953 C CA  . THR L 3 170 ? 96.307  16.230  -6.568  1.000 93.390  ? 175 THR LLL CA  1 
ATOM 17954 C C   . THR L 3 170 ? 96.285  14.697  -6.591  1.000 96.150  ? 175 THR LLL C   1 
ATOM 17955 O O   . THR L 3 170 ? 96.610  14.128  -5.555  1.000 107.760 ? 175 THR LLL O   1 
ATOM 17956 C CB  . THR L 3 170 ? 97.724  16.745  -6.891  1.000 88.140  ? 175 THR LLL CB  1 
ATOM 17957 O OG1 . THR L 3 170 ? 97.839  18.164  -6.754  1.000 74.780  ? 175 THR LLL OG1 1 
ATOM 17958 C CG2 . THR L 3 170 ? 98.157  16.405  -8.302  1.000 86.870  ? 175 THR LLL CG2 1 
ATOM 17959 N N   . PHE L 3 171 ? 95.947  14.060  -7.724  1.000 93.100  ? 176 PHE LLL N   1 
ATOM 17960 C CA  . PHE L 3 171 ? 95.950  12.582  -7.926  1.000 88.770  ? 176 PHE LLL CA  1 
ATOM 17961 C C   . PHE L 3 171 ? 97.297  12.141  -8.510  1.000 86.120  ? 176 PHE LLL C   1 
ATOM 17962 O O   . PHE L 3 171 ? 97.952  12.906  -9.211  1.000 75.200  ? 176 PHE LLL O   1 
ATOM 17963 C CB  . PHE L 3 171 ? 94.770  12.168  -8.820  1.000 73.980  ? 176 PHE LLL CB  1 
ATOM 17964 N N   . PRO L 3 172 ? 97.759  10.891  -8.266  1.000 91.590  ? 177 PRO LLL N   1 
ATOM 17965 C CA  . PRO L 3 172 ? 98.913  10.344  -8.977  1.000 88.040  ? 177 PRO LLL CA  1 
ATOM 17966 C C   . PRO L 3 172 ? 98.546  10.077  -10.443 1.000 91.440  ? 177 PRO LLL C   1 
ATOM 17967 O O   . PRO L 3 172 ? 97.389  9.797   -10.738 1.000 103.430 ? 177 PRO LLL O   1 
ATOM 17968 C CB  . PRO L 3 172 ? 99.234  9.034   -8.241  1.000 88.420  ? 177 PRO LLL CB  1 
ATOM 17969 C CG  . PRO L 3 172 ? 97.900  8.609   -7.666  1.000 96.790  ? 177 PRO LLL CG  1 
ATOM 17970 C CD  . PRO L 3 172 ? 97.172  9.906   -7.342  1.000 99.070  ? 177 PRO LLL CD  1 
ATOM 17971 N N   . ALA L 3 173 ? 99.539  10.149  -11.324 1.000 96.400  ? 178 ALA LLL N   1 
ATOM 17972 C CA  . ALA L 3 173 ? 99.391  9.962   -12.786 1.000 98.380  ? 178 ALA LLL CA  1 
ATOM 17973 C C   . ALA L 3 173 ? 99.005  8.509   -13.111 1.000 86.630  ? 178 ALA LLL C   1 
ATOM 17974 O O   . ALA L 3 173 ? 99.053  7.663   -12.229 1.000 80.890  ? 178 ALA LLL O   1 
ATOM 17975 C CB  . ALA L 3 173 ? 100.667 10.376  -13.487 1.000 104.930 ? 178 ALA LLL CB  1 
ATOM 17976 N N   . VAL L 3 174 ? 98.603  8.257   -14.354 1.000 84.710  ? 179 VAL LLL N   1 
ATOM 17977 C CA  . VAL L 3 174 ? 98.442  6.897   -14.944 1.000 88.230  ? 179 VAL LLL CA  1 
ATOM 17978 C C   . VAL L 3 174 ? 99.393  6.811   -16.132 1.000 84.950  ? 179 VAL LLL C   1 
ATOM 17979 O O   . VAL L 3 174 ? 99.410  7.788   -16.895 1.000 86.640  ? 179 VAL LLL O   1 
ATOM 17980 C CB  . VAL L 3 174 ? 96.994  6.634   -15.398 1.000 98.530  ? 179 VAL LLL CB  1 
ATOM 17981 C CG1 . VAL L 3 174 ? 96.676  5.143   -15.391 1.000 97.570  ? 179 VAL LLL CG1 1 
ATOM 17982 C CG2 . VAL L 3 174 ? 96.003  7.446   -14.573 1.000 106.930 ? 179 VAL LLL CG2 1 
ATOM 17983 N N   . LEU L 3 175 ? 100.122 5.699   -16.275 1.000 85.970  ? 180 LEU LLL N   1 
ATOM 17984 C CA  . LEU L 3 175 ? 100.942 5.366   -17.481 1.000 83.180  ? 180 LEU LLL CA  1 
ATOM 17985 C C   . LEU L 3 175 ? 100.026 4.642   -18.467 1.000 94.890  ? 180 LEU LLL C   1 
ATOM 17986 O O   . LEU L 3 175 ? 99.828  3.424   -18.290 1.000 102.510 ? 180 LEU LLL O   1 
ATOM 17987 C CB  . LEU L 3 175 ? 102.142 4.500   -17.101 1.000 65.470  ? 180 LEU LLL CB  1 
ATOM 17988 N N   . GLN L 3 176 ? 99.460  5.373   -19.438 1.000 100.300 ? 181 GLN LLL N   1 
ATOM 17989 C CA  . GLN L 3 176 ? 98.657  4.799   -20.549 1.000 96.410  ? 181 GLN LLL CA  1 
ATOM 17990 C C   . GLN L 3 176 ? 99.581  3.887   -21.381 1.000 97.610  ? 181 GLN LLL C   1 
ATOM 17991 O O   . GLN L 3 176 ? 100.822 4.100   -21.348 1.000 103.640 ? 181 GLN LLL O   1 
ATOM 17992 C CB  . GLN L 3 176 ? 97.979  5.919   -21.353 1.000 89.180  ? 181 GLN LLL CB  1 
ATOM 17993 C CG  . GLN L 3 176 ? 96.884  5.406   -22.289 1.000 87.890  ? 181 GLN LLL CG  1 
ATOM 17994 C CD  . GLN L 3 176 ? 95.788  4.659   -21.556 1.000 83.980  ? 181 GLN LLL CD  1 
ATOM 17995 O OE1 . GLN L 3 176 ? 95.695  3.426   -21.561 1.000 69.100  ? 181 GLN LLL OE1 1 
ATOM 17996 N NE2 . GLN L 3 176 ? 94.945  5.417   -20.879 1.000 78.490  ? 181 GLN LLL NE2 1 
ATOM 17997 N N   . SER L 3 177 ? 99.017  2.887   -22.075 1.000 90.810  ? 182 SER LLL N   1 
ATOM 17998 C CA  . SER L 3 177 ? 99.758  1.950   -22.962 1.000 83.270  ? 182 SER LLL CA  1 
ATOM 17999 C C   . SER L 3 177 ? 100.456 2.719   -24.096 1.000 87.620  ? 182 SER LLL C   1 
ATOM 18000 O O   . SER L 3 177 ? 101.432 2.173   -24.651 1.000 80.550  ? 182 SER LLL O   1 
ATOM 18001 C CB  . SER L 3 177 ? 98.858  0.885   -23.510 1.000 75.180  ? 182 SER LLL CB  1 
ATOM 18002 O OG  . SER L 3 177 ? 99.638  -0.149  -24.069 1.000 71.160  ? 182 SER LLL OG  1 
ATOM 18003 N N   . SER L 3 178 ? 99.979  3.934   -24.419 1.000 91.040  ? 183 SER LLL N   1 
ATOM 18004 C CA  . SER L 3 178 ? 100.579 4.874   -25.404 1.000 91.410  ? 183 SER LLL CA  1 
ATOM 18005 C C   . SER L 3 178 ? 102.010 5.270   -24.991 1.000 110.690 ? 183 SER LLL C   1 
ATOM 18006 O O   . SER L 3 178 ? 102.775 5.756   -25.859 1.000 114.000 ? 183 SER LLL O   1 
ATOM 18007 C CB  . SER L 3 178 ? 99.695  6.091   -25.584 1.000 83.500  ? 183 SER LLL CB  1 
ATOM 18008 O OG  . SER L 3 178 ? 99.244  6.602   -24.336 1.000 74.250  ? 183 SER LLL OG  1 
ATOM 18009 N N   . GLY L 3 179 ? 102.365 5.072   -23.719 1.000 114.560 ? 184 GLY LLL N   1 
ATOM 18010 C CA  . GLY L 3 179 ? 103.663 5.475   -23.148 1.000 102.230 ? 184 GLY LLL CA  1 
ATOM 18011 C C   . GLY L 3 179 ? 103.605 6.900   -22.628 1.000 93.980  ? 184 GLY LLL C   1 
ATOM 18012 O O   . GLY L 3 179 ? 104.657 7.398   -22.205 1.000 92.890  ? 184 GLY LLL O   1 
ATOM 18013 N N   . LEU L 3 180 ? 102.424 7.536   -22.689 1.000 90.090  ? 185 LEU LLL N   1 
ATOM 18014 C CA  . LEU L 3 180 ? 102.169 8.928   -22.221 1.000 91.680  ? 185 LEU LLL CA  1 
ATOM 18015 C C   . LEU L 3 180 ? 101.416 8.894   -20.884 1.000 89.300  ? 185 LEU LLL C   1 
ATOM 18016 O O   . LEU L 3 180 ? 100.494 8.073   -20.745 1.000 84.090  ? 185 LEU LLL O   1 
ATOM 18017 C CB  . LEU L 3 180 ? 101.371 9.713   -23.271 1.000 89.680  ? 185 LEU LLL CB  1 
ATOM 18018 C CG  . LEU L 3 180 ? 102.100 10.154  -24.546 1.000 78.020  ? 185 LEU LLL CG  1 
ATOM 18019 C CD1 . LEU L 3 180 ? 103.328 10.980  -24.212 1.000 72.890  ? 185 LEU LLL CD1 1 
ATOM 18020 C CD2 . LEU L 3 180 ? 102.450 8.967   -25.437 1.000 73.670  ? 185 LEU LLL CD2 1 
ATOM 18021 N N   . TYR L 3 181 ? 101.790 9.782   -19.959 1.000 106.750 ? 186 TYR LLL N   1 
ATOM 18022 C CA  . TYR L 3 181 ? 101.188 9.937   -18.603 1.000 115.180 ? 186 TYR LLL CA  1 
ATOM 18023 C C   . TYR L 3 181 ? 99.952  10.841  -18.687 1.000 117.360 ? 186 TYR LLL C   1 
ATOM 18024 O O   . TYR L 3 181 ? 99.862  11.657  -19.612 1.000 119.430 ? 186 TYR LLL O   1 
ATOM 18025 C CB  . TYR L 3 181 ? 102.199 10.501  -17.582 1.000 110.650 ? 186 TYR LLL CB  1 
ATOM 18026 C CG  . TYR L 3 181 ? 103.382 9.616   -17.283 1.000 104.030 ? 186 TYR LLL CG  1 
ATOM 18027 C CD1 . TYR L 3 181 ? 103.336 8.632   -16.301 1.000 102.740 ? 186 TYR LLL CD1 1 
ATOM 18028 C CD2 . TYR L 3 181 ? 104.551 9.726   -18.029 1.000 97.170  ? 186 TYR LLL CD2 1 
ATOM 18029 C CE1 . TYR L 3 181 ? 104.415 7.794   -16.072 1.000 93.140  ? 186 TYR LLL CE1 1 
ATOM 18030 C CE2 . TYR L 3 181 ? 105.640 8.900   -17.802 1.000 96.060  ? 186 TYR LLL CE2 1 
ATOM 18031 C CZ  . TYR L 3 181 ? 105.562 7.923   -16.830 1.000 85.710  ? 186 TYR LLL CZ  1 
ATOM 18032 O OH  . TYR L 3 181 ? 106.633 7.106   -16.643 1.000 76.490  ? 186 TYR LLL OH  1 
ATOM 18033 N N   . SER L 3 182 ? 99.022  10.681  -17.746 1.000 118.760 ? 187 SER LLL N   1 
ATOM 18034 C CA  . SER L 3 182 ? 97.854  11.578  -17.549 1.000 116.540 ? 187 SER LLL CA  1 
ATOM 18035 C C   . SER L 3 182 ? 97.566  11.682  -16.053 1.000 110.950 ? 187 SER LLL C   1 
ATOM 18036 O O   . SER L 3 182 ? 97.543  10.627  -15.409 1.000 114.230 ? 187 SER LLL O   1 
ATOM 18037 C CB  . SER L 3 182 ? 96.624  11.154  -18.317 1.000 118.230 ? 187 SER LLL CB  1 
ATOM 18038 O OG  . SER L 3 182 ? 96.878  11.087  -19.710 1.000 111.880 ? 187 SER LLL OG  1 
ATOM 18039 N N   . LEU L 3 183 ? 97.388  12.908  -15.550 1.000 102.350 ? 188 LEU LLL N   1 
ATOM 18040 C CA  . LEU L 3 183 ? 97.256  13.258  -14.108 1.000 112.270 ? 188 LEU LLL CA  1 
ATOM 18041 C C   . LEU L 3 183 ? 96.178  14.343  -13.953 1.000 104.580 ? 188 LEU LLL C   1 
ATOM 18042 O O   . LEU L 3 183 ? 96.011  15.143  -14.883 1.000 99.780  ? 188 LEU LLL O   1 
ATOM 18043 C CB  . LEU L 3 183 ? 98.641  13.720  -13.633 1.000 125.050 ? 188 LEU LLL CB  1 
ATOM 18044 C CG  . LEU L 3 183 ? 98.745  14.407  -12.265 1.000 135.250 ? 188 LEU LLL CG  1 
ATOM 18045 C CD1 . LEU L 3 183 ? 100.139 14.210  -11.664 1.000 132.930 ? 188 LEU LLL CD1 1 
ATOM 18046 C CD2 . LEU L 3 183 ? 98.412  15.896  -12.359 1.000 126.040 ? 188 LEU LLL CD2 1 
ATOM 18047 N N   . SER L 3 184 ? 95.463  14.348  -12.822 1.000 104.890 ? 189 SER LLL N   1 
ATOM 18048 C CA  . SER L 3 184 ? 94.341  15.272  -12.488 1.000 100.160 ? 189 SER LLL CA  1 
ATOM 18049 C C   . SER L 3 184 ? 94.589  15.915  -11.118 1.000 99.340  ? 189 SER LLL C   1 
ATOM 18050 O O   . SER L 3 184 ? 95.439  15.385  -10.380 1.000 113.980 ? 189 SER LLL O   1 
ATOM 18051 C CB  . SER L 3 184 ? 93.029  14.527  -12.505 1.000 95.120  ? 189 SER LLL CB  1 
ATOM 18052 O OG  . SER L 3 184 ? 92.916  13.725  -13.671 1.000 90.290  ? 189 SER LLL OG  1 
ATOM 18053 N N   . SER L 3 185 ? 93.857  16.986  -10.776 1.000 93.890  ? 190 SER LLL N   1 
ATOM 18054 C CA  . SER L 3 185 ? 93.917  17.693  -9.464  1.000 104.980 ? 190 SER LLL CA  1 
ATOM 18055 C C   . SER L 3 185 ? 92.587  18.408  -9.187  1.000 109.400 ? 190 SER LLL C   1 
ATOM 18056 O O   . SER L 3 185 ? 92.113  19.080  -10.130 1.000 119.620 ? 190 SER LLL O   1 
ATOM 18057 C CB  . SER L 3 185 ? 95.071  18.684  -9.447  1.000 106.840 ? 190 SER LLL CB  1 
ATOM 18058 O OG  . SER L 3 185 ? 95.172  19.339  -8.193  1.000 99.240  ? 190 SER LLL OG  1 
ATOM 18059 N N   . VAL L 3 186 ? 92.045  18.303  -7.960  1.000 103.870 ? 191 VAL LLL N   1 
ATOM 18060 C CA  . VAL L 3 186 ? 90.849  19.072  -7.483  1.000 99.910  ? 191 VAL LLL CA  1 
ATOM 18061 C C   . VAL L 3 186 ? 91.064  19.536  -6.037  1.000 101.720 ? 191 VAL LLL C   1 
ATOM 18062 O O   . VAL L 3 186 ? 91.394  18.674  -5.214  1.000 116.640 ? 191 VAL LLL O   1 
ATOM 18063 C CB  . VAL L 3 186 ? 89.548  18.245  -7.579  1.000 91.970  ? 191 VAL LLL CB  1 
ATOM 18064 C CG1 . VAL L 3 186 ? 88.974  18.267  -8.986  1.000 92.060  ? 191 VAL LLL CG1 1 
ATOM 18065 C CG2 . VAL L 3 186 ? 89.717  16.810  -7.086  1.000 79.540  ? 191 VAL LLL CG2 1 
ATOM 18066 N N   . VAL L 3 187 ? 90.792  20.819  -5.733  1.000 98.840  ? 192 VAL LLL N   1 
ATOM 18067 C CA  . VAL L 3 187 ? 90.799  21.382  -4.342  1.000 103.320 ? 192 VAL LLL CA  1 
ATOM 18068 C C   . VAL L 3 187 ? 89.393  21.907  -4.028  1.000 98.560  ? 192 VAL LLL C   1 
ATOM 18069 O O   . VAL L 3 187 ? 88.534  21.056  -3.747  1.000 87.380  ? 192 VAL LLL O   1 
ATOM 18070 C CB  . VAL L 3 187 ? 91.856  22.485  -4.118  1.000 100.380 ? 192 VAL LLL CB  1 
ATOM 18071 C CG1 . VAL L 3 187 ? 93.265  21.932  -3.924  1.000 93.550  ? 192 VAL LLL CG1 1 
ATOM 18072 C CG2 . VAL L 3 187 ? 91.828  23.539  -5.215  1.000 94.260  ? 192 VAL LLL CG2 1 
ATOM 18073 N N   . ASN L 3 202 ? 97.585  26.307  -12.080 1.000 108.570 ? 207 ASN LLL N   1 
ATOM 18074 C CA  . ASN L 3 202 ? 99.038  26.524  -12.329 1.000 109.280 ? 207 ASN LLL CA  1 
ATOM 18075 C C   . ASN L 3 202 ? 99.729  25.172  -12.575 1.000 108.230 ? 207 ASN LLL C   1 
ATOM 18076 O O   . ASN L 3 202 ? 100.114 24.521  -11.578 1.000 94.470  ? 207 ASN LLL O   1 
ATOM 18077 C CB  . ASN L 3 202 ? 99.693  27.279  -11.167 1.000 104.090 ? 207 ASN LLL CB  1 
ATOM 18078 C CG  . ASN L 3 202 ? 99.018  28.598  -10.858 1.000 97.510  ? 207 ASN LLL CG  1 
ATOM 18079 O OD1 . ASN L 3 202 ? 98.977  29.475  -11.712 1.000 106.890 ? 207 ASN LLL OD1 1 
ATOM 18080 N ND2 . ASN L 3 202 ? 98.490  28.749  -9.653  1.000 95.680  ? 207 ASN LLL ND2 1 
ATOM 18081 N N   . VAL L 3 203 ? 99.840  24.752  -13.841 1.000 104.970 ? 208 VAL LLL N   1 
ATOM 18082 C CA  . VAL L 3 203 ? 100.471 23.456  -14.229 1.000 103.870 ? 208 VAL LLL CA  1 
ATOM 18083 C C   . VAL L 3 203 ? 101.878 23.750  -14.758 1.000 105.360 ? 208 VAL LLL C   1 
ATOM 18084 O O   . VAL L 3 203 ? 102.037 24.738  -15.507 1.000 111.480 ? 208 VAL LLL O   1 
ATOM 18085 C CB  . VAL L 3 203 ? 99.623  22.633  -15.224 1.000 110.990 ? 208 VAL LLL CB  1 
ATOM 18086 C CG1 . VAL L 3 203 ? 99.486  23.282  -16.597 1.000 112.220 ? 208 VAL LLL CG1 1 
ATOM 18087 C CG2 . VAL L 3 203 ? 100.157 21.218  -15.375 1.000 115.000 ? 208 VAL LLL CG2 1 
ATOM 18088 N N   . ASN L 3 204 ? 102.858 22.928  -14.369 1.000 103.530 ? 209 ASN LLL N   1 
ATOM 18089 C CA  . ASN L 3 204 ? 104.282 23.057  -14.776 1.000 101.870 ? 209 ASN LLL CA  1 
ATOM 18090 C C   . ASN L 3 204 ? 104.834 21.660  -15.101 1.000 99.640  ? 209 ASN LLL C   1 
ATOM 18091 O O   . ASN L 3 204 ? 104.553 20.729  -14.347 1.000 98.030  ? 209 ASN LLL O   1 
ATOM 18092 C CB  . ASN L 3 204 ? 105.110 23.797  -13.709 1.000 96.490  ? 209 ASN LLL CB  1 
ATOM 18093 C CG  . ASN L 3 204 ? 106.321 24.516  -14.271 1.000 88.640  ? 209 ASN LLL CG  1 
ATOM 18094 O OD1 . ASN L 3 204 ? 107.037 23.968  -15.119 1.000 78.480  ? 209 ASN LLL OD1 1 
ATOM 18095 N ND2 . ASN L 3 204 ? 106.545 25.744  -13.813 1.000 71.720  ? 209 ASN LLL ND2 1 
ATOM 18096 N N   . HIS L 3 205 ? 105.600 21.521  -16.188 1.000 91.410  ? 210 HIS LLL N   1 
ATOM 18097 C CA  . HIS L 3 205 ? 106.269 20.260  -16.618 1.000 89.650  ? 210 HIS LLL CA  1 
ATOM 18098 C C   . HIS L 3 205 ? 107.655 20.619  -17.177 1.000 95.690  ? 210 HIS LLL C   1 
ATOM 18099 O O   . HIS L 3 205 ? 107.776 20.779  -18.413 1.000 92.220  ? 210 HIS LLL O   1 
ATOM 18100 C CB  . HIS L 3 205 ? 105.377 19.540  -17.621 1.000 95.600  ? 210 HIS LLL CB  1 
ATOM 18101 C CG  . HIS L 3 205 ? 105.888 18.244  -18.156 1.000 96.900  ? 210 HIS LLL CG  1 
ATOM 18102 N ND1 . HIS L 3 205 ? 106.420 18.137  -19.422 1.000 94.830  ? 210 HIS LLL ND1 1 
ATOM 18103 C CD2 . HIS L 3 205 ? 105.866 16.993  -17.653 1.000 101.290 ? 210 HIS LLL CD2 1 
ATOM 18104 C CE1 . HIS L 3 205 ? 106.736 16.880  -19.666 1.000 92.290  ? 210 HIS LLL CE1 1 
ATOM 18105 N NE2 . HIS L 3 205 ? 106.401 16.159  -18.603 1.000 92.380  ? 210 HIS LLL NE2 1 
ATOM 18106 N N   . LYS L 3 206 ? 108.650 20.746  -16.287 1.000 100.650 ? 211 LYS LLL N   1 
ATOM 18107 C CA  . LYS L 3 206 ? 110.016 21.278  -16.572 1.000 91.350  ? 211 LYS LLL CA  1 
ATOM 18108 C C   . LYS L 3 206 ? 110.610 20.611  -17.819 1.000 90.930  ? 211 LYS LLL C   1 
ATOM 18109 O O   . LYS L 3 206 ? 111.144 21.314  -18.673 1.000 94.230  ? 211 LYS LLL O   1 
ATOM 18110 C CB  . LYS L 3 206 ? 110.958 21.111  -15.370 1.000 73.980  ? 211 LYS LLL CB  1 
ATOM 18111 N N   . PRO L 3 207 ? 110.532 19.268  -17.988 1.000 93.160  ? 212 PRO LLL N   1 
ATOM 18112 C CA  . PRO L 3 207 ? 111.140 18.601  -19.144 1.000 96.270  ? 212 PRO LLL CA  1 
ATOM 18113 C C   . PRO L 3 207 ? 110.687 19.094  -20.532 1.000 102.910 ? 212 PRO LLL C   1 
ATOM 18114 O O   . PRO L 3 207 ? 111.388 18.787  -21.492 1.000 84.760  ? 212 PRO LLL O   1 
ATOM 18115 C CB  . PRO L 3 207 ? 110.730 17.123  -18.974 1.000 96.950  ? 212 PRO LLL CB  1 
ATOM 18116 C CG  . PRO L 3 207 ? 110.478 16.969  -17.489 1.000 94.780  ? 212 PRO LLL CG  1 
ATOM 18117 C CD  . PRO L 3 207 ? 109.888 18.305  -17.071 1.000 101.180 ? 212 PRO LLL CD  1 
ATOM 18118 N N   . SER L 3 208 ? 109.552 19.811  -20.611 1.000 120.100 ? 213 SER LLL N   1 
ATOM 18119 C CA  . SER L 3 208 ? 108.941 20.327  -21.871 1.000 116.010 ? 213 SER LLL CA  1 
ATOM 18120 C C   . SER L 3 208 ? 108.717 21.852  -21.819 1.000 108.900 ? 213 SER LLL C   1 
ATOM 18121 O O   . SER L 3 208 ? 108.039 22.361  -22.726 1.000 93.470  ? 213 SER LLL O   1 
ATOM 18122 C CB  . SER L 3 208 ? 107.653 19.589  -22.185 1.000 111.210 ? 213 SER LLL CB  1 
ATOM 18123 O OG  . SER L 3 208 ? 106.522 20.228  -21.603 1.000 101.750 ? 213 SER LLL OG  1 
ATOM 18124 N N   . ASN L 3 209 ? 109.242 22.554  -20.805 1.000 109.960 ? 214 ASN LLL N   1 
ATOM 18125 C CA  . ASN L 3 209 ? 109.201 24.041  -20.692 1.000 98.920  ? 214 ASN LLL CA  1 
ATOM 18126 C C   . ASN L 3 209 ? 107.753 24.549  -20.692 1.000 97.260  ? 214 ASN LLL C   1 
ATOM 18127 O O   . ASN L 3 209 ? 107.547 25.730  -21.042 1.000 97.380  ? 214 ASN LLL O   1 
ATOM 18128 C CB  . ASN L 3 209 ? 109.995 24.702  -21.822 1.000 94.540  ? 214 ASN LLL CB  1 
ATOM 18129 C CG  . ASN L 3 209 ? 111.461 24.350  -21.766 1.000 90.250  ? 214 ASN LLL CG  1 
ATOM 18130 O OD1 . ASN L 3 209 ? 112.183 24.911  -20.945 1.000 88.700  ? 214 ASN LLL OD1 1 
ATOM 18131 N ND2 . ASN L 3 209 ? 111.902 23.446  -22.631 1.000 78.920  ? 214 ASN LLL ND2 1 
ATOM 18132 N N   . THR L 3 210 ? 106.803 23.705  -20.277 1.000 99.490  ? 215 THR LLL N   1 
ATOM 18133 C CA  . THR L 3 210 ? 105.343 23.998  -20.270 1.000 94.620  ? 215 THR LLL CA  1 
ATOM 18134 C C   . THR L 3 210 ? 104.979 24.599  -18.907 1.000 95.740  ? 215 THR LLL C   1 
ATOM 18135 O O   . THR L 3 210 ? 105.224 23.922  -17.889 1.000 93.750  ? 215 THR LLL O   1 
ATOM 18136 C CB  . THR L 3 210 ? 104.512 22.739  -20.563 1.000 84.860  ? 215 THR LLL CB  1 
ATOM 18137 O OG1 . THR L 3 210 ? 104.922 22.141  -21.794 1.000 70.800  ? 215 THR LLL OG1 1 
ATOM 18138 C CG2 . THR L 3 210 ? 103.028 23.032  -20.608 1.000 81.580  ? 215 THR LLL CG2 1 
ATOM 18139 N N   . LYS L 3 211 ? 104.433 25.821  -18.891 1.000 98.730  ? 216 LYS LLL N   1 
ATOM 18140 C CA  . LYS L 3 211 ? 104.158 26.595  -17.650 1.000 114.750 ? 216 LYS LLL CA  1 
ATOM 18141 C C   . LYS L 3 211 ? 102.836 27.357  -17.802 1.000 125.350 ? 216 LYS LLL C   1 
ATOM 18142 O O   . LYS L 3 211 ? 102.761 28.503  -17.327 1.000 133.330 ? 216 LYS LLL O   1 
ATOM 18143 C CB  . LYS L 3 211 ? 105.325 27.550  -17.355 1.000 112.280 ? 216 LYS LLL CB  1 
ATOM 18144 C CG  . LYS L 3 211 ? 105.323 28.140  -15.948 1.000 109.590 ? 216 LYS LLL CG  1 
ATOM 18145 C CD  . LYS L 3 211 ? 106.579 28.927  -15.622 1.000 106.990 ? 216 LYS LLL CD  1 
ATOM 18146 C CE  . LYS L 3 211 ? 106.760 29.191  -14.141 1.000 97.650  ? 216 LYS LLL CE  1 
ATOM 18147 N NZ  . LYS L 3 211 ? 107.587 30.395  -13.909 1.000 93.050  ? 216 LYS LLL NZ  1 
ATOM 18148 N N   . VAL L 3 212 ? 101.805 26.725  -18.383 1.000 129.400 ? 217 VAL LLL N   1 
ATOM 18149 C CA  . VAL L 3 212 ? 100.515 27.383  -18.769 1.000 124.700 ? 217 VAL LLL CA  1 
ATOM 18150 C C   . VAL L 3 212 ? 99.547  27.365  -17.573 1.000 109.680 ? 217 VAL LLL C   1 
ATOM 18151 O O   . VAL L 3 212 ? 99.363  26.272  -16.972 1.000 98.610  ? 217 VAL LLL O   1 
ATOM 18152 C CB  . VAL L 3 212 ? 99.902  26.740  -20.034 1.000 130.750 ? 217 VAL LLL CB  1 
ATOM 18153 C CG1 . VAL L 3 212 ? 100.805 26.942  -21.248 1.000 121.940 ? 217 VAL LLL CG1 1 
ATOM 18154 C CG2 . VAL L 3 212 ? 99.564  25.260  -19.854 1.000 128.770 ? 217 VAL LLL CG2 1 
ATOM 18155 N N   . ASP L 3 213 ? 98.972  28.533  -17.226 1.000 96.970  ? 218 ASP LLL N   1 
ATOM 18156 C CA  . ASP L 3 213 ? 97.968  28.716  -16.125 1.000 84.060  ? 218 ASP LLL CA  1 
ATOM 18157 C C   . ASP L 3 213 ? 96.636  29.074  -16.785 1.000 71.040  ? 218 ASP LLL C   1 
ATOM 18158 O O   . ASP L 3 213 ? 95.642  29.082  -16.103 1.000 56.600  ? 218 ASP LLL O   1 
ATOM 18159 C CB  . ASP L 3 213 ? 98.391  29.708  -15.019 1.000 76.530  ? 218 ASP LLL CB  1 
ATOM 18160 C CG  . ASP L 3 213 ? 99.266  30.894  -15.425 1.000 77.410  ? 218 ASP LLL CG  1 
ATOM 18161 O OD1 . ASP L 3 213 ? 98.969  31.523  -16.467 1.000 77.570  ? 218 ASP LLL OD1 1 
ATOM 18162 O OD2 . ASP L 3 213 ? 100.228 31.207  -14.672 1.000 67.050  ? 218 ASP LLL OD2 1 
ATOM 18163 N N   . SER M 2 2   ? 107.675 -17.838 69.405  1.000 61.260  ? 2   SER MMM N   1 
ATOM 18164 C CA  . SER M 2 2   ? 108.267 -18.845 68.464  1.000 64.740  ? 2   SER MMM CA  1 
ATOM 18165 C C   . SER M 2 2   ? 107.155 -19.650 67.703  1.000 62.120  ? 2   SER MMM C   1 
ATOM 18166 O O   . SER M 2 2   ? 107.303 -20.884 67.409  1.000 46.870  ? 2   SER MMM O   1 
ATOM 18167 C CB  . SER M 2 2   ? 109.380 -19.671 69.166  1.000 65.300  ? 2   SER MMM CB  1 
ATOM 18168 O OG  . SER M 2 2   ? 108.980 -20.295 70.383  1.000 61.160  ? 2   SER MMM OG  1 
ATOM 18169 N N   . VAL M 2 3   ? 106.118 -18.932 67.245  1.000 60.950  ? 3   VAL MMM N   1 
ATOM 18170 C CA  . VAL M 2 3   ? 105.086 -19.411 66.268  1.000 62.220  ? 3   VAL MMM CA  1 
ATOM 18171 C C   . VAL M 2 3   ? 105.116 -18.495 65.045  1.000 60.680  ? 3   VAL MMM C   1 
ATOM 18172 O O   . VAL M 2 3   ? 105.317 -17.301 65.231  1.000 58.020  ? 3   VAL MMM O   1 
ATOM 18173 C CB  . VAL M 2 3   ? 103.658 -19.419 66.848  1.000 63.160  ? 3   VAL MMM CB  1 
ATOM 18174 C CG1 . VAL M 2 3   ? 102.715 -20.248 65.955  1.000 61.020  ? 3   VAL MMM CG1 1 
ATOM 18175 C CG2 . VAL M 2 3   ? 103.606 -19.855 68.314  1.000 64.200  ? 3   VAL MMM CG2 1 
ATOM 18176 N N   . LEU M 2 4   ? 104.862 -19.023 63.850  1.000 63.040  ? 4   LEU MMM N   1 
ATOM 18177 C CA  . LEU M 2 4   ? 104.693 -18.155 62.657  1.000 55.620  ? 4   LEU MMM CA  1 
ATOM 18178 C C   . LEU M 2 4   ? 103.212 -17.807 62.530  1.000 55.380  ? 4   LEU MMM C   1 
ATOM 18179 O O   . LEU M 2 4   ? 102.360 -18.731 62.583  1.000 57.410  ? 4   LEU MMM O   1 
ATOM 18180 C CB  . LEU M 2 4   ? 105.221 -18.862 61.409  1.000 53.060  ? 4   LEU MMM CB  1 
ATOM 18181 C CG  . LEU M 2 4   ? 106.690 -19.266 61.467  1.000 49.850  ? 4   LEU MMM CG  1 
ATOM 18182 C CD1 . LEU M 2 4   ? 107.159 -19.794 60.136  1.000 48.320  ? 4   LEU MMM CD1 1 
ATOM 18183 C CD2 . LEU M 2 4   ? 107.562 -18.114 61.903  1.000 47.470  ? 4   LEU MMM CD2 1 
ATOM 18184 N N   . THR M 2 5   ? 102.925 -16.512 62.421  1.000 52.600  ? 5   THR MMM N   1 
ATOM 18185 C CA  . THR M 2 5   ? 101.551 -15.957 62.364  1.000 58.390  ? 5   THR MMM CA  1 
ATOM 18186 C C   . THR M 2 5   ? 101.290 -15.510 60.922  1.000 64.990  ? 5   THR MMM C   1 
ATOM 18187 O O   . THR M 2 5   ? 102.012 -14.583 60.460  1.000 58.830  ? 5   THR MMM O   1 
ATOM 18188 C CB  . THR M 2 5   ? 101.388 -14.866 63.431  1.000 57.710  ? 5   THR MMM CB  1 
ATOM 18189 O OG1 . THR M 2 5   ? 102.593 -14.108 63.444  1.000 59.090  ? 5   THR MMM OG1 1 
ATOM 18190 C CG2 . THR M 2 5   ? 101.186 -15.421 64.827  1.000 56.690  ? 5   THR MMM CG2 1 
ATOM 18191 N N   . GLN M 2 6   ? 100.351 -16.171 60.225  1.000 71.190  ? 6   GLN MMM N   1 
ATOM 18192 C CA  . GLN M 2 6   ? 99.867  -15.726 58.886  1.000 65.430  ? 6   GLN MMM CA  1 
ATOM 18193 C C   . GLN M 2 6   ? 98.336  -15.638 58.877  1.000 64.990  ? 6   GLN MMM C   1 
ATOM 18194 O O   . GLN M 2 6   ? 97.653  -16.363 59.596  1.000 58.660  ? 6   GLN MMM O   1 
ATOM 18195 C CB  . GLN M 2 6   ? 100.441 -16.624 57.787  1.000 61.080  ? 6   GLN MMM CB  1 
ATOM 18196 C CG  . GLN M 2 6   ? 99.817  -18.004 57.696  1.000 60.750  ? 6   GLN MMM CG  1 
ATOM 18197 C CD  . GLN M 2 6   ? 100.630 -18.936 56.828  1.000 62.590  ? 6   GLN MMM CD  1 
ATOM 18198 O OE1 . GLN M 2 6   ? 101.748 -19.318 57.197  1.000 57.230  ? 6   GLN MMM OE1 1 
ATOM 18199 N NE2 . GLN M 2 6   ? 100.076 -19.313 55.676  1.000 54.000  ? 6   GLN MMM NE2 1 
ATOM 18200 N N   . PRO M 2 7   ? 97.741  -14.716 58.084  1.000 66.170  ? 7   PRO MMM N   1 
ATOM 18201 C CA  . PRO M 2 7   ? 96.286  -14.581 58.012  1.000 66.020  ? 7   PRO MMM CA  1 
ATOM 18202 C C   . PRO M 2 7   ? 95.612  -15.910 57.685  1.000 67.850  ? 7   PRO MMM C   1 
ATOM 18203 O O   . PRO M 2 7   ? 96.051  -16.590 56.761  1.000 64.010  ? 7   PRO MMM O   1 
ATOM 18204 C CB  . PRO M 2 7   ? 96.083  -13.569 56.872  1.000 71.230  ? 7   PRO MMM CB  1 
ATOM 18205 C CG  . PRO M 2 7   ? 97.353  -12.730 56.897  1.000 72.380  ? 7   PRO MMM CG  1 
ATOM 18206 C CD  . PRO M 2 7   ? 98.441  -13.728 57.244  1.000 70.890  ? 7   PRO MMM CD  1 
ATOM 18207 N N   . PRO M 2 8   ? 94.571  -16.339 58.436  1.000 79.410  ? 8   PRO MMM N   1 
ATOM 18208 C CA  . PRO M 2 8   ? 93.860  -17.588 58.141  1.000 77.020  ? 8   PRO MMM CA  1 
ATOM 18209 C C   . PRO M 2 8   ? 93.242  -17.609 56.737  1.000 75.050  ? 8   PRO MMM C   1 
ATOM 18210 O O   . PRO M 2 8   ? 93.200  -18.654 56.136  1.000 59.560  ? 8   PRO MMM O   1 
ATOM 18211 C CB  . PRO M 2 8   ? 92.757  -17.680 59.211  1.000 79.740  ? 8   PRO MMM CB  1 
ATOM 18212 C CG  . PRO M 2 8   ? 92.661  -16.275 59.793  1.000 89.660  ? 8   PRO MMM CG  1 
ATOM 18213 C CD  . PRO M 2 8   ? 94.050  -15.685 59.649  1.000 89.320  ? 8   PRO MMM CD  1 
ATOM 18214 N N   . SER M 2 9   ? 92.795  -16.456 56.245  1.000 85.850  ? 9   SER MMM N   1 
ATOM 18215 C CA  . SER M 2 9   ? 92.259  -16.316 54.867  1.000 84.930  ? 9   SER MMM CA  1 
ATOM 18216 C C   . SER M 2 9   ? 92.728  -14.997 54.241  1.000 78.670  ? 9   SER MMM C   1 
ATOM 18217 O O   . SER M 2 9   ? 93.077  -14.036 54.984  1.000 57.240  ? 9   SER MMM O   1 
ATOM 18218 C CB  . SER M 2 9   ? 90.758  -16.437 54.849  1.000 91.020  ? 9   SER MMM CB  1 
ATOM 18219 O OG  . SER M 2 9   ? 90.159  -15.360 55.546  1.000 98.050  ? 9   SER MMM OG  1 
ATOM 18220 N N   . ALA M 2 10  ? 92.740  -14.991 52.908  1.000 81.600  ? 10  ALA MMM N   1 
ATOM 18221 C CA  . ALA M 2 10  ? 93.002  -13.827 52.037  1.000 84.670  ? 10  ALA MMM CA  1 
ATOM 18222 C C   . ALA M 2 10  ? 92.249  -14.055 50.736  1.000 86.590  ? 10  ALA MMM C   1 
ATOM 18223 O O   . ALA M 2 10  ? 91.933  -15.233 50.437  1.000 74.120  ? 10  ALA MMM O   1 
ATOM 18224 C CB  . ALA M 2 10  ? 94.476  -13.680 51.777  1.000 85.080  ? 10  ALA MMM CB  1 
ATOM 18225 N N   . SER M 2 11  ? 91.964  -12.975 50.008  1.000 93.230  ? 11  SER MMM N   1 
ATOM 18226 C CA  . SER M 2 11  ? 91.206  -13.017 48.732  1.000 92.310  ? 11  SER MMM CA  1 
ATOM 18227 C C   . SER M 2 11  ? 91.593  -11.836 47.836  1.000 85.580  ? 11  SER MMM C   1 
ATOM 18228 O O   . SER M 2 11  ? 92.272  -10.906 48.329  1.000 76.650  ? 11  SER MMM O   1 
ATOM 18229 C CB  . SER M 2 11  ? 89.742  -13.028 49.010  1.000 92.890  ? 11  SER MMM CB  1 
ATOM 18230 O OG  . SER M 2 11  ? 89.368  -11.816 49.656  1.000 93.690  ? 11  SER MMM OG  1 
ATOM 18231 N N   . GLY M 2 12  ? 91.184  -11.900 46.565  1.000 83.490  ? 12  GLY MMM N   1 
ATOM 18232 C CA  . GLY M 2 12  ? 91.425  -10.849 45.556  1.000 84.990  ? 12  GLY MMM CA  1 
ATOM 18233 C C   . GLY M 2 12  ? 90.581  -11.043 44.306  1.000 93.430  ? 12  GLY MMM C   1 
ATOM 18234 O O   . GLY M 2 12  ? 90.026  -12.185 44.123  1.000 87.550  ? 12  GLY MMM O   1 
ATOM 18235 N N   . THR M 2 13  ? 90.488  -9.975  43.495  1.000 89.820  ? 13  THR MMM N   1 
ATOM 18236 C CA  . THR M 2 13  ? 89.866  -9.936  42.141  1.000 93.640  ? 13  THR MMM CA  1 
ATOM 18237 C C   . THR M 2 13  ? 90.874  -10.389 41.091  1.000 91.980  ? 13  THR MMM C   1 
ATOM 18238 O O   . THR M 2 13  ? 92.018  -9.940  41.139  1.000 83.740  ? 13  THR MMM O   1 
ATOM 18239 C CB  . THR M 2 13  ? 89.529  -8.489  41.756  1.000 90.860  ? 13  THR MMM CB  1 
ATOM 18240 O OG1 . THR M 2 13  ? 88.954  -7.851  42.895  1.000 89.890  ? 13  THR MMM OG1 1 
ATOM 18241 C CG2 . THR M 2 13  ? 88.663  -8.344  40.521  1.000 86.950  ? 13  THR MMM CG2 1 
ATOM 18242 N N   . PRO M 2 14  ? 90.527  -11.270 40.121  1.000 86.650  ? 14  PRO MMM N   1 
ATOM 18243 C CA  . PRO M 2 14  ? 91.491  -11.720 39.110  1.000 88.700  ? 14  PRO MMM CA  1 
ATOM 18244 C C   . PRO M 2 14  ? 92.260  -10.521 38.533  1.000 89.270  ? 14  PRO MMM C   1 
ATOM 18245 O O   . PRO M 2 14  ? 91.639  -9.512  38.285  1.000 101.400 ? 14  PRO MMM O   1 
ATOM 18246 C CB  . PRO M 2 14  ? 90.608  -12.418 38.066  1.000 81.220  ? 14  PRO MMM CB  1 
ATOM 18247 C CG  . PRO M 2 14  ? 89.410  -12.908 38.873  1.000 82.490  ? 14  PRO MMM CG  1 
ATOM 18248 C CD  . PRO M 2 14  ? 89.193  -11.867 39.966  1.000 81.200  ? 14  PRO MMM CD  1 
ATOM 18249 N N   . GLY M 2 15  ? 93.579  -10.637 38.386  1.000 85.000  ? 15  GLY MMM N   1 
ATOM 18250 C CA  . GLY M 2 15  ? 94.459  -9.575  37.860  1.000 80.670  ? 15  GLY MMM CA  1 
ATOM 18251 C C   . GLY M 2 15  ? 95.100  -8.752  38.963  1.000 83.790  ? 15  GLY MMM C   1 
ATOM 18252 O O   . GLY M 2 15  ? 96.114  -8.098  38.676  1.000 83.360  ? 15  GLY MMM O   1 
ATOM 18253 N N   . GLN M 2 16  ? 94.540  -8.786  40.183  1.000 92.000  ? 16  GLN MMM N   1 
ATOM 18254 C CA  . GLN M 2 16  ? 95.068  -8.022  41.355  1.000 93.040  ? 16  GLN MMM CA  1 
ATOM 18255 C C   . GLN M 2 16  ? 96.381  -8.634  41.851  1.000 82.150  ? 16  GLN MMM C   1 
ATOM 18256 O O   . GLN M 2 16  ? 96.685  -9.789  41.451  1.000 77.170  ? 16  GLN MMM O   1 
ATOM 18257 C CB  . GLN M 2 16  ? 94.081  -8.004  42.528  1.000 96.820  ? 16  GLN MMM CB  1 
ATOM 18258 C CG  . GLN M 2 16  ? 93.198  -6.764  42.589  1.000 100.850 ? 16  GLN MMM CG  1 
ATOM 18259 C CD  . GLN M 2 16  ? 92.346  -6.745  43.836  1.000 99.790  ? 16  GLN MMM CD  1 
ATOM 18260 O OE1 . GLN M 2 16  ? 91.871  -7.787  44.310  1.000 93.570  ? 16  GLN MMM OE1 1 
ATOM 18261 N NE2 . GLN M 2 16  ? 92.149  -5.545  44.376  1.000 85.950  ? 16  GLN MMM NE2 1 
ATOM 18262 N N   . ARG M 2 17  ? 97.092  -7.872  42.699  1.000 76.260  ? 17  ARG MMM N   1 
ATOM 18263 C CA  . ARG M 2 17  ? 98.187  -8.335  43.595  1.000 71.340  ? 17  ARG MMM CA  1 
ATOM 18264 C C   . ARG M 2 17  ? 97.593  -8.586  44.984  1.000 69.710  ? 17  ARG MMM C   1 
ATOM 18265 O O   . ARG M 2 17  ? 97.015  -7.666  45.544  1.000 70.950  ? 17  ARG MMM O   1 
ATOM 18266 C CB  . ARG M 2 17  ? 99.357  -7.338  43.683  1.000 55.450  ? 17  ARG MMM CB  1 
ATOM 18267 N N   . VAL M 2 18  ? 97.713  -9.811  45.498  1.000 76.470  ? 18  VAL MMM N   1 
ATOM 18268 C CA  . VAL M 2 18  ? 97.364  -10.196 46.898  1.000 68.380  ? 18  VAL MMM CA  1 
ATOM 18269 C C   . VAL M 2 18  ? 98.669  -10.371 47.668  1.000 62.380  ? 18  VAL MMM C   1 
ATOM 18270 O O   . VAL M 2 18  ? 99.670  -10.796 47.042  1.000 64.450  ? 18  VAL MMM O   1 
ATOM 18271 C CB  . VAL M 2 18  ? 96.546  -11.493 46.937  1.000 72.130  ? 18  VAL MMM CB  1 
ATOM 18272 C CG1 . VAL M 2 18  ? 95.977  -11.725 48.327  1.000 75.240  ? 18  VAL MMM CG1 1 
ATOM 18273 C CG2 . VAL M 2 18  ? 95.466  -11.507 45.858  1.000 77.170  ? 18  VAL MMM CG2 1 
ATOM 18274 N N   . THR M 2 19  ? 98.649  -10.057 48.963  1.000 57.230  ? 19  THR MMM N   1 
ATOM 18275 C CA  . THR M 2 19  ? 99.844  -10.112 49.839  1.000 61.270  ? 19  THR MMM CA  1 
ATOM 18276 C C   . THR M 2 19  ? 99.504  -10.958 51.072  1.000 59.840  ? 19  THR MMM C   1 
ATOM 18277 O O   . THR M 2 19  ? 98.574  -10.571 51.816  1.000 63.380  ? 19  THR MMM O   1 
ATOM 18278 C CB  . THR M 2 19  ? 100.355 -8.688  50.119  1.000 63.720  ? 19  THR MMM CB  1 
ATOM 18279 O OG1 . THR M 2 19  ? 101.677 -8.795  50.643  1.000 66.480  ? 19  THR MMM OG1 1 
ATOM 18280 C CG2 . THR M 2 19  ? 99.513  -7.892  51.096  1.000 64.570  ? 19  THR MMM CG2 1 
ATOM 18281 N N   . ILE M 2 20  ? 100.194 -12.091 51.261  1.000 58.820  ? 20  ILE MMM N   1 
ATOM 18282 C CA  . ILE M 2 20  ? 100.063 -12.926 52.495  1.000 58.830  ? 20  ILE MMM CA  1 
ATOM 18283 C C   . ILE M 2 20  ? 101.308 -12.704 53.361  1.000 55.920  ? 20  ILE MMM C   1 
ATOM 18284 O O   . ILE M 2 20  ? 102.428 -12.979 52.879  1.000 55.870  ? 20  ILE MMM O   1 
ATOM 18285 C CB  . ILE M 2 20  ? 99.876  -14.416 52.167  1.000 56.960  ? 20  ILE MMM CB  1 
ATOM 18286 C CG1 . ILE M 2 20  ? 98.853  -14.647 51.062  1.000 56.450  ? 20  ILE MMM CG1 1 
ATOM 18287 C CG2 . ILE M 2 20  ? 99.536  -15.172 53.444  1.000 58.590  ? 20  ILE MMM CG2 1 
ATOM 18288 C CD1 . ILE M 2 20  ? 98.790  -16.078 50.555  1.000 59.340  ? 20  ILE MMM CD1 1 
ATOM 18289 N N   . SER M 2 21  ? 101.121 -12.237 54.595  1.000 51.750  ? 21  SER MMM N   1 
ATOM 18290 C CA  . SER M 2 21  ? 102.234 -11.922 55.526  1.000 54.080  ? 21  SER MMM CA  1 
ATOM 18291 C C   . SER M 2 21  ? 102.506 -13.139 56.414  1.000 55.460  ? 21  SER MMM C   1 
ATOM 18292 O O   . SER M 2 21  ? 101.571 -13.938 56.636  1.000 52.340  ? 21  SER MMM O   1 
ATOM 18293 C CB  . SER M 2 21  ? 101.945 -10.695 56.344  1.000 50.340  ? 21  SER MMM CB  1 
ATOM 18294 O OG  . SER M 2 21  ? 100.743 -10.854 57.066  1.000 57.770  ? 21  SER MMM OG  1 
ATOM 18295 N N   . CYS M 2 22  ? 103.758 -13.279 56.854  1.000 57.040  ? 22  CYS MMM N   1 
ATOM 18296 C CA  . CYS M 2 22  ? 104.212 -14.300 57.832  1.000 54.290  ? 22  CYS MMM CA  1 
ATOM 18297 C C   . CYS M 2 22  ? 105.153 -13.637 58.837  1.000 56.560  ? 22  CYS MMM C   1 
ATOM 18298 O O   . CYS M 2 22  ? 106.208 -13.121 58.432  1.000 60.600  ? 22  CYS MMM O   1 
ATOM 18299 C CB  . CYS M 2 22  ? 104.898 -15.476 57.152  1.000 55.800  ? 22  CYS MMM CB  1 
ATOM 18300 S SG  . CYS M 2 22  ? 104.653 -16.957 58.147  1.000 53.700  ? 22  CYS MMM SG  1 
ATOM 18301 N N   . SER M 2 23  ? 104.738 -13.574 60.098  1.000 57.460  ? 23  SER MMM N   1 
ATOM 18302 C CA  . SER M 2 23  ? 105.457 -12.846 61.174  1.000 56.680  ? 23  SER MMM CA  1 
ATOM 18303 C C   . SER M 2 23  ? 105.978 -13.870 62.170  1.000 53.260  ? 23  SER MMM C   1 
ATOM 18304 O O   . SER M 2 23  ? 105.170 -14.746 62.576  1.000 61.550  ? 23  SER MMM O   1 
ATOM 18305 C CB  . SER M 2 23  ? 104.557 -11.854 61.849  1.000 62.500  ? 23  SER MMM CB  1 
ATOM 18306 O OG  . SER M 2 23  ? 104.448 -10.666 61.082  1.000 79.140  ? 23  SER MMM OG  1 
ATOM 18307 N N   . GLY M 2 24  ? 107.265 -13.780 62.515  1.000 45.130  ? 24  GLY MMM N   1 
ATOM 18308 C CA  . GLY M 2 24  ? 107.901 -14.686 63.484  1.000 43.900  ? 24  GLY MMM CA  1 
ATOM 18309 C C   . GLY M 2 24  ? 108.643 -13.923 64.555  1.000 40.270  ? 24  GLY MMM C   1 
ATOM 18310 O O   . GLY M 2 24  ? 108.256 -12.781 64.840  1.000 51.060  ? 24  GLY MMM O   1 
ATOM 18311 N N   . GLY M 2 25  ? 109.707 -14.520 65.091  1.000 36.700  ? 25  GLY MMM N   1 
ATOM 18312 C CA  . GLY M 2 25  ? 110.617 -13.892 66.072  1.000 41.120  ? 25  GLY MMM CA  1 
ATOM 18313 C C   . GLY M 2 25  ? 112.079 -14.137 65.737  1.000 41.730  ? 25  GLY MMM C   1 
ATOM 18314 O O   . GLY M 2 25  ? 112.361 -14.972 64.851  1.000 45.270  ? 25  GLY MMM O   1 
ATOM 18315 N N   . SER M 2 26  ? 112.986 -13.483 66.456  1.000 42.920  ? 26  SER MMM N   1 
ATOM 18316 C CA  . SER M 2 26  ? 114.453 -13.632 66.294  1.000 45.940  ? 26  SER MMM CA  1 
ATOM 18317 C C   . SER M 2 26  ? 114.861 -15.117 66.268  1.000 42.900  ? 26  SER MMM C   1 
ATOM 18318 O O   . SER M 2 26  ? 115.755 -15.454 65.498  1.000 36.020  ? 26  SER MMM O   1 
ATOM 18319 C CB  . SER M 2 26  ? 115.185 -12.868 67.366  1.000 52.550  ? 26  SER MMM CB  1 
ATOM 18320 O OG  . SER M 2 26  ? 114.996 -13.480 68.634  1.000 60.630  ? 26  SER MMM OG  1 
ATOM 18321 N N   . SER M 2 27  ? 114.211 -15.967 67.065  1.000 47.840  ? 27  SER MMM N   1 
ATOM 18322 C CA  . SER M 2 27  ? 114.518 -17.415 67.204  1.000 52.180  ? 27  SER MMM CA  1 
ATOM 18323 C C   . SER M 2 27  ? 114.243 -18.193 65.897  1.000 50.940  ? 27  SER MMM C   1 
ATOM 18324 O O   . SER M 2 27  ? 114.911 -19.226 65.648  1.000 48.420  ? 27  SER MMM O   1 
ATOM 18325 C CB  . SER M 2 27  ? 113.752 -18.016 68.354  1.000 56.880  ? 27  SER MMM CB  1 
ATOM 18326 O OG  . SER M 2 27  ? 114.407 -19.186 68.769  1.000 64.530  ? 27  SER MMM OG  1 
ATOM 18327 N N   . ASN M 2 28  ? 113.300 -17.738 65.073  1.000 46.870  ? 28  ASN MMM N   1 
ATOM 18328 C CA  . ASN M 2 28  ? 112.976 -18.405 63.783  1.000 42.140  ? 28  ASN MMM CA  1 
ATOM 18329 C C   . ASN M 2 28  ? 113.371 -17.473 62.622  1.000 40.490  ? 28  ASN MMM C   1 
ATOM 18330 O O   . ASN M 2 28  ? 114.545 -17.536 62.190  1.000 36.200  ? 28  ASN MMM O   1 
ATOM 18331 C CB  . ASN M 2 28  ? 111.537 -18.930 63.754  1.000 40.160  ? 28  ASN MMM CB  1 
ATOM 18332 C CG  . ASN M 2 28  ? 110.516 -17.936 64.221  1.000 39.020  ? 28  ASN MMM CG  1 
ATOM 18333 O OD1 . ASN M 2 28  ? 110.382 -16.876 63.624  1.000 34.460  ? 28  ASN MMM OD1 1 
ATOM 18334 N ND2 . ASN M 2 28  ? 109.781 -18.292 65.256  1.000 42.850  ? 28  ASN MMM ND2 1 
ATOM 18335 N N   . ILE M 2 29  ? 112.439 -16.635 62.150  1.000 36.530  ? 29  ILE MMM N   1 
ATOM 18336 C CA  . ILE M 2 29  ? 112.556 -15.904 60.853  1.000 37.130  ? 29  ILE MMM CA  1 
ATOM 18337 C C   . ILE M 2 29  ? 113.717 -14.911 60.908  1.000 36.780  ? 29  ILE MMM C   1 
ATOM 18338 O O   . ILE M 2 29  ? 114.285 -14.627 59.825  1.000 45.440  ? 29  ILE MMM O   1 
ATOM 18339 C CB  . ILE M 2 29  ? 111.230 -15.222 60.462  1.000 36.320  ? 29  ILE MMM CB  1 
ATOM 18340 C CG1 . ILE M 2 29  ? 110.145 -16.266 60.184  1.000 37.190  ? 29  ILE MMM CG1 1 
ATOM 18341 C CG2 . ILE M 2 29  ? 111.445 -14.276 59.286  1.000 35.660  ? 29  ILE MMM CG2 1 
ATOM 18342 C CD1 . ILE M 2 29  ? 108.866 -15.719 59.584  1.000 38.340  ? 29  ILE MMM CD1 1 
ATOM 18343 N N   . GLY M 2 30  ? 114.051 -14.410 62.098  1.000 35.950  ? 30  GLY MMM N   1 
ATOM 18344 C CA  . GLY M 2 30  ? 115.161 -13.462 62.299  1.000 35.990  ? 30  GLY MMM CA  1 
ATOM 18345 C C   . GLY M 2 30  ? 116.464 -14.041 61.792  1.000 36.730  ? 30  GLY MMM C   1 
ATOM 18346 O O   . GLY M 2 30  ? 117.133 -13.398 60.947  1.000 31.970  ? 30  GLY MMM O   1 
ATOM 18347 N N   . SER M 2 31  ? 116.758 -15.266 62.217  1.000 41.400  ? 31  SER MMM N   1 
ATOM 18348 C CA  . SER M 2 31  ? 118.048 -15.957 61.970  1.000 42.890  ? 31  SER MMM CA  1 
ATOM 18349 C C   . SER M 2 31  ? 117.924 -17.079 60.939  1.000 34.550  ? 31  SER MMM C   1 
ATOM 18350 O O   . SER M 2 31  ? 118.977 -17.595 60.611  1.000 32.580  ? 31  SER MMM O   1 
ATOM 18351 C CB  . SER M 2 31  ? 118.589 -16.500 63.259  1.000 49.730  ? 31  SER MMM CB  1 
ATOM 18352 O OG  . SER M 2 31  ? 118.959 -15.448 64.144  1.000 65.600  ? 31  SER MMM OG  1 
ATOM 18353 N N   . ASN M 2 32  ? 116.719 -17.425 60.454  1.000 30.030  ? 32  ASN MMM N   1 
ATOM 18354 C CA  . ASN M 2 32  ? 116.518 -18.569 59.520  1.000 30.350  ? 32  ASN MMM CA  1 
ATOM 18355 C C   . ASN M 2 32  ? 115.620 -18.176 58.340  1.000 30.940  ? 32  ASN MMM C   1 
ATOM 18356 O O   . ASN M 2 32  ? 114.765 -17.302 58.455  1.000 31.750  ? 32  ASN MMM O   1 
ATOM 18357 C CB  . ASN M 2 32  ? 116.042 -19.810 60.270  1.000 30.090  ? 32  ASN MMM CB  1 
ATOM 18358 C CG  . ASN M 2 32  ? 116.987 -20.178 61.400  1.000 32.010  ? 32  ASN MMM CG  1 
ATOM 18359 O OD1 . ASN M 2 32  ? 118.120 -20.601 61.172  1.000 32.840  ? 32  ASN MMM OD1 1 
ATOM 18360 N ND2 . ASN M 2 32  ? 116.539 -20.038 62.641  1.000 34.780  ? 32  ASN MMM ND2 1 
ATOM 18361 N N   . PRO M 2 33  ? 115.817 -18.785 57.143  1.000 28.750  ? 33  PRO MMM N   1 
ATOM 18362 C CA  . PRO M 2 33  ? 115.037 -18.471 55.958  1.000 27.630  ? 33  PRO MMM CA  1 
ATOM 18363 C C   . PRO M 2 33  ? 113.635 -19.075 55.987  1.000 30.340  ? 33  PRO MMM C   1 
ATOM 18364 O O   . PRO M 2 33  ? 113.475 -20.192 56.517  1.000 37.760  ? 33  PRO MMM O   1 
ATOM 18365 C CB  . PRO M 2 33  ? 115.771 -19.175 54.807  1.000 27.100  ? 33  PRO MMM CB  1 
ATOM 18366 C CG  . PRO M 2 33  ? 117.071 -19.596 55.367  1.000 27.160  ? 33  PRO MMM CG  1 
ATOM 18367 C CD  . PRO M 2 33  ? 116.803 -19.828 56.841  1.000 29.210  ? 33  PRO MMM CD  1 
ATOM 18368 N N   . VAL M 2 34  ? 112.697 -18.380 55.341  1.000 30.260  ? 34  VAL MMM N   1 
ATOM 18369 C CA  . VAL M 2 34  ? 111.288 -18.829 55.145  1.000 29.540  ? 34  VAL MMM CA  1 
ATOM 18370 C C   . VAL M 2 34  ? 111.125 -19.444 53.753  1.000 29.240  ? 34  VAL MMM C   1 
ATOM 18371 O O   . VAL M 2 34  ? 111.430 -18.737 52.772  1.000 31.650  ? 34  VAL MMM O   1 
ATOM 18372 C CB  . VAL M 2 34  ? 110.337 -17.641 55.295  1.000 28.120  ? 34  VAL MMM CB  1 
ATOM 18373 C CG1 . VAL M 2 34  ? 108.900 -18.062 55.037  1.000 28.690  ? 34  VAL MMM CG1 1 
ATOM 18374 C CG2 . VAL M 2 34  ? 110.502 -16.981 56.646  1.000 27.380  ? 34  VAL MMM CG2 1 
ATOM 18375 N N   . ASN M 2 35  ? 110.648 -20.686 53.665  1.000 27.120  ? 35  ASN MMM N   1 
ATOM 18376 C CA  . ASN M 2 35  ? 110.089 -21.246 52.410  1.000 26.940  ? 35  ASN MMM CA  1 
ATOM 18377 C C   . ASN M 2 35  ? 108.562 -21.110 52.464  1.000 29.160  ? 35  ASN MMM C   1 
ATOM 18378 O O   . ASN M 2 35  ? 107.979 -21.208 53.568  1.000 30.720  ? 35  ASN MMM O   1 
ATOM 18379 C CB  . ASN M 2 35  ? 110.499 -22.698 52.160  1.000 27.460  ? 35  ASN MMM CB  1 
ATOM 18380 C CG  . ASN M 2 35  ? 111.983 -22.906 51.968  1.000 28.190  ? 35  ASN MMM CG  1 
ATOM 18381 O OD1 . ASN M 2 35  ? 112.784 -22.159 52.532  1.000 32.810  ? 35  ASN MMM OD1 1 
ATOM 18382 N ND2 . ASN M 2 35  ? 112.363 -23.946 51.224  1.000 23.170  ? 35  ASN MMM ND2 1 
ATOM 18383 N N   . TRP M 2 36  ? 107.962 -20.855 51.306  1.000 32.560  ? 36  TRP MMM N   1 
ATOM 18384 C CA  . TRP M 2 36  ? 106.496 -20.885 51.073  1.000 34.920  ? 36  TRP MMM CA  1 
ATOM 18385 C C   . TRP M 2 36  ? 106.144 -22.162 50.306  1.000 37.020  ? 36  TRP MMM C   1 
ATOM 18386 O O   . TRP M 2 36  ? 106.838 -22.462 49.308  1.000 37.120  ? 36  TRP MMM O   1 
ATOM 18387 C CB  . TRP M 2 36  ? 106.053 -19.635 50.298  1.000 33.910  ? 36  TRP MMM CB  1 
ATOM 18388 C CG  . TRP M 2 36  ? 106.102 -18.369 51.090  1.000 31.900  ? 36  TRP MMM CG  1 
ATOM 18389 C CD1 . TRP M 2 36  ? 107.142 -17.494 51.173  1.000 33.020  ? 36  TRP MMM CD1 1 
ATOM 18390 C CD2 . TRP M 2 36  ? 105.062 -17.853 51.949  1.000 30.790  ? 36  TRP MMM CD2 1 
ATOM 18391 N NE1 . TRP M 2 36  ? 106.833 -16.466 52.031  1.000 35.120  ? 36  TRP MMM NE1 1 
ATOM 18392 C CE2 . TRP M 2 36  ? 105.562 -16.661 52.519  1.000 33.130  ? 36  TRP MMM CE2 1 
ATOM 18393 C CE3 . TRP M 2 36  ? 103.774 -18.275 52.276  1.000 30.120  ? 36  TRP MMM CE3 1 
ATOM 18394 C CZ2 . TRP M 2 36  ? 104.807 -15.883 53.401  1.000 31.770  ? 36  TRP MMM CZ2 1 
ATOM 18395 C CZ3 . TRP M 2 36  ? 103.024 -17.494 53.132  1.000 32.590  ? 36  TRP MMM CZ3 1 
ATOM 18396 C CH2 . TRP M 2 36  ? 103.537 -16.318 53.690  1.000 31.490  ? 36  TRP MMM CH2 1 
ATOM 18397 N N   . PHE M 2 37  ? 105.108 -22.878 50.747  1.000 39.430  ? 37  PHE MMM N   1 
ATOM 18398 C CA  . PHE M 2 37  ? 104.597 -24.086 50.043  1.000 42.710  ? 37  PHE MMM CA  1 
ATOM 18399 C C   . PHE M 2 37  ? 103.159 -23.832 49.600  1.000 43.310  ? 37  PHE MMM C   1 
ATOM 18400 O O   . PHE M 2 37  ? 102.372 -23.267 50.390  1.000 40.260  ? 37  PHE MMM O   1 
ATOM 18401 C CB  . PHE M 2 37  ? 104.724 -25.327 50.925  1.000 40.850  ? 37  PHE MMM CB  1 
ATOM 18402 C CG  . PHE M 2 37  ? 106.126 -25.560 51.423  1.000 40.170  ? 37  PHE MMM CG  1 
ATOM 18403 C CD1 . PHE M 2 37  ? 107.076 -26.167 50.616  1.000 39.210  ? 37  PHE MMM CD1 1 
ATOM 18404 C CD2 . PHE M 2 37  ? 106.496 -25.128 52.677  1.000 41.020  ? 37  PHE MMM CD2 1 
ATOM 18405 C CE1 . PHE M 2 37  ? 108.367 -26.383 51.065  1.000 36.810  ? 37  PHE MMM CE1 1 
ATOM 18406 C CE2 . PHE M 2 37  ? 107.787 -25.340 53.129  1.000 42.700  ? 37  PHE MMM CE2 1 
ATOM 18407 C CZ  . PHE M 2 37  ? 108.718 -25.959 52.316  1.000 41.940  ? 37  PHE MMM CZ  1 
ATOM 18408 N N   . GLN M 2 38  ? 102.865 -24.190 48.348  1.000 47.690  ? 38  GLN MMM N   1 
ATOM 18409 C CA  . GLN M 2 38  ? 101.518 -24.057 47.733  1.000 52.930  ? 38  GLN MMM CA  1 
ATOM 18410 C C   . GLN M 2 38  ? 100.865 -25.431 47.817  1.000 56.320  ? 38  GLN MMM C   1 
ATOM 18411 O O   . GLN M 2 38  ? 101.600 -26.423 47.573  1.000 53.440  ? 38  GLN MMM O   1 
ATOM 18412 C CB  . GLN M 2 38  ? 101.626 -23.575 46.287  1.000 52.140  ? 38  GLN MMM CB  1 
ATOM 18413 C CG  . GLN M 2 38  ? 100.283 -23.371 45.606  1.000 49.760  ? 38  GLN MMM CG  1 
ATOM 18414 C CD  . GLN M 2 38  ? 100.455 -23.064 44.145  1.000 48.350  ? 38  GLN MMM CD  1 
ATOM 18415 O OE1 . GLN M 2 38  ? 100.904 -23.911 43.372  1.000 43.930  ? 38  GLN MMM OE1 1 
ATOM 18416 N NE2 . GLN M 2 38  ? 100.069 -21.852 43.772  1.000 46.340  ? 38  GLN MMM NE2 1 
ATOM 18417 N N   . GLN M 2 39  ? 99.582  -25.481 48.217  1.000 54.690  ? 39  GLN MMM N   1 
ATOM 18418 C CA  . GLN M 2 39  ? 98.831  -26.748 48.372  1.000 54.800  ? 39  GLN MMM CA  1 
ATOM 18419 C C   . GLN M 2 39  ? 97.428  -26.593 47.787  1.000 57.750  ? 39  GLN MMM C   1 
ATOM 18420 O O   . GLN M 2 39  ? 96.613  -25.816 48.336  1.000 48.810  ? 39  GLN MMM O   1 
ATOM 18421 C CB  . GLN M 2 39  ? 98.754  -27.179 49.837  1.000 55.610  ? 39  GLN MMM CB  1 
ATOM 18422 C CG  . GLN M 2 39  ? 98.359  -28.640 50.012  1.000 54.410  ? 39  GLN MMM CG  1 
ATOM 18423 C CD  . GLN M 2 39  ? 98.316  -29.069 51.455  1.000 53.380  ? 39  GLN MMM CD  1 
ATOM 18424 O OE1 . GLN M 2 39  ? 98.072  -28.250 52.354  1.000 55.100  ? 39  GLN MMM OE1 1 
ATOM 18425 N NE2 . GLN M 2 39  ? 98.513  -30.360 51.672  1.000 58.390  ? 39  GLN MMM NE2 1 
ATOM 18426 N N   . PHE M 2 40  ? 97.165  -27.345 46.726  1.000 64.000  ? 40  PHE MMM N   1 
ATOM 18427 C CA  . PHE M 2 40  ? 95.809  -27.563 46.171  1.000 64.720  ? 40  PHE MMM CA  1 
ATOM 18428 C C   . PHE M 2 40  ? 95.179  -28.713 46.938  1.000 62.320  ? 40  PHE MMM C   1 
ATOM 18429 O O   . PHE M 2 40  ? 95.871  -29.686 47.235  1.000 61.570  ? 40  PHE MMM O   1 
ATOM 18430 C CB  . PHE M 2 40  ? 95.873  -27.870 44.672  1.000 65.480  ? 40  PHE MMM CB  1 
ATOM 18431 C CG  . PHE M 2 40  ? 96.590  -26.805 43.895  1.000 63.580  ? 40  PHE MMM CG  1 
ATOM 18432 C CD1 . PHE M 2 40  ? 96.142  -25.497 43.975  1.000 61.720  ? 40  PHE MMM CD1 1 
ATOM 18433 C CD2 . PHE M 2 40  ? 97.705  -27.098 43.121  1.000 60.430  ? 40  PHE MMM CD2 1 
ATOM 18434 C CE1 . PHE M 2 40  ? 96.798  -24.494 43.291  1.000 62.210  ? 40  PHE MMM CE1 1 
ATOM 18435 C CE2 . PHE M 2 40  ? 98.358  -26.090 42.435  1.000 60.590  ? 40  PHE MMM CE2 1 
ATOM 18436 C CZ  . PHE M 2 40  ? 97.901  -24.793 42.520  1.000 61.020  ? 40  PHE MMM CZ  1 
ATOM 18437 N N   . PRO M 2 41  ? 93.860  -28.628 47.247  1.000 62.670  ? 41  PRO MMM N   1 
ATOM 18438 C CA  . PRO M 2 41  ? 93.093  -29.742 47.809  1.000 58.020  ? 41  PRO MMM CA  1 
ATOM 18439 C C   . PRO M 2 41  ? 93.498  -31.116 47.262  1.000 51.510  ? 41  PRO MMM C   1 
ATOM 18440 O O   . PRO M 2 41  ? 93.657  -31.247 46.064  1.000 48.410  ? 41  PRO MMM O   1 
ATOM 18441 C CB  . PRO M 2 41  ? 91.657  -29.426 47.358  1.000 59.010  ? 41  PRO MMM CB  1 
ATOM 18442 C CG  . PRO M 2 41  ? 91.606  -27.905 47.340  1.000 62.380  ? 41  PRO MMM CG  1 
ATOM 18443 C CD  . PRO M 2 41  ? 93.012  -27.448 47.012  1.000 62.260  ? 41  PRO MMM CD  1 
ATOM 18444 N N   . GLY M 2 42  ? 93.718  -32.071 48.161  1.000 50.250  ? 42  GLY MMM N   1 
ATOM 18445 C CA  . GLY M 2 42  ? 93.934  -33.491 47.826  1.000 56.100  ? 42  GLY MMM CA  1 
ATOM 18446 C C   . GLY M 2 42  ? 95.277  -33.758 47.174  1.000 61.880  ? 42  GLY MMM C   1 
ATOM 18447 O O   . GLY M 2 42  ? 95.459  -34.906 46.726  1.000 64.020  ? 42  GLY MMM O   1 
ATOM 18448 N N   . THR M 2 43  ? 96.177  -32.767 47.092  1.000 70.090  ? 43  THR MMM N   1 
ATOM 18449 C CA  . THR M 2 43  ? 97.597  -32.987 46.698  1.000 66.720  ? 43  THR MMM CA  1 
ATOM 18450 C C   . THR M 2 43  ? 98.504  -32.616 47.882  1.000 63.480  ? 43  THR MMM C   1 
ATOM 18451 O O   . THR M 2 43  ? 98.034  -32.006 48.894  1.000 49.600  ? 43  THR MMM O   1 
ATOM 18452 C CB  . THR M 2 43  ? 97.986  -32.253 45.404  1.000 59.450  ? 43  THR MMM CB  1 
ATOM 18453 O OG1 . THR M 2 43  ? 97.640  -30.875 45.520  1.000 62.100  ? 43  THR MMM OG1 1 
ATOM 18454 N N   . ALA M 2 44  ? 99.777  -32.982 47.754  1.000 60.720  ? 44  ALA MMM N   1 
ATOM 18455 C CA  . ALA M 2 44  ? 100.850 -32.647 48.710  1.000 60.930  ? 44  ALA MMM CA  1 
ATOM 18456 C C   . ALA M 2 44  ? 101.124 -31.153 48.634  1.000 60.270  ? 44  ALA MMM C   1 
ATOM 18457 O O   . ALA M 2 44  ? 100.766 -30.516 47.652  1.000 71.740  ? 44  ALA MMM O   1 
ATOM 18458 C CB  . ALA M 2 44  ? 102.083 -33.443 48.360  1.000 62.210  ? 44  ALA MMM CB  1 
ATOM 18459 N N   . PRO M 2 45  ? 101.782 -30.555 49.652  1.000 60.050  ? 45  PRO MMM N   1 
ATOM 18460 C CA  . PRO M 2 45  ? 102.421 -29.251 49.510  1.000 52.450  ? 45  PRO MMM CA  1 
ATOM 18461 C C   . PRO M 2 45  ? 103.523 -29.342 48.453  1.000 48.560  ? 45  PRO MMM C   1 
ATOM 18462 O O   . PRO M 2 45  ? 104.049 -30.418 48.249  1.000 49.820  ? 45  PRO MMM O   1 
ATOM 18463 C CB  . PRO M 2 45  ? 103.071 -28.970 50.873  1.000 54.990  ? 45  PRO MMM CB  1 
ATOM 18464 C CG  . PRO M 2 45  ? 102.316 -29.868 51.816  1.000 61.200  ? 45  PRO MMM CG  1 
ATOM 18465 C CD  . PRO M 2 45  ? 101.990 -31.104 50.997  1.000 64.740  ? 45  PRO MMM CD  1 
ATOM 18466 N N   . LYS M 2 46  ? 103.826 -28.220 47.802  1.000 45.880  ? 46  LYS MMM N   1 
ATOM 18467 C CA  . LYS M 2 46  ? 104.935 -28.116 46.824  1.000 44.520  ? 46  LYS MMM CA  1 
ATOM 18468 C C   . LYS M 2 46  ? 105.659 -26.800 47.099  1.000 41.600  ? 46  LYS MMM C   1 
ATOM 18469 O O   . LYS M 2 46  ? 105.004 -25.830 47.588  1.000 34.120  ? 46  LYS MMM O   1 
ATOM 18470 C CB  . LYS M 2 46  ? 104.377 -28.191 45.399  1.000 47.670  ? 46  LYS MMM CB  1 
ATOM 18471 C CG  . LYS M 2 46  ? 105.368 -28.092 44.251  1.000 48.660  ? 46  LYS MMM CG  1 
ATOM 18472 C CD  . LYS M 2 46  ? 104.724 -28.580 42.940  1.000 50.830  ? 46  LYS MMM CD  1 
ATOM 18473 C CE  . LYS M 2 46  ? 105.460 -28.171 41.686  1.000 53.250  ? 46  LYS MMM CE  1 
ATOM 18474 N NZ  . LYS M 2 46  ? 106.854 -28.654 41.732  1.000 53.970  ? 46  LYS MMM NZ  1 
ATOM 18475 N N   . LEU M 2 47  ? 106.965 -26.785 46.831  1.000 37.980  ? 47  LEU MMM N   1 
ATOM 18476 C CA  . LEU M 2 47  ? 107.803 -25.578 47.041  1.000 35.790  ? 47  LEU MMM CA  1 
ATOM 18477 C C   . LEU M 2 47  ? 107.359 -24.492 46.062  1.000 35.960  ? 47  LEU MMM C   1 
ATOM 18478 O O   . LEU M 2 47  ? 107.330 -24.776 44.849  1.000 34.800  ? 47  LEU MMM O   1 
ATOM 18479 C CB  . LEU M 2 47  ? 109.268 -25.956 46.815  1.000 34.180  ? 47  LEU MMM CB  1 
ATOM 18480 C CG  . LEU M 2 47  ? 110.270 -24.844 47.099  1.000 30.900  ? 47  LEU MMM CG  1 
ATOM 18481 C CD1 . LEU M 2 47  ? 110.154 -24.372 48.530  1.000 30.980  ? 47  LEU MMM CD1 1 
ATOM 18482 C CD2 . LEU M 2 47  ? 111.686 -25.335 46.869  1.000 28.920  ? 47  LEU MMM CD2 1 
ATOM 18483 N N   . LEU M 2 48  ? 107.016 -23.311 46.579  1.000 36.360  ? 48  LEU MMM N   1 
ATOM 18484 C CA  . LEU M 2 48  ? 106.594 -22.129 45.776  1.000 36.320  ? 48  LEU MMM CA  1 
ATOM 18485 C C   . LEU M 2 48  ? 107.703 -21.063 45.825  1.000 35.790  ? 48  LEU MMM C   1 
ATOM 18486 O O   . LEU M 2 48  ? 108.182 -20.638 44.769  1.000 34.130  ? 48  LEU MMM O   1 
ATOM 18487 C CB  . LEU M 2 48  ? 105.283 -21.596 46.357  1.000 36.530  ? 48  LEU MMM CB  1 
ATOM 18488 C CG  . LEU M 2 48  ? 104.717 -20.381 45.620  1.000 36.560  ? 48  LEU MMM CG  1 
ATOM 18489 C CD1 . LEU M 2 48  ? 104.198 -20.827 44.268  1.000 34.030  ? 48  LEU MMM CD1 1 
ATOM 18490 C CD2 . LEU M 2 48  ? 103.664 -19.637 46.446  1.000 36.200  ? 48  LEU MMM CD2 1 
ATOM 18491 N N   . ILE M 2 49  ? 108.093 -20.655 47.032  1.000 37.290  ? 49  ILE MMM N   1 
ATOM 18492 C CA  . ILE M 2 49  ? 109.239 -19.740 47.289  1.000 37.830  ? 49  ILE MMM CA  1 
ATOM 18493 C C   . ILE M 2 49  ? 110.172 -20.428 48.276  1.000 35.020  ? 49  ILE MMM C   1 
ATOM 18494 O O   . ILE M 2 49  ? 109.644 -21.047 49.197  1.000 41.500  ? 49  ILE MMM O   1 
ATOM 18495 C CB  . ILE M 2 49  ? 108.738 -18.392 47.844  1.000 41.160  ? 49  ILE MMM CB  1 
ATOM 18496 C CG1 . ILE M 2 49  ? 107.834 -17.663 46.844  1.000 41.010  ? 49  ILE MMM CG1 1 
ATOM 18497 C CG2 . ILE M 2 49  ? 109.903 -17.522 48.301  1.000 41.350  ? 49  ILE MMM CG2 1 
ATOM 18498 C CD1 . ILE M 2 49  ? 108.560 -17.210 45.612  1.000 39.560  ? 49  ILE MMM CD1 1 
ATOM 18499 N N   . TYR M 2 50  ? 111.487 -20.292 48.102  1.000 32.890  ? 50  TYR MMM N   1 
ATOM 18500 C CA  . TYR M 2 50  ? 112.515 -20.676 49.106  1.000 34.540  ? 50  TYR MMM CA  1 
ATOM 18501 C C   . TYR M 2 50  ? 113.421 -19.488 49.446  1.000 31.730  ? 50  TYR MMM C   1 
ATOM 18502 O O   . TYR M 2 50  ? 113.492 -18.532 48.694  1.000 32.720  ? 50  TYR MMM O   1 
ATOM 18503 C CB  . TYR M 2 50  ? 113.315 -21.878 48.605  1.000 34.980  ? 50  TYR MMM CB  1 
ATOM 18504 C CG  . TYR M 2 50  ? 114.316 -21.596 47.524  1.000 31.750  ? 50  TYR MMM CG  1 
ATOM 18505 C CD1 . TYR M 2 50  ? 113.939 -21.518 46.193  1.000 31.670  ? 50  TYR MMM CD1 1 
ATOM 18506 C CD2 . TYR M 2 50  ? 115.652 -21.461 47.825  1.000 31.650  ? 50  TYR MMM CD2 1 
ATOM 18507 C CE1 . TYR M 2 50  ? 114.855 -21.279 45.178  1.000 29.400  ? 50  TYR MMM CE1 1 
ATOM 18508 C CE2 . TYR M 2 50  ? 116.587 -21.237 46.820  1.000 33.240  ? 50  TYR MMM CE2 1 
ATOM 18509 C CZ  . TYR M 2 50  ? 116.192 -21.145 45.496  1.000 29.120  ? 50  TYR MMM CZ  1 
ATOM 18510 O OH  . TYR M 2 50  ? 117.142 -20.894 44.557  1.000 26.180  ? 50  TYR MMM OH  1 
ATOM 18511 N N   . ALA M 2 51  ? 114.100 -19.559 50.576  1.000 28.330  ? 51  ALA MMM N   1 
ATOM 18512 C CA  . ALA M 2 51  ? 115.077 -18.539 51.022  1.000 28.700  ? 51  ALA MMM CA  1 
ATOM 18513 C C   . ALA M 2 51  ? 114.446 -17.149 50.935  1.000 26.920  ? 51  ALA MMM C   1 
ATOM 18514 O O   . ALA M 2 51  ? 115.094 -16.228 50.434  1.000 26.290  ? 51  ALA MMM O   1 
ATOM 18515 C CB  . ALA M 2 51  ? 116.358 -18.649 50.224  1.000 28.790  ? 51  ALA MMM CB  1 
ATOM 18516 N N   . ASN M 2 52  ? 113.207 -17.027 51.404  1.000 28.030  ? 52  ASN MMM N   1 
ATOM 18517 C CA  . ASN M 2 52  ? 112.482 -15.741 51.623  1.000 30.300  ? 52  ASN MMM CA  1 
ATOM 18518 C C   . ASN M 2 52  ? 111.915 -15.200 50.309  1.000 30.630  ? 52  ASN MMM C   1 
ATOM 18519 O O   . ASN M 2 52  ? 110.732 -14.725 50.367  1.000 31.340  ? 52  ASN MMM O   1 
ATOM 18520 C CB  . ASN M 2 52  ? 113.361 -14.682 52.282  1.000 30.310  ? 52  ASN MMM CB  1 
ATOM 18521 C CG  . ASN M 2 52  ? 113.990 -15.173 53.568  1.000 32.410  ? 52  ASN MMM CG  1 
ATOM 18522 O OD1 . ASN M 2 52  ? 113.298 -15.464 54.548  1.000 38.080  ? 52  ASN MMM OD1 1 
ATOM 18523 N ND2 . ASN M 2 52  ? 115.310 -15.225 53.585  1.000 30.960  ? 52  ASN MMM ND2 1 
ATOM 18524 N N   . THR M 2 53  ? 112.693 -15.269 49.209  1.000 29.720  ? 53  THR MMM N   1 
ATOM 18525 C CA  . THR M 2 53  ? 112.526 -14.421 47.997  1.000 30.160  ? 53  THR MMM CA  1 
ATOM 18526 C C   . THR M 2 53  ? 112.884 -15.130 46.685  1.000 29.790  ? 53  THR MMM C   1 
ATOM 18527 O O   . THR M 2 53  ? 112.892 -14.452 45.681  1.000 34.310  ? 53  THR MMM O   1 
ATOM 18528 C CB  . THR M 2 53  ? 113.394 -13.157 48.076  1.000 31.700  ? 53  THR MMM CB  1 
ATOM 18529 O OG1 . THR M 2 53  ? 114.778 -13.465 48.297  1.000 31.430  ? 53  THR MMM OG1 1 
ATOM 18530 C CG2 . THR M 2 53  ? 112.920 -12.214 49.160  1.000 33.560  ? 53  THR MMM CG2 1 
ATOM 18531 N N   . GLN M 2 54  ? 113.130 -16.433 46.653  1.000 29.490  ? 54  GLN MMM N   1 
ATOM 18532 C CA  . GLN M 2 54  ? 113.681 -17.118 45.453  1.000 32.480  ? 54  GLN MMM CA  1 
ATOM 18533 C C   . GLN M 2 54  ? 112.654 -18.098 44.894  1.000 39.370  ? 54  GLN MMM C   1 
ATOM 18534 O O   . GLN M 2 54  ? 111.984 -18.751 45.694  1.000 44.050  ? 54  GLN MMM O   1 
ATOM 18535 C CB  . GLN M 2 54  ? 114.963 -17.847 45.810  1.000 30.490  ? 54  GLN MMM CB  1 
ATOM 18536 C CG  . GLN M 2 54  ? 115.945 -16.944 46.511  1.000 32.000  ? 54  GLN MMM CG  1 
ATOM 18537 C CD  . GLN M 2 54  ? 116.478 -15.919 45.566  1.000 29.610  ? 54  GLN MMM CD  1 
ATOM 18538 O OE1 . GLN M 2 54  ? 117.131 -16.324 44.618  1.000 29.120  ? 54  GLN MMM OE1 1 
ATOM 18539 N NE2 . GLN M 2 54  ? 116.251 -14.636 45.850  1.000 25.950  ? 54  GLN MMM NE2 1 
ATOM 18540 N N   . ARG M 2 55  ? 112.559 -18.196 43.564  1.000 45.500  ? 55  ARG MMM N   1 
ATOM 18541 C CA  . ARG M 2 55  ? 111.619 -19.106 42.865  1.000 45.440  ? 55  ARG MMM CA  1 
ATOM 18542 C C   . ARG M 2 55  ? 112.383 -20.317 42.355  1.000 47.400  ? 55  ARG MMM C   1 
ATOM 18543 O O   . ARG M 2 55  ? 113.436 -20.187 41.752  1.000 50.320  ? 55  ARG MMM O   1 
ATOM 18544 C CB  . ARG M 2 55  ? 110.936 -18.382 41.710  1.000 50.930  ? 55  ARG MMM CB  1 
ATOM 18545 C CG  . ARG M 2 55  ? 109.870 -17.402 42.180  1.000 55.790  ? 55  ARG MMM CG  1 
ATOM 18546 C CD  . ARG M 2 55  ? 109.078 -16.783 41.055  1.000 62.960  ? 55  ARG MMM CD  1 
ATOM 18547 N NE  . ARG M 2 55  ? 109.956 -16.288 39.992  1.000 66.330  ? 55  ARG MMM NE  1 
ATOM 18548 C CZ  . ARG M 2 55  ? 110.540 -15.098 39.965  1.000 67.120  ? 55  ARG MMM CZ  1 
ATOM 18549 N NH1 . ARG M 2 55  ? 110.334 -14.223 40.943  1.000 74.120  ? 55  ARG MMM NH1 1 
ATOM 18550 N NH2 . ARG M 2 55  ? 111.289 -14.785 38.924  1.000 64.060  ? 55  ARG MMM NH2 1 
ATOM 18551 N N   . PRO M 2 56  ? 111.879 -21.547 42.574  1.000 49.130  ? 56  PRO MMM N   1 
ATOM 18552 C CA  . PRO M 2 56  ? 112.441 -22.707 41.885  1.000 47.600  ? 56  PRO MMM CA  1 
ATOM 18553 C C   . PRO M 2 56  ? 111.976 -22.619 40.426  1.000 48.770  ? 56  PRO MMM C   1 
ATOM 18554 O O   . PRO M 2 56  ? 111.038 -21.890 40.173  1.000 43.530  ? 56  PRO MMM O   1 
ATOM 18555 C CB  . PRO M 2 56  ? 111.844 -23.882 42.670  1.000 47.120  ? 56  PRO MMM CB  1 
ATOM 18556 C CG  . PRO M 2 56  ? 110.526 -23.349 43.249  1.000 43.850  ? 56  PRO MMM CG  1 
ATOM 18557 C CD  . PRO M 2 56  ? 110.730 -21.868 43.440  1.000 44.770  ? 56  PRO MMM CD  1 
ATOM 18558 N N   . SER M 2 57  ? 112.652 -23.304 39.498  1.000 59.580  ? 57  SER MMM N   1 
ATOM 18559 C CA  . SER M 2 57  ? 112.238 -23.288 38.066  1.000 67.220  ? 57  SER MMM CA  1 
ATOM 18560 C C   . SER M 2 57  ? 110.811 -23.853 37.963  1.000 63.500  ? 57  SER MMM C   1 
ATOM 18561 O O   . SER M 2 57  ? 110.543 -24.884 38.592  1.000 57.570  ? 57  SER MMM O   1 
ATOM 18562 C CB  . SER M 2 57  ? 113.225 -24.022 37.192  1.000 68.970  ? 57  SER MMM CB  1 
ATOM 18563 O OG  . SER M 2 57  ? 112.695 -24.226 35.897  1.000 70.000  ? 57  SER MMM OG  1 
ATOM 18564 N N   . GLY M 2 58  ? 109.917 -23.169 37.253  1.000 64.650  ? 58  GLY MMM N   1 
ATOM 18565 C CA  . GLY M 2 58  ? 108.521 -23.609 37.064  1.000 72.930  ? 58  GLY MMM CA  1 
ATOM 18566 C C   . GLY M 2 58  ? 107.528 -22.672 37.729  1.000 76.740  ? 58  GLY MMM C   1 
ATOM 18567 O O   . GLY M 2 58  ? 106.324 -22.749 37.391  1.000 85.580  ? 58  GLY MMM O   1 
ATOM 18568 N N   . VAL M 2 59  ? 108.005 -21.804 38.623  1.000 71.310  ? 59  VAL MMM N   1 
ATOM 18569 C CA  . VAL M 2 59  ? 107.146 -20.811 39.328  1.000 64.210  ? 59  VAL MMM CA  1 
ATOM 18570 C C   . VAL M 2 59  ? 107.219 -19.494 38.564  1.000 65.560  ? 59  VAL MMM C   1 
ATOM 18571 O O   . VAL M 2 59  ? 108.287 -18.910 38.409  1.000 59.780  ? 59  VAL MMM O   1 
ATOM 18572 C CB  . VAL M 2 59  ? 107.520 -20.651 40.811  1.000 54.270  ? 59  VAL MMM CB  1 
ATOM 18573 C CG1 . VAL M 2 59  ? 106.636 -19.639 41.520  1.000 50.740  ? 59  VAL MMM CG1 1 
ATOM 18574 C CG2 . VAL M 2 59  ? 107.471 -21.977 41.548  1.000 51.210  ? 59  VAL MMM CG2 1 
ATOM 18575 N N   . PRO M 2 60  ? 106.072 -19.012 38.045  1.000 69.260  ? 60  PRO MMM N   1 
ATOM 18576 C CA  . PRO M 2 60  ? 106.009 -17.714 37.371  1.000 67.020  ? 60  PRO MMM CA  1 
ATOM 18577 C C   . PRO M 2 60  ? 106.603 -16.510 38.124  1.000 59.020  ? 60  PRO MMM C   1 
ATOM 18578 O O   . PRO M 2 60  ? 106.532 -16.476 39.338  1.000 55.740  ? 60  PRO MMM O   1 
ATOM 18579 C CB  . PRO M 2 60  ? 104.494 -17.492 37.225  1.000 74.530  ? 60  PRO MMM CB  1 
ATOM 18580 C CG  . PRO M 2 60  ? 103.910 -18.887 37.141  1.000 80.560  ? 60  PRO MMM CG  1 
ATOM 18581 C CD  . PRO M 2 60  ? 104.775 -19.716 38.065  1.000 74.910  ? 60  PRO MMM CD  1 
ATOM 18582 N N   . ASP M 2 61  ? 107.100 -15.534 37.368  1.000 60.260  ? 61  ASP MMM N   1 
ATOM 18583 C CA  . ASP M 2 61  ? 107.586 -14.216 37.874  1.000 63.820  ? 61  ASP MMM CA  1 
ATOM 18584 C C   . ASP M 2 61  ? 106.559 -13.536 38.793  1.000 57.510  ? 61  ASP MMM C   1 
ATOM 18585 O O   . ASP M 2 61  ? 106.996 -12.736 39.620  1.000 50.730  ? 61  ASP MMM O   1 
ATOM 18586 C CB  . ASP M 2 61  ? 108.191 -13.362 36.761  1.000 71.640  ? 61  ASP MMM CB  1 
ATOM 18587 C CG  . ASP M 2 61  ? 107.214 -12.630 35.856  1.000 79.050  ? 61  ASP MMM CG  1 
ATOM 18588 O OD1 . ASP M 2 61  ? 106.053 -13.093 35.745  1.000 84.710  ? 61  ASP MMM OD1 1 
ATOM 18589 O OD2 . ASP M 2 61  ? 107.617 -11.596 35.309  1.000 80.440  ? 61  ASP MMM OD2 1 
ATOM 18590 N N   . ARG M 2 62  ? 105.265 -13.824 38.633  1.000 53.830  ? 62  ARG MMM N   1 
ATOM 18591 C CA  . ARG M 2 62  ? 104.144 -13.218 39.391  1.000 55.670  ? 62  ARG MMM CA  1 
ATOM 18592 C C   . ARG M 2 62  ? 104.380 -13.377 40.892  1.000 64.800  ? 62  ARG MMM C   1 
ATOM 18593 O O   . ARG M 2 62  ? 104.229 -12.377 41.654  1.000 70.700  ? 62  ARG MMM O   1 
ATOM 18594 C CB  . ARG M 2 62  ? 102.827 -13.900 39.015  1.000 57.440  ? 62  ARG MMM CB  1 
ATOM 18595 C CG  . ARG M 2 62  ? 102.636 -14.115 37.513  1.000 63.440  ? 62  ARG MMM CG  1 
ATOM 18596 C CD  . ARG M 2 62  ? 101.247 -14.577 37.100  1.000 62.400  ? 62  ARG MMM CD  1 
ATOM 18597 N NE  . ARG M 2 62  ? 100.541 -15.294 38.157  1.000 62.240  ? 62  ARG MMM NE  1 
ATOM 18598 C CZ  . ARG M 2 62  ? 100.097 -16.548 38.090  1.000 57.680  ? 62  ARG MMM CZ  1 
ATOM 18599 N NH1 . ARG M 2 62  ? 100.297 -17.299 37.017  1.000 58.710  ? 62  ARG MMM NH1 1 
ATOM 18600 N NH2 . ARG M 2 62  ? 99.457  -17.048 39.127  1.000 51.060  ? 62  ARG MMM NH2 1 
ATOM 18601 N N   . PHE M 2 63  ? 104.756 -14.594 41.294  1.000 65.430  ? 63  PHE MMM N   1 
ATOM 18602 C CA  . PHE M 2 63  ? 105.077 -14.987 42.692  1.000 52.570  ? 63  PHE MMM CA  1 
ATOM 18603 C C   . PHE M 2 63  ? 106.409 -14.374 43.130  1.000 49.950  ? 63  PHE MMM C   1 
ATOM 18604 O O   . PHE M 2 63  ? 107.450 -14.535 42.440  1.000 47.000  ? 63  PHE MMM O   1 
ATOM 18605 C CB  . PHE M 2 63  ? 105.115 -16.504 42.798  1.000 48.100  ? 63  PHE MMM CB  1 
ATOM 18606 C CG  . PHE M 2 63  ? 103.777 -17.159 42.558  1.000 47.110  ? 63  PHE MMM CG  1 
ATOM 18607 C CD1 . PHE M 2 63  ? 102.810 -17.213 43.560  1.000 42.380  ? 63  PHE MMM CD1 1 
ATOM 18608 C CD2 . PHE M 2 63  ? 103.491 -17.723 41.329  1.000 47.800  ? 63  PHE MMM CD2 1 
ATOM 18609 C CE1 . PHE M 2 63  ? 101.603 -17.841 43.353  1.000 38.800  ? 63  PHE MMM CE1 1 
ATOM 18610 C CE2 . PHE M 2 63  ? 102.275 -18.347 41.114  1.000 48.020  ? 63  PHE MMM CE2 1 
ATOM 18611 C CZ  . PHE M 2 63  ? 101.336 -18.395 42.126  1.000 45.370  ? 63  PHE MMM CZ  1 
ATOM 18612 N N   . SER M 2 64  ? 106.377 -13.664 44.251  1.000 49.190  ? 64  SER MMM N   1 
ATOM 18613 C CA  . SER M 2 64  ? 107.532 -12.895 44.766  1.000 55.720  ? 64  SER MMM CA  1 
ATOM 18614 C C   . SER M 2 64  ? 107.448 -12.801 46.294  1.000 58.150  ? 64  SER MMM C   1 
ATOM 18615 O O   . SER M 2 64  ? 106.363 -13.040 46.847  1.000 55.250  ? 64  SER MMM O   1 
ATOM 18616 C CB  . SER M 2 64  ? 107.554 -11.538 44.152  1.000 56.630  ? 64  SER MMM CB  1 
ATOM 18617 O OG  . SER M 2 64  ? 106.685 -10.683 44.867  1.000 54.420  ? 64  SER MMM OG  1 
ATOM 18618 N N   . GLY M 2 65  ? 108.551 -12.443 46.947  1.000 56.110  ? 65  GLY MMM N   1 
ATOM 18619 C CA  . GLY M 2 65  ? 108.608 -12.280 48.406  1.000 53.800  ? 65  GLY MMM CA  1 
ATOM 18620 C C   . GLY M 2 65  ? 109.325 -11.005 48.789  1.000 54.010  ? 65  GLY MMM C   1 
ATOM 18621 O O   . GLY M 2 65  ? 110.068 -10.475 47.964  1.000 57.480  ? 65  GLY MMM O   1 
ATOM 18622 N N   . SER M 2 66  ? 109.100 -10.544 50.015  1.000 53.410  ? 66  SER MMM N   1 
ATOM 18623 C CA  . SER M 2 66  ? 109.895 -9.489  50.682  1.000 53.250  ? 66  SER MMM CA  1 
ATOM 18624 C C   . SER M 2 66  ? 110.171 -9.930  52.118  1.000 49.350  ? 66  SER MMM C   1 
ATOM 18625 O O   . SER M 2 66  ? 109.279 -10.568 52.726  1.000 48.700  ? 66  SER MMM O   1 
ATOM 18626 C CB  . SER M 2 66  ? 109.177 -8.173  50.631  1.000 58.350  ? 66  SER MMM CB  1 
ATOM 18627 O OG  . SER M 2 66  ? 108.266 -8.042  51.718  1.000 61.210  ? 66  SER MMM OG  1 
ATOM 18628 N N   . LYS M 2 67  ? 111.385 -9.650  52.597  1.000 44.870  ? 67  LYS MMM N   1 
ATOM 18629 C CA  . LYS M 2 67  ? 111.829 -9.897  53.993  1.000 45.510  ? 67  LYS MMM CA  1 
ATOM 18630 C C   . LYS M 2 67  ? 112.128 -8.539  54.623  1.000 47.450  ? 67  LYS MMM C   1 
ATOM 18631 O O   . LYS M 2 67  ? 112.862 -7.762  54.008  1.000 54.750  ? 67  LYS MMM O   1 
ATOM 18632 C CB  . LYS M 2 67  ? 113.074 -10.796 54.038  1.000 43.210  ? 67  LYS MMM CB  1 
ATOM 18633 C CG  . LYS M 2 67  ? 113.545 -11.178 55.439  1.000 43.940  ? 67  LYS MMM CG  1 
ATOM 18634 C CD  . LYS M 2 67  ? 114.914 -11.829 55.507  1.000 41.650  ? 67  LYS MMM CD  1 
ATOM 18635 C CE  . LYS M 2 67  ? 115.039 -12.783 56.686  1.000 46.110  ? 67  LYS MMM CE  1 
ATOM 18636 N NZ  . LYS M 2 67  ? 114.982 -12.113 58.012  1.000 47.340  ? 67  LYS MMM NZ  1 
ATOM 18637 N N   . SER M 2 68  ? 111.575 -8.266  55.797  1.000 50.090  ? 68  SER MMM N   1 
ATOM 18638 C CA  . SER M 2 68  ? 112.005 -7.142  56.664  1.000 53.060  ? 68  SER MMM CA  1 
ATOM 18639 C C   . SER M 2 68  ? 112.165 -7.671  58.085  1.000 53.060  ? 68  SER MMM C   1 
ATOM 18640 O O   . SER M 2 68  ? 111.125 -7.909  58.727  1.000 55.950  ? 68  SER MMM O   1 
ATOM 18641 C CB  . SER M 2 68  ? 111.038 -5.990  56.587  1.000 57.730  ? 68  SER MMM CB  1 
ATOM 18642 O OG  . SER M 2 68  ? 111.578 -4.836  57.209  1.000 54.920  ? 68  SER MMM OG  1 
ATOM 18643 N N   . GLY M 2 69  ? 113.414 -7.903  58.520  1.000 51.910  ? 69  GLY MMM N   1 
ATOM 18644 C CA  . GLY M 2 69  ? 113.746 -8.493  59.834  1.000 51.860  ? 69  GLY MMM CA  1 
ATOM 18645 C C   . GLY M 2 69  ? 112.920 -9.751  60.096  1.000 56.910  ? 69  GLY MMM C   1 
ATOM 18646 O O   . GLY M 2 69  ? 112.923 -10.684 59.234  1.000 53.100  ? 69  GLY MMM O   1 
ATOM 18647 N N   . THR M 2 70  ? 112.163 -9.735  61.199  1.000 53.940  ? 70  THR MMM N   1 
ATOM 18648 C CA  . THR M 2 70  ? 111.435 -10.888 61.787  1.000 50.780  ? 70  THR MMM CA  1 
ATOM 18649 C C   . THR M 2 70  ? 110.161 -11.226 60.994  1.000 54.670  ? 70  THR MMM C   1 
ATOM 18650 O O   . THR M 2 70  ? 109.479 -12.213 61.352  1.000 56.090  ? 70  THR MMM O   1 
ATOM 18651 C CB  . THR M 2 70  ? 111.128 -10.601 63.272  1.000 51.350  ? 70  THR MMM CB  1 
ATOM 18652 O OG1 . THR M 2 70  ? 110.219 -11.548 63.817  1.000 49.840  ? 70  THR MMM OG1 1 
ATOM 18653 C CG2 . THR M 2 70  ? 110.554 -9.221  63.532  1.000 53.930  ? 70  THR MMM CG2 1 
ATOM 18654 N N   . SER M 2 71  ? 109.806 -10.455 59.971  1.000 60.830  ? 71  SER MMM N   1 
ATOM 18655 C CA  . SER M 2 71  ? 108.569 -10.675 59.175  1.000 67.780  ? 71  SER MMM CA  1 
ATOM 18656 C C   . SER M 2 71  ? 108.937 -10.811 57.704  1.000 66.380  ? 71  SER MMM C   1 
ATOM 18657 O O   . SER M 2 71  ? 109.891 -10.130 57.254  1.000 67.990  ? 71  SER MMM O   1 
ATOM 18658 C CB  . SER M 2 71  ? 107.541 -9.581  59.372  1.000 72.040  ? 71  SER MMM CB  1 
ATOM 18659 O OG  . SER M 2 71  ? 108.123 -8.282  59.350  1.000 79.640  ? 71  SER MMM OG  1 
ATOM 18660 N N   . VAL M 2 72  ? 108.188 -11.662 57.007  1.000 61.800  ? 72  VAL MMM N   1 
ATOM 18661 C CA  . VAL M 2 72  ? 108.288 -11.911 55.545  1.000 61.260  ? 72  VAL MMM CA  1 
ATOM 18662 C C   . VAL M 2 72  ? 106.874 -11.789 54.982  1.000 63.240  ? 72  VAL MMM C   1 
ATOM 18663 O O   . VAL M 2 72  ? 105.922 -12.034 55.732  1.000 68.680  ? 72  VAL MMM O   1 
ATOM 18664 C CB  . VAL M 2 72  ? 108.892 -13.297 55.267  1.000 58.050  ? 72  VAL MMM CB  1 
ATOM 18665 C CG1 . VAL M 2 72  ? 108.614 -13.795 53.855  1.000 65.130  ? 72  VAL MMM CG1 1 
ATOM 18666 C CG2 . VAL M 2 72  ? 110.386 -13.300 55.532  1.000 54.980  ? 72  VAL MMM CG2 1 
ATOM 18667 N N   . SER M 2 73  ? 106.743 -11.436 53.708  1.000 64.240  ? 73  SER MMM N   1 
ATOM 18668 C CA  . SER M 2 73  ? 105.463 -11.524 52.966  1.000 59.140  ? 73  SER MMM CA  1 
ATOM 18669 C C   . SER M 2 73  ? 105.675 -12.281 51.648  1.000 54.220  ? 73  SER MMM C   1 
ATOM 18670 O O   . SER M 2 73  ? 106.845 -12.313 51.133  1.000 45.040  ? 73  SER MMM O   1 
ATOM 18671 C CB  . SER M 2 73  ? 104.878 -10.165 52.754  1.000 61.270  ? 73  SER MMM CB  1 
ATOM 18672 O OG  . SER M 2 73  ? 105.744 -9.373  51.972  1.000 58.830  ? 73  SER MMM OG  1 
ATOM 18673 N N   . LEU M 2 74  ? 104.613 -12.931 51.193  1.000 48.500  ? 74  LEU MMM N   1 
ATOM 18674 C CA  . LEU M 2 74  ? 104.476 -13.530 49.844  1.000 49.010  ? 74  LEU MMM CA  1 
ATOM 18675 C C   . LEU M 2 74  ? 103.567 -12.605 49.049  1.000 52.560  ? 74  LEU MMM C   1 
ATOM 18676 O O   . LEU M 2 74  ? 102.554 -12.160 49.618  1.000 59.440  ? 74  LEU MMM O   1 
ATOM 18677 C CB  . LEU M 2 74  ? 103.868 -14.930 49.944  1.000 44.800  ? 74  LEU MMM CB  1 
ATOM 18678 C CG  . LEU M 2 74  ? 103.397 -15.542 48.627  1.000 44.770  ? 74  LEU MMM CG  1 
ATOM 18679 C CD1 . LEU M 2 74  ? 104.560 -15.772 47.678  1.000 43.740  ? 74  LEU MMM CD1 1 
ATOM 18680 C CD2 . LEU M 2 74  ? 102.649 -16.850 48.864  1.000 48.910  ? 74  LEU MMM CD2 1 
ATOM 18681 N N   . ALA M 2 75  ? 103.933 -12.322 47.800  1.000 54.330  ? 75  ALA MMM N   1 
ATOM 18682 C CA  . ALA M 2 75  ? 103.168 -11.476 46.865  1.000 53.170  ? 75  ALA MMM CA  1 
ATOM 18683 C C   . ALA M 2 75  ? 102.777 -12.298 45.635  1.000 51.340  ? 75  ALA MMM C   1 
ATOM 18684 O O   . ALA M 2 75  ? 103.657 -12.624 44.820  1.000 51.460  ? 75  ALA MMM O   1 
ATOM 18685 C CB  . ALA M 2 75  ? 103.998 -10.275 46.505  1.000 51.990  ? 75  ALA MMM CB  1 
ATOM 18686 N N   . ILE M 2 76  ? 101.491 -12.611 45.516  1.000 54.840  ? 76  ILE MMM N   1 
ATOM 18687 C CA  . ILE M 2 76  ? 100.904 -13.192 44.275  1.000 67.860  ? 76  ILE MMM CA  1 
ATOM 18688 C C   . ILE M 2 76  ? 100.349 -12.042 43.435  1.000 69.510  ? 76  ILE MMM C   1 
ATOM 18689 O O   . ILE M 2 76  ? 99.299  -11.527 43.811  1.000 74.320  ? 76  ILE MMM O   1 
ATOM 18690 C CB  . ILE M 2 76  ? 99.810  -14.223 44.607  1.000 68.730  ? 76  ILE MMM CB  1 
ATOM 18691 C CG1 . ILE M 2 76  ? 100.290 -15.222 45.661  1.000 65.190  ? 76  ILE MMM CG1 1 
ATOM 18692 C CG2 . ILE M 2 76  ? 99.341  -14.907 43.326  1.000 72.980  ? 76  ILE MMM CG2 1 
ATOM 18693 C CD1 . ILE M 2 76  ? 99.231  -16.159 46.155  1.000 66.620  ? 76  ILE MMM CD1 1 
ATOM 18694 N N   . SER M 2 77  ? 101.046 -11.640 42.372  1.000 69.580  ? 77  SER MMM N   1 
ATOM 18695 C CA  . SER M 2 77  ? 100.582 -10.597 41.422  1.000 66.710  ? 77  SER MMM CA  1 
ATOM 18696 C C   . SER M 2 77  ? 99.929  -11.293 40.231  1.000 68.140  ? 77  SER MMM C   1 
ATOM 18697 O O   . SER M 2 77  ? 100.143 -12.520 40.071  1.000 66.310  ? 77  SER MMM O   1 
ATOM 18698 C CB  . SER M 2 77  ? 101.691 -9.675  41.003  1.000 65.750  ? 77  SER MMM CB  1 
ATOM 18699 O OG  . SER M 2 77  ? 102.592 -10.330 40.129  1.000 69.660  ? 77  SER MMM OG  1 
ATOM 18700 N N   . GLY M 2 78  ? 99.147  -10.548 39.447  1.000 63.820  ? 78  GLY MMM N   1 
ATOM 18701 C CA  . GLY M 2 78  ? 98.399  -11.084 38.297  1.000 64.350  ? 78  GLY MMM CA  1 
ATOM 18702 C C   . GLY M 2 78  ? 97.575  -12.288 38.700  1.000 58.300  ? 78  GLY MMM C   1 
ATOM 18703 O O   . GLY M 2 78  ? 97.719  -13.353 38.064  1.000 55.320  ? 78  GLY MMM O   1 
ATOM 18704 N N   . LEU M 2 79  ? 96.758  -12.121 39.735  1.000 57.160  ? 79  LEU MMM N   1 
ATOM 18705 C CA  . LEU M 2 79  ? 96.001  -13.236 40.369  1.000 65.500  ? 79  LEU MMM CA  1 
ATOM 18706 C C   . LEU M 2 79  ? 95.176  -13.980 39.319  1.000 63.870  ? 79  LEU MMM C   1 
ATOM 18707 O O   . LEU M 2 79  ? 94.557  -13.314 38.500  1.000 74.010  ? 79  LEU MMM O   1 
ATOM 18708 C CB  . LEU M 2 79  ? 95.131  -12.680 41.496  1.000 65.070  ? 79  LEU MMM CB  1 
ATOM 18709 C CG  . LEU M 2 79  ? 94.450  -13.751 42.347  1.000 69.530  ? 79  LEU MMM CG  1 
ATOM 18710 C CD1 . LEU M 2 79  ? 95.469  -14.561 43.128  1.000 66.480  ? 79  LEU MMM CD1 1 
ATOM 18711 C CD2 . LEU M 2 79  ? 93.454  -13.108 43.311  1.000 81.030  ? 79  LEU MMM CD2 1 
ATOM 18712 N N   . GLN M 2 80  ? 95.182  -15.311 39.357  1.000 68.350  ? 80  GLN MMM N   1 
ATOM 18713 C CA  . GLN M 2 80  ? 94.401  -16.197 38.456  1.000 72.850  ? 80  GLN MMM CA  1 
ATOM 18714 C C   . GLN M 2 80  ? 93.652  -17.232 39.308  1.000 82.360  ? 80  GLN MMM C   1 
ATOM 18715 O O   . GLN M 2 80  ? 93.937  -17.335 40.510  1.000 88.640  ? 80  GLN MMM O   1 
ATOM 18716 C CB  . GLN M 2 80  ? 95.312  -16.892 37.450  1.000 66.840  ? 80  GLN MMM CB  1 
ATOM 18717 C CG  . GLN M 2 80  ? 96.030  -15.927 36.526  1.000 71.930  ? 80  GLN MMM CG  1 
ATOM 18718 C CD  . GLN M 2 80  ? 96.903  -16.655 35.527  1.000 82.170  ? 80  GLN MMM CD  1 
ATOM 18719 O OE1 . GLN M 2 80  ? 96.763  -17.857 35.301  1.000 81.250  ? 80  GLN MMM OE1 1 
ATOM 18720 N NE2 . GLN M 2 80  ? 97.816  -15.925 34.902  1.000 89.150  ? 80  GLN MMM NE2 1 
ATOM 18721 N N   . SER M 2 81  ? 92.684  -17.938 38.712  1.000 83.630  ? 81  SER MMM N   1 
ATOM 18722 C CA  . SER M 2 81  ? 91.792  -18.896 39.410  1.000 78.620  ? 81  SER MMM CA  1 
ATOM 18723 C C   . SER M 2 81  ? 92.605  -20.135 39.781  1.000 81.860  ? 81  SER MMM C   1 
ATOM 18724 O O   . SER M 2 81  ? 92.302  -20.726 40.839  1.000 80.510  ? 81  SER MMM O   1 
ATOM 18725 C CB  . SER M 2 81  ? 90.581  -19.246 38.581  1.000 76.010  ? 81  SER MMM CB  1 
ATOM 18726 O OG  . SER M 2 81  ? 90.934  -19.900 37.362  1.000 70.980  ? 81  SER MMM OG  1 
ATOM 18727 N N   . GLU M 2 82  ? 93.607  -20.476 38.962  1.000 82.310  ? 82  GLU MMM N   1 
ATOM 18728 C CA  . GLU M 2 82  ? 94.489  -21.664 39.163  1.000 76.970  ? 82  GLU MMM CA  1 
ATOM 18729 C C   . GLU M 2 82  ? 95.338  -21.447 40.421  1.000 69.910  ? 82  GLU MMM C   1 
ATOM 18730 O O   . GLU M 2 82  ? 96.000  -22.414 40.834  1.000 62.090  ? 82  GLU MMM O   1 
ATOM 18731 C CB  . GLU M 2 82  ? 95.347  -21.935 37.922  1.000 76.390  ? 82  GLU MMM CB  1 
ATOM 18732 C CG  . GLU M 2 82  ? 94.555  -22.213 36.658  1.000 78.580  ? 82  GLU MMM CG  1 
ATOM 18733 C CD  . GLU M 2 82  ? 94.168  -20.991 35.831  1.000 88.670  ? 82  GLU MMM CD  1 
ATOM 18734 O OE1 . GLU M 2 82  ? 94.329  -19.839 36.314  1.000 92.740  ? 82  GLU MMM OE1 1 
ATOM 18735 O OE2 . GLU M 2 82  ? 93.684  -21.188 34.699  1.000 95.160  ? 82  GLU MMM OE2 1 
ATOM 18736 N N   . ASP M 2 83  ? 95.311  -20.236 41.006  1.000 65.490  ? 83  ASP MMM N   1 
ATOM 18737 C CA  . ASP M 2 83  ? 96.055  -19.848 42.239  1.000 69.170  ? 83  ASP MMM CA  1 
ATOM 18738 C C   . ASP M 2 83  ? 95.211  -20.101 43.497  1.000 72.470  ? 83  ASP MMM C   1 
ATOM 18739 O O   . ASP M 2 83  ? 95.695  -19.794 44.612  1.000 69.830  ? 83  ASP MMM O   1 
ATOM 18740 C CB  . ASP M 2 83  ? 96.456  -18.368 42.214  1.000 65.240  ? 83  ASP MMM CB  1 
ATOM 18741 C CG  . ASP M 2 83  ? 97.478  -18.032 41.147  1.000 63.960  ? 83  ASP MMM CG  1 
ATOM 18742 O OD1 . ASP M 2 83  ? 98.089  -18.988 40.611  1.000 56.650  ? 83  ASP MMM OD1 1 
ATOM 18743 O OD2 . ASP M 2 83  ? 97.690  -16.810 40.887  1.000 62.340  ? 83  ASP MMM OD2 1 
ATOM 18744 N N   . GLU M 2 84  ? 93.991  -20.607 43.343  1.000 73.760  ? 84  GLU MMM N   1 
ATOM 18745 C CA  . GLU M 2 84  ? 93.103  -20.887 44.497  1.000 75.650  ? 84  GLU MMM CA  1 
ATOM 18746 C C   . GLU M 2 84  ? 93.660  -22.123 45.189  1.000 72.910  ? 84  GLU MMM C   1 
ATOM 18747 O O   . GLU M 2 84  ? 93.891  -23.161 44.482  1.000 63.010  ? 84  GLU MMM O   1 
ATOM 18748 C CB  . GLU M 2 84  ? 91.645  -21.079 44.074  1.000 87.780  ? 84  GLU MMM CB  1 
ATOM 18749 C CG  . GLU M 2 84  ? 90.745  -20.023 44.688  1.000 90.630  ? 84  GLU MMM CG  1 
ATOM 18750 C CD  . GLU M 2 84  ? 89.248  -20.256 44.585  1.000 90.080  ? 84  GLU MMM CD  1 
ATOM 18751 O OE1 . GLU M 2 84  ? 88.852  -21.426 44.380  1.000 87.270  ? 84  GLU MMM OE1 1 
ATOM 18752 O OE2 . GLU M 2 84  ? 88.485  -19.270 44.706  1.000 88.580  ? 84  GLU MMM OE2 1 
ATOM 18753 N N   . GLY M 2 85  ? 93.937  -21.998 46.489  1.000 71.490  ? 85  GLY MMM N   1 
ATOM 18754 C CA  . GLY M 2 85  ? 94.585  -23.053 47.289  1.000 68.950  ? 85  GLY MMM CA  1 
ATOM 18755 C C   . GLY M 2 85  ? 95.027  -22.520 48.638  1.000 68.410  ? 85  GLY MMM C   1 
ATOM 18756 O O   . GLY M 2 85  ? 94.707  -21.345 48.952  1.000 62.260  ? 85  GLY MMM O   1 
ATOM 18757 N N   . ASP M 2 86  ? 95.731  -23.357 49.407  1.000 66.700  ? 86  ASP MMM N   1 
ATOM 18758 C CA  . ASP M 2 86  ? 96.304  -23.014 50.740  1.000 65.240  ? 86  ASP MMM CA  1 
ATOM 18759 C C   . ASP M 2 86  ? 97.797  -22.675 50.547  1.000 54.560  ? 86  ASP MMM C   1 
ATOM 18760 O O   . ASP M 2 86  ? 98.488  -23.389 49.765  1.000 47.180  ? 86  ASP MMM O   1 
ATOM 18761 C CB  . ASP M 2 86  ? 96.036  -24.146 51.748  1.000 73.580  ? 86  ASP MMM CB  1 
ATOM 18762 C CG  . ASP M 2 86  ? 94.572  -24.447 52.075  1.000 73.960  ? 86  ASP MMM CG  1 
ATOM 18763 O OD1 . ASP M 2 86  ? 93.724  -23.580 51.759  1.000 70.790  ? 86  ASP MMM OD1 1 
ATOM 18764 O OD2 . ASP M 2 86  ? 94.279  -25.570 52.536  1.000 71.100  ? 86  ASP MMM OD2 1 
ATOM 18765 N N   . TYR M 2 87  ? 98.281  -21.610 51.198  1.000 45.750  ? 87  TYR MMM N   1 
ATOM 18766 C CA  . TYR M 2 87  ? 99.692  -21.145 51.141  1.000 44.910  ? 87  TYR MMM CA  1 
ATOM 18767 C C   . TYR M 2 87  ? 100.270 -21.277 52.545  1.000 46.890  ? 87  TYR MMM C   1 
ATOM 18768 O O   . TYR M 2 87  ? 99.799  -20.613 53.495  1.000 50.860  ? 87  TYR MMM O   1 
ATOM 18769 C CB  . TYR M 2 87  ? 99.774  -19.732 50.545  1.000 44.480  ? 87  TYR MMM CB  1 
ATOM 18770 C CG  . TYR M 2 87  ? 99.435  -19.722 49.079  1.000 43.700  ? 87  TYR MMM CG  1 
ATOM 18771 C CD1 . TYR M 2 87  ? 98.123  -19.849 48.664  1.000 44.960  ? 87  TYR MMM CD1 1 
ATOM 18772 C CD2 . TYR M 2 87  ? 100.420 -19.691 48.108  1.000 42.430  ? 87  TYR MMM CD2 1 
ATOM 18773 C CE1 . TYR M 2 87  ? 97.787  -19.909 47.323  1.000 45.440  ? 87  TYR MMM CE1 1 
ATOM 18774 C CE2 . TYR M 2 87  ? 100.105 -19.787 46.760  1.000 44.540  ? 87  TYR MMM CE2 1 
ATOM 18775 C CZ  . TYR M 2 87  ? 98.782  -19.904 46.365  1.000 44.610  ? 87  TYR MMM CZ  1 
ATOM 18776 O OH  . TYR M 2 87  ? 98.434  -19.957 45.045  1.000 42.390  ? 87  TYR MMM OH  1 
ATOM 18777 N N   . HIS M 2 88  ? 101.265 -22.156 52.670  1.000 45.470  ? 88  HIS MMM N   1 
ATOM 18778 C CA  . HIS M 2 88  ? 101.920 -22.529 53.950  1.000 41.690  ? 88  HIS MMM CA  1 
ATOM 18779 C C   . HIS M 2 88  ? 103.283 -21.848 54.113  1.000 36.370  ? 88  HIS MMM C   1 
ATOM 18780 O O   . HIS M 2 88  ? 104.134 -21.925 53.200  1.000 37.010  ? 88  HIS MMM O   1 
ATOM 18781 C CB  . HIS M 2 88  ? 101.975 -24.050 54.087  1.000 46.450  ? 88  HIS MMM CB  1 
ATOM 18782 C CG  . HIS M 2 88  ? 100.634 -24.703 54.029  1.000 53.200  ? 88  HIS MMM CG  1 
ATOM 18783 N ND1 . HIS M 2 88  ? 99.718  -24.623 55.068  1.000 61.450  ? 88  HIS MMM ND1 1 
ATOM 18784 C CD2 . HIS M 2 88  ? 100.038 -25.449 53.073  1.000 57.320  ? 88  HIS MMM CD2 1 
ATOM 18785 C CE1 . HIS M 2 88  ? 98.611  -25.263 54.741  1.000 60.880  ? 88  HIS MMM CE1 1 
ATOM 18786 N NE2 . HIS M 2 88  ? 98.794  -25.812 53.542  1.000 59.050  ? 88  HIS MMM NE2 1 
ATOM 18787 N N   . CYS M 2 89  ? 103.464 -21.178 55.240  1.000 33.480  ? 89  CYS MMM N   1 
ATOM 18788 C CA  . CYS M 2 89  ? 104.704 -20.471 55.624  1.000 36.810  ? 89  CYS MMM CA  1 
ATOM 18789 C C   . CYS M 2 89  ? 105.531 -21.305 56.596  1.000 33.530  ? 89  CYS MMM C   1 
ATOM 18790 O O   . CYS M 2 89  ? 104.942 -21.737 57.581  1.000 39.590  ? 89  CYS MMM O   1 
ATOM 18791 C CB  . CYS M 2 89  ? 104.281 -19.135 56.239  1.000 42.060  ? 89  CYS MMM CB  1 
ATOM 18792 S SG  . CYS M 2 89  ? 105.677 -18.075 56.650  1.000 53.540  ? 89  CYS MMM SG  1 
ATOM 18793 N N   . ALA M 2 90  ? 106.810 -21.559 56.337  1.000 29.290  ? 90  ALA MMM N   1 
ATOM 18794 C CA  . ALA M 2 90  ? 107.658 -22.429 57.198  1.000 28.460  ? 90  ALA MMM CA  1 
ATOM 18795 C C   . ALA M 2 90  ? 109.063 -21.872 57.386  1.000 28.780  ? 90  ALA MMM C   1 
ATOM 18796 O O   . ALA M 2 90  ? 109.568 -21.198 56.468  1.000 30.890  ? 90  ALA MMM O   1 
ATOM 18797 C CB  . ALA M 2 90  ? 107.735 -23.844 56.716  1.000 27.510  ? 90  ALA MMM CB  1 
ATOM 18798 N N   . ALA M 2 91  ? 109.671 -22.152 58.535  1.000 31.080  ? 91  ALA MMM N   1 
ATOM 18799 C CA  . ALA M 2 91  ? 111.029 -21.673 58.894  1.000 33.300  ? 91  ALA MMM CA  1 
ATOM 18800 C C   . ALA M 2 91  ? 111.539 -22.441 60.112  1.000 31.800  ? 91  ALA MMM C   1 
ATOM 18801 O O   . ALA M 2 91  ? 110.712 -22.778 60.984  1.000 31.090  ? 91  ALA MMM O   1 
ATOM 18802 C CB  . ALA M 2 91  ? 110.989 -20.190 59.166  1.000 32.950  ? 91  ALA MMM CB  1 
ATOM 18803 N N   . TRP M 2 92  ? 112.847 -22.683 60.172  1.000 30.860  ? 92  TRP MMM N   1 
ATOM 18804 C CA  . TRP M 2 92  ? 113.483 -23.354 61.336  1.000 31.570  ? 92  TRP MMM CA  1 
ATOM 18805 C C   . TRP M 2 92  ? 113.457 -22.429 62.546  1.000 32.570  ? 92  TRP MMM C   1 
ATOM 18806 O O   . TRP M 2 92  ? 113.657 -21.229 62.356  1.000 35.150  ? 92  TRP MMM O   1 
ATOM 18807 C CB  . TRP M 2 92  ? 114.920 -23.754 61.022  1.000 29.740  ? 92  TRP MMM CB  1 
ATOM 18808 C CG  . TRP M 2 92  ? 115.613 -24.469 62.133  1.000 25.800  ? 92  TRP MMM CG  1 
ATOM 18809 C CD1 . TRP M 2 92  ? 116.461 -23.936 63.050  1.000 26.680  ? 92  TRP MMM CD1 1 
ATOM 18810 C CD2 . TRP M 2 92  ? 115.525 -25.870 62.427  1.000 24.870  ? 92  TRP MMM CD2 1 
ATOM 18811 N NE1 . TRP M 2 92  ? 116.913 -24.913 63.902  1.000 26.300  ? 92  TRP MMM NE1 1 
ATOM 18812 C CE2 . TRP M 2 92  ? 116.337 -26.106 63.551  1.000 24.920  ? 92  TRP MMM CE2 1 
ATOM 18813 C CE3 . TRP M 2 92  ? 114.802 -26.938 61.879  1.000 25.360  ? 92  TRP MMM CE3 1 
ATOM 18814 C CZ2 . TRP M 2 92  ? 116.485 -27.372 64.113  1.000 24.710  ? 92  TRP MMM CZ2 1 
ATOM 18815 C CZ3 . TRP M 2 92  ? 114.945 -28.186 62.442  1.000 25.840  ? 92  TRP MMM CZ3 1 
ATOM 18816 C CH2 . TRP M 2 92  ? 115.776 -28.400 63.542  1.000 25.240  ? 92  TRP MMM CH2 1 
ATOM 18817 N N   . ASP M 2 93  ? 113.217 -22.974 63.741  1.000 33.690  ? 93  ASP MMM N   1 
ATOM 18818 C CA  . ASP M 2 93  ? 113.283 -22.198 65.007  1.000 33.930  ? 93  ASP MMM CA  1 
ATOM 18819 C C   . ASP M 2 93  ? 114.445 -22.731 65.839  1.000 30.690  ? 93  ASP MMM C   1 
ATOM 18820 O O   . ASP M 2 93  ? 114.410 -23.912 66.184  1.000 31.670  ? 93  ASP MMM O   1 
ATOM 18821 C CB  . ASP M 2 93  ? 111.958 -22.227 65.771  1.000 34.870  ? 93  ASP MMM CB  1 
ATOM 18822 C CG  . ASP M 2 93  ? 112.019 -21.364 67.007  1.000 35.970  ? 93  ASP MMM CG  1 
ATOM 18823 O OD1 . ASP M 2 93  ? 112.926 -21.609 67.836  1.000 35.660  ? 93  ASP MMM OD1 1 
ATOM 18824 O OD2 . ASP M 2 93  ? 111.207 -20.432 67.098  1.000 42.610  ? 93  ASP MMM OD2 1 
ATOM 18825 N N   . ASP M 2 94  ? 115.423 -21.874 66.128  1.000 28.720  ? 94  ASP MMM N   1 
ATOM 18826 C CA  . ASP M 2 94  ? 116.684 -22.238 66.816  1.000 29.480  ? 94  ASP MMM CA  1 
ATOM 18827 C C   . ASP M 2 94  ? 116.475 -22.694 68.255  1.000 31.790  ? 94  ASP MMM C   1 
ATOM 18828 O O   . ASP M 2 94  ? 117.258 -23.537 68.718  1.000 34.210  ? 94  ASP MMM O   1 
ATOM 18829 C CB  . ASP M 2 94  ? 117.686 -21.083 66.812  1.000 28.520  ? 94  ASP MMM CB  1 
ATOM 18830 C CG  . ASP M 2 94  ? 118.331 -20.871 65.459  1.000 29.190  ? 94  ASP MMM CG  1 
ATOM 18831 O OD1 . ASP M 2 94  ? 118.557 -21.899 64.762  1.000 32.020  ? 94  ASP MMM OD1 1 
ATOM 18832 O OD2 . ASP M 2 94  ? 118.603 -19.695 65.105  1.000 28.070  ? 94  ASP MMM OD2 1 
ATOM 18833 N N   . SER M 2 95  ? 115.482 -22.134 68.941  1.000 33.410  ? 95  SER MMM N   1 
ATOM 18834 C CA  . SER M 2 95  ? 115.196 -22.449 70.362  1.000 35.230  ? 95  SER MMM CA  1 
ATOM 18835 C C   . SER M 2 95  ? 114.404 -23.767 70.475  1.000 34.030  ? 95  SER MMM C   1 
ATOM 18836 O O   . SER M 2 95  ? 114.754 -24.591 71.304  1.000 35.630  ? 95  SER MMM O   1 
ATOM 18837 C CB  . SER M 2 95  ? 114.475 -21.303 71.058  1.000 39.490  ? 95  SER MMM CB  1 
ATOM 18838 O OG  . SER M 2 95  ? 113.190 -21.051 70.492  1.000 46.800  ? 95  SER MMM OG  1 
ATOM 18839 N N   . LEU M 2 96  ? 113.442 -24.008 69.584  1.000 34.840  ? 96  LEU MMM N   1 
ATOM 18840 C CA  . LEU M 2 96  ? 112.576 -25.221 69.600  1.000 34.750  ? 96  LEU MMM CA  1 
ATOM 18841 C C   . LEU M 2 96  ? 113.328 -26.355 68.904  1.000 34.940  ? 96  LEU MMM C   1 
ATOM 18842 O O   . LEU M 2 96  ? 112.817 -27.470 68.928  1.000 40.680  ? 96  LEU MMM O   1 
ATOM 18843 C CB  . LEU M 2 96  ? 111.221 -25.018 68.912  1.000 36.280  ? 96  LEU MMM CB  1 
ATOM 18844 C CG  . LEU M 2 96  ? 110.393 -23.829 69.400  1.000 35.510  ? 96  LEU MMM CG  1 
ATOM 18845 C CD1 . LEU M 2 96  ? 109.050 -23.781 68.719  1.000 34.020  ? 96  LEU MMM CD1 1 
ATOM 18846 C CD2 . LEU M 2 96  ? 110.231 -23.877 70.913  1.000 36.930  ? 96  LEU MMM CD2 1 
ATOM 18847 N N   . LYS M 2 97  ? 114.470 -26.088 68.287  1.000 36.770  ? 97  LYS MMM N   1 
ATOM 18848 C CA  . LYS M 2 97  ? 115.201 -27.071 67.445  1.000 41.090  ? 97  LYS MMM CA  1 
ATOM 18849 C C   . LYS M 2 97  ? 114.192 -27.877 66.605  1.000 37.140  ? 97  LYS MMM C   1 
ATOM 18850 O O   . LYS M 2 97  ? 114.147 -29.133 66.690  1.000 33.520  ? 97  LYS MMM O   1 
ATOM 18851 C CB  . LYS M 2 97  ? 116.098 -27.945 68.326  1.000 48.400  ? 97  LYS MMM CB  1 
ATOM 18852 C CG  . LYS M 2 97  ? 117.277 -27.203 68.938  1.000 58.720  ? 97  LYS MMM CG  1 
ATOM 18853 C CD  . LYS M 2 97  ? 118.476 -28.108 69.277  1.000 67.950  ? 97  LYS MMM CD  1 
ATOM 18854 C CE  . LYS M 2 97  ? 119.529 -27.405 70.112  1.000 72.920  ? 97  LYS MMM CE  1 
ATOM 18855 N NZ  . LYS M 2 97  ? 119.813 -26.046 69.581  1.000 74.170  ? 97  LYS MMM NZ  1 
ATOM 18856 N N   . GLY M 2 98  ? 113.414 -27.173 65.793  1.000 31.890  ? 98  GLY MMM N   1 
ATOM 18857 C CA  . GLY M 2 98  ? 112.466 -27.813 64.871  1.000 31.940  ? 98  GLY MMM CA  1 
ATOM 18858 C C   . GLY M 2 98  ? 111.964 -26.845 63.820  1.000 31.170  ? 98  GLY MMM C   1 
ATOM 18859 O O   . GLY M 2 98  ? 112.271 -25.639 63.904  1.000 28.660  ? 98  GLY MMM O   1 
ATOM 18860 N N   . TRP M 2 99  ? 111.205 -27.367 62.874  1.000 31.180  ? 99  TRP MMM N   1 
ATOM 18861 C CA  . TRP M 2 99  ? 110.477 -26.558 61.873  1.000 33.400  ? 99  TRP MMM CA  1 
ATOM 18862 C C   . TRP M 2 99  ? 109.180 -26.057 62.504  1.000 34.720  ? 99  TRP MMM C   1 
ATOM 18863 O O   . TRP M 2 99  ? 108.416 -26.890 63.019  1.000 36.170  ? 99  TRP MMM O   1 
ATOM 18864 C CB  . TRP M 2 99  ? 110.250 -27.366 60.584  1.000 31.270  ? 99  TRP MMM CB  1 
ATOM 18865 C CG  . TRP M 2 99  ? 111.531 -27.666 59.871  1.000 30.790  ? 99  TRP MMM CG  1 
ATOM 18866 C CD1 . TRP M 2 99  ? 112.277 -28.803 59.960  1.000 31.410  ? 99  TRP MMM CD1 1 
ATOM 18867 C CD2 . TRP M 2 99  ? 112.263 -26.779 59.012  1.000 30.350  ? 99  TRP MMM CD2 1 
ATOM 18868 N NE1 . TRP M 2 99  ? 113.405 -28.696 59.194  1.000 32.180  ? 99  TRP MMM NE1 1 
ATOM 18869 C CE2 . TRP M 2 99  ? 113.420 -27.462 58.600  1.000 30.880  ? 99  TRP MMM CE2 1 
ATOM 18870 C CE3 . TRP M 2 99  ? 112.060 -25.476 58.567  1.000 32.150  ? 99  TRP MMM CE3 1 
ATOM 18871 C CZ2 . TRP M 2 99  ? 114.355 -26.894 57.739  1.000 31.780  ? 99  TRP MMM CZ2 1 
ATOM 18872 C CZ3 . TRP M 2 99  ? 112.981 -24.920 57.706  1.000 37.210  ? 99  TRP MMM CZ3 1 
ATOM 18873 C CH2 . TRP M 2 99  ? 114.127 -25.613 57.316  1.000 33.470  ? 99  TRP MMM CH2 1 
ATOM 18874 N N   . VAL M 2 100 ? 108.944 -24.744 62.437  1.000 35.450  ? 100 VAL MMM N   1 
ATOM 18875 C CA  . VAL M 2 100 ? 107.617 -24.120 62.712  1.000 35.330  ? 100 VAL MMM CA  1 
ATOM 18876 C C   . VAL M 2 100 ? 106.958 -23.745 61.377  1.000 35.470  ? 100 VAL MMM C   1 
ATOM 18877 O O   . VAL M 2 100 ? 107.685 -23.335 60.423  1.000 34.990  ? 100 VAL MMM O   1 
ATOM 18878 C CB  . VAL M 2 100 ? 107.736 -22.920 63.660  1.000 35.990  ? 100 VAL MMM CB  1 
ATOM 18879 C CG1 . VAL M 2 100 ? 108.354 -23.358 64.966  1.000 38.490  ? 100 VAL MMM CG1 1 
ATOM 18880 C CG2 . VAL M 2 100 ? 108.544 -21.775 63.069  1.000 39.390  ? 100 VAL MMM CG2 1 
ATOM 18881 N N   . PHE M 2 101 ? 105.638 -23.942 61.289  1.000 34.370  ? 101 PHE MMM N   1 
ATOM 18882 C CA  . PHE M 2 101 ? 104.802 -23.528 60.133  1.000 33.100  ? 101 PHE MMM CA  1 
ATOM 18883 C C   . PHE M 2 101 ? 103.849 -22.460 60.632  1.000 36.530  ? 101 PHE MMM C   1 
ATOM 18884 O O   . PHE M 2 101 ? 103.793 -22.237 61.853  1.000 40.280  ? 101 PHE MMM O   1 
ATOM 18885 C CB  . PHE M 2 101 ? 104.023 -24.693 59.520  1.000 30.570  ? 101 PHE MMM CB  1 
ATOM 18886 C CG  . PHE M 2 101 ? 104.875 -25.671 58.760  1.000 30.710  ? 101 PHE MMM CG  1 
ATOM 18887 C CD1 . PHE M 2 101 ? 105.600 -26.638 59.441  1.000 32.050  ? 101 PHE MMM CD1 1 
ATOM 18888 C CD2 . PHE M 2 101 ? 104.973 -25.619 57.385  1.000 32.580  ? 101 PHE MMM CD2 1 
ATOM 18889 C CE1 . PHE M 2 101 ? 106.401 -27.541 58.757  1.000 33.460  ? 101 PHE MMM CE1 1 
ATOM 18890 C CE2 . PHE M 2 101 ? 105.790 -26.513 56.700  1.000 35.910  ? 101 PHE MMM CE2 1 
ATOM 18891 C CZ  . PHE M 2 101 ? 106.519 -27.462 57.391  1.000 34.430  ? 101 PHE MMM CZ  1 
ATOM 18892 N N   . GLY M 2 102 ? 103.190 -21.779 59.699  1.000 42.020  ? 102 GLY MMM N   1 
ATOM 18893 C CA  . GLY M 2 102 ? 102.051 -20.894 59.980  1.000 42.810  ? 102 GLY MMM CA  1 
ATOM 18894 C C   . GLY M 2 102 ? 100.777 -21.703 60.000  1.000 40.080  ? 102 GLY MMM C   1 
ATOM 18895 O O   . GLY M 2 102 ? 100.869 -22.931 59.890  1.000 37.140  ? 102 GLY MMM O   1 
ATOM 18896 N N   . GLY M 2 103 ? 99.639  -21.029 60.142  1.000 42.750  ? 103 GLY MMM N   1 
ATOM 18897 C CA  . GLY M 2 103 ? 98.314  -21.669 60.175  1.000 46.140  ? 103 GLY MMM CA  1 
ATOM 18898 C C   . GLY M 2 103 ? 97.967  -22.200 58.805  1.000 47.110  ? 103 GLY MMM C   1 
ATOM 18899 O O   . GLY M 2 103 ? 97.250  -23.201 58.696  1.000 54.710  ? 103 GLY MMM O   1 
ATOM 18900 N N   . GLY M 2 104 ? 98.512  -21.564 57.778  1.000 46.700  ? 104 GLY MMM N   1 
ATOM 18901 C CA  . GLY M 2 104 ? 97.985  -21.696 56.417  1.000 48.840  ? 104 GLY MMM CA  1 
ATOM 18902 C C   . GLY M 2 104 ? 97.086  -20.535 56.097  1.000 48.350  ? 104 GLY MMM C   1 
ATOM 18903 O O   . GLY M 2 104 ? 96.522  -19.952 57.024  1.000 47.590  ? 104 GLY MMM O   1 
ATOM 18904 N N   . THR M 2 105 ? 97.009  -20.197 54.817  1.000 53.810  ? 105 THR MMM N   1 
ATOM 18905 C CA  . THR M 2 105 ? 96.218  -19.077 54.266  1.000 59.250  ? 105 THR MMM CA  1 
ATOM 18906 C C   . THR M 2 105 ? 95.442  -19.642 53.081  1.000 65.730  ? 105 THR MMM C   1 
ATOM 18907 O O   . THR M 2 105 ? 96.096  -20.016 52.103  1.000 58.790  ? 105 THR MMM O   1 
ATOM 18908 C CB  . THR M 2 105 ? 97.145  -17.920 53.884  1.000 58.180  ? 105 THR MMM CB  1 
ATOM 18909 O OG1 . THR M 2 105 ? 97.838  -17.498 55.060  1.000 62.030  ? 105 THR MMM OG1 1 
ATOM 18910 C CG2 . THR M 2 105 ? 96.414  -16.746 53.286  1.000 59.110  ? 105 THR MMM CG2 1 
ATOM 18911 N N   . LYS M 2 106 ? 94.118  -19.767 53.197  1.000 79.890  ? 106 LYS MMM N   1 
ATOM 18912 C CA  . LYS M 2 106 ? 93.258  -20.142 52.045  1.000 85.060  ? 106 LYS MMM CA  1 
ATOM 18913 C C   . LYS M 2 106 ? 93.030  -18.867 51.231  1.000 89.370  ? 106 LYS MMM C   1 
ATOM 18914 O O   . LYS M 2 106 ? 92.424  -17.907 51.771  1.000 77.430  ? 106 LYS MMM O   1 
ATOM 18915 C CB  . LYS M 2 106 ? 91.957  -20.828 52.473  1.000 85.110  ? 106 LYS MMM CB  1 
ATOM 18916 C CG  . LYS M 2 106 ? 91.235  -21.548 51.344  1.000 87.240  ? 106 LYS MMM CG  1 
ATOM 18917 C CD  . LYS M 2 106 ? 89.925  -22.205 51.764  1.000 96.600  ? 106 LYS MMM CD  1 
ATOM 18918 C CE  . LYS M 2 106 ? 90.077  -23.375 52.721  1.000 104.880 ? 106 LYS MMM CE  1 
ATOM 18919 N NZ  . LYS M 2 106 ? 90.539  -24.605 52.039  1.000 105.210 ? 106 LYS MMM NZ  1 
ATOM 18920 N N   . LEU M 2 107 ? 93.559  -18.849 50.008  1.000 87.890  ? 107 LEU MMM N   1 
ATOM 18921 C CA  . LEU M 2 107 ? 93.397  -17.745 49.038  1.000 83.320  ? 107 LEU MMM CA  1 
ATOM 18922 C C   . LEU M 2 107 ? 92.171  -18.056 48.185  1.000 85.380  ? 107 LEU MMM C   1 
ATOM 18923 O O   . LEU M 2 107 ? 92.227  -19.073 47.435  1.000 73.750  ? 107 LEU MMM O   1 
ATOM 18924 C CB  . LEU M 2 107 ? 94.659  -17.664 48.173  1.000 86.120  ? 107 LEU MMM CB  1 
ATOM 18925 C CG  . LEU M 2 107 ? 94.708  -16.497 47.188  1.000 80.950  ? 107 LEU MMM CG  1 
ATOM 18926 C CD1 . LEU M 2 107 ? 94.906  -15.173 47.918  1.000 71.770  ? 107 LEU MMM CD1 1 
ATOM 18927 C CD2 . LEU M 2 107 ? 95.776  -16.747 46.135  1.000 77.240  ? 107 LEU MMM CD2 1 
ATOM 18928 N N   . THR M 2 108 ? 91.115  -17.254 48.327  1.000 97.670  ? 108 THR MMM N   1 
ATOM 18929 C CA  . THR M 2 108 ? 89.871  -17.354 47.524  1.000 103.020 ? 108 THR MMM CA  1 
ATOM 18930 C C   . THR M 2 108 ? 89.909  -16.273 46.440  1.000 95.130  ? 108 THR MMM C   1 
ATOM 18931 O O   . THR M 2 108 ? 90.334  -15.145 46.739  1.000 73.570  ? 108 THR MMM O   1 
ATOM 18932 C CB  . THR M 2 108 ? 88.595  -17.293 48.378  1.000 107.010 ? 108 THR MMM CB  1 
ATOM 18933 O OG1 . THR M 2 108 ? 88.764  -16.321 49.416  1.000 113.060 ? 108 THR MMM OG1 1 
ATOM 18934 C CG2 . THR M 2 108 ? 88.225  -18.637 48.977  1.000 92.450  ? 108 THR MMM CG2 1 
ATOM 18935 N N   . VAL M 2 109 ? 89.383  -16.575 45.249  1.000 91.900  ? 109 VAL MMM N   1 
ATOM 18936 C CA  . VAL M 2 109 ? 89.422  -15.655 44.076  1.000 89.340  ? 109 VAL MMM CA  1 
ATOM 18937 C C   . VAL M 2 109 ? 87.996  -15.238 43.649  1.000 83.740  ? 109 VAL MMM C   1 
ATOM 18938 O O   . VAL M 2 109 ? 87.072  -15.966 43.237  1.000 65.970  ? 109 VAL MMM O   1 
ATOM 18939 C CB  . VAL M 2 109 ? 90.232  -16.333 42.960  1.000 91.370  ? 109 VAL MMM CB  1 
ATOM 18940 C CG1 . VAL M 2 109 ? 89.449  -17.439 42.261  1.000 89.970  ? 109 VAL MMM CG1 1 
ATOM 18941 C CG2 . VAL M 2 109 ? 90.753  -15.307 41.976  1.000 99.450  ? 109 VAL MMM CG2 1 
ATOM 18942 N N   . GLU N 3 1   ? 113.828 -36.846 37.841  1.000 56.740  ? 1   GLU NNN N   1 
ATOM 18943 C CA  . GLU N 3 1   ? 112.988 -36.216 38.897  1.000 52.110  ? 1   GLU NNN CA  1 
ATOM 18944 C C   . GLU N 3 1   ? 113.420 -36.799 40.241  1.000 48.610  ? 1   GLU NNN C   1 
ATOM 18945 O O   . GLU N 3 1   ? 114.247 -37.737 40.299  1.000 43.130  ? 1   GLU NNN O   1 
ATOM 18946 C CB  . GLU N 3 1   ? 111.476 -36.403 38.655  1.000 47.390  ? 1   GLU NNN CB  1 
ATOM 18947 N N   . VAL N 3 2   ? 112.924 -36.193 41.305  1.000 52.660  ? 2   VAL NNN N   1 
ATOM 18948 C CA  . VAL N 3 2   ? 113.055 -36.682 42.705  1.000 55.150  ? 2   VAL NNN CA  1 
ATOM 18949 C C   . VAL N 3 2   ? 111.664 -37.157 43.088  1.000 54.090  ? 2   VAL NNN C   1 
ATOM 18950 O O   . VAL N 3 2   ? 110.709 -36.373 42.939  1.000 53.770  ? 2   VAL NNN O   1 
ATOM 18951 C CB  . VAL N 3 2   ? 113.572 -35.570 43.648  1.000 55.630  ? 2   VAL NNN CB  1 
ATOM 18952 C CG1 . VAL N 3 2   ? 113.164 -35.772 45.096  1.000 50.980  ? 2   VAL NNN CG1 1 
ATOM 18953 C CG2 . VAL N 3 2   ? 115.086 -35.433 43.552  1.000 55.610  ? 2   VAL NNN CG2 1 
ATOM 18954 N N   . GLN N 3 3   ? 111.540 -38.391 43.565  1.000 55.790  ? 3   GLN NNN N   1 
ATOM 18955 C CA  . GLN N 3 3   ? 110.233 -38.918 44.039  1.000 58.770  ? 3   GLN NNN CA  1 
ATOM 18956 C C   . GLN N 3 3   ? 110.443 -39.500 45.452  1.000 48.090  ? 3   GLN NNN C   1 
ATOM 18957 O O   . GLN N 3 3   ? 111.419 -40.262 45.658  1.000 41.410  ? 3   GLN NNN O   1 
ATOM 18958 C CB  . GLN N 3 3   ? 109.690 -39.875 42.966  1.000 64.700  ? 3   GLN NNN CB  1 
ATOM 18959 C CG  . GLN N 3 3   ? 108.176 -40.079 42.923  1.000 67.140  ? 3   GLN NNN CG  1 
ATOM 18960 C CD  . GLN N 3 3   ? 107.825 -41.501 42.545  1.000 71.110  ? 3   GLN NNN CD  1 
ATOM 18961 O OE1 . GLN N 3 3   ? 108.698 -42.351 42.330  1.000 66.560  ? 3   GLN NNN OE1 1 
ATOM 18962 N NE2 . GLN N 3 3   ? 106.530 -41.775 42.483  1.000 67.770  ? 3   GLN NNN NE2 1 
ATOM 18963 N N   . LEU N 3 4   ? 109.572 -39.088 46.379  1.000 38.080  ? 4   LEU NNN N   1 
ATOM 18964 C CA  . LEU N 3 4   ? 109.418 -39.695 47.715  1.000 34.160  ? 4   LEU NNN CA  1 
ATOM 18965 C C   . LEU N 3 4   ? 108.050 -40.379 47.754  1.000 34.140  ? 4   LEU NNN C   1 
ATOM 18966 O O   . LEU N 3 4   ? 107.070 -39.772 47.286  1.000 29.790  ? 4   LEU NNN O   1 
ATOM 18967 C CB  . LEU N 3 4   ? 109.530 -38.600 48.780  1.000 33.510  ? 4   LEU NNN CB  1 
ATOM 18968 C CG  . LEU N 3 4   ? 110.823 -37.785 48.777  1.000 30.800  ? 4   LEU NNN CG  1 
ATOM 18969 C CD1 . LEU N 3 4   ? 110.722 -36.577 49.695  1.000 28.610  ? 4   LEU NNN CD1 1 
ATOM 18970 C CD2 . LEU N 3 4   ? 112.022 -38.658 49.137  1.000 30.170  ? 4   LEU NNN CD2 1 
ATOM 18971 N N   . VAL N 3 5   ? 108.004 -41.607 48.277  1.000 39.940  ? 5   VAL NNN N   1 
ATOM 18972 C CA  . VAL N 3 5   ? 106.740 -42.394 48.387  1.000 44.400  ? 5   VAL NNN CA  1 
ATOM 18973 C C   . VAL N 3 5   ? 106.579 -42.923 49.810  1.000 42.820  ? 5   VAL NNN C   1 
ATOM 18974 O O   . VAL N 3 5   ? 107.415 -43.729 50.249  1.000 34.880  ? 5   VAL NNN O   1 
ATOM 18975 C CB  . VAL N 3 5   ? 106.668 -43.529 47.357  1.000 45.740  ? 5   VAL NNN CB  1 
ATOM 18976 C CG1 . VAL N 3 5   ? 105.228 -43.955 47.141  1.000 46.670  ? 5   VAL NNN CG1 1 
ATOM 18977 C CG2 . VAL N 3 5   ? 107.326 -43.138 46.045  1.000 48.300  ? 5   VAL NNN CG2 1 
ATOM 18978 N N   . GLU N 3 6   ? 105.530 -42.453 50.475  1.000 44.390  ? 6   GLU NNN N   1 
ATOM 18979 C CA  . GLU N 3 6   ? 105.153 -42.869 51.839  1.000 48.770  ? 6   GLU NNN CA  1 
ATOM 18980 C C   . GLU N 3 6   ? 104.229 -44.084 51.748  1.000 51.440  ? 6   GLU NNN C   1 
ATOM 18981 O O   . GLU N 3 6   ? 103.625 -44.283 50.685  1.000 45.190  ? 6   GLU NNN O   1 
ATOM 18982 C CB  . GLU N 3 6   ? 104.487 -41.722 52.589  1.000 54.290  ? 6   GLU NNN CB  1 
ATOM 18983 C CG  . GLU N 3 6   ? 105.368 -40.498 52.730  1.000 52.110  ? 6   GLU NNN CG  1 
ATOM 18984 C CD  . GLU N 3 6   ? 105.119 -39.431 51.684  1.000 54.360  ? 6   GLU NNN CD  1 
ATOM 18985 O OE1 . GLU N 3 6   ? 104.601 -39.765 50.600  1.000 54.620  ? 6   GLU NNN OE1 1 
ATOM 18986 O OE2 . GLU N 3 6   ? 105.423 -38.262 51.965  1.000 57.740  ? 6   GLU NNN OE2 1 
ATOM 18987 N N   . SER N 3 7   ? 104.154 -44.846 52.840  1.000 57.930  ? 7   SER NNN N   1 
ATOM 18988 C CA  . SER N 3 7   ? 103.429 -46.135 52.955  1.000 55.970  ? 7   SER NNN CA  1 
ATOM 18989 C C   . SER N 3 7   ? 103.455 -46.594 54.413  1.000 62.240  ? 7   SER NNN C   1 
ATOM 18990 O O   . SER N 3 7   ? 104.312 -46.105 55.174  1.000 62.540  ? 7   SER NNN O   1 
ATOM 18991 C CB  . SER N 3 7   ? 104.054 -47.170 52.063  1.000 47.890  ? 7   SER NNN CB  1 
ATOM 18992 O OG  . SER N 3 7   ? 105.421 -47.324 52.398  1.000 39.670  ? 7   SER NNN OG  1 
ATOM 18993 N N   . GLY N 3 8   ? 102.537 -47.495 54.771  1.000 64.570  ? 8   GLY NNN N   1 
ATOM 18994 C CA  . GLY N 3 8   ? 102.397 -48.073 56.121  1.000 56.110  ? 8   GLY NNN CA  1 
ATOM 18995 C C   . GLY N 3 8   ? 101.245 -47.450 56.888  1.000 49.550  ? 8   GLY NNN C   1 
ATOM 18996 O O   . GLY N 3 8   ? 100.859 -48.030 57.921  1.000 45.210  ? 8   GLY NNN O   1 
ATOM 18997 N N   . GLY N 3 9   ? 100.726 -46.310 56.411  1.000 46.290  ? 9   GLY NNN N   1 
ATOM 18998 C CA  . GLY N 3 9   ? 99.580  -45.620 57.030  1.000 47.990  ? 9   GLY NNN CA  1 
ATOM 18999 C C   . GLY N 3 9   ? 98.326  -46.459 56.916  1.000 50.410  ? 9   GLY NNN C   1 
ATOM 19000 O O   . GLY N 3 9   ? 98.191  -47.193 55.928  1.000 54.640  ? 9   GLY NNN O   1 
ATOM 19001 N N   . GLY N 3 10  ? 97.442  -46.377 57.902  1.000 53.660  ? 10  GLY NNN N   1 
ATOM 19002 C CA  . GLY N 3 10  ? 96.111  -47.006 57.850  1.000 53.660  ? 10  GLY NNN CA  1 
ATOM 19003 C C   . GLY N 3 10  ? 95.252  -46.641 59.051  1.000 58.490  ? 10  GLY NNN C   1 
ATOM 19004 O O   . GLY N 3 10  ? 95.480  -45.582 59.702  1.000 55.040  ? 10  GLY NNN O   1 
ATOM 19005 N N   . LEU N 3 11  ? 94.304  -47.531 59.353  1.000 60.660  ? 11  LEU NNN N   1 
ATOM 19006 C CA  . LEU N 3 11  ? 93.369  -47.447 60.500  1.000 57.170  ? 11  LEU NNN CA  1 
ATOM 19007 C C   . LEU N 3 11  ? 93.972  -48.236 61.663  1.000 50.630  ? 11  LEU NNN C   1 
ATOM 19008 O O   . LEU N 3 11  ? 94.407  -49.393 61.447  1.000 42.270  ? 11  LEU NNN O   1 
ATOM 19009 C CB  . LEU N 3 11  ? 92.038  -48.061 60.044  1.000 57.910  ? 11  LEU NNN CB  1 
ATOM 19010 C CG  . LEU N 3 11  ? 90.812  -47.886 60.943  1.000 57.930  ? 11  LEU NNN CG  1 
ATOM 19011 C CD1 . LEU N 3 11  ? 90.676  -49.039 61.930  1.000 67.350  ? 11  LEU NNN CD1 1 
ATOM 19012 C CD2 . LEU N 3 11  ? 90.757  -46.531 61.650  1.000 55.720  ? 11  LEU NNN CD2 1 
ATOM 19013 N N   . VAL N 3 12  ? 94.040  -47.611 62.832  1.000 49.160  ? 12  VAL NNN N   1 
ATOM 19014 C CA  . VAL N 3 12  ? 94.576  -48.211 64.081  1.000 54.300  ? 12  VAL NNN CA  1 
ATOM 19015 C C   . VAL N 3 12  ? 93.784  -47.626 65.247  1.000 61.540  ? 12  VAL NNN C   1 
ATOM 19016 O O   . VAL N 3 12  ? 93.229  -46.537 65.081  1.000 58.480  ? 12  VAL NNN O   1 
ATOM 19017 C CB  . VAL N 3 12  ? 96.085  -47.937 64.227  1.000 53.920  ? 12  VAL NNN CB  1 
ATOM 19018 C CG1 . VAL N 3 12  ? 96.400  -46.446 64.183  1.000 50.650  ? 12  VAL NNN CG1 1 
ATOM 19019 C CG2 . VAL N 3 12  ? 96.673  -48.580 65.478  1.000 52.950  ? 12  VAL NNN CG2 1 
ATOM 19020 N N   . LYS N 3 13  ? 93.650  -48.362 66.354  1.000 66.360  ? 13  LYS NNN N   1 
ATOM 19021 C CA  . LYS N 3 13  ? 92.815  -47.949 67.523  1.000 63.920  ? 13  LYS NNN CA  1 
ATOM 19022 C C   . LYS N 3 13  ? 93.709  -47.138 68.456  1.000 55.850  ? 13  LYS NNN C   1 
ATOM 19023 O O   . LYS N 3 13  ? 94.913  -47.355 68.491  1.000 51.960  ? 13  LYS NNN O   1 
ATOM 19024 C CB  . LYS N 3 13  ? 92.173  -49.174 68.186  1.000 72.530  ? 13  LYS NNN CB  1 
ATOM 19025 C CG  . LYS N 3 13  ? 91.137  -49.923 67.344  1.000 75.420  ? 13  LYS NNN CG  1 
ATOM 19026 C CD  . LYS N 3 13  ? 90.760  -51.312 67.858  1.000 74.840  ? 13  LYS NNN CD  1 
ATOM 19027 C CE  . LYS N 3 13  ? 89.760  -51.313 69.000  1.000 80.740  ? 13  LYS NNN CE  1 
ATOM 19028 N NZ  . LYS N 3 13  ? 88.484  -50.639 68.646  1.000 87.230  ? 13  LYS NNN NZ  1 
ATOM 19029 N N   . PRO N 3 14  ? 93.167  -46.151 69.199  1.000 50.410  ? 14  PRO NNN N   1 
ATOM 19030 C CA  . PRO N 3 14  ? 93.931  -45.442 70.226  1.000 47.380  ? 14  PRO NNN CA  1 
ATOM 19031 C C   . PRO N 3 14  ? 94.779  -46.418 71.041  1.000 48.090  ? 14  PRO NNN C   1 
ATOM 19032 O O   . PRO N 3 14  ? 94.378  -47.564 71.176  1.000 50.860  ? 14  PRO NNN O   1 
ATOM 19033 C CB  . PRO N 3 14  ? 92.851  -44.812 71.114  1.000 45.780  ? 14  PRO NNN CB  1 
ATOM 19034 C CG  . PRO N 3 14  ? 91.707  -44.558 70.163  1.000 49.330  ? 14  PRO NNN CG  1 
ATOM 19035 C CD  . PRO N 3 14  ? 91.784  -45.654 69.104  1.000 53.220  ? 14  PRO NNN CD  1 
ATOM 19036 N N   . GLY N 3 15  ? 95.917  -45.947 71.549  1.000 46.180  ? 15  GLY NNN N   1 
ATOM 19037 C CA  . GLY N 3 15  ? 96.912  -46.791 72.232  1.000 42.210  ? 15  GLY NNN CA  1 
ATOM 19038 C C   . GLY N 3 15  ? 97.663  -47.664 71.245  1.000 39.530  ? 15  GLY NNN C   1 
ATOM 19039 O O   . GLY N 3 15  ? 98.618  -48.301 71.663  1.000 37.540  ? 15  GLY NNN O   1 
ATOM 19040 N N   . GLY N 3 16  ? 97.265  -47.664 69.971  1.000 41.620  ? 16  GLY NNN N   1 
ATOM 19041 C CA  . GLY N 3 16  ? 97.831  -48.536 68.925  1.000 44.440  ? 16  GLY NNN CA  1 
ATOM 19042 C C   . GLY N 3 16  ? 99.230  -48.120 68.514  1.000 49.060  ? 16  GLY NNN C   1 
ATOM 19043 O O   . GLY N 3 16  ? 99.767  -47.150 69.097  1.000 55.550  ? 16  GLY NNN O   1 
ATOM 19044 N N   . SER N 3 17  ? 99.804  -48.833 67.545  1.000 52.620  ? 17  SER NNN N   1 
ATOM 19045 C CA  . SER N 3 17  ? 101.185 -48.628 67.032  1.000 53.180  ? 17  SER NNN CA  1 
ATOM 19046 C C   . SER N 3 17  ? 101.161 -48.754 65.505  1.000 61.710  ? 17  SER NNN C   1 
ATOM 19047 O O   . SER N 3 17  ? 100.170 -49.291 64.975  1.000 82.270  ? 17  SER NNN O   1 
ATOM 19048 C CB  . SER N 3 17  ? 102.136 -49.588 67.686  1.000 45.810  ? 17  SER NNN CB  1 
ATOM 19049 O OG  . SER N 3 17  ? 103.334 -49.706 66.971  1.000 46.800  ? 17  SER NNN OG  1 
ATOM 19050 N N   . LEU N 3 18  ? 102.199 -48.267 64.826  1.000 62.220  ? 18  LEU NNN N   1 
ATOM 19051 C CA  . LEU N 3 18  ? 102.227 -48.125 63.346  1.000 53.970  ? 18  LEU NNN CA  1 
ATOM 19052 C C   . LEU N 3 18  ? 103.624 -47.645 62.893  1.000 52.570  ? 18  LEU NNN C   1 
ATOM 19053 O O   . LEU N 3 18  ? 104.141 -46.714 63.532  1.000 50.420  ? 18  LEU NNN O   1 
ATOM 19054 C CB  . LEU N 3 18  ? 101.150 -47.124 62.958  1.000 48.460  ? 18  LEU NNN CB  1 
ATOM 19055 C CG  . LEU N 3 18  ? 100.663 -47.176 61.521  1.000 51.170  ? 18  LEU NNN CG  1 
ATOM 19056 C CD1 . LEU N 3 18  ? 100.678 -48.595 60.969  1.000 49.170  ? 18  LEU NNN CD1 1 
ATOM 19057 C CD2 . LEU N 3 18  ? 99.274  -46.553 61.433  1.000 52.960  ? 18  LEU NNN CD2 1 
ATOM 19058 N N   . ARG N 3 19  ? 104.190 -48.276 61.859  1.000 48.560  ? 19  ARG NNN N   1 
ATOM 19059 C CA  . ARG N 3 19  ? 105.499 -47.893 61.262  1.000 48.710  ? 19  ARG NNN CA  1 
ATOM 19060 C C   . ARG N 3 19  ? 105.273 -47.375 59.841  1.000 48.640  ? 19  ARG NNN C   1 
ATOM 19061 O O   . ARG N 3 19  ? 104.686 -48.099 59.026  1.000 55.530  ? 19  ARG NNN O   1 
ATOM 19062 C CB  . ARG N 3 19  ? 106.468 -49.079 61.257  1.000 47.370  ? 19  ARG NNN CB  1 
ATOM 19063 C CG  . ARG N 3 19  ? 107.825 -48.813 60.619  1.000 46.260  ? 19  ARG NNN CG  1 
ATOM 19064 C CD  . ARG N 3 19  ? 108.806 -49.848 61.149  1.000 49.190  ? 19  ARG NNN CD  1 
ATOM 19065 N NE  . ARG N 3 19  ? 110.204 -49.665 60.806  1.000 52.640  ? 19  ARG NNN NE  1 
ATOM 19066 C CZ  . ARG N 3 19  ? 110.863 -50.333 59.851  1.000 52.680  ? 19  ARG NNN CZ  1 
ATOM 19067 N NH1 . ARG N 3 19  ? 110.228 -51.210 59.088  1.000 50.560  ? 19  ARG NNN NH1 1 
ATOM 19068 N NH2 . ARG N 3 19  ? 112.150 -50.094 59.637  1.000 51.210  ? 19  ARG NNN NH2 1 
ATOM 19069 N N   . LEU N 3 20  ? 105.706 -46.143 59.580  1.000 47.750  ? 20  LEU NNN N   1 
ATOM 19070 C CA  . LEU N 3 20  ? 105.584 -45.473 58.264  1.000 46.910  ? 20  LEU NNN CA  1 
ATOM 19071 C C   . LEU N 3 20  ? 106.916 -45.636 57.544  1.000 51.130  ? 20  LEU NNN C   1 
ATOM 19072 O O   . LEU N 3 20  ? 107.964 -45.723 58.231  1.000 50.170  ? 20  LEU NNN O   1 
ATOM 19073 C CB  . LEU N 3 20  ? 105.213 -44.003 58.453  1.000 45.610  ? 20  LEU NNN CB  1 
ATOM 19074 C CG  . LEU N 3 20  ? 103.852 -43.755 59.100  1.000 47.830  ? 20  LEU NNN CG  1 
ATOM 19075 C CD1 . LEU N 3 20  ? 103.408 -42.295 58.948  1.000 48.850  ? 20  LEU NNN CD1 1 
ATOM 19076 C CD2 . LEU N 3 20  ? 102.815 -44.718 58.548  1.000 46.860  ? 20  LEU NNN CD2 1 
ATOM 19077 N N   . SER N 3 21  ? 106.843 -45.732 56.213  1.000 50.440  ? 21  SER NNN N   1 
ATOM 19078 C CA  . SER N 3 21  ? 107.993 -45.891 55.297  1.000 51.190  ? 21  SER NNN CA  1 
ATOM 19079 C C   . SER N 3 21  ? 107.989 -44.778 54.251  1.000 50.170  ? 21  SER NNN C   1 
ATOM 19080 O O   . SER N 3 21  ? 106.925 -44.538 53.652  1.000 50.800  ? 21  SER NNN O   1 
ATOM 19081 C CB  . SER N 3 21  ? 107.930 -47.223 54.647  1.000 58.350  ? 21  SER NNN CB  1 
ATOM 19082 O OG  . SER N 3 21  ? 108.492 -48.195 55.497  1.000 69.110  ? 21  SER NNN OG  1 
ATOM 19083 N N   . CYS N 3 22  ? 109.144 -44.142 54.043  1.000 49.010  ? 22  CYS NNN N   1 
ATOM 19084 C CA  . CYS N 3 22  ? 109.413 -43.255 52.882  1.000 48.440  ? 22  CYS NNN CA  1 
ATOM 19085 C C   . CYS N 3 22  ? 110.432 -43.945 51.981  1.000 53.960  ? 22  CYS NNN C   1 
ATOM 19086 O O   . CYS N 3 22  ? 111.505 -44.346 52.492  1.000 53.540  ? 22  CYS NNN O   1 
ATOM 19087 C CB  . CYS N 3 22  ? 109.959 -41.891 53.279  1.000 46.210  ? 22  CYS NNN CB  1 
ATOM 19088 S SG  . CYS N 3 22  ? 109.633 -40.632 52.023  1.000 40.600  ? 22  CYS NNN SG  1 
ATOM 19089 N N   . ALA N 3 23  ? 110.096 -44.115 50.703  1.000 53.660  ? 23  ALA NNN N   1 
ATOM 19090 C CA  . ALA N 3 23  ? 110.980 -44.682 49.668  1.000 50.920  ? 23  ALA NNN CA  1 
ATOM 19091 C C   . ALA N 3 23  ? 111.452 -43.528 48.791  1.000 53.300  ? 23  ALA NNN C   1 
ATOM 19092 O O   . ALA N 3 23  ? 110.607 -42.899 48.114  1.000 48.050  ? 23  ALA NNN O   1 
ATOM 19093 C CB  . ALA N 3 23  ? 110.259 -45.724 48.871  1.000 55.690  ? 23  ALA NNN CB  1 
ATOM 19094 N N   . ALA N 3 24  ? 112.760 -43.269 48.826  1.000 51.270  ? 24  ALA NNN N   1 
ATOM 19095 C CA  . ALA N 3 24  ? 113.434 -42.194 48.067  1.000 49.880  ? 24  ALA NNN CA  1 
ATOM 19096 C C   . ALA N 3 24  ? 114.102 -42.781 46.812  1.000 49.520  ? 24  ALA NNN C   1 
ATOM 19097 O O   . ALA N 3 24  ? 114.959 -43.693 46.936  1.000 40.010  ? 24  ALA NNN O   1 
ATOM 19098 C CB  . ALA N 3 24  ? 114.432 -41.496 48.959  1.000 50.000  ? 24  ALA NNN CB  1 
ATOM 19099 N N   . SER N 3 25  ? 113.772 -42.149 45.681  1.000 51.940  ? 25  SER NNN N   1 
ATOM 19100 C CA  . SER N 3 25  ? 114.340 -42.498 44.363  1.000 53.160  ? 25  SER NNN CA  1 
ATOM 19101 C C   . SER N 3 25  ? 114.599 -41.162 43.668  1.000 52.500  ? 25  SER NNN C   1 
ATOM 19102 O O   . SER N 3 25  ? 113.749 -40.278 43.789  1.000 50.090  ? 25  SER NNN O   1 
ATOM 19103 C CB  . SER N 3 25  ? 113.320 -43.257 43.591  1.000 55.940  ? 25  SER NNN CB  1 
ATOM 19104 O OG  . SER N 3 25  ? 112.031 -42.700 43.790  1.000 55.930  ? 25  SER NNN OG  1 
ATOM 19105 N N   . GLY N 3 26  ? 115.736 -41.009 42.996  1.000 48.880  ? 26  GLY NNN N   1 
ATOM 19106 C CA  . GLY N 3 26  ? 116.003 -39.776 42.237  1.000 44.440  ? 26  GLY NNN CA  1 
ATOM 19107 C C   . GLY N 3 26  ? 117.200 -39.025 42.770  1.000 43.000  ? 26  GLY NNN C   1 
ATOM 19108 O O   . GLY N 3 26  ? 117.677 -38.126 42.069  1.000 48.160  ? 26  GLY NNN O   1 
ATOM 19109 N N   . PHE N 3 27  ? 117.675 -39.394 43.956  1.000 38.340  ? 27  PHE NNN N   1 
ATOM 19110 C CA  . PHE N 3 27  ? 118.781 -38.641 44.590  1.000 39.580  ? 27  PHE NNN CA  1 
ATOM 19111 C C   . PHE N 3 27  ? 119.541 -39.536 45.556  1.000 36.370  ? 27  PHE NNN C   1 
ATOM 19112 O O   . PHE N 3 27  ? 119.008 -40.582 45.943  1.000 39.550  ? 27  PHE NNN O   1 
ATOM 19113 C CB  . PHE N 3 27  ? 118.245 -37.413 45.328  1.000 41.070  ? 27  PHE NNN CB  1 
ATOM 19114 C CG  . PHE N 3 27  ? 117.323 -37.653 46.494  1.000 38.600  ? 27  PHE NNN CG  1 
ATOM 19115 C CD1 . PHE N 3 27  ? 116.000 -38.010 46.298  1.000 40.060  ? 27  PHE NNN CD1 1 
ATOM 19116 C CD2 . PHE N 3 27  ? 117.764 -37.463 47.790  1.000 36.150  ? 27  PHE NNN CD2 1 
ATOM 19117 C CE1 . PHE N 3 27  ? 115.153 -38.209 47.373  1.000 39.410  ? 27  PHE NNN CE1 1 
ATOM 19118 C CE2 . PHE N 3 27  ? 116.917 -37.666 48.864  1.000 38.260  ? 27  PHE NNN CE2 1 
ATOM 19119 C CZ  . PHE N 3 27  ? 115.613 -38.033 48.653  1.000 38.160  ? 27  PHE NNN CZ  1 
ATOM 19120 N N   . THR N 3 28  ? 120.755 -39.127 45.919  1.000 33.940  ? 28  THR NNN N   1 
ATOM 19121 C CA  . THR N 3 28  ? 121.521 -39.889 46.928  1.000 36.840  ? 28  THR NNN CA  1 
ATOM 19122 C C   . THR N 3 28  ? 120.883 -39.612 48.281  1.000 41.400  ? 28  THR NNN C   1 
ATOM 19123 O O   . THR N 3 28  ? 121.270 -38.636 48.902  1.000 71.170  ? 28  THR NNN O   1 
ATOM 19124 C CB  . THR N 3 28  ? 123.006 -39.525 46.892  1.000 34.810  ? 28  THR NNN CB  1 
ATOM 19125 O OG1 . THR N 3 28  ? 123.362 -39.351 45.522  1.000 35.340  ? 28  THR NNN OG1 1 
ATOM 19126 C CG2 . THR N 3 28  ? 123.890 -40.580 47.517  1.000 32.230  ? 28  THR NNN CG2 1 
ATOM 19127 N N   . PHE N 3 29  ? 119.953 -40.452 48.720  1.000 36.520  ? 29  PHE NNN N   1 
ATOM 19128 C CA  . PHE N 3 29  ? 119.228 -40.240 49.997  1.000 37.800  ? 29  PHE NNN CA  1 
ATOM 19129 C C   . PHE N 3 29  ? 120.243 -40.133 51.124  1.000 34.660  ? 29  PHE NNN C   1 
ATOM 19130 O O   . PHE N 3 29  ? 120.019 -39.349 52.040  1.000 33.890  ? 29  PHE NNN O   1 
ATOM 19131 C CB  . PHE N 3 29  ? 118.217 -41.378 50.149  1.000 36.460  ? 29  PHE NNN CB  1 
ATOM 19132 C CG  . PHE N 3 29  ? 117.582 -41.594 51.498  1.000 35.280  ? 29  PHE NNN CG  1 
ATOM 19133 C CD1 . PHE N 3 29  ? 116.446 -40.891 51.869  1.000 33.680  ? 29  PHE NNN CD1 1 
ATOM 19134 C CD2 . PHE N 3 29  ? 118.074 -42.550 52.365  1.000 36.990  ? 29  PHE NNN CD2 1 
ATOM 19135 C CE1 . PHE N 3 29  ? 115.848 -41.115 53.095  1.000 34.450  ? 29  PHE NNN CE1 1 
ATOM 19136 C CE2 . PHE N 3 29  ? 117.479 -42.765 53.594  1.000 38.610  ? 29  PHE NNN CE2 1 
ATOM 19137 C CZ  . PHE N 3 29  ? 116.374 -42.040 53.960  1.000 38.460  ? 29  PHE NNN CZ  1 
ATOM 19138 N N   . SER N 3 30  ? 121.355 -40.837 51.006  1.000 33.280  ? 30  SER NNN N   1 
ATOM 19139 C CA  . SER N 3 30  ? 122.361 -40.878 52.078  1.000 35.010  ? 30  SER NNN CA  1 
ATOM 19140 C C   . SER N 3 30  ? 123.109 -39.563 52.240  1.000 37.940  ? 30  SER NNN C   1 
ATOM 19141 O O   . SER N 3 30  ? 124.052 -39.547 53.038  1.000 47.240  ? 30  SER NNN O   1 
ATOM 19142 C CB  . SER N 3 30  ? 123.340 -41.947 51.754  1.000 37.230  ? 30  SER NNN CB  1 
ATOM 19143 O OG  . SER N 3 30  ? 124.361 -41.456 50.892  1.000 41.010  ? 30  SER NNN OG  1 
ATOM 19144 N N   . SER N 3 31  ? 122.737 -38.510 51.526  1.000 36.050  ? 31  SER NNN N   1 
ATOM 19145 C CA  . SER N 3 31  ? 123.538 -37.264 51.567  1.000 33.740  ? 31  SER NNN CA  1 
ATOM 19146 C C   . SER N 3 31  ? 122.695 -36.130 52.138  1.000 31.870  ? 31  SER NNN C   1 
ATOM 19147 O O   . SER N 3 31  ? 123.235 -35.031 52.283  1.000 29.620  ? 31  SER NNN O   1 
ATOM 19148 C CB  . SER N 3 31  ? 124.025 -36.933 50.194  1.000 33.790  ? 31  SER NNN CB  1 
ATOM 19149 O OG  . SER N 3 31  ? 124.869 -37.957 49.698  1.000 35.260  ? 31  SER NNN OG  1 
ATOM 19150 N N   . TYR N 3 32  ? 121.452 -36.414 52.518  1.000 31.200  ? 32  TYR NNN N   1 
ATOM 19151 C CA  . TYR N 3 32  ? 120.552 -35.316 52.926  1.000 31.570  ? 32  TYR NNN CA  1 
ATOM 19152 C C   . TYR N 3 32  ? 119.763 -35.615 54.200  1.000 30.390  ? 32  TYR NNN C   1 
ATOM 19153 O O   . TYR N 3 32  ? 119.359 -36.761 54.377  1.000 27.970  ? 32  TYR NNN O   1 
ATOM 19154 C CB  . TYR N 3 32  ? 119.516 -35.103 51.824  1.000 31.980  ? 32  TYR NNN CB  1 
ATOM 19155 C CG  . TYR N 3 32  ? 120.030 -34.735 50.454  1.000 28.990  ? 32  TYR NNN CG  1 
ATOM 19156 C CD1 . TYR N 3 32  ? 120.390 -35.709 49.545  1.000 28.510  ? 32  TYR NNN CD1 1 
ATOM 19157 C CD2 . TYR N 3 32  ? 120.093 -33.417 50.044  1.000 30.150  ? 32  TYR NNN CD2 1 
ATOM 19158 C CE1 . TYR N 3 32  ? 120.849 -35.391 48.282  1.000 30.810  ? 32  TYR NNN CE1 1 
ATOM 19159 C CE2 . TYR N 3 32  ? 120.539 -33.079 48.779  1.000 32.410  ? 32  TYR NNN CE2 1 
ATOM 19160 C CZ  . TYR N 3 32  ? 120.921 -34.070 47.897  1.000 32.440  ? 32  TYR NNN CZ  1 
ATOM 19161 O OH  . TYR N 3 32  ? 121.356 -33.763 46.645  1.000 34.310  ? 32  TYR NNN OH  1 
ATOM 19162 N N   . THR N 3 33  ? 119.579 -34.614 55.064  1.000 30.120  ? 33  THR NNN N   1 
ATOM 19163 C CA  . THR N 3 33  ? 118.691 -34.726 56.242  1.000 29.870  ? 33  THR NNN CA  1 
ATOM 19164 C C   . THR N 3 33  ? 117.255 -34.820 55.720  1.000 29.480  ? 33  THR NNN C   1 
ATOM 19165 O O   . THR N 3 33  ? 116.935 -34.240 54.662  1.000 27.360  ? 33  THR NNN O   1 
ATOM 19166 C CB  . THR N 3 33  ? 119.022 -33.682 57.300  1.000 32.710  ? 33  THR NNN CB  1 
ATOM 19167 O OG1 . THR N 3 33  ? 118.277 -32.538 56.919  1.000 35.910  ? 33  THR NNN OG1 1 
ATOM 19168 C CG2 . THR N 3 33  ? 120.515 -33.410 57.389  1.000 36.040  ? 33  THR NNN CG2 1 
ATOM 19169 N N   . MET N 3 34  ? 116.433 -35.612 56.403  1.000 31.320  ? 34  MET NNN N   1 
ATOM 19170 C CA  . MET N 3 34  ? 115.059 -35.968 55.963  1.000 30.110  ? 34  MET NNN CA  1 
ATOM 19171 C C   . MET N 3 34  ? 114.086 -35.681 57.098  1.000 26.030  ? 34  MET NNN C   1 
ATOM 19172 O O   . MET N 3 34  ? 114.492 -35.769 58.254  1.000 26.650  ? 34  MET NNN O   1 
ATOM 19173 C CB  . MET N 3 34  ? 114.990 -37.444 55.561  1.000 32.190  ? 34  MET NNN CB  1 
ATOM 19174 C CG  . MET N 3 34  ? 115.780 -37.764 54.288  1.000 35.300  ? 34  MET NNN CG  1 
ATOM 19175 S SD  . MET N 3 34  ? 115.128 -37.011 52.759  1.000 39.440  ? 34  MET NNN SD  1 
ATOM 19176 C CE  . MET N 3 34  ? 113.412 -37.569 52.825  1.000 40.370  ? 34  MET NNN CE  1 
ATOM 19177 N N   . ASN N 3 35  ? 112.848 -35.354 56.753  1.000 25.740  ? 35  ASN NNN N   1 
ATOM 19178 C CA  . ASN N 3 35  ? 111.820 -34.843 57.692  1.000 27.340  ? 35  ASN NNN CA  1 
ATOM 19179 C C   . ASN N 3 35  ? 110.517 -35.638 57.550  1.000 26.620  ? 35  ASN NNN C   1 
ATOM 19180 O O   . ASN N 3 35  ? 110.250 -36.189 56.461  1.000 29.910  ? 35  ASN NNN O   1 
ATOM 19181 C CB  . ASN N 3 35  ? 111.588 -33.347 57.462  1.000 29.380  ? 35  ASN NNN CB  1 
ATOM 19182 C CG  . ASN N 3 35  ? 112.713 -32.492 58.002  1.000 31.110  ? 35  ASN NNN CG  1 
ATOM 19183 O OD1 . ASN N 3 35  ? 112.699 -32.110 59.173  1.000 33.670  ? 35  ASN NNN OD1 1 
ATOM 19184 N ND2 . ASN N 3 35  ? 113.693 -32.200 57.159  1.000 29.670  ? 35  ASN NNN ND2 1 
ATOM 19185 N N   . TRP N 3 36  ? 109.747 -35.708 58.632  1.000 26.190  ? 36  TRP NNN N   1 
ATOM 19186 C CA  . TRP N 3 36  ? 108.305 -36.065 58.643  1.000 26.780  ? 36  TRP NNN CA  1 
ATOM 19187 C C   . TRP N 3 36  ? 107.532 -34.809 59.027  1.000 26.940  ? 36  TRP NNN C   1 
ATOM 19188 O O   . TRP N 3 36  ? 107.889 -34.201 60.029  1.000 30.200  ? 36  TRP NNN O   1 
ATOM 19189 C CB  . TRP N 3 36  ? 107.998 -37.226 59.606  1.000 26.000  ? 36  TRP NNN CB  1 
ATOM 19190 C CG  . TRP N 3 36  ? 108.543 -38.549 59.170  1.000 25.440  ? 36  TRP NNN CG  1 
ATOM 19191 C CD1 . TRP N 3 36  ? 109.684 -39.153 59.606  1.000 25.440  ? 36  TRP NNN CD1 1 
ATOM 19192 C CD2 . TRP N 3 36  ? 107.985 -39.427 58.186  1.000 25.410  ? 36  TRP NNN CD2 1 
ATOM 19193 N NE1 . TRP N 3 36  ? 109.870 -40.345 58.968  1.000 25.740  ? 36  TRP NNN NE1 1 
ATOM 19194 C CE2 . TRP N 3 36  ? 108.847 -40.539 58.085  1.000 25.300  ? 36  TRP NNN CE2 1 
ATOM 19195 C CE3 . TRP N 3 36  ? 106.838 -39.386 57.391  1.000 27.310  ? 36  TRP NNN CE3 1 
ATOM 19196 C CZ2 . TRP N 3 36  ? 108.603 -41.596 57.217  1.000 24.480  ? 36  TRP NNN CZ2 1 
ATOM 19197 C CZ3 . TRP N 3 36  ? 106.591 -40.435 56.531  1.000 28.230  ? 36  TRP NNN CZ3 1 
ATOM 19198 C CH2 . TRP N 3 36  ? 107.469 -41.520 56.447  1.000 26.090  ? 36  TRP NNN CH2 1 
ATOM 19199 N N   . VAL N 3 37  ? 106.514 -34.450 58.256  1.000 29.150  ? 37  VAL NNN N   1 
ATOM 19200 C CA  . VAL N 3 37  ? 105.552 -33.354 58.569  1.000 33.170  ? 37  VAL NNN CA  1 
ATOM 19201 C C   . VAL N 3 37  ? 104.149 -33.935 58.426  1.000 35.560  ? 37  VAL NNN C   1 
ATOM 19202 O O   . VAL N 3 37  ? 103.954 -34.716 57.500  1.000 37.610  ? 37  VAL NNN O   1 
ATOM 19203 C CB  . VAL N 3 37  ? 105.767 -32.153 57.629  1.000 36.710  ? 37  VAL NNN CB  1 
ATOM 19204 C CG1 . VAL N 3 37  ? 104.781 -31.035 57.896  1.000 38.820  ? 37  VAL NNN CG1 1 
ATOM 19205 C CG2 . VAL N 3 37  ? 107.183 -31.613 57.701  1.000 39.010  ? 37  VAL NNN CG2 1 
ATOM 19206 N N   . ARG N 3 38  ? 103.205 -33.577 59.288  1.000 40.580  ? 38  ARG NNN N   1 
ATOM 19207 C CA  . ARG N 3 38  ? 101.824 -34.121 59.213  1.000 45.100  ? 38  ARG NNN CA  1 
ATOM 19208 C C   . ARG N 3 38  ? 100.813 -32.988 59.084  1.000 42.860  ? 38  ARG NNN C   1 
ATOM 19209 O O   . ARG N 3 38  ? 101.144 -31.851 59.462  1.000 44.510  ? 38  ARG NNN O   1 
ATOM 19210 C CB  . ARG N 3 38  ? 101.492 -34.967 60.445  1.000 53.350  ? 38  ARG NNN CB  1 
ATOM 19211 C CG  . ARG N 3 38  ? 101.367 -34.176 61.736  1.000 57.280  ? 38  ARG NNN CG  1 
ATOM 19212 C CD  . ARG N 3 38  ? 101.004 -35.094 62.881  1.000 55.660  ? 38  ARG NNN CD  1 
ATOM 19213 N NE  . ARG N 3 38  ? 101.176 -34.428 64.146  1.000 52.580  ? 38  ARG NNN NE  1 
ATOM 19214 C CZ  . ARG N 3 38  ? 100.961 -34.989 65.315  1.000 55.740  ? 38  ARG NNN CZ  1 
ATOM 19215 N NH1 . ARG N 3 38  ? 100.557 -36.245 65.382  1.000 52.410  ? 38  ARG NNN NH1 1 
ATOM 19216 N NH2 . ARG N 3 38  ? 101.178 -34.299 66.423  1.000 64.420  ? 38  ARG NNN NH2 1 
ATOM 19217 N N   . GLN N 3 39  ? 99.613  -33.322 58.611  1.000 41.920  ? 39  GLN NNN N   1 
ATOM 19218 C CA  . GLN N 3 39  ? 98.507  -32.364 58.356  1.000 41.810  ? 39  GLN NNN CA  1 
ATOM 19219 C C   . GLN N 3 39  ? 97.172  -32.972 58.795  1.000 40.890  ? 39  GLN NNN C   1 
ATOM 19220 O O   . GLN N 3 39  ? 96.632  -33.842 58.079  1.000 39.650  ? 39  GLN NNN O   1 
ATOM 19221 C CB  . GLN N 3 39  ? 98.456  -32.026 56.868  1.000 44.520  ? 39  GLN NNN CB  1 
ATOM 19222 C CG  . GLN N 3 39  ? 97.646  -30.777 56.577  1.000 41.410  ? 39  GLN NNN CG  1 
ATOM 19223 C CD  . GLN N 3 39  ? 97.816  -30.314 55.157  1.000 36.990  ? 39  GLN NNN CD  1 
ATOM 19224 O OE1 . GLN N 3 39  ? 98.112  -31.110 54.250  1.000 30.340  ? 39  GLN NNN OE1 1 
ATOM 19225 N NE2 . GLN N 3 39  ? 97.633  -29.011 54.992  1.000 36.940  ? 39  GLN NNN NE2 1 
ATOM 19226 N N   . ALA N 3 40  ? 96.661  -32.531 59.936  1.000 43.360  ? 40  ALA NNN N   1 
ATOM 19227 C CA  . ALA N 3 40  ? 95.381  -32.994 60.511  1.000 50.650  ? 40  ALA NNN CA  1 
ATOM 19228 C C   . ALA N 3 40  ? 94.257  -32.436 59.645  1.000 61.650  ? 40  ALA NNN C   1 
ATOM 19229 O O   . ALA N 3 40  ? 94.375  -31.313 59.145  1.000 56.500  ? 40  ALA NNN O   1 
ATOM 19230 C CB  . ALA N 3 40  ? 95.263  -32.540 61.948  1.000 54.450  ? 40  ALA NNN CB  1 
ATOM 19231 N N   . PRO N 3 41  ? 93.150  -33.189 59.428  1.000 79.340  ? 41  PRO NNN N   1 
ATOM 19232 C CA  . PRO N 3 41  ? 92.223  -32.855 58.347  1.000 79.620  ? 41  PRO NNN CA  1 
ATOM 19233 C C   . PRO N 3 41  ? 91.712  -31.425 58.572  1.000 74.890  ? 41  PRO NNN C   1 
ATOM 19234 O O   . PRO N 3 41  ? 91.259  -31.160 59.676  1.000 77.640  ? 41  PRO NNN O   1 
ATOM 19235 C CB  . PRO N 3 41  ? 91.119  -33.923 58.441  1.000 79.610  ? 41  PRO NNN CB  1 
ATOM 19236 C CG  . PRO N 3 41  ? 91.718  -35.044 59.294  1.000 77.700  ? 41  PRO NNN CG  1 
ATOM 19237 C CD  . PRO N 3 41  ? 92.726  -34.368 60.208  1.000 80.190  ? 41  PRO NNN CD  1 
ATOM 19238 N N   . GLY N 3 42  ? 91.881  -30.540 57.576  1.000 64.880  ? 42  GLY NNN N   1 
ATOM 19239 C CA  . GLY N 3 42  ? 91.325  -29.172 57.566  1.000 60.600  ? 42  GLY NNN CA  1 
ATOM 19240 C C   . GLY N 3 42  ? 92.184  -28.161 58.313  1.000 58.950  ? 42  GLY NNN C   1 
ATOM 19241 O O   . GLY N 3 42  ? 91.950  -26.953 58.115  1.000 52.690  ? 42  GLY NNN O   1 
ATOM 19242 N N   . LYS N 3 43  ? 93.143  -28.623 59.136  1.000 59.120  ? 43  LYS NNN N   1 
ATOM 19243 C CA  . LYS N 3 43  ? 94.143  -27.763 59.843  1.000 54.640  ? 43  LYS NNN CA  1 
ATOM 19244 C C   . LYS N 3 43  ? 95.406  -27.607 58.953  1.000 50.900  ? 43  LYS NNN C   1 
ATOM 19245 O O   . LYS N 3 43  ? 95.437  -28.158 57.800  1.000 49.380  ? 43  LYS NNN O   1 
ATOM 19246 C CB  . LYS N 3 43  ? 94.373  -28.317 61.258  1.000 45.260  ? 43  LYS NNN CB  1 
ATOM 19247 N N   . GLY N 3 44  ? 96.406  -26.852 59.424  1.000 46.020  ? 44  GLY NNN N   1 
ATOM 19248 C CA  . GLY N 3 44  ? 97.627  -26.535 58.657  1.000 46.530  ? 44  GLY NNN CA  1 
ATOM 19249 C C   . GLY N 3 44  ? 98.658  -27.645 58.753  1.000 45.490  ? 44  GLY NNN C   1 
ATOM 19250 O O   . GLY N 3 44  ? 98.290  -28.774 59.136  1.000 47.960  ? 44  GLY NNN O   1 
ATOM 19251 N N   . LEU N 3 45  ? 99.919  -27.347 58.435  1.000 43.940  ? 45  LEU NNN N   1 
ATOM 19252 C CA  . LEU N 3 45  ? 101.038 -28.321 58.531  1.000 42.610  ? 45  LEU NNN CA  1 
ATOM 19253 C C   . LEU N 3 45  ? 101.630 -28.293 59.936  1.000 43.770  ? 45  LEU NNN C   1 
ATOM 19254 O O   . LEU N 3 45  ? 101.467 -27.267 60.606  1.000 51.720  ? 45  LEU NNN O   1 
ATOM 19255 C CB  . LEU N 3 45  ? 102.084 -27.982 57.471  1.000 39.160  ? 45  LEU NNN CB  1 
ATOM 19256 C CG  . LEU N 3 45  ? 101.627 -28.304 56.049  1.000 39.720  ? 45  LEU NNN CG  1 
ATOM 19257 C CD1 . LEU N 3 45  ? 102.604 -27.823 55.002  1.000 40.560  ? 45  LEU NNN CD1 1 
ATOM 19258 C CD2 . LEU N 3 45  ? 101.374 -29.788 55.893  1.000 39.980  ? 45  LEU NNN CD2 1 
ATOM 19259 N N   . GLN N 3 46  ? 102.246 -29.395 60.362  1.000 39.080  ? 46  GLN NNN N   1 
ATOM 19260 C CA  . GLN N 3 46  ? 102.944 -29.496 61.671  1.000 35.940  ? 46  GLN NNN CA  1 
ATOM 19261 C C   . GLN N 3 46  ? 104.108 -30.469 61.531  1.000 36.820  ? 46  GLN NNN C   1 
ATOM 19262 O O   . GLN N 3 46  ? 103.858 -31.665 61.256  1.000 37.280  ? 46  GLN NNN O   1 
ATOM 19263 C CB  . GLN N 3 46  ? 101.995 -29.934 62.778  1.000 33.260  ? 46  GLN NNN CB  1 
ATOM 19264 C CG  . GLN N 3 46  ? 102.654 -30.113 64.133  1.000 31.380  ? 46  GLN NNN CG  1 
ATOM 19265 C CD  . GLN N 3 46  ? 101.758 -30.794 65.140  1.000 31.230  ? 46  GLN NNN CD  1 
ATOM 19266 O OE1 . GLN N 3 46  ? 101.089 -31.791 64.869  1.000 29.320  ? 46  GLN NNN OE1 1 
ATOM 19267 N NE2 . GLN N 3 46  ? 101.783 -30.301 66.362  1.000 33.400  ? 46  GLN NNN NE2 1 
ATOM 19268 N N   . TRP N 3 47  ? 105.333 -29.956 61.693  1.000 33.450  ? 47  TRP NNN N   1 
ATOM 19269 C CA  . TRP N 3 47  ? 106.577 -30.758 61.614  1.000 29.270  ? 47  TRP NNN CA  1 
ATOM 19270 C C   . TRP N 3 47  ? 106.566 -31.792 62.736  1.000 28.590  ? 47  TRP NNN C   1 
ATOM 19271 O O   . TRP N 3 47  ? 106.139 -31.449 63.857  1.000 30.900  ? 47  TRP NNN O   1 
ATOM 19272 C CB  . TRP N 3 47  ? 107.798 -29.855 61.709  1.000 30.110  ? 47  TRP NNN CB  1 
ATOM 19273 C CG  . TRP N 3 47  ? 109.085 -30.609 61.849  1.000 31.750  ? 47  TRP NNN CG  1 
ATOM 19274 C CD1 . TRP N 3 47  ? 109.764 -31.298 60.880  1.000 31.550  ? 47  TRP NNN CD1 1 
ATOM 19275 C CD2 . TRP N 3 47  ? 109.845 -30.744 63.050  1.000 30.230  ? 47  TRP NNN CD2 1 
ATOM 19276 N NE1 . TRP N 3 47  ? 110.901 -31.852 61.398  1.000 30.150  ? 47  TRP NNN NE1 1 
ATOM 19277 C CE2 . TRP N 3 47  ? 110.988 -31.525 62.724  1.000 30.560  ? 47  TRP NNN CE2 1 
ATOM 19278 C CE3 . TRP N 3 47  ? 109.693 -30.268 64.353  1.000 29.300  ? 47  TRP NNN CE3 1 
ATOM 19279 C CZ2 . TRP N 3 47  ? 111.959 -31.834 63.660  1.000 31.840  ? 47  TRP NNN CZ2 1 
ATOM 19280 C CZ3 . TRP N 3 47  ? 110.654 -30.587 65.283  1.000 31.980  ? 47  TRP NNN CZ3 1 
ATOM 19281 C CH2 . TRP N 3 47  ? 111.777 -31.349 64.939  1.000 34.060  ? 47  TRP NNN CH2 1 
ATOM 19282 N N   . VAL N 3 48  ? 107.011 -33.004 62.437  1.000 27.440  ? 48  VAL NNN N   1 
ATOM 19283 C CA  . VAL N 3 48  ? 106.978 -34.164 63.362  1.000 27.660  ? 48  VAL NNN CA  1 
ATOM 19284 C C   . VAL N 3 48  ? 108.399 -34.436 63.825  1.000 28.080  ? 48  VAL NNN C   1 
ATOM 19285 O O   . VAL N 3 48  ? 108.616 -34.460 65.038  1.000 30.140  ? 48  VAL NNN O   1 
ATOM 19286 C CB  . VAL N 3 48  ? 106.383 -35.397 62.673  1.000 29.820  ? 48  VAL NNN CB  1 
ATOM 19287 C CG1 . VAL N 3 48  ? 106.705 -36.675 63.423  1.000 31.460  ? 48  VAL NNN CG1 1 
ATOM 19288 C CG2 . VAL N 3 48  ? 104.876 -35.237 62.499  1.000 30.380  ? 48  VAL NNN CG2 1 
ATOM 19289 N N   . SER N 3 49  ? 109.327 -34.684 62.900  1.000 29.700  ? 49  SER NNN N   1 
ATOM 19290 C CA  . SER N 3 49  ? 110.686 -35.143 63.228  1.000 30.400  ? 49  SER NNN CA  1 
ATOM 19291 C C   . SER N 3 49  ? 111.688 -34.933 62.069  1.000 28.590  ? 49  SER NNN C   1 
ATOM 19292 O O   . SER N 3 49  ? 111.282 -35.026 60.907  1.000 32.260  ? 49  SER NNN O   1 
ATOM 19293 C CB  . SER N 3 49  ? 110.634 -36.578 63.694  1.000 31.020  ? 49  SER NNN CB  1 
ATOM 19294 O OG  . SER N 3 49  ? 111.917 -37.007 64.117  1.000 37.390  ? 49  SER NNN OG  1 
ATOM 19295 N N   . SER N 3 50  ? 112.939 -34.648 62.406  1.000 26.400  ? 50  SER NNN N   1 
ATOM 19296 C CA  . SER N 3 50  ? 114.101 -34.551 61.496  1.000 26.950  ? 50  SER NNN CA  1 
ATOM 19297 C C   . SER N 3 50  ? 115.148 -35.615 61.830  1.000 29.310  ? 50  SER NNN C   1 
ATOM 19298 O O   . SER N 3 50  ? 115.306 -35.958 63.013  1.000 33.890  ? 50  SER NNN O   1 
ATOM 19299 C CB  . SER N 3 50  ? 114.762 -33.205 61.617  1.000 28.150  ? 50  SER NNN CB  1 
ATOM 19300 O OG  . SER N 3 50  ? 115.888 -33.145 60.750  1.000 30.360  ? 50  SER NNN OG  1 
ATOM 19301 N N   . ILE N 3 51  ? 115.889 -36.066 60.832  1.000 29.330  ? 51  ILE NNN N   1 
ATOM 19302 C CA  . ILE N 3 51  ? 117.056 -36.962 61.029  1.000 30.320  ? 51  ILE NNN CA  1 
ATOM 19303 C C   . ILE N 3 51  ? 118.150 -36.554 60.045  1.000 28.030  ? 51  ILE NNN C   1 
ATOM 19304 O O   . ILE N 3 51  ? 117.832 -36.391 58.874  1.000 26.090  ? 51  ILE NNN O   1 
ATOM 19305 C CB  . ILE N 3 51  ? 116.683 -38.451 60.894  1.000 33.320  ? 51  ILE NNN CB  1 
ATOM 19306 C CG1 . ILE N 3 51  ? 117.872 -39.352 61.232  1.000 36.650  ? 51  ILE NNN CG1 1 
ATOM 19307 C CG2 . ILE N 3 51  ? 116.128 -38.760 59.510  1.000 32.820  ? 51  ILE NNN CG2 1 
ATOM 19308 C CD1 . ILE N 3 51  ? 117.514 -40.797 61.413  1.000 39.220  ? 51  ILE NNN CD1 1 
ATOM 19309 N N   . SER N 3 52  ? 119.382 -36.426 60.526  1.000 28.930  ? 52  SER NNN N   1 
ATOM 19310 C CA  . SER N 3 52  ? 120.582 -36.074 59.724  1.000 32.010  ? 52  SER NNN CA  1 
ATOM 19311 C C   . SER N 3 52  ? 120.911 -37.201 58.739  1.000 32.540  ? 52  SER NNN C   1 
ATOM 19312 O O   . SER N 3 52  ? 120.336 -38.306 58.877  1.000 27.530  ? 52  SER NNN O   1 
ATOM 19313 C CB  . SER N 3 52  ? 121.779 -35.699 60.606  1.000 34.930  ? 52  SER NNN CB  1 
ATOM 19314 O OG  . SER N 3 52  ? 122.413 -36.811 61.242  1.000 34.710  ? 52  SER NNN OG  1 
ATOM 19315 N N   . SER N 3 53  ? 121.775 -36.916 57.757  1.000 35.330  ? 53  SER NNN N   1 
ATOM 19316 C CA  . SER N 3 53  ? 122.197 -37.890 56.714  1.000 36.630  ? 53  SER NNN CA  1 
ATOM 19317 C C   . SER N 3 53  ? 122.687 -39.193 57.370  1.000 33.890  ? 53  SER NNN C   1 
ATOM 19318 O O   . SER N 3 53  ? 122.331 -40.270 56.884  1.000 31.560  ? 53  SER NNN O   1 
ATOM 19319 C CB  . SER N 3 53  ? 123.238 -37.275 55.792  1.000 39.740  ? 53  SER NNN CB  1 
ATOM 19320 O OG  . SER N 3 53  ? 124.507 -37.197 56.411  1.000 43.890  ? 53  SER NNN OG  1 
ATOM 19321 N N   . SER N 3 54  ? 123.462 -39.088 58.449  1.000 31.480  ? 54  SER NNN N   1 
ATOM 19322 C CA  . SER N 3 54  ? 124.171 -40.216 59.093  1.000 32.850  ? 54  SER NNN CA  1 
ATOM 19323 C C   . SER N 3 54  ? 123.471 -40.644 60.381  1.000 33.210  ? 54  SER NNN C   1 
ATOM 19324 O O   . SER N 3 54  ? 124.044 -41.427 61.162  1.000 32.140  ? 54  SER NNN O   1 
ATOM 19325 C CB  . SER N 3 54  ? 125.585 -39.819 59.365  1.000 33.350  ? 54  SER NNN CB  1 
ATOM 19326 O OG  . SER N 3 54  ? 126.422 -40.211 58.314  1.000 38.120  ? 54  SER NNN OG  1 
ATOM 19327 N N   . SER N 3 55  ? 122.286 -40.101 60.627  1.000 35.500  ? 55  SER NNN N   1 
ATOM 19328 C CA  . SER N 3 55  ? 121.460 -40.423 61.813  1.000 34.080  ? 55  SER NNN CA  1 
ATOM 19329 C C   . SER N 3 55  ? 122.239 -39.962 63.052  1.000 34.810  ? 55  SER NNN C   1 
ATOM 19330 O O   . SER N 3 55  ? 121.944 -40.479 64.131  1.000 39.290  ? 55  SER NNN O   1 
ATOM 19331 C CB  . SER N 3 55  ? 121.092 -41.884 61.775  1.000 31.400  ? 55  SER NNN CB  1 
ATOM 19332 O OG  . SER N 3 55  ? 120.950 -42.336 60.431  1.000 28.790  ? 55  SER NNN OG  1 
ATOM 19333 N N   . THR N 3 56  ? 123.167 -38.990 62.916  1.000 32.870  ? 56  THR NNN N   1 
ATOM 19334 C CA  . THR N 3 56  ? 123.823 -38.318 64.057  1.000 31.670  ? 56  THR NNN CA  1 
ATOM 19335 C C   . THR N 3 56  ? 122.836 -37.442 64.830  1.000 34.970  ? 56  THR NNN C   1 
ATOM 19336 O O   . THR N 3 56  ? 122.977 -37.389 66.050  1.000 46.940  ? 56  THR NNN O   1 
ATOM 19337 C CB  . THR N 3 56  ? 124.989 -37.416 63.676  1.000 27.450  ? 56  THR NNN CB  1 
ATOM 19338 O OG1 . THR N 3 56  ? 125.912 -38.271 63.032  1.000 28.050  ? 56  THR NNN OG1 1 
ATOM 19339 N N   . TYR N 3 57  ? 121.921 -36.732 64.169  1.000 32.950  ? 57  TYR NNN N   1 
ATOM 19340 C CA  . TYR N 3 57  ? 121.016 -35.777 64.867  1.000 32.710  ? 57  TYR NNN CA  1 
ATOM 19341 C C   . TYR N 3 57  ? 119.549 -36.027 64.500  1.000 33.950  ? 57  TYR NNN C   1 
ATOM 19342 O O   . TYR N 3 57  ? 119.113 -35.750 63.346  1.000 36.890  ? 57  TYR NNN O   1 
ATOM 19343 C CB  . TYR N 3 57  ? 121.483 -34.357 64.529  1.000 29.740  ? 57  TYR NNN CB  1 
ATOM 19344 C CG  . TYR N 3 57  ? 122.877 -34.019 64.999  1.000 30.040  ? 57  TYR NNN CG  1 
ATOM 19345 C CD1 . TYR N 3 57  ? 123.969 -34.435 64.266  1.000 32.820  ? 57  TYR NNN CD1 1 
ATOM 19346 C CD2 . TYR N 3 57  ? 123.128 -33.302 66.164  1.000 30.960  ? 57  TYR NNN CD2 1 
ATOM 19347 C CE1 . TYR N 3 57  ? 125.272 -34.142 64.666  1.000 32.080  ? 57  TYR NNN CE1 1 
ATOM 19348 C CE2 . TYR N 3 57  ? 124.422 -33.058 66.609  1.000 29.240  ? 57  TYR NNN CE2 1 
ATOM 19349 C CZ  . TYR N 3 57  ? 125.500 -33.471 65.848  1.000 29.710  ? 57  TYR NNN CZ  1 
ATOM 19350 O OH  . TYR N 3 57  ? 126.795 -33.221 66.187  1.000 29.250  ? 57  TYR NNN OH  1 
ATOM 19351 N N   . MET N 3 58  ? 118.799 -36.547 65.470  1.000 31.790  ? 58  MET NNN N   1 
ATOM 19352 C CA  . MET N 3 58  ? 117.328 -36.692 65.375  1.000 29.460  ? 58  MET NNN CA  1 
ATOM 19353 C C   . MET N 3 58  ? 116.706 -35.612 66.254  1.000 26.810  ? 58  MET NNN C   1 
ATOM 19354 O O   . MET N 3 58  ? 117.237 -35.354 67.321  1.000 25.240  ? 58  MET NNN O   1 
ATOM 19355 C CB  . MET N 3 58  ? 116.873 -38.085 65.833  1.000 29.980  ? 58  MET NNN CB  1 
ATOM 19356 C CG  . MET N 3 58  ? 117.210 -39.194 64.850  1.000 29.200  ? 58  MET NNN CG  1 
ATOM 19357 S SD  . MET N 3 58  ? 119.011 -39.588 64.748  1.000 32.010  ? 58  MET NNN SD  1 
ATOM 19358 C CE  . MET N 3 58  ? 119.450 -40.091 66.412  1.000 29.680  ? 58  MET NNN CE  1 
ATOM 19359 N N   . TYR N 3 59  ? 115.666 -34.949 65.767  1.000 27.670  ? 59  TYR NNN N   1 
ATOM 19360 C CA  . TYR N 3 59  ? 114.882 -33.921 66.497  1.000 29.530  ? 59  TYR NNN CA  1 
ATOM 19361 C C   . TYR N 3 59  ? 113.400 -34.280 66.355  1.000 28.600  ? 59  TYR NNN C   1 
ATOM 19362 O O   . TYR N 3 59  ? 112.998 -34.818 65.294  1.000 28.820  ? 59  TYR NNN O   1 
ATOM 19363 C CB  . TYR N 3 59  ? 115.106 -32.524 65.916  1.000 31.090  ? 59  TYR NNN CB  1 
ATOM 19364 C CG  . TYR N 3 59  ? 116.528 -32.052 65.953  1.000 33.060  ? 59  TYR NNN CG  1 
ATOM 19365 C CD1 . TYR N 3 59  ? 117.072 -31.546 67.114  1.000 37.070  ? 59  TYR NNN CD1 1 
ATOM 19366 C CD2 . TYR N 3 59  ? 117.327 -32.098 64.829  1.000 38.270  ? 59  TYR NNN CD2 1 
ATOM 19367 C CE1 . TYR N 3 59  ? 118.388 -31.112 67.173  1.000 41.570  ? 59  TYR NNN CE1 1 
ATOM 19368 C CE2 . TYR N 3 59  ? 118.646 -31.674 64.869  1.000 41.950  ? 59  TYR NNN CE2 1 
ATOM 19369 C CZ  . TYR N 3 59  ? 119.185 -31.188 66.044  1.000 41.160  ? 59  TYR NNN CZ  1 
ATOM 19370 O OH  . TYR N 3 59  ? 120.482 -30.768 66.075  1.000 37.610  ? 59  TYR NNN OH  1 
ATOM 19371 N N   . TYR N 3 60  ? 112.601 -33.978 67.372  1.000 25.560  ? 60  TYR NNN N   1 
ATOM 19372 C CA  . TYR N 3 60  ? 111.146 -34.251 67.361  1.000 24.910  ? 60  TYR NNN CA  1 
ATOM 19373 C C   . TYR N 3 60  ? 110.407 -32.999 67.811  1.000 26.320  ? 60  TYR NNN C   1 
ATOM 19374 O O   . TYR N 3 60  ? 110.911 -32.292 68.690  1.000 28.170  ? 60  TYR NNN O   1 
ATOM 19375 C CB  . TYR N 3 60  ? 110.802 -35.445 68.253  1.000 22.870  ? 60  TYR NNN CB  1 
ATOM 19376 C CG  . TYR N 3 60  ? 111.572 -36.696 67.932  1.000 22.150  ? 60  TYR NNN CG  1 
ATOM 19377 C CD1 . TYR N 3 60  ? 112.845 -36.884 68.430  1.000 22.300  ? 60  TYR NNN CD1 1 
ATOM 19378 C CD2 . TYR N 3 60  ? 111.029 -37.694 67.141  1.000 21.780  ? 60  TYR NNN CD2 1 
ATOM 19379 C CE1 . TYR N 3 60  ? 113.575 -38.024 68.144  1.000 23.600  ? 60  TYR NNN CE1 1 
ATOM 19380 C CE2 . TYR N 3 60  ? 111.733 -38.848 66.867  1.000 22.030  ? 60  TYR NNN CE2 1 
ATOM 19381 C CZ  . TYR N 3 60  ? 113.010 -39.020 67.379  1.000 23.090  ? 60  TYR NNN CZ  1 
ATOM 19382 O OH  . TYR N 3 60  ? 113.776 -40.126 67.128  1.000 23.630  ? 60  TYR NNN OH  1 
ATOM 19383 N N   . GLY N 3 61  ? 109.253 -32.753 67.200  1.000 27.520  ? 61  GLY NNN N   1 
ATOM 19384 C CA  . GLY N 3 61  ? 108.218 -31.854 67.722  1.000 30.810  ? 61  GLY NNN CA  1 
ATOM 19385 C C   . GLY N 3 61  ? 107.801 -32.295 69.112  1.000 32.590  ? 61  GLY NNN C   1 
ATOM 19386 O O   . GLY N 3 61  ? 107.886 -33.503 69.398  1.000 33.790  ? 61  GLY NNN O   1 
ATOM 19387 N N   . ASP N 3 62  ? 107.397 -31.342 69.957  1.000 32.800  ? 62  ASP NNN N   1 
ATOM 19388 C CA  . ASP N 3 62  ? 106.977 -31.622 71.345  1.000 32.720  ? 62  ASP NNN CA  1 
ATOM 19389 C C   . ASP N 3 62  ? 105.758 -32.539 71.297  1.000 31.740  ? 62  ASP NNN C   1 
ATOM 19390 O O   . ASP N 3 62  ? 105.735 -33.492 72.063  1.000 34.870  ? 62  ASP NNN O   1 
ATOM 19391 C CB  . ASP N 3 62  ? 106.747 -30.323 72.112  1.000 36.340  ? 62  ASP NNN CB  1 
ATOM 19392 C CG  . ASP N 3 62  ? 108.033 -29.715 72.659  1.000 40.920  ? 62  ASP NNN CG  1 
ATOM 19393 O OD1 . ASP N 3 62  ? 109.037 -30.445 72.785  1.000 44.300  ? 62  ASP NNN OD1 1 
ATOM 19394 O OD2 . ASP N 3 62  ? 108.035 -28.513 72.943  1.000 42.580  ? 62  ASP NNN OD2 1 
ATOM 19395 N N   . SER N 3 63  ? 104.806 -32.311 70.402  1.000 32.450  ? 63  SER NNN N   1 
ATOM 19396 C CA  . SER N 3 63  ? 103.508 -33.040 70.393  1.000 34.340  ? 63  SER NNN CA  1 
ATOM 19397 C C   . SER N 3 63  ? 103.723 -34.556 70.346  1.000 32.500  ? 63  SER NNN C   1 
ATOM 19398 O O   . SER N 3 63  ? 102.808 -35.276 70.742  1.000 40.690  ? 63  SER NNN O   1 
ATOM 19399 C CB  . SER N 3 63  ? 102.657 -32.602 69.262  1.000 36.860  ? 63  SER NNN CB  1 
ATOM 19400 O OG  . SER N 3 63  ? 103.493 -32.229 68.192  1.000 44.050  ? 63  SER NNN OG  1 
ATOM 19401 N N   . VAL N 3 64  ? 104.880 -35.043 69.906  1.000 31.790  ? 64  VAL NNN N   1 
ATOM 19402 C CA  . VAL N 3 64  ? 105.115 -36.513 69.792  1.000 34.210  ? 64  VAL NNN CA  1 
ATOM 19403 C C   . VAL N 3 64  ? 106.358 -36.944 70.576  1.000 35.340  ? 64  VAL NNN C   1 
ATOM 19404 O O   . VAL N 3 64  ? 106.689 -38.123 70.440  1.000 36.440  ? 64  VAL NNN O   1 
ATOM 19405 C CB  . VAL N 3 64  ? 105.239 -36.944 68.319  1.000 37.160  ? 64  VAL NNN CB  1 
ATOM 19406 C CG1 . VAL N 3 64  ? 104.024 -36.524 67.498  1.000 36.160  ? 64  VAL NNN CG1 1 
ATOM 19407 C CG2 . VAL N 3 64  ? 106.525 -36.424 67.680  1.000 38.570  ? 64  VAL NNN CG2 1 
ATOM 19408 N N   . LYS N 3 65  ? 107.012 -36.048 71.338  1.000 35.610  ? 65  LYS NNN N   1 
ATOM 19409 C CA  . LYS N 3 65  ? 108.179 -36.372 72.205  1.000 34.670  ? 65  LYS NNN CA  1 
ATOM 19410 C C   . LYS N 3 65  ? 107.844 -37.645 72.974  1.000 35.030  ? 65  LYS NNN C   1 
ATOM 19411 O O   . LYS N 3 65  ? 106.737 -37.728 73.555  1.000 38.840  ? 65  LYS NNN O   1 
ATOM 19412 C CB  . LYS N 3 65  ? 108.490 -35.279 73.234  1.000 36.470  ? 65  LYS NNN CB  1 
ATOM 19413 C CG  . LYS N 3 65  ? 109.643 -34.342 72.936  1.000 44.160  ? 65  LYS NNN CG  1 
ATOM 19414 C CD  . LYS N 3 65  ? 110.391 -33.920 74.228  1.000 54.160  ? 65  LYS NNN CD  1 
ATOM 19415 C CE  . LYS N 3 65  ? 110.898 -32.478 74.260  1.000 64.200  ? 65  LYS NNN CE  1 
ATOM 19416 N NZ  . LYS N 3 65  ? 111.609 -32.077 73.013  1.000 68.950  ? 65  LYS NNN NZ  1 
ATOM 19417 N N   . GLY N 3 66  ? 108.719 -38.637 72.935  1.000 35.660  ? 66  GLY NNN N   1 
ATOM 19418 C CA  . GLY N 3 66  ? 108.557 -39.816 73.801  1.000 39.470  ? 66  GLY NNN CA  1 
ATOM 19419 C C   . GLY N 3 66  ? 107.751 -40.926 73.158  1.000 39.840  ? 66  GLY NNN C   1 
ATOM 19420 O O   . GLY N 3 66  ? 107.836 -42.032 73.691  1.000 45.430  ? 66  GLY NNN O   1 
ATOM 19421 N N   . ARG N 3 67  ? 106.999 -40.671 72.083  1.000 40.650  ? 67  ARG NNN N   1 
ATOM 19422 C CA  . ARG N 3 67  ? 106.076 -41.677 71.479  1.000 41.450  ? 67  ARG NNN CA  1 
ATOM 19423 C C   . ARG N 3 67  ? 106.587 -42.123 70.104  1.000 41.690  ? 67  ARG NNN C   1 
ATOM 19424 O O   . ARG N 3 67  ? 106.547 -43.340 69.803  1.000 41.610  ? 67  ARG NNN O   1 
ATOM 19425 C CB  . ARG N 3 67  ? 104.652 -41.113 71.395  1.000 40.730  ? 67  ARG NNN CB  1 
ATOM 19426 C CG  . ARG N 3 67  ? 104.107 -40.653 72.737  1.000 41.560  ? 67  ARG NNN CG  1 
ATOM 19427 C CD  . ARG N 3 67  ? 102.641 -40.295 72.741  1.000 40.230  ? 67  ARG NNN CD  1 
ATOM 19428 N NE  . ARG N 3 67  ? 102.344 -39.121 71.936  1.000 38.550  ? 67  ARG NNN NE  1 
ATOM 19429 C CZ  . ARG N 3 67  ? 101.652 -39.149 70.802  1.000 41.730  ? 67  ARG NNN CZ  1 
ATOM 19430 N NH1 . ARG N 3 67  ? 101.151 -40.297 70.347  1.000 43.410  ? 67  ARG NNN NH1 1 
ATOM 19431 N NH2 . ARG N 3 67  ? 101.454 -38.023 70.127  1.000 40.050  ? 67  ARG NNN NH2 1 
ATOM 19432 N N   . PHE N 3 68  ? 107.019 -41.171 69.281  1.000 42.330  ? 68  PHE NNN N   1 
ATOM 19433 C CA  . PHE N 3 68  ? 107.471 -41.411 67.887  1.000 41.840  ? 68  PHE NNN CA  1 
ATOM 19434 C C   . PHE N 3 68  ? 108.989 -41.568 67.856  1.000 38.350  ? 68  PHE NNN C   1 
ATOM 19435 O O   . PHE N 3 68  ? 109.675 -40.994 68.698  1.000 46.440  ? 68  PHE NNN O   1 
ATOM 19436 C CB  . PHE N 3 68  ? 107.011 -40.265 66.987  1.000 42.290  ? 68  PHE NNN CB  1 
ATOM 19437 C CG  . PHE N 3 68  ? 105.528 -40.211 66.739  1.000 44.590  ? 68  PHE NNN CG  1 
ATOM 19438 C CD1 . PHE N 3 68  ? 104.636 -40.914 67.533  1.000 45.220  ? 68  PHE NNN CD1 1 
ATOM 19439 C CD2 . PHE N 3 68  ? 105.023 -39.424 65.715  1.000 47.330  ? 68  PHE NNN CD2 1 
ATOM 19440 C CE1 . PHE N 3 68  ? 103.272 -40.839 67.307  1.000 46.130  ? 68  PHE NNN CE1 1 
ATOM 19441 C CE2 . PHE N 3 68  ? 103.658 -39.354 65.488  1.000 50.100  ? 68  PHE NNN CE2 1 
ATOM 19442 C CZ  . PHE N 3 68  ? 102.784 -40.062 66.286  1.000 51.180  ? 68  PHE NNN CZ  1 
ATOM 19443 N N   . THR N 3 69  ? 109.501 -42.322 66.892  1.000 35.160  ? 69  THR NNN N   1 
ATOM 19444 C CA  . THR N 3 69  ? 110.959 -42.475 66.660  1.000 35.050  ? 69  THR NNN CA  1 
ATOM 19445 C C   . THR N 3 69  ? 111.227 -42.455 65.157  1.000 39.660  ? 69  THR NNN C   1 
ATOM 19446 O O   . THR N 3 69  ? 110.652 -43.293 64.443  1.000 48.080  ? 69  THR NNN O   1 
ATOM 19447 C CB  . THR N 3 69  ? 111.491 -43.749 67.318  1.000 30.720  ? 69  THR NNN CB  1 
ATOM 19448 O OG1 . THR N 3 69  ? 110.876 -43.782 68.596  1.000 31.830  ? 69  THR NNN OG1 1 
ATOM 19449 C CG2 . THR N 3 69  ? 112.991 -43.770 67.440  1.000 28.370  ? 69  THR NNN CG2 1 
ATOM 19450 N N   . ILE N 3 70  ? 112.069 -41.527 64.710  1.000 39.350  ? 70  ILE NNN N   1 
ATOM 19451 C CA  . ILE N 3 70  ? 112.524 -41.433 63.297  1.000 38.200  ? 70  ILE NNN CA  1 
ATOM 19452 C C   . ILE N 3 70  ? 113.740 -42.359 63.136  1.000 36.660  ? 70  ILE NNN C   1 
ATOM 19453 O O   . ILE N 3 70  ? 114.509 -42.518 64.100  1.000 30.780  ? 70  ILE NNN O   1 
ATOM 19454 C CB  . ILE N 3 70  ? 112.848 -39.971 62.920  1.000 36.810  ? 70  ILE NNN CB  1 
ATOM 19455 C CG1 . ILE N 3 70  ? 112.832 -39.754 61.402  1.000 35.830  ? 70  ILE NNN CG1 1 
ATOM 19456 C CG2 . ILE N 3 70  ? 114.154 -39.518 63.543  1.000 38.740  ? 70  ILE NNN CG2 1 
ATOM 19457 C CD1 . ILE N 3 70  ? 112.842 -38.304 61.008  1.000 35.590  ? 70  ILE NNN CD1 1 
ATOM 19458 N N   . SER N 3 71  ? 113.901 -42.962 61.966  1.000 36.310  ? 71  SER NNN N   1 
ATOM 19459 C CA  . SER N 3 71  ? 115.102 -43.751 61.610  1.000 36.620  ? 71  SER NNN CA  1 
ATOM 19460 C C   . SER N 3 71  ? 115.237 -43.802 60.085  1.000 37.290  ? 71  SER NNN C   1 
ATOM 19461 O O   . SER N 3 71  ? 114.233 -43.572 59.382  1.000 33.380  ? 71  SER NNN O   1 
ATOM 19462 C CB  . SER N 3 71  ? 115.022 -45.125 62.212  1.000 35.330  ? 71  SER NNN CB  1 
ATOM 19463 O OG  . SER N 3 71  ? 114.024 -45.920 61.578  1.000 35.170  ? 71  SER NNN OG  1 
ATOM 19464 N N   . ARG N 3 72  ? 116.427 -44.108 59.593  1.000 38.430  ? 72  ARG NNN N   1 
ATOM 19465 C CA  . ARG N 3 72  ? 116.668 -44.279 58.143  1.000 42.420  ? 72  ARG NNN CA  1 
ATOM 19466 C C   . ARG N 3 72  ? 117.546 -45.521 57.916  1.000 45.670  ? 72  ARG NNN C   1 
ATOM 19467 O O   . ARG N 3 72  ? 118.299 -45.907 58.837  1.000 44.970  ? 72  ARG NNN O   1 
ATOM 19468 C CB  . ARG N 3 72  ? 117.310 -43.001 57.598  1.000 45.290  ? 72  ARG NNN CB  1 
ATOM 19469 C CG  . ARG N 3 72  ? 118.650 -42.664 58.252  1.000 48.370  ? 72  ARG NNN CG  1 
ATOM 19470 C CD  . ARG N 3 72  ? 119.178 -41.295 57.862  1.000 48.260  ? 72  ARG NNN CD  1 
ATOM 19471 N NE  . ARG N 3 72  ? 119.218 -41.103 56.413  1.000 44.010  ? 72  ARG NNN NE  1 
ATOM 19472 C CZ  . ARG N 3 72  ? 119.035 -39.947 55.796  1.000 41.930  ? 72  ARG NNN CZ  1 
ATOM 19473 N NH1 . ARG N 3 72  ? 119.092 -39.920 54.484  1.000 44.540  ? 72  ARG NNN NH1 1 
ATOM 19474 N NH2 . ARG N 3 72  ? 118.780 -38.831 56.460  1.000 41.350  ? 72  ARG NNN NH2 1 
ATOM 19475 N N   . ASP N 3 73  ? 117.439 -46.121 56.729  1.000 47.280  ? 73  ASP NNN N   1 
ATOM 19476 C CA  . ASP N 3 73  ? 118.324 -47.199 56.208  1.000 49.340  ? 73  ASP NNN CA  1 
ATOM 19477 C C   . ASP N 3 73  ? 118.888 -46.704 54.874  1.000 49.360  ? 73  ASP NNN C   1 
ATOM 19478 O O   . ASP N 3 73  ? 118.151 -46.743 53.853  1.000 41.680  ? 73  ASP NNN O   1 
ATOM 19479 C CB  . ASP N 3 73  ? 117.562 -48.517 56.052  1.000 52.930  ? 73  ASP NNN CB  1 
ATOM 19480 C CG  . ASP N 3 73  ? 118.414 -49.731 55.703  1.000 53.620  ? 73  ASP NNN CG  1 
ATOM 19481 O OD1 . ASP N 3 73  ? 119.638 -49.555 55.344  1.000 51.760  ? 73  ASP NNN OD1 1 
ATOM 19482 O OD2 . ASP N 3 73  ? 117.838 -50.853 55.791  1.000 49.240  ? 73  ASP NNN OD2 1 
ATOM 19483 N N   . ASN N 3 74  ? 120.127 -46.205 54.908  1.000 52.630  ? 74  ASN NNN N   1 
ATOM 19484 C CA  . ASN N 3 74  ? 120.757 -45.512 53.753  1.000 49.750  ? 74  ASN NNN CA  1 
ATOM 19485 C C   . ASN N 3 74  ? 121.056 -46.542 52.662  1.000 47.920  ? 74  ASN NNN C   1 
ATOM 19486 O O   . ASN N 3 74  ? 121.047 -46.160 51.492  1.000 53.630  ? 74  ASN NNN O   1 
ATOM 19487 C CB  . ASN N 3 74  ? 121.990 -44.689 54.148  1.000 43.340  ? 74  ASN NNN CB  1 
ATOM 19488 C CG  . ASN N 3 74  ? 121.641 -43.327 54.715  1.000 37.830  ? 74  ASN NNN CG  1 
ATOM 19489 O OD1 . ASN N 3 74  ? 120.486 -42.876 54.652  1.000 32.500  ? 74  ASN NNN OD1 1 
ATOM 19490 N ND2 . ASN N 3 74  ? 122.650 -42.665 55.259  1.000 36.910  ? 74  ASN NNN ND2 1 
ATOM 19491 N N   . ALA N 3 75  ? 121.268 -47.803 53.030  1.000 45.730  ? 75  ALA NNN N   1 
ATOM 19492 C CA  . ALA N 3 75  ? 121.447 -48.899 52.055  1.000 43.220  ? 75  ALA NNN CA  1 
ATOM 19493 C C   . ALA N 3 75  ? 120.135 -49.206 51.355  1.000 40.100  ? 75  ALA NNN C   1 
ATOM 19494 O O   . ALA N 3 75  ? 120.187 -49.606 50.208  1.000 43.250  ? 75  ALA NNN O   1 
ATOM 19495 C CB  . ALA N 3 75  ? 122.008 -50.117 52.722  1.000 46.720  ? 75  ALA NNN CB  1 
ATOM 19496 N N   . ARG N 3 76  ? 118.979 -49.043 52.012  1.000 41.230  ? 76  ARG NNN N   1 
ATOM 19497 C CA  . ARG N 3 76  ? 117.668 -49.418 51.430  1.000 48.040  ? 76  ARG NNN CA  1 
ATOM 19498 C C   . ARG N 3 76  ? 116.959 -48.147 50.931  1.000 43.540  ? 76  ARG NNN C   1 
ATOM 19499 O O   . ARG N 3 76  ? 115.786 -48.267 50.543  1.000 37.850  ? 76  ARG NNN O   1 
ATOM 19500 C CB  . ARG N 3 76  ? 116.810 -50.226 52.435  1.000 62.020  ? 76  ARG NNN CB  1 
ATOM 19501 C CG  . ARG N 3 76  ? 117.169 -51.718 52.555  1.000 67.460  ? 76  ARG NNN CG  1 
ATOM 19502 C CD  . ARG N 3 76  ? 116.351 -52.600 53.509  1.000 68.920  ? 76  ARG NNN CD  1 
ATOM 19503 N NE  . ARG N 3 76  ? 117.111 -53.693 54.158  1.000 67.980  ? 76  ARG NNN NE  1 
ATOM 19504 C CZ  . ARG N 3 76  ? 117.916 -53.567 55.224  1.000 53.830  ? 76  ARG NNN CZ  1 
ATOM 19505 N N   . ASN N 3 77  ? 117.616 -46.976 50.930  1.000 42.310  ? 77  ASN NNN N   1 
ATOM 19506 C CA  . ASN N 3 77  ? 117.048 -45.690 50.422  1.000 45.270  ? 77  ASN NNN CA  1 
ATOM 19507 C C   . ASN N 3 77  ? 115.680 -45.418 51.062  1.000 44.170  ? 77  ASN NNN C   1 
ATOM 19508 O O   . ASN N 3 77  ? 114.739 -45.046 50.317  1.000 40.430  ? 77  ASN NNN O   1 
ATOM 19509 C CB  . ASN N 3 77  ? 116.868 -45.673 48.898  1.000 47.750  ? 77  ASN NNN CB  1 
ATOM 19510 C CG  . ASN N 3 77  ? 118.149 -45.379 48.140  1.000 51.020  ? 77  ASN NNN CG  1 
ATOM 19511 O OD1 . ASN N 3 77  ? 118.775 -44.339 48.321  1.000 45.910  ? 77  ASN NNN OD1 1 
ATOM 19512 N ND2 . ASN N 3 77  ? 118.557 -46.294 47.273  1.000 58.420  ? 77  ASN NNN ND2 1 
ATOM 19513 N N   . SER N 3 78  ? 115.555 -45.590 52.383  1.000 42.770  ? 78  SER NNN N   1 
ATOM 19514 C CA  . SER N 3 78  ? 114.256 -45.527 53.109  1.000 40.380  ? 78  SER NNN CA  1 
ATOM 19515 C C   . SER N 3 78  ? 114.366 -44.763 54.428  1.000 38.450  ? 78  SER NNN C   1 
ATOM 19516 O O   . SER N 3 78  ? 115.300 -45.006 55.195  1.000 39.560  ? 78  SER NNN O   1 
ATOM 19517 C CB  . SER N 3 78  ? 113.712 -46.899 53.341  1.000 39.980  ? 78  SER NNN CB  1 
ATOM 19518 O OG  . SER N 3 78  ? 113.257 -47.440 52.122  1.000 43.390  ? 78  SER NNN OG  1 
ATOM 19519 N N   . LEU N 3 79  ? 113.393 -43.898 54.678  1.000 35.530  ? 79  LEU NNN N   1 
ATOM 19520 C CA  . LEU N 3 79  ? 113.187 -43.181 55.959  1.000 33.460  ? 79  LEU NNN CA  1 
ATOM 19521 C C   . LEU N 3 79  ? 111.980 -43.825 56.646  1.000 34.160  ? 79  LEU NNN C   1 
ATOM 19522 O O   . LEU N 3 79  ? 111.015 -44.183 55.933  1.000 34.090  ? 79  LEU NNN O   1 
ATOM 19523 C CB  . LEU N 3 79  ? 112.934 -41.707 55.647  1.000 31.760  ? 79  LEU NNN CB  1 
ATOM 19524 C CG  . LEU N 3 79  ? 112.419 -40.864 56.801  1.000 32.220  ? 79  LEU NNN CG  1 
ATOM 19525 C CD1 . LEU N 3 79  ? 113.564 -40.454 57.694  1.000 33.340  ? 79  LEU NNN CD1 1 
ATOM 19526 C CD2 . LEU N 3 79  ? 111.680 -39.640 56.294  1.000 34.200  ? 79  LEU NNN CD2 1 
ATOM 19527 N N   . TYR N 3 80  ? 112.035 -43.987 57.969  1.000 35.030  ? 80  TYR NNN N   1 
ATOM 19528 C CA  . TYR N 3 80  ? 110.963 -44.627 58.775  1.000 36.100  ? 80  TYR NNN CA  1 
ATOM 19529 C C   . TYR N 3 80  ? 110.546 -43.711 59.933  1.000 37.270  ? 80  TYR NNN C   1 
ATOM 19530 O O   . TYR N 3 80  ? 111.389 -42.953 60.474  1.000 33.550  ? 80  TYR NNN O   1 
ATOM 19531 C CB  . TYR N 3 80  ? 111.410 -45.985 59.317  1.000 34.190  ? 80  TYR NNN CB  1 
ATOM 19532 C CG  . TYR N 3 80  ? 111.967 -46.929 58.287  1.000 34.440  ? 80  TYR NNN CG  1 
ATOM 19533 C CD1 . TYR N 3 80  ? 111.149 -47.523 57.338  1.000 35.210  ? 80  TYR NNN CD1 1 
ATOM 19534 C CD2 . TYR N 3 80  ? 113.318 -47.235 58.260  1.000 34.600  ? 80  TYR NNN CD2 1 
ATOM 19535 C CE1 . TYR N 3 80  ? 111.652 -48.429 56.411  1.000 35.130  ? 80  TYR NNN CE1 1 
ATOM 19536 C CE2 . TYR N 3 80  ? 113.838 -48.114 57.324  1.000 35.270  ? 80  TYR NNN CE2 1 
ATOM 19537 C CZ  . TYR N 3 80  ? 113.003 -48.717 56.397  1.000 36.040  ? 80  TYR NNN CZ  1 
ATOM 19538 O OH  . TYR N 3 80  ? 113.517 -49.586 55.475  1.000 42.790  ? 80  TYR NNN OH  1 
ATOM 19539 N N   . LEU N 3 81  ? 109.265 -43.800 60.293  1.000 37.780  ? 81  LEU NNN N   1 
ATOM 19540 C CA  . LEU N 3 81  ? 108.708 -43.210 61.533  1.000 39.480  ? 81  LEU NNN CA  1 
ATOM 19541 C C   . LEU N 3 81  ? 107.957 -44.305 62.294  1.000 40.570  ? 81  LEU NNN C   1 
ATOM 19542 O O   . LEU N 3 81  ? 106.950 -44.807 61.780  1.000 39.970  ? 81  LEU NNN O   1 
ATOM 19543 C CB  . LEU N 3 81  ? 107.776 -42.045 61.206  1.000 39.540  ? 81  LEU NNN CB  1 
ATOM 19544 C CG  . LEU N 3 81  ? 107.201 -41.314 62.421  1.000 39.260  ? 81  LEU NNN CG  1 
ATOM 19545 C CD1 . LEU N 3 81  ? 108.304 -40.667 63.216  1.000 38.940  ? 81  LEU NNN CD1 1 
ATOM 19546 C CD2 . LEU N 3 81  ? 106.166 -40.278 62.008  1.000 39.490  ? 81  LEU NNN CD2 1 
ATOM 19547 N N   . GLN N 3 82  ? 108.445 -44.646 63.484  1.000 41.480  ? 82  GLN NNN N   1 
ATOM 19548 C CA  . GLN N 3 82  ? 107.814 -45.588 64.433  1.000 39.410  ? 82  GLN NNN CA  1 
ATOM 19549 C C   . GLN N 3 82  ? 106.853 -44.804 65.329  1.000 42.670  ? 82  GLN NNN C   1 
ATOM 19550 O O   . GLN N 3 82  ? 107.338 -44.001 66.146  1.000 53.370  ? 82  GLN NNN O   1 
ATOM 19551 C CB  . GLN N 3 82  ? 108.900 -46.279 65.251  1.000 38.540  ? 82  GLN NNN CB  1 
ATOM 19552 C CG  . GLN N 3 82  ? 108.357 -47.346 66.180  1.000 41.240  ? 82  GLN NNN CG  1 
ATOM 19553 C CD  . GLN N 3 82  ? 107.506 -48.322 65.424  1.000 41.250  ? 82  GLN NNN CD  1 
ATOM 19554 O OE1 . GLN N 3 82  ? 107.997 -49.004 64.520  1.000 43.120  ? 82  GLN NNN OE1 1 
ATOM 19555 N NE2 . GLN N 3 82  ? 106.233 -48.365 65.795  1.000 42.980  ? 82  GLN NNN NE2 1 
ATOM 19556 N N   . MET N 3 83  ? 105.548 -45.030 65.180  1.000 44.460  ? 83  MET NNN N   1 
ATOM 19557 C CA  . MET N 3 83  ? 104.492 -44.306 65.931  1.000 48.950  ? 83  MET NNN CA  1 
ATOM 19558 C C   . MET N 3 83  ? 103.904 -45.245 66.988  1.000 49.330  ? 83  MET NNN C   1 
ATOM 19559 O O   . MET N 3 83  ? 103.152 -46.162 66.611  1.000 50.460  ? 83  MET NNN O   1 
ATOM 19560 C CB  . MET N 3 83  ? 103.383 -43.820 64.990  1.000 52.310  ? 83  MET NNN CB  1 
ATOM 19561 C CG  . MET N 3 83  ? 103.892 -42.909 63.885  1.000 52.170  ? 83  MET NNN CG  1 
ATOM 19562 S SD  . MET N 3 83  ? 102.744 -42.728 62.515  1.000 54.480  ? 83  MET NNN SD  1 
ATOM 19563 C CE  . MET N 3 83  ? 101.657 -41.468 63.192  1.000 46.670  ? 83  MET NNN CE  1 
ATOM 19564 N N   . ASN N 3 84  ? 104.243 -45.023 68.263  1.000 46.620  ? 84  ASN NNN N   1 
ATOM 19565 C CA  . ASN N 3 84  ? 103.703 -45.797 69.411  1.000 45.630  ? 84  ASN NNN CA  1 
ATOM 19566 C C   . ASN N 3 84  ? 102.694 -44.930 70.156  1.000 45.890  ? 84  ASN NNN C   1 
ATOM 19567 O O   . ASN N 3 84  ? 102.767 -43.703 70.001  1.000 47.110  ? 84  ASN NNN O   1 
ATOM 19568 C CB  . ASN N 3 84  ? 104.821 -46.236 70.347  1.000 45.550  ? 84  ASN NNN CB  1 
ATOM 19569 C CG  . ASN N 3 84  ? 105.810 -47.160 69.666  1.000 49.080  ? 84  ASN NNN CG  1 
ATOM 19570 O OD1 . ASN N 3 84  ? 105.530 -47.762 68.624  1.000 47.670  ? 84  ASN NNN OD1 1 
ATOM 19571 N ND2 . ASN N 3 84  ? 106.973 -47.286 70.276  1.000 52.050  ? 84  ASN NNN ND2 1 
ATOM 19572 N N   . SER N 3 85  ? 101.796 -45.551 70.922  1.000 43.940  ? 85  SER NNN N   1 
ATOM 19573 C CA  . SER N 3 85  ? 100.866 -44.861 71.854  1.000 46.100  ? 85  SER NNN CA  1 
ATOM 19574 C C   . SER N 3 85  ? 100.023 -43.840 71.086  1.000 47.330  ? 85  SER NNN C   1 
ATOM 19575 O O   . SER N 3 85  ? 99.756  -42.732 71.614  1.000 53.490  ? 85  SER NNN O   1 
ATOM 19576 C CB  . SER N 3 85  ? 101.618 -44.202 72.971  1.000 47.300  ? 85  SER NNN CB  1 
ATOM 19577 O OG  . SER N 3 85  ? 102.528 -45.113 73.556  1.000 49.890  ? 85  SER NNN OG  1 
ATOM 19578 N N   . LEU N 3 86  ? 99.608  -44.218 69.886  1.000 46.430  ? 86  LEU NNN N   1 
ATOM 19579 C CA  . LEU N 3 86  ? 98.831  -43.345 68.973  1.000 53.610  ? 86  LEU NNN CA  1 
ATOM 19580 C C   . LEU N 3 86  ? 97.584  -42.797 69.679  1.000 48.540  ? 86  LEU NNN C   1 
ATOM 19581 O O   . LEU N 3 86  ? 96.966  -43.530 70.456  1.000 54.970  ? 86  LEU NNN O   1 
ATOM 19582 C CB  . LEU N 3 86  ? 98.468  -44.143 67.716  1.000 62.520  ? 86  LEU NNN CB  1 
ATOM 19583 C CG  . LEU N 3 86  ? 99.569  -44.149 66.650  1.000 67.600  ? 86  LEU NNN CG  1 
ATOM 19584 C CD1 . LEU N 3 86  ? 99.315  -45.198 65.573  1.000 67.740  ? 86  LEU NNN CD1 1 
ATOM 19585 C CD2 . LEU N 3 86  ? 99.697  -42.760 66.038  1.000 69.290  ? 86  LEU NNN CD2 1 
ATOM 19586 N N   . ARG N 3 87  ? 97.242  -41.541 69.415  1.000 46.440  ? 87  ARG NNN N   1 
ATOM 19587 C CA  . ARG N 3 87  ? 96.047  -40.864 69.978  1.000 48.740  ? 87  ARG NNN CA  1 
ATOM 19588 C C   . ARG N 3 87  ? 95.143  -40.396 68.841  1.000 50.740  ? 87  ARG NNN C   1 
ATOM 19589 O O   . ARG N 3 87  ? 95.595  -40.436 67.702  1.000 59.750  ? 87  ARG NNN O   1 
ATOM 19590 C CB  . ARG N 3 87  ? 96.483  -39.673 70.826  1.000 48.240  ? 87  ARG NNN CB  1 
ATOM 19591 C CG  . ARG N 3 87  ? 97.640  -40.005 71.751  1.000 48.880  ? 87  ARG NNN CG  1 
ATOM 19592 C CD  . ARG N 3 87  ? 98.122  -38.723 72.383  1.000 50.610  ? 87  ARG NNN CD  1 
ATOM 19593 N NE  . ARG N 3 87  ? 99.184  -38.956 73.342  1.000 50.700  ? 87  ARG NNN NE  1 
ATOM 19594 C CZ  . ARG N 3 87  ? 99.924  -38.001 73.853  1.000 52.120  ? 87  ARG NNN CZ  1 
ATOM 19595 N NH1 . ARG N 3 87  ? 99.724  -36.751 73.477  1.000 63.310  ? 87  ARG NNN NH1 1 
ATOM 19596 N NH2 . ARG N 3 87  ? 100.853 -38.298 74.727  1.000 52.080  ? 87  ARG NNN NH2 1 
ATOM 19597 N N   . VAL N 3 88  ? 93.939  -39.935 69.174  1.000 50.450  ? 88  VAL NNN N   1 
ATOM 19598 C CA  . VAL N 3 88  ? 92.944  -39.383 68.210  1.000 50.060  ? 88  VAL NNN CA  1 
ATOM 19599 C C   . VAL N 3 88  ? 93.573  -38.196 67.465  1.000 48.520  ? 88  VAL NNN C   1 
ATOM 19600 O O   . VAL N 3 88  ? 93.468  -38.155 66.232  1.000 44.610  ? 88  VAL NNN O   1 
ATOM 19601 C CB  . VAL N 3 88  ? 91.622  -39.048 68.930  1.000 49.380  ? 88  VAL NNN CB  1 
ATOM 19602 C CG1 . VAL N 3 88  ? 90.733  -38.041 68.204  1.000 50.250  ? 88  VAL NNN CG1 1 
ATOM 19603 C CG2 . VAL N 3 88  ? 90.870  -40.338 69.219  1.000 45.340  ? 88  VAL NNN CG2 1 
ATOM 19604 N N   . GLU N 3 89  ? 94.238  -37.305 68.203  1.000 49.890  ? 89  GLU NNN N   1 
ATOM 19605 C CA  . GLU N 3 89  ? 94.862  -36.063 67.666  1.000 52.010  ? 89  GLU NNN CA  1 
ATOM 19606 C C   . GLU N 3 89  ? 95.893  -36.429 66.589  1.000 51.730  ? 89  GLU NNN C   1 
ATOM 19607 O O   . GLU N 3 89  ? 96.051  -35.650 65.641  1.000 60.220  ? 89  GLU NNN O   1 
ATOM 19608 C CB  . GLU N 3 89  ? 95.532  -35.225 68.761  1.000 58.790  ? 89  GLU NNN CB  1 
ATOM 19609 C CG  . GLU N 3 89  ? 94.764  -35.168 70.079  1.000 63.430  ? 89  GLU NNN CG  1 
ATOM 19610 C CD  . GLU N 3 89  ? 95.283  -36.145 71.123  1.000 66.350  ? 89  GLU NNN CD  1 
ATOM 19611 O OE1 . GLU N 3 89  ? 96.378  -35.885 71.684  1.000 57.460  ? 89  GLU NNN OE1 1 
ATOM 19612 O OE2 . GLU N 3 89  ? 94.616  -37.186 71.343  1.000 76.030  ? 89  GLU NNN OE2 1 
ATOM 19613 N N   . ASP N 3 90  ? 96.555  -37.583 66.696  1.000 50.450  ? 90  ASP NNN N   1 
ATOM 19614 C CA  . ASP N 3 90  ? 97.616  -38.006 65.737  1.000 55.110  ? 90  ASP NNN CA  1 
ATOM 19615 C C   . ASP N 3 90  ? 97.034  -38.299 64.352  1.000 53.320  ? 90  ASP NNN C   1 
ATOM 19616 O O   . ASP N 3 90  ? 97.850  -38.536 63.422  1.000 46.410  ? 90  ASP NNN O   1 
ATOM 19617 C CB  . ASP N 3 90  ? 98.410  -39.218 66.236  1.000 55.160  ? 90  ASP NNN CB  1 
ATOM 19618 C CG  . ASP N 3 90  ? 99.218  -38.923 67.482  1.000 59.090  ? 90  ASP NNN CG  1 
ATOM 19619 O OD1 . ASP N 3 90  ? 99.531  -37.714 67.718  1.000 59.290  ? 90  ASP NNN OD1 1 
ATOM 19620 O OD2 . ASP N 3 90  ? 99.511  -39.890 68.221  1.000 57.720  ? 90  ASP NNN OD2 1 
ATOM 19621 N N   . THR N 3 91  ? 95.705  -38.303 64.201  1.000 54.520  ? 91  THR NNN N   1 
ATOM 19622 C CA  . THR N 3 91  ? 95.058  -38.471 62.877  1.000 57.120  ? 91  THR NNN CA  1 
ATOM 19623 C C   . THR N 3 91  ? 95.514  -37.333 61.962  1.000 54.240  ? 91  THR NNN C   1 
ATOM 19624 O O   . THR N 3 91  ? 95.314  -36.155 62.342  1.000 52.510  ? 91  THR NNN O   1 
ATOM 19625 C CB  . THR N 3 91  ? 93.527  -38.468 62.951  1.000 61.610  ? 91  THR NNN CB  1 
ATOM 19626 O OG1 . THR N 3 91  ? 93.135  -37.240 63.573  1.000 74.810  ? 91  THR NNN OG1 1 
ATOM 19627 C CG2 . THR N 3 91  ? 92.936  -39.638 63.709  1.000 66.640  ? 91  THR NNN CG2 1 
ATOM 19628 N N   . ALA N 3 92  ? 96.109  -37.681 60.818  1.000 48.030  ? 92  ALA NNN N   1 
ATOM 19629 C CA  . ALA N 3 92  ? 96.642  -36.719 59.829  1.000 44.010  ? 92  ALA NNN CA  1 
ATOM 19630 C C   . ALA N 3 92  ? 97.146  -37.475 58.607  1.000 43.390  ? 92  ALA NNN C   1 
ATOM 19631 O O   . ALA N 3 92  ? 97.316  -38.716 58.694  1.000 43.180  ? 92  ALA NNN O   1 
ATOM 19632 C CB  . ALA N 3 92  ? 97.744  -35.896 60.427  1.000 42.060  ? 92  ALA NNN CB  1 
ATOM 19633 N N   . VAL N 3 93  ? 97.371  -36.744 57.516  1.000 45.050  ? 93  VAL NNN N   1 
ATOM 19634 C CA  . VAL N 3 93  ? 98.218  -37.210 56.388  1.000 49.720  ? 93  VAL NNN CA  1 
ATOM 19635 C C   . VAL N 3 93  ? 99.665  -36.992 56.827  1.000 46.810  ? 93  VAL NNN C   1 
ATOM 19636 O O   . VAL N 3 93  ? 99.947  -35.874 57.313  1.000 47.070  ? 93  VAL NNN O   1 
ATOM 19637 C CB  . VAL N 3 93  ? 97.907  -36.450 55.089  1.000 57.920  ? 93  VAL NNN CB  1 
ATOM 19638 C CG1 . VAL N 3 93  ? 98.776  -36.997 53.950  1.000 65.380  ? 93  VAL NNN CG1 1 
ATOM 19639 C CG2 . VAL N 3 93  ? 96.415  -36.461 54.751  1.000 59.020  ? 93  VAL NNN CG2 1 
ATOM 19640 N N   . TYR N 3 94  ? 100.520 -38.011 56.699  1.000 42.600  ? 94  TYR NNN N   1 
ATOM 19641 C CA  . TYR N 3 94  ? 101.945 -37.979 57.118  1.000 41.500  ? 94  TYR NNN CA  1 
ATOM 19642 C C   . TYR N 3 94  ? 102.806 -37.848 55.866  1.000 37.880  ? 94  TYR NNN C   1 
ATOM 19643 O O   . TYR N 3 94  ? 103.005 -38.861 55.176  1.000 38.030  ? 94  TYR NNN O   1 
ATOM 19644 C CB  . TYR N 3 94  ? 102.293 -39.190 58.000  1.000 42.120  ? 94  TYR NNN CB  1 
ATOM 19645 C CG  . TYR N 3 94  ? 101.873 -39.003 59.434  1.000 39.260  ? 94  TYR NNN CG  1 
ATOM 19646 C CD1 . TYR N 3 94  ? 100.534 -38.911 59.760  1.000 40.480  ? 94  TYR NNN CD1 1 
ATOM 19647 C CD2 . TYR N 3 94  ? 102.799 -38.865 60.449  1.000 36.740  ? 94  TYR NNN CD2 1 
ATOM 19648 C CE1 . TYR N 3 94  ? 100.119 -38.707 61.068  1.000 42.320  ? 94  TYR NNN CE1 1 
ATOM 19649 C CE2 . TYR N 3 94  ? 102.404 -38.646 61.756  1.000 38.710  ? 94  TYR NNN CE2 1 
ATOM 19650 C CZ  . TYR N 3 94  ? 101.057 -38.565 62.072  1.000 41.340  ? 94  TYR NNN CZ  1 
ATOM 19651 O OH  . TYR N 3 94  ? 100.625 -38.369 63.362  1.000 37.800  ? 94  TYR NNN OH  1 
ATOM 19652 N N   . TYR N 3 95  ? 103.268 -36.625 55.601  1.000 38.800  ? 95  TYR NNN N   1 
ATOM 19653 C CA  . TYR N 3 95  ? 104.203 -36.266 54.495  1.000 37.940  ? 95  TYR NNN CA  1 
ATOM 19654 C C   . TYR N 3 95  ? 105.663 -36.558 54.898  1.000 34.000  ? 95  TYR NNN C   1 
ATOM 19655 O O   . TYR N 3 95  ? 106.055 -36.460 56.064  1.000 28.530  ? 95  TYR NNN O   1 
ATOM 19656 C CB  . TYR N 3 95  ? 103.966 -34.826 53.991  1.000 33.290  ? 95  TYR NNN CB  1 
ATOM 19657 C CG  . TYR N 3 95  ? 102.595 -34.554 53.413  1.000 31.530  ? 95  TYR NNN CG  1 
ATOM 19658 C CD1 . TYR N 3 95  ? 102.225 -35.019 52.161  1.000 33.050  ? 95  TYR NNN CD1 1 
ATOM 19659 C CD2 . TYR N 3 95  ? 101.658 -33.809 54.107  1.000 30.560  ? 95  TYR NNN CD2 1 
ATOM 19660 C CE1 . TYR N 3 95  ? 100.962 -34.779 51.637  1.000 35.570  ? 95  TYR NNN CE1 1 
ATOM 19661 C CE2 . TYR N 3 95  ? 100.378 -33.574 53.596  1.000 34.490  ? 95  TYR NNN CE2 1 
ATOM 19662 C CZ  . TYR N 3 95  ? 100.018 -34.043 52.344  1.000 32.060  ? 95  TYR NNN CZ  1 
ATOM 19663 N N   . CYS N 3 96  ? 106.440 -36.962 53.906  1.000 35.920  ? 96  CYS NNN N   1 
ATOM 19664 C CA  . CYS N 3 96  ? 107.899 -37.198 53.950  1.000 40.370  ? 96  CYS NNN CA  1 
ATOM 19665 C C   . CYS N 3 96  ? 108.585 -36.126 53.085  1.000 43.360  ? 96  CYS NNN C   1 
ATOM 19666 O O   . CYS N 3 96  ? 108.184 -35.980 51.915  1.000 46.230  ? 96  CYS NNN O   1 
ATOM 19667 C CB  . CYS N 3 96  ? 108.158 -38.615 53.450  1.000 43.210  ? 96  CYS NNN CB  1 
ATOM 19668 S SG  . CYS N 3 96  ? 109.891 -39.127 53.529  1.000 51.050  ? 96  CYS NNN SG  1 
ATOM 19669 N N   . ALA N 3 97  ? 109.537 -35.363 53.632  1.000 43.930  ? 97  ALA NNN N   1 
ATOM 19670 C CA  . ALA N 3 97  ? 110.112 -34.154 52.986  1.000 39.160  ? 97  ALA NNN CA  1 
ATOM 19671 C C   . ALA N 3 97  ? 111.637 -34.116 53.129  1.000 33.680  ? 97  ALA NNN C   1 
ATOM 19672 O O   . ALA N 3 97  ? 112.143 -34.438 54.204  1.000 35.150  ? 97  ALA NNN O   1 
ATOM 19673 C CB  . ALA N 3 97  ? 109.482 -32.878 53.504  1.000 39.540  ? 97  ALA NNN CB  1 
ATOM 19674 N N   . ARG N 3 98  ? 112.332 -33.718 52.068  1.000 30.810  ? 98  ARG NNN N   1 
ATOM 19675 C CA  . ARG N 3 98  ? 113.804 -33.548 52.069  1.000 31.040  ? 98  ARG NNN CA  1 
ATOM 19676 C C   . ARG N 3 98  ? 114.176 -32.114 52.478  1.000 33.130  ? 98  ARG NNN C   1 
ATOM 19677 O O   . ARG N 3 98  ? 113.440 -31.167 52.091  1.000 33.310  ? 98  ARG NNN O   1 
ATOM 19678 C CB  . ARG N 3 98  ? 114.404 -33.814 50.690  1.000 29.710  ? 98  ARG NNN CB  1 
ATOM 19679 C CG  . ARG N 3 98  ? 115.920 -33.876 50.713  1.000 31.700  ? 98  ARG NNN CG  1 
ATOM 19680 C CD  . ARG N 3 98  ? 116.490 -34.149 49.348  1.000 33.190  ? 98  ARG NNN CD  1 
ATOM 19681 N NE  . ARG N 3 98  ? 116.338 -32.997 48.487  1.000 34.940  ? 98  ARG NNN NE  1 
ATOM 19682 C CZ  . ARG N 3 98  ? 116.899 -32.864 47.299  1.000 35.220  ? 98  ARG NNN CZ  1 
ATOM 19683 N NH1 . ARG N 3 98  ? 117.665 -33.827 46.800  1.000 33.750  ? 98  ARG NNN NH1 1 
ATOM 19684 N NH2 . ARG N 3 98  ? 116.679 -31.758 46.614  1.000 34.990  ? 98  ARG NNN NH2 1 
ATOM 19685 N N   . TYR N 3 99  ? 115.304 -31.969 53.189  1.000 30.920  ? 99  TYR NNN N   1 
ATOM 19686 C CA  . TYR N 3 99  ? 115.868 -30.633 53.490  1.000 28.280  ? 99  TYR NNN CA  1 
ATOM 19687 C C   . TYR N 3 99  ? 117.210 -30.586 52.772  1.000 28.460  ? 99  TYR NNN C   1 
ATOM 19688 O O   . TYR N 3 99  ? 118.021 -31.498 52.970  1.000 27.360  ? 99  TYR NNN O   1 
ATOM 19689 C CB  . TYR N 3 99  ? 116.132 -30.409 54.980  1.000 26.300  ? 99  TYR NNN CB  1 
ATOM 19690 C CG  . TYR N 3 99  ? 117.150 -29.340 55.303  1.000 25.660  ? 99  TYR NNN CG  1 
ATOM 19691 C CD1 . TYR N 3 99  ? 116.797 -28.005 55.336  1.000 26.700  ? 99  TYR NNN CD1 1 
ATOM 19692 C CD2 . TYR N 3 99  ? 118.468 -29.656 55.588  1.000 24.510  ? 99  TYR NNN CD2 1 
ATOM 19693 C CE1 . TYR N 3 99  ? 117.722 -27.016 55.623  1.000 25.540  ? 99  TYR NNN CE1 1 
ATOM 19694 C CE2 . TYR N 3 99  ? 119.408 -28.682 55.869  1.000 25.590  ? 99  TYR NNN CE2 1 
ATOM 19695 C CZ  . TYR N 3 99  ? 119.033 -27.354 55.890  1.000 24.210  ? 99  TYR NNN CZ  1 
ATOM 19696 O OH  . TYR N 3 99  ? 119.956 -26.392 56.176  1.000 20.030  ? 99  TYR NNN OH  1 
ATOM 19697 N N   . ALA N 3 100 ? 117.422 -29.569 51.947  1.000 27.330  ? 100 ALA NNN N   1 
ATOM 19698 C CA  . ALA N 3 100 ? 118.741 -29.392 51.303  1.000 28.180  ? 100 ALA NNN CA  1 
ATOM 19699 C C   . ALA N 3 100 ? 119.261 -28.030 51.732  1.000 27.420  ? 100 ALA NNN C   1 
ATOM 19700 O O   . ALA N 3 100 ? 118.464 -27.159 51.969  1.000 24.250  ? 100 ALA NNN O   1 
ATOM 19701 C CB  . ALA N 3 100 ? 118.559 -29.471 49.828  1.000 29.530  ? 100 ALA NNN CB  1 
ATOM 19702 N N   . HIS N 3 101 ? 120.571 -27.875 51.837  1.000 29.360  ? 101 HIS NNN N   1 
ATOM 19703 C CA  . HIS N 3 101 ? 121.165 -26.597 52.290  1.000 31.050  ? 101 HIS NNN CA  1 
ATOM 19704 C C   . HIS N 3 101 ? 120.776 -25.502 51.316  1.000 34.500  ? 101 HIS NNN C   1 
ATOM 19705 O O   . HIS N 3 101 ? 120.831 -25.792 50.117  1.000 52.550  ? 101 HIS NNN O   1 
ATOM 19706 C CB  . HIS N 3 101 ? 122.688 -26.730 52.367  1.000 29.600  ? 101 HIS NNN CB  1 
ATOM 19707 C CG  . HIS N 3 101 ? 123.400 -25.515 52.846  1.000 26.350  ? 101 HIS NNN CG  1 
ATOM 19708 N ND1 . HIS N 3 101 ? 124.410 -24.933 52.124  1.000 27.100  ? 101 HIS NNN ND1 1 
ATOM 19709 C CD2 . HIS N 3 101 ? 123.267 -24.787 53.972  1.000 25.110  ? 101 HIS NNN CD2 1 
ATOM 19710 C CE1 . HIS N 3 101 ? 124.868 -23.891 52.779  1.000 25.160  ? 101 HIS NNN CE1 1 
ATOM 19711 N NE2 . HIS N 3 101 ? 124.182 -23.777 53.912  1.000 24.740  ? 101 HIS NNN NE2 1 
ATOM 19712 N N   . ASP N 3 102 ? 120.344 -24.341 51.815  1.000 29.290  ? 102 ASP NNN N   1 
ATOM 19713 C CA  . ASP N 3 102 ? 119.976 -23.168 50.981  1.000 28.350  ? 102 ASP NNN CA  1 
ATOM 19714 C C   . ASP N 3 102 ? 118.579 -23.347 50.401  1.000 27.980  ? 102 ASP NNN C   1 
ATOM 19715 O O   . ASP N 3 102 ? 117.808 -22.386 50.432  1.000 24.060  ? 102 ASP NNN O   1 
ATOM 19716 C CB  . ASP N 3 102 ? 121.015 -22.841 49.917  1.000 27.230  ? 102 ASP NNN CB  1 
ATOM 19717 C CG  . ASP N 3 102 ? 121.013 -21.396 49.510  1.000 24.300  ? 102 ASP NNN CG  1 
ATOM 19718 O OD1 . ASP N 3 102 ? 121.062 -20.545 50.404  1.000 22.000  ? 102 ASP NNN OD1 1 
ATOM 19719 O OD2 . ASP N 3 102 ? 120.985 -21.153 48.309  1.000 24.510  ? 102 ASP NNN OD2 1 
ATOM 19720 N N   . TRP N 3 103 ? 118.281 -24.537 49.903  1.000 28.880  ? 103 TRP NNN N   1 
ATOM 19721 C CA  . TRP N 3 103 ? 116.956 -24.829 49.320  1.000 28.520  ? 103 TRP NNN CA  1 
ATOM 19722 C C   . TRP N 3 103 ? 115.992 -24.999 50.475  1.000 29.090  ? 103 TRP NNN C   1 
ATOM 19723 O O   . TRP N 3 103 ? 114.822 -24.661 50.291  1.000 27.280  ? 103 TRP NNN O   1 
ATOM 19724 C CB  . TRP N 3 103 ? 117.061 -26.115 48.511  1.000 27.190  ? 103 TRP NNN CB  1 
ATOM 19725 C CG  . TRP N 3 103 ? 117.544 -25.935 47.110  1.000 26.580  ? 103 TRP NNN CG  1 
ATOM 19726 C CD1 . TRP N 3 103 ? 118.795 -26.179 46.631  1.000 26.050  ? 103 TRP NNN CD1 1 
ATOM 19727 C CD2 . TRP N 3 103 ? 116.761 -25.488 45.995  1.000 25.200  ? 103 TRP NNN CD2 1 
ATOM 19728 N NE1 . TRP N 3 103 ? 118.844 -25.906 45.293  1.000 24.520  ? 103 TRP NNN NE1 1 
ATOM 19729 C CE2 . TRP N 3 103 ? 117.612 -25.481 44.875  1.000 23.880  ? 103 TRP NNN CE2 1 
ATOM 19730 C CE3 . TRP N 3 103 ? 115.431 -25.093 45.836  1.000 24.490  ? 103 TRP NNN CE3 1 
ATOM 19731 C CZ2 . TRP N 3 103 ? 117.172 -25.094 43.614  1.000 22.210  ? 103 TRP NNN CZ2 1 
ATOM 19732 C CZ3 . TRP N 3 103 ? 114.998 -24.712 44.590  1.000 22.590  ? 103 TRP NNN CZ3 1 
ATOM 19733 C CH2 . TRP N 3 103 ? 115.860 -24.705 43.497  1.000 22.270  ? 103 TRP NNN CH2 1 
ATOM 19734 N N   . ASN N 3 104 ? 116.486 -25.507 51.601  1.000 30.600  ? 104 ASN NNN N   1 
ATOM 19735 C CA  . ASN N 3 104 ? 115.659 -25.734 52.818  1.000 35.230  ? 104 ASN NNN CA  1 
ATOM 19736 C C   . ASN N 3 104 ? 114.732 -26.919 52.552  1.000 33.880  ? 104 ASN NNN C   1 
ATOM 19737 O O   . ASN N 3 104 ? 115.130 -27.774 51.771  1.000 36.220  ? 104 ASN NNN O   1 
ATOM 19738 C CB  . ASN N 3 104 ? 115.105 -24.438 53.412  1.000 41.090  ? 104 ASN NNN CB  1 
ATOM 19739 C CG  . ASN N 3 104 ? 116.152 -23.374 53.654  1.000 44.010  ? 104 ASN NNN CG  1 
ATOM 19740 O OD1 . ASN N 3 104 ? 116.013 -22.251 53.184  1.000 38.200  ? 104 ASN NNN OD1 1 
ATOM 19741 N ND2 . ASN N 3 104 ? 117.192 -23.712 54.397  1.000 42.290  ? 104 ASN NNN ND2 1 
ATOM 19742 N N   . VAL N 3 105 ? 113.565 -26.989 53.181  1.000 35.430  ? 105 VAL NNN N   1 
ATOM 19743 C CA  . VAL N 3 105 ? 112.627 -28.104 52.843  1.000 34.140  ? 105 VAL NNN CA  1 
ATOM 19744 C C   . VAL N 3 105 ? 112.151 -27.849 51.415  1.000 33.660  ? 105 VAL NNN C   1 
ATOM 19745 O O   . VAL N 3 105 ? 111.580 -26.748 51.192  1.000 36.060  ? 105 VAL NNN O   1 
ATOM 19746 C CB  . VAL N 3 105 ? 111.471 -28.207 53.855  1.000 34.090  ? 105 VAL NNN CB  1 
ATOM 19747 C CG1 . VAL N 3 105 ? 110.326 -29.068 53.354  1.000 34.180  ? 105 VAL NNN CG1 1 
ATOM 19748 C CG2 . VAL N 3 105 ? 111.973 -28.745 55.181  1.000 35.930  ? 105 VAL NNN CG2 1 
ATOM 19749 N N   . ASP N 3 106 ? 112.396 -28.794 50.486  1.000 30.070  ? 106 ASP NNN N   1 
ATOM 19750 C CA  . ASP N 3 106 ? 112.103 -28.620 49.039  1.000 27.140  ? 106 ASP NNN CA  1 
ATOM 19751 C C   . ASP N 3 106 ? 111.080 -29.651 48.542  1.000 26.540  ? 106 ASP NNN C   1 
ATOM 19752 O O   . ASP N 3 106 ? 109.976 -29.240 48.152  1.000 29.620  ? 106 ASP NNN O   1 
ATOM 19753 C CB  . ASP N 3 106 ? 113.394 -28.566 48.214  1.000 26.350  ? 106 ASP NNN CB  1 
ATOM 19754 C CG  . ASP N 3 106 ? 114.349 -29.741 48.311  1.000 26.940  ? 106 ASP NNN CG  1 
ATOM 19755 O OD1 . ASP N 3 106 ? 113.998 -30.763 48.899  1.000 29.640  ? 106 ASP NNN OD1 1 
ATOM 19756 O OD2 . ASP N 3 106 ? 115.437 -29.619 47.764  1.000 26.320  ? 106 ASP NNN OD2 1 
ATOM 19757 N N   . TYR N 3 107 ? 111.433 -30.925 48.484  1.000 27.220  ? 107 TYR NNN N   1 
ATOM 19758 C CA  . TYR N 3 107 ? 110.582 -31.979 47.885  1.000 29.850  ? 107 TYR NNN CA  1 
ATOM 19759 C C   . TYR N 3 107 ? 109.777 -32.663 48.980  1.000 33.030  ? 107 TYR NNN C   1 
ATOM 19760 O O   . TYR N 3 107 ? 110.328 -32.929 50.057  1.000 37.930  ? 107 TYR NNN O   1 
ATOM 19761 C CB  . TYR N 3 107 ? 111.427 -33.007 47.146  1.000 32.020  ? 107 TYR NNN CB  1 
ATOM 19762 C CG  . TYR N 3 107 ? 112.024 -32.489 45.869  1.000 33.010  ? 107 TYR NNN CG  1 
ATOM 19763 C CD1 . TYR N 3 107 ? 111.253 -32.378 44.731  1.000 33.930  ? 107 TYR NNN CD1 1 
ATOM 19764 C CD2 . TYR N 3 107 ? 113.356 -32.122 45.798  1.000 35.370  ? 107 TYR NNN CD2 1 
ATOM 19765 C CE1 . TYR N 3 107 ? 111.780 -31.896 43.547  1.000 35.470  ? 107 TYR NNN CE1 1 
ATOM 19766 C CE2 . TYR N 3 107 ? 113.906 -31.655 44.614  1.000 37.120  ? 107 TYR NNN CE2 1 
ATOM 19767 C CZ  . TYR N 3 107 ? 113.110 -31.544 43.487  1.000 35.030  ? 107 TYR NNN CZ  1 
ATOM 19768 O OH  . TYR N 3 107 ? 113.595 -31.055 42.321  1.000 33.740  ? 107 TYR NNN OH  1 
ATOM 19769 N N   . TRP N 3 108 ? 108.506 -32.929 48.675  1.000 36.170  ? 108 TRP NNN N   1 
ATOM 19770 C CA  . TRP N 3 108 ? 107.532 -33.657 49.527  1.000 34.700  ? 108 TRP NNN CA  1 
ATOM 19771 C C   . TRP N 3 108 ? 107.078 -34.920 48.787  1.000 34.160  ? 108 TRP NNN C   1 
ATOM 19772 O O   . TRP N 3 108 ? 107.082 -34.924 47.566  1.000 32.920  ? 108 TRP NNN O   1 
ATOM 19773 C CB  . TRP N 3 108 ? 106.340 -32.758 49.863  1.000 34.830  ? 108 TRP NNN CB  1 
ATOM 19774 C CG  . TRP N 3 108 ? 106.671 -31.510 50.619  1.000 35.780  ? 108 TRP NNN CG  1 
ATOM 19775 C CD1 . TRP N 3 108 ? 107.435 -30.474 50.191  1.000 37.460  ? 108 TRP NNN CD1 1 
ATOM 19776 C CD2 . TRP N 3 108 ? 106.196 -31.133 51.924  1.000 39.980  ? 108 TRP NNN CD2 1 
ATOM 19777 N NE1 . TRP N 3 108 ? 107.475 -29.485 51.133  1.000 39.890  ? 108 TRP NNN NE1 1 
ATOM 19778 C CE2 . TRP N 3 108 ? 106.719 -29.859 52.209  1.000 38.810  ? 108 TRP NNN CE2 1 
ATOM 19779 C CE3 . TRP N 3 108 ? 105.366 -31.734 52.875  1.000 44.020  ? 108 TRP NNN CE3 1 
ATOM 19780 C CZ2 . TRP N 3 108 ? 106.482 -29.201 53.411  1.000 39.090  ? 108 TRP NNN CZ2 1 
ATOM 19781 C CZ3 . TRP N 3 108 ? 105.118 -31.084 54.059  1.000 42.520  ? 108 TRP NNN CZ3 1 
ATOM 19782 C CH2 . TRP N 3 108 ? 105.689 -29.843 54.332  1.000 40.390  ? 108 TRP NNN CH2 1 
ATOM 19783 N N   . GLY N 3 109 ? 106.697 -35.963 49.518  1.000 38.920  ? 109 GLY NNN N   1 
ATOM 19784 C CA  . GLY N 3 109 ? 106.035 -37.164 48.971  1.000 41.530  ? 109 GLY NNN CA  1 
ATOM 19785 C C   . GLY N 3 109 ? 104.550 -36.903 48.837  1.000 46.190  ? 109 GLY NNN C   1 
ATOM 19786 O O   . GLY N 3 109 ? 104.135 -35.718 49.083  1.000 45.450  ? 109 GLY NNN O   1 
ATOM 19787 N N   . GLN N 3 110 ? 103.766 -37.933 48.480  1.000 48.220  ? 110 GLN NNN N   1 
ATOM 19788 C CA  . GLN N 3 110 ? 102.314 -37.780 48.187  1.000 52.180  ? 110 GLN NNN CA  1 
ATOM 19789 C C   . GLN N 3 110 ? 101.554 -37.751 49.515  1.000 49.820  ? 110 GLN NNN C   1 
ATOM 19790 O O   . GLN N 3 110 ? 100.399 -37.278 49.539  1.000 36.670  ? 110 GLN NNN O   1 
ATOM 19791 C CB  . GLN N 3 110 ? 101.807 -38.889 47.269  1.000 58.650  ? 110 GLN NNN CB  1 
ATOM 19792 C CG  . GLN N 3 110 ? 101.812 -40.280 47.884  1.000 72.500  ? 110 GLN NNN CG  1 
ATOM 19793 C CD  . GLN N 3 110 ? 103.146 -40.986 47.838  1.000 81.410  ? 110 GLN NNN CD  1 
ATOM 19794 O OE1 . GLN N 3 110 ? 104.050 -40.617 47.078  1.000 91.020  ? 110 GLN NNN OE1 1 
ATOM 19795 N NE2 . GLN N 3 110 ? 103.265 -42.012 48.669  1.000 77.310  ? 110 GLN NNN NE2 1 
ATOM 19796 N N   . GLY N 3 111 ? 102.206 -38.236 50.576  1.000 56.590  ? 111 GLY NNN N   1 
ATOM 19797 C CA  . GLY N 3 111 ? 101.609 -38.393 51.918  1.000 56.990  ? 111 GLY NNN CA  1 
ATOM 19798 C C   . GLY N 3 111 ? 100.906 -39.732 52.035  1.000 52.550  ? 111 GLY NNN C   1 
ATOM 19799 O O   . GLY N 3 111 ? 100.518 -40.285 50.990  1.000 52.700  ? 111 GLY NNN O   1 
ATOM 19800 N N   . THR N 3 112 ? 100.781 -40.245 53.256  1.000 51.290  ? 112 THR NNN N   1 
ATOM 19801 C CA  . THR N 3 112 ? 100.050 -41.495 53.584  1.000 50.540  ? 112 THR NNN CA  1 
ATOM 19802 C C   . THR N 3 112 ? 99.114  -41.204 54.751  1.000 46.510  ? 112 THR NNN C   1 
ATOM 19803 O O   . THR N 3 112 ? 99.551  -40.532 55.686  1.000 42.080  ? 112 THR NNN O   1 
ATOM 19804 C CB  . THR N 3 112 ? 101.004 -42.647 53.901  1.000 49.940  ? 112 THR NNN CB  1 
ATOM 19805 O OG1 . THR N 3 112 ? 100.215 -43.826 53.996  1.000 56.290  ? 112 THR NNN OG1 1 
ATOM 19806 C CG2 . THR N 3 112 ? 101.751 -42.487 55.202  1.000 52.940  ? 112 THR NNN CG2 1 
ATOM 19807 N N   . LEU N 3 113 ? 97.871  -41.675 54.686  1.000 48.720  ? 113 LEU NNN N   1 
ATOM 19808 C CA  . LEU N 3 113 ? 96.856  -41.314 55.709  1.000 51.620  ? 113 LEU NNN CA  1 
ATOM 19809 C C   . LEU N 3 113 ? 97.000  -42.241 56.914  1.000 53.600  ? 113 LEU NNN C   1 
ATOM 19810 O O   . LEU N 3 113 ? 97.016  -43.490 56.706  1.000 56.840  ? 113 LEU NNN O   1 
ATOM 19811 C CB  . LEU N 3 113 ? 95.442  -41.419 55.140  1.000 52.210  ? 113 LEU NNN CB  1 
ATOM 19812 C CG  . LEU N 3 113 ? 94.351  -41.047 56.142  1.000 55.160  ? 113 LEU NNN CG  1 
ATOM 19813 C CD1 . LEU N 3 113 ? 94.611  -39.669 56.730  1.000 54.260  ? 113 LEU NNN CD1 1 
ATOM 19814 C CD2 . LEU N 3 113 ? 92.966  -41.070 55.505  1.000 56.910  ? 113 LEU NNN CD2 1 
ATOM 19815 N N   . VAL N 3 114 ? 97.106  -41.649 58.108  1.000 51.850  ? 114 VAL NNN N   1 
ATOM 19816 C CA  . VAL N 3 114 ? 97.018  -42.365 59.411  1.000 54.800  ? 114 VAL NNN CA  1 
ATOM 19817 C C   . VAL N 3 114 ? 95.742  -41.888 60.097  1.000 55.000  ? 114 VAL NNN C   1 
ATOM 19818 O O   . VAL N 3 114 ? 95.714  -40.700 60.510  1.000 44.750  ? 114 VAL NNN O   1 
ATOM 19819 C CB  . VAL N 3 114 ? 98.257  -42.124 60.295  1.000 56.210  ? 114 VAL NNN CB  1 
ATOM 19820 C CG1 . VAL N 3 114 ? 98.039  -42.604 61.719  1.000 58.070  ? 114 VAL NNN CG1 1 
ATOM 19821 C CG2 . VAL N 3 114 ? 99.485  -42.808 59.728  1.000 56.630  ? 114 VAL NNN CG2 1 
ATOM 19822 N N   . THR N 3 115 ? 94.747  -42.779 60.226  1.000 61.890  ? 115 THR NNN N   1 
ATOM 19823 C CA  . THR N 3 115 ? 93.512  -42.519 61.001  1.000 63.780  ? 115 THR NNN CA  1 
ATOM 19824 C C   . THR N 3 115 ? 93.542  -43.360 62.275  1.000 69.650  ? 115 THR NNN C   1 
ATOM 19825 O O   . THR N 3 115 ? 93.547  -44.605 62.153  1.000 73.060  ? 115 THR NNN O   1 
ATOM 19826 C CB  . THR N 3 115 ? 92.252  -42.771 60.174  1.000 59.600  ? 115 THR NNN CB  1 
ATOM 19827 O OG1 . THR N 3 115 ? 92.556  -42.368 58.841  1.000 56.500  ? 115 THR NNN OG1 1 
ATOM 19828 C CG2 . THR N 3 115 ? 91.063  -41.994 60.690  1.000 59.390  ? 115 THR NNN CG2 1 
ATOM 19829 N N   . VAL N 3 116 ? 93.565  -42.697 63.435  1.000 72.760  ? 116 VAL NNN N   1 
ATOM 19830 C CA  . VAL N 3 116 ? 93.503  -43.339 64.778  1.000 76.230  ? 116 VAL NNN CA  1 
ATOM 19831 C C   . VAL N 3 116 ? 92.133  -43.041 65.401  1.000 75.500  ? 116 VAL NNN C   1 
ATOM 19832 O O   . VAL N 3 116 ? 91.903  -41.911 65.837  1.000 69.070  ? 116 VAL NNN O   1 
ATOM 19833 C CB  . VAL N 3 116 ? 94.706  -42.963 65.676  1.000 81.520  ? 116 VAL NNN CB  1 
ATOM 19834 C CG1 . VAL N 3 116 ? 95.008  -41.488 65.743  1.000 80.330  ? 116 VAL NNN CG1 1 
ATOM 19835 C CG2 . VAL N 3 116 ? 94.641  -43.648 67.036  1.000 87.450  ? 116 VAL NNN CG2 1 
ATOM 19836 N N   . SER N 3 117 ? 91.281  -44.064 65.439  1.000 83.240  ? 117 SER NNN N   1 
ATOM 19837 C CA  . SER N 3 117 ? 89.867  -44.048 65.903  1.000 81.680  ? 117 SER NNN CA  1 
ATOM 19838 C C   . SER N 3 117 ? 89.479  -45.441 66.421  1.000 84.510  ? 117 SER NNN C   1 
ATOM 19839 O O   . SER N 3 117 ? 90.195  -46.398 66.150  1.000 86.480  ? 117 SER NNN O   1 
ATOM 19840 C CB  . SER N 3 117 ? 88.934  -43.679 64.795  1.000 75.990  ? 117 SER NNN CB  1 
ATOM 19841 O OG  . SER N 3 117 ? 87.623  -43.520 65.301  1.000 74.690  ? 117 SER NNN OG  1 
ATOM 19842 N N   . SER N 3 118 ? 88.260  -45.587 66.947  1.000 74.440  ? 118 SER NNN N   1 
ATOM 19843 C CA  . SER N 3 118 ? 87.739  -46.886 67.462  1.000 67.720  ? 118 SER NNN CA  1 
ATOM 19844 C C   . SER N 3 118 ? 86.842  -47.618 66.437  1.000 59.210  ? 118 SER NNN C   1 
ATOM 19845 O O   . SER N 3 118 ? 85.879  -47.169 65.803  1.000 44.810  ? 118 SER NNN O   1 
ATOM 19846 C CB  . SER N 3 118 ? 87.068  -46.628 68.764  1.000 60.610  ? 118 SER NNN CB  1 
ATOM 19847 O OG  . SER N 3 118 ? 87.727  -45.548 69.411  1.000 53.460  ? 118 SER NNN OG  1 
ATOM 19848 N N   . GLU O 3 1   ? 122.076 -17.847 3.664   1.000 49.750  ? 1   GLU YYY N   1 
ATOM 19849 C CA  . GLU O 3 1   ? 121.490 -18.684 4.719   1.000 46.200  ? 1   GLU YYY CA  1 
ATOM 19850 C C   . GLU O 3 1   ? 122.418 -19.889 4.932   1.000 43.080  ? 1   GLU YYY C   1 
ATOM 19851 O O   . GLU O 3 1   ? 123.405 -20.035 4.215   1.000 38.040  ? 1   GLU YYY O   1 
ATOM 19852 C CB  . GLU O 3 1   ? 120.055 -19.075 4.336   1.000 42.540  ? 1   GLU YYY CB  1 
ATOM 19853 N N   . VAL O 3 2   ? 122.061 -20.741 5.886   1.000 41.220  ? 2   VAL YYY N   1 
ATOM 19854 C CA  . VAL O 3 2   ? 122.592 -22.125 6.013   1.000 42.520  ? 2   VAL YYY CA  1 
ATOM 19855 C C   . VAL O 3 2   ? 121.475 -23.048 5.573   1.000 45.530  ? 2   VAL YYY C   1 
ATOM 19856 O O   . VAL O 3 2   ? 120.364 -22.929 6.115   1.000 42.970  ? 2   VAL YYY O   1 
ATOM 19857 C CB  . VAL O 3 2   ? 123.048 -22.437 7.450   1.000 43.820  ? 2   VAL YYY CB  1 
ATOM 19858 C CG1 . VAL O 3 2   ? 123.057 -23.924 7.761   1.000 42.090  ? 2   VAL YYY CG1 1 
ATOM 19859 C CG2 . VAL O 3 2   ? 124.409 -21.863 7.750   1.000 47.450  ? 2   VAL YYY CG2 1 
ATOM 19860 N N   . GLN O 3 3   ? 121.727 -23.913 4.599   1.000 52.880  ? 3   GLN YYY N   1 
ATOM 19861 C CA  . GLN O 3 3   ? 120.697 -24.831 4.059   1.000 53.290  ? 3   GLN YYY CA  1 
ATOM 19862 C C   . GLN O 3 3   ? 121.298 -26.248 4.048   1.000 46.430  ? 3   GLN YYY C   1 
ATOM 19863 O O   . GLN O 3 3   ? 122.432 -26.427 3.562   1.000 48.070  ? 3   GLN YYY O   1 
ATOM 19864 C CB  . GLN O 3 3   ? 120.233 -24.266 2.705   1.000 61.160  ? 3   GLN YYY CB  1 
ATOM 19865 C CG  . GLN O 3 3   ? 118.831 -24.655 2.248   1.000 71.460  ? 3   GLN YYY CG  1 
ATOM 19866 C CD  . GLN O 3 3   ? 118.776 -24.930 0.760   1.000 79.480  ? 3   GLN YYY CD  1 
ATOM 19867 O OE1 . GLN O 3 3   ? 119.779 -24.856 0.044   1.000 78.960  ? 3   GLN YYY OE1 1 
ATOM 19868 N NE2 . GLN O 3 3   ? 117.593 -25.278 0.291   1.000 84.830  ? 3   GLN YYY NE2 1 
ATOM 19869 N N   . LEU O 3 4   ? 120.575 -27.180 4.662   1.000 39.910  ? 4   LEU YYY N   1 
ATOM 19870 C CA  . LEU O 3 4   ? 120.855 -28.635 4.645   1.000 36.560  ? 4   LEU YYY CA  1 
ATOM 19871 C C   . LEU O 3 4   ? 119.711 -29.300 3.881   1.000 34.390  ? 4   LEU YYY C   1 
ATOM 19872 O O   . LEU O 3 4   ? 118.550 -28.930 4.133   1.000 32.760  ? 4   LEU YYY O   1 
ATOM 19873 C CB  . LEU O 3 4   ? 120.924 -29.173 6.076   1.000 35.340  ? 4   LEU YYY CB  1 
ATOM 19874 C CG  . LEU O 3 4   ? 121.945 -28.507 6.991   1.000 34.810  ? 4   LEU YYY CG  1 
ATOM 19875 C CD1 . LEU O 3 4   ? 121.783 -29.037 8.403   1.000 35.610  ? 4   LEU YYY CD1 1 
ATOM 19876 C CD2 . LEU O 3 4   ? 123.378 -28.726 6.518   1.000 36.280  ? 4   LEU YYY CD2 1 
ATOM 19877 N N   . VAL O 3 5   ? 120.030 -30.204 2.954   1.000 33.450  ? 5   VAL YYY N   1 
ATOM 19878 C CA  . VAL O 3 5   ? 119.014 -30.878 2.100   1.000 34.340  ? 5   VAL YYY CA  1 
ATOM 19879 C C   . VAL O 3 5   ? 119.272 -32.379 2.112   1.000 38.360  ? 5   VAL YYY C   1 
ATOM 19880 O O   . VAL O 3 5   ? 120.353 -32.815 1.650   1.000 42.460  ? 5   VAL YYY O   1 
ATOM 19881 C CB  . VAL O 3 5   ? 118.998 -30.336 0.669   1.000 34.320  ? 5   VAL YYY CB  1 
ATOM 19882 C CG1 . VAL O 3 5   ? 117.681 -30.677 -0.003  1.000 37.350  ? 5   VAL YYY CG1 1 
ATOM 19883 C CG2 . VAL O 3 5   ? 119.239 -28.836 0.638   1.000 36.550  ? 5   VAL YYY CG2 1 
ATOM 19884 N N   . GLU O 3 6   ? 118.295 -33.118 2.634   1.000 40.780  ? 6   GLU YYY N   1 
ATOM 19885 C CA  . GLU O 3 6   ? 118.336 -34.591 2.715   1.000 40.110  ? 6   GLU YYY CA  1 
ATOM 19886 C C   . GLU O 3 6   ? 117.737 -35.164 1.434   1.000 37.390  ? 6   GLU YYY C   1 
ATOM 19887 O O   . GLU O 3 6   ? 116.999 -34.449 0.737   1.000 36.290  ? 6   GLU YYY O   1 
ATOM 19888 C CB  . GLU O 3 6   ? 117.594 -35.084 3.959   1.000 43.090  ? 6   GLU YYY CB  1 
ATOM 19889 C CG  . GLU O 3 6   ? 118.212 -34.567 5.252   1.000 44.030  ? 6   GLU YYY CG  1 
ATOM 19890 C CD  . GLU O 3 6   ? 117.519 -33.336 5.804   1.000 45.000  ? 6   GLU YYY CD  1 
ATOM 19891 O OE1 . GLU O 3 6   ? 116.870 -32.633 5.026   1.000 50.280  ? 6   GLU YYY OE1 1 
ATOM 19892 O OE2 . GLU O 3 6   ? 117.611 -33.112 7.016   1.000 48.590  ? 6   GLU YYY OE2 1 
ATOM 19893 N N   . SER O 3 7   ? 118.055 -36.429 1.175   1.000 34.850  ? 7   SER YYY N   1 
ATOM 19894 C CA  . SER O 3 7   ? 117.650 -37.207 -0.017  1.000 33.710  ? 7   SER YYY CA  1 
ATOM 19895 C C   . SER O 3 7   ? 118.039 -38.674 0.204   1.000 34.460  ? 7   SER YYY C   1 
ATOM 19896 O O   . SER O 3 7   ? 118.903 -38.942 1.085   1.000 32.140  ? 7   SER YYY O   1 
ATOM 19897 C CB  . SER O 3 7   ? 118.282 -36.653 -1.229  1.000 31.590  ? 7   SER YYY CB  1 
ATOM 19898 O OG  . SER O 3 7   ? 119.688 -36.658 -1.064  1.000 32.920  ? 7   SER YYY OG  1 
ATOM 19899 N N   . GLY O 3 8   ? 117.428 -39.568 -0.577  1.000 33.440  ? 8   GLY YYY N   1 
ATOM 19900 C CA  . GLY O 3 8   ? 117.759 -41.002 -0.585  1.000 33.540  ? 8   GLY YYY CA  1 
ATOM 19901 C C   . GLY O 3 8   ? 116.697 -41.828 0.103   1.000 33.520  ? 8   GLY YYY C   1 
ATOM 19902 O O   . GLY O 3 8   ? 116.701 -43.067 -0.066  1.000 35.240  ? 8   GLY YYY O   1 
ATOM 19903 N N   . GLY O 3 9   ? 115.816 -41.172 0.854   1.000 33.290  ? 9   GLY YYY N   1 
ATOM 19904 C CA  . GLY O 3 9   ? 114.712 -41.822 1.584   1.000 30.970  ? 9   GLY YYY CA  1 
ATOM 19905 C C   . GLY O 3 9   ? 113.722 -42.435 0.631   1.000 29.070  ? 9   GLY YYY C   1 
ATOM 19906 O O   . GLY O 3 9   ? 113.526 -41.865 -0.433  1.000 27.970  ? 9   GLY YYY O   1 
ATOM 19907 N N   . GLY O 3 10  ? 113.123 -43.557 1.011   1.000 32.220  ? 10  GLY YYY N   1 
ATOM 19908 C CA  . GLY O 3 10  ? 112.055 -44.207 0.237   1.000 34.640  ? 10  GLY YYY CA  1 
ATOM 19909 C C   . GLY O 3 10  ? 111.513 -45.448 0.922   1.000 35.590  ? 10  GLY YYY C   1 
ATOM 19910 O O   . GLY O 3 10  ? 111.569 -45.545 2.168   1.000 38.310  ? 10  GLY YYY O   1 
ATOM 19911 N N   . LEU O 3 11  ? 110.916 -46.322 0.118   1.000 36.720  ? 11  LEU YYY N   1 
ATOM 19912 C CA  . LEU O 3 11  ? 110.185 -47.528 0.587   1.000 35.290  ? 11  LEU YYY CA  1 
ATOM 19913 C C   . LEU O 3 11  ? 111.125 -48.718 0.465   1.000 31.310  ? 11  LEU YYY C   1 
ATOM 19914 O O   . LEU O 3 11  ? 111.679 -48.895 -0.607  1.000 31.220  ? 11  LEU YYY O   1 
ATOM 19915 C CB  . LEU O 3 11  ? 108.927 -47.711 -0.263  1.000 36.400  ? 11  LEU YYY CB  1 
ATOM 19916 C CG  . LEU O 3 11  ? 107.864 -48.616 0.331   1.000 41.600  ? 11  LEU YYY CG  1 
ATOM 19917 C CD1 . LEU O 3 11  ? 106.529 -48.170 -0.215  1.000 43.170  ? 11  LEU YYY CD1 1 
ATOM 19918 C CD2 . LEU O 3 11  ? 108.072 -50.104 0.022   1.000 48.030  ? 11  LEU YYY CD2 1 
ATOM 19919 N N   . VAL O 3 12  ? 111.295 -49.489 1.533   1.000 29.920  ? 12  VAL YYY N   1 
ATOM 19920 C CA  . VAL O 3 12  ? 112.056 -50.770 1.482   1.000 33.680  ? 12  VAL YYY CA  1 
ATOM 19921 C C   . VAL O 3 12  ? 111.320 -51.788 2.353   1.000 36.080  ? 12  VAL YYY C   1 
ATOM 19922 O O   . VAL O 3 12  ? 110.626 -51.356 3.271   1.000 39.400  ? 12  VAL YYY O   1 
ATOM 19923 C CB  . VAL O 3 12  ? 113.525 -50.591 1.900   1.000 36.610  ? 12  VAL YYY CB  1 
ATOM 19924 C CG1 . VAL O 3 12  ? 114.179 -49.346 1.323   1.000 41.840  ? 12  VAL YYY CG1 1 
ATOM 19925 C CG2 . VAL O 3 12  ? 113.641 -50.588 3.399   1.000 38.910  ? 12  VAL YYY CG2 1 
ATOM 19926 N N   . LYS O 3 13  ? 111.533 -53.079 2.085   1.000 39.650  ? 13  LYS YYY N   1 
ATOM 19927 C CA  . LYS O 3 13  ? 110.992 -54.218 2.872   1.000 37.930  ? 13  LYS YYY CA  1 
ATOM 19928 C C   . LYS O 3 13  ? 111.947 -54.468 4.031   1.000 37.470  ? 13  LYS YYY C   1 
ATOM 19929 O O   . LYS O 3 13  ? 113.138 -54.216 3.904   1.000 35.540  ? 13  LYS YYY O   1 
ATOM 19930 C CB  . LYS O 3 13  ? 110.758 -55.446 1.977   1.000 37.250  ? 13  LYS YYY CB  1 
ATOM 19931 C CG  . LYS O 3 13  ? 109.464 -55.312 1.171   1.000 38.500  ? 13  LYS YYY CG  1 
ATOM 19932 C CD  . LYS O 3 13  ? 108.998 -56.474 0.318   1.000 37.440  ? 13  LYS YYY CD  1 
ATOM 19933 C CE  . LYS O 3 13  ? 107.972 -55.983 -0.683  1.000 36.840  ? 13  LYS YYY CE  1 
ATOM 19934 N NZ  . LYS O 3 13  ? 108.071 -56.682 -1.985  1.000 38.060  ? 13  LYS YYY NZ  1 
ATOM 19935 N N   . PRO O 3 14  ? 111.446 -54.933 5.197   1.000 36.200  ? 14  PRO YYY N   1 
ATOM 19936 C CA  . PRO O 3 14  ? 112.299 -55.341 6.295   1.000 33.920  ? 14  PRO YYY CA  1 
ATOM 19937 C C   . PRO O 3 14  ? 113.501 -56.145 5.771   1.000 33.570  ? 14  PRO YYY C   1 
ATOM 19938 O O   . PRO O 3 14  ? 113.369 -56.784 4.763   1.000 32.570  ? 14  PRO YYY O   1 
ATOM 19939 C CB  . PRO O 3 14  ? 111.395 -56.223 7.154   1.000 36.160  ? 14  PRO YYY CB  1 
ATOM 19940 C CG  . PRO O 3 14  ? 109.992 -55.695 6.908   1.000 36.370  ? 14  PRO YYY CG  1 
ATOM 19941 C CD  . PRO O 3 14  ? 110.022 -55.070 5.533   1.000 35.960  ? 14  PRO YYY CD  1 
ATOM 19942 N N   . GLY O 3 15  ? 114.620 -56.072 6.471   1.000 36.100  ? 15  GLY YYY N   1 
ATOM 19943 C CA  . GLY O 3 15  ? 115.906 -56.648 6.037   1.000 38.400  ? 15  GLY YYY CA  1 
ATOM 19944 C C   . GLY O 3 15  ? 116.511 -55.868 4.878   1.000 41.380  ? 15  GLY YYY C   1 
ATOM 19945 O O   . GLY O 3 15  ? 117.619 -56.187 4.453   1.000 45.580  ? 15  GLY YYY O   1 
ATOM 19946 N N   . GLY O 3 16  ? 115.807 -54.832 4.408   1.000 44.760  ? 16  GLY YYY N   1 
ATOM 19947 C CA  . GLY O 3 16  ? 116.234 -53.947 3.302   1.000 45.760  ? 16  GLY YYY CA  1 
ATOM 19948 C C   . GLY O 3 16  ? 117.419 -53.078 3.679   1.000 45.700  ? 16  GLY YYY C   1 
ATOM 19949 O O   . GLY O 3 16  ? 117.876 -53.152 4.848   1.000 46.830  ? 16  GLY YYY O   1 
ATOM 19950 N N   . SER O 3 17  ? 117.897 -52.278 2.731   1.000 44.380  ? 17  SER YYY N   1 
ATOM 19951 C CA  . SER O 3 17  ? 119.054 -51.361 2.885   1.000 43.190  ? 17  SER YYY CA  1 
ATOM 19952 C C   . SER O 3 17  ? 118.705 -50.037 2.197   1.000 46.930  ? 17  SER YYY C   1 
ATOM 19953 O O   . SER O 3 17  ? 117.717 -50.007 1.436   1.000 47.630  ? 17  SER YYY O   1 
ATOM 19954 C CB  . SER O 3 17  ? 120.311 -51.979 2.348   1.000 41.580  ? 17  SER YYY CB  1 
ATOM 19955 O OG  . SER O 3 17  ? 120.317 -51.970 0.933   1.000 49.860  ? 17  SER YYY OG  1 
ATOM 19956 N N   . LEU O 3 18  ? 119.464 -48.976 2.487   1.000 49.200  ? 18  LEU YYY N   1 
ATOM 19957 C CA  . LEU O 3 18  ? 119.149 -47.586 2.062   1.000 44.710  ? 18  LEU YYY CA  1 
ATOM 19958 C C   . LEU O 3 18  ? 120.282 -46.641 2.478   1.000 38.770  ? 18  LEU YYY C   1 
ATOM 19959 O O   . LEU O 3 18  ? 120.731 -46.772 3.617   1.000 37.110  ? 18  LEU YYY O   1 
ATOM 19960 C CB  . LEU O 3 18  ? 117.821 -47.189 2.720   1.000 43.510  ? 18  LEU YYY CB  1 
ATOM 19961 C CG  . LEU O 3 18  ? 117.041 -46.075 2.042   1.000 46.640  ? 18  LEU YYY CG  1 
ATOM 19962 C CD1 . LEU O 3 18  ? 117.243 -46.055 0.543   1.000 47.040  ? 18  LEU YYY CD1 1 
ATOM 19963 C CD2 . LEU O 3 18  ? 115.567 -46.235 2.341   1.000 49.540  ? 18  LEU YYY CD2 1 
ATOM 19964 N N   . ARG O 3 19  ? 120.724 -45.751 1.590   1.000 35.510  ? 19  ARG YYY N   1 
ATOM 19965 C CA  . ARG O 3 19  ? 121.775 -44.734 1.870   1.000 36.560  ? 19  ARG YYY CA  1 
ATOM 19966 C C   . ARG O 3 19  ? 121.141 -43.344 1.761   1.000 38.920  ? 19  ARG YYY C   1 
ATOM 19967 O O   . ARG O 3 19  ? 120.589 -43.022 0.704   1.000 40.150  ? 19  ARG YYY O   1 
ATOM 19968 C CB  . ARG O 3 19  ? 122.977 -44.858 0.932   1.000 40.420  ? 19  ARG YYY CB  1 
ATOM 19969 C CG  . ARG O 3 19  ? 124.083 -43.850 1.228   1.000 44.330  ? 19  ARG YYY CG  1 
ATOM 19970 C CD  . ARG O 3 19  ? 125.094 -43.532 0.146   1.000 45.670  ? 19  ARG YYY CD  1 
ATOM 19971 N NE  . ARG O 3 19  ? 126.488 -43.589 0.642   1.000 50.820  ? 19  ARG YYY NE  1 
ATOM 19972 C CZ  . ARG O 3 19  ? 127.541 -42.908 0.167   1.000 52.130  ? 19  ARG YYY CZ  1 
ATOM 19973 N NH1 . ARG O 3 19  ? 128.733 -43.094 0.722   1.000 51.650  ? 19  ARG YYY NH1 1 
ATOM 19974 N NH2 . ARG O 3 19  ? 127.424 -42.009 -0.804  1.000 45.800  ? 19  ARG YYY NH2 1 
ATOM 19975 N N   . LEU O 3 20  ? 121.222 -42.554 2.838   1.000 38.790  ? 20  LEU YYY N   1 
ATOM 19976 C CA  . LEU O 3 20  ? 120.669 -41.181 2.935   1.000 33.020  ? 20  LEU YYY CA  1 
ATOM 19977 C C   . LEU O 3 20  ? 121.804 -40.202 2.688   1.000 32.520  ? 20  LEU YYY C   1 
ATOM 19978 O O   . LEU O 3 20  ? 122.967 -40.556 2.999   1.000 31.650  ? 20  LEU YYY O   1 
ATOM 19979 C CB  . LEU O 3 20  ? 120.045 -40.982 4.318   1.000 30.260  ? 20  LEU YYY CB  1 
ATOM 19980 C CG  . LEU O 3 20  ? 118.844 -41.872 4.618   1.000 29.900  ? 20  LEU YYY CG  1 
ATOM 19981 C CD1 . LEU O 3 20  ? 118.063 -41.389 5.816   1.000 31.050  ? 20  LEU YYY CD1 1 
ATOM 19982 C CD2 . LEU O 3 20  ? 117.938 -41.969 3.413   1.000 29.270  ? 20  LEU YYY CD2 1 
ATOM 19983 N N   . SER O 3 21  ? 121.473 -39.048 2.102   1.000 31.990  ? 21  SER YYY N   1 
ATOM 19984 C CA  . SER O 3 21  ? 122.416 -37.965 1.731   1.000 31.040  ? 21  SER YYY CA  1 
ATOM 19985 C C   . SER O 3 21  ? 121.959 -36.634 2.323   1.000 32.600  ? 21  SER YYY C   1 
ATOM 19986 O O   . SER O 3 21  ? 120.775 -36.298 2.155   1.000 36.380  ? 21  SER YYY O   1 
ATOM 19987 C CB  . SER O 3 21  ? 122.505 -37.862 0.259   1.000 31.040  ? 21  SER YYY CB  1 
ATOM 19988 O OG  . SER O 3 21  ? 123.407 -38.817 -0.226  1.000 38.840  ? 21  SER YYY OG  1 
ATOM 19989 N N   . CYS O 3 22  ? 122.862 -35.903 2.978   1.000 32.150  ? 22  CYS YYY N   1 
ATOM 19990 C CA  . CYS O 3 22  ? 122.687 -34.481 3.362   1.000 30.930  ? 22  CYS YYY CA  1 
ATOM 19991 C C   . CYS O 3 22  ? 123.634 -33.636 2.511   1.000 30.180  ? 22  CYS YYY C   1 
ATOM 19992 O O   . CYS O 3 22  ? 124.846 -33.932 2.491   1.000 31.120  ? 22  CYS YYY O   1 
ATOM 19993 C CB  . CYS O 3 22  ? 122.990 -34.232 4.832   1.000 31.850  ? 22  CYS YYY CB  1 
ATOM 19994 S SG  . CYS O 3 22  ? 122.285 -32.684 5.468   1.000 33.270  ? 22  CYS YYY SG  1 
ATOM 19995 N N   . ALA O 3 23  ? 123.093 -32.634 1.829   1.000 28.520  ? 23  ALA YYY N   1 
ATOM 19996 C CA  . ALA O 3 23  ? 123.863 -31.630 1.076   1.000 29.560  ? 23  ALA YYY CA  1 
ATOM 19997 C C   . ALA O 3 23  ? 123.872 -30.338 1.878   1.000 32.290  ? 23  ALA YYY C   1 
ATOM 19998 O O   . ALA O 3 23  ? 122.782 -29.749 2.043   1.000 37.220  ? 23  ALA YYY O   1 
ATOM 19999 C CB  . ALA O 3 23  ? 123.252 -31.427 -0.281  1.000 30.810  ? 23  ALA YYY CB  1 
ATOM 20000 N N   . ALA O 3 24  ? 125.056 -29.936 2.339   1.000 34.380  ? 24  ALA YYY N   1 
ATOM 20001 C CA  . ALA O 3 24  ? 125.300 -28.677 3.069   1.000 36.170  ? 24  ALA YYY CA  1 
ATOM 20002 C C   . ALA O 3 24  ? 125.810 -27.564 2.122   1.000 36.730  ? 24  ALA YYY C   1 
ATOM 20003 O O   . ALA O 3 24  ? 126.875 -27.739 1.468   1.000 36.370  ? 24  ALA YYY O   1 
ATOM 20004 C CB  . ALA O 3 24  ? 126.280 -28.976 4.167   1.000 35.950  ? 24  ALA YYY CB  1 
ATOM 20005 N N   . SER O 3 25  ? 125.088 -26.446 2.093   1.000 34.950  ? 25  SER YYY N   1 
ATOM 20006 C CA  . SER O 3 25  ? 125.552 -25.125 1.599   1.000 38.200  ? 25  SER YYY CA  1 
ATOM 20007 C C   . SER O 3 25  ? 125.348 -24.056 2.688   1.000 37.780  ? 25  SER YYY C   1 
ATOM 20008 O O   . SER O 3 25  ? 124.481 -24.232 3.556   1.000 43.690  ? 25  SER YYY O   1 
ATOM 20009 C CB  . SER O 3 25  ? 124.808 -24.755 0.353   1.000 42.370  ? 25  SER YYY CB  1 
ATOM 20010 O OG  . SER O 3 25  ? 123.417 -24.611 0.625   1.000 45.980  ? 25  SER YYY OG  1 
ATOM 20011 N N   . GLY O 3 26  ? 126.106 -22.971 2.635   1.000 35.870  ? 26  GLY YYY N   1 
ATOM 20012 C CA  . GLY O 3 26  ? 125.889 -21.793 3.488   1.000 33.310  ? 26  GLY YYY CA  1 
ATOM 20013 C C   . GLY O 3 26  ? 126.975 -21.599 4.524   1.000 30.930  ? 26  GLY YYY C   1 
ATOM 20014 O O   . GLY O 3 26  ? 126.918 -20.594 5.234   1.000 32.500  ? 26  GLY YYY O   1 
ATOM 20015 N N   . PHE O 3 27  ? 127.930 -22.515 4.626   1.000 28.300  ? 27  PHE YYY N   1 
ATOM 20016 C CA  . PHE O 3 27  ? 128.919 -22.561 5.721   1.000 26.440  ? 27  PHE YYY CA  1 
ATOM 20017 C C   . PHE O 3 27  ? 130.010 -23.567 5.395   1.000 26.450  ? 27  PHE YYY C   1 
ATOM 20018 O O   . PHE O 3 27  ? 129.754 -24.452 4.615   1.000 31.000  ? 27  PHE YYY O   1 
ATOM 20019 C CB  . PHE O 3 27  ? 128.220 -22.977 7.016   1.000 26.320  ? 27  PHE YYY CB  1 
ATOM 20020 C CG  . PHE O 3 27  ? 127.731 -24.403 7.097   1.000 23.680  ? 27  PHE YYY CG  1 
ATOM 20021 C CD1 . PHE O 3 27  ? 126.556 -24.768 6.470   1.000 24.250  ? 27  PHE YYY CD1 1 
ATOM 20022 C CD2 . PHE O 3 27  ? 128.390 -25.347 7.859   1.000 21.180  ? 27  PHE YYY CD2 1 
ATOM 20023 C CE1 . PHE O 3 27  ? 126.065 -26.060 6.579   1.000 24.200  ? 27  PHE YYY CE1 1 
ATOM 20024 C CE2 . PHE O 3 27  ? 127.906 -26.636 7.963   1.000 21.750  ? 27  PHE YYY CE2 1 
ATOM 20025 C CZ  . PHE O 3 27  ? 126.738 -26.995 7.331   1.000 22.880  ? 27  PHE YYY CZ  1 
ATOM 20026 N N   . THR O 3 28  ? 131.150 -23.463 6.044   1.000 26.030  ? 28  THR YYY N   1 
ATOM 20027 C CA  . THR O 3 28  ? 132.272 -24.427 5.934   1.000 24.170  ? 28  THR YYY CA  1 
ATOM 20028 C C   . THR O 3 28  ? 131.847 -25.745 6.583   1.000 23.570  ? 28  THR YYY C   1 
ATOM 20029 O O   . THR O 3 28  ? 132.268 -26.040 7.701   1.000 24.890  ? 28  THR YYY O   1 
ATOM 20030 C CB  . THR O 3 28  ? 133.532 -23.877 6.599   1.000 24.820  ? 28  THR YYY CB  1 
ATOM 20031 O OG1 . THR O 3 28  ? 133.811 -22.624 5.993   1.000 24.030  ? 28  THR YYY OG1 1 
ATOM 20032 C CG2 . THR O 3 28  ? 134.728 -24.790 6.436   1.000 27.660  ? 28  THR YYY CG2 1 
ATOM 20033 N N   . PHE O 3 29  ? 130.996 -26.499 5.919   1.000 23.150  ? 29  PHE YYY N   1 
ATOM 20034 C CA  . PHE O 3 29  ? 130.610 -27.886 6.294   1.000 23.790  ? 29  PHE YYY CA  1 
ATOM 20035 C C   . PHE O 3 29  ? 131.739 -28.693 6.927   1.000 21.500  ? 29  PHE YYY C   1 
ATOM 20036 O O   . PHE O 3 29  ? 131.491 -29.410 7.892   1.000 23.030  ? 29  PHE YYY O   1 
ATOM 20037 C CB  . PHE O 3 29  ? 130.213 -28.657 5.045   1.000 26.020  ? 29  PHE YYY CB  1 
ATOM 20038 C CG  . PHE O 3 29  ? 129.847 -30.092 5.319   1.000 25.430  ? 29  PHE YYY CG  1 
ATOM 20039 C CD1 . PHE O 3 29  ? 128.656 -30.409 5.975   1.000 24.380  ? 29  PHE YYY CD1 1 
ATOM 20040 C CD2 . PHE O 3 29  ? 130.722 -31.105 5.001   1.000 25.620  ? 29  PHE YYY CD2 1 
ATOM 20041 C CE1 . PHE O 3 29  ? 128.332 -31.715 6.262   1.000 23.140  ? 29  PHE YYY CE1 1 
ATOM 20042 C CE2 . PHE O 3 29  ? 130.388 -32.420 5.268   1.000 25.640  ? 29  PHE YYY CE2 1 
ATOM 20043 C CZ  . PHE O 3 29  ? 129.187 -32.716 5.896   1.000 24.530  ? 29  PHE YYY CZ  1 
ATOM 20044 N N   . SER O 3 30  ? 132.926 -28.582 6.362   1.000 21.190  ? 30  SER YYY N   1 
ATOM 20045 C CA  . SER O 3 30  ? 134.120 -29.341 6.791   1.000 22.960  ? 30  SER YYY CA  1 
ATOM 20046 C C   . SER O 3 30  ? 134.584 -28.938 8.197   1.000 24.340  ? 30  SER YYY C   1 
ATOM 20047 O O   . SER O 3 30  ? 135.586 -29.536 8.674   1.000 28.250  ? 30  SER YYY O   1 
ATOM 20048 C CB  . SER O 3 30  ? 135.242 -29.156 5.799   1.000 23.910  ? 30  SER YYY CB  1 
ATOM 20049 O OG  . SER O 3 30  ? 135.770 -27.837 5.895   1.000 24.050  ? 30  SER YYY OG  1 
ATOM 20050 N N   . SER O 3 31  ? 133.919 -27.970 8.842   1.000 24.580  ? 31  SER YYY N   1 
ATOM 20051 C CA  . SER O 3 31  ? 134.353 -27.377 10.140  1.000 23.800  ? 31  SER YYY CA  1 
ATOM 20052 C C   . SER O 3 31  ? 133.516 -27.886 11.307  1.000 23.020  ? 31  SER YYY C   1 
ATOM 20053 O O   . SER O 3 31  ? 133.985 -27.727 12.426  1.000 25.640  ? 31  SER YYY O   1 
ATOM 20054 C CB  . SER O 3 31  ? 134.354 -25.862 10.094  1.000 22.910  ? 31  SER YYY CB  1 
ATOM 20055 O OG  . SER O 3 31  ? 135.449 -25.394 9.320   1.000 22.130  ? 31  SER YYY OG  1 
ATOM 20056 N N   . TYR O 3 32  ? 132.364 -28.505 11.042  1.000 23.940  ? 32  TYR YYY N   1 
ATOM 20057 C CA  . TYR O 3 32  ? 131.308 -28.776 12.053  1.000 25.800  ? 32  TYR YYY CA  1 
ATOM 20058 C C   . TYR O 3 32  ? 131.047 -30.272 12.206  1.000 25.000  ? 32  TYR YYY C   1 
ATOM 20059 O O   . TYR O 3 32  ? 131.004 -30.984 11.201  1.000 22.340  ? 32  TYR YYY O   1 
ATOM 20060 C CB  . TYR O 3 32  ? 130.033 -28.057 11.642  1.000 28.200  ? 32  TYR YYY CB  1 
ATOM 20061 C CG  . TYR O 3 32  ? 130.188 -26.564 11.636  1.000 31.970  ? 32  TYR YYY CG  1 
ATOM 20062 C CD1 . TYR O 3 32  ? 130.785 -25.915 10.581  1.000 33.470  ? 32  TYR YYY CD1 1 
ATOM 20063 C CD2 . TYR O 3 32  ? 129.766 -25.805 12.711  1.000 37.600  ? 32  TYR YYY CD2 1 
ATOM 20064 C CE1 . TYR O 3 32  ? 130.918 -24.537 10.578  1.000 39.620  ? 32  TYR YYY CE1 1 
ATOM 20065 C CE2 . TYR O 3 32  ? 129.897 -24.427 12.726  1.000 38.550  ? 32  TYR YYY CE2 1 
ATOM 20066 C CZ  . TYR O 3 32  ? 130.473 -23.784 11.649  1.000 39.030  ? 32  TYR YYY CZ  1 
ATOM 20067 O OH  . TYR O 3 32  ? 130.616 -22.424 11.633  1.000 39.580  ? 32  TYR YYY OH  1 
ATOM 20068 N N   . THR O 3 33  ? 130.843 -30.733 13.443  1.000 25.640  ? 33  THR YYY N   1 
ATOM 20069 C CA  . THR O 3 33  ? 130.262 -32.083 13.669  1.000 24.100  ? 33  THR YYY CA  1 
ATOM 20070 C C   . THR O 3 33  ? 128.805 -32.039 13.185  1.000 24.350  ? 33  THR YYY C   1 
ATOM 20071 O O   . THR O 3 33  ? 128.159 -30.994 13.263  1.000 22.150  ? 33  THR YYY O   1 
ATOM 20072 C CB  . THR O 3 33  ? 130.556 -32.621 15.064  1.000 22.070  ? 33  THR YYY CB  1 
ATOM 20073 O OG1 . THR O 3 33  ? 129.521 -32.104 15.862  1.000 21.020  ? 33  THR YYY OG1 1 
ATOM 20074 C CG2 . THR O 3 33  ? 131.914 -32.199 15.575  1.000 22.720  ? 33  THR YYY CG2 1 
ATOM 20075 N N   . MET O 3 34  ? 128.350 -33.143 12.603  1.000 26.590  ? 34  MET YYY N   1 
ATOM 20076 C CA  . MET O 3 34  ? 127.031 -33.250 11.931  1.000 27.080  ? 34  MET YYY CA  1 
ATOM 20077 C C   . MET O 3 34  ? 126.292 -34.463 12.508  1.000 26.600  ? 34  MET YYY C   1 
ATOM 20078 O O   . MET O 3 34  ? 126.958 -35.419 12.939  1.000 25.680  ? 34  MET YYY O   1 
ATOM 20079 C CB  . MET O 3 34  ? 127.199 -33.394 10.420  1.000 27.790  ? 34  MET YYY CB  1 
ATOM 20080 C CG  . MET O 3 34  ? 127.769 -32.148 9.753   1.000 29.840  ? 34  MET YYY CG  1 
ATOM 20081 S SD  . MET O 3 34  ? 126.669 -30.675 9.747   1.000 31.680  ? 34  MET YYY SD  1 
ATOM 20082 C CE  . MET O 3 34  ? 125.175 -31.384 9.044   1.000 31.070  ? 34  MET YYY CE  1 
ATOM 20083 N N   . ASN O 3 35  ? 124.961 -34.396 12.525  1.000 26.200  ? 35  ASN YYY N   1 
ATOM 20084 C CA  . ASN O 3 35  ? 124.080 -35.357 13.228  1.000 27.790  ? 35  ASN YYY CA  1 
ATOM 20085 C C   . ASN O 3 35  ? 122.993 -35.859 12.277  1.000 29.360  ? 35  ASN YYY C   1 
ATOM 20086 O O   . ASN O 3 35  ? 122.614 -35.127 11.336  1.000 31.670  ? 35  ASN YYY O   1 
ATOM 20087 C CB  . ASN O 3 35  ? 123.482 -34.723 14.491  1.000 28.290  ? 35  ASN YYY CB  1 
ATOM 20088 C CG  . ASN O 3 35  ? 124.485 -34.617 15.623  1.000 27.520  ? 35  ASN YYY CG  1 
ATOM 20089 O OD1 . ASN O 3 35  ? 124.668 -35.530 16.413  1.000 26.690  ? 35  ASN YYY OD1 1 
ATOM 20090 N ND2 . ASN O 3 35  ? 125.149 -33.493 15.710  1.000 28.590  ? 35  ASN YYY ND2 1 
ATOM 20091 N N   . TRP O 3 36  ? 122.513 -37.081 12.521  1.000 30.710  ? 36  TRP YYY N   1 
ATOM 20092 C CA  . TRP O 3 36  ? 121.213 -37.601 12.004  1.000 30.470  ? 36  TRP YYY CA  1 
ATOM 20093 C C   . TRP O 3 36  ? 120.271 -37.742 13.205  1.000 30.190  ? 36  TRP YYY C   1 
ATOM 20094 O O   . TRP O 3 36  ? 120.700 -38.326 14.217  1.000 29.760  ? 36  TRP YYY O   1 
ATOM 20095 C CB  . TRP O 3 36  ? 121.383 -38.937 11.259  1.000 28.740  ? 36  TRP YYY CB  1 
ATOM 20096 C CG  . TRP O 3 36  ? 122.107 -38.836 9.955   1.000 26.960  ? 36  TRP YYY CG  1 
ATOM 20097 C CD1 . TRP O 3 36  ? 123.417 -39.116 9.715   1.000 26.630  ? 36  TRP YYY CD1 1 
ATOM 20098 C CD2 . TRP O 3 36  ? 121.570 -38.393 8.702   1.000 27.110  ? 36  TRP YYY CD2 1 
ATOM 20099 N NE1 . TRP O 3 36  ? 123.732 -38.881 8.405   1.000 25.720  ? 36  TRP YYY NE1 1 
ATOM 20100 C CE2 . TRP O 3 36  ? 122.618 -38.436 7.760   1.000 25.860  ? 36  TRP YYY CE2 1 
ATOM 20101 C CE3 . TRP O 3 36  ? 120.305 -37.965 8.282   1.000 27.550  ? 36  TRP YYY CE3 1 
ATOM 20102 C CZ2 . TRP O 3 36  ? 122.436 -38.072 6.431   1.000 26.040  ? 36  TRP YYY CZ2 1 
ATOM 20103 C CZ3 . TRP O 3 36  ? 120.123 -37.604 6.966   1.000 25.190  ? 36  TRP YYY CZ3 1 
ATOM 20104 C CH2 . TRP O 3 36  ? 121.173 -37.659 6.058   1.000 25.670  ? 36  TRP YYY CH2 1 
ATOM 20105 N N   . VAL O 3 37  ? 119.066 -37.196 13.106  1.000 31.330  ? 37  VAL YYY N   1 
ATOM 20106 C CA  . VAL O 3 37  ? 117.984 -37.366 14.114  1.000 33.500  ? 37  VAL YYY CA  1 
ATOM 20107 C C   . VAL O 3 37  ? 116.740 -37.798 13.345  1.000 33.510  ? 37  VAL YYY C   1 
ATOM 20108 O O   . VAL O 3 37  ? 116.514 -37.244 12.250  1.000 33.410  ? 37  VAL YYY O   1 
ATOM 20109 C CB  . VAL O 3 37  ? 117.729 -36.058 14.889  1.000 36.760  ? 37  VAL YYY CB  1 
ATOM 20110 C CG1 . VAL O 3 37  ? 116.593 -36.199 15.891  1.000 40.910  ? 37  VAL YYY CG1 1 
ATOM 20111 C CG2 . VAL O 3 37  ? 118.974 -35.551 15.592  1.000 36.870  ? 37  VAL YYY CG2 1 
ATOM 20112 N N   . ARG O 3 38  ? 115.964 -38.744 13.878  1.000 33.010  ? 38  ARG YYY N   1 
ATOM 20113 C CA  . ARG O 3 38  ? 114.771 -39.265 13.158  1.000 34.340  ? 38  ARG YYY CA  1 
ATOM 20114 C C   . ARG O 3 38  ? 113.519 -39.067 13.996  1.000 30.390  ? 38  ARG YYY C   1 
ATOM 20115 O O   . ARG O 3 38  ? 113.652 -38.916 15.221  1.000 28.600  ? 38  ARG YYY O   1 
ATOM 20116 C CB  . ARG O 3 38  ? 114.924 -40.743 12.798  1.000 38.420  ? 38  ARG YYY CB  1 
ATOM 20117 C CG  . ARG O 3 38  ? 114.893 -41.674 14.004  1.000 41.050  ? 38  ARG YYY CG  1 
ATOM 20118 C CD  . ARG O 3 38  ? 115.010 -43.121 13.564  1.000 40.790  ? 38  ARG YYY CD  1 
ATOM 20119 N NE  . ARG O 3 38  ? 115.320 -43.966 14.689  1.000 36.250  ? 38  ARG YYY NE  1 
ATOM 20120 C CZ  . ARG O 3 38  ? 115.561 -45.256 14.597  1.000 39.950  ? 38  ARG YYY CZ  1 
ATOM 20121 N NH1 . ARG O 3 38  ? 115.505 -45.859 13.425  1.000 43.950  ? 38  ARG YYY NH1 1 
ATOM 20122 N NH2 . ARG O 3 38  ? 115.859 -45.956 15.680  1.000 43.700  ? 38  ARG YYY NH2 1 
ATOM 20123 N N   . GLN O 3 39  ? 112.364 -39.091 13.326  1.000 28.380  ? 39  GLN YYY N   1 
ATOM 20124 C CA  . GLN O 3 39  ? 111.032 -38.826 13.929  1.000 29.250  ? 39  GLN YYY CA  1 
ATOM 20125 C C   . GLN O 3 39  ? 110.005 -39.805 13.364  1.000 30.340  ? 39  GLN YYY C   1 
ATOM 20126 O O   . GLN O 3 39  ? 109.560 -39.610 12.231  1.000 29.660  ? 39  GLN YYY O   1 
ATOM 20127 C CB  . GLN O 3 39  ? 110.604 -37.386 13.663  1.000 28.440  ? 39  GLN YYY CB  1 
ATOM 20128 C CG  . GLN O 3 39  ? 109.451 -36.946 14.538  1.000 27.590  ? 39  GLN YYY CG  1 
ATOM 20129 C CD  . GLN O 3 39  ? 109.126 -35.490 14.351  1.000 26.550  ? 39  GLN YYY CD  1 
ATOM 20130 O OE1 . GLN O 3 39  ? 109.433 -34.888 13.326  1.000 24.490  ? 39  GLN YYY OE1 1 
ATOM 20131 N NE2 . GLN O 3 39  ? 108.491 -34.923 15.365  1.000 28.470  ? 39  GLN YYY NE2 1 
ATOM 20132 N N   . ALA O 3 40  ? 109.661 -40.830 14.142  1.000 34.670  ? 40  ALA YYY N   1 
ATOM 20133 C CA  . ALA O 3 40  ? 108.710 -41.897 13.782  1.000 35.060  ? 40  ALA YYY CA  1 
ATOM 20134 C C   . ALA O 3 40  ? 107.314 -41.291 13.720  1.000 40.720  ? 40  ALA YYY C   1 
ATOM 20135 O O   . ALA O 3 40  ? 106.992 -40.401 14.503  1.000 40.890  ? 40  ALA YYY O   1 
ATOM 20136 C CB  . ALA O 3 40  ? 108.826 -43.023 14.776  1.000 33.750  ? 40  ALA YYY CB  1 
ATOM 20137 N N   . PRO O 3 41  ? 106.442 -41.746 12.794  1.000 49.600  ? 41  PRO YYY N   1 
ATOM 20138 C CA  . PRO O 3 41  ? 105.201 -41.024 12.515  1.000 52.220  ? 41  PRO YYY CA  1 
ATOM 20139 C C   . PRO O 3 41  ? 104.399 -40.898 13.820  1.000 52.630  ? 41  PRO YYY C   1 
ATOM 20140 O O   . PRO O 3 41  ? 104.209 -41.903 14.479  1.000 49.740  ? 41  PRO YYY O   1 
ATOM 20141 C CB  . PRO O 3 41  ? 104.492 -41.881 11.451  1.000 55.420  ? 41  PRO YYY CB  1 
ATOM 20142 C CG  . PRO O 3 41  ? 105.579 -42.792 10.880  1.000 53.820  ? 41  PRO YYY CG  1 
ATOM 20143 C CD  . PRO O 3 41  ? 106.540 -43.004 12.028  1.000 52.680  ? 41  PRO YYY CD  1 
ATOM 20144 N N   . GLY O 3 42  ? 104.038 -39.666 14.191  1.000 52.080  ? 42  GLY YYY N   1 
ATOM 20145 C CA  . GLY O 3 42  ? 103.163 -39.359 15.340  1.000 44.800  ? 42  GLY YYY CA  1 
ATOM 20146 C C   . GLY O 3 42  ? 103.938 -39.197 16.633  1.000 40.020  ? 42  GLY YYY C   1 
ATOM 20147 O O   . GLY O 3 42  ? 103.381 -38.512 17.530  1.000 36.660  ? 42  GLY YYY O   1 
ATOM 20148 N N   . LYS O 3 43  ? 105.128 -39.819 16.735  1.000 35.610  ? 43  LYS YYY N   1 
ATOM 20149 C CA  . LYS O 3 43  ? 105.973 -39.864 17.951  1.000 31.790  ? 43  LYS YYY CA  1 
ATOM 20150 C C   . LYS O 3 43  ? 106.987 -38.681 17.927  1.000 32.810  ? 43  LYS YYY C   1 
ATOM 20151 O O   . LYS O 3 43  ? 106.956 -37.832 16.997  1.000 27.650  ? 43  LYS YYY O   1 
ATOM 20152 C CB  . LYS O 3 43  ? 106.579 -41.272 18.047  1.000 25.920  ? 43  LYS YYY CB  1 
ATOM 20153 N N   . GLY O 3 44  ? 107.846 -38.580 18.950  1.000 35.480  ? 44  GLY YYY N   1 
ATOM 20154 C CA  . GLY O 3 44  ? 108.773 -37.446 19.153  1.000 36.910  ? 44  GLY YYY CA  1 
ATOM 20155 C C   . GLY O 3 44  ? 110.070 -37.635 18.391  1.000 41.350  ? 44  GLY YYY C   1 
ATOM 20156 O O   . GLY O 3 44  ? 110.078 -38.464 17.455  1.000 45.840  ? 44  GLY YYY O   1 
ATOM 20157 N N   . LEU O 3 45  ? 111.137 -36.913 18.768  1.000 39.460  ? 45  LEU YYY N   1 
ATOM 20158 C CA  . LEU O 3 45  ? 112.453 -36.972 18.060  1.000 33.850  ? 45  LEU YYY CA  1 
ATOM 20159 C C   . LEU O 3 45  ? 113.325 -38.044 18.702  1.000 29.780  ? 45  LEU YYY C   1 
ATOM 20160 O O   . LEU O 3 45  ? 113.064 -38.351 19.851  1.000 32.490  ? 45  LEU YYY O   1 
ATOM 20161 C CB  . LEU O 3 45  ? 113.138 -35.603 18.123  1.000 32.070  ? 45  LEU YYY CB  1 
ATOM 20162 C CG  . LEU O 3 45  ? 112.448 -34.496 17.337  1.000 30.380  ? 45  LEU YYY CG  1 
ATOM 20163 C CD1 . LEU O 3 45  ? 113.209 -33.195 17.501  1.000 32.010  ? 45  LEU YYY CD1 1 
ATOM 20164 C CD2 . LEU O 3 45  ? 112.382 -34.838 15.864  1.000 28.890  ? 45  LEU YYY CD2 1 
ATOM 20165 N N   . GLN O 3 46  ? 114.307 -38.581 17.977  1.000 28.570  ? 46  GLN YYY N   1 
ATOM 20166 C CA  . GLN O 3 46  ? 115.279 -39.587 18.486  1.000 27.900  ? 46  GLN YYY CA  1 
ATOM 20167 C C   . GLN O 3 46  ? 116.578 -39.484 17.688  1.000 28.650  ? 46  GLN YYY C   1 
ATOM 20168 O O   . GLN O 3 46  ? 116.575 -39.709 16.454  1.000 30.110  ? 46  GLN YYY O   1 
ATOM 20169 C CB  . GLN O 3 46  ? 114.732 -41.009 18.382  1.000 28.930  ? 46  GLN YYY CB  1 
ATOM 20170 C CG  . GLN O 3 46  ? 115.710 -42.070 18.877  1.000 29.790  ? 46  GLN YYY CG  1 
ATOM 20171 C CD  . GLN O 3 46  ? 115.340 -43.476 18.479  1.000 31.770  ? 46  GLN YYY CD  1 
ATOM 20172 O OE1 . GLN O 3 46  ? 114.861 -43.753 17.374  1.000 34.330  ? 46  GLN YYY OE1 1 
ATOM 20173 N NE2 . GLN O 3 46  ? 115.577 -44.391 19.396  1.000 32.060  ? 46  GLN YYY NE2 1 
ATOM 20174 N N   . TRP O 3 47  ? 117.663 -39.121 18.368  1.000 30.050  ? 47  TRP YYY N   1 
ATOM 20175 C CA  . TRP O 3 47  ? 119.016 -38.982 17.776  1.000 28.570  ? 47  TRP YYY CA  1 
ATOM 20176 C C   . TRP O 3 47  ? 119.471 -40.346 17.255  1.000 27.880  ? 47  TRP YYY C   1 
ATOM 20177 O O   . TRP O 3 47  ? 119.245 -41.353 17.932  1.000 26.640  ? 47  TRP YYY O   1 
ATOM 20178 C CB  . TRP O 3 47  ? 119.996 -38.428 18.807  1.000 27.170  ? 47  TRP YYY CB  1 
ATOM 20179 C CG  . TRP O 3 47  ? 121.417 -38.448 18.348  1.000 27.210  ? 47  TRP YYY CG  1 
ATOM 20180 C CD1 . TRP O 3 47  ? 122.012 -37.609 17.452  1.000 28.450  ? 47  TRP YYY CD1 1 
ATOM 20181 C CD2 . TRP O 3 47  ? 122.434 -39.356 18.773  1.000 27.070  ? 47  TRP YYY CD2 1 
ATOM 20182 N NE1 . TRP O 3 47  ? 123.326 -37.944 17.283  1.000 28.080  ? 47  TRP YYY NE1 1 
ATOM 20183 C CE2 . TRP O 3 47  ? 123.616 -39.003 18.094  1.000 28.500  ? 47  TRP YYY CE2 1 
ATOM 20184 C CE3 . TRP O 3 47  ? 122.465 -40.426 19.664  1.000 29.270  ? 47  TRP YYY CE3 1 
ATOM 20185 C CZ2 . TRP O 3 47  ? 124.817 -39.691 18.286  1.000 30.700  ? 47  TRP YYY CZ2 1 
ATOM 20186 C CZ3 . TRP O 3 47  ? 123.651 -41.102 19.851  1.000 30.010  ? 47  TRP YYY CZ3 1 
ATOM 20187 C CH2 . TRP O 3 47  ? 124.808 -40.742 19.170  1.000 29.020  ? 47  TRP YYY CH2 1 
ATOM 20188 N N   . VAL O 3 48  ? 120.117 -40.346 16.092  1.000 27.810  ? 48  VAL YYY N   1 
ATOM 20189 C CA  . VAL O 3 48  ? 120.558 -41.571 15.379  1.000 28.830  ? 48  VAL YYY CA  1 
ATOM 20190 C C   . VAL O 3 48  ? 122.069 -41.677 15.503  1.000 27.620  ? 48  VAL YYY C   1 
ATOM 20191 O O   . VAL O 3 48  ? 122.557 -42.699 15.998  1.000 36.610  ? 48  VAL YYY O   1 
ATOM 20192 C CB  . VAL O 3 48  ? 120.136 -41.533 13.904  1.000 30.450  ? 48  VAL YYY CB  1 
ATOM 20193 C CG1 . VAL O 3 48  ? 120.902 -42.549 13.079  1.000 30.200  ? 48  VAL YYY CG1 1 
ATOM 20194 C CG2 . VAL O 3 48  ? 118.629 -41.709 13.750  1.000 32.110  ? 48  VAL YYY CG2 1 
ATOM 20195 N N   . SER O 3 49  ? 122.786 -40.664 15.039  1.000 24.390  ? 49  SER YYY N   1 
ATOM 20196 C CA  . SER O 3 49  ? 124.258 -40.740 14.925  1.000 25.520  ? 49  SER YYY CA  1 
ATOM 20197 C C   . SER O 3 49  ? 124.919 -39.366 14.821  1.000 24.920  ? 49  SER YYY C   1 
ATOM 20198 O O   . SER O 3 49  ? 124.308 -38.452 14.239  1.000 21.970  ? 49  SER YYY O   1 
ATOM 20199 C CB  . SER O 3 49  ? 124.638 -41.652 13.784  1.000 26.620  ? 49  SER YYY CB  1 
ATOM 20200 O OG  . SER O 3 49  ? 126.037 -41.827 13.714  1.000 26.830  ? 49  SER YYY OG  1 
ATOM 20201 N N   . SER O 3 50  ? 126.122 -39.259 15.390  1.000 24.330  ? 50  SER YYY N   1 
ATOM 20202 C CA  . SER O 3 50  ? 127.037 -38.102 15.292  1.000 25.610  ? 50  SER YYY CA  1 
ATOM 20203 C C   . SER O 3 50  ? 128.321 -38.447 14.543  1.000 24.400  ? 50  SER YYY C   1 
ATOM 20204 O O   . SER O 3 50  ? 128.804 -39.581 14.666  1.000 20.120  ? 50  SER YYY O   1 
ATOM 20205 C CB  . SER O 3 50  ? 127.428 -37.623 16.665  1.000 27.820  ? 50  SER YYY CB  1 
ATOM 20206 O OG  . SER O 3 50  ? 128.330 -36.498 16.556  1.000 30.110  ? 50  SER YYY OG  1 
ATOM 20207 N N   . ILE O 3 51  ? 128.891 -37.463 13.859  1.000 26.350  ? 51  ILE YYY N   1 
ATOM 20208 C CA  . ILE O 3 51  ? 130.236 -37.592 13.246  1.000 26.260  ? 51  ILE YYY CA  1 
ATOM 20209 C C   . ILE O 3 51  ? 130.971 -36.265 13.399  1.000 25.040  ? 51  ILE YYY C   1 
ATOM 20210 O O   . ILE O 3 51  ? 130.373 -35.241 13.065  1.000 23.260  ? 51  ILE YYY O   1 
ATOM 20211 C CB  . ILE O 3 51  ? 130.186 -38.065 11.783  1.000 25.800  ? 51  ILE YYY CB  1 
ATOM 20212 C CG1 . ILE O 3 51  ? 131.592 -38.357 11.266  1.000 24.480  ? 51  ILE YYY CG1 1 
ATOM 20213 C CG2 . ILE O 3 51  ? 129.432 -37.078 10.911  1.000 25.980  ? 51  ILE YYY CG2 1 
ATOM 20214 C CD1 . ILE O 3 51  ? 131.607 -39.077 9.980   1.000 25.840  ? 51  ILE YYY CD1 1 
ATOM 20215 N N   . SER O 3 52  ? 132.221 -36.316 13.860  1.000 24.490  ? 52  SER YYY N   1 
ATOM 20216 C CA  . SER O 3 52  ? 133.109 -35.141 14.032  1.000 26.230  ? 52  SER YYY CA  1 
ATOM 20217 C C   . SER O 3 52  ? 133.463 -34.527 12.675  1.000 29.010  ? 52  SER YYY C   1 
ATOM 20218 O O   . SER O 3 52  ? 133.199 -35.171 11.650  1.000 29.310  ? 52  SER YYY O   1 
ATOM 20219 C CB  . SER O 3 52  ? 134.334 -35.486 14.872  1.000 27.810  ? 52  SER YYY CB  1 
ATOM 20220 O OG  . SER O 3 52  ? 135.321 -36.241 14.191  1.000 26.660  ? 52  SER YYY OG  1 
ATOM 20221 N N   . SER O 3 53  ? 134.015 -33.308 12.670  1.000 32.590  ? 53  SER YYY N   1 
ATOM 20222 C CA  . SER O 3 53  ? 134.431 -32.578 11.440  1.000 31.430  ? 53  SER YYY CA  1 
ATOM 20223 C C   . SER O 3 53  ? 135.332 -33.474 10.579  1.000 30.950  ? 53  SER YYY C   1 
ATOM 20224 O O   . SER O 3 53  ? 135.145 -33.478 9.362   1.000 26.970  ? 53  SER YYY O   1 
ATOM 20225 C CB  . SER O 3 53  ? 135.106 -31.270 11.784  1.000 34.120  ? 53  SER YYY CB  1 
ATOM 20226 O OG  . SER O 3 53  ? 136.453 -31.456 12.245  1.000 36.620  ? 53  SER YYY OG  1 
ATOM 20227 N N   . SER O 3 54  ? 136.268 -34.216 11.180  1.000 31.620  ? 54  SER YYY N   1 
ATOM 20228 C CA  . SER O 3 54  ? 137.308 -34.986 10.454  1.000 33.620  ? 54  SER YYY CA  1 
ATOM 20229 C C   . SER O 3 54  ? 136.993 -36.480 10.487  1.000 34.130  ? 54  SER YYY C   1 
ATOM 20230 O O   . SER O 3 54  ? 137.876 -37.296 10.109  1.000 40.740  ? 54  SER YYY O   1 
ATOM 20231 C CB  . SER O 3 54  ? 138.655 -34.711 11.037  1.000 36.120  ? 54  SER YYY CB  1 
ATOM 20232 O OG  . SER O 3 54  ? 139.280 -33.696 10.288  1.000 43.620  ? 54  SER YYY OG  1 
ATOM 20233 N N   . SER O 3 55  ? 135.800 -36.840 10.948  1.000 30.300  ? 55  SER YYY N   1 
ATOM 20234 C CA  . SER O 3 55  ? 135.343 -38.247 11.023  1.000 29.580  ? 55  SER YYY CA  1 
ATOM 20235 C C   . SER O 3 55  ? 136.239 -39.032 11.994  1.000 30.920  ? 55  SER YYY C   1 
ATOM 20236 O O   . SER O 3 55  ? 136.287 -40.262 11.871  1.000 37.040  ? 55  SER YYY O   1 
ATOM 20237 C CB  . SER O 3 55  ? 135.311 -38.819 9.631   1.000 31.040  ? 55  SER YYY CB  1 
ATOM 20238 O OG  . SER O 3 55  ? 134.995 -37.812 8.673   1.000 31.480  ? 55  SER YYY OG  1 
ATOM 20239 N N   . THR O 3 56  ? 136.894 -38.358 12.955  1.000 32.020  ? 56  THR YYY N   1 
ATOM 20240 C CA  . THR O 3 56  ? 137.638 -38.989 14.090  1.000 29.550  ? 56  THR YYY CA  1 
ATOM 20241 C C   . THR O 3 56  ? 136.673 -39.606 15.095  1.000 29.910  ? 56  THR YYY C   1 
ATOM 20242 O O   . THR O 3 56  ? 137.059 -40.598 15.681  1.000 33.020  ? 56  THR YYY O   1 
ATOM 20243 C CB  . THR O 3 56  ? 138.488 -38.031 14.931  1.000 26.080  ? 56  THR YYY CB  1 
ATOM 20244 O OG1 . THR O 3 56  ? 139.401 -37.530 13.971  1.000 24.170  ? 56  THR YYY OG1 1 
ATOM 20245 N N   . TYR O 3 57  ? 135.497 -39.025 15.327  1.000 29.420  ? 57  TYR YYY N   1 
ATOM 20246 C CA  . TYR O 3 57  ? 134.543 -39.562 16.331  1.000 31.620  ? 57  TYR YYY CA  1 
ATOM 20247 C C   . TYR O 3 57  ? 133.153 -39.736 15.706  1.000 33.920  ? 57  TYR YYY C   1 
ATOM 20248 O O   . TYR O 3 57  ? 132.430 -38.728 15.463  1.000 40.020  ? 57  TYR YYY O   1 
ATOM 20249 C CB  . TYR O 3 57  ? 134.509 -38.668 17.572  1.000 30.870  ? 57  TYR YYY CB  1 
ATOM 20250 C CG  . TYR O 3 57  ? 135.831 -38.526 18.279  1.000 31.300  ? 57  TYR YYY CG  1 
ATOM 20251 C CD1 . TYR O 3 57  ? 136.812 -37.684 17.778  1.000 33.480  ? 57  TYR YYY CD1 1 
ATOM 20252 C CD2 . TYR O 3 57  ? 136.108 -39.227 19.447  1.000 30.470  ? 57  TYR YYY CD2 1 
ATOM 20253 C CE1 . TYR O 3 57  ? 138.020 -37.530 18.438  1.000 36.040  ? 57  TYR YYY CE1 1 
ATOM 20254 C CE2 . TYR O 3 57  ? 137.316 -39.095 20.109  1.000 31.020  ? 57  TYR YYY CE2 1 
ATOM 20255 C CZ  . TYR O 3 57  ? 138.273 -38.232 19.610  1.000 33.380  ? 57  TYR YYY CZ  1 
ATOM 20256 O OH  . TYR O 3 57  ? 139.495 -38.108 20.204  1.000 32.320  ? 57  TYR YYY OH  1 
ATOM 20257 N N   . MET O 3 58  ? 132.772 -40.993 15.491  1.000 30.740  ? 58  MET YYY N   1 
ATOM 20258 C CA  . MET O 3 58  ? 131.376 -41.363 15.164  1.000 30.570  ? 58  MET YYY CA  1 
ATOM 20259 C C   . MET O 3 58  ? 130.736 -41.945 16.427  1.000 28.470  ? 58  MET YYY C   1 
ATOM 20260 O O   . MET O 3 58  ? 131.409 -42.670 17.126  1.000 30.580  ? 58  MET YYY O   1 
ATOM 20261 C CB  . MET O 3 58  ? 131.336 -42.377 14.012  1.000 31.970  ? 58  MET YYY CB  1 
ATOM 20262 C CG  . MET O 3 58  ? 131.614 -41.754 12.672  1.000 31.780  ? 58  MET YYY CG  1 
ATOM 20263 S SD  . MET O 3 58  ? 133.341 -41.530 12.371  1.000 35.780  ? 58  MET YYY SD  1 
ATOM 20264 C CE  . MET O 3 58  ? 133.702 -43.200 11.835  1.000 37.030  ? 58  MET YYY CE  1 
ATOM 20265 N N   . TYR O 3 59  ? 129.494 -41.579 16.716  1.000 27.490  ? 59  TYR YYY N   1 
ATOM 20266 C CA  . TYR O 3 59  ? 128.662 -42.126 17.818  1.000 28.150  ? 59  TYR YYY CA  1 
ATOM 20267 C C   . TYR O 3 59  ? 127.309 -42.539 17.251  1.000 28.340  ? 59  TYR YYY C   1 
ATOM 20268 O O   . TYR O 3 59  ? 126.824 -41.869 16.307  1.000 26.670  ? 59  TYR YYY O   1 
ATOM 20269 C CB  . TYR O 3 59  ? 128.437 -41.078 18.906  1.000 30.770  ? 59  TYR YYY CB  1 
ATOM 20270 C CG  . TYR O 3 59  ? 129.689 -40.604 19.586  1.000 33.110  ? 59  TYR YYY CG  1 
ATOM 20271 C CD1 . TYR O 3 59  ? 130.328 -41.372 20.541  1.000 33.930  ? 59  TYR YYY CD1 1 
ATOM 20272 C CD2 . TYR O 3 59  ? 130.228 -39.376 19.276  1.000 37.070  ? 59  TYR YYY CD2 1 
ATOM 20273 C CE1 . TYR O 3 59  ? 131.488 -40.947 21.160  1.000 35.360  ? 59  TYR YYY CE1 1 
ATOM 20274 C CE2 . TYR O 3 59  ? 131.367 -38.913 19.920  1.000 40.550  ? 59  TYR YYY CE2 1 
ATOM 20275 C CZ  . TYR O 3 59  ? 132.009 -39.705 20.856  1.000 37.610  ? 59  TYR YYY CZ  1 
ATOM 20276 O OH  . TYR O 3 59  ? 133.142 -39.253 21.464  1.000 35.790  ? 59  TYR YYY OH  1 
ATOM 20277 N N   . TYR O 3 60  ? 126.715 -43.592 17.817  1.000 26.780  ? 60  TYR YYY N   1 
ATOM 20278 C CA  . TYR O 3 60  ? 125.383 -44.073 17.384  1.000 25.680  ? 60  TYR YYY CA  1 
ATOM 20279 C C   . TYR O 3 60  ? 124.505 -44.263 18.614  1.000 25.510  ? 60  TYR YYY C   1 
ATOM 20280 O O   . TYR O 3 60  ? 125.005 -44.675 19.639  1.000 26.220  ? 60  TYR YYY O   1 
ATOM 20281 C CB  . TYR O 3 60  ? 125.506 -45.359 16.564  1.000 24.150  ? 60  TYR YYY CB  1 
ATOM 20282 C CG  . TYR O 3 60  ? 126.446 -45.274 15.394  1.000 24.240  ? 60  TYR YYY CG  1 
ATOM 20283 C CD1 . TYR O 3 60  ? 127.805 -45.453 15.576  1.000 22.940  ? 60  TYR YYY CD1 1 
ATOM 20284 C CD2 . TYR O 3 60  ? 125.986 -45.016 14.105  1.000 24.530  ? 60  TYR YYY CD2 1 
ATOM 20285 C CE1 . TYR O 3 60  ? 128.686 -45.371 14.514  1.000 23.270  ? 60  TYR YYY CE1 1 
ATOM 20286 C CE2 . TYR O 3 60  ? 126.862 -44.935 13.029  1.000 22.950  ? 60  TYR YYY CE2 1 
ATOM 20287 C CZ  . TYR O 3 60  ? 128.218 -45.101 13.240  1.000 22.240  ? 60  TYR YYY CZ  1 
ATOM 20288 O OH  . TYR O 3 60  ? 129.114 -45.042 12.218  1.000 21.440  ? 60  TYR YYY OH  1 
ATOM 20289 N N   . GLY O 3 61  ? 123.221 -43.950 18.470  1.000 27.330  ? 61  GLY YYY N   1 
ATOM 20290 C CA  . GLY O 3 61  ? 122.145 -44.413 19.360  1.000 27.410  ? 61  GLY YYY CA  1 
ATOM 20291 C C   . GLY O 3 61  ? 122.223 -45.920 19.314  1.000 28.330  ? 61  GLY YYY C   1 
ATOM 20292 O O   . GLY O 3 61  ? 122.634 -46.434 18.308  1.000 27.370  ? 61  GLY YYY O   1 
ATOM 20293 N N   . ASP O 3 62  ? 121.775 -46.621 20.354  1.000 34.950  ? 62  ASP YYY N   1 
ATOM 20294 C CA  . ASP O 3 62  ? 121.932 -48.099 20.409  1.000 36.440  ? 62  ASP YYY CA  1 
ATOM 20295 C C   . ASP O 3 62  ? 120.822 -48.743 19.585  1.000 35.340  ? 62  ASP YYY C   1 
ATOM 20296 O O   . ASP O 3 62  ? 120.994 -49.888 19.156  1.000 37.990  ? 62  ASP YYY O   1 
ATOM 20297 C CB  . ASP O 3 62  ? 122.023 -48.623 21.845  1.000 40.670  ? 62  ASP YYY CB  1 
ATOM 20298 C CG  . ASP O 3 62  ? 121.039 -47.994 22.811  1.000 47.220  ? 62  ASP YYY CG  1 
ATOM 20299 O OD1 . ASP O 3 62  ? 121.182 -46.790 23.097  1.000 53.670  ? 62  ASP YYY OD1 1 
ATOM 20300 O OD2 . ASP O 3 62  ? 120.149 -48.722 23.286  1.000 59.450  ? 62  ASP YYY OD2 1 
ATOM 20301 N N   . SER O 3 63  ? 119.732 -48.025 19.382  1.000 33.490  ? 63  SER YYY N   1 
ATOM 20302 C CA  . SER O 3 63  ? 118.581 -48.526 18.600  1.000 33.660  ? 63  SER YYY CA  1 
ATOM 20303 C C   . SER O 3 63  ? 119.161 -48.930 17.244  1.000 29.560  ? 63  SER YYY C   1 
ATOM 20304 O O   . SER O 3 63  ? 118.560 -49.757 16.621  1.000 34.510  ? 63  SER YYY O   1 
ATOM 20305 C CB  . SER O 3 63  ? 117.451 -47.545 18.450  1.000 36.130  ? 63  SER YYY CB  1 
ATOM 20306 O OG  . SER O 3 63  ? 117.905 -46.432 17.709  1.000 40.880  ? 63  SER YYY OG  1 
ATOM 20307 N N   . VAL O 3 64  ? 120.273 -48.355 16.783  1.000 26.150  ? 64  VAL YYY N   1 
ATOM 20308 C CA  . VAL O 3 64  ? 120.826 -48.635 15.431  1.000 26.050  ? 64  VAL YYY CA  1 
ATOM 20309 C C   . VAL O 3 64  ? 122.286 -49.074 15.489  1.000 25.010  ? 64  VAL YYY C   1 
ATOM 20310 O O   . VAL O 3 64  ? 122.843 -49.221 14.397  1.000 22.370  ? 64  VAL YYY O   1 
ATOM 20311 C CB  . VAL O 3 64  ? 120.693 -47.405 14.522  1.000 27.890  ? 64  VAL YYY CB  1 
ATOM 20312 C CG1 . VAL O 3 64  ? 119.265 -46.909 14.448  1.000 29.030  ? 64  VAL YYY CG1 1 
ATOM 20313 C CG2 . VAL O 3 64  ? 121.623 -46.280 14.922  1.000 28.780  ? 64  VAL YYY CG2 1 
ATOM 20314 N N   . LYS O 3 65  ? 122.881 -49.271 16.676  1.000 26.480  ? 65  LYS YYY N   1 
ATOM 20315 C CA  . LYS O 3 65  ? 124.285 -49.758 16.828  1.000 26.250  ? 65  LYS YYY CA  1 
ATOM 20316 C C   . LYS O 3 65  ? 124.431 -50.985 15.916  1.000 29.080  ? 65  LYS YYY C   1 
ATOM 20317 O O   . LYS O 3 65  ? 123.545 -51.880 15.935  1.000 29.480  ? 65  LYS YYY O   1 
ATOM 20318 C CB  . LYS O 3 65  ? 124.614 -50.158 18.271  1.000 23.850  ? 65  LYS YYY CB  1 
ATOM 20319 N N   . GLY O 3 66  ? 125.452 -51.008 15.079  1.000 29.290  ? 66  GLY YYY N   1 
ATOM 20320 C CA  . GLY O 3 66  ? 125.759 -52.219 14.309  1.000 29.990  ? 66  GLY YYY CA  1 
ATOM 20321 C C   . GLY O 3 66  ? 125.079 -52.260 12.957  1.000 29.000  ? 66  GLY YYY C   1 
ATOM 20322 O O   . GLY O 3 66  ? 125.568 -52.995 12.103  1.000 35.200  ? 66  GLY YYY O   1 
ATOM 20323 N N   . ARG O 3 67  ? 124.012 -51.500 12.729  1.000 27.750  ? 67  ARG YYY N   1 
ATOM 20324 C CA  . ARG O 3 67  ? 123.205 -51.593 11.478  1.000 28.780  ? 67  ARG YYY CA  1 
ATOM 20325 C C   . ARG O 3 67  ? 123.426 -50.365 10.595  1.000 30.690  ? 67  ARG YYY C   1 
ATOM 20326 O O   . ARG O 3 67  ? 123.597 -50.538 9.386   1.000 35.140  ? 67  ARG YYY O   1 
ATOM 20327 C CB  . ARG O 3 67  ? 121.734 -51.763 11.817  1.000 29.390  ? 67  ARG YYY CB  1 
ATOM 20328 C CG  . ARG O 3 67  ? 121.458 -52.998 12.664  1.000 31.940  ? 67  ARG YYY CG  1 
ATOM 20329 C CD  . ARG O 3 67  ? 119.970 -53.309 12.868  1.000 31.410  ? 67  ARG YYY CD  1 
ATOM 20330 N NE  . ARG O 3 67  ? 119.254 -52.250 13.562  1.000 29.800  ? 67  ARG YYY NE  1 
ATOM 20331 C CZ  . ARG O 3 67  ? 118.358 -51.447 13.004  1.000 30.720  ? 67  ARG YYY CZ  1 
ATOM 20332 N NH1 . ARG O 3 67  ? 118.019 -51.576 11.742  1.000 31.290  ? 67  ARG YYY NH1 1 
ATOM 20333 N NH2 . ARG O 3 67  ? 117.787 -50.503 13.716  1.000 32.190  ? 67  ARG YYY NH2 1 
ATOM 20334 N N   . PHE O 3 68  ? 123.447 -49.180 11.193  1.000 30.620  ? 68  PHE YYY N   1 
ATOM 20335 C CA  . PHE O 3 68  ? 123.650 -47.884 10.507  1.000 27.880  ? 68  PHE YYY CA  1 
ATOM 20336 C C   . PHE O 3 68  ? 125.130 -47.508 10.545  1.000 23.660  ? 68  PHE YYY C   1 
ATOM 20337 O O   . PHE O 3 68  ? 125.832 -47.876 11.462  1.000 23.140  ? 68  PHE YYY O   1 
ATOM 20338 C CB  . PHE O 3 68  ? 122.774 -46.820 11.172  1.000 31.160  ? 68  PHE YYY CB  1 
ATOM 20339 C CG  . PHE O 3 68  ? 121.294 -47.005 10.963  1.000 32.540  ? 68  PHE YYY CG  1 
ATOM 20340 C CD1 . PHE O 3 68  ? 120.770 -48.221 10.534  1.000 34.880  ? 68  PHE YYY CD1 1 
ATOM 20341 C CD2 . PHE O 3 68  ? 120.422 -45.970 11.228  1.000 32.470  ? 68  PHE YYY CD2 1 
ATOM 20342 C CE1 . PHE O 3 68  ? 119.413 -48.385 10.348  1.000 35.380  ? 68  PHE YYY CE1 1 
ATOM 20343 C CE2 . PHE O 3 68  ? 119.061 -46.140 11.042  1.000 35.900  ? 68  PHE YYY CE2 1 
ATOM 20344 C CZ  . PHE O 3 68  ? 118.561 -47.344 10.601  1.000 35.500  ? 68  PHE YYY CZ  1 
ATOM 20345 N N   . THR O 3 69  ? 125.584 -46.765 9.551   1.000 22.820  ? 69  THR YYY N   1 
ATOM 20346 C CA  . THR O 3 69  ? 126.947 -46.178 9.506   1.000 23.800  ? 69  THR YYY CA  1 
ATOM 20347 C C   . THR O 3 69  ? 126.858 -44.749 8.982   1.000 22.830  ? 69  THR YYY C   1 
ATOM 20348 O O   . THR O 3 69  ? 126.345 -44.557 7.878   1.000 23.110  ? 69  THR YYY O   1 
ATOM 20349 C CB  . THR O 3 69  ? 127.886 -47.031 8.659   1.000 25.050  ? 69  THR YYY CB  1 
ATOM 20350 O OG1 . THR O 3 69  ? 127.600 -48.371 9.056   1.000 28.780  ? 69  THR YYY OG1 1 
ATOM 20351 C CG2 . THR O 3 69  ? 129.342 -46.681 8.851   1.000 25.210  ? 69  THR YYY CG2 1 
ATOM 20352 N N   . ILE O 3 70  ? 127.334 -43.800 9.780   1.000 22.570  ? 70  ILE YYY N   1 
ATOM 20353 C CA  . ILE O 3 70  ? 127.419 -42.365 9.404   1.000 21.970  ? 70  ILE YYY CA  1 
ATOM 20354 C C   . ILE O 3 70  ? 128.745 -42.173 8.669   1.000 21.000  ? 70  ILE YYY C   1 
ATOM 20355 O O   . ILE O 3 70  ? 129.730 -42.852 9.005   1.000 20.640  ? 70  ILE YYY O   1 
ATOM 20356 C CB  . ILE O 3 70  ? 127.306 -41.456 10.646  1.000 22.180  ? 70  ILE YYY CB  1 
ATOM 20357 C CG1 . ILE O 3 70  ? 126.925 -40.021 10.278  1.000 22.400  ? 70  ILE YYY CG1 1 
ATOM 20358 C CG2 . ILE O 3 70  ? 128.580 -41.492 11.463  1.000 21.580  ? 70  ILE YYY CG2 1 
ATOM 20359 C CD1 . ILE O 3 70  ? 126.512 -39.190 11.462  1.000 22.200  ? 70  ILE YYY CD1 1 
ATOM 20360 N N   . SER O 3 71  ? 128.768 -41.282 7.690   1.000 19.770  ? 71  SER YYY N   1 
ATOM 20361 C CA  . SER O 3 71  ? 130.012 -40.888 7.012   1.000 20.970  ? 71  SER YYY CA  1 
ATOM 20362 C C   . SER O 3 71  ? 129.833 -39.496 6.435   1.000 21.870  ? 71  SER YYY C   1 
ATOM 20363 O O   . SER O 3 71  ? 128.693 -39.083 6.203   1.000 22.670  ? 71  SER YYY O   1 
ATOM 20364 C CB  . SER O 3 71  ? 130.398 -41.899 5.963   1.000 22.010  ? 71  SER YYY CB  1 
ATOM 20365 O OG  . SER O 3 71  ? 129.517 -41.867 4.865   1.000 22.560  ? 71  SER YYY OG  1 
ATOM 20366 N N   . ARG O 3 72  ? 130.951 -38.837 6.155   1.000 23.730  ? 72  ARG YYY N   1 
ATOM 20367 C CA  . ARG O 3 72  ? 130.955 -37.547 5.441   1.000 24.990  ? 72  ARG YYY CA  1 
ATOM 20368 C C   . ARG O 3 72  ? 132.020 -37.569 4.337   1.000 23.900  ? 72  ARG YYY C   1 
ATOM 20369 O O   . ARG O 3 72  ? 132.972 -38.395 4.420   1.000 21.540  ? 72  ARG YYY O   1 
ATOM 20370 C CB  . ARG O 3 72  ? 131.175 -36.448 6.473   1.000 26.720  ? 72  ARG YYY CB  1 
ATOM 20371 C CG  . ARG O 3 72  ? 132.506 -36.550 7.208   1.000 27.230  ? 72  ARG YYY CG  1 
ATOM 20372 C CD  . ARG O 3 72  ? 132.588 -35.601 8.384   1.000 28.290  ? 72  ARG YYY CD  1 
ATOM 20373 N NE  . ARG O 3 72  ? 132.299 -34.225 8.006   1.000 31.180  ? 72  ARG YYY NE  1 
ATOM 20374 C CZ  . ARG O 3 72  ? 131.715 -33.316 8.797   1.000 31.810  ? 72  ARG YYY CZ  1 
ATOM 20375 N NH1 . ARG O 3 72  ? 131.498 -32.097 8.331   1.000 34.380  ? 72  ARG YYY NH1 1 
ATOM 20376 N NH2 . ARG O 3 72  ? 131.340 -33.623 10.028  1.000 29.310  ? 72  ARG YYY NH2 1 
ATOM 20377 N N   . ASP O 3 73  ? 131.825 -36.715 3.333   1.000 23.360  ? 73  ASP YYY N   1 
ATOM 20378 C CA  . ASP O 3 73  ? 132.847 -36.358 2.321   1.000 23.770  ? 73  ASP YYY CA  1 
ATOM 20379 C C   . ASP O 3 73  ? 132.976 -34.841 2.336   1.000 23.120  ? 73  ASP YYY C   1 
ATOM 20380 O O   . ASP O 3 73  ? 132.071 -34.151 1.800   1.000 22.740  ? 73  ASP YYY O   1 
ATOM 20381 C CB  . ASP O 3 73  ? 132.462 -36.914 0.945   1.000 26.060  ? 73  ASP YYY CB  1 
ATOM 20382 C CG  . ASP O 3 73  ? 133.531 -36.772 -0.123  1.000 26.880  ? 73  ASP YYY CG  1 
ATOM 20383 O OD1 . ASP O 3 73  ? 134.557 -36.073 0.125   1.000 22.380  ? 73  ASP YYY OD1 1 
ATOM 20384 O OD2 . ASP O 3 73  ? 133.304 -37.359 -1.205  1.000 32.880  ? 73  ASP YYY OD2 1 
ATOM 20385 N N   . ASN O 3 74  ? 134.037 -34.343 2.967   1.000 24.840  ? 74  ASN YYY N   1 
ATOM 20386 C CA  . ASN O 3 74  ? 134.248 -32.884 3.187   1.000 25.320  ? 74  ASN YYY CA  1 
ATOM 20387 C C   . ASN O 3 74  ? 134.569 -32.219 1.851   1.000 26.330  ? 74  ASN YYY C   1 
ATOM 20388 O O   . ASN O 3 74  ? 134.235 -31.049 1.709   1.000 33.350  ? 74  ASN YYY O   1 
ATOM 20389 C CB  . ASN O 3 74  ? 135.297 -32.569 4.256   1.000 23.540  ? 74  ASN YYY CB  1 
ATOM 20390 C CG  . ASN O 3 74  ? 134.774 -32.715 5.674   1.000 22.970  ? 74  ASN YYY CG  1 
ATOM 20391 O OD1 . ASN O 3 74  ? 133.559 -32.853 5.917   1.000 20.520  ? 74  ASN YYY OD1 1 
ATOM 20392 N ND2 . ASN O 3 74  ? 135.679 -32.701 6.627   1.000 22.830  ? 74  ASN YYY ND2 1 
ATOM 20393 N N   . ALA O 3 75  ? 135.130 -32.940 0.893   1.000 26.340  ? 75  ALA YYY N   1 
ATOM 20394 C CA  . ALA O 3 75  ? 135.328 -32.422 -0.480  1.000 27.050  ? 75  ALA YYY CA  1 
ATOM 20395 C C   . ALA O 3 75  ? 133.983 -32.300 -1.212  1.000 26.680  ? 75  ALA YYY C   1 
ATOM 20396 O O   . ALA O 3 75  ? 133.882 -31.426 -2.044  1.000 23.320  ? 75  ALA YYY O   1 
ATOM 20397 C CB  . ALA O 3 75  ? 136.281 -33.290 -1.250  1.000 29.120  ? 75  ALA YYY CB  1 
ATOM 20398 N N   . ARG O 3 76  ? 132.986 -33.131 -0.921  1.000 30.020  ? 76  ARG YYY N   1 
ATOM 20399 C CA  . ARG O 3 76  ? 131.680 -33.104 -1.647  1.000 32.810  ? 76  ARG YYY CA  1 
ATOM 20400 C C   . ARG O 3 76  ? 130.629 -32.360 -0.805  1.000 30.860  ? 76  ARG YYY C   1 
ATOM 20401 O O   . ARG O 3 76  ? 129.479 -32.321 -1.233  1.000 29.570  ? 76  ARG YYY O   1 
ATOM 20402 C CB  . ARG O 3 76  ? 131.209 -34.527 -2.023  1.000 40.380  ? 76  ARG YYY CB  1 
ATOM 20403 C CG  . ARG O 3 76  ? 131.938 -35.258 -3.149  1.000 48.310  ? 76  ARG YYY CG  1 
ATOM 20404 C CD  . ARG O 3 76  ? 131.869 -34.788 -4.604  1.000 55.950  ? 76  ARG YYY CD  1 
ATOM 20405 N NE  . ARG O 3 76  ? 132.270 -35.863 -5.526  1.000 58.430  ? 76  ARG YYY NE  1 
ATOM 20406 C CZ  . ARG O 3 76  ? 133.544 -36.172 -5.862  1.000 52.680  ? 76  ARG YYY CZ  1 
ATOM 20407 N N   . ASN O 3 77  ? 130.999 -31.757 0.338   1.000 33.970  ? 77  ASN YYY N   1 
ATOM 20408 C CA  . ASN O 3 77  ? 130.065 -30.995 1.227   1.000 34.790  ? 77  ASN YYY CA  1 
ATOM 20409 C C   . ASN O 3 77  ? 128.826 -31.844 1.552   1.000 33.530  ? 77  ASN YYY C   1 
ATOM 20410 O O   . ASN O 3 77  ? 127.688 -31.290 1.513   1.000 29.610  ? 77  ASN YYY O   1 
ATOM 20411 C CB  . ASN O 3 77  ? 129.545 -29.679 0.613   1.000 36.270  ? 77  ASN YYY CB  1 
ATOM 20412 C CG  . ASN O 3 77  ? 130.530 -28.535 0.696   1.000 38.000  ? 77  ASN YYY CG  1 
ATOM 20413 O OD1 . ASN O 3 77  ? 130.956 -28.149 1.776   1.000 41.720  ? 77  ASN YYY OD1 1 
ATOM 20414 N ND2 . ASN O 3 77  ? 130.904 -27.981 -0.440  1.000 41.060  ? 77  ASN YYY ND2 1 
ATOM 20415 N N   . SER O 3 78  ? 129.013 -33.134 1.871   1.000 32.940  ? 78  SER YYY N   1 
ATOM 20416 C CA  . SER O 3 78  ? 127.892 -34.088 2.046   1.000 31.200  ? 78  SER YYY CA  1 
ATOM 20417 C C   . SER O 3 78  ? 128.084 -35.016 3.248   1.000 29.110  ? 78  SER YYY C   1 
ATOM 20418 O O   . SER O 3 78  ? 129.197 -35.540 3.451   1.000 28.510  ? 78  SER YYY O   1 
ATOM 20419 C CB  . SER O 3 78  ? 127.690 -34.858 0.806   1.000 32.930  ? 78  SER YYY CB  1 
ATOM 20420 O OG  . SER O 3 78  ? 127.097 -34.037 -0.195  1.000 35.510  ? 78  SER YYY OG  1 
ATOM 20421 N N   . LEU O 3 79  ? 127.000 -35.197 4.006   1.000 26.500  ? 79  LEU YYY N   1 
ATOM 20422 C CA  . LEU O 3 79  ? 126.889 -36.174 5.106   1.000 26.610  ? 79  LEU YYY CA  1 
ATOM 20423 C C   . LEU O 3 79  ? 126.039 -37.348 4.609   1.000 27.160  ? 79  LEU YYY C   1 
ATOM 20424 O O   . LEU O 3 79  ? 125.060 -37.099 3.881   1.000 23.810  ? 79  LEU YYY O   1 
ATOM 20425 C CB  . LEU O 3 79  ? 126.231 -35.472 6.299   1.000 25.720  ? 79  LEU YYY CB  1 
ATOM 20426 C CG  . LEU O 3 79  ? 125.810 -36.386 7.450   1.000 25.300  ? 79  LEU YYY CG  1 
ATOM 20427 C CD1 . LEU O 3 79  ? 127.004 -36.742 8.310   1.000 23.490  ? 79  LEU YYY CD1 1 
ATOM 20428 C CD2 . LEU O 3 79  ? 124.725 -35.735 8.287   1.000 26.420  ? 79  LEU YYY CD2 1 
ATOM 20429 N N   . TYR O 3 80  ? 126.405 -38.578 4.978   1.000 28.700  ? 80  TYR YYY N   1 
ATOM 20430 C CA  . TYR O 3 80  ? 125.709 -39.824 4.565   1.000 29.200  ? 80  TYR YYY CA  1 
ATOM 20431 C C   . TYR O 3 80  ? 125.341 -40.674 5.788   1.000 26.320  ? 80  TYR YYY C   1 
ATOM 20432 O O   . TYR O 3 80  ? 126.073 -40.670 6.784   1.000 23.400  ? 80  TYR YYY O   1 
ATOM 20433 C CB  . TYR O 3 80  ? 126.556 -40.642 3.580   1.000 32.340  ? 80  TYR YYY CB  1 
ATOM 20434 C CG  . TYR O 3 80  ? 127.078 -39.865 2.399   1.000 33.810  ? 80  TYR YYY CG  1 
ATOM 20435 C CD1 . TYR O 3 80  ? 126.229 -39.426 1.392   1.000 33.500  ? 80  TYR YYY CD1 1 
ATOM 20436 C CD2 . TYR O 3 80  ? 128.428 -39.568 2.293   1.000 36.240  ? 80  TYR YYY CD2 1 
ATOM 20437 C CE1 . TYR O 3 80  ? 126.694 -38.652 0.344   1.000 35.280  ? 80  TYR YYY CE1 1 
ATOM 20438 C CE2 . TYR O 3 80  ? 128.921 -38.834 1.225   1.000 39.640  ? 80  TYR YYY CE2 1 
ATOM 20439 C CZ  . TYR O 3 80  ? 128.055 -38.390 0.240   1.000 38.780  ? 80  TYR YYY CZ  1 
ATOM 20440 O OH  . TYR O 3 80  ? 128.607 -37.666 -0.790  1.000 46.580  ? 80  TYR YYY OH  1 
ATOM 20441 N N   . LEU O 3 81  ? 124.242 -41.397 5.675   1.000 27.270  ? 81  LEU YYY N   1 
ATOM 20442 C CA  . LEU O 3 81  ? 123.826 -42.479 6.604   1.000 30.380  ? 81  LEU YYY CA  1 
ATOM 20443 C C   . LEU O 3 81  ? 123.531 -43.758 5.804   1.000 30.990  ? 81  LEU YYY C   1 
ATOM 20444 O O   . LEU O 3 81  ? 122.593 -43.758 5.033   1.000 30.020  ? 81  LEU YYY O   1 
ATOM 20445 C CB  . LEU O 3 81  ? 122.599 -42.044 7.416   1.000 29.720  ? 81  LEU YYY CB  1 
ATOM 20446 C CG  . LEU O 3 81  ? 122.166 -43.037 8.487   1.000 29.380  ? 81  LEU YYY CG  1 
ATOM 20447 C CD1 . LEU O 3 81  ? 123.261 -43.214 9.526   1.000 29.810  ? 81  LEU YYY CD1 1 
ATOM 20448 C CD2 . LEU O 3 81  ? 120.881 -42.614 9.140   1.000 29.040  ? 81  LEU YYY CD2 1 
ATOM 20449 N N   . GLN O 3 82  ? 124.333 -44.799 6.006   1.000 31.470  ? 82  GLN YYY N   1 
ATOM 20450 C CA  . GLN O 3 82  ? 124.158 -46.155 5.435   1.000 33.840  ? 82  GLN YYY CA  1 
ATOM 20451 C C   . GLN O 3 82  ? 123.261 -46.968 6.389   1.000 35.440  ? 82  GLN YYY C   1 
ATOM 20452 O O   . GLN O 3 82  ? 123.726 -47.292 7.480   1.000 35.290  ? 82  GLN YYY O   1 
ATOM 20453 C CB  . GLN O 3 82  ? 125.511 -46.834 5.250   1.000 36.500  ? 82  GLN YYY CB  1 
ATOM 20454 C CG  . GLN O 3 82  ? 125.418 -48.205 4.587   1.000 37.560  ? 82  GLN YYY CG  1 
ATOM 20455 C CD  . GLN O 3 82  ? 124.661 -48.104 3.295   1.000 40.380  ? 82  GLN YYY CD  1 
ATOM 20456 O OE1 . GLN O 3 82  ? 125.074 -47.412 2.365   1.000 46.770  ? 82  GLN YYY OE1 1 
ATOM 20457 N NE2 . GLN O 3 82  ? 123.538 -48.792 3.238   1.000 37.940  ? 82  GLN YYY NE2 1 
ATOM 20458 N N   . MET O 3 83  ? 122.033 -47.280 5.981   1.000 36.450  ? 83  MET YYY N   1 
ATOM 20459 C CA  . MET O 3 83  ? 121.034 -48.015 6.798   1.000 35.650  ? 83  MET YYY CA  1 
ATOM 20460 C C   . MET O 3 83  ? 120.905 -49.444 6.255   1.000 34.320  ? 83  MET YYY C   1 
ATOM 20461 O O   . MET O 3 83  ? 120.338 -49.622 5.195   1.000 34.040  ? 83  MET YYY O   1 
ATOM 20462 C CB  . MET O 3 83  ? 119.671 -47.315 6.747   1.000 37.470  ? 83  MET YYY CB  1 
ATOM 20463 C CG  . MET O 3 83  ? 119.706 -45.860 7.200   1.000 38.740  ? 83  MET YYY CG  1 
ATOM 20464 S SD  . MET O 3 83  ? 118.225 -44.950 6.639   1.000 38.320  ? 83  MET YYY SD  1 
ATOM 20465 C CE  . MET O 3 83  ? 117.113 -45.400 7.958   1.000 37.750  ? 83  MET YYY CE  1 
ATOM 20466 N N   . ASN O 3 84  ? 121.452 -50.422 6.963   1.000 32.270  ? 84  ASN YYY N   1 
ATOM 20467 C CA  . ASN O 3 84  ? 121.379 -51.868 6.646   1.000 30.720  ? 84  ASN YYY CA  1 
ATOM 20468 C C   . ASN O 3 84  ? 120.411 -52.527 7.613   1.000 29.630  ? 84  ASN YYY C   1 
ATOM 20469 O O   . ASN O 3 84  ? 120.169 -51.938 8.669   1.000 33.590  ? 84  ASN YYY O   1 
ATOM 20470 C CB  . ASN O 3 84  ? 122.757 -52.515 6.757   1.000 33.110  ? 84  ASN YYY CB  1 
ATOM 20471 C CG  . ASN O 3 84  ? 123.742 -51.945 5.750   1.000 38.600  ? 84  ASN YYY CG  1 
ATOM 20472 O OD1 . ASN O 3 84  ? 123.360 -51.340 4.746   1.000 41.280  ? 84  ASN YYY OD1 1 
ATOM 20473 N ND2 . ASN O 3 84  ? 125.030 -52.118 6.007   1.000 37.110  ? 84  ASN YYY ND2 1 
ATOM 20474 N N   . SER O 3 85  ? 119.879 -53.694 7.256   1.000 29.420  ? 85  SER YYY N   1 
ATOM 20475 C CA  . SER O 3 85  ? 119.056 -54.559 8.141   1.000 29.550  ? 85  SER YYY CA  1 
ATOM 20476 C C   . SER O 3 85  ? 117.870 -53.762 8.674   1.000 30.740  ? 85  SER YYY C   1 
ATOM 20477 O O   . SER O 3 85  ? 117.496 -53.938 9.857   1.000 35.200  ? 85  SER YYY O   1 
ATOM 20478 C CB  . SER O 3 85  ? 119.871 -55.114 9.268   1.000 29.590  ? 85  SER YYY CB  1 
ATOM 20479 O OG  . SER O 3 85  ? 121.117 -55.634 8.832   1.000 29.670  ? 85  SER YYY OG  1 
ATOM 20480 N N   . LEU O 3 86  ? 117.289 -52.927 7.819   1.000 33.020  ? 86  LEU YYY N   1 
ATOM 20481 C CA  . LEU O 3 86  ? 116.165 -52.029 8.180   1.000 37.490  ? 86  LEU YYY CA  1 
ATOM 20482 C C   . LEU O 3 86  ? 115.023 -52.835 8.802   1.000 42.330  ? 86  LEU YYY C   1 
ATOM 20483 O O   . LEU O 3 86  ? 114.770 -53.955 8.361   1.000 40.670  ? 86  LEU YYY O   1 
ATOM 20484 C CB  . LEU O 3 86  ? 115.715 -51.265 6.937   1.000 35.310  ? 86  LEU YYY CB  1 
ATOM 20485 C CG  . LEU O 3 86  ? 116.516 -50.004 6.664   1.000 34.490  ? 86  LEU YYY CG  1 
ATOM 20486 C CD1 . LEU O 3 86  ? 116.271 -49.431 5.290   1.000 37.410  ? 86  LEU YYY CD1 1 
ATOM 20487 C CD2 . LEU O 3 86  ? 116.188 -48.969 7.686   1.000 33.540  ? 86  LEU YYY CD2 1 
ATOM 20488 N N   . ARG O 3 87  ? 114.368 -52.262 9.808   1.000 45.840  ? 87  ARG YYY N   1 
ATOM 20489 C CA  . ARG O 3 87  ? 113.211 -52.875 10.499  1.000 47.310  ? 87  ARG YYY CA  1 
ATOM 20490 C C   . ARG O 3 87  ? 112.018 -51.943 10.377  1.000 42.980  ? 87  ARG YYY C   1 
ATOM 20491 O O   . ARG O 3 87  ? 112.203 -50.809 9.911   1.000 36.590  ? 87  ARG YYY O   1 
ATOM 20492 C CB  . ARG O 3 87  ? 113.554 -53.110 11.964  1.000 53.140  ? 87  ARG YYY CB  1 
ATOM 20493 C CG  . ARG O 3 87  ? 114.932 -53.728 12.167  1.000 54.920  ? 87  ARG YYY CG  1 
ATOM 20494 C CD  . ARG O 3 87  ? 115.247 -53.711 13.645  1.000 54.410  ? 87  ARG YYY CD  1 
ATOM 20495 N NE  . ARG O 3 87  ? 116.512 -54.336 13.952  1.000 55.500  ? 87  ARG YYY NE  1 
ATOM 20496 C CZ  . ARG O 3 87  ? 117.116 -54.207 15.120  1.000 61.850  ? 87  ARG YYY CZ  1 
ATOM 20497 N NH1 . ARG O 3 87  ? 116.558 -53.464 16.058  1.000 65.990  ? 87  ARG YYY NH1 1 
ATOM 20498 N NH2 . ARG O 3 87  ? 118.277 -54.793 15.355  1.000 64.670  ? 87  ARG YYY NH2 1 
ATOM 20499 N N   . VAL O 3 88  ? 110.847 -52.422 10.783  1.000 44.370  ? 88  VAL YYY N   1 
ATOM 20500 C CA  . VAL O 3 88  ? 109.572 -51.650 10.704  1.000 42.880  ? 88  VAL YYY CA  1 
ATOM 20501 C C   . VAL O 3 88  ? 109.726 -50.408 11.591  1.000 43.040  ? 88  VAL YYY C   1 
ATOM 20502 O O   . VAL O 3 88  ? 109.358 -49.299 11.123  1.000 36.600  ? 88  VAL YYY O   1 
ATOM 20503 C CB  . VAL O 3 88  ? 108.358 -52.500 11.120  1.000 40.920  ? 88  VAL YYY CB  1 
ATOM 20504 C CG1 . VAL O 3 88  ? 107.075 -51.699 10.990  1.000 40.270  ? 88  VAL YYY CG1 1 
ATOM 20505 C CG2 . VAL O 3 88  ? 108.270 -53.805 10.342  1.000 44.080  ? 88  VAL YYY CG2 1 
ATOM 20506 N N   . GLU O 3 89  ? 110.315 -50.572 12.786  1.000 46.470  ? 89  GLU YYY N   1 
ATOM 20507 C CA  . GLU O 3 89  ? 110.517 -49.486 13.784  1.000 50.890  ? 89  GLU YYY CA  1 
ATOM 20508 C C   . GLU O 3 89  ? 111.338 -48.349 13.166  1.000 48.150  ? 89  GLU YYY C   1 
ATOM 20509 O O   . GLU O 3 89  ? 111.097 -47.192 13.526  1.000 62.260  ? 89  GLU YYY O   1 
ATOM 20510 C CB  . GLU O 3 89  ? 111.220 -49.982 15.053  1.000 55.120  ? 89  GLU YYY CB  1 
ATOM 20511 C CG  . GLU O 3 89  ? 110.755 -51.346 15.535  1.000 58.680  ? 89  GLU YYY CG  1 
ATOM 20512 C CD  . GLU O 3 89  ? 111.696 -52.459 15.124  1.000 62.560  ? 89  GLU YYY CD  1 
ATOM 20513 O OE1 . GLU O 3 89  ? 112.816 -52.511 15.694  1.000 57.870  ? 89  GLU YYY OE1 1 
ATOM 20514 O OE2 . GLU O 3 89  ? 111.327 -53.227 14.200  1.000 68.300  ? 89  GLU YYY OE2 1 
ATOM 20515 N N   . ASP O 3 90  ? 112.251 -48.650 12.246  1.000 41.370  ? 90  ASP YYY N   1 
ATOM 20516 C CA  . ASP O 3 90  ? 113.147 -47.635 11.630  1.000 40.550  ? 90  ASP YYY CA  1 
ATOM 20517 C C   . ASP O 3 90  ? 112.361 -46.665 10.740  1.000 39.030  ? 90  ASP YYY C   1 
ATOM 20518 O O   . ASP O 3 90  ? 112.981 -45.685 10.262  1.000 41.310  ? 90  ASP YYY O   1 
ATOM 20519 C CB  . ASP O 3 90  ? 114.273 -48.284 10.833  1.000 40.390  ? 90  ASP YYY CB  1 
ATOM 20520 C CG  . ASP O 3 90  ? 115.236 -49.082 11.687  1.000 41.960  ? 90  ASP YYY CG  1 
ATOM 20521 O OD1 . ASP O 3 90  ? 115.351 -48.769 12.889  1.000 46.200  ? 90  ASP YYY OD1 1 
ATOM 20522 O OD2 . ASP O 3 90  ? 115.883 -49.994 11.128  1.000 38.950  ? 90  ASP YYY OD2 1 
ATOM 20523 N N   . THR O 3 91  ? 111.066 -46.905 10.502  1.000 36.270  ? 91  THR YYY N   1 
ATOM 20524 C CA  . THR O 3 91  ? 110.199 -45.968 9.744   1.000 35.670  ? 91  THR YYY CA  1 
ATOM 20525 C C   . THR O 3 91  ? 110.183 -44.630 10.475  1.000 39.320  ? 91  THR YYY C   1 
ATOM 20526 O O   . THR O 3 91  ? 109.844 -44.628 11.681  1.000 45.380  ? 91  THR YYY O   1 
ATOM 20527 C CB  . THR O 3 91  ? 108.766 -46.471 9.589   1.000 35.100  ? 91  THR YYY CB  1 
ATOM 20528 O OG1 . THR O 3 91  ? 108.868 -47.654 8.815   1.000 34.490  ? 91  THR YYY OG1 1 
ATOM 20529 C CG2 . THR O 3 91  ? 107.866 -45.477 8.894   1.000 36.390  ? 91  THR YYY CG2 1 
ATOM 20530 N N   . ALA O 3 92  ? 110.538 -43.555 9.767   1.000 38.620  ? 92  ALA YYY N   1 
ATOM 20531 C CA  . ALA O 3 92  ? 110.587 -42.176 10.296  1.000 39.150  ? 92  ALA YYY CA  1 
ATOM 20532 C C   . ALA O 3 92  ? 110.961 -41.195 9.193   1.000 36.970  ? 92  ALA YYY C   1 
ATOM 20533 O O   . ALA O 3 92  ? 111.414 -41.644 8.151   1.000 41.520  ? 92  ALA YYY O   1 
ATOM 20534 C CB  . ALA O 3 92  ? 111.590 -42.101 11.420  1.000 43.110  ? 92  ALA YYY CB  1 
ATOM 20535 N N   . VAL O 3 93  ? 110.775 -39.906 9.443   1.000 35.140  ? 93  VAL YYY N   1 
ATOM 20536 C CA  . VAL O 3 93  ? 111.475 -38.817 8.710   1.000 35.920  ? 93  VAL YYY CA  1 
ATOM 20537 C C   . VAL O 3 93  ? 112.889 -38.729 9.297   1.000 33.070  ? 93  VAL YYY C   1 
ATOM 20538 O O   . VAL O 3 93  ? 113.004 -38.707 10.541  1.000 33.070  ? 93  VAL YYY O   1 
ATOM 20539 C CB  . VAL O 3 93  ? 110.731 -37.478 8.841   1.000 39.690  ? 93  VAL YYY CB  1 
ATOM 20540 C CG1 . VAL O 3 93  ? 111.455 -36.377 8.089   1.000 41.450  ? 93  VAL YYY CG1 1 
ATOM 20541 C CG2 . VAL O 3 93  ? 109.280 -37.588 8.396   1.000 41.740  ? 93  VAL YYY CG2 1 
ATOM 20542 N N   . TYR O 3 94  ? 113.915 -38.722 8.447   1.000 30.410  ? 94  TYR YYY N   1 
ATOM 20543 C CA  . TYR O 3 94  ? 115.350 -38.667 8.841   1.000 28.890  ? 94  TYR YYY CA  1 
ATOM 20544 C C   . TYR O 3 94  ? 115.859 -37.245 8.572   1.000 30.070  ? 94  TYR YYY C   1 
ATOM 20545 O O   . TYR O 3 94  ? 116.103 -36.884 7.394   1.000 28.720  ? 94  TYR YYY O   1 
ATOM 20546 C CB  . TYR O 3 94  ? 116.158 -39.755 8.127   1.000 26.620  ? 94  TYR YYY CB  1 
ATOM 20547 C CG  . TYR O 3 94  ? 116.000 -41.106 8.768   1.000 25.420  ? 94  TYR YYY CG  1 
ATOM 20548 C CD1 . TYR O 3 94  ? 114.770 -41.751 8.787   1.000 24.850  ? 94  TYR YYY CD1 1 
ATOM 20549 C CD2 . TYR O 3 94  ? 117.062 -41.715 9.410   1.000 24.400  ? 94  TYR YYY CD2 1 
ATOM 20550 C CE1 . TYR O 3 94  ? 114.602 -42.962 9.433   1.000 24.360  ? 94  TYR YYY CE1 1 
ATOM 20551 C CE2 . TYR O 3 94  ? 116.913 -42.925 10.061  1.000 24.150  ? 94  TYR YYY CE2 1 
ATOM 20552 C CZ  . TYR O 3 94  ? 115.675 -43.545 10.078  1.000 25.600  ? 94  TYR YYY CZ  1 
ATOM 20553 O OH  . TYR O 3 94  ? 115.518 -44.746 10.707  1.000 25.500  ? 94  TYR YYY OH  1 
ATOM 20554 N N   . TYR O 3 95  ? 115.950 -36.444 9.641   1.000 29.410  ? 95  TYR YYY N   1 
ATOM 20555 C CA  . TYR O 3 95  ? 116.501 -35.063 9.636   1.000 26.620  ? 95  TYR YYY CA  1 
ATOM 20556 C C   . TYR O 3 95  ? 118.037 -35.092 9.740   1.000 27.390  ? 95  TYR YYY C   1 
ATOM 20557 O O   . TYR O 3 95  ? 118.649 -35.988 10.357  1.000 27.610  ? 95  TYR YYY O   1 
ATOM 20558 C CB  . TYR O 3 95  ? 115.823 -34.192 10.703  1.000 25.280  ? 95  TYR YYY CB  1 
ATOM 20559 C CG  . TYR O 3 95  ? 114.339 -33.972 10.539  1.000 25.390  ? 95  TYR YYY CG  1 
ATOM 20560 C CD1 . TYR O 3 95  ? 113.848 -33.076 9.615   1.000 26.920  ? 95  TYR YYY CD1 1 
ATOM 20561 C CD2 . TYR O 3 95  ? 113.408 -34.622 11.333  1.000 27.310  ? 95  TYR YYY CD2 1 
ATOM 20562 C CE1 . TYR O 3 95  ? 112.478 -32.850 9.463   1.000 28.530  ? 95  TYR YYY CE1 1 
ATOM 20563 C CE2 . TYR O 3 95  ? 112.037 -34.414 11.198  1.000 28.420  ? 95  TYR YYY CE2 1 
ATOM 20564 C CZ  . TYR O 3 95  ? 111.558 -33.517 10.257  1.000 27.520  ? 95  TYR YYY CZ  1 
ATOM 20565 N N   . CYS O 3 96  ? 118.686 -34.076 9.160   1.000 30.450  ? 96  CYS YYY N   1 
ATOM 20566 C CA  . CYS O 3 96  ? 120.168 -33.918 9.192   1.000 33.070  ? 96  CYS YYY CA  1 
ATOM 20567 C C   . CYS O 3 96  ? 120.411 -32.616 9.947   1.000 34.270  ? 96  CYS YYY C   1 
ATOM 20568 O O   . CYS O 3 96  ? 119.807 -31.617 9.554   1.000 33.210  ? 96  CYS YYY O   1 
ATOM 20569 C CB  . CYS O 3 96  ? 120.691 -33.830 7.761   1.000 34.090  ? 96  CYS YYY CB  1 
ATOM 20570 S SG  . CYS O 3 96  ? 122.253 -32.964 7.477   1.000 35.990  ? 96  CYS YYY SG  1 
ATOM 20571 N N   . ALA O 3 97  ? 121.241 -32.628 10.991  1.000 31.660  ? 97  ALA YYY N   1 
ATOM 20572 C CA  . ALA O 3 97  ? 121.380 -31.434 11.850  1.000 30.720  ? 97  ALA YYY CA  1 
ATOM 20573 C C   . ALA O 3 97  ? 122.840 -31.086 12.122  1.000 28.030  ? 97  ALA YYY C   1 
ATOM 20574 O O   . ALA O 3 97  ? 123.658 -31.990 12.121  1.000 25.730  ? 97  ALA YYY O   1 
ATOM 20575 C CB  . ALA O 3 97  ? 120.631 -31.694 13.122  1.000 31.200  ? 97  ALA YYY CB  1 
ATOM 20576 N N   . ARG O 3 98  ? 123.128 -29.813 12.392  1.000 26.670  ? 98  ARG YYY N   1 
ATOM 20577 C CA  . ARG O 3 98  ? 124.520 -29.349 12.599  1.000 28.820  ? 98  ARG YYY CA  1 
ATOM 20578 C C   . ARG O 3 98  ? 124.761 -29.044 14.068  1.000 30.620  ? 98  ARG YYY C   1 
ATOM 20579 O O   . ARG O 3 98  ? 123.896 -28.425 14.675  1.000 31.920  ? 98  ARG YYY O   1 
ATOM 20580 C CB  . ARG O 3 98  ? 124.762 -28.059 11.812  1.000 28.260  ? 98  ARG YYY CB  1 
ATOM 20581 C CG  . ARG O 3 98  ? 126.165 -27.485 11.929  1.000 28.100  ? 98  ARG YYY CG  1 
ATOM 20582 C CD  . ARG O 3 98  ? 126.244 -26.160 11.206  1.000 29.200  ? 98  ARG YYY CD  1 
ATOM 20583 N NE  . ARG O 3 98  ? 126.033 -25.025 12.084  1.000 30.360  ? 98  ARG YYY NE  1 
ATOM 20584 C CZ  . ARG O 3 98  ? 126.298 -23.770 11.757  1.000 33.420  ? 98  ARG YYY CZ  1 
ATOM 20585 N NH1 . ARG O 3 98  ? 126.794 -23.485 10.568  1.000 35.310  ? 98  ARG YYY NH1 1 
ATOM 20586 N NH2 . ARG O 3 98  ? 126.071 -22.800 12.620  1.000 33.280  ? 98  ARG YYY NH2 1 
ATOM 20587 N N   . TYR O 3 99  ? 125.904 -29.472 14.603  1.000 30.980  ? 99  TYR YYY N   1 
ATOM 20588 C CA  . TYR O 3 99  ? 126.262 -29.097 15.988  1.000 27.640  ? 99  TYR YYY CA  1 
ATOM 20589 C C   . TYR O 3 99  ? 127.321 -28.015 15.912  1.000 28.230  ? 99  TYR YYY C   1 
ATOM 20590 O O   . TYR O 3 99  ? 128.286 -28.163 15.159  1.000 28.450  ? 99  TYR YYY O   1 
ATOM 20591 C CB  . TYR O 3 99  ? 126.787 -30.278 16.802  1.000 24.370  ? 99  TYR YYY CB  1 
ATOM 20592 C CG  . TYR O 3 99  ? 127.471 -29.916 18.094  1.000 23.220  ? 99  TYR YYY CG  1 
ATOM 20593 C CD1 . TYR O 3 99  ? 126.746 -29.721 19.252  1.000 21.940  ? 99  TYR YYY CD1 1 
ATOM 20594 C CD2 . TYR O 3 99  ? 128.846 -29.776 18.168  1.000 23.250  ? 99  TYR YYY CD2 1 
ATOM 20595 C CE1 . TYR O 3 99  ? 127.362 -29.382 20.443  1.000 21.070  ? 99  TYR YYY CE1 1 
ATOM 20596 C CE2 . TYR O 3 99  ? 129.479 -29.428 19.348  1.000 21.750  ? 99  TYR YYY CE2 1 
ATOM 20597 C CZ  . TYR O 3 99  ? 128.733 -29.234 20.493  1.000 19.890  ? 99  TYR YYY CZ  1 
ATOM 20598 O OH  . TYR O 3 99  ? 129.345 -28.900 21.664  1.000 17.260  ? 99  TYR YYY OH  1 
ATOM 20599 N N   . ALA O 3 100 ? 127.118 -26.947 16.666  1.000 27.690  ? 100 ALA YYY N   1 
ATOM 20600 C CA  . ALA O 3 100 ? 128.145 -25.904 16.752  1.000 28.150  ? 100 ALA YYY CA  1 
ATOM 20601 C C   . ALA O 3 100 ? 128.420 -25.681 18.231  1.000 25.000  ? 100 ALA YYY C   1 
ATOM 20602 O O   . ALA O 3 100 ? 127.516 -25.854 19.014  1.000 21.620  ? 100 ALA YYY O   1 
ATOM 20603 C CB  . ALA O 3 100 ? 127.645 -24.669 16.088  1.000 30.330  ? 100 ALA YYY CB  1 
ATOM 20604 N N   . HIS O 3 101 ? 129.647 -25.336 18.579  1.000 25.420  ? 101 HIS YYY N   1 
ATOM 20605 C CA  . HIS O 3 101 ? 130.019 -25.086 19.987  1.000 28.680  ? 101 HIS YYY CA  1 
ATOM 20606 C C   . HIS O 3 101 ? 129.115 -24.007 20.561  1.000 33.030  ? 101 HIS YYY C   1 
ATOM 20607 O O   . HIS O 3 101 ? 128.926 -23.018 19.842  1.000 53.170  ? 101 HIS YYY O   1 
ATOM 20608 C CB  . HIS O 3 101 ? 131.484 -24.650 20.054  1.000 26.070  ? 101 HIS YYY CB  1 
ATOM 20609 C CG  . HIS O 3 101 ? 132.061 -24.608 21.422  1.000 22.170  ? 101 HIS YYY CG  1 
ATOM 20610 N ND1 . HIS O 3 101 ? 132.546 -23.449 21.969  1.000 21.720  ? 101 HIS YYY ND1 1 
ATOM 20611 C CD2 . HIS O 3 101 ? 132.244 -25.573 22.343  1.000 20.270  ? 101 HIS YYY CD2 1 
ATOM 20612 C CE1 . HIS O 3 101 ? 133.001 -23.698 23.174  1.000 20.730  ? 101 HIS YYY CE1 1 
ATOM 20613 N NE2 . HIS O 3 101 ? 132.823 -24.989 23.429  1.000 20.260  ? 101 HIS YYY NE2 1 
ATOM 20614 N N   . ASP O 3 102 ? 128.566 -24.209 21.761  1.000 29.060  ? 102 ASP YYY N   1 
ATOM 20615 C CA  . ASP O 3 102 ? 127.717 -23.213 22.470  1.000 26.800  ? 102 ASP YYY CA  1 
ATOM 20616 C C   . ASP O 3 102 ? 126.303 -23.191 21.893  1.000 25.800  ? 102 ASP YYY C   1 
ATOM 20617 O O   . ASP O 3 102 ? 125.358 -23.224 22.682  1.000 22.260  ? 102 ASP YYY O   1 
ATOM 20618 C CB  . ASP O 3 102 ? 128.379 -21.842 22.536  1.000 27.970  ? 102 ASP YYY CB  1 
ATOM 20619 C CG  . ASP O 3 102 ? 128.031 -21.035 23.756  1.000 26.740  ? 102 ASP YYY CG  1 
ATOM 20620 O OD1 . ASP O 3 102 ? 128.055 -21.602 24.855  1.000 25.620  ? 102 ASP YYY OD1 1 
ATOM 20621 O OD2 . ASP O 3 102 ? 127.773 -19.845 23.583  1.000 28.550  ? 102 ASP YYY OD2 1 
ATOM 20622 N N   . TRP O 3 103 ? 126.178 -23.137 20.572  1.000 25.640  ? 103 TRP YYY N   1 
ATOM 20623 C CA  . TRP O 3 103 ? 124.866 -23.084 19.899  1.000 25.420  ? 103 TRP YYY CA  1 
ATOM 20624 C C   . TRP O 3 103 ? 124.264 -24.470 19.990  1.000 26.530  ? 103 TRP YYY C   1 
ATOM 20625 O O   . TRP O 3 103 ? 123.039 -24.557 19.929  1.000 25.780  ? 103 TRP YYY O   1 
ATOM 20626 C CB  . TRP O 3 103 ? 125.089 -22.689 18.444  1.000 25.470  ? 103 TRP YYY CB  1 
ATOM 20627 C CG  . TRP O 3 103 ? 125.335 -21.238 18.187  1.000 25.900  ? 103 TRP YYY CG  1 
ATOM 20628 C CD1 . TRP O 3 103 ? 126.541 -20.615 18.075  1.000 29.250  ? 103 TRP YYY CD1 1 
ATOM 20629 C CD2 . TRP O 3 103 ? 124.338 -20.231 17.960  1.000 25.360  ? 103 TRP YYY CD2 1 
ATOM 20630 N NE1 . TRP O 3 103 ? 126.361 -19.286 17.812  1.000 28.370  ? 103 TRP YYY NE1 1 
ATOM 20631 C CE2 . TRP O 3 103 ? 125.021 -19.021 17.735  1.000 25.640  ? 103 TRP YYY CE2 1 
ATOM 20632 C CE3 . TRP O 3 103 ? 122.941 -20.231 17.933  1.000 27.120  ? 103 TRP YYY CE3 1 
ATOM 20633 C CZ2 . TRP O 3 103 ? 124.350 -17.828 17.483  1.000 25.660  ? 103 TRP YYY CZ2 1 
ATOM 20634 C CZ3 . TRP O 3 103 ? 122.280 -19.051 17.689  1.000 25.380  ? 103 TRP YYY CZ3 1 
ATOM 20635 C CH2 . TRP O 3 103 ? 122.976 -17.865 17.473  1.000 25.450  ? 103 TRP YYY CH2 1 
ATOM 20636 N N   . ASN O 3 104 ? 125.111 -25.491 20.103  1.000 28.330  ? 104 ASN YYY N   1 
ATOM 20637 C CA  . ASN O 3 104 ? 124.680 -26.904 20.225  1.000 30.330  ? 104 ASN YYY CA  1 
ATOM 20638 C C   . ASN O 3 104 ? 124.045 -27.328 18.902  1.000 31.490  ? 104 ASN YYY C   1 
ATOM 20639 O O   . ASN O 3 104 ? 124.507 -26.839 17.879  1.000 31.740  ? 104 ASN YYY O   1 
ATOM 20640 C CB  . ASN O 3 104 ? 123.965 -27.180 21.550  1.000 32.600  ? 104 ASN YYY CB  1 
ATOM 20641 C CG  . ASN O 3 104 ? 124.797 -26.858 22.771  1.000 32.650  ? 104 ASN YYY CG  1 
ATOM 20642 O OD1 . ASN O 3 104 ? 124.429 -26.000 23.564  1.000 37.240  ? 104 ASN YYY OD1 1 
ATOM 20643 N ND2 . ASN O 3 104 ? 125.909 -27.549 22.940  1.000 29.970  ? 104 ASN YYY ND2 1 
ATOM 20644 N N   . VAL O 3 105 ? 123.048 -28.208 18.913  1.000 34.010  ? 105 VAL YYY N   1 
ATOM 20645 C CA  . VAL O 3 105 ? 122.366 -28.542 17.630  1.000 31.830  ? 105 VAL YYY CA  1 
ATOM 20646 C C   . VAL O 3 105 ? 121.566 -27.314 17.204  1.000 31.180  ? 105 VAL YYY C   1 
ATOM 20647 O O   . VAL O 3 105 ? 120.720 -26.878 17.983  1.000 31.210  ? 105 VAL YYY O   1 
ATOM 20648 C CB  . VAL O 3 105 ? 121.550 -29.847 17.685  1.000 29.840  ? 105 VAL YYY CB  1 
ATOM 20649 C CG1 . VAL O 3 105 ? 120.676 -30.009 16.459  1.000 27.410  ? 105 VAL YYY CG1 1 
ATOM 20650 C CG2 . VAL O 3 105 ? 122.452 -31.058 17.842  1.000 30.140  ? 105 VAL YYY CG2 1 
ATOM 20651 N N   . ASP O 3 106 ? 121.872 -26.751 16.031  1.000 28.390  ? 106 ASP YYY N   1 
ATOM 20652 C CA  . ASP O 3 106 ? 121.234 -25.480 15.604  1.000 25.290  ? 106 ASP YYY CA  1 
ATOM 20653 C C   . ASP O 3 106 ? 120.428 -25.625 14.317  1.000 23.620  ? 106 ASP YYY C   1 
ATOM 20654 O O   . ASP O 3 106 ? 119.205 -25.453 14.373  1.000 23.790  ? 106 ASP YYY O   1 
ATOM 20655 C CB  . ASP O 3 106 ? 122.265 -24.353 15.462  1.000 23.390  ? 106 ASP YYY CB  1 
ATOM 20656 C CG  . ASP O 3 106 ? 123.594 -24.671 14.808  1.000 22.770  ? 106 ASP YYY CG  1 
ATOM 20657 O OD1 . ASP O 3 106 ? 123.653 -25.597 14.003  1.000 23.410  ? 106 ASP YYY OD1 1 
ATOM 20658 O OD2 . ASP O 3 106 ? 124.549 -23.943 15.083  1.000 24.490  ? 106 ASP YYY OD2 1 
ATOM 20659 N N   . TYR O 3 107 ? 121.091 -25.903 13.200  1.000 23.250  ? 107 TYR YYY N   1 
ATOM 20660 C CA  . TYR O 3 107 ? 120.393 -25.905 11.897  1.000 24.450  ? 107 TYR YYY CA  1 
ATOM 20661 C C   . TYR O 3 107 ? 119.956 -27.309 11.514  1.000 27.010  ? 107 TYR YYY C   1 
ATOM 20662 O O   . TYR O 3 107 ? 120.716 -28.238 11.756  1.000 24.120  ? 107 TYR YYY O   1 
ATOM 20663 C CB  . TYR O 3 107 ? 121.260 -25.244 10.830  1.000 23.360  ? 107 TYR YYY CB  1 
ATOM 20664 C CG  . TYR O 3 107 ? 121.357 -23.746 10.921  1.000 25.420  ? 107 TYR YYY CG  1 
ATOM 20665 C CD1 . TYR O 3 107 ? 120.327 -22.939 10.477  1.000 26.280  ? 107 TYR YYY CD1 1 
ATOM 20666 C CD2 . TYR O 3 107 ? 122.488 -23.135 11.430  1.000 27.410  ? 107 TYR YYY CD2 1 
ATOM 20667 C CE1 . TYR O 3 107 ? 120.414 -21.560 10.544  1.000 27.180  ? 107 TYR YYY CE1 1 
ATOM 20668 C CE2 . TYR O 3 107 ? 122.592 -21.758 11.503  1.000 28.680  ? 107 TYR YYY CE2 1 
ATOM 20669 C CZ  . TYR O 3 107 ? 121.551 -20.968 11.057  1.000 29.990  ? 107 TYR YYY CZ  1 
ATOM 20670 O OH  . TYR O 3 107 ? 121.643 -19.611 11.126  1.000 34.140  ? 107 TYR YYY OH  1 
ATOM 20671 N N   . TRP O 3 108 ? 118.764 -27.421 10.922  1.000 29.130  ? 108 TRP YYY N   1 
ATOM 20672 C CA  . TRP O 3 108 ? 118.194 -28.727 10.523  1.000 27.180  ? 108 TRP YYY CA  1 
ATOM 20673 C C   . TRP O 3 108 ? 117.814 -28.671 9.047   1.000 27.480  ? 108 TRP YYY C   1 
ATOM 20674 O O   . TRP O 3 108 ? 117.608 -27.559 8.554   1.000 28.260  ? 108 TRP YYY O   1 
ATOM 20675 C CB  . TRP O 3 108 ? 116.939 -29.023 11.345  1.000 28.150  ? 108 TRP YYY CB  1 
ATOM 20676 C CG  . TRP O 3 108 ? 117.089 -29.181 12.826  1.000 28.620  ? 108 TRP YYY CG  1 
ATOM 20677 C CD1 . TRP O 3 108 ? 117.433 -28.223 13.730  1.000 27.810  ? 108 TRP YYY CD1 1 
ATOM 20678 C CD2 . TRP O 3 108 ? 116.811 -30.366 13.589  1.000 29.300  ? 108 TRP YYY CD2 1 
ATOM 20679 N NE1 . TRP O 3 108 ? 117.432 -28.740 14.993  1.000 29.280  ? 108 TRP YYY NE1 1 
ATOM 20680 C CE2 . TRP O 3 108 ? 117.048 -30.051 14.941  1.000 27.660  ? 108 TRP YYY CE2 1 
ATOM 20681 C CE3 . TRP O 3 108 ? 116.406 -31.663 13.264  1.000 31.360  ? 108 TRP YYY CE3 1 
ATOM 20682 C CZ2 . TRP O 3 108 ? 116.894 -30.984 15.961  1.000 28.240  ? 108 TRP YYY CZ2 1 
ATOM 20683 C CZ3 . TRP O 3 108 ? 116.250 -32.585 14.272  1.000 30.480  ? 108 TRP YYY CZ3 1 
ATOM 20684 C CH2 . TRP O 3 108 ? 116.493 -32.248 15.602  1.000 29.430  ? 108 TRP YYY CH2 1 
ATOM 20685 N N   . GLY O 3 109 ? 117.762 -29.813 8.364   1.000 29.410  ? 109 GLY YYY N   1 
ATOM 20686 C CA  . GLY O 3 109 ? 117.280 -29.895 6.971   1.000 31.230  ? 109 GLY YYY CA  1 
ATOM 20687 C C   . GLY O 3 109 ? 115.782 -30.086 6.943   1.000 32.530  ? 109 GLY YYY C   1 
ATOM 20688 O O   . GLY O 3 109 ? 115.192 -30.005 8.019   1.000 30.760  ? 109 GLY YYY O   1 
ATOM 20689 N N   . GLN O 3 110 ? 115.207 -30.337 5.765   1.000 39.420  ? 110 GLN YYY N   1 
ATOM 20690 C CA  . GLN O 3 110 ? 113.749 -30.450 5.542   1.000 44.110  ? 110 GLN YYY CA  1 
ATOM 20691 C C   . GLN O 3 110 ? 113.292 -31.844 5.995   1.000 38.520  ? 110 GLN YYY C   1 
ATOM 20692 O O   . GLN O 3 110 ? 112.093 -32.018 6.271   1.000 37.190  ? 110 GLN YYY O   1 
ATOM 20693 C CB  . GLN O 3 110 ? 113.380 -30.221 4.072   1.000 53.080  ? 110 GLN YYY CB  1 
ATOM 20694 C CG  . GLN O 3 110 ? 113.682 -28.814 3.566   1.000 63.260  ? 110 GLN YYY CG  1 
ATOM 20695 C CD  . GLN O 3 110 ? 115.106 -28.654 3.080   1.000 73.320  ? 110 GLN YYY CD  1 
ATOM 20696 O OE1 . GLN O 3 110 ? 115.814 -29.637 2.829   1.000 80.370  ? 110 GLN YYY OE1 1 
ATOM 20697 N NE2 . GLN O 3 110 ? 115.540 -27.404 2.946   1.000 70.350  ? 110 GLN YYY NE2 1 
ATOM 20698 N N   . GLY O 3 111 ? 114.239 -32.781 6.075   1.000 35.270  ? 111 GLY YYY N   1 
ATOM 20699 C CA  . GLY O 3 111 ? 114.000 -34.200 6.377   1.000 38.230  ? 111 GLY YYY CA  1 
ATOM 20700 C C   . GLY O 3 111 ? 113.647 -34.985 5.128   1.000 39.840  ? 111 GLY YYY C   1 
ATOM 20701 O O   . GLY O 3 111 ? 113.156 -34.358 4.188   1.000 41.500  ? 111 GLY YYY O   1 
ATOM 20702 N N   . THR O 3 112 ? 113.904 -36.299 5.120   1.000 39.970  ? 112 THR YYY N   1 
ATOM 20703 C CA  . THR O 3 112 ? 113.560 -37.229 4.009   1.000 38.510  ? 112 THR YYY CA  1 
ATOM 20704 C C   . THR O 3 112 ? 112.884 -38.465 4.595   1.000 35.840  ? 112 THR YYY C   1 
ATOM 20705 O O   . THR O 3 112 ? 113.373 -38.960 5.610   1.000 34.740  ? 112 THR YYY O   1 
ATOM 20706 C CB  . THR O 3 112 ? 114.792 -37.612 3.179   1.000 38.570  ? 112 THR YYY CB  1 
ATOM 20707 O OG1 . THR O 3 112 ? 114.286 -38.283 2.026   1.000 37.000  ? 112 THR YYY OG1 1 
ATOM 20708 C CG2 . THR O 3 112 ? 115.773 -38.486 3.932   1.000 37.790  ? 112 THR YYY CG2 1 
ATOM 20709 N N   . LEU O 3 113 ? 111.791 -38.921 3.990   1.000 38.880  ? 113 LEU YYY N   1 
ATOM 20710 C CA  . LEU O 3 113 ? 110.951 -39.993 4.588   1.000 42.450  ? 113 LEU YYY CA  1 
ATOM 20711 C C   . LEU O 3 113 ? 111.531 -41.358 4.228   1.000 41.830  ? 113 LEU YYY C   1 
ATOM 20712 O O   . LEU O 3 113 ? 111.737 -41.611 3.033   1.000 49.610  ? 113 LEU YYY O   1 
ATOM 20713 C CB  . LEU O 3 113 ? 109.499 -39.886 4.105   1.000 45.580  ? 113 LEU YYY CB  1 
ATOM 20714 C CG  . LEU O 3 113 ? 108.581 -40.985 4.643   1.000 46.440  ? 113 LEU YYY CG  1 
ATOM 20715 C CD1 . LEU O 3 113 ? 108.614 -41.017 6.157   1.000 47.610  ? 113 LEU YYY CD1 1 
ATOM 20716 C CD2 . LEU O 3 113 ? 107.155 -40.811 4.154   1.000 46.910  ? 113 LEU YYY CD2 1 
ATOM 20717 N N   . VAL O 3 114 ? 111.749 -42.198 5.236   1.000 39.810  ? 114 VAL YYY N   1 
ATOM 20718 C CA  . VAL O 3 114 ? 112.094 -43.645 5.095   1.000 40.070  ? 114 VAL YYY CA  1 
ATOM 20719 C C   . VAL O 3 114 ? 110.922 -44.466 5.631   1.000 36.950  ? 114 VAL YYY C   1 
ATOM 20720 O O   . VAL O 3 114 ? 110.701 -44.426 6.839   1.000 37.290  ? 114 VAL YYY O   1 
ATOM 20721 C CB  . VAL O 3 114 ? 113.398 -44.010 5.813   1.000 40.540  ? 114 VAL YYY CB  1 
ATOM 20722 C CG1 . VAL O 3 114 ? 113.599 -45.513 5.895   1.000 39.120  ? 114 VAL YYY CG1 1 
ATOM 20723 C CG2 . VAL O 3 114 ? 114.610 -43.376 5.141   1.000 41.900  ? 114 VAL YYY CG2 1 
ATOM 20724 N N   . THR O 3 115 ? 110.209 -45.170 4.749   1.000 37.160  ? 115 THR YYY N   1 
ATOM 20725 C CA  . THR O 3 115 ? 109.111 -46.095 5.121   1.000 41.360  ? 115 THR YYY CA  1 
ATOM 20726 C C   . THR O 3 115 ? 109.550 -47.543 4.913   1.000 42.460  ? 115 THR YYY C   1 
ATOM 20727 O O   . THR O 3 115 ? 109.853 -47.898 3.779   1.000 43.000  ? 115 THR YYY O   1 
ATOM 20728 C CB  . THR O 3 115 ? 107.820 -45.775 4.364   1.000 45.610  ? 115 THR YYY CB  1 
ATOM 20729 O OG1 . THR O 3 115 ? 107.798 -44.360 4.160   1.000 50.340  ? 115 THR YYY OG1 1 
ATOM 20730 C CG2 . THR O 3 115 ? 106.594 -46.230 5.130   1.000 46.470  ? 115 THR YYY CG2 1 
ATOM 20731 N N   . VAL O 3 116 ? 109.585 -48.322 5.996   1.000 40.720  ? 116 VAL YYY N   1 
ATOM 20732 C CA  . VAL O 3 116 ? 109.944 -49.768 5.997   1.000 40.600  ? 116 VAL YYY CA  1 
ATOM 20733 C C   . VAL O 3 116 ? 108.688 -50.585 6.286   1.000 40.930  ? 116 VAL YYY C   1 
ATOM 20734 O O   . VAL O 3 116 ? 108.259 -50.637 7.439   1.000 51.170  ? 116 VAL YYY O   1 
ATOM 20735 C CB  . VAL O 3 116 ? 111.036 -50.072 7.034   1.000 44.010  ? 116 VAL YYY CB  1 
ATOM 20736 C CG1 . VAL O 3 116 ? 111.248 -51.567 7.202   1.000 48.690  ? 116 VAL YYY CG1 1 
ATOM 20737 C CG2 . VAL O 3 116 ? 112.344 -49.367 6.730   1.000 45.080  ? 116 VAL YYY CG2 1 
ATOM 20738 N N   . SER O 3 117 ? 108.165 -51.247 5.268   1.000 44.610  ? 117 SER YYY N   1 
ATOM 20739 C CA  . SER O 3 117 ? 106.905 -52.036 5.326   1.000 47.300  ? 117 SER YYY CA  1 
ATOM 20740 C C   . SER O 3 117 ? 107.101 -53.331 4.547   1.000 43.920  ? 117 SER YYY C   1 
ATOM 20741 O O   . SER O 3 117 ? 107.855 -53.304 3.550   1.000 46.600  ? 117 SER YYY O   1 
ATOM 20742 C CB  . SER O 3 117 ? 105.752 -51.207 4.805   1.000 51.690  ? 117 SER YYY CB  1 
ATOM 20743 O OG  . SER O 3 117 ? 104.513 -51.910 4.794   1.000 47.170  ? 117 SER YYY OG  1 
ATOM 20744 N N   . SER O 3 118 ? 106.518 -54.408 5.063   1.000 46.270  ? 118 SER YYY N   1 
ATOM 20745 C CA  . SER O 3 118 ? 106.515 -55.762 4.444   1.000 47.830  ? 118 SER YYY CA  1 
ATOM 20746 C C   . SER O 3 118 ? 105.514 -55.759 3.292   1.000 50.530  ? 118 SER YYY C   1 
ATOM 20747 O O   . SER O 3 118 ? 105.774 -56.502 2.326   1.000 61.940  ? 118 SER YYY O   1 
ATOM 20748 C CB  . SER O 3 118 ? 106.251 -56.862 5.444   1.000 43.130  ? 118 SER YYY CB  1 
ATOM 20749 O OG  . SER O 3 118 ? 104.900 -56.809 5.902   1.000 44.280  ? 118 SER YYY OG  1 
ATOM 20750 N N   . ALA O 3 119 ? 104.473 -54.920 3.373   1.000 48.540  ? 119 ALA YYY N   1 
ATOM 20751 C CA  . ALA O 3 119 ? 103.428 -54.724 2.337   1.000 53.140  ? 119 ALA YYY CA  1 
ATOM 20752 C C   . ALA O 3 119 ? 104.056 -54.531 0.955   1.000 55.760  ? 119 ALA YYY C   1 
ATOM 20753 O O   . ALA O 3 119 ? 105.065 -53.811 0.872   1.000 60.350  ? 119 ALA YYY O   1 
ATOM 20754 C CB  . ALA O 3 119 ? 102.553 -53.540 2.682   1.000 55.060  ? 119 ALA YYY CB  1 
ATOM 20755 N N   . SER O 3 120 ? 103.504 -55.195 -0.070  1.000 61.750  ? 120 SER YYY N   1 
ATOM 20756 C CA  . SER O 3 120 ? 103.888 -55.036 -1.498  1.000 59.830  ? 120 SER YYY CA  1 
ATOM 20757 C C   . SER O 3 120 ? 102.806 -54.218 -2.202  1.000 57.660  ? 120 SER YYY C   1 
ATOM 20758 O O   . SER O 3 120 ? 101.666 -54.168 -1.676  1.000 54.210  ? 120 SER YYY O   1 
ATOM 20759 C CB  . SER O 3 120 ? 104.125 -56.357 -2.184  1.000 59.670  ? 120 SER YYY CB  1 
ATOM 20760 O OG  . SER O 3 120 ? 104.872 -57.225 -1.353  1.000 57.800  ? 120 SER YYY OG  1 
ATOM 20761 N N   . THR O 3 121 ? 103.153 -53.656 -3.362  1.000 59.630  ? 121 THR YYY N   1 
ATOM 20762 C CA  . THR O 3 121 ? 102.384 -52.584 -4.047  1.000 64.690  ? 121 THR YYY CA  1 
ATOM 20763 C C   . THR O 3 121 ? 101.210 -53.219 -4.821  1.000 60.120  ? 121 THR YYY C   1 
ATOM 20764 O O   . THR O 3 121 ? 101.343 -53.386 -6.033  1.000 65.480  ? 121 THR YYY O   1 
ATOM 20765 C CB  . THR O 3 121 ? 103.287 -51.640 -4.878  1.000 69.410  ? 121 THR YYY CB  1 
ATOM 20766 O OG1 . THR O 3 121 ? 103.541 -52.088 -6.213  1.000 66.210  ? 121 THR YYY OG1 1 
ATOM 20767 C CG2 . THR O 3 121 ? 104.631 -51.347 -4.234  1.000 70.450  ? 121 THR YYY CG2 1 
ATOM 20768 N N   . LYS O 3 122 ? 100.073 -53.462 -4.152  1.000 60.700  ? 122 LYS YYY N   1 
ATOM 20769 C CA  . LYS O 3 122 ? 98.738  -53.600 -4.824  1.000 58.470  ? 122 LYS YYY CA  1 
ATOM 20770 C C   . LYS O 3 122 ? 98.339  -52.229 -5.412  1.000 56.950  ? 122 LYS YYY C   1 
ATOM 20771 O O   . LYS O 3 122 ? 98.582  -51.184 -4.796  1.000 49.500  ? 122 LYS YYY O   1 
ATOM 20772 C CB  . LYS O 3 122 ? 97.642  -54.151 -3.896  1.000 48.240  ? 122 LYS YYY CB  1 
ATOM 20773 N N   . GLY O 3 123 ? 97.742  -52.254 -6.599  1.000 60.960  ? 123 GLY YYY N   1 
ATOM 20774 C CA  . GLY O 3 123 ? 96.980  -51.130 -7.170  1.000 64.500  ? 123 GLY YYY CA  1 
ATOM 20775 C C   . GLY O 3 123 ? 95.636  -50.993 -6.469  1.000 69.160  ? 123 GLY YYY C   1 
ATOM 20776 O O   . GLY O 3 123 ? 95.145  -51.944 -5.847  1.000 82.570  ? 123 GLY YYY O   1 
ATOM 20777 N N   . PRO O 3 124 ? 94.995  -49.807 -6.539  1.000 70.840  ? 124 PRO YYY N   1 
ATOM 20778 C CA  . PRO O 3 124 ? 93.701  -49.584 -5.886  1.000 69.540  ? 124 PRO YYY CA  1 
ATOM 20779 C C   . PRO O 3 124 ? 92.541  -50.199 -6.672  1.000 74.250  ? 124 PRO YYY C   1 
ATOM 20780 O O   . PRO O 3 124 ? 92.748  -50.632 -7.811  1.000 75.920  ? 124 PRO YYY O   1 
ATOM 20781 C CB  . PRO O 3 124 ? 93.562  -48.059 -5.871  1.000 67.200  ? 124 PRO YYY CB  1 
ATOM 20782 C CG  . PRO O 3 124 ? 94.331  -47.607 -7.074  1.000 69.890  ? 124 PRO YYY CG  1 
ATOM 20783 C CD  . PRO O 3 124 ? 95.465  -48.607 -7.244  1.000 74.600  ? 124 PRO YYY CD  1 
ATOM 20784 N N   . SER O 3 125 ? 91.368  -50.235 -6.040  1.000 73.890  ? 125 SER YYY N   1 
ATOM 20785 C CA  . SER O 3 125 ? 90.066  -50.575 -6.675  1.000 71.390  ? 125 SER YYY CA  1 
ATOM 20786 C C   . SER O 3 125 ? 89.055  -49.486 -6.298  1.000 76.170  ? 125 SER YYY C   1 
ATOM 20787 O O   . SER O 3 125 ? 88.983  -49.139 -5.090  1.000 75.850  ? 125 SER YYY O   1 
ATOM 20788 C CB  . SER O 3 125 ? 89.596  -51.952 -6.304  1.000 66.750  ? 125 SER YYY CB  1 
ATOM 20789 O OG  . SER O 3 125 ? 89.942  -52.288 -4.971  1.000 62.120  ? 125 SER YYY OG  1 
ATOM 20790 N N   . VAL O 3 126 ? 88.386  -48.907 -7.304  1.000 75.030  ? 126 VAL YYY N   1 
ATOM 20791 C CA  . VAL O 3 126 ? 87.538  -47.689 -7.150  1.000 75.600  ? 126 VAL YYY CA  1 
ATOM 20792 C C   . VAL O 3 126 ? 86.068  -48.144 -7.159  1.000 75.050  ? 126 VAL YYY C   1 
ATOM 20793 O O   . VAL O 3 126 ? 85.692  -48.979 -8.004  1.000 70.280  ? 126 VAL YYY O   1 
ATOM 20794 C CB  . VAL O 3 126 ? 87.859  -46.615 -8.212  1.000 77.700  ? 126 VAL YYY CB  1 
ATOM 20795 C CG1 . VAL O 3 126 ? 87.273  -45.278 -7.810  1.000 86.330  ? 126 VAL YYY CG1 1 
ATOM 20796 C CG2 . VAL O 3 126 ? 89.349  -46.462 -8.475  1.000 78.870  ? 126 VAL YYY CG2 1 
ATOM 20797 N N   . PHE O 3 127 ? 85.297  -47.716 -6.165  1.000 76.520  ? 127 PHE YYY N   1 
ATOM 20798 C CA  . PHE O 3 127 ? 83.855  -48.015 -6.039  1.000 80.810  ? 127 PHE YYY CA  1 
ATOM 20799 C C   . PHE O 3 127 ? 83.163  -46.664 -6.119  1.000 81.900  ? 127 PHE YYY C   1 
ATOM 20800 O O   . PHE O 3 127 ? 83.730  -45.674 -5.682  1.000 71.850  ? 127 PHE YYY O   1 
ATOM 20801 C CB  . PHE O 3 127 ? 83.572  -48.799 -4.750  1.000 91.040  ? 127 PHE YYY CB  1 
ATOM 20802 C CG  . PHE O 3 127 ? 83.853  -50.289 -4.786  1.000 96.520  ? 127 PHE YYY CG  1 
ATOM 20803 C CD1 . PHE O 3 127 ? 85.150  -50.775 -4.912  1.000 88.460  ? 127 PHE YYY CD1 1 
ATOM 20804 C CD2 . PHE O 3 127 ? 82.820  -51.212 -4.624  1.000 95.000  ? 127 PHE YYY CD2 1 
ATOM 20805 C CE1 . PHE O 3 127 ? 85.402  -52.139 -4.908  1.000 84.530  ? 127 PHE YYY CE1 1 
ATOM 20806 C CE2 . PHE O 3 127 ? 83.072  -52.575 -4.629  1.000 89.170  ? 127 PHE YYY CE2 1 
ATOM 20807 C CZ  . PHE O 3 127 ? 84.361  -53.033 -4.777  1.000 90.640  ? 127 PHE YYY CZ  1 
ATOM 20808 N N   . PRO O 3 128 ? 81.961  -46.567 -6.733  1.000 89.290  ? 128 PRO YYY N   1 
ATOM 20809 C CA  . PRO O 3 128 ? 81.162  -45.347 -6.667  1.000 87.330  ? 128 PRO YYY CA  1 
ATOM 20810 C C   . PRO O 3 128 ? 80.475  -45.261 -5.290  1.000 83.300  ? 128 PRO YYY C   1 
ATOM 20811 O O   . PRO O 3 128 ? 79.972  -46.269 -4.824  1.000 82.840  ? 128 PRO YYY O   1 
ATOM 20812 C CB  . PRO O 3 128 ? 80.144  -45.531 -7.802  1.000 94.380  ? 128 PRO YYY CB  1 
ATOM 20813 C CG  . PRO O 3 128 ? 79.946  -47.039 -7.887  1.000 95.470  ? 128 PRO YYY CG  1 
ATOM 20814 C CD  . PRO O 3 128 ? 81.287  -47.632 -7.496  1.000 95.110  ? 128 PRO YYY CD  1 
ATOM 20815 N N   . LEU O 3 129 ? 80.527  -44.092 -4.652  1.000 78.610  ? 129 LEU YYY N   1 
ATOM 20816 C CA  . LEU O 3 129 ? 79.800  -43.809 -3.390  1.000 81.660  ? 129 LEU YYY CA  1 
ATOM 20817 C C   . LEU O 3 129 ? 78.577  -42.962 -3.755  1.000 87.700  ? 129 LEU YYY C   1 
ATOM 20818 O O   . LEU O 3 129 ? 78.702  -41.713 -3.823  1.000 91.080  ? 129 LEU YYY O   1 
ATOM 20819 C CB  . LEU O 3 129 ? 80.738  -43.107 -2.400  1.000 88.830  ? 129 LEU YYY CB  1 
ATOM 20820 C CG  . LEU O 3 129 ? 81.802  -43.989 -1.747  1.000 83.980  ? 129 LEU YYY CG  1 
ATOM 20821 C CD1 . LEU O 3 129 ? 81.244  -44.770 -0.572  1.000 81.670  ? 129 LEU YYY CD1 1 
ATOM 20822 C CD2 . LEU O 3 129 ? 82.382  -44.947 -2.758  1.000 85.010  ? 129 LEU YYY CD2 1 
ATOM 20823 N N   . ALA O 3 130 ? 77.453  -43.641 -4.021  1.000 88.730  ? 130 ALA YYY N   1 
ATOM 20824 C CA  . ALA O 3 130 ? 76.220  -43.090 -4.635  1.000 82.620  ? 130 ALA YYY CA  1 
ATOM 20825 C C   . ALA O 3 130 ? 75.377  -42.376 -3.576  1.000 89.260  ? 130 ALA YYY C   1 
ATOM 20826 O O   . ALA O 3 130 ? 75.473  -42.697 -2.388  1.000 91.810  ? 130 ALA YYY O   1 
ATOM 20827 C CB  . ALA O 3 130 ? 75.467  -44.213 -5.307  1.000 70.610  ? 130 ALA YYY CB  1 
ATOM 20828 N N   . PRO O 3 131 ? 74.567  -41.354 -3.957  1.000 89.630  ? 131 PRO YYY N   1 
ATOM 20829 C CA  . PRO O 3 131 ? 73.570  -40.761 -3.058  1.000 89.540  ? 131 PRO YYY CA  1 
ATOM 20830 C C   . PRO O 3 131 ? 72.115  -41.205 -3.321  1.000 83.430  ? 131 PRO YYY C   1 
ATOM 20831 O O   . PRO O 3 131 ? 71.453  -41.651 -2.379  1.000 68.880  ? 131 PRO YYY O   1 
ATOM 20832 C CB  . PRO O 3 131 ? 73.795  -39.283 -3.401  1.000 86.910  ? 131 PRO YYY CB  1 
ATOM 20833 C CG  . PRO O 3 131 ? 74.016  -39.292 -4.915  1.000 84.200  ? 131 PRO YYY CG  1 
ATOM 20834 C CD  . PRO O 3 131 ? 74.635  -40.637 -5.242  1.000 81.610  ? 131 PRO YYY CD  1 
ATOM 20835 N N   . ALA O 3 142 ? 77.179  -34.628 -1.256  1.000 92.010  ? 147 ALA YYY N   1 
ATOM 20836 C CA  . ALA O 3 142 ? 76.261  -35.748 -0.915  1.000 95.280  ? 147 ALA YYY CA  1 
ATOM 20837 C C   . ALA O 3 142 ? 76.725  -37.070 -1.567  1.000 104.060 ? 147 ALA YYY C   1 
ATOM 20838 O O   . ALA O 3 142 ? 76.195  -38.134 -1.157  1.000 106.270 ? 147 ALA YYY O   1 
ATOM 20839 C CB  . ALA O 3 142 ? 74.832  -35.390 -1.302  1.000 84.560  ? 147 ALA YYY CB  1 
ATOM 20840 N N   . LEU O 3 143 ? 77.646  -37.018 -2.548  1.000 105.670 ? 148 LEU YYY N   1 
ATOM 20841 C CA  . LEU O 3 143 ? 78.277  -38.204 -3.208  1.000 98.410  ? 148 LEU YYY CA  1 
ATOM 20842 C C   . LEU O 3 143 ? 79.805  -38.076 -3.171  1.000 92.010  ? 148 LEU YYY C   1 
ATOM 20843 O O   . LEU O 3 143 ? 80.315  -36.951 -2.929  1.000 88.530  ? 148 LEU YYY O   1 
ATOM 20844 C CB  . LEU O 3 143 ? 77.785  -38.369 -4.659  1.000 101.970 ? 148 LEU YYY CB  1 
ATOM 20845 C CG  . LEU O 3 143 ? 78.202  -37.309 -5.693  1.000 98.530  ? 148 LEU YYY CG  1 
ATOM 20846 C CD1 . LEU O 3 143 ? 79.608  -37.559 -6.260  1.000 91.770  ? 148 LEU YYY CD1 1 
ATOM 20847 C CD2 . LEU O 3 143 ? 77.204  -37.247 -6.838  1.000 93.270  ? 148 LEU YYY CD2 1 
ATOM 20848 N N   . GLY O 3 144 ? 80.494  -39.188 -3.464  1.000 83.520  ? 149 GLY YYY N   1 
ATOM 20849 C CA  . GLY O 3 144 ? 81.966  -39.278 -3.562  1.000 86.030  ? 149 GLY YYY CA  1 
ATOM 20850 C C   . GLY O 3 144 ? 82.455  -40.533 -4.282  1.000 90.330  ? 149 GLY YYY C   1 
ATOM 20851 O O   . GLY O 3 144 ? 81.628  -41.197 -4.941  1.000 93.210  ? 149 GLY YYY O   1 
ATOM 20852 N N   . CYS O 3 145 ? 83.757  -40.846 -4.150  1.000 97.610  ? 150 CYS YYY N   1 
ATOM 20853 C CA  . CYS O 3 145 ? 84.439  -42.085 -4.634  1.000 98.290  ? 150 CYS YYY CA  1 
ATOM 20854 C C   . CYS O 3 145 ? 85.196  -42.764 -3.482  1.000 94.140  ? 150 CYS YYY C   1 
ATOM 20855 O O   . CYS O 3 145 ? 85.595  -42.049 -2.549  1.000 91.440  ? 150 CYS YYY O   1 
ATOM 20856 C CB  . CYS O 3 145 ? 85.420  -41.769 -5.760  1.000 104.800 ? 150 CYS YYY CB  1 
ATOM 20857 S SG  . CYS O 3 145 ? 84.660  -41.523 -7.382  1.000 114.890 ? 150 CYS YYY SG  1 
ATOM 20858 N N   . LEU O 3 146 ? 85.378  -44.089 -3.566  1.000 102.180 ? 151 LEU YYY N   1 
ATOM 20859 C CA  . LEU O 3 146 ? 86.132  -44.945 -2.594  1.000 101.400 ? 151 LEU YYY CA  1 
ATOM 20860 C C   . LEU O 3 146 ? 87.342  -45.541 -3.323  1.000 92.360  ? 151 LEU YYY C   1 
ATOM 20861 O O   . LEU O 3 146 ? 87.167  -45.991 -4.473  1.000 113.450 ? 151 LEU YYY O   1 
ATOM 20862 C CB  . LEU O 3 146 ? 85.174  -46.025 -2.064  1.000 103.910 ? 151 LEU YYY CB  1 
ATOM 20863 C CG  . LEU O 3 146 ? 85.697  -47.081 -1.098  1.000 102.800 ? 151 LEU YYY CG  1 
ATOM 20864 C CD1 . LEU O 3 146 ? 86.353  -48.234 -1.833  1.000 105.190 ? 151 LEU YYY CD1 1 
ATOM 20865 C CD2 . LEU O 3 146 ? 86.619  -46.474 -0.059  1.000 112.650 ? 151 LEU YYY CD2 1 
ATOM 20866 N N   . VAL O 3 147 ? 88.536  -45.468 -2.726  1.000 75.320  ? 152 VAL YYY N   1 
ATOM 20867 C CA  . VAL O 3 147 ? 89.800  -46.061 -3.261  1.000 69.610  ? 152 VAL YYY CA  1 
ATOM 20868 C C   . VAL O 3 147 ? 90.310  -47.055 -2.209  1.000 68.150  ? 152 VAL YYY C   1 
ATOM 20869 O O   . VAL O 3 147 ? 90.742  -46.607 -1.116  1.000 68.160  ? 152 VAL YYY O   1 
ATOM 20870 C CB  . VAL O 3 147 ? 90.830  -44.959 -3.583  1.000 68.340  ? 152 VAL YYY CB  1 
ATOM 20871 C CG1 . VAL O 3 147 ? 92.148  -45.508 -4.139  1.000 67.900  ? 152 VAL YYY CG1 1 
ATOM 20872 C CG2 . VAL O 3 147 ? 90.233  -43.905 -4.511  1.000 68.200  ? 152 VAL YYY CG2 1 
ATOM 20873 N N   . LYS O 3 148 ? 90.205  -48.358 -2.501  1.000 69.890  ? 153 LYS YYY N   1 
ATOM 20874 C CA  . LYS O 3 148 ? 90.365  -49.442 -1.487  1.000 74.070  ? 153 LYS YYY CA  1 
ATOM 20875 C C   . LYS O 3 148 ? 91.640  -50.235 -1.772  1.000 69.760  ? 153 LYS YYY C   1 
ATOM 20876 O O   . LYS O 3 148 ? 92.004  -50.351 -2.962  1.000 72.290  ? 153 LYS YYY O   1 
ATOM 20877 C CB  . LYS O 3 148 ? 89.146  -50.376 -1.401  1.000 76.060  ? 153 LYS YYY CB  1 
ATOM 20878 C CG  . LYS O 3 148 ? 88.929  -50.940 0.007   1.000 78.670  ? 153 LYS YYY CG  1 
ATOM 20879 C CD  . LYS O 3 148 ? 87.814  -51.966 0.157   1.000 81.420  ? 153 LYS YYY CD  1 
ATOM 20880 C CE  . LYS O 3 148 ? 87.886  -53.113 -0.833  1.000 79.950  ? 153 LYS YYY CE  1 
ATOM 20881 N NZ  . LYS O 3 148 ? 87.100  -54.285 -0.380  1.000 78.090  ? 153 LYS YYY NZ  1 
ATOM 20882 N N   . ASP O 3 149 ? 92.275  -50.730 -0.695  1.000 63.420  ? 154 ASP YYY N   1 
ATOM 20883 C CA  . ASP O 3 149 ? 93.408  -51.703 -0.670  1.000 64.330  ? 154 ASP YYY CA  1 
ATOM 20884 C C   . ASP O 3 149 ? 94.465  -51.346 -1.738  1.000 66.860  ? 154 ASP YYY C   1 
ATOM 20885 O O   . ASP O 3 149 ? 94.592  -52.113 -2.747  1.000 72.330  ? 154 ASP YYY O   1 
ATOM 20886 C CB  . ASP O 3 149 ? 92.908  -53.154 -0.793  1.000 61.050  ? 154 ASP YYY CB  1 
ATOM 20887 C CG  . ASP O 3 149 ? 91.862  -53.566 0.234   1.000 62.830  ? 154 ASP YYY CG  1 
ATOM 20888 O OD1 . ASP O 3 149 ? 92.108  -53.398 1.441   1.000 64.380  ? 154 ASP YYY OD1 1 
ATOM 20889 O OD2 . ASP O 3 149 ? 90.810  -54.062 -0.182  1.000 64.260  ? 154 ASP YYY OD2 1 
ATOM 20890 N N   . TYR O 3 150 ? 95.205  -50.241 -1.534  1.000 69.850  ? 155 TYR YYY N   1 
ATOM 20891 C CA  . TYR O 3 150 ? 96.343  -49.797 -2.379  1.000 66.480  ? 155 TYR YYY CA  1 
ATOM 20892 C C   . TYR O 3 150 ? 97.594  -49.618 -1.506  1.000 73.830  ? 155 TYR YYY C   1 
ATOM 20893 O O   . TYR O 3 150 ? 97.481  -49.450 -0.284  1.000 72.740  ? 155 TYR YYY O   1 
ATOM 20894 C CB  . TYR O 3 150 ? 96.014  -48.511 -3.142  1.000 64.070  ? 155 TYR YYY CB  1 
ATOM 20895 C CG  . TYR O 3 150 ? 95.989  -47.251 -2.318  1.000 61.460  ? 155 TYR YYY CG  1 
ATOM 20896 C CD1 . TYR O 3 150 ? 97.159  -46.574 -2.007  1.000 61.950  ? 155 TYR YYY CD1 1 
ATOM 20897 C CD2 . TYR O 3 150 ? 94.790  -46.705 -1.889  1.000 58.740  ? 155 TYR YYY CD2 1 
ATOM 20898 C CE1 . TYR O 3 150 ? 97.140  -45.408 -1.258  1.000 59.830  ? 155 TYR YYY CE1 1 
ATOM 20899 C CE2 . TYR O 3 150 ? 94.758  -45.533 -1.151  1.000 60.530  ? 155 TYR YYY CE2 1 
ATOM 20900 C CZ  . TYR O 3 150 ? 95.938  -44.884 -0.823  1.000 58.920  ? 155 TYR YYY CZ  1 
ATOM 20901 O OH  . TYR O 3 150 ? 95.956  -43.728 -0.089  1.000 49.920  ? 155 TYR YYY OH  1 
ATOM 20902 N N   . PHE O 3 151 ? 98.769  -49.649 -2.146  1.000 82.720  ? 156 PHE YYY N   1 
ATOM 20903 C CA  . PHE O 3 151 ? 100.115 -49.497 -1.528  1.000 77.700  ? 156 PHE YYY CA  1 
ATOM 20904 C C   . PHE O 3 151 ? 101.121 -49.135 -2.624  1.000 77.210  ? 156 PHE YYY C   1 
ATOM 20905 O O   . PHE O 3 151 ? 101.028 -49.693 -3.715  1.000 67.090  ? 156 PHE YYY O   1 
ATOM 20906 C CB  . PHE O 3 151 ? 100.542 -50.794 -0.836  1.000 71.610  ? 156 PHE YYY CB  1 
ATOM 20907 C CG  . PHE O 3 151 ? 101.772 -50.645 0.024   1.000 69.610  ? 156 PHE YYY CG  1 
ATOM 20908 C CD1 . PHE O 3 151 ? 101.688 -49.991 1.245   1.000 68.390  ? 156 PHE YYY CD1 1 
ATOM 20909 C CD2 . PHE O 3 151 ? 103.007 -51.136 -0.377  1.000 66.910  ? 156 PHE YYY CD2 1 
ATOM 20910 C CE1 . PHE O 3 151 ? 102.809 -49.801 2.033   1.000 68.730  ? 156 PHE YYY CE1 1 
ATOM 20911 C CE2 . PHE O 3 151 ? 104.128 -50.942 0.414   1.000 70.760  ? 156 PHE YYY CE2 1 
ATOM 20912 C CZ  . PHE O 3 151 ? 104.023 -50.292 1.625   1.000 69.200  ? 156 PHE YYY CZ  1 
ATOM 20913 N N   . PRO O 3 152 ? 102.095 -48.209 -2.421  1.000 78.670  ? 157 PRO YYY N   1 
ATOM 20914 C CA  . PRO O 3 152 ? 102.173 -47.334 -1.244  1.000 72.880  ? 157 PRO YYY CA  1 
ATOM 20915 C C   . PRO O 3 152 ? 101.347 -46.041 -1.306  1.000 68.540  ? 157 PRO YYY C   1 
ATOM 20916 O O   . PRO O 3 152 ? 100.490 -45.949 -2.166  1.000 49.880  ? 157 PRO YYY O   1 
ATOM 20917 C CB  . PRO O 3 152 ? 103.676 -47.050 -1.171  1.000 77.770  ? 157 PRO YYY CB  1 
ATOM 20918 C CG  . PRO O 3 152 ? 104.111 -47.022 -2.624  1.000 80.570  ? 157 PRO YYY CG  1 
ATOM 20919 C CD  . PRO O 3 152 ? 103.272 -48.085 -3.291  1.000 79.090  ? 157 PRO YYY CD  1 
ATOM 20920 N N   . GLU O 3 153 ? 101.694 -45.070 -0.439  1.000 74.680  ? 158 GLU YYY N   1 
ATOM 20921 C CA  . GLU O 3 153 ? 100.793 -44.015 0.111   1.000 75.250  ? 158 GLU YYY CA  1 
ATOM 20922 C C   . GLU O 3 153 ? 100.258 -43.067 -0.961  1.000 84.590  ? 158 GLU YYY C   1 
ATOM 20923 O O   . GLU O 3 153 ? 99.050  -42.816 -0.978  1.000 100.830 ? 158 GLU YYY O   1 
ATOM 20924 C CB  . GLU O 3 153 ? 101.496 -43.240 1.231   1.000 70.510  ? 158 GLU YYY CB  1 
ATOM 20925 C CG  . GLU O 3 153 ? 100.729 -42.007 1.737   1.000 76.510  ? 158 GLU YYY CG  1 
ATOM 20926 C CD  . GLU O 3 153 ? 99.245  -42.142 2.085   1.000 71.270  ? 158 GLU YYY CD  1 
ATOM 20927 O OE1 . GLU O 3 153 ? 98.955  -42.442 3.245   1.000 75.090  ? 158 GLU YYY OE1 1 
ATOM 20928 O OE2 . GLU O 3 153 ? 98.381  -41.946 1.190   1.000 58.190  ? 158 GLU YYY OE2 1 
ATOM 20929 N N   . PRO O 3 154 ? 101.072 -42.485 -1.879  1.000 72.030  ? 159 PRO YYY N   1 
ATOM 20930 C CA  . PRO O 3 154 ? 100.580 -41.365 -2.698  1.000 62.360  ? 159 PRO YYY CA  1 
ATOM 20931 C C   . PRO O 3 154 ? 99.424  -41.715 -3.667  1.000 55.180  ? 159 PRO YYY C   1 
ATOM 20932 O O   . PRO O 3 154 ? 99.665  -42.338 -4.691  1.000 50.830  ? 159 PRO YYY O   1 
ATOM 20933 C CB  . PRO O 3 154 ? 101.849 -40.901 -3.433  1.000 59.470  ? 159 PRO YYY CB  1 
ATOM 20934 C CG  . PRO O 3 154 ? 102.767 -42.122 -3.457  1.000 58.590  ? 159 PRO YYY CG  1 
ATOM 20935 C CD  . PRO O 3 154 ? 102.440 -42.912 -2.211  1.000 58.890  ? 159 PRO YYY CD  1 
ATOM 20936 N N   . VAL O 3 155 ? 98.188  -41.317 -3.321  1.000 55.470  ? 160 VAL YYY N   1 
ATOM 20937 C CA  . VAL O 3 155 ? 96.997  -41.348 -4.238  1.000 62.550  ? 160 VAL YYY CA  1 
ATOM 20938 C C   . VAL O 3 155 ? 96.364  -39.944 -4.295  1.000 65.360  ? 160 VAL YYY C   1 
ATOM 20939 O O   . VAL O 3 155 ? 96.036  -39.394 -3.211  1.000 65.710  ? 160 VAL YYY O   1 
ATOM 20940 C CB  . VAL O 3 155 ? 95.934  -42.395 -3.837  1.000 58.590  ? 160 VAL YYY CB  1 
ATOM 20941 C CG1 . VAL O 3 155 ? 94.591  -42.188 -4.528  1.000 57.720  ? 160 VAL YYY CG1 1 
ATOM 20942 C CG2 . VAL O 3 155 ? 96.383  -43.821 -4.054  1.000 55.430  ? 160 VAL YYY CG2 1 
ATOM 20943 N N   . THR O 3 156 ? 96.145  -39.432 -5.517  1.000 65.580  ? 161 THR YYY N   1 
ATOM 20944 C CA  . THR O 3 156 ? 95.491  -38.129 -5.823  1.000 68.750  ? 161 THR YYY CA  1 
ATOM 20945 C C   . THR O 3 156 ? 94.124  -38.403 -6.446  1.000 75.130  ? 161 THR YYY C   1 
ATOM 20946 O O   . THR O 3 156 ? 94.004  -39.346 -7.271  1.000 67.970  ? 161 THR YYY O   1 
ATOM 20947 C CB  . THR O 3 156 ? 96.397  -37.254 -6.713  1.000 66.360  ? 161 THR YYY CB  1 
ATOM 20948 O OG1 . THR O 3 156 ? 96.677  -37.962 -7.925  1.000 63.270  ? 161 THR YYY OG1 1 
ATOM 20949 C CG2 . THR O 3 156 ? 97.689  -36.880 -6.017  1.000 67.780  ? 161 THR YYY CG2 1 
ATOM 20950 N N   . VAL O 3 157 ? 93.118  -37.616 -6.048  1.000 76.090  ? 162 VAL YYY N   1 
ATOM 20951 C CA  . VAL O 3 157 ? 91.715  -37.706 -6.552  1.000 71.770  ? 162 VAL YYY CA  1 
ATOM 20952 C C   . VAL O 3 157 ? 91.376  -36.332 -7.149  1.000 66.220  ? 162 VAL YYY C   1 
ATOM 20953 O O   . VAL O 3 157 ? 91.831  -35.316 -6.650  1.000 55.920  ? 162 VAL YYY O   1 
ATOM 20954 C CB  . VAL O 3 157 ? 90.716  -38.127 -5.439  1.000 70.690  ? 162 VAL YYY CB  1 
ATOM 20955 C CG1 . VAL O 3 157 ? 89.298  -38.237 -5.951  1.000 71.900  ? 162 VAL YYY CG1 1 
ATOM 20956 C CG2 . VAL O 3 157 ? 91.136  -39.446 -4.802  1.000 68.070  ? 162 VAL YYY CG2 1 
ATOM 20957 N N   . SER O 3 158 ? 90.597  -36.325 -8.221  1.000 72.160  ? 163 SER YYY N   1 
ATOM 20958 C CA  . SER O 3 158 ? 90.272  -35.162 -9.074  1.000 79.560  ? 163 SER YYY CA  1 
ATOM 20959 C C   . SER O 3 158 ? 88.921  -35.431 -9.734  1.000 96.150  ? 163 SER YYY C   1 
ATOM 20960 O O   . SER O 3 158 ? 88.501  -36.604 -9.669  1.000 109.950 ? 163 SER YYY O   1 
ATOM 20961 C CB  . SER O 3 158 ? 91.369  -34.903 -10.060 1.000 75.860  ? 163 SER YYY CB  1 
ATOM 20962 O OG  . SER O 3 158 ? 91.042  -33.805 -10.887 1.000 80.620  ? 163 SER YYY OG  1 
ATOM 20963 N N   . TRP O 3 159 ? 88.238  -34.421 -10.293 1.000 105.160 ? 164 TRP YYY N   1 
ATOM 20964 C CA  . TRP O 3 159 ? 86.875  -34.562 -10.903 1.000 94.410  ? 164 TRP YYY CA  1 
ATOM 20965 C C   . TRP O 3 159 ? 86.708  -33.849 -12.266 1.000 88.750  ? 164 TRP YYY C   1 
ATOM 20966 O O   . TRP O 3 159 ? 85.574  -33.899 -12.802 1.000 63.640  ? 164 TRP YYY O   1 
ATOM 20967 C CB  . TRP O 3 159 ? 85.880  -34.039 -9.847  1.000 86.240  ? 164 TRP YYY CB  1 
ATOM 20968 C CG  . TRP O 3 159 ? 85.942  -34.775 -8.537  1.000 80.100  ? 164 TRP YYY CG  1 
ATOM 20969 C CD1 . TRP O 3 159 ? 86.898  -34.644 -7.567  1.000 72.410  ? 164 TRP YYY CD1 1 
ATOM 20970 C CD2 . TRP O 3 159 ? 85.005  -35.758 -8.041  1.000 77.060  ? 164 TRP YYY CD2 1 
ATOM 20971 N NE1 . TRP O 3 159 ? 86.628  -35.479 -6.514  1.000 69.450  ? 164 TRP YYY NE1 1 
ATOM 20972 C CE2 . TRP O 3 159 ? 85.468  -36.169 -6.769  1.000 73.170  ? 164 TRP YYY CE2 1 
ATOM 20973 C CE3 . TRP O 3 159 ? 83.825  -36.330 -8.538  1.000 75.290  ? 164 TRP YYY CE3 1 
ATOM 20974 C CZ2 . TRP O 3 159 ? 84.794  -37.126 -6.005  1.000 70.650  ? 164 TRP YYY CZ2 1 
ATOM 20975 C CZ3 . TRP O 3 159 ? 83.163  -37.275 -7.781  1.000 73.500  ? 164 TRP YYY CZ3 1 
ATOM 20976 C CH2 . TRP O 3 159 ? 83.646  -37.670 -6.535  1.000 71.650  ? 164 TRP YYY CH2 1 
ATOM 20977 N N   . ASN O 3 160 ? 87.784  -33.237 -12.803 1.000 94.500  ? 165 ASN YYY N   1 
ATOM 20978 C CA  . ASN O 3 160 ? 87.795  -32.232 -13.905 1.000 92.420  ? 165 ASN YYY CA  1 
ATOM 20979 C C   . ASN O 3 160 ? 87.308  -30.870 -13.387 1.000 104.040 ? 165 ASN YYY C   1 
ATOM 20980 O O   . ASN O 3 160 ? 86.233  -30.416 -13.834 1.000 112.660 ? 165 ASN YYY O   1 
ATOM 20981 C CB  . ASN O 3 160 ? 86.954  -32.673 -15.104 1.000 88.050  ? 165 ASN YYY CB  1 
ATOM 20982 C CG  . ASN O 3 160 ? 87.409  -34.005 -15.641 1.000 86.650  ? 165 ASN YYY CG  1 
ATOM 20983 O OD1 . ASN O 3 160 ? 88.551  -34.385 -15.403 1.000 82.310  ? 165 ASN YYY OD1 1 
ATOM 20984 N ND2 . ASN O 3 160 ? 86.531  -34.701 -16.349 1.000 84.110  ? 165 ASN YYY ND2 1 
ATOM 20985 N N   . SER O 3 161 ? 88.081  -30.212 -12.517 1.000 99.480  ? 166 SER YYY N   1 
ATOM 20986 C CA  . SER O 3 161 ? 87.760  -28.876 -11.957 1.000 98.950  ? 166 SER YYY CA  1 
ATOM 20987 C C   . SER O 3 161 ? 86.300  -28.848 -11.472 1.000 97.950  ? 166 SER YYY C   1 
ATOM 20988 O O   . SER O 3 161 ? 85.504  -28.111 -12.085 1.000 95.000  ? 166 SER YYY O   1 
ATOM 20989 C CB  . SER O 3 161 ? 88.024  -27.796 -12.991 1.000 89.430  ? 166 SER YYY CB  1 
ATOM 20990 N N   . GLY O 3 162 ? 85.959  -29.660 -10.459 1.000 94.860  ? 167 GLY YYY N   1 
ATOM 20991 C CA  . GLY O 3 162 ? 84.787  -29.474 -9.564  1.000 93.850  ? 167 GLY YYY CA  1 
ATOM 20992 C C   . GLY O 3 162 ? 85.317  -29.018 -8.197  1.000 101.070 ? 167 GLY YYY C   1 
ATOM 20993 O O   . GLY O 3 162 ? 85.593  -29.893 -7.355  1.000 112.630 ? 167 GLY YYY O   1 
ATOM 20994 N N   . ALA O 3 163 ? 85.493  -27.701 -8.013  1.000 98.260  ? 168 ALA YYY N   1 
ATOM 20995 C CA  . ALA O 3 163 ? 86.017  -27.040 -6.790  1.000 86.930  ? 168 ALA YYY CA  1 
ATOM 20996 C C   . ALA O 3 163 ? 84.931  -26.130 -6.176  1.000 72.700  ? 168 ALA YYY C   1 
ATOM 20997 O O   . ALA O 3 163 ? 84.083  -26.646 -5.382  1.000 51.970  ? 168 ALA YYY O   1 
ATOM 20998 C CB  . ALA O 3 163 ? 87.279  -26.280 -7.148  1.000 79.790  ? 168 ALA YYY CB  1 
ATOM 20999 N N   . VAL O 3 168 ? 83.218  -30.734 -1.326  1.000 107.100 ? 173 VAL YYY N   1 
ATOM 21000 C CA  . VAL O 3 168 ? 84.307  -30.855 -2.346  1.000 104.960 ? 173 VAL YYY CA  1 
ATOM 21001 C C   . VAL O 3 168 ? 85.634  -31.286 -1.665  1.000 96.140  ? 173 VAL YYY C   1 
ATOM 21002 O O   . VAL O 3 168 ? 86.696  -30.732 -2.020  1.000 79.810  ? 173 VAL YYY O   1 
ATOM 21003 C CB  . VAL O 3 168 ? 84.438  -29.532 -3.137  1.000 99.940  ? 173 VAL YYY CB  1 
ATOM 21004 C CG1 . VAL O 3 168 ? 85.128  -29.780 -4.471  1.000 99.730  ? 173 VAL YYY CG1 1 
ATOM 21005 C CG2 . VAL O 3 168 ? 83.099  -28.807 -3.333  1.000 80.810  ? 173 VAL YYY CG2 1 
ATOM 21006 N N   . HIS O 3 169 ? 85.591  -32.285 -0.760  1.000 94.540  ? 174 HIS YYY N   1 
ATOM 21007 C CA  . HIS O 3 169 ? 86.646  -32.636 0.242   1.000 93.000  ? 174 HIS YYY CA  1 
ATOM 21008 C C   . HIS O 3 169 ? 87.065  -34.121 0.124   1.000 83.180  ? 174 HIS YYY C   1 
ATOM 21009 O O   . HIS O 3 169 ? 86.234  -34.989 0.429   1.000 70.080  ? 174 HIS YYY O   1 
ATOM 21010 C CB  . HIS O 3 169 ? 86.149  -32.240 1.654   1.000 96.290  ? 174 HIS YYY CB  1 
ATOM 21011 C CG  . HIS O 3 169 ? 87.017  -32.666 2.798   1.000 101.140 ? 174 HIS YYY CG  1 
ATOM 21012 N ND1 . HIS O 3 169 ? 86.577  -33.552 3.769   1.000 98.550  ? 174 HIS YYY ND1 1 
ATOM 21013 C CD2 . HIS O 3 169 ? 88.287  -32.344 3.142   1.000 102.010 ? 174 HIS YYY CD2 1 
ATOM 21014 C CE1 . HIS O 3 169 ? 87.534  -33.755 4.654   1.000 90.970  ? 174 HIS YYY CE1 1 
ATOM 21015 N NE2 . HIS O 3 169 ? 88.593  -33.030 4.289   1.000 95.410  ? 174 HIS YYY NE2 1 
ATOM 21016 N N   . THR O 3 170 ? 88.319  -34.377 -0.299  1.000 84.430  ? 175 THR YYY N   1 
ATOM 21017 C CA  . THR O 3 170 ? 89.073  -35.666 -0.218  1.000 84.730  ? 175 THR YYY CA  1 
ATOM 21018 C C   . THR O 3 170 ? 89.590  -35.837 1.217   1.000 93.150  ? 175 THR YYY C   1 
ATOM 21019 O O   . THR O 3 170 ? 90.044  -34.827 1.804   1.000 105.570 ? 175 THR YYY O   1 
ATOM 21020 C CB  . THR O 3 170 ? 90.283  -35.688 -1.173  1.000 79.880  ? 175 THR YYY CB  1 
ATOM 21021 O OG1 . THR O 3 170 ? 89.909  -35.443 -2.525  1.000 73.060  ? 175 THR YYY OG1 1 
ATOM 21022 C CG2 . THR O 3 170 ? 91.025  -37.006 -1.181  1.000 83.780  ? 175 THR YYY CG2 1 
ATOM 21023 N N   . PHE O 3 171 ? 89.538  -37.058 1.766   1.000 99.830  ? 176 PHE YYY N   1 
ATOM 21024 C CA  . PHE O 3 171 ? 90.015  -37.375 3.142   1.000 102.690 ? 176 PHE YYY CA  1 
ATOM 21025 C C   . PHE O 3 171 ? 91.431  -37.930 3.043   1.000 103.790 ? 176 PHE YYY C   1 
ATOM 21026 O O   . PHE O 3 171 ? 91.776  -38.556 2.046   1.000 116.850 ? 176 PHE YYY O   1 
ATOM 21027 C CB  . PHE O 3 171 ? 89.044  -38.306 3.881   1.000 99.590  ? 176 PHE YYY CB  1 
ATOM 21028 C CG  . PHE O 3 171 ? 87.771  -37.620 4.321   1.000 97.160  ? 176 PHE YYY CG  1 
ATOM 21029 C CD1 . PHE O 3 171 ? 86.905  -37.083 3.376   1.000 97.880  ? 176 PHE YYY CD1 1 
ATOM 21030 C CD2 . PHE O 3 171 ? 87.462  -37.449 5.661   1.000 88.730  ? 176 PHE YYY CD2 1 
ATOM 21031 C CE1 . PHE O 3 171 ? 85.743  -36.430 3.758   1.000 91.960  ? 176 PHE YYY CE1 1 
ATOM 21032 C CE2 . PHE O 3 171 ? 86.291  -36.790 6.037   1.000 88.930  ? 176 PHE YYY CE2 1 
ATOM 21033 C CZ  . PHE O 3 171 ? 85.446  -36.281 5.089   1.000 90.350  ? 176 PHE YYY CZ  1 
ATOM 21034 N N   . PRO O 3 172 ? 92.301  -37.736 4.066   1.000 97.880  ? 177 PRO YYY N   1 
ATOM 21035 C CA  . PRO O 3 172 ? 93.573  -38.458 4.134   1.000 81.520  ? 177 PRO YYY CA  1 
ATOM 21036 C C   . PRO O 3 172 ? 93.312  -39.942 4.425   1.000 68.390  ? 177 PRO YYY C   1 
ATOM 21037 O O   . PRO O 3 172 ? 92.307  -40.269 5.057   1.000 61.200  ? 177 PRO YYY O   1 
ATOM 21038 C CB  . PRO O 3 172 ? 94.331  -37.784 5.278   1.000 87.970  ? 177 PRO YYY CB  1 
ATOM 21039 C CG  . PRO O 3 172 ? 93.217  -37.250 6.172   1.000 100.620 ? 177 PRO YYY CG  1 
ATOM 21040 C CD  . PRO O 3 172 ? 92.092  -36.870 5.237   1.000 100.170 ? 177 PRO YYY CD  1 
ATOM 21041 N N   . ALA O 3 173 ? 94.209  -40.795 3.936   1.000 65.370  ? 178 ALA YYY N   1 
ATOM 21042 C CA  . ALA O 3 173 ? 94.043  -42.264 3.865   1.000 72.370  ? 178 ALA YYY CA  1 
ATOM 21043 C C   . ALA O 3 173 ? 94.035  -42.866 5.277   1.000 69.410  ? 178 ALA YYY C   1 
ATOM 21044 O O   . ALA O 3 173 ? 94.400  -42.165 6.245   1.000 62.450  ? 178 ALA YYY O   1 
ATOM 21045 C CB  . ALA O 3 173 ? 95.158  -42.843 3.021   1.000 78.950  ? 178 ALA YYY CB  1 
ATOM 21046 N N   . VAL O 3 174 ? 93.622  -44.130 5.381   1.000 64.980  ? 179 VAL YYY N   1 
ATOM 21047 C CA  . VAL O 3 174 ? 93.676  -44.933 6.634   1.000 71.930  ? 179 VAL YYY CA  1 
ATOM 21048 C C   . VAL O 3 174 ? 94.626  -46.099 6.364   1.000 73.830  ? 179 VAL YYY C   1 
ATOM 21049 O O   . VAL O 3 174 ? 94.553  -46.680 5.264   1.000 77.540  ? 179 VAL YYY O   1 
ATOM 21050 C CB  . VAL O 3 174 ? 92.288  -45.427 7.081   1.000 73.020  ? 179 VAL YYY CB  1 
ATOM 21051 C CG1 . VAL O 3 174 ? 91.783  -46.586 6.224   1.000 69.450  ? 179 VAL YYY CG1 1 
ATOM 21052 C CG2 . VAL O 3 174 ? 92.256  -45.822 8.557   1.000 76.410  ? 179 VAL YYY CG2 1 
ATOM 21053 N N   . LEU O 3 175 ? 95.523  -46.354 7.320   1.000 68.680  ? 180 LEU YYY N   1 
ATOM 21054 C CA  . LEU O 3 175 ? 96.451  -47.507 7.317   1.000 72.830  ? 180 LEU YYY CA  1 
ATOM 21055 C C   . LEU O 3 175 ? 95.732  -48.690 7.982   1.000 70.290  ? 180 LEU YYY C   1 
ATOM 21056 O O   . LEU O 3 175 ? 95.711  -48.745 9.223   1.000 76.670  ? 180 LEU YYY O   1 
ATOM 21057 C CB  . LEU O 3 175 ? 97.726  -47.097 8.067   1.000 73.810  ? 180 LEU YYY CB  1 
ATOM 21058 C CG  . LEU O 3 175 ? 98.943  -48.009 7.914   1.000 67.430  ? 180 LEU YYY CG  1 
ATOM 21059 C CD1 . LEU O 3 175 ? 99.441  -48.025 6.474   1.000 62.690  ? 180 LEU YYY CD1 1 
ATOM 21060 C CD2 . LEU O 3 175 ? 100.042 -47.565 8.878   1.000 64.120  ? 180 LEU YYY CD2 1 
ATOM 21061 N N   . GLN O 3 176 ? 95.136  -49.581 7.188   1.000 66.280  ? 181 GLN YYY N   1 
ATOM 21062 C CA  . GLN O 3 176 ? 94.538  -50.849 7.684   1.000 64.400  ? 181 GLN YYY CA  1 
ATOM 21063 C C   . GLN O 3 176 ? 95.686  -51.722 8.244   1.000 60.250  ? 181 GLN YYY C   1 
ATOM 21064 O O   . GLN O 3 176 ? 96.844  -51.515 7.871   1.000 55.470  ? 181 GLN YYY O   1 
ATOM 21065 C CB  . GLN O 3 176 ? 93.693  -51.492 6.571   1.000 63.830  ? 181 GLN YYY CB  1 
ATOM 21066 N N   . SER O 3 177 ? 95.364  -52.652 9.145   1.000 63.550  ? 182 SER YYY N   1 
ATOM 21067 C CA  . SER O 3 177 ? 96.282  -53.671 9.721   1.000 61.300  ? 182 SER YYY CA  1 
ATOM 21068 C C   . SER O 3 177 ? 96.921  -54.524 8.619   1.000 63.990  ? 182 SER YYY C   1 
ATOM 21069 O O   . SER O 3 177 ? 97.966  -55.109 8.902   1.000 79.680  ? 182 SER YYY O   1 
ATOM 21070 C CB  . SER O 3 177 ? 95.561  -54.545 10.723  1.000 59.990  ? 182 SER YYY CB  1 
ATOM 21071 O OG  . SER O 3 177 ? 94.438  -55.174 10.128  1.000 60.970  ? 182 SER YYY OG  1 
ATOM 21072 N N   . SER O 3 178 ? 96.315  -54.606 7.426   1.000 62.760  ? 183 SER YYY N   1 
ATOM 21073 C CA  . SER O 3 178 ? 96.850  -55.275 6.204   1.000 61.210  ? 183 SER YYY CA  1 
ATOM 21074 C C   . SER O 3 178 ? 98.213  -54.675 5.808   1.000 61.690  ? 183 SER YYY C   1 
ATOM 21075 O O   . SER O 3 178 ? 98.992  -55.337 5.065   1.000 53.870  ? 183 SER YYY O   1 
ATOM 21076 C CB  . SER O 3 178 ? 95.902  -55.152 5.024   1.000 62.960  ? 183 SER YYY CB  1 
ATOM 21077 O OG  . SER O 3 178 ? 94.542  -55.118 5.408   1.000 73.240  ? 183 SER YYY OG  1 
ATOM 21078 N N   . GLY O 3 179 ? 98.479  -53.431 6.235   1.000 70.520  ? 184 GLY YYY N   1 
ATOM 21079 C CA  . GLY O 3 179 ? 99.586  -52.595 5.709   1.000 72.620  ? 184 GLY YYY CA  1 
ATOM 21080 C C   . GLY O 3 179 ? 99.161  -51.861 4.444   1.000 74.400  ? 184 GLY YYY C   1 
ATOM 21081 O O   . GLY O 3 179 ? 100.004 -51.116 3.914   1.000 80.640  ? 184 GLY YYY O   1 
ATOM 21082 N N   . LEU O 3 180 ? 97.889  -52.013 4.043   1.000 71.130  ? 185 LEU YYY N   1 
ATOM 21083 C CA  . LEU O 3 180 ? 97.284  -51.468 2.795   1.000 63.210  ? 185 LEU YYY CA  1 
ATOM 21084 C C   . LEU O 3 180 ? 96.397  -50.282 3.173   1.000 57.460  ? 185 LEU YYY C   1 
ATOM 21085 O O   . LEU O 3 180 ? 95.683  -50.363 4.185   1.000 53.890  ? 185 LEU YYY O   1 
ATOM 21086 C CB  . LEU O 3 180 ? 96.427  -52.513 2.057   1.000 63.160  ? 185 LEU YYY CB  1 
ATOM 21087 C CG  . LEU O 3 180 ? 97.015  -53.867 1.629   1.000 67.310  ? 185 LEU YYY CG  1 
ATOM 21088 C CD1 . LEU O 3 180 ? 96.122  -54.505 0.561   1.000 64.210  ? 185 LEU YYY CD1 1 
ATOM 21089 C CD2 . LEU O 3 180 ? 98.468  -53.791 1.147   1.000 69.360  ? 185 LEU YYY CD2 1 
ATOM 21090 N N   . TYR O 3 181 ? 96.486  -49.203 2.392   1.000 61.060  ? 186 TYR YYY N   1 
ATOM 21091 C CA  . TYR O 3 181 ? 95.794  -47.913 2.624   1.000 62.040  ? 186 TYR YYY CA  1 
ATOM 21092 C C   . TYR O 3 181 ? 94.408  -47.958 1.968   1.000 57.990  ? 186 TYR YYY C   1 
ATOM 21093 O O   . TYR O 3 181 ? 94.174  -48.772 1.035   1.000 55.180  ? 186 TYR YYY O   1 
ATOM 21094 C CB  . TYR O 3 181 ? 96.628  -46.755 2.077   1.000 66.390  ? 186 TYR YYY CB  1 
ATOM 21095 C CG  . TYR O 3 181 ? 97.963  -46.512 2.741   1.000 68.740  ? 186 TYR YYY CG  1 
ATOM 21096 C CD1 . TYR O 3 181 ? 99.044  -47.348 2.522   1.000 65.260  ? 186 TYR YYY CD1 1 
ATOM 21097 C CD2 . TYR O 3 181 ? 98.152  -45.416 3.570   1.000 78.930  ? 186 TYR YYY CD2 1 
ATOM 21098 C CE1 . TYR O 3 181 ? 100.272 -47.113 3.123   1.000 71.050  ? 186 TYR YYY CE1 1 
ATOM 21099 C CE2 . TYR O 3 181 ? 99.367  -45.171 4.188   1.000 81.270  ? 186 TYR YYY CE2 1 
ATOM 21100 C CZ  . TYR O 3 181 ? 100.436 -46.015 3.952   1.000 79.810  ? 186 TYR YYY CZ  1 
ATOM 21101 O OH  . TYR O 3 181 ? 101.629 -45.749 4.556   1.000 86.130  ? 186 TYR YYY OH  1 
ATOM 21102 N N   . SER O 3 182 ? 93.511  -47.098 2.449   1.000 59.150  ? 187 SER YYY N   1 
ATOM 21103 C CA  . SER O 3 182 ? 92.200  -46.799 1.821   1.000 59.360  ? 187 SER YYY CA  1 
ATOM 21104 C C   . SER O 3 182 ? 91.904  -45.318 2.051   1.000 60.620  ? 187 SER YYY C   1 
ATOM 21105 O O   . SER O 3 182 ? 92.165  -44.875 3.175   1.000 53.410  ? 187 SER YYY O   1 
ATOM 21106 C CB  . SER O 3 182 ? 91.099  -47.672 2.384   1.000 58.210  ? 187 SER YYY CB  1 
ATOM 21107 O OG  . SER O 3 182 ? 91.349  -49.044 2.131   1.000 54.370  ? 187 SER YYY OG  1 
ATOM 21108 N N   . LEU O 3 183 ? 91.385  -44.607 1.040   1.000 65.710  ? 188 LEU YYY N   1 
ATOM 21109 C CA  . LEU O 3 183 ? 90.933  -43.193 1.172   1.000 74.490  ? 188 LEU YYY CA  1 
ATOM 21110 C C   . LEU O 3 183 ? 89.657  -42.997 0.344   1.000 81.750  ? 188 LEU YYY C   1 
ATOM 21111 O O   . LEU O 3 183 ? 89.522  -43.675 -0.685  1.000 85.800  ? 188 LEU YYY O   1 
ATOM 21112 C CB  . LEU O 3 183 ? 92.063  -42.213 0.818   1.000 74.040  ? 188 LEU YYY CB  1 
ATOM 21113 C CG  . LEU O 3 183 ? 92.626  -42.255 -0.607  1.000 82.760  ? 188 LEU YYY CG  1 
ATOM 21114 C CD1 . LEU O 3 183 ? 91.734  -41.506 -1.599  1.000 84.020  ? 188 LEU YYY CD1 1 
ATOM 21115 C CD2 . LEU O 3 183 ? 94.031  -41.683 -0.624  1.000 93.320  ? 188 LEU YYY CD2 1 
ATOM 21116 N N   . SER O 3 184 ? 88.760  -42.114 0.801   1.000 88.820  ? 189 SER YYY N   1 
ATOM 21117 C CA  . SER O 3 184 ? 87.487  -41.745 0.124   1.000 84.130  ? 189 SER YYY CA  1 
ATOM 21118 C C   . SER O 3 184 ? 87.416  -40.223 -0.066  1.000 74.760  ? 189 SER YYY C   1 
ATOM 21119 O O   . SER O 3 184 ? 88.200  -39.499 0.587   1.000 70.130  ? 189 SER YYY O   1 
ATOM 21120 C CB  . SER O 3 184 ? 86.314  -42.266 0.911   1.000 85.100  ? 189 SER YYY CB  1 
ATOM 21121 O OG  . SER O 3 184 ? 86.440  -41.929 2.277   1.000 93.800  ? 189 SER YYY OG  1 
ATOM 21122 N N   . SER O 3 185 ? 86.486  -39.769 -0.915  1.000 65.730  ? 190 SER YYY N   1 
ATOM 21123 C CA  . SER O 3 185 ? 86.399  -38.383 -1.449  1.000 62.450  ? 190 SER YYY CA  1 
ATOM 21124 C C   . SER O 3 185 ? 84.938  -38.030 -1.711  1.000 62.720  ? 190 SER YYY C   1 
ATOM 21125 O O   . SER O 3 185 ? 84.252  -38.854 -2.304  1.000 64.870  ? 190 SER YYY O   1 
ATOM 21126 C CB  . SER O 3 185 ? 87.226  -38.252 -2.701  1.000 55.900  ? 190 SER YYY CB  1 
ATOM 21127 O OG  . SER O 3 185 ? 87.217  -36.928 -3.174  1.000 45.580  ? 190 SER YYY OG  1 
ATOM 21128 N N   . VAL O 3 186 ? 84.480  -36.855 -1.264  1.000 68.310  ? 191 VAL YYY N   1 
ATOM 21129 C CA  . VAL O 3 186 ? 83.032  -36.476 -1.250  1.000 72.620  ? 191 VAL YYY CA  1 
ATOM 21130 C C   . VAL O 3 186 ? 82.856  -35.009 -1.652  1.000 82.020  ? 191 VAL YYY C   1 
ATOM 21131 O O   . VAL O 3 186 ? 83.749  -34.178 -1.313  1.000 76.880  ? 191 VAL YYY O   1 
ATOM 21132 C CB  . VAL O 3 186 ? 82.372  -36.728 0.118   1.000 69.530  ? 191 VAL YYY CB  1 
ATOM 21133 C CG1 . VAL O 3 186 ? 82.003  -38.187 0.296   1.000 71.930  ? 191 VAL YYY CG1 1 
ATOM 21134 C CG2 . VAL O 3 186 ? 83.223  -36.227 1.274   1.000 70.860  ? 191 VAL YYY CG2 1 
ATOM 21135 N N   . VAL O 3 187 ? 81.691  -34.722 -2.258  1.000 86.210  ? 192 VAL YYY N   1 
ATOM 21136 C CA  . VAL O 3 187 ? 81.306  -33.412 -2.861  1.000 79.180  ? 192 VAL YYY CA  1 
ATOM 21137 C C   . VAL O 3 187 ? 79.787  -33.204 -2.669  1.000 75.140  ? 192 VAL YYY C   1 
ATOM 21138 O O   . VAL O 3 187 ? 79.399  -32.320 -1.846  1.000 61.140  ? 192 VAL YYY O   1 
ATOM 21139 C CB  . VAL O 3 187 ? 81.791  -33.379 -4.331  1.000 73.270  ? 192 VAL YYY CB  1 
ATOM 21140 C CG1 . VAL O 3 187 ? 81.300  -34.572 -5.150  1.000 64.590  ? 192 VAL YYY CG1 1 
ATOM 21141 C CG2 . VAL O 3 187 ? 81.482  -32.055 -5.019  1.000 77.520  ? 192 VAL YYY CG2 1 
ATOM 21142 N N   . CYS O 3 201 ? 84.799  -39.467 -10.941 1.000 88.620  ? 206 CYS YYY N   1 
ATOM 21143 C CA  . CYS O 3 201 ? 86.062  -39.006 -10.303 1.000 86.210  ? 206 CYS YYY CA  1 
ATOM 21144 C C   . CYS O 3 201 ? 87.278  -39.582 -11.031 1.000 87.420  ? 206 CYS YYY C   1 
ATOM 21145 O O   . CYS O 3 201 ? 87.131  -40.607 -11.716 1.000 80.170  ? 206 CYS YYY O   1 
ATOM 21146 C CB  . CYS O 3 201 ? 86.145  -39.424 -8.841  1.000 90.340  ? 206 CYS YYY CB  1 
ATOM 21147 S SG  . CYS O 3 201 ? 86.240  -41.216 -8.605  1.000 85.460  ? 206 CYS YYY SG  1 
ATOM 21148 N N   . ASN O 3 202 ? 88.433  -38.941 -10.849 1.000 89.830  ? 207 ASN YYY N   1 
ATOM 21149 C CA  . ASN O 3 202 ? 89.731  -39.274 -11.499 1.000 96.890  ? 207 ASN YYY CA  1 
ATOM 21150 C C   . ASN O 3 202 ? 90.740  -39.585 -10.386 1.000 102.480 ? 207 ASN YYY C   1 
ATOM 21151 O O   . ASN O 3 202 ? 91.271  -38.631 -9.779  1.000 112.360 ? 207 ASN YYY O   1 
ATOM 21152 C CB  . ASN O 3 202 ? 90.263  -38.152 -12.410 1.000 94.200  ? 207 ASN YYY CB  1 
ATOM 21153 C CG  . ASN O 3 202 ? 89.224  -37.529 -13.322 1.000 91.970  ? 207 ASN YYY CG  1 
ATOM 21154 O OD1 . ASN O 3 202 ? 88.851  -36.373 -13.119 1.000 89.040  ? 207 ASN YYY OD1 1 
ATOM 21155 N ND2 . ASN O 3 202 ? 88.767  -38.269 -14.326 1.000 85.440  ? 207 ASN YYY ND2 1 
ATOM 21156 N N   . VAL O 3 203 ? 90.999  -40.874 -10.145 1.000 99.670  ? 208 VAL YYY N   1 
ATOM 21157 C CA  . VAL O 3 203 ? 92.016  -41.403 -9.188  1.000 93.950  ? 208 VAL YYY CA  1 
ATOM 21158 C C   . VAL O 3 203 ? 93.293  -41.725 -9.986  1.000 89.560  ? 208 VAL YYY C   1 
ATOM 21159 O O   . VAL O 3 203 ? 93.196  -42.251 -11.103 1.000 85.280  ? 208 VAL YYY O   1 
ATOM 21160 C CB  . VAL O 3 203 ? 91.452  -42.656 -8.475  1.000 93.950  ? 208 VAL YYY CB  1 
ATOM 21161 C CG1 . VAL O 3 203 ? 92.448  -43.314 -7.535  1.000 92.660  ? 208 VAL YYY CG1 1 
ATOM 21162 C CG2 . VAL O 3 203 ? 90.153  -42.374 -7.733  1.000 93.310  ? 208 VAL YYY CG2 1 
ATOM 21163 N N   . ASN O 3 204 ? 94.456  -41.421 -9.417  1.000 94.080  ? 209 ASN YYY N   1 
ATOM 21164 C CA  . ASN O 3 204 ? 95.798  -41.756 -9.964  1.000 89.400  ? 209 ASN YYY CA  1 
ATOM 21165 C C   . ASN O 3 204 ? 96.638  -42.361 -8.821  1.000 80.470  ? 209 ASN YYY C   1 
ATOM 21166 O O   . ASN O 3 204 ? 96.611  -41.802 -7.684  1.000 69.810  ? 209 ASN YYY O   1 
ATOM 21167 C CB  . ASN O 3 204 ? 96.425  -40.512 -10.601 1.000 92.190  ? 209 ASN YYY CB  1 
ATOM 21168 C CG  . ASN O 3 204 ? 97.561  -40.790 -11.571 1.000 96.100  ? 209 ASN YYY CG  1 
ATOM 21169 O OD1 . ASN O 3 204 ? 98.310  -41.765 -11.461 1.000 104.160 ? 209 ASN YYY OD1 1 
ATOM 21170 N ND2 . ASN O 3 204 ? 97.749  -39.873 -12.494 1.000 95.940  ? 209 ASN YYY ND2 1 
ATOM 21171 N N   . HIS O 3 205 ? 97.336  -43.461 -9.107  1.000 79.220  ? 210 HIS YYY N   1 
ATOM 21172 C CA  . HIS O 3 205 ? 98.256  -44.156 -8.169  1.000 77.840  ? 210 HIS YYY CA  1 
ATOM 21173 C C   . HIS O 3 205 ? 99.486  -44.659 -8.943  1.000 77.100  ? 210 HIS YYY C   1 
ATOM 21174 O O   . HIS O 3 205 ? 99.471  -45.841 -9.355  1.000 73.480  ? 210 HIS YYY O   1 
ATOM 21175 C CB  . HIS O 3 205 ? 97.475  -45.262 -7.446  1.000 71.510  ? 210 HIS YYY CB  1 
ATOM 21176 C CG  . HIS O 3 205 ? 98.260  -46.009 -6.418  1.000 66.620  ? 210 HIS YYY CG  1 
ATOM 21177 N ND1 . HIS O 3 205 ? 98.704  -47.286 -6.646  1.000 63.230  ? 210 HIS YYY ND1 1 
ATOM 21178 C CD2 . HIS O 3 205 ? 98.681  -45.670 -5.182  1.000 63.550  ? 210 HIS YYY CD2 1 
ATOM 21179 C CE1 . HIS O 3 205 ? 99.348  -47.706 -5.582  1.000 60.020  ? 210 HIS YYY CE1 1 
ATOM 21180 N NE2 . HIS O 3 205 ? 99.373  -46.724 -4.680  1.000 58.670  ? 210 HIS YYY NE2 1 
ATOM 21181 N N   . LYS O 3 206 ? 100.496 -43.796 -9.123  1.000 73.970  ? 211 LYS YYY N   1 
ATOM 21182 C CA  . LYS O 3 206 ? 101.653 -44.023 -10.038 1.000 75.170  ? 211 LYS YYY CA  1 
ATOM 21183 C C   . LYS O 3 206 ? 102.285 -45.387 -9.774  1.000 79.070  ? 211 LYS YYY C   1 
ATOM 21184 O O   . LYS O 3 206 ? 102.593 -46.101 -10.722 1.000 90.950  ? 211 LYS YYY O   1 
ATOM 21185 C CB  . LYS O 3 206 ? 102.727 -42.934 -9.927  1.000 75.820  ? 211 LYS YYY CB  1 
ATOM 21186 C CG  . LYS O 3 206 ? 102.421 -41.632 -10.660 1.000 78.380  ? 211 LYS YYY CG  1 
ATOM 21187 C CD  . LYS O 3 206 ? 103.660 -40.892 -11.164 1.000 78.710  ? 211 LYS YYY CD  1 
ATOM 21188 C CE  . LYS O 3 206 ? 103.647 -39.401 -10.882 1.000 79.140  ? 211 LYS YYY CE  1 
ATOM 21189 N NZ  . LYS O 3 206 ? 102.368 -38.759 -11.272 1.000 78.380  ? 211 LYS YYY NZ  1 
ATOM 21190 N N   . PRO O 3 207 ? 102.512 -45.812 -8.507  1.000 74.880  ? 212 PRO YYY N   1 
ATOM 21191 C CA  . PRO O 3 207 ? 103.187 -47.089 -8.249  1.000 73.720  ? 212 PRO YYY CA  1 
ATOM 21192 C C   . PRO O 3 207 ? 102.513 -48.347 -8.838  1.000 77.820  ? 212 PRO YYY C   1 
ATOM 21193 O O   . PRO O 3 207 ? 103.165 -49.391 -8.888  1.000 77.580  ? 212 PRO YYY O   1 
ATOM 21194 C CB  . PRO O 3 207 ? 103.200 -47.172 -6.719  1.000 69.090  ? 212 PRO YYY CB  1 
ATOM 21195 C CG  . PRO O 3 207 ? 103.113 -45.740 -6.257  1.000 68.930  ? 212 PRO YYY CG  1 
ATOM 21196 C CD  . PRO O 3 207 ? 102.201 -45.079 -7.269  1.000 70.750  ? 212 PRO YYY CD  1 
ATOM 21197 N N   . SER O 3 208 ? 101.244 -48.238 -9.267  1.000 75.500  ? 213 SER YYY N   1 
ATOM 21198 C CA  . SER O 3 208 ? 100.425 -49.345 -9.830  1.000 74.220  ? 213 SER YYY CA  1 
ATOM 21199 C C   . SER O 3 208 ? 99.906  -49.009 -11.238 1.000 69.440  ? 213 SER YYY C   1 
ATOM 21200 O O   . SER O 3 208 ? 99.076  -49.777 -11.750 1.000 68.490  ? 213 SER YYY O   1 
ATOM 21201 C CB  . SER O 3 208 ? 99.296  -49.682 -8.892  1.000 75.780  ? 213 SER YYY CB  1 
ATOM 21202 O OG  . SER O 3 208 ? 98.364  -50.530 -9.523  1.000 83.320  ? 213 SER YYY OG  1 
ATOM 21203 N N   . ASN O 3 209 ? 100.399 -47.932 -11.862 1.000 67.430  ? 214 ASN YYY N   1 
ATOM 21204 C CA  . ASN O 3 209 ? 100.085 -47.556 -13.274 1.000 77.790  ? 214 ASN YYY CA  1 
ATOM 21205 C C   . ASN O 3 209 ? 98.570  -47.314 -13.431 1.000 73.360  ? 214 ASN YYY C   1 
ATOM 21206 O O   . ASN O 3 209 ? 98.054  -47.435 -14.567 1.000 63.190  ? 214 ASN YYY O   1 
ATOM 21207 C CB  . ASN O 3 209 ? 100.585 -48.606 -14.283 1.000 82.340  ? 214 ASN YYY CB  1 
ATOM 21208 C CG  . ASN O 3 209 ? 102.038 -49.031 -14.132 1.000 80.020  ? 214 ASN YYY CG  1 
ATOM 21209 O OD1 . ASN O 3 209 ? 102.330 -50.222 -14.043 1.000 76.820  ? 214 ASN YYY OD1 1 
ATOM 21210 N ND2 . ASN O 3 209 ? 102.959 -48.084 -14.079 1.000 76.090  ? 214 ASN YYY ND2 1 
ATOM 21211 N N   . THR O 3 210 ? 97.881  -46.976 -12.335 1.000 74.330  ? 215 THR YYY N   1 
ATOM 21212 C CA  . THR O 3 210 ? 96.405  -46.825 -12.256 1.000 75.430  ? 215 THR YYY CA  1 
ATOM 21213 C C   . THR O 3 210 ? 96.044  -45.363 -12.542 1.000 77.240  ? 215 THR YYY C   1 
ATOM 21214 O O   . THR O 3 210 ? 96.524  -44.492 -11.797 1.000 72.210  ? 215 THR YYY O   1 
ATOM 21215 C CB  . THR O 3 210 ? 95.878  -47.306 -10.894 1.000 75.700  ? 215 THR YYY CB  1 
ATOM 21216 O OG1 . THR O 3 210 ? 96.168  -48.695 -10.730 1.000 66.390  ? 215 THR YYY OG1 1 
ATOM 21217 C CG2 . THR O 3 210 ? 94.384  -47.139 -10.731 1.000 79.640  ? 215 THR YYY CG2 1 
ATOM 21218 N N   . LYS O 3 211 ? 95.208  -45.125 -13.559 1.000 85.110  ? 216 LYS YYY N   1 
ATOM 21219 C CA  . LYS O 3 211 ? 94.628  -43.791 -13.886 1.000 90.010  ? 216 LYS YYY CA  1 
ATOM 21220 C C   . LYS O 3 211 ? 93.143  -43.942 -14.262 1.000 78.860  ? 216 LYS YYY C   1 
ATOM 21221 O O   . LYS O 3 211 ? 92.741  -43.418 -15.324 1.000 74.190  ? 216 LYS YYY O   1 
ATOM 21222 C CB  . LYS O 3 211 ? 95.439  -43.096 -14.991 1.000 98.190  ? 216 LYS YYY CB  1 
ATOM 21223 C CG  . LYS O 3 211 ? 95.053  -41.645 -15.306 1.000 103.040 ? 216 LYS YYY CG  1 
ATOM 21224 C CD  . LYS O 3 211 ? 94.638  -40.841 -14.084 1.000 103.460 ? 216 LYS YYY CD  1 
ATOM 21225 C CE  . LYS O 3 211 ? 94.113  -39.459 -14.381 1.000 94.020  ? 216 LYS YYY CE  1 
ATOM 21226 N NZ  . LYS O 3 211 ? 93.975  -38.712 -13.110 1.000 91.490  ? 216 LYS YYY NZ  1 
ATOM 21227 N N   . VAL O 3 212 ? 92.350  -44.569 -13.389 1.000 77.450  ? 217 VAL YYY N   1 
ATOM 21228 C CA  . VAL O 3 212 ? 90.920  -44.930 -13.637 1.000 89.000  ? 217 VAL YYY CA  1 
ATOM 21229 C C   . VAL O 3 212 ? 89.992  -43.730 -13.361 1.000 86.840  ? 217 VAL YYY C   1 
ATOM 21230 O O   . VAL O 3 212 ? 90.119  -43.110 -12.290 1.000 74.970  ? 217 VAL YYY O   1 
ATOM 21231 C CB  . VAL O 3 212 ? 90.527  -46.186 -12.826 1.000 95.650  ? 217 VAL YYY CB  1 
ATOM 21232 C CG1 . VAL O 3 212 ? 89.015  -46.395 -12.743 1.000 95.600  ? 217 VAL YYY CG1 1 
ATOM 21233 C CG2 . VAL O 3 212 ? 91.202  -47.423 -13.403 1.000 97.570  ? 217 VAL YYY CG2 1 
ATOM 21234 N N   . ASP O 3 213 ? 89.062  -43.461 -14.296 1.000 87.830  ? 218 ASP YYY N   1 
ATOM 21235 C CA  . ASP O 3 213 ? 87.950  -42.473 -14.165 1.000 89.730  ? 218 ASP YYY CA  1 
ATOM 21236 C C   . ASP O 3 213 ? 86.625  -43.225 -13.931 1.000 88.010  ? 218 ASP YYY C   1 
ATOM 21237 O O   . ASP O 3 213 ? 86.241  -44.002 -14.814 1.000 99.180  ? 218 ASP YYY O   1 
ATOM 21238 C CB  . ASP O 3 213 ? 87.870  -41.548 -15.389 1.000 87.510  ? 218 ASP YYY CB  1 
ATOM 21239 C CG  . ASP O 3 213 ? 89.185  -40.930 -15.868 1.000 90.090  ? 218 ASP YYY CG  1 
ATOM 21240 O OD1 . ASP O 3 213 ? 90.067  -40.615 -15.026 1.000 94.530  ? 218 ASP YYY OD1 1 
ATOM 21241 O OD2 . ASP O 3 213 ? 89.325  -40.753 -17.094 1.000 79.030  ? 218 ASP YYY OD2 1 
ATOM 21242 N N   . LYS O 3 214 ? 85.969  -43.013 -12.778 1.000 87.550  ? 219 LYS YYY N   1 
ATOM 21243 C CA  . LYS O 3 214 ? 84.755  -43.750 -12.321 1.000 83.660  ? 219 LYS YYY CA  1 
ATOM 21244 C C   . LYS O 3 214 ? 83.560  -42.798 -12.297 1.000 84.390  ? 219 LYS YYY C   1 
ATOM 21245 O O   . LYS O 3 214 ? 83.771  -41.594 -12.061 1.000 86.420  ? 219 LYS YYY O   1 
ATOM 21246 C CB  . LYS O 3 214 ? 84.946  -44.330 -10.917 1.000 81.040  ? 219 LYS YYY CB  1 
ATOM 21247 C CG  . LYS O 3 214 ? 83.886  -45.322 -10.455 1.000 79.560  ? 219 LYS YYY CG  1 
ATOM 21248 C CD  . LYS O 3 214 ? 83.837  -46.577 -11.302 1.000 84.400  ? 219 LYS YYY CD  1 
ATOM 21249 C CE  . LYS O 3 214 ? 83.025  -47.688 -10.669 1.000 86.310  ? 219 LYS YYY CE  1 
ATOM 21250 N NZ  . LYS O 3 214 ? 82.742  -48.792 -11.619 1.000 86.010  ? 219 LYS YYY NZ  1 
ATOM 21251 N N   . LYS O 3 215 ? 82.357  -43.339 -12.504 1.000 84.430  ? 220 LYS YYY N   1 
ATOM 21252 C CA  . LYS O 3 215 ? 81.102  -42.554 -12.631 1.000 88.740  ? 220 LYS YYY CA  1 
ATOM 21253 C C   . LYS O 3 215 ? 80.267  -42.707 -11.352 1.000 85.210  ? 220 LYS YYY C   1 
ATOM 21254 O O   . LYS O 3 215 ? 80.071  -43.858 -10.897 1.000 73.810  ? 220 LYS YYY O   1 
ATOM 21255 C CB  . LYS O 3 215 ? 80.318  -42.994 -13.874 1.000 97.000  ? 220 LYS YYY CB  1 
ATOM 21256 C CG  . LYS O 3 215 ? 79.093  -42.144 -14.214 1.000 101.900 ? 220 LYS YYY CG  1 
ATOM 21257 C CD  . LYS O 3 215 ? 78.144  -42.760 -15.238 1.000 98.680  ? 220 LYS YYY CD  1 
ATOM 21258 C CE  . LYS O 3 215 ? 76.771  -42.119 -15.238 1.000 87.580  ? 220 LYS YYY CE  1 
ATOM 21259 N NZ  . LYS O 3 215 ? 76.089  -42.354 -16.528 1.000 86.040  ? 220 LYS YYY NZ  1 
ATOM 21260 N N   . VAL O 3 216 ? 79.790  -41.572 -10.822 1.000 89.570  ? 221 VAL YYY N   1 
ATOM 21261 C CA  . VAL O 3 216 ? 78.866  -41.460 -9.649  1.000 94.970  ? 221 VAL YYY CA  1 
ATOM 21262 C C   . VAL O 3 216 ? 77.729  -40.500 -10.030 1.000 89.780  ? 221 VAL YYY C   1 
ATOM 21263 O O   . VAL O 3 216 ? 76.547  -40.826 -9.891  1.000 90.300  ? 221 VAL YYY O   1 
ATOM 21264 C CB  . VAL O 3 216 ? 79.589  -40.995 -8.362  1.000 96.230  ? 221 VAL YYY CB  1 
ATOM 21265 C CG1 . VAL O 3 216 ? 80.321  -42.138 -7.682  1.000 95.160  ? 221 VAL YYY CG1 1 
ATOM 21266 C CG2 . VAL O 3 216 ? 80.542  -39.831 -8.602  1.000 100.390 ? 221 VAL YYY CG2 1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   18  ?   ?   ?   AAA . n 
A 1 2   SER 2   19  ?   ?   ?   AAA . n 
A 1 3   HIS 3   20  ?   ?   ?   AAA . n 
A 1 4   MET 4   21  ?   ?   ?   AAA . n 
A 1 5   GLY 5   22  ?   ?   ?   AAA . n 
A 1 6   GLY 6   23  ?   ?   ?   AAA . n 
A 1 7   VAL 7   24  24  VAL ALA AAA . n 
A 1 8   GLU 8   25  25  GLU ALA AAA . n 
A 1 9   VAL 9   26  26  VAL VAL AAA . n 
A 1 10  LEU 10  27  27  LEU LEU AAA . n 
A 1 11  GLU 11  28  28  GLU GLU AAA . n 
A 1 12  VAL 12  29  29  VAL VAL AAA . n 
A 1 13  LYS 13  30  30  LYS LYS AAA . n 
A 1 14  THR 14  31  31  THR THR AAA . n 
A 1 15  GLY 15  32  32  GLY GLY AAA . n 
A 1 16  VAL 16  33  33  VAL VAL AAA . n 
A 1 17  ASP 17  34  34  ASP ASP AAA . n 
A 1 18  SER 18  35  35  SER SER AAA . n 
A 1 19  ILE 19  36  36  ILE ILE AAA . n 
A 1 20  THR 20  37  37  THR THR AAA . n 
A 1 21  GLU 21  38  38  GLU GLU AAA . n 
A 1 22  VAL 22  39  39  VAL VAL AAA . n 
A 1 23  GLU 23  40  40  GLU GLU AAA . n 
A 1 24  CYS 24  41  41  CYS CYS AAA . n 
A 1 25  PHE 25  42  42  PHE PHE AAA . n 
A 1 26  LEU 26  43  43  LEU LEU AAA . n 
A 1 27  THR 27  44  44  THR THR AAA . n 
A 1 28  PRO 28  45  45  PRO PRO AAA . n 
A 1 29  GLU 29  46  46  GLU GLU AAA . n 
A 1 30  MET 30  47  47  MET MET AAA . n 
A 1 31  GLY 31  48  48  GLY GLY AAA . n 
A 1 32  ASP 32  49  49  ASP ASP AAA . n 
A 1 33  PRO 33  50  50  PRO PRO AAA . n 
A 1 34  ASP 34  51  51  ASP ASP AAA . n 
A 1 35  GLU 35  52  52  GLU GLU AAA . n 
A 1 36  HIS 36  53  53  HIS HIS AAA . n 
A 1 37  LEU 37  54  54  LEU LEU AAA . n 
A 1 38  ARG 38  55  55  ARG ARG AAA . n 
A 1 39  GLY 39  56  56  GLY GLY AAA . n 
A 1 40  PHE 40  57  57  PHE PHE AAA . n 
A 1 41  SER 41  58  58  SER SER AAA . n 
A 1 42  LYS 42  59  59  LYS LYS AAA . n 
A 1 43  SER 43  60  60  SER SER AAA . n 
A 1 44  ILE 44  61  61  ILE ILE AAA . n 
A 1 45  SER 45  62  62  SER SER AAA . n 
A 1 46  ILE 46  63  63  ILE ILE AAA . n 
A 1 47  SER 47  64  64  SER SER AAA . n 
A 1 48  ASP 48  65  65  ASP ASP AAA . n 
A 1 49  THR 49  66  66  THR THR AAA . n 
A 1 50  PHE 50  67  67  PHE PHE AAA . n 
A 1 51  GLU 51  68  68  GLU GLU AAA . n 
A 1 52  SER 52  69  69  SER SER AAA . n 
A 1 53  ASP 53  70  70  ASP ASP AAA . n 
A 1 54  SER 54  71  71  SER SER AAA . n 
A 1 55  PRO 55  72  72  PRO PRO AAA . n 
A 1 56  ASN 56  73  73  ASN ASN AAA . n 
A 1 57  ARG 57  74  74  ARG ARG AAA . n 
A 1 58  ASP 58  75  75  ASP ASP AAA . n 
A 1 59  MET 59  76  76  MET MET AAA . n 
A 1 60  LEU 60  77  77  LEU LEU AAA . n 
A 1 61  PRO 61  78  78  PRO PRO AAA . n 
A 1 62  CYS 62  79  79  CYS CYS AAA . n 
A 1 63  TYR 63  80  80  TYR TYR AAA . n 
A 1 64  SER 64  81  81  SER SER AAA . n 
A 1 65  VAL 65  82  82  VAL VAL AAA . n 
A 1 66  ALA 66  83  83  ALA ALA AAA . n 
A 1 67  ARG 67  84  84  ARG ARG AAA . n 
A 1 68  ILE 68  85  85  ILE ILE AAA . n 
A 1 69  PRO 69  86  86  PRO PRO AAA . n 
A 1 70  LEU 70  87  87  LEU LEU AAA . n 
A 1 71  PRO 71  88  88  PRO PRO AAA . n 
A 1 72  ASN 72  89  89  ASN ASN AAA . n 
A 1 73  LEU 73  90  90  LEU LEU AAA . n 
A 1 74  ASN 74  91  91  ASN ALA AAA . n 
A 1 75  GLU 75  92  ?   ?   ?   AAA . n 
A 1 76  ASP 76  93  ?   ?   ?   AAA . n 
A 1 77  LEU 77  94  ?   ?   ?   AAA . n 
A 1 78  THR 78  95  ?   ?   ?   AAA . n 
A 1 79  CYS 79  96  ?   ?   ?   AAA . n 
A 1 80  GLY 80  97  ?   ?   ?   AAA . n 
A 1 81  ASN 81  98  98  ASN ALA AAA . n 
A 1 82  ILE 82  99  99  ILE ILE AAA . n 
A 1 83  LEU 83  100 100 LEU LEU AAA . n 
A 1 84  MET 84  101 101 MET MET AAA . n 
A 1 85  TRP 85  102 102 TRP TRP AAA . n 
A 1 86  GLU 86  103 103 GLU GLU AAA . n 
A 1 87  ALA 87  104 104 ALA ALA AAA . n 
A 1 88  VAL 88  105 105 VAL VAL AAA . n 
A 1 89  THR 89  106 106 THR THR AAA . n 
A 1 90  LEU 90  107 107 LEU LEU AAA . n 
A 1 91  LYS 91  108 108 LYS LYS AAA . n 
A 1 92  THR 92  109 109 THR THR AAA . n 
A 1 93  GLU 93  110 110 GLU GLU AAA . n 
A 1 94  VAL 94  111 111 VAL VAL AAA . n 
A 1 95  ILE 95  112 112 ILE ILE AAA . n 
A 1 96  GLY 96  113 113 GLY GLY AAA . n 
A 1 97  VAL 97  114 114 VAL VAL AAA . n 
A 1 98  THR 98  115 115 THR THR AAA . n 
A 1 99  SER 99  116 116 SER SER AAA . n 
A 1 100 LEU 100 117 117 LEU LEU AAA . n 
A 1 101 MET 101 118 118 MET MET AAA . n 
A 1 102 ASN 102 119 119 ASN ASN AAA . n 
A 1 103 VAL 103 120 120 VAL VAL AAA . n 
A 1 104 HIS 104 121 121 HIS HIS AAA . n 
A 1 105 SER 105 122 122 SER SER AAA . n 
A 1 106 ASN 106 123 123 ASN ASN AAA . n 
A 1 107 GLY 107 124 124 GLY GLY AAA . n 
A 1 108 GLN 108 125 125 GLN GLN AAA . n 
A 1 109 ALA 109 126 126 ALA ALA AAA . n 
A 1 110 THR 110 127 127 THR THR AAA . n 
A 1 111 HIS 111 128 128 HIS HIS AAA . n 
A 1 112 ASP 112 129 129 ASP ASP AAA . n 
A 1 113 ASN 113 130 130 ASN ASN AAA . n 
A 1 114 GLY 114 131 131 GLY GLY AAA . n 
A 1 115 ALA 115 132 132 ALA ALA AAA . n 
A 1 116 GLY 116 133 133 GLY GLY AAA . n 
A 1 117 LYS 117 134 134 LYS LYS AAA . n 
A 1 118 PRO 118 135 135 PRO PRO AAA . n 
A 1 119 VAL 119 136 136 VAL VAL AAA . n 
A 1 120 GLN 120 137 137 GLN GLN AAA . n 
A 1 121 GLY 121 138 138 GLY GLY AAA . n 
A 1 122 THR 122 139 139 THR THR AAA . n 
A 1 123 SER 123 140 140 SER SER AAA . n 
A 1 124 PHE 124 141 141 PHE PHE AAA . n 
A 1 125 HIS 125 142 142 HIS HIS AAA . n 
A 1 126 PHE 126 143 143 PHE PHE AAA . n 
A 1 127 PHE 127 144 144 PHE PHE AAA . n 
A 1 128 SER 128 145 145 SER SER AAA . n 
A 1 129 VAL 129 146 146 VAL VAL AAA . n 
A 1 130 GLY 130 147 147 GLY GLY AAA . n 
A 1 131 GLY 131 148 148 GLY GLY AAA . n 
A 1 132 GLU 132 149 149 GLU GLU AAA . n 
A 1 133 ALA 133 150 150 ALA ALA AAA . n 
A 1 134 LEU 134 151 151 LEU LEU AAA . n 
A 1 135 GLU 135 152 152 GLU GLU AAA . n 
A 1 136 LEU 136 153 153 LEU LEU AAA . n 
A 1 137 GLN 137 154 154 GLN GLN AAA . n 
A 1 138 GLY 138 155 155 GLY GLY AAA . n 
A 1 139 VAL 139 156 156 VAL VAL AAA . n 
A 1 140 LEU 140 157 157 LEU LEU AAA . n 
A 1 141 PHE 141 158 158 PHE PHE AAA . n 
A 1 142 ASN 142 159 159 ASN ASN AAA . n 
A 1 143 TYR 143 160 160 TYR TYR AAA . n 
A 1 144 ARG 144 161 161 ARG ARG AAA . n 
A 1 145 THR 145 162 162 THR THR AAA . n 
A 1 146 LYS 146 163 163 LYS LYS AAA . n 
A 1 147 TYR 147 164 164 TYR TYR AAA . n 
A 1 148 PRO 148 165 165 PRO PRO AAA . n 
A 1 149 ASP 149 166 166 ASP ASP AAA . n 
A 1 150 GLY 150 167 167 GLY GLY AAA . n 
A 1 151 THR 151 168 168 THR THR AAA . n 
A 1 152 ILE 152 169 169 ILE ILE AAA . n 
A 1 153 PHE 153 170 170 PHE PHE AAA . n 
A 1 154 PRO 154 171 171 PRO PRO AAA . n 
A 1 155 LYS 155 172 172 LYS LYS AAA . n 
A 1 156 ASN 156 173 173 ASN ASN AAA . n 
A 1 157 ALA 157 174 174 ALA ALA AAA . n 
A 1 158 THR 158 175 175 THR THR AAA . n 
A 1 159 VAL 159 176 176 VAL VAL AAA . n 
A 1 160 GLN 160 177 177 GLN GLN AAA . n 
A 1 161 SER 161 178 178 SER SER AAA . n 
A 1 162 GLN 162 179 179 GLN GLN AAA . n 
A 1 163 VAL 163 180 180 VAL VAL AAA . n 
A 1 164 MET 164 181 181 MET MET AAA . n 
A 1 165 ASN 165 182 182 ASN ASN AAA . n 
A 1 166 THR 166 183 183 THR THR AAA . n 
A 1 167 GLU 167 184 184 GLU GLU AAA . n 
A 1 168 HIS 168 185 185 HIS HIS AAA . n 
A 1 169 LYS 169 186 186 LYS LYS AAA . n 
A 1 170 ALA 170 187 187 ALA ALA AAA . n 
A 1 171 TYR 171 188 188 TYR TYR AAA . n 
A 1 172 LEU 172 189 189 LEU LEU AAA . n 
A 1 173 ASP 173 190 190 ASP ASP AAA . n 
A 1 174 LYS 174 191 191 LYS LYS AAA . n 
A 1 175 ASN 175 192 192 ASN ASN AAA . n 
A 1 176 LYS 176 193 193 LYS LYS AAA . n 
A 1 177 ALA 177 194 194 ALA ALA AAA . n 
A 1 178 TYR 178 195 195 TYR TYR AAA . n 
A 1 179 PRO 179 196 196 PRO PRO AAA . n 
A 1 180 VAL 180 197 197 VAL VAL AAA . n 
A 1 181 GLU 181 198 198 GLU GLU AAA . n 
A 1 182 CYS 182 199 199 CYS CYS AAA . n 
A 1 183 TRP 183 200 200 TRP TRP AAA . n 
A 1 184 VAL 184 201 201 VAL VAL AAA . n 
A 1 185 PRO 185 202 202 PRO PRO AAA . n 
A 1 186 ASP 186 203 203 ASP ASP AAA . n 
A 1 187 PRO 187 204 204 PRO PRO AAA . n 
A 1 188 THR 188 205 205 THR THR AAA . n 
A 1 189 ARG 189 206 206 ARG ARG AAA . n 
A 1 190 ASN 190 207 207 ASN ASN AAA . n 
A 1 191 GLU 191 208 208 GLU GLU AAA . n 
A 1 192 ASN 192 209 209 ASN ASN AAA . n 
A 1 193 THR 193 210 210 THR THR AAA . n 
A 1 194 ARG 194 211 211 ARG ARG AAA . n 
A 1 195 TYR 195 212 212 TYR TYR AAA . n 
A 1 196 PHE 196 213 213 PHE PHE AAA . n 
A 1 197 GLY 197 214 214 GLY GLY AAA . n 
A 1 198 THR 198 215 215 THR THR AAA . n 
A 1 199 LEU 199 216 216 LEU LEU AAA . n 
A 1 200 THR 200 217 217 THR THR AAA . n 
A 1 201 GLY 201 218 218 GLY GLY AAA . n 
A 1 202 GLY 202 219 219 GLY GLY AAA . n 
A 1 203 GLU 203 220 220 GLU GLU AAA . n 
A 1 204 ASN 204 221 221 ASN ASN AAA . n 
A 1 205 VAL 205 222 222 VAL VAL AAA . n 
A 1 206 PRO 206 223 223 PRO PRO AAA . n 
A 1 207 PRO 207 224 224 PRO PRO AAA . n 
A 1 208 VAL 208 225 225 VAL VAL AAA . n 
A 1 209 LEU 209 226 226 LEU LEU AAA . n 
A 1 210 HIS 210 227 227 HIS HIS AAA . n 
A 1 211 ILE 211 228 228 ILE ILE AAA . n 
A 1 212 THR 212 229 229 THR THR AAA . n 
A 1 213 ASN 213 230 230 ASN ASN AAA . n 
A 1 214 THR 214 231 231 THR THR AAA . n 
A 1 215 ALA 215 232 232 ALA ALA AAA . n 
A 1 216 THR 216 233 233 THR THR AAA . n 
A 1 217 THR 217 234 234 THR THR AAA . n 
A 1 218 VAL 218 235 235 VAL VAL AAA . n 
A 1 219 LEU 219 236 236 LEU LEU AAA . n 
A 1 220 LEU 220 237 237 LEU LEU AAA . n 
A 1 221 ASP 221 238 238 ASP ASP AAA . n 
A 1 222 GLU 222 239 239 GLU GLU AAA . n 
A 1 223 PHE 223 240 240 PHE PHE AAA . n 
A 1 224 GLY 224 241 241 GLY GLY AAA . n 
A 1 225 VAL 225 242 242 VAL VAL AAA . n 
A 1 226 GLY 226 243 243 GLY GLY AAA . n 
A 1 227 PRO 227 244 244 PRO PRO AAA . n 
A 1 228 LEU 228 245 245 LEU LEU AAA . n 
A 1 229 CYS 229 246 246 CYS CYS AAA . n 
A 1 230 LYS 230 247 247 LYS LYS AAA . n 
A 1 231 GLY 231 248 248 GLY GLY AAA . n 
A 1 232 ASP 232 249 249 ASP ASP AAA . n 
A 1 233 ASN 233 250 250 ASN ASN AAA . n 
A 1 234 LEU 234 251 251 LEU LEU AAA . n 
A 1 235 TYR 235 252 252 TYR TYR AAA . n 
A 1 236 LEU 236 253 253 LEU LEU AAA . n 
A 1 237 SER 237 254 254 SER SER AAA . n 
A 1 238 ALA 238 255 255 ALA ALA AAA . n 
A 1 239 VAL 239 256 256 VAL VAL AAA . n 
A 1 240 ASP 240 257 257 ASP ASP AAA . n 
A 1 241 VAL 241 258 258 VAL VAL AAA . n 
A 1 242 CYS 242 259 259 CYS CYS AAA . n 
A 1 243 GLY 243 260 260 GLY GLY AAA . n 
A 1 244 MET 244 261 261 MET MET AAA . n 
A 1 245 PHE 245 262 262 PHE PHE AAA . n 
A 1 246 THR 246 263 263 THR THR AAA . n 
A 1 247 ASN 247 264 264 ASN ASN AAA . n 
A 1 248 ARG 248 265 265 ARG ARG AAA . n 
A 1 249 SER 249 266 266 SER SER AAA . n 
A 1 250 GLY 250 267 267 GLY GLY AAA . n 
A 1 251 SER 251 268 268 SER SER AAA . n 
A 1 252 GLN 252 269 269 GLN GLN AAA . n 
A 1 253 GLN 253 270 270 GLN GLN AAA . n 
A 1 254 TRP 254 271 271 TRP TRP AAA . n 
A 1 255 ARG 255 272 272 ARG ARG AAA . n 
A 1 256 GLY 256 273 273 GLY GLY AAA . n 
A 1 257 LEU 257 274 274 LEU LEU AAA . n 
A 1 258 SER 258 275 275 SER SER AAA . n 
A 1 259 ARG 259 276 276 ARG ARG AAA . n 
A 1 260 TYR 260 277 277 TYR TYR AAA . n 
A 1 261 PHE 261 278 278 PHE PHE AAA . n 
A 1 262 LYS 262 279 279 LYS LYS AAA . n 
A 1 263 VAL 263 280 280 VAL VAL AAA . n 
A 1 264 GLN 264 281 281 GLN GLN AAA . n 
A 1 265 LEU 265 282 282 LEU LEU AAA . n 
A 1 266 ARG 266 283 283 ARG ARG AAA . n 
A 1 267 LYS 267 284 284 LYS LYS AAA . n 
A 1 268 ARG 268 285 285 ARG ARG AAA . n 
A 1 269 ARG 269 286 286 ARG ARG AAA . n 
A 1 270 VAL 270 287 287 VAL VAL AAA . n 
A 1 271 LYS 271 288 288 LYS LYS AAA . n 
A 1 272 ASN 272 289 289 ASN ALA AAA . n 
B 1 1   GLY 1   18  ?   ?   ?   BBB . n 
B 1 2   SER 2   19  ?   ?   ?   BBB . n 
B 1 3   HIS 3   20  ?   ?   ?   BBB . n 
B 1 4   MET 4   21  ?   ?   ?   BBB . n 
B 1 5   GLY 5   22  ?   ?   ?   BBB . n 
B 1 6   GLY 6   23  ?   ?   ?   BBB . n 
B 1 7   VAL 7   24  24  VAL ALA BBB . n 
B 1 8   GLU 8   25  25  GLU GLU BBB . n 
B 1 9   VAL 9   26  26  VAL VAL BBB . n 
B 1 10  LEU 10  27  27  LEU LEU BBB . n 
B 1 11  GLU 11  28  28  GLU GLU BBB . n 
B 1 12  VAL 12  29  29  VAL VAL BBB . n 
B 1 13  LYS 13  30  30  LYS LYS BBB . n 
B 1 14  THR 14  31  31  THR THR BBB . n 
B 1 15  GLY 15  32  32  GLY GLY BBB . n 
B 1 16  VAL 16  33  33  VAL VAL BBB . n 
B 1 17  ASP 17  34  34  ASP ASP BBB . n 
B 1 18  SER 18  35  35  SER SER BBB . n 
B 1 19  ILE 19  36  36  ILE ILE BBB . n 
B 1 20  THR 20  37  37  THR THR BBB . n 
B 1 21  GLU 21  38  38  GLU GLU BBB . n 
B 1 22  VAL 22  39  39  VAL VAL BBB . n 
B 1 23  GLU 23  40  40  GLU GLU BBB . n 
B 1 24  CYS 24  41  41  CYS CYS BBB . n 
B 1 25  PHE 25  42  42  PHE PHE BBB . n 
B 1 26  LEU 26  43  43  LEU LEU BBB . n 
B 1 27  THR 27  44  44  THR THR BBB . n 
B 1 28  PRO 28  45  45  PRO PRO BBB . n 
B 1 29  GLU 29  46  46  GLU GLU BBB . n 
B 1 30  MET 30  47  47  MET MET BBB . n 
B 1 31  GLY 31  48  48  GLY GLY BBB . n 
B 1 32  ASP 32  49  49  ASP ASP BBB . n 
B 1 33  PRO 33  50  50  PRO PRO BBB . n 
B 1 34  ASP 34  51  51  ASP ASP BBB . n 
B 1 35  GLU 35  52  52  GLU GLU BBB . n 
B 1 36  HIS 36  53  53  HIS HIS BBB . n 
B 1 37  LEU 37  54  54  LEU LEU BBB . n 
B 1 38  ARG 38  55  55  ARG ARG BBB . n 
B 1 39  GLY 39  56  56  GLY GLY BBB . n 
B 1 40  PHE 40  57  57  PHE PHE BBB . n 
B 1 41  SER 41  58  58  SER SER BBB . n 
B 1 42  LYS 42  59  59  LYS LYS BBB . n 
B 1 43  SER 43  60  60  SER SER BBB . n 
B 1 44  ILE 44  61  61  ILE ILE BBB . n 
B 1 45  SER 45  62  62  SER SER BBB . n 
B 1 46  ILE 46  63  63  ILE ILE BBB . n 
B 1 47  SER 47  64  64  SER SER BBB . n 
B 1 48  ASP 48  65  65  ASP ASP BBB . n 
B 1 49  THR 49  66  66  THR THR BBB . n 
B 1 50  PHE 50  67  67  PHE PHE BBB . n 
B 1 51  GLU 51  68  68  GLU GLU BBB . n 
B 1 52  SER 52  69  69  SER SER BBB . n 
B 1 53  ASP 53  70  70  ASP ASP BBB . n 
B 1 54  SER 54  71  71  SER SER BBB . n 
B 1 55  PRO 55  72  72  PRO PRO BBB . n 
B 1 56  ASN 56  73  73  ASN ASN BBB . n 
B 1 57  ARG 57  74  74  ARG ARG BBB . n 
B 1 58  ASP 58  75  75  ASP ASP BBB . n 
B 1 59  MET 59  76  76  MET MET BBB . n 
B 1 60  LEU 60  77  77  LEU LEU BBB . n 
B 1 61  PRO 61  78  78  PRO PRO BBB . n 
B 1 62  CYS 62  79  79  CYS CYS BBB . n 
B 1 63  TYR 63  80  80  TYR TYR BBB . n 
B 1 64  SER 64  81  81  SER SER BBB . n 
B 1 65  VAL 65  82  82  VAL VAL BBB . n 
B 1 66  ALA 66  83  83  ALA ALA BBB . n 
B 1 67  ARG 67  84  84  ARG ARG BBB . n 
B 1 68  ILE 68  85  85  ILE ILE BBB . n 
B 1 69  PRO 69  86  86  PRO PRO BBB . n 
B 1 70  LEU 70  87  87  LEU LEU BBB . n 
B 1 71  PRO 71  88  88  PRO PRO BBB . n 
B 1 72  ASN 72  89  89  ASN ASN BBB . n 
B 1 73  LEU 73  90  90  LEU LEU BBB . n 
B 1 74  ASN 74  91  91  ASN ALA BBB . n 
B 1 75  GLU 75  92  ?   ?   ?   BBB . n 
B 1 76  ASP 76  93  ?   ?   ?   BBB . n 
B 1 77  LEU 77  94  ?   ?   ?   BBB . n 
B 1 78  THR 78  95  ?   ?   ?   BBB . n 
B 1 79  CYS 79  96  ?   ?   ?   BBB . n 
B 1 80  GLY 80  97  ?   ?   ?   BBB . n 
B 1 81  ASN 81  98  ?   ?   ?   BBB . n 
B 1 82  ILE 82  99  99  ILE ILE BBB . n 
B 1 83  LEU 83  100 100 LEU LEU BBB . n 
B 1 84  MET 84  101 101 MET MET BBB . n 
B 1 85  TRP 85  102 102 TRP TRP BBB . n 
B 1 86  GLU 86  103 103 GLU GLU BBB . n 
B 1 87  ALA 87  104 104 ALA ALA BBB . n 
B 1 88  VAL 88  105 105 VAL VAL BBB . n 
B 1 89  THR 89  106 106 THR THR BBB . n 
B 1 90  LEU 90  107 107 LEU LEU BBB . n 
B 1 91  LYS 91  108 108 LYS LYS BBB . n 
B 1 92  THR 92  109 109 THR THR BBB . n 
B 1 93  GLU 93  110 110 GLU GLU BBB . n 
B 1 94  VAL 94  111 111 VAL VAL BBB . n 
B 1 95  ILE 95  112 112 ILE ILE BBB . n 
B 1 96  GLY 96  113 113 GLY GLY BBB . n 
B 1 97  VAL 97  114 114 VAL VAL BBB . n 
B 1 98  THR 98  115 115 THR THR BBB . n 
B 1 99  SER 99  116 116 SER SER BBB . n 
B 1 100 LEU 100 117 117 LEU LEU BBB . n 
B 1 101 MET 101 118 118 MET MET BBB . n 
B 1 102 ASN 102 119 119 ASN ASN BBB . n 
B 1 103 VAL 103 120 120 VAL VAL BBB . n 
B 1 104 HIS 104 121 121 HIS HIS BBB . n 
B 1 105 SER 105 122 122 SER SER BBB . n 
B 1 106 ASN 106 123 123 ASN ASN BBB . n 
B 1 107 GLY 107 124 124 GLY GLY BBB . n 
B 1 108 GLN 108 125 125 GLN GLN BBB . n 
B 1 109 ALA 109 126 126 ALA ALA BBB . n 
B 1 110 THR 110 127 127 THR THR BBB . n 
B 1 111 HIS 111 128 128 HIS HIS BBB . n 
B 1 112 ASP 112 129 129 ASP ASP BBB . n 
B 1 113 ASN 113 130 130 ASN ASN BBB . n 
B 1 114 GLY 114 131 131 GLY GLY BBB . n 
B 1 115 ALA 115 132 132 ALA ALA BBB . n 
B 1 116 GLY 116 133 133 GLY GLY BBB . n 
B 1 117 LYS 117 134 134 LYS LYS BBB . n 
B 1 118 PRO 118 135 135 PRO PRO BBB . n 
B 1 119 VAL 119 136 136 VAL VAL BBB . n 
B 1 120 GLN 120 137 137 GLN GLN BBB . n 
B 1 121 GLY 121 138 138 GLY GLY BBB . n 
B 1 122 THR 122 139 139 THR THR BBB . n 
B 1 123 SER 123 140 140 SER SER BBB . n 
B 1 124 PHE 124 141 141 PHE PHE BBB . n 
B 1 125 HIS 125 142 142 HIS HIS BBB . n 
B 1 126 PHE 126 143 143 PHE PHE BBB . n 
B 1 127 PHE 127 144 144 PHE PHE BBB . n 
B 1 128 SER 128 145 145 SER SER BBB . n 
B 1 129 VAL 129 146 146 VAL VAL BBB . n 
B 1 130 GLY 130 147 147 GLY GLY BBB . n 
B 1 131 GLY 131 148 148 GLY GLY BBB . n 
B 1 132 GLU 132 149 149 GLU GLU BBB . n 
B 1 133 ALA 133 150 150 ALA ALA BBB . n 
B 1 134 LEU 134 151 151 LEU LEU BBB . n 
B 1 135 GLU 135 152 152 GLU GLU BBB . n 
B 1 136 LEU 136 153 153 LEU LEU BBB . n 
B 1 137 GLN 137 154 154 GLN GLN BBB . n 
B 1 138 GLY 138 155 155 GLY GLY BBB . n 
B 1 139 VAL 139 156 156 VAL VAL BBB . n 
B 1 140 LEU 140 157 157 LEU LEU BBB . n 
B 1 141 PHE 141 158 158 PHE PHE BBB . n 
B 1 142 ASN 142 159 159 ASN ASN BBB . n 
B 1 143 TYR 143 160 160 TYR TYR BBB . n 
B 1 144 ARG 144 161 161 ARG ARG BBB . n 
B 1 145 THR 145 162 162 THR THR BBB . n 
B 1 146 LYS 146 163 163 LYS LYS BBB . n 
B 1 147 TYR 147 164 164 TYR TYR BBB . n 
B 1 148 PRO 148 165 165 PRO PRO BBB . n 
B 1 149 ASP 149 166 166 ASP ASP BBB . n 
B 1 150 GLY 150 167 167 GLY GLY BBB . n 
B 1 151 THR 151 168 168 THR THR BBB . n 
B 1 152 ILE 152 169 169 ILE ILE BBB . n 
B 1 153 PHE 153 170 170 PHE PHE BBB . n 
B 1 154 PRO 154 171 171 PRO PRO BBB . n 
B 1 155 LYS 155 172 172 LYS LYS BBB . n 
B 1 156 ASN 156 173 173 ASN ASN BBB . n 
B 1 157 ALA 157 174 174 ALA ALA BBB . n 
B 1 158 THR 158 175 175 THR THR BBB . n 
B 1 159 VAL 159 176 176 VAL VAL BBB . n 
B 1 160 GLN 160 177 177 GLN GLN BBB . n 
B 1 161 SER 161 178 178 SER SER BBB . n 
B 1 162 GLN 162 179 179 GLN GLN BBB . n 
B 1 163 VAL 163 180 180 VAL VAL BBB . n 
B 1 164 MET 164 181 181 MET MET BBB . n 
B 1 165 ASN 165 182 182 ASN ASN BBB . n 
B 1 166 THR 166 183 183 THR THR BBB . n 
B 1 167 GLU 167 184 184 GLU GLU BBB . n 
B 1 168 HIS 168 185 185 HIS HIS BBB . n 
B 1 169 LYS 169 186 186 LYS LYS BBB . n 
B 1 170 ALA 170 187 187 ALA ALA BBB . n 
B 1 171 TYR 171 188 188 TYR TYR BBB . n 
B 1 172 LEU 172 189 189 LEU LEU BBB . n 
B 1 173 ASP 173 190 190 ASP ASP BBB . n 
B 1 174 LYS 174 191 191 LYS LYS BBB . n 
B 1 175 ASN 175 192 192 ASN ASN BBB . n 
B 1 176 LYS 176 193 193 LYS LYS BBB . n 
B 1 177 ALA 177 194 194 ALA ALA BBB . n 
B 1 178 TYR 178 195 195 TYR TYR BBB . n 
B 1 179 PRO 179 196 196 PRO PRO BBB . n 
B 1 180 VAL 180 197 197 VAL VAL BBB . n 
B 1 181 GLU 181 198 198 GLU GLU BBB . n 
B 1 182 CYS 182 199 199 CYS CYS BBB . n 
B 1 183 TRP 183 200 200 TRP TRP BBB . n 
B 1 184 VAL 184 201 201 VAL VAL BBB . n 
B 1 185 PRO 185 202 202 PRO PRO BBB . n 
B 1 186 ASP 186 203 203 ASP ASP BBB . n 
B 1 187 PRO 187 204 204 PRO PRO BBB . n 
B 1 188 THR 188 205 205 THR THR BBB . n 
B 1 189 ARG 189 206 206 ARG ARG BBB . n 
B 1 190 ASN 190 207 207 ASN ASN BBB . n 
B 1 191 GLU 191 208 208 GLU GLU BBB . n 
B 1 192 ASN 192 209 209 ASN ASN BBB . n 
B 1 193 THR 193 210 210 THR THR BBB . n 
B 1 194 ARG 194 211 211 ARG ARG BBB . n 
B 1 195 TYR 195 212 212 TYR TYR BBB . n 
B 1 196 PHE 196 213 213 PHE PHE BBB . n 
B 1 197 GLY 197 214 214 GLY GLY BBB . n 
B 1 198 THR 198 215 215 THR THR BBB . n 
B 1 199 LEU 199 216 216 LEU LEU BBB . n 
B 1 200 THR 200 217 217 THR THR BBB . n 
B 1 201 GLY 201 218 218 GLY GLY BBB . n 
B 1 202 GLY 202 219 219 GLY GLY BBB . n 
B 1 203 GLU 203 220 220 GLU GLU BBB . n 
B 1 204 ASN 204 221 221 ASN ASN BBB . n 
B 1 205 VAL 205 222 222 VAL VAL BBB . n 
B 1 206 PRO 206 223 223 PRO PRO BBB . n 
B 1 207 PRO 207 224 224 PRO PRO BBB . n 
B 1 208 VAL 208 225 225 VAL VAL BBB . n 
B 1 209 LEU 209 226 226 LEU LEU BBB . n 
B 1 210 HIS 210 227 227 HIS HIS BBB . n 
B 1 211 ILE 211 228 228 ILE ILE BBB . n 
B 1 212 THR 212 229 229 THR THR BBB . n 
B 1 213 ASN 213 230 230 ASN ASN BBB . n 
B 1 214 THR 214 231 231 THR THR BBB . n 
B 1 215 ALA 215 232 232 ALA ALA BBB . n 
B 1 216 THR 216 233 233 THR THR BBB . n 
B 1 217 THR 217 234 234 THR THR BBB . n 
B 1 218 VAL 218 235 235 VAL VAL BBB . n 
B 1 219 LEU 219 236 236 LEU LEU BBB . n 
B 1 220 LEU 220 237 237 LEU LEU BBB . n 
B 1 221 ASP 221 238 238 ASP ASP BBB . n 
B 1 222 GLU 222 239 239 GLU GLU BBB . n 
B 1 223 PHE 223 240 240 PHE PHE BBB . n 
B 1 224 GLY 224 241 241 GLY GLY BBB . n 
B 1 225 VAL 225 242 242 VAL VAL BBB . n 
B 1 226 GLY 226 243 243 GLY GLY BBB . n 
B 1 227 PRO 227 244 244 PRO PRO BBB . n 
B 1 228 LEU 228 245 245 LEU LEU BBB . n 
B 1 229 CYS 229 246 246 CYS CYS BBB . n 
B 1 230 LYS 230 247 247 LYS LYS BBB . n 
B 1 231 GLY 231 248 248 GLY GLY BBB . n 
B 1 232 ASP 232 249 249 ASP ASP BBB . n 
B 1 233 ASN 233 250 250 ASN ASN BBB . n 
B 1 234 LEU 234 251 251 LEU LEU BBB . n 
B 1 235 TYR 235 252 252 TYR TYR BBB . n 
B 1 236 LEU 236 253 253 LEU LEU BBB . n 
B 1 237 SER 237 254 254 SER SER BBB . n 
B 1 238 ALA 238 255 255 ALA ALA BBB . n 
B 1 239 VAL 239 256 256 VAL VAL BBB . n 
B 1 240 ASP 240 257 257 ASP ASP BBB . n 
B 1 241 VAL 241 258 258 VAL VAL BBB . n 
B 1 242 CYS 242 259 259 CYS CYS BBB . n 
B 1 243 GLY 243 260 260 GLY GLY BBB . n 
B 1 244 MET 244 261 261 MET MET BBB . n 
B 1 245 PHE 245 262 262 PHE PHE BBB . n 
B 1 246 THR 246 263 263 THR THR BBB . n 
B 1 247 ASN 247 264 264 ASN ASN BBB . n 
B 1 248 ARG 248 265 265 ARG ARG BBB . n 
B 1 249 SER 249 266 266 SER SER BBB . n 
B 1 250 GLY 250 267 267 GLY GLY BBB . n 
B 1 251 SER 251 268 268 SER SER BBB . n 
B 1 252 GLN 252 269 269 GLN GLN BBB . n 
B 1 253 GLN 253 270 270 GLN GLN BBB . n 
B 1 254 TRP 254 271 271 TRP TRP BBB . n 
B 1 255 ARG 255 272 272 ARG ARG BBB . n 
B 1 256 GLY 256 273 273 GLY GLY BBB . n 
B 1 257 LEU 257 274 274 LEU LEU BBB . n 
B 1 258 SER 258 275 275 SER SER BBB . n 
B 1 259 ARG 259 276 276 ARG ARG BBB . n 
B 1 260 TYR 260 277 277 TYR TYR BBB . n 
B 1 261 PHE 261 278 278 PHE PHE BBB . n 
B 1 262 LYS 262 279 279 LYS LYS BBB . n 
B 1 263 VAL 263 280 280 VAL VAL BBB . n 
B 1 264 GLN 264 281 281 GLN GLN BBB . n 
B 1 265 LEU 265 282 282 LEU LEU BBB . n 
B 1 266 ARG 266 283 283 ARG ARG BBB . n 
B 1 267 LYS 267 284 284 LYS LYS BBB . n 
B 1 268 ARG 268 285 285 ARG ARG BBB . n 
B 1 269 ARG 269 286 286 ARG ARG BBB . n 
B 1 270 VAL 270 287 287 VAL VAL BBB . n 
B 1 271 LYS 271 288 288 LYS LYS BBB . n 
B 1 272 ASN 272 289 ?   ?   ?   BBB . n 
C 1 1   GLY 1   18  ?   ?   ?   CCC . n 
C 1 2   SER 2   19  ?   ?   ?   CCC . n 
C 1 3   HIS 3   20  ?   ?   ?   CCC . n 
C 1 4   MET 4   21  ?   ?   ?   CCC . n 
C 1 5   GLY 5   22  ?   ?   ?   CCC . n 
C 1 6   GLY 6   23  ?   ?   ?   CCC . n 
C 1 7   VAL 7   24  ?   ?   ?   CCC . n 
C 1 8   GLU 8   25  25  GLU ALA CCC . n 
C 1 9   VAL 9   26  26  VAL VAL CCC . n 
C 1 10  LEU 10  27  27  LEU LEU CCC . n 
C 1 11  GLU 11  28  28  GLU GLU CCC . n 
C 1 12  VAL 12  29  29  VAL VAL CCC . n 
C 1 13  LYS 13  30  30  LYS LYS CCC . n 
C 1 14  THR 14  31  31  THR THR CCC . n 
C 1 15  GLY 15  32  32  GLY GLY CCC . n 
C 1 16  VAL 16  33  33  VAL ALA CCC . n 
C 1 17  ASP 17  34  34  ASP ASP CCC . n 
C 1 18  SER 18  35  35  SER SER CCC . n 
C 1 19  ILE 19  36  36  ILE ILE CCC . n 
C 1 20  THR 20  37  37  THR THR CCC . n 
C 1 21  GLU 21  38  38  GLU GLU CCC . n 
C 1 22  VAL 22  39  39  VAL VAL CCC . n 
C 1 23  GLU 23  40  40  GLU GLU CCC . n 
C 1 24  CYS 24  41  41  CYS CYS CCC . n 
C 1 25  PHE 25  42  42  PHE PHE CCC . n 
C 1 26  LEU 26  43  43  LEU LEU CCC . n 
C 1 27  THR 27  44  44  THR THR CCC . n 
C 1 28  PRO 28  45  45  PRO PRO CCC . n 
C 1 29  GLU 29  46  46  GLU GLU CCC . n 
C 1 30  MET 30  47  47  MET MET CCC . n 
C 1 31  GLY 31  48  48  GLY GLY CCC . n 
C 1 32  ASP 32  49  49  ASP ASP CCC . n 
C 1 33  PRO 33  50  50  PRO PRO CCC . n 
C 1 34  ASP 34  51  51  ASP ASP CCC . n 
C 1 35  GLU 35  52  52  GLU GLU CCC . n 
C 1 36  HIS 36  53  53  HIS HIS CCC . n 
C 1 37  LEU 37  54  54  LEU LEU CCC . n 
C 1 38  ARG 38  55  55  ARG ARG CCC . n 
C 1 39  GLY 39  56  56  GLY GLY CCC . n 
C 1 40  PHE 40  57  57  PHE PHE CCC . n 
C 1 41  SER 41  58  58  SER SER CCC . n 
C 1 42  LYS 42  59  59  LYS LYS CCC . n 
C 1 43  SER 43  60  60  SER SER CCC . n 
C 1 44  ILE 44  61  61  ILE ILE CCC . n 
C 1 45  SER 45  62  62  SER SER CCC . n 
C 1 46  ILE 46  63  63  ILE ILE CCC . n 
C 1 47  SER 47  64  64  SER SER CCC . n 
C 1 48  ASP 48  65  65  ASP ASP CCC . n 
C 1 49  THR 49  66  66  THR THR CCC . n 
C 1 50  PHE 50  67  67  PHE PHE CCC . n 
C 1 51  GLU 51  68  68  GLU GLU CCC . n 
C 1 52  SER 52  69  69  SER SER CCC . n 
C 1 53  ASP 53  70  70  ASP ASP CCC . n 
C 1 54  SER 54  71  71  SER SER CCC . n 
C 1 55  PRO 55  72  72  PRO PRO CCC . n 
C 1 56  ASN 56  73  73  ASN ASN CCC . n 
C 1 57  ARG 57  74  74  ARG ARG CCC . n 
C 1 58  ASP 58  75  75  ASP ASP CCC . n 
C 1 59  MET 59  76  76  MET MET CCC . n 
C 1 60  LEU 60  77  77  LEU LEU CCC . n 
C 1 61  PRO 61  78  78  PRO PRO CCC . n 
C 1 62  CYS 62  79  79  CYS CYS CCC . n 
C 1 63  TYR 63  80  80  TYR TYR CCC . n 
C 1 64  SER 64  81  81  SER SER CCC . n 
C 1 65  VAL 65  82  82  VAL VAL CCC . n 
C 1 66  ALA 66  83  83  ALA ALA CCC . n 
C 1 67  ARG 67  84  84  ARG ARG CCC . n 
C 1 68  ILE 68  85  85  ILE ILE CCC . n 
C 1 69  PRO 69  86  86  PRO PRO CCC . n 
C 1 70  LEU 70  87  87  LEU LEU CCC . n 
C 1 71  PRO 71  88  88  PRO PRO CCC . n 
C 1 72  ASN 72  89  89  ASN ASN CCC . n 
C 1 73  LEU 73  90  90  LEU LEU CCC . n 
C 1 74  ASN 74  91  ?   ?   ?   CCC . n 
C 1 75  GLU 75  92  ?   ?   ?   CCC . n 
C 1 76  ASP 76  93  ?   ?   ?   CCC . n 
C 1 77  LEU 77  94  ?   ?   ?   CCC . n 
C 1 78  THR 78  95  ?   ?   ?   CCC . n 
C 1 79  CYS 79  96  ?   ?   ?   CCC . n 
C 1 80  GLY 80  97  ?   ?   ?   CCC . n 
C 1 81  ASN 81  98  ?   ?   ?   CCC . n 
C 1 82  ILE 82  99  99  ILE ILE CCC . n 
C 1 83  LEU 83  100 100 LEU LEU CCC . n 
C 1 84  MET 84  101 101 MET MET CCC . n 
C 1 85  TRP 85  102 102 TRP TRP CCC . n 
C 1 86  GLU 86  103 103 GLU GLU CCC . n 
C 1 87  ALA 87  104 104 ALA ALA CCC . n 
C 1 88  VAL 88  105 105 VAL VAL CCC . n 
C 1 89  THR 89  106 106 THR THR CCC . n 
C 1 90  LEU 90  107 107 LEU LEU CCC . n 
C 1 91  LYS 91  108 108 LYS LYS CCC . n 
C 1 92  THR 92  109 109 THR THR CCC . n 
C 1 93  GLU 93  110 110 GLU GLU CCC . n 
C 1 94  VAL 94  111 111 VAL VAL CCC . n 
C 1 95  ILE 95  112 112 ILE ILE CCC . n 
C 1 96  GLY 96  113 113 GLY GLY CCC . n 
C 1 97  VAL 97  114 114 VAL VAL CCC . n 
C 1 98  THR 98  115 115 THR THR CCC . n 
C 1 99  SER 99  116 116 SER SER CCC . n 
C 1 100 LEU 100 117 117 LEU LEU CCC . n 
C 1 101 MET 101 118 118 MET MET CCC . n 
C 1 102 ASN 102 119 119 ASN ASN CCC . n 
C 1 103 VAL 103 120 120 VAL VAL CCC . n 
C 1 104 HIS 104 121 121 HIS HIS CCC . n 
C 1 105 SER 105 122 122 SER SER CCC . n 
C 1 106 ASN 106 123 123 ASN ASN CCC . n 
C 1 107 GLY 107 124 124 GLY GLY CCC . n 
C 1 108 GLN 108 125 125 GLN GLN CCC . n 
C 1 109 ALA 109 126 126 ALA ALA CCC . n 
C 1 110 THR 110 127 127 THR THR CCC . n 
C 1 111 HIS 111 128 128 HIS HIS CCC . n 
C 1 112 ASP 112 129 129 ASP ASP CCC . n 
C 1 113 ASN 113 130 130 ASN ASN CCC . n 
C 1 114 GLY 114 131 131 GLY GLY CCC . n 
C 1 115 ALA 115 132 132 ALA ALA CCC . n 
C 1 116 GLY 116 133 133 GLY GLY CCC . n 
C 1 117 LYS 117 134 134 LYS LYS CCC . n 
C 1 118 PRO 118 135 135 PRO PRO CCC . n 
C 1 119 VAL 119 136 136 VAL VAL CCC . n 
C 1 120 GLN 120 137 137 GLN GLN CCC . n 
C 1 121 GLY 121 138 138 GLY GLY CCC . n 
C 1 122 THR 122 139 139 THR THR CCC . n 
C 1 123 SER 123 140 140 SER SER CCC . n 
C 1 124 PHE 124 141 141 PHE PHE CCC . n 
C 1 125 HIS 125 142 142 HIS HIS CCC . n 
C 1 126 PHE 126 143 143 PHE PHE CCC . n 
C 1 127 PHE 127 144 144 PHE PHE CCC . n 
C 1 128 SER 128 145 145 SER SER CCC . n 
C 1 129 VAL 129 146 146 VAL VAL CCC . n 
C 1 130 GLY 130 147 147 GLY GLY CCC . n 
C 1 131 GLY 131 148 148 GLY GLY CCC . n 
C 1 132 GLU 132 149 149 GLU GLU CCC . n 
C 1 133 ALA 133 150 150 ALA ALA CCC . n 
C 1 134 LEU 134 151 151 LEU LEU CCC . n 
C 1 135 GLU 135 152 152 GLU GLU CCC . n 
C 1 136 LEU 136 153 153 LEU LEU CCC . n 
C 1 137 GLN 137 154 154 GLN GLN CCC . n 
C 1 138 GLY 138 155 155 GLY GLY CCC . n 
C 1 139 VAL 139 156 156 VAL VAL CCC . n 
C 1 140 LEU 140 157 157 LEU LEU CCC . n 
C 1 141 PHE 141 158 158 PHE PHE CCC . n 
C 1 142 ASN 142 159 159 ASN ASN CCC . n 
C 1 143 TYR 143 160 160 TYR TYR CCC . n 
C 1 144 ARG 144 161 161 ARG ARG CCC . n 
C 1 145 THR 145 162 162 THR THR CCC . n 
C 1 146 LYS 146 163 163 LYS LYS CCC . n 
C 1 147 TYR 147 164 164 TYR TYR CCC . n 
C 1 148 PRO 148 165 165 PRO PRO CCC . n 
C 1 149 ASP 149 166 166 ASP ASP CCC . n 
C 1 150 GLY 150 167 167 GLY GLY CCC . n 
C 1 151 THR 151 168 168 THR THR CCC . n 
C 1 152 ILE 152 169 169 ILE ILE CCC . n 
C 1 153 PHE 153 170 170 PHE PHE CCC . n 
C 1 154 PRO 154 171 171 PRO PRO CCC . n 
C 1 155 LYS 155 172 172 LYS LYS CCC . n 
C 1 156 ASN 156 173 173 ASN ASN CCC . n 
C 1 157 ALA 157 174 174 ALA ALA CCC . n 
C 1 158 THR 158 175 175 THR THR CCC . n 
C 1 159 VAL 159 176 176 VAL VAL CCC . n 
C 1 160 GLN 160 177 177 GLN GLN CCC . n 
C 1 161 SER 161 178 178 SER SER CCC . n 
C 1 162 GLN 162 179 179 GLN GLN CCC . n 
C 1 163 VAL 163 180 180 VAL VAL CCC . n 
C 1 164 MET 164 181 181 MET MET CCC . n 
C 1 165 ASN 165 182 182 ASN ASN CCC . n 
C 1 166 THR 166 183 183 THR THR CCC . n 
C 1 167 GLU 167 184 184 GLU GLU CCC . n 
C 1 168 HIS 168 185 185 HIS HIS CCC . n 
C 1 169 LYS 169 186 186 LYS LYS CCC . n 
C 1 170 ALA 170 187 187 ALA ALA CCC . n 
C 1 171 TYR 171 188 188 TYR TYR CCC . n 
C 1 172 LEU 172 189 189 LEU LEU CCC . n 
C 1 173 ASP 173 190 190 ASP ASP CCC . n 
C 1 174 LYS 174 191 191 LYS LYS CCC . n 
C 1 175 ASN 175 192 192 ASN ASN CCC . n 
C 1 176 LYS 176 193 193 LYS LYS CCC . n 
C 1 177 ALA 177 194 194 ALA ALA CCC . n 
C 1 178 TYR 178 195 195 TYR TYR CCC . n 
C 1 179 PRO 179 196 196 PRO PRO CCC . n 
C 1 180 VAL 180 197 197 VAL VAL CCC . n 
C 1 181 GLU 181 198 198 GLU GLU CCC . n 
C 1 182 CYS 182 199 199 CYS CYS CCC . n 
C 1 183 TRP 183 200 200 TRP TRP CCC . n 
C 1 184 VAL 184 201 201 VAL VAL CCC . n 
C 1 185 PRO 185 202 202 PRO PRO CCC . n 
C 1 186 ASP 186 203 203 ASP ASP CCC . n 
C 1 187 PRO 187 204 204 PRO PRO CCC . n 
C 1 188 THR 188 205 205 THR THR CCC . n 
C 1 189 ARG 189 206 206 ARG ARG CCC . n 
C 1 190 ASN 190 207 207 ASN ASN CCC . n 
C 1 191 GLU 191 208 208 GLU GLU CCC . n 
C 1 192 ASN 192 209 209 ASN ASN CCC . n 
C 1 193 THR 193 210 210 THR THR CCC . n 
C 1 194 ARG 194 211 211 ARG ARG CCC . n 
C 1 195 TYR 195 212 212 TYR TYR CCC . n 
C 1 196 PHE 196 213 213 PHE PHE CCC . n 
C 1 197 GLY 197 214 214 GLY GLY CCC . n 
C 1 198 THR 198 215 215 THR THR CCC . n 
C 1 199 LEU 199 216 216 LEU LEU CCC . n 
C 1 200 THR 200 217 217 THR THR CCC . n 
C 1 201 GLY 201 218 218 GLY GLY CCC . n 
C 1 202 GLY 202 219 219 GLY GLY CCC . n 
C 1 203 GLU 203 220 220 GLU GLU CCC . n 
C 1 204 ASN 204 221 221 ASN ASN CCC . n 
C 1 205 VAL 205 222 222 VAL VAL CCC . n 
C 1 206 PRO 206 223 223 PRO PRO CCC . n 
C 1 207 PRO 207 224 224 PRO PRO CCC . n 
C 1 208 VAL 208 225 225 VAL VAL CCC . n 
C 1 209 LEU 209 226 226 LEU LEU CCC . n 
C 1 210 HIS 210 227 227 HIS HIS CCC . n 
C 1 211 ILE 211 228 228 ILE ILE CCC . n 
C 1 212 THR 212 229 229 THR THR CCC . n 
C 1 213 ASN 213 230 230 ASN ASN CCC . n 
C 1 214 THR 214 231 231 THR THR CCC . n 
C 1 215 ALA 215 232 232 ALA ALA CCC . n 
C 1 216 THR 216 233 233 THR THR CCC . n 
C 1 217 THR 217 234 234 THR THR CCC . n 
C 1 218 VAL 218 235 235 VAL VAL CCC . n 
C 1 219 LEU 219 236 236 LEU LEU CCC . n 
C 1 220 LEU 220 237 237 LEU LEU CCC . n 
C 1 221 ASP 221 238 238 ASP ASP CCC . n 
C 1 222 GLU 222 239 239 GLU GLU CCC . n 
C 1 223 PHE 223 240 240 PHE PHE CCC . n 
C 1 224 GLY 224 241 241 GLY GLY CCC . n 
C 1 225 VAL 225 242 242 VAL VAL CCC . n 
C 1 226 GLY 226 243 243 GLY GLY CCC . n 
C 1 227 PRO 227 244 244 PRO PRO CCC . n 
C 1 228 LEU 228 245 245 LEU LEU CCC . n 
C 1 229 CYS 229 246 246 CYS CYS CCC . n 
C 1 230 LYS 230 247 247 LYS LYS CCC . n 
C 1 231 GLY 231 248 248 GLY GLY CCC . n 
C 1 232 ASP 232 249 249 ASP ASP CCC . n 
C 1 233 ASN 233 250 250 ASN ASN CCC . n 
C 1 234 LEU 234 251 251 LEU LEU CCC . n 
C 1 235 TYR 235 252 252 TYR TYR CCC . n 
C 1 236 LEU 236 253 253 LEU LEU CCC . n 
C 1 237 SER 237 254 254 SER SER CCC . n 
C 1 238 ALA 238 255 255 ALA ALA CCC . n 
C 1 239 VAL 239 256 256 VAL VAL CCC . n 
C 1 240 ASP 240 257 257 ASP ASP CCC . n 
C 1 241 VAL 241 258 258 VAL VAL CCC . n 
C 1 242 CYS 242 259 259 CYS CYS CCC . n 
C 1 243 GLY 243 260 260 GLY GLY CCC . n 
C 1 244 MET 244 261 261 MET MET CCC . n 
C 1 245 PHE 245 262 262 PHE PHE CCC . n 
C 1 246 THR 246 263 263 THR THR CCC . n 
C 1 247 ASN 247 264 264 ASN ASN CCC . n 
C 1 248 ARG 248 265 265 ARG ARG CCC . n 
C 1 249 SER 249 266 266 SER SER CCC . n 
C 1 250 GLY 250 267 267 GLY GLY CCC . n 
C 1 251 SER 251 268 268 SER SER CCC . n 
C 1 252 GLN 252 269 269 GLN GLN CCC . n 
C 1 253 GLN 253 270 270 GLN GLN CCC . n 
C 1 254 TRP 254 271 271 TRP TRP CCC . n 
C 1 255 ARG 255 272 272 ARG ARG CCC . n 
C 1 256 GLY 256 273 273 GLY GLY CCC . n 
C 1 257 LEU 257 274 274 LEU LEU CCC . n 
C 1 258 SER 258 275 275 SER SER CCC . n 
C 1 259 ARG 259 276 276 ARG ARG CCC . n 
C 1 260 TYR 260 277 277 TYR TYR CCC . n 
C 1 261 PHE 261 278 278 PHE PHE CCC . n 
C 1 262 LYS 262 279 279 LYS LYS CCC . n 
C 1 263 VAL 263 280 280 VAL VAL CCC . n 
C 1 264 GLN 264 281 281 GLN GLN CCC . n 
C 1 265 LEU 265 282 282 LEU LEU CCC . n 
C 1 266 ARG 266 283 283 ARG ARG CCC . n 
C 1 267 LYS 267 284 284 LYS LYS CCC . n 
C 1 268 ARG 268 285 285 ARG ARG CCC . n 
C 1 269 ARG 269 286 286 ARG ARG CCC . n 
C 1 270 VAL 270 287 287 VAL VAL CCC . n 
C 1 271 LYS 271 288 288 LYS LYS CCC . n 
C 1 272 ASN 272 289 289 ASN ALA CCC . n 
D 1 1   GLY 1   18  ?   ?   ?   DDD . n 
D 1 2   SER 2   19  ?   ?   ?   DDD . n 
D 1 3   HIS 3   20  ?   ?   ?   DDD . n 
D 1 4   MET 4   21  ?   ?   ?   DDD . n 
D 1 5   GLY 5   22  ?   ?   ?   DDD . n 
D 1 6   GLY 6   23  ?   ?   ?   DDD . n 
D 1 7   VAL 7   24  24  VAL ALA DDD . n 
D 1 8   GLU 8   25  25  GLU ALA DDD . n 
D 1 9   VAL 9   26  26  VAL VAL DDD . n 
D 1 10  LEU 10  27  27  LEU LEU DDD . n 
D 1 11  GLU 11  28  28  GLU GLU DDD . n 
D 1 12  VAL 12  29  29  VAL VAL DDD . n 
D 1 13  LYS 13  30  30  LYS LYS DDD . n 
D 1 14  THR 14  31  31  THR THR DDD . n 
D 1 15  GLY 15  32  32  GLY GLY DDD . n 
D 1 16  VAL 16  33  33  VAL VAL DDD . n 
D 1 17  ASP 17  34  34  ASP ASP DDD . n 
D 1 18  SER 18  35  35  SER SER DDD . n 
D 1 19  ILE 19  36  36  ILE ILE DDD . n 
D 1 20  THR 20  37  37  THR THR DDD . n 
D 1 21  GLU 21  38  38  GLU GLU DDD . n 
D 1 22  VAL 22  39  39  VAL VAL DDD . n 
D 1 23  GLU 23  40  40  GLU GLU DDD . n 
D 1 24  CYS 24  41  41  CYS CYS DDD . n 
D 1 25  PHE 25  42  42  PHE PHE DDD . n 
D 1 26  LEU 26  43  43  LEU LEU DDD . n 
D 1 27  THR 27  44  44  THR THR DDD . n 
D 1 28  PRO 28  45  45  PRO PRO DDD . n 
D 1 29  GLU 29  46  46  GLU GLU DDD . n 
D 1 30  MET 30  47  47  MET MET DDD . n 
D 1 31  GLY 31  48  48  GLY GLY DDD . n 
D 1 32  ASP 32  49  49  ASP ASP DDD . n 
D 1 33  PRO 33  50  50  PRO PRO DDD . n 
D 1 34  ASP 34  51  51  ASP ASP DDD . n 
D 1 35  GLU 35  52  52  GLU GLU DDD . n 
D 1 36  HIS 36  53  53  HIS HIS DDD . n 
D 1 37  LEU 37  54  54  LEU LEU DDD . n 
D 1 38  ARG 38  55  55  ARG ARG DDD . n 
D 1 39  GLY 39  56  56  GLY GLY DDD . n 
D 1 40  PHE 40  57  57  PHE PHE DDD . n 
D 1 41  SER 41  58  58  SER SER DDD . n 
D 1 42  LYS 42  59  59  LYS LYS DDD . n 
D 1 43  SER 43  60  60  SER SER DDD . n 
D 1 44  ILE 44  61  61  ILE ILE DDD . n 
D 1 45  SER 45  62  62  SER SER DDD . n 
D 1 46  ILE 46  63  63  ILE ILE DDD . n 
D 1 47  SER 47  64  64  SER SER DDD . n 
D 1 48  ASP 48  65  65  ASP ASP DDD . n 
D 1 49  THR 49  66  66  THR THR DDD . n 
D 1 50  PHE 50  67  67  PHE PHE DDD . n 
D 1 51  GLU 51  68  68  GLU GLU DDD . n 
D 1 52  SER 52  69  69  SER SER DDD . n 
D 1 53  ASP 53  70  70  ASP ASP DDD . n 
D 1 54  SER 54  71  71  SER SER DDD . n 
D 1 55  PRO 55  72  72  PRO PRO DDD . n 
D 1 56  ASN 56  73  73  ASN ASN DDD . n 
D 1 57  ARG 57  74  74  ARG ARG DDD . n 
D 1 58  ASP 58  75  75  ASP ASP DDD . n 
D 1 59  MET 59  76  76  MET MET DDD . n 
D 1 60  LEU 60  77  77  LEU LEU DDD . n 
D 1 61  PRO 61  78  78  PRO PRO DDD . n 
D 1 62  CYS 62  79  79  CYS CYS DDD . n 
D 1 63  TYR 63  80  80  TYR TYR DDD . n 
D 1 64  SER 64  81  81  SER SER DDD . n 
D 1 65  VAL 65  82  82  VAL VAL DDD . n 
D 1 66  ALA 66  83  83  ALA ALA DDD . n 
D 1 67  ARG 67  84  84  ARG ARG DDD . n 
D 1 68  ILE 68  85  85  ILE ILE DDD . n 
D 1 69  PRO 69  86  86  PRO PRO DDD . n 
D 1 70  LEU 70  87  87  LEU LEU DDD . n 
D 1 71  PRO 71  88  88  PRO PRO DDD . n 
D 1 72  ASN 72  89  89  ASN ASN DDD . n 
D 1 73  LEU 73  90  90  LEU LEU DDD . n 
D 1 74  ASN 74  91  91  ASN ALA DDD . n 
D 1 75  GLU 75  92  ?   ?   ?   DDD . n 
D 1 76  ASP 76  93  ?   ?   ?   DDD . n 
D 1 77  LEU 77  94  ?   ?   ?   DDD . n 
D 1 78  THR 78  95  ?   ?   ?   DDD . n 
D 1 79  CYS 79  96  ?   ?   ?   DDD . n 
D 1 80  GLY 80  97  97  GLY ALA DDD . n 
D 1 81  ASN 81  98  98  ASN ALA DDD . n 
D 1 82  ILE 82  99  99  ILE ILE DDD . n 
D 1 83  LEU 83  100 100 LEU LEU DDD . n 
D 1 84  MET 84  101 101 MET MET DDD . n 
D 1 85  TRP 85  102 102 TRP TRP DDD . n 
D 1 86  GLU 86  103 103 GLU GLU DDD . n 
D 1 87  ALA 87  104 104 ALA ALA DDD . n 
D 1 88  VAL 88  105 105 VAL VAL DDD . n 
D 1 89  THR 89  106 106 THR THR DDD . n 
D 1 90  LEU 90  107 107 LEU LEU DDD . n 
D 1 91  LYS 91  108 108 LYS LYS DDD . n 
D 1 92  THR 92  109 109 THR THR DDD . n 
D 1 93  GLU 93  110 110 GLU GLU DDD . n 
D 1 94  VAL 94  111 111 VAL VAL DDD . n 
D 1 95  ILE 95  112 112 ILE ILE DDD . n 
D 1 96  GLY 96  113 113 GLY GLY DDD . n 
D 1 97  VAL 97  114 114 VAL VAL DDD . n 
D 1 98  THR 98  115 115 THR THR DDD . n 
D 1 99  SER 99  116 116 SER SER DDD . n 
D 1 100 LEU 100 117 117 LEU LEU DDD . n 
D 1 101 MET 101 118 118 MET MET DDD . n 
D 1 102 ASN 102 119 119 ASN ASN DDD . n 
D 1 103 VAL 103 120 120 VAL VAL DDD . n 
D 1 104 HIS 104 121 121 HIS HIS DDD . n 
D 1 105 SER 105 122 122 SER SER DDD . n 
D 1 106 ASN 106 123 123 ASN ASN DDD . n 
D 1 107 GLY 107 124 124 GLY GLY DDD . n 
D 1 108 GLN 108 125 125 GLN GLN DDD . n 
D 1 109 ALA 109 126 126 ALA ALA DDD . n 
D 1 110 THR 110 127 127 THR THR DDD . n 
D 1 111 HIS 111 128 128 HIS HIS DDD . n 
D 1 112 ASP 112 129 129 ASP ASP DDD . n 
D 1 113 ASN 113 130 130 ASN ASN DDD . n 
D 1 114 GLY 114 131 131 GLY GLY DDD . n 
D 1 115 ALA 115 132 132 ALA ALA DDD . n 
D 1 116 GLY 116 133 133 GLY GLY DDD . n 
D 1 117 LYS 117 134 134 LYS LYS DDD . n 
D 1 118 PRO 118 135 135 PRO PRO DDD . n 
D 1 119 VAL 119 136 136 VAL VAL DDD . n 
D 1 120 GLN 120 137 137 GLN GLN DDD . n 
D 1 121 GLY 121 138 138 GLY GLY DDD . n 
D 1 122 THR 122 139 139 THR THR DDD . n 
D 1 123 SER 123 140 140 SER SER DDD . n 
D 1 124 PHE 124 141 141 PHE PHE DDD . n 
D 1 125 HIS 125 142 142 HIS HIS DDD . n 
D 1 126 PHE 126 143 143 PHE PHE DDD . n 
D 1 127 PHE 127 144 144 PHE PHE DDD . n 
D 1 128 SER 128 145 145 SER SER DDD . n 
D 1 129 VAL 129 146 146 VAL VAL DDD . n 
D 1 130 GLY 130 147 147 GLY GLY DDD . n 
D 1 131 GLY 131 148 148 GLY GLY DDD . n 
D 1 132 GLU 132 149 149 GLU GLU DDD . n 
D 1 133 ALA 133 150 150 ALA ALA DDD . n 
D 1 134 LEU 134 151 151 LEU LEU DDD . n 
D 1 135 GLU 135 152 152 GLU GLU DDD . n 
D 1 136 LEU 136 153 153 LEU LEU DDD . n 
D 1 137 GLN 137 154 154 GLN GLN DDD . n 
D 1 138 GLY 138 155 155 GLY GLY DDD . n 
D 1 139 VAL 139 156 156 VAL VAL DDD . n 
D 1 140 LEU 140 157 157 LEU LEU DDD . n 
D 1 141 PHE 141 158 158 PHE PHE DDD . n 
D 1 142 ASN 142 159 159 ASN ASN DDD . n 
D 1 143 TYR 143 160 160 TYR TYR DDD . n 
D 1 144 ARG 144 161 161 ARG ARG DDD . n 
D 1 145 THR 145 162 162 THR THR DDD . n 
D 1 146 LYS 146 163 163 LYS LYS DDD . n 
D 1 147 TYR 147 164 164 TYR TYR DDD . n 
D 1 148 PRO 148 165 165 PRO PRO DDD . n 
D 1 149 ASP 149 166 166 ASP ASP DDD . n 
D 1 150 GLY 150 167 167 GLY GLY DDD . n 
D 1 151 THR 151 168 168 THR THR DDD . n 
D 1 152 ILE 152 169 169 ILE ILE DDD . n 
D 1 153 PHE 153 170 170 PHE PHE DDD . n 
D 1 154 PRO 154 171 171 PRO PRO DDD . n 
D 1 155 LYS 155 172 172 LYS LYS DDD . n 
D 1 156 ASN 156 173 173 ASN ASN DDD . n 
D 1 157 ALA 157 174 174 ALA ALA DDD . n 
D 1 158 THR 158 175 175 THR THR DDD . n 
D 1 159 VAL 159 176 176 VAL VAL DDD . n 
D 1 160 GLN 160 177 177 GLN GLN DDD . n 
D 1 161 SER 161 178 178 SER SER DDD . n 
D 1 162 GLN 162 179 179 GLN GLN DDD . n 
D 1 163 VAL 163 180 180 VAL VAL DDD . n 
D 1 164 MET 164 181 181 MET MET DDD . n 
D 1 165 ASN 165 182 182 ASN ASN DDD . n 
D 1 166 THR 166 183 183 THR THR DDD . n 
D 1 167 GLU 167 184 184 GLU GLU DDD . n 
D 1 168 HIS 168 185 185 HIS HIS DDD . n 
D 1 169 LYS 169 186 186 LYS LYS DDD . n 
D 1 170 ALA 170 187 187 ALA ALA DDD . n 
D 1 171 TYR 171 188 188 TYR TYR DDD . n 
D 1 172 LEU 172 189 189 LEU LEU DDD . n 
D 1 173 ASP 173 190 190 ASP ASP DDD . n 
D 1 174 LYS 174 191 191 LYS LYS DDD . n 
D 1 175 ASN 175 192 192 ASN ASN DDD . n 
D 1 176 LYS 176 193 193 LYS LYS DDD . n 
D 1 177 ALA 177 194 194 ALA ALA DDD . n 
D 1 178 TYR 178 195 195 TYR TYR DDD . n 
D 1 179 PRO 179 196 196 PRO PRO DDD . n 
D 1 180 VAL 180 197 197 VAL VAL DDD . n 
D 1 181 GLU 181 198 198 GLU GLU DDD . n 
D 1 182 CYS 182 199 199 CYS CYS DDD . n 
D 1 183 TRP 183 200 200 TRP TRP DDD . n 
D 1 184 VAL 184 201 201 VAL VAL DDD . n 
D 1 185 PRO 185 202 202 PRO PRO DDD . n 
D 1 186 ASP 186 203 203 ASP ASP DDD . n 
D 1 187 PRO 187 204 204 PRO PRO DDD . n 
D 1 188 THR 188 205 205 THR THR DDD . n 
D 1 189 ARG 189 206 206 ARG ARG DDD . n 
D 1 190 ASN 190 207 207 ASN ASN DDD . n 
D 1 191 GLU 191 208 208 GLU GLU DDD . n 
D 1 192 ASN 192 209 209 ASN ASN DDD . n 
D 1 193 THR 193 210 210 THR THR DDD . n 
D 1 194 ARG 194 211 211 ARG ARG DDD . n 
D 1 195 TYR 195 212 212 TYR TYR DDD . n 
D 1 196 PHE 196 213 213 PHE PHE DDD . n 
D 1 197 GLY 197 214 214 GLY GLY DDD . n 
D 1 198 THR 198 215 215 THR THR DDD . n 
D 1 199 LEU 199 216 216 LEU LEU DDD . n 
D 1 200 THR 200 217 217 THR THR DDD . n 
D 1 201 GLY 201 218 218 GLY GLY DDD . n 
D 1 202 GLY 202 219 219 GLY GLY DDD . n 
D 1 203 GLU 203 220 220 GLU GLU DDD . n 
D 1 204 ASN 204 221 221 ASN ASN DDD . n 
D 1 205 VAL 205 222 222 VAL VAL DDD . n 
D 1 206 PRO 206 223 223 PRO PRO DDD . n 
D 1 207 PRO 207 224 224 PRO PRO DDD . n 
D 1 208 VAL 208 225 225 VAL VAL DDD . n 
D 1 209 LEU 209 226 226 LEU LEU DDD . n 
D 1 210 HIS 210 227 227 HIS HIS DDD . n 
D 1 211 ILE 211 228 228 ILE ILE DDD . n 
D 1 212 THR 212 229 229 THR THR DDD . n 
D 1 213 ASN 213 230 230 ASN ASN DDD . n 
D 1 214 THR 214 231 231 THR THR DDD . n 
D 1 215 ALA 215 232 232 ALA ALA DDD . n 
D 1 216 THR 216 233 233 THR THR DDD . n 
D 1 217 THR 217 234 234 THR THR DDD . n 
D 1 218 VAL 218 235 235 VAL VAL DDD . n 
D 1 219 LEU 219 236 236 LEU LEU DDD . n 
D 1 220 LEU 220 237 237 LEU LEU DDD . n 
D 1 221 ASP 221 238 238 ASP ASP DDD . n 
D 1 222 GLU 222 239 239 GLU GLU DDD . n 
D 1 223 PHE 223 240 240 PHE PHE DDD . n 
D 1 224 GLY 224 241 241 GLY GLY DDD . n 
D 1 225 VAL 225 242 242 VAL VAL DDD . n 
D 1 226 GLY 226 243 243 GLY GLY DDD . n 
D 1 227 PRO 227 244 244 PRO PRO DDD . n 
D 1 228 LEU 228 245 245 LEU LEU DDD . n 
D 1 229 CYS 229 246 246 CYS CYS DDD . n 
D 1 230 LYS 230 247 247 LYS LYS DDD . n 
D 1 231 GLY 231 248 248 GLY GLY DDD . n 
D 1 232 ASP 232 249 249 ASP ASP DDD . n 
D 1 233 ASN 233 250 250 ASN ASN DDD . n 
D 1 234 LEU 234 251 251 LEU LEU DDD . n 
D 1 235 TYR 235 252 252 TYR TYR DDD . n 
D 1 236 LEU 236 253 253 LEU LEU DDD . n 
D 1 237 SER 237 254 254 SER SER DDD . n 
D 1 238 ALA 238 255 255 ALA ALA DDD . n 
D 1 239 VAL 239 256 256 VAL VAL DDD . n 
D 1 240 ASP 240 257 257 ASP ASP DDD . n 
D 1 241 VAL 241 258 258 VAL VAL DDD . n 
D 1 242 CYS 242 259 259 CYS CYS DDD . n 
D 1 243 GLY 243 260 260 GLY GLY DDD . n 
D 1 244 MET 244 261 261 MET MET DDD . n 
D 1 245 PHE 245 262 262 PHE PHE DDD . n 
D 1 246 THR 246 263 263 THR THR DDD . n 
D 1 247 ASN 247 264 264 ASN ASN DDD . n 
D 1 248 ARG 248 265 265 ARG ARG DDD . n 
D 1 249 SER 249 266 266 SER SER DDD . n 
D 1 250 GLY 250 267 267 GLY GLY DDD . n 
D 1 251 SER 251 268 268 SER SER DDD . n 
D 1 252 GLN 252 269 269 GLN GLN DDD . n 
D 1 253 GLN 253 270 270 GLN GLN DDD . n 
D 1 254 TRP 254 271 271 TRP TRP DDD . n 
D 1 255 ARG 255 272 272 ARG ARG DDD . n 
D 1 256 GLY 256 273 273 GLY GLY DDD . n 
D 1 257 LEU 257 274 274 LEU LEU DDD . n 
D 1 258 SER 258 275 275 SER SER DDD . n 
D 1 259 ARG 259 276 276 ARG ARG DDD . n 
D 1 260 TYR 260 277 277 TYR TYR DDD . n 
D 1 261 PHE 261 278 278 PHE PHE DDD . n 
D 1 262 LYS 262 279 279 LYS LYS DDD . n 
D 1 263 VAL 263 280 280 VAL VAL DDD . n 
D 1 264 GLN 264 281 281 GLN GLN DDD . n 
D 1 265 LEU 265 282 282 LEU LEU DDD . n 
D 1 266 ARG 266 283 283 ARG ARG DDD . n 
D 1 267 LYS 267 284 284 LYS LYS DDD . n 
D 1 268 ARG 268 285 285 ARG ARG DDD . n 
D 1 269 ARG 269 286 286 ARG ARG DDD . n 
D 1 270 VAL 270 287 287 VAL VAL DDD . n 
D 1 271 LYS 271 288 288 LYS LYS DDD . n 
D 1 272 ASN 272 289 289 ASN ALA DDD . n 
E 1 1   GLY 1   18  ?   ?   ?   EEE . n 
E 1 2   SER 2   19  ?   ?   ?   EEE . n 
E 1 3   HIS 3   20  ?   ?   ?   EEE . n 
E 1 4   MET 4   21  21  MET ALA EEE . n 
E 1 5   GLY 5   22  22  GLY ALA EEE . n 
E 1 6   GLY 6   23  23  GLY ALA EEE . n 
E 1 7   VAL 7   24  24  VAL ALA EEE . n 
E 1 8   GLU 8   25  25  GLU GLU EEE . n 
E 1 9   VAL 9   26  26  VAL VAL EEE . n 
E 1 10  LEU 10  27  27  LEU LEU EEE . n 
E 1 11  GLU 11  28  28  GLU GLU EEE . n 
E 1 12  VAL 12  29  29  VAL VAL EEE . n 
E 1 13  LYS 13  30  30  LYS LYS EEE . n 
E 1 14  THR 14  31  31  THR THR EEE . n 
E 1 15  GLY 15  32  32  GLY GLY EEE . n 
E 1 16  VAL 16  33  33  VAL VAL EEE . n 
E 1 17  ASP 17  34  34  ASP ASP EEE . n 
E 1 18  SER 18  35  35  SER SER EEE . n 
E 1 19  ILE 19  36  36  ILE ILE EEE . n 
E 1 20  THR 20  37  37  THR THR EEE . n 
E 1 21  GLU 21  38  38  GLU GLU EEE . n 
E 1 22  VAL 22  39  39  VAL VAL EEE . n 
E 1 23  GLU 23  40  40  GLU GLU EEE . n 
E 1 24  CYS 24  41  41  CYS CYS EEE . n 
E 1 25  PHE 25  42  42  PHE PHE EEE . n 
E 1 26  LEU 26  43  43  LEU LEU EEE . n 
E 1 27  THR 27  44  44  THR THR EEE . n 
E 1 28  PRO 28  45  45  PRO PRO EEE . n 
E 1 29  GLU 29  46  46  GLU GLU EEE . n 
E 1 30  MET 30  47  47  MET MET EEE . n 
E 1 31  GLY 31  48  48  GLY GLY EEE . n 
E 1 32  ASP 32  49  49  ASP ASP EEE . n 
E 1 33  PRO 33  50  50  PRO PRO EEE . n 
E 1 34  ASP 34  51  51  ASP ASP EEE . n 
E 1 35  GLU 35  52  52  GLU GLU EEE . n 
E 1 36  HIS 36  53  53  HIS HIS EEE . n 
E 1 37  LEU 37  54  54  LEU LEU EEE . n 
E 1 38  ARG 38  55  55  ARG ARG EEE . n 
E 1 39  GLY 39  56  56  GLY GLY EEE . n 
E 1 40  PHE 40  57  57  PHE PHE EEE . n 
E 1 41  SER 41  58  58  SER SER EEE . n 
E 1 42  LYS 42  59  59  LYS LYS EEE . n 
E 1 43  SER 43  60  60  SER SER EEE . n 
E 1 44  ILE 44  61  61  ILE ILE EEE . n 
E 1 45  SER 45  62  62  SER SER EEE . n 
E 1 46  ILE 46  63  63  ILE ILE EEE . n 
E 1 47  SER 47  64  64  SER SER EEE . n 
E 1 48  ASP 48  65  65  ASP ASP EEE . n 
E 1 49  THR 49  66  66  THR THR EEE . n 
E 1 50  PHE 50  67  67  PHE PHE EEE . n 
E 1 51  GLU 51  68  68  GLU GLU EEE . n 
E 1 52  SER 52  69  69  SER SER EEE . n 
E 1 53  ASP 53  70  70  ASP ASP EEE . n 
E 1 54  SER 54  71  71  SER SER EEE . n 
E 1 55  PRO 55  72  72  PRO PRO EEE . n 
E 1 56  ASN 56  73  73  ASN ASN EEE . n 
E 1 57  ARG 57  74  74  ARG ARG EEE . n 
E 1 58  ASP 58  75  75  ASP ASP EEE . n 
E 1 59  MET 59  76  76  MET MET EEE . n 
E 1 60  LEU 60  77  77  LEU LEU EEE . n 
E 1 61  PRO 61  78  78  PRO PRO EEE . n 
E 1 62  CYS 62  79  79  CYS CYS EEE . n 
E 1 63  TYR 63  80  80  TYR TYR EEE . n 
E 1 64  SER 64  81  81  SER SER EEE . n 
E 1 65  VAL 65  82  82  VAL VAL EEE . n 
E 1 66  ALA 66  83  83  ALA ALA EEE . n 
E 1 67  ARG 67  84  84  ARG ARG EEE . n 
E 1 68  ILE 68  85  85  ILE ILE EEE . n 
E 1 69  PRO 69  86  86  PRO PRO EEE . n 
E 1 70  LEU 70  87  87  LEU LEU EEE . n 
E 1 71  PRO 71  88  88  PRO PRO EEE . n 
E 1 72  ASN 72  89  89  ASN ASN EEE . n 
E 1 73  LEU 73  90  90  LEU LEU EEE . n 
E 1 74  ASN 74  91  91  ASN ASN EEE . n 
E 1 75  GLU 75  92  ?   ?   ?   EEE . n 
E 1 76  ASP 76  93  ?   ?   ?   EEE . n 
E 1 77  LEU 77  94  ?   ?   ?   EEE . n 
E 1 78  THR 78  95  ?   ?   ?   EEE . n 
E 1 79  CYS 79  96  ?   ?   ?   EEE . n 
E 1 80  GLY 80  97  ?   ?   ?   EEE . n 
E 1 81  ASN 81  98  ?   ?   ?   EEE . n 
E 1 82  ILE 82  99  99  ILE ALA EEE . n 
E 1 83  LEU 83  100 100 LEU LEU EEE . n 
E 1 84  MET 84  101 101 MET MET EEE . n 
E 1 85  TRP 85  102 102 TRP TRP EEE . n 
E 1 86  GLU 86  103 103 GLU GLU EEE . n 
E 1 87  ALA 87  104 104 ALA ALA EEE . n 
E 1 88  VAL 88  105 105 VAL VAL EEE . n 
E 1 89  THR 89  106 106 THR THR EEE . n 
E 1 90  LEU 90  107 107 LEU LEU EEE . n 
E 1 91  LYS 91  108 108 LYS LYS EEE . n 
E 1 92  THR 92  109 109 THR THR EEE . n 
E 1 93  GLU 93  110 110 GLU GLU EEE . n 
E 1 94  VAL 94  111 111 VAL VAL EEE . n 
E 1 95  ILE 95  112 112 ILE ILE EEE . n 
E 1 96  GLY 96  113 113 GLY GLY EEE . n 
E 1 97  VAL 97  114 114 VAL VAL EEE . n 
E 1 98  THR 98  115 115 THR THR EEE . n 
E 1 99  SER 99  116 116 SER SER EEE . n 
E 1 100 LEU 100 117 117 LEU LEU EEE . n 
E 1 101 MET 101 118 118 MET MET EEE . n 
E 1 102 ASN 102 119 119 ASN ASN EEE . n 
E 1 103 VAL 103 120 120 VAL VAL EEE . n 
E 1 104 HIS 104 121 121 HIS HIS EEE . n 
E 1 105 SER 105 122 122 SER SER EEE . n 
E 1 106 ASN 106 123 123 ASN ASN EEE . n 
E 1 107 GLY 107 124 124 GLY GLY EEE . n 
E 1 108 GLN 108 125 125 GLN GLN EEE . n 
E 1 109 ALA 109 126 126 ALA ALA EEE . n 
E 1 110 THR 110 127 127 THR THR EEE . n 
E 1 111 HIS 111 128 128 HIS HIS EEE . n 
E 1 112 ASP 112 129 129 ASP ASP EEE . n 
E 1 113 ASN 113 130 130 ASN ASN EEE . n 
E 1 114 GLY 114 131 131 GLY GLY EEE . n 
E 1 115 ALA 115 132 132 ALA ALA EEE . n 
E 1 116 GLY 116 133 133 GLY GLY EEE . n 
E 1 117 LYS 117 134 134 LYS LYS EEE . n 
E 1 118 PRO 118 135 135 PRO PRO EEE . n 
E 1 119 VAL 119 136 136 VAL VAL EEE . n 
E 1 120 GLN 120 137 137 GLN GLN EEE . n 
E 1 121 GLY 121 138 138 GLY GLY EEE . n 
E 1 122 THR 122 139 139 THR THR EEE . n 
E 1 123 SER 123 140 140 SER SER EEE . n 
E 1 124 PHE 124 141 141 PHE PHE EEE . n 
E 1 125 HIS 125 142 142 HIS HIS EEE . n 
E 1 126 PHE 126 143 143 PHE PHE EEE . n 
E 1 127 PHE 127 144 144 PHE PHE EEE . n 
E 1 128 SER 128 145 145 SER SER EEE . n 
E 1 129 VAL 129 146 146 VAL VAL EEE . n 
E 1 130 GLY 130 147 147 GLY GLY EEE . n 
E 1 131 GLY 131 148 148 GLY GLY EEE . n 
E 1 132 GLU 132 149 149 GLU GLU EEE . n 
E 1 133 ALA 133 150 150 ALA ALA EEE . n 
E 1 134 LEU 134 151 151 LEU LEU EEE . n 
E 1 135 GLU 135 152 152 GLU GLU EEE . n 
E 1 136 LEU 136 153 153 LEU LEU EEE . n 
E 1 137 GLN 137 154 154 GLN GLN EEE . n 
E 1 138 GLY 138 155 155 GLY GLY EEE . n 
E 1 139 VAL 139 156 156 VAL VAL EEE . n 
E 1 140 LEU 140 157 157 LEU LEU EEE . n 
E 1 141 PHE 141 158 158 PHE PHE EEE . n 
E 1 142 ASN 142 159 159 ASN ASN EEE . n 
E 1 143 TYR 143 160 160 TYR TYR EEE . n 
E 1 144 ARG 144 161 161 ARG ARG EEE . n 
E 1 145 THR 145 162 162 THR THR EEE . n 
E 1 146 LYS 146 163 163 LYS LYS EEE . n 
E 1 147 TYR 147 164 164 TYR TYR EEE . n 
E 1 148 PRO 148 165 165 PRO PRO EEE . n 
E 1 149 ASP 149 166 166 ASP ASP EEE . n 
E 1 150 GLY 150 167 167 GLY GLY EEE . n 
E 1 151 THR 151 168 168 THR THR EEE . n 
E 1 152 ILE 152 169 169 ILE ILE EEE . n 
E 1 153 PHE 153 170 170 PHE PHE EEE . n 
E 1 154 PRO 154 171 171 PRO PRO EEE . n 
E 1 155 LYS 155 172 172 LYS LYS EEE . n 
E 1 156 ASN 156 173 173 ASN ASN EEE . n 
E 1 157 ALA 157 174 174 ALA ALA EEE . n 
E 1 158 THR 158 175 175 THR THR EEE . n 
E 1 159 VAL 159 176 176 VAL VAL EEE . n 
E 1 160 GLN 160 177 177 GLN GLN EEE . n 
E 1 161 SER 161 178 178 SER SER EEE . n 
E 1 162 GLN 162 179 179 GLN GLN EEE . n 
E 1 163 VAL 163 180 180 VAL VAL EEE . n 
E 1 164 MET 164 181 181 MET MET EEE . n 
E 1 165 ASN 165 182 182 ASN ASN EEE . n 
E 1 166 THR 166 183 183 THR THR EEE . n 
E 1 167 GLU 167 184 184 GLU GLU EEE . n 
E 1 168 HIS 168 185 185 HIS HIS EEE . n 
E 1 169 LYS 169 186 186 LYS LYS EEE . n 
E 1 170 ALA 170 187 187 ALA ALA EEE . n 
E 1 171 TYR 171 188 188 TYR TYR EEE . n 
E 1 172 LEU 172 189 189 LEU LEU EEE . n 
E 1 173 ASP 173 190 190 ASP ASP EEE . n 
E 1 174 LYS 174 191 191 LYS LYS EEE . n 
E 1 175 ASN 175 192 192 ASN ASN EEE . n 
E 1 176 LYS 176 193 193 LYS LYS EEE . n 
E 1 177 ALA 177 194 194 ALA ALA EEE . n 
E 1 178 TYR 178 195 195 TYR TYR EEE . n 
E 1 179 PRO 179 196 196 PRO PRO EEE . n 
E 1 180 VAL 180 197 197 VAL VAL EEE . n 
E 1 181 GLU 181 198 198 GLU GLU EEE . n 
E 1 182 CYS 182 199 199 CYS CYS EEE . n 
E 1 183 TRP 183 200 200 TRP TRP EEE . n 
E 1 184 VAL 184 201 201 VAL VAL EEE . n 
E 1 185 PRO 185 202 202 PRO PRO EEE . n 
E 1 186 ASP 186 203 203 ASP ASP EEE . n 
E 1 187 PRO 187 204 204 PRO PRO EEE . n 
E 1 188 THR 188 205 205 THR THR EEE . n 
E 1 189 ARG 189 206 206 ARG ARG EEE . n 
E 1 190 ASN 190 207 207 ASN ASN EEE . n 
E 1 191 GLU 191 208 208 GLU GLU EEE . n 
E 1 192 ASN 192 209 209 ASN ASN EEE . n 
E 1 193 THR 193 210 210 THR THR EEE . n 
E 1 194 ARG 194 211 211 ARG ARG EEE . n 
E 1 195 TYR 195 212 212 TYR TYR EEE . n 
E 1 196 PHE 196 213 213 PHE PHE EEE . n 
E 1 197 GLY 197 214 214 GLY GLY EEE . n 
E 1 198 THR 198 215 215 THR THR EEE . n 
E 1 199 LEU 199 216 216 LEU LEU EEE . n 
E 1 200 THR 200 217 217 THR THR EEE . n 
E 1 201 GLY 201 218 218 GLY GLY EEE . n 
E 1 202 GLY 202 219 219 GLY GLY EEE . n 
E 1 203 GLU 203 220 220 GLU GLU EEE . n 
E 1 204 ASN 204 221 221 ASN ASN EEE . n 
E 1 205 VAL 205 222 222 VAL VAL EEE . n 
E 1 206 PRO 206 223 223 PRO PRO EEE . n 
E 1 207 PRO 207 224 224 PRO PRO EEE . n 
E 1 208 VAL 208 225 225 VAL VAL EEE . n 
E 1 209 LEU 209 226 226 LEU LEU EEE . n 
E 1 210 HIS 210 227 227 HIS HIS EEE . n 
E 1 211 ILE 211 228 228 ILE ILE EEE . n 
E 1 212 THR 212 229 229 THR THR EEE . n 
E 1 213 ASN 213 230 230 ASN ASN EEE . n 
E 1 214 THR 214 231 231 THR THR EEE . n 
E 1 215 ALA 215 232 232 ALA ALA EEE . n 
E 1 216 THR 216 233 233 THR THR EEE . n 
E 1 217 THR 217 234 234 THR THR EEE . n 
E 1 218 VAL 218 235 235 VAL VAL EEE . n 
E 1 219 LEU 219 236 236 LEU LEU EEE . n 
E 1 220 LEU 220 237 237 LEU LEU EEE . n 
E 1 221 ASP 221 238 238 ASP ASP EEE . n 
E 1 222 GLU 222 239 239 GLU GLU EEE . n 
E 1 223 PHE 223 240 240 PHE PHE EEE . n 
E 1 224 GLY 224 241 241 GLY GLY EEE . n 
E 1 225 VAL 225 242 242 VAL VAL EEE . n 
E 1 226 GLY 226 243 243 GLY GLY EEE . n 
E 1 227 PRO 227 244 244 PRO PRO EEE . n 
E 1 228 LEU 228 245 245 LEU LEU EEE . n 
E 1 229 CYS 229 246 246 CYS CYS EEE . n 
E 1 230 LYS 230 247 247 LYS LYS EEE . n 
E 1 231 GLY 231 248 248 GLY GLY EEE . n 
E 1 232 ASP 232 249 249 ASP ASP EEE . n 
E 1 233 ASN 233 250 250 ASN ASN EEE . n 
E 1 234 LEU 234 251 251 LEU LEU EEE . n 
E 1 235 TYR 235 252 252 TYR TYR EEE . n 
E 1 236 LEU 236 253 253 LEU LEU EEE . n 
E 1 237 SER 237 254 254 SER SER EEE . n 
E 1 238 ALA 238 255 255 ALA ALA EEE . n 
E 1 239 VAL 239 256 256 VAL VAL EEE . n 
E 1 240 ASP 240 257 257 ASP ASP EEE . n 
E 1 241 VAL 241 258 258 VAL VAL EEE . n 
E 1 242 CYS 242 259 259 CYS CYS EEE . n 
E 1 243 GLY 243 260 260 GLY GLY EEE . n 
E 1 244 MET 244 261 261 MET MET EEE . n 
E 1 245 PHE 245 262 262 PHE PHE EEE . n 
E 1 246 THR 246 263 263 THR THR EEE . n 
E 1 247 ASN 247 264 264 ASN ASN EEE . n 
E 1 248 ARG 248 265 265 ARG ARG EEE . n 
E 1 249 SER 249 266 266 SER SER EEE . n 
E 1 250 GLY 250 267 267 GLY GLY EEE . n 
E 1 251 SER 251 268 268 SER SER EEE . n 
E 1 252 GLN 252 269 269 GLN GLN EEE . n 
E 1 253 GLN 253 270 270 GLN GLN EEE . n 
E 1 254 TRP 254 271 271 TRP TRP EEE . n 
E 1 255 ARG 255 272 272 ARG ARG EEE . n 
E 1 256 GLY 256 273 273 GLY GLY EEE . n 
E 1 257 LEU 257 274 274 LEU LEU EEE . n 
E 1 258 SER 258 275 275 SER SER EEE . n 
E 1 259 ARG 259 276 276 ARG ARG EEE . n 
E 1 260 TYR 260 277 277 TYR TYR EEE . n 
E 1 261 PHE 261 278 278 PHE PHE EEE . n 
E 1 262 LYS 262 279 279 LYS LYS EEE . n 
E 1 263 VAL 263 280 280 VAL VAL EEE . n 
E 1 264 GLN 264 281 281 GLN GLN EEE . n 
E 1 265 LEU 265 282 282 LEU LEU EEE . n 
E 1 266 ARG 266 283 283 ARG ARG EEE . n 
E 1 267 LYS 267 284 284 LYS LYS EEE . n 
E 1 268 ARG 268 285 285 ARG ARG EEE . n 
E 1 269 ARG 269 286 286 ARG ARG EEE . n 
E 1 270 VAL 270 287 287 VAL VAL EEE . n 
E 1 271 LYS 271 288 288 LYS LYS EEE . n 
E 1 272 ASN 272 289 289 ASN ALA EEE . n 
F 2 1   GLN 1   1   ?   ?   ?   FFF . n 
F 2 2   SER 2   2   2   SER SER FFF . n 
F 2 3   VAL 3   3   3   VAL VAL FFF . n 
F 2 4   LEU 4   4   4   LEU LEU FFF . n 
F 2 5   THR 5   5   5   THR THR FFF . n 
F 2 6   GLN 6   6   6   GLN GLN FFF . n 
F 2 7   PRO 7   7   7   PRO PRO FFF . n 
F 2 8   PRO 8   8   8   PRO PRO FFF . n 
F 2 9   SER 9   9   9   SER SER FFF . n 
F 2 10  ALA 10  10  10  ALA ALA FFF . n 
F 2 11  SER 11  11  11  SER SER FFF . n 
F 2 12  GLY 12  12  12  GLY GLY FFF . n 
F 2 13  THR 13  13  13  THR THR FFF . n 
F 2 14  PRO 14  14  14  PRO PRO FFF . n 
F 2 15  GLY 15  15  15  GLY GLY FFF . n 
F 2 16  GLN 16  16  16  GLN GLN FFF . n 
F 2 17  ARG 17  17  17  ARG ARG FFF . n 
F 2 18  VAL 18  18  18  VAL VAL FFF . n 
F 2 19  THR 19  19  19  THR THR FFF . n 
F 2 20  ILE 20  20  20  ILE ILE FFF . n 
F 2 21  SER 21  21  21  SER SER FFF . n 
F 2 22  CYS 22  22  22  CYS CYS FFF . n 
F 2 23  SER 23  23  23  SER SER FFF . n 
F 2 24  GLY 24  24  24  GLY GLY FFF . n 
F 2 25  GLY 25  25  25  GLY GLY FFF . n 
F 2 26  SER 26  26  26  SER SER FFF . n 
F 2 27  SER 27  27  27  SER SER FFF . n 
F 2 28  ASN 28  28  28  ASN ASN FFF . n 
F 2 29  ILE 29  29  29  ILE ILE FFF . n 
F 2 30  GLY 30  30  30  GLY GLY FFF . n 
F 2 31  SER 31  31  31  SER SER FFF . n 
F 2 32  ASN 32  32  32  ASN ASN FFF . n 
F 2 33  PRO 33  33  33  PRO PRO FFF . n 
F 2 34  VAL 34  34  34  VAL VAL FFF . n 
F 2 35  ASN 35  35  35  ASN ASN FFF . n 
F 2 36  TRP 36  36  36  TRP TRP FFF . n 
F 2 37  PHE 37  37  37  PHE PHE FFF . n 
F 2 38  GLN 38  38  38  GLN GLN FFF . n 
F 2 39  GLN 39  39  39  GLN GLN FFF . n 
F 2 40  PHE 40  40  40  PHE PHE FFF . n 
F 2 41  PRO 41  41  41  PRO PRO FFF . n 
F 2 42  GLY 42  42  42  GLY GLY FFF . n 
F 2 43  THR 43  43  43  THR THR FFF . n 
F 2 44  ALA 44  44  44  ALA ALA FFF . n 
F 2 45  PRO 45  45  45  PRO PRO FFF . n 
F 2 46  LYS 46  46  46  LYS LYS FFF . n 
F 2 47  LEU 47  47  47  LEU LEU FFF . n 
F 2 48  LEU 48  48  48  LEU LEU FFF . n 
F 2 49  ILE 49  49  49  ILE ILE FFF . n 
F 2 50  TYR 50  50  50  TYR TYR FFF . n 
F 2 51  ALA 51  51  51  ALA ALA FFF . n 
F 2 52  ASN 52  52  52  ASN ASN FFF . n 
F 2 53  THR 53  53  53  THR THR FFF . n 
F 2 54  GLN 54  54  54  GLN GLN FFF . n 
F 2 55  ARG 55  55  55  ARG ARG FFF . n 
F 2 56  PRO 56  56  56  PRO PRO FFF . n 
F 2 57  SER 57  57  57  SER SER FFF . n 
F 2 58  GLY 58  58  58  GLY GLY FFF . n 
F 2 59  VAL 59  59  59  VAL VAL FFF . n 
F 2 60  PRO 60  60  60  PRO PRO FFF . n 
F 2 61  ASP 61  61  61  ASP ASP FFF . n 
F 2 62  ARG 62  62  62  ARG ARG FFF . n 
F 2 63  PHE 63  63  63  PHE PHE FFF . n 
F 2 64  SER 64  64  64  SER SER FFF . n 
F 2 65  GLY 65  65  65  GLY GLY FFF . n 
F 2 66  SER 66  66  66  SER SER FFF . n 
F 2 67  LYS 67  67  67  LYS LYS FFF . n 
F 2 68  SER 68  68  68  SER SER FFF . n 
F 2 69  GLY 69  69  69  GLY GLY FFF . n 
F 2 70  THR 70  70  70  THR THR FFF . n 
F 2 71  SER 71  71  71  SER SER FFF . n 
F 2 72  VAL 72  72  72  VAL VAL FFF . n 
F 2 73  SER 73  73  73  SER SER FFF . n 
F 2 74  LEU 74  74  74  LEU LEU FFF . n 
F 2 75  ALA 75  75  75  ALA ALA FFF . n 
F 2 76  ILE 76  76  76  ILE ILE FFF . n 
F 2 77  SER 77  77  77  SER SER FFF . n 
F 2 78  GLY 78  78  78  GLY GLY FFF . n 
F 2 79  LEU 79  79  79  LEU LEU FFF . n 
F 2 80  GLN 80  80  80  GLN GLN FFF . n 
F 2 81  SER 81  81  81  SER SER FFF . n 
F 2 82  GLU 82  82  82  GLU GLU FFF . n 
F 2 83  ASP 83  83  83  ASP ASP FFF . n 
F 2 84  GLU 84  84  84  GLU GLU FFF . n 
F 2 85  GLY 85  85  85  GLY GLY FFF . n 
F 2 86  ASP 86  86  86  ASP ASP FFF . n 
F 2 87  TYR 87  87  87  TYR TYR FFF . n 
F 2 88  HIS 88  88  88  HIS HIS FFF . n 
F 2 89  CYS 89  89  89  CYS CYS FFF . n 
F 2 90  ALA 90  90  90  ALA ALA FFF . n 
F 2 91  ALA 91  91  91  ALA ALA FFF . n 
F 2 92  TRP 92  92  92  TRP TRP FFF . n 
F 2 93  ASP 93  93  93  ASP ASP FFF . n 
F 2 94  ASP 94  94  94  ASP ASP FFF . n 
F 2 95  SER 95  95  95  SER SER FFF . n 
F 2 96  LEU 96  96  96  LEU LEU FFF . n 
F 2 97  LYS 97  97  97  LYS LYS FFF . n 
F 2 98  GLY 98  98  98  GLY GLY FFF . n 
F 2 99  TRP 99  99  99  TRP TRP FFF . n 
F 2 100 VAL 100 100 100 VAL VAL FFF . n 
F 2 101 PHE 101 101 101 PHE PHE FFF . n 
F 2 102 GLY 102 102 102 GLY GLY FFF . n 
F 2 103 GLY 103 103 103 GLY GLY FFF . n 
F 2 104 GLY 104 104 104 GLY GLY FFF . n 
F 2 105 THR 105 105 105 THR THR FFF . n 
F 2 106 LYS 106 106 106 LYS LYS FFF . n 
F 2 107 LEU 107 107 107 LEU LEU FFF . n 
F 2 108 THR 108 108 108 THR THR FFF . n 
F 2 109 VAL 109 109 109 VAL VAL FFF . n 
F 2 110 LEU 110 110 110 LEU LEU FFF . n 
F 2 111 GLY 111 111 111 GLY GLY FFF . n 
F 2 112 ALA 112 112 112 ALA ALA FFF . n 
F 2 113 PRO 113 113 113 PRO PRO FFF . n 
F 2 114 LYS 114 114 114 LYS LYS FFF . n 
F 2 115 ALA 115 115 115 ALA ALA FFF . n 
F 2 116 ASN 116 116 116 ASN ASN FFF . n 
F 2 117 PRO 117 117 117 PRO PRO FFF . n 
F 2 118 THR 118 118 118 THR THR FFF . n 
F 2 119 VAL 119 119 119 VAL VAL FFF . n 
F 2 120 THR 120 120 120 THR THR FFF . n 
F 2 121 LEU 121 121 121 LEU LEU FFF . n 
F 2 122 PHE 122 122 122 PHE PHE FFF . n 
F 2 123 PRO 123 123 123 PRO PRO FFF . n 
F 2 124 PRO 124 124 124 PRO PRO FFF . n 
F 2 125 SER 125 125 125 SER SER FFF . n 
F 2 126 SER 126 126 126 SER SER FFF . n 
F 2 127 GLU 127 127 ?   ?   ?   FFF . n 
F 2 128 GLU 128 128 ?   ?   ?   FFF . n 
F 2 129 LEU 129 129 ?   ?   ?   FFF . n 
F 2 130 GLN 130 130 ?   ?   ?   FFF . n 
F 2 131 ALA 131 131 ?   ?   ?   FFF . n 
F 2 132 ASN 132 132 132 ASN ASN FFF . n 
F 2 133 LYS 133 133 133 LYS LYS FFF . n 
F 2 134 ALA 134 134 134 ALA ALA FFF . n 
F 2 135 THR 135 135 135 THR THR FFF . n 
F 2 136 LEU 136 136 136 LEU LEU FFF . n 
F 2 137 VAL 137 137 137 VAL VAL FFF . n 
F 2 138 CYS 138 138 138 CYS CYS FFF . n 
F 2 139 LEU 139 139 139 LEU LEU FFF . n 
F 2 140 ILE 140 140 140 ILE ILE FFF . n 
F 2 141 SER 141 141 141 SER SER FFF . n 
F 2 142 ASP 142 142 142 ASP ASP FFF . n 
F 2 143 PHE 143 143 143 PHE PHE FFF . n 
F 2 144 TYR 144 144 144 TYR TYR FFF . n 
F 2 145 PRO 145 145 145 PRO PRO FFF . n 
F 2 146 GLY 146 146 146 GLY GLY FFF . n 
F 2 147 ALA 147 147 147 ALA ALA FFF . n 
F 2 148 VAL 148 148 148 VAL VAL FFF . n 
F 2 149 THR 149 149 149 THR THR FFF . n 
F 2 150 VAL 150 150 150 VAL VAL FFF . n 
F 2 151 ALA 151 151 151 ALA ALA FFF . n 
F 2 152 TRP 152 152 152 TRP TRP FFF . n 
F 2 153 LYS 153 153 ?   ?   ?   FFF . n 
F 2 154 ALA 154 154 ?   ?   ?   FFF . n 
F 2 155 ASP 155 155 ?   ?   ?   FFF . n 
F 2 156 GLY 156 156 ?   ?   ?   FFF . n 
F 2 157 SER 157 157 ?   ?   ?   FFF . n 
F 2 158 PRO 158 158 ?   ?   ?   FFF . n 
F 2 159 VAL 159 159 ?   ?   ?   FFF . n 
F 2 160 LYS 160 160 ?   ?   ?   FFF . n 
F 2 161 ALA 161 161 161 ALA ALA FFF . n 
F 2 162 GLY 162 162 162 GLY GLY FFF . n 
F 2 163 VAL 163 163 163 VAL VAL FFF . n 
F 2 164 GLU 164 164 164 GLU GLU FFF . n 
F 2 165 THR 165 165 165 THR THR FFF . n 
F 2 166 THR 166 166 166 THR THR FFF . n 
F 2 167 LYS 167 167 167 LYS LYS FFF . n 
F 2 168 PRO 168 168 168 PRO PRO FFF . n 
F 2 169 SER 169 169 169 SER SER FFF . n 
F 2 170 LYS 170 170 170 LYS LYS FFF . n 
F 2 171 GLN 171 171 171 GLN GLN FFF . n 
F 2 172 SER 172 172 172 SER SER FFF . n 
F 2 173 ASN 173 173 173 ASN ASN FFF . n 
F 2 174 ASN 174 174 174 ASN ASN FFF . n 
F 2 175 LYS 175 175 175 LYS LYS FFF . n 
F 2 176 THR 176 176 176 THR THR FFF . n 
F 2 177 ALA 177 177 177 ALA ALA FFF . n 
F 2 178 ALA 178 178 178 ALA ALA FFF . n 
F 2 179 SER 179 179 179 SER SER FFF . n 
F 2 180 SER 180 180 180 SER SER FFF . n 
F 2 181 TYR 181 181 181 TYR TYR FFF . n 
F 2 182 LEU 182 182 182 LEU LEU FFF . n 
F 2 183 SER 183 183 183 SER SER FFF . n 
F 2 184 LEU 184 184 184 LEU LEU FFF . n 
F 2 185 THR 185 185 185 THR THR FFF . n 
F 2 186 PRO 186 186 186 PRO PRO FFF . n 
F 2 187 GLU 187 187 ?   ?   ?   FFF . n 
F 2 188 GLN 188 188 ?   ?   ?   FFF . n 
F 2 189 TRP 189 189 ?   ?   ?   FFF . n 
F 2 190 LYS 190 190 ?   ?   ?   FFF . n 
F 2 191 SER 191 191 ?   ?   ?   FFF . n 
F 2 192 HIS 192 192 ?   ?   ?   FFF . n 
F 2 193 ARG 193 193 ?   ?   ?   FFF . n 
F 2 194 SER 194 194 194 SER SER FFF . n 
F 2 195 TYR 195 195 195 TYR TYR FFF . n 
F 2 196 SER 196 196 196 SER SER FFF . n 
F 2 197 CYS 197 197 197 CYS CYS FFF . n 
F 2 198 GLN 198 198 198 GLN GLN FFF . n 
F 2 199 VAL 199 199 199 VAL VAL FFF . n 
F 2 200 THR 200 200 200 THR THR FFF . n 
F 2 201 HIS 201 201 201 HIS HIS FFF . n 
F 2 202 GLU 202 202 202 GLU GLU FFF . n 
F 2 203 GLY 203 203 203 GLY GLY FFF . n 
F 2 204 THR 204 204 204 THR THR FFF . n 
F 2 205 THR 205 205 205 THR THR FFF . n 
F 2 206 VAL 206 206 206 VAL VAL FFF . n 
F 2 207 GLU 207 207 207 GLU GLU FFF . n 
F 2 208 LYS 208 208 208 LYS LYS FFF . n 
F 2 209 THR 209 209 209 THR THR FFF . n 
F 2 210 VAL 210 210 210 VAL VAL FFF . n 
F 2 211 ALA 211 211 211 ALA ALA FFF . n 
F 2 212 PRO 212 212 212 PRO PRO FFF . n 
G 2 1   GLN 1   1   ?   ?   ?   GGG . n 
G 2 2   SER 2   2   ?   ?   ?   GGG . n 
G 2 3   VAL 3   3   ?   ?   ?   GGG . n 
G 2 4   LEU 4   4   4   LEU LEU GGG . n 
G 2 5   THR 5   5   5   THR THR GGG . n 
G 2 6   GLN 6   6   6   GLN GLN GGG . n 
G 2 7   PRO 7   7   7   PRO PRO GGG . n 
G 2 8   PRO 8   8   8   PRO PRO GGG . n 
G 2 9   SER 9   9   9   SER SER GGG . n 
G 2 10  ALA 10  10  10  ALA ALA GGG . n 
G 2 11  SER 11  11  11  SER SER GGG . n 
G 2 12  GLY 12  12  12  GLY GLY GGG . n 
G 2 13  THR 13  13  13  THR THR GGG . n 
G 2 14  PRO 14  14  14  PRO PRO GGG . n 
G 2 15  GLY 15  15  15  GLY GLY GGG . n 
G 2 16  GLN 16  16  16  GLN GLN GGG . n 
G 2 17  ARG 17  17  17  ARG ARG GGG . n 
G 2 18  VAL 18  18  18  VAL VAL GGG . n 
G 2 19  THR 19  19  19  THR THR GGG . n 
G 2 20  ILE 20  20  20  ILE ILE GGG . n 
G 2 21  SER 21  21  21  SER SER GGG . n 
G 2 22  CYS 22  22  22  CYS CYS GGG . n 
G 2 23  SER 23  23  23  SER SER GGG . n 
G 2 24  GLY 24  24  24  GLY GLY GGG . n 
G 2 25  GLY 25  25  25  GLY GLY GGG . n 
G 2 26  SER 26  26  26  SER SER GGG . n 
G 2 27  SER 27  27  27  SER SER GGG . n 
G 2 28  ASN 28  28  28  ASN ASN GGG . n 
G 2 29  ILE 29  29  29  ILE ILE GGG . n 
G 2 30  GLY 30  30  30  GLY GLY GGG . n 
G 2 31  SER 31  31  31  SER SER GGG . n 
G 2 32  ASN 32  32  32  ASN ASN GGG . n 
G 2 33  PRO 33  33  33  PRO PRO GGG . n 
G 2 34  VAL 34  34  34  VAL VAL GGG . n 
G 2 35  ASN 35  35  35  ASN ASN GGG . n 
G 2 36  TRP 36  36  36  TRP TRP GGG . n 
G 2 37  PHE 37  37  37  PHE PHE GGG . n 
G 2 38  GLN 38  38  38  GLN GLN GGG . n 
G 2 39  GLN 39  39  39  GLN GLN GGG . n 
G 2 40  PHE 40  40  40  PHE PHE GGG . n 
G 2 41  PRO 41  41  41  PRO PRO GGG . n 
G 2 42  GLY 42  42  42  GLY GLY GGG . n 
G 2 43  THR 43  43  43  THR THR GGG . n 
G 2 44  ALA 44  44  44  ALA ALA GGG . n 
G 2 45  PRO 45  45  45  PRO PRO GGG . n 
G 2 46  LYS 46  46  46  LYS LYS GGG . n 
G 2 47  LEU 47  47  47  LEU LEU GGG . n 
G 2 48  LEU 48  48  48  LEU LEU GGG . n 
G 2 49  ILE 49  49  49  ILE ILE GGG . n 
G 2 50  TYR 50  50  50  TYR TYR GGG . n 
G 2 51  ALA 51  51  51  ALA ALA GGG . n 
G 2 52  ASN 52  52  52  ASN ASN GGG . n 
G 2 53  THR 53  53  53  THR THR GGG . n 
G 2 54  GLN 54  54  54  GLN GLN GGG . n 
G 2 55  ARG 55  55  55  ARG ARG GGG . n 
G 2 56  PRO 56  56  56  PRO PRO GGG . n 
G 2 57  SER 57  57  57  SER SER GGG . n 
G 2 58  GLY 58  58  58  GLY GLY GGG . n 
G 2 59  VAL 59  59  59  VAL VAL GGG . n 
G 2 60  PRO 60  60  60  PRO PRO GGG . n 
G 2 61  ASP 61  61  61  ASP ASP GGG . n 
G 2 62  ARG 62  62  62  ARG ARG GGG . n 
G 2 63  PHE 63  63  63  PHE PHE GGG . n 
G 2 64  SER 64  64  64  SER SER GGG . n 
G 2 65  GLY 65  65  65  GLY GLY GGG . n 
G 2 66  SER 66  66  66  SER SER GGG . n 
G 2 67  LYS 67  67  67  LYS LYS GGG . n 
G 2 68  SER 68  68  68  SER SER GGG . n 
G 2 69  GLY 69  69  69  GLY GLY GGG . n 
G 2 70  THR 70  70  70  THR THR GGG . n 
G 2 71  SER 71  71  71  SER SER GGG . n 
G 2 72  VAL 72  72  72  VAL VAL GGG . n 
G 2 73  SER 73  73  73  SER SER GGG . n 
G 2 74  LEU 74  74  74  LEU LEU GGG . n 
G 2 75  ALA 75  75  75  ALA ALA GGG . n 
G 2 76  ILE 76  76  76  ILE ILE GGG . n 
G 2 77  SER 77  77  77  SER SER GGG . n 
G 2 78  GLY 78  78  78  GLY GLY GGG . n 
G 2 79  LEU 79  79  79  LEU LEU GGG . n 
G 2 80  GLN 80  80  80  GLN GLN GGG . n 
G 2 81  SER 81  81  81  SER SER GGG . n 
G 2 82  GLU 82  82  82  GLU GLU GGG . n 
G 2 83  ASP 83  83  83  ASP ASP GGG . n 
G 2 84  GLU 84  84  84  GLU GLU GGG . n 
G 2 85  GLY 85  85  85  GLY GLY GGG . n 
G 2 86  ASP 86  86  86  ASP ASP GGG . n 
G 2 87  TYR 87  87  87  TYR TYR GGG . n 
G 2 88  HIS 88  88  88  HIS HIS GGG . n 
G 2 89  CYS 89  89  89  CYS CYS GGG . n 
G 2 90  ALA 90  90  90  ALA ALA GGG . n 
G 2 91  ALA 91  91  91  ALA ALA GGG . n 
G 2 92  TRP 92  92  92  TRP TRP GGG . n 
G 2 93  ASP 93  93  93  ASP ASP GGG . n 
G 2 94  ASP 94  94  94  ASP ASP GGG . n 
G 2 95  SER 95  95  95  SER SER GGG . n 
G 2 96  LEU 96  96  96  LEU LEU GGG . n 
G 2 97  LYS 97  97  97  LYS LYS GGG . n 
G 2 98  GLY 98  98  98  GLY GLY GGG . n 
G 2 99  TRP 99  99  99  TRP TRP GGG . n 
G 2 100 VAL 100 100 100 VAL VAL GGG . n 
G 2 101 PHE 101 101 101 PHE PHE GGG . n 
G 2 102 GLY 102 102 102 GLY GLY GGG . n 
G 2 103 GLY 103 103 103 GLY GLY GGG . n 
G 2 104 GLY 104 104 104 GLY GLY GGG . n 
G 2 105 THR 105 105 105 THR THR GGG . n 
G 2 106 LYS 106 106 106 LYS LYS GGG . n 
G 2 107 LEU 107 107 107 LEU LEU GGG . n 
G 2 108 THR 108 108 108 THR THR GGG . n 
G 2 109 VAL 109 109 109 VAL VAL GGG . n 
G 2 110 LEU 110 110 110 LEU LEU GGG . n 
G 2 111 GLY 111 111 111 GLY GLY GGG . n 
G 2 112 ALA 112 112 112 ALA ALA GGG . n 
G 2 113 PRO 113 113 113 PRO PRO GGG . n 
G 2 114 LYS 114 114 114 LYS LYS GGG . n 
G 2 115 ALA 115 115 115 ALA ALA GGG . n 
G 2 116 ASN 116 116 116 ASN ASN GGG . n 
G 2 117 PRO 117 117 117 PRO PRO GGG . n 
G 2 118 THR 118 118 118 THR THR GGG . n 
G 2 119 VAL 119 119 119 VAL VAL GGG . n 
G 2 120 THR 120 120 120 THR THR GGG . n 
G 2 121 LEU 121 121 121 LEU LEU GGG . n 
G 2 122 PHE 122 122 122 PHE PHE GGG . n 
G 2 123 PRO 123 123 123 PRO PRO GGG . n 
G 2 124 PRO 124 124 124 PRO PRO GGG . n 
G 2 125 SER 125 125 ?   ?   ?   GGG . n 
G 2 126 SER 126 126 ?   ?   ?   GGG . n 
G 2 127 GLU 127 127 ?   ?   ?   GGG . n 
G 2 128 GLU 128 128 ?   ?   ?   GGG . n 
G 2 129 LEU 129 129 ?   ?   ?   GGG . n 
G 2 130 GLN 130 130 ?   ?   ?   GGG . n 
G 2 131 ALA 131 131 ?   ?   ?   GGG . n 
G 2 132 ASN 132 132 ?   ?   ?   GGG . n 
G 2 133 LYS 133 133 ?   ?   ?   GGG . n 
G 2 134 ALA 134 134 134 ALA ALA GGG . n 
G 2 135 THR 135 135 135 THR THR GGG . n 
G 2 136 LEU 136 136 136 LEU LEU GGG . n 
G 2 137 VAL 137 137 137 VAL VAL GGG . n 
G 2 138 CYS 138 138 138 CYS CYS GGG . n 
G 2 139 LEU 139 139 139 LEU LEU GGG . n 
G 2 140 ILE 140 140 140 ILE ILE GGG . n 
G 2 141 SER 141 141 141 SER SER GGG . n 
G 2 142 ASP 142 142 142 ASP ASP GGG . n 
G 2 143 PHE 143 143 143 PHE PHE GGG . n 
G 2 144 TYR 144 144 144 TYR TYR GGG . n 
G 2 145 PRO 145 145 145 PRO PRO GGG . n 
G 2 146 GLY 146 146 146 GLY GLY GGG . n 
G 2 147 ALA 147 147 147 ALA ALA GGG . n 
G 2 148 VAL 148 148 148 VAL VAL GGG . n 
G 2 149 THR 149 149 149 THR THR GGG . n 
G 2 150 VAL 150 150 ?   ?   ?   GGG . n 
G 2 151 ALA 151 151 ?   ?   ?   GGG . n 
G 2 152 TRP 152 152 ?   ?   ?   GGG . n 
G 2 153 LYS 153 153 ?   ?   ?   GGG . n 
G 2 154 ALA 154 154 ?   ?   ?   GGG . n 
G 2 155 ASP 155 155 ?   ?   ?   GGG . n 
G 2 156 GLY 156 156 ?   ?   ?   GGG . n 
G 2 157 SER 157 157 ?   ?   ?   GGG . n 
G 2 158 PRO 158 158 ?   ?   ?   GGG . n 
G 2 159 VAL 159 159 ?   ?   ?   GGG . n 
G 2 160 LYS 160 160 ?   ?   ?   GGG . n 
G 2 161 ALA 161 161 ?   ?   ?   GGG . n 
G 2 162 GLY 162 162 162 GLY GLY GGG . n 
G 2 163 VAL 163 163 163 VAL VAL GGG . n 
G 2 164 GLU 164 164 164 GLU GLU GGG . n 
G 2 165 THR 165 165 165 THR THR GGG . n 
G 2 166 THR 166 166 166 THR THR GGG . n 
G 2 167 LYS 167 167 167 LYS LYS GGG . n 
G 2 168 PRO 168 168 168 PRO PRO GGG . n 
G 2 169 SER 169 169 169 SER SER GGG . n 
G 2 170 LYS 170 170 170 LYS LYS GGG . n 
G 2 171 GLN 171 171 171 GLN GLN GGG . n 
G 2 172 SER 172 172 172 SER SER GGG . n 
G 2 173 ASN 173 173 173 ASN ASN GGG . n 
G 2 174 ASN 174 174 174 ASN ASN GGG . n 
G 2 175 LYS 175 175 175 LYS LYS GGG . n 
G 2 176 THR 176 176 176 THR THR GGG . n 
G 2 177 ALA 177 177 177 ALA ALA GGG . n 
G 2 178 ALA 178 178 178 ALA ALA GGG . n 
G 2 179 SER 179 179 179 SER SER GGG . n 
G 2 180 SER 180 180 180 SER SER GGG . n 
G 2 181 TYR 181 181 181 TYR TYR GGG . n 
G 2 182 LEU 182 182 182 LEU LEU GGG . n 
G 2 183 SER 183 183 ?   ?   ?   GGG . n 
G 2 184 LEU 184 184 ?   ?   ?   GGG . n 
G 2 185 THR 185 185 ?   ?   ?   GGG . n 
G 2 186 PRO 186 186 ?   ?   ?   GGG . n 
G 2 187 GLU 187 187 ?   ?   ?   GGG . n 
G 2 188 GLN 188 188 ?   ?   ?   GGG . n 
G 2 189 TRP 189 189 ?   ?   ?   GGG . n 
G 2 190 LYS 190 190 ?   ?   ?   GGG . n 
G 2 191 SER 191 191 ?   ?   ?   GGG . n 
G 2 192 HIS 192 192 ?   ?   ?   GGG . n 
G 2 193 ARG 193 193 ?   ?   ?   GGG . n 
G 2 194 SER 194 194 ?   ?   ?   GGG . n 
G 2 195 TYR 195 195 195 TYR TYR GGG . n 
G 2 196 SER 196 196 196 SER SER GGG . n 
G 2 197 CYS 197 197 197 CYS CYS GGG . n 
G 2 198 GLN 198 198 198 GLN GLN GGG . n 
G 2 199 VAL 199 199 199 VAL VAL GGG . n 
G 2 200 THR 200 200 200 THR THR GGG . n 
G 2 201 HIS 201 201 201 HIS HIS GGG . n 
G 2 202 GLU 202 202 202 GLU GLU GGG . n 
G 2 203 GLY 203 203 203 GLY GLY GGG . n 
G 2 204 THR 204 204 204 THR THR GGG . n 
G 2 205 THR 205 205 205 THR THR GGG . n 
G 2 206 VAL 206 206 206 VAL VAL GGG . n 
G 2 207 GLU 207 207 207 GLU GLU GGG . n 
G 2 208 LYS 208 208 208 LYS LYS GGG . n 
G 2 209 THR 209 209 209 THR THR GGG . n 
G 2 210 VAL 210 210 210 VAL VAL GGG . n 
G 2 211 ALA 211 211 211 ALA ALA GGG . n 
G 2 212 PRO 212 212 212 PRO PRO GGG . n 
H 3 1   GLU 1   1   1   GLU GLU HHH . n 
H 3 2   VAL 2   2   2   VAL VAL HHH . n 
H 3 3   GLN 3   3   3   GLN GLN HHH . n 
H 3 4   LEU 4   4   4   LEU LEU HHH . n 
H 3 5   VAL 5   5   5   VAL VAL HHH . n 
H 3 6   GLU 6   6   6   GLU GLU HHH . n 
H 3 7   SER 7   7   7   SER SER HHH . n 
H 3 8   GLY 8   8   8   GLY GLY HHH . n 
H 3 9   GLY 9   9   9   GLY GLY HHH . n 
H 3 10  GLY 10  10  10  GLY GLY HHH . n 
H 3 11  LEU 11  11  11  LEU LEU HHH . n 
H 3 12  VAL 12  12  12  VAL VAL HHH . n 
H 3 13  LYS 13  13  13  LYS LYS HHH . n 
H 3 14  PRO 14  14  14  PRO PRO HHH . n 
H 3 15  GLY 15  15  15  GLY GLY HHH . n 
H 3 16  GLY 16  16  16  GLY GLY HHH . n 
H 3 17  SER 17  17  17  SER SER HHH . n 
H 3 18  LEU 18  18  18  LEU LEU HHH . n 
H 3 19  ARG 19  19  19  ARG ARG HHH . n 
H 3 20  LEU 20  20  20  LEU LEU HHH . n 
H 3 21  SER 21  21  21  SER SER HHH . n 
H 3 22  CYS 22  22  22  CYS CYS HHH . n 
H 3 23  ALA 23  23  23  ALA ALA HHH . n 
H 3 24  ALA 24  24  24  ALA ALA HHH . n 
H 3 25  SER 25  25  25  SER SER HHH . n 
H 3 26  GLY 26  26  26  GLY GLY HHH . n 
H 3 27  PHE 27  27  27  PHE PHE HHH . n 
H 3 28  THR 28  28  28  THR THR HHH . n 
H 3 29  PHE 29  29  29  PHE PHE HHH . n 
H 3 30  SER 30  30  30  SER SER HHH . n 
H 3 31  SER 31  31  31  SER SER HHH . n 
H 3 32  TYR 32  32  32  TYR TYR HHH . n 
H 3 33  THR 33  33  33  THR THR HHH . n 
H 3 34  MET 34  34  34  MET MET HHH . n 
H 3 35  ASN 35  35  35  ASN ASN HHH . n 
H 3 36  TRP 36  36  36  TRP TRP HHH . n 
H 3 37  VAL 37  37  37  VAL VAL HHH . n 
H 3 38  ARG 38  38  38  ARG ARG HHH . n 
H 3 39  GLN 39  39  39  GLN GLN HHH . n 
H 3 40  ALA 40  40  40  ALA ALA HHH . n 
H 3 41  PRO 41  41  41  PRO PRO HHH . n 
H 3 42  GLY 42  42  42  GLY GLY HHH . n 
H 3 43  LYS 43  43  43  LYS LYS HHH . n 
H 3 44  GLY 44  44  44  GLY GLY HHH . n 
H 3 45  LEU 45  45  45  LEU LEU HHH . n 
H 3 46  GLN 46  46  46  GLN GLN HHH . n 
H 3 47  TRP 47  47  47  TRP TRP HHH . n 
H 3 48  VAL 48  48  48  VAL VAL HHH . n 
H 3 49  SER 49  49  49  SER SER HHH . n 
H 3 50  SER 50  50  50  SER SER HHH . n 
H 3 51  ILE 51  51  51  ILE ILE HHH . n 
H 3 52  SER 52  52  52  SER SER HHH . n 
H 3 53  SER 53  53  53  SER SER HHH . n 
H 3 54  SER 54  54  54  SER SER HHH . n 
H 3 55  SER 55  55  55  SER SER HHH . n 
H 3 56  THR 56  56  56  THR THR HHH . n 
H 3 57  TYR 57  57  57  TYR TYR HHH . n 
H 3 58  MET 58  58  58  MET MET HHH . n 
H 3 59  TYR 59  59  59  TYR TYR HHH . n 
H 3 60  TYR 60  60  60  TYR TYR HHH . n 
H 3 61  GLY 61  61  61  GLY GLY HHH . n 
H 3 62  ASP 62  62  62  ASP ASP HHH . n 
H 3 63  SER 63  63  63  SER SER HHH . n 
H 3 64  VAL 64  64  64  VAL VAL HHH . n 
H 3 65  LYS 65  65  65  LYS LYS HHH . n 
H 3 66  GLY 66  66  66  GLY GLY HHH . n 
H 3 67  ARG 67  67  67  ARG ARG HHH . n 
H 3 68  PHE 68  68  68  PHE PHE HHH . n 
H 3 69  THR 69  69  69  THR THR HHH . n 
H 3 70  ILE 70  70  70  ILE ILE HHH . n 
H 3 71  SER 71  71  71  SER SER HHH . n 
H 3 72  ARG 72  72  72  ARG ARG HHH . n 
H 3 73  ASP 73  73  73  ASP ASP HHH . n 
H 3 74  ASN 74  74  74  ASN ASN HHH . n 
H 3 75  ALA 75  75  75  ALA ALA HHH . n 
H 3 76  ARG 76  76  76  ARG ARG HHH . n 
H 3 77  ASN 77  77  77  ASN ASN HHH . n 
H 3 78  SER 78  78  78  SER SER HHH . n 
H 3 79  LEU 79  79  79  LEU LEU HHH . n 
H 3 80  TYR 80  80  80  TYR TYR HHH . n 
H 3 81  LEU 81  81  81  LEU LEU HHH . n 
H 3 82  GLN 82  82  82  GLN GLN HHH . n 
H 3 83  MET 83  83  83  MET MET HHH . n 
H 3 84  ASN 84  84  84  ASN ASN HHH . n 
H 3 85  SER 85  85  85  SER SER HHH . n 
H 3 86  LEU 86  86  86  LEU LEU HHH . n 
H 3 87  ARG 87  87  87  ARG ARG HHH . n 
H 3 88  VAL 88  88  88  VAL VAL HHH . n 
H 3 89  GLU 89  89  89  GLU GLU HHH . n 
H 3 90  ASP 90  90  90  ASP ASP HHH . n 
H 3 91  THR 91  91  91  THR THR HHH . n 
H 3 92  ALA 92  92  92  ALA ALA HHH . n 
H 3 93  VAL 93  93  93  VAL VAL HHH . n 
H 3 94  TYR 94  94  94  TYR TYR HHH . n 
H 3 95  TYR 95  95  95  TYR TYR HHH . n 
H 3 96  CYS 96  96  96  CYS CYS HHH . n 
H 3 97  ALA 97  97  97  ALA ALA HHH . n 
H 3 98  ARG 98  98  98  ARG ARG HHH . n 
H 3 99  TYR 99  99  99  TYR TYR HHH . n 
H 3 100 ALA 100 100 100 ALA ALA HHH . n 
H 3 101 HIS 101 101 101 HIS HIS HHH . n 
H 3 102 ASP 102 102 102 ASP ASP HHH . n 
H 3 103 TRP 103 103 103 TRP TRP HHH . n 
H 3 104 ASN 104 104 104 ASN ASN HHH . n 
H 3 105 VAL 105 105 105 VAL VAL HHH . n 
H 3 106 ASP 106 106 106 ASP ASP HHH . n 
H 3 107 TYR 107 107 107 TYR TYR HHH . n 
H 3 108 TRP 108 108 108 TRP TRP HHH . n 
H 3 109 GLY 109 109 109 GLY GLY HHH . n 
H 3 110 GLN 110 110 110 GLN GLN HHH . n 
H 3 111 GLY 111 111 111 GLY GLY HHH . n 
H 3 112 THR 112 112 112 THR THR HHH . n 
H 3 113 LEU 113 113 113 LEU LEU HHH . n 
H 3 114 VAL 114 114 114 VAL VAL HHH . n 
H 3 115 THR 115 115 115 THR THR HHH . n 
H 3 116 VAL 116 116 116 VAL VAL HHH . n 
H 3 117 SER 117 117 117 SER SER HHH . n 
H 3 118 SER 118 118 118 SER SER HHH . n 
H 3 119 ALA 119 119 119 ALA ALA HHH . n 
H 3 120 SER 120 120 120 SER SER HHH . n 
H 3 121 THR 121 121 121 THR THR HHH . n 
H 3 122 LYS 122 122 122 LYS LYS HHH . n 
H 3 123 GLY 123 123 123 GLY GLY HHH . n 
H 3 124 PRO 124 124 124 PRO PRO HHH . n 
H 3 125 SER 125 125 125 SER SER HHH . n 
H 3 126 VAL 126 126 126 VAL VAL HHH . n 
H 3 127 PHE 127 132 ?   ?   ?   HHH . n 
H 3 128 PRO 128 133 ?   ?   ?   HHH . n 
H 3 129 LEU 129 134 ?   ?   ?   HHH . n 
H 3 130 ALA 130 135 ?   ?   ?   HHH . n 
H 3 131 PRO 131 136 ?   ?   ?   HHH . n 
H 3 132 SER 132 137 ?   ?   ?   HHH . n 
H 3 133 SER 133 138 ?   ?   ?   HHH . n 
H 3 134 LYS 134 139 ?   ?   ?   HHH . n 
H 3 135 SER 135 140 ?   ?   ?   HHH . n 
H 3 136 THR 136 141 ?   ?   ?   HHH . n 
H 3 137 SER 137 142 ?   ?   ?   HHH . n 
H 3 138 GLY 138 143 ?   ?   ?   HHH . n 
H 3 139 GLY 139 144 ?   ?   ?   HHH . n 
H 3 140 THR 140 145 ?   ?   ?   HHH . n 
H 3 141 ALA 141 146 ?   ?   ?   HHH . n 
H 3 142 ALA 142 147 ?   ?   ?   HHH . n 
H 3 143 LEU 143 148 ?   ?   ?   HHH . n 
H 3 144 GLY 144 149 ?   ?   ?   HHH . n 
H 3 145 CYS 145 150 ?   ?   ?   HHH . n 
H 3 146 LEU 146 151 ?   ?   ?   HHH . n 
H 3 147 VAL 147 152 152 VAL VAL HHH . n 
H 3 148 LYS 148 153 153 LYS LYS HHH . n 
H 3 149 ASP 149 154 154 ASP ASP HHH . n 
H 3 150 TYR 150 155 155 TYR TYR HHH . n 
H 3 151 PHE 151 156 156 PHE PHE HHH . n 
H 3 152 PRO 152 157 157 PRO PRO HHH . n 
H 3 153 GLU 153 158 158 GLU GLU HHH . n 
H 3 154 PRO 154 159 159 PRO PRO HHH . n 
H 3 155 VAL 155 160 ?   ?   ?   HHH . n 
H 3 156 THR 156 161 ?   ?   ?   HHH . n 
H 3 157 VAL 157 162 ?   ?   ?   HHH . n 
H 3 158 SER 158 163 ?   ?   ?   HHH . n 
H 3 159 TRP 159 164 ?   ?   ?   HHH . n 
H 3 160 ASN 160 165 ?   ?   ?   HHH . n 
H 3 161 SER 161 166 ?   ?   ?   HHH . n 
H 3 162 GLY 162 167 ?   ?   ?   HHH . n 
H 3 163 ALA 163 168 ?   ?   ?   HHH . n 
H 3 164 LEU 164 169 ?   ?   ?   HHH . n 
H 3 165 THR 165 170 ?   ?   ?   HHH . n 
H 3 166 SER 166 171 ?   ?   ?   HHH . n 
H 3 167 GLY 167 172 ?   ?   ?   HHH . n 
H 3 168 VAL 168 173 ?   ?   ?   HHH . n 
H 3 169 HIS 169 174 ?   ?   ?   HHH . n 
H 3 170 THR 170 175 175 THR THR HHH . n 
H 3 171 PHE 171 176 176 PHE PHE HHH . n 
H 3 172 PRO 172 177 177 PRO PRO HHH . n 
H 3 173 ALA 173 178 178 ALA ALA HHH . n 
H 3 174 VAL 174 179 179 VAL VAL HHH . n 
H 3 175 LEU 175 180 180 LEU LEU HHH . n 
H 3 176 GLN 176 181 181 GLN GLN HHH . n 
H 3 177 SER 177 182 182 SER SER HHH . n 
H 3 178 SER 178 183 183 SER SER HHH . n 
H 3 179 GLY 179 184 184 GLY GLY HHH . n 
H 3 180 LEU 180 185 185 LEU LEU HHH . n 
H 3 181 TYR 181 186 186 TYR TYR HHH . n 
H 3 182 SER 182 187 187 SER SER HHH . n 
H 3 183 LEU 183 188 188 LEU LEU HHH . n 
H 3 184 SER 184 189 189 SER SER HHH . n 
H 3 185 SER 185 190 ?   ?   ?   HHH . n 
H 3 186 VAL 186 191 ?   ?   ?   HHH . n 
H 3 187 VAL 187 192 ?   ?   ?   HHH . n 
H 3 188 THR 188 193 ?   ?   ?   HHH . n 
H 3 189 VAL 189 194 ?   ?   ?   HHH . n 
H 3 190 PRO 190 195 ?   ?   ?   HHH . n 
H 3 191 SER 191 196 ?   ?   ?   HHH . n 
H 3 192 SER 192 197 ?   ?   ?   HHH . n 
H 3 193 SER 193 198 ?   ?   ?   HHH . n 
H 3 194 LEU 194 199 ?   ?   ?   HHH . n 
H 3 195 GLY 195 200 ?   ?   ?   HHH . n 
H 3 196 THR 196 201 ?   ?   ?   HHH . n 
H 3 197 GLN 197 202 ?   ?   ?   HHH . n 
H 3 198 THR 198 203 ?   ?   ?   HHH . n 
H 3 199 TYR 199 204 ?   ?   ?   HHH . n 
H 3 200 ILE 200 205 ?   ?   ?   HHH . n 
H 3 201 CYS 201 206 ?   ?   ?   HHH . n 
H 3 202 ASN 202 207 ?   ?   ?   HHH . n 
H 3 203 VAL 203 208 ?   ?   ?   HHH . n 
H 3 204 ASN 204 209 ?   ?   ?   HHH . n 
H 3 205 HIS 205 210 ?   ?   ?   HHH . n 
H 3 206 LYS 206 211 ?   ?   ?   HHH . n 
H 3 207 PRO 207 212 ?   ?   ?   HHH . n 
H 3 208 SER 208 213 ?   ?   ?   HHH . n 
H 3 209 ASN 209 214 ?   ?   ?   HHH . n 
H 3 210 THR 210 215 ?   ?   ?   HHH . n 
H 3 211 LYS 211 216 ?   ?   ?   HHH . n 
H 3 212 VAL 212 217 ?   ?   ?   HHH . n 
H 3 213 ASP 213 218 ?   ?   ?   HHH . n 
H 3 214 LYS 214 219 ?   ?   ?   HHH . n 
H 3 215 LYS 215 220 ?   ?   ?   HHH . n 
H 3 216 VAL 216 221 ?   ?   ?   HHH . n 
H 3 217 GLU 217 222 ?   ?   ?   HHH . n 
H 3 218 PRO 218 223 ?   ?   ?   HHH . n 
H 3 219 LYS 219 224 ?   ?   ?   HHH . n 
H 3 220 SER 220 225 ?   ?   ?   HHH . n 
H 3 221 CYS 221 226 ?   ?   ?   HHH . n 
H 3 222 ASP 222 227 ?   ?   ?   HHH . n 
H 3 223 LYS 223 228 ?   ?   ?   HHH . n 
H 3 224 THR 224 229 ?   ?   ?   HHH . n 
H 3 225 HIS 225 230 ?   ?   ?   HHH . n 
H 3 226 THR 226 231 ?   ?   ?   HHH . n 
H 3 227 CYS 227 232 ?   ?   ?   HHH . n 
H 3 228 PRO 228 233 ?   ?   ?   HHH . n 
H 3 229 PRO 229 234 ?   ?   ?   HHH . n 
H 3 230 CYS 230 235 ?   ?   ?   HHH . n 
H 3 231 PRO 231 236 ?   ?   ?   HHH . n 
H 3 232 ALA 232 237 ?   ?   ?   HHH . n 
H 3 233 PRO 233 238 ?   ?   ?   HHH . n 
H 3 234 GLU 234 239 ?   ?   ?   HHH . n 
H 3 235 LEU 235 240 ?   ?   ?   HHH . n 
H 3 236 LEU 236 241 ?   ?   ?   HHH . n 
H 3 237 GLY 237 242 ?   ?   ?   HHH . n 
H 3 238 GLY 238 243 ?   ?   ?   HHH . n 
H 3 239 PRO 239 244 ?   ?   ?   HHH . n 
H 3 240 SER 240 245 ?   ?   ?   HHH . n 
H 3 241 VAL 241 246 ?   ?   ?   HHH . n 
H 3 242 PHE 242 247 ?   ?   ?   HHH . n 
H 3 243 LEU 243 248 ?   ?   ?   HHH . n 
H 3 244 PHE 244 249 ?   ?   ?   HHH . n 
H 3 245 PRO 245 250 ?   ?   ?   HHH . n 
H 3 246 PRO 246 251 ?   ?   ?   HHH . n 
H 3 247 LYS 247 252 ?   ?   ?   HHH . n 
H 3 248 PRO 248 253 ?   ?   ?   HHH . n 
H 3 249 LYS 249 254 ?   ?   ?   HHH . n 
H 3 250 ASP 250 255 ?   ?   ?   HHH . n 
H 3 251 THR 251 256 ?   ?   ?   HHH . n 
H 3 252 LEU 252 257 ?   ?   ?   HHH . n 
H 3 253 MET 253 258 ?   ?   ?   HHH . n 
H 3 254 ILE 254 259 ?   ?   ?   HHH . n 
H 3 255 SER 255 260 ?   ?   ?   HHH . n 
H 3 256 ARG 256 261 ?   ?   ?   HHH . n 
H 3 257 THR 257 262 ?   ?   ?   HHH . n 
H 3 258 PRO 258 263 ?   ?   ?   HHH . n 
H 3 259 GLU 259 264 ?   ?   ?   HHH . n 
H 3 260 VAL 260 265 ?   ?   ?   HHH . n 
H 3 261 THR 261 266 ?   ?   ?   HHH . n 
H 3 262 CYS 262 267 ?   ?   ?   HHH . n 
H 3 263 VAL 263 268 ?   ?   ?   HHH . n 
H 3 264 VAL 264 269 ?   ?   ?   HHH . n 
H 3 265 VAL 265 270 ?   ?   ?   HHH . n 
H 3 266 ASP 266 271 ?   ?   ?   HHH . n 
H 3 267 VAL 267 272 ?   ?   ?   HHH . n 
H 3 268 SER 268 273 ?   ?   ?   HHH . n 
H 3 269 HIS 269 274 ?   ?   ?   HHH . n 
H 3 270 GLU 270 275 ?   ?   ?   HHH . n 
H 3 271 ASP 271 276 ?   ?   ?   HHH . n 
H 3 272 PRO 272 277 ?   ?   ?   HHH . n 
H 3 273 GLU 273 278 ?   ?   ?   HHH . n 
H 3 274 VAL 274 279 ?   ?   ?   HHH . n 
H 3 275 LYS 275 280 ?   ?   ?   HHH . n 
H 3 276 PHE 276 281 ?   ?   ?   HHH . n 
H 3 277 ASN 277 282 ?   ?   ?   HHH . n 
H 3 278 TRP 278 283 ?   ?   ?   HHH . n 
H 3 279 TYR 279 284 ?   ?   ?   HHH . n 
H 3 280 VAL 280 285 ?   ?   ?   HHH . n 
H 3 281 ASP 281 286 ?   ?   ?   HHH . n 
H 3 282 GLY 282 287 ?   ?   ?   HHH . n 
H 3 283 VAL 283 288 ?   ?   ?   HHH . n 
H 3 284 GLU 284 289 ?   ?   ?   HHH . n 
H 3 285 VAL 285 290 ?   ?   ?   HHH . n 
H 3 286 HIS 286 291 ?   ?   ?   HHH . n 
H 3 287 ASN 287 292 ?   ?   ?   HHH . n 
H 3 288 ALA 288 293 ?   ?   ?   HHH . n 
H 3 289 LYS 289 294 ?   ?   ?   HHH . n 
H 3 290 THR 290 295 ?   ?   ?   HHH . n 
H 3 291 LYS 291 296 ?   ?   ?   HHH . n 
H 3 292 PRO 292 297 ?   ?   ?   HHH . n 
H 3 293 ARG 293 298 ?   ?   ?   HHH . n 
H 3 294 GLU 294 299 ?   ?   ?   HHH . n 
H 3 295 GLU 295 300 ?   ?   ?   HHH . n 
H 3 296 GLN 296 301 ?   ?   ?   HHH . n 
H 3 297 TYR 297 302 ?   ?   ?   HHH . n 
H 3 298 ASN 298 303 ?   ?   ?   HHH . n 
H 3 299 SER 299 304 ?   ?   ?   HHH . n 
H 3 300 THR 300 305 ?   ?   ?   HHH . n 
H 3 301 TYR 301 306 ?   ?   ?   HHH . n 
H 3 302 ARG 302 307 ?   ?   ?   HHH . n 
H 3 303 VAL 303 308 ?   ?   ?   HHH . n 
H 3 304 VAL 304 309 ?   ?   ?   HHH . n 
H 3 305 SER 305 310 ?   ?   ?   HHH . n 
H 3 306 VAL 306 311 ?   ?   ?   HHH . n 
H 3 307 LEU 307 312 ?   ?   ?   HHH . n 
H 3 308 THR 308 313 ?   ?   ?   HHH . n 
H 3 309 VAL 309 314 ?   ?   ?   HHH . n 
H 3 310 LEU 310 315 ?   ?   ?   HHH . n 
H 3 311 HIS 311 316 ?   ?   ?   HHH . n 
H 3 312 GLN 312 317 ?   ?   ?   HHH . n 
H 3 313 ASP 313 318 ?   ?   ?   HHH . n 
H 3 314 TRP 314 319 ?   ?   ?   HHH . n 
H 3 315 LEU 315 320 ?   ?   ?   HHH . n 
H 3 316 ASN 316 321 ?   ?   ?   HHH . n 
H 3 317 GLY 317 322 ?   ?   ?   HHH . n 
H 3 318 LYS 318 323 ?   ?   ?   HHH . n 
H 3 319 GLU 319 324 ?   ?   ?   HHH . n 
H 3 320 TYR 320 325 ?   ?   ?   HHH . n 
H 3 321 LYS 321 326 ?   ?   ?   HHH . n 
H 3 322 CYS 322 327 ?   ?   ?   HHH . n 
H 3 323 LYS 323 328 ?   ?   ?   HHH . n 
H 3 324 VAL 324 329 ?   ?   ?   HHH . n 
H 3 325 SER 325 330 ?   ?   ?   HHH . n 
H 3 326 ASN 326 331 ?   ?   ?   HHH . n 
H 3 327 LYS 327 332 ?   ?   ?   HHH . n 
H 3 328 ALA 328 333 ?   ?   ?   HHH . n 
H 3 329 LEU 329 334 ?   ?   ?   HHH . n 
H 3 330 PRO 330 335 ?   ?   ?   HHH . n 
H 3 331 ALA 331 336 ?   ?   ?   HHH . n 
H 3 332 PRO 332 337 ?   ?   ?   HHH . n 
H 3 333 ILE 333 338 ?   ?   ?   HHH . n 
H 3 334 GLU 334 339 ?   ?   ?   HHH . n 
H 3 335 LYS 335 340 ?   ?   ?   HHH . n 
H 3 336 THR 336 341 ?   ?   ?   HHH . n 
H 3 337 ILE 337 342 ?   ?   ?   HHH . n 
H 3 338 SER 338 343 ?   ?   ?   HHH . n 
H 3 339 LYS 339 344 ?   ?   ?   HHH . n 
H 3 340 ALA 340 345 ?   ?   ?   HHH . n 
H 3 341 LYS 341 346 ?   ?   ?   HHH . n 
H 3 342 GLY 342 347 ?   ?   ?   HHH . n 
H 3 343 GLN 343 348 ?   ?   ?   HHH . n 
H 3 344 PRO 344 349 ?   ?   ?   HHH . n 
H 3 345 ARG 345 350 ?   ?   ?   HHH . n 
H 3 346 GLU 346 351 ?   ?   ?   HHH . n 
H 3 347 PRO 347 352 ?   ?   ?   HHH . n 
H 3 348 GLN 348 353 ?   ?   ?   HHH . n 
H 3 349 VAL 349 354 ?   ?   ?   HHH . n 
H 3 350 TYR 350 355 ?   ?   ?   HHH . n 
H 3 351 THR 351 356 ?   ?   ?   HHH . n 
H 3 352 LEU 352 357 ?   ?   ?   HHH . n 
H 3 353 PRO 353 358 ?   ?   ?   HHH . n 
H 3 354 PRO 354 359 ?   ?   ?   HHH . n 
H 3 355 SER 355 360 ?   ?   ?   HHH . n 
H 3 356 ARG 356 361 ?   ?   ?   HHH . n 
H 3 357 ASP 357 362 ?   ?   ?   HHH . n 
H 3 358 GLU 358 363 ?   ?   ?   HHH . n 
H 3 359 LEU 359 364 ?   ?   ?   HHH . n 
H 3 360 THR 360 365 ?   ?   ?   HHH . n 
H 3 361 LYS 361 366 ?   ?   ?   HHH . n 
H 3 362 ASN 362 367 ?   ?   ?   HHH . n 
H 3 363 GLN 363 368 ?   ?   ?   HHH . n 
H 3 364 VAL 364 369 ?   ?   ?   HHH . n 
H 3 365 SER 365 370 ?   ?   ?   HHH . n 
H 3 366 LEU 366 371 ?   ?   ?   HHH . n 
H 3 367 THR 367 372 ?   ?   ?   HHH . n 
H 3 368 CYS 368 373 ?   ?   ?   HHH . n 
H 3 369 LEU 369 374 ?   ?   ?   HHH . n 
H 3 370 VAL 370 375 ?   ?   ?   HHH . n 
H 3 371 LYS 371 376 ?   ?   ?   HHH . n 
H 3 372 GLY 372 377 ?   ?   ?   HHH . n 
H 3 373 PHE 373 378 ?   ?   ?   HHH . n 
H 3 374 TYR 374 379 ?   ?   ?   HHH . n 
H 3 375 PRO 375 380 ?   ?   ?   HHH . n 
H 3 376 SER 376 381 ?   ?   ?   HHH . n 
H 3 377 ASP 377 382 ?   ?   ?   HHH . n 
H 3 378 ILE 378 383 ?   ?   ?   HHH . n 
H 3 379 ALA 379 384 ?   ?   ?   HHH . n 
H 3 380 VAL 380 385 ?   ?   ?   HHH . n 
H 3 381 GLU 381 386 ?   ?   ?   HHH . n 
H 3 382 TRP 382 387 ?   ?   ?   HHH . n 
H 3 383 GLU 383 388 ?   ?   ?   HHH . n 
H 3 384 SER 384 389 ?   ?   ?   HHH . n 
H 3 385 ASN 385 390 ?   ?   ?   HHH . n 
H 3 386 GLY 386 391 ?   ?   ?   HHH . n 
H 3 387 GLN 387 392 ?   ?   ?   HHH . n 
H 3 388 PRO 388 393 ?   ?   ?   HHH . n 
H 3 389 GLU 389 394 ?   ?   ?   HHH . n 
H 3 390 ASN 390 395 ?   ?   ?   HHH . n 
H 3 391 ASN 391 396 ?   ?   ?   HHH . n 
H 3 392 TYR 392 397 ?   ?   ?   HHH . n 
H 3 393 LYS 393 398 ?   ?   ?   HHH . n 
H 3 394 THR 394 399 ?   ?   ?   HHH . n 
H 3 395 THR 395 400 ?   ?   ?   HHH . n 
H 3 396 PRO 396 401 ?   ?   ?   HHH . n 
H 3 397 PRO 397 402 ?   ?   ?   HHH . n 
H 3 398 VAL 398 403 ?   ?   ?   HHH . n 
I 2 1   GLN 1   1   ?   ?   ?   III . n 
I 2 2   SER 2   2   2   SER SER III . n 
I 2 3   VAL 3   3   3   VAL VAL III . n 
I 2 4   LEU 4   4   4   LEU LEU III . n 
I 2 5   THR 5   5   5   THR THR III . n 
I 2 6   GLN 6   6   6   GLN GLN III . n 
I 2 7   PRO 7   7   7   PRO PRO III . n 
I 2 8   PRO 8   8   8   PRO PRO III . n 
I 2 9   SER 9   9   9   SER SER III . n 
I 2 10  ALA 10  10  10  ALA ALA III . n 
I 2 11  SER 11  11  11  SER SER III . n 
I 2 12  GLY 12  12  12  GLY GLY III . n 
I 2 13  THR 13  13  13  THR THR III . n 
I 2 14  PRO 14  14  14  PRO PRO III . n 
I 2 15  GLY 15  15  15  GLY GLY III . n 
I 2 16  GLN 16  16  16  GLN GLN III . n 
I 2 17  ARG 17  17  17  ARG ARG III . n 
I 2 18  VAL 18  18  18  VAL VAL III . n 
I 2 19  THR 19  19  19  THR THR III . n 
I 2 20  ILE 20  20  20  ILE ILE III . n 
I 2 21  SER 21  21  21  SER SER III . n 
I 2 22  CYS 22  22  22  CYS CYS III . n 
I 2 23  SER 23  23  23  SER SER III . n 
I 2 24  GLY 24  24  24  GLY GLY III . n 
I 2 25  GLY 25  25  25  GLY GLY III . n 
I 2 26  SER 26  26  26  SER SER III . n 
I 2 27  SER 27  27  27  SER SER III . n 
I 2 28  ASN 28  28  28  ASN ASN III . n 
I 2 29  ILE 29  29  29  ILE ILE III . n 
I 2 30  GLY 30  30  30  GLY GLY III . n 
I 2 31  SER 31  31  31  SER SER III . n 
I 2 32  ASN 32  32  32  ASN ASN III . n 
I 2 33  PRO 33  33  33  PRO PRO III . n 
I 2 34  VAL 34  34  34  VAL VAL III . n 
I 2 35  ASN 35  35  35  ASN ASN III . n 
I 2 36  TRP 36  36  36  TRP TRP III . n 
I 2 37  PHE 37  37  37  PHE PHE III . n 
I 2 38  GLN 38  38  38  GLN GLN III . n 
I 2 39  GLN 39  39  39  GLN GLN III . n 
I 2 40  PHE 40  40  40  PHE PHE III . n 
I 2 41  PRO 41  41  41  PRO PRO III . n 
I 2 42  GLY 42  42  42  GLY GLY III . n 
I 2 43  THR 43  43  43  THR THR III . n 
I 2 44  ALA 44  44  44  ALA ALA III . n 
I 2 45  PRO 45  45  45  PRO PRO III . n 
I 2 46  LYS 46  46  46  LYS LYS III . n 
I 2 47  LEU 47  47  47  LEU LEU III . n 
I 2 48  LEU 48  48  48  LEU LEU III . n 
I 2 49  ILE 49  49  49  ILE ILE III . n 
I 2 50  TYR 50  50  50  TYR TYR III . n 
I 2 51  ALA 51  51  51  ALA ALA III . n 
I 2 52  ASN 52  52  52  ASN ASN III . n 
I 2 53  THR 53  53  53  THR THR III . n 
I 2 54  GLN 54  54  54  GLN GLN III . n 
I 2 55  ARG 55  55  55  ARG ARG III . n 
I 2 56  PRO 56  56  56  PRO PRO III . n 
I 2 57  SER 57  57  57  SER SER III . n 
I 2 58  GLY 58  58  58  GLY GLY III . n 
I 2 59  VAL 59  59  59  VAL VAL III . n 
I 2 60  PRO 60  60  60  PRO PRO III . n 
I 2 61  ASP 61  61  61  ASP ASP III . n 
I 2 62  ARG 62  62  62  ARG ARG III . n 
I 2 63  PHE 63  63  63  PHE PHE III . n 
I 2 64  SER 64  64  64  SER SER III . n 
I 2 65  GLY 65  65  65  GLY GLY III . n 
I 2 66  SER 66  66  66  SER SER III . n 
I 2 67  LYS 67  67  67  LYS LYS III . n 
I 2 68  SER 68  68  68  SER SER III . n 
I 2 69  GLY 69  69  69  GLY GLY III . n 
I 2 70  THR 70  70  70  THR THR III . n 
I 2 71  SER 71  71  71  SER SER III . n 
I 2 72  VAL 72  72  72  VAL VAL III . n 
I 2 73  SER 73  73  73  SER SER III . n 
I 2 74  LEU 74  74  74  LEU LEU III . n 
I 2 75  ALA 75  75  75  ALA ALA III . n 
I 2 76  ILE 76  76  76  ILE ILE III . n 
I 2 77  SER 77  77  77  SER SER III . n 
I 2 78  GLY 78  78  78  GLY GLY III . n 
I 2 79  LEU 79  79  79  LEU LEU III . n 
I 2 80  GLN 80  80  80  GLN GLN III . n 
I 2 81  SER 81  81  81  SER SER III . n 
I 2 82  GLU 82  82  82  GLU GLU III . n 
I 2 83  ASP 83  83  83  ASP ASP III . n 
I 2 84  GLU 84  84  84  GLU GLU III . n 
I 2 85  GLY 85  85  85  GLY GLY III . n 
I 2 86  ASP 86  86  86  ASP ASP III . n 
I 2 87  TYR 87  87  87  TYR TYR III . n 
I 2 88  HIS 88  88  88  HIS HIS III . n 
I 2 89  CYS 89  89  89  CYS CYS III . n 
I 2 90  ALA 90  90  90  ALA ALA III . n 
I 2 91  ALA 91  91  91  ALA ALA III . n 
I 2 92  TRP 92  92  92  TRP TRP III . n 
I 2 93  ASP 93  93  93  ASP ASP III . n 
I 2 94  ASP 94  94  94  ASP ASP III . n 
I 2 95  SER 95  95  95  SER SER III . n 
I 2 96  LEU 96  96  96  LEU LEU III . n 
I 2 97  LYS 97  97  97  LYS LYS III . n 
I 2 98  GLY 98  98  98  GLY GLY III . n 
I 2 99  TRP 99  99  99  TRP TRP III . n 
I 2 100 VAL 100 100 100 VAL VAL III . n 
I 2 101 PHE 101 101 101 PHE PHE III . n 
I 2 102 GLY 102 102 102 GLY GLY III . n 
I 2 103 GLY 103 103 103 GLY GLY III . n 
I 2 104 GLY 104 104 104 GLY GLY III . n 
I 2 105 THR 105 105 105 THR THR III . n 
I 2 106 LYS 106 106 106 LYS LYS III . n 
I 2 107 LEU 107 107 107 LEU LEU III . n 
I 2 108 THR 108 108 108 THR THR III . n 
I 2 109 VAL 109 109 109 VAL VAL III . n 
I 2 110 LEU 110 110 110 LEU LEU III . n 
I 2 111 GLY 111 111 111 GLY GLY III . n 
I 2 112 ALA 112 112 112 ALA ALA III . n 
I 2 113 PRO 113 113 113 PRO PRO III . n 
I 2 114 LYS 114 114 ?   ?   ?   III . n 
I 2 115 ALA 115 115 ?   ?   ?   III . n 
I 2 116 ASN 116 116 ?   ?   ?   III . n 
I 2 117 PRO 117 117 ?   ?   ?   III . n 
I 2 118 THR 118 118 ?   ?   ?   III . n 
I 2 119 VAL 119 119 ?   ?   ?   III . n 
I 2 120 THR 120 120 ?   ?   ?   III . n 
I 2 121 LEU 121 121 ?   ?   ?   III . n 
I 2 122 PHE 122 122 ?   ?   ?   III . n 
I 2 123 PRO 123 123 ?   ?   ?   III . n 
I 2 124 PRO 124 124 ?   ?   ?   III . n 
I 2 125 SER 125 125 ?   ?   ?   III . n 
I 2 126 SER 126 126 ?   ?   ?   III . n 
I 2 127 GLU 127 127 ?   ?   ?   III . n 
I 2 128 GLU 128 128 ?   ?   ?   III . n 
I 2 129 LEU 129 129 ?   ?   ?   III . n 
I 2 130 GLN 130 130 ?   ?   ?   III . n 
I 2 131 ALA 131 131 ?   ?   ?   III . n 
I 2 132 ASN 132 132 132 ASN ASN III . n 
I 2 133 LYS 133 133 133 LYS LYS III . n 
I 2 134 ALA 134 134 134 ALA ALA III . n 
I 2 135 THR 135 135 135 THR THR III . n 
I 2 136 LEU 136 136 136 LEU LEU III . n 
I 2 137 VAL 137 137 137 VAL VAL III . n 
I 2 138 CYS 138 138 138 CYS CYS III . n 
I 2 139 LEU 139 139 139 LEU LEU III . n 
I 2 140 ILE 140 140 ?   ?   ?   III . n 
I 2 141 SER 141 141 ?   ?   ?   III . n 
I 2 142 ASP 142 142 ?   ?   ?   III . n 
I 2 143 PHE 143 143 ?   ?   ?   III . n 
I 2 144 TYR 144 144 ?   ?   ?   III . n 
I 2 145 PRO 145 145 ?   ?   ?   III . n 
I 2 146 GLY 146 146 ?   ?   ?   III . n 
I 2 147 ALA 147 147 ?   ?   ?   III . n 
I 2 148 VAL 148 148 ?   ?   ?   III . n 
I 2 149 THR 149 149 ?   ?   ?   III . n 
I 2 150 VAL 150 150 ?   ?   ?   III . n 
I 2 151 ALA 151 151 ?   ?   ?   III . n 
I 2 152 TRP 152 152 ?   ?   ?   III . n 
I 2 153 LYS 153 153 ?   ?   ?   III . n 
I 2 154 ALA 154 154 ?   ?   ?   III . n 
I 2 155 ASP 155 155 ?   ?   ?   III . n 
I 2 156 GLY 156 156 ?   ?   ?   III . n 
I 2 157 SER 157 157 ?   ?   ?   III . n 
I 2 158 PRO 158 158 ?   ?   ?   III . n 
I 2 159 VAL 159 159 ?   ?   ?   III . n 
I 2 160 LYS 160 160 ?   ?   ?   III . n 
I 2 161 ALA 161 161 ?   ?   ?   III . n 
I 2 162 GLY 162 162 ?   ?   ?   III . n 
I 2 163 VAL 163 163 163 VAL VAL III . n 
I 2 164 GLU 164 164 164 GLU GLU III . n 
I 2 165 THR 165 165 165 THR THR III . n 
I 2 166 THR 166 166 166 THR THR III . n 
I 2 167 LYS 167 167 167 LYS LYS III . n 
I 2 168 PRO 168 168 168 PRO PRO III . n 
I 2 169 SER 169 169 169 SER SER III . n 
I 2 170 LYS 170 170 ?   ?   ?   III . n 
I 2 171 GLN 171 171 ?   ?   ?   III . n 
I 2 172 SER 172 172 ?   ?   ?   III . n 
I 2 173 ASN 173 173 ?   ?   ?   III . n 
I 2 174 ASN 174 174 ?   ?   ?   III . n 
I 2 175 LYS 175 175 ?   ?   ?   III . n 
I 2 176 THR 176 176 ?   ?   ?   III . n 
I 2 177 ALA 177 177 ?   ?   ?   III . n 
I 2 178 ALA 178 178 178 ALA ALA III . n 
I 2 179 SER 179 179 179 SER SER III . n 
I 2 180 SER 180 180 180 SER SER III . n 
I 2 181 TYR 181 181 181 TYR TYR III . n 
I 2 182 LEU 182 182 182 LEU LEU III . n 
I 2 183 SER 183 183 183 SER SER III . n 
I 2 184 LEU 184 184 184 LEU LEU III . n 
I 2 185 THR 185 185 185 THR THR III . n 
I 2 186 PRO 186 186 186 PRO PRO III . n 
I 2 187 GLU 187 187 ?   ?   ?   III . n 
I 2 188 GLN 188 188 ?   ?   ?   III . n 
I 2 189 TRP 189 189 ?   ?   ?   III . n 
I 2 190 LYS 190 190 ?   ?   ?   III . n 
I 2 191 SER 191 191 ?   ?   ?   III . n 
I 2 192 HIS 192 192 ?   ?   ?   III . n 
I 2 193 ARG 193 193 ?   ?   ?   III . n 
I 2 194 SER 194 194 ?   ?   ?   III . n 
I 2 195 TYR 195 195 ?   ?   ?   III . n 
I 2 196 SER 196 196 ?   ?   ?   III . n 
I 2 197 CYS 197 197 ?   ?   ?   III . n 
I 2 198 GLN 198 198 ?   ?   ?   III . n 
I 2 199 VAL 199 199 ?   ?   ?   III . n 
I 2 200 THR 200 200 ?   ?   ?   III . n 
I 2 201 HIS 201 201 ?   ?   ?   III . n 
I 2 202 GLU 202 202 ?   ?   ?   III . n 
I 2 203 GLY 203 203 ?   ?   ?   III . n 
I 2 204 THR 204 204 ?   ?   ?   III . n 
I 2 205 THR 205 205 ?   ?   ?   III . n 
I 2 206 VAL 206 206 ?   ?   ?   III . n 
I 2 207 GLU 207 207 ?   ?   ?   III . n 
I 2 208 LYS 208 208 ?   ?   ?   III . n 
I 2 209 THR 209 209 ?   ?   ?   III . n 
I 2 210 VAL 210 210 ?   ?   ?   III . n 
I 2 211 ALA 211 211 ?   ?   ?   III . n 
I 2 212 PRO 212 212 ?   ?   ?   III . n 
J 3 1   GLU 1   1   1   GLU GLU JJJ . n 
J 3 2   VAL 2   2   2   VAL VAL JJJ . n 
J 3 3   GLN 3   3   3   GLN GLN JJJ . n 
J 3 4   LEU 4   4   4   LEU LEU JJJ . n 
J 3 5   VAL 5   5   5   VAL VAL JJJ . n 
J 3 6   GLU 6   6   6   GLU GLU JJJ . n 
J 3 7   SER 7   7   7   SER SER JJJ . n 
J 3 8   GLY 8   8   8   GLY GLY JJJ . n 
J 3 9   GLY 9   9   9   GLY GLY JJJ . n 
J 3 10  GLY 10  10  10  GLY GLY JJJ . n 
J 3 11  LEU 11  11  11  LEU LEU JJJ . n 
J 3 12  VAL 12  12  12  VAL VAL JJJ . n 
J 3 13  LYS 13  13  13  LYS LYS JJJ . n 
J 3 14  PRO 14  14  14  PRO PRO JJJ . n 
J 3 15  GLY 15  15  15  GLY GLY JJJ . n 
J 3 16  GLY 16  16  16  GLY GLY JJJ . n 
J 3 17  SER 17  17  17  SER SER JJJ . n 
J 3 18  LEU 18  18  18  LEU LEU JJJ . n 
J 3 19  ARG 19  19  19  ARG ARG JJJ . n 
J 3 20  LEU 20  20  20  LEU LEU JJJ . n 
J 3 21  SER 21  21  21  SER SER JJJ . n 
J 3 22  CYS 22  22  22  CYS CYS JJJ . n 
J 3 23  ALA 23  23  23  ALA ALA JJJ . n 
J 3 24  ALA 24  24  24  ALA ALA JJJ . n 
J 3 25  SER 25  25  25  SER SER JJJ . n 
J 3 26  GLY 26  26  26  GLY GLY JJJ . n 
J 3 27  PHE 27  27  27  PHE PHE JJJ . n 
J 3 28  THR 28  28  28  THR THR JJJ . n 
J 3 29  PHE 29  29  29  PHE PHE JJJ . n 
J 3 30  SER 30  30  30  SER SER JJJ . n 
J 3 31  SER 31  31  31  SER SER JJJ . n 
J 3 32  TYR 32  32  32  TYR TYR JJJ . n 
J 3 33  THR 33  33  33  THR THR JJJ . n 
J 3 34  MET 34  34  34  MET MET JJJ . n 
J 3 35  ASN 35  35  35  ASN ASN JJJ . n 
J 3 36  TRP 36  36  36  TRP TRP JJJ . n 
J 3 37  VAL 37  37  37  VAL VAL JJJ . n 
J 3 38  ARG 38  38  38  ARG ARG JJJ . n 
J 3 39  GLN 39  39  39  GLN GLN JJJ . n 
J 3 40  ALA 40  40  40  ALA ALA JJJ . n 
J 3 41  PRO 41  41  41  PRO PRO JJJ . n 
J 3 42  GLY 42  42  42  GLY GLY JJJ . n 
J 3 43  LYS 43  43  43  LYS LYS JJJ . n 
J 3 44  GLY 44  44  44  GLY GLY JJJ . n 
J 3 45  LEU 45  45  45  LEU LEU JJJ . n 
J 3 46  GLN 46  46  46  GLN GLN JJJ . n 
J 3 47  TRP 47  47  47  TRP TRP JJJ . n 
J 3 48  VAL 48  48  48  VAL VAL JJJ . n 
J 3 49  SER 49  49  49  SER SER JJJ . n 
J 3 50  SER 50  50  50  SER SER JJJ . n 
J 3 51  ILE 51  51  51  ILE ILE JJJ . n 
J 3 52  SER 52  52  52  SER SER JJJ . n 
J 3 53  SER 53  53  53  SER SER JJJ . n 
J 3 54  SER 54  54  54  SER SER JJJ . n 
J 3 55  SER 55  55  55  SER SER JJJ . n 
J 3 56  THR 56  56  56  THR THR JJJ . n 
J 3 57  TYR 57  57  57  TYR TYR JJJ . n 
J 3 58  MET 58  58  58  MET MET JJJ . n 
J 3 59  TYR 59  59  59  TYR TYR JJJ . n 
J 3 60  TYR 60  60  60  TYR TYR JJJ . n 
J 3 61  GLY 61  61  61  GLY GLY JJJ . n 
J 3 62  ASP 62  62  62  ASP ASP JJJ . n 
J 3 63  SER 63  63  63  SER SER JJJ . n 
J 3 64  VAL 64  64  64  VAL VAL JJJ . n 
J 3 65  LYS 65  65  65  LYS LYS JJJ . n 
J 3 66  GLY 66  66  66  GLY GLY JJJ . n 
J 3 67  ARG 67  67  67  ARG ARG JJJ . n 
J 3 68  PHE 68  68  68  PHE PHE JJJ . n 
J 3 69  THR 69  69  69  THR THR JJJ . n 
J 3 70  ILE 70  70  70  ILE ILE JJJ . n 
J 3 71  SER 71  71  71  SER SER JJJ . n 
J 3 72  ARG 72  72  72  ARG ARG JJJ . n 
J 3 73  ASP 73  73  73  ASP ASP JJJ . n 
J 3 74  ASN 74  74  74  ASN ASN JJJ . n 
J 3 75  ALA 75  75  75  ALA ALA JJJ . n 
J 3 76  ARG 76  76  76  ARG ARG JJJ . n 
J 3 77  ASN 77  77  77  ASN ASN JJJ . n 
J 3 78  SER 78  78  78  SER SER JJJ . n 
J 3 79  LEU 79  79  79  LEU LEU JJJ . n 
J 3 80  TYR 80  80  80  TYR TYR JJJ . n 
J 3 81  LEU 81  81  81  LEU LEU JJJ . n 
J 3 82  GLN 82  82  82  GLN GLN JJJ . n 
J 3 83  MET 83  83  83  MET MET JJJ . n 
J 3 84  ASN 84  84  84  ASN ASN JJJ . n 
J 3 85  SER 85  85  85  SER SER JJJ . n 
J 3 86  LEU 86  86  86  LEU LEU JJJ . n 
J 3 87  ARG 87  87  87  ARG ARG JJJ . n 
J 3 88  VAL 88  88  88  VAL VAL JJJ . n 
J 3 89  GLU 89  89  89  GLU GLU JJJ . n 
J 3 90  ASP 90  90  90  ASP ASP JJJ . n 
J 3 91  THR 91  91  91  THR THR JJJ . n 
J 3 92  ALA 92  92  92  ALA ALA JJJ . n 
J 3 93  VAL 93  93  93  VAL VAL JJJ . n 
J 3 94  TYR 94  94  94  TYR TYR JJJ . n 
J 3 95  TYR 95  95  95  TYR TYR JJJ . n 
J 3 96  CYS 96  96  96  CYS CYS JJJ . n 
J 3 97  ALA 97  97  97  ALA ALA JJJ . n 
J 3 98  ARG 98  98  98  ARG ARG JJJ . n 
J 3 99  TYR 99  99  99  TYR TYR JJJ . n 
J 3 100 ALA 100 100 100 ALA ALA JJJ . n 
J 3 101 HIS 101 101 101 HIS HIS JJJ . n 
J 3 102 ASP 102 102 102 ASP ASP JJJ . n 
J 3 103 TRP 103 103 103 TRP TRP JJJ . n 
J 3 104 ASN 104 104 104 ASN ASN JJJ . n 
J 3 105 VAL 105 105 105 VAL VAL JJJ . n 
J 3 106 ASP 106 106 106 ASP ASP JJJ . n 
J 3 107 TYR 107 107 107 TYR TYR JJJ . n 
J 3 108 TRP 108 108 108 TRP TRP JJJ . n 
J 3 109 GLY 109 109 109 GLY GLY JJJ . n 
J 3 110 GLN 110 110 110 GLN GLN JJJ . n 
J 3 111 GLY 111 111 111 GLY GLY JJJ . n 
J 3 112 THR 112 112 112 THR THR JJJ . n 
J 3 113 LEU 113 113 113 LEU LEU JJJ . n 
J 3 114 VAL 114 114 114 VAL VAL JJJ . n 
J 3 115 THR 115 115 115 THR THR JJJ . n 
J 3 116 VAL 116 116 116 VAL VAL JJJ . n 
J 3 117 SER 117 117 117 SER SER JJJ . n 
J 3 118 SER 118 118 118 SER SER JJJ . n 
J 3 119 ALA 119 119 119 ALA ALA JJJ . n 
J 3 120 SER 120 120 120 SER SER JJJ . n 
J 3 121 THR 121 121 121 THR THR JJJ . n 
J 3 122 LYS 122 122 122 LYS LYS JJJ . n 
J 3 123 GLY 123 123 123 GLY GLY JJJ . n 
J 3 124 PRO 124 124 124 PRO PRO JJJ . n 
J 3 125 SER 125 125 125 SER SER JJJ . n 
J 3 126 VAL 126 126 126 VAL VAL JJJ . n 
J 3 127 PHE 127 127 127 PHE PHE JJJ . n 
J 3 128 PRO 128 133 ?   ?   ?   JJJ . n 
J 3 129 LEU 129 134 ?   ?   ?   JJJ . n 
J 3 130 ALA 130 135 ?   ?   ?   JJJ . n 
J 3 131 PRO 131 136 ?   ?   ?   JJJ . n 
J 3 132 SER 132 137 ?   ?   ?   JJJ . n 
J 3 133 SER 133 138 ?   ?   ?   JJJ . n 
J 3 134 LYS 134 139 ?   ?   ?   JJJ . n 
J 3 135 SER 135 140 ?   ?   ?   JJJ . n 
J 3 136 THR 136 141 ?   ?   ?   JJJ . n 
J 3 137 SER 137 142 ?   ?   ?   JJJ . n 
J 3 138 GLY 138 143 ?   ?   ?   JJJ . n 
J 3 139 GLY 139 144 ?   ?   ?   JJJ . n 
J 3 140 THR 140 145 ?   ?   ?   JJJ . n 
J 3 141 ALA 141 146 ?   ?   ?   JJJ . n 
J 3 142 ALA 142 147 147 ALA ALA JJJ . n 
J 3 143 LEU 143 148 148 LEU LEU JJJ . n 
J 3 144 GLY 144 149 149 GLY GLY JJJ . n 
J 3 145 CYS 145 150 150 CYS CYS JJJ . n 
J 3 146 LEU 146 151 151 LEU LEU JJJ . n 
J 3 147 VAL 147 152 152 VAL VAL JJJ . n 
J 3 148 LYS 148 153 153 LYS LYS JJJ . n 
J 3 149 ASP 149 154 154 ASP ASP JJJ . n 
J 3 150 TYR 150 155 155 TYR TYR JJJ . n 
J 3 151 PHE 151 156 156 PHE PHE JJJ . n 
J 3 152 PRO 152 157 157 PRO PRO JJJ . n 
J 3 153 GLU 153 158 158 GLU GLU JJJ . n 
J 3 154 PRO 154 159 159 PRO PRO JJJ . n 
J 3 155 VAL 155 160 160 VAL VAL JJJ . n 
J 3 156 THR 156 161 161 THR THR JJJ . n 
J 3 157 VAL 157 162 162 VAL VAL JJJ . n 
J 3 158 SER 158 163 163 SER SER JJJ . n 
J 3 159 TRP 159 164 164 TRP TRP JJJ . n 
J 3 160 ASN 160 165 165 ASN ASN JJJ . n 
J 3 161 SER 161 166 ?   ?   ?   JJJ . n 
J 3 162 GLY 162 167 ?   ?   ?   JJJ . n 
J 3 163 ALA 163 168 ?   ?   ?   JJJ . n 
J 3 164 LEU 164 169 ?   ?   ?   JJJ . n 
J 3 165 THR 165 170 ?   ?   ?   JJJ . n 
J 3 166 SER 166 171 ?   ?   ?   JJJ . n 
J 3 167 GLY 167 172 ?   ?   ?   JJJ . n 
J 3 168 VAL 168 173 ?   ?   ?   JJJ . n 
J 3 169 HIS 169 174 ?   ?   ?   JJJ . n 
J 3 170 THR 170 175 175 THR THR JJJ . n 
J 3 171 PHE 171 176 176 PHE PHE JJJ . n 
J 3 172 PRO 172 177 177 PRO PRO JJJ . n 
J 3 173 ALA 173 178 178 ALA ALA JJJ . n 
J 3 174 VAL 174 179 179 VAL VAL JJJ . n 
J 3 175 LEU 175 180 180 LEU LEU JJJ . n 
J 3 176 GLN 176 181 181 GLN GLN JJJ . n 
J 3 177 SER 177 182 182 SER SER JJJ . n 
J 3 178 SER 178 183 183 SER SER JJJ . n 
J 3 179 GLY 179 184 184 GLY GLY JJJ . n 
J 3 180 LEU 180 185 185 LEU LEU JJJ . n 
J 3 181 TYR 181 186 186 TYR TYR JJJ . n 
J 3 182 SER 182 187 187 SER SER JJJ . n 
J 3 183 LEU 183 188 188 LEU LEU JJJ . n 
J 3 184 SER 184 189 189 SER SER JJJ . n 
J 3 185 SER 185 190 190 SER SER JJJ . n 
J 3 186 VAL 186 191 191 VAL VAL JJJ . n 
J 3 187 VAL 187 192 ?   ?   ?   JJJ . n 
J 3 188 THR 188 193 ?   ?   ?   JJJ . n 
J 3 189 VAL 189 194 ?   ?   ?   JJJ . n 
J 3 190 PRO 190 195 ?   ?   ?   JJJ . n 
J 3 191 SER 191 196 ?   ?   ?   JJJ . n 
J 3 192 SER 192 197 ?   ?   ?   JJJ . n 
J 3 193 SER 193 198 ?   ?   ?   JJJ . n 
J 3 194 LEU 194 199 ?   ?   ?   JJJ . n 
J 3 195 GLY 195 200 ?   ?   ?   JJJ . n 
J 3 196 THR 196 201 ?   ?   ?   JJJ . n 
J 3 197 GLN 197 202 ?   ?   ?   JJJ . n 
J 3 198 THR 198 203 ?   ?   ?   JJJ . n 
J 3 199 TYR 199 204 ?   ?   ?   JJJ . n 
J 3 200 ILE 200 205 ?   ?   ?   JJJ . n 
J 3 201 CYS 201 206 206 CYS CYS JJJ . n 
J 3 202 ASN 202 207 207 ASN ASN JJJ . n 
J 3 203 VAL 203 208 208 VAL VAL JJJ . n 
J 3 204 ASN 204 209 209 ASN ASN JJJ . n 
J 3 205 HIS 205 210 210 HIS HIS JJJ . n 
J 3 206 LYS 206 211 211 LYS LYS JJJ . n 
J 3 207 PRO 207 212 212 PRO PRO JJJ . n 
J 3 208 SER 208 213 213 SER SER JJJ . n 
J 3 209 ASN 209 214 214 ASN ASN JJJ . n 
J 3 210 THR 210 215 215 THR THR JJJ . n 
J 3 211 LYS 211 216 216 LYS LYS JJJ . n 
J 3 212 VAL 212 217 217 VAL VAL JJJ . n 
J 3 213 ASP 213 218 218 ASP ASP JJJ . n 
J 3 214 LYS 214 219 219 LYS LYS JJJ . n 
J 3 215 LYS 215 220 ?   ?   ?   JJJ . n 
J 3 216 VAL 216 221 ?   ?   ?   JJJ . n 
J 3 217 GLU 217 222 ?   ?   ?   JJJ . n 
J 3 218 PRO 218 223 ?   ?   ?   JJJ . n 
J 3 219 LYS 219 224 ?   ?   ?   JJJ . n 
J 3 220 SER 220 225 ?   ?   ?   JJJ . n 
J 3 221 CYS 221 226 ?   ?   ?   JJJ . n 
J 3 222 ASP 222 227 ?   ?   ?   JJJ . n 
J 3 223 LYS 223 228 ?   ?   ?   JJJ . n 
J 3 224 THR 224 229 ?   ?   ?   JJJ . n 
J 3 225 HIS 225 230 ?   ?   ?   JJJ . n 
J 3 226 THR 226 231 ?   ?   ?   JJJ . n 
J 3 227 CYS 227 232 ?   ?   ?   JJJ . n 
J 3 228 PRO 228 233 ?   ?   ?   JJJ . n 
J 3 229 PRO 229 234 ?   ?   ?   JJJ . n 
J 3 230 CYS 230 235 ?   ?   ?   JJJ . n 
J 3 231 PRO 231 236 ?   ?   ?   JJJ . n 
J 3 232 ALA 232 237 ?   ?   ?   JJJ . n 
J 3 233 PRO 233 238 ?   ?   ?   JJJ . n 
J 3 234 GLU 234 239 ?   ?   ?   JJJ . n 
J 3 235 LEU 235 240 ?   ?   ?   JJJ . n 
J 3 236 LEU 236 241 ?   ?   ?   JJJ . n 
J 3 237 GLY 237 242 ?   ?   ?   JJJ . n 
J 3 238 GLY 238 243 ?   ?   ?   JJJ . n 
J 3 239 PRO 239 244 ?   ?   ?   JJJ . n 
J 3 240 SER 240 245 ?   ?   ?   JJJ . n 
J 3 241 VAL 241 246 ?   ?   ?   JJJ . n 
J 3 242 PHE 242 247 ?   ?   ?   JJJ . n 
J 3 243 LEU 243 248 ?   ?   ?   JJJ . n 
J 3 244 PHE 244 249 ?   ?   ?   JJJ . n 
J 3 245 PRO 245 250 ?   ?   ?   JJJ . n 
J 3 246 PRO 246 251 ?   ?   ?   JJJ . n 
J 3 247 LYS 247 252 ?   ?   ?   JJJ . n 
J 3 248 PRO 248 253 ?   ?   ?   JJJ . n 
J 3 249 LYS 249 254 ?   ?   ?   JJJ . n 
J 3 250 ASP 250 255 ?   ?   ?   JJJ . n 
J 3 251 THR 251 256 ?   ?   ?   JJJ . n 
J 3 252 LEU 252 257 ?   ?   ?   JJJ . n 
J 3 253 MET 253 258 ?   ?   ?   JJJ . n 
J 3 254 ILE 254 259 ?   ?   ?   JJJ . n 
J 3 255 SER 255 260 ?   ?   ?   JJJ . n 
J 3 256 ARG 256 261 ?   ?   ?   JJJ . n 
J 3 257 THR 257 262 ?   ?   ?   JJJ . n 
J 3 258 PRO 258 263 ?   ?   ?   JJJ . n 
J 3 259 GLU 259 264 ?   ?   ?   JJJ . n 
J 3 260 VAL 260 265 ?   ?   ?   JJJ . n 
J 3 261 THR 261 266 ?   ?   ?   JJJ . n 
J 3 262 CYS 262 267 ?   ?   ?   JJJ . n 
J 3 263 VAL 263 268 ?   ?   ?   JJJ . n 
J 3 264 VAL 264 269 ?   ?   ?   JJJ . n 
J 3 265 VAL 265 270 ?   ?   ?   JJJ . n 
J 3 266 ASP 266 271 ?   ?   ?   JJJ . n 
J 3 267 VAL 267 272 ?   ?   ?   JJJ . n 
J 3 268 SER 268 273 ?   ?   ?   JJJ . n 
J 3 269 HIS 269 274 ?   ?   ?   JJJ . n 
J 3 270 GLU 270 275 ?   ?   ?   JJJ . n 
J 3 271 ASP 271 276 ?   ?   ?   JJJ . n 
J 3 272 PRO 272 277 ?   ?   ?   JJJ . n 
J 3 273 GLU 273 278 ?   ?   ?   JJJ . n 
J 3 274 VAL 274 279 ?   ?   ?   JJJ . n 
J 3 275 LYS 275 280 ?   ?   ?   JJJ . n 
J 3 276 PHE 276 281 ?   ?   ?   JJJ . n 
J 3 277 ASN 277 282 ?   ?   ?   JJJ . n 
J 3 278 TRP 278 283 ?   ?   ?   JJJ . n 
J 3 279 TYR 279 284 ?   ?   ?   JJJ . n 
J 3 280 VAL 280 285 ?   ?   ?   JJJ . n 
J 3 281 ASP 281 286 ?   ?   ?   JJJ . n 
J 3 282 GLY 282 287 ?   ?   ?   JJJ . n 
J 3 283 VAL 283 288 ?   ?   ?   JJJ . n 
J 3 284 GLU 284 289 ?   ?   ?   JJJ . n 
J 3 285 VAL 285 290 ?   ?   ?   JJJ . n 
J 3 286 HIS 286 291 ?   ?   ?   JJJ . n 
J 3 287 ASN 287 292 ?   ?   ?   JJJ . n 
J 3 288 ALA 288 293 ?   ?   ?   JJJ . n 
J 3 289 LYS 289 294 ?   ?   ?   JJJ . n 
J 3 290 THR 290 295 ?   ?   ?   JJJ . n 
J 3 291 LYS 291 296 ?   ?   ?   JJJ . n 
J 3 292 PRO 292 297 ?   ?   ?   JJJ . n 
J 3 293 ARG 293 298 ?   ?   ?   JJJ . n 
J 3 294 GLU 294 299 ?   ?   ?   JJJ . n 
J 3 295 GLU 295 300 ?   ?   ?   JJJ . n 
J 3 296 GLN 296 301 ?   ?   ?   JJJ . n 
J 3 297 TYR 297 302 ?   ?   ?   JJJ . n 
J 3 298 ASN 298 303 ?   ?   ?   JJJ . n 
J 3 299 SER 299 304 ?   ?   ?   JJJ . n 
J 3 300 THR 300 305 ?   ?   ?   JJJ . n 
J 3 301 TYR 301 306 ?   ?   ?   JJJ . n 
J 3 302 ARG 302 307 ?   ?   ?   JJJ . n 
J 3 303 VAL 303 308 ?   ?   ?   JJJ . n 
J 3 304 VAL 304 309 ?   ?   ?   JJJ . n 
J 3 305 SER 305 310 ?   ?   ?   JJJ . n 
J 3 306 VAL 306 311 ?   ?   ?   JJJ . n 
J 3 307 LEU 307 312 ?   ?   ?   JJJ . n 
J 3 308 THR 308 313 ?   ?   ?   JJJ . n 
J 3 309 VAL 309 314 ?   ?   ?   JJJ . n 
J 3 310 LEU 310 315 ?   ?   ?   JJJ . n 
J 3 311 HIS 311 316 ?   ?   ?   JJJ . n 
J 3 312 GLN 312 317 ?   ?   ?   JJJ . n 
J 3 313 ASP 313 318 ?   ?   ?   JJJ . n 
J 3 314 TRP 314 319 ?   ?   ?   JJJ . n 
J 3 315 LEU 315 320 ?   ?   ?   JJJ . n 
J 3 316 ASN 316 321 ?   ?   ?   JJJ . n 
J 3 317 GLY 317 322 ?   ?   ?   JJJ . n 
J 3 318 LYS 318 323 ?   ?   ?   JJJ . n 
J 3 319 GLU 319 324 ?   ?   ?   JJJ . n 
J 3 320 TYR 320 325 ?   ?   ?   JJJ . n 
J 3 321 LYS 321 326 ?   ?   ?   JJJ . n 
J 3 322 CYS 322 327 ?   ?   ?   JJJ . n 
J 3 323 LYS 323 328 ?   ?   ?   JJJ . n 
J 3 324 VAL 324 329 ?   ?   ?   JJJ . n 
J 3 325 SER 325 330 ?   ?   ?   JJJ . n 
J 3 326 ASN 326 331 ?   ?   ?   JJJ . n 
J 3 327 LYS 327 332 ?   ?   ?   JJJ . n 
J 3 328 ALA 328 333 ?   ?   ?   JJJ . n 
J 3 329 LEU 329 334 ?   ?   ?   JJJ . n 
J 3 330 PRO 330 335 ?   ?   ?   JJJ . n 
J 3 331 ALA 331 336 ?   ?   ?   JJJ . n 
J 3 332 PRO 332 337 ?   ?   ?   JJJ . n 
J 3 333 ILE 333 338 ?   ?   ?   JJJ . n 
J 3 334 GLU 334 339 ?   ?   ?   JJJ . n 
J 3 335 LYS 335 340 ?   ?   ?   JJJ . n 
J 3 336 THR 336 341 ?   ?   ?   JJJ . n 
J 3 337 ILE 337 342 ?   ?   ?   JJJ . n 
J 3 338 SER 338 343 ?   ?   ?   JJJ . n 
J 3 339 LYS 339 344 ?   ?   ?   JJJ . n 
J 3 340 ALA 340 345 ?   ?   ?   JJJ . n 
J 3 341 LYS 341 346 ?   ?   ?   JJJ . n 
J 3 342 GLY 342 347 ?   ?   ?   JJJ . n 
J 3 343 GLN 343 348 ?   ?   ?   JJJ . n 
J 3 344 PRO 344 349 ?   ?   ?   JJJ . n 
J 3 345 ARG 345 350 ?   ?   ?   JJJ . n 
J 3 346 GLU 346 351 ?   ?   ?   JJJ . n 
J 3 347 PRO 347 352 ?   ?   ?   JJJ . n 
J 3 348 GLN 348 353 ?   ?   ?   JJJ . n 
J 3 349 VAL 349 354 ?   ?   ?   JJJ . n 
J 3 350 TYR 350 355 ?   ?   ?   JJJ . n 
J 3 351 THR 351 356 ?   ?   ?   JJJ . n 
J 3 352 LEU 352 357 ?   ?   ?   JJJ . n 
J 3 353 PRO 353 358 ?   ?   ?   JJJ . n 
J 3 354 PRO 354 359 ?   ?   ?   JJJ . n 
J 3 355 SER 355 360 ?   ?   ?   JJJ . n 
J 3 356 ARG 356 361 ?   ?   ?   JJJ . n 
J 3 357 ASP 357 362 ?   ?   ?   JJJ . n 
J 3 358 GLU 358 363 ?   ?   ?   JJJ . n 
J 3 359 LEU 359 364 ?   ?   ?   JJJ . n 
J 3 360 THR 360 365 ?   ?   ?   JJJ . n 
J 3 361 LYS 361 366 ?   ?   ?   JJJ . n 
J 3 362 ASN 362 367 ?   ?   ?   JJJ . n 
J 3 363 GLN 363 368 ?   ?   ?   JJJ . n 
J 3 364 VAL 364 369 ?   ?   ?   JJJ . n 
J 3 365 SER 365 370 ?   ?   ?   JJJ . n 
J 3 366 LEU 366 371 ?   ?   ?   JJJ . n 
J 3 367 THR 367 372 ?   ?   ?   JJJ . n 
J 3 368 CYS 368 373 ?   ?   ?   JJJ . n 
J 3 369 LEU 369 374 ?   ?   ?   JJJ . n 
J 3 370 VAL 370 375 ?   ?   ?   JJJ . n 
J 3 371 LYS 371 376 ?   ?   ?   JJJ . n 
J 3 372 GLY 372 377 ?   ?   ?   JJJ . n 
J 3 373 PHE 373 378 ?   ?   ?   JJJ . n 
J 3 374 TYR 374 379 ?   ?   ?   JJJ . n 
J 3 375 PRO 375 380 ?   ?   ?   JJJ . n 
J 3 376 SER 376 381 ?   ?   ?   JJJ . n 
J 3 377 ASP 377 382 ?   ?   ?   JJJ . n 
J 3 378 ILE 378 383 ?   ?   ?   JJJ . n 
J 3 379 ALA 379 384 ?   ?   ?   JJJ . n 
J 3 380 VAL 380 385 ?   ?   ?   JJJ . n 
J 3 381 GLU 381 386 ?   ?   ?   JJJ . n 
J 3 382 TRP 382 387 ?   ?   ?   JJJ . n 
J 3 383 GLU 383 388 ?   ?   ?   JJJ . n 
J 3 384 SER 384 389 ?   ?   ?   JJJ . n 
J 3 385 ASN 385 390 ?   ?   ?   JJJ . n 
J 3 386 GLY 386 391 ?   ?   ?   JJJ . n 
J 3 387 GLN 387 392 ?   ?   ?   JJJ . n 
J 3 388 PRO 388 393 ?   ?   ?   JJJ . n 
J 3 389 GLU 389 394 ?   ?   ?   JJJ . n 
J 3 390 ASN 390 395 ?   ?   ?   JJJ . n 
J 3 391 ASN 391 396 ?   ?   ?   JJJ . n 
J 3 392 TYR 392 397 ?   ?   ?   JJJ . n 
J 3 393 LYS 393 398 ?   ?   ?   JJJ . n 
J 3 394 THR 394 399 ?   ?   ?   JJJ . n 
J 3 395 THR 395 400 ?   ?   ?   JJJ . n 
J 3 396 PRO 396 401 ?   ?   ?   JJJ . n 
J 3 397 PRO 397 402 ?   ?   ?   JJJ . n 
J 3 398 VAL 398 403 ?   ?   ?   JJJ . n 
K 2 1   GLN 1   1   ?   ?   ?   KKK . n 
K 2 2   SER 2   2   2   SER SER KKK . n 
K 2 3   VAL 3   3   3   VAL VAL KKK . n 
K 2 4   LEU 4   4   4   LEU LEU KKK . n 
K 2 5   THR 5   5   5   THR THR KKK . n 
K 2 6   GLN 6   6   6   GLN GLN KKK . n 
K 2 7   PRO 7   7   7   PRO PRO KKK . n 
K 2 8   PRO 8   8   8   PRO PRO KKK . n 
K 2 9   SER 9   9   9   SER SER KKK . n 
K 2 10  ALA 10  10  10  ALA ALA KKK . n 
K 2 11  SER 11  11  11  SER SER KKK . n 
K 2 12  GLY 12  12  12  GLY GLY KKK . n 
K 2 13  THR 13  13  13  THR THR KKK . n 
K 2 14  PRO 14  14  14  PRO PRO KKK . n 
K 2 15  GLY 15  15  15  GLY GLY KKK . n 
K 2 16  GLN 16  16  16  GLN GLN KKK . n 
K 2 17  ARG 17  17  17  ARG ARG KKK . n 
K 2 18  VAL 18  18  18  VAL VAL KKK . n 
K 2 19  THR 19  19  19  THR THR KKK . n 
K 2 20  ILE 20  20  20  ILE ILE KKK . n 
K 2 21  SER 21  21  21  SER SER KKK . n 
K 2 22  CYS 22  22  22  CYS CYS KKK . n 
K 2 23  SER 23  23  23  SER SER KKK . n 
K 2 24  GLY 24  24  24  GLY GLY KKK . n 
K 2 25  GLY 25  25  25  GLY GLY KKK . n 
K 2 26  SER 26  26  26  SER SER KKK . n 
K 2 27  SER 27  27  27  SER SER KKK . n 
K 2 28  ASN 28  28  28  ASN ASN KKK . n 
K 2 29  ILE 29  29  29  ILE ILE KKK . n 
K 2 30  GLY 30  30  30  GLY GLY KKK . n 
K 2 31  SER 31  31  31  SER SER KKK . n 
K 2 32  ASN 32  32  32  ASN ASN KKK . n 
K 2 33  PRO 33  33  33  PRO PRO KKK . n 
K 2 34  VAL 34  34  34  VAL VAL KKK . n 
K 2 35  ASN 35  35  35  ASN ASN KKK . n 
K 2 36  TRP 36  36  36  TRP TRP KKK . n 
K 2 37  PHE 37  37  37  PHE PHE KKK . n 
K 2 38  GLN 38  38  38  GLN GLN KKK . n 
K 2 39  GLN 39  39  39  GLN GLN KKK . n 
K 2 40  PHE 40  40  40  PHE PHE KKK . n 
K 2 41  PRO 41  41  41  PRO PRO KKK . n 
K 2 42  GLY 42  42  42  GLY GLY KKK . n 
K 2 43  THR 43  43  43  THR THR KKK . n 
K 2 44  ALA 44  44  44  ALA ALA KKK . n 
K 2 45  PRO 45  45  45  PRO PRO KKK . n 
K 2 46  LYS 46  46  46  LYS LYS KKK . n 
K 2 47  LEU 47  47  47  LEU LEU KKK . n 
K 2 48  LEU 48  48  48  LEU LEU KKK . n 
K 2 49  ILE 49  49  49  ILE ILE KKK . n 
K 2 50  TYR 50  50  50  TYR TYR KKK . n 
K 2 51  ALA 51  51  51  ALA ALA KKK . n 
K 2 52  ASN 52  52  52  ASN ASN KKK . n 
K 2 53  THR 53  53  53  THR THR KKK . n 
K 2 54  GLN 54  54  54  GLN GLN KKK . n 
K 2 55  ARG 55  55  55  ARG ARG KKK . n 
K 2 56  PRO 56  56  56  PRO PRO KKK . n 
K 2 57  SER 57  57  57  SER SER KKK . n 
K 2 58  GLY 58  58  58  GLY GLY KKK . n 
K 2 59  VAL 59  59  59  VAL VAL KKK . n 
K 2 60  PRO 60  60  60  PRO PRO KKK . n 
K 2 61  ASP 61  61  61  ASP ASP KKK . n 
K 2 62  ARG 62  62  62  ARG ARG KKK . n 
K 2 63  PHE 63  63  63  PHE PHE KKK . n 
K 2 64  SER 64  64  64  SER SER KKK . n 
K 2 65  GLY 65  65  65  GLY GLY KKK . n 
K 2 66  SER 66  66  66  SER SER KKK . n 
K 2 67  LYS 67  67  67  LYS LYS KKK . n 
K 2 68  SER 68  68  68  SER SER KKK . n 
K 2 69  GLY 69  69  69  GLY GLY KKK . n 
K 2 70  THR 70  70  70  THR THR KKK . n 
K 2 71  SER 71  71  71  SER SER KKK . n 
K 2 72  VAL 72  72  72  VAL VAL KKK . n 
K 2 73  SER 73  73  73  SER SER KKK . n 
K 2 74  LEU 74  74  74  LEU LEU KKK . n 
K 2 75  ALA 75  75  75  ALA ALA KKK . n 
K 2 76  ILE 76  76  76  ILE ILE KKK . n 
K 2 77  SER 77  77  77  SER SER KKK . n 
K 2 78  GLY 78  78  78  GLY GLY KKK . n 
K 2 79  LEU 79  79  79  LEU LEU KKK . n 
K 2 80  GLN 80  80  80  GLN GLN KKK . n 
K 2 81  SER 81  81  81  SER SER KKK . n 
K 2 82  GLU 82  82  82  GLU GLU KKK . n 
K 2 83  ASP 83  83  83  ASP ASP KKK . n 
K 2 84  GLU 84  84  84  GLU GLU KKK . n 
K 2 85  GLY 85  85  85  GLY GLY KKK . n 
K 2 86  ASP 86  86  86  ASP ASP KKK . n 
K 2 87  TYR 87  87  87  TYR TYR KKK . n 
K 2 88  HIS 88  88  88  HIS HIS KKK . n 
K 2 89  CYS 89  89  89  CYS CYS KKK . n 
K 2 90  ALA 90  90  90  ALA ALA KKK . n 
K 2 91  ALA 91  91  91  ALA ALA KKK . n 
K 2 92  TRP 92  92  92  TRP TRP KKK . n 
K 2 93  ASP 93  93  93  ASP ASP KKK . n 
K 2 94  ASP 94  94  94  ASP ASP KKK . n 
K 2 95  SER 95  95  95  SER SER KKK . n 
K 2 96  LEU 96  96  96  LEU LEU KKK . n 
K 2 97  LYS 97  97  97  LYS LYS KKK . n 
K 2 98  GLY 98  98  98  GLY GLY KKK . n 
K 2 99  TRP 99  99  99  TRP TRP KKK . n 
K 2 100 VAL 100 100 100 VAL VAL KKK . n 
K 2 101 PHE 101 101 101 PHE PHE KKK . n 
K 2 102 GLY 102 102 102 GLY GLY KKK . n 
K 2 103 GLY 103 103 103 GLY GLY KKK . n 
K 2 104 GLY 104 104 104 GLY GLY KKK . n 
K 2 105 THR 105 105 105 THR THR KKK . n 
K 2 106 LYS 106 106 106 LYS LYS KKK . n 
K 2 107 LEU 107 107 107 LEU LEU KKK . n 
K 2 108 THR 108 108 108 THR THR KKK . n 
K 2 109 VAL 109 109 109 VAL VAL KKK . n 
K 2 110 LEU 110 110 110 LEU LEU KKK . n 
K 2 111 GLY 111 111 111 GLY GLY KKK . n 
K 2 112 ALA 112 112 112 ALA ALA KKK . n 
K 2 113 PRO 113 113 113 PRO PRO KKK . n 
K 2 114 LYS 114 114 ?   ?   ?   KKK . n 
K 2 115 ALA 115 115 ?   ?   ?   KKK . n 
K 2 116 ASN 116 116 ?   ?   ?   KKK . n 
K 2 117 PRO 117 117 ?   ?   ?   KKK . n 
K 2 118 THR 118 118 ?   ?   ?   KKK . n 
K 2 119 VAL 119 119 ?   ?   ?   KKK . n 
K 2 120 THR 120 120 ?   ?   ?   KKK . n 
K 2 121 LEU 121 121 ?   ?   ?   KKK . n 
K 2 122 PHE 122 122 ?   ?   ?   KKK . n 
K 2 123 PRO 123 123 ?   ?   ?   KKK . n 
K 2 124 PRO 124 124 ?   ?   ?   KKK . n 
K 2 125 SER 125 125 ?   ?   ?   KKK . n 
K 2 126 SER 126 126 ?   ?   ?   KKK . n 
K 2 127 GLU 127 127 ?   ?   ?   KKK . n 
K 2 128 GLU 128 128 ?   ?   ?   KKK . n 
K 2 129 LEU 129 129 ?   ?   ?   KKK . n 
K 2 130 GLN 130 130 ?   ?   ?   KKK . n 
K 2 131 ALA 131 131 ?   ?   ?   KKK . n 
K 2 132 ASN 132 132 ?   ?   ?   KKK . n 
K 2 133 LYS 133 133 ?   ?   ?   KKK . n 
K 2 134 ALA 134 134 ?   ?   ?   KKK . n 
K 2 135 THR 135 135 ?   ?   ?   KKK . n 
K 2 136 LEU 136 136 ?   ?   ?   KKK . n 
K 2 137 VAL 137 137 ?   ?   ?   KKK . n 
K 2 138 CYS 138 138 ?   ?   ?   KKK . n 
K 2 139 LEU 139 139 139 LEU LEU KKK . n 
K 2 140 ILE 140 140 140 ILE ILE KKK . n 
K 2 141 SER 141 141 141 SER SER KKK . n 
K 2 142 ASP 142 142 142 ASP ASP KKK . n 
K 2 143 PHE 143 143 143 PHE PHE KKK . n 
K 2 144 TYR 144 144 144 TYR TYR KKK . n 
K 2 145 PRO 145 145 145 PRO PRO KKK . n 
K 2 146 GLY 146 146 146 GLY GLY KKK . n 
K 2 147 ALA 147 147 147 ALA ALA KKK . n 
K 2 148 VAL 148 148 148 VAL VAL KKK . n 
K 2 149 THR 149 149 ?   ?   ?   KKK . n 
K 2 150 VAL 150 150 ?   ?   ?   KKK . n 
K 2 151 ALA 151 151 ?   ?   ?   KKK . n 
K 2 152 TRP 152 152 ?   ?   ?   KKK . n 
K 2 153 LYS 153 153 ?   ?   ?   KKK . n 
K 2 154 ALA 154 154 ?   ?   ?   KKK . n 
K 2 155 ASP 155 155 ?   ?   ?   KKK . n 
K 2 156 GLY 156 156 ?   ?   ?   KKK . n 
K 2 157 SER 157 157 ?   ?   ?   KKK . n 
K 2 158 PRO 158 158 ?   ?   ?   KKK . n 
K 2 159 VAL 159 159 ?   ?   ?   KKK . n 
K 2 160 LYS 160 160 ?   ?   ?   KKK . n 
K 2 161 ALA 161 161 ?   ?   ?   KKK . n 
K 2 162 GLY 162 162 ?   ?   ?   KKK . n 
K 2 163 VAL 163 163 ?   ?   ?   KKK . n 
K 2 164 GLU 164 164 ?   ?   ?   KKK . n 
K 2 165 THR 165 165 165 THR THR KKK . n 
K 2 166 THR 166 166 166 THR THR KKK . n 
K 2 167 LYS 167 167 167 LYS LYS KKK . n 
K 2 168 PRO 168 168 168 PRO PRO KKK . n 
K 2 169 SER 169 169 169 SER SER KKK . n 
K 2 170 LYS 170 170 170 LYS LYS KKK . n 
K 2 171 GLN 171 171 ?   ?   ?   KKK . n 
K 2 172 SER 172 172 ?   ?   ?   KKK . n 
K 2 173 ASN 173 173 ?   ?   ?   KKK . n 
K 2 174 ASN 174 174 ?   ?   ?   KKK . n 
K 2 175 LYS 175 175 ?   ?   ?   KKK . n 
K 2 176 THR 176 176 ?   ?   ?   KKK . n 
K 2 177 ALA 177 177 177 ALA ALA KKK . n 
K 2 178 ALA 178 178 178 ALA ALA KKK . n 
K 2 179 SER 179 179 179 SER SER KKK . n 
K 2 180 SER 180 180 180 SER SER KKK . n 
K 2 181 TYR 181 181 181 TYR TYR KKK . n 
K 2 182 LEU 182 182 182 LEU LEU KKK . n 
K 2 183 SER 183 183 ?   ?   ?   KKK . n 
K 2 184 LEU 184 184 ?   ?   ?   KKK . n 
K 2 185 THR 185 185 ?   ?   ?   KKK . n 
K 2 186 PRO 186 186 ?   ?   ?   KKK . n 
K 2 187 GLU 187 187 ?   ?   ?   KKK . n 
K 2 188 GLN 188 188 ?   ?   ?   KKK . n 
K 2 189 TRP 189 189 ?   ?   ?   KKK . n 
K 2 190 LYS 190 190 ?   ?   ?   KKK . n 
K 2 191 SER 191 191 ?   ?   ?   KKK . n 
K 2 192 HIS 192 192 ?   ?   ?   KKK . n 
K 2 193 ARG 193 193 ?   ?   ?   KKK . n 
K 2 194 SER 194 194 ?   ?   ?   KKK . n 
K 2 195 TYR 195 195 ?   ?   ?   KKK . n 
K 2 196 SER 196 196 ?   ?   ?   KKK . n 
K 2 197 CYS 197 197 ?   ?   ?   KKK . n 
K 2 198 GLN 198 198 ?   ?   ?   KKK . n 
K 2 199 VAL 199 199 ?   ?   ?   KKK . n 
K 2 200 THR 200 200 ?   ?   ?   KKK . n 
K 2 201 HIS 201 201 ?   ?   ?   KKK . n 
K 2 202 GLU 202 202 ?   ?   ?   KKK . n 
K 2 203 GLY 203 203 ?   ?   ?   KKK . n 
K 2 204 THR 204 204 ?   ?   ?   KKK . n 
K 2 205 THR 205 205 ?   ?   ?   KKK . n 
K 2 206 VAL 206 206 ?   ?   ?   KKK . n 
K 2 207 GLU 207 207 ?   ?   ?   KKK . n 
K 2 208 LYS 208 208 ?   ?   ?   KKK . n 
K 2 209 THR 209 209 ?   ?   ?   KKK . n 
K 2 210 VAL 210 210 ?   ?   ?   KKK . n 
K 2 211 ALA 211 211 ?   ?   ?   KKK . n 
K 2 212 PRO 212 212 ?   ?   ?   KKK . n 
L 3 1   GLU 1   1   1   GLU GLU LLL . n 
L 3 2   VAL 2   2   2   VAL VAL LLL . n 
L 3 3   GLN 3   3   3   GLN GLN LLL . n 
L 3 4   LEU 4   4   4   LEU LEU LLL . n 
L 3 5   VAL 5   5   5   VAL VAL LLL . n 
L 3 6   GLU 6   6   6   GLU GLU LLL . n 
L 3 7   SER 7   7   7   SER SER LLL . n 
L 3 8   GLY 8   8   8   GLY GLY LLL . n 
L 3 9   GLY 9   9   9   GLY GLY LLL . n 
L 3 10  GLY 10  10  10  GLY GLY LLL . n 
L 3 11  LEU 11  11  11  LEU LEU LLL . n 
L 3 12  VAL 12  12  12  VAL VAL LLL . n 
L 3 13  LYS 13  13  13  LYS LYS LLL . n 
L 3 14  PRO 14  14  14  PRO PRO LLL . n 
L 3 15  GLY 15  15  15  GLY GLY LLL . n 
L 3 16  GLY 16  16  16  GLY GLY LLL . n 
L 3 17  SER 17  17  17  SER SER LLL . n 
L 3 18  LEU 18  18  18  LEU LEU LLL . n 
L 3 19  ARG 19  19  19  ARG ARG LLL . n 
L 3 20  LEU 20  20  20  LEU LEU LLL . n 
L 3 21  SER 21  21  21  SER SER LLL . n 
L 3 22  CYS 22  22  22  CYS CYS LLL . n 
L 3 23  ALA 23  23  23  ALA ALA LLL . n 
L 3 24  ALA 24  24  24  ALA ALA LLL . n 
L 3 25  SER 25  25  25  SER SER LLL . n 
L 3 26  GLY 26  26  26  GLY GLY LLL . n 
L 3 27  PHE 27  27  27  PHE PHE LLL . n 
L 3 28  THR 28  28  28  THR THR LLL . n 
L 3 29  PHE 29  29  29  PHE PHE LLL . n 
L 3 30  SER 30  30  30  SER SER LLL . n 
L 3 31  SER 31  31  31  SER SER LLL . n 
L 3 32  TYR 32  32  32  TYR TYR LLL . n 
L 3 33  THR 33  33  33  THR THR LLL . n 
L 3 34  MET 34  34  34  MET MET LLL . n 
L 3 35  ASN 35  35  35  ASN ASN LLL . n 
L 3 36  TRP 36  36  36  TRP TRP LLL . n 
L 3 37  VAL 37  37  37  VAL VAL LLL . n 
L 3 38  ARG 38  38  38  ARG ARG LLL . n 
L 3 39  GLN 39  39  39  GLN GLN LLL . n 
L 3 40  ALA 40  40  40  ALA ALA LLL . n 
L 3 41  PRO 41  41  41  PRO PRO LLL . n 
L 3 42  GLY 42  42  42  GLY GLY LLL . n 
L 3 43  LYS 43  43  43  LYS LYS LLL . n 
L 3 44  GLY 44  44  44  GLY GLY LLL . n 
L 3 45  LEU 45  45  45  LEU LEU LLL . n 
L 3 46  GLN 46  46  46  GLN GLN LLL . n 
L 3 47  TRP 47  47  47  TRP TRP LLL . n 
L 3 48  VAL 48  48  48  VAL VAL LLL . n 
L 3 49  SER 49  49  49  SER SER LLL . n 
L 3 50  SER 50  50  50  SER SER LLL . n 
L 3 51  ILE 51  51  51  ILE ILE LLL . n 
L 3 52  SER 52  52  52  SER SER LLL . n 
L 3 53  SER 53  53  53  SER SER LLL . n 
L 3 54  SER 54  54  54  SER SER LLL . n 
L 3 55  SER 55  55  55  SER SER LLL . n 
L 3 56  THR 56  56  56  THR THR LLL . n 
L 3 57  TYR 57  57  57  TYR TYR LLL . n 
L 3 58  MET 58  58  58  MET MET LLL . n 
L 3 59  TYR 59  59  59  TYR TYR LLL . n 
L 3 60  TYR 60  60  60  TYR TYR LLL . n 
L 3 61  GLY 61  61  61  GLY GLY LLL . n 
L 3 62  ASP 62  62  62  ASP ASP LLL . n 
L 3 63  SER 63  63  63  SER SER LLL . n 
L 3 64  VAL 64  64  64  VAL VAL LLL . n 
L 3 65  LYS 65  65  65  LYS LYS LLL . n 
L 3 66  GLY 66  66  66  GLY GLY LLL . n 
L 3 67  ARG 67  67  67  ARG ARG LLL . n 
L 3 68  PHE 68  68  68  PHE PHE LLL . n 
L 3 69  THR 69  69  69  THR THR LLL . n 
L 3 70  ILE 70  70  70  ILE ILE LLL . n 
L 3 71  SER 71  71  71  SER SER LLL . n 
L 3 72  ARG 72  72  72  ARG ARG LLL . n 
L 3 73  ASP 73  73  73  ASP ASP LLL . n 
L 3 74  ASN 74  74  74  ASN ASN LLL . n 
L 3 75  ALA 75  75  75  ALA ALA LLL . n 
L 3 76  ARG 76  76  76  ARG ARG LLL . n 
L 3 77  ASN 77  77  77  ASN ASN LLL . n 
L 3 78  SER 78  78  78  SER SER LLL . n 
L 3 79  LEU 79  79  79  LEU LEU LLL . n 
L 3 80  TYR 80  80  80  TYR TYR LLL . n 
L 3 81  LEU 81  81  81  LEU LEU LLL . n 
L 3 82  GLN 82  82  82  GLN GLN LLL . n 
L 3 83  MET 83  83  83  MET MET LLL . n 
L 3 84  ASN 84  84  84  ASN ASN LLL . n 
L 3 85  SER 85  85  85  SER SER LLL . n 
L 3 86  LEU 86  86  86  LEU LEU LLL . n 
L 3 87  ARG 87  87  87  ARG ARG LLL . n 
L 3 88  VAL 88  88  88  VAL VAL LLL . n 
L 3 89  GLU 89  89  89  GLU GLU LLL . n 
L 3 90  ASP 90  90  90  ASP ASP LLL . n 
L 3 91  THR 91  91  91  THR THR LLL . n 
L 3 92  ALA 92  92  92  ALA ALA LLL . n 
L 3 93  VAL 93  93  93  VAL VAL LLL . n 
L 3 94  TYR 94  94  94  TYR TYR LLL . n 
L 3 95  TYR 95  95  95  TYR TYR LLL . n 
L 3 96  CYS 96  96  96  CYS CYS LLL . n 
L 3 97  ALA 97  97  97  ALA ALA LLL . n 
L 3 98  ARG 98  98  98  ARG ARG LLL . n 
L 3 99  TYR 99  99  99  TYR TYR LLL . n 
L 3 100 ALA 100 100 100 ALA ALA LLL . n 
L 3 101 HIS 101 101 101 HIS HIS LLL . n 
L 3 102 ASP 102 102 102 ASP ASP LLL . n 
L 3 103 TRP 103 103 103 TRP TRP LLL . n 
L 3 104 ASN 104 104 104 ASN ASN LLL . n 
L 3 105 VAL 105 105 105 VAL VAL LLL . n 
L 3 106 ASP 106 106 106 ASP ASP LLL . n 
L 3 107 TYR 107 107 107 TYR TYR LLL . n 
L 3 108 TRP 108 108 108 TRP TRP LLL . n 
L 3 109 GLY 109 109 109 GLY GLY LLL . n 
L 3 110 GLN 110 110 110 GLN GLN LLL . n 
L 3 111 GLY 111 111 111 GLY GLY LLL . n 
L 3 112 THR 112 112 112 THR THR LLL . n 
L 3 113 LEU 113 113 113 LEU LEU LLL . n 
L 3 114 VAL 114 114 114 VAL VAL LLL . n 
L 3 115 THR 115 115 115 THR THR LLL . n 
L 3 116 VAL 116 116 116 VAL VAL LLL . n 
L 3 117 SER 117 117 117 SER SER LLL . n 
L 3 118 SER 118 118 118 SER SER LLL . n 
L 3 119 ALA 119 119 119 ALA ALA LLL . n 
L 3 120 SER 120 120 120 SER SER LLL . n 
L 3 121 THR 121 121 121 THR THR LLL . n 
L 3 122 LYS 122 122 122 LYS LYS LLL . n 
L 3 123 GLY 123 123 123 GLY GLY LLL . n 
L 3 124 PRO 124 124 124 PRO PRO LLL . n 
L 3 125 SER 125 125 125 SER SER LLL . n 
L 3 126 VAL 126 126 126 VAL VAL LLL . n 
L 3 127 PHE 127 132 ?   ?   ?   LLL . n 
L 3 128 PRO 128 133 ?   ?   ?   LLL . n 
L 3 129 LEU 129 134 ?   ?   ?   LLL . n 
L 3 130 ALA 130 135 ?   ?   ?   LLL . n 
L 3 131 PRO 131 136 ?   ?   ?   LLL . n 
L 3 132 SER 132 137 ?   ?   ?   LLL . n 
L 3 133 SER 133 138 ?   ?   ?   LLL . n 
L 3 134 LYS 134 139 ?   ?   ?   LLL . n 
L 3 135 SER 135 140 ?   ?   ?   LLL . n 
L 3 136 THR 136 141 ?   ?   ?   LLL . n 
L 3 137 SER 137 142 ?   ?   ?   LLL . n 
L 3 138 GLY 138 143 ?   ?   ?   LLL . n 
L 3 139 GLY 139 144 ?   ?   ?   LLL . n 
L 3 140 THR 140 145 ?   ?   ?   LLL . n 
L 3 141 ALA 141 146 ?   ?   ?   LLL . n 
L 3 142 ALA 142 147 ?   ?   ?   LLL . n 
L 3 143 LEU 143 148 ?   ?   ?   LLL . n 
L 3 144 GLY 144 149 ?   ?   ?   LLL . n 
L 3 145 CYS 145 150 150 CYS CYS LLL . n 
L 3 146 LEU 146 151 151 LEU LEU LLL . n 
L 3 147 VAL 147 152 152 VAL VAL LLL . n 
L 3 148 LYS 148 153 153 LYS LYS LLL . n 
L 3 149 ASP 149 154 154 ASP ASP LLL . n 
L 3 150 TYR 150 155 155 TYR TYR LLL . n 
L 3 151 PHE 151 156 156 PHE PHE LLL . n 
L 3 152 PRO 152 157 157 PRO PRO LLL . n 
L 3 153 GLU 153 158 158 GLU GLU LLL . n 
L 3 154 PRO 154 159 159 PRO PRO LLL . n 
L 3 155 VAL 155 160 160 VAL VAL LLL . n 
L 3 156 THR 156 161 161 THR THR LLL . n 
L 3 157 VAL 157 162 162 VAL VAL LLL . n 
L 3 158 SER 158 163 ?   ?   ?   LLL . n 
L 3 159 TRP 159 164 ?   ?   ?   LLL . n 
L 3 160 ASN 160 165 ?   ?   ?   LLL . n 
L 3 161 SER 161 166 ?   ?   ?   LLL . n 
L 3 162 GLY 162 167 ?   ?   ?   LLL . n 
L 3 163 ALA 163 168 ?   ?   ?   LLL . n 
L 3 164 LEU 164 169 ?   ?   ?   LLL . n 
L 3 165 THR 165 170 ?   ?   ?   LLL . n 
L 3 166 SER 166 171 ?   ?   ?   LLL . n 
L 3 167 GLY 167 172 ?   ?   ?   LLL . n 
L 3 168 VAL 168 173 ?   ?   ?   LLL . n 
L 3 169 HIS 169 174 174 HIS HIS LLL . n 
L 3 170 THR 170 175 175 THR THR LLL . n 
L 3 171 PHE 171 176 176 PHE PHE LLL . n 
L 3 172 PRO 172 177 177 PRO PRO LLL . n 
L 3 173 ALA 173 178 178 ALA ALA LLL . n 
L 3 174 VAL 174 179 179 VAL VAL LLL . n 
L 3 175 LEU 175 180 180 LEU LEU LLL . n 
L 3 176 GLN 176 181 181 GLN GLN LLL . n 
L 3 177 SER 177 182 182 SER SER LLL . n 
L 3 178 SER 178 183 183 SER SER LLL . n 
L 3 179 GLY 179 184 184 GLY GLY LLL . n 
L 3 180 LEU 180 185 185 LEU LEU LLL . n 
L 3 181 TYR 181 186 186 TYR TYR LLL . n 
L 3 182 SER 182 187 187 SER SER LLL . n 
L 3 183 LEU 183 188 188 LEU LEU LLL . n 
L 3 184 SER 184 189 189 SER SER LLL . n 
L 3 185 SER 185 190 190 SER SER LLL . n 
L 3 186 VAL 186 191 191 VAL VAL LLL . n 
L 3 187 VAL 187 192 192 VAL VAL LLL . n 
L 3 188 THR 188 193 ?   ?   ?   LLL . n 
L 3 189 VAL 189 194 ?   ?   ?   LLL . n 
L 3 190 PRO 190 195 ?   ?   ?   LLL . n 
L 3 191 SER 191 196 ?   ?   ?   LLL . n 
L 3 192 SER 192 197 ?   ?   ?   LLL . n 
L 3 193 SER 193 198 ?   ?   ?   LLL . n 
L 3 194 LEU 194 199 ?   ?   ?   LLL . n 
L 3 195 GLY 195 200 ?   ?   ?   LLL . n 
L 3 196 THR 196 201 ?   ?   ?   LLL . n 
L 3 197 GLN 197 202 ?   ?   ?   LLL . n 
L 3 198 THR 198 203 ?   ?   ?   LLL . n 
L 3 199 TYR 199 204 ?   ?   ?   LLL . n 
L 3 200 ILE 200 205 ?   ?   ?   LLL . n 
L 3 201 CYS 201 206 ?   ?   ?   LLL . n 
L 3 202 ASN 202 207 207 ASN ASN LLL . n 
L 3 203 VAL 203 208 208 VAL VAL LLL . n 
L 3 204 ASN 204 209 209 ASN ASN LLL . n 
L 3 205 HIS 205 210 210 HIS HIS LLL . n 
L 3 206 LYS 206 211 211 LYS LYS LLL . n 
L 3 207 PRO 207 212 212 PRO PRO LLL . n 
L 3 208 SER 208 213 213 SER SER LLL . n 
L 3 209 ASN 209 214 214 ASN ASN LLL . n 
L 3 210 THR 210 215 215 THR THR LLL . n 
L 3 211 LYS 211 216 216 LYS LYS LLL . n 
L 3 212 VAL 212 217 217 VAL VAL LLL . n 
L 3 213 ASP 213 218 218 ASP ASP LLL . n 
L 3 214 LYS 214 219 ?   ?   ?   LLL . n 
L 3 215 LYS 215 220 ?   ?   ?   LLL . n 
L 3 216 VAL 216 221 ?   ?   ?   LLL . n 
L 3 217 GLU 217 222 ?   ?   ?   LLL . n 
L 3 218 PRO 218 223 ?   ?   ?   LLL . n 
L 3 219 LYS 219 224 ?   ?   ?   LLL . n 
L 3 220 SER 220 225 ?   ?   ?   LLL . n 
L 3 221 CYS 221 226 ?   ?   ?   LLL . n 
L 3 222 ASP 222 227 ?   ?   ?   LLL . n 
L 3 223 LYS 223 228 ?   ?   ?   LLL . n 
L 3 224 THR 224 229 ?   ?   ?   LLL . n 
L 3 225 HIS 225 230 ?   ?   ?   LLL . n 
L 3 226 THR 226 231 ?   ?   ?   LLL . n 
L 3 227 CYS 227 232 ?   ?   ?   LLL . n 
L 3 228 PRO 228 233 ?   ?   ?   LLL . n 
L 3 229 PRO 229 234 ?   ?   ?   LLL . n 
L 3 230 CYS 230 235 ?   ?   ?   LLL . n 
L 3 231 PRO 231 236 ?   ?   ?   LLL . n 
L 3 232 ALA 232 237 ?   ?   ?   LLL . n 
L 3 233 PRO 233 238 ?   ?   ?   LLL . n 
L 3 234 GLU 234 239 ?   ?   ?   LLL . n 
L 3 235 LEU 235 240 ?   ?   ?   LLL . n 
L 3 236 LEU 236 241 ?   ?   ?   LLL . n 
L 3 237 GLY 237 242 ?   ?   ?   LLL . n 
L 3 238 GLY 238 243 ?   ?   ?   LLL . n 
L 3 239 PRO 239 244 ?   ?   ?   LLL . n 
L 3 240 SER 240 245 ?   ?   ?   LLL . n 
L 3 241 VAL 241 246 ?   ?   ?   LLL . n 
L 3 242 PHE 242 247 ?   ?   ?   LLL . n 
L 3 243 LEU 243 248 ?   ?   ?   LLL . n 
L 3 244 PHE 244 249 ?   ?   ?   LLL . n 
L 3 245 PRO 245 250 ?   ?   ?   LLL . n 
L 3 246 PRO 246 251 ?   ?   ?   LLL . n 
L 3 247 LYS 247 252 ?   ?   ?   LLL . n 
L 3 248 PRO 248 253 ?   ?   ?   LLL . n 
L 3 249 LYS 249 254 ?   ?   ?   LLL . n 
L 3 250 ASP 250 255 ?   ?   ?   LLL . n 
L 3 251 THR 251 256 ?   ?   ?   LLL . n 
L 3 252 LEU 252 257 ?   ?   ?   LLL . n 
L 3 253 MET 253 258 ?   ?   ?   LLL . n 
L 3 254 ILE 254 259 ?   ?   ?   LLL . n 
L 3 255 SER 255 260 ?   ?   ?   LLL . n 
L 3 256 ARG 256 261 ?   ?   ?   LLL . n 
L 3 257 THR 257 262 ?   ?   ?   LLL . n 
L 3 258 PRO 258 263 ?   ?   ?   LLL . n 
L 3 259 GLU 259 264 ?   ?   ?   LLL . n 
L 3 260 VAL 260 265 ?   ?   ?   LLL . n 
L 3 261 THR 261 266 ?   ?   ?   LLL . n 
L 3 262 CYS 262 267 ?   ?   ?   LLL . n 
L 3 263 VAL 263 268 ?   ?   ?   LLL . n 
L 3 264 VAL 264 269 ?   ?   ?   LLL . n 
L 3 265 VAL 265 270 ?   ?   ?   LLL . n 
L 3 266 ASP 266 271 ?   ?   ?   LLL . n 
L 3 267 VAL 267 272 ?   ?   ?   LLL . n 
L 3 268 SER 268 273 ?   ?   ?   LLL . n 
L 3 269 HIS 269 274 ?   ?   ?   LLL . n 
L 3 270 GLU 270 275 ?   ?   ?   LLL . n 
L 3 271 ASP 271 276 ?   ?   ?   LLL . n 
L 3 272 PRO 272 277 ?   ?   ?   LLL . n 
L 3 273 GLU 273 278 ?   ?   ?   LLL . n 
L 3 274 VAL 274 279 ?   ?   ?   LLL . n 
L 3 275 LYS 275 280 ?   ?   ?   LLL . n 
L 3 276 PHE 276 281 ?   ?   ?   LLL . n 
L 3 277 ASN 277 282 ?   ?   ?   LLL . n 
L 3 278 TRP 278 283 ?   ?   ?   LLL . n 
L 3 279 TYR 279 284 ?   ?   ?   LLL . n 
L 3 280 VAL 280 285 ?   ?   ?   LLL . n 
L 3 281 ASP 281 286 ?   ?   ?   LLL . n 
L 3 282 GLY 282 287 ?   ?   ?   LLL . n 
L 3 283 VAL 283 288 ?   ?   ?   LLL . n 
L 3 284 GLU 284 289 ?   ?   ?   LLL . n 
L 3 285 VAL 285 290 ?   ?   ?   LLL . n 
L 3 286 HIS 286 291 ?   ?   ?   LLL . n 
L 3 287 ASN 287 292 ?   ?   ?   LLL . n 
L 3 288 ALA 288 293 ?   ?   ?   LLL . n 
L 3 289 LYS 289 294 ?   ?   ?   LLL . n 
L 3 290 THR 290 295 ?   ?   ?   LLL . n 
L 3 291 LYS 291 296 ?   ?   ?   LLL . n 
L 3 292 PRO 292 297 ?   ?   ?   LLL . n 
L 3 293 ARG 293 298 ?   ?   ?   LLL . n 
L 3 294 GLU 294 299 ?   ?   ?   LLL . n 
L 3 295 GLU 295 300 ?   ?   ?   LLL . n 
L 3 296 GLN 296 301 ?   ?   ?   LLL . n 
L 3 297 TYR 297 302 ?   ?   ?   LLL . n 
L 3 298 ASN 298 303 ?   ?   ?   LLL . n 
L 3 299 SER 299 304 ?   ?   ?   LLL . n 
L 3 300 THR 300 305 ?   ?   ?   LLL . n 
L 3 301 TYR 301 306 ?   ?   ?   LLL . n 
L 3 302 ARG 302 307 ?   ?   ?   LLL . n 
L 3 303 VAL 303 308 ?   ?   ?   LLL . n 
L 3 304 VAL 304 309 ?   ?   ?   LLL . n 
L 3 305 SER 305 310 ?   ?   ?   LLL . n 
L 3 306 VAL 306 311 ?   ?   ?   LLL . n 
L 3 307 LEU 307 312 ?   ?   ?   LLL . n 
L 3 308 THR 308 313 ?   ?   ?   LLL . n 
L 3 309 VAL 309 314 ?   ?   ?   LLL . n 
L 3 310 LEU 310 315 ?   ?   ?   LLL . n 
L 3 311 HIS 311 316 ?   ?   ?   LLL . n 
L 3 312 GLN 312 317 ?   ?   ?   LLL . n 
L 3 313 ASP 313 318 ?   ?   ?   LLL . n 
L 3 314 TRP 314 319 ?   ?   ?   LLL . n 
L 3 315 LEU 315 320 ?   ?   ?   LLL . n 
L 3 316 ASN 316 321 ?   ?   ?   LLL . n 
L 3 317 GLY 317 322 ?   ?   ?   LLL . n 
L 3 318 LYS 318 323 ?   ?   ?   LLL . n 
L 3 319 GLU 319 324 ?   ?   ?   LLL . n 
L 3 320 TYR 320 325 ?   ?   ?   LLL . n 
L 3 321 LYS 321 326 ?   ?   ?   LLL . n 
L 3 322 CYS 322 327 ?   ?   ?   LLL . n 
L 3 323 LYS 323 328 ?   ?   ?   LLL . n 
L 3 324 VAL 324 329 ?   ?   ?   LLL . n 
L 3 325 SER 325 330 ?   ?   ?   LLL . n 
L 3 326 ASN 326 331 ?   ?   ?   LLL . n 
L 3 327 LYS 327 332 ?   ?   ?   LLL . n 
L 3 328 ALA 328 333 ?   ?   ?   LLL . n 
L 3 329 LEU 329 334 ?   ?   ?   LLL . n 
L 3 330 PRO 330 335 ?   ?   ?   LLL . n 
L 3 331 ALA 331 336 ?   ?   ?   LLL . n 
L 3 332 PRO 332 337 ?   ?   ?   LLL . n 
L 3 333 ILE 333 338 ?   ?   ?   LLL . n 
L 3 334 GLU 334 339 ?   ?   ?   LLL . n 
L 3 335 LYS 335 340 ?   ?   ?   LLL . n 
L 3 336 THR 336 341 ?   ?   ?   LLL . n 
L 3 337 ILE 337 342 ?   ?   ?   LLL . n 
L 3 338 SER 338 343 ?   ?   ?   LLL . n 
L 3 339 LYS 339 344 ?   ?   ?   LLL . n 
L 3 340 ALA 340 345 ?   ?   ?   LLL . n 
L 3 341 LYS 341 346 ?   ?   ?   LLL . n 
L 3 342 GLY 342 347 ?   ?   ?   LLL . n 
L 3 343 GLN 343 348 ?   ?   ?   LLL . n 
L 3 344 PRO 344 349 ?   ?   ?   LLL . n 
L 3 345 ARG 345 350 ?   ?   ?   LLL . n 
L 3 346 GLU 346 351 ?   ?   ?   LLL . n 
L 3 347 PRO 347 352 ?   ?   ?   LLL . n 
L 3 348 GLN 348 353 ?   ?   ?   LLL . n 
L 3 349 VAL 349 354 ?   ?   ?   LLL . n 
L 3 350 TYR 350 355 ?   ?   ?   LLL . n 
L 3 351 THR 351 356 ?   ?   ?   LLL . n 
L 3 352 LEU 352 357 ?   ?   ?   LLL . n 
L 3 353 PRO 353 358 ?   ?   ?   LLL . n 
L 3 354 PRO 354 359 ?   ?   ?   LLL . n 
L 3 355 SER 355 360 ?   ?   ?   LLL . n 
L 3 356 ARG 356 361 ?   ?   ?   LLL . n 
L 3 357 ASP 357 362 ?   ?   ?   LLL . n 
L 3 358 GLU 358 363 ?   ?   ?   LLL . n 
L 3 359 LEU 359 364 ?   ?   ?   LLL . n 
L 3 360 THR 360 365 ?   ?   ?   LLL . n 
L 3 361 LYS 361 366 ?   ?   ?   LLL . n 
L 3 362 ASN 362 367 ?   ?   ?   LLL . n 
L 3 363 GLN 363 368 ?   ?   ?   LLL . n 
L 3 364 VAL 364 369 ?   ?   ?   LLL . n 
L 3 365 SER 365 370 ?   ?   ?   LLL . n 
L 3 366 LEU 366 371 ?   ?   ?   LLL . n 
L 3 367 THR 367 372 ?   ?   ?   LLL . n 
L 3 368 CYS 368 373 ?   ?   ?   LLL . n 
L 3 369 LEU 369 374 ?   ?   ?   LLL . n 
L 3 370 VAL 370 375 ?   ?   ?   LLL . n 
L 3 371 LYS 371 376 ?   ?   ?   LLL . n 
L 3 372 GLY 372 377 ?   ?   ?   LLL . n 
L 3 373 PHE 373 378 ?   ?   ?   LLL . n 
L 3 374 TYR 374 379 ?   ?   ?   LLL . n 
L 3 375 PRO 375 380 ?   ?   ?   LLL . n 
L 3 376 SER 376 381 ?   ?   ?   LLL . n 
L 3 377 ASP 377 382 ?   ?   ?   LLL . n 
L 3 378 ILE 378 383 ?   ?   ?   LLL . n 
L 3 379 ALA 379 384 ?   ?   ?   LLL . n 
L 3 380 VAL 380 385 ?   ?   ?   LLL . n 
L 3 381 GLU 381 386 ?   ?   ?   LLL . n 
L 3 382 TRP 382 387 ?   ?   ?   LLL . n 
L 3 383 GLU 383 388 ?   ?   ?   LLL . n 
L 3 384 SER 384 389 ?   ?   ?   LLL . n 
L 3 385 ASN 385 390 ?   ?   ?   LLL . n 
L 3 386 GLY 386 391 ?   ?   ?   LLL . n 
L 3 387 GLN 387 392 ?   ?   ?   LLL . n 
L 3 388 PRO 388 393 ?   ?   ?   LLL . n 
L 3 389 GLU 389 394 ?   ?   ?   LLL . n 
L 3 390 ASN 390 395 ?   ?   ?   LLL . n 
L 3 391 ASN 391 396 ?   ?   ?   LLL . n 
L 3 392 TYR 392 397 ?   ?   ?   LLL . n 
L 3 393 LYS 393 398 ?   ?   ?   LLL . n 
L 3 394 THR 394 399 ?   ?   ?   LLL . n 
L 3 395 THR 395 400 ?   ?   ?   LLL . n 
L 3 396 PRO 396 401 ?   ?   ?   LLL . n 
L 3 397 PRO 397 402 ?   ?   ?   LLL . n 
L 3 398 VAL 398 403 ?   ?   ?   LLL . n 
M 2 1   GLN 1   1   ?   ?   ?   MMM . n 
M 2 2   SER 2   2   2   SER SER MMM . n 
M 2 3   VAL 3   3   3   VAL VAL MMM . n 
M 2 4   LEU 4   4   4   LEU LEU MMM . n 
M 2 5   THR 5   5   5   THR THR MMM . n 
M 2 6   GLN 6   6   6   GLN GLN MMM . n 
M 2 7   PRO 7   7   7   PRO PRO MMM . n 
M 2 8   PRO 8   8   8   PRO PRO MMM . n 
M 2 9   SER 9   9   9   SER SER MMM . n 
M 2 10  ALA 10  10  10  ALA ALA MMM . n 
M 2 11  SER 11  11  11  SER SER MMM . n 
M 2 12  GLY 12  12  12  GLY GLY MMM . n 
M 2 13  THR 13  13  13  THR THR MMM . n 
M 2 14  PRO 14  14  14  PRO PRO MMM . n 
M 2 15  GLY 15  15  15  GLY GLY MMM . n 
M 2 16  GLN 16  16  16  GLN GLN MMM . n 
M 2 17  ARG 17  17  17  ARG ARG MMM . n 
M 2 18  VAL 18  18  18  VAL VAL MMM . n 
M 2 19  THR 19  19  19  THR THR MMM . n 
M 2 20  ILE 20  20  20  ILE ILE MMM . n 
M 2 21  SER 21  21  21  SER SER MMM . n 
M 2 22  CYS 22  22  22  CYS CYS MMM . n 
M 2 23  SER 23  23  23  SER SER MMM . n 
M 2 24  GLY 24  24  24  GLY GLY MMM . n 
M 2 25  GLY 25  25  25  GLY GLY MMM . n 
M 2 26  SER 26  26  26  SER SER MMM . n 
M 2 27  SER 27  27  27  SER SER MMM . n 
M 2 28  ASN 28  28  28  ASN ASN MMM . n 
M 2 29  ILE 29  29  29  ILE ILE MMM . n 
M 2 30  GLY 30  30  30  GLY GLY MMM . n 
M 2 31  SER 31  31  31  SER SER MMM . n 
M 2 32  ASN 32  32  32  ASN ASN MMM . n 
M 2 33  PRO 33  33  33  PRO PRO MMM . n 
M 2 34  VAL 34  34  34  VAL VAL MMM . n 
M 2 35  ASN 35  35  35  ASN ASN MMM . n 
M 2 36  TRP 36  36  36  TRP TRP MMM . n 
M 2 37  PHE 37  37  37  PHE PHE MMM . n 
M 2 38  GLN 38  38  38  GLN GLN MMM . n 
M 2 39  GLN 39  39  39  GLN GLN MMM . n 
M 2 40  PHE 40  40  40  PHE PHE MMM . n 
M 2 41  PRO 41  41  41  PRO PRO MMM . n 
M 2 42  GLY 42  42  42  GLY GLY MMM . n 
M 2 43  THR 43  43  43  THR THR MMM . n 
M 2 44  ALA 44  44  44  ALA ALA MMM . n 
M 2 45  PRO 45  45  45  PRO PRO MMM . n 
M 2 46  LYS 46  46  46  LYS LYS MMM . n 
M 2 47  LEU 47  47  47  LEU LEU MMM . n 
M 2 48  LEU 48  48  48  LEU LEU MMM . n 
M 2 49  ILE 49  49  49  ILE ILE MMM . n 
M 2 50  TYR 50  50  50  TYR TYR MMM . n 
M 2 51  ALA 51  51  51  ALA ALA MMM . n 
M 2 52  ASN 52  52  52  ASN ASN MMM . n 
M 2 53  THR 53  53  53  THR THR MMM . n 
M 2 54  GLN 54  54  54  GLN GLN MMM . n 
M 2 55  ARG 55  55  55  ARG ARG MMM . n 
M 2 56  PRO 56  56  56  PRO PRO MMM . n 
M 2 57  SER 57  57  57  SER SER MMM . n 
M 2 58  GLY 58  58  58  GLY GLY MMM . n 
M 2 59  VAL 59  59  59  VAL VAL MMM . n 
M 2 60  PRO 60  60  60  PRO PRO MMM . n 
M 2 61  ASP 61  61  61  ASP ASP MMM . n 
M 2 62  ARG 62  62  62  ARG ARG MMM . n 
M 2 63  PHE 63  63  63  PHE PHE MMM . n 
M 2 64  SER 64  64  64  SER SER MMM . n 
M 2 65  GLY 65  65  65  GLY GLY MMM . n 
M 2 66  SER 66  66  66  SER SER MMM . n 
M 2 67  LYS 67  67  67  LYS LYS MMM . n 
M 2 68  SER 68  68  68  SER SER MMM . n 
M 2 69  GLY 69  69  69  GLY GLY MMM . n 
M 2 70  THR 70  70  70  THR THR MMM . n 
M 2 71  SER 71  71  71  SER SER MMM . n 
M 2 72  VAL 72  72  72  VAL VAL MMM . n 
M 2 73  SER 73  73  73  SER SER MMM . n 
M 2 74  LEU 74  74  74  LEU LEU MMM . n 
M 2 75  ALA 75  75  75  ALA ALA MMM . n 
M 2 76  ILE 76  76  76  ILE ILE MMM . n 
M 2 77  SER 77  77  77  SER SER MMM . n 
M 2 78  GLY 78  78  78  GLY GLY MMM . n 
M 2 79  LEU 79  79  79  LEU LEU MMM . n 
M 2 80  GLN 80  80  80  GLN GLN MMM . n 
M 2 81  SER 81  81  81  SER SER MMM . n 
M 2 82  GLU 82  82  82  GLU GLU MMM . n 
M 2 83  ASP 83  83  83  ASP ASP MMM . n 
M 2 84  GLU 84  84  84  GLU GLU MMM . n 
M 2 85  GLY 85  85  85  GLY GLY MMM . n 
M 2 86  ASP 86  86  86  ASP ASP MMM . n 
M 2 87  TYR 87  87  87  TYR TYR MMM . n 
M 2 88  HIS 88  88  88  HIS HIS MMM . n 
M 2 89  CYS 89  89  89  CYS CYS MMM . n 
M 2 90  ALA 90  90  90  ALA ALA MMM . n 
M 2 91  ALA 91  91  91  ALA ALA MMM . n 
M 2 92  TRP 92  92  92  TRP TRP MMM . n 
M 2 93  ASP 93  93  93  ASP ASP MMM . n 
M 2 94  ASP 94  94  94  ASP ASP MMM . n 
M 2 95  SER 95  95  95  SER SER MMM . n 
M 2 96  LEU 96  96  96  LEU LEU MMM . n 
M 2 97  LYS 97  97  97  LYS LYS MMM . n 
M 2 98  GLY 98  98  98  GLY GLY MMM . n 
M 2 99  TRP 99  99  99  TRP TRP MMM . n 
M 2 100 VAL 100 100 100 VAL VAL MMM . n 
M 2 101 PHE 101 101 101 PHE PHE MMM . n 
M 2 102 GLY 102 102 102 GLY GLY MMM . n 
M 2 103 GLY 103 103 103 GLY GLY MMM . n 
M 2 104 GLY 104 104 104 GLY GLY MMM . n 
M 2 105 THR 105 105 105 THR THR MMM . n 
M 2 106 LYS 106 106 106 LYS LYS MMM . n 
M 2 107 LEU 107 107 107 LEU LEU MMM . n 
M 2 108 THR 108 108 108 THR THR MMM . n 
M 2 109 VAL 109 109 109 VAL VAL MMM . n 
M 2 110 LEU 110 110 ?   ?   ?   MMM . n 
M 2 111 GLY 111 111 ?   ?   ?   MMM . n 
M 2 112 ALA 112 112 ?   ?   ?   MMM . n 
M 2 113 PRO 113 113 ?   ?   ?   MMM . n 
M 2 114 LYS 114 114 ?   ?   ?   MMM . n 
M 2 115 ALA 115 115 ?   ?   ?   MMM . n 
M 2 116 ASN 116 116 ?   ?   ?   MMM . n 
M 2 117 PRO 117 117 ?   ?   ?   MMM . n 
M 2 118 THR 118 118 ?   ?   ?   MMM . n 
M 2 119 VAL 119 119 ?   ?   ?   MMM . n 
M 2 120 THR 120 120 ?   ?   ?   MMM . n 
M 2 121 LEU 121 121 ?   ?   ?   MMM . n 
M 2 122 PHE 122 122 ?   ?   ?   MMM . n 
M 2 123 PRO 123 123 ?   ?   ?   MMM . n 
M 2 124 PRO 124 124 ?   ?   ?   MMM . n 
M 2 125 SER 125 125 ?   ?   ?   MMM . n 
M 2 126 SER 126 126 ?   ?   ?   MMM . n 
M 2 127 GLU 127 127 ?   ?   ?   MMM . n 
M 2 128 GLU 128 128 ?   ?   ?   MMM . n 
M 2 129 LEU 129 129 ?   ?   ?   MMM . n 
M 2 130 GLN 130 130 ?   ?   ?   MMM . n 
M 2 131 ALA 131 131 ?   ?   ?   MMM . n 
M 2 132 ASN 132 132 ?   ?   ?   MMM . n 
M 2 133 LYS 133 133 ?   ?   ?   MMM . n 
M 2 134 ALA 134 134 ?   ?   ?   MMM . n 
M 2 135 THR 135 135 ?   ?   ?   MMM . n 
M 2 136 LEU 136 136 ?   ?   ?   MMM . n 
M 2 137 VAL 137 137 ?   ?   ?   MMM . n 
M 2 138 CYS 138 138 ?   ?   ?   MMM . n 
M 2 139 LEU 139 139 ?   ?   ?   MMM . n 
M 2 140 ILE 140 140 ?   ?   ?   MMM . n 
M 2 141 SER 141 141 ?   ?   ?   MMM . n 
M 2 142 ASP 142 142 ?   ?   ?   MMM . n 
M 2 143 PHE 143 143 ?   ?   ?   MMM . n 
M 2 144 TYR 144 144 ?   ?   ?   MMM . n 
M 2 145 PRO 145 145 ?   ?   ?   MMM . n 
M 2 146 GLY 146 146 ?   ?   ?   MMM . n 
M 2 147 ALA 147 147 ?   ?   ?   MMM . n 
M 2 148 VAL 148 148 ?   ?   ?   MMM . n 
M 2 149 THR 149 149 ?   ?   ?   MMM . n 
M 2 150 VAL 150 150 ?   ?   ?   MMM . n 
M 2 151 ALA 151 151 ?   ?   ?   MMM . n 
M 2 152 TRP 152 152 ?   ?   ?   MMM . n 
M 2 153 LYS 153 153 ?   ?   ?   MMM . n 
M 2 154 ALA 154 154 ?   ?   ?   MMM . n 
M 2 155 ASP 155 155 ?   ?   ?   MMM . n 
M 2 156 GLY 156 156 ?   ?   ?   MMM . n 
M 2 157 SER 157 157 ?   ?   ?   MMM . n 
M 2 158 PRO 158 158 ?   ?   ?   MMM . n 
M 2 159 VAL 159 159 ?   ?   ?   MMM . n 
M 2 160 LYS 160 160 ?   ?   ?   MMM . n 
M 2 161 ALA 161 161 ?   ?   ?   MMM . n 
M 2 162 GLY 162 162 ?   ?   ?   MMM . n 
M 2 163 VAL 163 163 ?   ?   ?   MMM . n 
M 2 164 GLU 164 164 ?   ?   ?   MMM . n 
M 2 165 THR 165 165 ?   ?   ?   MMM . n 
M 2 166 THR 166 166 ?   ?   ?   MMM . n 
M 2 167 LYS 167 167 ?   ?   ?   MMM . n 
M 2 168 PRO 168 168 ?   ?   ?   MMM . n 
M 2 169 SER 169 169 ?   ?   ?   MMM . n 
M 2 170 LYS 170 170 ?   ?   ?   MMM . n 
M 2 171 GLN 171 171 ?   ?   ?   MMM . n 
M 2 172 SER 172 172 ?   ?   ?   MMM . n 
M 2 173 ASN 173 173 ?   ?   ?   MMM . n 
M 2 174 ASN 174 174 ?   ?   ?   MMM . n 
M 2 175 LYS 175 175 ?   ?   ?   MMM . n 
M 2 176 THR 176 176 ?   ?   ?   MMM . n 
M 2 177 ALA 177 177 ?   ?   ?   MMM . n 
M 2 178 ALA 178 178 ?   ?   ?   MMM . n 
M 2 179 SER 179 179 ?   ?   ?   MMM . n 
M 2 180 SER 180 180 ?   ?   ?   MMM . n 
M 2 181 TYR 181 181 ?   ?   ?   MMM . n 
M 2 182 LEU 182 182 ?   ?   ?   MMM . n 
M 2 183 SER 183 183 ?   ?   ?   MMM . n 
M 2 184 LEU 184 184 ?   ?   ?   MMM . n 
M 2 185 THR 185 185 ?   ?   ?   MMM . n 
M 2 186 PRO 186 186 ?   ?   ?   MMM . n 
M 2 187 GLU 187 187 ?   ?   ?   MMM . n 
M 2 188 GLN 188 188 ?   ?   ?   MMM . n 
M 2 189 TRP 189 189 ?   ?   ?   MMM . n 
M 2 190 LYS 190 190 ?   ?   ?   MMM . n 
M 2 191 SER 191 191 ?   ?   ?   MMM . n 
M 2 192 HIS 192 192 ?   ?   ?   MMM . n 
M 2 193 ARG 193 193 ?   ?   ?   MMM . n 
M 2 194 SER 194 194 ?   ?   ?   MMM . n 
M 2 195 TYR 195 195 ?   ?   ?   MMM . n 
M 2 196 SER 196 196 ?   ?   ?   MMM . n 
M 2 197 CYS 197 197 ?   ?   ?   MMM . n 
M 2 198 GLN 198 198 ?   ?   ?   MMM . n 
M 2 199 VAL 199 199 ?   ?   ?   MMM . n 
M 2 200 THR 200 200 ?   ?   ?   MMM . n 
M 2 201 HIS 201 201 ?   ?   ?   MMM . n 
M 2 202 GLU 202 202 ?   ?   ?   MMM . n 
M 2 203 GLY 203 203 ?   ?   ?   MMM . n 
M 2 204 THR 204 204 ?   ?   ?   MMM . n 
M 2 205 THR 205 205 ?   ?   ?   MMM . n 
M 2 206 VAL 206 206 ?   ?   ?   MMM . n 
M 2 207 GLU 207 207 ?   ?   ?   MMM . n 
M 2 208 LYS 208 208 ?   ?   ?   MMM . n 
M 2 209 THR 209 209 ?   ?   ?   MMM . n 
M 2 210 VAL 210 210 ?   ?   ?   MMM . n 
M 2 211 ALA 211 211 ?   ?   ?   MMM . n 
M 2 212 PRO 212 212 ?   ?   ?   MMM . n 
N 3 1   GLU 1   1   1   GLU GLU NNN . n 
N 3 2   VAL 2   2   2   VAL VAL NNN . n 
N 3 3   GLN 3   3   3   GLN GLN NNN . n 
N 3 4   LEU 4   4   4   LEU LEU NNN . n 
N 3 5   VAL 5   5   5   VAL VAL NNN . n 
N 3 6   GLU 6   6   6   GLU GLU NNN . n 
N 3 7   SER 7   7   7   SER SER NNN . n 
N 3 8   GLY 8   8   8   GLY GLY NNN . n 
N 3 9   GLY 9   9   9   GLY GLY NNN . n 
N 3 10  GLY 10  10  10  GLY GLY NNN . n 
N 3 11  LEU 11  11  11  LEU LEU NNN . n 
N 3 12  VAL 12  12  12  VAL VAL NNN . n 
N 3 13  LYS 13  13  13  LYS LYS NNN . n 
N 3 14  PRO 14  14  14  PRO PRO NNN . n 
N 3 15  GLY 15  15  15  GLY GLY NNN . n 
N 3 16  GLY 16  16  16  GLY GLY NNN . n 
N 3 17  SER 17  17  17  SER SER NNN . n 
N 3 18  LEU 18  18  18  LEU LEU NNN . n 
N 3 19  ARG 19  19  19  ARG ARG NNN . n 
N 3 20  LEU 20  20  20  LEU LEU NNN . n 
N 3 21  SER 21  21  21  SER SER NNN . n 
N 3 22  CYS 22  22  22  CYS CYS NNN . n 
N 3 23  ALA 23  23  23  ALA ALA NNN . n 
N 3 24  ALA 24  24  24  ALA ALA NNN . n 
N 3 25  SER 25  25  25  SER SER NNN . n 
N 3 26  GLY 26  26  26  GLY GLY NNN . n 
N 3 27  PHE 27  27  27  PHE PHE NNN . n 
N 3 28  THR 28  28  28  THR THR NNN . n 
N 3 29  PHE 29  29  29  PHE PHE NNN . n 
N 3 30  SER 30  30  30  SER SER NNN . n 
N 3 31  SER 31  31  31  SER SER NNN . n 
N 3 32  TYR 32  32  32  TYR TYR NNN . n 
N 3 33  THR 33  33  33  THR THR NNN . n 
N 3 34  MET 34  34  34  MET MET NNN . n 
N 3 35  ASN 35  35  35  ASN ASN NNN . n 
N 3 36  TRP 36  36  36  TRP TRP NNN . n 
N 3 37  VAL 37  37  37  VAL VAL NNN . n 
N 3 38  ARG 38  38  38  ARG ARG NNN . n 
N 3 39  GLN 39  39  39  GLN GLN NNN . n 
N 3 40  ALA 40  40  40  ALA ALA NNN . n 
N 3 41  PRO 41  41  41  PRO PRO NNN . n 
N 3 42  GLY 42  42  42  GLY GLY NNN . n 
N 3 43  LYS 43  43  43  LYS LYS NNN . n 
N 3 44  GLY 44  44  44  GLY GLY NNN . n 
N 3 45  LEU 45  45  45  LEU LEU NNN . n 
N 3 46  GLN 46  46  46  GLN GLN NNN . n 
N 3 47  TRP 47  47  47  TRP TRP NNN . n 
N 3 48  VAL 48  48  48  VAL VAL NNN . n 
N 3 49  SER 49  49  49  SER SER NNN . n 
N 3 50  SER 50  50  50  SER SER NNN . n 
N 3 51  ILE 51  51  51  ILE ILE NNN . n 
N 3 52  SER 52  52  52  SER SER NNN . n 
N 3 53  SER 53  53  53  SER SER NNN . n 
N 3 54  SER 54  54  54  SER SER NNN . n 
N 3 55  SER 55  55  55  SER SER NNN . n 
N 3 56  THR 56  56  56  THR THR NNN . n 
N 3 57  TYR 57  57  57  TYR TYR NNN . n 
N 3 58  MET 58  58  58  MET MET NNN . n 
N 3 59  TYR 59  59  59  TYR TYR NNN . n 
N 3 60  TYR 60  60  60  TYR TYR NNN . n 
N 3 61  GLY 61  61  61  GLY GLY NNN . n 
N 3 62  ASP 62  62  62  ASP ASP NNN . n 
N 3 63  SER 63  63  63  SER SER NNN . n 
N 3 64  VAL 64  64  64  VAL VAL NNN . n 
N 3 65  LYS 65  65  65  LYS LYS NNN . n 
N 3 66  GLY 66  66  66  GLY GLY NNN . n 
N 3 67  ARG 67  67  67  ARG ARG NNN . n 
N 3 68  PHE 68  68  68  PHE PHE NNN . n 
N 3 69  THR 69  69  69  THR THR NNN . n 
N 3 70  ILE 70  70  70  ILE ILE NNN . n 
N 3 71  SER 71  71  71  SER SER NNN . n 
N 3 72  ARG 72  72  72  ARG ARG NNN . n 
N 3 73  ASP 73  73  73  ASP ASP NNN . n 
N 3 74  ASN 74  74  74  ASN ASN NNN . n 
N 3 75  ALA 75  75  75  ALA ALA NNN . n 
N 3 76  ARG 76  76  76  ARG ARG NNN . n 
N 3 77  ASN 77  77  77  ASN ASN NNN . n 
N 3 78  SER 78  78  78  SER SER NNN . n 
N 3 79  LEU 79  79  79  LEU LEU NNN . n 
N 3 80  TYR 80  80  80  TYR TYR NNN . n 
N 3 81  LEU 81  81  81  LEU LEU NNN . n 
N 3 82  GLN 82  82  82  GLN GLN NNN . n 
N 3 83  MET 83  83  83  MET MET NNN . n 
N 3 84  ASN 84  84  84  ASN ASN NNN . n 
N 3 85  SER 85  85  85  SER SER NNN . n 
N 3 86  LEU 86  86  86  LEU LEU NNN . n 
N 3 87  ARG 87  87  87  ARG ARG NNN . n 
N 3 88  VAL 88  88  88  VAL VAL NNN . n 
N 3 89  GLU 89  89  89  GLU GLU NNN . n 
N 3 90  ASP 90  90  90  ASP ASP NNN . n 
N 3 91  THR 91  91  91  THR THR NNN . n 
N 3 92  ALA 92  92  92  ALA ALA NNN . n 
N 3 93  VAL 93  93  93  VAL VAL NNN . n 
N 3 94  TYR 94  94  94  TYR TYR NNN . n 
N 3 95  TYR 95  95  95  TYR TYR NNN . n 
N 3 96  CYS 96  96  96  CYS CYS NNN . n 
N 3 97  ALA 97  97  97  ALA ALA NNN . n 
N 3 98  ARG 98  98  98  ARG ARG NNN . n 
N 3 99  TYR 99  99  99  TYR TYR NNN . n 
N 3 100 ALA 100 100 100 ALA ALA NNN . n 
N 3 101 HIS 101 101 101 HIS HIS NNN . n 
N 3 102 ASP 102 102 102 ASP ASP NNN . n 
N 3 103 TRP 103 103 103 TRP TRP NNN . n 
N 3 104 ASN 104 104 104 ASN ASN NNN . n 
N 3 105 VAL 105 105 105 VAL VAL NNN . n 
N 3 106 ASP 106 106 106 ASP ASP NNN . n 
N 3 107 TYR 107 107 107 TYR TYR NNN . n 
N 3 108 TRP 108 108 108 TRP TRP NNN . n 
N 3 109 GLY 109 109 109 GLY GLY NNN . n 
N 3 110 GLN 110 110 110 GLN GLN NNN . n 
N 3 111 GLY 111 111 111 GLY GLY NNN . n 
N 3 112 THR 112 112 112 THR THR NNN . n 
N 3 113 LEU 113 113 113 LEU LEU NNN . n 
N 3 114 VAL 114 114 114 VAL VAL NNN . n 
N 3 115 THR 115 115 115 THR THR NNN . n 
N 3 116 VAL 116 116 116 VAL VAL NNN . n 
N 3 117 SER 117 117 117 SER SER NNN . n 
N 3 118 SER 118 118 118 SER SER NNN . n 
N 3 119 ALA 119 119 ?   ?   ?   NNN . n 
N 3 120 SER 120 120 ?   ?   ?   NNN . n 
N 3 121 THR 121 121 ?   ?   ?   NNN . n 
N 3 122 LYS 122 122 ?   ?   ?   NNN . n 
N 3 123 GLY 123 123 ?   ?   ?   NNN . n 
N 3 124 PRO 124 124 ?   ?   ?   NNN . n 
N 3 125 SER 125 125 ?   ?   ?   NNN . n 
N 3 126 VAL 126 126 ?   ?   ?   NNN . n 
N 3 127 PHE 127 127 ?   ?   ?   NNN . n 
N 3 128 PRO 128 128 ?   ?   ?   NNN . n 
N 3 129 LEU 129 129 ?   ?   ?   NNN . n 
N 3 130 ALA 130 130 ?   ?   ?   NNN . n 
N 3 131 PRO 131 131 ?   ?   ?   NNN . n 
N 3 132 SER 132 132 ?   ?   ?   NNN . n 
N 3 133 SER 133 133 ?   ?   ?   NNN . n 
N 3 134 LYS 134 134 ?   ?   ?   NNN . n 
N 3 135 SER 135 135 ?   ?   ?   NNN . n 
N 3 136 THR 136 136 ?   ?   ?   NNN . n 
N 3 137 SER 137 137 ?   ?   ?   NNN . n 
N 3 138 GLY 138 138 ?   ?   ?   NNN . n 
N 3 139 GLY 139 139 ?   ?   ?   NNN . n 
N 3 140 THR 140 140 ?   ?   ?   NNN . n 
N 3 141 ALA 141 141 ?   ?   ?   NNN . n 
N 3 142 ALA 142 142 ?   ?   ?   NNN . n 
N 3 143 LEU 143 143 ?   ?   ?   NNN . n 
N 3 144 GLY 144 144 ?   ?   ?   NNN . n 
N 3 145 CYS 145 145 ?   ?   ?   NNN . n 
N 3 146 LEU 146 146 ?   ?   ?   NNN . n 
N 3 147 VAL 147 147 ?   ?   ?   NNN . n 
N 3 148 LYS 148 148 ?   ?   ?   NNN . n 
N 3 149 ASP 149 149 ?   ?   ?   NNN . n 
N 3 150 TYR 150 150 ?   ?   ?   NNN . n 
N 3 151 PHE 151 151 ?   ?   ?   NNN . n 
N 3 152 PRO 152 152 ?   ?   ?   NNN . n 
N 3 153 GLU 153 153 ?   ?   ?   NNN . n 
N 3 154 PRO 154 154 ?   ?   ?   NNN . n 
N 3 155 VAL 155 155 ?   ?   ?   NNN . n 
N 3 156 THR 156 156 ?   ?   ?   NNN . n 
N 3 157 VAL 157 157 ?   ?   ?   NNN . n 
N 3 158 SER 158 158 ?   ?   ?   NNN . n 
N 3 159 TRP 159 159 ?   ?   ?   NNN . n 
N 3 160 ASN 160 160 ?   ?   ?   NNN . n 
N 3 161 SER 161 161 ?   ?   ?   NNN . n 
N 3 162 GLY 162 162 ?   ?   ?   NNN . n 
N 3 163 ALA 163 163 ?   ?   ?   NNN . n 
N 3 164 LEU 164 164 ?   ?   ?   NNN . n 
N 3 165 THR 165 165 ?   ?   ?   NNN . n 
N 3 166 SER 166 166 ?   ?   ?   NNN . n 
N 3 167 GLY 167 167 ?   ?   ?   NNN . n 
N 3 168 VAL 168 168 ?   ?   ?   NNN . n 
N 3 169 HIS 169 169 ?   ?   ?   NNN . n 
N 3 170 THR 170 170 ?   ?   ?   NNN . n 
N 3 171 PHE 171 171 ?   ?   ?   NNN . n 
N 3 172 PRO 172 172 ?   ?   ?   NNN . n 
N 3 173 ALA 173 173 ?   ?   ?   NNN . n 
N 3 174 VAL 174 174 ?   ?   ?   NNN . n 
N 3 175 LEU 175 175 ?   ?   ?   NNN . n 
N 3 176 GLN 176 176 ?   ?   ?   NNN . n 
N 3 177 SER 177 177 ?   ?   ?   NNN . n 
N 3 178 SER 178 178 ?   ?   ?   NNN . n 
N 3 179 GLY 179 179 ?   ?   ?   NNN . n 
N 3 180 LEU 180 180 ?   ?   ?   NNN . n 
N 3 181 TYR 181 181 ?   ?   ?   NNN . n 
N 3 182 SER 182 182 ?   ?   ?   NNN . n 
N 3 183 LEU 183 183 ?   ?   ?   NNN . n 
N 3 184 SER 184 184 ?   ?   ?   NNN . n 
N 3 185 SER 185 185 ?   ?   ?   NNN . n 
N 3 186 VAL 186 186 ?   ?   ?   NNN . n 
N 3 187 VAL 187 187 ?   ?   ?   NNN . n 
N 3 188 THR 188 188 ?   ?   ?   NNN . n 
N 3 189 VAL 189 189 ?   ?   ?   NNN . n 
N 3 190 PRO 190 190 ?   ?   ?   NNN . n 
N 3 191 SER 191 191 ?   ?   ?   NNN . n 
N 3 192 SER 192 192 ?   ?   ?   NNN . n 
N 3 193 SER 193 193 ?   ?   ?   NNN . n 
N 3 194 LEU 194 194 ?   ?   ?   NNN . n 
N 3 195 GLY 195 195 ?   ?   ?   NNN . n 
N 3 196 THR 196 196 ?   ?   ?   NNN . n 
N 3 197 GLN 197 197 ?   ?   ?   NNN . n 
N 3 198 THR 198 198 ?   ?   ?   NNN . n 
N 3 199 TYR 199 199 ?   ?   ?   NNN . n 
N 3 200 ILE 200 200 ?   ?   ?   NNN . n 
N 3 201 CYS 201 201 ?   ?   ?   NNN . n 
N 3 202 ASN 202 202 ?   ?   ?   NNN . n 
N 3 203 VAL 203 203 ?   ?   ?   NNN . n 
N 3 204 ASN 204 204 ?   ?   ?   NNN . n 
N 3 205 HIS 205 205 ?   ?   ?   NNN . n 
N 3 206 LYS 206 206 ?   ?   ?   NNN . n 
N 3 207 PRO 207 207 ?   ?   ?   NNN . n 
N 3 208 SER 208 208 ?   ?   ?   NNN . n 
N 3 209 ASN 209 209 ?   ?   ?   NNN . n 
N 3 210 THR 210 210 ?   ?   ?   NNN . n 
N 3 211 LYS 211 211 ?   ?   ?   NNN . n 
N 3 212 VAL 212 212 ?   ?   ?   NNN . n 
N 3 213 ASP 213 213 ?   ?   ?   NNN . n 
N 3 214 LYS 214 214 ?   ?   ?   NNN . n 
N 3 215 LYS 215 215 ?   ?   ?   NNN . n 
N 3 216 VAL 216 216 ?   ?   ?   NNN . n 
N 3 217 GLU 217 217 ?   ?   ?   NNN . n 
N 3 218 PRO 218 218 ?   ?   ?   NNN . n 
N 3 219 LYS 219 219 ?   ?   ?   NNN . n 
N 3 220 SER 220 220 ?   ?   ?   NNN . n 
N 3 221 CYS 221 221 ?   ?   ?   NNN . n 
N 3 222 ASP 222 222 ?   ?   ?   NNN . n 
N 3 223 LYS 223 223 ?   ?   ?   NNN . n 
N 3 224 THR 224 224 ?   ?   ?   NNN . n 
N 3 225 HIS 225 225 ?   ?   ?   NNN . n 
N 3 226 THR 226 226 ?   ?   ?   NNN . n 
N 3 227 CYS 227 227 ?   ?   ?   NNN . n 
N 3 228 PRO 228 228 ?   ?   ?   NNN . n 
N 3 229 PRO 229 229 ?   ?   ?   NNN . n 
N 3 230 CYS 230 230 ?   ?   ?   NNN . n 
N 3 231 PRO 231 231 ?   ?   ?   NNN . n 
N 3 232 ALA 232 232 ?   ?   ?   NNN . n 
N 3 233 PRO 233 233 ?   ?   ?   NNN . n 
N 3 234 GLU 234 234 ?   ?   ?   NNN . n 
N 3 235 LEU 235 235 ?   ?   ?   NNN . n 
N 3 236 LEU 236 236 ?   ?   ?   NNN . n 
N 3 237 GLY 237 237 ?   ?   ?   NNN . n 
N 3 238 GLY 238 238 ?   ?   ?   NNN . n 
N 3 239 PRO 239 239 ?   ?   ?   NNN . n 
N 3 240 SER 240 240 ?   ?   ?   NNN . n 
N 3 241 VAL 241 241 ?   ?   ?   NNN . n 
N 3 242 PHE 242 242 ?   ?   ?   NNN . n 
N 3 243 LEU 243 243 ?   ?   ?   NNN . n 
N 3 244 PHE 244 244 ?   ?   ?   NNN . n 
N 3 245 PRO 245 245 ?   ?   ?   NNN . n 
N 3 246 PRO 246 246 ?   ?   ?   NNN . n 
N 3 247 LYS 247 247 ?   ?   ?   NNN . n 
N 3 248 PRO 248 248 ?   ?   ?   NNN . n 
N 3 249 LYS 249 249 ?   ?   ?   NNN . n 
N 3 250 ASP 250 250 ?   ?   ?   NNN . n 
N 3 251 THR 251 251 ?   ?   ?   NNN . n 
N 3 252 LEU 252 252 ?   ?   ?   NNN . n 
N 3 253 MET 253 253 ?   ?   ?   NNN . n 
N 3 254 ILE 254 254 ?   ?   ?   NNN . n 
N 3 255 SER 255 255 ?   ?   ?   NNN . n 
N 3 256 ARG 256 256 ?   ?   ?   NNN . n 
N 3 257 THR 257 257 ?   ?   ?   NNN . n 
N 3 258 PRO 258 258 ?   ?   ?   NNN . n 
N 3 259 GLU 259 259 ?   ?   ?   NNN . n 
N 3 260 VAL 260 260 ?   ?   ?   NNN . n 
N 3 261 THR 261 261 ?   ?   ?   NNN . n 
N 3 262 CYS 262 262 ?   ?   ?   NNN . n 
N 3 263 VAL 263 263 ?   ?   ?   NNN . n 
N 3 264 VAL 264 264 ?   ?   ?   NNN . n 
N 3 265 VAL 265 265 ?   ?   ?   NNN . n 
N 3 266 ASP 266 266 ?   ?   ?   NNN . n 
N 3 267 VAL 267 267 ?   ?   ?   NNN . n 
N 3 268 SER 268 268 ?   ?   ?   NNN . n 
N 3 269 HIS 269 269 ?   ?   ?   NNN . n 
N 3 270 GLU 270 270 ?   ?   ?   NNN . n 
N 3 271 ASP 271 271 ?   ?   ?   NNN . n 
N 3 272 PRO 272 272 ?   ?   ?   NNN . n 
N 3 273 GLU 273 273 ?   ?   ?   NNN . n 
N 3 274 VAL 274 274 ?   ?   ?   NNN . n 
N 3 275 LYS 275 275 ?   ?   ?   NNN . n 
N 3 276 PHE 276 276 ?   ?   ?   NNN . n 
N 3 277 ASN 277 277 ?   ?   ?   NNN . n 
N 3 278 TRP 278 278 ?   ?   ?   NNN . n 
N 3 279 TYR 279 279 ?   ?   ?   NNN . n 
N 3 280 VAL 280 280 ?   ?   ?   NNN . n 
N 3 281 ASP 281 281 ?   ?   ?   NNN . n 
N 3 282 GLY 282 282 ?   ?   ?   NNN . n 
N 3 283 VAL 283 283 ?   ?   ?   NNN . n 
N 3 284 GLU 284 284 ?   ?   ?   NNN . n 
N 3 285 VAL 285 285 ?   ?   ?   NNN . n 
N 3 286 HIS 286 286 ?   ?   ?   NNN . n 
N 3 287 ASN 287 287 ?   ?   ?   NNN . n 
N 3 288 ALA 288 288 ?   ?   ?   NNN . n 
N 3 289 LYS 289 289 ?   ?   ?   NNN . n 
N 3 290 THR 290 290 ?   ?   ?   NNN . n 
N 3 291 LYS 291 291 ?   ?   ?   NNN . n 
N 3 292 PRO 292 292 ?   ?   ?   NNN . n 
N 3 293 ARG 293 293 ?   ?   ?   NNN . n 
N 3 294 GLU 294 294 ?   ?   ?   NNN . n 
N 3 295 GLU 295 295 ?   ?   ?   NNN . n 
N 3 296 GLN 296 296 ?   ?   ?   NNN . n 
N 3 297 TYR 297 297 ?   ?   ?   NNN . n 
N 3 298 ASN 298 298 ?   ?   ?   NNN . n 
N 3 299 SER 299 299 ?   ?   ?   NNN . n 
N 3 300 THR 300 300 ?   ?   ?   NNN . n 
N 3 301 TYR 301 301 ?   ?   ?   NNN . n 
N 3 302 ARG 302 302 ?   ?   ?   NNN . n 
N 3 303 VAL 303 303 ?   ?   ?   NNN . n 
N 3 304 VAL 304 304 ?   ?   ?   NNN . n 
N 3 305 SER 305 305 ?   ?   ?   NNN . n 
N 3 306 VAL 306 306 ?   ?   ?   NNN . n 
N 3 307 LEU 307 307 ?   ?   ?   NNN . n 
N 3 308 THR 308 308 ?   ?   ?   NNN . n 
N 3 309 VAL 309 309 ?   ?   ?   NNN . n 
N 3 310 LEU 310 310 ?   ?   ?   NNN . n 
N 3 311 HIS 311 311 ?   ?   ?   NNN . n 
N 3 312 GLN 312 312 ?   ?   ?   NNN . n 
N 3 313 ASP 313 313 ?   ?   ?   NNN . n 
N 3 314 TRP 314 314 ?   ?   ?   NNN . n 
N 3 315 LEU 315 315 ?   ?   ?   NNN . n 
N 3 316 ASN 316 316 ?   ?   ?   NNN . n 
N 3 317 GLY 317 317 ?   ?   ?   NNN . n 
N 3 318 LYS 318 318 ?   ?   ?   NNN . n 
N 3 319 GLU 319 319 ?   ?   ?   NNN . n 
N 3 320 TYR 320 320 ?   ?   ?   NNN . n 
N 3 321 LYS 321 321 ?   ?   ?   NNN . n 
N 3 322 CYS 322 322 ?   ?   ?   NNN . n 
N 3 323 LYS 323 323 ?   ?   ?   NNN . n 
N 3 324 VAL 324 324 ?   ?   ?   NNN . n 
N 3 325 SER 325 325 ?   ?   ?   NNN . n 
N 3 326 ASN 326 326 ?   ?   ?   NNN . n 
N 3 327 LYS 327 327 ?   ?   ?   NNN . n 
N 3 328 ALA 328 328 ?   ?   ?   NNN . n 
N 3 329 LEU 329 329 ?   ?   ?   NNN . n 
N 3 330 PRO 330 330 ?   ?   ?   NNN . n 
N 3 331 ALA 331 331 ?   ?   ?   NNN . n 
N 3 332 PRO 332 332 ?   ?   ?   NNN . n 
N 3 333 ILE 333 333 ?   ?   ?   NNN . n 
N 3 334 GLU 334 334 ?   ?   ?   NNN . n 
N 3 335 LYS 335 335 ?   ?   ?   NNN . n 
N 3 336 THR 336 336 ?   ?   ?   NNN . n 
N 3 337 ILE 337 337 ?   ?   ?   NNN . n 
N 3 338 SER 338 338 ?   ?   ?   NNN . n 
N 3 339 LYS 339 339 ?   ?   ?   NNN . n 
N 3 340 ALA 340 340 ?   ?   ?   NNN . n 
N 3 341 LYS 341 341 ?   ?   ?   NNN . n 
N 3 342 GLY 342 342 ?   ?   ?   NNN . n 
N 3 343 GLN 343 343 ?   ?   ?   NNN . n 
N 3 344 PRO 344 344 ?   ?   ?   NNN . n 
N 3 345 ARG 345 345 ?   ?   ?   NNN . n 
N 3 346 GLU 346 346 ?   ?   ?   NNN . n 
N 3 347 PRO 347 347 ?   ?   ?   NNN . n 
N 3 348 GLN 348 348 ?   ?   ?   NNN . n 
N 3 349 VAL 349 349 ?   ?   ?   NNN . n 
N 3 350 TYR 350 350 ?   ?   ?   NNN . n 
N 3 351 THR 351 351 ?   ?   ?   NNN . n 
N 3 352 LEU 352 352 ?   ?   ?   NNN . n 
N 3 353 PRO 353 353 ?   ?   ?   NNN . n 
N 3 354 PRO 354 354 ?   ?   ?   NNN . n 
N 3 355 SER 355 355 ?   ?   ?   NNN . n 
N 3 356 ARG 356 356 ?   ?   ?   NNN . n 
N 3 357 ASP 357 357 ?   ?   ?   NNN . n 
N 3 358 GLU 358 358 ?   ?   ?   NNN . n 
N 3 359 LEU 359 359 ?   ?   ?   NNN . n 
N 3 360 THR 360 360 ?   ?   ?   NNN . n 
N 3 361 LYS 361 361 ?   ?   ?   NNN . n 
N 3 362 ASN 362 362 ?   ?   ?   NNN . n 
N 3 363 GLN 363 363 ?   ?   ?   NNN . n 
N 3 364 VAL 364 364 ?   ?   ?   NNN . n 
N 3 365 SER 365 365 ?   ?   ?   NNN . n 
N 3 366 LEU 366 366 ?   ?   ?   NNN . n 
N 3 367 THR 367 367 ?   ?   ?   NNN . n 
N 3 368 CYS 368 368 ?   ?   ?   NNN . n 
N 3 369 LEU 369 369 ?   ?   ?   NNN . n 
N 3 370 VAL 370 370 ?   ?   ?   NNN . n 
N 3 371 LYS 371 371 ?   ?   ?   NNN . n 
N 3 372 GLY 372 372 ?   ?   ?   NNN . n 
N 3 373 PHE 373 373 ?   ?   ?   NNN . n 
N 3 374 TYR 374 374 ?   ?   ?   NNN . n 
N 3 375 PRO 375 375 ?   ?   ?   NNN . n 
N 3 376 SER 376 376 ?   ?   ?   NNN . n 
N 3 377 ASP 377 377 ?   ?   ?   NNN . n 
N 3 378 ILE 378 378 ?   ?   ?   NNN . n 
N 3 379 ALA 379 379 ?   ?   ?   NNN . n 
N 3 380 VAL 380 380 ?   ?   ?   NNN . n 
N 3 381 GLU 381 381 ?   ?   ?   NNN . n 
N 3 382 TRP 382 382 ?   ?   ?   NNN . n 
N 3 383 GLU 383 383 ?   ?   ?   NNN . n 
N 3 384 SER 384 384 ?   ?   ?   NNN . n 
N 3 385 ASN 385 385 ?   ?   ?   NNN . n 
N 3 386 GLY 386 386 ?   ?   ?   NNN . n 
N 3 387 GLN 387 387 ?   ?   ?   NNN . n 
N 3 388 PRO 388 388 ?   ?   ?   NNN . n 
N 3 389 GLU 389 389 ?   ?   ?   NNN . n 
N 3 390 ASN 390 390 ?   ?   ?   NNN . n 
N 3 391 ASN 391 391 ?   ?   ?   NNN . n 
N 3 392 TYR 392 392 ?   ?   ?   NNN . n 
N 3 393 LYS 393 393 ?   ?   ?   NNN . n 
N 3 394 THR 394 394 ?   ?   ?   NNN . n 
N 3 395 THR 395 395 ?   ?   ?   NNN . n 
N 3 396 PRO 396 396 ?   ?   ?   NNN . n 
N 3 397 PRO 397 397 ?   ?   ?   NNN . n 
N 3 398 VAL 398 398 ?   ?   ?   NNN . n 
O 3 1   GLU 1   1   1   GLU GLU YYY . n 
O 3 2   VAL 2   2   2   VAL VAL YYY . n 
O 3 3   GLN 3   3   3   GLN GLN YYY . n 
O 3 4   LEU 4   4   4   LEU LEU YYY . n 
O 3 5   VAL 5   5   5   VAL VAL YYY . n 
O 3 6   GLU 6   6   6   GLU GLU YYY . n 
O 3 7   SER 7   7   7   SER SER YYY . n 
O 3 8   GLY 8   8   8   GLY GLY YYY . n 
O 3 9   GLY 9   9   9   GLY GLY YYY . n 
O 3 10  GLY 10  10  10  GLY GLY YYY . n 
O 3 11  LEU 11  11  11  LEU LEU YYY . n 
O 3 12  VAL 12  12  12  VAL VAL YYY . n 
O 3 13  LYS 13  13  13  LYS LYS YYY . n 
O 3 14  PRO 14  14  14  PRO PRO YYY . n 
O 3 15  GLY 15  15  15  GLY GLY YYY . n 
O 3 16  GLY 16  16  16  GLY GLY YYY . n 
O 3 17  SER 17  17  17  SER SER YYY . n 
O 3 18  LEU 18  18  18  LEU LEU YYY . n 
O 3 19  ARG 19  19  19  ARG ARG YYY . n 
O 3 20  LEU 20  20  20  LEU LEU YYY . n 
O 3 21  SER 21  21  21  SER SER YYY . n 
O 3 22  CYS 22  22  22  CYS CYS YYY . n 
O 3 23  ALA 23  23  23  ALA ALA YYY . n 
O 3 24  ALA 24  24  24  ALA ALA YYY . n 
O 3 25  SER 25  25  25  SER SER YYY . n 
O 3 26  GLY 26  26  26  GLY GLY YYY . n 
O 3 27  PHE 27  27  27  PHE PHE YYY . n 
O 3 28  THR 28  28  28  THR THR YYY . n 
O 3 29  PHE 29  29  29  PHE PHE YYY . n 
O 3 30  SER 30  30  30  SER SER YYY . n 
O 3 31  SER 31  31  31  SER SER YYY . n 
O 3 32  TYR 32  32  32  TYR TYR YYY . n 
O 3 33  THR 33  33  33  THR THR YYY . n 
O 3 34  MET 34  34  34  MET MET YYY . n 
O 3 35  ASN 35  35  35  ASN ASN YYY . n 
O 3 36  TRP 36  36  36  TRP TRP YYY . n 
O 3 37  VAL 37  37  37  VAL VAL YYY . n 
O 3 38  ARG 38  38  38  ARG ARG YYY . n 
O 3 39  GLN 39  39  39  GLN GLN YYY . n 
O 3 40  ALA 40  40  40  ALA ALA YYY . n 
O 3 41  PRO 41  41  41  PRO PRO YYY . n 
O 3 42  GLY 42  42  42  GLY GLY YYY . n 
O 3 43  LYS 43  43  43  LYS LYS YYY . n 
O 3 44  GLY 44  44  44  GLY GLY YYY . n 
O 3 45  LEU 45  45  45  LEU LEU YYY . n 
O 3 46  GLN 46  46  46  GLN GLN YYY . n 
O 3 47  TRP 47  47  47  TRP TRP YYY . n 
O 3 48  VAL 48  48  48  VAL VAL YYY . n 
O 3 49  SER 49  49  49  SER SER YYY . n 
O 3 50  SER 50  50  50  SER SER YYY . n 
O 3 51  ILE 51  51  51  ILE ILE YYY . n 
O 3 52  SER 52  52  52  SER SER YYY . n 
O 3 53  SER 53  53  53  SER SER YYY . n 
O 3 54  SER 54  54  54  SER SER YYY . n 
O 3 55  SER 55  55  55  SER SER YYY . n 
O 3 56  THR 56  56  56  THR THR YYY . n 
O 3 57  TYR 57  57  57  TYR TYR YYY . n 
O 3 58  MET 58  58  58  MET MET YYY . n 
O 3 59  TYR 59  59  59  TYR TYR YYY . n 
O 3 60  TYR 60  60  60  TYR TYR YYY . n 
O 3 61  GLY 61  61  61  GLY GLY YYY . n 
O 3 62  ASP 62  62  62  ASP ASP YYY . n 
O 3 63  SER 63  63  63  SER SER YYY . n 
O 3 64  VAL 64  64  64  VAL VAL YYY . n 
O 3 65  LYS 65  65  65  LYS LYS YYY . n 
O 3 66  GLY 66  66  66  GLY GLY YYY . n 
O 3 67  ARG 67  67  67  ARG ARG YYY . n 
O 3 68  PHE 68  68  68  PHE PHE YYY . n 
O 3 69  THR 69  69  69  THR THR YYY . n 
O 3 70  ILE 70  70  70  ILE ILE YYY . n 
O 3 71  SER 71  71  71  SER SER YYY . n 
O 3 72  ARG 72  72  72  ARG ARG YYY . n 
O 3 73  ASP 73  73  73  ASP ASP YYY . n 
O 3 74  ASN 74  74  74  ASN ASN YYY . n 
O 3 75  ALA 75  75  75  ALA ALA YYY . n 
O 3 76  ARG 76  76  76  ARG ARG YYY . n 
O 3 77  ASN 77  77  77  ASN ASN YYY . n 
O 3 78  SER 78  78  78  SER SER YYY . n 
O 3 79  LEU 79  79  79  LEU LEU YYY . n 
O 3 80  TYR 80  80  80  TYR TYR YYY . n 
O 3 81  LEU 81  81  81  LEU LEU YYY . n 
O 3 82  GLN 82  82  82  GLN GLN YYY . n 
O 3 83  MET 83  83  83  MET MET YYY . n 
O 3 84  ASN 84  84  84  ASN ASN YYY . n 
O 3 85  SER 85  85  85  SER SER YYY . n 
O 3 86  LEU 86  86  86  LEU LEU YYY . n 
O 3 87  ARG 87  87  87  ARG ARG YYY . n 
O 3 88  VAL 88  88  88  VAL VAL YYY . n 
O 3 89  GLU 89  89  89  GLU GLU YYY . n 
O 3 90  ASP 90  90  90  ASP ASP YYY . n 
O 3 91  THR 91  91  91  THR THR YYY . n 
O 3 92  ALA 92  92  92  ALA ALA YYY . n 
O 3 93  VAL 93  93  93  VAL VAL YYY . n 
O 3 94  TYR 94  94  94  TYR TYR YYY . n 
O 3 95  TYR 95  95  95  TYR TYR YYY . n 
O 3 96  CYS 96  96  96  CYS CYS YYY . n 
O 3 97  ALA 97  97  97  ALA ALA YYY . n 
O 3 98  ARG 98  98  98  ARG ARG YYY . n 
O 3 99  TYR 99  99  99  TYR TYR YYY . n 
O 3 100 ALA 100 100 100 ALA ALA YYY . n 
O 3 101 HIS 101 101 101 HIS HIS YYY . n 
O 3 102 ASP 102 102 102 ASP ASP YYY . n 
O 3 103 TRP 103 103 103 TRP TRP YYY . n 
O 3 104 ASN 104 104 104 ASN ASN YYY . n 
O 3 105 VAL 105 105 105 VAL VAL YYY . n 
O 3 106 ASP 106 106 106 ASP ASP YYY . n 
O 3 107 TYR 107 107 107 TYR TYR YYY . n 
O 3 108 TRP 108 108 108 TRP TRP YYY . n 
O 3 109 GLY 109 109 109 GLY GLY YYY . n 
O 3 110 GLN 110 110 110 GLN GLN YYY . n 
O 3 111 GLY 111 111 111 GLY GLY YYY . n 
O 3 112 THR 112 112 112 THR THR YYY . n 
O 3 113 LEU 113 113 113 LEU LEU YYY . n 
O 3 114 VAL 114 114 114 VAL VAL YYY . n 
O 3 115 THR 115 115 115 THR THR YYY . n 
O 3 116 VAL 116 116 116 VAL VAL YYY . n 
O 3 117 SER 117 117 117 SER SER YYY . n 
O 3 118 SER 118 118 118 SER SER YYY . n 
O 3 119 ALA 119 119 119 ALA ALA YYY . n 
O 3 120 SER 120 120 120 SER SER YYY . n 
O 3 121 THR 121 121 121 THR THR YYY . n 
O 3 122 LYS 122 122 122 LYS LYS YYY . n 
O 3 123 GLY 123 123 123 GLY GLY YYY . n 
O 3 124 PRO 124 124 124 PRO PRO YYY . n 
O 3 125 SER 125 125 125 SER SER YYY . n 
O 3 126 VAL 126 126 126 VAL VAL YYY . n 
O 3 127 PHE 127 127 127 PHE PHE YYY . n 
O 3 128 PRO 128 128 128 PRO PRO YYY . n 
O 3 129 LEU 129 129 129 LEU LEU YYY . n 
O 3 130 ALA 130 130 130 ALA ALA YYY . n 
O 3 131 PRO 131 131 131 PRO PRO YYY . n 
O 3 132 SER 132 137 ?   ?   ?   YYY . n 
O 3 133 SER 133 138 ?   ?   ?   YYY . n 
O 3 134 LYS 134 139 ?   ?   ?   YYY . n 
O 3 135 SER 135 140 ?   ?   ?   YYY . n 
O 3 136 THR 136 141 ?   ?   ?   YYY . n 
O 3 137 SER 137 142 ?   ?   ?   YYY . n 
O 3 138 GLY 138 143 ?   ?   ?   YYY . n 
O 3 139 GLY 139 144 ?   ?   ?   YYY . n 
O 3 140 THR 140 145 ?   ?   ?   YYY . n 
O 3 141 ALA 141 146 ?   ?   ?   YYY . n 
O 3 142 ALA 142 147 147 ALA ALA YYY . n 
O 3 143 LEU 143 148 148 LEU LEU YYY . n 
O 3 144 GLY 144 149 149 GLY GLY YYY . n 
O 3 145 CYS 145 150 150 CYS CYS YYY . n 
O 3 146 LEU 146 151 151 LEU LEU YYY . n 
O 3 147 VAL 147 152 152 VAL VAL YYY . n 
O 3 148 LYS 148 153 153 LYS LYS YYY . n 
O 3 149 ASP 149 154 154 ASP ASP YYY . n 
O 3 150 TYR 150 155 155 TYR TYR YYY . n 
O 3 151 PHE 151 156 156 PHE PHE YYY . n 
O 3 152 PRO 152 157 157 PRO PRO YYY . n 
O 3 153 GLU 153 158 158 GLU GLU YYY . n 
O 3 154 PRO 154 159 159 PRO PRO YYY . n 
O 3 155 VAL 155 160 160 VAL VAL YYY . n 
O 3 156 THR 156 161 161 THR THR YYY . n 
O 3 157 VAL 157 162 162 VAL VAL YYY . n 
O 3 158 SER 158 163 163 SER SER YYY . n 
O 3 159 TRP 159 164 164 TRP TRP YYY . n 
O 3 160 ASN 160 165 165 ASN ASN YYY . n 
O 3 161 SER 161 166 166 SER ALA YYY . n 
O 3 162 GLY 162 167 167 GLY ALA YYY . n 
O 3 163 ALA 163 168 168 ALA ALA YYY . n 
O 3 164 LEU 164 169 ?   ?   ?   YYY . n 
O 3 165 THR 165 170 ?   ?   ?   YYY . n 
O 3 166 SER 166 171 ?   ?   ?   YYY . n 
O 3 167 GLY 167 172 ?   ?   ?   YYY . n 
O 3 168 VAL 168 173 173 VAL VAL YYY . n 
O 3 169 HIS 169 174 174 HIS HIS YYY . n 
O 3 170 THR 170 175 175 THR THR YYY . n 
O 3 171 PHE 171 176 176 PHE PHE YYY . n 
O 3 172 PRO 172 177 177 PRO PRO YYY . n 
O 3 173 ALA 173 178 178 ALA ALA YYY . n 
O 3 174 VAL 174 179 179 VAL VAL YYY . n 
O 3 175 LEU 175 180 180 LEU LEU YYY . n 
O 3 176 GLN 176 181 181 GLN GLN YYY . n 
O 3 177 SER 177 182 182 SER SER YYY . n 
O 3 178 SER 178 183 183 SER SER YYY . n 
O 3 179 GLY 179 184 184 GLY GLY YYY . n 
O 3 180 LEU 180 185 185 LEU LEU YYY . n 
O 3 181 TYR 181 186 186 TYR TYR YYY . n 
O 3 182 SER 182 187 187 SER SER YYY . n 
O 3 183 LEU 183 188 188 LEU LEU YYY . n 
O 3 184 SER 184 189 189 SER SER YYY . n 
O 3 185 SER 185 190 190 SER SER YYY . n 
O 3 186 VAL 186 191 191 VAL VAL YYY . n 
O 3 187 VAL 187 192 192 VAL VAL YYY . n 
O 3 188 THR 188 193 ?   ?   ?   YYY . n 
O 3 189 VAL 189 194 ?   ?   ?   YYY . n 
O 3 190 PRO 190 195 ?   ?   ?   YYY . n 
O 3 191 SER 191 196 ?   ?   ?   YYY . n 
O 3 192 SER 192 197 ?   ?   ?   YYY . n 
O 3 193 SER 193 198 ?   ?   ?   YYY . n 
O 3 194 LEU 194 199 ?   ?   ?   YYY . n 
O 3 195 GLY 195 200 ?   ?   ?   YYY . n 
O 3 196 THR 196 201 ?   ?   ?   YYY . n 
O 3 197 GLN 197 202 ?   ?   ?   YYY . n 
O 3 198 THR 198 203 ?   ?   ?   YYY . n 
O 3 199 TYR 199 204 ?   ?   ?   YYY . n 
O 3 200 ILE 200 205 ?   ?   ?   YYY . n 
O 3 201 CYS 201 206 206 CYS CYS YYY . n 
O 3 202 ASN 202 207 207 ASN ASN YYY . n 
O 3 203 VAL 203 208 208 VAL VAL YYY . n 
O 3 204 ASN 204 209 209 ASN ASN YYY . n 
O 3 205 HIS 205 210 210 HIS HIS YYY . n 
O 3 206 LYS 206 211 211 LYS LYS YYY . n 
O 3 207 PRO 207 212 212 PRO PRO YYY . n 
O 3 208 SER 208 213 213 SER SER YYY . n 
O 3 209 ASN 209 214 214 ASN ASN YYY . n 
O 3 210 THR 210 215 215 THR THR YYY . n 
O 3 211 LYS 211 216 216 LYS LYS YYY . n 
O 3 212 VAL 212 217 217 VAL VAL YYY . n 
O 3 213 ASP 213 218 218 ASP ASP YYY . n 
O 3 214 LYS 214 219 219 LYS LYS YYY . n 
O 3 215 LYS 215 220 220 LYS LYS YYY . n 
O 3 216 VAL 216 221 221 VAL VAL YYY . n 
O 3 217 GLU 217 222 ?   ?   ?   YYY . n 
O 3 218 PRO 218 223 ?   ?   ?   YYY . n 
O 3 219 LYS 219 224 ?   ?   ?   YYY . n 
O 3 220 SER 220 225 ?   ?   ?   YYY . n 
O 3 221 CYS 221 226 ?   ?   ?   YYY . n 
O 3 222 ASP 222 227 ?   ?   ?   YYY . n 
O 3 223 LYS 223 228 ?   ?   ?   YYY . n 
O 3 224 THR 224 229 ?   ?   ?   YYY . n 
O 3 225 HIS 225 230 ?   ?   ?   YYY . n 
O 3 226 THR 226 231 ?   ?   ?   YYY . n 
O 3 227 CYS 227 232 ?   ?   ?   YYY . n 
O 3 228 PRO 228 233 ?   ?   ?   YYY . n 
O 3 229 PRO 229 234 ?   ?   ?   YYY . n 
O 3 230 CYS 230 235 ?   ?   ?   YYY . n 
O 3 231 PRO 231 236 ?   ?   ?   YYY . n 
O 3 232 ALA 232 237 ?   ?   ?   YYY . n 
O 3 233 PRO 233 238 ?   ?   ?   YYY . n 
O 3 234 GLU 234 239 ?   ?   ?   YYY . n 
O 3 235 LEU 235 240 ?   ?   ?   YYY . n 
O 3 236 LEU 236 241 ?   ?   ?   YYY . n 
O 3 237 GLY 237 242 ?   ?   ?   YYY . n 
O 3 238 GLY 238 243 ?   ?   ?   YYY . n 
O 3 239 PRO 239 244 ?   ?   ?   YYY . n 
O 3 240 SER 240 245 ?   ?   ?   YYY . n 
O 3 241 VAL 241 246 ?   ?   ?   YYY . n 
O 3 242 PHE 242 247 ?   ?   ?   YYY . n 
O 3 243 LEU 243 248 ?   ?   ?   YYY . n 
O 3 244 PHE 244 249 ?   ?   ?   YYY . n 
O 3 245 PRO 245 250 ?   ?   ?   YYY . n 
O 3 246 PRO 246 251 ?   ?   ?   YYY . n 
O 3 247 LYS 247 252 ?   ?   ?   YYY . n 
O 3 248 PRO 248 253 ?   ?   ?   YYY . n 
O 3 249 LYS 249 254 ?   ?   ?   YYY . n 
O 3 250 ASP 250 255 ?   ?   ?   YYY . n 
O 3 251 THR 251 256 ?   ?   ?   YYY . n 
O 3 252 LEU 252 257 ?   ?   ?   YYY . n 
O 3 253 MET 253 258 ?   ?   ?   YYY . n 
O 3 254 ILE 254 259 ?   ?   ?   YYY . n 
O 3 255 SER 255 260 ?   ?   ?   YYY . n 
O 3 256 ARG 256 261 ?   ?   ?   YYY . n 
O 3 257 THR 257 262 ?   ?   ?   YYY . n 
O 3 258 PRO 258 263 ?   ?   ?   YYY . n 
O 3 259 GLU 259 264 ?   ?   ?   YYY . n 
O 3 260 VAL 260 265 ?   ?   ?   YYY . n 
O 3 261 THR 261 266 ?   ?   ?   YYY . n 
O 3 262 CYS 262 267 ?   ?   ?   YYY . n 
O 3 263 VAL 263 268 ?   ?   ?   YYY . n 
O 3 264 VAL 264 269 ?   ?   ?   YYY . n 
O 3 265 VAL 265 270 ?   ?   ?   YYY . n 
O 3 266 ASP 266 271 ?   ?   ?   YYY . n 
O 3 267 VAL 267 272 ?   ?   ?   YYY . n 
O 3 268 SER 268 273 ?   ?   ?   YYY . n 
O 3 269 HIS 269 274 ?   ?   ?   YYY . n 
O 3 270 GLU 270 275 ?   ?   ?   YYY . n 
O 3 271 ASP 271 276 ?   ?   ?   YYY . n 
O 3 272 PRO 272 277 ?   ?   ?   YYY . n 
O 3 273 GLU 273 278 ?   ?   ?   YYY . n 
O 3 274 VAL 274 279 ?   ?   ?   YYY . n 
O 3 275 LYS 275 280 ?   ?   ?   YYY . n 
O 3 276 PHE 276 281 ?   ?   ?   YYY . n 
O 3 277 ASN 277 282 ?   ?   ?   YYY . n 
O 3 278 TRP 278 283 ?   ?   ?   YYY . n 
O 3 279 TYR 279 284 ?   ?   ?   YYY . n 
O 3 280 VAL 280 285 ?   ?   ?   YYY . n 
O 3 281 ASP 281 286 ?   ?   ?   YYY . n 
O 3 282 GLY 282 287 ?   ?   ?   YYY . n 
O 3 283 VAL 283 288 ?   ?   ?   YYY . n 
O 3 284 GLU 284 289 ?   ?   ?   YYY . n 
O 3 285 VAL 285 290 ?   ?   ?   YYY . n 
O 3 286 HIS 286 291 ?   ?   ?   YYY . n 
O 3 287 ASN 287 292 ?   ?   ?   YYY . n 
O 3 288 ALA 288 293 ?   ?   ?   YYY . n 
O 3 289 LYS 289 294 ?   ?   ?   YYY . n 
O 3 290 THR 290 295 ?   ?   ?   YYY . n 
O 3 291 LYS 291 296 ?   ?   ?   YYY . n 
O 3 292 PRO 292 297 ?   ?   ?   YYY . n 
O 3 293 ARG 293 298 ?   ?   ?   YYY . n 
O 3 294 GLU 294 299 ?   ?   ?   YYY . n 
O 3 295 GLU 295 300 ?   ?   ?   YYY . n 
O 3 296 GLN 296 301 ?   ?   ?   YYY . n 
O 3 297 TYR 297 302 ?   ?   ?   YYY . n 
O 3 298 ASN 298 303 ?   ?   ?   YYY . n 
O 3 299 SER 299 304 ?   ?   ?   YYY . n 
O 3 300 THR 300 305 ?   ?   ?   YYY . n 
O 3 301 TYR 301 306 ?   ?   ?   YYY . n 
O 3 302 ARG 302 307 ?   ?   ?   YYY . n 
O 3 303 VAL 303 308 ?   ?   ?   YYY . n 
O 3 304 VAL 304 309 ?   ?   ?   YYY . n 
O 3 305 SER 305 310 ?   ?   ?   YYY . n 
O 3 306 VAL 306 311 ?   ?   ?   YYY . n 
O 3 307 LEU 307 312 ?   ?   ?   YYY . n 
O 3 308 THR 308 313 ?   ?   ?   YYY . n 
O 3 309 VAL 309 314 ?   ?   ?   YYY . n 
O 3 310 LEU 310 315 ?   ?   ?   YYY . n 
O 3 311 HIS 311 316 ?   ?   ?   YYY . n 
O 3 312 GLN 312 317 ?   ?   ?   YYY . n 
O 3 313 ASP 313 318 ?   ?   ?   YYY . n 
O 3 314 TRP 314 319 ?   ?   ?   YYY . n 
O 3 315 LEU 315 320 ?   ?   ?   YYY . n 
O 3 316 ASN 316 321 ?   ?   ?   YYY . n 
O 3 317 GLY 317 322 ?   ?   ?   YYY . n 
O 3 318 LYS 318 323 ?   ?   ?   YYY . n 
O 3 319 GLU 319 324 ?   ?   ?   YYY . n 
O 3 320 TYR 320 325 ?   ?   ?   YYY . n 
O 3 321 LYS 321 326 ?   ?   ?   YYY . n 
O 3 322 CYS 322 327 ?   ?   ?   YYY . n 
O 3 323 LYS 323 328 ?   ?   ?   YYY . n 
O 3 324 VAL 324 329 ?   ?   ?   YYY . n 
O 3 325 SER 325 330 ?   ?   ?   YYY . n 
O 3 326 ASN 326 331 ?   ?   ?   YYY . n 
O 3 327 LYS 327 332 ?   ?   ?   YYY . n 
O 3 328 ALA 328 333 ?   ?   ?   YYY . n 
O 3 329 LEU 329 334 ?   ?   ?   YYY . n 
O 3 330 PRO 330 335 ?   ?   ?   YYY . n 
O 3 331 ALA 331 336 ?   ?   ?   YYY . n 
O 3 332 PRO 332 337 ?   ?   ?   YYY . n 
O 3 333 ILE 333 338 ?   ?   ?   YYY . n 
O 3 334 GLU 334 339 ?   ?   ?   YYY . n 
O 3 335 LYS 335 340 ?   ?   ?   YYY . n 
O 3 336 THR 336 341 ?   ?   ?   YYY . n 
O 3 337 ILE 337 342 ?   ?   ?   YYY . n 
O 3 338 SER 338 343 ?   ?   ?   YYY . n 
O 3 339 LYS 339 344 ?   ?   ?   YYY . n 
O 3 340 ALA 340 345 ?   ?   ?   YYY . n 
O 3 341 LYS 341 346 ?   ?   ?   YYY . n 
O 3 342 GLY 342 347 ?   ?   ?   YYY . n 
O 3 343 GLN 343 348 ?   ?   ?   YYY . n 
O 3 344 PRO 344 349 ?   ?   ?   YYY . n 
O 3 345 ARG 345 350 ?   ?   ?   YYY . n 
O 3 346 GLU 346 351 ?   ?   ?   YYY . n 
O 3 347 PRO 347 352 ?   ?   ?   YYY . n 
O 3 348 GLN 348 353 ?   ?   ?   YYY . n 
O 3 349 VAL 349 354 ?   ?   ?   YYY . n 
O 3 350 TYR 350 355 ?   ?   ?   YYY . n 
O 3 351 THR 351 356 ?   ?   ?   YYY . n 
O 3 352 LEU 352 357 ?   ?   ?   YYY . n 
O 3 353 PRO 353 358 ?   ?   ?   YYY . n 
O 3 354 PRO 354 359 ?   ?   ?   YYY . n 
O 3 355 SER 355 360 ?   ?   ?   YYY . n 
O 3 356 ARG 356 361 ?   ?   ?   YYY . n 
O 3 357 ASP 357 362 ?   ?   ?   YYY . n 
O 3 358 GLU 358 363 ?   ?   ?   YYY . n 
O 3 359 LEU 359 364 ?   ?   ?   YYY . n 
O 3 360 THR 360 365 ?   ?   ?   YYY . n 
O 3 361 LYS 361 366 ?   ?   ?   YYY . n 
O 3 362 ASN 362 367 ?   ?   ?   YYY . n 
O 3 363 GLN 363 368 ?   ?   ?   YYY . n 
O 3 364 VAL 364 369 ?   ?   ?   YYY . n 
O 3 365 SER 365 370 ?   ?   ?   YYY . n 
O 3 366 LEU 366 371 ?   ?   ?   YYY . n 
O 3 367 THR 367 372 ?   ?   ?   YYY . n 
O 3 368 CYS 368 373 ?   ?   ?   YYY . n 
O 3 369 LEU 369 374 ?   ?   ?   YYY . n 
O 3 370 VAL 370 375 ?   ?   ?   YYY . n 
O 3 371 LYS 371 376 ?   ?   ?   YYY . n 
O 3 372 GLY 372 377 ?   ?   ?   YYY . n 
O 3 373 PHE 373 378 ?   ?   ?   YYY . n 
O 3 374 TYR 374 379 ?   ?   ?   YYY . n 
O 3 375 PRO 375 380 ?   ?   ?   YYY . n 
O 3 376 SER 376 381 ?   ?   ?   YYY . n 
O 3 377 ASP 377 382 ?   ?   ?   YYY . n 
O 3 378 ILE 378 383 ?   ?   ?   YYY . n 
O 3 379 ALA 379 384 ?   ?   ?   YYY . n 
O 3 380 VAL 380 385 ?   ?   ?   YYY . n 
O 3 381 GLU 381 386 ?   ?   ?   YYY . n 
O 3 382 TRP 382 387 ?   ?   ?   YYY . n 
O 3 383 GLU 383 388 ?   ?   ?   YYY . n 
O 3 384 SER 384 389 ?   ?   ?   YYY . n 
O 3 385 ASN 385 390 ?   ?   ?   YYY . n 
O 3 386 GLY 386 391 ?   ?   ?   YYY . n 
O 3 387 GLN 387 392 ?   ?   ?   YYY . n 
O 3 388 PRO 388 393 ?   ?   ?   YYY . n 
O 3 389 GLU 389 394 ?   ?   ?   YYY . n 
O 3 390 ASN 390 395 ?   ?   ?   YYY . n 
O 3 391 ASN 391 396 ?   ?   ?   YYY . n 
O 3 392 TYR 392 397 ?   ?   ?   YYY . n 
O 3 393 LYS 393 398 ?   ?   ?   YYY . n 
O 3 394 THR 394 399 ?   ?   ?   YYY . n 
O 3 395 THR 395 400 ?   ?   ?   YYY . n 
O 3 396 PRO 396 401 ?   ?   ?   YYY . n 
O 3 397 PRO 397 402 ?   ?   ?   YYY . n 
O 3 398 VAL 398 403 ?   ?   ?   YYY . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentadecameric 
_pdbx_struct_assembly.oligomeric_count     15 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2023-02-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER AAA 71  ? ? -155.86 78.93   
2  1 ASP AAA 166 ? ? -34.60  119.51  
3  1 MET AAA 181 ? ? -175.04 133.45  
4  1 ARG AAA 206 ? ? -129.70 -150.13 
5  1 THR AAA 229 ? ? -170.48 145.16  
6  1 SER BBB 71  ? ? -154.40 78.13   
7  1 ASP BBB 166 ? ? -35.15  118.79  
8  1 MET BBB 181 ? ? -174.09 133.98  
9  1 ARG BBB 206 ? ? -130.53 -150.11 
10 1 THR BBB 229 ? ? -170.54 143.21  
11 1 LEU CCC 27  ? ? -95.97  -158.45 
12 1 ASP CCC 49  ? ? 42.77   74.60   
13 1 GLU CCC 52  ? ? -48.94  -15.07  
14 1 SER CCC 71  ? ? -154.69 77.75   
15 1 ALA CCC 126 ? ? -39.97  123.15  
16 1 ASP CCC 166 ? ? -38.86  120.68  
17 1 MET CCC 181 ? ? -173.61 133.74  
18 1 ARG CCC 206 ? ? -130.92 -149.91 
19 1 THR CCC 229 ? ? -172.23 142.58  
20 1 LEU DDD 27  ? ? -96.13  -157.26 
21 1 SER DDD 71  ? ? -156.22 79.61   
22 1 ASP DDD 166 ? ? -33.89  118.17  
23 1 MET DDD 181 ? ? -174.92 133.73  
24 1 ARG DDD 206 ? ? -132.22 -150.01 
25 1 THR DDD 229 ? ? -173.49 142.38  
26 1 LEU EEE 27  ? ? -96.93  -139.60 
27 1 SER EEE 71  ? ? -155.39 78.22   
28 1 ASP EEE 166 ? ? -36.33  120.39  
29 1 MET EEE 181 ? ? -174.69 133.41  
30 1 ARG EEE 206 ? ? -164.24 75.90   
31 1 THR EEE 229 ? ? -172.16 144.26  
32 1 ASN FFF 28  ? ? -113.89 -92.73  
33 1 PRO FFF 41  ? ? -36.81  131.35  
34 1 ASN FFF 52  ? ? 80.18   -42.09  
35 1 ASP FFF 61  ? ? -37.58  -37.13  
36 1 PRO FFF 117 ? ? -69.59  88.30   
37 1 PRO FFF 124 ? ? -55.61  -179.29 
38 1 SER FFF 125 ? ? -141.11 -43.63  
39 1 ASP FFF 142 ? ? 55.00   74.41   
40 1 ASN FFF 174 ? ? 30.75   62.39   
41 1 HIS FFF 201 ? ? -164.25 99.71   
42 1 VAL FFF 206 ? ? -144.19 45.98   
43 1 ASN GGG 28  ? ? -107.81 -96.92  
44 1 ASN GGG 52  ? ? 79.55   -42.49  
45 1 ASP GGG 61  ? ? -38.47  -37.21  
46 1 ASP GGG 142 ? ? -5.06   93.30   
47 1 ASN GGG 174 ? ? 31.55   63.31   
48 1 HIS GGG 201 ? ? -164.83 103.65  
49 1 VAL GGG 206 ? ? -141.17 43.86   
50 1 ALA GGG 211 ? ? -154.39 87.03   
51 1 LEU HHH 18  ? ? -176.27 134.14  
52 1 SER HHH 30  ? ? -67.47  6.59    
53 1 ASP HHH 102 ? ? 75.46   -42.55  
54 1 ASN HHH 104 ? ? 73.11   -148.65 
55 1 ASP HHH 106 ? ? -123.05 -63.70  
56 1 LYS HHH 153 ? ? -141.28 -40.96  
57 1 ASP HHH 154 ? ? -150.38 81.09   
58 1 PRO HHH 157 ? ? -4.84   69.46   
59 1 GLU HHH 158 ? ? 164.54  116.71  
60 1 ASN III 28  ? ? -112.93 -93.57  
61 1 ASN III 52  ? ? 80.25   -42.88  
62 1 ASP III 61  ? ? -37.81  -36.26  
63 1 LEU III 184 ? ? 174.49  179.25  
64 1 PRO JJJ 14  ? ? -41.98  150.64  
65 1 LEU JJJ 18  ? ? -174.65 135.51  
66 1 THR JJJ 28  ? ? -68.15  71.83   
67 1 ASP JJJ 102 ? ? 72.63   -36.00  
68 1 ASN JJJ 104 ? ? 79.93   -149.20 
69 1 ASP JJJ 154 ? ? 41.22   73.97   
70 1 ASN KKK 28  ? ? -113.58 -92.04  
71 1 ASN KKK 52  ? ? 80.18   -43.40  
72 1 LYS KKK 97  ? ? 39.90   59.09   
73 1 SER KKK 141 ? ? -137.43 -42.35  
74 1 SER KKK 169 ? ? -112.62 -167.65 
75 1 LEU LLL 18  ? ? -170.98 134.44  
76 1 THR LLL 28  ? ? -68.52  73.62   
77 1 ASP LLL 102 ? ? 70.73   -36.66  
78 1 ASN LLL 104 ? ? 80.02   -149.18 
79 1 ASP LLL 154 ? ? 41.11   74.34   
80 1 LYS LLL 216 ? ? -142.17 41.53   
81 1 ASN MMM 28  ? ? -113.35 -91.68  
82 1 PRO MMM 41  ? ? -36.14  131.11  
83 1 ASN MMM 52  ? ? 79.79   -42.10  
84 1 PRO NNN 14  ? ? -42.42  150.32  
85 1 LEU NNN 18  ? ? -175.10 133.67  
86 1 ASP NNN 102 ? ? 79.52   -43.91  
87 1 ASN NNN 104 ? ? 71.97   -151.93 
88 1 PRO YYY 14  ? ? -41.99  150.32  
89 1 LEU YYY 18  ? ? -175.86 134.72  
90 1 THR YYY 28  ? ? -68.96  74.47   
91 1 ASP YYY 102 ? ? 77.91   -47.53  
92 1 ASN YYY 104 ? ? 67.80   -147.15 
93 1 ASP YYY 154 ? ? 43.74   70.25   
94 1 ASN YYY 165 ? ? 74.92   68.11   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 AAA VAL 24  ? CG1 ? A VAL 7   CG1 
2   1 Y 1 AAA VAL 24  ? CG2 ? A VAL 7   CG2 
3   1 Y 1 AAA GLU 25  ? CG  ? A GLU 8   CG  
4   1 Y 1 AAA GLU 25  ? CD  ? A GLU 8   CD  
5   1 Y 1 AAA GLU 25  ? OE1 ? A GLU 8   OE1 
6   1 Y 1 AAA GLU 25  ? OE2 ? A GLU 8   OE2 
7   1 Y 1 AAA GLU 28  ? CG  ? A GLU 11  CG  
8   1 Y 1 AAA GLU 28  ? CD  ? A GLU 11  CD  
9   1 Y 1 AAA GLU 28  ? OE1 ? A GLU 11  OE1 
10  1 Y 1 AAA GLU 28  ? OE2 ? A GLU 11  OE2 
11  1 Y 1 AAA ASP 34  ? CG  ? A ASP 17  CG  
12  1 Y 1 AAA ASP 34  ? OD1 ? A ASP 17  OD1 
13  1 Y 1 AAA ASP 34  ? OD2 ? A ASP 17  OD2 
14  1 Y 1 AAA ASN 91  ? CG  ? A ASN 74  CG  
15  1 Y 1 AAA ASN 91  ? OD1 ? A ASN 74  OD1 
16  1 Y 1 AAA ASN 91  ? ND2 ? A ASN 74  ND2 
17  1 Y 1 AAA ASN 98  ? CG  ? A ASN 81  CG  
18  1 Y 1 AAA ASN 98  ? OD1 ? A ASN 81  OD1 
19  1 Y 1 AAA ASN 98  ? ND2 ? A ASN 81  ND2 
20  1 Y 1 AAA ARG 206 ? NE  ? A ARG 189 NE  
21  1 Y 1 AAA ARG 206 ? CZ  ? A ARG 189 CZ  
22  1 Y 1 AAA ARG 206 ? NH1 ? A ARG 189 NH1 
23  1 Y 1 AAA ARG 206 ? NH2 ? A ARG 189 NH2 
24  1 Y 1 AAA GLU 208 ? CG  ? A GLU 191 CG  
25  1 Y 1 AAA GLU 208 ? CD  ? A GLU 191 CD  
26  1 Y 1 AAA GLU 208 ? OE1 ? A GLU 191 OE1 
27  1 Y 1 AAA GLU 208 ? OE2 ? A GLU 191 OE2 
28  1 Y 1 AAA LYS 288 ? CG  ? A LYS 271 CG  
29  1 Y 1 AAA LYS 288 ? CD  ? A LYS 271 CD  
30  1 Y 1 AAA LYS 288 ? CE  ? A LYS 271 CE  
31  1 Y 1 AAA LYS 288 ? NZ  ? A LYS 271 NZ  
32  1 Y 1 AAA ASN 289 ? CG  ? A ASN 272 CG  
33  1 Y 1 AAA ASN 289 ? OD1 ? A ASN 272 OD1 
34  1 Y 1 AAA ASN 289 ? ND2 ? A ASN 272 ND2 
35  1 Y 1 BBB VAL 24  ? CG1 ? B VAL 7   CG1 
36  1 Y 1 BBB VAL 24  ? CG2 ? B VAL 7   CG2 
37  1 Y 1 BBB VAL 33  ? CG1 ? B VAL 16  CG1 
38  1 Y 1 BBB VAL 33  ? CG2 ? B VAL 16  CG2 
39  1 Y 1 BBB ASN 91  ? CG  ? B ASN 74  CG  
40  1 Y 1 BBB ASN 91  ? OD1 ? B ASN 74  OD1 
41  1 Y 1 BBB ASN 91  ? ND2 ? B ASN 74  ND2 
42  1 Y 1 BBB LYS 288 ? CG  ? B LYS 271 CG  
43  1 Y 1 BBB LYS 288 ? CD  ? B LYS 271 CD  
44  1 Y 1 BBB LYS 288 ? CE  ? B LYS 271 CE  
45  1 Y 1 BBB LYS 288 ? NZ  ? B LYS 271 NZ  
46  1 Y 1 CCC GLU 25  ? CG  ? C GLU 8   CG  
47  1 Y 1 CCC GLU 25  ? CD  ? C GLU 8   CD  
48  1 Y 1 CCC GLU 25  ? OE1 ? C GLU 8   OE1 
49  1 Y 1 CCC GLU 25  ? OE2 ? C GLU 8   OE2 
50  1 Y 1 CCC VAL 33  ? CG1 ? C VAL 16  CG1 
51  1 Y 1 CCC VAL 33  ? CG2 ? C VAL 16  CG2 
52  1 Y 1 CCC ARG 286 ? CG  ? C ARG 269 CG  
53  1 Y 1 CCC ARG 286 ? CD  ? C ARG 269 CD  
54  1 Y 1 CCC ARG 286 ? NE  ? C ARG 269 NE  
55  1 Y 1 CCC ARG 286 ? CZ  ? C ARG 269 CZ  
56  1 Y 1 CCC ARG 286 ? NH1 ? C ARG 269 NH1 
57  1 Y 1 CCC ARG 286 ? NH2 ? C ARG 269 NH2 
58  1 Y 1 CCC LYS 288 ? CG  ? C LYS 271 CG  
59  1 Y 1 CCC LYS 288 ? CD  ? C LYS 271 CD  
60  1 Y 1 CCC LYS 288 ? CE  ? C LYS 271 CE  
61  1 Y 1 CCC LYS 288 ? NZ  ? C LYS 271 NZ  
62  1 Y 1 CCC ASN 289 ? CG  ? C ASN 272 CG  
63  1 Y 1 CCC ASN 289 ? OD1 ? C ASN 272 OD1 
64  1 Y 1 CCC ASN 289 ? ND2 ? C ASN 272 ND2 
65  1 Y 1 DDD VAL 24  ? CG1 ? D VAL 7   CG1 
66  1 Y 1 DDD VAL 24  ? CG2 ? D VAL 7   CG2 
67  1 Y 1 DDD GLU 25  ? CG  ? D GLU 8   CG  
68  1 Y 1 DDD GLU 25  ? CD  ? D GLU 8   CD  
69  1 Y 1 DDD GLU 25  ? OE1 ? D GLU 8   OE1 
70  1 Y 1 DDD GLU 25  ? OE2 ? D GLU 8   OE2 
71  1 Y 1 DDD ASN 91  ? CG  ? D ASN 74  CG  
72  1 Y 1 DDD ASN 91  ? OD1 ? D ASN 74  OD1 
73  1 Y 1 DDD ASN 91  ? ND2 ? D ASN 74  ND2 
74  1 Y 1 DDD ASN 98  ? CG  ? D ASN 81  CG  
75  1 Y 1 DDD ASN 98  ? OD1 ? D ASN 81  OD1 
76  1 Y 1 DDD ASN 98  ? ND2 ? D ASN 81  ND2 
77  1 Y 1 DDD ARG 286 ? CG  ? D ARG 269 CG  
78  1 Y 1 DDD ARG 286 ? CD  ? D ARG 269 CD  
79  1 Y 1 DDD ARG 286 ? NE  ? D ARG 269 NE  
80  1 Y 1 DDD ARG 286 ? CZ  ? D ARG 269 CZ  
81  1 Y 1 DDD ARG 286 ? NH1 ? D ARG 269 NH1 
82  1 Y 1 DDD ARG 286 ? NH2 ? D ARG 269 NH2 
83  1 Y 1 DDD LYS 288 ? CG  ? D LYS 271 CG  
84  1 Y 1 DDD LYS 288 ? CD  ? D LYS 271 CD  
85  1 Y 1 DDD LYS 288 ? CE  ? D LYS 271 CE  
86  1 Y 1 DDD LYS 288 ? NZ  ? D LYS 271 NZ  
87  1 Y 1 DDD ASN 289 ? CG  ? D ASN 272 CG  
88  1 Y 1 DDD ASN 289 ? OD1 ? D ASN 272 OD1 
89  1 Y 1 DDD ASN 289 ? ND2 ? D ASN 272 ND2 
90  1 Y 1 EEE MET 21  ? CG  ? E MET 4   CG  
91  1 Y 1 EEE MET 21  ? SD  ? E MET 4   SD  
92  1 Y 1 EEE MET 21  ? CE  ? E MET 4   CE  
93  1 Y 1 EEE VAL 24  ? CG1 ? E VAL 7   CG1 
94  1 Y 1 EEE VAL 24  ? CG2 ? E VAL 7   CG2 
95  1 Y 1 EEE GLU 28  ? CG  ? E GLU 11  CG  
96  1 Y 1 EEE GLU 28  ? CD  ? E GLU 11  CD  
97  1 Y 1 EEE GLU 28  ? OE1 ? E GLU 11  OE1 
98  1 Y 1 EEE GLU 28  ? OE2 ? E GLU 11  OE2 
99  1 Y 1 EEE ILE 99  ? CG1 ? E ILE 82  CG1 
100 1 Y 1 EEE ILE 99  ? CG2 ? E ILE 82  CG2 
101 1 Y 1 EEE ILE 99  ? CD1 ? E ILE 82  CD1 
102 1 Y 1 EEE ARG 286 ? CG  ? E ARG 269 CG  
103 1 Y 1 EEE ARG 286 ? CD  ? E ARG 269 CD  
104 1 Y 1 EEE ARG 286 ? NE  ? E ARG 269 NE  
105 1 Y 1 EEE ARG 286 ? CZ  ? E ARG 269 CZ  
106 1 Y 1 EEE ARG 286 ? NH1 ? E ARG 269 NH1 
107 1 Y 1 EEE ARG 286 ? NH2 ? E ARG 269 NH2 
108 1 Y 1 EEE LYS 288 ? CG  ? E LYS 271 CG  
109 1 Y 1 EEE LYS 288 ? CD  ? E LYS 271 CD  
110 1 Y 1 EEE LYS 288 ? CE  ? E LYS 271 CE  
111 1 Y 1 EEE LYS 288 ? NZ  ? E LYS 271 NZ  
112 1 Y 1 EEE ASN 289 ? CG  ? E ASN 272 CG  
113 1 Y 1 EEE ASN 289 ? OD1 ? E ASN 272 OD1 
114 1 Y 1 EEE ASN 289 ? ND2 ? E ASN 272 ND2 
115 1 Y 1 FFF ARG 17  ? CG  ? F ARG 17  CG  
116 1 Y 1 FFF ARG 17  ? CD  ? F ARG 17  CD  
117 1 Y 1 FFF ARG 17  ? NE  ? F ARG 17  NE  
118 1 Y 1 FFF ARG 17  ? CZ  ? F ARG 17  CZ  
119 1 Y 1 FFF ARG 17  ? NH1 ? F ARG 17  NH1 
120 1 Y 1 FFF ARG 17  ? NH2 ? F ARG 17  NH2 
121 1 Y 1 FFF THR 43  ? CG2 ? F THR 43  CG2 
122 1 Y 1 FFF LYS 114 ? CG  ? F LYS 114 CG  
123 1 Y 1 FFF LYS 114 ? CD  ? F LYS 114 CD  
124 1 Y 1 FFF LYS 114 ? CE  ? F LYS 114 CE  
125 1 Y 1 FFF LYS 114 ? NZ  ? F LYS 114 NZ  
126 1 Y 1 FFF LYS 133 ? CG  ? F LYS 133 CG  
127 1 Y 1 FFF LYS 133 ? CD  ? F LYS 133 CD  
128 1 Y 1 FFF LYS 133 ? CE  ? F LYS 133 CE  
129 1 Y 1 FFF LYS 133 ? NZ  ? F LYS 133 NZ  
130 1 Y 1 FFF PHE 143 ? CG  ? F PHE 143 CG  
131 1 Y 1 FFF PHE 143 ? CD1 ? F PHE 143 CD1 
132 1 Y 1 FFF PHE 143 ? CD2 ? F PHE 143 CD2 
133 1 Y 1 FFF PHE 143 ? CE1 ? F PHE 143 CE1 
134 1 Y 1 FFF PHE 143 ? CE2 ? F PHE 143 CE2 
135 1 Y 1 FFF PHE 143 ? CZ  ? F PHE 143 CZ  
136 1 Y 1 FFF TYR 144 ? CG  ? F TYR 144 CG  
137 1 Y 1 FFF TYR 144 ? CD1 ? F TYR 144 CD1 
138 1 Y 1 FFF TYR 144 ? CD2 ? F TYR 144 CD2 
139 1 Y 1 FFF TYR 144 ? CE1 ? F TYR 144 CE1 
140 1 Y 1 FFF TYR 144 ? CE2 ? F TYR 144 CE2 
141 1 Y 1 FFF TYR 144 ? CZ  ? F TYR 144 CZ  
142 1 Y 1 FFF TYR 144 ? OH  ? F TYR 144 OH  
143 1 Y 1 FFF LYS 167 ? CG  ? F LYS 167 CG  
144 1 Y 1 FFF LYS 167 ? CD  ? F LYS 167 CD  
145 1 Y 1 FFF LYS 167 ? CE  ? F LYS 167 CE  
146 1 Y 1 FFF LYS 167 ? NZ  ? F LYS 167 NZ  
147 1 Y 1 FFF LYS 170 ? CG  ? F LYS 170 CG  
148 1 Y 1 FFF LYS 170 ? CD  ? F LYS 170 CD  
149 1 Y 1 FFF LYS 170 ? CE  ? F LYS 170 CE  
150 1 Y 1 FFF LYS 170 ? NZ  ? F LYS 170 NZ  
151 1 Y 1 FFF GLN 171 ? CG  ? F GLN 171 CG  
152 1 Y 1 FFF GLN 171 ? CD  ? F GLN 171 CD  
153 1 Y 1 FFF GLN 171 ? OE1 ? F GLN 171 OE1 
154 1 Y 1 FFF GLN 171 ? NE2 ? F GLN 171 NE2 
155 1 Y 1 FFF LYS 175 ? CG  ? F LYS 175 CG  
156 1 Y 1 FFF LYS 175 ? CD  ? F LYS 175 CD  
157 1 Y 1 FFF LYS 175 ? CE  ? F LYS 175 CE  
158 1 Y 1 FFF LYS 175 ? NZ  ? F LYS 175 NZ  
159 1 Y 1 FFF TYR 195 ? CG  ? F TYR 195 CG  
160 1 Y 1 FFF TYR 195 ? CD1 ? F TYR 195 CD1 
161 1 Y 1 FFF TYR 195 ? CD2 ? F TYR 195 CD2 
162 1 Y 1 FFF TYR 195 ? CE1 ? F TYR 195 CE1 
163 1 Y 1 FFF TYR 195 ? CE2 ? F TYR 195 CE2 
164 1 Y 1 FFF TYR 195 ? CZ  ? F TYR 195 CZ  
165 1 Y 1 FFF TYR 195 ? OH  ? F TYR 195 OH  
166 1 Y 1 FFF GLN 198 ? CG  ? F GLN 198 CG  
167 1 Y 1 FFF GLN 198 ? CD  ? F GLN 198 CD  
168 1 Y 1 FFF GLN 198 ? OE1 ? F GLN 198 OE1 
169 1 Y 1 FFF GLN 198 ? NE2 ? F GLN 198 NE2 
170 1 Y 1 FFF GLU 207 ? CG  ? F GLU 207 CG  
171 1 Y 1 FFF GLU 207 ? CD  ? F GLU 207 CD  
172 1 Y 1 FFF GLU 207 ? OE1 ? F GLU 207 OE1 
173 1 Y 1 FFF GLU 207 ? OE2 ? F GLU 207 OE2 
174 1 Y 1 FFF LYS 208 ? CG  ? F LYS 208 CG  
175 1 Y 1 FFF LYS 208 ? CD  ? F LYS 208 CD  
176 1 Y 1 FFF LYS 208 ? CE  ? F LYS 208 CE  
177 1 Y 1 FFF LYS 208 ? NZ  ? F LYS 208 NZ  
178 1 Y 1 GGG THR 43  ? CG2 ? G THR 43  CG2 
179 1 Y 1 GGG ASP 61  ? CG  ? G ASP 61  CG  
180 1 Y 1 GGG ASP 61  ? OD1 ? G ASP 61  OD1 
181 1 Y 1 GGG ASP 61  ? OD2 ? G ASP 61  OD2 
182 1 Y 1 GGG LYS 114 ? CG  ? G LYS 114 CG  
183 1 Y 1 GGG LYS 114 ? CD  ? G LYS 114 CD  
184 1 Y 1 GGG LYS 114 ? CE  ? G LYS 114 CE  
185 1 Y 1 GGG LYS 114 ? NZ  ? G LYS 114 NZ  
186 1 Y 1 GGG LEU 136 ? CG  ? G LEU 136 CG  
187 1 Y 1 GGG LEU 136 ? CD1 ? G LEU 136 CD1 
188 1 Y 1 GGG LEU 136 ? CD2 ? G LEU 136 CD2 
189 1 Y 1 GGG ILE 140 ? CG1 ? G ILE 140 CG1 
190 1 Y 1 GGG ILE 140 ? CG2 ? G ILE 140 CG2 
191 1 Y 1 GGG ILE 140 ? CD1 ? G ILE 140 CD1 
192 1 Y 1 GGG ASP 142 ? CG  ? G ASP 142 CG  
193 1 Y 1 GGG ASP 142 ? OD1 ? G ASP 142 OD1 
194 1 Y 1 GGG ASP 142 ? OD2 ? G ASP 142 OD2 
195 1 Y 1 GGG PHE 143 ? CG  ? G PHE 143 CG  
196 1 Y 1 GGG PHE 143 ? CD1 ? G PHE 143 CD1 
197 1 Y 1 GGG PHE 143 ? CD2 ? G PHE 143 CD2 
198 1 Y 1 GGG PHE 143 ? CE1 ? G PHE 143 CE1 
199 1 Y 1 GGG PHE 143 ? CE2 ? G PHE 143 CE2 
200 1 Y 1 GGG PHE 143 ? CZ  ? G PHE 143 CZ  
201 1 Y 1 GGG TYR 144 ? CG  ? G TYR 144 CG  
202 1 Y 1 GGG TYR 144 ? CD1 ? G TYR 144 CD1 
203 1 Y 1 GGG TYR 144 ? CD2 ? G TYR 144 CD2 
204 1 Y 1 GGG TYR 144 ? CE1 ? G TYR 144 CE1 
205 1 Y 1 GGG TYR 144 ? CE2 ? G TYR 144 CE2 
206 1 Y 1 GGG TYR 144 ? CZ  ? G TYR 144 CZ  
207 1 Y 1 GGG TYR 144 ? OH  ? G TYR 144 OH  
208 1 Y 1 GGG LYS 167 ? CG  ? G LYS 167 CG  
209 1 Y 1 GGG LYS 167 ? CD  ? G LYS 167 CD  
210 1 Y 1 GGG LYS 167 ? CE  ? G LYS 167 CE  
211 1 Y 1 GGG LYS 167 ? NZ  ? G LYS 167 NZ  
212 1 Y 1 GGG LYS 170 ? CG  ? G LYS 170 CG  
213 1 Y 1 GGG LYS 170 ? CD  ? G LYS 170 CD  
214 1 Y 1 GGG LYS 170 ? CE  ? G LYS 170 CE  
215 1 Y 1 GGG LYS 170 ? NZ  ? G LYS 170 NZ  
216 1 Y 1 GGG GLN 171 ? CG  ? G GLN 171 CG  
217 1 Y 1 GGG GLN 171 ? CD  ? G GLN 171 CD  
218 1 Y 1 GGG GLN 171 ? OE1 ? G GLN 171 OE1 
219 1 Y 1 GGG GLN 171 ? NE2 ? G GLN 171 NE2 
220 1 Y 1 GGG ASN 174 ? CG  ? G ASN 174 CG  
221 1 Y 1 GGG ASN 174 ? OD1 ? G ASN 174 OD1 
222 1 Y 1 GGG ASN 174 ? ND2 ? G ASN 174 ND2 
223 1 Y 1 GGG LYS 175 ? CG  ? G LYS 175 CG  
224 1 Y 1 GGG LYS 175 ? CD  ? G LYS 175 CD  
225 1 Y 1 GGG LYS 175 ? CE  ? G LYS 175 CE  
226 1 Y 1 GGG LYS 175 ? NZ  ? G LYS 175 NZ  
227 1 Y 1 GGG TYR 195 ? CG  ? G TYR 195 CG  
228 1 Y 1 GGG TYR 195 ? CD1 ? G TYR 195 CD1 
229 1 Y 1 GGG TYR 195 ? CD2 ? G TYR 195 CD2 
230 1 Y 1 GGG TYR 195 ? CE1 ? G TYR 195 CE1 
231 1 Y 1 GGG TYR 195 ? CE2 ? G TYR 195 CE2 
232 1 Y 1 GGG TYR 195 ? CZ  ? G TYR 195 CZ  
233 1 Y 1 GGG TYR 195 ? OH  ? G TYR 195 OH  
234 1 Y 1 GGG GLN 198 ? CG  ? G GLN 198 CG  
235 1 Y 1 GGG GLN 198 ? CD  ? G GLN 198 CD  
236 1 Y 1 GGG GLN 198 ? OE1 ? G GLN 198 OE1 
237 1 Y 1 GGG GLN 198 ? NE2 ? G GLN 198 NE2 
238 1 Y 1 GGG GLU 202 ? CG  ? G GLU 202 CG  
239 1 Y 1 GGG GLU 202 ? CD  ? G GLU 202 CD  
240 1 Y 1 GGG GLU 202 ? OE1 ? G GLU 202 OE1 
241 1 Y 1 GGG GLU 202 ? OE2 ? G GLU 202 OE2 
242 1 Y 1 GGG GLU 207 ? CG  ? G GLU 207 CG  
243 1 Y 1 GGG GLU 207 ? CD  ? G GLU 207 CD  
244 1 Y 1 GGG GLU 207 ? OE1 ? G GLU 207 OE1 
245 1 Y 1 GGG GLU 207 ? OE2 ? G GLU 207 OE2 
246 1 Y 1 GGG LYS 208 ? CG  ? G LYS 208 CG  
247 1 Y 1 GGG LYS 208 ? CD  ? G LYS 208 CD  
248 1 Y 1 GGG LYS 208 ? CE  ? G LYS 208 CE  
249 1 Y 1 GGG LYS 208 ? NZ  ? G LYS 208 NZ  
250 1 Y 1 HHH GLU 1   ? CG  ? H GLU 1   CG  
251 1 Y 1 HHH GLU 1   ? CD  ? H GLU 1   CD  
252 1 Y 1 HHH GLU 1   ? OE1 ? H GLU 1   OE1 
253 1 Y 1 HHH GLU 1   ? OE2 ? H GLU 1   OE2 
254 1 Y 1 HHH LYS 43  ? CG  ? H LYS 43  CG  
255 1 Y 1 HHH LYS 43  ? CD  ? H LYS 43  CD  
256 1 Y 1 HHH LYS 43  ? CE  ? H LYS 43  CE  
257 1 Y 1 HHH LYS 43  ? NZ  ? H LYS 43  NZ  
258 1 Y 1 HHH THR 56  ? CG2 ? H THR 56  CG2 
259 1 Y 1 HHH ARG 76  ? NH1 ? H ARG 76  NH1 
260 1 Y 1 HHH ARG 76  ? NH2 ? H ARG 76  NH2 
261 1 Y 1 HHH TYR 95  ? OH  ? H TYR 95  OH  
262 1 Y 1 HHH LYS 122 ? CG  ? H LYS 122 CG  
263 1 Y 1 HHH LYS 122 ? CD  ? H LYS 122 CD  
264 1 Y 1 HHH LYS 122 ? CE  ? H LYS 122 CE  
265 1 Y 1 HHH LYS 122 ? NZ  ? H LYS 122 NZ  
266 1 Y 1 HHH LYS 153 ? CG  ? H LYS 148 CG  
267 1 Y 1 HHH LYS 153 ? CD  ? H LYS 148 CD  
268 1 Y 1 HHH LYS 153 ? CE  ? H LYS 148 CE  
269 1 Y 1 HHH LYS 153 ? NZ  ? H LYS 148 NZ  
270 1 Y 1 HHH GLN 181 ? CG  ? H GLN 176 CG  
271 1 Y 1 HHH GLN 181 ? CD  ? H GLN 176 CD  
272 1 Y 1 HHH GLN 181 ? OE1 ? H GLN 176 OE1 
273 1 Y 1 HHH GLN 181 ? NE2 ? H GLN 176 NE2 
274 1 Y 1 III ASN 28  ? CG  ? I ASN 28  CG  
275 1 Y 1 III ASN 28  ? OD1 ? I ASN 28  OD1 
276 1 Y 1 III ASN 28  ? ND2 ? I ASN 28  ND2 
277 1 Y 1 III THR 43  ? CG2 ? I THR 43  CG2 
278 1 Y 1 III ASN 132 ? CG  ? I ASN 132 CG  
279 1 Y 1 III ASN 132 ? OD1 ? I ASN 132 OD1 
280 1 Y 1 III ASN 132 ? ND2 ? I ASN 132 ND2 
281 1 Y 1 III LYS 133 ? CG  ? I LYS 133 CG  
282 1 Y 1 III LYS 133 ? CD  ? I LYS 133 CD  
283 1 Y 1 III LYS 133 ? CE  ? I LYS 133 CE  
284 1 Y 1 III LYS 133 ? NZ  ? I LYS 133 NZ  
285 1 Y 1 III GLU 164 ? CG  ? I GLU 164 CG  
286 1 Y 1 III GLU 164 ? CD  ? I GLU 164 CD  
287 1 Y 1 III GLU 164 ? OE1 ? I GLU 164 OE1 
288 1 Y 1 III GLU 164 ? OE2 ? I GLU 164 OE2 
289 1 Y 1 III THR 165 ? OG1 ? I THR 165 OG1 
290 1 Y 1 III THR 165 ? CG2 ? I THR 165 CG2 
291 1 Y 1 III THR 166 ? OG1 ? I THR 166 OG1 
292 1 Y 1 III THR 166 ? CG2 ? I THR 166 CG2 
293 1 Y 1 III LYS 167 ? CG  ? I LYS 167 CG  
294 1 Y 1 III LYS 167 ? CD  ? I LYS 167 CD  
295 1 Y 1 III LYS 167 ? CE  ? I LYS 167 CE  
296 1 Y 1 III LYS 167 ? NZ  ? I LYS 167 NZ  
297 1 Y 1 III TYR 181 ? CG  ? I TYR 181 CG  
298 1 Y 1 III TYR 181 ? CD1 ? I TYR 181 CD1 
299 1 Y 1 III TYR 181 ? CD2 ? I TYR 181 CD2 
300 1 Y 1 III TYR 181 ? CE1 ? I TYR 181 CE1 
301 1 Y 1 III TYR 181 ? CE2 ? I TYR 181 CE2 
302 1 Y 1 III TYR 181 ? CZ  ? I TYR 181 CZ  
303 1 Y 1 III TYR 181 ? OH  ? I TYR 181 OH  
304 1 Y 1 III LEU 182 ? CG  ? I LEU 182 CG  
305 1 Y 1 III LEU 182 ? CD1 ? I LEU 182 CD1 
306 1 Y 1 III LEU 182 ? CD2 ? I LEU 182 CD2 
307 1 Y 1 JJJ GLU 1   ? CG  ? J GLU 1   CG  
308 1 Y 1 JJJ GLU 1   ? CD  ? J GLU 1   CD  
309 1 Y 1 JJJ GLU 1   ? OE1 ? J GLU 1   OE1 
310 1 Y 1 JJJ GLU 1   ? OE2 ? J GLU 1   OE2 
311 1 Y 1 JJJ LYS 13  ? CG  ? J LYS 13  CG  
312 1 Y 1 JJJ LYS 13  ? CD  ? J LYS 13  CD  
313 1 Y 1 JJJ LYS 13  ? CE  ? J LYS 13  CE  
314 1 Y 1 JJJ LYS 13  ? NZ  ? J LYS 13  NZ  
315 1 Y 1 JJJ LYS 43  ? CG  ? J LYS 43  CG  
316 1 Y 1 JJJ LYS 43  ? CD  ? J LYS 43  CD  
317 1 Y 1 JJJ LYS 43  ? CE  ? J LYS 43  CE  
318 1 Y 1 JJJ LYS 43  ? NZ  ? J LYS 43  NZ  
319 1 Y 1 JJJ THR 56  ? CG2 ? J THR 56  CG2 
320 1 Y 1 JJJ LYS 65  ? CG  ? J LYS 65  CG  
321 1 Y 1 JJJ LYS 65  ? CD  ? J LYS 65  CD  
322 1 Y 1 JJJ LYS 65  ? CE  ? J LYS 65  CE  
323 1 Y 1 JJJ LYS 65  ? NZ  ? J LYS 65  NZ  
324 1 Y 1 JJJ ARG 76  ? NH1 ? J ARG 76  NH1 
325 1 Y 1 JJJ ARG 76  ? NH2 ? J ARG 76  NH2 
326 1 Y 1 JJJ TYR 95  ? OH  ? J TYR 95  OH  
327 1 Y 1 JJJ LYS 122 ? CG  ? J LYS 122 CG  
328 1 Y 1 JJJ LYS 122 ? CD  ? J LYS 122 CD  
329 1 Y 1 JJJ LYS 122 ? CE  ? J LYS 122 CE  
330 1 Y 1 JJJ LYS 122 ? NZ  ? J LYS 122 NZ  
331 1 Y 1 JJJ VAL 126 ? CG1 ? J VAL 126 CG1 
332 1 Y 1 JJJ VAL 126 ? CG2 ? J VAL 126 CG2 
333 1 Y 1 JJJ LEU 148 ? CG  ? J LEU 143 CG  
334 1 Y 1 JJJ LEU 148 ? CD1 ? J LEU 143 CD1 
335 1 Y 1 JJJ LEU 148 ? CD2 ? J LEU 143 CD2 
336 1 Y 1 JJJ LYS 153 ? CG  ? J LYS 148 CG  
337 1 Y 1 JJJ LYS 153 ? CD  ? J LYS 148 CD  
338 1 Y 1 JJJ LYS 153 ? CE  ? J LYS 148 CE  
339 1 Y 1 JJJ LYS 153 ? NZ  ? J LYS 148 NZ  
340 1 Y 1 JJJ ASP 154 ? CG  ? J ASP 149 CG  
341 1 Y 1 JJJ ASP 154 ? OD1 ? J ASP 149 OD1 
342 1 Y 1 JJJ ASP 154 ? OD2 ? J ASP 149 OD2 
343 1 Y 1 JJJ GLN 181 ? CG  ? J GLN 176 CG  
344 1 Y 1 JJJ GLN 181 ? CD  ? J GLN 176 CD  
345 1 Y 1 JJJ GLN 181 ? OE1 ? J GLN 176 OE1 
346 1 Y 1 JJJ GLN 181 ? NE2 ? J GLN 176 NE2 
347 1 Y 1 JJJ LYS 211 ? CG  ? J LYS 206 CG  
348 1 Y 1 JJJ LYS 211 ? CD  ? J LYS 206 CD  
349 1 Y 1 JJJ LYS 211 ? CE  ? J LYS 206 CE  
350 1 Y 1 JJJ LYS 211 ? NZ  ? J LYS 206 NZ  
351 1 Y 1 JJJ LYS 216 ? CG  ? J LYS 211 CG  
352 1 Y 1 JJJ LYS 216 ? CD  ? J LYS 211 CD  
353 1 Y 1 JJJ LYS 216 ? CE  ? J LYS 211 CE  
354 1 Y 1 JJJ LYS 216 ? NZ  ? J LYS 211 NZ  
355 1 Y 1 JJJ LYS 219 ? CG  ? J LYS 214 CG  
356 1 Y 1 JJJ LYS 219 ? CD  ? J LYS 214 CD  
357 1 Y 1 JJJ LYS 219 ? CE  ? J LYS 214 CE  
358 1 Y 1 JJJ LYS 219 ? NZ  ? J LYS 214 NZ  
359 1 Y 1 KKK THR 43  ? CG2 ? K THR 43  CG2 
360 1 Y 1 KKK SER 57  ? OG  ? K SER 57  OG  
361 1 Y 1 KKK GLU 82  ? CG  ? K GLU 82  CG  
362 1 Y 1 KKK GLU 82  ? CD  ? K GLU 82  CD  
363 1 Y 1 KKK GLU 82  ? OE1 ? K GLU 82  OE1 
364 1 Y 1 KKK GLU 82  ? OE2 ? K GLU 82  OE2 
365 1 Y 1 KKK TYR 144 ? CG  ? K TYR 144 CG  
366 1 Y 1 KKK TYR 144 ? CD1 ? K TYR 144 CD1 
367 1 Y 1 KKK TYR 144 ? CD2 ? K TYR 144 CD2 
368 1 Y 1 KKK TYR 144 ? CE1 ? K TYR 144 CE1 
369 1 Y 1 KKK TYR 144 ? CE2 ? K TYR 144 CE2 
370 1 Y 1 KKK TYR 144 ? CZ  ? K TYR 144 CZ  
371 1 Y 1 KKK TYR 144 ? OH  ? K TYR 144 OH  
372 1 Y 1 KKK LYS 167 ? CG  ? K LYS 167 CG  
373 1 Y 1 KKK LYS 167 ? CD  ? K LYS 167 CD  
374 1 Y 1 KKK LYS 167 ? CE  ? K LYS 167 CE  
375 1 Y 1 KKK LYS 167 ? NZ  ? K LYS 167 NZ  
376 1 Y 1 KKK LYS 170 ? CG  ? K LYS 170 CG  
377 1 Y 1 KKK LYS 170 ? CD  ? K LYS 170 CD  
378 1 Y 1 KKK LYS 170 ? CE  ? K LYS 170 CE  
379 1 Y 1 KKK LYS 170 ? NZ  ? K LYS 170 NZ  
380 1 Y 1 LLL GLU 1   ? CG  ? L GLU 1   CG  
381 1 Y 1 LLL GLU 1   ? CD  ? L GLU 1   CD  
382 1 Y 1 LLL GLU 1   ? OE1 ? L GLU 1   OE1 
383 1 Y 1 LLL GLU 1   ? OE2 ? L GLU 1   OE2 
384 1 Y 1 LLL LYS 13  ? CG  ? L LYS 13  CG  
385 1 Y 1 LLL LYS 13  ? CD  ? L LYS 13  CD  
386 1 Y 1 LLL LYS 13  ? CE  ? L LYS 13  CE  
387 1 Y 1 LLL LYS 13  ? NZ  ? L LYS 13  NZ  
388 1 Y 1 LLL LYS 43  ? CG  ? L LYS 43  CG  
389 1 Y 1 LLL LYS 43  ? CD  ? L LYS 43  CD  
390 1 Y 1 LLL LYS 43  ? CE  ? L LYS 43  CE  
391 1 Y 1 LLL LYS 43  ? NZ  ? L LYS 43  NZ  
392 1 Y 1 LLL THR 56  ? CG2 ? L THR 56  CG2 
393 1 Y 1 LLL LYS 65  ? CG  ? L LYS 65  CG  
394 1 Y 1 LLL LYS 65  ? CD  ? L LYS 65  CD  
395 1 Y 1 LLL LYS 65  ? CE  ? L LYS 65  CE  
396 1 Y 1 LLL LYS 65  ? NZ  ? L LYS 65  NZ  
397 1 Y 1 LLL ARG 76  ? NH1 ? L ARG 76  NH1 
398 1 Y 1 LLL ARG 76  ? NH2 ? L ARG 76  NH2 
399 1 Y 1 LLL TYR 95  ? OH  ? L TYR 95  OH  
400 1 Y 1 LLL LYS 122 ? CG  ? L LYS 122 CG  
401 1 Y 1 LLL LYS 122 ? CD  ? L LYS 122 CD  
402 1 Y 1 LLL LYS 122 ? CE  ? L LYS 122 CE  
403 1 Y 1 LLL LYS 122 ? NZ  ? L LYS 122 NZ  
404 1 Y 1 LLL LYS 153 ? CG  ? L LYS 148 CG  
405 1 Y 1 LLL LYS 153 ? CD  ? L LYS 148 CD  
406 1 Y 1 LLL LYS 153 ? CE  ? L LYS 148 CE  
407 1 Y 1 LLL LYS 153 ? NZ  ? L LYS 148 NZ  
408 1 Y 1 LLL PHE 176 ? CG  ? L PHE 171 CG  
409 1 Y 1 LLL PHE 176 ? CD1 ? L PHE 171 CD1 
410 1 Y 1 LLL PHE 176 ? CD2 ? L PHE 171 CD2 
411 1 Y 1 LLL PHE 176 ? CE1 ? L PHE 171 CE1 
412 1 Y 1 LLL PHE 176 ? CE2 ? L PHE 171 CE2 
413 1 Y 1 LLL PHE 176 ? CZ  ? L PHE 171 CZ  
414 1 Y 1 LLL LEU 180 ? CG  ? L LEU 175 CG  
415 1 Y 1 LLL LEU 180 ? CD1 ? L LEU 175 CD1 
416 1 Y 1 LLL LEU 180 ? CD2 ? L LEU 175 CD2 
417 1 Y 1 LLL LYS 211 ? CG  ? L LYS 206 CG  
418 1 Y 1 LLL LYS 211 ? CD  ? L LYS 206 CD  
419 1 Y 1 LLL LYS 211 ? CE  ? L LYS 206 CE  
420 1 Y 1 LLL LYS 211 ? NZ  ? L LYS 206 NZ  
421 1 Y 1 MMM ARG 17  ? CG  ? M ARG 17  CG  
422 1 Y 1 MMM ARG 17  ? CD  ? M ARG 17  CD  
423 1 Y 1 MMM ARG 17  ? NE  ? M ARG 17  NE  
424 1 Y 1 MMM ARG 17  ? CZ  ? M ARG 17  CZ  
425 1 Y 1 MMM ARG 17  ? NH1 ? M ARG 17  NH1 
426 1 Y 1 MMM ARG 17  ? NH2 ? M ARG 17  NH2 
427 1 Y 1 MMM THR 43  ? CG2 ? M THR 43  CG2 
428 1 Y 1 NNN GLU 1   ? CG  ? N GLU 1   CG  
429 1 Y 1 NNN GLU 1   ? CD  ? N GLU 1   CD  
430 1 Y 1 NNN GLU 1   ? OE1 ? N GLU 1   OE1 
431 1 Y 1 NNN GLU 1   ? OE2 ? N GLU 1   OE2 
432 1 Y 1 NNN LYS 43  ? CG  ? N LYS 43  CG  
433 1 Y 1 NNN LYS 43  ? CD  ? N LYS 43  CD  
434 1 Y 1 NNN LYS 43  ? CE  ? N LYS 43  CE  
435 1 Y 1 NNN LYS 43  ? NZ  ? N LYS 43  NZ  
436 1 Y 1 NNN THR 56  ? CG2 ? N THR 56  CG2 
437 1 Y 1 NNN ARG 76  ? NH1 ? N ARG 76  NH1 
438 1 Y 1 NNN ARG 76  ? NH2 ? N ARG 76  NH2 
439 1 Y 1 NNN TYR 95  ? OH  ? N TYR 95  OH  
440 1 Y 1 YYY GLU 1   ? CG  ? O GLU 1   CG  
441 1 Y 1 YYY GLU 1   ? CD  ? O GLU 1   CD  
442 1 Y 1 YYY GLU 1   ? OE1 ? O GLU 1   OE1 
443 1 Y 1 YYY GLU 1   ? OE2 ? O GLU 1   OE2 
444 1 Y 1 YYY LYS 43  ? CG  ? O LYS 43  CG  
445 1 Y 1 YYY LYS 43  ? CD  ? O LYS 43  CD  
446 1 Y 1 YYY LYS 43  ? CE  ? O LYS 43  CE  
447 1 Y 1 YYY LYS 43  ? NZ  ? O LYS 43  NZ  
448 1 Y 1 YYY THR 56  ? CG2 ? O THR 56  CG2 
449 1 Y 1 YYY LYS 65  ? CG  ? O LYS 65  CG  
450 1 Y 1 YYY LYS 65  ? CD  ? O LYS 65  CD  
451 1 Y 1 YYY LYS 65  ? CE  ? O LYS 65  CE  
452 1 Y 1 YYY LYS 65  ? NZ  ? O LYS 65  NZ  
453 1 Y 1 YYY ARG 76  ? NH1 ? O ARG 76  NH1 
454 1 Y 1 YYY ARG 76  ? NH2 ? O ARG 76  NH2 
455 1 Y 1 YYY TYR 95  ? OH  ? O TYR 95  OH  
456 1 Y 1 YYY LYS 122 ? CG  ? O LYS 122 CG  
457 1 Y 1 YYY LYS 122 ? CD  ? O LYS 122 CD  
458 1 Y 1 YYY LYS 122 ? CE  ? O LYS 122 CE  
459 1 Y 1 YYY LYS 122 ? NZ  ? O LYS 122 NZ  
460 1 Y 1 YYY SER 166 ? OG  ? O SER 161 OG  
461 1 Y 1 YYY GLN 181 ? CG  ? O GLN 176 CG  
462 1 Y 1 YYY GLN 181 ? CD  ? O GLN 176 CD  
463 1 Y 1 YYY GLN 181 ? OE1 ? O GLN 176 OE1 
464 1 Y 1 YYY GLN 181 ? NE2 ? O GLN 176 NE2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 AAA GLY 18  ? A GLY 1   
2    1 Y 1 AAA SER 19  ? A SER 2   
3    1 Y 1 AAA HIS 20  ? A HIS 3   
4    1 Y 1 AAA MET 21  ? A MET 4   
5    1 Y 1 AAA GLY 22  ? A GLY 5   
6    1 Y 1 AAA GLY 23  ? A GLY 6   
7    1 Y 1 AAA GLU 92  ? A GLU 75  
8    1 Y 1 AAA ASP 93  ? A ASP 76  
9    1 Y 1 AAA LEU 94  ? A LEU 77  
10   1 Y 1 AAA THR 95  ? A THR 78  
11   1 Y 1 AAA CYS 96  ? A CYS 79  
12   1 Y 1 AAA GLY 97  ? A GLY 80  
13   1 Y 1 BBB GLY 18  ? B GLY 1   
14   1 Y 1 BBB SER 19  ? B SER 2   
15   1 Y 1 BBB HIS 20  ? B HIS 3   
16   1 Y 1 BBB MET 21  ? B MET 4   
17   1 Y 1 BBB GLY 22  ? B GLY 5   
18   1 Y 1 BBB GLY 23  ? B GLY 6   
19   1 Y 1 BBB GLU 92  ? B GLU 75  
20   1 Y 1 BBB ASP 93  ? B ASP 76  
21   1 Y 1 BBB LEU 94  ? B LEU 77  
22   1 Y 1 BBB THR 95  ? B THR 78  
23   1 Y 1 BBB CYS 96  ? B CYS 79  
24   1 Y 1 BBB GLY 97  ? B GLY 80  
25   1 Y 1 BBB ASN 98  ? B ASN 81  
26   1 Y 1 BBB ASN 289 ? B ASN 272 
27   1 Y 1 CCC GLY 18  ? C GLY 1   
28   1 Y 1 CCC SER 19  ? C SER 2   
29   1 Y 1 CCC HIS 20  ? C HIS 3   
30   1 Y 1 CCC MET 21  ? C MET 4   
31   1 Y 1 CCC GLY 22  ? C GLY 5   
32   1 Y 1 CCC GLY 23  ? C GLY 6   
33   1 Y 1 CCC VAL 24  ? C VAL 7   
34   1 Y 1 CCC ASN 91  ? C ASN 74  
35   1 Y 1 CCC GLU 92  ? C GLU 75  
36   1 Y 1 CCC ASP 93  ? C ASP 76  
37   1 Y 1 CCC LEU 94  ? C LEU 77  
38   1 Y 1 CCC THR 95  ? C THR 78  
39   1 Y 1 CCC CYS 96  ? C CYS 79  
40   1 Y 1 CCC GLY 97  ? C GLY 80  
41   1 Y 1 CCC ASN 98  ? C ASN 81  
42   1 Y 1 DDD GLY 18  ? D GLY 1   
43   1 Y 1 DDD SER 19  ? D SER 2   
44   1 Y 1 DDD HIS 20  ? D HIS 3   
45   1 Y 1 DDD MET 21  ? D MET 4   
46   1 Y 1 DDD GLY 22  ? D GLY 5   
47   1 Y 1 DDD GLY 23  ? D GLY 6   
48   1 Y 1 DDD GLU 92  ? D GLU 75  
49   1 Y 1 DDD ASP 93  ? D ASP 76  
50   1 Y 1 DDD LEU 94  ? D LEU 77  
51   1 Y 1 DDD THR 95  ? D THR 78  
52   1 Y 1 DDD CYS 96  ? D CYS 79  
53   1 Y 1 EEE GLY 18  ? E GLY 1   
54   1 Y 1 EEE SER 19  ? E SER 2   
55   1 Y 1 EEE HIS 20  ? E HIS 3   
56   1 Y 1 EEE GLU 92  ? E GLU 75  
57   1 Y 1 EEE ASP 93  ? E ASP 76  
58   1 Y 1 EEE LEU 94  ? E LEU 77  
59   1 Y 1 EEE THR 95  ? E THR 78  
60   1 Y 1 EEE CYS 96  ? E CYS 79  
61   1 Y 1 EEE GLY 97  ? E GLY 80  
62   1 Y 1 EEE ASN 98  ? E ASN 81  
63   1 Y 1 FFF GLN 1   ? F GLN 1   
64   1 Y 1 FFF GLU 127 ? F GLU 127 
65   1 Y 1 FFF GLU 128 ? F GLU 128 
66   1 Y 1 FFF LEU 129 ? F LEU 129 
67   1 Y 1 FFF GLN 130 ? F GLN 130 
68   1 Y 1 FFF ALA 131 ? F ALA 131 
69   1 Y 1 FFF LYS 153 ? F LYS 153 
70   1 Y 1 FFF ALA 154 ? F ALA 154 
71   1 Y 1 FFF ASP 155 ? F ASP 155 
72   1 Y 1 FFF GLY 156 ? F GLY 156 
73   1 Y 1 FFF SER 157 ? F SER 157 
74   1 Y 1 FFF PRO 158 ? F PRO 158 
75   1 Y 1 FFF VAL 159 ? F VAL 159 
76   1 Y 1 FFF LYS 160 ? F LYS 160 
77   1 Y 1 FFF GLU 187 ? F GLU 187 
78   1 Y 1 FFF GLN 188 ? F GLN 188 
79   1 Y 1 FFF TRP 189 ? F TRP 189 
80   1 Y 1 FFF LYS 190 ? F LYS 190 
81   1 Y 1 FFF SER 191 ? F SER 191 
82   1 Y 1 FFF HIS 192 ? F HIS 192 
83   1 Y 1 FFF ARG 193 ? F ARG 193 
84   1 Y 1 GGG GLN 1   ? G GLN 1   
85   1 Y 1 GGG SER 2   ? G SER 2   
86   1 Y 1 GGG VAL 3   ? G VAL 3   
87   1 Y 1 GGG SER 125 ? G SER 125 
88   1 Y 1 GGG SER 126 ? G SER 126 
89   1 Y 1 GGG GLU 127 ? G GLU 127 
90   1 Y 1 GGG GLU 128 ? G GLU 128 
91   1 Y 1 GGG LEU 129 ? G LEU 129 
92   1 Y 1 GGG GLN 130 ? G GLN 130 
93   1 Y 1 GGG ALA 131 ? G ALA 131 
94   1 Y 1 GGG ASN 132 ? G ASN 132 
95   1 Y 1 GGG LYS 133 ? G LYS 133 
96   1 Y 1 GGG VAL 150 ? G VAL 150 
97   1 Y 1 GGG ALA 151 ? G ALA 151 
98   1 Y 1 GGG TRP 152 ? G TRP 152 
99   1 Y 1 GGG LYS 153 ? G LYS 153 
100  1 Y 1 GGG ALA 154 ? G ALA 154 
101  1 Y 1 GGG ASP 155 ? G ASP 155 
102  1 Y 1 GGG GLY 156 ? G GLY 156 
103  1 Y 1 GGG SER 157 ? G SER 157 
104  1 Y 1 GGG PRO 158 ? G PRO 158 
105  1 Y 1 GGG VAL 159 ? G VAL 159 
106  1 Y 1 GGG LYS 160 ? G LYS 160 
107  1 Y 1 GGG ALA 161 ? G ALA 161 
108  1 Y 1 GGG SER 183 ? G SER 183 
109  1 Y 1 GGG LEU 184 ? G LEU 184 
110  1 Y 1 GGG THR 185 ? G THR 185 
111  1 Y 1 GGG PRO 186 ? G PRO 186 
112  1 Y 1 GGG GLU 187 ? G GLU 187 
113  1 Y 1 GGG GLN 188 ? G GLN 188 
114  1 Y 1 GGG TRP 189 ? G TRP 189 
115  1 Y 1 GGG LYS 190 ? G LYS 190 
116  1 Y 1 GGG SER 191 ? G SER 191 
117  1 Y 1 GGG HIS 192 ? G HIS 192 
118  1 Y 1 GGG ARG 193 ? G ARG 193 
119  1 Y 1 GGG SER 194 ? G SER 194 
120  1 Y 1 HHH PHE 132 ? H PHE 127 
121  1 Y 1 HHH PRO 133 ? H PRO 128 
122  1 Y 1 HHH LEU 134 ? H LEU 129 
123  1 Y 1 HHH ALA 135 ? H ALA 130 
124  1 Y 1 HHH PRO 136 ? H PRO 131 
125  1 Y 1 HHH SER 137 ? H SER 132 
126  1 Y 1 HHH SER 138 ? H SER 133 
127  1 Y 1 HHH LYS 139 ? H LYS 134 
128  1 Y 1 HHH SER 140 ? H SER 135 
129  1 Y 1 HHH THR 141 ? H THR 136 
130  1 Y 1 HHH SER 142 ? H SER 137 
131  1 Y 1 HHH GLY 143 ? H GLY 138 
132  1 Y 1 HHH GLY 144 ? H GLY 139 
133  1 Y 1 HHH THR 145 ? H THR 140 
134  1 Y 1 HHH ALA 146 ? H ALA 141 
135  1 Y 1 HHH ALA 147 ? H ALA 142 
136  1 Y 1 HHH LEU 148 ? H LEU 143 
137  1 Y 1 HHH GLY 149 ? H GLY 144 
138  1 Y 1 HHH CYS 150 ? H CYS 145 
139  1 Y 1 HHH LEU 151 ? H LEU 146 
140  1 Y 1 HHH VAL 160 ? H VAL 155 
141  1 Y 1 HHH THR 161 ? H THR 156 
142  1 Y 1 HHH VAL 162 ? H VAL 157 
143  1 Y 1 HHH SER 163 ? H SER 158 
144  1 Y 1 HHH TRP 164 ? H TRP 159 
145  1 Y 1 HHH ASN 165 ? H ASN 160 
146  1 Y 1 HHH SER 166 ? H SER 161 
147  1 Y 1 HHH GLY 167 ? H GLY 162 
148  1 Y 1 HHH ALA 168 ? H ALA 163 
149  1 Y 1 HHH LEU 169 ? H LEU 164 
150  1 Y 1 HHH THR 170 ? H THR 165 
151  1 Y 1 HHH SER 171 ? H SER 166 
152  1 Y 1 HHH GLY 172 ? H GLY 167 
153  1 Y 1 HHH VAL 173 ? H VAL 168 
154  1 Y 1 HHH HIS 174 ? H HIS 169 
155  1 Y 1 HHH SER 190 ? H SER 185 
156  1 Y 1 HHH VAL 191 ? H VAL 186 
157  1 Y 1 HHH VAL 192 ? H VAL 187 
158  1 Y 1 HHH THR 193 ? H THR 188 
159  1 Y 1 HHH VAL 194 ? H VAL 189 
160  1 Y 1 HHH PRO 195 ? H PRO 190 
161  1 Y 1 HHH SER 196 ? H SER 191 
162  1 Y 1 HHH SER 197 ? H SER 192 
163  1 Y 1 HHH SER 198 ? H SER 193 
164  1 Y 1 HHH LEU 199 ? H LEU 194 
165  1 Y 1 HHH GLY 200 ? H GLY 195 
166  1 Y 1 HHH THR 201 ? H THR 196 
167  1 Y 1 HHH GLN 202 ? H GLN 197 
168  1 Y 1 HHH THR 203 ? H THR 198 
169  1 Y 1 HHH TYR 204 ? H TYR 199 
170  1 Y 1 HHH ILE 205 ? H ILE 200 
171  1 Y 1 HHH CYS 206 ? H CYS 201 
172  1 Y 1 HHH ASN 207 ? H ASN 202 
173  1 Y 1 HHH VAL 208 ? H VAL 203 
174  1 Y 1 HHH ASN 209 ? H ASN 204 
175  1 Y 1 HHH HIS 210 ? H HIS 205 
176  1 Y 1 HHH LYS 211 ? H LYS 206 
177  1 Y 1 HHH PRO 212 ? H PRO 207 
178  1 Y 1 HHH SER 213 ? H SER 208 
179  1 Y 1 HHH ASN 214 ? H ASN 209 
180  1 Y 1 HHH THR 215 ? H THR 210 
181  1 Y 1 HHH LYS 216 ? H LYS 211 
182  1 Y 1 HHH VAL 217 ? H VAL 212 
183  1 Y 1 HHH ASP 218 ? H ASP 213 
184  1 Y 1 HHH LYS 219 ? H LYS 214 
185  1 Y 1 HHH LYS 220 ? H LYS 215 
186  1 Y 1 HHH VAL 221 ? H VAL 216 
187  1 Y 1 HHH GLU 222 ? H GLU 217 
188  1 Y 1 HHH PRO 223 ? H PRO 218 
189  1 Y 1 HHH LYS 224 ? H LYS 219 
190  1 Y 1 HHH SER 225 ? H SER 220 
191  1 Y 1 HHH CYS 226 ? H CYS 221 
192  1 Y 1 HHH ASP 227 ? H ASP 222 
193  1 Y 1 HHH LYS 228 ? H LYS 223 
194  1 Y 1 HHH THR 229 ? H THR 224 
195  1 Y 1 HHH HIS 230 ? H HIS 225 
196  1 Y 1 HHH THR 231 ? H THR 226 
197  1 Y 1 HHH CYS 232 ? H CYS 227 
198  1 Y 1 HHH PRO 233 ? H PRO 228 
199  1 Y 1 HHH PRO 234 ? H PRO 229 
200  1 Y 1 HHH CYS 235 ? H CYS 230 
201  1 Y 1 HHH PRO 236 ? H PRO 231 
202  1 Y 1 HHH ALA 237 ? H ALA 232 
203  1 Y 1 HHH PRO 238 ? H PRO 233 
204  1 Y 1 HHH GLU 239 ? H GLU 234 
205  1 Y 1 HHH LEU 240 ? H LEU 235 
206  1 Y 1 HHH LEU 241 ? H LEU 236 
207  1 Y 1 HHH GLY 242 ? H GLY 237 
208  1 Y 1 HHH GLY 243 ? H GLY 238 
209  1 Y 1 HHH PRO 244 ? H PRO 239 
210  1 Y 1 HHH SER 245 ? H SER 240 
211  1 Y 1 HHH VAL 246 ? H VAL 241 
212  1 Y 1 HHH PHE 247 ? H PHE 242 
213  1 Y 1 HHH LEU 248 ? H LEU 243 
214  1 Y 1 HHH PHE 249 ? H PHE 244 
215  1 Y 1 HHH PRO 250 ? H PRO 245 
216  1 Y 1 HHH PRO 251 ? H PRO 246 
217  1 Y 1 HHH LYS 252 ? H LYS 247 
218  1 Y 1 HHH PRO 253 ? H PRO 248 
219  1 Y 1 HHH LYS 254 ? H LYS 249 
220  1 Y 1 HHH ASP 255 ? H ASP 250 
221  1 Y 1 HHH THR 256 ? H THR 251 
222  1 Y 1 HHH LEU 257 ? H LEU 252 
223  1 Y 1 HHH MET 258 ? H MET 253 
224  1 Y 1 HHH ILE 259 ? H ILE 254 
225  1 Y 1 HHH SER 260 ? H SER 255 
226  1 Y 1 HHH ARG 261 ? H ARG 256 
227  1 Y 1 HHH THR 262 ? H THR 257 
228  1 Y 1 HHH PRO 263 ? H PRO 258 
229  1 Y 1 HHH GLU 264 ? H GLU 259 
230  1 Y 1 HHH VAL 265 ? H VAL 260 
231  1 Y 1 HHH THR 266 ? H THR 261 
232  1 Y 1 HHH CYS 267 ? H CYS 262 
233  1 Y 1 HHH VAL 268 ? H VAL 263 
234  1 Y 1 HHH VAL 269 ? H VAL 264 
235  1 Y 1 HHH VAL 270 ? H VAL 265 
236  1 Y 1 HHH ASP 271 ? H ASP 266 
237  1 Y 1 HHH VAL 272 ? H VAL 267 
238  1 Y 1 HHH SER 273 ? H SER 268 
239  1 Y 1 HHH HIS 274 ? H HIS 269 
240  1 Y 1 HHH GLU 275 ? H GLU 270 
241  1 Y 1 HHH ASP 276 ? H ASP 271 
242  1 Y 1 HHH PRO 277 ? H PRO 272 
243  1 Y 1 HHH GLU 278 ? H GLU 273 
244  1 Y 1 HHH VAL 279 ? H VAL 274 
245  1 Y 1 HHH LYS 280 ? H LYS 275 
246  1 Y 1 HHH PHE 281 ? H PHE 276 
247  1 Y 1 HHH ASN 282 ? H ASN 277 
248  1 Y 1 HHH TRP 283 ? H TRP 278 
249  1 Y 1 HHH TYR 284 ? H TYR 279 
250  1 Y 1 HHH VAL 285 ? H VAL 280 
251  1 Y 1 HHH ASP 286 ? H ASP 281 
252  1 Y 1 HHH GLY 287 ? H GLY 282 
253  1 Y 1 HHH VAL 288 ? H VAL 283 
254  1 Y 1 HHH GLU 289 ? H GLU 284 
255  1 Y 1 HHH VAL 290 ? H VAL 285 
256  1 Y 1 HHH HIS 291 ? H HIS 286 
257  1 Y 1 HHH ASN 292 ? H ASN 287 
258  1 Y 1 HHH ALA 293 ? H ALA 288 
259  1 Y 1 HHH LYS 294 ? H LYS 289 
260  1 Y 1 HHH THR 295 ? H THR 290 
261  1 Y 1 HHH LYS 296 ? H LYS 291 
262  1 Y 1 HHH PRO 297 ? H PRO 292 
263  1 Y 1 HHH ARG 298 ? H ARG 293 
264  1 Y 1 HHH GLU 299 ? H GLU 294 
265  1 Y 1 HHH GLU 300 ? H GLU 295 
266  1 Y 1 HHH GLN 301 ? H GLN 296 
267  1 Y 1 HHH TYR 302 ? H TYR 297 
268  1 Y 1 HHH ASN 303 ? H ASN 298 
269  1 Y 1 HHH SER 304 ? H SER 299 
270  1 Y 1 HHH THR 305 ? H THR 300 
271  1 Y 1 HHH TYR 306 ? H TYR 301 
272  1 Y 1 HHH ARG 307 ? H ARG 302 
273  1 Y 1 HHH VAL 308 ? H VAL 303 
274  1 Y 1 HHH VAL 309 ? H VAL 304 
275  1 Y 1 HHH SER 310 ? H SER 305 
276  1 Y 1 HHH VAL 311 ? H VAL 306 
277  1 Y 1 HHH LEU 312 ? H LEU 307 
278  1 Y 1 HHH THR 313 ? H THR 308 
279  1 Y 1 HHH VAL 314 ? H VAL 309 
280  1 Y 1 HHH LEU 315 ? H LEU 310 
281  1 Y 1 HHH HIS 316 ? H HIS 311 
282  1 Y 1 HHH GLN 317 ? H GLN 312 
283  1 Y 1 HHH ASP 318 ? H ASP 313 
284  1 Y 1 HHH TRP 319 ? H TRP 314 
285  1 Y 1 HHH LEU 320 ? H LEU 315 
286  1 Y 1 HHH ASN 321 ? H ASN 316 
287  1 Y 1 HHH GLY 322 ? H GLY 317 
288  1 Y 1 HHH LYS 323 ? H LYS 318 
289  1 Y 1 HHH GLU 324 ? H GLU 319 
290  1 Y 1 HHH TYR 325 ? H TYR 320 
291  1 Y 1 HHH LYS 326 ? H LYS 321 
292  1 Y 1 HHH CYS 327 ? H CYS 322 
293  1 Y 1 HHH LYS 328 ? H LYS 323 
294  1 Y 1 HHH VAL 329 ? H VAL 324 
295  1 Y 1 HHH SER 330 ? H SER 325 
296  1 Y 1 HHH ASN 331 ? H ASN 326 
297  1 Y 1 HHH LYS 332 ? H LYS 327 
298  1 Y 1 HHH ALA 333 ? H ALA 328 
299  1 Y 1 HHH LEU 334 ? H LEU 329 
300  1 Y 1 HHH PRO 335 ? H PRO 330 
301  1 Y 1 HHH ALA 336 ? H ALA 331 
302  1 Y 1 HHH PRO 337 ? H PRO 332 
303  1 Y 1 HHH ILE 338 ? H ILE 333 
304  1 Y 1 HHH GLU 339 ? H GLU 334 
305  1 Y 1 HHH LYS 340 ? H LYS 335 
306  1 Y 1 HHH THR 341 ? H THR 336 
307  1 Y 1 HHH ILE 342 ? H ILE 337 
308  1 Y 1 HHH SER 343 ? H SER 338 
309  1 Y 1 HHH LYS 344 ? H LYS 339 
310  1 Y 1 HHH ALA 345 ? H ALA 340 
311  1 Y 1 HHH LYS 346 ? H LYS 341 
312  1 Y 1 HHH GLY 347 ? H GLY 342 
313  1 Y 1 HHH GLN 348 ? H GLN 343 
314  1 Y 1 HHH PRO 349 ? H PRO 344 
315  1 Y 1 HHH ARG 350 ? H ARG 345 
316  1 Y 1 HHH GLU 351 ? H GLU 346 
317  1 Y 1 HHH PRO 352 ? H PRO 347 
318  1 Y 1 HHH GLN 353 ? H GLN 348 
319  1 Y 1 HHH VAL 354 ? H VAL 349 
320  1 Y 1 HHH TYR 355 ? H TYR 350 
321  1 Y 1 HHH THR 356 ? H THR 351 
322  1 Y 1 HHH LEU 357 ? H LEU 352 
323  1 Y 1 HHH PRO 358 ? H PRO 353 
324  1 Y 1 HHH PRO 359 ? H PRO 354 
325  1 Y 1 HHH SER 360 ? H SER 355 
326  1 Y 1 HHH ARG 361 ? H ARG 356 
327  1 Y 1 HHH ASP 362 ? H ASP 357 
328  1 Y 1 HHH GLU 363 ? H GLU 358 
329  1 Y 1 HHH LEU 364 ? H LEU 359 
330  1 Y 1 HHH THR 365 ? H THR 360 
331  1 Y 1 HHH LYS 366 ? H LYS 361 
332  1 Y 1 HHH ASN 367 ? H ASN 362 
333  1 Y 1 HHH GLN 368 ? H GLN 363 
334  1 Y 1 HHH VAL 369 ? H VAL 364 
335  1 Y 1 HHH SER 370 ? H SER 365 
336  1 Y 1 HHH LEU 371 ? H LEU 366 
337  1 Y 1 HHH THR 372 ? H THR 367 
338  1 Y 1 HHH CYS 373 ? H CYS 368 
339  1 Y 1 HHH LEU 374 ? H LEU 369 
340  1 Y 1 HHH VAL 375 ? H VAL 370 
341  1 Y 1 HHH LYS 376 ? H LYS 371 
342  1 Y 1 HHH GLY 377 ? H GLY 372 
343  1 Y 1 HHH PHE 378 ? H PHE 373 
344  1 Y 1 HHH TYR 379 ? H TYR 374 
345  1 Y 1 HHH PRO 380 ? H PRO 375 
346  1 Y 1 HHH SER 381 ? H SER 376 
347  1 Y 1 HHH ASP 382 ? H ASP 377 
348  1 Y 1 HHH ILE 383 ? H ILE 378 
349  1 Y 1 HHH ALA 384 ? H ALA 379 
350  1 Y 1 HHH VAL 385 ? H VAL 380 
351  1 Y 1 HHH GLU 386 ? H GLU 381 
352  1 Y 1 HHH TRP 387 ? H TRP 382 
353  1 Y 1 HHH GLU 388 ? H GLU 383 
354  1 Y 1 HHH SER 389 ? H SER 384 
355  1 Y 1 HHH ASN 390 ? H ASN 385 
356  1 Y 1 HHH GLY 391 ? H GLY 386 
357  1 Y 1 HHH GLN 392 ? H GLN 387 
358  1 Y 1 HHH PRO 393 ? H PRO 388 
359  1 Y 1 HHH GLU 394 ? H GLU 389 
360  1 Y 1 HHH ASN 395 ? H ASN 390 
361  1 Y 1 HHH ASN 396 ? H ASN 391 
362  1 Y 1 HHH TYR 397 ? H TYR 392 
363  1 Y 1 HHH LYS 398 ? H LYS 393 
364  1 Y 1 HHH THR 399 ? H THR 394 
365  1 Y 1 HHH THR 400 ? H THR 395 
366  1 Y 1 HHH PRO 401 ? H PRO 396 
367  1 Y 1 HHH PRO 402 ? H PRO 397 
368  1 Y 1 HHH VAL 403 ? H VAL 398 
369  1 Y 1 III GLN 1   ? I GLN 1   
370  1 Y 1 III LYS 114 ? I LYS 114 
371  1 Y 1 III ALA 115 ? I ALA 115 
372  1 Y 1 III ASN 116 ? I ASN 116 
373  1 Y 1 III PRO 117 ? I PRO 117 
374  1 Y 1 III THR 118 ? I THR 118 
375  1 Y 1 III VAL 119 ? I VAL 119 
376  1 Y 1 III THR 120 ? I THR 120 
377  1 Y 1 III LEU 121 ? I LEU 121 
378  1 Y 1 III PHE 122 ? I PHE 122 
379  1 Y 1 III PRO 123 ? I PRO 123 
380  1 Y 1 III PRO 124 ? I PRO 124 
381  1 Y 1 III SER 125 ? I SER 125 
382  1 Y 1 III SER 126 ? I SER 126 
383  1 Y 1 III GLU 127 ? I GLU 127 
384  1 Y 1 III GLU 128 ? I GLU 128 
385  1 Y 1 III LEU 129 ? I LEU 129 
386  1 Y 1 III GLN 130 ? I GLN 130 
387  1 Y 1 III ALA 131 ? I ALA 131 
388  1 Y 1 III ILE 140 ? I ILE 140 
389  1 Y 1 III SER 141 ? I SER 141 
390  1 Y 1 III ASP 142 ? I ASP 142 
391  1 Y 1 III PHE 143 ? I PHE 143 
392  1 Y 1 III TYR 144 ? I TYR 144 
393  1 Y 1 III PRO 145 ? I PRO 145 
394  1 Y 1 III GLY 146 ? I GLY 146 
395  1 Y 1 III ALA 147 ? I ALA 147 
396  1 Y 1 III VAL 148 ? I VAL 148 
397  1 Y 1 III THR 149 ? I THR 149 
398  1 Y 1 III VAL 150 ? I VAL 150 
399  1 Y 1 III ALA 151 ? I ALA 151 
400  1 Y 1 III TRP 152 ? I TRP 152 
401  1 Y 1 III LYS 153 ? I LYS 153 
402  1 Y 1 III ALA 154 ? I ALA 154 
403  1 Y 1 III ASP 155 ? I ASP 155 
404  1 Y 1 III GLY 156 ? I GLY 156 
405  1 Y 1 III SER 157 ? I SER 157 
406  1 Y 1 III PRO 158 ? I PRO 158 
407  1 Y 1 III VAL 159 ? I VAL 159 
408  1 Y 1 III LYS 160 ? I LYS 160 
409  1 Y 1 III ALA 161 ? I ALA 161 
410  1 Y 1 III GLY 162 ? I GLY 162 
411  1 Y 1 III LYS 170 ? I LYS 170 
412  1 Y 1 III GLN 171 ? I GLN 171 
413  1 Y 1 III SER 172 ? I SER 172 
414  1 Y 1 III ASN 173 ? I ASN 173 
415  1 Y 1 III ASN 174 ? I ASN 174 
416  1 Y 1 III LYS 175 ? I LYS 175 
417  1 Y 1 III THR 176 ? I THR 176 
418  1 Y 1 III ALA 177 ? I ALA 177 
419  1 Y 1 III GLU 187 ? I GLU 187 
420  1 Y 1 III GLN 188 ? I GLN 188 
421  1 Y 1 III TRP 189 ? I TRP 189 
422  1 Y 1 III LYS 190 ? I LYS 190 
423  1 Y 1 III SER 191 ? I SER 191 
424  1 Y 1 III HIS 192 ? I HIS 192 
425  1 Y 1 III ARG 193 ? I ARG 193 
426  1 Y 1 III SER 194 ? I SER 194 
427  1 Y 1 III TYR 195 ? I TYR 195 
428  1 Y 1 III SER 196 ? I SER 196 
429  1 Y 1 III CYS 197 ? I CYS 197 
430  1 Y 1 III GLN 198 ? I GLN 198 
431  1 Y 1 III VAL 199 ? I VAL 199 
432  1 Y 1 III THR 200 ? I THR 200 
433  1 Y 1 III HIS 201 ? I HIS 201 
434  1 Y 1 III GLU 202 ? I GLU 202 
435  1 Y 1 III GLY 203 ? I GLY 203 
436  1 Y 1 III THR 204 ? I THR 204 
437  1 Y 1 III THR 205 ? I THR 205 
438  1 Y 1 III VAL 206 ? I VAL 206 
439  1 Y 1 III GLU 207 ? I GLU 207 
440  1 Y 1 III LYS 208 ? I LYS 208 
441  1 Y 1 III THR 209 ? I THR 209 
442  1 Y 1 III VAL 210 ? I VAL 210 
443  1 Y 1 III ALA 211 ? I ALA 211 
444  1 Y 1 III PRO 212 ? I PRO 212 
445  1 Y 1 JJJ PRO 133 ? J PRO 128 
446  1 Y 1 JJJ LEU 134 ? J LEU 129 
447  1 Y 1 JJJ ALA 135 ? J ALA 130 
448  1 Y 1 JJJ PRO 136 ? J PRO 131 
449  1 Y 1 JJJ SER 137 ? J SER 132 
450  1 Y 1 JJJ SER 138 ? J SER 133 
451  1 Y 1 JJJ LYS 139 ? J LYS 134 
452  1 Y 1 JJJ SER 140 ? J SER 135 
453  1 Y 1 JJJ THR 141 ? J THR 136 
454  1 Y 1 JJJ SER 142 ? J SER 137 
455  1 Y 1 JJJ GLY 143 ? J GLY 138 
456  1 Y 1 JJJ GLY 144 ? J GLY 139 
457  1 Y 1 JJJ THR 145 ? J THR 140 
458  1 Y 1 JJJ ALA 146 ? J ALA 141 
459  1 Y 1 JJJ SER 166 ? J SER 161 
460  1 Y 1 JJJ GLY 167 ? J GLY 162 
461  1 Y 1 JJJ ALA 168 ? J ALA 163 
462  1 Y 1 JJJ LEU 169 ? J LEU 164 
463  1 Y 1 JJJ THR 170 ? J THR 165 
464  1 Y 1 JJJ SER 171 ? J SER 166 
465  1 Y 1 JJJ GLY 172 ? J GLY 167 
466  1 Y 1 JJJ VAL 173 ? J VAL 168 
467  1 Y 1 JJJ HIS 174 ? J HIS 169 
468  1 Y 1 JJJ VAL 192 ? J VAL 187 
469  1 Y 1 JJJ THR 193 ? J THR 188 
470  1 Y 1 JJJ VAL 194 ? J VAL 189 
471  1 Y 1 JJJ PRO 195 ? J PRO 190 
472  1 Y 1 JJJ SER 196 ? J SER 191 
473  1 Y 1 JJJ SER 197 ? J SER 192 
474  1 Y 1 JJJ SER 198 ? J SER 193 
475  1 Y 1 JJJ LEU 199 ? J LEU 194 
476  1 Y 1 JJJ GLY 200 ? J GLY 195 
477  1 Y 1 JJJ THR 201 ? J THR 196 
478  1 Y 1 JJJ GLN 202 ? J GLN 197 
479  1 Y 1 JJJ THR 203 ? J THR 198 
480  1 Y 1 JJJ TYR 204 ? J TYR 199 
481  1 Y 1 JJJ ILE 205 ? J ILE 200 
482  1 Y 1 JJJ LYS 220 ? J LYS 215 
483  1 Y 1 JJJ VAL 221 ? J VAL 216 
484  1 Y 1 JJJ GLU 222 ? J GLU 217 
485  1 Y 1 JJJ PRO 223 ? J PRO 218 
486  1 Y 1 JJJ LYS 224 ? J LYS 219 
487  1 Y 1 JJJ SER 225 ? J SER 220 
488  1 Y 1 JJJ CYS 226 ? J CYS 221 
489  1 Y 1 JJJ ASP 227 ? J ASP 222 
490  1 Y 1 JJJ LYS 228 ? J LYS 223 
491  1 Y 1 JJJ THR 229 ? J THR 224 
492  1 Y 1 JJJ HIS 230 ? J HIS 225 
493  1 Y 1 JJJ THR 231 ? J THR 226 
494  1 Y 1 JJJ CYS 232 ? J CYS 227 
495  1 Y 1 JJJ PRO 233 ? J PRO 228 
496  1 Y 1 JJJ PRO 234 ? J PRO 229 
497  1 Y 1 JJJ CYS 235 ? J CYS 230 
498  1 Y 1 JJJ PRO 236 ? J PRO 231 
499  1 Y 1 JJJ ALA 237 ? J ALA 232 
500  1 Y 1 JJJ PRO 238 ? J PRO 233 
501  1 Y 1 JJJ GLU 239 ? J GLU 234 
502  1 Y 1 JJJ LEU 240 ? J LEU 235 
503  1 Y 1 JJJ LEU 241 ? J LEU 236 
504  1 Y 1 JJJ GLY 242 ? J GLY 237 
505  1 Y 1 JJJ GLY 243 ? J GLY 238 
506  1 Y 1 JJJ PRO 244 ? J PRO 239 
507  1 Y 1 JJJ SER 245 ? J SER 240 
508  1 Y 1 JJJ VAL 246 ? J VAL 241 
509  1 Y 1 JJJ PHE 247 ? J PHE 242 
510  1 Y 1 JJJ LEU 248 ? J LEU 243 
511  1 Y 1 JJJ PHE 249 ? J PHE 244 
512  1 Y 1 JJJ PRO 250 ? J PRO 245 
513  1 Y 1 JJJ PRO 251 ? J PRO 246 
514  1 Y 1 JJJ LYS 252 ? J LYS 247 
515  1 Y 1 JJJ PRO 253 ? J PRO 248 
516  1 Y 1 JJJ LYS 254 ? J LYS 249 
517  1 Y 1 JJJ ASP 255 ? J ASP 250 
518  1 Y 1 JJJ THR 256 ? J THR 251 
519  1 Y 1 JJJ LEU 257 ? J LEU 252 
520  1 Y 1 JJJ MET 258 ? J MET 253 
521  1 Y 1 JJJ ILE 259 ? J ILE 254 
522  1 Y 1 JJJ SER 260 ? J SER 255 
523  1 Y 1 JJJ ARG 261 ? J ARG 256 
524  1 Y 1 JJJ THR 262 ? J THR 257 
525  1 Y 1 JJJ PRO 263 ? J PRO 258 
526  1 Y 1 JJJ GLU 264 ? J GLU 259 
527  1 Y 1 JJJ VAL 265 ? J VAL 260 
528  1 Y 1 JJJ THR 266 ? J THR 261 
529  1 Y 1 JJJ CYS 267 ? J CYS 262 
530  1 Y 1 JJJ VAL 268 ? J VAL 263 
531  1 Y 1 JJJ VAL 269 ? J VAL 264 
532  1 Y 1 JJJ VAL 270 ? J VAL 265 
533  1 Y 1 JJJ ASP 271 ? J ASP 266 
534  1 Y 1 JJJ VAL 272 ? J VAL 267 
535  1 Y 1 JJJ SER 273 ? J SER 268 
536  1 Y 1 JJJ HIS 274 ? J HIS 269 
537  1 Y 1 JJJ GLU 275 ? J GLU 270 
538  1 Y 1 JJJ ASP 276 ? J ASP 271 
539  1 Y 1 JJJ PRO 277 ? J PRO 272 
540  1 Y 1 JJJ GLU 278 ? J GLU 273 
541  1 Y 1 JJJ VAL 279 ? J VAL 274 
542  1 Y 1 JJJ LYS 280 ? J LYS 275 
543  1 Y 1 JJJ PHE 281 ? J PHE 276 
544  1 Y 1 JJJ ASN 282 ? J ASN 277 
545  1 Y 1 JJJ TRP 283 ? J TRP 278 
546  1 Y 1 JJJ TYR 284 ? J TYR 279 
547  1 Y 1 JJJ VAL 285 ? J VAL 280 
548  1 Y 1 JJJ ASP 286 ? J ASP 281 
549  1 Y 1 JJJ GLY 287 ? J GLY 282 
550  1 Y 1 JJJ VAL 288 ? J VAL 283 
551  1 Y 1 JJJ GLU 289 ? J GLU 284 
552  1 Y 1 JJJ VAL 290 ? J VAL 285 
553  1 Y 1 JJJ HIS 291 ? J HIS 286 
554  1 Y 1 JJJ ASN 292 ? J ASN 287 
555  1 Y 1 JJJ ALA 293 ? J ALA 288 
556  1 Y 1 JJJ LYS 294 ? J LYS 289 
557  1 Y 1 JJJ THR 295 ? J THR 290 
558  1 Y 1 JJJ LYS 296 ? J LYS 291 
559  1 Y 1 JJJ PRO 297 ? J PRO 292 
560  1 Y 1 JJJ ARG 298 ? J ARG 293 
561  1 Y 1 JJJ GLU 299 ? J GLU 294 
562  1 Y 1 JJJ GLU 300 ? J GLU 295 
563  1 Y 1 JJJ GLN 301 ? J GLN 296 
564  1 Y 1 JJJ TYR 302 ? J TYR 297 
565  1 Y 1 JJJ ASN 303 ? J ASN 298 
566  1 Y 1 JJJ SER 304 ? J SER 299 
567  1 Y 1 JJJ THR 305 ? J THR 300 
568  1 Y 1 JJJ TYR 306 ? J TYR 301 
569  1 Y 1 JJJ ARG 307 ? J ARG 302 
570  1 Y 1 JJJ VAL 308 ? J VAL 303 
571  1 Y 1 JJJ VAL 309 ? J VAL 304 
572  1 Y 1 JJJ SER 310 ? J SER 305 
573  1 Y 1 JJJ VAL 311 ? J VAL 306 
574  1 Y 1 JJJ LEU 312 ? J LEU 307 
575  1 Y 1 JJJ THR 313 ? J THR 308 
576  1 Y 1 JJJ VAL 314 ? J VAL 309 
577  1 Y 1 JJJ LEU 315 ? J LEU 310 
578  1 Y 1 JJJ HIS 316 ? J HIS 311 
579  1 Y 1 JJJ GLN 317 ? J GLN 312 
580  1 Y 1 JJJ ASP 318 ? J ASP 313 
581  1 Y 1 JJJ TRP 319 ? J TRP 314 
582  1 Y 1 JJJ LEU 320 ? J LEU 315 
583  1 Y 1 JJJ ASN 321 ? J ASN 316 
584  1 Y 1 JJJ GLY 322 ? J GLY 317 
585  1 Y 1 JJJ LYS 323 ? J LYS 318 
586  1 Y 1 JJJ GLU 324 ? J GLU 319 
587  1 Y 1 JJJ TYR 325 ? J TYR 320 
588  1 Y 1 JJJ LYS 326 ? J LYS 321 
589  1 Y 1 JJJ CYS 327 ? J CYS 322 
590  1 Y 1 JJJ LYS 328 ? J LYS 323 
591  1 Y 1 JJJ VAL 329 ? J VAL 324 
592  1 Y 1 JJJ SER 330 ? J SER 325 
593  1 Y 1 JJJ ASN 331 ? J ASN 326 
594  1 Y 1 JJJ LYS 332 ? J LYS 327 
595  1 Y 1 JJJ ALA 333 ? J ALA 328 
596  1 Y 1 JJJ LEU 334 ? J LEU 329 
597  1 Y 1 JJJ PRO 335 ? J PRO 330 
598  1 Y 1 JJJ ALA 336 ? J ALA 331 
599  1 Y 1 JJJ PRO 337 ? J PRO 332 
600  1 Y 1 JJJ ILE 338 ? J ILE 333 
601  1 Y 1 JJJ GLU 339 ? J GLU 334 
602  1 Y 1 JJJ LYS 340 ? J LYS 335 
603  1 Y 1 JJJ THR 341 ? J THR 336 
604  1 Y 1 JJJ ILE 342 ? J ILE 337 
605  1 Y 1 JJJ SER 343 ? J SER 338 
606  1 Y 1 JJJ LYS 344 ? J LYS 339 
607  1 Y 1 JJJ ALA 345 ? J ALA 340 
608  1 Y 1 JJJ LYS 346 ? J LYS 341 
609  1 Y 1 JJJ GLY 347 ? J GLY 342 
610  1 Y 1 JJJ GLN 348 ? J GLN 343 
611  1 Y 1 JJJ PRO 349 ? J PRO 344 
612  1 Y 1 JJJ ARG 350 ? J ARG 345 
613  1 Y 1 JJJ GLU 351 ? J GLU 346 
614  1 Y 1 JJJ PRO 352 ? J PRO 347 
615  1 Y 1 JJJ GLN 353 ? J GLN 348 
616  1 Y 1 JJJ VAL 354 ? J VAL 349 
617  1 Y 1 JJJ TYR 355 ? J TYR 350 
618  1 Y 1 JJJ THR 356 ? J THR 351 
619  1 Y 1 JJJ LEU 357 ? J LEU 352 
620  1 Y 1 JJJ PRO 358 ? J PRO 353 
621  1 Y 1 JJJ PRO 359 ? J PRO 354 
622  1 Y 1 JJJ SER 360 ? J SER 355 
623  1 Y 1 JJJ ARG 361 ? J ARG 356 
624  1 Y 1 JJJ ASP 362 ? J ASP 357 
625  1 Y 1 JJJ GLU 363 ? J GLU 358 
626  1 Y 1 JJJ LEU 364 ? J LEU 359 
627  1 Y 1 JJJ THR 365 ? J THR 360 
628  1 Y 1 JJJ LYS 366 ? J LYS 361 
629  1 Y 1 JJJ ASN 367 ? J ASN 362 
630  1 Y 1 JJJ GLN 368 ? J GLN 363 
631  1 Y 1 JJJ VAL 369 ? J VAL 364 
632  1 Y 1 JJJ SER 370 ? J SER 365 
633  1 Y 1 JJJ LEU 371 ? J LEU 366 
634  1 Y 1 JJJ THR 372 ? J THR 367 
635  1 Y 1 JJJ CYS 373 ? J CYS 368 
636  1 Y 1 JJJ LEU 374 ? J LEU 369 
637  1 Y 1 JJJ VAL 375 ? J VAL 370 
638  1 Y 1 JJJ LYS 376 ? J LYS 371 
639  1 Y 1 JJJ GLY 377 ? J GLY 372 
640  1 Y 1 JJJ PHE 378 ? J PHE 373 
641  1 Y 1 JJJ TYR 379 ? J TYR 374 
642  1 Y 1 JJJ PRO 380 ? J PRO 375 
643  1 Y 1 JJJ SER 381 ? J SER 376 
644  1 Y 1 JJJ ASP 382 ? J ASP 377 
645  1 Y 1 JJJ ILE 383 ? J ILE 378 
646  1 Y 1 JJJ ALA 384 ? J ALA 379 
647  1 Y 1 JJJ VAL 385 ? J VAL 380 
648  1 Y 1 JJJ GLU 386 ? J GLU 381 
649  1 Y 1 JJJ TRP 387 ? J TRP 382 
650  1 Y 1 JJJ GLU 388 ? J GLU 383 
651  1 Y 1 JJJ SER 389 ? J SER 384 
652  1 Y 1 JJJ ASN 390 ? J ASN 385 
653  1 Y 1 JJJ GLY 391 ? J GLY 386 
654  1 Y 1 JJJ GLN 392 ? J GLN 387 
655  1 Y 1 JJJ PRO 393 ? J PRO 388 
656  1 Y 1 JJJ GLU 394 ? J GLU 389 
657  1 Y 1 JJJ ASN 395 ? J ASN 390 
658  1 Y 1 JJJ ASN 396 ? J ASN 391 
659  1 Y 1 JJJ TYR 397 ? J TYR 392 
660  1 Y 1 JJJ LYS 398 ? J LYS 393 
661  1 Y 1 JJJ THR 399 ? J THR 394 
662  1 Y 1 JJJ THR 400 ? J THR 395 
663  1 Y 1 JJJ PRO 401 ? J PRO 396 
664  1 Y 1 JJJ PRO 402 ? J PRO 397 
665  1 Y 1 JJJ VAL 403 ? J VAL 398 
666  1 Y 1 KKK GLN 1   ? K GLN 1   
667  1 Y 1 KKK LYS 114 ? K LYS 114 
668  1 Y 1 KKK ALA 115 ? K ALA 115 
669  1 Y 1 KKK ASN 116 ? K ASN 116 
670  1 Y 1 KKK PRO 117 ? K PRO 117 
671  1 Y 1 KKK THR 118 ? K THR 118 
672  1 Y 1 KKK VAL 119 ? K VAL 119 
673  1 Y 1 KKK THR 120 ? K THR 120 
674  1 Y 1 KKK LEU 121 ? K LEU 121 
675  1 Y 1 KKK PHE 122 ? K PHE 122 
676  1 Y 1 KKK PRO 123 ? K PRO 123 
677  1 Y 1 KKK PRO 124 ? K PRO 124 
678  1 Y 1 KKK SER 125 ? K SER 125 
679  1 Y 1 KKK SER 126 ? K SER 126 
680  1 Y 1 KKK GLU 127 ? K GLU 127 
681  1 Y 1 KKK GLU 128 ? K GLU 128 
682  1 Y 1 KKK LEU 129 ? K LEU 129 
683  1 Y 1 KKK GLN 130 ? K GLN 130 
684  1 Y 1 KKK ALA 131 ? K ALA 131 
685  1 Y 1 KKK ASN 132 ? K ASN 132 
686  1 Y 1 KKK LYS 133 ? K LYS 133 
687  1 Y 1 KKK ALA 134 ? K ALA 134 
688  1 Y 1 KKK THR 135 ? K THR 135 
689  1 Y 1 KKK LEU 136 ? K LEU 136 
690  1 Y 1 KKK VAL 137 ? K VAL 137 
691  1 Y 1 KKK CYS 138 ? K CYS 138 
692  1 Y 1 KKK THR 149 ? K THR 149 
693  1 Y 1 KKK VAL 150 ? K VAL 150 
694  1 Y 1 KKK ALA 151 ? K ALA 151 
695  1 Y 1 KKK TRP 152 ? K TRP 152 
696  1 Y 1 KKK LYS 153 ? K LYS 153 
697  1 Y 1 KKK ALA 154 ? K ALA 154 
698  1 Y 1 KKK ASP 155 ? K ASP 155 
699  1 Y 1 KKK GLY 156 ? K GLY 156 
700  1 Y 1 KKK SER 157 ? K SER 157 
701  1 Y 1 KKK PRO 158 ? K PRO 158 
702  1 Y 1 KKK VAL 159 ? K VAL 159 
703  1 Y 1 KKK LYS 160 ? K LYS 160 
704  1 Y 1 KKK ALA 161 ? K ALA 161 
705  1 Y 1 KKK GLY 162 ? K GLY 162 
706  1 Y 1 KKK VAL 163 ? K VAL 163 
707  1 Y 1 KKK GLU 164 ? K GLU 164 
708  1 Y 1 KKK GLN 171 ? K GLN 171 
709  1 Y 1 KKK SER 172 ? K SER 172 
710  1 Y 1 KKK ASN 173 ? K ASN 173 
711  1 Y 1 KKK ASN 174 ? K ASN 174 
712  1 Y 1 KKK LYS 175 ? K LYS 175 
713  1 Y 1 KKK THR 176 ? K THR 176 
714  1 Y 1 KKK SER 183 ? K SER 183 
715  1 Y 1 KKK LEU 184 ? K LEU 184 
716  1 Y 1 KKK THR 185 ? K THR 185 
717  1 Y 1 KKK PRO 186 ? K PRO 186 
718  1 Y 1 KKK GLU 187 ? K GLU 187 
719  1 Y 1 KKK GLN 188 ? K GLN 188 
720  1 Y 1 KKK TRP 189 ? K TRP 189 
721  1 Y 1 KKK LYS 190 ? K LYS 190 
722  1 Y 1 KKK SER 191 ? K SER 191 
723  1 Y 1 KKK HIS 192 ? K HIS 192 
724  1 Y 1 KKK ARG 193 ? K ARG 193 
725  1 Y 1 KKK SER 194 ? K SER 194 
726  1 Y 1 KKK TYR 195 ? K TYR 195 
727  1 Y 1 KKK SER 196 ? K SER 196 
728  1 Y 1 KKK CYS 197 ? K CYS 197 
729  1 Y 1 KKK GLN 198 ? K GLN 198 
730  1 Y 1 KKK VAL 199 ? K VAL 199 
731  1 Y 1 KKK THR 200 ? K THR 200 
732  1 Y 1 KKK HIS 201 ? K HIS 201 
733  1 Y 1 KKK GLU 202 ? K GLU 202 
734  1 Y 1 KKK GLY 203 ? K GLY 203 
735  1 Y 1 KKK THR 204 ? K THR 204 
736  1 Y 1 KKK THR 205 ? K THR 205 
737  1 Y 1 KKK VAL 206 ? K VAL 206 
738  1 Y 1 KKK GLU 207 ? K GLU 207 
739  1 Y 1 KKK LYS 208 ? K LYS 208 
740  1 Y 1 KKK THR 209 ? K THR 209 
741  1 Y 1 KKK VAL 210 ? K VAL 210 
742  1 Y 1 KKK ALA 211 ? K ALA 211 
743  1 Y 1 KKK PRO 212 ? K PRO 212 
744  1 Y 1 LLL PHE 132 ? L PHE 127 
745  1 Y 1 LLL PRO 133 ? L PRO 128 
746  1 Y 1 LLL LEU 134 ? L LEU 129 
747  1 Y 1 LLL ALA 135 ? L ALA 130 
748  1 Y 1 LLL PRO 136 ? L PRO 131 
749  1 Y 1 LLL SER 137 ? L SER 132 
750  1 Y 1 LLL SER 138 ? L SER 133 
751  1 Y 1 LLL LYS 139 ? L LYS 134 
752  1 Y 1 LLL SER 140 ? L SER 135 
753  1 Y 1 LLL THR 141 ? L THR 136 
754  1 Y 1 LLL SER 142 ? L SER 137 
755  1 Y 1 LLL GLY 143 ? L GLY 138 
756  1 Y 1 LLL GLY 144 ? L GLY 139 
757  1 Y 1 LLL THR 145 ? L THR 140 
758  1 Y 1 LLL ALA 146 ? L ALA 141 
759  1 Y 1 LLL ALA 147 ? L ALA 142 
760  1 Y 1 LLL LEU 148 ? L LEU 143 
761  1 Y 1 LLL GLY 149 ? L GLY 144 
762  1 Y 1 LLL SER 163 ? L SER 158 
763  1 Y 1 LLL TRP 164 ? L TRP 159 
764  1 Y 1 LLL ASN 165 ? L ASN 160 
765  1 Y 1 LLL SER 166 ? L SER 161 
766  1 Y 1 LLL GLY 167 ? L GLY 162 
767  1 Y 1 LLL ALA 168 ? L ALA 163 
768  1 Y 1 LLL LEU 169 ? L LEU 164 
769  1 Y 1 LLL THR 170 ? L THR 165 
770  1 Y 1 LLL SER 171 ? L SER 166 
771  1 Y 1 LLL GLY 172 ? L GLY 167 
772  1 Y 1 LLL VAL 173 ? L VAL 168 
773  1 Y 1 LLL THR 193 ? L THR 188 
774  1 Y 1 LLL VAL 194 ? L VAL 189 
775  1 Y 1 LLL PRO 195 ? L PRO 190 
776  1 Y 1 LLL SER 196 ? L SER 191 
777  1 Y 1 LLL SER 197 ? L SER 192 
778  1 Y 1 LLL SER 198 ? L SER 193 
779  1 Y 1 LLL LEU 199 ? L LEU 194 
780  1 Y 1 LLL GLY 200 ? L GLY 195 
781  1 Y 1 LLL THR 201 ? L THR 196 
782  1 Y 1 LLL GLN 202 ? L GLN 197 
783  1 Y 1 LLL THR 203 ? L THR 198 
784  1 Y 1 LLL TYR 204 ? L TYR 199 
785  1 Y 1 LLL ILE 205 ? L ILE 200 
786  1 Y 1 LLL CYS 206 ? L CYS 201 
787  1 Y 1 LLL LYS 219 ? L LYS 214 
788  1 Y 1 LLL LYS 220 ? L LYS 215 
789  1 Y 1 LLL VAL 221 ? L VAL 216 
790  1 Y 1 LLL GLU 222 ? L GLU 217 
791  1 Y 1 LLL PRO 223 ? L PRO 218 
792  1 Y 1 LLL LYS 224 ? L LYS 219 
793  1 Y 1 LLL SER 225 ? L SER 220 
794  1 Y 1 LLL CYS 226 ? L CYS 221 
795  1 Y 1 LLL ASP 227 ? L ASP 222 
796  1 Y 1 LLL LYS 228 ? L LYS 223 
797  1 Y 1 LLL THR 229 ? L THR 224 
798  1 Y 1 LLL HIS 230 ? L HIS 225 
799  1 Y 1 LLL THR 231 ? L THR 226 
800  1 Y 1 LLL CYS 232 ? L CYS 227 
801  1 Y 1 LLL PRO 233 ? L PRO 228 
802  1 Y 1 LLL PRO 234 ? L PRO 229 
803  1 Y 1 LLL CYS 235 ? L CYS 230 
804  1 Y 1 LLL PRO 236 ? L PRO 231 
805  1 Y 1 LLL ALA 237 ? L ALA 232 
806  1 Y 1 LLL PRO 238 ? L PRO 233 
807  1 Y 1 LLL GLU 239 ? L GLU 234 
808  1 Y 1 LLL LEU 240 ? L LEU 235 
809  1 Y 1 LLL LEU 241 ? L LEU 236 
810  1 Y 1 LLL GLY 242 ? L GLY 237 
811  1 Y 1 LLL GLY 243 ? L GLY 238 
812  1 Y 1 LLL PRO 244 ? L PRO 239 
813  1 Y 1 LLL SER 245 ? L SER 240 
814  1 Y 1 LLL VAL 246 ? L VAL 241 
815  1 Y 1 LLL PHE 247 ? L PHE 242 
816  1 Y 1 LLL LEU 248 ? L LEU 243 
817  1 Y 1 LLL PHE 249 ? L PHE 244 
818  1 Y 1 LLL PRO 250 ? L PRO 245 
819  1 Y 1 LLL PRO 251 ? L PRO 246 
820  1 Y 1 LLL LYS 252 ? L LYS 247 
821  1 Y 1 LLL PRO 253 ? L PRO 248 
822  1 Y 1 LLL LYS 254 ? L LYS 249 
823  1 Y 1 LLL ASP 255 ? L ASP 250 
824  1 Y 1 LLL THR 256 ? L THR 251 
825  1 Y 1 LLL LEU 257 ? L LEU 252 
826  1 Y 1 LLL MET 258 ? L MET 253 
827  1 Y 1 LLL ILE 259 ? L ILE 254 
828  1 Y 1 LLL SER 260 ? L SER 255 
829  1 Y 1 LLL ARG 261 ? L ARG 256 
830  1 Y 1 LLL THR 262 ? L THR 257 
831  1 Y 1 LLL PRO 263 ? L PRO 258 
832  1 Y 1 LLL GLU 264 ? L GLU 259 
833  1 Y 1 LLL VAL 265 ? L VAL 260 
834  1 Y 1 LLL THR 266 ? L THR 261 
835  1 Y 1 LLL CYS 267 ? L CYS 262 
836  1 Y 1 LLL VAL 268 ? L VAL 263 
837  1 Y 1 LLL VAL 269 ? L VAL 264 
838  1 Y 1 LLL VAL 270 ? L VAL 265 
839  1 Y 1 LLL ASP 271 ? L ASP 266 
840  1 Y 1 LLL VAL 272 ? L VAL 267 
841  1 Y 1 LLL SER 273 ? L SER 268 
842  1 Y 1 LLL HIS 274 ? L HIS 269 
843  1 Y 1 LLL GLU 275 ? L GLU 270 
844  1 Y 1 LLL ASP 276 ? L ASP 271 
845  1 Y 1 LLL PRO 277 ? L PRO 272 
846  1 Y 1 LLL GLU 278 ? L GLU 273 
847  1 Y 1 LLL VAL 279 ? L VAL 274 
848  1 Y 1 LLL LYS 280 ? L LYS 275 
849  1 Y 1 LLL PHE 281 ? L PHE 276 
850  1 Y 1 LLL ASN 282 ? L ASN 277 
851  1 Y 1 LLL TRP 283 ? L TRP 278 
852  1 Y 1 LLL TYR 284 ? L TYR 279 
853  1 Y 1 LLL VAL 285 ? L VAL 280 
854  1 Y 1 LLL ASP 286 ? L ASP 281 
855  1 Y 1 LLL GLY 287 ? L GLY 282 
856  1 Y 1 LLL VAL 288 ? L VAL 283 
857  1 Y 1 LLL GLU 289 ? L GLU 284 
858  1 Y 1 LLL VAL 290 ? L VAL 285 
859  1 Y 1 LLL HIS 291 ? L HIS 286 
860  1 Y 1 LLL ASN 292 ? L ASN 287 
861  1 Y 1 LLL ALA 293 ? L ALA 288 
862  1 Y 1 LLL LYS 294 ? L LYS 289 
863  1 Y 1 LLL THR 295 ? L THR 290 
864  1 Y 1 LLL LYS 296 ? L LYS 291 
865  1 Y 1 LLL PRO 297 ? L PRO 292 
866  1 Y 1 LLL ARG 298 ? L ARG 293 
867  1 Y 1 LLL GLU 299 ? L GLU 294 
868  1 Y 1 LLL GLU 300 ? L GLU 295 
869  1 Y 1 LLL GLN 301 ? L GLN 296 
870  1 Y 1 LLL TYR 302 ? L TYR 297 
871  1 Y 1 LLL ASN 303 ? L ASN 298 
872  1 Y 1 LLL SER 304 ? L SER 299 
873  1 Y 1 LLL THR 305 ? L THR 300 
874  1 Y 1 LLL TYR 306 ? L TYR 301 
875  1 Y 1 LLL ARG 307 ? L ARG 302 
876  1 Y 1 LLL VAL 308 ? L VAL 303 
877  1 Y 1 LLL VAL 309 ? L VAL 304 
878  1 Y 1 LLL SER 310 ? L SER 305 
879  1 Y 1 LLL VAL 311 ? L VAL 306 
880  1 Y 1 LLL LEU 312 ? L LEU 307 
881  1 Y 1 LLL THR 313 ? L THR 308 
882  1 Y 1 LLL VAL 314 ? L VAL 309 
883  1 Y 1 LLL LEU 315 ? L LEU 310 
884  1 Y 1 LLL HIS 316 ? L HIS 311 
885  1 Y 1 LLL GLN 317 ? L GLN 312 
886  1 Y 1 LLL ASP 318 ? L ASP 313 
887  1 Y 1 LLL TRP 319 ? L TRP 314 
888  1 Y 1 LLL LEU 320 ? L LEU 315 
889  1 Y 1 LLL ASN 321 ? L ASN 316 
890  1 Y 1 LLL GLY 322 ? L GLY 317 
891  1 Y 1 LLL LYS 323 ? L LYS 318 
892  1 Y 1 LLL GLU 324 ? L GLU 319 
893  1 Y 1 LLL TYR 325 ? L TYR 320 
894  1 Y 1 LLL LYS 326 ? L LYS 321 
895  1 Y 1 LLL CYS 327 ? L CYS 322 
896  1 Y 1 LLL LYS 328 ? L LYS 323 
897  1 Y 1 LLL VAL 329 ? L VAL 324 
898  1 Y 1 LLL SER 330 ? L SER 325 
899  1 Y 1 LLL ASN 331 ? L ASN 326 
900  1 Y 1 LLL LYS 332 ? L LYS 327 
901  1 Y 1 LLL ALA 333 ? L ALA 328 
902  1 Y 1 LLL LEU 334 ? L LEU 329 
903  1 Y 1 LLL PRO 335 ? L PRO 330 
904  1 Y 1 LLL ALA 336 ? L ALA 331 
905  1 Y 1 LLL PRO 337 ? L PRO 332 
906  1 Y 1 LLL ILE 338 ? L ILE 333 
907  1 Y 1 LLL GLU 339 ? L GLU 334 
908  1 Y 1 LLL LYS 340 ? L LYS 335 
909  1 Y 1 LLL THR 341 ? L THR 336 
910  1 Y 1 LLL ILE 342 ? L ILE 337 
911  1 Y 1 LLL SER 343 ? L SER 338 
912  1 Y 1 LLL LYS 344 ? L LYS 339 
913  1 Y 1 LLL ALA 345 ? L ALA 340 
914  1 Y 1 LLL LYS 346 ? L LYS 341 
915  1 Y 1 LLL GLY 347 ? L GLY 342 
916  1 Y 1 LLL GLN 348 ? L GLN 343 
917  1 Y 1 LLL PRO 349 ? L PRO 344 
918  1 Y 1 LLL ARG 350 ? L ARG 345 
919  1 Y 1 LLL GLU 351 ? L GLU 346 
920  1 Y 1 LLL PRO 352 ? L PRO 347 
921  1 Y 1 LLL GLN 353 ? L GLN 348 
922  1 Y 1 LLL VAL 354 ? L VAL 349 
923  1 Y 1 LLL TYR 355 ? L TYR 350 
924  1 Y 1 LLL THR 356 ? L THR 351 
925  1 Y 1 LLL LEU 357 ? L LEU 352 
926  1 Y 1 LLL PRO 358 ? L PRO 353 
927  1 Y 1 LLL PRO 359 ? L PRO 354 
928  1 Y 1 LLL SER 360 ? L SER 355 
929  1 Y 1 LLL ARG 361 ? L ARG 356 
930  1 Y 1 LLL ASP 362 ? L ASP 357 
931  1 Y 1 LLL GLU 363 ? L GLU 358 
932  1 Y 1 LLL LEU 364 ? L LEU 359 
933  1 Y 1 LLL THR 365 ? L THR 360 
934  1 Y 1 LLL LYS 366 ? L LYS 361 
935  1 Y 1 LLL ASN 367 ? L ASN 362 
936  1 Y 1 LLL GLN 368 ? L GLN 363 
937  1 Y 1 LLL VAL 369 ? L VAL 364 
938  1 Y 1 LLL SER 370 ? L SER 365 
939  1 Y 1 LLL LEU 371 ? L LEU 366 
940  1 Y 1 LLL THR 372 ? L THR 367 
941  1 Y 1 LLL CYS 373 ? L CYS 368 
942  1 Y 1 LLL LEU 374 ? L LEU 369 
943  1 Y 1 LLL VAL 375 ? L VAL 370 
944  1 Y 1 LLL LYS 376 ? L LYS 371 
945  1 Y 1 LLL GLY 377 ? L GLY 372 
946  1 Y 1 LLL PHE 378 ? L PHE 373 
947  1 Y 1 LLL TYR 379 ? L TYR 374 
948  1 Y 1 LLL PRO 380 ? L PRO 375 
949  1 Y 1 LLL SER 381 ? L SER 376 
950  1 Y 1 LLL ASP 382 ? L ASP 377 
951  1 Y 1 LLL ILE 383 ? L ILE 378 
952  1 Y 1 LLL ALA 384 ? L ALA 379 
953  1 Y 1 LLL VAL 385 ? L VAL 380 
954  1 Y 1 LLL GLU 386 ? L GLU 381 
955  1 Y 1 LLL TRP 387 ? L TRP 382 
956  1 Y 1 LLL GLU 388 ? L GLU 383 
957  1 Y 1 LLL SER 389 ? L SER 384 
958  1 Y 1 LLL ASN 390 ? L ASN 385 
959  1 Y 1 LLL GLY 391 ? L GLY 386 
960  1 Y 1 LLL GLN 392 ? L GLN 387 
961  1 Y 1 LLL PRO 393 ? L PRO 388 
962  1 Y 1 LLL GLU 394 ? L GLU 389 
963  1 Y 1 LLL ASN 395 ? L ASN 390 
964  1 Y 1 LLL ASN 396 ? L ASN 391 
965  1 Y 1 LLL TYR 397 ? L TYR 392 
966  1 Y 1 LLL LYS 398 ? L LYS 393 
967  1 Y 1 LLL THR 399 ? L THR 394 
968  1 Y 1 LLL THR 400 ? L THR 395 
969  1 Y 1 LLL PRO 401 ? L PRO 396 
970  1 Y 1 LLL PRO 402 ? L PRO 397 
971  1 Y 1 LLL VAL 403 ? L VAL 398 
972  1 Y 1 MMM GLN 1   ? M GLN 1   
973  1 Y 1 MMM LEU 110 ? M LEU 110 
974  1 Y 1 MMM GLY 111 ? M GLY 111 
975  1 Y 1 MMM ALA 112 ? M ALA 112 
976  1 Y 1 MMM PRO 113 ? M PRO 113 
977  1 Y 1 MMM LYS 114 ? M LYS 114 
978  1 Y 1 MMM ALA 115 ? M ALA 115 
979  1 Y 1 MMM ASN 116 ? M ASN 116 
980  1 Y 1 MMM PRO 117 ? M PRO 117 
981  1 Y 1 MMM THR 118 ? M THR 118 
982  1 Y 1 MMM VAL 119 ? M VAL 119 
983  1 Y 1 MMM THR 120 ? M THR 120 
984  1 Y 1 MMM LEU 121 ? M LEU 121 
985  1 Y 1 MMM PHE 122 ? M PHE 122 
986  1 Y 1 MMM PRO 123 ? M PRO 123 
987  1 Y 1 MMM PRO 124 ? M PRO 124 
988  1 Y 1 MMM SER 125 ? M SER 125 
989  1 Y 1 MMM SER 126 ? M SER 126 
990  1 Y 1 MMM GLU 127 ? M GLU 127 
991  1 Y 1 MMM GLU 128 ? M GLU 128 
992  1 Y 1 MMM LEU 129 ? M LEU 129 
993  1 Y 1 MMM GLN 130 ? M GLN 130 
994  1 Y 1 MMM ALA 131 ? M ALA 131 
995  1 Y 1 MMM ASN 132 ? M ASN 132 
996  1 Y 1 MMM LYS 133 ? M LYS 133 
997  1 Y 1 MMM ALA 134 ? M ALA 134 
998  1 Y 1 MMM THR 135 ? M THR 135 
999  1 Y 1 MMM LEU 136 ? M LEU 136 
1000 1 Y 1 MMM VAL 137 ? M VAL 137 
1001 1 Y 1 MMM CYS 138 ? M CYS 138 
1002 1 Y 1 MMM LEU 139 ? M LEU 139 
1003 1 Y 1 MMM ILE 140 ? M ILE 140 
1004 1 Y 1 MMM SER 141 ? M SER 141 
1005 1 Y 1 MMM ASP 142 ? M ASP 142 
1006 1 Y 1 MMM PHE 143 ? M PHE 143 
1007 1 Y 1 MMM TYR 144 ? M TYR 144 
1008 1 Y 1 MMM PRO 145 ? M PRO 145 
1009 1 Y 1 MMM GLY 146 ? M GLY 146 
1010 1 Y 1 MMM ALA 147 ? M ALA 147 
1011 1 Y 1 MMM VAL 148 ? M VAL 148 
1012 1 Y 1 MMM THR 149 ? M THR 149 
1013 1 Y 1 MMM VAL 150 ? M VAL 150 
1014 1 Y 1 MMM ALA 151 ? M ALA 151 
1015 1 Y 1 MMM TRP 152 ? M TRP 152 
1016 1 Y 1 MMM LYS 153 ? M LYS 153 
1017 1 Y 1 MMM ALA 154 ? M ALA 154 
1018 1 Y 1 MMM ASP 155 ? M ASP 155 
1019 1 Y 1 MMM GLY 156 ? M GLY 156 
1020 1 Y 1 MMM SER 157 ? M SER 157 
1021 1 Y 1 MMM PRO 158 ? M PRO 158 
1022 1 Y 1 MMM VAL 159 ? M VAL 159 
1023 1 Y 1 MMM LYS 160 ? M LYS 160 
1024 1 Y 1 MMM ALA 161 ? M ALA 161 
1025 1 Y 1 MMM GLY 162 ? M GLY 162 
1026 1 Y 1 MMM VAL 163 ? M VAL 163 
1027 1 Y 1 MMM GLU 164 ? M GLU 164 
1028 1 Y 1 MMM THR 165 ? M THR 165 
1029 1 Y 1 MMM THR 166 ? M THR 166 
1030 1 Y 1 MMM LYS 167 ? M LYS 167 
1031 1 Y 1 MMM PRO 168 ? M PRO 168 
1032 1 Y 1 MMM SER 169 ? M SER 169 
1033 1 Y 1 MMM LYS 170 ? M LYS 170 
1034 1 Y 1 MMM GLN 171 ? M GLN 171 
1035 1 Y 1 MMM SER 172 ? M SER 172 
1036 1 Y 1 MMM ASN 173 ? M ASN 173 
1037 1 Y 1 MMM ASN 174 ? M ASN 174 
1038 1 Y 1 MMM LYS 175 ? M LYS 175 
1039 1 Y 1 MMM THR 176 ? M THR 176 
1040 1 Y 1 MMM ALA 177 ? M ALA 177 
1041 1 Y 1 MMM ALA 178 ? M ALA 178 
1042 1 Y 1 MMM SER 179 ? M SER 179 
1043 1 Y 1 MMM SER 180 ? M SER 180 
1044 1 Y 1 MMM TYR 181 ? M TYR 181 
1045 1 Y 1 MMM LEU 182 ? M LEU 182 
1046 1 Y 1 MMM SER 183 ? M SER 183 
1047 1 Y 1 MMM LEU 184 ? M LEU 184 
1048 1 Y 1 MMM THR 185 ? M THR 185 
1049 1 Y 1 MMM PRO 186 ? M PRO 186 
1050 1 Y 1 MMM GLU 187 ? M GLU 187 
1051 1 Y 1 MMM GLN 188 ? M GLN 188 
1052 1 Y 1 MMM TRP 189 ? M TRP 189 
1053 1 Y 1 MMM LYS 190 ? M LYS 190 
1054 1 Y 1 MMM SER 191 ? M SER 191 
1055 1 Y 1 MMM HIS 192 ? M HIS 192 
1056 1 Y 1 MMM ARG 193 ? M ARG 193 
1057 1 Y 1 MMM SER 194 ? M SER 194 
1058 1 Y 1 MMM TYR 195 ? M TYR 195 
1059 1 Y 1 MMM SER 196 ? M SER 196 
1060 1 Y 1 MMM CYS 197 ? M CYS 197 
1061 1 Y 1 MMM GLN 198 ? M GLN 198 
1062 1 Y 1 MMM VAL 199 ? M VAL 199 
1063 1 Y 1 MMM THR 200 ? M THR 200 
1064 1 Y 1 MMM HIS 201 ? M HIS 201 
1065 1 Y 1 MMM GLU 202 ? M GLU 202 
1066 1 Y 1 MMM GLY 203 ? M GLY 203 
1067 1 Y 1 MMM THR 204 ? M THR 204 
1068 1 Y 1 MMM THR 205 ? M THR 205 
1069 1 Y 1 MMM VAL 206 ? M VAL 206 
1070 1 Y 1 MMM GLU 207 ? M GLU 207 
1071 1 Y 1 MMM LYS 208 ? M LYS 208 
1072 1 Y 1 MMM THR 209 ? M THR 209 
1073 1 Y 1 MMM VAL 210 ? M VAL 210 
1074 1 Y 1 MMM ALA 211 ? M ALA 211 
1075 1 Y 1 MMM PRO 212 ? M PRO 212 
1076 1 Y 1 NNN ALA 119 ? N ALA 119 
1077 1 Y 1 NNN SER 120 ? N SER 120 
1078 1 Y 1 NNN THR 121 ? N THR 121 
1079 1 Y 1 NNN LYS 122 ? N LYS 122 
1080 1 Y 1 NNN GLY 123 ? N GLY 123 
1081 1 Y 1 NNN PRO 124 ? N PRO 124 
1082 1 Y 1 NNN SER 125 ? N SER 125 
1083 1 Y 1 NNN VAL 126 ? N VAL 126 
1084 1 Y 1 NNN PHE 127 ? N PHE 127 
1085 1 Y 1 NNN PRO 128 ? N PRO 128 
1086 1 Y 1 NNN LEU 129 ? N LEU 129 
1087 1 Y 1 NNN ALA 130 ? N ALA 130 
1088 1 Y 1 NNN PRO 131 ? N PRO 131 
1089 1 Y 1 NNN SER 132 ? N SER 132 
1090 1 Y 1 NNN SER 133 ? N SER 133 
1091 1 Y 1 NNN LYS 134 ? N LYS 134 
1092 1 Y 1 NNN SER 135 ? N SER 135 
1093 1 Y 1 NNN THR 136 ? N THR 136 
1094 1 Y 1 NNN SER 137 ? N SER 137 
1095 1 Y 1 NNN GLY 138 ? N GLY 138 
1096 1 Y 1 NNN GLY 139 ? N GLY 139 
1097 1 Y 1 NNN THR 140 ? N THR 140 
1098 1 Y 1 NNN ALA 141 ? N ALA 141 
1099 1 Y 1 NNN ALA 142 ? N ALA 142 
1100 1 Y 1 NNN LEU 143 ? N LEU 143 
1101 1 Y 1 NNN GLY 144 ? N GLY 144 
1102 1 Y 1 NNN CYS 145 ? N CYS 145 
1103 1 Y 1 NNN LEU 146 ? N LEU 146 
1104 1 Y 1 NNN VAL 147 ? N VAL 147 
1105 1 Y 1 NNN LYS 148 ? N LYS 148 
1106 1 Y 1 NNN ASP 149 ? N ASP 149 
1107 1 Y 1 NNN TYR 150 ? N TYR 150 
1108 1 Y 1 NNN PHE 151 ? N PHE 151 
1109 1 Y 1 NNN PRO 152 ? N PRO 152 
1110 1 Y 1 NNN GLU 153 ? N GLU 153 
1111 1 Y 1 NNN PRO 154 ? N PRO 154 
1112 1 Y 1 NNN VAL 155 ? N VAL 155 
1113 1 Y 1 NNN THR 156 ? N THR 156 
1114 1 Y 1 NNN VAL 157 ? N VAL 157 
1115 1 Y 1 NNN SER 158 ? N SER 158 
1116 1 Y 1 NNN TRP 159 ? N TRP 159 
1117 1 Y 1 NNN ASN 160 ? N ASN 160 
1118 1 Y 1 NNN SER 161 ? N SER 161 
1119 1 Y 1 NNN GLY 162 ? N GLY 162 
1120 1 Y 1 NNN ALA 163 ? N ALA 163 
1121 1 Y 1 NNN LEU 164 ? N LEU 164 
1122 1 Y 1 NNN THR 165 ? N THR 165 
1123 1 Y 1 NNN SER 166 ? N SER 166 
1124 1 Y 1 NNN GLY 167 ? N GLY 167 
1125 1 Y 1 NNN VAL 168 ? N VAL 168 
1126 1 Y 1 NNN HIS 169 ? N HIS 169 
1127 1 Y 1 NNN THR 170 ? N THR 170 
1128 1 Y 1 NNN PHE 171 ? N PHE 171 
1129 1 Y 1 NNN PRO 172 ? N PRO 172 
1130 1 Y 1 NNN ALA 173 ? N ALA 173 
1131 1 Y 1 NNN VAL 174 ? N VAL 174 
1132 1 Y 1 NNN LEU 175 ? N LEU 175 
1133 1 Y 1 NNN GLN 176 ? N GLN 176 
1134 1 Y 1 NNN SER 177 ? N SER 177 
1135 1 Y 1 NNN SER 178 ? N SER 178 
1136 1 Y 1 NNN GLY 179 ? N GLY 179 
1137 1 Y 1 NNN LEU 180 ? N LEU 180 
1138 1 Y 1 NNN TYR 181 ? N TYR 181 
1139 1 Y 1 NNN SER 182 ? N SER 182 
1140 1 Y 1 NNN LEU 183 ? N LEU 183 
1141 1 Y 1 NNN SER 184 ? N SER 184 
1142 1 Y 1 NNN SER 185 ? N SER 185 
1143 1 Y 1 NNN VAL 186 ? N VAL 186 
1144 1 Y 1 NNN VAL 187 ? N VAL 187 
1145 1 Y 1 NNN THR 188 ? N THR 188 
1146 1 Y 1 NNN VAL 189 ? N VAL 189 
1147 1 Y 1 NNN PRO 190 ? N PRO 190 
1148 1 Y 1 NNN SER 191 ? N SER 191 
1149 1 Y 1 NNN SER 192 ? N SER 192 
1150 1 Y 1 NNN SER 193 ? N SER 193 
1151 1 Y 1 NNN LEU 194 ? N LEU 194 
1152 1 Y 1 NNN GLY 195 ? N GLY 195 
1153 1 Y 1 NNN THR 196 ? N THR 196 
1154 1 Y 1 NNN GLN 197 ? N GLN 197 
1155 1 Y 1 NNN THR 198 ? N THR 198 
1156 1 Y 1 NNN TYR 199 ? N TYR 199 
1157 1 Y 1 NNN ILE 200 ? N ILE 200 
1158 1 Y 1 NNN CYS 201 ? N CYS 201 
1159 1 Y 1 NNN ASN 202 ? N ASN 202 
1160 1 Y 1 NNN VAL 203 ? N VAL 203 
1161 1 Y 1 NNN ASN 204 ? N ASN 204 
1162 1 Y 1 NNN HIS 205 ? N HIS 205 
1163 1 Y 1 NNN LYS 206 ? N LYS 206 
1164 1 Y 1 NNN PRO 207 ? N PRO 207 
1165 1 Y 1 NNN SER 208 ? N SER 208 
1166 1 Y 1 NNN ASN 209 ? N ASN 209 
1167 1 Y 1 NNN THR 210 ? N THR 210 
1168 1 Y 1 NNN LYS 211 ? N LYS 211 
1169 1 Y 1 NNN VAL 212 ? N VAL 212 
1170 1 Y 1 NNN ASP 213 ? N ASP 213 
1171 1 Y 1 NNN LYS 214 ? N LYS 214 
1172 1 Y 1 NNN LYS 215 ? N LYS 215 
1173 1 Y 1 NNN VAL 216 ? N VAL 216 
1174 1 Y 1 NNN GLU 217 ? N GLU 217 
1175 1 Y 1 NNN PRO 218 ? N PRO 218 
1176 1 Y 1 NNN LYS 219 ? N LYS 219 
1177 1 Y 1 NNN SER 220 ? N SER 220 
1178 1 Y 1 NNN CYS 221 ? N CYS 221 
1179 1 Y 1 NNN ASP 222 ? N ASP 222 
1180 1 Y 1 NNN LYS 223 ? N LYS 223 
1181 1 Y 1 NNN THR 224 ? N THR 224 
1182 1 Y 1 NNN HIS 225 ? N HIS 225 
1183 1 Y 1 NNN THR 226 ? N THR 226 
1184 1 Y 1 NNN CYS 227 ? N CYS 227 
1185 1 Y 1 NNN PRO 228 ? N PRO 228 
1186 1 Y 1 NNN PRO 229 ? N PRO 229 
1187 1 Y 1 NNN CYS 230 ? N CYS 230 
1188 1 Y 1 NNN PRO 231 ? N PRO 231 
1189 1 Y 1 NNN ALA 232 ? N ALA 232 
1190 1 Y 1 NNN PRO 233 ? N PRO 233 
1191 1 Y 1 NNN GLU 234 ? N GLU 234 
1192 1 Y 1 NNN LEU 235 ? N LEU 235 
1193 1 Y 1 NNN LEU 236 ? N LEU 236 
1194 1 Y 1 NNN GLY 237 ? N GLY 237 
1195 1 Y 1 NNN GLY 238 ? N GLY 238 
1196 1 Y 1 NNN PRO 239 ? N PRO 239 
1197 1 Y 1 NNN SER 240 ? N SER 240 
1198 1 Y 1 NNN VAL 241 ? N VAL 241 
1199 1 Y 1 NNN PHE 242 ? N PHE 242 
1200 1 Y 1 NNN LEU 243 ? N LEU 243 
1201 1 Y 1 NNN PHE 244 ? N PHE 244 
1202 1 Y 1 NNN PRO 245 ? N PRO 245 
1203 1 Y 1 NNN PRO 246 ? N PRO 246 
1204 1 Y 1 NNN LYS 247 ? N LYS 247 
1205 1 Y 1 NNN PRO 248 ? N PRO 248 
1206 1 Y 1 NNN LYS 249 ? N LYS 249 
1207 1 Y 1 NNN ASP 250 ? N ASP 250 
1208 1 Y 1 NNN THR 251 ? N THR 251 
1209 1 Y 1 NNN LEU 252 ? N LEU 252 
1210 1 Y 1 NNN MET 253 ? N MET 253 
1211 1 Y 1 NNN ILE 254 ? N ILE 254 
1212 1 Y 1 NNN SER 255 ? N SER 255 
1213 1 Y 1 NNN ARG 256 ? N ARG 256 
1214 1 Y 1 NNN THR 257 ? N THR 257 
1215 1 Y 1 NNN PRO 258 ? N PRO 258 
1216 1 Y 1 NNN GLU 259 ? N GLU 259 
1217 1 Y 1 NNN VAL 260 ? N VAL 260 
1218 1 Y 1 NNN THR 261 ? N THR 261 
1219 1 Y 1 NNN CYS 262 ? N CYS 262 
1220 1 Y 1 NNN VAL 263 ? N VAL 263 
1221 1 Y 1 NNN VAL 264 ? N VAL 264 
1222 1 Y 1 NNN VAL 265 ? N VAL 265 
1223 1 Y 1 NNN ASP 266 ? N ASP 266 
1224 1 Y 1 NNN VAL 267 ? N VAL 267 
1225 1 Y 1 NNN SER 268 ? N SER 268 
1226 1 Y 1 NNN HIS 269 ? N HIS 269 
1227 1 Y 1 NNN GLU 270 ? N GLU 270 
1228 1 Y 1 NNN ASP 271 ? N ASP 271 
1229 1 Y 1 NNN PRO 272 ? N PRO 272 
1230 1 Y 1 NNN GLU 273 ? N GLU 273 
1231 1 Y 1 NNN VAL 274 ? N VAL 274 
1232 1 Y 1 NNN LYS 275 ? N LYS 275 
1233 1 Y 1 NNN PHE 276 ? N PHE 276 
1234 1 Y 1 NNN ASN 277 ? N ASN 277 
1235 1 Y 1 NNN TRP 278 ? N TRP 278 
1236 1 Y 1 NNN TYR 279 ? N TYR 279 
1237 1 Y 1 NNN VAL 280 ? N VAL 280 
1238 1 Y 1 NNN ASP 281 ? N ASP 281 
1239 1 Y 1 NNN GLY 282 ? N GLY 282 
1240 1 Y 1 NNN VAL 283 ? N VAL 283 
1241 1 Y 1 NNN GLU 284 ? N GLU 284 
1242 1 Y 1 NNN VAL 285 ? N VAL 285 
1243 1 Y 1 NNN HIS 286 ? N HIS 286 
1244 1 Y 1 NNN ASN 287 ? N ASN 287 
1245 1 Y 1 NNN ALA 288 ? N ALA 288 
1246 1 Y 1 NNN LYS 289 ? N LYS 289 
1247 1 Y 1 NNN THR 290 ? N THR 290 
1248 1 Y 1 NNN LYS 291 ? N LYS 291 
1249 1 Y 1 NNN PRO 292 ? N PRO 292 
1250 1 Y 1 NNN ARG 293 ? N ARG 293 
1251 1 Y 1 NNN GLU 294 ? N GLU 294 
1252 1 Y 1 NNN GLU 295 ? N GLU 295 
1253 1 Y 1 NNN GLN 296 ? N GLN 296 
1254 1 Y 1 NNN TYR 297 ? N TYR 297 
1255 1 Y 1 NNN ASN 298 ? N ASN 298 
1256 1 Y 1 NNN SER 299 ? N SER 299 
1257 1 Y 1 NNN THR 300 ? N THR 300 
1258 1 Y 1 NNN TYR 301 ? N TYR 301 
1259 1 Y 1 NNN ARG 302 ? N ARG 302 
1260 1 Y 1 NNN VAL 303 ? N VAL 303 
1261 1 Y 1 NNN VAL 304 ? N VAL 304 
1262 1 Y 1 NNN SER 305 ? N SER 305 
1263 1 Y 1 NNN VAL 306 ? N VAL 306 
1264 1 Y 1 NNN LEU 307 ? N LEU 307 
1265 1 Y 1 NNN THR 308 ? N THR 308 
1266 1 Y 1 NNN VAL 309 ? N VAL 309 
1267 1 Y 1 NNN LEU 310 ? N LEU 310 
1268 1 Y 1 NNN HIS 311 ? N HIS 311 
1269 1 Y 1 NNN GLN 312 ? N GLN 312 
1270 1 Y 1 NNN ASP 313 ? N ASP 313 
1271 1 Y 1 NNN TRP 314 ? N TRP 314 
1272 1 Y 1 NNN LEU 315 ? N LEU 315 
1273 1 Y 1 NNN ASN 316 ? N ASN 316 
1274 1 Y 1 NNN GLY 317 ? N GLY 317 
1275 1 Y 1 NNN LYS 318 ? N LYS 318 
1276 1 Y 1 NNN GLU 319 ? N GLU 319 
1277 1 Y 1 NNN TYR 320 ? N TYR 320 
1278 1 Y 1 NNN LYS 321 ? N LYS 321 
1279 1 Y 1 NNN CYS 322 ? N CYS 322 
1280 1 Y 1 NNN LYS 323 ? N LYS 323 
1281 1 Y 1 NNN VAL 324 ? N VAL 324 
1282 1 Y 1 NNN SER 325 ? N SER 325 
1283 1 Y 1 NNN ASN 326 ? N ASN 326 
1284 1 Y 1 NNN LYS 327 ? N LYS 327 
1285 1 Y 1 NNN ALA 328 ? N ALA 328 
1286 1 Y 1 NNN LEU 329 ? N LEU 329 
1287 1 Y 1 NNN PRO 330 ? N PRO 330 
1288 1 Y 1 NNN ALA 331 ? N ALA 331 
1289 1 Y 1 NNN PRO 332 ? N PRO 332 
1290 1 Y 1 NNN ILE 333 ? N ILE 333 
1291 1 Y 1 NNN GLU 334 ? N GLU 334 
1292 1 Y 1 NNN LYS 335 ? N LYS 335 
1293 1 Y 1 NNN THR 336 ? N THR 336 
1294 1 Y 1 NNN ILE 337 ? N ILE 337 
1295 1 Y 1 NNN SER 338 ? N SER 338 
1296 1 Y 1 NNN LYS 339 ? N LYS 339 
1297 1 Y 1 NNN ALA 340 ? N ALA 340 
1298 1 Y 1 NNN LYS 341 ? N LYS 341 
1299 1 Y 1 NNN GLY 342 ? N GLY 342 
1300 1 Y 1 NNN GLN 343 ? N GLN 343 
1301 1 Y 1 NNN PRO 344 ? N PRO 344 
1302 1 Y 1 NNN ARG 345 ? N ARG 345 
1303 1 Y 1 NNN GLU 346 ? N GLU 346 
1304 1 Y 1 NNN PRO 347 ? N PRO 347 
1305 1 Y 1 NNN GLN 348 ? N GLN 348 
1306 1 Y 1 NNN VAL 349 ? N VAL 349 
1307 1 Y 1 NNN TYR 350 ? N TYR 350 
1308 1 Y 1 NNN THR 351 ? N THR 351 
1309 1 Y 1 NNN LEU 352 ? N LEU 352 
1310 1 Y 1 NNN PRO 353 ? N PRO 353 
1311 1 Y 1 NNN PRO 354 ? N PRO 354 
1312 1 Y 1 NNN SER 355 ? N SER 355 
1313 1 Y 1 NNN ARG 356 ? N ARG 356 
1314 1 Y 1 NNN ASP 357 ? N ASP 357 
1315 1 Y 1 NNN GLU 358 ? N GLU 358 
1316 1 Y 1 NNN LEU 359 ? N LEU 359 
1317 1 Y 1 NNN THR 360 ? N THR 360 
1318 1 Y 1 NNN LYS 361 ? N LYS 361 
1319 1 Y 1 NNN ASN 362 ? N ASN 362 
1320 1 Y 1 NNN GLN 363 ? N GLN 363 
1321 1 Y 1 NNN VAL 364 ? N VAL 364 
1322 1 Y 1 NNN SER 365 ? N SER 365 
1323 1 Y 1 NNN LEU 366 ? N LEU 366 
1324 1 Y 1 NNN THR 367 ? N THR 367 
1325 1 Y 1 NNN CYS 368 ? N CYS 368 
1326 1 Y 1 NNN LEU 369 ? N LEU 369 
1327 1 Y 1 NNN VAL 370 ? N VAL 370 
1328 1 Y 1 NNN LYS 371 ? N LYS 371 
1329 1 Y 1 NNN GLY 372 ? N GLY 372 
1330 1 Y 1 NNN PHE 373 ? N PHE 373 
1331 1 Y 1 NNN TYR 374 ? N TYR 374 
1332 1 Y 1 NNN PRO 375 ? N PRO 375 
1333 1 Y 1 NNN SER 376 ? N SER 376 
1334 1 Y 1 NNN ASP 377 ? N ASP 377 
1335 1 Y 1 NNN ILE 378 ? N ILE 378 
1336 1 Y 1 NNN ALA 379 ? N ALA 379 
1337 1 Y 1 NNN VAL 380 ? N VAL 380 
1338 1 Y 1 NNN GLU 381 ? N GLU 381 
1339 1 Y 1 NNN TRP 382 ? N TRP 382 
1340 1 Y 1 NNN GLU 383 ? N GLU 383 
1341 1 Y 1 NNN SER 384 ? N SER 384 
1342 1 Y 1 NNN ASN 385 ? N ASN 385 
1343 1 Y 1 NNN GLY 386 ? N GLY 386 
1344 1 Y 1 NNN GLN 387 ? N GLN 387 
1345 1 Y 1 NNN PRO 388 ? N PRO 388 
1346 1 Y 1 NNN GLU 389 ? N GLU 389 
1347 1 Y 1 NNN ASN 390 ? N ASN 390 
1348 1 Y 1 NNN ASN 391 ? N ASN 391 
1349 1 Y 1 NNN TYR 392 ? N TYR 392 
1350 1 Y 1 NNN LYS 393 ? N LYS 393 
1351 1 Y 1 NNN THR 394 ? N THR 394 
1352 1 Y 1 NNN THR 395 ? N THR 395 
1353 1 Y 1 NNN PRO 396 ? N PRO 396 
1354 1 Y 1 NNN PRO 397 ? N PRO 397 
1355 1 Y 1 NNN VAL 398 ? N VAL 398 
1356 1 Y 1 YYY SER 137 ? O SER 132 
1357 1 Y 1 YYY SER 138 ? O SER 133 
1358 1 Y 1 YYY LYS 139 ? O LYS 134 
1359 1 Y 1 YYY SER 140 ? O SER 135 
1360 1 Y 1 YYY THR 141 ? O THR 136 
1361 1 Y 1 YYY SER 142 ? O SER 137 
1362 1 Y 1 YYY GLY 143 ? O GLY 138 
1363 1 Y 1 YYY GLY 144 ? O GLY 139 
1364 1 Y 1 YYY THR 145 ? O THR 140 
1365 1 Y 1 YYY ALA 146 ? O ALA 141 
1366 1 Y 1 YYY LEU 169 ? O LEU 164 
1367 1 Y 1 YYY THR 170 ? O THR 165 
1368 1 Y 1 YYY SER 171 ? O SER 166 
1369 1 Y 1 YYY GLY 172 ? O GLY 167 
1370 1 Y 1 YYY THR 193 ? O THR 188 
1371 1 Y 1 YYY VAL 194 ? O VAL 189 
1372 1 Y 1 YYY PRO 195 ? O PRO 190 
1373 1 Y 1 YYY SER 196 ? O SER 191 
1374 1 Y 1 YYY SER 197 ? O SER 192 
1375 1 Y 1 YYY SER 198 ? O SER 193 
1376 1 Y 1 YYY LEU 199 ? O LEU 194 
1377 1 Y 1 YYY GLY 200 ? O GLY 195 
1378 1 Y 1 YYY THR 201 ? O THR 196 
1379 1 Y 1 YYY GLN 202 ? O GLN 197 
1380 1 Y 1 YYY THR 203 ? O THR 198 
1381 1 Y 1 YYY TYR 204 ? O TYR 199 
1382 1 Y 1 YYY ILE 205 ? O ILE 200 
1383 1 Y 1 YYY GLU 222 ? O GLU 217 
1384 1 Y 1 YYY PRO 223 ? O PRO 218 
1385 1 Y 1 YYY LYS 224 ? O LYS 219 
1386 1 Y 1 YYY SER 225 ? O SER 220 
1387 1 Y 1 YYY CYS 226 ? O CYS 221 
1388 1 Y 1 YYY ASP 227 ? O ASP 222 
1389 1 Y 1 YYY LYS 228 ? O LYS 223 
1390 1 Y 1 YYY THR 229 ? O THR 224 
1391 1 Y 1 YYY HIS 230 ? O HIS 225 
1392 1 Y 1 YYY THR 231 ? O THR 226 
1393 1 Y 1 YYY CYS 232 ? O CYS 227 
1394 1 Y 1 YYY PRO 233 ? O PRO 228 
1395 1 Y 1 YYY PRO 234 ? O PRO 229 
1396 1 Y 1 YYY CYS 235 ? O CYS 230 
1397 1 Y 1 YYY PRO 236 ? O PRO 231 
1398 1 Y 1 YYY ALA 237 ? O ALA 232 
1399 1 Y 1 YYY PRO 238 ? O PRO 233 
1400 1 Y 1 YYY GLU 239 ? O GLU 234 
1401 1 Y 1 YYY LEU 240 ? O LEU 235 
1402 1 Y 1 YYY LEU 241 ? O LEU 236 
1403 1 Y 1 YYY GLY 242 ? O GLY 237 
1404 1 Y 1 YYY GLY 243 ? O GLY 238 
1405 1 Y 1 YYY PRO 244 ? O PRO 239 
1406 1 Y 1 YYY SER 245 ? O SER 240 
1407 1 Y 1 YYY VAL 246 ? O VAL 241 
1408 1 Y 1 YYY PHE 247 ? O PHE 242 
1409 1 Y 1 YYY LEU 248 ? O LEU 243 
1410 1 Y 1 YYY PHE 249 ? O PHE 244 
1411 1 Y 1 YYY PRO 250 ? O PRO 245 
1412 1 Y 1 YYY PRO 251 ? O PRO 246 
1413 1 Y 1 YYY LYS 252 ? O LYS 247 
1414 1 Y 1 YYY PRO 253 ? O PRO 248 
1415 1 Y 1 YYY LYS 254 ? O LYS 249 
1416 1 Y 1 YYY ASP 255 ? O ASP 250 
1417 1 Y 1 YYY THR 256 ? O THR 251 
1418 1 Y 1 YYY LEU 257 ? O LEU 252 
1419 1 Y 1 YYY MET 258 ? O MET 253 
1420 1 Y 1 YYY ILE 259 ? O ILE 254 
1421 1 Y 1 YYY SER 260 ? O SER 255 
1422 1 Y 1 YYY ARG 261 ? O ARG 256 
1423 1 Y 1 YYY THR 262 ? O THR 257 
1424 1 Y 1 YYY PRO 263 ? O PRO 258 
1425 1 Y 1 YYY GLU 264 ? O GLU 259 
1426 1 Y 1 YYY VAL 265 ? O VAL 260 
1427 1 Y 1 YYY THR 266 ? O THR 261 
1428 1 Y 1 YYY CYS 267 ? O CYS 262 
1429 1 Y 1 YYY VAL 268 ? O VAL 263 
1430 1 Y 1 YYY VAL 269 ? O VAL 264 
1431 1 Y 1 YYY VAL 270 ? O VAL 265 
1432 1 Y 1 YYY ASP 271 ? O ASP 266 
1433 1 Y 1 YYY VAL 272 ? O VAL 267 
1434 1 Y 1 YYY SER 273 ? O SER 268 
1435 1 Y 1 YYY HIS 274 ? O HIS 269 
1436 1 Y 1 YYY GLU 275 ? O GLU 270 
1437 1 Y 1 YYY ASP 276 ? O ASP 271 
1438 1 Y 1 YYY PRO 277 ? O PRO 272 
1439 1 Y 1 YYY GLU 278 ? O GLU 273 
1440 1 Y 1 YYY VAL 279 ? O VAL 274 
1441 1 Y 1 YYY LYS 280 ? O LYS 275 
1442 1 Y 1 YYY PHE 281 ? O PHE 276 
1443 1 Y 1 YYY ASN 282 ? O ASN 277 
1444 1 Y 1 YYY TRP 283 ? O TRP 278 
1445 1 Y 1 YYY TYR 284 ? O TYR 279 
1446 1 Y 1 YYY VAL 285 ? O VAL 280 
1447 1 Y 1 YYY ASP 286 ? O ASP 281 
1448 1 Y 1 YYY GLY 287 ? O GLY 282 
1449 1 Y 1 YYY VAL 288 ? O VAL 283 
1450 1 Y 1 YYY GLU 289 ? O GLU 284 
1451 1 Y 1 YYY VAL 290 ? O VAL 285 
1452 1 Y 1 YYY HIS 291 ? O HIS 286 
1453 1 Y 1 YYY ASN 292 ? O ASN 287 
1454 1 Y 1 YYY ALA 293 ? O ALA 288 
1455 1 Y 1 YYY LYS 294 ? O LYS 289 
1456 1 Y 1 YYY THR 295 ? O THR 290 
1457 1 Y 1 YYY LYS 296 ? O LYS 291 
1458 1 Y 1 YYY PRO 297 ? O PRO 292 
1459 1 Y 1 YYY ARG 298 ? O ARG 293 
1460 1 Y 1 YYY GLU 299 ? O GLU 294 
1461 1 Y 1 YYY GLU 300 ? O GLU 295 
1462 1 Y 1 YYY GLN 301 ? O GLN 296 
1463 1 Y 1 YYY TYR 302 ? O TYR 297 
1464 1 Y 1 YYY ASN 303 ? O ASN 298 
1465 1 Y 1 YYY SER 304 ? O SER 299 
1466 1 Y 1 YYY THR 305 ? O THR 300 
1467 1 Y 1 YYY TYR 306 ? O TYR 301 
1468 1 Y 1 YYY ARG 307 ? O ARG 302 
1469 1 Y 1 YYY VAL 308 ? O VAL 303 
1470 1 Y 1 YYY VAL 309 ? O VAL 304 
1471 1 Y 1 YYY SER 310 ? O SER 305 
1472 1 Y 1 YYY VAL 311 ? O VAL 306 
1473 1 Y 1 YYY LEU 312 ? O LEU 307 
1474 1 Y 1 YYY THR 313 ? O THR 308 
1475 1 Y 1 YYY VAL 314 ? O VAL 309 
1476 1 Y 1 YYY LEU 315 ? O LEU 310 
1477 1 Y 1 YYY HIS 316 ? O HIS 311 
1478 1 Y 1 YYY GLN 317 ? O GLN 312 
1479 1 Y 1 YYY ASP 318 ? O ASP 313 
1480 1 Y 1 YYY TRP 319 ? O TRP 314 
1481 1 Y 1 YYY LEU 320 ? O LEU 315 
1482 1 Y 1 YYY ASN 321 ? O ASN 316 
1483 1 Y 1 YYY GLY 322 ? O GLY 317 
1484 1 Y 1 YYY LYS 323 ? O LYS 318 
1485 1 Y 1 YYY GLU 324 ? O GLU 319 
1486 1 Y 1 YYY TYR 325 ? O TYR 320 
1487 1 Y 1 YYY LYS 326 ? O LYS 321 
1488 1 Y 1 YYY CYS 327 ? O CYS 322 
1489 1 Y 1 YYY LYS 328 ? O LYS 323 
1490 1 Y 1 YYY VAL 329 ? O VAL 324 
1491 1 Y 1 YYY SER 330 ? O SER 325 
1492 1 Y 1 YYY ASN 331 ? O ASN 326 
1493 1 Y 1 YYY LYS 332 ? O LYS 327 
1494 1 Y 1 YYY ALA 333 ? O ALA 328 
1495 1 Y 1 YYY LEU 334 ? O LEU 329 
1496 1 Y 1 YYY PRO 335 ? O PRO 330 
1497 1 Y 1 YYY ALA 336 ? O ALA 331 
1498 1 Y 1 YYY PRO 337 ? O PRO 332 
1499 1 Y 1 YYY ILE 338 ? O ILE 333 
1500 1 Y 1 YYY GLU 339 ? O GLU 334 
1501 1 Y 1 YYY LYS 340 ? O LYS 335 
1502 1 Y 1 YYY THR 341 ? O THR 336 
1503 1 Y 1 YYY ILE 342 ? O ILE 337 
1504 1 Y 1 YYY SER 343 ? O SER 338 
1505 1 Y 1 YYY LYS 344 ? O LYS 339 
1506 1 Y 1 YYY ALA 345 ? O ALA 340 
1507 1 Y 1 YYY LYS 346 ? O LYS 341 
1508 1 Y 1 YYY GLY 347 ? O GLY 342 
1509 1 Y 1 YYY GLN 348 ? O GLN 343 
1510 1 Y 1 YYY PRO 349 ? O PRO 344 
1511 1 Y 1 YYY ARG 350 ? O ARG 345 
1512 1 Y 1 YYY GLU 351 ? O GLU 346 
1513 1 Y 1 YYY PRO 352 ? O PRO 347 
1514 1 Y 1 YYY GLN 353 ? O GLN 348 
1515 1 Y 1 YYY VAL 354 ? O VAL 349 
1516 1 Y 1 YYY TYR 355 ? O TYR 350 
1517 1 Y 1 YYY THR 356 ? O THR 351 
1518 1 Y 1 YYY LEU 357 ? O LEU 352 
1519 1 Y 1 YYY PRO 358 ? O PRO 353 
1520 1 Y 1 YYY PRO 359 ? O PRO 354 
1521 1 Y 1 YYY SER 360 ? O SER 355 
1522 1 Y 1 YYY ARG 361 ? O ARG 356 
1523 1 Y 1 YYY ASP 362 ? O ASP 357 
1524 1 Y 1 YYY GLU 363 ? O GLU 358 
1525 1 Y 1 YYY LEU 364 ? O LEU 359 
1526 1 Y 1 YYY THR 365 ? O THR 360 
1527 1 Y 1 YYY LYS 366 ? O LYS 361 
1528 1 Y 1 YYY ASN 367 ? O ASN 362 
1529 1 Y 1 YYY GLN 368 ? O GLN 363 
1530 1 Y 1 YYY VAL 369 ? O VAL 364 
1531 1 Y 1 YYY SER 370 ? O SER 365 
1532 1 Y 1 YYY LEU 371 ? O LEU 366 
1533 1 Y 1 YYY THR 372 ? O THR 367 
1534 1 Y 1 YYY CYS 373 ? O CYS 368 
1535 1 Y 1 YYY LEU 374 ? O LEU 369 
1536 1 Y 1 YYY VAL 375 ? O VAL 370 
1537 1 Y 1 YYY LYS 376 ? O LYS 371 
1538 1 Y 1 YYY GLY 377 ? O GLY 372 
1539 1 Y 1 YYY PHE 378 ? O PHE 373 
1540 1 Y 1 YYY TYR 379 ? O TYR 374 
1541 1 Y 1 YYY PRO 380 ? O PRO 375 
1542 1 Y 1 YYY SER 381 ? O SER 376 
1543 1 Y 1 YYY ASP 382 ? O ASP 377 
1544 1 Y 1 YYY ILE 383 ? O ILE 378 
1545 1 Y 1 YYY ALA 384 ? O ALA 379 
1546 1 Y 1 YYY VAL 385 ? O VAL 380 
1547 1 Y 1 YYY GLU 386 ? O GLU 381 
1548 1 Y 1 YYY TRP 387 ? O TRP 382 
1549 1 Y 1 YYY GLU 388 ? O GLU 383 
1550 1 Y 1 YYY SER 389 ? O SER 384 
1551 1 Y 1 YYY ASN 390 ? O ASN 385 
1552 1 Y 1 YYY GLY 391 ? O GLY 386 
1553 1 Y 1 YYY GLN 392 ? O GLN 387 
1554 1 Y 1 YYY PRO 393 ? O PRO 388 
1555 1 Y 1 YYY GLU 394 ? O GLU 389 
1556 1 Y 1 YYY ASN 395 ? O ASN 390 
1557 1 Y 1 YYY ASN 396 ? O ASN 391 
1558 1 Y 1 YYY TYR 397 ? O TYR 392 
1559 1 Y 1 YYY LYS 398 ? O LYS 393 
1560 1 Y 1 YYY THR 399 ? O THR 394 
1561 1 Y 1 YYY THR 400 ? O THR 395 
1562 1 Y 1 YYY PRO 401 ? O PRO 396 
1563 1 Y 1 YYY PRO 402 ? O PRO 397 
1564 1 Y 1 YYY VAL 403 ? O VAL 398 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           FOR2327 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
