data_6ZLR
# 
_entry.id   6ZLR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.336 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6ZLR         
WWPDB D_1292109738 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6ZLR 
_pdbx_database_status.recvd_initial_deposition_date   2020-07-01 
_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 
'de Nicola, G.F.' 1 0000-0003-4649-9452 
'Nichols, C.E.'   2 0000-0002-2159-371X 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Front Pharmacol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1663-9812 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                615211 
_citation.page_last                 615211 
_citation.title                     
;A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex-An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site Surface.
;
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3389/fphar.2020.615211 
_citation.pdbx_database_id_PubMed   33381049 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nichols, C.'     1 ? 
primary 'Ng, J.'          2 ? 
primary 'Keshu, A.'       3 ? 
primary 'Fraternali, F.'  4 ? 
primary 'De Nicola, G.F.' 5 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6ZLR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     207.130 
_cell.length_a_esd                 ? 
_cell.length_b                     207.130 
_cell.length_b_esd                 ? 
_cell.length_c                     199.866 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         6ZLR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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 'Spike glycoprotein'                     26095.348 3 ? ? ? ? 
2 polymer     man 'CR3022 FAB HEAVY CHAIN'                 23455.420 3 ? ? ? ? 
3 polymer     man 'CR3022 FAB LIGHT CHAIN'                 24376.963 3 ? ? ? ? 
4 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   3 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'S glycoprotein,E2,Peplomer protein' 
# 
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 
;RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYAD
SFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGST
PCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFSGHHHHHH
;
;RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYAD
SFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGST
PCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFSGHHHHHH
;
EEE,AAA,DDD ? 
2 'polypeptide(L)' no no 
;QMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTAY
LQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
;
;QMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTAY
LQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
;
HHH,BBB,FFF ? 
3 'polypeptide(L)' no no 
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECS
;
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECS
;
LLL,CCC,GGG ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   VAL n 
1 3   GLN n 
1 4   PRO n 
1 5   THR n 
1 6   GLU n 
1 7   SER n 
1 8   ILE n 
1 9   VAL n 
1 10  ARG n 
1 11  PHE n 
1 12  PRO n 
1 13  ASN n 
1 14  ILE n 
1 15  THR n 
1 16  ASN n 
1 17  LEU n 
1 18  CYS n 
1 19  PRO n 
1 20  PHE n 
1 21  GLY n 
1 22  GLU n 
1 23  VAL n 
1 24  PHE n 
1 25  ASN n 
1 26  ALA n 
1 27  THR n 
1 28  ARG n 
1 29  PHE n 
1 30  ALA n 
1 31  SER n 
1 32  VAL n 
1 33  TYR n 
1 34  ALA n 
1 35  TRP n 
1 36  ASN n 
1 37  ARG n 
1 38  LYS n 
1 39  ARG n 
1 40  ILE n 
1 41  SER n 
1 42  ASN n 
1 43  CYS n 
1 44  VAL n 
1 45  ALA n 
1 46  ASP n 
1 47  TYR n 
1 48  SER n 
1 49  VAL n 
1 50  LEU n 
1 51  TYR n 
1 52  ASN n 
1 53  SER n 
1 54  ALA n 
1 55  SER n 
1 56  PHE n 
1 57  SER n 
1 58  THR n 
1 59  PHE n 
1 60  LYS n 
1 61  CYS n 
1 62  TYR n 
1 63  GLY n 
1 64  VAL n 
1 65  SER n 
1 66  PRO n 
1 67  THR n 
1 68  LYS n 
1 69  LEU n 
1 70  ASN n 
1 71  ASP n 
1 72  LEU n 
1 73  CYS n 
1 74  PHE n 
1 75  THR n 
1 76  ASN n 
1 77  VAL n 
1 78  TYR n 
1 79  ALA n 
1 80  ASP n 
1 81  SER n 
1 82  PHE n 
1 83  VAL n 
1 84  ILE n 
1 85  ARG n 
1 86  GLY n 
1 87  ASP n 
1 88  GLU n 
1 89  VAL n 
1 90  ARG n 
1 91  GLN n 
1 92  ILE n 
1 93  ALA n 
1 94  PRO n 
1 95  GLY n 
1 96  GLN n 
1 97  THR n 
1 98  GLY n 
1 99  LYS n 
1 100 ILE n 
1 101 ALA n 
1 102 ASP n 
1 103 TYR n 
1 104 ASN n 
1 105 TYR n 
1 106 LYS n 
1 107 LEU n 
1 108 PRO n 
1 109 ASP n 
1 110 ASP n 
1 111 PHE n 
1 112 THR n 
1 113 GLY n 
1 114 CYS n 
1 115 VAL n 
1 116 ILE n 
1 117 ALA n 
1 118 TRP n 
1 119 ASN n 
1 120 SER n 
1 121 ASN n 
1 122 ASN n 
1 123 LEU n 
1 124 ASP n 
1 125 SER n 
1 126 LYS n 
1 127 VAL n 
1 128 GLY n 
1 129 GLY n 
1 130 ASN n 
1 131 TYR n 
1 132 ASN n 
1 133 TYR n 
1 134 LEU n 
1 135 TYR n 
1 136 ARG n 
1 137 LEU n 
1 138 PHE n 
1 139 ARG n 
1 140 LYS n 
1 141 SER n 
1 142 ASN n 
1 143 LEU n 
1 144 LYS n 
1 145 PRO n 
1 146 PHE n 
1 147 GLU n 
1 148 ARG n 
1 149 ASP n 
1 150 ILE n 
1 151 SER n 
1 152 THR n 
1 153 GLU n 
1 154 ILE n 
1 155 TYR n 
1 156 GLN n 
1 157 ALA n 
1 158 GLY n 
1 159 SER n 
1 160 THR n 
1 161 PRO n 
1 162 CYS n 
1 163 ASN n 
1 164 GLY n 
1 165 VAL n 
1 166 GLU n 
1 167 GLY n 
1 168 PHE n 
1 169 ASN n 
1 170 CYS n 
1 171 TYR n 
1 172 PHE n 
1 173 PRO n 
1 174 LEU n 
1 175 GLN n 
1 176 SER n 
1 177 TYR n 
1 178 GLY n 
1 179 PHE n 
1 180 GLN n 
1 181 PRO n 
1 182 THR n 
1 183 ASN n 
1 184 GLY n 
1 185 VAL n 
1 186 GLY n 
1 187 TYR n 
1 188 GLN n 
1 189 PRO n 
1 190 TYR n 
1 191 ARG n 
1 192 VAL n 
1 193 VAL n 
1 194 VAL n 
1 195 LEU n 
1 196 SER n 
1 197 PHE n 
1 198 GLU n 
1 199 LEU n 
1 200 LEU n 
1 201 HIS n 
1 202 ALA n 
1 203 PRO n 
1 204 ALA n 
1 205 THR n 
1 206 VAL n 
1 207 CYS n 
1 208 GLY n 
1 209 PRO n 
1 210 LYS n 
1 211 LYS n 
1 212 SER n 
1 213 THR n 
1 214 ASN n 
1 215 LEU n 
1 216 VAL n 
1 217 LYS n 
1 218 ASN n 
1 219 LYS n 
1 220 CYS n 
1 221 VAL n 
1 222 ASN n 
1 223 PHE n 
1 224 SER n 
1 225 GLY n 
1 226 HIS n 
1 227 HIS n 
1 228 HIS n 
1 229 HIS n 
1 230 HIS n 
1 231 HIS n 
2 1   GLN n 
2 2   MET n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   THR n 
2 10  GLU n 
2 11  VAL n 
2 12  LYS n 
2 13  LYS n 
2 14  PRO n 
2 15  GLY n 
2 16  GLU n 
2 17  SER n 
2 18  LEU n 
2 19  LYS n 
2 20  ILE n 
2 21  SER n 
2 22  CYS n 
2 23  LYS n 
2 24  GLY n 
2 25  SER n 
2 26  GLY n 
2 27  TYR n 
2 28  GLY n 
2 29  PHE n 
2 30  ILE n 
2 31  THR n 
2 32  TYR n 
2 33  TRP n 
2 34  ILE n 
2 35  GLY n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  MET n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  MET n 
2 49  GLY n 
2 50  ILE n 
2 51  ILE n 
2 52  TYR n 
2 53  PRO n 
2 54  GLY n 
2 55  ASP n 
2 56  SER n 
2 57  GLU n 
2 58  THR n 
2 59  ARG n 
2 60  TYR n 
2 61  SER n 
2 62  PRO n 
2 63  SER n 
2 64  PHE n 
2 65  GLN n 
2 66  GLY n 
2 67  GLN n 
2 68  VAL n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ALA n 
2 73  ASP n 
2 74  LYS n 
2 75  SER n 
2 76  ILE n 
2 77  ASN n 
2 78  THR n 
2 79  ALA n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  TRP n 
2 84  SER n 
2 85  SER n 
2 86  LEU n 
2 87  LYS n 
2 88  ALA n 
2 89  SER n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  ILE n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  GLY n 
2 99  GLY n 
2 100 SER n 
2 101 GLY n 
2 102 ILE n 
2 103 SER n 
2 104 THR n 
2 105 PRO n 
2 106 MET n 
2 107 ASP n 
2 108 VAL n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 THR n 
2 114 THR n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 SER n 
2 120 ALA n 
2 121 SER n 
2 122 THR n 
2 123 LYS n 
2 124 GLY n 
2 125 PRO n 
2 126 SER n 
2 127 VAL n 
2 128 PHE n 
2 129 PRO n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 SER n 
2 134 SER n 
2 135 LYS n 
2 136 SER n 
2 137 THR n 
2 138 SER n 
2 139 GLY n 
2 140 GLY n 
2 141 THR n 
2 142 ALA n 
2 143 ALA n 
2 144 LEU n 
2 145 GLY n 
2 146 CYS n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 ASP n 
2 151 TYR n 
2 152 PHE n 
2 153 PRO n 
2 154 GLU n 
2 155 PRO n 
2 156 VAL n 
2 157 THR n 
2 158 VAL n 
2 159 SER n 
2 160 TRP n 
2 161 ASN n 
2 162 SER n 
2 163 GLY n 
2 164 ALA n 
2 165 LEU n 
2 166 THR n 
2 167 SER n 
2 168 GLY n 
2 169 VAL n 
2 170 HIS n 
2 171 THR n 
2 172 PHE n 
2 173 PRO n 
2 174 ALA n 
2 175 VAL n 
2 176 LEU n 
2 177 GLN n 
2 178 SER n 
2 179 SER n 
2 180 GLY n 
2 181 LEU n 
2 182 TYR n 
2 183 SER n 
2 184 LEU n 
2 185 SER n 
2 186 SER n 
2 187 VAL n 
2 188 VAL n 
2 189 THR n 
2 190 VAL n 
2 191 PRO n 
2 192 SER n 
2 193 SER n 
2 194 SER n 
2 195 LEU n 
2 196 GLY n 
2 197 THR n 
2 198 GLN n 
2 199 THR n 
2 200 TYR n 
2 201 ILE n 
2 202 CYS n 
2 203 ASN n 
2 204 VAL n 
2 205 ASN n 
2 206 HIS n 
2 207 LYS n 
2 208 PRO n 
2 209 SER n 
2 210 ASN n 
2 211 THR n 
2 212 LYS n 
2 213 VAL n 
2 214 ASP n 
2 215 LYS n 
2 216 LYS n 
2 217 VAL n 
2 218 GLU n 
2 219 PRO n 
2 220 LYS n 
2 221 SER n 
2 222 CYS n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   LEU n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   ASP n 
3 10  SER n 
3 11  LEU n 
3 12  ALA n 
3 13  VAL n 
3 14  SER n 
3 15  LEU n 
3 16  GLY n 
3 17  GLU n 
3 18  ARG n 
3 19  ALA n 
3 20  THR n 
3 21  ILE n 
3 22  ASN n 
3 23  CYS n 
3 24  LYS n 
3 25  SER n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  VAL n 
3 30  LEU n 
3 31  TYR n 
3 32  SER n 
3 33  SER n 
3 34  ILE n 
3 35  ASN n 
3 36  LYS n 
3 37  ASN n 
3 38  TYR n 
3 39  LEU n 
3 40  ALA n 
3 41  TRP n 
3 42  TYR n 
3 43  GLN n 
3 44  GLN n 
3 45  LYS n 
3 46  PRO n 
3 47  GLY n 
3 48  GLN n 
3 49  PRO n 
3 50  PRO n 
3 51  LYS n 
3 52  LEU n 
3 53  LEU n 
3 54  ILE n 
3 55  TYR n 
3 56  TRP n 
3 57  ALA n 
3 58  SER n 
3 59  THR n 
3 60  ARG n 
3 61  GLU n 
3 62  SER n 
3 63  GLY n 
3 64  VAL n 
3 65  PRO n 
3 66  ASP n 
3 67  ARG n 
3 68  PHE n 
3 69  SER n 
3 70  GLY n 
3 71  SER n 
3 72  GLY n 
3 73  SER n 
3 74  GLY n 
3 75  THR n 
3 76  ASP n 
3 77  PHE n 
3 78  THR n 
3 79  LEU n 
3 80  THR n 
3 81  ILE n 
3 82  SER n 
3 83  SER n 
3 84  LEU n 
3 85  GLN n 
3 86  ALA n 
3 87  GLU n 
3 88  ASP n 
3 89  VAL n 
3 90  ALA n 
3 91  VAL n 
3 92  TYR n 
3 93  TYR n 
3 94  CYS n 
3 95  GLN n 
3 96  GLN n 
3 97  TYR n 
3 98  TYR n 
3 99  SER n 
3 100 THR n 
3 101 PRO n 
3 102 TYR n 
3 103 THR n 
3 104 PHE n 
3 105 GLY n 
3 106 GLN n 
3 107 GLY n 
3 108 THR n 
3 109 LYS n 
3 110 VAL n 
3 111 GLU n 
3 112 ILE n 
3 113 LYS n 
3 114 ARG n 
3 115 THR n 
3 116 VAL n 
3 117 ALA n 
3 118 ALA n 
3 119 PRO n 
3 120 SER n 
3 121 VAL n 
3 122 PHE n 
3 123 ILE n 
3 124 PHE n 
3 125 PRO n 
3 126 PRO n 
3 127 SER n 
3 128 ASP n 
3 129 GLU n 
3 130 GLN n 
3 131 LEU n 
3 132 LYS n 
3 133 SER n 
3 134 GLY n 
3 135 THR n 
3 136 ALA n 
3 137 SER n 
3 138 VAL n 
3 139 VAL n 
3 140 CYS n 
3 141 LEU n 
3 142 LEU n 
3 143 ASN n 
3 144 ASN n 
3 145 PHE n 
3 146 TYR n 
3 147 PRO n 
3 148 ARG n 
3 149 GLU n 
3 150 ALA n 
3 151 LYS n 
3 152 VAL n 
3 153 GLN n 
3 154 TRP n 
3 155 LYS n 
3 156 VAL n 
3 157 ASP n 
3 158 ASN n 
3 159 ALA n 
3 160 LEU n 
3 161 GLN n 
3 162 SER n 
3 163 GLY n 
3 164 ASN n 
3 165 SER n 
3 166 GLN n 
3 167 GLU n 
3 168 SER n 
3 169 VAL n 
3 170 THR n 
3 171 GLU n 
3 172 GLN n 
3 173 ASP n 
3 174 SER n 
3 175 LYS n 
3 176 ASP n 
3 177 SER n 
3 178 THR n 
3 179 TYR n 
3 180 SER n 
3 181 LEU n 
3 182 SER n 
3 183 SER n 
3 184 THR n 
3 185 LEU n 
3 186 THR n 
3 187 LEU n 
3 188 SER n 
3 189 LYS n 
3 190 ALA n 
3 191 ASP n 
3 192 TYR n 
3 193 GLU n 
3 194 LYS n 
3 195 HIS n 
3 196 LYS n 
3 197 VAL n 
3 198 TYR n 
3 199 ALA n 
3 200 CYS n 
3 201 GLU n 
3 202 VAL n 
3 203 THR n 
3 204 HIS n 
3 205 GLN n 
3 206 GLY n 
3 207 LEU n 
3 208 SER n 
3 209 SER n 
3 210 PRO n 
3 211 VAL n 
3 212 THR n 
3 213 LYS n 
3 214 SER n 
3 215 PHE n 
3 216 ASN n 
3 217 ARG n 
3 218 GLY n 
3 219 GLU n 
3 220 CYS n 
3 221 SER 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' 1 231 2019-nCoV ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? 
? ? ? ? ? ? 'cabbage looper' 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 222 Human     ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? Human            'Homo sapiens'    9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 221 Human     ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? Human            'Homo sapiens'    9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 SPIKE_SARS2 P0DTC2 ? 1 
;RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYAD
SFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGST
PCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF
;
319 
2 PDB 6ZLR        6ZLR   ? 2 ? 1   
3 PDB 6ZLR        6ZLR   ? 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 6ZLR EEE 1 ? 223 ? P0DTC2 319 ? 541 ? 319 541 
2 2 6ZLR HHH 1 ? 222 ? 6ZLR   1   ? 222 ? 1   222 
3 3 6ZLR LLL 1 ? 221 ? 6ZLR   1   ? 221 ? 1   221 
4 1 6ZLR AAA 1 ? 223 ? P0DTC2 319 ? 541 ? 319 541 
5 2 6ZLR BBB 1 ? 222 ? 6ZLR   1   ? 222 ? 1   222 
6 3 6ZLR CCC 1 ? 221 ? 6ZLR   1   ? 221 ? 1   221 
7 1 6ZLR DDD 1 ? 223 ? P0DTC2 319 ? 541 ? 319 541 
8 2 6ZLR FFF 1 ? 222 ? 6ZLR   1   ? 222 ? 1   222 
9 3 6ZLR GGG 1 ? 221 ? 6ZLR   1   ? 221 ? 1   221 
# 
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 6ZLR SER EEE 224 ? UNP P0DTC2 ? ? 'expression tag' 542 1  
1 6ZLR GLY EEE 225 ? UNP P0DTC2 ? ? 'expression tag' 543 2  
1 6ZLR HIS EEE 226 ? UNP P0DTC2 ? ? 'expression tag' 544 3  
1 6ZLR HIS EEE 227 ? UNP P0DTC2 ? ? 'expression tag' 545 4  
1 6ZLR HIS EEE 228 ? UNP P0DTC2 ? ? 'expression tag' 546 5  
1 6ZLR HIS EEE 229 ? UNP P0DTC2 ? ? 'expression tag' 547 6  
1 6ZLR HIS EEE 230 ? UNP P0DTC2 ? ? 'expression tag' 548 7  
1 6ZLR HIS EEE 231 ? UNP P0DTC2 ? ? 'expression tag' 549 8  
4 6ZLR SER AAA 224 ? UNP P0DTC2 ? ? 'expression tag' 542 9  
4 6ZLR GLY AAA 225 ? UNP P0DTC2 ? ? 'expression tag' 543 10 
4 6ZLR HIS AAA 226 ? UNP P0DTC2 ? ? 'expression tag' 544 11 
4 6ZLR HIS AAA 227 ? UNP P0DTC2 ? ? 'expression tag' 545 12 
4 6ZLR HIS AAA 228 ? UNP P0DTC2 ? ? 'expression tag' 546 13 
4 6ZLR HIS AAA 229 ? UNP P0DTC2 ? ? 'expression tag' 547 14 
4 6ZLR HIS AAA 230 ? UNP P0DTC2 ? ? 'expression tag' 548 15 
4 6ZLR HIS AAA 231 ? UNP P0DTC2 ? ? 'expression tag' 549 16 
7 6ZLR SER DDD 224 ? UNP P0DTC2 ? ? 'expression tag' 542 17 
7 6ZLR GLY DDD 225 ? UNP P0DTC2 ? ? 'expression tag' 543 18 
7 6ZLR HIS DDD 226 ? UNP P0DTC2 ? ? 'expression tag' 544 19 
7 6ZLR HIS DDD 227 ? UNP P0DTC2 ? ? 'expression tag' 545 20 
7 6ZLR HIS DDD 228 ? UNP P0DTC2 ? ? 'expression tag' 546 21 
7 6ZLR HIS DDD 229 ? UNP P0DTC2 ? ? 'expression tag' 547 22 
7 6ZLR HIS DDD 230 ? UNP P0DTC2 ? ? 'expression tag' 548 23 
7 6ZLR HIS DDD 231 ? UNP P0DTC2 ? ? 'expression tag' 549 24 
# 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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                   6ZLR 
_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            5.13 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         76.02 
_exptl_crystal.description                 'Thin Rod' 
_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              7.7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M SODIUM MALONATE, 0.1 M TRIS PH 7.7, 22% W/V POLYETHYLENE GLYCOL 1,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-05-20 
_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   0.9999 
_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                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6ZLR 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.09 
_reflns.d_resolution_low                 68.028 
_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                       72060 
_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             91.1 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  4.7 
_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            4.6 
_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                  ? 
_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                     0.933 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.09 
_reflns_shell.d_res_low                   3.16 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.5 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           4356 
_reflns_shell.percent_possible_all        90.6 
_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             4.6 
_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             ? 
_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                0.415 
_reflns_shell.pdbx_CC_star                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            0.063 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            0.063 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -0.125 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               55.640 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.885 
_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                                 6ZLR 
_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                            3.100 
_refine.ls_d_res_low                             68.028 
_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                     71615 
_refine.ls_number_reflns_R_free                  3669 
_refine.ls_number_reflns_R_work                  67946 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.525 
_refine.ls_percent_reflns_R_free                 5.123 
_refine.ls_R_factor_all                          0.219 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2472 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2176 
_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                      ? 
_refine.ls_wR_factor_R_work                      ? 
_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                      6W41 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.908 
_refine.pdbx_overall_ESU_R_Free                  0.375 
_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                             19.006 
_refine.overall_SU_ML                            0.303 
_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                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.100 
_refine_hist.d_res_low                        68.028 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               14736 
_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        14694 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_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' ? 0.008  0.013   15134 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017   13355 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.548  1.650   20619 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.227  1.573   31205 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.622  5.000   1902  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 35.099 23.393  672   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.873 15.000  2364  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.110 15.000  51    ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.057  0.200   1986  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020   16981 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020   3130  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.183  0.200   2181  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.189  0.200   12015 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.169  0.200   7262  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.078  0.200   6876  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200   217   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.210  0.200   8     ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200   50    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.187  0.200   2     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 4.992  5.871   7635  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.992  5.870   7634  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 8.047  8.792   9528  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 8.047  8.793   9529  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.153  6.224   7499  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.149  6.223   7497  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 8.243  9.157   11091 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 8.243  9.157   11091 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 13.544 110.057 59019 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 13.544 110.056 59019 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.025  0.050   6128  ? r_ncsr_local_group_1           ? ? 
'X-RAY DIFFRACTION' ? 0.023  0.050   6134  ? r_ncsr_local_group_2           ? ? 
'X-RAY DIFFRACTION' ? 0.023  0.050   6545  ? r_ncsr_local_group_3           ? ? 
'X-RAY DIFFRACTION' ? 0.029  0.050   6557  ? r_ncsr_local_group_4           ? ? 
'X-RAY DIFFRACTION' ? 0.031  0.050   6804  ? r_ncsr_local_group_5           ? ? 
'X-RAY DIFFRACTION' ? 0.027  0.050   6770  ? r_ncsr_local_group_6           ? ? 
'X-RAY DIFFRACTION' ? 0.024  0.050   6153  ? r_ncsr_local_group_7           ? ? 
'X-RAY DIFFRACTION' ? 0.030  0.050   6544  ? r_ncsr_local_group_8           ? ? 
'X-RAY DIFFRACTION' ? 0.039  0.050   6757  ? r_ncsr_local_group_9           ? ? 
# 
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' 3.100  3.180  . . 291 5035 92.0498 . . . 0.357 . 0.350 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.180  3.268  . . 239 4921 91.9950 . . . 0.345 . 0.319 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.268  3.362  . . 257 4791 92.0664 . . . 0.334 . 0.299 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.362  3.466  . . 262 4616 91.8471 . . . 0.307 . 0.283 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.466  3.579  . . 258 4498 91.8679 . . . 0.306 . 0.264 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.579  3.705  . . 266 4323 91.6883 . . . 0.272 . 0.246 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.705  3.845  . . 195 4196 91.0052 . . . 0.282 . 0.230 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.845  4.001  . . 199 4045 91.1121 . . . 0.252 . 0.218 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.001  4.179  . . 209 3836 90.8172 . . . 0.264 . 0.210 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.179  4.383  . . 205 3671 90.6879 . . . 0.197 . 0.182 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.383  4.620  . . 173 3529 90.5135 . . . 0.189 . 0.159 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.620  4.900  . . 167 3326 90.4220 . . . 0.167 . 0.160 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.900  5.238  . . 150 3124 89.6004 . . . 0.211 . 0.162 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.238  5.657  . . 158 2864 88.8040 . . . 0.180 . 0.172 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.657  6.196  . . 159 2614 88.2559 . . . 0.220 . 0.176 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.196  6.926  . . 120 2406 87.7083 . . . 0.194 . 0.161 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.926  7.994  . . 141 2111 88.0375 . . . 0.187 . 0.164 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 7.994  9.783  . . 106 1789 87.4078 . . . 0.216 . 0.174 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 9.783  13.805 . . 82  1423 86.5938 . . . 0.237 . 0.207 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 13.805 68.028 . . 32  828  83.2527 . . . 0.360 . 0.325 . . . . . . . . . . . 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 'Chains E A' 1 
2 'Chains E D' 2 
3 'Chains H B' 3 
4 'Chains H F' 4 
5 'Chains L C' 5 
6 'Chains L G' 6 
7 'Chains A D' 7 
8 'Chains B F' 8 
9 'Chains C G' 9 
# 
loop_
_struct_ncs_ens.details 
_struct_ncs_ens.id 
_struct_ncs_ens.point_group 
? 1 ? 
? 2 ? 
? 3 ? 
? 4 ? 
? 5 ? 
? 6 ? 
? 7 ? 
? 8 ? 
? 9 ? 
# 
_struct.entry_id                     6ZLR 
_struct.title                        
'Soaking competent crystal form of the SARS-CoV-2 Receptor Binding Domain (RBD):CR3022 complex.' 
_struct.pdbx_descriptor              'Spike glycoprotein, CR3022 FAB HEAVY CHAIN, CR3022 FAB LIGHT CHAIN' 
_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        6ZLR 
_struct_keywords.text            'SARS-COV-2, VIRAL PROTEIN COMPLEX, ANTIBODY, 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 2 ? 
C N N 3 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 1 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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 PHE A 20  ? ASN A 25  ? PHE EEE 338 ASN EEE 343 1 ? 6 
HELX_P HELX_P2  AA2 TYR A 47  ? ASN A 52  ? TYR EEE 365 ASN EEE 370 1 ? 6 
HELX_P HELX_P3  AA3 SER A 65  ? LEU A 69  ? SER EEE 383 LEU EEE 387 5 ? 5 
HELX_P HELX_P4  AA4 ASP A 87  ? ILE A 92  ? ASP EEE 405 ILE EEE 410 5 ? 6 
HELX_P HELX_P5  AA5 GLY A 98  ? ASN A 104 ? GLY EEE 416 ASN EEE 422 1 ? 7 
HELX_P HELX_P6  AA6 PRO B 62  ? GLN B 65  ? PRO HHH 62  GLN HHH 65  5 ? 4 
HELX_P HELX_P7  AA7 LYS B 87  ? THR B 91  ? LYS HHH 87  THR HHH 91  5 ? 5 
HELX_P HELX_P8  AA8 SER B 162 ? ALA B 164 ? SER HHH 162 ALA HHH 164 5 ? 3 
HELX_P HELX_P9  AA9 SER B 193 ? GLY B 196 ? SER HHH 193 GLY HHH 196 5 ? 4 
HELX_P HELX_P10 AB1 LYS B 207 ? ASN B 210 ? LYS HHH 207 ASN HHH 210 5 ? 4 
HELX_P HELX_P11 AB2 GLN C 85  ? VAL C 89  ? GLN LLL 85  VAL LLL 89  5 ? 5 
HELX_P HELX_P12 AB3 SER C 127 ? GLY C 134 ? SER LLL 127 GLY LLL 134 1 ? 8 
HELX_P HELX_P13 AB4 LYS C 189 ? GLU C 193 ? LYS LLL 189 GLU LLL 193 1 ? 5 
HELX_P HELX_P14 AB5 PHE D 20  ? ASN D 25  ? PHE AAA 338 ASN AAA 343 1 ? 6 
HELX_P HELX_P15 AB6 TYR D 47  ? ASN D 52  ? TYR AAA 365 ASN AAA 370 1 ? 6 
HELX_P HELX_P16 AB7 SER D 65  ? LEU D 69  ? SER AAA 383 LEU AAA 387 5 ? 5 
HELX_P HELX_P17 AB8 ASP D 87  ? ILE D 92  ? ASP AAA 405 ILE AAA 410 5 ? 6 
HELX_P HELX_P18 AB9 GLY D 98  ? ASN D 104 ? GLY AAA 416 ASN AAA 422 1 ? 7 
HELX_P HELX_P19 AC1 LYS E 87  ? THR E 91  ? LYS BBB 87  THR BBB 91  5 ? 5 
HELX_P HELX_P20 AC2 SER E 162 ? ALA E 164 ? SER BBB 162 ALA BBB 164 5 ? 3 
HELX_P HELX_P21 AC3 SER E 193 ? GLY E 196 ? SER BBB 193 GLY BBB 196 5 ? 4 
HELX_P HELX_P22 AC4 LYS E 207 ? ASN E 210 ? LYS BBB 207 ASN BBB 210 5 ? 4 
HELX_P HELX_P23 AC5 GLN F 85  ? VAL F 89  ? GLN CCC 85  VAL CCC 89  5 ? 5 
HELX_P HELX_P24 AC6 SER F 127 ? GLY F 134 ? SER CCC 127 GLY CCC 134 1 ? 8 
HELX_P HELX_P25 AC7 LYS F 189 ? GLU F 193 ? LYS CCC 189 GLU CCC 193 1 ? 5 
HELX_P HELX_P26 AC8 PHE G 20  ? ASN G 25  ? PHE DDD 338 ASN DDD 343 1 ? 6 
HELX_P HELX_P27 AC9 TYR G 47  ? ASN G 52  ? TYR DDD 365 ASN DDD 370 1 ? 6 
HELX_P HELX_P28 AD1 SER G 65  ? LEU G 69  ? SER DDD 383 LEU DDD 387 5 ? 5 
HELX_P HELX_P29 AD2 ASP G 87  ? ILE G 92  ? ASP DDD 405 ILE DDD 410 5 ? 6 
HELX_P HELX_P30 AD3 GLY G 98  ? ASN G 104 ? GLY DDD 416 ASN DDD 422 1 ? 7 
HELX_P HELX_P31 AD4 PRO H 62  ? GLN H 65  ? PRO FFF 62  GLN FFF 65  5 ? 4 
HELX_P HELX_P32 AD5 LYS H 87  ? THR H 91  ? LYS FFF 87  THR FFF 91  5 ? 5 
HELX_P HELX_P33 AD6 SER H 162 ? ALA H 164 ? SER FFF 162 ALA FFF 164 5 ? 3 
HELX_P HELX_P34 AD7 SER H 193 ? GLY H 196 ? SER FFF 193 GLY FFF 196 5 ? 4 
HELX_P HELX_P35 AD8 LYS H 207 ? ASN H 210 ? LYS FFF 207 ASN FFF 210 5 ? 4 
HELX_P HELX_P36 AD9 GLN I 85  ? VAL I 89  ? GLN GGG 85  VAL GGG 89  5 ? 5 
HELX_P HELX_P37 AE1 SER I 127 ? GLY I 134 ? SER GGG 127 GLY GGG 134 1 ? 8 
HELX_P HELX_P38 AE2 LYS I 189 ? LYS I 194 ? LYS GGG 189 LYS GGG 194 1 ? 6 
# 
_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 ?   ? A CYS 18  SG  ? ? ? 1_555 A CYS 43  SG ? ? EEE CYS 336 EEE CYS 361 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
disulf2  disulf ?   ? A CYS 61  SG  ? ? ? 1_555 A CYS 114 SG ? ? EEE CYS 379 EEE CYS 432 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
disulf3  disulf ?   ? A CYS 73  SG  ? ? ? 1_555 A CYS 207 SG ? ? EEE CYS 391 EEE CYS 525 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf4  disulf ?   ? A CYS 162 SG  ? ? ? 1_555 A CYS 170 SG ? ? EEE CYS 480 EEE CYS 488 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf5  disulf ?   ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? HHH CYS 22  HHH CYS 96  1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf6  disulf ?   ? B CYS 146 SG  ? ? ? 1_555 B CYS 202 SG ? ? HHH CYS 146 HHH CYS 202 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
disulf7  disulf ?   ? C CYS 23  SG  ? ? ? 1_555 C CYS 94  SG ? ? LLL CYS 23  LLL CYS 94  1_555 ? ? ? ? ? ? ? 2.112 ? ? 
disulf8  disulf ?   ? C CYS 140 SG  ? ? ? 1_555 C CYS 200 SG ? ? LLL CYS 140 LLL CYS 200 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
disulf9  disulf ?   ? D CYS 18  SG  ? ? ? 1_555 D CYS 43  SG ? ? AAA CYS 336 AAA CYS 361 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf10 disulf ?   ? D CYS 61  SG  ? ? ? 1_555 D CYS 114 SG ? ? AAA CYS 379 AAA CYS 432 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf11 disulf ?   ? D CYS 73  SG  ? ? ? 1_555 D CYS 207 SG ? ? AAA CYS 391 AAA CYS 525 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf12 disulf ?   ? D CYS 162 SG  ? ? ? 1_555 D CYS 170 SG ? ? AAA CYS 480 AAA CYS 488 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf13 disulf ?   ? E CYS 22  SG  ? ? ? 1_555 E CYS 96  SG ? ? BBB CYS 22  BBB CYS 96  1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf14 disulf ?   ? E CYS 146 SG  ? ? ? 1_555 E CYS 202 SG ? ? BBB CYS 146 BBB CYS 202 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
disulf15 disulf ?   ? F CYS 23  SG  ? ? ? 1_555 F CYS 94  SG ? ? CCC CYS 23  CCC CYS 94  1_555 ? ? ? ? ? ? ? 2.112 ? ? 
disulf16 disulf ?   ? F CYS 140 SG  ? ? ? 1_555 F CYS 200 SG ? ? CCC CYS 140 CCC CYS 200 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
disulf17 disulf ?   ? G CYS 18  SG  ? ? ? 1_555 G CYS 43  SG ? ? DDD CYS 336 DDD CYS 361 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf18 disulf ?   ? G CYS 61  SG  ? ? ? 1_555 G CYS 114 SG ? ? DDD CYS 379 DDD CYS 432 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
disulf19 disulf ?   ? G CYS 73  SG  ? ? ? 1_555 G CYS 207 SG ? ? DDD CYS 391 DDD CYS 525 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf20 disulf ?   ? G CYS 162 SG  ? ? ? 1_555 G CYS 170 SG ? ? DDD CYS 480 DDD CYS 488 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
disulf21 disulf ?   ? H CYS 22  SG  ? ? ? 1_555 H CYS 96  SG ? ? FFF CYS 22  FFF CYS 96  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf22 disulf ?   ? H CYS 146 SG  ? ? ? 1_555 H CYS 202 SG ? ? FFF CYS 146 FFF CYS 202 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
disulf23 disulf ?   ? I CYS 23  SG  ? ? ? 1_555 I CYS 94  SG ? ? GGG CYS 23  GGG CYS 94  1_555 ? ? ? ? ? ? ? 2.111 ? ? 
disulf24 disulf ?   ? I CYS 140 SG  ? ? ? 1_555 I CYS 200 SG ? ? GGG CYS 140 GGG CYS 200 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
covale1  covale one ? A ASN 25  ND2 ? ? ? 1_555 J NAG .   C1 ? ? EEE ASN 343 EEE NAG 601 1_555 ? ? ? ? ? ? ? 1.398 ? 
N-Glycosylation 
covale2  covale one ? G ASN 25  ND2 ? ? ? 1_555 L NAG .   C1 ? ? DDD ASN 343 DDD NAG 601 1_555 ? ? ? ? ? ? ? 1.428 ? 
N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 152 B . ? PHE 152 HHH PRO 153 B ? PRO 153 HHH 1 -8.31 
2  GLU 154 B . ? GLU 154 HHH PRO 155 B ? PRO 155 HHH 1 -5.90 
3  SER 7   C . ? SER 7   LLL PRO 8   C ? PRO 8   LLL 1 -9.76 
4  THR 100 C . ? THR 100 LLL PRO 101 C ? PRO 101 LLL 1 3.57  
5  TYR 146 C . ? TYR 146 LLL PRO 147 C ? PRO 147 LLL 1 -3.11 
6  PHE 152 E . ? PHE 152 BBB PRO 153 E ? PRO 153 BBB 1 -8.53 
7  GLU 154 E . ? GLU 154 BBB PRO 155 E ? PRO 155 BBB 1 -8.35 
8  SER 7   F . ? SER 7   CCC PRO 8   F ? PRO 8   CCC 1 -7.04 
9  THR 100 F . ? THR 100 CCC PRO 101 F ? PRO 101 CCC 1 2.91  
10 TYR 146 F . ? TYR 146 CCC PRO 147 F ? PRO 147 CCC 1 -3.47 
11 PHE 152 H . ? PHE 152 FFF PRO 153 H ? PRO 153 FFF 1 -7.84 
12 GLU 154 H . ? GLU 154 FFF PRO 155 H ? PRO 155 FFF 1 -5.86 
13 SER 7   I . ? SER 7   GGG PRO 8   I ? PRO 8   GGG 1 -9.08 
14 THR 100 I . ? THR 100 GGG PRO 101 I ? PRO 101 GGG 1 2.99  
15 TYR 146 I . ? TYR 146 GGG PRO 147 I ? PRO 147 GGG 1 -2.51 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 3 ? 
AB2 ? 4 ? 
AB3 ? 6 ? 
AB4 ? 4 ? 
AB5 ? 2 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 3 ? 
AC1 ? 2 ? 
AC2 ? 2 ? 
AC3 ? 4 ? 
AC4 ? 6 ? 
AC5 ? 4 ? 
AC6 ? 4 ? 
AC7 ? 4 ? 
AC8 ? 3 ? 
AC9 ? 4 ? 
AD1 ? 6 ? 
AD2 ? 4 ? 
AD3 ? 2 ? 
AD4 ? 4 ? 
AD5 ? 4 ? 
AD6 ? 5 ? 
AD7 ? 3 ? 
AD8 ? 2 ? 
AD9 ? 2 ? 
AE1 ? 4 ? 
AE2 ? 6 ? 
AE3 ? 4 ? 
AE4 ? 4 ? 
AE5 ? 4 ? 
AE6 ? 3 ? 
AE7 ? 4 ? 
AE8 ? 6 ? 
AE9 ? 4 ? 
AF1 ? 2 ? 
AF2 ? 4 ? 
AF3 ? 4 ? 
# 
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 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? 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 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB3 5 6 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? 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 ? parallel      
AB9 2 3 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC4 4 5 ? anti-parallel 
AC4 5 6 ? anti-parallel 
AC5 1 2 ? parallel      
AC5 2 3 ? anti-parallel 
AC5 3 4 ? 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 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? parallel      
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD1 4 5 ? anti-parallel 
AD1 5 6 ? anti-parallel 
AD2 1 2 ? parallel      
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD6 4 5 ? anti-parallel 
AD7 1 2 ? parallel      
AD7 2 3 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? parallel      
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE2 4 5 ? anti-parallel 
AE2 5 6 ? anti-parallel 
AE3 1 2 ? parallel      
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? anti-parallel 
AE8 1 2 ? parallel      
AE8 2 3 ? anti-parallel 
AE8 3 4 ? anti-parallel 
AE8 4 5 ? anti-parallel 
AE8 5 6 ? anti-parallel 
AE9 1 2 ? parallel      
AE9 2 3 ? anti-parallel 
AE9 3 4 ? anti-parallel 
AF1 1 2 ? anti-parallel 
AF2 1 2 ? anti-parallel 
AF2 2 3 ? anti-parallel 
AF2 3 4 ? anti-parallel 
AF3 1 2 ? anti-parallel 
AF3 2 3 ? anti-parallel 
AF3 3 4 ? 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 ASN A 36  ? ILE A 40  ? ASN EEE 354 ILE EEE 358 
AA1 2 ASN A 76  ? ARG A 85  ? ASN EEE 394 ARG EEE 403 
AA1 3 PRO A 189 ? GLU A 198 ? PRO EEE 507 GLU EEE 516 
AA1 4 GLY A 113 ? ASN A 119 ? GLY EEE 431 ASN EEE 437 
AA1 5 THR A 58  ? TYR A 62  ? THR EEE 376 TYR EEE 380 
AA2 1 CYS A 43  ? VAL A 44  ? CYS EEE 361 VAL EEE 362 
AA2 2 VAL A 206 ? CYS A 207 ? VAL EEE 524 CYS EEE 525 
AA2 3 CYS A 73  ? PHE A 74  ? CYS EEE 391 PHE EEE 392 
AA3 1 LEU A 134 ? ARG A 136 ? LEU EEE 452 ARG EEE 454 
AA3 2 LEU A 174 ? SER A 176 ? LEU EEE 492 SER EEE 494 
AA4 1 TYR A 155 ? GLN A 156 ? TYR EEE 473 GLN EEE 474 
AA4 2 CYS A 170 ? TYR A 171 ? CYS EEE 488 TYR EEE 489 
AA5 1 GLN B 3   ? GLN B 6   ? GLN HHH 3   GLN HHH 6   
AA5 2 LEU B 18  ? SER B 25  ? LEU HHH 18  SER HHH 25  
AA5 3 THR B 78  ? TRP B 83  ? THR HHH 78  TRP HHH 83  
AA5 4 THR B 69  ? ASP B 73  ? THR HHH 69  ASP HHH 73  
AA6 1 GLU B 10  ? LYS B 12  ? GLU HHH 10  LYS HHH 12  
AA6 2 THR B 113 ? VAL B 117 ? THR HHH 113 VAL HHH 117 
AA6 3 ALA B 92  ? GLY B 99  ? ALA HHH 92  GLY HHH 99  
AA6 4 TRP B 33  ? GLN B 39  ? TRP HHH 33  GLN HHH 39  
AA6 5 LEU B 45  ? TYR B 52  ? LEU HHH 45  TYR HHH 52  
AA6 6 GLU B 57  ? TYR B 60  ? GLU HHH 57  TYR HHH 60  
AA7 1 GLU B 10  ? LYS B 12  ? GLU HHH 10  LYS HHH 12  
AA7 2 THR B 113 ? VAL B 117 ? THR HHH 113 VAL HHH 117 
AA7 3 ALA B 92  ? GLY B 99  ? ALA HHH 92  GLY HHH 99  
AA7 4 VAL B 108 ? TRP B 109 ? VAL HHH 108 TRP HHH 109 
AA8 1 SER B 126 ? LEU B 130 ? SER HHH 126 LEU HHH 130 
AA8 2 THR B 141 ? TYR B 151 ? THR HHH 141 TYR HHH 151 
AA8 3 TYR B 182 ? PRO B 191 ? TYR HHH 182 PRO HHH 191 
AA8 4 VAL B 169 ? THR B 171 ? VAL HHH 169 THR HHH 171 
AA9 1 SER B 126 ? LEU B 130 ? SER HHH 126 LEU HHH 130 
AA9 2 THR B 141 ? TYR B 151 ? THR HHH 141 TYR HHH 151 
AA9 3 TYR B 182 ? PRO B 191 ? TYR HHH 182 PRO HHH 191 
AA9 4 VAL B 175 ? LEU B 176 ? VAL HHH 175 LEU HHH 176 
AB1 1 THR B 157 ? TRP B 160 ? THR HHH 157 TRP HHH 160 
AB1 2 TYR B 200 ? HIS B 206 ? TYR HHH 200 HIS HHH 206 
AB1 3 THR B 211 ? VAL B 217 ? THR HHH 211 VAL HHH 217 
AB2 1 LEU C 4   ? SER C 7   ? LEU LLL 4   SER LLL 7   
AB2 2 ALA C 19  ? SER C 25  ? ALA LLL 19  SER LLL 25  
AB2 3 ASP C 76  ? ILE C 81  ? ASP LLL 76  ILE LLL 81  
AB2 4 PHE C 68  ? SER C 73  ? PHE LLL 68  SER LLL 73  
AB3 1 SER C 10  ? VAL C 13  ? SER LLL 10  VAL LLL 13  
AB3 2 THR C 108 ? ILE C 112 ? THR LLL 108 ILE LLL 112 
AB3 3 ALA C 90  ? GLN C 96  ? ALA LLL 90  GLN LLL 96  
AB3 4 LEU C 39  ? GLN C 44  ? LEU LLL 39  GLN LLL 44  
AB3 5 LYS C 51  ? TYR C 55  ? LYS LLL 51  TYR LLL 55  
AB3 6 THR C 59  ? ARG C 60  ? THR LLL 59  ARG LLL 60  
AB4 1 SER C 10  ? VAL C 13  ? SER LLL 10  VAL LLL 13  
AB4 2 THR C 108 ? ILE C 112 ? THR LLL 108 ILE LLL 112 
AB4 3 ALA C 90  ? GLN C 96  ? ALA LLL 90  GLN LLL 96  
AB4 4 THR C 103 ? PHE C 104 ? THR LLL 103 PHE LLL 104 
AB5 1 LEU C 30  ? TYR C 31  ? LEU LLL 30  TYR LLL 31  
AB5 2 LYS C 36  ? ASN C 37  ? LYS LLL 36  ASN LLL 37  
AB6 1 SER C 120 ? PHE C 124 ? SER LLL 120 PHE LLL 124 
AB6 2 THR C 135 ? PHE C 145 ? THR LLL 135 PHE LLL 145 
AB6 3 TYR C 179 ? SER C 188 ? TYR LLL 179 SER LLL 188 
AB6 4 SER C 165 ? GLN C 166 ? SER LLL 165 GLN LLL 166 
AB7 1 ALA C 159 ? GLN C 161 ? ALA LLL 159 GLN LLL 161 
AB7 2 ALA C 150 ? VAL C 156 ? ALA LLL 150 VAL LLL 156 
AB7 3 VAL C 197 ? HIS C 204 ? VAL LLL 197 HIS LLL 204 
AB7 4 VAL C 211 ? ASN C 216 ? VAL LLL 211 ASN LLL 216 
AB8 1 ASN D 36  ? ILE D 40  ? ASN AAA 354 ILE AAA 358 
AB8 2 ASN D 76  ? ARG D 85  ? ASN AAA 394 ARG AAA 403 
AB8 3 PRO D 189 ? GLU D 198 ? PRO AAA 507 GLU AAA 516 
AB8 4 GLY D 113 ? ASN D 119 ? GLY AAA 431 ASN AAA 437 
AB8 5 THR D 58  ? TYR D 62  ? THR AAA 376 TYR AAA 380 
AB9 1 CYS D 43  ? VAL D 44  ? CYS AAA 361 VAL AAA 362 
AB9 2 VAL D 206 ? CYS D 207 ? VAL AAA 524 CYS AAA 525 
AB9 3 CYS D 73  ? PHE D 74  ? CYS AAA 391 PHE AAA 392 
AC1 1 LEU D 134 ? ARG D 136 ? LEU AAA 452 ARG AAA 454 
AC1 2 LEU D 174 ? SER D 176 ? LEU AAA 492 SER AAA 494 
AC2 1 TYR D 155 ? GLN D 156 ? TYR AAA 473 GLN AAA 474 
AC2 2 CYS D 170 ? TYR D 171 ? CYS AAA 488 TYR AAA 489 
AC3 1 GLN E 3   ? GLN E 6   ? GLN BBB 3   GLN BBB 6   
AC3 2 LEU E 18  ? SER E 25  ? LEU BBB 18  SER BBB 25  
AC3 3 THR E 78  ? TRP E 83  ? THR BBB 78  TRP BBB 83  
AC3 4 THR E 69  ? ASP E 73  ? THR BBB 69  ASP BBB 73  
AC4 1 GLU E 10  ? LYS E 12  ? GLU BBB 10  LYS BBB 12  
AC4 2 THR E 113 ? VAL E 117 ? THR BBB 113 VAL BBB 117 
AC4 3 ALA E 92  ? GLY E 99  ? ALA BBB 92  GLY BBB 99  
AC4 4 TRP E 33  ? GLN E 39  ? TRP BBB 33  GLN BBB 39  
AC4 5 LEU E 45  ? TYR E 52  ? LEU BBB 45  TYR BBB 52  
AC4 6 GLU E 57  ? TYR E 60  ? GLU BBB 57  TYR BBB 60  
AC5 1 GLU E 10  ? LYS E 12  ? GLU BBB 10  LYS BBB 12  
AC5 2 THR E 113 ? VAL E 117 ? THR BBB 113 VAL BBB 117 
AC5 3 ALA E 92  ? GLY E 99  ? ALA BBB 92  GLY BBB 99  
AC5 4 VAL E 108 ? TRP E 109 ? VAL BBB 108 TRP BBB 109 
AC6 1 SER E 126 ? LEU E 130 ? SER BBB 126 LEU BBB 130 
AC6 2 THR E 141 ? TYR E 151 ? THR BBB 141 TYR BBB 151 
AC6 3 TYR E 182 ? PRO E 191 ? TYR BBB 182 PRO BBB 191 
AC6 4 VAL E 169 ? THR E 171 ? VAL BBB 169 THR BBB 171 
AC7 1 SER E 126 ? LEU E 130 ? SER BBB 126 LEU BBB 130 
AC7 2 THR E 141 ? TYR E 151 ? THR BBB 141 TYR BBB 151 
AC7 3 TYR E 182 ? PRO E 191 ? TYR BBB 182 PRO BBB 191 
AC7 4 VAL E 175 ? LEU E 176 ? VAL BBB 175 LEU BBB 176 
AC8 1 THR E 157 ? TRP E 160 ? THR BBB 157 TRP BBB 160 
AC8 2 TYR E 200 ? HIS E 206 ? TYR BBB 200 HIS BBB 206 
AC8 3 THR E 211 ? VAL E 217 ? THR BBB 211 VAL BBB 217 
AC9 1 LEU F 4   ? SER F 7   ? LEU CCC 4   SER CCC 7   
AC9 2 ALA F 19  ? SER F 25  ? ALA CCC 19  SER CCC 25  
AC9 3 ASP F 76  ? ILE F 81  ? ASP CCC 76  ILE CCC 81  
AC9 4 PHE F 68  ? SER F 73  ? PHE CCC 68  SER CCC 73  
AD1 1 SER F 10  ? VAL F 13  ? SER CCC 10  VAL CCC 13  
AD1 2 THR F 108 ? ILE F 112 ? THR CCC 108 ILE CCC 112 
AD1 3 ALA F 90  ? GLN F 96  ? ALA CCC 90  GLN CCC 96  
AD1 4 LEU F 39  ? GLN F 44  ? LEU CCC 39  GLN CCC 44  
AD1 5 LYS F 51  ? TYR F 55  ? LYS CCC 51  TYR CCC 55  
AD1 6 THR F 59  ? ARG F 60  ? THR CCC 59  ARG CCC 60  
AD2 1 SER F 10  ? VAL F 13  ? SER CCC 10  VAL CCC 13  
AD2 2 THR F 108 ? ILE F 112 ? THR CCC 108 ILE CCC 112 
AD2 3 ALA F 90  ? GLN F 96  ? ALA CCC 90  GLN CCC 96  
AD2 4 THR F 103 ? PHE F 104 ? THR CCC 103 PHE CCC 104 
AD3 1 LEU F 30  ? TYR F 31  ? LEU CCC 30  TYR CCC 31  
AD3 2 LYS F 36  ? ASN F 37  ? LYS CCC 36  ASN CCC 37  
AD4 1 SER F 120 ? PHE F 124 ? SER CCC 120 PHE CCC 124 
AD4 2 THR F 135 ? PHE F 145 ? THR CCC 135 PHE CCC 145 
AD4 3 TYR F 179 ? SER F 188 ? TYR CCC 179 SER CCC 188 
AD4 4 SER F 165 ? VAL F 169 ? SER CCC 165 VAL CCC 169 
AD5 1 ALA F 159 ? GLN F 161 ? ALA CCC 159 GLN CCC 161 
AD5 2 ALA F 150 ? VAL F 156 ? ALA CCC 150 VAL CCC 156 
AD5 3 VAL F 197 ? HIS F 204 ? VAL CCC 197 HIS CCC 204 
AD5 4 VAL F 211 ? ASN F 216 ? VAL CCC 211 ASN CCC 216 
AD6 1 ASN G 36  ? ILE G 40  ? ASN DDD 354 ILE DDD 358 
AD6 2 ASN G 76  ? ARG G 85  ? ASN DDD 394 ARG DDD 403 
AD6 3 PRO G 189 ? GLU G 198 ? PRO DDD 507 GLU DDD 516 
AD6 4 GLY G 113 ? ASN G 119 ? GLY DDD 431 ASN DDD 437 
AD6 5 THR G 58  ? TYR G 62  ? THR DDD 376 TYR DDD 380 
AD7 1 CYS G 43  ? VAL G 44  ? CYS DDD 361 VAL DDD 362 
AD7 2 VAL G 206 ? CYS G 207 ? VAL DDD 524 CYS DDD 525 
AD7 3 CYS G 73  ? PHE G 74  ? CYS DDD 391 PHE DDD 392 
AD8 1 LEU G 134 ? ARG G 136 ? LEU DDD 452 ARG DDD 454 
AD8 2 LEU G 174 ? SER G 176 ? LEU DDD 492 SER DDD 494 
AD9 1 TYR G 155 ? GLN G 156 ? TYR DDD 473 GLN DDD 474 
AD9 2 CYS G 170 ? TYR G 171 ? CYS DDD 488 TYR DDD 489 
AE1 1 GLN H 3   ? GLN H 6   ? GLN FFF 3   GLN FFF 6   
AE1 2 LEU H 18  ? SER H 25  ? LEU FFF 18  SER FFF 25  
AE1 3 THR H 78  ? TRP H 83  ? THR FFF 78  TRP FFF 83  
AE1 4 THR H 69  ? ASP H 73  ? THR FFF 69  ASP FFF 73  
AE2 1 GLU H 10  ? LYS H 12  ? GLU FFF 10  LYS FFF 12  
AE2 2 THR H 113 ? VAL H 117 ? THR FFF 113 VAL FFF 117 
AE2 3 ALA H 92  ? GLY H 99  ? ALA FFF 92  GLY FFF 99  
AE2 4 TRP H 33  ? GLN H 39  ? TRP FFF 33  GLN FFF 39  
AE2 5 LEU H 45  ? TYR H 52  ? LEU FFF 45  TYR FFF 52  
AE2 6 GLU H 57  ? TYR H 60  ? GLU FFF 57  TYR FFF 60  
AE3 1 GLU H 10  ? LYS H 12  ? GLU FFF 10  LYS FFF 12  
AE3 2 THR H 113 ? VAL H 117 ? THR FFF 113 VAL FFF 117 
AE3 3 ALA H 92  ? GLY H 99  ? ALA FFF 92  GLY FFF 99  
AE3 4 VAL H 108 ? TRP H 109 ? VAL FFF 108 TRP FFF 109 
AE4 1 SER H 126 ? LEU H 130 ? SER FFF 126 LEU FFF 130 
AE4 2 THR H 141 ? TYR H 151 ? THR FFF 141 TYR FFF 151 
AE4 3 TYR H 182 ? PRO H 191 ? TYR FFF 182 PRO FFF 191 
AE4 4 VAL H 169 ? THR H 171 ? VAL FFF 169 THR FFF 171 
AE5 1 SER H 126 ? LEU H 130 ? SER FFF 126 LEU FFF 130 
AE5 2 THR H 141 ? TYR H 151 ? THR FFF 141 TYR FFF 151 
AE5 3 TYR H 182 ? PRO H 191 ? TYR FFF 182 PRO FFF 191 
AE5 4 VAL H 175 ? LEU H 176 ? VAL FFF 175 LEU FFF 176 
AE6 1 THR H 157 ? TRP H 160 ? THR FFF 157 TRP FFF 160 
AE6 2 TYR H 200 ? HIS H 206 ? TYR FFF 200 HIS FFF 206 
AE6 3 THR H 211 ? VAL H 217 ? THR FFF 211 VAL FFF 217 
AE7 1 LEU I 4   ? SER I 7   ? LEU GGG 4   SER GGG 7   
AE7 2 ALA I 19  ? SER I 25  ? ALA GGG 19  SER GGG 25  
AE7 3 ASP I 76  ? ILE I 81  ? ASP GGG 76  ILE GGG 81  
AE7 4 PHE I 68  ? SER I 73  ? PHE GGG 68  SER GGG 73  
AE8 1 SER I 10  ? VAL I 13  ? SER GGG 10  VAL GGG 13  
AE8 2 THR I 108 ? ILE I 112 ? THR GGG 108 ILE GGG 112 
AE8 3 ALA I 90  ? GLN I 96  ? ALA GGG 90  GLN GGG 96  
AE8 4 LEU I 39  ? GLN I 44  ? LEU GGG 39  GLN GGG 44  
AE8 5 LYS I 51  ? TYR I 55  ? LYS GGG 51  TYR GGG 55  
AE8 6 THR I 59  ? ARG I 60  ? THR GGG 59  ARG GGG 60  
AE9 1 SER I 10  ? VAL I 13  ? SER GGG 10  VAL GGG 13  
AE9 2 THR I 108 ? ILE I 112 ? THR GGG 108 ILE GGG 112 
AE9 3 ALA I 90  ? GLN I 96  ? ALA GGG 90  GLN GGG 96  
AE9 4 THR I 103 ? PHE I 104 ? THR GGG 103 PHE GGG 104 
AF1 1 LEU I 30  ? TYR I 31  ? LEU GGG 30  TYR GGG 31  
AF1 2 LYS I 36  ? ASN I 37  ? LYS GGG 36  ASN GGG 37  
AF2 1 SER I 120 ? PHE I 124 ? SER GGG 120 PHE GGG 124 
AF2 2 THR I 135 ? PHE I 145 ? THR GGG 135 PHE GGG 145 
AF2 3 TYR I 179 ? SER I 188 ? TYR GGG 179 SER GGG 188 
AF2 4 SER I 165 ? GLN I 166 ? SER GGG 165 GLN GGG 166 
AF3 1 ALA I 159 ? LEU I 160 ? ALA GGG 159 LEU GGG 160 
AF3 2 LYS I 151 ? VAL I 156 ? LYS GGG 151 VAL GGG 156 
AF3 3 VAL I 197 ? THR I 203 ? VAL GGG 197 THR GGG 203 
AF3 4 VAL I 211 ? ASN I 216 ? VAL GGG 211 ASN GGG 216 
# 
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 ILE A 40  ? N ILE EEE 358 O VAL A 77  ? O VAL EEE 395 
AA1 2 3 N ILE A 84  ? N ILE EEE 402 O TYR A 190 ? O TYR EEE 508 
AA1 3 4 O VAL A 193 ? O VAL EEE 511 N ILE A 116 ? N ILE EEE 434 
AA1 4 5 O GLY A 113 ? O GLY EEE 431 N TYR A 62  ? N TYR EEE 380 
AA2 1 2 N CYS A 43  ? N CYS EEE 361 O CYS A 207 ? O CYS EEE 525 
AA2 2 3 O VAL A 206 ? O VAL EEE 524 N PHE A 74  ? N PHE EEE 392 
AA3 1 2 N TYR A 135 ? N TYR EEE 453 O GLN A 175 ? O GLN EEE 493 
AA4 1 2 N TYR A 155 ? N TYR EEE 473 O TYR A 171 ? O TYR EEE 489 
AA5 1 2 N VAL B 5   ? N VAL HHH 5   O LYS B 23  ? O LYS HHH 23  
AA5 2 3 N CYS B 22  ? N CYS HHH 22  O ALA B 79  ? O ALA HHH 79  
AA5 3 4 O TYR B 80  ? O TYR HHH 80  N SER B 71  ? N SER HHH 71  
AA6 1 2 N GLU B 10  ? N GLU HHH 10  O THR B 114 ? O THR HHH 114 
AA6 2 3 O VAL B 115 ? O VAL HHH 115 N ALA B 92  ? N ALA HHH 92  
AA6 3 4 O GLY B 99  ? O GLY HHH 99  N TRP B 33  ? N TRP HHH 33  
AA6 4 5 N ARG B 38  ? N ARG HHH 38  O GLU B 46  ? O GLU HHH 46  
AA6 5 6 N ILE B 50  ? N ILE HHH 50  O ARG B 59  ? O ARG HHH 59  
AA7 1 2 N GLU B 10  ? N GLU HHH 10  O THR B 114 ? O THR HHH 114 
AA7 2 3 O VAL B 115 ? O VAL HHH 115 N ALA B 92  ? N ALA HHH 92  
AA7 3 4 N GLY B 98  ? N GLY HHH 98  O VAL B 108 ? O VAL HHH 108 
AA8 1 2 N LEU B 130 ? N LEU HHH 130 O GLY B 145 ? O GLY HHH 145 
AA8 2 3 N TYR B 151 ? N TYR HHH 151 O TYR B 182 ? O TYR HHH 182 
AA8 3 4 O VAL B 187 ? O VAL HHH 187 N HIS B 170 ? N HIS HHH 170 
AA9 1 2 N LEU B 130 ? N LEU HHH 130 O GLY B 145 ? O GLY HHH 145 
AA9 2 3 N TYR B 151 ? N TYR HHH 151 O TYR B 182 ? O TYR HHH 182 
AA9 3 4 O SER B 183 ? O SER HHH 183 N VAL B 175 ? N VAL HHH 175 
AB1 1 2 N SER B 159 ? N SER HHH 159 O ASN B 203 ? O ASN HHH 203 
AB1 2 3 N VAL B 204 ? N VAL HHH 204 O VAL B 213 ? O VAL HHH 213 
AB2 1 2 N SER C 7   ? N SER LLL 7   O ASN C 22  ? O ASN LLL 22  
AB2 2 3 N ALA C 19  ? N ALA LLL 19  O ILE C 81  ? O ILE LLL 81  
AB2 3 4 O THR C 80  ? O THR LLL 80  N SER C 69  ? N SER LLL 69  
AB3 1 2 N LEU C 11  ? N LEU LLL 11  O GLU C 111 ? O GLU LLL 111 
AB3 2 3 O VAL C 110 ? O VAL LLL 110 N ALA C 90  ? N ALA LLL 90  
AB3 3 4 O GLN C 95  ? O GLN LLL 95  N ALA C 40  ? N ALA LLL 40  
AB3 4 5 N GLN C 43  ? N GLN LLL 43  O LYS C 51  ? O LYS LLL 51  
AB3 5 6 N TYR C 55  ? N TYR LLL 55  O THR C 59  ? O THR LLL 59  
AB4 1 2 N LEU C 11  ? N LEU LLL 11  O GLU C 111 ? O GLU LLL 111 
AB4 2 3 O VAL C 110 ? O VAL LLL 110 N ALA C 90  ? N ALA LLL 90  
AB4 3 4 N GLN C 96  ? N GLN LLL 96  O THR C 103 ? O THR LLL 103 
AB5 1 2 N TYR C 31  ? N TYR LLL 31  O LYS C 36  ? O LYS LLL 36  
AB6 1 2 N PHE C 122 ? N PHE LLL 122 O LEU C 141 ? O LEU LLL 141 
AB6 2 3 N CYS C 140 ? N CYS LLL 140 O SER C 183 ? O SER LLL 183 
AB6 3 4 O THR C 184 ? O THR LLL 184 N GLN C 166 ? N GLN LLL 166 
AB7 1 2 O ALA C 159 ? O ALA LLL 159 N VAL C 156 ? N VAL LLL 156 
AB7 2 3 N GLN C 153 ? N GLN LLL 153 O GLU C 201 ? O GLU LLL 201 
AB7 3 4 N VAL C 202 ? N VAL LLL 202 O VAL C 211 ? O VAL LLL 211 
AB8 1 2 N ILE D 40  ? N ILE AAA 358 O VAL D 77  ? O VAL AAA 395 
AB8 2 3 N ILE D 84  ? N ILE AAA 402 O TYR D 190 ? O TYR AAA 508 
AB8 3 4 O VAL D 193 ? O VAL AAA 511 N ILE D 116 ? N ILE AAA 434 
AB8 4 5 O GLY D 113 ? O GLY AAA 431 N TYR D 62  ? N TYR AAA 380 
AB9 1 2 N CYS D 43  ? N CYS AAA 361 O CYS D 207 ? O CYS AAA 525 
AB9 2 3 O VAL D 206 ? O VAL AAA 524 N PHE D 74  ? N PHE AAA 392 
AC1 1 2 N TYR D 135 ? N TYR AAA 453 O GLN D 175 ? O GLN AAA 493 
AC2 1 2 N TYR D 155 ? N TYR AAA 473 O TYR D 171 ? O TYR AAA 489 
AC3 1 2 N VAL E 5   ? N VAL BBB 5   O LYS E 23  ? O LYS BBB 23  
AC3 2 3 N CYS E 22  ? N CYS BBB 22  O ALA E 79  ? O ALA BBB 79  
AC3 3 4 O TYR E 80  ? O TYR BBB 80  N SER E 71  ? N SER BBB 71  
AC4 1 2 N GLU E 10  ? N GLU BBB 10  O THR E 114 ? O THR BBB 114 
AC4 2 3 O VAL E 115 ? O VAL BBB 115 N ALA E 92  ? N ALA BBB 92  
AC4 3 4 O GLY E 99  ? O GLY BBB 99  N TRP E 33  ? N TRP BBB 33  
AC4 4 5 N ARG E 38  ? N ARG BBB 38  O GLU E 46  ? O GLU BBB 46  
AC4 5 6 N ILE E 50  ? N ILE BBB 50  O ARG E 59  ? O ARG BBB 59  
AC5 1 2 N GLU E 10  ? N GLU BBB 10  O THR E 114 ? O THR BBB 114 
AC5 2 3 O VAL E 115 ? O VAL BBB 115 N ALA E 92  ? N ALA BBB 92  
AC5 3 4 N GLY E 98  ? N GLY BBB 98  O VAL E 108 ? O VAL BBB 108 
AC6 1 2 N LEU E 130 ? N LEU BBB 130 O GLY E 145 ? O GLY BBB 145 
AC6 2 3 N TYR E 151 ? N TYR BBB 151 O TYR E 182 ? O TYR BBB 182 
AC6 3 4 O VAL E 187 ? O VAL BBB 187 N HIS E 170 ? N HIS BBB 170 
AC7 1 2 N LEU E 130 ? N LEU BBB 130 O GLY E 145 ? O GLY BBB 145 
AC7 2 3 N TYR E 151 ? N TYR BBB 151 O TYR E 182 ? O TYR BBB 182 
AC7 3 4 O SER E 183 ? O SER BBB 183 N VAL E 175 ? N VAL BBB 175 
AC8 1 2 N SER E 159 ? N SER BBB 159 O ASN E 203 ? O ASN BBB 203 
AC8 2 3 N VAL E 204 ? N VAL BBB 204 O VAL E 213 ? O VAL BBB 213 
AC9 1 2 N SER F 7   ? N SER CCC 7   O ASN F 22  ? O ASN CCC 22  
AC9 2 3 N ALA F 19  ? N ALA CCC 19  O ILE F 81  ? O ILE CCC 81  
AC9 3 4 O THR F 80  ? O THR CCC 80  N SER F 69  ? N SER CCC 69  
AD1 1 2 N LEU F 11  ? N LEU CCC 11  O GLU F 111 ? O GLU CCC 111 
AD1 2 3 O VAL F 110 ? O VAL CCC 110 N ALA F 90  ? N ALA CCC 90  
AD1 3 4 O GLN F 95  ? O GLN CCC 95  N ALA F 40  ? N ALA CCC 40  
AD1 4 5 N GLN F 43  ? N GLN CCC 43  O LYS F 51  ? O LYS CCC 51  
AD1 5 6 N TYR F 55  ? N TYR CCC 55  O THR F 59  ? O THR CCC 59  
AD2 1 2 N LEU F 11  ? N LEU CCC 11  O GLU F 111 ? O GLU CCC 111 
AD2 2 3 O VAL F 110 ? O VAL CCC 110 N ALA F 90  ? N ALA CCC 90  
AD2 3 4 N GLN F 96  ? N GLN CCC 96  O THR F 103 ? O THR CCC 103 
AD3 1 2 N TYR F 31  ? N TYR CCC 31  O LYS F 36  ? O LYS CCC 36  
AD4 1 2 N PHE F 122 ? N PHE CCC 122 O LEU F 141 ? O LEU CCC 141 
AD4 2 3 N CYS F 140 ? N CYS CCC 140 O SER F 183 ? O SER CCC 183 
AD4 3 4 O SER F 182 ? O SER CCC 182 N SER F 168 ? N SER CCC 168 
AD5 1 2 O ALA F 159 ? O ALA CCC 159 N VAL F 156 ? N VAL CCC 156 
AD5 2 3 N GLN F 153 ? N GLN CCC 153 O GLU F 201 ? O GLU CCC 201 
AD5 3 4 N VAL F 202 ? N VAL CCC 202 O VAL F 211 ? O VAL CCC 211 
AD6 1 2 N ILE G 40  ? N ILE DDD 358 O VAL G 77  ? O VAL DDD 395 
AD6 2 3 N ASP G 80  ? N ASP DDD 398 O VAL G 194 ? O VAL DDD 512 
AD6 3 4 O VAL G 193 ? O VAL DDD 511 N ILE G 116 ? N ILE DDD 434 
AD6 4 5 O GLY G 113 ? O GLY DDD 431 N TYR G 62  ? N TYR DDD 380 
AD7 1 2 N CYS G 43  ? N CYS DDD 361 O CYS G 207 ? O CYS DDD 525 
AD7 2 3 O VAL G 206 ? O VAL DDD 524 N PHE G 74  ? N PHE DDD 392 
AD8 1 2 N TYR G 135 ? N TYR DDD 453 O GLN G 175 ? O GLN DDD 493 
AD9 1 2 N TYR G 155 ? N TYR DDD 473 O TYR G 171 ? O TYR DDD 489 
AE1 1 2 N VAL H 5   ? N VAL FFF 5   O LYS H 23  ? O LYS FFF 23  
AE1 2 3 N CYS H 22  ? N CYS FFF 22  O ALA H 79  ? O ALA FFF 79  
AE1 3 4 O TYR H 80  ? O TYR FFF 80  N SER H 71  ? N SER FFF 71  
AE2 1 2 N GLU H 10  ? N GLU FFF 10  O THR H 114 ? O THR FFF 114 
AE2 2 3 O VAL H 115 ? O VAL FFF 115 N ALA H 92  ? N ALA FFF 92  
AE2 3 4 O GLY H 99  ? O GLY FFF 99  N TRP H 33  ? N TRP FFF 33  
AE2 4 5 N ARG H 38  ? N ARG FFF 38  O GLU H 46  ? O GLU FFF 46  
AE2 5 6 N ILE H 50  ? N ILE FFF 50  O ARG H 59  ? O ARG FFF 59  
AE3 1 2 N GLU H 10  ? N GLU FFF 10  O THR H 114 ? O THR FFF 114 
AE3 2 3 O VAL H 115 ? O VAL FFF 115 N ALA H 92  ? N ALA FFF 92  
AE3 3 4 N GLY H 98  ? N GLY FFF 98  O VAL H 108 ? O VAL FFF 108 
AE4 1 2 N LEU H 130 ? N LEU FFF 130 O GLY H 145 ? O GLY FFF 145 
AE4 2 3 N TYR H 151 ? N TYR FFF 151 O TYR H 182 ? O TYR FFF 182 
AE4 3 4 O VAL H 187 ? O VAL FFF 187 N HIS H 170 ? N HIS FFF 170 
AE5 1 2 N LEU H 130 ? N LEU FFF 130 O GLY H 145 ? O GLY FFF 145 
AE5 2 3 N TYR H 151 ? N TYR FFF 151 O TYR H 182 ? O TYR FFF 182 
AE5 3 4 O SER H 183 ? O SER FFF 183 N VAL H 175 ? N VAL FFF 175 
AE6 1 2 N SER H 159 ? N SER FFF 159 O ASN H 203 ? O ASN FFF 203 
AE6 2 3 N VAL H 204 ? N VAL FFF 204 O VAL H 213 ? O VAL FFF 213 
AE7 1 2 N SER I 7   ? N SER GGG 7   O ASN I 22  ? O ASN GGG 22  
AE7 2 3 N ALA I 19  ? N ALA GGG 19  O ILE I 81  ? O ILE GGG 81  
AE7 3 4 O THR I 80  ? O THR GGG 80  N SER I 69  ? N SER GGG 69  
AE8 1 2 N LEU I 11  ? N LEU GGG 11  O GLU I 111 ? O GLU GGG 111 
AE8 2 3 O VAL I 110 ? O VAL GGG 110 N ALA I 90  ? N ALA GGG 90  
AE8 3 4 O GLN I 95  ? O GLN GGG 95  N ALA I 40  ? N ALA GGG 40  
AE8 4 5 N GLN I 43  ? N GLN GGG 43  O LYS I 51  ? O LYS GGG 51  
AE8 5 6 N TYR I 55  ? N TYR GGG 55  O THR I 59  ? O THR GGG 59  
AE9 1 2 N LEU I 11  ? N LEU GGG 11  O GLU I 111 ? O GLU GGG 111 
AE9 2 3 O VAL I 110 ? O VAL GGG 110 N ALA I 90  ? N ALA GGG 90  
AE9 3 4 N GLN I 96  ? N GLN GGG 96  O THR I 103 ? O THR GGG 103 
AF1 1 2 N TYR I 31  ? N TYR GGG 31  O LYS I 36  ? O LYS GGG 36  
AF2 1 2 N PHE I 122 ? N PHE GGG 122 O LEU I 141 ? O LEU GGG 141 
AF2 2 3 N VAL I 138 ? N VAL GGG 138 O LEU I 185 ? O LEU GGG 185 
AF2 3 4 O THR I 184 ? O THR GGG 184 N GLN I 166 ? N GLN GGG 166 
AF3 1 2 O ALA I 159 ? O ALA GGG 159 N VAL I 156 ? N VAL GGG 156 
AF3 2 3 N GLN I 153 ? N GLN GGG 153 O GLU I 201 ? O GLU GGG 201 
AF3 3 4 N VAL I 202 ? N VAL GGG 202 O VAL I 211 ? O VAL GGG 211 
# 
_atom_sites.entry_id                    6ZLR 
_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]   0.004828 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004828 
_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]   0.005003 
_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.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 2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S 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   . THR A 1 15  ? -5.843  32.760  36.030  1.000 156.014 ? 333 THR EEE N   1 
ATOM   2     C CA  . THR A 1 15  ? -6.637  33.230  34.845  1.000 157.395 ? 333 THR EEE CA  1 
ATOM   3     C C   . THR A 1 15  ? -6.344  34.712  34.566  1.000 161.984 ? 333 THR EEE C   1 
ATOM   4     O O   . THR A 1 15  ? -6.078  35.029  33.389  1.000 164.986 ? 333 THR EEE O   1 
ATOM   5     C CB  . THR A 1 15  ? -8.147  33.007  35.033  1.000 149.128 ? 333 THR EEE CB  1 
ATOM   6     O OG1 . THR A 1 15  ? -8.396  31.605  35.140  1.000 140.634 ? 333 THR EEE OG1 1 
ATOM   7     C CG2 . THR A 1 15  ? -8.994  33.558  33.904  1.000 137.347 ? 333 THR EEE CG2 1 
ATOM   8     N N   . ASN A 1 16  ? -6.388  35.578  35.593  1.000 150.705 ? 334 ASN EEE N   1 
ATOM   9     C CA  . ASN A 1 16  ? -6.581  37.044  35.410  1.000 129.389 ? 334 ASN EEE CA  1 
ATOM   10    C C   . ASN A 1 16  ? -5.267  37.836  35.585  1.000 119.458 ? 334 ASN EEE C   1 
ATOM   11    O O   . ASN A 1 16  ? -5.326  38.895  36.236  1.000 115.342 ? 334 ASN EEE O   1 
ATOM   12    C CB  . ASN A 1 16  ? -7.743  37.561  36.272  1.000 117.718 ? 334 ASN EEE CB  1 
ATOM   13    C CG  . ASN A 1 16  ? -7.484  37.571  37.765  1.000 111.774 ? 334 ASN EEE CG  1 
ATOM   14    O OD1 . ASN A 1 16  ? -6.613  36.867  38.273  1.000 100.741 ? 334 ASN EEE OD1 1 
ATOM   15    N ND2 . ASN A 1 16  ? -8.250  38.379  38.478  1.000 104.055 ? 334 ASN EEE ND2 1 
ATOM   16    N N   . LEU A 1 17  ? -4.154  37.413  34.957  1.000 107.840 ? 335 LEU EEE N   1 
ATOM   17    C CA  . LEU A 1 17  ? -2.997  38.309  34.632  1.000 105.401 ? 335 LEU EEE CA  1 
ATOM   18    C C   . LEU A 1 17  ? -3.484  39.346  33.605  1.000 107.438 ? 335 LEU EEE C   1 
ATOM   19    O O   . LEU A 1 17  ? -4.251  38.960  32.718  1.000 127.618 ? 335 LEU EEE O   1 
ATOM   20    C CB  . LEU A 1 17  ? -1.820  37.485  34.085  1.000 102.833 ? 335 LEU EEE CB  1 
ATOM   21    C CG  . LEU A 1 17  ? -0.601  38.265  33.572  1.000 102.810 ? 335 LEU EEE CG  1 
ATOM   22    C CD1 . LEU A 1 17  ? 0.306   38.706  34.713  1.000 106.220 ? 335 LEU EEE CD1 1 
ATOM   23    C CD2 . LEU A 1 17  ? 0.187   37.449  32.550  1.000 94.146  ? 335 LEU EEE CD2 1 
ATOM   24    N N   . CYS A 1 18  ? -3.070  40.615  33.706  1.000 104.955 ? 336 CYS EEE N   1 
ATOM   25    C CA  . CYS A 1 18  ? -3.503  41.703  32.780  1.000 98.895  ? 336 CYS EEE CA  1 
ATOM   26    C C   . CYS A 1 18  ? -2.926  41.474  31.391  1.000 92.832  ? 336 CYS EEE C   1 
ATOM   27    O O   . CYS A 1 18  ? -1.738  41.211  31.240  1.000 78.552  ? 336 CYS EEE O   1 
ATOM   28    C CB  . CYS A 1 18  ? -3.091  43.083  33.265  1.000 107.838 ? 336 CYS EEE CB  1 
ATOM   29    S SG  . CYS A 1 18  ? -4.091  43.672  34.655  1.000 129.270 ? 336 CYS EEE SG  1 
ATOM   30    N N   . PRO A 1 19  ? -3.747  41.595  30.326  1.000 97.302  ? 337 PRO EEE N   1 
ATOM   31    C CA  . PRO A 1 19  ? -3.383  41.058  29.018  1.000 104.136 ? 337 PRO EEE CA  1 
ATOM   32    C C   . PRO A 1 19  ? -2.480  42.022  28.238  1.000 107.604 ? 337 PRO EEE C   1 
ATOM   33    O O   . PRO A 1 19  ? -2.804  42.336  27.109  1.000 114.645 ? 337 PRO EEE O   1 
ATOM   34    C CB  . PRO A 1 19  ? -4.760  40.895  28.360  1.000 102.027 ? 337 PRO EEE CB  1 
ATOM   35    C CG  . PRO A 1 19  ? -5.533  42.094  28.880  1.000 96.207  ? 337 PRO EEE CG  1 
ATOM   36    C CD  . PRO A 1 19  ? -5.056  42.268  30.310  1.000 92.872  ? 337 PRO EEE CD  1 
ATOM   37    N N   . PHE A 1 20  ? -1.380  42.469  28.854  1.000 99.280  ? 338 PHE EEE N   1 
ATOM   38    C CA  . PHE A 1 20  ? -0.344  43.302  28.192  1.000 96.901  ? 338 PHE EEE CA  1 
ATOM   39    C C   . PHE A 1 20  ? 0.317   42.467  27.090  1.000 94.126  ? 338 PHE EEE C   1 
ATOM   40    O O   . PHE A 1 20  ? 0.778   43.064  26.108  1.000 88.724  ? 338 PHE EEE O   1 
ATOM   41    C CB  . PHE A 1 20  ? 0.695   43.816  29.195  1.000 95.795  ? 338 PHE EEE CB  1 
ATOM   42    C CG  . PHE A 1 20  ? 0.204   44.842  30.186  1.000 96.112  ? 338 PHE EEE CG  1 
ATOM   43    C CD1 . PHE A 1 20  ? -0.471  45.980  29.771  1.000 95.677  ? 338 PHE EEE CD1 1 
ATOM   44    C CD2 . PHE A 1 20  ? 0.455   44.688  31.540  1.000 98.969  ? 338 PHE EEE CD2 1 
ATOM   45    C CE1 . PHE A 1 20  ? -0.917  46.917  30.690  1.000 95.458  ? 338 PHE EEE CE1 1 
ATOM   46    C CE2 . PHE A 1 20  ? 0.015   45.630  32.457  1.000 99.909  ? 338 PHE EEE CE2 1 
ATOM   47    C CZ  . PHE A 1 20  ? -0.675  46.740  32.031  1.000 98.034  ? 338 PHE EEE CZ  1 
ATOM   48    N N   . GLY A 1 21  ? 0.359   41.137  27.254  1.000 93.709  ? 339 GLY EEE N   1 
ATOM   49    C CA  . GLY A 1 21  ? 0.943   40.192  26.281  1.000 101.541 ? 339 GLY EEE CA  1 
ATOM   50    C C   . GLY A 1 21  ? 0.379   40.421  24.895  1.000 102.082 ? 339 GLY EEE C   1 
ATOM   51    O O   . GLY A 1 21  ? 1.167   40.600  23.936  1.000 91.938  ? 339 GLY EEE O   1 
ATOM   52    N N   . GLU A 1 22  ? -0.951  40.470  24.808  1.000 102.153 ? 340 GLU EEE N   1 
ATOM   53    C CA  . GLU A 1 22  ? -1.691  40.579  23.524  1.000 104.014 ? 340 GLU EEE CA  1 
ATOM   54    C C   . GLU A 1 22  ? -1.678  42.030  23.009  1.000 98.427  ? 340 GLU EEE C   1 
ATOM   55    O O   . GLU A 1 22  ? -2.023  42.196  21.837  1.000 93.416  ? 340 GLU EEE O   1 
ATOM   56    C CB  . GLU A 1 22  ? -3.103  39.997  23.676  1.000 110.207 ? 340 GLU EEE CB  1 
ATOM   57    C CG  . GLU A 1 22  ? -4.110  40.910  24.362  1.000 118.799 ? 340 GLU EEE CG  1 
ATOM   58    C CD  . GLU A 1 22  ? -5.475  40.288  24.620  1.000 120.498 ? 340 GLU EEE CD  1 
ATOM   59    O OE1 . GLU A 1 22  ? -5.565  39.389  25.483  1.000 120.530 ? 340 GLU EEE OE1 1 
ATOM   60    O OE2 . GLU A 1 22  ? -6.457  40.732  23.975  1.000 119.677 ? 340 GLU EEE OE2 1 
ATOM   61    N N   . VAL A 1 23  ? -1.288  43.029  23.822  1.000 89.592  ? 341 VAL EEE N   1 
ATOM   62    C CA  . VAL A 1 23  ? -1.220  44.476  23.426  1.000 78.749  ? 341 VAL EEE CA  1 
ATOM   63    C C   . VAL A 1 23  ? 0.134   44.766  22.772  1.000 79.360  ? 341 VAL EEE C   1 
ATOM   64    O O   . VAL A 1 23  ? 0.169   45.531  21.766  1.000 73.366  ? 341 VAL EEE O   1 
ATOM   65    C CB  . VAL A 1 23  ? -1.420  45.423  24.623  1.000 72.210  ? 341 VAL EEE CB  1 
ATOM   66    C CG1 . VAL A 1 23  ? -1.286  46.880  24.198  1.000 66.852  ? 341 VAL EEE CG1 1 
ATOM   67    C CG2 . VAL A 1 23  ? -2.748  45.190  25.325  1.000 72.858  ? 341 VAL EEE CG2 1 
ATOM   68    N N   . PHE A 1 24  ? 1.194   44.216  23.378  1.000 80.112  ? 342 PHE EEE N   1 
ATOM   69    C CA  . PHE A 1 24  ? 2.620   44.439  23.026  1.000 84.851  ? 342 PHE EEE CA  1 
ATOM   70    C C   . PHE A 1 24  ? 3.039   43.466  21.923  1.000 90.480  ? 342 PHE EEE C   1 
ATOM   71    O O   . PHE A 1 24  ? 3.703   43.914  20.967  1.000 81.553  ? 342 PHE EEE O   1 
ATOM   72    C CB  . PHE A 1 24  ? 3.525   44.279  24.256  1.000 80.926  ? 342 PHE EEE CB  1 
ATOM   73    C CG  . PHE A 1 24  ? 3.634   45.492  25.148  1.000 74.065  ? 342 PHE EEE CG  1 
ATOM   74    C CD1 . PHE A 1 24  ? 2.741   45.691  26.189  1.000 69.048  ? 342 PHE EEE CD1 1 
ATOM   75    C CD2 . PHE A 1 24  ? 4.619   46.444  24.943  1.000 67.573  ? 342 PHE EEE CD2 1 
ATOM   76    C CE1 . PHE A 1 24  ? 2.826   46.811  27.003  1.000 62.025  ? 342 PHE EEE CE1 1 
ATOM   77    C CE2 . PHE A 1 24  ? 4.708   47.557  25.762  1.000 65.026  ? 342 PHE EEE CE2 1 
ATOM   78    C CZ  . PHE A 1 24  ? 3.810   47.742  26.787  1.000 61.340  ? 342 PHE EEE CZ  1 
ATOM   79    N N   . ASN A 1 25  ? 2.673   42.185  22.060  1.000 99.620  ? 343 ASN EEE N   1 
ATOM   80    C CA  . ASN A 1 25  ? 3.098   41.100  21.130  1.000 108.706 ? 343 ASN EEE CA  1 
ATOM   81    C C   . ASN A 1 25  ? 1.993   40.880  20.082  1.000 105.152 ? 343 ASN EEE C   1 
ATOM   82    O O   . ASN A 1 25  ? 2.005   39.834  19.409  1.000 116.870 ? 343 ASN EEE O   1 
ATOM   83    C CB  . ASN A 1 25  ? 3.485   39.804  21.861  1.000 115.799 ? 343 ASN EEE CB  1 
ATOM   84    C CG  . ASN A 1 25  ? 4.673   39.926  22.795  1.000 118.377 ? 343 ASN EEE CG  1 
ATOM   85    O OD1 . ASN A 1 25  ? 5.244   40.999  22.969  1.000 122.118 ? 343 ASN EEE OD1 1 
ATOM   86    N ND2 . ASN A 1 25  ? 5.048   38.819  23.404  1.000 124.918 ? 343 ASN EEE ND2 1 
ATOM   87    N N   . ALA A 1 26  ? 1.088   41.852  19.928  1.000 96.538  ? 344 ALA EEE N   1 
ATOM   88    C CA  . ALA A 1 26  ? 0.065   41.928  18.859  1.000 95.341  ? 344 ALA EEE CA  1 
ATOM   89    C C   . ALA A 1 26  ? 0.738   41.949  17.483  1.000 93.216  ? 344 ALA EEE C   1 
ATOM   90    O O   . ALA A 1 26  ? 1.578   42.828  17.252  1.000 94.575  ? 344 ALA EEE O   1 
ATOM   91    C CB  . ALA A 1 26  ? -0.760  43.172  19.058  1.000 99.220  ? 344 ALA EEE CB  1 
ATOM   92    N N   . THR A 1 27  ? 0.356   41.043  16.582  1.000 95.176  ? 345 THR EEE N   1 
ATOM   93    C CA  . THR A 1 27  ? 0.970   40.918  15.232  1.000 98.303  ? 345 THR EEE CA  1 
ATOM   94    C C   . THR A 1 27  ? 0.559   42.128  14.376  1.000 98.839  ? 345 THR EEE C   1 
ATOM   95    O O   . THR A 1 27  ? 1.400   42.564  13.568  1.000 92.746  ? 345 THR EEE O   1 
ATOM   96    C CB  . THR A 1 27  ? 0.647   39.556  14.612  1.000 96.812  ? 345 THR EEE CB  1 
ATOM   97    O OG1 . THR A 1 27  ? -0.698  39.270  14.986  1.000 100.593 ? 345 THR EEE OG1 1 
ATOM   98    C CG2 . THR A 1 27  ? 1.575   38.453  15.081  1.000 95.897  ? 345 THR EEE CG2 1 
ATOM   99    N N   . ARG A 1 28  ? -0.651  42.672  14.567  1.000 101.071 ? 346 ARG EEE N   1 
ATOM   100   C CA  . ARG A 1 28  ? -1.108  43.921  13.884  1.000 104.639 ? 346 ARG EEE CA  1 
ATOM   101   C C   . ARG A 1 28  ? -1.067  45.114  14.857  1.000 92.953  ? 346 ARG EEE C   1 
ATOM   102   O O   . ARG A 1 28  ? -1.595  45.007  15.979  1.000 88.946  ? 346 ARG EEE O   1 
ATOM   103   C CB  . ARG A 1 28  ? -2.507  43.735  13.280  1.000 118.934 ? 346 ARG EEE CB  1 
ATOM   104   C CG  . ARG A 1 28  ? -3.256  45.033  12.967  1.000 130.323 ? 346 ARG EEE CG  1 
ATOM   105   C CD  . ARG A 1 28  ? -4.427  44.905  11.996  1.000 133.895 ? 346 ARG EEE CD  1 
ATOM   106   N NE  . ARG A 1 28  ? -3.930  44.825  10.625  1.000 144.848 ? 346 ARG EEE NE  1 
ATOM   107   C CZ  . ARG A 1 28  ? -3.612  43.702  9.974   1.000 150.786 ? 346 ARG EEE CZ  1 
ATOM   108   N NH1 . ARG A 1 28  ? -3.758  42.517  10.547  1.000 156.948 ? 346 ARG EEE NH1 1 
ATOM   109   N NH2 . ARG A 1 28  ? -3.146  43.772  8.739   1.000 150.816 ? 346 ARG EEE NH2 1 
ATOM   110   N N   . PHE A 1 29  ? -0.439  46.211  14.434  1.000 82.039  ? 347 PHE EEE N   1 
ATOM   111   C CA  . PHE A 1 29  ? -0.493  47.516  15.138  1.000 76.881  ? 347 PHE EEE CA  1 
ATOM   112   C C   . PHE A 1 29  ? -1.344  48.458  14.298  1.000 71.452  ? 347 PHE EEE C   1 
ATOM   113   O O   . PHE A 1 29  ? -1.587  48.145  13.122  1.000 74.856  ? 347 PHE EEE O   1 
ATOM   114   C CB  . PHE A 1 29  ? 0.908   48.074  15.402  1.000 78.925  ? 347 PHE EEE CB  1 
ATOM   115   C CG  . PHE A 1 29  ? 1.353   47.866  16.826  1.000 80.565  ? 347 PHE EEE CG  1 
ATOM   116   C CD1 . PHE A 1 29  ? 1.384   46.589  17.368  1.000 81.084  ? 347 PHE EEE CD1 1 
ATOM   117   C CD2 . PHE A 1 29  ? 1.673   48.939  17.642  1.000 80.098  ? 347 PHE EEE CD2 1 
ATOM   118   C CE1 . PHE A 1 29  ? 1.738   46.380  18.691  1.000 74.222  ? 347 PHE EEE CE1 1 
ATOM   119   C CE2 . PHE A 1 29  ? 2.041   48.728  18.963  1.000 83.815  ? 347 PHE EEE CE2 1 
ATOM   120   C CZ  . PHE A 1 29  ? 2.072   47.448  19.483  1.000 78.843  ? 347 PHE EEE CZ  1 
ATOM   121   N N   . ALA A 1 30  ? -1.778  49.559  14.905  1.000 67.338  ? 348 ALA EEE N   1 
ATOM   122   C CA  . ALA A 1 30  ? -2.712  50.550  14.329  1.000 70.529  ? 348 ALA EEE CA  1 
ATOM   123   C C   . ALA A 1 30  ? -1.938  51.724  13.705  1.000 71.920  ? 348 ALA EEE C   1 
ATOM   124   O O   . ALA A 1 30  ? -0.814  51.987  14.141  1.000 78.472  ? 348 ALA EEE O   1 
ATOM   125   C CB  . ALA A 1 30  ? -3.637  51.009  15.426  1.000 70.206  ? 348 ALA EEE CB  1 
ATOM   126   N N   . SER A 1 31  ? -2.510  52.413  12.712  1.000 73.727  ? 349 SER EEE N   1 
ATOM   127   C CA  . SER A 1 31  ? -1.996  53.723  12.230  1.000 79.641  ? 349 SER EEE CA  1 
ATOM   128   C C   . SER A 1 31  ? -2.181  54.745  13.350  1.000 79.129  ? 349 SER EEE C   1 
ATOM   129   O O   . SER A 1 31  ? -3.174  54.649  14.082  1.000 74.174  ? 349 SER EEE O   1 
ATOM   130   C CB  . SER A 1 31  ? -2.679  54.176  10.973  1.000 84.488  ? 349 SER EEE CB  1 
ATOM   131   O OG  . SER A 1 31  ? -2.214  53.437  9.861   1.000 85.634  ? 349 SER EEE OG  1 
ATOM   132   N N   . VAL A 1 32  ? -1.261  55.693  13.476  1.000 80.396  ? 350 VAL EEE N   1 
ATOM   133   C CA  . VAL A 1 32  ? -1.267  56.664  14.608  1.000 89.762  ? 350 VAL EEE CA  1 
ATOM   134   C C   . VAL A 1 32  ? -2.587  57.462  14.655  1.000 92.502  ? 350 VAL EEE C   1 
ATOM   135   O O   . VAL A 1 32  ? -3.046  57.717  15.778  1.000 99.398  ? 350 VAL EEE O   1 
ATOM   136   C CB  . VAL A 1 32  ? -0.038  57.591  14.553  1.000 95.782  ? 350 VAL EEE CB  1 
ATOM   137   C CG1 . VAL A 1 32  ? -0.037  58.477  13.311  1.000 102.164 ? 350 VAL EEE CG1 1 
ATOM   138   C CG2 . VAL A 1 32  ? 0.076   58.430  15.819  1.000 92.975  ? 350 VAL EEE CG2 1 
ATOM   139   N N   . TYR A 1 33  ? -3.156  57.892  13.520  1.000 92.062  ? 351 TYR EEE N   1 
ATOM   140   C CA  . TYR A 1 33  ? -4.352  58.792  13.466  1.000 90.357  ? 351 TYR EEE CA  1 
ATOM   141   C C   . TYR A 1 33  ? -5.561  58.046  14.038  1.000 79.212  ? 351 TYR EEE C   1 
ATOM   142   O O   . TYR A 1 33  ? -6.407  58.690  14.748  1.000 79.081  ? 351 TYR EEE O   1 
ATOM   143   C CB  . TYR A 1 33  ? -4.648  59.277  12.040  1.000 91.412  ? 351 TYR EEE CB  1 
ATOM   144   C CG  . TYR A 1 33  ? -5.339  58.263  11.156  1.000 93.559  ? 351 TYR EEE CG  1 
ATOM   145   C CD1 . TYR A 1 33  ? -4.625  57.242  10.542  1.000 96.071  ? 351 TYR EEE CD1 1 
ATOM   146   C CD2 . TYR A 1 33  ? -6.707  58.313  10.929  1.000 93.189  ? 351 TYR EEE CD2 1 
ATOM   147   C CE1 . TYR A 1 33  ? -5.249  56.310  9.725   1.000 88.917  ? 351 TYR EEE CE1 1 
ATOM   148   C CE2 . TYR A 1 33  ? -7.349  57.383  10.123  1.000 87.101  ? 351 TYR EEE CE2 1 
ATOM   149   C CZ  . TYR A 1 33  ? -6.613  56.380  9.514   1.000 81.636  ? 351 TYR EEE CZ  1 
ATOM   150   O OH  . TYR A 1 33  ? -7.199  55.448  8.716   1.000 68.796  ? 351 TYR EEE OH  1 
ATOM   151   N N   . ALA A 1 34  ? -5.595  56.740  13.725  1.000 63.989  ? 352 ALA EEE N   1 
ATOM   152   C CA  . ALA A 1 34  ? -6.622  55.734  14.081  1.000 61.964  ? 352 ALA EEE CA  1 
ATOM   153   C C   . ALA A 1 34  ? -6.078  54.857  15.213  1.000 63.088  ? 352 ALA EEE C   1 
ATOM   154   O O   . ALA A 1 34  ? -6.123  53.603  15.122  1.000 54.703  ? 352 ALA EEE O   1 
ATOM   155   C CB  . ALA A 1 34  ? -6.967  54.910  12.865  1.000 58.865  ? 352 ALA EEE CB  1 
ATOM   156   N N   . TRP A 1 35  ? -5.543  55.511  16.239  1.000 61.512  ? 353 TRP EEE N   1 
ATOM   157   C CA  . TRP A 1 35  ? -4.795  54.829  17.319  1.000 54.385  ? 353 TRP EEE CA  1 
ATOM   158   C C   . TRP A 1 35  ? -5.733  53.942  18.123  1.000 52.709  ? 353 TRP EEE C   1 
ATOM   159   O O   . TRP A 1 35  ? -6.865  54.353  18.388  1.000 57.515  ? 353 TRP EEE O   1 
ATOM   160   C CB  . TRP A 1 35  ? -4.052  55.820  18.208  1.000 48.738  ? 353 TRP EEE CB  1 
ATOM   161   C CG  . TRP A 1 35  ? -4.846  56.972  18.724  1.000 44.388  ? 353 TRP EEE CG  1 
ATOM   162   C CD1 . TRP A 1 35  ? -4.985  58.204  18.155  1.000 46.654  ? 353 TRP EEE CD1 1 
ATOM   163   C CD2 . TRP A 1 35  ? -5.526  57.023  19.983  1.000 43.625  ? 353 TRP EEE CD2 1 
ATOM   164   N NE1 . TRP A 1 35  ? -5.735  59.016  18.959  1.000 49.703  ? 353 TRP EEE NE1 1 
ATOM   165   C CE2 . TRP A 1 35  ? -6.073  58.321  20.093  1.000 48.095  ? 353 TRP EEE CE2 1 
ATOM   166   C CE3 . TRP A 1 35  ? -5.721  56.102  21.017  1.000 43.817  ? 353 TRP EEE CE3 1 
ATOM   167   C CZ2 . TRP A 1 35  ? -6.817  58.716  21.206  1.000 51.235  ? 353 TRP EEE CZ2 1 
ATOM   168   C CZ3 . TRP A 1 35  ? -6.455  56.494  22.112  1.000 47.301  ? 353 TRP EEE CZ3 1 
ATOM   169   C CH2 . TRP A 1 35  ? -7.001  57.779  22.200  1.000 50.868  ? 353 TRP EEE CH2 1 
ATOM   170   N N   . ASN A 1 36  ? -5.225  52.777  18.489  1.000 53.355  ? 354 ASN EEE N   1 
ATOM   171   C CA  . ASN A 1 36  ? -5.937  51.727  19.253  1.000 59.836  ? 354 ASN EEE CA  1 
ATOM   172   C C   . ASN A 1 36  ? -5.780  51.977  20.754  1.000 59.688  ? 354 ASN EEE C   1 
ATOM   173   O O   . ASN A 1 36  ? -4.663  52.262  21.169  1.000 70.940  ? 354 ASN EEE O   1 
ATOM   174   C CB  . ASN A 1 36  ? -5.394  50.349  18.894  1.000 62.070  ? 354 ASN EEE CB  1 
ATOM   175   C CG  . ASN A 1 36  ? -6.522  49.347  18.871  1.000 68.040  ? 354 ASN EEE CG  1 
ATOM   176   O OD1 . ASN A 1 36  ? -7.203  49.173  19.882  1.000 77.132  ? 354 ASN EEE OD1 1 
ATOM   177   N ND2 . ASN A 1 36  ? -6.767  48.753  17.712  1.000 65.358  ? 354 ASN EEE ND2 1 
ATOM   178   N N   . ARG A 1 37  ? -6.865  51.895  21.522  1.000 58.722  ? 355 ARG EEE N   1 
ATOM   179   C CA  . ARG A 1 37  ? -6.855  52.004  23.006  1.000 57.179  ? 355 ARG EEE CA  1 
ATOM   180   C C   . ARG A 1 37  ? -7.517  50.751  23.564  1.000 58.489  ? 355 ARG EEE C   1 
ATOM   181   O O   . ARG A 1 37  ? -8.731  50.583  23.342  1.000 59.729  ? 355 ARG EEE O   1 
ATOM   182   C CB  . ARG A 1 37  ? -7.592  53.244  23.522  1.000 55.405  ? 355 ARG EEE CB  1 
ATOM   183   C CG  . ARG A 1 37  ? -8.009  53.158  24.985  1.000 55.250  ? 355 ARG EEE CG  1 
ATOM   184   C CD  . ARG A 1 37  ? -8.425  54.493  25.569  1.000 54.891  ? 355 ARG EEE CD  1 
ATOM   185   N NE  . ARG A 1 37  ? -7.330  55.443  25.646  1.000 51.349  ? 355 ARG EEE NE  1 
ATOM   186   C CZ  . ARG A 1 37  ? -7.336  56.566  26.358  1.000 55.833  ? 355 ARG EEE CZ  1 
ATOM   187   N NH1 . ARG A 1 37  ? -8.380  56.916  27.092  1.000 54.174  ? 355 ARG EEE NH1 1 
ATOM   188   N NH2 . ARG A 1 37  ? -6.273  57.345  26.341  1.000 61.488  ? 355 ARG EEE NH2 1 
ATOM   189   N N   . LYS A 1 38  ? -6.733  49.927  24.262  1.000 64.184  ? 356 LYS EEE N   1 
ATOM   190   C CA  . LYS A 1 38  ? -7.214  48.781  25.069  1.000 64.178  ? 356 LYS EEE CA  1 
ATOM   191   C C   . LYS A 1 38  ? -7.463  49.300  26.480  1.000 62.539  ? 356 LYS EEE C   1 
ATOM   192   O O   . LYS A 1 38  ? -6.539  49.896  27.035  1.000 69.705  ? 356 LYS EEE O   1 
ATOM   193   C CB  . LYS A 1 38  ? -6.159  47.677  25.100  1.000 66.993  ? 356 LYS EEE CB  1 
ATOM   194   C CG  . LYS A 1 38  ? -6.643  46.340  25.622  1.000 74.118  ? 356 LYS EEE CG  1 
ATOM   195   C CD  . LYS A 1 38  ? -7.144  45.439  24.500  1.000 84.819  ? 356 LYS EEE CD  1 
ATOM   196   C CE  . LYS A 1 38  ? -6.914  43.958  24.743  1.000 88.453  ? 356 LYS EEE CE  1 
ATOM   197   N NZ  . LYS A 1 38  ? -7.456  43.537  26.058  1.000 96.386  ? 356 LYS EEE NZ  1 
ATOM   198   N N   . ARG A 1 39  ? -8.668  49.130  27.011  1.000 64.967  ? 357 ARG EEE N   1 
ATOM   199   C CA  . ARG A 1 39  ? -8.952  49.387  28.445  1.000 68.571  ? 357 ARG EEE CA  1 
ATOM   200   C C   . ARG A 1 39  ? -8.444  48.173  29.215  1.000 70.854  ? 357 ARG EEE C   1 
ATOM   201   O O   . ARG A 1 39  ? -8.625  47.044  28.713  1.000 65.419  ? 357 ARG EEE O   1 
ATOM   202   C CB  . ARG A 1 39  ? -10.435 49.666  28.711  1.000 73.663  ? 357 ARG EEE CB  1 
ATOM   203   C CG  . ARG A 1 39  ? -10.978 49.020  29.979  1.000 75.451  ? 357 ARG EEE CG  1 
ATOM   204   C CD  . ARG A 1 39  ? -12.481 49.119  30.073  1.000 81.065  ? 357 ARG EEE CD  1 
ATOM   205   N NE  . ARG A 1 39  ? -12.855 50.405  30.645  1.000 84.670  ? 357 ARG EEE NE  1 
ATOM   206   C CZ  . ARG A 1 39  ? -13.432 50.568  31.835  1.000 86.287  ? 357 ARG EEE CZ  1 
ATOM   207   N NH1 . ARG A 1 39  ? -13.751 49.518  32.580  1.000 83.975  ? 357 ARG EEE NH1 1 
ATOM   208   N NH2 . ARG A 1 39  ? -13.722 51.788  32.259  1.000 84.435  ? 357 ARG EEE NH2 1 
ATOM   209   N N   . ILE A 1 40  ? -7.787  48.426  30.349  1.000 79.928  ? 358 ILE EEE N   1 
ATOM   210   C CA  . ILE A 1 40  ? -7.350  47.403  31.341  1.000 84.633  ? 358 ILE EEE CA  1 
ATOM   211   C C   . ILE A 1 40  ? -8.190  47.603  32.610  1.000 87.577  ? 358 ILE EEE C   1 
ATOM   212   O O   . ILE A 1 40  ? -8.216  48.750  33.142  1.000 78.310  ? 358 ILE EEE O   1 
ATOM   213   C CB  . ILE A 1 40  ? -5.837  47.505  31.619  1.000 89.942  ? 358 ILE EEE CB  1 
ATOM   214   C CG1 . ILE A 1 40  ? -4.992  47.545  30.339  1.000 89.320  ? 358 ILE EEE CG1 1 
ATOM   215   C CG2 . ILE A 1 40  ? -5.399  46.384  32.545  1.000 101.135 ? 358 ILE EEE CG2 1 
ATOM   216   C CD1 . ILE A 1 40  ? -4.975  46.255  29.544  1.000 85.696  ? 358 ILE EEE CD1 1 
ATOM   217   N N   . SER A 1 41  ? -8.878  46.532  33.032  1.000 89.943  ? 359 SER EEE N   1 
ATOM   218   C CA  . SER A 1 41  ? -9.690  46.428  34.276  1.000 94.924  ? 359 SER EEE CA  1 
ATOM   219   C C   . SER A 1 41  ? -9.698  44.969  34.749  1.000 96.964  ? 359 SER EEE C   1 
ATOM   220   O O   . SER A 1 41  ? -9.489  44.077  33.903  1.000 89.203  ? 359 SER EEE O   1 
ATOM   221   C CB  . SER A 1 41  ? -11.099 46.948  34.072  1.000 96.188  ? 359 SER EEE CB  1 
ATOM   222   O OG  . SER A 1 41  ? -11.118 48.364  33.941  1.000 100.310 ? 359 SER EEE OG  1 
ATOM   223   N N   . ASN A 1 42  ? -9.897  44.756  36.056  1.000 106.057 ? 360 ASN EEE N   1 
ATOM   224   C CA  . ASN A 1 42  ? -10.252 43.452  36.680  1.000 111.871 ? 360 ASN EEE CA  1 
ATOM   225   C C   . ASN A 1 42  ? -9.175  42.416  36.352  1.000 119.698 ? 360 ASN EEE C   1 
ATOM   226   O O   . ASN A 1 42  ? -9.525  41.309  35.879  1.000 126.370 ? 360 ASN EEE O   1 
ATOM   227   C CB  . ASN A 1 42  ? -11.627 42.961  36.222  1.000 113.426 ? 360 ASN EEE CB  1 
ATOM   228   C CG  . ASN A 1 42  ? -12.720 43.965  36.501  1.000 112.150 ? 360 ASN EEE CG  1 
ATOM   229   O OD1 . ASN A 1 42  ? -13.159 44.670  35.594  1.000 106.686 ? 360 ASN EEE OD1 1 
ATOM   230   N ND2 . ASN A 1 42  ? -13.144 44.048  37.750  1.000 114.372 ? 360 ASN EEE ND2 1 
ATOM   231   N N   . CYS A 1 43  ? -7.912  42.763  36.606  1.000 118.663 ? 361 CYS EEE N   1 
ATOM   232   C CA  . CYS A 1 43  ? -6.752  41.849  36.433  1.000 129.668 ? 361 CYS EEE CA  1 
ATOM   233   C C   . CYS A 1 43  ? -5.565  42.350  37.257  1.000 121.133 ? 361 CYS EEE C   1 
ATOM   234   O O   . CYS A 1 43  ? -5.561  43.531  37.642  1.000 102.746 ? 361 CYS EEE O   1 
ATOM   235   C CB  . CYS A 1 43  ? -6.374  41.706  34.962  1.000 139.148 ? 361 CYS EEE CB  1 
ATOM   236   S SG  . CYS A 1 43  ? -6.010  43.283  34.145  1.000 143.182 ? 361 CYS EEE SG  1 
ATOM   237   N N   . VAL A 1 44  ? -4.606  41.455  37.514  1.000 130.594 ? 362 VAL EEE N   1 
ATOM   238   C CA  . VAL A 1 44  ? -3.344  41.726  38.263  1.000 127.327 ? 362 VAL EEE CA  1 
ATOM   239   C C   . VAL A 1 44  ? -2.203  41.897  37.246  1.000 120.136 ? 362 VAL EEE C   1 
ATOM   240   O O   . VAL A 1 44  ? -1.973  40.980  36.407  1.000 116.712 ? 362 VAL EEE O   1 
ATOM   241   C CB  . VAL A 1 44  ? -3.066  40.615  39.292  1.000 128.212 ? 362 VAL EEE CB  1 
ATOM   242   C CG1 . VAL A 1 44  ? -1.914  40.974  40.210  1.000 129.407 ? 362 VAL EEE CG1 1 
ATOM   243   C CG2 . VAL A 1 44  ? -4.303  40.300  40.122  1.000 125.352 ? 362 VAL EEE CG2 1 
ATOM   244   N N   . ALA A 1 45  ? -1.516  43.040  37.322  1.000 108.181 ? 363 ALA EEE N   1 
ATOM   245   C CA  . ALA A 1 45  ? -0.585  43.551  36.291  1.000 113.391 ? 363 ALA EEE CA  1 
ATOM   246   C C   . ALA A 1 45  ? 0.858   43.427  36.782  1.000 109.858 ? 363 ALA EEE C   1 
ATOM   247   O O   . ALA A 1 45  ? 1.203   44.059  37.806  1.000 112.907 ? 363 ALA EEE O   1 
ATOM   248   C CB  . ALA A 1 45  ? -0.932  44.983  35.962  1.000 118.941 ? 363 ALA EEE CB  1 
ATOM   249   N N   . ASP A 1 46  ? 1.670   42.652  36.066  1.000 99.592  ? 364 ASP EEE N   1 
ATOM   250   C CA  . ASP A 1 46  ? 3.087   42.412  36.427  1.000 104.591 ? 364 ASP EEE CA  1 
ATOM   251   C C   . ASP A 1 46  ? 3.969   43.354  35.606  1.000 95.354  ? 364 ASP EEE C   1 
ATOM   252   O O   . ASP A 1 46  ? 4.461   42.923  34.546  1.000 99.836  ? 364 ASP EEE O   1 
ATOM   253   C CB  . ASP A 1 46  ? 3.459   40.949  36.195  1.000 115.934 ? 364 ASP EEE CB  1 
ATOM   254   C CG  . ASP A 1 46  ? 4.867   40.638  36.650  1.000 119.585 ? 364 ASP EEE CG  1 
ATOM   255   O OD1 . ASP A 1 46  ? 5.641   40.117  35.829  1.000 113.791 ? 364 ASP EEE OD1 1 
ATOM   256   O OD2 . ASP A 1 46  ? 5.174   40.947  37.817  1.000 135.282 ? 364 ASP EEE OD2 1 
ATOM   257   N N   . TYR A 1 47  ? 4.185   44.582  36.079  1.000 80.552  ? 365 TYR EEE N   1 
ATOM   258   C CA  . TYR A 1 47  ? 4.837   45.646  35.275  1.000 77.723  ? 365 TYR EEE CA  1 
ATOM   259   C C   . TYR A 1 47  ? 6.340   45.356  35.145  1.000 79.861  ? 365 TYR EEE C   1 
ATOM   260   O O   . TYR A 1 47  ? 7.000   45.971  34.285  1.000 69.719  ? 365 TYR EEE O   1 
ATOM   261   C CB  . TYR A 1 47  ? 4.565   47.023  35.868  1.000 78.014  ? 365 TYR EEE CB  1 
ATOM   262   C CG  . TYR A 1 47  ? 3.117   47.456  35.874  1.000 84.447  ? 365 TYR EEE CG  1 
ATOM   263   C CD1 . TYR A 1 47  ? 2.592   48.299  34.901  1.000 81.979  ? 365 TYR EEE CD1 1 
ATOM   264   C CD2 . TYR A 1 47  ? 2.270   47.060  36.896  1.000 89.594  ? 365 TYR EEE CD2 1 
ATOM   265   C CE1 . TYR A 1 47  ? 1.270   48.722  34.940  1.000 74.728  ? 365 TYR EEE CE1 1 
ATOM   266   C CE2 . TYR A 1 47  ? 0.947   47.475  36.950  1.000 83.969  ? 365 TYR EEE CE2 1 
ATOM   267   C CZ  . TYR A 1 47  ? 0.441   48.303  35.968  1.000 74.063  ? 365 TYR EEE CZ  1 
ATOM   268   O OH  . TYR A 1 47  ? -0.866  48.683  36.063  1.000 65.858  ? 365 TYR EEE OH  1 
ATOM   269   N N   . SER A 1 48  ? 6.868   44.430  35.953  1.000 84.104  ? 366 SER EEE N   1 
ATOM   270   C CA  . SER A 1 48  ? 8.274   43.947  35.879  1.000 83.572  ? 366 SER EEE CA  1 
ATOM   271   C C   . SER A 1 48  ? 8.603   43.383  34.487  1.000 85.536  ? 366 SER EEE C   1 
ATOM   272   O O   . SER A 1 48  ? 9.714   43.692  33.994  1.000 95.582  ? 366 SER EEE O   1 
ATOM   273   C CB  . SER A 1 48  ? 8.548   42.938  36.943  1.000 83.500  ? 366 SER EEE CB  1 
ATOM   274   O OG  . SER A 1 48  ? 7.745   41.791  36.750  1.000 89.176  ? 366 SER EEE OG  1 
ATOM   275   N N   . VAL A 1 49  ? 7.700   42.588  33.887  1.000 82.503  ? 367 VAL EEE N   1 
ATOM   276   C CA  . VAL A 1 49  ? 7.884   41.981  32.528  1.000 80.143  ? 367 VAL EEE CA  1 
ATOM   277   C C   . VAL A 1 49  ? 8.345   43.095  31.589  1.000 70.623  ? 367 VAL EEE C   1 
ATOM   278   O O   . VAL A 1 49  ? 9.217   42.837  30.734  1.000 57.020  ? 367 VAL EEE O   1 
ATOM   279   C CB  . VAL A 1 49  ? 6.612   41.300  31.975  1.000 82.881  ? 367 VAL EEE CB  1 
ATOM   280   C CG1 . VAL A 1 49  ? 6.791   40.876  30.526  1.000 84.512  ? 367 VAL EEE CG1 1 
ATOM   281   C CG2 . VAL A 1 49  ? 6.172   40.097  32.795  1.000 82.633  ? 367 VAL EEE CG2 1 
ATOM   282   N N   . LEU A 1 50  ? 7.778   44.290  31.775  1.000 70.657  ? 368 LEU EEE N   1 
ATOM   283   C CA  . LEU A 1 50  ? 7.967   45.452  30.870  1.000 76.089  ? 368 LEU EEE CA  1 
ATOM   284   C C   . LEU A 1 50  ? 9.374   46.044  31.011  1.000 78.938  ? 368 LEU EEE C   1 
ATOM   285   O O   . LEU A 1 50  ? 10.067  46.076  29.985  1.000 71.625  ? 368 LEU EEE O   1 
ATOM   286   C CB  . LEU A 1 50  ? 6.889   46.502  31.149  1.000 74.621  ? 368 LEU EEE CB  1 
ATOM   287   C CG  . LEU A 1 50  ? 5.691   46.475  30.198  1.000 75.437  ? 368 LEU EEE CG  1 
ATOM   288   C CD1 . LEU A 1 50  ? 5.358   45.060  29.740  1.000 74.445  ? 368 LEU EEE CD1 1 
ATOM   289   C CD2 . LEU A 1 50  ? 4.473   47.125  30.842  1.000 77.103  ? 368 LEU EEE CD2 1 
ATOM   290   N N   . TYR A 1 51  ? 9.781   46.517  32.196  1.000 79.323  ? 369 TYR EEE N   1 
ATOM   291   C CA  . TYR A 1 51  ? 11.028  47.322  32.347  1.000 80.474  ? 369 TYR EEE CA  1 
ATOM   292   C C   . TYR A 1 51  ? 12.274  46.428  32.449  1.000 81.387  ? 369 TYR EEE C   1 
ATOM   293   O O   . TYR A 1 51  ? 13.389  46.931  32.201  1.000 79.295  ? 369 TYR EEE O   1 
ATOM   294   C CB  . TYR A 1 51  ? 10.939  48.331  33.494  1.000 78.463  ? 369 TYR EEE CB  1 
ATOM   295   C CG  . TYR A 1 51  ? 10.552  47.776  34.833  1.000 71.698  ? 369 TYR EEE CG  1 
ATOM   296   C CD1 . TYR A 1 51  ? 9.243   47.839  35.256  1.000 74.354  ? 369 TYR EEE CD1 1 
ATOM   297   C CD2 . TYR A 1 51  ? 11.496  47.236  35.683  1.000 72.660  ? 369 TYR EEE CD2 1 
ATOM   298   C CE1 . TYR A 1 51  ? 8.862   47.358  36.491  1.000 80.028  ? 369 TYR EEE CE1 1 
ATOM   299   C CE2 . TYR A 1 51  ? 11.136  46.747  36.927  1.000 79.829  ? 369 TYR EEE CE2 1 
ATOM   300   C CZ  . TYR A 1 51  ? 9.811   46.807  37.326  1.000 85.051  ? 369 TYR EEE CZ  1 
ATOM   301   O OH  . TYR A 1 51  ? 9.397   46.335  38.536  1.000 99.024  ? 369 TYR EEE OH  1 
ATOM   302   N N   . ASN A 1 52  ? 12.112  45.139  32.744  1.000 86.153  ? 370 ASN EEE N   1 
ATOM   303   C CA  . ASN A 1 52  ? 13.244  44.178  32.768  1.000 90.581  ? 370 ASN EEE CA  1 
ATOM   304   C C   . ASN A 1 52  ? 13.545  43.718  31.337  1.000 90.288  ? 370 ASN EEE C   1 
ATOM   305   O O   . ASN A 1 52  ? 14.601  43.096  31.138  1.000 96.707  ? 370 ASN EEE O   1 
ATOM   306   C CB  . ASN A 1 52  ? 12.973  43.015  33.721  1.000 94.023  ? 370 ASN EEE CB  1 
ATOM   307   C CG  . ASN A 1 52  ? 12.862  43.459  35.168  1.000 96.115  ? 370 ASN EEE CG  1 
ATOM   308   O OD1 . ASN A 1 52  ? 13.401  44.497  35.559  1.000 79.823  ? 370 ASN EEE OD1 1 
ATOM   309   N ND2 . ASN A 1 52  ? 12.143  42.692  35.975  1.000 106.755 ? 370 ASN EEE ND2 1 
ATOM   310   N N   . SER A 1 53  ? 12.655  44.002  30.383  1.000 85.827  ? 371 SER EEE N   1 
ATOM   311   C CA  . SER A 1 53  ? 12.890  43.752  28.940  1.000 84.113  ? 371 SER EEE CA  1 
ATOM   312   C C   . SER A 1 53  ? 14.027  44.662  28.474  1.000 87.321  ? 371 SER EEE C   1 
ATOM   313   O O   . SER A 1 53  ? 14.067  45.837  28.887  1.000 73.970  ? 371 SER EEE O   1 
ATOM   314   C CB  . SER A 1 53  ? 11.645  43.954  28.113  1.000 79.412  ? 371 SER EEE CB  1 
ATOM   315   O OG  . SER A 1 53  ? 11.955  43.906  26.727  1.000 79.364  ? 371 SER EEE OG  1 
ATOM   316   N N   . ALA A 1 54  ? 14.923  44.121  27.654  1.000 101.958 ? 372 ALA EEE N   1 
ATOM   317   C CA  . ALA A 1 54  ? 16.082  44.846  27.085  1.000 117.110 ? 372 ALA EEE CA  1 
ATOM   318   C C   . ALA A 1 54  ? 15.809  45.144  25.607  1.000 116.268 ? 372 ALA EEE C   1 
ATOM   319   O O   . ALA A 1 54  ? 16.761  45.528  24.892  1.000 132.451 ? 372 ALA EEE O   1 
ATOM   320   C CB  . ALA A 1 54  ? 17.344  44.035  27.277  1.000 120.691 ? 372 ALA EEE CB  1 
ATOM   321   N N   . SER A 1 55  ? 14.551  45.008  25.176  1.000 98.598  ? 373 SER EEE N   1 
ATOM   322   C CA  . SER A 1 55  ? 14.141  45.095  23.752  1.000 90.840  ? 373 SER EEE CA  1 
ATOM   323   C C   . SER A 1 55  ? 13.382  46.405  23.479  1.000 80.363  ? 373 SER EEE C   1 
ATOM   324   O O   . SER A 1 55  ? 12.721  46.479  22.436  1.000 79.963  ? 373 SER EEE O   1 
ATOM   325   C CB  . SER A 1 55  ? 13.338  43.872  23.363  1.000 89.610  ? 373 SER EEE CB  1 
ATOM   326   O OG  . SER A 1 55  ? 12.162  43.752  24.149  1.000 85.013  ? 373 SER EEE OG  1 
ATOM   327   N N   . PHE A 1 56  ? 13.549  47.437  24.309  1.000 68.625  ? 374 PHE EEE N   1 
ATOM   328   C CA  . PHE A 1 56  ? 12.818  48.716  24.162  1.000 66.625  ? 374 PHE EEE CA  1 
ATOM   329   C C   . PHE A 1 56  ? 13.787  49.870  23.886  1.000 62.853  ? 374 PHE EEE C   1 
ATOM   330   O O   . PHE A 1 56  ? 14.665  50.076  24.707  1.000 64.595  ? 374 PHE EEE O   1 
ATOM   331   C CB  . PHE A 1 56  ? 11.974  48.952  25.414  1.000 68.575  ? 374 PHE EEE CB  1 
ATOM   332   C CG  . PHE A 1 56  ? 10.777  48.041  25.559  1.000 71.696  ? 374 PHE EEE CG  1 
ATOM   333   C CD1 . PHE A 1 56  ? 10.021  47.656  24.459  1.000 77.481  ? 374 PHE EEE CD1 1 
ATOM   334   C CD2 . PHE A 1 56  ? 10.372  47.597  26.810  1.000 70.775  ? 374 PHE EEE CD2 1 
ATOM   335   C CE1 . PHE A 1 56  ? 8.918   46.821  24.605  1.000 75.013  ? 374 PHE EEE CE1 1 
ATOM   336   C CE2 . PHE A 1 56  ? 9.267   46.766  26.953  1.000 70.836  ? 374 PHE EEE CE2 1 
ATOM   337   C CZ  . PHE A 1 56  ? 8.539   46.381  25.854  1.000 69.833  ? 374 PHE EEE CZ  1 
ATOM   338   N N   . SER A 1 57  ? 13.605  50.591  22.774  1.000 60.923  ? 375 SER EEE N   1 
ATOM   339   C CA  . SER A 1 57  ? 14.321  51.848  22.424  1.000 64.098  ? 375 SER EEE CA  1 
ATOM   340   C C   . SER A 1 57  ? 14.065  52.932  23.470  1.000 62.494  ? 375 SER EEE C   1 
ATOM   341   O O   . SER A 1 57  ? 14.993  53.668  23.785  1.000 67.604  ? 375 SER EEE O   1 
ATOM   342   C CB  . SER A 1 57  ? 13.921  52.369  21.071  1.000 69.361  ? 375 SER EEE CB  1 
ATOM   343   O OG  . SER A 1 57  ? 14.557  51.623  20.047  1.000 85.589  ? 375 SER EEE OG  1 
ATOM   344   N N   . THR A 1 58  ? 12.827  53.076  23.923  1.000 60.702  ? 376 THR EEE N   1 
ATOM   345   C CA  . THR A 1 58  ? 12.345  54.233  24.719  1.000 57.283  ? 376 THR EEE CA  1 
ATOM   346   C C   . THR A 1 58  ? 11.476  53.690  25.859  1.000 54.339  ? 376 THR EEE C   1 
ATOM   347   O O   . THR A 1 58  ? 10.789  52.679  25.626  1.000 53.005  ? 376 THR EEE O   1 
ATOM   348   C CB  . THR A 1 58  ? 11.596  55.182  23.777  1.000 57.926  ? 376 THR EEE CB  1 
ATOM   349   O OG1 . THR A 1 58  ? 12.564  55.882  23.006  1.000 57.663  ? 376 THR EEE OG1 1 
ATOM   350   C CG2 . THR A 1 58  ? 10.701  56.175  24.479  1.000 63.071  ? 376 THR EEE CG2 1 
ATOM   351   N N   . PHE A 1 59  ? 11.497  54.307  27.041  1.000 46.690  ? 377 PHE EEE N   1 
ATOM   352   C CA  . PHE A 1 59  ? 10.627  53.922  28.182  1.000 45.717  ? 377 PHE EEE CA  1 
ATOM   353   C C   . PHE A 1 59  ? 10.546  55.113  29.139  1.000 50.092  ? 377 PHE EEE C   1 
ATOM   354   O O   . PHE A 1 59  ? 10.952  55.027  30.320  1.000 59.568  ? 377 PHE EEE O   1 
ATOM   355   C CB  . PHE A 1 59  ? 11.155  52.635  28.820  1.000 44.893  ? 377 PHE EEE CB  1 
ATOM   356   C CG  . PHE A 1 59  ? 10.154  51.805  29.585  1.000 45.503  ? 377 PHE EEE CG  1 
ATOM   357   C CD1 . PHE A 1 59  ? 9.354   52.368  30.565  1.000 48.247  ? 377 PHE EEE CD1 1 
ATOM   358   C CD2 . PHE A 1 59  ? 10.023  50.443  29.342  1.000 47.430  ? 377 PHE EEE CD2 1 
ATOM   359   C CE1 . PHE A 1 59  ? 8.439   51.596  31.271  1.000 49.813  ? 377 PHE EEE CE1 1 
ATOM   360   C CE2 . PHE A 1 59  ? 9.114   49.665  30.049  1.000 50.003  ? 377 PHE EEE CE2 1 
ATOM   361   C CZ  . PHE A 1 59  ? 8.316   50.249  31.009  1.000 50.639  ? 377 PHE EEE CZ  1 
ATOM   362   N N   . LYS A 1 60  ? 10.049  56.234  28.614  1.000 50.050  ? 378 LYS EEE N   1 
ATOM   363   C CA  . LYS A 1 60  ? 9.940   57.517  29.354  1.000 48.663  ? 378 LYS EEE CA  1 
ATOM   364   C C   . LYS A 1 60  ? 8.618   57.498  30.114  1.000 46.960  ? 378 LYS EEE C   1 
ATOM   365   O O   . LYS A 1 60  ? 7.563   57.515  29.460  1.000 49.544  ? 378 LYS EEE O   1 
ATOM   366   C CB  . LYS A 1 60  ? 10.005  58.714  28.399  1.000 49.396  ? 378 LYS EEE CB  1 
ATOM   367   C CG  . LYS A 1 60  ? 10.888  58.515  27.175  1.000 52.476  ? 378 LYS EEE CG  1 
ATOM   368   C CD  . LYS A 1 60  ? 11.794  59.676  26.873  1.000 56.348  ? 378 LYS EEE CD  1 
ATOM   369   C CE  . LYS A 1 60  ? 11.062  60.969  26.602  1.000 58.049  ? 378 LYS EEE CE  1 
ATOM   370   N NZ  . LYS A 1 60  ? 12.018  62.096  26.519  1.000 59.122  ? 378 LYS EEE NZ  1 
ATOM   371   N N   . CYS A 1 61  ? 8.666   57.407  31.436  1.000 46.817  ? 379 CYS EEE N   1 
ATOM   372   C CA  . CYS A 1 61  ? 7.451   57.471  32.279  1.000 48.800  ? 379 CYS EEE CA  1 
ATOM   373   C C   . CYS A 1 61  ? 7.335   58.872  32.849  1.000 45.644  ? 379 CYS EEE C   1 
ATOM   374   O O   . CYS A 1 61  ? 8.378   59.485  33.068  1.000 49.512  ? 379 CYS EEE O   1 
ATOM   375   C CB  . CYS A 1 61  ? 7.492   56.405  33.356  1.000 53.601  ? 379 CYS EEE CB  1 
ATOM   376   S SG  . CYS A 1 61  ? 7.472   54.766  32.594  1.000 68.959  ? 379 CYS EEE SG  1 
ATOM   377   N N   . TYR A 1 62  ? 6.106   59.354  33.020  1.000 43.655  ? 380 TYR EEE N   1 
ATOM   378   C CA  . TYR A 1 62  ? 5.773   60.727  33.480  1.000 42.270  ? 380 TYR EEE CA  1 
ATOM   379   C C   . TYR A 1 62  ? 4.855   60.607  34.701  1.000 45.403  ? 380 TYR EEE C   1 
ATOM   380   O O   . TYR A 1 62  ? 3.880   59.867  34.623  1.000 54.627  ? 380 TYR EEE O   1 
ATOM   381   C CB  . TYR A 1 62  ? 5.165   61.524  32.321  1.000 38.158  ? 380 TYR EEE CB  1 
ATOM   382   C CG  . TYR A 1 62  ? 6.064   61.703  31.115  1.000 35.701  ? 380 TYR EEE CG  1 
ATOM   383   C CD1 . TYR A 1 62  ? 6.348   60.659  30.238  1.000 35.337  ? 380 TYR EEE CD1 1 
ATOM   384   C CD2 . TYR A 1 62  ? 6.608   62.945  30.817  1.000 33.878  ? 380 TYR EEE CD2 1 
ATOM   385   C CE1 . TYR A 1 62  ? 7.163   60.844  29.124  1.000 34.253  ? 380 TYR EEE CE1 1 
ATOM   386   C CE2 . TYR A 1 62  ? 7.426   63.146  29.714  1.000 33.152  ? 380 TYR EEE CE2 1 
ATOM   387   C CZ  . TYR A 1 62  ? 7.715   62.091  28.869  1.000 34.413  ? 380 TYR EEE CZ  1 
ATOM   388   O OH  . TYR A 1 62  ? 8.519   62.342  27.793  1.000 38.079  ? 380 TYR EEE OH  1 
ATOM   389   N N   . GLY A 1 63  ? 5.215   61.224  35.824  1.000 47.082  ? 381 GLY EEE N   1 
ATOM   390   C CA  . GLY A 1 63  ? 4.382   61.270  37.044  1.000 49.446  ? 381 GLY EEE CA  1 
ATOM   391   C C   . GLY A 1 63  ? 4.320   59.955  37.820  1.000 48.989  ? 381 GLY EEE C   1 
ATOM   392   O O   . GLY A 1 63  ? 3.667   59.926  38.874  1.000 52.435  ? 381 GLY EEE O   1 
ATOM   393   N N   . VAL A 1 64  ? 4.968   58.885  37.383  1.000 49.648  ? 382 VAL EEE N   1 
ATOM   394   C CA  . VAL A 1 64  ? 4.813   57.582  38.092  1.000 52.763  ? 382 VAL EEE CA  1 
ATOM   395   C C   . VAL A 1 64  ? 5.976   56.656  37.725  1.000 55.116  ? 382 VAL EEE C   1 
ATOM   396   O O   . VAL A 1 64  ? 6.470   56.744  36.580  1.000 59.675  ? 382 VAL EEE O   1 
ATOM   397   C CB  . VAL A 1 64  ? 3.450   56.965  37.741  1.000 57.607  ? 382 VAL EEE CB  1 
ATOM   398   C CG1 . VAL A 1 64  ? 3.431   56.420  36.312  1.000 57.972  ? 382 VAL EEE CG1 1 
ATOM   399   C CG2 . VAL A 1 64  ? 3.045   55.906  38.754  1.000 62.423  ? 382 VAL EEE CG2 1 
ATOM   400   N N   . SER A 1 65  ? 6.391   55.816  38.672  1.000 49.524  ? 383 SER EEE N   1 
ATOM   401   C CA  . SER A 1 65  ? 7.588   54.944  38.572  1.000 50.418  ? 383 SER EEE CA  1 
ATOM   402   C C   . SER A 1 65  ? 7.140   53.521  38.288  1.000 49.362  ? 383 SER EEE C   1 
ATOM   403   O O   . SER A 1 65  ? 6.473   52.914  39.113  1.000 55.799  ? 383 SER EEE O   1 
ATOM   404   C CB  . SER A 1 65  ? 8.375   54.989  39.843  1.000 55.488  ? 383 SER EEE CB  1 
ATOM   405   O OG  . SER A 1 65  ? 8.757   56.313  40.154  1.000 63.732  ? 383 SER EEE OG  1 
ATOM   406   N N   . PRO A 1 66  ? 7.479   52.928  37.132  1.000 51.219  ? 384 PRO EEE N   1 
ATOM   407   C CA  . PRO A 1 66  ? 7.054   51.564  36.823  1.000 58.837  ? 384 PRO EEE CA  1 
ATOM   408   C C   . PRO A 1 66  ? 7.537   50.559  37.877  1.000 65.446  ? 384 PRO EEE C   1 
ATOM   409   O O   . PRO A 1 66  ? 6.872   49.537  38.062  1.000 71.233  ? 384 PRO EEE O   1 
ATOM   410   C CB  . PRO A 1 66  ? 7.644   51.269  35.434  1.000 57.149  ? 384 PRO EEE CB  1 
ATOM   411   C CG  . PRO A 1 66  ? 8.684   52.326  35.225  1.000 55.105  ? 384 PRO EEE CG  1 
ATOM   412   C CD  . PRO A 1 66  ? 8.257   53.529  36.049  1.000 53.417  ? 384 PRO EEE CD  1 
ATOM   413   N N   . THR A 1 67  ? 8.646   50.896  38.546  1.000 76.402  ? 385 THR EEE N   1 
ATOM   414   C CA  . THR A 1 67  ? 9.330   50.056  39.566  1.000 80.750  ? 385 THR EEE CA  1 
ATOM   415   C C   . THR A 1 67  ? 8.502   50.025  40.858  1.000 80.907  ? 385 THR EEE C   1 
ATOM   416   O O   . THR A 1 67  ? 8.697   49.093  41.641  1.000 87.482  ? 385 THR EEE O   1 
ATOM   417   C CB  . THR A 1 67  ? 10.779  50.522  39.790  1.000 82.736  ? 385 THR EEE CB  1 
ATOM   418   O OG1 . THR A 1 67  ? 10.780  51.856  40.301  1.000 75.375  ? 385 THR EEE OG1 1 
ATOM   419   C CG2 . THR A 1 67  ? 11.617  50.451  38.527  1.000 82.313  ? 385 THR EEE CG2 1 
ATOM   420   N N   . LYS A 1 68  ? 7.586   50.976  41.050  1.000 83.463  ? 386 LYS EEE N   1 
ATOM   421   C CA  . LYS A 1 68  ? 6.867   51.173  42.334  1.000 89.863  ? 386 LYS EEE CA  1 
ATOM   422   C C   . LYS A 1 68  ? 5.351   51.027  42.168  1.000 96.109  ? 386 LYS EEE C   1 
ATOM   423   O O   . LYS A 1 68  ? 4.653   51.499  43.071  1.000 111.922 ? 386 LYS EEE O   1 
ATOM   424   C CB  . LYS A 1 68  ? 7.129   52.573  42.899  1.000 92.742  ? 386 LYS EEE CB  1 
ATOM   425   C CG  . LYS A 1 68  ? 8.562   52.898  43.279  1.000 102.767 ? 386 LYS EEE CG  1 
ATOM   426   C CD  . LYS A 1 68  ? 8.758   54.391  43.530  1.000 114.569 ? 386 LYS EEE CD  1 
ATOM   427   C CE  . LYS A 1 68  ? 9.922   54.700  44.445  1.000 116.442 ? 386 LYS EEE CE  1 
ATOM   428   N NZ  . LYS A 1 68  ? 9.825   53.987  45.741  1.000 119.977 ? 386 LYS EEE NZ  1 
ATOM   429   N N   . LEU A 1 69  ? 4.829   50.420  41.101  1.000 102.506 ? 387 LEU EEE N   1 
ATOM   430   C CA  . LEU A 1 69  ? 3.349   50.353  40.931  1.000 121.015 ? 387 LEU EEE CA  1 
ATOM   431   C C   . LEU A 1 69  ? 2.876   48.910  40.731  1.000 129.171 ? 387 LEU EEE C   1 
ATOM   432   O O   . LEU A 1 69  ? 1.647   48.756  40.521  1.000 135.427 ? 387 LEU EEE O   1 
ATOM   433   C CB  . LEU A 1 69  ? 2.885   51.280  39.797  1.000 125.829 ? 387 LEU EEE CB  1 
ATOM   434   C CG  . LEU A 1 69  ? 3.645   51.222  38.470  1.000 118.628 ? 387 LEU EEE CG  1 
ATOM   435   C CD1 . LEU A 1 69  ? 3.339   49.963  37.699  1.000 106.208 ? 387 LEU EEE CD1 1 
ATOM   436   C CD2 . LEU A 1 69  ? 3.305   52.421  37.602  1.000 113.785 ? 387 LEU EEE CD2 1 
ATOM   437   N N   . ASN A 1 70  ? 3.769   47.909  40.855  1.000 136.416 ? 388 ASN EEE N   1 
ATOM   438   C CA  . ASN A 1 70  ? 3.365   46.475  40.964  1.000 142.373 ? 388 ASN EEE CA  1 
ATOM   439   C C   . ASN A 1 70  ? 3.072   46.175  42.446  1.000 137.298 ? 388 ASN EEE C   1 
ATOM   440   O O   . ASN A 1 70  ? 3.009   44.980  42.822  1.000 147.867 ? 388 ASN EEE O   1 
ATOM   441   C CB  . ASN A 1 70  ? 4.335   45.511  40.258  1.000 143.566 ? 388 ASN EEE CB  1 
ATOM   442   C CG  . ASN A 1 70  ? 5.788   45.665  40.645  1.000 141.718 ? 388 ASN EEE CG  1 
ATOM   443   O OD1 . ASN A 1 70  ? 6.197   45.242  41.722  1.000 138.026 ? 388 ASN EEE OD1 1 
ATOM   444   N ND2 . ASN A 1 70  ? 6.578   46.237  39.755  1.000 133.966 ? 388 ASN EEE ND2 1 
ATOM   445   N N   . ASP A 1 71  ? 2.872   47.235  43.240  1.000 130.452 ? 389 ASP EEE N   1 
ATOM   446   C CA  . ASP A 1 71  ? 2.195   47.202  44.564  1.000 129.425 ? 389 ASP EEE CA  1 
ATOM   447   C C   . ASP A 1 71  ? 1.254   48.414  44.722  1.000 117.233 ? 389 ASP EEE C   1 
ATOM   448   O O   . ASP A 1 71  ? 1.011   48.822  45.879  1.000 105.179 ? 389 ASP EEE O   1 
ATOM   449   C CB  . ASP A 1 71  ? 3.223   47.188  45.693  1.000 130.849 ? 389 ASP EEE CB  1 
ATOM   450   C CG  . ASP A 1 71  ? 3.763   48.571  45.966  1.000 134.567 ? 389 ASP EEE CG  1 
ATOM   451   O OD1 . ASP A 1 71  ? 3.646   49.024  47.118  1.000 150.109 ? 389 ASP EEE OD1 1 
ATOM   452   O OD2 . ASP A 1 71  ? 4.250   49.193  45.011  1.000 124.742 ? 389 ASP EEE OD2 1 
ATOM   453   N N   . LEU A 1 72  ? 0.725   48.979  43.632  1.000 109.336 ? 390 LEU EEE N   1 
ATOM   454   C CA  . LEU A 1 72  ? -0.358  50.000  43.719  1.000 111.290 ? 390 LEU EEE CA  1 
ATOM   455   C C   . LEU A 1 72  ? -1.551  49.641  42.811  1.000 126.611 ? 390 LEU EEE C   1 
ATOM   456   O O   . LEU A 1 72  ? -1.381  48.803  41.870  1.000 113.122 ? 390 LEU EEE O   1 
ATOM   457   C CB  . LEU A 1 72  ? 0.199   51.394  43.413  1.000 100.199 ? 390 LEU EEE CB  1 
ATOM   458   C CG  . LEU A 1 72  ? -0.487  52.498  44.229  1.000 96.769  ? 390 LEU EEE CG  1 
ATOM   459   C CD1 . LEU A 1 72  ? -0.214  52.339  45.717  1.000 92.445  ? 390 LEU EEE CD1 1 
ATOM   460   C CD2 . LEU A 1 72  ? -0.096  53.888  43.761  1.000 94.517  ? 390 LEU EEE CD2 1 
ATOM   461   N N   . CYS A 1 73  ? -2.720  50.232  43.124  1.000 141.603 ? 391 CYS EEE N   1 
ATOM   462   C CA  . CYS A 1 73  ? -4.048  49.990  42.483  1.000 144.403 ? 391 CYS EEE CA  1 
ATOM   463   C C   . CYS A 1 73  ? -4.629  51.288  41.902  1.000 131.946 ? 391 CYS EEE C   1 
ATOM   464   O O   . CYS A 1 73  ? -4.442  52.357  42.523  1.000 112.011 ? 391 CYS EEE O   1 
ATOM   465   C CB  . CYS A 1 73  ? -5.059  49.411  43.471  1.000 155.756 ? 391 CYS EEE CB  1 
ATOM   466   S SG  . CYS A 1 73  ? -4.628  47.754  44.068  1.000 173.620 ? 391 CYS EEE SG  1 
ATOM   467   N N   . PHE A 1 74  ? -5.342  51.172  40.774  1.000 127.742 ? 392 PHE EEE N   1 
ATOM   468   C CA  . PHE A 1 74  ? -5.933  52.280  39.972  1.000 124.875 ? 392 PHE EEE CA  1 
ATOM   469   C C   . PHE A 1 74  ? -7.330  51.865  39.474  1.000 120.084 ? 392 PHE EEE C   1 
ATOM   470   O O   . PHE A 1 74  ? -7.543  50.641  39.280  1.000 126.547 ? 392 PHE EEE O   1 
ATOM   471   C CB  . PHE A 1 74  ? -5.031  52.610  38.776  1.000 128.165 ? 392 PHE EEE CB  1 
ATOM   472   C CG  . PHE A 1 74  ? -3.597  52.970  39.089  1.000 121.769 ? 392 PHE EEE CG  1 
ATOM   473   C CD1 . PHE A 1 74  ? -2.602  51.999  39.073  1.000 113.214 ? 392 PHE EEE CD1 1 
ATOM   474   C CD2 . PHE A 1 74  ? -3.238  54.281  39.372  1.000 111.582 ? 392 PHE EEE CD2 1 
ATOM   475   C CE1 . PHE A 1 74  ? -1.286  52.331  39.356  1.000 106.032 ? 392 PHE EEE CE1 1 
ATOM   476   C CE2 . PHE A 1 74  ? -1.922  54.609  39.659  1.000 103.679 ? 392 PHE EEE CE2 1 
ATOM   477   C CZ  . PHE A 1 74  ? -0.949  53.635  39.644  1.000 104.425 ? 392 PHE EEE CZ  1 
ATOM   478   N N   . THR A 1 75  ? -8.242  52.830  39.266  1.000 108.418 ? 393 THR EEE N   1 
ATOM   479   C CA  . THR A 1 75  ? -9.624  52.611  38.734  1.000 102.452 ? 393 THR EEE CA  1 
ATOM   480   C C   . THR A 1 75  ? -9.550  52.090  37.295  1.000 95.746  ? 393 THR EEE C   1 
ATOM   481   O O   . THR A 1 75  ? -10.231 51.107  36.976  1.000 88.665  ? 393 THR EEE O   1 
ATOM   482   C CB  . THR A 1 75  ? -10.480 53.886  38.749  1.000 103.610 ? 393 THR EEE CB  1 
ATOM   483   O OG1 . THR A 1 75  ? -9.694  54.959  38.228  1.000 102.577 ? 393 THR EEE OG1 1 
ATOM   484   C CG2 . THR A 1 75  ? -10.995 54.231  40.130  1.000 113.878 ? 393 THR EEE CG2 1 
ATOM   485   N N   . ASN A 1 76  ? -8.746  52.740  36.456  1.000 94.755  ? 394 ASN EEE N   1 
ATOM   486   C CA  . ASN A 1 76  ? -8.588  52.352  35.034  1.000 88.388  ? 394 ASN EEE CA  1 
ATOM   487   C C   . ASN A 1 76  ? -7.167  52.631  34.553  1.000 76.378  ? 394 ASN EEE C   1 
ATOM   488   O O   . ASN A 1 76  ? -6.576  53.682  34.886  1.000 63.081  ? 394 ASN EEE O   1 
ATOM   489   C CB  . ASN A 1 76  ? -9.607  53.044  34.133  1.000 97.207  ? 394 ASN EEE CB  1 
ATOM   490   C CG  . ASN A 1 76  ? -10.925 52.312  34.121  1.000 104.819 ? 394 ASN EEE CG  1 
ATOM   491   O OD1 . ASN A 1 76  ? -11.024 51.215  33.573  1.000 133.019 ? 394 ASN EEE OD1 1 
ATOM   492   N ND2 . ASN A 1 76  ? -11.924 52.900  34.754  1.000 99.178  ? 394 ASN EEE ND2 1 
ATOM   493   N N   . VAL A 1 77  ? -6.680  51.692  33.754  1.000 67.369  ? 395 VAL EEE N   1 
ATOM   494   C CA  . VAL A 1 77  ? -5.401  51.778  33.011  1.000 65.538  ? 395 VAL EEE CA  1 
ATOM   495   C C   . VAL A 1 77  ? -5.745  51.620  31.536  1.000 59.071  ? 395 VAL EEE C   1 
ATOM   496   O O   . VAL A 1 77  ? -6.508  50.700  31.217  1.000 60.287  ? 395 VAL EEE O   1 
ATOM   497   C CB  . VAL A 1 77  ? -4.425  50.691  33.492  1.000 74.794  ? 395 VAL EEE CB  1 
ATOM   498   C CG1 . VAL A 1 77  ? -3.128  50.687  32.692  1.000 80.332  ? 395 VAL EEE CG1 1 
ATOM   499   C CG2 . VAL A 1 77  ? -4.149  50.834  34.976  1.000 78.064  ? 395 VAL EEE CG2 1 
ATOM   500   N N   . TYR A 1 78  ? -5.204  52.492  30.691  1.000 52.970  ? 396 TYR EEE N   1 
ATOM   501   C CA  . TYR A 1 78  ? -5.401  52.463  29.224  1.000 53.776  ? 396 TYR EEE CA  1 
ATOM   502   C C   . TYR A 1 78  ? -4.044  52.190  28.561  1.000 51.779  ? 396 TYR EEE C   1 
ATOM   503   O O   . TYR A 1 78  ? -3.042  52.806  28.958  1.000 52.165  ? 396 TYR EEE O   1 
ATOM   504   C CB  . TYR A 1 78  ? -6.064  53.762  28.750  1.000 57.589  ? 396 TYR EEE CB  1 
ATOM   505   C CG  . TYR A 1 78  ? -7.380  54.114  29.408  1.000 57.925  ? 396 TYR EEE CG  1 
ATOM   506   C CD1 . TYR A 1 78  ? -8.496  53.313  29.239  1.000 57.282  ? 396 TYR EEE CD1 1 
ATOM   507   C CD2 . TYR A 1 78  ? -7.524  55.270  30.172  1.000 58.846  ? 396 TYR EEE CD2 1 
ATOM   508   C CE1 . TYR A 1 78  ? -9.710  53.624  29.840  1.000 61.592  ? 396 TYR EEE CE1 1 
ATOM   509   C CE2 . TYR A 1 78  ? -8.730  55.596  30.780  1.000 57.346  ? 396 TYR EEE CE2 1 
ATOM   510   C CZ  . TYR A 1 78  ? -9.828  54.768  30.617  1.000 58.867  ? 396 TYR EEE CZ  1 
ATOM   511   O OH  . TYR A 1 78  ? -11.023 55.079  31.205  1.000 54.228  ? 396 TYR EEE OH  1 
ATOM   512   N N   . ALA A 1 79  ? -4.037  51.299  27.568  1.000 51.302  ? 397 ALA EEE N   1 
ATOM   513   C CA  . ALA A 1 79  ? -2.868  50.923  26.741  1.000 53.059  ? 397 ALA EEE CA  1 
ATOM   514   C C   . ALA A 1 79  ? -3.102  51.315  25.270  1.000 50.023  ? 397 ALA EEE C   1 
ATOM   515   O O   . ALA A 1 79  ? -3.698  50.508  24.508  1.000 46.956  ? 397 ALA EEE O   1 
ATOM   516   C CB  . ALA A 1 79  ? -2.616  49.441  26.905  1.000 55.252  ? 397 ALA EEE CB  1 
ATOM   517   N N   . ASP A 1 80  ? -2.625  52.501  24.884  1.000 50.079  ? 398 ASP EEE N   1 
ATOM   518   C CA  . ASP A 1 80  ? -2.775  53.054  23.508  1.000 55.495  ? 398 ASP EEE CA  1 
ATOM   519   C C   . ASP A 1 80  ? -1.601  52.553  22.668  1.000 55.428  ? 398 ASP EEE C   1 
ATOM   520   O O   . ASP A 1 80  ? -0.476  52.744  23.106  1.000 74.194  ? 398 ASP EEE O   1 
ATOM   521   C CB  . ASP A 1 80  ? -2.868  54.585  23.519  1.000 54.871  ? 398 ASP EEE CB  1 
ATOM   522   C CG  . ASP A 1 80  ? -3.919  55.104  24.485  1.000 56.870  ? 398 ASP EEE CG  1 
ATOM   523   O OD1 . ASP A 1 80  ? -4.803  54.318  24.832  1.000 60.643  ? 398 ASP EEE OD1 1 
ATOM   524   O OD2 . ASP A 1 80  ? -3.844  56.287  24.886  1.000 57.838  ? 398 ASP EEE OD2 1 
ATOM   525   N N   . SER A 1 81  ? -1.859  51.916  21.532  1.000 51.607  ? 399 SER EEE N   1 
ATOM   526   C CA  . SER A 1 81  ? -0.830  51.322  20.647  1.000 51.606  ? 399 SER EEE CA  1 
ATOM   527   C C   . SER A 1 81  ? -0.958  51.931  19.258  1.000 52.116  ? 399 SER EEE C   1 
ATOM   528   O O   . SER A 1 81  ? -2.069  52.135  18.827  1.000 54.734  ? 399 SER EEE O   1 
ATOM   529   C CB  . SER A 1 81  ? -0.922  49.806  20.601  1.000 52.761  ? 399 SER EEE CB  1 
ATOM   530   O OG  . SER A 1 81  ? -2.261  49.349  20.522  1.000 57.302  ? 399 SER EEE OG  1 
ATOM   531   N N   . PHE A 1 82  ? 0.151   52.185  18.576  1.000 59.996  ? 400 PHE EEE N   1 
ATOM   532   C CA  . PHE A 1 82  ? 0.152   52.671  17.174  1.000 60.639  ? 400 PHE EEE CA  1 
ATOM   533   C C   . PHE A 1 82  ? 1.566   52.576  16.606  1.000 60.503  ? 400 PHE EEE C   1 
ATOM   534   O O   . PHE A 1 82  ? 2.421   52.055  17.318  1.000 64.979  ? 400 PHE EEE O   1 
ATOM   535   C CB  . PHE A 1 82  ? -0.382  54.099  17.121  1.000 60.858  ? 400 PHE EEE CB  1 
ATOM   536   C CG  . PHE A 1 82  ? 0.272   55.044  18.088  1.000 62.527  ? 400 PHE EEE CG  1 
ATOM   537   C CD1 . PHE A 1 82  ? 1.456   55.681  17.756  1.000 64.230  ? 400 PHE EEE CD1 1 
ATOM   538   C CD2 . PHE A 1 82  ? -0.317  55.321  19.313  1.000 64.472  ? 400 PHE EEE CD2 1 
ATOM   539   C CE1 . PHE A 1 82  ? 2.038   56.581  18.633  1.000 67.165  ? 400 PHE EEE CE1 1 
ATOM   540   C CE2 . PHE A 1 82  ? 0.264   56.223  20.188  1.000 67.992  ? 400 PHE EEE CE2 1 
ATOM   541   C CZ  . PHE A 1 82  ? 1.443   56.848  19.848  1.000 69.304  ? 400 PHE EEE CZ  1 
ATOM   542   N N   . VAL A 1 83  ? 1.786   53.048  15.375  1.000 60.003  ? 401 VAL EEE N   1 
ATOM   543   C CA  . VAL A 1 83  ? 3.112   53.023  14.697  1.000 59.026  ? 401 VAL EEE CA  1 
ATOM   544   C C   . VAL A 1 83  ? 3.385   54.384  14.065  1.000 61.429  ? 401 VAL EEE C   1 
ATOM   545   O O   . VAL A 1 83  ? 2.493   54.925  13.366  1.000 62.883  ? 401 VAL EEE O   1 
ATOM   546   C CB  . VAL A 1 83  ? 3.203   51.913  13.635  1.000 60.462  ? 401 VAL EEE CB  1 
ATOM   547   C CG1 . VAL A 1 83  ? 4.434   52.079  12.756  1.000 61.104  ? 401 VAL EEE CG1 1 
ATOM   548   C CG2 . VAL A 1 83  ? 3.188   50.526  14.262  1.000 62.322  ? 401 VAL EEE CG2 1 
ATOM   549   N N   . ILE A 1 84  ? 4.611   54.864  14.272  1.000 68.163  ? 402 ILE EEE N   1 
ATOM   550   C CA  . ILE A 1 84  ? 5.185   56.115  13.703  1.000 70.501  ? 402 ILE EEE CA  1 
ATOM   551   C C   . ILE A 1 84  ? 6.654   55.838  13.365  1.000 72.274  ? 402 ILE EEE C   1 
ATOM   552   O O   . ILE A 1 84  ? 7.120   54.694  13.591  1.000 69.117  ? 402 ILE EEE O   1 
ATOM   553   C CB  . ILE A 1 84  ? 5.034   57.259  14.724  1.000 75.449  ? 402 ILE EEE CB  1 
ATOM   554   C CG1 . ILE A 1 84  ? 5.461   56.813  16.127  1.000 76.250  ? 402 ILE EEE CG1 1 
ATOM   555   C CG2 . ILE A 1 84  ? 3.614   57.796  14.723  1.000 75.263  ? 402 ILE EEE CG2 1 
ATOM   556   C CD1 . ILE A 1 84  ? 5.674   57.948  17.085  1.000 77.664  ? 402 ILE EEE CD1 1 
ATOM   557   N N   . ARG A 1 85  ? 7.367   56.842  12.854  1.000 76.360  ? 403 ARG EEE N   1 
ATOM   558   C CA  . ARG A 1 85  ? 8.815   56.719  12.545  1.000 79.655  ? 403 ARG EEE CA  1 
ATOM   559   C C   . ARG A 1 85  ? 9.615   57.287  13.720  1.000 80.390  ? 403 ARG EEE C   1 
ATOM   560   O O   . ARG A 1 85  ? 9.047   58.073  14.496  1.000 85.425  ? 403 ARG EEE O   1 
ATOM   561   C CB  . ARG A 1 85  ? 9.139   57.381  11.204  1.000 81.407  ? 403 ARG EEE CB  1 
ATOM   562   C CG  . ARG A 1 85  ? 8.954   58.888  11.149  1.000 80.491  ? 403 ARG EEE CG  1 
ATOM   563   C CD  . ARG A 1 85  ? 9.162   59.443  9.743   1.000 82.996  ? 403 ARG EEE CD  1 
ATOM   564   N NE  . ARG A 1 85  ? 8.972   60.892  9.755   1.000 88.337  ? 403 ARG EEE NE  1 
ATOM   565   C CZ  . ARG A 1 85  ? 9.934   61.825  9.766   1.000 92.427  ? 403 ARG EEE CZ  1 
ATOM   566   N NH1 . ARG A 1 85  ? 11.220  61.507  9.730   1.000 93.603  ? 403 ARG EEE NH1 1 
ATOM   567   N NH2 . ARG A 1 85  ? 9.595   63.101  9.824   1.000 90.348  ? 403 ARG EEE NH2 1 
ATOM   568   N N   . GLY A 1 86  ? 10.874  56.868  13.845  1.000 76.362  ? 404 GLY EEE N   1 
ATOM   569   C CA  . GLY A 1 86  ? 11.753  57.164  14.991  1.000 73.737  ? 404 GLY EEE CA  1 
ATOM   570   C C   . GLY A 1 86  ? 11.846  58.650  15.294  1.000 73.171  ? 404 GLY EEE C   1 
ATOM   571   O O   . GLY A 1 86  ? 11.788  59.003  16.484  1.000 65.581  ? 404 GLY EEE O   1 
ATOM   572   N N   . ASP A 1 87  ? 11.974  59.499  14.270  1.000 78.365  ? 405 ASP EEE N   1 
ATOM   573   C CA  . ASP A 1 87  ? 12.076  60.980  14.426  1.000 87.339  ? 405 ASP EEE CA  1 
ATOM   574   C C   . ASP A 1 87  ? 10.897  61.521  15.244  1.000 88.612  ? 405 ASP EEE C   1 
ATOM   575   O O   . ASP A 1 87  ? 11.024  62.638  15.791  1.000 81.601  ? 405 ASP EEE O   1 
ATOM   576   C CB  . ASP A 1 87  ? 12.065  61.709  13.080  1.000 94.029  ? 405 ASP EEE CB  1 
ATOM   577   C CG  . ASP A 1 87  ? 13.400  61.726  12.363  1.000 101.202 ? 405 ASP EEE CG  1 
ATOM   578   O OD1 . ASP A 1 87  ? 14.025  62.806  12.338  1.000 103.819 ? 405 ASP EEE OD1 1 
ATOM   579   O OD2 . ASP A 1 87  ? 13.792  60.668  11.821  1.000 107.763 ? 405 ASP EEE OD2 1 
ATOM   580   N N   . GLU A 1 88  ? 9.792   60.769  15.291  1.000 94.905  ? 406 GLU EEE N   1 
ATOM   581   C CA  . GLU A 1 88  ? 8.474   61.227  15.801  1.000 88.576  ? 406 GLU EEE CA  1 
ATOM   582   C C   . GLU A 1 88  ? 8.212   60.646  17.202  1.000 75.386  ? 406 GLU EEE C   1 
ATOM   583   O O   . GLU A 1 88  ? 7.283   61.133  17.848  1.000 76.320  ? 406 GLU EEE O   1 
ATOM   584   C CB  . GLU A 1 88  ? 7.373   60.856  14.796  1.000 96.566  ? 406 GLU EEE CB  1 
ATOM   585   C CG  . GLU A 1 88  ? 7.365   61.702  13.524  1.000 103.827 ? 406 GLU EEE CG  1 
ATOM   586   C CD  . GLU A 1 88  ? 6.382   61.272  12.438  1.000 105.009 ? 406 GLU EEE CD  1 
ATOM   587   O OE1 . GLU A 1 88  ? 5.849   60.146  12.541  1.000 96.323  ? 406 GLU EEE OE1 1 
ATOM   588   O OE2 . GLU A 1 88  ? 6.157   62.058  11.481  1.000 101.501 ? 406 GLU EEE OE2 1 
ATOM   589   N N   . VAL A 1 89  ? 9.000   59.687  17.701  1.000 60.603  ? 407 VAL EEE N   1 
ATOM   590   C CA  . VAL A 1 89  ? 8.721   59.095  19.041  1.000 55.762  ? 407 VAL EEE CA  1 
ATOM   591   C C   . VAL A 1 89  ? 8.932   60.174  20.095  1.000 58.344  ? 407 VAL EEE C   1 
ATOM   592   O O   . VAL A 1 89  ? 8.234   60.118  21.107  1.000 56.068  ? 407 VAL EEE O   1 
ATOM   593   C CB  . VAL A 1 89  ? 9.568   57.857  19.368  1.000 54.141  ? 407 VAL EEE CB  1 
ATOM   594   C CG1 . VAL A 1 89  ? 9.197   57.276  20.731  1.000 51.188  ? 407 VAL EEE CG1 1 
ATOM   595   C CG2 . VAL A 1 89  ? 9.455   56.808  18.282  1.000 55.345  ? 407 VAL EEE CG2 1 
ATOM   596   N N   . ARG A 1 90  ? 9.868   61.101  19.875  1.000 69.158  ? 408 ARG EEE N   1 
ATOM   597   C CA  . ARG A 1 90  ? 10.086  62.259  20.783  1.000 83.511  ? 408 ARG EEE CA  1 
ATOM   598   C C   . ARG A 1 90  ? 8.776   63.038  20.963  1.000 78.751  ? 408 ARG EEE C   1 
ATOM   599   O O   . ARG A 1 90  ? 8.614   63.657  22.034  1.000 79.092  ? 408 ARG EEE O   1 
ATOM   600   C CB  . ARG A 1 90  ? 11.181  63.184  20.247  1.000 105.355 ? 408 ARG EEE CB  1 
ATOM   601   C CG  . ARG A 1 90  ? 10.900  63.792  18.875  1.000 122.353 ? 408 ARG EEE CG  1 
ATOM   602   C CD  . ARG A 1 90  ? 11.533  65.156  18.626  1.000 128.584 ? 408 ARG EEE CD  1 
ATOM   603   N NE  . ARG A 1 90  ? 12.837  65.284  19.277  1.000 146.573 ? 408 ARG EEE NE  1 
ATOM   604   C CZ  . ARG A 1 90  ? 13.970  64.691  18.882  1.000 143.965 ? 408 ARG EEE CZ  1 
ATOM   605   N NH1 . ARG A 1 90  ? 15.080  64.879  19.579  1.000 139.806 ? 408 ARG EEE NH1 1 
ATOM   606   N NH2 . ARG A 1 90  ? 13.991  63.912  17.808  1.000 141.126 ? 408 ARG EEE NH2 1 
ATOM   607   N N   . GLN A 1 91  ? 7.900   63.015  19.949  1.000 74.501  ? 409 GLN EEE N   1 
ATOM   608   C CA  . GLN A 1 91  ? 6.634   63.793  19.880  1.000 70.489  ? 409 GLN EEE CA  1 
ATOM   609   C C   . GLN A 1 91  ? 5.565   63.151  20.774  1.000 61.888  ? 409 GLN EEE C   1 
ATOM   610   O O   . GLN A 1 91  ? 4.620   63.859  21.122  1.000 68.895  ? 409 GLN EEE O   1 
ATOM   611   C CB  . GLN A 1 91  ? 6.112   63.911  18.443  1.000 71.514  ? 409 GLN EEE CB  1 
ATOM   612   C CG  . GLN A 1 91  ? 6.430   65.234  17.770  1.000 78.048  ? 409 GLN EEE CG  1 
ATOM   613   C CD  . GLN A 1 91  ? 5.911   65.290  16.351  1.000 80.390  ? 409 GLN EEE CD  1 
ATOM   614   O OE1 . GLN A 1 91  ? 4.753   65.617  16.089  1.000 79.979  ? 409 GLN EEE OE1 1 
ATOM   615   N NE2 . GLN A 1 91  ? 6.776   64.975  15.406  1.000 85.386  ? 409 GLN EEE NE2 1 
ATOM   616   N N   . ILE A 1 92  ? 5.695   61.875  21.135  1.000 50.966  ? 410 ILE EEE N   1 
ATOM   617   C CA  . ILE A 1 92  ? 4.714   61.183  22.014  1.000 47.875  ? 410 ILE EEE CA  1 
ATOM   618   C C   . ILE A 1 92  ? 5.061   61.501  23.463  1.000 45.673  ? 410 ILE EEE C   1 
ATOM   619   O O   . ILE A 1 92  ? 5.516   60.606  24.155  1.000 44.350  ? 410 ILE EEE O   1 
ATOM   620   C CB  . ILE A 1 92  ? 4.722   59.669  21.758  1.000 50.774  ? 410 ILE EEE CB  1 
ATOM   621   C CG1 . ILE A 1 92  ? 4.595   59.357  20.267  1.000 53.133  ? 410 ILE EEE CG1 1 
ATOM   622   C CG2 . ILE A 1 92  ? 3.641   58.969  22.575  1.000 53.757  ? 410 ILE EEE CG2 1 
ATOM   623   C CD1 . ILE A 1 92  ? 3.435   60.051  19.585  1.000 55.651  ? 410 ILE EEE CD1 1 
ATOM   624   N N   . ALA A 1 93  ? 4.845   62.739  23.897  1.000 47.737  ? 411 ALA EEE N   1 
ATOM   625   C CA  . ALA A 1 93  ? 5.233   63.221  25.245  1.000 51.875  ? 411 ALA EEE CA  1 
ATOM   626   C C   . ALA A 1 93  ? 4.500   64.506  25.588  1.000 50.887  ? 411 ALA EEE C   1 
ATOM   627   O O   . ALA A 1 93  ? 4.300   65.350  24.721  1.000 52.986  ? 411 ALA EEE O   1 
ATOM   628   C CB  . ALA A 1 93  ? 6.724   63.465  25.307  1.000 58.831  ? 411 ALA EEE CB  1 
ATOM   629   N N   . PRO A 1 94  ? 4.136   64.733  26.867  1.000 50.621  ? 412 PRO EEE N   1 
ATOM   630   C CA  . PRO A 1 94  ? 3.487   65.979  27.255  1.000 54.118  ? 412 PRO EEE CA  1 
ATOM   631   C C   . PRO A 1 94  ? 4.253   67.174  26.683  1.000 56.309  ? 412 PRO EEE C   1 
ATOM   632   O O   . PRO A 1 94  ? 5.466   67.140  26.672  1.000 64.455  ? 412 PRO EEE O   1 
ATOM   633   C CB  . PRO A 1 94  ? 3.533   65.986  28.788  1.000 55.506  ? 412 PRO EEE CB  1 
ATOM   634   C CG  . PRO A 1 94  ? 4.477   64.851  29.136  1.000 56.100  ? 412 PRO EEE CG  1 
ATOM   635   C CD  . PRO A 1 94  ? 4.341   63.842  28.013  1.000 51.561  ? 412 PRO EEE CD  1 
ATOM   636   N N   . GLY A 1 95  ? 3.511   68.156  26.177  1.000 58.253  ? 413 GLY EEE N   1 
ATOM   637   C CA  . GLY A 1 95  ? 4.011   69.495  25.825  1.000 57.491  ? 413 GLY EEE CA  1 
ATOM   638   C C   . GLY A 1 95  ? 4.774   69.530  24.511  1.000 56.043  ? 413 GLY EEE C   1 
ATOM   639   O O   . GLY A 1 95  ? 5.466   70.527  24.293  1.000 67.897  ? 413 GLY EEE O   1 
ATOM   640   N N   . GLN A 1 96  ? 4.633   68.528  23.644  1.000 51.533  ? 414 GLN EEE N   1 
ATOM   641   C CA  . GLN A 1 96  ? 5.286   68.501  22.308  1.000 57.047  ? 414 GLN EEE CA  1 
ATOM   642   C C   . GLN A 1 96  ? 4.386   69.179  21.266  1.000 59.599  ? 414 GLN EEE C   1 
ATOM   643   O O   . GLN A 1 96  ? 3.221   69.498  21.592  1.000 61.947  ? 414 GLN EEE O   1 
ATOM   644   C CB  . GLN A 1 96  ? 5.569   67.060  21.910  1.000 61.945  ? 414 GLN EEE CB  1 
ATOM   645   C CG  . GLN A 1 96  ? 6.560   66.377  22.839  1.000 67.631  ? 414 GLN EEE CG  1 
ATOM   646   C CD  . GLN A 1 96  ? 7.947   66.946  22.661  1.000 70.536  ? 414 GLN EEE CD  1 
ATOM   647   O OE1 . GLN A 1 96  ? 8.433   67.103  21.539  1.000 72.016  ? 414 GLN EEE OE1 1 
ATOM   648   N NE2 . GLN A 1 96  ? 8.590   67.260  23.776  1.000 66.099  ? 414 GLN EEE NE2 1 
ATOM   649   N N   . THR A 1 97  ? 4.917   69.408  20.059  1.000 62.761  ? 415 THR EEE N   1 
ATOM   650   C CA  . THR A 1 97  ? 4.165   69.936  18.883  1.000 66.705  ? 415 THR EEE CA  1 
ATOM   651   C C   . THR A 1 97  ? 4.722   69.278  17.613  1.000 67.609  ? 415 THR EEE C   1 
ATOM   652   O O   . THR A 1 97  ? 5.812   68.690  17.705  1.000 66.327  ? 415 THR EEE O   1 
ATOM   653   C CB  . THR A 1 97  ? 4.200   71.473  18.809  1.000 64.797  ? 415 THR EEE CB  1 
ATOM   654   O OG1 . THR A 1 97  ? 5.495   71.817  18.328  1.000 62.375  ? 415 THR EEE OG1 1 
ATOM   655   C CG2 . THR A 1 97  ? 3.925   72.181  20.123  1.000 64.123  ? 415 THR EEE CG2 1 
ATOM   656   N N   . GLY A 1 98  ? 3.984   69.368  16.495  1.000 73.466  ? 416 GLY EEE N   1 
ATOM   657   C CA  . GLY A 1 98  ? 4.330   68.778  15.184  1.000 72.844  ? 416 GLY EEE CA  1 
ATOM   658   C C   . GLY A 1 98  ? 3.149   68.044  14.574  1.000 70.759  ? 416 GLY EEE C   1 
ATOM   659   O O   . GLY A 1 98  ? 2.040   68.171  15.107  1.000 68.960  ? 416 GLY EEE O   1 
ATOM   660   N N   . LYS A 1 99  ? 3.390   67.295  13.499  1.000 71.631  ? 417 LYS EEE N   1 
ATOM   661   C CA  . LYS A 1 99  ? 2.364   66.490  12.793  1.000 79.611  ? 417 LYS EEE CA  1 
ATOM   662   C C   . LYS A 1 99  ? 1.671   65.566  13.792  1.000 76.978  ? 417 LYS EEE C   1 
ATOM   663   O O   . LYS A 1 99  ? 0.428   65.587  13.867  1.000 96.505  ? 417 LYS EEE O   1 
ATOM   664   C CB  . LYS A 1 99  ? 2.982   65.647  11.671  1.000 88.701  ? 417 LYS EEE CB  1 
ATOM   665   C CG  . LYS A 1 99  ? 3.538   66.438  10.492  1.000 101.016 ? 417 LYS EEE CG  1 
ATOM   666   C CD  . LYS A 1 99  ? 2.609   67.553  10.001  1.000 109.833 ? 417 LYS EEE CD  1 
ATOM   667   C CE  . LYS A 1 99  ? 3.249   68.481  8.992   1.000 108.409 ? 417 LYS EEE CE  1 
ATOM   668   N NZ  . LYS A 1 99  ? 2.311   69.558  8.605   1.000 109.797 ? 417 LYS EEE NZ  1 
ATOM   669   N N   . ILE A 1 100 ? 2.449   64.775  14.524  1.000 63.778  ? 418 ILE EEE N   1 
ATOM   670   C CA  . ILE A 1 100 ? 1.908   63.632  15.311  1.000 59.308  ? 418 ILE EEE CA  1 
ATOM   671   C C   . ILE A 1 100 ? 1.276   64.148  16.595  1.000 59.148  ? 418 ILE EEE C   1 
ATOM   672   O O   . ILE A 1 100 ? 0.206   63.675  16.963  1.000 63.836  ? 418 ILE EEE O   1 
ATOM   673   C CB  . ILE A 1 100 ? 2.999   62.607  15.626  1.000 56.983  ? 418 ILE EEE CB  1 
ATOM   674   C CG1 . ILE A 1 100 ? 3.704   62.135  14.356  1.000 59.534  ? 418 ILE EEE CG1 1 
ATOM   675   C CG2 . ILE A 1 100 ? 2.420   61.454  16.418  1.000 57.524  ? 418 ILE EEE CG2 1 
ATOM   676   C CD1 . ILE A 1 100 ? 2.767   61.737  13.248  1.000 58.796  ? 418 ILE EEE CD1 1 
ATOM   677   N N   . ALA A 1 101 ? 1.950   65.056  17.271  1.000 62.285  ? 419 ALA EEE N   1 
ATOM   678   C CA  . ALA A 1 101 ? 1.502   65.586  18.570  1.000 66.691  ? 419 ALA EEE CA  1 
ATOM   679   C C   . ALA A 1 101 ? 0.194   66.346  18.366  1.000 67.045  ? 419 ALA EEE C   1 
ATOM   680   O O   . ALA A 1 101 ? -0.672  66.246  19.229  1.000 70.016  ? 419 ALA EEE O   1 
ATOM   681   C CB  . ALA A 1 101 ? 2.581   66.459  19.169  1.000 71.596  ? 419 ALA EEE CB  1 
ATOM   682   N N   . ASP A 1 102 ? 0.058   67.082  17.269  1.000 67.924  ? 420 ASP EEE N   1 
ATOM   683   C CA  . ASP A 1 102 ? -1.034  68.077  17.128  1.000 77.472  ? 420 ASP EEE CA  1 
ATOM   684   C C   . ASP A 1 102 ? -2.227  67.473  16.386  1.000 76.393  ? 420 ASP EEE C   1 
ATOM   685   O O   . ASP A 1 102 ? -3.353  67.884  16.708  1.000 70.079  ? 420 ASP EEE O   1 
ATOM   686   C CB  . ASP A 1 102 ? -0.520  69.356  16.467  1.000 83.676  ? 420 ASP EEE CB  1 
ATOM   687   C CG  . ASP A 1 102 ? 0.396   70.138  17.401  1.000 79.378  ? 420 ASP EEE CG  1 
ATOM   688   O OD1 . ASP A 1 102 ? 0.545   69.703  18.565  1.000 76.837  ? 420 ASP EEE OD1 1 
ATOM   689   O OD2 . ASP A 1 102 ? 0.942   71.178  16.973  1.000 73.479  ? 420 ASP EEE OD2 1 
ATOM   690   N N   . TYR A 1 103 ? -1.998  66.555  15.438  1.000 74.616  ? 421 TYR EEE N   1 
ATOM   691   C CA  . TYR A 1 103 ? -3.035  66.105  14.473  1.000 74.720  ? 421 TYR EEE CA  1 
ATOM   692   C C   . TYR A 1 103 ? -3.339  64.601  14.623  1.000 76.133  ? 421 TYR EEE C   1 
ATOM   693   O O   . TYR A 1 103 ? -4.245  64.096  13.908  1.000 93.896  ? 421 TYR EEE O   1 
ATOM   694   C CB  . TYR A 1 103 ? -2.616  66.448  13.034  1.000 73.200  ? 421 TYR EEE CB  1 
ATOM   695   C CG  . TYR A 1 103 ? -2.458  67.914  12.678  1.000 75.574  ? 421 TYR EEE CG  1 
ATOM   696   C CD1 . TYR A 1 103 ? -2.858  68.943  13.530  1.000 75.992  ? 421 TYR EEE CD1 1 
ATOM   697   C CD2 . TYR A 1 103 ? -1.927  68.280  11.447  1.000 74.296  ? 421 TYR EEE CD2 1 
ATOM   698   C CE1 . TYR A 1 103 ? -2.716  70.278  13.176  1.000 73.934  ? 421 TYR EEE CE1 1 
ATOM   699   C CE2 . TYR A 1 103 ? -1.773  69.611  11.078  1.000 73.879  ? 421 TYR EEE CE2 1 
ATOM   700   C CZ  . TYR A 1 103 ? -2.171  70.616  11.944  1.000 76.160  ? 421 TYR EEE CZ  1 
ATOM   701   O OH  . TYR A 1 103 ? -2.026  71.926  11.575  1.000 76.309  ? 421 TYR EEE OH  1 
ATOM   702   N N   . ASN A 1 104 ? -2.667  63.864  15.511  1.000 70.157  ? 422 ASN EEE N   1 
ATOM   703   C CA  . ASN A 1 104 ? -2.771  62.375  15.467  1.000 70.174  ? 422 ASN EEE CA  1 
ATOM   704   C C   . ASN A 1 104 ? -2.978  61.774  16.868  1.000 69.215  ? 422 ASN EEE C   1 
ATOM   705   O O   . ASN A 1 104 ? -3.987  61.042  17.052  1.000 73.428  ? 422 ASN EEE O   1 
ATOM   706   C CB  . ASN A 1 104 ? -1.574  61.772  14.725  1.000 65.976  ? 422 ASN EEE CB  1 
ATOM   707   C CG  . ASN A 1 104 ? -1.526  62.140  13.254  1.000 63.709  ? 422 ASN EEE CG  1 
ATOM   708   O OD1 . ASN A 1 104 ? -1.952  61.347  12.411  1.000 68.964  ? 422 ASN EEE OD1 1 
ATOM   709   N ND2 . ASN A 1 104 ? -1.008  63.318  12.927  1.000 50.724  ? 422 ASN EEE ND2 1 
ATOM   710   N N   . TYR A 1 105 ? -2.054  62.049  17.795  1.000 62.379  ? 423 TYR EEE N   1 
ATOM   711   C CA  . TYR A 1 105 ? -2.056  61.575  19.200  1.000 53.715  ? 423 TYR EEE CA  1 
ATOM   712   C C   . TYR A 1 105 ? -1.440  62.655  20.083  1.000 52.071  ? 423 TYR EEE C   1 
ATOM   713   O O   . TYR A 1 105 ? -0.232  62.864  19.950  1.000 53.226  ? 423 TYR EEE O   1 
ATOM   714   C CB  . TYR A 1 105 ? -1.246  60.290  19.331  1.000 51.727  ? 423 TYR EEE CB  1 
ATOM   715   C CG  . TYR A 1 105 ? -1.432  59.600  20.656  1.000 55.080  ? 423 TYR EEE CG  1 
ATOM   716   C CD1 . TYR A 1 105 ? -2.501  58.753  20.863  1.000 58.367  ? 423 TYR EEE CD1 1 
ATOM   717   C CD2 . TYR A 1 105 ? -0.553  59.787  21.710  1.000 60.600  ? 423 TYR EEE CD2 1 
ATOM   718   C CE1 . TYR A 1 105 ? -2.693  58.114  22.079  1.000 59.280  ? 423 TYR EEE CE1 1 
ATOM   719   C CE2 . TYR A 1 105 ? -0.728  59.154  22.931  1.000 59.181  ? 423 TYR EEE CE2 1 
ATOM   720   C CZ  . TYR A 1 105 ? -1.809  58.318  23.122  1.000 56.579  ? 423 TYR EEE CZ  1 
ATOM   721   O OH  . TYR A 1 105 ? -2.016  57.702  24.321  1.000 50.788  ? 423 TYR EEE OH  1 
ATOM   722   N N   . LYS A 1 106 ? -2.251  63.341  20.890  1.000 51.894  ? 424 LYS EEE N   1 
ATOM   723   C CA  . LYS A 1 106 ? -1.806  64.376  21.861  1.000 53.619  ? 424 LYS EEE CA  1 
ATOM   724   C C   . LYS A 1 106 ? -1.903  63.775  23.265  1.000 56.816  ? 424 LYS EEE C   1 
ATOM   725   O O   . LYS A 1 106 ? -2.855  63.012  23.506  1.000 69.171  ? 424 LYS EEE O   1 
ATOM   726   C CB  . LYS A 1 106 ? -2.674  65.635  21.774  1.000 54.178  ? 424 LYS EEE CB  1 
ATOM   727   C CG  . LYS A 1 106 ? -2.076  66.909  22.363  1.000 60.751  ? 424 LYS EEE CG  1 
ATOM   728   C CD  . LYS A 1 106 ? -1.894  68.030  21.335  1.000 69.086  ? 424 LYS EEE CD  1 
ATOM   729   C CE  . LYS A 1 106 ? -1.386  69.340  21.911  1.000 71.363  ? 424 LYS EEE CE  1 
ATOM   730   N NZ  . LYS A 1 106 ? 0.008   69.232  22.400  1.000 70.867  ? 424 LYS EEE NZ  1 
ATOM   731   N N   . LEU A 1 107 ? -0.938  64.088  24.132  1.000 50.615  ? 425 LEU EEE N   1 
ATOM   732   C CA  . LEU A 1 107 ? -0.970  63.768  25.576  1.000 45.614  ? 425 LEU EEE CA  1 
ATOM   733   C C   . LEU A 1 107 ? -1.176  65.062  26.349  1.000 44.985  ? 425 LEU EEE C   1 
ATOM   734   O O   . LEU A 1 107 ? -0.708  66.114  25.929  1.000 41.211  ? 425 LEU EEE O   1 
ATOM   735   C CB  . LEU A 1 107 ? 0.347   63.098  25.958  1.000 47.117  ? 425 LEU EEE CB  1 
ATOM   736   C CG  . LEU A 1 107 ? 0.547   61.686  25.414  1.000 51.060  ? 425 LEU EEE CG  1 
ATOM   737   C CD1 . LEU A 1 107 ? 1.938   61.148  25.728  1.000 51.759  ? 425 LEU EEE CD1 1 
ATOM   738   C CD2 . LEU A 1 107 ? -0.503  60.753  25.982  1.000 55.957  ? 425 LEU EEE CD2 1 
ATOM   739   N N   . PRO A 1 108 ? -1.876  65.014  27.501  1.000 49.120  ? 426 PRO EEE N   1 
ATOM   740   C CA  . PRO A 1 108 ? -2.104  66.200  28.327  1.000 52.114  ? 426 PRO EEE CA  1 
ATOM   741   C C   . PRO A 1 108 ? -0.843  66.675  29.058  1.000 54.910  ? 426 PRO EEE C   1 
ATOM   742   O O   . PRO A 1 108 ? 0.065   65.889  29.242  1.000 61.448  ? 426 PRO EEE O   1 
ATOM   743   C CB  . PRO A 1 108 ? -3.137  65.735  29.368  1.000 52.422  ? 426 PRO EEE CB  1 
ATOM   744   C CG  . PRO A 1 108 ? -2.931  64.236  29.463  1.000 52.492  ? 426 PRO EEE CG  1 
ATOM   745   C CD  . PRO A 1 108 ? -2.469  63.800  28.084  1.000 51.052  ? 426 PRO EEE CD  1 
ATOM   746   N N   . ASP A 1 109 ? -0.842  67.925  29.505  1.000 56.448  ? 427 ASP EEE N   1 
ATOM   747   C CA  . ASP A 1 109 ? 0.314   68.518  30.221  1.000 66.978  ? 427 ASP EEE CA  1 
ATOM   748   C C   . ASP A 1 109 ? 0.563   67.750  31.522  1.000 73.290  ? 427 ASP EEE C   1 
ATOM   749   O O   . ASP A 1 109 ? 1.750   67.564  31.859  1.000 84.594  ? 427 ASP EEE O   1 
ATOM   750   C CB  . ASP A 1 109 ? 0.125   70.014  30.457  1.000 72.498  ? 427 ASP EEE CB  1 
ATOM   751   C CG  . ASP A 1 109 ? 0.189   70.813  29.163  1.000 78.292  ? 427 ASP EEE CG  1 
ATOM   752   O OD1 . ASP A 1 109 ? -0.412  71.908  29.126  1.000 81.569  ? 427 ASP EEE OD1 1 
ATOM   753   O OD2 . ASP A 1 109 ? 0.823   70.327  28.186  1.000 73.134  ? 427 ASP EEE OD2 1 
ATOM   754   N N   . ASP A 1 110 ? -0.484  67.293  32.215  1.000 75.253  ? 428 ASP EEE N   1 
ATOM   755   C CA  . ASP A 1 110 ? -0.357  66.631  33.544  1.000 80.303  ? 428 ASP EEE CA  1 
ATOM   756   C C   . ASP A 1 110 ? -0.419  65.103  33.377  1.000 69.083  ? 428 ASP EEE C   1 
ATOM   757   O O   . ASP A 1 110 ? -0.901  64.424  34.295  1.000 67.791  ? 428 ASP EEE O   1 
ATOM   758   C CB  . ASP A 1 110 ? -1.404  67.185  34.518  1.000 90.954  ? 428 ASP EEE CB  1 
ATOM   759   C CG  . ASP A 1 110 ? -2.857  66.913  34.138  1.000 96.044  ? 428 ASP EEE CG  1 
ATOM   760   O OD1 . ASP A 1 110 ? -3.152  66.809  32.918  1.000 92.456  ? 428 ASP EEE OD1 1 
ATOM   761   O OD2 . ASP A 1 110 ? -3.689  66.810  35.072  1.000 104.449 ? 428 ASP EEE OD2 1 
ATOM   762   N N   . PHE A 1 111 ? 0.070   64.586  32.249  1.000 57.364  ? 429 PHE EEE N   1 
ATOM   763   C CA  . PHE A 1 111 ? 0.044   63.147  31.898  1.000 52.881  ? 429 PHE EEE CA  1 
ATOM   764   C C   . PHE A 1 111 ? 0.727   62.324  32.997  1.000 51.081  ? 429 PHE EEE C   1 
ATOM   765   O O   . PHE A 1 111 ? 1.812   62.721  33.482  1.000 48.416  ? 429 PHE EEE O   1 
ATOM   766   C CB  . PHE A 1 111 ? 0.735   62.925  30.552  1.000 49.878  ? 429 PHE EEE CB  1 
ATOM   767   C CG  . PHE A 1 111 ? 0.943   61.479  30.176  1.000 48.666  ? 429 PHE EEE CG  1 
ATOM   768   C CD1 . PHE A 1 111 ? -0.129  60.614  30.051  1.000 47.782  ? 429 PHE EEE CD1 1 
ATOM   769   C CD2 . PHE A 1 111 ? 2.209   60.985  29.915  1.000 50.075  ? 429 PHE EEE CD2 1 
ATOM   770   C CE1 . PHE A 1 111 ? 0.060   59.292  29.679  1.000 49.222  ? 429 PHE EEE CE1 1 
ATOM   771   C CE2 . PHE A 1 111 ? 2.395   59.662  29.540  1.000 50.828  ? 429 PHE EEE CE2 1 
ATOM   772   C CZ  . PHE A 1 111 ? 1.321   58.817  29.417  1.000 49.600  ? 429 PHE EEE CZ  1 
ATOM   773   N N   . THR A 1 112 ? 0.114   61.198  33.369  1.000 50.242  ? 430 THR EEE N   1 
ATOM   774   C CA  . THR A 1 112 ? 0.725   60.182  34.263  1.000 53.264  ? 430 THR EEE CA  1 
ATOM   775   C C   . THR A 1 112 ? 0.733   58.816  33.568  1.000 50.527  ? 430 THR EEE C   1 
ATOM   776   O O   . THR A 1 112 ? -0.317  58.142  33.526  1.000 54.414  ? 430 THR EEE O   1 
ATOM   777   C CB  . THR A 1 112 ? 0.062   60.130  35.646  1.000 55.065  ? 430 THR EEE CB  1 
ATOM   778   O OG1 . THR A 1 112 ? -1.056  59.235  35.623  1.000 63.637  ? 430 THR EEE OG1 1 
ATOM   779   C CG2 . THR A 1 112 ? -0.336  61.506  36.130  1.000 54.809  ? 430 THR EEE CG2 1 
ATOM   780   N N   . GLY A 1 113 ? 1.901   58.416  33.070  1.000 48.841  ? 431 GLY EEE N   1 
ATOM   781   C CA  . GLY A 1 113 ? 2.108   57.082  32.493  1.000 49.152  ? 431 GLY EEE CA  1 
ATOM   782   C C   . GLY A 1 113 ? 3.397   56.979  31.705  1.000 47.540  ? 431 GLY EEE C   1 
ATOM   783   O O   . GLY A 1 113 ? 4.245   57.883  31.795  1.000 46.527  ? 431 GLY EEE O   1 
ATOM   784   N N   . CYS A 1 114 ? 3.499   55.905  30.929  1.000 47.946  ? 432 CYS EEE N   1 
ATOM   785   C CA  . CYS A 1 114 ? 4.744   55.385  30.342  1.000 49.749  ? 432 CYS EEE CA  1 
ATOM   786   C C   . CYS A 1 114 ? 4.596   55.367  28.828  1.000 47.341  ? 432 CYS EEE C   1 
ATOM   787   O O   . CYS A 1 114 ? 3.585   54.840  28.352  1.000 49.914  ? 432 CYS EEE O   1 
ATOM   788   C CB  . CYS A 1 114 ? 5.016   54.005  30.927  1.000 54.899  ? 432 CYS EEE CB  1 
ATOM   789   S SG  . CYS A 1 114 ? 5.477   54.108  32.679  1.000 68.480  ? 432 CYS EEE SG  1 
ATOM   790   N N   . VAL A 1 115 ? 5.556   55.961  28.127  1.000 45.082  ? 433 VAL EEE N   1 
ATOM   791   C CA  . VAL A 1 115 ? 5.624   55.968  26.643  1.000 45.886  ? 433 VAL EEE CA  1 
ATOM   792   C C   . VAL A 1 115 ? 6.723   54.993  26.222  1.000 47.719  ? 433 VAL EEE C   1 
ATOM   793   O O   . VAL A 1 115 ? 7.909   55.358  26.315  1.000 53.877  ? 433 VAL EEE O   1 
ATOM   794   C CB  . VAL A 1 115 ? 5.892   57.391  26.136  1.000 45.939  ? 433 VAL EEE CB  1 
ATOM   795   C CG1 . VAL A 1 115 ? 6.115   57.433  24.635  1.000 50.172  ? 433 VAL EEE CG1 1 
ATOM   796   C CG2 . VAL A 1 115 ? 4.778   58.326  26.544  1.000 44.633  ? 433 VAL EEE CG2 1 
ATOM   797   N N   . ILE A 1 116 ? 6.334   53.801  25.785  1.000 45.097  ? 434 ILE EEE N   1 
ATOM   798   C CA  . ILE A 1 116 ? 7.257   52.680  25.466  1.000 46.015  ? 434 ILE EEE CA  1 
ATOM   799   C C   . ILE A 1 116 ? 7.286   52.483  23.958  1.000 50.199  ? 434 ILE EEE C   1 
ATOM   800   O O   . ILE A 1 116 ? 6.204   52.297  23.388  1.000 58.478  ? 434 ILE EEE O   1 
ATOM   801   C CB  . ILE A 1 116 ? 6.757   51.428  26.193  1.000 47.815  ? 434 ILE EEE CB  1 
ATOM   802   C CG1 . ILE A 1 116 ? 6.661   51.707  27.697  1.000 49.660  ? 434 ILE EEE CG1 1 
ATOM   803   C CG2 . ILE A 1 116 ? 7.628   50.225  25.859  1.000 51.223  ? 434 ILE EEE CG2 1 
ATOM   804   C CD1 . ILE A 1 116 ? 5.914   50.662  28.475  1.000 52.447  ? 434 ILE EEE CD1 1 
ATOM   805   N N   . ALA A 1 117 ? 8.469   52.494  23.347  1.000 55.553  ? 435 ALA EEE N   1 
ATOM   806   C CA  . ALA A 1 117 ? 8.641   52.374  21.879  1.000 63.604  ? 435 ALA EEE CA  1 
ATOM   807   C C   . ALA A 1 117 ? 9.783   51.409  21.550  1.000 68.555  ? 435 ALA EEE C   1 
ATOM   808   O O   . ALA A 1 117 ? 10.666  51.251  22.399  1.000 82.110  ? 435 ALA EEE O   1 
ATOM   809   C CB  . ALA A 1 117 ? 8.880   53.742  21.278  1.000 61.730  ? 435 ALA EEE CB  1 
ATOM   810   N N   . TRP A 1 118 ? 9.764   50.815  20.352  1.000 72.465  ? 436 TRP EEE N   1 
ATOM   811   C CA  . TRP A 1 118 ? 10.869  49.973  19.829  1.000 77.476  ? 436 TRP EEE CA  1 
ATOM   812   C C   . TRP A 1 118 ? 10.877  49.916  18.304  1.000 86.183  ? 436 TRP EEE C   1 
ATOM   813   O O   . TRP A 1 118 ? 9.797   49.917  17.711  1.000 89.264  ? 436 TRP EEE O   1 
ATOM   814   C CB  . TRP A 1 118 ? 10.793  48.574  20.422  1.000 77.795  ? 436 TRP EEE CB  1 
ATOM   815   C CG  . TRP A 1 118 ? 9.614   47.736  20.041  1.000 80.068  ? 436 TRP EEE CG  1 
ATOM   816   C CD1 . TRP A 1 118 ? 9.586   46.738  19.110  1.000 83.113  ? 436 TRP EEE CD1 1 
ATOM   817   C CD2 . TRP A 1 118 ? 8.333   47.707  20.695  1.000 83.873  ? 436 TRP EEE CD2 1 
ATOM   818   N NE1 . TRP A 1 118 ? 8.369   46.110  19.118  1.000 82.784  ? 436 TRP EEE NE1 1 
ATOM   819   C CE2 . TRP A 1 118 ? 7.578   46.683  20.078  1.000 80.374  ? 436 TRP EEE CE2 1 
ATOM   820   C CE3 . TRP A 1 118 ? 7.736   48.468  21.707  1.000 84.461  ? 436 TRP EEE CE3 1 
ATOM   821   C CZ2 . TRP A 1 118 ? 6.266   46.396  20.451  1.000 74.469  ? 436 TRP EEE CZ2 1 
ATOM   822   C CZ3 . TRP A 1 118 ? 6.437   48.185  22.068  1.000 79.456  ? 436 TRP EEE CZ3 1 
ATOM   823   C CH2 . TRP A 1 118 ? 5.718   47.162  21.452  1.000 73.922  ? 436 TRP EEE CH2 1 
ATOM   824   N N   . ASN A 1 119 ? 12.076  49.839  17.718  1.000 97.100  ? 437 ASN EEE N   1 
ATOM   825   C CA  . ASN A 1 119 ? 12.294  49.688  16.256  1.000 100.616 ? 437 ASN EEE CA  1 
ATOM   826   C C   . ASN A 1 119 ? 11.618  48.382  15.824  1.000 100.470 ? 437 ASN EEE C   1 
ATOM   827   O O   . ASN A 1 119 ? 11.860  47.348  16.465  1.000 83.320  ? 437 ASN EEE O   1 
ATOM   828   C CB  . ASN A 1 119 ? 13.782  49.782  15.903  1.000 105.255 ? 437 ASN EEE CB  1 
ATOM   829   C CG  . ASN A 1 119 ? 14.050  49.823  14.411  1.000 109.908 ? 437 ASN EEE CG  1 
ATOM   830   O OD1 . ASN A 1 119 ? 13.822  48.836  13.719  1.000 119.163 ? 437 ASN EEE OD1 1 
ATOM   831   N ND2 . ASN A 1 119 ? 14.576  50.935  13.910  1.000 100.092 ? 437 ASN EEE ND2 1 
ATOM   832   N N   . SER A 1 120 ? 10.748  48.462  14.815  1.000 116.625 ? 438 SER EEE N   1 
ATOM   833   C CA  . SER A 1 120 ? 9.955   47.334  14.262  1.000 125.209 ? 438 SER EEE CA  1 
ATOM   834   C C   . SER A 1 120 ? 10.190  47.256  12.750  1.000 128.628 ? 438 SER EEE C   1 
ATOM   835   O O   . SER A 1 120 ? 9.219   46.994  12.021  1.000 137.490 ? 438 SER EEE O   1 
ATOM   836   C CB  . SER A 1 120 ? 8.491   47.517  14.583  1.000 129.343 ? 438 SER EEE CB  1 
ATOM   837   O OG  . SER A 1 120 ? 8.029   48.765  14.075  1.000 135.918 ? 438 SER EEE OG  1 
ATOM   838   N N   . ASN A 1 121 ? 11.431  47.494  12.311  1.000 127.808 ? 439 ASN EEE N   1 
ATOM   839   C CA  . ASN A 1 121 ? 11.824  47.533  10.875  1.000 116.593 ? 439 ASN EEE CA  1 
ATOM   840   C C   . ASN A 1 121 ? 11.708  46.121  10.292  1.000 110.628 ? 439 ASN EEE C   1 
ATOM   841   O O   . ASN A 1 121 ? 11.408  45.998  9.089   1.000 109.338 ? 439 ASN EEE O   1 
ATOM   842   C CB  . ASN A 1 121 ? 13.233  48.101  10.687  1.000 107.208 ? 439 ASN EEE CB  1 
ATOM   843   C CG  . ASN A 1 121 ? 13.480  48.615  9.285   1.000 107.292 ? 439 ASN EEE CG  1 
ATOM   844   O OD1 . ASN A 1 121 ? 12.572  49.093  8.611   1.000 108.708 ? 439 ASN EEE OD1 1 
ATOM   845   N ND2 . ASN A 1 121 ? 14.718  48.540  8.839   1.000 113.195 ? 439 ASN EEE ND2 1 
ATOM   846   N N   . ASN A 1 122 ? 11.911  45.101  11.130  1.000 107.345 ? 440 ASN EEE N   1 
ATOM   847   C CA  . ASN A 1 122 ? 11.814  43.665  10.749  1.000 109.007 ? 440 ASN EEE CA  1 
ATOM   848   C C   . ASN A 1 122 ? 10.342  43.288  10.504  1.000 114.453 ? 440 ASN EEE C   1 
ATOM   849   O O   . ASN A 1 122 ? 10.115  42.360  9.713   1.000 128.183 ? 440 ASN EEE O   1 
ATOM   850   C CB  . ASN A 1 122 ? 12.504  42.747  11.773  1.000 101.102 ? 440 ASN EEE CB  1 
ATOM   851   C CG  . ASN A 1 122 ? 12.020  42.947  13.194  1.000 100.008 ? 440 ASN EEE CG  1 
ATOM   852   O OD1 . ASN A 1 122 ? 11.922  44.075  13.673  1.000 108.722 ? 440 ASN EEE OD1 1 
ATOM   853   N ND2 . ASN A 1 122 ? 11.697  41.862  13.872  1.000 93.121  ? 440 ASN EEE ND2 1 
ATOM   854   N N   . LEU A 1 123 ? 9.374   43.981  11.123  1.000 109.776 ? 441 LEU EEE N   1 
ATOM   855   C CA  . LEU A 1 123 ? 7.933   43.594  11.079  1.000 92.775  ? 441 LEU EEE CA  1 
ATOM   856   C C   . LEU A 1 123 ? 7.140   44.490  10.125  1.000 82.108  ? 441 LEU EEE C   1 
ATOM   857   O O   . LEU A 1 123 ? 6.265   43.952  9.449   1.000 86.582  ? 441 LEU EEE O   1 
ATOM   858   C CB  . LEU A 1 123 ? 7.342   43.656  12.491  1.000 91.654  ? 441 LEU EEE CB  1 
ATOM   859   C CG  . LEU A 1 123 ? 7.882   42.623  13.481  1.000 90.509  ? 441 LEU EEE CG  1 
ATOM   860   C CD1 . LEU A 1 123 ? 7.005   42.566  14.729  1.000 90.303  ? 441 LEU EEE CD1 1 
ATOM   861   C CD2 . LEU A 1 123 ? 7.983   41.245  12.849  1.000 85.289  ? 441 LEU EEE CD2 1 
ATOM   862   N N   . ASP A 1 124 ? 7.435   45.787  10.066  1.000 82.780  ? 442 ASP EEE N   1 
ATOM   863   C CA  . ASP A 1 124 ? 6.560   46.803  9.425   1.000 95.892  ? 442 ASP EEE CA  1 
ATOM   864   C C   . ASP A 1 124 ? 7.259   47.447  8.214   1.000 100.809 ? 442 ASP EEE C   1 
ATOM   865   O O   . ASP A 1 124 ? 6.883   48.595  7.869   1.000 96.840  ? 442 ASP EEE O   1 
ATOM   866   C CB  . ASP A 1 124 ? 6.120   47.847  10.459  1.000 103.003 ? 442 ASP EEE CB  1 
ATOM   867   C CG  . ASP A 1 124 ? 5.291   47.274  11.605  1.000 97.781  ? 442 ASP EEE CG  1 
ATOM   868   O OD1 . ASP A 1 124 ? 4.581   46.280  11.378  1.000 82.503  ? 442 ASP EEE OD1 1 
ATOM   869   O OD2 . ASP A 1 124 ? 5.357   47.833  12.718  1.000 100.922 ? 442 ASP EEE OD2 1 
ATOM   870   N N   . SER A 1 125 ? 8.207   46.750  7.571   1.000 107.604 ? 443 SER EEE N   1 
ATOM   871   C CA  . SER A 1 125 ? 8.836   47.179  6.288   1.000 117.272 ? 443 SER EEE CA  1 
ATOM   872   C C   . SER A 1 125 ? 8.627   46.115  5.207   1.000 129.487 ? 443 SER EEE C   1 
ATOM   873   O O   . SER A 1 125 ? 8.470   44.931  5.554   1.000 127.244 ? 443 SER EEE O   1 
ATOM   874   C CB  . SER A 1 125 ? 10.294  47.495  6.451   1.000 118.157 ? 443 SER EEE CB  1 
ATOM   875   O OG  . SER A 1 125 ? 10.455  48.749  7.088   1.000 128.176 ? 443 SER EEE OG  1 
ATOM   876   N N   . LYS A 1 126 ? 8.602   46.545  3.944   1.000 140.558 ? 444 LYS EEE N   1 
ATOM   877   C CA  . LYS A 1 126 ? 8.516   45.665  2.750   1.000 141.975 ? 444 LYS EEE CA  1 
ATOM   878   C C   . LYS A 1 126 ? 9.461   46.216  1.682   1.000 148.910 ? 444 LYS EEE C   1 
ATOM   879   O O   . LYS A 1 126 ? 9.737   47.440  1.707   1.000 149.374 ? 444 LYS EEE O   1 
ATOM   880   C CB  . LYS A 1 126 ? 7.083   45.589  2.213   1.000 134.014 ? 444 LYS EEE CB  1 
ATOM   881   C CG  . LYS A 1 126 ? 6.110   44.791  3.070   1.000 129.503 ? 444 LYS EEE CG  1 
ATOM   882   C CD  . LYS A 1 126 ? 4.679   44.907  2.614   1.000 130.662 ? 444 LYS EEE CD  1 
ATOM   883   C CE  . LYS A 1 126 ? 3.696   44.538  3.702   1.000 134.276 ? 444 LYS EEE CE  1 
ATOM   884   N NZ  . LYS A 1 126 ? 2.304   44.602  3.208   1.000 140.995 ? 444 LYS EEE NZ  1 
ATOM   885   N N   . VAL A 1 127 ? 9.907   45.335  0.786   1.000 143.354 ? 445 VAL EEE N   1 
ATOM   886   C CA  . VAL A 1 127 ? 10.853  45.619  -0.335  1.000 136.789 ? 445 VAL EEE CA  1 
ATOM   887   C C   . VAL A 1 127 ? 10.466  46.926  -1.060  1.000 138.675 ? 445 VAL EEE C   1 
ATOM   888   O O   . VAL A 1 127 ? 11.317  47.841  -1.101  1.000 134.696 ? 445 VAL EEE O   1 
ATOM   889   C CB  . VAL A 1 127 ? 10.932  44.406  -1.283  1.000 127.777 ? 445 VAL EEE CB  1 
ATOM   890   C CG1 . VAL A 1 127 ? 11.619  43.226  -0.605  1.000 112.440 ? 445 VAL EEE CG1 1 
ATOM   891   C CG2 . VAL A 1 127 ? 9.569   43.994  -1.833  1.000 125.613 ? 445 VAL EEE CG2 1 
ATOM   892   N N   . GLY A 1 128 ? 9.234   47.046  -1.573  1.000 134.687 ? 446 GLY EEE N   1 
ATOM   893   C CA  . GLY A 1 128 ? 8.796   48.193  -2.402  1.000 132.887 ? 446 GLY EEE CA  1 
ATOM   894   C C   . GLY A 1 128 ? 8.249   49.349  -1.572  1.000 138.226 ? 446 GLY EEE C   1 
ATOM   895   O O   . GLY A 1 128 ? 7.779   50.346  -2.167  1.000 127.736 ? 446 GLY EEE O   1 
ATOM   896   N N   . GLY A 1 129 ? 8.319   49.238  -0.243  1.000 152.187 ? 447 GLY EEE N   1 
ATOM   897   C CA  . GLY A 1 129 ? 7.693   50.176  0.709   1.000 154.251 ? 447 GLY EEE CA  1 
ATOM   898   C C   . GLY A 1 129 ? 6.348   49.659  1.199   1.000 153.734 ? 447 GLY EEE C   1 
ATOM   899   O O   . GLY A 1 129 ? 5.488   49.386  0.351   1.000 151.541 ? 447 GLY EEE O   1 
ATOM   900   N N   . ASN A 1 130 ? 6.201   49.488  2.518   1.000 154.200 ? 448 ASN EEE N   1 
ATOM   901   C CA  . ASN A 1 130 ? 4.920   49.259  3.244   1.000 145.455 ? 448 ASN EEE CA  1 
ATOM   902   C C   . ASN A 1 130 ? 4.168   50.591  3.355   1.000 137.013 ? 448 ASN EEE C   1 
ATOM   903   O O   . ASN A 1 130 ? 4.760   51.552  3.870   1.000 134.310 ? 448 ASN EEE O   1 
ATOM   904   C CB  . ASN A 1 130 ? 5.189   48.687  4.639   1.000 147.221 ? 448 ASN EEE CB  1 
ATOM   905   C CG  . ASN A 1 130 ? 3.951   48.229  5.374   1.000 137.901 ? 448 ASN EEE CG  1 
ATOM   906   O OD1 . ASN A 1 130 ? 2.845   48.529  4.970   1.000 144.251 ? 448 ASN EEE OD1 1 
ATOM   907   N ND2 . ASN A 1 130 ? 4.121   47.506  6.464   1.000 122.286 ? 448 ASN EEE ND2 1 
ATOM   908   N N   . TYR A 1 131 ? 2.918   50.660  2.900   1.000 127.609 ? 449 TYR EEE N   1 
ATOM   909   C CA  . TYR A 1 131 ? 2.140   51.930  2.863   1.000 130.289 ? 449 TYR EEE CA  1 
ATOM   910   C C   . TYR A 1 131 ? 0.799   51.732  3.601   1.000 125.253 ? 449 TYR EEE C   1 
ATOM   911   O O   . TYR A 1 131 ? -0.162  52.501  3.351   1.000 118.644 ? 449 TYR EEE O   1 
ATOM   912   C CB  . TYR A 1 131 ? 1.962   52.384  1.408   1.000 129.963 ? 449 TYR EEE CB  1 
ATOM   913   C CG  . TYR A 1 131 ? 3.200   52.870  0.689   1.000 132.103 ? 449 TYR EEE CG  1 
ATOM   914   C CD1 . TYR A 1 131 ? 3.949   52.025  -0.118  1.000 130.385 ? 449 TYR EEE CD1 1 
ATOM   915   C CD2 . TYR A 1 131 ? 3.595   54.198  0.762   1.000 131.066 ? 449 TYR EEE CD2 1 
ATOM   916   C CE1 . TYR A 1 131 ? 5.074   52.473  -0.799  1.000 123.972 ? 449 TYR EEE CE1 1 
ATOM   917   C CE2 . TYR A 1 131 ? 4.714   54.664  0.089   1.000 128.753 ? 449 TYR EEE CE2 1 
ATOM   918   C CZ  . TYR A 1 131 ? 5.458   53.797  -0.691  1.000 125.833 ? 449 TYR EEE CZ  1 
ATOM   919   O OH  . TYR A 1 131 ? 6.558   54.249  -1.354  1.000 129.912 ? 449 TYR EEE OH  1 
ATOM   920   N N   . ASN A 1 132 ? 0.724   50.754  4.509   1.000 117.534 ? 450 ASN EEE N   1 
ATOM   921   C CA  . ASN A 1 132 ? -0.483  50.453  5.329   1.000 104.849 ? 450 ASN EEE CA  1 
ATOM   922   C C   . ASN A 1 132 ? -0.593  51.440  6.497   1.000 107.430 ? 450 ASN EEE C   1 
ATOM   923   O O   . ASN A 1 132 ? -1.720  51.669  6.961   1.000 118.749 ? 450 ASN EEE O   1 
ATOM   924   C CB  . ASN A 1 132 ? -0.454  49.019  5.855   1.000 97.365  ? 450 ASN EEE CB  1 
ATOM   925   C CG  . ASN A 1 132 ? -0.402  48.024  4.723   1.000 101.986 ? 450 ASN EEE CG  1 
ATOM   926   O OD1 . ASN A 1 132 ? -1.416  47.439  4.392   1.000 117.135 ? 450 ASN EEE OD1 1 
ATOM   927   N ND2 . ASN A 1 132 ? 0.753   47.836  4.108   1.000 104.534 ? 450 ASN EEE ND2 1 
ATOM   928   N N   . TYR A 1 133 ? 0.539   51.954  6.986   1.000 106.333 ? 451 TYR EEE N   1 
ATOM   929   C CA  . TYR A 1 133 ? 0.610   52.860  8.161   1.000 98.420  ? 451 TYR EEE CA  1 
ATOM   930   C C   . TYR A 1 133 ? 0.468   54.298  7.658   1.000 91.706  ? 451 TYR EEE C   1 
ATOM   931   O O   . TYR A 1 133 ? 1.266   54.675  6.781   1.000 89.542  ? 451 TYR EEE O   1 
ATOM   932   C CB  . TYR A 1 133 ? 1.898   52.593  8.938   1.000 92.271  ? 451 TYR EEE CB  1 
ATOM   933   C CG  . TYR A 1 133 ? 1.928   51.231  9.585   1.000 86.569  ? 451 TYR EEE CG  1 
ATOM   934   C CD1 . TYR A 1 133 ? 1.170   50.980  10.716  1.000 85.852  ? 451 TYR EEE CD1 1 
ATOM   935   C CD2 . TYR A 1 133 ? 2.682   50.190  9.063   1.000 80.989  ? 451 TYR EEE CD2 1 
ATOM   936   C CE1 . TYR A 1 133 ? 1.176   49.739  11.331  1.000 80.804  ? 451 TYR EEE CE1 1 
ATOM   937   C CE2 . TYR A 1 133 ? 2.707   48.943  9.673   1.000 77.717  ? 451 TYR EEE CE2 1 
ATOM   938   C CZ  . TYR A 1 133 ? 1.946   48.718  10.808  1.000 76.988  ? 451 TYR EEE CZ  1 
ATOM   939   O OH  . TYR A 1 133 ? 1.934   47.508  11.433  1.000 77.351  ? 451 TYR EEE OH  1 
ATOM   940   N N   . LEU A 1 134 ? -0.523  55.041  8.171   1.000 88.146  ? 452 LEU EEE N   1 
ATOM   941   C CA  . LEU A 1 134 ? -0.855  56.435  7.750   1.000 93.408  ? 452 LEU EEE CA  1 
ATOM   942   C C   . LEU A 1 134 ? -0.732  57.403  8.929   1.000 80.622  ? 452 LEU EEE C   1 
ATOM   943   O O   . LEU A 1 134 ? -0.609  56.934  10.086  1.000 75.478  ? 452 LEU EEE O   1 
ATOM   944   C CB  . LEU A 1 134 ? -2.288  56.515  7.209   1.000 108.283 ? 452 LEU EEE CB  1 
ATOM   945   C CG  . LEU A 1 134 ? -2.721  55.435  6.220   1.000 113.481 ? 452 LEU EEE CG  1 
ATOM   946   C CD1 . LEU A 1 134 ? -4.166  55.661  5.811   1.000 114.035 ? 452 LEU EEE CD1 1 
ATOM   947   C CD2 . LEU A 1 134 ? -1.830  55.410  4.992   1.000 120.358 ? 452 LEU EEE CD2 1 
ATOM   948   N N   . TYR A 1 135 ? -0.830  58.699  8.615   1.000 74.816  ? 453 TYR EEE N   1 
ATOM   949   C CA  . TYR A 1 135 ? -0.768  59.841  9.563   1.000 82.765  ? 453 TYR EEE CA  1 
ATOM   950   C C   . TYR A 1 135 ? -1.560  61.020  8.985   1.000 78.026  ? 453 TYR EEE C   1 
ATOM   951   O O   . TYR A 1 135 ? -1.516  61.243  7.769   1.000 78.124  ? 453 TYR EEE O   1 
ATOM   952   C CB  . TYR A 1 135 ? 0.684   60.228  9.882   1.000 90.932  ? 453 TYR EEE CB  1 
ATOM   953   C CG  . TYR A 1 135 ? 1.528   60.789  8.754   1.000 95.785  ? 453 TYR EEE CG  1 
ATOM   954   C CD1 . TYR A 1 135 ? 1.686   62.161  8.584   1.000 93.260  ? 453 TYR EEE CD1 1 
ATOM   955   C CD2 . TYR A 1 135 ? 2.224   59.945  7.892   1.000 95.800  ? 453 TYR EEE CD2 1 
ATOM   956   C CE1 . TYR A 1 135 ? 2.467   62.676  7.561   1.000 95.843  ? 453 TYR EEE CE1 1 
ATOM   957   C CE2 . TYR A 1 135 ? 3.012   60.446  6.869   1.000 93.691  ? 453 TYR EEE CE2 1 
ATOM   958   C CZ  . TYR A 1 135 ? 3.136   61.815  6.704   1.000 96.058  ? 453 TYR EEE CZ  1 
ATOM   959   O OH  . TYR A 1 135 ? 3.914   62.304  5.695   1.000 95.675  ? 453 TYR EEE OH  1 
ATOM   960   N N   . ARG A 1 136 ? -2.289  61.733  9.838   1.000 78.162  ? 454 ARG EEE N   1 
ATOM   961   C CA  . ARG A 1 136 ? -3.064  62.933  9.442   1.000 89.168  ? 454 ARG EEE CA  1 
ATOM   962   C C   . ARG A 1 136 ? -2.059  64.052  9.163   1.000 87.698  ? 454 ARG EEE C   1 
ATOM   963   O O   . ARG A 1 136 ? -1.298  64.388  10.079  1.000 89.297  ? 454 ARG EEE O   1 
ATOM   964   C CB  . ARG A 1 136 ? -4.073  63.300  10.536  1.000 104.249 ? 454 ARG EEE CB  1 
ATOM   965   C CG  . ARG A 1 136 ? -4.962  64.502  10.226  1.000 115.353 ? 454 ARG EEE CG  1 
ATOM   966   C CD  . ARG A 1 136 ? -6.127  64.608  11.207  1.000 112.010 ? 454 ARG EEE CD  1 
ATOM   967   N NE  . ARG A 1 136 ? -6.863  63.349  11.233  1.000 110.371 ? 454 ARG EEE NE  1 
ATOM   968   C CZ  . ARG A 1 136 ? -7.784  63.002  10.337  1.000 101.441 ? 454 ARG EEE CZ  1 
ATOM   969   N NH1 . ARG A 1 136 ? -8.100  63.821  9.350   1.000 104.982 ? 454 ARG EEE NH1 1 
ATOM   970   N NH2 . ARG A 1 136 ? -8.387  61.832  10.422  1.000 96.201  ? 454 ARG EEE NH2 1 
ATOM   971   N N   . LEU A 1 137 ? -2.057  64.583  7.939   1.000 85.557  ? 455 LEU EEE N   1 
ATOM   972   C CA  . LEU A 1 137 ? -1.130  65.651  7.506   1.000 89.917  ? 455 LEU EEE CA  1 
ATOM   973   C C   . LEU A 1 137 ? -1.740  67.029  7.791   1.000 91.851  ? 455 LEU EEE C   1 
ATOM   974   O O   . LEU A 1 137 ? -0.955  67.942  8.161   1.000 89.894  ? 455 LEU EEE O   1 
ATOM   975   C CB  . LEU A 1 137 ? -0.828  65.474  6.018   1.000 94.254  ? 455 LEU EEE CB  1 
ATOM   976   C CG  . LEU A 1 137 ? 0.199   66.455  5.456   1.000 100.482 ? 455 LEU EEE CG  1 
ATOM   977   C CD1 . LEU A 1 137 ? 1.511   66.393  6.231   1.000 99.981  ? 455 LEU EEE CD1 1 
ATOM   978   C CD2 . LEU A 1 137 ? 0.433   66.194  3.970   1.000 102.757 ? 455 LEU EEE CD2 1 
ATOM   979   N N   . PHE A 1 138 ? -3.063  67.180  7.616   1.000 90.989  ? 456 PHE EEE N   1 
ATOM   980   C CA  . PHE A 1 138 ? -3.782  68.474  7.794   1.000 92.325  ? 456 PHE EEE CA  1 
ATOM   981   C C   . PHE A 1 138 ? -5.009  68.338  8.706   1.000 78.937  ? 456 PHE EEE C   1 
ATOM   982   O O   . PHE A 1 138 ? -5.703  67.292  8.706   1.000 63.554  ? 456 PHE EEE O   1 
ATOM   983   C CB  . PHE A 1 138 ? -4.216  69.058  6.451   1.000 105.154 ? 456 PHE EEE CB  1 
ATOM   984   C CG  . PHE A 1 138 ? -3.109  69.167  5.441   1.000 108.641 ? 456 PHE EEE CG  1 
ATOM   985   C CD1 . PHE A 1 138 ? -2.133  70.144  5.566   1.000 101.735 ? 456 PHE EEE CD1 1 
ATOM   986   C CD2 . PHE A 1 138 ? -3.035  68.275  4.381   1.000 110.569 ? 456 PHE EEE CD2 1 
ATOM   987   C CE1 . PHE A 1 138 ? -1.101  70.223  4.644   1.000 104.557 ? 456 PHE EEE CE1 1 
ATOM   988   C CE2 . PHE A 1 138 ? -2.012  68.364  3.452   1.000 104.852 ? 456 PHE EEE CE2 1 
ATOM   989   C CZ  . PHE A 1 138 ? -1.042  69.333  3.591   1.000 109.546 ? 456 PHE EEE CZ  1 
ATOM   990   N N   . ARG A 1 139 ? -5.285  69.420  9.437   1.000 71.509  ? 457 ARG EEE N   1 
ATOM   991   C CA  . ARG A 1 139 ? -6.443  69.553  10.352  1.000 75.606  ? 457 ARG EEE CA  1 
ATOM   992   C C   . ARG A 1 139 ? -6.602  71.024  10.758  1.000 77.237  ? 457 ARG EEE C   1 
ATOM   993   O O   . ARG A 1 139 ? -5.574  71.701  10.965  1.000 83.977  ? 457 ARG EEE O   1 
ATOM   994   C CB  . ARG A 1 139 ? -6.238  68.681  11.592  1.000 79.193  ? 457 ARG EEE CB  1 
ATOM   995   C CG  . ARG A 1 139 ? -7.537  68.377  12.317  1.000 80.611  ? 457 ARG EEE CG  1 
ATOM   996   C CD  . ARG A 1 139 ? -7.330  67.377  13.427  1.000 76.990  ? 457 ARG EEE CD  1 
ATOM   997   N NE  . ARG A 1 139 ? -8.567  66.931  14.063  1.000 72.413  ? 457 ARG EEE NE  1 
ATOM   998   C CZ  . ARG A 1 139 ? -9.222  67.581  15.031  1.000 66.578  ? 457 ARG EEE CZ  1 
ATOM   999   N NH1 . ARG A 1 139 ? -8.786  68.752  15.490  1.000 65.271  ? 457 ARG EEE NH1 1 
ATOM   1000  N NH2 . ARG A 1 139 ? -10.317 67.037  15.537  1.000 61.276  ? 457 ARG EEE NH2 1 
ATOM   1001  N N   . LYS A 1 140 ? -7.847  71.480  10.876  1.000 81.531  ? 458 LYS EEE N   1 
ATOM   1002  C CA  . LYS A 1 140 ? -8.227  72.909  11.048  1.000 91.347  ? 458 LYS EEE CA  1 
ATOM   1003  C C   . LYS A 1 140 ? -7.757  73.405  12.420  1.000 90.963  ? 458 LYS EEE C   1 
ATOM   1004  O O   . LYS A 1 140 ? -7.317  74.555  12.510  1.000 87.452  ? 458 LYS EEE O   1 
ATOM   1005  C CB  . LYS A 1 140 ? -9.736  73.061  10.809  1.000 100.455 ? 458 LYS EEE CB  1 
ATOM   1006  C CG  . LYS A 1 140 ? -10.140 72.880  9.343   1.000 106.957 ? 458 LYS EEE CG  1 
ATOM   1007  C CD  . LYS A 1 140 ? -11.472 72.195  9.054   1.000 104.092 ? 458 LYS EEE CD  1 
ATOM   1008  C CE  . LYS A 1 140 ? -11.405 71.367  7.784   1.000 100.352 ? 458 LYS EEE CE  1 
ATOM   1009  N NZ  . LYS A 1 140 ? -12.694 70.697  7.509   1.000 99.635  ? 458 LYS EEE NZ  1 
ATOM   1010  N N   . SER A 1 141 ? -7.832  72.558  13.445  1.000 103.515 ? 459 SER EEE N   1 
ATOM   1011  C CA  . SER A 1 141 ? -7.301  72.834  14.808  1.000 101.586 ? 459 SER EEE CA  1 
ATOM   1012  C C   . SER A 1 141 ? -6.562  71.593  15.328  1.000 104.155 ? 459 SER EEE C   1 
ATOM   1013  O O   . SER A 1 141 ? -6.766  70.474  14.771  1.000 76.784  ? 459 SER EEE O   1 
ATOM   1014  C CB  . SER A 1 141 ? -8.396  73.276  15.750  1.000 94.304  ? 459 SER EEE CB  1 
ATOM   1015  O OG  . SER A 1 141 ? -9.382  72.260  15.884  1.000 92.935  ? 459 SER EEE OG  1 
ATOM   1016  N N   . ASN A 1 142 ? -5.724  71.789  16.348  1.000 107.551 ? 460 ASN EEE N   1 
ATOM   1017  C CA  . ASN A 1 142 ? -4.955  70.699  17.005  1.000 103.888 ? 460 ASN EEE CA  1 
ATOM   1018  C C   . ASN A 1 142 ? -5.935  69.813  17.778  1.000 95.554  ? 460 ASN EEE C   1 
ATOM   1019  O O   . ASN A 1 142 ? -6.962  70.343  18.242  1.000 97.676  ? 460 ASN EEE O   1 
ATOM   1020  C CB  . ASN A 1 142 ? -3.856  71.251  17.916  1.000 98.900  ? 460 ASN EEE CB  1 
ATOM   1021  C CG  . ASN A 1 142 ? -2.905  72.162  17.176  1.000 92.333  ? 460 ASN EEE CG  1 
ATOM   1022  O OD1 . ASN A 1 142 ? -2.993  72.300  15.959  1.000 84.032  ? 460 ASN EEE OD1 1 
ATOM   1023  N ND2 . ASN A 1 142 ? -2.013  72.803  17.909  1.000 102.439 ? 460 ASN EEE ND2 1 
ATOM   1024  N N   . LEU A 1 143 ? -5.625  68.521  17.898  1.000 75.006  ? 461 LEU EEE N   1 
ATOM   1025  C CA  . LEU A 1 143 ? -6.375  67.570  18.751  1.000 61.786  ? 461 LEU EEE CA  1 
ATOM   1026  C C   . LEU A 1 143 ? -6.340  68.043  20.206  1.000 59.332  ? 461 LEU EEE C   1 
ATOM   1027  O O   . LEU A 1 143 ? -5.347  68.677  20.622  1.000 53.229  ? 461 LEU EEE O   1 
ATOM   1028  C CB  . LEU A 1 143 ? -5.738  66.189  18.641  1.000 61.986  ? 461 LEU EEE CB  1 
ATOM   1029  C CG  . LEU A 1 143 ? -5.965  65.448  17.327  1.000 69.321  ? 461 LEU EEE CG  1 
ATOM   1030  C CD1 . LEU A 1 143 ? -5.419  64.025  17.400  1.000 72.570  ? 461 LEU EEE CD1 1 
ATOM   1031  C CD2 . LEU A 1 143 ? -7.443  65.427  16.973  1.000 77.980  ? 461 LEU EEE CD2 1 
ATOM   1032  N N   . LYS A 1 144 ? -7.395  67.736  20.956  1.000 58.594  ? 462 LYS EEE N   1 
ATOM   1033  C CA  . LYS A 1 144 ? -7.363  67.766  22.434  1.000 60.447  ? 462 LYS EEE CA  1 
ATOM   1034  C C   . LYS A 1 144 ? -6.669  66.486  22.897  1.000 57.083  ? 462 LYS EEE C   1 
ATOM   1035  O O   . LYS A 1 144 ? -6.564  65.514  22.156  1.000 51.819  ? 462 LYS EEE O   1 
ATOM   1036  C CB  . LYS A 1 144 ? -8.780  67.951  22.988  1.000 69.182  ? 462 LYS EEE CB  1 
ATOM   1037  C CG  . LYS A 1 144 ? -9.461  69.256  22.577  1.000 81.205  ? 462 LYS EEE CG  1 
ATOM   1038  C CD  . LYS A 1 144 ? -10.033 70.076  23.743  1.000 94.537  ? 462 LYS EEE CD  1 
ATOM   1039  C CE  . LYS A 1 144 ? -11.292 69.497  24.364  1.000 105.548 ? 462 LYS EEE CE  1 
ATOM   1040  N NZ  . LYS A 1 144 ? -12.441 69.573  23.430  1.000 111.798 ? 462 LYS EEE NZ  1 
ATOM   1041  N N   . PRO A 1 145 ? -6.113  66.464  24.122  1.000 58.599  ? 463 PRO EEE N   1 
ATOM   1042  C CA  . PRO A 1 145 ? -5.541  65.240  24.681  1.000 58.104  ? 463 PRO EEE CA  1 
ATOM   1043  C C   . PRO A 1 145 ? -6.451  64.012  24.519  1.000 53.315  ? 463 PRO EEE C   1 
ATOM   1044  O O   . PRO A 1 145 ? -7.621  64.087  24.832  1.000 44.852  ? 463 PRO EEE O   1 
ATOM   1045  C CB  . PRO A 1 145 ? -5.430  65.601  26.169  1.000 64.056  ? 463 PRO EEE CB  1 
ATOM   1046  C CG  . PRO A 1 145 ? -5.178  67.102  26.174  1.000 63.822  ? 463 PRO EEE CG  1 
ATOM   1047  C CD  . PRO A 1 145 ? -5.994  67.626  25.018  1.000 60.579  ? 463 PRO EEE CD  1 
ATOM   1048  N N   . PHE A 1 146 ? -5.887  62.913  24.026  1.000 52.451  ? 464 PHE EEE N   1 
ATOM   1049  C CA  . PHE A 1 146 ? -6.582  61.615  23.850  1.000 52.433  ? 464 PHE EEE CA  1 
ATOM   1050  C C   . PHE A 1 146 ? -7.760  61.791  22.905  1.000 54.523  ? 464 PHE EEE C   1 
ATOM   1051  O O   . PHE A 1 146 ? -8.758  61.072  23.074  1.000 61.981  ? 464 PHE EEE O   1 
ATOM   1052  C CB  . PHE A 1 146 ? -7.070  61.073  25.196  1.000 52.161  ? 464 PHE EEE CB  1 
ATOM   1053  C CG  . PHE A 1 146 ? -5.964  60.786  26.176  1.000 50.541  ? 464 PHE EEE CG  1 
ATOM   1054  C CD1 . PHE A 1 146 ? -4.917  59.942  25.824  1.000 47.454  ? 464 PHE EEE CD1 1 
ATOM   1055  C CD2 . PHE A 1 146 ? -5.968  61.368  27.432  1.000 46.818  ? 464 PHE EEE CD2 1 
ATOM   1056  C CE1 . PHE A 1 146 ? -3.895  59.686  26.713  1.000 46.028  ? 464 PHE EEE CE1 1 
ATOM   1057  C CE2 . PHE A 1 146 ? -4.943  61.111  28.321  1.000 45.638  ? 464 PHE EEE CE2 1 
ATOM   1058  C CZ  . PHE A 1 146 ? -3.914  60.272  27.960  1.000 47.395  ? 464 PHE EEE CZ  1 
ATOM   1059  N N   . GLU A 1 147 ? -7.659  62.728  21.963  1.000 59.963  ? 465 GLU EEE N   1 
ATOM   1060  C CA  . GLU A 1 147 ? -8.657  62.862  20.869  1.000 62.272  ? 465 GLU EEE CA  1 
ATOM   1061  C C   . GLU A 1 147 ? -8.201  61.960  19.724  1.000 58.976  ? 465 GLU EEE C   1 
ATOM   1062  O O   . GLU A 1 147 ? -6.977  61.765  19.553  1.000 52.187  ? 465 GLU EEE O   1 
ATOM   1063  C CB  . GLU A 1 147 ? -8.858  64.316  20.438  1.000 66.139  ? 465 GLU EEE CB  1 
ATOM   1064  C CG  . GLU A 1 147 ? -10.031 64.525  19.485  1.000 67.065  ? 465 GLU EEE CG  1 
ATOM   1065  C CD  . GLU A 1 147 ? -10.508 65.967  19.300  1.000 67.869  ? 465 GLU EEE CD  1 
ATOM   1066  O OE1 . GLU A 1 147 ? -9.709  66.914  19.487  1.000 68.277  ? 465 GLU EEE OE1 1 
ATOM   1067  O OE2 . GLU A 1 147 ? -11.695 66.150  18.970  1.000 69.472  ? 465 GLU EEE OE2 1 
ATOM   1068  N N   . ARG A 1 148 ? -9.177  61.430  18.999  1.000 59.693  ? 466 ARG EEE N   1 
ATOM   1069  C CA  . ARG A 1 148 ? -8.984  60.434  17.928  1.000 69.291  ? 466 ARG EEE CA  1 
ATOM   1070  C C   . ARG A 1 148 ? -9.911  60.809  16.776  1.000 78.401  ? 466 ARG EEE C   1 
ATOM   1071  O O   . ARG A 1 148 ? -11.141 60.664  16.917  1.000 89.085  ? 466 ARG EEE O   1 
ATOM   1072  C CB  . ARG A 1 148 ? -9.303  59.050  18.479  1.000 70.439  ? 466 ARG EEE CB  1 
ATOM   1073  C CG  . ARG A 1 148 ? -9.033  57.913  17.514  1.000 69.663  ? 466 ARG EEE CG  1 
ATOM   1074  C CD  . ARG A 1 148 ? -9.626  56.709  18.177  1.000 73.733  ? 466 ARG EEE CD  1 
ATOM   1075  N NE  . ARG A 1 148 ? -9.363  55.545  17.386  1.000 82.132  ? 466 ARG EEE NE  1 
ATOM   1076  C CZ  . ARG A 1 148 ? -10.003 54.396  17.523  1.000 105.551 ? 466 ARG EEE CZ  1 
ATOM   1077  N NH1 . ARG A 1 148 ? -10.957 54.261  18.434  1.000 112.282 ? 466 ARG EEE NH1 1 
ATOM   1078  N NH2 . ARG A 1 148 ? -9.678  53.380  16.740  1.000 120.008 ? 466 ARG EEE NH2 1 
ATOM   1079  N N   . ASP A 1 149 ? -9.326  61.319  15.699  1.000 80.941  ? 467 ASP EEE N   1 
ATOM   1080  C CA  . ASP A 1 149 ? -10.048 61.751  14.483  1.000 74.030  ? 467 ASP EEE CA  1 
ATOM   1081  C C   . ASP A 1 149 ? -9.741  60.726  13.396  1.000 72.303  ? 467 ASP EEE C   1 
ATOM   1082  O O   . ASP A 1 149 ? -8.544  60.575  13.081  1.000 85.063  ? 467 ASP EEE O   1 
ATOM   1083  C CB  . ASP A 1 149 ? -9.596  63.166  14.128  1.000 77.496  ? 467 ASP EEE CB  1 
ATOM   1084  C CG  . ASP A 1 149 ? -10.366 63.820  13.008  1.000 75.189  ? 467 ASP EEE CG  1 
ATOM   1085  O OD1 . ASP A 1 149 ? -11.037 63.080  12.256  1.000 79.955  ? 467 ASP EEE OD1 1 
ATOM   1086  O OD2 . ASP A 1 149 ? -10.273 65.065  12.901  1.000 72.128  ? 467 ASP EEE OD2 1 
ATOM   1087  N N   . ILE A 1 150 ? -10.766 60.044  12.876  1.000 71.545  ? 468 ILE EEE N   1 
ATOM   1088  C CA  . ILE A 1 150 ? -10.651 59.089  11.724  1.000 71.585  ? 468 ILE EEE CA  1 
ATOM   1089  C C   . ILE A 1 150 ? -11.428 59.627  10.509  1.000 67.337  ? 468 ILE EEE C   1 
ATOM   1090  O O   . ILE A 1 150 ? -11.540 58.886  9.511   1.000 58.919  ? 468 ILE EEE O   1 
ATOM   1091  C CB  . ILE A 1 150 ? -11.093 57.662  12.115  1.000 74.737  ? 468 ILE EEE CB  1 
ATOM   1092  C CG1 . ILE A 1 150 ? -12.495 57.628  12.731  1.000 78.691  ? 468 ILE EEE CG1 1 
ATOM   1093  C CG2 . ILE A 1 150 ? -10.064 57.040  13.042  1.000 77.996  ? 468 ILE EEE CG2 1 
ATOM   1094  C CD1 . ILE A 1 150 ? -12.949 56.245  13.181  1.000 75.801  ? 468 ILE EEE CD1 1 
ATOM   1095  N N   . SER A 1 151 ? -11.895 60.880  10.567  1.000 65.503  ? 469 SER EEE N   1 
ATOM   1096  C CA  . SER A 1 151 ? -12.570 61.591  9.447   1.000 74.399  ? 469 SER EEE CA  1 
ATOM   1097  C C   . SER A 1 151 ? -11.638 61.682  8.227   1.000 77.519  ? 469 SER EEE C   1 
ATOM   1098  O O   . SER A 1 151 ? -10.427 61.880  8.419   1.000 82.683  ? 469 SER EEE O   1 
ATOM   1099  C CB  . SER A 1 151 ? -13.078 62.962  9.874   1.000 76.250  ? 469 SER EEE CB  1 
ATOM   1100  O OG  . SER A 1 151 ? -12.083 63.962  9.747   1.000 74.387  ? 469 SER EEE OG  1 
ATOM   1101  N N   . THR A 1 152 ? -12.191 61.531  7.018   1.000 79.856  ? 470 THR EEE N   1 
ATOM   1102  C CA  . THR A 1 152 ? -11.459 61.675  5.732   1.000 77.861  ? 470 THR EEE CA  1 
ATOM   1103  C C   . THR A 1 152 ? -12.009 62.894  4.964   1.000 85.199  ? 470 THR EEE C   1 
ATOM   1104  O O   . THR A 1 152 ? -11.919 62.910  3.715   1.000 82.448  ? 470 THR EEE O   1 
ATOM   1105  C CB  . THR A 1 152 ? -11.477 60.332  4.987   1.000 67.920  ? 470 THR EEE CB  1 
ATOM   1106  O OG1 . THR A 1 152 ? -12.815 59.865  4.888   1.000 64.548  ? 470 THR EEE OG1 1 
ATOM   1107  C CG2 . THR A 1 152 ? -10.703 59.244  5.695   1.000 62.958  ? 470 THR EEE CG2 1 
ATOM   1108  N N   . GLU A 1 153 ? -12.527 63.894  5.691   1.000 98.536  ? 471 GLU EEE N   1 
ATOM   1109  C CA  . GLU A 1 153 ? -12.880 65.240  5.159   1.000 113.359 ? 471 GLU EEE CA  1 
ATOM   1110  C C   . GLU A 1 153 ? -11.728 65.745  4.288   1.000 124.251 ? 471 GLU EEE C   1 
ATOM   1111  O O   . GLU A 1 153 ? -10.587 65.721  4.755   1.000 146.182 ? 471 GLU EEE O   1 
ATOM   1112  C CB  . GLU A 1 153 ? -13.057 66.271  6.281   1.000 121.425 ? 471 GLU EEE CB  1 
ATOM   1113  C CG  . GLU A 1 153 ? -14.135 65.928  7.288   1.000 128.165 ? 471 GLU EEE CG  1 
ATOM   1114  C CD  . GLU A 1 153 ? -15.520 66.375  6.875   1.000 128.948 ? 471 GLU EEE CD  1 
ATOM   1115  O OE1 . GLU A 1 153 ? -16.436 65.530  6.869   1.000 132.948 ? 471 GLU EEE OE1 1 
ATOM   1116  O OE2 . GLU A 1 153 ? -15.677 67.573  6.577   1.000 124.608 ? 471 GLU EEE OE2 1 
ATOM   1117  N N   . ILE A 1 154 ? -12.015 66.243  3.093   1.000 125.878 ? 472 ILE EEE N   1 
ATOM   1118  C CA  . ILE A 1 154 ? -10.997 66.947  2.260   1.000 123.308 ? 472 ILE EEE CA  1 
ATOM   1119  C C   . ILE A 1 154 ? -10.656 68.268  2.965   1.000 118.963 ? 472 ILE EEE C   1 
ATOM   1120  O O   . ILE A 1 154 ? -11.579 68.993  3.349   1.000 104.564 ? 472 ILE EEE O   1 
ATOM   1121  C CB  . ILE A 1 154 ? -11.509 67.144  0.819   1.000 124.910 ? 472 ILE EEE CB  1 
ATOM   1122  C CG1 . ILE A 1 154 ? -11.956 65.822  0.173   1.000 114.765 ? 472 ILE EEE CG1 1 
ATOM   1123  C CG2 . ILE A 1 154 ? -10.480 67.884  -0.030  1.000 135.072 ? 472 ILE EEE CG2 1 
ATOM   1124  C CD1 . ILE A 1 154 ? -10.985 64.660  0.357   1.000 98.820  ? 472 ILE EEE CD1 1 
ATOM   1125  N N   . TYR A 1 155 ? -9.373  68.538  3.187   1.000 124.326 ? 473 TYR EEE N   1 
ATOM   1126  C CA  . TYR A 1 155 ? -8.901  69.743  3.909   1.000 135.204 ? 473 TYR EEE CA  1 
ATOM   1127  C C   . TYR A 1 155 ? -8.968  70.943  2.964   1.000 139.291 ? 473 TYR EEE C   1 
ATOM   1128  O O   . TYR A 1 155 ? -8.378  70.861  1.869   1.000 141.232 ? 473 TYR EEE O   1 
ATOM   1129  C CB  . TYR A 1 155 ? -7.477  69.530  4.420   1.000 133.252 ? 473 TYR EEE CB  1 
ATOM   1130  C CG  . TYR A 1 155 ? -6.914  70.683  5.211   1.000 136.236 ? 473 TYR EEE CG  1 
ATOM   1131  C CD1 . TYR A 1 155 ? -7.298  70.902  6.527   1.000 138.751 ? 473 TYR EEE CD1 1 
ATOM   1132  C CD2 . TYR A 1 155 ? -5.997  71.557  4.646   1.000 128.679 ? 473 TYR EEE CD2 1 
ATOM   1133  C CE1 . TYR A 1 155 ? -6.775  71.950  7.264   1.000 131.986 ? 473 TYR EEE CE1 1 
ATOM   1134  C CE2 . TYR A 1 155 ? -5.461  72.608  5.373   1.000 122.257 ? 473 TYR EEE CE2 1 
ATOM   1135  C CZ  . TYR A 1 155 ? -5.854  72.805  6.687   1.000 117.280 ? 473 TYR EEE CZ  1 
ATOM   1136  O OH  . TYR A 1 155 ? -5.355  73.834  7.425   1.000 99.908  ? 473 TYR EEE OH  1 
ATOM   1137  N N   . GLN A 1 156 ? -9.654  72.010  3.381   1.000 138.393 ? 474 GLN EEE N   1 
ATOM   1138  C CA  . GLN A 1 156 ? -9.722  73.286  2.621   1.000 145.097 ? 474 GLN EEE CA  1 
ATOM   1139  C C   . GLN A 1 156 ? -8.563  74.187  3.063   1.000 148.182 ? 474 GLN EEE C   1 
ATOM   1140  O O   . GLN A 1 156 ? -8.635  74.743  4.182   1.000 130.828 ? 474 GLN EEE O   1 
ATOM   1141  C CB  . GLN A 1 156 ? -11.080 73.954  2.832   1.000 143.393 ? 474 GLN EEE CB  1 
ATOM   1142  C CG  . GLN A 1 156 ? -11.257 75.240  2.037   1.000 140.994 ? 474 GLN EEE CG  1 
ATOM   1143  C CD  . GLN A 1 156 ? -12.582 75.892  2.342   1.000 143.700 ? 474 GLN EEE CD  1 
ATOM   1144  O OE1 . GLN A 1 156 ? -13.558 75.231  2.696   1.000 140.272 ? 474 GLN EEE OE1 1 
ATOM   1145  N NE2 . GLN A 1 156 ? -12.635 77.204  2.199   1.000 149.732 ? 474 GLN EEE NE2 1 
ATOM   1146  N N   . ALA A 1 157 ? -7.538  74.321  2.216   1.000 151.299 ? 475 ALA EEE N   1 
ATOM   1147  C CA  . ALA A 1 157 ? -6.343  75.162  2.465   1.000 137.235 ? 475 ALA EEE CA  1 
ATOM   1148  C C   . ALA A 1 157 ? -6.560  76.578  1.919   1.000 130.875 ? 475 ALA EEE C   1 
ATOM   1149  O O   . ALA A 1 157 ? -5.981  77.502  2.521   1.000 122.791 ? 475 ALA EEE O   1 
ATOM   1150  C CB  . ALA A 1 157 ? -5.113  74.520  1.868   1.000 124.704 ? 475 ALA EEE CB  1 
ATOM   1151  N N   . GLY A 1 158 ? -7.372  76.738  0.857   1.000 130.864 ? 476 GLY EEE N   1 
ATOM   1152  C CA  . GLY A 1 158 ? -7.553  77.995  0.093   1.000 131.061 ? 476 GLY EEE CA  1 
ATOM   1153  C C   . GLY A 1 158 ? -8.892  78.684  0.372   1.000 139.134 ? 476 GLY EEE C   1 
ATOM   1154  O O   . GLY A 1 158 ? -9.738  78.072  1.060   1.000 151.659 ? 476 GLY EEE O   1 
ATOM   1155  N N   . SER A 1 159 ? -9.080  79.910  -0.144  1.000 140.736 ? 477 SER EEE N   1 
ATOM   1156  C CA  . SER A 1 159 ? -10.302 80.753  0.013   1.000 136.227 ? 477 SER EEE CA  1 
ATOM   1157  C C   . SER A 1 159 ? -11.542 79.971  -0.415  1.000 147.109 ? 477 SER EEE C   1 
ATOM   1158  O O   . SER A 1 159 ? -12.507 79.925  0.364   1.000 150.373 ? 477 SER EEE O   1 
ATOM   1159  C CB  . SER A 1 159 ? -10.209 82.021  -0.781  1.000 131.140 ? 477 SER EEE CB  1 
ATOM   1160  O OG  . SER A 1 159 ? -8.962  82.635  -0.545  1.000 135.630 ? 477 SER EEE OG  1 
ATOM   1161  N N   . THR A 1 160 ? -11.516 79.404  -1.620  1.000 155.029 ? 478 THR EEE N   1 
ATOM   1162  C CA  . THR A 1 160 ? -12.672 78.717  -2.255  1.000 151.775 ? 478 THR EEE CA  1 
ATOM   1163  C C   . THR A 1 160 ? -12.887 77.375  -1.550  1.000 152.355 ? 478 THR EEE C   1 
ATOM   1164  O O   . THR A 1 160 ? -11.921 76.670  -1.260  1.000 138.608 ? 478 THR EEE O   1 
ATOM   1165  C CB  . THR A 1 160 ? -12.455 78.609  -3.769  1.000 141.715 ? 478 THR EEE CB  1 
ATOM   1166  O OG1 . THR A 1 160 ? -11.291 77.800  -3.936  1.000 142.342 ? 478 THR EEE OG1 1 
ATOM   1167  C CG2 . THR A 1 160 ? -12.292 79.957  -4.442  1.000 128.493 ? 478 THR EEE CG2 1 
ATOM   1168  N N   . PRO A 1 161 ? -14.140 77.010  -1.181  1.000 151.909 ? 479 PRO EEE N   1 
ATOM   1169  C CA  . PRO A 1 161 ? -14.412 75.722  -0.548  1.000 148.134 ? 479 PRO EEE CA  1 
ATOM   1170  C C   . PRO A 1 161 ? -14.350 74.597  -1.582  1.000 140.151 ? 479 PRO EEE C   1 
ATOM   1171  O O   . PRO A 1 161 ? -14.838 74.801  -2.666  1.000 136.065 ? 479 PRO EEE O   1 
ATOM   1172  C CB  . PRO A 1 161 ? -15.832 75.823  0.036   1.000 140.435 ? 479 PRO EEE CB  1 
ATOM   1173  C CG  . PRO A 1 161 ? -16.292 77.242  -0.261  1.000 138.956 ? 479 PRO EEE CG  1 
ATOM   1174  C CD  . PRO A 1 161 ? -15.364 77.807  -1.320  1.000 141.524 ? 479 PRO EEE CD  1 
ATOM   1175  N N   . CYS A 1 162 ? -13.724 73.472  -1.232  1.000 144.452 ? 480 CYS EEE N   1 
ATOM   1176  C CA  . CYS A 1 162 ? -13.846 72.191  -1.968  1.000 143.349 ? 480 CYS EEE CA  1 
ATOM   1177  C C   . CYS A 1 162 ? -15.205 71.600  -1.617  1.000 137.304 ? 480 CYS EEE C   1 
ATOM   1178  O O   . CYS A 1 162 ? -15.609 71.726  -0.445  1.000 138.318 ? 480 CYS EEE O   1 
ATOM   1179  C CB  . CYS A 1 162 ? -12.769 71.188  -1.580  1.000 151.721 ? 480 CYS EEE CB  1 
ATOM   1180  S SG  . CYS A 1 162 ? -11.428 71.871  -0.575  1.000 182.008 ? 480 CYS EEE SG  1 
ATOM   1181  N N   . ASN A 1 163 ? -15.899 71.031  -2.594  1.000 137.281 ? 481 ASN EEE N   1 
ATOM   1182  C CA  . ASN A 1 163 ? -17.209 70.371  -2.357  1.000 139.839 ? 481 ASN EEE CA  1 
ATOM   1183  C C   . ASN A 1 163 ? -16.935 68.865  -2.385  1.000 136.715 ? 481 ASN EEE C   1 
ATOM   1184  O O   . ASN A 1 163 ? -17.494 68.166  -3.243  1.000 142.904 ? 481 ASN EEE O   1 
ATOM   1185  C CB  . ASN A 1 163 ? -18.293 70.877  -3.316  1.000 130.688 ? 481 ASN EEE CB  1 
ATOM   1186  C CG  . ASN A 1 163 ? -18.642 72.337  -3.095  1.000 121.852 ? 481 ASN EEE CG  1 
ATOM   1187  O OD1 . ASN A 1 163 ? -19.215 72.717  -2.074  1.000 109.879 ? 481 ASN EEE OD1 1 
ATOM   1188  N ND2 . ASN A 1 163 ? -18.307 73.173  -4.060  1.000 120.978 ? 481 ASN EEE ND2 1 
ATOM   1189  N N   . GLY A 1 164 ? -16.073 68.407  -1.472  1.000 128.400 ? 482 GLY EEE N   1 
ATOM   1190  C CA  . GLY A 1 164 ? -15.552 67.027  -1.430  1.000 117.171 ? 482 GLY EEE CA  1 
ATOM   1191  C C   . GLY A 1 164 ? -14.683 66.728  -2.640  1.000 116.901 ? 482 GLY EEE C   1 
ATOM   1192  O O   . GLY A 1 164 ? -14.490 65.547  -2.962  1.000 105.464 ? 482 GLY EEE O   1 
ATOM   1193  N N   . VAL A 1 165 ? -14.169 67.772  -3.288  1.000 125.659 ? 483 VAL EEE N   1 
ATOM   1194  C CA  . VAL A 1 165 ? -13.448 67.718  -4.594  1.000 136.427 ? 483 VAL EEE CA  1 
ATOM   1195  C C   . VAL A 1 165 ? -11.960 67.990  -4.320  1.000 144.862 ? 483 VAL EEE C   1 
ATOM   1196  O O   . VAL A 1 165 ? -11.667 68.988  -3.640  1.000 137.451 ? 483 VAL EEE O   1 
ATOM   1197  C CB  . VAL A 1 165 ? -14.097 68.725  -5.571  1.000 134.458 ? 483 VAL EEE CB  1 
ATOM   1198  C CG1 . VAL A 1 165 ? -13.201 69.914  -5.921  1.000 133.458 ? 483 VAL EEE CG1 1 
ATOM   1199  C CG2 . VAL A 1 165 ? -14.607 68.031  -6.827  1.000 123.941 ? 483 VAL EEE CG2 1 
ATOM   1200  N N   . GLU A 1 166 ? -11.055 67.117  -4.781  1.000 143.359 ? 484 GLU EEE N   1 
ATOM   1201  C CA  . GLU A 1 166 ? -9.602  67.182  -4.438  1.000 144.039 ? 484 GLU EEE CA  1 
ATOM   1202  C C   . GLU A 1 166 ? -8.821  67.886  -5.561  1.000 144.742 ? 484 GLU EEE C   1 
ATOM   1203  O O   . GLU A 1 166 ? -9.051  67.544  -6.736  1.000 136.428 ? 484 GLU EEE O   1 
ATOM   1204  C CB  . GLU A 1 166 ? -9.051  65.779  -4.162  1.000 137.208 ? 484 GLU EEE CB  1 
ATOM   1205  C CG  . GLU A 1 166 ? -7.653  65.814  -3.570  1.000 141.627 ? 484 GLU EEE CG  1 
ATOM   1206  C CD  . GLU A 1 166 ? -7.021  64.472  -3.244  1.000 142.452 ? 484 GLU EEE CD  1 
ATOM   1207  O OE1 . GLU A 1 166 ? -5.966  64.474  -2.562  1.000 139.147 ? 484 GLU EEE OE1 1 
ATOM   1208  O OE2 . GLU A 1 166 ? -7.585  63.431  -3.643  1.000 134.952 ? 484 GLU EEE OE2 1 
ATOM   1209  N N   . GLY A 1 167 ? -7.897  68.801  -5.224  1.000 147.597 ? 485 GLY EEE N   1 
ATOM   1210  C CA  . GLY A 1 167 ? -6.971  69.447  -6.188  1.000 143.089 ? 485 GLY EEE CA  1 
ATOM   1211  C C   . GLY A 1 167 ? -6.163  70.575  -5.557  1.000 142.469 ? 485 GLY EEE C   1 
ATOM   1212  O O   . GLY A 1 167 ? -5.835  70.467  -4.369  1.000 135.388 ? 485 GLY EEE O   1 
ATOM   1213  N N   . PHE A 1 168 ? -5.846  71.619  -6.332  1.000 147.295 ? 486 PHE EEE N   1 
ATOM   1214  C CA  . PHE A 1 168 ? -5.203  72.882  -5.874  1.000 154.291 ? 486 PHE EEE CA  1 
ATOM   1215  C C   . PHE A 1 168 ? -5.880  73.347  -4.569  1.000 171.399 ? 486 PHE EEE C   1 
ATOM   1216  O O   . PHE A 1 168 ? -7.103  73.542  -4.558  1.000 184.045 ? 486 PHE EEE O   1 
ATOM   1217  C CB  . PHE A 1 168 ? -5.255  73.907  -7.018  1.000 150.896 ? 486 PHE EEE CB  1 
ATOM   1218  C CG  . PHE A 1 168 ? -4.894  75.340  -6.692  1.000 161.073 ? 486 PHE EEE CG  1 
ATOM   1219  C CD1 . PHE A 1 168 ? -3.594  75.703  -6.356  1.000 154.405 ? 486 PHE EEE CD1 1 
ATOM   1220  C CD2 . PHE A 1 168 ? -5.850  76.347  -6.785  1.000 163.334 ? 486 PHE EEE CD2 1 
ATOM   1221  C CE1 . PHE A 1 168 ? -3.272  77.027  -6.082  1.000 151.511 ? 486 PHE EEE CE1 1 
ATOM   1222  C CE2 . PHE A 1 168 ? -5.525  77.670  -6.514  1.000 155.060 ? 486 PHE EEE CE2 1 
ATOM   1223  C CZ  . PHE A 1 168 ? -4.236  78.008  -6.163  1.000 152.722 ? 486 PHE EEE CZ  1 
ATOM   1224  N N   . ASN A 1 169 ? -5.098  73.461  -3.490  1.000 177.120 ? 487 ASN EEE N   1 
ATOM   1225  C CA  . ASN A 1 169 ? -5.495  73.984  -2.148  1.000 171.591 ? 487 ASN EEE CA  1 
ATOM   1226  C C   . ASN A 1 169 ? -6.631  73.149  -1.535  1.000 170.423 ? 487 ASN EEE C   1 
ATOM   1227  O O   . ASN A 1 169 ? -7.379  73.703  -0.692  1.000 153.369 ? 487 ASN EEE O   1 
ATOM   1228  C CB  . ASN A 1 169 ? -5.900  75.469  -2.188  1.000 160.632 ? 487 ASN EEE CB  1 
ATOM   1229  C CG  . ASN A 1 169 ? -4.728  76.411  -2.365  1.000 159.681 ? 487 ASN EEE CG  1 
ATOM   1230  O OD1 . ASN A 1 169 ? -4.859  77.434  -3.031  1.000 159.570 ? 487 ASN EEE OD1 1 
ATOM   1231  N ND2 . ASN A 1 169 ? -3.586  76.070  -1.787  1.000 169.201 ? 487 ASN EEE ND2 1 
ATOM   1232  N N   . CYS A 1 170 ? -6.754  71.868  -1.898  1.000 172.048 ? 488 CYS EEE N   1 
ATOM   1233  C CA  . CYS A 1 170 ? -7.808  70.956  -1.384  1.000 161.966 ? 488 CYS EEE CA  1 
ATOM   1234  C C   . CYS A 1 170 ? -7.290  69.515  -1.322  1.000 146.135 ? 488 CYS EEE C   1 
ATOM   1235  O O   . CYS A 1 170 ? -7.345  68.826  -2.360  1.000 142.861 ? 488 CYS EEE O   1 
ATOM   1236  C CB  . CYS A 1 170 ? -9.037  71.028  -2.278  1.000 171.274 ? 488 CYS EEE CB  1 
ATOM   1237  S SG  . CYS A 1 170 ? -10.082 72.478  -1.968  1.000 190.234 ? 488 CYS EEE SG  1 
ATOM   1238  N N   . TYR A 1 171 ? -6.804  69.068  -0.164  1.000 134.584 ? 489 TYR EEE N   1 
ATOM   1239  C CA  . TYR A 1 171 ? -6.030  67.804  -0.054  1.000 131.933 ? 489 TYR EEE CA  1 
ATOM   1240  C C   . TYR A 1 171 ? -6.798  66.777  0.784   1.000 112.212 ? 489 TYR EEE C   1 
ATOM   1241  O O   . TYR A 1 171 ? -7.489  67.158  1.763   1.000 71.136  ? 489 TYR EEE O   1 
ATOM   1242  C CB  . TYR A 1 171 ? -4.646  68.078  0.543   1.000 148.570 ? 489 TYR EEE CB  1 
ATOM   1243  C CG  . TYR A 1 171 ? -3.900  69.234  -0.085  1.000 154.133 ? 489 TYR EEE CG  1 
ATOM   1244  C CD1 . TYR A 1 171 ? -3.250  69.094  -1.303  1.000 139.127 ? 489 TYR EEE CD1 1 
ATOM   1245  C CD2 . TYR A 1 171 ? -3.823  70.467  0.551   1.000 159.731 ? 489 TYR EEE CD2 1 
ATOM   1246  C CE1 . TYR A 1 171 ? -2.539  70.142  -1.870  1.000 135.347 ? 489 TYR EEE CE1 1 
ATOM   1247  C CE2 . TYR A 1 171 ? -3.138  71.532  -0.011  1.000 147.677 ? 489 TYR EEE CE2 1 
ATOM   1248  C CZ  . TYR A 1 171 ? -2.497  71.369  -1.227  1.000 143.146 ? 489 TYR EEE CZ  1 
ATOM   1249  O OH  . TYR A 1 171 ? -1.824  72.427  -1.762  1.000 135.792 ? 489 TYR EEE OH  1 
ATOM   1250  N N   . PHE A 1 172 ? -6.671  65.507  0.377   1.000 109.314 ? 490 PHE EEE N   1 
ATOM   1251  C CA  . PHE A 1 172 ? -6.989  64.294  1.173   1.000 116.876 ? 490 PHE EEE CA  1 
ATOM   1252  C C   . PHE A 1 172 ? -6.130  64.348  2.427   1.000 127.979 ? 490 PHE EEE C   1 
ATOM   1253  O O   . PHE A 1 172 ? -4.915  64.510  2.329   1.000 145.054 ? 490 PHE EEE O   1 
ATOM   1254  C CB  . PHE A 1 172 ? -6.684  63.029  0.369   1.000 107.184 ? 490 PHE EEE CB  1 
ATOM   1255  C CG  . PHE A 1 172 ? -7.088  61.712  0.989   1.000 102.985 ? 490 PHE EEE CG  1 
ATOM   1256  C CD1 . PHE A 1 172 ? -8.402  61.264  0.962   1.000 101.010 ? 490 PHE EEE CD1 1 
ATOM   1257  C CD2 . PHE A 1 172 ? -6.132  60.877  1.535   1.000 95.209  ? 490 PHE EEE CD2 1 
ATOM   1258  C CE1 . PHE A 1 172 ? -8.748  60.024  1.486   1.000 91.230  ? 490 PHE EEE CE1 1 
ATOM   1259  C CE2 . PHE A 1 172 ? -6.474  59.635  2.054   1.000 90.457  ? 490 PHE EEE CE2 1 
ATOM   1260  C CZ  . PHE A 1 172 ? -7.783  59.212  2.034   1.000 86.537  ? 490 PHE EEE CZ  1 
ATOM   1261  N N   . PRO A 1 173 ? -6.719  64.223  3.634   1.000 126.895 ? 491 PRO EEE N   1 
ATOM   1262  C CA  . PRO A 1 173 ? -6.027  64.628  4.856   1.000 121.513 ? 491 PRO EEE CA  1 
ATOM   1263  C C   . PRO A 1 173 ? -5.002  63.604  5.367   1.000 118.693 ? 491 PRO EEE C   1 
ATOM   1264  O O   . PRO A 1 173 ? -4.235  63.982  6.227   1.000 130.926 ? 491 PRO EEE O   1 
ATOM   1265  C CB  . PRO A 1 173 ? -7.183  64.790  5.844   1.000 118.026 ? 491 PRO EEE CB  1 
ATOM   1266  C CG  . PRO A 1 173 ? -8.146  63.696  5.420   1.000 119.455 ? 491 PRO EEE CG  1 
ATOM   1267  C CD  . PRO A 1 173 ? -8.049  63.654  3.901   1.000 123.367 ? 491 PRO EEE CD  1 
ATOM   1268  N N   . LEU A 1 174 ? -4.997  62.373  4.836   1.000 106.947 ? 492 LEU EEE N   1 
ATOM   1269  C CA  . LEU A 1 174 ? -4.071  61.298  5.286   1.000 108.536 ? 492 LEU EEE CA  1 
ATOM   1270  C C   . LEU A 1 174 ? -2.972  61.068  4.251   1.000 114.638 ? 492 LEU EEE C   1 
ATOM   1271  O O   . LEU A 1 174 ? -3.293  60.852  3.073   1.000 110.729 ? 492 LEU EEE O   1 
ATOM   1272  C CB  . LEU A 1 174 ? -4.845  59.998  5.502   1.000 104.352 ? 492 LEU EEE CB  1 
ATOM   1273  C CG  . LEU A 1 174 ? -5.998  60.081  6.496   1.000 104.083 ? 492 LEU EEE CG  1 
ATOM   1274  C CD1 . LEU A 1 174 ? -6.509  58.688  6.802   1.000 100.349 ? 492 LEU EEE CD1 1 
ATOM   1275  C CD2 . LEU A 1 174 ? -5.591  60.803  7.774   1.000 102.565 ? 492 LEU EEE CD2 1 
ATOM   1276  N N   . GLN A 1 175 ? -1.724  61.091  4.711   1.000 125.182 ? 493 GLN EEE N   1 
ATOM   1277  C CA  . GLN A 1 175 ? -0.514  60.701  3.947   1.000 111.028 ? 493 GLN EEE CA  1 
ATOM   1278  C C   . GLN A 1 175 ? -0.041  59.358  4.485   1.000 101.826 ? 493 GLN EEE C   1 
ATOM   1279  O O   . GLN A 1 175 ? -0.309  59.074  5.662   1.000 104.829 ? 493 GLN EEE O   1 
ATOM   1280  C CB  . GLN A 1 175 ? 0.604   61.739  4.102   1.000 113.295 ? 493 GLN EEE CB  1 
ATOM   1281  C CG  . GLN A 1 175 ? 0.592   62.825  3.039   1.000 110.181 ? 493 GLN EEE CG  1 
ATOM   1282  C CD  . GLN A 1 175 ? 1.442   62.533  1.826   1.000 108.517 ? 493 GLN EEE CD  1 
ATOM   1283  O OE1 . GLN A 1 175 ? 2.046   61.461  1.677   1.000 100.196 ? 493 GLN EEE OE1 1 
ATOM   1284  N NE2 . GLN A 1 175 ? 1.481   63.522  0.952   1.000 105.462 ? 493 GLN EEE NE2 1 
ATOM   1285  N N   . SER A 1 176 ? 0.644   58.579  3.658   1.000 94.389  ? 494 SER EEE N   1 
ATOM   1286  C CA  . SER A 1 176 ? 1.168   57.244  4.034   1.000 98.910  ? 494 SER EEE CA  1 
ATOM   1287  C C   . SER A 1 176 ? 2.656   57.345  4.409   1.000 107.882 ? 494 SER EEE C   1 
ATOM   1288  O O   . SER A 1 176 ? 3.367   58.144  3.769   1.000 107.038 ? 494 SER EEE O   1 
ATOM   1289  C CB  . SER A 1 176 ? 0.923   56.274  2.916   1.000 91.327  ? 494 SER EEE CB  1 
ATOM   1290  O OG  . SER A 1 176 ? 1.495   55.010  3.214   1.000 94.446  ? 494 SER EEE OG  1 
ATOM   1291  N N   . TYR A 1 177 ? 3.103   56.590  5.423   1.000 115.630 ? 495 TYR EEE N   1 
ATOM   1292  C CA  . TYR A 1 177 ? 4.541   56.323  5.704   1.000 112.565 ? 495 TYR EEE CA  1 
ATOM   1293  C C   . TYR A 1 177 ? 5.082   55.403  4.607   1.000 119.971 ? 495 TYR EEE C   1 
ATOM   1294  O O   . TYR A 1 177 ? 4.409   54.385  4.317   1.000 116.575 ? 495 TYR EEE O   1 
ATOM   1295  C CB  . TYR A 1 177 ? 4.767   55.656  7.070   1.000 107.588 ? 495 TYR EEE CB  1 
ATOM   1296  C CG  . TYR A 1 177 ? 4.604   56.581  8.249   1.000 105.322 ? 495 TYR EEE CG  1 
ATOM   1297  C CD1 . TYR A 1 177 ? 5.357   57.742  8.347   1.000 107.872 ? 495 TYR EEE CD1 1 
ATOM   1298  C CD2 . TYR A 1 177 ? 3.696   56.308  9.259   1.000 93.645  ? 495 TYR EEE CD2 1 
ATOM   1299  C CE1 . TYR A 1 177 ? 5.218   58.607  9.420   1.000 98.987  ? 495 TYR EEE CE1 1 
ATOM   1300  C CE2 . TYR A 1 177 ? 3.548   57.155  10.343  1.000 86.219  ? 495 TYR EEE CE2 1 
ATOM   1301  C CZ  . TYR A 1 177 ? 4.310   58.308  10.417  1.000 88.967  ? 495 TYR EEE CZ  1 
ATOM   1302  O OH  . TYR A 1 177 ? 4.182   59.157  11.469  1.000 85.352  ? 495 TYR EEE OH  1 
ATOM   1303  N N   . GLY A 1 178 ? 6.247   55.742  4.037   1.000 121.482 ? 496 GLY EEE N   1 
ATOM   1304  C CA  . GLY A 1 178 ? 6.949   54.942  3.011   1.000 116.512 ? 496 GLY EEE CA  1 
ATOM   1305  C C   . GLY A 1 178 ? 8.011   54.053  3.637   1.000 116.446 ? 496 GLY EEE C   1 
ATOM   1306  O O   . GLY A 1 178 ? 9.208   54.280  3.350   1.000 126.244 ? 496 GLY EEE O   1 
ATOM   1307  N N   . PHE A 1 179 ? 7.600   53.076  4.457   1.000 117.947 ? 497 PHE EEE N   1 
ATOM   1308  C CA  . PHE A 1 179 ? 8.506   52.258  5.313   1.000 125.222 ? 497 PHE EEE CA  1 
ATOM   1309  C C   . PHE A 1 179 ? 9.254   51.209  4.480   1.000 126.077 ? 497 PHE EEE C   1 
ATOM   1310  O O   . PHE A 1 179 ? 8.747   50.069  4.339   1.000 116.569 ? 497 PHE EEE O   1 
ATOM   1311  C CB  . PHE A 1 179 ? 7.747   51.557  6.449   1.000 131.505 ? 497 PHE EEE CB  1 
ATOM   1312  C CG  . PHE A 1 179 ? 7.279   52.444  7.578   1.000 132.812 ? 497 PHE EEE CG  1 
ATOM   1313  C CD1 . PHE A 1 179 ? 8.067   53.485  8.045   1.000 135.599 ? 497 PHE EEE CD1 1 
ATOM   1314  C CD2 . PHE A 1 179 ? 6.055   52.220  8.191   1.000 127.252 ? 497 PHE EEE CD2 1 
ATOM   1315  C CE1 . PHE A 1 179 ? 7.631   54.297  9.079   1.000 132.497 ? 497 PHE EEE CE1 1 
ATOM   1316  C CE2 . PHE A 1 179 ? 5.621   53.036  9.223   1.000 125.223 ? 497 PHE EEE CE2 1 
ATOM   1317  C CZ  . PHE A 1 179 ? 6.410   54.070  9.667   1.000 128.100 ? 497 PHE EEE CZ  1 
ATOM   1318  N N   . GLN A 1 180 ? 10.441  51.577  3.984   1.000 131.727 ? 498 GLN EEE N   1 
ATOM   1319  C CA  . GLN A 1 180 ? 11.377  50.681  3.248   1.000 131.022 ? 498 GLN EEE CA  1 
ATOM   1320  C C   . GLN A 1 180 ? 12.451  50.198  4.223   1.000 129.668 ? 498 GLN EEE C   1 
ATOM   1321  O O   . GLN A 1 180 ? 12.869  50.956  5.106   1.000 119.313 ? 498 GLN EEE O   1 
ATOM   1322  C CB  . GLN A 1 180 ? 11.993  51.401  2.043   1.000 132.980 ? 498 GLN EEE CB  1 
ATOM   1323  C CG  . GLN A 1 180 ? 10.989  52.222  1.240   1.000 131.817 ? 498 GLN EEE CG  1 
ATOM   1324  C CD  . GLN A 1 180 ? 11.480  52.552  -0.147  1.000 128.690 ? 498 GLN EEE CD  1 
ATOM   1325  O OE1 . GLN A 1 180 ? 11.572  51.678  -1.008  1.000 135.864 ? 498 GLN EEE OE1 1 
ATOM   1326  N NE2 . GLN A 1 180 ? 11.772  53.822  -0.377  1.000 105.880 ? 498 GLN EEE NE2 1 
ATOM   1327  N N   . PRO A 1 181 ? 12.914  48.927  4.096   1.000 128.337 ? 499 PRO EEE N   1 
ATOM   1328  C CA  . PRO A 1 181 ? 13.932  48.368  4.990   1.000 125.394 ? 499 PRO EEE CA  1 
ATOM   1329  C C   . PRO A 1 181 ? 15.253  49.154  4.984   1.000 120.157 ? 499 PRO EEE C   1 
ATOM   1330  O O   . PRO A 1 181 ? 15.905  49.192  6.002   1.000 105.014 ? 499 PRO EEE O   1 
ATOM   1331  C CB  . PRO A 1 181 ? 14.178  46.948  4.445   1.000 113.120 ? 499 PRO EEE CB  1 
ATOM   1332  C CG  . PRO A 1 181 ? 12.912  46.616  3.693   1.000 111.513 ? 499 PRO EEE CG  1 
ATOM   1333  C CD  . PRO A 1 181 ? 12.458  47.938  3.106   1.000 119.224 ? 499 PRO EEE CD  1 
ATOM   1334  N N   . THR A 1 182 ? 15.589  49.771  3.848   1.000 124.162 ? 500 THR EEE N   1 
ATOM   1335  C CA  . THR A 1 182 ? 16.878  50.467  3.598   1.000 119.120 ? 500 THR EEE CA  1 
ATOM   1336  C C   . THR A 1 182 ? 16.805  51.937  4.038   1.000 113.931 ? 500 THR EEE C   1 
ATOM   1337  O O   . THR A 1 182 ? 17.832  52.627  3.895   1.000 97.137  ? 500 THR EEE O   1 
ATOM   1338  C CB  . THR A 1 182 ? 17.256  50.337  2.118   1.000 119.444 ? 500 THR EEE CB  1 
ATOM   1339  O OG1 . THR A 1 182 ? 16.289  51.067  1.357   1.000 120.530 ? 500 THR EEE OG1 1 
ATOM   1340  C CG2 . THR A 1 182 ? 17.315  48.894  1.661   1.000 112.531 ? 500 THR EEE CG2 1 
ATOM   1341  N N   . ASN A 1 183 ? 15.653  52.403  4.537   1.000 114.461 ? 501 ASN EEE N   1 
ATOM   1342  C CA  . ASN A 1 183 ? 15.489  53.776  5.094   1.000 110.285 ? 501 ASN EEE CA  1 
ATOM   1343  C C   . ASN A 1 183 ? 16.413  53.928  6.306   1.000 108.652 ? 501 ASN EEE C   1 
ATOM   1344  O O   . ASN A 1 183 ? 16.652  52.907  6.985   1.000 105.072 ? 501 ASN EEE O   1 
ATOM   1345  C CB  . ASN A 1 183 ? 14.065  54.063  5.579   1.000 115.112 ? 501 ASN EEE CB  1 
ATOM   1346  C CG  . ASN A 1 183 ? 13.023  54.129  4.487   1.000 114.347 ? 501 ASN EEE CG  1 
ATOM   1347  O OD1 . ASN A 1 183 ? 11.892  53.682  4.685   1.000 128.393 ? 501 ASN EEE OD1 1 
ATOM   1348  N ND2 . ASN A 1 183 ? 13.382  54.708  3.355   1.000 105.002 ? 501 ASN EEE ND2 1 
ATOM   1349  N N   . GLY A 1 184 ? 16.881  55.150  6.585   1.000 102.361 ? 502 GLY EEE N   1 
ATOM   1350  C CA  . GLY A 1 184 ? 17.678  55.470  7.787   1.000 100.813 ? 502 GLY EEE CA  1 
ATOM   1351  C C   . GLY A 1 184 ? 16.837  55.326  9.045   1.000 104.443 ? 502 GLY EEE C   1 
ATOM   1352  O O   . GLY A 1 184 ? 15.619  55.574  8.960   1.000 125.225 ? 502 GLY EEE O   1 
ATOM   1353  N N   . VAL A 1 185 ? 17.432  54.903  10.166  1.000 105.738 ? 503 VAL EEE N   1 
ATOM   1354  C CA  . VAL A 1 185 ? 16.729  54.874  11.485  1.000 105.240 ? 503 VAL EEE CA  1 
ATOM   1355  C C   . VAL A 1 185 ? 16.084  56.250  11.633  1.000 102.502 ? 503 VAL EEE C   1 
ATOM   1356  O O   . VAL A 1 185 ? 16.751  57.237  11.287  1.000 93.218  ? 503 VAL EEE O   1 
ATOM   1357  C CB  . VAL A 1 185 ? 17.656  54.543  12.673  1.000 103.990 ? 503 VAL EEE CB  1 
ATOM   1358  C CG1 . VAL A 1 185 ? 17.018  54.917  14.002  1.000 105.977 ? 503 VAL EEE CG1 1 
ATOM   1359  C CG2 . VAL A 1 185 ? 18.061  53.078  12.689  1.000 102.894 ? 503 VAL EEE CG2 1 
ATOM   1360  N N   . GLY A 1 186 ? 14.825  56.313  12.063  1.000 100.959 ? 504 GLY EEE N   1 
ATOM   1361  C CA  . GLY A 1 186 ? 14.107  57.593  12.204  1.000 99.643  ? 504 GLY EEE CA  1 
ATOM   1362  C C   . GLY A 1 186 ? 13.131  57.808  11.064  1.000 102.493 ? 504 GLY EEE C   1 
ATOM   1363  O O   . GLY A 1 186 ? 12.141  58.520  11.265  1.000 102.977 ? 504 GLY EEE O   1 
ATOM   1364  N N   . TYR A 1 187 ? 13.401  57.220  9.903   1.000 103.468 ? 505 TYR EEE N   1 
ATOM   1365  C CA  . TYR A 1 187 ? 12.395  57.004  8.835   1.000 100.446 ? 505 TYR EEE CA  1 
ATOM   1366  C C   . TYR A 1 187 ? 11.913  55.555  8.915   1.000 100.575 ? 505 TYR EEE C   1 
ATOM   1367  O O   . TYR A 1 187 ? 10.957  55.216  8.214   1.000 115.226 ? 505 TYR EEE O   1 
ATOM   1368  C CB  . TYR A 1 187 ? 12.954  57.365  7.459   1.000 106.665 ? 505 TYR EEE CB  1 
ATOM   1369  C CG  . TYR A 1 187 ? 12.740  58.801  7.070   1.000 115.879 ? 505 TYR EEE CG  1 
ATOM   1370  C CD1 . TYR A 1 187 ? 13.768  59.736  7.158   1.000 115.759 ? 505 TYR EEE CD1 1 
ATOM   1371  C CD2 . TYR A 1 187 ? 11.501  59.238  6.628   1.000 118.487 ? 505 TYR EEE CD2 1 
ATOM   1372  C CE1 . TYR A 1 187 ? 13.572  61.064  6.813   1.000 114.531 ? 505 TYR EEE CE1 1 
ATOM   1373  C CE2 . TYR A 1 187 ? 11.289  60.563  6.275   1.000 124.064 ? 505 TYR EEE CE2 1 
ATOM   1374  C CZ  . TYR A 1 187 ? 12.329  61.479  6.367   1.000 120.033 ? 505 TYR EEE CZ  1 
ATOM   1375  O OH  . TYR A 1 187 ? 12.159  62.788  6.015   1.000 107.061 ? 505 TYR EEE OH  1 
ATOM   1376  N N   . GLN A 1 188 ? 12.512  54.725  9.770   1.000 96.086  ? 506 GLN EEE N   1 
ATOM   1377  C CA  . GLN A 1 188 ? 12.042  53.329  9.942   1.000 97.568  ? 506 GLN EEE CA  1 
ATOM   1378  C C   . GLN A 1 188 ? 10.892  53.343  10.931  1.000 96.276  ? 506 GLN EEE C   1 
ATOM   1379  O O   . GLN A 1 188 ? 10.792  54.247  11.753  1.000 86.410  ? 506 GLN EEE O   1 
ATOM   1380  C CB  . GLN A 1 188 ? 13.142  52.412  10.462  1.000 101.899 ? 506 GLN EEE CB  1 
ATOM   1381  C CG  . GLN A 1 188 ? 14.505  52.760  9.903   1.000 97.862  ? 506 GLN EEE CG  1 
ATOM   1382  C CD  . GLN A 1 188 ? 15.526  51.680  10.142  1.000 95.022  ? 506 GLN EEE CD  1 
ATOM   1383  O OE1 . GLN A 1 188 ? 15.242  50.626  10.714  1.000 95.242  ? 506 GLN EEE OE1 1 
ATOM   1384  N NE2 . GLN A 1 188 ? 16.736  51.952  9.685   1.000 87.743  ? 506 GLN EEE NE2 1 
ATOM   1385  N N   . PRO A 1 189 ? 10.011  52.324  10.892  1.000 103.662 ? 507 PRO EEE N   1 
ATOM   1386  C CA  . PRO A 1 189 ? 8.879   52.247  11.814  1.000 107.220 ? 507 PRO EEE CA  1 
ATOM   1387  C C   . PRO A 1 189 ? 9.279   51.842  13.241  1.000 101.610 ? 507 PRO EEE C   1 
ATOM   1388  O O   . PRO A 1 189 ? 10.154  51.010  13.399  1.000 96.479  ? 507 PRO EEE O   1 
ATOM   1389  C CB  . PRO A 1 189 ? 7.999   51.158  11.184  1.000 109.474 ? 507 PRO EEE CB  1 
ATOM   1390  C CG  . PRO A 1 189 ? 8.998   50.249  10.499  1.000 109.480 ? 507 PRO EEE CG  1 
ATOM   1391  C CD  . PRO A 1 189 ? 10.054  51.191  9.955   1.000 107.460 ? 507 PRO EEE CD  1 
ATOM   1392  N N   . TYR A 1 190 ? 8.626   52.453  14.231  1.000 95.934  ? 508 TYR EEE N   1 
ATOM   1393  C CA  . TYR A 1 190 ? 8.695   52.094  15.669  1.000 90.306  ? 508 TYR EEE CA  1 
ATOM   1394  C C   . TYR A 1 190 ? 7.273   51.872  16.189  1.000 76.680  ? 508 TYR EEE C   1 
ATOM   1395  O O   . TYR A 1 190 ? 6.416   52.756  15.982  1.000 73.618  ? 508 TYR EEE O   1 
ATOM   1396  C CB  . TYR A 1 190 ? 9.357   53.211  16.478  1.000 99.239  ? 508 TYR EEE CB  1 
ATOM   1397  C CG  . TYR A 1 190 ? 10.854  53.320  16.347  1.000 105.308 ? 508 TYR EEE CG  1 
ATOM   1398  C CD1 . TYR A 1 190 ? 11.443  53.711  15.155  1.000 107.563 ? 508 TYR EEE CD1 1 
ATOM   1399  C CD2 . TYR A 1 190 ? 11.684  53.051  17.426  1.000 108.859 ? 508 TYR EEE CD2 1 
ATOM   1400  C CE1 . TYR A 1 190 ? 12.819  53.830  15.034  1.000 111.224 ? 508 TYR EEE CE1 1 
ATOM   1401  C CE2 . TYR A 1 190 ? 13.062  53.167  17.322  1.000 109.716 ? 508 TYR EEE CE2 1 
ATOM   1402  C CZ  . TYR A 1 190 ? 13.633  53.559  16.124  1.000 108.522 ? 508 TYR EEE CZ  1 
ATOM   1403  O OH  . TYR A 1 190 ? 14.990  53.662  16.026  1.000 101.744 ? 508 TYR EEE OH  1 
ATOM   1404  N N   . ARG A 1 191 ? 7.032   50.737  16.841  1.000 68.632  ? 509 ARG EEE N   1 
ATOM   1405  C CA  . ARG A 1 191 ? 5.764   50.464  17.562  1.000 68.964  ? 509 ARG EEE CA  1 
ATOM   1406  C C   . ARG A 1 191 ? 5.801   51.135  18.933  1.000 61.858  ? 509 ARG EEE C   1 
ATOM   1407  O O   . ARG A 1 191 ? 6.754   50.902  19.665  1.000 63.141  ? 509 ARG EEE O   1 
ATOM   1408  C CB  . ARG A 1 191 ? 5.552   48.959  17.731  1.000 73.044  ? 509 ARG EEE CB  1 
ATOM   1409  C CG  . ARG A 1 191 ? 5.393   48.249  16.399  1.000 79.692  ? 509 ARG EEE CG  1 
ATOM   1410  C CD  . ARG A 1 191 ? 4.993   46.802  16.548  1.000 79.579  ? 509 ARG EEE CD  1 
ATOM   1411  N NE  . ARG A 1 191 ? 4.669   46.290  15.230  1.000 85.116  ? 509 ARG EEE NE  1 
ATOM   1412  C CZ  . ARG A 1 191 ? 4.038   45.150  14.998  1.000 85.114  ? 509 ARG EEE CZ  1 
ATOM   1413  N NH1 . ARG A 1 191 ? 3.644   44.381  16.004  1.000 79.491  ? 509 ARG EEE NH1 1 
ATOM   1414  N NH2 . ARG A 1 191 ? 3.788   44.794  13.749  1.000 88.132  ? 509 ARG EEE NH2 1 
ATOM   1415  N N   . VAL A 1 192 ? 4.743   51.853  19.288  1.000 57.208  ? 510 VAL EEE N   1 
ATOM   1416  C CA  . VAL A 1 192 ? 4.617   52.596  20.571  1.000 52.434  ? 510 VAL EEE CA  1 
ATOM   1417  C C   . VAL A 1 192 ? 3.431   52.045  21.363  1.000 50.301  ? 510 VAL EEE C   1 
ATOM   1418  O O   . VAL A 1 192 ? 2.423   51.709  20.742  1.000 54.186  ? 510 VAL EEE O   1 
ATOM   1419  C CB  . VAL A 1 192 ? 4.423   54.087  20.284  1.000 51.453  ? 510 VAL EEE CB  1 
ATOM   1420  C CG1 . VAL A 1 192 ? 4.358   54.910  21.566  1.000 52.239  ? 510 VAL EEE CG1 1 
ATOM   1421  C CG2 . VAL A 1 192 ? 5.494   54.587  19.336  1.000 51.790  ? 510 VAL EEE CG2 1 
ATOM   1422  N N   . VAL A 1 193 ? 3.568   51.957  22.680  1.000 45.340  ? 511 VAL EEE N   1 
ATOM   1423  C CA  . VAL A 1 193 ? 2.448   51.682  23.615  1.000 44.731  ? 511 VAL EEE CA  1 
ATOM   1424  C C   . VAL A 1 193 ? 2.486   52.755  24.690  1.000 47.840  ? 511 VAL EEE C   1 
ATOM   1425  O O   . VAL A 1 193 ? 3.561   52.931  25.299  1.000 61.229  ? 511 VAL EEE O   1 
ATOM   1426  C CB  . VAL A 1 193 ? 2.538   50.291  24.256  1.000 45.061  ? 511 VAL EEE CB  1 
ATOM   1427  C CG1 . VAL A 1 193 ? 1.478   50.105  25.335  1.000 47.701  ? 511 VAL EEE CG1 1 
ATOM   1428  C CG2 . VAL A 1 193 ? 2.440   49.196  23.212  1.000 43.571  ? 511 VAL EEE CG2 1 
ATOM   1429  N N   . VAL A 1 194 ? 1.355   53.411  24.931  1.000 46.557  ? 512 VAL EEE N   1 
ATOM   1430  C CA  . VAL A 1 194 ? 1.219   54.442  25.993  1.000 43.583  ? 512 VAL EEE CA  1 
ATOM   1431  C C   . VAL A 1 194 ? 0.269   53.905  27.061  1.000 47.929  ? 512 VAL EEE C   1 
ATOM   1432  O O   . VAL A 1 194 ? -0.964  53.864  26.816  1.000 53.333  ? 512 VAL EEE O   1 
ATOM   1433  C CB  . VAL A 1 194 ? 0.750   55.789  25.428  1.000 40.955  ? 512 VAL EEE CB  1 
ATOM   1434  C CG1 . VAL A 1 194 ? 0.752   56.858  26.505  1.000 41.806  ? 512 VAL EEE CG1 1 
ATOM   1435  C CG2 . VAL A 1 194 ? 1.596   56.212  24.235  1.000 41.881  ? 512 VAL EEE CG2 1 
ATOM   1436  N N   . LEU A 1 195 ? 0.850   53.491  28.190  1.000 47.582  ? 513 LEU EEE N   1 
ATOM   1437  C CA  . LEU A 1 195 ? 0.140   53.206  29.461  1.000 46.317  ? 513 LEU EEE CA  1 
ATOM   1438  C C   . LEU A 1 195 ? -0.240  54.546  30.090  1.000 46.023  ? 513 LEU EEE C   1 
ATOM   1439  O O   . LEU A 1 195 ? 0.653   55.393  30.222  1.000 51.556  ? 513 LEU EEE O   1 
ATOM   1440  C CB  . LEU A 1 195 ? 1.054   52.386  30.375  1.000 48.435  ? 513 LEU EEE CB  1 
ATOM   1441  C CG  . LEU A 1 195 ? 1.639   51.111  29.756  1.000 52.086  ? 513 LEU EEE CG  1 
ATOM   1442  C CD1 . LEU A 1 195 ? 2.502   50.360  30.758  1.000 54.222  ? 513 LEU EEE CD1 1 
ATOM   1443  C CD2 . LEU A 1 195 ? 0.545   50.199  29.229  1.000 53.343  ? 513 LEU EEE CD2 1 
ATOM   1444  N N   . SER A 1 196 ? -1.525  54.763  30.375  1.000 47.828  ? 514 SER EEE N   1 
ATOM   1445  C CA  . SER A 1 196 ? -2.054  55.939  31.118  1.000 50.168  ? 514 SER EEE CA  1 
ATOM   1446  C C   . SER A 1 196 ? -2.872  55.435  32.311  1.000 49.250  ? 514 SER EEE C   1 
ATOM   1447  O O   . SER A 1 196 ? -3.526  54.384  32.169  1.000 51.390  ? 514 SER EEE O   1 
ATOM   1448  C CB  . SER A 1 196 ? -2.856  56.858  30.219  1.000 54.136  ? 514 SER EEE CB  1 
ATOM   1449  O OG  . SER A 1 196 ? -3.780  56.134  29.424  1.000 58.505  ? 514 SER EEE OG  1 
ATOM   1450  N N   . PHE A 1 197 ? -2.802  56.131  33.448  1.000 51.352  ? 515 PHE EEE N   1 
ATOM   1451  C CA  . PHE A 1 197 ? -3.358  55.689  34.757  1.000 58.596  ? 515 PHE EEE CA  1 
ATOM   1452  C C   . PHE A 1 197 ? -4.249  56.787  35.342  1.000 67.002  ? 515 PHE EEE C   1 
ATOM   1453  O O   . PHE A 1 197 ? -3.782  57.938  35.436  1.000 66.855  ? 515 PHE EEE O   1 
ATOM   1454  C CB  . PHE A 1 197 ? -2.242  55.361  35.758  1.000 58.218  ? 515 PHE EEE CB  1 
ATOM   1455  C CG  . PHE A 1 197 ? -1.210  54.373  35.274  1.000 54.229  ? 515 PHE EEE CG  1 
ATOM   1456  C CD1 . PHE A 1 197 ? -1.309  53.034  35.592  1.000 53.380  ? 515 PHE EEE CD1 1 
ATOM   1457  C CD2 . PHE A 1 197 ? -0.135  54.778  34.500  1.000 56.029  ? 515 PHE EEE CD2 1 
ATOM   1458  C CE1 . PHE A 1 197 ? -0.362  52.122  35.144  1.000 56.978  ? 515 PHE EEE CE1 1 
ATOM   1459  C CE2 . PHE A 1 197 ? 0.802   53.863  34.037  1.000 55.758  ? 515 PHE EEE CE2 1 
ATOM   1460  C CZ  . PHE A 1 197 ? 0.693   52.537  34.367  1.000 54.597  ? 515 PHE EEE CZ  1 
ATOM   1461  N N   . GLU A 1 198 ? -5.478  56.433  35.738  1.000 80.896  ? 516 GLU EEE N   1 
ATOM   1462  C CA  . GLU A 1 198 ? -6.413  57.342  36.458  1.000 96.856  ? 516 GLU EEE CA  1 
ATOM   1463  C C   . GLU A 1 198 ? -6.839  56.667  37.769  1.000 107.890 ? 516 GLU EEE C   1 
ATOM   1464  O O   . GLU A 1 198 ? -6.920  55.421  37.796  1.000 109.861 ? 516 GLU EEE O   1 
ATOM   1465  C CB  . GLU A 1 198 ? -7.613  57.702  35.575  1.000 103.379 ? 516 GLU EEE CB  1 
ATOM   1466  C CG  . GLU A 1 198 ? -8.492  56.513  35.197  1.000 112.839 ? 516 GLU EEE CG  1 
ATOM   1467  C CD  . GLU A 1 198 ? -9.703  56.827  34.325  1.000 113.184 ? 516 GLU EEE CD  1 
ATOM   1468  O OE1 . GLU A 1 198 ? -9.667  57.852  33.582  1.000 97.902  ? 516 GLU EEE OE1 1 
ATOM   1469  O OE2 . GLU A 1 198 ? -10.679 56.031  34.376  1.000 103.384 ? 516 GLU EEE OE2 1 
ATOM   1470  N N   . LEU A 1 199 ? -7.059  57.464  38.818  1.000 115.565 ? 517 LEU EEE N   1 
ATOM   1471  C CA  . LEU A 1 199 ? -7.564  57.017  40.145  1.000 113.132 ? 517 LEU EEE CA  1 
ATOM   1472  C C   . LEU A 1 199 ? -8.711  57.955  40.540  1.000 114.061 ? 517 LEU EEE C   1 
ATOM   1473  O O   . LEU A 1 199 ? -8.438  59.113  40.890  1.000 104.216 ? 517 LEU EEE O   1 
ATOM   1474  C CB  . LEU A 1 199 ? -6.403  57.025  41.153  1.000 114.136 ? 517 LEU EEE CB  1 
ATOM   1475  C CG  . LEU A 1 199 ? -6.551  56.127  42.382  1.000 110.259 ? 517 LEU EEE CG  1 
ATOM   1476  C CD1 . LEU A 1 199 ? -5.188  55.699  42.922  1.000 105.390 ? 517 LEU EEE CD1 1 
ATOM   1477  C CD2 . LEU A 1 199 ? -7.362  56.835  43.458  1.000 106.371 ? 517 LEU EEE CD2 1 
ATOM   1478  N N   . LEU A 1 200 ? -9.949  57.473  40.429  1.000 133.491 ? 518 LEU EEE N   1 
ATOM   1479  C CA  . LEU A 1 200 ? -11.188 58.188  40.847  1.000 141.153 ? 518 LEU EEE CA  1 
ATOM   1480  C C   . LEU A 1 200 ? -11.556 57.708  42.260  1.000 159.617 ? 518 LEU EEE C   1 
ATOM   1481  O O   . LEU A 1 200 ? -10.872 56.794  42.764  1.000 169.285 ? 518 LEU EEE O   1 
ATOM   1482  C CB  . LEU A 1 200 ? -12.308 57.904  39.836  1.000 124.320 ? 518 LEU EEE CB  1 
ATOM   1483  C CG  . LEU A 1 200 ? -11.897 57.928  38.362  1.000 111.039 ? 518 LEU EEE CG  1 
ATOM   1484  C CD1 . LEU A 1 200 ? -12.980 57.327  37.475  1.000 101.202 ? 518 LEU EEE CD1 1 
ATOM   1485  C CD2 . LEU A 1 200 ? -11.543 59.344  37.929  1.000 100.864 ? 518 LEU EEE CD2 1 
ATOM   1486  N N   . HIS A 1 201 ? -12.571 58.309  42.888  1.000 164.603 ? 519 HIS EEE N   1 
ATOM   1487  C CA  . HIS A 1 201 ? -13.214 57.777  44.122  1.000 152.909 ? 519 HIS EEE CA  1 
ATOM   1488  C C   . HIS A 1 201 ? -14.289 56.761  43.691  1.000 138.493 ? 519 HIS EEE C   1 
ATOM   1489  O O   . HIS A 1 201 ? -15.485 56.996  43.956  1.000 125.123 ? 519 HIS EEE O   1 
ATOM   1490  C CB  . HIS A 1 201 ? -13.678 58.929  45.038  1.000 150.417 ? 519 HIS EEE CB  1 
ATOM   1491  C CG  . HIS A 1 201 ? -12.558 59.724  45.641  1.000 147.341 ? 519 HIS EEE CG  1 
ATOM   1492  N ND1 . HIS A 1 201 ? -11.903 59.337  46.804  1.000 135.450 ? 519 HIS EEE ND1 1 
ATOM   1493  C CD2 . HIS A 1 201 ? -11.982 60.890  45.267  1.000 143.197 ? 519 HIS EEE CD2 1 
ATOM   1494  C CE1 . HIS A 1 201 ? -10.971 60.220  47.108  1.000 128.063 ? 519 HIS EEE CE1 1 
ATOM   1495  N NE2 . HIS A 1 201 ? -10.997 61.182  46.181  1.000 135.413 ? 519 HIS EEE NE2 1 
ATOM   1496  N N   . ALA A 1 202 ? -13.840 55.699  43.007  1.000 128.144 ? 520 ALA EEE N   1 
ATOM   1497  C CA  . ALA A 1 202 ? -14.586 54.468  42.647  1.000 120.071 ? 520 ALA EEE CA  1 
ATOM   1498  C C   . ALA A 1 202 ? -13.704 53.266  42.999  1.000 120.792 ? 520 ALA EEE C   1 
ATOM   1499  O O   . ALA A 1 202 ? -12.529 53.438  43.324  1.000 106.211 ? 520 ALA EEE O   1 
ATOM   1500  C CB  . ALA A 1 202 ? -14.947 54.502  41.177  1.000 108.278 ? 520 ALA EEE CB  1 
ATOM   1501  N N   . PRO A 1 203 ? -14.216 52.010  42.969  1.000 120.762 ? 521 PRO EEE N   1 
ATOM   1502  C CA  . PRO A 1 203 ? -13.376 50.831  43.213  1.000 117.089 ? 521 PRO EEE CA  1 
ATOM   1503  C C   . PRO A 1 203 ? -12.171 50.745  42.259  1.000 111.523 ? 521 PRO EEE C   1 
ATOM   1504  O O   . PRO A 1 203 ? -12.316 51.111  41.112  1.000 113.919 ? 521 PRO EEE O   1 
ATOM   1505  C CB  . PRO A 1 203 ? -14.316 49.634  42.980  1.000 109.167 ? 521 PRO EEE CB  1 
ATOM   1506  C CG  . PRO A 1 203 ? -15.701 50.205  43.187  1.000 108.581 ? 521 PRO EEE CG  1 
ATOM   1507  C CD  . PRO A 1 203 ? -15.619 51.648  42.722  1.000 112.028 ? 521 PRO EEE CD  1 
ATOM   1508  N N   . ALA A 1 204 ? -11.022 50.274  42.756  1.000 102.428 ? 522 ALA EEE N   1 
ATOM   1509  C CA  . ALA A 1 204 ? -9.789  50.018  41.974  1.000 100.982 ? 522 ALA EEE CA  1 
ATOM   1510  C C   . ALA A 1 204 ? -9.727  48.531  41.607  1.000 101.925 ? 522 ALA EEE C   1 
ATOM   1511  O O   . ALA A 1 204 ? -9.939  47.706  42.501  1.000 101.367 ? 522 ALA EEE O   1 
ATOM   1512  C CB  . ALA A 1 204 ? -8.585  50.443  42.775  1.000 99.473  ? 522 ALA EEE CB  1 
ATOM   1513  N N   . THR A 1 205 ? -9.467  48.199  40.340  1.000 112.694 ? 523 THR EEE N   1 
ATOM   1514  C CA  . THR A 1 205 ? -9.565  46.810  39.808  1.000 126.816 ? 523 THR EEE CA  1 
ATOM   1515  C C   . THR A 1 205 ? -8.259  46.370  39.126  1.000 132.168 ? 523 THR EEE C   1 
ATOM   1516  O O   . THR A 1 205 ? -8.176  45.170  38.789  1.000 123.862 ? 523 THR EEE O   1 
ATOM   1517  C CB  . THR A 1 205 ? -10.771 46.676  38.865  1.000 132.685 ? 523 THR EEE CB  1 
ATOM   1518  O OG1 . THR A 1 205 ? -10.647 47.629  37.809  1.000 138.793 ? 523 THR EEE OG1 1 
ATOM   1519  C CG2 . THR A 1 205 ? -12.100 46.879  39.561  1.000 126.533 ? 523 THR EEE CG2 1 
ATOM   1520  N N   . VAL A 1 206 ? -7.296  47.283  38.920  1.000 135.927 ? 524 VAL EEE N   1 
ATOM   1521  C CA  . VAL A 1 206 ? -5.964  46.988  38.303  1.000 142.262 ? 524 VAL EEE CA  1 
ATOM   1522  C C   . VAL A 1 206 ? -4.877  47.211  39.360  1.000 150.565 ? 524 VAL EEE C   1 
ATOM   1523  O O   . VAL A 1 206 ? -4.586  48.394  39.678  1.000 163.078 ? 524 VAL EEE O   1 
ATOM   1524  C CB  . VAL A 1 206 ? -5.678  47.834  37.047  1.000 136.300 ? 524 VAL EEE CB  1 
ATOM   1525  C CG1 . VAL A 1 206 ? -4.400  47.379  36.355  1.000 132.691 ? 524 VAL EEE CG1 1 
ATOM   1526  C CG2 . VAL A 1 206 ? -6.840  47.831  36.068  1.000 140.852 ? 524 VAL EEE CG2 1 
ATOM   1527  N N   . CYS A 1 207 ? -4.287  46.113  39.846  1.000 144.954 ? 525 CYS EEE N   1 
ATOM   1528  C CA  . CYS A 1 207 ? -3.369  46.068  41.013  1.000 137.941 ? 525 CYS EEE CA  1 
ATOM   1529  C C   . CYS A 1 207 ? -2.133  45.240  40.684  1.000 133.764 ? 525 CYS EEE C   1 
ATOM   1530  O O   . CYS A 1 207 ? -2.231  44.374  39.802  1.000 130.700 ? 525 CYS EEE O   1 
ATOM   1531  C CB  . CYS A 1 207 ? -4.078  45.454  42.213  1.000 139.553 ? 525 CYS EEE CB  1 
ATOM   1532  S SG  . CYS A 1 207 ? -5.495  46.441  42.757  1.000 142.039 ? 525 CYS EEE SG  1 
ATOM   1533  N N   . GLY A 1 208 ? -1.025  45.498  41.380  1.000 136.811 ? 526 GLY EEE N   1 
ATOM   1534  C CA  . GLY A 1 208 ? 0.212   44.699  41.268  1.000 150.703 ? 526 GLY EEE CA  1 
ATOM   1535  C C   . GLY A 1 208 ? 0.140   43.433  42.118  1.000 147.418 ? 526 GLY EEE C   1 
ATOM   1536  O O   . GLY A 1 208 ? -0.765  43.316  42.946  1.000 136.713 ? 526 GLY EEE O   1 
ATOM   1537  N N   . PRO A 1 209 ? 1.066   42.451  41.930  1.000 143.025 ? 527 PRO EEE N   1 
ATOM   1538  C CA  . PRO A 1 209 ? 1.061   41.217  42.724  1.000 135.999 ? 527 PRO EEE CA  1 
ATOM   1539  C C   . PRO A 1 209 ? 1.174   41.499  44.235  1.000 143.593 ? 527 PRO EEE C   1 
ATOM   1540  O O   . PRO A 1 209 ? 0.554   40.775  44.998  1.000 143.544 ? 527 PRO EEE O   1 
ATOM   1541  C CB  . PRO A 1 209 ? 2.247   40.382  42.195  1.000 121.896 ? 527 PRO EEE CB  1 
ATOM   1542  C CG  . PRO A 1 209 ? 3.079   41.345  41.355  1.000 122.622 ? 527 PRO EEE CG  1 
ATOM   1543  C CD  . PRO A 1 209 ? 2.145   42.461  40.926  1.000 129.668 ? 527 PRO EEE CD  1 
ATOM   1544  N N   . LYS A 1 210 ? 1.938   42.532  44.624  1.000 139.186 ? 528 LYS EEE N   1 
ATOM   1545  C CA  . LYS A 1 210 ? 2.066   43.035  46.023  1.000 116.040 ? 528 LYS EEE CA  1 
ATOM   1546  C C   . LYS A 1 210 ? 0.855   43.927  46.329  1.000 99.240  ? 528 LYS EEE C   1 
ATOM   1547  O O   . LYS A 1 210 ? 0.107   43.743  47.276  1.000 89.053  ? 528 LYS EEE O   1 
ATOM   1548  C CB  . LYS A 1 210 ? 3.391   43.788  46.213  1.000 101.538 ? 528 LYS EEE CB  1 
ATOM   1549  N N   . GLN B 2 1   ? 16.327  45.639  41.254  1.000 73.721  ? 1   GLN HHH N   1 
ATOM   1550  C CA  . GLN B 2 1   ? 17.015  46.795  41.913  1.000 79.669  ? 1   GLN HHH CA  1 
ATOM   1551  C C   . GLN B 2 1   ? 18.290  47.117  41.129  1.000 75.418  ? 1   GLN HHH C   1 
ATOM   1552  O O   . GLN B 2 1   ? 18.892  46.162  40.632  1.000 90.014  ? 1   GLN HHH O   1 
ATOM   1553  C CB  . GLN B 2 1   ? 17.340  46.472  43.378  1.000 85.123  ? 1   GLN HHH CB  1 
ATOM   1554  C CG  . GLN B 2 1   ? 18.116  47.569  44.110  1.000 95.825  ? 1   GLN HHH CG  1 
ATOM   1555  C CD  . GLN B 2 1   ? 17.375  48.884  44.226  1.000 102.908 ? 1   GLN HHH CD  1 
ATOM   1556  O OE1 . GLN B 2 1   ? 16.146  48.924  44.273  1.000 113.642 ? 1   GLN HHH OE1 1 
ATOM   1557  N NE2 . GLN B 2 1   ? 18.114  49.984  44.290  1.000 99.404  ? 1   GLN HHH NE2 1 
ATOM   1558  N N   . MET B 2 2   ? 18.686  48.393  41.045  1.000 65.183  ? 2   MET HHH N   1 
ATOM   1559  C CA  . MET B 2 2   ? 19.939  48.826  40.366  1.000 62.251  ? 2   MET HHH CA  1 
ATOM   1560  C C   . MET B 2 2   ? 20.620  49.960  41.142  1.000 57.850  ? 2   MET HHH C   1 
ATOM   1561  O O   . MET B 2 2   ? 20.004  50.495  42.073  1.000 49.526  ? 2   MET HHH O   1 
ATOM   1562  C CB  . MET B 2 2   ? 19.661  49.276  38.931  1.000 63.713  ? 2   MET HHH CB  1 
ATOM   1563  C CG  . MET B 2 2   ? 18.960  50.627  38.842  1.000 62.425  ? 2   MET HHH CG  1 
ATOM   1564  S SD  . MET B 2 2   ? 20.088  52.035  38.615  1.000 54.506  ? 2   MET HHH SD  1 
ATOM   1565  C CE  . MET B 2 2   ? 20.989  51.433  37.191  1.000 56.870  ? 2   MET HHH CE  1 
ATOM   1566  N N   . GLN B 2 3   ? 21.863  50.282  40.753  1.000 56.713  ? 3   GLN HHH N   1 
ATOM   1567  C CA  . GLN B 2 3   ? 22.792  51.188  41.479  1.000 54.330  ? 3   GLN HHH CA  1 
ATOM   1568  C C   . GLN B 2 3   ? 23.620  52.014  40.482  1.000 46.013  ? 3   GLN HHH C   1 
ATOM   1569  O O   . GLN B 2 3   ? 23.772  51.585  39.332  1.000 41.631  ? 3   GLN HHH O   1 
ATOM   1570  C CB  . GLN B 2 3   ? 23.688  50.345  42.384  1.000 62.515  ? 3   GLN HHH CB  1 
ATOM   1571  C CG  . GLN B 2 3   ? 24.492  49.291  41.631  1.000 73.397  ? 3   GLN HHH CG  1 
ATOM   1572  C CD  . GLN B 2 3   ? 25.480  48.568  42.516  1.000 85.198  ? 3   GLN HHH CD  1 
ATOM   1573  O OE1 . GLN B 2 3   ? 25.244  48.433  43.714  1.000 101.420 ? 3   GLN HHH OE1 1 
ATOM   1574  N NE2 . GLN B 2 3   ? 26.583  48.094  41.938  1.000 75.305  ? 3   GLN HHH NE2 1 
ATOM   1575  N N   . LEU B 2 4   ? 24.146  53.156  40.933  1.000 40.381  ? 4   LEU HHH N   1 
ATOM   1576  C CA  . LEU B 2 4   ? 24.912  54.140  40.116  1.000 39.962  ? 4   LEU HHH CA  1 
ATOM   1577  C C   . LEU B 2 4   ? 26.329  54.307  40.686  1.000 40.606  ? 4   LEU HHH C   1 
ATOM   1578  O O   . LEU B 2 4   ? 26.474  54.418  41.915  1.000 47.672  ? 4   LEU HHH O   1 
ATOM   1579  C CB  . LEU B 2 4   ? 24.178  55.479  40.180  1.000 40.134  ? 4   LEU HHH CB  1 
ATOM   1580  C CG  . LEU B 2 4   ? 23.328  55.879  38.984  1.000 38.153  ? 4   LEU HHH CG  1 
ATOM   1581  C CD1 . LEU B 2 4   ? 22.366  54.785  38.572  1.000 40.568  ? 4   LEU HHH CD1 1 
ATOM   1582  C CD2 . LEU B 2 4   ? 22.573  57.142  39.337  1.000 36.022  ? 4   LEU HHH CD2 1 
ATOM   1583  N N   . VAL B 2 5   ? 27.346  54.375  39.838  1.000 38.194  ? 5   VAL HHH N   1 
ATOM   1584  C CA  . VAL B 2 5   ? 28.762  54.446  40.296  1.000 37.774  ? 5   VAL HHH CA  1 
ATOM   1585  C C   . VAL B 2 5   ? 29.461  55.583  39.560  1.000 38.394  ? 5   VAL HHH C   1 
ATOM   1586  O O   . VAL B 2 5   ? 29.441  55.576  38.309  1.000 43.382  ? 5   VAL HHH O   1 
ATOM   1587  C CB  . VAL B 2 5   ? 29.475  53.109  40.070  1.000 36.299  ? 5   VAL HHH CB  1 
ATOM   1588  C CG1 . VAL B 2 5   ? 30.961  53.296  39.822  1.000 37.197  ? 5   VAL HHH CG1 1 
ATOM   1589  C CG2 . VAL B 2 5   ? 29.223  52.181  41.240  1.000 36.526  ? 5   VAL HHH CG2 1 
ATOM   1590  N N   . GLN B 2 6   ? 30.037  56.517  40.313  1.000 33.553  ? 6   GLN HHH N   1 
ATOM   1591  C CA  . GLN B 2 6   ? 30.592  57.750  39.728  1.000 33.306  ? 6   GLN HHH CA  1 
ATOM   1592  C C   . GLN B 2 6   ? 32.104  57.616  39.564  1.000 33.354  ? 6   GLN HHH C   1 
ATOM   1593  O O   . GLN B 2 6   ? 32.713  56.724  40.189  1.000 30.778  ? 6   GLN HHH O   1 
ATOM   1594  C CB  . GLN B 2 6   ? 30.269  58.965  40.587  1.000 35.502  ? 6   GLN HHH CB  1 
ATOM   1595  C CG  . GLN B 2 6   ? 28.801  59.091  40.945  1.000 35.633  ? 6   GLN HHH CG  1 
ATOM   1596  C CD  . GLN B 2 6   ? 28.440  60.463  41.475  1.000 35.450  ? 6   GLN HHH CD  1 
ATOM   1597  O OE1 . GLN B 2 6   ? 27.655  60.594  42.424  1.000 33.888  ? 6   GLN HHH OE1 1 
ATOM   1598  N NE2 . GLN B 2 6   ? 29.011  61.495  40.863  1.000 32.711  ? 6   GLN HHH NE2 1 
ATOM   1599  N N   . SER B 2 7   ? 32.661  58.484  38.719  1.000 34.097  ? 7   SER HHH N   1 
ATOM   1600  C CA  . SER B 2 7   ? 34.113  58.670  38.529  1.000 34.082  ? 7   SER HHH CA  1 
ATOM   1601  C C   . SER B 2 7   ? 34.724  59.085  39.881  1.000 34.979  ? 7   SER HHH C   1 
ATOM   1602  O O   . SER B 2 7   ? 33.972  59.492  40.821  1.000 34.072  ? 7   SER HHH O   1 
ATOM   1603  C CB  . SER B 2 7   ? 34.391  59.656  37.399  1.000 34.870  ? 7   SER HHH CB  1 
ATOM   1604  O OG  . SER B 2 7   ? 34.342  61.010  37.844  1.000 39.401  ? 7   SER HHH OG  1 
ATOM   1605  N N   . GLY B 2 8   ? 36.042  58.932  40.002  1.000 33.252  ? 8   GLY HHH N   1 
ATOM   1606  C CA  . GLY B 2 8   ? 36.786  59.214  41.237  1.000 31.283  ? 8   GLY HHH CA  1 
ATOM   1607  C C   . GLY B 2 8   ? 37.024  60.691  41.383  1.000 31.153  ? 8   GLY HHH C   1 
ATOM   1608  O O   . GLY B 2 8   ? 36.648  61.452  40.416  1.000 30.574  ? 8   GLY HHH O   1 
ATOM   1609  N N   . THR B 2 9   ? 37.621  61.056  42.527  1.000 30.949  ? 9   THR HHH N   1 
ATOM   1610  C CA  . THR B 2 9   ? 37.990  62.434  42.946  1.000 30.949  ? 9   THR HHH CA  1 
ATOM   1611  C C   . THR B 2 9   ? 38.761  63.155  41.835  1.000 33.464  ? 9   THR HHH C   1 
ATOM   1612  O O   . THR B 2 9   ? 39.619  62.536  41.225  1.000 38.931  ? 9   THR HHH O   1 
ATOM   1613  C CB  . THR B 2 9   ? 38.905  62.433  44.176  1.000 29.058  ? 9   THR HHH CB  1 
ATOM   1614  O OG1 . THR B 2 9   ? 38.335  61.637  45.205  1.000 26.770  ? 9   THR HHH OG1 1 
ATOM   1615  C CG2 . THR B 2 9   ? 39.195  63.822  44.695  1.000 30.470  ? 9   THR HHH CG2 1 
ATOM   1616  N N   . GLU B 2 10  ? 38.470  64.429  41.604  1.000 35.996  ? 10  GLU HHH N   1 
ATOM   1617  C CA  . GLU B 2 10  ? 39.209  65.289  40.657  1.000 36.774  ? 10  GLU HHH CA  1 
ATOM   1618  C C   . GLU B 2 10  ? 39.798  66.453  41.450  1.000 37.051  ? 10  GLU HHH C   1 
ATOM   1619  O O   . GLU B 2 10  ? 39.197  66.872  42.481  1.000 34.906  ? 10  GLU HHH O   1 
ATOM   1620  C CB  . GLU B 2 10  ? 38.273  65.753  39.551  1.000 40.625  ? 10  GLU HHH CB  1 
ATOM   1621  C CG  . GLU B 2 10  ? 37.549  64.604  38.863  1.000 46.857  ? 10  GLU HHH CG  1 
ATOM   1622  C CD  . GLU B 2 10  ? 38.270  63.962  37.683  1.000 52.685  ? 10  GLU HHH CD  1 
ATOM   1623  O OE1 . GLU B 2 10  ? 39.370  64.485  37.279  1.000 48.303  ? 10  GLU HHH OE1 1 
ATOM   1624  O OE2 . GLU B 2 10  ? 37.713  62.942  37.156  1.000 53.429  ? 10  GLU HHH OE2 1 
ATOM   1625  N N   . VAL B 2 11  ? 40.963  66.907  40.994  1.000 39.288  ? 11  VAL HHH N   1 
ATOM   1626  C CA  . VAL B 2 11  ? 41.659  68.132  41.480  1.000 38.089  ? 11  VAL HHH CA  1 
ATOM   1627  C C   . VAL B 2 11  ? 42.229  68.848  40.256  1.000 39.484  ? 11  VAL HHH C   1 
ATOM   1628  O O   . VAL B 2 11  ? 43.154  68.286  39.644  1.000 46.083  ? 11  VAL HHH O   1 
ATOM   1629  C CB  . VAL B 2 11  ? 42.761  67.799  42.494  1.000 34.114  ? 11  VAL HHH CB  1 
ATOM   1630  C CG1 . VAL B 2 11  ? 43.544  69.034  42.874  1.000 33.761  ? 11  VAL HHH CG1 1 
ATOM   1631  C CG2 . VAL B 2 11  ? 42.199  67.151  43.736  1.000 35.459  ? 11  VAL HHH CG2 1 
ATOM   1632  N N   . LYS B 2 12  ? 41.687  70.021  39.928  1.000 36.876  ? 12  LYS HHH N   1 
ATOM   1633  C CA  . LYS B 2 12  ? 41.993  70.753  38.680  1.000 37.194  ? 12  LYS HHH CA  1 
ATOM   1634  C C   . LYS B 2 12  ? 42.369  72.190  39.018  1.000 39.351  ? 12  LYS HHH C   1 
ATOM   1635  O O   . LYS B 2 12  ? 42.072  72.641  40.131  1.000 36.263  ? 12  LYS HHH O   1 
ATOM   1636  C CB  . LYS B 2 12  ? 40.777  70.741  37.759  1.000 37.626  ? 12  LYS HHH CB  1 
ATOM   1637  C CG  . LYS B 2 12  ? 40.057  69.408  37.677  1.000 40.274  ? 12  LYS HHH CG  1 
ATOM   1638  C CD  . LYS B 2 12  ? 40.824  68.344  36.945  1.000 41.484  ? 12  LYS HHH CD  1 
ATOM   1639  C CE  . LYS B 2 12  ? 40.875  68.600  35.455  1.000 42.740  ? 12  LYS HHH CE  1 
ATOM   1640  N NZ  . LYS B 2 12  ? 41.457  67.437  34.741  1.000 47.725  ? 12  LYS HHH NZ  1 
ATOM   1641  N N   . LYS B 2 13  ? 43.002  72.870  38.061  1.000 44.670  ? 13  LYS HHH N   1 
ATOM   1642  C CA  . LYS B 2 13  ? 43.330  74.314  38.144  1.000 45.398  ? 13  LYS HHH CA  1 
ATOM   1643  C C   . LYS B 2 13  ? 42.225  75.088  37.430  1.000 42.147  ? 13  LYS HHH C   1 
ATOM   1644  O O   . LYS B 2 13  ? 41.566  74.577  36.518  1.000 34.285  ? 13  LYS HHH O   1 
ATOM   1645  C CB  . LYS B 2 13  ? 44.696  74.595  37.507  1.000 49.114  ? 13  LYS HHH CB  1 
ATOM   1646  C CG  . LYS B 2 13  ? 45.839  73.693  37.961  1.000 48.990  ? 13  LYS HHH CG  1 
ATOM   1647  C CD  . LYS B 2 13  ? 46.204  73.888  39.412  1.000 52.024  ? 13  LYS HHH CD  1 
ATOM   1648  C CE  . LYS B 2 13  ? 47.509  74.623  39.623  1.000 53.234  ? 13  LYS HHH CE  1 
ATOM   1649  N NZ  . LYS B 2 13  ? 48.654  73.683  39.625  1.000 52.541  ? 13  LYS HHH NZ  1 
ATOM   1650  N N   . PRO B 2 14  ? 41.997  76.357  37.826  1.000 40.428  ? 14  PRO HHH N   1 
ATOM   1651  C CA  . PRO B 2 14  ? 41.027  77.197  37.136  1.000 41.811  ? 14  PRO HHH CA  1 
ATOM   1652  C C   . PRO B 2 14  ? 41.380  77.225  35.643  1.000 43.562  ? 14  PRO HHH C   1 
ATOM   1653  O O   . PRO B 2 14  ? 42.530  77.401  35.332  1.000 43.033  ? 14  PRO HHH O   1 
ATOM   1654  C CB  . PRO B 2 14  ? 41.149  78.572  37.809  1.000 40.999  ? 14  PRO HHH CB  1 
ATOM   1655  C CG  . PRO B 2 14  ? 41.787  78.273  39.158  1.000 42.123  ? 14  PRO HHH CG  1 
ATOM   1656  C CD  . PRO B 2 14  ? 42.654  77.045  38.948  1.000 41.657  ? 14  PRO HHH CD  1 
ATOM   1657  N N   . GLY B 2 15  ? 40.383  77.008  34.779  1.000 46.428  ? 15  GLY HHH N   1 
ATOM   1658  C CA  . GLY B 2 15  ? 40.496  77.114  33.316  1.000 47.408  ? 15  GLY HHH CA  1 
ATOM   1659  C C   . GLY B 2 15  ? 40.549  75.752  32.654  1.000 53.250  ? 15  GLY HHH C   1 
ATOM   1660  O O   . GLY B 2 15  ? 40.355  75.701  31.419  1.000 63.095  ? 15  GLY HHH O   1 
ATOM   1661  N N   . GLU B 2 16  ? 40.823  74.689  33.417  1.000 53.902  ? 16  GLU HHH N   1 
ATOM   1662  C CA  . GLU B 2 16  ? 40.890  73.309  32.873  1.000 51.901  ? 16  GLU HHH CA  1 
ATOM   1663  C C   . GLU B 2 16  ? 39.458  72.862  32.573  1.000 45.789  ? 16  GLU HHH C   1 
ATOM   1664  O O   . GLU B 2 16  ? 38.545  73.247  33.333  1.000 38.044  ? 16  GLU HHH O   1 
ATOM   1665  C CB  . GLU B 2 16  ? 41.605  72.367  33.847  1.000 58.967  ? 16  GLU HHH CB  1 
ATOM   1666  C CG  . GLU B 2 16  ? 43.095  72.644  34.018  1.000 61.885  ? 16  GLU HHH CG  1 
ATOM   1667  C CD  . GLU B 2 16  ? 43.897  71.677  34.893  1.000 63.871  ? 16  GLU HHH CD  1 
ATOM   1668  O OE1 . GLU B 2 16  ? 43.419  70.573  35.183  1.000 70.587  ? 16  GLU HHH OE1 1 
ATOM   1669  O OE2 . GLU B 2 16  ? 45.017  72.023  35.283  1.000 63.545  ? 16  GLU HHH OE2 1 
ATOM   1670  N N   . SER B 2 17  ? 39.269  72.122  31.480  1.000 47.292  ? 17  SER HHH N   1 
ATOM   1671  C CA  . SER B 2 17  ? 38.012  71.391  31.181  1.000 51.249  ? 17  SER HHH CA  1 
ATOM   1672  C C   . SER B 2 17  ? 37.915  70.214  32.151  1.000 49.875  ? 17  SER HHH C   1 
ATOM   1673  O O   . SER B 2 17  ? 38.952  69.809  32.676  1.000 50.095  ? 17  SER HHH O   1 
ATOM   1674  C CB  . SER B 2 17  ? 37.965  70.923  29.750  1.000 55.993  ? 17  SER HHH CB  1 
ATOM   1675  O OG  . SER B 2 17  ? 39.001  69.985  29.486  1.000 66.453  ? 17  SER HHH OG  1 
ATOM   1676  N N   . LEU B 2 18  ? 36.712  69.707  32.392  1.000 48.405  ? 18  LEU HHH N   1 
ATOM   1677  C CA  . LEU B 2 18  ? 36.498  68.484  33.192  1.000 44.976  ? 18  LEU HHH CA  1 
ATOM   1678  C C   . LEU B 2 18  ? 35.198  67.817  32.751  1.000 41.205  ? 18  LEU HHH C   1 
ATOM   1679  O O   . LEU B 2 18  ? 34.278  68.536  32.370  1.000 45.336  ? 18  LEU HHH O   1 
ATOM   1680  C CB  . LEU B 2 18  ? 36.453  68.871  34.671  1.000 44.139  ? 18  LEU HHH CB  1 
ATOM   1681  C CG  . LEU B 2 18  ? 36.120  67.721  35.621  1.000 44.861  ? 18  LEU HHH CG  1 
ATOM   1682  C CD1 . LEU B 2 18  ? 37.076  66.546  35.451  1.000 44.868  ? 18  LEU HHH CD1 1 
ATOM   1683  C CD2 . LEU B 2 18  ? 36.141  68.190  37.061  1.000 43.463  ? 18  LEU HHH CD2 1 
ATOM   1684  N N   . LYS B 2 19  ? 35.160  66.493  32.754  1.000 38.684  ? 19  LYS HHH N   1 
ATOM   1685  C CA  . LYS B 2 19  ? 33.950  65.693  32.449  1.000 38.531  ? 19  LYS HHH CA  1 
ATOM   1686  C C   . LYS B 2 19  ? 33.945  64.527  33.422  1.000 37.831  ? 19  LYS HHH C   1 
ATOM   1687  O O   . LYS B 2 19  ? 34.755  63.622  33.233  1.000 41.443  ? 19  LYS HHH O   1 
ATOM   1688  C CB  . LYS B 2 19  ? 33.949  65.211  30.992  1.000 41.819  ? 19  LYS HHH CB  1 
ATOM   1689  C CG  . LYS B 2 19  ? 32.923  64.141  30.646  1.000 45.932  ? 19  LYS HHH CG  1 
ATOM   1690  C CD  . LYS B 2 19  ? 32.267  64.328  29.294  1.000 50.743  ? 19  LYS HHH CD  1 
ATOM   1691  C CE  . LYS B 2 19  ? 32.740  63.382  28.213  1.000 52.403  ? 19  LYS HHH CE  1 
ATOM   1692  N NZ  . LYS B 2 19  ? 31.973  63.666  26.978  1.000 56.820  ? 19  LYS HHH NZ  1 
ATOM   1693  N N   . ILE B 2 20  ? 33.082  64.573  34.434  1.000 37.896  ? 20  ILE HHH N   1 
ATOM   1694  C CA  . ILE B 2 20  ? 32.892  63.455  35.402  1.000 37.763  ? 20  ILE HHH CA  1 
ATOM   1695  C C   . ILE B 2 20  ? 31.761  62.567  34.895  1.000 37.087  ? 20  ILE HHH C   1 
ATOM   1696  O O   . ILE B 2 20  ? 30.984  63.021  34.036  1.000 36.218  ? 20  ILE HHH O   1 
ATOM   1697  C CB  . ILE B 2 20  ? 32.633  63.984  36.817  1.000 36.819  ? 20  ILE HHH CB  1 
ATOM   1698  C CG1 . ILE B 2 20  ? 31.186  64.410  37.020  1.000 37.302  ? 20  ILE HHH CG1 1 
ATOM   1699  C CG2 . ILE B 2 20  ? 33.593  65.119  37.138  1.000 36.686  ? 20  ILE HHH CG2 1 
ATOM   1700  C CD1 . ILE B 2 20  ? 30.908  64.831  38.437  1.000 40.664  ? 20  ILE HHH CD1 1 
ATOM   1701  N N   . SER B 2 21  ? 31.696  61.338  35.389  1.000 39.961  ? 21  SER HHH N   1 
ATOM   1702  C CA  . SER B 2 21  ? 30.783  60.301  34.846  1.000 43.969  ? 21  SER HHH CA  1 
ATOM   1703  C C   . SER B 2 21  ? 30.028  59.616  35.987  1.000 41.722  ? 21  SER HHH C   1 
ATOM   1704  O O   . SER B 2 21  ? 30.370  59.867  37.176  1.000 39.561  ? 21  SER HHH O   1 
ATOM   1705  C CB  . SER B 2 21  ? 31.513  59.308  33.982  1.000 43.981  ? 21  SER HHH CB  1 
ATOM   1706  O OG  . SER B 2 21  ? 32.448  58.598  34.773  1.000 45.633  ? 21  SER HHH OG  1 
ATOM   1707  N N   . CYS B 2 22  ? 29.013  58.847  35.578  1.000 39.218  ? 22  CYS HHH N   1 
ATOM   1708  C CA  . CYS B 2 22  ? 27.972  58.165  36.387  1.000 41.037  ? 22  CYS HHH CA  1 
ATOM   1709  C C   . CYS B 2 22  ? 27.395  57.050  35.517  1.000 40.489  ? 22  CYS HHH C   1 
ATOM   1710  O O   . CYS B 2 22  ? 26.686  57.353  34.556  1.000 39.374  ? 22  CYS HHH O   1 
ATOM   1711  C CB  . CYS B 2 22  ? 26.865  59.125  36.816  1.000 42.849  ? 22  CYS HHH CB  1 
ATOM   1712  S SG  . CYS B 2 22  ? 25.542  58.368  37.791  1.000 42.875  ? 22  CYS HHH SG  1 
ATOM   1713  N N   . LYS B 2 23  ? 27.771  55.816  35.817  1.000 45.111  ? 23  LYS HHH N   1 
ATOM   1714  C CA  . LYS B 2 23  ? 27.357  54.611  35.072  1.000 48.954  ? 23  LYS HHH CA  1 
ATOM   1715  C C   . LYS B 2 23  ? 26.435  53.803  35.983  1.000 52.014  ? 23  LYS HHH C   1 
ATOM   1716  O O   . LYS B 2 23  ? 26.747  53.663  37.190  1.000 51.647  ? 23  LYS HHH O   1 
ATOM   1717  C CB  . LYS B 2 23  ? 28.571  53.800  34.617  1.000 53.697  ? 23  LYS HHH CB  1 
ATOM   1718  C CG  . LYS B 2 23  ? 28.241  52.433  34.039  1.000 59.636  ? 23  LYS HHH CG  1 
ATOM   1719  C CD  . LYS B 2 23  ? 29.426  51.699  33.462  1.000 63.121  ? 23  LYS HHH CD  1 
ATOM   1720  C CE  . LYS B 2 23  ? 29.011  50.341  32.948  1.000 70.949  ? 23  LYS HHH CE  1 
ATOM   1721  N NZ  . LYS B 2 23  ? 29.952  49.855  31.919  1.000 78.799  ? 23  LYS HHH NZ  1 
ATOM   1722  N N   . GLY B 2 24  ? 25.332  53.315  35.410  1.000 50.679  ? 24  GLY HHH N   1 
ATOM   1723  C CA  . GLY B 2 24  ? 24.319  52.516  36.110  1.000 48.303  ? 24  GLY HHH CA  1 
ATOM   1724  C C   . GLY B 2 24  ? 24.401  51.071  35.696  1.000 47.354  ? 24  GLY HHH C   1 
ATOM   1725  O O   . GLY B 2 24  ? 24.560  50.812  34.504  1.000 42.266  ? 24  GLY HHH O   1 
ATOM   1726  N N   . SER B 2 25  ? 24.336  50.179  36.677  1.000 54.301  ? 25  SER HHH N   1 
ATOM   1727  C CA  . SER B 2 25  ? 24.384  48.710  36.510  1.000 62.385  ? 25  SER HHH CA  1 
ATOM   1728  C C   . SER B 2 25  ? 23.229  48.114  37.312  1.000 64.233  ? 25  SER HHH C   1 
ATOM   1729  O O   . SER B 2 25  ? 22.954  48.606  38.424  1.000 60.063  ? 25  SER HHH O   1 
ATOM   1730  C CB  . SER B 2 25  ? 25.737  48.137  36.914  1.000 66.867  ? 25  SER HHH CB  1 
ATOM   1731  O OG  . SER B 2 25  ? 25.995  48.330  38.297  1.000 76.805  ? 25  SER HHH OG  1 
ATOM   1732  N N   . GLY B 2 26  ? 22.592  47.082  36.756  1.000 71.759  ? 26  GLY HHH N   1 
ATOM   1733  C CA  . GLY B 2 26  ? 21.351  46.488  37.279  1.000 74.918  ? 26  GLY HHH CA  1 
ATOM   1734  C C   . GLY B 2 26  ? 20.280  46.499  36.213  1.000 75.214  ? 26  GLY HHH C   1 
ATOM   1735  O O   . GLY B 2 26  ? 20.311  47.378  35.323  1.000 77.539  ? 26  GLY HHH O   1 
ATOM   1736  N N   . TYR B 2 27  ? 19.373  45.536  36.262  1.000 83.449  ? 27  TYR HHH N   1 
ATOM   1737  C CA  . TYR B 2 27  ? 18.219  45.512  35.335  1.000 95.547  ? 27  TYR HHH CA  1 
ATOM   1738  C C   . TYR B 2 27  ? 17.224  46.565  35.811  1.000 80.896  ? 27  TYR HHH C   1 
ATOM   1739  O O   . TYR B 2 27  ? 17.213  46.932  37.006  1.000 64.238  ? 27  TYR HHH O   1 
ATOM   1740  C CB  . TYR B 2 27  ? 17.587  44.124  35.164  1.000 112.209 ? 27  TYR HHH CB  1 
ATOM   1741  C CG  . TYR B 2 27  ? 17.701  43.196  36.343  1.000 111.984 ? 27  TYR HHH CG  1 
ATOM   1742  C CD1 . TYR B 2 27  ? 17.062  43.480  37.540  1.000 109.039 ? 27  TYR HHH CD1 1 
ATOM   1743  C CD2 . TYR B 2 27  ? 18.453  42.031  36.250  1.000 103.643 ? 27  TYR HHH CD2 1 
ATOM   1744  C CE1 . TYR B 2 27  ? 17.166  42.618  38.621  1.000 110.575 ? 27  TYR HHH CE1 1 
ATOM   1745  C CE2 . TYR B 2 27  ? 18.566  41.160  37.321  1.000 103.455 ? 27  TYR HHH CE2 1 
ATOM   1746  C CZ  . TYR B 2 27  ? 17.920  41.458  38.510  1.000 111.213 ? 27  TYR HHH CZ  1 
ATOM   1747  O OH  . TYR B 2 27  ? 18.020  40.613  39.576  1.000 109.158 ? 27  TYR HHH OH  1 
ATOM   1748  N N   . GLY B 2 28  ? 16.444  47.041  34.843  1.000 75.076  ? 28  GLY HHH N   1 
ATOM   1749  C CA  . GLY B 2 28  ? 15.481  48.134  34.983  1.000 64.111  ? 28  GLY HHH CA  1 
ATOM   1750  C C   . GLY B 2 28  ? 16.124  49.448  34.619  1.000 59.156  ? 28  GLY HHH C   1 
ATOM   1751  O O   . GLY B 2 28  ? 15.697  50.428  35.198  1.000 56.956  ? 28  GLY HHH O   1 
ATOM   1752  N N   . PHE B 2 29  ? 17.102  49.493  33.703  1.000 55.239  ? 29  PHE HHH N   1 
ATOM   1753  C CA  . PHE B 2 29  ? 17.852  50.755  33.470  1.000 54.967  ? 29  PHE HHH CA  1 
ATOM   1754  C C   . PHE B 2 29  ? 17.212  51.624  32.385  1.000 55.977  ? 29  PHE HHH C   1 
ATOM   1755  O O   . PHE B 2 29  ? 17.348  52.852  32.497  1.000 55.986  ? 29  PHE HHH O   1 
ATOM   1756  C CB  . PHE B 2 29  ? 19.324  50.535  33.126  1.000 55.662  ? 29  PHE HHH CB  1 
ATOM   1757  C CG  . PHE B 2 29  ? 20.079  51.844  33.028  1.000 51.946  ? 29  PHE HHH CG  1 
ATOM   1758  C CD1 . PHE B 2 29  ? 20.396  52.576  34.163  1.000 47.345  ? 29  PHE HHH CD1 1 
ATOM   1759  C CD2 . PHE B 2 29  ? 20.388  52.399  31.795  1.000 52.410  ? 29  PHE HHH CD2 1 
ATOM   1760  C CE1 . PHE B 2 29  ? 21.045  53.797  34.073  1.000 43.141  ? 29  PHE HHH CE1 1 
ATOM   1761  C CE2 . PHE B 2 29  ? 21.037  53.622  31.702  1.000 49.092  ? 29  PHE HHH CE2 1 
ATOM   1762  C CZ  . PHE B 2 29  ? 21.370  54.312  32.842  1.000 45.353  ? 29  PHE HHH CZ  1 
ATOM   1763  N N   . ILE B 2 30  ? 16.583  51.033  31.363  1.000 60.961  ? 30  ILE HHH N   1 
ATOM   1764  C CA  . ILE B 2 30  ? 15.984  51.772  30.199  1.000 57.261  ? 30  ILE HHH CA  1 
ATOM   1765  C C   . ILE B 2 30  ? 15.050  52.863  30.735  1.000 52.403  ? 30  ILE HHH C   1 
ATOM   1766  O O   . ILE B 2 30  ? 14.938  53.903  30.066  1.000 52.426  ? 30  ILE HHH O   1 
ATOM   1767  C CB  . ILE B 2 30  ? 15.282  50.802  29.217  1.000 56.499  ? 30  ILE HHH CB  1 
ATOM   1768  C CG1 . ILE B 2 30  ? 16.298  49.783  28.657  1.000 67.523  ? 30  ILE HHH CG1 1 
ATOM   1769  C CG2 . ILE B 2 30  ? 14.555  51.556  28.111  1.000 48.760  ? 30  ILE HHH CG2 1 
ATOM   1770  C CD1 . ILE B 2 30  ? 15.737  48.671  27.754  1.000 66.448  ? 30  ILE HHH CD1 1 
ATOM   1771  N N   . THR B 2 31  ? 14.487  52.649  31.929  1.000 48.632  ? 31  THR HHH N   1 
ATOM   1772  C CA  . THR B 2 31  ? 13.448  53.486  32.594  1.000 50.083  ? 31  THR HHH CA  1 
ATOM   1773  C C   . THR B 2 31  ? 14.038  54.719  33.319  1.000 51.849  ? 31  THR HHH C   1 
ATOM   1774  O O   . THR B 2 31  ? 13.286  55.722  33.462  1.000 53.871  ? 31  THR HHH O   1 
ATOM   1775  C CB  . THR B 2 31  ? 12.620  52.633  33.569  1.000 49.390  ? 31  THR HHH CB  1 
ATOM   1776  O OG1 . THR B 2 31  ? 11.933  53.493  34.466  1.000 53.022  ? 31  THR HHH OG1 1 
ATOM   1777  C CG2 . THR B 2 31  ? 13.428  51.728  34.464  1.000 49.678  ? 31  THR HHH CG2 1 
ATOM   1778  N N   . TYR B 2 32  ? 15.308  54.676  33.757  1.000 50.728  ? 32  TYR HHH N   1 
ATOM   1779  C CA  . TYR B 2 32  ? 15.900  55.635  34.733  1.000 43.566  ? 32  TYR HHH CA  1 
ATOM   1780  C C   . TYR B 2 32  ? 16.274  56.944  34.050  1.000 40.649  ? 32  TYR HHH C   1 
ATOM   1781  O O   . TYR B 2 32  ? 16.956  56.936  33.018  1.000 36.475  ? 32  TYR HHH O   1 
ATOM   1782  C CB  . TYR B 2 32  ? 17.112  55.040  35.467  1.000 43.368  ? 32  TYR HHH CB  1 
ATOM   1783  C CG  . TYR B 2 32  ? 16.734  54.355  36.753  1.000 41.287  ? 32  TYR HHH CG  1 
ATOM   1784  C CD1 . TYR B 2 32  ? 16.500  55.079  37.910  1.000 41.999  ? 32  TYR HHH CD1 1 
ATOM   1785  C CD2 . TYR B 2 32  ? 16.485  52.996  36.786  1.000 42.052  ? 32  TYR HHH CD2 1 
ATOM   1786  C CE1 . TYR B 2 32  ? 16.075  54.463  39.077  1.000 42.613  ? 32  TYR HHH CE1 1 
ATOM   1787  C CE2 . TYR B 2 32  ? 16.055  52.361  37.944  1.000 44.272  ? 32  TYR HHH CE2 1 
ATOM   1788  C CZ  . TYR B 2 32  ? 15.856  53.098  39.096  1.000 44.448  ? 32  TYR HHH CZ  1 
ATOM   1789  O OH  . TYR B 2 32  ? 15.435  52.501  40.249  1.000 47.986  ? 32  TYR HHH OH  1 
ATOM   1790  N N   . TRP B 2 33  ? 15.814  58.035  34.654  1.000 43.871  ? 33  TRP HHH N   1 
ATOM   1791  C CA  . TRP B 2 33  ? 16.203  59.441  34.358  1.000 45.570  ? 33  TRP HHH CA  1 
ATOM   1792  C C   . TRP B 2 33  ? 17.290  59.867  35.345  1.000 41.132  ? 33  TRP HHH C   1 
ATOM   1793  O O   . TRP B 2 33  ? 17.018  59.830  36.558  1.000 41.322  ? 33  TRP HHH O   1 
ATOM   1794  C CB  . TRP B 2 33  ? 14.996  60.383  34.486  1.000 49.744  ? 33  TRP HHH CB  1 
ATOM   1795  C CG  . TRP B 2 33  ? 13.941  60.221  33.438  1.000 51.015  ? 33  TRP HHH CG  1 
ATOM   1796  C CD1 . TRP B 2 33  ? 13.101  59.159  33.255  1.000 53.009  ? 33  TRP HHH CD1 1 
ATOM   1797  C CD2 . TRP B 2 33  ? 13.594  61.200  32.450  1.000 51.341  ? 33  TRP HHH CD2 1 
ATOM   1798  N NE1 . TRP B 2 33  ? 12.285  59.395  32.187  1.000 56.321  ? 33  TRP HHH NE1 1 
ATOM   1799  C CE2 . TRP B 2 33  ? 12.560  60.645  31.679  1.000 54.936  ? 33  TRP HHH CE2 1 
ATOM   1800  C CE3 . TRP B 2 33  ? 14.063  62.482  32.145  1.000 51.243  ? 33  TRP HHH CE3 1 
ATOM   1801  C CZ2 . TRP B 2 33  ? 11.994  61.340  30.610  1.000 54.047  ? 33  TRP HHH CZ2 1 
ATOM   1802  C CZ3 . TRP B 2 33  ? 13.508  63.166  31.089  1.000 49.765  ? 33  TRP HHH CZ3 1 
ATOM   1803  C CH2 . TRP B 2 33  ? 12.482  62.597  30.336  1.000 52.839  ? 33  TRP HHH CH2 1 
ATOM   1804  N N   . ILE B 2 34  ? 18.431  60.338  34.849  1.000 39.064  ? 34  ILE HHH N   1 
ATOM   1805  C CA  . ILE B 2 34  ? 19.650  60.561  35.679  1.000 39.074  ? 34  ILE HHH CA  1 
ATOM   1806  C C   . ILE B 2 34  ? 19.938  62.053  35.843  1.000 36.945  ? 34  ILE HHH C   1 
ATOM   1807  O O   . ILE B 2 34  ? 20.219  62.736  34.856  1.000 40.238  ? 34  ILE HHH O   1 
ATOM   1808  C CB  . ILE B 2 34  ? 20.832  59.811  35.067  1.000 41.895  ? 34  ILE HHH CB  1 
ATOM   1809  C CG1 . ILE B 2 34  ? 20.630  58.308  35.256  1.000 44.968  ? 34  ILE HHH CG1 1 
ATOM   1810  C CG2 . ILE B 2 34  ? 22.147  60.314  35.650  1.000 42.063  ? 34  ILE HHH CG2 1 
ATOM   1811  C CD1 . ILE B 2 34  ? 21.562  57.480  34.431  1.000 48.929  ? 34  ILE HHH CD1 1 
ATOM   1812  N N   . GLY B 2 35  ? 19.882  62.522  37.081  1.000 36.218  ? 35  GLY HHH N   1 
ATOM   1813  C CA  . GLY B 2 35  ? 20.078  63.933  37.432  1.000 36.876  ? 35  GLY HHH CA  1 
ATOM   1814  C C   . GLY B 2 35  ? 21.391  64.135  38.157  1.000 37.757  ? 35  GLY HHH C   1 
ATOM   1815  O O   . GLY B 2 35  ? 22.015  63.159  38.603  1.000 37.686  ? 35  GLY HHH O   1 
ATOM   1816  N N   . TRP B 2 36  ? 21.810  65.383  38.230  1.000 36.770  ? 36  TRP HHH N   1 
ATOM   1817  C CA  . TRP B 2 36  ? 23.078  65.811  38.851  1.000 34.917  ? 36  TRP HHH CA  1 
ATOM   1818  C C   . TRP B 2 36  ? 22.704  66.805  39.942  1.000 33.541  ? 36  TRP HHH C   1 
ATOM   1819  O O   . TRP B 2 36  ? 21.942  67.724  39.671  1.000 36.449  ? 36  TRP HHH O   1 
ATOM   1820  C CB  . TRP B 2 36  ? 24.006  66.422  37.792  1.000 36.971  ? 36  TRP HHH CB  1 
ATOM   1821  C CG  . TRP B 2 36  ? 24.596  65.408  36.861  1.000 36.287  ? 36  TRP HHH CG  1 
ATOM   1822  C CD1 . TRP B 2 36  ? 24.207  65.097  35.593  1.000 38.174  ? 36  TRP HHH CD1 1 
ATOM   1823  C CD2 . TRP B 2 36  ? 25.688  64.538  37.159  1.000 36.420  ? 36  TRP HHH CD2 1 
ATOM   1824  N NE1 . TRP B 2 36  ? 24.982  64.094  35.081  1.000 38.857  ? 36  TRP HHH NE1 1 
ATOM   1825  C CE2 . TRP B 2 36  ? 25.911  63.739  36.016  1.000 38.216  ? 36  TRP HHH CE2 1 
ATOM   1826  C CE3 . TRP B 2 36  ? 26.496  64.367  38.285  1.000 36.113  ? 36  TRP HHH CE3 1 
ATOM   1827  C CZ2 . TRP B 2 36  ? 26.917  62.779  35.962  1.000 37.247  ? 36  TRP HHH CZ2 1 
ATOM   1828  C CZ3 . TRP B 2 36  ? 27.484  63.415  38.237  1.000 37.967  ? 36  TRP HHH CZ3 1 
ATOM   1829  C CH2 . TRP B 2 36  ? 27.698  62.641  37.089  1.000 38.749  ? 36  TRP HHH CH2 1 
ATOM   1830  N N   . VAL B 2 37  ? 23.210  66.606  41.145  1.000 33.932  ? 37  VAL HHH N   1 
ATOM   1831  C CA  . VAL B 2 37  ? 23.002  67.522  42.298  1.000 34.229  ? 37  VAL HHH CA  1 
ATOM   1832  C C   . VAL B 2 37  ? 24.376  68.017  42.744  1.000 35.044  ? 37  VAL HHH C   1 
ATOM   1833  O O   . VAL B 2 37  ? 25.309  67.209  42.803  1.000 36.034  ? 37  VAL HHH O   1 
ATOM   1834  C CB  . VAL B 2 37  ? 22.279  66.775  43.428  1.000 33.771  ? 37  VAL HHH CB  1 
ATOM   1835  C CG1 . VAL B 2 37  ? 22.125  67.635  44.668  1.000 35.297  ? 37  VAL HHH CG1 1 
ATOM   1836  C CG2 . VAL B 2 37  ? 20.951  66.220  42.951  1.000 33.202  ? 37  VAL HHH CG2 1 
ATOM   1837  N N   . ARG B 2 38  ? 24.501  69.296  43.059  1.000 36.535  ? 38  ARG HHH N   1 
ATOM   1838  C CA  . ARG B 2 38  ? 25.766  69.859  43.577  1.000 40.221  ? 38  ARG HHH CA  1 
ATOM   1839  C C   . ARG B 2 38  ? 25.626  70.155  45.063  1.000 39.495  ? 38  ARG HHH C   1 
ATOM   1840  O O   . ARG B 2 38  ? 24.603  70.719  45.458  1.000 43.124  ? 38  ARG HHH O   1 
ATOM   1841  C CB  . ARG B 2 38  ? 26.153  71.137  42.836  1.000 44.373  ? 38  ARG HHH CB  1 
ATOM   1842  C CG  . ARG B 2 38  ? 27.416  71.751  43.399  1.000 48.203  ? 38  ARG HHH CG  1 
ATOM   1843  C CD  . ARG B 2 38  ? 27.812  72.974  42.620  1.000 51.990  ? 38  ARG HHH CD  1 
ATOM   1844  N NE  . ARG B 2 38  ? 26.985  74.096  43.012  1.000 52.538  ? 38  ARG HHH NE  1 
ATOM   1845  C CZ  . ARG B 2 38  ? 27.076  75.285  42.456  1.000 53.320  ? 38  ARG HHH CZ  1 
ATOM   1846  N NH1 . ARG B 2 38  ? 27.993  75.510  41.529  1.000 55.687  ? 38  ARG HHH NH1 1 
ATOM   1847  N NH2 . ARG B 2 38  ? 26.262  76.246  42.842  1.000 54.277  ? 38  ARG HHH NH2 1 
ATOM   1848  N N   . GLN B 2 39  ? 26.646  69.803  45.841  1.000 41.147  ? 39  GLN HHH N   1 
ATOM   1849  C CA  . GLN B 2 39  ? 26.715  70.131  47.284  1.000 43.315  ? 39  GLN HHH CA  1 
ATOM   1850  C C   . GLN B 2 39  ? 28.061  70.786  47.575  1.000 49.828  ? 39  GLN HHH C   1 
ATOM   1851  O O   . GLN B 2 39  ? 29.085  70.071  47.617  1.000 48.343  ? 39  GLN HHH O   1 
ATOM   1852  C CB  . GLN B 2 39  ? 26.533  68.897  48.155  1.000 39.342  ? 39  GLN HHH CB  1 
ATOM   1853  C CG  . GLN B 2 39  ? 26.484  69.243  49.627  1.000 39.241  ? 39  GLN HHH CG  1 
ATOM   1854  C CD  . GLN B 2 39  ? 26.080  68.041  50.436  1.000 42.102  ? 39  GLN HHH CD  1 
ATOM   1855  O OE1 . GLN B 2 39  ? 25.251  68.143  51.338  1.000 41.697  ? 39  GLN HHH OE1 1 
ATOM   1856  N NE2 . GLN B 2 39  ? 26.656  66.894  50.103  1.000 38.406  ? 39  GLN HHH NE2 1 
ATOM   1857  N N   . MET B 2 40  ? 28.048  72.103  47.775  1.000 54.376  ? 40  MET HHH N   1 
ATOM   1858  C CA  . MET B 2 40  ? 29.279  72.863  48.084  1.000 49.199  ? 40  MET HHH CA  1 
ATOM   1859  C C   . MET B 2 40  ? 29.678  72.572  49.522  1.000 43.653  ? 40  MET HHH C   1 
ATOM   1860  O O   . MET B 2 40  ? 28.870  72.147  50.327  1.000 41.656  ? 40  MET HHH O   1 
ATOM   1861  C CB  . MET B 2 40  ? 29.064  74.357  47.859  1.000 52.567  ? 40  MET HHH CB  1 
ATOM   1862  C CG  . MET B 2 40  ? 28.909  74.665  46.385  1.000 55.941  ? 40  MET HHH CG  1 
ATOM   1863  S SD  . MET B 2 40  ? 28.643  76.408  46.066  1.000 59.513  ? 40  MET HHH SD  1 
ATOM   1864  C CE  . MET B 2 40  ? 29.330  76.524  44.413  1.000 65.271  ? 40  MET HHH CE  1 
ATOM   1865  N N   . PRO B 2 41  ? 30.962  72.742  49.860  1.000 44.444  ? 41  PRO HHH N   1 
ATOM   1866  C CA  . PRO B 2 41  ? 31.447  72.420  51.193  1.000 44.912  ? 41  PRO HHH CA  1 
ATOM   1867  C C   . PRO B 2 41  ? 30.674  73.185  52.270  1.000 46.953  ? 41  PRO HHH C   1 
ATOM   1868  O O   . PRO B 2 41  ? 30.724  74.422  52.280  1.000 43.270  ? 41  PRO HHH O   1 
ATOM   1869  C CB  . PRO B 2 41  ? 32.916  72.861  51.148  1.000 45.636  ? 41  PRO HHH CB  1 
ATOM   1870  C CG  . PRO B 2 41  ? 33.280  72.808  49.669  1.000 44.236  ? 41  PRO HHH CG  1 
ATOM   1871  C CD  . PRO B 2 41  ? 32.021  73.233  48.960  1.000 45.903  ? 41  PRO HHH CD  1 
ATOM   1872  N N   . GLY B 2 42  ? 29.999  72.420  53.139  1.000 49.121  ? 42  GLY HHH N   1 
ATOM   1873  C CA  . GLY B 2 42  ? 29.246  72.915  54.305  1.000 47.512  ? 42  GLY HHH CA  1 
ATOM   1874  C C   . GLY B 2 42  ? 27.843  73.343  53.924  1.000 48.272  ? 42  GLY HHH C   1 
ATOM   1875  O O   . GLY B 2 42  ? 27.115  73.733  54.820  1.000 53.474  ? 42  GLY HHH O   1 
ATOM   1876  N N   . LYS B 2 43  ? 27.473  73.289  52.643  1.000 48.177  ? 43  LYS HHH N   1 
ATOM   1877  C CA  . LYS B 2 43  ? 26.174  73.807  52.147  1.000 49.678  ? 43  LYS HHH CA  1 
ATOM   1878  C C   . LYS B 2 43  ? 25.204  72.654  51.922  1.000 49.923  ? 43  LYS HHH C   1 
ATOM   1879  O O   . LYS B 2 43  ? 25.624  71.489  52.051  1.000 51.787  ? 43  LYS HHH O   1 
ATOM   1880  C CB  . LYS B 2 43  ? 26.345  74.557  50.825  1.000 53.096  ? 43  LYS HHH CB  1 
ATOM   1881  C CG  . LYS B 2 43  ? 27.449  75.592  50.830  1.000 57.857  ? 43  LYS HHH CG  1 
ATOM   1882  C CD  . LYS B 2 43  ? 27.354  76.584  51.981  1.000 58.083  ? 43  LYS HHH CD  1 
ATOM   1883  C CE  . LYS B 2 43  ? 28.346  77.717  51.837  1.000 59.579  ? 43  LYS HHH CE  1 
ATOM   1884  N NZ  . LYS B 2 43  ? 27.697  79.046  51.979  1.000 62.184  ? 43  LYS HHH NZ  1 
ATOM   1885  N N   . GLY B 2 44  ? 23.968  73.001  51.564  1.000 48.757  ? 44  GLY HHH N   1 
ATOM   1886  C CA  . GLY B 2 44  ? 22.929  72.048  51.152  1.000 47.391  ? 44  GLY HHH CA  1 
ATOM   1887  C C   . GLY B 2 44  ? 23.053  71.642  49.693  1.000 44.343  ? 44  GLY HHH C   1 
ATOM   1888  O O   . GLY B 2 44  ? 24.015  72.085  48.996  1.000 43.122  ? 44  GLY HHH O   1 
ATOM   1889  N N   . LEU B 2 45  ? 22.070  70.848  49.264  1.000 42.568  ? 45  LEU HHH N   1 
ATOM   1890  C CA  . LEU B 2 45  ? 21.922  70.240  47.916  1.000 41.312  ? 45  LEU HHH CA  1 
ATOM   1891  C C   . LEU B 2 45  ? 21.312  71.272  46.972  1.000 40.277  ? 45  LEU HHH C   1 
ATOM   1892  O O   . LEU B 2 45  ? 20.498  72.076  47.436  1.000 41.674  ? 45  LEU HHH O   1 
ATOM   1893  C CB  . LEU B 2 45  ? 21.001  69.021  48.027  1.000 41.958  ? 45  LEU HHH CB  1 
ATOM   1894  C CG  . LEU B 2 45  ? 21.385  68.007  49.095  1.000 41.902  ? 45  LEU HHH CG  1 
ATOM   1895  C CD1 . LEU B 2 45  ? 20.337  66.907  49.188  1.000 41.305  ? 45  LEU HHH CD1 1 
ATOM   1896  C CD2 . LEU B 2 45  ? 22.766  67.432  48.806  1.000 42.988  ? 45  LEU HHH CD2 1 
ATOM   1897  N N   . GLU B 2 46  ? 21.718  71.245  45.706  1.000 40.399  ? 46  GLU HHH N   1 
ATOM   1898  C CA  . GLU B 2 46  ? 21.241  72.138  44.619  1.000 41.478  ? 46  GLU HHH CA  1 
ATOM   1899  C C   . GLU B 2 46  ? 21.057  71.264  43.378  1.000 40.095  ? 46  GLU HHH C   1 
ATOM   1900  O O   . GLU B 2 46  ? 22.045  70.663  42.930  1.000 38.967  ? 46  GLU HHH O   1 
ATOM   1901  C CB  . GLU B 2 46  ? 22.242  73.264  44.331  1.000 45.056  ? 46  GLU HHH CB  1 
ATOM   1902  C CG  . GLU B 2 46  ? 22.823  73.930  45.574  1.000 53.576  ? 46  GLU HHH CG  1 
ATOM   1903  C CD  . GLU B 2 46  ? 24.168  74.618  45.375  1.000 60.111  ? 46  GLU HHH CD  1 
ATOM   1904  O OE1 . GLU B 2 46  ? 24.275  75.377  44.372  1.000 58.542  ? 46  GLU HHH OE1 1 
ATOM   1905  O OE2 . GLU B 2 46  ? 25.110  74.373  46.206  1.000 59.148  ? 46  GLU HHH OE2 1 
ATOM   1906  N N   . TRP B 2 47  ? 19.838  71.146  42.863  1.000 41.235  ? 47  TRP HHH N   1 
ATOM   1907  C CA  . TRP B 2 47  ? 19.564  70.321  41.658  1.000 39.675  ? 47  TRP HHH CA  1 
ATOM   1908  C C   . TRP B 2 47  ? 20.075  71.066  40.426  1.000 36.466  ? 47  TRP HHH C   1 
ATOM   1909  O O   . TRP B 2 47  ? 19.724  72.235  40.265  1.000 40.148  ? 47  TRP HHH O   1 
ATOM   1910  C CB  . TRP B 2 47  ? 18.072  70.002  41.574  1.000 42.228  ? 47  TRP HHH CB  1 
ATOM   1911  C CG  . TRP B 2 47  ? 17.691  69.098  40.444  1.000 45.899  ? 47  TRP HHH CG  1 
ATOM   1912  C CD1 . TRP B 2 47  ? 17.665  67.732  40.439  1.000 46.371  ? 47  TRP HHH CD1 1 
ATOM   1913  C CD2 . TRP B 2 47  ? 17.215  69.516  39.152  1.000 50.567  ? 47  TRP HHH CD2 1 
ATOM   1914  N NE1 . TRP B 2 47  ? 17.244  67.273  39.218  1.000 50.172  ? 47  TRP HHH NE1 1 
ATOM   1915  C CE2 . TRP B 2 47  ? 16.948  68.343  38.411  1.000 49.819  ? 47  TRP HHH CE2 1 
ATOM   1916  C CE3 . TRP B 2 47  ? 16.988  70.766  38.557  1.000 50.696  ? 47  TRP HHH CE3 1 
ATOM   1917  C CZ2 . TRP B 2 47  ? 16.454  68.390  37.107  1.000 47.048  ? 47  TRP HHH CZ2 1 
ATOM   1918  C CZ3 . TRP B 2 47  ? 16.511  70.807  37.265  1.000 50.728  ? 47  TRP HHH CZ3 1 
ATOM   1919  C CH2 . TRP B 2 47  ? 16.240  69.633  36.556  1.000 49.010  ? 47  TRP HHH CH2 1 
ATOM   1920  N N   . MET B 2 48  ? 20.898  70.421  39.613  1.000 34.726  ? 48  MET HHH N   1 
ATOM   1921  C CA  . MET B 2 48  ? 21.598  71.069  38.476  1.000 36.969  ? 48  MET HHH CA  1 
ATOM   1922  C C   . MET B 2 48  ? 20.827  70.800  37.188  1.000 36.826  ? 48  MET HHH C   1 
ATOM   1923  O O   . MET B 2 48  ? 20.694  71.728  36.388  1.000 42.769  ? 48  MET HHH O   1 
ATOM   1924  C CB  . MET B 2 48  ? 23.024  70.537  38.299  1.000 39.604  ? 48  MET HHH CB  1 
ATOM   1925  C CG  . MET B 2 48  ? 23.871  70.626  39.553  1.000 39.374  ? 48  MET HHH CG  1 
ATOM   1926  S SD  . MET B 2 48  ? 25.515  69.969  39.239  1.000 39.123  ? 48  MET HHH SD  1 
ATOM   1927  C CE  . MET B 2 48  ? 26.168  71.280  38.215  1.000 39.394  ? 48  MET HHH CE  1 
ATOM   1928  N N   . GLY B 2 49  ? 20.377  69.568  36.987  1.000 35.874  ? 49  GLY HHH N   1 
ATOM   1929  C CA  . GLY B 2 49  ? 19.688  69.159  35.753  1.000 36.485  ? 49  GLY HHH CA  1 
ATOM   1930  C C   . GLY B 2 49  ? 19.450  67.666  35.731  1.000 40.692  ? 49  GLY HHH C   1 
ATOM   1931  O O   . GLY B 2 49  ? 19.932  66.957  36.630  1.000 44.776  ? 49  GLY HHH O   1 
ATOM   1932  N N   . ILE B 2 50  ? 18.721  67.192  34.734  1.000 41.083  ? 50  ILE HHH N   1 
ATOM   1933  C CA  . ILE B 2 50  ? 18.378  65.753  34.602  1.000 41.198  ? 50  ILE HHH CA  1 
ATOM   1934  C C   . ILE B 2 50  ? 18.485  65.425  33.125  1.000 34.909  ? 50  ILE HHH C   1 
ATOM   1935  O O   . ILE B 2 50  ? 18.279  66.326  32.312  1.000 31.833  ? 50  ILE HHH O   1 
ATOM   1936  C CB  . ILE B 2 50  ? 16.975  65.487  35.187  1.000 48.494  ? 50  ILE HHH CB  1 
ATOM   1937  C CG1 . ILE B 2 50  ? 16.632  63.996  35.264  1.000 55.687  ? 50  ILE HHH CG1 1 
ATOM   1938  C CG2 . ILE B 2 50  ? 15.920  66.274  34.423  1.000 46.505  ? 50  ILE HHH CG2 1 
ATOM   1939  C CD1 . ILE B 2 50  ? 15.392  63.691  36.087  1.000 60.389  ? 50  ILE HHH CD1 1 
ATOM   1940  N N   . ILE B 2 51  ? 18.847  64.197  32.804  1.000 32.257  ? 51  ILE HHH N   1 
ATOM   1941  C CA  . ILE B 2 51  ? 18.844  63.721  31.403  1.000 34.501  ? 51  ILE HHH CA  1 
ATOM   1942  C C   . ILE B 2 51  ? 18.127  62.379  31.361  1.000 34.942  ? 51  ILE HHH C   1 
ATOM   1943  O O   . ILE B 2 51  ? 18.121  61.684  32.386  1.000 32.733  ? 51  ILE HHH O   1 
ATOM   1944  C CB  . ILE B 2 51  ? 20.268  63.633  30.837  1.000 39.120  ? 51  ILE HHH CB  1 
ATOM   1945  C CG1 . ILE B 2 51  ? 20.265  63.768  29.314  1.000 44.813  ? 51  ILE HHH CG1 1 
ATOM   1946  C CG2 . ILE B 2 51  ? 20.954  62.345  31.258  1.000 42.003  ? 51  ILE HHH CG2 1 
ATOM   1947  C CD1 . ILE B 2 51  ? 21.641  63.912  28.692  1.000 45.703  ? 51  ILE HHH CD1 1 
ATOM   1948  N N   . TYR B 2 52  ? 17.518  62.073  30.215  1.000 38.825  ? 52  TYR HHH N   1 
ATOM   1949  C CA  . TYR B 2 52  ? 17.040  60.718  29.862  1.000 43.130  ? 52  TYR HHH CA  1 
ATOM   1950  C C   . TYR B 2 52  ? 18.075  60.115  28.922  1.000 47.438  ? 52  TYR HHH C   1 
ATOM   1951  O O   . TYR B 2 52  ? 18.334  60.660  27.864  1.000 53.543  ? 52  TYR HHH O   1 
ATOM   1952  C CB  . TYR B 2 52  ? 15.632  60.734  29.265  1.000 40.228  ? 52  TYR HHH CB  1 
ATOM   1953  C CG  . TYR B 2 52  ? 15.111  59.342  29.015  1.000 41.201  ? 52  TYR HHH CG  1 
ATOM   1954  C CD1 . TYR B 2 52  ? 14.648  58.547  30.057  1.000 41.911  ? 52  TYR HHH CD1 1 
ATOM   1955  C CD2 . TYR B 2 52  ? 15.172  58.779  27.749  1.000 40.580  ? 52  TYR HHH CD2 1 
ATOM   1956  C CE1 . TYR B 2 52  ? 14.221  57.242  29.837  1.000 43.544  ? 52  TYR HHH CE1 1 
ATOM   1957  C CE2 . TYR B 2 52  ? 14.754  57.479  27.514  1.000 42.134  ? 52  TYR HHH CE2 1 
ATOM   1958  C CZ  . TYR B 2 52  ? 14.295  56.699  28.561  1.000 44.211  ? 52  TYR HHH CZ  1 
ATOM   1959  O OH  . TYR B 2 52  ? 13.899  55.422  28.285  1.000 46.981  ? 52  TYR HHH OH  1 
ATOM   1960  N N   . PRO B 2 53  ? 18.733  59.005  29.301  1.000 49.785  ? 53  PRO HHH N   1 
ATOM   1961  C CA  . PRO B 2 53  ? 19.771  58.422  28.461  1.000 51.266  ? 53  PRO HHH CA  1 
ATOM   1962  C C   . PRO B 2 53  ? 19.260  57.972  27.086  1.000 51.427  ? 53  PRO HHH C   1 
ATOM   1963  O O   . PRO B 2 53  ? 19.955  58.180  26.130  1.000 50.673  ? 53  PRO HHH O   1 
ATOM   1964  C CB  . PRO B 2 53  ? 20.245  57.203  29.261  1.000 56.948  ? 53  PRO HHH CB  1 
ATOM   1965  C CG  . PRO B 2 53  ? 19.799  57.469  30.687  1.000 57.676  ? 53  PRO HHH CG  1 
ATOM   1966  C CD  . PRO B 2 53  ? 18.517  58.262  30.549  1.000 53.873  ? 53  PRO HHH CD  1 
ATOM   1967  N N   . GLY B 2 54  ? 18.081  57.349  27.034  1.000 56.186  ? 54  GLY HHH N   1 
ATOM   1968  C CA  . GLY B 2 54  ? 17.508  56.732  25.819  1.000 57.054  ? 54  GLY HHH CA  1 
ATOM   1969  C C   . GLY B 2 54  ? 17.515  57.649  24.601  1.000 56.294  ? 54  GLY HHH C   1 
ATOM   1970  O O   . GLY B 2 54  ? 17.789  57.130  23.520  1.000 58.442  ? 54  GLY HHH O   1 
ATOM   1971  N N   . ASP B 2 55  ? 17.218  58.945  24.751  1.000 56.811  ? 55  ASP HHH N   1 
ATOM   1972  C CA  . ASP B 2 55  ? 17.137  59.913  23.617  1.000 60.166  ? 55  ASP HHH CA  1 
ATOM   1973  C C   . ASP B 2 55  ? 17.851  61.236  23.948  1.000 57.209  ? 55  ASP HHH C   1 
ATOM   1974  O O   . ASP B 2 55  ? 17.704  62.179  23.170  1.000 55.381  ? 55  ASP HHH O   1 
ATOM   1975  C CB  . ASP B 2 55  ? 15.681  60.157  23.197  1.000 63.895  ? 55  ASP HHH CB  1 
ATOM   1976  C CG  . ASP B 2 55  ? 14.825  60.896  24.221  1.000 71.101  ? 55  ASP HHH CG  1 
ATOM   1977  O OD1 . ASP B 2 55  ? 15.254  61.005  25.388  1.000 69.358  ? 55  ASP HHH OD1 1 
ATOM   1978  O OD2 . ASP B 2 55  ? 13.726  61.362  23.842  1.000 82.397  ? 55  ASP HHH OD2 1 
ATOM   1979  N N   . SER B 2 56  ? 18.593  61.317  25.051  1.000 54.843  ? 56  SER HHH N   1 
ATOM   1980  C CA  . SER B 2 56  ? 19.361  62.520  25.485  1.000 50.698  ? 56  SER HHH CA  1 
ATOM   1981  C C   . SER B 2 56  ? 18.454  63.739  25.684  1.000 44.230  ? 56  SER HHH C   1 
ATOM   1982  O O   . SER B 2 56  ? 18.897  64.847  25.366  1.000 38.886  ? 56  SER HHH O   1 
ATOM   1983  C CB  . SER B 2 56  ? 20.470  62.838  24.514  1.000 49.575  ? 56  SER HHH CB  1 
ATOM   1984  O OG  . SER B 2 56  ? 21.393  61.771  24.435  1.000 48.549  ? 56  SER HHH OG  1 
ATOM   1985  N N   . GLU B 2 57  ? 17.244  63.561  26.201  1.000 46.344  ? 57  GLU HHH N   1 
ATOM   1986  C CA  . GLU B 2 57  ? 16.371  64.712  26.569  1.000 53.735  ? 57  GLU HHH CA  1 
ATOM   1987  C C   . GLU B 2 57  ? 16.961  65.328  27.835  1.000 52.552  ? 57  GLU HHH C   1 
ATOM   1988  O O   . GLU B 2 57  ? 17.059  64.611  28.830  1.000 56.285  ? 57  GLU HHH O   1 
ATOM   1989  C CB  . GLU B 2 57  ? 14.908  64.313  26.820  1.000 57.278  ? 57  GLU HHH CB  1 
ATOM   1990  C CG  . GLU B 2 57  ? 13.993  65.517  27.055  1.000 55.712  ? 57  GLU HHH CG  1 
ATOM   1991  C CD  . GLU B 2 57  ? 12.659  65.305  27.767  1.000 52.307  ? 57  GLU HHH CD  1 
ATOM   1992  O OE1 . GLU B 2 57  ? 11.960  64.311  27.477  1.000 52.407  ? 57  GLU HHH OE1 1 
ATOM   1993  O OE2 . GLU B 2 57  ? 12.309  66.162  28.602  1.000 48.654  ? 57  GLU HHH OE2 1 
ATOM   1994  N N   . THR B 2 58  ? 17.332  66.600  27.798  1.000 51.277  ? 58  THR HHH N   1 
ATOM   1995  C CA  . THR B 2 58  ? 18.138  67.244  28.864  1.000 49.956  ? 58  THR HHH CA  1 
ATOM   1996  C C   . THR B 2 58  ? 17.398  68.476  29.381  1.000 48.926  ? 58  THR HHH C   1 
ATOM   1997  O O   . THR B 2 58  ? 17.130  69.368  28.575  1.000 57.684  ? 58  THR HHH O   1 
ATOM   1998  C CB  . THR B 2 58  ? 19.529  67.625  28.349  1.000 49.472  ? 58  THR HHH CB  1 
ATOM   1999  O OG1 . THR B 2 58  ? 19.986  66.653  27.413  1.000 49.474  ? 58  THR HHH OG1 1 
ATOM   2000  C CG2 . THR B 2 58  ? 20.543  67.687  29.454  1.000 50.346  ? 58  THR HHH CG2 1 
ATOM   2001  N N   . ARG B 2 59  ? 17.099  68.516  30.677  1.000 45.975  ? 59  ARG HHH N   1 
ATOM   2002  C CA  . ARG B 2 59  ? 16.471  69.671  31.366  1.000 44.237  ? 59  ARG HHH CA  1 
ATOM   2003  C C   . ARG B 2 59  ? 17.472  70.223  32.373  1.000 44.004  ? 59  ARG HHH C   1 
ATOM   2004  O O   . ARG B 2 59  ? 18.014  69.426  33.157  1.000 49.432  ? 59  ARG HHH O   1 
ATOM   2005  C CB  . ARG B 2 59  ? 15.199  69.245  32.102  1.000 44.277  ? 59  ARG HHH CB  1 
ATOM   2006  C CG  . ARG B 2 59  ? 14.228  68.454  31.244  1.000 45.017  ? 59  ARG HHH CG  1 
ATOM   2007  C CD  . ARG B 2 59  ? 12.933  69.203  31.053  1.000 48.277  ? 59  ARG HHH CD  1 
ATOM   2008  N NE  . ARG B 2 59  ? 11.835  68.700  31.864  1.000 46.772  ? 59  ARG HHH NE  1 
ATOM   2009  C CZ  . ARG B 2 59  ? 11.129  67.600  31.596  1.000 46.315  ? 59  ARG HHH CZ  1 
ATOM   2010  N NH1 . ARG B 2 59  ? 11.434  66.814  30.572  1.000 41.849  ? 59  ARG HHH NH1 1 
ATOM   2011  N NH2 . ARG B 2 59  ? 10.125  67.276  32.390  1.000 49.922  ? 59  ARG HHH NH2 1 
ATOM   2012  N N   . TYR B 2 60  ? 17.714  71.532  32.342  1.000 44.273  ? 60  TYR HHH N   1 
ATOM   2013  C CA  . TYR B 2 60  ? 18.668  72.234  33.232  1.000 47.068  ? 60  TYR HHH CA  1 
ATOM   2014  C C   . TYR B 2 60  ? 17.882  72.977  34.311  1.000 47.217  ? 60  TYR HHH C   1 
ATOM   2015  O O   . TYR B 2 60  ? 16.709  73.241  34.121  1.000 57.618  ? 60  TYR HHH O   1 
ATOM   2016  C CB  . TYR B 2 60  ? 19.563  73.161  32.408  1.000 50.672  ? 60  TYR HHH CB  1 
ATOM   2017  C CG  . TYR B 2 60  ? 20.628  72.476  31.578  1.000 54.915  ? 60  TYR HHH CG  1 
ATOM   2018  C CD1 . TYR B 2 60  ? 21.642  73.197  30.973  1.000 65.438  ? 60  TYR HHH CD1 1 
ATOM   2019  C CD2 . TYR B 2 60  ? 20.634  71.114  31.385  1.000 54.647  ? 60  TYR HHH CD2 1 
ATOM   2020  C CE1 . TYR B 2 60  ? 22.631  72.588  30.220  1.000 63.324  ? 60  TYR HHH CE1 1 
ATOM   2021  C CE2 . TYR B 2 60  ? 21.614  70.487  30.645  1.000 56.099  ? 60  TYR HHH CE2 1 
ATOM   2022  C CZ  . TYR B 2 60  ? 22.610  71.221  30.057  1.000 56.935  ? 60  TYR HHH CZ  1 
ATOM   2023  O OH  . TYR B 2 60  ? 23.543  70.558  29.334  1.000 58.434  ? 60  TYR HHH OH  1 
ATOM   2024  N N   . SER B 2 61  ? 18.512  73.263  35.443  1.000 48.443  ? 61  SER HHH N   1 
ATOM   2025  C CA  . SER B 2 61  ? 18.044  74.276  36.418  1.000 47.887  ? 61  SER HHH CA  1 
ATOM   2026  C C   . SER B 2 61  ? 18.481  75.641  35.909  1.000 50.922  ? 61  SER HHH C   1 
ATOM   2027  O O   . SER B 2 61  ? 19.550  75.764  35.309  1.000 47.585  ? 61  SER HHH O   1 
ATOM   2028  C CB  . SER B 2 61  ? 18.582  74.028  37.795  1.000 51.274  ? 61  SER HHH CB  1 
ATOM   2029  O OG  . SER B 2 61  ? 18.670  75.244  38.533  1.000 53.204  ? 61  SER HHH OG  1 
ATOM   2030  N N   . PRO B 2 62  ? 17.662  76.692  36.136  1.000 56.642  ? 62  PRO HHH N   1 
ATOM   2031  C CA  . PRO B 2 62  ? 18.016  78.062  35.765  1.000 55.063  ? 62  PRO HHH CA  1 
ATOM   2032  C C   . PRO B 2 62  ? 19.456  78.447  36.132  1.000 54.214  ? 62  PRO HHH C   1 
ATOM   2033  O O   . PRO B 2 62  ? 20.069  79.139  35.351  1.000 57.935  ? 62  PRO HHH O   1 
ATOM   2034  C CB  . PRO B 2 62  ? 17.067  78.929  36.608  1.000 54.058  ? 62  PRO HHH CB  1 
ATOM   2035  C CG  . PRO B 2 62  ? 15.854  78.047  36.853  1.000 56.496  ? 62  PRO HHH CG  1 
ATOM   2036  C CD  . PRO B 2 62  ? 16.358  76.619  36.811  1.000 57.099  ? 62  PRO HHH CD  1 
ATOM   2037  N N   . SER B 2 63  ? 19.946  78.005  37.297  1.000 51.422  ? 63  SER HHH N   1 
ATOM   2038  C CA  . SER B 2 63  ? 21.243  78.448  37.872  1.000 52.762  ? 63  SER HHH CA  1 
ATOM   2039  C C   . SER B 2 63  ? 22.419  77.823  37.115  1.000 52.505  ? 63  SER HHH C   1 
ATOM   2040  O O   . SER B 2 63  ? 23.538  78.338  37.252  1.000 58.948  ? 63  SER HHH O   1 
ATOM   2041  C CB  . SER B 2 63  ? 21.325  78.149  39.339  1.000 55.060  ? 63  SER HHH CB  1 
ATOM   2042  O OG  . SER B 2 63  ? 20.163  78.608  40.005  1.000 62.574  ? 63  SER HHH OG  1 
ATOM   2043  N N   . PHE B 2 64  ? 22.188  76.743  36.369  1.000 52.386  ? 64  PHE HHH N   1 
ATOM   2044  C CA  . PHE B 2 64  ? 23.249  75.955  35.693  1.000 51.809  ? 64  PHE HHH CA  1 
ATOM   2045  C C   . PHE B 2 64  ? 23.010  75.900  34.181  1.000 56.509  ? 64  PHE HHH C   1 
ATOM   2046  O O   . PHE B 2 64  ? 23.796  75.222  33.499  1.000 68.446  ? 64  PHE HHH O   1 
ATOM   2047  C CB  . PHE B 2 64  ? 23.335  74.546  36.290  1.000 52.019  ? 64  PHE HHH CB  1 
ATOM   2048  C CG  . PHE B 2 64  ? 23.610  74.522  37.773  1.000 49.718  ? 64  PHE HHH CG  1 
ATOM   2049  C CD1 . PHE B 2 64  ? 24.899  74.645  38.266  1.000 49.155  ? 64  PHE HHH CD1 1 
ATOM   2050  C CD2 . PHE B 2 64  ? 22.567  74.421  38.679  1.000 49.920  ? 64  PHE HHH CD2 1 
ATOM   2051  C CE1 . PHE B 2 64  ? 25.136  74.647  39.631  1.000 47.961  ? 64  PHE HHH CE1 1 
ATOM   2052  C CE2 . PHE B 2 64  ? 22.805  74.430  40.043  1.000 48.780  ? 64  PHE HHH CE2 1 
ATOM   2053  C CZ  . PHE B 2 64  ? 24.085  74.551  40.515  1.000 47.914  ? 64  PHE HHH CZ  1 
ATOM   2054  N N   . GLN B 2 65  ? 21.993  76.587  33.658  1.000 60.838  ? 65  GLN HHH N   1 
ATOM   2055  C CA  . GLN B 2 65  ? 21.797  76.714  32.189  1.000 65.017  ? 65  GLN HHH CA  1 
ATOM   2056  C C   . GLN B 2 65  ? 23.103  77.244  31.578  1.000 61.352  ? 65  GLN HHH C   1 
ATOM   2057  O O   . GLN B 2 65  ? 23.582  78.295  32.050  1.000 59.316  ? 65  GLN HHH O   1 
ATOM   2058  C CB  . GLN B 2 65  ? 20.597  77.616  31.871  1.000 73.837  ? 65  GLN HHH CB  1 
ATOM   2059  C CG  . GLN B 2 65  ? 20.294  77.752  30.379  1.000 81.029  ? 65  GLN HHH CG  1 
ATOM   2060  C CD  . GLN B 2 65  ? 19.846  76.457  29.735  1.000 82.782  ? 65  GLN HHH CD  1 
ATOM   2061  O OE1 . GLN B 2 65  ? 18.985  75.751  30.256  1.000 77.970  ? 65  GLN HHH OE1 1 
ATOM   2062  N NE2 . GLN B 2 65  ? 20.424  76.136  28.585  1.000 86.096  ? 65  GLN HHH NE2 1 
ATOM   2063  N N   . GLY B 2 66  ? 23.687  76.513  30.622  1.000 57.732  ? 66  GLY HHH N   1 
ATOM   2064  C CA  . GLY B 2 66  ? 24.864  76.952  29.843  1.000 59.418  ? 66  GLY HHH CA  1 
ATOM   2065  C C   . GLY B 2 66  ? 26.105  77.234  30.694  1.000 59.706  ? 66  GLY HHH C   1 
ATOM   2066  O O   . GLY B 2 66  ? 27.090  77.715  30.115  1.000 62.246  ? 66  GLY HHH O   1 
ATOM   2067  N N   . GLN B 2 67  ? 26.082  76.931  32.003  1.000 58.915  ? 67  GLN HHH N   1 
ATOM   2068  C CA  . GLN B 2 67  ? 27.261  76.897  32.917  1.000 52.366  ? 67  GLN HHH CA  1 
ATOM   2069  C C   . GLN B 2 67  ? 27.933  75.516  32.888  1.000 46.545  ? 67  GLN HHH C   1 
ATOM   2070  O O   . GLN B 2 67  ? 29.152  75.469  33.102  1.000 48.335  ? 67  GLN HHH O   1 
ATOM   2071  C CB  . GLN B 2 67  ? 26.856  77.241  34.348  1.000 55.812  ? 67  GLN HHH CB  1 
ATOM   2072  C CG  . GLN B 2 67  ? 26.350  78.669  34.498  1.000 63.901  ? 67  GLN HHH CG  1 
ATOM   2073  C CD  . GLN B 2 67  ? 27.352  79.711  34.062  1.000 70.547  ? 67  GLN HHH CD  1 
ATOM   2074  O OE1 . GLN B 2 67  ? 28.567  79.496  34.081  1.000 76.596  ? 67  GLN HHH OE1 1 
ATOM   2075  N NE2 . GLN B 2 67  ? 26.838  80.867  33.672  1.000 73.268  ? 67  GLN HHH NE2 1 
ATOM   2076  N N   . VAL B 2 68  ? 27.170  74.448  32.643  1.000 42.502  ? 68  VAL HHH N   1 
ATOM   2077  C CA  . VAL B 2 68  ? 27.664  73.048  32.472  1.000 41.018  ? 68  VAL HHH CA  1 
ATOM   2078  C C   . VAL B 2 68  ? 26.956  72.429  31.269  1.000 38.715  ? 68  VAL HHH C   1 
ATOM   2079  O O   . VAL B 2 68  ? 26.041  73.074  30.725  1.000 36.280  ? 68  VAL HHH O   1 
ATOM   2080  C CB  . VAL B 2 68  ? 27.398  72.190  33.724  1.000 41.693  ? 68  VAL HHH CB  1 
ATOM   2081  C CG1 . VAL B 2 68  ? 27.881  72.874  34.993  1.000 42.888  ? 68  VAL HHH CG1 1 
ATOM   2082  C CG2 . VAL B 2 68  ? 25.928  71.820  33.848  1.000 41.948  ? 68  VAL HHH CG2 1 
ATOM   2083  N N   . THR B 2 69  ? 27.323  71.191  30.946  1.000 38.854  ? 69  THR HHH N   1 
ATOM   2084  C CA  . THR B 2 69  ? 26.696  70.347  29.902  1.000 44.105  ? 69  THR HHH CA  1 
ATOM   2085  C C   . THR B 2 69  ? 26.489  68.927  30.441  1.000 48.659  ? 69  THR HHH C   1 
ATOM   2086  O O   . THR B 2 69  ? 27.502  68.191  30.616  1.000 49.305  ? 69  THR HHH O   1 
ATOM   2087  C CB  . THR B 2 69  ? 27.536  70.294  28.620  1.000 44.149  ? 69  THR HHH CB  1 
ATOM   2088  O OG1 . THR B 2 69  ? 27.467  71.595  28.051  1.000 47.049  ? 69  THR HHH OG1 1 
ATOM   2089  C CG2 . THR B 2 69  ? 27.035  69.307  27.585  1.000 43.964  ? 69  THR HHH CG2 1 
ATOM   2090  N N   . ILE B 2 70  ? 25.221  68.552  30.620  1.000 44.835  ? 70  ILE HHH N   1 
ATOM   2091  C CA  . ILE B 2 70  ? 24.808  67.154  30.906  1.000 41.184  ? 70  ILE HHH CA  1 
ATOM   2092  C C   . ILE B 2 70  ? 24.622  66.442  29.569  1.000 40.067  ? 70  ILE HHH C   1 
ATOM   2093  O O   . ILE B 2 70  ? 23.937  66.984  28.716  1.000 45.654  ? 70  ILE HHH O   1 
ATOM   2094  C CB  . ILE B 2 70  ? 23.539  67.151  31.760  1.000 41.150  ? 70  ILE HHH CB  1 
ATOM   2095  C CG1 . ILE B 2 70  ? 23.750  67.978  33.029  1.000 43.279  ? 70  ILE HHH CG1 1 
ATOM   2096  C CG2 . ILE B 2 70  ? 23.105  65.723  32.044  1.000 41.856  ? 70  ILE HHH CG2 1 
ATOM   2097  C CD1 . ILE B 2 70  ? 22.499  68.262  33.819  1.000 43.499  ? 70  ILE HHH CD1 1 
ATOM   2098  N N   . SER B 2 71  ? 25.235  65.276  29.411  1.000 39.455  ? 71  SER HHH N   1 
ATOM   2099  C CA  . SER B 2 71  ? 25.263  64.466  28.170  1.000 41.374  ? 71  SER HHH CA  1 
ATOM   2100  C C   . SER B 2 71  ? 25.029  63.013  28.567  1.000 41.979  ? 71  SER HHH C   1 
ATOM   2101  O O   . SER B 2 71  ? 24.982  62.758  29.784  1.000 43.206  ? 71  SER HHH O   1 
ATOM   2102  C CB  . SER B 2 71  ? 26.568  64.654  27.420  1.000 45.823  ? 71  SER HHH CB  1 
ATOM   2103  O OG  . SER B 2 71  ? 27.675  64.857  28.297  1.000 50.674  ? 71  SER HHH OG  1 
ATOM   2104  N N   . ALA B 2 72  ? 24.877  62.101  27.609  1.000 43.102  ? 72  ALA HHH N   1 
ATOM   2105  C CA  . ALA B 2 72  ? 24.587  60.685  27.919  1.000 46.429  ? 72  ALA HHH CA  1 
ATOM   2106  C C   . ALA B 2 72  ? 25.129  59.772  26.826  1.000 47.803  ? 72  ALA HHH C   1 
ATOM   2107  O O   . ALA B 2 72  ? 25.385  60.244  25.722  1.000 54.185  ? 72  ALA HHH O   1 
ATOM   2108  C CB  . ALA B 2 72  ? 23.102  60.488  28.094  1.000 50.377  ? 72  ALA HHH CB  1 
ATOM   2109  N N   . ASP B 2 73  ? 25.298  58.500  27.161  1.000 50.635  ? 73  ASP HHH N   1 
ATOM   2110  C CA  . ASP B 2 73  ? 25.709  57.427  26.225  1.000 55.719  ? 73  ASP HHH CA  1 
ATOM   2111  C C   . ASP B 2 73  ? 24.969  56.165  26.673  1.000 64.533  ? 73  ASP HHH C   1 
ATOM   2112  O O   . ASP B 2 73  ? 25.433  55.489  27.631  1.000 59.340  ? 73  ASP HHH O   1 
ATOM   2113  C CB  . ASP B 2 73  ? 27.230  57.281  26.188  1.000 56.289  ? 73  ASP HHH CB  1 
ATOM   2114  C CG  . ASP B 2 73  ? 27.747  56.319  25.128  1.000 58.025  ? 73  ASP HHH CG  1 
ATOM   2115  O OD1 . ASP B 2 73  ? 27.005  55.380  24.773  1.000 60.522  ? 73  ASP HHH OD1 1 
ATOM   2116  O OD2 . ASP B 2 73  ? 28.894  56.514  24.665  1.000 64.107  ? 73  ASP HHH OD2 1 
ATOM   2117  N N   . LYS B 2 74  ? 23.830  55.913  26.025  1.000 70.601  ? 74  LYS HHH N   1 
ATOM   2118  C CA  . LYS B 2 74  ? 22.868  54.836  26.377  1.000 72.060  ? 74  LYS HHH CA  1 
ATOM   2119  C C   . LYS B 2 74  ? 23.531  53.475  26.168  1.000 65.404  ? 74  LYS HHH C   1 
ATOM   2120  O O   . LYS B 2 74  ? 23.061  52.527  26.796  1.000 71.132  ? 74  LYS HHH O   1 
ATOM   2121  C CB  . LYS B 2 74  ? 21.573  54.967  25.560  1.000 81.664  ? 74  LYS HHH CB  1 
ATOM   2122  C CG  . LYS B 2 74  ? 21.773  55.171  24.063  1.000 87.539  ? 74  LYS HHH CG  1 
ATOM   2123  C CD  . LYS B 2 74  ? 20.515  55.384  23.262  1.000 86.847  ? 74  LYS HHH CD  1 
ATOM   2124  C CE  . LYS B 2 74  ? 20.830  55.811  21.842  1.000 82.383  ? 74  LYS HHH CE  1 
ATOM   2125  N NZ  . LYS B 2 74  ? 19.748  56.602  21.221  1.000 80.311  ? 74  LYS HHH NZ  1 
ATOM   2126  N N   . SER B 2 75  ? 24.576  53.387  25.336  1.000 63.884  ? 75  SER HHH N   1 
ATOM   2127  C CA  . SER B 2 75  ? 25.245  52.113  24.952  1.000 62.091  ? 75  SER HHH CA  1 
ATOM   2128  C C   . SER B 2 75  ? 26.020  51.533  26.141  1.000 57.314  ? 75  SER HHH C   1 
ATOM   2129  O O   . SER B 2 75  ? 26.176  50.306  26.190  1.000 57.524  ? 75  SER HHH O   1 
ATOM   2130  C CB  . SER B 2 75  ? 26.133  52.280  23.739  1.000 62.286  ? 75  SER HHH CB  1 
ATOM   2131  O OG  . SER B 2 75  ? 27.173  53.212  23.979  1.000 64.171  ? 75  SER HHH OG  1 
ATOM   2132  N N   . ILE B 2 76  ? 26.447  52.377  27.084  1.000 56.739  ? 76  ILE HHH N   1 
ATOM   2133  C CA  . ILE B 2 76  ? 27.249  51.972  28.281  1.000 53.687  ? 76  ILE HHH CA  1 
ATOM   2134  C C   . ILE B 2 76  ? 26.532  52.397  29.573  1.000 55.408  ? 76  ILE HHH C   1 
ATOM   2135  O O   . ILE B 2 76  ? 27.127  52.228  30.631  1.000 53.344  ? 76  ILE HHH O   1 
ATOM   2136  C CB  . ILE B 2 76  ? 28.682  52.537  28.181  1.000 49.706  ? 76  ILE HHH CB  1 
ATOM   2137  C CG1 . ILE B 2 76  ? 28.696  53.989  27.695  1.000 51.169  ? 76  ILE HHH CG1 1 
ATOM   2138  C CG2 . ILE B 2 76  ? 29.524  51.646  27.292  1.000 48.878  ? 76  ILE HHH CG2 1 
ATOM   2139  C CD1 . ILE B 2 76  ? 30.058  54.656  27.691  1.000 50.782  ? 76  ILE HHH CD1 1 
ATOM   2140  N N   . ASN B 2 77  ? 25.293  52.897  29.486  1.000 58.245  ? 77  ASN HHH N   1 
ATOM   2141  C CA  . ASN B 2 77  ? 24.422  53.239  30.646  1.000 57.574  ? 77  ASN HHH CA  1 
ATOM   2142  C C   . ASN B 2 77  ? 25.073  54.359  31.468  1.000 52.296  ? 77  ASN HHH C   1 
ATOM   2143  O O   . ASN B 2 77  ? 25.056  54.267  32.704  1.000 46.985  ? 77  ASN HHH O   1 
ATOM   2144  C CB  . ASN B 2 77  ? 24.113  51.988  31.475  1.000 57.733  ? 77  ASN HHH CB  1 
ATOM   2145  C CG  . ASN B 2 77  ? 23.240  51.016  30.715  1.000 58.152  ? 77  ASN HHH CG  1 
ATOM   2146  O OD1 . ASN B 2 77  ? 22.854  51.280  29.589  1.000 67.354  ? 77  ASN HHH OD1 1 
ATOM   2147  N ND2 . ASN B 2 77  ? 22.888  49.904  31.323  1.000 60.412  ? 77  ASN HHH ND2 1 
ATOM   2148  N N   . THR B 2 78  ? 25.602  55.386  30.806  1.000 46.494  ? 78  THR HHH N   1 
ATOM   2149  C CA  . THR B 2 78  ? 26.490  56.380  31.453  1.000 48.238  ? 78  THR HHH CA  1 
ATOM   2150  C C   . THR B 2 78  ? 26.002  57.785  31.143  1.000 41.731  ? 78  THR HHH C   1 
ATOM   2151  O O   . THR B 2 78  ? 25.881  58.131  29.961  1.000 44.481  ? 78  THR HHH O   1 
ATOM   2152  C CB  . THR B 2 78  ? 27.953  56.219  31.018  1.000 55.159  ? 78  THR HHH CB  1 
ATOM   2153  O OG1 . THR B 2 78  ? 28.289  54.835  31.096  1.000 56.554  ? 78  THR HHH OG1 1 
ATOM   2154  C CG2 . THR B 2 78  ? 28.917  57.016  31.874  1.000 58.035  ? 78  THR HHH CG2 1 
ATOM   2155  N N   . ALA B 2 79  ? 25.767  58.550  32.197  1.000 37.878  ? 79  ALA HHH N   1 
ATOM   2156  C CA  . ALA B 2 79  ? 25.494  59.997  32.143  1.000 38.954  ? 79  ALA HHH CA  1 
ATOM   2157  C C   . ALA B 2 79  ? 26.780  60.749  32.471  1.000 38.449  ? 79  ALA HHH C   1 
ATOM   2158  O O   . ALA B 2 79  ? 27.582  60.251  33.290  1.000 35.624  ? 79  ALA HHH O   1 
ATOM   2159  C CB  . ALA B 2 79  ? 24.403  60.350  33.117  1.000 42.261  ? 79  ALA HHH CB  1 
ATOM   2160  N N   . TYR B 2 80  ? 26.953  61.921  31.863  1.000 38.944  ? 80  TYR HHH N   1 
ATOM   2161  C CA  . TYR B 2 80  ? 28.173  62.753  31.975  1.000 37.499  ? 80  TYR HHH CA  1 
ATOM   2162  C C   . TYR B 2 80  ? 27.752  64.157  32.372  1.000 39.131  ? 80  TYR HHH C   1 
ATOM   2163  O O   . TYR B 2 80  ? 26.697  64.611  31.946  1.000 43.915  ? 80  TYR HHH O   1 
ATOM   2164  C CB  . TYR B 2 80  ? 28.961  62.773  30.667  1.000 36.618  ? 80  TYR HHH CB  1 
ATOM   2165  C CG  . TYR B 2 80  ? 29.516  61.442  30.214  1.000 39.117  ? 80  TYR HHH CG  1 
ATOM   2166  C CD1 . TYR B 2 80  ? 30.803  61.036  30.537  1.000 40.976  ? 80  TYR HHH CD1 1 
ATOM   2167  C CD2 . TYR B 2 80  ? 28.741  60.573  29.469  1.000 40.726  ? 80  TYR HHH CD2 1 
ATOM   2168  C CE1 . TYR B 2 80  ? 31.313  59.821  30.098  1.000 43.753  ? 80  TYR HHH CE1 1 
ATOM   2169  C CE2 . TYR B 2 80  ? 29.227  59.345  29.040  1.000 42.369  ? 80  TYR HHH CE2 1 
ATOM   2170  C CZ  . TYR B 2 80  ? 30.522  58.967  29.344  1.000 43.342  ? 80  TYR HHH CZ  1 
ATOM   2171  O OH  . TYR B 2 80  ? 30.974  57.749  28.911  1.000 41.315  ? 80  TYR HHH OH  1 
ATOM   2172  N N   . LEU B 2 81  ? 28.569  64.806  33.191  1.000 41.536  ? 81  LEU HHH N   1 
ATOM   2173  C CA  . LEU B 2 81  ? 28.435  66.235  33.553  1.000 41.940  ? 81  LEU HHH CA  1 
ATOM   2174  C C   . LEU B 2 81  ? 29.801  66.879  33.286  1.000 47.470  ? 81  LEU HHH C   1 
ATOM   2175  O O   . LEU B 2 81  ? 30.753  66.414  33.907  1.000 53.323  ? 81  LEU HHH O   1 
ATOM   2176  C CB  . LEU B 2 81  ? 27.985  66.315  35.016  1.000 39.163  ? 81  LEU HHH CB  1 
ATOM   2177  C CG  . LEU B 2 81  ? 28.199  67.656  35.712  1.000 40.168  ? 81  LEU HHH CG  1 
ATOM   2178  C CD1 . LEU B 2 81  ? 27.439  68.753  34.997  1.000 41.770  ? 81  LEU HHH CD1 1 
ATOM   2179  C CD2 . LEU B 2 81  ? 27.761  67.597  37.165  1.000 41.213  ? 81  LEU HHH CD2 1 
ATOM   2180  N N   . GLN B 2 82  ? 29.902  67.849  32.356  1.000 50.359  ? 82  GLN HHH N   1 
ATOM   2181  C CA  . GLN B 2 82  ? 31.196  68.443  31.913  1.000 50.354  ? 82  GLN HHH CA  1 
ATOM   2182  C C   . GLN B 2 82  ? 31.179  69.970  31.939  1.000 49.472  ? 82  GLN HHH C   1 
ATOM   2183  O O   . GLN B 2 82  ? 30.141  70.580  31.696  1.000 56.306  ? 82  GLN HHH O   1 
ATOM   2184  C CB  . GLN B 2 82  ? 31.614  67.964  30.523  1.000 54.407  ? 82  GLN HHH CB  1 
ATOM   2185  C CG  . GLN B 2 82  ? 30.801  68.513  29.356  1.000 61.977  ? 82  GLN HHH CG  1 
ATOM   2186  C CD  . GLN B 2 82  ? 31.086  67.757  28.077  1.000 67.100  ? 82  GLN HHH CD  1 
ATOM   2187  O OE1 . GLN B 2 82  ? 32.237  67.540  27.704  1.000 77.207  ? 82  GLN HHH OE1 1 
ATOM   2188  N NE2 . GLN B 2 82  ? 30.035  67.320  27.398  1.000 66.314  ? 82  GLN HHH NE2 1 
ATOM   2189  N N   . TRP B 2 83  ? 32.340  70.540  32.242  1.000 49.619  ? 83  TRP HHH N   1 
ATOM   2190  C CA  . TRP B 2 83  ? 32.673  71.981  32.146  1.000 48.587  ? 83  TRP HHH CA  1 
ATOM   2191  C C   . TRP B 2 83  ? 33.669  72.177  30.991  1.000 54.370  ? 83  TRP HHH C   1 
ATOM   2192  O O   . TRP B 2 83  ? 34.545  71.314  30.807  1.000 60.341  ? 83  TRP HHH O   1 
ATOM   2193  C CB  . TRP B 2 83  ? 33.264  72.456  33.477  1.000 44.578  ? 83  TRP HHH CB  1 
ATOM   2194  C CG  . TRP B 2 83  ? 32.362  72.376  34.670  1.000 41.244  ? 83  TRP HHH CG  1 
ATOM   2195  C CD1 . TRP B 2 83  ? 31.706  73.422  35.239  1.000 41.174  ? 83  TRP HHH CD1 1 
ATOM   2196  C CD2 . TRP B 2 83  ? 32.069  71.229  35.490  1.000 41.475  ? 83  TRP HHH CD2 1 
ATOM   2197  N NE1 . TRP B 2 83  ? 31.009  73.011  36.340  1.000 42.162  ? 83  TRP HHH NE1 1 
ATOM   2198  C CE2 . TRP B 2 83  ? 31.206  71.669  36.518  1.000 42.767  ? 83  TRP HHH CE2 1 
ATOM   2199  C CE3 . TRP B 2 83  ? 32.438  69.881  35.467  1.000 39.508  ? 83  TRP HHH CE3 1 
ATOM   2200  C CZ2 . TRP B 2 83  ? 30.721  70.820  37.515  1.000 41.944  ? 83  TRP HHH CZ2 1 
ATOM   2201  C CZ3 . TRP B 2 83  ? 31.948  69.039  36.443  1.000 40.743  ? 83  TRP HHH CZ3 1 
ATOM   2202  C CH2 . TRP B 2 83  ? 31.102  69.501  37.458  1.000 41.970  ? 83  TRP HHH CH2 1 
ATOM   2203  N N   . SER B 2 84  ? 33.555  73.256  30.217  1.000 60.515  ? 84  SER HHH N   1 
ATOM   2204  C CA  . SER B 2 84  ? 34.583  73.633  29.210  1.000 57.877  ? 84  SER HHH CA  1 
ATOM   2205  C C   . SER B 2 84  ? 35.733  74.325  29.948  1.000 53.207  ? 84  SER HHH C   1 
ATOM   2206  O O   . SER B 2 84  ? 36.883  73.968  29.652  1.000 56.425  ? 84  SER HHH O   1 
ATOM   2207  C CB  . SER B 2 84  ? 34.018  74.469  28.107  1.000 61.460  ? 84  SER HHH CB  1 
ATOM   2208  O OG  . SER B 2 84  ? 33.312  75.567  28.652  1.000 75.811  ? 84  SER HHH OG  1 
ATOM   2209  N N   . SER B 2 85  ? 35.430  75.204  30.913  1.000 46.669  ? 85  SER HHH N   1 
ATOM   2210  C CA  . SER B 2 85  ? 36.436  75.966  31.708  1.000 47.541  ? 85  SER HHH CA  1 
ATOM   2211  C C   . SER B 2 85  ? 36.048  76.121  33.195  1.000 46.299  ? 85  SER HHH C   1 
ATOM   2212  O O   . SER B 2 85  ? 35.142  76.939  33.511  1.000 46.370  ? 85  SER HHH O   1 
ATOM   2213  C CB  . SER B 2 85  ? 36.654  77.307  31.065  1.000 50.707  ? 85  SER HHH CB  1 
ATOM   2214  O OG  . SER B 2 85  ? 37.565  78.099  31.817  1.000 53.785  ? 85  SER HHH OG  1 
ATOM   2215  N N   . LEU B 2 86  ? 36.777  75.441  34.089  1.000 44.113  ? 86  LEU HHH N   1 
ATOM   2216  C CA  . LEU B 2 86  ? 36.456  75.372  35.544  1.000 42.932  ? 86  LEU HHH CA  1 
ATOM   2217  C C   . LEU B 2 86  ? 36.812  76.679  36.242  1.000 41.366  ? 86  LEU HHH C   1 
ATOM   2218  O O   . LEU B 2 86  ? 37.875  77.232  35.981  1.000 37.848  ? 86  LEU HHH O   1 
ATOM   2219  C CB  . LEU B 2 86  ? 37.200  74.203  36.197  1.000 43.983  ? 86  LEU HHH CB  1 
ATOM   2220  C CG  . LEU B 2 86  ? 36.508  72.852  36.051  1.000 45.871  ? 86  LEU HHH CG  1 
ATOM   2221  C CD1 . LEU B 2 86  ? 37.404  71.735  36.528  1.000 44.227  ? 86  LEU HHH CD1 1 
ATOM   2222  C CD2 . LEU B 2 86  ? 35.184  72.846  36.807  1.000 49.525  ? 86  LEU HHH CD2 1 
ATOM   2223  N N   . LYS B 2 87  ? 35.923  77.151  37.100  1.000 47.094  ? 87  LYS HHH N   1 
ATOM   2224  C CA  . LYS B 2 87  ? 36.185  78.273  38.044  1.000 54.413  ? 87  LYS HHH CA  1 
ATOM   2225  C C   . LYS B 2 87  ? 36.463  77.634  39.407  1.000 48.633  ? 87  LYS HHH C   1 
ATOM   2226  O O   . LYS B 2 87  ? 36.044  76.487  39.624  1.000 41.056  ? 87  LYS HHH O   1 
ATOM   2227  C CB  . LYS B 2 87  ? 35.013  79.278  38.080  1.000 65.731  ? 87  LYS HHH CB  1 
ATOM   2228  C CG  . LYS B 2 87  ? 34.525  79.746  36.708  1.000 73.618  ? 87  LYS HHH CG  1 
ATOM   2229  C CD  . LYS B 2 87  ? 33.094  80.262  36.596  1.000 74.589  ? 87  LYS HHH CD  1 
ATOM   2230  C CE  . LYS B 2 87  ? 32.741  80.541  35.143  1.000 81.571  ? 87  LYS HHH CE  1 
ATOM   2231  N NZ  . LYS B 2 87  ? 31.332  80.216  34.803  1.000 89.276  ? 87  LYS HHH NZ  1 
ATOM   2232  N N   . ALA B 2 88  ? 37.147  78.360  40.287  1.000 52.417  ? 88  ALA HHH N   1 
ATOM   2233  C CA  . ALA B 2 88  ? 37.446  77.946  41.677  1.000 53.337  ? 88  ALA HHH CA  1 
ATOM   2234  C C   . ALA B 2 88  ? 36.139  77.741  42.446  1.000 55.341  ? 88  ALA HHH C   1 
ATOM   2235  O O   . ALA B 2 88  ? 36.116  76.870  43.312  1.000 51.774  ? 88  ALA HHH O   1 
ATOM   2236  C CB  . ALA B 2 88  ? 38.319  78.980  42.343  1.000 56.285  ? 88  ALA HHH CB  1 
ATOM   2237  N N   . SER B 2 89  ? 35.096  78.522  42.133  1.000 65.110  ? 89  SER HHH N   1 
ATOM   2238  C CA  . SER B 2 89  ? 33.750  78.482  42.774  1.000 57.800  ? 89  SER HHH CA  1 
ATOM   2239  C C   . SER B 2 89  ? 33.050  77.151  42.484  1.000 52.243  ? 89  SER HHH C   1 
ATOM   2240  O O   . SER B 2 89  ? 32.115  76.841  43.232  1.000 57.956  ? 89  SER HHH O   1 
ATOM   2241  C CB  . SER B 2 89  ? 32.896  79.647  42.338  1.000 58.621  ? 89  SER HHH CB  1 
ATOM   2242  O OG  . SER B 2 89  ? 32.833  79.734  40.918  1.000 68.781  ? 89  SER HHH OG  1 
ATOM   2243  N N   . ASP B 2 90  ? 33.500  76.395  41.471  1.000 46.728  ? 90  ASP HHH N   1 
ATOM   2244  C CA  . ASP B 2 90  ? 32.918  75.089  41.055  1.000 45.943  ? 90  ASP HHH CA  1 
ATOM   2245  C C   . ASP B 2 90  ? 33.348  73.963  42.007  1.000 43.564  ? 90  ASP HHH C   1 
ATOM   2246  O O   . ASP B 2 90  ? 32.910  72.817  41.799  1.000 41.072  ? 90  ASP HHH O   1 
ATOM   2247  C CB  . ASP B 2 90  ? 33.306  74.741  39.615  1.000 48.788  ? 90  ASP HHH CB  1 
ATOM   2248  C CG  . ASP B 2 90  ? 32.444  75.428  38.567  1.000 55.626  ? 90  ASP HHH CG  1 
ATOM   2249  O OD1 . ASP B 2 90  ? 31.210  75.397  38.716  1.000 65.428  ? 90  ASP HHH OD1 1 
ATOM   2250  O OD2 . ASP B 2 90  ? 33.009  75.985  37.605  1.000 58.000  ? 90  ASP HHH OD2 1 
ATOM   2251  N N   . THR B 2 91  ? 34.187  74.266  43.000  1.000 43.749  ? 91  THR HHH N   1 
ATOM   2252  C CA  . THR B 2 91  ? 34.687  73.295  44.005  1.000 43.949  ? 91  THR HHH CA  1 
ATOM   2253  C C   . THR B 2 91  ? 33.514  72.814  44.841  1.000 47.588  ? 91  THR HHH C   1 
ATOM   2254  O O   . THR B 2 91  ? 32.963  73.636  45.619  1.000 52.606  ? 91  THR HHH O   1 
ATOM   2255  C CB  . THR B 2 91  ? 35.714  73.898  44.966  1.000 40.276  ? 91  THR HHH CB  1 
ATOM   2256  O OG1 . THR B 2 91  ? 36.847  74.241  44.173  1.000 39.238  ? 91  THR HHH OG1 1 
ATOM   2257  C CG2 . THR B 2 91  ? 36.093  72.952  46.084  1.000 39.087  ? 91  THR HHH CG2 1 
ATOM   2258  N N   . ALA B 2 92  ? 33.165  71.541  44.697  1.000 48.092  ? 92  ALA HHH N   1 
ATOM   2259  C CA  . ALA B 2 92  ? 32.070  70.920  45.461  1.000 52.593  ? 92  ALA HHH CA  1 
ATOM   2260  C C   . ALA B 2 92  ? 32.167  69.407  45.364  1.000 50.963  ? 92  ALA HHH C   1 
ATOM   2261  O O   . ALA B 2 92  ? 33.195  68.912  44.908  1.000 55.274  ? 92  ALA HHH O   1 
ATOM   2262  C CB  . ALA B 2 92  ? 30.756  71.406  44.924  1.000 58.603  ? 92  ALA HHH CB  1 
ATOM   2263  N N   . ILE B 2 93  ? 31.131  68.720  45.833  1.000 47.270  ? 93  ILE HHH N   1 
ATOM   2264  C CA  . ILE B 2 93  ? 30.918  67.275  45.567  1.000 45.871  ? 93  ILE HHH CA  1 
ATOM   2265  C C   . ILE B 2 93  ? 29.630  67.178  44.757  1.000 41.730  ? 93  ILE HHH C   1 
ATOM   2266  O O   . ILE B 2 93  ? 28.645  67.812  45.133  1.000 44.375  ? 93  ILE HHH O   1 
ATOM   2267  C CB  . ILE B 2 93  ? 30.909  66.428  46.856  1.000 45.257  ? 93  ILE HHH CB  1 
ATOM   2268  C CG1 . ILE B 2 93  ? 30.412  65.015  46.569  1.000 49.131  ? 93  ILE HHH CG1 1 
ATOM   2269  C CG2 . ILE B 2 93  ? 30.103  67.083  47.952  1.000 46.566  ? 93  ILE HHH CG2 1 
ATOM   2270  C CD1 . ILE B 2 93  ? 30.527  64.073  47.739  1.000 55.683  ? 93  ILE HHH CD1 1 
ATOM   2271  N N   . TYR B 2 94  ? 29.691  66.452  43.648  1.000 38.212  ? 94  TYR HHH N   1 
ATOM   2272  C CA  . TYR B 2 94  ? 28.618  66.312  42.644  1.000 35.988  ? 94  TYR HHH CA  1 
ATOM   2273  C C   . TYR B 2 94  ? 28.072  64.881  42.703  1.000 32.783  ? 94  TYR HHH C   1 
ATOM   2274  O O   . TYR B 2 94  ? 28.782  63.932  42.329  1.000 29.153  ? 94  TYR HHH O   1 
ATOM   2275  C CB  . TYR B 2 94  ? 29.176  66.685  41.270  1.000 39.101  ? 94  TYR HHH CB  1 
ATOM   2276  C CG  . TYR B 2 94  ? 29.607  68.123  41.136  1.000 41.294  ? 94  TYR HHH CG  1 
ATOM   2277  C CD1 . TYR B 2 94  ? 28.734  69.073  40.651  1.000 42.081  ? 94  TYR HHH CD1 1 
ATOM   2278  C CD2 . TYR B 2 94  ? 30.867  68.547  41.506  1.000 43.664  ? 94  TYR HHH CD2 1 
ATOM   2279  C CE1 . TYR B 2 94  ? 29.096  70.401  40.535  1.000 45.971  ? 94  TYR HHH CE1 1 
ATOM   2280  C CE2 . TYR B 2 94  ? 31.247  69.876  41.394  1.000 46.253  ? 94  TYR HHH CE2 1 
ATOM   2281  C CZ  . TYR B 2 94  ? 30.361  70.812  40.896  1.000 46.662  ? 94  TYR HHH CZ  1 
ATOM   2282  O OH  . TYR B 2 94  ? 30.697  72.135  40.761  1.000 47.777  ? 94  TYR HHH OH  1 
ATOM   2283  N N   . TYR B 2 95  ? 26.836  64.746  43.186  1.000 31.550  ? 95  TYR HHH N   1 
ATOM   2284  C CA  . TYR B 2 95  ? 26.044  63.492  43.170  1.000 30.127  ? 95  TYR HHH CA  1 
ATOM   2285  C C   . TYR B 2 95  ? 25.275  63.380  41.853  1.000 30.248  ? 95  TYR HHH C   1 
ATOM   2286  O O   . TYR B 2 95  ? 24.749  64.370  41.376  1.000 28.734  ? 95  TYR HHH O   1 
ATOM   2287  C CB  . TYR B 2 95  ? 25.077  63.468  44.351  1.000 28.001  ? 95  TYR HHH CB  1 
ATOM   2288  C CG  . TYR B 2 95  ? 25.755  63.524  45.688  1.000 27.212  ? 95  TYR HHH CG  1 
ATOM   2289  C CD1 . TYR B 2 95  ? 26.297  62.385  46.261  1.000 27.789  ? 95  TYR HHH CD1 1 
ATOM   2290  C CD2 . TYR B 2 95  ? 25.863  64.719  46.375  1.000 29.014  ? 95  TYR HHH CD2 1 
ATOM   2291  C CE1 . TYR B 2 95  ? 26.930  62.426  47.492  1.000 29.765  ? 95  TYR HHH CE1 1 
ATOM   2292  C CE2 . TYR B 2 95  ? 26.493  64.783  47.608  1.000 31.665  ? 95  TYR HHH CE2 1 
ATOM   2293  C CZ  . TYR B 2 95  ? 27.028  63.631  48.168  1.000 32.674  ? 95  TYR HHH CZ  1 
ATOM   2294  O OH  . TYR B 2 95  ? 27.657  63.698  49.378  1.000 35.235  ? 95  TYR HHH OH  1 
ATOM   2295  N N   . CYS B 2 96  ? 25.223  62.184  41.275  1.000 31.428  ? 96  CYS HHH N   1 
ATOM   2296  C CA  . CYS B 2 96  ? 24.199  61.822  40.281  1.000 33.335  ? 96  CYS HHH CA  1 
ATOM   2297  C C   . CYS B 2 96  ? 23.169  61.004  41.049  1.000 35.519  ? 96  CYS HHH C   1 
ATOM   2298  O O   . CYS B 2 96  ? 23.574  60.213  41.902  1.000 33.781  ? 96  CYS HHH O   1 
ATOM   2299  C CB  . CYS B 2 96  ? 24.772  61.090  39.078  1.000 32.795  ? 96  CYS HHH CB  1 
ATOM   2300  S SG  . CYS B 2 96  ? 25.484  59.504  39.529  1.000 34.987  ? 96  CYS HHH SG  1 
ATOM   2301  N N   . ALA B 2 97  ? 21.890  61.281  40.817  1.000 40.012  ? 97  ALA HHH N   1 
ATOM   2302  C CA  . ALA B 2 97  ? 20.754  60.521  41.363  1.000 43.539  ? 97  ALA HHH CA  1 
ATOM   2303  C C   . ALA B 2 97  ? 19.905  59.999  40.206  1.000 46.821  ? 97  ALA HHH C   1 
ATOM   2304  O O   . ALA B 2 97  ? 19.999  60.543  39.096  1.000 50.220  ? 97  ALA HHH O   1 
ATOM   2305  C CB  . ALA B 2 97  ? 19.965  61.409  42.280  1.000 49.153  ? 97  ALA HHH CB  1 
ATOM   2306  N N   . GLY B 2 98  ? 19.102  58.973  40.468  1.000 54.910  ? 98  GLY HHH N   1 
ATOM   2307  C CA  . GLY B 2 98  ? 18.271  58.286  39.467  1.000 58.356  ? 98  GLY HHH CA  1 
ATOM   2308  C C   . GLY B 2 98  ? 16.827  58.189  39.928  1.000 66.847  ? 98  GLY HHH C   1 
ATOM   2309  O O   . GLY B 2 98  ? 16.578  57.667  41.041  1.000 64.682  ? 98  GLY HHH O   1 
ATOM   2310  N N   . GLY B 2 99  ? 15.913  58.696  39.098  1.000 77.536  ? 99  GLY HHH N   1 
ATOM   2311  C CA  . GLY B 2 99  ? 14.468  58.398  39.148  1.000 77.374  ? 99  GLY HHH CA  1 
ATOM   2312  C C   . GLY B 2 99  ? 14.040  57.529  37.973  1.000 73.001  ? 99  GLY HHH C   1 
ATOM   2313  O O   . GLY B 2 99  ? 14.486  57.791  36.825  1.000 67.775  ? 99  GLY HHH O   1 
ATOM   2314  N N   . SER B 2 100 ? 13.191  56.530  38.232  1.000 72.001  ? 100 SER HHH N   1 
ATOM   2315  C CA  . SER B 2 100 ? 12.665  55.601  37.194  1.000 72.643  ? 100 SER HHH CA  1 
ATOM   2316  C C   . SER B 2 100 ? 11.652  56.328  36.286  1.000 66.293  ? 100 SER HHH C   1 
ATOM   2317  O O   . SER B 2 100 ? 11.223  55.750  35.289  1.000 71.666  ? 100 SER HHH O   1 
ATOM   2318  C CB  . SER B 2 100 ? 12.102  54.356  37.828  1.000 70.908  ? 100 SER HHH CB  1 
ATOM   2319  O OG  . SER B 2 100 ? 11.466  54.677  39.048  1.000 77.978  ? 100 SER HHH OG  1 
ATOM   2320  N N   . GLY B 2 101 ? 11.323  57.583  36.577  1.000 56.435  ? 101 GLY HHH N   1 
ATOM   2321  C CA  . GLY B 2 101 ? 10.523  58.423  35.676  1.000 51.569  ? 101 GLY HHH CA  1 
ATOM   2322  C C   . GLY B 2 101 ? 10.930  59.881  35.743  1.000 50.291  ? 101 GLY HHH C   1 
ATOM   2323  O O   . GLY B 2 101 ? 11.780  60.269  36.579  1.000 51.373  ? 101 GLY HHH O   1 
ATOM   2324  N N   . ILE B 2 102 ? 10.382  60.667  34.838  1.000 48.533  ? 102 ILE HHH N   1 
ATOM   2325  C CA  . ILE B 2 102 ? 10.562  62.135  34.849  1.000 54.225  ? 102 ILE HHH CA  1 
ATOM   2326  C C   . ILE B 2 102 ? 9.388   62.491  35.721  1.000 54.862  ? 102 ILE HHH C   1 
ATOM   2327  O O   . ILE B 2 102 ? 8.334   62.000  35.362  1.000 70.291  ? 102 ILE HHH O   1 
ATOM   2328  C CB  . ILE B 2 102 ? 10.304  62.882  33.537  1.000 54.792  ? 102 ILE HHH CB  1 
ATOM   2329  C CG1 . ILE B 2 102 ? 10.587  64.373  33.666  1.000 49.489  ? 102 ILE HHH CG1 1 
ATOM   2330  C CG2 . ILE B 2 102 ? 8.868   62.713  33.113  1.000 62.269  ? 102 ILE HHH CG2 1 
ATOM   2331  C CD1 . ILE B 2 102 ? 12.007  64.705  33.992  1.000 52.543  ? 102 ILE HHH CD1 1 
ATOM   2332  N N   . SER B 2 103 ? 9.564   63.297  36.747  1.000 52.966  ? 103 SER HHH N   1 
ATOM   2333  C CA  . SER B 2 103 ? 8.562   63.708  37.778  1.000 50.625  ? 103 SER HHH CA  1 
ATOM   2334  C C   . SER B 2 103 ? 8.353   62.529  38.731  1.000 52.079  ? 103 SER HHH C   1 
ATOM   2335  O O   . SER B 2 103 ? 7.215   62.095  39.065  1.000 48.439  ? 103 SER HHH O   1 
ATOM   2336  C CB  . SER B 2 103 ? 7.292   64.273  37.208  1.000 52.531  ? 103 SER HHH CB  1 
ATOM   2337  O OG  . SER B 2 103 ? 6.817   65.327  38.024  1.000 54.007  ? 103 SER HHH OG  1 
ATOM   2338  N N   . THR B 2 104 ? 9.505   62.087  39.206  1.000 60.140  ? 104 THR HHH N   1 
ATOM   2339  C CA  . THR B 2 104 ? 9.732   60.910  40.057  1.000 57.542  ? 104 THR HHH CA  1 
ATOM   2340  C C   . THR B 2 104 ? 10.785  61.298  41.087  1.000 55.354  ? 104 THR HHH C   1 
ATOM   2341  O O   . THR B 2 104 ? 11.718  62.068  40.793  1.000 55.648  ? 104 THR HHH O   1 
ATOM   2342  C CB  . THR B 2 104 ? 10.130  59.722  39.175  1.000 64.785  ? 104 THR HHH CB  1 
ATOM   2343  O OG1 . THR B 2 104 ? 8.943   59.353  38.475  1.000 64.968  ? 104 THR HHH OG1 1 
ATOM   2344  C CG2 . THR B 2 104 ? 10.709  58.546  39.936  1.000 67.490  ? 104 THR HHH CG2 1 
ATOM   2345  N N   . PRO B 2 105 ? 10.670  60.760  42.322  1.000 52.323  ? 105 PRO HHH N   1 
ATOM   2346  C CA  . PRO B 2 105 ? 11.687  60.982  43.343  1.000 50.189  ? 105 PRO HHH CA  1 
ATOM   2347  C C   . PRO B 2 105 ? 12.985  60.296  42.896  1.000 51.528  ? 105 PRO HHH C   1 
ATOM   2348  O O   . PRO B 2 105 ? 12.920  59.300  42.168  1.000 49.708  ? 105 PRO HHH O   1 
ATOM   2349  C CB  . PRO B 2 105 ? 11.092  60.303  44.587  1.000 47.460  ? 105 PRO HHH CB  1 
ATOM   2350  C CG  . PRO B 2 105 ? 10.236  59.187  44.012  1.000 48.953  ? 105 PRO HHH CG  1 
ATOM   2351  C CD  . PRO B 2 105 ? 9.617   59.833  42.788  1.000 52.975  ? 105 PRO HHH CD  1 
ATOM   2352  N N   . MET B 2 106 ? 14.123  60.798  43.369  1.000 52.725  ? 106 MET HHH N   1 
ATOM   2353  C CA  . MET B 2 106 ? 15.441  60.153  43.157  1.000 50.630  ? 106 MET HHH CA  1 
ATOM   2354  C C   . MET B 2 106 ? 15.634  59.004  44.155  1.000 47.426  ? 106 MET HHH C   1 
ATOM   2355  O O   . MET B 2 106 ? 16.065  59.273  45.297  1.000 40.554  ? 106 MET HHH O   1 
ATOM   2356  C CB  . MET B 2 106 ? 16.525  61.215  43.275  1.000 54.535  ? 106 MET HHH CB  1 
ATOM   2357  C CG  . MET B 2 106 ? 16.391  62.227  42.159  1.000 58.193  ? 106 MET HHH CG  1 
ATOM   2358  S SD  . MET B 2 106 ? 16.990  63.863  42.608  1.000 66.462  ? 106 MET HHH SD  1 
ATOM   2359  C CE  . MET B 2 106 ? 17.261  64.443  40.936  1.000 70.304  ? 106 MET HHH CE  1 
ATOM   2360  N N   . ASP B 2 107 ? 15.291  57.777  43.710  1.000 48.994  ? 107 ASP HHH N   1 
ATOM   2361  C CA  . ASP B 2 107 ? 15.315  56.492  44.472  1.000 48.693  ? 107 ASP HHH CA  1 
ATOM   2362  C C   . ASP B 2 107 ? 16.763  56.177  44.811  1.000 48.732  ? 107 ASP HHH C   1 
ATOM   2363  O O   . ASP B 2 107 ? 17.022  55.859  45.988  1.000 55.319  ? 107 ASP HHH O   1 
ATOM   2364  C CB  . ASP B 2 107 ? 14.854  55.248  43.686  1.000 51.906  ? 107 ASP HHH CB  1 
ATOM   2365  C CG  . ASP B 2 107 ? 13.577  55.345  42.870  1.000 63.778  ? 107 ASP HHH CG  1 
ATOM   2366  O OD1 . ASP B 2 107 ? 12.559  55.824  43.397  1.000 85.858  ? 107 ASP HHH OD1 1 
ATOM   2367  O OD2 . ASP B 2 107 ? 13.599  54.917  41.715  1.000 67.825  ? 107 ASP HHH OD2 1 
ATOM   2368  N N   . VAL B 2 108 ? 17.626  56.271  43.785  1.000 44.898  ? 108 VAL HHH N   1 
ATOM   2369  C CA  . VAL B 2 108 ? 19.017  55.735  43.711  1.000 42.216  ? 108 VAL HHH CA  1 
ATOM   2370  C C   . VAL B 2 108 ? 20.006  56.891  43.568  1.000 40.608  ? 108 VAL HHH C   1 
ATOM   2371  O O   . VAL B 2 108 ? 19.752  57.781  42.754  1.000 39.719  ? 108 VAL HHH O   1 
ATOM   2372  C CB  . VAL B 2 108 ? 19.132  54.764  42.526  1.000 42.511  ? 108 VAL HHH CB  1 
ATOM   2373  C CG1 . VAL B 2 108 ? 20.573  54.393  42.228  1.000 43.844  ? 108 VAL HHH CG1 1 
ATOM   2374  C CG2 . VAL B 2 108 ? 18.279  53.524  42.769  1.000 46.718  ? 108 VAL HHH CG2 1 
ATOM   2375  N N   . TRP B 2 109 ? 21.107  56.844  44.322  1.000 41.530  ? 109 TRP HHH N   1 
ATOM   2376  C CA  . TRP B 2 109 ? 22.181  57.880  44.344  1.000 39.621  ? 109 TRP HHH CA  1 
ATOM   2377  C C   . TRP B 2 109 ? 23.564  57.257  44.072  1.000 39.360  ? 109 TRP HHH C   1 
ATOM   2378  O O   . TRP B 2 109 ? 23.809  56.102  44.475  1.000 39.797  ? 109 TRP HHH O   1 
ATOM   2379  C CB  . TRP B 2 109 ? 22.182  58.613  45.690  1.000 36.711  ? 109 TRP HHH CB  1 
ATOM   2380  C CG  . TRP B 2 109 ? 20.999  59.501  45.907  1.000 33.879  ? 109 TRP HHH CG  1 
ATOM   2381  C CD1 . TRP B 2 109 ? 19.758  59.135  46.327  1.000 32.910  ? 109 TRP HHH CD1 1 
ATOM   2382  C CD2 . TRP B 2 109 ? 20.964  60.926  45.748  1.000 31.981  ? 109 TRP HHH CD2 1 
ATOM   2383  N NE1 . TRP B 2 109 ? 18.953  60.235  46.420  1.000 33.572  ? 109 TRP HHH NE1 1 
ATOM   2384  C CE2 . TRP B 2 109 ? 19.665  61.347  46.071  1.000 31.327  ? 109 TRP HHH CE2 1 
ATOM   2385  C CE3 . TRP B 2 109 ? 21.904  61.884  45.369  1.000 31.493  ? 109 TRP HHH CE3 1 
ATOM   2386  C CZ2 . TRP B 2 109 ? 19.277  62.679  46.009  1.000 31.604  ? 109 TRP HHH CZ2 1 
ATOM   2387  C CZ3 . TRP B 2 109 ? 21.526  63.206  45.321  1.000 31.022  ? 109 TRP HHH CZ3 1 
ATOM   2388  C CH2 . TRP B 2 109 ? 20.226  63.594  45.622  1.000 31.261  ? 109 TRP HHH CH2 1 
ATOM   2389  N N   . GLY B 2 110 ? 24.446  58.011  43.417  1.000 38.679  ? 110 GLY HHH N   1 
ATOM   2390  C CA  . GLY B 2 110 ? 25.887  57.714  43.329  1.000 37.825  ? 110 GLY HHH CA  1 
ATOM   2391  C C   . GLY B 2 110 ? 26.573  58.009  44.646  1.000 37.460  ? 110 GLY HHH C   1 
ATOM   2392  O O   . GLY B 2 110 ? 25.933  58.606  45.511  1.000 36.617  ? 110 GLY HHH O   1 
ATOM   2393  N N   . GLN B 2 111 ? 27.830  57.592  44.797  1.000 38.839  ? 111 GLN HHH N   1 
ATOM   2394  C CA  . GLN B 2 111 ? 28.632  57.796  46.036  1.000 39.103  ? 111 GLN HHH CA  1 
ATOM   2395  C C   . GLN B 2 111 ? 29.113  59.251  46.102  1.000 39.149  ? 111 GLN HHH C   1 
ATOM   2396  O O   . GLN B 2 111 ? 29.505  59.686  47.178  1.000 37.773  ? 111 GLN HHH O   1 
ATOM   2397  C CB  . GLN B 2 111 ? 29.798  56.808  46.086  1.000 38.262  ? 111 GLN HHH CB  1 
ATOM   2398  C CG  . GLN B 2 111 ? 30.901  57.073  45.069  1.000 38.155  ? 111 GLN HHH CG  1 
ATOM   2399  C CD  . GLN B 2 111 ? 30.703  56.394  43.736  1.000 38.043  ? 111 GLN HHH CD  1 
ATOM   2400  O OE1 . GLN B 2 111 ? 29.836  55.558  43.549  1.000 44.055  ? 111 GLN HHH OE1 1 
ATOM   2401  N NE2 . GLN B 2 111 ? 31.519  56.761  42.770  1.000 38.243  ? 111 GLN HHH NE2 1 
ATOM   2402  N N   . GLY B 2 112 ? 29.066  59.972  44.981  1.000 41.552  ? 112 GLY HHH N   1 
ATOM   2403  C CA  . GLY B 2 112 ? 29.518  61.371  44.882  1.000 41.117  ? 112 GLY HHH CA  1 
ATOM   2404  C C   . GLY B 2 112 ? 30.895  61.430  44.263  1.000 40.974  ? 112 GLY HHH C   1 
ATOM   2405  O O   . GLY B 2 112 ? 31.681  60.499  44.518  1.000 47.737  ? 112 GLY HHH O   1 
ATOM   2406  N N   . THR B 2 113 ? 31.156  62.438  43.433  1.000 37.980  ? 113 THR HHH N   1 
ATOM   2407  C CA  . THR B 2 113 ? 32.496  62.741  42.880  1.000 36.217  ? 113 THR HHH CA  1 
ATOM   2408  C C   . THR B 2 113 ? 32.940  64.072  43.467  1.000 37.005  ? 113 THR HHH C   1 
ATOM   2409  O O   . THR B 2 113 ? 32.303  65.071  43.152  1.000 38.426  ? 113 THR HHH O   1 
ATOM   2410  C CB  . THR B 2 113 ? 32.496  62.857  41.354  1.000 33.792  ? 113 THR HHH CB  1 
ATOM   2411  O OG1 . THR B 2 113 ? 32.077  61.627  40.771  1.000 31.679  ? 113 THR HHH OG1 1 
ATOM   2412  C CG2 . THR B 2 113 ? 33.860  63.217  40.818  1.000 33.978  ? 113 THR HHH CG2 1 
ATOM   2413  N N   . THR B 2 114 ? 33.980  64.077  44.296  1.000 40.705  ? 114 THR HHH N   1 
ATOM   2414  C CA  . THR B 2 114 ? 34.563  65.314  44.884  1.000 38.527  ? 114 THR HHH CA  1 
ATOM   2415  C C   . THR B 2 114 ? 35.445  66.014  43.836  1.000 37.592  ? 114 THR HHH C   1 
ATOM   2416  O O   . THR B 2 114 ? 36.405  65.410  43.353  1.000 36.417  ? 114 THR HHH O   1 
ATOM   2417  C CB  . THR B 2 114 ? 35.325  64.985  46.172  1.000 35.491  ? 114 THR HHH CB  1 
ATOM   2418  O OG1 . THR B 2 114 ? 34.396  64.397  47.080  1.000 32.220  ? 114 THR HHH OG1 1 
ATOM   2419  C CG2 . THR B 2 114 ? 35.992  66.201  46.774  1.000 34.844  ? 114 THR HHH CG2 1 
ATOM   2420  N N   . VAL B 2 115 ? 35.105  67.246  43.485  1.000 38.175  ? 115 VAL HHH N   1 
ATOM   2421  C CA  . VAL B 2 115 ? 35.896  68.100  42.557  1.000 38.745  ? 115 VAL HHH CA  1 
ATOM   2422  C C   . VAL B 2 115 ? 36.473  69.254  43.377  1.000 38.781  ? 115 VAL HHH C   1 
ATOM   2423  O O   . VAL B 2 115 ? 35.694  69.993  44.021  1.000 37.808  ? 115 VAL HHH O   1 
ATOM   2424  C CB  . VAL B 2 115 ? 35.019  68.609  41.401  1.000 40.866  ? 115 VAL HHH CB  1 
ATOM   2425  C CG1 . VAL B 2 115 ? 35.769  69.577  40.499  1.000 43.654  ? 115 VAL HHH CG1 1 
ATOM   2426  C CG2 . VAL B 2 115 ? 34.427  67.455  40.608  1.000 40.889  ? 115 VAL HHH CG2 1 
ATOM   2427  N N   . THR B 2 116 ? 37.796  69.398  43.364  1.000 39.614  ? 116 THR HHH N   1 
ATOM   2428  C CA  . THR B 2 116 ? 38.500  70.535  43.994  1.000 38.595  ? 116 THR HHH CA  1 
ATOM   2429  C C   . THR B 2 116 ? 39.139  71.346  42.878  1.000 38.018  ? 116 THR HHH C   1 
ATOM   2430  O O   . THR B 2 116 ? 39.977  70.787  42.171  1.000 37.462  ? 116 THR HHH O   1 
ATOM   2431  C CB  . THR B 2 116 ? 39.562  70.049  44.975  1.000 41.556  ? 116 THR HHH CB  1 
ATOM   2432  O OG1 . THR B 2 116 ? 38.996  69.008  45.774  1.000 43.474  ? 116 THR HHH OG1 1 
ATOM   2433  C CG2 . THR B 2 116 ? 40.121  71.174  45.820  1.000 42.610  ? 116 THR HHH CG2 1 
ATOM   2434  N N   . VAL B 2 117 ? 38.713  72.594  42.706  1.000 39.994  ? 117 VAL HHH N   1 
ATOM   2435  C CA  . VAL B 2 117 ? 39.338  73.544  41.742  1.000 41.443  ? 117 VAL HHH CA  1 
ATOM   2436  C C   . VAL B 2 117 ? 40.080  74.583  42.583  1.000 39.650  ? 117 VAL HHH C   1 
ATOM   2437  O O   . VAL B 2 117 ? 39.451  75.223  43.446  1.000 43.686  ? 117 VAL HHH O   1 
ATOM   2438  C CB  . VAL B 2 117 ? 38.296  74.155  40.780  1.000 44.208  ? 117 VAL HHH CB  1 
ATOM   2439  C CG1 . VAL B 2 117 ? 38.936  75.021  39.715  1.000 46.031  ? 117 VAL HHH CG1 1 
ATOM   2440  C CG2 . VAL B 2 117 ? 37.457  73.090  40.101  1.000 45.152  ? 117 VAL HHH CG2 1 
ATOM   2441  N N   . SER B 2 118 ? 41.391  74.689  42.394  1.000 38.521  ? 118 SER HHH N   1 
ATOM   2442  C CA  . SER B 2 118 ? 42.292  75.582  43.174  1.000 40.414  ? 118 SER HHH CA  1 
ATOM   2443  C C   . SER B 2 118 ? 43.572  75.780  42.372  1.000 41.914  ? 118 SER HHH C   1 
ATOM   2444  O O   . SER B 2 118 ? 44.046  74.794  41.748  1.000 41.677  ? 118 SER HHH O   1 
ATOM   2445  C CB  . SER B 2 118 ? 42.574  75.030  44.566  1.000 39.800  ? 118 SER HHH CB  1 
ATOM   2446  O OG  . SER B 2 118 ? 43.568  75.765  45.268  1.000 34.958  ? 118 SER HHH OG  1 
ATOM   2447  N N   . SER B 2 119 ? 44.089  77.008  42.374  1.000 42.868  ? 119 SER HHH N   1 
ATOM   2448  C CA  . SER B 2 119 ? 45.384  77.349  41.730  1.000 45.714  ? 119 SER HHH CA  1 
ATOM   2449  C C   . SER B 2 119 ? 46.550  76.742  42.533  1.000 41.195  ? 119 SER HHH C   1 
ATOM   2450  O O   . SER B 2 119 ? 47.674  76.756  42.022  1.000 39.637  ? 119 SER HHH O   1 
ATOM   2451  C CB  . SER B 2 119 ? 45.518  78.833  41.565  1.000 46.644  ? 119 SER HHH CB  1 
ATOM   2452  O OG  . SER B 2 119 ? 45.518  79.457  42.834  1.000 50.716  ? 119 SER HHH OG  1 
ATOM   2453  N N   . ALA B 2 120 ? 46.284  76.210  43.731  1.000 37.665  ? 120 ALA HHH N   1 
ATOM   2454  C CA  . ALA B 2 120 ? 47.267  75.502  44.585  1.000 35.210  ? 120 ALA HHH CA  1 
ATOM   2455  C C   . ALA B 2 120 ? 47.800  74.257  43.865  1.000 34.401  ? 120 ALA HHH C   1 
ATOM   2456  O O   . ALA B 2 120 ? 47.006  73.551  43.200  1.000 30.835  ? 120 ALA HHH O   1 
ATOM   2457  C CB  . ALA B 2 120 ? 46.629  75.123  45.898  1.000 35.010  ? 120 ALA HHH CB  1 
ATOM   2458  N N   . SER B 2 121 ? 49.098  74.004  44.038  1.000 35.923  ? 121 SER HHH N   1 
ATOM   2459  C CA  . SER B 2 121 ? 49.840  72.809  43.555  1.000 38.179  ? 121 SER HHH CA  1 
ATOM   2460  C C   . SER B 2 121 ? 49.906  71.779  44.673  1.000 34.233  ? 121 SER HHH C   1 
ATOM   2461  O O   . SER B 2 121 ? 49.887  72.178  45.845  1.000 30.370  ? 121 SER HHH O   1 
ATOM   2462  C CB  . SER B 2 121 ? 51.249  73.150  43.133  1.000 43.073  ? 121 SER HHH CB  1 
ATOM   2463  O OG  . SER B 2 121 ? 51.270  73.961  41.972  1.000 50.166  ? 121 SER HHH OG  1 
ATOM   2464  N N   . THR B 2 122 ? 50.025  70.505  44.317  1.000 35.206  ? 122 THR HHH N   1 
ATOM   2465  C CA  . THR B 2 122 ? 50.220  69.406  45.293  1.000 36.866  ? 122 THR HHH CA  1 
ATOM   2466  C C   . THR B 2 122 ? 51.323  69.812  46.265  1.000 36.784  ? 122 THR HHH C   1 
ATOM   2467  O O   . THR B 2 122 ? 52.432  70.134  45.800  1.000 46.714  ? 122 THR HHH O   1 
ATOM   2468  C CB  . THR B 2 122 ? 50.607  68.093  44.611  1.000 37.246  ? 122 THR HHH CB  1 
ATOM   2469  O OG1 . THR B 2 122 ? 49.537  67.765  43.736  1.000 41.706  ? 122 THR HHH OG1 1 
ATOM   2470  C CG2 . THR B 2 122 ? 50.824  66.967  45.588  1.000 36.691  ? 122 THR HHH CG2 1 
ATOM   2471  N N   . LYS B 2 123 ? 51.023  69.815  47.556  1.000 34.004  ? 123 LYS HHH N   1 
ATOM   2472  C CA  . LYS B 2 123 ? 52.035  70.067  48.604  1.000 34.064  ? 123 LYS HHH CA  1 
ATOM   2473  C C   . LYS B 2 123 ? 51.777  69.165  49.813  1.000 31.424  ? 123 LYS HHH C   1 
ATOM   2474  O O   . LYS B 2 123 ? 50.654  69.155  50.328  1.000 27.889  ? 123 LYS HHH O   1 
ATOM   2475  C CB  . LYS B 2 123 ? 52.059  71.529  49.046  1.000 38.154  ? 123 LYS HHH CB  1 
ATOM   2476  C CG  . LYS B 2 123 ? 53.249  71.796  49.942  1.000 44.328  ? 123 LYS HHH CG  1 
ATOM   2477  C CD  . LYS B 2 123 ? 53.217  72.986  50.823  1.000 49.491  ? 123 LYS HHH CD  1 
ATOM   2478  C CE  . LYS B 2 123 ? 54.277  72.754  51.884  1.000 63.020  ? 123 LYS HHH CE  1 
ATOM   2479  N NZ  . LYS B 2 123 ? 54.503  73.922  52.763  1.000 76.757  ? 123 LYS HHH NZ  1 
ATOM   2480  N N   . GLY B 2 124 ? 52.825  68.477  50.274  1.000 31.200  ? 124 GLY HHH N   1 
ATOM   2481  C CA  . GLY B 2 124 ? 52.776  67.563  51.427  1.000 29.189  ? 124 GLY HHH CA  1 
ATOM   2482  C C   . GLY B 2 124 ? 52.702  68.341  52.725  1.000 30.029  ? 124 GLY HHH C   1 
ATOM   2483  O O   . GLY B 2 124 ? 53.225  69.445  52.836  1.000 31.478  ? 124 GLY HHH O   1 
ATOM   2484  N N   . PRO B 2 125 ? 52.049  67.779  53.755  1.000 34.070  ? 125 PRO HHH N   1 
ATOM   2485  C CA  . PRO B 2 125 ? 51.854  68.480  55.017  1.000 34.350  ? 125 PRO HHH CA  1 
ATOM   2486  C C   . PRO B 2 125 ? 53.142  68.552  55.826  1.000 35.736  ? 125 PRO HHH C   1 
ATOM   2487  O O   . PRO B 2 125 ? 53.998  67.721  55.670  1.000 37.490  ? 125 PRO HHH O   1 
ATOM   2488  C CB  . PRO B 2 125 ? 50.879  67.602  55.804  1.000 34.511  ? 125 PRO HHH CB  1 
ATOM   2489  C CG  . PRO B 2 125 ? 51.088  66.214  55.226  1.000 34.904  ? 125 PRO HHH CG  1 
ATOM   2490  C CD  . PRO B 2 125 ? 51.473  66.427  53.773  1.000 37.152  ? 125 PRO HHH CD  1 
ATOM   2491  N N   . SER B 2 126 ? 53.211  69.543  56.697  1.000 39.314  ? 126 SER HHH N   1 
ATOM   2492  C CA  . SER B 2 126 ? 54.255  69.672  57.738  1.000 40.323  ? 126 SER HHH CA  1 
ATOM   2493  C C   . SER B 2 126 ? 53.600  69.291  59.067  1.000 37.093  ? 126 SER HHH C   1 
ATOM   2494  O O   . SER B 2 126 ? 52.510  69.808  59.348  1.000 39.306  ? 126 SER HHH O   1 
ATOM   2495  C CB  . SER B 2 126 ? 54.835  71.078  57.744  1.000 42.793  ? 126 SER HHH CB  1 
ATOM   2496  O OG  . SER B 2 126 ? 55.068  71.556  56.415  1.000 45.452  ? 126 SER HHH OG  1 
ATOM   2497  N N   . VAL B 2 127 ? 54.199  68.376  59.822  1.000 34.666  ? 127 VAL HHH N   1 
ATOM   2498  C CA  . VAL B 2 127 ? 53.592  67.862  61.076  1.000 35.486  ? 127 VAL HHH CA  1 
ATOM   2499  C C   . VAL B 2 127 ? 54.348  68.426  62.274  1.000 35.092  ? 127 VAL HHH C   1 
ATOM   2500  O O   . VAL B 2 127 ? 55.566  68.253  62.314  1.000 40.096  ? 127 VAL HHH O   1 
ATOM   2501  C CB  . VAL B 2 127 ? 53.575  66.332  61.097  1.000 35.743  ? 127 VAL HHH CB  1 
ATOM   2502  C CG1 . VAL B 2 127 ? 52.800  65.839  62.305  1.000 37.670  ? 127 VAL HHH CG1 1 
ATOM   2503  C CG2 . VAL B 2 127 ? 52.968  65.797  59.814  1.000 36.470  ? 127 VAL HHH CG2 1 
ATOM   2504  N N   . PHE B 2 128 ? 53.629  69.056  63.203  1.000 31.827  ? 128 PHE HHH N   1 
ATOM   2505  C CA  . PHE B 2 128 ? 54.187  69.707  64.411  1.000 30.776  ? 128 PHE HHH CA  1 
ATOM   2506  C C   . PHE B 2 128 ? 53.491  69.147  65.634  1.000 32.289  ? 128 PHE HHH C   1 
ATOM   2507  O O   . PHE B 2 128 ? 52.283  68.978  65.607  1.000 36.061  ? 128 PHE HHH O   1 
ATOM   2508  C CB  . PHE B 2 128 ? 53.953  71.218  64.383  1.000 30.822  ? 128 PHE HHH CB  1 
ATOM   2509  C CG  . PHE B 2 128 ? 54.443  71.906  63.138  1.000 28.993  ? 128 PHE HHH CG  1 
ATOM   2510  C CD1 . PHE B 2 128 ? 55.776  71.835  62.779  1.000 28.645  ? 128 PHE HHH CD1 1 
ATOM   2511  C CD2 . PHE B 2 128 ? 53.582  72.618  62.329  1.000 28.071  ? 128 PHE HHH CD2 1 
ATOM   2512  C CE1 . PHE B 2 128 ? 56.233  72.456  61.630  1.000 28.031  ? 128 PHE HHH CE1 1 
ATOM   2513  C CE2 . PHE B 2 128 ? 54.042  73.223  61.170  1.000 29.201  ? 128 PHE HHH CE2 1 
ATOM   2514  C CZ  . PHE B 2 128 ? 55.368  73.153  60.830  1.000 28.018  ? 128 PHE HHH CZ  1 
ATOM   2515  N N   . PRO B 2 129 ? 54.210  68.899  66.746  1.000 35.569  ? 129 PRO HHH N   1 
ATOM   2516  C CA  . PRO B 2 129 ? 53.595  68.385  67.967  1.000 36.470  ? 129 PRO HHH CA  1 
ATOM   2517  C C   . PRO B 2 129 ? 52.848  69.479  68.724  1.000 38.312  ? 129 PRO HHH C   1 
ATOM   2518  O O   . PRO B 2 129 ? 53.398  70.548  68.879  1.000 41.239  ? 129 PRO HHH O   1 
ATOM   2519  C CB  . PRO B 2 129 ? 54.779  67.924  68.829  1.000 36.656  ? 129 PRO HHH CB  1 
ATOM   2520  C CG  . PRO B 2 129 ? 55.931  68.795  68.367  1.000 35.914  ? 129 PRO HHH CG  1 
ATOM   2521  C CD  . PRO B 2 129 ? 55.658  69.093  66.902  1.000 35.951  ? 129 PRO HHH CD  1 
ATOM   2522  N N   . LEU B 2 130 ? 51.611  69.186  69.122  1.000 40.620  ? 130 LEU HHH N   1 
ATOM   2523  C CA  . LEU B 2 130 ? 50.898  69.886  70.216  1.000 40.879  ? 130 LEU HHH CA  1 
ATOM   2524  C C   . LEU B 2 130 ? 51.282  69.169  71.513  1.000 43.230  ? 130 LEU HHH C   1 
ATOM   2525  O O   . LEU B 2 130 ? 50.568  68.251  71.935  1.000 42.918  ? 130 LEU HHH O   1 
ATOM   2526  C CB  . LEU B 2 130 ? 49.395  69.884  69.939  1.000 40.801  ? 130 LEU HHH CB  1 
ATOM   2527  C CG  . LEU B 2 130 ? 49.009  70.422  68.563  1.000 42.549  ? 130 LEU HHH CG  1 
ATOM   2528  C CD1 . LEU B 2 130 ? 47.498  70.465  68.405  1.000 44.875  ? 130 LEU HHH CD1 1 
ATOM   2529  C CD2 . LEU B 2 130 ? 49.621  71.793  68.301  1.000 42.999  ? 130 LEU HHH CD2 1 
ATOM   2530  N N   . ALA B 2 131 ? 52.433  69.554  72.071  1.000 48.556  ? 131 ALA HHH N   1 
ATOM   2531  C CA  . ALA B 2 131 ? 53.065  68.954  73.267  1.000 52.373  ? 131 ALA HHH CA  1 
ATOM   2532  C C   . ALA B 2 131 ? 52.163  69.137  74.481  1.000 51.452  ? 131 ALA HHH C   1 
ATOM   2533  O O   . ALA B 2 131 ? 51.634  70.219  74.705  1.000 53.366  ? 131 ALA HHH O   1 
ATOM   2534  C CB  . ALA B 2 131 ? 54.419  69.582  73.485  1.000 55.168  ? 131 ALA HHH CB  1 
ATOM   2535  N N   . PRO B 2 132 ? 51.993  68.098  75.321  1.000 53.222  ? 132 PRO HHH N   1 
ATOM   2536  C CA  . PRO B 2 132 ? 51.173  68.212  76.529  1.000 59.275  ? 132 PRO HHH CA  1 
ATOM   2537  C C   . PRO B 2 132 ? 51.895  69.100  77.551  1.000 67.606  ? 132 PRO HHH C   1 
ATOM   2538  O O   . PRO B 2 132 ? 53.081  68.924  77.698  1.000 71.722  ? 132 PRO HHH O   1 
ATOM   2539  C CB  . PRO B 2 132 ? 51.097  66.771  77.056  1.000 57.283  ? 132 PRO HHH CB  1 
ATOM   2540  C CG  . PRO B 2 132 ? 52.372  66.109  76.536  1.000 54.612  ? 132 PRO HHH CG  1 
ATOM   2541  C CD  . PRO B 2 132 ? 52.643  66.782  75.201  1.000 54.853  ? 132 PRO HHH CD  1 
ATOM   2542  N N   . SER B 2 133 ? 51.202  70.027  78.213  1.000 80.586  ? 133 SER HHH N   1 
ATOM   2543  C CA  . SER B 2 133 ? 51.808  70.833  79.308  1.000 86.297  ? 133 SER HHH CA  1 
ATOM   2544  C C   . SER B 2 133 ? 52.214  69.864  80.417  1.000 98.753  ? 133 SER HHH C   1 
ATOM   2545  O O   . SER B 2 133 ? 51.401  68.954  80.733  1.000 91.389  ? 133 SER HHH O   1 
ATOM   2546  C CB  . SER B 2 133 ? 50.907  71.907  79.830  1.000 80.947  ? 133 SER HHH CB  1 
ATOM   2547  O OG  . SER B 2 133 ? 49.795  71.316  80.460  1.000 87.901  ? 133 SER HHH OG  1 
ATOM   2548  N N   . SER B 2 134 ? 53.450  70.013  80.907  1.000 125.851 ? 134 SER HHH N   1 
ATOM   2549  C CA  . SER B 2 134 ? 54.025  69.281  82.067  1.000 133.743 ? 134 SER HHH CA  1 
ATOM   2550  C C   . SER B 2 134 ? 53.206  69.636  83.312  1.000 137.052 ? 134 SER HHH C   1 
ATOM   2551  O O   . SER B 2 134 ? 52.836  68.702  84.056  1.000 155.579 ? 134 SER HHH O   1 
ATOM   2552  C CB  . SER B 2 134 ? 55.474  69.620  82.249  1.000 122.592 ? 134 SER HHH CB  1 
ATOM   2553  O OG  . SER B 2 134 ? 55.606  71.010  82.491  1.000 121.164 ? 134 SER HHH OG  1 
ATOM   2554  N N   . LYS B 2 135 ? 52.924  70.931  83.500  1.000 117.969 ? 135 LYS HHH N   1 
ATOM   2555  C CA  . LYS B 2 135 ? 52.006  71.441  84.553  1.000 120.400 ? 135 LYS HHH CA  1 
ATOM   2556  C C   . LYS B 2 135 ? 50.548  71.212  84.136  1.000 115.559 ? 135 LYS HHH C   1 
ATOM   2557  O O   . LYS B 2 135 ? 50.017  72.124  83.488  1.000 111.196 ? 135 LYS HHH O   1 
ATOM   2558  C CB  . LYS B 2 135 ? 52.238  72.940  84.787  1.000 126.728 ? 135 LYS HHH CB  1 
ATOM   2559  C CG  . LYS B 2 135 ? 53.536  73.317  85.495  1.000 133.599 ? 135 LYS HHH CG  1 
ATOM   2560  C CD  . LYS B 2 135 ? 53.350  74.317  86.623  1.000 126.877 ? 135 LYS HHH CD  1 
ATOM   2561  C CE  . LYS B 2 135 ? 52.800  73.673  87.880  1.000 128.941 ? 135 LYS HHH CE  1 
ATOM   2562  N NZ  . LYS B 2 135 ? 51.706  74.471  88.479  1.000 140.543 ? 135 LYS HHH NZ  1 
ATOM   2563  N N   . SER B 2 136 ? 49.954  70.049  84.452  1.000 117.667 ? 136 SER HHH N   1 
ATOM   2564  C CA  . SER B 2 136 ? 48.533  69.675  84.171  1.000 119.839 ? 136 SER HHH CA  1 
ATOM   2565  C C   . SER B 2 136 ? 47.937  68.966  85.398  1.000 129.872 ? 136 SER HHH C   1 
ATOM   2566  O O   . SER B 2 136 ? 48.722  68.639  86.312  1.000 120.862 ? 136 SER HHH O   1 
ATOM   2567  C CB  . SER B 2 136 ? 48.382  68.834  82.901  1.000 111.912 ? 136 SER HHH CB  1 
ATOM   2568  O OG  . SER B 2 136 ? 49.082  67.597  82.980  1.000 95.784  ? 136 SER HHH OG  1 
ATOM   2569  N N   . THR B 2 137 ? 46.607  68.764  85.433  1.000 142.641 ? 137 THR HHH N   1 
ATOM   2570  C CA  . THR B 2 137 ? 45.883  68.163  86.594  1.000 136.018 ? 137 THR HHH CA  1 
ATOM   2571  C C   . THR B 2 137 ? 46.421  66.730  86.780  1.000 135.787 ? 137 THR HHH C   1 
ATOM   2572  O O   . THR B 2 137 ? 46.117  65.854  85.934  1.000 145.805 ? 137 THR HHH O   1 
ATOM   2573  C CB  . THR B 2 137 ? 44.351  68.310  86.482  1.000 124.419 ? 137 THR HHH CB  1 
ATOM   2574  O OG1 . THR B 2 137 ? 43.841  67.499  85.423  1.000 134.137 ? 137 THR HHH OG1 1 
ATOM   2575  C CG2 . THR B 2 137 ? 43.883  69.735  86.259  1.000 111.960 ? 137 THR HHH CG2 1 
ATOM   2576  N N   . SER B 2 138 ? 47.204  66.530  87.852  1.000 133.717 ? 138 SER HHH N   1 
ATOM   2577  C CA  . SER B 2 138 ? 48.079  65.361  88.163  1.000 124.861 ? 138 SER HHH CA  1 
ATOM   2578  C C   . SER B 2 138 ? 47.298  64.035  88.269  1.000 134.877 ? 138 SER HHH C   1 
ATOM   2579  O O   . SER B 2 138 ? 47.834  63.010  87.804  1.000 139.616 ? 138 SER HHH O   1 
ATOM   2580  C CB  . SER B 2 138 ? 48.855  65.650  89.429  1.000 105.866 ? 138 SER HHH CB  1 
ATOM   2581  O OG  . SER B 2 138 ? 49.703  64.574  89.778  1.000 93.918  ? 138 SER HHH OG  1 
ATOM   2582  N N   . GLY B 2 139 ? 46.100  64.034  88.872  1.000 137.185 ? 139 GLY HHH N   1 
ATOM   2583  C CA  . GLY B 2 139 ? 45.231  62.844  89.004  1.000 127.086 ? 139 GLY HHH CA  1 
ATOM   2584  C C   . GLY B 2 139 ? 44.291  62.661  87.814  1.000 123.724 ? 139 GLY HHH C   1 
ATOM   2585  O O   . GLY B 2 139 ? 43.865  61.505  87.586  1.000 112.072 ? 139 GLY HHH O   1 
ATOM   2586  N N   . GLY B 2 140 ? 43.963  63.751  87.098  1.000 115.872 ? 140 GLY HHH N   1 
ATOM   2587  C CA  . GLY B 2 140 ? 43.037  63.773  85.946  1.000 103.879 ? 140 GLY HHH CA  1 
ATOM   2588  C C   . GLY B 2 140 ? 43.742  63.477  84.629  1.000 93.437  ? 140 GLY HHH C   1 
ATOM   2589  O O   . GLY B 2 140 ? 44.763  62.742  84.617  1.000 74.602  ? 140 GLY HHH O   1 
ATOM   2590  N N   . THR B 2 141 ? 43.215  64.033  83.539  1.000 86.770  ? 141 THR HHH N   1 
ATOM   2591  C CA  . THR B 2 141 ? 43.632  63.688  82.155  1.000 82.263  ? 141 THR HHH CA  1 
ATOM   2592  C C   . THR B 2 141 ? 44.419  64.858  81.541  1.000 69.406  ? 141 THR HHH C   1 
ATOM   2593  O O   . THR B 2 141 ? 44.189  66.011  81.929  1.000 75.398  ? 141 THR HHH O   1 
ATOM   2594  C CB  . THR B 2 141 ? 42.420  63.233  81.331  1.000 86.047  ? 141 THR HHH CB  1 
ATOM   2595  O OG1 . THR B 2 141 ? 42.932  62.846  80.053  1.000 110.760 ? 141 THR HHH OG1 1 
ATOM   2596  C CG2 . THR B 2 141 ? 41.342  64.288  81.184  1.000 85.278  ? 141 THR HHH CG2 1 
ATOM   2597  N N   . ALA B 2 142 ? 45.340  64.552  80.625  1.000 59.541  ? 142 ALA HHH N   1 
ATOM   2598  C CA  . ALA B 2 142 ? 46.129  65.518  79.829  1.000 53.467  ? 142 ALA HHH CA  1 
ATOM   2599  C C   . ALA B 2 142 ? 45.768  65.359  78.355  1.000 47.231  ? 142 ALA HHH C   1 
ATOM   2600  O O   . ALA B 2 142 ? 45.316  64.291  77.975  1.000 49.928  ? 142 ALA HHH O   1 
ATOM   2601  C CB  . ALA B 2 142 ? 47.603  65.293  80.035  1.000 54.840  ? 142 ALA HHH CB  1 
ATOM   2602  N N   . ALA B 2 143 ? 45.965  66.406  77.566  1.000 42.714  ? 143 ALA HHH N   1 
ATOM   2603  C CA  . ALA B 2 143 ? 45.734  66.394  76.113  1.000 38.587  ? 143 ALA HHH CA  1 
ATOM   2604  C C   . ALA B 2 143 ? 47.045  66.727  75.405  1.000 39.352  ? 143 ALA HHH C   1 
ATOM   2605  O O   . ALA B 2 143 ? 47.838  67.568  75.919  1.000 39.250  ? 143 ALA HHH O   1 
ATOM   2606  C CB  . ALA B 2 143 ? 44.652  67.363  75.745  1.000 38.440  ? 143 ALA HHH CB  1 
ATOM   2607  N N   . LEU B 2 144 ? 47.240  66.064  74.270  1.000 39.617  ? 144 LEU HHH N   1 
ATOM   2608  C CA  . LEU B 2 144 ? 48.381  66.242  73.349  1.000 37.499  ? 144 LEU HHH CA  1 
ATOM   2609  C C   . LEU B 2 144 ? 47.864  65.996  71.933  1.000 36.925  ? 144 LEU HHH C   1 
ATOM   2610  O O   . LEU B 2 144 ? 46.710  65.531  71.801  1.000 35.827  ? 144 LEU HHH O   1 
ATOM   2611  C CB  . LEU B 2 144 ? 49.477  65.257  73.748  1.000 35.300  ? 144 LEU HHH CB  1 
ATOM   2612  C CG  . LEU B 2 144 ? 49.105  63.781  73.634  1.000 35.771  ? 144 LEU HHH CG  1 
ATOM   2613  C CD1 . LEU B 2 144 ? 49.782  63.152  72.429  1.000 37.436  ? 144 LEU HHH CD1 1 
ATOM   2614  C CD2 . LEU B 2 144 ? 49.487  63.008  74.892  1.000 36.722  ? 144 LEU HHH CD2 1 
ATOM   2615  N N   . GLY B 2 145 ? 48.659  66.310  70.915  1.000 37.066  ? 145 GLY HHH N   1 
ATOM   2616  C CA  . GLY B 2 145 ? 48.182  66.184  69.533  1.000 37.725  ? 145 GLY HHH CA  1 
ATOM   2617  C C   . GLY B 2 145 ? 49.245  66.509  68.515  1.000 37.542  ? 145 GLY HHH C   1 
ATOM   2618  O O   . GLY B 2 145 ? 50.386  66.731  68.899  1.000 38.880  ? 145 GLY HHH O   1 
ATOM   2619  N N   . CYS B 2 146 ? 48.828  66.537  67.256  1.000 40.492  ? 146 CYS HHH N   1 
ATOM   2620  C CA  . CYS B 2 146 ? 49.612  66.953  66.078  1.000 41.118  ? 146 CYS HHH CA  1 
ATOM   2621  C C   . CYS B 2 146 ? 48.869  68.050  65.348  1.000 35.070  ? 146 CYS HHH C   1 
ATOM   2622  O O   . CYS B 2 146 ? 47.654  68.015  65.328  1.000 33.086  ? 146 CYS HHH O   1 
ATOM   2623  C CB  . CYS B 2 146 ? 49.814  65.802  65.112  1.000 48.415  ? 146 CYS HHH CB  1 
ATOM   2624  S SG  . CYS B 2 146 ? 51.053  64.679  65.779  1.000 60.478  ? 146 CYS HHH SG  1 
ATOM   2625  N N   . LEU B 2 147 ? 49.623  68.967  64.771  1.000 32.197  ? 147 LEU HHH N   1 
ATOM   2626  C CA  . LEU B 2 147 ? 49.124  69.976  63.830  1.000 32.519  ? 147 LEU HHH CA  1 
ATOM   2627  C C   . LEU B 2 147 ? 49.603  69.545  62.451  1.000 30.662  ? 147 LEU HHH C   1 
ATOM   2628  O O   . LEU B 2 147 ? 50.807  69.457  62.261  1.000 31.423  ? 147 LEU HHH O   1 
ATOM   2629  C CB  . LEU B 2 147 ? 49.692  71.329  64.255  1.000 35.126  ? 147 LEU HHH CB  1 
ATOM   2630  C CG  . LEU B 2 147 ? 49.225  72.533  63.444  1.000 36.281  ? 147 LEU HHH CG  1 
ATOM   2631  C CD1 . LEU B 2 147 ? 47.705  72.696  63.523  1.000 37.978  ? 147 LEU HHH CD1 1 
ATOM   2632  C CD2 . LEU B 2 147 ? 49.930  73.784  63.950  1.000 34.477  ? 147 LEU HHH CD2 1 
ATOM   2633  N N   . VAL B 2 148 ? 48.679  69.182  61.575  1.000 30.501  ? 148 VAL HHH N   1 
ATOM   2634  C CA  . VAL B 2 148 ? 48.980  68.807  60.170  1.000 31.924  ? 148 VAL HHH CA  1 
ATOM   2635  C C   . VAL B 2 148 ? 48.669  70.040  59.338  1.000 33.296  ? 148 VAL HHH C   1 
ATOM   2636  O O   . VAL B 2 148 ? 47.478  70.299  59.080  1.000 35.108  ? 148 VAL HHH O   1 
ATOM   2637  C CB  . VAL B 2 148 ? 48.169  67.573  59.745  1.000 32.379  ? 148 VAL HHH CB  1 
ATOM   2638  C CG1 . VAL B 2 148 ? 48.552  67.084  58.366  1.000 32.026  ? 148 VAL HHH CG1 1 
ATOM   2639  C CG2 . VAL B 2 148 ? 48.318  66.444  60.758  1.000 33.503  ? 148 VAL HHH CG2 1 
ATOM   2640  N N   . LYS B 2 149 ? 49.708  70.799  58.990  1.000 36.987  ? 149 LYS HHH N   1 
ATOM   2641  C CA  . LYS B 2 149 ? 49.585  72.194  58.479  1.000 40.225  ? 149 LYS HHH CA  1 
ATOM   2642  C C   . LYS B 2 149 ? 50.091  72.292  57.036  1.000 34.629  ? 149 LYS HHH C   1 
ATOM   2643  O O   . LYS B 2 149 ? 51.112  71.684  56.716  1.000 35.494  ? 149 LYS HHH O   1 
ATOM   2644  C CB  . LYS B 2 149 ? 50.337  73.156  59.407  1.000 44.446  ? 149 LYS HHH CB  1 
ATOM   2645  C CG  . LYS B 2 149 ? 49.901  74.612  59.312  1.000 48.041  ? 149 LYS HHH CG  1 
ATOM   2646  C CD  . LYS B 2 149 ? 50.746  75.559  60.140  1.000 53.623  ? 149 LYS HHH CD  1 
ATOM   2647  C CE  . LYS B 2 149 ? 50.837  76.949  59.542  1.000 59.804  ? 149 LYS HHH CE  1 
ATOM   2648  N NZ  . LYS B 2 149 ? 49.486  77.515  59.314  1.000 64.366  ? 149 LYS HHH NZ  1 
ATOM   2649  N N   . ASP B 2 150 ? 49.377  73.041  56.208  1.000 33.211  ? 150 ASP HHH N   1 
ATOM   2650  C CA  . ASP B 2 150 ? 49.862  73.539  54.895  1.000 37.573  ? 150 ASP HHH CA  1 
ATOM   2651  C C   . ASP B 2 150 ? 50.028  72.359  53.930  1.000 35.500  ? 150 ASP HHH C   1 
ATOM   2652  O O   . ASP B 2 150 ? 51.170  72.055  53.571  1.000 39.818  ? 150 ASP HHH O   1 
ATOM   2653  C CB  . ASP B 2 150 ? 51.171  74.322  55.050  1.000 39.776  ? 150 ASP HHH CB  1 
ATOM   2654  C CG  . ASP B 2 150 ? 51.094  75.551  55.945  1.000 42.859  ? 150 ASP HHH CG  1 
ATOM   2655  O OD1 . ASP B 2 150 ? 50.011  76.140  56.023  1.000 48.726  ? 150 ASP HHH OD1 1 
ATOM   2656  O OD2 . ASP B 2 150 ? 52.131  75.917  56.552  1.000 45.486  ? 150 ASP HHH OD2 1 
ATOM   2657  N N   . TYR B 2 151 ? 48.927  71.729  53.521  1.000 30.909  ? 151 TYR HHH N   1 
ATOM   2658  C CA  . TYR B 2 151 ? 48.921  70.624  52.532  1.000 30.894  ? 151 TYR HHH CA  1 
ATOM   2659  C C   . TYR B 2 151 ? 47.833  70.861  51.484  1.000 30.583  ? 151 TYR HHH C   1 
ATOM   2660  O O   . TYR B 2 151 ? 46.894  71.630  51.751  1.000 32.916  ? 151 TYR HHH O   1 
ATOM   2661  C CB  . TYR B 2 151 ? 48.749  69.259  53.214  1.000 30.757  ? 151 TYR HHH CB  1 
ATOM   2662  C CG  . TYR B 2 151 ? 47.416  68.998  53.870  1.000 28.902  ? 151 TYR HHH CG  1 
ATOM   2663  C CD1 . TYR B 2 151 ? 47.197  69.336  55.193  1.000 28.221  ? 151 TYR HHH CD1 1 
ATOM   2664  C CD2 . TYR B 2 151 ? 46.384  68.387  53.178  1.000 29.027  ? 151 TYR HHH CD2 1 
ATOM   2665  C CE1 . TYR B 2 151 ? 45.984  69.089  55.814  1.000 29.047  ? 151 TYR HHH CE1 1 
ATOM   2666  C CE2 . TYR B 2 151 ? 45.158  68.147  53.777  1.000 30.229  ? 151 TYR HHH CE2 1 
ATOM   2667  C CZ  . TYR B 2 151 ? 44.960  68.483  55.109  1.000 29.977  ? 151 TYR HHH CZ  1 
ATOM   2668  O OH  . TYR B 2 151 ? 43.768  68.228  55.730  1.000 27.369  ? 151 TYR HHH OH  1 
ATOM   2669  N N   . PHE B 2 152 ? 47.968  70.178  50.345  1.000 28.890  ? 152 PHE HHH N   1 
ATOM   2670  C CA  . PHE B 2 152 ? 47.020  70.212  49.212  1.000 28.392  ? 152 PHE HHH CA  1 
ATOM   2671  C C   . PHE B 2 152 ? 47.295  69.011  48.317  1.000 31.532  ? 152 PHE HHH C   1 
ATOM   2672  O O   . PHE B 2 152 ? 48.449  68.662  48.087  1.000 36.666  ? 152 PHE HHH O   1 
ATOM   2673  C CB  . PHE B 2 152 ? 47.184  71.496  48.395  1.000 27.115  ? 152 PHE HHH CB  1 
ATOM   2674  C CG  . PHE B 2 152 ? 46.145  71.646  47.314  1.000 27.103  ? 152 PHE HHH CG  1 
ATOM   2675  C CD1 . PHE B 2 152 ? 44.938  72.266  47.580  1.000 27.471  ? 152 PHE HHH CD1 1 
ATOM   2676  C CD2 . PHE B 2 152 ? 46.355  71.137  46.043  1.000 27.476  ? 152 PHE HHH CD2 1 
ATOM   2677  C CE1 . PHE B 2 152 ? 43.964  72.372  46.599  1.000 27.244  ? 152 PHE HHH CE1 1 
ATOM   2678  C CE2 . PHE B 2 152 ? 45.386  71.250  45.061  1.000 26.884  ? 152 PHE HHH CE2 1 
ATOM   2679  C CZ  . PHE B 2 152 ? 44.190  71.855  45.346  1.000 26.692  ? 152 PHE HHH CZ  1 
ATOM   2680  N N   . PRO B 2 153 ? 46.265  68.348  47.757  1.000 32.092  ? 153 PRO HHH N   1 
ATOM   2681  C CA  . PRO B 2 153 ? 44.879  68.623  48.112  1.000 32.819  ? 153 PRO HHH CA  1 
ATOM   2682  C C   . PRO B 2 153 ? 44.477  67.884  49.396  1.000 33.850  ? 153 PRO HHH C   1 
ATOM   2683  O O   . PRO B 2 153 ? 45.333  67.357  50.075  1.000 34.259  ? 153 PRO HHH O   1 
ATOM   2684  C CB  . PRO B 2 153 ? 44.143  68.097  46.871  1.000 33.016  ? 153 PRO HHH CB  1 
ATOM   2685  C CG  . PRO B 2 153 ? 44.958  66.899  46.443  1.000 32.772  ? 153 PRO HHH CG  1 
ATOM   2686  C CD  . PRO B 2 153 ? 46.386  67.345  46.686  1.000 32.669  ? 153 PRO HHH CD  1 
ATOM   2687  N N   . GLU B 2 154 ? 43.181  67.899  49.712  1.000 34.921  ? 154 GLU HHH N   1 
ATOM   2688  C CA  . GLU B 2 154 ? 42.559  66.936  50.647  1.000 33.436  ? 154 GLU HHH CA  1 
ATOM   2689  C C   . GLU B 2 154 ? 42.577  65.565  49.975  1.000 33.732  ? 154 GLU HHH C   1 
ATOM   2690  O O   . GLU B 2 154 ? 42.593  65.481  48.742  1.000 34.772  ? 154 GLU HHH O   1 
ATOM   2691  C CB  . GLU B 2 154 ? 41.132  67.382  50.937  1.000 37.475  ? 154 GLU HHH CB  1 
ATOM   2692  C CG  . GLU B 2 154 ? 41.026  68.456  51.993  1.000 39.517  ? 154 GLU HHH CG  1 
ATOM   2693  C CD  . GLU B 2 154 ? 40.647  67.860  53.344  1.000 44.222  ? 154 GLU HHH CD  1 
ATOM   2694  O OE1 . GLU B 2 154 ? 41.419  67.006  53.899  1.000 42.651  ? 154 GLU HHH OE1 1 
ATOM   2695  O OE2 . GLU B 2 154 ? 39.562  68.228  53.848  1.000 47.916  ? 154 GLU HHH OE2 1 
ATOM   2696  N N   . PRO B 2 155 ? 42.568  64.434  50.727  1.000 32.532  ? 155 PRO HHH N   1 
ATOM   2697  C CA  . PRO B 2 155 ? 42.666  64.411  52.193  1.000 31.067  ? 155 PRO HHH CA  1 
ATOM   2698  C C   . PRO B 2 155 ? 43.983  63.918  52.815  1.000 29.017  ? 155 PRO HHH C   1 
ATOM   2699  O O   . PRO B 2 155 ? 44.864  63.520  52.090  1.000 30.385  ? 155 PRO HHH O   1 
ATOM   2700  C CB  . PRO B 2 155 ? 41.610  63.346  52.482  1.000 31.110  ? 155 PRO HHH CB  1 
ATOM   2701  C CG  . PRO B 2 155 ? 41.796  62.331  51.362  1.000 30.449  ? 155 PRO HHH CG  1 
ATOM   2702  C CD  . PRO B 2 155 ? 42.370  63.086  50.179  1.000 29.914  ? 155 PRO HHH CD  1 
ATOM   2703  N N   . VAL B 2 156 ? 44.094  63.955  54.142  1.000 27.298  ? 156 VAL HHH N   1 
ATOM   2704  C CA  . VAL B 2 156 ? 45.190  63.273  54.898  1.000 27.919  ? 156 VAL HHH CA  1 
ATOM   2705  C C   . VAL B 2 156 ? 44.541  62.266  55.820  1.000 30.001  ? 156 VAL HHH C   1 
ATOM   2706  O O   . VAL B 2 156 ? 43.383  62.496  56.149  1.000 40.045  ? 156 VAL HHH O   1 
ATOM   2707  C CB  . VAL B 2 156 ? 46.072  64.224  55.720  1.000 25.440  ? 156 VAL HHH CB  1 
ATOM   2708  C CG1 . VAL B 2 156 ? 46.923  65.060  54.791  1.000 26.799  ? 156 VAL HHH CG1 1 
ATOM   2709  C CG2 . VAL B 2 156 ? 45.282  65.086  56.685  1.000 24.212  ? 156 VAL HHH CG2 1 
ATOM   2710  N N   . THR B 2 157 ? 45.243  61.197  56.177  1.000 30.543  ? 157 THR HHH N   1 
ATOM   2711  C CA  . THR B 2 157 ? 44.831  60.273  57.257  1.000 33.490  ? 157 THR HHH CA  1 
ATOM   2712  C C   . THR B 2 157 ? 45.760  60.532  58.437  1.000 30.698  ? 157 THR HHH C   1 
ATOM   2713  O O   . THR B 2 157 ? 46.967  60.656  58.224  1.000 29.492  ? 157 THR HHH O   1 
ATOM   2714  C CB  . THR B 2 157 ? 44.832  58.795  56.829  1.000 38.551  ? 157 THR HHH CB  1 
ATOM   2715  O OG1 . THR B 2 157 ? 46.201  58.400  56.840  1.000 49.762  ? 157 THR HHH OG1 1 
ATOM   2716  C CG2 . THR B 2 157 ? 44.211  58.517  55.473  1.000 38.630  ? 157 THR HHH CG2 1 
ATOM   2717  N N   . VAL B 2 158 ? 45.185  60.640  59.625  1.000 31.328  ? 158 VAL HHH N   1 
ATOM   2718  C CA  . VAL B 2 158 ? 45.927  60.769  60.905  1.000 33.683  ? 158 VAL HHH CA  1 
ATOM   2719  C C   . VAL B 2 158 ? 45.487  59.628  61.822  1.000 35.604  ? 158 VAL HHH C   1 
ATOM   2720  O O   . VAL B 2 158 ? 44.297  59.578  62.184  1.000 40.920  ? 158 VAL HHH O   1 
ATOM   2721  C CB  . VAL B 2 158 ? 45.662  62.126  61.570  1.000 33.666  ? 158 VAL HHH CB  1 
ATOM   2722  C CG1 . VAL B 2 158 ? 46.485  62.260  62.839  1.000 36.890  ? 158 VAL HHH CG1 1 
ATOM   2723  C CG2 . VAL B 2 158 ? 45.928  63.270  60.618  1.000 33.546  ? 158 VAL HHH CG2 1 
ATOM   2724  N N   . SER B 2 159 ? 46.418  58.741  62.148  1.000 34.911  ? 159 SER HHH N   1 
ATOM   2725  C CA  . SER B 2 159 ? 46.266  57.673  63.159  1.000 36.464  ? 159 SER HHH CA  1 
ATOM   2726  C C   . SER B 2 159 ? 47.276  57.947  64.273  1.000 33.350  ? 159 SER HHH C   1 
ATOM   2727  O O   . SER B 2 159 ? 48.062  58.875  64.096  1.000 26.324  ? 159 SER HHH O   1 
ATOM   2728  C CB  . SER B 2 159 ? 46.444  56.308  62.529  1.000 38.715  ? 159 SER HHH CB  1 
ATOM   2729  O OG  . SER B 2 159 ? 47.642  56.254  61.768  1.000 39.891  ? 159 SER HHH OG  1 
ATOM   2730  N N   . TRP B 2 160 ? 47.219  57.163  65.357  1.000 35.077  ? 160 TRP HHH N   1 
ATOM   2731  C CA  . TRP B 2 160 ? 48.046  57.318  66.587  1.000 36.313  ? 160 TRP HHH CA  1 
ATOM   2732  C C   . TRP B 2 160 ? 48.652  55.971  67.011  1.000 39.794  ? 160 TRP HHH C   1 
ATOM   2733  O O   . TRP B 2 160 ? 47.901  54.995  67.132  1.000 41.673  ? 160 TRP HHH O   1 
ATOM   2734  C CB  . TRP B 2 160 ? 47.208  57.900  67.734  1.000 33.906  ? 160 TRP HHH CB  1 
ATOM   2735  C CG  . TRP B 2 160 ? 46.984  59.372  67.631  1.000 30.322  ? 160 TRP HHH CG  1 
ATOM   2736  C CD1 . TRP B 2 160 ? 45.923  60.013  67.066  1.000 29.657  ? 160 TRP HHH CD1 1 
ATOM   2737  C CD2 . TRP B 2 160 ? 47.870  60.395  68.089  1.000 29.287  ? 160 TRP HHH CD2 1 
ATOM   2738  N NE1 . TRP B 2 160 ? 46.085  61.362  67.144  1.000 29.450  ? 160 TRP HHH NE1 1 
ATOM   2739  C CE2 . TRP B 2 160 ? 47.270  61.627  67.772  1.000 30.964  ? 160 TRP HHH CE2 1 
ATOM   2740  C CE3 . TRP B 2 160 ? 49.106  60.393  68.734  1.000 30.284  ? 160 TRP HHH CE3 1 
ATOM   2741  C CZ2 . TRP B 2 160 ? 47.877  62.846  68.077  1.000 33.193  ? 160 TRP HHH CZ2 1 
ATOM   2742  C CZ3 . TRP B 2 160 ? 49.701  61.593  69.042  1.000 30.735  ? 160 TRP HHH CZ3 1 
ATOM   2743  C CH2 . TRP B 2 160 ? 49.097  62.805  68.716  1.000 32.051  ? 160 TRP HHH CH2 1 
ATOM   2744  N N   . ASN B 2 161 ? 49.958  55.933  67.277  1.000 42.053  ? 161 ASN HHH N   1 
ATOM   2745  C CA  . ASN B 2 161 ? 50.678  54.728  67.772  1.000 43.095  ? 161 ASN HHH CA  1 
ATOM   2746  C C   . ASN B 2 161 ? 50.469  53.595  66.753  1.000 44.342  ? 161 ASN HHH C   1 
ATOM   2747  O O   . ASN B 2 161 ? 50.200  52.436  67.146  1.000 44.376  ? 161 ASN HHH O   1 
ATOM   2748  C CB  . ASN B 2 161 ? 50.252  54.401  69.208  1.000 43.364  ? 161 ASN HHH CB  1 
ATOM   2749  C CG  . ASN B 2 161 ? 50.734  55.432  70.211  1.000 43.058  ? 161 ASN HHH CG  1 
ATOM   2750  O OD1 . ASN B 2 161 ? 51.652  56.190  69.931  1.000 43.062  ? 161 ASN HHH OD1 1 
ATOM   2751  N ND2 . ASN B 2 161 ? 50.155  55.451  71.398  1.000 46.504  ? 161 ASN HHH ND2 1 
ATOM   2752  N N   . SER B 2 162 ? 50.626  53.931  65.472  1.000 43.183  ? 162 SER HHH N   1 
ATOM   2753  C CA  . SER B 2 162 ? 50.446  53.023  64.311  1.000 39.423  ? 162 SER HHH CA  1 
ATOM   2754  C C   . SER B 2 162 ? 49.052  52.411  64.305  1.000 36.349  ? 162 SER HHH C   1 
ATOM   2755  O O   . SER B 2 162 ? 48.946  51.308  63.820  1.000 39.980  ? 162 SER HHH O   1 
ATOM   2756  C CB  . SER B 2 162 ? 51.499  51.949  64.297  1.000 39.243  ? 162 SER HHH CB  1 
ATOM   2757  O OG  . SER B 2 162 ? 52.796  52.517  64.381  1.000 39.200  ? 162 SER HHH OG  1 
ATOM   2758  N N   . GLY B 2 163 ? 48.027  53.107  64.792  1.000 36.576  ? 163 GLY HHH N   1 
ATOM   2759  C CA  . GLY B 2 163 ? 46.620  52.640  64.736  1.000 39.146  ? 163 GLY HHH CA  1 
ATOM   2760  C C   . GLY B 2 163 ? 46.154  51.964  66.020  1.000 38.291  ? 163 GLY HHH C   1 
ATOM   2761  O O   . GLY B 2 163 ? 44.942  51.724  66.144  1.000 36.078  ? 163 GLY HHH O   1 
ATOM   2762  N N   . ALA B 2 164 ? 47.080  51.688  66.945  1.000 42.286  ? 164 ALA HHH N   1 
ATOM   2763  C CA  . ALA B 2 164 ? 46.833  51.029  68.252  1.000 44.793  ? 164 ALA HHH CA  1 
ATOM   2764  C C   . ALA B 2 164 ? 45.855  51.870  69.077  1.000 46.692  ? 164 ALA HHH C   1 
ATOM   2765  O O   . ALA B 2 164 ? 44.900  51.285  69.619  1.000 51.534  ? 164 ALA HHH O   1 
ATOM   2766  C CB  . ALA B 2 164 ? 48.134  50.836  69.003  1.000 44.774  ? 164 ALA HHH CB  1 
ATOM   2767  N N   . LEU B 2 165 ? 46.099  53.186  69.142  1.000 44.355  ? 165 LEU HHH N   1 
ATOM   2768  C CA  . LEU B 2 165 ? 45.348  54.169  69.961  1.000 44.247  ? 165 LEU HHH CA  1 
ATOM   2769  C C   . LEU B 2 165 ? 44.283  54.879  69.114  1.000 41.806  ? 165 LEU HHH C   1 
ATOM   2770  O O   . LEU B 2 165 ? 44.645  55.597  68.157  1.000 38.013  ? 165 LEU HHH O   1 
ATOM   2771  C CB  . LEU B 2 165 ? 46.353  55.172  70.542  1.000 44.897  ? 165 LEU HHH CB  1 
ATOM   2772  C CG  . LEU B 2 165 ? 45.772  56.298  71.398  1.000 43.514  ? 165 LEU HHH CG  1 
ATOM   2773  C CD1 . LEU B 2 165 ? 44.935  55.758  72.553  1.000 46.554  ? 165 LEU HHH CD1 1 
ATOM   2774  C CD2 . LEU B 2 165 ? 46.882  57.177  71.944  1.000 41.593  ? 165 LEU HHH CD2 1 
ATOM   2775  N N   . THR B 2 166 ? 43.014  54.671  69.461  1.000 43.837  ? 166 THR HHH N   1 
ATOM   2776  C CA  . THR B 2 166 ? 41.832  55.300  68.808  1.000 49.541  ? 166 THR HHH CA  1 
ATOM   2777  C C   . THR B 2 166 ? 40.912  55.922  69.867  1.000 47.072  ? 166 THR HHH C   1 
ATOM   2778  O O   . THR B 2 166 ? 40.153  56.850  69.525  1.000 42.169  ? 166 THR HHH O   1 
ATOM   2779  C CB  . THR B 2 166 ? 41.047  54.281  67.971  1.000 51.888  ? 166 THR HHH CB  1 
ATOM   2780  O OG1 . THR B 2 166 ? 40.518  53.338  68.903  1.000 58.812  ? 166 THR HHH OG1 1 
ATOM   2781  C CG2 . THR B 2 166 ? 41.882  53.579  66.920  1.000 52.050  ? 166 THR HHH CG2 1 
ATOM   2782  N N   . SER B 2 167 ? 40.969  55.409  71.097  1.000 47.553  ? 167 SER HHH N   1 
ATOM   2783  C CA  . SER B 2 167 ? 40.169  55.889  72.247  1.000 45.164  ? 167 SER HHH CA  1 
ATOM   2784  C C   . SER B 2 167 ? 40.602  57.313  72.622  1.000 40.989  ? 167 SER HHH C   1 
ATOM   2785  O O   . SER B 2 167 ? 41.804  57.579  72.821  1.000 36.158  ? 167 SER HHH O   1 
ATOM   2786  C CB  . SER B 2 167 ? 40.286  54.941  73.401  1.000 47.327  ? 167 SER HHH CB  1 
ATOM   2787  O OG  . SER B 2 167 ? 39.511  55.392  74.494  1.000 50.260  ? 167 SER HHH OG  1 
ATOM   2788  N N   . GLY B 2 168 ? 39.630  58.210  72.697  1.000 40.314  ? 168 GLY HHH N   1 
ATOM   2789  C CA  . GLY B 2 168 ? 39.846  59.601  73.126  1.000 38.765  ? 168 GLY HHH CA  1 
ATOM   2790  C C   . GLY B 2 168 ? 40.507  60.451  72.060  1.000 34.244  ? 168 GLY HHH C   1 
ATOM   2791  O O   . GLY B 2 168 ? 40.934  61.556  72.413  1.000 34.017  ? 168 GLY HHH O   1 
ATOM   2792  N N   . VAL B 2 169 ? 40.568  59.980  70.812  1.000 30.855  ? 169 VAL HHH N   1 
ATOM   2793  C CA  . VAL B 2 169 ? 41.125  60.763  69.667  1.000 29.675  ? 169 VAL HHH CA  1 
ATOM   2794  C C   . VAL B 2 169 ? 40.030  61.631  69.060  1.000 27.559  ? 169 VAL HHH C   1 
ATOM   2795  O O   . VAL B 2 169 ? 38.940  61.134  68.877  1.000 26.835  ? 169 VAL HHH O   1 
ATOM   2796  C CB  . VAL B 2 169 ? 41.755  59.864  68.587  1.000 29.566  ? 169 VAL HHH CB  1 
ATOM   2797  C CG1 . VAL B 2 169 ? 42.270  60.677  67.404  1.000 27.959  ? 169 VAL HHH CG1 1 
ATOM   2798  C CG2 . VAL B 2 169 ? 42.865  58.997  69.176  1.000 30.273  ? 169 VAL HHH CG2 1 
ATOM   2799  N N   . HIS B 2 170 ? 40.366  62.872  68.734  1.000 29.930  ? 170 HIS HHH N   1 
ATOM   2800  C CA  . HIS B 2 170 ? 39.584  63.772  67.854  1.000 32.646  ? 170 HIS HHH CA  1 
ATOM   2801  C C   . HIS B 2 170 ? 40.490  64.287  66.728  1.000 32.665  ? 170 HIS HHH C   1 
ATOM   2802  O O   . HIS B 2 170 ? 41.417  65.082  67.023  1.000 32.179  ? 170 HIS HHH O   1 
ATOM   2803  C CB  . HIS B 2 170 ? 38.997  64.920  68.687  1.000 33.996  ? 170 HIS HHH CB  1 
ATOM   2804  C CG  . HIS B 2 170 ? 37.927  64.489  69.623  1.000 35.543  ? 170 HIS HHH CG  1 
ATOM   2805  N ND1 . HIS B 2 170 ? 36.738  63.933  69.178  1.000 39.746  ? 170 HIS HHH ND1 1 
ATOM   2806  C CD2 . HIS B 2 170 ? 37.850  64.544  70.966  1.000 37.727  ? 170 HIS HHH CD2 1 
ATOM   2807  C CE1 . HIS B 2 170 ? 35.973  63.657  70.212  1.000 43.178  ? 170 HIS HHH CE1 1 
ATOM   2808  N NE2 . HIS B 2 170 ? 36.641  64.013  71.322  1.000 42.715  ? 170 HIS HHH NE2 1 
ATOM   2809  N N   . THR B 2 171 ? 40.255  63.856  65.492  1.000 32.027  ? 171 THR HHH N   1 
ATOM   2810  C CA  . THR B 2 171 ? 40.841  64.498  64.288  1.000 33.572  ? 171 THR HHH CA  1 
ATOM   2811  C C   . THR B 2 171 ? 39.807  65.487  63.742  1.000 32.281  ? 171 THR HHH C   1 
ATOM   2812  O O   . THR B 2 171 ? 38.779  65.042  63.215  1.000 35.193  ? 171 THR HHH O   1 
ATOM   2813  C CB  . THR B 2 171 ? 41.268  63.476  63.228  1.000 37.270  ? 171 THR HHH CB  1 
ATOM   2814  O OG1 . THR B 2 171 ? 42.218  62.564  63.784  1.000 39.735  ? 171 THR HHH OG1 1 
ATOM   2815  C CG2 . THR B 2 171 ? 41.876  64.128  62.006  1.000 38.140  ? 171 THR HHH CG2 1 
ATOM   2816  N N   . PHE B 2 172 ? 40.084  66.778  63.853  1.000 28.950  ? 172 PHE HHH N   1 
ATOM   2817  C CA  . PHE B 2 172 ? 39.209  67.875  63.378  1.000 26.763  ? 172 PHE HHH CA  1 
ATOM   2818  C C   . PHE B 2 172 ? 39.180  67.895  61.853  1.000 26.176  ? 172 PHE HHH C   1 
ATOM   2819  O O   . PHE B 2 172 ? 40.088  67.418  61.172  1.000 24.281  ? 172 PHE HHH O   1 
ATOM   2820  C CB  . PHE B 2 172 ? 39.681  69.219  63.946  1.000 27.232  ? 172 PHE HHH CB  1 
ATOM   2821  C CG  . PHE B 2 172 ? 39.488  69.324  65.434  1.000 26.278  ? 172 PHE HHH CG  1 
ATOM   2822  C CD1 . PHE B 2 172 ? 40.485  68.961  66.329  1.000 25.515  ? 172 PHE HHH CD1 1 
ATOM   2823  C CD2 . PHE B 2 172 ? 38.259  69.706  65.933  1.000 26.093  ? 172 PHE HHH CD2 1 
ATOM   2824  C CE1 . PHE B 2 172 ? 40.250  68.981  67.693  1.000 25.018  ? 172 PHE HHH CE1 1 
ATOM   2825  C CE2 . PHE B 2 172 ? 38.038  69.762  67.299  1.000 25.756  ? 172 PHE HHH CE2 1 
ATOM   2826  C CZ  . PHE B 2 172 ? 39.036  69.407  68.175  1.000 25.033  ? 172 PHE HHH CZ  1 
ATOM   2827  N N   . PRO B 2 173 ? 38.094  68.440  61.280  1.000 26.567  ? 173 PRO HHH N   1 
ATOM   2828  C CA  . PRO B 2 173 ? 38.026  68.763  59.862  1.000 28.798  ? 173 PRO HHH CA  1 
ATOM   2829  C C   . PRO B 2 173 ? 39.115  69.744  59.442  1.000 30.032  ? 173 PRO HHH C   1 
ATOM   2830  O O   . PRO B 2 173 ? 39.396  70.654  60.160  1.000 29.604  ? 173 PRO HHH O   1 
ATOM   2831  C CB  . PRO B 2 173 ? 36.685  69.472  59.686  1.000 27.681  ? 173 PRO HHH CB  1 
ATOM   2832  C CG  . PRO B 2 173 ? 35.864  68.968  60.837  1.000 28.387  ? 173 PRO HHH CG  1 
ATOM   2833  C CD  . PRO B 2 173 ? 36.844  68.742  61.968  1.000 27.335  ? 173 PRO HHH CD  1 
ATOM   2834  N N   . ALA B 2 174 ? 39.689  69.519  58.273  1.000 33.166  ? 174 ALA HHH N   1 
ATOM   2835  C CA  . ALA B 2 174 ? 40.602  70.489  57.650  1.000 35.866  ? 174 ALA HHH CA  1 
ATOM   2836  C C   . ALA B 2 174 ? 39.861  71.804  57.476  1.000 34.888  ? 174 ALA HHH C   1 
ATOM   2837  O O   . ALA B 2 174 ? 38.657  71.747  57.238  1.000 33.942  ? 174 ALA HHH O   1 
ATOM   2838  C CB  . ALA B 2 174 ? 41.076  69.972  56.329  1.000 39.402  ? 174 ALA HHH CB  1 
ATOM   2839  N N   . VAL B 2 175 ? 40.570  72.923  57.616  1.000 37.204  ? 175 VAL HHH N   1 
ATOM   2840  C CA  . VAL B 2 175 ? 40.110  74.270  57.172  1.000 38.560  ? 175 VAL HHH CA  1 
ATOM   2841  C C   . VAL B 2 175 ? 40.981  74.651  55.983  1.000 38.099  ? 175 VAL HHH C   1 
ATOM   2842  O O   . VAL B 2 175 ? 42.165  74.293  55.973  1.000 37.931  ? 175 VAL HHH O   1 
ATOM   2843  C CB  . VAL B 2 175 ? 40.188  75.317  58.297  1.000 40.521  ? 175 VAL HHH CB  1 
ATOM   2844  C CG1 . VAL B 2 175 ? 39.592  74.777  59.584  1.000 41.248  ? 175 VAL HHH CG1 1 
ATOM   2845  C CG2 . VAL B 2 175 ? 41.617  75.787  58.556  1.000 45.647  ? 175 VAL HHH CG2 1 
ATOM   2846  N N   . LEU B 2 176 ? 40.388  75.325  55.011  1.000 38.830  ? 176 LEU HHH N   1 
ATOM   2847  C CA  . LEU B 2 176 ? 41.109  75.946  53.884  1.000 37.510  ? 176 LEU HHH CA  1 
ATOM   2848  C C   . LEU B 2 176 ? 41.631  77.292  54.384  1.000 40.533  ? 176 LEU HHH C   1 
ATOM   2849  O O   . LEU B 2 176 ? 40.808  78.146  54.722  1.000 41.322  ? 176 LEU HHH O   1 
ATOM   2850  C CB  . LEU B 2 176 ? 40.109  76.074  52.743  1.000 37.735  ? 176 LEU HHH CB  1 
ATOM   2851  C CG  . LEU B 2 176 ? 40.663  76.523  51.402  1.000 42.289  ? 176 LEU HHH CG  1 
ATOM   2852  C CD1 . LEU B 2 176 ? 41.914  75.726  51.038  1.000 43.354  ? 176 LEU HHH CD1 1 
ATOM   2853  C CD2 . LEU B 2 176 ? 39.567  76.456  50.343  1.000 45.079  ? 176 LEU HHH CD2 1 
ATOM   2854  N N   . GLN B 2 177 ? 42.948  77.437  54.541  1.000 46.916  ? 177 GLN HHH N   1 
ATOM   2855  C CA  . GLN B 2 177 ? 43.589  78.717  54.959  1.000 49.672  ? 177 GLN HHH CA  1 
ATOM   2856  C C   . GLN B 2 177 ? 43.572  79.671  53.759  1.000 52.938  ? 177 GLN HHH C   1 
ATOM   2857  O O   . GLN B 2 177 ? 43.351  79.183  52.635  1.000 54.757  ? 177 GLN HHH O   1 
ATOM   2858  C CB  . GLN B 2 177 ? 45.017  78.487  55.448  1.000 48.337  ? 177 GLN HHH CB  1 
ATOM   2859  C CG  . GLN B 2 177 ? 45.116  77.557  56.646  1.000 49.283  ? 177 GLN HHH CG  1 
ATOM   2860  C CD  . GLN B 2 177 ? 46.532  77.085  56.866  1.000 51.610  ? 177 GLN HHH CD  1 
ATOM   2861  O OE1 . GLN B 2 177 ? 47.058  77.151  57.970  1.000 59.061  ? 177 GLN HHH OE1 1 
ATOM   2862  N NE2 . GLN B 2 177 ? 47.164  76.595  55.814  1.000 53.008  ? 177 GLN HHH NE2 1 
ATOM   2863  N N   . SER B 2 178 ? 43.793  80.973  53.968  1.000 56.890  ? 178 SER HHH N   1 
ATOM   2864  C CA  . SER B 2 178 ? 43.748  81.993  52.878  1.000 56.806  ? 178 SER HHH CA  1 
ATOM   2865  C C   . SER B 2 178 ? 44.928  81.784  51.910  1.000 52.821  ? 178 SER HHH C   1 
ATOM   2866  O O   . SER B 2 178 ? 44.855  82.304  50.786  1.000 52.144  ? 178 SER HHH O   1 
ATOM   2867  C CB  . SER B 2 178 ? 43.686  83.395  53.417  1.000 54.581  ? 178 SER HHH CB  1 
ATOM   2868  O OG  . SER B 2 178 ? 44.740  83.601  54.334  1.000 62.122  ? 178 SER HHH OG  1 
ATOM   2869  N N   . SER B 2 179 ? 45.949  81.009  52.302  1.000 47.535  ? 179 SER HHH N   1 
ATOM   2870  C CA  . SER B 2 179 ? 47.059  80.556  51.414  1.000 43.205  ? 179 SER HHH CA  1 
ATOM   2871  C C   . SER B 2 179 ? 46.588  79.518  50.378  1.000 38.545  ? 179 SER HHH C   1 
ATOM   2872  O O   . SER B 2 179 ? 47.360  79.176  49.502  1.000 34.354  ? 179 SER HHH O   1 
ATOM   2873  C CB  . SER B 2 179 ? 48.204  80.026  52.237  1.000 43.730  ? 179 SER HHH CB  1 
ATOM   2874  O OG  . SER B 2 179 ? 47.835  78.881  52.980  1.000 39.352  ? 179 SER HHH OG  1 
ATOM   2875  N N   . GLY B 2 180 ? 45.362  79.013  50.488  1.000 41.000  ? 180 GLY HHH N   1 
ATOM   2876  C CA  . GLY B 2 180 ? 44.790  78.001  49.573  1.000 42.242  ? 180 GLY HHH CA  1 
ATOM   2877  C C   . GLY B 2 180 ? 45.204  76.591  49.948  1.000 40.485  ? 180 GLY HHH C   1 
ATOM   2878  O O   . GLY B 2 180 ? 44.766  75.645  49.248  1.000 43.974  ? 180 GLY HHH O   1 
ATOM   2879  N N   . LEU B 2 181 ? 46.016  76.476  51.002  1.000 36.966  ? 181 LEU HHH N   1 
ATOM   2880  C CA  . LEU B 2 181 ? 46.499  75.216  51.611  1.000 35.301  ? 181 LEU HHH CA  1 
ATOM   2881  C C   . LEU B 2 181 ? 45.589  74.863  52.786  1.000 35.212  ? 181 LEU HHH C   1 
ATOM   2882  O O   . LEU B 2 181 ? 45.166  75.790  53.498  1.000 33.309  ? 181 LEU HHH O   1 
ATOM   2883  C CB  . LEU B 2 181 ? 47.933  75.418  52.118  1.000 34.831  ? 181 LEU HHH CB  1 
ATOM   2884  C CG  . LEU B 2 181 ? 48.987  75.739  51.064  1.000 33.551  ? 181 LEU HHH CG  1 
ATOM   2885  C CD1 . LEU B 2 181 ? 50.348  75.824  51.720  1.000 32.626  ? 181 LEU HHH CD1 1 
ATOM   2886  C CD2 . LEU B 2 181 ? 48.994  74.702  49.949  1.000 33.103  ? 181 LEU HHH CD2 1 
ATOM   2887  N N   . TYR B 2 182 ? 45.350  73.566  53.005  1.000 35.203  ? 182 TYR HHH N   1 
ATOM   2888  C CA  . TYR B 2 182 ? 44.519  73.023  54.112  1.000 31.574  ? 182 TYR HHH CA  1 
ATOM   2889  C C   . TYR B 2 182 ? 45.373  72.815  55.363  1.000 31.662  ? 182 TYR HHH C   1 
ATOM   2890  O O   . TYR B 2 182 ? 46.604  72.737  55.282  1.000 33.079  ? 182 TYR HHH O   1 
ATOM   2891  C CB  . TYR B 2 182 ? 43.872  71.702  53.710  1.000 30.073  ? 182 TYR HHH CB  1 
ATOM   2892  C CG  . TYR B 2 182 ? 42.897  71.823  52.576  1.000 29.914  ? 182 TYR HHH CG  1 
ATOM   2893  C CD1 . TYR B 2 182 ? 43.314  71.644  51.270  1.000 32.110  ? 182 TYR HHH CD1 1 
ATOM   2894  C CD2 . TYR B 2 182 ? 41.562  72.090  52.796  1.000 29.929  ? 182 TYR HHH CD2 1 
ATOM   2895  C CE1 . TYR B 2 182 ? 42.429  71.716  50.210  1.000 32.406  ? 182 TYR HHH CE1 1 
ATOM   2896  C CE2 . TYR B 2 182 ? 40.668  72.185  51.745  1.000 31.043  ? 182 TYR HHH CE2 1 
ATOM   2897  C CZ  . TYR B 2 182 ? 41.108  71.990  50.452  1.000 31.147  ? 182 TYR HHH CZ  1 
ATOM   2898  O OH  . TYR B 2 182 ? 40.295  72.070  49.378  1.000 34.864  ? 182 TYR HHH OH  1 
ATOM   2899  N N   . SER B 2 183 ? 44.712  72.693  56.507  1.000 30.663  ? 183 SER HHH N   1 
ATOM   2900  C CA  . SER B 2 183 ? 45.348  72.612  57.842  1.000 29.077  ? 183 SER HHH CA  1 
ATOM   2901  C C   . SER B 2 183 ? 44.341  72.065  58.844  1.000 28.508  ? 183 SER HHH C   1 
ATOM   2902  O O   . SER B 2 183 ? 43.164  72.470  58.822  1.000 31.323  ? 183 SER HHH O   1 
ATOM   2903  C CB  . SER B 2 183 ? 45.850  73.953  58.272  1.000 29.641  ? 183 SER HHH CB  1 
ATOM   2904  O OG  . SER B 2 183 ? 46.315  73.904  59.609  1.000 30.664  ? 183 SER HHH OG  1 
ATOM   2905  N N   . LEU B 2 184 ? 44.825  71.236  59.742  1.000 28.214  ? 184 LEU HHH N   1 
ATOM   2906  C CA  . LEU B 2 184 ? 44.012  70.258  60.490  1.000 31.226  ? 184 LEU HHH CA  1 
ATOM   2907  C C   . LEU B 2 184 ? 44.802  69.963  61.746  1.000 31.563  ? 184 LEU HHH C   1 
ATOM   2908  O O   . LEU B 2 184 ? 46.035  70.017  61.666  1.000 37.044  ? 184 LEU HHH O   1 
ATOM   2909  C CB  . LEU B 2 184 ? 43.888  69.047  59.559  1.000 34.566  ? 184 LEU HHH CB  1 
ATOM   2910  C CG  . LEU B 2 184 ? 43.359  67.742  60.131  1.000 36.042  ? 184 LEU HHH CG  1 
ATOM   2911  C CD1 . LEU B 2 184 ? 42.795  66.881  59.018  1.000 38.916  ? 184 LEU HHH CD1 1 
ATOM   2912  C CD2 . LEU B 2 184 ? 44.435  66.971  60.858  1.000 34.442  ? 184 LEU HHH CD2 1 
ATOM   2913  N N   . SER B 2 185 ? 44.159  69.729  62.873  1.000 33.515  ? 185 SER HHH N   1 
ATOM   2914  C CA  . SER B 2 185 ? 44.894  69.259  64.077  1.000 37.890  ? 185 SER HHH CA  1 
ATOM   2915  C C   . SER B 2 185 ? 44.154  68.046  64.646  1.000 36.385  ? 185 SER HHH C   1 
ATOM   2916  O O   . SER B 2 185 ? 42.932  68.005  64.536  1.000 42.905  ? 185 SER HHH O   1 
ATOM   2917  C CB  . SER B 2 185 ? 45.171  70.363  65.096  1.000 40.036  ? 185 SER HHH CB  1 
ATOM   2918  O OG  . SER B 2 185 ? 44.060  71.222  65.244  1.000 51.191  ? 185 SER HHH OG  1 
ATOM   2919  N N   . SER B 2 186 ? 44.910  67.041  65.087  1.000 33.381  ? 186 SER HHH N   1 
ATOM   2920  C CA  . SER B 2 186 ? 44.423  65.773  65.677  1.000 32.105  ? 186 SER HHH CA  1 
ATOM   2921  C C   . SER B 2 186 ? 44.876  65.750  67.129  1.000 33.499  ? 186 SER HHH C   1 
ATOM   2922  O O   . SER B 2 186 ? 46.056  65.958  67.387  1.000 33.691  ? 186 SER HHH O   1 
ATOM   2923  C CB  . SER B 2 186 ? 44.937  64.572  64.930  1.000 30.525  ? 186 SER HHH CB  1 
ATOM   2924  O OG  . SER B 2 186 ? 44.375  63.369  65.428  1.000 28.017  ? 186 SER HHH OG  1 
ATOM   2925  N N   . VAL B 2 187 ? 43.953  65.548  68.049  1.000 34.701  ? 187 VAL HHH N   1 
ATOM   2926  C CA  . VAL B 2 187 ? 44.261  65.646  69.499  1.000 36.386  ? 187 VAL HHH CA  1 
ATOM   2927  C C   . VAL B 2 187 ? 43.806  64.337  70.119  1.000 35.749  ? 187 VAL HHH C   1 
ATOM   2928  O O   . VAL B 2 187 ? 42.989  63.654  69.485  1.000 36.447  ? 187 VAL HHH O   1 
ATOM   2929  C CB  . VAL B 2 187 ? 43.559  66.865  70.128  1.000 38.728  ? 187 VAL HHH CB  1 
ATOM   2930  C CG1 . VAL B 2 187 ? 44.023  68.169  69.498  1.000 40.152  ? 187 VAL HHH CG1 1 
ATOM   2931  C CG2 . VAL B 2 187 ? 42.043  66.766  70.035  1.000 38.926  ? 187 VAL HHH CG2 1 
ATOM   2932  N N   . VAL B 2 188 ? 44.307  64.024  71.308  1.000 35.118  ? 188 VAL HHH N   1 
ATOM   2933  C CA  . VAL B 2 188 ? 43.884  62.828  72.086  1.000 35.587  ? 188 VAL HHH CA  1 
ATOM   2934  C C   . VAL B 2 188 ? 44.047  63.150  73.571  1.000 37.945  ? 188 VAL HHH C   1 
ATOM   2935  O O   . VAL B 2 188 ? 45.017  63.845  73.909  1.000 38.425  ? 188 VAL HHH O   1 
ATOM   2936  C CB  . VAL B 2 188 ? 44.689  61.587  71.663  1.000 35.892  ? 188 VAL HHH CB  1 
ATOM   2937  C CG1 . VAL B 2 188 ? 46.186  61.848  71.700  1.000 37.353  ? 188 VAL HHH CG1 1 
ATOM   2938  C CG2 . VAL B 2 188 ? 44.334  60.354  72.486  1.000 35.823  ? 188 VAL HHH CG2 1 
ATOM   2939  N N   . THR B 2 189 ? 43.116  62.675  74.403  1.000 41.317  ? 189 THR HHH N   1 
ATOM   2940  C CA  . THR B 2 189 ? 43.192  62.730  75.886  1.000 42.573  ? 189 THR HHH CA  1 
ATOM   2941  C C   . THR B 2 189 ? 43.679  61.375  76.404  1.000 44.706  ? 189 THR HHH C   1 
ATOM   2942  O O   . THR B 2 189 ? 43.117  60.345  75.990  1.000 47.342  ? 189 THR HHH O   1 
ATOM   2943  C CB  . THR B 2 189 ? 41.864  63.167  76.515  1.000 41.156  ? 189 THR HHH CB  1 
ATOM   2944  O OG1 . THR B 2 189 ? 40.805  62.442  75.906  1.000 41.164  ? 189 THR HHH OG1 1 
ATOM   2945  C CG2 . THR B 2 189 ? 41.581  64.640  76.340  1.000 43.832  ? 189 THR HHH CG2 1 
ATOM   2946  N N   . VAL B 2 190 ? 44.713  61.402  77.246  1.000 47.496  ? 190 VAL HHH N   1 
ATOM   2947  C CA  . VAL B 2 190 ? 45.311  60.209  77.904  1.000 52.959  ? 190 VAL HHH CA  1 
ATOM   2948  C C   . VAL B 2 190 ? 45.520  60.526  79.378  1.000 61.561  ? 190 VAL HHH C   1 
ATOM   2949  O O   . VAL B 2 190 ? 45.623  61.689  79.753  1.000 62.561  ? 190 VAL HHH O   1 
ATOM   2950  C CB  . VAL B 2 190 ? 46.627  59.812  77.217  1.000 53.513  ? 190 VAL HHH CB  1 
ATOM   2951  C CG1 . VAL B 2 190 ? 46.390  59.546  75.743  1.000 56.305  ? 190 VAL HHH CG1 1 
ATOM   2952  C CG2 . VAL B 2 190 ? 47.719  60.853  77.405  1.000 53.034  ? 190 VAL HHH CG2 1 
ATOM   2953  N N   . PRO B 2 191 ? 45.571  59.506  80.265  1.000 73.646  ? 191 PRO HHH N   1 
ATOM   2954  C CA  . PRO B 2 191 ? 45.930  59.724  81.666  1.000 77.510  ? 191 PRO HHH CA  1 
ATOM   2955  C C   . PRO B 2 191 ? 47.272  60.454  81.816  1.000 80.623  ? 191 PRO HHH C   1 
ATOM   2956  O O   . PRO B 2 191 ? 48.213  60.086  81.129  1.000 84.038  ? 191 PRO HHH O   1 
ATOM   2957  C CB  . PRO B 2 191 ? 46.023  58.293  82.210  1.000 75.878  ? 191 PRO HHH CB  1 
ATOM   2958  C CG  . PRO B 2 191 ? 45.021  57.537  81.372  1.000 72.386  ? 191 PRO HHH CG  1 
ATOM   2959  C CD  . PRO B 2 191 ? 45.228  58.104  79.987  1.000 73.638  ? 191 PRO HHH CD  1 
ATOM   2960  N N   . SER B 2 192 ? 47.340  61.460  82.696  1.000 77.567  ? 192 SER HHH N   1 
ATOM   2961  C CA  . SER B 2 192 ? 48.555  62.303  82.864  1.000 78.158  ? 192 SER HHH CA  1 
ATOM   2962  C C   . SER B 2 192 ? 49.722  61.457  83.392  1.000 74.558  ? 192 SER HHH C   1 
ATOM   2963  O O   . SER B 2 192 ? 50.844  61.753  83.017  1.000 73.820  ? 192 SER HHH O   1 
ATOM   2964  C CB  . SER B 2 192 ? 48.293  63.516  83.729  1.000 82.491  ? 192 SER HHH CB  1 
ATOM   2965  O OG  . SER B 2 192 ? 47.409  63.205  84.794  1.000 90.741  ? 192 SER HHH OG  1 
ATOM   2966  N N   . SER B 2 193 ? 49.469  60.436  84.214  1.000 75.466  ? 193 SER HHH N   1 
ATOM   2967  C CA  . SER B 2 193 ? 50.506  59.505  84.744  1.000 75.562  ? 193 SER HHH CA  1 
ATOM   2968  C C   . SER B 2 193 ? 51.212  58.754  83.600  1.000 78.064  ? 193 SER HHH C   1 
ATOM   2969  O O   . SER B 2 193 ? 52.407  58.405  83.758  1.000 78.047  ? 193 SER HHH O   1 
ATOM   2970  C CB  . SER B 2 193 ? 49.909  58.539  85.721  1.000 73.600  ? 193 SER HHH CB  1 
ATOM   2971  O OG  . SER B 2 193 ? 48.939  57.736  85.075  1.000 69.448  ? 193 SER HHH OG  1 
ATOM   2972  N N   . SER B 2 194 ? 50.528  58.526  82.474  1.000 77.281  ? 194 SER HHH N   1 
ATOM   2973  C CA  . SER B 2 194 ? 51.066  57.759  81.317  1.000 75.879  ? 194 SER HHH CA  1 
ATOM   2974  C C   . SER B 2 194 ? 51.981  58.634  80.447  1.000 73.791  ? 194 SER HHH C   1 
ATOM   2975  O O   . SER B 2 194 ? 52.425  58.134  79.408  1.000 85.605  ? 194 SER HHH O   1 
ATOM   2976  C CB  . SER B 2 194 ? 49.945  57.173  80.486  1.000 78.492  ? 194 SER HHH CB  1 
ATOM   2977  O OG  . SER B 2 194 ? 49.247  58.185  79.758  1.000 79.999  ? 194 SER HHH OG  1 
ATOM   2978  N N   . LEU B 2 195 ? 52.235  59.893  80.812  1.000 69.820  ? 195 LEU HHH N   1 
ATOM   2979  C CA  . LEU B 2 195 ? 53.025  60.812  79.952  1.000 67.774  ? 195 LEU HHH CA  1 
ATOM   2980  C C   . LEU B 2 195 ? 54.508  60.440  80.016  1.000 69.029  ? 195 LEU HHH C   1 
ATOM   2981  O O   . LEU B 2 195 ? 55.228  60.776  79.049  1.000 69.811  ? 195 LEU HHH O   1 
ATOM   2982  C CB  . LEU B 2 195 ? 52.791  62.267  80.366  1.000 62.095  ? 195 LEU HHH CB  1 
ATOM   2983  C CG  . LEU B 2 195 ? 51.521  62.908  79.807  1.000 58.698  ? 195 LEU HHH CG  1 
ATOM   2984  C CD1 . LEU B 2 195 ? 51.421  64.361  80.228  1.000 62.699  ? 195 LEU HHH CD1 1 
ATOM   2985  C CD2 . LEU B 2 195 ? 51.473  62.817  78.295  1.000 57.519  ? 195 LEU HHH CD2 1 
ATOM   2986  N N   . GLY B 2 196 ? 54.947  59.771  81.086  1.000 68.786  ? 196 GLY HHH N   1 
ATOM   2987  C CA  . GLY B 2 196 ? 56.365  59.382  81.248  1.000 71.776  ? 196 GLY HHH CA  1 
ATOM   2988  C C   . GLY B 2 196 ? 56.646  57.999  80.676  1.000 72.077  ? 196 GLY HHH C   1 
ATOM   2989  O O   . GLY B 2 196 ? 57.792  57.742  80.230  1.000 70.750  ? 196 GLY HHH O   1 
ATOM   2990  N N   . THR B 2 197 ? 55.601  57.178  80.602  1.000 74.564  ? 197 THR HHH N   1 
ATOM   2991  C CA  . THR B 2 197 ? 55.693  55.697  80.506  1.000 72.569  ? 197 THR HHH CA  1 
ATOM   2992  C C   . THR B 2 197 ? 55.310  55.226  79.096  1.000 65.777  ? 197 THR HHH C   1 
ATOM   2993  O O   . THR B 2 197 ? 55.867  54.225  78.654  1.000 66.180  ? 197 THR HHH O   1 
ATOM   2994  C CB  . THR B 2 197 ? 54.823  55.054  81.600  1.000 77.718  ? 197 THR HHH CB  1 
ATOM   2995  O OG1 . THR B 2 197 ? 53.500  54.808  81.100  1.000 79.992  ? 197 THR HHH OG1 1 
ATOM   2996  C CG2 . THR B 2 197 ? 54.744  55.901  82.859  1.000 74.435  ? 197 THR HHH CG2 1 
ATOM   2997  N N   . GLN B 2 198 ? 54.456  55.963  78.389  1.000 61.926  ? 198 GLN HHH N   1 
ATOM   2998  C CA  . GLN B 2 198 ? 53.870  55.539  77.095  1.000 60.509  ? 198 GLN HHH CA  1 
ATOM   2999  C C   . GLN B 2 198 ? 54.391  56.487  76.014  1.000 55.995  ? 198 GLN HHH C   1 
ATOM   3000  O O   . GLN B 2 198 ? 54.369  57.703  76.240  1.000 60.297  ? 198 GLN HHH O   1 
ATOM   3001  C CB  . GLN B 2 198 ? 52.342  55.538  77.211  1.000 64.378  ? 198 GLN HHH CB  1 
ATOM   3002  C CG  . GLN B 2 198 ? 51.614  55.129  75.937  1.000 67.203  ? 198 GLN HHH CG  1 
ATOM   3003  C CD  . GLN B 2 198 ? 51.920  53.711  75.564  1.000 71.108  ? 198 GLN HHH CD  1 
ATOM   3004  O OE1 . GLN B 2 198 ? 52.825  53.463  74.775  1.000 72.698  ? 198 GLN HHH OE1 1 
ATOM   3005  N NE2 . GLN B 2 198 ? 51.184  52.782  76.160  1.000 78.912  ? 198 GLN HHH NE2 1 
ATOM   3006  N N   . THR B 2 199 ? 54.852  55.942  74.898  1.000 53.706  ? 199 THR HHH N   1 
ATOM   3007  C CA  . THR B 2 199 ? 55.222  56.710  73.686  1.000 52.593  ? 199 THR HHH CA  1 
ATOM   3008  C C   . THR B 2 199 ? 53.950  57.092  72.916  1.000 54.518  ? 199 THR HHH C   1 
ATOM   3009  O O   . THR B 2 199 ? 53.094  56.182  72.687  1.000 53.403  ? 199 THR HHH O   1 
ATOM   3010  C CB  . THR B 2 199 ? 56.102  55.889  72.739  1.000 54.363  ? 199 THR HHH CB  1 
ATOM   3011  O OG1 . THR B 2 199 ? 57.243  55.368  73.407  1.000 54.984  ? 199 THR HHH OG1 1 
ATOM   3012  C CG2 . THR B 2 199 ? 56.527  56.716  71.550  1.000 57.230  ? 199 THR HHH CG2 1 
ATOM   3013  N N   . TYR B 2 200 ? 53.810  58.379  72.558  1.000 49.793  ? 200 TYR HHH N   1 
ATOM   3014  C CA  . TYR B 2 200 ? 52.728  58.916  71.699  1.000 44.434  ? 200 TYR HHH CA  1 
ATOM   3015  C C   . TYR B 2 200 ? 53.334  59.383  70.383  1.000 41.948  ? 200 TYR HHH C   1 
ATOM   3016  O O   . TYR B 2 200 ? 54.227  60.235  70.402  1.000 42.776  ? 200 TYR HHH O   1 
ATOM   3017  C CB  . TYR B 2 200 ? 51.972  60.018  72.429  1.000 43.128  ? 200 TYR HHH CB  1 
ATOM   3018  C CG  . TYR B 2 200 ? 51.219  59.453  73.594  1.000 42.011  ? 200 TYR HHH CG  1 
ATOM   3019  C CD1 . TYR B 2 200 ? 50.151  58.611  73.379  1.000 42.038  ? 200 TYR HHH CD1 1 
ATOM   3020  C CD2 . TYR B 2 200 ? 51.622  59.681  74.895  1.000 42.540  ? 200 TYR HHH CD2 1 
ATOM   3021  C CE1 . TYR B 2 200 ? 49.459  58.051  74.436  1.000 44.540  ? 200 TYR HHH CE1 1 
ATOM   3022  C CE2 . TYR B 2 200 ? 50.941  59.128  75.964  1.000 45.276  ? 200 TYR HHH CE2 1 
ATOM   3023  C CZ  . TYR B 2 200 ? 49.854  58.306  75.735  1.000 44.633  ? 200 TYR HHH CZ  1 
ATOM   3024  O OH  . TYR B 2 200 ? 49.176  57.748  76.779  1.000 44.100  ? 200 TYR HHH OH  1 
ATOM   3025  N N   . ILE B 2 201 ? 52.880  58.778  69.288  1.000 41.021  ? 201 ILE HHH N   1 
ATOM   3026  C CA  . ILE B 2 201 ? 53.293  59.110  67.895  1.000 41.187  ? 201 ILE HHH CA  1 
ATOM   3027  C C   . ILE B 2 201 ? 52.029  59.300  67.070  1.000 42.716  ? 201 ILE HHH C   1 
ATOM   3028  O O   . ILE B 2 201 ? 51.169  58.399  67.135  1.000 45.819  ? 201 ILE HHH O   1 
ATOM   3029  C CB  . ILE B 2 201 ? 54.136  57.983  67.283  1.000 40.369  ? 201 ILE HHH CB  1 
ATOM   3030  C CG1 . ILE B 2 201 ? 55.404  57.699  68.088  1.000 40.922  ? 201 ILE HHH CG1 1 
ATOM   3031  C CG2 . ILE B 2 201 ? 54.432  58.303  65.827  1.000 40.750  ? 201 ILE HHH CG2 1 
ATOM   3032  C CD1 . ILE B 2 201 ? 56.337  56.733  67.400  1.000 42.773  ? 201 ILE HHH CD1 1 
ATOM   3033  N N   . CYS B 2 202 ? 51.930  60.386  66.303  1.000 43.010  ? 202 CYS HHH N   1 
ATOM   3034  C CA  . CYS B 2 202 ? 50.875  60.520  65.272  1.000 46.867  ? 202 CYS HHH CA  1 
ATOM   3035  C C   . CYS B 2 202 ? 51.466  60.179  63.889  1.000 40.849  ? 202 CYS HHH C   1 
ATOM   3036  O O   . CYS B 2 202 ? 52.575  60.609  63.574  1.000 36.460  ? 202 CYS HHH O   1 
ATOM   3037  C CB  . CYS B 2 202 ? 50.206  61.887  65.312  1.000 54.475  ? 202 CYS HHH CB  1 
ATOM   3038  S SG  . CYS B 2 202 ? 51.125  63.175  64.433  1.000 65.069  ? 202 CYS HHH SG  1 
ATOM   3039  N N   . ASN B 2 203 ? 50.726  59.399  63.106  1.000 36.348  ? 203 ASN HHH N   1 
ATOM   3040  C CA  . ASN B 2 203 ? 51.125  58.930  61.766  1.000 32.801  ? 203 ASN HHH CA  1 
ATOM   3041  C C   . ASN B 2 203 ? 50.264  59.713  60.794  1.000 31.142  ? 203 ASN HHH C   1 
ATOM   3042  O O   . ASN B 2 203 ? 49.032  59.707  60.927  1.000 32.176  ? 203 ASN HHH O   1 
ATOM   3043  C CB  . ASN B 2 203 ? 50.987  57.418  61.660  1.000 34.371  ? 203 ASN HHH CB  1 
ATOM   3044  C CG  . ASN B 2 203 ? 51.332  56.751  62.976  1.000 34.924  ? 203 ASN HHH CG  1 
ATOM   3045  O OD1 . ASN B 2 203 ? 50.451  56.579  63.821  1.000 38.437  ? 203 ASN HHH OD1 1 
ATOM   3046  N ND2 . ASN B 2 203 ? 52.610  56.445  63.188  1.000 29.346  ? 203 ASN HHH ND2 1 
ATOM   3047  N N   . VAL B 2 204 ? 50.917  60.473  59.938  1.000 30.998  ? 204 VAL HHH N   1 
ATOM   3048  C CA  . VAL B 2 204 ? 50.240  61.313  58.917  1.000 29.683  ? 204 VAL HHH CA  1 
ATOM   3049  C C   . VAL B 2 204 ? 50.564  60.719  57.556  1.000 28.256  ? 204 VAL HHH C   1 
ATOM   3050  O O   . VAL B 2 204 ? 51.734  60.394  57.313  1.000 28.473  ? 204 VAL HHH O   1 
ATOM   3051  C CB  . VAL B 2 204 ? 50.676  62.776  59.040  1.000 31.805  ? 204 VAL HHH CB  1 
ATOM   3052  C CG1 . VAL B 2 204 ? 49.895  63.663  58.090  1.000 34.894  ? 204 VAL HHH CG1 1 
ATOM   3053  C CG2 . VAL B 2 204 ? 50.517  63.276  60.466  1.000 32.593  ? 204 VAL HHH CG2 1 
ATOM   3054  N N   . ASN B 2 205 ? 49.535  60.481  56.758  1.000 29.078  ? 205 ASN HHH N   1 
ATOM   3055  C CA  . ASN B 2 205 ? 49.694  59.946  55.390  1.000 31.225  ? 205 ASN HHH CA  1 
ATOM   3056  C C   . ASN B 2 205 ? 49.000  60.932  54.439  1.000 31.862  ? 205 ASN HHH C   1 
ATOM   3057  O O   . ASN B 2 205 ? 47.826  61.249  54.660  1.000 31.595  ? 205 ASN HHH O   1 
ATOM   3058  C CB  . ASN B 2 205 ? 49.212  58.492  55.276  1.000 31.781  ? 205 ASN HHH CB  1 
ATOM   3059  C CG  . ASN B 2 205 ? 49.601  57.878  53.947  1.000 33.113  ? 205 ASN HHH CG  1 
ATOM   3060  O OD1 . ASN B 2 205 ? 50.615  58.280  53.389  1.000 31.405  ? 205 ASN HHH OD1 1 
ATOM   3061  N ND2 . ASN B 2 205 ? 48.808  56.961  53.404  1.000 34.549  ? 205 ASN HHH ND2 1 
ATOM   3062  N N   . HIS B 2 206 ? 49.738  61.453  53.462  1.000 31.548  ? 206 HIS HHH N   1 
ATOM   3063  C CA  . HIS B 2 206 ? 49.209  62.297  52.367  1.000 30.676  ? 206 HIS HHH CA  1 
ATOM   3064  C C   . HIS B 2 206 ? 49.546  61.617  51.039  1.000 30.661  ? 206 HIS HHH C   1 
ATOM   3065  O O   . HIS B 2 206 ? 50.607  61.914  50.459  1.000 28.050  ? 206 HIS HHH O   1 
ATOM   3066  C CB  . HIS B 2 206 ? 49.739  63.730  52.498  1.000 30.062  ? 206 HIS HHH CB  1 
ATOM   3067  C CG  . HIS B 2 206 ? 49.098  64.684  51.551  1.000 29.278  ? 206 HIS HHH CG  1 
ATOM   3068  N ND1 . HIS B 2 206 ? 49.811  65.568  50.777  1.000 30.344  ? 206 HIS HHH ND1 1 
ATOM   3069  C CD2 . HIS B 2 206 ? 47.803  64.866  51.236  1.000 30.852  ? 206 HIS HHH CD2 1 
ATOM   3070  C CE1 . HIS B 2 206 ? 48.982  66.281  50.046  1.000 31.805  ? 206 HIS HHH CE1 1 
ATOM   3071  N NE2 . HIS B 2 206 ? 47.739  65.879  50.326  1.000 32.581  ? 206 HIS HHH NE2 1 
ATOM   3072  N N   . LYS B 2 207 ? 48.655  60.742  50.576  1.000 33.611  ? 207 LYS HHH N   1 
ATOM   3073  C CA  . LYS B 2 207 ? 48.894  59.910  49.363  1.000 38.129  ? 207 LYS HHH CA  1 
ATOM   3074  C C   . LYS B 2 207 ? 49.267  60.796  48.174  1.000 36.100  ? 207 LYS HHH C   1 
ATOM   3075  O O   . LYS B 2 207 ? 50.211  60.473  47.459  1.000 37.909  ? 207 LYS HHH O   1 
ATOM   3076  C CB  . LYS B 2 207 ? 47.691  59.011  49.064  1.000 44.168  ? 207 LYS HHH CB  1 
ATOM   3077  C CG  . LYS B 2 207 ? 47.521  57.813  49.995  1.000 52.028  ? 207 LYS HHH CG  1 
ATOM   3078  C CD  . LYS B 2 207 ? 47.098  56.561  49.247  1.000 62.328  ? 207 LYS HHH CD  1 
ATOM   3079  C CE  . LYS B 2 207 ? 47.066  55.323  50.116  1.000 72.368  ? 207 LYS HHH CE  1 
ATOM   3080  N NZ  . LYS B 2 207 ? 45.920  55.387  51.050  1.000 83.569  ? 207 LYS HHH NZ  1 
ATOM   3081  N N   . PRO B 2 208 ? 48.545  61.910  47.903  1.000 37.449  ? 208 PRO HHH N   1 
ATOM   3082  C CA  . PRO B 2 208 ? 48.799  62.756  46.733  1.000 35.249  ? 208 PRO HHH CA  1 
ATOM   3083  C C   . PRO B 2 208 ? 50.256  63.211  46.595  1.000 33.139  ? 208 PRO HHH C   1 
ATOM   3084  O O   . PRO B 2 208 ? 50.739  63.259  45.487  1.000 31.572  ? 208 PRO HHH O   1 
ATOM   3085  C CB  . PRO B 2 208 ? 47.909  63.983  46.970  1.000 36.122  ? 208 PRO HHH CB  1 
ATOM   3086  C CG  . PRO B 2 208 ? 46.755  63.408  47.733  1.000 40.367  ? 208 PRO HHH CG  1 
ATOM   3087  C CD  . PRO B 2 208 ? 47.373  62.377  48.655  1.000 42.264  ? 208 PRO HHH CD  1 
ATOM   3088  N N   . SER B 2 209 ? 50.898  63.536  47.723  1.000 31.137  ? 209 SER HHH N   1 
ATOM   3089  C CA  . SER B 2 209 ? 52.286  64.058  47.803  1.000 29.091  ? 209 SER HHH CA  1 
ATOM   3090  C C   . SER B 2 209 ? 53.251  62.936  48.177  1.000 30.789  ? 209 SER HHH C   1 
ATOM   3091  O O   . SER B 2 209 ? 54.463  63.204  48.321  1.000 29.457  ? 209 SER HHH O   1 
ATOM   3092  C CB  . SER B 2 209 ? 52.350  65.175  48.786  1.000 26.024  ? 209 SER HHH CB  1 
ATOM   3093  O OG  . SER B 2 209 ? 52.360  64.675  50.110  1.000 22.758  ? 209 SER HHH OG  1 
ATOM   3094  N N   . ASN B 2 210 ? 52.711  61.730  48.337  1.000 38.280  ? 210 ASN HHH N   1 
ATOM   3095  C CA  . ASN B 2 210 ? 53.458  60.493  48.695  1.000 42.942  ? 210 ASN HHH CA  1 
ATOM   3096  C C   . ASN B 2 210 ? 54.285  60.784  49.945  1.000 36.970  ? 210 ASN HHH C   1 
ATOM   3097  O O   . ASN B 2 210 ? 55.458  60.502  49.957  1.000 37.344  ? 210 ASN HHH O   1 
ATOM   3098  C CB  . ASN B 2 210 ? 54.287  59.975  47.511  1.000 46.951  ? 210 ASN HHH CB  1 
ATOM   3099  C CG  . ASN B 2 210 ? 54.723  58.530  47.650  1.000 49.406  ? 210 ASN HHH CG  1 
ATOM   3100  O OD1 . ASN B 2 210 ? 55.232  58.135  48.702  1.000 50.791  ? 210 ASN HHH OD1 1 
ATOM   3101  N ND2 . ASN B 2 210 ? 54.545  57.739  46.595  1.000 54.545  ? 210 ASN HHH ND2 1 
ATOM   3102  N N   . THR B 2 211 ? 53.629  61.274  50.981  1.000 34.748  ? 211 THR HHH N   1 
ATOM   3103  C CA  . THR B 2 211 ? 54.226  61.750  52.247  1.000 37.951  ? 211 THR HHH CA  1 
ATOM   3104  C C   . THR B 2 211 ? 53.737  60.867  53.376  1.000 36.968  ? 211 THR HHH C   1 
ATOM   3105  O O   . THR B 2 211 ? 52.561  61.008  53.688  1.000 39.106  ? 211 THR HHH O   1 
ATOM   3106  C CB  . THR B 2 211 ? 53.784  63.194  52.519  1.000 42.220  ? 211 THR HHH CB  1 
ATOM   3107  O OG1 . THR B 2 211 ? 54.414  63.983  51.510  1.000 53.501  ? 211 THR HHH OG1 1 
ATOM   3108  C CG2 . THR B 2 211 ? 54.099  63.699  53.911  1.000 40.438  ? 211 THR HHH CG2 1 
ATOM   3109  N N   . LYS B 2 212 ? 54.578  59.978  53.899  1.000 40.592  ? 212 LYS HHH N   1 
ATOM   3110  C CA  . LYS B 2 212 ? 54.274  59.201  55.134  1.000 43.383  ? 212 LYS HHH CA  1 
ATOM   3111  C C   . LYS B 2 212 ? 55.209  59.731  56.222  1.000 37.057  ? 212 LYS HHH C   1 
ATOM   3112  O O   . LYS B 2 212 ? 56.424  59.680  56.031  1.000 34.403  ? 212 LYS HHH O   1 
ATOM   3113  C CB  . LYS B 2 212 ? 54.330  57.666  54.967  1.000 47.736  ? 212 LYS HHH CB  1 
ATOM   3114  C CG  . LYS B 2 212 ? 53.318  56.961  55.879  1.000 56.651  ? 212 LYS HHH CG  1 
ATOM   3115  C CD  . LYS B 2 212 ? 53.237  55.468  55.863  1.000 59.440  ? 212 LYS HHH CD  1 
ATOM   3116  C CE  . LYS B 2 212 ? 51.930  54.987  55.275  1.000 64.874  ? 212 LYS HHH CE  1 
ATOM   3117  N NZ  . LYS B 2 212 ? 52.174  53.713  54.560  1.000 76.663  ? 212 LYS HHH NZ  1 
ATOM   3118  N N   . VAL B 2 213 ? 54.643  60.263  57.304  1.000 34.895  ? 213 VAL HHH N   1 
ATOM   3119  C CA  . VAL B 2 213 ? 55.405  60.941  58.379  1.000 36.349  ? 213 VAL HHH CA  1 
ATOM   3120  C C   . VAL B 2 213 ? 54.865  60.469  59.718  1.000 36.647  ? 213 VAL HHH C   1 
ATOM   3121  O O   . VAL B 2 213 ? 53.643  60.396  59.871  1.000 39.718  ? 213 VAL HHH O   1 
ATOM   3122  C CB  . VAL B 2 213 ? 55.305  62.464  58.235  1.000 39.839  ? 213 VAL HHH CB  1 
ATOM   3123  C CG1 . VAL B 2 213 ? 55.629  63.211  59.531  1.000 40.468  ? 213 VAL HHH CG1 1 
ATOM   3124  C CG2 . VAL B 2 213 ? 56.195  62.927  57.086  1.000 43.677  ? 213 VAL HHH CG2 1 
ATOM   3125  N N   . ASP B 2 214 ? 55.789  60.119  60.605  1.000 40.076  ? 214 ASP HHH N   1 
ATOM   3126  C CA  . ASP B 2 214 ? 55.549  59.716  62.008  1.000 46.364  ? 214 ASP HHH CA  1 
ATOM   3127  C C   . ASP B 2 214 ? 56.191  60.799  62.873  1.000 49.356  ? 214 ASP HHH C   1 
ATOM   3128  O O   . ASP B 2 214 ? 57.413  61.017  62.745  1.000 55.221  ? 214 ASP HHH O   1 
ATOM   3129  C CB  . ASP B 2 214 ? 56.124  58.328  62.297  1.000 50.261  ? 214 ASP HHH CB  1 
ATOM   3130  C CG  . ASP B 2 214 ? 55.467  57.190  61.524  1.000 58.252  ? 214 ASP HHH CG  1 
ATOM   3131  O OD1 . ASP B 2 214 ? 54.244  57.306  61.150  1.000 63.744  ? 214 ASP HHH OD1 1 
ATOM   3132  O OD2 . ASP B 2 214 ? 56.180  56.198  61.283  1.000 66.400  ? 214 ASP HHH OD2 1 
ATOM   3133  N N   . LYS B 2 215 ? 55.396  61.486  63.684  1.000 50.509  ? 215 LYS HHH N   1 
ATOM   3134  C CA  . LYS B 2 215 ? 55.885  62.571  64.563  1.000 47.828  ? 215 LYS HHH CA  1 
ATOM   3135  C C   . LYS B 2 215 ? 55.657  62.175  66.011  1.000 44.918  ? 215 LYS HHH C   1 
ATOM   3136  O O   . LYS B 2 215 ? 54.521  61.861  66.360  1.000 48.398  ? 215 LYS HHH O   1 
ATOM   3137  C CB  . LYS B 2 215 ? 55.166  63.889  64.289  1.000 53.298  ? 215 LYS HHH CB  1 
ATOM   3138  C CG  . LYS B 2 215 ? 55.830  65.087  64.934  1.000 59.613  ? 215 LYS HHH CG  1 
ATOM   3139  C CD  . LYS B 2 215 ? 57.289  65.244  64.533  1.000 65.957  ? 215 LYS HHH CD  1 
ATOM   3140  C CE  . LYS B 2 215 ? 57.917  66.465  65.165  1.000 71.464  ? 215 LYS HHH CE  1 
ATOM   3141  N NZ  . LYS B 2 215 ? 58.924  67.087  64.278  1.000 74.596  ? 215 LYS HHH NZ  1 
ATOM   3142  N N   . LYS B 2 216 ? 56.714  62.188  66.809  1.000 47.086  ? 216 LYS HHH N   1 
ATOM   3143  C CA  . LYS B 2 216 ? 56.658  61.839  68.241  1.000 50.071  ? 216 LYS HHH CA  1 
ATOM   3144  C C   . LYS B 2 216 ? 56.269  63.094  69.015  1.000 52.488  ? 216 LYS HHH C   1 
ATOM   3145  O O   . LYS B 2 216 ? 56.904  64.151  68.843  1.000 57.922  ? 216 LYS HHH O   1 
ATOM   3146  C CB  . LYS B 2 216 ? 57.997  61.290  68.722  1.000 55.825  ? 216 LYS HHH CB  1 
ATOM   3147  C CG  . LYS B 2 216 ? 57.998  60.926  70.194  1.000 61.075  ? 216 LYS HHH CG  1 
ATOM   3148  C CD  . LYS B 2 216 ? 59.235  60.196  70.630  1.000 67.315  ? 216 LYS HHH CD  1 
ATOM   3149  C CE  . LYS B 2 216 ? 59.089  59.694  72.049  1.000 70.930  ? 216 LYS HHH CE  1 
ATOM   3150  N NZ  . LYS B 2 216 ? 60.254  58.885  72.464  1.000 72.739  ? 216 LYS HHH NZ  1 
ATOM   3151  N N   . VAL B 2 217 ? 55.229  62.977  69.820  1.000 50.487  ? 217 VAL HHH N   1 
ATOM   3152  C CA  . VAL B 2 217 ? 54.735  64.069  70.690  1.000 47.624  ? 217 VAL HHH CA  1 
ATOM   3153  C C   . VAL B 2 217 ? 55.140  63.693  72.107  1.000 50.202  ? 217 VAL HHH C   1 
ATOM   3154  O O   . VAL B 2 217 ? 54.685  62.642  72.580  1.000 48.174  ? 217 VAL HHH O   1 
ATOM   3155  C CB  . VAL B 2 217 ? 53.214  64.201  70.541  1.000 47.203  ? 217 VAL HHH CB  1 
ATOM   3156  C CG1 . VAL B 2 217 ? 52.662  65.324  71.396  1.000 50.664  ? 217 VAL HHH CG1 1 
ATOM   3157  C CG2 . VAL B 2 217 ? 52.801  64.373  69.087  1.000 46.437  ? 217 VAL HHH CG2 1 
ATOM   3158  N N   . GLU B 2 218 ? 56.000  64.485  72.743  1.000 58.488  ? 218 GLU HHH N   1 
ATOM   3159  C CA  . GLU B 2 218 ? 56.411  64.239  74.157  1.000 65.917  ? 218 GLU HHH CA  1 
ATOM   3160  C C   . GLU B 2 218 ? 56.440  65.559  74.915  1.000 66.515  ? 218 GLU HHH C   1 
ATOM   3161  O O   . GLU B 2 218 ? 56.528  66.622  74.299  1.000 62.529  ? 218 GLU HHH O   1 
ATOM   3162  C CB  . GLU B 2 218 ? 57.748  63.489  74.226  1.000 69.134  ? 218 GLU HHH CB  1 
ATOM   3163  C CG  . GLU B 2 218 ? 58.922  64.225  73.602  1.000 69.656  ? 218 GLU HHH CG  1 
ATOM   3164  C CD  . GLU B 2 218 ? 60.162  63.377  73.379  1.000 72.034  ? 218 GLU HHH CD  1 
ATOM   3165  O OE1 . GLU B 2 218 ? 60.254  62.284  73.996  1.000 70.596  ? 218 GLU HHH OE1 1 
ATOM   3166  O OE2 . GLU B 2 218 ? 61.024  63.800  72.571  1.000 72.408  ? 218 GLU HHH OE2 1 
ATOM   3167  N N   . PRO B 2 219 ? 56.369  65.512  76.269  1.000 69.713  ? 219 PRO HHH N   1 
ATOM   3168  C CA  . PRO B 2 219 ? 56.336  66.725  77.089  1.000 73.546  ? 219 PRO HHH CA  1 
ATOM   3169  C C   . PRO B 2 219 ? 57.591  67.572  76.833  1.000 77.368  ? 219 PRO HHH C   1 
ATOM   3170  O O   . PRO B 2 219 ? 58.666  67.012  76.827  1.000 68.143  ? 219 PRO HHH O   1 
ATOM   3171  C CB  . PRO B 2 219 ? 56.298  66.233  78.547  1.000 68.653  ? 219 PRO HHH CB  1 
ATOM   3172  C CG  . PRO B 2 219 ? 55.867  64.781  78.434  1.000 69.740  ? 219 PRO HHH CG  1 
ATOM   3173  C CD  . PRO B 2 219 ? 56.366  64.289  77.089  1.000 66.273  ? 219 PRO HHH CD  1 
ATOM   3174  N N   . LYS B 2 220 ? 57.413  68.871  76.582  1.000 89.728  ? 220 LYS HHH N   1 
ATOM   3175  C CA  . LYS B 2 220 ? 58.489  69.764  76.077  1.000 102.417 ? 220 LYS HHH CA  1 
ATOM   3176  C C   . LYS B 2 220 ? 59.579  69.862  77.157  1.000 113.054 ? 220 LYS HHH C   1 
ATOM   3177  O O   . LYS B 2 220 ? 59.210  69.932  78.343  1.000 114.162 ? 220 LYS HHH O   1 
ATOM   3178  C CB  . LYS B 2 220 ? 57.900  71.127  75.694  1.000 100.951 ? 220 LYS HHH CB  1 
ATOM   3179  C CG  . LYS B 2 220 ? 58.738  71.961  74.734  1.000 104.177 ? 220 LYS HHH CG  1 
ATOM   3180  C CD  . LYS B 2 220 ? 58.307  73.422  74.687  1.000 110.617 ? 220 LYS HHH CD  1 
ATOM   3181  C CE  . LYS B 2 220 ? 59.056  74.253  73.661  1.000 110.483 ? 220 LYS HHH CE  1 
ATOM   3182  N NZ  . LYS B 2 220 ? 58.609  73.970  72.275  1.000 111.646 ? 220 LYS HHH NZ  1 
ATOM   3183  N N   . SER B 2 221 ? 60.864  69.800  76.771  1.000 122.958 ? 221 SER HHH N   1 
ATOM   3184  C CA  . SER B 2 221 ? 62.035  70.093  77.648  1.000 120.798 ? 221 SER HHH CA  1 
ATOM   3185  C C   . SER B 2 221 ? 61.851  71.495  78.244  1.000 141.850 ? 221 SER HHH C   1 
ATOM   3186  O O   . SER B 2 221 ? 61.743  71.609  79.481  1.000 132.417 ? 221 SER HHH O   1 
ATOM   3187  C CB  . SER B 2 221 ? 63.347  69.996  76.897  1.000 108.535 ? 221 SER HHH CB  1 
ATOM   3188  O OG  . SER B 2 221 ? 63.766  68.649  76.775  1.000 98.757  ? 221 SER HHH OG  1 
ATOM   3189  N N   . CYS B 2 222 ? 61.789  72.498  77.354  1.000 169.308 ? 222 CYS HHH N   1 
ATOM   3190  C CA  . CYS B 2 222 ? 61.495  73.945  77.589  1.000 170.805 ? 222 CYS HHH CA  1 
ATOM   3191  C C   . CYS B 2 222 ? 62.542  74.560  78.525  1.000 160.219 ? 222 CYS HHH C   1 
ATOM   3192  O O   . CYS B 2 222 ? 63.552  73.943  78.862  1.000 154.125 ? 222 CYS HHH O   1 
ATOM   3193  C CB  . CYS B 2 222 ? 60.066  74.175  78.083  1.000 172.770 ? 222 CYS HHH CB  1 
ATOM   3194  S SG  . CYS B 2 222 ? 59.871  74.331  79.880  1.000 161.069 ? 222 CYS HHH SG  1 
ATOM   3195  O OXT . CYS B 2 222 ? 62.379  75.706  78.936  1.000 138.438 ? 222 CYS HHH OXT 1 
ATOM   3196  N N   . ASP C 3 1   ? 8.277   77.696  38.348  1.000 95.829  ? 1   ASP LLL N   1 
ATOM   3197  C CA  . ASP C 3 1   ? 9.525   77.600  39.157  1.000 86.922  ? 1   ASP LLL CA  1 
ATOM   3198  C C   . ASP C 3 1   ? 9.134   77.631  40.640  1.000 78.785  ? 1   ASP LLL C   1 
ATOM   3199  O O   . ASP C 3 1   ? 8.971   78.740  41.201  1.000 76.429  ? 1   ASP LLL O   1 
ATOM   3200  C CB  . ASP C 3 1   ? 10.537  78.675  38.752  1.000 89.953  ? 1   ASP LLL CB  1 
ATOM   3201  C CG  . ASP C 3 1   ? 11.953  78.138  38.614  1.000 90.738  ? 1   ASP LLL CG  1 
ATOM   3202  O OD1 . ASP C 3 1   ? 12.409  77.980  37.459  1.000 85.856  ? 1   ASP LLL OD1 1 
ATOM   3203  O OD2 . ASP C 3 1   ? 12.595  77.909  39.663  1.000 86.879  ? 1   ASP LLL OD2 1 
ATOM   3204  N N   . ILE C 3 2   ? 8.995   76.438  41.221  1.000 71.760  ? 2   ILE LLL N   1 
ATOM   3205  C CA  . ILE C 3 2   ? 8.574   76.197  42.628  1.000 64.707  ? 2   ILE LLL CA  1 
ATOM   3206  C C   . ILE C 3 2   ? 9.790   76.354  43.530  1.000 62.239  ? 2   ILE LLL C   1 
ATOM   3207  O O   . ILE C 3 2   ? 10.888  75.962  43.141  1.000 72.997  ? 2   ILE LLL O   1 
ATOM   3208  C CB  . ILE C 3 2   ? 7.952   74.804  42.811  1.000 62.595  ? 2   ILE LLL CB  1 
ATOM   3209  C CG1 . ILE C 3 2   ? 6.804   74.587  41.826  1.000 63.573  ? 2   ILE LLL CG1 1 
ATOM   3210  C CG2 . ILE C 3 2   ? 7.539   74.589  44.265  1.000 62.290  ? 2   ILE LLL CG2 1 
ATOM   3211  C CD1 . ILE C 3 2   ? 6.141   73.235  41.924  1.000 66.372  ? 2   ILE LLL CD1 1 
ATOM   3212  N N   . GLN C 3 3   ? 9.559   76.874  44.718  1.000 57.173  ? 3   GLN LLL N   1 
ATOM   3213  C CA  . GLN C 3 3   ? 10.600  77.162  45.711  1.000 59.235  ? 3   GLN LLL CA  1 
ATOM   3214  C C   . GLN C 3 3   ? 10.106  76.526  47.009  1.000 55.083  ? 3   GLN LLL C   1 
ATOM   3215  O O   . GLN C 3 3   ? 8.901   76.555  47.257  1.000 58.853  ? 3   GLN LLL O   1 
ATOM   3216  C CB  . GLN C 3 3   ? 10.794  78.676  45.714  1.000 65.739  ? 3   GLN LLL CB  1 
ATOM   3217  C CG  . GLN C 3 3   ? 11.788  79.183  46.741  1.000 78.474  ? 3   GLN LLL CG  1 
ATOM   3218  C CD  . GLN C 3 3   ? 11.610  80.671  46.919  1.000 90.238  ? 3   GLN LLL CD  1 
ATOM   3219  O OE1 . GLN C 3 3   ? 10.490  81.162  47.081  1.000 88.512  ? 3   GLN LLL OE1 1 
ATOM   3220  N NE2 . GLN C 3 3   ? 12.714  81.401  46.859  1.000 97.850  ? 3   GLN LLL NE2 1 
ATOM   3221  N N   . LEU C 3 4   ? 10.987  75.898  47.772  1.000 53.091  ? 4   LEU LLL N   1 
ATOM   3222  C CA  . LEU C 3 4   ? 10.629  75.279  49.069  1.000 51.738  ? 4   LEU LLL CA  1 
ATOM   3223  C C   . LEU C 3 4   ? 11.358  76.037  50.166  1.000 53.139  ? 4   LEU LLL C   1 
ATOM   3224  O O   . LEU C 3 4   ? 12.512  76.419  49.931  1.000 64.634  ? 4   LEU LLL O   1 
ATOM   3225  C CB  . LEU C 3 4   ? 11.057  73.810  49.065  1.000 52.139  ? 4   LEU LLL CB  1 
ATOM   3226  C CG  . LEU C 3 4   ? 10.493  72.945  47.945  1.000 50.003  ? 4   LEU LLL CG  1 
ATOM   3227  C CD1 . LEU C 3 4   ? 10.992  71.533  48.090  1.000 50.073  ? 4   LEU LLL CD1 1 
ATOM   3228  C CD2 . LEU C 3 4   ? 8.983   72.969  47.950  1.000 50.598  ? 4   LEU LLL CD2 1 
ATOM   3229  N N   . THR C 3 5   ? 10.709  76.250  51.306  1.000 54.637  ? 5   THR LLL N   1 
ATOM   3230  C CA  . THR C 3 5   ? 11.361  76.759  52.538  1.000 55.803  ? 5   THR LLL CA  1 
ATOM   3231  C C   . THR C 3 5   ? 11.128  75.747  53.654  1.000 54.081  ? 5   THR LLL C   1 
ATOM   3232  O O   . THR C 3 5   ? 9.954   75.490  53.999  1.000 58.881  ? 5   THR LLL O   1 
ATOM   3233  C CB  . THR C 3 5   ? 10.864  78.154  52.934  1.000 58.187  ? 5   THR LLL CB  1 
ATOM   3234  O OG1 . THR C 3 5   ? 10.569  78.866  51.730  1.000 64.753  ? 5   THR LLL OG1 1 
ATOM   3235  C CG2 . THR C 3 5   ? 11.885  78.898  53.770  1.000 56.857  ? 5   THR LLL CG2 1 
ATOM   3236  N N   . GLN C 3 6   ? 12.212  75.183  54.179  1.000 51.814  ? 6   GLN LLL N   1 
ATOM   3237  C CA  . GLN C 3 6   ? 12.171  74.287  55.362  1.000 54.073  ? 6   GLN LLL CA  1 
ATOM   3238  C C   . GLN C 3 6   ? 12.269  75.132  56.625  1.000 55.754  ? 6   GLN LLL C   1 
ATOM   3239  O O   . GLN C 3 6   ? 12.746  76.275  56.532  1.000 61.525  ? 6   GLN LLL O   1 
ATOM   3240  C CB  . GLN C 3 6   ? 13.328  73.294  55.374  1.000 53.085  ? 6   GLN LLL CB  1 
ATOM   3241  C CG  . GLN C 3 6   ? 13.064  72.047  54.557  1.000 50.699  ? 6   GLN LLL CG  1 
ATOM   3242  C CD  . GLN C 3 6   ? 14.262  71.151  54.658  1.000 50.188  ? 6   GLN LLL CD  1 
ATOM   3243  O OE1 . GLN C 3 6   ? 15.091  71.129  53.763  1.000 58.499  ? 6   GLN LLL OE1 1 
ATOM   3244  N NE2 . GLN C 3 6   ? 14.396  70.473  55.782  1.000 44.654  ? 6   GLN LLL NE2 1 
ATOM   3245  N N   . SER C 3 7   ? 11.840  74.568  57.749  1.000 56.153  ? 7   SER LLL N   1 
ATOM   3246  C CA  . SER C 3 7   ? 11.974  75.174  59.094  1.000 56.471  ? 7   SER LLL CA  1 
ATOM   3247  C C   . SER C 3 7   ? 11.770  74.091  60.143  1.000 52.227  ? 7   SER LLL C   1 
ATOM   3248  O O   . SER C 3 7   ? 10.993  73.162  59.937  1.000 53.458  ? 7   SER LLL O   1 
ATOM   3249  C CB  . SER C 3 7   ? 10.994  76.295  59.280  1.000 60.930  ? 7   SER LLL CB  1 
ATOM   3250  O OG  . SER C 3 7   ? 9.671   75.795  59.175  1.000 68.313  ? 7   SER LLL OG  1 
ATOM   3251  N N   . PRO C 3 8   ? 12.482  74.151  61.284  1.000 53.750  ? 8   PRO LLL N   1 
ATOM   3252  C CA  . PRO C 3 8   ? 13.589  75.091  61.469  1.000 61.529  ? 8   PRO LLL CA  1 
ATOM   3253  C C   . PRO C 3 8   ? 14.877  74.702  60.716  1.000 68.293  ? 8   PRO LLL C   1 
ATOM   3254  O O   . PRO C 3 8   ? 14.913  73.660  60.099  1.000 72.093  ? 8   PRO LLL O   1 
ATOM   3255  C CB  . PRO C 3 8   ? 13.802  75.049  62.991  1.000 61.575  ? 8   PRO LLL CB  1 
ATOM   3256  C CG  . PRO C 3 8   ? 13.361  73.656  63.401  1.000 57.881  ? 8   PRO LLL CG  1 
ATOM   3257  C CD  . PRO C 3 8   ? 12.206  73.344  62.480  1.000 56.259  ? 8   PRO LLL CD  1 
ATOM   3258  N N   . ASP C 3 9   ? 15.907  75.553  60.772  1.000 72.251  ? 9   ASP LLL N   1 
ATOM   3259  C CA  . ASP C 3 9   ? 17.245  75.262  60.192  1.000 71.179  ? 9   ASP LLL CA  1 
ATOM   3260  C C   . ASP C 3 9   ? 17.924  74.193  61.050  1.000 68.392  ? 9   ASP LLL C   1 
ATOM   3261  O O   . ASP C 3 9   ? 18.516  73.255  60.496  1.000 74.779  ? 9   ASP LLL O   1 
ATOM   3262  C CB  . ASP C 3 9   ? 18.119  76.518  60.135  1.000 72.791  ? 9   ASP LLL CB  1 
ATOM   3263  C CG  . ASP C 3 9   ? 17.544  77.640  59.286  1.000 74.543  ? 9   ASP LLL CG  1 
ATOM   3264  O OD1 . ASP C 3 9   ? 17.348  78.738  59.836  1.000 77.148  ? 9   ASP LLL OD1 1 
ATOM   3265  O OD2 . ASP C 3 9   ? 17.313  77.414  58.082  1.000 65.765  ? 9   ASP LLL OD2 1 
ATOM   3266  N N   . SER C 3 10  ? 17.825  74.364  62.364  1.000 65.406  ? 10  SER LLL N   1 
ATOM   3267  C CA  . SER C 3 10  ? 18.520  73.588  63.414  1.000 66.744  ? 10  SER LLL CA  1 
ATOM   3268  C C   . SER C 3 10  ? 17.466  72.992  64.345  1.000 63.146  ? 10  SER LLL C   1 
ATOM   3269  O O   . SER C 3 10  ? 16.449  73.634  64.568  1.000 66.275  ? 10  SER LLL O   1 
ATOM   3270  C CB  . SER C 3 10  ? 19.477  74.507  64.137  1.000 72.988  ? 10  SER LLL CB  1 
ATOM   3271  O OG  . SER C 3 10  ? 19.878  73.995  65.400  1.000 84.094  ? 10  SER LLL OG  1 
ATOM   3272  N N   . LEU C 3 11  ? 17.707  71.814  64.896  1.000 59.889  ? 11  LEU LLL N   1 
ATOM   3273  C CA  . LEU C 3 11  ? 16.692  71.128  65.727  1.000 56.206  ? 11  LEU LLL CA  1 
ATOM   3274  C C   . LEU C 3 11  ? 17.382  70.134  66.643  1.000 51.957  ? 11  LEU LLL C   1 
ATOM   3275  O O   . LEU C 3 11  ? 18.012  69.227  66.120  1.000 58.601  ? 11  LEU LLL O   1 
ATOM   3276  C CB  . LEU C 3 11  ? 15.737  70.412  64.779  1.000 58.537  ? 11  LEU LLL CB  1 
ATOM   3277  C CG  . LEU C 3 11  ? 14.687  69.547  65.453  1.000 59.457  ? 11  LEU LLL CG  1 
ATOM   3278  C CD1 . LEU C 3 11  ? 13.798  70.409  66.328  1.000 64.338  ? 11  LEU LLL CD1 1 
ATOM   3279  C CD2 . LEU C 3 11  ? 13.865  68.802  64.414  1.000 61.276  ? 11  LEU LLL CD2 1 
ATOM   3280  N N   . ALA C 3 12  ? 17.279  70.320  67.953  1.000 50.622  ? 12  ALA LLL N   1 
ATOM   3281  C CA  . ALA C 3 12  ? 17.947  69.455  68.955  1.000 52.471  ? 12  ALA LLL CA  1 
ATOM   3282  C C   . ALA C 3 12  ? 16.870  68.763  69.780  1.000 50.287  ? 12  ALA LLL C   1 
ATOM   3283  O O   . ALA C 3 12  ? 15.945  69.447  70.236  1.000 57.588  ? 12  ALA LLL O   1 
ATOM   3284  C CB  . ALA C 3 12  ? 18.876  70.259  69.832  1.000 55.627  ? 12  ALA LLL CB  1 
ATOM   3285  N N   . VAL C 3 13  ? 16.997  67.455  69.950  1.000 46.476  ? 13  VAL LLL N   1 
ATOM   3286  C CA  . VAL C 3 13  ? 15.909  66.587  70.470  1.000 47.086  ? 13  VAL LLL CA  1 
ATOM   3287  C C   . VAL C 3 13  ? 16.519  65.465  71.300  1.000 51.092  ? 13  VAL LLL C   1 
ATOM   3288  O O   . VAL C 3 13  ? 17.442  64.809  70.792  1.000 56.837  ? 13  VAL LLL O   1 
ATOM   3289  C CB  . VAL C 3 13  ? 15.112  66.002  69.301  1.000 42.815  ? 13  VAL LLL CB  1 
ATOM   3290  C CG1 . VAL C 3 13  ? 14.179  64.904  69.766  1.000 43.732  ? 13  VAL LLL CG1 1 
ATOM   3291  C CG2 . VAL C 3 13  ? 14.362  67.085  68.557  1.000 42.581  ? 13  VAL LLL CG2 1 
ATOM   3292  N N   . SER C 3 14  ? 15.998  65.243  72.509  1.000 52.762  ? 14  SER LLL N   1 
ATOM   3293  C CA  . SER C 3 14  ? 16.497  64.215  73.458  1.000 54.638  ? 14  SER LLL CA  1 
ATOM   3294  C C   . SER C 3 14  ? 16.275  62.832  72.846  1.000 52.788  ? 14  SER LLL C   1 
ATOM   3295  O O   . SER C 3 14  ? 15.458  62.725  71.921  1.000 47.979  ? 14  SER LLL O   1 
ATOM   3296  C CB  . SER C 3 14  ? 15.845  64.362  74.797  1.000 58.960  ? 14  SER LLL CB  1 
ATOM   3297  O OG  . SER C 3 14  ? 15.913  65.713  75.243  1.000 66.250  ? 14  SER LLL OG  1 
ATOM   3298  N N   . LEU C 3 15  ? 17.025  61.823  73.281  1.000 56.047  ? 15  LEU LLL N   1 
ATOM   3299  C CA  . LEU C 3 15  ? 16.875  60.455  72.723  1.000 60.059  ? 15  LEU LLL CA  1 
ATOM   3300  C C   . LEU C 3 15  ? 15.469  59.951  73.051  1.000 58.885  ? 15  LEU LLL C   1 
ATOM   3301  O O   . LEU C 3 15  ? 15.023  60.084  74.204  1.000 50.880  ? 15  LEU LLL O   1 
ATOM   3302  C CB  . LEU C 3 15  ? 17.938  59.520  73.299  1.000 63.789  ? 15  LEU LLL CB  1 
ATOM   3303  C CG  . LEU C 3 15  ? 19.276  59.513  72.572  1.000 63.200  ? 15  LEU LLL CG  1 
ATOM   3304  C CD1 . LEU C 3 15  ? 20.304  58.773  73.412  1.000 66.643  ? 15  LEU LLL CD1 1 
ATOM   3305  C CD2 . LEU C 3 15  ? 19.157  58.854  71.208  1.000 62.721  ? 15  LEU LLL CD2 1 
ATOM   3306  N N   . GLY C 3 16  ? 14.787  59.427  72.041  1.000 62.971  ? 16  GLY LLL N   1 
ATOM   3307  C CA  . GLY C 3 16  ? 13.457  58.823  72.187  1.000 62.893  ? 16  GLY LLL CA  1 
ATOM   3308  C C   . GLY C 3 16  ? 12.341  59.844  72.148  1.000 59.442  ? 16  GLY LLL C   1 
ATOM   3309  O O   . GLY C 3 16  ? 11.207  59.432  72.413  1.000 68.901  ? 16  GLY LLL O   1 
ATOM   3310  N N   . GLU C 3 17  ? 12.632  61.113  71.849  1.000 58.633  ? 17  GLU LLL N   1 
ATOM   3311  C CA  . GLU C 3 17  ? 11.611  62.195  71.757  1.000 65.348  ? 17  GLU LLL CA  1 
ATOM   3312  C C   . GLU C 3 17  ? 11.208  62.384  70.293  1.000 59.962  ? 17  GLU LLL C   1 
ATOM   3313  O O   . GLU C 3 17  ? 11.779  61.714  69.430  1.000 54.988  ? 17  GLU LLL O   1 
ATOM   3314  C CB  . GLU C 3 17  ? 12.120  63.521  72.339  1.000 77.573  ? 17  GLU LLL CB  1 
ATOM   3315  C CG  . GLU C 3 17  ? 12.309  63.519  73.849  1.000 83.875  ? 17  GLU LLL CG  1 
ATOM   3316  C CD  . GLU C 3 17  ? 11.106  63.080  74.672  1.000 87.677  ? 17  GLU LLL CD  1 
ATOM   3317  O OE1 . GLU C 3 17  ? 10.228  63.927  74.965  1.000 93.325  ? 17  GLU LLL OE1 1 
ATOM   3318  O OE2 . GLU C 3 17  ? 11.056  61.884  75.019  1.000 89.711  ? 17  GLU LLL OE2 1 
ATOM   3319  N N   . ARG C 3 18  ? 10.259  63.288  70.057  1.000 64.761  ? 18  ARG LLL N   1 
ATOM   3320  C CA  . ARG C 3 18  ? 9.652   63.584  68.737  1.000 71.194  ? 18  ARG LLL CA  1 
ATOM   3321  C C   . ARG C 3 18  ? 10.426  64.733  68.090  1.000 63.417  ? 18  ARG LLL C   1 
ATOM   3322  O O   . ARG C 3 18  ? 10.678  65.738  68.769  1.000 63.786  ? 18  ARG LLL O   1 
ATOM   3323  C CB  . ARG C 3 18  ? 8.153   63.874  68.923  1.000 86.303  ? 18  ARG LLL CB  1 
ATOM   3324  C CG  . ARG C 3 18  ? 7.600   65.141  68.267  1.000 93.745  ? 18  ARG LLL CG  1 
ATOM   3325  C CD  . ARG C 3 18  ? 6.105   65.288  68.557  1.000 94.626  ? 18  ARG LLL CD  1 
ATOM   3326  N NE  . ARG C 3 18  ? 5.499   63.958  68.530  1.000 102.629 ? 18  ARG LLL NE  1 
ATOM   3327  C CZ  . ARG C 3 18  ? 4.972   63.362  67.455  1.000 103.508 ? 18  ARG LLL CZ  1 
ATOM   3328  N NH1 . ARG C 3 18  ? 4.891   64.000  66.298  1.000 110.833 ? 18  ARG LLL NH1 1 
ATOM   3329  N NH2 . ARG C 3 18  ? 4.495   62.132  67.553  1.000 95.691  ? 18  ARG LLL NH2 1 
ATOM   3330  N N   . ALA C 3 19  ? 10.780  64.573  66.819  1.000 58.669  ? 19  ALA LLL N   1 
ATOM   3331  C CA  . ALA C 3 19  ? 11.344  65.634  65.958  1.000 54.583  ? 19  ALA LLL CA  1 
ATOM   3332  C C   . ALA C 3 19  ? 10.385  65.862  64.797  1.000 47.051  ? 19  ALA LLL C   1 
ATOM   3333  O O   . ALA C 3 19  ? 10.014  64.876  64.138  1.000 42.190  ? 19  ALA LLL O   1 
ATOM   3334  C CB  . ALA C 3 19  ? 12.707  65.220  65.460  1.000 60.327  ? 19  ALA LLL CB  1 
ATOM   3335  N N   . THR C 3 20  ? 10.033  67.120  64.553  1.000 45.177  ? 20  THR LLL N   1 
ATOM   3336  C CA  . THR C 3 20  ? 9.132   67.538  63.451  1.000 48.342  ? 20  THR LLL CA  1 
ATOM   3337  C C   . THR C 3 20  ? 9.866   68.594  62.625  1.000 45.839  ? 20  THR LLL C   1 
ATOM   3338  O O   . THR C 3 20  ? 10.439  69.523  63.225  1.000 47.459  ? 20  THR LLL O   1 
ATOM   3339  C CB  . THR C 3 20  ? 7.773   68.004  63.997  1.000 51.575  ? 20  THR LLL CB  1 
ATOM   3340  O OG1 . THR C 3 20  ? 8.051   68.686  65.218  1.000 60.015  ? 20  THR LLL OG1 1 
ATOM   3341  C CG2 . THR C 3 20  ? 6.799   66.875  64.269  1.000 52.171  ? 20  THR LLL CG2 1 
ATOM   3342  N N   . ILE C 3 21  ? 9.853   68.425  61.303  1.000 43.711  ? 21  ILE LLL N   1 
ATOM   3343  C CA  . ILE C 3 21  ? 10.470  69.345  60.307  1.000 43.033  ? 21  ILE LLL CA  1 
ATOM   3344  C C   . ILE C 3 21  ? 9.368   69.779  59.347  1.000 41.402  ? 21  ILE LLL C   1 
ATOM   3345  O O   . ILE C 3 21  ? 8.629   68.887  58.892  1.000 40.679  ? 21  ILE LLL O   1 
ATOM   3346  C CB  . ILE C 3 21  ? 11.633  68.632  59.582  1.000 46.575  ? 21  ILE LLL CB  1 
ATOM   3347  C CG1 . ILE C 3 21  ? 12.613  68.018  60.588  1.000 51.785  ? 21  ILE LLL CG1 1 
ATOM   3348  C CG2 . ILE C 3 21  ? 12.337  69.578  58.623  1.000 46.890  ? 21  ILE LLL CG2 1 
ATOM   3349  C CD1 . ILE C 3 21  ? 13.705  67.174  59.986  1.000 52.894  ? 21  ILE LLL CD1 1 
ATOM   3350  N N   . ASN C 3 22  ? 9.297   71.074  59.027  1.000 44.099  ? 22  ASN LLL N   1 
ATOM   3351  C CA  . ASN C 3 22  ? 8.240   71.670  58.160  1.000 52.504  ? 22  ASN LLL CA  1 
ATOM   3352  C C   . ASN C 3 22  ? 8.824   72.103  56.807  1.000 53.477  ? 22  ASN LLL C   1 
ATOM   3353  O O   . ASN C 3 22  ? 9.891   72.752  56.811  1.000 53.301  ? 22  ASN LLL O   1 
ATOM   3354  C CB  . ASN C 3 22  ? 7.548   72.850  58.852  1.000 55.345  ? 22  ASN LLL CB  1 
ATOM   3355  C CG  . ASN C 3 22  ? 6.691   72.412  60.015  1.000 60.196  ? 22  ASN LLL CG  1 
ATOM   3356  O OD1 . ASN C 3 22  ? 5.977   71.419  59.925  1.000 68.484  ? 22  ASN LLL OD1 1 
ATOM   3357  N ND2 . ASN C 3 22  ? 6.763   73.134  61.119  1.000 67.425  ? 22  ASN LLL ND2 1 
ATOM   3358  N N   . CYS C 3 23  ? 8.121   71.778  55.712  1.000 54.207  ? 23  CYS LLL N   1 
ATOM   3359  C CA  . CYS C 3 23  ? 8.386   72.237  54.321  1.000 58.573  ? 23  CYS LLL CA  1 
ATOM   3360  C C   . CYS C 3 23  ? 7.188   73.065  53.845  1.000 58.868  ? 23  CYS LLL C   1 
ATOM   3361  O O   . CYS C 3 23  ? 6.052   72.549  53.870  1.000 61.591  ? 23  CYS LLL O   1 
ATOM   3362  C CB  . CYS C 3 23  ? 8.634   71.050  53.389  1.000 67.691  ? 23  CYS LLL CB  1 
ATOM   3363  S SG  . CYS C 3 23  ? 9.415   71.470  51.800  1.000 84.178  ? 23  CYS LLL SG  1 
ATOM   3364  N N   . LYS C 3 24  ? 7.437   74.312  53.458  1.000 60.272  ? 24  LYS LLL N   1 
ATOM   3365  C CA  . LYS C 3 24  ? 6.437   75.235  52.864  1.000 64.123  ? 24  LYS LLL CA  1 
ATOM   3366  C C   . LYS C 3 24  ? 6.784   75.389  51.386  1.000 59.802  ? 24  LYS LLL C   1 
ATOM   3367  O O   . LYS C 3 24  ? 7.907   75.861  51.105  1.000 64.964  ? 24  LYS LLL O   1 
ATOM   3368  C CB  . LYS C 3 24  ? 6.510   76.595  53.564  1.000 73.264  ? 24  LYS LLL CB  1 
ATOM   3369  C CG  . LYS C 3 24  ? 5.187   77.282  53.872  1.000 79.586  ? 24  LYS LLL CG  1 
ATOM   3370  C CD  . LYS C 3 24  ? 5.341   78.492  54.806  1.000 80.971  ? 24  LYS LLL CD  1 
ATOM   3371  C CE  . LYS C 3 24  ? 4.494   78.423  56.065  1.000 83.515  ? 24  LYS LLL CE  1 
ATOM   3372  N NZ  . LYS C 3 24  ? 3.042   78.368  55.762  1.000 89.576  ? 24  LYS LLL NZ  1 
ATOM   3373  N N   . SER C 3 25  ? 5.896   74.973  50.482  1.000 57.018  ? 25  SER LLL N   1 
ATOM   3374  C CA  . SER C 3 25  ? 6.086   75.118  49.016  1.000 58.575  ? 25  SER LLL CA  1 
ATOM   3375  C C   . SER C 3 25  ? 5.427   76.419  48.566  1.000 61.171  ? 25  SER LLL C   1 
ATOM   3376  O O   . SER C 3 25  ? 4.326   76.725  49.065  1.000 66.972  ? 25  SER LLL O   1 
ATOM   3377  C CB  . SER C 3 25  ? 5.569   73.928  48.246  1.000 59.632  ? 25  SER LLL CB  1 
ATOM   3378  O OG  . SER C 3 25  ? 4.208   73.677  48.526  1.000 57.966  ? 25  SER LLL OG  1 
ATOM   3379  N N   . SER C 3 26  ? 6.075   77.142  47.649  1.000 66.056  ? 26  SER LLL N   1 
ATOM   3380  C CA  . SER C 3 26  ? 5.587   78.433  47.098  1.000 67.906  ? 26  SER LLL CA  1 
ATOM   3381  C C   . SER C 3 26  ? 4.328   78.189  46.267  1.000 62.890  ? 26  SER LLL C   1 
ATOM   3382  O O   . SER C 3 26  ? 3.712   79.167  45.853  1.000 74.270  ? 26  SER LLL O   1 
ATOM   3383  C CB  . SER C 3 26  ? 6.648   79.137  46.279  1.000 71.083  ? 26  SER LLL CB  1 
ATOM   3384  O OG  . SER C 3 26  ? 6.904   78.440  45.064  1.000 73.636  ? 26  SER LLL OG  1 
ATOM   3385  N N   . GLN C 3 27  ? 3.948   76.937  46.042  1.000 58.146  ? 27  GLN LLL N   1 
ATOM   3386  C CA  . GLN C 3 27  ? 2.854   76.595  45.108  1.000 62.233  ? 27  GLN LLL CA  1 
ATOM   3387  C C   . GLN C 3 27  ? 2.431   75.146  45.360  1.000 66.636  ? 27  GLN LLL C   1 
ATOM   3388  O O   . GLN C 3 27  ? 3.232   74.398  45.923  1.000 81.365  ? 27  GLN LLL O   1 
ATOM   3389  C CB  . GLN C 3 27  ? 3.397   76.887  43.712  1.000 60.312  ? 27  GLN LLL CB  1 
ATOM   3390  C CG  . GLN C 3 27  ? 2.589   76.320  42.567  1.000 64.428  ? 27  GLN LLL CG  1 
ATOM   3391  C CD  . GLN C 3 27  ? 3.379   76.482  41.293  1.000 68.708  ? 27  GLN LLL CD  1 
ATOM   3392  O OE1 . GLN C 3 27  ? 4.213   77.391  41.175  1.000 66.218  ? 27  GLN LLL OE1 1 
ATOM   3393  N NE2 . GLN C 3 27  ? 3.146   75.568  40.356  1.000 70.347  ? 27  GLN LLL NE2 1 
ATOM   3394  N N   . SER C 3 28  ? 1.211   74.770  44.980  1.000 70.352  ? 28  SER LLL N   1 
ATOM   3395  C CA  . SER C 3 28  ? 0.683   73.395  45.162  1.000 71.876  ? 28  SER LLL CA  1 
ATOM   3396  C C   . SER C 3 28  ? 1.440   72.442  44.233  1.000 70.959  ? 28  SER LLL C   1 
ATOM   3397  O O   . SER C 3 28  ? 1.937   72.888  43.171  1.000 62.364  ? 28  SER LLL O   1 
ATOM   3398  C CB  . SER C 3 28  ? -0.805  73.301  44.937  1.000 80.919  ? 28  SER LLL CB  1 
ATOM   3399  O OG  . SER C 3 28  ? -1.240  71.949  45.045  1.000 87.302  ? 28  SER LLL OG  1 
ATOM   3400  N N   . VAL C 3 29  ? 1.495   71.173  44.640  1.000 73.723  ? 29  VAL LLL N   1 
ATOM   3401  C CA  . VAL C 3 29  ? 2.313   70.089  44.028  1.000 72.581  ? 29  VAL LLL CA  1 
ATOM   3402  C C   . VAL C 3 29  ? 1.433   68.844  43.924  1.000 77.864  ? 29  VAL LLL C   1 
ATOM   3403  O O   . VAL C 3 29  ? 1.964   67.730  44.024  1.000 82.584  ? 29  VAL LLL O   1 
ATOM   3404  C CB  . VAL C 3 29  ? 3.576   69.831  44.872  1.000 73.700  ? 29  VAL LLL CB  1 
ATOM   3405  C CG1 . VAL C 3 29  ? 4.530   71.012  44.820  1.000 72.282  ? 29  VAL LLL CG1 1 
ATOM   3406  C CG2 . VAL C 3 29  ? 3.244   69.487  46.316  1.000 70.795  ? 29  VAL LLL CG2 1 
ATOM   3407  N N   . LEU C 3 30  ? 0.130   69.056  43.743  1.000 83.629  ? 30  LEU LLL N   1 
ATOM   3408  C CA  . LEU C 3 30  ? -0.908  68.000  43.694  1.000 82.781  ? 30  LEU LLL CA  1 
ATOM   3409  C C   . LEU C 3 30  ? -1.163  67.608  42.228  1.000 85.665  ? 30  LEU LLL C   1 
ATOM   3410  O O   . LEU C 3 30  ? -1.600  68.471  41.448  1.000 90.125  ? 30  LEU LLL O   1 
ATOM   3411  C CB  . LEU C 3 30  ? -2.159  68.559  44.379  1.000 83.830  ? 30  LEU LLL CB  1 
ATOM   3412  C CG  . LEU C 3 30  ? -3.214  67.543  44.812  1.000 91.429  ? 30  LEU LLL CG  1 
ATOM   3413  C CD1 . LEU C 3 30  ? -4.089  67.091  43.640  1.000 94.879  ? 30  LEU LLL CD1 1 
ATOM   3414  C CD2 . LEU C 3 30  ? -2.557  66.363  45.508  1.000 94.454  ? 30  LEU LLL CD2 1 
ATOM   3415  N N   . TYR C 3 31  ? -0.857  66.365  41.847  1.000 91.777  ? 31  TYR LLL N   1 
ATOM   3416  C CA  . TYR C 3 31  ? -1.279  65.770  40.548  1.000 92.759  ? 31  TYR LLL CA  1 
ATOM   3417  C C   . TYR C 3 31  ? -2.749  65.377  40.684  1.000 95.519  ? 31  TYR LLL C   1 
ATOM   3418  O O   . TYR C 3 31  ? -3.117  64.649  41.629  1.000 92.349  ? 31  TYR LLL O   1 
ATOM   3419  C CB  . TYR C 3 31  ? -0.414  64.575  40.129  1.000 99.079  ? 31  TYR LLL CB  1 
ATOM   3420  C CG  . TYR C 3 31  ? 0.689   64.897  39.147  1.000 99.724  ? 31  TYR LLL CG  1 
ATOM   3421  C CD1 . TYR C 3 31  ? 1.693   65.790  39.474  1.000 101.538 ? 31  TYR LLL CD1 1 
ATOM   3422  C CD2 . TYR C 3 31  ? 0.741   64.303  37.894  1.000 96.038  ? 31  TYR LLL CD2 1 
ATOM   3423  C CE1 . TYR C 3 31  ? 2.707   66.098  38.584  1.000 95.841  ? 31  TYR LLL CE1 1 
ATOM   3424  C CE2 . TYR C 3 31  ? 1.739   64.611  36.981  1.000 88.303  ? 31  TYR LLL CE2 1 
ATOM   3425  C CZ  . TYR C 3 31  ? 2.725   65.515  37.329  1.000 90.372  ? 31  TYR LLL CZ  1 
ATOM   3426  O OH  . TYR C 3 31  ? 3.725   65.829  36.459  1.000 82.985  ? 31  TYR LLL OH  1 
ATOM   3427  N N   . SER C 3 32  ? -3.572  65.888  39.779  1.000 102.815 ? 32  SER LLL N   1 
ATOM   3428  C CA  . SER C 3 32  ? -5.040  65.697  39.779  1.000 97.868  ? 32  SER LLL CA  1 
ATOM   3429  C C   . SER C 3 32  ? -5.374  64.222  39.524  1.000 94.801  ? 32  SER LLL C   1 
ATOM   3430  O O   . SER C 3 32  ? -6.173  63.665  40.283  1.000 77.781  ? 32  SER LLL O   1 
ATOM   3431  C CB  . SER C 3 32  ? -5.662  66.595  38.755  1.000 96.131  ? 32  SER LLL CB  1 
ATOM   3432  O OG  . SER C 3 32  ? -6.877  67.110  39.240  1.000 97.968  ? 32  SER LLL OG  1 
ATOM   3433  N N   . SER C 3 33  ? -4.728  63.619  38.518  1.000 104.880 ? 33  SER LLL N   1 
ATOM   3434  C CA  . SER C 3 33  ? -5.033  62.272  37.949  1.000 113.616 ? 33  SER LLL CA  1 
ATOM   3435  C C   . SER C 3 33  ? -4.938  61.176  39.019  1.000 115.611 ? 33  SER LLL C   1 
ATOM   3436  O O   . SER C 3 33  ? -5.848  60.334  39.060  1.000 129.209 ? 33  SER LLL O   1 
ATOM   3437  C CB  . SER C 3 33  ? -4.142  61.966  36.781  1.000 110.884 ? 33  SER LLL CB  1 
ATOM   3438  O OG  . SER C 3 33  ? -2.910  62.644  36.935  1.000 118.550 ? 33  SER LLL OG  1 
ATOM   3439  N N   . ILE C 3 34  ? -3.870  61.163  39.821  1.000 107.898 ? 34  ILE LLL N   1 
ATOM   3440  C CA  . ILE C 3 34  ? -3.787  60.354  41.078  1.000 94.781  ? 34  ILE LLL CA  1 
ATOM   3441  C C   . ILE C 3 34  ? -3.678  61.342  42.240  1.000 81.496  ? 34  ILE LLL C   1 
ATOM   3442  O O   . ILE C 3 34  ? -2.769  62.163  42.205  1.000 91.758  ? 34  ILE LLL O   1 
ATOM   3443  C CB  . ILE C 3 34  ? -2.616  59.348  41.051  1.000 97.559  ? 34  ILE LLL CB  1 
ATOM   3444  C CG1 . ILE C 3 34  ? -1.322  59.984  40.538  1.000 100.323 ? 34  ILE LLL CG1 1 
ATOM   3445  C CG2 . ILE C 3 34  ? -2.980  58.106  40.249  1.000 97.308  ? 34  ILE LLL CG2 1 
ATOM   3446  C CD1 . ILE C 3 34  ? -0.075  59.179  40.837  1.000 105.761 ? 34  ILE LLL CD1 1 
ATOM   3447  N N   . ASN C 3 35  ? -4.591  61.298  43.204  1.000 71.544  ? 35  ASN LLL N   1 
ATOM   3448  C CA  . ASN C 3 35  ? -4.690  62.313  44.293  1.000 73.384  ? 35  ASN LLL CA  1 
ATOM   3449  C C   . ASN C 3 35  ? -3.481  62.155  45.233  1.000 72.860  ? 35  ASN LLL C   1 
ATOM   3450  O O   . ASN C 3 35  ? -3.643  61.547  46.306  1.000 77.861  ? 35  ASN LLL O   1 
ATOM   3451  C CB  . ASN C 3 35  ? -6.029  62.184  45.030  1.000 72.933  ? 35  ASN LLL CB  1 
ATOM   3452  C CG  . ASN C 3 35  ? -6.282  63.284  46.040  1.000 72.169  ? 35  ASN LLL CG  1 
ATOM   3453  O OD1 . ASN C 3 35  ? -6.144  64.462  45.726  1.000 67.563  ? 35  ASN LLL OD1 1 
ATOM   3454  N ND2 . ASN C 3 35  ? -6.684  62.909  47.245  1.000 71.704  ? 35  ASN LLL ND2 1 
ATOM   3455  N N   . LYS C 3 36  ? -2.314  62.690  44.846  1.000 70.386  ? 36  LYS LLL N   1 
ATOM   3456  C CA  . LYS C 3 36  ? -0.995  62.504  45.527  1.000 61.805  ? 36  LYS LLL CA  1 
ATOM   3457  C C   . LYS C 3 36  ? -0.129  63.766  45.403  1.000 57.017  ? 36  LYS LLL C   1 
ATOM   3458  O O   . LYS C 3 36  ? -0.039  64.303  44.270  1.000 44.293  ? 36  LYS LLL O   1 
ATOM   3459  C CB  . LYS C 3 36  ? -0.246  61.321  44.912  1.000 62.891  ? 36  LYS LLL CB  1 
ATOM   3460  C CG  . LYS C 3 36  ? -0.137  60.092  45.809  1.000 69.727  ? 36  LYS LLL CG  1 
ATOM   3461  C CD  . LYS C 3 36  ? -1.310  59.128  45.732  1.000 75.006  ? 36  LYS LLL CD  1 
ATOM   3462  C CE  . LYS C 3 36  ? -0.920  57.702  46.081  1.000 72.096  ? 36  LYS LLL CE  1 
ATOM   3463  N NZ  . LYS C 3 36  ? -0.683  57.550  47.534  1.000 67.658  ? 36  LYS LLL NZ  1 
ATOM   3464  N N   . ASN C 3 37  ? 0.490   64.211  46.507  1.000 56.114  ? 37  ASN LLL N   1 
ATOM   3465  C CA  . ASN C 3 37  ? 1.401   65.391  46.499  1.000 57.188  ? 37  ASN LLL CA  1 
ATOM   3466  C C   . ASN C 3 37  ? 2.816   64.926  46.104  1.000 60.172  ? 37  ASN LLL C   1 
ATOM   3467  O O   . ASN C 3 37  ? 3.288   63.931  46.701  1.000 55.178  ? 37  ASN LLL O   1 
ATOM   3468  C CB  . ASN C 3 37  ? 1.414   66.127  47.841  1.000 55.328  ? 37  ASN LLL CB  1 
ATOM   3469  C CG  . ASN C 3 37  ? 0.173   66.944  48.116  1.000 54.105  ? 37  ASN LLL CG  1 
ATOM   3470  O OD1 . ASN C 3 37  ? -0.011  68.048  47.575  1.000 57.584  ? 37  ASN LLL OD1 1 
ATOM   3471  N ND2 . ASN C 3 37  ? -0.649  66.420  49.006  1.000 48.719  ? 37  ASN LLL ND2 1 
ATOM   3472  N N   . TYR C 3 38  ? 3.464   65.632  45.160  1.000 58.082  ? 38  TYR LLL N   1 
ATOM   3473  C CA  . TYR C 3 38  ? 4.777   65.273  44.544  1.000 54.365  ? 38  TYR LLL CA  1 
ATOM   3474  C C   . TYR C 3 38  ? 5.914   65.952  45.334  1.000 52.283  ? 38  TYR LLL C   1 
ATOM   3475  O O   . TYR C 3 38  ? 6.571   66.886  44.831  1.000 52.545  ? 38  TYR LLL O   1 
ATOM   3476  C CB  . TYR C 3 38  ? 4.769   65.604  43.045  1.000 51.482  ? 38  TYR LLL CB  1 
ATOM   3477  C CG  . TYR C 3 38  ? 4.126   64.527  42.215  1.000 50.354  ? 38  TYR LLL CG  1 
ATOM   3478  C CD1 . TYR C 3 38  ? 4.804   63.885  41.195  1.000 52.433  ? 38  TYR LLL CD1 1 
ATOM   3479  C CD2 . TYR C 3 38  ? 2.856   64.084  42.517  1.000 49.098  ? 38  TYR LLL CD2 1 
ATOM   3480  C CE1 . TYR C 3 38  ? 4.217   62.855  40.475  1.000 52.426  ? 38  TYR LLL CE1 1 
ATOM   3481  C CE2 . TYR C 3 38  ? 2.258   63.052  41.816  1.000 50.013  ? 38  TYR LLL CE2 1 
ATOM   3482  C CZ  . TYR C 3 38  ? 2.935   62.442  40.785  1.000 49.601  ? 38  TYR LLL CZ  1 
ATOM   3483  O OH  . TYR C 3 38  ? 2.314   61.433  40.126  1.000 51.932  ? 38  TYR LLL OH  1 
ATOM   3484  N N   . LEU C 3 39  ? 6.123   65.474  46.562  1.000 48.615  ? 39  LEU LLL N   1 
ATOM   3485  C CA  . LEU C 3 39  ? 7.017   66.035  47.609  1.000 44.184  ? 39  LEU LLL CA  1 
ATOM   3486  C C   . LEU C 3 39  ? 7.734   64.842  48.242  1.000 48.015  ? 39  LEU LLL C   1 
ATOM   3487  O O   . LEU C 3 39  ? 7.041   63.849  48.580  1.000 51.993  ? 39  LEU LLL O   1 
ATOM   3488  C CB  . LEU C 3 39  ? 6.156   66.774  48.640  1.000 39.735  ? 39  LEU LLL CB  1 
ATOM   3489  C CG  . LEU C 3 39  ? 6.840   67.717  49.631  1.000 38.732  ? 39  LEU LLL CG  1 
ATOM   3490  C CD1 . LEU C 3 39  ? 7.553   66.951  50.724  1.000 36.434  ? 39  LEU LLL CD1 1 
ATOM   3491  C CD2 . LEU C 3 39  ? 7.772   68.710  48.942  1.000 41.566  ? 39  LEU LLL CD2 1 
ATOM   3492  N N   . ALA C 3 40  ? 9.062   64.920  48.343  1.000 48.140  ? 40  ALA LLL N   1 
ATOM   3493  C CA  . ALA C 3 40  ? 9.931   63.843  48.864  1.000 44.535  ? 40  ALA LLL CA  1 
ATOM   3494  C C   . ALA C 3 40  ? 10.778  64.372  50.021  1.000 41.130  ? 40  ALA LLL C   1 
ATOM   3495  O O   . ALA C 3 40  ? 11.012  65.601  50.087  1.000 39.919  ? 40  ALA LLL O   1 
ATOM   3496  C CB  . ALA C 3 40  ? 10.795  63.304  47.759  1.000 47.468  ? 40  ALA LLL CB  1 
ATOM   3497  N N   . TRP C 3 41  ? 11.220  63.459  50.884  1.000 39.594  ? 41  TRP LLL N   1 
ATOM   3498  C CA  . TRP C 3 41  ? 12.127  63.737  52.026  1.000 41.951  ? 41  TRP LLL CA  1 
ATOM   3499  C C   . TRP C 3 41  ? 13.389  62.876  51.924  1.000 41.398  ? 41  TRP LLL C   1 
ATOM   3500  O O   . TRP C 3 41  ? 13.267  61.646  51.735  1.000 41.142  ? 41  TRP LLL O   1 
ATOM   3501  C CB  . TRP C 3 41  ? 11.401  63.491  53.345  1.000 46.495  ? 41  TRP LLL CB  1 
ATOM   3502  C CG  . TRP C 3 41  ? 10.353  64.511  53.652  1.000 51.259  ? 41  TRP LLL CG  1 
ATOM   3503  C CD1 . TRP C 3 41  ? 9.013   64.408  53.422  1.000 55.496  ? 41  TRP LLL CD1 1 
ATOM   3504  C CD2 . TRP C 3 41  ? 10.553  65.792  54.269  1.000 52.770  ? 41  TRP LLL CD2 1 
ATOM   3505  N NE1 . TRP C 3 41  ? 8.365   65.535  53.853  1.000 55.053  ? 41  TRP LLL NE1 1 
ATOM   3506  C CE2 . TRP C 3 41  ? 9.285   66.402  54.376  1.000 53.345  ? 41  TRP LLL CE2 1 
ATOM   3507  C CE3 . TRP C 3 41  ? 11.673  66.477  54.745  1.000 51.564  ? 41  TRP LLL CE3 1 
ATOM   3508  C CZ2 . TRP C 3 41  ? 9.113   67.665  54.935  1.000 52.289  ? 41  TRP LLL CZ2 1 
ATOM   3509  C CZ3 . TRP C 3 41  ? 11.501  67.724  55.299  1.000 50.716  ? 41  TRP LLL CZ3 1 
ATOM   3510  C CH2 . TRP C 3 41  ? 10.239  68.307  55.390  1.000 51.749  ? 41  TRP LLL CH2 1 
ATOM   3511  N N   . TYR C 3 42  ? 14.558  63.509  52.055  1.000 39.569  ? 42  TYR LLL N   1 
ATOM   3512  C CA  . TYR C 3 42  ? 15.887  62.854  52.043  1.000 35.435  ? 42  TYR LLL CA  1 
ATOM   3513  C C   . TYR C 3 42  ? 16.571  63.043  53.398  1.000 35.845  ? 42  TYR LLL C   1 
ATOM   3514  O O   . TYR C 3 42  ? 16.409  64.105  54.057  1.000 32.927  ? 42  TYR LLL O   1 
ATOM   3515  C CB  . TYR C 3 42  ? 16.722  63.412  50.894  1.000 33.160  ? 42  TYR LLL CB  1 
ATOM   3516  C CG  . TYR C 3 42  ? 16.142  63.125  49.537  1.000 33.094  ? 42  TYR LLL CG  1 
ATOM   3517  C CD1 . TYR C 3 42  ? 15.250  64.001  48.940  1.000 32.215  ? 42  TYR LLL CD1 1 
ATOM   3518  C CD2 . TYR C 3 42  ? 16.450  61.953  48.867  1.000 33.065  ? 42  TYR LLL CD2 1 
ATOM   3519  C CE1 . TYR C 3 42  ? 14.697  63.733  47.700  1.000 31.720  ? 42  TYR LLL CE1 1 
ATOM   3520  C CE2 . TYR C 3 42  ? 15.916  61.677  47.617  1.000 34.054  ? 42  TYR LLL CE2 1 
ATOM   3521  C CZ  . TYR C 3 42  ? 15.040  62.572  47.030  1.000 33.396  ? 42  TYR LLL CZ  1 
ATOM   3522  O OH  . TYR C 3 42  ? 14.520  62.293  45.802  1.000 33.342  ? 42  TYR LLL OH  1 
ATOM   3523  N N   . GLN C 3 43  ? 17.298  62.000  53.804  1.000 38.432  ? 43  GLN LLL N   1 
ATOM   3524  C CA  . GLN C 3 43  ? 18.279  62.011  54.921  1.000 40.315  ? 43  GLN LLL CA  1 
ATOM   3525  C C   . GLN C 3 43  ? 19.692  62.035  54.318  1.000 42.727  ? 43  GLN LLL C   1 
ATOM   3526  O O   . GLN C 3 43  ? 19.944  61.247  53.369  1.000 43.171  ? 43  GLN LLL O   1 
ATOM   3527  C CB  . GLN C 3 43  ? 18.034  60.771  55.779  1.000 39.053  ? 43  GLN LLL CB  1 
ATOM   3528  C CG  . GLN C 3 43  ? 19.045  60.563  56.891  1.000 37.393  ? 43  GLN LLL CG  1 
ATOM   3529  C CD  . GLN C 3 43  ? 18.768  59.275  57.618  1.000 34.237  ? 43  GLN LLL CD  1 
ATOM   3530  O OE1 . GLN C 3 43  ? 19.114  58.198  57.125  1.000 34.414  ? 43  GLN LLL OE1 1 
ATOM   3531  N NE2 . GLN C 3 43  ? 18.131  59.392  58.775  1.000 28.675  ? 43  GLN LLL NE2 1 
ATOM   3532  N N   . GLN C 3 44  ? 20.572  62.904  54.828  1.000 42.366  ? 44  GLN LLL N   1 
ATOM   3533  C CA  . GLN C 3 44  ? 22.014  62.911  54.455  1.000 42.300  ? 44  GLN LLL CA  1 
ATOM   3534  C C   . GLN C 3 44  ? 22.862  63.002  55.723  1.000 43.292  ? 44  GLN LLL C   1 
ATOM   3535  O O   . GLN C 3 44  ? 22.656  63.927  56.508  1.000 42.481  ? 44  GLN LLL O   1 
ATOM   3536  C CB  . GLN C 3 44  ? 22.337  64.072  53.521  1.000 39.527  ? 44  GLN LLL CB  1 
ATOM   3537  C CG  . GLN C 3 44  ? 23.633  63.881  52.755  1.000 37.744  ? 44  GLN LLL CG  1 
ATOM   3538  C CD  . GLN C 3 44  ? 24.125  65.203  52.226  1.000 39.181  ? 44  GLN LLL CD  1 
ATOM   3539  O OE1 . GLN C 3 44  ? 23.699  66.286  52.665  1.000 35.024  ? 44  GLN LLL OE1 1 
ATOM   3540  N NE2 . GLN C 3 44  ? 25.039  65.114  51.275  1.000 41.332  ? 44  GLN LLL NE2 1 
ATOM   3541  N N   . LYS C 3 45  ? 23.767  62.051  55.917  1.000 48.832  ? 45  LYS LLL N   1 
ATOM   3542  C CA  . LYS C 3 45  ? 24.735  62.033  57.036  1.000 54.236  ? 45  LYS LLL CA  1 
ATOM   3543  C C   . LYS C 3 45  ? 26.087  62.458  56.495  1.000 61.715  ? 45  LYS LLL C   1 
ATOM   3544  O O   . LYS C 3 45  ? 26.336  62.367  55.290  1.000 65.140  ? 45  LYS LLL O   1 
ATOM   3545  C CB  . LYS C 3 45  ? 24.818  60.625  57.623  1.000 51.570  ? 45  LYS LLL CB  1 
ATOM   3546  C CG  . LYS C 3 45  ? 23.500  60.143  58.181  1.000 51.938  ? 45  LYS LLL CG  1 
ATOM   3547  C CD  . LYS C 3 45  ? 23.549  58.716  58.611  1.000 53.074  ? 45  LYS LLL CD  1 
ATOM   3548  C CE  . LYS C 3 45  ? 22.288  58.286  59.309  1.000 52.546  ? 45  LYS LLL CE  1 
ATOM   3549  N NZ  . LYS C 3 45  ? 22.386  56.856  59.668  1.000 55.014  ? 45  LYS LLL NZ  1 
ATOM   3550  N N   . PRO C 3 46  ? 27.007  62.871  57.385  1.000 61.131  ? 46  PRO LLL N   1 
ATOM   3551  C CA  . PRO C 3 46  ? 28.369  63.204  56.968  1.000 54.828  ? 46  PRO LLL CA  1 
ATOM   3552  C C   . PRO C 3 46  ? 29.005  62.158  56.030  1.000 57.363  ? 46  PRO LLL C   1 
ATOM   3553  O O   . PRO C 3 46  ? 28.888  60.949  56.289  1.000 51.029  ? 46  PRO LLL O   1 
ATOM   3554  C CB  . PRO C 3 46  ? 29.117  63.263  58.299  1.000 58.453  ? 46  PRO LLL CB  1 
ATOM   3555  C CG  . PRO C 3 46  ? 28.051  63.615  59.331  1.000 61.629  ? 46  PRO LLL CG  1 
ATOM   3556  C CD  . PRO C 3 46  ? 26.761  63.012  58.831  1.000 59.324  ? 46  PRO LLL CD  1 
ATOM   3557  N N   . GLY C 3 47  ? 29.638  62.655  54.955  1.000 63.139  ? 47  GLY LLL N   1 
ATOM   3558  C CA  . GLY C 3 47  ? 30.436  61.900  53.962  1.000 60.828  ? 47  GLY LLL CA  1 
ATOM   3559  C C   . GLY C 3 47  ? 29.635  60.842  53.222  1.000 60.621  ? 47  GLY LLL C   1 
ATOM   3560  O O   . GLY C 3 47  ? 30.257  59.864  52.770  1.000 60.620  ? 47  GLY LLL O   1 
ATOM   3561  N N   . GLN C 3 48  ? 28.316  61.016  53.097  1.000 57.961  ? 48  GLN LLL N   1 
ATOM   3562  C CA  . GLN C 3 48  ? 27.405  60.009  52.498  1.000 50.840  ? 48  GLN LLL CA  1 
ATOM   3563  C C   . GLN C 3 48  ? 26.482  60.688  51.494  1.000 44.512  ? 48  GLN LLL C   1 
ATOM   3564  O O   . GLN C 3 48  ? 26.133  61.859  51.638  1.000 44.744  ? 48  GLN LLL O   1 
ATOM   3565  C CB  . GLN C 3 48  ? 26.592  59.302  53.583  1.000 53.378  ? 48  GLN LLL CB  1 
ATOM   3566  C CG  . GLN C 3 48  ? 27.423  58.389  54.478  1.000 54.650  ? 48  GLN LLL CG  1 
ATOM   3567  C CD  . GLN C 3 48  ? 26.609  57.285  55.116  1.000 57.647  ? 48  GLN LLL CD  1 
ATOM   3568  O OE1 . GLN C 3 48  ? 25.420  57.434  55.412  1.000 51.530  ? 48  GLN LLL OE1 1 
ATOM   3569  N NE2 . GLN C 3 48  ? 27.260  56.158  55.349  1.000 59.863  ? 48  GLN LLL NE2 1 
ATOM   3570  N N   . PRO C 3 49  ? 26.032  59.968  50.447  1.000 40.769  ? 49  PRO LLL N   1 
ATOM   3571  C CA  . PRO C 3 49  ? 24.983  60.488  49.578  1.000 41.403  ? 49  PRO LLL CA  1 
ATOM   3572  C C   . PRO C 3 49  ? 23.679  60.635  50.351  1.000 44.776  ? 49  PRO LLL C   1 
ATOM   3573  O O   . PRO C 3 49  ? 23.469  59.977  51.369  1.000 49.081  ? 49  PRO LLL O   1 
ATOM   3574  C CB  . PRO C 3 49  ? 24.851  59.435  48.472  1.000 40.440  ? 49  PRO LLL CB  1 
ATOM   3575  C CG  . PRO C 3 49  ? 25.410  58.170  49.090  1.000 41.604  ? 49  PRO LLL CG  1 
ATOM   3576  C CD  . PRO C 3 49  ? 26.483  58.628  50.054  1.000 41.320  ? 49  PRO LLL CD  1 
ATOM   3577  N N   . PRO C 3 50  ? 22.771  61.525  49.903  1.000 44.506  ? 50  PRO LLL N   1 
ATOM   3578  C CA  . PRO C 3 50  ? 21.406  61.562  50.416  1.000 41.265  ? 50  PRO LLL CA  1 
ATOM   3579  C C   . PRO C 3 50  ? 20.697  60.223  50.188  1.000 43.526  ? 50  PRO LLL C   1 
ATOM   3580  O O   . PRO C 3 50  ? 20.978  59.559  49.196  1.000 44.526  ? 50  PRO LLL O   1 
ATOM   3581  C CB  . PRO C 3 50  ? 20.717  62.629  49.569  1.000 42.215  ? 50  PRO LLL CB  1 
ATOM   3582  C CG  . PRO C 3 50  ? 21.841  63.473  49.027  1.000 43.375  ? 50  PRO LLL CG  1 
ATOM   3583  C CD  . PRO C 3 50  ? 23.006  62.525  48.856  1.000 43.884  ? 50  PRO LLL CD  1 
ATOM   3584  N N   . LYS C 3 51  ? 19.803  59.868  51.110  1.000 44.391  ? 51  LYS LLL N   1 
ATOM   3585  C CA  . LYS C 3 51  ? 18.998  58.621  51.097  1.000 45.805  ? 51  LYS LLL CA  1 
ATOM   3586  C C   . LYS C 3 51  ? 17.526  59.031  51.043  1.000 44.260  ? 51  LYS LLL C   1 
ATOM   3587  O O   . LYS C 3 51  ? 17.126  59.898  51.872  1.000 42.577  ? 51  LYS LLL O   1 
ATOM   3588  C CB  . LYS C 3 51  ? 19.328  57.815  52.362  1.000 54.145  ? 51  LYS LLL CB  1 
ATOM   3589  C CG  . LYS C 3 51  ? 18.663  56.454  52.531  1.000 59.797  ? 51  LYS LLL CG  1 
ATOM   3590  C CD  . LYS C 3 51  ? 18.289  56.162  53.990  1.000 67.893  ? 51  LYS LLL CD  1 
ATOM   3591  C CE  . LYS C 3 51  ? 18.890  54.880  54.516  1.000 79.520  ? 51  LYS LLL CE  1 
ATOM   3592  N NZ  . LYS C 3 51  ? 18.066  53.701  54.159  1.000 86.339  ? 51  LYS LLL NZ  1 
ATOM   3593  N N   . LEU C 3 52  ? 16.749  58.451  50.116  1.000 41.725  ? 52  LEU LLL N   1 
ATOM   3594  C CA  . LEU C 3 52  ? 15.283  58.697  50.034  1.000 40.499  ? 52  LEU LLL CA  1 
ATOM   3595  C C   . LEU C 3 52  ? 14.566  57.971  51.180  1.000 39.773  ? 52  LEU LLL C   1 
ATOM   3596  O O   . LEU C 3 52  ? 14.616  56.717  51.203  1.000 35.605  ? 52  LEU LLL O   1 
ATOM   3597  C CB  . LEU C 3 52  ? 14.754  58.219  48.682  1.000 40.440  ? 52  LEU LLL CB  1 
ATOM   3598  C CG  . LEU C 3 52  ? 13.266  58.484  48.451  1.000 37.539  ? 52  LEU LLL CG  1 
ATOM   3599  C CD1 . LEU C 3 52  ? 12.996  59.960  48.212  1.000 36.636  ? 52  LEU LLL CD1 1 
ATOM   3600  C CD2 . LEU C 3 52  ? 12.760  57.677  47.279  1.000 36.751  ? 52  LEU LLL CD2 1 
ATOM   3601  N N   . LEU C 3 53  ? 13.927  58.745  52.072  1.000 40.902  ? 53  LEU LLL N   1 
ATOM   3602  C CA  . LEU C 3 53  ? 13.083  58.265  53.205  1.000 43.120  ? 53  LEU LLL CA  1 
ATOM   3603  C C   . LEU C 3 53  ? 11.629  58.136  52.745  1.000 43.171  ? 53  LEU LLL C   1 
ATOM   3604  O O   . LEU C 3 53  ? 11.026  57.053  52.908  1.000 39.222  ? 53  LEU LLL O   1 
ATOM   3605  C CB  . LEU C 3 53  ? 13.124  59.256  54.373  1.000 41.957  ? 53  LEU LLL CB  1 
ATOM   3606  C CG  . LEU C 3 53  ? 14.451  59.386  55.109  1.000 41.556  ? 53  LEU LLL CG  1 
ATOM   3607  C CD1 . LEU C 3 53  ? 14.318  60.387  56.245  1.000 41.188  ? 53  LEU LLL CD1 1 
ATOM   3608  C CD2 . LEU C 3 53  ? 14.947  58.047  55.628  1.000 40.420  ? 53  LEU LLL CD2 1 
ATOM   3609  N N   . ILE C 3 54  ? 11.074  59.234  52.241  1.000 42.804  ? 54  ILE LLL N   1 
ATOM   3610  C CA  . ILE C 3 54  ? 9.609   59.364  52.008  1.000 45.222  ? 54  ILE LLL CA  1 
ATOM   3611  C C   . ILE C 3 54  ? 9.352   60.068  50.673  1.000 44.129  ? 54  ILE LLL C   1 
ATOM   3612  O O   . ILE C 3 54  ? 10.042  61.076  50.404  1.000 48.975  ? 54  ILE LLL O   1 
ATOM   3613  C CB  . ILE C 3 54  ? 8.973   60.082  53.210  1.000 47.583  ? 54  ILE LLL CB  1 
ATOM   3614  C CG1 . ILE C 3 54  ? 8.848   59.108  54.390  1.000 50.220  ? 54  ILE LLL CG1 1 
ATOM   3615  C CG2 . ILE C 3 54  ? 7.637   60.697  52.818  1.000 50.316  ? 54  ILE LLL CG2 1 
ATOM   3616  C CD1 . ILE C 3 54  ? 8.481   59.735  55.724  1.000 52.444  ? 54  ILE LLL CD1 1 
ATOM   3617  N N   . TYR C 3 55  ? 8.414   59.528  49.883  1.000 42.124  ? 55  TYR LLL N   1 
ATOM   3618  C CA  . TYR C 3 55  ? 7.925   60.121  48.614  1.000 45.098  ? 55  TYR LLL CA  1 
ATOM   3619  C C   . TYR C 3 55  ? 6.395   60.162  48.623  1.000 45.289  ? 55  TYR LLL C   1 
ATOM   3620  O O   . TYR C 3 55  ? 5.782   59.509  49.494  1.000 45.477  ? 55  TYR LLL O   1 
ATOM   3621  C CB  . TYR C 3 55  ? 8.462   59.353  47.410  1.000 46.838  ? 55  TYR LLL CB  1 
ATOM   3622  C CG  . TYR C 3 55  ? 7.917   57.959  47.264  1.000 47.705  ? 55  TYR LLL CG  1 
ATOM   3623  C CD1 . TYR C 3 55  ? 8.552   56.889  47.864  1.000 48.981  ? 55  TYR LLL CD1 1 
ATOM   3624  C CD2 . TYR C 3 55  ? 6.787   57.711  46.513  1.000 48.401  ? 55  TYR LLL CD2 1 
ATOM   3625  C CE1 . TYR C 3 55  ? 8.071   55.602  47.738  1.000 48.876  ? 55  TYR LLL CE1 1 
ATOM   3626  C CE2 . TYR C 3 55  ? 6.292   56.427  46.375  1.000 51.866  ? 55  TYR LLL CE2 1 
ATOM   3627  C CZ  . TYR C 3 55  ? 6.939   55.371  46.989  1.000 50.935  ? 55  TYR LLL CZ  1 
ATOM   3628  O OH  . TYR C 3 55  ? 6.473   54.099  46.870  1.000 55.186  ? 55  TYR LLL OH  1 
ATOM   3629  N N   . TRP C 3 56  ? 5.820   60.915  47.676  1.000 45.259  ? 56  TRP LLL N   1 
ATOM   3630  C CA  . TRP C 3 56  ? 4.384   61.299  47.629  1.000 42.837  ? 56  TRP LLL CA  1 
ATOM   3631  C C   . TRP C 3 56  ? 3.967   61.796  49.017  1.000 42.807  ? 56  TRP LLL C   1 
ATOM   3632  O O   . TRP C 3 56  ? 2.986   61.292  49.582  1.000 39.450  ? 56  TRP LLL O   1 
ATOM   3633  C CB  . TRP C 3 56  ? 3.519   60.142  47.114  1.000 41.643  ? 56  TRP LLL CB  1 
ATOM   3634  C CG  . TRP C 3 56  ? 3.508   60.003  45.620  1.000 40.046  ? 56  TRP LLL CG  1 
ATOM   3635  C CD1 . TRP C 3 56  ? 3.751   60.974  44.685  1.000 40.343  ? 56  TRP LLL CD1 1 
ATOM   3636  C CD2 . TRP C 3 56  ? 3.178   58.821  44.875  1.000 38.234  ? 56  TRP LLL CD2 1 
ATOM   3637  N NE1 . TRP C 3 56  ? 3.626   60.466  43.417  1.000 39.976  ? 56  TRP LLL NE1 1 
ATOM   3638  C CE2 . TRP C 3 56  ? 3.268   59.149  43.505  1.000 40.223  ? 56  TRP LLL CE2 1 
ATOM   3639  C CE3 . TRP C 3 56  ? 2.824   57.523  45.235  1.000 40.458  ? 56  TRP LLL CE3 1 
ATOM   3640  C CZ2 . TRP C 3 56  ? 3.037   58.217  42.498  1.000 41.284  ? 56  TRP LLL CZ2 1 
ATOM   3641  C CZ3 . TRP C 3 56  ? 2.591   56.605  44.239  1.000 44.027  ? 56  TRP LLL CZ3 1 
ATOM   3642  C CH2 . TRP C 3 56  ? 2.704   56.947  42.890  1.000 41.738  ? 56  TRP LLL CH2 1 
ATOM   3643  N N   . ALA C 3 57  ? 4.769   62.710  49.559  1.000 47.516  ? 57  ALA LLL N   1 
ATOM   3644  C CA  . ALA C 3 57  ? 4.509   63.503  50.783  1.000 51.308  ? 57  ALA LLL CA  1 
ATOM   3645  C C   . ALA C 3 57  ? 4.433   62.624  52.035  1.000 48.791  ? 57  ALA LLL C   1 
ATOM   3646  O O   . ALA C 3 57  ? 4.712   63.199  53.122  1.000 44.779  ? 57  ALA LLL O   1 
ATOM   3647  C CB  . ALA C 3 57  ? 3.249   64.317  50.627  1.000 52.370  ? 57  ALA LLL CB  1 
ATOM   3648  N N   . SER C 3 58  ? 4.094   61.328  51.903  1.000 46.739  ? 58  SER LLL N   1 
ATOM   3649  C CA  . SER C 3 58  ? 3.760   60.449  53.059  1.000 49.283  ? 58  SER LLL CA  1 
ATOM   3650  C C   . SER C 3 58  ? 3.967   58.937  52.832  1.000 47.955  ? 58  SER LLL C   1 
ATOM   3651  O O   . SER C 3 58  ? 3.650   58.199  53.775  1.000 46.491  ? 58  SER LLL O   1 
ATOM   3652  C CB  . SER C 3 58  ? 2.339   60.681  53.444  1.000 51.465  ? 58  SER LLL CB  1 
ATOM   3653  O OG  . SER C 3 58  ? 1.489   60.040  52.493  1.000 54.900  ? 58  SER LLL OG  1 
ATOM   3654  N N   . THR C 3 59  ? 4.425   58.456  51.669  1.000 45.947  ? 59  THR LLL N   1 
ATOM   3655  C CA  . THR C 3 59  ? 4.705   57.009  51.440  1.000 42.929  ? 59  THR LLL CA  1 
ATOM   3656  C C   . THR C 3 59  ? 6.165   56.726  51.805  1.000 45.853  ? 59  THR LLL C   1 
ATOM   3657  O O   . THR C 3 59  ? 7.061   57.447  51.312  1.000 49.576  ? 59  THR LLL O   1 
ATOM   3658  C CB  . THR C 3 59  ? 4.405   56.598  49.996  1.000 42.633  ? 59  THR LLL CB  1 
ATOM   3659  O OG1 . THR C 3 59  ? 3.073   57.022  49.719  1.000 42.408  ? 59  THR LLL OG1 1 
ATOM   3660  C CG2 . THR C 3 59  ? 4.536   55.113  49.743  1.000 42.308  ? 59  THR LLL CG2 1 
ATOM   3661  N N   . ARG C 3 60  ? 6.395   55.710  52.636  1.000 48.480  ? 60  ARG LLL N   1 
ATOM   3662  C CA  . ARG C 3 60  ? 7.743   55.281  53.090  1.000 48.121  ? 60  ARG LLL CA  1 
ATOM   3663  C C   . ARG C 3 60  ? 8.425   54.477  51.982  1.000 47.953  ? 60  ARG LLL C   1 
ATOM   3664  O O   . ARG C 3 60  ? 7.826   53.491  51.523  1.000 48.731  ? 60  ARG LLL O   1 
ATOM   3665  C CB  . ARG C 3 60  ? 7.633   54.423  54.351  1.000 50.097  ? 60  ARG LLL CB  1 
ATOM   3666  C CG  . ARG C 3 60  ? 7.923   55.184  55.632  1.000 55.739  ? 60  ARG LLL CG  1 
ATOM   3667  C CD  . ARG C 3 60  ? 8.082   54.217  56.781  1.000 63.232  ? 60  ARG LLL CD  1 
ATOM   3668  N NE  . ARG C 3 60  ? 6.815   53.587  57.091  1.000 68.326  ? 60  ARG LLL NE  1 
ATOM   3669  C CZ  . ARG C 3 60  ? 5.837   54.141  57.794  1.000 74.457  ? 60  ARG LLL CZ  1 
ATOM   3670  N NH1 . ARG C 3 60  ? 5.948   55.367  58.282  1.000 74.928  ? 60  ARG LLL NH1 1 
ATOM   3671  N NH2 . ARG C 3 60  ? 4.739   53.445  58.019  1.000 84.186  ? 60  ARG LLL NH2 1 
ATOM   3672  N N   . GLU C 3 61  ? 9.629   54.883  51.572  1.000 50.390  ? 61  GLU LLL N   1 
ATOM   3673  C CA  . GLU C 3 61  ? 10.500  54.103  50.648  1.000 51.961  ? 61  GLU LLL CA  1 
ATOM   3674  C C   . GLU C 3 61  ? 10.818  52.783  51.355  1.000 45.969  ? 61  GLU LLL C   1 
ATOM   3675  O O   . GLU C 3 61  ? 10.868  52.784  52.604  1.000 42.028  ? 61  GLU LLL O   1 
ATOM   3676  C CB  . GLU C 3 61  ? 11.742  54.925  50.276  1.000 55.987  ? 61  GLU LLL CB  1 
ATOM   3677  C CG  . GLU C 3 61  ? 12.773  54.191  49.426  1.000 60.012  ? 61  GLU LLL CG  1 
ATOM   3678  C CD  . GLU C 3 61  ? 12.367  53.856  48.002  1.000 59.175  ? 61  GLU LLL CD  1 
ATOM   3679  O OE1 . GLU C 3 61  ? 13.070  54.299  47.066  1.000 58.594  ? 61  GLU LLL OE1 1 
ATOM   3680  O OE2 . GLU C 3 61  ? 11.374  53.127  47.836  1.000 62.127  ? 61  GLU LLL OE2 1 
ATOM   3681  N N   . SER C 3 62  ? 10.977  51.682  50.625  1.000 43.416  ? 62  SER LLL N   1 
ATOM   3682  C CA  . SER C 3 62  ? 11.121  50.357  51.275  1.000 48.760  ? 62  SER LLL CA  1 
ATOM   3683  C C   . SER C 3 62  ? 12.400  50.371  52.114  1.000 44.172  ? 62  SER LLL C   1 
ATOM   3684  O O   . SER C 3 62  ? 13.290  51.150  51.809  1.000 37.743  ? 62  SER LLL O   1 
ATOM   3685  C CB  . SER C 3 62  ? 11.035  49.179  50.320  1.000 52.561  ? 62  SER LLL CB  1 
ATOM   3686  O OG  . SER C 3 62  ? 11.825  49.393  49.174  1.000 56.651  ? 62  SER LLL OG  1 
ATOM   3687  N N   . GLY C 3 63  ? 12.402  49.583  53.188  1.000 47.004  ? 63  GLY LLL N   1 
ATOM   3688  C CA  . GLY C 3 63  ? 13.461  49.512  54.207  1.000 44.817  ? 63  GLY LLL CA  1 
ATOM   3689  C C   . GLY C 3 63  ? 13.591  50.787  55.008  1.000 41.571  ? 63  GLY LLL C   1 
ATOM   3690  O O   . GLY C 3 63  ? 14.704  51.043  55.471  1.000 47.443  ? 63  GLY LLL O   1 
ATOM   3691  N N   . VAL C 3 64  ? 12.524  51.566  55.171  1.000 39.400  ? 64  VAL LLL N   1 
ATOM   3692  C CA  . VAL C 3 64  ? 12.536  52.742  56.089  1.000 40.089  ? 64  VAL LLL CA  1 
ATOM   3693  C C   . VAL C 3 64  ? 11.710  52.397  57.314  1.000 43.020  ? 64  VAL LLL C   1 
ATOM   3694  O O   . VAL C 3 64  ? 10.563  52.005  57.181  1.000 41.001  ? 64  VAL LLL O   1 
ATOM   3695  C CB  . VAL C 3 64  ? 12.025  54.015  55.408  1.000 37.468  ? 64  VAL LLL CB  1 
ATOM   3696  C CG1 . VAL C 3 64  ? 11.917  55.176  56.385  1.000 37.013  ? 64  VAL LLL CG1 1 
ATOM   3697  C CG2 . VAL C 3 64  ? 12.925  54.398  54.252  1.000 39.090  ? 64  VAL LLL CG2 1 
ATOM   3698  N N   . PRO C 3 65  ? 12.261  52.543  58.535  1.000 53.089  ? 65  PRO LLL N   1 
ATOM   3699  C CA  . PRO C 3 65  ? 11.568  52.095  59.738  1.000 60.403  ? 65  PRO LLL CA  1 
ATOM   3700  C C   . PRO C 3 65  ? 10.279  52.893  59.953  1.000 61.263  ? 65  PRO LLL C   1 
ATOM   3701  O O   . PRO C 3 65  ? 10.130  53.953  59.378  1.000 60.156  ? 65  PRO LLL O   1 
ATOM   3702  C CB  . PRO C 3 65  ? 12.517  52.350  60.917  1.000 66.087  ? 65  PRO LLL CB  1 
ATOM   3703  C CG  . PRO C 3 65  ? 13.835  52.808  60.281  1.000 69.538  ? 65  PRO LLL CG  1 
ATOM   3704  C CD  . PRO C 3 65  ? 13.556  53.167  58.830  1.000 63.786  ? 65  PRO LLL CD  1 
ATOM   3705  N N   . ASP C 3 66  ? 9.425   52.387  60.835  1.000 61.174  ? 66  ASP LLL N   1 
ATOM   3706  C CA  . ASP C 3 66  ? 8.066   52.935  61.059  1.000 61.894  ? 66  ASP LLL CA  1 
ATOM   3707  C C   . ASP C 3 66  ? 8.178   54.348  61.643  1.000 57.621  ? 66  ASP LLL C   1 
ATOM   3708  O O   . ASP C 3 66  ? 7.248   55.133  61.433  1.000 56.573  ? 66  ASP LLL O   1 
ATOM   3709  C CB  . ASP C 3 66  ? 7.252   51.989  61.938  1.000 68.266  ? 66  ASP LLL CB  1 
ATOM   3710  C CG  . ASP C 3 66  ? 7.072   50.612  61.311  1.000 73.270  ? 66  ASP LLL CG  1 
ATOM   3711  O OD1 . ASP C 3 66  ? 6.867   50.553  60.081  1.000 78.902  ? 66  ASP LLL OD1 1 
ATOM   3712  O OD2 . ASP C 3 66  ? 7.164   49.607  62.044  1.000 75.645  ? 66  ASP LLL OD2 1 
ATOM   3713  N N   . ARG C 3 67  ? 9.277   54.676  62.330  1.000 54.862  ? 67  ARG LLL N   1 
ATOM   3714  C CA  . ARG C 3 67  ? 9.349   55.891  63.187  1.000 54.471  ? 67  ARG LLL CA  1 
ATOM   3715  C C   . ARG C 3 67  ? 9.414   57.151  62.317  1.000 51.198  ? 67  ARG LLL C   1 
ATOM   3716  O O   . ARG C 3 67  ? 9.176   58.262  62.855  1.000 56.009  ? 67  ARG LLL O   1 
ATOM   3717  C CB  . ARG C 3 67  ? 10.498  55.776  64.194  1.000 59.612  ? 67  ARG LLL CB  1 
ATOM   3718  C CG  . ARG C 3 67  ? 11.888  55.643  63.595  1.000 61.923  ? 67  ARG LLL CG  1 
ATOM   3719  C CD  . ARG C 3 67  ? 12.984  55.952  64.611  1.000 58.703  ? 67  ARG LLL CD  1 
ATOM   3720  N NE  . ARG C 3 67  ? 14.304  56.052  63.997  1.000 57.666  ? 67  ARG LLL NE  1 
ATOM   3721  C CZ  . ARG C 3 67  ? 15.010  55.025  63.523  1.000 57.476  ? 67  ARG LLL CZ  1 
ATOM   3722  N NH1 . ARG C 3 67  ? 14.547  53.797  63.579  1.000 67.067  ? 67  ARG LLL NH1 1 
ATOM   3723  N NH2 . ARG C 3 67  ? 16.191  55.208  62.982  1.000 55.012  ? 67  ARG LLL NH2 1 
ATOM   3724  N N   . PHE C 3 68  ? 9.702   56.993  61.028  1.000 48.214  ? 68  PHE LLL N   1 
ATOM   3725  C CA  . PHE C 3 68  ? 9.626   58.084  60.021  1.000 49.292  ? 68  PHE LLL CA  1 
ATOM   3726  C C   . PHE C 3 68  ? 8.225   58.092  59.431  1.000 49.175  ? 68  PHE LLL C   1 
ATOM   3727  O O   . PHE C 3 68  ? 7.786   57.040  58.957  1.000 55.658  ? 68  PHE LLL O   1 
ATOM   3728  C CB  . PHE C 3 68  ? 10.643  57.884  58.893  1.000 48.046  ? 68  PHE LLL CB  1 
ATOM   3729  C CG  . PHE C 3 68  ? 12.066  58.016  59.342  1.000 41.638  ? 68  PHE LLL CG  1 
ATOM   3730  C CD1 . PHE C 3 68  ? 12.769  56.915  59.792  1.000 40.627  ? 68  PHE LLL CD1 1 
ATOM   3731  C CD2 . PHE C 3 68  ? 12.662  59.255  59.383  1.000 42.161  ? 68  PHE LLL CD2 1 
ATOM   3732  C CE1 . PHE C 3 68  ? 14.068  57.043  60.242  1.000 43.494  ? 68  PHE LLL CE1 1 
ATOM   3733  C CE2 . PHE C 3 68  ? 13.961  59.390  59.842  1.000 48.446  ? 68  PHE LLL CE2 1 
ATOM   3734  C CZ  . PHE C 3 68  ? 14.666  58.281  60.261  1.000 47.717  ? 68  PHE LLL CZ  1 
ATOM   3735  N N   . SER C 3 69  ? 7.550   59.236  59.453  1.000 48.935  ? 69  SER LLL N   1 
ATOM   3736  C CA  . SER C 3 69  ? 6.230   59.400  58.794  1.000 49.184  ? 69  SER LLL CA  1 
ATOM   3737  C C   . SER C 3 69  ? 6.153   60.802  58.218  1.000 44.477  ? 69  SER LLL C   1 
ATOM   3738  O O   . SER C 3 69  ? 6.679   61.731  58.842  1.000 41.657  ? 69  SER LLL O   1 
ATOM   3739  C CB  . SER C 3 69  ? 5.100   59.128  59.741  1.000 53.910  ? 69  SER LLL CB  1 
ATOM   3740  O OG  . SER C 3 69  ? 5.089   60.096  60.773  1.000 59.296  ? 69  SER LLL OG  1 
ATOM   3741  N N   . GLY C 3 70  ? 5.553   60.918  57.042  1.000 48.274  ? 70  GLY LLL N   1 
ATOM   3742  C CA  . GLY C 3 70  ? 5.414   62.189  56.309  1.000 53.657  ? 70  GLY LLL CA  1 
ATOM   3743  C C   . GLY C 3 70  ? 3.953   62.545  56.199  1.000 58.975  ? 70  GLY LLL C   1 
ATOM   3744  O O   . GLY C 3 70  ? 3.126   61.616  56.193  1.000 67.405  ? 70  GLY LLL O   1 
ATOM   3745  N N   . SER C 3 71  ? 3.634   63.834  56.152  1.000 63.857  ? 71  SER LLL N   1 
ATOM   3746  C CA  . SER C 3 71  ? 2.230   64.308  56.125  1.000 67.166  ? 71  SER LLL CA  1 
ATOM   3747  C C   . SER C 3 71  ? 2.159   65.702  55.507  1.000 69.686  ? 71  SER LLL C   1 
ATOM   3748  O O   . SER C 3 71  ? 3.231   66.246  55.093  1.000 76.301  ? 71  SER LLL O   1 
ATOM   3749  C CB  . SER C 3 71  ? 1.651   64.272  57.505  1.000 67.208  ? 71  SER LLL CB  1 
ATOM   3750  O OG  . SER C 3 71  ? 2.465   65.012  58.392  1.000 68.977  ? 71  SER LLL OG  1 
ATOM   3751  N N   . GLY C 3 72  ? 0.933   66.223  55.427  1.000 65.729  ? 72  GLY LLL N   1 
ATOM   3752  C CA  . GLY C 3 72  ? 0.621   67.559  54.893  1.000 62.831  ? 72  GLY LLL CA  1 
ATOM   3753  C C   . GLY C 3 72  ? -0.135  67.449  53.589  1.000 60.257  ? 72  GLY LLL C   1 
ATOM   3754  O O   . GLY C 3 72  ? -0.304  66.319  53.087  1.000 54.905  ? 72  GLY LLL O   1 
ATOM   3755  N N   . SER C 3 73  ? -0.567  68.593  53.067  1.000 62.557  ? 73  SER LLL N   1 
ATOM   3756  C CA  . SER C 3 73  ? -1.311  68.712  51.792  1.000 64.603  ? 73  SER LLL CA  1 
ATOM   3757  C C   . SER C 3 73  ? -1.198  70.128  51.225  1.000 61.205  ? 73  SER LLL C   1 
ATOM   3758  O O   . SER C 3 73  ? -0.912  71.056  51.987  1.000 67.713  ? 73  SER LLL O   1 
ATOM   3759  C CB  . SER C 3 73  ? -2.732  68.332  51.996  1.000 69.439  ? 73  SER LLL CB  1 
ATOM   3760  O OG  . SER C 3 73  ? -3.262  67.865  50.772  1.000 80.740  ? 73  SER LLL OG  1 
ATOM   3761  N N   . GLY C 3 74  ? -1.433  70.288  49.928  1.000 57.380  ? 74  GLY LLL N   1 
ATOM   3762  C CA  . GLY C 3 74  ? -1.384  71.605  49.278  1.000 58.592  ? 74  GLY LLL CA  1 
ATOM   3763  C C   . GLY C 3 74  ? 0.021   72.161  49.320  1.000 57.630  ? 74  GLY LLL C   1 
ATOM   3764  O O   . GLY C 3 74  ? 0.789   71.787  48.440  1.000 62.338  ? 74  GLY LLL O   1 
ATOM   3765  N N   . THR C 3 75  ? 0.353   72.989  50.317  1.000 56.362  ? 75  THR LLL N   1 
ATOM   3766  C CA  . THR C 3 75  ? 1.658   73.701  50.392  1.000 56.412  ? 75  THR LLL CA  1 
ATOM   3767  C C   . THR C 3 75  ? 2.369   73.502  51.735  1.000 58.606  ? 75  THR LLL C   1 
ATOM   3768  O O   . THR C 3 75  ? 3.557   73.914  51.802  1.000 77.211  ? 75  THR LLL O   1 
ATOM   3769  C CB  . THR C 3 75  ? 1.536   75.210  50.126  1.000 55.494  ? 75  THR LLL CB  1 
ATOM   3770  O OG1 . THR C 3 75  ? 0.956   75.842  51.267  1.000 52.522  ? 75  THR LLL OG1 1 
ATOM   3771  C CG2 . THR C 3 75  ? 0.741   75.537  48.883  1.000 56.083  ? 75  THR LLL CG2 1 
ATOM   3772  N N   . ASP C 3 76  ? 1.722   72.927  52.757  1.000 54.491  ? 76  ASP LLL N   1 
ATOM   3773  C CA  . ASP C 3 76  ? 2.359   72.744  54.092  1.000 54.225  ? 76  ASP LLL CA  1 
ATOM   3774  C C   . ASP C 3 76  ? 2.533   71.248  54.332  1.000 52.757  ? 76  ASP LLL C   1 
ATOM   3775  O O   . ASP C 3 76  ? 1.513   70.517  54.312  1.000 48.792  ? 76  ASP LLL O   1 
ATOM   3776  C CB  . ASP C 3 76  ? 1.608   73.468  55.211  1.000 56.293  ? 76  ASP LLL CB  1 
ATOM   3777  C CG  . ASP C 3 76  ? 1.559   74.976  55.001  1.000 64.824  ? 76  ASP LLL CG  1 
ATOM   3778  O OD1 . ASP C 3 76  ? 0.436   75.522  54.965  1.000 73.082  ? 76  ASP LLL OD1 1 
ATOM   3779  O OD2 . ASP C 3 76  ? 2.641   75.599  54.856  1.000 69.882  ? 76  ASP LLL OD2 1 
ATOM   3780  N N   . PHE C 3 77  ? 3.797   70.825  54.493  1.000 49.215  ? 77  PHE LLL N   1 
ATOM   3781  C CA  . PHE C 3 77  ? 4.210   69.407  54.635  1.000 43.941  ? 77  PHE LLL CA  1 
ATOM   3782  C C   . PHE C 3 77  ? 5.101   69.252  55.860  1.000 44.375  ? 77  PHE LLL C   1 
ATOM   3783  O O   . PHE C 3 77  ? 5.753   70.235  56.268  1.000 43.760  ? 77  PHE LLL O   1 
ATOM   3784  C CB  . PHE C 3 77  ? 4.928   68.930  53.380  1.000 40.685  ? 77  PHE LLL CB  1 
ATOM   3785  C CG  . PHE C 3 77  ? 4.064   68.941  52.152  1.000 39.824  ? 77  PHE LLL CG  1 
ATOM   3786  C CD1 . PHE C 3 77  ? 3.217   67.881  51.874  1.000 42.135  ? 77  PHE LLL CD1 1 
ATOM   3787  C CD2 . PHE C 3 77  ? 4.092   70.017  51.282  1.000 40.448  ? 77  PHE LLL CD2 1 
ATOM   3788  C CE1 . PHE C 3 77  ? 2.413   67.899  50.741  1.000 43.720  ? 77  PHE LLL CE1 1 
ATOM   3789  C CE2 . PHE C 3 77  ? 3.314   70.021  50.134  1.000 41.071  ? 77  PHE LLL CE2 1 
ATOM   3790  C CZ  . PHE C 3 77  ? 2.466   68.968  49.872  1.000 42.870  ? 77  PHE LLL CZ  1 
ATOM   3791  N N   . THR C 3 78  ? 5.132   68.033  56.399  1.000 46.864  ? 78  THR LLL N   1 
ATOM   3792  C CA  . THR C 3 78  ? 5.831   67.706  57.662  1.000 51.298  ? 78  THR LLL CA  1 
ATOM   3793  C C   . THR C 3 78  ? 6.485   66.332  57.551  1.000 55.218  ? 78  THR LLL C   1 
ATOM   3794  O O   . THR C 3 78  ? 5.787   65.366  57.152  1.000 65.010  ? 78  THR LLL O   1 
ATOM   3795  C CB  . THR C 3 78  ? 4.861   67.781  58.847  1.000 53.785  ? 78  THR LLL CB  1 
ATOM   3796  O OG1 . THR C 3 78  ? 4.692   69.171  59.109  1.000 52.789  ? 78  THR LLL OG1 1 
ATOM   3797  C CG2 . THR C 3 78  ? 5.346   67.086  60.102  1.000 54.380  ? 78  THR LLL CG2 1 
ATOM   3798  N N   . LEU C 3 79  ? 7.773   66.270  57.899  1.000 53.696  ? 79  LEU LLL N   1 
ATOM   3799  C CA  . LEU C 3 79  ? 8.478   65.011  58.249  1.000 49.244  ? 79  LEU LLL CA  1 
ATOM   3800  C C   . LEU C 3 79  ? 8.559   64.904  59.775  1.000 46.780  ? 79  LEU LLL C   1 
ATOM   3801  O O   . LEU C 3 79  ? 8.941   65.904  60.438  1.000 42.602  ? 79  LEU LLL O   1 
ATOM   3802  C CB  . LEU C 3 79  ? 9.870   64.999  57.613  1.000 47.084  ? 79  LEU LLL CB  1 
ATOM   3803  C CG  . LEU C 3 79  ? 10.666  63.721  57.846  1.000 45.569  ? 79  LEU LLL CG  1 
ATOM   3804  C CD1 . LEU C 3 79  ? 10.011  62.549  57.151  1.000 46.767  ? 79  LEU LLL CD1 1 
ATOM   3805  C CD2 . LEU C 3 79  ? 12.092  63.891  57.368  1.000 48.863  ? 79  LEU LLL CD2 1 
ATOM   3806  N N   . THR C 3 80  ? 8.207   63.733  60.305  1.000 46.809  ? 80  THR LLL N   1 
ATOM   3807  C CA  . THR C 3 80  ? 8.141   63.462  61.759  1.000 50.006  ? 80  THR LLL CA  1 
ATOM   3808  C C   . THR C 3 80  ? 8.929   62.197  62.092  1.000 53.016  ? 80  THR LLL C   1 
ATOM   3809  O O   . THR C 3 80  ? 8.666   61.143  61.484  1.000 53.531  ? 80  THR LLL O   1 
ATOM   3810  C CB  . THR C 3 80  ? 6.697   63.301  62.243  1.000 52.596  ? 80  THR LLL CB  1 
ATOM   3811  O OG1 . THR C 3 80  ? 5.949   64.467  61.890  1.000 52.264  ? 80  THR LLL OG1 1 
ATOM   3812  C CG2 . THR C 3 80  ? 6.626   63.074  63.738  1.000 54.298  ? 80  THR LLL CG2 1 
ATOM   3813  N N   . ILE C 3 81  ? 9.850   62.319  63.043  1.000 58.728  ? 81  ILE LLL N   1 
ATOM   3814  C CA  . ILE C 3 81  ? 10.546  61.185  63.705  1.000 59.936  ? 81  ILE LLL CA  1 
ATOM   3815  C C   . ILE C 3 81  ? 9.971   61.115  65.119  1.000 59.935  ? 81  ILE LLL C   1 
ATOM   3816  O O   . ILE C 3 81  ? 10.263  62.022  65.907  1.000 69.253  ? 81  ILE LLL O   1 
ATOM   3817  C CB  . ILE C 3 81  ? 12.080  61.401  63.703  1.000 63.476  ? 81  ILE LLL CB  1 
ATOM   3818  C CG1 . ILE C 3 81  ? 12.612  61.682  62.292  1.000 64.834  ? 81  ILE LLL CG1 1 
ATOM   3819  C CG2 . ILE C 3 81  ? 12.819  60.233  64.355  1.000 62.974  ? 81  ILE LLL CG2 1 
ATOM   3820  C CD1 . ILE C 3 81  ? 14.114  61.929  62.207  1.000 63.767  ? 81  ILE LLL CD1 1 
ATOM   3821  N N   . SER C 3 82  ? 9.120   60.136  65.410  1.000 56.014  ? 82  SER LLL N   1 
ATOM   3822  C CA  . SER C 3 82  ? 8.880   59.667  66.802  1.000 59.524  ? 82  SER LLL CA  1 
ATOM   3823  C C   . SER C 3 82  ? 10.107  58.856  67.247  1.000 67.954  ? 82  SER LLL C   1 
ATOM   3824  O O   . SER C 3 82  ? 10.655  58.157  66.382  1.000 88.268  ? 82  SER LLL O   1 
ATOM   3825  C CB  . SER C 3 82  ? 7.657   58.836  66.848  1.000 59.007  ? 82  SER LLL CB  1 
ATOM   3826  O OG  . SER C 3 82  ? 7.780   57.778  65.906  1.000 59.307  ? 82  SER LLL OG  1 
ATOM   3827  N N   . SER C 3 83  ? 10.522  58.919  68.517  1.000 70.959  ? 83  SER LLL N   1 
ATOM   3828  C CA  . SER C 3 83  ? 11.696  58.171  69.066  1.000 68.276  ? 83  SER LLL CA  1 
ATOM   3829  C C   . SER C 3 83  ? 12.962  58.462  68.255  1.000 60.946  ? 83  SER LLL C   1 
ATOM   3830  O O   . SER C 3 83  ? 13.400  57.581  67.494  1.000 58.595  ? 83  SER LLL O   1 
ATOM   3831  C CB  . SER C 3 83  ? 11.453  56.675  69.107  1.000 73.121  ? 83  SER LLL CB  1 
ATOM   3832  O OG  . SER C 3 83  ? 10.913  56.277  70.352  1.000 84.307  ? 83  SER LLL OG  1 
ATOM   3833  N N   . LEU C 3 84  ? 13.549  59.640  68.428  1.000 57.077  ? 84  LEU LLL N   1 
ATOM   3834  C CA  . LEU C 3 84  ? 14.845  59.959  67.794  1.000 50.954  ? 84  LEU LLL CA  1 
ATOM   3835  C C   . LEU C 3 84  ? 15.860  58.938  68.295  1.000 50.640  ? 84  LEU LLL C   1 
ATOM   3836  O O   . LEU C 3 84  ? 15.897  58.681  69.497  1.000 53.419  ? 84  LEU LLL O   1 
ATOM   3837  C CB  . LEU C 3 84  ? 15.280  61.381  68.133  1.000 51.710  ? 84  LEU LLL CB  1 
ATOM   3838  C CG  . LEU C 3 84  ? 16.417  61.908  67.258  1.000 54.030  ? 84  LEU LLL CG  1 
ATOM   3839  C CD1 . LEU C 3 84  ? 15.952  62.088  65.821  1.000 54.558  ? 84  LEU LLL CD1 1 
ATOM   3840  C CD2 . LEU C 3 84  ? 16.951  63.223  67.786  1.000 55.912  ? 84  LEU LLL CD2 1 
ATOM   3841  N N   . GLN C 3 85  ? 16.595  58.330  67.370  1.000 53.392  ? 85  GLN LLL N   1 
ATOM   3842  C CA  . GLN C 3 85  ? 17.643  57.310  67.640  1.000 53.024  ? 85  GLN LLL CA  1 
ATOM   3843  C C   . GLN C 3 85  ? 19.001  57.958  67.387  1.000 53.367  ? 85  GLN LLL C   1 
ATOM   3844  O O   . GLN C 3 85  ? 19.026  58.997  66.685  1.000 51.023  ? 85  GLN LLL O   1 
ATOM   3845  C CB  . GLN C 3 85  ? 17.398  56.107  66.729  1.000 54.393  ? 85  GLN LLL CB  1 
ATOM   3846  C CG  . GLN C 3 85  ? 16.041  55.467  66.976  1.000 53.049  ? 85  GLN LLL CG  1 
ATOM   3847  C CD  . GLN C 3 85  ? 15.944  54.946  68.392  1.000 53.298  ? 85  GLN LLL CD  1 
ATOM   3848  O OE1 . GLN C 3 85  ? 16.856  54.290  68.881  1.000 56.387  ? 85  GLN LLL OE1 1 
ATOM   3849  N NE2 . GLN C 3 85  ? 14.827  55.193  69.061  1.000 55.383  ? 85  GLN LLL NE2 1 
ATOM   3850  N N   . ALA C 3 86  ? 20.085  57.417  67.946  1.000 53.383  ? 86  ALA LLL N   1 
ATOM   3851  C CA  . ALA C 3 86  ? 21.451  57.995  67.793  1.000 56.315  ? 86  ALA LLL CA  1 
ATOM   3852  C C   . ALA C 3 86  ? 21.784  58.202  66.304  1.000 52.248  ? 86  ALA LLL C   1 
ATOM   3853  O O   . ALA C 3 86  ? 22.372  59.230  65.922  1.000 51.305  ? 86  ALA LLL O   1 
ATOM   3854  C CB  . ALA C 3 86  ? 22.463  57.094  68.458  1.000 58.133  ? 86  ALA LLL CB  1 
ATOM   3855  N N   . GLU C 3 87  ? 21.311  57.252  65.512  1.000 49.731  ? 87  GLU LLL N   1 
ATOM   3856  C CA  . GLU C 3 87  ? 21.564  57.006  64.073  1.000 50.449  ? 87  GLU LLL CA  1 
ATOM   3857  C C   . GLU C 3 87  ? 20.727  57.947  63.215  1.000 48.964  ? 87  GLU LLL C   1 
ATOM   3858  O O   . GLU C 3 87  ? 20.780  57.814  61.999  1.000 56.318  ? 87  GLU LLL O   1 
ATOM   3859  C CB  . GLU C 3 87  ? 21.166  55.557  63.799  1.000 52.194  ? 87  GLU LLL CB  1 
ATOM   3860  C CG  . GLU C 3 87  ? 20.576  54.962  65.040  1.000 58.887  ? 87  GLU LLL CG  1 
ATOM   3861  C CD  . GLU C 3 87  ? 19.998  53.571  65.015  1.000 73.306  ? 87  GLU LLL CD  1 
ATOM   3862  O OE1 . GLU C 3 87  ? 19.834  53.018  63.910  1.000 82.655  ? 87  GLU LLL OE1 1 
ATOM   3863  O OE2 . GLU C 3 87  ? 19.711  53.051  66.120  1.000 79.340  ? 87  GLU LLL OE2 1 
ATOM   3864  N N   . ASP C 3 88  ? 19.933  58.821  63.828  1.000 46.312  ? 88  ASP LLL N   1 
ATOM   3865  C CA  . ASP C 3 88  ? 19.042  59.754  63.099  1.000 44.164  ? 88  ASP LLL CA  1 
ATOM   3866  C C   . ASP C 3 88  ? 19.716  61.120  63.012  1.000 40.972  ? 88  ASP LLL C   1 
ATOM   3867  O O   . ASP C 3 88  ? 19.187  61.972  62.264  1.000 38.689  ? 88  ASP LLL O   1 
ATOM   3868  C CB  . ASP C 3 88  ? 17.664  59.813  63.757  1.000 44.750  ? 88  ASP LLL CB  1 
ATOM   3869  C CG  . ASP C 3 88  ? 16.871  58.550  63.515  1.000 46.201  ? 88  ASP LLL CG  1 
ATOM   3870  O OD1 . ASP C 3 88  ? 17.106  57.933  62.456  1.000 52.219  ? 88  ASP LLL OD1 1 
ATOM   3871  O OD2 . ASP C 3 88  ? 16.036  58.190  64.378  1.000 45.742  ? 88  ASP LLL OD2 1 
ATOM   3872  N N   . VAL C 3 89  ? 20.825  61.322  63.734  1.000 36.262  ? 89  VAL LLL N   1 
ATOM   3873  C CA  . VAL C 3 89  ? 21.598  62.588  63.630  1.000 36.339  ? 89  VAL LLL CA  1 
ATOM   3874  C C   . VAL C 3 89  ? 21.981  62.748  62.162  1.000 36.897  ? 89  VAL LLL C   1 
ATOM   3875  O O   . VAL C 3 89  ? 22.816  61.940  61.690  1.000 39.633  ? 89  VAL LLL O   1 
ATOM   3876  C CB  . VAL C 3 89  ? 22.876  62.605  64.483  1.000 38.668  ? 89  VAL LLL CB  1 
ATOM   3877  C CG1 . VAL C 3 89  ? 23.666  63.882  64.222  1.000 40.799  ? 89  VAL LLL CG1 1 
ATOM   3878  C CG2 . VAL C 3 89  ? 22.628  62.441  65.971  1.000 38.992  ? 89  VAL LLL CG2 1 
ATOM   3879  N N   . ALA C 3 90  ? 21.400  63.724  61.469  1.000 35.109  ? 90  ALA LLL N   1 
ATOM   3880  C CA  . ALA C 3 90  ? 21.652  63.964  60.034  1.000 35.712  ? 90  ALA LLL CA  1 
ATOM   3881  C C   . ALA C 3 90  ? 21.060  65.305  59.619  1.000 34.431  ? 90  ALA LLL C   1 
ATOM   3882  O O   . ALA C 3 90  ? 20.428  65.962  60.435  1.000 34.397  ? 90  ALA LLL O   1 
ATOM   3883  C CB  . ALA C 3 90  ? 21.044  62.851  59.210  1.000 36.844  ? 90  ALA LLL CB  1 
ATOM   3884  N N   . VAL C 3 91  ? 21.255  65.666  58.365  1.000 33.708  ? 91  VAL LLL N   1 
ATOM   3885  C CA  . VAL C 3 91  ? 20.495  66.771  57.732  1.000 35.745  ? 91  VAL LLL CA  1 
ATOM   3886  C C   . VAL C 3 91  ? 19.353  66.142  56.936  1.000 35.591  ? 91  VAL LLL C   1 
ATOM   3887  O O   . VAL C 3 91  ? 19.565  65.068  56.329  1.000 34.697  ? 91  VAL LLL O   1 
ATOM   3888  C CB  . VAL C 3 91  ? 21.404  67.638  56.851  1.000 36.386  ? 91  VAL LLL CB  1 
ATOM   3889  C CG1 . VAL C 3 91  ? 20.607  68.721  56.150  1.000 36.689  ? 91  VAL LLL CG1 1 
ATOM   3890  C CG2 . VAL C 3 91  ? 22.535  68.234  57.666  1.000 36.854  ? 91  VAL LLL CG2 1 
ATOM   3891  N N   . TYR C 3 92  ? 18.179  66.771  56.974  1.000 33.831  ? 92  TYR LLL N   1 
ATOM   3892  C CA  . TYR C 3 92  ? 16.986  66.316  56.231  1.000 33.873  ? 92  TYR LLL CA  1 
ATOM   3893  C C   . TYR C 3 92  ? 16.572  67.436  55.276  1.000 36.815  ? 92  TYR LLL C   1 
ATOM   3894  O O   . TYR C 3 92  ? 16.376  68.593  55.737  1.000 33.539  ? 92  TYR LLL O   1 
ATOM   3895  C CB  . TYR C 3 92  ? 15.888  65.916  57.211  1.000 32.825  ? 92  TYR LLL CB  1 
ATOM   3896  C CG  . TYR C 3 92  ? 16.246  64.752  58.095  1.000 31.794  ? 92  TYR LLL CG  1 
ATOM   3897  C CD1 . TYR C 3 92  ? 16.923  64.937  59.294  1.000 30.432  ? 92  TYR LLL CD1 1 
ATOM   3898  C CD2 . TYR C 3 92  ? 15.907  63.461  57.730  1.000 31.663  ? 92  TYR LLL CD2 1 
ATOM   3899  C CE1 . TYR C 3 92  ? 17.254  63.868  60.109  1.000 29.203  ? 92  TYR LLL CE1 1 
ATOM   3900  C CE2 . TYR C 3 92  ? 16.217  62.381  58.541  1.000 30.348  ? 92  TYR LLL CE2 1 
ATOM   3901  C CZ  . TYR C 3 92  ? 16.901  62.584  59.729  1.000 30.108  ? 92  TYR LLL CZ  1 
ATOM   3902  O OH  . TYR C 3 92  ? 17.218  61.510  60.509  1.000 30.808  ? 92  TYR LLL OH  1 
ATOM   3903  N N   . TYR C 3 93  ? 16.475  67.102  53.986  1.000 38.284  ? 93  TYR LLL N   1 
ATOM   3904  C CA  . TYR C 3 93  ? 15.997  68.007  52.915  1.000 40.074  ? 93  TYR LLL CA  1 
ATOM   3905  C C   . TYR C 3 93  ? 14.639  67.514  52.407  1.000 44.030  ? 93  TYR LLL C   1 
ATOM   3906  O O   . TYR C 3 93  ? 14.476  66.293  52.222  1.000 47.402  ? 93  TYR LLL O   1 
ATOM   3907  C CB  . TYR C 3 93  ? 16.998  68.066  51.760  1.000 40.001  ? 93  TYR LLL CB  1 
ATOM   3908  C CG  . TYR C 3 93  ? 18.413  68.434  52.126  1.000 38.851  ? 93  TYR LLL CG  1 
ATOM   3909  C CD1 . TYR C 3 93  ? 18.886  69.735  52.016  1.000 38.907  ? 93  TYR LLL CD1 1 
ATOM   3910  C CD2 . TYR C 3 93  ? 19.302  67.464  52.529  1.000 39.203  ? 93  TYR LLL CD2 1 
ATOM   3911  C CE1 . TYR C 3 93  ? 20.197  70.067  52.320  1.000 35.765  ? 93  TYR LLL CE1 1 
ATOM   3912  C CE2 . TYR C 3 93  ? 20.616  67.777  52.839  1.000 41.593  ? 93  TYR LLL CE2 1 
ATOM   3913  C CZ  . TYR C 3 93  ? 21.066  69.082  52.735  1.000 37.692  ? 93  TYR LLL CZ  1 
ATOM   3914  O OH  . TYR C 3 93  ? 22.360  69.361  53.044  1.000 35.371  ? 93  TYR LLL OH  1 
ATOM   3915  N N   . CYS C 3 94  ? 13.694  68.435  52.194  1.000 45.127  ? 94  CYS LLL N   1 
ATOM   3916  C CA  . CYS C 3 94  ? 12.477  68.201  51.381  1.000 45.867  ? 94  CYS LLL CA  1 
ATOM   3917  C C   . CYS C 3 94  ? 12.807  68.563  49.934  1.000 39.925  ? 94  CYS LLL C   1 
ATOM   3918  O O   . CYS C 3 94  ? 13.652  69.427  49.719  1.000 37.788  ? 94  CYS LLL O   1 
ATOM   3919  C CB  . CYS C 3 94  ? 11.270  68.971  51.909  1.000 56.997  ? 94  CYS LLL CB  1 
ATOM   3920  S SG  . CYS C 3 94  ? 11.409  70.782  51.903  1.000 69.979  ? 94  CYS LLL SG  1 
ATOM   3921  N N   . GLN C 3 95  ? 12.193  67.877  48.985  1.000 38.917  ? 95  GLN LLL N   1 
ATOM   3922  C CA  . GLN C 3 95  ? 12.378  68.116  47.536  1.000 42.468  ? 95  GLN LLL CA  1 
ATOM   3923  C C   . GLN C 3 95  ? 11.009  67.955  46.891  1.000 45.734  ? 95  GLN LLL C   1 
ATOM   3924  O O   . GLN C 3 95  ? 10.332  66.960  47.230  1.000 50.286  ? 95  GLN LLL O   1 
ATOM   3925  C CB  . GLN C 3 95  ? 13.360  67.110  46.930  1.000 46.345  ? 95  GLN LLL CB  1 
ATOM   3926  C CG  . GLN C 3 95  ? 13.588  67.240  45.423  1.000 48.345  ? 95  GLN LLL CG  1 
ATOM   3927  C CD  . GLN C 3 95  ? 13.512  65.915  44.696  1.000 47.878  ? 95  GLN LLL CD  1 
ATOM   3928  O OE1 . GLN C 3 95  ? 13.292  64.874  45.296  1.000 50.430  ? 95  GLN LLL OE1 1 
ATOM   3929  N NE2 . GLN C 3 95  ? 13.677  65.932  43.383  1.000 48.140  ? 95  GLN LLL NE2 1 
ATOM   3930  N N   . GLN C 3 96  ? 10.631  68.900  46.024  1.000 43.969  ? 96  GLN LLL N   1 
ATOM   3931  C CA  . GLN C 3 96  ? 9.459   68.784  45.125  1.000 46.352  ? 96  GLN LLL CA  1 
ATOM   3932  C C   . GLN C 3 96  ? 9.922   68.156  43.805  1.000 48.313  ? 96  GLN LLL C   1 
ATOM   3933  O O   . GLN C 3 96  ? 10.997  68.541  43.296  1.000 51.463  ? 96  GLN LLL O   1 
ATOM   3934  C CB  . GLN C 3 96  ? 8.795   70.147  44.923  1.000 47.471  ? 96  GLN LLL CB  1 
ATOM   3935  C CG  . GLN C 3 96  ? 9.603   71.136  44.099  1.000 48.083  ? 96  GLN LLL CG  1 
ATOM   3936  C CD  . GLN C 3 96  ? 9.415   70.999  42.605  1.000 49.674  ? 96  GLN LLL CD  1 
ATOM   3937  O OE1 . GLN C 3 96  ? 8.597   70.210  42.122  1.000 47.217  ? 96  GLN LLL OE1 1 
ATOM   3938  N NE2 . GLN C 3 96  ? 10.193  71.771  41.856  1.000 46.393  ? 96  GLN LLL NE2 1 
ATOM   3939  N N   . TYR C 3 97  ? 9.146   67.208  43.284  1.000 48.940  ? 97  TYR LLL N   1 
ATOM   3940  C CA  . TYR C 3 97  ? 9.336   66.624  41.933  1.000 52.036  ? 97  TYR LLL CA  1 
ATOM   3941  C C   . TYR C 3 97  ? 8.022   66.750  41.156  1.000 55.784  ? 97  TYR LLL C   1 
ATOM   3942  O O   . TYR C 3 97  ? 7.709   65.836  40.367  1.000 52.769  ? 97  TYR LLL O   1 
ATOM   3943  C CB  . TYR C 3 97  ? 9.843   65.186  42.048  1.000 51.464  ? 97  TYR LLL CB  1 
ATOM   3944  C CG  . TYR C 3 97  ? 9.025   64.237  42.889  1.000 48.778  ? 97  TYR LLL CG  1 
ATOM   3945  C CD1 . TYR C 3 97  ? 9.106   64.228  44.276  1.000 46.379  ? 97  TYR LLL CD1 1 
ATOM   3946  C CD2 . TYR C 3 97  ? 8.234   63.276  42.284  1.000 50.896  ? 97  TYR LLL CD2 1 
ATOM   3947  C CE1 . TYR C 3 97  ? 8.385   63.321  45.039  1.000 47.364  ? 97  TYR LLL CE1 1 
ATOM   3948  C CE2 . TYR C 3 97  ? 7.500   62.365  43.030  1.000 53.046  ? 97  TYR LLL CE2 1 
ATOM   3949  C CZ  . TYR C 3 97  ? 7.585   62.378  44.413  1.000 50.494  ? 97  TYR LLL CZ  1 
ATOM   3950  O OH  . TYR C 3 97  ? 6.876   61.450  45.123  1.000 45.389  ? 97  TYR LLL OH  1 
ATOM   3951  N N   . TYR C 3 98  ? 7.293   67.854  41.376  1.000 59.205  ? 98  TYR LLL N   1 
ATOM   3952  C CA  . TYR C 3 98  ? 6.022   68.179  40.679  1.000 62.303  ? 98  TYR LLL CA  1 
ATOM   3953  C C   . TYR C 3 98  ? 6.355   68.590  39.240  1.000 57.040  ? 98  TYR LLL C   1 
ATOM   3954  O O   . TYR C 3 98  ? 5.771   68.040  38.293  1.000 58.161  ? 98  TYR LLL O   1 
ATOM   3955  C CB  . TYR C 3 98  ? 5.232   69.269  41.417  1.000 68.672  ? 98  TYR LLL CB  1 
ATOM   3956  C CG  . TYR C 3 98  ? 3.995   69.721  40.680  1.000 74.772  ? 98  TYR LLL CG  1 
ATOM   3957  C CD1 . TYR C 3 98  ? 2.876   68.906  40.580  1.000 81.282  ? 98  TYR LLL CD1 1 
ATOM   3958  C CD2 . TYR C 3 98  ? 3.960   70.943  40.033  1.000 79.564  ? 98  TYR LLL CD2 1 
ATOM   3959  C CE1 . TYR C 3 98  ? 1.761   69.295  39.857  1.000 85.768  ? 98  TYR LLL CE1 1 
ATOM   3960  C CE2 . TYR C 3 98  ? 2.835   71.365  39.342  1.000 82.810  ? 98  TYR LLL CE2 1 
ATOM   3961  C CZ  . TYR C 3 98  ? 1.738   70.530  39.240  1.000 84.977  ? 98  TYR LLL CZ  1 
ATOM   3962  O OH  . TYR C 3 98  ? 0.638   70.925  38.541  1.000 87.334  ? 98  TYR LLL OH  1 
ATOM   3963  N N   . SER C 3 99  ? 7.294   69.523  39.089  1.000 52.435  ? 99  SER LLL N   1 
ATOM   3964  C CA  . SER C 3 99  ? 7.745   70.061  37.782  1.000 55.274  ? 99  SER LLL CA  1 
ATOM   3965  C C   . SER C 3 99  ? 9.256   70.331  37.799  1.000 54.041  ? 99  SER LLL C   1 
ATOM   3966  O O   . SER C 3 99  ? 9.767   70.781  38.847  1.000 52.235  ? 99  SER LLL O   1 
ATOM   3967  C CB  . SER C 3 99  ? 6.976   71.309  37.458  1.000 58.708  ? 99  SER LLL CB  1 
ATOM   3968  O OG  . SER C 3 99  ? 7.262   72.331  38.399  1.000 57.593  ? 99  SER LLL OG  1 
ATOM   3969  N N   . THR C 3 100 ? 9.946   70.084  36.682  1.000 48.925  ? 100 THR LLL N   1 
ATOM   3970  C CA  . THR C 3 100 ? 11.345  70.536  36.471  1.000 49.407  ? 100 THR LLL CA  1 
ATOM   3971  C C   . THR C 3 100 ? 11.282  72.050  36.340  1.000 51.141  ? 100 THR LLL C   1 
ATOM   3972  O O   . THR C 3 100 ? 10.365  72.543  35.691  1.000 54.946  ? 100 THR LLL O   1 
ATOM   3973  C CB  . THR C 3 100 ? 12.004  69.906  35.237  1.000 50.623  ? 100 THR LLL CB  1 
ATOM   3974  O OG1 . THR C 3 100 ? 11.493  70.531  34.060  1.000 52.277  ? 100 THR LLL OG1 1 
ATOM   3975  C CG2 . THR C 3 100 ? 11.807  68.410  35.167  1.000 50.118  ? 100 THR LLL CG2 1 
ATOM   3976  N N   . PRO C 3 101 ? 12.190  72.842  36.957  1.000 51.577  ? 101 PRO LLL N   1 
ATOM   3977  C CA  . PRO C 3 101 ? 13.325  72.326  37.719  1.000 51.831  ? 101 PRO LLL CA  1 
ATOM   3978  C C   . PRO C 3 101 ? 12.977  71.834  39.131  1.000 51.223  ? 101 PRO LLL C   1 
ATOM   3979  O O   . PRO C 3 101 ? 12.393  72.610  39.877  1.000 56.402  ? 101 PRO LLL O   1 
ATOM   3980  C CB  . PRO C 3 101 ? 14.222  73.569  37.844  1.000 53.098  ? 101 PRO LLL CB  1 
ATOM   3981  C CG  . PRO C 3 101 ? 13.249  74.716  37.926  1.000 52.495  ? 101 PRO LLL CG  1 
ATOM   3982  C CD  . PRO C 3 101 ? 12.134  74.312  36.982  1.000 54.292  ? 101 PRO LLL CD  1 
ATOM   3983  N N   . TYR C 3 102 ? 13.361  70.596  39.478  1.000 46.239  ? 102 TYR LLL N   1 
ATOM   3984  C CA  . TYR C 3 102 ? 13.203  70.060  40.854  1.000 44.879  ? 102 TYR LLL CA  1 
ATOM   3985  C C   . TYR C 3 102 ? 13.915  71.023  41.804  1.000 41.594  ? 102 TYR LLL C   1 
ATOM   3986  O O   . TYR C 3 102 ? 14.865  71.699  41.352  1.000 43.202  ? 102 TYR LLL O   1 
ATOM   3987  C CB  . TYR C 3 102 ? 13.804  68.669  41.030  1.000 46.028  ? 102 TYR LLL CB  1 
ATOM   3988  C CG  . TYR C 3 102 ? 13.276  67.545  40.173  1.000 51.944  ? 102 TYR LLL CG  1 
ATOM   3989  C CD1 . TYR C 3 102 ? 13.947  66.332  40.176  1.000 61.691  ? 102 TYR LLL CD1 1 
ATOM   3990  C CD2 . TYR C 3 102 ? 12.148  67.648  39.368  1.000 54.758  ? 102 TYR LLL CD2 1 
ATOM   3991  C CE1 . TYR C 3 102 ? 13.519  65.248  39.427  1.000 64.084  ? 102 TYR LLL CE1 1 
ATOM   3992  C CE2 . TYR C 3 102 ? 11.709  66.571  38.604  1.000 55.341  ? 102 TYR LLL CE2 1 
ATOM   3993  C CZ  . TYR C 3 102 ? 12.400  65.367  38.627  1.000 60.799  ? 102 TYR LLL CZ  1 
ATOM   3994  O OH  . TYR C 3 102 ? 12.032  64.271  37.899  1.000 66.007  ? 102 TYR LLL OH  1 
ATOM   3995  N N   . THR C 3 103 ? 13.476  71.108  43.057  1.000 38.776  ? 103 THR LLL N   1 
ATOM   3996  C CA  . THR C 3 103 ? 14.089  72.032  44.045  1.000 44.327  ? 103 THR LLL CA  1 
ATOM   3997  C C   . THR C 3 103 ? 14.065  71.420  45.446  1.000 42.312  ? 103 THR LLL C   1 
ATOM   3998  O O   . THR C 3 103 ? 13.116  70.708  45.764  1.000 48.479  ? 103 THR LLL O   1 
ATOM   3999  C CB  . THR C 3 103 ? 13.452  73.427  43.994  1.000 47.241  ? 103 THR LLL CB  1 
ATOM   4000  O OG1 . THR C 3 103 ? 12.035  73.271  43.985  1.000 49.726  ? 103 THR LLL OG1 1 
ATOM   4001  C CG2 . THR C 3 103 ? 13.909  74.233  42.791  1.000 47.200  ? 103 THR LLL CG2 1 
ATOM   4002  N N   . PHE C 3 104 ? 15.120  71.679  46.219  1.000 40.254  ? 104 PHE LLL N   1 
ATOM   4003  C CA  . PHE C 3 104 ? 15.341  71.164  47.588  1.000 38.070  ? 104 PHE LLL CA  1 
ATOM   4004  C C   . PHE C 3 104 ? 15.083  72.309  48.556  1.000 34.141  ? 104 PHE LLL C   1 
ATOM   4005  O O   . PHE C 3 104 ? 15.213  73.447  48.154  1.000 29.680  ? 104 PHE LLL O   1 
ATOM   4006  C CB  . PHE C 3 104 ? 16.775  70.646  47.778  1.000 40.533  ? 104 PHE LLL CB  1 
ATOM   4007  C CG  . PHE C 3 104 ? 17.135  69.382  47.023  1.000 41.000  ? 104 PHE LLL CG  1 
ATOM   4008  C CD1 . PHE C 3 104 ? 17.891  69.431  45.858  1.000 39.419  ? 104 PHE LLL CD1 1 
ATOM   4009  C CD2 . PHE C 3 104 ? 16.731  68.133  47.479  1.000 39.439  ? 104 PHE LLL CD2 1 
ATOM   4010  C CE1 . PHE C 3 104 ? 18.192  68.271  45.161  1.000 37.519  ? 104 PHE LLL CE1 1 
ATOM   4011  C CE2 . PHE C 3 104 ? 17.054  66.974  46.788  1.000 37.301  ? 104 PHE LLL CE2 1 
ATOM   4012  C CZ  . PHE C 3 104 ? 17.768  67.047  45.621  1.000 37.121  ? 104 PHE LLL CZ  1 
ATOM   4013  N N   . GLY C 3 105 ? 14.735  71.983  49.797  1.000 37.771  ? 105 GLY LLL N   1 
ATOM   4014  C CA  . GLY C 3 105 ? 14.786  72.911  50.938  1.000 40.668  ? 105 GLY LLL CA  1 
ATOM   4015  C C   . GLY C 3 105 ? 16.223  73.253  51.277  1.000 45.745  ? 105 GLY LLL C   1 
ATOM   4016  O O   . GLY C 3 105 ? 17.141  72.600  50.721  1.000 45.870  ? 105 GLY LLL O   1 
ATOM   4017  N N   . GLN C 3 106 ? 16.429  74.237  52.154  1.000 50.184  ? 106 GLN LLL N   1 
ATOM   4018  C CA  . GLN C 3 106 ? 17.791  74.666  52.573  1.000 57.215  ? 106 GLN LLL CA  1 
ATOM   4019  C C   . GLN C 3 106 ? 18.403  73.588  53.474  1.000 51.027  ? 106 GLN LLL C   1 
ATOM   4020  O O   . GLN C 3 106 ? 19.634  73.560  53.612  1.000 52.358  ? 106 GLN LLL O   1 
ATOM   4021  C CB  . GLN C 3 106 ? 17.763  76.053  53.228  1.000 66.879  ? 106 GLN LLL CB  1 
ATOM   4022  C CG  . GLN C 3 106 ? 17.240  76.090  54.658  1.000 68.352  ? 106 GLN LLL CG  1 
ATOM   4023  C CD  . GLN C 3 106 ? 15.738  76.145  54.739  1.000 76.093  ? 106 GLN LLL CD  1 
ATOM   4024  O OE1 . GLN C 3 106 ? 15.035  76.223  53.729  1.000 82.567  ? 106 GLN LLL OE1 1 
ATOM   4025  N NE2 . GLN C 3 106 ? 15.236  76.101  55.962  1.000 81.183  ? 106 GLN LLL NE2 1 
ATOM   4026  N N   . GLY C 3 107 ? 17.570  72.723  54.049  1.000 46.982  ? 107 GLY LLL N   1 
ATOM   4027  C CA  . GLY C 3 107 ? 18.008  71.598  54.896  1.000 44.926  ? 107 GLY LLL CA  1 
ATOM   4028  C C   . GLY C 3 107 ? 17.726  71.869  56.361  1.000 43.649  ? 107 GLY LLL C   1 
ATOM   4029  O O   . GLY C 3 107 ? 17.699  73.040  56.749  1.000 49.363  ? 107 GLY LLL O   1 
ATOM   4030  N N   . THR C 3 108 ? 17.536  70.819  57.156  1.000 42.360  ? 108 THR LLL N   1 
ATOM   4031  C CA  . THR C 3 108 ? 17.305  70.920  58.616  1.000 44.055  ? 108 THR LLL CA  1 
ATOM   4032  C C   . THR C 3 108 ? 18.278  70.002  59.355  1.000 44.171  ? 108 THR LLL C   1 
ATOM   4033  O O   . THR C 3 108 ? 18.111  68.771  59.273  1.000 42.480  ? 108 THR LLL O   1 
ATOM   4034  C CB  . THR C 3 108 ? 15.845  70.604  58.931  1.000 50.250  ? 108 THR LLL CB  1 
ATOM   4035  O OG1 . THR C 3 108 ? 15.097  71.646  58.300  1.000 52.319  ? 108 THR LLL OG1 1 
ATOM   4036  C CG2 . THR C 3 108 ? 15.561  70.521  60.416  1.000 50.792  ? 108 THR LLL CG2 1 
ATOM   4037  N N   . LYS C 3 109 ? 19.253  70.613  60.033  1.000 46.169  ? 109 LYS LLL N   1 
ATOM   4038  C CA  . LYS C 3 109 ? 20.272  69.956  60.887  1.000 49.886  ? 109 LYS LLL CA  1 
ATOM   4039  C C   . LYS C 3 109 ? 19.561  69.381  62.118  1.000 46.267  ? 109 LYS LLL C   1 
ATOM   4040  O O   . LYS C 3 109 ? 18.871  70.146  62.801  1.000 48.519  ? 109 LYS LLL O   1 
ATOM   4041  C CB  . LYS C 3 109 ? 21.360  70.990  61.223  1.000 58.437  ? 109 LYS LLL CB  1 
ATOM   4042  C CG  . LYS C 3 109 ? 22.384  70.602  62.284  1.000 68.033  ? 109 LYS LLL CG  1 
ATOM   4043  C CD  . LYS C 3 109 ? 23.350  69.519  61.821  1.000 77.928  ? 109 LYS LLL CD  1 
ATOM   4044  C CE  . LYS C 3 109 ? 23.998  68.719  62.938  1.000 78.990  ? 109 LYS LLL CE  1 
ATOM   4045  N NZ  . LYS C 3 109 ? 24.037  67.263  62.625  1.000 74.090  ? 109 LYS LLL NZ  1 
ATOM   4046  N N   . VAL C 3 110 ? 19.700  68.082  62.385  1.000 42.618  ? 110 VAL LLL N   1 
ATOM   4047  C CA  . VAL C 3 110 ? 19.094  67.409  63.573  1.000 42.368  ? 110 VAL LLL CA  1 
ATOM   4048  C C   . VAL C 3 110 ? 20.212  66.871  64.476  1.000 45.392  ? 110 VAL LLL C   1 
ATOM   4049  O O   . VAL C 3 110 ? 20.975  66.002  64.011  1.000 55.194  ? 110 VAL LLL O   1 
ATOM   4050  C CB  . VAL C 3 110 ? 18.125  66.294  63.144  1.000 41.519  ? 110 VAL LLL CB  1 
ATOM   4051  C CG1 . VAL C 3 110 ? 17.636  65.478  64.333  1.000 40.556  ? 110 VAL LLL CG1 1 
ATOM   4052  C CG2 . VAL C 3 110 ? 16.942  66.850  62.370  1.000 42.296  ? 110 VAL LLL CG2 1 
ATOM   4053  N N   . GLU C 3 111 ? 20.295  67.362  65.719  1.000 45.551  ? 111 GLU LLL N   1 
ATOM   4054  C CA  . GLU C 3 111 ? 21.282  66.934  66.746  1.000 48.696  ? 111 GLU LLL CA  1 
ATOM   4055  C C   . GLU C 3 111 ? 20.545  66.108  67.794  1.000 46.937  ? 111 GLU LLL C   1 
ATOM   4056  O O   . GLU C 3 111 ? 19.328  66.294  67.912  1.000 53.153  ? 111 GLU LLL O   1 
ATOM   4057  C CB  . GLU C 3 111 ? 21.932  68.102  67.507  1.000 59.054  ? 111 GLU LLL CB  1 
ATOM   4058  C CG  . GLU C 3 111 ? 21.894  69.465  66.823  1.000 68.691  ? 111 GLU LLL CG  1 
ATOM   4059  C CD  . GLU C 3 111 ? 22.617  70.605  67.551  1.000 77.149  ? 111 GLU LLL CD  1 
ATOM   4060  O OE1 . GLU C 3 111 ? 23.069  70.416  68.704  1.000 68.915  ? 111 GLU LLL OE1 1 
ATOM   4061  O OE2 . GLU C 3 111 ? 22.715  71.708  66.964  1.000 89.496  ? 111 GLU LLL OE2 1 
ATOM   4062  N N   . ILE C 3 112 ? 21.267  65.293  68.556  1.000 46.271  ? 112 ILE LLL N   1 
ATOM   4063  C CA  . ILE C 3 112 ? 20.806  64.752  69.872  1.000 50.649  ? 112 ILE LLL CA  1 
ATOM   4064  C C   . ILE C 3 112 ? 20.918  65.862  70.920  1.000 52.673  ? 112 ILE LLL C   1 
ATOM   4065  O O   . ILE C 3 112 ? 22.013  66.432  71.041  1.000 58.062  ? 112 ILE LLL O   1 
ATOM   4066  C CB  . ILE C 3 112 ? 21.664  63.544  70.303  1.000 53.218  ? 112 ILE LLL CB  1 
ATOM   4067  C CG1 . ILE C 3 112 ? 21.609  62.409  69.278  1.000 54.480  ? 112 ILE LLL CG1 1 
ATOM   4068  C CG2 . ILE C 3 112 ? 21.284  63.076  71.707  1.000 49.762  ? 112 ILE LLL CG2 1 
ATOM   4069  C CD1 . ILE C 3 112 ? 20.196  61.947  68.954  1.000 62.391  ? 112 ILE LLL CD1 1 
ATOM   4070  N N   . LYS C 3 113 ? 19.853  66.135  71.674  1.000 56.898  ? 113 LYS LLL N   1 
ATOM   4071  C CA  . LYS C 3 113 ? 19.922  67.000  72.881  1.000 59.038  ? 113 LYS LLL CA  1 
ATOM   4072  C C   . LYS C 3 113 ? 20.195  66.116  74.092  1.000 53.161  ? 113 LYS LLL C   1 
ATOM   4073  O O   . LYS C 3 113 ? 19.449  65.144  74.297  1.000 62.553  ? 113 LYS LLL O   1 
ATOM   4074  C CB  . LYS C 3 113 ? 18.636  67.794  73.137  1.000 65.434  ? 113 LYS LLL CB  1 
ATOM   4075  C CG  . LYS C 3 113 ? 18.783  68.813  74.261  1.000 74.357  ? 113 LYS LLL CG  1 
ATOM   4076  C CD  . LYS C 3 113 ? 17.642  69.769  74.428  1.000 78.653  ? 113 LYS LLL CD  1 
ATOM   4077  C CE  . LYS C 3 113 ? 16.689  69.324  75.511  1.000 84.557  ? 113 LYS LLL CE  1 
ATOM   4078  N NZ  . LYS C 3 113 ? 15.608  70.323  75.678  1.000 93.684  ? 113 LYS LLL NZ  1 
ATOM   4079  N N   . ARG C 3 114 ? 21.212  66.469  74.866  1.000 50.961  ? 114 ARG LLL N   1 
ATOM   4080  C CA  . ARG C 3 114 ? 21.540  65.814  76.156  1.000 54.237  ? 114 ARG LLL CA  1 
ATOM   4081  C C   . ARG C 3 114 ? 21.735  66.917  77.199  1.000 56.676  ? 114 ARG LLL C   1 
ATOM   4082  O O   . ARG C 3 114 ? 21.581  68.113  76.841  1.000 47.345  ? 114 ARG LLL O   1 
ATOM   4083  C CB  . ARG C 3 114 ? 22.807  64.972  76.012  1.000 52.805  ? 114 ARG LLL CB  1 
ATOM   4084  C CG  . ARG C 3 114 ? 23.948  65.718  75.328  1.000 53.118  ? 114 ARG LLL CG  1 
ATOM   4085  C CD  . ARG C 3 114 ? 25.316  65.252  75.766  1.000 52.204  ? 114 ARG LLL CD  1 
ATOM   4086  N NE  . ARG C 3 114 ? 25.482  65.530  77.184  1.000 54.346  ? 114 ARG LLL NE  1 
ATOM   4087  C CZ  . ARG C 3 114 ? 26.384  64.962  77.977  1.000 54.195  ? 114 ARG LLL CZ  1 
ATOM   4088  N NH1 . ARG C 3 114 ? 27.246  64.070  77.513  1.000 51.811  ? 114 ARG LLL NH1 1 
ATOM   4089  N NH2 . ARG C 3 114 ? 26.416  65.300  79.252  1.000 59.905  ? 114 ARG LLL NH2 1 
ATOM   4090  N N   . THR C 3 115 ? 22.064  66.535  78.435  1.000 60.008  ? 115 THR LLL N   1 
ATOM   4091  C CA  . THR C 3 115 ? 22.353  67.494  79.534  1.000 63.298  ? 115 THR LLL CA  1 
ATOM   4092  C C   . THR C 3 115 ? 23.581  68.316  79.148  1.000 65.035  ? 115 THR LLL C   1 
ATOM   4093  O O   . THR C 3 115 ? 24.477  67.772  78.449  1.000 66.711  ? 115 THR LLL O   1 
ATOM   4094  C CB  . THR C 3 115 ? 22.586  66.810  80.887  1.000 64.108  ? 115 THR LLL CB  1 
ATOM   4095  O OG1 . THR C 3 115 ? 23.438  65.687  80.641  1.000 57.490  ? 115 THR LLL OG1 1 
ATOM   4096  C CG2 . THR C 3 115 ? 21.287  66.423  81.571  1.000 65.223  ? 115 THR LLL CG2 1 
ATOM   4097  N N   . VAL C 3 116 ? 23.607  69.570  79.601  1.000 58.664  ? 116 VAL LLL N   1 
ATOM   4098  C CA  . VAL C 3 116 ? 24.779  70.468  79.430  1.000 52.934  ? 116 VAL LLL CA  1 
ATOM   4099  C C   . VAL C 3 116 ? 26.011  69.745  79.984  1.000 47.650  ? 116 VAL LLL C   1 
ATOM   4100  O O   . VAL C 3 116 ? 25.901  69.047  81.004  1.000 37.084  ? 116 VAL LLL O   1 
ATOM   4101  C CB  . VAL C 3 116 ? 24.539  71.826  80.104  1.000 52.984  ? 116 VAL LLL CB  1 
ATOM   4102  C CG1 . VAL C 3 116 ? 25.742  72.752  79.968  1.000 52.611  ? 116 VAL LLL CG1 1 
ATOM   4103  C CG2 . VAL C 3 116 ? 23.297  72.490  79.525  1.000 54.329  ? 116 VAL LLL CG2 1 
ATOM   4104  N N   . ALA C 3 117 ? 27.125  69.862  79.272  1.000 48.916  ? 117 ALA LLL N   1 
ATOM   4105  C CA  . ALA C 3 117 ? 28.455  69.382  79.695  1.000 52.964  ? 117 ALA LLL CA  1 
ATOM   4106  C C   . ALA C 3 117 ? 29.484  70.468  79.359  1.000 54.140  ? 117 ALA LLL C   1 
ATOM   4107  O O   . ALA C 3 117 ? 29.529  70.892  78.187  1.000 55.890  ? 117 ALA LLL O   1 
ATOM   4108  C CB  . ALA C 3 117 ? 28.765  68.072  79.013  1.000 53.527  ? 117 ALA LLL CB  1 
ATOM   4109  N N   . ALA C 3 118 ? 30.249  70.918  80.356  1.000 51.754  ? 118 ALA LLL N   1 
ATOM   4110  C CA  . ALA C 3 118 ? 31.238  72.010  80.210  1.000 50.882  ? 118 ALA LLL CA  1 
ATOM   4111  C C   . ALA C 3 118 ? 32.426  71.468  79.441  1.000 48.876  ? 118 ALA LLL C   1 
ATOM   4112  O O   . ALA C 3 118 ? 32.715  70.281  79.546  1.000 46.055  ? 118 ALA LLL O   1 
ATOM   4113  C CB  . ALA C 3 118 ? 31.682  72.524  81.553  1.000 53.914  ? 118 ALA LLL CB  1 
ATOM   4114  N N   . PRO C 3 119 ? 33.124  72.309  78.640  1.000 47.936  ? 119 PRO LLL N   1 
ATOM   4115  C CA  . PRO C 3 119 ? 34.330  71.873  77.945  1.000 46.229  ? 119 PRO LLL CA  1 
ATOM   4116  C C   . PRO C 3 119 ? 35.529  71.800  78.896  1.000 47.023  ? 119 PRO LLL C   1 
ATOM   4117  O O   . PRO C 3 119 ? 35.666  72.670  79.732  1.000 46.242  ? 119 PRO LLL O   1 
ATOM   4118  C CB  . PRO C 3 119 ? 34.516  72.938  76.854  1.000 43.823  ? 119 PRO LLL CB  1 
ATOM   4119  C CG  . PRO C 3 119 ? 33.913  74.180  77.443  1.000 42.532  ? 119 PRO LLL CG  1 
ATOM   4120  C CD  . PRO C 3 119 ? 32.770  73.697  78.313  1.000 44.541  ? 119 PRO LLL CD  1 
ATOM   4121  N N   . SER C 3 120 ? 36.336  70.742  78.755  1.000 50.332  ? 120 SER LLL N   1 
ATOM   4122  C CA  . SER C 3 120 ? 37.745  70.686  79.220  1.000 51.320  ? 120 SER LLL CA  1 
ATOM   4123  C C   . SER C 3 120 ? 38.565  71.563  78.271  1.000 53.637  ? 120 SER LLL C   1 
ATOM   4124  O O   . SER C 3 120 ? 38.514  71.300  77.046  1.000 54.952  ? 120 SER LLL O   1 
ATOM   4125  C CB  . SER C 3 120 ? 38.279  69.279  79.255  1.000 50.695  ? 120 SER LLL CB  1 
ATOM   4126  O OG  . SER C 3 120 ? 37.806  68.572  80.382  1.000 58.717  ? 120 SER LLL OG  1 
ATOM   4127  N N   . VAL C 3 121 ? 39.276  72.558  78.811  1.000 51.221  ? 121 VAL LLL N   1 
ATOM   4128  C CA  . VAL C 3 121 ? 40.074  73.515  77.998  1.000 48.221  ? 121 VAL LLL CA  1 
ATOM   4129  C C   . VAL C 3 121 ? 41.566  73.183  78.109  1.000 45.925  ? 121 VAL LLL C   1 
ATOM   4130  O O   . VAL C 3 121 ? 42.052  72.898  79.214  1.000 44.238  ? 121 VAL LLL O   1 
ATOM   4131  C CB  . VAL C 3 121 ? 39.779  74.961  78.407  1.000 48.575  ? 121 VAL LLL CB  1 
ATOM   4132  C CG1 . VAL C 3 121 ? 40.398  75.940  77.417  1.000 50.163  ? 121 VAL LLL CG1 1 
ATOM   4133  C CG2 . VAL C 3 121 ? 38.281  75.185  78.540  1.000 49.148  ? 121 VAL LLL CG2 1 
ATOM   4134  N N   . PHE C 3 122 ? 42.248  73.194  76.970  1.000 45.327  ? 122 PHE LLL N   1 
ATOM   4135  C CA  . PHE C 3 122 ? 43.707  72.975  76.854  1.000 48.460  ? 122 PHE LLL CA  1 
ATOM   4136  C C   . PHE C 3 122 ? 44.256  73.971  75.842  1.000 44.080  ? 122 PHE LLL C   1 
ATOM   4137  O O   . PHE C 3 122 ? 43.595  74.198  74.812  1.000 44.383  ? 122 PHE LLL O   1 
ATOM   4138  C CB  . PHE C 3 122 ? 44.017  71.555  76.373  1.000 52.714  ? 122 PHE LLL CB  1 
ATOM   4139  C CG  . PHE C 3 122 ? 43.418  70.471  77.222  1.000 50.075  ? 122 PHE LLL CG  1 
ATOM   4140  C CD1 . PHE C 3 122 ? 42.171  69.955  76.917  1.000 45.436  ? 122 PHE LLL CD1 1 
ATOM   4141  C CD2 . PHE C 3 122 ? 44.104  69.981  78.324  1.000 54.009  ? 122 PHE LLL CD2 1 
ATOM   4142  C CE1 . PHE C 3 122 ? 41.621  68.960  77.700  1.000 47.181  ? 122 PHE LLL CE1 1 
ATOM   4143  C CE2 . PHE C 3 122 ? 43.539  68.999  79.118  1.000 55.236  ? 122 PHE LLL CE2 1 
ATOM   4144  C CZ  . PHE C 3 122 ? 42.301  68.487  78.801  1.000 52.158  ? 122 PHE LLL CZ  1 
ATOM   4145  N N   . ILE C 3 123 ? 45.450  74.488  76.101  1.000 40.602  ? 123 ILE LLL N   1 
ATOM   4146  C CA  . ILE C 3 123 ? 46.114  75.459  75.191  1.000 40.788  ? 123 ILE LLL CA  1 
ATOM   4147  C C   . ILE C 3 123 ? 47.504  74.941  74.850  1.000 36.162  ? 123 ILE LLL C   1 
ATOM   4148  O O   . ILE C 3 123 ? 48.199  74.527  75.754  1.000 38.684  ? 123 ILE LLL O   1 
ATOM   4149  C CB  . ILE C 3 123 ? 46.167  76.852  75.835  1.000 43.086  ? 123 ILE LLL CB  1 
ATOM   4150  C CG1 . ILE C 3 123 ? 46.683  77.895  74.844  1.000 45.555  ? 123 ILE LLL CG1 1 
ATOM   4151  C CG2 . ILE C 3 123 ? 46.974  76.827  77.125  1.000 42.408  ? 123 ILE LLL CG2 1 
ATOM   4152  C CD1 . ILE C 3 123 ? 46.680  79.287  75.393  1.000 49.060  ? 123 ILE LLL CD1 1 
ATOM   4153  N N   . PHE C 3 124 ? 47.874  74.967  73.581  1.000 32.854  ? 124 PHE LLL N   1 
ATOM   4154  C CA  . PHE C 3 124 ? 49.165  74.445  73.100  1.000 33.767  ? 124 PHE LLL CA  1 
ATOM   4155  C C   . PHE C 3 124 ? 49.955  75.597  72.516  1.000 33.809  ? 124 PHE LLL C   1 
ATOM   4156  O O   . PHE C 3 124 ? 49.496  76.272  71.602  1.000 34.844  ? 124 PHE LLL O   1 
ATOM   4157  C CB  . PHE C 3 124 ? 48.931  73.343  72.072  1.000 36.097  ? 124 PHE LLL CB  1 
ATOM   4158  C CG  . PHE C 3 124 ? 48.089  72.214  72.594  1.000 37.277  ? 124 PHE LLL CG  1 
ATOM   4159  C CD1 . PHE C 3 124 ? 48.598  71.348  73.544  1.000 39.293  ? 124 PHE LLL CD1 1 
ATOM   4160  C CD2 . PHE C 3 124 ? 46.792  72.040  72.157  1.000 38.691  ? 124 PHE LLL CD2 1 
ATOM   4161  C CE1 . PHE C 3 124 ? 47.832  70.306  74.035  1.000 42.214  ? 124 PHE LLL CE1 1 
ATOM   4162  C CE2 . PHE C 3 124 ? 46.021  71.002  72.652  1.000 42.036  ? 124 PHE LLL CE2 1 
ATOM   4163  C CZ  . PHE C 3 124 ? 46.540  70.140  73.594  1.000 44.056  ? 124 PHE LLL CZ  1 
ATOM   4164  N N   . PRO C 3 125 ? 51.177  75.841  73.011  1.000 34.720  ? 125 PRO LLL N   1 
ATOM   4165  C CA  . PRO C 3 125 ? 52.064  76.808  72.384  1.000 36.797  ? 125 PRO LLL CA  1 
ATOM   4166  C C   . PRO C 3 125 ? 52.558  76.233  71.068  1.000 38.857  ? 125 PRO LLL C   1 
ATOM   4167  O O   . PRO C 3 125 ? 52.418  75.046  70.811  1.000 37.716  ? 125 PRO LLL O   1 
ATOM   4168  C CB  . PRO C 3 125 ? 53.205  76.940  73.389  1.000 36.482  ? 125 PRO LLL CB  1 
ATOM   4169  C CG  . PRO C 3 125 ? 53.251  75.586  74.033  1.000 37.611  ? 125 PRO LLL CG  1 
ATOM   4170  C CD  . PRO C 3 125 ? 51.795  75.176  74.160  1.000 36.556  ? 125 PRO LLL CD  1 
ATOM   4171  N N   . PRO C 3 126 ? 53.133  77.057  70.183  1.000 42.481  ? 126 PRO LLL N   1 
ATOM   4172  C CA  . PRO C 3 126 ? 53.722  76.539  68.958  1.000 46.528  ? 126 PRO LLL CA  1 
ATOM   4173  C C   . PRO C 3 126 ? 54.985  75.728  69.269  1.000 48.106  ? 126 PRO LLL C   1 
ATOM   4174  O O   . PRO C 3 126 ? 55.636  75.972  70.256  1.000 42.161  ? 126 PRO LLL O   1 
ATOM   4175  C CB  . PRO C 3 126 ? 53.997  77.796  68.118  1.000 48.589  ? 126 PRO LLL CB  1 
ATOM   4176  C CG  . PRO C 3 126 ? 54.088  78.920  69.131  1.000 46.729  ? 126 PRO LLL CG  1 
ATOM   4177  C CD  . PRO C 3 126 ? 53.196  78.515  70.286  1.000 43.842  ? 126 PRO LLL CD  1 
ATOM   4178  N N   . SER C 3 127 ? 55.239  74.733  68.424  1.000 57.394  ? 127 SER LLL N   1 
ATOM   4179  C CA  . SER C 3 127 ? 56.444  73.867  68.417  1.000 58.317  ? 127 SER LLL CA  1 
ATOM   4180  C C   . SER C 3 127 ? 57.665  74.719  68.086  1.000 60.363  ? 127 SER LLL C   1 
ATOM   4181  O O   . SER C 3 127 ? 57.519  75.700  67.311  1.000 55.107  ? 127 SER LLL O   1 
ATOM   4182  C CB  . SER C 3 127 ? 56.278  72.788  67.393  1.000 60.195  ? 127 SER LLL CB  1 
ATOM   4183  O OG  . SER C 3 127 ? 55.755  73.342  66.187  1.000 60.966  ? 127 SER LLL OG  1 
ATOM   4184  N N   . ASP C 3 128 ? 58.830  74.339  68.609  1.000 61.175  ? 128 ASP LLL N   1 
ATOM   4185  C CA  . ASP C 3 128 ? 60.117  74.997  68.265  1.000 58.820  ? 128 ASP LLL CA  1 
ATOM   4186  C C   . ASP C 3 128 ? 60.355  74.808  66.768  1.000 54.702  ? 128 ASP LLL C   1 
ATOM   4187  O O   . ASP C 3 128 ? 60.851  75.762  66.120  1.000 50.441  ? 128 ASP LLL O   1 
ATOM   4188  C CB  . ASP C 3 128 ? 61.250  74.454  69.141  1.000 66.315  ? 128 ASP LLL CB  1 
ATOM   4189  C CG  . ASP C 3 128 ? 61.220  74.961  70.584  1.000 75.615  ? 128 ASP LLL CG  1 
ATOM   4190  O OD1 . ASP C 3 128 ? 60.670  76.062  70.801  1.000 80.732  ? 128 ASP LLL OD1 1 
ATOM   4191  O OD2 . ASP C 3 128 ? 61.730  74.251  71.490  1.000 80.603  ? 128 ASP LLL OD2 1 
ATOM   4192  N N   . GLU C 3 129 ? 59.973  73.630  66.253  1.000 57.371  ? 129 GLU LLL N   1 
ATOM   4193  C CA  . GLU C 3 129 ? 60.155  73.205  64.837  1.000 57.018  ? 129 GLU LLL CA  1 
ATOM   4194  C C   . GLU C 3 129 ? 59.381  74.166  63.916  1.000 52.774  ? 129 GLU LLL C   1 
ATOM   4195  O O   . GLU C 3 129 ? 59.953  74.604  62.901  1.000 47.304  ? 129 GLU LLL O   1 
ATOM   4196  C CB  . GLU C 3 129 ? 59.734  71.737  64.674  1.000 61.487  ? 129 GLU LLL CB  1 
ATOM   4197  C CG  . GLU C 3 129 ? 60.315  71.058  63.429  1.000 68.282  ? 129 GLU LLL CG  1 
ATOM   4198  C CD  . GLU C 3 129 ? 59.404  70.028  62.754  1.000 74.069  ? 129 GLU LLL CD  1 
ATOM   4199  O OE1 . GLU C 3 129 ? 58.644  69.348  63.488  1.000 73.900  ? 129 GLU LLL OE1 1 
ATOM   4200  O OE2 . GLU C 3 129 ? 59.430  69.918  61.490  1.000 67.109  ? 129 GLU LLL OE2 1 
ATOM   4201  N N   . GLN C 3 130 ? 58.139  74.520  64.258  1.000 52.419  ? 130 GLN LLL N   1 
ATOM   4202  C CA  . GLN C 3 130 ? 57.316  75.429  63.414  1.000 53.093  ? 130 GLN LLL CA  1 
ATOM   4203  C C   . GLN C 3 130 ? 57.952  76.820  63.395  1.000 54.694  ? 130 GLN LLL C   1 
ATOM   4204  O O   . GLN C 3 130 ? 57.883  77.484  62.346  1.000 57.978  ? 130 GLN LLL O   1 
ATOM   4205  C CB  . GLN C 3 130 ? 55.869  75.532  63.908  1.000 50.402  ? 130 GLN LLL CB  1 
ATOM   4206  C CG  . GLN C 3 130 ? 54.976  76.360  62.984  1.000 46.316  ? 130 GLN LLL CG  1 
ATOM   4207  C CD  . GLN C 3 130 ? 53.576  76.505  63.526  1.000 44.927  ? 130 GLN LLL CD  1 
ATOM   4208  O OE1 . GLN C 3 130 ? 53.328  76.252  64.708  1.000 41.341  ? 130 GLN LLL OE1 1 
ATOM   4209  N NE2 . GLN C 3 130 ? 52.654  76.916  62.661  1.000 41.255  ? 130 GLN LLL NE2 1 
ATOM   4210  N N   . LEU C 3 131 ? 58.513  77.258  64.524  1.000 58.108  ? 131 LEU LLL N   1 
ATOM   4211  C CA  . LEU C 3 131 ? 59.049  78.633  64.677  1.000 58.169  ? 131 LEU LLL CA  1 
ATOM   4212  C C   . LEU C 3 131 ? 60.232  78.810  63.724  1.000 61.172  ? 131 LEU LLL C   1 
ATOM   4213  O O   . LEU C 3 131 ? 60.377  79.924  63.182  1.000 56.647  ? 131 LEU LLL O   1 
ATOM   4214  C CB  . LEU C 3 131 ? 59.458  78.871  66.133  1.000 59.418  ? 131 LEU LLL CB  1 
ATOM   4215  C CG  . LEU C 3 131 ? 58.311  79.120  67.108  1.000 57.262  ? 131 LEU LLL CG  1 
ATOM   4216  C CD1 . LEU C 3 131 ? 58.793  79.023  68.551  1.000 54.317  ? 131 LEU LLL CD1 1 
ATOM   4217  C CD2 . LEU C 3 131 ? 57.665  80.469  66.838  1.000 57.331  ? 131 LEU LLL CD2 1 
ATOM   4218  N N   . LYS C 3 132 ? 61.027  77.755  63.515  1.000 64.710  ? 132 LYS LLL N   1 
ATOM   4219  C CA  . LYS C 3 132 ? 62.132  77.769  62.522  1.000 72.416  ? 132 LYS LLL CA  1 
ATOM   4220  C C   . LYS C 3 132 ? 61.586  78.110  61.129  1.000 75.213  ? 132 LYS LLL C   1 
ATOM   4221  O O   . LYS C 3 132 ? 62.261  78.873  60.415  1.000 77.202  ? 132 LYS LLL O   1 
ATOM   4222  C CB  . LYS C 3 132 ? 62.877  76.434  62.513  1.000 75.156  ? 132 LYS LLL CB  1 
ATOM   4223  C CG  . LYS C 3 132 ? 63.848  76.257  63.670  1.000 83.272  ? 132 LYS LLL CG  1 
ATOM   4224  C CD  . LYS C 3 132 ? 64.773  75.059  63.527  1.000 84.514  ? 132 LYS LLL CD  1 
ATOM   4225  C CE  . LYS C 3 132 ? 64.140  73.774  64.016  1.000 86.493  ? 132 LYS LLL CE  1 
ATOM   4226  N NZ  . LYS C 3 132 ? 65.148  72.701  64.145  1.000 90.620  ? 132 LYS LLL NZ  1 
ATOM   4227  N N   . SER C 3 133 ? 60.418  77.575  60.756  1.000 76.489  ? 133 SER LLL N   1 
ATOM   4228  C CA  . SER C 3 133 ? 59.794  77.787  59.424  1.000 76.441  ? 133 SER LLL CA  1 
ATOM   4229  C C   . SER C 3 133 ? 59.300  79.238  59.280  1.000 80.161  ? 133 SER LLL C   1 
ATOM   4230  O O   . SER C 3 133 ? 59.092  79.668  58.132  1.000 87.151  ? 133 SER LLL O   1 
ATOM   4231  C CB  . SER C 3 133 ? 58.688  76.789  59.171  1.000 78.344  ? 133 SER LLL CB  1 
ATOM   4232  O OG  . SER C 3 133 ? 57.536  77.079  59.956  1.000 85.790  ? 133 SER LLL OG  1 
ATOM   4233  N N   . GLY C 3 134 ? 59.093  79.963  60.388  1.000 79.620  ? 134 GLY LLL N   1 
ATOM   4234  C CA  . GLY C 3 134 ? 58.793  81.412  60.380  1.000 76.569  ? 134 GLY LLL CA  1 
ATOM   4235  C C   . GLY C 3 134 ? 57.313  81.744  60.526  1.000 71.475  ? 134 GLY LLL C   1 
ATOM   4236  O O   . GLY C 3 134 ? 56.972  82.933  60.336  1.000 69.218  ? 134 GLY LLL O   1 
ATOM   4237  N N   . THR C 3 135 ? 56.451  80.765  60.842  1.000 68.099  ? 135 THR LLL N   1 
ATOM   4238  C CA  . THR C 3 135 ? 55.078  81.016  61.373  1.000 66.409  ? 135 THR LLL CA  1 
ATOM   4239  C C   . THR C 3 135 ? 54.942  80.371  62.760  1.000 54.609  ? 135 THR LLL C   1 
ATOM   4240  O O   . THR C 3 135 ? 55.859  79.630  63.183  1.000 49.091  ? 135 THR LLL O   1 
ATOM   4241  C CB  . THR C 3 135 ? 53.963  80.576  60.410  1.000 74.812  ? 135 THR LLL CB  1 
ATOM   4242  O OG1 . THR C 3 135 ? 54.072  79.158  60.249  1.000 88.525  ? 135 THR LLL OG1 1 
ATOM   4243  C CG2 . THR C 3 135 ? 54.009  81.296  59.073  1.000 70.441  ? 135 THR LLL CG2 1 
ATOM   4244  N N   . ALA C 3 136 ? 53.851  80.695  63.458  1.000 46.842  ? 136 ALA LLL N   1 
ATOM   4245  C CA  . ALA C 3 136 ? 53.541  80.222  64.828  1.000 45.596  ? 136 ALA LLL CA  1 
ATOM   4246  C C   . ALA C 3 136 ? 52.038  79.977  64.938  1.000 44.514  ? 136 ALA LLL C   1 
ATOM   4247  O O   . ALA C 3 136 ? 51.267  80.869  64.610  1.000 45.845  ? 136 ALA LLL O   1 
ATOM   4248  C CB  . ALA C 3 136 ? 53.997  81.204  65.865  1.000 45.257  ? 136 ALA LLL CB  1 
ATOM   4249  N N   . SER C 3 137 ? 51.657  78.770  65.334  1.000 42.887  ? 137 SER LLL N   1 
ATOM   4250  C CA  . SER C 3 137 ? 50.247  78.366  65.509  1.000 41.279  ? 137 SER LLL CA  1 
ATOM   4251  C C   . SER C 3 137 ? 50.026  78.056  66.993  1.000 40.315  ? 137 SER LLL C   1 
ATOM   4252  O O   . SER C 3 137 ? 50.714  77.190  67.541  1.000 44.039  ? 137 SER LLL O   1 
ATOM   4253  C CB  . SER C 3 137 ? 49.899  77.215  64.594  1.000 40.899  ? 137 SER LLL CB  1 
ATOM   4254  O OG  . SER C 3 137 ? 49.856  77.631  63.234  1.000 38.857  ? 137 SER LLL OG  1 
ATOM   4255  N N   . VAL C 3 138 ? 49.131  78.795  67.630  1.000 38.725  ? 138 VAL LLL N   1 
ATOM   4256  C CA  . VAL C 3 138 ? 48.692  78.567  69.031  1.000 37.871  ? 138 VAL LLL CA  1 
ATOM   4257  C C   . VAL C 3 138 ? 47.305  77.939  68.966  1.000 38.578  ? 138 VAL LLL C   1 
ATOM   4258  O O   . VAL C 3 138 ? 46.389  78.542  68.365  1.000 36.454  ? 138 VAL LLL O   1 
ATOM   4259  C CB  . VAL C 3 138 ? 48.661  79.880  69.825  1.000 41.138  ? 138 VAL LLL CB  1 
ATOM   4260  C CG1 . VAL C 3 138 ? 48.485  79.625  71.311  1.000 41.964  ? 138 VAL LLL CG1 1 
ATOM   4261  C CG2 . VAL C 3 138 ? 49.896  80.717  69.556  1.000 42.304  ? 138 VAL LLL CG2 1 
ATOM   4262  N N   . VAL C 3 139 ? 47.167  76.749  69.538  1.000 41.560  ? 139 VAL LLL N   1 
ATOM   4263  C CA  . VAL C 3 139 ? 45.914  75.956  69.430  1.000 42.787  ? 139 VAL LLL CA  1 
ATOM   4264  C C   . VAL C 3 139 ? 45.242  75.956  70.794  1.000 43.487  ? 139 VAL LLL C   1 
ATOM   4265  O O   . VAL C 3 139 ? 45.936  75.808  71.812  1.000 38.535  ? 139 VAL LLL O   1 
ATOM   4266  C CB  . VAL C 3 139 ? 46.177  74.533  68.914  1.000 41.353  ? 139 VAL LLL CB  1 
ATOM   4267  C CG1 . VAL C 3 139 ? 44.898  73.722  68.812  1.000 42.752  ? 139 VAL LLL CG1 1 
ATOM   4268  C CG2 . VAL C 3 139 ? 46.867  74.576  67.567  1.000 41.673  ? 139 VAL LLL CG2 1 
ATOM   4269  N N   . CYS C 3 140 ? 43.931  76.160  70.785  1.000 47.381  ? 140 CYS LLL N   1 
ATOM   4270  C CA  . CYS C 3 140 ? 43.066  76.002  71.968  1.000 49.672  ? 140 CYS LLL CA  1 
ATOM   4271  C C   . CYS C 3 140 ? 42.078  74.877  71.691  1.000 47.211  ? 140 CYS LLL C   1 
ATOM   4272  O O   . CYS C 3 140 ? 41.430  74.920  70.631  1.000 43.796  ? 140 CYS LLL O   1 
ATOM   4273  C CB  . CYS C 3 140 ? 42.322  77.287  72.283  1.000 53.887  ? 140 CYS LLL CB  1 
ATOM   4274  S SG  . CYS C 3 140 ? 41.636  77.269  73.956  1.000 54.726  ? 140 CYS LLL SG  1 
ATOM   4275  N N   . LEU C 3 141 ? 42.021  73.907  72.602  1.000 46.749  ? 141 LEU LLL N   1 
ATOM   4276  C CA  . LEU C 3 141 ? 41.126  72.736  72.514  1.000 47.996  ? 141 LEU LLL CA  1 
ATOM   4277  C C   . LEU C 3 141 ? 40.017  72.883  73.552  1.000 45.969  ? 141 LEU LLL C   1 
ATOM   4278  O O   . LEU C 3 141 ? 40.332  73.036  74.743  1.000 42.200  ? 141 LEU LLL O   1 
ATOM   4279  C CB  . LEU C 3 141 ? 41.940  71.462  72.759  1.000 51.714  ? 141 LEU LLL CB  1 
ATOM   4280  C CG  . LEU C 3 141 ? 41.137  70.164  72.695  1.000 52.649  ? 141 LEU LLL CG  1 
ATOM   4281  C CD1 . LEU C 3 141 ? 40.413  70.041  71.365  1.000 53.585  ? 141 LEU LLL CD1 1 
ATOM   4282  C CD2 . LEU C 3 141 ? 42.038  68.963  72.915  1.000 51.137  ? 141 LEU LLL CD2 1 
ATOM   4283  N N   . LEU C 3 142 ? 38.768  72.863  73.095  1.000 47.621  ? 142 LEU LLL N   1 
ATOM   4284  C CA  . LEU C 3 142 ? 37.566  72.638  73.936  1.000 49.337  ? 142 LEU LLL CA  1 
ATOM   4285  C C   . LEU C 3 142 ? 37.141  71.178  73.725  1.000 50.052  ? 142 LEU LLL C   1 
ATOM   4286  O O   . LEU C 3 142 ? 36.747  70.844  72.586  1.000 50.443  ? 142 LEU LLL O   1 
ATOM   4287  C CB  . LEU C 3 142 ? 36.450  73.599  73.515  1.000 52.756  ? 142 LEU LLL CB  1 
ATOM   4288  C CG  . LEU C 3 142 ? 36.575  75.057  73.952  1.000 52.927  ? 142 LEU LLL CG  1 
ATOM   4289  C CD1 . LEU C 3 142 ? 37.809  75.709  73.338  1.000 54.928  ? 142 LEU LLL CD1 1 
ATOM   4290  C CD2 . LEU C 3 142 ? 35.321  75.841  73.574  1.000 50.027  ? 142 LEU LLL CD2 1 
ATOM   4291  N N   . ASN C 3 143 ? 37.227  70.341  74.763  1.000 50.505  ? 143 ASN LLL N   1 
ATOM   4292  C CA  . ASN C 3 143 ? 37.031  68.871  74.652  1.000 49.317  ? 143 ASN LLL CA  1 
ATOM   4293  C C   . ASN C 3 143 ? 35.689  68.440  75.280  1.000 48.440  ? 143 ASN LLL C   1 
ATOM   4294  O O   . ASN C 3 143 ? 35.431  68.806  76.441  1.000 44.960  ? 143 ASN LLL O   1 
ATOM   4295  C CB  . ASN C 3 143 ? 38.216  68.147  75.277  1.000 50.280  ? 143 ASN LLL CB  1 
ATOM   4296  C CG  . ASN C 3 143 ? 38.449  66.777  74.685  1.000 52.566  ? 143 ASN LLL CG  1 
ATOM   4297  O OD1 . ASN C 3 143 ? 38.307  66.592  73.469  1.000 51.417  ? 143 ASN LLL OD1 1 
ATOM   4298  N ND2 . ASN C 3 143 ? 38.873  65.853  75.539  1.000 47.054  ? 143 ASN LLL ND2 1 
ATOM   4299  N N   . ASN C 3 144 ? 34.864  67.714  74.511  1.000 49.627  ? 144 ASN LLL N   1 
ATOM   4300  C CA  . ASN C 3 144 ? 33.630  66.986  74.940  1.000 50.474  ? 144 ASN LLL CA  1 
ATOM   4301  C C   . ASN C 3 144 ? 32.681  67.878  75.747  1.000 49.712  ? 144 ASN LLL C   1 
ATOM   4302  O O   . ASN C 3 144 ? 32.584  67.697  76.980  1.000 45.797  ? 144 ASN LLL O   1 
ATOM   4303  C CB  . ASN C 3 144 ? 33.957  65.736  75.753  1.000 50.955  ? 144 ASN LLL CB  1 
ATOM   4304  C CG  . ASN C 3 144 ? 34.993  64.888  75.065  1.000 49.065  ? 144 ASN LLL CG  1 
ATOM   4305  O OD1 . ASN C 3 144 ? 34.869  64.613  73.874  1.000 50.823  ? 144 ASN LLL OD1 1 
ATOM   4306  N ND2 . ASN C 3 144 ? 36.001  64.482  75.811  1.000 54.586  ? 144 ASN LLL ND2 1 
ATOM   4307  N N   . PHE C 3 145 ? 31.967  68.760  75.049  1.000 49.059  ? 145 PHE LLL N   1 
ATOM   4308  C CA  . PHE C 3 145 ? 30.986  69.709  75.631  1.000 47.022  ? 145 PHE LLL CA  1 
ATOM   4309  C C   . PHE C 3 145 ? 29.691  69.651  74.824  1.000 49.479  ? 145 PHE LLL C   1 
ATOM   4310  O O   . PHE C 3 145 ? 29.730  69.219  73.659  1.000 49.101  ? 145 PHE LLL O   1 
ATOM   4311  C CB  . PHE C 3 145 ? 31.548  71.129  75.646  1.000 45.064  ? 145 PHE LLL CB  1 
ATOM   4312  C CG  . PHE C 3 145 ? 31.852  71.701  74.290  1.000 44.896  ? 145 PHE LLL CG  1 
ATOM   4313  C CD1 . PHE C 3 145 ? 30.914  72.455  73.610  1.000 46.686  ? 145 PHE LLL CD1 1 
ATOM   4314  C CD2 . PHE C 3 145 ? 33.080  71.488  73.694  1.000 47.604  ? 145 PHE LLL CD2 1 
ATOM   4315  C CE1 . PHE C 3 145 ? 31.194  72.974  72.359  1.000 49.029  ? 145 PHE LLL CE1 1 
ATOM   4316  C CE2 . PHE C 3 145 ? 33.363  72.021  72.445  1.000 48.952  ? 145 PHE LLL CE2 1 
ATOM   4317  C CZ  . PHE C 3 145 ? 32.417  72.753  71.776  1.000 48.730  ? 145 PHE LLL CZ  1 
ATOM   4318  N N   . TYR C 3 146 ? 28.587  70.042  75.468  1.000 51.804  ? 146 TYR LLL N   1 
ATOM   4319  C CA  . TYR C 3 146 ? 27.240  70.211  74.867  1.000 50.612  ? 146 TYR LLL CA  1 
ATOM   4320  C C   . TYR C 3 146 ? 26.563  71.363  75.595  1.000 45.114  ? 146 TYR LLL C   1 
ATOM   4321  O O   . TYR C 3 146 ? 26.713  71.445  76.809  1.000 39.944  ? 146 TYR LLL O   1 
ATOM   4322  C CB  . TYR C 3 146 ? 26.391  68.929  74.948  1.000 49.454  ? 146 TYR LLL CB  1 
ATOM   4323  C CG  . TYR C 3 146 ? 25.128  69.080  74.148  1.000 48.496  ? 146 TYR LLL CG  1 
ATOM   4324  C CD1 . TYR C 3 146 ? 25.137  68.913  72.778  1.000 46.991  ? 146 TYR LLL CD1 1 
ATOM   4325  C CD2 . TYR C 3 146 ? 23.962  69.541  74.730  1.000 51.461  ? 146 TYR LLL CD2 1 
ATOM   4326  C CE1 . TYR C 3 146 ? 24.004  69.137  72.013  1.000 50.387  ? 146 TYR LLL CE1 1 
ATOM   4327  C CE2 . TYR C 3 146 ? 22.817  69.769  73.980  1.000 53.193  ? 146 TYR LLL CE2 1 
ATOM   4328  C CZ  . TYR C 3 146 ? 22.834  69.568  72.614  1.000 51.505  ? 146 TYR LLL CZ  1 
ATOM   4329  O OH  . TYR C 3 146 ? 21.713  69.797  71.862  1.000 50.840  ? 146 TYR LLL OH  1 
ATOM   4330  N N   . PRO C 3 147 ? 25.841  72.284  74.909  1.000 48.059  ? 147 PRO LLL N   1 
ATOM   4331  C CA  . PRO C 3 147 ? 25.697  72.307  73.447  1.000 55.014  ? 147 PRO LLL CA  1 
ATOM   4332  C C   . PRO C 3 147 ? 26.883  72.921  72.686  1.000 59.922  ? 147 PRO LLL C   1 
ATOM   4333  O O   . PRO C 3 147 ? 27.870  73.252  73.305  1.000 53.756  ? 147 PRO LLL O   1 
ATOM   4334  C CB  . PRO C 3 147 ? 24.488  73.230  73.235  1.000 53.693  ? 147 PRO LLL CB  1 
ATOM   4335  C CG  . PRO C 3 147 ? 24.662  74.238  74.340  1.000 55.289  ? 147 PRO LLL CG  1 
ATOM   4336  C CD  . PRO C 3 147 ? 25.105  73.397  75.528  1.000 52.957  ? 147 PRO LLL CD  1 
ATOM   4337  N N   . ARG C 3 148 ? 26.737  73.077  71.366  1.000 68.910  ? 148 ARG LLL N   1 
ATOM   4338  C CA  . ARG C 3 148 ? 27.844  73.441  70.447  1.000 72.538  ? 148 ARG LLL CA  1 
ATOM   4339  C C   . ARG C 3 148 ? 28.249  74.902  70.638  1.000 73.595  ? 148 ARG LLL C   1 
ATOM   4340  O O   . ARG C 3 148 ? 29.420  75.208  70.356  1.000 89.491  ? 148 ARG LLL O   1 
ATOM   4341  C CB  . ARG C 3 148 ? 27.441  73.206  68.990  1.000 74.103  ? 148 ARG LLL CB  1 
ATOM   4342  C CG  . ARG C 3 148 ? 28.606  73.249  68.016  1.000 74.952  ? 148 ARG LLL CG  1 
ATOM   4343  C CD  . ARG C 3 148 ? 28.337  73.973  66.696  1.000 74.633  ? 148 ARG LLL CD  1 
ATOM   4344  N NE  . ARG C 3 148 ? 29.448  74.816  66.204  1.000 79.453  ? 148 ARG LLL NE  1 
ATOM   4345  C CZ  . ARG C 3 148 ? 30.217  75.682  66.919  1.000 70.464  ? 148 ARG LLL CZ  1 
ATOM   4346  N NH1 . ARG C 3 148 ? 30.052  75.881  68.218  1.000 70.975  ? 148 ARG LLL NH1 1 
ATOM   4347  N NH2 . ARG C 3 148 ? 31.181  76.357  66.317  1.000 62.284  ? 148 ARG LLL NH2 1 
ATOM   4348  N N   . GLU C 3 149 ? 27.333  75.777  71.059  1.000 72.547  ? 149 GLU LLL N   1 
ATOM   4349  C CA  . GLU C 3 149 ? 27.616  77.247  71.136  1.000 72.817  ? 149 GLU LLL CA  1 
ATOM   4350  C C   . GLU C 3 149 ? 28.597  77.483  72.285  1.000 66.707  ? 149 GLU LLL C   1 
ATOM   4351  O O   . GLU C 3 149 ? 28.336  77.015  73.417  1.000 60.038  ? 149 GLU LLL O   1 
ATOM   4352  C CB  . GLU C 3 149 ? 26.386  78.138  71.344  1.000 80.347  ? 149 GLU LLL CB  1 
ATOM   4353  C CG  . GLU C 3 149 ? 25.320  78.009  70.266  1.000 95.121  ? 149 GLU LLL CG  1 
ATOM   4354  C CD  . GLU C 3 149 ? 24.403  76.795  70.420  1.000 110.741 ? 149 GLU LLL CD  1 
ATOM   4355  O OE1 . GLU C 3 149 ? 23.670  76.698  71.443  1.000 122.771 ? 149 GLU LLL OE1 1 
ATOM   4356  O OE2 . GLU C 3 149 ? 24.450  75.915  69.540  1.000 112.135 ? 149 GLU LLL OE2 1 
ATOM   4357  N N   . ALA C 3 150 ? 29.707  78.146  71.961  1.000 63.574  ? 150 ALA LLL N   1 
ATOM   4358  C CA  . ALA C 3 150 ? 30.789  78.527  72.890  1.000 55.702  ? 150 ALA LLL CA  1 
ATOM   4359  C C   . ALA C 3 150 ? 31.568  79.698  72.283  1.000 52.760  ? 150 ALA LLL C   1 
ATOM   4360  O O   . ALA C 3 150 ? 31.859  79.686  71.080  1.000 49.208  ? 150 ALA LLL O   1 
ATOM   4361  C CB  . ALA C 3 150 ? 31.659  77.332  73.152  1.000 56.515  ? 150 ALA LLL CB  1 
ATOM   4362  N N   . LYS C 3 151 ? 31.834  80.712  73.093  1.000 53.870  ? 151 LYS LLL N   1 
ATOM   4363  C CA  . LYS C 3 151 ? 32.672  81.871  72.716  1.000 55.220  ? 151 LYS LLL CA  1 
ATOM   4364  C C   . LYS C 3 151 ? 34.119  81.507  73.060  1.000 51.750  ? 151 LYS LLL C   1 
ATOM   4365  O O   . LYS C 3 151 ? 34.379  81.098  74.214  1.000 52.398  ? 151 LYS LLL O   1 
ATOM   4366  C CB  . LYS C 3 151 ? 32.145  83.123  73.422  1.000 64.922  ? 151 LYS LLL CB  1 
ATOM   4367  C CG  . LYS C 3 151 ? 33.007  84.363  73.269  1.000 77.038  ? 151 LYS LLL CG  1 
ATOM   4368  C CD  . LYS C 3 151 ? 32.262  85.581  72.758  1.000 81.607  ? 151 LYS LLL CD  1 
ATOM   4369  C CE  . LYS C 3 151 ? 33.191  86.500  71.989  1.000 93.410  ? 151 LYS LLL CE  1 
ATOM   4370  N NZ  . LYS C 3 151 ? 32.844  87.929  72.166  1.000 103.401 ? 151 LYS LLL NZ  1 
ATOM   4371  N N   . VAL C 3 152 ? 35.015  81.609  72.083  1.000 49.904  ? 152 VAL LLL N   1 
ATOM   4372  C CA  . VAL C 3 152 ? 36.480  81.450  72.306  1.000 55.280  ? 152 VAL LLL CA  1 
ATOM   4373  C C   . VAL C 3 152 ? 37.147  82.786  71.999  1.000 52.625  ? 152 VAL LLL C   1 
ATOM   4374  O O   . VAL C 3 152 ? 37.043  83.228  70.852  1.000 52.844  ? 152 VAL LLL O   1 
ATOM   4375  C CB  . VAL C 3 152 ? 37.066  80.318  71.444  1.000 61.516  ? 152 VAL LLL CB  1 
ATOM   4376  C CG1 . VAL C 3 152 ? 38.582  80.299  71.495  1.000 64.441  ? 152 VAL LLL CG1 1 
ATOM   4377  C CG2 . VAL C 3 152 ? 36.513  78.964  71.858  1.000 66.029  ? 152 VAL LLL CG2 1 
ATOM   4378  N N   . GLN C 3 153 ? 37.782  83.395  72.995  1.000 54.087  ? 153 GLN LLL N   1 
ATOM   4379  C CA  . GLN C 3 153 ? 38.447  84.717  72.873  1.000 60.152  ? 153 GLN LLL CA  1 
ATOM   4380  C C   . GLN C 3 153 ? 39.953  84.537  73.053  1.000 57.697  ? 153 GLN LLL C   1 
ATOM   4381  O O   . GLN C 3 153 ? 40.360  84.028  74.112  1.000 57.860  ? 153 GLN LLL O   1 
ATOM   4382  C CB  . GLN C 3 153 ? 37.920  85.682  73.934  1.000 70.617  ? 153 GLN LLL CB  1 
ATOM   4383  C CG  . GLN C 3 153 ? 38.101  87.145  73.566  1.000 75.818  ? 153 GLN LLL CG  1 
ATOM   4384  C CD  . GLN C 3 153 ? 36.773  87.774  73.200  1.000 79.240  ? 153 GLN LLL CD  1 
ATOM   4385  O OE1 . GLN C 3 153 ? 35.723  87.489  73.788  1.000 68.132  ? 153 GLN LLL OE1 1 
ATOM   4386  N NE2 . GLN C 3 153 ? 36.818  88.646  72.207  1.000 86.869  ? 153 GLN LLL NE2 1 
ATOM   4387  N N   . TRP C 3 154 ? 40.745  84.913  72.051  1.000 54.138  ? 154 TRP LLL N   1 
ATOM   4388  C CA  . TRP C 3 154 ? 42.223  84.884  72.157  1.000 54.096  ? 154 TRP LLL CA  1 
ATOM   4389  C C   . TRP C 3 154 ? 42.673  86.184  72.822  1.000 53.793  ? 154 TRP LLL C   1 
ATOM   4390  O O   . TRP C 3 154 ? 42.125  87.231  72.460  1.000 61.229  ? 154 TRP LLL O   1 
ATOM   4391  C CB  . TRP C 3 154 ? 42.865  84.678  70.782  1.000 57.071  ? 154 TRP LLL CB  1 
ATOM   4392  C CG  . TRP C 3 154 ? 42.881  83.249  70.326  1.000 54.136  ? 154 TRP LLL CG  1 
ATOM   4393  C CD1 . TRP C 3 154 ? 42.107  82.683  69.356  1.000 52.910  ? 154 TRP LLL CD1 1 
ATOM   4394  C CD2 . TRP C 3 154 ? 43.699  82.191  70.845  1.000 49.841  ? 154 TRP LLL CD2 1 
ATOM   4395  N NE1 . TRP C 3 154 ? 42.394  81.354  69.228  1.000 49.477  ? 154 TRP LLL NE1 1 
ATOM   4396  C CE2 . TRP C 3 154 ? 43.368  81.025  70.129  1.000 50.860  ? 154 TRP LLL CE2 1 
ATOM   4397  C CE3 . TRP C 3 154 ? 44.678  82.116  71.837  1.000 50.459  ? 154 TRP LLL CE3 1 
ATOM   4398  C CZ2 . TRP C 3 154 ? 43.987  79.801  70.373  1.000 54.658  ? 154 TRP LLL CZ2 1 
ATOM   4399  C CZ3 . TRP C 3 154 ? 45.292  80.910  72.081  1.000 50.077  ? 154 TRP LLL CZ3 1 
ATOM   4400  C CH2 . TRP C 3 154 ? 44.946  79.766  71.360  1.000 52.984  ? 154 TRP LLL CH2 1 
ATOM   4401  N N   . LYS C 3 155 ? 43.623  86.110  73.758  1.000 55.580  ? 155 LYS LLL N   1 
ATOM   4402  C CA  . LYS C 3 155 ? 44.211  87.286  74.453  1.000 54.486  ? 155 LYS LLL CA  1 
ATOM   4403  C C   . LYS C 3 155 ? 45.732  87.216  74.410  1.000 51.848  ? 155 LYS LLL C   1 
ATOM   4404  O O   . LYS C 3 155 ? 46.301  86.264  74.959  1.000 47.400  ? 155 LYS LLL O   1 
ATOM   4405  C CB  . LYS C 3 155 ? 43.730  87.344  75.899  1.000 57.793  ? 155 LYS LLL CB  1 
ATOM   4406  C CG  . LYS C 3 155 ? 42.366  87.976  76.028  1.000 62.627  ? 155 LYS LLL CG  1 
ATOM   4407  C CD  . LYS C 3 155 ? 41.656  87.678  77.315  1.000 71.515  ? 155 LYS LLL CD  1 
ATOM   4408  C CE  . LYS C 3 155 ? 40.227  88.171  77.225  1.000 83.034  ? 155 LYS LLL CE  1 
ATOM   4409  N NZ  . LYS C 3 155 ? 39.543  88.113  78.534  1.000 96.668  ? 155 LYS LLL NZ  1 
ATOM   4410  N N   . VAL C 3 156 ? 46.348  88.220  73.799  1.000 50.126  ? 156 VAL LLL N   1 
ATOM   4411  C CA  . VAL C 3 156 ? 47.822  88.312  73.637  1.000 54.416  ? 156 VAL LLL CA  1 
ATOM   4412  C C   . VAL C 3 156 ? 48.307  89.543  74.402  1.000 57.618  ? 156 VAL LLL C   1 
ATOM   4413  O O   . VAL C 3 156 ? 48.028  90.688  73.945  1.000 60.220  ? 156 VAL LLL O   1 
ATOM   4414  C CB  . VAL C 3 156 ? 48.171  88.356  72.141  1.000 55.418  ? 156 VAL LLL CB  1 
ATOM   4415  C CG1 . VAL C 3 156 ? 49.663  88.476  71.883  1.000 56.349  ? 156 VAL LLL CG1 1 
ATOM   4416  C CG2 . VAL C 3 156 ? 47.620  87.127  71.453  1.000 56.660  ? 156 VAL LLL CG2 1 
ATOM   4417  N N   . ASP C 3 157 ? 48.994  89.306  75.524  1.000 56.773  ? 157 ASP LLL N   1 
ATOM   4418  C CA  . ASP C 3 157 ? 49.371  90.355  76.501  1.000 57.365  ? 157 ASP LLL CA  1 
ATOM   4419  C C   . ASP C 3 157 ? 48.103  91.134  76.828  1.000 55.271  ? 157 ASP LLL C   1 
ATOM   4420  O O   . ASP C 3 157 ? 48.138  92.371  76.819  1.000 62.981  ? 157 ASP LLL O   1 
ATOM   4421  C CB  . ASP C 3 157 ? 50.487  91.253  75.963  1.000 58.197  ? 157 ASP LLL CB  1 
ATOM   4422  C CG  . ASP C 3 157 ? 51.861  90.633  76.085  1.000 64.528  ? 157 ASP LLL CG  1 
ATOM   4423  O OD1 . ASP C 3 157 ? 52.012  89.649  76.886  1.000 61.191  ? 157 ASP LLL OD1 1 
ATOM   4424  O OD2 . ASP C 3 157 ? 52.769  91.141  75.377  1.000 69.269  ? 157 ASP LLL OD2 1 
ATOM   4425  N N   . ASN C 3 158 ? 46.998  90.424  77.028  1.000 54.027  ? 158 ASN LLL N   1 
ATOM   4426  C CA  . ASN C 3 158 ? 45.749  91.014  77.587  1.000 53.261  ? 158 ASN LLL CA  1 
ATOM   4427  C C   . ASN C 3 158 ? 45.028  91.866  76.516  1.000 51.339  ? 158 ASN LLL C   1 
ATOM   4428  O O   . ASN C 3 158 ? 44.012  92.495  76.843  1.000 50.970  ? 158 ASN LLL O   1 
ATOM   4429  C CB  . ASN C 3 158 ? 46.070  91.764  78.888  1.000 54.357  ? 158 ASN LLL CB  1 
ATOM   4430  C CG  . ASN C 3 158 ? 45.028  91.553  79.956  1.000 56.851  ? 158 ASN LLL CG  1 
ATOM   4431  O OD1 . ASN C 3 158 ? 44.456  90.475  80.027  1.000 61.437  ? 158 ASN LLL OD1 1 
ATOM   4432  N ND2 . ASN C 3 158 ? 44.783  92.559  80.789  1.000 59.291  ? 158 ASN LLL ND2 1 
ATOM   4433  N N   . ALA C 3 159 ? 45.514  91.868  75.268  1.000 52.831  ? 159 ALA LLL N   1 
ATOM   4434  C CA  . ALA C 3 159 ? 44.853  92.461  74.077  1.000 52.029  ? 159 ALA LLL CA  1 
ATOM   4435  C C   . ALA C 3 159 ? 43.989  91.403  73.378  1.000 51.590  ? 159 ALA LLL C   1 
ATOM   4436  O O   . ALA C 3 159 ? 44.564  90.388  72.919  1.000 52.322  ? 159 ALA LLL O   1 
ATOM   4437  C CB  . ALA C 3 159 ? 45.902  92.994  73.127  1.000 50.676  ? 159 ALA LLL CB  1 
ATOM   4438  N N   . LEU C 3 160 ? 42.678  91.631  73.240  1.000 50.636  ? 160 LEU LLL N   1 
ATOM   4439  C CA  . LEU C 3 160 ? 41.797  90.691  72.485  1.000 58.678  ? 160 LEU LLL CA  1 
ATOM   4440  C C   . LEU C 3 160 ? 42.232  90.636  71.008  1.000 58.892  ? 160 LEU LLL C   1 
ATOM   4441  O O   . LEU C 3 160 ? 42.151  91.688  70.336  1.000 57.366  ? 160 LEU LLL O   1 
ATOM   4442  C CB  . LEU C 3 160 ? 40.325  91.110  72.593  1.000 63.504  ? 160 LEU LLL CB  1 
ATOM   4443  C CG  . LEU C 3 160 ? 39.811  91.502  73.981  1.000 69.471  ? 160 LEU LLL CG  1 
ATOM   4444  C CD1 . LEU C 3 160 ? 38.305  91.292  74.081  1.000 73.732  ? 160 LEU LLL CD1 1 
ATOM   4445  C CD2 . LEU C 3 160 ? 40.481  90.729  75.093  1.000 70.501  ? 160 LEU LLL CD2 1 
ATOM   4446  N N   . GLN C 3 161 ? 42.633  89.456  70.509  1.000 56.648  ? 161 GLN LLL N   1 
ATOM   4447  C CA  . GLN C 3 161 ? 42.986  89.244  69.087  1.000 55.347  ? 161 GLN LLL CA  1 
ATOM   4448  C C   . GLN C 3 161 ? 41.745  88.897  68.299  1.000 51.892  ? 161 GLN LLL C   1 
ATOM   4449  O O   . GLN C 3 161 ? 40.910  88.189  68.833  1.000 53.695  ? 161 GLN LLL O   1 
ATOM   4450  C CB  . GLN C 3 161 ? 43.955  88.094  68.902  1.000 61.362  ? 161 GLN LLL CB  1 
ATOM   4451  C CG  . GLN C 3 161 ? 45.311  88.414  69.487  1.000 71.650  ? 161 GLN LLL CG  1 
ATOM   4452  C CD  . GLN C 3 161 ? 45.931  89.665  68.916  1.000 70.632  ? 161 GLN LLL CD  1 
ATOM   4453  O OE1 . GLN C 3 161 ? 46.127  89.792  67.703  1.000 63.940  ? 161 GLN LLL OE1 1 
ATOM   4454  N NE2 . GLN C 3 161 ? 46.254  90.590  69.812  1.000 71.719  ? 161 GLN LLL NE2 1 
ATOM   4455  N N   . SER C 3 162 ? 41.703  89.352  67.054  1.000 50.807  ? 162 SER LLL N   1 
ATOM   4456  C CA  . SER C 3 162 ? 40.514  89.275  66.183  1.000 52.851  ? 162 SER LLL CA  1 
ATOM   4457  C C   . SER C 3 162 ? 40.923  89.027  64.723  1.000 56.743  ? 162 SER LLL C   1 
ATOM   4458  O O   . SER C 3 162 ? 41.871  89.703  64.239  1.000 62.144  ? 162 SER LLL O   1 
ATOM   4459  C CB  . SER C 3 162 ? 39.730  90.520  66.358  1.000 52.331  ? 162 SER LLL CB  1 
ATOM   4460  O OG  . SER C 3 162 ? 38.652  90.554  65.446  1.000 57.642  ? 162 SER LLL OG  1 
ATOM   4461  N N   . GLY C 3 163 ? 40.266  88.045  64.086  1.000 59.702  ? 163 GLY LLL N   1 
ATOM   4462  C CA  . GLY C 3 163 ? 40.354  87.707  62.647  1.000 63.147  ? 163 GLY LLL CA  1 
ATOM   4463  C C   . GLY C 3 163 ? 41.688  87.110  62.204  1.000 64.489  ? 163 GLY LLL C   1 
ATOM   4464  O O   . GLY C 3 163 ? 41.910  87.040  60.976  1.000 60.624  ? 163 GLY LLL O   1 
ATOM   4465  N N   . ASN C 3 164 ? 42.533  86.656  63.135  1.000 65.415  ? 164 ASN LLL N   1 
ATOM   4466  C CA  . ASN C 3 164 ? 43.774  85.883  62.843  1.000 62.532  ? 164 ASN LLL CA  1 
ATOM   4467  C C   . ASN C 3 164 ? 43.607  84.473  63.435  1.000 59.852  ? 164 ASN LLL C   1 
ATOM   4468  O O   . ASN C 3 164 ? 44.605  83.859  63.836  1.000 70.625  ? 164 ASN LLL O   1 
ATOM   4469  C CB  . ASN C 3 164 ? 45.023  86.614  63.349  1.000 61.530  ? 164 ASN LLL CB  1 
ATOM   4470  C CG  . ASN C 3 164 ? 44.920  87.046  64.802  1.000 65.169  ? 164 ASN LLL CG  1 
ATOM   4471  O OD1 . ASN C 3 164 ? 43.881  86.863  65.448  1.000 65.218  ? 164 ASN LLL OD1 1 
ATOM   4472  N ND2 . ASN C 3 164 ? 45.985  87.636  65.325  1.000 62.950  ? 164 ASN LLL ND2 1 
ATOM   4473  N N   . SER C 3 165 ? 42.377  83.972  63.498  1.000 51.652  ? 165 SER LLL N   1 
ATOM   4474  C CA  . SER C 3 165 ? 42.037  82.681  64.148  1.000 50.049  ? 165 SER LLL CA  1 
ATOM   4475  C C   . SER C 3 165 ? 40.893  82.006  63.385  1.000 47.892  ? 165 SER LLL C   1 
ATOM   4476  O O   . SER C 3 165 ? 40.045  82.741  62.889  1.000 52.649  ? 165 SER LLL O   1 
ATOM   4477  C CB  . SER C 3 165 ? 41.705  82.897  65.615  1.000 48.177  ? 165 SER LLL CB  1 
ATOM   4478  O OG  . SER C 3 165 ? 40.373  83.340  65.771  1.000 49.143  ? 165 SER LLL OG  1 
ATOM   4479  N N   . GLN C 3 166 ? 40.883  80.673  63.272  1.000 45.677  ? 166 GLN LLL N   1 
ATOM   4480  C CA  . GLN C 3 166 ? 39.736  79.895  62.716  1.000 49.107  ? 166 GLN LLL CA  1 
ATOM   4481  C C   . GLN C 3 166 ? 39.367  78.796  63.715  1.000 46.245  ? 166 GLN LLL C   1 
ATOM   4482  O O   . GLN C 3 166 ? 40.255  78.301  64.422  1.000 43.936  ? 166 GLN LLL O   1 
ATOM   4483  C CB  . GLN C 3 166 ? 40.024  79.277  61.342  1.000 55.184  ? 166 GLN LLL CB  1 
ATOM   4484  C CG  . GLN C 3 166 ? 41.086  80.021  60.539  1.000 63.092  ? 166 GLN LLL CG  1 
ATOM   4485  C CD  . GLN C 3 166 ? 41.211  79.536  59.114  1.000 68.193  ? 166 GLN LLL CD  1 
ATOM   4486  O OE1 . GLN C 3 166 ? 42.291  79.131  58.650  1.000 62.261  ? 166 GLN LLL OE1 1 
ATOM   4487  N NE2 . GLN C 3 166 ? 40.087  79.586  58.409  1.000 66.941  ? 166 GLN LLL NE2 1 
ATOM   4488  N N   . GLU C 3 167 ? 38.081  78.465  63.796  1.000 47.086  ? 167 GLU LLL N   1 
ATOM   4489  C CA  . GLU C 3 167 ? 37.557  77.407  64.698  1.000 45.994  ? 167 GLU LLL CA  1 
ATOM   4490  C C   . GLU C 3 167 ? 37.250  76.195  63.829  1.000 41.974  ? 167 GLU LLL C   1 
ATOM   4491  O O   . GLU C 3 167 ? 37.202  76.338  62.606  1.000 38.961  ? 167 GLU LLL O   1 
ATOM   4492  C CB  . GLU C 3 167 ? 36.322  77.862  65.478  1.000 51.316  ? 167 GLU LLL CB  1 
ATOM   4493  C CG  . GLU C 3 167 ? 36.584  79.081  66.342  1.000 60.755  ? 167 GLU LLL CG  1 
ATOM   4494  C CD  . GLU C 3 167 ? 35.554  79.435  67.398  1.000 63.910  ? 167 GLU LLL CD  1 
ATOM   4495  O OE1 . GLU C 3 167 ? 34.390  78.999  67.262  1.000 62.851  ? 167 GLU LLL OE1 1 
ATOM   4496  O OE2 . GLU C 3 167 ? 35.928  80.173  68.340  1.000 61.490  ? 167 GLU LLL OE2 1 
ATOM   4497  N N   . SER C 3 168 ? 37.066  75.043  64.451  1.000 40.111  ? 168 SER LLL N   1 
ATOM   4498  C CA  . SER C 3 168 ? 36.857  73.749  63.765  1.000 41.352  ? 168 SER LLL CA  1 
ATOM   4499  C C   . SER C 3 168 ? 36.179  72.798  64.754  1.000 42.915  ? 168 SER LLL C   1 
ATOM   4500  O O   . SER C 3 168 ? 36.626  72.763  65.911  1.000 46.587  ? 168 SER LLL O   1 
ATOM   4501  C CB  . SER C 3 168 ? 38.176  73.235  63.283  1.000 42.468  ? 168 SER LLL CB  1 
ATOM   4502  O OG  . SER C 3 168 ? 38.013  72.267  62.269  1.000 44.439  ? 168 SER LLL OG  1 
ATOM   4503  N N   . VAL C 3 169 ? 35.127  72.092  64.339  1.000 39.906  ? 169 VAL LLL N   1 
ATOM   4504  C CA  . VAL C 3 169 ? 34.259  71.325  65.277  1.000 37.530  ? 169 VAL LLL CA  1 
ATOM   4505  C C   . VAL C 3 169 ? 34.053  69.898  64.777  1.000 34.910  ? 169 VAL LLL C   1 
ATOM   4506  O O   . VAL C 3 169 ? 33.827  69.712  63.556  1.000 31.444  ? 169 VAL LLL O   1 
ATOM   4507  C CB  . VAL C 3 169 ? 32.918  72.046  65.458  1.000 38.738  ? 169 VAL LLL CB  1 
ATOM   4508  C CG1 . VAL C 3 169 ? 31.936  71.243  66.290  1.000 39.978  ? 169 VAL LLL CG1 1 
ATOM   4509  C CG2 . VAL C 3 169 ? 33.153  73.401  66.080  1.000 43.135  ? 169 VAL LLL CG2 1 
ATOM   4510  N N   . THR C 3 170 ? 34.071  68.947  65.715  1.000 33.009  ? 170 THR LLL N   1 
ATOM   4511  C CA  . THR C 3 170 ? 33.820  67.516  65.447  1.000 34.762  ? 170 THR LLL CA  1 
ATOM   4512  C C   . THR C 3 170 ? 32.324  67.308  65.196  1.000 38.559  ? 170 THR LLL C   1 
ATOM   4513  O O   . THR C 3 170 ? 31.540  68.142  65.652  1.000 37.160  ? 170 THR LLL O   1 
ATOM   4514  C CB  . THR C 3 170 ? 34.329  66.629  66.590  1.000 34.412  ? 170 THR LLL CB  1 
ATOM   4515  O OG1 . THR C 3 170 ? 33.511  66.739  67.763  1.000 35.271  ? 170 THR LLL OG1 1 
ATOM   4516  C CG2 . THR C 3 170 ? 35.768  66.941  66.933  1.000 33.546  ? 170 THR LLL CG2 1 
ATOM   4517  N N   . GLU C 3 171 ? 31.970  66.243  64.460  1.000 48.255  ? 171 GLU LLL N   1 
ATOM   4518  C CA  . GLU C 3 171 ? 30.607  65.650  64.408  1.000 54.755  ? 171 GLU LLL CA  1 
ATOM   4519  C C   . GLU C 3 171 ? 30.176  65.327  65.839  1.000 47.772  ? 171 GLU LLL C   1 
ATOM   4520  O O   . GLU C 3 171 ? 31.020  64.878  66.646  1.000 44.976  ? 171 GLU LLL O   1 
ATOM   4521  C CB  . GLU C 3 171 ? 30.551  64.334  63.606  1.000 72.819  ? 171 GLU LLL CB  1 
ATOM   4522  C CG  . GLU C 3 171 ? 31.089  64.390  62.178  1.000 87.266  ? 171 GLU LLL CG  1 
ATOM   4523  C CD  . GLU C 3 171 ? 30.555  65.523  61.303  1.000 103.356 ? 171 GLU LLL CD  1 
ATOM   4524  O OE1 . GLU C 3 171 ? 30.989  65.626  60.128  1.000 98.758  ? 171 GLU LLL OE1 1 
ATOM   4525  O OE2 . GLU C 3 171 ? 29.689  66.295  61.782  1.000 112.439 ? 171 GLU LLL OE2 1 
ATOM   4526  N N   . GLN C 3 172 ? 28.902  65.508  66.152  1.000 42.450  ? 172 GLN LLL N   1 
ATOM   4527  C CA  . GLN C 3 172 ? 28.401  65.078  67.472  1.000 43.544  ? 172 GLN LLL CA  1 
ATOM   4528  C C   . GLN C 3 172 ? 28.824  63.620  67.680  1.000 39.728  ? 172 GLN LLL C   1 
ATOM   4529  O O   . GLN C 3 172 ? 28.616  62.822  66.764  1.000 35.692  ? 172 GLN LLL O   1 
ATOM   4530  C CB  . GLN C 3 172 ? 26.890  65.274  67.539  1.000 47.489  ? 172 GLN LLL CB  1 
ATOM   4531  C CG  . GLN C 3 172 ? 26.345  65.116  68.948  1.000 46.664  ? 172 GLN LLL CG  1 
ATOM   4532  C CD  . GLN C 3 172 ? 24.886  65.460  68.993  1.000 45.135  ? 172 GLN LLL CD  1 
ATOM   4533  O OE1 . GLN C 3 172 ? 24.116  65.102  68.100  1.000 47.894  ? 172 GLN LLL OE1 1 
ATOM   4534  N NE2 . GLN C 3 172 ? 24.517  66.179  70.036  1.000 46.629  ? 172 GLN LLL NE2 1 
ATOM   4535  N N   . ASP C 3 173 ? 29.403  63.308  68.837  1.000 42.633  ? 173 ASP LLL N   1 
ATOM   4536  C CA  . ASP C 3 173 ? 29.970  61.976  69.177  1.000 50.558  ? 173 ASP LLL CA  1 
ATOM   4537  C C   . ASP C 3 173 ? 28.869  60.912  69.232  1.000 57.108  ? 173 ASP LLL C   1 
ATOM   4538  O O   . ASP C 3 173 ? 27.807  61.180  69.820  1.000 59.432  ? 173 ASP LLL O   1 
ATOM   4539  C CB  . ASP C 3 173 ? 30.710  62.022  70.512  1.000 53.302  ? 173 ASP LLL CB  1 
ATOM   4540  C CG  . ASP C 3 173 ? 31.610  60.829  70.758  1.000 60.467  ? 173 ASP LLL CG  1 
ATOM   4541  O OD1 . ASP C 3 173 ? 32.759  60.893  70.275  1.000 63.651  ? 173 ASP LLL OD1 1 
ATOM   4542  O OD2 . ASP C 3 173 ? 31.151  59.844  71.425  1.000 61.600  ? 173 ASP LLL OD2 1 
ATOM   4543  N N   . SER C 3 174 ? 29.154  59.727  68.678  1.000 67.786  ? 174 SER LLL N   1 
ATOM   4544  C CA  . SER C 3 174 ? 28.239  58.562  68.572  1.000 73.577  ? 174 SER LLL CA  1 
ATOM   4545  C C   . SER C 3 174 ? 27.778  58.110  69.961  1.000 72.169  ? 174 SER LLL C   1 
ATOM   4546  O O   . SER C 3 174 ? 26.597  57.766  70.082  1.000 66.758  ? 174 SER LLL O   1 
ATOM   4547  C CB  . SER C 3 174 ? 28.903  57.417  67.840  1.000 80.414  ? 174 SER LLL CB  1 
ATOM   4548  O OG  . SER C 3 174 ? 29.793  57.882  66.829  1.000 80.395  ? 174 SER LLL OG  1 
ATOM   4549  N N   . LYS C 3 175 ? 28.681  58.083  70.951  1.000 70.150  ? 175 LYS LLL N   1 
ATOM   4550  C CA  . LYS C 3 175 ? 28.422  57.480  72.289  1.000 76.361  ? 175 LYS LLL CA  1 
ATOM   4551  C C   . LYS C 3 175 ? 27.851  58.526  73.255  1.000 74.673  ? 175 LYS LLL C   1 
ATOM   4552  O O   . LYS C 3 175 ? 26.861  58.196  73.916  1.000 82.097  ? 175 LYS LLL O   1 
ATOM   4553  C CB  . LYS C 3 175 ? 29.685  56.873  72.910  1.000 88.809  ? 175 LYS LLL CB  1 
ATOM   4554  C CG  . LYS C 3 175 ? 30.484  55.940  72.012  1.000 101.160 ? 175 LYS LLL CG  1 
ATOM   4555  C CD  . LYS C 3 175 ? 31.874  55.625  72.549  1.000 99.087  ? 175 LYS LLL CD  1 
ATOM   4556  C CE  . LYS C 3 175 ? 32.898  55.402  71.454  1.000 100.342 ? 175 LYS LLL CE  1 
ATOM   4557  N NZ  . LYS C 3 175 ? 32.601  54.197  70.642  1.000 103.211 ? 175 LYS LLL NZ  1 
ATOM   4558  N N   . ASP C 3 176 ? 28.471  59.708  73.391  1.000 74.384  ? 176 ASP LLL N   1 
ATOM   4559  C CA  . ASP C 3 176 ? 28.167  60.674  74.493  1.000 67.835  ? 176 ASP LLL CA  1 
ATOM   4560  C C   . ASP C 3 176 ? 27.528  61.967  73.958  1.000 55.352  ? 176 ASP LLL C   1 
ATOM   4561  O O   . ASP C 3 176 ? 27.228  62.836  74.784  1.000 59.308  ? 176 ASP LLL O   1 
ATOM   4562  C CB  . ASP C 3 176 ? 29.399  60.942  75.380  1.000 70.807  ? 176 ASP LLL CB  1 
ATOM   4563  C CG  . ASP C 3 176 ? 30.557  61.705  74.742  1.000 73.300  ? 176 ASP LLL CG  1 
ATOM   4564  O OD1 . ASP C 3 176 ? 30.435  62.087  73.567  1.000 82.506  ? 176 ASP LLL OD1 1 
ATOM   4565  O OD2 . ASP C 3 176 ? 31.585  61.912  75.435  1.000 70.717  ? 176 ASP LLL OD2 1 
ATOM   4566  N N   . SER C 3 177 ? 27.302  62.097  72.651  1.000 45.409  ? 177 SER LLL N   1 
ATOM   4567  C CA  . SER C 3 177 ? 26.585  63.244  72.031  1.000 47.814  ? 177 SER LLL CA  1 
ATOM   4568  C C   . SER C 3 177 ? 27.235  64.591  72.384  1.000 44.576  ? 177 SER LLL C   1 
ATOM   4569  O O   . SER C 3 177 ? 26.511  65.576  72.558  1.000 46.674  ? 177 SER LLL O   1 
ATOM   4570  C CB  . SER C 3 177 ? 25.134  63.249  72.439  1.000 52.927  ? 177 SER LLL CB  1 
ATOM   4571  O OG  . SER C 3 177 ? 24.491  62.052  72.043  1.000 57.141  ? 177 SER LLL OG  1 
ATOM   4572  N N   . THR C 3 178 ? 28.558  64.658  72.453  1.000 44.522  ? 178 THR LLL N   1 
ATOM   4573  C CA  . THR C 3 178 ? 29.314  65.909  72.721  1.000 42.727  ? 178 THR LLL CA  1 
ATOM   4574  C C   . THR C 3 178 ? 30.022  66.360  71.450  1.000 41.610  ? 178 THR LLL C   1 
ATOM   4575  O O   . THR C 3 178 ? 30.256  65.533  70.559  1.000 44.688  ? 178 THR LLL O   1 
ATOM   4576  C CB  . THR C 3 178 ? 30.313  65.722  73.867  1.000 42.630  ? 178 THR LLL CB  1 
ATOM   4577  O OG1 . THR C 3 178 ? 31.345  64.813  73.481  1.000 42.091  ? 178 THR LLL OG1 1 
ATOM   4578  C CG2 . THR C 3 178 ? 29.622  65.195  75.099  1.000 45.287  ? 178 THR LLL CG2 1 
ATOM   4579  N N   . TYR C 3 179 ? 30.319  67.649  71.373  1.000 40.071  ? 179 TYR LLL N   1 
ATOM   4580  C CA  . TYR C 3 179 ? 31.196  68.230  70.335  1.000 42.618  ? 179 TYR LLL CA  1 
ATOM   4581  C C   . TYR C 3 179 ? 32.585  68.448  70.960  1.000 39.947  ? 179 TYR LLL C   1 
ATOM   4582  O O   . TYR C 3 179 ? 32.712  68.496  72.199  1.000 36.889  ? 179 TYR LLL O   1 
ATOM   4583  C CB  . TYR C 3 179 ? 30.546  69.495  69.767  1.000 45.567  ? 179 TYR LLL CB  1 
ATOM   4584  C CG  . TYR C 3 179 ? 29.178  69.309  69.156  1.000 48.429  ? 179 TYR LLL CG  1 
ATOM   4585  C CD1 . TYR C 3 179 ? 29.029  69.039  67.806  1.000 53.208  ? 179 TYR LLL CD1 1 
ATOM   4586  C CD2 . TYR C 3 179 ? 28.023  69.479  69.900  1.000 52.350  ? 179 TYR LLL CD2 1 
ATOM   4587  C CE1 . TYR C 3 179 ? 27.778  68.914  67.221  1.000 58.143  ? 179 TYR LLL CE1 1 
ATOM   4588  C CE2 . TYR C 3 179 ? 26.765  69.335  69.334  1.000 56.142  ? 179 TYR LLL CE2 1 
ATOM   4589  C CZ  . TYR C 3 179 ? 26.636  69.053  67.986  1.000 56.423  ? 179 TYR LLL CZ  1 
ATOM   4590  O OH  . TYR C 3 179 ? 25.407  68.910  67.400  1.000 55.591  ? 179 TYR LLL OH  1 
ATOM   4591  N N   . SER C 3 180 ? 33.609  68.518  70.112  1.000 36.209  ? 180 SER LLL N   1 
ATOM   4592  C CA  . SER C 3 180 ? 34.950  69.061  70.437  1.000 36.000  ? 180 SER LLL CA  1 
ATOM   4593  C C   . SER C 3 180 ? 35.304  70.134  69.394  1.000 38.265  ? 180 SER LLL C   1 
ATOM   4594  O O   . SER C 3 180 ? 34.830  70.043  68.231  1.000 36.410  ? 180 SER LLL O   1 
ATOM   4595  C CB  . SER C 3 180 ? 35.985  67.975  70.539  1.000 35.722  ? 180 SER LLL CB  1 
ATOM   4596  O OG  . SER C 3 180 ? 35.877  67.277  71.775  1.000 36.145  ? 180 SER LLL OG  1 
ATOM   4597  N N   . LEU C 3 181 ? 36.065  71.146  69.818  1.000 38.206  ? 181 LEU LLL N   1 
ATOM   4598  C CA  . LEU C 3 181 ? 36.324  72.374  69.035  1.000 36.564  ? 181 LEU LLL CA  1 
ATOM   4599  C C   . LEU C 3 181 ? 37.800  72.740  69.186  1.000 35.594  ? 181 LEU LLL C   1 
ATOM   4600  O O   . LEU C 3 181 ? 38.317  72.645  70.308  1.000 33.968  ? 181 LEU LLL O   1 
ATOM   4601  C CB  . LEU C 3 181 ? 35.401  73.473  69.564  1.000 39.136  ? 181 LEU LLL CB  1 
ATOM   4602  C CG  . LEU C 3 181 ? 35.450  74.818  68.841  1.000 43.304  ? 181 LEU LLL CG  1 
ATOM   4603  C CD1 . LEU C 3 181 ? 34.106  75.539  68.978  1.000 41.653  ? 181 LEU LLL CD1 1 
ATOM   4604  C CD2 . LEU C 3 181 ? 36.585  75.704  69.354  1.000 45.213  ? 181 LEU LLL CD2 1 
ATOM   4605  N N   . SER C 3 182 ? 38.446  73.121  68.082  1.000 36.113  ? 182 SER LLL N   1 
ATOM   4606  C CA  . SER C 3 182 ? 39.837  73.634  68.027  1.000 36.654  ? 182 SER LLL CA  1 
ATOM   4607  C C   . SER C 3 182 ? 39.834  75.052  67.443  1.000 37.083  ? 182 SER LLL C   1 
ATOM   4608  O O   . SER C 3 182 ? 39.434  75.229  66.280  1.000 35.926  ? 182 SER LLL O   1 
ATOM   4609  C CB  . SER C 3 182 ? 40.734  72.721  67.245  1.000 38.151  ? 182 SER LLL CB  1 
ATOM   4610  O OG  . SER C 3 182 ? 40.654  72.982  65.846  1.000 40.885  ? 182 SER LLL OG  1 
ATOM   4611  N N   . SER C 3 183 ? 40.241  76.022  68.259  1.000 36.716  ? 183 SER LLL N   1 
ATOM   4612  C CA  . SER C 3 183 ? 40.574  77.404  67.851  1.000 36.905  ? 183 SER LLL CA  1 
ATOM   4613  C C   . SER C 3 183 ? 42.078  77.465  67.619  1.000 37.515  ? 183 SER LLL C   1 
ATOM   4614  O O   . SER C 3 183 ? 42.837  76.992  68.489  1.000 34.344  ? 183 SER LLL O   1 
ATOM   4615  C CB  . SER C 3 183 ? 40.141  78.394  68.887  1.000 39.110  ? 183 SER LLL CB  1 
ATOM   4616  O OG  . SER C 3 183 ? 40.071  79.710  68.347  1.000 42.526  ? 183 SER LLL OG  1 
ATOM   4617  N N   . THR C 3 184 ? 42.482  77.999  66.472  1.000 38.473  ? 184 THR LLL N   1 
ATOM   4618  C CA  . THR C 3 184 ? 43.894  78.009  66.030  1.000 41.545  ? 184 THR LLL CA  1 
ATOM   4619  C C   . THR C 3 184 ? 44.272  79.440  65.695  1.000 42.206  ? 184 THR LLL C   1 
ATOM   4620  O O   . THR C 3 184 ? 43.803  79.934  64.641  1.000 42.659  ? 184 THR LLL O   1 
ATOM   4621  C CB  . THR C 3 184 ? 44.098  77.118  64.804  1.000 44.574  ? 184 THR LLL CB  1 
ATOM   4622  O OG1 . THR C 3 184 ? 43.428  75.873  65.042  1.000 51.106  ? 184 THR LLL OG1 1 
ATOM   4623  C CG2 . THR C 3 184 ? 45.568  76.956  64.480  1.000 43.957  ? 184 THR LLL CG2 1 
ATOM   4624  N N   . LEU C 3 185 ? 45.064  80.065  66.568  1.000 44.332  ? 185 LEU LLL N   1 
ATOM   4625  C CA  . LEU C 3 185 ? 45.567  81.451  66.393  1.000 45.577  ? 185 LEU LLL CA  1 
ATOM   4626  C C   . LEU C 3 185 ? 46.874  81.383  65.602  1.000 46.162  ? 185 LEU LLL C   1 
ATOM   4627  O O   . LEU C 3 185 ? 47.778  80.675  66.030  1.000 48.421  ? 185 LEU LLL O   1 
ATOM   4628  C CB  . LEU C 3 185 ? 45.754  82.059  67.785  1.000 46.393  ? 185 LEU LLL CB  1 
ATOM   4629  C CG  . LEU C 3 185 ? 46.415  83.431  67.819  1.000 47.920  ? 185 LEU LLL CG  1 
ATOM   4630  C CD1 . LEU C 3 185 ? 45.428  84.510  67.429  1.000 48.284  ? 185 LEU LLL CD1 1 
ATOM   4631  C CD2 . LEU C 3 185 ? 46.991  83.713  69.195  1.000 51.407  ? 185 LEU LLL CD2 1 
ATOM   4632  N N   . THR C 3 186 ? 46.947  82.070  64.468  1.000 50.455  ? 186 THR LLL N   1 
ATOM   4633  C CA  . THR C 3 186 ? 48.080  82.007  63.502  1.000 56.009  ? 186 THR LLL CA  1 
ATOM   4634  C C   . THR C 3 186 ? 48.722  83.395  63.393  1.000 56.209  ? 186 THR LLL C   1 
ATOM   4635  O O   . THR C 3 186 ? 47.983  84.377  63.145  1.000 63.075  ? 186 THR LLL O   1 
ATOM   4636  C CB  . THR C 3 186 ? 47.586  81.501  62.141  1.000 59.251  ? 186 THR LLL CB  1 
ATOM   4637  O OG1 . THR C 3 186 ? 46.866  80.299  62.419  1.000 66.786  ? 186 THR LLL OG1 1 
ATOM   4638  C CG2 . THR C 3 186 ? 48.683  81.249  61.129  1.000 58.781  ? 186 THR LLL CG2 1 
ATOM   4639  N N   . LEU C 3 187 ? 50.037  83.487  63.599  1.000 55.619  ? 187 LEU LLL N   1 
ATOM   4640  C CA  . LEU C 3 187 ? 50.786  84.763  63.458  1.000 57.817  ? 187 LEU LLL CA  1 
ATOM   4641  C C   . LEU C 3 187 ? 52.247  84.460  63.102  1.000 54.088  ? 187 LEU LLL C   1 
ATOM   4642  O O   . LEU C 3 187 ? 52.684  83.343  63.392  1.000 47.294  ? 187 LEU LLL O   1 
ATOM   4643  C CB  . LEU C 3 187 ? 50.620  85.626  64.723  1.000 57.688  ? 187 LEU LLL CB  1 
ATOM   4644  C CG  . LEU C 3 187 ? 50.869  84.977  66.090  1.000 53.426  ? 187 LEU LLL CG  1 
ATOM   4645  C CD1 . LEU C 3 187 ? 51.292  86.014  67.109  1.000 54.061  ? 187 LEU LLL CD1 1 
ATOM   4646  C CD2 . LEU C 3 187 ? 49.632  84.298  66.636  1.000 52.685  ? 187 LEU LLL CD2 1 
ATOM   4647  N N   . SER C 3 188 ? 52.928  85.411  62.441  1.000 57.114  ? 188 SER LLL N   1 
ATOM   4648  C CA  . SER C 3 188 ? 54.359  85.357  62.029  1.000 58.415  ? 188 SER LLL CA  1 
ATOM   4649  C C   . SER C 3 188 ? 55.268  85.171  63.251  1.000 56.641  ? 188 SER LLL C   1 
ATOM   4650  O O   . SER C 3 188 ? 54.875  85.584  64.368  1.000 48.964  ? 188 SER LLL O   1 
ATOM   4651  C CB  . SER C 3 188 ? 54.768  86.594  61.257  1.000 60.784  ? 188 SER LLL CB  1 
ATOM   4652  O OG  . SER C 3 188 ? 54.683  87.770  62.059  1.000 60.626  ? 188 SER LLL OG  1 
ATOM   4653  N N   . LYS C 3 189 ? 56.446  84.580  63.037  1.000 57.872  ? 189 LYS LLL N   1 
ATOM   4654  C CA  . LYS C 3 189 ? 57.424  84.313  64.120  1.000 59.790  ? 189 LYS LLL CA  1 
ATOM   4655  C C   . LYS C 3 189 ? 57.746  85.636  64.812  1.000 59.106  ? 189 LYS LLL C   1 
ATOM   4656  O O   . LYS C 3 189 ? 57.773  85.665  66.063  1.000 56.456  ? 189 LYS LLL O   1 
ATOM   4657  C CB  . LYS C 3 189 ? 58.710  83.684  63.588  1.000 62.046  ? 189 LYS LLL CB  1 
ATOM   4658  C CG  . LYS C 3 189 ? 59.701  83.338  64.687  1.000 68.522  ? 189 LYS LLL CG  1 
ATOM   4659  C CD  . LYS C 3 189 ? 61.118  83.173  64.206  1.000 79.081  ? 189 LYS LLL CD  1 
ATOM   4660  C CE  . LYS C 3 189 ? 62.051  82.812  65.343  1.000 85.483  ? 189 LYS LLL CE  1 
ATOM   4661  N NZ  . LYS C 3 189 ? 63.456  82.712  64.880  1.000 92.213  ? 189 LYS LLL NZ  1 
ATOM   4662  N N   . ALA C 3 190 ? 57.998  86.671  64.005  1.000 57.580  ? 190 ALA LLL N   1 
ATOM   4663  C CA  . ALA C 3 190 ? 58.178  88.075  64.430  1.000 58.061  ? 190 ALA LLL CA  1 
ATOM   4664  C C   . ALA C 3 190 ? 57.110  88.444  65.468  1.000 60.766  ? 190 ALA LLL C   1 
ATOM   4665  O O   . ALA C 3 190 ? 57.476  88.678  66.642  1.000 62.906  ? 190 ALA LLL O   1 
ATOM   4666  C CB  . ALA C 3 190 ? 58.112  88.981  63.226  1.000 57.829  ? 190 ALA LLL CB  1 
ATOM   4667  N N   . ASP C 3 191 ? 55.837  88.471  65.061  1.000 61.190  ? 191 ASP LLL N   1 
ATOM   4668  C CA  . ASP C 3 191 ? 54.707  88.943  65.907  1.000 61.400  ? 191 ASP LLL CA  1 
ATOM   4669  C C   . ASP C 3 191 ? 54.541  88.012  67.113  1.000 55.711  ? 191 ASP LLL C   1 
ATOM   4670  O O   . ASP C 3 191 ? 54.073  88.509  68.152  1.000 57.885  ? 191 ASP LLL O   1 
ATOM   4671  C CB  . ASP C 3 191 ? 53.424  89.122  65.091  1.000 65.458  ? 191 ASP LLL CB  1 
ATOM   4672  C CG  . ASP C 3 191 ? 53.514  90.261  64.075  1.000 70.676  ? 191 ASP LLL CG  1 
ATOM   4673  O OD1 . ASP C 3 191 ? 54.426  91.091  64.196  1.000 73.526  ? 191 ASP LLL OD1 1 
ATOM   4674  O OD2 . ASP C 3 191 ? 52.679  90.313  63.157  1.000 71.294  ? 191 ASP LLL OD2 1 
ATOM   4675  N N   . TYR C 3 192 ? 54.921  86.734  67.004  1.000 49.500  ? 192 TYR LLL N   1 
ATOM   4676  C CA  . TYR C 3 192 ? 54.814  85.771  68.132  1.000 49.988  ? 192 TYR LLL CA  1 
ATOM   4677  C C   . TYR C 3 192 ? 55.748  86.229  69.261  1.000 52.360  ? 192 TYR LLL C   1 
ATOM   4678  O O   . TYR C 3 192 ? 55.355  86.149  70.450  1.000 47.502  ? 192 TYR LLL O   1 
ATOM   4679  C CB  . TYR C 3 192 ? 55.079  84.314  67.716  1.000 47.998  ? 192 TYR LLL CB  1 
ATOM   4680  C CG  . TYR C 3 192 ? 55.031  83.328  68.870  1.000 42.121  ? 192 TYR LLL CG  1 
ATOM   4681  C CD1 . TYR C 3 192 ? 53.851  83.085  69.557  1.000 38.765  ? 192 TYR LLL CD1 1 
ATOM   4682  C CD2 . TYR C 3 192 ? 56.168  82.661  69.309  1.000 38.886  ? 192 TYR LLL CD2 1 
ATOM   4683  C CE1 . TYR C 3 192 ? 53.805  82.223  70.643  1.000 38.172  ? 192 TYR LLL CE1 1 
ATOM   4684  C CE2 . TYR C 3 192 ? 56.135  81.790  70.389  1.000 37.426  ? 192 TYR LLL CE2 1 
ATOM   4685  C CZ  . TYR C 3 192 ? 54.949  81.575  71.065  1.000 36.345  ? 192 TYR LLL CZ  1 
ATOM   4686  O OH  . TYR C 3 192 ? 54.882  80.734  72.137  1.000 34.110  ? 192 TYR LLL OH  1 
ATOM   4687  N N   . GLU C 3 193 ? 56.947  86.704  68.905  1.000 58.384  ? 193 GLU LLL N   1 
ATOM   4688  C CA  . GLU C 3 193 ? 58.059  86.924  69.874  1.000 65.088  ? 193 GLU LLL CA  1 
ATOM   4689  C C   . GLU C 3 193 ? 58.001  88.345  70.442  1.000 68.413  ? 193 GLU LLL C   1 
ATOM   4690  O O   . GLU C 3 193 ? 58.825  88.638  71.307  1.000 70.146  ? 193 GLU LLL O   1 
ATOM   4691  C CB  . GLU C 3 193 ? 59.397  86.569  69.226  1.000 69.882  ? 193 GLU LLL CB  1 
ATOM   4692  C CG  . GLU C 3 193 ? 59.634  85.061  69.216  1.000 77.184  ? 193 GLU LLL CG  1 
ATOM   4693  C CD  . GLU C 3 193 ? 60.796  84.531  68.396  1.000 80.241  ? 193 GLU LLL CD  1 
ATOM   4694  O OE1 . GLU C 3 193 ? 61.515  85.371  67.810  1.000 76.891  ? 193 GLU LLL OE1 1 
ATOM   4695  O OE2 . GLU C 3 193 ? 60.959  83.275  68.342  1.000 75.457  ? 193 GLU LLL OE2 1 
ATOM   4696  N N   . LYS C 3 194 ? 57.031  89.163  70.019  1.000 71.991  ? 194 LYS LLL N   1 
ATOM   4697  C CA  . LYS C 3 194 ? 56.789  90.525  70.566  1.000 66.783  ? 194 LYS LLL CA  1 
ATOM   4698  C C   . LYS C 3 194 ? 56.033  90.438  71.886  1.000 62.186  ? 194 LYS LLL C   1 
ATOM   4699  O O   . LYS C 3 194 ? 56.059  91.414  72.613  1.000 78.974  ? 194 LYS LLL O   1 
ATOM   4700  C CB  . LYS C 3 194 ? 55.960  91.389  69.615  1.000 67.700  ? 194 LYS LLL CB  1 
ATOM   4701  C CG  . LYS C 3 194 ? 56.508  91.455  68.203  1.000 76.812  ? 194 LYS LLL CG  1 
ATOM   4702  C CD  . LYS C 3 194 ? 55.793  92.442  67.327  1.000 77.660  ? 194 LYS LLL CD  1 
ATOM   4703  C CE  . LYS C 3 194 ? 56.339  93.838  67.471  1.000 84.886  ? 194 LYS LLL CE  1 
ATOM   4704  N NZ  . LYS C 3 194 ? 56.425  94.505  66.150  1.000 92.761  ? 194 LYS LLL NZ  1 
ATOM   4705  N N   . HIS C 3 195 ? 55.366  89.328  72.172  1.000 56.923  ? 195 HIS LLL N   1 
ATOM   4706  C CA  . HIS C 3 195 ? 54.436  89.212  73.319  1.000 54.999  ? 195 HIS LLL CA  1 
ATOM   4707  C C   . HIS C 3 195 ? 54.867  88.085  74.249  1.000 50.271  ? 195 HIS LLL C   1 
ATOM   4708  O O   . HIS C 3 195 ? 55.728  87.309  73.853  1.000 54.969  ? 195 HIS LLL O   1 
ATOM   4709  C CB  . HIS C 3 195 ? 53.010  89.049  72.803  1.000 56.609  ? 195 HIS LLL CB  1 
ATOM   4710  C CG  . HIS C 3 195 ? 52.628  90.068  71.787  1.000 61.704  ? 195 HIS LLL CG  1 
ATOM   4711  N ND1 . HIS C 3 195 ? 52.285  89.724  70.486  1.000 67.506  ? 195 HIS LLL ND1 1 
ATOM   4712  C CD2 . HIS C 3 195 ? 52.497  91.405  71.882  1.000 62.535  ? 195 HIS LLL CD2 1 
ATOM   4713  C CE1 . HIS C 3 195 ? 51.961  90.808  69.820  1.000 69.644  ? 195 HIS LLL CE1 1 
ATOM   4714  N NE2 . HIS C 3 195 ? 52.092  91.853  70.655  1.000 73.034  ? 195 HIS LLL NE2 1 
ATOM   4715  N N   . LYS C 3 196 ? 54.265  88.024  75.432  1.000 51.714  ? 196 LYS LLL N   1 
ATOM   4716  C CA  . LYS C 3 196 ? 54.650  87.106  76.531  1.000 59.866  ? 196 LYS LLL CA  1 
ATOM   4717  C C   . LYS C 3 196 ? 53.480  86.160  76.823  1.000 58.515  ? 196 LYS LLL C   1 
ATOM   4718  O O   . LYS C 3 196 ? 53.673  84.936  76.690  1.000 60.396  ? 196 LYS LLL O   1 
ATOM   4719  C CB  . LYS C 3 196 ? 55.068  87.922  77.762  1.000 72.306  ? 196 LYS LLL CB  1 
ATOM   4720  C CG  . LYS C 3 196 ? 55.565  87.137  78.980  1.000 80.584  ? 196 LYS LLL CG  1 
ATOM   4721  C CD  . LYS C 3 196 ? 56.632  86.078  78.693  1.000 91.106  ? 196 LYS LLL CD  1 
ATOM   4722  C CE  . LYS C 3 196 ? 57.786  86.533  77.804  1.000 96.316  ? 196 LYS LLL CE  1 
ATOM   4723  N NZ  . LYS C 3 196 ? 58.701  87.492  78.471  1.000 100.525 ? 196 LYS LLL NZ  1 
ATOM   4724  N N   . VAL C 3 197 ? 52.320  86.711  77.201  1.000 53.641  ? 197 VAL LLL N   1 
ATOM   4725  C CA  . VAL C 3 197 ? 51.143  85.929  77.674  1.000 48.294  ? 197 VAL LLL CA  1 
ATOM   4726  C C   . VAL C 3 197 ? 50.193  85.679  76.507  1.000 49.572  ? 197 VAL LLL C   1 
ATOM   4727  O O   . VAL C 3 197 ? 49.545  86.644  76.051  1.000 53.455  ? 197 VAL LLL O   1 
ATOM   4728  C CB  . VAL C 3 197 ? 50.417  86.649  78.815  1.000 46.723  ? 197 VAL LLL CB  1 
ATOM   4729  C CG1 . VAL C 3 197 ? 49.111  85.963  79.202  1.000 47.903  ? 197 VAL LLL CG1 1 
ATOM   4730  C CG2 . VAL C 3 197 ? 51.329  86.772  80.015  1.000 47.285  ? 197 VAL LLL CG2 1 
ATOM   4731  N N   . TYR C 3 198 ? 50.085  84.417  76.097  1.000 46.482  ? 198 TYR LLL N   1 
ATOM   4732  C CA  . TYR C 3 198 ? 49.059  83.922  75.155  1.000 43.690  ? 198 TYR LLL CA  1 
ATOM   4733  C C   . TYR C 3 198 ? 47.979  83.210  75.961  1.000 44.012  ? 198 TYR LLL C   1 
ATOM   4734  O O   . TYR C 3 198 ? 48.332  82.300  76.705  1.000 44.841  ? 198 TYR LLL O   1 
ATOM   4735  C CB  . TYR C 3 198 ? 49.736  83.018  74.139  1.000 41.799  ? 198 TYR LLL CB  1 
ATOM   4736  C CG  . TYR C 3 198 ? 50.591  83.800  73.190  1.000 39.394  ? 198 TYR LLL CG  1 
ATOM   4737  C CD1 . TYR C 3 198 ? 50.088  84.241  71.975  1.000 39.474  ? 198 TYR LLL CD1 1 
ATOM   4738  C CD2 . TYR C 3 198 ? 51.883  84.133  73.532  1.000 39.375  ? 198 TYR LLL CD2 1 
ATOM   4739  C CE1 . TYR C 3 198 ? 50.863  84.975  71.095  1.000 39.987  ? 198 TYR LLL CE1 1 
ATOM   4740  C CE2 . TYR C 3 198 ? 52.678  84.860  72.665  1.000 41.706  ? 198 TYR LLL CE2 1 
ATOM   4741  C CZ  . TYR C 3 198 ? 52.165  85.281  71.448  1.000 42.427  ? 198 TYR LLL CZ  1 
ATOM   4742  O OH  . TYR C 3 198 ? 52.955  86.019  70.617  1.000 46.823  ? 198 TYR LLL OH  1 
ATOM   4743  N N   . ALA C 3 199 ? 46.724  83.636  75.835  1.000 45.382  ? 199 ALA LLL N   1 
ATOM   4744  C CA  . ALA C 3 199 ? 45.603  83.117  76.652  1.000 46.938  ? 199 ALA LLL CA  1 
ATOM   4745  C C   . ALA C 3 199 ? 44.392  82.810  75.782  1.000 46.400  ? 199 ALA LLL C   1 
ATOM   4746  O O   . ALA C 3 199 ? 44.183  83.433  74.736  1.000 47.667  ? 199 ALA LLL O   1 
ATOM   4747  C CB  . ALA C 3 199 ? 45.218  84.087  77.737  1.000 50.454  ? 199 ALA LLL CB  1 
ATOM   4748  N N   . CYS C 3 200 ? 43.601  81.881  76.270  1.000 46.483  ? 200 CYS LLL N   1 
ATOM   4749  C CA  . CYS C 3 200 ? 42.432  81.343  75.578  1.000 48.727  ? 200 CYS LLL CA  1 
ATOM   4750  C C   . CYS C 3 200 ? 41.300  81.382  76.593  1.000 49.380  ? 200 CYS LLL C   1 
ATOM   4751  O O   . CYS C 3 200 ? 41.375  80.627  77.570  1.000 48.866  ? 200 CYS LLL O   1 
ATOM   4752  C CB  . CYS C 3 200 ? 42.732  79.931  75.099  1.000 54.064  ? 200 CYS LLL CB  1 
ATOM   4753  S SG  . CYS C 3 200 ? 41.320  79.240  74.213  1.000 68.506  ? 200 CYS LLL SG  1 
ATOM   4754  N N   . GLU C 3 201 ? 40.336  82.281  76.407  1.000 53.308  ? 201 GLU LLL N   1 
ATOM   4755  C CA  . GLU C 3 201 ? 39.195  82.471  77.338  1.000 55.202  ? 201 GLU LLL CA  1 
ATOM   4756  C C   . GLU C 3 201 ? 37.945  81.840  76.722  1.000 51.086  ? 201 GLU LLL C   1 
ATOM   4757  O O   . GLU C 3 201 ? 37.475  82.328  75.675  1.000 49.687  ? 201 GLU LLL O   1 
ATOM   4758  C CB  . GLU C 3 201 ? 38.981  83.958  77.634  1.000 62.818  ? 201 GLU LLL CB  1 
ATOM   4759  C CG  . GLU C 3 201 ? 37.838  84.211  78.606  1.000 69.347  ? 201 GLU LLL CG  1 
ATOM   4760  C CD  . GLU C 3 201 ? 37.343  85.645  78.675  1.000 68.913  ? 201 GLU LLL CD  1 
ATOM   4761  O OE1 . GLU C 3 201 ? 37.443  86.231  79.772  1.000 65.363  ? 201 GLU LLL OE1 1 
ATOM   4762  O OE2 . GLU C 3 201 ? 36.851  86.168  77.635  1.000 73.057  ? 201 GLU LLL OE2 1 
ATOM   4763  N N   . VAL C 3 202 ? 37.418  80.808  77.374  1.000 47.535  ? 202 VAL LLL N   1 
ATOM   4764  C CA  . VAL C 3 202 ? 36.253  80.023  76.877  1.000 51.295  ? 202 VAL LLL CA  1 
ATOM   4765  C C   . VAL C 3 202 ? 35.014  80.371  77.697  1.000 50.101  ? 202 VAL LLL C   1 
ATOM   4766  O O   . VAL C 3 202 ? 35.054  80.179  78.923  1.000 49.466  ? 202 VAL LLL O   1 
ATOM   4767  C CB  . VAL C 3 202 ? 36.533  78.514  76.959  1.000 55.457  ? 202 VAL LLL CB  1 
ATOM   4768  C CG1 . VAL C 3 202 ? 35.288  77.700  76.620  1.000 58.635  ? 202 VAL LLL CG1 1 
ATOM   4769  C CG2 . VAL C 3 202 ? 37.704  78.121  76.074  1.000 54.549  ? 202 VAL LLL CG2 1 
ATOM   4770  N N   . THR C 3 203 ? 33.953  80.818  77.030  1.000 49.955  ? 203 THR LLL N   1 
ATOM   4771  C CA  . THR C 3 203 ? 32.606  81.003  77.628  1.000 50.908  ? 203 THR LLL CA  1 
ATOM   4772  C C   . THR C 3 203 ? 31.652  79.957  77.055  1.000 51.371  ? 203 THR LLL C   1 
ATOM   4773  O O   . THR C 3 203 ? 31.553  79.844  75.821  1.000 48.364  ? 203 THR LLL O   1 
ATOM   4774  C CB  . THR C 3 203 ? 32.054  82.400  77.366  1.000 50.010  ? 203 THR LLL CB  1 
ATOM   4775  O OG1 . THR C 3 203 ? 33.196  83.253  77.419  1.000 51.631  ? 203 THR LLL OG1 1 
ATOM   4776  C CG2 . THR C 3 203 ? 30.978  82.789  78.357  1.000 51.868  ? 203 THR LLL CG2 1 
ATOM   4777  N N   . HIS C 3 204 ? 31.001  79.215  77.939  1.000 53.593  ? 204 HIS LLL N   1 
ATOM   4778  C CA  . HIS C 3 204 ? 30.089  78.105  77.591  1.000 55.032  ? 204 HIS LLL CA  1 
ATOM   4779  C C   . HIS C 3 204 ? 28.980  78.042  78.628  1.000 54.685  ? 204 HIS LLL C   1 
ATOM   4780  O O   . HIS C 3 204 ? 29.223  78.396  79.781  1.000 53.582  ? 204 HIS LLL O   1 
ATOM   4781  C CB  . HIS C 3 204 ? 30.833  76.768  77.529  1.000 55.662  ? 204 HIS LLL CB  1 
ATOM   4782  C CG  . HIS C 3 204 ? 29.962  75.672  77.021  1.000 52.842  ? 204 HIS LLL CG  1 
ATOM   4783  N ND1 . HIS C 3 204 ? 29.466  74.684  77.841  1.000 53.107  ? 204 HIS LLL ND1 1 
ATOM   4784  C CD2 . HIS C 3 204 ? 29.441  75.459  75.798  1.000 51.430  ? 204 HIS LLL CD2 1 
ATOM   4785  C CE1 . HIS C 3 204 ? 28.704  73.878  77.136  1.000 53.904  ? 204 HIS LLL CE1 1 
ATOM   4786  N NE2 . HIS C 3 204 ? 28.673  74.335  75.879  1.000 54.078  ? 204 HIS LLL NE2 1 
ATOM   4787  N N   . GLN C 3 205 ? 27.819  77.569  78.205  1.000 56.565  ? 205 GLN LLL N   1 
ATOM   4788  C CA  . GLN C 3 205 ? 26.609  77.537  79.053  1.000 60.173  ? 205 GLN LLL CA  1 
ATOM   4789  C C   . GLN C 3 205 ? 26.853  76.664  80.296  1.000 54.282  ? 205 GLN LLL C   1 
ATOM   4790  O O   . GLN C 3 205 ? 26.199  76.908  81.295  1.000 64.252  ? 205 GLN LLL O   1 
ATOM   4791  C CB  . GLN C 3 205 ? 25.437  77.097  78.183  1.000 62.242  ? 205 GLN LLL CB  1 
ATOM   4792  C CG  . GLN C 3 205 ? 24.137  76.928  78.946  1.000 64.177  ? 205 GLN LLL CG  1 
ATOM   4793  C CD  . GLN C 3 205 ? 23.122  76.243  78.067  1.000 65.938  ? 205 GLN LLL CD  1 
ATOM   4794  O OE1 . GLN C 3 205 ? 23.124  76.417  76.848  1.000 63.276  ? 205 GLN LLL OE1 1 
ATOM   4795  N NE2 . GLN C 3 205 ? 22.254  75.450  78.677  1.000 67.967  ? 205 GLN LLL NE2 1 
ATOM   4796  N N   . GLY C 3 206 ? 27.766  75.702  80.268  1.000 52.635  ? 206 GLY LLL N   1 
ATOM   4797  C CA  . GLY C 3 206 ? 28.033  74.812  81.422  1.000 54.605  ? 206 GLY LLL CA  1 
ATOM   4798  C C   . GLY C 3 206 ? 29.121  75.345  82.351  1.000 55.666  ? 206 GLY LLL C   1 
ATOM   4799  O O   . GLY C 3 206 ? 29.532  74.609  83.286  1.000 43.362  ? 206 GLY LLL O   1 
ATOM   4800  N N   . LEU C 3 207 ? 29.622  76.555  82.085  1.000 59.098  ? 207 LEU LLL N   1 
ATOM   4801  C CA  . LEU C 3 207 ? 30.667  77.214  82.908  1.000 64.612  ? 207 LEU LLL CA  1 
ATOM   4802  C C   . LEU C 3 207 ? 30.043  78.432  83.584  1.000 69.263  ? 207 LEU LLL C   1 
ATOM   4803  O O   . LEU C 3 207 ? 29.708  79.378  82.842  1.000 79.802  ? 207 LEU LLL O   1 
ATOM   4804  C CB  . LEU C 3 207 ? 31.827  77.655  82.008  1.000 63.023  ? 207 LEU LLL CB  1 
ATOM   4805  C CG  . LEU C 3 207 ? 32.685  76.539  81.419  1.000 58.635  ? 207 LEU LLL CG  1 
ATOM   4806  C CD1 . LEU C 3 207 ? 33.694  77.120  80.431  1.000 58.130  ? 207 LEU LLL CD1 1 
ATOM   4807  C CD2 . LEU C 3 207 ? 33.388  75.745  82.518  1.000 55.215  ? 207 LEU LLL CD2 1 
ATOM   4808  N N   . SER C 3 208 ? 29.912  78.411  84.916  1.000 73.192  ? 208 SER LLL N   1 
ATOM   4809  C CA  . SER C 3 208 ? 29.374  79.528  85.746  1.000 76.506  ? 208 SER LLL CA  1 
ATOM   4810  C C   . SER C 3 208 ? 30.136  80.827  85.441  1.000 71.972  ? 208 SER LLL C   1 
ATOM   4811  O O   . SER C 3 208 ? 29.518  81.916  85.413  1.000 67.850  ? 208 SER LLL O   1 
ATOM   4812  C CB  . SER C 3 208 ? 29.443  79.195  87.217  1.000 80.085  ? 208 SER LLL CB  1 
ATOM   4813  O OG  . SER C 3 208 ? 30.792  79.089  87.646  1.000 80.195  ? 208 SER LLL OG  1 
ATOM   4814  N N   . SER C 3 209 ? 31.439  80.698  85.208  1.000 67.883  ? 209 SER LLL N   1 
ATOM   4815  C CA  . SER C 3 209 ? 32.363  81.812  84.905  1.000 66.889  ? 209 SER LLL CA  1 
ATOM   4816  C C   . SER C 3 209 ? 33.289  81.406  83.756  1.000 64.634  ? 209 SER LLL C   1 
ATOM   4817  O O   . SER C 3 209 ? 33.725  80.263  83.693  1.000 60.188  ? 209 SER LLL O   1 
ATOM   4818  C CB  . SER C 3 209 ? 33.098  82.170  86.160  1.000 66.778  ? 209 SER LLL CB  1 
ATOM   4819  O OG  . SER C 3 209 ? 34.280  82.870  85.852  1.000 77.792  ? 209 SER LLL OG  1 
ATOM   4820  N N   . PRO C 3 210 ? 33.561  82.295  82.775  1.000 65.944  ? 210 PRO LLL N   1 
ATOM   4821  C CA  . PRO C 3 210 ? 34.503  82.002  81.690  1.000 64.416  ? 210 PRO LLL CA  1 
ATOM   4822  C C   . PRO C 3 210 ? 35.881  81.499  82.148  1.000 63.543  ? 210 PRO LLL C   1 
ATOM   4823  O O   . PRO C 3 210 ? 36.525  82.188  82.892  1.000 69.752  ? 210 PRO LLL O   1 
ATOM   4824  C CB  . PRO C 3 210 ? 34.667  83.350  80.973  1.000 61.131  ? 210 PRO LLL CB  1 
ATOM   4825  C CG  . PRO C 3 210 ? 33.363  84.079  81.250  1.000 64.583  ? 210 PRO LLL CG  1 
ATOM   4826  C CD  . PRO C 3 210 ? 32.904  83.598  82.610  1.000 67.813  ? 210 PRO LLL CD  1 
ATOM   4827  N N   . VAL C 3 211 ? 36.298  80.321  81.668  1.000 61.243  ? 211 VAL LLL N   1 
ATOM   4828  C CA  . VAL C 3 211 ? 37.603  79.676  82.001  1.000 59.802  ? 211 VAL LLL CA  1 
ATOM   4829  C C   . VAL C 3 211 ? 38.673  80.137  81.005  1.000 59.251  ? 211 VAL LLL C   1 
ATOM   4830  O O   . VAL C 3 211 ? 38.406  80.138  79.784  1.000 58.235  ? 211 VAL LLL O   1 
ATOM   4831  C CB  . VAL C 3 211 ? 37.503  78.140  82.002  1.000 61.552  ? 211 VAL LLL CB  1 
ATOM   4832  C CG1 . VAL C 3 211 ? 38.872  77.493  82.152  1.000 62.070  ? 211 VAL LLL CG1 1 
ATOM   4833  C CG2 . VAL C 3 211 ? 36.547  77.624  83.073  1.000 63.791  ? 211 VAL LLL CG2 1 
ATOM   4834  N N   . THR C 3 212 ? 39.850  80.482  81.526  1.000 55.226  ? 212 THR LLL N   1 
ATOM   4835  C CA  . THR C 3 212 ? 41.045  80.913  80.756  1.000 52.279  ? 212 THR LLL CA  1 
ATOM   4836  C C   . THR C 3 212 ? 42.184  79.929  81.031  1.000 48.283  ? 212 THR LLL C   1 
ATOM   4837  O O   . THR C 3 212 ? 42.445  79.644  82.201  1.000 47.132  ? 212 THR LLL O   1 
ATOM   4838  C CB  . THR C 3 212 ? 41.490  82.331  81.139  1.000 52.481  ? 212 THR LLL CB  1 
ATOM   4839  O OG1 . THR C 3 212 ? 40.353  83.189  81.080  1.000 54.342  ? 212 THR LLL OG1 1 
ATOM   4840  C CG2 . THR C 3 212 ? 42.582  82.878  80.246  1.000 51.720  ? 212 THR LLL CG2 1 
ATOM   4841  N N   . LYS C 3 213 ? 42.818  79.414  79.985  1.000 45.024  ? 213 LYS LLL N   1 
ATOM   4842  C CA  . LYS C 3 213 ? 44.107  78.699  80.079  1.000 44.447  ? 213 LYS LLL CA  1 
ATOM   4843  C C   . LYS C 3 213 ? 45.084  79.519  79.255  1.000 43.723  ? 213 LYS LLL C   1 
ATOM   4844  O O   . LYS C 3 213 ? 44.686  79.992  78.180  1.000 45.224  ? 213 LYS LLL O   1 
ATOM   4845  C CB  . LYS C 3 213 ? 44.014  77.277  79.531  1.000 48.105  ? 213 LYS LLL CB  1 
ATOM   4846  C CG  . LYS C 3 213 ? 42.763  76.507  79.922  1.000 52.447  ? 213 LYS LLL CG  1 
ATOM   4847  C CD  . LYS C 3 213 ? 42.706  76.156  81.387  1.000 56.012  ? 213 LYS LLL CD  1 
ATOM   4848  C CE  . LYS C 3 213 ? 43.539  74.948  81.736  1.000 63.548  ? 213 LYS LLL CE  1 
ATOM   4849  N NZ  . LYS C 3 213 ? 42.981  74.262  82.925  1.000 71.225  ? 213 LYS LLL NZ  1 
ATOM   4850  N N   . SER C 3 214 ? 46.297  79.706  79.754  1.000 42.724  ? 214 SER LLL N   1 
ATOM   4851  C CA  . SER C 3 214 ? 47.297  80.564  79.082  1.000 45.307  ? 214 SER LLL CA  1 
ATOM   4852  C C   . SER C 3 214 ? 48.691  79.994  79.309  1.000 43.416  ? 214 SER LLL C   1 
ATOM   4853  O O   . SER C 3 214 ? 48.819  79.045  80.068  1.000 45.266  ? 214 SER LLL O   1 
ATOM   4854  C CB  . SER C 3 214 ? 47.184  81.982  79.580  1.000 49.858  ? 214 SER LLL CB  1 
ATOM   4855  O OG  . SER C 3 214 ? 47.801  82.136  80.844  1.000 53.958  ? 214 SER LLL OG  1 
ATOM   4856  N N   . PHE C 3 215 ? 49.692  80.583  78.676  1.000 45.004  ? 215 PHE LLL N   1 
ATOM   4857  C CA  . PHE C 3 215 ? 51.114  80.223  78.860  1.000 47.664  ? 215 PHE LLL CA  1 
ATOM   4858  C C   . PHE C 3 215 ? 51.973  81.441  78.526  1.000 50.718  ? 215 PHE LLL C   1 
ATOM   4859  O O   . PHE C 3 215 ? 51.534  82.297  77.725  1.000 49.405  ? 215 PHE LLL O   1 
ATOM   4860  C CB  . PHE C 3 215 ? 51.486  79.031  77.980  1.000 46.808  ? 215 PHE LLL CB  1 
ATOM   4861  C CG  . PHE C 3 215 ? 51.504  79.354  76.514  1.000 44.033  ? 215 PHE LLL CG  1 
ATOM   4862  C CD1 . PHE C 3 215 ? 50.357  79.228  75.761  1.000 42.394  ? 215 PHE LLL CD1 1 
ATOM   4863  C CD2 . PHE C 3 215 ? 52.652  79.830  75.907  1.000 46.765  ? 215 PHE LLL CD2 1 
ATOM   4864  C CE1 . PHE C 3 215 ? 50.360  79.544  74.413  1.000 43.197  ? 215 PHE LLL CE1 1 
ATOM   4865  C CE2 . PHE C 3 215 ? 52.652  80.166  74.561  1.000 50.557  ? 215 PHE LLL CE2 1 
ATOM   4866  C CZ  . PHE C 3 215 ? 51.508  80.010  73.813  1.000 47.244  ? 215 PHE LLL CZ  1 
ATOM   4867  N N   . ASN C 3 216 ? 53.157  81.496  79.134  1.000 53.652  ? 216 ASN LLL N   1 
ATOM   4868  C CA  . ASN C 3 216 ? 54.147  82.583  78.957  1.000 55.507  ? 216 ASN LLL CA  1 
ATOM   4869  C C   . ASN C 3 216 ? 55.183  82.071  77.958  1.000 48.607  ? 216 ASN LLL C   1 
ATOM   4870  O O   . ASN C 3 216 ? 55.681  80.974  78.186  1.000 51.728  ? 216 ASN LLL O   1 
ATOM   4871  C CB  . ASN C 3 216 ? 54.726  82.989  80.319  1.000 61.994  ? 216 ASN LLL CB  1 
ATOM   4872  C CG  . ASN C 3 216 ? 53.711  83.697  81.198  1.000 64.419  ? 216 ASN LLL CG  1 
ATOM   4873  O OD1 . ASN C 3 216 ? 52.504  83.490  81.065  1.000 66.844  ? 216 ASN LLL OD1 1 
ATOM   4874  N ND2 . ASN C 3 216 ? 54.196  84.547  82.092  1.000 71.386  ? 216 ASN LLL ND2 1 
ATOM   4875  N N   . ARG C 3 217 ? 55.469  82.820  76.897  1.000 45.003  ? 217 ARG LLL N   1 
ATOM   4876  C CA  . ARG C 3 217 ? 56.379  82.372  75.817  1.000 50.544  ? 217 ARG LLL CA  1 
ATOM   4877  C C   . ARG C 3 217 ? 57.736  81.984  76.419  1.000 55.407  ? 217 ARG LLL C   1 
ATOM   4878  O O   . ARG C 3 217 ? 58.289  82.766  77.177  1.000 54.861  ? 217 ARG LLL O   1 
ATOM   4879  C CB  . ARG C 3 217 ? 56.551  83.466  74.768  1.000 53.062  ? 217 ARG LLL CB  1 
ATOM   4880  C CG  . ARG C 3 217 ? 57.413  83.051  73.588  1.000 57.187  ? 217 ARG LLL CG  1 
ATOM   4881  C CD  . ARG C 3 217 ? 57.342  84.102  72.503  1.000 61.348  ? 217 ARG LLL CD  1 
ATOM   4882  N NE  . ARG C 3 217 ? 57.570  85.411  73.087  1.000 61.067  ? 217 ARG LLL NE  1 
ATOM   4883  C CZ  . ARG C 3 217 ? 58.753  85.891  73.438  1.000 59.302  ? 217 ARG LLL CZ  1 
ATOM   4884  N NH1 . ARG C 3 217 ? 59.850  85.187  73.253  1.000 63.689  ? 217 ARG LLL NH1 1 
ATOM   4885  N NH2 . ARG C 3 217 ? 58.839  87.086  73.981  1.000 64.410  ? 217 ARG LLL NH2 1 
ATOM   4886  N N   . GLY C 3 218 ? 58.236  80.793  76.086  1.000 69.496  ? 218 GLY LLL N   1 
ATOM   4887  C CA  . GLY C 3 218 ? 59.521  80.232  76.561  1.000 70.130  ? 218 GLY LLL CA  1 
ATOM   4888  C C   . GLY C 3 218 ? 59.424  79.679  77.977  1.000 77.134  ? 218 GLY LLL C   1 
ATOM   4889  O O   . GLY C 3 218 ? 60.088  80.253  78.841  1.000 82.461  ? 218 GLY LLL O   1 
ATOM   4890  N N   . GLU C 3 219 ? 58.622  78.618  78.188  1.000 85.485  ? 219 GLU LLL N   1 
ATOM   4891  C CA  . GLU C 3 219 ? 58.480  77.826  79.446  1.000 87.026  ? 219 GLU LLL CA  1 
ATOM   4892  C C   . GLU C 3 219 ? 57.825  76.479  79.100  1.000 90.032  ? 219 GLU LLL C   1 
ATOM   4893  O O   . GLU C 3 219 ? 57.111  75.840  79.871  1.000 90.664  ? 219 GLU LLL O   1 
ATOM   4894  C CB  . GLU C 3 219 ? 57.666  78.600  80.488  1.000 85.222  ? 219 GLU LLL CB  1 
ATOM   4895  C CG  . GLU C 3 219 ? 58.293  79.931  80.878  1.000 87.949  ? 219 GLU LLL CG  1 
ATOM   4896  C CD  . GLU C 3 219 ? 57.540  80.778  81.888  1.000 99.451  ? 219 GLU LLL CD  1 
ATOM   4897  O OE1 . GLU C 3 219 ? 56.691  80.224  82.604  1.000 114.685 ? 219 GLU LLL OE1 1 
ATOM   4898  O OE2 . GLU C 3 219 ? 57.825  81.996  81.958  1.000 103.276 ? 219 GLU LLL OE2 1 
ATOM   4899  N N   . THR D 1 15  ? -4.418  71.757  91.684  1.000 142.440 ? 333 THR AAA N   1 
ATOM   4900  C CA  . THR D 1 15  ? -5.112  71.245  92.914  1.000 148.611 ? 333 THR AAA CA  1 
ATOM   4901  C C   . THR D 1 15  ? -4.607  69.831  93.254  1.000 150.515 ? 333 THR AAA C   1 
ATOM   4902  O O   . THR D 1 15  ? -4.271  69.595  94.422  1.000 157.909 ? 333 THR AAA O   1 
ATOM   4903  C CB  . THR D 1 15  ? -6.645  71.230  92.754  1.000 138.548 ? 333 THR AAA CB  1 
ATOM   4904  O OG1 . THR D 1 15  ? -7.131  72.552  92.520  1.000 138.595 ? 333 THR AAA OG1 1 
ATOM   4905  C CG2 . THR D 1 15  ? -7.370  70.678  93.963  1.000 122.216 ? 333 THR AAA CG2 1 
ATOM   4906  N N   . ASN D 1 16  ? -4.568  68.923  92.273  1.000 142.048 ? 334 ASN AAA N   1 
ATOM   4907  C CA  . ASN D 1 16  ? -4.726  67.459  92.502  1.000 133.124 ? 334 ASN AAA CA  1 
ATOM   4908  C C   . ASN D 1 16  ? -3.392  66.705  92.364  1.000 128.515 ? 334 ASN AAA C   1 
ATOM   4909  O O   . ASN D 1 16  ? -3.405  65.647  91.709  1.000 128.141 ? 334 ASN AAA O   1 
ATOM   4910  C CB  . ASN D 1 16  ? -5.855  66.902  91.620  1.000 127.130 ? 334 ASN AAA CB  1 
ATOM   4911  C CG  . ASN D 1 16  ? -5.571  66.887  90.130  1.000 120.663 ? 334 ASN AAA CG  1 
ATOM   4912  O OD1 . ASN D 1 16  ? -4.710  67.609  89.631  1.000 100.643 ? 334 ASN AAA OD1 1 
ATOM   4913  N ND2 . ASN D 1 16  ? -6.303  66.051  89.414  1.000 118.024 ? 334 ASN AAA ND2 1 
ATOM   4914  N N   . LEU D 1 17  ? -2.312  67.154  93.025  1.000 115.122 ? 335 LEU AAA N   1 
ATOM   4915  C CA  . LEU D 1 17  ? -1.124  66.286  93.329  1.000 112.268 ? 335 LEU AAA CA  1 
ATOM   4916  C C   . LEU D 1 17  ? -1.575  65.218  94.342  1.000 116.087 ? 335 LEU AAA C   1 
ATOM   4917  O O   . LEU D 1 17  ? -2.355  65.580  95.235  1.000 106.171 ? 335 LEU AAA O   1 
ATOM   4918  C CB  . LEU D 1 17  ? 0.030   67.137  93.886  1.000 107.214 ? 335 LEU AAA CB  1 
ATOM   4919  C CG  . LEU D 1 17  ? 1.285   66.378  94.348  1.000 108.709 ? 335 LEU AAA CG  1 
ATOM   4920  C CD1 . LEU D 1 17  ? 2.177   65.982  93.173  1.000 105.482 ? 335 LEU AAA CD1 1 
ATOM   4921  C CD2 . LEU D 1 17  ? 2.092   67.202  95.353  1.000 96.875  ? 335 LEU AAA CD2 1 
ATOM   4922  N N   . CYS D 1 18  ? -1.131  63.959  94.221  1.000 122.743 ? 336 CYS AAA N   1 
ATOM   4923  C CA  . CYS D 1 18  ? -1.531  62.846  95.134  1.000 119.993 ? 336 CYS AAA CA  1 
ATOM   4924  C C   . CYS D 1 18  ? -0.949  63.075  96.524  1.000 109.126 ? 336 CYS AAA C   1 
ATOM   4925  O O   . CYS D 1 18  ? 0.236   63.349  96.669  1.000 100.621 ? 336 CYS AAA O   1 
ATOM   4926  C CB  . CYS D 1 18  ? -1.096  61.474  94.630  1.000 125.088 ? 336 CYS AAA CB  1 
ATOM   4927  S SG  . CYS D 1 18  ? -2.099  60.871  93.243  1.000 144.474 ? 336 CYS AAA SG  1 
ATOM   4928  N N   . PRO D 1 19  ? -1.759  62.928  97.595  1.000 109.765 ? 337 PRO AAA N   1 
ATOM   4929  C CA  . PRO D 1 19  ? -1.382  63.433  98.913  1.000 106.188 ? 337 PRO AAA CA  1 
ATOM   4930  C C   . PRO D 1 19  ? -0.470  62.451  99.661  1.000 109.374 ? 337 PRO AAA C   1 
ATOM   4931  O O   . PRO D 1 19  ? -0.800  62.076  100.773 1.000 118.296 ? 337 PRO AAA O   1 
ATOM   4932  C CB  . PRO D 1 19  ? -2.755  63.582  99.585  1.000 103.148 ? 337 PRO AAA CB  1 
ATOM   4933  C CG  . PRO D 1 19  ? -3.538  62.398  99.041  1.000 104.155 ? 337 PRO AAA CG  1 
ATOM   4934  C CD  . PRO D 1 19  ? -3.063  62.239  97.608  1.000 107.030 ? 337 PRO AAA CD  1 
ATOM   4935  N N   . PHE D 1 20  ? 0.639   62.040  99.039  1.000 102.430 ? 338 PHE AAA N   1 
ATOM   4936  C CA  . PHE D 1 20  ? 1.681   61.201  99.685  1.000 95.080  ? 338 PHE AAA CA  1 
ATOM   4937  C C   . PHE D 1 20  ? 2.321   61.989  100.838 1.000 89.944  ? 338 PHE AAA C   1 
ATOM   4938  O O   . PHE D 1 20  ? 2.776   61.342  101.821 1.000 83.683  ? 338 PHE AAA O   1 
ATOM   4939  C CB  . PHE D 1 20  ? 2.730   60.735  98.672  1.000 93.485  ? 338 PHE AAA CB  1 
ATOM   4940  C CG  . PHE D 1 20  ? 2.264   59.693  97.686  1.000 96.891  ? 338 PHE AAA CG  1 
ATOM   4941  C CD1 . PHE D 1 20  ? 1.672   58.517  98.121  1.000 99.433  ? 338 PHE AAA CD1 1 
ATOM   4942  C CD2 . PHE D 1 20  ? 2.449   59.869  96.322  1.000 103.893 ? 338 PHE AAA CD2 1 
ATOM   4943  C CE1 . PHE D 1 20  ? 1.250   57.552  97.215  1.000 100.857 ? 338 PHE AAA CE1 1 
ATOM   4944  C CE2 . PHE D 1 20  ? 2.022   58.908  95.416  1.000 108.014 ? 338 PHE AAA CE2 1 
ATOM   4945  C CZ  . PHE D 1 20  ? 1.445   57.740  95.863  1.000 103.074 ? 338 PHE AAA CZ  1 
ATOM   4946  N N   . GLY D 1 21  ? 2.354   63.326  100.724 1.000 82.864  ? 339 GLY AAA N   1 
ATOM   4947  C CA  . GLY D 1 21  ? 2.900   64.234  101.750 1.000 84.044  ? 339 GLY AAA CA  1 
ATOM   4948  C C   . GLY D 1 21  ? 2.303   63.938  103.112 1.000 85.199  ? 339 GLY AAA C   1 
ATOM   4949  O O   . GLY D 1 21  ? 3.069   63.725  104.079 1.000 86.336  ? 339 GLY AAA O   1 
ATOM   4950  N N   . GLU D 1 22  ? 0.971   63.877  103.170 1.000 89.465  ? 340 GLU AAA N   1 
ATOM   4951  C CA  . GLU D 1 22  ? 0.198   63.710  104.433 1.000 96.988  ? 340 GLU AAA CA  1 
ATOM   4952  C C   . GLU D 1 22  ? 0.233   62.241  104.906 1.000 86.689  ? 340 GLU AAA C   1 
ATOM   4953  O O   . GLU D 1 22  ? -0.142  62.030  106.070 1.000 85.031  ? 340 GLU AAA O   1 
ATOM   4954  C CB  . GLU D 1 22  ? -1.228  64.267  104.277 1.000 103.889 ? 340 GLU AAA CB  1 
ATOM   4955  C CG  . GLU D 1 22  ? -2.208  63.335  103.569 1.000 113.396 ? 340 GLU AAA CG  1 
ATOM   4956  C CD  . GLU D 1 22  ? -3.618  63.874  103.352 1.000 113.215 ? 340 GLU AAA CD  1 
ATOM   4957  O OE1 . GLU D 1 22  ? -3.783  64.806  102.536 1.000 104.027 ? 340 GLU AAA OE1 1 
ATOM   4958  O OE2 . GLU D 1 22  ? -4.559  63.358  103.998 1.000 111.284 ? 340 GLU AAA OE2 1 
ATOM   4959  N N   . VAL D 1 23  ? 0.662   61.277  104.072 1.000 74.431  ? 341 VAL AAA N   1 
ATOM   4960  C CA  . VAL D 1 23  ? 0.733   59.822  104.428 1.000 71.485  ? 341 VAL AAA CA  1 
ATOM   4961  C C   . VAL D 1 23  ? 2.070   59.531  105.113 1.000 75.497  ? 341 VAL AAA C   1 
ATOM   4962  O O   . VAL D 1 23  ? 2.084   58.739  106.115 1.000 69.302  ? 341 VAL AAA O   1 
ATOM   4963  C CB  . VAL D 1 23  ? 0.584   58.900  103.202 1.000 68.078  ? 341 VAL AAA CB  1 
ATOM   4964  C CG1 . VAL D 1 23  ? 0.724   57.435  103.593 1.000 67.352  ? 341 VAL AAA CG1 1 
ATOM   4965  C CG2 . VAL D 1 23  ? -0.725  59.131  102.463 1.000 70.050  ? 341 VAL AAA CG2 1 
ATOM   4966  N N   . PHE D 1 24  ? 3.141   60.104  104.545 1.000 74.331  ? 342 PHE AAA N   1 
ATOM   4967  C CA  . PHE D 1 24  ? 4.559   59.845  104.913 1.000 70.246  ? 342 PHE AAA CA  1 
ATOM   4968  C C   . PHE D 1 24  ? 4.974   60.797  106.034 1.000 72.432  ? 342 PHE AAA C   1 
ATOM   4969  O O   . PHE D 1 24  ? 5.639   60.317  106.981 1.000 69.636  ? 342 PHE AAA O   1 
ATOM   4970  C CB  . PHE D 1 24  ? 5.486   60.005  103.704 1.000 66.717  ? 342 PHE AAA CB  1 
ATOM   4971  C CG  . PHE D 1 24  ? 5.581   58.802  102.795 1.000 60.284  ? 342 PHE AAA CG  1 
ATOM   4972  C CD1 . PHE D 1 24  ? 4.670   58.600  101.768 1.000 59.192  ? 342 PHE AAA CD1 1 
ATOM   4973  C CD2 . PHE D 1 24  ? 6.600   57.876  102.956 1.000 56.873  ? 342 PHE AAA CD2 1 
ATOM   4974  C CE1 . PHE D 1 24  ? 4.761   57.491  100.943 1.000 58.580  ? 342 PHE AAA CE1 1 
ATOM   4975  C CE2 . PHE D 1 24  ? 6.703   56.779  102.111 1.000 58.442  ? 342 PHE AAA CE2 1 
ATOM   4976  C CZ  . PHE D 1 24  ? 5.786   56.591  101.104 1.000 56.571  ? 342 PHE AAA CZ  1 
ATOM   4977  N N   . ASN D 1 25  ? 4.598   62.079  105.925 1.000 76.470  ? 343 ASN AAA N   1 
ATOM   4978  C CA  . ASN D 1 25  ? 4.995   63.143  106.889 1.000 82.135  ? 343 ASN AAA CA  1 
ATOM   4979  C C   . ASN D 1 25  ? 3.870   63.321  107.924 1.000 76.687  ? 343 ASN AAA C   1 
ATOM   4980  O O   . ASN D 1 25  ? 3.849   64.361  108.608 1.000 74.366  ? 343 ASN AAA O   1 
ATOM   4981  C CB  . ASN D 1 25  ? 5.385   64.454  106.182 1.000 93.533  ? 343 ASN AAA CB  1 
ATOM   4982  C CG  . ASN D 1 25  ? 6.581   64.349  105.245 1.000 96.339  ? 343 ASN AAA CG  1 
ATOM   4983  O OD1 . ASN D 1 25  ? 7.223   63.301  105.146 1.000 95.765  ? 343 ASN AAA OD1 1 
ATOM   4984  N ND2 . ASN D 1 25  ? 6.840   65.410  104.496 1.000 93.185  ? 343 ASN AAA ND2 1 
ATOM   4985  N N   . ALA D 1 26  ? 2.971   62.338  108.042 1.000 79.413  ? 344 ALA AAA N   1 
ATOM   4986  C CA  . ALA D 1 26  ? 1.907   62.241  109.076 1.000 78.131  ? 344 ALA AAA CA  1 
ATOM   4987  C C   . ALA D 1 26  ? 2.538   62.200  110.470 1.000 71.782  ? 344 ALA AAA C   1 
ATOM   4988  O O   . ALA D 1 26  ? 3.375   61.308  110.704 1.000 67.445  ? 344 ALA AAA O   1 
ATOM   4989  C CB  . ALA D 1 26  ? 1.077   60.999  108.847 1.000 78.213  ? 344 ALA AAA CB  1 
ATOM   4990  N N   . THR D 1 27  ? 2.110   63.082  111.377 1.000 69.665  ? 345 THR AAA N   1 
ATOM   4991  C CA  . THR D 1 27  ? 2.696   63.232  112.738 1.000 68.844  ? 345 THR AAA CA  1 
ATOM   4992  C C   . THR D 1 27  ? 2.375   61.985  113.576 1.000 65.706  ? 345 THR AAA C   1 
ATOM   4993  O O   . THR D 1 27  ? 3.237   61.567  114.357 1.000 57.237  ? 345 THR AAA O   1 
ATOM   4994  C CB  . THR D 1 27  ? 2.242   64.555  113.372 1.000 70.912  ? 345 THR AAA CB  1 
ATOM   4995  O OG1 . THR D 1 27  ? 0.882   64.745  112.985 1.000 69.947  ? 345 THR AAA OG1 1 
ATOM   4996  C CG2 . THR D 1 27  ? 3.058   65.755  112.931 1.000 74.114  ? 345 THR AAA CG2 1 
ATOM   4997  N N   . ARG D 1 28  ? 1.194   61.390  113.391 1.000 71.658  ? 346 ARG AAA N   1 
ATOM   4998  C CA  . ARG D 1 28  ? 0.774   60.127  114.055 1.000 77.746  ? 346 ARG AAA CA  1 
ATOM   4999  C C   . ARG D 1 28  ? 0.807   58.973  113.037 1.000 68.016  ? 346 ARG AAA C   1 
ATOM   5000  O O   . ARG D 1 28  ? 0.262   59.113  111.918 1.000 63.270  ? 346 ARG AAA O   1 
ATOM   5001  C CB  . ARG D 1 28  ? -0.621  60.307  114.668 1.000 103.077 ? 346 ARG AAA CB  1 
ATOM   5002  C CG  . ARG D 1 28  ? -1.381  59.012  114.961 1.000 130.987 ? 346 ARG AAA CG  1 
ATOM   5003  C CD  . ARG D 1 28  ? -2.670  59.203  115.765 1.000 129.043 ? 346 ARG AAA CD  1 
ATOM   5004  N NE  . ARG D 1 28  ? -2.371  59.374  117.184 1.000 138.731 ? 346 ARG AAA NE  1 
ATOM   5005  C CZ  . ARG D 1 28  ? -2.129  60.537  117.796 1.000 136.962 ? 346 ARG AAA CZ  1 
ATOM   5006  N NH1 . ARG D 1 28  ? -2.179  61.684  117.136 1.000 129.337 ? 346 ARG AAA NH1 1 
ATOM   5007  N NH2 . ARG D 1 28  ? -1.838  60.549  119.086 1.000 142.674 ? 346 ARG AAA NH2 1 
ATOM   5008  N N   . PHE D 1 29  ? 1.405   57.848  113.421 1.000 58.799  ? 347 PHE AAA N   1 
ATOM   5009  C CA  . PHE D 1 29  ? 1.334   56.568  112.673 1.000 54.966  ? 347 PHE AAA CA  1 
ATOM   5010  C C   . PHE D 1 29  ? 0.460   55.598  113.460 1.000 49.178  ? 347 PHE AAA C   1 
ATOM   5011  O O   . PHE D 1 29  ? 0.215   55.873  114.642 1.000 54.499  ? 347 PHE AAA O   1 
ATOM   5012  C CB  . PHE D 1 29  ? 2.738   56.009  112.413 1.000 56.815  ? 347 PHE AAA CB  1 
ATOM   5013  C CG  . PHE D 1 29  ? 3.207   56.252  111.002 1.000 51.492  ? 347 PHE AAA CG  1 
ATOM   5014  C CD1 . PHE D 1 29  ? 3.222   57.540  110.482 1.000 47.508  ? 347 PHE AAA CD1 1 
ATOM   5015  C CD2 . PHE D 1 29  ? 3.543   55.191  110.176 1.000 48.865  ? 347 PHE AAA CD2 1 
ATOM   5016  C CE1 . PHE D 1 29  ? 3.590   57.774  109.171 1.000 47.127  ? 347 PHE AAA CE1 1 
ATOM   5017  C CE2 . PHE D 1 29  ? 3.931   55.425  108.869 1.000 48.191  ? 347 PHE AAA CE2 1 
ATOM   5018  C CZ  . PHE D 1 29  ? 3.946   56.713  108.373 1.000 51.066  ? 347 PHE AAA CZ  1 
ATOM   5019  N N   . ALA D 1 30  ? 0.040   54.509  112.815 1.000 43.754  ? 348 ALA AAA N   1 
ATOM   5020  C CA  . ALA D 1 30  ? -0.876  53.484  113.363 1.000 42.897  ? 348 ALA AAA CA  1 
ATOM   5021  C C   . ALA D 1 30  ? -0.098  52.311  113.979 1.000 42.938  ? 348 ALA AAA C   1 
ATOM   5022  O O   . ALA D 1 30  ? 1.044   52.073  113.556 1.000 48.765  ? 348 ALA AAA O   1 
ATOM   5023  C CB  . ALA D 1 30  ? -1.768  53.017  112.250 1.000 41.390  ? 348 ALA AAA CB  1 
ATOM   5024  N N   . SER D 1 31  ? -0.677  51.593  114.945 1.000 44.855  ? 349 SER AAA N   1 
ATOM   5025  C CA  . SER D 1 31  ? -0.147  50.282  115.410 1.000 45.753  ? 349 SER AAA CA  1 
ATOM   5026  C C   . SER D 1 31  ? -0.271  49.279  114.263 1.000 43.648  ? 349 SER AAA C   1 
ATOM   5027  O O   . SER D 1 31  ? -1.262  49.360  113.520 1.000 40.991  ? 349 SER AAA O   1 
ATOM   5028  C CB  . SER D 1 31  ? -0.855  49.782  116.644 1.000 44.272  ? 349 SER AAA CB  1 
ATOM   5029  O OG  . SER D 1 31  ? -0.391  50.454  117.799 1.000 43.984  ? 349 SER AAA OG  1 
ATOM   5030  N N   . VAL D 1 32  ? 0.677   48.357  114.148 1.000 46.403  ? 350 VAL AAA N   1 
ATOM   5031  C CA  . VAL D 1 32  ? 0.709   47.391  113.014 1.000 53.886  ? 350 VAL AAA CA  1 
ATOM   5032  C C   . VAL D 1 32  ? -0.597  46.571  112.932 1.000 58.217  ? 350 VAL AAA C   1 
ATOM   5033  O O   . VAL D 1 32  ? -1.036  46.328  111.791 1.000 61.817  ? 350 VAL AAA O   1 
ATOM   5034  C CB  . VAL D 1 32  ? 1.953   46.485  113.078 1.000 56.235  ? 350 VAL AAA CB  1 
ATOM   5035  C CG1 . VAL D 1 32  ? 1.952   45.589  114.301 1.000 57.948  ? 350 VAL AAA CG1 1 
ATOM   5036  C CG2 . VAL D 1 32  ? 2.106   45.652  111.815 1.000 55.931  ? 350 VAL AAA CG2 1 
ATOM   5037  N N   . TYR D 1 33  ? -1.172  46.112  114.057 1.000 59.239  ? 351 TYR AAA N   1 
ATOM   5038  C CA  . TYR D 1 33  ? -2.344  45.181  114.080 1.000 57.274  ? 351 TYR AAA CA  1 
ATOM   5039  C C   . TYR D 1 33  ? -3.568  45.899  113.492 1.000 51.883  ? 351 TYR AAA C   1 
ATOM   5040  O O   . TYR D 1 33  ? -4.383  45.234  112.756 1.000 53.381  ? 351 TYR AAA O   1 
ATOM   5041  C CB  . TYR D 1 33  ? -2.647  44.668  115.496 1.000 53.646  ? 351 TYR AAA CB  1 
ATOM   5042  C CG  . TYR D 1 33  ? -3.397  45.642  116.374 1.000 51.210  ? 351 TYR AAA CG  1 
ATOM   5043  C CD1 . TYR D 1 33  ? -2.733  46.673  117.014 1.000 51.318  ? 351 TYR AAA CD1 1 
ATOM   5044  C CD2 . TYR D 1 33  ? -4.771  45.545  116.566 1.000 52.645  ? 351 TYR AAA CD2 1 
ATOM   5045  C CE1 . TYR D 1 33  ? -3.404  47.581  117.816 1.000 52.639  ? 351 TYR AAA CE1 1 
ATOM   5046  C CE2 . TYR D 1 33  ? -5.463  46.446  117.361 1.000 50.147  ? 351 TYR AAA CE2 1 
ATOM   5047  C CZ  . TYR D 1 33  ? -4.775  47.471  117.988 1.000 49.649  ? 351 TYR AAA CZ  1 
ATOM   5048  O OH  . TYR D 1 33  ? -5.418  48.380  118.774 1.000 44.020  ? 351 TYR AAA OH  1 
ATOM   5049  N N   . ALA D 1 34  ? -3.647  47.198  113.823 1.000 42.281  ? 352 ALA AAA N   1 
ATOM   5050  C CA  . ALA D 1 34  ? -4.704  48.170  113.465 1.000 40.891  ? 352 ALA AAA CA  1 
ATOM   5051  C C   . ALA D 1 34  ? -4.176  49.094  112.371 1.000 41.461  ? 352 ALA AAA C   1 
ATOM   5052  O O   . ALA D 1 34  ? -4.275  50.358  112.483 1.000 36.096  ? 352 ALA AAA O   1 
ATOM   5053  C CB  . ALA D 1 34  ? -5.101  48.966  114.674 1.000 40.193  ? 352 ALA AAA CB  1 
ATOM   5054  N N   . TRP D 1 35  ? -3.604  48.477  111.343 1.000 42.020  ? 353 TRP AAA N   1 
ATOM   5055  C CA  . TRP D 1 35  ? -2.877  49.207  110.287 1.000 40.831  ? 353 TRP AAA CA  1 
ATOM   5056  C C   . TRP D 1 35  ? -3.835  50.085  109.497 1.000 40.491  ? 353 TRP AAA C   1 
ATOM   5057  O O   . TRP D 1 35  ? -4.948  49.661  109.215 1.000 45.603  ? 353 TRP AAA O   1 
ATOM   5058  C CB  . TRP D 1 35  ? -2.090  48.256  109.393 1.000 41.406  ? 353 TRP AAA CB  1 
ATOM   5059  C CG  . TRP D 1 35  ? -2.828  47.082  108.842 1.000 39.369  ? 353 TRP AAA CG  1 
ATOM   5060  C CD1 . TRP D 1 35  ? -2.918  45.829  109.377 1.000 39.433  ? 353 TRP AAA CD1 1 
ATOM   5061  C CD2 . TRP D 1 35  ? -3.489  47.035  107.574 1.000 41.579  ? 353 TRP AAA CD2 1 
ATOM   5062  N NE1 . TRP D 1 35  ? -3.636  45.011  108.547 1.000 43.537  ? 353 TRP AAA NE1 1 
ATOM   5063  C CE2 . TRP D 1 35  ? -3.988  45.720  107.426 1.000 45.647  ? 353 TRP AAA CE2 1 
ATOM   5064  C CE3 . TRP D 1 35  ? -3.719  47.976  106.564 1.000 42.830  ? 353 TRP AAA CE3 1 
ATOM   5065  C CZ2 . TRP D 1 35  ? -4.704  45.331  106.291 1.000 48.624  ? 353 TRP AAA CZ2 1 
ATOM   5066  C CZ3 . TRP D 1 35  ? -4.428  47.594  105.448 1.000 45.488  ? 353 TRP AAA CZ3 1 
ATOM   5067  C CH2 . TRP D 1 35  ? -4.913  46.288  105.317 1.000 48.387  ? 353 TRP AAA CH2 1 
ATOM   5068  N N   . ASN D 1 36  ? -3.358  51.274  109.169 1.000 45.726  ? 354 ASN AAA N   1 
ATOM   5069  C CA  . ASN D 1 36  ? -4.058  52.336  108.415 1.000 50.156  ? 354 ASN AAA CA  1 
ATOM   5070  C C   . ASN D 1 36  ? -3.872  52.083  106.918 1.000 51.701  ? 354 ASN AAA C   1 
ATOM   5071  O O   . ASN D 1 36  ? -2.727  51.808  106.511 1.000 59.767  ? 354 ASN AAA O   1 
ATOM   5072  C CB  . ASN D 1 36  ? -3.468  53.692  108.770 1.000 51.464  ? 354 ASN AAA CB  1 
ATOM   5073  C CG  . ASN D 1 36  ? -4.491  54.785  108.729 1.000 57.442  ? 354 ASN AAA CG  1 
ATOM   5074  O OD1 . ASN D 1 36  ? -5.200  54.940  107.742 1.000 64.570  ? 354 ASN AAA OD1 1 
ATOM   5075  N ND2 . ASN D 1 36  ? -4.566  55.529  109.813 1.000 65.789  ? 354 ASN AAA ND2 1 
ATOM   5076  N N   . ARG D 1 37  ? -4.952  52.172  106.138 1.000 50.767  ? 355 ARG AAA N   1 
ATOM   5077  C CA  . ARG D 1 37  ? -4.906  52.113  104.653 1.000 50.273  ? 355 ARG AAA CA  1 
ATOM   5078  C C   . ARG D 1 37  ? -5.545  53.390  104.112 1.000 51.761  ? 355 ARG AAA C   1 
ATOM   5079  O O   . ARG D 1 37  ? -6.745  53.573  104.339 1.000 49.580  ? 355 ARG AAA O   1 
ATOM   5080  C CB  . ARG D 1 37  ? -5.629  50.882  104.097 1.000 46.767  ? 355 ARG AAA CB  1 
ATOM   5081  C CG  . ARG D 1 37  ? -6.035  51.013  102.633 1.000 44.315  ? 355 ARG AAA CG  1 
ATOM   5082  C CD  . ARG D 1 37  ? -6.397  49.696  101.984 1.000 41.871  ? 355 ARG AAA CD  1 
ATOM   5083  N NE  . ARG D 1 37  ? -5.282  48.762  101.918 1.000 40.310  ? 355 ARG AAA NE  1 
ATOM   5084  C CZ  . ARG D 1 37  ? -5.252  47.657  101.174 1.000 45.058  ? 355 ARG AAA CZ  1 
ATOM   5085  N NH1 . ARG D 1 37  ? -6.283  47.323  100.417 1.000 45.048  ? 355 ARG AAA NH1 1 
ATOM   5086  N NH2 . ARG D 1 37  ? -4.197  46.852  101.217 1.000 49.544  ? 355 ARG AAA NH2 1 
ATOM   5087  N N   . LYS D 1 38  ? -4.745  54.238  103.463 1.000 58.839  ? 356 LYS AAA N   1 
ATOM   5088  C CA  . LYS D 1 38  ? -5.205  55.440  102.726 1.000 63.351  ? 356 LYS AAA CA  1 
ATOM   5089  C C   . LYS D 1 38  ? -5.411  55.014  101.278 1.000 67.519  ? 356 LYS AAA C   1 
ATOM   5090  O O   . LYS D 1 38  ? -4.474  54.434  100.707 1.000 71.303  ? 356 LYS AAA O   1 
ATOM   5091  C CB  . LYS D 1 38  ? -4.170  56.563  102.813 1.000 62.570  ? 356 LYS AAA CB  1 
ATOM   5092  C CG  . LYS D 1 38  ? -4.611  57.911  102.263 1.000 61.873  ? 356 LYS AAA CG  1 
ATOM   5093  C CD  . LYS D 1 38  ? -5.443  58.738  103.215 1.000 66.331  ? 356 LYS AAA CD  1 
ATOM   5094  C CE  . LYS D 1 38  ? -5.200  60.227  103.049 1.000 70.967  ? 356 LYS AAA CE  1 
ATOM   5095  N NZ  . LYS D 1 38  ? -5.521  60.686  101.675 1.000 72.817  ? 356 LYS AAA NZ  1 
ATOM   5096  N N   . ARG D 1 39  ? -6.607  55.234  100.739 1.000 73.555  ? 357 ARG AAA N   1 
ATOM   5097  C CA  . ARG D 1 39  ? -6.892  55.018  99.299  1.000 80.931  ? 357 ARG AAA CA  1 
ATOM   5098  C C   . ARG D 1 39  ? -6.348  56.240  98.563  1.000 83.457  ? 357 ARG AAA C   1 
ATOM   5099  O O   . ARG D 1 39  ? -6.517  57.371  99.095  1.000 68.318  ? 357 ARG AAA O   1 
ATOM   5100  C CB  . ARG D 1 39  ? -8.387  54.809  99.047  1.000 85.623  ? 357 ARG AAA CB  1 
ATOM   5101  C CG  . ARG D 1 39  ? -8.935  55.517  97.814  1.000 90.948  ? 357 ARG AAA CG  1 
ATOM   5102  C CD  . ARG D 1 39  ? -10.416 55.282  97.649  1.000 91.303  ? 357 ARG AAA CD  1 
ATOM   5103  N NE  . ARG D 1 39  ? -10.612 53.937  97.115  1.000 98.587  ? 357 ARG AAA NE  1 
ATOM   5104  C CZ  . ARG D 1 39  ? -11.147 53.649  95.941  1.000 93.537  ? 357 ARG AAA CZ  1 
ATOM   5105  N NH1 . ARG D 1 39  ? -11.532 54.623  95.126  1.000 88.754  ? 357 ARG AAA NH1 1 
ATOM   5106  N NH2 . ARG D 1 39  ? -11.265 52.374  95.588  1.000 85.327  ? 357 ARG AAA NH2 1 
ATOM   5107  N N   . ILE D 1 40  ? -5.690  55.995  97.425  1.000 92.711  ? 358 ILE AAA N   1 
ATOM   5108  C CA  . ILE D 1 40  ? -5.262  57.031  96.441  1.000 92.201  ? 358 ILE AAA CA  1 
ATOM   5109  C C   . ILE D 1 40  ? -6.104  56.841  95.175  1.000 96.485  ? 358 ILE AAA C   1 
ATOM   5110  O O   . ILE D 1 40  ? -6.114  55.682  94.620  1.000 95.186  ? 358 ILE AAA O   1 
ATOM   5111  C CB  . ILE D 1 40  ? -3.753  56.938  96.148  1.000 97.401  ? 358 ILE AAA CB  1 
ATOM   5112  C CG1 . ILE D 1 40  ? -2.897  56.912  97.420  1.000 99.863  ? 358 ILE AAA CG1 1 
ATOM   5113  C CG2 . ILE D 1 40  ? -3.335  58.079  95.236  1.000 107.018 ? 358 ILE AAA CG2 1 
ATOM   5114  C CD1 . ILE D 1 40  ? -2.901  58.215  98.214  1.000 97.841  ? 358 ILE AAA CD1 1 
ATOM   5115  N N   . SER D 1 41  ? -6.808  57.913  94.773  1.000 92.405  ? 359 SER AAA N   1 
ATOM   5116  C CA  . SER D 1 41  ? -7.636  58.020  93.541  1.000 97.728  ? 359 SER AAA CA  1 
ATOM   5117  C C   . SER D 1 41  ? -7.686  59.488  93.103  1.000 94.532  ? 359 SER AAA C   1 
ATOM   5118  O O   . SER D 1 41  ? -7.498  60.364  93.971  1.000 86.021  ? 359 SER AAA O   1 
ATOM   5119  C CB  . SER D 1 41  ? -9.033  57.445  93.738  1.000 101.134 ? 359 SER AAA CB  1 
ATOM   5120  O OG  . SER D 1 41  ? -9.000  56.019  93.821  1.000 109.938 ? 359 SER AAA OG  1 
ATOM   5121  N N   . ASN D 1 42  ? -7.884  59.727  91.799  1.000 99.849  ? 360 ASN AAA N   1 
ATOM   5122  C CA  . ASN D 1 42  ? -8.259  61.041  91.206  1.000 98.960  ? 360 ASN AAA CA  1 
ATOM   5123  C C   . ASN D 1 42  ? -7.202  62.088  91.560  1.000 101.934 ? 360 ASN AAA C   1 
ATOM   5124  O O   . ASN D 1 42  ? -7.571  63.171  92.059  1.000 98.353  ? 360 ASN AAA O   1 
ATOM   5125  C CB  . ASN D 1 42  ? -9.642  61.496  91.673  1.000 105.524 ? 360 ASN AAA CB  1 
ATOM   5126  C CG  . ASN D 1 42  ? -10.716 60.483  91.353  1.000 111.446 ? 360 ASN AAA CG  1 
ATOM   5127  O OD1 . ASN D 1 42  ? -11.139 59.725  92.227  1.000 117.933 ? 360 ASN AAA OD1 1 
ATOM   5128  N ND2 . ASN D 1 42  ? -11.132 60.443  90.098  1.000 112.162 ? 360 ASN AAA ND2 1 
ATOM   5129  N N   . CYS D 1 43  ? -5.934  61.768  91.303  1.000 115.436 ? 361 CYS AAA N   1 
ATOM   5130  C CA  . CYS D 1 43  ? -4.784  62.691  91.493  1.000 121.732 ? 361 CYS AAA CA  1 
ATOM   5131  C C   . CYS D 1 43  ? -3.584  62.209  90.667  1.000 121.885 ? 361 CYS AAA C   1 
ATOM   5132  O O   . CYS D 1 43  ? -3.564  61.014  90.278  1.000 112.813 ? 361 CYS AAA O   1 
ATOM   5133  C CB  . CYS D 1 43  ? -4.418  62.814  92.968  1.000 127.058 ? 361 CYS AAA CB  1 
ATOM   5134  S SG  . CYS D 1 43  ? -4.037  61.230  93.760  1.000 132.279 ? 361 CYS AAA SG  1 
ATOM   5135  N N   . VAL D 1 44  ? -2.630  63.118  90.426  1.000 115.390 ? 362 VAL AAA N   1 
ATOM   5136  C CA  . VAL D 1 44  ? -1.366  62.874  89.670  1.000 106.275 ? 362 VAL AAA CA  1 
ATOM   5137  C C   . VAL D 1 44  ? -0.223  62.688  90.678  1.000 102.504 ? 362 VAL AAA C   1 
ATOM   5138  O O   . VAL D 1 44  ? -0.000  63.601  91.528  1.000 98.619  ? 362 VAL AAA O   1 
ATOM   5139  C CB  . VAL D 1 44  ? -1.077  64.018  88.682  1.000 112.611 ? 362 VAL AAA CB  1 
ATOM   5140  C CG1 . VAL D 1 44  ? 0.042   63.650  87.724  1.000 115.499 ? 362 VAL AAA CG1 1 
ATOM   5141  C CG2 . VAL D 1 44  ? -2.324  64.442  87.915  1.000 117.094 ? 362 VAL AAA CG2 1 
ATOM   5142  N N   . ALA D 1 45  ? 0.472   61.550  90.573  1.000 100.039 ? 363 ALA AAA N   1 
ATOM   5143  C CA  . ALA D 1 45  ? 1.404   61.013  91.593  1.000 104.216 ? 363 ALA AAA CA  1 
ATOM   5144  C C   . ALA D 1 45  ? 2.845   61.137  91.097  1.000 96.763  ? 363 ALA AAA C   1 
ATOM   5145  O O   . ALA D 1 45  ? 3.190   60.519  90.072  1.000 96.729  ? 363 ALA AAA O   1 
ATOM   5146  C CB  . ALA D 1 45  ? 1.064   59.573  91.904  1.000 110.341 ? 363 ALA AAA CB  1 
ATOM   5147  N N   . ASP D 1 46  ? 3.660   61.897  91.823  1.000 89.704  ? 364 ASP AAA N   1 
ATOM   5148  C CA  . ASP D 1 46  ? 5.087   62.119  91.490  1.000 83.830  ? 364 ASP AAA CA  1 
ATOM   5149  C C   . ASP D 1 46  ? 5.947   61.155  92.305  1.000 70.442  ? 364 ASP AAA C   1 
ATOM   5150  O O   . ASP D 1 46  ? 6.418   61.557  93.372  1.000 63.432  ? 364 ASP AAA O   1 
ATOM   5151  C CB  . ASP D 1 46  ? 5.463   63.574  91.758  1.000 93.022  ? 364 ASP AAA CB  1 
ATOM   5152  C CG  . ASP D 1 46  ? 6.875   63.883  91.317  1.000 98.446  ? 364 ASP AAA CG  1 
ATOM   5153  O OD1 . ASP D 1 46  ? 7.643   64.388  92.158  1.000 111.289 ? 364 ASP AAA OD1 1 
ATOM   5154  O OD2 . ASP D 1 46  ? 7.192   63.590  90.143  1.000 96.420  ? 364 ASP AAA OD2 1 
ATOM   5155  N N   . TYR D 1 47  ? 6.164   59.938  91.816  1.000 67.509  ? 365 TYR AAA N   1 
ATOM   5156  C CA  . TYR D 1 47  ? 6.806   58.850  92.600  1.000 75.796  ? 365 TYR AAA CA  1 
ATOM   5157  C C   . TYR D 1 47  ? 8.305   59.131  92.776  1.000 79.157  ? 365 TYR AAA C   1 
ATOM   5158  O O   . TYR D 1 47  ? 8.952   58.501  93.630  1.000 77.241  ? 365 TYR AAA O   1 
ATOM   5159  C CB  . TYR D 1 47  ? 6.558   57.492  91.942  1.000 84.021  ? 365 TYR AAA CB  1 
ATOM   5160  C CG  . TYR D 1 47  ? 5.114   57.058  91.899  1.000 94.573  ? 365 TYR AAA CG  1 
ATOM   5161  C CD1 . TYR D 1 47  ? 4.587   56.191  92.849  1.000 91.328  ? 365 TYR AAA CD1 1 
ATOM   5162  C CD2 . TYR D 1 47  ? 4.263   57.503  90.896  1.000 103.324 ? 365 TYR AAA CD2 1 
ATOM   5163  C CE1 . TYR D 1 47  ? 3.256   55.799  92.812  1.000 86.465  ? 365 TYR AAA CE1 1 
ATOM   5164  C CE2 . TYR D 1 47  ? 2.937   57.102  90.833  1.000 97.314  ? 365 TYR AAA CE2 1 
ATOM   5165  C CZ  . TYR D 1 47  ? 2.433   56.247  91.793  1.000 87.022  ? 365 TYR AAA CZ  1 
ATOM   5166  O OH  . TYR D 1 47  ? 1.135   55.862  91.692  1.000 77.936  ? 365 TYR AAA OH  1 
ATOM   5167  N N   . SER D 1 48  ? 8.849   60.067  91.998  1.000 84.616  ? 366 SER AAA N   1 
ATOM   5168  C CA  . SER D 1 48  ? 10.255  60.541  92.098  1.000 78.672  ? 366 SER AAA CA  1 
ATOM   5169  C C   . SER D 1 48  ? 10.562  61.087  93.501  1.000 78.481  ? 366 SER AAA C   1 
ATOM   5170  O O   . SER D 1 48  ? 11.654  60.773  93.998  1.000 79.297  ? 366 SER AAA O   1 
ATOM   5171  C CB  . SER D 1 48  ? 10.537  61.564  91.043  1.000 79.922  ? 366 SER AAA CB  1 
ATOM   5172  O OG  . SER D 1 48  ? 9.740   62.717  91.240  1.000 77.350  ? 366 SER AAA OG  1 
ATOM   5173  N N   . VAL D 1 49  ? 9.653   61.878  94.102  1.000 74.140  ? 367 VAL AAA N   1 
ATOM   5174  C CA  . VAL D 1 49  ? 9.801   62.455  95.477  1.000 68.440  ? 367 VAL AAA CA  1 
ATOM   5175  C C   . VAL D 1 49  ? 10.237  61.322  96.403  1.000 64.369  ? 367 VAL AAA C   1 
ATOM   5176  O O   . VAL D 1 49  ? 11.068  61.570  97.289  1.000 64.402  ? 367 VAL AAA O   1 
ATOM   5177  C CB  . VAL D 1 49  ? 8.516   63.121  96.014  1.000 72.221  ? 367 VAL AAA CB  1 
ATOM   5178  C CG1 . VAL D 1 49  ? 8.640   63.483  97.496  1.000 77.401  ? 367 VAL AAA CG1 1 
ATOM   5179  C CG2 . VAL D 1 49  ? 8.098   64.350  95.211  1.000 69.245  ? 367 VAL AAA CG2 1 
ATOM   5180  N N   . LEU D 1 50  ? 9.701   60.125  96.180  1.000 65.822  ? 368 LEU AAA N   1 
ATOM   5181  C CA  . LEU D 1 50  ? 9.901   58.951  97.067  1.000 78.038  ? 368 LEU AAA CA  1 
ATOM   5182  C C   . LEU D 1 50  ? 11.312  58.376  96.930  1.000 83.277  ? 368 LEU AAA C   1 
ATOM   5183  O O   . LEU D 1 50  ? 11.997  58.332  97.961  1.000 90.040  ? 368 LEU AAA O   1 
ATOM   5184  C CB  . LEU D 1 50  ? 8.838   57.898  96.759  1.000 80.027  ? 368 LEU AAA CB  1 
ATOM   5185  C CG  . LEU D 1 50  ? 7.661   57.865  97.725  1.000 80.827  ? 368 LEU AAA CG  1 
ATOM   5186  C CD1 . LEU D 1 50  ? 7.281   59.265  98.200  1.000 76.549  ? 368 LEU AAA CD1 1 
ATOM   5187  C CD2 . LEU D 1 50  ? 6.479   57.181  97.061  1.000 88.848  ? 368 LEU AAA CD2 1 
ATOM   5188  N N   . TYR D 1 51  ? 11.725  57.924  95.741  1.000 88.055  ? 369 TYR AAA N   1 
ATOM   5189  C CA  . TYR D 1 51  ? 12.976  57.122  95.586  1.000 96.716  ? 369 TYR AAA CA  1 
ATOM   5190  C C   . TYR D 1 51  ? 14.218  58.031  95.498  1.000 95.776  ? 369 TYR AAA C   1 
ATOM   5191  O O   . TYR D 1 51  ? 15.335  57.537  95.748  1.000 82.066  ? 369 TYR AAA O   1 
ATOM   5192  C CB  . TYR D 1 51  ? 12.881  56.122  94.429  1.000 97.374  ? 369 TYR AAA CB  1 
ATOM   5193  C CG  . TYR D 1 51  ? 12.494  56.692  93.089  1.000 97.620  ? 369 TYR AAA CG  1 
ATOM   5194  C CD1 . TYR D 1 51  ? 11.185  56.614  92.644  1.000 99.938  ? 369 TYR AAA CD1 1 
ATOM   5195  C CD2 . TYR D 1 51  ? 13.433  57.276  92.253  1.000 97.123  ? 369 TYR AAA CD2 1 
ATOM   5196  C CE1 . TYR D 1 51  ? 10.811  57.123  91.413  1.000 96.329  ? 369 TYR AAA CE1 1 
ATOM   5197  C CE2 . TYR D 1 51  ? 13.076  57.782  91.015  1.000 90.654  ? 369 TYR AAA CE2 1 
ATOM   5198  C CZ  . TYR D 1 51  ? 11.761  57.699  90.594  1.000 88.371  ? 369 TYR AAA CZ  1 
ATOM   5199  O OH  . TYR D 1 51  ? 11.368  58.196  89.392  1.000 85.726  ? 369 TYR AAA OH  1 
ATOM   5200  N N   . ASN D 1 52  ? 14.050  59.323  95.215  1.000 89.969  ? 370 ASN AAA N   1 
ATOM   5201  C CA  . ASN D 1 52  ? 15.172  60.298  95.213  1.000 85.503  ? 370 ASN AAA CA  1 
ATOM   5202  C C   . ASN D 1 52  ? 15.445  60.760  96.644  1.000 83.017  ? 370 ASN AAA C   1 
ATOM   5203  O O   . ASN D 1 52  ? 16.477  61.406  96.860  1.000 89.821  ? 370 ASN AAA O   1 
ATOM   5204  C CB  . ASN D 1 52  ? 14.891  61.479  94.282  1.000 86.117  ? 370 ASN AAA CB  1 
ATOM   5205  C CG  . ASN D 1 52  ? 14.790  61.064  92.830  1.000 87.377  ? 370 ASN AAA CG  1 
ATOM   5206  O OD1 . ASN D 1 52  ? 15.334  60.037  92.420  1.000 86.449  ? 370 ASN AAA OD1 1 
ATOM   5207  N ND2 . ASN D 1 52  ? 14.092  61.866  92.048  1.000 87.760  ? 370 ASN AAA ND2 1 
ATOM   5208  N N   . SER D 1 53  ? 14.550  60.462  97.585  1.000 86.311  ? 371 SER AAA N   1 
ATOM   5209  C CA  . SER D 1 53  ? 14.783  60.702  99.030  1.000 88.921  ? 371 SER AAA CA  1 
ATOM   5210  C C   . SER D 1 53  ? 15.913  59.783  99.491  1.000 85.151  ? 371 SER AAA C   1 
ATOM   5211  O O   . SER D 1 53  ? 15.958  58.616  99.061  1.000 74.601  ? 371 SER AAA O   1 
ATOM   5212  C CB  . SER D 1 53  ? 13.547  60.503  99.855  1.000 94.532  ? 371 SER AAA CB  1 
ATOM   5213  O OG  . SER D 1 53  ? 13.861  60.571  101.240 1.000 94.252  ? 371 SER AAA OG  1 
ATOM   5214  N N   . ALA D 1 54  ? 16.801  60.313  100.328 1.000 85.937  ? 372 ALA AAA N   1 
ATOM   5215  C CA  . ALA D 1 54  ? 17.958  59.587  100.887 1.000 92.634  ? 372 ALA AAA CA  1 
ATOM   5216  C C   . ALA D 1 54  ? 17.671  59.226  102.348 1.000 90.186  ? 372 ALA AAA C   1 
ATOM   5217  O O   . ALA D 1 54  ? 18.634  58.853  103.053 1.000 99.333  ? 372 ALA AAA O   1 
ATOM   5218  C CB  . ALA D 1 54  ? 19.195  60.441  100.742 1.000 99.002  ? 372 ALA AAA CB  1 
ATOM   5219  N N   . SER D 1 55  ? 16.402  59.304  102.771 1.000 83.905  ? 373 SER AAA N   1 
ATOM   5220  C CA  . SER D 1 55  ? 16.001  59.218  104.200 1.000 77.318  ? 373 SER AAA CA  1 
ATOM   5221  C C   . SER D 1 55  ? 15.324  57.874  104.516 1.000 65.505  ? 373 SER AAA C   1 
ATOM   5222  O O   . SER D 1 55  ? 14.685  57.780  105.570 1.000 64.433  ? 373 SER AAA O   1 
ATOM   5223  C CB  . SER D 1 55  ? 15.148  60.408  104.593 1.000 72.738  ? 373 SER AAA CB  1 
ATOM   5224  O OG  . SER D 1 55  ? 13.965  60.459  103.818 1.000 65.228  ? 373 SER AAA OG  1 
ATOM   5225  N N   . PHE D 1 56  ? 15.508  56.848  103.684 1.000 56.697  ? 374 PHE AAA N   1 
ATOM   5226  C CA  . PHE D 1 56  ? 14.755  55.575  103.787 1.000 55.299  ? 374 PHE AAA CA  1 
ATOM   5227  C C   . PHE D 1 56  ? 15.709  54.406  104.027 1.000 49.305  ? 374 PHE AAA C   1 
ATOM   5228  O O   . PHE D 1 56  ? 16.570  54.203  103.207 1.000 56.779  ? 374 PHE AAA O   1 
ATOM   5229  C CB  . PHE D 1 56  ? 13.908  55.390  102.527 1.000 61.338  ? 374 PHE AAA CB  1 
ATOM   5230  C CG  . PHE D 1 56  ? 12.737  56.337  102.394 1.000 68.428  ? 374 PHE AAA CG  1 
ATOM   5231  C CD1 . PHE D 1 56  ? 11.984  56.711  103.502 1.000 73.139  ? 374 PHE AAA CD1 1 
ATOM   5232  C CD2 . PHE D 1 56  ? 12.358  56.834  101.156 1.000 73.125  ? 374 PHE AAA CD2 1 
ATOM   5233  C CE1 . PHE D 1 56  ? 10.902  57.572  103.381 1.000 75.022  ? 374 PHE AAA CE1 1 
ATOM   5234  C CE2 . PHE D 1 56  ? 11.257  57.672  101.029 1.000 74.275  ? 374 PHE AAA CE2 1 
ATOM   5235  C CZ  . PHE D 1 56  ? 10.538  58.051  102.142 1.000 72.600  ? 374 PHE AAA CZ  1 
ATOM   5236  N N   . SER D 1 57  ? 15.537  53.677  105.128 1.000 50.667  ? 375 SER AAA N   1 
ATOM   5237  C CA  . SER D 1 57  ? 16.274  52.434  105.493 1.000 55.589  ? 375 SER AAA CA  1 
ATOM   5238  C C   . SER D 1 57  ? 16.044  51.336  104.460 1.000 56.382  ? 375 SER AAA C   1 
ATOM   5239  O O   . SER D 1 57  ? 16.990  50.626  104.150 1.000 59.423  ? 375 SER AAA O   1 
ATOM   5240  C CB  . SER D 1 57  ? 15.872  51.910  106.846 1.000 59.128  ? 375 SER AAA CB  1 
ATOM   5241  O OG  . SER D 1 57  ? 16.487  52.669  107.874 1.000 72.753  ? 375 SER AAA OG  1 
ATOM   5242  N N   . THR D 1 58  ? 14.808  51.176  104.003 1.000 59.530  ? 376 THR AAA N   1 
ATOM   5243  C CA  . THR D 1 58  ? 14.362  50.070  103.123 1.000 53.441  ? 376 THR AAA CA  1 
ATOM   5244  C C   . THR D 1 58  ? 13.508  50.677  102.009 1.000 49.729  ? 376 THR AAA C   1 
ATOM   5245  O O   . THR D 1 58  ? 12.809  51.672  102.283 1.000 46.491  ? 376 THR AAA O   1 
ATOM   5246  C CB  . THR D 1 58  ? 13.653  49.024  103.987 1.000 55.057  ? 376 THR AAA CB  1 
ATOM   5247  O OG1 . THR D 1 58  ? 14.685  48.207  104.531 1.000 55.036  ? 376 THR AAA OG1 1 
ATOM   5248  C CG2 . THR D 1 58  ? 12.685  48.138  103.247 1.000 57.073  ? 376 THR AAA CG2 1 
ATOM   5249  N N   . PHE D 1 59  ? 13.577  50.116  100.800 1.000 45.717  ? 377 PHE AAA N   1 
ATOM   5250  C CA  . PHE D 1 59  ? 12.708  50.523  99.665  1.000 43.223  ? 377 PHE AAA CA  1 
ATOM   5251  C C   . PHE D 1 59  ? 12.695  49.381  98.654  1.000 45.670  ? 377 PHE AAA C   1 
ATOM   5252  O O   . PHE D 1 59  ? 13.113  49.540  97.497  1.000 47.100  ? 377 PHE AAA O   1 
ATOM   5253  C CB  . PHE D 1 59  ? 13.156  51.863  99.105  1.000 39.206  ? 377 PHE AAA CB  1 
ATOM   5254  C CG  . PHE D 1 59  ? 12.102  52.654  98.381  1.000 41.211  ? 377 PHE AAA CG  1 
ATOM   5255  C CD1 . PHE D 1 59  ? 11.286  52.078  97.413  1.000 39.834  ? 377 PHE AAA CD1 1 
ATOM   5256  C CD2 . PHE D 1 59  ? 11.990  54.023  98.610  1.000 44.086  ? 377 PHE AAA CD2 1 
ATOM   5257  C CE1 . PHE D 1 59  ? 10.367  52.858  96.717  1.000 40.964  ? 377 PHE AAA CE1 1 
ATOM   5258  C CE2 . PHE D 1 59  ? 11.077  54.799  97.904  1.000 42.076  ? 377 PHE AAA CE2 1 
ATOM   5259  C CZ  . PHE D 1 59  ? 10.265  54.213  96.959  1.000 41.647  ? 377 PHE AAA CZ  1 
ATOM   5260  N N   . LYS D 1 60  ? 12.189  48.240  99.111  1.000 50.299  ? 378 LYS AAA N   1 
ATOM   5261  C CA  . LYS D 1 60  ? 12.068  46.996  98.311  1.000 50.710  ? 378 LYS AAA CA  1 
ATOM   5262  C C   . LYS D 1 60  ? 10.728  47.072  97.580  1.000 51.950  ? 378 LYS AAA C   1 
ATOM   5263  O O   . LYS D 1 60  ? 9.681   47.014  98.251  1.000 54.514  ? 378 LYS AAA O   1 
ATOM   5264  C CB  . LYS D 1 60  ? 12.163  45.751  99.204  1.000 49.045  ? 378 LYS AAA CB  1 
ATOM   5265  C CG  . LYS D 1 60  ? 12.968  45.905  100.496 1.000 48.158  ? 378 LYS AAA CG  1 
ATOM   5266  C CD  . LYS D 1 60  ? 13.948  44.809  100.796 1.000 46.183  ? 378 LYS AAA CD  1 
ATOM   5267  C CE  . LYS D 1 60  ? 13.318  43.441  100.870 1.000 48.469  ? 378 LYS AAA CE  1 
ATOM   5268  N NZ  . LYS D 1 60  ? 14.349  42.380  100.854 1.000 49.176  ? 378 LYS AAA NZ  1 
ATOM   5269  N N   . CYS D 1 61  ? 10.752  47.231  96.260  1.000 53.876  ? 379 CYS AAA N   1 
ATOM   5270  C CA  . CYS D 1 61  ? 9.524   47.127  95.434  1.000 54.690  ? 379 CYS AAA CA  1 
ATOM   5271  C C   . CYS D 1 61  ? 9.435   45.726  94.844  1.000 56.133  ? 379 CYS AAA C   1 
ATOM   5272  O O   . CYS D 1 61  ? 10.485  45.137  94.595  1.000 57.746  ? 379 CYS AAA O   1 
ATOM   5273  C CB  . CYS D 1 61  ? 9.496   48.197  94.368  1.000 54.751  ? 379 CYS AAA CB  1 
ATOM   5274  S SG  . CYS D 1 61  ? 9.449   49.819  95.158  1.000 62.827  ? 379 CYS AAA SG  1 
ATOM   5275  N N   . TYR D 1 62  ? 8.213   45.220  94.693  1.000 54.233  ? 380 TYR AAA N   1 
ATOM   5276  C CA  . TYR D 1 62  ? 7.906   43.859  94.194  1.000 51.263  ? 380 TYR AAA CA  1 
ATOM   5277  C C   . TYR D 1 62  ? 6.976   44.000  92.978  1.000 57.919  ? 380 TYR AAA C   1 
ATOM   5278  O O   . TYR D 1 62  ? 6.003   44.764  93.053  1.000 54.155  ? 380 TYR AAA O   1 
ATOM   5279  C CB  . TYR D 1 62  ? 7.320   43.042  95.341  1.000 46.012  ? 380 TYR AAA CB  1 
ATOM   5280  C CG  . TYR D 1 62  ? 8.212   42.856  96.550  1.000 42.033  ? 380 TYR AAA CG  1 
ATOM   5281  C CD1 . TYR D 1 62  ? 8.473   43.893  97.439  1.000 40.043  ? 380 TYR AAA CD1 1 
ATOM   5282  C CD2 . TYR D 1 62  ? 8.747   41.606  96.846  1.000 39.070  ? 380 TYR AAA CD2 1 
ATOM   5283  C CE1 . TYR D 1 62  ? 9.269   43.701  98.564  1.000 40.658  ? 380 TYR AAA CE1 1 
ATOM   5284  C CE2 . TYR D 1 62  ? 9.557   41.397  97.953  1.000 38.735  ? 380 TYR AAA CE2 1 
ATOM   5285  C CZ  . TYR D 1 62  ? 9.802   42.439  98.835  1.000 41.518  ? 380 TYR AAA CZ  1 
ATOM   5286  O OH  . TYR D 1 62  ? 10.602  42.184  99.922  1.000 38.814  ? 380 TYR AAA OH  1 
ATOM   5287  N N   . GLY D 1 63  ? 7.303   43.369  91.849  1.000 59.972  ? 381 GLY AAA N   1 
ATOM   5288  C CA  . GLY D 1 63  ? 6.409   43.271  90.673  1.000 60.057  ? 381 GLY AAA CA  1 
ATOM   5289  C C   . GLY D 1 63  ? 6.185   44.586  89.933  1.000 58.282  ? 381 GLY AAA C   1 
ATOM   5290  O O   . GLY D 1 63  ? 5.347   44.623  89.027  1.000 60.408  ? 381 GLY AAA O   1 
ATOM   5291  N N   . VAL D 1 64  ? 6.887   45.651  90.291  1.000 57.022  ? 382 VAL AAA N   1 
ATOM   5292  C CA  . VAL D 1 64  ? 6.695   46.962  89.621  1.000 64.470  ? 382 VAL AAA CA  1 
ATOM   5293  C C   . VAL D 1 64  ? 7.894   47.859  89.938  1.000 69.273  ? 382 VAL AAA C   1 
ATOM   5294  O O   . VAL D 1 64  ? 8.459   47.722  91.048  1.000 83.388  ? 382 VAL AAA O   1 
ATOM   5295  C CB  . VAL D 1 64  ? 5.365   47.594  90.057  1.000 62.917  ? 382 VAL AAA CB  1 
ATOM   5296  C CG1 . VAL D 1 64  ? 5.449   48.142  91.470  1.000 61.939  ? 382 VAL AAA CG1 1 
ATOM   5297  C CG2 . VAL D 1 64  ? 4.918   48.651  89.064  1.000 62.476  ? 382 VAL AAA CG2 1 
ATOM   5298  N N   . SER D 1 65  ? 8.264   48.729  88.994  1.000 67.072  ? 383 SER AAA N   1 
ATOM   5299  C CA  . SER D 1 65  ? 9.470   49.589  89.052  1.000 63.035  ? 383 SER AAA CA  1 
ATOM   5300  C C   . SER D 1 65  ? 9.049   51.014  89.379  1.000 57.259  ? 383 SER AAA C   1 
ATOM   5301  O O   . SER D 1 65  ? 8.392   51.655  88.566  1.000 54.133  ? 383 SER AAA O   1 
ATOM   5302  C CB  . SER D 1 65  ? 10.206  49.540  87.752  1.000 68.752  ? 383 SER AAA CB  1 
ATOM   5303  O OG  . SER D 1 65  ? 10.494  48.201  87.369  1.000 75.319  ? 383 SER AAA OG  1 
ATOM   5304  N N   . PRO D 1 66  ? 9.413   51.566  90.559  1.000 55.156  ? 384 PRO AAA N   1 
ATOM   5305  C CA  . PRO D 1 66  ? 8.974   52.916  90.924  1.000 56.342  ? 384 PRO AAA CA  1 
ATOM   5306  C C   . PRO D 1 66  ? 9.469   53.971  89.922  1.000 60.914  ? 384 PRO AAA C   1 
ATOM   5307  O O   . PRO D 1 66  ? 8.834   54.997  89.770  1.000 56.916  ? 384 PRO AAA O   1 
ATOM   5308  C CB  . PRO D 1 66  ? 9.563   53.139  92.325  1.000 54.548  ? 384 PRO AAA CB  1 
ATOM   5309  C CG  . PRO D 1 66  ? 10.665  52.102  92.451  1.000 53.861  ? 384 PRO AAA CG  1 
ATOM   5310  C CD  . PRO D 1 66  ? 10.250  50.932  91.590  1.000 52.351  ? 384 PRO AAA CD  1 
ATOM   5311  N N   . THR D 1 67  ? 10.577  53.646  89.247  1.000 74.135  ? 385 THR AAA N   1 
ATOM   5312  C CA  . THR D 1 67  ? 11.318  54.492  88.278  1.000 73.265  ? 385 THR AAA CA  1 
ATOM   5313  C C   . THR D 1 67  ? 10.508  54.587  86.979  1.000 74.713  ? 385 THR AAA C   1 
ATOM   5314  O O   . THR D 1 67  ? 10.736  55.541  86.241  1.000 81.271  ? 385 THR AAA O   1 
ATOM   5315  C CB  . THR D 1 67  ? 12.741  53.938  88.072  1.000 71.986  ? 385 THR AAA CB  1 
ATOM   5316  O OG1 . THR D 1 67  ? 12.702  52.636  87.486  1.000 66.425  ? 385 THR AAA OG1 1 
ATOM   5317  C CG2 . THR D 1 67  ? 13.543  53.820  89.354  1.000 70.657  ? 385 THR AAA CG2 1 
ATOM   5318  N N   . LYS D 1 68  ? 9.574   53.666  86.727  1.000 81.752  ? 386 LYS AAA N   1 
ATOM   5319  C CA  . LYS D 1 68  ? 8.893   53.533  85.414  1.000 85.521  ? 386 LYS AAA CA  1 
ATOM   5320  C C   . LYS D 1 68  ? 7.378   53.720  85.533  1.000 84.959  ? 386 LYS AAA C   1 
ATOM   5321  O O   . LYS D 1 68  ? 6.707   53.328  84.580  1.000 86.364  ? 386 LYS AAA O   1 
ATOM   5322  C CB  . LYS D 1 68  ? 9.120   52.140  84.823  1.000 90.043  ? 386 LYS AAA CB  1 
ATOM   5323  C CG  . LYS D 1 68  ? 10.547  51.789  84.422  1.000 101.978 ? 386 LYS AAA CG  1 
ATOM   5324  C CD  . LYS D 1 68  ? 10.706  50.293  84.147  1.000 113.147 ? 386 LYS AAA CD  1 
ATOM   5325  C CE  . LYS D 1 68  ? 11.692  49.961  83.049  1.000 115.204 ? 386 LYS AAA CE  1 
ATOM   5326  N NZ  . LYS D 1 68  ? 11.257  50.511  81.747  1.000 117.726 ? 386 LYS AAA NZ  1 
ATOM   5327  N N   . LEU D 1 69  ? 6.835   54.282  86.615  1.000 85.820  ? 387 LEU AAA N   1 
ATOM   5328  C CA  . LEU D 1 69  ? 5.353   54.337  86.757  1.000 98.362  ? 387 LEU AAA CA  1 
ATOM   5329  C C   . LEU D 1 69  ? 4.861   55.765  87.002  1.000 106.168 ? 387 LEU AAA C   1 
ATOM   5330  O O   . LEU D 1 69  ? 3.638   55.924  87.224  1.000 119.234 ? 387 LEU AAA O   1 
ATOM   5331  C CB  . LEU D 1 69  ? 4.875   53.362  87.841  1.000 104.709 ? 387 LEU AAA CB  1 
ATOM   5332  C CG  . LEU D 1 69  ? 5.608   53.373  89.183  1.000 105.896 ? 387 LEU AAA CG  1 
ATOM   5333  C CD1 . LEU D 1 69  ? 5.302   54.611  89.998  1.000 103.991 ? 387 LEU AAA CD1 1 
ATOM   5334  C CD2 . LEU D 1 69  ? 5.241   52.146  89.994  1.000 105.876 ? 387 LEU AAA CD2 1 
ATOM   5335  N N   . ASN D 1 70  ? 5.750   56.757  86.897  1.000 123.370 ? 388 ASN AAA N   1 
ATOM   5336  C CA  . ASN D 1 70  ? 5.382   58.200  86.824  1.000 137.092 ? 388 ASN AAA CA  1 
ATOM   5337  C C   . ASN D 1 70  ? 5.073   58.537  85.353  1.000 133.319 ? 388 ASN AAA C   1 
ATOM   5338  O O   . ASN D 1 70  ? 5.019   59.743  85.010  1.000 126.892 ? 388 ASN AAA O   1 
ATOM   5339  C CB  . ASN D 1 70  ? 6.403   59.119  87.520  1.000 139.389 ? 388 ASN AAA CB  1 
ATOM   5340  C CG  . ASN D 1 70  ? 7.845   58.885  87.113  1.000 145.083 ? 388 ASN AAA CG  1 
ATOM   5341  O OD1 . ASN D 1 70  ? 8.260   59.293  86.030  1.000 156.791 ? 388 ASN AAA OD1 1 
ATOM   5342  N ND2 . ASN D 1 70  ? 8.623   58.263  87.990  1.000 132.329 ? 388 ASN AAA ND2 1 
ATOM   5343  N N   . ASP D 1 71  ? 4.851   57.501  84.530  1.000 130.114 ? 389 ASP AAA N   1 
ATOM   5344  C CA  . ASP D 1 71  ? 4.177   57.576  83.206  1.000 126.715 ? 389 ASP AAA CA  1 
ATOM   5345  C C   . ASP D 1 71  ? 3.240   56.368  83.011  1.000 117.832 ? 389 ASP AAA C   1 
ATOM   5346  O O   . ASP D 1 71  ? 3.005   55.968  81.847  1.000 108.596 ? 389 ASP AAA O   1 
ATOM   5347  C CB  . ASP D 1 71  ? 5.202   57.614  82.076  1.000 138.330 ? 389 ASP AAA CB  1 
ATOM   5348  C CG  . ASP D 1 71  ? 5.756   56.237  81.781  1.000 143.790 ? 389 ASP AAA CG  1 
ATOM   5349  O OD1 . ASP D 1 71  ? 5.655   55.811  80.624  1.000 160.653 ? 389 ASP AAA OD1 1 
ATOM   5350  O OD2 . ASP D 1 71  ? 6.240   55.592  82.724  1.000 136.893 ? 389 ASP AAA OD2 1 
ATOM   5351  N N   . LEU D 1 72  ? 2.711   55.785  84.091  1.000 112.796 ? 390 LEU AAA N   1 
ATOM   5352  C CA  . LEU D 1 72  ? 1.629   54.766  83.991  1.000 96.866  ? 390 LEU AAA CA  1 
ATOM   5353  C C   . LEU D 1 72  ? 0.443   55.131  84.895  1.000 96.805  ? 390 LEU AAA C   1 
ATOM   5354  O O   . LEU D 1 72  ? 0.615   55.938  85.848  1.000 83.163  ? 390 LEU AAA O   1 
ATOM   5355  C CB  . LEU D 1 72  ? 2.180   53.372  84.310  1.000 87.537  ? 390 LEU AAA CB  1 
ATOM   5356  C CG  . LEU D 1 72  ? 1.510   52.243  83.531  1.000 84.608  ? 390 LEU AAA CG  1 
ATOM   5357  C CD1 . LEU D 1 72  ? 1.753   52.400  82.030  1.000 85.363  ? 390 LEU AAA CD1 1 
ATOM   5358  C CD2 . LEU D 1 72  ? 1.995   50.893  84.030  1.000 80.037  ? 390 LEU AAA CD2 1 
ATOM   5359  N N   . CYS D 1 73  ? -0.721  54.541  84.570  1.000 104.842 ? 391 CYS AAA N   1 
ATOM   5360  C CA  . CYS D 1 73  ? -2.039  54.717  85.239  1.000 101.229 ? 391 CYS AAA CA  1 
ATOM   5361  C C   . CYS D 1 73  ? -2.538  53.382  85.815  1.000 100.358 ? 391 CYS AAA C   1 
ATOM   5362  O O   . CYS D 1 73  ? -2.302  52.323  85.194  1.000 90.749  ? 391 CYS AAA O   1 
ATOM   5363  C CB  . CYS D 1 73  ? -3.078  55.267  84.275  1.000 95.081  ? 391 CYS AAA CB  1 
ATOM   5364  S SG  . CYS D 1 73  ? -2.716  56.957  83.740  1.000 110.790 ? 391 CYS AAA SG  1 
ATOM   5365  N N   . PHE D 1 74  ? -3.234  53.467  86.952  1.000 103.695 ? 392 PHE AAA N   1 
ATOM   5366  C CA  . PHE D 1 74  ? -3.774  52.332  87.747  1.000 102.201 ? 392 PHE AAA CA  1 
ATOM   5367  C C   . PHE D 1 74  ? -5.186  52.693  88.232  1.000 107.627 ? 392 PHE AAA C   1 
ATOM   5368  O O   . PHE D 1 74  ? -5.447  53.914  88.446  1.000 101.302 ? 392 PHE AAA O   1 
ATOM   5369  C CB  . PHE D 1 74  ? -2.861  52.034  88.942  1.000 102.270 ? 392 PHE AAA CB  1 
ATOM   5370  C CG  . PHE D 1 74  ? -1.416  51.734  88.617  1.000 92.650  ? 392 PHE AAA CG  1 
ATOM   5371  C CD1 . PHE D 1 74  ? -0.459  52.734  88.652  1.000 87.242  ? 392 PHE AAA CD1 1 
ATOM   5372  C CD2 . PHE D 1 74  ? -1.002  50.440  88.332  1.000 93.024  ? 392 PHE AAA CD2 1 
ATOM   5373  C CE1 . PHE D 1 74  ? 0.869   52.455  88.378  1.000 90.553  ? 392 PHE AAA CE1 1 
ATOM   5374  C CE2 . PHE D 1 74  ? 0.327   50.159  88.058  1.000 87.416  ? 392 PHE AAA CE2 1 
ATOM   5375  C CZ  . PHE D 1 74  ? 1.257   51.171  88.063  1.000 93.855  ? 392 PHE AAA CZ  1 
ATOM   5376  N N   . THR D 1 75  ? -6.056  51.682  88.415  1.000 105.614 ? 393 THR AAA N   1 
ATOM   5377  C CA  . THR D 1 75  ? -7.452  51.834  88.929  1.000 95.613  ? 393 THR AAA CA  1 
ATOM   5378  C C   . THR D 1 75  ? -7.400  52.332  90.370  1.000 80.099  ? 393 THR AAA C   1 
ATOM   5379  O O   . THR D 1 75  ? -8.112  53.306  90.695  1.000 69.277  ? 393 THR AAA O   1 
ATOM   5380  C CB  . THR D 1 75  ? -8.262  50.530  88.883  1.000 99.060  ? 393 THR AAA CB  1 
ATOM   5381  O OG1 . THR D 1 75  ? -7.431  49.473  89.354  1.000 99.103  ? 393 THR AAA OG1 1 
ATOM   5382  C CG2 . THR D 1 75  ? -8.768  50.190  87.500  1.000 101.499 ? 393 THR AAA CG2 1 
ATOM   5383  N N   . ASN D 1 76  ? -6.580  51.686  91.197  1.000 77.603  ? 394 ASN AAA N   1 
ATOM   5384  C CA  . ASN D 1 76  ? -6.438  52.060  92.623  1.000 84.070  ? 394 ASN AAA CA  1 
ATOM   5385  C C   . ASN D 1 76  ? -5.028  51.789  93.129  1.000 83.241  ? 394 ASN AAA C   1 
ATOM   5386  O O   . ASN D 1 76  ? -4.415  50.752  92.764  1.000 64.296  ? 394 ASN AAA O   1 
ATOM   5387  C CB  . ASN D 1 76  ? -7.457  51.333  93.490  1.000 92.562  ? 394 ASN AAA CB  1 
ATOM   5388  C CG  . ASN D 1 76  ? -8.775  52.061  93.516  1.000 96.831  ? 394 ASN AAA CG  1 
ATOM   5389  O OD1 . ASN D 1 76  ? -8.866  53.147  94.093  1.000 116.417 ? 394 ASN AAA OD1 1 
ATOM   5390  N ND2 . ASN D 1 76  ? -9.765  51.461  92.879  1.000 81.720  ? 394 ASN AAA ND2 1 
ATOM   5391  N N   . VAL D 1 77  ? -4.569  52.727  93.951  1.000 92.590  ? 395 VAL AAA N   1 
ATOM   5392  C CA  . VAL D 1 77  ? -3.285  52.663  94.695  1.000 92.627  ? 395 VAL AAA CA  1 
ATOM   5393  C C   . VAL D 1 77  ? -3.627  52.801  96.177  1.000 84.985  ? 395 VAL AAA C   1 
ATOM   5394  O O   . VAL D 1 77  ? -4.398  53.727  96.526  1.000 76.678  ? 395 VAL AAA O   1 
ATOM   5395  C CB  . VAL D 1 77  ? -2.329  53.769  94.223  1.000 99.605  ? 395 VAL AAA CB  1 
ATOM   5396  C CG1 . VAL D 1 77  ? -1.033  53.772  95.020  1.000 101.203 ? 395 VAL AAA CG1 1 
ATOM   5397  C CG2 . VAL D 1 77  ? -2.066  53.654  92.727  1.000 105.023 ? 395 VAL AAA CG2 1 
ATOM   5398  N N   . TYR D 1 78  ? -3.094  51.899  97.001  1.000 79.813  ? 396 TYR AAA N   1 
ATOM   5399  C CA  . TYR D 1 78  ? -3.323  51.868  98.465  1.000 76.136  ? 396 TYR AAA CA  1 
ATOM   5400  C C   . TYR D 1 78  ? -1.983  52.111  99.174  1.000 63.976  ? 396 TYR AAA C   1 
ATOM   5401  O O   . TYR D 1 78  ? -0.988  51.489  98.791  1.000 52.940  ? 396 TYR AAA O   1 
ATOM   5402  C CB  . TYR D 1 78  ? -3.992  50.548  98.871  1.000 78.056  ? 396 TYR AAA CB  1 
ATOM   5403  C CG  . TYR D 1 78  ? -5.314  50.243  98.204  1.000 76.869  ? 396 TYR AAA CG  1 
ATOM   5404  C CD1 . TYR D 1 78  ? -6.429  51.066  98.373  1.000 74.848  ? 396 TYR AAA CD1 1 
ATOM   5405  C CD2 . TYR D 1 78  ? -5.459  49.108  97.419  1.000 74.125  ? 396 TYR AAA CD2 1 
ATOM   5406  C CE1 . TYR D 1 78  ? -7.642  50.775  97.763  1.000 73.941  ? 396 TYR AAA CE1 1 
ATOM   5407  C CE2 . TYR D 1 78  ? -6.665  48.799  96.815  1.000 74.394  ? 396 TYR AAA CE2 1 
ATOM   5408  C CZ  . TYR D 1 78  ? -7.760  49.632  96.984  1.000 78.837  ? 396 TYR AAA CZ  1 
ATOM   5409  O OH  . TYR D 1 78  ? -8.929  49.291  96.367  1.000 84.921  ? 396 TYR AAA OH  1 
ATOM   5410  N N   . ALA D 1 79  ? -1.987  52.989  100.183 1.000 56.777  ? 397 ALA AAA N   1 
ATOM   5411  C CA  . ALA D 1 79  ? -0.836  53.332  101.045 1.000 53.908  ? 397 ALA AAA CA  1 
ATOM   5412  C C   . ALA D 1 79  ? -1.112  52.906  102.499 1.000 50.477  ? 397 ALA AAA C   1 
ATOM   5413  O O   . ALA D 1 79  ? -1.722  53.692  103.269 1.000 42.644  ? 397 ALA AAA O   1 
ATOM   5414  C CB  . ALA D 1 79  ? -0.575  54.811  100.925 1.000 56.252  ? 397 ALA AAA CB  1 
ATOM   5415  N N   . ASP D 1 80  ? -0.643  51.711  102.864 1.000 50.344  ? 398 ASP AAA N   1 
ATOM   5416  C CA  . ASP D 1 80  ? -0.796  51.120  104.220 1.000 51.615  ? 398 ASP AAA CA  1 
ATOM   5417  C C   . ASP D 1 80  ? 0.362   51.613  105.086 1.000 48.343  ? 398 ASP AAA C   1 
ATOM   5418  O O   . ASP D 1 80  ? 1.500   51.445  104.672 1.000 55.879  ? 398 ASP AAA O   1 
ATOM   5419  C CB  . ASP D 1 80  ? -0.858  49.591  104.158 1.000 54.255  ? 398 ASP AAA CB  1 
ATOM   5420  C CG  . ASP D 1 80  ? -1.890  49.087  103.159 1.000 58.230  ? 398 ASP AAA CG  1 
ATOM   5421  O OD1 . ASP D 1 80  ? -2.795  49.885  102.829 1.000 62.613  ? 398 ASP AAA OD1 1 
ATOM   5422  O OD2 . ASP D 1 80  ? -1.774  47.921  102.702 1.000 55.601  ? 398 ASP AAA OD2 1 
ATOM   5423  N N   . SER D 1 81  ? 0.072   52.237  106.222 1.000 47.707  ? 399 SER AAA N   1 
ATOM   5424  C CA  . SER D 1 81  ? 1.078   52.842  107.130 1.000 47.366  ? 399 SER AAA CA  1 
ATOM   5425  C C   . SER D 1 81  ? 0.940   52.203  108.504 1.000 43.934  ? 399 SER AAA C   1 
ATOM   5426  O O   . SER D 1 81  ? -0.163  51.959  108.910 1.000 41.485  ? 399 SER AAA O   1 
ATOM   5427  C CB  . SER D 1 81  ? 0.965   54.355  107.207 1.000 47.599  ? 399 SER AAA CB  1 
ATOM   5428  O OG  . SER D 1 81  ? -0.382  54.784  107.247 1.000 48.489  ? 399 SER AAA OG  1 
ATOM   5429  N N   . PHE D 1 82  ? 2.047   51.946  109.182 1.000 46.401  ? 400 PHE AAA N   1 
ATOM   5430  C CA  . PHE D 1 82  ? 2.056   51.421  110.562 1.000 44.339  ? 400 PHE AAA CA  1 
ATOM   5431  C C   . PHE D 1 82  ? 3.462   51.527  111.145 1.000 42.486  ? 400 PHE AAA C   1 
ATOM   5432  O O   . PHE D 1 82  ? 4.302   52.077  110.459 1.000 49.766  ? 400 PHE AAA O   1 
ATOM   5433  C CB  . PHE D 1 82  ? 1.547   49.988  110.553 1.000 43.974  ? 400 PHE AAA CB  1 
ATOM   5434  C CG  . PHE D 1 82  ? 2.235   49.073  109.582 1.000 45.601  ? 400 PHE AAA CG  1 
ATOM   5435  C CD1 . PHE D 1 82  ? 3.418   48.440  109.929 1.000 48.786  ? 400 PHE AAA CD1 1 
ATOM   5436  C CD2 . PHE D 1 82  ? 1.687   48.819  108.342 1.000 45.468  ? 400 PHE AAA CD2 1 
ATOM   5437  C CE1 . PHE D 1 82  ? 4.038   47.547  109.061 1.000 48.074  ? 400 PHE AAA CE1 1 
ATOM   5438  C CE2 . PHE D 1 82  ? 2.299   47.913  107.482 1.000 48.968  ? 400 PHE AAA CE2 1 
ATOM   5439  C CZ  . PHE D 1 82  ? 3.477   47.283  107.838 1.000 47.507  ? 400 PHE AAA CZ  1 
ATOM   5440  N N   . VAL D 1 83  ? 3.691   51.032  112.363 1.000 42.332  ? 401 VAL AAA N   1 
ATOM   5441  C CA  . VAL D 1 83  ? 5.020   51.068  113.045 1.000 40.019  ? 401 VAL AAA CA  1 
ATOM   5442  C C   . VAL D 1 83  ? 5.335   49.699  113.647 1.000 42.827  ? 401 VAL AAA C   1 
ATOM   5443  O O   . VAL D 1 83  ? 4.447   49.128  114.339 1.000 49.906  ? 401 VAL AAA O   1 
ATOM   5444  C CB  . VAL D 1 83  ? 5.081   52.154  114.130 1.000 38.475  ? 401 VAL AAA CB  1 
ATOM   5445  C CG1 . VAL D 1 83  ? 6.319   51.999  114.998 1.000 39.577  ? 401 VAL AAA CG1 1 
ATOM   5446  C CG2 . VAL D 1 83  ? 5.021   53.550  113.534 1.000 38.714  ? 401 VAL AAA CG2 1 
ATOM   5447  N N   . ILE D 1 84  ? 6.572   49.246  113.433 1.000 42.624  ? 402 ILE AAA N   1 
ATOM   5448  C CA  . ILE D 1 84  ? 7.156   47.988  113.985 1.000 44.662  ? 402 ILE AAA CA  1 
ATOM   5449  C C   . ILE D 1 84  ? 8.611   48.271  114.371 1.000 48.341  ? 402 ILE AAA C   1 
ATOM   5450  O O   . ILE D 1 84  ? 9.059   49.425  114.183 1.000 46.616  ? 402 ILE AAA O   1 
ATOM   5451  C CB  . ILE D 1 84  ? 7.044   46.851  112.954 1.000 44.480  ? 402 ILE AAA CB  1 
ATOM   5452  C CG1 . ILE D 1 84  ? 7.483   47.322  111.567 1.000 44.589  ? 402 ILE AAA CG1 1 
ATOM   5453  C CG2 . ILE D 1 84  ? 5.635   46.292  112.927 1.000 48.536  ? 402 ILE AAA CG2 1 
ATOM   5454  C CD1 . ILE D 1 84  ? 7.789   46.204  110.602 1.000 44.576  ? 402 ILE AAA CD1 1 
ATOM   5455  N N   . ARG D 1 85  ? 9.328   47.272  114.885 1.000 47.760  ? 403 ARG AAA N   1 
ATOM   5456  C CA  . ARG D 1 85  ? 10.765  47.414  115.228 1.000 49.141  ? 403 ARG AAA CA  1 
ATOM   5457  C C   . ARG D 1 85  ? 11.597  46.867  114.062 1.000 51.784  ? 403 ARG AAA C   1 
ATOM   5458  O O   . ARG D 1 85  ? 11.050  46.086  113.238 1.000 55.959  ? 403 ARG AAA O   1 
ATOM   5459  C CB  . ARG D 1 85  ? 11.068  46.739  116.569 1.000 49.989  ? 403 ARG AAA CB  1 
ATOM   5460  C CG  . ARG D 1 85  ? 10.899  45.226  116.581 1.000 51.475  ? 403 ARG AAA CG  1 
ATOM   5461  C CD  . ARG D 1 85  ? 11.068  44.657  117.977 1.000 54.414  ? 403 ARG AAA CD  1 
ATOM   5462  N NE  . ARG D 1 85  ? 10.890  43.209  117.968 1.000 59.616  ? 403 ARG AAA NE  1 
ATOM   5463  C CZ  . ARG D 1 85  ? 11.862  42.287  117.992 1.000 64.909  ? 403 ARG AAA CZ  1 
ATOM   5464  N NH1 . ARG D 1 85  ? 13.150  42.615  118.053 1.000 67.567  ? 403 ARG AAA NH1 1 
ATOM   5465  N NH2 . ARG D 1 85  ? 11.527  41.009  117.975 1.000 68.151  ? 403 ARG AAA NH2 1 
ATOM   5466  N N   . GLY D 1 86  ? 12.859  47.289  113.986 1.000 48.575  ? 404 GLY AAA N   1 
ATOM   5467  C CA  . GLY D 1 86  ? 13.760  47.029  112.850 1.000 48.675  ? 404 GLY AAA CA  1 
ATOM   5468  C C   . GLY D 1 86  ? 13.886  45.550  112.534 1.000 48.292  ? 404 GLY AAA C   1 
ATOM   5469  O O   . GLY D 1 86  ? 13.870  45.213  111.333 1.000 52.193  ? 404 GLY AAA O   1 
ATOM   5470  N N   . ASP D 1 87  ? 13.985  44.692  113.553 1.000 48.104  ? 405 ASP AAA N   1 
ATOM   5471  C CA  . ASP D 1 87  ? 14.113  43.219  113.377 1.000 57.909  ? 405 ASP AAA CA  1 
ATOM   5472  C C   . ASP D 1 87  ? 12.969  42.671  112.512 1.000 60.542  ? 405 ASP AAA C   1 
ATOM   5473  O O   . ASP D 1 87  ? 13.113  41.554  111.980 1.000 65.107  ? 405 ASP AAA O   1 
ATOM   5474  C CB  . ASP D 1 87  ? 14.089  42.474  114.715 1.000 65.572  ? 405 ASP AAA CB  1 
ATOM   5475  C CG  . ASP D 1 87  ? 15.420  42.463  115.444 1.000 70.412  ? 405 ASP AAA CG  1 
ATOM   5476  O OD1 . ASP D 1 87  ? 16.087  41.415  115.445 1.000 73.556  ? 405 ASP AAA OD1 1 
ATOM   5477  O OD2 . ASP D 1 87  ? 15.774  43.505  116.011 1.000 88.441  ? 405 ASP AAA OD2 1 
ATOM   5478  N N   . GLU D 1 88  ? 11.859  43.410  112.419 1.000 63.324  ? 406 GLU AAA N   1 
ATOM   5479  C CA  . GLU D 1 88  ? 10.565  42.935  111.866 1.000 54.770  ? 406 GLU AAA CA  1 
ATOM   5480  C C   . GLU D 1 88  ? 10.331  43.520  110.463 1.000 52.710  ? 406 GLU AAA C   1 
ATOM   5481  O O   . GLU D 1 88  ? 9.404   43.042  109.788 1.000 63.186  ? 406 GLU AAA O   1 
ATOM   5482  C CB  . GLU D 1 88  ? 9.443   43.286  112.854 1.000 54.513  ? 406 GLU AAA CB  1 
ATOM   5483  C CG  . GLU D 1 88  ? 9.412   42.409  114.109 1.000 49.595  ? 406 GLU AAA CG  1 
ATOM   5484  C CD  . GLU D 1 88  ? 8.410   42.826  115.177 1.000 47.037  ? 406 GLU AAA CD  1 
ATOM   5485  O OE1 . GLU D 1 88  ? 7.868   43.948  115.084 1.000 47.772  ? 406 GLU AAA OE1 1 
ATOM   5486  O OE2 . GLU D 1 88  ? 8.175   42.024  116.104 1.000 46.293  ? 406 GLU AAA OE2 1 
ATOM   5487  N N   . VAL D 1 89  ? 11.127  44.479  109.988 1.000 45.631  ? 407 VAL AAA N   1 
ATOM   5488  C CA  . VAL D 1 89  ? 10.868  45.076  108.643 1.000 44.359  ? 407 VAL AAA CA  1 
ATOM   5489  C C   . VAL D 1 89  ? 11.097  44.011  107.568 1.000 46.453  ? 407 VAL AAA C   1 
ATOM   5490  O O   . VAL D 1 89  ? 10.406  44.064  106.552 1.000 45.122  ? 407 VAL AAA O   1 
ATOM   5491  C CB  . VAL D 1 89  ? 11.712  46.323  108.353 1.000 40.833  ? 407 VAL AAA CB  1 
ATOM   5492  C CG1 . VAL D 1 89  ? 11.358  46.913  106.995 1.000 37.606  ? 407 VAL AAA CG1 1 
ATOM   5493  C CG2 . VAL D 1 89  ? 11.569  47.368  109.456 1.000 42.747  ? 407 VAL AAA CG2 1 
ATOM   5494  N N   . ARG D 1 90  ? 12.027  43.086  107.789 1.000 56.011  ? 408 ARG AAA N   1 
ATOM   5495  C CA  . ARG D 1 90  ? 12.258  41.913  106.900 1.000 70.407  ? 408 ARG AAA CA  1 
ATOM   5496  C C   . ARG D 1 90  ? 10.946  41.136  106.689 1.000 70.083  ? 408 ARG AAA C   1 
ATOM   5497  O O   . ARG D 1 90  ? 10.805  40.489  105.632 1.000 66.981  ? 408 ARG AAA O   1 
ATOM   5498  C CB  . ARG D 1 90  ? 13.330  40.976  107.479 1.000 82.540  ? 408 ARG AAA CB  1 
ATOM   5499  C CG  . ARG D 1 90  ? 13.009  40.407  108.858 1.000 94.674  ? 408 ARG AAA CG  1 
ATOM   5500  C CD  . ARG D 1 90  ? 13.602  39.035  109.150 1.000 103.708 ? 408 ARG AAA CD  1 
ATOM   5501  N NE  . ARG D 1 90  ? 14.923  38.855  108.551 1.000 121.524 ? 408 ARG AAA NE  1 
ATOM   5502  C CZ  . ARG D 1 90  ? 16.058  39.422  108.972 1.000 124.550 ? 408 ARG AAA CZ  1 
ATOM   5503  N NH1 . ARG D 1 90  ? 17.191  39.178  108.330 1.000 125.310 ? 408 ARG AAA NH1 1 
ATOM   5504  N NH2 . ARG D 1 90  ? 16.068  40.227  110.022 1.000 120.395 ? 408 ARG AAA NH2 1 
ATOM   5505  N N   . GLN D 1 91  ? 10.045  41.167  107.680 1.000 68.058  ? 409 GLN AAA N   1 
ATOM   5506  C CA  . GLN D 1 91  ? 8.781   40.380  107.713 1.000 57.957  ? 409 GLN AAA CA  1 
ATOM   5507  C C   . GLN D 1 91  ? 7.727   41.035  106.815 1.000 54.270  ? 409 GLN AAA C   1 
ATOM   5508  O O   . GLN D 1 91  ? 6.785   40.325  106.458 1.000 57.847  ? 409 GLN AAA O   1 
ATOM   5509  C CB  . GLN D 1 91  ? 8.258   40.237  109.143 1.000 54.568  ? 409 GLN AAA CB  1 
ATOM   5510  C CG  . GLN D 1 91  ? 8.573   38.891  109.773 1.000 54.720  ? 409 GLN AAA CG  1 
ATOM   5511  C CD  . GLN D 1 91  ? 8.066   38.816  111.193 1.000 57.955  ? 409 GLN AAA CD  1 
ATOM   5512  O OE1 . GLN D 1 91  ? 6.902   38.479  111.450 1.000 60.393  ? 409 GLN AAA OE1 1 
ATOM   5513  N NE2 . GLN D 1 91  ? 8.950   39.144  112.127 1.000 57.876  ? 409 GLN AAA NE2 1 
ATOM   5514  N N   . ILE D 1 92  ? 7.853   42.325  106.483 1.000 44.235  ? 410 ILE AAA N   1 
ATOM   5515  C CA  . ILE D 1 92  ? 6.856   43.035  105.632 1.000 41.336  ? 410 ILE AAA CA  1 
ATOM   5516  C C   . ILE D 1 92  ? 7.194   42.758  104.178 1.000 40.851  ? 410 ILE AAA C   1 
ATOM   5517  O O   . ILE D 1 92  ? 7.629   43.698  103.500 1.000 38.504  ? 410 ILE AAA O   1 
ATOM   5518  C CB  . ILE D 1 92  ? 6.851   44.543  105.916 1.000 45.244  ? 410 ILE AAA CB  1 
ATOM   5519  C CG1 . ILE D 1 92  ? 6.703   44.808  107.415 1.000 52.620  ? 410 ILE AAA CG1 1 
ATOM   5520  C CG2 . ILE D 1 92  ? 5.782   45.270  105.103 1.000 42.566  ? 410 ILE AAA CG2 1 
ATOM   5521  C CD1 . ILE D 1 92  ? 5.550   44.080  108.061 1.000 52.537  ? 410 ILE AAA CD1 1 
ATOM   5522  N N   . ALA D 1 93  ? 6.999   41.520  103.725 1.000 47.550  ? 411 ALA AAA N   1 
ATOM   5523  C CA  . ALA D 1 93  ? 7.408   41.053  102.383 1.000 54.058  ? 411 ALA AAA CA  1 
ATOM   5524  C C   . ALA D 1 93  ? 6.692   39.765  102.014 1.000 54.547  ? 411 ALA AAA C   1 
ATOM   5525  O O   . ALA D 1 93  ? 6.504   38.896  102.853 1.000 56.768  ? 411 ALA AAA O   1 
ATOM   5526  C CB  . ALA D 1 93  ? 8.896   40.816  102.346 1.000 63.103  ? 411 ALA AAA CB  1 
ATOM   5527  N N   . PRO D 1 94  ? 6.325   39.578  100.728 1.000 54.581  ? 412 PRO AAA N   1 
ATOM   5528  C CA  . PRO D 1 94  ? 5.706   38.338  100.283 1.000 51.784  ? 412 PRO AAA CA  1 
ATOM   5529  C C   . PRO D 1 94  ? 6.454   37.129  100.833 1.000 49.046  ? 412 PRO AAA C   1 
ATOM   5530  O O   . PRO D 1 94  ? 7.647   37.162  100.865 1.000 50.865  ? 412 PRO AAA O   1 
ATOM   5531  C CB  . PRO D 1 94  ? 5.812   38.362  98.755  1.000 54.009  ? 412 PRO AAA CB  1 
ATOM   5532  C CG  . PRO D 1 94  ? 6.690   39.560  98.461  1.000 60.282  ? 412 PRO AAA CG  1 
ATOM   5533  C CD  . PRO D 1 94  ? 6.491   40.522  99.616  1.000 58.140  ? 412 PRO AAA CD  1 
ATOM   5534  N N   . GLY D 1 95  ? 5.700   36.136  101.295 1.000 53.055  ? 413 GLY AAA N   1 
ATOM   5535  C CA  . GLY D 1 95  ? 6.189   34.783  101.612 1.000 53.846  ? 413 GLY AAA CA  1 
ATOM   5536  C C   . GLY D 1 95  ? 6.911   34.693  102.942 1.000 52.290  ? 413 GLY AAA C   1 
ATOM   5537  O O   . GLY D 1 95  ? 7.549   33.670  103.135 1.000 60.613  ? 413 GLY AAA O   1 
ATOM   5538  N N   . GLN D 1 96  ? 6.780   35.674  103.835 1.000 54.080  ? 414 GLN AAA N   1 
ATOM   5539  C CA  . GLN D 1 96  ? 7.411   35.670  105.179 1.000 58.038  ? 414 GLN AAA CA  1 
ATOM   5540  C C   . GLN D 1 96  ? 6.544   34.936  106.204 1.000 56.929  ? 414 GLN AAA C   1 
ATOM   5541  O O   . GLN D 1 96  ? 5.384   34.587  105.865 1.000 64.068  ? 414 GLN AAA O   1 
ATOM   5542  C CB  . GLN D 1 96  ? 7.654   37.120  105.598 1.000 66.421  ? 414 GLN AAA CB  1 
ATOM   5543  C CG  . GLN D 1 96  ? 8.720   37.793  104.748 1.000 73.738  ? 414 GLN AAA CG  1 
ATOM   5544  C CD  . GLN D 1 96  ? 10.066  37.172  105.066 1.000 79.661  ? 414 GLN AAA CD  1 
ATOM   5545  O OE1 . GLN D 1 96  ? 10.424  36.953  106.231 1.000 71.164  ? 414 GLN AAA OE1 1 
ATOM   5546  N NE2 . GLN D 1 96  ? 10.806  36.832  104.018 1.000 88.243  ? 414 GLN AAA NE2 1 
ATOM   5547  N N   . THR D 1 97  ? 7.094   34.703  107.401 1.000 54.082  ? 415 THR AAA N   1 
ATOM   5548  C CA  . THR D 1 97  ? 6.356   34.169  108.580 1.000 59.306  ? 415 THR AAA CA  1 
ATOM   5549  C C   . THR D 1 97  ? 6.889   34.824  109.865 1.000 62.281  ? 415 THR AAA C   1 
ATOM   5550  O O   . THR D 1 97  ? 7.969   35.429  109.780 1.000 60.293  ? 415 THR AAA O   1 
ATOM   5551  C CB  . THR D 1 97  ? 6.391   32.635  108.645 1.000 60.316  ? 415 THR AAA CB  1 
ATOM   5552  O OG1 . THR D 1 97  ? 7.693   32.301  109.114 1.000 60.007  ? 415 THR AAA OG1 1 
ATOM   5553  C CG2 . THR D 1 97  ? 6.069   31.939  107.336 1.000 60.806  ? 415 THR AAA CG2 1 
ATOM   5554  N N   . GLY D 1 98  ? 6.131   34.730  110.978 1.000 68.398  ? 416 GLY AAA N   1 
ATOM   5555  C CA  . GLY D 1 98  ? 6.444   35.317  112.301 1.000 66.213  ? 416 GLY AAA CA  1 
ATOM   5556  C C   . GLY D 1 98  ? 5.260   36.043  112.910 1.000 61.929  ? 416 GLY AAA C   1 
ATOM   5557  O O   . GLY D 1 98  ? 4.173   35.912  112.349 1.000 67.852  ? 416 GLY AAA O   1 
ATOM   5558  N N   . LYS D 1 99  ? 5.462   36.759  114.025 1.000 62.408  ? 417 LYS AAA N   1 
ATOM   5559  C CA  . LYS D 1 99  ? 4.413   37.567  114.711 1.000 61.414  ? 417 LYS AAA CA  1 
ATOM   5560  C C   . LYS D 1 99  ? 3.780   38.514  113.700 1.000 54.869  ? 417 LYS AAA C   1 
ATOM   5561  O O   . LYS D 1 99  ? 2.561   38.505  113.599 1.000 63.298  ? 417 LYS AAA O   1 
ATOM   5562  C CB  . LYS D 1 99  ? 4.935   38.437  115.865 1.000 71.787  ? 417 LYS AAA CB  1 
ATOM   5563  C CG  . LYS D 1 99  ? 5.495   37.685  117.064 1.000 92.088  ? 417 LYS AAA CG  1 
ATOM   5564  C CD  . LYS D 1 99  ? 4.607   36.543  117.525 1.000 107.555 ? 417 LYS AAA CD  1 
ATOM   5565  C CE  . LYS D 1 99  ? 5.250   35.591  118.515 1.000 119.776 ? 417 LYS AAA CE  1 
ATOM   5566  N NZ  . LYS D 1 99  ? 4.427   34.371  118.731 1.000 112.263 ? 417 LYS AAA NZ  1 
ATOM   5567  N N   . ILE D 1 100 ? 4.573   39.307  112.986 1.000 45.437  ? 418 ILE AAA N   1 
ATOM   5568  C CA  . ILE D 1 100 ? 4.039   40.452  112.194 1.000 43.969  ? 418 ILE AAA CA  1 
ATOM   5569  C C   . ILE D 1 100 ? 3.425   39.940  110.903 1.000 45.156  ? 418 ILE AAA C   1 
ATOM   5570  O O   . ILE D 1 100 ? 2.345   40.408  110.529 1.000 44.299  ? 418 ILE AAA O   1 
ATOM   5571  C CB  . ILE D 1 100 ? 5.122   41.489  111.892 1.000 42.247  ? 418 ILE AAA CB  1 
ATOM   5572  C CG1 . ILE D 1 100 ? 5.791   41.959  113.177 1.000 44.011  ? 418 ILE AAA CG1 1 
ATOM   5573  C CG2 . ILE D 1 100 ? 4.523   42.652  111.122 1.000 42.437  ? 418 ILE AAA CG2 1 
ATOM   5574  C CD1 . ILE D 1 100 ? 4.818   42.363  114.255 1.000 46.897  ? 418 ILE AAA CD1 1 
ATOM   5575  N N   . ALA D 1 101 ? 4.123   39.041  110.230 1.000 48.937  ? 419 ALA AAA N   1 
ATOM   5576  C CA  . ALA D 1 101 ? 3.689   38.513  108.925 1.000 52.933  ? 419 ALA AAA CA  1 
ATOM   5577  C C   . ALA D 1 101 ? 2.388   37.732  109.098 1.000 49.015  ? 419 ALA AAA C   1 
ATOM   5578  O O   . ALA D 1 101 ? 1.526   37.841  108.228 1.000 50.513  ? 419 ALA AAA O   1 
ATOM   5579  C CB  . ALA D 1 101 ? 4.773   37.653  108.341 1.000 57.615  ? 419 ALA AAA CB  1 
ATOM   5580  N N   . ASP D 1 102 ? 2.250   36.982  110.186 1.000 45.149  ? 420 ASP AAA N   1 
ATOM   5581  C CA  . ASP D 1 102 ? 1.156   35.990  110.304 1.000 48.164  ? 420 ASP AAA CA  1 
ATOM   5582  C C   . ASP D 1 102 ? -0.030  36.581  111.065 1.000 45.551  ? 420 ASP AAA C   1 
ATOM   5583  O O   . ASP D 1 102 ? -1.153  36.162  110.746 1.000 54.557  ? 420 ASP AAA O   1 
ATOM   5584  C CB  . ASP D 1 102 ? 1.645   34.676  110.920 1.000 53.352  ? 420 ASP AAA CB  1 
ATOM   5585  C CG  . ASP D 1 102 ? 2.572   33.924  109.987 1.000 58.981  ? 420 ASP AAA CG  1 
ATOM   5586  O OD1 . ASP D 1 102 ? 2.723   34.389  108.848 1.000 57.976  ? 420 ASP AAA OD1 1 
ATOM   5587  O OD2 . ASP D 1 102 ? 3.123   32.881  110.404 1.000 61.018  ? 420 ASP AAA OD2 1 
ATOM   5588  N N   . TYR D 1 103 ? 0.181   37.491  112.017 1.000 39.589  ? 421 TYR AAA N   1 
ATOM   5589  C CA  . TYR D 1 103 ? -0.872  37.916  112.982 1.000 37.370  ? 421 TYR AAA CA  1 
ATOM   5590  C C   . TYR D 1 103 ? -1.210  39.419  112.841 1.000 38.775  ? 421 TYR AAA C   1 
ATOM   5591  O O   . TYR D 1 103 ? -2.130  39.909  113.543 1.000 39.148  ? 421 TYR AAA O   1 
ATOM   5592  C CB  . TYR D 1 103 ? -0.450  37.580  114.420 1.000 34.672  ? 421 TYR AAA CB  1 
ATOM   5593  C CG  . TYR D 1 103 ? -0.189  36.129  114.771 1.000 34.515  ? 421 TYR AAA CG  1 
ATOM   5594  C CD1 . TYR D 1 103 ? -0.515  35.084  113.922 1.000 35.151  ? 421 TYR AAA CD1 1 
ATOM   5595  C CD2 . TYR D 1 103 ? 0.348   35.790  116.008 1.000 34.111  ? 421 TYR AAA CD2 1 
ATOM   5596  C CE1 . TYR D 1 103 ? -0.304  33.760  114.279 1.000 35.907  ? 421 TYR AAA CE1 1 
ATOM   5597  C CE2 . TYR D 1 103 ? 0.563   34.472  116.385 1.000 32.959  ? 421 TYR AAA CE2 1 
ATOM   5598  C CZ  . TYR D 1 103 ? 0.233   33.449  115.517 1.000 34.838  ? 421 TYR AAA CZ  1 
ATOM   5599  O OH  . TYR D 1 103 ? 0.408   32.143  115.879 1.000 35.343  ? 421 TYR AAA OH  1 
ATOM   5600  N N   . ASN D 1 104 ? -0.543  40.174  111.962 1.000 39.073  ? 422 ASN AAA N   1 
ATOM   5601  C CA  . ASN D 1 104 ? -0.660  41.659  112.017 1.000 40.379  ? 422 ASN AAA CA  1 
ATOM   5602  C C   . ASN D 1 104 ? -0.866  42.263  110.618 1.000 40.302  ? 422 ASN AAA C   1 
ATOM   5603  O O   . ASN D 1 104 ? -1.874  42.987  110.432 1.000 44.784  ? 422 ASN AAA O   1 
ATOM   5604  C CB  . ASN D 1 104 ? 0.525   42.262  112.783 1.000 39.377  ? 422 ASN AAA CB  1 
ATOM   5605  C CG  . ASN D 1 104 ? 0.546   41.896  114.260 1.000 38.170  ? 422 ASN AAA CG  1 
ATOM   5606  O OD1 . ASN D 1 104 ? 0.099   42.668  115.110 1.000 41.886  ? 422 ASN AAA OD1 1 
ATOM   5607  N ND2 . ASN D 1 104 ? 1.082   40.733  114.585 1.000 31.914  ? 422 ASN AAA ND2 1 
ATOM   5608  N N   . TYR D 1 105 ? 0.063   42.008  109.697 1.000 41.591  ? 423 TYR AAA N   1 
ATOM   5609  C CA  . TYR D 1 105 ? 0.068   42.503  108.298 1.000 42.571  ? 423 TYR AAA CA  1 
ATOM   5610  C C   . TYR D 1 105 ? 0.716   41.450  107.404 1.000 48.582  ? 423 TYR AAA C   1 
ATOM   5611  O O   . TYR D 1 105 ? 1.925   41.251  107.560 1.000 56.618  ? 423 TYR AAA O   1 
ATOM   5612  C CB  . TYR D 1 105 ? 0.865   43.798  108.196 1.000 40.841  ? 423 TYR AAA CB  1 
ATOM   5613  C CG  . TYR D 1 105 ? 0.672   44.514  106.894 1.000 45.109  ? 423 TYR AAA CG  1 
ATOM   5614  C CD1 . TYR D 1 105 ? -0.417  45.344  106.700 1.000 52.396  ? 423 TYR AAA CD1 1 
ATOM   5615  C CD2 . TYR D 1 105 ? 1.564   44.376  105.851 1.000 49.111  ? 423 TYR AAA CD2 1 
ATOM   5616  C CE1 . TYR D 1 105 ? -0.615  46.026  105.506 1.000 54.213  ? 423 TYR AAA CE1 1 
ATOM   5617  C CE2 . TYR D 1 105 ? 1.383   45.046  104.649 1.000 52.440  ? 423 TYR AAA CE2 1 
ATOM   5618  C CZ  . TYR D 1 105 ? 0.288   45.874  104.472 1.000 52.527  ? 423 TYR AAA CZ  1 
ATOM   5619  O OH  . TYR D 1 105 ? 0.070   46.523  103.295 1.000 52.534  ? 423 TYR AAA OH  1 
ATOM   5620  N N   . LYS D 1 106 ? -0.062  40.764  106.558 1.000 52.146  ? 424 LYS AAA N   1 
ATOM   5621  C CA  . LYS D 1 106 ? 0.430   39.751  105.579 1.000 49.770  ? 424 LYS AAA CA  1 
ATOM   5622  C C   . LYS D 1 106 ? 0.331   40.374  104.191 1.000 54.690  ? 424 LYS AAA C   1 
ATOM   5623  O O   . LYS D 1 106 ? -0.635  41.146  103.965 1.000 60.212  ? 424 LYS AAA O   1 
ATOM   5624  C CB  . LYS D 1 106 ? -0.400  38.465  105.623 1.000 52.361  ? 424 LYS AAA CB  1 
ATOM   5625  C CG  . LYS D 1 106 ? 0.250   37.209  105.049 1.000 53.244  ? 424 LYS AAA CG  1 
ATOM   5626  C CD  . LYS D 1 106 ? 0.293   36.088  106.096 1.000 58.318  ? 424 LYS AAA CD  1 
ATOM   5627  C CE  . LYS D 1 106 ? 0.669   34.706  105.604 1.000 63.935  ? 424 LYS AAA CE  1 
ATOM   5628  N NZ  . LYS D 1 106 ? 2.080   34.641  105.152 1.000 72.258  ? 424 LYS AAA NZ  1 
ATOM   5629  N N   . LEU D 1 107 ? 1.308   40.082  103.328 1.000 56.332  ? 425 LEU AAA N   1 
ATOM   5630  C CA  . LEU D 1 107 ? 1.302   40.457  101.892 1.000 53.865  ? 425 LEU AAA CA  1 
ATOM   5631  C C   . LEU D 1 107 ? 1.142   39.190  101.075 1.000 49.495  ? 425 LEU AAA C   1 
ATOM   5632  O O   . LEU D 1 107 ? 1.609   38.130  101.484 1.000 47.335  ? 425 LEU AAA O   1 
ATOM   5633  C CB  . LEU D 1 107 ? 2.610   41.170  101.546 1.000 57.914  ? 425 LEU AAA CB  1 
ATOM   5634  C CG  . LEU D 1 107 ? 2.752   42.577  102.123 1.000 62.233  ? 425 LEU AAA CG  1 
ATOM   5635  C CD1 . LEU D 1 107 ? 4.135   43.134  101.831 1.000 61.345  ? 425 LEU AAA CD1 1 
ATOM   5636  C CD2 . LEU D 1 107 ? 1.656   43.502  101.598 1.000 60.762  ? 425 LEU AAA CD2 1 
ATOM   5637  N N   . PRO D 1 108 ? 0.463   39.266  99.911  1.000 50.764  ? 426 PRO AAA N   1 
ATOM   5638  C CA  . PRO D 1 108 ? 0.240   38.089  99.066  1.000 53.484  ? 426 PRO AAA CA  1 
ATOM   5639  C C   . PRO D 1 108 ? 1.500   37.629  98.330  1.000 54.395  ? 426 PRO AAA C   1 
ATOM   5640  O O   . PRO D 1 108 ? 2.379   38.433  98.171  1.000 60.501  ? 426 PRO AAA O   1 
ATOM   5641  C CB  . PRO D 1 108 ? -0.798  38.551  98.034  1.000 54.862  ? 426 PRO AAA CB  1 
ATOM   5642  C CG  . PRO D 1 108 ? -0.632  40.060  97.992  1.000 53.959  ? 426 PRO AAA CG  1 
ATOM   5643  C CD  . PRO D 1 108 ? -0.165  40.483  99.372  1.000 51.897  ? 426 PRO AAA CD  1 
ATOM   5644  N N   . ASP D 1 109 ? 1.534   36.380  97.865  1.000 54.056  ? 427 ASP AAA N   1 
ATOM   5645  C CA  . ASP D 1 109 ? 2.694   35.826  97.125  1.000 59.459  ? 427 ASP AAA CA  1 
ATOM   5646  C C   . ASP D 1 109 ? 2.980   36.656  95.867  1.000 67.733  ? 427 ASP AAA C   1 
ATOM   5647  O O   . ASP D 1 109 ? 4.171   36.883  95.579  1.000 78.097  ? 427 ASP AAA O   1 
ATOM   5648  C CB  . ASP D 1 109 ? 2.484   34.355  96.786  1.000 60.751  ? 427 ASP AAA CB  1 
ATOM   5649  C CG  . ASP D 1 109 ? 2.586   33.464  98.004  1.000 68.922  ? 427 ASP AAA CG  1 
ATOM   5650  O OD1 . ASP D 1 109 ? 2.034   32.357  97.936  1.000 77.559  ? 427 ASP AAA OD1 1 
ATOM   5651  O OD2 . ASP D 1 109 ? 3.220   33.891  99.011  1.000 73.604  ? 427 ASP AAA OD2 1 
ATOM   5652  N N   . ASP D 1 110 ? 1.952   37.103  95.143  1.000 73.336  ? 428 ASP AAA N   1 
ATOM   5653  C CA  . ASP D 1 110 ? 2.124   37.817  93.841  1.000 72.156  ? 428 ASP AAA CA  1 
ATOM   5654  C C   . ASP D 1 110 ? 1.904   39.319  94.082  1.000 58.469  ? 428 ASP AAA C   1 
ATOM   5655  O O   . ASP D 1 110 ? 1.356   40.014  93.203  1.000 54.235  ? 428 ASP AAA O   1 
ATOM   5656  C CB  . ASP D 1 110 ? 1.233   37.224  92.736  1.000 84.545  ? 428 ASP AAA CB  1 
ATOM   5657  C CG  . ASP D 1 110 ? -0.268  37.295  93.008  1.000 101.761 ? 428 ASP AAA CG  1 
ATOM   5658  O OD1 . ASP D 1 110 ? -0.675  37.287  94.212  1.000 104.110 ? 428 ASP AAA OD1 1 
ATOM   5659  O OD2 . ASP D 1 110 ? -1.030  37.365  92.013  1.000 102.867 ? 428 ASP AAA OD2 1 
ATOM   5660  N N   . PHE D 1 111 ? 2.371   39.823  95.222  1.000 50.720  ? 429 PHE AAA N   1 
ATOM   5661  C CA  . PHE D 1 111 ? 2.268   41.252  95.631  1.000 51.442  ? 429 PHE AAA CA  1 
ATOM   5662  C C   . PHE D 1 111 ? 2.913   42.140  94.570  1.000 49.044  ? 429 PHE AAA C   1 
ATOM   5663  O O   . PHE D 1 111 ? 4.009   41.790  94.076  1.000 50.229  ? 429 PHE AAA O   1 
ATOM   5664  C CB  . PHE D 1 111 ? 2.953   41.474  96.983  1.000 52.189  ? 429 PHE AAA CB  1 
ATOM   5665  C CG  . PHE D 1 111 ? 3.092   42.915  97.412  1.000 51.044  ? 429 PHE AAA CG  1 
ATOM   5666  C CD1 . PHE D 1 111 ? 1.995   43.747  97.550  1.000 49.632  ? 429 PHE AAA CD1 1 
ATOM   5667  C CD2 . PHE D 1 111 ? 4.336   43.433  97.721  1.000 53.815  ? 429 PHE AAA CD2 1 
ATOM   5668  C CE1 . PHE D 1 111 ? 2.144   45.062  97.973  1.000 46.996  ? 429 PHE AAA CE1 1 
ATOM   5669  C CE2 . PHE D 1 111 ? 4.482   44.756  98.129  1.000 51.265  ? 429 PHE AAA CE2 1 
ATOM   5670  C CZ  . PHE D 1 111 ? 3.386   45.566  98.259  1.000 44.261  ? 429 PHE AAA CZ  1 
ATOM   5671  N N   . THR D 1 112 ? 2.265   43.257  94.238  1.000 47.995  ? 430 THR AAA N   1 
ATOM   5672  C CA  . THR D 1 112 ? 2.853   44.323  93.387  1.000 53.598  ? 430 THR AAA CA  1 
ATOM   5673  C C   . THR D 1 112 ? 2.828   45.668  94.122  1.000 56.342  ? 430 THR AAA C   1 
ATOM   5674  O O   . THR D 1 112 ? 1.780   46.308  94.175  1.000 49.736  ? 430 THR AAA O   1 
ATOM   5675  C CB  . THR D 1 112 ? 2.202   44.396  92.000  1.000 55.512  ? 430 THR AAA CB  1 
ATOM   5676  O OG1 . THR D 1 112 ? 1.074   45.263  92.033  1.000 56.997  ? 430 THR AAA OG1 1 
ATOM   5677  C CG2 . THR D 1 112 ? 1.802   43.036  91.480  1.000 53.659  ? 430 THR AAA CG2 1 
ATOM   5678  N N   . GLY D 1 113 ? 3.981   46.078  94.645  1.000 66.517  ? 431 GLY AAA N   1 
ATOM   5679  C CA  . GLY D 1 113 ? 4.171   47.401  95.259  1.000 70.686  ? 431 GLY AAA CA  1 
ATOM   5680  C C   . GLY D 1 113 ? 5.470   47.510  96.042  1.000 68.093  ? 431 GLY AAA C   1 
ATOM   5681  O O   . GLY D 1 113 ? 6.331   46.622  95.950  1.000 57.335  ? 431 GLY AAA O   1 
ATOM   5682  N N   . CYS D 1 114 ? 5.566   48.571  96.828  1.000 62.723  ? 432 CYS AAA N   1 
ATOM   5683  C CA  . CYS D 1 114 ? 6.803   49.101  97.427  1.000 61.074  ? 432 CYS AAA CA  1 
ATOM   5684  C C   . CYS D 1 114 ? 6.655   49.078  98.941  1.000 58.377  ? 432 CYS AAA C   1 
ATOM   5685  O O   . CYS D 1 114 ? 5.645   49.558  99.429  1.000 62.779  ? 432 CYS AAA O   1 
ATOM   5686  C CB  . CYS D 1 114 ? 7.043   50.501  96.882  1.000 65.694  ? 432 CYS AAA CB  1 
ATOM   5687  S SG  . CYS D 1 114 ? 7.482   50.485  95.121  1.000 72.294  ? 432 CYS AAA SG  1 
ATOM   5688  N N   . VAL D 1 115 ? 7.622   48.483  99.630  1.000 56.595  ? 433 VAL AAA N   1 
ATOM   5689  C CA  . VAL D 1 115 ? 7.696   48.434  101.117 1.000 51.107  ? 433 VAL AAA CA  1 
ATOM   5690  C C   . VAL D 1 115 ? 8.771   49.427  101.543 1.000 51.777  ? 433 VAL AAA C   1 
ATOM   5691  O O   . VAL D 1 115 ? 9.950   49.099  101.407 1.000 57.075  ? 433 VAL AAA O   1 
ATOM   5692  C CB  . VAL D 1 115 ? 8.006   47.006  101.595 1.000 49.794  ? 433 VAL AAA CB  1 
ATOM   5693  C CG1 . VAL D 1 115 ? 8.223   46.929  103.096 1.000 49.369  ? 433 VAL AAA CG1 1 
ATOM   5694  C CG2 . VAL D 1 115 ? 6.922   46.048  101.152 1.000 51.151  ? 433 VAL AAA CG2 1 
ATOM   5695  N N   . ILE D 1 116 ? 8.361   50.601  102.005 1.000 52.059  ? 434 ILE AAA N   1 
ATOM   5696  C CA  . ILE D 1 116 ? 9.259   51.728  102.370 1.000 51.804  ? 434 ILE AAA CA  1 
ATOM   5697  C C   . ILE D 1 116 ? 9.264   51.862  103.887 1.000 60.042  ? 434 ILE AAA C   1 
ATOM   5698  O O   . ILE D 1 116 ? 8.178   52.051  104.452 1.000 75.243  ? 434 ILE AAA O   1 
ATOM   5699  C CB  . ILE D 1 116 ? 8.749   53.006  101.717 1.000 49.221  ? 434 ILE AAA CB  1 
ATOM   5700  C CG1 . ILE D 1 116 ? 8.587   52.786  100.219 1.000 52.763  ? 434 ILE AAA CG1 1 
ATOM   5701  C CG2 . ILE D 1 116 ? 9.656   54.167  102.060 1.000 51.090  ? 434 ILE AAA CG2 1 
ATOM   5702  C CD1 . ILE D 1 116 ? 7.848   53.904  99.510  1.000 58.056  ? 434 ILE AAA CD1 1 
ATOM   5703  N N   . ALA D 1 117 ? 10.441  51.798  104.508 1.000 61.969  ? 435 ALA AAA N   1 
ATOM   5704  C CA  . ALA D 1 117 ? 10.607  51.835  105.975 1.000 60.975  ? 435 ALA AAA CA  1 
ATOM   5705  C C   . ALA D 1 117 ? 11.736  52.802  106.333 1.000 60.178  ? 435 ALA AAA C   1 
ATOM   5706  O O   . ALA D 1 117 ? 12.621  52.996  105.495 1.000 64.078  ? 435 ALA AAA O   1 
ATOM   5707  C CB  . ALA D 1 117 ? 10.872  50.442  106.478 1.000 55.061  ? 435 ALA AAA CB  1 
ATOM   5708  N N   . TRP D 1 118 ? 11.686  53.385  107.530 1.000 59.902  ? 436 TRP AAA N   1 
ATOM   5709  C CA  . TRP D 1 118 ? 12.766  54.247  108.066 1.000 59.792  ? 436 TRP AAA CA  1 
ATOM   5710  C C   . TRP D 1 118 ? 12.757  54.291  109.592 1.000 62.826  ? 436 TRP AAA C   1 
ATOM   5711  O O   . TRP D 1 118 ? 11.676  54.268  110.177 1.000 69.972  ? 436 TRP AAA O   1 
ATOM   5712  C CB  . TRP D 1 118 ? 12.669  55.651  107.478 1.000 56.589  ? 436 TRP AAA CB  1 
ATOM   5713  C CG  . TRP D 1 118 ? 11.474  56.464  107.853 1.000 51.238  ? 436 TRP AAA CG  1 
ATOM   5714  C CD1 . TRP D 1 118 ? 11.417  57.441  108.802 1.000 50.976  ? 436 TRP AAA CD1 1 
ATOM   5715  C CD2 . TRP D 1 118 ? 10.197  56.463  107.197 1.000 53.184  ? 436 TRP AAA CD2 1 
ATOM   5716  N NE1 . TRP D 1 118 ? 10.183  58.025  108.803 1.000 56.620  ? 436 TRP AAA NE1 1 
ATOM   5717  C CE2 . TRP D 1 118 ? 9.415   57.459  107.822 1.000 55.010  ? 436 TRP AAA CE2 1 
ATOM   5718  C CE3 . TRP D 1 118 ? 9.632   55.708  106.162 1.000 54.866  ? 436 TRP AAA CE3 1 
ATOM   5719  C CZ2 . TRP D 1 118 ? 8.104   57.732  107.441 1.000 52.874  ? 436 TRP AAA CZ2 1 
ATOM   5720  C CZ3 . TRP D 1 118 ? 8.329   55.962  105.796 1.000 56.604  ? 436 TRP AAA CZ3 1 
ATOM   5721  C CH2 . TRP D 1 118 ? 7.583   56.969  106.424 1.000 57.329  ? 436 TRP AAA CH2 1 
ATOM   5722  N N   . ASN D 1 119 ? 13.946  54.381  110.191 1.000 61.476  ? 437 ASN AAA N   1 
ATOM   5723  C CA  . ASN D 1 119 ? 14.140  54.532  111.654 1.000 53.032  ? 437 ASN AAA CA  1 
ATOM   5724  C C   . ASN D 1 119 ? 13.449  55.835  112.084 1.000 54.276  ? 437 ASN AAA C   1 
ATOM   5725  O O   . ASN D 1 119 ? 13.676  56.879  111.455 1.000 47.682  ? 437 ASN AAA O   1 
ATOM   5726  C CB  . ASN D 1 119 ? 15.622  54.452  112.013 1.000 49.426  ? 437 ASN AAA CB  1 
ATOM   5727  C CG  . ASN D 1 119 ? 15.879  54.423  113.502 1.000 47.481  ? 437 ASN AAA CG  1 
ATOM   5728  O OD1 . ASN D 1 119 ? 15.624  55.407  114.194 1.000 46.236  ? 437 ASN AAA OD1 1 
ATOM   5729  N ND2 . ASN D 1 119 ? 16.424  53.319  113.993 1.000 43.557  ? 437 ASN AAA ND2 1 
ATOM   5730  N N   . SER D 1 120 ? 12.569  55.736  113.081 1.000 62.719  ? 438 SER AAA N   1 
ATOM   5731  C CA  . SER D 1 120 ? 11.747  56.845  113.632 1.000 64.473  ? 438 SER AAA CA  1 
ATOM   5732  C C   . SER D 1 120 ? 11.964  56.915  115.142 1.000 61.416  ? 438 SER AAA C   1 
ATOM   5733  O O   . SER D 1 120 ? 10.986  57.145  115.864 1.000 68.258  ? 438 SER AAA O   1 
ATOM   5734  C CB  . SER D 1 120 ? 10.295  56.632  113.308 1.000 63.973  ? 438 SER AAA CB  1 
ATOM   5735  O OG  . SER D 1 120 ? 9.854   55.366  113.791 1.000 57.788  ? 438 SER AAA OG  1 
ATOM   5736  N N   . ASN D 1 121 ? 13.204  56.703  115.589 1.000 56.486  ? 439 ASN AAA N   1 
ATOM   5737  C CA  . ASN D 1 121 ? 13.577  56.655  117.025 1.000 53.492  ? 439 ASN AAA CA  1 
ATOM   5738  C C   . ASN D 1 121 ? 13.427  58.058  117.619 1.000 55.053  ? 439 ASN AAA C   1 
ATOM   5739  O O   . ASN D 1 121 ? 13.122  58.165  118.816 1.000 48.583  ? 439 ASN AAA O   1 
ATOM   5740  C CB  . ASN D 1 121 ? 14.989  56.109  117.207 1.000 54.022  ? 439 ASN AAA CB  1 
ATOM   5741  C CG  . ASN D 1 121 ? 15.237  55.575  118.596 1.000 60.042  ? 439 ASN AAA CG  1 
ATOM   5742  O OD1 . ASN D 1 121 ? 14.329  55.077  119.258 1.000 70.010  ? 439 ASN AAA OD1 1 
ATOM   5743  N ND2 . ASN D 1 121 ? 16.476  55.665  119.036 1.000 60.887  ? 439 ASN AAA ND2 1 
ATOM   5744  N N   . ASN D 1 122 ? 13.614  59.091  116.794 1.000 66.463  ? 440 ASN AAA N   1 
ATOM   5745  C CA  . ASN D 1 122 ? 13.491  60.523  117.191 1.000 70.878  ? 440 ASN AAA CA  1 
ATOM   5746  C C   . ASN D 1 122 ? 12.008  60.866  117.421 1.000 67.222  ? 440 ASN AAA C   1 
ATOM   5747  O O   . ASN D 1 122 ? 11.753  61.786  118.213 1.000 70.434  ? 440 ASN AAA O   1 
ATOM   5748  C CB  . ASN D 1 122 ? 14.181  61.463  116.187 1.000 73.659  ? 440 ASN AAA CB  1 
ATOM   5749  C CG  . ASN D 1 122 ? 13.714  61.276  114.755 1.000 77.519  ? 440 ASN AAA CG  1 
ATOM   5750  O OD1 . ASN D 1 122 ? 13.645  60.143  114.256 1.000 83.456  ? 440 ASN AAA OD1 1 
ATOM   5751  N ND2 . ASN D 1 122 ? 13.366  62.378  114.101 1.000 69.245  ? 440 ASN AAA ND2 1 
ATOM   5752  N N   . LEU D 1 123 ? 11.065  60.158  116.781 1.000 63.668  ? 441 LEU AAA N   1 
ATOM   5753  C CA  . LEU D 1 123 ? 9.615   60.507  116.811 1.000 60.474  ? 441 LEU AAA CA  1 
ATOM   5754  C C   . LEU D 1 123 ? 8.833   59.587  117.755 1.000 59.405  ? 441 LEU AAA C   1 
ATOM   5755  O O   . LEU D 1 123 ? 7.938   60.104  118.429 1.000 68.454  ? 441 LEU AAA O   1 
ATOM   5756  C CB  . LEU D 1 123 ? 9.045   60.434  115.394 1.000 58.816  ? 441 LEU AAA CB  1 
ATOM   5757  C CG  . LEU D 1 123 ? 9.576   61.488  114.421 1.000 61.815  ? 441 LEU AAA CG  1 
ATOM   5758  C CD1 . LEU D 1 123 ? 8.756   61.500  113.139 1.000 59.757  ? 441 LEU AAA CD1 1 
ATOM   5759  C CD2 . LEU D 1 123 ? 9.617   62.876  115.064 1.000 59.653  ? 441 LEU AAA CD2 1 
ATOM   5760  N N   . ASP D 1 124 ? 9.158   58.293  117.815 1.000 55.234  ? 442 ASP AAA N   1 
ATOM   5761  C CA  . ASP D 1 124 ? 8.299   57.253  118.437 1.000 53.450  ? 442 ASP AAA CA  1 
ATOM   5762  C C   . ASP D 1 124 ? 8.993   56.617  119.646 1.000 59.393  ? 442 ASP AAA C   1 
ATOM   5763  O O   . ASP D 1 124 ? 8.632   55.460  119.986 1.000 54.724  ? 442 ASP AAA O   1 
ATOM   5764  C CB  . ASP D 1 124 ? 7.906   56.202  117.395 1.000 51.868  ? 442 ASP AAA CB  1 
ATOM   5765  C CG  . ASP D 1 124 ? 7.067   56.751  116.257 1.000 49.179  ? 442 ASP AAA CG  1 
ATOM   5766  O OD1 . ASP D 1 124 ? 6.334   57.731  116.496 1.000 47.631  ? 442 ASP AAA OD1 1 
ATOM   5767  O OD2 . ASP D 1 124 ? 7.154   56.198  115.144 1.000 43.634  ? 442 ASP AAA OD2 1 
ATOM   5768  N N   . SER D 1 125 ? 9.921   57.337  120.297 1.000 64.585  ? 443 SER AAA N   1 
ATOM   5769  C CA  . SER D 1 125 ? 10.552  56.923  121.584 1.000 66.724  ? 443 SER AAA CA  1 
ATOM   5770  C C   . SER D 1 125 ? 10.304  57.978  122.664 1.000 67.906  ? 443 SER AAA C   1 
ATOM   5771  O O   . SER D 1 125 ? 10.069  59.146  122.310 1.000 71.291  ? 443 SER AAA O   1 
ATOM   5772  C CB  . SER D 1 125 ? 12.014  56.646  121.422 1.000 64.549  ? 443 SER AAA CB  1 
ATOM   5773  O OG  . SER D 1 125 ? 12.208  55.402  120.773 1.000 70.803  ? 443 SER AAA OG  1 
ATOM   5774  N N   . LYS D 1 126 ? 10.320  57.556  123.928 1.000 68.247  ? 444 LYS AAA N   1 
ATOM   5775  C CA  . LYS D 1 126 ? 10.237  58.439  125.118 1.000 76.300  ? 444 LYS AAA CA  1 
ATOM   5776  C C   . LYS D 1 126 ? 11.192  57.894  126.181 1.000 78.394  ? 444 LYS AAA C   1 
ATOM   5777  O O   . LYS D 1 126 ? 11.487  56.674  126.153 1.000 72.833  ? 444 LYS AAA O   1 
ATOM   5778  C CB  . LYS D 1 126 ? 8.807   58.515  125.671 1.000 83.875  ? 444 LYS AAA CB  1 
ATOM   5779  C CG  . LYS D 1 126 ? 7.845   59.354  124.840 1.000 89.540  ? 444 LYS AAA CG  1 
ATOM   5780  C CD  . LYS D 1 126 ? 6.394   59.207  125.236 1.000 98.500  ? 444 LYS AAA CD  1 
ATOM   5781  C CE  . LYS D 1 126 ? 5.436   59.465  124.089 1.000 99.421  ? 444 LYS AAA CE  1 
ATOM   5782  N NZ  . LYS D 1 126 ? 4.042   59.198  124.505 1.000 101.786 ? 444 LYS AAA NZ  1 
ATOM   5783  N N   . VAL D 1 127 ? 11.618  58.782  127.080 1.000 79.401  ? 445 VAL AAA N   1 
ATOM   5784  C CA  . VAL D 1 127 ? 12.511  58.524  128.247 1.000 84.327  ? 445 VAL AAA CA  1 
ATOM   5785  C C   . VAL D 1 127 ? 12.145  57.197  128.942 1.000 84.852  ? 445 VAL AAA C   1 
ATOM   5786  O O   . VAL D 1 127 ? 13.025  56.311  128.994 1.000 91.254  ? 445 VAL AAA O   1 
ATOM   5787  C CB  . VAL D 1 127 ? 12.473  59.728  129.213 1.000 95.599  ? 445 VAL AAA CB  1 
ATOM   5788  C CG1 . VAL D 1 127 ? 13.133  60.953  128.587 1.000 92.641  ? 445 VAL AAA CG1 1 
ATOM   5789  C CG2 . VAL D 1 127 ? 11.061  60.075  129.700 1.000 95.109  ? 445 VAL AAA CG2 1 
ATOM   5790  N N   . GLY D 1 128 ? 10.907  57.031  129.428 1.000 77.319  ? 446 GLY AAA N   1 
ATOM   5791  C CA  . GLY D 1 128 ? 10.494  55.869  130.251 1.000 74.188  ? 446 GLY AAA CA  1 
ATOM   5792  C C   . GLY D 1 128 ? 10.020  54.692  129.407 1.000 74.787  ? 446 GLY AAA C   1 
ATOM   5793  O O   . GLY D 1 128 ? 9.588   53.665  129.987 1.000 77.803  ? 446 GLY AAA O   1 
ATOM   5794  N N   . GLY D 1 129 ? 10.098  54.827  128.079 1.000 73.454  ? 447 GLY AAA N   1 
ATOM   5795  C CA  . GLY D 1 129 ? 9.479   53.912  127.103 1.000 69.242  ? 447 GLY AAA CA  1 
ATOM   5796  C C   . GLY D 1 129 ? 8.124   54.422  126.637 1.000 58.811  ? 447 GLY AAA C   1 
ATOM   5797  O O   . GLY D 1 129 ? 7.264   54.621  127.490 1.000 63.210  ? 447 GLY AAA O   1 
ATOM   5798  N N   . ASN D 1 130 ? 7.963   54.623  125.326 1.000 52.417  ? 448 ASN AAA N   1 
ATOM   5799  C CA  . ASN D 1 130 ? 6.674   54.782  124.598 1.000 49.662  ? 448 ASN AAA CA  1 
ATOM   5800  C C   . ASN D 1 130 ? 6.010   53.408  124.450 1.000 50.034  ? 448 ASN AAA C   1 
ATOM   5801  O O   . ASN D 1 130 ? 6.657   52.475  123.925 1.000 49.096  ? 448 ASN AAA O   1 
ATOM   5802  C CB  . ASN D 1 130 ? 6.922   55.366  123.208 1.000 52.783  ? 448 ASN AAA CB  1 
ATOM   5803  C CG  . ASN D 1 130 ? 5.667   55.756  122.468 1.000 56.054  ? 448 ASN AAA CG  1 
ATOM   5804  O OD1 . ASN D 1 130 ? 4.569   55.429  122.901 1.000 58.451  ? 448 ASN AAA OD1 1 
ATOM   5805  N ND2 . ASN D 1 130 ? 5.830   56.449  121.352 1.000 61.821  ? 448 ASN AAA ND2 1 
ATOM   5806  N N   . TYR D 1 131 ? 4.765   53.256  124.902 1.000 50.037  ? 449 TYR AAA N   1 
ATOM   5807  C CA  . TYR D 1 131 ? 4.079   51.938  124.888 1.000 49.702  ? 449 TYR AAA CA  1 
ATOM   5808  C C   . TYR D 1 131 ? 2.779   52.003  124.063 1.000 51.706  ? 449 TYR AAA C   1 
ATOM   5809  O O   . TYR D 1 131 ? 1.958   51.082  124.174 1.000 46.766  ? 449 TYR AAA O   1 
ATOM   5810  C CB  . TYR D 1 131 ? 3.905   51.459  126.333 1.000 46.413  ? 449 TYR AAA CB  1 
ATOM   5811  C CG  . TYR D 1 131 ? 5.162   50.994  127.035 1.000 40.971  ? 449 TYR AAA CG  1 
ATOM   5812  C CD1 . TYR D 1 131 ? 5.894   51.849  127.857 1.000 39.348  ? 449 TYR AAA CD1 1 
ATOM   5813  C CD2 . TYR D 1 131 ? 5.591   49.680  126.931 1.000 38.746  ? 449 TYR AAA CD2 1 
ATOM   5814  C CE1 . TYR D 1 131 ? 7.040   51.432  128.513 1.000 36.287  ? 449 TYR AAA CE1 1 
ATOM   5815  C CE2 . TYR D 1 131 ? 6.737   49.244  127.587 1.000 37.224  ? 449 TYR AAA CE2 1 
ATOM   5816  C CZ  . TYR D 1 131 ? 7.467   50.125  128.369 1.000 37.400  ? 449 TYR AAA CZ  1 
ATOM   5817  O OH  . TYR D 1 131 ? 8.599   49.709  129.008 1.000 37.242  ? 449 TYR AAA OH  1 
ATOM   5818  N N   . ASN D 1 132 ? 2.614   53.039  123.235 1.000 53.683  ? 450 ASN AAA N   1 
ATOM   5819  C CA  . ASN D 1 132 ? 1.355   53.338  122.503 1.000 57.337  ? 450 ASN AAA CA  1 
ATOM   5820  C C   . ASN D 1 132 ? 1.254   52.475  121.238 1.000 57.937  ? 450 ASN AAA C   1 
ATOM   5821  O O   . ASN D 1 132 ? 0.119   52.251  120.777 1.000 64.787  ? 450 ASN AAA O   1 
ATOM   5822  C CB  . ASN D 1 132 ? 1.228   54.830  122.204 1.000 59.181  ? 450 ASN AAA CB  1 
ATOM   5823  C CG  . ASN D 1 132 ? 1.259   55.650  123.477 1.000 64.817  ? 450 ASN AAA CG  1 
ATOM   5824  O OD1 . ASN D 1 132 ? 0.226   56.026  124.022 1.000 69.007  ? 450 ASN AAA OD1 1 
ATOM   5825  N ND2 . ASN D 1 132 ? 2.449   55.904  123.988 1.000 78.828  ? 450 ASN AAA ND2 1 
ATOM   5826  N N   . TYR D 1 133 ? 2.378   51.986  120.709 1.000 56.058  ? 451 TYR AAA N   1 
ATOM   5827  C CA  . TYR D 1 133 ? 2.434   51.105  119.511 1.000 49.810  ? 451 TYR AAA CA  1 
ATOM   5828  C C   . TYR D 1 133 ? 2.302   49.659  119.975 1.000 48.320  ? 451 TYR AAA C   1 
ATOM   5829  O O   . TYR D 1 133 ? 3.114   49.270  120.848 1.000 56.585  ? 451 TYR AAA O   1 
ATOM   5830  C CB  . TYR D 1 133 ? 3.724   51.368  118.733 1.000 47.831  ? 451 TYR AAA CB  1 
ATOM   5831  C CG  . TYR D 1 133 ? 3.758   52.740  118.120 1.000 47.247  ? 451 TYR AAA CG  1 
ATOM   5832  C CD1 . TYR D 1 133 ? 2.994   53.015  117.006 1.000 48.538  ? 451 TYR AAA CD1 1 
ATOM   5833  C CD2 . TYR D 1 133 ? 4.503   53.771  118.666 1.000 49.320  ? 451 TYR AAA CD2 1 
ATOM   5834  C CE1 . TYR D 1 133 ? 2.980   54.271  116.426 1.000 49.958  ? 451 TYR AAA CE1 1 
ATOM   5835  C CE2 . TYR D 1 133 ? 4.488   55.037  118.109 1.000 51.406  ? 451 TYR AAA CE2 1 
ATOM   5836  C CZ  . TYR D 1 133 ? 3.724   55.286  116.985 1.000 50.601  ? 451 TYR AAA CZ  1 
ATOM   5837  O OH  . TYR D 1 133 ? 3.704   56.517  116.407 1.000 54.999  ? 451 TYR AAA OH  1 
ATOM   5838  N N   . LEU D 1 134 ? 1.296   48.937  119.454 1.000 43.616  ? 452 LEU AAA N   1 
ATOM   5839  C CA  . LEU D 1 134 ? 0.962   47.542  119.856 1.000 44.184  ? 452 LEU AAA CA  1 
ATOM   5840  C C   . LEU D 1 134 ? 1.072   46.598  118.666 1.000 40.895  ? 452 LEU AAA C   1 
ATOM   5841  O O   . LEU D 1 134 ? 1.166   47.072  117.520 1.000 41.448  ? 452 LEU AAA O   1 
ATOM   5842  C CB  . LEU D 1 134 ? -0.466  47.451  120.395 1.000 47.846  ? 452 LEU AAA CB  1 
ATOM   5843  C CG  . LEU D 1 134 ? -0.883  48.494  121.427 1.000 51.458  ? 452 LEU AAA CG  1 
ATOM   5844  C CD1 . LEU D 1 134 ? -2.304  48.207  121.864 1.000 51.207  ? 452 LEU AAA CD1 1 
ATOM   5845  C CD2 . LEU D 1 134 ? 0.037   48.522  122.648 1.000 58.310  ? 452 LEU AAA CD2 1 
ATOM   5846  N N   . TYR D 1 135 ? 1.017   45.304  118.969 1.000 39.241  ? 453 TYR AAA N   1 
ATOM   5847  C CA  . TYR D 1 135 ? 1.149   44.184  118.006 1.000 42.654  ? 453 TYR AAA CA  1 
ATOM   5848  C C   . TYR D 1 135 ? 0.387   42.985  118.555 1.000 43.093  ? 453 TYR AAA C   1 
ATOM   5849  O O   . TYR D 1 135 ? 0.429   42.751  119.778 1.000 43.991  ? 453 TYR AAA O   1 
ATOM   5850  C CB  . TYR D 1 135 ? 2.619   43.845  117.715 1.000 46.354  ? 453 TYR AAA CB  1 
ATOM   5851  C CG  . TYR D 1 135 ? 3.460   43.272  118.837 1.000 45.438  ? 453 TYR AAA CG  1 
ATOM   5852  C CD1 . TYR D 1 135 ? 3.658   41.906  118.965 1.000 46.445  ? 453 TYR AAA CD1 1 
ATOM   5853  C CD2 . TYR D 1 135 ? 4.133   44.099  119.715 1.000 45.000  ? 453 TYR AAA CD2 1 
ATOM   5854  C CE1 . TYR D 1 135 ? 4.433   41.374  119.978 1.000 50.068  ? 453 TYR AAA CE1 1 
ATOM   5855  C CE2 . TYR D 1 135 ? 4.931   43.585  120.724 1.000 48.010  ? 453 TYR AAA CE2 1 
ATOM   5856  C CZ  . TYR D 1 135 ? 5.075   42.217  120.867 1.000 52.180  ? 453 TYR AAA CZ  1 
ATOM   5857  O OH  . TYR D 1 135 ? 5.854   41.715  121.874 1.000 57.673  ? 453 TYR AAA OH  1 
ATOM   5858  N N   . ARG D 1 136 ? -0.296  42.259  117.671 1.000 43.214  ? 454 ARG AAA N   1 
ATOM   5859  C CA  . ARG D 1 136 ? -1.039  41.039  118.046 1.000 47.972  ? 454 ARG AAA CA  1 
ATOM   5860  C C   . ARG D 1 136 ? -0.001  39.955  118.329 1.000 48.701  ? 454 ARG AAA C   1 
ATOM   5861  O O   . ARG D 1 136 ? 0.776   39.652  117.424 1.000 51.197  ? 454 ARG AAA O   1 
ATOM   5862  C CB  . ARG D 1 136 ? -2.020  40.661  116.934 1.000 51.825  ? 454 ARG AAA CB  1 
ATOM   5863  C CG  . ARG D 1 136 ? -2.870  39.430  117.222 1.000 51.734  ? 454 ARG AAA CG  1 
ATOM   5864  C CD  . ARG D 1 136 ? -3.994  39.301  116.207 1.000 54.598  ? 454 ARG AAA CD  1 
ATOM   5865  N NE  . ARG D 1 136 ? -4.787  40.517  116.194 1.000 55.038  ? 454 ARG AAA NE  1 
ATOM   5866  C CZ  . ARG D 1 136 ? -5.742  40.794  117.075 1.000 55.687  ? 454 ARG AAA CZ  1 
ATOM   5867  N NH1 . ARG D 1 136 ? -6.069  39.912  118.012 1.000 54.049  ? 454 ARG AAA NH1 1 
ATOM   5868  N NH2 . ARG D 1 136 ? -6.375  41.954  117.000 1.000 58.334  ? 454 ARG AAA NH2 1 
ATOM   5869  N N   . LEU D 1 137 ? 0.005   39.414  119.547 1.000 49.524  ? 455 LEU AAA N   1 
ATOM   5870  C CA  . LEU D 1 137 ? 0.983   38.401  119.999 1.000 50.826  ? 455 LEU AAA CA  1 
ATOM   5871  C C   . LEU D 1 137 ? 0.438   37.001  119.713 1.000 51.319  ? 455 LEU AAA C   1 
ATOM   5872  O O   . LEU D 1 137 ? 1.250   36.114  119.392 1.000 46.787  ? 455 LEU AAA O   1 
ATOM   5873  C CB  . LEU D 1 137 ? 1.240   38.605  121.490 1.000 56.119  ? 455 LEU AAA CB  1 
ATOM   5874  C CG  . LEU D 1 137 ? 2.269   37.658  122.091 1.000 66.199  ? 455 LEU AAA CG  1 
ATOM   5875  C CD1 . LEU D 1 137 ? 3.609   37.773  121.364 1.000 75.277  ? 455 LEU AAA CD1 1 
ATOM   5876  C CD2 . LEU D 1 137 ? 2.437   37.919  123.573 1.000 69.273  ? 455 LEU AAA CD2 1 
ATOM   5877  N N   . PHE D 1 138 ? -0.884  36.807  119.837 1.000 54.672  ? 456 PHE AAA N   1 
ATOM   5878  C CA  . PHE D 1 138 ? -1.566  35.500  119.640 1.000 56.120  ? 456 PHE AAA CA  1 
ATOM   5879  C C   . PHE D 1 138 ? -2.753  35.610  118.674 1.000 53.678  ? 456 PHE AAA C   1 
ATOM   5880  O O   . PHE D 1 138 ? -3.455  36.646  118.632 1.000 50.963  ? 456 PHE AAA O   1 
ATOM   5881  C CB  . PHE D 1 138 ? -2.052  34.958  120.978 1.000 59.127  ? 456 PHE AAA CB  1 
ATOM   5882  C CG  . PHE D 1 138 ? -1.002  34.925  122.054 1.000 61.619  ? 456 PHE AAA CG  1 
ATOM   5883  C CD1 . PHE D 1 138 ? 0.001   33.970  122.024 1.000 65.223  ? 456 PHE AAA CD1 1 
ATOM   5884  C CD2 . PHE D 1 138 ? -1.018  35.850  123.085 1.000 64.144  ? 456 PHE AAA CD2 1 
ATOM   5885  C CE1 . PHE D 1 138 ? 0.969   33.940  123.013 1.000 66.167  ? 456 PHE AAA CE1 1 
ATOM   5886  C CE2 . PHE D 1 138 ? -0.051  35.819  124.074 1.000 65.532  ? 456 PHE AAA CE2 1 
ATOM   5887  C CZ  . PHE D 1 138 ? 0.937   34.861  124.037 1.000 67.461  ? 456 PHE AAA CZ  1 
ATOM   5888  N N   . ARG D 1 139 ? -2.977  34.531  117.927 1.000 50.320  ? 457 ARG AAA N   1 
ATOM   5889  C CA  . ARG D 1 139 ? -4.109  34.385  116.984 1.000 52.060  ? 457 ARG AAA CA  1 
ATOM   5890  C C   . ARG D 1 139 ? -4.234  32.914  116.580 1.000 61.543  ? 457 ARG AAA C   1 
ATOM   5891  O O   . ARG D 1 139 ? -3.181  32.256  116.401 1.000 64.770  ? 457 ARG AAA O   1 
ATOM   5892  C CB  . ARG D 1 139 ? -3.909  35.257  115.750 1.000 48.134  ? 457 ARG AAA CB  1 
ATOM   5893  C CG  . ARG D 1 139 ? -5.202  35.532  115.008 1.000 53.900  ? 457 ARG AAA CG  1 
ATOM   5894  C CD  . ARG D 1 139 ? -5.033  36.544  113.900 1.000 56.763  ? 457 ARG AAA CD  1 
ATOM   5895  N NE  . ARG D 1 139 ? -6.285  36.967  113.273 1.000 58.228  ? 457 ARG AAA NE  1 
ATOM   5896  C CZ  . ARG D 1 139 ? -6.928  36.308  112.302 1.000 58.510  ? 457 ARG AAA CZ  1 
ATOM   5897  N NH1 . ARG D 1 139 ? -6.469  35.149  111.854 1.000 56.751  ? 457 ARG AAA NH1 1 
ATOM   5898  N NH2 . ARG D 1 139 ? -8.049  36.802  111.798 1.000 57.868  ? 457 ARG AAA NH2 1 
ATOM   5899  N N   . LYS D 1 140 ? -5.479  32.433  116.452 1.000 70.050  ? 458 LYS AAA N   1 
ATOM   5900  C CA  . LYS D 1 140 ? -5.832  31.000  116.271 1.000 69.758  ? 458 LYS AAA CA  1 
ATOM   5901  C C   . LYS D 1 140 ? -5.325  30.520  114.905 1.000 67.524  ? 458 LYS AAA C   1 
ATOM   5902  O O   . LYS D 1 140 ? -4.857  29.376  114.823 1.000 72.899  ? 458 LYS AAA O   1 
ATOM   5903  C CB  . LYS D 1 140 ? -7.342  30.823  116.466 1.000 76.526  ? 458 LYS AAA CB  1 
ATOM   5904  C CG  . LYS D 1 140 ? -7.787  30.987  117.913 1.000 85.262  ? 458 LYS AAA CG  1 
ATOM   5905  C CD  . LYS D 1 140 ? -9.239  31.355  118.128 1.000 93.024  ? 458 LYS AAA CD  1 
ATOM   5906  C CE  . LYS D 1 140 ? -9.429  32.135  119.419 1.000 97.878  ? 458 LYS AAA CE  1 
ATOM   5907  N NZ  . LYS D 1 140 ? -10.856 32.235  119.804 1.000 103.769 ? 458 LYS AAA NZ  1 
ATOM   5908  N N   . SER D 1 141 ? -5.407  31.367  113.878 1.000 66.270  ? 459 SER AAA N   1 
ATOM   5909  C CA  . SER D 1 141 ? -4.885  31.095  112.510 1.000 63.886  ? 459 SER AAA CA  1 
ATOM   5910  C C   . SER D 1 141 ? -4.198  32.355  111.976 1.000 59.490  ? 459 SER AAA C   1 
ATOM   5911  O O   . SER D 1 141 ? -4.419  33.460  112.551 1.000 53.341  ? 459 SER AAA O   1 
ATOM   5912  C CB  . SER D 1 141 ? -5.976  30.631  111.575 1.000 65.206  ? 459 SER AAA CB  1 
ATOM   5913  O OG  . SER D 1 141 ? -6.986  31.628  111.440 1.000 70.749  ? 459 SER AAA OG  1 
ATOM   5914  N N   . ASN D 1 142 ? -3.385  32.191  110.930 1.000 55.259  ? 460 ASN AAA N   1 
ATOM   5915  C CA  . ASN D 1 142 ? -2.635  33.307  110.293 1.000 55.814  ? 460 ASN AAA CA  1 
ATOM   5916  C C   . ASN D 1 142 ? -3.632  34.198  109.543 1.000 50.918  ? 460 ASN AAA C   1 
ATOM   5917  O O   . ASN D 1 142 ? -4.652  33.661  109.079 1.000 52.847  ? 460 ASN AAA O   1 
ATOM   5918  C CB  . ASN D 1 142 ? -1.531  32.802  109.361 1.000 59.417  ? 460 ASN AAA CB  1 
ATOM   5919  C CG  . ASN D 1 142 ? -0.624  31.777  110.015 1.000 62.086  ? 460 ASN AAA CG  1 
ATOM   5920  O OD1 . ASN D 1 142 ? -0.715  31.516  111.213 1.000 69.366  ? 460 ASN AAA OD1 1 
ATOM   5921  N ND2 . ASN D 1 142 ? 0.279   31.205  109.244 1.000 58.265  ? 460 ASN AAA ND2 1 
ATOM   5922  N N   . LEU D 1 143 ? -3.362  35.503  109.457 1.000 45.089  ? 461 LEU AAA N   1 
ATOM   5923  C CA  . LEU D 1 143 ? -4.129  36.459  108.622 1.000 43.341  ? 461 LEU AAA CA  1 
ATOM   5924  C C   . LEU D 1 143 ? -4.081  36.021  107.157 1.000 45.862  ? 461 LEU AAA C   1 
ATOM   5925  O O   . LEU D 1 143 ? -3.082  35.428  106.735 1.000 46.677  ? 461 LEU AAA O   1 
ATOM   5926  C CB  . LEU D 1 143 ? -3.521  37.855  108.759 1.000 41.939  ? 461 LEU AAA CB  1 
ATOM   5927  C CG  . LEU D 1 143 ? -3.783  38.573  110.079 1.000 43.766  ? 461 LEU AAA CG  1 
ATOM   5928  C CD1 . LEU D 1 143 ? -3.272  40.004  110.034 1.000 45.848  ? 461 LEU AAA CD1 1 
ATOM   5929  C CD2 . LEU D 1 143 ? -5.257  38.572  110.407 1.000 43.166  ? 461 LEU AAA CD2 1 
ATOM   5930  N N   . LYS D 1 144 ? -5.133  36.324  106.405 1.000 50.596  ? 462 LYS AAA N   1 
ATOM   5931  C CA  . LYS D 1 144 ? -5.094  36.323  104.921 1.000 56.152  ? 462 LYS AAA CA  1 
ATOM   5932  C C   . LYS D 1 144 ? -4.419  37.622  104.484 1.000 51.463  ? 462 LYS AAA C   1 
ATOM   5933  O O   . LYS D 1 144 ? -4.347  38.583  105.239 1.000 54.850  ? 462 LYS AAA O   1 
ATOM   5934  C CB  . LYS D 1 144 ? -6.500  36.127  104.341 1.000 65.099  ? 462 LYS AAA CB  1 
ATOM   5935  C CG  . LYS D 1 144 ? -7.174  34.819  104.767 1.000 74.649  ? 462 LYS AAA CG  1 
ATOM   5936  C CD  . LYS D 1 144 ? -7.846  34.032  103.659 1.000 78.211  ? 462 LYS AAA CD  1 
ATOM   5937  C CE  . LYS D 1 144 ? -9.164  34.625  103.208 1.000 80.029  ? 462 LYS AAA CE  1 
ATOM   5938  N NZ  . LYS D 1 144 ? -10.191 34.557  104.273 1.000 82.884  ? 462 LYS AAA NZ  1 
ATOM   5939  N N   . PRO D 1 145 ? -3.827  37.671  103.278 1.000 46.294  ? 463 PRO AAA N   1 
ATOM   5940  C CA  . PRO D 1 145 ? -3.280  38.909  102.736 1.000 43.976  ? 463 PRO AAA CA  1 
ATOM   5941  C C   . PRO D 1 145 ? -4.204  40.120  102.892 1.000 42.100  ? 463 PRO AAA C   1 
ATOM   5942  O O   . PRO D 1 145 ? -5.344  40.021  102.559 1.000 38.801  ? 463 PRO AAA O   1 
ATOM   5943  C CB  . PRO D 1 145 ? -3.102  38.553  101.255 1.000 46.197  ? 463 PRO AAA CB  1 
ATOM   5944  C CG  . PRO D 1 145 ? -2.737  37.088  101.297 1.000 46.879  ? 463 PRO AAA CG  1 
ATOM   5945  C CD  . PRO D 1 145 ? -3.600  36.518  102.401 1.000 48.240  ? 463 PRO AAA CD  1 
ATOM   5946  N N   . PHE D 1 146 ? -3.668  41.225  103.398 1.000 46.033  ? 464 PHE AAA N   1 
ATOM   5947  C CA  . PHE D 1 146 ? -4.395  42.505  103.582 1.000 53.314  ? 464 PHE AAA CA  1 
ATOM   5948  C C   . PHE D 1 146 ? -5.585  42.292  104.510 1.000 55.298  ? 464 PHE AAA C   1 
ATOM   5949  O O   . PHE D 1 146 ? -6.576  43.023  104.347 1.000 56.931  ? 464 PHE AAA O   1 
ATOM   5950  C CB  . PHE D 1 146 ? -4.878  43.058  102.239 1.000 57.800  ? 464 PHE AAA CB  1 
ATOM   5951  C CG  . PHE D 1 146 ? -3.767  43.392  101.283 1.000 67.824  ? 464 PHE AAA CG  1 
ATOM   5952  C CD1 . PHE D 1 146 ? -2.766  44.274  101.657 1.000 74.809  ? 464 PHE AAA CD1 1 
ATOM   5953  C CD2 . PHE D 1 146 ? -3.707  42.814  100.026 1.000 71.607  ? 464 PHE AAA CD2 1 
ATOM   5954  C CE1 . PHE D 1 146 ? -1.736  44.584  100.786 1.000 77.305  ? 464 PHE AAA CE1 1 
ATOM   5955  C CE2 . PHE D 1 146 ? -2.679  43.128  99.155  1.000 71.161  ? 464 PHE AAA CE2 1 
ATOM   5956  C CZ  . PHE D 1 146 ? -1.697  44.009  99.537  1.000 73.538  ? 464 PHE AAA CZ  1 
ATOM   5957  N N   . GLU D 1 147 ? -5.497  41.330  105.436 1.000 57.700  ? 465 GLU AAA N   1 
ATOM   5958  C CA  . GLU D 1 147 ? -6.497  41.160  106.523 1.000 53.173  ? 465 GLU AAA CA  1 
ATOM   5959  C C   . GLU D 1 147 ? -6.054  42.041  107.685 1.000 49.727  ? 465 GLU AAA C   1 
ATOM   5960  O O   . GLU D 1 147 ? -4.831  42.238  107.875 1.000 52.888  ? 465 GLU AAA O   1 
ATOM   5961  C CB  . GLU D 1 147 ? -6.672  39.698  106.944 1.000 53.146  ? 465 GLU AAA CB  1 
ATOM   5962  C CG  . GLU D 1 147 ? -7.844  39.450  107.890 1.000 52.681  ? 465 GLU AAA CG  1 
ATOM   5963  C CD  . GLU D 1 147 ? -8.287  37.994  108.065 1.000 52.650  ? 465 GLU AAA CD  1 
ATOM   5964  O OE1 . GLU D 1 147 ? -7.472  37.081  107.862 1.000 50.066  ? 465 GLU AAA OE1 1 
ATOM   5965  O OE2 . GLU D 1 147 ? -9.458  37.766  108.400 1.000 57.039  ? 465 GLU AAA OE2 1 
ATOM   5966  N N   . ARG D 1 148 ? -7.040  42.557  108.402 1.000 46.661  ? 466 ARG AAA N   1 
ATOM   5967  C CA  . ARG D 1 148 ? -6.873  43.515  109.509 1.000 49.958  ? 466 ARG AAA CA  1 
ATOM   5968  C C   . ARG D 1 148 ? -7.808  43.101  110.643 1.000 55.577  ? 466 ARG AAA C   1 
ATOM   5969  O O   . ARG D 1 148 ? -9.045  43.240  110.498 1.000 55.326  ? 466 ARG AAA O   1 
ATOM   5970  C CB  . ARG D 1 148 ? -7.217  44.892  108.972 1.000 48.483  ? 466 ARG AAA CB  1 
ATOM   5971  C CG  . ARG D 1 148 ? -6.981  46.020  109.951 1.000 48.611  ? 466 ARG AAA CG  1 
ATOM   5972  C CD  . ARG D 1 148 ? -7.607  47.204  109.278 1.000 52.241  ? 466 ARG AAA CD  1 
ATOM   5973  N NE  . ARG D 1 148 ? -7.400  48.326  110.144 1.000 61.042  ? 466 ARG AAA NE  1 
ATOM   5974  C CZ  . ARG D 1 148 ? -8.081  49.445  110.081 1.000 75.393  ? 466 ARG AAA CZ  1 
ATOM   5975  N NH1 . ARG D 1 148 ? -9.036  49.592  109.176 1.000 90.890  ? 466 ARG AAA NH1 1 
ATOM   5976  N NH2 . ARG D 1 148 ? -7.799  50.409  110.936 1.000 80.367  ? 466 ARG AAA NH2 1 
ATOM   5977  N N   . ASP D 1 149 ? -7.226  42.563  111.712 1.000 57.832  ? 467 ASP AAA N   1 
ATOM   5978  C CA  . ASP D 1 149 ? -7.956  42.076  112.905 1.000 52.970  ? 467 ASP AAA CA  1 
ATOM   5979  C C   . ASP D 1 149 ? -7.692  43.078  114.022 1.000 51.006  ? 467 ASP AAA C   1 
ATOM   5980  O O   . ASP D 1 149 ? -6.504  43.258  114.356 1.000 61.087  ? 467 ASP AAA O   1 
ATOM   5981  C CB  . ASP D 1 149 ? -7.477  40.669  113.244 1.000 55.617  ? 467 ASP AAA CB  1 
ATOM   5982  C CG  . ASP D 1 149 ? -8.254  39.973  114.344 1.000 58.761  ? 467 ASP AAA CG  1 
ATOM   5983  O OD1 . ASP D 1 149 ? -8.982  40.682  115.084 1.000 60.375  ? 467 ASP AAA OD1 1 
ATOM   5984  O OD2 . ASP D 1 149 ? -8.116  38.722  114.448 1.000 57.488  ? 467 ASP AAA OD2 1 
ATOM   5985  N N   . ILE D 1 150 ? -8.744  43.724  114.534 1.000 49.258  ? 468 ILE AAA N   1 
ATOM   5986  C CA  . ILE D 1 150 ? -8.675  44.660  115.696 1.000 50.890  ? 468 ILE AAA CA  1 
ATOM   5987  C C   . ILE D 1 150 ? -9.465  44.083  116.883 1.000 47.528  ? 468 ILE AAA C   1 
ATOM   5988  O O   . ILE D 1 150 ? -9.590  44.812  117.898 1.000 41.735  ? 468 ILE AAA O   1 
ATOM   5989  C CB  . ILE D 1 150 ? -9.152  46.075  115.307 1.000 52.385  ? 468 ILE AAA CB  1 
ATOM   5990  C CG1 . ILE D 1 150 ? -10.549 46.081  114.685 1.000 56.900  ? 468 ILE AAA CG1 1 
ATOM   5991  C CG2 . ILE D 1 150 ? -8.142  46.739  114.392 1.000 50.558  ? 468 ILE AAA CG2 1 
ATOM   5992  C CD1 . ILE D 1 150 ? -11.104 47.481  114.512 1.000 60.890  ? 468 ILE AAA CD1 1 
ATOM   5993  N N   . SER D 1 151 ? -9.908  42.817  116.794 1.000 43.318  ? 469 SER AAA N   1 
ATOM   5994  C CA  . SER D 1 151 ? -10.585 42.075  117.892 1.000 45.946  ? 469 SER AAA CA  1 
ATOM   5995  C C   . SER D 1 151 ? -9.661  41.992  119.120 1.000 47.097  ? 469 SER AAA C   1 
ATOM   5996  O O   . SER D 1 151 ? -8.455  41.805  118.937 1.000 51.976  ? 469 SER AAA O   1 
ATOM   5997  C CB  . SER D 1 151 ? -11.064 40.699  117.438 1.000 44.454  ? 469 SER AAA CB  1 
ATOM   5998  O OG  . SER D 1 151 ? -10.068 39.702  117.586 1.000 40.708  ? 469 SER AAA OG  1 
ATOM   5999  N N   . THR D 1 152 ? -10.213 42.152  120.326 1.000 45.043  ? 470 THR AAA N   1 
ATOM   6000  C CA  . THR D 1 152 ? -9.479  42.025  121.610 1.000 42.949  ? 470 THR AAA CA  1 
ATOM   6001  C C   . THR D 1 152 ? -10.043 40.822  122.380 1.000 44.041  ? 470 THR AAA C   1 
ATOM   6002  O O   . THR D 1 152 ? -9.970  40.813  123.619 1.000 41.497  ? 470 THR AAA O   1 
ATOM   6003  C CB  . THR D 1 152 ? -9.495  43.365  122.354 1.000 41.563  ? 470 THR AAA CB  1 
ATOM   6004  O OG1 . THR D 1 152 ? -10.823 43.857  122.421 1.000 43.030  ? 470 THR AAA OG1 1 
ATOM   6005  C CG2 . THR D 1 152 ? -8.691  44.429  121.656 1.000 43.049  ? 470 THR AAA CG2 1 
ATOM   6006  N N   . GLU D 1 153 ? -10.550 39.825  121.654 1.000 49.249  ? 471 GLU AAA N   1 
ATOM   6007  C CA  . GLU D 1 153 ? -10.928 38.495  122.201 1.000 56.781  ? 471 GLU AAA CA  1 
ATOM   6008  C C   . GLU D 1 153 ? -9.758  37.968  123.024 1.000 50.426  ? 471 GLU AAA C   1 
ATOM   6009  O O   . GLU D 1 153 ? -8.615  37.994  122.519 1.000 51.201  ? 471 GLU AAA O   1 
ATOM   6010  C CB  . GLU D 1 153 ? -11.217 37.484  121.090 1.000 69.651  ? 471 GLU AAA CB  1 
ATOM   6011  C CG  . GLU D 1 153 ? -12.321 37.912  120.133 1.000 81.736  ? 471 GLU AAA CG  1 
ATOM   6012  C CD  . GLU D 1 153 ? -13.720 37.591  120.637 1.000 87.894  ? 471 GLU AAA CD  1 
ATOM   6013  O OE1 . GLU D 1 153 ? -14.555 38.528  120.726 1.000 87.978  ? 471 GLU AAA OE1 1 
ATOM   6014  O OE2 . GLU D 1 153 ? -13.960 36.405  120.946 1.000 96.797  ? 471 GLU AAA OE2 1 
ATOM   6015  N N   . ILE D 1 154 ? -10.035 37.476  124.223 1.000 45.332  ? 472 ILE AAA N   1 
ATOM   6016  C CA  . ILE D 1 154 ? -9.002  36.838  125.080 1.000 44.774  ? 472 ILE AAA CA  1 
ATOM   6017  C C   . ILE D 1 154 ? -8.599  35.525  124.404 1.000 46.311  ? 472 ILE AAA C   1 
ATOM   6018  O O   . ILE D 1 154 ? -9.501  34.749  124.040 1.000 47.524  ? 472 ILE AAA O   1 
ATOM   6019  C CB  . ILE D 1 154 ? -9.520  36.646  126.518 1.000 42.615  ? 472 ILE AAA CB  1 
ATOM   6020  C CG1 . ILE D 1 154 ? -10.002 37.960  127.139 1.000 41.571  ? 472 ILE AAA CG1 1 
ATOM   6021  C CG2 . ILE D 1 154 ? -8.476  35.972  127.385 1.000 44.734  ? 472 ILE AAA CG2 1 
ATOM   6022  C CD1 . ILE D 1 154 ? -9.079  39.134  126.974 1.000 40.131  ? 472 ILE AAA CD1 1 
ATOM   6023  N N   . TYR D 1 155 ? -7.297  35.312  124.204 1.000 47.093  ? 473 TYR AAA N   1 
ATOM   6024  C CA  . TYR D 1 155 ? -6.766  34.145  123.470 1.000 50.199  ? 473 TYR AAA CA  1 
ATOM   6025  C C   . TYR D 1 155 ? -6.793  32.945  124.406 1.000 52.424  ? 473 TYR AAA C   1 
ATOM   6026  O O   . TYR D 1 155 ? -6.213  33.052  125.505 1.000 50.373  ? 473 TYR AAA O   1 
ATOM   6027  C CB  . TYR D 1 155 ? -5.352  34.418  122.955 1.000 51.965  ? 473 TYR AAA CB  1 
ATOM   6028  C CG  . TYR D 1 155 ? -4.750  33.284  122.156 1.000 57.760  ? 473 TYR AAA CG  1 
ATOM   6029  C CD1 . TYR D 1 155 ? -5.094  33.069  120.827 1.000 57.814  ? 473 TYR AAA CD1 1 
ATOM   6030  C CD2 . TYR D 1 155 ? -3.820  32.425  122.729 1.000 64.018  ? 473 TYR AAA CD2 1 
ATOM   6031  C CE1 . TYR D 1 155 ? -4.535  32.035  120.095 1.000 60.853  ? 473 TYR AAA CE1 1 
ATOM   6032  C CE2 . TYR D 1 155 ? -3.254  31.383  122.013 1.000 62.347  ? 473 TYR AAA CE2 1 
ATOM   6033  C CZ  . TYR D 1 155 ? -3.626  31.182  120.698 1.000 63.202  ? 473 TYR AAA CZ  1 
ATOM   6034  O OH  . TYR D 1 155 ? -3.072  30.157  119.998 1.000 67.690  ? 473 TYR AAA OH  1 
ATOM   6035  N N   . GLN D 1 156 ? -7.428  31.854  123.972 1.000 60.192  ? 474 GLN AAA N   1 
ATOM   6036  C CA  . GLN D 1 156 ? -7.468  30.579  124.729 1.000 68.164  ? 474 GLN AAA CA  1 
ATOM   6037  C C   . GLN D 1 156 ? -6.266  29.725  124.318 1.000 65.004  ? 474 GLN AAA C   1 
ATOM   6038  O O   . GLN D 1 156 ? -6.293  29.166  123.209 1.000 66.504  ? 474 GLN AAA O   1 
ATOM   6039  C CB  . GLN D 1 156 ? -8.796  29.858  124.483 1.000 74.583  ? 474 GLN AAA CB  1 
ATOM   6040  C CG  . GLN D 1 156 ? -8.947  28.589  125.308 1.000 74.946  ? 474 GLN AAA CG  1 
ATOM   6041  C CD  . GLN D 1 156 ? -10.263 27.909  125.052 1.000 76.307  ? 474 GLN AAA CD  1 
ATOM   6042  O OE1 . GLN D 1 156 ? -11.252 28.552  124.695 1.000 78.158  ? 474 GLN AAA OE1 1 
ATOM   6043  N NE2 . GLN D 1 156 ? -10.272 26.600  125.250 1.000 76.274  ? 474 GLN AAA NE2 1 
ATOM   6044  N N   . ALA D 1 157 ? -5.255  29.641  125.182 1.000 66.013  ? 475 ALA AAA N   1 
ATOM   6045  C CA  . ALA D 1 157 ? -4.020  28.853  124.961 1.000 71.068  ? 475 ALA AAA CA  1 
ATOM   6046  C C   . ALA D 1 157 ? -4.184  27.437  125.524 1.000 71.504  ? 475 ALA AAA C   1 
ATOM   6047  O O   . ALA D 1 157 ? -3.558  26.539  124.958 1.000 73.702  ? 475 ALA AAA O   1 
ATOM   6048  C CB  . ALA D 1 157 ? -2.838  29.562  125.575 1.000 72.511  ? 475 ALA AAA CB  1 
ATOM   6049  N N   . GLY D 1 158 ? -5.009  27.254  126.568 1.000 78.286  ? 476 GLY AAA N   1 
ATOM   6050  C CA  . GLY D 1 158 ? -5.145  26.004  127.348 1.000 82.807  ? 476 GLY AAA CA  1 
ATOM   6051  C C   . GLY D 1 158 ? -6.474  25.299  127.131 1.000 85.903  ? 476 GLY AAA C   1 
ATOM   6052  O O   . GLY D 1 158 ? -7.341  25.872  126.421 1.000 86.977  ? 476 GLY AAA O   1 
ATOM   6053  N N   . SER D 1 159 ? -6.619  24.100  127.723 1.000 82.787  ? 477 SER AAA N   1 
ATOM   6054  C CA  . SER D 1 159 ? -7.811  23.208  127.648 1.000 80.249  ? 477 SER AAA CA  1 
ATOM   6055  C C   . SER D 1 159 ? -9.072  24.004  127.996 1.000 80.005  ? 477 SER AAA C   1 
ATOM   6056  O O   . SER D 1 159 ? -10.037 23.983  127.216 1.000 80.882  ? 477 SER AAA O   1 
ATOM   6057  C CB  . SER D 1 159 ? -7.711  22.016  128.585 1.000 81.146  ? 477 SER AAA CB  1 
ATOM   6058  O OG  . SER D 1 159 ? -6.370  21.630  128.846 1.000 88.276  ? 477 SER AAA OG  1 
ATOM   6059  N N   . THR D 1 160 ? -9.055  24.648  129.163 1.000 80.208  ? 478 THR AAA N   1 
ATOM   6060  C CA  . THR D 1 160 ? -10.226 25.316  129.783 1.000 83.421  ? 478 THR AAA CA  1 
ATOM   6061  C C   . THR D 1 160 ? -10.519 26.599  129.007 1.000 78.162  ? 478 THR AAA C   1 
ATOM   6062  O O   . THR D 1 160 ? -9.592  27.323  128.662 1.000 82.120  ? 478 THR AAA O   1 
ATOM   6063  C CB  . THR D 1 160 ? -9.965  25.503  131.284 1.000 81.479  ? 478 THR AAA CB  1 
ATOM   6064  O OG1 . THR D 1 160 ? -8.821  26.347  131.368 1.000 77.119  ? 478 THR AAA OG1 1 
ATOM   6065  C CG2 . THR D 1 160 ? -9.694  24.206  132.025 1.000 76.499  ? 478 THR AAA CG2 1 
ATOM   6066  N N   . PRO D 1 161 ? -11.789 26.883  128.637 1.000 77.769  ? 479 PRO AAA N   1 
ATOM   6067  C CA  . PRO D 1 161 ? -12.128 28.104  127.912 1.000 78.193  ? 479 PRO AAA CA  1 
ATOM   6068  C C   . PRO D 1 161 ? -12.123 29.294  128.866 1.000 76.245  ? 479 PRO AAA C   1 
ATOM   6069  O O   . PRO D 1 161 ? -12.567 29.136  129.971 1.000 83.162  ? 479 PRO AAA O   1 
ATOM   6070  C CB  . PRO D 1 161 ? -13.543 27.899  127.340 1.000 78.403  ? 479 PRO AAA CB  1 
ATOM   6071  C CG  . PRO D 1 161 ? -13.982 26.508  127.813 1.000 80.912  ? 479 PRO AAA CG  1 
ATOM   6072  C CD  . PRO D 1 161 ? -12.977 26.044  128.855 1.000 79.717  ? 479 PRO AAA CD  1 
ATOM   6073  N N   . CYS D 1 162 ? -11.590 30.427  128.422 1.000 81.815  ? 480 CYS AAA N   1 
ATOM   6074  C CA  . CYS D 1 162 ? -11.775 31.740  129.098 1.000 85.804  ? 480 CYS AAA CA  1 
ATOM   6075  C C   . CYS D 1 162 ? -13.162 32.233  128.716 1.000 82.105  ? 480 CYS AAA C   1 
ATOM   6076  O O   . CYS D 1 162 ? -13.545 32.036  127.551 1.000 79.674  ? 480 CYS AAA O   1 
ATOM   6077  C CB  . CYS D 1 162 ? -10.746 32.786  128.688 1.000 92.677  ? 480 CYS AAA CB  1 
ATOM   6078  S SG  . CYS D 1 162 ? -9.358  32.107  127.740 1.000 103.818 ? 480 CYS AAA SG  1 
ATOM   6079  N N   . ASN D 1 163 ? -13.894 32.805  129.665 1.000 78.312  ? 481 ASN AAA N   1 
ATOM   6080  C CA  . ASN D 1 163 ? -15.216 33.414  129.385 1.000 80.616  ? 481 ASN AAA CA  1 
ATOM   6081  C C   . ASN D 1 163 ? -14.996 34.925  129.364 1.000 76.155  ? 481 ASN AAA C   1 
ATOM   6082  O O   . ASN D 1 163 ? -15.676 35.630  130.117 1.000 82.907  ? 481 ASN AAA O   1 
ATOM   6083  C CB  . ASN D 1 163 ? -16.282 32.893  130.358 1.000 81.775  ? 481 ASN AAA CB  1 
ATOM   6084  C CG  . ASN D 1 163 ? -16.638 31.443  130.095 1.000 83.745  ? 481 ASN AAA CG  1 
ATOM   6085  O OD1 . ASN D 1 163 ? -17.238 31.122  129.076 1.000 95.424  ? 481 ASN AAA OD1 1 
ATOM   6086  N ND2 . ASN D 1 163 ? -16.258 30.548  130.988 1.000 90.231  ? 481 ASN AAA ND2 1 
ATOM   6087  N N   . GLY D 1 164 ? -14.057 35.389  128.536 1.000 66.427  ? 482 GLY AAA N   1 
ATOM   6088  C CA  . GLY D 1 164 ? -13.629 36.799  128.511 1.000 63.487  ? 482 GLY AAA CA  1 
ATOM   6089  C C   . GLY D 1 164 ? -12.876 37.152  129.780 1.000 65.924  ? 482 GLY AAA C   1 
ATOM   6090  O O   . GLY D 1 164 ? -12.754 38.354  130.076 1.000 60.963  ? 482 GLY AAA O   1 
ATOM   6091  N N   . VAL D 1 165 ? -12.358 36.143  130.486 1.000 71.561  ? 483 VAL AAA N   1 
ATOM   6092  C CA  . VAL D 1 165 ? -11.607 36.309  131.764 1.000 81.383  ? 483 VAL AAA CA  1 
ATOM   6093  C C   . VAL D 1 165 ? -10.124 36.040  131.466 1.000 84.043  ? 483 VAL AAA C   1 
ATOM   6094  O O   . VAL D 1 165 ? -9.833  34.983  130.865 1.000 102.365 ? 483 VAL AAA O   1 
ATOM   6095  C CB  . VAL D 1 165 ? -12.207 35.383  132.848 1.000 93.848  ? 483 VAL AAA CB  1 
ATOM   6096  C CG1 . VAL D 1 165 ? -11.301 34.210  133.238 1.000 104.415 ? 483 VAL AAA CG1 1 
ATOM   6097  C CG2 . VAL D 1 165 ? -12.629 36.181  134.075 1.000 91.458  ? 483 VAL AAA CG2 1 
ATOM   6098  N N   . GLU D 1 166 ? -9.219  36.941  131.869 1.000 77.787  ? 484 GLU AAA N   1 
ATOM   6099  C CA  . GLU D 1 166 ? -7.750  36.794  131.662 1.000 86.108  ? 484 GLU AAA CA  1 
ATOM   6100  C C   . GLU D 1 166 ? -7.106  36.040  132.851 1.000 88.730  ? 484 GLU AAA C   1 
ATOM   6101  O O   . GLU D 1 166 ? -7.485  36.323  133.993 1.000 85.713  ? 484 GLU AAA O   1 
ATOM   6102  C CB  . GLU D 1 166 ? -7.137  38.177  131.419 1.000 90.901  ? 484 GLU AAA CB  1 
ATOM   6103  C CG  . GLU D 1 166 ? -5.666  38.105  131.023 1.000 111.608 ? 484 GLU AAA CG  1 
ATOM   6104  C CD  . GLU D 1 166 ? -4.982  39.424  130.686 1.000 113.605 ? 484 GLU AAA CD  1 
ATOM   6105  O OE1 . GLU D 1 166 ? -3.864  39.380  130.073 1.000 112.809 ? 484 GLU AAA OE1 1 
ATOM   6106  O OE2 . GLU D 1 166 ? -5.571  40.488  131.010 1.000 93.566  ? 484 GLU AAA OE2 1 
ATOM   6107  N N   . GLY D 1 167 ? -6.169  35.109  132.597 1.000 88.318  ? 485 GLY AAA N   1 
ATOM   6108  C CA  . GLY D 1 167 ? -5.437  34.345  133.631 1.000 82.230  ? 485 GLY AAA CA  1 
ATOM   6109  C C   . GLY D 1 167 ? -4.528  33.272  133.051 1.000 83.639  ? 485 GLY AAA C   1 
ATOM   6110  O O   . GLY D 1 167 ? -4.050  33.452  131.923 1.000 85.340  ? 485 GLY AAA O   1 
ATOM   6111  N N   . PHE D 1 168 ? -4.266  32.202  133.812 1.000 92.326  ? 486 PHE AAA N   1 
ATOM   6112  C CA  . PHE D 1 168 ? -3.461  31.014  133.399 1.000 101.710 ? 486 PHE AAA CA  1 
ATOM   6113  C C   . PHE D 1 168 ? -3.951  30.571  132.013 1.000 95.350  ? 486 PHE AAA C   1 
ATOM   6114  O O   . PHE D 1 168 ? -5.167  30.305  131.890 1.000 89.267  ? 486 PHE AAA O   1 
ATOM   6115  C CB  . PHE D 1 168 ? -3.551  29.923  134.482 1.000 106.630 ? 486 PHE AAA CB  1 
ATOM   6116  C CG  . PHE D 1 168 ? -3.063  28.531  134.130 1.000 115.493 ? 486 PHE AAA CG  1 
ATOM   6117  C CD1 . PHE D 1 168 ? -1.712  28.266  133.922 1.000 118.832 ? 486 PHE AAA CD1 1 
ATOM   6118  C CD2 . PHE D 1 168 ? -3.950  27.458  134.071 1.000 110.031 ? 486 PHE AAA CD2 1 
ATOM   6119  C CE1 . PHE D 1 168 ? -1.272  26.978  133.629 1.000 114.516 ? 486 PHE AAA CE1 1 
ATOM   6120  C CE2 . PHE D 1 168 ? -3.510  26.173  133.777 1.000 107.654 ? 486 PHE AAA CE2 1 
ATOM   6121  C CZ  . PHE D 1 168 ? -2.171  25.935  133.558 1.000 111.425 ? 486 PHE AAA CZ  1 
ATOM   6122  N N   . ASN D 1 169 ? -3.062  30.555  131.004 1.000 86.455  ? 487 ASN AAA N   1 
ATOM   6123  C CA  . ASN D 1 169 ? -3.331  30.060  129.620 1.000 87.549  ? 487 ASN AAA CA  1 
ATOM   6124  C C   . ASN D 1 169 ? -4.487  30.837  128.957 1.000 83.931  ? 487 ASN AAA C   1 
ATOM   6125  O O   . ASN D 1 169 ? -5.171  30.272  128.081 1.000 86.732  ? 487 ASN AAA O   1 
ATOM   6126  C CB  . ASN D 1 169 ? -3.609  28.553  129.605 1.000 91.208  ? 487 ASN AAA CB  1 
ATOM   6127  C CG  . ASN D 1 169 ? -2.375  27.698  129.798 1.000 93.199  ? 487 ASN AAA CG  1 
ATOM   6128  O OD1 . ASN D 1 169 ? -2.446  26.635  130.411 1.000 103.240 ? 487 ASN AAA OD1 1 
ATOM   6129  N ND2 . ASN D 1 169 ? -1.246  28.134  129.264 1.000 89.782  ? 487 ASN AAA ND2 1 
ATOM   6130  N N   . CYS D 1 170 ? -4.688  32.099  129.331 1.000 76.631  ? 488 CYS AAA N   1 
ATOM   6131  C CA  . CYS D 1 170 ? -5.757  32.978  128.782 1.000 70.093  ? 488 CYS AAA CA  1 
ATOM   6132  C C   . CYS D 1 170 ? -5.274  34.428  128.757 1.000 59.016  ? 488 CYS AAA C   1 
ATOM   6133  O O   . CYS D 1 170 ? -5.376  35.098  129.791 1.000 58.109  ? 488 CYS AAA O   1 
ATOM   6134  C CB  . CYS D 1 170 ? -7.031  32.860  129.608 1.000 73.845  ? 488 CYS AAA CB  1 
ATOM   6135  S SG  . CYS D 1 170 ? -7.996  31.413  129.131 1.000 91.346  ? 488 CYS AAA SG  1 
ATOM   6136  N N   . TYR D 1 171 ? -4.768  34.892  127.619 1.000 51.888  ? 489 TYR AAA N   1 
ATOM   6137  C CA  . TYR D 1 171 ? -4.044  36.184  127.538 1.000 50.874  ? 489 TYR AAA CA  1 
ATOM   6138  C C   . TYR D 1 171 ? -4.832  37.175  126.682 1.000 45.877  ? 489 TYR AAA C   1 
ATOM   6139  O O   . TYR D 1 171 ? -5.484  36.752  125.694 1.000 43.011  ? 489 TYR AAA O   1 
ATOM   6140  C CB  . TYR D 1 171 ? -2.633  35.974  126.988 1.000 50.830  ? 489 TYR AAA CB  1 
ATOM   6141  C CG  . TYR D 1 171 ? -1.865  34.848  127.632 1.000 50.949  ? 489 TYR AAA CG  1 
ATOM   6142  C CD1 . TYR D 1 171 ? -1.296  35.001  128.886 1.000 54.851  ? 489 TYR AAA CD1 1 
ATOM   6143  C CD2 . TYR D 1 171 ? -1.705  33.626  127.003 1.000 52.220  ? 489 TYR AAA CD2 1 
ATOM   6144  C CE1 . TYR D 1 171 ? -0.586  33.977  129.497 1.000 51.257  ? 489 TYR AAA CE1 1 
ATOM   6145  C CE2 . TYR D 1 171 ? -0.996  32.592  127.597 1.000 52.482  ? 489 TYR AAA CE2 1 
ATOM   6146  C CZ  . TYR D 1 171 ? -0.445  32.769  128.852 1.000 48.952  ? 489 TYR AAA CZ  1 
ATOM   6147  O OH  . TYR D 1 171 ? 0.265   31.786  129.453 1.000 56.542  ? 489 TYR AAA OH  1 
ATOM   6148  N N   . PHE D 1 172 ? -4.766  38.451  127.070 1.000 44.261  ? 490 PHE AAA N   1 
ATOM   6149  C CA  . PHE D 1 172 ? -5.120  39.621  126.227 1.000 44.570  ? 490 PHE AAA CA  1 
ATOM   6150  C C   . PHE D 1 172 ? -4.215  39.579  125.009 1.000 46.596  ? 490 PHE AAA C   1 
ATOM   6151  O O   . PHE D 1 172 ? -3.002  39.477  125.159 1.000 53.524  ? 490 PHE AAA O   1 
ATOM   6152  C CB  . PHE D 1 172 ? -4.932  40.929  126.993 1.000 45.790  ? 490 PHE AAA CB  1 
ATOM   6153  C CG  . PHE D 1 172 ? -5.433  42.177  126.309 1.000 48.190  ? 490 PHE AAA CG  1 
ATOM   6154  C CD1 . PHE D 1 172 ? -6.777  42.517  126.329 1.000 50.974  ? 490 PHE AAA CD1 1 
ATOM   6155  C CD2 . PHE D 1 172 ? -4.550  43.058  125.707 1.000 55.490  ? 490 PHE AAA CD2 1 
ATOM   6156  C CE1 . PHE D 1 172 ? -7.234  43.691  125.748 1.000 50.955  ? 490 PHE AAA CE1 1 
ATOM   6157  C CE2 . PHE D 1 172 ? -5.007  44.221  125.103 1.000 56.823  ? 490 PHE AAA CE2 1 
ATOM   6158  C CZ  . PHE D 1 172 ? -6.348  44.539  125.130 1.000 54.636  ? 490 PHE AAA CZ  1 
ATOM   6159  N N   . PRO D 1 173 ? -4.759  39.635  123.777 1.000 47.438  ? 491 PRO AAA N   1 
ATOM   6160  C CA  . PRO D 1 173 ? -4.012  39.231  122.593 1.000 48.508  ? 491 PRO AAA CA  1 
ATOM   6161  C C   . PRO D 1 173 ? -3.000  40.279  122.102 1.000 48.750  ? 491 PRO AAA C   1 
ATOM   6162  O O   . PRO D 1 173 ? -2.211  39.922  121.252 1.000 59.869  ? 491 PRO AAA O   1 
ATOM   6163  C CB  . PRO D 1 173 ? -5.140  39.007  121.569 1.000 47.666  ? 491 PRO AAA CB  1 
ATOM   6164  C CG  . PRO D 1 173 ? -6.146  40.059  121.931 1.000 47.824  ? 491 PRO AAA CG  1 
ATOM   6165  C CD  . PRO D 1 173 ? -6.099  40.126  123.441 1.000 49.142  ? 491 PRO AAA CD  1 
ATOM   6166  N N   . LEU D 1 174 ? -3.036  41.511  122.619 1.000 41.267  ? 492 LEU AAA N   1 
ATOM   6167  C CA  . LEU D 1 174 ? -2.105  42.591  122.203 1.000 40.090  ? 492 LEU AAA CA  1 
ATOM   6168  C C   . LEU D 1 174 ? -1.038  42.828  123.273 1.000 45.179  ? 492 LEU AAA C   1 
ATOM   6169  O O   . LEU D 1 174 ? -1.395  43.064  124.426 1.000 50.922  ? 492 LEU AAA O   1 
ATOM   6170  C CB  . LEU D 1 174 ? -2.876  43.888  121.954 1.000 38.201  ? 492 LEU AAA CB  1 
ATOM   6171  C CG  . LEU D 1 174 ? -4.055  43.788  120.998 1.000 37.390  ? 492 LEU AAA CG  1 
ATOM   6172  C CD1 . LEU D 1 174 ? -4.590  45.175  120.709 1.000 35.836  ? 492 LEU AAA CD1 1 
ATOM   6173  C CD2 . LEU D 1 174 ? -3.664  43.065  119.714 1.000 39.343  ? 492 LEU AAA CD2 1 
ATOM   6174  N N   . GLN D 1 175 ? 0.228   42.830  122.852 1.000 52.651  ? 493 GLN AAA N   1 
ATOM   6175  C CA  . GLN D 1 175 ? 1.419   43.245  123.635 1.000 52.720  ? 493 GLN AAA CA  1 
ATOM   6176  C C   . GLN D 1 175 ? 1.865   44.606  123.111 1.000 49.572  ? 493 GLN AAA C   1 
ATOM   6177  O O   . GLN D 1 175 ? 1.591   44.910  121.931 1.000 47.487  ? 493 GLN AAA O   1 
ATOM   6178  C CB  . GLN D 1 175 ? 2.544   42.233  123.442 1.000 60.144  ? 493 GLN AAA CB  1 
ATOM   6179  C CG  . GLN D 1 175 ? 2.674   41.201  124.554 1.000 64.367  ? 493 GLN AAA CG  1 
ATOM   6180  C CD  . GLN D 1 175 ? 3.963   41.396  125.306 1.000 64.410  ? 493 GLN AAA CD  1 
ATOM   6181  O OE1 . GLN D 1 175 ? 4.235   42.507  125.741 1.000 71.277  ? 493 GLN AAA OE1 1 
ATOM   6182  N NE2 . GLN D 1 175 ? 4.768   40.348  125.424 1.000 60.565  ? 493 GLN AAA NE2 1 
ATOM   6183  N N   . SER D 1 176 ? 2.544   45.376  123.947 1.000 52.381  ? 494 SER AAA N   1 
ATOM   6184  C CA  . SER D 1 176 ? 3.060   46.717  123.596 1.000 55.430  ? 494 SER AAA CA  1 
ATOM   6185  C C   . SER D 1 176 ? 4.554   46.639  123.218 1.000 54.598  ? 494 SER AAA C   1 
ATOM   6186  O O   . SER D 1 176 ? 5.281   45.851  123.839 1.000 54.736  ? 494 SER AAA O   1 
ATOM   6187  C CB  . SER D 1 176 ? 2.809   47.659  124.740 1.000 59.240  ? 494 SER AAA CB  1 
ATOM   6188  O OG  . SER D 1 176 ? 3.391   48.923  124.471 1.000 67.929  ? 494 SER AAA OG  1 
ATOM   6189  N N   . TYR D 1 177 ? 4.991   47.411  122.216 1.000 53.231  ? 495 TYR AAA N   1 
ATOM   6190  C CA  . TYR D 1 177 ? 6.424   47.683  121.938 1.000 53.067  ? 495 TYR AAA CA  1 
ATOM   6191  C C   . TYR D 1 177 ? 6.967   48.601  123.038 1.000 59.779  ? 495 TYR AAA C   1 
ATOM   6192  O O   . TYR D 1 177 ? 6.282   49.625  123.329 1.000 64.236  ? 495 TYR AAA O   1 
ATOM   6193  C CB  . TYR D 1 177 ? 6.629   48.359  120.579 1.000 49.359  ? 495 TYR AAA CB  1 
ATOM   6194  C CG  . TYR D 1 177 ? 6.496   47.446  119.391 1.000 44.661  ? 495 TYR AAA CG  1 
ATOM   6195  C CD1 . TYR D 1 177 ? 7.267   46.301  119.285 1.000 45.690  ? 495 TYR AAA CD1 1 
ATOM   6196  C CD2 . TYR D 1 177 ? 5.595   47.718  118.378 1.000 42.144  ? 495 TYR AAA CD2 1 
ATOM   6197  C CE1 . TYR D 1 177 ? 7.141   45.440  118.206 1.000 43.553  ? 495 TYR AAA CE1 1 
ATOM   6198  C CE2 . TYR D 1 177 ? 5.456   46.873  117.290 1.000 40.438  ? 495 TYR AAA CE2 1 
ATOM   6199  C CZ  . TYR D 1 177 ? 6.241   45.738  117.203 1.000 42.789  ? 495 TYR AAA CZ  1 
ATOM   6200  O OH  . TYR D 1 177 ? 6.140   44.893  116.147 1.000 42.359  ? 495 TYR AAA OH  1 
ATOM   6201  N N   . GLY D 1 178 ? 8.146   48.252  123.581 1.000 60.527  ? 496 GLY AAA N   1 
ATOM   6202  C CA  . GLY D 1 178 ? 8.845   49.003  124.637 1.000 62.073  ? 496 GLY AAA CA  1 
ATOM   6203  C C   . GLY D 1 178 ? 9.875   49.970  124.086 1.000 60.338  ? 496 GLY AAA C   1 
ATOM   6204  O O   . GLY D 1 178 ? 11.048  49.804  124.437 1.000 72.313  ? 496 GLY AAA O   1 
ATOM   6205  N N   . PHE D 1 179 ? 9.454   50.964  123.302 1.000 52.122  ? 497 PHE AAA N   1 
ATOM   6206  C CA  . PHE D 1 179 ? 10.345  51.822  122.473 1.000 53.930  ? 497 PHE AAA CA  1 
ATOM   6207  C C   . PHE D 1 179 ? 11.032  52.886  123.339 1.000 58.143  ? 497 PHE AAA C   1 
ATOM   6208  O O   . PHE D 1 179 ? 10.497  54.016  123.480 1.000 53.170  ? 497 PHE AAA O   1 
ATOM   6209  C CB  . PHE D 1 179 ? 9.587   52.508  121.330 1.000 53.658  ? 497 PHE AAA CB  1 
ATOM   6210  C CG  . PHE D 1 179 ? 9.125   51.614  120.207 1.000 51.516  ? 497 PHE AAA CG  1 
ATOM   6211  C CD1 . PHE D 1 179 ? 9.924   50.586  119.746 1.000 51.756  ? 497 PHE AAA CD1 1 
ATOM   6212  C CD2 . PHE D 1 179 ? 7.913   51.838  119.572 1.000 51.346  ? 497 PHE AAA CD2 1 
ATOM   6213  C CE1 . PHE D 1 179 ? 9.509   49.785  118.696 1.000 53.533  ? 497 PHE AAA CE1 1 
ATOM   6214  C CE2 . PHE D 1 179 ? 7.495   51.027  118.530 1.000 50.008  ? 497 PHE AAA CE2 1 
ATOM   6215  C CZ  . PHE D 1 179 ? 8.298   50.008  118.087 1.000 49.860  ? 497 PHE AAA CZ  1 
ATOM   6216  N N   . GLN D 1 180 ? 12.229  52.550  123.837 1.000 67.641  ? 498 GLN AAA N   1 
ATOM   6217  C CA  . GLN D 1 180 ? 13.144  53.467  124.576 1.000 70.753  ? 498 GLN AAA CA  1 
ATOM   6218  C C   . GLN D 1 180 ? 14.220  53.970  123.615 1.000 73.435  ? 498 GLN AAA C   1 
ATOM   6219  O O   . GLN D 1 180 ? 14.650  53.227  122.723 1.000 75.631  ? 498 GLN AAA O   1 
ATOM   6220  C CB  . GLN D 1 180 ? 13.771  52.750  125.777 1.000 70.760  ? 498 GLN AAA CB  1 
ATOM   6221  C CG  . GLN D 1 180 ? 12.790  51.900  126.579 1.000 69.451  ? 498 GLN AAA CG  1 
ATOM   6222  C CD  . GLN D 1 180 ? 13.310  51.604  127.963 1.000 67.847  ? 498 GLN AAA CD  1 
ATOM   6223  O OE1 . GLN D 1 180 ? 13.413  52.489  128.808 1.000 76.532  ? 498 GLN AAA OE1 1 
ATOM   6224  N NE2 . GLN D 1 180 ? 13.641  50.351  128.208 1.000 65.765  ? 498 GLN AAA NE2 1 
ATOM   6225  N N   . PRO D 1 181 ? 14.672  55.243  123.756 1.000 71.017  ? 499 PRO AAA N   1 
ATOM   6226  C CA  . PRO D 1 181 ? 15.680  55.822  122.866 1.000 69.750  ? 499 PRO AAA CA  1 
ATOM   6227  C C   . PRO D 1 181 ? 17.017  55.066  122.871 1.000 68.492  ? 499 PRO AAA C   1 
ATOM   6228  O O   . PRO D 1 181 ? 17.678  55.051  121.869 1.000 70.648  ? 499 PRO AAA O   1 
ATOM   6229  C CB  . PRO D 1 181 ? 15.896  57.241  123.406 1.000 69.827  ? 499 PRO AAA CB  1 
ATOM   6230  C CG  . PRO D 1 181 ? 14.630  57.548  124.156 1.000 70.907  ? 499 PRO AAA CG  1 
ATOM   6231  C CD  . PRO D 1 181 ? 14.203  56.218  124.749 1.000 72.099  ? 499 PRO AAA CD  1 
ATOM   6232  N N   . THR D 1 182 ? 17.361  54.450  124.000 1.000 68.440  ? 500 THR AAA N   1 
ATOM   6233  C CA  . THR D 1 182 ? 18.659  53.776  124.249 1.000 68.907  ? 500 THR AAA CA  1 
ATOM   6234  C C   . THR D 1 182 ? 18.603  52.305  123.808 1.000 67.730  ? 500 THR AAA C   1 
ATOM   6235  O O   . THR D 1 182 ? 19.621  51.609  123.980 1.000 73.754  ? 500 THR AAA O   1 
ATOM   6236  C CB  . THR D 1 182 ? 19.021  53.904  125.732 1.000 76.301  ? 500 THR AAA CB  1 
ATOM   6237  O OG1 . THR D 1 182 ? 18.071  53.147  126.490 1.000 75.392  ? 500 THR AAA OG1 1 
ATOM   6238  C CG2 . THR D 1 182 ? 19.042  55.348  126.196 1.000 79.385  ? 500 THR AAA CG2 1 
ATOM   6239  N N   . ASN D 1 183 ? 17.466  51.831  123.288 1.000 68.830  ? 501 ASN AAA N   1 
ATOM   6240  C CA  . ASN D 1 183 ? 17.323  50.459  122.725 1.000 70.421  ? 501 ASN AAA CA  1 
ATOM   6241  C C   . ASN D 1 183 ? 18.271  50.319  121.532 1.000 65.756  ? 501 ASN AAA C   1 
ATOM   6242  O O   . ASN D 1 183 ? 18.500  51.340  120.862 1.000 61.855  ? 501 ASN AAA O   1 
ATOM   6243  C CB  . ASN D 1 183 ? 15.904  50.150  122.226 1.000 76.820  ? 501 ASN AAA CB  1 
ATOM   6244  C CG  . ASN D 1 183 ? 14.857  50.056  123.314 1.000 72.877  ? 501 ASN AAA CG  1 
ATOM   6245  O OD1 . ASN D 1 183 ? 13.727  50.490  123.112 1.000 74.421  ? 501 ASN AAA OD1 1 
ATOM   6246  N ND2 . ASN D 1 183 ? 15.213  49.477  124.449 1.000 60.247  ? 501 ASN AAA ND2 1 
ATOM   6247  N N   . GLY D 1 184 ? 18.756  49.104  121.256 1.000 64.428  ? 502 GLY AAA N   1 
ATOM   6248  C CA  . GLY D 1 184 ? 19.551  48.786  120.052 1.000 66.142  ? 502 GLY AAA CA  1 
ATOM   6249  C C   . GLY D 1 184 ? 18.704  48.916  118.799 1.000 67.791  ? 502 GLY AAA C   1 
ATOM   6250  O O   . GLY D 1 184 ? 17.498  48.643  118.893 1.000 78.816  ? 502 GLY AAA O   1 
ATOM   6251  N N   . VAL D 1 185 ? 19.283  49.348  117.670 1.000 73.455  ? 503 VAL AAA N   1 
ATOM   6252  C CA  . VAL D 1 185 ? 18.574  49.355  116.355 1.000 77.191  ? 503 VAL AAA CA  1 
ATOM   6253  C C   . VAL D 1 185 ? 17.965  47.962  116.226 1.000 83.755  ? 503 VAL AAA C   1 
ATOM   6254  O O   . VAL D 1 185 ? 18.660  46.977  116.579 1.000 98.947  ? 503 VAL AAA O   1 
ATOM   6255  C CB  . VAL D 1 185 ? 19.492  49.689  115.161 1.000 77.947  ? 503 VAL AAA CB  1 
ATOM   6256  C CG1 . VAL D 1 185 ? 18.921  49.205  113.834 1.000 77.652  ? 503 VAL AAA CG1 1 
ATOM   6257  C CG2 . VAL D 1 185 ? 19.793  51.177  115.087 1.000 82.296  ? 503 VAL AAA CG2 1 
ATOM   6258  N N   . GLY D 1 186 ? 16.714  47.872  115.798 1.000 79.139  ? 504 GLY AAA N   1 
ATOM   6259  C CA  . GLY D 1 186 ? 16.049  46.564  115.685 1.000 77.472  ? 504 GLY AAA CA  1 
ATOM   6260  C C   . GLY D 1 186 ? 15.066  46.338  116.814 1.000 68.419  ? 504 GLY AAA C   1 
ATOM   6261  O O   . GLY D 1 186 ? 14.080  45.629  116.578 1.000 70.016  ? 504 GLY AAA O   1 
ATOM   6262  N N   . TYR D 1 187 ? 15.328  46.920  117.983 1.000 59.836  ? 505 TYR AAA N   1 
ATOM   6263  C CA  . TYR D 1 187 ? 14.299  47.154  119.019 1.000 59.776  ? 505 TYR AAA CA  1 
ATOM   6264  C C   . TYR D 1 187 ? 13.814  48.599  118.922 1.000 52.463  ? 505 TYR AAA C   1 
ATOM   6265  O O   . TYR D 1 187 ? 12.851  48.929  119.602 1.000 63.826  ? 505 TYR AAA O   1 
ATOM   6266  C CB  . TYR D 1 187 ? 14.822  46.775  120.404 1.000 66.952  ? 505 TYR AAA CB  1 
ATOM   6267  C CG  . TYR D 1 187 ? 14.501  45.353  120.804 1.000 74.342  ? 505 TYR AAA CG  1 
ATOM   6268  C CD1 . TYR D 1 187 ? 15.472  44.364  120.796 1.000 75.264  ? 505 TYR AAA CD1 1 
ATOM   6269  C CD2 . TYR D 1 187 ? 13.218  44.991  121.193 1.000 79.263  ? 505 TYR AAA CD2 1 
ATOM   6270  C CE1 . TYR D 1 187 ? 15.182  43.057  121.168 1.000 78.593  ? 505 TYR AAA CE1 1 
ATOM   6271  C CE2 . TYR D 1 187 ? 12.912  43.689  121.564 1.000 86.047  ? 505 TYR AAA CE2 1 
ATOM   6272  C CZ  . TYR D 1 187 ? 13.895  42.711  121.551 1.000 83.934  ? 505 TYR AAA CZ  1 
ATOM   6273  O OH  . TYR D 1 187 ? 13.577  41.422  121.901 1.000 72.495  ? 505 TYR AAA OH  1 
ATOM   6274  N N   . GLN D 1 188 ? 14.405  49.430  118.074 1.000 46.237  ? 506 GLN AAA N   1 
ATOM   6275  C CA  . GLN D 1 188 ? 13.908  50.818  117.912 1.000 53.239  ? 506 GLN AAA CA  1 
ATOM   6276  C C   . GLN D 1 188 ? 12.769  50.806  116.909 1.000 53.576  ? 506 GLN AAA C   1 
ATOM   6277  O O   . GLN D 1 188 ? 12.680  49.902  116.088 1.000 53.277  ? 506 GLN AAA O   1 
ATOM   6278  C CB  . GLN D 1 188 ? 14.980  51.774  117.408 1.000 60.473  ? 506 GLN AAA CB  1 
ATOM   6279  C CG  . GLN D 1 188 ? 16.350  51.444  117.947 1.000 64.941  ? 506 GLN AAA CG  1 
ATOM   6280  C CD  . GLN D 1 188 ? 17.347  52.550  117.725 1.000 60.507  ? 506 GLN AAA CD  1 
ATOM   6281  O OE1 . GLN D 1 188 ? 17.047  53.611  117.182 1.000 55.613  ? 506 GLN AAA OE1 1 
ATOM   6282  N NE2 . GLN D 1 188 ? 18.563  52.287  118.155 1.000 56.795  ? 506 GLN AAA NE2 1 
ATOM   6283  N N   . PRO D 1 189 ? 11.878  51.817  116.949 1.000 53.461  ? 507 PRO AAA N   1 
ATOM   6284  C CA  . PRO D 1 189 ? 10.757  51.883  116.018 1.000 53.409  ? 507 PRO AAA CA  1 
ATOM   6285  C C   . PRO D 1 189 ? 11.156  52.304  114.601 1.000 54.783  ? 507 PRO AAA C   1 
ATOM   6286  O O   . PRO D 1 189 ? 12.001  53.156  114.460 1.000 50.270  ? 507 PRO AAA O   1 
ATOM   6287  C CB  . PRO D 1 189 ? 9.864   52.962  116.644 1.000 55.633  ? 507 PRO AAA CB  1 
ATOM   6288  C CG  . PRO D 1 189 ? 10.830  53.874  117.357 1.000 53.072  ? 507 PRO AAA CG  1 
ATOM   6289  C CD  . PRO D 1 189 ? 11.893  52.941  117.899 1.000 52.795  ? 507 PRO AAA CD  1 
ATOM   6290  N N   . TYR D 1 190 ? 10.517  51.687  113.603 1.000 60.162  ? 508 TYR AAA N   1 
ATOM   6291  C CA  . TYR D 1 190 ? 10.585  52.057  112.165 1.000 60.766  ? 508 TYR AAA CA  1 
ATOM   6292  C C   . TYR D 1 190 ? 9.163   52.275  111.646 1.000 51.557  ? 508 TYR AAA C   1 
ATOM   6293  O O   . TYR D 1 190 ? 8.343   51.374  111.814 1.000 53.261  ? 508 TYR AAA O   1 
ATOM   6294  C CB  . TYR D 1 190 ? 11.261  50.953  111.341 1.000 66.178  ? 508 TYR AAA CB  1 
ATOM   6295  C CG  . TYR D 1 190 ? 12.756  50.859  111.493 1.000 72.053  ? 508 TYR AAA CG  1 
ATOM   6296  C CD1 . TYR D 1 190 ? 13.329  50.460  112.690 1.000 75.109  ? 508 TYR AAA CD1 1 
ATOM   6297  C CD2 . TYR D 1 190 ? 13.601  51.161  110.436 1.000 75.178  ? 508 TYR AAA CD2 1 
ATOM   6298  C CE1 . TYR D 1 190 ? 14.705  50.378  112.839 1.000 74.802  ? 508 TYR AAA CE1 1 
ATOM   6299  C CE2 . TYR D 1 190 ? 14.977  51.067  110.565 1.000 75.573  ? 508 TYR AAA CE2 1 
ATOM   6300  C CZ  . TYR D 1 190 ? 15.528  50.672  111.771 1.000 73.413  ? 508 TYR AAA CZ  1 
ATOM   6301  O OH  . TYR D 1 190 ? 16.875  50.564  111.926 1.000 72.715  ? 508 TYR AAA OH  1 
ATOM   6302  N N   . ARG D 1 191 ? 8.894   53.423  111.034 1.000 43.331  ? 509 ARG AAA N   1 
ATOM   6303  C CA  . ARG D 1 191 ? 7.633   53.686  110.304 1.000 41.781  ? 509 ARG AAA CA  1 
ATOM   6304  C C   . ARG D 1 191 ? 7.701   53.043  108.924 1.000 42.308  ? 509 ARG AAA C   1 
ATOM   6305  O O   . ARG D 1 191 ? 8.678   53.276  108.207 1.000 54.555  ? 509 ARG AAA O   1 
ATOM   6306  C CB  . ARG D 1 191 ? 7.400   55.183  110.147 1.000 41.880  ? 509 ARG AAA CB  1 
ATOM   6307  C CG  . ARG D 1 191 ? 7.234   55.877  111.480 1.000 46.309  ? 509 ARG AAA CG  1 
ATOM   6308  C CD  . ARG D 1 191 ? 6.823   57.320  111.349 1.000 50.819  ? 509 ARG AAA CD  1 
ATOM   6309  N NE  . ARG D 1 191 ? 6.477   57.805  112.671 1.000 51.959  ? 509 ARG AAA NE  1 
ATOM   6310  C CZ  . ARG D 1 191 ? 5.801   58.915  112.914 1.000 57.432  ? 509 ARG AAA CZ  1 
ATOM   6311  N NH1 . ARG D 1 191 ? 5.384   59.682  111.920 1.000 58.616  ? 509 ARG AAA NH1 1 
ATOM   6312  N NH2 . ARG D 1 191 ? 5.534   59.257  114.161 1.000 61.315  ? 509 ARG AAA NH2 1 
ATOM   6313  N N   . VAL D 1 192 ? 6.653   52.329  108.541 1.000 41.292  ? 510 VAL AAA N   1 
ATOM   6314  C CA  . VAL D 1 192 ? 6.548   51.635  107.232 1.000 42.307  ? 510 VAL AAA CA  1 
ATOM   6315  C C   . VAL D 1 192 ? 5.371   52.211  106.448 1.000 41.884  ? 510 VAL AAA C   1 
ATOM   6316  O O   . VAL D 1 192 ? 4.359   52.539  107.056 1.000 44.152  ? 510 VAL AAA O   1 
ATOM   6317  C CB  . VAL D 1 192 ? 6.379   50.134  107.466 1.000 46.971  ? 510 VAL AAA CB  1 
ATOM   6318  C CG1 . VAL D 1 192 ? 6.334   49.359  106.158 1.000 49.293  ? 510 VAL AAA CG1 1 
ATOM   6319  C CG2 . VAL D 1 192 ? 7.473   49.608  108.388 1.000 49.529  ? 510 VAL AAA CG2 1 
ATOM   6320  N N   . VAL D 1 193 ? 5.532   52.345  105.139 1.000 41.994  ? 511 VAL AAA N   1 
ATOM   6321  C CA  . VAL D 1 193 ? 4.423   52.614  104.185 1.000 43.036  ? 511 VAL AAA CA  1 
ATOM   6322  C C   . VAL D 1 193 ? 4.481   51.541  103.107 1.000 50.498  ? 511 VAL AAA C   1 
ATOM   6323  O O   . VAL D 1 193 ? 5.562   51.383  102.518 1.000 63.151  ? 511 VAL AAA O   1 
ATOM   6324  C CB  . VAL D 1 193 ? 4.523   54.005  103.559 1.000 38.370  ? 511 VAL AAA CB  1 
ATOM   6325  C CG1 . VAL D 1 193 ? 3.460   54.206  102.491 1.000 38.725  ? 511 VAL AAA CG1 1 
ATOM   6326  C CG2 . VAL D 1 193 ? 4.442   55.080  104.619 1.000 38.537  ? 511 VAL AAA CG2 1 
ATOM   6327  N N   . VAL D 1 194 ? 3.361   50.862  102.853 1.000 53.077  ? 512 VAL AAA N   1 
ATOM   6328  C CA  . VAL D 1 194 ? 3.252   49.848  101.772 1.000 52.403  ? 512 VAL AAA CA  1 
ATOM   6329  C C   . VAL D 1 194 ? 2.304   50.389  100.703 1.000 58.351  ? 512 VAL AAA C   1 
ATOM   6330  O O   . VAL D 1 194 ? 1.069   50.395  100.937 1.000 66.856  ? 512 VAL AAA O   1 
ATOM   6331  C CB  . VAL D 1 194 ? 2.813   48.477  102.302 1.000 50.805  ? 512 VAL AAA CB  1 
ATOM   6332  C CG1 . VAL D 1 194 ? 2.846   47.431  101.205 1.000 53.428  ? 512 VAL AAA CG1 1 
ATOM   6333  C CG2 . VAL D 1 194 ? 3.676   48.031  103.467 1.000 48.835  ? 512 VAL AAA CG2 1 
ATOM   6334  N N   . LEU D 1 195 ? 2.893   50.838  99.587  1.000 60.823  ? 513 LEU AAA N   1 
ATOM   6335  C CA  . LEU D 1 195 ? 2.192   51.121  98.310  1.000 61.649  ? 513 LEU AAA CA  1 
ATOM   6336  C C   . LEU D 1 195 ? 1.826   49.778  97.672  1.000 62.903  ? 513 LEU AAA C   1 
ATOM   6337  O O   . LEU D 1 195 ? 2.719   48.948  97.543  1.000 57.708  ? 513 LEU AAA O   1 
ATOM   6338  C CB  . LEU D 1 195 ? 3.098   51.949  97.392  1.000 59.905  ? 513 LEU AAA CB  1 
ATOM   6339  C CG  . LEU D 1 195 ? 3.655   53.227  98.015  1.000 60.943  ? 513 LEU AAA CG  1 
ATOM   6340  C CD1 . LEU D 1 195 ? 4.551   53.950  97.025  1.000 62.971  ? 513 LEU AAA CD1 1 
ATOM   6341  C CD2 . LEU D 1 195 ? 2.542   54.140  98.516  1.000 59.083  ? 513 LEU AAA CD2 1 
ATOM   6342  N N   . SER D 1 196 ? 0.547   49.568  97.350  1.000 65.033  ? 514 SER AAA N   1 
ATOM   6343  C CA  . SER D 1 196 ? 0.040   48.442  96.524  1.000 60.595  ? 514 SER AAA CA  1 
ATOM   6344  C C   . SER D 1 196 ? -0.727  49.018  95.328  1.000 55.371  ? 514 SER AAA C   1 
ATOM   6345  O O   . SER D 1 196 ? -1.358  50.083  95.479  1.000 46.296  ? 514 SER AAA O   1 
ATOM   6346  C CB  . SER D 1 196 ? -0.796  47.490  97.350  1.000 64.096  ? 514 SER AAA CB  1 
ATOM   6347  O OG  . SER D 1 196 ? -1.745  48.195  98.143  1.000 67.777  ? 514 SER AAA OG  1 
ATOM   6348  N N   . PHE D 1 197 ? -0.640  48.339  94.183  1.000 57.409  ? 515 PHE AAA N   1 
ATOM   6349  C CA  . PHE D 1 197 ? -1.188  48.782  92.875  1.000 65.675  ? 515 PHE AAA CA  1 
ATOM   6350  C C   . PHE D 1 197 ? -2.060  47.675  92.278  1.000 66.446  ? 515 PHE AAA C   1 
ATOM   6351  O O   . PHE D 1 197 ? -1.601  46.518  92.196  1.000 57.831  ? 515 PHE AAA O   1 
ATOM   6352  C CB  . PHE D 1 197 ? -0.062  49.119  91.888  1.000 72.720  ? 515 PHE AAA CB  1 
ATOM   6353  C CG  . PHE D 1 197 ? 0.951   50.118  92.385  1.000 70.094  ? 515 PHE AAA CG  1 
ATOM   6354  C CD1 . PHE D 1 197 ? 0.812   51.475  92.110  1.000 67.900  ? 515 PHE AAA CD1 1 
ATOM   6355  C CD2 . PHE D 1 197 ? 2.029   49.698  93.151  1.000 67.907  ? 515 PHE AAA CD2 1 
ATOM   6356  C CE1 . PHE D 1 197 ? 1.739   52.390  92.579  1.000 67.397  ? 515 PHE AAA CE1 1 
ATOM   6357  C CE2 . PHE D 1 197 ? 2.959   50.614  93.619  1.000 67.314  ? 515 PHE AAA CE2 1 
ATOM   6358  C CZ  . PHE D 1 197 ? 2.802   51.958  93.344  1.000 70.841  ? 515 PHE AAA CZ  1 
ATOM   6359  N N   . GLU D 1 198 ? -3.270  48.032  91.842  1.000 75.778  ? 516 GLU AAA N   1 
ATOM   6360  C CA  . GLU D 1 198 ? -4.173  47.134  91.075  1.000 87.128  ? 516 GLU AAA CA  1 
ATOM   6361  C C   . GLU D 1 198 ? -4.546  47.845  89.770  1.000 83.877  ? 516 GLU AAA C   1 
ATOM   6362  O O   . GLU D 1 198 ? -4.660  49.082  89.767  1.000 69.127  ? 516 GLU AAA O   1 
ATOM   6363  C CB  . GLU D 1 198 ? -5.402  46.727  91.903  1.000 98.470  ? 516 GLU AAA CB  1 
ATOM   6364  C CG  . GLU D 1 198 ? -6.269  47.901  92.335  1.000 108.045 ? 516 GLU AAA CG  1 
ATOM   6365  C CD  . GLU D 1 198 ? -7.457  47.578  93.233  1.000 104.823 ? 516 GLU AAA CD  1 
ATOM   6366  O OE1 . GLU D 1 198 ? -7.397  46.563  93.967  1.000 90.753  ? 516 GLU AAA OE1 1 
ATOM   6367  O OE2 . GLU D 1 198 ? -8.439  48.361  93.198  1.000 100.304 ? 516 GLU AAA OE2 1 
ATOM   6368  N N   . LEU D 1 199 ? -4.713  47.064  88.704  1.000 95.304  ? 517 LEU AAA N   1 
ATOM   6369  C CA  . LEU D 1 199 ? -5.241  47.488  87.383  1.000 106.738 ? 517 LEU AAA CA  1 
ATOM   6370  C C   . LEU D 1 199 ? -6.374  46.515  87.014  1.000 116.491 ? 517 LEU AAA C   1 
ATOM   6371  O O   . LEU D 1 199 ? -6.091  45.335  86.693  1.000 119.629 ? 517 LEU AAA O   1 
ATOM   6372  C CB  . LEU D 1 199 ? -4.079  47.458  86.382  1.000 105.767 ? 517 LEU AAA CB  1 
ATOM   6373  C CG  . LEU D 1 199 ? -4.229  48.265  85.093  1.000 99.190  ? 517 LEU AAA CG  1 
ATOM   6374  C CD1 . LEU D 1 199 ? -2.861  48.599  84.526  1.000 95.350  ? 517 LEU AAA CD1 1 
ATOM   6375  C CD2 . LEU D 1 199 ? -5.058  47.518  84.056  1.000 103.298 ? 517 LEU AAA CD2 1 
ATOM   6376  N N   . LEU D 1 200 ? -7.618  46.980  87.129  1.000 124.478 ? 518 LEU AAA N   1 
ATOM   6377  C CA  . LEU D 1 200 ? -8.841  46.238  86.717  1.000 135.251 ? 518 LEU AAA CA  1 
ATOM   6378  C C   . LEU D 1 200 ? -9.226  46.737  85.319  1.000 136.006 ? 518 LEU AAA C   1 
ATOM   6379  O O   . LEU D 1 200 ? -8.556  47.679  84.831  1.000 143.099 ? 518 LEU AAA O   1 
ATOM   6380  C CB  . LEU D 1 200 ? -9.957  46.476  87.745  1.000 139.077 ? 518 LEU AAA CB  1 
ATOM   6381  C CG  . LEU D 1 200 ? -9.534  46.428  89.218  1.000 127.863 ? 518 LEU AAA CG  1 
ATOM   6382  C CD1 . LEU D 1 200 ? -10.648 46.952  90.117  1.000 117.003 ? 518 LEU AAA CD1 1 
ATOM   6383  C CD2 . LEU D 1 200 ? -9.104  45.022  89.634  1.000 114.545 ? 518 LEU AAA CD2 1 
ATOM   6384  N N   . HIS D 1 201 ? -10.243 46.140  84.688  1.000 132.516 ? 519 HIS AAA N   1 
ATOM   6385  C CA  . HIS D 1 201 ? -10.854 46.661  83.435  1.000 132.366 ? 519 HIS AAA CA  1 
ATOM   6386  C C   . HIS D 1 201 ? -11.934 47.685  83.825  1.000 118.391 ? 519 HIS AAA C   1 
ATOM   6387  O O   . HIS D 1 201 ? -13.089 47.514  83.416  1.000 127.807 ? 519 HIS AAA O   1 
ATOM   6388  C CB  . HIS D 1 201 ? -11.305 45.498  82.524  1.000 136.499 ? 519 HIS AAA CB  1 
ATOM   6389  C CG  . HIS D 1 201 ? -10.182 44.673  81.969  1.000 138.068 ? 519 HIS AAA CG  1 
ATOM   6390  N ND1 . HIS D 1 201 ? -9.496  45.024  80.815  1.000 135.216 ? 519 HIS AAA ND1 1 
ATOM   6391  C CD2 . HIS D 1 201 ? -9.629  43.511  82.386  1.000 134.956 ? 519 HIS AAA CD2 1 
ATOM   6392  C CE1 . HIS D 1 201 ? -8.567  44.123  80.558  1.000 127.313 ? 519 HIS AAA CE1 1 
ATOM   6393  N NE2 . HIS D 1 201 ? -8.628  43.186  81.505  1.000 129.901 ? 519 HIS AAA NE2 1 
ATOM   6394  N N   . ALA D 1 202 ? -11.536 48.712  84.594  1.000 103.142 ? 520 ALA AAA N   1 
ATOM   6395  C CA  . ALA D 1 202 ? -12.335 49.896  84.996  1.000 101.009 ? 520 ALA AAA CA  1 
ATOM   6396  C C   . ALA D 1 202 ? -11.516 51.154  84.690  1.000 101.352 ? 520 ALA AAA C   1 
ATOM   6397  O O   . ALA D 1 202 ? -10.337 51.046  84.351  1.000 93.697  ? 520 ALA AAA O   1 
ATOM   6398  C CB  . ALA D 1 202 ? -12.706 49.777  86.456  1.000 88.008  ? 520 ALA AAA CB  1 
ATOM   6399  N N   . PRO D 1 203 ? -12.090 52.379  84.770  1.000 96.086  ? 521 PRO AAA N   1 
ATOM   6400  C CA  . PRO D 1 203 ? -11.312 53.604  84.545  1.000 96.322  ? 521 PRO AAA CA  1 
ATOM   6401  C C   . PRO D 1 203 ? -10.098 53.730  85.485  1.000 102.313 ? 521 PRO AAA C   1 
ATOM   6402  O O   . PRO D 1 203 ? -10.210 53.320  86.626  1.000 130.251 ? 521 PRO AAA O   1 
ATOM   6403  C CB  . PRO D 1 203 ? -12.309 54.741  84.836  1.000 94.221  ? 521 PRO AAA CB  1 
ATOM   6404  C CG  . PRO D 1 203 ? -13.679 54.109  84.673  1.000 91.378  ? 521 PRO AAA CG  1 
ATOM   6405  C CD  . PRO D 1 203 ? -13.506 52.655  85.063  1.000 90.372  ? 521 PRO AAA CD  1 
ATOM   6406  N N   . ALA D 1 204 ? -8.973  54.265  84.999  1.000 95.881  ? 522 ALA AAA N   1 
ATOM   6407  C CA  . ALA D 1 204 ? -7.736  54.527  85.784  1.000 85.424  ? 522 ALA AAA CA  1 
ATOM   6408  C C   . ALA D 1 204 ? -7.696  56.009  86.178  1.000 86.805  ? 522 ALA AAA C   1 
ATOM   6409  O O   . ALA D 1 204 ? -7.925  56.843  85.296  1.000 86.161  ? 522 ALA AAA O   1 
ATOM   6410  C CB  . ALA D 1 204 ? -6.524  54.131  84.975  1.000 78.741  ? 522 ALA AAA CB  1 
ATOM   6411  N N   . THR D 1 205 ? -7.426  56.334  87.446  1.000 95.549  ? 523 THR AAA N   1 
ATOM   6412  C CA  . THR D 1 205 ? -7.540  57.723  87.990  1.000 105.925 ? 523 THR AAA CA  1 
ATOM   6413  C C   . THR D 1 205 ? -6.243  58.180  88.680  1.000 108.601 ? 523 THR AAA C   1 
ATOM   6414  O O   . THR D 1 205 ? -6.173  59.380  89.051  1.000 98.010  ? 523 THR AAA O   1 
ATOM   6415  C CB  . THR D 1 205 ? -8.739  57.839  88.946  1.000 109.933 ? 523 THR AAA CB  1 
ATOM   6416  O OG1 . THR D 1 205 ? -8.599  56.859  89.984  1.000 114.302 ? 523 THR AAA OG1 1 
ATOM   6417  C CG2 . THR D 1 205 ? -10.069 57.658  88.241  1.000 100.674 ? 523 THR AAA CG2 1 
ATOM   6418  N N   . VAL D 1 206 ? -5.270  57.277  88.870  1.000 122.843 ? 524 VAL AAA N   1 
ATOM   6419  C CA  . VAL D 1 206 ? -3.942  57.578  89.495  1.000 129.530 ? 524 VAL AAA CA  1 
ATOM   6420  C C   . VAL D 1 206 ? -2.856  57.400  88.431  1.000 135.201 ? 524 VAL AAA C   1 
ATOM   6421  O O   . VAL D 1 206 ? -2.557  56.241  88.077  1.000 132.283 ? 524 VAL AAA O   1 
ATOM   6422  C CB  . VAL D 1 206 ? -3.638  56.703  90.726  1.000 132.318 ? 524 VAL AAA CB  1 
ATOM   6423  C CG1 . VAL D 1 206 ? -2.371  57.163  91.428  1.000 133.050 ? 524 VAL AAA CG1 1 
ATOM   6424  C CG2 . VAL D 1 206 ? -4.792  56.671  91.705  1.000 139.984 ? 524 VAL AAA CG2 1 
ATOM   6425  N N   . CYS D 1 207 ? -2.286  58.520  87.974  1.000 130.722 ? 525 CYS AAA N   1 
ATOM   6426  C CA  . CYS D 1 207 ? -1.384  58.617  86.800  1.000 118.832 ? 525 CYS AAA CA  1 
ATOM   6427  C C   . CYS D 1 207 ? -0.144  59.429  87.167  1.000 114.815 ? 525 CYS AAA C   1 
ATOM   6428  O O   . CYS D 1 207 ? -0.240  60.271  88.069  1.000 100.181 ? 525 CYS AAA O   1 
ATOM   6429  C CB  . CYS D 1 207 ? -2.114  59.270  85.637  1.000 112.066 ? 525 CYS AAA CB  1 
ATOM   6430  S SG  . CYS D 1 207 ? -3.531  58.287  85.078  1.000 106.711 ? 525 CYS AAA SG  1 
ATOM   6431  N N   . GLY D 1 208 ? 0.970   59.161  86.486  1.000 114.076 ? 526 GLY AAA N   1 
ATOM   6432  C CA  . GLY D 1 208 ? 2.212   59.947  86.597  1.000 124.878 ? 526 GLY AAA CA  1 
ATOM   6433  C C   . GLY D 1 208 ? 2.128   61.231  85.775  1.000 129.088 ? 526 GLY AAA C   1 
ATOM   6434  O O   . GLY D 1 208 ? 1.219   61.364  84.954  1.000 129.887 ? 526 GLY AAA O   1 
ATOM   6435  N N   . PRO D 1 209 ? 3.044   62.213  85.984  1.000 129.712 ? 527 PRO AAA N   1 
ATOM   6436  C CA  . PRO D 1 209 ? 3.015   63.470  85.229  1.000 121.569 ? 527 PRO AAA CA  1 
ATOM   6437  C C   . PRO D 1 209 ? 3.118   63.239  83.710  1.000 116.534 ? 527 PRO AAA C   1 
ATOM   6438  O O   . PRO D 1 209 ? 2.467   63.976  82.977  1.000 100.105 ? 527 PRO AAA O   1 
ATOM   6439  C CB  . PRO D 1 209 ? 4.192   64.299  85.778  1.000 121.656 ? 527 PRO AAA CB  1 
ATOM   6440  C CG  . PRO D 1 209 ? 5.043   63.322  86.588  1.000 124.058 ? 527 PRO AAA CG  1 
ATOM   6441  C CD  . PRO D 1 209 ? 4.130   62.178  86.981  1.000 124.930 ? 527 PRO AAA CD  1 
ATOM   6442  N N   . LYS D 1 210 ? 3.893   62.229  83.284  1.000 118.593 ? 528 LYS AAA N   1 
ATOM   6443  C CA  . LYS D 1 210 ? 4.009   61.775  81.867  1.000 112.370 ? 528 LYS AAA CA  1 
ATOM   6444  C C   . LYS D 1 210 ? 2.805   60.883  81.534  1.000 108.762 ? 528 LYS AAA C   1 
ATOM   6445  O O   . LYS D 1 210 ? 2.008   61.102  80.626  1.000 106.353 ? 528 LYS AAA O   1 
ATOM   6446  C CB  . LYS D 1 210 ? 5.332   61.035  81.643  1.000 102.733 ? 528 LYS AAA CB  1 
ATOM   6447  N N   . GLN E 2 1   ? 17.538  59.016  86.178  1.000 86.055  ? 1   GLN BBB N   1 
ATOM   6448  C CA  . GLN E 2 1   ? 18.240  57.892  85.475  1.000 91.112  ? 1   GLN BBB CA  1 
ATOM   6449  C C   . GLN E 2 1   ? 19.540  57.599  86.223  1.000 79.453  ? 1   GLN BBB C   1 
ATOM   6450  O O   . GLN E 2 1   ? 20.069  58.565  86.780  1.000 88.674  ? 1   GLN BBB O   1 
ATOM   6451  C CB  . GLN E 2 1   ? 18.515  58.277  84.018  1.000 106.268 ? 1   GLN BBB CB  1 
ATOM   6452  C CG  . GLN E 2 1   ? 19.321  57.241  83.230  1.000 119.857 ? 1   GLN BBB CG  1 
ATOM   6453  C CD  . GLN E 2 1   ? 18.626  55.905  83.073  1.000 122.968 ? 1   GLN BBB CD  1 
ATOM   6454  O OE1 . GLN E 2 1   ? 17.404  55.822  83.031  1.000 127.163 ? 1   GLN BBB OE1 1 
ATOM   6455  N NE2 . GLN E 2 1   ? 19.401  54.838  82.956  1.000 118.671 ? 1   GLN BBB NE2 1 
ATOM   6456  N N   . MET E 2 2   ? 20.025  56.348  86.231  1.000 64.098  ? 2   MET BBB N   1 
ATOM   6457  C CA  . MET E 2 2   ? 21.334  55.970  86.851  1.000 63.518  ? 2   MET BBB CA  1 
ATOM   6458  C C   . MET E 2 2   ? 22.013  54.857  86.035  1.000 63.699  ? 2   MET BBB C   1 
ATOM   6459  O O   . MET E 2 2   ? 21.353  54.321  85.129  1.000 68.848  ? 2   MET BBB O   1 
ATOM   6460  C CB  . MET E 2 2   ? 21.149  55.508  88.302  1.000 58.417  ? 2   MET BBB CB  1 
ATOM   6461  C CG  . MET E 2 2   ? 20.470  54.193  88.446  1.000 55.599  ? 2   MET BBB CG  1 
ATOM   6462  S SD  . MET E 2 2   ? 21.649  52.842  88.550  1.000 54.998  ? 2   MET BBB SD  1 
ATOM   6463  C CE  . MET E 2 2   ? 22.581  53.333  89.992  1.000 55.526  ? 2   MET BBB CE  1 
ATOM   6464  N N   . GLN E 2 3   ? 23.267  54.511  86.375  1.000 59.412  ? 3   GLN BBB N   1 
ATOM   6465  C CA  . GLN E 2 3   ? 24.165  53.616  85.591  1.000 54.549  ? 3   GLN BBB CA  1 
ATOM   6466  C C   . GLN E 2 3   ? 25.059  52.783  86.523  1.000 46.772  ? 3   GLN BBB C   1 
ATOM   6467  O O   . GLN E 2 3   ? 25.264  53.173  87.665  1.000 40.934  ? 3   GLN BBB O   1 
ATOM   6468  C CB  . GLN E 2 3   ? 25.022  54.450  84.643  1.000 62.724  ? 3   GLN BBB CB  1 
ATOM   6469  C CG  . GLN E 2 3   ? 25.868  55.500  85.351  1.000 73.341  ? 3   GLN BBB CG  1 
ATOM   6470  C CD  . GLN E 2 3   ? 26.828  56.190  84.409  1.000 83.702  ? 3   GLN BBB CD  1 
ATOM   6471  O OE1 . GLN E 2 3   ? 26.602  56.256  83.201  1.000 87.540  ? 3   GLN BBB OE1 1 
ATOM   6472  N NE2 . GLN E 2 3   ? 27.905  56.732  84.965  1.000 97.577  ? 3   GLN BBB NE2 1 
ATOM   6473  N N   . LEU E 2 4   ? 25.561  51.653  86.028  1.000 46.399  ? 4   LEU BBB N   1 
ATOM   6474  C CA  . LEU E 2 4   ? 26.346  50.636  86.780  1.000 47.377  ? 4   LEU BBB CA  1 
ATOM   6475  C C   . LEU E 2 4   ? 27.724  50.464  86.126  1.000 49.119  ? 4   LEU BBB C   1 
ATOM   6476  O O   . LEU E 2 4   ? 27.811  50.410  84.892  1.000 56.888  ? 4   LEU BBB O   1 
ATOM   6477  C CB  . LEU E 2 4   ? 25.598  49.305  86.743  1.000 51.454  ? 4   LEU BBB CB  1 
ATOM   6478  C CG  . LEU E 2 4   ? 24.809  48.916  87.989  1.000 53.841  ? 4   LEU BBB CG  1 
ATOM   6479  C CD1 . LEU E 2 4   ? 23.809  50.003  88.383  1.000 53.003  ? 4   LEU BBB CD1 1 
ATOM   6480  C CD2 . LEU E 2 4   ? 24.087  47.601  87.731  1.000 56.034  ? 4   LEU BBB CD2 1 
ATOM   6481  N N   . VAL E 2 5   ? 28.788  50.364  86.916  1.000 45.744  ? 5   VAL BBB N   1 
ATOM   6482  C CA  . VAL E 2 5   ? 30.184  50.356  86.389  1.000 38.617  ? 5   VAL BBB CA  1 
ATOM   6483  C C   . VAL E 2 5   ? 30.934  49.213  87.047  1.000 35.482  ? 5   VAL BBB C   1 
ATOM   6484  O O   . VAL E 2 5   ? 30.953  49.166  88.285  1.000 38.037  ? 5   VAL BBB O   1 
ATOM   6485  C CB  . VAL E 2 5   ? 30.878  51.694  86.669  1.000 38.679  ? 5   VAL BBB CB  1 
ATOM   6486  C CG1 . VAL E 2 5   ? 32.383  51.516  86.746  1.000 40.229  ? 5   VAL BBB CG1 1 
ATOM   6487  C CG2 . VAL E 2 5   ? 30.476  52.756  85.654  1.000 39.925  ? 5   VAL BBB CG2 1 
ATOM   6488  N N   . GLN E 2 6   ? 31.494  48.312  86.250  1.000 33.360  ? 6   GLN BBB N   1 
ATOM   6489  C CA  . GLN E 2 6   ? 32.103  47.071  86.790  1.000 34.057  ? 6   GLN BBB CA  1 
ATOM   6490  C C   . GLN E 2 6   ? 33.618  47.230  86.888  1.000 31.867  ? 6   GLN BBB C   1 
ATOM   6491  O O   . GLN E 2 6   ? 34.174  48.147  86.243  1.000 26.013  ? 6   GLN BBB O   1 
ATOM   6492  C CB  . GLN E 2 6   ? 31.764  45.852  85.935  1.000 34.078  ? 6   GLN BBB CB  1 
ATOM   6493  C CG  . GLN E 2 6   ? 30.279  45.714  85.661  1.000 32.809  ? 6   GLN BBB CG  1 
ATOM   6494  C CD  . GLN E 2 6   ? 29.909  44.346  85.150  1.000 30.475  ? 6   GLN BBB CD  1 
ATOM   6495  O OE1 . GLN E 2 6   ? 29.072  44.240  84.247  1.000 28.784  ? 6   GLN BBB OE1 1 
ATOM   6496  N NE2 . GLN E 2 6   ? 30.540  43.316  85.712  1.000 25.342  ? 6   GLN BBB NE2 1 
ATOM   6497  N N   . SER E 2 7   ? 34.225  46.349  87.684  1.000 32.078  ? 7   SER BBB N   1 
ATOM   6498  C CA  . SER E 2 7   ? 35.687  46.178  87.786  1.000 34.770  ? 7   SER BBB CA  1 
ATOM   6499  C C   . SER E 2 7   ? 36.230  45.811  86.390  1.000 36.223  ? 7   SER BBB C   1 
ATOM   6500  O O   . SER E 2 7   ? 35.444  45.405  85.491  1.000 33.367  ? 7   SER BBB O   1 
ATOM   6501  C CB  . SER E 2 7   ? 36.045  45.162  88.873  1.000 36.396  ? 7   SER BBB CB  1 
ATOM   6502  O OG  . SER E 2 7   ? 36.020  43.817  88.391  1.000 38.201  ? 7   SER BBB OG  1 
ATOM   6503  N N   . GLY E 2 8   ? 37.529  46.012  86.194  1.000 37.697  ? 8   GLY BBB N   1 
ATOM   6504  C CA  . GLY E 2 8   ? 38.205  45.786  84.908  1.000 36.911  ? 8   GLY BBB CA  1 
ATOM   6505  C C   . GLY E 2 8   ? 38.503  44.317  84.733  1.000 36.127  ? 8   GLY BBB C   1 
ATOM   6506  O O   . GLY E 2 8   ? 38.167  43.509  85.681  1.000 34.335  ? 8   GLY BBB O   1 
ATOM   6507  N N   . THR E 2 9   ? 39.121  44.011  83.581  1.000 33.672  ? 9   THR BBB N   1 
ATOM   6508  C CA  . THR E 2 9   ? 39.404  42.636  83.090  1.000 35.055  ? 9   THR BBB CA  1 
ATOM   6509  C C   . THR E 2 9   ? 40.244  41.876  84.115  1.000 34.633  ? 9   THR BBB C   1 
ATOM   6510  O O   . THR E 2 9   ? 41.132  42.483  84.692  1.000 36.698  ? 9   THR BBB O   1 
ATOM   6511  C CB  . THR E 2 9   ? 40.129  42.671  81.746  1.000 34.497  ? 9   THR BBB CB  1 
ATOM   6512  O OG1 . THR E 2 9   ? 39.205  43.295  80.854  1.000 33.487  ? 9   THR BBB OG1 1 
ATOM   6513  C CG2 . THR E 2 9   ? 40.533  41.299  81.234  1.000 35.869  ? 9   THR BBB CG2 1 
ATOM   6514  N N   . GLU E 2 10  ? 39.963  40.595  84.314  1.000 35.653  ? 10  GLU BBB N   1 
ATOM   6515  C CA  . GLU E 2 10  ? 40.738  39.713  85.215  1.000 38.696  ? 10  GLU BBB CA  1 
ATOM   6516  C C   . GLU E 2 10  ? 41.291  38.564  84.383  1.000 38.242  ? 10  GLU BBB C   1 
ATOM   6517  O O   . GLU E 2 10  ? 40.643  38.177  83.374  1.000 38.271  ? 10  GLU BBB O   1 
ATOM   6518  C CB  . GLU E 2 10  ? 39.856  39.220  86.356  1.000 42.625  ? 10  GLU BBB CB  1 
ATOM   6519  C CG  . GLU E 2 10  ? 39.181  40.361  87.110  1.000 47.510  ? 10  GLU BBB CG  1 
ATOM   6520  C CD  . GLU E 2 10  ? 39.967  40.963  88.268  1.000 49.208  ? 10  GLU BBB CD  1 
ATOM   6521  O OE1 . GLU E 2 10  ? 41.019  40.375  88.661  1.000 43.653  ? 10  GLU BBB OE1 1 
ATOM   6522  O OE2 . GLU E 2 10  ? 39.493  41.994  88.808  1.000 50.819  ? 10  GLU BBB OE2 1 
ATOM   6523  N N   . VAL E 2 11  ? 42.476  38.097  84.766  1.000 36.391  ? 11  VAL BBB N   1 
ATOM   6524  C CA  . VAL E 2 11  ? 43.182  36.938  84.154  1.000 35.945  ? 11  VAL BBB CA  1 
ATOM   6525  C C   . VAL E 2 11  ? 43.865  36.181  85.287  1.000 38.056  ? 11  VAL BBB C   1 
ATOM   6526  O O   . VAL E 2 11  ? 44.816  36.722  85.858  1.000 45.522  ? 11  VAL BBB O   1 
ATOM   6527  C CB  . VAL E 2 11  ? 44.207  37.362  83.088  1.000 33.582  ? 11  VAL BBB CB  1 
ATOM   6528  C CG1 . VAL E 2 11  ? 45.000  36.164  82.595  1.000 34.154  ? 11  VAL BBB CG1 1 
ATOM   6529  C CG2 . VAL E 2 11  ? 43.565  38.087  81.918  1.000 33.330  ? 11  VAL BBB CG2 1 
ATOM   6530  N N   . LYS E 2 12  ? 43.370  34.989  85.607  1.000 39.098  ? 12  LYS BBB N   1 
ATOM   6531  C CA  . LYS E 2 12  ? 43.720  34.227  86.826  1.000 37.897  ? 12  LYS BBB CA  1 
ATOM   6532  C C   . LYS E 2 12  ? 44.115  32.811  86.426  1.000 39.579  ? 12  LYS BBB C   1 
ATOM   6533  O O   . LYS E 2 12  ? 43.794  32.392  85.318  1.000 35.851  ? 12  LYS BBB O   1 
ATOM   6534  C CB  . LYS E 2 12  ? 42.525  34.197  87.773  1.000 38.511  ? 12  LYS BBB CB  1 
ATOM   6535  C CG  . LYS E 2 12  ? 41.781  35.520  87.901  1.000 42.079  ? 12  LYS BBB CG  1 
ATOM   6536  C CD  . LYS E 2 12  ? 42.566  36.598  88.636  1.000 46.320  ? 12  LYS BBB CD  1 
ATOM   6537  C CE  . LYS E 2 12  ? 42.716  36.312  90.116  1.000 48.034  ? 12  LYS BBB CE  1 
ATOM   6538  N NZ  . LYS E 2 12  ? 43.306  37.459  90.828  1.000 48.398  ? 12  LYS BBB NZ  1 
ATOM   6539  N N   . LYS E 2 13  ? 44.815  32.129  87.321  1.000 45.401  ? 13  LYS BBB N   1 
ATOM   6540  C CA  . LYS E 2 13  ? 45.190  30.705  87.186  1.000 49.082  ? 13  LYS BBB CA  1 
ATOM   6541  C C   . LYS E 2 13  ? 44.145  29.884  87.925  1.000 48.700  ? 13  LYS BBB C   1 
ATOM   6542  O O   . LYS E 2 13  ? 43.518  30.353  88.876  1.000 45.178  ? 13  LYS BBB O   1 
ATOM   6543  C CB  . LYS E 2 13  ? 46.590  30.453  87.763  1.000 56.221  ? 13  LYS BBB CB  1 
ATOM   6544  C CG  . LYS E 2 13  ? 47.693  31.383  87.268  1.000 56.829  ? 13  LYS BBB CG  1 
ATOM   6545  C CD  . LYS E 2 13  ? 47.985  31.243  85.778  1.000 58.797  ? 13  LYS BBB CD  1 
ATOM   6546  C CE  . LYS E 2 13  ? 49.241  30.449  85.477  1.000 57.662  ? 13  LYS BBB CE  1 
ATOM   6547  N NZ  . LYS E 2 13  ? 50.433  31.315  85.476  1.000 57.664  ? 13  LYS BBB NZ  1 
ATOM   6548  N N   . PRO E 2 14  ? 43.932  28.622  87.511  1.000 51.247  ? 14  PRO BBB N   1 
ATOM   6549  C CA  . PRO E 2 14  ? 43.017  27.748  88.232  1.000 56.849  ? 14  PRO BBB CA  1 
ATOM   6550  C C   . PRO E 2 14  ? 43.457  27.687  89.703  1.000 55.933  ? 14  PRO BBB C   1 
ATOM   6551  O O   . PRO E 2 14  ? 44.628  27.546  89.955  1.000 51.307  ? 14  PRO BBB O   1 
ATOM   6552  C CB  . PRO E 2 14  ? 43.144  26.393  87.519  1.000 62.716  ? 14  PRO BBB CB  1 
ATOM   6553  C CG  . PRO E 2 14  ? 43.727  26.731  86.157  1.000 61.717  ? 14  PRO BBB CG  1 
ATOM   6554  C CD  . PRO E 2 14  ? 44.579  27.964  86.368  1.000 53.952  ? 14  PRO BBB CD  1 
ATOM   6555  N N   . GLY E 2 15  ? 42.506  27.844  90.623  1.000 57.367  ? 15  GLY BBB N   1 
ATOM   6556  C CA  . GLY E 2 15  ? 42.723  27.718  92.076  1.000 56.011  ? 15  GLY BBB CA  1 
ATOM   6557  C C   . GLY E 2 15  ? 42.771  29.070  92.768  1.000 54.273  ? 15  GLY BBB C   1 
ATOM   6558  O O   . GLY E 2 15  ? 42.679  29.090  94.009  1.000 56.786  ? 15  GLY BBB O   1 
ATOM   6559  N N   . GLU E 2 16  ? 42.926  30.155  92.008  1.000 49.890  ? 16  GLU BBB N   1 
ATOM   6560  C CA  . GLU E 2 16  ? 42.978  31.524  92.567  1.000 50.968  ? 16  GLU BBB CA  1 
ATOM   6561  C C   . GLU E 2 16  ? 41.563  31.910  92.999  1.000 48.671  ? 16  GLU BBB C   1 
ATOM   6562  O O   . GLU E 2 16  ? 40.621  31.531  92.311  1.000 52.320  ? 16  GLU BBB O   1 
ATOM   6563  C CB  . GLU E 2 16  ? 43.583  32.507  91.555  1.000 53.889  ? 16  GLU BBB CB  1 
ATOM   6564  C CG  . GLU E 2 16  ? 45.082  32.297  91.346  1.000 55.056  ? 16  GLU BBB CG  1 
ATOM   6565  C CD  . GLU E 2 16  ? 45.820  33.290  90.460  1.000 55.173  ? 16  GLU BBB CD  1 
ATOM   6566  O OE1 . GLU E 2 16  ? 45.287  34.384  90.185  1.000 56.962  ? 16  GLU BBB OE1 1 
ATOM   6567  O OE2 . GLU E 2 16  ? 46.939  32.961  90.055  1.000 54.346  ? 16  GLU BBB OE2 1 
ATOM   6568  N N   . SER E 2 17  ? 41.435  32.599  94.130  1.000 48.492  ? 17  SER BBB N   1 
ATOM   6569  C CA  . SER E 2 17  ? 40.202  33.304  94.551  1.000 47.889  ? 17  SER BBB CA  1 
ATOM   6570  C C   . SER E 2 17  ? 40.045  34.528  93.655  1.000 44.305  ? 17  SER BBB C   1 
ATOM   6571  O O   . SER E 2 17  ? 41.048  34.962  93.070  1.000 47.298  ? 17  SER BBB O   1 
ATOM   6572  C CB  . SER E 2 17  ? 40.267  33.690  95.994  1.000 51.076  ? 17  SER BBB CB  1 
ATOM   6573  O OG  . SER E 2 17  ? 41.381  34.535  96.223  1.000 59.006  ? 17  SER BBB OG  1 
ATOM   6574  N N   . LEU E 2 18  ? 38.834  35.046  93.526  1.000 42.277  ? 18  LEU BBB N   1 
ATOM   6575  C CA  . LEU E 2 18  ? 38.566  36.280  92.753  1.000 44.915  ? 18  LEU BBB CA  1 
ATOM   6576  C C   . LEU E 2 18  ? 37.275  36.903  93.283  1.000 44.880  ? 18  LEU BBB C   1 
ATOM   6577  O O   . LEU E 2 18  ? 36.374  36.148  93.672  1.000 48.964  ? 18  LEU BBB O   1 
ATOM   6578  C CB  . LEU E 2 18  ? 38.463  35.950  91.259  1.000 47.170  ? 18  LEU BBB CB  1 
ATOM   6579  C CG  . LEU E 2 18  ? 37.982  37.098  90.367  1.000 53.070  ? 18  LEU BBB CG  1 
ATOM   6580  C CD1 . LEU E 2 18  ? 38.888  38.318  90.487  1.000 58.932  ? 18  LEU BBB CD1 1 
ATOM   6581  C CD2 . LEU E 2 18  ? 37.885  36.660  88.915  1.000 53.193  ? 18  LEU BBB CD2 1 
ATOM   6582  N N   . LYS E 2 19  ? 37.222  38.233  93.319  1.000 41.909  ? 19  LYS BBB N   1 
ATOM   6583  C CA  . LYS E 2 19  ? 36.021  39.004  93.686  1.000 44.914  ? 19  LYS BBB CA  1 
ATOM   6584  C C   . LYS E 2 19  ? 35.945  40.189  92.730  1.000 47.960  ? 19  LYS BBB C   1 
ATOM   6585  O O   . LYS E 2 19  ? 36.761  41.095  92.887  1.000 51.360  ? 19  LYS BBB O   1 
ATOM   6586  C CB  . LYS E 2 19  ? 36.103  39.440  95.152  1.000 47.629  ? 19  LYS BBB CB  1 
ATOM   6587  C CG  . LYS E 2 19  ? 35.097  40.501  95.589  1.000 55.101  ? 19  LYS BBB CG  1 
ATOM   6588  C CD  . LYS E 2 19  ? 34.537  40.300  96.972  1.000 59.186  ? 19  LYS BBB CD  1 
ATOM   6589  C CE  . LYS E 2 19  ? 35.137  41.208  98.023  1.000 62.409  ? 19  LYS BBB CE  1 
ATOM   6590  N NZ  . LYS E 2 19  ? 34.574  40.898  99.356  1.000 69.041  ? 19  LYS BBB NZ  1 
ATOM   6591  N N   . ILE E 2 20  ? 35.002  40.171  91.784  1.000 49.735  ? 20  ILE BBB N   1 
ATOM   6592  C CA  . ILE E 2 20  ? 34.740  41.313  90.862  1.000 49.801  ? 20  ILE BBB CA  1 
ATOM   6593  C C   . ILE E 2 20  ? 33.637  42.167  91.470  1.000 46.270  ? 20  ILE BBB C   1 
ATOM   6594  O O   . ILE E 2 20  ? 32.924  41.664  92.361  1.000 50.530  ? 20  ILE BBB O   1 
ATOM   6595  C CB  . ILE E 2 20  ? 34.387  40.822  89.450  1.000 56.221  ? 20  ILE BBB CB  1 
ATOM   6596  C CG1 . ILE E 2 20  ? 32.922  40.423  89.314  1.000 59.004  ? 20  ILE BBB CG1 1 
ATOM   6597  C CG2 . ILE E 2 20  ? 35.302  39.673  89.037  1.000 59.524  ? 20  ILE BBB CG2 1 
ATOM   6598  C CD1 . ILE E 2 20  ? 32.555  40.060  87.905  1.000 64.434  ? 20  ILE BBB CD1 1 
ATOM   6599  N N   . SER E 2 21  ? 33.499  43.404  91.006  1.000 42.252  ? 21  SER BBB N   1 
ATOM   6600  C CA  . SER E 2 21  ? 32.578  44.386  91.616  1.000 42.487  ? 21  SER BBB CA  1 
ATOM   6601  C C   . SER E 2 21  ? 31.751  45.073  90.531  1.000 44.294  ? 21  SER BBB C   1 
ATOM   6602  O O   . SER E 2 21  ? 32.045  44.869  89.320  1.000 48.459  ? 21  SER BBB O   1 
ATOM   6603  C CB  . SER E 2 21  ? 33.339  45.380  92.456  1.000 45.665  ? 21  SER BBB CB  1 
ATOM   6604  O OG  . SER E 2 21  ? 34.189  46.166  91.633  1.000 51.156  ? 21  SER BBB OG  1 
ATOM   6605  N N   . CYS E 2 22  ? 30.748  45.822  91.002  1.000 45.197  ? 22  CYS BBB N   1 
ATOM   6606  C CA  . CYS E 2 22  ? 29.674  46.524  90.260  1.000 47.612  ? 22  CYS BBB CA  1 
ATOM   6607  C C   . CYS E 2 22  ? 29.132  47.614  91.181  1.000 46.517  ? 22  CYS BBB C   1 
ATOM   6608  O O   . CYS E 2 22  ? 28.457  47.282  92.167  1.000 44.899  ? 22  CYS BBB O   1 
ATOM   6609  C CB  . CYS E 2 22  ? 28.538  45.586  89.854  1.000 53.977  ? 22  CYS BBB CB  1 
ATOM   6610  S SG  . CYS E 2 22  ? 27.213  46.420  88.918  1.000 64.200  ? 22  CYS BBB SG  1 
ATOM   6611  N N   . LYS E 2 23  ? 29.459  48.863  90.875  1.000 49.677  ? 23  LYS BBB N   1 
ATOM   6612  C CA  . LYS E 2 23  ? 29.061  50.047  91.661  1.000 54.744  ? 23  LYS BBB CA  1 
ATOM   6613  C C   . LYS E 2 23  ? 28.071  50.852  90.824  1.000 54.116  ? 23  LYS BBB C   1 
ATOM   6614  O O   . LYS E 2 23  ? 28.302  51.001  89.612  1.000 55.830  ? 23  LYS BBB O   1 
ATOM   6615  C CB  . LYS E 2 23  ? 30.299  50.865  92.055  1.000 66.663  ? 23  LYS BBB CB  1 
ATOM   6616  C CG  . LYS E 2 23  ? 30.006  52.238  92.647  1.000 76.273  ? 23  LYS BBB CG  1 
ATOM   6617  C CD  . LYS E 2 23  ? 31.228  52.957  93.151  1.000 75.918  ? 23  LYS BBB CD  1 
ATOM   6618  C CE  . LYS E 2 23  ? 30.877  54.308  93.731  1.000 81.504  ? 23  LYS BBB CE  1 
ATOM   6619  N NZ  . LYS E 2 23  ? 31.895  54.735  94.716  1.000 85.072  ? 23  LYS BBB NZ  1 
ATOM   6620  N N   . GLY E 2 24  ? 27.017  51.352  91.467  1.000 52.476  ? 24  GLY BBB N   1 
ATOM   6621  C CA  . GLY E 2 24  ? 25.979  52.177  90.831  1.000 53.846  ? 24  GLY BBB CA  1 
ATOM   6622  C C   . GLY E 2 24  ? 26.091  53.616  91.267  1.000 52.536  ? 24  GLY BBB C   1 
ATOM   6623  O O   . GLY E 2 24  ? 26.278  53.844  92.450  1.000 47.715  ? 24  GLY BBB O   1 
ATOM   6624  N N   . SER E 2 25  ? 25.986  54.531  90.314  1.000 58.221  ? 25  SER BBB N   1 
ATOM   6625  C CA  . SER E 2 25  ? 26.020  55.994  90.513  1.000 67.833  ? 25  SER BBB CA  1 
ATOM   6626  C C   . SER E 2 25  ? 24.819  56.602  89.779  1.000 69.724  ? 25  SER BBB C   1 
ATOM   6627  O O   . SER E 2 25  ? 24.480  56.145  88.672  1.000 60.363  ? 25  SER BBB O   1 
ATOM   6628  C CB  . SER E 2 25  ? 27.348  56.581  90.052  1.000 77.587  ? 25  SER BBB CB  1 
ATOM   6629  O OG  . SER E 2 25  ? 27.555  56.387  88.653  1.000 87.819  ? 25  SER BBB OG  1 
ATOM   6630  N N   . GLY E 2 26  ? 24.192  57.598  90.400  1.000 81.708  ? 26  GLY BBB N   1 
ATOM   6631  C CA  . GLY E 2 26  ? 22.921  58.202  89.968  1.000 85.681  ? 26  GLY BBB CA  1 
ATOM   6632  C C   . GLY E 2 26  ? 21.907  58.127  91.091  1.000 94.767  ? 26  GLY BBB C   1 
ATOM   6633  O O   . GLY E 2 26  ? 21.987  57.189  91.926  1.000 88.840  ? 26  GLY BBB O   1 
ATOM   6634  N N   . TYR E 2 27  ? 20.996  59.091  91.146  1.000 112.218 ? 27  TYR BBB N   1 
ATOM   6635  C CA  . TYR E 2 27  ? 19.934  59.089  92.178  1.000 111.082 ? 27  TYR BBB CA  1 
ATOM   6636  C C   . TYR E 2 27  ? 18.883  58.070  91.754  1.000 89.838  ? 27  TYR BBB C   1 
ATOM   6637  O O   . TYR E 2 27  ? 18.763  57.736  90.558  1.000 73.083  ? 27  TYR BBB O   1 
ATOM   6638  C CB  . TYR E 2 27  ? 19.358  60.479  92.470  1.000 113.665 ? 27  TYR BBB CB  1 
ATOM   6639  C CG  . TYR E 2 27  ? 19.361  61.444  91.318  1.000 110.736 ? 27  TYR BBB CG  1 
ATOM   6640  C CD1 . TYR E 2 27  ? 18.581  61.218  90.193  1.000 104.516 ? 27  TYR BBB CD1 1 
ATOM   6641  C CD2 . TYR E 2 27  ? 20.154  62.585  91.363  1.000 106.225 ? 27  TYR BBB CD2 1 
ATOM   6642  C CE1 . TYR E 2 27  ? 18.577  62.122  89.142  1.000 104.317 ? 27  TYR BBB CE1 1 
ATOM   6643  C CE2 . TYR E 2 27  ? 20.168  63.492  90.318  1.000 103.130 ? 27  TYR BBB CE2 1 
ATOM   6644  C CZ  . TYR E 2 27  ? 19.371  63.261  89.209  1.000 107.069 ? 27  TYR BBB CZ  1 
ATOM   6645  O OH  . TYR E 2 27  ? 19.391  64.164  88.187  1.000 107.323 ? 27  TYR BBB OH  1 
ATOM   6646  N N   . GLY E 2 28  ? 18.178  57.589  92.769  1.000 77.711  ? 28  GLY BBB N   1 
ATOM   6647  C CA  . GLY E 2 28  ? 17.174  56.529  92.686  1.000 71.388  ? 28  GLY BBB CA  1 
ATOM   6648  C C   . GLY E 2 28  ? 17.806  55.198  92.992  1.000 64.901  ? 28  GLY BBB C   1 
ATOM   6649  O O   . GLY E 2 28  ? 17.359  54.217  92.404  1.000 67.490  ? 28  GLY BBB O   1 
ATOM   6650  N N   . PHE E 2 29  ? 18.817  55.141  93.861  1.000 62.627  ? 29  PHE BBB N   1 
ATOM   6651  C CA  . PHE E 2 29  ? 19.610  53.891  94.016  1.000 66.188  ? 29  PHE BBB CA  1 
ATOM   6652  C C   . PHE E 2 29  ? 19.043  52.961  95.095  1.000 65.613  ? 29  PHE BBB C   1 
ATOM   6653  O O   . PHE E 2 29  ? 19.207  51.735  94.922  1.000 61.094  ? 29  PHE BBB O   1 
ATOM   6654  C CB  . PHE E 2 29  ? 21.095  54.136  94.285  1.000 62.559  ? 29  PHE BBB CB  1 
ATOM   6655  C CG  . PHE E 2 29  ? 21.873  52.840  94.271  1.000 56.356  ? 29  PHE BBB CG  1 
ATOM   6656  C CD1 . PHE E 2 29  ? 22.137  52.175  93.082  1.000 50.422  ? 29  PHE BBB CD1 1 
ATOM   6657  C CD2 . PHE E 2 29  ? 22.281  52.244  95.457  1.000 55.243  ? 29  PHE BBB CD2 1 
ATOM   6658  C CE1 . PHE E 2 29  ? 22.814  50.960  93.082  1.000 49.858  ? 29  PHE BBB CE1 1 
ATOM   6659  C CE2 . PHE E 2 29  ? 22.958  51.029  95.451  1.000 51.160  ? 29  PHE BBB CE2 1 
ATOM   6660  C CZ  . PHE E 2 29  ? 23.221  50.388  94.265  1.000 48.217  ? 29  PHE BBB CZ  1 
ATOM   6661  N N   . ILE E 2 30  ? 18.439  53.505  96.158  1.000 70.215  ? 30  ILE BBB N   1 
ATOM   6662  C CA  . ILE E 2 30  ? 17.888  52.730  97.323  1.000 67.798  ? 30  ILE BBB CA  1 
ATOM   6663  C C   . ILE E 2 30  ? 17.018  51.583  96.792  1.000 64.459  ? 30  ILE BBB C   1 
ATOM   6664  O O   . ILE E 2 30  ? 16.977  50.518  97.433  1.000 58.102  ? 30  ILE BBB O   1 
ATOM   6665  C CB  . ILE E 2 30  ? 17.071  53.599  98.314  1.000 68.674  ? 30  ILE BBB CB  1 
ATOM   6666  C CG1 . ILE E 2 30  ? 17.769  54.914  98.703  1.000 84.042  ? 30  ILE BBB CG1 1 
ATOM   6667  C CG2 . ILE E 2 30  ? 16.726  52.742  99.525  1.000 58.956  ? 30  ILE BBB CG2 1 
ATOM   6668  C CD1 . ILE E 2 30  ? 16.997  55.830  99.659  1.000 78.446  ? 30  ILE BBB CD1 1 
ATOM   6669  N N   . THR E 2 31  ? 16.388  51.815  95.633  1.000 63.980  ? 31  THR BBB N   1 
ATOM   6670  C CA  . THR E 2 31  ? 15.326  50.987  94.995  1.000 55.331  ? 31  THR BBB CA  1 
ATOM   6671  C C   . THR E 2 31  ? 15.901  49.794  94.203  1.000 46.284  ? 31  THR BBB C   1 
ATOM   6672  O O   . THR E 2 31  ? 15.171  48.792  94.068  1.000 52.265  ? 31  THR BBB O   1 
ATOM   6673  C CB  . THR E 2 31  ? 14.433  51.875  94.110  1.000 52.789  ? 31  THR BBB CB  1 
ATOM   6674  O OG1 . THR E 2 31  ? 13.685  51.037  93.243  1.000 60.211  ? 31  THR BBB OG1 1 
ATOM   6675  C CG2 . THR E 2 31  ? 15.182  52.819  93.202  1.000 51.989  ? 31  THR BBB CG2 1 
ATOM   6676  N N   . TYR E 2 32  ? 17.137  49.875  93.703  1.000 40.685  ? 32  TYR BBB N   1 
ATOM   6677  C CA  . TYR E 2 32  ? 17.691  48.961  92.665  1.000 39.122  ? 32  TYR BBB CA  1 
ATOM   6678  C C   . TYR E 2 32  ? 18.126  47.627  93.268  1.000 37.044  ? 32  TYR BBB C   1 
ATOM   6679  O O   . TYR E 2 32  ? 18.844  47.594  94.259  1.000 36.038  ? 32  TYR BBB O   1 
ATOM   6680  C CB  . TYR E 2 32  ? 18.847  49.593  91.883  1.000 40.485  ? 32  TYR BBB CB  1 
ATOM   6681  C CG  . TYR E 2 32  ? 18.385  50.329  90.650  1.000 41.041  ? 32  TYR BBB CG  1 
ATOM   6682  C CD1 . TYR E 2 32  ? 18.121  49.647  89.468  1.000 43.550  ? 32  TYR BBB CD1 1 
ATOM   6683  C CD2 . TYR E 2 32  ? 18.138  51.697  90.685  1.000 39.605  ? 32  TYR BBB CD2 1 
ATOM   6684  C CE1 . TYR E 2 32  ? 17.639  50.315  88.352  1.000 44.909  ? 32  TYR BBB CE1 1 
ATOM   6685  C CE2 . TYR E 2 32  ? 17.678  52.384  89.574  1.000 39.064  ? 32  TYR BBB CE2 1 
ATOM   6686  C CZ  . TYR E 2 32  ? 17.417  51.688  88.408  1.000 43.327  ? 32  TYR BBB CZ  1 
ATOM   6687  O OH  . TYR E 2 32  ? 16.955  52.373  87.317  1.000 50.158  ? 32  TYR BBB OH  1 
ATOM   6688  N N   . TRP E 2 33  ? 17.653  46.551  92.654  1.000 39.426  ? 33  TRP BBB N   1 
ATOM   6689  C CA  . TRP E 2 33  ? 18.070  45.146  92.900  1.000 44.742  ? 33  TRP BBB CA  1 
ATOM   6690  C C   . TRP E 2 33  ? 19.089  44.746  91.835  1.000 47.690  ? 33  TRP BBB C   1 
ATOM   6691  O O   . TRP E 2 33  ? 18.746  44.814  90.634  1.000 47.262  ? 33  TRP BBB O   1 
ATOM   6692  C CB  . TRP E 2 33  ? 16.877  44.190  92.826  1.000 46.918  ? 33  TRP BBB CB  1 
ATOM   6693  C CG  . TRP E 2 33  ? 15.888  44.301  93.936  1.000 46.339  ? 33  TRP BBB CG  1 
ATOM   6694  C CD1 . TRP E 2 33  ? 15.036  45.342  94.188  1.000 48.060  ? 33  TRP BBB CD1 1 
ATOM   6695  C CD2 . TRP E 2 33  ? 15.616  43.287  94.911  1.000 42.533  ? 33  TRP BBB CD2 1 
ATOM   6696  N NE1 . TRP E 2 33  ? 14.281  45.060  95.294  1.000 46.985  ? 33  TRP BBB NE1 1 
ATOM   6697  C CE2 . TRP E 2 33  ? 14.611  43.801  95.749  1.000 44.127  ? 33  TRP BBB CE2 1 
ATOM   6698  C CE3 . TRP E 2 33  ? 16.127  42.008  95.153  1.000 43.065  ? 33  TRP BBB CE3 1 
ATOM   6699  C CZ2 . TRP E 2 33  ? 14.122  43.066  96.829  1.000 44.492  ? 33  TRP BBB CZ2 1 
ATOM   6700  C CZ3 . TRP E 2 33  ? 15.651  41.286  96.224  1.000 43.323  ? 33  TRP BBB CZ3 1 
ATOM   6701  C CH2 . TRP E 2 33  ? 14.645  41.807  97.035  1.000 46.520  ? 33  TRP BBB CH2 1 
ATOM   6702  N N   . ILE E 2 34  ? 20.259  44.270  92.258  1.000 49.945  ? 34  ILE BBB N   1 
ATOM   6703  C CA  . ILE E 2 34  ? 21.434  44.088  91.360  1.000 48.788  ? 34  ILE BBB CA  1 
ATOM   6704  C C   . ILE E 2 34  ? 21.737  42.605  91.171  1.000 46.607  ? 34  ILE BBB C   1 
ATOM   6705  O O   . ILE E 2 34  ? 22.076  41.929  92.144  1.000 46.096  ? 34  ILE BBB O   1 
ATOM   6706  C CB  . ILE E 2 34  ? 22.627  44.876  91.907  1.000 49.692  ? 34  ILE BBB CB  1 
ATOM   6707  C CG1 . ILE E 2 34  ? 22.378  46.372  91.698  1.000 51.956  ? 34  ILE BBB CG1 1 
ATOM   6708  C CG2 . ILE E 2 34  ? 23.911  44.416  91.256  1.000 50.131  ? 34  ILE BBB CG2 1 
ATOM   6709  C CD1 . ILE E 2 34  ? 23.205  47.255  92.569  1.000 56.504  ? 34  ILE BBB CD1 1 
ATOM   6710  N N   . GLY E 2 35  ? 21.623  42.138  89.932  1.000 48.951  ? 35  GLY BBB N   1 
ATOM   6711  C CA  . GLY E 2 35  ? 21.814  40.721  89.570  1.000 47.294  ? 35  GLY BBB CA  1 
ATOM   6712  C C   . GLY E 2 35  ? 23.068  40.517  88.753  1.000 44.224  ? 35  GLY BBB C   1 
ATOM   6713  O O   . GLY E 2 35  ? 23.599  41.479  88.208  1.000 50.300  ? 35  GLY BBB O   1 
ATOM   6714  N N   . TRP E 2 36  ? 23.505  39.278  88.664  1.000 41.949  ? 36  TRP BBB N   1 
ATOM   6715  C CA  . TRP E 2 36  ? 24.743  38.869  87.970  1.000 46.255  ? 36  TRP BBB CA  1 
ATOM   6716  C C   . TRP E 2 36  ? 24.350  37.895  86.868  1.000 45.984  ? 36  TRP BBB C   1 
ATOM   6717  O O   . TRP E 2 36  ? 23.617  36.960  87.159  1.000 47.189  ? 36  TRP BBB O   1 
ATOM   6718  C CB  . TRP E 2 36  ? 25.722  38.244  88.972  1.000 50.722  ? 36  TRP BBB CB  1 
ATOM   6719  C CG  . TRP E 2 36  ? 26.354  39.247  89.885  1.000 57.394  ? 36  TRP BBB CG  1 
ATOM   6720  C CD1 . TRP E 2 36  ? 26.045  39.516  91.185  1.000 59.522  ? 36  TRP BBB CD1 1 
ATOM   6721  C CD2 . TRP E 2 36  ? 27.415  40.143  89.534  1.000 67.023  ? 36  TRP BBB CD2 1 
ATOM   6722  N NE1 . TRP E 2 36  ? 26.845  40.517  91.667  1.000 63.895  ? 36  TRP BBB NE1 1 
ATOM   6723  C CE2 . TRP E 2 36  ? 27.703  40.913  90.678  1.000 70.348  ? 36  TRP BBB CE2 1 
ATOM   6724  C CE3 . TRP E 2 36  ? 28.141  40.360  88.360  1.000 70.119  ? 36  TRP BBB CE3 1 
ATOM   6725  C CZ2 . TRP E 2 36  ? 28.691  41.892  90.672  1.000 76.131  ? 36  TRP BBB CZ2 1 
ATOM   6726  C CZ3 . TRP E 2 36  ? 29.116  41.326  88.359  1.000 71.250  ? 36  TRP BBB CZ3 1 
ATOM   6727  C CH2 . TRP E 2 36  ? 29.389  42.076  89.501  1.000 72.462  ? 36  TRP BBB CH2 1 
ATOM   6728  N N   . VAL E 2 37  ? 24.786  38.148  85.646  1.000 44.233  ? 37  VAL BBB N   1 
ATOM   6729  C CA  . VAL E 2 37  ? 24.529  37.270  84.476  1.000 40.555  ? 37  VAL BBB CA  1 
ATOM   6730  C C   . VAL E 2 37  ? 25.880  36.800  83.945  1.000 42.657  ? 37  VAL BBB C   1 
ATOM   6731  O O   . VAL E 2 37  ? 26.793  37.621  83.830  1.000 44.363  ? 37  VAL BBB O   1 
ATOM   6732  C CB  . VAL E 2 37  ? 23.738  38.037  83.409  1.000 38.095  ? 37  VAL BBB CB  1 
ATOM   6733  C CG1 . VAL E 2 37  ? 23.516  37.200  82.163  1.000 36.925  ? 37  VAL BBB CG1 1 
ATOM   6734  C CG2 . VAL E 2 37  ? 22.437  38.574  83.983  1.000 39.605  ? 37  VAL BBB CG2 1 
ATOM   6735  N N   . ARG E 2 38  ? 26.001  35.524  83.610  1.000 45.942  ? 38  ARG BBB N   1 
ATOM   6736  C CA  . ARG E 2 38  ? 27.236  34.973  83.011  1.000 44.862  ? 38  ARG BBB CA  1 
ATOM   6737  C C   . ARG E 2 38  ? 27.002  34.706  81.525  1.000 46.289  ? 38  ARG BBB C   1 
ATOM   6738  O O   . ARG E 2 38  ? 25.946  34.143  81.176  1.000 52.274  ? 38  ARG BBB O   1 
ATOM   6739  C CB  . ARG E 2 38  ? 27.655  33.674  83.688  1.000 43.893  ? 38  ARG BBB CB  1 
ATOM   6740  C CG  . ARG E 2 38  ? 28.885  33.074  83.033  1.000 48.398  ? 38  ARG BBB CG  1 
ATOM   6741  C CD  . ARG E 2 38  ? 29.369  31.848  83.758  1.000 52.303  ? 38  ARG BBB CD  1 
ATOM   6742  N NE  . ARG E 2 38  ? 28.506  30.730  83.427  1.000 55.318  ? 38  ARG BBB NE  1 
ATOM   6743  C CZ  . ARG E 2 38  ? 28.630  29.526  83.962  1.000 56.506  ? 38  ARG BBB CZ  1 
ATOM   6744  N NH1 . ARG E 2 38  ? 29.583  29.290  84.852  1.000 58.965  ? 38  ARG BBB NH1 1 
ATOM   6745  N NH2 . ARG E 2 38  ? 27.813  28.560  83.593  1.000 56.355  ? 38  ARG BBB NH2 1 
ATOM   6746  N N   . GLN E 2 39  ? 27.967  35.088  80.690  1.000 43.408  ? 39  GLN BBB N   1 
ATOM   6747  C CA  . GLN E 2 39  ? 27.951  34.770  79.244  1.000 40.592  ? 39  GLN BBB CA  1 
ATOM   6748  C C   . GLN E 2 39  ? 29.282  34.136  78.866  1.000 40.635  ? 39  GLN BBB C   1 
ATOM   6749  O O   . GLN E 2 39  ? 30.291  34.862  78.763  1.000 41.384  ? 39  GLN BBB O   1 
ATOM   6750  C CB  . GLN E 2 39  ? 27.692  36.014  78.399  1.000 37.218  ? 39  GLN BBB CB  1 
ATOM   6751  C CG  . GLN E 2 39  ? 27.589  35.694  76.919  1.000 33.660  ? 39  GLN BBB CG  1 
ATOM   6752  C CD  . GLN E 2 39  ? 27.012  36.873  76.192  1.000 32.782  ? 39  GLN BBB CD  1 
ATOM   6753  O OE1 . GLN E 2 39  ? 26.079  36.717  75.402  1.000 30.978  ? 39  GLN BBB OE1 1 
ATOM   6754  N NE2 . GLN E 2 39  ? 27.570  38.048  76.480  1.000 31.055  ? 39  GLN BBB NE2 1 
ATOM   6755  N N   . MET E 2 40  ? 29.270  32.823  78.662  1.000 44.727  ? 40  MET BBB N   1 
ATOM   6756  C CA  . MET E 2 40  ? 30.490  32.082  78.278  1.000 45.621  ? 40  MET BBB CA  1 
ATOM   6757  C C   . MET E 2 40  ? 30.782  32.375  76.814  1.000 45.353  ? 40  MET BBB C   1 
ATOM   6758  O O   . MET E 2 40  ? 29.905  32.792  76.068  1.000 47.674  ? 40  MET BBB O   1 
ATOM   6759  C CB  . MET E 2 40  ? 30.311  30.588  78.520  1.000 48.156  ? 40  MET BBB CB  1 
ATOM   6760  C CG  . MET E 2 40  ? 30.238  30.272  79.993  1.000 53.214  ? 40  MET BBB CG  1 
ATOM   6761  S SD  . MET E 2 40  ? 30.177  28.486  80.323  1.000 61.448  ? 40  MET BBB SD  1 
ATOM   6762  C CE  . MET E 2 40  ? 30.892  28.407  81.959  1.000 62.778  ? 40  MET BBB CE  1 
ATOM   6763  N N   . PRO E 2 41  ? 32.042  32.222  76.380  1.000 44.654  ? 41  PRO BBB N   1 
ATOM   6764  C CA  . PRO E 2 41  ? 32.427  32.515  75.008  1.000 45.437  ? 41  PRO BBB CA  1 
ATOM   6765  C C   . PRO E 2 41  ? 31.570  31.740  74.002  1.000 51.233  ? 41  PRO BBB C   1 
ATOM   6766  O O   . PRO E 2 41  ? 31.610  30.490  74.009  1.000 53.093  ? 41  PRO BBB O   1 
ATOM   6767  C CB  . PRO E 2 41  ? 33.879  32.029  74.927  1.000 46.166  ? 41  PRO BBB CB  1 
ATOM   6768  C CG  . PRO E 2 41  ? 34.371  32.057  76.357  1.000 46.005  ? 41  PRO BBB CG  1 
ATOM   6769  C CD  . PRO E 2 41  ? 33.159  31.735  77.193  1.000 46.071  ? 41  PRO BBB CD  1 
ATOM   6770  N N   . GLY E 2 42  ? 30.820  32.487  73.186  1.000 55.304  ? 42  GLY BBB N   1 
ATOM   6771  C CA  . GLY E 2 42  ? 29.995  31.953  72.087  1.000 57.627  ? 42  GLY BBB CA  1 
ATOM   6772  C C   . GLY E 2 42  ? 28.634  31.498  72.569  1.000 57.477  ? 42  GLY BBB C   1 
ATOM   6773  O O   . GLY E 2 42  ? 27.852  31.066  71.730  1.000 67.814  ? 42  GLY BBB O   1 
ATOM   6774  N N   . LYS E 2 43  ? 28.353  31.595  73.869  1.000 55.335  ? 43  LYS BBB N   1 
ATOM   6775  C CA  . LYS E 2 43  ? 27.087  31.102  74.463  1.000 55.320  ? 43  LYS BBB CA  1 
ATOM   6776  C C   . LYS E 2 43  ? 26.156  32.284  74.711  1.000 53.435  ? 43  LYS BBB C   1 
ATOM   6777  O O   . LYS E 2 43  ? 26.577  33.443  74.529  1.000 52.183  ? 43  LYS BBB O   1 
ATOM   6778  C CB  . LYS E 2 43  ? 27.337  30.380  75.787  1.000 57.396  ? 43  LYS BBB CB  1 
ATOM   6779  C CG  . LYS E 2 43  ? 28.432  29.330  75.726  1.000 58.624  ? 43  LYS BBB CG  1 
ATOM   6780  C CD  . LYS E 2 43  ? 28.280  28.316  74.632  1.000 55.464  ? 43  LYS BBB CD  1 
ATOM   6781  C CE  . LYS E 2 43  ? 29.430  27.336  74.684  1.000 60.525  ? 43  LYS BBB CE  1 
ATOM   6782  N NZ  . LYS E 2 43  ? 29.017  25.958  74.336  1.000 67.469  ? 43  LYS BBB NZ  1 
ATOM   6783  N N   . GLY E 2 44  ? 24.935  31.975  75.129  1.000 50.244  ? 44  GLY BBB N   1 
ATOM   6784  C CA  . GLY E 2 44  ? 23.955  32.973  75.573  1.000 46.823  ? 44  GLY BBB CA  1 
ATOM   6785  C C   . GLY E 2 44  ? 24.132  33.302  77.041  1.000 47.245  ? 44  GLY BBB C   1 
ATOM   6786  O O   . GLY E 2 44  ? 25.133  32.835  77.685  1.000 43.854  ? 44  GLY BBB O   1 
ATOM   6787  N N   . LEU E 2 45  ? 23.149  34.053  77.541  1.000 51.069  ? 45  LEU BBB N   1 
ATOM   6788  C CA  . LEU E 2 45  ? 23.055  34.634  78.908  1.000 50.857  ? 45  LEU BBB CA  1 
ATOM   6789  C C   . LEU E 2 45  ? 22.549  33.561  79.876  1.000 50.617  ? 45  LEU BBB C   1 
ATOM   6790  O O   . LEU E 2 45  ? 21.727  32.726  79.456  1.000 54.059  ? 45  LEU BBB O   1 
ATOM   6791  C CB  . LEU E 2 45  ? 22.090  35.826  78.867  1.000 45.195  ? 45  LEU BBB CB  1 
ATOM   6792  C CG  . LEU E 2 45  ? 22.402  36.856  77.785  1.000 43.172  ? 45  LEU BBB CG  1 
ATOM   6793  C CD1 . LEU E 2 45  ? 21.331  37.933  77.725  1.000 40.615  ? 45  LEU BBB CD1 1 
ATOM   6794  C CD2 . LEU E 2 45  ? 23.794  37.454  78.005  1.000 44.856  ? 45  LEU BBB CD2 1 
ATOM   6795  N N   . GLU E 2 46  ? 23.056  33.591  81.108  1.000 47.314  ? 46  GLU BBB N   1 
ATOM   6796  C CA  . GLU E 2 46  ? 22.671  32.690  82.219  1.000 47.830  ? 46  GLU BBB CA  1 
ATOM   6797  C C   . GLU E 2 46  ? 22.538  33.566  83.466  1.000 49.197  ? 46  GLU BBB C   1 
ATOM   6798  O O   . GLU E 2 46  ? 23.544  34.153  83.857  1.000 51.176  ? 46  GLU BBB O   1 
ATOM   6799  C CB  . GLU E 2 46  ? 23.712  31.584  82.433  1.000 45.742  ? 46  GLU BBB CB  1 
ATOM   6800  C CG  . GLU E 2 46  ? 24.186  30.918  81.148  1.000 49.968  ? 46  GLU BBB CG  1 
ATOM   6801  C CD  . GLU E 2 46  ? 25.545  30.240  81.244  1.000 58.080  ? 46  GLU BBB CD  1 
ATOM   6802  O OE1 . GLU E 2 46  ? 25.710  29.455  82.209  1.000 52.356  ? 46  GLU BBB OE1 1 
ATOM   6803  O OE2 . GLU E 2 46  ? 26.444  30.512  80.356  1.000 64.096  ? 46  GLU BBB OE2 1 
ATOM   6804  N N   . TRP E 2 47  ? 21.340  33.696  84.039  1.000 48.516  ? 47  TRP BBB N   1 
ATOM   6805  C CA  . TRP E 2 47  ? 21.134  34.469  85.286  1.000 44.642  ? 47  TRP BBB CA  1 
ATOM   6806  C C   . TRP E 2 47  ? 21.696  33.667  86.464  1.000 48.450  ? 47  TRP BBB C   1 
ATOM   6807  O O   . TRP E 2 47  ? 21.350  32.490  86.609  1.000 51.801  ? 47  TRP BBB O   1 
ATOM   6808  C CB  . TRP E 2 47  ? 19.665  34.800  85.455  1.000 43.808  ? 47  TRP BBB CB  1 
ATOM   6809  C CG  . TRP E 2 47  ? 19.339  35.647  86.645  1.000 44.123  ? 47  TRP BBB CG  1 
ATOM   6810  C CD1 . TRP E 2 47  ? 19.271  37.007  86.687  1.000 41.460  ? 47  TRP BBB CD1 1 
ATOM   6811  C CD2 . TRP E 2 47  ? 18.924  35.175  87.942  1.000 44.964  ? 47  TRP BBB CD2 1 
ATOM   6812  N NE1 . TRP E 2 47  ? 18.866  37.422  87.930  1.000 43.629  ? 47  TRP BBB NE1 1 
ATOM   6813  C CE2 . TRP E 2 47  ? 18.651  36.320  88.721  1.000 45.409  ? 47  TRP BBB CE2 1 
ATOM   6814  C CE3 . TRP E 2 47  ? 18.752  33.903  88.514  1.000 42.979  ? 47  TRP BBB CE3 1 
ATOM   6815  C CZ2 . TRP E 2 47  ? 18.228  36.222  90.046  1.000 45.394  ? 47  TRP BBB CZ2 1 
ATOM   6816  C CZ3 . TRP E 2 47  ? 18.344  33.810  89.827  1.000 43.455  ? 47  TRP BBB CZ3 1 
ATOM   6817  C CH2 . TRP E 2 47  ? 18.076  34.960  90.578  1.000 44.738  ? 47  TRP BBB CH2 1 
ATOM   6818  N N   . MET E 2 48  ? 22.576  34.282  87.251  1.000 53.450  ? 48  MET BBB N   1 
ATOM   6819  C CA  . MET E 2 48  ? 23.340  33.606  88.332  1.000 50.864  ? 48  MET BBB CA  1 
ATOM   6820  C C   . MET E 2 48  ? 22.647  33.855  89.671  1.000 47.362  ? 48  MET BBB C   1 
ATOM   6821  O O   . MET E 2 48  ? 22.568  32.912  90.466  1.000 46.939  ? 48  MET BBB O   1 
ATOM   6822  C CB  . MET E 2 48  ? 24.774  34.132  88.428  1.000 53.729  ? 48  MET BBB CB  1 
ATOM   6823  C CG  . MET E 2 48  ? 25.535  34.100  87.116  1.000 57.028  ? 48  MET BBB CG  1 
ATOM   6824  S SD  . MET E 2 48  ? 27.191  34.755  87.326  1.000 58.361  ? 48  MET BBB SD  1 
ATOM   6825  C CE  . MET E 2 48  ? 27.920  33.420  88.279  1.000 55.226  ? 48  MET BBB CE  1 
ATOM   6826  N N   . GLY E 2 49  ? 22.193  35.087  89.916  1.000 41.208  ? 49  GLY BBB N   1 
ATOM   6827  C CA  . GLY E 2 49  ? 21.565  35.469  91.191  1.000 37.224  ? 49  GLY BBB CA  1 
ATOM   6828  C C   . GLY E 2 49  ? 21.310  36.955  91.249  1.000 34.853  ? 49  GLY BBB C   1 
ATOM   6829  O O   . GLY E 2 49  ? 21.735  37.669  90.343  1.000 35.573  ? 49  GLY BBB O   1 
ATOM   6830  N N   . ILE E 2 50  ? 20.627  37.414  92.282  1.000 34.597  ? 50  ILE BBB N   1 
ATOM   6831  C CA  . ILE E 2 50  ? 20.279  38.849  92.446  1.000 36.015  ? 50  ILE BBB CA  1 
ATOM   6832  C C   . ILE E 2 50  ? 20.469  39.164  93.922  1.000 38.366  ? 50  ILE BBB C   1 
ATOM   6833  O O   . ILE E 2 50  ? 20.334  38.236  94.751  1.000 35.472  ? 50  ILE BBB O   1 
ATOM   6834  C CB  . ILE E 2 50  ? 18.847  39.115  91.944  1.000 36.178  ? 50  ILE BBB CB  1 
ATOM   6835  C CG1 . ILE E 2 50  ? 18.487  40.601  91.924  1.000 37.548  ? 50  ILE BBB CG1 1 
ATOM   6836  C CG2 . ILE E 2 50  ? 17.851  38.312  92.764  1.000 38.679  ? 50  ILE BBB CG2 1 
ATOM   6837  C CD1 . ILE E 2 50  ? 17.182  40.907  91.219  1.000 38.090  ? 50  ILE BBB CD1 1 
ATOM   6838  N N   . ILE E 2 51  ? 20.827  40.403  94.233  1.000 42.359  ? 51  ILE BBB N   1 
ATOM   6839  C CA  . ILE E 2 51  ? 20.920  40.854  95.643  1.000 47.237  ? 51  ILE BBB CA  1 
ATOM   6840  C C   . ILE E 2 51  ? 20.204  42.189  95.754  1.000 46.566  ? 51  ILE BBB C   1 
ATOM   6841  O O   . ILE E 2 51  ? 20.132  42.911  94.737  1.000 42.659  ? 51  ILE BBB O   1 
ATOM   6842  C CB  . ILE E 2 51  ? 22.384  40.927  96.123  1.000 53.634  ? 51  ILE BBB CB  1 
ATOM   6843  C CG1 . ILE E 2 51  ? 22.475  40.744  97.640  1.000 56.933  ? 51  ILE BBB CG1 1 
ATOM   6844  C CG2 . ILE E 2 51  ? 23.046  42.218  95.675  1.000 56.411  ? 51  ILE BBB CG2 1 
ATOM   6845  C CD1 . ILE E 2 51  ? 23.880  40.543  98.157  1.000 54.709  ? 51  ILE BBB CD1 1 
ATOM   6846  N N   . TYR E 2 52  ? 19.660  42.459  96.939  1.000 50.522  ? 52  TYR BBB N   1 
ATOM   6847  C CA  . TYR E 2 52  ? 19.174  43.800  97.337  1.000 54.734  ? 52  TYR BBB CA  1 
ATOM   6848  C C   . TYR E 2 52  ? 20.244  44.394  98.244  1.000 62.617  ? 52  TYR BBB C   1 
ATOM   6849  O O   . TYR E 2 52  ? 20.560  43.826  99.288  1.000 55.701  ? 52  TYR BBB O   1 
ATOM   6850  C CB  . TYR E 2 52  ? 17.799  43.747  98.000  1.000 46.839  ? 52  TYR BBB CB  1 
ATOM   6851  C CG  . TYR E 2 52  ? 17.255  45.119  98.296  1.000 42.308  ? 52  TYR BBB CG  1 
ATOM   6852  C CD1 . TYR E 2 52  ? 16.741  45.928  97.305  1.000 42.727  ? 52  TYR BBB CD1 1 
ATOM   6853  C CD2 . TYR E 2 52  ? 17.309  45.643  99.572  1.000 44.118  ? 52  TYR BBB CD2 1 
ATOM   6854  C CE1 . TYR E 2 52  ? 16.269  47.208  97.583  1.000 45.312  ? 52  TYR BBB CE1 1 
ATOM   6855  C CE2 . TYR E 2 52  ? 16.828  46.911  99.876  1.000 43.753  ? 52  TYR BBB CE2 1 
ATOM   6856  C CZ  . TYR E 2 52  ? 16.314  47.706  98.875  1.000 44.227  ? 52  TYR BBB CZ  1 
ATOM   6857  O OH  . TYR E 2 52  ? 15.855  48.952  99.186  1.000 46.041  ? 52  TYR BBB OH  1 
ATOM   6858  N N   . PRO E 2 53  ? 20.853  45.533  97.854  1.000 71.330  ? 53  PRO BBB N   1 
ATOM   6859  C CA  . PRO E 2 53  ? 21.900  46.143  98.661  1.000 74.477  ? 53  PRO BBB CA  1 
ATOM   6860  C C   . PRO E 2 53  ? 21.415  46.531  100.067 1.000 76.080  ? 53  PRO BBB C   1 
ATOM   6861  O O   . PRO E 2 53  ? 22.154  46.294  100.997 1.000 80.626  ? 53  PRO BBB O   1 
ATOM   6862  C CB  . PRO E 2 53  ? 22.246  47.427  97.883  1.000 81.366  ? 53  PRO BBB CB  1 
ATOM   6863  C CG  . PRO E 2 53  ? 21.771  47.184  96.470  1.000 79.180  ? 53  PRO BBB CG  1 
ATOM   6864  C CD  . PRO E 2 53  ? 20.552  46.303  96.636  1.000 75.330  ? 53  PRO BBB CD  1 
ATOM   6865  N N   . GLY E 2 54  ? 20.221  47.140  100.172 1.000 70.765  ? 54  GLY BBB N   1 
ATOM   6866  C CA  . GLY E 2 54  ? 19.687  47.744  101.406 1.000 64.259  ? 54  GLY BBB CA  1 
ATOM   6867  C C   . GLY E 2 54  ? 19.766  46.818  102.614 1.000 63.699  ? 54  GLY BBB C   1 
ATOM   6868  O O   . GLY E 2 54  ? 20.077  47.342  103.692 1.000 74.424  ? 54  GLY BBB O   1 
ATOM   6869  N N   . ASP E 2 55  ? 19.488  45.513  102.468 1.000 60.733  ? 55  ASP BBB N   1 
ATOM   6870  C CA  . ASP E 2 55  ? 19.446  44.544  103.601 1.000 65.288  ? 55  ASP BBB CA  1 
ATOM   6871  C C   . ASP E 2 55  ? 20.151  43.227  103.235 1.000 59.897  ? 55  ASP BBB C   1 
ATOM   6872  O O   . ASP E 2 55  ? 20.036  42.271  104.018 1.000 51.144  ? 55  ASP BBB O   1 
ATOM   6873  C CB  . ASP E 2 55  ? 18.005  44.294  104.069 1.000 72.568  ? 55  ASP BBB CB  1 
ATOM   6874  C CG  . ASP E 2 55  ? 17.118  43.536  103.086 1.000 79.825  ? 55  ASP BBB CG  1 
ATOM   6875  O OD1 . ASP E 2 55  ? 17.512  43.414  101.899 1.000 88.627  ? 55  ASP BBB OD1 1 
ATOM   6876  O OD2 . ASP E 2 55  ? 16.027  43.076  103.510 1.000 77.333  ? 55  ASP BBB OD2 1 
ATOM   6877  N N   . SER E 2 56  ? 20.860  43.162  102.107 1.000 63.661  ? 56  SER BBB N   1 
ATOM   6878  C CA  . SER E 2 56  ? 21.650  41.978  101.665 1.000 64.525  ? 56  SER BBB CA  1 
ATOM   6879  C C   . SER E 2 56  ? 20.763  40.740  101.476 1.000 58.541  ? 56  SER BBB C   1 
ATOM   6880  O O   . SER E 2 56  ? 21.235  39.634  101.769 1.000 45.251  ? 56  SER BBB O   1 
ATOM   6881  C CB  . SER E 2 56  ? 22.777  41.680  102.625 1.000 67.411  ? 56  SER BBB CB  1 
ATOM   6882  O OG  . SER E 2 56  ? 23.666  42.781  102.715 1.000 71.010  ? 56  SER BBB OG  1 
ATOM   6883  N N   . GLU E 2 57  ? 19.530  40.906  100.990 1.000 61.814  ? 57  GLU BBB N   1 
ATOM   6884  C CA  . GLU E 2 57  ? 18.676  39.752  100.598 1.000 61.698  ? 57  GLU BBB CA  1 
ATOM   6885  C C   . GLU E 2 57  ? 19.257  39.165  99.314  1.000 54.385  ? 57  GLU BBB C   1 
ATOM   6886  O O   . GLU E 2 57  ? 19.323  39.898  98.330  1.000 59.783  ? 57  GLU BBB O   1 
ATOM   6887  C CB  . GLU E 2 57  ? 17.214  40.152  100.366 1.000 69.764  ? 57  GLU BBB CB  1 
ATOM   6888  C CG  . GLU E 2 57  ? 16.305  38.940  100.171 1.000 75.878  ? 57  GLU BBB CG  1 
ATOM   6889  C CD  . GLU E 2 57  ? 14.895  39.158  99.635  1.000 74.655  ? 57  GLU BBB CD  1 
ATOM   6890  O OE1 . GLU E 2 57  ? 14.243  40.197  99.936  1.000 72.546  ? 57  GLU BBB OE1 1 
ATOM   6891  O OE2 . GLU E 2 57  ? 14.436  38.248  98.927  1.000 69.203  ? 57  GLU BBB OE2 1 
ATOM   6892  N N   . THR E 2 58  ? 19.643  37.899  99.321  1.000 49.480  ? 58  THR BBB N   1 
ATOM   6893  C CA  . THR E 2 58  ? 20.414  37.269  98.223  1.000 52.786  ? 58  THR BBB CA  1 
ATOM   6894  C C   . THR E 2 58  ? 19.656  36.043  97.717  1.000 54.377  ? 58  THR BBB C   1 
ATOM   6895  O O   . THR E 2 58  ? 19.455  35.115  98.519  1.000 59.543  ? 58  THR BBB O   1 
ATOM   6896  C CB  . THR E 2 58  ? 21.824  36.882  98.698  1.000 52.523  ? 58  THR BBB CB  1 
ATOM   6897  O OG1 . THR E 2 58  ? 22.292  37.851  99.638  1.000 57.166  ? 58  THR BBB OG1 1 
ATOM   6898  C CG2 . THR E 2 58  ? 22.809  36.767  97.556  1.000 50.327  ? 58  THR BBB CG2 1 
ATOM   6899  N N   . ARG E 2 59  ? 19.278  36.034  96.439  1.000 53.899  ? 59  ARG BBB N   1 
ATOM   6900  C CA  . ARG E 2 59  ? 18.610  34.884  95.766  1.000 51.732  ? 59  ARG BBB CA  1 
ATOM   6901  C C   . ARG E 2 59  ? 19.555  34.334  94.697  1.000 43.472  ? 59  ARG BBB C   1 
ATOM   6902  O O   . ARG E 2 59  ? 20.041  35.143  93.886  1.000 42.563  ? 59  ARG BBB O   1 
ATOM   6903  C CB  . ARG E 2 59  ? 17.295  35.347  95.131  1.000 56.983  ? 59  ARG BBB CB  1 
ATOM   6904  C CG  . ARG E 2 59  ? 16.366  36.094  96.086  1.000 60.101  ? 59  ARG BBB CG  1 
ATOM   6905  C CD  . ARG E 2 59  ? 15.077  35.338  96.337  1.000 62.104  ? 59  ARG BBB CD  1 
ATOM   6906  N NE  . ARG E 2 59  ? 13.935  35.849  95.579  1.000 59.550  ? 59  ARG BBB NE  1 
ATOM   6907  C CZ  . ARG E 2 59  ? 13.218  36.928  95.901  1.000 55.258  ? 59  ARG BBB CZ  1 
ATOM   6908  N NH1 . ARG E 2 59  ? 13.514  37.652  96.959  1.000 52.597  ? 59  ARG BBB NH1 1 
ATOM   6909  N NH2 . ARG E 2 59  ? 12.184  37.282  95.172  1.000 58.613  ? 59  ARG BBB NH2 1 
ATOM   6910  N N   . TYR E 2 60  ? 19.802  33.029  94.703  1.000 40.717  ? 60  TYR BBB N   1 
ATOM   6911  C CA  . TYR E 2 60  ? 20.705  32.340  93.746  1.000 46.674  ? 60  TYR BBB CA  1 
ATOM   6912  C C   . TYR E 2 60  ? 19.872  31.607  92.688  1.000 50.943  ? 60  TYR BBB C   1 
ATOM   6913  O O   . TYR E 2 60  ? 18.708  31.317  92.929  1.000 55.929  ? 60  TYR BBB O   1 
ATOM   6914  C CB  . TYR E 2 60  ? 21.630  31.378  94.497  1.000 46.262  ? 60  TYR BBB CB  1 
ATOM   6915  C CG  . TYR E 2 60  ? 22.773  32.035  95.235  1.000 49.460  ? 60  TYR BBB CG  1 
ATOM   6916  C CD1 . TYR E 2 60  ? 23.870  31.291  95.663  1.000 53.304  ? 60  TYR BBB CD1 1 
ATOM   6917  C CD2 . TYR E 2 60  ? 22.765  33.391  95.528  1.000 49.742  ? 60  TYR BBB CD2 1 
ATOM   6918  C CE1 . TYR E 2 60  ? 24.929  31.876  96.337  1.000 52.001  ? 60  TYR BBB CE1 1 
ATOM   6919  C CE2 . TYR E 2 60  ? 23.814  33.988  96.203  1.000 49.188  ? 60  TYR BBB CE2 1 
ATOM   6920  C CZ  . TYR E 2 60  ? 24.891  33.229  96.608  1.000 51.428  ? 60  TYR BBB CZ  1 
ATOM   6921  O OH  . TYR E 2 60  ? 25.872  33.867  97.288  1.000 55.703  ? 60  TYR BBB OH  1 
ATOM   6922  N N   . SER E 2 61  ? 20.452  31.355  91.518  1.000 55.258  ? 61  SER BBB N   1 
ATOM   6923  C CA  . SER E 2 61  ? 19.956  30.343  90.555  1.000 52.602  ? 61  SER BBB CA  1 
ATOM   6924  C C   . SER E 2 61  ? 20.453  28.977  91.008  1.000 47.514  ? 61  SER BBB C   1 
ATOM   6925  O O   . SER E 2 61  ? 21.556  28.852  91.524  1.000 38.707  ? 61  SER BBB O   1 
ATOM   6926  C CB  . SER E 2 61  ? 20.383  30.622  89.146  1.000 55.921  ? 61  SER BBB CB  1 
ATOM   6927  O OG  . SER E 2 61  ? 20.427  29.412  88.399  1.000 55.272  ? 61  SER BBB OG  1 
ATOM   6928  N N   . PRO E 2 62  ? 19.628  27.926  90.836  1.000 52.540  ? 62  PRO BBB N   1 
ATOM   6929  C CA  . PRO E 2 62  ? 20.009  26.562  91.184  1.000 57.112  ? 62  PRO BBB CA  1 
ATOM   6930  C C   . PRO E 2 62  ? 21.400  26.168  90.682  1.000 59.594  ? 62  PRO BBB C   1 
ATOM   6931  O O   . PRO E 2 62  ? 22.070  25.450  91.379  1.000 60.110  ? 62  PRO BBB O   1 
ATOM   6932  C CB  . PRO E 2 62  ? 18.974  25.702  90.444  1.000 61.205  ? 62  PRO BBB CB  1 
ATOM   6933  C CG  . PRO E 2 62  ? 17.746  26.587  90.365  1.000 62.702  ? 62  PRO BBB CG  1 
ATOM   6934  C CD  . PRO E 2 62  ? 18.262  28.009  90.301  1.000 58.356  ? 62  PRO BBB CD  1 
ATOM   6935  N N   . SER E 2 63  ? 21.787  26.624  89.489  1.000 63.230  ? 63  SER BBB N   1 
ATOM   6936  C CA  . SER E 2 63  ? 23.033  26.187  88.798  1.000 66.270  ? 63  SER BBB CA  1 
ATOM   6937  C C   . SER E 2 63  ? 24.270  26.798  89.471  1.000 69.119  ? 63  SER BBB C   1 
ATOM   6938  O O   . SER E 2 63  ? 25.374  26.279  89.237  1.000 66.213  ? 63  SER BBB O   1 
ATOM   6939  C CB  . SER E 2 63  ? 23.006  26.537  87.333  1.000 68.503  ? 63  SER BBB CB  1 
ATOM   6940  O OG  . SER E 2 63  ? 21.716  26.344  86.784  1.000 73.010  ? 63  SER BBB OG  1 
ATOM   6941  N N   . PHE E 2 64  ? 24.099  27.874  90.247  1.000 72.541  ? 64  PHE BBB N   1 
ATOM   6942  C CA  . PHE E 2 64  ? 25.213  28.647  90.855  1.000 67.514  ? 64  PHE BBB CA  1 
ATOM   6943  C C   . PHE E 2 64  ? 25.104  28.669  92.379  1.000 67.771  ? 64  PHE BBB C   1 
ATOM   6944  O O   . PHE E 2 64  ? 25.940  29.325  93.005  1.000 75.707  ? 64  PHE BBB O   1 
ATOM   6945  C CB  . PHE E 2 64  ? 25.220  30.069  90.294  1.000 69.873  ? 64  PHE BBB CB  1 
ATOM   6946  C CG  . PHE E 2 64  ? 25.387  30.133  88.799  1.000 70.965  ? 64  PHE BBB CG  1 
ATOM   6947  C CD1 . PHE E 2 64  ? 26.642  30.033  88.221  1.000 69.129  ? 64  PHE BBB CD1 1 
ATOM   6948  C CD2 . PHE E 2 64  ? 24.285  30.269  87.970  1.000 70.237  ? 64  PHE BBB CD2 1 
ATOM   6949  C CE1 . PHE E 2 64  ? 26.790  30.089  86.849  1.000 64.742  ? 64  PHE BBB CE1 1 
ATOM   6950  C CE2 . PHE E 2 64  ? 24.437  30.318  86.593  1.000 68.847  ? 64  PHE BBB CE2 1 
ATOM   6951  C CZ  . PHE E 2 64  ? 25.691  30.225  86.035  1.000 65.928  ? 64  PHE BBB CZ  1 
ATOM   6952  N N   . GLN E 2 65  ? 24.126  27.976  92.966  1.000 69.194  ? 65  GLN BBB N   1 
ATOM   6953  C CA  . GLN E 2 65  ? 24.036  27.804  94.439  1.000 67.155  ? 65  GLN BBB CA  1 
ATOM   6954  C C   . GLN E 2 65  ? 25.382  27.263  94.924  1.000 59.888  ? 65  GLN BBB C   1 
ATOM   6955  O O   . GLN E 2 65  ? 25.827  26.233  94.378  1.000 52.161  ? 65  GLN BBB O   1 
ATOM   6956  C CB  . GLN E 2 65  ? 22.866  26.889  94.822  1.000 77.930  ? 65  GLN BBB CB  1 
ATOM   6957  C CG  . GLN E 2 65  ? 22.682  26.691  96.326  1.000 80.912  ? 65  GLN BBB CG  1 
ATOM   6958  C CD  . GLN E 2 65  ? 22.267  27.960  97.032  1.000 85.942  ? 65  GLN BBB CD  1 
ATOM   6959  O OE1 . GLN E 2 65  ? 21.365  28.682  96.597  1.000 87.572  ? 65  GLN BBB OE1 1 
ATOM   6960  N NE2 . GLN E 2 65  ? 22.920  28.231  98.151  1.000 88.182  ? 65  GLN BBB NE2 1 
ATOM   6961  N N   . GLY E 2 66  ? 26.029  27.973  95.854  1.000 60.853  ? 66  GLY BBB N   1 
ATOM   6962  C CA  . GLY E 2 66  ? 27.259  27.514  96.536  1.000 66.864  ? 66  GLY BBB CA  1 
ATOM   6963  C C   . GLY E 2 66  ? 28.436  27.247  95.599  1.000 66.825  ? 66  GLY BBB C   1 
ATOM   6964  O O   . GLY E 2 66  ? 29.442  26.668  96.075  1.000 65.099  ? 66  GLY BBB O   1 
ATOM   6965  N N   . GLN E 2 67  ? 28.324  27.615  94.314  1.000 69.422  ? 67  GLN BBB N   1 
ATOM   6966  C CA  . GLN E 2 67  ? 29.442  27.670  93.328  1.000 64.348  ? 67  GLN BBB CA  1 
ATOM   6967  C C   . GLN E 2 67  ? 30.100  29.057  93.365  1.000 56.506  ? 67  GLN BBB C   1 
ATOM   6968  O O   . GLN E 2 67  ? 31.305  29.119  93.070  1.000 54.066  ? 67  GLN BBB O   1 
ATOM   6969  C CB  . GLN E 2 67  ? 28.941  27.364  91.915  1.000 70.088  ? 67  GLN BBB CB  1 
ATOM   6970  C CG  . GLN E 2 67  ? 28.407  25.946  91.756  1.000 75.390  ? 67  GLN BBB CG  1 
ATOM   6971  C CD  . GLN E 2 67  ? 29.401  24.870  92.120  1.000 73.151  ? 67  GLN BBB CD  1 
ATOM   6972  O OE1 . GLN E 2 67  ? 30.616  25.043  92.032  1.000 79.326  ? 67  GLN BBB OE1 1 
ATOM   6973  N NE2 . GLN E 2 67  ? 28.871  23.731  92.528  1.000 70.493  ? 67  GLN BBB NE2 1 
ATOM   6974  N N   . VAL E 2 68  ? 29.335  30.118  93.672  1.000 47.456  ? 68  VAL BBB N   1 
ATOM   6975  C CA  . VAL E 2 68  ? 29.822  31.520  93.832  1.000 44.278  ? 68  VAL BBB CA  1 
ATOM   6976  C C   . VAL E 2 68  ? 29.176  32.120  95.081  1.000 45.779  ? 68  VAL BBB C   1 
ATOM   6977  O O   . VAL E 2 68  ? 28.325  31.430  95.688  1.000 51.910  ? 68  VAL BBB O   1 
ATOM   6978  C CB  . VAL E 2 68  ? 29.474  32.387  92.612  1.000 42.774  ? 68  VAL BBB CB  1 
ATOM   6979  C CG1 . VAL E 2 68  ? 29.872  31.724  91.310  1.000 44.226  ? 68  VAL BBB CG1 1 
ATOM   6980  C CG2 . VAL E 2 68  ? 27.998  32.742  92.577  1.000 43.733  ? 68  VAL BBB CG2 1 
ATOM   6981  N N   . THR E 2 69  ? 29.515  33.381  95.394  1.000 42.047  ? 69  THR BBB N   1 
ATOM   6982  C CA  . THR E 2 69  ? 28.964  34.170  96.524  1.000 39.442  ? 69  THR BBB CA  1 
ATOM   6983  C C   . THR E 2 69  ? 28.701  35.609  96.079  1.000 40.708  ? 69  THR BBB C   1 
ATOM   6984  O O   . THR E 2 69  ? 29.694  36.376  95.854  1.000 44.424  ? 69  THR BBB O   1 
ATOM   6985  C CB  . THR E 2 69  ? 29.905  34.203  97.736  1.000 41.277  ? 69  THR BBB CB  1 
ATOM   6986  O OG1 . THR E 2 69  ? 30.135  32.878  98.201  1.000 43.675  ? 69  THR BBB OG1 1 
ATOM   6987  C CG2 . THR E 2 69  ? 29.374  35.042  98.879  1.000 43.420  ? 69  THR BBB CG2 1 
ATOM   6988  N N   . ILE E 2 70  ? 27.420  35.974  96.008  1.000 41.129  ? 70  ILE BBB N   1 
ATOM   6989  C CA  . ILE E 2 70  ? 26.965  37.372  95.775  1.000 40.447  ? 70  ILE BBB CA  1 
ATOM   6990  C C   . ILE E 2 70  ? 26.854  38.063  97.127  1.000 38.309  ? 70  ILE BBB C   1 
ATOM   6991  O O   . ILE E 2 70  ? 26.247  37.487  98.012  1.000 40.084  ? 70  ILE BBB O   1 
ATOM   6992  C CB  . ILE E 2 70  ? 25.632  37.378  95.016  1.000 42.533  ? 70  ILE BBB CB  1 
ATOM   6993  C CG1 . ILE E 2 70  ? 25.756  36.552  93.727  1.000 44.683  ? 70  ILE BBB CG1 1 
ATOM   6994  C CG2 . ILE E 2 70  ? 25.155  38.814  94.787  1.000 41.397  ? 70  ILE BBB CG2 1 
ATOM   6995  C CD1 . ILE E 2 70  ? 24.454  36.291  93.015  1.000 46.836  ? 70  ILE BBB CD1 1 
ATOM   6996  N N   . SER E 2 71  ? 27.455  39.238  97.260  1.000 39.754  ? 71  SER BBB N   1 
ATOM   6997  C CA  . SER E 2 71  ? 27.528  40.045  98.505  1.000 40.327  ? 71  SER BBB CA  1 
ATOM   6998  C C   . SER E 2 71  ? 27.244  41.491  98.121  1.000 39.052  ? 71  SER BBB C   1 
ATOM   6999  O O   . SER E 2 71  ? 27.160  41.766  96.923  1.000 37.919  ? 71  SER BBB O   1 
ATOM   7000  C CB  . SER E 2 71  ? 28.871  39.883  99.198  1.000 43.776  ? 71  SER BBB CB  1 
ATOM   7001  O OG  . SER E 2 71  ? 29.931  39.698  98.260  1.000 50.158  ? 71  SER BBB OG  1 
ATOM   7002  N N   . ALA E 2 72  ? 27.090  42.388  99.084  1.000 41.545  ? 72  ALA BBB N   1 
ATOM   7003  C CA  . ALA E 2 72  ? 26.769  43.804  98.795  1.000 46.014  ? 72  ALA BBB CA  1 
ATOM   7004  C C   . ALA E 2 72  ? 27.364  44.697  99.881  1.000 50.122  ? 72  ALA BBB C   1 
ATOM   7005  O O   . ALA E 2 72  ? 27.702  44.183  100.960 1.000 48.526  ? 72  ALA BBB O   1 
ATOM   7006  C CB  . ALA E 2 72  ? 25.275  43.999  98.681  1.000 48.882  ? 72  ALA BBB CB  1 
ATOM   7007  N N   . ASP E 2 73  ? 27.491  45.985  99.575  1.000 54.207  ? 73  ASP BBB N   1 
ATOM   7008  C CA  . ASP E 2 73  ? 27.947  47.030  100.520 1.000 59.170  ? 73  ASP BBB CA  1 
ATOM   7009  C C   . ASP E 2 73  ? 27.187  48.303  100.156 1.000 61.333  ? 73  ASP BBB C   1 
ATOM   7010  O O   . ASP E 2 73  ? 27.599  49.015  99.188  1.000 61.967  ? 73  ASP BBB O   1 
ATOM   7011  C CB  . ASP E 2 73  ? 29.469  47.175  100.488 1.000 66.805  ? 73  ASP BBB CB  1 
ATOM   7012  C CG  . ASP E 2 73  ? 30.035  48.107  101.552 1.000 72.679  ? 73  ASP BBB CG  1 
ATOM   7013  O OD1 . ASP E 2 73  ? 29.302  49.041  101.978 1.000 79.696  ? 73  ASP BBB OD1 1 
ATOM   7014  O OD2 . ASP E 2 73  ? 31.204  47.902  101.941 1.000 73.733  ? 73  ASP BBB OD2 1 
ATOM   7015  N N   . LYS E 2 74  ? 26.090  48.528  100.881 1.000 60.966  ? 74  LYS BBB N   1 
ATOM   7016  C CA  . LYS E 2 74  ? 25.118  49.614  100.613 1.000 68.345  ? 74  LYS BBB CA  1 
ATOM   7017  C C   . LYS E 2 74  ? 25.787  50.976  100.808 1.000 68.607  ? 74  LYS BBB C   1 
ATOM   7018  O O   . LYS E 2 74  ? 25.273  51.941  100.224 1.000 71.049  ? 74  LYS BBB O   1 
ATOM   7019  C CB  . LYS E 2 74  ? 23.887  49.454  101.510 1.000 75.317  ? 74  LYS BBB CB  1 
ATOM   7020  C CG  . LYS E 2 74  ? 24.177  49.200  102.987 1.000 77.852  ? 74  LYS BBB CG  1 
ATOM   7021  C CD  . LYS E 2 74  ? 22.918  49.013  103.805 1.000 80.358  ? 74  LYS BBB CD  1 
ATOM   7022  C CE  . LYS E 2 74  ? 23.196  48.528  105.206 1.000 79.507  ? 74  LYS BBB CE  1 
ATOM   7023  N NZ  . LYS E 2 74  ? 21.915  48.431  105.932 1.000 80.086  ? 74  LYS BBB NZ  1 
ATOM   7024  N N   . SER E 2 75  ? 26.881  51.050  101.583 1.000 64.172  ? 75  SER BBB N   1 
ATOM   7025  C CA  . SER E 2 75  ? 27.557  52.324  101.954 1.000 59.825  ? 75  SER BBB CA  1 
ATOM   7026  C C   . SER E 2 75  ? 28.264  52.932  100.737 1.000 61.649  ? 75  SER BBB C   1 
ATOM   7027  O O   . SER E 2 75  ? 28.412  54.167  100.708 1.000 52.807  ? 75  SER BBB O   1 
ATOM   7028  C CB  . SER E 2 75  ? 28.496  52.137  103.105 1.000 54.869  ? 75  SER BBB CB  1 
ATOM   7029  O OG  . SER E 2 75  ? 29.447  51.152  102.799 1.000 52.164  ? 75  SER BBB OG  1 
ATOM   7030  N N   . ILE E 2 76  ? 28.637  52.105  99.750  1.000 70.545  ? 76  ILE BBB N   1 
ATOM   7031  C CA  . ILE E 2 76  ? 29.367  52.545  98.516  1.000 71.917  ? 76  ILE BBB CA  1 
ATOM   7032  C C   . ILE E 2 76  ? 28.583  52.160  97.250  1.000 73.254  ? 76  ILE BBB C   1 
ATOM   7033  O O   . ILE E 2 76  ? 29.121  52.373  96.156  1.000 69.872  ? 76  ILE BBB O   1 
ATOM   7034  C CB  . ILE E 2 76  ? 30.799  51.974  98.518  1.000 66.655  ? 76  ILE BBB CB  1 
ATOM   7035  C CG1 . ILE E 2 76  ? 30.831  50.511  98.981  1.000 61.464  ? 76  ILE BBB CG1 1 
ATOM   7036  C CG2 . ILE E 2 76  ? 31.700  52.857  99.368  1.000 69.728  ? 76  ILE BBB CG2 1 
ATOM   7037  C CD1 . ILE E 2 76  ? 32.188  49.834  98.876  1.000 55.354  ? 76  ILE BBB CD1 1 
ATOM   7038  N N   . ASN E 2 77  ? 27.349  51.653  97.394  1.000 68.596  ? 77  ASN BBB N   1 
ATOM   7039  C CA  . ASN E 2 77  ? 26.420  51.352  96.273  1.000 61.027  ? 77  ASN BBB CA  1 
ATOM   7040  C C   . ASN E 2 77  ? 27.016  50.244  95.397  1.000 55.034  ? 77  ASN BBB C   1 
ATOM   7041  O O   . ASN E 2 77  ? 26.927  50.362  94.171  1.000 54.017  ? 77  ASN BBB O   1 
ATOM   7042  C CB  . ASN E 2 77  ? 26.075  52.624  95.484  1.000 57.347  ? 77  ASN BBB CB  1 
ATOM   7043  C CG  . ASN E 2 77  ? 25.254  53.591  96.309  1.000 62.324  ? 77  ASN BBB CG  1 
ATOM   7044  O OD1 . ASN E 2 77  ? 24.946  53.312  97.464  1.000 68.430  ? 77  ASN BBB OD1 1 
ATOM   7045  N ND2 . ASN E 2 77  ? 24.868  54.715  95.726  1.000 65.727  ? 77  ASN BBB ND2 1 
ATOM   7046  N N   . THR E 2 78  ? 27.582  49.200  95.995  1.000 51.255  ? 78  THR BBB N   1 
ATOM   7047  C CA  . THR E 2 78  ? 28.431  48.217  95.277  1.000 59.459  ? 78  THR BBB CA  1 
ATOM   7048  C C   . THR E 2 78  ? 27.973  46.794  95.585  1.000 56.918  ? 78  THR BBB C   1 
ATOM   7049  O O   . THR E 2 78  ? 27.936  46.423  96.767  1.000 57.508  ? 78  THR BBB O   1 
ATOM   7050  C CB  . THR E 2 78  ? 29.920  48.381  95.634  1.000 68.367  ? 78  THR BBB CB  1 
ATOM   7051  O OG1 . THR E 2 78  ? 30.244  49.771  95.549  1.000 76.083  ? 78  THR BBB OG1 1 
ATOM   7052  C CG2 . THR E 2 78  ? 30.848  47.600  94.728  1.000 69.191  ? 78  THR BBB CG2 1 
ATOM   7053  N N   . ALA E 2 79  ? 27.686  46.030  94.537  1.000 53.794  ? 79  ALA BBB N   1 
ATOM   7054  C CA  . ALA E 2 79  ? 27.466  44.566  94.584  1.000 53.480  ? 79  ALA BBB CA  1 
ATOM   7055  C C   . ALA E 2 79  ? 28.752  43.843  94.196  1.000 47.962  ? 79  ALA BBB C   1 
ATOM   7056  O O   . ALA E 2 79  ? 29.486  44.366  93.349  1.000 53.183  ? 79  ALA BBB O   1 
ATOM   7057  C CB  . ALA E 2 79  ? 26.351  44.191  93.640  1.000 60.809  ? 79  ALA BBB CB  1 
ATOM   7058  N N   . TYR E 2 80  ? 28.987  42.667  94.764  1.000 46.956  ? 80  TYR BBB N   1 
ATOM   7059  C CA  . TYR E 2 80  ? 30.219  41.860  94.562  1.000 54.355  ? 80  TYR BBB CA  1 
ATOM   7060  C C   . TYR E 2 80  ? 29.805  40.445  94.171  1.000 53.941  ? 80  TYR BBB C   1 
ATOM   7061  O O   . TYR E 2 80  ? 28.785  39.951  94.662  1.000 66.764  ? 80  TYR BBB O   1 
ATOM   7062  C CB  . TYR E 2 80  ? 31.094  41.821  95.824  1.000 60.091  ? 80  TYR BBB CB  1 
ATOM   7063  C CG  . TYR E 2 80  ? 31.651  43.153  96.277  1.000 66.302  ? 80  TYR BBB CG  1 
ATOM   7064  C CD1 . TYR E 2 80  ? 32.931  43.564  95.932  1.000 63.008  ? 80  TYR BBB CD1 1 
ATOM   7065  C CD2 . TYR E 2 80  ? 30.892  44.019  97.056  1.000 76.531  ? 80  TYR BBB CD2 1 
ATOM   7066  C CE1 . TYR E 2 80  ? 33.436  44.789  96.348  1.000 64.468  ? 80  TYR BBB CE1 1 
ATOM   7067  C CE2 . TYR E 2 80  ? 31.374  45.254  97.464  1.000 72.228  ? 80  TYR BBB CE2 1 
ATOM   7068  C CZ  . TYR E 2 80  ? 32.657  45.639  97.117  1.000 67.355  ? 80  TYR BBB CZ  1 
ATOM   7069  O OH  . TYR E 2 80  ? 33.134  46.853  97.518  1.000 66.461  ? 80  TYR BBB OH  1 
ATOM   7070  N N   . LEU E 2 81  ? 30.573  39.831  93.283  1.000 53.726  ? 81  LEU BBB N   1 
ATOM   7071  C CA  . LEU E 2 81  ? 30.432  38.404  92.899  1.000 55.805  ? 81  LEU BBB CA  1 
ATOM   7072  C C   . LEU E 2 81  ? 31.818  37.757  93.049  1.000 49.200  ? 81  LEU BBB C   1 
ATOM   7073  O O   . LEU E 2 81  ? 32.737  38.255  92.372  1.000 49.085  ? 81  LEU BBB O   1 
ATOM   7074  C CB  . LEU E 2 81  ? 29.876  38.353  91.467  1.000 58.565  ? 81  LEU BBB CB  1 
ATOM   7075  C CG  . LEU E 2 81  ? 30.056  37.029  90.721  1.000 60.544  ? 81  LEU BBB CG  1 
ATOM   7076  C CD1 . LEU E 2 81  ? 29.392  35.867  91.445  1.000 59.610  ? 81  LEU BBB CD1 1 
ATOM   7077  C CD2 . LEU E 2 81  ? 29.520  37.130  89.304  1.000 63.585  ? 81  LEU BBB CD2 1 
ATOM   7078  N N   . GLN E 2 82  ? 31.980  36.756  93.934  1.000 42.579  ? 82  GLN BBB N   1 
ATOM   7079  C CA  . GLN E 2 82  ? 33.312  36.185  94.286  1.000 43.831  ? 82  GLN BBB CA  1 
ATOM   7080  C C   . GLN E 2 82  ? 33.330  34.654  94.250  1.000 42.592  ? 82  GLN BBB C   1 
ATOM   7081  O O   . GLN E 2 82  ? 32.322  34.023  94.527  1.000 44.258  ? 82  GLN BBB O   1 
ATOM   7082  C CB  . GLN E 2 82  ? 33.805  36.670  95.652  1.000 48.455  ? 82  GLN BBB CB  1 
ATOM   7083  C CG  . GLN E 2 82  ? 33.068  36.117  96.860  1.000 52.026  ? 82  GLN BBB CG  1 
ATOM   7084  C CD  . GLN E 2 82  ? 33.409  36.901  98.111  1.000 50.801  ? 82  GLN BBB CD  1 
ATOM   7085  O OE1 . GLN E 2 82  ? 34.573  37.061  98.454  1.000 50.686  ? 82  GLN BBB OE1 1 
ATOM   7086  N NE2 . GLN E 2 82  ? 32.401  37.428  98.792  1.000 51.527  ? 82  GLN BBB NE2 1 
ATOM   7087  N N   . TRP E 2 83  ? 34.483  34.112  93.873  1.000 47.190  ? 83  TRP BBB N   1 
ATOM   7088  C CA  . TRP E 2 83  ? 34.849  32.675  93.900  1.000 51.567  ? 83  TRP BBB CA  1 
ATOM   7089  C C   . TRP E 2 83  ? 35.914  32.448  94.986  1.000 52.188  ? 83  TRP BBB C   1 
ATOM   7090  O O   . TRP E 2 83  ? 36.780  33.320  95.192  1.000 52.729  ? 83  TRP BBB O   1 
ATOM   7091  C CB  . TRP E 2 83  ? 35.372  32.239  92.523  1.000 53.120  ? 83  TRP BBB CB  1 
ATOM   7092  C CG  . TRP E 2 83  ? 34.380  32.304  91.400  1.000 52.007  ? 83  TRP BBB CG  1 
ATOM   7093  C CD1 . TRP E 2 83  ? 33.706  31.248  90.861  1.000 52.960  ? 83  TRP BBB CD1 1 
ATOM   7094  C CD2 . TRP E 2 83  ? 33.991  33.457  90.629  1.000 48.725  ? 83  TRP BBB CD2 1 
ATOM   7095  N NE1 . TRP E 2 83  ? 32.910  31.667  89.832  1.000 54.302  ? 83  TRP BBB NE1 1 
ATOM   7096  C CE2 . TRP E 2 83  ? 33.061  33.018  89.662  1.000 48.803  ? 83  TRP BBB CE2 1 
ATOM   7097  C CE3 . TRP E 2 83  ? 34.333  34.810  90.650  1.000 48.797  ? 83  TRP BBB CE3 1 
ATOM   7098  C CZ2 . TRP E 2 83  ? 32.469  33.877  88.735  1.000 45.378  ? 83  TRP BBB CZ2 1 
ATOM   7099  C CZ3 . TRP E 2 83  ? 33.745  35.660  89.736  1.000 50.433  ? 83  TRP BBB CZ3 1 
ATOM   7100  C CH2 . TRP E 2 83  ? 32.829  35.200  88.792  1.000 47.016  ? 83  TRP BBB CH2 1 
ATOM   7101  N N   . SER E 2 84  ? 35.850  31.304  95.659  1.000 52.229  ? 84  SER BBB N   1 
ATOM   7102  C CA  . SER E 2 84  ? 36.894  30.814  96.583  1.000 55.764  ? 84  SER BBB CA  1 
ATOM   7103  C C   . SER E 2 84  ? 38.047  30.268  95.747  1.000 58.556  ? 84  SER BBB C   1 
ATOM   7104  O O   . SER E 2 84  ? 39.188  30.632  96.042  1.000 70.524  ? 84  SER BBB O   1 
ATOM   7105  C CB  . SER E 2 84  ? 36.353  29.760  97.512  1.000 60.445  ? 84  SER BBB CB  1 
ATOM   7106  O OG  . SER E 2 84  ? 35.607  28.776  96.797  1.000 67.029  ? 84  SER BBB OG  1 
ATOM   7107  N N   . SER E 2 85  ? 37.750  29.465  94.721  1.000 58.228  ? 85  SER BBB N   1 
ATOM   7108  C CA  . SER E 2 85  ? 38.743  28.691  93.923  1.000 60.491  ? 85  SER BBB CA  1 
ATOM   7109  C C   . SER E 2 85  ? 38.277  28.529  92.467  1.000 61.516  ? 85  SER BBB C   1 
ATOM   7110  O O   . SER E 2 85  ? 37.398  27.669  92.189  1.000 63.660  ? 85  SER BBB O   1 
ATOM   7111  C CB  . SER E 2 85  ? 39.034  27.353  94.548  1.000 63.710  ? 85  SER BBB CB  1 
ATOM   7112  O OG  . SER E 2 85  ? 39.927  26.600  93.739  1.000 67.471  ? 85  SER BBB OG  1 
ATOM   7113  N N   . LEU E 2 86  ? 38.903  29.281  91.554  1.000 59.082  ? 86  LEU BBB N   1 
ATOM   7114  C CA  . LEU E 2 86  ? 38.482  29.403  90.135  1.000 51.640  ? 86  LEU BBB CA  1 
ATOM   7115  C C   . LEU E 2 86  ? 38.843  28.132  89.372  1.000 51.049  ? 86  LEU BBB C   1 
ATOM   7116  O O   . LEU E 2 86  ? 39.961  27.627  89.525  1.000 43.562  ? 86  LEU BBB O   1 
ATOM   7117  C CB  . LEU E 2 86  ? 39.149  30.621  89.495  1.000 49.681  ? 86  LEU BBB CB  1 
ATOM   7118  C CG  . LEU E 2 86  ? 38.432  31.944  89.737  1.000 50.643  ? 86  LEU BBB CG  1 
ATOM   7119  C CD1 . LEU E 2 86  ? 39.268  33.107  89.242  1.000 51.969  ? 86  LEU BBB CD1 1 
ATOM   7120  C CD2 . LEU E 2 86  ? 37.064  31.962  89.076  1.000 51.903  ? 86  LEU BBB CD2 1 
ATOM   7121  N N   . LYS E 2 87  ? 37.900  27.644  88.573  1.000 57.010  ? 87  LYS BBB N   1 
ATOM   7122  C CA  . LYS E 2 87  ? 38.140  26.557  87.590  1.000 60.122  ? 87  LYS BBB CA  1 
ATOM   7123  C C   . LYS E 2 87  ? 38.302  27.248  86.235  1.000 52.490  ? 87  LYS BBB C   1 
ATOM   7124  O O   . LYS E 2 87  ? 37.830  28.413  86.085  1.000 46.461  ? 87  LYS BBB O   1 
ATOM   7125  C CB  . LYS E 2 87  ? 36.999  25.526  87.597  1.000 69.884  ? 87  LYS BBB CB  1 
ATOM   7126  C CG  . LYS E 2 87  ? 36.544  25.026  88.969  1.000 75.788  ? 87  LYS BBB CG  1 
ATOM   7127  C CD  . LYS E 2 87  ? 35.142  24.412  88.994  1.000 76.112  ? 87  LYS BBB CD  1 
ATOM   7128  C CE  . LYS E 2 87  ? 34.631  24.169  90.405  1.000 90.994  ? 87  LYS BBB CE  1 
ATOM   7129  N NZ  . LYS E 2 87  ? 33.185  24.497  90.580  1.000 104.351 ? 87  LYS BBB NZ  1 
ATOM   7130  N N   . ALA E 2 88  ? 38.953  26.576  85.290  1.000 48.386  ? 88  ALA BBB N   1 
ATOM   7131  C CA  . ALA E 2 88  ? 39.143  27.068  83.906  1.000 46.319  ? 88  ALA BBB CA  1 
ATOM   7132  C C   . ALA E 2 88  ? 37.776  27.265  83.234  1.000 47.452  ? 88  ALA BBB C   1 
ATOM   7133  O O   . ALA E 2 88  ? 37.671  28.166  82.401  1.000 44.489  ? 88  ALA BBB O   1 
ATOM   7134  C CB  . ALA E 2 88  ? 40.012  26.109  83.131  1.000 45.762  ? 88  ALA BBB CB  1 
ATOM   7135  N N   . SER E 2 89  ? 36.774  26.453  83.591  1.000 51.838  ? 89  SER BBB N   1 
ATOM   7136  C CA  . SER E 2 89  ? 35.388  26.487  83.050  1.000 49.841  ? 89  SER BBB CA  1 
ATOM   7137  C C   . SER E 2 89  ? 34.693  27.802  83.411  1.000 47.290  ? 89  SER BBB C   1 
ATOM   7138  O O   . SER E 2 89  ? 33.713  28.117  82.729  1.000 47.823  ? 89  SER BBB O   1 
ATOM   7139  C CB  . SER E 2 89  ? 34.581  25.294  83.525  1.000 51.029  ? 89  SER BBB CB  1 
ATOM   7140  O OG  . SER E 2 89  ? 34.612  25.173  84.938  1.000 52.616  ? 89  SER BBB OG  1 
ATOM   7141  N N   . ASP E 2 90  ? 35.194  28.536  84.415  1.000 46.245  ? 90  ASP BBB N   1 
ATOM   7142  C CA  . ASP E 2 90  ? 34.606  29.813  84.911  1.000 50.681  ? 90  ASP BBB CA  1 
ATOM   7143  C C   . ASP E 2 90  ? 34.969  30.981  83.980  1.000 49.954  ? 90  ASP BBB C   1 
ATOM   7144  O O   . ASP E 2 90  ? 34.506  32.115  84.254  1.000 42.045  ? 90  ASP BBB O   1 
ATOM   7145  C CB  . ASP E 2 90  ? 35.072  30.119  86.339  1.000 54.280  ? 90  ASP BBB CB  1 
ATOM   7146  C CG  . ASP E 2 90  ? 34.290  29.391  87.413  1.000 58.045  ? 90  ASP BBB CG  1 
ATOM   7147  O OD1 . ASP E 2 90  ? 33.036  29.428  87.334  1.000 59.195  ? 90  ASP BBB OD1 1 
ATOM   7148  O OD2 . ASP E 2 90  ? 34.941  28.793  88.312  1.000 60.915  ? 90  ASP BBB OD2 1 
ATOM   7149  N N   . THR E 2 91  ? 35.788  30.737  82.947  1.000 49.215  ? 91  THR BBB N   1 
ATOM   7150  C CA  . THR E 2 91  ? 36.206  31.751  81.942  1.000 42.554  ? 91  THR BBB CA  1 
ATOM   7151  C C   . THR E 2 91  ? 34.977  32.224  81.184  1.000 41.924  ? 91  THR BBB C   1 
ATOM   7152  O O   . THR E 2 91  ? 34.410  31.416  80.415  1.000 42.583  ? 91  THR BBB O   1 
ATOM   7153  C CB  . THR E 2 91  ? 37.175  31.194  80.899  1.000 39.156  ? 91  THR BBB CB  1 
ATOM   7154  O OG1 . THR E 2 91  ? 38.358  30.821  81.595  1.000 35.530  ? 91  THR BBB OG1 1 
ATOM   7155  C CG2 . THR E 2 91  ? 37.482  32.194  79.807  1.000 38.380  ? 91  THR BBB CG2 1 
ATOM   7156  N N   . ALA E 2 92  ? 34.594  33.474  81.398  1.000 41.622  ? 92  ALA BBB N   1 
ATOM   7157  C CA  . ALA E 2 92  ? 33.433  34.076  80.716  1.000 44.566  ? 92  ALA BBB CA  1 
ATOM   7158  C C   . ALA E 2 92  ? 33.510  35.590  80.818  1.000 42.013  ? 92  ALA BBB C   1 
ATOM   7159  O O   . ALA E 2 92  ? 34.555  36.101  81.220  1.000 51.053  ? 92  ALA BBB O   1 
ATOM   7160  C CB  . ALA E 2 92  ? 32.160  33.549  81.321  1.000 48.456  ? 92  ALA BBB CB  1 
ATOM   7161  N N   . ILE E 2 93  ? 32.450  36.259  80.396  1.000 38.464  ? 93  ILE BBB N   1 
ATOM   7162  C CA  . ILE E 2 93  ? 32.223  37.688  80.713  1.000 40.959  ? 93  ILE BBB CA  1 
ATOM   7163  C C   . ILE E 2 93  ? 30.985  37.754  81.612  1.000 40.735  ? 93  ILE BBB C   1 
ATOM   7164  O O   . ILE E 2 93  ? 29.967  37.120  81.278  1.000 46.226  ? 93  ILE BBB O   1 
ATOM   7165  C CB  . ILE E 2 93  ? 32.120  38.547  79.443  1.000 44.542  ? 93  ILE BBB CB  1 
ATOM   7166  C CG1 . ILE E 2 93  ? 31.642  39.955  79.809  1.000 54.108  ? 93  ILE BBB CG1 1 
ATOM   7167  C CG2 . ILE E 2 93  ? 31.249  37.895  78.386  1.000 46.703  ? 93  ILE BBB CG2 1 
ATOM   7168  C CD1 . ILE E 2 93  ? 31.671  40.933  78.656  1.000 62.072  ? 93  ILE BBB CD1 1 
ATOM   7169  N N   . TYR E 2 94  ? 31.111  38.453  82.739  1.000 36.865  ? 94  TYR BBB N   1 
ATOM   7170  C CA  . TYR E 2 94  ? 30.089  38.553  83.805  1.000 33.534  ? 94  TYR BBB CA  1 
ATOM   7171  C C   . TYR E 2 94  ? 29.532  39.978  83.817  1.000 33.901  ? 94  TYR BBB C   1 
ATOM   7172  O O   . TYR E 2 94  ? 30.257  40.912  84.181  1.000 33.802  ? 94  TYR BBB O   1 
ATOM   7173  C CB  . TYR E 2 94  ? 30.701  38.145  85.144  1.000 31.869  ? 94  TYR BBB CB  1 
ATOM   7174  C CG  . TYR E 2 94  ? 31.155  36.712  85.214  1.000 33.062  ? 94  TYR BBB CG  1 
ATOM   7175  C CD1 . TYR E 2 94  ? 30.334  35.736  85.735  1.000 34.742  ? 94  TYR BBB CD1 1 
ATOM   7176  C CD2 . TYR E 2 94  ? 32.408  36.318  84.775  1.000 36.016  ? 94  TYR BBB CD2 1 
ATOM   7177  C CE1 . TYR E 2 94  ? 30.729  34.408  85.802  1.000 34.998  ? 94  TYR BBB CE1 1 
ATOM   7178  C CE2 . TYR E 2 94  ? 32.827  34.996  84.850  1.000 34.420  ? 94  TYR BBB CE2 1 
ATOM   7179  C CZ  . TYR E 2 94  ? 31.984  34.036  85.363  1.000 33.254  ? 94  TYR BBB CZ  1 
ATOM   7180  O OH  . TYR E 2 94  ? 32.391  32.737  85.438  1.000 36.620  ? 94  TYR BBB OH  1 
ATOM   7181  N N   . TYR E 2 95  ? 28.273  40.122  83.411  1.000 36.163  ? 95  TYR BBB N   1 
ATOM   7182  C CA  . TYR E 2 95  ? 27.474  41.368  83.511  1.000 38.428  ? 95  TYR BBB CA  1 
ATOM   7183  C C   . TYR E 2 95  ? 26.768  41.431  84.874  1.000 40.617  ? 95  TYR BBB C   1 
ATOM   7184  O O   . TYR E 2 95  ? 26.300  40.416  85.379  1.000 42.660  ? 95  TYR BBB O   1 
ATOM   7185  C CB  . TYR E 2 95  ? 26.451  41.421  82.377  1.000 38.678  ? 95  TYR BBB CB  1 
ATOM   7186  C CG  . TYR E 2 95  ? 27.043  41.371  80.992  1.000 37.638  ? 95  TYR BBB CG  1 
ATOM   7187  C CD1 . TYR E 2 95  ? 27.530  42.513  80.392  1.000 38.371  ? 95  TYR BBB CD1 1 
ATOM   7188  C CD2 . TYR E 2 95  ? 27.123  40.186  80.283  1.000 39.506  ? 95  TYR BBB CD2 1 
ATOM   7189  C CE1 . TYR E 2 95  ? 28.087  42.488  79.126  1.000 39.191  ? 95  TYR BBB CE1 1 
ATOM   7190  C CE2 . TYR E 2 95  ? 27.672  40.136  79.014  1.000 40.544  ? 95  TYR BBB CE2 1 
ATOM   7191  C CZ  . TYR E 2 95  ? 28.156  41.294  78.432  1.000 40.427  ? 95  TYR BBB CZ  1 
ATOM   7192  O OH  . TYR E 2 95  ? 28.708  41.252  77.185  1.000 42.083  ? 95  TYR BBB OH  1 
ATOM   7193  N N   . CYS E 2 96  ? 26.713  42.610  85.477  1.000 44.896  ? 96  CYS BBB N   1 
ATOM   7194  C CA  . CYS E 2 96  ? 25.730  42.932  86.535  1.000 47.374  ? 96  CYS BBB CA  1 
ATOM   7195  C C   . CYS E 2 96  ? 24.642  43.756  85.845  1.000 48.419  ? 96  CYS BBB C   1 
ATOM   7196  O O   . CYS E 2 96  ? 24.992  44.610  85.014  1.000 49.918  ? 96  CYS BBB O   1 
ATOM   7197  C CB  . CYS E 2 96  ? 26.381  43.664  87.703  1.000 47.877  ? 96  CYS BBB CB  1 
ATOM   7198  S SG  . CYS E 2 96  ? 27.006  45.296  87.215  1.000 53.214  ? 96  CYS BBB SG  1 
ATOM   7199  N N   . ALA E 2 97  ? 23.380  43.455  86.127  1.000 48.604  ? 97  ALA BBB N   1 
ATOM   7200  C CA  . ALA E 2 97  ? 22.216  44.224  85.641  1.000 51.554  ? 97  ALA BBB CA  1 
ATOM   7201  C C   . ALA E 2 97  ? 21.406  44.710  86.841  1.000 56.020  ? 97  ALA BBB C   1 
ATOM   7202  O O   . ALA E 2 97  ? 21.547  44.112  87.935  1.000 53.538  ? 97  ALA BBB O   1 
ATOM   7203  C CB  . ALA E 2 97  ? 21.386  43.362  84.744  1.000 55.932  ? 97  ALA BBB CB  1 
ATOM   7204  N N   . GLY E 2 98  ? 20.590  45.747  86.630  1.000 59.220  ? 98  GLY BBB N   1 
ATOM   7205  C CA  . GLY E 2 98  ? 19.846  46.440  87.700  1.000 60.429  ? 98  GLY BBB CA  1 
ATOM   7206  C C   . GLY E 2 98  ? 18.384  46.580  87.347  1.000 61.755  ? 98  GLY BBB C   1 
ATOM   7207  O O   . GLY E 2 98  ? 18.084  47.137  86.263  1.000 59.287  ? 98  GLY BBB O   1 
ATOM   7208  N N   . GLY E 2 99  ? 17.518  46.043  88.210  1.000 65.162  ? 99  GLY BBB N   1 
ATOM   7209  C CA  . GLY E 2 99  ? 16.073  46.336  88.241  1.000 70.420  ? 99  GLY BBB CA  1 
ATOM   7210  C C   . GLY E 2 99  ? 15.701  47.163  89.463  1.000 68.701  ? 99  GLY BBB C   1 
ATOM   7211  O O   . GLY E 2 99  ? 16.206  46.850  90.574  1.000 70.817  ? 99  GLY BBB O   1 
ATOM   7212  N N   . SER E 2 100 ? 14.833  48.170  89.286  1.000 63.126  ? 100 SER BBB N   1 
ATOM   7213  C CA  . SER E 2 100 ? 14.347  49.052  90.383  1.000 59.959  ? 100 SER BBB CA  1 
ATOM   7214  C C   . SER E 2 100 ? 13.376  48.284  91.305  1.000 58.630  ? 100 SER BBB C   1 
ATOM   7215  O O   . SER E 2 100 ? 12.937  48.842  92.315  1.000 66.268  ? 100 SER BBB O   1 
ATOM   7216  C CB  . SER E 2 100 ? 13.750  50.312  89.824  1.000 58.919  ? 100 SER BBB CB  1 
ATOM   7217  O OG  . SER E 2 100 ? 13.081  50.026  88.613  1.000 63.574  ? 100 SER BBB OG  1 
ATOM   7218  N N   . GLY E 2 101 ? 13.076  47.025  91.010  1.000 56.325  ? 101 GLY BBB N   1 
ATOM   7219  C CA  . GLY E 2 101 ? 12.343  46.142  91.931  1.000 53.681  ? 101 GLY BBB CA  1 
ATOM   7220  C C   . GLY E 2 101 ? 12.767  44.688  91.783  1.000 53.162  ? 101 GLY BBB C   1 
ATOM   7221  O O   . GLY E 2 101 ? 13.559  44.335  90.890  1.000 46.559  ? 101 GLY BBB O   1 
ATOM   7222  N N   . ILE E 2 102 ? 12.287  43.861  92.690  1.000 53.519  ? 102 ILE BBB N   1 
ATOM   7223  C CA  . ILE E 2 102 ? 12.476  42.396  92.642  1.000 55.104  ? 102 ILE BBB CA  1 
ATOM   7224  C C   . ILE E 2 102 ? 11.238  42.067  91.853  1.000 57.517  ? 102 ILE BBB C   1 
ATOM   7225  O O   . ILE E 2 102 ? 10.200  42.567  92.296  1.000 62.533  ? 102 ILE BBB O   1 
ATOM   7226  C CB  . ILE E 2 102 ? 12.290  41.636  93.957  1.000 59.679  ? 102 ILE BBB CB  1 
ATOM   7227  C CG1 . ILE E 2 102 ? 12.557  40.146  93.816  1.000 55.489  ? 102 ILE BBB CG1 1 
ATOM   7228  C CG2 . ILE E 2 102 ? 10.877  41.814  94.481  1.000 72.015  ? 102 ILE BBB CG2 1 
ATOM   7229  C CD1 . ILE E 2 102 ? 13.938  39.813  93.417  1.000 58.065  ? 102 ILE BBB CD1 1 
ATOM   7230  N N   . SER E 2 103 ? 11.341  41.288  90.797  1.000 53.978  ? 103 SER BBB N   1 
ATOM   7231  C CA  . SER E 2 103 ? 10.267  40.926  89.822  1.000 50.429  ? 103 SER BBB CA  1 
ATOM   7232  C C   . SER E 2 103 ? 9.984   42.141  88.936  1.000 51.259  ? 103 SER BBB C   1 
ATOM   7233  O O   . SER E 2 103 ? 8.829   42.567  88.680  1.000 44.844  ? 103 SER BBB O   1 
ATOM   7234  C CB  . SER E 2 103 ? 9.052   40.322  90.444  1.000 53.341  ? 103 SER BBB CB  1 
ATOM   7235  O OG  . SER E 2 103 ? 8.519   39.311  89.597  1.000 58.339  ? 103 SER BBB OG  1 
ATOM   7236  N N   . THR E 2 104 ? 11.104  42.598  88.399  1.000 60.799  ? 104 THR BBB N   1 
ATOM   7237  C CA  . THR E 2 104 ? 11.276  43.788  87.555  1.000 61.043  ? 104 THR BBB CA  1 
ATOM   7238  C C   . THR E 2 104 ? 12.267  43.407  86.459  1.000 64.098  ? 104 THR BBB C   1 
ATOM   7239  O O   . THR E 2 104 ? 13.199  42.608  86.678  1.000 60.218  ? 104 THR BBB O   1 
ATOM   7240  C CB  . THR E 2 104 ? 11.731  44.958  88.431  1.000 62.774  ? 104 THR BBB CB  1 
ATOM   7241  O OG1 . THR E 2 104 ? 10.587  45.312  89.206  1.000 72.500  ? 104 THR BBB OG1 1 
ATOM   7242  C CG2 . THR E 2 104 ? 12.273  46.149  87.664  1.000 63.488  ? 104 THR BBB CG2 1 
ATOM   7243  N N   . PRO E 2 105 ? 12.097  43.978  85.243  1.000 63.128  ? 105 PRO BBB N   1 
ATOM   7244  C CA  . PRO E 2 105 ? 13.067  43.764  84.172  1.000 59.960  ? 105 PRO BBB CA  1 
ATOM   7245  C C   . PRO E 2 105 ? 14.390  44.428  84.576  1.000 61.698  ? 105 PRO BBB C   1 
ATOM   7246  O O   . PRO E 2 105 ? 14.365  45.413  85.314  1.000 64.768  ? 105 PRO BBB O   1 
ATOM   7247  C CB  . PRO E 2 105 ? 12.424  44.476  82.973  1.000 58.265  ? 105 PRO BBB CB  1 
ATOM   7248  C CG  . PRO E 2 105 ? 11.582  45.575  83.609  1.000 59.357  ? 105 PRO BBB CG  1 
ATOM   7249  C CD  . PRO E 2 105 ? 11.025  44.919  84.856  1.000 62.014  ? 105 PRO BBB CD  1 
ATOM   7250  N N   . MET E 2 106 ? 15.506  43.923  84.058  1.000 56.981  ? 106 MET BBB N   1 
ATOM   7251  C CA  . MET E 2 106 ? 16.839  44.560  84.199  1.000 53.556  ? 106 MET BBB CA  1 
ATOM   7252  C C   . MET E 2 106 ? 16.975  45.738  83.214  1.000 52.720  ? 106 MET BBB C   1 
ATOM   7253  O O   . MET E 2 106 ? 17.354  45.482  82.044  1.000 50.410  ? 106 MET BBB O   1 
ATOM   7254  C CB  . MET E 2 106 ? 17.875  43.474  83.945  1.000 54.160  ? 106 MET BBB CB  1 
ATOM   7255  C CG  . MET E 2 106 ? 17.816  42.433  85.041  1.000 59.763  ? 106 MET BBB CG  1 
ATOM   7256  S SD  . MET E 2 106 ? 18.502  40.828  84.589  1.000 66.335  ? 106 MET BBB SD  1 
ATOM   7257  C CE  . MET E 2 106 ? 18.903  40.301  86.254  1.000 69.336  ? 106 MET BBB CE  1 
ATOM   7258  N N   . ASP E 2 107 ? 16.631  46.960  83.678  1.000 54.825  ? 107 ASP BBB N   1 
ATOM   7259  C CA  . ASP E 2 107 ? 16.582  48.240  82.910  1.000 58.211  ? 107 ASP BBB CA  1 
ATOM   7260  C C   . ASP E 2 107 ? 18.006  48.587  82.471  1.000 60.631  ? 107 ASP BBB C   1 
ATOM   7261  O O   . ASP E 2 107 ? 18.193  48.910  81.277  1.000 62.963  ? 107 ASP BBB O   1 
ATOM   7262  C CB  . ASP E 2 107 ? 16.140  49.485  83.709  1.000 64.426  ? 107 ASP BBB CB  1 
ATOM   7263  C CG  . ASP E 2 107 ? 14.944  49.371  84.650  1.000 77.152  ? 107 ASP BBB CG  1 
ATOM   7264  O OD1 . ASP E 2 107 ? 13.907  48.844  84.243  1.000 96.771  ? 107 ASP BBB OD1 1 
ATOM   7265  O OD2 . ASP E 2 107 ? 15.049  49.841  85.793  1.000 80.331  ? 107 ASP BBB OD2 1 
ATOM   7266  N N   . VAL E 2 108 ? 18.941  48.509  83.434  1.000 54.196  ? 108 VAL BBB N   1 
ATOM   7267  C CA  . VAL E 2 108 ? 20.322  49.068  83.409  1.000 48.511  ? 108 VAL BBB CA  1 
ATOM   7268  C C   . VAL E 2 108 ? 21.329  47.923  83.522  1.000 49.491  ? 108 VAL BBB C   1 
ATOM   7269  O O   . VAL E 2 108 ? 21.124  47.022  84.365  1.000 49.322  ? 108 VAL BBB O   1 
ATOM   7270  C CB  . VAL E 2 108 ? 20.512  50.065  84.561  1.000 48.399  ? 108 VAL BBB CB  1 
ATOM   7271  C CG1 . VAL E 2 108 ? 21.967  50.460  84.736  1.000 48.635  ? 108 VAL BBB CG1 1 
ATOM   7272  C CG2 . VAL E 2 108 ? 19.629  51.292  84.366  1.000 52.344  ? 108 VAL BBB CG2 1 
ATOM   7273  N N   . TRP E 2 109 ? 22.394  47.982  82.709  1.000 47.512  ? 109 TRP BBB N   1 
ATOM   7274  C CA  . TRP E 2 109 ? 23.469  46.957  82.641  1.000 42.451  ? 109 TRP BBB CA  1 
ATOM   7275  C C   . TRP E 2 109 ? 24.858  47.589  82.860  1.000 40.050  ? 109 TRP BBB C   1 
ATOM   7276  O O   . TRP E 2 109 ? 25.083  48.732  82.435  1.000 36.298  ? 109 TRP BBB O   1 
ATOM   7277  C CB  . TRP E 2 109 ? 23.402  46.238  81.293  1.000 39.541  ? 109 TRP BBB CB  1 
ATOM   7278  C CG  . TRP E 2 109 ? 22.233  45.326  81.132  1.000 39.092  ? 109 TRP BBB CG  1 
ATOM   7279  C CD1 . TRP E 2 109 ? 20.963  45.668  80.776  1.000 40.559  ? 109 TRP BBB CD1 1 
ATOM   7280  C CD2 . TRP E 2 109 ? 22.240  43.900  81.273  1.000 38.771  ? 109 TRP BBB CD2 1 
ATOM   7281  N NE1 . TRP E 2 109 ? 20.175  44.550  80.720  1.000 41.175  ? 109 TRP BBB NE1 1 
ATOM   7282  C CE2 . TRP E 2 109 ? 20.937  43.449  80.999  1.000 38.253  ? 109 TRP BBB CE2 1 
ATOM   7283  C CE3 . TRP E 2 109 ? 23.218  42.960  81.596  1.000 42.697  ? 109 TRP BBB CE3 1 
ATOM   7284  C CZ2 . TRP E 2 109 ? 20.592  42.102  81.042  1.000 40.695  ? 109 TRP BBB CZ2 1 
ATOM   7285  C CZ3 . TRP E 2 109 ? 22.879  41.624  81.634  1.000 43.599  ? 109 TRP BBB CZ3 1 
ATOM   7286  C CH2 . TRP E 2 109 ? 21.580  41.202  81.368  1.000 41.802  ? 109 TRP BBB CH2 1 
ATOM   7287  N N   . GLY E 2 110 ? 25.767  46.832  83.478  1.000 41.394  ? 110 GLY BBB N   1 
ATOM   7288  C CA  . GLY E 2 110 ? 27.215  47.107  83.496  1.000 43.190  ? 110 GLY BBB CA  1 
ATOM   7289  C C   . GLY E 2 110 ? 27.827  46.830  82.140  1.000 45.451  ? 110 GLY BBB C   1 
ATOM   7290  O O   . GLY E 2 110 ? 27.150  46.235  81.307  1.000 53.219  ? 110 GLY BBB O   1 
ATOM   7291  N N   . GLN E 2 111 ? 29.061  47.270  81.912  1.000 47.630  ? 111 GLN BBB N   1 
ATOM   7292  C CA  . GLN E 2 111 ? 29.782  47.100  80.620  1.000 46.311  ? 111 GLN BBB CA  1 
ATOM   7293  C C   . GLN E 2 111 ? 30.285  45.653  80.510  1.000 41.780  ? 111 GLN BBB C   1 
ATOM   7294  O O   . GLN E 2 111 ? 30.628  45.235  79.410  1.000 39.304  ? 111 GLN BBB O   1 
ATOM   7295  C CB  . GLN E 2 111 ? 30.928  48.112  80.505  1.000 47.192  ? 111 GLN BBB CB  1 
ATOM   7296  C CG  . GLN E 2 111 ? 32.111  47.854  81.440  1.000 45.844  ? 111 GLN BBB CG  1 
ATOM   7297  C CD  . GLN E 2 111 ? 31.975  48.496  82.802  1.000 46.814  ? 111 GLN BBB CD  1 
ATOM   7298  O OE1 . GLN E 2 111 ? 31.101  49.324  83.052  1.000 53.648  ? 111 GLN BBB OE1 1 
ATOM   7299  N NE2 . GLN E 2 111 ? 32.842  48.103  83.717  1.000 43.261  ? 111 GLN BBB NE2 1 
ATOM   7300  N N   . GLY E 2 112 ? 30.317  44.919  81.619  1.000 39.076  ? 112 GLY BBB N   1 
ATOM   7301  C CA  . GLY E 2 112 ? 30.795  43.529  81.664  1.000 40.627  ? 112 GLY BBB CA  1 
ATOM   7302  C C   . GLY E 2 112 ? 32.207  43.491  82.200  1.000 39.825  ? 112 GLY BBB C   1 
ATOM   7303  O O   . GLY E 2 112 ? 32.952  44.434  81.922  1.000 45.719  ? 112 GLY BBB O   1 
ATOM   7304  N N   . THR E 2 113 ? 32.542  42.471  82.981  1.000 38.473  ? 113 THR BBB N   1 
ATOM   7305  C CA  . THR E 2 113 ? 33.920  42.190  83.436  1.000 41.356  ? 113 THR BBB CA  1 
ATOM   7306  C C   . THR E 2 113 ? 34.350  40.889  82.776  1.000 45.552  ? 113 THR BBB C   1 
ATOM   7307  O O   . THR E 2 113 ? 33.728  39.856  83.102  1.000 50.368  ? 113 THR BBB O   1 
ATOM   7308  C CB  . THR E 2 113 ? 34.018  42.022  84.954  1.000 42.057  ? 113 THR BBB CB  1 
ATOM   7309  O OG1 . THR E 2 113 ? 33.603  43.234  85.585  1.000 44.404  ? 113 THR BBB OG1 1 
ATOM   7310  C CG2 . THR E 2 113 ? 35.419  41.656  85.398  1.000 41.418  ? 113 THR BBB CG2 1 
ATOM   7311  N N   . THR E 2 114 ? 35.351  40.933  81.888  1.000 46.295  ? 114 THR BBB N   1 
ATOM   7312  C CA  . THR E 2 114 ? 35.884  39.709  81.235  1.000 41.594  ? 114 THR BBB CA  1 
ATOM   7313  C C   . THR E 2 114 ? 36.840  39.003  82.201  1.000 42.751  ? 114 THR BBB C   1 
ATOM   7314  O O   . THR E 2 114 ? 37.827  39.614  82.622  1.000 46.665  ? 114 THR BBB O   1 
ATOM   7315  C CB  . THR E 2 114 ? 36.536  40.014  79.890  1.000 38.958  ? 114 THR BBB CB  1 
ATOM   7316  O OG1 . THR E 2 114 ? 35.557  40.630  79.064  1.000 38.057  ? 114 THR BBB OG1 1 
ATOM   7317  C CG2 . THR E 2 114 ? 37.051  38.766  79.221  1.000 39.239  ? 114 THR BBB CG2 1 
ATOM   7318  N N   . VAL E 2 115 ? 36.528  37.758  82.555  1.000 40.669  ? 115 VAL BBB N   1 
ATOM   7319  C CA  . VAL E 2 115 ? 37.379  36.902  83.419  1.000 39.992  ? 115 VAL BBB CA  1 
ATOM   7320  C C   . VAL E 2 115 ? 37.941  35.778  82.548  1.000 39.465  ? 115 VAL BBB C   1 
ATOM   7321  O O   . VAL E 2 115 ? 37.140  35.055  81.927  1.000 39.416  ? 115 VAL BBB O   1 
ATOM   7322  C CB  . VAL E 2 115 ? 36.567  36.362  84.606  1.000 40.629  ? 115 VAL BBB CB  1 
ATOM   7323  C CG1 . VAL E 2 115 ? 37.393  35.402  85.452  1.000 43.609  ? 115 VAL BBB CG1 1 
ATOM   7324  C CG2 . VAL E 2 115 ? 36.000  37.488  85.452  1.000 40.575  ? 115 VAL BBB CG2 1 
ATOM   7325  N N   . THR E 2 116 ? 39.265  35.658  82.489  1.000 37.724  ? 116 THR BBB N   1 
ATOM   7326  C CA  . THR E 2 116 ? 39.957  34.567  81.766  1.000 36.795  ? 116 THR BBB CA  1 
ATOM   7327  C C   . THR E 2 116 ? 40.682  33.717  82.796  1.000 37.593  ? 116 THR BBB C   1 
ATOM   7328  O O   . THR E 2 116 ? 41.552  34.255  83.447  1.000 41.407  ? 116 THR BBB O   1 
ATOM   7329  C CB  . THR E 2 116 ? 40.943  35.122  80.738  1.000 36.824  ? 116 THR BBB CB  1 
ATOM   7330  O OG1 . THR E 2 116 ? 40.358  36.214  80.031  1.000 38.849  ? 116 THR BBB OG1 1 
ATOM   7331  C CG2 . THR E 2 116 ? 41.392  34.056  79.773  1.000 36.721  ? 116 THR BBB CG2 1 
ATOM   7332  N N   . VAL E 2 117 ? 40.293  32.462  82.974  1.000 40.281  ? 117 VAL BBB N   1 
ATOM   7333  C CA  . VAL E 2 117 ? 40.979  31.498  83.884  1.000 40.578  ? 117 VAL BBB CA  1 
ATOM   7334  C C   . VAL E 2 117 ? 41.679  30.473  82.984  1.000 42.870  ? 117 VAL BBB C   1 
ATOM   7335  O O   . VAL E 2 117 ? 40.999  29.837  82.152  1.000 47.646  ? 117 VAL BBB O   1 
ATOM   7336  C CB  . VAL E 2 117 ? 40.000  30.853  84.887  1.000 42.059  ? 117 VAL BBB CB  1 
ATOM   7337  C CG1 . VAL E 2 117 ? 40.709  29.940  85.875  1.000 44.286  ? 117 VAL BBB CG1 1 
ATOM   7338  C CG2 . VAL E 2 117 ? 39.179  31.898  85.631  1.000 40.766  ? 117 VAL BBB CG2 1 
ATOM   7339  N N   . SER E 2 118 ? 43.003  30.385  83.084  1.000 44.210  ? 118 SER BBB N   1 
ATOM   7340  C CA  . SER E 2 118 ? 43.868  29.522  82.237  1.000 46.097  ? 118 SER BBB CA  1 
ATOM   7341  C C   . SER E 2 118 ? 45.214  29.340  82.939  1.000 47.082  ? 118 SER BBB C   1 
ATOM   7342  O O   . SER E 2 118 ? 45.707  30.315  83.549  1.000 43.431  ? 118 SER BBB O   1 
ATOM   7343  C CB  . SER E 2 118 ? 44.034  30.113  80.845  1.000 47.289  ? 118 SER BBB CB  1 
ATOM   7344  O OG  . SER E 2 118 ? 44.989  29.411  80.059  1.000 43.001  ? 118 SER BBB OG  1 
ATOM   7345  N N   . SER E 2 119 ? 45.767  28.131  82.866  1.000 49.470  ? 119 SER BBB N   1 
ATOM   7346  C CA  . SER E 2 119 ? 47.109  27.796  83.404  1.000 51.847  ? 119 SER BBB CA  1 
ATOM   7347  C C   . SER E 2 119 ? 48.193  28.452  82.537  1.000 52.204  ? 119 SER BBB C   1 
ATOM   7348  O O   . SER E 2 119 ? 49.373  28.426  82.937  1.000 53.491  ? 119 SER BBB O   1 
ATOM   7349  C CB  . SER E 2 119 ? 47.298  26.311  83.490  1.000 57.515  ? 119 SER BBB CB  1 
ATOM   7350  O OG  . SER E 2 119 ? 47.243  25.736  82.193  1.000 64.757  ? 119 SER BBB OG  1 
ATOM   7351  N N   . ALA E 2 120 ? 47.811  29.031  81.391  1.000 49.458  ? 120 ALA BBB N   1 
ATOM   7352  C CA  . ALA E 2 120 ? 48.696  29.776  80.470  1.000 44.288  ? 120 ALA BBB CA  1 
ATOM   7353  C C   . ALA E 2 120 ? 49.273  30.999  81.178  1.000 40.847  ? 120 ALA BBB C   1 
ATOM   7354  O O   . ALA E 2 120 ? 48.538  31.677  81.943  1.000 36.657  ? 120 ALA BBB O   1 
ATOM   7355  C CB  . ALA E 2 120 ? 47.922  30.171  79.243  1.000 43.630  ? 120 ALA BBB CB  1 
ATOM   7356  N N   . SER E 2 121 ? 50.554  31.246  80.904  1.000 42.511  ? 121 SER BBB N   1 
ATOM   7357  C CA  . SER E 2 121 ? 51.311  32.452  81.311  1.000 47.894  ? 121 SER BBB CA  1 
ATOM   7358  C C   . SER E 2 121 ? 51.255  33.487  80.191  1.000 45.636  ? 121 SER BBB C   1 
ATOM   7359  O O   . SER E 2 121 ? 51.134  33.109  79.014  1.000 41.072  ? 121 SER BBB O   1 
ATOM   7360  C CB  . SER E 2 121 ? 52.735  32.126  81.654  1.000 51.292  ? 121 SER BBB CB  1 
ATOM   7361  O OG  . SER E 2 121 ? 52.809  31.529  82.938  1.000 55.901  ? 121 SER BBB OG  1 
ATOM   7362  N N   . THR E 2 122 ? 51.361  34.755  80.574  1.000 46.063  ? 122 THR BBB N   1 
ATOM   7363  C CA  . THR E 2 122 ? 51.428  35.891  79.625  1.000 46.672  ? 122 THR BBB CA  1 
ATOM   7364  C C   . THR E 2 122 ? 52.479  35.574  78.567  1.000 43.984  ? 122 THR BBB C   1 
ATOM   7365  O O   . THR E 2 122 ? 53.626  35.297  78.937  1.000 44.280  ? 122 THR BBB O   1 
ATOM   7366  C CB  . THR E 2 122 ? 51.778  37.199  80.330  1.000 48.072  ? 122 THR BBB CB  1 
ATOM   7367  O OG1 . THR E 2 122 ? 50.750  37.419  81.292  1.000 55.451  ? 122 THR BBB OG1 1 
ATOM   7368  C CG2 . THR E 2 122 ? 51.854  38.366  79.379  1.000 47.927  ? 122 THR BBB CG2 1 
ATOM   7369  N N   . LYS E 2 123 ? 52.085  35.592  77.302  1.000 41.609  ? 123 LYS BBB N   1 
ATOM   7370  C CA  . LYS E 2 123 ? 53.025  35.395  76.179  1.000 40.341  ? 123 LYS BBB CA  1 
ATOM   7371  C C   . LYS E 2 123 ? 52.626  36.301  75.015  1.000 36.520  ? 123 LYS BBB C   1 
ATOM   7372  O O   . LYS E 2 123 ? 51.478  36.266  74.587  1.000 33.574  ? 123 LYS BBB O   1 
ATOM   7373  C CB  . LYS E 2 123 ? 53.091  33.941  75.708  1.000 46.481  ? 123 LYS BBB CB  1 
ATOM   7374  C CG  . LYS E 2 123 ? 54.222  33.733  74.724  1.000 52.317  ? 123 LYS BBB CG  1 
ATOM   7375  C CD  . LYS E 2 123 ? 54.165  32.534  73.830  1.000 59.708  ? 123 LYS BBB CD  1 
ATOM   7376  C CE  . LYS E 2 123 ? 55.112  32.805  72.673  1.000 68.992  ? 123 LYS BBB CE  1 
ATOM   7377  N NZ  . LYS E 2 123 ? 55.270  31.658  71.756  1.000 75.885  ? 123 LYS BBB NZ  1 
ATOM   7378  N N   . GLY E 2 124 ? 53.595  37.056  74.508  1.000 36.783  ? 124 GLY BBB N   1 
ATOM   7379  C CA  . GLY E 2 124 ? 53.436  37.961  73.361  1.000 34.360  ? 124 GLY BBB CA  1 
ATOM   7380  C C   . GLY E 2 124 ? 53.333  37.174  72.059  1.000 34.661  ? 124 GLY BBB C   1 
ATOM   7381  O O   . GLY E 2 124 ? 53.915  36.097  71.903  1.000 33.867  ? 124 GLY BBB O   1 
ATOM   7382  N N   . PRO E 2 125 ? 52.591  37.713  71.078  1.000 35.030  ? 125 PRO BBB N   1 
ATOM   7383  C CA  . PRO E 2 125 ? 52.308  37.000  69.836  1.000 35.235  ? 125 PRO BBB CA  1 
ATOM   7384  C C   . PRO E 2 125 ? 53.516  36.928  68.914  1.000 32.767  ? 125 PRO BBB C   1 
ATOM   7385  O O   . PRO E 2 125 ? 54.356  37.777  68.986  1.000 33.703  ? 125 PRO BBB O   1 
ATOM   7386  C CB  . PRO E 2 125 ? 51.255  37.854  69.125  1.000 36.772  ? 125 PRO BBB CB  1 
ATOM   7387  C CG  . PRO E 2 125 ? 51.495  39.245  69.686  1.000 39.004  ? 125 PRO BBB CG  1 
ATOM   7388  C CD  . PRO E 2 125 ? 52.001  39.054  71.104  1.000 37.777  ? 125 PRO BBB CD  1 
ATOM   7389  N N   . SER E 2 126 ? 53.531  35.918  68.061  1.000 32.669  ? 126 SER BBB N   1 
ATOM   7390  C CA  . SER E 2 126 ? 54.485  35.785  66.937  1.000 36.543  ? 126 SER BBB CA  1 
ATOM   7391  C C   . SER E 2 126 ? 53.703  36.114  65.657  1.000 36.935  ? 126 SER BBB C   1 
ATOM   7392  O O   . SER E 2 126 ? 52.604  35.592  65.480  1.000 39.725  ? 126 SER BBB O   1 
ATOM   7393  C CB  . SER E 2 126 ? 55.113  34.404  66.907  1.000 36.559  ? 126 SER BBB CB  1 
ATOM   7394  O OG  . SER E 2 126 ? 55.402  33.920  68.217  1.000 37.130  ? 126 SER BBB OG  1 
ATOM   7395  N N   . VAL E 2 127 ? 54.206  37.011  64.822  1.000 33.149  ? 127 VAL BBB N   1 
ATOM   7396  C CA  . VAL E 2 127 ? 53.461  37.508  63.638  1.000 29.247  ? 127 VAL BBB CA  1 
ATOM   7397  C C   . VAL E 2 127 ? 54.150  36.970  62.400  1.000 29.161  ? 127 VAL BBB C   1 
ATOM   7398  O O   . VAL E 2 127 ? 55.351  37.166  62.270  1.000 35.279  ? 127 VAL BBB O   1 
ATOM   7399  C CB  . VAL E 2 127 ? 53.409  39.038  63.628  1.000 30.166  ? 127 VAL BBB CB  1 
ATOM   7400  C CG1 . VAL E 2 127 ? 52.572  39.544  62.486  1.000 31.163  ? 127 VAL BBB CG1 1 
ATOM   7401  C CG2 . VAL E 2 127 ? 52.894  39.580  64.950  1.000 30.676  ? 127 VAL BBB CG2 1 
ATOM   7402  N N   . PHE E 2 128 ? 53.388  36.332  61.523  1.000 29.413  ? 128 PHE BBB N   1 
ATOM   7403  C CA  . PHE E 2 128 ? 53.859  35.684  60.270  1.000 29.986  ? 128 PHE BBB CA  1 
ATOM   7404  C C   . PHE E 2 128 ? 53.056  36.240  59.105  1.000 29.803  ? 128 PHE BBB C   1 
ATOM   7405  O O   . PHE E 2 128 ? 51.866  36.471  59.231  1.000 31.147  ? 128 PHE BBB O   1 
ATOM   7406  C CB  . PHE E 2 128 ? 53.662  34.166  60.334  1.000 30.079  ? 128 PHE BBB CB  1 
ATOM   7407  C CG  . PHE E 2 128 ? 54.309  33.508  61.529  1.000 29.552  ? 128 PHE BBB CG  1 
ATOM   7408  C CD1 . PHE E 2 128 ? 55.677  33.620  61.731  1.000 29.644  ? 128 PHE BBB CD1 1 
ATOM   7409  C CD2 . PHE E 2 128 ? 53.565  32.812  62.468  1.000 28.887  ? 128 PHE BBB CD2 1 
ATOM   7410  C CE1 . PHE E 2 128 ? 56.292  33.037  62.830  1.000 28.251  ? 128 PHE BBB CE1 1 
ATOM   7411  C CE2 . PHE E 2 128 ? 54.179  32.254  63.579  1.000 29.664  ? 128 PHE BBB CE2 1 
ATOM   7412  C CZ  . PHE E 2 128 ? 55.540  32.374  63.764  1.000 28.329  ? 128 PHE BBB CZ  1 
ATOM   7413  N N   . PRO E 2 129 ? 53.666  36.468  57.926  1.000 29.941  ? 129 PRO BBB N   1 
ATOM   7414  C CA  . PRO E 2 129 ? 52.941  36.990  56.776  1.000 29.508  ? 129 PRO BBB CA  1 
ATOM   7415  C C   . PRO E 2 129 ? 52.107  35.906  56.099  1.000 30.615  ? 129 PRO BBB C   1 
ATOM   7416  O O   . PRO E 2 129 ? 52.619  34.834  55.886  1.000 30.293  ? 129 PRO BBB O   1 
ATOM   7417  C CB  . PRO E 2 129 ? 54.042  37.459  55.822  1.000 30.282  ? 129 PRO BBB CB  1 
ATOM   7418  C CG  . PRO E 2 129 ? 55.207  36.559  56.150  1.000 30.680  ? 129 PRO BBB CG  1 
ATOM   7419  C CD  . PRO E 2 129 ? 55.089  36.270  57.635  1.000 30.895  ? 129 PRO BBB CD  1 
ATOM   7420  N N   . LEU E 2 130 ? 50.852  36.236  55.800  1.000 33.550  ? 130 LEU BBB N   1 
ATOM   7421  C CA  . LEU E 2 130 ? 50.048  35.582  54.739  1.000 34.164  ? 130 LEU BBB CA  1 
ATOM   7422  C C   . LEU E 2 130 ? 50.370  36.309  53.432  1.000 33.094  ? 130 LEU BBB C   1 
ATOM   7423  O O   . LEU E 2 130 ? 49.669  37.263  53.074  1.000 28.306  ? 130 LEU BBB O   1 
ATOM   7424  C CB  . LEU E 2 130 ? 48.567  35.628  55.113  1.000 35.538  ? 130 LEU BBB CB  1 
ATOM   7425  C CG  . LEU E 2 130 ? 48.252  35.083  56.499  1.000 37.693  ? 130 LEU BBB CG  1 
ATOM   7426  C CD1 . LEU E 2 130 ? 46.756  35.095  56.735  1.000 38.797  ? 130 LEU BBB CD1 1 
ATOM   7427  C CD2 . LEU E 2 130 ? 48.832  33.684  56.678  1.000 40.767  ? 130 LEU BBB CD2 1 
ATOM   7428  N N   . ALA E 2 131 ? 51.449  35.866  52.785  1.000 36.044  ? 131 ALA BBB N   1 
ATOM   7429  C CA  . ALA E 2 131 ? 52.029  36.480  51.571  1.000 37.775  ? 131 ALA BBB CA  1 
ATOM   7430  C C   . ALA E 2 131 ? 51.059  36.318  50.416  1.000 38.743  ? 131 ALA BBB C   1 
ATOM   7431  O O   . ALA E 2 131 ? 50.522  35.235  50.208  1.000 36.265  ? 131 ALA BBB O   1 
ATOM   7432  C CB  . ALA E 2 131 ? 53.359  35.840  51.249  1.000 41.644  ? 131 ALA BBB CB  1 
ATOM   7433  N N   . PRO E 2 132 ? 50.838  37.379  49.610  1.000 42.585  ? 132 PRO BBB N   1 
ATOM   7434  C CA  . PRO E 2 132 ? 49.944  37.291  48.459  1.000 46.833  ? 132 PRO BBB CA  1 
ATOM   7435  C C   . PRO E 2 132 ? 50.569  36.410  47.378  1.000 51.039  ? 132 PRO BBB C   1 
ATOM   7436  O O   . PRO E 2 132 ? 51.738  36.593  47.147  1.000 51.846  ? 132 PRO BBB O   1 
ATOM   7437  C CB  . PRO E 2 132 ? 49.847  38.739  47.960  1.000 44.628  ? 132 PRO BBB CB  1 
ATOM   7438  C CG  . PRO E 2 132 ? 51.120  39.390  48.427  1.000 44.698  ? 132 PRO BBB CG  1 
ATOM   7439  C CD  . PRO E 2 132 ? 51.498  38.689  49.717  1.000 44.156  ? 132 PRO BBB CD  1 
ATOM   7440  N N   . SER E 2 133 ? 49.813  35.501  46.753  1.000 63.317  ? 133 SER BBB N   1 
ATOM   7441  C CA  . SER E 2 133 ? 50.318  34.729  45.589  1.000 77.248  ? 133 SER BBB CA  1 
ATOM   7442  C C   . SER E 2 133 ? 50.657  35.731  44.481  1.000 93.291  ? 133 SER BBB C   1 
ATOM   7443  O O   . SER E 2 133 ? 49.834  36.656  44.237  1.000 82.723  ? 133 SER BBB O   1 
ATOM   7444  C CB  . SER E 2 133 ? 49.364  33.681  45.106  1.000 74.404  ? 133 SER BBB CB  1 
ATOM   7445  O OG  . SER E 2 133 ? 48.238  34.294  44.522  1.000 84.098  ? 133 SER BBB OG  1 
ATOM   7446  N N   . SER E 2 134 ? 51.866  35.588  43.923  1.000 115.996 ? 134 SER BBB N   1 
ATOM   7447  C CA  . SER E 2 134 ? 52.413  36.367  42.785  1.000 118.142 ? 134 SER BBB CA  1 
ATOM   7448  C C   . SER E 2 134 ? 51.542  36.096  41.558  1.000 117.640 ? 134 SER BBB C   1 
ATOM   7449  O O   . SER E 2 134 ? 51.134  37.066  40.890  1.000 132.755 ? 134 SER BBB O   1 
ATOM   7450  C CB  . SER E 2 134 ? 53.843  35.983  42.539  1.000 115.885 ? 134 SER BBB CB  1 
ATOM   7451  O OG  . SER E 2 134 ? 53.926  34.588  42.274  1.000 103.562 ? 134 SER BBB OG  1 
ATOM   7452  N N   . LYS E 2 135 ? 51.253  34.816  41.301  1.000 101.223 ? 135 LYS BBB N   1 
ATOM   7453  C CA  . LYS E 2 135 ? 50.283  34.367  40.270  1.000 107.764 ? 135 LYS BBB CA  1 
ATOM   7454  C C   . LYS E 2 135 ? 48.857  34.539  40.799  1.000 110.595 ? 135 LYS BBB C   1 
ATOM   7455  O O   . LYS E 2 135 ? 48.384  33.594  41.456  1.000 106.576 ? 135 LYS BBB O   1 
ATOM   7456  C CB  . LYS E 2 135 ? 50.530  32.899  39.908  1.000 111.731 ? 135 LYS BBB CB  1 
ATOM   7457  C CG  . LYS E 2 135 ? 51.749  32.646  39.027  1.000 120.056 ? 135 LYS BBB CG  1 
ATOM   7458  C CD  . LYS E 2 135 ? 51.472  31.703  37.868  1.000 123.214 ? 135 LYS BBB CD  1 
ATOM   7459  C CE  . LYS E 2 135 ? 50.724  32.376  36.734  1.000 124.781 ? 135 LYS BBB CE  1 
ATOM   7460  N NZ  . LYS E 2 135 ? 49.617  31.531  36.229  1.000 131.195 ? 135 LYS BBB NZ  1 
ATOM   7461  N N   . SER E 2 136 ? 48.229  35.702  40.552  1.000 121.185 ? 136 SER BBB N   1 
ATOM   7462  C CA  . SER E 2 136 ? 46.812  36.029  40.902  1.000 125.590 ? 136 SER BBB CA  1 
ATOM   7463  C C   . SER E 2 136 ? 46.144  36.756  39.722  1.000 131.447 ? 136 SER BBB C   1 
ATOM   7464  O O   . SER E 2 136 ? 46.875  37.103  38.776  1.000 134.458 ? 136 SER BBB O   1 
ATOM   7465  C CB  . SER E 2 136 ? 46.698  36.822  42.206  1.000 118.577 ? 136 SER BBB CB  1 
ATOM   7466  O OG  . SER E 2 136 ? 47.377  38.067  42.140  1.000 101.510 ? 136 SER BBB OG  1 
ATOM   7467  N N   . THR E 2 137 ? 44.815  36.947  39.761  1.000 129.379 ? 137 THR BBB N   1 
ATOM   7468  C CA  . THR E 2 137 ? 44.019  37.566  38.659  1.000 118.501 ? 137 THR BBB CA  1 
ATOM   7469  C C   . THR E 2 137 ? 44.545  39.002  38.455  1.000 120.217 ? 137 THR BBB C   1 
ATOM   7470  O O   . THR E 2 137 ? 44.311  39.862  39.342  1.000 125.887 ? 137 THR BBB O   1 
ATOM   7471  C CB  . THR E 2 137 ? 42.497  37.437  38.884  1.000 105.235 ? 137 THR BBB CB  1 
ATOM   7472  O OG1 . THR E 2 137 ? 42.071  38.237  39.992  1.000 112.824 ? 137 THR BBB OG1 1 
ATOM   7473  C CG2 . THR E 2 137 ? 42.042  36.007  39.099  1.000 97.342  ? 137 THR BBB CG2 1 
ATOM   7474  N N   . SER E 2 138 ? 45.244  39.219  37.330  1.000 116.487 ? 138 SER BBB N   1 
ATOM   7475  C CA  . SER E 2 138 ? 46.101  40.389  36.973  1.000 107.976 ? 138 SER BBB CA  1 
ATOM   7476  C C   . SER E 2 138 ? 45.348  41.733  36.987  1.000 102.070 ? 138 SER BBB C   1 
ATOM   7477  O O   . SER E 2 138 ? 45.941  42.726  37.448  1.000 111.607 ? 138 SER BBB O   1 
ATOM   7478  C CB  . SER E 2 138 ? 46.739  40.141  35.618  1.000 99.550  ? 138 SER BBB CB  1 
ATOM   7479  O OG  . SER E 2 138 ? 47.600  41.203  35.247  1.000 93.139  ? 138 SER BBB OG  1 
ATOM   7480  N N   . GLY E 2 139 ? 44.112  41.783  36.478  1.000 102.725 ? 139 GLY BBB N   1 
ATOM   7481  C CA  . GLY E 2 139 ? 43.272  43.000  36.448  1.000 99.982  ? 139 GLY BBB CA  1 
ATOM   7482  C C   . GLY E 2 139 ? 42.404  43.147  37.695  1.000 98.021  ? 139 GLY BBB C   1 
ATOM   7483  O O   . GLY E 2 139 ? 41.983  44.289  37.971  1.000 89.192  ? 139 GLY BBB O   1 
ATOM   7484  N N   . GLY E 2 140 ? 42.113  42.040  38.404  1.000 98.055  ? 140 GLY BBB N   1 
ATOM   7485  C CA  . GLY E 2 140 ? 41.274  41.987  39.621  1.000 79.079  ? 140 GLY BBB CA  1 
ATOM   7486  C C   . GLY E 2 140 ? 42.085  42.247  40.882  1.000 67.442  ? 140 GLY BBB C   1 
ATOM   7487  O O   . GLY E 2 140 ? 43.102  42.960  40.823  1.000 52.596  ? 140 GLY BBB O   1 
ATOM   7488  N N   . THR E 2 141 ? 41.661  41.676  42.003  1.000 62.200  ? 141 THR BBB N   1 
ATOM   7489  C CA  . THR E 2 141 ? 42.180  42.008  43.355  1.000 60.893  ? 141 THR BBB CA  1 
ATOM   7490  C C   . THR E 2 141 ? 43.029  40.839  43.889  1.000 51.952  ? 141 THR BBB C   1 
ATOM   7491  O O   . THR E 2 141 ? 42.821  39.704  43.461  1.000 56.171  ? 141 THR BBB O   1 
ATOM   7492  C CB  . THR E 2 141 ? 41.016  42.431  44.268  1.000 61.981  ? 141 THR BBB CB  1 
ATOM   7493  O OG1 . THR E 2 141 ? 41.568  42.781  45.537  1.000 77.103  ? 141 THR BBB OG1 1 
ATOM   7494  C CG2 . THR E 2 141 ? 39.971  41.359  44.480  1.000 64.942  ? 141 THR BBB CG2 1 
ATOM   7495  N N   . ALA E 2 142 ? 43.977  41.130  44.775  1.000 44.159  ? 142 ALA BBB N   1 
ATOM   7496  C CA  . ALA E 2 142 ? 44.797  40.151  45.518  1.000 44.477  ? 142 ALA BBB CA  1 
ATOM   7497  C C   . ALA E 2 142 ? 44.509  40.287  47.010  1.000 41.202  ? 142 ALA BBB C   1 
ATOM   7498  O O   . ALA E 2 142 ? 44.056  41.340  47.439  1.000 42.102  ? 142 ALA BBB O   1 
ATOM   7499  C CB  . ALA E 2 142 ? 46.261  40.380  45.249  1.000 48.037  ? 142 ALA BBB CB  1 
ATOM   7500  N N   . ALA E 2 143 ? 44.793  39.247  47.777  1.000 38.290  ? 143 ALA BBB N   1 
ATOM   7501  C CA  . ALA E 2 143 ? 44.637  39.249  49.242  1.000 36.576  ? 143 ALA BBB CA  1 
ATOM   7502  C C   . ALA E 2 143 ? 45.990  38.932  49.852  1.000 35.369  ? 143 ALA BBB C   1 
ATOM   7503  O O   . ALA E 2 143 ? 46.744  38.118  49.263  1.000 34.409  ? 143 ALA BBB O   1 
ATOM   7504  C CB  . ALA E 2 143 ? 43.604  38.244  49.684  1.000 38.740  ? 143 ALA BBB CB  1 
ATOM   7505  N N   . LEU E 2 144 ? 46.242  39.552  50.997  1.000 34.156  ? 144 LEU BBB N   1 
ATOM   7506  C CA  . LEU E 2 144 ? 47.440  39.345  51.834  1.000 34.012  ? 144 LEU BBB CA  1 
ATOM   7507  C C   . LEU E 2 144 ? 47.017  39.572  53.281  1.000 32.911  ? 144 LEU BBB C   1 
ATOM   7508  O O   . LEU E 2 144 ? 45.891  40.075  53.499  1.000 32.627  ? 144 LEU BBB O   1 
ATOM   7509  C CB  . LEU E 2 144 ? 48.519  40.332  51.378  1.000 35.751  ? 144 LEU BBB CB  1 
ATOM   7510  C CG  . LEU E 2 144 ? 48.161  41.815  51.523  1.000 35.933  ? 144 LEU BBB CG  1 
ATOM   7511  C CD1 . LEU E 2 144 ? 48.930  42.423  52.676  1.000 39.071  ? 144 LEU BBB CD1 1 
ATOM   7512  C CD2 . LEU E 2 144 ? 48.453  42.588  50.253  1.000 33.605  ? 144 LEU BBB CD2 1 
ATOM   7513  N N   . GLY E 2 145 ? 47.874  39.220  54.234  1.000 31.742  ? 145 GLY BBB N   1 
ATOM   7514  C CA  . GLY E 2 145 ? 47.504  39.344  55.649  1.000 31.592  ? 145 GLY BBB CA  1 
ATOM   7515  C C   . GLY E 2 145 ? 48.624  38.987  56.584  1.000 31.123  ? 145 GLY BBB C   1 
ATOM   7516  O O   . GLY E 2 145 ? 49.716  38.739  56.126  1.000 30.618  ? 145 GLY BBB O   1 
ATOM   7517  N N   . CYS E 2 146 ? 48.299  38.949  57.867  1.000 37.431  ? 146 CYS BBB N   1 
ATOM   7518  C CA  . CYS E 2 146 ? 49.161  38.522  58.989  1.000 40.624  ? 146 CYS BBB CA  1 
ATOM   7519  C C   . CYS E 2 146 ? 48.483  37.400  59.744  1.000 36.358  ? 146 CYS BBB C   1 
ATOM   7520  O O   . CYS E 2 146 ? 47.279  37.428  59.837  1.000 38.742  ? 146 CYS BBB O   1 
ATOM   7521  C CB  . CYS E 2 146 ? 49.394  39.663  59.954  1.000 46.368  ? 146 CYS BBB CB  1 
ATOM   7522  S SG  . CYS E 2 146 ? 50.582  40.797  59.217  1.000 64.354  ? 146 CYS BBB SG  1 
ATOM   7523  N N   . LEU E 2 147 ? 49.282  36.477  60.244  1.000 33.808  ? 147 LEU BBB N   1 
ATOM   7524  C CA  . LEU E 2 147 ? 48.867  35.446  61.204  1.000 32.745  ? 147 LEU BBB CA  1 
ATOM   7525  C C   . LEU E 2 147 ? 49.450  35.851  62.552  1.000 31.205  ? 147 LEU BBB C   1 
ATOM   7526  O O   . LEU E 2 147 ? 50.656  35.914  62.656  1.000 30.902  ? 147 LEU BBB O   1 
ATOM   7527  C CB  . LEU E 2 147 ? 49.393  34.099  60.709  1.000 32.623  ? 147 LEU BBB CB  1 
ATOM   7528  C CG  . LEU E 2 147 ? 48.982  32.901  61.554  1.000 33.364  ? 147 LEU BBB CG  1 
ATOM   7529  C CD1 . LEU E 2 147 ? 47.463  32.736  61.534  1.000 33.638  ? 147 LEU BBB CD1 1 
ATOM   7530  C CD2 . LEU E 2 147 ? 49.709  31.657  61.071  1.000 32.849  ? 147 LEU BBB CD2 1 
ATOM   7531  N N   . VAL E 2 148 ? 48.604  36.215  63.503  1.000 32.206  ? 148 VAL BBB N   1 
ATOM   7532  C CA  . VAL E 2 148 ? 49.012  36.593  64.880  1.000 30.948  ? 148 VAL BBB CA  1 
ATOM   7533  C C   . VAL E 2 148 ? 48.765  35.359  65.736  1.000 32.054  ? 148 VAL BBB C   1 
ATOM   7534  O O   . VAL E 2 148 ? 47.603  35.108  66.086  1.000 31.322  ? 148 VAL BBB O   1 
ATOM   7535  C CB  . VAL E 2 148 ? 48.237  37.825  65.372  1.000 30.038  ? 148 VAL BBB CB  1 
ATOM   7536  C CG1 . VAL E 2 148 ? 48.766  38.317  66.712  1.000 31.873  ? 148 VAL BBB CG1 1 
ATOM   7537  C CG2 . VAL E 2 148 ? 48.274  38.941  64.349  1.000 28.800  ? 148 VAL BBB CG2 1 
ATOM   7538  N N   . LYS E 2 149 ? 49.831  34.605  66.006  1.000 37.417  ? 149 LYS BBB N   1 
ATOM   7539  C CA  . LYS E 2 149 ? 49.776  33.217  66.537  1.000 40.624  ? 149 LYS BBB CA  1 
ATOM   7540  C C   . LYS E 2 149 ? 50.427  33.148  67.928  1.000 37.364  ? 149 LYS BBB C   1 
ATOM   7541  O O   . LYS E 2 149 ? 51.455  33.775  68.155  1.000 34.438  ? 149 LYS BBB O   1 
ATOM   7542  C CB  . LYS E 2 149 ? 50.453  32.267  65.544  1.000 42.598  ? 149 LYS BBB CB  1 
ATOM   7543  C CG  . LYS E 2 149 ? 50.078  30.805  65.696  1.000 48.693  ? 149 LYS BBB CG  1 
ATOM   7544  C CD  . LYS E 2 149 ? 50.903  29.867  64.824  1.000 56.032  ? 149 LYS BBB CD  1 
ATOM   7545  C CE  . LYS E 2 149 ? 51.065  28.478  65.408  1.000 58.507  ? 149 LYS BBB CE  1 
ATOM   7546  N NZ  . LYS E 2 149 ? 49.750  27.872  65.726  1.000 60.390  ? 149 LYS BBB NZ  1 
ATOM   7547  N N   . ASP E 2 150 ? 49.814  32.397  68.829  1.000 38.662  ? 150 ASP BBB N   1 
ATOM   7548  C CA  . ASP E 2 150 ? 50.436  31.917  70.089  1.000 39.716  ? 150 ASP BBB CA  1 
ATOM   7549  C C   . ASP E 2 150 ? 50.655  33.101  71.031  1.000 38.164  ? 150 ASP BBB C   1 
ATOM   7550  O O   . ASP E 2 150 ? 51.830  33.418  71.306  1.000 41.866  ? 150 ASP BBB O   1 
ATOM   7551  C CB  . ASP E 2 150 ? 51.740  31.158  69.823  1.000 38.453  ? 150 ASP BBB CB  1 
ATOM   7552  C CG  . ASP E 2 150 ? 51.570  29.907  68.968  1.000 41.148  ? 150 ASP BBB CG  1 
ATOM   7553  O OD1 . ASP E 2 150 ? 50.447  29.307  68.966  1.000 40.608  ? 150 ASP BBB OD1 1 
ATOM   7554  O OD2 . ASP E 2 150 ? 52.566  29.541  68.291  1.000 45.663  ? 150 ASP BBB OD2 1 
ATOM   7555  N N   . TYR E 2 151 ? 49.567  33.711  71.509  1.000 33.506  ? 151 TYR BBB N   1 
ATOM   7556  C CA  . TYR E 2 151 ? 49.607  34.800  72.512  1.000 31.759  ? 151 TYR BBB CA  1 
ATOM   7557  C C   . TYR E 2 151 ? 48.605  34.507  73.630  1.000 31.489  ? 151 TYR BBB C   1 
ATOM   7558  O O   . TYR E 2 151 ? 47.659  33.733  73.434  1.000 30.891  ? 151 TYR BBB O   1 
ATOM   7559  C CB  . TYR E 2 151 ? 49.362  36.165  71.855  1.000 30.508  ? 151 TYR BBB CB  1 
ATOM   7560  C CG  . TYR E 2 151 ? 47.977  36.408  71.303  1.000 28.745  ? 151 TYR BBB CG  1 
ATOM   7561  C CD1 . TYR E 2 151 ? 47.655  36.087  70.000  1.000 27.955  ? 151 TYR BBB CD1 1 
ATOM   7562  C CD2 . TYR E 2 151 ? 46.992  36.992  72.073  1.000 30.406  ? 151 TYR BBB CD2 1 
ATOM   7563  C CE1 . TYR E 2 151 ? 46.394  36.316  69.479  1.000 27.844  ? 151 TYR BBB CE1 1 
ATOM   7564  C CE2 . TYR E 2 151 ? 45.717  37.223  71.577  1.000 31.149  ? 151 TYR BBB CE2 1 
ATOM   7565  C CZ  . TYR E 2 151 ? 45.413  36.882  70.271  1.000 30.224  ? 151 TYR BBB CZ  1 
ATOM   7566  O OH  . TYR E 2 151 ? 44.161  37.126  69.765  1.000 31.237  ? 151 TYR BBB OH  1 
ATOM   7567  N N   . PHE E 2 152 ? 48.821  35.154  74.772  1.000 32.571  ? 152 PHE BBB N   1 
ATOM   7568  C CA  . PHE E 2 152 ? 47.957  35.098  75.974  1.000 33.540  ? 152 PHE BBB CA  1 
ATOM   7569  C C   . PHE E 2 152 ? 48.274  36.300  76.851  1.000 32.414  ? 152 PHE BBB C   1 
ATOM   7570  O O   . PHE E 2 152 ? 49.430  36.676  76.977  1.000 32.027  ? 152 PHE BBB O   1 
ATOM   7571  C CB  . PHE E 2 152 ? 48.193  33.805  76.761  1.000 35.553  ? 152 PHE BBB CB  1 
ATOM   7572  C CG  . PHE E 2 152 ? 47.256  33.635  77.934  1.000 36.169  ? 152 PHE BBB CG  1 
ATOM   7573  C CD1 . PHE E 2 152 ? 46.027  33.016  77.773  1.000 36.574  ? 152 PHE BBB CD1 1 
ATOM   7574  C CD2 . PHE E 2 152 ? 47.579  34.129  79.190  1.000 36.390  ? 152 PHE BBB CD2 1 
ATOM   7575  C CE1 . PHE E 2 152 ? 45.148  32.895  78.837  1.000 35.038  ? 152 PHE BBB CE1 1 
ATOM   7576  C CE2 . PHE E 2 152 ? 46.706  33.995  80.257  1.000 33.648  ? 152 PHE BBB CE2 1 
ATOM   7577  C CZ  . PHE E 2 152 ? 45.494  33.376  80.076  1.000 33.595  ? 152 PHE BBB CZ  1 
ATOM   7578  N N   . PRO E 2 153 ? 47.280  36.931  77.499  1.000 34.788  ? 153 PRO BBB N   1 
ATOM   7579  C CA  . PRO E 2 153 ? 45.874  36.628  77.260  1.000 38.279  ? 153 PRO BBB CA  1 
ATOM   7580  C C   . PRO E 2 153 ? 45.344  37.379  76.031  1.000 41.919  ? 153 PRO BBB C   1 
ATOM   7581  O O   . PRO E 2 153 ? 46.131  37.911  75.278  1.000 42.343  ? 153 PRO BBB O   1 
ATOM   7582  C CB  . PRO E 2 153 ? 45.223  37.119  78.564  1.000 40.908  ? 153 PRO BBB CB  1 
ATOM   7583  C CG  . PRO E 2 153 ? 46.060  38.320  78.956  1.000 39.952  ? 153 PRO BBB CG  1 
ATOM   7584  C CD  . PRO E 2 153 ? 47.473  37.940  78.555  1.000 37.534  ? 153 PRO BBB CD  1 
ATOM   7585  N N   . GLU E 2 154 ? 44.027  37.376  75.839  1.000 45.631  ? 154 GLU BBB N   1 
ATOM   7586  C CA  . GLU E 2 154 ? 43.336  38.351  74.959  1.000 45.032  ? 154 GLU BBB CA  1 
ATOM   7587  C C   . GLU E 2 154 ? 43.437  39.731  75.604  1.000 43.011  ? 154 GLU BBB C   1 
ATOM   7588  O O   . GLU E 2 154 ? 43.580  39.821  76.832  1.000 41.590  ? 154 GLU BBB O   1 
ATOM   7589  C CB  . GLU E 2 154 ? 41.877  37.928  74.801  1.000 50.404  ? 154 GLU BBB CB  1 
ATOM   7590  C CG  . GLU E 2 154 ? 41.683  36.782  73.837  1.000 51.787  ? 154 GLU BBB CG  1 
ATOM   7591  C CD  . GLU E 2 154 ? 41.241  37.253  72.465  1.000 57.397  ? 154 GLU BBB CD  1 
ATOM   7592  O OE1 . GLU E 2 154 ? 41.926  38.150  71.853  1.000 56.652  ? 154 GLU BBB OE1 1 
ATOM   7593  O OE2 . GLU E 2 154 ? 40.162  36.786  72.052  1.000 60.219  ? 154 GLU BBB OE2 1 
ATOM   7594  N N   . PRO E 2 155 ? 43.354  40.849  74.839  1.000 40.539  ? 155 PRO BBB N   1 
ATOM   7595  C CA  . PRO E 2 155 ? 43.343  40.856  73.372  1.000 39.600  ? 155 PRO BBB CA  1 
ATOM   7596  C C   . PRO E 2 155 ? 44.601  41.380  72.647  1.000 38.481  ? 155 PRO BBB C   1 
ATOM   7597  O O   . PRO E 2 155 ? 45.520  41.832  73.293  1.000 38.689  ? 155 PRO BBB O   1 
ATOM   7598  C CB  . PRO E 2 155 ? 42.241  41.897  73.156  1.000 38.064  ? 155 PRO BBB CB  1 
ATOM   7599  C CG  . PRO E 2 155 ? 42.500  42.945  74.232  1.000 36.427  ? 155 PRO BBB CG  1 
ATOM   7600  C CD  . PRO E 2 155 ? 43.143  42.199  75.382  1.000 37.407  ? 155 PRO BBB CD  1 
ATOM   7601  N N   . VAL E 2 156 ? 44.602  41.356  71.311  1.000 34.048  ? 156 VAL BBB N   1 
ATOM   7602  C CA  . VAL E 2 156 ? 45.591  42.088  70.468  1.000 32.527  ? 156 VAL BBB CA  1 
ATOM   7603  C C   . VAL E 2 156 ? 44.829  43.097  69.626  1.000 33.220  ? 156 VAL BBB C   1 
ATOM   7604  O O   . VAL E 2 156 ? 43.668  42.860  69.402  1.000 40.412  ? 156 VAL BBB O   1 
ATOM   7605  C CB  . VAL E 2 156 ? 46.408  41.159  69.560  1.000 31.315  ? 156 VAL BBB CB  1 
ATOM   7606  C CG1 . VAL E 2 156 ? 47.358  40.321  70.381  1.000 32.573  ? 156 VAL BBB CG1 1 
ATOM   7607  C CG2 . VAL E 2 156 ? 45.540  40.287  68.671  1.000 31.506  ? 156 VAL BBB CG2 1 
ATOM   7608  N N   . THR E 2 157 ? 45.468  44.183  69.212  1.000 35.654  ? 157 THR BBB N   1 
ATOM   7609  C CA  . THR E 2 157 ? 44.972  45.103  68.156  1.000 37.474  ? 157 THR BBB CA  1 
ATOM   7610  C C   . THR E 2 157 ? 45.829  44.851  66.917  1.000 32.097  ? 157 THR BBB C   1 
ATOM   7611  O O   . THR E 2 157 ? 47.040  44.732  67.046  1.000 31.519  ? 157 THR BBB O   1 
ATOM   7612  C CB  . THR E 2 157 ? 45.005  46.588  68.571  1.000 42.681  ? 157 THR BBB CB  1 
ATOM   7613  O OG1 . THR E 2 157 ? 46.361  47.019  68.481  1.000 51.160  ? 157 THR BBB OG1 1 
ATOM   7614  C CG2 . THR E 2 157 ? 44.480  46.870  69.965  1.000 44.302  ? 157 THR BBB CG2 1 
ATOM   7615  N N   . VAL E 2 158 ? 45.190  44.757  65.763  1.000 30.575  ? 158 VAL BBB N   1 
ATOM   7616  C CA  . VAL E 2 158 ? 45.841  44.669  64.431  1.000 30.032  ? 158 VAL BBB CA  1 
ATOM   7617  C C   . VAL E 2 158 ? 45.303  45.813  63.579  1.000 31.274  ? 158 VAL BBB C   1 
ATOM   7618  O O   . VAL E 2 158 ? 44.103  45.848  63.321  1.000 33.576  ? 158 VAL BBB O   1 
ATOM   7619  C CB  . VAL E 2 158 ? 45.565  43.319  63.759  1.000 29.814  ? 158 VAL BBB CB  1 
ATOM   7620  C CG1 . VAL E 2 158 ? 46.277  43.230  62.430  1.000 30.981  ? 158 VAL BBB CG1 1 
ATOM   7621  C CG2 . VAL E 2 158 ? 45.957  42.166  64.657  1.000 31.145  ? 158 VAL BBB CG2 1 
ATOM   7622  N N   . SER E 2 159 ? 46.175  46.742  63.213  1.000 34.016  ? 159 SER BBB N   1 
ATOM   7623  C CA  . SER E 2 159 ? 45.940  47.807  62.205  1.000 34.916  ? 159 SER BBB CA  1 
ATOM   7624  C C   . SER E 2 159 ? 46.931  47.566  61.065  1.000 32.892  ? 159 SER BBB C   1 
ATOM   7625  O O   . SER E 2 159 ? 47.740  46.641  61.188  1.000 27.652  ? 159 SER BBB O   1 
ATOM   7626  C CB  . SER E 2 159 ? 46.089  49.176  62.815  1.000 36.369  ? 159 SER BBB CB  1 
ATOM   7627  O OG  . SER E 2 159 ? 47.292  49.233  63.574  1.000 40.212  ? 159 SER BBB OG  1 
ATOM   7628  N N   . TRP E 2 160 ? 46.831  48.350  59.988  1.000 33.256  ? 160 TRP BBB N   1 
ATOM   7629  C CA  . TRP E 2 160 ? 47.592  48.179  58.717  1.000 32.581  ? 160 TRP BBB CA  1 
ATOM   7630  C C   . TRP E 2 160 ? 48.176  49.525  58.266  1.000 33.186  ? 160 TRP BBB C   1 
ATOM   7631  O O   . TRP E 2 160 ? 47.426  50.495  58.192  1.000 31.949  ? 160 TRP BBB O   1 
ATOM   7632  C CB  . TRP E 2 160 ? 46.686  47.597  57.625  1.000 31.772  ? 160 TRP BBB CB  1 
ATOM   7633  C CG  . TRP E 2 160 ? 46.471  46.126  57.738  1.000 29.458  ? 160 TRP BBB CG  1 
ATOM   7634  C CD1 . TRP E 2 160 ? 45.445  45.490  58.357  1.000 29.357  ? 160 TRP BBB CD1 1 
ATOM   7635  C CD2 . TRP E 2 160 ? 47.306  45.101  57.195  1.000 29.979  ? 160 TRP BBB CD2 1 
ATOM   7636  N NE1 . TRP E 2 160 ? 45.597  44.137  58.250  1.000 30.415  ? 160 TRP BBB NE1 1 
ATOM   7637  C CE2 . TRP E 2 160 ? 46.722  43.867  57.530  1.000 29.551  ? 160 TRP BBB CE2 1 
ATOM   7638  C CE3 . TRP E 2 160 ? 48.492  45.101  56.453  1.000 32.666  ? 160 TRP BBB CE3 1 
ATOM   7639  C CZ2 . TRP E 2 160 ? 47.287  42.651  57.160  1.000 30.361  ? 160 TRP BBB CZ2 1 
ATOM   7640  C CZ3 . TRP E 2 160 ? 49.060  43.898  56.094  1.000 31.109  ? 160 TRP BBB CZ3 1 
ATOM   7641  C CH2 . TRP E 2 160 ? 48.459  42.691  56.438  1.000 30.751  ? 160 TRP BBB CH2 1 
ATOM   7642  N N   . ASN E 2 161 ? 49.462  49.557  57.918  1.000 34.489  ? 161 ASN BBB N   1 
ATOM   7643  C CA  . ASN E 2 161 ? 50.166  50.754  57.387  1.000 33.655  ? 161 ASN BBB CA  1 
ATOM   7644  C C   . ASN E 2 161 ? 50.045  51.878  58.431  1.000 32.939  ? 161 ASN BBB C   1 
ATOM   7645  O O   . ASN E 2 161 ? 49.781  53.029  58.060  1.000 33.775  ? 161 ASN BBB O   1 
ATOM   7646  C CB  . ASN E 2 161 ? 49.639  51.080  55.982  1.000 32.660  ? 161 ASN BBB CB  1 
ATOM   7647  C CG  . ASN E 2 161 ? 50.034  50.073  54.923  1.000 31.673  ? 161 ASN BBB CG  1 
ATOM   7648  O OD1 . ASN E 2 161 ? 50.960  49.312  55.115  1.000 36.029  ? 161 ASN BBB OD1 1 
ATOM   7649  N ND2 . ASN E 2 161 ? 49.395  50.101  53.772  1.000 30.113  ? 161 ASN BBB ND2 1 
ATOM   7650  N N   . SER E 2 162 ? 50.249  51.546  59.701  1.000 32.160  ? 162 SER BBB N   1 
ATOM   7651  C CA  . SER E 2 162 ? 50.133  52.461  60.871  1.000 32.891  ? 162 SER BBB CA  1 
ATOM   7652  C C   . SER E 2 162 ? 48.744  53.087  60.951  1.000 33.186  ? 162 SER BBB C   1 
ATOM   7653  O O   . SER E 2 162 ? 48.671  54.211  61.428  1.000 35.642  ? 162 SER BBB O   1 
ATOM   7654  C CB  . SER E 2 162 ? 51.178  53.539  60.845  1.000 30.704  ? 162 SER BBB CB  1 
ATOM   7655  O OG  . SER E 2 162 ? 52.460  52.957  60.748  1.000 32.774  ? 162 SER BBB OG  1 
ATOM   7656  N N   . GLY E 2 163 ? 47.692  52.391  60.519  1.000 33.728  ? 163 GLY BBB N   1 
ATOM   7657  C CA  . GLY E 2 163 ? 46.299  52.884  60.616  1.000 35.202  ? 163 GLY BBB CA  1 
ATOM   7658  C C   . GLY E 2 163 ? 45.800  53.549  59.338  1.000 33.341  ? 163 GLY BBB C   1 
ATOM   7659  O O   . GLY E 2 163 ? 44.592  53.812  59.254  1.000 34.703  ? 163 GLY BBB O   1 
ATOM   7660  N N   . ALA E 2 164 ? 46.688  53.787  58.373  1.000 32.927  ? 164 ALA BBB N   1 
ATOM   7661  C CA  . ALA E 2 164 ? 46.394  54.423  57.068  1.000 36.343  ? 164 ALA BBB CA  1 
ATOM   7662  C C   . ALA E 2 164 ? 45.369  53.593  56.294  1.000 39.599  ? 164 ALA BBB C   1 
ATOM   7663  O O   . ALA E 2 164 ? 44.420  54.198  55.779  1.000 47.908  ? 164 ALA BBB O   1 
ATOM   7664  C CB  . ALA E 2 164 ? 47.660  54.601  56.261  1.000 36.002  ? 164 ALA BBB CB  1 
ATOM   7665  N N   . LEU E 2 165 ? 45.564  52.271  56.237  1.000 38.946  ? 165 LEU BBB N   1 
ATOM   7666  C CA  . LEU E 2 165 ? 44.733  51.297  55.475  1.000 38.217  ? 165 LEU BBB CA  1 
ATOM   7667  C C   . LEU E 2 165 ? 43.701  50.640  56.397  1.000 37.591  ? 165 LEU BBB C   1 
ATOM   7668  O O   . LEU E 2 165 ? 44.109  49.931  57.350  1.000 37.689  ? 165 LEU BBB O   1 
ATOM   7669  C CB  . LEU E 2 165 ? 45.678  50.259  54.868  1.000 40.212  ? 165 LEU BBB CB  1 
ATOM   7670  C CG  . LEU E 2 165 ? 45.067  49.052  54.157  1.000 39.424  ? 165 LEU BBB CG  1 
ATOM   7671  C CD1 . LEU E 2 165 ? 44.122  49.455  53.040  1.000 41.689  ? 165 LEU BBB CD1 1 
ATOM   7672  C CD2 . LEU E 2 165 ? 46.173  48.168  53.606  1.000 36.937  ? 165 LEU BBB CD2 1 
ATOM   7673  N N   . THR E 2 166 ? 42.418  50.873  56.116  1.000 39.505  ? 166 THR BBB N   1 
ATOM   7674  C CA  . THR E 2 166 ? 41.270  50.294  56.870  1.000 44.899  ? 166 THR BBB CA  1 
ATOM   7675  C C   . THR E 2 166 ? 40.261  49.659  55.906  1.000 44.337  ? 166 THR BBB C   1 
ATOM   7676  O O   . THR E 2 166 ? 39.532  48.725  56.337  1.000 44.852  ? 166 THR BBB O   1 
ATOM   7677  C CB  . THR E 2 166 ? 40.563  51.351  57.723  1.000 46.103  ? 166 THR BBB CB  1 
ATOM   7678  O OG1 . THR E 2 166 ? 39.976  52.262  56.799  1.000 56.879  ? 166 THR BBB OG1 1 
ATOM   7679  C CG2 . THR E 2 166 ? 41.477  52.098  58.667  1.000 45.345  ? 166 THR BBB CG2 1 
ATOM   7680  N N   . SER E 2 167 ? 40.223  50.143  54.663  1.000 43.903  ? 167 SER BBB N   1 
ATOM   7681  C CA  . SER E 2 167 ? 39.304  49.647  53.616  1.000 44.634  ? 167 SER BBB CA  1 
ATOM   7682  C C   . SER E 2 167 ? 39.665  48.202  53.239  1.000 38.963  ? 167 SER BBB C   1 
ATOM   7683  O O   . SER E 2 167 ? 40.829  47.925  52.920  1.000 40.727  ? 167 SER BBB O   1 
ATOM   7684  C CB  . SER E 2 167 ? 39.317  50.551  52.423  1.000 48.601  ? 167 SER BBB CB  1 
ATOM   7685  O OG  . SER E 2 167 ? 38.340  50.108  51.493  1.000 55.386  ? 167 SER BBB OG  1 
ATOM   7686  N N   . GLY E 2 168 ? 38.689  47.307  53.291  1.000 34.350  ? 168 GLY BBB N   1 
ATOM   7687  C CA  . GLY E 2 168 ? 38.836  45.921  52.820  1.000 34.506  ? 168 GLY BBB CA  1 
ATOM   7688  C C   . GLY E 2 168 ? 39.609  45.064  53.799  1.000 34.030  ? 168 GLY BBB C   1 
ATOM   7689  O O   . GLY E 2 168 ? 40.007  43.949  53.391  1.000 35.424  ? 168 GLY BBB O   1 
ATOM   7690  N N   . VAL E 2 169 ? 39.793  45.540  55.038  1.000 33.103  ? 169 VAL BBB N   1 
ATOM   7691  C CA  . VAL E 2 169 ? 40.457  44.762  56.129  1.000 31.873  ? 169 VAL BBB CA  1 
ATOM   7692  C C   . VAL E 2 169 ? 39.429  43.870  56.828  1.000 30.854  ? 169 VAL BBB C   1 
ATOM   7693  O O   . VAL E 2 169 ? 38.345  44.350  57.127  1.000 32.729  ? 169 VAL BBB O   1 
ATOM   7694  C CB  . VAL E 2 169 ? 41.157  45.680  57.145  1.000 31.620  ? 169 VAL BBB CB  1 
ATOM   7695  C CG1 . VAL E 2 169 ? 41.776  44.878  58.282  1.000 31.716  ? 169 VAL BBB CG1 1 
ATOM   7696  C CG2 . VAL E 2 169 ? 42.206  46.559  56.473  1.000 32.176  ? 169 VAL BBB CG2 1 
ATOM   7697  N N   . HIS E 2 170 ? 39.792  42.624  57.102  1.000 31.182  ? 170 HIS BBB N   1 
ATOM   7698  C CA  . HIS E 2 170 ? 39.039  41.687  57.976  1.000 31.386  ? 170 HIS BBB CA  1 
ATOM   7699  C C   . HIS E 2 170 ? 39.997  41.135  59.033  1.000 30.507  ? 170 HIS BBB C   1 
ATOM   7700  O O   . HIS E 2 170 ? 40.917  40.357  58.655  1.000 30.690  ? 170 HIS BBB O   1 
ATOM   7701  C CB  . HIS E 2 170 ? 38.426  40.553  57.146  1.000 32.384  ? 170 HIS BBB CB  1 
ATOM   7702  C CG  . HIS E 2 170 ? 37.365  40.994  56.206  1.000 33.672  ? 170 HIS BBB CG  1 
ATOM   7703  N ND1 . HIS E 2 170 ? 36.175  41.551  56.643  1.000 34.694  ? 170 HIS BBB ND1 1 
ATOM   7704  C CD2 . HIS E 2 170 ? 37.295  40.919  54.861  1.000 34.699  ? 170 HIS BBB CD2 1 
ATOM   7705  C CE1 . HIS E 2 170 ? 35.426  41.834  55.594  1.000 37.200  ? 170 HIS BBB CE1 1 
ATOM   7706  N NE2 . HIS E 2 170 ? 36.082  41.426  54.484  1.000 36.320  ? 170 HIS BBB NE2 1 
ATOM   7707  N N   . THR E 2 171 ? 39.828  41.548  60.290  1.000 28.618  ? 171 THR BBB N   1 
ATOM   7708  C CA  . THR E 2 171 ? 40.532  40.925  61.441  1.000 29.343  ? 171 THR BBB CA  1 
ATOM   7709  C C   . THR E 2 171 ? 39.566  39.905  62.055  1.000 28.910  ? 171 THR BBB C   1 
ATOM   7710  O O   . THR E 2 171 ? 38.575  40.311  62.653  1.000 30.321  ? 171 THR BBB O   1 
ATOM   7711  C CB  . THR E 2 171 ? 41.031  41.956  62.467  1.000 29.796  ? 171 THR BBB CB  1 
ATOM   7712  O OG1 . THR E 2 171 ? 41.917  42.893  61.845  1.000 30.125  ? 171 THR BBB OG1 1 
ATOM   7713  C CG2 . THR E 2 171 ? 41.748  41.308  63.629  1.000 29.745  ? 171 THR BBB CG2 1 
ATOM   7714  N N   . PHE E 2 172 ? 39.857  38.621  61.909  1.000 26.722  ? 172 PHE BBB N   1 
ATOM   7715  C CA  . PHE E 2 172 ? 39.014  37.508  62.401  1.000 25.147  ? 172 PHE BBB CA  1 
ATOM   7716  C C   . PHE E 2 172 ? 39.082  37.439  63.922  1.000 26.057  ? 172 PHE BBB C   1 
ATOM   7717  O O   . PHE E 2 172 ? 40.022  37.926  64.551  1.000 26.445  ? 172 PHE BBB O   1 
ATOM   7718  C CB  . PHE E 2 172 ? 39.459  36.183  61.776  1.000 26.285  ? 172 PHE BBB CB  1 
ATOM   7719  C CG  . PHE E 2 172 ? 39.185  36.127  60.300  1.000 25.903  ? 172 PHE BBB CG  1 
ATOM   7720  C CD1 . PHE E 2 172 ? 40.184  36.405  59.391  1.000 26.813  ? 172 PHE BBB CD1 1 
ATOM   7721  C CD2 . PHE E 2 172 ? 37.914  35.875  59.833  1.000 26.787  ? 172 PHE BBB CD2 1 
ATOM   7722  C CE1 . PHE E 2 172 ? 39.927  36.422  58.035  1.000 28.006  ? 172 PHE BBB CE1 1 
ATOM   7723  C CE2 . PHE E 2 172 ? 37.656  35.863  58.477  1.000 28.323  ? 172 PHE BBB CE2 1 
ATOM   7724  C CZ  . PHE E 2 172 ? 38.658  36.158  57.584  1.000 29.556  ? 172 PHE BBB CZ  1 
ATOM   7725  N N   . PRO E 2 173 ? 38.047  36.841  64.551  1.000 26.523  ? 173 PRO BBB N   1 
ATOM   7726  C CA  . PRO E 2 173 ? 38.071  36.502  65.967  1.000 26.860  ? 173 PRO BBB CA  1 
ATOM   7727  C C   . PRO E 2 173 ? 39.201  35.545  66.312  1.000 29.601  ? 173 PRO BBB C   1 
ATOM   7728  O O   . PRO E 2 173 ? 39.467  34.639  65.553  1.000 32.152  ? 173 PRO BBB O   1 
ATOM   7729  C CB  . PRO E 2 173 ? 36.771  35.740  66.182  1.000 26.041  ? 173 PRO BBB CB  1 
ATOM   7730  C CG  . PRO E 2 173 ? 35.875  36.301  65.130  1.000 26.374  ? 173 PRO BBB CG  1 
ATOM   7731  C CD  . PRO E 2 173 ? 36.775  36.461  63.930  1.000 26.581  ? 173 PRO BBB CD  1 
ATOM   7732  N N   . ALA E 2 174 ? 39.834  35.773  67.448  1.000 34.275  ? 174 ALA BBB N   1 
ATOM   7733  C CA  . ALA E 2 174 ? 40.828  34.823  67.979  1.000 40.256  ? 174 ALA BBB CA  1 
ATOM   7734  C C   . ALA E 2 174 ? 40.125  33.495  68.220  1.000 41.684  ? 174 ALA BBB C   1 
ATOM   7735  O O   . ALA E 2 174 ? 38.931  33.528  68.550  1.000 43.120  ? 174 ALA BBB O   1 
ATOM   7736  C CB  . ALA E 2 174 ? 41.427  35.354  69.248  1.000 46.316  ? 174 ALA BBB CB  1 
ATOM   7737  N N   . VAL E 2 175 ? 40.841  32.391  68.028  1.000 44.225  ? 175 VAL BBB N   1 
ATOM   7738  C CA  . VAL E 2 175 ? 40.445  31.041  68.518  1.000 45.172  ? 175 VAL BBB CA  1 
ATOM   7739  C C   . VAL E 2 175 ? 41.419  30.683  69.634  1.000 45.175  ? 175 VAL BBB C   1 
ATOM   7740  O O   . VAL E 2 175 ? 42.604  31.072  69.564  1.000 42.864  ? 175 VAL BBB O   1 
ATOM   7741  C CB  . VAL E 2 175 ? 40.447  29.989  67.396  1.000 48.700  ? 175 VAL BBB CB  1 
ATOM   7742  C CG1 . VAL E 2 175 ? 39.691  30.500  66.178  1.000 52.014  ? 175 VAL BBB CG1 1 
ATOM   7743  C CG2 . VAL E 2 175 ? 41.860  29.555  67.007  1.000 52.534  ? 175 VAL BBB CG2 1 
ATOM   7744  N N   . LEU E 2 176 ? 40.918  29.988  70.642  1.000 46.765  ? 176 LEU BBB N   1 
ATOM   7745  C CA  . LEU E 2 176 ? 41.747  29.366  71.692  1.000 44.906  ? 176 LEU BBB CA  1 
ATOM   7746  C C   . LEU E 2 176 ? 42.242  28.029  71.140  1.000 46.537  ? 176 LEU BBB C   1 
ATOM   7747  O O   . LEU E 2 176 ? 41.400  27.149  70.871  1.000 45.016  ? 176 LEU BBB O   1 
ATOM   7748  C CB  . LEU E 2 176 ? 40.838  29.206  72.906  1.000 43.020  ? 176 LEU BBB CB  1 
ATOM   7749  C CG  . LEU E 2 176 ? 41.495  28.829  74.222  1.000 43.983  ? 176 LEU BBB CG  1 
ATOM   7750  C CD1 . LEU E 2 176 ? 42.824  29.541  74.452  1.000 44.847  ? 176 LEU BBB CD1 1 
ATOM   7751  C CD2 . LEU E 2 176 ? 40.513  29.159  75.343  1.000 46.277  ? 176 LEU BBB CD2 1 
ATOM   7752  N N   . GLN E 2 177 ? 43.542  27.915  70.875  1.000 49.628  ? 177 GLN BBB N   1 
ATOM   7753  C CA  . GLN E 2 177 ? 44.163  26.652  70.392  1.000 53.848  ? 177 GLN BBB CA  1 
ATOM   7754  C C   . GLN E 2 177 ? 44.246  25.674  71.571  1.000 54.249  ? 177 GLN BBB C   1 
ATOM   7755  O O   . GLN E 2 177 ? 44.116  26.137  72.719  1.000 56.396  ? 177 GLN BBB O   1 
ATOM   7756  C CB  . GLN E 2 177 ? 45.548  26.916  69.798  1.000 53.205  ? 177 GLN BBB CB  1 
ATOM   7757  C CG  . GLN E 2 177 ? 45.534  27.855  68.601  1.000 52.042  ? 177 GLN BBB CG  1 
ATOM   7758  C CD  . GLN E 2 177 ? 46.925  28.343  68.266  1.000 54.887  ? 177 GLN BBB CD  1 
ATOM   7759  O OE1 . GLN E 2 177 ? 47.356  28.269  67.120  1.000 60.012  ? 177 GLN BBB OE1 1 
ATOM   7760  N NE2 . GLN E 2 177 ? 47.651  28.835  69.260  1.000 50.655  ? 177 GLN BBB NE2 1 
ATOM   7761  N N   . SER E 2 178 ? 44.483  24.385  71.311  1.000 56.496  ? 178 SER BBB N   1 
ATOM   7762  C CA  . SER E 2 178 ? 44.561  23.332  72.359  1.000 56.273  ? 178 SER BBB CA  1 
ATOM   7763  C C   . SER E 2 178 ? 45.792  23.557  73.252  1.000 54.386  ? 178 SER BBB C   1 
ATOM   7764  O O   . SER E 2 178 ? 45.798  23.013  74.364  1.000 58.264  ? 178 SER BBB O   1 
ATOM   7765  C CB  . SER E 2 178 ? 44.540  21.952  71.753  1.000 57.195  ? 178 SER BBB CB  1 
ATOM   7766  O OG  . SER E 2 178 ? 45.535  21.840  70.754  1.000 59.554  ? 178 SER BBB OG  1 
ATOM   7767  N N   . SER E 2 179 ? 46.770  24.365  72.815  1.000 52.206  ? 179 SER BBB N   1 
ATOM   7768  C CA  . SER E 2 179 ? 47.950  24.787  73.622  1.000 47.926  ? 179 SER BBB CA  1 
ATOM   7769  C C   . SER E 2 179 ? 47.558  25.808  74.701  1.000 45.097  ? 179 SER BBB C   1 
ATOM   7770  O O   . SER E 2 179 ? 48.418  26.158  75.521  1.000 42.730  ? 179 SER BBB O   1 
ATOM   7771  C CB  . SER E 2 179 ? 49.052  25.341  72.738  1.000 47.482  ? 179 SER BBB CB  1 
ATOM   7772  O OG  . SER E 2 179 ? 48.635  26.500  72.030  1.000 43.121  ? 179 SER BBB OG  1 
ATOM   7773  N N   . GLY E 2 180 ? 46.323  26.308  74.684  1.000 45.537  ? 180 GLY BBB N   1 
ATOM   7774  C CA  . GLY E 2 180 ? 45.831  27.304  75.655  1.000 47.665  ? 180 GLY BBB CA  1 
ATOM   7775  C C   . GLY E 2 180 ? 46.214  28.723  75.262  1.000 46.823  ? 180 GLY BBB C   1 
ATOM   7776  O O   . GLY E 2 180 ? 45.834  29.681  76.006  1.000 48.269  ? 180 GLY BBB O   1 
ATOM   7777  N N   . LEU E 2 181 ? 46.938  28.852  74.144  1.000 41.587  ? 181 LEU BBB N   1 
ATOM   7778  C CA  . LEU E 2 181 ? 47.348  30.133  73.513  1.000 37.859  ? 181 LEU BBB CA  1 
ATOM   7779  C C   . LEU E 2 181 ? 46.335  30.500  72.428  1.000 36.967  ? 181 LEU BBB C   1 
ATOM   7780  O O   . LEU E 2 181 ? 45.837  29.592  71.749  1.000 40.157  ? 181 LEU BBB O   1 
ATOM   7781  C CB  . LEU E 2 181 ? 48.738  29.963  72.903  1.000 36.914  ? 181 LEU BBB CB  1 
ATOM   7782  C CG  . LEU E 2 181 ? 49.869  29.654  73.888  1.000 38.353  ? 181 LEU BBB CG  1 
ATOM   7783  C CD1 . LEU E 2 181 ? 51.217  29.635  73.195  1.000 39.297  ? 181 LEU BBB CD1 1 
ATOM   7784  C CD2 . LEU E 2 181 ? 49.924  30.670  75.018  1.000 40.206  ? 181 LEU BBB CD2 1 
ATOM   7785  N N   . TYR E 2 182 ? 46.059  31.793  72.270  1.000 36.918  ? 182 TYR BBB N   1 
ATOM   7786  C CA  . TYR E 2 182 ? 45.125  32.346  71.257  1.000 34.609  ? 182 TYR BBB CA  1 
ATOM   7787  C C   . TYR E 2 182 ? 45.860  32.585  69.935  1.000 35.173  ? 182 TYR BBB C   1 
ATOM   7788  O O   . TYR E 2 182 ? 47.104  32.665  69.909  1.000 36.475  ? 182 TYR BBB O   1 
ATOM   7789  C CB  . TYR E 2 182 ? 44.513  33.649  71.756  1.000 32.547  ? 182 TYR BBB CB  1 
ATOM   7790  C CG  . TYR E 2 182 ? 43.621  33.482  72.954  1.000 33.478  ? 182 TYR BBB CG  1 
ATOM   7791  C CD1 . TYR E 2 182 ? 44.119  33.628  74.237  1.000 35.474  ? 182 TYR BBB CD1 1 
ATOM   7792  C CD2 . TYR E 2 182 ? 42.273  33.205  72.811  1.000 32.997  ? 182 TYR BBB CD2 1 
ATOM   7793  C CE1 . TYR E 2 182 ? 43.301  33.519  75.350  1.000 37.210  ? 182 TYR BBB CE1 1 
ATOM   7794  C CE2 . TYR E 2 182 ? 41.449  33.066  73.910  1.000 34.228  ? 182 TYR BBB CE2 1 
ATOM   7795  C CZ  . TYR E 2 182 ? 41.965  33.225  75.180  1.000 36.872  ? 182 TYR BBB CZ  1 
ATOM   7796  O OH  . TYR E 2 182 ? 41.151  33.104  76.255  1.000 46.238  ? 182 TYR BBB OH  1 
ATOM   7797  N N   . SER E 2 183 ? 45.088  32.716  68.861  1.000 35.836  ? 183 SER BBB N   1 
ATOM   7798  C CA  . SER E 2 183 ? 45.593  32.796  67.475  1.000 35.924  ? 183 SER BBB CA  1 
ATOM   7799  C C   . SER E 2 183 ? 44.494  33.321  66.556  1.000 34.536  ? 183 SER BBB C   1 
ATOM   7800  O O   . SER E 2 183 ? 43.340  32.900  66.660  1.000 34.647  ? 183 SER BBB O   1 
ATOM   7801  C CB  . SER E 2 183 ? 46.078  31.465  67.007  1.000 39.963  ? 183 SER BBB CB  1 
ATOM   7802  O OG  . SER E 2 183 ? 46.432  31.508  65.639  1.000 46.382  ? 183 SER BBB OG  1 
ATOM   7803  N N   . LEU E 2 184 ? 44.899  34.155  65.622  1.000 34.888  ? 184 LEU BBB N   1 
ATOM   7804  C CA  . LEU E 2 184 ? 44.035  35.133  64.941  1.000 36.735  ? 184 LEU BBB CA  1 
ATOM   7805  C C   . LEU E 2 184 ? 44.736  35.445  63.630  1.000 34.536  ? 184 LEU BBB C   1 
ATOM   7806  O O   . LEU E 2 184 ? 45.961  35.369  63.614  1.000 31.539  ? 184 LEU BBB O   1 
ATOM   7807  C CB  . LEU E 2 184 ? 43.964  36.328  65.893  1.000 40.254  ? 184 LEU BBB CB  1 
ATOM   7808  C CG  . LEU E 2 184 ? 43.362  37.624  65.372  1.000 43.261  ? 184 LEU BBB CG  1 
ATOM   7809  C CD1 . LEU E 2 184 ? 42.858  38.449  66.551  1.000 47.336  ? 184 LEU BBB CD1 1 
ATOM   7810  C CD2 . LEU E 2 184 ? 44.381  38.433  64.589  1.000 44.748  ? 184 LEU BBB CD2 1 
ATOM   7811  N N   . SER E 2 185 ? 44.014  35.704  62.554  1.000 36.463  ? 185 SER BBB N   1 
ATOM   7812  C CA  . SER E 2 185 ? 44.644  36.199  61.305  1.000 38.811  ? 185 SER BBB CA  1 
ATOM   7813  C C   . SER E 2 185 ? 43.865  37.427  60.819  1.000 35.586  ? 185 SER BBB C   1 
ATOM   7814  O O   . SER E 2 185 ? 42.658  37.462  61.021  1.000 33.616  ? 185 SER BBB O   1 
ATOM   7815  C CB  . SER E 2 185 ? 44.826  35.114  60.256  1.000 41.809  ? 185 SER BBB CB  1 
ATOM   7816  O OG  . SER E 2 185 ? 43.711  34.257  60.183  1.000 56.421  ? 185 SER BBB OG  1 
ATOM   7817  N N   . SER E 2 186 ? 44.574  38.445  60.327  1.000 34.108  ? 186 SER BBB N   1 
ATOM   7818  C CA  . SER E 2 186 ? 44.027  39.701  59.757  1.000 32.363  ? 186 SER BBB CA  1 
ATOM   7819  C C   . SER E 2 186 ? 44.374  39.734  58.275  1.000 29.235  ? 186 SER BBB C   1 
ATOM   7820  O O   . SER E 2 186 ? 45.527  39.551  57.940  1.000 28.513  ? 186 SER BBB O   1 
ATOM   7821  C CB  . SER E 2 186 ? 44.568  40.921  60.460  1.000 32.849  ? 186 SER BBB CB  1 
ATOM   7822  O OG  . SER E 2 186 ? 43.934  42.115  59.998  1.000 29.342  ? 186 SER BBB OG  1 
ATOM   7823  N N   . VAL E 2 187 ? 43.391  39.936  57.422  1.000 28.022  ? 187 VAL BBB N   1 
ATOM   7824  C CA  . VAL E 2 187 ? 43.598  39.881  55.954  1.000 29.126  ? 187 VAL BBB CA  1 
ATOM   7825  C C   . VAL E 2 187 ? 43.078  41.195  55.396  1.000 31.712  ? 187 VAL BBB C   1 
ATOM   7826  O O   . VAL E 2 187 ? 42.309  41.869  56.116  1.000 34.406  ? 187 VAL BBB O   1 
ATOM   7827  C CB  . VAL E 2 187 ? 42.873  38.680  55.327  1.000 29.538  ? 187 VAL BBB CB  1 
ATOM   7828  C CG1 . VAL E 2 187 ? 43.399  37.367  55.882  1.000 32.168  ? 187 VAL BBB CG1 1 
ATOM   7829  C CG2 . VAL E 2 187 ? 41.367  38.755  55.526  1.000 30.317  ? 187 VAL BBB CG2 1 
ATOM   7830  N N   . VAL E 2 188 ? 43.481  41.531  54.176  1.000 31.239  ? 188 VAL BBB N   1 
ATOM   7831  C CA  . VAL E 2 188 ? 42.995  42.738  53.458  1.000 30.480  ? 188 VAL BBB CA  1 
ATOM   7832  C C   . VAL E 2 188 ? 43.060  42.433  51.964  1.000 31.130  ? 188 VAL BBB C   1 
ATOM   7833  O O   . VAL E 2 188 ? 44.013  41.736  51.542  1.000 33.115  ? 188 VAL BBB O   1 
ATOM   7834  C CB  . VAL E 2 188 ? 43.826  43.979  53.836  1.000 30.796  ? 188 VAL BBB CB  1 
ATOM   7835  C CG1 . VAL E 2 188 ? 45.331  43.731  53.678  1.000 32.409  ? 188 VAL BBB CG1 1 
ATOM   7836  C CG2 . VAL E 2 188 ? 43.392  45.214  53.058  1.000 29.869  ? 188 VAL BBB CG2 1 
ATOM   7837  N N   . THR E 2 189 ? 42.073  42.911  51.203  1.000 32.534  ? 189 THR BBB N   1 
ATOM   7838  C CA  . THR E 2 189 ? 42.074  42.864  49.715  1.000 34.870  ? 189 THR BBB CA  1 
ATOM   7839  C C   . THR E 2 189 ? 42.508  44.231  49.166  1.000 34.820  ? 189 THR BBB C   1 
ATOM   7840  O O   . THR E 2 189 ? 41.971  45.264  49.635  1.000 32.760  ? 189 THR BBB O   1 
ATOM   7841  C CB  . THR E 2 189 ? 40.721  42.405  49.172  1.000 35.008  ? 189 THR BBB CB  1 
ATOM   7842  O OG1 . THR E 2 189 ? 39.712  43.086  49.918  1.000 38.791  ? 189 THR BBB OG1 1 
ATOM   7843  C CG2 . THR E 2 189 ? 40.539  40.910  49.299  1.000 33.987  ? 189 THR BBB CG2 1 
ATOM   7844  N N   . VAL E 2 190 ? 43.486  44.214  48.253  1.000 33.332  ? 190 VAL BBB N   1 
ATOM   7845  C CA  . VAL E 2 190 ? 44.055  45.409  47.569  1.000 33.930  ? 190 VAL BBB CA  1 
ATOM   7846  C C   . VAL E 2 190 ? 44.174  45.113  46.079  1.000 34.421  ? 190 VAL BBB C   1 
ATOM   7847  O O   . VAL E 2 190 ? 44.253  43.962  45.695  1.000 33.082  ? 190 VAL BBB O   1 
ATOM   7848  C CB  . VAL E 2 190 ? 45.413  45.784  48.182  1.000 33.364  ? 190 VAL BBB CB  1 
ATOM   7849  C CG1 . VAL E 2 190 ? 45.275  46.028  49.674  1.000 36.309  ? 190 VAL BBB CG1 1 
ATOM   7850  C CG2 . VAL E 2 190 ? 46.477  44.740  47.917  1.000 33.378  ? 190 VAL BBB CG2 1 
ATOM   7851  N N   . PRO E 2 191 ? 44.198  46.125  45.189  1.000 38.355  ? 191 PRO BBB N   1 
ATOM   7852  C CA  . PRO E 2 191 ? 44.446  45.891  43.768  1.000 40.094  ? 191 PRO BBB CA  1 
ATOM   7853  C C   . PRO E 2 191 ? 45.750  45.119  43.521  1.000 40.811  ? 191 PRO BBB C   1 
ATOM   7854  O O   . PRO E 2 191 ? 46.741  45.448  44.154  1.000 43.587  ? 191 PRO BBB O   1 
ATOM   7855  C CB  . PRO E 2 191 ? 44.556  47.316  43.201  1.000 41.227  ? 191 PRO BBB CB  1 
ATOM   7856  C CG  . PRO E 2 191 ? 43.742  48.175  44.142  1.000 41.537  ? 191 PRO BBB CG  1 
ATOM   7857  C CD  . PRO E 2 191 ? 43.958  47.544  45.499  1.000 41.045  ? 191 PRO BBB CD  1 
ATOM   7858  N N   . SER E 2 192 ? 45.744  44.133  42.620  1.000 43.595  ? 192 SER BBB N   1 
ATOM   7859  C CA  . SER E 2 192 ? 46.935  43.279  42.349  1.000 48.070  ? 192 SER BBB CA  1 
ATOM   7860  C C   . SER E 2 192 ? 48.081  44.117  41.772  1.000 49.342  ? 192 SER BBB C   1 
ATOM   7861  O O   . SER E 2 192 ? 49.233  43.806  42.095  1.000 53.247  ? 192 SER BBB O   1 
ATOM   7862  C CB  . SER E 2 192 ? 46.633  42.086  41.479  1.000 46.952  ? 192 SER BBB CB  1 
ATOM   7863  O OG  . SER E 2 192 ? 45.703  42.418  40.479  1.000 52.140  ? 192 SER BBB OG  1 
ATOM   7864  N N   . SER E 2 193 ? 47.786  45.153  40.984  1.000 51.521  ? 193 SER BBB N   1 
ATOM   7865  C CA  . SER E 2 193 ? 48.802  46.072  40.399  1.000 51.017  ? 193 SER BBB CA  1 
ATOM   7866  C C   . SER E 2 193 ? 49.588  46.789  41.505  1.000 50.631  ? 193 SER BBB C   1 
ATOM   7867  O O   . SER E 2 193 ? 50.772  47.096  41.276  1.000 62.188  ? 193 SER BBB O   1 
ATOM   7868  C CB  . SER E 2 193 ? 48.164  47.055  39.469  1.000 49.785  ? 193 SER BBB CB  1 
ATOM   7869  O OG  . SER E 2 193 ? 47.273  47.879  40.181  1.000 49.474  ? 193 SER BBB OG  1 
ATOM   7870  N N   . SER E 2 194 ? 48.978  47.013  42.669  1.000 50.294  ? 194 SER BBB N   1 
ATOM   7871  C CA  . SER E 2 194 ? 49.585  47.755  43.801  1.000 50.842  ? 194 SER BBB CA  1 
ATOM   7872  C C   . SER E 2 194 ? 50.532  46.868  44.612  1.000 46.442  ? 194 SER BBB C   1 
ATOM   7873  O O   . SER E 2 194 ? 51.052  47.373  45.613  1.000 49.737  ? 194 SER BBB O   1 
ATOM   7874  C CB  . SER E 2 194 ? 48.525  48.352  44.694  1.000 55.698  ? 194 SER BBB CB  1 
ATOM   7875  O OG  . SER E 2 194 ? 47.896  47.343  45.480  1.000 60.296  ? 194 SER BBB OG  1 
ATOM   7876  N N   . LEU E 2 195 ? 50.758  45.611  44.227  1.000 44.926  ? 195 LEU BBB N   1 
ATOM   7877  C CA  . LEU E 2 195 ? 51.604  44.691  45.036  1.000 46.394  ? 195 LEU BBB CA  1 
ATOM   7878  C C   . LEU E 2 195 ? 53.078  45.070  44.888  1.000 49.497  ? 195 LEU BBB C   1 
ATOM   7879  O O   . LEU E 2 195 ? 53.862  44.781  45.825  1.000 48.681  ? 195 LEU BBB O   1 
ATOM   7880  C CB  . LEU E 2 195 ? 51.373  43.239  44.608  1.000 43.736  ? 195 LEU BBB CB  1 
ATOM   7881  C CG  . LEU E 2 195 ? 50.135  42.575  45.201  1.000 42.184  ? 195 LEU BBB CG  1 
ATOM   7882  C CD1 . LEU E 2 195 ? 50.056  41.130  44.771  1.000 41.538  ? 195 LEU BBB CD1 1 
ATOM   7883  C CD2 . LEU E 2 195 ? 50.141  42.667  46.709  1.000 43.560  ? 195 LEU BBB CD2 1 
ATOM   7884  N N   . GLY E 2 196 ? 53.425  45.704  43.764  1.000 52.201  ? 196 GLY BBB N   1 
ATOM   7885  C CA  . GLY E 2 196 ? 54.810  46.085  43.442  1.000 54.287  ? 196 GLY BBB CA  1 
ATOM   7886  C C   . GLY E 2 196 ? 55.124  47.489  43.904  1.000 55.987  ? 196 GLY BBB C   1 
ATOM   7887  O O   . GLY E 2 196 ? 56.316  47.780  44.094  1.000 61.398  ? 196 GLY BBB O   1 
ATOM   7888  N N   . THR E 2 197 ? 54.094  48.309  44.107  1.000 53.098  ? 197 THR BBB N   1 
ATOM   7889  C CA  . THR E 2 197 ? 54.204  49.785  44.198  1.000 52.252  ? 197 THR BBB CA  1 
ATOM   7890  C C   . THR E 2 197 ? 53.964  50.254  45.637  1.000 54.334  ? 197 THR BBB C   1 
ATOM   7891  O O   . THR E 2 197 ? 54.529  51.292  46.011  1.000 68.200  ? 197 THR BBB O   1 
ATOM   7892  C CB  . THR E 2 197 ? 53.245  50.443  43.199  1.000 52.167  ? 197 THR BBB CB  1 
ATOM   7893  O OG1 . THR E 2 197 ? 51.985  50.690  43.830  1.000 52.482  ? 197 THR BBB OG1 1 
ATOM   7894  C CG2 . THR E 2 197 ? 53.060  49.620  41.945  1.000 49.053  ? 197 THR BBB CG2 1 
ATOM   7895  N N   . GLN E 2 198 ? 53.208  49.501  46.430  1.000 49.235  ? 198 GLN BBB N   1 
ATOM   7896  C CA  . GLN E 2 198 ? 52.755  49.934  47.772  1.000 48.670  ? 198 GLN BBB CA  1 
ATOM   7897  C C   . GLN E 2 198 ? 53.391  48.993  48.800  1.000 41.327  ? 198 GLN BBB C   1 
ATOM   7898  O O   . GLN E 2 198 ? 53.390  47.782  48.564  1.000 41.213  ? 198 GLN BBB O   1 
ATOM   7899  C CB  . GLN E 2 198 ? 51.220  49.948  47.798  1.000 53.391  ? 198 GLN BBB CB  1 
ATOM   7900  C CG  . GLN E 2 198 ? 50.628  50.379  49.130  1.000 59.374  ? 198 GLN BBB CG  1 
ATOM   7901  C CD  . GLN E 2 198 ? 50.983  51.796  49.463  1.000 63.921  ? 198 GLN BBB CD  1 
ATOM   7902  O OE1 . GLN E 2 198 ? 52.002  52.063  50.113  1.000 66.269  ? 198 GLN BBB OE1 1 
ATOM   7903  N NE2 . GLN E 2 198 ? 50.135  52.698  48.990  1.000 66.030  ? 198 GLN BBB NE2 1 
ATOM   7904  N N   . THR E 2 199 ? 53.935  49.533  49.885  1.000 37.248  ? 199 THR BBB N   1 
ATOM   7905  C CA  . THR E 2 199 ? 54.330  48.746  51.080  1.000 34.265  ? 199 THR BBB CA  1 
ATOM   7906  C C   . THR E 2 199 ? 53.093  48.440  51.948  1.000 34.388  ? 199 THR BBB C   1 
ATOM   7907  O O   . THR E 2 199 ? 52.316  49.383  52.281  1.000 36.509  ? 199 THR BBB O   1 
ATOM   7908  C CB  . THR E 2 199 ? 55.421  49.468  51.867  1.000 32.368  ? 199 THR BBB CB  1 
ATOM   7909  O OG1 . THR E 2 199 ? 56.612  49.339  51.102  1.000 31.602  ? 199 THR BBB OG1 1 
ATOM   7910  C CG2 . THR E 2 199 ? 55.664  48.878  53.230  1.000 33.513  ? 199 THR BBB CG2 1 
ATOM   7911  N N   . TYR E 2 200 ? 52.934  47.159  52.308  1.000 31.623  ? 200 TYR BBB N   1 
ATOM   7912  C CA  . TYR E 2 200 ? 51.909  46.637  53.241  1.000 28.473  ? 200 TYR BBB CA  1 
ATOM   7913  C C   . TYR E 2 200 ? 52.595  46.128  54.497  1.000 28.655  ? 200 TYR BBB C   1 
ATOM   7914  O O   . TYR E 2 200 ? 53.451  45.252  54.391  1.000 28.594  ? 200 TYR BBB O   1 
ATOM   7915  C CB  . TYR E 2 200 ? 51.087  45.557  52.561  1.000 28.213  ? 200 TYR BBB CB  1 
ATOM   7916  C CG  . TYR E 2 200 ? 50.262  46.140  51.455  1.000 28.495  ? 200 TYR BBB CG  1 
ATOM   7917  C CD1 . TYR E 2 200 ? 49.240  47.009  51.747  1.000 28.669  ? 200 TYR BBB CD1 1 
ATOM   7918  C CD2 . TYR E 2 200 ? 50.548  45.895  50.130  1.000 28.600  ? 200 TYR BBB CD2 1 
ATOM   7919  C CE1 . TYR E 2 200 ? 48.456  47.561  50.753  1.000 28.144  ? 200 TYR BBB CE1 1 
ATOM   7920  C CE2 . TYR E 2 200 ? 49.766  46.422  49.121  1.000 28.363  ? 200 TYR BBB CE2 1 
ATOM   7921  C CZ  . TYR E 2 200 ? 48.732  47.282  49.433  1.000 27.701  ? 200 TYR BBB CZ  1 
ATOM   7922  O OH  . TYR E 2 200 ? 47.977  47.859  48.456  1.000 29.897  ? 200 TYR BBB OH  1 
ATOM   7923  N N   . ILE E 2 201 ? 52.235  46.725  55.634  1.000 29.956  ? 201 ILE BBB N   1 
ATOM   7924  C CA  . ILE E 2 201 ? 52.729  46.372  56.992  1.000 31.489  ? 201 ILE BBB CA  1 
ATOM   7925  C C   . ILE E 2 201 ? 51.521  46.187  57.901  1.000 33.166  ? 201 ILE BBB C   1 
ATOM   7926  O O   . ILE E 2 201 ? 50.669  47.090  57.898  1.000 31.602  ? 201 ILE BBB O   1 
ATOM   7927  C CB  . ILE E 2 201 ? 53.647  47.471  57.542  1.000 32.277  ? 201 ILE BBB CB  1 
ATOM   7928  C CG1 . ILE E 2 201 ? 54.915  47.607  56.698  1.000 33.182  ? 201 ILE BBB CG1 1 
ATOM   7929  C CG2 . ILE E 2 201 ? 53.963  47.199  59.008  1.000 34.411  ? 201 ILE BBB CG2 1 
ATOM   7930  C CD1 . ILE E 2 201 ? 56.011  48.447  57.339  1.000 34.333  ? 201 ILE BBB CD1 1 
ATOM   7931  N N   . CYS E 2 202 ? 51.460  45.093  58.667  1.000 36.327  ? 202 CYS BBB N   1 
ATOM   7932  C CA  . CYS E 2 202 ? 50.473  44.954  59.768  1.000 40.941  ? 202 CYS BBB CA  1 
ATOM   7933  C C   . CYS E 2 202 ? 51.145  45.273  61.107  1.000 35.481  ? 202 CYS BBB C   1 
ATOM   7934  O O   . CYS E 2 202 ? 52.258  44.809  61.338  1.000 32.099  ? 202 CYS BBB O   1 
ATOM   7935  C CB  . CYS E 2 202 ? 49.793  43.592  59.771  1.000 48.936  ? 202 CYS BBB CB  1 
ATOM   7936  S SG  . CYS E 2 202 ? 50.757  42.291  60.568  1.000 63.571  ? 202 CYS BBB SG  1 
ATOM   7937  N N   . ASN E 2 203 ? 50.464  46.053  61.940  1.000 32.273  ? 203 ASN BBB N   1 
ATOM   7938  C CA  . ASN E 2 203 ? 50.955  46.495  63.260  1.000 29.937  ? 203 ASN BBB CA  1 
ATOM   7939  C C   . ASN E 2 203 ? 50.149  45.699  64.256  1.000 28.675  ? 203 ASN BBB C   1 
ATOM   7940  O O   . ASN E 2 203 ? 48.922  45.762  64.227  1.000 30.140  ? 203 ASN BBB O   1 
ATOM   7941  C CB  . ASN E 2 203 ? 50.827  48.006  63.416  1.000 29.648  ? 203 ASN BBB CB  1 
ATOM   7942  C CG  . ASN E 2 203 ? 51.095  48.699  62.098  1.000 29.495  ? 203 ASN BBB CG  1 
ATOM   7943  O OD1 . ASN E 2 203 ? 50.182  48.874  61.293  1.000 31.350  ? 203 ASN BBB OD1 1 
ATOM   7944  N ND2 . ASN E 2 203 ? 52.339  49.047  61.837  1.000 26.298  ? 203 ASN BBB ND2 1 
ATOM   7945  N N   . VAL E 2 204 ? 50.847  44.912  65.046  1.000 30.018  ? 204 VAL BBB N   1 
ATOM   7946  C CA  . VAL E 2 204 ? 50.246  44.079  66.112  1.000 29.995  ? 204 VAL BBB CA  1 
ATOM   7947  C C   . VAL E 2 204 ? 50.670  44.697  67.439  1.000 29.324  ? 204 VAL BBB C   1 
ATOM   7948  O O   . VAL E 2 204 ? 51.846  45.013  67.594  1.000 26.865  ? 204 VAL BBB O   1 
ATOM   7949  C CB  . VAL E 2 204 ? 50.682  42.619  65.950  1.000 30.725  ? 204 VAL BBB CB  1 
ATOM   7950  C CG1 . VAL E 2 204 ? 49.963  41.731  66.939  1.000 32.855  ? 204 VAL BBB CG1 1 
ATOM   7951  C CG2 . VAL E 2 204 ? 50.441  42.134  64.532  1.000 29.902  ? 204 VAL BBB CG2 1 
ATOM   7952  N N   . ASN E 2 205 ? 49.705  44.968  68.301  1.000 30.945  ? 205 ASN BBB N   1 
ATOM   7953  C CA  . ASN E 2 205 ? 49.970  45.474  69.658  1.000 34.303  ? 205 ASN BBB CA  1 
ATOM   7954  C C   . ASN E 2 205 ? 49.348  44.475  70.642  1.000 36.992  ? 205 ASN BBB C   1 
ATOM   7955  O O   . ASN E 2 205 ? 48.157  44.176  70.508  1.000 41.350  ? 205 ASN BBB O   1 
ATOM   7956  C CB  . ASN E 2 205 ? 49.494  46.916  69.817  1.000 34.157  ? 205 ASN BBB CB  1 
ATOM   7957  C CG  . ASN E 2 205 ? 50.003  47.511  71.111  1.000 37.676  ? 205 ASN BBB CG  1 
ATOM   7958  O OD1 . ASN E 2 205 ? 51.047  47.090  71.618  1.000 44.461  ? 205 ASN BBB OD1 1 
ATOM   7959  N ND2 . ASN E 2 205 ? 49.262  48.446  71.669  1.000 40.110  ? 205 ASN BBB ND2 1 
ATOM   7960  N N   . HIS E 2 206 ? 50.152  43.929  71.554  1.000 35.907  ? 206 HIS BBB N   1 
ATOM   7961  C CA  . HIS E 2 206 ? 49.685  43.073  72.667  1.000 37.264  ? 206 HIS BBB CA  1 
ATOM   7962  C C   . HIS E 2 206 ? 50.040  43.769  73.981  1.000 38.543  ? 206 HIS BBB C   1 
ATOM   7963  O O   . HIS E 2 206 ? 51.109  43.485  74.526  1.000 37.866  ? 206 HIS BBB O   1 
ATOM   7964  C CB  . HIS E 2 206 ? 50.254  41.661  72.519  1.000 35.545  ? 206 HIS BBB CB  1 
ATOM   7965  C CG  . HIS E 2 206 ? 49.675  40.686  73.485  1.000 36.311  ? 206 HIS BBB CG  1 
ATOM   7966  N ND1 . HIS E 2 206 ? 50.447  39.792  74.179  1.000 38.000  ? 206 HIS BBB ND1 1 
ATOM   7967  C CD2 . HIS E 2 206 ? 48.408  40.455  73.878  1.000 36.623  ? 206 HIS BBB CD2 1 
ATOM   7968  C CE1 . HIS E 2 206 ? 49.686  39.045  74.950  1.000 37.713  ? 206 HIS BBB CE1 1 
ATOM   7969  N NE2 . HIS E 2 206 ? 48.438  39.435  74.791  1.000 37.477  ? 206 HIS BBB NE2 1 
ATOM   7970  N N   . LYS E 2 207 ? 49.162  44.650  74.459  1.000 41.423  ? 207 LYS BBB N   1 
ATOM   7971  C CA  . LYS E 2 207 ? 49.398  45.473  75.669  1.000 45.837  ? 207 LYS BBB CA  1 
ATOM   7972  C C   . LYS E 2 207 ? 49.773  44.577  76.853  1.000 45.532  ? 207 LYS BBB C   1 
ATOM   7973  O O   . LYS E 2 207 ? 50.705  44.900  77.585  1.000 42.850  ? 207 LYS BBB O   1 
ATOM   7974  C CB  . LYS E 2 207 ? 48.183  46.354  75.972  1.000 51.665  ? 207 LYS BBB CB  1 
ATOM   7975  C CG  . LYS E 2 207 ? 48.014  47.558  75.059  1.000 60.990  ? 207 LYS BBB CG  1 
ATOM   7976  C CD  . LYS E 2 207 ? 47.616  48.811  75.809  1.000 72.976  ? 207 LYS BBB CD  1 
ATOM   7977  C CE  . LYS E 2 207 ? 47.518  50.047  74.935  1.000 77.605  ? 207 LYS BBB CE  1 
ATOM   7978  N NZ  . LYS E 2 207 ? 46.360  49.949  74.016  1.000 80.393  ? 207 LYS BBB NZ  1 
ATOM   7979  N N   . PRO E 2 208 ? 49.062  43.452  77.114  1.000 46.181  ? 208 PRO BBB N   1 
ATOM   7980  C CA  . PRO E 2 208 ? 49.359  42.605  78.273  1.000 44.291  ? 208 PRO BBB CA  1 
ATOM   7981  C C   . PRO E 2 208 ? 50.820  42.149  78.377  1.000 43.603  ? 208 PRO BBB C   1 
ATOM   7982  O O   . PRO E 2 208 ? 51.315  42.112  79.481  1.000 44.633  ? 208 PRO BBB O   1 
ATOM   7983  C CB  . PRO E 2 208 ? 48.478  41.382  78.049  1.000 43.549  ? 208 PRO BBB CB  1 
ATOM   7984  C CG  . PRO E 2 208 ? 47.297  41.929  77.302  1.000 44.186  ? 208 PRO BBB CG  1 
ATOM   7985  C CD  . PRO E 2 208 ? 47.883  42.976  76.374  1.000 44.476  ? 208 PRO BBB CD  1 
ATOM   7986  N N   . SER E 2 209 ? 51.456  41.843  77.243  1.000 42.175  ? 209 SER BBB N   1 
ATOM   7987  C CA  . SER E 2 209 ? 52.868  41.375  77.145  1.000 41.445  ? 209 SER BBB CA  1 
ATOM   7988  C C   . SER E 2 209 ? 53.789  42.538  76.768  1.000 42.508  ? 209 SER BBB C   1 
ATOM   7989  O O   . SER E 2 209 ? 55.002  42.325  76.622  1.000 40.082  ? 209 SER BBB O   1 
ATOM   7990  C CB  . SER E 2 209 ? 52.991  40.259  76.158  1.000 39.813  ? 209 SER BBB CB  1 
ATOM   7991  O OG  . SER E 2 209 ? 52.962  40.766  74.844  1.000 38.408  ? 209 SER BBB OG  1 
ATOM   7992  N N   . ASN E 2 210 ? 53.205  43.722  76.615  1.000 48.664  ? 210 ASN BBB N   1 
ATOM   7993  C CA  . ASN E 2 210 ? 53.893  44.987  76.251  1.000 51.646  ? 210 ASN BBB CA  1 
ATOM   7994  C C   . ASN E 2 210 ? 54.724  44.748  74.984  1.000 49.509  ? 210 ASN BBB C   1 
ATOM   7995  O O   . ASN E 2 210 ? 55.898  45.068  74.986  1.000 50.006  ? 210 ASN BBB O   1 
ATOM   7996  C CB  . ASN E 2 210 ? 54.698  45.534  77.427  1.000 53.998  ? 210 ASN BBB CB  1 
ATOM   7997  C CG  . ASN E 2 210 ? 54.890  47.022  77.287  1.000 65.176  ? 210 ASN BBB CG  1 
ATOM   7998  O OD1 . ASN E 2 210 ? 54.530  47.612  76.268  1.000 72.490  ? 210 ASN BBB OD1 1 
ATOM   7999  N ND2 . ASN E 2 210 ? 55.434  47.634  78.317  1.000 86.201  ? 210 ASN BBB ND2 1 
ATOM   8000  N N   . THR E 2 211 ? 54.095  44.205  73.948  1.000 48.473  ? 211 THR BBB N   1 
ATOM   8001  C CA  . THR E 2 211 ? 54.713  43.714  72.697  1.000 46.747  ? 211 THR BBB CA  1 
ATOM   8002  C C   . THR E 2 211 ? 54.140  44.495  71.531  1.000 44.769  ? 211 THR BBB C   1 
ATOM   8003  O O   . THR E 2 211 ? 52.959  44.309  71.257  1.000 50.108  ? 211 THR BBB O   1 
ATOM   8004  C CB  . THR E 2 211 ? 54.349  42.243  72.476  1.000 49.336  ? 211 THR BBB CB  1 
ATOM   8005  O OG1 . THR E 2 211 ? 55.059  41.540  73.487  1.000 51.374  ? 211 THR BBB OG1 1 
ATOM   8006  C CG2 . THR E 2 211 ? 54.699  41.697  71.109  1.000 51.736  ? 211 THR BBB CG2 1 
ATOM   8007  N N   . LYS E 2 212 ? 54.944  45.321  70.880  1.000 44.320  ? 212 LYS BBB N   1 
ATOM   8008  C CA  . LYS E 2 212 ? 54.580  45.968  69.595  1.000 45.626  ? 212 LYS BBB CA  1 
ATOM   8009  C C   . LYS E 2 212 ? 55.393  45.285  68.484  1.000 38.672  ? 212 LYS BBB C   1 
ATOM   8010  O O   . LYS E 2 212 ? 56.586  45.137  68.628  1.000 40.530  ? 212 LYS BBB O   1 
ATOM   8011  C CB  . LYS E 2 212 ? 54.726  47.496  69.701  1.000 52.622  ? 212 LYS BBB CB  1 
ATOM   8012  C CG  . LYS E 2 212 ? 53.666  48.290  68.949  1.000 64.087  ? 212 LYS BBB CG  1 
ATOM   8013  C CD  . LYS E 2 212 ? 53.623  49.772  69.280  1.000 63.644  ? 212 LYS BBB CD  1 
ATOM   8014  C CE  . LYS E 2 212 ? 52.194  50.244  69.459  1.000 63.345  ? 212 LYS BBB CE  1 
ATOM   8015  N NZ  . LYS E 2 212 ? 52.126  51.248  70.537  1.000 66.162  ? 212 LYS BBB NZ  1 
ATOM   8016  N N   . VAL E 2 213 ? 54.728  44.823  67.437  1.000 37.160  ? 213 VAL BBB N   1 
ATOM   8017  C CA  . VAL E 2 213 ? 55.373  44.160  66.266  1.000 35.461  ? 213 VAL BBB CA  1 
ATOM   8018  C C   . VAL E 2 213 ? 54.792  44.755  64.994  1.000 37.277  ? 213 VAL BBB C   1 
ATOM   8019  O O   . VAL E 2 213 ? 53.561  44.828  64.910  1.000 42.303  ? 213 VAL BBB O   1 
ATOM   8020  C CB  . VAL E 2 213 ? 55.158  42.642  66.263  1.000 33.719  ? 213 VAL BBB CB  1 
ATOM   8021  C CG1 . VAL E 2 213 ? 55.637  42.037  64.956  1.000 31.030  ? 213 VAL BBB CG1 1 
ATOM   8022  C CG2 . VAL E 2 213 ? 55.841  41.988  67.447  1.000 35.640  ? 213 VAL BBB CG2 1 
ATOM   8023  N N   . ASP E 2 214 ? 55.662  45.183  64.081  1.000 37.685  ? 214 ASP BBB N   1 
ATOM   8024  C CA  . ASP E 2 214 ? 55.302  45.671  62.728  1.000 38.163  ? 214 ASP BBB CA  1 
ATOM   8025  C C   . ASP E 2 214 ? 55.902  44.681  61.747  1.000 37.410  ? 214 ASP BBB C   1 
ATOM   8026  O O   . ASP E 2 214 ? 57.115  44.520  61.766  1.000 48.004  ? 214 ASP BBB O   1 
ATOM   8027  C CB  . ASP E 2 214 ? 55.824  47.079  62.455  1.000 40.062  ? 214 ASP BBB CB  1 
ATOM   8028  C CG  . ASP E 2 214 ? 55.206  48.172  63.312  1.000 47.292  ? 214 ASP BBB CG  1 
ATOM   8029  O OD1 . ASP E 2 214 ? 54.060  48.006  63.880  1.000 49.423  ? 214 ASP BBB OD1 1 
ATOM   8030  O OD2 . ASP E 2 214 ? 55.833  49.235  63.335  1.000 58.077  ? 214 ASP BBB OD2 1 
ATOM   8031  N N   . LYS E 2 215 ? 55.069  43.989  60.988  1.000 39.200  ? 215 LYS BBB N   1 
ATOM   8032  C CA  . LYS E 2 215 ? 55.507  42.908  60.076  1.000 41.344  ? 215 LYS BBB CA  1 
ATOM   8033  C C   . LYS E 2 215 ? 55.178  43.325  58.655  1.000 38.030  ? 215 LYS BBB C   1 
ATOM   8034  O O   . LYS E 2 215 ? 54.015  43.613  58.392  1.000 40.886  ? 215 LYS BBB O   1 
ATOM   8035  C CB  . LYS E 2 215 ? 54.813  41.585  60.403  1.000 46.496  ? 215 LYS BBB CB  1 
ATOM   8036  C CG  . LYS E 2 215 ? 55.393  40.385  59.682  1.000 49.666  ? 215 LYS BBB CG  1 
ATOM   8037  C CD  . LYS E 2 215 ? 56.855  40.184  59.909  1.000 57.161  ? 215 LYS BBB CD  1 
ATOM   8038  C CE  . LYS E 2 215 ? 57.375  39.088  59.004  1.000 70.229  ? 215 LYS BBB CE  1 
ATOM   8039  N NZ  . LYS E 2 215 ? 58.745  38.671  59.366  1.000 78.187  ? 215 LYS BBB NZ  1 
ATOM   8040  N N   . LYS E 2 216 ? 56.180  43.343  57.790  1.000 36.955  ? 216 LYS BBB N   1 
ATOM   8041  C CA  . LYS E 2 216 ? 56.017  43.677  56.362  1.000 35.183  ? 216 LYS BBB CA  1 
ATOM   8042  C C   . LYS E 2 216 ? 55.590  42.415  55.622  1.000 34.292  ? 216 LYS BBB C   1 
ATOM   8043  O O   . LYS E 2 216 ? 56.232  41.363  55.749  1.000 41.370  ? 216 LYS BBB O   1 
ATOM   8044  C CB  . LYS E 2 216 ? 57.317  44.224  55.786  1.000 38.523  ? 216 LYS BBB CB  1 
ATOM   8045  C CG  . LYS E 2 216 ? 57.234  44.556  54.313  1.000 44.036  ? 216 LYS BBB CG  1 
ATOM   8046  C CD  . LYS E 2 216 ? 58.355  45.430  53.844  1.000 51.626  ? 216 LYS BBB CD  1 
ATOM   8047  C CE  . LYS E 2 216 ? 58.149  45.881  52.415  1.000 59.322  ? 216 LYS BBB CE  1 
ATOM   8048  N NZ  . LYS E 2 216 ? 59.323  46.648  51.939  1.000 67.318  ? 216 LYS BBB NZ  1 
ATOM   8049  N N   . VAL E 2 217 ? 54.501  42.515  54.895  1.000 34.424  ? 217 VAL BBB N   1 
ATOM   8050  C CA  . VAL E 2 217 ? 53.950  41.407  54.084  1.000 35.418  ? 217 VAL BBB CA  1 
ATOM   8051  C C   . VAL E 2 217 ? 54.249  41.771  52.640  1.000 37.590  ? 217 VAL BBB C   1 
ATOM   8052  O O   . VAL E 2 217 ? 53.745  42.822  52.186  1.000 35.719  ? 217 VAL BBB O   1 
ATOM   8053  C CB  . VAL E 2 217 ? 52.444  41.257  54.335  1.000 35.664  ? 217 VAL BBB CB  1 
ATOM   8054  C CG1 . VAL E 2 217 ? 51.845  40.128  53.519  1.000 36.575  ? 217 VAL BBB CG1 1 
ATOM   8055  C CG2 . VAL E 2 217 ? 52.138  41.083  55.812  1.000 35.626  ? 217 VAL BBB CG2 1 
ATOM   8056  N N   . GLU E 2 218 ? 55.074  40.967  51.972  1.000 44.961  ? 218 GLU BBB N   1 
ATOM   8057  C CA  . GLU E 2 218 ? 55.404  41.201  50.548  1.000 50.604  ? 218 GLU BBB CA  1 
ATOM   8058  C C   . GLU E 2 218 ? 55.339  39.887  49.793  1.000 49.331  ? 218 GLU BBB C   1 
ATOM   8059  O O   . GLU E 2 218 ? 55.482  38.810  50.384  1.000 47.529  ? 218 GLU BBB O   1 
ATOM   8060  C CB  . GLU E 2 218 ? 56.747  41.913  50.386  1.000 58.149  ? 218 GLU BBB CB  1 
ATOM   8061  C CG  . GLU E 2 218 ? 57.949  41.184  50.949  1.000 61.590  ? 218 GLU BBB CG  1 
ATOM   8062  C CD  . GLU E 2 218 ? 59.217  42.044  51.040  1.000 64.986  ? 218 GLU BBB CD  1 
ATOM   8063  O OE1 . GLU E 2 218 ? 59.218  43.193  50.535  1.000 60.912  ? 218 GLU BBB OE1 1 
ATOM   8064  O OE2 . GLU E 2 218 ? 60.216  41.574  51.619  1.000 67.867  ? 218 GLU BBB OE2 1 
ATOM   8065  N N   . PRO E 2 219 ? 55.127  39.967  48.459  1.000 51.047  ? 219 PRO BBB N   1 
ATOM   8066  C CA  . PRO E 2 219 ? 55.039  38.774  47.617  1.000 56.311  ? 219 PRO BBB CA  1 
ATOM   8067  C C   . PRO E 2 219 ? 56.350  37.984  47.731  1.000 67.146  ? 219 PRO BBB C   1 
ATOM   8068  O O   . PRO E 2 219 ? 57.414  38.615  47.658  1.000 68.332  ? 219 PRO BBB O   1 
ATOM   8069  C CB  . PRO E 2 219 ? 54.837  39.301  46.190  1.000 54.465  ? 219 PRO BBB CB  1 
ATOM   8070  C CG  . PRO E 2 219 ? 54.432  40.764  46.355  1.000 53.570  ? 219 PRO BBB CG  1 
ATOM   8071  C CD  . PRO E 2 219 ? 54.972  41.215  47.694  1.000 51.011  ? 219 PRO BBB CD  1 
ATOM   8072  N N   . LYS E 2 220 ? 56.262  36.667  47.950  1.000 72.752  ? 220 LYS BBB N   1 
ATOM   8073  C CA  . LYS E 2 220 ? 57.445  35.841  48.311  1.000 78.808  ? 220 LYS BBB CA  1 
ATOM   8074  C C   . LYS E 2 220 ? 58.417  35.843  47.120  1.000 86.216  ? 220 LYS BBB C   1 
ATOM   8075  O O   . LYS E 2 220 ? 57.928  35.777  45.978  1.000 78.472  ? 220 LYS BBB O   1 
ATOM   8076  C CB  . LYS E 2 220 ? 57.011  34.429  48.718  1.000 79.798  ? 220 LYS BBB CB  1 
ATOM   8077  C CG  . LYS E 2 220 ? 58.020  33.666  49.574  1.000 84.087  ? 220 LYS BBB CG  1 
ATOM   8078  C CD  . LYS E 2 220 ? 57.777  32.169  49.624  1.000 91.849  ? 220 LYS BBB CD  1 
ATOM   8079  C CE  . LYS E 2 220 ? 58.560  31.464  50.709  1.000 92.864  ? 220 LYS BBB CE  1 
ATOM   8080  N NZ  . LYS E 2 220 ? 57.873  31.604  52.013  1.000 99.567  ? 220 LYS BBB NZ  1 
ATOM   8081  N N   . SER E 2 221 ? 59.728  35.988  47.375  1.000 99.934  ? 221 SER BBB N   1 
ATOM   8082  C CA  . SER E 2 221 ? 60.824  35.831  46.377  1.000 101.621 ? 221 SER BBB CA  1 
ATOM   8083  C C   . SER E 2 221 ? 60.690  34.445  45.738  1.000 122.916 ? 221 SER BBB C   1 
ATOM   8084  O O   . SER E 2 221 ? 60.461  34.382  44.511  1.000 128.981 ? 221 SER BBB O   1 
ATOM   8085  C CB  . SER E 2 221 ? 62.185  36.005  47.008  1.000 96.097  ? 221 SER BBB CB  1 
ATOM   8086  O OG  . SER E 2 221 ? 62.466  37.371  47.268  1.000 94.335  ? 221 SER BBB OG  1 
ATOM   8087  N N   . CYS E 2 222 ? 60.773  33.398  46.579  1.000 146.665 ? 222 CYS BBB N   1 
ATOM   8088  C CA  . CYS E 2 222 ? 60.456  31.959  46.315  1.000 149.054 ? 222 CYS BBB CA  1 
ATOM   8089  C C   . CYS E 2 222 ? 61.372  31.400  45.222  1.000 145.890 ? 222 CYS BBB C   1 
ATOM   8090  O O   . CYS E 2 222 ? 62.329  32.046  44.789  1.000 133.630 ? 222 CYS BBB O   1 
ATOM   8091  C CB  . CYS E 2 222 ? 58.975  31.730  45.994  1.000 148.945 ? 222 CYS BBB CB  1 
ATOM   8092  S SG  . CYS E 2 222 ? 58.527  31.677  44.239  1.000 137.580 ? 222 CYS BBB SG  1 
ATOM   8093  O OXT . CYS E 2 222 ? 61.158  30.272  44.781  1.000 138.898 ? 222 CYS BBB OXT 1 
ATOM   8094  N N   . ASP F 3 1   ? 10.202  27.275  89.169  1.000 96.305  ? 1   ASP CCC N   1 
ATOM   8095  C CA  . ASP F 3 1   ? 11.357  27.209  88.229  1.000 90.843  ? 1   ASP CCC CA  1 
ATOM   8096  C C   . ASP F 3 1   ? 10.807  27.104  86.801  1.000 83.275  ? 1   ASP CCC C   1 
ATOM   8097  O O   . ASP F 3 1   ? 10.565  25.978  86.292  1.000 80.774  ? 1   ASP CCC O   1 
ATOM   8098  C CB  . ASP F 3 1   ? 12.322  26.073  88.582  1.000 95.800  ? 1   ASP CCC CB  1 
ATOM   8099  C CG  . ASP F 3 1   ? 13.779  26.500  88.572  1.000 99.616  ? 1   ASP CCC CG  1 
ATOM   8100  O OD1 . ASP F 3 1   ? 14.350  26.575  89.675  1.000 96.554  ? 1   ASP CCC OD1 1 
ATOM   8101  O OD2 . ASP F 3 1   ? 14.324  26.780  87.469  1.000 104.335 ? 1   ASP CCC OD2 1 
ATOM   8102  N N   . ILE F 3 2   ? 10.607  28.270  86.192  1.000 73.770  ? 2   ILE CCC N   1 
ATOM   8103  C CA  . ILE F 3 2   ? 10.048  28.447  84.823  1.000 67.179  ? 2   ILE CCC CA  1 
ATOM   8104  C C   . ILE F 3 2   ? 11.192  28.291  83.832  1.000 69.017  ? 2   ILE CCC C   1 
ATOM   8105  O O   . ILE F 3 2   ? 12.320  28.698  84.131  1.000 85.193  ? 2   ILE CCC O   1 
ATOM   8106  C CB  . ILE F 3 2   ? 9.380   29.824  84.677  1.000 58.029  ? 2   ILE CCC CB  1 
ATOM   8107  C CG1 . ILE F 3 2   ? 8.305   30.022  85.750  1.000 50.927  ? 2   ILE CCC CG1 1 
ATOM   8108  C CG2 . ILE F 3 2   ? 8.868   30.019  83.255  1.000 56.847  ? 2   ILE CCC CG2 1 
ATOM   8109  C CD1 . ILE F 3 2   ? 7.673   31.376  85.764  1.000 51.221  ? 2   ILE CCC CD1 1 
ATOM   8110  N N   . GLN F 3 3   ? 10.878  27.747  82.675  1.000 72.055  ? 3   GLN CCC N   1 
ATOM   8111  C CA  . GLN F 3 3   ? 11.857  27.455  81.613  1.000 72.288  ? 3   GLN CCC CA  1 
ATOM   8112  C C   . GLN F 3 3   ? 11.297  28.085  80.339  1.000 67.143  ? 3   GLN CCC C   1 
ATOM   8113  O O   . GLN F 3 3   ? 10.074  28.066  80.169  1.000 78.735  ? 3   GLN CCC O   1 
ATOM   8114  C CB  . GLN F 3 3   ? 12.031  25.945  81.624  1.000 77.879  ? 3   GLN CCC CB  1 
ATOM   8115  C CG  . GLN F 3 3   ? 12.913  25.376  80.538  1.000 91.187  ? 3   GLN CCC CG  1 
ATOM   8116  C CD  . GLN F 3 3   ? 13.033  23.889  80.783  1.000 101.159 ? 3   GLN CCC CD  1 
ATOM   8117  O OE1 . GLN F 3 3   ? 12.050  23.195  81.062  1.000 106.259 ? 3   GLN CCC OE1 1 
ATOM   8118  N NE2 . GLN F 3 3   ? 14.255  23.385  80.714  1.000 101.691 ? 3   GLN CCC NE2 1 
ATOM   8119  N N   . LEU F 3 4   ? 12.139  28.730  79.546  1.000 58.166  ? 4   LEU CCC N   1 
ATOM   8120  C CA  . LEU F 3 4   ? 11.714  29.400  78.296  1.000 49.066  ? 4   LEU CCC CA  1 
ATOM   8121  C C   . LEU F 3 4   ? 12.364  28.668  77.134  1.000 49.444  ? 4   LEU CCC C   1 
ATOM   8122  O O   . LEU F 3 4   ? 13.545  28.300  77.262  1.000 40.578  ? 4   LEU CCC O   1 
ATOM   8123  C CB  . LEU F 3 4   ? 12.163  30.859  78.316  1.000 46.422  ? 4   LEU CCC CB  1 
ATOM   8124  C CG  . LEU F 3 4   ? 11.654  31.699  79.478  1.000 49.471  ? 4   LEU CCC CG  1 
ATOM   8125  C CD1 . LEU F 3 4   ? 12.136  33.135  79.328  1.000 52.526  ? 4   LEU CCC CD1 1 
ATOM   8126  C CD2 . LEU F 3 4   ? 10.138  31.666  79.570  1.000 52.188  ? 4   LEU CCC CD2 1 
ATOM   8127  N N   . THR F 3 5   ? 11.614  28.461  76.051  1.000 56.406  ? 5   THR CCC N   1 
ATOM   8128  C CA  . THR F 3 5   ? 12.168  27.976  74.762  1.000 59.990  ? 5   THR CCC CA  1 
ATOM   8129  C C   . THR F 3 5   ? 11.869  29.020  73.689  1.000 58.259  ? 5   THR CCC C   1 
ATOM   8130  O O   . THR F 3 5   ? 10.676  29.298  73.454  1.000 56.048  ? 5   THR CCC O   1 
ATOM   8131  C CB  . THR F 3 5   ? 11.639  26.588  74.385  1.000 62.514  ? 5   THR CCC CB  1 
ATOM   8132  O OG1 . THR F 3 5   ? 11.474  25.851  75.597  1.000 65.595  ? 5   THR CCC OG1 1 
ATOM   8133  C CG2 . THR F 3 5   ? 12.570  25.860  73.436  1.000 59.621  ? 5   THR CCC CG2 1 
ATOM   8134  N N   . GLN F 3 6   ? 12.923  29.584  73.098  1.000 55.353  ? 6   GLN CCC N   1 
ATOM   8135  C CA  . GLN F 3 6   ? 12.811  30.504  71.943  1.000 54.544  ? 6   GLN CCC CA  1 
ATOM   8136  C C   . GLN F 3 6   ? 12.839  29.686  70.659  1.000 53.817  ? 6   GLN CCC C   1 
ATOM   8137  O O   . GLN F 3 6   ? 13.342  28.549  70.689  1.000 49.264  ? 6   GLN CCC O   1 
ATOM   8138  C CB  . GLN F 3 6   ? 13.964  31.500  71.879  1.000 55.044  ? 6   GLN CCC CB  1 
ATOM   8139  C CG  . GLN F 3 6   ? 13.759  32.734  72.725  1.000 52.454  ? 6   GLN CCC CG  1 
ATOM   8140  C CD  . GLN F 3 6   ? 14.957  33.621  72.549  1.000 51.553  ? 6   GLN CCC CD  1 
ATOM   8141  O OE1 . GLN F 3 6   ? 15.851  33.626  73.384  1.000 56.607  ? 6   GLN CCC OE1 1 
ATOM   8142  N NE2 . GLN F 3 6   ? 15.008  34.323  71.429  1.000 46.899  ? 6   GLN CCC NE2 1 
ATOM   8143  N N   . SER F 3 7   ? 12.337  30.273  69.575  1.000 55.693  ? 7   SER CCC N   1 
ATOM   8144  C CA  . SER F 3 7   ? 12.395  29.710  68.205  1.000 53.869  ? 7   SER CCC CA  1 
ATOM   8145  C C   . SER F 3 7   ? 12.136  30.829  67.203  1.000 52.072  ? 7   SER CCC C   1 
ATOM   8146  O O   . SER F 3 7   ? 11.354  31.738  67.475  1.000 47.181  ? 7   SER CCC O   1 
ATOM   8147  C CB  . SER F 3 7   ? 11.408  28.602  68.045  1.000 54.706  ? 7   SER CCC CB  1 
ATOM   8148  O OG  . SER F 3 7   ? 10.095  29.104  68.247  1.000 59.810  ? 7   SER CCC OG  1 
ATOM   8149  N N   . PRO F 3 8   ? 12.795  30.817  66.027  1.000 50.931  ? 8   PRO CCC N   1 
ATOM   8150  C CA  . PRO F 3 8   ? 13.861  29.853  65.738  1.000 50.444  ? 8   PRO CCC CA  1 
ATOM   8151  C C   . PRO F 3 8   ? 15.203  30.179  66.414  1.000 48.906  ? 8   PRO CCC C   1 
ATOM   8152  O O   . PRO F 3 8   ? 15.296  31.196  67.078  1.000 47.029  ? 8   PRO CCC O   1 
ATOM   8153  C CB  . PRO F 3 8   ? 13.974  29.953  64.213  1.000 56.095  ? 8   PRO CCC CB  1 
ATOM   8154  C CG  . PRO F 3 8   ? 13.554  31.386  63.886  1.000 56.450  ? 8   PRO CCC CG  1 
ATOM   8155  C CD  . PRO F 3 8   ? 12.497  31.727  64.908  1.000 54.253  ? 8   PRO CCC CD  1 
ATOM   8156  N N   . ASP F 3 9   ? 16.216  29.327  66.243  1.000 52.143  ? 9   ASP CCC N   1 
ATOM   8157  C CA  . ASP F 3 9   ? 17.588  29.619  66.742  1.000 63.658  ? 9   ASP CCC CA  1 
ATOM   8158  C C   . ASP F 3 9   ? 18.214  30.712  65.867  1.000 65.807  ? 9   ASP CCC C   1 
ATOM   8159  O O   . ASP F 3 9   ? 18.840  31.642  66.399  1.000 73.440  ? 9   ASP CCC O   1 
ATOM   8160  C CB  . ASP F 3 9   ? 18.473  28.370  66.714  1.000 67.358  ? 9   ASP CCC CB  1 
ATOM   8161  C CG  . ASP F 3 9   ? 17.979  27.247  67.602  1.000 69.857  ? 9   ASP CCC CG  1 
ATOM   8162  O OD1 . ASP F 3 9   ? 17.832  26.151  67.062  1.000 79.242  ? 9   ASP CCC OD1 1 
ATOM   8163  O OD2 . ASP F 3 9   ? 17.770  27.473  68.827  1.000 72.080  ? 9   ASP CCC OD2 1 
ATOM   8164  N N   . SER F 3 10  ? 18.042  30.552  64.560  1.000 62.122  ? 10  SER CCC N   1 
ATOM   8165  C CA  . SER F 3 10  ? 18.670  31.339  63.478  1.000 54.982  ? 10  SER CCC CA  1 
ATOM   8166  C C   . SER F 3 10  ? 17.552  31.938  62.626  1.000 50.241  ? 10  SER CCC C   1 
ATOM   8167  O O   . SER F 3 10  ? 16.524  31.286  62.445  1.000 51.248  ? 10  SER CCC O   1 
ATOM   8168  C CB  . SER F 3 10  ? 19.567  30.426  62.686  1.000 59.635  ? 10  SER CCC CB  1 
ATOM   8169  O OG  . SER F 3 10  ? 19.855  30.933  61.386  1.000 73.654  ? 10  SER CCC OG  1 
ATOM   8170  N N   . LEU F 3 11  ? 17.747  33.128  62.093  1.000 48.882  ? 11  LEU CCC N   1 
ATOM   8171  C CA  . LEU F 3 11  ? 16.670  33.818  61.351  1.000 47.910  ? 11  LEU CCC CA  1 
ATOM   8172  C C   . LEU F 3 11  ? 17.284  34.839  60.411  1.000 45.811  ? 11  LEU CCC C   1 
ATOM   8173  O O   . LEU F 3 11  ? 17.913  35.744  60.908  1.000 45.990  ? 11  LEU CCC O   1 
ATOM   8174  C CB  . LEU F 3 11  ? 15.761  34.499  62.370  1.000 48.832  ? 11  LEU CCC CB  1 
ATOM   8175  C CG  . LEU F 3 11  ? 14.650  35.348  61.770  1.000 50.108  ? 11  LEU CCC CG  1 
ATOM   8176  C CD1 . LEU F 3 11  ? 13.734  34.472  60.934  1.000 54.949  ? 11  LEU CCC CD1 1 
ATOM   8177  C CD2 . LEU F 3 11  ? 13.862  36.058  62.862  1.000 51.039  ? 11  LEU CCC CD2 1 
ATOM   8178  N N   . ALA F 3 12  ? 17.094  34.676  59.107  1.000 48.322  ? 12  ALA CCC N   1 
ATOM   8179  C CA  . ALA F 3 12  ? 17.601  35.596  58.066  1.000 48.709  ? 12  ALA CCC CA  1 
ATOM   8180  C C   . ALA F 3 12  ? 16.413  36.247  57.362  1.000 42.708  ? 12  ALA CCC C   1 
ATOM   8181  O O   . ALA F 3 12  ? 15.508  35.528  56.967  1.000 45.205  ? 12  ALA CCC O   1 
ATOM   8182  C CB  . ALA F 3 12  ? 18.484  34.838  57.106  1.000 51.002  ? 12  ALA CCC CB  1 
ATOM   8183  N N   . VAL F 3 13  ? 16.454  37.558  57.182  1.000 39.463  ? 13  VAL CCC N   1 
ATOM   8184  C CA  . VAL F 3 13  ? 15.306  38.370  56.696  1.000 39.864  ? 13  VAL CCC CA  1 
ATOM   8185  C C   . VAL F 3 13  ? 15.839  39.527  55.856  1.000 41.539  ? 13  VAL CCC C   1 
ATOM   8186  O O   . VAL F 3 13  ? 16.777  40.188  56.331  1.000 45.722  ? 13  VAL CCC O   1 
ATOM   8187  C CB  . VAL F 3 13  ? 14.525  38.904  57.897  1.000 40.877  ? 13  VAL CCC CB  1 
ATOM   8188  C CG1 . VAL F 3 13  ? 13.568  40.011  57.520  1.000 42.392  ? 13  VAL CCC CG1 1 
ATOM   8189  C CG2 . VAL F 3 13  ? 13.810  37.782  58.613  1.000 42.580  ? 13  VAL CCC CG2 1 
ATOM   8190  N N   . SER F 3 14  ? 15.250  39.773  54.685  1.000 42.298  ? 14  SER CCC N   1 
ATOM   8191  C CA  . SER F 3 14  ? 15.667  40.834  53.736  1.000 42.720  ? 14  SER CCC CA  1 
ATOM   8192  C C   . SER F 3 14  ? 15.475  42.195  54.396  1.000 46.063  ? 14  SER CCC C   1 
ATOM   8193  O O   . SER F 3 14  ? 14.728  42.269  55.378  1.000 46.683  ? 14  SER CCC O   1 
ATOM   8194  C CB  . SER F 3 14  ? 14.929  40.729  52.442  1.000 44.578  ? 14  SER CCC CB  1 
ATOM   8195  O OG  . SER F 3 14  ? 15.083  39.419  51.913  1.000 49.838  ? 14  SER CCC OG  1 
ATOM   8196  N N   . LEU F 3 15  ? 16.183  43.220  53.921  1.000 51.121  ? 15  LEU CCC N   1 
ATOM   8197  C CA  . LEU F 3 15  ? 16.089  44.579  54.515  1.000 45.955  ? 15  LEU CCC CA  1 
ATOM   8198  C C   . LEU F 3 15  ? 14.659  45.074  54.316  1.000 43.756  ? 15  LEU CCC C   1 
ATOM   8199  O O   . LEU F 3 15  ? 14.107  44.919  53.198  1.000 39.639  ? 15  LEU CCC O   1 
ATOM   8200  C CB  . LEU F 3 15  ? 17.111  45.521  53.881  1.000 46.217  ? 15  LEU CCC CB  1 
ATOM   8201  C CG  . LEU F 3 15  ? 18.486  45.477  54.536  1.000 48.691  ? 15  LEU CCC CG  1 
ATOM   8202  C CD1 . LEU F 3 15  ? 19.598  45.919  53.580  1.000 51.021  ? 15  LEU CCC CD1 1 
ATOM   8203  C CD2 . LEU F 3 15  ? 18.482  46.285  55.827  1.000 50.141  ? 15  LEU CCC CD2 1 
ATOM   8204  N N   . GLY F 3 16  ? 14.067  45.585  55.391  1.000 45.388  ? 16  GLY CCC N   1 
ATOM   8205  C CA  . GLY F 3 16  ? 12.723  46.173  55.348  1.000 48.676  ? 16  GLY CCC CA  1 
ATOM   8206  C C   . GLY F 3 16  ? 11.611  45.142  55.427  1.000 50.865  ? 16  GLY CCC C   1 
ATOM   8207  O O   . GLY F 3 16  ? 10.461  45.563  55.246  1.000 51.435  ? 16  GLY CCC O   1 
ATOM   8208  N N   . GLU F 3 17  ? 11.920  43.860  55.680  1.000 52.700  ? 17  GLU CCC N   1 
ATOM   8209  C CA  . GLU F 3 17  ? 10.912  42.773  55.837  1.000 53.536  ? 17  GLU CCC CA  1 
ATOM   8210  C C   . GLU F 3 17  ? 10.621  42.578  57.325  1.000 49.770  ? 17  GLU CCC C   1 
ATOM   8211  O O   . GLU F 3 17  ? 11.272  43.229  58.134  1.000 46.493  ? 17  GLU CCC O   1 
ATOM   8212  C CB  . GLU F 3 17  ? 11.377  41.455  55.215  1.000 60.898  ? 17  GLU CCC CB  1 
ATOM   8213  C CG  . GLU F 3 17  ? 11.464  41.469  53.698  1.000 72.955  ? 17  GLU CCC CG  1 
ATOM   8214  C CD  . GLU F 3 17  ? 10.208  41.903  52.960  1.000 77.436  ? 17  GLU CCC CD  1 
ATOM   8215  O OE1 . GLU F 3 17  ? 9.347   41.040  52.687  1.000 80.833  ? 17  GLU CCC OE1 1 
ATOM   8216  O OE2 . GLU F 3 17  ? 10.105  43.108  52.652  1.000 80.811  ? 17  GLU CCC OE2 1 
ATOM   8217  N N   . ARG F 3 18  ? 9.663   41.709  57.650  1.000 51.437  ? 18  ARG CCC N   1 
ATOM   8218  C CA  . ARG F 3 18  ? 9.202   41.413  59.030  1.000 52.669  ? 18  ARG CCC CA  1 
ATOM   8219  C C   . ARG F 3 18  ? 10.020  40.241  59.578  1.000 50.210  ? 18  ARG CCC C   1 
ATOM   8220  O O   . ARG F 3 18  ? 10.165  39.233  58.868  1.000 55.756  ? 18  ARG CCC O   1 
ATOM   8221  C CB  . ARG F 3 18  ? 7.692   41.154  59.013  1.000 64.327  ? 18  ARG CCC CB  1 
ATOM   8222  C CG  . ARG F 3 18  ? 7.202   39.884  59.714  1.000 78.070  ? 18  ARG CCC CG  1 
ATOM   8223  C CD  . ARG F 3 18  ? 5.695   39.689  59.507  1.000 84.125  ? 18  ARG CCC CD  1 
ATOM   8224  N NE  . ARG F 3 18  ? 5.074   41.006  59.573  1.000 90.152  ? 18  ARG CCC NE  1 
ATOM   8225  C CZ  . ARG F 3 18  ? 4.605   41.591  60.675  1.000 98.047  ? 18  ARG CCC CZ  1 
ATOM   8226  N NH1 . ARG F 3 18  ? 4.599   40.949  61.833  1.000 109.809 ? 18  ARG CCC NH1 1 
ATOM   8227  N NH2 . ARG F 3 18  ? 4.129   42.823  60.611  1.000 96.261  ? 18  ARG CCC NH2 1 
ATOM   8228  N N   . ALA F 3 19  ? 10.550  40.386  60.791  1.000 45.644  ? 19  ALA CCC N   1 
ATOM   8229  C CA  . ALA F 3 19  ? 11.204  39.307  61.562  1.000 43.125  ? 19  ALA CCC CA  1 
ATOM   8230  C C   . ALA F 3 19  ? 10.390  39.059  62.828  1.000 44.273  ? 19  ALA CCC C   1 
ATOM   8231  O O   . ALA F 3 19  ? 10.082  40.038  63.545  1.000 44.364  ? 19  ALA CCC O   1 
ATOM   8232  C CB  . ALA F 3 19  ? 12.608  39.688  61.900  1.000 42.891  ? 19  ALA CCC CB  1 
ATOM   8233  N N   . THR F 3 20  ? 10.019  37.799  63.052  1.000 43.170  ? 20  THR CCC N   1 
ATOM   8234  C CA  . THR F 3 20  ? 9.179   37.359  64.194  1.000 44.653  ? 20  THR CCC CA  1 
ATOM   8235  C C   . THR F 3 20  ? 9.953   36.276  64.948  1.000 44.296  ? 20  THR CCC C   1 
ATOM   8236  O O   . THR F 3 20  ? 10.482  35.353  64.294  1.000 42.238  ? 20  THR CCC O   1 
ATOM   8237  C CB  . THR F 3 20  ? 7.788   36.933  63.711  1.000 46.516  ? 20  THR CCC CB  1 
ATOM   8238  O OG1 . THR F 3 20  ? 7.986   36.294  62.455  1.000 51.451  ? 20  THR CCC OG1 1 
ATOM   8239  C CG2 . THR F 3 20  ? 6.822   38.080  63.491  1.000 48.379  ? 20  THR CCC CG2 1 
ATOM   8240  N N   . ILE F 3 21  ? 10.062  36.438  66.266  1.000 47.218  ? 21  ILE CCC N   1 
ATOM   8241  C CA  . ILE F 3 21  ? 10.767  35.510  67.197  1.000 46.939  ? 21  ILE CCC CA  1 
ATOM   8242  C C   . ILE F 3 21  ? 9.750   35.070  68.251  1.000 48.428  ? 21  ILE CCC C   1 
ATOM   8243  O O   . ILE F 3 21  ? 9.025   35.957  68.768  1.000 48.869  ? 21  ILE CCC O   1 
ATOM   8244  C CB  . ILE F 3 21  ? 11.986  36.209  67.831  1.000 49.009  ? 21  ILE CCC CB  1 
ATOM   8245  C CG1 . ILE F 3 21  ? 12.893  36.820  66.762  1.000 50.536  ? 21  ILE CCC CG1 1 
ATOM   8246  C CG2 . ILE F 3 21  ? 12.764  35.256  68.738  1.000 50.770  ? 21  ILE CCC CG2 1 
ATOM   8247  C CD1 . ILE F 3 21  ? 14.016  37.667  67.305  1.000 50.830  ? 21  ILE CCC CD1 1 
ATOM   8248  N N   . ASN F 3 22  ? 9.706   33.765  68.550  1.000 47.188  ? 22  ASN CCC N   1 
ATOM   8249  C CA  . ASN F 3 22  ? 8.692   33.147  69.448  1.000 50.841  ? 22  ASN CCC CA  1 
ATOM   8250  C C   . ASN F 3 22  ? 9.349   32.677  70.754  1.000 56.428  ? 22  ASN CCC C   1 
ATOM   8251  O O   . ASN F 3 22  ? 10.425  32.035  70.677  1.000 52.935  ? 22  ASN CCC O   1 
ATOM   8252  C CB  . ASN F 3 22  ? 7.967   31.997  68.744  1.000 48.215  ? 22  ASN CCC CB  1 
ATOM   8253  C CG  . ASN F 3 22  ? 7.035   32.483  67.651  1.000 45.315  ? 22  ASN CCC CG  1 
ATOM   8254  O OD1 . ASN F 3 22  ? 6.314   33.455  67.842  1.000 39.846  ? 22  ASN CCC OD1 1 
ATOM   8255  N ND2 . ASN F 3 22  ? 7.055   31.847  66.492  1.000 45.744  ? 22  ASN CCC ND2 1 
ATOM   8256  N N   . CYS F 3 23  ? 8.712   32.989  71.897  1.000 62.825  ? 23  CYS CCC N   1 
ATOM   8257  C CA  . CYS F 3 23  ? 9.075   32.522  73.267  1.000 69.968  ? 23  CYS CCC CA  1 
ATOM   8258  C C   . CYS F 3 23  ? 7.913   31.686  73.815  1.000 68.055  ? 23  CYS CCC C   1 
ATOM   8259  O O   . CYS F 3 23  ? 6.777   32.204  73.872  1.000 62.384  ? 23  CYS CCC O   1 
ATOM   8260  C CB  . CYS F 3 23  ? 9.391   33.686  74.208  1.000 79.116  ? 23  CYS CCC CB  1 
ATOM   8261  S SG  . CYS F 3 23  ? 10.303  33.222  75.713  1.000 95.004  ? 23  CYS CCC SG  1 
ATOM   8262  N N   . LYS F 3 24  ? 8.190   30.429  74.163  1.000 68.687  ? 24  LYS CCC N   1 
ATOM   8263  C CA  . LYS F 3 24  ? 7.230   29.505  74.814  1.000 74.174  ? 24  LYS CCC CA  1 
ATOM   8264  C C   . LYS F 3 24  ? 7.678   29.325  76.263  1.000 71.067  ? 24  LYS CCC C   1 
ATOM   8265  O O   . LYS F 3 24  ? 8.821   28.831  76.453  1.000 74.591  ? 24  LYS CCC O   1 
ATOM   8266  C CB  . LYS F 3 24  ? 7.237   28.162  74.080  1.000 86.979  ? 24  LYS CCC CB  1 
ATOM   8267  C CG  . LYS F 3 24  ? 5.876   27.513  73.844  1.000 97.509  ? 24  LYS CCC CG  1 
ATOM   8268  C CD  . LYS F 3 24  ? 5.953   26.324  72.863  1.000 101.894 ? 24  LYS CCC CD  1 
ATOM   8269  C CE  . LYS F 3 24  ? 5.040   26.451  71.654  1.000 106.173 ? 24  LYS CCC CE  1 
ATOM   8270  N NZ  . LYS F 3 24  ? 3.607   26.442  72.038  1.000 110.991 ? 24  LYS CCC NZ  1 
ATOM   8271  N N   . SER F 3 25  ? 6.853   29.736  77.233  1.000 64.353  ? 25  SER CCC N   1 
ATOM   8272  C CA  . SER F 3 25  ? 7.138   29.565  78.684  1.000 65.223  ? 25  SER CCC CA  1 
ATOM   8273  C C   . SER F 3 25  ? 6.508   28.259  79.165  1.000 70.919  ? 25  SER CCC C   1 
ATOM   8274  O O   . SER F 3 25  ? 5.378   27.958  78.743  1.000 90.464  ? 25  SER CCC O   1 
ATOM   8275  C CB  . SER F 3 25  ? 6.668   30.741  79.504  1.000 61.924  ? 25  SER CCC CB  1 
ATOM   8276  O OG  . SER F 3 25  ? 5.279   30.982  79.329  1.000 59.560  ? 25  SER CCC OG  1 
ATOM   8277  N N   . SER F 3 26  ? 7.213   27.508  80.012  1.000 73.481  ? 26  SER CCC N   1 
ATOM   8278  C CA  . SER F 3 26  ? 6.749   26.211  80.573  1.000 69.881  ? 26  SER CCC CA  1 
ATOM   8279  C C   . SER F 3 26  ? 5.558   26.456  81.506  1.000 67.725  ? 26  SER CCC C   1 
ATOM   8280  O O   . SER F 3 26  ? 4.951   25.476  81.932  1.000 74.989  ? 26  SER CCC O   1 
ATOM   8281  C CB  . SER F 3 26  ? 7.862   25.482  81.290  1.000 68.789  ? 26  SER CCC CB  1 
ATOM   8282  O OG  . SER F 3 26  ? 8.220   26.158  82.494  1.000 77.244  ? 26  SER CCC OG  1 
ATOM   8283  N N   . GLN F 3 27  ? 5.220   27.711  81.796  1.000 62.190  ? 27  GLN CCC N   1 
ATOM   8284  C CA  . GLN F 3 27  ? 4.203   28.042  82.821  1.000 60.552  ? 27  GLN CCC CA  1 
ATOM   8285  C C   . GLN F 3 27  ? 3.748   29.488  82.618  1.000 55.825  ? 27  GLN CCC C   1 
ATOM   8286  O O   . GLN F 3 27  ? 4.505   30.246  82.001  1.000 62.600  ? 27  GLN CCC O   1 
ATOM   8287  C CB  . GLN F 3 27  ? 4.845   27.752  84.175  1.000 65.459  ? 27  GLN CCC CB  1 
ATOM   8288  C CG  . GLN F 3 27  ? 4.061   28.279  85.366  1.000 74.603  ? 27  GLN CCC CG  1 
ATOM   8289  C CD  . GLN F 3 27  ? 4.905   28.194  86.611  1.000 84.246  ? 27  GLN CCC CD  1 
ATOM   8290  O OE1 . GLN F 3 27  ? 5.750   27.306  86.739  1.000 84.172  ? 27  GLN CCC OE1 1 
ATOM   8291  N NE2 . GLN F 3 27  ? 4.711   29.141  87.517  1.000 87.898  ? 27  GLN CCC NE2 1 
ATOM   8292  N N   . SER F 3 28  ? 2.553   29.850  83.089  1.000 54.257  ? 28  SER CCC N   1 
ATOM   8293  C CA  . SER F 3 28  ? 1.996   31.222  82.967  1.000 54.775  ? 28  SER CCC CA  1 
ATOM   8294  C C   . SER F 3 28  ? 2.812   32.184  83.832  1.000 52.893  ? 28  SER CCC C   1 
ATOM   8295  O O   . SER F 3 28  ? 3.387   31.743  84.846  1.000 49.792  ? 28  SER CCC O   1 
ATOM   8296  C CB  . SER F 3 28  ? 0.532   31.299  83.313  1.000 56.402  ? 28  SER CCC CB  1 
ATOM   8297  O OG  . SER F 3 28  ? 0.081   32.650  83.237  1.000 64.366  ? 28  SER CCC OG  1 
ATOM   8298  N N   . VAL F 3 29  ? 2.830   33.454  83.421  1.000 54.759  ? 29  VAL CCC N   1 
ATOM   8299  C CA  . VAL F 3 29  ? 3.685   34.545  83.978  1.000 56.242  ? 29  VAL CCC CA  1 
ATOM   8300  C C   . VAL F 3 29  ? 2.810   35.784  84.136  1.000 55.422  ? 29  VAL CCC C   1 
ATOM   8301  O O   . VAL F 3 29  ? 3.330   36.903  84.007  1.000 44.624  ? 29  VAL CCC O   1 
ATOM   8302  C CB  . VAL F 3 29  ? 4.890   34.821  83.057  1.000 60.095  ? 29  VAL CCC CB  1 
ATOM   8303  C CG1 . VAL F 3 29  ? 5.848   33.637  83.035  1.000 63.089  ? 29  VAL CCC CG1 1 
ATOM   8304  C CG2 . VAL F 3 29  ? 4.457   35.173  81.637  1.000 61.042  ? 29  VAL CCC CG2 1 
ATOM   8305  N N   . LEU F 3 30  ? 1.522   35.566  84.400  1.000 61.515  ? 30  LEU CCC N   1 
ATOM   8306  C CA  . LEU F 3 30  ? 0.492   36.627  84.506  1.000 68.307  ? 30  LEU CCC CA  1 
ATOM   8307  C C   . LEU F 3 30  ? 0.352   37.042  85.981  1.000 65.643  ? 30  LEU CCC C   1 
ATOM   8308  O O   . LEU F 3 30  ? -0.018  36.194  86.805  1.000 64.982  ? 30  LEU CCC O   1 
ATOM   8309  C CB  . LEU F 3 30  ? -0.810  36.063  83.922  1.000 71.983  ? 30  LEU CCC CB  1 
ATOM   8310  C CG  . LEU F 3 30  ? -1.886  37.084  83.547  1.000 78.288  ? 30  LEU CCC CG  1 
ATOM   8311  C CD1 . LEU F 3 30  ? -2.677  37.547  84.765  1.000 82.136  ? 30  LEU CCC CD1 1 
ATOM   8312  C CD2 . LEU F 3 30  ? -1.292  38.280  82.815  1.000 81.976  ? 30  LEU CCC CD2 1 
ATOM   8313  N N   . TYR F 3 31  ? 0.680   38.294  86.309  1.000 66.092  ? 31  TYR CCC N   1 
ATOM   8314  C CA  . TYR F 3 31  ? 0.362   38.907  87.623  1.000 71.045  ? 31  TYR CCC CA  1 
ATOM   8315  C C   . TYR F 3 31  ? -1.107  39.303  87.575  1.000 73.513  ? 31  TYR CCC C   1 
ATOM   8316  O O   . TYR F 3 31  ? -1.548  40.025  86.652  1.000 67.164  ? 31  TYR CCC O   1 
ATOM   8317  C CB  . TYR F 3 31  ? 1.258   40.098  87.982  1.000 72.913  ? 31  TYR CCC CB  1 
ATOM   8318  C CG  . TYR F 3 31  ? 2.427   39.755  88.881  1.000 69.805  ? 31  TYR CCC CG  1 
ATOM   8319  C CD1 . TYR F 3 31  ? 3.373   38.813  88.504  1.000 69.022  ? 31  TYR CCC CD1 1 
ATOM   8320  C CD2 . TYR F 3 31  ? 2.588   40.371  90.109  1.000 67.995  ? 31  TYR CCC CD2 1 
ATOM   8321  C CE1 . TYR F 3 31  ? 4.435   38.482  89.330  1.000 67.666  ? 31  TYR CCC CE1 1 
ATOM   8322  C CE2 . TYR F 3 31  ? 3.663   40.078  90.932  1.000 67.747  ? 31  TYR CCC CE2 1 
ATOM   8323  C CZ  . TYR F 3 31  ? 4.580   39.117  90.548  1.000 67.474  ? 31  TYR CCC CZ  1 
ATOM   8324  O OH  . TYR F 3 31  ? 5.626   38.802  91.363  1.000 66.399  ? 31  TYR CCC OH  1 
ATOM   8325  N N   . SER F 3 32  ? -1.849  38.798  88.551  1.000 78.604  ? 32  SER CCC N   1 
ATOM   8326  C CA  . SER F 3 32  ? -3.319  38.934  88.613  1.000 70.757  ? 32  SER CCC CA  1 
ATOM   8327  C C   . SER F 3 32  ? -3.683  40.394  88.902  1.000 62.796  ? 32  SER CCC C   1 
ATOM   8328  O O   . SER F 3 32  ? -4.523  40.938  88.178  1.000 58.869  ? 32  SER CCC O   1 
ATOM   8329  C CB  . SER F 3 32  ? -3.866  37.987  89.607  1.000 71.771  ? 32  SER CCC CB  1 
ATOM   8330  O OG  . SER F 3 32  ? -4.927  37.306  88.991  1.000 85.608  ? 32  SER CCC OG  1 
ATOM   8331  N N   . SER F 3 33  ? -2.983  41.015  89.857  1.000 62.788  ? 33  SER CCC N   1 
ATOM   8332  C CA  . SER F 3 33  ? -3.254  42.358  90.447  1.000 67.097  ? 33  SER CCC CA  1 
ATOM   8333  C C   . SER F 3 33  ? -3.277  43.451  89.376  1.000 69.268  ? 33  SER CCC C   1 
ATOM   8334  O O   . SER F 3 33  ? -4.193  44.280  89.396  1.000 63.785  ? 33  SER CCC O   1 
ATOM   8335  C CB  . SER F 3 33  ? -2.248  42.686  91.524  1.000 65.027  ? 33  SER CCC CB  1 
ATOM   8336  O OG  . SER F 3 33  ? -1.028  42.013  91.269  1.000 62.752  ? 33  SER CCC OG  1 
ATOM   8337  N N   . ILE F 3 34  ? -2.271  43.484  88.508  1.000 84.091  ? 34  ILE CCC N   1 
ATOM   8338  C CA  . ILE F 3 34  ? -2.251  44.318  87.268  1.000 90.757  ? 34  ILE CCC CA  1 
ATOM   8339  C C   . ILE F 3 34  ? -2.198  43.337  86.098  1.000 86.881  ? 34  ILE CCC C   1 
ATOM   8340  O O   . ILE F 3 34  ? -1.283  42.503  86.068  1.000 102.967 ? 34  ILE CCC O   1 
ATOM   8341  C CB  . ILE F 3 34  ? -1.066  45.310  87.258  1.000 100.154 ? 34  ILE CCC CB  1 
ATOM   8342  C CG1 . ILE F 3 34  ? 0.256   44.649  87.680  1.000 108.686 ? 34  ILE CCC CG1 1 
ATOM   8343  C CG2 . ILE F 3 34  ? -1.370  46.527  88.118  1.000 99.452  ? 34  ILE CCC CG2 1 
ATOM   8344  C CD1 . ILE F 3 34  ? 1.487   45.440  87.318  1.000 114.388 ? 34  ILE CCC CD1 1 
ATOM   8345  N N   . ASN F 3 35  ? -3.159  43.407  85.188  1.000 81.250  ? 35  ASN CCC N   1 
ATOM   8346  C CA  . ASN F 3 35  ? -3.337  42.387  84.123  1.000 87.455  ? 35  ASN CCC CA  1 
ATOM   8347  C C   . ASN F 3 35  ? -2.196  42.521  83.101  1.000 78.581  ? 35  ASN CCC C   1 
ATOM   8348  O O   . ASN F 3 35  ? -2.443  43.138  82.046  1.000 87.521  ? 35  ASN CCC O   1 
ATOM   8349  C CB  . ASN F 3 35  ? -4.729  42.529  83.500  1.000 98.828  ? 35  ASN CCC CB  1 
ATOM   8350  C CG  . ASN F 3 35  ? -5.067  41.425  82.523  1.000 102.742 ? 35  ASN CCC CG  1 
ATOM   8351  O OD1 . ASN F 3 35  ? -4.860  40.238  82.801  1.000 103.600 ? 35  ASN CCC OD1 1 
ATOM   8352  N ND2 . ASN F 3 35  ? -5.596  41.822  81.380  1.000 104.046 ? 35  ASN CCC ND2 1 
ATOM   8353  N N   . LYS F 3 36  ? -1.010  41.964  83.403  1.000 67.792  ? 36  LYS CCC N   1 
ATOM   8354  C CA  . LYS F 3 36  ? 0.266   42.131  82.635  1.000 57.082  ? 36  LYS CCC CA  1 
ATOM   8355  C C   . LYS F 3 36  ? 1.153   40.882  82.737  1.000 53.244  ? 36  LYS CCC C   1 
ATOM   8356  O O   . LYS F 3 36  ? 1.322   40.365  83.853  1.000 47.242  ? 36  LYS CCC O   1 
ATOM   8357  C CB  . LYS F 3 36  ? 1.060   43.321  83.179  1.000 53.719  ? 36  LYS CCC CB  1 
ATOM   8358  C CG  . LYS F 3 36  ? 1.107   44.542  82.269  1.000 55.484  ? 36  LYS CCC CG  1 
ATOM   8359  C CD  . LYS F 3 36  ? -0.039  45.508  82.467  1.000 60.873  ? 36  LYS CCC CD  1 
ATOM   8360  C CE  . LYS F 3 36  ? 0.260   46.937  82.060  1.000 65.404  ? 36  LYS CCC CE  1 
ATOM   8361  N NZ  . LYS F 3 36  ? 0.418   47.086  80.593  1.000 71.046  ? 36  LYS CCC NZ  1 
ATOM   8362  N N   . ASN F 3 37  ? 1.702   40.411  81.613  1.000 54.540  ? 37  ASN CCC N   1 
ATOM   8363  C CA  . ASN F 3 37  ? 2.604   39.226  81.579  1.000 59.379  ? 37  ASN CCC CA  1 
ATOM   8364  C C   . ASN F 3 37  ? 4.050   39.675  81.882  1.000 61.007  ? 37  ASN CCC C   1 
ATOM   8365  O O   . ASN F 3 37  ? 4.493   40.695  81.290  1.000 65.125  ? 37  ASN CCC O   1 
ATOM   8366  C CB  . ASN F 3 37  ? 2.506   38.495  80.239  1.000 65.149  ? 37  ASN CCC CB  1 
ATOM   8367  C CG  . ASN F 3 37  ? 1.241   37.675  80.053  1.000 67.704  ? 37  ASN CCC CG  1 
ATOM   8368  O OD1 . ASN F 3 37  ? 1.100   36.562  80.592  1.000 66.205  ? 37  ASN CCC OD1 1 
ATOM   8369  N ND2 . ASN F 3 37  ? 0.347   38.198  79.226  1.000 66.533  ? 37  ASN CCC ND2 1 
ATOM   8370  N N   . TYR F 3 38  ? 4.756   38.961  82.777  1.000 60.173  ? 38  TYR CCC N   1 
ATOM   8371  C CA  . TYR F 3 38  ? 6.110   39.308  83.321  1.000 55.795  ? 38  TYR CCC CA  1 
ATOM   8372  C C   . TYR F 3 38  ? 7.201   38.653  82.459  1.000 54.317  ? 38  TYR CCC C   1 
ATOM   8373  O O   . TYR F 3 38  ? 7.898   37.728  82.921  1.000 52.895  ? 38  TYR CCC O   1 
ATOM   8374  C CB  . TYR F 3 38  ? 6.205   38.982  84.821  1.000 52.539  ? 38  TYR CCC CB  1 
ATOM   8375  C CG  . TYR F 3 38  ? 5.631   40.087  85.672  1.000 53.482  ? 38  TYR CCC CG  1 
ATOM   8376  C CD1 . TYR F 3 38  ? 6.365   40.711  86.664  1.000 58.107  ? 38  TYR CCC CD1 1 
ATOM   8377  C CD2 . TYR F 3 38  ? 4.370   40.588  85.414  1.000 56.197  ? 38  TYR CCC CD2 1 
ATOM   8378  C CE1 . TYR F 3 38  ? 5.837   41.758  87.408  1.000 58.828  ? 38  TYR CCC CE1 1 
ATOM   8379  C CE2 . TYR F 3 38  ? 3.828   41.623  86.150  1.000 57.610  ? 38  TYR CCC CE2 1 
ATOM   8380  C CZ  . TYR F 3 38  ? 4.567   42.225  87.141  1.000 55.867  ? 38  TYR CCC CZ  1 
ATOM   8381  O OH  . TYR F 3 38  ? 3.995   43.253  87.831  1.000 60.639  ? 38  TYR CCC OH  1 
ATOM   8382  N N   . LEU F 3 39  ? 7.324   39.149  81.222  1.000 53.895  ? 39  LEU CCC N   1 
ATOM   8383  C CA  . LEU F 3 39  ? 8.161   38.604  80.117  1.000 48.791  ? 39  LEU CCC CA  1 
ATOM   8384  C C   . LEU F 3 39  ? 8.817   39.805  79.449  1.000 50.013  ? 39  LEU CCC C   1 
ATOM   8385  O O   . LEU F 3 39  ? 8.094   40.788  79.170  1.000 44.307  ? 39  LEU CCC O   1 
ATOM   8386  C CB  . LEU F 3 39  ? 7.252   37.850  79.138  1.000 47.581  ? 39  LEU CCC CB  1 
ATOM   8387  C CG  . LEU F 3 39  ? 7.881   36.910  78.105  1.000 45.123  ? 39  LEU CCC CG  1 
ATOM   8388  C CD1 . LEU F 3 39  ? 8.527   37.685  76.985  1.000 46.195  ? 39  LEU CCC CD1 1 
ATOM   8389  C CD2 . LEU F 3 39  ? 8.866   35.930  78.714  1.000 43.924  ? 39  LEU CCC CD2 1 
ATOM   8390  N N   . ALA F 3 40  ? 10.135  39.744  79.263  1.000 57.735  ? 40  ALA CCC N   1 
ATOM   8391  C CA  . ALA F 3 40  ? 10.960  40.844  78.710  1.000 60.773  ? 40  ALA CCC CA  1 
ATOM   8392  C C   . ALA F 3 40  ? 11.740  40.339  77.500  1.000 56.244  ? 40  ALA CCC C   1 
ATOM   8393  O O   . ALA F 3 40  ? 11.993  39.111  77.409  1.000 48.885  ? 40  ALA CCC O   1 
ATOM   8394  C CB  . ALA F 3 40  ? 11.902  41.381  79.761  1.000 66.630  ? 40  ALA CCC CB  1 
ATOM   8395  N N   . TRP F 3 41  ? 12.108  41.272  76.622  1.000 56.946  ? 41  TRP CCC N   1 
ATOM   8396  C CA  . TRP F 3 41  ? 12.942  41.019  75.419  1.000 59.784  ? 41  TRP CCC CA  1 
ATOM   8397  C C   . TRP F 3 41  ? 14.204  41.891  75.451  1.000 52.995  ? 41  TRP CCC C   1 
ATOM   8398  O O   . TRP F 3 41  ? 14.079  43.116  75.634  1.000 48.414  ? 41  TRP CCC O   1 
ATOM   8399  C CB  . TRP F 3 41  ? 12.119  41.267  74.154  1.000 59.312  ? 41  TRP CCC CB  1 
ATOM   8400  C CG  . TRP F 3 41  ? 11.061  40.240  73.912  1.000 53.331  ? 41  TRP CCC CG  1 
ATOM   8401  C CD1 . TRP F 3 41  ? 9.742   40.330  74.240  1.000 55.619  ? 41  TRP CCC CD1 1 
ATOM   8402  C CD2 . TRP F 3 41  ? 11.234  38.964  73.279  1.000 47.228  ? 41  TRP CCC CD2 1 
ATOM   8403  N NE1 . TRP F 3 41  ? 9.078   39.201  73.842  1.000 53.611  ? 41  TRP CCC NE1 1 
ATOM   8404  C CE2 . TRP F 3 41  ? 9.973   38.347  73.249  1.000 47.511  ? 41  TRP CCC CE2 1 
ATOM   8405  C CE3 . TRP F 3 41  ? 12.320  38.292  72.716  1.000 50.667  ? 41  TRP CCC CE3 1 
ATOM   8406  C CZ2 . TRP F 3 41  ? 9.774   37.092  72.685  1.000 47.684  ? 41  TRP CCC CZ2 1 
ATOM   8407  C CZ3 . TRP F 3 41  ? 12.123  37.048  72.156  1.000 50.530  ? 41  TRP CCC CZ3 1 
ATOM   8408  C CH2 . TRP F 3 41  ? 10.865  36.458  72.147  1.000 46.513  ? 41  TRP CCC CH2 1 
ATOM   8409  N N   . TYR F 3 42  ? 15.358  41.266  75.233  1.000 50.365  ? 42  TYR CCC N   1 
ATOM   8410  C CA  . TYR F 3 42  ? 16.680  41.927  75.157  1.000 48.148  ? 42  TYR CCC CA  1 
ATOM   8411  C C   . TYR F 3 42  ? 17.261  41.742  73.753  1.000 44.270  ? 42  TYR CCC C   1 
ATOM   8412  O O   . TYR F 3 42  ? 17.072  40.685  73.114  1.000 42.468  ? 42  TYR CCC O   1 
ATOM   8413  C CB  . TYR F 3 42  ? 17.608  41.377  76.243  1.000 50.833  ? 42  TYR CCC CB  1 
ATOM   8414  C CG  . TYR F 3 42  ? 17.116  41.646  77.639  1.000 52.171  ? 42  TYR CCC CG  1 
ATOM   8415  C CD1 . TYR F 3 42  ? 16.321  40.725  78.293  1.000 54.250  ? 42  TYR CCC CD1 1 
ATOM   8416  C CD2 . TYR F 3 42  ? 17.412  42.827  78.292  1.000 55.472  ? 42  TYR CCC CD2 1 
ATOM   8417  C CE1 . TYR F 3 42  ? 15.832  40.966  79.566  1.000 56.186  ? 42  TYR CCC CE1 1 
ATOM   8418  C CE2 . TYR F 3 42  ? 16.934  43.084  79.566  1.000 60.200  ? 42  TYR CCC CE2 1 
ATOM   8419  C CZ  . TYR F 3 42  ? 16.138  42.150  80.205  1.000 60.653  ? 42  TYR CCC CZ  1 
ATOM   8420  O OH  . TYR F 3 42  ? 15.664  42.382  81.463  1.000 70.807  ? 42  TYR CCC OH  1 
ATOM   8421  N N   . GLN F 3 43  ? 17.951  42.786  73.302  1.000 41.305  ? 43  GLN CCC N   1 
ATOM   8422  C CA  . GLN F 3 43  ? 18.871  42.787  72.140  1.000 39.834  ? 43  GLN CCC CA  1 
ATOM   8423  C C   . GLN F 3 43  ? 20.302  42.770  72.679  1.000 37.697  ? 43  GLN CCC C   1 
ATOM   8424  O O   . GLN F 3 43  ? 20.581  43.520  73.631  1.000 37.942  ? 43  GLN CCC O   1 
ATOM   8425  C CB  . GLN F 3 43  ? 18.572  44.029  71.305  1.000 41.396  ? 43  GLN CCC CB  1 
ATOM   8426  C CG  . GLN F 3 43  ? 19.533  44.281  70.154  1.000 41.043  ? 43  GLN CCC CG  1 
ATOM   8427  C CD  . GLN F 3 43  ? 19.159  45.570  69.459  1.000 42.976  ? 43  GLN CCC CD  1 
ATOM   8428  O OE1 . GLN F 3 43  ? 19.466  46.670  69.928  1.000 45.996  ? 43  GLN CCC OE1 1 
ATOM   8429  N NE2 . GLN F 3 43  ? 18.442  45.448  68.351  1.000 38.207  ? 43  GLN CCC NE2 1 
ATOM   8430  N N   . GLN F 3 44  ? 21.165  41.924  72.124  1.000 38.871  ? 44  GLN CCC N   1 
ATOM   8431  C CA  . GLN F 3 44  ? 22.622  41.950  72.421  1.000 41.610  ? 44  GLN CCC CA  1 
ATOM   8432  C C   . GLN F 3 44  ? 23.399  41.902  71.103  1.000 41.134  ? 44  GLN CCC C   1 
ATOM   8433  O O   . GLN F 3 44  ? 23.187  40.945  70.321  1.000 41.688  ? 44  GLN CCC O   1 
ATOM   8434  C CB  . GLN F 3 44  ? 23.037  40.799  73.335  1.000 40.181  ? 44  GLN CCC CB  1 
ATOM   8435  C CG  . GLN F 3 44  ? 24.363  41.033  74.034  1.000 38.522  ? 44  GLN CCC CG  1 
ATOM   8436  C CD  . GLN F 3 44  ? 24.927  39.732  74.539  1.000 39.515  ? 44  GLN CCC CD  1 
ATOM   8437  O OE1 . GLN F 3 44  ? 24.458  38.641  74.192  1.000 38.502  ? 44  GLN CCC OE1 1 
ATOM   8438  N NE2 . GLN F 3 44  ? 25.955  39.846  75.359  1.000 40.478  ? 44  GLN CCC NE2 1 
ATOM   8439  N N   . LYS F 3 45  ? 24.249  42.906  70.879  1.000 38.079  ? 45  LYS CCC N   1 
ATOM   8440  C CA  . LYS F 3 45  ? 25.169  42.937  69.726  1.000 37.634  ? 45  LYS CCC CA  1 
ATOM   8441  C C   . LYS F 3 45  ? 26.548  42.549  70.215  1.000 41.117  ? 45  LYS CCC C   1 
ATOM   8442  O O   . LYS F 3 45  ? 26.848  42.659  71.401  1.000 43.670  ? 45  LYS CCC O   1 
ATOM   8443  C CB  . LYS F 3 45  ? 25.210  44.319  69.098  1.000 35.540  ? 45  LYS CCC CB  1 
ATOM   8444  C CG  . LYS F 3 45  ? 23.860  44.808  68.636  1.000 37.670  ? 45  LYS CCC CG  1 
ATOM   8445  C CD  . LYS F 3 45  ? 23.864  46.242  68.199  1.000 38.654  ? 45  LYS CCC CD  1 
ATOM   8446  C CE  . LYS F 3 45  ? 22.557  46.587  67.534  1.000 40.937  ? 45  LYS CCC CE  1 
ATOM   8447  N NZ  . LYS F 3 45  ? 22.625  47.930  66.927  1.000 43.935  ? 45  LYS CCC NZ  1 
ATOM   8448  N N   . PRO F 3 46  ? 27.413  42.081  69.297  1.000 42.508  ? 46  PRO CCC N   1 
ATOM   8449  C CA  . PRO F 3 46  ? 28.773  41.687  69.662  1.000 42.325  ? 46  PRO CCC CA  1 
ATOM   8450  C C   . PRO F 3 46  ? 29.507  42.700  70.561  1.000 47.020  ? 46  PRO CCC C   1 
ATOM   8451  O O   . PRO F 3 46  ? 29.432  43.909  70.299  1.000 45.875  ? 46  PRO CCC O   1 
ATOM   8452  C CB  . PRO F 3 46  ? 29.452  41.599  68.304  1.000 43.092  ? 46  PRO CCC CB  1 
ATOM   8453  C CG  . PRO F 3 46  ? 28.336  41.202  67.364  1.000 45.777  ? 46  PRO CCC CG  1 
ATOM   8454  C CD  . PRO F 3 46  ? 27.096  41.898  67.874  1.000 42.196  ? 46  PRO CCC CD  1 
ATOM   8455  N N   . GLY F 3 47  ? 30.171  42.181  71.607  1.000 52.379  ? 47  GLY CCC N   1 
ATOM   8456  C CA  . GLY F 3 47  ? 31.054  42.908  72.546  1.000 50.192  ? 47  GLY CCC CA  1 
ATOM   8457  C C   . GLY F 3 47  ? 30.326  44.004  73.309  1.000 51.479  ? 47  GLY CCC C   1 
ATOM   8458  O O   . GLY F 3 47  ? 30.992  44.964  73.719  1.000 61.156  ? 47  GLY CCC O   1 
ATOM   8459  N N   . GLN F 3 48  ? 29.015  43.868  73.511  1.000 51.637  ? 48  GLN CCC N   1 
ATOM   8460  C CA  . GLN F 3 48  ? 28.161  44.901  74.152  1.000 52.268  ? 48  GLN CCC CA  1 
ATOM   8461  C C   . GLN F 3 48  ? 27.283  44.233  75.203  1.000 54.845  ? 48  GLN CCC C   1 
ATOM   8462  O O   . GLN F 3 48  ? 26.934  43.057  75.087  1.000 55.366  ? 48  GLN CCC O   1 
ATOM   8463  C CB  . GLN F 3 48  ? 27.301  45.626  73.110  1.000 50.157  ? 48  GLN CCC CB  1 
ATOM   8464  C CG  . GLN F 3 48  ? 28.091  46.511  72.158  1.000 48.943  ? 48  GLN CCC CG  1 
ATOM   8465  C CD  . GLN F 3 48  ? 27.235  47.582  71.513  1.000 47.601  ? 48  GLN CCC CD  1 
ATOM   8466  O OE1 . GLN F 3 48  ? 26.045  47.416  71.272  1.000 42.610  ? 48  GLN CCC OE1 1 
ATOM   8467  N NE2 . GLN F 3 48  ? 27.838  48.713  71.195  1.000 52.103  ? 48  GLN CCC NE2 1 
ATOM   8468  N N   . PRO F 3 49  ? 26.862  44.971  76.251  1.000 60.356  ? 49  PRO CCC N   1 
ATOM   8469  C CA  . PRO F 3 49  ? 25.846  44.458  77.160  1.000 57.692  ? 49  PRO CCC CA  1 
ATOM   8470  C C   . PRO F 3 49  ? 24.517  44.289  76.430  1.000 51.094  ? 49  PRO CCC C   1 
ATOM   8471  O O   . PRO F 3 49  ? 24.260  44.938  75.414  1.000 43.545  ? 49  PRO CCC O   1 
ATOM   8472  C CB  . PRO F 3 49  ? 25.752  45.524  78.260  1.000 58.270  ? 49  PRO CCC CB  1 
ATOM   8473  C CG  . PRO F 3 49  ? 26.256  46.792  77.596  1.000 60.202  ? 49  PRO CCC CG  1 
ATOM   8474  C CD  . PRO F 3 49  ? 27.305  46.329  76.608  1.000 62.766  ? 49  PRO CCC CD  1 
ATOM   8475  N N   . PRO F 3 50  ? 23.647  43.392  76.932  1.000 46.483  ? 50  PRO CCC N   1 
ATOM   8476  C CA  . PRO F 3 50  ? 22.262  43.325  76.495  1.000 45.120  ? 50  PRO CCC CA  1 
ATOM   8477  C C   . PRO F 3 50  ? 21.551  44.659  76.733  1.000 43.113  ? 50  PRO CCC C   1 
ATOM   8478  O O   . PRO F 3 50  ? 21.858  45.325  77.700  1.000 41.789  ? 50  PRO CCC O   1 
ATOM   8479  C CB  . PRO F 3 50  ? 21.637  42.253  77.393  1.000 48.092  ? 50  PRO CCC CB  1 
ATOM   8480  C CG  . PRO F 3 50  ? 22.793  41.416  77.846  1.000 50.421  ? 50  PRO CCC CG  1 
ATOM   8481  C CD  . PRO F 3 50  ? 23.959  42.380  77.943  1.000 50.420  ? 50  PRO CCC CD  1 
ATOM   8482  N N   . LYS F 3 51  ? 20.617  44.989  75.844  1.000 44.303  ? 51  LYS CCC N   1 
ATOM   8483  C CA  . LYS F 3 51  ? 19.783  46.210  75.877  1.000 48.004  ? 51  LYS CCC CA  1 
ATOM   8484  C C   . LYS F 3 51  ? 18.323  45.762  76.034  1.000 50.952  ? 51  LYS CCC C   1 
ATOM   8485  O O   . LYS F 3 51  ? 17.877  44.896  75.250  1.000 57.240  ? 51  LYS CCC O   1 
ATOM   8486  C CB  . LYS F 3 51  ? 20.023  46.995  74.587  1.000 53.297  ? 51  LYS CCC CB  1 
ATOM   8487  C CG  . LYS F 3 51  ? 19.339  48.359  74.493  1.000 64.686  ? 51  LYS CCC CG  1 
ATOM   8488  C CD  . LYS F 3 51  ? 18.926  48.761  73.072  1.000 76.262  ? 51  LYS CCC CD  1 
ATOM   8489  C CE  . LYS F 3 51  ? 19.724  49.918  72.498  1.000 88.636  ? 51  LYS CCC CE  1 
ATOM   8490  N NZ  . LYS F 3 51  ? 19.146  51.222  72.890  1.000 93.570  ? 51  LYS CCC NZ  1 
ATOM   8491  N N   . LEU F 3 52  ? 17.608  46.307  77.018  1.000 48.584  ? 52  LEU CCC N   1 
ATOM   8492  C CA  . LEU F 3 52  ? 16.156  46.062  77.198  1.000 45.094  ? 52  LEU CCC CA  1 
ATOM   8493  C C   . LEU F 3 52  ? 15.368  46.800  76.113  1.000 41.573  ? 52  LEU CCC C   1 
ATOM   8494  O O   . LEU F 3 52  ? 15.410  48.037  76.101  1.000 35.656  ? 52  LEU CCC O   1 
ATOM   8495  C CB  . LEU F 3 52  ? 15.728  46.531  78.587  1.000 48.286  ? 52  LEU CCC CB  1 
ATOM   8496  C CG  . LEU F 3 52  ? 14.270  46.253  78.931  1.000 46.050  ? 52  LEU CCC CG  1 
ATOM   8497  C CD1 . LEU F 3 52  ? 14.041  44.774  79.191  1.000 43.213  ? 52  LEU CCC CD1 1 
ATOM   8498  C CD2 . LEU F 3 52  ? 13.856  47.073  80.135  1.000 47.059  ? 52  LEU CCC CD2 1 
ATOM   8499  N N   . LEU F 3 53  ? 14.681  46.039  75.250  1.000 45.264  ? 53  LEU CCC N   1 
ATOM   8500  C CA  . LEU F 3 53  ? 13.759  46.517  74.180  1.000 48.487  ? 53  LEU CCC CA  1 
ATOM   8501  C C   . LEU F 3 53  ? 12.343  46.624  74.735  1.000 48.262  ? 53  LEU CCC C   1 
ATOM   8502  O O   . LEU F 3 53  ? 11.730  47.711  74.619  1.000 47.840  ? 53  LEU CCC O   1 
ATOM   8503  C CB  . LEU F 3 53  ? 13.736  45.511  73.026  1.000 50.327  ? 53  LEU CCC CB  1 
ATOM   8504  C CG  . LEU F 3 53  ? 15.007  45.399  72.191  1.000 50.613  ? 53  LEU CCC CG  1 
ATOM   8505  C CD1 . LEU F 3 53  ? 14.823  44.343  71.121  1.000 47.015  ? 53  LEU CCC CD1 1 
ATOM   8506  C CD2 . LEU F 3 53  ? 15.328  46.743  71.562  1.000 53.223  ? 53  LEU CCC CD2 1 
ATOM   8507  N N   . ILE F 3 54  ? 11.834  45.509  75.265  1.000 50.743  ? 54  ILE CCC N   1 
ATOM   8508  C CA  . ILE F 3 54  ? 10.392  45.366  75.608  1.000 53.732  ? 54  ILE CCC CA  1 
ATOM   8509  C C   . ILE F 3 54  ? 10.238  44.623  76.936  1.000 50.426  ? 54  ILE CCC C   1 
ATOM   8510  O O   . ILE F 3 54  ? 10.938  43.610  77.135  1.000 41.310  ? 54  ILE CCC O   1 
ATOM   8511  C CB  . ILE F 3 54  ? 9.665   44.676  74.440  1.000 60.880  ? 54  ILE CCC CB  1 
ATOM   8512  C CG1 . ILE F 3 54  ? 9.450   45.666  73.288  1.000 61.746  ? 54  ILE CCC CG1 1 
ATOM   8513  C CG2 . ILE F 3 54  ? 8.366   44.045  74.912  1.000 63.673  ? 54  ILE CCC CG2 1 
ATOM   8514  C CD1 . ILE F 3 54  ? 9.044   45.037  71.991  1.000 61.005  ? 54  ILE CCC CD1 1 
ATOM   8515  N N   . TYR F 3 55  ? 9.358   45.138  77.808  1.000 49.798  ? 55  TYR CCC N   1 
ATOM   8516  C CA  . TYR F 3 55  ? 8.982   44.519  79.108  1.000 50.397  ? 55  TYR CCC CA  1 
ATOM   8517  C C   . TYR F 3 55  ? 7.453   44.479  79.196  1.000 53.369  ? 55  TYR CCC C   1 
ATOM   8518  O O   . TYR F 3 55  ? 6.778   45.156  78.385  1.000 49.968  ? 55  TYR CCC O   1 
ATOM   8519  C CB  . TYR F 3 55  ? 9.617   45.258  80.292  1.000 45.640  ? 55  TYR CCC CB  1 
ATOM   8520  C CG  . TYR F 3 55  ? 9.091   46.648  80.503  1.000 42.759  ? 55  TYR CCC CG  1 
ATOM   8521  C CD1 . TYR F 3 55  ? 9.658   47.733  79.861  1.000 44.867  ? 55  TYR CCC CD1 1 
ATOM   8522  C CD2 . TYR F 3 55  ? 8.022   46.881  81.335  1.000 41.925  ? 55  TYR CCC CD2 1 
ATOM   8523  C CE1 . TYR F 3 55  ? 9.153   49.012  80.012  1.000 44.252  ? 55  TYR CCC CE1 1 
ATOM   8524  C CE2 . TYR F 3 55  ? 7.505   48.153  81.506  1.000 43.472  ? 55  TYR CCC CE2 1 
ATOM   8525  C CZ  . TYR F 3 55  ? 8.078   49.221  80.849  1.000 42.665  ? 55  TYR CCC CZ  1 
ATOM   8526  O OH  . TYR F 3 55  ? 7.572   50.465  81.012  1.000 42.823  ? 55  TYR CCC OH  1 
ATOM   8527  N N   . TRP F 3 56  ? 6.943   43.708  80.165  1.000 55.711  ? 56  TRP CCC N   1 
ATOM   8528  C CA  . TRP F 3 56  ? 5.511   43.336  80.302  1.000 50.990  ? 56  TRP CCC CA  1 
ATOM   8529  C C   . TRP F 3 56  ? 5.005   42.836  78.944  1.000 50.289  ? 56  TRP CCC C   1 
ATOM   8530  O O   . TRP F 3 56  ? 3.959   43.332  78.457  1.000 41.578  ? 56  TRP CCC O   1 
ATOM   8531  C CB  . TRP F 3 56  ? 4.688   44.513  80.843  1.000 50.159  ? 56  TRP CCC CB  1 
ATOM   8532  C CG  . TRP F 3 56  ? 4.754   44.697  82.327  1.000 47.609  ? 56  TRP CCC CG  1 
ATOM   8533  C CD1 . TRP F 3 56  ? 5.061   43.754  83.265  1.000 49.426  ? 56  TRP CCC CD1 1 
ATOM   8534  C CD2 . TRP F 3 56  ? 4.433   45.894  83.054  1.000 41.756  ? 56  TRP CCC CD2 1 
ATOM   8535  N NE1 . TRP F 3 56  ? 4.974   44.289  84.523  1.000 47.039  ? 56  TRP CCC NE1 1 
ATOM   8536  C CE2 . TRP F 3 56  ? 4.575   45.595  84.426  1.000 42.205  ? 56  TRP CCC CE2 1 
ATOM   8537  C CE3 . TRP F 3 56  ? 4.041   47.180  82.675  1.000 42.383  ? 56  TRP CCC CE3 1 
ATOM   8538  C CZ2 . TRP F 3 56  ? 4.366   46.541  85.421  1.000 42.376  ? 56  TRP CCC CZ2 1 
ATOM   8539  C CZ3 . TRP F 3 56  ? 3.829   48.119  83.657  1.000 44.657  ? 56  TRP CCC CZ3 1 
ATOM   8540  C CH2 . TRP F 3 56  ? 3.986   47.799  85.010  1.000 46.233  ? 56  TRP CCC CH2 1 
ATOM   8541  N N   . ALA F 3 57  ? 5.783   41.931  78.339  1.000 50.735  ? 57  ALA CCC N   1 
ATOM   8542  C CA  . ALA F 3 57  ? 5.453   41.157  77.120  1.000 50.595  ? 57  ALA CCC CA  1 
ATOM   8543  C C   . ALA F 3 57  ? 5.263   42.054  75.893  1.000 47.099  ? 57  ALA CCC C   1 
ATOM   8544  O O   . ALA F 3 57  ? 5.470   41.500  74.787  1.000 42.583  ? 57  ALA CCC O   1 
ATOM   8545  C CB  . ALA F 3 57  ? 4.223   40.324  77.360  1.000 53.584  ? 57  ALA CCC CB  1 
ATOM   8546  N N   . SER F 3 58  ? 4.918   43.345  76.069  1.000 47.777  ? 58  SER CCC N   1 
ATOM   8547  C CA  . SER F 3 58  ? 4.494   44.244  74.961  1.000 52.493  ? 58  SER CCC CA  1 
ATOM   8548  C C   . SER F 3 58  ? 4.699   45.754  75.205  1.000 56.890  ? 58  SER CCC C   1 
ATOM   8549  O O   . SER F 3 58  ? 4.300   46.514  74.304  1.000 53.533  ? 58  SER CCC O   1 
ATOM   8550  C CB  . SER F 3 58  ? 3.055   43.999  74.657  1.000 55.042  ? 58  SER CCC CB  1 
ATOM   8551  O OG  . SER F 3 58  ? 2.248   44.595  75.659  1.000 61.514  ? 58  SER CCC OG  1 
ATOM   8552  N N   . THR F 3 59  ? 5.239   46.217  76.342  1.000 60.851  ? 59  THR CCC N   1 
ATOM   8553  C CA  . THR F 3 59  ? 5.536   47.665  76.568  1.000 58.478  ? 59  THR CCC CA  1 
ATOM   8554  C C   . THR F 3 59  ? 6.964   47.972  76.097  1.000 58.524  ? 59  THR CCC C   1 
ATOM   8555  O O   . THR F 3 59  ? 7.900   47.246  76.514  1.000 54.810  ? 59  THR CCC O   1 
ATOM   8556  C CB  . THR F 3 59  ? 5.342   48.059  78.035  1.000 58.705  ? 59  THR CCC CB  1 
ATOM   8557  O OG1 . THR F 3 59  ? 4.039   47.620  78.403  1.000 68.851  ? 59  THR CCC OG1 1 
ATOM   8558  C CG2 . THR F 3 59  ? 5.464   49.544  78.290  1.000 54.612  ? 59  THR CCC CG2 1 
ATOM   8559  N N   . ARG F 3 60  ? 7.119   49.008  75.268  1.000 54.127  ? 60  ARG CCC N   1 
ATOM   8560  C CA  . ARG F 3 60  ? 8.431   49.463  74.738  1.000 54.530  ? 60  ARG CCC CA  1 
ATOM   8561  C C   . ARG F 3 60  ? 9.186   50.256  75.809  1.000 58.194  ? 60  ARG CCC C   1 
ATOM   8562  O O   . ARG F 3 60  ? 8.608   51.227  76.334  1.000 62.187  ? 60  ARG CCC O   1 
ATOM   8563  C CB  . ARG F 3 60  ? 8.230   50.345  73.507  1.000 54.374  ? 60  ARG CCC CB  1 
ATOM   8564  C CG  . ARG F 3 60  ? 8.480   49.625  72.196  1.000 55.828  ? 60  ARG CCC CG  1 
ATOM   8565  C CD  . ARG F 3 60  ? 8.532   50.636  71.073  1.000 63.047  ? 60  ARG CCC CD  1 
ATOM   8566  N NE  . ARG F 3 60  ? 7.240   51.265  70.848  1.000 63.769  ? 60  ARG CCC NE  1 
ATOM   8567  C CZ  . ARG F 3 60  ? 6.224   50.699  70.202  1.000 69.487  ? 60  ARG CCC CZ  1 
ATOM   8568  N NH1 . ARG F 3 60  ? 6.309   49.474  69.702  1.000 67.314  ? 60  ARG CCC NH1 1 
ATOM   8569  N NH2 . ARG F 3 60  ? 5.099   51.371  70.062  1.000 80.519  ? 60  ARG CCC NH2 1 
ATOM   8570  N N   . GLU F 3 61  ? 10.428  49.865  76.114  1.000 58.076  ? 61  GLU CCC N   1 
ATOM   8571  C CA  . GLU F 3 61  ? 11.355  50.646  76.981  1.000 60.107  ? 61  GLU CCC CA  1 
ATOM   8572  C C   . GLU F 3 61  ? 11.594  51.986  76.275  1.000 61.809  ? 61  GLU CCC C   1 
ATOM   8573  O O   . GLU F 3 61  ? 11.554  51.999  75.033  1.000 68.635  ? 61  GLU CCC O   1 
ATOM   8574  C CB  . GLU F 3 61  ? 12.626  49.830  77.239  1.000 62.750  ? 61  GLU CCC CB  1 
ATOM   8575  C CG  . GLU F 3 61  ? 13.736  50.570  77.978  1.000 67.849  ? 61  GLU CCC CG  1 
ATOM   8576  C CD  . GLU F 3 61  ? 13.478  50.905  79.433  1.000 69.474  ? 61  GLU CCC CD  1 
ATOM   8577  O OE1 . GLU F 3 61  ? 14.252  50.442  80.296  1.000 73.686  ? 61  GLU CCC OE1 1 
ATOM   8578  O OE2 . GLU F 3 61  ? 12.523  51.647  79.698  1.000 72.308  ? 61  GLU CCC OE2 1 
ATOM   8579  N N   . SER F 3 62  ? 11.772  53.088  77.005  1.000 62.845  ? 62  SER CCC N   1 
ATOM   8580  C CA  . SER F 3 62  ? 11.824  54.427  76.361  1.000 66.174  ? 62  SER CCC CA  1 
ATOM   8581  C C   . SER F 3 62  ? 13.056  54.468  75.451  1.000 60.725  ? 62  SER CCC C   1 
ATOM   8582  O O   . SER F 3 62  ? 14.013  53.712  75.705  1.000 52.271  ? 62  SER CCC O   1 
ATOM   8583  C CB  . SER F 3 62  ? 11.756  55.588  77.330  1.000 70.549  ? 62  SER CCC CB  1 
ATOM   8584  O OG  . SER F 3 62  ? 12.649  55.417  78.410  1.000 78.530  ? 62  SER CCC OG  1 
ATOM   8585  N N   . GLY F 3 63  ? 12.960  55.252  74.375  1.000 60.011  ? 63  GLY CCC N   1 
ATOM   8586  C CA  . GLY F 3 63  ? 13.966  55.360  73.305  1.000 58.477  ? 63  GLY CCC CA  1 
ATOM   8587  C C   . GLY F 3 63  ? 14.107  54.082  72.503  1.000 52.493  ? 63  GLY CCC C   1 
ATOM   8588  O O   . GLY F 3 63  ? 15.206  53.834  71.983  1.000 56.472  ? 63  GLY CCC O   1 
ATOM   8589  N N   . VAL F 3 64  ? 13.042  53.293  72.388  1.000 46.507  ? 64  VAL CCC N   1 
ATOM   8590  C CA  . VAL F 3 64  ? 13.011  52.135  71.454  1.000 44.558  ? 64  VAL CCC CA  1 
ATOM   8591  C C   . VAL F 3 64  ? 12.091  52.497  70.302  1.000 43.831  ? 64  VAL CCC C   1 
ATOM   8592  O O   . VAL F 3 64  ? 10.961  52.891  70.525  1.000 38.240  ? 64  VAL CCC O   1 
ATOM   8593  C CB  . VAL F 3 64  ? 12.574  50.838  72.150  1.000 43.749  ? 64  VAL CCC CB  1 
ATOM   8594  C CG1 . VAL F 3 64  ? 12.408  49.699  71.163  1.000 44.859  ? 64  VAL CCC CG1 1 
ATOM   8595  C CG2 . VAL F 3 64  ? 13.555  50.437  73.235  1.000 43.010  ? 64  VAL CCC CG2 1 
ATOM   8596  N N   . PRO F 3 65  ? 12.542  52.370  69.041  1.000 54.388  ? 65  PRO CCC N   1 
ATOM   8597  C CA  . PRO F 3 65  ? 11.747  52.823  67.900  1.000 57.874  ? 65  PRO CCC CA  1 
ATOM   8598  C C   . PRO F 3 65  ? 10.458  52.000  67.768  1.000 53.844  ? 65  PRO CCC C   1 
ATOM   8599  O O   . PRO F 3 65  ? 10.381  50.913  68.328  1.000 43.309  ? 65  PRO CCC O   1 
ATOM   8600  C CB  . PRO F 3 65  ? 12.615  52.594  66.646  1.000 67.163  ? 65  PRO CCC CB  1 
ATOM   8601  C CG  . PRO F 3 65  ? 13.982  52.091  67.173  1.000 71.733  ? 65  PRO CCC CG  1 
ATOM   8602  C CD  . PRO F 3 65  ? 13.823  51.756  68.645  1.000 63.977  ? 65  PRO CCC CD  1 
ATOM   8603  N N   . ASP F 3 66  ? 9.535   52.496  66.953  1.000 52.595  ? 66  ASP CCC N   1 
ATOM   8604  C CA  . ASP F 3 66  ? 8.189   51.909  66.781  1.000 54.284  ? 66  ASP CCC CA  1 
ATOM   8605  C C   . ASP F 3 66  ? 8.290   50.508  66.189  1.000 48.657  ? 66  ASP CCC C   1 
ATOM   8606  O O   . ASP F 3 66  ? 7.379   49.713  66.450  1.000 55.070  ? 66  ASP CCC O   1 
ATOM   8607  C CB  . ASP F 3 66  ? 7.307   52.822  65.934  1.000 61.147  ? 66  ASP CCC CB  1 
ATOM   8608  C CG  . ASP F 3 66  ? 7.056   54.152  66.618  1.000 72.693  ? 66  ASP CCC CG  1 
ATOM   8609  O OD1 . ASP F 3 66  ? 6.914   54.162  67.872  1.000 83.138  ? 66  ASP CCC OD1 1 
ATOM   8610  O OD2 . ASP F 3 66  ? 7.038   55.167  65.901  1.000 78.981  ? 66  ASP CCC OD2 1 
ATOM   8611  N N   . ARG F 3 67  ? 9.343   50.206  65.440  1.000 47.884  ? 67  ARG CCC N   1 
ATOM   8612  C CA  . ARG F 3 67  ? 9.369   48.993  64.580  1.000 49.310  ? 67  ARG CCC CA  1 
ATOM   8613  C C   . ARG F 3 67  ? 9.511   47.728  65.437  1.000 45.846  ? 67  ARG CCC C   1 
ATOM   8614  O O   . ARG F 3 67  ? 9.248   46.629  64.925  1.000 49.029  ? 67  ARG CCC O   1 
ATOM   8615  C CB  . ARG F 3 67  ? 10.441  49.132  63.496  1.000 53.586  ? 67  ARG CCC CB  1 
ATOM   8616  C CG  . ARG F 3 67  ? 11.868  49.254  64.008  1.000 59.239  ? 67  ARG CCC CG  1 
ATOM   8617  C CD  . ARG F 3 67  ? 12.900  48.901  62.943  1.000 56.940  ? 67  ARG CCC CD  1 
ATOM   8618  N NE  . ARG F 3 67  ? 14.253  48.789  63.469  1.000 50.838  ? 67  ARG CCC NE  1 
ATOM   8619  C CZ  . ARG F 3 67  ? 14.999  49.808  63.896  1.000 51.886  ? 67  ARG CCC CZ  1 
ATOM   8620  N NH1 . ARG F 3 67  ? 14.541  51.044  63.872  1.000 60.391  ? 67  ARG CCC NH1 1 
ATOM   8621  N NH2 . ARG F 3 67  ? 16.219  49.597  64.348  1.000 48.441  ? 67  ARG CCC NH2 1 
ATOM   8622  N N   . PHE F 3 68  ? 9.886   47.880  66.702  1.000 46.525  ? 68  PHE CCC N   1 
ATOM   8623  C CA  . PHE F 3 68  ? 9.870   46.791  67.709  1.000 50.608  ? 68  PHE CCC CA  1 
ATOM   8624  C C   . PHE F 3 68  ? 8.505   46.779  68.390  1.000 53.591  ? 68  PHE CCC C   1 
ATOM   8625  O O   . PHE F 3 68  ? 8.083   47.815  68.896  1.000 55.112  ? 68  PHE CCC O   1 
ATOM   8626  C CB  . PHE F 3 68  ? 10.960  46.985  68.762  1.000 51.625  ? 68  PHE CCC CB  1 
ATOM   8627  C CG  . PHE F 3 68  ? 12.351  46.847  68.212  1.000 48.202  ? 68  PHE CCC CG  1 
ATOM   8628  C CD1 . PHE F 3 68  ? 13.038  47.955  67.743  1.000 46.027  ? 68  PHE CCC CD1 1 
ATOM   8629  C CD2 . PHE F 3 68  ? 12.941  45.601  68.123  1.000 47.001  ? 68  PHE CCC CD2 1 
ATOM   8630  C CE1 . PHE F 3 68  ? 14.314  47.815  67.236  1.000 46.571  ? 68  PHE CCC CE1 1 
ATOM   8631  C CE2 . PHE F 3 68  ? 14.209  45.461  67.588  1.000 48.613  ? 68  PHE CCC CE2 1 
ATOM   8632  C CZ  . PHE F 3 68  ? 14.891  46.571  67.149  1.000 49.969  ? 68  PHE CCC CZ  1 
ATOM   8633  N N   . SER F 3 69  ? 7.829   45.635  68.397  1.000 53.314  ? 69  SER CCC N   1 
ATOM   8634  C CA  . SER F 3 69  ? 6.560   45.445  69.135  1.000 51.146  ? 69  SER CCC CA  1 
ATOM   8635  C C   . SER F 3 69  ? 6.543   44.031  69.703  1.000 52.500  ? 69  SER CCC C   1 
ATOM   8636  O O   . SER F 3 69  ? 7.080   43.115  69.056  1.000 52.003  ? 69  SER CCC O   1 
ATOM   8637  C CB  . SER F 3 69  ? 5.386   45.708  68.258  1.000 50.496  ? 69  SER CCC CB  1 
ATOM   8638  O OG  . SER F 3 69  ? 5.334   44.748  67.221  1.000 52.700  ? 69  SER CCC OG  1 
ATOM   8639  N N   . GLY F 3 70  ? 6.001   43.886  70.905  1.000 56.558  ? 70  GLY CCC N   1 
ATOM   8640  C CA  . GLY F 3 70  ? 5.904   42.590  71.596  1.000 60.319  ? 70  GLY CCC CA  1 
ATOM   8641  C C   . GLY F 3 70  ? 4.453   42.221  71.781  1.000 61.980  ? 70  GLY CCC C   1 
ATOM   8642  O O   . GLY F 3 70  ? 3.627   43.150  71.860  1.000 54.886  ? 70  GLY CCC O   1 
ATOM   8643  N N   . SER F 3 71  ? 4.144   40.926  71.844  1.000 67.147  ? 71  SER CCC N   1 
ATOM   8644  C CA  . SER F 3 71  ? 2.750   40.437  71.973  1.000 64.666  ? 71  SER CCC CA  1 
ATOM   8645  C C   . SER F 3 71  ? 2.735   39.026  72.564  1.000 65.156  ? 71  SER CCC C   1 
ATOM   8646  O O   . SER F 3 71  ? 3.829   38.484  72.900  1.000 58.406  ? 71  SER CCC O   1 
ATOM   8647  C CB  . SER F 3 71  ? 2.062   40.495  70.650  1.000 63.401  ? 71  SER CCC CB  1 
ATOM   8648  O OG  . SER F 3 71  ? 2.820   39.775  69.692  1.000 72.964  ? 71  SER CCC OG  1 
ATOM   8649  N N   . GLY F 3 72  ? 1.525   38.487  72.720  1.000 70.341  ? 72  GLY CCC N   1 
ATOM   8650  C CA  . GLY F 3 72  ? 1.265   37.140  73.257  1.000 70.218  ? 72  GLY CCC CA  1 
ATOM   8651  C C   . GLY F 3 72  ? 0.575   37.220  74.603  1.000 67.005  ? 72  GLY CCC C   1 
ATOM   8652  O O   . GLY F 3 72  ? 0.416   38.363  75.136  1.000 52.331  ? 72  GLY CCC O   1 
ATOM   8653  N N   . SER F 3 73  ? 0.183   36.053  75.127  1.000 63.718  ? 73  SER CCC N   1 
ATOM   8654  C CA  . SER F 3 73  ? -0.492  35.912  76.440  1.000 63.008  ? 73  SER CCC CA  1 
ATOM   8655  C C   . SER F 3 73  ? -0.357  34.484  76.973  1.000 56.439  ? 73  SER CCC C   1 
ATOM   8656  O O   . SER F 3 73  ? -0.101  33.571  76.178  1.000 52.271  ? 73  SER CCC O   1 
ATOM   8657  C CB  . SER F 3 73  ? -1.924  36.308  76.349  1.000 62.946  ? 73  SER CCC CB  1 
ATOM   8658  O OG  . SER F 3 73  ? -2.361  36.750  77.621  1.000 66.546  ? 73  SER CCC OG  1 
ATOM   8659  N N   . GLY F 3 74  ? -0.512  34.315  78.286  1.000 53.333  ? 74  GLY CCC N   1 
ATOM   8660  C CA  . GLY F 3 74  ? -0.440  32.979  78.896  1.000 55.531  ? 74  GLY CCC CA  1 
ATOM   8661  C C   . GLY F 3 74  ? 0.964   32.435  78.784  1.000 53.914  ? 74  GLY CCC C   1 
ATOM   8662  O O   . GLY F 3 74  ? 1.788   32.823  79.649  1.000 64.822  ? 74  GLY CCC O   1 
ATOM   8663  N N   . THR F 3 75  ? 1.246   31.609  77.766  1.000 48.545  ? 75  THR CCC N   1 
ATOM   8664  C CA  . THR F 3 75  ? 2.571   30.937  77.622  1.000 54.010  ? 75  THR CCC CA  1 
ATOM   8665  C C   . THR F 3 75  ? 3.219   31.165  76.245  1.000 60.956  ? 75  THR CCC C   1 
ATOM   8666  O O   . THR F 3 75  ? 4.406   30.748  76.083  1.000 70.237  ? 75  THR CCC O   1 
ATOM   8667  C CB  . THR F 3 75  ? 2.506   29.426  77.889  1.000 51.016  ? 75  THR CCC CB  1 
ATOM   8668  O OG1 . THR F 3 75  ? 1.853   28.788  76.792  1.000 49.951  ? 75  THR CCC OG1 1 
ATOM   8669  C CG2 . THR F 3 75  ? 1.818   29.085  79.192  1.000 53.265  ? 75  THR CCC CG2 1 
ATOM   8670  N N   . ASP F 3 76  ? 2.517   31.769  75.278  1.000 59.775  ? 76  ASP CCC N   1 
ATOM   8671  C CA  . ASP F 3 76  ? 3.057   31.966  73.902  1.000 57.637  ? 76  ASP CCC CA  1 
ATOM   8672  C C   . ASP F 3 76  ? 3.228   33.466  73.671  1.000 57.198  ? 76  ASP CCC C   1 
ATOM   8673  O O   . ASP F 3 76  ? 2.209   34.199  73.767  1.000 50.349  ? 76  ASP CCC O   1 
ATOM   8674  C CB  . ASP F 3 76  ? 2.180   31.269  72.859  1.000 62.594  ? 76  ASP CCC CB  1 
ATOM   8675  C CG  . ASP F 3 76  ? 2.129   29.751  73.043  1.000 72.199  ? 76  ASP CCC CG  1 
ATOM   8676  O OD1 . ASP F 3 76  ? 1.017   29.195  73.161  1.000 75.608  ? 76  ASP CCC OD1 1 
ATOM   8677  O OD2 . ASP F 3 76  ? 3.209   29.123  73.079  1.000 73.084  ? 76  ASP CCC OD2 1 
ATOM   8678  N N   . PHE F 3 77  ? 4.475   33.895  73.427  1.000 58.125  ? 77  PHE CCC N   1 
ATOM   8679  C CA  . PHE F 3 77  ? 4.872   35.324  73.274  1.000 54.991  ? 77  PHE CCC CA  1 
ATOM   8680  C C   . PHE F 3 77  ? 5.701   35.520  72.003  1.000 51.041  ? 77  PHE CCC C   1 
ATOM   8681  O O   . PHE F 3 77  ? 6.356   34.566  71.538  1.000 44.771  ? 77  PHE CCC O   1 
ATOM   8682  C CB  . PHE F 3 77  ? 5.663   35.799  74.495  1.000 53.645  ? 77  PHE CCC CB  1 
ATOM   8683  C CG  . PHE F 3 77  ? 4.879   35.759  75.778  1.000 47.962  ? 77  PHE CCC CG  1 
ATOM   8684  C CD1 . PHE F 3 77  ? 4.030   36.802  76.112  1.000 44.226  ? 77  PHE CCC CD1 1 
ATOM   8685  C CD2 . PHE F 3 77  ? 4.962   34.663  76.630  1.000 42.506  ? 77  PHE CCC CD2 1 
ATOM   8686  C CE1 . PHE F 3 77  ? 3.293   36.753  77.284  1.000 42.064  ? 77  PHE CCC CE1 1 
ATOM   8687  C CE2 . PHE F 3 77  ? 4.222   34.624  77.804  1.000 40.024  ? 77  PHE CCC CE2 1 
ATOM   8688  C CZ  . PHE F 3 77  ? 3.382   35.661  78.125  1.000 39.283  ? 77  PHE CCC CZ  1 
ATOM   8689  N N   . THR F 3 78  ? 5.692   36.750  71.486  1.000 50.394  ? 78  THR CCC N   1 
ATOM   8690  C CA  . THR F 3 78  ? 6.304   37.114  70.189  1.000 51.694  ? 78  THR CCC CA  1 
ATOM   8691  C C   . THR F 3 78  ? 6.955   38.490  70.287  1.000 52.832  ? 78  THR CCC C   1 
ATOM   8692  O O   . THR F 3 78  ? 6.271   39.449  70.731  1.000 49.743  ? 78  THR CCC O   1 
ATOM   8693  C CB  . THR F 3 78  ? 5.254   37.068  69.076  1.000 53.443  ? 78  THR CCC CB  1 
ATOM   8694  O OG1 . THR F 3 78  ? 5.133   35.682  68.776  1.000 58.705  ? 78  THR CCC OG1 1 
ATOM   8695  C CG2 . THR F 3 78  ? 5.616   37.824  67.818  1.000 52.997  ? 78  THR CCC CG2 1 
ATOM   8696  N N   . LEU F 3 79  ? 8.217   38.552  69.851  1.000 52.931  ? 79  LEU CCC N   1 
ATOM   8697  C CA  . LEU F 3 79  ? 8.901   39.810  69.464  1.000 51.018  ? 79  LEU CCC CA  1 
ATOM   8698  C C   . LEU F 3 79  ? 8.866   39.936  67.938  1.000 47.572  ? 79  LEU CCC C   1 
ATOM   8699  O O   . LEU F 3 79  ? 9.186   38.943  67.233  1.000 44.773  ? 79  LEU CCC O   1 
ATOM   8700  C CB  . LEU F 3 79  ? 10.338  39.790  69.985  1.000 51.505  ? 79  LEU CCC CB  1 
ATOM   8701  C CG  . LEU F 3 79  ? 11.127  41.072  69.717  1.000 50.811  ? 79  LEU CCC CG  1 
ATOM   8702  C CD1 . LEU F 3 79  ? 10.529  42.255  70.461  1.000 50.421  ? 79  LEU CCC CD1 1 
ATOM   8703  C CD2 . LEU F 3 79  ? 12.579  40.883  70.090  1.000 51.236  ? 79  LEU CCC CD2 1 
ATOM   8704  N N   . THR F 3 80  ? 8.485   41.117  67.459  1.000 45.527  ? 80  THR CCC N   1 
ATOM   8705  C CA  . THR F 3 80  ? 8.310   41.409  66.022  1.000 47.524  ? 80  THR CCC CA  1 
ATOM   8706  C C   . THR F 3 80  ? 9.076   42.680  65.671  1.000 50.553  ? 80  THR CCC C   1 
ATOM   8707  O O   . THR F 3 80  ? 8.861   43.720  66.321  1.000 52.551  ? 80  THR CCC O   1 
ATOM   8708  C CB  . THR F 3 80  ? 6.835   41.593  65.650  1.000 48.223  ? 80  THR CCC CB  1 
ATOM   8709  O OG1 . THR F 3 80  ? 6.100   40.435  66.045  1.000 46.546  ? 80  THR CCC OG1 1 
ATOM   8710  C CG2 . THR F 3 80  ? 6.650   41.857  64.174  1.000 48.737  ? 80  THR CCC CG2 1 
ATOM   8711  N N   . ILE F 3 81  ? 9.930   42.578  64.659  1.000 53.327  ? 81  ILE CCC N   1 
ATOM   8712  C CA  . ILE F 3 81  ? 10.574  43.728  63.968  1.000 49.816  ? 81  ILE CCC CA  1 
ATOM   8713  C C   . ILE F 3 81  ? 9.906   43.816  62.599  1.000 48.091  ? 81  ILE CCC C   1 
ATOM   8714  O O   . ILE F 3 81  ? 10.159  42.920  61.785  1.000 58.348  ? 81  ILE CCC O   1 
ATOM   8715  C CB  . ILE F 3 81  ? 12.103  43.516  63.866  1.000 53.853  ? 81  ILE CCC CB  1 
ATOM   8716  C CG1 . ILE F 3 81  ? 12.725  43.185  65.228  1.000 56.231  ? 81  ILE CCC CG1 1 
ATOM   8717  C CG2 . ILE F 3 81  ? 12.772  44.711  63.223  1.000 57.923  ? 81  ILE CCC CG2 1 
ATOM   8718  C CD1 . ILE F 3 81  ? 14.201  42.913  65.228  1.000 53.752  ? 81  ILE CCC CD1 1 
ATOM   8719  N N   . SER F 3 82  ? 9.023   44.788  62.389  1.000 44.224  ? 82  SER CCC N   1 
ATOM   8720  C CA  . SER F 3 82  ? 8.629   45.250  61.033  1.000 47.253  ? 82  SER CCC CA  1 
ATOM   8721  C C   . SER F 3 82  ? 9.792   46.074  60.479  1.000 54.257  ? 82  SER CCC C   1 
ATOM   8722  O O   . SER F 3 82  ? 10.412  46.770  61.295  1.000 78.733  ? 82  SER CCC O   1 
ATOM   8723  C CB  . SER F 3 82  ? 7.399   46.074  61.097  1.000 44.860  ? 82  SER CCC CB  1 
ATOM   8724  O OG  . SER F 3 82  ? 7.591   47.139  62.014  1.000 39.360  ? 82  SER CCC OG  1 
ATOM   8725  N N   . SER F 3 83  ? 10.098  46.015  59.181  1.000 54.738  ? 83  SER CCC N   1 
ATOM   8726  C CA  . SER F 3 83  ? 11.247  46.737  58.560  1.000 50.262  ? 83  SER CCC CA  1 
ATOM   8727  C C   . SER F 3 83  ? 12.553  46.409  59.286  1.000 46.185  ? 83  SER CCC C   1 
ATOM   8728  O O   . SER F 3 83  ? 13.071  47.281  60.011  1.000 45.886  ? 83  SER CCC O   1 
ATOM   8729  C CB  . SER F 3 83  ? 11.040  48.228  58.512  1.000 50.773  ? 83  SER CCC CB  1 
ATOM   8730  O OG  . SER F 3 83  ? 10.425  48.610  57.299  1.000 55.707  ? 83  SER CCC OG  1 
ATOM   8731  N N   . LEU F 3 84  ? 13.099  45.218  59.077  1.000 43.271  ? 84  LEU CCC N   1 
ATOM   8732  C CA  . LEU F 3 84  ? 14.404  44.878  59.687  1.000 38.356  ? 84  LEU CCC CA  1 
ATOM   8733  C C   . LEU F 3 84  ? 15.417  45.859  59.112  1.000 36.346  ? 84  LEU CCC C   1 
ATOM   8734  O O   . LEU F 3 84  ? 15.425  46.041  57.913  1.000 32.690  ? 84  LEU CCC O   1 
ATOM   8735  C CB  . LEU F 3 84  ? 14.789  43.438  59.378  1.000 38.087  ? 84  LEU CCC CB  1 
ATOM   8736  C CG  . LEU F 3 84  ? 16.057  42.993  60.089  1.000 39.566  ? 84  LEU CCC CG  1 
ATOM   8737  C CD1 . LEU F 3 84  ? 15.770  42.623  61.523  1.000 38.931  ? 84  LEU CCC CD1 1 
ATOM   8738  C CD2 . LEU F 3 84  ? 16.703  41.840  59.362  1.000 42.846  ? 84  LEU CCC CD2 1 
ATOM   8739  N N   . GLN F 3 85  ? 16.167  46.521  59.981  1.000 40.893  ? 85  GLN CCC N   1 
ATOM   8740  C CA  . GLN F 3 85  ? 17.215  47.496  59.613  1.000 43.767  ? 85  GLN CCC CA  1 
ATOM   8741  C C   . GLN F 3 85  ? 18.580  46.824  59.774  1.000 46.657  ? 85  GLN CCC C   1 
ATOM   8742  O O   . GLN F 3 85  ? 18.639  45.793  60.456  1.000 45.290  ? 85  GLN CCC O   1 
ATOM   8743  C CB  . GLN F 3 85  ? 17.105  48.705  60.525  1.000 44.836  ? 85  GLN CCC CB  1 
ATOM   8744  C CG  . GLN F 3 85  ? 15.783  49.425  60.384  1.000 46.681  ? 85  GLN CCC CG  1 
ATOM   8745  C CD  . GLN F 3 85  ? 15.619  49.851  58.947  1.000 47.915  ? 85  GLN CCC CD  1 
ATOM   8746  O OE1 . GLN F 3 85  ? 16.442  50.586  58.425  1.000 54.388  ? 85  GLN CCC OE1 1 
ATOM   8747  N NE2 . GLN F 3 85  ? 14.623  49.317  58.270  1.000 48.972  ? 85  GLN CCC NE2 1 
ATOM   8748  N N   . ALA F 3 86  ? 19.632  47.391  59.191  1.000 47.731  ? 86  ALA CCC N   1 
ATOM   8749  C CA  . ALA F 3 86  ? 20.993  46.827  59.268  1.000 48.633  ? 86  ALA CCC CA  1 
ATOM   8750  C C   . ALA F 3 86  ? 21.475  46.840  60.719  1.000 47.022  ? 86  ALA CCC C   1 
ATOM   8751  O O   . ALA F 3 86  ? 22.363  46.013  61.026  1.000 44.514  ? 86  ALA CCC O   1 
ATOM   8752  C CB  . ALA F 3 86  ? 21.910  47.597  58.366  1.000 52.273  ? 86  ALA CCC CB  1 
ATOM   8753  N N   . GLU F 3 87  ? 20.939  47.739  61.552  1.000 46.610  ? 87  GLU CCC N   1 
ATOM   8754  C CA  . GLU F 3 87  ? 21.358  47.922  62.965  1.000 50.513  ? 87  GLU CCC CA  1 
ATOM   8755  C C   . GLU F 3 87  ? 20.619  46.937  63.866  1.000 53.157  ? 87  GLU CCC C   1 
ATOM   8756  O O   . GLU F 3 87  ? 20.769  47.037  65.087  1.000 58.770  ? 87  GLU CCC O   1 
ATOM   8757  C CB  . GLU F 3 87  ? 21.073  49.352  63.388  1.000 52.711  ? 87  GLU CCC CB  1 
ATOM   8758  C CG  . GLU F 3 87  ? 21.338  50.322  62.256  1.000 61.966  ? 87  GLU CCC CG  1 
ATOM   8759  C CD  . GLU F 3 87  ? 20.115  50.869  61.534  1.000 67.463  ? 87  GLU CCC CD  1 
ATOM   8760  O OE1 . GLU F 3 87  ? 19.028  50.897  62.163  1.000 75.632  ? 87  GLU CCC OE1 1 
ATOM   8761  O OE2 . GLU F 3 87  ? 20.242  51.273  60.346  1.000 65.324  ? 87  GLU CCC OE2 1 
ATOM   8762  N N   . ASP F 3 88  ? 19.802  46.058  63.288  1.000 51.153  ? 88  ASP CCC N   1 
ATOM   8763  C CA  . ASP F 3 88  ? 18.966  45.100  64.062  1.000 44.339  ? 88  ASP CCC CA  1 
ATOM   8764  C C   . ASP F 3 88  ? 19.662  43.750  64.073  1.000 40.561  ? 88  ASP CCC C   1 
ATOM   8765  O O   . ASP F 3 88  ? 19.261  42.907  64.875  1.000 38.867  ? 88  ASP CCC O   1 
ATOM   8766  C CB  . ASP F 3 88  ? 17.539  45.052  63.525  1.000 41.692  ? 88  ASP CCC CB  1 
ATOM   8767  C CG  . ASP F 3 88  ? 16.812  46.352  63.799  1.000 45.176  ? 88  ASP CCC CG  1 
ATOM   8768  O OD1 . ASP F 3 88  ? 17.204  47.046  64.781  1.000 48.728  ? 88  ASP CCC OD1 1 
ATOM   8769  O OD2 . ASP F 3 88  ? 15.905  46.701  63.018  1.000 44.907  ? 88  ASP CCC OD2 1 
ATOM   8770  N N   . VAL F 3 89  ? 20.702  43.583  63.267  1.000 37.938  ? 89  VAL CCC N   1 
ATOM   8771  C CA  . VAL F 3 89  ? 21.506  42.335  63.286  1.000 39.455  ? 89  VAL CCC CA  1 
ATOM   8772  C C   . VAL F 3 89  ? 22.055  42.177  64.693  1.000 38.727  ? 89  VAL CCC C   1 
ATOM   8773  O O   . VAL F 3 89  ? 22.959  42.937  65.048  1.000 37.586  ? 89  VAL CCC O   1 
ATOM   8774  C CB  . VAL F 3 89  ? 22.635  42.342  62.250  1.000 43.557  ? 89  VAL CCC CB  1 
ATOM   8775  C CG1 . VAL F 3 89  ? 23.557  41.148  62.447  1.000 43.032  ? 89  VAL CCC CG1 1 
ATOM   8776  C CG2 . VAL F 3 89  ? 22.070  42.368  60.837  1.000 48.320  ? 89  VAL CCC CG2 1 
ATOM   8777  N N   . ALA F 3 90  ? 21.513  41.227  65.450  1.000 39.494  ? 90  ALA CCC N   1 
ATOM   8778  C CA  . ALA F 3 90  ? 21.939  40.944  66.839  1.000 39.147  ? 90  ALA CCC CA  1 
ATOM   8779  C C   . ALA F 3 90  ? 21.355  39.617  67.296  1.000 35.534  ? 90  ALA CCC C   1 
ATOM   8780  O O   . ALA F 3 90  ? 20.635  38.984  66.526  1.000 37.292  ? 90  ALA CCC O   1 
ATOM   8781  C CB  . ALA F 3 90  ? 21.494  42.057  67.748  1.000 40.959  ? 90  ALA CCC CB  1 
ATOM   8782  N N   . VAL F 3 91  ? 21.668  39.228  68.520  1.000 34.118  ? 91  VAL CCC N   1 
ATOM   8783  C CA  . VAL F 3 91  ? 20.968  38.101  69.185  1.000 35.780  ? 91  VAL CCC CA  1 
ATOM   8784  C C   . VAL F 3 91  ? 19.877  38.683  70.079  1.000 35.612  ? 91  VAL CCC C   1 
ATOM   8785  O O   . VAL F 3 91  ? 20.120  39.725  70.704  1.000 38.734  ? 91  VAL CCC O   1 
ATOM   8786  C CB  . VAL F 3 91  ? 21.947  37.224  69.968  1.000 37.226  ? 91  VAL CCC CB  1 
ATOM   8787  C CG1 . VAL F 3 91  ? 21.214  36.122  70.700  1.000 40.467  ? 91  VAL CCC CG1 1 
ATOM   8788  C CG2 . VAL F 3 91  ? 23.008  36.653  69.046  1.000 38.255  ? 91  VAL CCC CG2 1 
ATOM   8789  N N   . TYR F 3 92  ? 18.708  38.051  70.086  1.000 34.402  ? 92  TYR CCC N   1 
ATOM   8790  C CA  . TYR F 3 92  ? 17.546  38.483  70.893  1.000 35.242  ? 92  TYR CCC CA  1 
ATOM   8791  C C   . TYR F 3 92  ? 17.189  37.358  71.858  1.000 39.556  ? 92  TYR CCC C   1 
ATOM   8792  O O   . TYR F 3 92  ? 16.992  36.205  71.397  1.000 40.046  ? 92  TYR CCC O   1 
ATOM   8793  C CB  . TYR F 3 92  ? 16.385  38.866  69.984  1.000 32.262  ? 92  TYR CCC CB  1 
ATOM   8794  C CG  . TYR F 3 92  ? 16.673  40.047  69.107  1.000 31.282  ? 92  TYR CCC CG  1 
ATOM   8795  C CD1 . TYR F 3 92  ? 17.286  39.895  67.877  1.000 31.083  ? 92  TYR CCC CD1 1 
ATOM   8796  C CD2 . TYR F 3 92  ? 16.311  41.318  69.505  1.000 32.272  ? 92  TYR CCC CD2 1 
ATOM   8797  C CE1 . TYR F 3 92  ? 17.526  40.983  67.058  1.000 31.699  ? 92  TYR CCC CE1 1 
ATOM   8798  C CE2 . TYR F 3 92  ? 16.541  42.421  68.697  1.000 32.896  ? 92  TYR CCC CE2 1 
ATOM   8799  C CZ  . TYR F 3 92  ? 17.153  42.251  67.473  1.000 32.894  ? 92  TYR CCC CZ  1 
ATOM   8800  O OH  . TYR F 3 92  ? 17.389  43.354  66.706  1.000 36.318  ? 92  TYR CCC OH  1 
ATOM   8801  N N   . TYR F 3 93  ? 17.162  37.687  73.152  1.000 41.430  ? 93  TYR CCC N   1 
ATOM   8802  C CA  . TYR F 3 93  ? 16.768  36.770  74.244  1.000 42.105  ? 93  TYR CCC CA  1 
ATOM   8803  C C   . TYR F 3 93  ? 15.440  37.250  74.834  1.000 45.834  ? 93  TYR CCC C   1 
ATOM   8804  O O   . TYR F 3 93  ? 15.284  38.472  75.044  1.000 44.388  ? 93  TYR CCC O   1 
ATOM   8805  C CB  . TYR F 3 93  ? 17.848  36.722  75.326  1.000 41.780  ? 93  TYR CCC CB  1 
ATOM   8806  C CG  . TYR F 3 93  ? 19.245  36.378  74.869  1.000 41.043  ? 93  TYR CCC CG  1 
ATOM   8807  C CD1 . TYR F 3 93  ? 19.741  35.081  74.913  1.000 40.460  ? 93  TYR CCC CD1 1 
ATOM   8808  C CD2 . TYR F 3 93  ? 20.092  37.372  74.423  1.000 42.362  ? 93  TYR CCC CD2 1 
ATOM   8809  C CE1 . TYR F 3 93  ? 21.034  34.781  74.515  1.000 41.064  ? 93  TYR CCC CE1 1 
ATOM   8810  C CE2 . TYR F 3 93  ? 21.388  37.093  74.018  1.000 40.813  ? 93  TYR CCC CE2 1 
ATOM   8811  C CZ  . TYR F 3 93  ? 21.867  35.800  74.071  1.000 40.461  ? 93  TYR CCC CZ  1 
ATOM   8812  O OH  . TYR F 3 93  ? 23.151  35.590  73.655  1.000 40.759  ? 93  TYR CCC OH  1 
ATOM   8813  N N   . CYS F 3 94  ? 14.515  36.317  75.090  1.000 52.190  ? 94  CYS CCC N   1 
ATOM   8814  C CA  . CYS F 3 94  ? 13.350  36.530  75.988  1.000 53.949  ? 94  CYS CCC CA  1 
ATOM   8815  C C   . CYS F 3 94  ? 13.784  36.154  77.402  1.000 51.106  ? 94  CYS CCC C   1 
ATOM   8816  O O   . CYS F 3 94  ? 14.654  35.277  77.552  1.000 46.464  ? 94  CYS CCC O   1 
ATOM   8817  C CB  . CYS F 3 94  ? 12.115  35.748  75.546  1.000 65.538  ? 94  CYS CCC CB  1 
ATOM   8818  S SG  . CYS F 3 94  ? 12.280  33.935  75.500  1.000 77.637  ? 94  CYS CCC SG  1 
ATOM   8819  N N   . GLN F 3 95  ? 13.248  36.845  78.398  1.000 49.032  ? 95  GLN CCC N   1 
ATOM   8820  C CA  . GLN F 3 95  ? 13.529  36.575  79.831  1.000 50.534  ? 95  GLN CCC CA  1 
ATOM   8821  C C   . GLN F 3 95  ? 12.202  36.718  80.567  1.000 49.833  ? 95  GLN CCC C   1 
ATOM   8822  O O   . GLN F 3 95  ? 11.493  37.713  80.284  1.000 48.190  ? 95  GLN CCC O   1 
ATOM   8823  C CB  . GLN F 3 95  ? 14.560  37.564  80.381  1.000 51.595  ? 95  GLN CCC CB  1 
ATOM   8824  C CG  . GLN F 3 95  ? 14.877  37.404  81.866  1.000 52.193  ? 95  GLN CCC CG  1 
ATOM   8825  C CD  . GLN F 3 95  ? 14.878  38.722  82.609  1.000 57.059  ? 95  GLN CCC CD  1 
ATOM   8826  O OE1 . GLN F 3 95  ? 14.579  39.779  82.054  1.000 62.313  ? 95  GLN CCC OE1 1 
ATOM   8827  N NE2 . GLN F 3 95  ? 15.187  38.671  83.897  1.000 64.113  ? 95  GLN CCC NE2 1 
ATOM   8828  N N   . GLN F 3 96  ? 11.888  35.757  81.442  1.000 47.421  ? 96  GLN CCC N   1 
ATOM   8829  C CA  . GLN F 3 96  ? 10.772  35.848  82.418  1.000 47.028  ? 96  GLN CCC CA  1 
ATOM   8830  C C   . GLN F 3 96  ? 11.326  36.460  83.713  1.000 48.826  ? 96  GLN CCC C   1 
ATOM   8831  O O   . GLN F 3 96  ? 12.438  36.071  84.146  1.000 50.778  ? 96  GLN CCC O   1 
ATOM   8832  C CB  . GLN F 3 96  ? 10.126  34.478  82.651  1.000 44.662  ? 96  GLN CCC CB  1 
ATOM   8833  C CG  . GLN F 3 96  ? 11.002  33.480  83.409  1.000 42.380  ? 96  GLN CCC CG  1 
ATOM   8834  C CD  . GLN F 3 96  ? 10.904  33.594  84.912  1.000 40.684  ? 96  GLN CCC CD  1 
ATOM   8835  O OE1 . GLN F 3 96  ? 10.117  34.376  85.460  1.000 37.848  ? 96  GLN CCC OE1 1 
ATOM   8836  N NE2 . GLN F 3 96  ? 11.719  32.801  85.593  1.000 36.946  ? 96  GLN CCC NE2 1 
ATOM   8837  N N   . TYR F 3 97  ? 10.587  37.400  84.292  1.000 46.530  ? 97  TYR CCC N   1 
ATOM   8838  C CA  . TYR F 3 97  ? 10.860  37.975  85.626  1.000 45.867  ? 97  TYR CCC CA  1 
ATOM   8839  C C   . TYR F 3 97  ? 9.603   37.833  86.488  1.000 53.098  ? 97  TYR CCC C   1 
ATOM   8840  O O   . TYR F 3 97  ? 9.314   38.746  87.283  1.000 59.034  ? 97  TYR CCC O   1 
ATOM   8841  C CB  . TYR F 3 97  ? 11.341  39.416  85.473  1.000 44.602  ? 97  TYR CCC CB  1 
ATOM   8842  C CG  . TYR F 3 97  ? 10.454  40.367  84.705  1.000 42.194  ? 97  TYR CCC CG  1 
ATOM   8843  C CD1 . TYR F 3 97  ? 10.444  40.397  83.319  1.000 40.641  ? 97  TYR CCC CD1 1 
ATOM   8844  C CD2 . TYR F 3 97  ? 9.696   41.316  85.372  1.000 43.119  ? 97  TYR CCC CD2 1 
ATOM   8845  C CE1 . TYR F 3 97  ? 9.665   41.313  82.618  1.000 40.163  ? 97  TYR CCC CE1 1 
ATOM   8846  C CE2 . TYR F 3 97  ? 8.932   42.254  84.690  1.000 42.675  ? 97  TYR CCC CE2 1 
ATOM   8847  C CZ  . TYR F 3 97  ? 8.897   42.241  83.307  1.000 40.756  ? 97  TYR CCC CZ  1 
ATOM   8848  O OH  . TYR F 3 97  ? 8.131   43.173  82.668  1.000 36.540  ? 97  TYR CCC OH  1 
ATOM   8849  N N   . TYR F 3 98  ? 8.875   36.724  86.320  1.000 59.663  ? 98  TYR CCC N   1 
ATOM   8850  C CA  . TYR F 3 98  ? 7.652   36.396  87.098  1.000 65.991  ? 98  TYR CCC CA  1 
ATOM   8851  C C   . TYR F 3 98  ? 8.092   35.984  88.510  1.000 61.773  ? 98  TYR CCC C   1 
ATOM   8852  O O   . TYR F 3 98  ? 7.564   36.535  89.498  1.000 61.316  ? 98  TYR CCC O   1 
ATOM   8853  C CB  . TYR F 3 98  ? 6.805   35.314  86.407  1.000 72.334  ? 98  TYR CCC CB  1 
ATOM   8854  C CG  . TYR F 3 98  ? 5.624   34.851  87.228  1.000 73.192  ? 98  TYR CCC CG  1 
ATOM   8855  C CD1 . TYR F 3 98  ? 4.505   35.664  87.381  1.000 73.848  ? 98  TYR CCC CD1 1 
ATOM   8856  C CD2 . TYR F 3 98  ? 5.639   33.633  87.896  1.000 68.344  ? 98  TYR CCC CD2 1 
ATOM   8857  C CE1 . TYR F 3 98  ? 3.425   35.276  88.162  1.000 72.307  ? 98  TYR CCC CE1 1 
ATOM   8858  C CE2 . TYR F 3 98  ? 4.569   33.228  88.679  1.000 70.338  ? 98  TYR CCC CE2 1 
ATOM   8859  C CZ  . TYR F 3 98  ? 3.463   34.056  88.820  1.000 73.247  ? 98  TYR CCC CZ  1 
ATOM   8860  O OH  . TYR F 3 98  ? 2.408   33.663  89.587  1.000 67.144  ? 98  TYR CCC OH  1 
ATOM   8861  N N   . SER F 3 99  ? 9.047   35.060  88.592  1.000 56.514  ? 99  SER CCC N   1 
ATOM   8862  C CA  . SER F 3 99  ? 9.582   34.503  89.859  1.000 58.564  ? 99  SER CCC CA  1 
ATOM   8863  C C   . SER F 3 99  ? 11.085  34.213  89.727  1.000 62.312  ? 99  SER CCC C   1 
ATOM   8864  O O   . SER F 3 99  ? 11.504  33.738  88.643  1.000 61.942  ? 99  SER CCC O   1 
ATOM   8865  C CB  . SER F 3 99  ? 8.830   33.251  90.221  1.000 59.124  ? 99  SER CCC CB  1 
ATOM   8866  O OG  . SER F 3 99  ? 9.053   32.232  89.253  1.000 54.840  ? 99  SER CCC OG  1 
ATOM   8867  N N   . THR F 3 100 ? 11.855  34.450  90.796  1.000 56.379  ? 100 THR CCC N   1 
ATOM   8868  C CA  . THR F 3 100 ? 13.259  33.985  90.919  1.000 52.434  ? 100 THR CCC CA  1 
ATOM   8869  C C   . THR F 3 100 ? 13.205  32.470  91.027  1.000 52.305  ? 100 THR CCC C   1 
ATOM   8870  O O   . THR F 3 100 ? 12.341  31.965  91.726  1.000 50.399  ? 100 THR CCC O   1 
ATOM   8871  C CB  . THR F 3 100 ? 14.000  34.604  92.115  1.000 52.625  ? 100 THR CCC CB  1 
ATOM   8872  O OG1 . THR F 3 100 ? 13.684  33.887  93.311  1.000 47.217  ? 100 THR CCC OG1 1 
ATOM   8873  C CG2 . THR F 3 100 ? 13.730  36.087  92.275  1.000 52.200  ? 100 THR CCC CG2 1 
ATOM   8874  N N   . PRO F 3 101 ? 14.076  31.695  90.340  1.000 57.977  ? 101 PRO CCC N   1 
ATOM   8875  C CA  . PRO F 3 101 ? 15.152  32.235  89.509  1.000 58.123  ? 101 PRO CCC CA  1 
ATOM   8876  C C   . PRO F 3 101 ? 14.692  32.722  88.128  1.000 55.920  ? 101 PRO CCC C   1 
ATOM   8877  O O   . PRO F 3 101 ? 14.086  31.941  87.420  1.000 59.997  ? 101 PRO CCC O   1 
ATOM   8878  C CB  . PRO F 3 101 ? 16.085  31.025  89.334  1.000 58.816  ? 101 PRO CCC CB  1 
ATOM   8879  C CG  . PRO F 3 101 ? 15.149  29.854  89.334  1.000 56.504  ? 101 PRO CCC CG  1 
ATOM   8880  C CD  . PRO F 3 101 ? 14.071  30.223  90.337  1.000 59.645  ? 101 PRO CCC CD  1 
ATOM   8881  N N   . TYR F 3 102 ? 15.021  33.970  87.768  1.000 51.892  ? 102 TYR CCC N   1 
ATOM   8882  C CA  . TYR F 3 102 ? 14.780  34.523  86.414  1.000 47.138  ? 102 TYR CCC CA  1 
ATOM   8883  C C   . TYR F 3 102 ? 15.467  33.587  85.420  1.000 45.363  ? 102 TYR CCC C   1 
ATOM   8884  O O   . TYR F 3 102 ? 16.450  32.906  85.801  1.000 36.048  ? 102 TYR CCC O   1 
ATOM   8885  C CB  . TYR F 3 102 ? 15.351  35.926  86.243  1.000 48.669  ? 102 TYR CCC CB  1 
ATOM   8886  C CG  . TYR F 3 102 ? 14.846  37.028  87.141  1.000 51.849  ? 102 TYR CCC CG  1 
ATOM   8887  C CD1 . TYR F 3 102 ? 15.454  38.270  87.088  1.000 60.654  ? 102 TYR CCC CD1 1 
ATOM   8888  C CD2 . TYR F 3 102 ? 13.790  36.877  88.023  1.000 54.643  ? 102 TYR CCC CD2 1 
ATOM   8889  C CE1 . TYR F 3 102 ? 15.025  39.334  87.864  1.000 68.667  ? 102 TYR CCC CE1 1 
ATOM   8890  C CE2 . TYR F 3 102 ? 13.362  37.923  88.832  1.000 58.941  ? 102 TYR CCC CE2 1 
ATOM   8891  C CZ  . TYR F 3 102 ? 13.982  39.163  88.754  1.000 63.703  ? 102 TYR CCC CZ  1 
ATOM   8892  O OH  . TYR F 3 102 ? 13.612  40.241  89.512  1.000 65.393  ? 102 TYR CCC OH  1 
ATOM   8893  N N   . THR F 3 103 ? 14.965  33.522  84.190  1.000 51.877  ? 103 THR CCC N   1 
ATOM   8894  C CA  . THR F 3 103 ? 15.530  32.615  83.150  1.000 57.530  ? 103 THR CCC CA  1 
ATOM   8895  C C   . THR F 3 103 ? 15.392  33.252  81.763  1.000 54.325  ? 103 THR CCC C   1 
ATOM   8896  O O   . THR F 3 103 ? 14.395  33.961  81.514  1.000 49.457  ? 103 THR CCC O   1 
ATOM   8897  C CB  . THR F 3 103 ? 14.887  31.221  83.215  1.000 61.140  ? 103 THR CCC CB  1 
ATOM   8898  O OG1 . THR F 3 103 ? 13.467  31.372  83.340  1.000 63.862  ? 103 THR CCC OG1 1 
ATOM   8899  C CG2 . THR F 3 103 ? 15.430  30.391  84.361  1.000 62.213  ? 103 THR CCC CG2 1 
ATOM   8900  N N   . PHE F 3 104 ? 16.396  33.016  80.921  1.000 52.245  ? 104 PHE CCC N   1 
ATOM   8901  C CA  . PHE F 3 104 ? 16.506  33.563  79.549  1.000 51.168  ? 104 PHE CCC CA  1 
ATOM   8902  C C   . PHE F 3 104 ? 16.203  32.431  78.579  1.000 46.778  ? 104 PHE CCC C   1 
ATOM   8903  O O   . PHE F 3 104 ? 16.435  31.271  78.952  1.000 43.976  ? 104 PHE CCC O   1 
ATOM   8904  C CB  . PHE F 3 104 ? 17.921  34.085  79.260  1.000 53.993  ? 104 PHE CCC CB  1 
ATOM   8905  C CG  . PHE F 3 104 ? 18.346  35.325  80.013  1.000 52.317  ? 104 PHE CCC CG  1 
ATOM   8906  C CD1 . PHE F 3 104 ? 19.229  35.236  81.079  1.000 49.593  ? 104 PHE CCC CD1 1 
ATOM   8907  C CD2 . PHE F 3 104 ? 17.880  36.581  79.642  1.000 48.053  ? 104 PHE CCC CD2 1 
ATOM   8908  C CE1 . PHE F 3 104 ? 19.605  36.374  81.774  1.000 48.240  ? 104 PHE CCC CE1 1 
ATOM   8909  C CE2 . PHE F 3 104 ? 18.255  37.718  80.342  1.000 46.863  ? 104 PHE CCC CE2 1 
ATOM   8910  C CZ  . PHE F 3 104 ? 19.115  37.612  81.408  1.000 47.170  ? 104 PHE CCC CZ  1 
ATOM   8911  N N   . GLY F 3 105 ? 15.760  32.777  77.373  1.000 45.018  ? 105 GLY CCC N   1 
ATOM   8912  C CA  . GLY F 3 105 ? 15.768  31.869  76.214  1.000 45.775  ? 105 GLY CCC CA  1 
ATOM   8913  C C   . GLY F 3 105 ? 17.184  31.532  75.788  1.000 43.069  ? 105 GLY CCC C   1 
ATOM   8914  O O   . GLY F 3 105 ? 18.119  32.176  76.281  1.000 42.320  ? 105 GLY CCC O   1 
ATOM   8915  N N   . GLN F 3 106 ? 17.336  30.543  74.910  1.000 46.065  ? 106 GLN CCC N   1 
ATOM   8916  C CA  . GLN F 3 106 ? 18.651  30.111  74.378  1.000 52.372  ? 106 GLN CCC CA  1 
ATOM   8917  C C   . GLN F 3 106 ? 19.198  31.213  73.451  1.000 50.953  ? 106 GLN CCC C   1 
ATOM   8918  O O   . GLN F 3 106 ? 20.422  31.258  73.229  1.000 48.985  ? 106 GLN CCC O   1 
ATOM   8919  C CB  . GLN F 3 106 ? 18.537  28.727  73.726  1.000 58.332  ? 106 GLN CCC CB  1 
ATOM   8920  C CG  . GLN F 3 106 ? 17.939  28.711  72.323  1.000 61.822  ? 106 GLN CCC CG  1 
ATOM   8921  C CD  . GLN F 3 106 ? 16.431  28.657  72.317  1.000 66.673  ? 106 GLN CCC CD  1 
ATOM   8922  O OE1 . GLN F 3 106 ? 15.774  28.509  73.350  1.000 73.480  ? 106 GLN CCC OE1 1 
ATOM   8923  N NE2 . GLN F 3 106 ? 15.859  28.744  71.125  1.000 65.942  ? 106 GLN CCC NE2 1 
ATOM   8924  N N   . GLY F 3 107 ? 18.323  32.081  72.942  1.000 50.585  ? 107 GLY CCC N   1 
ATOM   8925  C CA  . GLY F 3 107 ? 18.693  33.215  72.080  1.000 49.749  ? 107 GLY CCC CA  1 
ATOM   8926  C C   . GLY F 3 107 ? 18.337  32.952  70.626  1.000 50.361  ? 107 GLY CCC C   1 
ATOM   8927  O O   . GLY F 3 107 ? 18.336  31.773  70.202  1.000 56.955  ? 107 GLY CCC O   1 
ATOM   8928  N N   . THR F 3 108 ? 18.085  34.014  69.864  1.000 47.880  ? 108 THR CCC N   1 
ATOM   8929  C CA  . THR F 3 108 ? 17.768  33.937  68.418  1.000 46.401  ? 108 THR CCC CA  1 
ATOM   8930  C C   . THR F 3 108 ? 18.705  34.865  67.639  1.000 43.358  ? 108 THR CCC C   1 
ATOM   8931  O O   . THR F 3 108 ? 18.557  36.077  67.763  1.000 42.319  ? 108 THR CCC O   1 
ATOM   8932  C CB  . THR F 3 108 ? 16.287  34.256  68.211  1.000 48.638  ? 108 THR CCC CB  1 
ATOM   8933  O OG1 . THR F 3 108 ? 15.578  33.201  68.861  1.000 49.817  ? 108 THR CCC OG1 1 
ATOM   8934  C CG2 . THR F 3 108 ? 15.903  34.367  66.754  1.000 49.689  ? 108 THR CCC CG2 1 
ATOM   8935  N N   . LYS F 3 109 ? 19.629  34.278  66.882  1.000 44.659  ? 109 LYS CCC N   1 
ATOM   8936  C CA  . LYS F 3 109 ? 20.575  34.951  65.950  1.000 47.810  ? 109 LYS CCC CA  1 
ATOM   8937  C C   . LYS F 3 109 ? 19.757  35.547  64.795  1.000 43.050  ? 109 LYS CCC C   1 
ATOM   8938  O O   . LYS F 3 109 ? 19.044  34.779  64.137  1.000 49.649  ? 109 LYS CCC O   1 
ATOM   8939  C CB  . LYS F 3 109 ? 21.624  33.911  65.515  1.000 58.698  ? 109 LYS CCC CB  1 
ATOM   8940  C CG  . LYS F 3 109 ? 22.432  34.201  64.248  1.000 71.204  ? 109 LYS CCC CG  1 
ATOM   8941  C CD  . LYS F 3 109 ? 23.485  35.270  64.454  1.000 81.606  ? 109 LYS CCC CD  1 
ATOM   8942  C CE  . LYS F 3 109 ? 23.710  36.197  63.271  1.000 85.967  ? 109 LYS CCC CE  1 
ATOM   8943  N NZ  . LYS F 3 109 ? 23.927  37.595  63.727  1.000 84.532  ? 109 LYS CCC NZ  1 
ATOM   8944  N N   . VAL F 3 110 ? 19.868  36.852  64.543  1.000 38.764  ? 110 VAL CCC N   1 
ATOM   8945  C CA  . VAL F 3 110 ? 19.151  37.541  63.422  1.000 36.724  ? 110 VAL CCC CA  1 
ATOM   8946  C C   . VAL F 3 110 ? 20.172  38.127  62.434  1.000 35.893  ? 110 VAL CCC C   1 
ATOM   8947  O O   . VAL F 3 110 ? 20.950  38.971  62.854  1.000 33.964  ? 110 VAL CCC O   1 
ATOM   8948  C CB  . VAL F 3 110 ? 18.191  38.623  63.950  1.000 34.668  ? 110 VAL CCC CB  1 
ATOM   8949  C CG1 . VAL F 3 110 ? 17.596  39.475  62.840  1.000 33.648  ? 110 VAL CCC CG1 1 
ATOM   8950  C CG2 . VAL F 3 110 ? 17.081  38.015  64.781  1.000 35.184  ? 110 VAL CCC CG2 1 
ATOM   8951  N N   . GLU F 3 111 ? 20.152  37.678  61.176  1.000 38.212  ? 111 GLU CCC N   1 
ATOM   8952  C CA  . GLU F 3 111 ? 21.023  38.130  60.057  1.000 40.806  ? 111 GLU CCC CA  1 
ATOM   8953  C C   . GLU F 3 111 ? 20.163  38.938  59.091  1.000 39.060  ? 111 GLU CCC C   1 
ATOM   8954  O O   . GLU F 3 111 ? 18.948  38.746  59.081  1.000 39.019  ? 111 GLU CCC O   1 
ATOM   8955  C CB  . GLU F 3 111 ? 21.615  36.981  59.222  1.000 48.609  ? 111 GLU CCC CB  1 
ATOM   8956  C CG  . GLU F 3 111 ? 21.589  35.588  59.860  1.000 59.142  ? 111 GLU CCC CG  1 
ATOM   8957  C CD  . GLU F 3 111 ? 22.304  34.477  59.088  1.000 65.687  ? 111 GLU CCC CD  1 
ATOM   8958  O OE1 . GLU F 3 111 ? 22.681  34.681  57.904  1.000 55.050  ? 111 GLU CCC OE1 1 
ATOM   8959  O OE2 . GLU F 3 111 ? 22.468  33.383  59.679  1.000 77.275  ? 111 GLU CCC OE2 1 
ATOM   8960  N N   . ILE F 3 112 ? 20.795  39.763  58.264  1.000 41.097  ? 112 ILE CCC N   1 
ATOM   8961  C CA  . ILE F 3 112 ? 20.205  40.316  57.009  1.000 42.005  ? 112 ILE CCC CA  1 
ATOM   8962  C C   . ILE F 3 112 ? 20.271  39.226  55.942  1.000 44.672  ? 112 ILE CCC C   1 
ATOM   8963  O O   . ILE F 3 112 ? 21.377  38.698  55.729  1.000 46.734  ? 112 ILE CCC O   1 
ATOM   8964  C CB  . ILE F 3 112 ? 20.987  41.558  56.542  1.000 43.641  ? 112 ILE CCC CB  1 
ATOM   8965  C CG1 . ILE F 3 112 ? 20.959  42.677  57.582  1.000 45.461  ? 112 ILE CCC CG1 1 
ATOM   8966  C CG2 . ILE F 3 112 ? 20.513  42.025  55.181  1.000 44.805  ? 112 ILE CCC CG2 1 
ATOM   8967  C CD1 . ILE F 3 112 ? 19.577  43.070  58.004  1.000 47.254  ? 112 ILE CCC CD1 1 
ATOM   8968  N N   . LYS F 3 113 ? 19.158  38.936  55.268  1.000 45.669  ? 113 LYS CCC N   1 
ATOM   8969  C CA  . LYS F 3 113 ? 19.164  38.112  54.034  1.000 48.530  ? 113 LYS CCC CA  1 
ATOM   8970  C C   . LYS F 3 113 ? 19.328  39.029  52.823  1.000 46.602  ? 113 LYS CCC C   1 
ATOM   8971  O O   . LYS F 3 113 ? 18.563  39.984  52.697  1.000 49.539  ? 113 LYS CCC O   1 
ATOM   8972  C CB  . LYS F 3 113 ? 17.887  37.287  53.863  1.000 55.548  ? 113 LYS CCC CB  1 
ATOM   8973  C CG  . LYS F 3 113 ? 17.957  36.300  52.707  1.000 63.777  ? 113 LYS CCC CG  1 
ATOM   8974  C CD  . LYS F 3 113 ? 16.774  35.377  52.600  1.000 65.474  ? 113 LYS CCC CD  1 
ATOM   8975  C CE  . LYS F 3 113 ? 15.779  35.856  51.573  1.000 69.472  ? 113 LYS CCC CE  1 
ATOM   8976  N NZ  . LYS F 3 113 ? 14.628  34.932  51.498  1.000 76.946  ? 113 LYS CCC NZ  1 
ATOM   8977  N N   . ARG F 3 114 ? 20.290  38.729  51.963  1.000 44.002  ? 114 ARG CCC N   1 
ATOM   8978  C CA  . ARG F 3 114 ? 20.509  39.424  50.668  1.000 45.756  ? 114 ARG CCC CA  1 
ATOM   8979  C C   . ARG F 3 114 ? 20.667  38.358  49.588  1.000 45.943  ? 114 ARG CCC C   1 
ATOM   8980  O O   . ARG F 3 114 ? 20.565  37.159  49.922  1.000 43.898  ? 114 ARG CCC O   1 
ATOM   8981  C CB  . ARG F 3 114 ? 21.756  40.307  50.726  1.000 47.188  ? 114 ARG CCC CB  1 
ATOM   8982  C CG  . ARG F 3 114 ? 22.967  39.589  51.310  1.000 48.868  ? 114 ARG CCC CG  1 
ATOM   8983  C CD  . ARG F 3 114 ? 24.298  40.091  50.796  1.000 47.281  ? 114 ARG CCC CD  1 
ATOM   8984  N NE  . ARG F 3 114 ? 24.364  39.860  49.368  1.000 48.857  ? 114 ARG CCC NE  1 
ATOM   8985  C CZ  . ARG F 3 114 ? 25.184  40.477  48.527  1.000 47.955  ? 114 ARG CCC CZ  1 
ATOM   8986  N NH1 . ARG F 3 114 ? 26.068  41.362  48.950  1.000 45.667  ? 114 ARG CCC NH1 1 
ATOM   8987  N NH2 . ARG F 3 114 ? 25.132  40.179  47.245  1.000 53.545  ? 114 ARG CCC NH2 1 
ATOM   8988  N N   . THR F 3 115 ? 20.901  38.781  48.344  1.000 48.049  ? 115 THR CCC N   1 
ATOM   8989  C CA  . THR F 3 115 ? 21.147  37.866  47.202  1.000 46.928  ? 115 THR CCC CA  1 
ATOM   8990  C C   . THR F 3 115 ? 22.420  37.076  47.484  1.000 41.478  ? 115 THR CCC C   1 
ATOM   8991  O O   . THR F 3 115 ? 23.335  37.622  48.127  1.000 34.376  ? 115 THR CCC O   1 
ATOM   8992  C CB  . THR F 3 115 ? 21.267  38.598  45.858  1.000 50.177  ? 115 THR CCC CB  1 
ATOM   8993  O OG1 . THR F 3 115 ? 22.101  39.737  46.061  1.000 49.146  ? 115 THR CCC OG1 1 
ATOM   8994  C CG2 . THR F 3 115 ? 19.929  39.019  45.289  1.000 52.154  ? 115 THR CCC CG2 1 
ATOM   8995  N N   . VAL F 3 116 ? 22.454  35.843  46.990  1.000 41.705  ? 116 VAL CCC N   1 
ATOM   8996  C CA  . VAL F 3 116 ? 23.650  34.965  47.046  1.000 41.201  ? 116 VAL CCC CA  1 
ATOM   8997  C C   . VAL F 3 116 ? 24.826  35.736  46.455  1.000 37.814  ? 116 VAL CCC C   1 
ATOM   8998  O O   . VAL F 3 116 ? 24.625  36.447  45.464  1.000 33.177  ? 116 VAL CCC O   1 
ATOM   8999  C CB  . VAL F 3 116 ? 23.429  33.643  46.303  1.000 45.035  ? 116 VAL CCC CB  1 
ATOM   9000  C CG1 . VAL F 3 116 ? 24.627  32.732  46.485  1.000 46.657  ? 116 VAL CCC CG1 1 
ATOM   9001  C CG2 . VAL F 3 116 ? 22.147  32.947  46.745  1.000 49.699  ? 116 VAL CCC CG2 1 
ATOM   9002  N N   . ALA F 3 117 ? 25.985  35.636  47.104  1.000 38.447  ? 117 ALA CCC N   1 
ATOM   9003  C CA  . ALA F 3 117 ? 27.277  36.175  46.633  1.000 38.889  ? 117 ALA CCC CA  1 
ATOM   9004  C C   . ALA F 3 117 ? 28.356  35.121  46.882  1.000 37.131  ? 117 ALA CCC C   1 
ATOM   9005  O O   . ALA F 3 117 ? 28.473  34.655  48.026  1.000 35.989  ? 117 ALA CCC O   1 
ATOM   9006  C CB  . ALA F 3 117 ? 27.573  37.463  47.338  1.000 38.781  ? 117 ALA CCC CB  1 
ATOM   9007  N N   . ALA F 3 118 ? 29.066  34.717  45.829  1.000 39.049  ? 118 ALA CCC N   1 
ATOM   9008  C CA  . ALA F 3 118 ? 30.062  33.624  45.875  1.000 41.309  ? 118 ALA CCC CA  1 
ATOM   9009  C C   . ALA F 3 118 ? 31.298  34.154  46.573  1.000 39.753  ? 118 ALA CCC C   1 
ATOM   9010  O O   . ALA F 3 118 ? 31.581  35.335  46.462  1.000 43.206  ? 118 ALA CCC O   1 
ATOM   9011  C CB  . ALA F 3 118 ? 30.396  33.134  44.494  1.000 42.709  ? 118 ALA CCC CB  1 
ATOM   9012  N N   . PRO F 3 119 ? 32.042  33.316  47.319  1.000 39.084  ? 119 PRO CCC N   1 
ATOM   9013  C CA  . PRO F 3 119 ? 33.276  33.762  47.950  1.000 40.142  ? 119 PRO CCC CA  1 
ATOM   9014  C C   . PRO F 3 119 ? 34.421  33.859  46.936  1.000 42.160  ? 119 PRO CCC C   1 
ATOM   9015  O O   . PRO F 3 119 ? 34.515  33.004  46.077  1.000 43.917  ? 119 PRO CCC O   1 
ATOM   9016  C CB  . PRO F 3 119 ? 33.541  32.683  49.009  1.000 40.510  ? 119 PRO CCC CB  1 
ATOM   9017  C CG  . PRO F 3 119 ? 32.898  31.430  48.446  1.000 41.082  ? 119 PRO CCC CG  1 
ATOM   9018  C CD  . PRO F 3 119 ? 31.707  31.918  47.639  1.000 40.654  ? 119 PRO CCC CD  1 
ATOM   9019  N N   . SER F 3 120 ? 35.221  34.926  47.044  1.000 44.897  ? 120 SER CCC N   1 
ATOM   9020  C CA  . SER F 3 120 ? 36.592  35.027  46.484  1.000 45.791  ? 120 SER CCC CA  1 
ATOM   9021  C C   . SER F 3 120 ? 37.494  34.162  47.359  1.000 46.030  ? 120 SER CCC C   1 
ATOM   9022  O O   . SER F 3 120 ? 37.525  34.419  48.584  1.000 47.293  ? 120 SER CCC O   1 
ATOM   9023  C CB  . SER F 3 120 ? 37.105  36.451  46.442  1.000 49.846  ? 120 SER CCC CB  1 
ATOM   9024  O OG  . SER F 3 120 ? 36.477  37.214  45.423  1.000 56.015  ? 120 SER CCC OG  1 
ATOM   9025  N N   . VAL F 3 121 ? 38.173  33.168  46.772  1.000 46.167  ? 121 VAL CCC N   1 
ATOM   9026  C CA  . VAL F 3 121 ? 39.018  32.199  47.532  1.000 43.224  ? 121 VAL CCC CA  1 
ATOM   9027  C C   . VAL F 3 121 ? 40.498  32.530  47.331  1.000 39.340  ? 121 VAL CCC C   1 
ATOM   9028  O O   . VAL F 3 121 ? 40.914  32.822  46.205  1.000 45.038  ? 121 VAL CCC O   1 
ATOM   9029  C CB  . VAL F 3 121 ? 38.692  30.749  47.142  1.000 45.373  ? 121 VAL CCC CB  1 
ATOM   9030  C CG1 . VAL F 3 121 ? 39.378  29.761  48.070  1.000 45.928  ? 121 VAL CCC CG1 1 
ATOM   9031  C CG2 . VAL F 3 121 ? 37.186  30.515  47.128  1.000 44.814  ? 121 VAL CCC CG2 1 
ATOM   9032  N N   . PHE F 3 122 ? 41.256  32.513  48.419  1.000 35.509  ? 122 PHE CCC N   1 
ATOM   9033  C CA  . PHE F 3 122 ? 42.721  32.725  48.435  1.000 34.810  ? 122 PHE CCC CA  1 
ATOM   9034  C C   . PHE F 3 122 ? 43.324  31.712  49.403  1.000 35.168  ? 122 PHE CCC C   1 
ATOM   9035  O O   . PHE F 3 122 ? 42.719  31.463  50.464  1.000 31.618  ? 122 PHE CCC O   1 
ATOM   9036  C CB  . PHE F 3 122 ? 43.069  34.140  48.892  1.000 34.481  ? 122 PHE CCC CB  1 
ATOM   9037  C CG  . PHE F 3 122 ? 42.403  35.246  48.117  1.000 34.626  ? 122 PHE CCC CG  1 
ATOM   9038  C CD1 . PHE F 3 122 ? 41.178  35.757  48.512  1.000 35.372  ? 122 PHE CCC CD1 1 
ATOM   9039  C CD2 . PHE F 3 122 ? 43.000  35.777  46.987  1.000 35.714  ? 122 PHE CCC CD2 1 
ATOM   9040  C CE1 . PHE F 3 122 ? 40.576  36.789  47.806  1.000 34.995  ? 122 PHE CCC CE1 1 
ATOM   9041  C CE2 . PHE F 3 122 ? 42.401  36.810  46.282  1.000 34.330  ? 122 PHE CCC CE2 1 
ATOM   9042  C CZ  . PHE F 3 122 ? 41.183  37.306  46.684  1.000 33.872  ? 122 PHE CCC CZ  1 
ATOM   9043  N N   . ILE F 3 123 ? 44.498  31.183  49.069  1.000 36.652  ? 123 ILE CCC N   1 
ATOM   9044  C CA  . ILE F 3 123 ? 45.223  30.205  49.930  1.000 33.954  ? 123 ILE CCC CA  1 
ATOM   9045  C C   . ILE F 3 123 ? 46.627  30.736  50.205  1.000 32.353  ? 123 ILE CCC C   1 
ATOM   9046  O O   . ILE F 3 123 ? 47.265  31.177  49.278  1.000 31.310  ? 123 ILE CCC O   1 
ATOM   9047  C CB  . ILE F 3 123 ? 45.257  28.826  49.262  1.000 33.073  ? 123 ILE CCC CB  1 
ATOM   9048  C CG1 . ILE F 3 123 ? 45.858  27.771  50.192  1.000 35.298  ? 123 ILE CCC CG1 1 
ATOM   9049  C CG2 . ILE F 3 123 ? 45.997  28.878  47.943  1.000 32.158  ? 123 ILE CCC CG2 1 
ATOM   9050  C CD1 . ILE F 3 123 ? 45.849  26.381  49.612  1.000 37.347  ? 123 ILE CCC CD1 1 
ATOM   9051  N N   . PHE F 3 124 ? 47.075  30.684  51.450  1.000 33.292  ? 124 PHE CCC N   1 
ATOM   9052  C CA  . PHE F 3 124 ? 48.391  31.206  51.875  1.000 32.364  ? 124 PHE CCC CA  1 
ATOM   9053  C C   . PHE F 3 124 ? 49.220  30.042  52.366  1.000 31.022  ? 124 PHE CCC C   1 
ATOM   9054  O O   . PHE F 3 124 ? 48.816  29.336  53.281  1.000 32.757  ? 124 PHE CCC O   1 
ATOM   9055  C CB  . PHE F 3 124 ? 48.222  32.281  52.952  1.000 33.564  ? 124 PHE CCC CB  1 
ATOM   9056  C CG  . PHE F 3 124 ? 47.334  33.406  52.503  1.000 35.099  ? 124 PHE CCC CG  1 
ATOM   9057  C CD1 . PHE F 3 124 ? 47.744  34.283  51.513  1.000 36.846  ? 124 PHE CCC CD1 1 
ATOM   9058  C CD2 . PHE F 3 124 ? 46.068  33.552  53.028  1.000 36.152  ? 124 PHE CCC CD2 1 
ATOM   9059  C CE1 . PHE F 3 124 ? 46.896  35.271  51.051  1.000 37.506  ? 124 PHE CCC CE1 1 
ATOM   9060  C CE2 . PHE F 3 124 ? 45.239  34.574  52.605  1.000 36.799  ? 124 PHE CCC CE2 1 
ATOM   9061  C CZ  . PHE F 3 124 ? 45.657  35.432  51.622  1.000 37.863  ? 124 PHE CCC CZ  1 
ATOM   9062  N N   . PRO F 3 125 ? 50.412  29.834  51.796  1.000 31.644  ? 125 PRO CCC N   1 
ATOM   9063  C CA  . PRO F 3 125 ? 51.347  28.856  52.337  1.000 34.826  ? 125 PRO CCC CA  1 
ATOM   9064  C C   . PRO F 3 125 ? 51.922  29.369  53.645  1.000 35.007  ? 125 PRO CCC C   1 
ATOM   9065  O O   . PRO F 3 125 ? 51.761  30.526  53.978  1.000 35.064  ? 125 PRO CCC O   1 
ATOM   9066  C CB  . PRO F 3 125 ? 52.428  28.772  51.265  1.000 34.804  ? 125 PRO CCC CB  1 
ATOM   9067  C CG  . PRO F 3 125 ? 52.425  30.166  50.677  1.000 35.614  ? 125 PRO CCC CG  1 
ATOM   9068  C CD  . PRO F 3 125 ? 50.960  30.561  50.652  1.000 34.158  ? 125 PRO CCC CD  1 
ATOM   9069  N N   . PRO F 3 126 ? 52.558  28.514  54.460  1.000 38.441  ? 126 PRO CCC N   1 
ATOM   9070  C CA  . PRO F 3 126 ? 53.238  28.987  55.658  1.000 38.130  ? 126 PRO CCC CA  1 
ATOM   9071  C C   . PRO F 3 126 ? 54.504  29.757  55.267  1.000 38.106  ? 126 PRO CCC C   1 
ATOM   9072  O O   . PRO F 3 126 ? 55.114  29.462  54.250  1.000 34.409  ? 126 PRO CCC O   1 
ATOM   9073  C CB  . PRO F 3 126 ? 53.530  27.708  56.454  1.000 37.828  ? 126 PRO CCC CB  1 
ATOM   9074  C CG  . PRO F 3 126 ? 53.527  26.602  55.428  1.000 37.872  ? 126 PRO CCC CG  1 
ATOM   9075  C CD  . PRO F 3 126 ? 52.602  27.054  54.317  1.000 40.107  ? 126 PRO CCC CD  1 
ATOM   9076  N N   . SER F 3 127 ? 54.834  30.747  56.090  1.000 41.215  ? 127 SER CCC N   1 
ATOM   9077  C CA  . SER F 3 127 ? 56.068  31.567  56.014  1.000 47.604  ? 127 SER CCC CA  1 
ATOM   9078  C C   . SER F 3 127 ? 57.295  30.688  56.261  1.000 49.200  ? 127 SER CCC C   1 
ATOM   9079  O O   . SER F 3 127 ? 57.180  29.734  57.042  1.000 50.365  ? 127 SER CCC O   1 
ATOM   9080  C CB  . SER F 3 127 ? 55.991  32.652  57.040  1.000 50.265  ? 127 SER CCC CB  1 
ATOM   9081  O OG  . SER F 3 127 ? 55.528  32.107  58.273  1.000 54.336  ? 127 SER CCC OG  1 
ATOM   9082  N N   . ASP F 3 128 ? 58.432  31.033  55.663  1.000 51.723  ? 128 ASP CCC N   1 
ATOM   9083  C CA  . ASP F 3 128 ? 59.727  30.352  55.927  1.000 55.083  ? 128 ASP CCC CA  1 
ATOM   9084  C C   . ASP F 3 128 ? 60.065  30.553  57.408  1.000 56.304  ? 128 ASP CCC C   1 
ATOM   9085  O O   . ASP F 3 128 ? 60.598  29.605  58.037  1.000 51.379  ? 128 ASP CCC O   1 
ATOM   9086  C CB  . ASP F 3 128 ? 60.849  30.871  55.024  1.000 63.644  ? 128 ASP CCC CB  1 
ATOM   9087  C CG  . ASP F 3 128 ? 60.783  30.419  53.570  1.000 74.057  ? 128 ASP CCC CG  1 
ATOM   9088  O OD1 . ASP F 3 128 ? 59.989  29.493  53.245  1.000 75.794  ? 128 ASP CCC OD1 1 
ATOM   9089  O OD2 . ASP F 3 128 ? 61.541  30.997  52.761  1.000 78.749  ? 128 ASP CCC OD2 1 
ATOM   9090  N N   . GLU F 3 129 ? 59.730  31.737  57.940  1.000 60.442  ? 129 GLU CCC N   1 
ATOM   9091  C CA  . GLU F 3 129 ? 60.010  32.152  59.339  1.000 58.886  ? 129 GLU CCC CA  1 
ATOM   9092  C C   . GLU F 3 129 ? 59.257  31.231  60.316  1.000 54.140  ? 129 GLU CCC C   1 
ATOM   9093  O O   . GLU F 3 129 ? 59.876  30.789  61.300  1.000 52.123  ? 129 GLU CCC O   1 
ATOM   9094  C CB  . GLU F 3 129 ? 59.673  33.634  59.499  1.000 66.103  ? 129 GLU CCC CB  1 
ATOM   9095  C CG  . GLU F 3 129 ? 60.385  34.304  60.674  1.000 74.498  ? 129 GLU CCC CG  1 
ATOM   9096  C CD  . GLU F 3 129 ? 59.555  35.367  61.391  1.000 83.865  ? 129 GLU CCC CD  1 
ATOM   9097  O OE1 . GLU F 3 129 ? 58.722  36.043  60.714  1.000 79.036  ? 129 GLU CCC OE1 1 
ATOM   9098  O OE2 . GLU F 3 129 ? 59.707  35.494  62.637  1.000 86.841  ? 129 GLU CCC OE2 1 
ATOM   9099  N N   . GLN F 3 130 ? 57.991  30.895  60.051  1.000 49.373  ? 130 GLN CCC N   1 
ATOM   9100  C CA  . GLN F 3 130 ? 57.204  29.988  60.937  1.000 48.135  ? 130 GLN CCC CA  1 
ATOM   9101  C C   . GLN F 3 130 ? 57.827  28.586  60.921  1.000 47.278  ? 130 GLN CCC C   1 
ATOM   9102  O O   . GLN F 3 130 ? 57.808  27.907  61.958  1.000 42.995  ? 130 GLN CCC O   1 
ATOM   9103  C CB  . GLN F 3 130 ? 55.729  29.905  60.524  1.000 46.601  ? 130 GLN CCC CB  1 
ATOM   9104  C CG  . GLN F 3 130 ? 54.878  29.082  61.495  1.000 47.205  ? 130 GLN CCC CG  1 
ATOM   9105  C CD  . GLN F 3 130 ? 53.441  28.951  61.054  1.000 46.003  ? 130 GLN CCC CD  1 
ATOM   9106  O OE1 . GLN F 3 130 ? 53.108  29.218  59.903  1.000 49.134  ? 130 GLN CCC OE1 1 
ATOM   9107  N NE2 . GLN F 3 130 ? 52.580  28.535  61.969  1.000 41.358  ? 130 GLN CCC NE2 1 
ATOM   9108  N N   . LEU F 3 131 ? 58.320  28.146  59.768  1.000 50.146  ? 131 LEU CCC N   1 
ATOM   9109  C CA  . LEU F 3 131 ? 58.834  26.768  59.589  1.000 55.153  ? 131 LEU CCC CA  1 
ATOM   9110  C C   . LEU F 3 131 ? 60.077  26.576  60.461  1.000 60.237  ? 131 LEU CCC C   1 
ATOM   9111  O O   . LEU F 3 131 ? 60.264  25.463  60.971  1.000 60.812  ? 131 LEU CCC O   1 
ATOM   9112  C CB  . LEU F 3 131 ? 59.133  26.535  58.105  1.000 57.201  ? 131 LEU CCC CB  1 
ATOM   9113  C CG  . LEU F 3 131 ? 57.913  26.298  57.221  1.000 54.666  ? 131 LEU CCC CG  1 
ATOM   9114  C CD1 . LEU F 3 131 ? 58.265  26.437  55.746  1.000 52.439  ? 131 LEU CCC CD1 1 
ATOM   9115  C CD2 . LEU F 3 131 ? 57.314  24.931  57.509  1.000 55.987  ? 131 LEU CCC CD2 1 
ATOM   9116  N N   . LYS F 3 132 ? 60.885  27.623  60.639  1.000 65.956  ? 132 LYS CCC N   1 
ATOM   9117  C CA  . LYS F 3 132 ? 62.042  27.605  61.574  1.000 68.869  ? 132 LYS CCC CA  1 
ATOM   9118  C C   . LYS F 3 132 ? 61.561  27.256  62.990  1.000 62.810  ? 132 LYS CCC C   1 
ATOM   9119  O O   . LYS F 3 132 ? 62.259  26.491  63.667  1.000 62.553  ? 132 LYS CCC O   1 
ATOM   9120  C CB  . LYS F 3 132 ? 62.791  28.941  61.552  1.000 75.903  ? 132 LYS CCC CB  1 
ATOM   9121  C CG  . LYS F 3 132 ? 63.707  29.126  60.349  1.000 88.173  ? 132 LYS CCC CG  1 
ATOM   9122  C CD  . LYS F 3 132 ? 64.648  30.320  60.441  1.000 96.460  ? 132 LYS CCC CD  1 
ATOM   9123  C CE  . LYS F 3 132 ? 64.000  31.613  59.988  1.000 103.824 ? 132 LYS CCC CE  1 
ATOM   9124  N NZ  . LYS F 3 132 ? 64.988  32.694  59.779  1.000 103.059 ? 132 LYS CCC NZ  1 
ATOM   9125  N N   . SER F 3 133 ? 60.415  27.786  63.421  1.000 60.973  ? 133 SER CCC N   1 
ATOM   9126  C CA  . SER F 3 133 ? 59.851  27.549  64.777  1.000 63.803  ? 133 SER CCC CA  1 
ATOM   9127  C C   . SER F 3 133 ? 59.363  26.096  64.924  1.000 66.536  ? 133 SER CCC C   1 
ATOM   9128  O O   . SER F 3 133 ? 59.191  25.655  66.076  1.000 69.656  ? 133 SER CCC O   1 
ATOM   9129  C CB  . SER F 3 133 ? 58.756  28.543  65.098  1.000 64.124  ? 133 SER CCC CB  1 
ATOM   9130  O OG  . SER F 3 133 ? 57.566  28.259  64.367  1.000 62.600  ? 133 SER CCC OG  1 
ATOM   9131  N N   . GLY F 3 134 ? 59.109  25.390  63.815  1.000 65.916  ? 134 GLY CCC N   1 
ATOM   9132  C CA  . GLY F 3 134 ? 58.787  23.949  63.804  1.000 61.276  ? 134 GLY CCC CA  1 
ATOM   9133  C C   . GLY F 3 134 ? 57.293  23.640  63.734  1.000 60.992  ? 134 GLY CCC C   1 
ATOM   9134  O O   . GLY F 3 134 ? 56.951  22.456  63.917  1.000 64.316  ? 134 GLY CCC O   1 
ATOM   9135  N N   . THR F 3 135 ? 56.417  24.629  63.498  1.000 58.975  ? 135 THR CCC N   1 
ATOM   9136  C CA  . THR F 3 135 ? 55.014  24.393  63.043  1.000 53.977  ? 135 THR CCC CA  1 
ATOM   9137  C C   . THR F 3 135 ? 54.804  25.067  61.681  1.000 44.965  ? 135 THR CCC C   1 
ATOM   9138  O O   . THR F 3 135 ? 55.700  25.811  61.222  1.000 40.726  ? 135 THR CCC O   1 
ATOM   9139  C CB  . THR F 3 135 ? 53.944  24.822  64.062  1.000 55.109  ? 135 THR CCC CB  1 
ATOM   9140  O OG1 . THR F 3 135 ? 54.074  26.233  64.255  1.000 65.361  ? 135 THR CCC OG1 1 
ATOM   9141  C CG2 . THR F 3 135 ? 54.040  24.071  65.373  1.000 53.696  ? 135 THR CCC CG2 1 
ATOM   9142  N N   . ALA F 3 136 ? 53.677  24.750  61.044  1.000 38.628  ? 136 ALA CCC N   1 
ATOM   9143  C CA  . ALA F 3 136 ? 53.288  25.238  59.704  1.000 38.253  ? 136 ALA CCC CA  1 
ATOM   9144  C C   . ALA F 3 136 ? 51.784  25.494  59.695  1.000 36.812  ? 136 ALA CCC C   1 
ATOM   9145  O O   . ALA F 3 136 ? 51.020  24.579  60.041  1.000 38.357  ? 136 ALA CCC O   1 
ATOM   9146  C CB  . ALA F 3 136 ? 53.678  24.255  58.630  1.000 37.103  ? 136 ALA CCC CB  1 
ATOM   9147  N N   . SER F 3 137 ? 51.388  26.716  59.355  1.000 34.065  ? 137 SER CCC N   1 
ATOM   9148  C CA  . SER F 3 137 ? 49.972  27.123  59.282  1.000 35.411  ? 137 SER CCC CA  1 
ATOM   9149  C C   . SER F 3 137 ? 49.632  27.449  57.826  1.000 35.519  ? 137 SER CCC C   1 
ATOM   9150  O O   . SER F 3 137 ? 50.288  28.323  57.249  1.000 44.190  ? 137 SER CCC O   1 
ATOM   9151  C CB  . SER F 3 137 ? 49.707  28.255  60.234  1.000 35.829  ? 137 SER CCC CB  1 
ATOM   9152  O OG  . SER F 3 137 ? 49.738  27.802  61.588  1.000 37.603  ? 137 SER CCC OG  1 
ATOM   9153  N N   . VAL F 3 138 ? 48.698  26.706  57.234  1.000 33.849  ? 138 VAL CCC N   1 
ATOM   9154  C CA  . VAL F 3 138 ? 48.170  26.951  55.864  1.000 32.522  ? 138 VAL CCC CA  1 
ATOM   9155  C C   . VAL F 3 138 ? 46.789  27.574  56.010  1.000 30.729  ? 138 VAL CCC C   1 
ATOM   9156  O O   . VAL F 3 138 ? 45.921  26.958  56.635  1.000 32.597  ? 138 VAL CCC O   1 
ATOM   9157  C CB  . VAL F 3 138 ? 48.117  25.663  55.037  1.000 35.581  ? 138 VAL CCC CB  1 
ATOM   9158  C CG1 . VAL F 3 138 ? 47.873  25.959  53.569  1.000 39.448  ? 138 VAL CCC CG1 1 
ATOM   9159  C CG2 . VAL F 3 138 ? 49.380  24.842  55.210  1.000 37.467  ? 138 VAL CCC CG2 1 
ATOM   9160  N N   . VAL F 3 139 ? 46.603  28.772  55.477  1.000 30.670  ? 139 VAL CCC N   1 
ATOM   9161  C CA  . VAL F 3 139 ? 45.355  29.552  55.676  1.000 31.574  ? 139 VAL CCC CA  1 
ATOM   9162  C C   . VAL F 3 139 ? 44.608  29.583  54.352  1.000 34.270  ? 139 VAL CCC C   1 
ATOM   9163  O O   . VAL F 3 139 ? 45.250  29.765  53.302  1.000 33.589  ? 139 VAL CCC O   1 
ATOM   9164  C CB  . VAL F 3 139 ? 45.639  30.969  56.197  1.000 31.009  ? 139 VAL CCC CB  1 
ATOM   9165  C CG1 . VAL F 3 139 ? 44.357  31.766  56.405  1.000 30.733  ? 139 VAL CCC CG1 1 
ATOM   9166  C CG2 . VAL F 3 139 ? 46.457  30.920  57.472  1.000 31.871  ? 139 VAL CCC CG2 1 
ATOM   9167  N N   . CYS F 3 140 ? 43.299  29.366  54.423  1.000 36.322  ? 140 CYS CCC N   1 
ATOM   9168  C CA  . CYS F 3 140 ? 42.370  29.532  53.291  1.000 39.100  ? 140 CYS CCC CA  1 
ATOM   9169  C C   . CYS F 3 140 ? 41.371  30.633  53.634  1.000 38.032  ? 140 CYS CCC C   1 
ATOM   9170  O O   . CYS F 3 140 ? 40.788  30.559  54.727  1.000 36.926  ? 140 CYS CCC O   1 
ATOM   9171  C CB  . CYS F 3 140 ? 41.642  28.241  52.990  1.000 42.606  ? 140 CYS CCC CB  1 
ATOM   9172  S SG  . CYS F 3 140 ? 40.882  28.295  51.355  1.000 50.332  ? 140 CYS CCC SG  1 
ATOM   9173  N N   . LEU F 3 141 ? 41.246  31.625  52.747  1.000 37.780  ? 141 LEU CCC N   1 
ATOM   9174  C CA  . LEU F 3 141 ? 40.371  32.806  52.929  1.000 39.442  ? 141 LEU CCC CA  1 
ATOM   9175  C C   . LEU F 3 141 ? 39.209  32.701  51.949  1.000 39.780  ? 141 LEU CCC C   1 
ATOM   9176  O O   . LEU F 3 141 ? 39.460  32.609  50.749  1.000 40.030  ? 141 LEU CCC O   1 
ATOM   9177  C CB  . LEU F 3 141 ? 41.172  34.091  52.694  1.000 39.518  ? 141 LEU CCC CB  1 
ATOM   9178  C CG  . LEU F 3 141 ? 40.369  35.385  52.795  1.000 40.347  ? 141 LEU CCC CG  1 
ATOM   9179  C CD1 . LEU F 3 141 ? 39.704  35.494  54.160  1.000 39.753  ? 141 LEU CCC CD1 1 
ATOM   9180  C CD2 . LEU F 3 141 ? 41.259  36.585  52.518  1.000 41.649  ? 141 LEU CCC CD2 1 
ATOM   9181  N N   . LEU F 3 142 ? 37.989  32.696  52.475  1.000 40.981  ? 142 LEU CCC N   1 
ATOM   9182  C CA  . LEU F 3 142 ? 36.737  32.926  51.714  1.000 42.476  ? 142 LEU CCC CA  1 
ATOM   9183  C C   . LEU F 3 142 ? 36.315  34.372  51.986  1.000 40.945  ? 142 LEU CCC C   1 
ATOM   9184  O O   . LEU F 3 142 ? 35.993  34.674  53.149  1.000 42.918  ? 142 LEU CCC O   1 
ATOM   9185  C CB  . LEU F 3 142 ? 35.667  31.926  52.180  1.000 44.347  ? 142 LEU CCC CB  1 
ATOM   9186  C CG  . LEU F 3 142 ? 35.774  30.503  51.627  1.000 43.577  ? 142 LEU CCC CG  1 
ATOM   9187  C CD1 . LEU F 3 142 ? 37.048  29.829  52.118  1.000 47.435  ? 142 LEU CCC CD1 1 
ATOM   9188  C CD2 . LEU F 3 142 ? 34.547  29.700  52.023  1.000 42.616  ? 142 LEU CCC CD2 1 
ATOM   9189  N N   . ASN F 3 143 ? 36.303  35.224  50.962  1.000 39.270  ? 143 ASN CCC N   1 
ATOM   9190  C CA  . ASN F 3 143 ? 36.107  36.688  51.115  1.000 39.252  ? 143 ASN CCC CA  1 
ATOM   9191  C C   . ASN F 3 143 ? 34.726  37.099  50.591  1.000 39.752  ? 143 ASN CCC C   1 
ATOM   9192  O O   . ASN F 3 143 ? 34.395  36.746  49.455  1.000 38.046  ? 143 ASN CCC O   1 
ATOM   9193  C CB  . ASN F 3 143 ? 37.239  37.449  50.424  1.000 39.452  ? 143 ASN CCC CB  1 
ATOM   9194  C CG  . ASN F 3 143 ? 37.491  38.809  51.023  1.000 38.128  ? 143 ASN CCC CG  1 
ATOM   9195  O OD1 . ASN F 3 143 ? 37.453  38.960  52.247  1.000 34.333  ? 143 ASN CCC OD1 1 
ATOM   9196  N ND2 . ASN F 3 143 ? 37.727  39.789  50.159  1.000 36.795  ? 143 ASN CCC ND2 1 
ATOM   9197  N N   . ASN F 3 144 ? 33.961  37.823  51.419  1.000 43.702  ? 144 ASN CCC N   1 
ATOM   9198  C CA  . ASN F 3 144 ? 32.698  38.555  51.087  1.000 43.073  ? 144 ASN CCC CA  1 
ATOM   9199  C C   . ASN F 3 144 ? 31.717  37.660  50.327  1.000 41.457  ? 144 ASN CCC C   1 
ATOM   9200  O O   . ASN F 3 144 ? 31.574  37.846  49.102  1.000 40.160  ? 144 ASN CCC O   1 
ATOM   9201  C CB  . ASN F 3 144 ? 32.955  39.824  50.277  1.000 42.540  ? 144 ASN CCC CB  1 
ATOM   9202  C CG  . ASN F 3 144 ? 34.062  40.662  50.867  1.000 41.079  ? 144 ASN CCC CG  1 
ATOM   9203  O OD1 . ASN F 3 144 ? 34.107  40.917  52.071  1.000 37.973  ? 144 ASN CCC OD1 1 
ATOM   9204  N ND2 . ASN F 3 144 ? 34.984  41.050  50.008  1.000 42.520  ? 144 ASN CCC ND2 1 
ATOM   9205  N N   . PHE F 3 145 ? 31.051  36.755  51.053  1.000 40.231  ? 145 PHE CCC N   1 
ATOM   9206  C CA  . PHE F 3 145 ? 30.047  35.805  50.523  1.000 37.482  ? 145 PHE CCC CA  1 
ATOM   9207  C C   . PHE F 3 145 ? 28.805  35.824  51.409  1.000 36.423  ? 145 PHE CCC C   1 
ATOM   9208  O O   . PHE F 3 145 ? 28.904  36.241  52.571  1.000 32.193  ? 145 PHE CCC O   1 
ATOM   9209  C CB  . PHE F 3 145 ? 30.630  34.400  50.427  1.000 36.255  ? 145 PHE CCC CB  1 
ATOM   9210  C CG  . PHE F 3 145 ? 31.034  33.801  51.744  1.000 37.002  ? 145 PHE CCC CG  1 
ATOM   9211  C CD1 . PHE F 3 145 ? 30.167  32.975  52.427  1.000 38.977  ? 145 PHE CCC CD1 1 
ATOM   9212  C CD2 . PHE F 3 145 ? 32.289  34.023  52.275  1.000 36.505  ? 145 PHE CCC CD2 1 
ATOM   9213  C CE1 . PHE F 3 145 ? 30.544  32.389  53.623  1.000 38.949  ? 145 PHE CCC CE1 1 
ATOM   9214  C CE2 . PHE F 3 145 ? 32.658  33.450  53.476  1.000 36.769  ? 145 PHE CCC CE2 1 
ATOM   9215  C CZ  . PHE F 3 145 ? 31.788  32.632  54.145  1.000 38.266  ? 145 PHE CCC CZ  1 
ATOM   9216  N N   . TYR F 3 146 ? 27.674  35.423  50.820  1.000 38.664  ? 146 TYR CCC N   1 
ATOM   9217  C CA  . TYR F 3 146 ? 26.370  35.200  51.486  1.000 39.559  ? 146 TYR CCC CA  1 
ATOM   9218  C C   . TYR F 3 146 ? 25.671  34.057  50.766  1.000 39.968  ? 146 TYR CCC C   1 
ATOM   9219  O O   . TYR F 3 146 ? 25.749  34.019  49.545  1.000 38.152  ? 146 TYR CCC O   1 
ATOM   9220  C CB  . TYR F 3 146 ? 25.482  36.448  51.483  1.000 39.516  ? 146 TYR CCC CB  1 
ATOM   9221  C CG  . TYR F 3 146 ? 24.284  36.239  52.372  1.000 39.314  ? 146 TYR CCC CG  1 
ATOM   9222  C CD1 . TYR F 3 146 ? 24.387  36.363  53.743  1.000 42.055  ? 146 TYR CCC CD1 1 
ATOM   9223  C CD2 . TYR F 3 146 ? 23.098  35.771  51.861  1.000 39.869  ? 146 TYR CCC CD2 1 
ATOM   9224  C CE1 . TYR F 3 146 ? 23.322  36.076  54.577  1.000 45.015  ? 146 TYR CCC CE1 1 
ATOM   9225  C CE2 . TYR F 3 146 ? 22.020  35.485  52.679  1.000 44.997  ? 146 TYR CCC CE2 1 
ATOM   9226  C CZ  . TYR F 3 146 ? 22.130  35.637  54.045  1.000 46.289  ? 146 TYR CCC CZ  1 
ATOM   9227  O OH  . TYR F 3 146 ? 21.084  35.342  54.870  1.000 54.076  ? 146 TYR CCC OH  1 
ATOM   9228  N N   . PRO F 3 147 ? 25.010  33.093  51.467  1.000 42.139  ? 147 PRO CCC N   1 
ATOM   9229  C CA  . PRO F 3 147 ? 24.971  33.021  52.933  1.000 42.328  ? 147 PRO CCC CA  1 
ATOM   9230  C C   . PRO F 3 147 ? 26.224  32.444  53.598  1.000 42.596  ? 147 PRO CCC C   1 
ATOM   9231  O O   . PRO F 3 147 ? 27.168  32.129  52.900  1.000 36.914  ? 147 PRO CCC O   1 
ATOM   9232  C CB  . PRO F 3 147 ? 23.812  32.062  53.192  1.000 42.824  ? 147 PRO CCC CB  1 
ATOM   9233  C CG  . PRO F 3 147 ? 23.952  31.091  52.047  1.000 43.235  ? 147 PRO CCC CG  1 
ATOM   9234  C CD  . PRO F 3 147 ? 24.245  31.990  50.867  1.000 42.084  ? 147 PRO CCC CD  1 
ATOM   9235  N N   . ARG F 3 148 ? 26.176  32.307  54.925  1.000 46.701  ? 148 ARG CCC N   1 
ATOM   9236  C CA  . ARG F 3 148 ? 27.343  31.915  55.755  1.000 47.237  ? 148 ARG CCC CA  1 
ATOM   9237  C C   . ARG F 3 148 ? 27.720  30.451  55.530  1.000 44.214  ? 148 ARG CCC C   1 
ATOM   9238  O O   . ARG F 3 148 ? 28.889  30.125  55.782  1.000 43.523  ? 148 ARG CCC O   1 
ATOM   9239  C CB  . ARG F 3 148 ? 27.059  32.125  57.244  1.000 51.558  ? 148 ARG CCC CB  1 
ATOM   9240  C CG  . ARG F 3 148 ? 28.321  32.025  58.084  1.000 56.560  ? 148 ARG CCC CG  1 
ATOM   9241  C CD  . ARG F 3 148 ? 28.105  31.480  59.481  1.000 61.417  ? 148 ARG CCC CD  1 
ATOM   9242  N NE  . ARG F 3 148 ? 29.250  30.771  60.083  1.000 65.079  ? 148 ARG CCC NE  1 
ATOM   9243  C CZ  . ARG F 3 148 ? 30.073  29.862  59.500  1.000 62.146  ? 148 ARG CCC CZ  1 
ATOM   9244  N NH1 . ARG F 3 148 ? 29.967  29.498  58.232  1.000 59.385  ? 148 ARG CCC NH1 1 
ATOM   9245  N NH2 . ARG F 3 148 ? 31.039  29.305  60.214  1.000 59.930  ? 148 ARG CCC NH2 1 
ATOM   9246  N N   . GLU F 3 149 ? 26.781  29.591  55.130  1.000 49.670  ? 149 GLU CCC N   1 
ATOM   9247  C CA  . GLU F 3 149 ? 27.055  28.133  54.942  1.000 57.899  ? 149 GLU CCC CA  1 
ATOM   9248  C C   . GLU F 3 149 ? 27.988  27.964  53.748  1.000 49.968  ? 149 GLU CCC C   1 
ATOM   9249  O O   . GLU F 3 149 ? 27.673  28.457  52.670  1.000 46.161  ? 149 GLU CCC O   1 
ATOM   9250  C CB  . GLU F 3 149 ? 25.814  27.251  54.728  1.000 71.667  ? 149 GLU CCC CB  1 
ATOM   9251  C CG  . GLU F 3 149 ? 24.818  27.286  55.879  1.000 95.343  ? 149 GLU CCC CG  1 
ATOM   9252  C CD  . GLU F 3 149 ? 23.882  28.496  55.858  1.000 119.658 ? 149 GLU CCC CD  1 
ATOM   9253  O OE1 . GLU F 3 149 ? 23.070  28.577  54.917  1.000 143.895 ? 149 GLU CCC OE1 1 
ATOM   9254  O OE2 . GLU F 3 149 ? 23.979  29.380  56.756  1.000 119.094 ? 149 GLU CCC OE2 1 
ATOM   9255  N N   . ALA F 3 150 ? 29.109  27.288  53.976  1.000 47.910  ? 150 ALA CCC N   1 
ATOM   9256  C CA  . ALA F 3 150 ? 30.085  26.886  52.946  1.000 49.032  ? 150 ALA CCC CA  1 
ATOM   9257  C C   . ALA F 3 150 ? 30.889  25.696  53.471  1.000 48.329  ? 150 ALA CCC C   1 
ATOM   9258  O O   . ALA F 3 150 ? 31.262  25.689  54.658  1.000 46.542  ? 150 ALA CCC O   1 
ATOM   9259  C CB  . ALA F 3 150 ? 30.959  28.060  52.597  1.000 52.863  ? 150 ALA CCC CB  1 
ATOM   9260  N N   . LYS F 3 151 ? 31.117  24.711  52.612  1.000 48.466  ? 151 LYS CCC N   1 
ATOM   9261  C CA  . LYS F 3 151 ? 32.016  23.576  52.900  1.000 53.094  ? 151 LYS CCC CA  1 
ATOM   9262  C C   . LYS F 3 151 ? 33.426  24.002  52.479  1.000 47.929  ? 151 LYS CCC C   1 
ATOM   9263  O O   . LYS F 3 151 ? 33.612  24.429  51.339  1.000 43.879  ? 151 LYS CCC O   1 
ATOM   9264  C CB  . LYS F 3 151 ? 31.493  22.318  52.199  1.000 65.984  ? 151 LYS CCC CB  1 
ATOM   9265  C CG  . LYS F 3 151 ? 32.418  21.108  52.258  1.000 76.614  ? 151 LYS CCC CG  1 
ATOM   9266  C CD  . LYS F 3 151 ? 31.787  19.861  52.829  1.000 85.028  ? 151 LYS CCC CD  1 
ATOM   9267  C CE  . LYS F 3 151 ? 32.796  19.034  53.604  1.000 98.667  ? 151 LYS CCC CE  1 
ATOM   9268  N NZ  . LYS F 3 151 ? 32.451  17.594  53.604  1.000 109.570 ? 151 LYS CCC NZ  1 
ATOM   9269  N N   . VAL F 3 152 ? 34.374  23.918  53.397  1.000 46.518  ? 152 VAL CCC N   1 
ATOM   9270  C CA  . VAL F 3 152 ? 35.817  24.122  53.119  1.000 50.005  ? 152 VAL CCC CA  1 
ATOM   9271  C C   . VAL F 3 152 ? 36.508  22.795  53.419  1.000 52.466  ? 152 VAL CCC C   1 
ATOM   9272  O O   . VAL F 3 152 ? 36.458  22.364  54.591  1.000 51.186  ? 152 VAL CCC O   1 
ATOM   9273  C CB  . VAL F 3 152 ? 36.394  25.257  53.978  1.000 54.539  ? 152 VAL CCC CB  1 
ATOM   9274  C CG1 . VAL F 3 152 ? 37.900  25.334  53.858  1.000 61.913  ? 152 VAL CCC CG1 1 
ATOM   9275  C CG2 . VAL F 3 152 ? 35.764  26.595  53.650  1.000 53.849  ? 152 VAL CCC CG2 1 
ATOM   9276  N N   . GLN F 3 153 ? 37.096  22.172  52.396  1.000 54.949  ? 153 GLN CCC N   1 
ATOM   9277  C CA  . GLN F 3 153 ? 37.774  20.858  52.504  1.000 57.587  ? 153 GLN CCC CA  1 
ATOM   9278  C C   . GLN F 3 153 ? 39.265  21.067  52.229  1.000 53.923  ? 153 GLN CCC C   1 
ATOM   9279  O O   . GLN F 3 153 ? 39.604  21.590  51.142  1.000 57.659  ? 153 GLN CCC O   1 
ATOM   9280  C CB  . GLN F 3 153 ? 37.175  19.871  51.508  1.000 67.172  ? 153 GLN CCC CB  1 
ATOM   9281  C CG  . GLN F 3 153 ? 37.486  18.413  51.818  1.000 73.526  ? 153 GLN CCC CG  1 
ATOM   9282  C CD  . GLN F 3 153 ? 36.261  17.667  52.281  1.000 77.244  ? 153 GLN CCC CD  1 
ATOM   9283  O OE1 . GLN F 3 153 ? 35.174  17.838  51.731  1.000 69.798  ? 153 GLN CCC OE1 1 
ATOM   9284  N NE2 . GLN F 3 153 ? 36.428  16.820  53.288  1.000 79.916  ? 153 GLN CCC NE2 1 
ATOM   9285  N N   . TRP F 3 154 ? 40.121  20.682  53.169  1.000 49.772  ? 154 TRP CCC N   1 
ATOM   9286  C CA  . TRP F 3 154 ? 41.593  20.706  52.968  1.000 49.093  ? 154 TRP CCC CA  1 
ATOM   9287  C C   . TRP F 3 154 ? 42.011  19.429  52.238  1.000 49.620  ? 154 TRP CCC C   1 
ATOM   9288  O O   . TRP F 3 154 ? 41.517  18.370  52.623  1.000 50.928  ? 154 TRP CCC O   1 
ATOM   9289  C CB  . TRP F 3 154 ? 42.321  20.865  54.311  1.000 47.994  ? 154 TRP CCC CB  1 
ATOM   9290  C CG  . TRP F 3 154 ? 42.350  22.276  54.802  1.000 44.657  ? 154 TRP CCC CG  1 
ATOM   9291  C CD1 . TRP F 3 154 ? 41.643  22.807  55.837  1.000 43.138  ? 154 TRP CCC CD1 1 
ATOM   9292  C CD2 . TRP F 3 154 ? 43.128  23.349  54.256  1.000 46.772  ? 154 TRP CCC CD2 1 
ATOM   9293  N NE1 . TRP F 3 154 ? 41.918  24.137  55.967  1.000 41.380  ? 154 TRP CCC NE1 1 
ATOM   9294  C CE2 . TRP F 3 154 ? 42.828  24.495  55.015  1.000 45.813  ? 154 TRP CCC CE2 1 
ATOM   9295  C CE3 . TRP F 3 154 ? 44.046  23.453  53.203  1.000 49.996  ? 154 TRP CCC CE3 1 
ATOM   9296  C CZ2 . TRP F 3 154 ? 43.425  25.725  54.759  1.000 50.225  ? 154 TRP CCC CZ2 1 
ATOM   9297  C CZ3 . TRP F 3 154 ? 44.634  24.671  52.949  1.000 50.824  ? 154 TRP CCC CZ3 1 
ATOM   9298  C CH2 . TRP F 3 154 ? 44.322  25.792  53.716  1.000 51.110  ? 154 TRP CCC CH2 1 
ATOM   9299  N N   . LYS F 3 155 ? 42.881  19.542  51.231  1.000 52.002  ? 155 LYS CCC N   1 
ATOM   9300  C CA  . LYS F 3 155 ? 43.405  18.393  50.447  1.000 53.070  ? 155 LYS CCC CA  1 
ATOM   9301  C C   . LYS F 3 155 ? 44.926  18.458  50.377  1.000 47.116  ? 155 LYS CCC C   1 
ATOM   9302  O O   . LYS F 3 155 ? 45.461  19.413  49.831  1.000 46.067  ? 155 LYS CCC O   1 
ATOM   9303  C CB  . LYS F 3 155 ? 42.784  18.379  49.052  1.000 57.430  ? 155 LYS CCC CB  1 
ATOM   9304  C CG  . LYS F 3 155 ? 41.419  17.713  49.049  1.000 60.586  ? 155 LYS CCC CG  1 
ATOM   9305  C CD  . LYS F 3 155 ? 40.628  17.934  47.802  1.000 65.039  ? 155 LYS CCC CD  1 
ATOM   9306  C CE  . LYS F 3 155 ? 39.244  17.352  47.957  1.000 69.277  ? 155 LYS CCC CE  1 
ATOM   9307  N NZ  . LYS F 3 155 ? 38.490  17.372  46.688  1.000 76.966  ? 155 LYS CCC NZ  1 
ATOM   9308  N N   . VAL F 3 156 ? 45.575  17.449  50.931  1.000 43.559  ? 156 VAL CCC N   1 
ATOM   9309  C CA  . VAL F 3 156 ? 47.052  17.348  51.016  1.000 45.394  ? 156 VAL CCC CA  1 
ATOM   9310  C C   . VAL F 3 156 ? 47.484  16.141  50.181  1.000 48.526  ? 156 VAL CCC C   1 
ATOM   9311  O O   . VAL F 3 156 ? 47.227  14.991  50.597  1.000 55.231  ? 156 VAL CCC O   1 
ATOM   9312  C CB  . VAL F 3 156 ? 47.477  17.267  52.488  1.000 44.442  ? 156 VAL CCC CB  1 
ATOM   9313  C CG1 . VAL F 3 156 ? 48.990  17.137  52.648  1.000 45.438  ? 156 VAL CCC CG1 1 
ATOM   9314  C CG2 . VAL F 3 156 ? 46.954  18.492  53.223  1.000 42.170  ? 156 VAL CCC CG2 1 
ATOM   9315  N N   . ASP F 3 157 ? 48.110  16.416  49.032  1.000 48.959  ? 157 ASP CCC N   1 
ATOM   9316  C CA  . ASP F 3 157 ? 48.408  15.425  47.969  1.000 47.642  ? 157 ASP CCC CA  1 
ATOM   9317  C C   . ASP F 3 157 ? 47.094  14.703  47.668  1.000 48.697  ? 157 ASP CCC C   1 
ATOM   9318  O O   . ASP F 3 157 ? 47.098  13.492  47.532  1.000 51.383  ? 157 ASP CCC O   1 
ATOM   9319  C CB  . ASP F 3 157 ? 49.543  14.488  48.384  1.000 48.085  ? 157 ASP CCC CB  1 
ATOM   9320  C CG  . ASP F 3 157 ? 50.925  15.120  48.307  1.000 50.549  ? 157 ASP CCC CG  1 
ATOM   9321  O OD1 . ASP F 3 157 ? 51.066  16.112  47.554  1.000 48.762  ? 157 ASP CCC OD1 1 
ATOM   9322  O OD2 . ASP F 3 157 ? 51.851  14.604  48.984  1.000 56.554  ? 157 ASP CCC OD2 1 
ATOM   9323  N N   . ASN F 3 158 ? 45.994  15.445  47.632  1.000 48.719  ? 158 ASN CCC N   1 
ATOM   9324  C CA  . ASN F 3 158 ? 44.670  14.965  47.177  1.000 48.935  ? 158 ASN CCC CA  1 
ATOM   9325  C C   . ASN F 3 158 ? 44.012  14.037  48.220  1.000 47.937  ? 158 ASN CCC C   1 
ATOM   9326  O O   . ASN F 3 158 ? 42.871  13.577  47.952  1.000 45.342  ? 158 ASN CCC O   1 
ATOM   9327  C CB  . ASN F 3 158 ? 44.798  14.376  45.773  1.000 48.468  ? 158 ASN CCC CB  1 
ATOM   9328  C CG  . ASN F 3 158 ? 43.592  14.698  44.917  1.000 51.477  ? 158 ASN CCC CG  1 
ATOM   9329  O OD1 . ASN F 3 158 ? 42.910  15.691  45.163  1.000 54.444  ? 158 ASN CCC OD1 1 
ATOM   9330  N ND2 . ASN F 3 158 ? 43.281  13.833  43.964  1.000 54.524  ? 158 ASN CCC ND2 1 
ATOM   9331  N N   . ALA F 3 159 ? 44.621  13.880  49.401  1.000 45.845  ? 159 ALA CCC N   1 
ATOM   9332  C CA  . ALA F 3 159 ? 44.030  13.247  50.606  1.000 47.113  ? 159 ALA CCC CA  1 
ATOM   9333  C C   . ALA F 3 159 ? 43.243  14.267  51.442  1.000 46.549  ? 159 ALA CCC C   1 
ATOM   9334  O O   . ALA F 3 159 ? 43.860  15.246  51.899  1.000 51.032  ? 159 ALA CCC O   1 
ATOM   9335  C CB  . ALA F 3 159 ? 45.144  12.650  51.435  1.000 50.796  ? 159 ALA CCC CB  1 
ATOM   9336  N N   . LEU F 3 160 ? 41.954  14.029  51.690  1.000 47.204  ? 160 LEU CCC N   1 
ATOM   9337  C CA  . LEU F 3 160 ? 41.123  14.936  52.538  1.000 53.749  ? 160 LEU CCC CA  1 
ATOM   9338  C C   . LEU F 3 160 ? 41.673  14.927  53.974  1.000 50.374  ? 160 LEU CCC C   1 
ATOM   9339  O O   . LEU F 3 160 ? 41.645  13.863  54.599  1.000 51.953  ? 160 LEU CCC O   1 
ATOM   9340  C CB  . LEU F 3 160 ? 39.643  14.533  52.544  1.000 60.422  ? 160 LEU CCC CB  1 
ATOM   9341  C CG  . LEU F 3 160 ? 39.055  14.029  51.226  1.000 75.791  ? 160 LEU CCC CG  1 
ATOM   9342  C CD1 . LEU F 3 160 ? 37.538  14.098  51.261  1.000 82.072  ? 160 LEU CCC CD1 1 
ATOM   9343  C CD2 . LEU F 3 160 ? 39.590  14.815  50.041  1.000 86.552  ? 160 LEU CCC CD2 1 
ATOM   9344  N N   . GLN F 3 161 ? 42.123  16.076  54.491  1.000 48.148  ? 161 GLN CCC N   1 
ATOM   9345  C CA  . GLN F 3 161 ? 42.552  16.233  55.898  1.000 45.445  ? 161 GLN CCC CA  1 
ATOM   9346  C C   . GLN F 3 161 ? 41.352  16.566  56.761  1.000 45.454  ? 161 GLN CCC C   1 
ATOM   9347  O O   . GLN F 3 161 ? 40.489  17.289  56.291  1.000 47.848  ? 161 GLN CCC O   1 
ATOM   9348  C CB  . GLN F 3 161 ? 43.529  17.378  56.043  1.000 50.105  ? 161 GLN CCC CB  1 
ATOM   9349  C CG  . GLN F 3 161 ? 44.848  17.085  55.360  1.000 55.141  ? 161 GLN CCC CG  1 
ATOM   9350  C CD  . GLN F 3 161 ? 45.507  15.829  55.869  1.000 55.938  ? 161 GLN CCC CD  1 
ATOM   9351  O OE1 . GLN F 3 161 ? 45.743  15.658  57.075  1.000 51.599  ? 161 GLN CCC OE1 1 
ATOM   9352  N NE2 . GLN F 3 161 ? 45.792  14.938  54.931  1.000 61.966  ? 161 GLN CCC NE2 1 
ATOM   9353  N N   . SER F 3 162 ? 41.359  16.084  57.997  1.000 47.081  ? 162 SER CCC N   1 
ATOM   9354  C CA  . SER F 3 162 ? 40.228  16.205  58.944  1.000 45.494  ? 162 SER CCC CA  1 
ATOM   9355  C C   . SER F 3 162 ? 40.731  16.374  60.390  1.000 49.735  ? 162 SER CCC C   1 
ATOM   9356  O O   . SER F 3 162 ? 41.703  15.675  60.784  1.000 48.706  ? 162 SER CCC O   1 
ATOM   9357  C CB  . SER F 3 162 ? 39.348  15.032  58.783  1.000 42.999  ? 162 SER CCC CB  1 
ATOM   9358  O OG  . SER F 3 162 ? 38.317  15.067  59.749  1.000 47.472  ? 162 SER CCC OG  1 
ATOM   9359  N N   . GLY F 3 163 ? 40.136  17.338  61.110  1.000 56.554  ? 163 GLY CCC N   1 
ATOM   9360  C CA  . GLY F 3 163 ? 40.327  17.613  62.552  1.000 60.359  ? 163 GLY CCC CA  1 
ATOM   9361  C C   . GLY F 3 163 ? 41.682  18.224  62.904  1.000 56.310  ? 163 GLY CCC C   1 
ATOM   9362  O O   . GLY F 3 163 ? 41.984  18.303  64.109  1.000 53.565  ? 163 GLY CCC O   1 
ATOM   9363  N N   . ASN F 3 164 ? 42.451  18.694  61.921  1.000 52.382  ? 164 ASN CCC N   1 
ATOM   9364  C CA  . ASN F 3 164 ? 43.687  19.490  62.124  1.000 53.126  ? 164 ASN CCC CA  1 
ATOM   9365  C C   . ASN F 3 164 ? 43.443  20.894  61.551  1.000 53.300  ? 164 ASN CCC C   1 
ATOM   9366  O O   . ASN F 3 164 ? 44.415  21.531  61.113  1.000 55.020  ? 164 ASN CCC O   1 
ATOM   9367  C CB  . ASN F 3 164 ? 44.909  18.785  61.524  1.000 56.150  ? 164 ASN CCC CB  1 
ATOM   9368  C CG  . ASN F 3 164 ? 44.725  18.364  60.078  1.000 58.604  ? 164 ASN CCC CG  1 
ATOM   9369  O OD1 . ASN F 3 164 ? 43.649  18.536  59.506  1.000 69.110  ? 164 ASN CCC OD1 1 
ATOM   9370  N ND2 . ASN F 3 164 ? 45.766  17.814  59.473  1.000 52.971  ? 164 ASN CCC ND2 1 
ATOM   9371  N N   . SER F 3 165 ? 42.192  21.361  61.561  1.000 49.728  ? 165 SER CCC N   1 
ATOM   9372  C CA  . SER F 3 165 ? 41.801  22.672  60.991  1.000 50.475  ? 165 SER CCC CA  1 
ATOM   9373  C C   . SER F 3 165 ? 40.715  23.312  61.864  1.000 51.149  ? 165 SER CCC C   1 
ATOM   9374  O O   . SER F 3 165 ? 39.888  22.553  62.398  1.000 55.391  ? 165 SER CCC O   1 
ATOM   9375  C CB  . SER F 3 165 ? 41.359  22.498  59.560  1.000 50.186  ? 165 SER CCC CB  1 
ATOM   9376  O OG  . SER F 3 165 ? 39.990  22.127  59.477  1.000 48.668  ? 165 SER CCC OG  1 
ATOM   9377  N N   . GLN F 3 166 ? 40.726  24.642  62.020  1.000 49.709  ? 166 GLN CCC N   1 
ATOM   9378  C CA  . GLN F 3 166 ? 39.599  25.400  62.630  1.000 50.576  ? 166 GLN CCC CA  1 
ATOM   9379  C C   . GLN F 3 166 ? 39.177  26.504  61.657  1.000 43.604  ? 166 GLN CCC C   1 
ATOM   9380  O O   . GLN F 3 166 ? 40.007  27.020  60.910  1.000 38.001  ? 166 GLN CCC O   1 
ATOM   9381  C CB  . GLN F 3 166 ? 39.951  25.999  63.996  1.000 59.747  ? 166 GLN CCC CB  1 
ATOM   9382  C CG  . GLN F 3 166 ? 40.979  25.195  64.783  1.000 71.815  ? 166 GLN CCC CG  1 
ATOM   9383  C CD  . GLN F 3 166 ? 41.157  25.678  66.206  1.000 77.199  ? 166 GLN CCC CD  1 
ATOM   9384  O OE1 . GLN F 3 166 ? 42.270  25.978  66.664  1.000 72.530  ? 166 GLN CCC OE1 1 
ATOM   9385  N NE2 . GLN F 3 166 ? 40.045  25.754  66.921  1.000 78.910  ? 166 GLN CCC NE2 1 
ATOM   9386  N N   . GLU F 3 167 ? 37.891  26.819  61.659  1.000 42.826  ? 167 GLU CCC N   1 
ATOM   9387  C CA  . GLU F 3 167 ? 37.294  27.904  60.857  1.000 41.152  ? 167 GLU CCC CA  1 
ATOM   9388  C C   . GLU F 3 167 ? 37.052  29.084  61.785  1.000 41.008  ? 167 GLU CCC C   1 
ATOM   9389  O O   . GLU F 3 167 ? 37.111  28.903  63.017  1.000 41.789  ? 167 GLU CCC O   1 
ATOM   9390  C CB  . GLU F 3 167 ? 35.991  27.447  60.215  1.000 42.889  ? 167 GLU CCC CB  1 
ATOM   9391  C CG  . GLU F 3 167 ? 36.196  26.334  59.198  1.000 47.645  ? 167 GLU CCC CG  1 
ATOM   9392  C CD  . GLU F 3 167 ? 34.984  26.049  58.323  1.000 49.122  ? 167 GLU CCC CD  1 
ATOM   9393  O OE1 . GLU F 3 167 ? 33.861  26.456  58.705  1.000 49.286  ? 167 GLU CCC OE1 1 
ATOM   9394  O OE2 . GLU F 3 167 ? 35.170  25.424  57.259  1.000 54.829  ? 167 GLU CCC OE2 1 
ATOM   9395  N N   . SER F 3 168 ? 36.803  30.248  61.199  1.000 38.332  ? 168 SER CCC N   1 
ATOM   9396  C CA  . SER F 3 168 ? 36.660  31.528  61.925  1.000 36.813  ? 168 SER CCC CA  1 
ATOM   9397  C C   . SER F 3 168 ? 35.931  32.499  60.999  1.000 36.861  ? 168 SER CCC C   1 
ATOM   9398  O O   . SER F 3 168 ? 36.287  32.512  59.804  1.000 40.329  ? 168 SER CCC O   1 
ATOM   9399  C CB  . SER F 3 168 ? 38.013  32.021  62.338  1.000 35.577  ? 168 SER CCC CB  1 
ATOM   9400  O OG  . SER F 3 168 ? 37.908  32.930  63.415  1.000 37.679  ? 168 SER CCC OG  1 
ATOM   9401  N N   . VAL F 3 169 ? 34.938  33.251  61.494  1.000 34.125  ? 169 VAL CCC N   1 
ATOM   9402  C CA  . VAL F 3 169 ? 34.041  34.064  60.615  1.000 32.271  ? 169 VAL CCC CA  1 
ATOM   9403  C C   . VAL F 3 169 ? 33.902  35.505  61.121  1.000 33.372  ? 169 VAL CCC C   1 
ATOM   9404  O O   . VAL F 3 169 ? 33.822  35.708  62.335  1.000 33.330  ? 169 VAL CCC O   1 
ATOM   9405  C CB  . VAL F 3 169 ? 32.681  33.371  60.502  1.000 29.677  ? 169 VAL CCC CB  1 
ATOM   9406  C CG1 . VAL F 3 169 ? 31.661  34.191  59.764  1.000 28.987  ? 169 VAL CCC CG1 1 
ATOM   9407  C CG2 . VAL F 3 169 ? 32.848  32.051  59.803  1.000 31.775  ? 169 VAL CCC CG2 1 
ATOM   9408  N N   . THR F 3 170 ? 33.820  36.463  60.198  1.000 32.385  ? 170 THR CCC N   1 
ATOM   9409  C CA  . THR F 3 170 ? 33.566  37.891  60.493  1.000 34.017  ? 170 THR CCC CA  1 
ATOM   9410  C C   . THR F 3 170 ? 32.092  38.091  60.867  1.000 37.311  ? 170 THR CCC C   1 
ATOM   9411  O O   . THR F 3 170 ? 31.276  37.251  60.498  1.000 36.707  ? 170 THR CCC O   1 
ATOM   9412  C CB  . THR F 3 170 ? 33.969  38.790  59.318  1.000 34.772  ? 170 THR CCC CB  1 
ATOM   9413  O OG1 . THR F 3 170 ? 33.067  38.675  58.213  1.000 33.073  ? 170 THR CCC OG1 1 
ATOM   9414  C CG2 . THR F 3 170 ? 35.383  38.505  58.869  1.000 36.496  ? 170 THR CCC CG2 1 
ATOM   9415  N N   . GLU F 3 171 ? 31.794  39.173  61.589  1.000 43.001  ? 171 GLU CCC N   1 
ATOM   9416  C CA  . GLU F 3 171 ? 30.438  39.759  61.756  1.000 45.140  ? 171 GLU CCC CA  1 
ATOM   9417  C C   . GLU F 3 171 ? 29.883  40.050  60.357  1.000 38.219  ? 171 GLU CCC C   1 
ATOM   9418  O O   . GLU F 3 171 ? 30.642  40.507  59.493  1.000 32.661  ? 171 GLU CCC O   1 
ATOM   9419  C CB  . GLU F 3 171 ? 30.418  41.101  62.518  1.000 60.809  ? 171 GLU CCC CB  1 
ATOM   9420  C CG  . GLU F 3 171 ? 31.202  41.202  63.818  1.000 76.246  ? 171 GLU CCC CG  1 
ATOM   9421  C CD  . GLU F 3 171 ? 30.925  40.124  64.852  1.000 99.788  ? 171 GLU CCC CD  1 
ATOM   9422  O OE1 . GLU F 3 171 ? 31.564  40.198  65.929  1.000 110.775 ? 171 GLU CCC OE1 1 
ATOM   9423  O OE2 . GLU F 3 171 ? 30.137  39.175  64.560  1.000 120.998 ? 171 GLU CCC OE2 1 
ATOM   9424  N N   . GLN F 3 172 ? 28.593  39.831  60.131  1.000 38.027  ? 172 GLN CCC N   1 
ATOM   9425  C CA  . GLN F 3 172 ? 27.969  40.257  58.863  1.000 37.698  ? 172 GLN CCC CA  1 
ATOM   9426  C C   . GLN F 3 172 ? 28.323  41.732  58.666  1.000 36.001  ? 172 GLN CCC C   1 
ATOM   9427  O O   . GLN F 3 172 ? 28.143  42.502  59.603  1.000 34.037  ? 172 GLN CCC O   1 
ATOM   9428  C CB  . GLN F 3 172 ? 26.464  40.007  58.882  1.000 39.408  ? 172 GLN CCC CB  1 
ATOM   9429  C CG  . GLN F 3 172 ? 25.829  40.164  57.511  1.000 39.331  ? 172 GLN CCC CG  1 
ATOM   9430  C CD  . GLN F 3 172 ? 24.374  39.787  57.549  1.000 40.759  ? 172 GLN CCC CD  1 
ATOM   9431  O OE1 . GLN F 3 172 ? 23.658  40.119  58.494  1.000 39.581  ? 172 GLN CCC OE1 1 
ATOM   9432  N NE2 . GLN F 3 172 ? 23.945  39.063  56.527  1.000 39.152  ? 172 GLN CCC NE2 1 
ATOM   9433  N N   . ASP F 3 173 ? 28.814  42.092  57.484  1.000 38.792  ? 173 ASP CCC N   1 
ATOM   9434  C CA  . ASP F 3 173 ? 29.270  43.462  57.134  1.000 43.540  ? 173 ASP CCC CA  1 
ATOM   9435  C C   . ASP F 3 173 ? 28.092  44.445  57.144  1.000 43.943  ? 173 ASP CCC C   1 
ATOM   9436  O O   . ASP F 3 173 ? 27.030  44.097  56.604  1.000 41.095  ? 173 ASP CCC O   1 
ATOM   9437  C CB  . ASP F 3 173 ? 29.916  43.478  55.748  1.000 48.354  ? 173 ASP CCC CB  1 
ATOM   9438  C CG  . ASP F 3 173 ? 30.717  44.737  55.475  1.000 51.378  ? 173 ASP CCC CG  1 
ATOM   9439  O OD1 . ASP F 3 173 ? 31.889  44.760  55.888  1.000 59.370  ? 173 ASP CCC OD1 1 
ATOM   9440  O OD2 . ASP F 3 173 ? 30.161  45.677  54.861  1.000 50.215  ? 173 ASP CCC OD2 1 
ATOM   9441  N N   . SER F 3 174 ? 28.291  45.652  57.691  1.000 51.021  ? 174 SER CCC N   1 
ATOM   9442  C CA  . SER F 3 174 ? 27.228  46.687  57.859  1.000 53.498  ? 174 SER CCC CA  1 
ATOM   9443  C C   . SER F 3 174 ? 26.719  47.149  56.490  1.000 57.218  ? 174 SER CCC C   1 
ATOM   9444  O O   . SER F 3 174 ? 25.508  47.353  56.379  1.000 48.511  ? 174 SER CCC O   1 
ATOM   9445  C CB  . SER F 3 174 ? 27.698  47.860  58.663  1.000 55.436  ? 174 SER CCC CB  1 
ATOM   9446  O OG  . SER F 3 174 ? 28.540  47.441  59.721  1.000 62.590  ? 174 SER CCC OG  1 
ATOM   9447  N N   . LYS F 3 175 ? 27.603  47.291  55.496  1.000 68.461  ? 175 LYS CCC N   1 
ATOM   9448  C CA  . LYS F 3 175 ? 27.275  47.919  54.184  1.000 71.291  ? 175 LYS CCC CA  1 
ATOM   9449  C C   . LYS F 3 175 ? 26.764  46.870  53.182  1.000 65.959  ? 175 LYS CCC C   1 
ATOM   9450  O O   . LYS F 3 175 ? 25.753  47.170  52.544  1.000 65.764  ? 175 LYS CCC O   1 
ATOM   9451  C CB  . LYS F 3 175 ? 28.476  48.638  53.561  1.000 88.672  ? 175 LYS CCC CB  1 
ATOM   9452  C CG  . LYS F 3 175 ? 29.322  49.524  54.472  1.000 104.559 ? 175 LYS CCC CG  1 
ATOM   9453  C CD  . LYS F 3 175 ? 30.752  49.685  53.921  1.000 121.880 ? 175 LYS CCC CD  1 
ATOM   9454  C CE  . LYS F 3 175 ? 31.844  49.694  54.973  1.000 130.753 ? 175 LYS CCC CE  1 
ATOM   9455  N NZ  . LYS F 3 175 ? 31.740  50.894  55.832  1.000 150.568 ? 175 LYS CCC NZ  1 
ATOM   9456  N N   . ASP F 3 176 ? 27.432  45.713  53.015  1.000 61.406  ? 176 ASP CCC N   1 
ATOM   9457  C CA  . ASP F 3 176 ? 27.110  44.735  51.930  1.000 55.785  ? 176 ASP CCC CA  1 
ATOM   9458  C C   . ASP F 3 176 ? 26.538  43.418  52.489  1.000 49.814  ? 176 ASP CCC C   1 
ATOM   9459  O O   . ASP F 3 176 ? 26.222  42.548  51.676  1.000 52.859  ? 176 ASP CCC O   1 
ATOM   9460  C CB  . ASP F 3 176 ? 28.297  44.495  50.982  1.000 58.716  ? 176 ASP CCC CB  1 
ATOM   9461  C CG  . ASP F 3 176 ? 29.511  43.783  51.570  1.000 66.840  ? 176 ASP CCC CG  1 
ATOM   9462  O OD1 . ASP F 3 176 ? 29.451  43.384  52.743  1.000 70.342  ? 176 ASP CCC OD1 1 
ATOM   9463  O OD2 . ASP F 3 176 ? 30.520  43.633  50.838  1.000 71.761  ? 176 ASP CCC OD2 1 
ATOM   9464  N N   . SER F 3 177 ? 26.380  43.268  53.802  1.000 42.199  ? 177 SER CCC N   1 
ATOM   9465  C CA  . SER F 3 177 ? 25.748  42.083  54.442  1.000 39.571  ? 177 SER CCC CA  1 
ATOM   9466  C C   . SER F 3 177 ? 26.435  40.770  54.036  1.000 36.181  ? 177 SER CCC C   1 
ATOM   9467  O O   . SER F 3 177 ? 25.729  39.754  53.891  1.000 35.416  ? 177 SER CCC O   1 
ATOM   9468  C CB  . SER F 3 177 ? 24.280  42.027  54.134  1.000 38.375  ? 177 SER CCC CB  1 
ATOM   9469  O OG  . SER F 3 177 ? 23.618  43.184  54.595  1.000 39.433  ? 177 SER CCC OG  1 
ATOM   9470  N N   . THR F 3 178 ? 27.757  40.762  53.895  1.000 32.642  ? 178 THR CCC N   1 
ATOM   9471  C CA  . THR F 3 178 ? 28.521  39.534  53.572  1.000 34.256  ? 178 THR CCC CA  1 
ATOM   9472  C C   . THR F 3 178 ? 29.322  39.091  54.792  1.000 34.097  ? 178 THR CCC C   1 
ATOM   9473  O O   . THR F 3 178 ? 29.610  39.918  55.657  1.000 34.026  ? 178 THR CCC O   1 
ATOM   9474  C CB  . THR F 3 178 ? 29.429  39.749  52.362  1.000 35.787  ? 178 THR CCC CB  1 
ATOM   9475  O OG1 . THR F 3 178 ? 30.456  40.679  52.695  1.000 38.609  ? 178 THR CCC OG1 1 
ATOM   9476  C CG2 . THR F 3 178 ? 28.653  40.272  51.179  1.000 38.025  ? 178 THR CCC CG2 1 
ATOM   9477  N N   . TYR F 3 179 ? 29.639  37.809  54.843  1.000 35.345  ? 179 TYR CCC N   1 
ATOM   9478  C CA  . TYR F 3 179 ? 30.595  37.227  55.808  1.000 35.429  ? 179 TYR CCC CA  1 
ATOM   9479  C C   . TYR F 3 179 ? 31.935  37.002  55.084  1.000 33.713  ? 179 TYR CCC C   1 
ATOM   9480  O O   . TYR F 3 179 ? 31.979  36.981  53.853  1.000 31.891  ? 179 TYR CCC O   1 
ATOM   9481  C CB  . TYR F 3 179 ? 30.004  35.951  56.407  1.000 35.742  ? 179 TYR CCC CB  1 
ATOM   9482  C CG  . TYR F 3 179 ? 28.677  36.099  57.113  1.000 35.319  ? 179 TYR CCC CG  1 
ATOM   9483  C CD1 . TYR F 3 179 ? 28.614  36.323  58.473  1.000 36.261  ? 179 TYR CCC CD1 1 
ATOM   9484  C CD2 . TYR F 3 179 ? 27.484  35.894  56.445  1.000 35.839  ? 179 TYR CCC CD2 1 
ATOM   9485  C CE1 . TYR F 3 179 ? 27.404  36.397  59.141  1.000 39.609  ? 179 TYR CCC CE1 1 
ATOM   9486  C CE2 . TYR F 3 179 ? 26.266  35.982  57.096  1.000 36.667  ? 179 TYR CCC CE2 1 
ATOM   9487  C CZ  . TYR F 3 179 ? 26.216  36.226  58.453  1.000 37.649  ? 179 TYR CCC CZ  1 
ATOM   9488  O OH  . TYR F 3 179 ? 25.014  36.324  59.107  1.000 36.110  ? 179 TYR CCC OH  1 
ATOM   9489  N N   . SER F 3 180 ? 33.012  36.905  55.853  1.000 33.566  ? 180 SER CCC N   1 
ATOM   9490  C CA  . SER F 3 180 ? 34.332  36.391  55.430  1.000 35.258  ? 180 SER CCC CA  1 
ATOM   9491  C C   . SER F 3 180 ? 34.768  35.309  56.431  1.000 36.516  ? 180 SER CCC C   1 
ATOM   9492  O O   . SER F 3 180 ? 34.394  35.392  57.626  1.000 35.216  ? 180 SER CCC O   1 
ATOM   9493  C CB  . SER F 3 180 ? 35.350  37.501  55.290  1.000 37.535  ? 180 SER CCC CB  1 
ATOM   9494  O OG  . SER F 3 180 ? 35.155  38.238  54.088  1.000 41.634  ? 180 SER CCC OG  1 
ATOM   9495  N N   . LEU F 3 181 ? 35.504  34.309  55.946  1.000 34.960  ? 181 LEU CCC N   1 
ATOM   9496  C CA  . LEU F 3 181 ? 35.808  33.070  56.690  1.000 35.070  ? 181 LEU CCC CA  1 
ATOM   9497  C C   . LEU F 3 181 ? 37.267  32.706  56.443  1.000 35.588  ? 181 LEU CCC C   1 
ATOM   9498  O O   . LEU F 3 181 ? 37.716  32.821  55.291  1.000 33.723  ? 181 LEU CCC O   1 
ATOM   9499  C CB  . LEU F 3 181 ? 34.855  31.972  56.203  1.000 36.100  ? 181 LEU CCC CB  1 
ATOM   9500  C CG  . LEU F 3 181 ? 34.969  30.615  56.900  1.000 36.693  ? 181 LEU CCC CG  1 
ATOM   9501  C CD1 . LEU F 3 181 ? 33.641  29.889  56.909  1.000 36.926  ? 181 LEU CCC CD1 1 
ATOM   9502  C CD2 . LEU F 3 181 ? 36.028  29.748  56.244  1.000 37.676  ? 181 LEU CCC CD2 1 
ATOM   9503  N N   . SER F 3 182 ? 37.963  32.284  57.501  1.000 37.819  ? 182 SER CCC N   1 
ATOM   9504  C CA  . SER F 3 182 ? 39.345  31.753  57.461  1.000 40.888  ? 182 SER CCC CA  1 
ATOM   9505  C C   . SER F 3 182 ? 39.353  30.321  58.001  1.000 38.735  ? 182 SER CCC C   1 
ATOM   9506  O O   . SER F 3 182 ? 39.008  30.107  59.166  1.000 37.937  ? 182 SER CCC O   1 
ATOM   9507  C CB  . SER F 3 182 ? 40.291  32.641  58.223  1.000 45.514  ? 182 SER CCC CB  1 
ATOM   9508  O OG  . SER F 3 182 ? 40.242  32.367  59.618  1.000 50.039  ? 182 SER CCC OG  1 
ATOM   9509  N N   . SER F 3 183 ? 39.727  29.382  57.140  1.000 38.375  ? 183 SER CCC N   1 
ATOM   9510  C CA  . SER F 3 183 ? 40.121  27.999  57.494  1.000 39.573  ? 183 SER CCC CA  1 
ATOM   9511  C C   . SER F 3 183 ? 41.638  27.967  57.643  1.000 39.462  ? 183 SER CCC C   1 
ATOM   9512  O O   . SER F 3 183 ? 42.333  28.475  56.756  1.000 40.740  ? 183 SER CCC O   1 
ATOM   9513  C CB  . SER F 3 183 ? 39.653  27.030  56.458  1.000 41.039  ? 183 SER CCC CB  1 
ATOM   9514  O OG  . SER F 3 183 ? 39.603  25.710  56.977  1.000 42.097  ? 183 SER CCC OG  1 
ATOM   9515  N N   . THR F 3 184 ? 42.122  27.413  58.742  1.000 39.642  ? 184 THR CCC N   1 
ATOM   9516  C CA  . THR F 3 184 ? 43.559  27.417  59.104  1.000 39.089  ? 184 THR CCC CA  1 
ATOM   9517  C C   . THR F 3 184 ? 43.975  25.980  59.397  1.000 39.679  ? 184 THR CCC C   1 
ATOM   9518  O O   . THR F 3 184 ? 43.544  25.439  60.455  1.000 42.993  ? 184 THR CCC O   1 
ATOM   9519  C CB  . THR F 3 184 ? 43.818  28.283  60.340  1.000 39.288  ? 184 THR CCC CB  1 
ATOM   9520  O OG1 . THR F 3 184 ? 43.114  29.515  60.177  1.000 40.511  ? 184 THR CCC OG1 1 
ATOM   9521  C CG2 . THR F 3 184 ? 45.294  28.484  60.575  1.000 37.319  ? 184 THR CCC CG2 1 
ATOM   9522  N N   . LEU F 3 185 ? 44.731  25.383  58.482  1.000 37.481  ? 185 LEU CCC N   1 
ATOM   9523  C CA  . LEU F 3 185 ? 45.243  23.997  58.595  1.000 36.987  ? 185 LEU CCC CA  1 
ATOM   9524  C C   . LEU F 3 185 ? 46.590  24.054  59.315  1.000 38.478  ? 185 LEU CCC C   1 
ATOM   9525  O O   . LEU F 3 185 ? 47.468  24.774  58.858  1.000 35.618  ? 185 LEU CCC O   1 
ATOM   9526  C CB  . LEU F 3 185 ? 45.362  23.414  57.187  1.000 36.084  ? 185 LEU CCC CB  1 
ATOM   9527  C CG  . LEU F 3 185 ? 46.024  22.047  57.089  1.000 34.362  ? 185 LEU CCC CG  1 
ATOM   9528  C CD1 . LEU F 3 185 ? 45.053  20.964  57.485  1.000 34.351  ? 185 LEU CCC CD1 1 
ATOM   9529  C CD2 . LEU F 3 185 ? 46.525  21.805  55.680  1.000 36.181  ? 185 LEU CCC CD2 1 
ATOM   9530  N N   . THR F 3 186 ? 46.726  23.332  60.423  1.000 44.780  ? 186 THR CCC N   1 
ATOM   9531  C CA  . THR F 3 186 ? 47.907  23.371  61.330  1.000 49.145  ? 186 THR CCC CA  1 
ATOM   9532  C C   . THR F 3 186 ? 48.564  21.991  61.357  1.000 47.121  ? 186 THR CCC C   1 
ATOM   9533  O O   . THR F 3 186 ? 47.854  20.999  61.617  1.000 52.543  ? 186 THR CCC O   1 
ATOM   9534  C CB  . THR F 3 186 ? 47.478  23.820  62.733  1.000 52.189  ? 186 THR CCC CB  1 
ATOM   9535  O OG1 . THR F 3 186 ? 46.715  25.011  62.536  1.000 56.702  ? 186 THR CCC OG1 1 
ATOM   9536  C CG2 . THR F 3 186 ? 48.628  24.068  63.686  1.000 51.866  ? 186 THR CCC CG2 1 
ATOM   9537  N N   . LEU F 3 187 ? 49.862  21.926  61.071  1.000 46.669  ? 187 LEU CCC N   1 
ATOM   9538  C CA  . LEU F 3 187 ? 50.633  20.661  61.137  1.000 53.761  ? 187 LEU CCC CA  1 
ATOM   9539  C C   . LEU F 3 187 ? 52.111  20.965  61.404  1.000 53.739  ? 187 LEU CCC C   1 
ATOM   9540  O O   . LEU F 3 187 ? 52.519  22.093  61.142  1.000 55.094  ? 187 LEU CCC O   1 
ATOM   9541  C CB  . LEU F 3 187 ? 50.401  19.844  59.856  1.000 57.508  ? 187 LEU CCC CB  1 
ATOM   9542  C CG  . LEU F 3 187 ? 50.575  20.543  58.508  1.000 58.073  ? 187 LEU CCC CG  1 
ATOM   9543  C CD1 . LEU F 3 187 ? 50.978  19.555  57.437  1.000 64.798  ? 187 LEU CCC CD1 1 
ATOM   9544  C CD2 . LEU F 3 187 ? 49.291  21.187  58.056  1.000 58.032  ? 187 LEU CCC CD2 1 
ATOM   9545  N N   . SER F 3 188 ? 52.842  19.999  61.973  1.000 56.824  ? 188 SER CCC N   1 
ATOM   9546  C CA  . SER F 3 188 ? 54.293  20.060  62.310  1.000 56.787  ? 188 SER CCC CA  1 
ATOM   9547  C C   . SER F 3 188 ? 55.124  20.283  61.044  1.000 50.246  ? 188 SER CCC C   1 
ATOM   9548  O O   . SER F 3 188 ? 54.673  19.899  59.944  1.000 44.722  ? 188 SER CCC O   1 
ATOM   9549  C CB  . SER F 3 188 ? 54.755  18.803  63.017  1.000 63.238  ? 188 SER CCC CB  1 
ATOM   9550  O OG  . SER F 3 188 ? 54.550  17.654  62.197  1.000 73.666  ? 188 SER CCC OG  1 
ATOM   9551  N N   . LYS F 3 189 ? 56.309  20.868  61.206  1.000 50.950  ? 189 LYS CCC N   1 
ATOM   9552  C CA  . LYS F 3 189 ? 57.258  21.133  60.094  1.000 55.840  ? 189 LYS CCC CA  1 
ATOM   9553  C C   . LYS F 3 189 ? 57.512  19.821  59.358  1.000 55.158  ? 189 LYS CCC C   1 
ATOM   9554  O O   . LYS F 3 189 ? 57.474  19.828  58.106  1.000 55.138  ? 189 LYS CCC O   1 
ATOM   9555  C CB  . LYS F 3 189 ? 58.591  21.704  60.583  1.000 58.917  ? 189 LYS CCC CB  1 
ATOM   9556  C CG  . LYS F 3 189 ? 59.536  22.057  59.441  1.000 62.217  ? 189 LYS CCC CG  1 
ATOM   9557  C CD  . LYS F 3 189 ? 60.967  22.255  59.847  1.000 69.536  ? 189 LYS CCC CD  1 
ATOM   9558  C CE  . LYS F 3 189 ? 61.824  22.634  58.658  1.000 76.933  ? 189 LYS CCC CE  1 
ATOM   9559  N NZ  . LYS F 3 189 ? 63.266  22.655  58.988  1.000 85.604  ? 189 LYS CCC NZ  1 
ATOM   9560  N N   . ALA F 3 190 ? 57.776  18.762  60.130  1.000 54.042  ? 190 ALA CCC N   1 
ATOM   9561  C CA  . ALA F 3 190 ? 57.922  17.369  59.659  1.000 55.060  ? 190 ALA CCC CA  1 
ATOM   9562  C C   . ALA F 3 190 ? 56.804  17.033  58.666  1.000 56.860  ? 190 ALA CCC C   1 
ATOM   9563  O O   . ALA F 3 190 ? 57.113  16.827  57.469  1.000 65.482  ? 190 ALA CCC O   1 
ATOM   9564  C CB  . ALA F 3 190 ? 57.909  16.434  60.839  1.000 54.993  ? 190 ALA CCC CB  1 
ATOM   9565  N N   . ASP F 3 191 ? 55.552  17.009  59.129  1.000 56.768  ? 191 ASP CCC N   1 
ATOM   9566  C CA  . ASP F 3 191 ? 54.381  16.574  58.319  1.000 61.223  ? 191 ASP CCC CA  1 
ATOM   9567  C C   . ASP F 3 191 ? 54.172  17.537  57.150  1.000 59.579  ? 191 ASP CCC C   1 
ATOM   9568  O O   . ASP F 3 191 ? 53.644  17.068  56.129  1.000 58.946  ? 191 ASP CCC O   1 
ATOM   9569  C CB  . ASP F 3 191 ? 53.116  16.429  59.173  1.000 67.579  ? 191 ASP CCC CB  1 
ATOM   9570  C CG  . ASP F 3 191 ? 53.199  15.272  60.148  1.000 76.305  ? 191 ASP CCC CG  1 
ATOM   9571  O OD1 . ASP F 3 191 ? 54.087  14.418  59.956  1.000 85.594  ? 191 ASP CCC OD1 1 
ATOM   9572  O OD2 . ASP F 3 191 ? 52.384  15.239  61.082  1.000 82.221  ? 191 ASP CCC OD2 1 
ATOM   9573  N N   . TYR F 3 192 ? 54.578  18.810  57.275  1.000 56.863  ? 192 TYR CCC N   1 
ATOM   9574  C CA  . TYR F 3 192 ? 54.418  19.803  56.181  1.000 53.411  ? 192 TYR CCC CA  1 
ATOM   9575  C C   . TYR F 3 192 ? 55.288  19.368  54.994  1.000 55.611  ? 192 TYR CCC C   1 
ATOM   9576  O O   . TYR F 3 192 ? 54.815  19.471  53.826  1.000 54.471  ? 192 TYR CCC O   1 
ATOM   9577  C CB  . TYR F 3 192 ? 54.722  21.243  56.613  1.000 48.749  ? 192 TYR CCC CB  1 
ATOM   9578  C CG  . TYR F 3 192 ? 54.589  22.252  55.489  1.000 44.758  ? 192 TYR CCC CG  1 
ATOM   9579  C CD1 . TYR F 3 192 ? 53.364  22.497  54.879  1.000 42.481  ? 192 TYR CCC CD1 1 
ATOM   9580  C CD2 . TYR F 3 192 ? 55.697  22.933  54.994  1.000 40.587  ? 192 TYR CCC CD2 1 
ATOM   9581  C CE1 . TYR F 3 192 ? 53.250  23.378  53.813  1.000 40.950  ? 192 TYR CCC CE1 1 
ATOM   9582  C CE2 . TYR F 3 192 ? 55.596  23.835  53.946  1.000 38.523  ? 192 TYR CCC CE2 1 
ATOM   9583  C CZ  . TYR F 3 192 ? 54.366  24.058  53.351  1.000 39.046  ? 192 TYR CCC CZ  1 
ATOM   9584  O OH  . TYR F 3 192 ? 54.247  24.942  52.319  1.000 36.709  ? 192 TYR CCC OH  1 
ATOM   9585  N N   . GLU F 3 193 ? 56.499  18.875  55.277  1.000 56.167  ? 193 GLU CCC N   1 
ATOM   9586  C CA  . GLU F 3 193 ? 57.553  18.668  54.250  1.000 60.233  ? 193 GLU CCC CA  1 
ATOM   9587  C C   . GLU F 3 193 ? 57.425  17.273  53.626  1.000 62.509  ? 193 GLU CCC C   1 
ATOM   9588  O O   . GLU F 3 193 ? 58.185  17.000  52.698  1.000 68.853  ? 193 GLU CCC O   1 
ATOM   9589  C CB  . GLU F 3 193 ? 58.931  18.931  54.863  1.000 65.624  ? 193 GLU CCC CB  1 
ATOM   9590  C CG  . GLU F 3 193 ? 59.236  20.419  54.951  1.000 78.547  ? 193 GLU CCC CG  1 
ATOM   9591  C CD  . GLU F 3 193 ? 60.491  20.838  55.699  1.000 88.997  ? 193 GLU CCC CD  1 
ATOM   9592  O OE1 . GLU F 3 193 ? 61.159  19.967  56.276  1.000 94.489  ? 193 GLU CCC OE1 1 
ATOM   9593  O OE2 . GLU F 3 193 ? 60.794  22.054  55.699  1.000 105.907 ? 193 GLU CCC OE2 1 
ATOM   9594  N N   . LYS F 3 194 ? 56.479  16.444  54.088  1.000 65.790  ? 194 LYS CCC N   1 
ATOM   9595  C CA  . LYS F 3 194 ? 56.211  15.091  53.532  1.000 66.509  ? 194 LYS CCC CA  1 
ATOM   9596  C C   . LYS F 3 194 ? 55.370  15.195  52.267  1.000 66.187  ? 194 LYS CCC C   1 
ATOM   9597  O O   . LYS F 3 194 ? 55.346  14.223  51.522  1.000 81.471  ? 194 LYS CCC O   1 
ATOM   9598  C CB  . LYS F 3 194 ? 55.440  14.212  54.517  1.000 71.835  ? 194 LYS CCC CB  1 
ATOM   9599  C CG  . LYS F 3 194 ? 56.073  14.123  55.892  1.000 79.689  ? 194 LYS CCC CG  1 
ATOM   9600  C CD  . LYS F 3 194 ? 55.510  13.059  56.785  1.000 79.824  ? 194 LYS CCC CD  1 
ATOM   9601  C CE  . LYS F 3 194 ? 56.039  11.706  56.362  1.000 84.750  ? 194 LYS CCC CE  1 
ATOM   9602  N NZ  . LYS F 3 194 ? 56.380  10.857  57.527  1.000 95.683  ? 194 LYS CCC NZ  1 
ATOM   9603  N N   . HIS F 3 195 ? 54.682  16.310  52.051  1.000 64.265  ? 195 HIS CCC N   1 
ATOM   9604  C CA  . HIS F 3 195 ? 53.687  16.449  50.961  1.000 60.548  ? 195 HIS CCC CA  1 
ATOM   9605  C C   . HIS F 3 195 ? 54.077  17.604  50.037  1.000 55.143  ? 195 HIS CCC C   1 
ATOM   9606  O O   . HIS F 3 195 ? 54.984  18.383  50.390  1.000 54.553  ? 195 HIS CCC O   1 
ATOM   9607  C CB  . HIS F 3 195 ? 52.297  16.605  51.567  1.000 62.401  ? 195 HIS CCC CB  1 
ATOM   9608  C CG  . HIS F 3 195 ? 51.979  15.571  52.593  1.000 69.859  ? 195 HIS CCC CG  1 
ATOM   9609  N ND1 . HIS F 3 195 ? 51.707  15.896  53.915  1.000 76.008  ? 195 HIS CCC ND1 1 
ATOM   9610  C CD2 . HIS F 3 195 ? 51.847  14.232  52.496  1.000 70.861  ? 195 HIS CCC CD2 1 
ATOM   9611  C CE1 . HIS F 3 195 ? 51.423  14.806  54.589  1.000 77.605  ? 195 HIS CCC CE1 1 
ATOM   9612  N NE2 . HIS F 3 195 ? 51.515  13.771  53.743  1.000 80.070  ? 195 HIS CCC NE2 1 
ATOM   9613  N N   . LYS F 3 196 ? 53.405  17.687  48.891  1.000 52.467  ? 196 LYS CCC N   1 
ATOM   9614  C CA  . LYS F 3 196 ? 53.734  18.628  47.790  1.000 52.329  ? 196 LYS CCC CA  1 
ATOM   9615  C C   . LYS F 3 196 ? 52.559  19.586  47.586  1.000 45.605  ? 196 LYS CCC C   1 
ATOM   9616  O O   . LYS F 3 196 ? 52.770  20.795  47.764  1.000 45.260  ? 196 LYS CCC O   1 
ATOM   9617  C CB  . LYS F 3 196 ? 54.072  17.837  46.518  1.000 58.105  ? 196 LYS CCC CB  1 
ATOM   9618  C CG  . LYS F 3 196 ? 54.513  18.647  45.301  1.000 64.632  ? 196 LYS CCC CG  1 
ATOM   9619  C CD  . LYS F 3 196 ? 55.599  19.697  45.556  1.000 73.959  ? 196 LYS CCC CD  1 
ATOM   9620  C CE  . LYS F 3 196 ? 56.783  19.241  46.394  1.000 76.487  ? 196 LYS CCC CE  1 
ATOM   9621  N NZ  . LYS F 3 196 ? 57.677  18.314  45.663  1.000 79.919  ? 196 LYS CCC NZ  1 
ATOM   9622  N N   . VAL F 3 197 ? 51.380  19.054  47.266  1.000 40.849  ? 197 VAL CCC N   1 
ATOM   9623  C CA  . VAL F 3 197 ? 50.167  19.846  46.907  1.000 40.557  ? 197 VAL CCC CA  1 
ATOM   9624  C C   . VAL F 3 197 ? 49.303  20.064  48.150  1.000 38.693  ? 197 VAL CCC C   1 
ATOM   9625  O O   . VAL F 3 197 ? 48.681  19.102  48.617  1.000 45.262  ? 197 VAL CCC O   1 
ATOM   9626  C CB  . VAL F 3 197 ? 49.338  19.156  45.812  1.000 39.663  ? 197 VAL CCC CB  1 
ATOM   9627  C CG1 . VAL F 3 197 ? 48.051  19.916  45.504  1.000 38.724  ? 197 VAL CCC CG1 1 
ATOM   9628  C CG2 . VAL F 3 197 ? 50.168  18.949  44.566  1.000 40.848  ? 197 VAL CCC CG2 1 
ATOM   9629  N N   . TYR F 3 198 ? 49.214  21.311  48.598  1.000 33.349  ? 198 TYR CCC N   1 
ATOM   9630  C CA  . TYR F 3 198 ? 48.232  21.785  49.589  1.000 31.520  ? 198 TYR CCC CA  1 
ATOM   9631  C C   . TYR F 3 198 ? 47.121  22.499  48.832  1.000 33.001  ? 198 TYR CCC C   1 
ATOM   9632  O O   . TYR F 3 198 ? 47.440  23.421  48.099  1.000 34.129  ? 198 TYR CCC O   1 
ATOM   9633  C CB  . TYR F 3 198 ? 48.955  22.676  50.591  1.000 30.010  ? 198 TYR CCC CB  1 
ATOM   9634  C CG  . TYR F 3 198 ? 49.865  21.878  51.477  1.000 28.900  ? 198 TYR CCC CG  1 
ATOM   9635  C CD1 . TYR F 3 198 ? 49.435  21.399  52.709  1.000 29.356  ? 198 TYR CCC CD1 1 
ATOM   9636  C CD2 . TYR F 3 198 ? 51.133  21.553  51.049  1.000 28.888  ? 198 TYR CCC CD2 1 
ATOM   9637  C CE1 . TYR F 3 198 ? 50.256  20.633  53.519  1.000 28.797  ? 198 TYR CCC CE1 1 
ATOM   9638  C CE2 . TYR F 3 198 ? 51.969  20.783  51.838  1.000 31.171  ? 198 TYR CCC CE2 1 
ATOM   9639  C CZ  . TYR F 3 198 ? 51.531  20.332  53.075  1.000 31.502  ? 198 TYR CCC CZ  1 
ATOM   9640  O OH  . TYR F 3 198 ? 52.384  19.585  53.829  1.000 35.553  ? 198 TYR CCC OH  1 
ATOM   9641  N N   . ALA F 3 199 ? 45.875  22.070  49.003  1.000 37.039  ? 199 ALA CCC N   1 
ATOM   9642  C CA  . ALA F 3 199 ? 44.710  22.605  48.274  1.000 40.947  ? 199 ALA CCC CA  1 
ATOM   9643  C C   . ALA F 3 199 ? 43.553  22.880  49.234  1.000 44.069  ? 199 ALA CCC C   1 
ATOM   9644  O O   . ALA F 3 199 ? 43.401  22.229  50.286  1.000 46.445  ? 199 ALA CCC O   1 
ATOM   9645  C CB  . ALA F 3 199 ? 44.282  21.659  47.187  1.000 44.746  ? 199 ALA CCC CB  1 
ATOM   9646  N N   . CYS F 3 200 ? 42.726  23.810  48.814  1.000 45.590  ? 200 CYS CCC N   1 
ATOM   9647  C CA  . CYS F 3 200 ? 41.587  24.315  49.581  1.000 47.358  ? 200 CYS CCC CA  1 
ATOM   9648  C C   . CYS F 3 200 ? 40.393  24.275  48.631  1.000 46.840  ? 200 CYS CCC C   1 
ATOM   9649  O O   . CYS F 3 200 ? 40.403  25.053  47.671  1.000 44.649  ? 200 CYS CCC O   1 
ATOM   9650  C CB  . CYS F 3 200 ? 41.907  25.714  50.082  1.000 49.848  ? 200 CYS CCC CB  1 
ATOM   9651  S SG  . CYS F 3 200 ? 40.521  26.381  51.024  1.000 64.565  ? 200 CYS CCC SG  1 
ATOM   9652  N N   . GLU F 3 201 ? 39.453  23.359  48.858  1.000 48.055  ? 201 GLU CCC N   1 
ATOM   9653  C CA  . GLU F 3 201 ? 38.282  23.150  47.970  1.000 48.976  ? 201 GLU CCC CA  1 
ATOM   9654  C C   . GLU F 3 201 ? 37.035  23.720  48.652  1.000 45.279  ? 201 GLU CCC C   1 
ATOM   9655  O O   . GLU F 3 201 ? 36.615  23.178  49.702  1.000 44.444  ? 201 GLU CCC O   1 
ATOM   9656  C CB  . GLU F 3 201 ? 38.108  21.664  47.646  1.000 56.618  ? 201 GLU CCC CB  1 
ATOM   9657  C CG  . GLU F 3 201 ? 36.929  21.388  46.732  1.000 64.045  ? 201 GLU CCC CG  1 
ATOM   9658  C CD  . GLU F 3 201 ? 36.373  19.980  46.789  1.000 69.503  ? 201 GLU CCC CD  1 
ATOM   9659  O OE1 . GLU F 3 201 ? 36.359  19.339  45.720  1.000 83.255  ? 201 GLU CCC OE1 1 
ATOM   9660  O OE2 . GLU F 3 201 ? 35.935  19.542  47.890  1.000 63.770  ? 201 GLU CCC OE2 1 
ATOM   9661  N N   . VAL F 3 202 ? 36.462  24.762  48.055  1.000 41.559  ? 202 VAL CCC N   1 
ATOM   9662  C CA  . VAL F 3 202 ? 35.327  25.537  48.631  1.000 40.021  ? 202 VAL CCC CA  1 
ATOM   9663  C C   . VAL F 3 202 ? 34.053  25.213  47.858  1.000 42.171  ? 202 VAL CCC C   1 
ATOM   9664  O O   . VAL F 3 202 ? 34.026  25.436  46.637  1.000 43.773  ? 202 VAL CCC O   1 
ATOM   9665  C CB  . VAL F 3 202 ? 35.602  27.046  48.586  1.000 38.281  ? 202 VAL CCC CB  1 
ATOM   9666  C CG1 . VAL F 3 202 ? 34.378  27.849  49.006  1.000 37.422  ? 202 VAL CCC CG1 1 
ATOM   9667  C CG2 . VAL F 3 202 ? 36.819  27.414  49.419  1.000 38.535  ? 202 VAL CCC CG2 1 
ATOM   9668  N N   . THR F 3 203 ? 33.026  24.747  48.564  1.000 45.132  ? 203 THR CCC N   1 
ATOM   9669  C CA  . THR F 3 203 ? 31.652  24.566  48.033  1.000 45.160  ? 203 THR CCC CA  1 
ATOM   9670  C C   . THR F 3 203 ? 30.737  25.590  48.687  1.000 43.205  ? 203 THR CCC C   1 
ATOM   9671  O O   . THR F 3 203 ? 30.709  25.656  49.927  1.000 39.106  ? 203 THR CCC O   1 
ATOM   9672  C CB  . THR F 3 203 ? 31.119  23.156  48.286  1.000 47.342  ? 203 THR CCC CB  1 
ATOM   9673  O OG1 . THR F 3 203 ? 32.247  22.291  48.173  1.000 53.748  ? 203 THR CCC OG1 1 
ATOM   9674  C CG2 . THR F 3 203 ? 30.023  22.779  47.314  1.000 48.086  ? 203 THR CCC CG2 1 
ATOM   9675  N N   . HIS F 3 204 ? 30.024  26.355  47.868  1.000 43.834  ? 204 HIS CCC N   1 
ATOM   9676  C CA  . HIS F 3 204 ? 29.100  27.421  48.324  1.000 42.529  ? 204 HIS CCC CA  1 
ATOM   9677  C C   . HIS F 3 204 ? 27.894  27.463  47.401  1.000 43.879  ? 204 HIS CCC C   1 
ATOM   9678  O O   . HIS F 3 204 ? 28.038  27.089  46.224  1.000 43.373  ? 204 HIS CCC O   1 
ATOM   9679  C CB  . HIS F 3 204 ? 29.810  28.772  48.358  1.000 41.465  ? 204 HIS CCC CB  1 
ATOM   9680  C CG  . HIS F 3 204 ? 28.965  29.838  48.951  1.000 39.641  ? 204 HIS CCC CG  1 
ATOM   9681  N ND1 . HIS F 3 204 ? 28.405  30.838  48.199  1.000 37.609  ? 204 HIS CCC ND1 1 
ATOM   9682  C CD2 . HIS F 3 204 ? 28.557  30.030  50.218  1.000 40.489  ? 204 HIS CCC CD2 1 
ATOM   9683  C CE1 . HIS F 3 204 ? 27.693  31.617  48.975  1.000 36.999  ? 204 HIS CCC CE1 1 
ATOM   9684  N NE2 . HIS F 3 204 ? 27.779  31.146  50.223  1.000 39.706  ? 204 HIS CCC NE2 1 
ATOM   9685  N N   . GLN F 3 205 ? 26.770  27.935  47.921  1.000 46.002  ? 205 GLN CCC N   1 
ATOM   9686  C CA  . GLN F 3 205 ? 25.497  28.013  47.173  1.000 48.927  ? 205 GLN CCC CA  1 
ATOM   9687  C C   . GLN F 3 205 ? 25.675  28.857  45.898  1.000 44.885  ? 205 GLN CCC C   1 
ATOM   9688  O O   . GLN F 3 205 ? 24.959  28.620  44.936  1.000 50.243  ? 205 GLN CCC O   1 
ATOM   9689  C CB  . GLN F 3 205 ? 24.416  28.551  48.107  1.000 53.359  ? 205 GLN CCC CB  1 
ATOM   9690  C CG  . GLN F 3 205 ? 23.069  28.739  47.430  1.000 58.115  ? 205 GLN CCC CG  1 
ATOM   9691  C CD  . GLN F 3 205 ? 22.075  29.311  48.403  1.000 63.547  ? 205 GLN CCC CD  1 
ATOM   9692  O OE1 . GLN F 3 205 ? 22.159  29.055  49.602  1.000 71.886  ? 205 GLN CCC OE1 1 
ATOM   9693  N NE2 . GLN F 3 205 ? 21.131  30.090  47.892  1.000 62.055  ? 205 GLN CCC NE2 1 
ATOM   9694  N N   . GLY F 3 206 ? 26.589  29.819  45.878  1.000 44.281  ? 206 GLY CCC N   1 
ATOM   9695  C CA  . GLY F 3 206 ? 26.757  30.735  44.734  1.000 43.364  ? 206 GLY CCC CA  1 
ATOM   9696  C C   . GLY F 3 206 ? 27.811  30.252  43.764  1.000 44.459  ? 206 GLY CCC C   1 
ATOM   9697  O O   . GLY F 3 206 ? 28.153  31.018  42.859  1.000 44.762  ? 206 GLY CCC O   1 
ATOM   9698  N N   . LEU F 3 207 ? 28.345  29.048  43.962  1.000 50.236  ? 207 LEU CCC N   1 
ATOM   9699  C CA  . LEU F 3 207 ? 29.359  28.432  43.069  1.000 56.977  ? 207 LEU CCC CA  1 
ATOM   9700  C C   . LEU F 3 207 ? 28.714  27.226  42.388  1.000 67.276  ? 207 LEU CCC C   1 
ATOM   9701  O O   . LEU F 3 207 ? 28.428  26.244  43.114  1.000 85.699  ? 207 LEU CCC O   1 
ATOM   9702  C CB  . LEU F 3 207 ? 30.569  27.993  43.901  1.000 57.952  ? 207 LEU CCC CB  1 
ATOM   9703  C CG  . LEU F 3 207 ? 31.438  29.115  44.478  1.000 54.654  ? 207 LEU CCC CG  1 
ATOM   9704  C CD1 . LEU F 3 207 ? 32.524  28.550  45.379  1.000 53.159  ? 207 LEU CCC CD1 1 
ATOM   9705  C CD2 . LEU F 3 207 ? 32.069  29.956  43.380  1.000 54.489  ? 207 LEU CCC CD2 1 
ATOM   9706  N N   . SER F 3 208 ? 28.506  27.290  41.068  1.000 70.718  ? 208 SER CCC N   1 
ATOM   9707  C CA  . SER F 3 208 ? 27.933  26.192  40.235  1.000 75.250  ? 208 SER CCC CA  1 
ATOM   9708  C C   . SER F 3 208 ? 28.737  24.899  40.437  1.000 71.601  ? 208 SER CCC C   1 
ATOM   9709  O O   . SER F 3 208 ? 28.143  23.802  40.444  1.000 80.903  ? 208 SER CCC O   1 
ATOM   9710  C CB  . SER F 3 208 ? 27.899  26.581  38.779  1.000 78.241  ? 208 SER CCC CB  1 
ATOM   9711  O OG  . SER F 3 208 ? 29.216  26.718  38.267  1.000 80.026  ? 208 SER CCC OG  1 
ATOM   9712  N N   . SER F 3 209 ? 30.048  25.043  40.603  1.000 65.862  ? 209 SER CCC N   1 
ATOM   9713  C CA  . SER F 3 209 ? 31.014  23.945  40.825  1.000 63.257  ? 209 SER CCC CA  1 
ATOM   9714  C C   . SER F 3 209 ? 31.990  24.350  41.934  1.000 57.887  ? 209 SER CCC C   1 
ATOM   9715  O O   . SER F 3 209 ? 32.393  25.509  42.019  1.000 60.666  ? 209 SER CCC O   1 
ATOM   9716  C CB  . SER F 3 209 ? 31.685  23.650  39.518  1.000 66.899  ? 209 SER CCC CB  1 
ATOM   9717  O OG  . SER F 3 209 ? 32.951  23.051  39.723  1.000 82.374  ? 209 SER CCC OG  1 
ATOM   9718  N N   . PRO F 3 210 ? 32.389  23.431  42.840  1.000 50.323  ? 210 PRO CCC N   1 
ATOM   9719  C CA  . PRO F 3 210 ? 33.419  23.710  43.839  1.000 49.375  ? 210 PRO CCC CA  1 
ATOM   9720  C C   . PRO F 3 210 ? 34.721  24.303  43.280  1.000 46.038  ? 210 PRO CCC C   1 
ATOM   9721  O O   . PRO F 3 210 ? 35.305  23.721  42.404  1.000 43.374  ? 210 PRO CCC O   1 
ATOM   9722  C CB  . PRO F 3 210 ? 33.724  22.336  44.444  1.000 48.852  ? 210 PRO CCC CB  1 
ATOM   9723  C CG  . PRO F 3 210 ? 32.414  21.604  44.303  1.000 53.316  ? 210 PRO CCC CG  1 
ATOM   9724  C CD  . PRO F 3 210 ? 31.835  22.083  42.988  1.000 53.459  ? 210 PRO CCC CD  1 
ATOM   9725  N N   . VAL F 3 211 ? 35.144  25.447  43.821  1.000 45.683  ? 211 VAL CCC N   1 
ATOM   9726  C CA  . VAL F 3 211 ? 36.428  26.123  43.469  1.000 47.572  ? 211 VAL CCC CA  1 
ATOM   9727  C C   . VAL F 3 211 ? 37.543  25.614  44.389  1.000 48.538  ? 211 VAL CCC C   1 
ATOM   9728  O O   . VAL F 3 211 ? 37.338  25.575  45.624  1.000 46.297  ? 211 VAL CCC O   1 
ATOM   9729  C CB  . VAL F 3 211 ? 36.340  27.657  43.558  1.000 47.384  ? 211 VAL CCC CB  1 
ATOM   9730  C CG1 . VAL F 3 211 ? 37.684  28.269  43.228  1.000 47.020  ? 211 VAL CCC CG1 1 
ATOM   9731  C CG2 . VAL F 3 211 ? 35.258  28.241  42.662  1.000 48.566  ? 211 VAL CCC CG2 1 
ATOM   9732  N N   . THR F 3 212 ? 38.695  25.288  43.797  1.000 49.616  ? 212 THR CCC N   1 
ATOM   9733  C CA  . THR F 3 212 ? 39.927  24.851  44.497  1.000 50.082  ? 212 THR CCC CA  1 
ATOM   9734  C C   . THR F 3 212 ? 41.037  25.861  44.208  1.000 45.253  ? 212 THR CCC C   1 
ATOM   9735  O O   . THR F 3 212 ? 41.253  26.180  43.043  1.000 46.665  ? 212 THR CCC O   1 
ATOM   9736  C CB  . THR F 3 212 ? 40.363  23.450  44.048  1.000 56.103  ? 212 THR CCC CB  1 
ATOM   9737  O OG1 . THR F 3 212 ? 39.245  22.567  44.147  1.000 60.266  ? 212 THR CCC OG1 1 
ATOM   9738  C CG2 . THR F 3 212 ? 41.511  22.896  44.866  1.000 58.933  ? 212 THR CCC CG2 1 
ATOM   9739  N N   . LYS F 3 213 ? 41.703  26.354  45.246  1.000 41.001  ? 213 LYS CCC N   1 
ATOM   9740  C CA  . LYS F 3 213 ? 42.980  27.090  45.116  1.000 39.337  ? 213 LYS CCC CA  1 
ATOM   9741  C C   . LYS F 3 213 ? 44.016  26.244  45.826  1.000 37.303  ? 213 LYS CCC C   1 
ATOM   9742  O O   . LYS F 3 213 ? 43.691  25.739  46.898  1.000 36.999  ? 213 LYS CCC O   1 
ATOM   9743  C CB  . LYS F 3 213 ? 42.886  28.477  45.746  1.000 42.696  ? 213 LYS CCC CB  1 
ATOM   9744  C CG  . LYS F 3 213 ? 41.611  29.247  45.432  1.000 47.954  ? 213 LYS CCC CG  1 
ATOM   9745  C CD  . LYS F 3 213 ? 41.486  29.654  43.980  1.000 51.796  ? 213 LYS CCC CD  1 
ATOM   9746  C CE  . LYS F 3 213 ? 42.308  30.874  43.636  1.000 55.809  ? 213 LYS CCC CE  1 
ATOM   9747  N NZ  . LYS F 3 213 ? 41.762  31.540  42.434  1.000 59.023  ? 213 LYS CCC NZ  1 
ATOM   9748  N N   . SER F 3 214 ? 45.188  26.074  45.238  1.000 37.875  ? 214 SER CCC N   1 
ATOM   9749  C CA  . SER F 3 214 ? 46.244  25.217  45.824  1.000 41.001  ? 214 SER CCC CA  1 
ATOM   9750  C C   . SER F 3 214 ? 47.624  25.812  45.552  1.000 38.141  ? 214 SER CCC C   1 
ATOM   9751  O O   . SER F 3 214 ? 47.706  26.796  44.824  1.000 38.725  ? 214 SER CCC O   1 
ATOM   9752  C CB  . SER F 3 214 ? 46.124  23.824  45.280  1.000 45.446  ? 214 SER CCC CB  1 
ATOM   9753  O OG  . SER F 3 214 ? 46.663  23.751  43.967  1.000 50.985  ? 214 SER CCC OG  1 
ATOM   9754  N N   . PHE F 3 215 ? 48.658  25.210  46.118  1.000 37.515  ? 215 PHE CCC N   1 
ATOM   9755  C CA  . PHE F 3 215 ? 50.067  25.572  45.857  1.000 41.175  ? 215 PHE CCC CA  1 
ATOM   9756  C C   . PHE F 3 215 ? 50.944  24.346  46.116  1.000 43.258  ? 215 PHE CCC C   1 
ATOM   9757  O O   . PHE F 3 215 ? 50.557  23.480  46.936  1.000 41.149  ? 215 PHE CCC O   1 
ATOM   9758  C CB  . PHE F 3 215 ? 50.490  26.746  46.741  1.000 40.493  ? 215 PHE CCC CB  1 
ATOM   9759  C CG  . PHE F 3 215 ? 50.595  26.391  48.196  1.000 38.577  ? 215 PHE CCC CG  1 
ATOM   9760  C CD1 . PHE F 3 215 ? 49.490  26.496  49.017  1.000 38.326  ? 215 PHE CCC CD1 1 
ATOM   9761  C CD2 . PHE F 3 215 ? 51.780  25.902  48.725  1.000 39.090  ? 215 PHE CCC CD2 1 
ATOM   9762  C CE1 . PHE F 3 215 ? 49.572  26.152  50.354  1.000 39.079  ? 215 PHE CCC CE1 1 
ATOM   9763  C CE2 . PHE F 3 215 ? 51.857  25.551  50.064  1.000 39.884  ? 215 PHE CCC CE2 1 
ATOM   9764  C CZ  . PHE F 3 215 ? 50.756  25.685  50.877  1.000 40.968  ? 215 PHE CCC CZ  1 
ATOM   9765  N N   . ASN F 3 216 ? 52.081  24.288  45.426  1.000 43.167  ? 216 ASN CCC N   1 
ATOM   9766  C CA  . ASN F 3 216 ? 53.064  23.183  45.523  1.000 43.441  ? 216 ASN CCC CA  1 
ATOM   9767  C C   . ASN F 3 216 ? 54.179  23.683  46.440  1.000 40.065  ? 216 ASN CCC C   1 
ATOM   9768  O O   . ASN F 3 216 ? 54.654  24.794  46.207  1.000 37.907  ? 216 ASN CCC O   1 
ATOM   9769  C CB  . ASN F 3 216 ? 53.532  22.741  44.132  1.000 45.906  ? 216 ASN CCC CB  1 
ATOM   9770  C CG  . ASN F 3 216 ? 52.438  22.075  43.319  1.000 46.464  ? 216 ASN CCC CG  1 
ATOM   9771  O OD1 . ASN F 3 216 ? 51.248  22.300  43.529  1.000 43.509  ? 216 ASN CCC OD1 1 
ATOM   9772  N ND2 . ASN F 3 216 ? 52.837  21.246  42.371  1.000 55.850  ? 216 ASN CCC ND2 1 
ATOM   9773  N N   . ARG F 3 217 ? 54.554  22.903  47.449  1.000 40.239  ? 217 ARG CCC N   1 
ATOM   9774  C CA  . ARG F 3 217 ? 55.532  23.338  48.474  1.000 45.379  ? 217 ARG CCC CA  1 
ATOM   9775  C C   . ARG F 3 217 ? 56.841  23.765  47.802  1.000 51.434  ? 217 ARG CCC C   1 
ATOM   9776  O O   . ARG F 3 217 ? 57.348  23.005  46.994  1.000 46.022  ? 217 ARG CCC O   1 
ATOM   9777  C CB  . ARG F 3 217 ? 55.769  22.228  49.488  1.000 43.297  ? 217 ARG CCC CB  1 
ATOM   9778  C CG  . ARG F 3 217 ? 56.659  22.652  50.640  1.000 46.220  ? 217 ARG CCC CG  1 
ATOM   9779  C CD  . ARG F 3 217 ? 56.634  21.564  51.699  1.000 51.229  ? 217 ARG CCC CD  1 
ATOM   9780  N NE  . ARG F 3 217 ? 56.867  20.272  51.073  1.000 53.999  ? 217 ARG CCC NE  1 
ATOM   9781  C CZ  . ARG F 3 217 ? 58.065  19.837  50.682  1.000 54.351  ? 217 ARG CCC CZ  1 
ATOM   9782  N NH1 . ARG F 3 217 ? 59.149  20.565  50.887  1.000 53.555  ? 217 ARG CCC NH1 1 
ATOM   9783  N NH2 . ARG F 3 217 ? 58.187  18.669  50.086  1.000 58.504  ? 217 ARG CCC NH2 1 
ATOM   9784  N N   . GLY F 3 218 ? 57.334  24.965  48.132  1.000 67.051  ? 218 GLY CCC N   1 
ATOM   9785  C CA  . GLY F 3 218 ? 58.575  25.572  47.601  1.000 73.004  ? 218 GLY CCC CA  1 
ATOM   9786  C C   . GLY F 3 218 ? 58.420  26.111  46.183  1.000 81.748  ? 218 GLY CCC C   1 
ATOM   9787  O O   . GLY F 3 218 ? 59.080  25.544  45.291  1.000 70.195  ? 218 GLY CCC O   1 
ATOM   9788  N N   . GLU F 3 219 ? 57.590  27.157  45.994  1.000 93.049  ? 219 GLU CCC N   1 
ATOM   9789  C CA  . GLU F 3 219 ? 57.369  27.910  44.722  1.000 89.931  ? 219 GLU CCC CA  1 
ATOM   9790  C C   . GLU F 3 219 ? 56.686  29.249  45.053  1.000 88.918  ? 219 GLU CCC C   1 
ATOM   9791  O O   . GLU F 3 219 ? 55.852  29.816  44.328  1.000 81.782  ? 219 GLU CCC O   1 
ATOM   9792  C CB  . GLU F 3 219 ? 56.533  27.090  43.730  1.000 92.114  ? 219 GLU CCC CB  1 
ATOM   9793  C CG  . GLU F 3 219 ? 57.151  25.746  43.359  1.000 94.229  ? 219 GLU CCC CG  1 
ATOM   9794  C CD  . GLU F 3 219 ? 56.341  24.847  42.435  1.000 97.720  ? 219 GLU CCC CD  1 
ATOM   9795  O OE1 . GLU F 3 219 ? 55.449  25.365  41.739  1.000 111.421 ? 219 GLU CCC OE1 1 
ATOM   9796  O OE2 . GLU F 3 219 ? 56.608  23.626  42.420  1.000 85.821  ? 219 GLU CCC OE2 1 
ATOM   9797  N N   . THR G 1 15  ? 34.597  112.068 13.462  1.000 149.995 ? 333 THR DDD N   1 
ATOM   9798  C CA  . THR G 1 15  ? 34.875  112.789 12.176  1.000 151.732 ? 333 THR DDD CA  1 
ATOM   9799  C C   . THR G 1 15  ? 36.307  112.502 11.707  1.000 166.409 ? 333 THR DDD C   1 
ATOM   9800  O O   . THR G 1 15  ? 36.453  112.164 10.513  1.000 193.044 ? 333 THR DDD O   1 
ATOM   9801  C CB  . THR G 1 15  ? 34.640  114.304 12.294  1.000 141.241 ? 333 THR DDD CB  1 
ATOM   9802  O OG1 . THR G 1 15  ? 33.260  114.537 12.569  1.000 135.725 ? 333 THR DDD OG1 1 
ATOM   9803  C CG2 . THR G 1 15  ? 35.001  115.077 11.043  1.000 133.110 ? 333 THR DDD CG2 1 
ATOM   9804  N N   . ASN G 1 16  ? 37.307  112.611 12.596  1.000 155.143 ? 334 ASN DDD N   1 
ATOM   9805  C CA  . ASN G 1 16  ? 38.739  112.801 12.216  1.000 130.653 ? 334 ASN DDD CA  1 
ATOM   9806  C C   . ASN G 1 16  ? 39.555  111.491 12.303  1.000 120.321 ? 334 ASN DDD C   1 
ATOM   9807  O O   . ASN G 1 16  ? 40.669  111.539 12.855  1.000 111.269 ? 334 ASN DDD O   1 
ATOM   9808  C CB  . ASN G 1 16  ? 39.373  113.971 12.989  1.000 110.009 ? 334 ASN DDD CB  1 
ATOM   9809  C CG  . ASN G 1 16  ? 39.553  113.739 14.477  1.000 97.692  ? 334 ASN DDD CG  1 
ATOM   9810  O OD1 . ASN G 1 16  ? 38.930  112.871 15.079  1.000 86.569  ? 334 ASN DDD OD1 1 
ATOM   9811  N ND2 . ASN G 1 16  ? 40.415  114.523 15.090  1.000 87.155  ? 334 ASN DDD ND2 1 
ATOM   9812  N N   . LEU G 1 17  ? 39.066  110.386 11.712  1.000 110.259 ? 335 LEU DDD N   1 
ATOM   9813  C CA  . LEU G 1 17  ? 39.898  109.218 11.290  1.000 111.634 ? 335 LEU DDD CA  1 
ATOM   9814  C C   . LEU G 1 17  ? 40.870  109.693 10.195  1.000 111.895 ? 335 LEU DDD C   1 
ATOM   9815  O O   . LEU G 1 17  ? 40.440  110.477 9.344   1.000 115.821 ? 335 LEU DDD O   1 
ATOM   9816  C CB  . LEU G 1 17  ? 39.000  108.075 10.783  1.000 105.872 ? 335 LEU DDD CB  1 
ATOM   9817  C CG  . LEU G 1 17  ? 39.723  106.834 10.234  1.000 107.440 ? 335 LEU DDD CG  1 
ATOM   9818  C CD1 . LEU G 1 17  ? 40.217  105.908 11.347  1.000 105.794 ? 335 LEU DDD CD1 1 
ATOM   9819  C CD2 . LEU G 1 17  ? 38.841  106.070 9.251   1.000 103.735 ? 335 LEU DDD CD2 1 
ATOM   9820  N N   . CYS G 1 18  ? 42.133  109.248 10.211  1.000 113.230 ? 336 CYS DDD N   1 
ATOM   9821  C CA  . CYS G 1 18  ? 43.169  109.646 9.215   1.000 101.657 ? 336 CYS DDD CA  1 
ATOM   9822  C C   . CYS G 1 18  ? 42.826  109.091 7.838   1.000 97.632  ? 336 CYS DDD C   1 
ATOM   9823  O O   . CYS G 1 18  ? 42.518  107.913 7.695   1.000 97.280  ? 336 CYS DDD O   1 
ATOM   9824  C CB  . CYS G 1 18  ? 44.558  109.175 9.617   1.000 102.915 ? 336 CYS DDD CB  1 
ATOM   9825  S SG  . CYS G 1 18  ? 45.281  110.159 10.956  1.000 122.724 ? 336 CYS DDD SG  1 
ATOM   9826  N N   . PRO G 1 19  ? 42.922  109.911 6.771   1.000 97.819  ? 337 PRO DDD N   1 
ATOM   9827  C CA  . PRO G 1 19  ? 42.324  109.567 5.484   1.000 103.040 ? 337 PRO DDD CA  1 
ATOM   9828  C C   . PRO G 1 19  ? 43.202  108.620 4.653   1.000 107.554 ? 337 PRO DDD C   1 
ATOM   9829  O O   . PRO G 1 19  ? 43.454  108.927 3.508   1.000 117.226 ? 337 PRO DDD O   1 
ATOM   9830  C CB  . PRO G 1 19  ? 42.210  110.960 4.843   1.000 96.388  ? 337 PRO DDD CB  1 
ATOM   9831  C CG  . PRO G 1 19  ? 43.469  111.662 5.291   1.000 86.936  ? 337 PRO DDD CG  1 
ATOM   9832  C CD  . PRO G 1 19  ? 43.655  111.185 6.715   1.000 88.543  ? 337 PRO DDD CD  1 
ATOM   9833  N N   . PHE G 1 20  ? 43.655  107.509 5.243   1.000 94.465  ? 338 PHE DDD N   1 
ATOM   9834  C CA  . PHE G 1 20  ? 44.422  106.454 4.534   1.000 80.231  ? 338 PHE DDD CA  1 
ATOM   9835  C C   . PHE G 1 20  ? 43.508  105.800 3.490   1.000 76.817  ? 338 PHE DDD C   1 
ATOM   9836  O O   . PHE G 1 20  ? 44.031  105.324 2.462   1.000 79.968  ? 338 PHE DDD O   1 
ATOM   9837  C CB  . PHE G 1 20  ? 44.975  105.411 5.508   1.000 78.003  ? 338 PHE DDD CB  1 
ATOM   9838  C CG  . PHE G 1 20  ? 46.075  105.881 6.425   1.000 79.186  ? 338 PHE DDD CG  1 
ATOM   9839  C CD1 . PHE G 1 20  ? 47.207  106.505 5.922   1.000 79.919  ? 338 PHE DDD CD1 1 
ATOM   9840  C CD2 . PHE G 1 20  ? 45.999  105.658 7.791   1.000 81.525  ? 338 PHE DDD CD2 1 
ATOM   9841  C CE1 . PHE G 1 20  ? 48.233  106.904 6.764   1.000 78.006  ? 338 PHE DDD CE1 1 
ATOM   9842  C CE2 . PHE G 1 20  ? 47.025  106.066 8.631   1.000 87.516  ? 338 PHE DDD CE2 1 
ATOM   9843  C CZ  . PHE G 1 20  ? 48.136  106.696 8.118   1.000 80.552  ? 338 PHE DDD CZ  1 
ATOM   9844  N N   . GLY G 1 21  ? 42.192  105.778 3.745   1.000 74.629  ? 339 GLY DDD N   1 
ATOM   9845  C CA  . GLY G 1 21  ? 41.189  105.173 2.845   1.000 79.110  ? 339 GLY DDD CA  1 
ATOM   9846  C C   . GLY G 1 21  ? 41.309  105.750 1.446   1.000 83.819  ? 339 GLY DDD C   1 
ATOM   9847  O O   . GLY G 1 21  ? 41.390  104.959 0.471   1.000 75.015  ? 339 GLY DDD O   1 
ATOM   9848  N N   . GLU G 1 22  ? 41.381  107.085 1.358   1.000 94.268  ? 340 GLU DDD N   1 
ATOM   9849  C CA  . GLU G 1 22  ? 41.403  107.835 0.075   1.000 96.062  ? 340 GLU DDD CA  1 
ATOM   9850  C C   . GLU G 1 22  ? 42.805  107.793 -0.558  1.000 86.583  ? 340 GLU DDD C   1 
ATOM   9851  O O   . GLU G 1 22  ? 42.878  108.137 -1.749  1.000 82.204  ? 340 GLU DDD O   1 
ATOM   9852  C CB  . GLU G 1 22  ? 40.869  109.261 0.273   1.000 104.493 ? 340 GLU DDD CB  1 
ATOM   9853  C CG  . GLU G 1 22  ? 41.858  110.253 0.876   1.000 109.377 ? 340 GLU DDD CG  1 
ATOM   9854  C CD  . GLU G 1 22  ? 41.283  111.633 1.198   1.000 112.164 ? 340 GLU DDD CD  1 
ATOM   9855  O OE1 . GLU G 1 22  ? 40.434  111.734 2.123   1.000 99.305  ? 340 GLU DDD OE1 1 
ATOM   9856  O OE2 . GLU G 1 22  ? 41.687  112.611 0.536   1.000 110.524 ? 340 GLU DDD OE2 1 
ATOM   9857  N N   . VAL G 1 23  ? 43.858  107.380 0.172   1.000 75.984  ? 341 VAL DDD N   1 
ATOM   9858  C CA  . VAL G 1 23  ? 45.263  107.275 -0.349  1.000 66.763  ? 341 VAL DDD CA  1 
ATOM   9859  C C   . VAL G 1 23  ? 45.458  105.921 -1.030  1.000 64.482  ? 341 VAL DDD C   1 
ATOM   9860  O O   . VAL G 1 23  ? 46.129  105.883 -2.105  1.000 62.401  ? 341 VAL DDD O   1 
ATOM   9861  C CB  . VAL G 1 23  ? 46.324  107.432 0.755   1.000 68.011  ? 341 VAL DDD CB  1 
ATOM   9862  C CG1 . VAL G 1 23  ? 47.730  107.286 0.192   1.000 68.070  ? 341 VAL DDD CG1 1 
ATOM   9863  C CG2 . VAL G 1 23  ? 46.191  108.748 1.501   1.000 77.727  ? 341 VAL DDD CG2 1 
ATOM   9864  N N   . PHE G 1 24  ? 44.943  104.869 -0.378  1.000 60.023  ? 342 PHE DDD N   1 
ATOM   9865  C CA  . PHE G 1 24  ? 45.108  103.438 -0.739  1.000 57.444  ? 342 PHE DDD CA  1 
ATOM   9866  C C   . PHE G 1 24  ? 44.045  103.039 -1.763  1.000 61.433  ? 342 PHE DDD C   1 
ATOM   9867  O O   . PHE G 1 24  ? 44.411  102.368 -2.751  1.000 66.995  ? 342 PHE DDD O   1 
ATOM   9868  C CB  . PHE G 1 24  ? 45.014  102.537 0.498   1.000 53.544  ? 342 PHE DDD CB  1 
ATOM   9869  C CG  . PHE G 1 24  ? 46.284  102.387 1.303   1.000 47.112  ? 342 PHE DDD CG  1 
ATOM   9870  C CD1 . PHE G 1 24  ? 46.605  103.291 2.308   1.000 46.737  ? 342 PHE DDD CD1 1 
ATOM   9871  C CD2 . PHE G 1 24  ? 47.146  101.328 1.081   1.000 42.675  ? 342 PHE DDD CD2 1 
ATOM   9872  C CE1 . PHE G 1 24  ? 47.758  103.142 3.067   1.000 45.109  ? 342 PHE DDD CE1 1 
ATOM   9873  C CE2 . PHE G 1 24  ? 48.311  101.198 1.826   1.000 42.662  ? 342 PHE DDD CE2 1 
ATOM   9874  C CZ  . PHE G 1 24  ? 48.615  102.099 2.821   1.000 42.735  ? 342 PHE DDD CZ  1 
ATOM   9875  N N   . ASN G 1 25  ? 42.786  103.427 -1.531  1.000 69.514  ? 343 ASN DDD N   1 
ATOM   9876  C CA  . ASN G 1 25  ? 41.630  103.025 -2.382  1.000 78.462  ? 343 ASN DDD CA  1 
ATOM   9877  C C   . ASN G 1 25  ? 41.361  104.127 -3.421  1.000 71.010  ? 343 ASN DDD C   1 
ATOM   9878  O O   . ASN G 1 25  ? 40.287  104.073 -4.052  1.000 65.854  ? 343 ASN DDD O   1 
ATOM   9879  C CB  . ASN G 1 25  ? 40.389  102.653 -1.554  1.000 87.179  ? 343 ASN DDD CB  1 
ATOM   9880  C CG  . ASN G 1 25  ? 40.541  101.422 -0.685  1.000 92.101  ? 343 ASN DDD CG  1 
ATOM   9881  O OD1 . ASN G 1 25  ? 41.615  100.805 -0.655  1.000 95.261  ? 343 ASN DDD OD1 1 
ATOM   9882  N ND2 . ASN G 1 25  ? 39.423  101.078 -0.035  1.000 98.705  ? 343 ASN DDD ND2 1 
ATOM   9883  N N   . ALA G 1 26  ? 42.326  105.033 -3.633  1.000 66.983  ? 344 ALA DDD N   1 
ATOM   9884  C CA  . ALA G 1 26  ? 42.338  106.058 -4.707  1.000 68.826  ? 344 ALA DDD CA  1 
ATOM   9885  C C   . ALA G 1 26  ? 42.239  105.393 -6.088  1.000 69.673  ? 344 ALA DDD C   1 
ATOM   9886  O O   . ALA G 1 26  ? 43.078  104.518 -6.390  1.000 73.969  ? 344 ALA DDD O   1 
ATOM   9887  C CB  . ALA G 1 26  ? 43.607  106.867 -4.614  1.000 69.335  ? 344 ALA DDD CB  1 
ATOM   9888  N N   . THR G 1 27  ? 41.286  105.819 -6.918  1.000 65.980  ? 345 THR DDD N   1 
ATOM   9889  C CA  . THR G 1 27  ? 40.975  105.157 -8.217  1.000 68.015  ? 345 THR DDD CA  1 
ATOM   9890  C C   . THR G 1 27  ? 42.102  105.436 -9.221  1.000 68.794  ? 345 THR DDD C   1 
ATOM   9891  O O   . THR G 1 27  ? 42.387  104.539 -10.026 1.000 60.591  ? 345 THR DDD O   1 
ATOM   9892  C CB  . THR G 1 27  ? 39.573  105.544 -8.700  1.000 66.481  ? 345 THR DDD CB  1 
ATOM   9893  O OG1 . THR G 1 27  ? 39.439  106.928 -8.379  1.000 66.321  ? 345 THR DDD OG1 1 
ATOM   9894  C CG2 . THR G 1 27  ? 38.467  104.729 -8.052  1.000 63.505  ? 345 THR DDD CG2 1 
ATOM   9895  N N   . ARG G 1 28  ? 42.741  106.608 -9.147  1.000 74.425  ? 346 ARG DDD N   1 
ATOM   9896  C CA  . ARG G 1 28  ? 43.947  106.968 -9.950  1.000 75.301  ? 346 ARG DDD CA  1 
ATOM   9897  C C   . ARG G 1 28  ? 45.191  106.965 -9.043  1.000 63.066  ? 346 ARG DDD C   1 
ATOM   9898  O O   . ARG G 1 28  ? 45.157  107.570 -7.938  1.000 54.803  ? 346 ARG DDD O   1 
ATOM   9899  C CB  . ARG G 1 28  ? 43.734  108.329 -10.630 1.000 93.309  ? 346 ARG DDD CB  1 
ATOM   9900  C CG  . ARG G 1 28  ? 45.010  109.064 -11.045 1.000 113.745 ? 346 ARG DDD CG  1 
ATOM   9901  C CD  . ARG G 1 28  ? 44.805  110.354 -11.834 1.000 116.368 ? 346 ARG DDD CD  1 
ATOM   9902  N NE  . ARG G 1 28  ? 44.461  110.063 -13.223 1.000 121.949 ? 346 ARG DDD NE  1 
ATOM   9903  C CZ  . ARG G 1 28  ? 43.225  109.891 -13.698 1.000 121.498 ? 346 ARG DDD CZ  1 
ATOM   9904  N NH1 . ARG G 1 28  ? 42.166  110.004 -12.911 1.000 116.224 ? 346 ARG DDD NH1 1 
ATOM   9905  N NH2 . ARG G 1 28  ? 43.053  109.598 -14.976 1.000 123.104 ? 346 ARG DDD NH2 1 
ATOM   9906  N N   . PHE G 1 29  ? 46.282  106.351 -9.501  1.000 55.099  ? 347 PHE DDD N   1 
ATOM   9907  C CA  . PHE G 1 29  ? 47.622  106.444 -8.861  1.000 52.777  ? 347 PHE DDD CA  1 
ATOM   9908  C C   . PHE G 1 29  ? 48.534  107.293 -9.734  1.000 46.748  ? 347 PHE DDD C   1 
ATOM   9909  O O   . PHE G 1 29  ? 48.164  107.530 -10.872 1.000 58.359  ? 347 PHE DDD O   1 
ATOM   9910  C CB  . PHE G 1 29  ? 48.210  105.055 -8.605  1.000 53.419  ? 347 PHE DDD CB  1 
ATOM   9911  C CG  . PHE G 1 29  ? 48.082  104.626 -7.168  1.000 52.766  ? 347 PHE DDD CG  1 
ATOM   9912  C CD1 . PHE G 1 29  ? 46.847  104.633 -6.541  1.000 53.261  ? 347 PHE DDD CD1 1 
ATOM   9913  C CD2 . PHE G 1 29  ? 49.196  104.289 -6.429  1.000 54.218  ? 347 PHE DDD CD2 1 
ATOM   9914  C CE1 . PHE G 1 29  ? 46.721  104.278 -5.211  1.000 53.742  ? 347 PHE DDD CE1 1 
ATOM   9915  C CE2 . PHE G 1 29  ? 49.067  103.918 -5.102  1.000 58.089  ? 347 PHE DDD CE2 1 
ATOM   9916  C CZ  . PHE G 1 29  ? 47.832  103.920 -4.495  1.000 58.132  ? 347 PHE DDD CZ  1 
ATOM   9917  N N   . ALA G 1 30  ? 49.671  107.718 -9.191  1.000 41.532  ? 348 ALA DDD N   1 
ATOM   9918  C CA  . ALA G 1 30  ? 50.673  108.594 -9.836  1.000 42.615  ? 348 ALA DDD CA  1 
ATOM   9919  C C   . ALA G 1 30  ? 51.777  107.779 -10.538 1.000 45.485  ? 348 ALA DDD C   1 
ATOM   9920  O O   . ALA G 1 30  ? 52.038  106.655 -10.114 1.000 58.535  ? 348 ALA DDD O   1 
ATOM   9921  C CB  . ALA G 1 30  ? 51.248  109.473 -8.765  1.000 42.015  ? 348 ALA DDD CB  1 
ATOM   9922  N N   . SER G 1 31  ? 52.416  108.316 -11.581 1.000 42.586  ? 349 SER DDD N   1 
ATOM   9923  C CA  . SER G 1 31  ? 53.667  107.752 -12.158 1.000 40.021  ? 349 SER DDD CA  1 
ATOM   9924  C C   . SER G 1 31  ? 54.771  107.915 -11.119 1.000 40.761  ? 349 SER DDD C   1 
ATOM   9925  O O   . SER G 1 31  ? 54.753  108.923 -10.382 1.000 38.686  ? 349 SER DDD O   1 
ATOM   9926  C CB  . SER G 1 31  ? 54.058  108.421 -13.441 1.000 39.862  ? 349 SER DDD CB  1 
ATOM   9927  O OG  . SER G 1 31  ? 53.244  107.979 -14.508 1.000 39.177  ? 349 SER DDD OG  1 
ATOM   9928  N N   . VAL G 1 32  ? 55.700  106.970 -11.058 1.000 42.044  ? 350 VAL DDD N   1 
ATOM   9929  C CA  . VAL G 1 32  ? 56.744  106.960 -9.992  1.000 46.754  ? 350 VAL DDD CA  1 
ATOM   9930  C C   . VAL G 1 32  ? 57.574  108.262 -10.001 1.000 45.995  ? 350 VAL DDD C   1 
ATOM   9931  O O   . VAL G 1 32  ? 57.928  108.718 -8.896  1.000 45.409  ? 350 VAL DDD O   1 
ATOM   9932  C CB  . VAL G 1 32  ? 57.643  105.718 -10.101 1.000 50.664  ? 350 VAL DDD CB  1 
ATOM   9933  C CG1 . VAL G 1 32  ? 58.440  105.690 -11.401 1.000 54.868  ? 350 VAL DDD CG1 1 
ATOM   9934  C CG2 . VAL G 1 32  ? 58.567  105.596 -8.896  1.000 51.213  ? 350 VAL DDD CG2 1 
ATOM   9935  N N   . TYR G 1 33  ? 57.938  108.812 -11.171 1.000 46.045  ? 351 TYR DDD N   1 
ATOM   9936  C CA  . TYR G 1 33  ? 58.870  109.974 -11.299 1.000 45.440  ? 351 TYR DDD CA  1 
ATOM   9937  C C   . TYR G 1 33  ? 58.217  111.211 -10.689 1.000 41.226  ? 351 TYR DDD C   1 
ATOM   9938  O O   . TYR G 1 33  ? 58.948  112.042 -10.042 1.000 36.882  ? 351 TYR DDD O   1 
ATOM   9939  C CB  . TYR G 1 33  ? 59.250  110.236 -12.759 1.000 46.354  ? 351 TYR DDD CB  1 
ATOM   9940  C CG  . TYR G 1 33  ? 58.205  110.956 -13.579 1.000 45.550  ? 351 TYR DDD CG  1 
ATOM   9941  C CD1 . TYR G 1 33  ? 57.133  110.273 -14.120 1.000 42.171  ? 351 TYR DDD CD1 1 
ATOM   9942  C CD2 . TYR G 1 33  ? 58.286  112.322 -13.821 1.000 45.826  ? 351 TYR DDD CD2 1 
ATOM   9943  C CE1 . TYR G 1 33  ? 56.178  110.918 -14.885 1.000 39.048  ? 351 TYR DDD CE1 1 
ATOM   9944  C CE2 . TYR G 1 33  ? 57.333  112.984 -14.577 1.000 40.688  ? 351 TYR DDD CE2 1 
ATOM   9945  C CZ  . TYR G 1 33  ? 56.284  112.273 -15.120 1.000 38.747  ? 351 TYR DDD CZ  1 
ATOM   9946  O OH  . TYR G 1 33  ? 55.352  112.897 -15.887 1.000 39.481  ? 351 TYR DDD OH  1 
ATOM   9947  N N   . ALA G 1 34  ? 56.894  111.279 -10.905 1.000 38.056  ? 352 ALA DDD N   1 
ATOM   9948  C CA  . ALA G 1 34  ? 55.949  112.330 -10.474 1.000 40.060  ? 352 ALA DDD CA  1 
ATOM   9949  C C   . ALA G 1 34  ? 55.146  111.807 -9.278  1.000 37.851  ? 352 ALA DDD C   1 
ATOM   9950  O O   . ALA G 1 34  ? 53.900  111.883 -9.279  1.000 39.632  ? 352 ALA DDD O   1 
ATOM   9951  C CB  . ALA G 1 34  ? 55.062  112.692 -11.639 1.000 40.792  ? 352 ALA DDD CB  1 
ATOM   9952  N N   . TRP G 1 35  ? 55.853  111.274 -8.294  1.000 35.679  ? 353 TRP DDD N   1 
ATOM   9953  C CA  . TRP G 1 35  ? 55.227  110.552 -7.164  1.000 36.797  ? 353 TRP DDD CA  1 
ATOM   9954  C C   . TRP G 1 35  ? 54.417  111.513 -6.307  1.000 37.249  ? 353 TRP DDD C   1 
ATOM   9955  O O   . TRP G 1 35  ? 54.861  112.635 -6.084  1.000 43.166  ? 353 TRP DDD O   1 
ATOM   9956  C CB  . TRP G 1 35  ? 56.256  109.789 -6.334  1.000 36.380  ? 353 TRP DDD CB  1 
ATOM   9957  C CG  . TRP G 1 35  ? 57.459  110.552 -5.894  1.000 34.501  ? 353 TRP DDD CG  1 
ATOM   9958  C CD1 . TRP G 1 35  ? 58.656  110.646 -6.539  1.000 35.834  ? 353 TRP DDD CD1 1 
ATOM   9959  C CD2 . TRP G 1 35  ? 57.605  111.250 -4.651  1.000 34.827  ? 353 TRP DDD CD2 1 
ATOM   9960  N NE1 . TRP G 1 35  ? 59.530  111.391 -5.797  1.000 36.816  ? 353 TRP DDD NE1 1 
ATOM   9961  C CE2 . TRP G 1 35  ? 58.916  111.764 -4.628  1.000 36.754  ? 353 TRP DDD CE2 1 
ATOM   9962  C CE3 . TRP G 1 35  ? 56.756  111.490 -3.563  1.000 37.266  ? 353 TRP DDD CE3 1 
ATOM   9963  C CZ2 . TRP G 1 35  ? 59.391  112.510 -3.551  1.000 37.984  ? 353 TRP DDD CZ2 1 
ATOM   9964  C CZ3 . TRP G 1 35  ? 57.226  112.221 -2.497  1.000 37.267  ? 353 TRP DDD CZ3 1 
ATOM   9965  C CH2 . TRP G 1 35  ? 58.528  112.718 -2.495  1.000 37.851  ? 353 TRP DDD CH2 1 
ATOM   9966  N N   . ASN G 1 36  ? 53.276  111.033 -5.852  1.000 39.036  ? 354 ASN DDD N   1 
ATOM   9967  C CA  . ASN G 1 36  ? 52.294  111.772 -5.033  1.000 45.411  ? 354 ASN DDD CA  1 
ATOM   9968  C C   . ASN G 1 36  ? 52.631  111.615 -3.552  1.000 46.313  ? 354 ASN DDD C   1 
ATOM   9969  O O   . ASN G 1 36  ? 52.923  110.495 -3.155  1.000 53.866  ? 354 ASN DDD O   1 
ATOM   9970  C CB  . ASN G 1 36  ? 50.893  111.242 -5.295  1.000 49.640  ? 354 ASN DDD CB  1 
ATOM   9971  C CG  . ASN G 1 36  ? 49.907  112.372 -5.281  1.000 57.437  ? 354 ASN DDD CG  1 
ATOM   9972  O OD1 . ASN G 1 36  ? 49.787  113.059 -4.259  1.000 65.871  ? 354 ASN DDD OD1 1 
ATOM   9973  N ND2 . ASN G 1 36  ? 49.274  112.590 -6.427  1.000 61.625  ? 354 ASN DDD ND2 1 
ATOM   9974  N N   . ARG G 1 37  ? 52.598  112.698 -2.778  1.000 46.426  ? 355 ARG DDD N   1 
ATOM   9975  C CA  . ARG G 1 37  ? 52.785  112.691 -1.301  1.000 46.911  ? 355 ARG DDD CA  1 
ATOM   9976  C C   . ARG G 1 37  ? 51.559  113.342 -0.660  1.000 49.693  ? 355 ARG DDD C   1 
ATOM   9977  O O   . ARG G 1 37  ? 51.370  114.548 -0.884  1.000 55.900  ? 355 ARG DDD O   1 
ATOM   9978  C CB  . ARG G 1 37  ? 54.069  113.426 -0.886  1.000 42.864  ? 355 ARG DDD CB  1 
ATOM   9979  C CG  . ARG G 1 37  ? 54.087  113.868 0.572   1.000 41.002  ? 355 ARG DDD CG  1 
ATOM   9980  C CD  . ARG G 1 37  ? 55.458  114.249 1.091   1.000 38.997  ? 355 ARG DDD CD  1 
ATOM   9981  N NE  . ARG G 1 37  ? 56.391  113.139 1.091   1.000 39.077  ? 355 ARG DDD NE  1 
ATOM   9982  C CZ  . ARG G 1 37  ? 57.571  113.121 1.716   1.000 41.789  ? 355 ARG DDD CZ  1 
ATOM   9983  N NH1 . ARG G 1 37  ? 57.995  114.156 2.420   1.000 39.714  ? 355 ARG DDD NH1 1 
ATOM   9984  N NH2 . ARG G 1 37  ? 58.326  112.041 1.665   1.000 48.302  ? 355 ARG DDD NH2 1 
ATOM   9985  N N   . LYS G 1 38  ? 50.782  112.574 0.107   1.000 52.053  ? 356 LYS DDD N   1 
ATOM   9986  C CA  . LYS G 1 38  ? 49.699  113.086 0.986   1.000 56.366  ? 356 LYS DDD CA  1 
ATOM   9987  C C   . LYS G 1 38  ? 50.294  113.315 2.366   1.000 61.483  ? 356 LYS DDD C   1 
ATOM   9988  O O   . LYS G 1 38  ? 50.893  112.370 2.888   1.000 75.515  ? 356 LYS DDD O   1 
ATOM   9989  C CB  . LYS G 1 38  ? 48.544  112.093 1.083   1.000 60.766  ? 356 LYS DDD CB  1 
ATOM   9990  C CG  . LYS G 1 38  ? 47.276  112.641 1.726   1.000 68.278  ? 356 LYS DDD CG  1 
ATOM   9991  C CD  . LYS G 1 38  ? 46.379  113.418 0.780   1.000 80.948  ? 356 LYS DDD CD  1 
ATOM   9992  C CE  . LYS G 1 38  ? 44.906  113.242 1.088   1.000 86.340  ? 356 LYS DDD CE  1 
ATOM   9993  N NZ  . LYS G 1 38  ? 44.579  113.735 2.446   1.000 92.963  ? 356 LYS DDD NZ  1 
ATOM   9994  N N   . ARG G 1 39  ? 50.197  114.533 2.899   1.000 71.932  ? 357 ARG DDD N   1 
ATOM   9995  C CA  . ARG G 1 39  ? 50.584  114.834 4.301   1.000 72.013  ? 357 ARG DDD CA  1 
ATOM   9996  C C   . ARG G 1 39  ? 49.431  114.356 5.181   1.000 72.722  ? 357 ARG DDD C   1 
ATOM   9997  O O   . ARG G 1 39  ? 48.264  114.545 4.775   1.000 72.785  ? 357 ARG DDD O   1 
ATOM   9998  C CB  . ARG G 1 39  ? 50.883  116.321 4.514   1.000 74.569  ? 357 ARG DDD CB  1 
ATOM   9999  C CG  . ARG G 1 39  ? 50.386  116.876 5.843   1.000 78.063  ? 357 ARG DDD CG  1 
ATOM   10000 C CD  . ARG G 1 39  ? 50.551  118.371 5.936   1.000 82.429  ? 357 ARG DDD CD  1 
ATOM   10001 N NE  . ARG G 1 39  ? 51.893  118.682 6.406   1.000 83.452  ? 357 ARG DDD NE  1 
ATOM   10002 C CZ  . ARG G 1 39  ? 52.179  119.264 7.568   1.000 82.007  ? 357 ARG DDD CZ  1 
ATOM   10003 N NH1 . ARG G 1 39  ? 51.202  119.637 8.389   1.000 75.518  ? 357 ARG DDD NH1 1 
ATOM   10004 N NH2 . ARG G 1 39  ? 53.446  119.498 7.879   1.000 75.927  ? 357 ARG DDD NH2 1 
ATOM   10005 N N   . ILE G 1 40  ? 49.765  113.711 6.299   1.000 74.185  ? 358 ILE DDD N   1 
ATOM   10006 C CA  . ILE G 1 40  ? 48.815  113.300 7.371   1.000 74.236  ? 358 ILE DDD CA  1 
ATOM   10007 C C   . ILE G 1 40  ? 49.135  114.143 8.614   1.000 77.660  ? 358 ILE DDD C   1 
ATOM   10008 O O   . ILE G 1 40  ? 50.325  114.154 9.048   1.000 64.479  ? 358 ILE DDD O   1 
ATOM   10009 C CB  . ILE G 1 40  ? 48.917  111.791 7.659   1.000 78.829  ? 358 ILE DDD CB  1 
ATOM   10010 C CG1 . ILE G 1 40  ? 48.881  110.924 6.394   1.000 80.042  ? 358 ILE DDD CG1 1 
ATOM   10011 C CG2 . ILE G 1 40  ? 47.855  111.386 8.660   1.000 84.774  ? 358 ILE DDD CG2 1 
ATOM   10012 C CD1 . ILE G 1 40  ? 47.560  110.886 5.683   1.000 79.983  ? 358 ILE DDD CD1 1 
ATOM   10013 N N   . SER G 1 41  ? 48.116  114.851 9.122   1.000 83.917  ? 359 SER DDD N   1 
ATOM   10014 C CA  . SER G 1 41  ? 48.133  115.677 10.361  1.000 87.223  ? 359 SER DDD CA  1 
ATOM   10015 C C   . SER G 1 41  ? 46.713  115.741 10.936  1.000 94.054  ? 359 SER DDD C   1 
ATOM   10016 O O   . SER G 1 41  ? 45.754  115.568 10.150  1.000 90.127  ? 359 SER DDD O   1 
ATOM   10017 C CB  . SER G 1 41  ? 48.676  117.073 10.112  1.000 86.327  ? 359 SER DDD CB  1 
ATOM   10018 O OG  . SER G 1 41  ? 50.074  117.052 9.859   1.000 94.185  ? 359 SER DDD OG  1 
ATOM   10019 N N   . ASN G 1 42  ? 46.602  115.940 12.256  1.000 100.698 ? 360 ASN DDD N   1 
ATOM   10020 C CA  . ASN G 1 42  ? 45.354  116.333 12.967  1.000 105.380 ? 360 ASN DDD CA  1 
ATOM   10021 C C   . ASN G 1 42  ? 44.266  115.285 12.714  1.000 110.550 ? 360 ASN DDD C   1 
ATOM   10022 O O   . ASN G 1 42  ? 43.138  115.664 12.303  1.000 105.912 ? 360 ASN DDD O   1 
ATOM   10023 C CB  . ASN G 1 42  ? 44.881  117.725 12.546  1.000 107.520 ? 360 ASN DDD CB  1 
ATOM   10024 C CG  . ASN G 1 42  ? 45.939  118.781 12.779  1.000 114.855 ? 360 ASN DDD CG  1 
ATOM   10025 O OD1 . ASN G 1 42  ? 46.630  119.197 11.850  1.000 118.284 ? 360 ASN DDD OD1 1 
ATOM   10026 N ND2 . ASN G 1 42  ? 46.099  119.195 14.024  1.000 117.549 ? 360 ASN DDD ND2 1 
ATOM   10027 N N   . CYS G 1 43  ? 44.598  114.014 12.945  1.000 114.607 ? 361 CYS DDD N   1 
ATOM   10028 C CA  . CYS G 1 43  ? 43.650  112.874 12.842  1.000 118.883 ? 361 CYS DDD CA  1 
ATOM   10029 C C   . CYS G 1 43  ? 44.181  111.670 13.636  1.000 114.696 ? 361 CYS DDD C   1 
ATOM   10030 O O   . CYS G 1 43  ? 45.402  111.631 13.926  1.000 106.268 ? 361 CYS DDD O   1 
ATOM   10031 C CB  . CYS G 1 43  ? 43.402  112.506 11.385  1.000 119.483 ? 361 CYS DDD CB  1 
ATOM   10032 S SG  . CYS G 1 43  ? 44.917  112.104 10.476  1.000 121.950 ? 361 CYS DDD SG  1 
ATOM   10033 N N   . VAL G 1 44  ? 43.282  110.733 13.955  1.000 113.086 ? 362 VAL DDD N   1 
ATOM   10034 C CA  . VAL G 1 44  ? 43.568  109.465 14.691  1.000 106.215 ? 362 VAL DDD CA  1 
ATOM   10035 C C   . VAL G 1 44  ? 43.644  108.320 13.669  1.000 104.665 ? 362 VAL DDD C   1 
ATOM   10036 O O   . VAL G 1 44  ? 42.660  108.115 12.892  1.000 91.999  ? 362 VAL DDD O   1 
ATOM   10037 C CB  . VAL G 1 44  ? 42.513  109.192 15.780  1.000 101.395 ? 362 VAL DDD CB  1 
ATOM   10038 C CG1 . VAL G 1 44  ? 42.953  108.066 16.709  1.000 103.878 ? 362 VAL DDD CG1 1 
ATOM   10039 C CG2 . VAL G 1 44  ? 42.166  110.448 16.574  1.000 97.230  ? 362 VAL DDD CG2 1 
ATOM   10040 N N   . ALA G 1 45  ? 44.773  107.599 13.676  1.000 102.827 ? 363 ALA DDD N   1 
ATOM   10041 C CA  . ALA G 1 45  ? 45.180  106.646 12.617  1.000 105.171 ? 363 ALA DDD CA  1 
ATOM   10042 C C   . ALA G 1 45  ? 45.056  105.208 13.126  1.000 91.514  ? 363 ALA DDD C   1 
ATOM   10043 O O   . ALA G 1 45  ? 45.750  104.858 14.093  1.000 89.670  ? 363 ALA DDD O   1 
ATOM   10044 C CB  . ALA G 1 45  ? 46.589  106.955 12.180  1.000 114.308 ? 363 ALA DDD CB  1 
ATOM   10045 N N   . ASP G 1 46  ? 44.212  104.409 12.477  1.000 83.830  ? 364 ASP DDD N   1 
ATOM   10046 C CA  . ASP G 1 46  ? 43.967  102.995 12.851  1.000 95.248  ? 364 ASP DDD CA  1 
ATOM   10047 C C   . ASP G 1 46  ? 44.836  102.088 11.971  1.000 90.603  ? 364 ASP DDD C   1 
ATOM   10048 O O   . ASP G 1 46  ? 44.327  101.606 10.938  1.000 96.021  ? 364 ASP DDD O   1 
ATOM   10049 C CB  . ASP G 1 46  ? 42.483  102.656 12.710  1.000 107.761 ? 364 ASP DDD CB  1 
ATOM   10050 C CG  . ASP G 1 46  ? 42.170  101.246 13.178  1.000 115.661 ? 364 ASP DDD CG  1 
ATOM   10051 O OD1 . ASP G 1 46  ? 41.571  100.490 12.390  1.000 102.262 ? 364 ASP DDD OD1 1 
ATOM   10052 O OD2 . ASP G 1 46  ? 42.554  100.913 14.326  1.000 134.630 ? 364 ASP DDD OD2 1 
ATOM   10053 N N   . TYR G 1 47  ? 46.088  101.844 12.364  1.000 78.489  ? 365 TYR DDD N   1 
ATOM   10054 C CA  . TYR G 1 47  ? 47.087  101.178 11.491  1.000 76.823  ? 365 TYR DDD CA  1 
ATOM   10055 C C   . TYR G 1 47  ? 46.759  99.687  11.360  1.000 78.859  ? 365 TYR DDD C   1 
ATOM   10056 O O   . TYR G 1 47  ? 47.295  99.028  10.458  1.000 88.191  ? 365 TYR DDD O   1 
ATOM   10057 C CB  . TYR G 1 47  ? 48.505  101.411 12.009  1.000 79.292  ? 365 TYR DDD CB  1 
ATOM   10058 C CG  . TYR G 1 47  ? 48.965  102.849 11.968  1.000 89.055  ? 365 TYR DDD CG  1 
ATOM   10059 C CD1 . TYR G 1 47  ? 49.726  103.352 10.920  1.000 90.893  ? 365 TYR DDD CD1 1 
ATOM   10060 C CD2 . TYR G 1 47  ? 48.661  103.712 13.007  1.000 94.632  ? 365 TYR DDD CD2 1 
ATOM   10061 C CE1 . TYR G 1 47  ? 50.172  104.666 10.915  1.000 88.864  ? 365 TYR DDD CE1 1 
ATOM   10062 C CE2 . TYR G 1 47  ? 49.097  105.027 13.017  1.000 89.686  ? 365 TYR DDD CE2 1 
ATOM   10063 C CZ  . TYR G 1 47  ? 49.850  105.510 11.965  1.000 87.549  ? 365 TYR DDD CZ  1 
ATOM   10064 O OH  . TYR G 1 47  ? 50.266  106.809 12.010  1.000 85.158  ? 365 TYR DDD OH  1 
ATOM   10065 N N   . SER G 1 48  ? 45.892  99.167  12.226  1.000 84.407  ? 366 SER DDD N   1 
ATOM   10066 C CA  . SER G 1 48  ? 45.394  97.766  12.181  1.000 86.374  ? 366 SER DDD CA  1 
ATOM   10067 C C   . SER G 1 48  ? 44.711  97.453  10.837  1.000 84.601  ? 366 SER DDD C   1 
ATOM   10068 O O   . SER G 1 48  ? 44.963  96.351  10.318  1.000 87.120  ? 366 SER DDD O   1 
ATOM   10069 C CB  . SER G 1 48  ? 44.460  97.512  13.328  1.000 87.866  ? 366 SER DDD CB  1 
ATOM   10070 O OG  . SER G 1 48  ? 43.297  98.327  13.216  1.000 90.311  ? 366 SER DDD OG  1 
ATOM   10071 N N   . VAL G 1 49  ? 43.881  98.365  10.301  1.000 88.305  ? 367 VAL DDD N   1 
ATOM   10072 C CA  . VAL G 1 49  ? 43.183  98.205  8.982   1.000 83.064  ? 367 VAL DDD CA  1 
ATOM   10073 C C   . VAL G 1 49  ? 44.228  97.739  7.968   1.000 76.043  ? 367 VAL DDD C   1 
ATOM   10074 O O   . VAL G 1 49  ? 43.890  96.888  7.132   1.000 69.822  ? 367 VAL DDD O   1 
ATOM   10075 C CB  . VAL G 1 49  ? 42.496  99.498  8.478   1.000 86.256  ? 367 VAL DDD CB  1 
ATOM   10076 C CG1 . VAL G 1 49  ? 41.996  99.361  7.044   1.000 85.710  ? 367 VAL DDD CG1 1 
ATOM   10077 C CG2 . VAL G 1 49  ? 41.354  99.955  9.372   1.000 87.592  ? 367 VAL DDD CG2 1 
ATOM   10078 N N   . LEU G 1 50  ? 45.446  98.278  8.072   1.000 70.511  ? 368 LEU DDD N   1 
ATOM   10079 C CA  . LEU G 1 50  ? 46.534  98.082  7.083   1.000 73.126  ? 368 LEU DDD CA  1 
ATOM   10080 C C   . LEU G 1 50  ? 47.104  96.666  7.169   1.000 77.701  ? 368 LEU DDD C   1 
ATOM   10081 O O   . LEU G 1 50  ? 47.039  95.973  6.138   1.000 82.901  ? 368 LEU DDD O   1 
ATOM   10082 C CB  . LEU G 1 50  ? 47.638  99.123  7.297   1.000 74.548  ? 368 LEU DDD CB  1 
ATOM   10083 C CG  . LEU G 1 50  ? 47.591  100.354 6.391   1.000 72.694  ? 368 LEU DDD CG  1 
ATOM   10084 C CD1 . LEU G 1 50  ? 46.165  100.705 5.999   1.000 72.004  ? 368 LEU DDD CD1 1 
ATOM   10085 C CD2 . LEU G 1 50  ? 48.279  101.544 7.058   1.000 72.068  ? 368 LEU DDD CD2 1 
ATOM   10086 N N   . TYR G 1 51  ? 47.662  96.250  8.315   1.000 80.412  ? 369 TYR DDD N   1 
ATOM   10087 C CA  . TYR G 1 51  ? 48.459  94.992  8.402   1.000 83.927  ? 369 TYR DDD CA  1 
ATOM   10088 C C   . TYR G 1 51  ? 47.546  93.768  8.568   1.000 84.370  ? 369 TYR DDD C   1 
ATOM   10089 O O   . TYR G 1 51  ? 48.001  92.652  8.276   1.000 98.219  ? 369 TYR DDD O   1 
ATOM   10090 C CB  . TYR G 1 51  ? 49.570  95.064  9.457   1.000 81.324  ? 369 TYR DDD CB  1 
ATOM   10091 C CG  . TYR G 1 51  ? 49.141  95.469  10.836  1.000 85.238  ? 369 TYR DDD CG  1 
ATOM   10092 C CD1 . TYR G 1 51  ? 49.264  96.782  11.253  1.000 85.606  ? 369 TYR DDD CD1 1 
ATOM   10093 C CD2 . TYR G 1 51  ? 48.638  94.537  11.727  1.000 91.992  ? 369 TYR DDD CD2 1 
ATOM   10094 C CE1 . TYR G 1 51  ? 48.885  97.171  12.523  1.000 88.757  ? 369 TYR DDD CE1 1 
ATOM   10095 C CE2 . TYR G 1 51  ? 48.254  94.908  13.005  1.000 98.242  ? 369 TYR DDD CE2 1 
ATOM   10096 C CZ  . TYR G 1 51  ? 48.371  96.232  13.396  1.000 98.822  ? 369 TYR DDD CZ  1 
ATOM   10097 O OH  . TYR G 1 51  ? 47.999  96.647  14.638  1.000 105.181 ? 369 TYR DDD OH  1 
ATOM   10098 N N   . ASN G 1 52  ? 46.291  93.949  8.969   1.000 87.646  ? 370 ASN DDD N   1 
ATOM   10099 C CA  . ASN G 1 52  ? 45.316  92.831  9.069   1.000 89.470  ? 370 ASN DDD CA  1 
ATOM   10100 C C   . ASN G 1 52  ? 44.721  92.554  7.686   1.000 86.847  ? 370 ASN DDD C   1 
ATOM   10101 O O   . ASN G 1 52  ? 44.051  91.523  7.538   1.000 106.374 ? 370 ASN DDD O   1 
ATOM   10102 C CB  . ASN G 1 52  ? 44.240  93.106  10.120  1.000 93.162  ? 370 ASN DDD CB  1 
ATOM   10103 C CG  . ASN G 1 52  ? 44.803  93.211  11.524  1.000 94.807  ? 370 ASN DDD CG  1 
ATOM   10104 O OD1 . ASN G 1 52  ? 45.866  92.667  11.832  1.000 81.367  ? 370 ASN DDD OD1 1 
ATOM   10105 N ND2 . ASN G 1 52  ? 44.099  93.925  12.386  1.000 104.999 ? 370 ASN DDD ND2 1 
ATOM   10106 N N   . SER G 1 53  ? 44.945  93.437  6.714   1.000 82.006  ? 371 SER DDD N   1 
ATOM   10107 C CA  . SER G 1 53  ? 44.559  93.210  5.300   1.000 79.354  ? 371 SER DDD CA  1 
ATOM   10108 C C   . SER G 1 53  ? 45.391  92.050  4.753   1.000 74.281  ? 371 SER DDD C   1 
ATOM   10109 O O   . SER G 1 53  ? 46.603  91.970  5.061   1.000 58.470  ? 371 SER DDD O   1 
ATOM   10110 C CB  . SER G 1 53  ? 44.724  94.448  4.459   1.000 78.196  ? 371 SER DDD CB  1 
ATOM   10111 O OG  . SER G 1 53  ? 44.535  94.147  3.088   1.000 79.835  ? 371 SER DDD OG  1 
ATOM   10112 N N   . ALA G 1 54  ? 44.743  91.183  3.981   1.000 75.559  ? 372 ALA DDD N   1 
ATOM   10113 C CA  . ALA G 1 54  ? 45.358  90.001  3.346   1.000 84.977  ? 372 ALA DDD CA  1 
ATOM   10114 C C   . ALA G 1 54  ? 45.522  90.274  1.847   1.000 84.576  ? 372 ALA DDD C   1 
ATOM   10115 O O   . ALA G 1 54  ? 45.739  89.303  1.085   1.000 87.000  ? 372 ALA DDD O   1 
ATOM   10116 C CB  . ALA G 1 54  ? 44.505  88.783  3.619   1.000 87.236  ? 372 ALA DDD CB  1 
ATOM   10117 N N   . SER G 1 55  ? 45.458  91.546  1.438   1.000 82.464  ? 373 SER DDD N   1 
ATOM   10118 C CA  . SER G 1 55  ? 45.456  91.959  0.010   1.000 77.554  ? 373 SER DDD CA  1 
ATOM   10119 C C   . SER G 1 55  ? 46.801  92.586  -0.399  1.000 67.799  ? 373 SER DDD C   1 
ATOM   10120 O O   . SER G 1 55  ? 46.831  93.217  -1.459  1.000 64.442  ? 373 SER DDD O   1 
ATOM   10121 C CB  . SER G 1 55  ? 44.281  92.873  -0.279  1.000 73.863  ? 373 SER DDD CB  1 
ATOM   10122 O OG  . SER G 1 55  ? 44.357  94.052  0.503   1.000 70.530  ? 373 SER DDD OG  1 
ATOM   10123 N N   . PHE G 1 56  ? 47.884  92.371  0.355   1.000 60.070  ? 374 PHE DDD N   1 
ATOM   10124 C CA  . PHE G 1 56  ? 49.166  93.082  0.124   1.000 57.411  ? 374 PHE DDD CA  1 
ATOM   10125 C C   . PHE G 1 56  ? 50.272  92.092  -0.234  1.000 55.170  ? 374 PHE DDD C   1 
ATOM   10126 O O   . PHE G 1 56  ? 50.519  91.211  0.589   1.000 66.040  ? 374 PHE DDD O   1 
ATOM   10127 C CB  . PHE G 1 56  ? 49.520  93.929  1.347   1.000 56.512  ? 374 PHE DDD CB  1 
ATOM   10128 C CG  . PHE G 1 56  ? 48.642  95.140  1.553   1.000 59.715  ? 374 PHE DDD CG  1 
ATOM   10129 C CD1 . PHE G 1 56  ? 48.177  95.893  0.481   1.000 65.229  ? 374 PHE DDD CD1 1 
ATOM   10130 C CD2 . PHE G 1 56  ? 48.304  95.558  2.832   1.000 61.345  ? 374 PHE DDD CD2 1 
ATOM   10131 C CE1 . PHE G 1 56  ? 47.366  97.002  0.678   1.000 64.109  ? 374 PHE DDD CE1 1 
ATOM   10132 C CE2 . PHE G 1 56  ? 47.514  96.680  3.032   1.000 61.162  ? 374 PHE DDD CE2 1 
ATOM   10133 C CZ  . PHE G 1 56  ? 47.042  97.395  1.954   1.000 63.635  ? 374 PHE DDD CZ  1 
ATOM   10134 N N   . SER G 1 57  ? 50.919  92.262  -1.396  1.000 50.067  ? 375 SER DDD N   1 
ATOM   10135 C CA  . SER G 1 57  ? 52.144  91.525  -1.815  1.000 50.588  ? 375 SER DDD CA  1 
ATOM   10136 C C   . SER G 1 57  ? 53.276  91.744  -0.815  1.000 46.557  ? 375 SER DDD C   1 
ATOM   10137 O O   . SER G 1 57  ? 53.969  90.808  -0.505  1.000 48.027  ? 375 SER DDD O   1 
ATOM   10138 C CB  . SER G 1 57  ? 52.620  91.939  -3.187  1.000 57.594  ? 375 SER DDD CB  1 
ATOM   10139 O OG  . SER G 1 57  ? 51.812  91.348  -4.189  1.000 73.565  ? 375 SER DDD OG  1 
ATOM   10140 N N   . THR G 1 58  ? 53.485  92.978  -0.384  1.000 48.398  ? 376 THR DDD N   1 
ATOM   10141 C CA  . THR G 1 58  ? 54.717  93.440  0.300   1.000 46.436  ? 376 THR DDD CA  1 
ATOM   10142 C C   . THR G 1 58  ? 54.293  94.324  1.471   1.000 46.022  ? 376 THR DDD C   1 
ATOM   10143 O O   . THR G 1 58  ? 53.272  95.037  1.307   1.000 51.765  ? 376 THR DDD O   1 
ATOM   10144 C CB  . THR G 1 58  ? 55.580  94.183  -0.723  1.000 47.609  ? 376 THR DDD CB  1 
ATOM   10145 O OG1 . THR G 1 58  ? 56.083  93.211  -1.639  1.000 48.894  ? 376 THR DDD OG1 1 
ATOM   10146 C CG2 . THR G 1 58  ? 56.675  95.024  -0.094  1.000 49.831  ? 376 THR DDD CG2 1 
ATOM   10147 N N   . PHE G 1 59  ? 55.006  94.274  2.601   1.000 40.677  ? 377 PHE DDD N   1 
ATOM   10148 C CA  . PHE G 1 59  ? 54.729  95.161  3.759   1.000 40.401  ? 377 PHE DDD CA  1 
ATOM   10149 C C   . PHE G 1 59  ? 55.984  95.217  4.625   1.000 41.307  ? 377 PHE DDD C   1 
ATOM   10150 O O   . PHE G 1 59  ? 55.970  94.835  5.796   1.000 44.950  ? 377 PHE DDD O   1 
ATOM   10151 C CB  . PHE G 1 59  ? 53.471  94.687  4.486   1.000 39.121  ? 377 PHE DDD CB  1 
ATOM   10152 C CG  . PHE G 1 59  ? 52.727  95.731  5.279   1.000 38.816  ? 377 PHE DDD CG  1 
ATOM   10153 C CD1 . PHE G 1 59  ? 53.382  96.539  6.189   1.000 39.203  ? 377 PHE DDD CD1 1 
ATOM   10154 C CD2 . PHE G 1 59  ? 51.347  95.869  5.146   1.000 41.014  ? 377 PHE DDD CD2 1 
ATOM   10155 C CE1 . PHE G 1 59  ? 52.679  97.476  6.934   1.000 40.572  ? 377 PHE DDD CE1 1 
ATOM   10156 C CE2 . PHE G 1 59  ? 50.638  96.807  5.892   1.000 41.269  ? 377 PHE DDD CE2 1 
ATOM   10157 C CZ  . PHE G 1 59  ? 51.311  97.611  6.786   1.000 41.546  ? 377 PHE DDD CZ  1 
ATOM   10158 N N   . LYS G 1 60  ? 57.059  95.709  4.026   1.000 43.638  ? 378 LYS DDD N   1 
ATOM   10159 C CA  . LYS G 1 60  ? 58.396  95.818  4.663   1.000 47.550  ? 378 LYS DDD CA  1 
ATOM   10160 C C   . LYS G 1 60  ? 58.435  97.132  5.430   1.000 47.760  ? 378 LYS DDD C   1 
ATOM   10161 O O   . LYS G 1 60  ? 58.427  98.178  4.780   1.000 53.138  ? 378 LYS DDD O   1 
ATOM   10162 C CB  . LYS G 1 60  ? 59.514  95.756  3.611   1.000 48.479  ? 378 LYS DDD CB  1 
ATOM   10163 C CG  . LYS G 1 60  ? 59.236  94.836  2.425   1.000 51.243  ? 378 LYS DDD CG  1 
ATOM   10164 C CD  . LYS G 1 60  ? 60.369  93.880  2.074   1.000 48.475  ? 378 LYS DDD CD  1 
ATOM   10165 C CE  . LYS G 1 60  ? 61.645  94.599  1.715   1.000 50.246  ? 378 LYS DDD CE  1 
ATOM   10166 N NZ  . LYS G 1 60  ? 62.602  93.693  1.050   1.000 49.554  ? 378 LYS DDD NZ  1 
ATOM   10167 N N   . CYS G 1 61  ? 58.442  97.075  6.757   1.000 49.506  ? 379 CYS DDD N   1 
ATOM   10168 C CA  . CYS G 1 61  ? 58.608  98.276  7.610   1.000 46.775  ? 379 CYS DDD CA  1 
ATOM   10169 C C   . CYS G 1 61  ? 60.050  98.363  8.069   1.000 40.651  ? 379 CYS DDD C   1 
ATOM   10170 O O   . CYS G 1 61  ? 60.652  97.315  8.218   1.000 39.107  ? 379 CYS DDD O   1 
ATOM   10171 C CB  . CYS G 1 61  ? 57.639  98.255  8.773   1.000 49.537  ? 379 CYS DDD CB  1 
ATOM   10172 S SG  . CYS G 1 61  ? 55.944  98.259  8.150   1.000 61.800  ? 379 CYS DDD SG  1 
ATOM   10173 N N   . TYR G 1 62  ? 60.563  99.581  8.210   1.000 40.442  ? 380 TYR DDD N   1 
ATOM   10174 C CA  . TYR G 1 62  ? 61.973  99.893  8.552   1.000 40.214  ? 380 TYR DDD CA  1 
ATOM   10175 C C   . TYR G 1 62  ? 61.964  100.801 9.782   1.000 40.769  ? 380 TYR DDD C   1 
ATOM   10176 O O   . TYR G 1 62  ? 61.226  101.780 9.782   1.000 43.540  ? 380 TYR DDD O   1 
ATOM   10177 C CB  . TYR G 1 62  ? 62.688  100.495 7.336   1.000 39.088  ? 380 TYR DDD CB  1 
ATOM   10178 C CG  . TYR G 1 62  ? 62.756  99.603  6.114   1.000 38.336  ? 380 TYR DDD CG  1 
ATOM   10179 C CD1 . TYR G 1 62  ? 61.641  99.335  5.327   1.000 38.505  ? 380 TYR DDD CD1 1 
ATOM   10180 C CD2 . TYR G 1 62  ? 63.964  99.057  5.707   1.000 38.843  ? 380 TYR DDD CD2 1 
ATOM   10181 C CE1 . TYR G 1 62  ? 61.723  98.534  4.194   1.000 40.777  ? 380 TYR DDD CE1 1 
ATOM   10182 C CE2 . TYR G 1 62  ? 64.068  98.251  4.581   1.000 40.685  ? 380 TYR DDD CE2 1 
ATOM   10183 C CZ  . TYR G 1 62  ? 62.944  97.984  3.818   1.000 44.027  ? 380 TYR DDD CZ  1 
ATOM   10184 O OH  . TYR G 1 62  ? 63.080  97.190  2.705   1.000 46.875  ? 380 TYR DDD OH  1 
ATOM   10185 N N   . GLY G 1 63  ? 62.682  100.412 10.836  1.000 46.503  ? 381 GLY DDD N   1 
ATOM   10186 C CA  . GLY G 1 63  ? 62.904  101.236 12.044  1.000 53.743  ? 381 GLY DDD CA  1 
ATOM   10187 C C   . GLY G 1 63  ? 61.683  101.351 12.950  1.000 56.582  ? 381 GLY DDD C   1 
ATOM   10188 O O   . GLY G 1 63  ? 61.773  102.007 14.004  1.000 56.827  ? 381 GLY DDD O   1 
ATOM   10189 N N   . VAL G 1 64  ? 60.556  100.742 12.605  1.000 59.601  ? 382 VAL DDD N   1 
ATOM   10190 C CA  . VAL G 1 64  ? 59.322  100.942 13.407  1.000 67.827  ? 382 VAL DDD CA  1 
ATOM   10191 C C   . VAL G 1 64  ? 58.343  99.797  13.132  1.000 71.560  ? 382 VAL DDD C   1 
ATOM   10192 O O   . VAL G 1 64  ? 58.341  99.281  11.993  1.000 80.992  ? 382 VAL DDD O   1 
ATOM   10193 C CB  . VAL G 1 64  ? 58.724  102.320 13.091  1.000 75.851  ? 382 VAL DDD CB  1 
ATOM   10194 C CG1 . VAL G 1 64  ? 58.066  102.338 11.717  1.000 78.119  ? 382 VAL DDD CG1 1 
ATOM   10195 C CG2 . VAL G 1 64  ? 57.747  102.760 14.171  1.000 81.077  ? 382 VAL DDD CG2 1 
ATOM   10196 N N   . SER G 1 65  ? 57.556  99.425  14.144  1.000 64.608  ? 383 SER DDD N   1 
ATOM   10197 C CA  . SER G 1 65  ? 56.668  98.237  14.149  1.000 64.028  ? 383 SER DDD CA  1 
ATOM   10198 C C   . SER G 1 65  ? 55.231  98.695  13.939  1.000 65.049  ? 383 SER DDD C   1 
ATOM   10199 O O   . SER G 1 65  ? 54.684  99.401  14.783  1.000 73.386  ? 383 SER DDD O   1 
ATOM   10200 C CB  . SER G 1 65  ? 56.792  97.486  15.438  1.000 65.188  ? 383 SER DDD CB  1 
ATOM   10201 O OG  . SER G 1 65  ? 58.145  97.217  15.770  1.000 68.997  ? 383 SER DDD OG  1 
ATOM   10202 N N   . PRO G 1 66  ? 54.567  98.326  12.823  1.000 61.831  ? 384 PRO DDD N   1 
ATOM   10203 C CA  . PRO G 1 66  ? 53.203  98.799  12.569  1.000 68.310  ? 384 PRO DDD CA  1 
ATOM   10204 C C   . PRO G 1 66  ? 52.229  98.375  13.680  1.000 78.110  ? 384 PRO DDD C   1 
ATOM   10205 O O   . PRO G 1 66  ? 51.240  99.066  13.916  1.000 79.987  ? 384 PRO DDD O   1 
ATOM   10206 C CB  . PRO G 1 66  ? 52.829  98.152  11.224  1.000 67.081  ? 384 PRO DDD CB  1 
ATOM   10207 C CG  . PRO G 1 66  ? 53.841  97.030  11.029  1.000 63.220  ? 384 PRO DDD CG  1 
ATOM   10208 C CD  . PRO G 1 66  ? 55.093  97.471  11.752  1.000 57.986  ? 384 PRO DDD CD  1 
ATOM   10209 N N   . THR G 1 67  ? 52.563  97.263  14.344  1.000 88.063  ? 385 THR DDD N   1 
ATOM   10210 C CA  . THR G 1 67  ? 51.776  96.604  15.414  1.000 88.197  ? 385 THR DDD CA  1 
ATOM   10211 C C   . THR G 1 67  ? 51.856  97.438  16.700  1.000 88.288  ? 385 THR DDD C   1 
ATOM   10212 O O   . THR G 1 67  ? 50.977  97.266  17.540  1.000 97.647  ? 385 THR DDD O   1 
ATOM   10213 C CB  . THR G 1 67  ? 52.237  95.148  15.599  1.000 89.112  ? 385 THR DDD CB  1 
ATOM   10214 O OG1 . THR G 1 67  ? 53.610  95.129  16.004  1.000 88.269  ? 385 THR DDD OG1 1 
ATOM   10215 C CG2 . THR G 1 67  ? 52.052  94.318  14.343  1.000 87.849  ? 385 THR DDD CG2 1 
ATOM   10216 N N   . LYS G 1 68  ? 52.835  98.336  16.833  1.000 92.865  ? 386 LYS DDD N   1 
ATOM   10217 C CA  . LYS G 1 68  ? 53.126  99.051  18.104  1.000 96.006  ? 386 LYS DDD CA  1 
ATOM   10218 C C   . LYS G 1 68  ? 53.002  100.571 17.948  1.000 95.602  ? 386 LYS DDD C   1 
ATOM   10219 O O   . LYS G 1 68  ? 53.540  101.263 18.821  1.000 93.646  ? 386 LYS DDD O   1 
ATOM   10220 C CB  . LYS G 1 68  ? 54.553  98.766  18.590  1.000 98.580  ? 386 LYS DDD CB  1 
ATOM   10221 C CG  . LYS G 1 68  ? 54.890  97.333  18.958  1.000 113.765 ? 386 LYS DDD CG  1 
ATOM   10222 C CD  . LYS G 1 68  ? 56.406  97.184  19.143  1.000 127.996 ? 386 LYS DDD CD  1 
ATOM   10223 C CE  . LYS G 1 68  ? 56.830  96.006  19.986  1.000 129.955 ? 386 LYS DDD CE  1 
ATOM   10224 N NZ  . LYS G 1 68  ? 56.283  96.138  21.352  1.000 134.523 ? 386 LYS DDD NZ  1 
ATOM   10225 N N   . LEU G 1 69  ? 52.338  101.104 16.919  1.000 97.169  ? 387 LEU DDD N   1 
ATOM   10226 C CA  . LEU G 1 69  ? 52.292  102.583 16.755  1.000 109.644 ? 387 LEU DDD CA  1 
ATOM   10227 C C   . LEU G 1 69  ? 50.852  103.095 16.660  1.000 130.124 ? 387 LEU DDD C   1 
ATOM   10228 O O   . LEU G 1 69  ? 50.706  104.318 16.450  1.000 157.644 ? 387 LEU DDD O   1 
ATOM   10229 C CB  . LEU G 1 69  ? 53.146  103.016 15.555  1.000 105.926 ? 387 LEU DDD CB  1 
ATOM   10230 C CG  . LEU G 1 69  ? 52.969  102.255 14.238  1.000 103.934 ? 387 LEU DDD CG  1 
ATOM   10231 C CD1 . LEU G 1 69  ? 51.649  102.598 13.555  1.000 102.403 ? 387 LEU DDD CD1 1 
ATOM   10232 C CD2 . LEU G 1 69  ? 54.134  102.558 13.304  1.000 102.457 ? 387 LEU DDD CD2 1 
ATOM   10233 N N   . ASN G 1 70  ? 49.842  102.234 16.864  1.000 134.432 ? 388 ASN DDD N   1 
ATOM   10234 C CA  . ASN G 1 70  ? 48.427  102.673 17.060  1.000 135.823 ? 388 ASN DDD CA  1 
ATOM   10235 C C   . ASN G 1 70  ? 48.231  102.964 18.558  1.000 134.389 ? 388 ASN DDD C   1 
ATOM   10236 O O   . ASN G 1 70  ? 47.062  103.039 19.026  1.000 156.496 ? 388 ASN DDD O   1 
ATOM   10237 C CB  . ASN G 1 70  ? 47.400  101.729 16.413  1.000 132.747 ? 388 ASN DDD CB  1 
ATOM   10238 C CG  . ASN G 1 70  ? 47.568  100.270 16.770  1.000 143.081 ? 388 ASN DDD CG  1 
ATOM   10239 O OD1 . ASN G 1 70  ? 47.221  99.852  17.871  1.000 160.033 ? 388 ASN DDD OD1 1 
ATOM   10240 N ND2 . ASN G 1 70  ? 48.077  99.486  15.837  1.000 150.403 ? 388 ASN DDD ND2 1 
ATOM   10241 N N   . ASP G 1 71  ? 49.347  103.147 19.277  1.000 120.264 ? 389 ASP DDD N   1 
ATOM   10242 C CA  . ASP G 1 71  ? 49.417  103.829 20.596  1.000 122.650 ? 389 ASP DDD CA  1 
ATOM   10243 C C   . ASP G 1 71  ? 50.659  104.741 20.666  1.000 116.017 ? 389 ASP DDD C   1 
ATOM   10244 O O   . ASP G 1 71  ? 51.156  104.980 21.786  1.000 113.119 ? 389 ASP DDD O   1 
ATOM   10245 C CB  . ASP G 1 71  ? 49.462  102.804 21.727  1.000 125.730 ? 389 ASP DDD CB  1 
ATOM   10246 C CG  . ASP G 1 71  ? 50.850  102.232 21.896  1.000 136.516 ? 389 ASP DDD CG  1 
ATOM   10247 O OD1 . ASP G 1 71  ? 51.384  102.336 23.009  1.000 166.020 ? 389 ASP DDD OD1 1 
ATOM   10248 O OD2 . ASP G 1 71  ? 51.396  101.734 20.899  1.000 127.282 ? 389 ASP DDD OD2 1 
ATOM   10249 N N   . LEU G 1 72  ? 51.161  105.248 19.536  1.000 110.512 ? 390 LEU DDD N   1 
ATOM   10250 C CA  . LEU G 1 72  ? 52.209  106.305 19.540  1.000 109.365 ? 390 LEU DDD CA  1 
ATOM   10251 C C   . LEU G 1 72  ? 51.801  107.496 18.655  1.000 120.419 ? 390 LEU DDD C   1 
ATOM   10252 O O   . LEU G 1 72  ? 50.883  107.342 17.785  1.000 128.034 ? 390 LEU DDD O   1 
ATOM   10253 C CB  . LEU G 1 72  ? 53.559  105.719 19.121  1.000 101.718 ? 390 LEU DDD CB  1 
ATOM   10254 C CG  . LEU G 1 72  ? 54.753  106.382 19.812  1.000 103.676 ? 390 LEU DDD CG  1 
ATOM   10255 C CD1 . LEU G 1 72  ? 54.710  106.164 21.322  1.000 100.577 ? 390 LEU DDD CD1 1 
ATOM   10256 C CD2 . LEU G 1 72  ? 56.070  105.890 19.234  1.000 106.235 ? 390 LEU DDD CD2 1 
ATOM   10257 N N   . CYS G 1 73  ? 52.435  108.650 18.924  1.000 116.664 ? 391 CYS DDD N   1 
ATOM   10258 C CA  . CYS G 1 73  ? 52.175  109.980 18.310  1.000 116.420 ? 391 CYS DDD CA  1 
ATOM   10259 C C   . CYS G 1 73  ? 53.438  110.518 17.632  1.000 104.906 ? 391 CYS DDD C   1 
ATOM   10260 O O   . CYS G 1 73  ? 54.548  110.294 18.168  1.000 91.921  ? 391 CYS DDD O   1 
ATOM   10261 C CB  . CYS G 1 73  ? 51.703  110.997 19.345  1.000 132.728 ? 391 CYS DDD CB  1 
ATOM   10262 S SG  . CYS G 1 73  ? 50.092  110.595 20.074  1.000 163.533 ? 391 CYS DDD SG  1 
ATOM   10263 N N   . PHE G 1 74  ? 53.249  111.224 16.510  1.000 108.024 ? 392 PHE DDD N   1 
ATOM   10264 C CA  . PHE G 1 74  ? 54.305  111.778 15.621  1.000 115.419 ? 392 PHE DDD CA  1 
ATOM   10265 C C   . PHE G 1 74  ? 53.899  113.190 15.155  1.000 116.998 ? 392 PHE DDD C   1 
ATOM   10266 O O   . PHE G 1 74  ? 52.669  113.439 15.047  1.000 120.228 ? 392 PHE DDD O   1 
ATOM   10267 C CB  . PHE G 1 74  ? 54.510  110.857 14.411  1.000 120.935 ? 392 PHE DDD CB  1 
ATOM   10268 C CG  . PHE G 1 74  ? 54.858  109.417 14.708  1.000 117.638 ? 392 PHE DDD CG  1 
ATOM   10269 C CD1 . PHE G 1 74  ? 53.866  108.449 14.779  1.000 113.586 ? 392 PHE DDD CD1 1 
ATOM   10270 C CD2 . PHE G 1 74  ? 56.180  109.024 14.893  1.000 117.603 ? 392 PHE DDD CD2 1 
ATOM   10271 C CE1 . PHE G 1 74  ? 54.188  107.127 15.048  1.000 115.296 ? 392 PHE DDD CE1 1 
ATOM   10272 C CE2 . PHE G 1 74  ? 56.498  107.703 15.167  1.000 111.469 ? 392 PHE DDD CE2 1 
ATOM   10273 C CZ  . PHE G 1 74  ? 55.502  106.756 15.235  1.000 114.406 ? 392 PHE DDD CZ  1 
ATOM   10274 N N   . THR G 1 75  ? 54.879  114.072 14.878  1.000 106.740 ? 393 THR DDD N   1 
ATOM   10275 C CA  . THR G 1 75  ? 54.672  115.461 14.361  1.000 99.546  ? 393 THR DDD CA  1 
ATOM   10276 C C   . THR G 1 75  ? 54.044  115.410 12.966  1.000 93.069  ? 393 THR DDD C   1 
ATOM   10277 O O   . THR G 1 75  ? 53.067  116.135 12.730  1.000 80.748  ? 393 THR DDD O   1 
ATOM   10278 C CB  . THR G 1 75  ? 55.971  116.277 14.277  1.000 100.093 ? 393 THR DDD CB  1 
ATOM   10279 O OG1 . THR G 1 75  ? 56.984  115.451 13.698  1.000 107.798 ? 393 THR DDD OG1 1 
ATOM   10280 C CG2 . THR G 1 75  ? 56.427  116.812 15.618  1.000 104.733 ? 393 THR DDD CG2 1 
ATOM   10281 N N   . ASN G 1 76  ? 54.593  114.577 12.083  1.000 98.931  ? 394 ASN DDD N   1 
ATOM   10282 C CA  . ASN G 1 76  ? 54.073  114.413 10.703  1.000 94.243  ? 394 ASN DDD CA  1 
ATOM   10283 C C   . ASN G 1 76  ? 54.266  112.983 10.207  1.000 78.891  ? 394 ASN DDD C   1 
ATOM   10284 O O   . ASN G 1 76  ? 55.327  112.355 10.472  1.000 71.824  ? 394 ASN DDD O   1 
ATOM   10285 C CB  . ASN G 1 76  ? 54.720  115.401 9.737   1.000 101.618 ? 394 ASN DDD CB  1 
ATOM   10286 C CG  . ASN G 1 76  ? 54.024  116.741 9.764   1.000 104.216 ? 394 ASN DDD CG  1 
ATOM   10287 O OD1 . ASN G 1 76  ? 52.894  116.871 9.303   1.000 128.808 ? 394 ASN DDD OD1 1 
ATOM   10288 N ND2 . ASN G 1 76  ? 54.693  117.728 10.324  1.000 91.924  ? 394 ASN DDD ND2 1 
ATOM   10289 N N   . VAL G 1 77  ? 53.257  112.529 9.476   1.000 71.356  ? 395 VAL DDD N   1 
ATOM   10290 C CA  . VAL G 1 77  ? 53.251  111.251 8.721   1.000 76.675  ? 395 VAL DDD CA  1 
ATOM   10291 C C   . VAL G 1 77  ? 53.004  111.594 7.253   1.000 72.839  ? 395 VAL DDD C   1 
ATOM   10292 O O   . VAL G 1 77  ? 52.085  112.386 6.994   1.000 80.156  ? 395 VAL DDD O   1 
ATOM   10293 C CB  . VAL G 1 77  ? 52.178  110.304 9.287   1.000 75.113  ? 395 VAL DDD CB  1 
ATOM   10294 C CG1 . VAL G 1 77  ? 52.080  109.009 8.494   1.000 76.155  ? 395 VAL DDD CG1 1 
ATOM   10295 C CG2 . VAL G 1 77  ? 52.434  110.015 10.756  1.000 75.806  ? 395 VAL DDD CG2 1 
ATOM   10296 N N   . TYR G 1 78  ? 53.803  111.034 6.346   1.000 66.614  ? 396 TYR DDD N   1 
ATOM   10297 C CA  . TYR G 1 78  ? 53.683  111.242 4.882   1.000 61.628  ? 396 TYR DDD CA  1 
ATOM   10298 C C   . TYR G 1 78  ? 53.357  109.897 4.220   1.000 58.011  ? 396 TYR DDD C   1 
ATOM   10299 O O   . TYR G 1 78  ? 54.014  108.888 4.553   1.000 60.697  ? 396 TYR DDD O   1 
ATOM   10300 C CB  . TYR G 1 78  ? 54.964  111.871 4.323   1.000 64.149  ? 396 TYR DDD CB  1 
ATOM   10301 C CG  . TYR G 1 78  ? 55.385  113.175 4.956   1.000 67.125  ? 396 TYR DDD CG  1 
ATOM   10302 C CD1 . TYR G 1 78  ? 54.592  114.312 4.859   1.000 72.044  ? 396 TYR DDD CD1 1 
ATOM   10303 C CD2 . TYR G 1 78  ? 56.600  113.287 5.623   1.000 68.059  ? 396 TYR DDD CD2 1 
ATOM   10304 C CE1 . TYR G 1 78  ? 54.975  115.512 5.442   1.000 71.545  ? 396 TYR DDD CE1 1 
ATOM   10305 C CE2 . TYR G 1 78  ? 56.999  114.481 6.207   1.000 67.154  ? 396 TYR DDD CE2 1 
ATOM   10306 C CZ  . TYR G 1 78  ? 56.185  115.596 6.112   1.000 66.426  ? 396 TYR DDD CZ  1 
ATOM   10307 O OH  . TYR G 1 78  ? 56.580  116.770 6.678   1.000 68.003  ? 396 TYR DDD OH  1 
ATOM   10308 N N   . ALA G 1 79  ? 52.382  109.893 3.306   1.000 52.494  ? 397 ALA DDD N   1 
ATOM   10309 C CA  . ALA G 1 79  ? 51.932  108.720 2.518   1.000 50.970  ? 397 ALA DDD CA  1 
ATOM   10310 C C   . ALA G 1 79  ? 52.200  108.956 1.022   1.000 47.111  ? 397 ALA DDD C   1 
ATOM   10311 O O   . ALA G 1 79  ? 51.332  109.563 0.318   1.000 45.506  ? 397 ALA DDD O   1 
ATOM   10312 C CB  . ALA G 1 79  ? 50.469  108.458 2.798   1.000 50.946  ? 397 ALA DDD CB  1 
ATOM   10313 N N   . ASP G 1 80  ? 53.350  108.471 0.545   1.000 41.819  ? 398 ASP DDD N   1 
ATOM   10314 C CA  . ASP G 1 80  ? 53.798  108.612 -0.864  1.000 41.688  ? 398 ASP DDD CA  1 
ATOM   10315 C C   . ASP G 1 80  ? 53.218  107.442 -1.657  1.000 42.132  ? 398 ASP DDD C   1 
ATOM   10316 O O   . ASP G 1 80  ? 53.403  106.311 -1.233  1.000 52.500  ? 398 ASP DDD O   1 
ATOM   10317 C CB  . ASP G 1 80  ? 55.322  108.679 -0.958  1.000 41.742  ? 398 ASP DDD CB  1 
ATOM   10318 C CG  . ASP G 1 80  ? 55.916  109.719 -0.026  1.000 45.869  ? 398 ASP DDD CG  1 
ATOM   10319 O OD1 . ASP G 1 80  ? 55.161  110.633 0.337   1.000 44.801  ? 398 ASP DDD OD1 1 
ATOM   10320 O OD2 . ASP G 1 80  ? 57.109  109.579 0.371   1.000 49.571  ? 398 ASP DDD OD2 1 
ATOM   10321 N N   . SER G 1 81  ? 52.508  107.710 -2.745  1.000 39.007  ? 399 SER DDD N   1 
ATOM   10322 C CA  . SER G 1 81  ? 51.831  106.690 -3.577  1.000 39.205  ? 399 SER DDD CA  1 
ATOM   10323 C C   . SER G 1 81  ? 52.350  106.801 -5.004  1.000 35.664  ? 399 SER DDD C   1 
ATOM   10324 O O   . SER G 1 81  ? 52.554  107.895 -5.452  1.000 37.452  ? 399 SER DDD O   1 
ATOM   10325 C CB  . SER G 1 81  ? 50.320  106.835 -3.512  1.000 44.724  ? 399 SER DDD CB  1 
ATOM   10326 O OG  . SER G 1 81  ? 49.900  108.190 -3.567  1.000 49.545  ? 399 SER DDD OG  1 
ATOM   10327 N N   . PHE G 1 82  ? 52.542  105.691 -5.694  1.000 36.075  ? 400 PHE DDD N   1 
ATOM   10328 C CA  . PHE G 1 82  ? 52.923  105.686 -7.131  1.000 37.302  ? 400 PHE DDD CA  1 
ATOM   10329 C C   . PHE G 1 82  ? 52.747  104.281 -7.703  1.000 34.541  ? 400 PHE DDD C   1 
ATOM   10330 O O   . PHE G 1 82  ? 52.252  103.450 -6.963  1.000 38.275  ? 400 PHE DDD O   1 
ATOM   10331 C CB  . PHE G 1 82  ? 54.355  106.182 -7.284  1.000 37.946  ? 400 PHE DDD CB  1 
ATOM   10332 C CG  . PHE G 1 82  ? 55.350  105.499 -6.386  1.000 39.115  ? 400 PHE DDD CG  1 
ATOM   10333 C CD1 . PHE G 1 82  ? 55.934  104.304 -6.759  1.000 37.880  ? 400 PHE DDD CD1 1 
ATOM   10334 C CD2 . PHE G 1 82  ? 55.727  106.077 -5.183  1.000 41.026  ? 400 PHE DDD CD2 1 
ATOM   10335 C CE1 . PHE G 1 82  ? 56.897  103.717 -5.953  1.000 40.534  ? 400 PHE DDD CE1 1 
ATOM   10336 C CE2 . PHE G 1 82  ? 56.699  105.494 -4.386  1.000 41.654  ? 400 PHE DDD CE2 1 
ATOM   10337 C CZ  . PHE G 1 82  ? 57.277  104.310 -4.768  1.000 39.675  ? 400 PHE DDD CZ  1 
ATOM   10338 N N   . VAL G 1 83  ? 53.120  104.049 -8.962  1.000 31.051  ? 401 VAL DDD N   1 
ATOM   10339 C CA  . VAL G 1 83  ? 53.020  102.719 -9.626  1.000 31.562  ? 401 VAL DDD CA  1 
ATOM   10340 C C   . VAL G 1 83  ? 54.329  102.399 -10.336 1.000 33.775  ? 401 VAL DDD C   1 
ATOM   10341 O O   . VAL G 1 83  ? 54.841  103.261 -11.076 1.000 39.382  ? 401 VAL DDD O   1 
ATOM   10342 C CB  . VAL G 1 83  ? 51.852  102.653 -10.617 1.000 30.953  ? 401 VAL DDD CB  1 
ATOM   10343 C CG1 . VAL G 1 83  ? 51.932  101.416 -11.490 1.000 30.231  ? 401 VAL DDD CG1 1 
ATOM   10344 C CG2 . VAL G 1 83  ? 50.515  102.730 -9.910  1.000 32.384  ? 401 VAL DDD CG2 1 
ATOM   10345 N N   . ILE G 1 84  ? 54.787  101.166 -10.145 1.000 37.052  ? 402 ILE DDD N   1 
ATOM   10346 C CA  . ILE G 1 84  ? 55.984  100.558 -10.788 1.000 42.942  ? 402 ILE DDD CA  1 
ATOM   10347 C C   . ILE G 1 84  ? 55.655  99.098  -11.114 1.000 45.363  ? 402 ILE DDD C   1 
ATOM   10348 O O   . ILE G 1 84  ? 54.516  98.673  -10.827 1.000 44.798  ? 402 ILE DDD O   1 
ATOM   10349 C CB  . ILE G 1 84  ? 57.197  100.680 -9.851  1.000 47.691  ? 402 ILE DDD CB  1 
ATOM   10350 C CG1 . ILE G 1 84  ? 56.847  100.265 -8.421  1.000 48.645  ? 402 ILE DDD CG1 1 
ATOM   10351 C CG2 . ILE G 1 84  ? 57.761  102.085 -9.891  1.000 48.675  ? 402 ILE DDD CG2 1 
ATOM   10352 C CD1 . ILE G 1 84  ? 58.054  100.019 -7.542  1.000 48.403  ? 402 ILE DDD CD1 1 
ATOM   10353 N N   . ARG G 1 85  ? 56.611  98.357  -11.679 1.000 48.005  ? 403 ARG DDD N   1 
ATOM   10354 C CA  . ARG G 1 85  ? 56.422  96.915  -11.989 1.000 49.090  ? 403 ARG DDD CA  1 
ATOM   10355 C C   . ARG G 1 85  ? 57.050  96.097  -10.863 1.000 49.443  ? 403 ARG DDD C   1 
ATOM   10356 O O   . ARG G 1 85  ? 57.898  96.648  -10.136 1.000 51.512  ? 403 ARG DDD O   1 
ATOM   10357 C CB  . ARG G 1 85  ? 56.973  96.579  -13.377 1.000 49.409  ? 403 ARG DDD CB  1 
ATOM   10358 C CG  . ARG G 1 85  ? 58.479  96.731  -13.525 1.000 50.002  ? 403 ARG DDD CG  1 
ATOM   10359 C CD  . ARG G 1 85  ? 58.922  96.551  -14.967 1.000 52.439  ? 403 ARG DDD CD  1 
ATOM   10360 N NE  . ARG G 1 85  ? 60.359  96.723  -15.100 1.000 55.800  ? 403 ARG DDD NE  1 
ATOM   10361 C CZ  . ARG G 1 85  ? 61.266  95.739  -15.186 1.000 69.359  ? 403 ARG DDD CZ  1 
ATOM   10362 N NH1 . ARG G 1 85  ? 60.923  94.460  -15.189 1.000 70.351  ? 403 ARG DDD NH1 1 
ATOM   10363 N NH2 . ARG G 1 85  ? 62.544  96.045  -15.301 1.000 81.641  ? 403 ARG DDD NH2 1 
ATOM   10364 N N   . GLY G 1 86  ? 56.615  94.846  -10.715 1.000 48.845  ? 404 GLY DDD N   1 
ATOM   10365 C CA  . GLY G 1 86  ? 56.976  93.952  -9.596  1.000 49.558  ? 404 GLY DDD CA  1 
ATOM   10366 C C   . GLY G 1 86  ? 58.479  93.824  -9.414  1.000 48.687  ? 404 GLY DDD C   1 
ATOM   10367 O O   . GLY G 1 86  ? 58.921  93.870  -8.250  1.000 52.148  ? 404 GLY DDD O   1 
ATOM   10368 N N   . ASP G 1 87  ? 59.242  93.686  -10.504 1.000 47.443  ? 405 ASP DDD N   1 
ATOM   10369 C CA  . ASP G 1 87  ? 60.726  93.559  -10.468 1.000 54.561  ? 405 ASP DDD CA  1 
ATOM   10370 C C   . ASP G 1 87  ? 61.352  94.725  -9.689  1.000 54.635  ? 405 ASP DDD C   1 
ATOM   10371 O O   . ASP G 1 87  ? 62.513  94.608  -9.271  1.000 52.648  ? 405 ASP DDD O   1 
ATOM   10372 C CB  . ASP G 1 87  ? 61.340  93.570  -11.871 1.000 63.022  ? 405 ASP DDD CB  1 
ATOM   10373 C CG  . ASP G 1 87  ? 61.275  92.239  -12.598 1.000 72.128  ? 405 ASP DDD CG  1 
ATOM   10374 O OD1 . ASP G 1 87  ? 62.323  91.583  -12.726 1.000 89.289  ? 405 ASP DDD OD1 1 
ATOM   10375 O OD2 . ASP G 1 87  ? 60.182  91.880  -13.055 1.000 74.797  ? 405 ASP DDD OD2 1 
ATOM   10376 N N   . GLU G 1 88  ? 60.625  95.836  -9.558  1.000 57.943  ? 406 GLU DDD N   1 
ATOM   10377 C CA  . GLU G 1 88  ? 61.144  97.145  -9.082  1.000 55.426  ? 406 GLU DDD CA  1 
ATOM   10378 C C   . GLU G 1 88  ? 60.691  97.407  -7.633  1.000 48.650  ? 406 GLU DDD C   1 
ATOM   10379 O O   . GLU G 1 88  ? 61.254  98.329  -7.020  1.000 47.203  ? 406 GLU DDD O   1 
ATOM   10380 C CB  . GLU G 1 88  ? 60.715  98.255  -10.058 1.000 56.952  ? 406 GLU DDD CB  1 
ATOM   10381 C CG  . GLU G 1 88  ? 61.492  98.247  -11.379 1.000 56.565  ? 406 GLU DDD CG  1 
ATOM   10382 C CD  . GLU G 1 88  ? 61.018  99.236  -12.432 1.000 54.757  ? 406 GLU DDD CD  1 
ATOM   10383 O OE1 . GLU G 1 88  ? 59.910  99.787  -12.244 1.000 53.835  ? 406 GLU DDD OE1 1 
ATOM   10384 O OE2 . GLU G 1 88  ? 61.752  99.449  -13.437 1.000 49.980  ? 406 GLU DDD OE2 1 
ATOM   10385 N N   . VAL G 1 89  ? 59.763  96.633  -7.064  1.000 40.201  ? 407 VAL DDD N   1 
ATOM   10386 C CA  . VAL G 1 89  ? 59.278  96.932  -5.685  1.000 38.071  ? 407 VAL DDD CA  1 
ATOM   10387 C C   . VAL G 1 89  ? 60.419  96.711  -4.702  1.000 41.522  ? 407 VAL DDD C   1 
ATOM   10388 O O   . VAL G 1 89  ? 60.450  97.435  -3.701  1.000 40.395  ? 407 VAL DDD O   1 
ATOM   10389 C CB  . VAL G 1 89  ? 58.044  96.125  -5.265  1.000 36.509  ? 407 VAL DDD CB  1 
ATOM   10390 C CG1 . VAL G 1 89  ? 57.570  96.545  -3.883  1.000 34.388  ? 407 VAL DDD CG1 1 
ATOM   10391 C CG2 . VAL G 1 89  ? 56.915  96.251  -6.274  1.000 38.844  ? 407 VAL DDD CG2 1 
ATOM   10392 N N   . ARG G 1 90  ? 61.303  95.746  -4.974  1.000 50.228  ? 408 ARG DDD N   1 
ATOM   10393 C CA  . ARG G 1 90  ? 62.529  95.498  -4.164  1.000 58.716  ? 408 ARG DDD CA  1 
ATOM   10394 C C   . ARG G 1 90  ? 63.351  96.795  -4.043  1.000 56.890  ? 408 ARG DDD C   1 
ATOM   10395 O O   . ARG G 1 90  ? 64.062  96.952  -3.028  1.000 56.061  ? 408 ARG DDD O   1 
ATOM   10396 C CB  . ARG G 1 90  ? 63.378  94.382  -4.788  1.000 73.486  ? 408 ARG DDD CB  1 
ATOM   10397 C CG  . ARG G 1 90  ? 63.848  94.664  -6.214  1.000 93.661  ? 408 ARG DDD CG  1 
ATOM   10398 C CD  . ARG G 1 90  ? 65.172  94.012  -6.603  1.000 101.624 ? 408 ARG DDD CD  1 
ATOM   10399 N NE  . ARG G 1 90  ? 65.325  92.678  -6.028  1.000 118.335 ? 408 ARG DDD NE  1 
ATOM   10400 C CZ  . ARG G 1 90  ? 64.663  91.577  -6.404  1.000 122.263 ? 408 ARG DDD CZ  1 
ATOM   10401 N NH1 . ARG G 1 90  ? 64.896  90.429  -5.788  1.000 123.177 ? 408 ARG DDD NH1 1 
ATOM   10402 N NH2 . ARG G 1 90  ? 63.778  91.610  -7.384  1.000 117.756 ? 408 ARG DDD NH2 1 
ATOM   10403 N N   . GLN G 1 91  ? 63.271  97.674  -5.053  1.000 53.910  ? 409 GLN DDD N   1 
ATOM   10404 C CA  . GLN G 1 91  ? 64.087  98.910  -5.182  1.000 49.983  ? 409 GLN DDD CA  1 
ATOM   10405 C C   . GLN G 1 91  ? 63.528  100.007 -4.268  1.000 47.613  ? 409 GLN DDD C   1 
ATOM   10406 O O   . GLN G 1 91  ? 64.268  100.942 -3.996  1.000 54.150  ? 409 GLN DDD O   1 
ATOM   10407 C CB  . GLN G 1 91  ? 64.115  99.398  -6.632  1.000 49.658  ? 409 GLN DDD CB  1 
ATOM   10408 C CG  . GLN G 1 91  ? 65.384  99.057  -7.391  1.000 51.613  ? 409 GLN DDD CG  1 
ATOM   10409 C CD  . GLN G 1 91  ? 65.341  99.609  -8.800  1.000 56.438  ? 409 GLN DDD CD  1 
ATOM   10410 O OE1 . GLN G 1 91  ? 65.669  100.770 -9.075  1.000 58.684  ? 409 GLN DDD OE1 1 
ATOM   10411 N NE2 . GLN G 1 91  ? 64.912  98.761  -9.721  1.000 64.671  ? 409 GLN DDD NE2 1 
ATOM   10412 N N   . ILE G 1 92  ? 62.279  99.917  -3.815  1.000 43.112  ? 410 ILE DDD N   1 
ATOM   10413 C CA  . ILE G 1 92  ? 61.677  100.938 -2.910  1.000 41.860  ? 410 ILE DDD CA  1 
ATOM   10414 C C   . ILE G 1 92  ? 62.084  100.600 -1.484  1.000 39.406  ? 410 ILE DDD C   1 
ATOM   10415 O O   . ILE G 1 92  ? 61.220  100.152 -0.726  1.000 39.065  ? 410 ILE DDD O   1 
ATOM   10416 C CB  . ILE G 1 92  ? 60.148  100.976 -3.056  1.000 44.763  ? 410 ILE DDD CB  1 
ATOM   10417 C CG1 . ILE G 1 92  ? 59.742  101.114 -4.521  1.000 46.924  ? 410 ILE DDD CG1 1 
ATOM   10418 C CG2 . ILE G 1 92  ? 59.535  102.074 -2.199  1.000 46.031  ? 410 ILE DDD CG2 1 
ATOM   10419 C CD1 . ILE G 1 92  ? 60.413  102.257 -5.239  1.000 47.998  ? 410 ILE DDD CD1 1 
ATOM   10420 N N   . ALA G 1 93  ? 63.354  100.805 -1.144  1.000 38.848  ? 411 ALA DDD N   1 
ATOM   10421 C CA  . ALA G 1 93  ? 63.925  100.427 0.168   1.000 41.602  ? 411 ALA DDD CA  1 
ATOM   10422 C C   . ALA G 1 93  ? 65.221  101.175 0.423   1.000 42.372  ? 411 ALA DDD C   1 
ATOM   10423 O O   . ALA G 1 93  ? 66.009  101.372 -0.495  1.000 45.331  ? 411 ALA DDD O   1 
ATOM   10424 C CB  . ALA G 1 93  ? 64.176  98.941  0.211   1.000 46.698  ? 411 ALA DDD CB  1 
ATOM   10425 N N   . PRO G 1 94  ? 65.524  101.542 1.684   1.000 43.424  ? 412 PRO DDD N   1 
ATOM   10426 C CA  . PRO G 1 94  ? 66.803  102.167 2.003   1.000 45.361  ? 412 PRO DDD CA  1 
ATOM   10427 C C   . PRO G 1 94  ? 67.967  101.404 1.369   1.000 42.128  ? 412 PRO DDD C   1 
ATOM   10428 O O   . PRO G 1 94  ? 67.926  100.206 1.370   1.000 44.626  ? 412 PRO DDD O   1 
ATOM   10429 C CB  . PRO G 1 94  ? 66.888  102.110 3.533   1.000 46.350  ? 412 PRO DDD CB  1 
ATOM   10430 C CG  . PRO G 1 94  ? 65.767  101.186 3.940   1.000 45.297  ? 412 PRO DDD CG  1 
ATOM   10431 C CD  . PRO G 1 94  ? 64.701  101.345 2.879   1.000 43.060  ? 412 PRO DDD CD  1 
ATOM   10432 N N   . GLY G 1 95  ? 68.919  102.142 0.807   1.000 42.658  ? 413 GLY DDD N   1 
ATOM   10433 C CA  . GLY G 1 95  ? 70.221  101.641 0.341   1.000 46.095  ? 413 GLY DDD CA  1 
ATOM   10434 C C   . GLY G 1 95  ? 70.156  100.841 -0.952  1.000 48.188  ? 413 GLY DDD C   1 
ATOM   10435 O O   . GLY G 1 95  ? 71.122  100.119 -1.213  1.000 58.242  ? 413 GLY DDD O   1 
ATOM   10436 N N   . GLN G 1 96  ? 69.104  100.976 -1.759  1.000 47.061  ? 414 GLN DDD N   1 
ATOM   10437 C CA  . GLN G 1 96  ? 68.987  100.290 -3.077  1.000 47.687  ? 414 GLN DDD CA  1 
ATOM   10438 C C   . GLN G 1 96  ? 69.622  101.154 -4.178  1.000 47.265  ? 414 GLN DDD C   1 
ATOM   10439 O O   . GLN G 1 96  ? 70.009  102.315 -3.885  1.000 41.495  ? 414 GLN DDD O   1 
ATOM   10440 C CB  . GLN G 1 96  ? 67.519  100.023 -3.387  1.000 50.834  ? 414 GLN DDD CB  1 
ATOM   10441 C CG  . GLN G 1 96  ? 66.883  99.059  -2.410  1.000 55.164  ? 414 GLN DDD CG  1 
ATOM   10442 C CD  . GLN G 1 96  ? 67.408  97.666  -2.594  1.000 58.008  ? 414 GLN DDD CD  1 
ATOM   10443 O OE1 . GLN G 1 96  ? 67.509  97.168  -3.716  1.000 63.031  ? 414 GLN DDD OE1 1 
ATOM   10444 N NE2 . GLN G 1 96  ? 67.751  97.042  -1.480  1.000 60.920  ? 414 GLN DDD NE2 1 
ATOM   10445 N N   . THR G 1 97  ? 69.751  100.598 -5.390  1.000 48.475  ? 415 THR DDD N   1 
ATOM   10446 C CA  . THR G 1 97  ? 70.203  101.324 -6.608  1.000 50.352  ? 415 THR DDD CA  1 
ATOM   10447 C C   . THR G 1 97  ? 69.440  100.769 -7.820  1.000 49.068  ? 415 THR DDD C   1 
ATOM   10448 O O   . THR G 1 97  ? 68.854  99.671  -7.685  1.000 48.786  ? 415 THR DDD O   1 
ATOM   10449 C CB  . THR G 1 97  ? 71.732  101.267 -6.789  1.000 50.760  ? 415 THR DDD CB  1 
ATOM   10450 O OG1 . THR G 1 97  ? 72.025  99.984  -7.328  1.000 52.315  ? 415 THR DDD OG1 1 
ATOM   10451 C CG2 . THR G 1 97  ? 72.542  101.468 -5.522  1.000 49.147  ? 415 THR DDD CG2 1 
ATOM   10452 N N   . GLY G 1 98  ? 69.443  101.515 -8.936  1.000 49.986  ? 416 GLY DDD N   1 
ATOM   10453 C CA  . GLY G 1 98  ? 68.751  101.169 -10.194 1.000 54.837  ? 416 GLY DDD CA  1 
ATOM   10454 C C   . GLY G 1 98  ? 67.993  102.356 -10.751 1.000 54.647  ? 416 GLY DDD C   1 
ATOM   10455 O O   . GLY G 1 98  ? 68.174  103.453 -10.217 1.000 60.735  ? 416 GLY DDD O   1 
ATOM   10456 N N   . LYS G 1 99  ? 67.182  102.140 -11.789 1.000 55.266  ? 417 LYS DDD N   1 
ATOM   10457 C CA  . LYS G 1 99  ? 66.367  103.194 -12.448 1.000 56.518  ? 417 LYS DDD CA  1 
ATOM   10458 C C   . LYS G 1 99  ? 65.514  103.869 -11.381 1.000 51.292  ? 417 LYS DDD C   1 
ATOM   10459 O O   . LYS G 1 99  ? 65.558  105.102 -11.302 1.000 55.275  ? 417 LYS DDD O   1 
ATOM   10460 C CB  . LYS G 1 99  ? 65.425  102.644 -13.527 1.000 70.568  ? 417 LYS DDD CB  1 
ATOM   10461 C CG  . LYS G 1 99  ? 66.091  102.004 -14.740 1.000 89.673  ? 417 LYS DDD CG  1 
ATOM   10462 C CD  . LYS G 1 99  ? 67.250  102.818 -15.305 1.000 104.934 ? 417 LYS DDD CD  1 
ATOM   10463 C CE  . LYS G 1 99  ? 68.040  102.095 -16.378 1.000 113.398 ? 417 LYS DDD CE  1 
ATOM   10464 N NZ  . LYS G 1 99  ? 69.113  102.964 -16.924 1.000 113.720 ? 417 LYS DDD NZ  1 
ATOM   10465 N N   . ILE G 1 100 ? 64.764  103.097 -10.597 1.000 44.381  ? 418 ILE DDD N   1 
ATOM   10466 C CA  . ILE G 1 100 ? 63.690  103.655 -9.729  1.000 42.051  ? 418 ILE DDD CA  1 
ATOM   10467 C C   . ILE G 1 100 ? 64.302  104.283 -8.487  1.000 43.174  ? 418 ILE DDD C   1 
ATOM   10468 O O   . ILE G 1 100 ? 63.878  105.371 -8.094  1.000 50.237  ? 418 ILE DDD O   1 
ATOM   10469 C CB  . ILE G 1 100 ? 62.678  102.577 -9.336  1.000 40.830  ? 418 ILE DDD CB  1 
ATOM   10470 C CG1 . ILE G 1 100 ? 62.112  101.877 -10.572 1.000 45.109  ? 418 ILE DDD CG1 1 
ATOM   10471 C CG2 . ILE G 1 100 ? 61.588  103.170 -8.470  1.000 38.613  ? 418 ILE DDD CG2 1 
ATOM   10472 C CD1 . ILE G 1 100 ? 61.643  102.828 -11.647 1.000 48.118  ? 418 ILE DDD CD1 1 
ATOM   10473 N N   . ALA G 1 101 ? 65.234  103.585 -7.866  1.000 44.699  ? 419 ALA DDD N   1 
ATOM   10474 C CA  . ALA G 1 101 ? 65.860  104.028 -6.612  1.000 46.616  ? 419 ALA DDD CA  1 
ATOM   10475 C C   . ALA G 1 101 ? 66.641  105.315 -6.869  1.000 47.018  ? 419 ALA DDD C   1 
ATOM   10476 O O   . ALA G 1 101 ? 66.620  106.182 -5.995  1.000 54.418  ? 419 ALA DDD O   1 
ATOM   10477 C CB  . ALA G 1 101 ? 66.755  102.941 -6.088  1.000 53.519  ? 419 ALA DDD CB  1 
ATOM   10478 N N   . ASP G 1 102 ? 67.300  105.436 -8.017  1.000 45.059  ? 420 ASP DDD N   1 
ATOM   10479 C CA  . ASP G 1 102 ? 68.291  106.519 -8.225  1.000 49.614  ? 420 ASP DDD CA  1 
ATOM   10480 C C   . ASP G 1 102 ? 67.660  107.718 -8.935  1.000 45.341  ? 420 ASP DDD C   1 
ATOM   10481 O O   . ASP G 1 102 ? 68.096  108.840 -8.640  1.000 46.739  ? 420 ASP DDD O   1 
ATOM   10482 C CB  . ASP G 1 102 ? 69.522  105.993 -8.960  1.000 55.721  ? 420 ASP DDD CB  1 
ATOM   10483 C CG  . ASP G 1 102 ? 70.357  105.086 -8.080  1.000 59.174  ? 420 ASP DDD CG  1 
ATOM   10484 O OD1 . ASP G 1 102 ? 69.992  104.948 -6.900  1.000 54.651  ? 420 ASP DDD OD1 1 
ATOM   10485 O OD2 . ASP G 1 102 ? 71.362  104.536 -8.579  1.000 66.338  ? 420 ASP DDD OD2 1 
ATOM   10486 N N   . TYR G 1 103 ? 66.689  107.501 -9.825  1.000 42.237  ? 421 TYR DDD N   1 
ATOM   10487 C CA  . TYR G 1 103 ? 66.204  108.546 -10.769 1.000 40.683  ? 421 TYR DDD CA  1 
ATOM   10488 C C   . TYR G 1 103 ? 64.717  108.879 -10.532 1.000 38.318  ? 421 TYR DDD C   1 
ATOM   10489 O O   . TYR G 1 103 ? 64.177  109.779 -11.230 1.000 41.385  ? 421 TYR DDD O   1 
ATOM   10490 C CB  . TYR G 1 103 ? 66.451  108.127 -12.227 1.000 41.801  ? 421 TYR DDD CB  1 
ATOM   10491 C CG  . TYR G 1 103 ? 67.883  107.893 -12.666 1.000 42.535  ? 421 TYR DDD CG  1 
ATOM   10492 C CD1 . TYR G 1 103 ? 68.976  108.241 -11.879 1.000 42.809  ? 421 TYR DDD CD1 1 
ATOM   10493 C CD2 . TYR G 1 103 ? 68.151  107.358 -13.923 1.000 43.096  ? 421 TYR DDD CD2 1 
ATOM   10494 C CE1 . TYR G 1 103 ? 70.280  108.025 -12.303 1.000 42.596  ? 421 TYR DDD CE1 1 
ATOM   10495 C CE2 . TYR G 1 103 ? 69.449  107.145 -14.370 1.000 43.833  ? 421 TYR DDD CE2 1 
ATOM   10496 C CZ  . TYR G 1 103 ? 70.517  107.476 -13.550 1.000 44.246  ? 421 TYR DDD CZ  1 
ATOM   10497 O OH  . TYR G 1 103 ? 71.809  107.278 -13.943 1.000 48.396  ? 421 TYR DDD OH  1 
ATOM   10498 N N   . ASN G 1 104 ? 64.033  108.233 -9.583  1.000 34.541  ? 422 ASN DDD N   1 
ATOM   10499 C CA  . ASN G 1 104 ? 62.551  108.365 -9.521  1.000 35.830  ? 422 ASN DDD CA  1 
ATOM   10500 C C   . ASN G 1 104 ? 62.071  108.608 -8.079  1.000 36.915  ? 422 ASN DDD C   1 
ATOM   10501 O O   . ASN G 1 104 ? 61.362  109.632 -7.864  1.000 38.064  ? 422 ASN DDD O   1 
ATOM   10502 C CB  . ASN G 1 104 ? 61.867  107.177 -10.213 1.000 34.166  ? 422 ASN DDD CB  1 
ATOM   10503 C CG  . ASN G 1 104 ? 62.123  107.105 -11.711 1.000 32.811  ? 422 ASN DDD CG  1 
ATOM   10504 O OD1 . ASN G 1 104 ? 61.290  107.527 -12.509 1.000 30.162  ? 422 ASN DDD OD1 1 
ATOM   10505 N ND2 . ASN G 1 104 ? 63.263  106.564 -12.116 1.000 30.327  ? 422 ASN DDD ND2 1 
ATOM   10506 N N   . TYR G 1 105 ? 62.408  107.702 -7.155  1.000 36.879  ? 423 TYR DDD N   1 
ATOM   10507 C CA  . TYR G 1 105 ? 62.014  107.729 -5.723  1.000 38.823  ? 423 TYR DDD CA  1 
ATOM   10508 C C   . TYR G 1 105 ? 63.129  107.091 -4.906  1.000 41.385  ? 423 TYR DDD C   1 
ATOM   10509 O O   . TYR G 1 105 ? 63.303  105.871 -5.046  1.000 45.622  ? 423 TYR DDD O   1 
ATOM   10510 C CB  . TYR G 1 105 ? 60.726  106.949 -5.484  1.000 40.161  ? 423 TYR DDD CB  1 
ATOM   10511 C CG  . TYR G 1 105 ? 60.135  107.145 -4.112  1.000 44.313  ? 423 TYR DDD CG  1 
ATOM   10512 C CD1 . TYR G 1 105 ? 59.331  108.223 -3.839  1.000 48.615  ? 423 TYR DDD CD1 1 
ATOM   10513 C CD2 . TYR G 1 105 ? 60.362  106.259 -3.080  1.000 48.368  ? 423 TYR DDD CD2 1 
ATOM   10514 C CE1 . TYR G 1 105 ? 58.764  108.421 -2.592  1.000 51.073  ? 423 TYR DDD CE1 1 
ATOM   10515 C CE2 . TYR G 1 105 ? 59.800  106.430 -1.825  1.000 46.934  ? 423 TYR DDD CE2 1 
ATOM   10516 C CZ  . TYR G 1 105 ? 58.996  107.521 -1.574  1.000 49.101  ? 423 TYR DDD CZ  1 
ATOM   10517 O OH  . TYR G 1 105 ? 58.444  107.730 -0.343  1.000 52.553  ? 423 TYR DDD OH  1 
ATOM   10518 N N   . LYS G 1 106 ? 63.878  107.895 -4.143  1.000 44.033  ? 424 LYS DDD N   1 
ATOM   10519 C CA  . LYS G 1 106 ? 64.967  107.438 -3.239  1.000 41.806  ? 424 LYS DDD CA  1 
ATOM   10520 C C   . LYS G 1 106 ? 64.460  107.551 -1.802  1.000 41.628  ? 424 LYS DDD C   1 
ATOM   10521 O O   . LYS G 1 106 ? 63.729  108.508 -1.508  1.000 46.078  ? 424 LYS DDD O   1 
ATOM   10522 C CB  . LYS G 1 106 ? 66.232  108.279 -3.423  1.000 42.121  ? 424 LYS DDD CB  1 
ATOM   10523 C CG  . LYS G 1 106 ? 67.534  107.652 -2.941  1.000 45.639  ? 424 LYS DDD CG  1 
ATOM   10524 C CD  . LYS G 1 106 ? 68.556  107.472 -4.075  1.000 52.575  ? 424 LYS DDD CD  1 
ATOM   10525 C CE  . LYS G 1 106 ? 69.920  106.984 -3.633  1.000 58.185  ? 424 LYS DDD CE  1 
ATOM   10526 N NZ  . LYS G 1 106 ? 69.853  105.578 -3.174  1.000 65.644  ? 424 LYS DDD NZ  1 
ATOM   10527 N N   . LEU G 1 107 ? 64.810  106.577 -0.968  1.000 43.168  ? 425 LEU DDD N   1 
ATOM   10528 C CA  . LEU G 1 107 ? 64.591  106.593 0.497   1.000 42.269  ? 425 LEU DDD CA  1 
ATOM   10529 C C   . LEU G 1 107 ? 65.949  106.764 1.167   1.000 47.680  ? 425 LEU DDD C   1 
ATOM   10530 O O   . LEU G 1 107 ? 66.962  106.270 0.667   1.000 52.403  ? 425 LEU DDD O   1 
ATOM   10531 C CB  . LEU G 1 107 ? 63.933  105.283 0.921   1.000 41.209  ? 425 LEU DDD CB  1 
ATOM   10532 C CG  . LEU G 1 107 ? 62.490  105.096 0.465   1.000 42.180  ? 425 LEU DDD CG  1 
ATOM   10533 C CD1 . LEU G 1 107 ? 61.956  103.715 0.824   1.000 42.594  ? 425 LEU DDD CD1 1 
ATOM   10534 C CD2 . LEU G 1 107 ? 61.606  106.150 1.083   1.000 42.883  ? 425 LEU DDD CD2 1 
ATOM   10535 N N   . PRO G 1 108 ? 66.008  107.481 2.310   1.000 48.511  ? 426 PRO DDD N   1 
ATOM   10536 C CA  . PRO G 1 108 ? 67.265  107.697 3.026   1.000 48.625  ? 426 PRO DDD CA  1 
ATOM   10537 C C   . PRO G 1 108 ? 67.773  106.433 3.736   1.000 50.071  ? 426 PRO DDD C   1 
ATOM   10538 O O   . PRO G 1 108 ? 66.987  105.558 3.997   1.000 48.728  ? 426 PRO DDD O   1 
ATOM   10539 C CB  . PRO G 1 108 ? 66.886  108.759 4.069   1.000 51.142  ? 426 PRO DDD CB  1 
ATOM   10540 C CG  . PRO G 1 108 ? 65.392  108.547 4.318   1.000 52.132  ? 426 PRO DDD CG  1 
ATOM   10541 C CD  . PRO G 1 108 ? 64.850  108.100 2.977   1.000 50.984  ? 426 PRO DDD CD  1 
ATOM   10542 N N   . ASP G 1 109 ? 69.059  106.397 4.071   1.000 56.423  ? 427 ASP DDD N   1 
ATOM   10543 C CA  . ASP G 1 109 ? 69.694  105.254 4.774   1.000 63.513  ? 427 ASP DDD CA  1 
ATOM   10544 C C   . ASP G 1 109 ? 68.990  104.988 6.108   1.000 71.615  ? 427 ASP DDD C   1 
ATOM   10545 O O   . ASP G 1 109 ? 68.825  103.811 6.440   1.000 85.887  ? 427 ASP DDD O   1 
ATOM   10546 C CB  . ASP G 1 109 ? 71.193  105.488 4.958   1.000 65.845  ? 427 ASP DDD CB  1 
ATOM   10547 C CG  . ASP G 1 109 ? 71.952  105.357 3.649   1.000 73.312  ? 427 ASP DDD CG  1 
ATOM   10548 O OD1 . ASP G 1 109 ? 73.023  105.981 3.527   1.000 71.746  ? 427 ASP DDD OD1 1 
ATOM   10549 O OD2 . ASP G 1 109 ? 71.455  104.632 2.751   1.000 84.503  ? 427 ASP DDD OD2 1 
ATOM   10550 N N   . ASP G 1 110 ? 68.584  106.027 6.838   1.000 78.958  ? 428 ASP DDD N   1 
ATOM   10551 C CA  . ASP G 1 110 ? 68.020  105.907 8.210   1.000 82.519  ? 428 ASP DDD CA  1 
ATOM   10552 C C   . ASP G 1 110 ? 66.485  105.964 8.147   1.000 73.056  ? 428 ASP DDD C   1 
ATOM   10553 O O   . ASP G 1 110 ? 65.885  106.454 9.112   1.000 79.713  ? 428 ASP DDD O   1 
ATOM   10554 C CB  . ASP G 1 110 ? 68.641  106.980 9.116   1.000 98.170  ? 428 ASP DDD CB  1 
ATOM   10555 C CG  . ASP G 1 110 ? 68.330  108.432 8.735   1.000 103.836 ? 428 ASP DDD CG  1 
ATOM   10556 O OD1 . ASP G 1 110 ? 68.161  108.708 7.529   1.000 91.987  ? 428 ASP DDD OD1 1 
ATOM   10557 O OD2 . ASP G 1 110 ? 68.264  109.288 9.654   1.000 110.924 ? 428 ASP DDD OD2 1 
ATOM   10558 N N   . PHE G 1 111 ? 65.878  105.493 7.053   1.000 61.328  ? 429 PHE DDD N   1 
ATOM   10559 C CA  . PHE G 1 111 ? 64.414  105.576 6.803   1.000 57.673  ? 429 PHE DDD CA  1 
ATOM   10560 C C   . PHE G 1 111 ? 63.643  104.912 7.954   1.000 58.495  ? 429 PHE DDD C   1 
ATOM   10561 O O   . PHE G 1 111 ? 64.053  103.803 8.408   1.000 62.245  ? 429 PHE DDD O   1 
ATOM   10562 C CB  . PHE G 1 111 ? 64.069  104.903 5.474   1.000 53.599  ? 429 PHE DDD CB  1 
ATOM   10563 C CG  . PHE G 1 111 ? 62.594  104.718 5.214   1.000 52.713  ? 429 PHE DDD CG  1 
ATOM   10564 C CD1 . PHE G 1 111 ? 61.742  105.804 5.149   1.000 55.239  ? 429 PHE DDD CD1 1 
ATOM   10565 C CD2 . PHE G 1 111 ? 62.051  103.464 4.993   1.000 53.081  ? 429 PHE DDD CD2 1 
ATOM   10566 C CE1 . PHE G 1 111 ? 60.392  105.638 4.872   1.000 54.294  ? 429 PHE DDD CE1 1 
ATOM   10567 C CE2 . PHE G 1 111 ? 60.702  103.302 4.722   1.000 53.907  ? 429 PHE DDD CE2 1 
ATOM   10568 C CZ  . PHE G 1 111 ? 59.872  104.389 4.656   1.000 52.123  ? 429 PHE DDD CZ  1 
ATOM   10569 N N   . THR G 1 112 ? 62.558  105.551 8.408   1.000 52.166  ? 430 THR DDD N   1 
ATOM   10570 C CA  . THR G 1 112 ? 61.601  104.945 9.372   1.000 53.961  ? 430 THR DDD CA  1 
ATOM   10571 C C   . THR G 1 112 ? 60.187  104.965 8.788   1.000 51.165  ? 430 THR DDD C   1 
ATOM   10572 O O   . THR G 1 112 ? 59.537  106.022 8.799   1.000 48.983  ? 430 THR DDD O   1 
ATOM   10573 C CB  . THR G 1 112 ? 61.669  105.592 10.763  1.000 57.080  ? 430 THR DDD CB  1 
ATOM   10574 O OG1 . THR G 1 112 ? 60.781  106.705 10.836  1.000 71.143  ? 430 THR DDD OG1 1 
ATOM   10575 C CG2 . THR G 1 112 ? 63.066  106.034 11.131  1.000 58.680  ? 430 THR DDD CG2 1 
ATOM   10576 N N   . GLY G 1 113 ? 59.722  103.808 8.317   1.000 52.822  ? 431 GLY DDD N   1 
ATOM   10577 C CA  . GLY G 1 113 ? 58.339  103.628 7.842   1.000 50.832  ? 431 GLY DDD CA  1 
ATOM   10578 C C   . GLY G 1 113 ? 58.149  102.340 7.066   1.000 47.552  ? 431 GLY DDD C   1 
ATOM   10579 O O   . GLY G 1 113 ? 59.041  101.481 7.092   1.000 47.174  ? 431 GLY DDD O   1 
ATOM   10580 N N   . CYS G 1 114 ? 57.027  102.252 6.363   1.000 48.912  ? 432 CYS DDD N   1 
ATOM   10581 C CA  . CYS G 1 114 ? 56.467  101.012 5.793   1.000 53.335  ? 432 CYS DDD CA  1 
ATOM   10582 C C   . CYS G 1 114 ? 56.330  101.180 4.284   1.000 49.593  ? 432 CYS DDD C   1 
ATOM   10583 O O   . CYS G 1 114 ? 55.802  102.201 3.851   1.000 59.921  ? 432 CYS DDD O   1 
ATOM   10584 C CB  . CYS G 1 114 ? 55.130  100.696 6.446   1.000 60.209  ? 432 CYS DDD CB  1 
ATOM   10585 S SG  . CYS G 1 114 ? 55.343  100.243 8.185   1.000 79.080  ? 432 CYS DDD SG  1 
ATOM   10586 N N   . VAL G 1 115 ? 56.827  100.210 3.534   1.000 43.653  ? 433 VAL DDD N   1 
ATOM   10587 C CA  . VAL G 1 115 ? 56.728  100.152 2.056   1.000 42.253  ? 433 VAL DDD CA  1 
ATOM   10588 C C   . VAL G 1 115 ? 55.705  99.071  1.719   1.000 43.735  ? 433 VAL DDD C   1 
ATOM   10589 O O   . VAL G 1 115 ? 56.047  97.868  1.786   1.000 45.901  ? 433 VAL DDD O   1 
ATOM   10590 C CB  . VAL G 1 115 ? 58.102  99.861  1.434   1.000 43.233  ? 433 VAL DDD CB  1 
ATOM   10591 C CG1 . VAL G 1 115 ? 58.014  99.678  -0.071  1.000 44.094  ? 433 VAL DDD CG1 1 
ATOM   10592 C CG2 . VAL G 1 115 ? 59.108  100.939 1.798   1.000 42.397  ? 433 VAL DDD CG2 1 
ATOM   10593 N N   . ILE G 1 116 ? 54.493  99.490  1.373   1.000 43.646  ? 434 ILE DDD N   1 
ATOM   10594 C CA  . ILE G 1 116 ? 53.336  98.588  1.127   1.000 45.883  ? 434 ILE DDD CA  1 
ATOM   10595 C C   . ILE G 1 116 ? 53.038  98.558  -0.368  1.000 48.609  ? 434 ILE DDD C   1 
ATOM   10596 O O   . ILE G 1 116 ? 52.833  99.644  -0.930  1.000 53.521  ? 434 ILE DDD O   1 
ATOM   10597 C CB  . ILE G 1 116 ? 52.142  99.110  1.927   1.000 47.079  ? 434 ILE DDD CB  1 
ATOM   10598 C CG1 . ILE G 1 116 ? 52.536  99.236  3.403   1.000 49.985  ? 434 ILE DDD CG1 1 
ATOM   10599 C CG2 . ILE G 1 116 ? 50.907  98.244  1.685   1.000 47.519  ? 434 ILE DDD CG2 1 
ATOM   10600 C CD1 . ILE G 1 116 ? 51.572  100.042 4.241   1.000 51.997  ? 434 ILE DDD CD1 1 
ATOM   10601 N N   . ALA G 1 117 ? 52.990  97.370  -0.973  1.000 48.868  ? 435 ALA DDD N   1 
ATOM   10602 C CA  . ALA G 1 117 ? 52.770  97.189  -2.426  1.000 46.124  ? 435 ALA DDD CA  1 
ATOM   10603 C C   . ALA G 1 117 ? 51.753  96.076  -2.673  1.000 44.827  ? 435 ALA DDD C   1 
ATOM   10604 O O   . ALA G 1 117 ? 51.630  95.199  -1.804  1.000 48.498  ? 435 ALA DDD O   1 
ATOM   10605 C CB  . ALA G 1 117 ? 54.081  96.903  -3.107  1.000 45.948  ? 435 ALA DDD CB  1 
ATOM   10606 N N   . TRP G 1 118 ? 51.064  96.120  -3.817  1.000 45.259  ? 436 TRP DDD N   1 
ATOM   10607 C CA  . TRP G 1 118 ? 50.148  95.043  -4.269  1.000 46.570  ? 436 TRP DDD CA  1 
ATOM   10608 C C   . TRP G 1 118 ? 49.962  95.046  -5.784  1.000 48.458  ? 436 TRP DDD C   1 
ATOM   10609 O O   . TRP G 1 118 ? 49.957  96.132  -6.381  1.000 51.021  ? 436 TRP DDD O   1 
ATOM   10610 C CB  . TRP G 1 118 ? 48.803  95.167  -3.569  1.000 49.475  ? 436 TRP DDD CB  1 
ATOM   10611 C CG  . TRP G 1 118 ? 47.975  96.378  -3.878  1.000 50.889  ? 436 TRP DDD CG  1 
ATOM   10612 C CD1 . TRP G 1 118 ? 46.904  96.436  -4.725  1.000 52.672  ? 436 TRP DDD CD1 1 
ATOM   10613 C CD2 . TRP G 1 118 ? 48.054  97.667  -3.240  1.000 48.751  ? 436 TRP DDD CD2 1 
ATOM   10614 N NE1 . TRP G 1 118 ? 46.331  97.678  -4.675  1.000 51.643  ? 436 TRP DDD NE1 1 
ATOM   10615 C CE2 . TRP G 1 118 ? 47.019  98.459  -3.783  1.000 47.858  ? 436 TRP DDD CE2 1 
ATOM   10616 C CE3 . TRP G 1 118 ? 48.909  98.232  -2.288  1.000 48.221  ? 436 TRP DDD CE3 1 
ATOM   10617 C CZ2 . TRP G 1 118 ? 46.821  99.786  -3.413  1.000 46.102  ? 436 TRP DDD CZ2 1 
ATOM   10618 C CZ3 . TRP G 1 118 ? 48.714  99.547  -1.923  1.000 48.115  ? 436 TRP DDD CZ3 1 
ATOM   10619 C CH2 . TRP G 1 118 ? 47.683  100.309 -2.477  1.000 47.721  ? 436 TRP DDD CH2 1 
ATOM   10620 N N   . ASN G 1 119 ? 49.805  93.849  -6.359  1.000 52.953  ? 437 ASN DDD N   1 
ATOM   10621 C CA  . ASN G 1 119 ? 49.544  93.639  -7.806  1.000 52.713  ? 437 ASN DDD CA  1 
ATOM   10622 C C   . ASN G 1 119 ? 48.236  94.363  -8.154  1.000 55.342  ? 437 ASN DDD C   1 
ATOM   10623 O O   . ASN G 1 119 ? 47.225  94.165  -7.444  1.000 57.065  ? 437 ASN DDD O   1 
ATOM   10624 C CB  . ASN G 1 119 ? 49.561  92.148  -8.152  1.000 50.882  ? 437 ASN DDD CB  1 
ATOM   10625 C CG  . ASN G 1 119 ? 49.489  91.874  -9.640  1.000 54.010  ? 437 ASN DDD CG  1 
ATOM   10626 O OD1 . ASN G 1 119 ? 48.464  92.139  -10.262 1.000 63.046  ? 437 ASN DDD OD1 1 
ATOM   10627 N ND2 . ASN G 1 119 ? 50.551  91.325  -10.219 1.000 47.867  ? 437 ASN DDD ND2 1 
ATOM   10628 N N   . SER G 1 120 ? 48.286  95.224  -9.170  1.000 56.040  ? 438 SER DDD N   1 
ATOM   10629 C CA  . SER G 1 120 ? 47.158  96.060  -9.651  1.000 59.021  ? 438 SER DDD CA  1 
ATOM   10630 C C   . SER G 1 120 ? 46.982  95.828  -11.151 1.000 57.404  ? 438 SER DDD C   1 
ATOM   10631 O O   . SER G 1 120 ? 46.700  96.801  -11.862 1.000 61.858  ? 438 SER DDD O   1 
ATOM   10632 C CB  . SER G 1 120 ? 47.399  97.516  -9.346  1.000 60.301  ? 438 SER DDD CB  1 
ATOM   10633 O OG  . SER G 1 120 ? 48.618  97.945  -9.936  1.000 64.083  ? 438 SER DDD OG  1 
ATOM   10634 N N   . ASN G 1 121 ? 47.156  94.583  -11.603 1.000 56.662  ? 439 ASN DDD N   1 
ATOM   10635 C CA  . ASN G 1 121 ? 47.071  94.191  -13.036 1.000 58.958  ? 439 ASN DDD CA  1 
ATOM   10636 C C   . ASN G 1 121 ? 45.626  94.358  -13.519 1.000 62.722  ? 439 ASN DDD C   1 
ATOM   10637 O O   . ASN G 1 121 ? 45.415  94.665  -14.709 1.000 58.147  ? 439 ASN DDD O   1 
ATOM   10638 C CB  . ASN G 1 121 ? 47.577  92.767  -13.258 1.000 56.128  ? 439 ASN DDD CB  1 
ATOM   10639 C CG  . ASN G 1 121 ? 47.965  92.504  -14.695 1.000 55.881  ? 439 ASN DDD CG  1 
ATOM   10640 O OD1 . ASN G 1 121 ? 48.419  93.398  -15.411 1.000 59.052  ? 439 ASN DDD OD1 1 
ATOM   10641 N ND2 . ASN G 1 121 ? 47.821  91.261  -15.116 1.000 59.022  ? 439 ASN DDD ND2 1 
ATOM   10642 N N   . ASN G 1 122 ? 44.674  94.166  -12.605 1.000 72.006  ? 440 ASN DDD N   1 
ATOM   10643 C CA  . ASN G 1 122 ? 43.215  94.293  -12.857 1.000 73.033  ? 440 ASN DDD CA  1 
ATOM   10644 C C   . ASN G 1 122 ? 42.862  95.778  -13.058 1.000 69.145  ? 440 ASN DDD C   1 
ATOM   10645 O O   . ASN G 1 122 ? 41.877  96.032  -13.763 1.000 76.551  ? 440 ASN DDD O   1 
ATOM   10646 C CB  . ASN G 1 122 ? 42.386  93.606  -11.757 1.000 72.353  ? 440 ASN DDD CB  1 
ATOM   10647 C CG  . ASN G 1 122 ? 42.734  94.074  -10.357 1.000 74.642  ? 440 ASN DDD CG  1 
ATOM   10648 O OD1 . ASN G 1 122 ? 43.898  94.092  -9.976  1.000 79.338  ? 440 ASN DDD OD1 1 
ATOM   10649 N ND2 . ASN G 1 122 ? 41.740  94.450  -9.572  1.000 75.276  ? 440 ASN DDD ND2 1 
ATOM   10650 N N   . LEU G 1 123 ? 43.630  96.724  -12.503 1.000 61.970  ? 441 LEU DDD N   1 
ATOM   10651 C CA  . LEU G 1 123 ? 43.281  98.174  -12.521 1.000 61.857  ? 441 LEU DDD CA  1 
ATOM   10652 C C   . LEU G 1 123 ? 44.103  98.944  -13.563 1.000 61.108  ? 441 LEU DDD C   1 
ATOM   10653 O O   . LEU G 1 123 ? 43.526  99.841  -14.189 1.000 61.528  ? 441 LEU DDD O   1 
ATOM   10654 C CB  . LEU G 1 123 ? 43.496  98.764  -11.124 1.000 63.016  ? 441 LEU DDD CB  1 
ATOM   10655 C CG  . LEU G 1 123 ? 42.567  98.240  -10.032 1.000 62.779  ? 441 LEU DDD CG  1 
ATOM   10656 C CD1 . LEU G 1 123 ? 42.685  99.094  -8.770  1.000 63.067  ? 441 LEU DDD CD1 1 
ATOM   10657 C CD2 . LEU G 1 123 ? 41.129  98.207  -10.524 1.000 59.952  ? 441 LEU DDD CD2 1 
ATOM   10658 N N   . ASP G 1 124 ? 45.387  98.621  -13.733 1.000 57.591  ? 442 ASP DDD N   1 
ATOM   10659 C CA  . ASP G 1 124 ? 46.365  99.477  -14.453 1.000 55.422  ? 442 ASP DDD CA  1 
ATOM   10660 C C   . ASP G 1 124 ? 46.892  98.773  -15.714 1.000 60.678  ? 442 ASP DDD C   1 
ATOM   10661 O O   . ASP G 1 124 ? 48.025  99.125  -16.142 1.000 70.657  ? 442 ASP DDD O   1 
ATOM   10662 C CB  . ASP G 1 124 ? 47.503  99.860  -13.499 1.000 54.825  ? 442 ASP DDD CB  1 
ATOM   10663 C CG  . ASP G 1 124 ? 47.057  100.705 -12.319 1.000 53.414  ? 442 ASP DDD CG  1 
ATOM   10664 O OD1 . ASP G 1 124 ? 46.080  101.440 -12.475 1.000 50.661  ? 442 ASP DDD OD1 1 
ATOM   10665 O OD2 . ASP G 1 124 ? 47.696  100.624 -11.257 1.000 55.193  ? 442 ASP DDD OD2 1 
ATOM   10666 N N   . SER G 1 125 ? 46.128  97.838  -16.302 1.000 59.595  ? 443 SER DDD N   1 
ATOM   10667 C CA  . SER G 1 125 ? 46.461  97.191  -17.606 1.000 60.352  ? 443 SER DDD CA  1 
ATOM   10668 C C   . SER G 1 125 ? 45.339  97.423  -18.620 1.000 66.335  ? 443 SER DDD C   1 
ATOM   10669 O O   . SER G 1 125 ? 44.190  97.628  -18.199 1.000 80.310  ? 443 SER DDD O   1 
ATOM   10670 C CB  . SER G 1 125 ? 46.751  95.732  -17.467 1.000 59.865  ? 443 SER DDD CB  1 
ATOM   10671 O OG  . SER G 1 125 ? 48.039  95.536  -16.908 1.000 61.297  ? 443 SER DDD OG  1 
ATOM   10672 N N   . LYS G 1 126 ? 45.695  97.444  -19.905 1.000 69.046  ? 444 LYS DDD N   1 
ATOM   10673 C CA  . LYS G 1 126 ? 44.753  97.566  -21.041 1.000 77.073  ? 444 LYS DDD CA  1 
ATOM   10674 C C   . LYS G 1 126 ? 45.196  96.602  -22.140 1.000 81.097  ? 444 LYS DDD C   1 
ATOM   10675 O O   . LYS G 1 126 ? 46.391  96.287  -22.209 1.000 81.706  ? 444 LYS DDD O   1 
ATOM   10676 C CB  . LYS G 1 126 ? 44.670  99.010  -21.552 1.000 78.312  ? 444 LYS DDD CB  1 
ATOM   10677 C CG  . LYS G 1 126 ? 43.887  99.959  -20.654 1.000 78.497  ? 444 LYS DDD CG  1 
ATOM   10678 C CD  . LYS G 1 126 ? 43.693  101.341 -21.271 1.000 82.300  ? 444 LYS DDD CD  1 
ATOM   10679 C CE  . LYS G 1 126 ? 43.360  102.424 -20.264 1.000 82.066  ? 444 LYS DDD CE  1 
ATOM   10680 N NZ  . LYS G 1 126 ? 43.955  103.741 -20.618 1.000 82.790  ? 444 LYS DDD NZ  1 
ATOM   10681 N N   . VAL G 1 127 ? 44.236  96.184  -22.964 1.000 89.544  ? 445 VAL DDD N   1 
ATOM   10682 C CA  . VAL G 1 127 ? 44.388  95.269  -24.135 1.000 90.643  ? 445 VAL DDD CA  1 
ATOM   10683 C C   . VAL G 1 127 ? 45.655  95.618  -24.939 1.000 86.948  ? 445 VAL DDD C   1 
ATOM   10684 O O   . VAL G 1 127 ? 46.520  94.733  -25.061 1.000 77.685  ? 445 VAL DDD O   1 
ATOM   10685 C CB  . VAL G 1 127 ? 43.107  95.303  -24.999 1.000 104.368 ? 445 VAL DDD CB  1 
ATOM   10686 C CG1 . VAL G 1 127 ? 41.930  94.667  -24.263 1.000 105.957 ? 445 VAL DDD CG1 1 
ATOM   10687 C CG2 . VAL G 1 127 ? 42.733  96.711  -25.477 1.000 100.287 ? 445 VAL DDD CG2 1 
ATOM   10688 N N   . GLY G 1 128 ? 45.789  96.857  -25.434 1.000 85.842  ? 446 GLY DDD N   1 
ATOM   10689 C CA  . GLY G 1 128 ? 46.876  97.272  -26.348 1.000 83.134  ? 446 GLY DDD CA  1 
ATOM   10690 C C   . GLY G 1 128 ? 48.122  97.738  -25.606 1.000 81.838  ? 446 GLY DDD C   1 
ATOM   10691 O O   . GLY G 1 128 ? 49.101  98.160  -26.273 1.000 78.704  ? 446 GLY DDD O   1 
ATOM   10692 N N   . GLY G 1 129 ? 48.105  97.658  -24.273 1.000 77.573  ? 447 GLY DDD N   1 
ATOM   10693 C CA  . GLY G 1 129 ? 49.116  98.269  -23.389 1.000 71.370  ? 447 GLY DDD CA  1 
ATOM   10694 C C   . GLY G 1 129 ? 48.647  99.622  -22.877 1.000 65.353  ? 447 GLY DDD C   1 
ATOM   10695 O O   . GLY G 1 129 ? 48.330  100.487 -23.711 1.000 66.355  ? 447 GLY DDD O   1 
ATOM   10696 N N   . ASN G 1 130 ? 48.572  99.777  -21.550 1.000 59.829  ? 448 ASN DDD N   1 
ATOM   10697 C CA  . ASN G 1 130 ? 48.442  101.066 -20.813 1.000 56.097  ? 448 ASN DDD CA  1 
ATOM   10698 C C   . ASN G 1 130 ? 49.806  101.756 -20.800 1.000 51.292  ? 448 ASN DDD C   1 
ATOM   10699 O O   . ASN G 1 130 ? 50.767  101.133 -20.337 1.000 51.639  ? 448 ASN DDD O   1 
ATOM   10700 C CB  . ASN G 1 130 ? 47.989  100.834 -19.370 1.000 60.322  ? 448 ASN DDD CB  1 
ATOM   10701 C CG  . ASN G 1 130 ? 47.632  102.098 -18.617 1.000 61.133  ? 448 ASN DDD CG  1 
ATOM   10702 O OD1 . ASN G 1 130 ? 47.922  103.206 -19.064 1.000 66.531  ? 448 ASN DDD OD1 1 
ATOM   10703 N ND2 . ASN G 1 130 ? 46.977  101.927 -17.479 1.000 65.439  ? 448 ASN DDD ND2 1 
ATOM   10704 N N   . TYR G 1 131 ? 49.903  102.991 -21.282 1.000 47.877  ? 449 TYR DDD N   1 
ATOM   10705 C CA  . TYR G 1 131 ? 51.203  103.692 -21.408 1.000 47.538  ? 449 TYR DDD CA  1 
ATOM   10706 C C   . TYR G 1 131 ? 51.187  105.014 -20.629 1.000 46.535  ? 449 TYR DDD C   1 
ATOM   10707 O O   . TYR G 1 131 ? 52.134  105.789 -20.794 1.000 42.247  ? 449 TYR DDD O   1 
ATOM   10708 C CB  . TYR G 1 131 ? 51.533  103.868 -22.888 1.000 47.445  ? 449 TYR DDD CB  1 
ATOM   10709 C CG  . TYR G 1 131 ? 51.939  102.627 -23.634 1.000 49.111  ? 449 TYR DDD CG  1 
ATOM   10710 C CD1 . TYR G 1 131 ? 51.017  101.903 -24.376 1.000 55.807  ? 449 TYR DDD CD1 1 
ATOM   10711 C CD2 . TYR G 1 131 ? 53.265  102.228 -23.680 1.000 50.338  ? 449 TYR DDD CD2 1 
ATOM   10712 C CE1 . TYR G 1 131 ? 51.393  100.783 -25.109 1.000 61.122  ? 449 TYR DDD CE1 1 
ATOM   10713 C CE2 . TYR G 1 131 ? 53.666  101.120 -24.411 1.000 53.611  ? 449 TYR DDD CE2 1 
ATOM   10714 C CZ  . TYR G 1 131 ? 52.729  100.399 -25.135 1.000 59.748  ? 449 TYR DDD CZ  1 
ATOM   10715 O OH  . TYR G 1 131 ? 53.142  99.301  -25.831 1.000 57.570  ? 449 TYR DDD OH  1 
ATOM   10716 N N   . ASN G 1 132 ? 50.224  105.194 -19.726 1.000 50.262  ? 450 ASN DDD N   1 
ATOM   10717 C CA  . ASN G 1 132 ? 50.026  106.437 -18.937 1.000 52.809  ? 450 ASN DDD CA  1 
ATOM   10718 C C   . ASN G 1 132 ? 50.992  106.458 -17.741 1.000 51.400  ? 450 ASN DDD C   1 
ATOM   10719 O O   . ASN G 1 132 ? 51.283  107.574 -17.272 1.000 59.480  ? 450 ASN DDD O   1 
ATOM   10720 C CB  . ASN G 1 132 ? 48.568  106.588 -18.499 1.000 57.009  ? 450 ASN DDD CB  1 
ATOM   10721 C CG  . ASN G 1 132 ? 47.613  106.545 -19.670 1.000 57.823  ? 450 ASN DDD CG  1 
ATOM   10722 O OD1 . ASN G 1 132 ? 47.207  107.581 -20.184 1.000 54.508  ? 450 ASN DDD OD1 1 
ATOM   10723 N ND2 . ASN G 1 132 ? 47.281  105.345 -20.116 1.000 72.073  ? 450 ASN DDD ND2 1 
ATOM   10724 N N   . TYR G 1 133 ? 51.472  105.300 -17.272 1.000 45.092  ? 451 TYR DDD N   1 
ATOM   10725 C CA  . TYR G 1 133 ? 52.462  105.190 -16.173 1.000 43.186  ? 451 TYR DDD CA  1 
ATOM   10726 C C   . TYR G 1 133 ? 53.870  105.285 -16.756 1.000 43.606  ? 451 TYR DDD C   1 
ATOM   10727 O O   . TYR G 1 133 ? 54.163  104.467 -17.645 1.000 43.885  ? 451 TYR DDD O   1 
ATOM   10728 C CB  . TYR G 1 133 ? 52.216  103.902 -15.392 1.000 42.249  ? 451 TYR DDD CB  1 
ATOM   10729 C CG  . TYR G 1 133 ? 50.920  103.928 -14.624 1.000 40.542  ? 451 TYR DDD CG  1 
ATOM   10730 C CD1 . TYR G 1 133 ? 50.784  104.698 -13.478 1.000 41.308  ? 451 TYR DDD CD1 1 
ATOM   10731 C CD2 . TYR G 1 133 ? 49.826  103.213 -15.056 1.000 39.178  ? 451 TYR DDD CD2 1 
ATOM   10732 C CE1 . TYR G 1 133 ? 49.598  104.743 -12.770 1.000 40.045  ? 451 TYR DDD CE1 1 
ATOM   10733 C CE2 . TYR G 1 133 ? 48.629  103.253 -14.365 1.000 42.104  ? 451 TYR DDD CE2 1 
ATOM   10734 C CZ  . TYR G 1 133 ? 48.516  104.016 -13.218 1.000 42.872  ? 451 TYR DDD CZ  1 
ATOM   10735 O OH  . TYR G 1 133 ? 47.340  104.058 -12.534 1.000 46.350  ? 451 TYR DDD OH  1 
ATOM   10736 N N   . LEU G 1 134 ? 54.676  106.252 -16.293 1.000 44.860  ? 452 LEU DDD N   1 
ATOM   10737 C CA  . LEU G 1 134 ? 56.046  106.549 -16.814 1.000 46.075  ? 452 LEU DDD CA  1 
ATOM   10738 C C   . LEU G 1 134 ? 57.084  106.443 -15.697 1.000 42.735  ? 452 LEU DDD C   1 
ATOM   10739 O O   . LEU G 1 134 ? 56.691  106.344 -14.505 1.000 43.737  ? 452 LEU DDD O   1 
ATOM   10740 C CB  . LEU G 1 134 ? 56.126  107.968 -17.378 1.000 51.964  ? 452 LEU DDD CB  1 
ATOM   10741 C CG  . LEU G 1 134 ? 54.978  108.430 -18.266 1.000 59.285  ? 452 LEU DDD CG  1 
ATOM   10742 C CD1 . LEU G 1 134 ? 55.150  109.891 -18.646 1.000 63.673  ? 452 LEU DDD CD1 1 
ATOM   10743 C CD2 . LEU G 1 134 ? 54.882  107.550 -19.496 1.000 63.819  ? 452 LEU DDD CD2 1 
ATOM   10744 N N   . TYR G 1 135 ? 58.355  106.513 -16.098 1.000 38.596  ? 453 TYR DDD N   1 
ATOM   10745 C CA  . TYR G 1 135 ? 59.551  106.412 -15.229 1.000 42.029  ? 453 TYR DDD CA  1 
ATOM   10746 C C   . TYR G 1 135 ? 60.711  107.159 -15.892 1.000 44.801  ? 453 TYR DDD C   1 
ATOM   10747 O O   . TYR G 1 135 ? 60.851  107.092 -17.119 1.000 47.285  ? 453 TYR DDD O   1 
ATOM   10748 C CB  . TYR G 1 135 ? 59.906  104.947 -14.933 1.000 41.695  ? 453 TYR DDD CB  1 
ATOM   10749 C CG  . TYR G 1 135 ? 60.383  104.073 -16.071 1.000 42.028  ? 453 TYR DDD CG  1 
ATOM   10750 C CD1 . TYR G 1 135 ? 61.738  103.858 -16.300 1.000 44.253  ? 453 TYR DDD CD1 1 
ATOM   10751 C CD2 . TYR G 1 135 ? 59.481  103.386 -16.868 1.000 41.918  ? 453 TYR DDD CD2 1 
ATOM   10752 C CE1 . TYR G 1 135 ? 62.182  103.003 -17.300 1.000 43.741  ? 453 TYR DDD CE1 1 
ATOM   10753 C CE2 . TYR G 1 135 ? 59.903  102.547 -17.888 1.000 42.531  ? 453 TYR DDD CE2 1 
ATOM   10754 C CZ  . TYR G 1 135 ? 61.258  102.347 -18.100 1.000 43.901  ? 453 TYR DDD CZ  1 
ATOM   10755 O OH  . TYR G 1 135 ? 61.679  101.521 -19.105 1.000 43.314  ? 453 TYR DDD OH  1 
ATOM   10756 N N   . ARG G 1 136 ? 61.507  107.866 -15.097 1.000 43.529  ? 454 ARG DDD N   1 
ATOM   10757 C CA  . ARG G 1 136 ? 62.705  108.584 -15.590 1.000 45.640  ? 454 ARG DDD CA  1 
ATOM   10758 C C   . ARG G 1 136 ? 63.775  107.539 -15.923 1.000 44.618  ? 454 ARG DDD C   1 
ATOM   10759 O O   . ARG G 1 136 ? 64.146  106.790 -15.025 1.000 43.441  ? 454 ARG DDD O   1 
ATOM   10760 C CB  . ARG G 1 136 ? 63.168  109.595 -14.538 1.000 47.838  ? 454 ARG DDD CB  1 
ATOM   10761 C CG  . ARG G 1 136 ? 64.366  110.446 -14.946 1.000 49.702  ? 454 ARG DDD CG  1 
ATOM   10762 C CD  . ARG G 1 136 ? 64.569  111.599 -13.971 1.000 50.183  ? 454 ARG DDD CD  1 
ATOM   10763 N NE  . ARG G 1 136 ? 63.344  112.377 -13.862 1.000 48.276  ? 454 ARG DDD NE  1 
ATOM   10764 C CZ  . ARG G 1 136 ? 62.977  113.302 -14.739 1.000 48.111  ? 454 ARG DDD CZ  1 
ATOM   10765 N NH1 . ARG G 1 136 ? 63.762  113.604 -15.768 1.000 49.629  ? 454 ARG DDD NH1 1 
ATOM   10766 N NH2 . ARG G 1 136 ? 61.821  113.921 -14.580 1.000 45.111  ? 454 ARG DDD NH2 1 
ATOM   10767 N N   . LEU G 1 137 ? 64.226  107.494 -17.173 1.000 43.779  ? 455 LEU DDD N   1 
ATOM   10768 C CA  . LEU G 1 137 ? 65.230  106.523 -17.660 1.000 45.994  ? 455 LEU DDD CA  1 
ATOM   10769 C C   . LEU G 1 137 ? 66.642  107.088 -17.501 1.000 47.046  ? 455 LEU DDD C   1 
ATOM   10770 O O   . LEU G 1 137 ? 67.558  106.290 -17.210 1.000 47.284  ? 455 LEU DDD O   1 
ATOM   10771 C CB  . LEU G 1 137 ? 64.925  106.212 -19.125 1.000 50.462  ? 455 LEU DDD CB  1 
ATOM   10772 C CG  . LEU G 1 137 ? 65.828  105.161 -19.756 1.000 55.985  ? 455 LEU DDD CG  1 
ATOM   10773 C CD1 . LEU G 1 137 ? 65.759  103.855 -18.970 1.000 61.668  ? 455 LEU DDD CD1 1 
ATOM   10774 C CD2 . LEU G 1 137 ? 65.442  104.925 -21.203 1.000 58.976  ? 455 LEU DDD CD2 1 
ATOM   10775 N N   . PHE G 1 138 ? 66.817  108.400 -17.702 1.000 53.463  ? 456 PHE DDD N   1 
ATOM   10776 C CA  . PHE G 1 138 ? 68.136  109.096 -17.660 1.000 51.675  ? 456 PHE DDD CA  1 
ATOM   10777 C C   . PHE G 1 138 ? 68.099  110.326 -16.747 1.000 49.183  ? 456 PHE DDD C   1 
ATOM   10778 O O   . PHE G 1 138 ? 67.078  111.057 -16.672 1.000 46.644  ? 456 PHE DDD O   1 
ATOM   10779 C CB  . PHE G 1 138 ? 68.578  109.535 -19.057 1.000 50.668  ? 456 PHE DDD CB  1 
ATOM   10780 C CG  . PHE G 1 138 ? 68.522  108.436 -20.080 1.000 49.795  ? 456 PHE DDD CG  1 
ATOM   10781 C CD1 . PHE G 1 138 ? 69.468  107.428 -20.082 1.000 51.803  ? 456 PHE DDD CD1 1 
ATOM   10782 C CD2 . PHE G 1 138 ? 67.516  108.411 -21.033 1.000 49.435  ? 456 PHE DDD CD2 1 
ATOM   10783 C CE1 . PHE G 1 138 ? 69.421  106.430 -21.038 1.000 52.186  ? 456 PHE DDD CE1 1 
ATOM   10784 C CE2 . PHE G 1 138 ? 67.479  107.419 -21.996 1.000 46.639  ? 456 PHE DDD CE2 1 
ATOM   10785 C CZ  . PHE G 1 138 ? 68.425  106.429 -21.988 1.000 48.044  ? 456 PHE DDD CZ  1 
ATOM   10786 N N   . ARG G 1 139 ? 69.232  110.547 -16.083 1.000 47.626  ? 457 ARG DDD N   1 
ATOM   10787 C CA  . ARG G 1 139 ? 69.457  111.699 -15.186 1.000 53.725  ? 457 ARG DDD CA  1 
ATOM   10788 C C   . ARG G 1 139 ? 70.952  111.808 -14.896 1.000 61.423  ? 457 ARG DDD C   1 
ATOM   10789 O O   . ARG G 1 139 ? 71.602  110.761 -14.728 1.000 59.408  ? 457 ARG DDD O   1 
ATOM   10790 C CB  . ARG G 1 139 ? 68.655  111.573 -13.891 1.000 54.016  ? 457 ARG DDD CB  1 
ATOM   10791 C CG  . ARG G 1 139 ? 68.453  112.911 -13.191 1.000 54.668  ? 457 ARG DDD CG  1 
ATOM   10792 C CD  . ARG G 1 139 ? 67.519  112.789 -12.017 1.000 54.711  ? 457 ARG DDD CD  1 
ATOM   10793 N NE  . ARG G 1 139 ? 67.145  114.050 -11.389 1.000 52.697  ? 457 ARG DDD NE  1 
ATOM   10794 C CZ  . ARG G 1 139 ? 67.851  114.681 -10.459 1.000 54.059  ? 457 ARG DDD CZ  1 
ATOM   10795 N NH1 . ARG G 1 139 ? 69.014  114.204 -10.057 1.000 58.257  ? 457 ARG DDD NH1 1 
ATOM   10796 N NH2 . ARG G 1 139 ? 67.390  115.800 -9.928  1.000 53.364  ? 457 ARG DDD NH2 1 
ATOM   10797 N N   . LYS G 1 140 ? 71.454  113.048 -14.842 1.000 68.795  ? 458 LYS DDD N   1 
ATOM   10798 C CA  . LYS G 1 140 ? 72.901  113.390 -14.774 1.000 67.128  ? 458 LYS DDD CA  1 
ATOM   10799 C C   . LYS G 1 140 ? 73.454  112.928 -13.419 1.000 60.717  ? 458 LYS DDD C   1 
ATOM   10800 O O   . LYS G 1 140 ? 74.593  112.426 -13.381 1.000 60.542  ? 458 LYS DDD O   1 
ATOM   10801 C CB  . LYS G 1 140 ? 73.079  114.892 -15.010 1.000 74.229  ? 458 LYS DDD CB  1 
ATOM   10802 C CG  . LYS G 1 140 ? 72.619  115.395 -16.372 1.000 85.240  ? 458 LYS DDD CG  1 
ATOM   10803 C CD  . LYS G 1 140 ? 72.304  116.876 -16.368 1.000 92.567  ? 458 LYS DDD CD  1 
ATOM   10804 C CE  . LYS G 1 140 ? 71.471  117.295 -17.559 1.000 97.358  ? 458 LYS DDD CE  1 
ATOM   10805 N NZ  . LYS G 1 140 ? 71.220  118.754 -17.527 1.000 100.669 ? 458 LYS DDD NZ  1 
ATOM   10806 N N   . SER G 1 141 ? 72.664  113.067 -12.353 1.000 53.876  ? 459 SER DDD N   1 
ATOM   10807 C CA  . SER G 1 141 ? 72.999  112.611 -10.982 1.000 51.323  ? 459 SER DDD CA  1 
ATOM   10808 C C   . SER G 1 141 ? 71.782  111.925 -10.356 1.000 46.308  ? 459 SER DDD C   1 
ATOM   10809 O O   . SER G 1 141 ? 70.651  112.121 -10.847 1.000 42.073  ? 459 SER DDD O   1 
ATOM   10810 C CB  . SER G 1 141 ? 73.498  113.755 -10.138 1.000 53.657  ? 459 SER DDD CB  1 
ATOM   10811 O OG  . SER G 1 141 ? 72.500  114.754 -9.981  1.000 48.460  ? 459 SER DDD OG  1 
ATOM   10812 N N   . ASN G 1 142 ? 72.025  111.126 -9.319  1.000 44.375  ? 460 ASN DDD N   1 
ATOM   10813 C CA  . ASN G 1 142 ? 70.966  110.396 -8.579  1.000 45.809  ? 460 ASN DDD CA  1 
ATOM   10814 C C   . ASN G 1 142 ? 70.151  111.415 -7.781  1.000 43.636  ? 460 ASN DDD C   1 
ATOM   10815 O O   . ASN G 1 142 ? 70.719  112.443 -7.387  1.000 42.483  ? 460 ASN DDD O   1 
ATOM   10816 C CB  . ASN G 1 142 ? 71.555  109.310 -7.675  1.000 48.393  ? 460 ASN DDD CB  1 
ATOM   10817 C CG  . ASN G 1 142 ? 72.421  108.335 -8.437  1.000 50.160  ? 460 ASN DDD CG  1 
ATOM   10818 O OD1 . ASN G 1 142 ? 72.501  108.388 -9.666  1.000 55.171  ? 460 ASN DDD OD1 1 
ATOM   10819 N ND2 . ASN G 1 142 ? 73.073  107.449 -7.709  1.000 53.449  ? 460 ASN DDD ND2 1 
ATOM   10820 N N   . LEU G 1 143 ? 68.864  111.140 -7.572  1.000 41.983  ? 461 LEU DDD N   1 
ATOM   10821 C CA  . LEU G 1 143 ? 67.989  111.936 -6.680  1.000 39.546  ? 461 LEU DDD CA  1 
ATOM   10822 C C   . LEU G 1 143 ? 68.551  111.903 -5.261  1.000 42.077  ? 461 LEU DDD C   1 
ATOM   10823 O O   . LEU G 1 143 ? 69.177  110.894 -4.870  1.000 41.301  ? 461 LEU DDD O   1 
ATOM   10824 C CB  . LEU G 1 143 ? 66.583  111.340 -6.685  1.000 39.444  ? 461 LEU DDD CB  1 
ATOM   10825 C CG  . LEU G 1 143 ? 65.768  111.554 -7.954  1.000 39.666  ? 461 LEU DDD CG  1 
ATOM   10826 C CD1 . LEU G 1 143 ? 64.334  111.065 -7.766  1.000 39.521  ? 461 LEU DDD CD1 1 
ATOM   10827 C CD2 . LEU G 1 143 ? 65.777  113.013 -8.356  1.000 42.448  ? 461 LEU DDD CD2 1 
ATOM   10828 N N   . LYS G 1 144 ? 68.317  112.974 -4.507  1.000 46.549  ? 462 LYS DDD N   1 
ATOM   10829 C CA  . LYS G 1 144 ? 68.466  112.961 -3.034  1.000 49.610  ? 462 LYS DDD CA  1 
ATOM   10830 C C   . LYS G 1 144 ? 67.206  112.321 -2.459  1.000 42.817  ? 462 LYS DDD C   1 
ATOM   10831 O O   . LYS G 1 144 ? 66.184  112.230 -3.129  1.000 36.942  ? 462 LYS DDD O   1 
ATOM   10832 C CB  . LYS G 1 144 ? 68.765  114.372 -2.514  1.000 57.345  ? 462 LYS DDD CB  1 
ATOM   10833 C CG  . LYS G 1 144 ? 70.053  115.003 -3.065  1.000 66.642  ? 462 LYS DDD CG  1 
ATOM   10834 C CD  . LYS G 1 144 ? 71.114  115.447 -2.029  1.000 77.694  ? 462 LYS DDD CD  1 
ATOM   10835 C CE  . LYS G 1 144 ? 70.699  116.631 -1.167  1.000 85.336  ? 462 LYS DDD CE  1 
ATOM   10836 N NZ  . LYS G 1 144 ? 70.600  117.882 -1.956  1.000 91.422  ? 462 LYS DDD NZ  1 
ATOM   10837 N N   . PRO G 1 145 ? 67.263  111.770 -1.234  1.000 40.791  ? 463 PRO DDD N   1 
ATOM   10838 C CA  . PRO G 1 145 ? 66.077  111.205 -0.594  1.000 44.380  ? 463 PRO DDD CA  1 
ATOM   10839 C C   . PRO G 1 145 ? 64.851  112.121 -0.664  1.000 46.434  ? 463 PRO DDD C   1 
ATOM   10840 O O   . PRO G 1 145 ? 64.970  113.290 -0.345  1.000 48.100  ? 463 PRO DDD O   1 
ATOM   10841 C CB  . PRO G 1 145 ? 66.535  111.027 0.856   1.000 44.484  ? 463 PRO DDD CB  1 
ATOM   10842 C CG  . PRO G 1 145 ? 68.011  110.718 0.711   1.000 43.515  ? 463 PRO DDD CG  1 
ATOM   10843 C CD  . PRO G 1 145 ? 68.478  111.601 -0.427  1.000 41.076  ? 463 PRO DDD CD  1 
ATOM   10844 N N   . PHE G 1 146 ? 63.715  111.570 -1.088  1.000 48.486  ? 464 PHE DDD N   1 
ATOM   10845 C CA  . PHE G 1 146 ? 62.423  112.292 -1.174  1.000 50.317  ? 464 PHE DDD CA  1 
ATOM   10846 C C   . PHE G 1 146 ? 62.558  113.506 -2.096  1.000 48.285  ? 464 PHE DDD C   1 
ATOM   10847 O O   . PHE G 1 146 ? 61.846  114.486 -1.888  1.000 44.946  ? 464 PHE DDD O   1 
ATOM   10848 C CB  . PHE G 1 146 ? 61.952  112.755 0.205   1.000 50.897  ? 464 PHE DDD CB  1 
ATOM   10849 C CG  . PHE G 1 146 ? 61.723  111.635 1.182   1.000 53.714  ? 464 PHE DDD CG  1 
ATOM   10850 C CD1 . PHE G 1 146 ? 60.844  110.607 0.881   1.000 53.374  ? 464 PHE DDD CD1 1 
ATOM   10851 C CD2 . PHE G 1 146 ? 62.387  111.606 2.396   1.000 56.369  ? 464 PHE DDD CD2 1 
ATOM   10852 C CE1 . PHE G 1 146 ? 60.632  109.577 1.783   1.000 51.950  ? 464 PHE DDD CE1 1 
ATOM   10853 C CE2 . PHE G 1 146 ? 62.180  110.567 3.290   1.000 57.909  ? 464 PHE DDD CE2 1 
ATOM   10854 C CZ  . PHE G 1 146 ? 61.295  109.563 2.988   1.000 54.560  ? 464 PHE DDD CZ  1 
ATOM   10855 N N   . GLU G 1 147 ? 63.438  113.425 -3.093  1.000 49.439  ? 465 GLU DDD N   1 
ATOM   10856 C CA  . GLU G 1 147 ? 63.492  114.382 -4.226  1.000 45.381  ? 465 GLU DDD CA  1 
ATOM   10857 C C   . GLU G 1 147 ? 62.501  113.881 -5.280  1.000 46.189  ? 465 GLU DDD C   1 
ATOM   10858 O O   . GLU G 1 147 ? 62.302  112.638 -5.407  1.000 49.686  ? 465 GLU DDD O   1 
ATOM   10859 C CB  . GLU G 1 147 ? 64.911  114.521 -4.788  1.000 42.064  ? 465 GLU DDD CB  1 
ATOM   10860 C CG  . GLU G 1 147 ? 65.069  115.629 -5.819  1.000 41.509  ? 465 GLU DDD CG  1 
ATOM   10861 C CD  . GLU G 1 147 ? 66.499  116.078 -6.119  1.000 44.677  ? 465 GLU DDD CD  1 
ATOM   10862 O OE1 . GLU G 1 147 ? 67.448  115.281 -5.962  1.000 48.528  ? 465 GLU DDD OE1 1 
ATOM   10863 O OE2 . GLU G 1 147 ? 66.671  117.245 -6.497  1.000 50.571  ? 465 GLU DDD OE2 1 
ATOM   10864 N N   . ARG G 1 148 ? 61.913  114.829 -5.996  1.000 43.847  ? 466 ARG DDD N   1 
ATOM   10865 C CA  . ARG G 1 148 ? 60.873  114.601 -7.020  1.000 45.256  ? 466 ARG DDD CA  1 
ATOM   10866 C C   . ARG G 1 148 ? 61.180  115.517 -8.202  1.000 47.387  ? 466 ARG DDD C   1 
ATOM   10867 O O   . ARG G 1 148 ? 61.018  116.743 -8.079  1.000 57.301  ? 466 ARG DDD O   1 
ATOM   10868 C CB  . ARG G 1 148 ? 59.528  114.923 -6.392  1.000 48.478  ? 466 ARG DDD CB  1 
ATOM   10869 C CG  . ARG G 1 148 ? 58.323  114.658 -7.264  1.000 52.658  ? 466 ARG DDD CG  1 
ATOM   10870 C CD  . ARG G 1 148 ? 57.200  115.370 -6.547  1.000 62.071  ? 466 ARG DDD CD  1 
ATOM   10871 N NE  . ARG G 1 148 ? 55.957  115.115 -7.219  1.000 73.264  ? 466 ARG DDD NE  1 
ATOM   10872 C CZ  . ARG G 1 148 ? 54.831  115.765 -6.988  1.000 89.738  ? 466 ARG DDD CZ  1 
ATOM   10873 N NH1 . ARG G 1 148 ? 54.787  116.742 -6.092  1.000 97.312  ? 466 ARG DDD NH1 1 
ATOM   10874 N NH2 . ARG G 1 148 ? 53.744  115.426 -7.664  1.000 94.184  ? 466 ARG DDD NH2 1 
ATOM   10875 N N   . ASP G 1 149 ? 61.661  114.934 -9.291  1.000 45.716  ? 467 ASP DDD N   1 
ATOM   10876 C CA  . ASP G 1 149 ? 62.027  115.630 -10.541 1.000 41.495  ? 467 ASP DDD CA  1 
ATOM   10877 C C   . ASP G 1 149 ? 60.939  115.320 -11.569 1.000 46.143  ? 467 ASP DDD C   1 
ATOM   10878 O O   . ASP G 1 149 ? 60.742  114.123 -11.861 1.000 50.119  ? 467 ASP DDD O   1 
ATOM   10879 C CB  . ASP G 1 149 ? 63.402  115.148 -10.980 1.000 42.305  ? 467 ASP DDD CB  1 
ATOM   10880 C CG  . ASP G 1 149 ? 63.991  115.896 -12.159 1.000 45.633  ? 467 ASP DDD CG  1 
ATOM   10881 O OD1 . ASP G 1 149 ? 63.221  116.575 -12.861 1.000 46.421  ? 467 ASP DDD OD1 1 
ATOM   10882 O OD2 . ASP G 1 149 ? 65.223  115.784 -12.367 1.000 47.915  ? 467 ASP DDD OD2 1 
ATOM   10883 N N   . ILE G 1 150 ? 60.240  116.353 -12.056 1.000 54.448  ? 468 ILE DDD N   1 
ATOM   10884 C CA  . ILE G 1 150 ? 59.210  116.244 -13.138 1.000 53.737  ? 468 ILE DDD CA  1 
ATOM   10885 C C   . ILE G 1 150 ? 59.680  116.987 -14.400 1.000 49.698  ? 468 ILE DDD C   1 
ATOM   10886 O O   . ILE G 1 150 ? 58.889  117.052 -15.352 1.000 46.132  ? 468 ILE DDD O   1 
ATOM   10887 C CB  . ILE G 1 150 ? 57.828  116.729 -12.654 1.000 54.560  ? 468 ILE DDD CB  1 
ATOM   10888 C CG1 . ILE G 1 150 ? 57.864  118.141 -12.071 1.000 54.419  ? 468 ILE DDD CG1 1 
ATOM   10889 C CG2 . ILE G 1 150 ? 57.249  115.740 -11.657 1.000 55.554  ? 468 ILE DDD CG2 1 
ATOM   10890 C CD1 . ILE G 1 150 ? 56.486  118.674 -11.744 1.000 55.384  ? 468 ILE DDD CD1 1 
ATOM   10891 N N   . SER G 1 151 ? 60.937  117.447 -14.432 1.000 46.142  ? 469 SER DDD N   1 
ATOM   10892 C CA  . SER G 1 151 ? 61.583  118.086 -15.608 1.000 47.095  ? 469 SER DDD CA  1 
ATOM   10893 C C   . SER G 1 151 ? 61.607  117.121 -16.804 1.000 45.983  ? 469 SER DDD C   1 
ATOM   10894 O O   . SER G 1 151 ? 61.833  115.927 -16.598 1.000 45.950  ? 469 SER DDD O   1 
ATOM   10895 C CB  . SER G 1 151 ? 62.969  118.594 -15.254 1.000 51.044  ? 469 SER DDD CB  1 
ATOM   10896 O OG  . SER G 1 151 ? 63.969  117.602 -15.434 1.000 50.391  ? 469 SER DDD OG  1 
ATOM   10897 N N   . THR G 1 152 ? 61.366  117.628 -18.014 1.000 45.673  ? 470 THR DDD N   1 
ATOM   10898 C CA  . THR G 1 152 ? 61.469  116.864 -19.284 1.000 45.869  ? 470 THR DDD CA  1 
ATOM   10899 C C   . THR G 1 152 ? 62.602  117.458 -20.133 1.000 45.886  ? 470 THR DDD C   1 
ATOM   10900 O O   . THR G 1 152 ? 62.523  117.361 -21.383 1.000 44.910  ? 470 THR DDD O   1 
ATOM   10901 C CB  . THR G 1 152 ? 60.097  116.771 -19.960 1.000 44.608  ? 470 THR DDD CB  1 
ATOM   10902 O OG1 . THR G 1 152 ? 59.554  118.082 -20.052 1.000 46.043  ? 470 THR DDD OG1 1 
ATOM   10903 C CG2 . THR G 1 152 ? 59.130  115.910 -19.180 1.000 45.792  ? 470 THR DDD CG2 1 
ATOM   10904 N N   . GLU G 1 153 ? 63.632  118.009 -19.476 1.000 48.608  ? 471 GLU DDD N   1 
ATOM   10905 C CA  . GLU G 1 153 ? 64.919  118.414 -20.104 1.000 57.285  ? 471 GLU DDD CA  1 
ATOM   10906 C C   . GLU G 1 153 ? 65.373  117.253 -20.997 1.000 53.211  ? 471 GLU DDD C   1 
ATOM   10907 O O   . GLU G 1 153 ? 65.375  116.076 -20.509 1.000 56.582  ? 471 GLU DDD O   1 
ATOM   10908 C CB  . GLU G 1 153 ? 66.051  118.593 -19.089 1.000 77.794  ? 471 GLU DDD CB  1 
ATOM   10909 C CG  . GLU G 1 153 ? 65.767  119.548 -17.952 1.000 91.802  ? 471 GLU DDD CG  1 
ATOM   10910 C CD  . GLU G 1 153 ? 66.114  120.982 -18.235 1.000 103.355 ? 471 GLU DDD CD  1 
ATOM   10911 O OE1 . GLU G 1 153 ? 65.231  121.844 -18.059 1.000 108.182 ? 471 GLU DDD OE1 1 
ATOM   10912 O OE2 . GLU G 1 153 ? 67.281  121.226 -18.591 1.000 106.979 ? 471 GLU DDD OE2 1 
ATOM   10913 N N   . ILE G 1 154 ? 65.779  117.537 -22.231 1.000 48.519  ? 472 ILE DDD N   1 
ATOM   10914 C CA  . ILE G 1 154 ? 66.387  116.499 -23.107 1.000 47.378  ? 472 ILE DDD CA  1 
ATOM   10915 C C   . ILE G 1 154 ? 67.754  116.130 -22.513 1.000 46.430  ? 472 ILE DDD C   1 
ATOM   10916 O O   . ILE G 1 154 ? 68.522  117.027 -22.203 1.000 45.540  ? 472 ILE DDD O   1 
ATOM   10917 C CB  . ILE G 1 154 ? 66.463  116.988 -24.562 1.000 46.924  ? 472 ILE DDD CB  1 
ATOM   10918 C CG1 . ILE G 1 154 ? 65.090  117.396 -25.102 1.000 47.036  ? 472 ILE DDD CG1 1 
ATOM   10919 C CG2 . ILE G 1 154 ? 67.118  115.947 -25.450 1.000 53.395  ? 472 ILE DDD CG2 1 
ATOM   10920 C CD1 . ILE G 1 154 ? 63.985  116.402 -24.875 1.000 49.150  ? 472 ILE DDD CD1 1 
ATOM   10921 N N   . TYR G 1 155 ? 68.012  114.842 -22.304 1.000 48.835  ? 473 TYR DDD N   1 
ATOM   10922 C CA  . TYR G 1 155 ? 69.239  114.336 -21.646 1.000 47.513  ? 473 TYR DDD CA  1 
ATOM   10923 C C   . TYR G 1 155 ? 70.361  114.355 -22.674 1.000 49.174  ? 473 TYR DDD C   1 
ATOM   10924 O O   . TYR G 1 155 ? 70.191  113.777 -23.757 1.000 48.053  ? 473 TYR DDD O   1 
ATOM   10925 C CB  . TYR G 1 155 ? 69.014  112.918 -21.127 1.000 47.867  ? 473 TYR DDD CB  1 
ATOM   10926 C CG  . TYR G 1 155 ? 70.192  112.287 -20.433 1.000 46.678  ? 473 TYR DDD CG  1 
ATOM   10927 C CD1 . TYR G 1 155 ? 70.494  112.608 -19.120 1.000 46.620  ? 473 TYR DDD CD1 1 
ATOM   10928 C CD2 . TYR G 1 155 ? 70.977  111.338 -21.071 1.000 46.523  ? 473 TYR DDD CD2 1 
ATOM   10929 C CE1 . TYR G 1 155 ? 71.562  112.020 -18.461 1.000 47.540  ? 473 TYR DDD CE1 1 
ATOM   10930 C CE2 . TYR G 1 155 ? 72.056  110.750 -20.430 1.000 46.980  ? 473 TYR DDD CE2 1 
ATOM   10931 C CZ  . TYR G 1 155 ? 72.337  111.080 -19.115 1.000 46.716  ? 473 TYR DDD CZ  1 
ATOM   10932 O OH  . TYR G 1 155 ? 73.363  110.495 -18.442 1.000 47.836  ? 473 TYR DDD OH  1 
ATOM   10933 N N   . GLN G 1 156 ? 71.475  114.999 -22.335 1.000 55.157  ? 474 GLN DDD N   1 
ATOM   10934 C CA  . GLN G 1 156 ? 72.692  115.032 -23.189 1.000 57.680  ? 474 GLN DDD CA  1 
ATOM   10935 C C   . GLN G 1 156 ? 73.577  113.844 -22.804 1.000 55.398  ? 474 GLN DDD C   1 
ATOM   10936 O O   . GLN G 1 156 ? 74.190  113.889 -21.730 1.000 55.707  ? 474 GLN DDD O   1 
ATOM   10937 C CB  . GLN G 1 156 ? 73.425  116.365 -23.038 1.000 63.996  ? 474 GLN DDD CB  1 
ATOM   10938 C CG  . GLN G 1 156 ? 74.629  116.497 -23.960 1.000 73.022  ? 474 GLN DDD CG  1 
ATOM   10939 C CD  . GLN G 1 156 ? 75.323  117.824 -23.776 1.000 79.430  ? 474 GLN DDD CD  1 
ATOM   10940 O OE1 . GLN G 1 156 ? 74.704  118.813 -23.382 1.000 78.039  ? 474 GLN DDD OE1 1 
ATOM   10941 N NE2 . GLN G 1 156 ? 76.615  117.856 -24.082 1.000 79.330  ? 474 GLN DDD NE2 1 
ATOM   10942 N N   . ALA G 1 157 ? 73.629  112.817 -23.652 1.000 58.492  ? 475 ALA DDD N   1 
ATOM   10943 C CA  . ALA G 1 157 ? 74.481  111.619 -23.465 1.000 60.819  ? 475 ALA DDD CA  1 
ATOM   10944 C C   . ALA G 1 157 ? 75.860  111.827 -24.115 1.000 62.469  ? 475 ALA DDD C   1 
ATOM   10945 O O   . ALA G 1 157 ? 76.828  111.269 -23.582 1.000 60.503  ? 475 ALA DDD O   1 
ATOM   10946 C CB  . ALA G 1 157 ? 73.783  110.409 -24.024 1.000 60.919  ? 475 ALA DDD CB  1 
ATOM   10947 N N   . GLY G 1 158 ? 75.940  112.612 -25.199 1.000 70.983  ? 476 GLY DDD N   1 
ATOM   10948 C CA  . GLY G 1 158 ? 77.122  112.714 -26.087 1.000 73.066  ? 476 GLY DDD CA  1 
ATOM   10949 C C   . GLY G 1 158 ? 77.808  114.067 -26.015 1.000 73.190  ? 476 GLY DDD C   1 
ATOM   10950 O O   . GLY G 1 158 ? 77.314  114.946 -25.276 1.000 65.962  ? 476 GLY DDD O   1 
ATOM   10951 N N   . SER G 1 159 ? 78.914  114.214 -26.761 1.000 82.980  ? 477 SER DDD N   1 
ATOM   10952 C CA  . SER G 1 159 ? 79.811  115.405 -26.794 1.000 85.432  ? 477 SER DDD CA  1 
ATOM   10953 C C   . SER G 1 159 ? 78.980  116.661 -27.061 1.000 79.574  ? 477 SER DDD C   1 
ATOM   10954 O O   . SER G 1 159 ? 79.082  117.626 -26.286 1.000 72.928  ? 477 SER DDD O   1 
ATOM   10955 C CB  . SER G 1 159 ? 80.900  115.297 -27.858 1.000 86.585  ? 477 SER DDD CB  1 
ATOM   10956 O OG  . SER G 1 159 ? 81.220  113.950 -28.191 1.000 90.822  ? 477 SER DDD OG  1 
ATOM   10957 N N   . THR G 1 160 ? 78.222  116.638 -28.161 1.000 80.127  ? 478 THR DDD N   1 
ATOM   10958 C CA  . THR G 1 160 ? 77.515  117.818 -28.713 1.000 82.549  ? 478 THR DDD CA  1 
ATOM   10959 C C   . THR G 1 160 ? 76.302  118.075 -27.822 1.000 82.106  ? 478 THR DDD C   1 
ATOM   10960 O O   . THR G 1 160 ? 75.615  117.131 -27.432 1.000 75.723  ? 478 THR DDD O   1 
ATOM   10961 C CB  . THR G 1 160 ? 77.192  117.640 -30.207 1.000 81.653  ? 478 THR DDD CB  1 
ATOM   10962 O OG1 . THR G 1 160 ? 76.135  116.696 -30.342 1.000 69.653  ? 478 THR DDD OG1 1 
ATOM   10963 C CG2 . THR G 1 160 ? 78.379  117.205 -31.050 1.000 82.785  ? 478 THR DDD CG2 1 
ATOM   10964 N N   . PRO G 1 161 ? 76.032  119.341 -27.415 1.000 87.670  ? 479 PRO DDD N   1 
ATOM   10965 C CA  . PRO G 1 161 ? 74.839  119.652 -26.639 1.000 85.748  ? 479 PRO DDD CA  1 
ATOM   10966 C C   . PRO G 1 161 ? 73.617  119.636 -27.558 1.000 79.656  ? 479 PRO DDD C   1 
ATOM   10967 O O   . PRO G 1 161 ? 73.720  120.078 -28.676 1.000 73.150  ? 479 PRO DDD O   1 
ATOM   10968 C CB  . PRO G 1 161 ? 75.053  121.071 -26.087 1.000 89.786  ? 479 PRO DDD CB  1 
ATOM   10969 C CG  . PRO G 1 161 ? 76.449  121.473 -26.526 1.000 91.226  ? 479 PRO DDD CG  1 
ATOM   10970 C CD  . PRO G 1 161 ? 76.850  120.539 -27.649 1.000 90.798  ? 479 PRO DDD CD  1 
ATOM   10971 N N   . CYS G 1 162 ? 72.514  119.087 -27.057 1.000 82.992  ? 480 CYS DDD N   1 
ATOM   10972 C CA  . CYS G 1 162 ? 71.166  119.215 -27.658 1.000 87.604  ? 480 CYS DDD CA  1 
ATOM   10973 C C   . CYS G 1 162 ? 70.675  120.604 -27.292 1.000 84.566  ? 480 CYS DDD C   1 
ATOM   10974 O O   . CYS G 1 162 ? 70.935  121.029 -26.150 1.000 93.047  ? 480 CYS DDD O   1 
ATOM   10975 C CB  . CYS G 1 162 ? 70.184  118.179 -27.121 1.000 97.752  ? 480 CYS DDD CB  1 
ATOM   10976 S SG  . CYS G 1 162 ? 70.972  116.847 -26.164 1.000 120.074 ? 480 CYS DDD SG  1 
ATOM   10977 N N   . ASN G 1 163 ? 70.025  121.294 -28.220 1.000 86.176  ? 481 ASN DDD N   1 
ATOM   10978 C CA  . ASN G 1 163 ? 69.409  122.617 -27.932 1.000 86.906  ? 481 ASN DDD CA  1 
ATOM   10979 C C   . ASN G 1 163 ? 67.906  122.364 -27.794 1.000 81.723  ? 481 ASN DDD C   1 
ATOM   10980 O O   . ASN G 1 163 ? 67.129  122.977 -28.533 1.000 89.093  ? 481 ASN DDD O   1 
ATOM   10981 C CB  . ASN G 1 163 ? 69.836  123.681 -28.954 1.000 84.806  ? 481 ASN DDD CB  1 
ATOM   10982 C CG  . ASN G 1 163 ? 71.312  124.029 -28.844 1.000 80.461  ? 481 ASN DDD CG  1 
ATOM   10983 O OD1 . ASN G 1 163 ? 71.740  124.645 -27.876 1.000 74.016  ? 481 ASN DDD OD1 1 
ATOM   10984 N ND2 . ASN G 1 163 ? 72.112  123.624 -29.817 1.000 79.687  ? 481 ASN DDD ND2 1 
ATOM   10985 N N   . GLY G 1 164 ? 67.539  121.462 -26.880 1.000 72.864  ? 482 GLY DDD N   1 
ATOM   10986 C CA  . GLY G 1 164 ? 66.164  120.968 -26.714 1.000 73.189  ? 482 GLY DDD CA  1 
ATOM   10987 C C   . GLY G 1 164 ? 65.729  120.143 -27.911 1.000 74.630  ? 482 GLY DDD C   1 
ATOM   10988 O O   . GLY G 1 164 ? 64.514  119.925 -28.051 1.000 66.278  ? 482 GLY DDD O   1 
ATOM   10989 N N   . VAL G 1 165 ? 66.682  119.650 -28.713 1.000 81.651  ? 483 VAL DDD N   1 
ATOM   10990 C CA  . VAL G 1 165 ? 66.408  118.840 -29.935 1.000 85.625  ? 483 VAL DDD CA  1 
ATOM   10991 C C   . VAL G 1 165 ? 66.723  117.372 -29.610 1.000 87.158  ? 483 VAL DDD C   1 
ATOM   10992 O O   . VAL G 1 165 ? 67.841  117.121 -29.101 1.000 85.574  ? 483 VAL DDD O   1 
ATOM   10993 C CB  . VAL G 1 165 ? 67.203  119.393 -31.139 1.000 91.021  ? 483 VAL DDD CB  1 
ATOM   10994 C CG1 . VAL G 1 165 ? 68.355  118.488 -31.591 1.000 91.747  ? 483 VAL DDD CG1 1 
ATOM   10995 C CG2 . VAL G 1 165 ? 66.276  119.717 -32.311 1.000 86.506  ? 483 VAL DDD CG2 1 
ATOM   10996 N N   . GLU G 1 166 ? 65.772  116.461 -29.870 1.000 85.787  ? 484 GLU DDD N   1 
ATOM   10997 C CA  . GLU G 1 166 ? 65.931  115.002 -29.627 1.000 92.806  ? 484 GLU DDD CA  1 
ATOM   10998 C C   . GLU G 1 166 ? 66.576  114.319 -30.856 1.000 95.380  ? 484 GLU DDD C   1 
ATOM   10999 O O   . GLU G 1 166 ? 66.166  114.624 -31.981 1.000 102.630 ? 484 GLU DDD O   1 
ATOM   11000 C CB  . GLU G 1 166 ? 64.588  114.369 -29.241 1.000 95.333  ? 484 GLU DDD CB  1 
ATOM   11001 C CG  . GLU G 1 166 ? 64.765  112.924 -28.792 1.000 111.719 ? 484 GLU DDD CG  1 
ATOM   11002 C CD  . GLU G 1 166 ? 63.540  112.101 -28.463 1.000 115.628 ? 484 GLU DDD CD  1 
ATOM   11003 O OE1 . GLU G 1 166 ? 63.707  111.052 -27.777 1.000 122.060 ? 484 GLU DDD OE1 1 
ATOM   11004 O OE2 . GLU G 1 166 ? 62.451  112.483 -28.944 1.000 100.755 ? 484 GLU DDD OE2 1 
ATOM   11005 N N   . GLY G 1 167 ? 67.562  113.430 -30.643 1.000 94.289  ? 485 GLY DDD N   1 
ATOM   11006 C CA  . GLY G 1 167 ? 68.219  112.643 -31.706 1.000 87.420  ? 485 GLY DDD CA  1 
ATOM   11007 C C   . GLY G 1 167 ? 69.383  111.817 -31.180 1.000 87.469  ? 485 GLY DDD C   1 
ATOM   11008 O O   . GLY G 1 167 ? 69.324  111.396 -30.011 1.000 92.278  ? 485 GLY DDD O   1 
ATOM   11009 N N   . PHE G 1 168 ? 70.378  111.533 -32.027 1.000 88.936  ? 486 PHE DDD N   1 
ATOM   11010 C CA  . PHE G 1 168 ? 71.603  110.761 -31.678 1.000 95.638  ? 486 PHE DDD CA  1 
ATOM   11011 C C   . PHE G 1 168 ? 72.178  111.341 -30.373 1.000 88.800  ? 486 PHE DDD C   1 
ATOM   11012 O O   . PHE G 1 168 ? 72.434  112.553 -30.330 1.000 81.327  ? 486 PHE DDD O   1 
ATOM   11013 C CB  . PHE G 1 168 ? 72.570  110.771 -32.870 1.000 107.928 ? 486 PHE DDD CB  1 
ATOM   11014 C CG  . PHE G 1 168 ? 73.994  110.309 -32.627 1.000 128.465 ? 486 PHE DDD CG  1 
ATOM   11015 C CD1 . PHE G 1 168 ? 74.289  108.973 -32.366 1.000 126.625 ? 486 PHE DDD CD1 1 
ATOM   11016 C CD2 . PHE G 1 168 ? 75.060  111.201 -32.732 1.000 125.629 ? 486 PHE DDD CD2 1 
ATOM   11017 C CE1 . PHE G 1 168 ? 75.603  108.553 -32.179 1.000 115.352 ? 486 PHE DDD CE1 1 
ATOM   11018 C CE2 . PHE G 1 168 ? 76.373  110.777 -32.551 1.000 111.386 ? 486 PHE DDD CE2 1 
ATOM   11019 C CZ  . PHE G 1 168 ? 76.643  109.455 -32.274 1.000 107.850 ? 486 PHE DDD CZ  1 
ATOM   11020 N N   . ASN G 1 169 ? 72.308  110.507 -29.331 1.000 80.840  ? 487 ASN DDD N   1 
ATOM   11021 C CA  . ASN G 1 169 ? 72.929  110.829 -28.012 1.000 77.067  ? 487 ASN DDD CA  1 
ATOM   11022 C C   . ASN G 1 169 ? 72.191  111.983 -27.322 1.000 63.812  ? 487 ASN DDD C   1 
ATOM   11023 O O   . ASN G 1 169 ? 72.812  112.685 -26.507 1.000 57.149  ? 487 ASN DDD O   1 
ATOM   11024 C CB  . ASN G 1 169 ? 74.424  111.137 -28.144 1.000 86.610  ? 487 ASN DDD CB  1 
ATOM   11025 C CG  . ASN G 1 169 ? 75.277  109.908 -28.383 1.000 95.482  ? 487 ASN DDD CG  1 
ATOM   11026 O OD1 . ASN G 1 169 ? 76.274  109.973 -29.098 1.000 109.387 ? 487 ASN DDD OD1 1 
ATOM   11027 N ND2 . ASN G 1 169 ? 74.912  108.787 -27.782 1.000 100.210 ? 487 ASN DDD ND2 1 
ATOM   11028 N N   . CYS G 1 170 ? 70.895  112.137 -27.578 1.000 58.917  ? 488 CYS DDD N   1 
ATOM   11029 C CA  . CYS G 1 170 ? 70.055  113.218 -26.995 1.000 61.191  ? 488 CYS DDD CA  1 
ATOM   11030 C C   . CYS G 1 170 ? 68.617  112.733 -26.824 1.000 53.895  ? 488 CYS DDD C   1 
ATOM   11031 O O   . CYS G 1 170 ? 67.860  112.775 -27.803 1.000 61.203  ? 488 CYS DDD O   1 
ATOM   11032 C CB  . CYS G 1 170 ? 70.088  114.456 -27.877 1.000 71.274  ? 488 CYS DDD CB  1 
ATOM   11033 S SG  . CYS G 1 170 ? 71.567  115.446 -27.560 1.000 91.575  ? 488 CYS DDD SG  1 
ATOM   11034 N N   . TYR G 1 171 ? 68.253  112.283 -25.626 1.000 45.393  ? 489 TYR DDD N   1 
ATOM   11035 C CA  . TYR G 1 171 ? 67.016  111.494 -25.428 1.000 45.874  ? 489 TYR DDD CA  1 
ATOM   11036 C C   . TYR G 1 171 ? 66.035  112.261 -24.553 1.000 43.206  ? 489 TYR DDD C   1 
ATOM   11037 O O   . TYR G 1 171 ? 66.474  112.979 -23.630 1.000 39.662  ? 489 TYR DDD O   1 
ATOM   11038 C CB  . TYR G 1 171 ? 67.329  110.127 -24.824 1.000 46.933  ? 489 TYR DDD CB  1 
ATOM   11039 C CG  . TYR G 1 171 ? 68.486  109.406 -25.461 1.000 46.200  ? 489 TYR DDD CG  1 
ATOM   11040 C CD1 . TYR G 1 171 ? 68.374  108.794 -26.702 1.000 46.556  ? 489 TYR DDD CD1 1 
ATOM   11041 C CD2 . TYR G 1 171 ? 69.701  109.338 -24.809 1.000 46.765  ? 489 TYR DDD CD2 1 
ATOM   11042 C CE1 . TYR G 1 171 ? 69.447  108.140 -27.285 1.000 48.286  ? 489 TYR DDD CE1 1 
ATOM   11043 C CE2 . TYR G 1 171 ? 70.777  108.665 -25.365 1.000 49.202  ? 489 TYR DDD CE2 1 
ATOM   11044 C CZ  . TYR G 1 171 ? 70.647  108.058 -26.600 1.000 51.232  ? 489 TYR DDD CZ  1 
ATOM   11045 O OH  . TYR G 1 171 ? 71.724  107.411 -27.129 1.000 58.046  ? 489 TYR DDD OH  1 
ATOM   11046 N N   . PHE G 1 172 ? 64.749  112.072 -24.855 1.000 42.974  ? 490 PHE DDD N   1 
ATOM   11047 C CA  . PHE G 1 172 ? 63.620  112.407 -23.959 1.000 45.314  ? 490 PHE DDD CA  1 
ATOM   11048 C C   . PHE G 1 172 ? 63.779  111.557 -22.712 1.000 46.951  ? 490 PHE DDD C   1 
ATOM   11049 O O   . PHE G 1 172 ? 63.926  110.350 -22.825 1.000 51.273  ? 490 PHE DDD O   1 
ATOM   11050 C CB  . PHE G 1 172 ? 62.288  112.134 -24.646 1.000 48.665  ? 490 PHE DDD CB  1 
ATOM   11051 C CG  . PHE G 1 172 ? 61.075  112.655 -23.921 1.000 55.774  ? 490 PHE DDD CG  1 
ATOM   11052 C CD1 . PHE G 1 172 ? 60.741  114.008 -23.946 1.000 63.689  ? 490 PHE DDD CD1 1 
ATOM   11053 C CD2 . PHE G 1 172 ? 60.226  111.779 -23.268 1.000 58.633  ? 490 PHE DDD CD2 1 
ATOM   11054 C CE1 . PHE G 1 172 ? 59.610  114.478 -23.294 1.000 68.901  ? 490 PHE DDD CE1 1 
ATOM   11055 C CE2 . PHE G 1 172 ? 59.081  112.249 -22.639 1.000 63.678  ? 490 PHE DDD CE2 1 
ATOM   11056 C CZ  . PHE G 1 172 ? 58.776  113.595 -22.648 1.000 68.413  ? 490 PHE DDD CZ  1 
ATOM   11057 N N   . PRO G 1 173 ? 63.771  112.142 -21.497 1.000 48.914  ? 491 PRO DDD N   1 
ATOM   11058 C CA  . PRO G 1 173 ? 64.254  111.435 -20.314 1.000 47.648  ? 491 PRO DDD CA  1 
ATOM   11059 C C   . PRO G 1 173 ? 63.243  110.439 -19.729 1.000 44.331  ? 491 PRO DDD C   1 
ATOM   11060 O O   . PRO G 1 173 ? 63.641  109.679 -18.897 1.000 46.258  ? 491 PRO DDD O   1 
ATOM   11061 C CB  . PRO G 1 173 ? 64.527  112.602 -19.350 1.000 50.580  ? 491 PRO DDD CB  1 
ATOM   11062 C CG  . PRO G 1 173 ? 63.446  113.588 -19.675 1.000 51.230  ? 491 PRO DDD CG  1 
ATOM   11063 C CD  . PRO G 1 173 ? 63.269  113.487 -21.176 1.000 51.175  ? 491 PRO DDD CD  1 
ATOM   11064 N N   . LEU G 1 174 ? 61.984  110.450 -20.173 1.000 44.289  ? 492 LEU DDD N   1 
ATOM   11065 C CA  . LEU G 1 174 ? 60.918  109.542 -19.656 1.000 46.946  ? 492 LEU DDD CA  1 
ATOM   11066 C C   . LEU G 1 174 ? 60.610  108.426 -20.660 1.000 48.055  ? 492 LEU DDD C   1 
ATOM   11067 O O   . LEU G 1 174 ? 60.363  108.723 -21.824 1.000 46.963  ? 492 LEU DDD O   1 
ATOM   11068 C CB  . LEU G 1 174 ? 59.646  110.342 -19.372 1.000 47.217  ? 492 LEU DDD CB  1 
ATOM   11069 C CG  . LEU G 1 174 ? 59.792  111.524 -18.418 1.000 47.944  ? 492 LEU DDD CG  1 
ATOM   11070 C CD1 . LEU G 1 174 ? 58.429  112.027 -17.974 1.000 46.722  ? 492 LEU DDD CD1 1 
ATOM   11071 C CD2 . LEU G 1 174 ? 60.602  111.155 -17.191 1.000 50.132  ? 492 LEU DDD CD2 1 
ATOM   11072 N N   . GLN G 1 175 ? 60.601  107.184 -20.184 1.000 53.983  ? 493 GLN DDD N   1 
ATOM   11073 C CA  . GLN G 1 175 ? 60.101  105.977 -20.893 1.000 55.578  ? 493 GLN DDD CA  1 
ATOM   11074 C C   . GLN G 1 175 ? 58.772  105.593 -20.258 1.000 54.508  ? 493 GLN DDD C   1 
ATOM   11075 O O   . GLN G 1 175 ? 58.558  105.912 -19.065 1.000 54.675  ? 493 GLN DDD O   1 
ATOM   11076 C CB  . GLN G 1 175 ? 61.075  104.814 -20.728 1.000 64.806  ? 493 GLN DDD CB  1 
ATOM   11077 C CG  . GLN G 1 175 ? 62.040  104.618 -21.886 1.000 71.147  ? 493 GLN DDD CG  1 
ATOM   11078 C CD  . GLN G 1 175 ? 61.732  103.331 -22.601 1.000 66.912  ? 493 GLN DDD CD  1 
ATOM   11079 O OE1 . GLN G 1 175 ? 60.579  103.106 -22.963 1.000 70.080  ? 493 GLN DDD OE1 1 
ATOM   11080 N NE2 . GLN G 1 175 ? 62.748  102.490 -22.776 1.000 57.922  ? 493 GLN DDD NE2 1 
ATOM   11081 N N   . SER G 1 176 ? 57.915  104.919 -21.014 1.000 54.811  ? 494 SER DDD N   1 
ATOM   11082 C CA  . SER G 1 176 ? 56.582  104.477 -20.535 1.000 52.844  ? 494 SER DDD CA  1 
ATOM   11083 C C   . SER G 1 176 ? 56.652  102.994 -20.150 1.000 50.384  ? 494 SER DDD C   1 
ATOM   11084 O O   . SER G 1 176 ? 57.377  102.244 -20.816 1.000 49.737  ? 494 SER DDD O   1 
ATOM   11085 C CB  . SER G 1 176 ? 55.551  104.756 -21.592 1.000 54.509  ? 494 SER DDD CB  1 
ATOM   11086 O OG  . SER G 1 176 ? 54.291  104.231 -21.219 1.000 58.383  ? 494 SER DDD OG  1 
ATOM   11087 N N   . TYR G 1 177 ? 55.943  102.581 -19.098 1.000 50.083  ? 495 TYR DDD N   1 
ATOM   11088 C CA  . TYR G 1 177 ? 55.654  101.149 -18.802 1.000 51.671  ? 495 TYR DDD CA  1 
ATOM   11089 C C   . TYR G 1 177 ? 54.636  100.656 -19.832 1.000 55.699  ? 495 TYR DDD C   1 
ATOM   11090 O O   . TYR G 1 177 ? 53.629  101.377 -20.067 1.000 57.388  ? 495 TYR DDD O   1 
ATOM   11091 C CB  . TYR G 1 177 ? 55.084  100.940 -17.395 1.000 46.913  ? 495 TYR DDD CB  1 
ATOM   11092 C CG  . TYR G 1 177 ? 56.086  101.093 -16.280 1.000 42.128  ? 495 TYR DDD CG  1 
ATOM   11093 C CD1 . TYR G 1 177 ? 57.220  100.311 -16.242 1.000 41.865  ? 495 TYR DDD CD1 1 
ATOM   11094 C CD2 . TYR G 1 177 ? 55.906  102.027 -15.271 1.000 41.354  ? 495 TYR DDD CD2 1 
ATOM   11095 C CE1 . TYR G 1 177 ? 58.152  100.450 -15.229 1.000 44.479  ? 495 TYR DDD CE1 1 
ATOM   11096 C CE2 . TYR G 1 177 ? 56.823  102.180 -14.247 1.000 41.613  ? 495 TYR DDD CE2 1 
ATOM   11097 C CZ  . TYR G 1 177 ? 57.947  101.377 -14.224 1.000 45.171  ? 495 TYR DDD CZ  1 
ATOM   11098 O OH  . TYR G 1 177 ? 58.871  101.497 -13.230 1.000 49.461  ? 495 TYR DDD OH  1 
ATOM   11099 N N   . GLY G 1 178 ? 54.890  99.489  -20.436 1.000 55.759  ? 496 GLY DDD N   1 
ATOM   11100 C CA  . GLY G 1 178 ? 53.996  98.853  -21.423 1.000 56.212  ? 496 GLY DDD CA  1 
ATOM   11101 C C   . GLY G 1 178 ? 53.111  97.818  -20.749 1.000 56.271  ? 496 GLY DDD C   1 
ATOM   11102 O O   . GLY G 1 178 ? 53.283  96.617  -21.045 1.000 73.337  ? 496 GLY DDD O   1 
ATOM   11103 N N   . PHE G 1 179 ? 52.210  98.256  -19.861 1.000 49.330  ? 497 PHE DDD N   1 
ATOM   11104 C CA  . PHE G 1 179 ? 51.434  97.379  -18.945 1.000 49.382  ? 497 PHE DDD CA  1 
ATOM   11105 C C   . PHE G 1 179 ? 50.309  96.670  -19.704 1.000 52.412  ? 497 PHE DDD C   1 
ATOM   11106 O O   . PHE G 1 179 ? 49.191  97.209  -19.769 1.000 45.963  ? 497 PHE DDD O   1 
ATOM   11107 C CB  . PHE G 1 179 ? 50.850  98.155  -17.759 1.000 50.023  ? 497 PHE DDD CB  1 
ATOM   11108 C CG  . PHE G 1 179 ? 51.830  98.558  -16.683 1.000 48.803  ? 497 PHE DDD CG  1 
ATOM   11109 C CD1 . PHE G 1 179 ? 52.872  97.728  -16.293 1.000 46.050  ? 497 PHE DDD CD1 1 
ATOM   11110 C CD2 . PHE G 1 179 ? 51.691  99.780  -16.043 1.000 49.109  ? 497 PHE DDD CD2 1 
ATOM   11111 C CE1 . PHE G 1 179 ? 53.768  98.132  -15.317 1.000 46.052  ? 497 PHE DDD CE1 1 
ATOM   11112 C CE2 . PHE G 1 179 ? 52.589  100.177 -15.068 1.000 47.284  ? 497 PHE DDD CE2 1 
ATOM   11113 C CZ  . PHE G 1 179 ? 53.624  99.352  -14.702 1.000 46.572  ? 497 PHE DDD CZ  1 
ATOM   11114 N N   . GLN G 1 180 ? 50.606  95.467  -20.212 1.000 59.644  ? 498 GLN DDD N   1 
ATOM   11115 C CA  . GLN G 1 180 ? 49.644  94.548  -20.877 1.000 61.655  ? 498 GLN DDD CA  1 
ATOM   11116 C C   . GLN G 1 180 ? 49.203  93.492  -19.865 1.000 62.130  ? 498 GLN DDD C   1 
ATOM   11117 O O   . GLN G 1 180 ? 50.002  93.067  -19.023 1.000 57.034  ? 498 GLN DDD O   1 
ATOM   11118 C CB  . GLN G 1 180 ? 50.273  93.909  -22.119 1.000 65.521  ? 498 GLN DDD CB  1 
ATOM   11119 C CG  . GLN G 1 180 ? 51.053  94.891  -22.986 1.000 66.210  ? 498 GLN DDD CG  1 
ATOM   11120 C CD  . GLN G 1 180 ? 51.261  94.389  -24.393 1.000 69.643  ? 498 GLN DDD CD  1 
ATOM   11121 O OE1 . GLN G 1 180 ? 50.322  94.326  -25.181 1.000 73.553  ? 498 GLN DDD OE1 1 
ATOM   11122 N NE2 . GLN G 1 180 ? 52.494  94.024  -24.718 1.000 69.554  ? 498 GLN DDD NE2 1 
ATOM   11123 N N   . PRO G 1 181 ? 47.917  93.060  -19.907 1.000 63.775  ? 499 PRO DDD N   1 
ATOM   11124 C CA  . PRO G 1 181 ? 47.388  92.077  -18.957 1.000 64.141  ? 499 PRO DDD CA  1 
ATOM   11125 C C   . PRO G 1 181 ? 48.125  90.733  -18.987 1.000 65.196  ? 499 PRO DDD C   1 
ATOM   11126 O O   . PRO G 1 181 ? 48.204  90.082  -17.980 1.000 63.014  ? 499 PRO DDD O   1 
ATOM   11127 C CB  . PRO G 1 181 ? 45.936  91.876  -19.413 1.000 67.066  ? 499 PRO DDD CB  1 
ATOM   11128 C CG  . PRO G 1 181 ? 45.596  93.145  -20.159 1.000 68.246  ? 499 PRO DDD CG  1 
ATOM   11129 C CD  . PRO G 1 181 ? 46.886  93.533  -20.846 1.000 66.487  ? 499 PRO DDD CD  1 
ATOM   11130 N N   . THR G 1 182 ? 48.657  90.368  -20.149 1.000 70.479  ? 500 THR DDD N   1 
ATOM   11131 C CA  . THR G 1 182 ? 49.303  89.063  -20.437 1.000 69.191  ? 500 THR DDD CA  1 
ATOM   11132 C C   . THR G 1 182 ? 50.797  89.103  -20.092 1.000 61.631  ? 500 THR DDD C   1 
ATOM   11133 O O   . THR G 1 182 ? 51.451  88.072  -20.287 1.000 56.273  ? 500 THR DDD O   1 
ATOM   11134 C CB  . THR G 1 182 ? 49.066  88.710  -21.911 1.000 77.918  ? 500 THR DDD CB  1 
ATOM   11135 O OG1 . THR G 1 182 ? 49.741  89.693  -22.700 1.000 86.505  ? 500 THR DDD OG1 1 
ATOM   11136 C CG2 . THR G 1 182 ? 47.593  88.675  -22.271 1.000 80.611  ? 500 THR DDD CG2 1 
ATOM   11137 N N   . ASN G 1 183 ? 51.324  90.243  -19.627 1.000 61.495  ? 501 ASN DDD N   1 
ATOM   11138 C CA  . ASN G 1 183 ? 52.738  90.379  -19.180 1.000 62.853  ? 501 ASN DDD CA  1 
ATOM   11139 C C   . ASN G 1 183 ? 52.959  89.461  -17.978 1.000 56.408  ? 501 ASN DDD C   1 
ATOM   11140 O O   . ASN G 1 183 ? 51.986  89.266  -17.231 1.000 45.635  ? 501 ASN DDD O   1 
ATOM   11141 C CB  . ASN G 1 183 ? 53.100  91.798  -18.730 1.000 69.549  ? 501 ASN DDD CB  1 
ATOM   11142 C CG  . ASN G 1 183 ? 53.119  92.828  -19.837 1.000 67.653  ? 501 ASN DDD CG  1 
ATOM   11143 O OD1 . ASN G 1 183 ? 52.714  93.969  -19.623 1.000 71.538  ? 501 ASN DDD OD1 1 
ATOM   11144 N ND2 . ASN G 1 183 ? 53.603  92.444  -21.005 1.000 61.148  ? 501 ASN DDD ND2 1 
ATOM   11145 N N   . GLY G 1 184 ? 54.189  88.959  -17.793 1.000 57.559  ? 502 GLY DDD N   1 
ATOM   11146 C CA  . GLY G 1 184 ? 54.579  88.139  -16.627 1.000 62.774  ? 502 GLY DDD CA  1 
ATOM   11147 C C   . GLY G 1 184 ? 54.547  88.962  -15.354 1.000 66.927  ? 502 GLY DDD C   1 
ATOM   11148 O O   . GLY G 1 184 ? 54.819  90.157  -15.456 1.000 83.655  ? 502 GLY DDD O   1 
ATOM   11149 N N   . VAL G 1 185 ? 54.197  88.382  -14.199 1.000 71.261  ? 503 VAL DDD N   1 
ATOM   11150 C CA  . VAL G 1 185 ? 54.285  89.098  -12.887 1.000 69.373  ? 503 VAL DDD CA  1 
ATOM   11151 C C   . VAL G 1 185 ? 55.687  89.694  -12.851 1.000 69.485  ? 503 VAL DDD C   1 
ATOM   11152 O O   . VAL G 1 185 ? 56.627  88.983  -13.271 1.000 70.323  ? 503 VAL DDD O   1 
ATOM   11153 C CB  . VAL G 1 185 ? 54.019  88.197  -11.664 1.000 70.354  ? 503 VAL DDD CB  1 
ATOM   11154 C CG1 . VAL G 1 185 ? 54.559  88.806  -10.377 1.000 69.172  ? 503 VAL DDD CG1 1 
ATOM   11155 C CG2 . VAL G 1 185 ? 52.541  87.883  -11.507 1.000 73.460  ? 503 VAL DDD CG2 1 
ATOM   11156 N N   . GLY G 1 186 ? 55.822  90.951  -12.436 1.000 64.219  ? 504 GLY DDD N   1 
ATOM   11157 C CA  . GLY G 1 186 ? 57.141  91.608  -12.411 1.000 68.504  ? 504 GLY DDD CA  1 
ATOM   11158 C C   . GLY G 1 186 ? 57.289  92.575  -13.567 1.000 68.153  ? 504 GLY DDD C   1 
ATOM   11159 O O   . GLY G 1 186 ? 58.037  93.555  -13.422 1.000 83.200  ? 504 GLY DDD O   1 
ATOM   11160 N N   . TYR G 1 187 ? 56.613  92.312  -14.680 1.000 58.978  ? 505 TYR DDD N   1 
ATOM   11161 C CA  . TYR G 1 187 ? 56.326  93.322  -15.719 1.000 56.434  ? 505 TYR DDD CA  1 
ATOM   11162 C C   . TYR G 1 187 ? 54.900  93.842  -15.519 1.000 51.129  ? 505 TYR DDD C   1 
ATOM   11163 O O   . TYR G 1 187 ? 54.528  94.792  -16.198 1.000 57.526  ? 505 TYR DDD O   1 
ATOM   11164 C CB  . TYR G 1 187 ? 56.584  92.741  -17.107 1.000 61.070  ? 505 TYR DDD CB  1 
ATOM   11165 C CG  . TYR G 1 187 ? 57.970  93.013  -17.622 1.000 69.408  ? 505 TYR DDD CG  1 
ATOM   11166 C CD1 . TYR G 1 187 ? 58.948  92.030  -17.657 1.000 73.098  ? 505 TYR DDD CD1 1 
ATOM   11167 C CD2 . TYR G 1 187 ? 58.301  94.281  -18.075 1.000 78.295  ? 505 TYR DDD CD2 1 
ATOM   11168 C CE1 . TYR G 1 187 ? 60.218  92.303  -18.152 1.000 82.231  ? 505 TYR DDD CE1 1 
ATOM   11169 C CE2 . TYR G 1 187 ? 59.564  94.570  -18.564 1.000 82.345  ? 505 TYR DDD CE2 1 
ATOM   11170 C CZ  . TYR G 1 187 ? 60.529  93.582  -18.606 1.000 82.124  ? 505 TYR DDD CZ  1 
ATOM   11171 O OH  . TYR G 1 187 ? 61.756  93.945  -19.089 1.000 81.252  ? 505 TYR DDD OH  1 
ATOM   11172 N N   . GLN G 1 188 ? 54.129  93.274  -14.598 1.000 45.975  ? 506 GLN DDD N   1 
ATOM   11173 C CA  . GLN G 1 188 ? 52.761  93.787  -14.343 1.000 48.530  ? 506 GLN DDD CA  1 
ATOM   11174 C C   . GLN G 1 188 ? 52.872  94.935  -13.362 1.000 45.340  ? 506 GLN DDD C   1 
ATOM   11175 O O   . GLN G 1 188 ? 53.840  95.017  -12.613 1.000 42.605  ? 506 GLN DDD O   1 
ATOM   11176 C CB  . GLN G 1 188 ? 51.833  92.733  -13.758 1.000 54.794  ? 506 GLN DDD CB  1 
ATOM   11177 C CG  . GLN G 1 188 ? 52.111  91.356  -14.304 1.000 57.902  ? 506 GLN DDD CG  1 
ATOM   11178 C CD  . GLN G 1 188 ? 51.013  90.375  -14.002 1.000 55.684  ? 506 GLN DDD CD  1 
ATOM   11179 O OE1 . GLN G 1 188 ? 50.000  90.687  -13.376 1.000 47.554  ? 506 GLN DDD OE1 1 
ATOM   11180 N NE2 . GLN G 1 188 ? 51.229  89.160  -14.463 1.000 64.859  ? 506 GLN DDD NE2 1 
ATOM   11181 N N   . PRO G 1 189 ? 51.874  95.837  -13.335 1.000 45.606  ? 507 PRO DDD N   1 
ATOM   11182 C CA  . PRO G 1 189 ? 51.893  96.975  -12.421 1.000 48.053  ? 507 PRO DDD CA  1 
ATOM   11183 C C   . PRO G 1 189 ? 51.584  96.593  -10.968 1.000 46.206  ? 507 PRO DDD C   1 
ATOM   11184 O O   . PRO G 1 189 ? 50.753  95.754  -10.749 1.000 46.936  ? 507 PRO DDD O   1 
ATOM   11185 C CB  . PRO G 1 189 ? 50.787  97.886  -12.978 1.000 49.440  ? 507 PRO DDD CB  1 
ATOM   11186 C CG  . PRO G 1 189 ? 49.817  96.936  -13.613 1.000 49.243  ? 507 PRO DDD CG  1 
ATOM   11187 C CD  . PRO G 1 189 ? 50.684  95.833  -14.199 1.000 48.703  ? 507 PRO DDD CD  1 
ATOM   11188 N N   . TYR G 1 190 ? 52.278  97.231  -10.026 1.000 48.534  ? 508 TYR DDD N   1 
ATOM   11189 C CA  . TYR G 1 190 ? 52.026  97.177  -8.564  1.000 49.355  ? 508 TYR DDD CA  1 
ATOM   11190 C C   . TYR G 1 190 ? 51.890  98.613  -8.057  1.000 42.655  ? 508 TYR DDD C   1 
ATOM   11191 O O   . TYR G 1 190 ? 52.773  99.432  -8.306  1.000 40.819  ? 508 TYR DDD O   1 
ATOM   11192 C CB  . TYR G 1 190 ? 53.175  96.485  -7.821  1.000 56.401  ? 508 TYR DDD CB  1 
ATOM   11193 C CG  . TYR G 1 190 ? 53.223  94.984  -7.960  1.000 65.829  ? 508 TYR DDD CG  1 
ATOM   11194 C CD1 . TYR G 1 190 ? 53.526  94.390  -9.177  1.000 77.475  ? 508 TYR DDD CD1 1 
ATOM   11195 C CD2 . TYR G 1 190 ? 52.998  94.153  -6.873  1.000 65.318  ? 508 TYR DDD CD2 1 
ATOM   11196 C CE1 . TYR G 1 190 ? 53.576  93.010  -9.316  1.000 80.160  ? 508 TYR DDD CE1 1 
ATOM   11197 C CE2 . TYR G 1 190 ? 53.055  92.775  -6.992  1.000 69.134  ? 508 TYR DDD CE2 1 
ATOM   11198 C CZ  . TYR G 1 190 ? 53.345  92.202  -8.216  1.000 76.458  ? 508 TYR DDD CZ  1 
ATOM   11199 O OH  . TYR G 1 190 ? 53.408  90.847  -8.340  1.000 90.000  ? 508 TYR DDD OH  1 
ATOM   11200 N N   . ARG G 1 191 ? 50.807  98.907  -7.360  1.000 40.776  ? 509 ARG DDD N   1 
ATOM   11201 C CA  . ARG G 1 191 ? 50.635  100.177 -6.621  1.000 42.117  ? 509 ARG DDD CA  1 
ATOM   11202 C C   . ARG G 1 191 ? 51.415  100.092 -5.319  1.000 40.958  ? 509 ARG DDD C   1 
ATOM   11203 O O   . ARG G 1 191 ? 51.331  99.073  -4.668  1.000 46.003  ? 509 ARG DDD O   1 
ATOM   11204 C CB  . ARG G 1 191 ? 49.158  100.438 -6.339  1.000 44.848  ? 509 ARG DDD CB  1 
ATOM   11205 C CG  . ARG G 1 191 ? 48.360  100.605 -7.618  1.000 46.713  ? 509 ARG DDD CG  1 
ATOM   11206 C CD  . ARG G 1 191 ? 46.945  101.030 -7.369  1.000 49.462  ? 509 ARG DDD CD  1 
ATOM   11207 N NE  . ARG G 1 191 ? 46.354  101.364 -8.651  1.000 52.944  ? 509 ARG DDD NE  1 
ATOM   11208 C CZ  . ARG G 1 191 ? 45.245  102.070 -8.804  1.000 56.760  ? 509 ARG DDD CZ  1 
ATOM   11209 N NH1 . ARG G 1 191 ? 44.579  102.512 -7.749  1.000 60.317  ? 509 ARG DDD NH1 1 
ATOM   11210 N NH2 . ARG G 1 191 ? 44.795  102.314 -10.016 1.000 58.725  ? 509 ARG DDD NH2 1 
ATOM   11211 N N   . VAL G 1 192 ? 52.140  101.147 -4.978  1.000 40.076  ? 510 VAL DDD N   1 
ATOM   11212 C CA  . VAL G 1 192 ? 52.965  101.243 -3.745  1.000 38.708  ? 510 VAL DDD CA  1 
ATOM   11213 C C   . VAL G 1 192 ? 52.454  102.419 -2.921  1.000 38.433  ? 510 VAL DDD C   1 
ATOM   11214 O O   . VAL G 1 192 ? 52.086  103.433 -3.512  1.000 40.694  ? 510 VAL DDD O   1 
ATOM   11215 C CB  . VAL G 1 192 ? 54.446  101.420 -4.116  1.000 39.363  ? 510 VAL DDD CB  1 
ATOM   11216 C CG1 . VAL G 1 192 ? 55.344  101.482 -2.893  1.000 37.838  ? 510 VAL DDD CG1 1 
ATOM   11217 C CG2 . VAL G 1 192 ? 54.880  100.310 -5.058  1.000 40.122  ? 510 VAL DDD CG2 1 
ATOM   11218 N N   . VAL G 1 193 ? 52.459  102.283 -1.602  1.000 37.938  ? 511 VAL DDD N   1 
ATOM   11219 C CA  . VAL G 1 193 ? 52.297  103.416 -0.652  1.000 39.885  ? 511 VAL DDD CA  1 
ATOM   11220 C C   . VAL G 1 193 ? 53.462  103.358 0.329   1.000 41.886  ? 511 VAL DDD C   1 
ATOM   11221 O O   . VAL G 1 193 ? 53.662  102.275 0.927   1.000 45.624  ? 511 VAL DDD O   1 
ATOM   11222 C CB  . VAL G 1 193 ? 50.960  103.349 0.102   1.000 40.657  ? 511 VAL DDD CB  1 
ATOM   11223 C CG1 . VAL G 1 193 ? 50.864  104.435 1.157   1.000 42.129  ? 511 VAL DDD CG1 1 
ATOM   11224 C CG2 . VAL G 1 193 ? 49.787  103.424 -0.851  1.000 42.510  ? 511 VAL DDD CG2 1 
ATOM   11225 N N   . VAL G 1 194 ? 54.168  104.473 0.515   1.000 40.430  ? 512 VAL DDD N   1 
ATOM   11226 C CA  . VAL G 1 194 ? 55.274  104.580 1.504   1.000 42.197  ? 512 VAL DDD CA  1 
ATOM   11227 C C   . VAL G 1 194 ? 54.845  105.536 2.614   1.000 47.307  ? 512 VAL DDD C   1 
ATOM   11228 O O   . VAL G 1 194 ? 54.844  106.782 2.367   1.000 54.563  ? 512 VAL DDD O   1 
ATOM   11229 C CB  . VAL G 1 194 ? 56.597  105.010 0.852   1.000 40.125  ? 512 VAL DDD CB  1 
ATOM   11230 C CG1 . VAL G 1 194 ? 57.740  104.974 1.855   1.000 41.372  ? 512 VAL DDD CG1 1 
ATOM   11231 C CG2 . VAL G 1 194 ? 56.921  104.147 -0.351  1.000 39.569  ? 512 VAL DDD CG2 1 
ATOM   11232 N N   . LEU G 1 195 ? 54.501  104.955 3.773   1.000 44.985  ? 513 LEU DDD N   1 
ATOM   11233 C CA  . LEU G 1 195 ? 54.331  105.665 5.064   1.000 44.464  ? 513 LEU DDD CA  1 
ATOM   11234 C C   . LEU G 1 195 ? 55.725  106.017 5.590   1.000 44.773  ? 513 LEU DDD C   1 
ATOM   11235 O O   . LEU G 1 195 ? 56.550  105.107 5.659   1.000 41.720  ? 513 LEU DDD O   1 
ATOM   11236 C CB  . LEU G 1 195 ? 53.575  104.761 6.041   1.000 44.288  ? 513 LEU DDD CB  1 
ATOM   11237 C CG  . LEU G 1 195 ? 52.248  104.191 5.543   1.000 50.448  ? 513 LEU DDD CG  1 
ATOM   11238 C CD1 . LEU G 1 195 ? 51.560  103.393 6.644   1.000 54.041  ? 513 LEU DDD CD1 1 
ATOM   11239 C CD2 . LEU G 1 195 ? 51.306  105.274 5.039   1.000 50.081  ? 513 LEU DDD CD2 1 
ATOM   11240 N N   . SER G 1 196 ? 55.985  107.302 5.864   1.000 48.928  ? 514 SER DDD N   1 
ATOM   11241 C CA  . SER G 1 196 ? 57.208  107.805 6.549   1.000 53.551  ? 514 SER DDD CA  1 
ATOM   11242 C C   . SER G 1 196 ? 56.782  108.613 7.782   1.000 59.457  ? 514 SER DDD C   1 
ATOM   11243 O O   . SER G 1 196 ? 55.724  109.274 7.715   1.000 58.254  ? 514 SER DDD O   1 
ATOM   11244 C CB  . SER G 1 196 ? 58.087  108.607 5.616   1.000 52.568  ? 514 SER DDD CB  1 
ATOM   11245 O OG  . SER G 1 196 ? 57.335  109.538 4.855   1.000 54.639  ? 514 SER DDD OG  1 
ATOM   11246 N N   . PHE G 1 197 ? 57.551  108.523 8.873   1.000 65.412  ? 515 PHE DDD N   1 
ATOM   11247 C CA  . PHE G 1 197 ? 57.218  109.081 10.214  1.000 63.099  ? 515 PHE DDD CA  1 
ATOM   11248 C C   . PHE G 1 197 ? 58.386  109.922 10.738  1.000 68.758  ? 515 PHE DDD C   1 
ATOM   11249 O O   . PHE G 1 197 ? 59.524  109.423 10.763  1.000 56.874  ? 515 PHE DDD O   1 
ATOM   11250 C CB  . PHE G 1 197 ? 56.937  107.963 11.222  1.000 59.916  ? 515 PHE DDD CB  1 
ATOM   11251 C CG  . PHE G 1 197 ? 55.889  106.966 10.802  1.000 56.017  ? 515 PHE DDD CG  1 
ATOM   11252 C CD1 . PHE G 1 197 ? 54.579  107.097 11.228  1.000 57.280  ? 515 PHE DDD CD1 1 
ATOM   11253 C CD2 . PHE G 1 197 ? 56.215  105.890 9.994   1.000 55.137  ? 515 PHE DDD CD2 1 
ATOM   11254 C CE1 . PHE G 1 197 ? 53.610  106.181 10.845  1.000 59.042  ? 515 PHE DDD CE1 1 
ATOM   11255 C CE2 . PHE G 1 197 ? 55.245  104.982 9.599   1.000 60.354  ? 515 PHE DDD CE2 1 
ATOM   11256 C CZ  . PHE G 1 197 ? 53.944  105.117 10.040  1.000 60.392  ? 515 PHE DDD CZ  1 
ATOM   11257 N N   . GLU G 1 198 ? 58.106  111.156 11.166  1.000 87.605  ? 516 GLU DDD N   1 
ATOM   11258 C CA  . GLU G 1 198 ? 59.100  112.069 11.796  1.000 100.040 ? 516 GLU DDD CA  1 
ATOM   11259 C C   . GLU G 1 198 ? 58.543  112.521 13.151  1.000 106.239 ? 516 GLU DDD C   1 
ATOM   11260 O O   . GLU G 1 198 ? 57.313  112.658 13.262  1.000 96.918  ? 516 GLU DDD O   1 
ATOM   11261 C CB  . GLU G 1 198 ? 59.426  113.256 10.876  1.000 110.095 ? 516 GLU DDD CB  1 
ATOM   11262 C CG  . GLU G 1 198 ? 58.233  114.165 10.577  1.000 119.153 ? 516 GLU DDD CG  1 
ATOM   11263 C CD  . GLU G 1 198 ? 58.496  115.366 9.677   1.000 118.487 ? 516 GLU DDD CD  1 
ATOM   11264 O OE1 . GLU G 1 198 ? 59.447  115.315 8.874   1.000 117.571 ? 516 GLU DDD OE1 1 
ATOM   11265 O OE2 . GLU G 1 198 ? 57.736  116.350 9.769   1.000 105.882 ? 516 GLU DDD OE2 1 
ATOM   11266 N N   . LEU G 1 199 ? 59.426  112.714 14.136  1.000 117.056 ? 517 LEU DDD N   1 
ATOM   11267 C CA  . LEU G 1 199 ? 59.098  113.245 15.489  1.000 123.448 ? 517 LEU DDD CA  1 
ATOM   11268 C C   . LEU G 1 199 ? 60.096  114.368 15.810  1.000 128.328 ? 517 LEU DDD C   1 
ATOM   11269 O O   . LEU G 1 199 ? 61.272  114.064 16.093  1.000 118.236 ? 517 LEU DDD O   1 
ATOM   11270 C CB  . LEU G 1 199 ? 59.145  112.094 16.507  1.000 115.546 ? 517 LEU DDD CB  1 
ATOM   11271 C CG  . LEU G 1 199 ? 58.344  112.281 17.799  1.000 103.006 ? 517 LEU DDD CG  1 
ATOM   11272 C CD1 . LEU G 1 199 ? 57.972  110.932 18.402  1.000 97.475  ? 517 LEU DDD CD1 1 
ATOM   11273 C CD2 . LEU G 1 199 ? 59.116  113.130 18.810  1.000 99.898  ? 517 LEU DDD CD2 1 
ATOM   11274 N N   . LEU G 1 200 ? 59.648  115.620 15.700  1.000 141.558 ? 518 LEU DDD N   1 
ATOM   11275 C CA  . LEU G 1 200 ? 60.435  116.842 16.017  1.000 155.265 ? 518 LEU DDD CA  1 
ATOM   11276 C C   . LEU G 1 200 ? 60.061  117.298 17.433  1.000 161.816 ? 518 LEU DDD C   1 
ATOM   11277 O O   . LEU G 1 200 ? 59.188  116.643 18.046  1.000 153.366 ? 518 LEU DDD O   1 
ATOM   11278 C CB  . LEU G 1 200 ? 60.127  117.920 14.968  1.000 148.735 ? 518 LEU DDD CB  1 
ATOM   11279 C CG  . LEU G 1 200 ? 60.109  117.450 13.512  1.000 134.466 ? 518 LEU DDD CG  1 
ATOM   11280 C CD1 . LEU G 1 200 ? 59.560  118.536 12.607  1.000 127.630 ? 518 LEU DDD CD1 1 
ATOM   11281 C CD2 . LEU G 1 200 ? 61.495  117.026 13.051  1.000 123.118 ? 518 LEU DDD CD2 1 
ATOM   11282 N N   . HIS G 1 201 ? 60.703  118.359 17.937  1.000 158.945 ? 519 HIS DDD N   1 
ATOM   11283 C CA  . HIS G 1 201 ? 60.383  118.985 19.249  1.000 143.027 ? 519 HIS DDD CA  1 
ATOM   11284 C C   . HIS G 1 201 ? 59.294  120.048 19.000  1.000 125.733 ? 519 HIS DDD C   1 
ATOM   11285 O O   . HIS G 1 201 ? 59.521  121.230 19.329  1.000 105.699 ? 519 HIS DDD O   1 
ATOM   11286 C CB  . HIS G 1 201 ? 61.669  119.486 19.951  1.000 141.328 ? 519 HIS DDD CB  1 
ATOM   11287 C CG  . HIS G 1 201 ? 62.675  118.425 20.296  1.000 136.932 ? 519 HIS DDD CG  1 
ATOM   11288 N ND1 . HIS G 1 201 ? 62.611  117.676 21.467  1.000 130.879 ? 519 HIS DDD ND1 1 
ATOM   11289 C CD2 . HIS G 1 201 ? 63.781  117.997 19.643  1.000 121.267 ? 519 HIS DDD CD2 1 
ATOM   11290 C CE1 . HIS G 1 201 ? 63.621  116.829 21.507  1.000 116.185 ? 519 HIS DDD CE1 1 
ATOM   11291 N NE2 . HIS G 1 201 ? 64.354  117.005 20.398  1.000 118.145 ? 519 HIS DDD NE2 1 
ATOM   11292 N N   . ALA G 1 202 ? 58.166  119.628 18.404  1.000 121.357 ? 520 ALA DDD N   1 
ATOM   11293 C CA  . ALA G 1 202 ? 56.935  120.411 18.118  1.000 112.971 ? 520 ALA DDD CA  1 
ATOM   11294 C C   . ALA G 1 202 ? 55.725  119.568 18.535  1.000 107.436 ? 520 ALA DDD C   1 
ATOM   11295 O O   . ALA G 1 202 ? 55.889  118.398 18.866  1.000 99.994  ? 520 ALA DDD O   1 
ATOM   11296 C CB  . ALA G 1 202 ? 56.896  120.773 16.646  1.000 105.157 ? 520 ALA DDD CB  1 
ATOM   11297 N N   . PRO G 1 203 ? 54.480  120.103 18.557  1.000 113.158 ? 521 PRO DDD N   1 
ATOM   11298 C CA  . PRO G 1 203 ? 53.306  119.292 18.903  1.000 114.469 ? 521 PRO DDD CA  1 
ATOM   11299 C C   . PRO G 1 203 ? 53.137  118.063 17.990  1.000 112.747 ? 521 PRO DDD C   1 
ATOM   11300 O O   . PRO G 1 203 ? 53.426  118.179 16.817  1.000 124.366 ? 521 PRO DDD O   1 
ATOM   11301 C CB  . PRO G 1 203 ? 52.105  120.243 18.718  1.000 112.087 ? 521 PRO DDD CB  1 
ATOM   11302 C CG  . PRO G 1 203 ? 52.697  121.646 18.745  1.000 115.457 ? 521 PRO DDD CG  1 
ATOM   11303 C CD  . PRO G 1 203 ? 54.130  121.504 18.265  1.000 116.998 ? 521 PRO DDD CD  1 
ATOM   11304 N N   . ALA G 1 204 ? 52.675  116.933 18.535  1.000 102.486 ? 522 ALA DDD N   1 
ATOM   11305 C CA  . ALA G 1 204 ? 52.315  115.708 17.777  1.000 103.056 ? 522 ALA DDD CA  1 
ATOM   11306 C C   . ALA G 1 204 ? 50.803  115.694 17.507  1.000 102.571 ? 522 ALA DDD C   1 
ATOM   11307 O O   . ALA G 1 204 ? 50.053  115.944 18.455  1.000 127.200 ? 522 ALA DDD O   1 
ATOM   11308 C CB  . ALA G 1 204 ? 52.752  114.490 18.552  1.000 101.468 ? 522 ALA DDD CB  1 
ATOM   11309 N N   . THR G 1 205 ? 50.370  115.432 16.271  1.000 97.153  ? 523 THR DDD N   1 
ATOM   11310 C CA  . THR G 1 205 ? 48.946  115.560 15.847  1.000 102.870 ? 523 THR DDD CA  1 
ATOM   11311 C C   . THR G 1 205 ? 48.422  114.263 15.208  1.000 112.075 ? 523 THR DDD C   1 
ATOM   11312 O O   . THR G 1 205 ? 47.191  114.210 14.946  1.000 104.629 ? 523 THR DDD O   1 
ATOM   11313 C CB  . THR G 1 205 ? 48.764  116.758 14.904  1.000 106.424 ? 523 THR DDD CB  1 
ATOM   11314 O OG1 . THR G 1 205 ? 49.633  116.608 13.782  1.000 113.863 ? 523 THR DDD OG1 1 
ATOM   11315 C CG2 . THR G 1 205 ? 49.053  118.089 15.563  1.000 107.829 ? 523 THR DDD CG2 1 
ATOM   11316 N N   . VAL G 1 206 ? 49.293  113.274 14.946  1.000 125.131 ? 524 VAL DDD N   1 
ATOM   11317 C CA  . VAL G 1 206 ? 48.915  111.948 14.360  1.000 133.342 ? 524 VAL DDD CA  1 
ATOM   11318 C C   . VAL G 1 206 ? 49.181  110.859 15.404  1.000 135.658 ? 524 VAL DDD C   1 
ATOM   11319 O O   . VAL G 1 206 ? 50.378  110.538 15.635  1.000 139.782 ? 524 VAL DDD O   1 
ATOM   11320 C CB  . VAL G 1 206 ? 49.656  111.633 13.045  1.000 131.510 ? 524 VAL DDD CB  1 
ATOM   11321 C CG1 . VAL G 1 206 ? 49.105  110.368 12.400  1.000 127.532 ? 524 VAL DDD CG1 1 
ATOM   11322 C CG2 . VAL G 1 206 ? 49.607  112.791 12.055  1.000 139.513 ? 524 VAL DDD CG2 1 
ATOM   11323 N N   . CYS G 1 207 ? 48.105  110.303 15.972  1.000 127.004 ? 525 CYS DDD N   1 
ATOM   11324 C CA  . CYS G 1 207 ? 48.124  109.380 17.136  1.000 120.328 ? 525 CYS DDD CA  1 
ATOM   11325 C C   . CYS G 1 207 ? 47.245  108.163 16.858  1.000 114.557 ? 525 CYS DDD C   1 
ATOM   11326 O O   . CYS G 1 207 ? 46.306  108.286 16.044  1.000 98.022  ? 525 CYS DDD O   1 
ATOM   11327 C CB  . CYS G 1 207 ? 47.610  110.095 18.376  1.000 124.033 ? 525 CYS DDD CB  1 
ATOM   11328 S SG  . CYS G 1 207 ? 48.680  111.469 18.864  1.000 157.578 ? 525 CYS DDD SG  1 
ATOM   11329 N N   . GLY G 1 208 ? 47.537  107.048 17.530  1.000 120.373 ? 526 GLY DDD N   1 
ATOM   11330 C CA  . GLY G 1 208 ? 46.707  105.831 17.484  1.000 126.213 ? 526 GLY DDD CA  1 
ATOM   11331 C C   . GLY G 1 208 ? 45.510  105.929 18.426  1.000 123.637 ? 526 GLY DDD C   1 
ATOM   11332 O O   . GLY G 1 208 ? 45.467  106.836 19.257  1.000 107.280 ? 526 GLY DDD O   1 
ATOM   11333 N N   . PRO G 1 209 ? 44.504  105.020 18.310  1.000 127.072 ? 527 PRO DDD N   1 
ATOM   11334 C CA  . PRO G 1 209 ? 43.330  105.045 19.187  1.000 125.661 ? 527 PRO DDD CA  1 
ATOM   11335 C C   . PRO G 1 209 ? 43.711  104.927 20.675  1.000 125.609 ? 527 PRO DDD C   1 
ATOM   11336 O O   . PRO G 1 209 ? 43.051  105.555 21.484  1.000 126.994 ? 527 PRO DDD O   1 
ATOM   11337 C CB  . PRO G 1 209 ? 42.446  103.865 18.722  1.000 114.579 ? 527 PRO DDD CB  1 
ATOM   11338 C CG  . PRO G 1 209 ? 43.333  103.018 17.818  1.000 111.688 ? 527 PRO DDD CG  1 
ATOM   11339 C CD  . PRO G 1 209 ? 44.431  103.934 17.316  1.000 115.227 ? 527 PRO DDD CD  1 
ATOM   11340 N N   . LYS G 1 210 ? 44.758  104.151 20.997  1.000 125.143 ? 528 LYS DDD N   1 
ATOM   11341 C CA  . LYS G 1 210 ? 45.356  104.042 22.360  1.000 121.978 ? 528 LYS DDD CA  1 
ATOM   11342 C C   . LYS G 1 210 ? 46.294  105.238 22.573  1.000 115.311 ? 528 LYS DDD C   1 
ATOM   11343 O O   . LYS G 1 210 ? 46.201  106.096 23.436  1.000 103.545 ? 528 LYS DDD O   1 
ATOM   11344 C CB  . LYS G 1 210 ? 46.115  102.720 22.527  1.000 108.418 ? 528 LYS DDD CB  1 
ATOM   11345 N N   . GLN H 2 1   ? 47.288  89.677  17.189  1.000 95.409  ? 1   GLN FFF N   1 
ATOM   11346 C CA  . GLN H 2 1   ? 48.502  89.029  17.781  1.000 93.404  ? 1   GLN FFF CA  1 
ATOM   11347 C C   . GLN H 2 1   ? 48.747  87.720  17.033  1.000 83.517  ? 1   GLN FFF C   1 
ATOM   11348 O O   . GLN H 2 1   ? 47.750  87.116  16.630  1.000 81.258  ? 1   GLN FFF O   1 
ATOM   11349 C CB  . GLN H 2 1   ? 48.305  88.770  19.279  1.000 104.686 ? 1   GLN FFF CB  1 
ATOM   11350 C CG  . GLN H 2 1   ? 49.451  88.009  19.951  1.000 117.480 ? 1   GLN FFF CG  1 
ATOM   11351 C CD  . GLN H 2 1   ? 50.781  88.735  19.928  1.000 123.595 ? 1   GLN FFF CD  1 
ATOM   11352 O OE1 . GLN H 2 1   ? 50.840  89.965  19.917  1.000 135.143 ? 1   GLN FFF OE1 1 
ATOM   11353 N NE2 . GLN H 2 1   ? 51.871  87.977  19.936  1.000 103.436 ? 1   GLN FFF NE2 1 
ATOM   11354 N N   . MET H 2 2   ? 50.010  87.310  16.866  1.000 78.395  ? 2   MET FFF N   1 
ATOM   11355 C CA  . MET H 2 2   ? 50.384  86.049  16.178  1.000 77.184  ? 2   MET FFF CA  1 
ATOM   11356 C C   . MET H 2 2   ? 51.564  85.362  16.880  1.000 70.410  ? 2   MET FFF C   1 
ATOM   11357 O O   . MET H 2 2   ? 52.186  85.992  17.768  1.000 64.163  ? 2   MET FFF O   1 
ATOM   11358 C CB  . MET H 2 2   ? 50.738  86.331  14.715  1.000 82.910  ? 2   MET FFF CB  1 
ATOM   11359 C CG  . MET H 2 2   ? 52.077  87.005  14.517  1.000 79.393  ? 2   MET FFF CG  1 
ATOM   11360 S SD  . MET H 2 2   ? 53.381  85.799  14.219  1.000 71.480  ? 2   MET FFF SD  1 
ATOM   11361 C CE  . MET H 2 2   ? 52.715  84.936  12.800  1.000 69.331  ? 2   MET FFF CE  1 
ATOM   11362 N N   . GLN H 2 3   ? 51.850  84.118  16.462  1.000 65.502  ? 3   GLN FFF N   1 
ATOM   11363 C CA  . GLN H 2 3   ? 52.775  83.168  17.134  1.000 60.861  ? 3   GLN FFF CA  1 
ATOM   11364 C C   . GLN H 2 3   ? 53.486  82.280  16.103  1.000 51.173  ? 3   GLN FFF C   1 
ATOM   11365 O O   . GLN H 2 3   ? 52.972  82.110  14.985  1.000 47.118  ? 3   GLN FFF O   1 
ATOM   11366 C CB  . GLN H 2 3   ? 51.992  82.305  18.120  1.000 70.421  ? 3   GLN FFF CB  1 
ATOM   11367 C CG  . GLN H 2 3   ? 50.840  81.547  17.481  1.000 82.118  ? 3   GLN FFF CG  1 
ATOM   11368 C CD  . GLN H 2 3   ? 50.137  80.626  18.450  1.000 94.118  ? 3   GLN FFF CD  1 
ATOM   11369 O OE1 . GLN H 2 3   ? 50.411  80.606  19.651  1.000 89.208  ? 3   GLN FFF OE1 1 
ATOM   11370 N NE2 . GLN H 2 3   ? 49.213  79.840  17.918  1.000 105.998 ? 3   GLN FFF NE2 1 
ATOM   11371 N N   . LEU H 2 4   ? 54.649  81.749  16.486  1.000 49.916  ? 4   LEU FFF N   1 
ATOM   11372 C CA  . LEU H 2 4   ? 55.574  80.970  15.616  1.000 51.482  ? 4   LEU FFF CA  1 
ATOM   11373 C C   . LEU H 2 4   ? 55.757  79.553  16.181  1.000 49.844  ? 4   LEU FFF C   1 
ATOM   11374 O O   . LEU H 2 4   ? 55.966  79.400  17.405  1.000 47.643  ? 4   LEU FFF O   1 
ATOM   11375 C CB  . LEU H 2 4   ? 56.929  81.684  15.574  1.000 51.808  ? 4   LEU FFF CB  1 
ATOM   11376 C CG  . LEU H 2 4   ? 57.236  82.518  14.337  1.000 50.050  ? 4   LEU FFF CG  1 
ATOM   11377 C CD1 . LEU H 2 4   ? 56.133  83.528  14.049  1.000 51.923  ? 4   LEU FFF CD1 1 
ATOM   11378 C CD2 . LEU H 2 4   ? 58.559  83.228  14.533  1.000 51.068  ? 4   LEU FFF CD2 1 
ATOM   11379 N N   . VAL H 2 5   ? 55.738  78.543  15.317  1.000 44.994  ? 5   VAL FFF N   1 
ATOM   11380 C CA  . VAL H 2 5   ? 55.809  77.122  15.752  1.000 39.850  ? 5   VAL FFF CA  1 
ATOM   11381 C C   . VAL H 2 5   ? 56.865  76.415  14.922  1.000 39.349  ? 5   VAL FFF C   1 
ATOM   11382 O O   . VAL H 2 5   ? 56.778  76.472  13.691  1.000 42.797  ? 5   VAL FFF O   1 
ATOM   11383 C CB  . VAL H 2 5   ? 54.446  76.440  15.616  1.000 37.792  ? 5   VAL FFF CB  1 
ATOM   11384 C CG1 . VAL H 2 5   ? 54.589  74.951  15.360  1.000 38.485  ? 5   VAL FFF CG1 1 
ATOM   11385 C CG2 . VAL H 2 5   ? 53.587  76.717  16.836  1.000 37.886  ? 5   VAL FFF CG2 1 
ATOM   11386 N N   . GLN H 2 6   ? 57.835  75.794  15.582  1.000 37.984  ? 6   GLN FFF N   1 
ATOM   11387 C CA  . GLN H 2 6   ? 59.002  75.203  14.884  1.000 35.604  ? 6   GLN FFF CA  1 
ATOM   11388 C C   . GLN H 2 6   ? 58.804  73.701  14.697  1.000 33.877  ? 6   GLN FFF C   1 
ATOM   11389 O O   . GLN H 2 6   ? 57.934  73.114  15.349  1.000 34.539  ? 6   GLN FFF O   1 
ATOM   11390 C CB  . GLN H 2 6   ? 60.291  75.471  15.651  1.000 33.887  ? 6   GLN FFF CB  1 
ATOM   11391 C CG  . GLN H 2 6   ? 60.479  76.931  16.009  1.000 32.075  ? 6   GLN FFF CG  1 
ATOM   11392 C CD  . GLN H 2 6   ? 61.901  77.252  16.392  1.000 32.107  ? 6   GLN FFF CD  1 
ATOM   11393 O OE1 . GLN H 2 6   ? 62.118  78.037  17.320  1.000 32.585  ? 6   GLN FFF OE1 1 
ATOM   11394 N NE2 . GLN H 2 6   ? 62.861  76.646  15.690  1.000 30.751  ? 6   GLN FFF NE2 1 
ATOM   11395 N N   . SER H 2 7   ? 59.602  73.131  13.810  1.000 33.867  ? 7   SER FFF N   1 
ATOM   11396 C CA  . SER H 2 7   ? 59.706  71.678  13.588  1.000 37.976  ? 7   SER FFF CA  1 
ATOM   11397 C C   . SER H 2 7   ? 60.179  71.023  14.900  1.000 42.001  ? 7   SER FFF C   1 
ATOM   11398 O O   . SER H 2 7   ? 60.688  71.749  15.823  1.000 38.461  ? 7   SER FFF O   1 
ATOM   11399 C CB  . SER H 2 7   ? 60.598  71.379  12.390  1.000 38.285  ? 7   SER FFF CB  1 
ATOM   11400 O OG  . SER H 2 7   ? 61.979  71.373  12.741  1.000 38.058  ? 7   SER FFF OG  1 
ATOM   11401 N N   . GLY H 2 8   ? 59.970  69.705  15.003  1.000 41.567  ? 8   GLY FFF N   1 
ATOM   11402 C CA  . GLY H 2 8   ? 60.312  68.916  16.192  1.000 41.157  ? 8   GLY FFF CA  1 
ATOM   11403 C C   . GLY H 2 8   ? 61.800  68.644  16.250  1.000 40.438  ? 8   GLY FFF C   1 
ATOM   11404 O O   . GLY H 2 8   ? 62.501  69.021  15.252  1.000 36.564  ? 8   GLY FFF O   1 
ATOM   11405 N N   . THR H 2 9   ? 62.232  68.008  17.354  1.000 38.113  ? 9   THR FFF N   1 
ATOM   11406 C CA  . THR H 2 9   ? 63.629  67.615  17.667  1.000 39.084  ? 9   THR FFF CA  1 
ATOM   11407 C C   . THR H 2 9   ? 64.238  66.830  16.507  1.000 40.775  ? 9   THR FFF C   1 
ATOM   11408 O O   . THR H 2 9   ? 63.554  65.975  15.956  1.000 45.881  ? 9   THR FFF O   1 
ATOM   11409 C CB  . THR H 2 9   ? 63.716  66.724  18.908  1.000 38.933  ? 9   THR FFF CB  1 
ATOM   11410 O OG1 . THR H 2 9   ? 63.131  67.445  19.981  1.000 41.786  ? 9   THR FFF OG1 1 
ATOM   11411 C CG2 . THR H 2 9   ? 65.134  66.348  19.287  1.000 40.550  ? 9   THR FFF CG2 1 
ATOM   11412 N N   . GLU H 2 10  ? 65.492  67.111  16.171  1.000 42.915  ? 10  GLU FFF N   1 
ATOM   11413 C CA  . GLU H 2 10  ? 66.235  66.381  15.128  1.000 44.860  ? 10  GLU FFF CA  1 
ATOM   11414 C C   . GLU H 2 10  ? 67.460  65.763  15.786  1.000 44.915  ? 10  GLU FFF C   1 
ATOM   11415 O O   . GLU H 2 10  ? 67.976  66.338  16.790  1.000 40.069  ? 10  GLU FFF O   1 
ATOM   11416 C CB  . GLU H 2 10  ? 66.614  67.328  13.998  1.000 51.488  ? 10  GLU FFF CB  1 
ATOM   11417 C CG  . GLU H 2 10  ? 65.418  68.061  13.418  1.000 58.315  ? 10  GLU FFF CG  1 
ATOM   11418 C CD  . GLU H 2 10  ? 64.697  67.371  12.275  1.000 62.926  ? 10  GLU FFF CD  1 
ATOM   11419 O OE1 . GLU H 2 10  ? 65.225  66.347  11.742  1.000 58.296  ? 10  GLU FFF OE1 1 
ATOM   11420 O OE2 . GLU H 2 10  ? 63.634  67.902  11.877  1.000 69.955  ? 10  GLU FFF OE2 1 
ATOM   11421 N N   . VAL H 2 11  ? 67.843  64.595  15.267  1.000 43.892  ? 11  VAL FFF N   1 
ATOM   11422 C CA  . VAL H 2 11  ? 69.062  63.844  15.674  1.000 39.828  ? 11  VAL FFF CA  1 
ATOM   11423 C C   . VAL H 2 11  ? 69.655  63.228  14.414  1.000 39.147  ? 11  VAL FFF C   1 
ATOM   11424 O O   . VAL H 2 11  ? 69.023  62.311  13.861  1.000 39.848  ? 11  VAL FFF O   1 
ATOM   11425 C CB  . VAL H 2 11  ? 68.746  62.759  16.709  1.000 39.254  ? 11  VAL FFF CB  1 
ATOM   11426 C CG1 . VAL H 2 11  ? 69.992  61.968  17.026  1.000 41.520  ? 11  VAL FFF CG1 1 
ATOM   11427 C CG2 . VAL H 2 11  ? 68.127  63.337  17.962  1.000 40.528  ? 11  VAL FFF CG2 1 
ATOM   11428 N N   . LYS H 2 12  ? 70.813  63.726  13.987  1.000 41.047  ? 12  LYS FFF N   1 
ATOM   11429 C CA  . LYS H 2 12  ? 71.421  63.388  12.680  1.000 42.226  ? 12  LYS FFF CA  1 
ATOM   11430 C C   . LYS H 2 12  ? 72.864  62.956  12.896  1.000 43.112  ? 12  LYS FFF C   1 
ATOM   11431 O O   . LYS H 2 12  ? 73.436  63.294  13.962  1.000 37.907  ? 12  LYS FFF O   1 
ATOM   11432 C CB  . LYS H 2 12  ? 71.375  64.609  11.760  1.000 44.365  ? 12  LYS FFF CB  1 
ATOM   11433 C CG  . LYS H 2 12  ? 70.052  65.364  11.770  1.000 43.386  ? 12  LYS FFF CG  1 
ATOM   11434 C CD  . LYS H 2 12  ? 68.891  64.609  11.141  1.000 42.373  ? 12  LYS FFF CD  1 
ATOM   11435 C CE  . LYS H 2 12  ? 69.028  64.547  9.636   1.000 41.786  ? 12  LYS FFF CE  1 
ATOM   11436 N NZ  . LYS H 2 12  ? 67.799  64.065  8.971   1.000 43.465  ? 12  LYS FFF NZ  1 
ATOM   11437 N N   . LYS H 2 13  ? 73.424  62.262  11.902  1.000 47.071  ? 13  LYS FFF N   1 
ATOM   11438 C CA  . LYS H 2 13  ? 74.855  61.866  11.875  1.000 47.665  ? 13  LYS FFF CA  1 
ATOM   11439 C C   . LYS H 2 13  ? 75.624  62.939  11.124  1.000 46.106  ? 13  LYS FFF C   1 
ATOM   11440 O O   . LYS H 2 13  ? 75.078  63.584  10.240  1.000 42.439  ? 13  LYS FFF O   1 
ATOM   11441 C CB  . LYS H 2 13  ? 75.038  60.503  11.203  1.000 52.096  ? 13  LYS FFF CB  1 
ATOM   11442 C CG  . LYS H 2 13  ? 74.124  59.399  11.719  1.000 58.197  ? 13  LYS FFF CG  1 
ATOM   11443 C CD  . LYS H 2 13  ? 74.401  59.003  13.150  1.000 63.478  ? 13  LYS FFF CD  1 
ATOM   11444 C CE  . LYS H 2 13  ? 75.108  57.670  13.273  1.000 65.894  ? 13  LYS FFF CE  1 
ATOM   11445 N NZ  . LYS H 2 13  ? 74.157  56.534  13.322  1.000 70.092  ? 13  LYS FFF NZ  1 
ATOM   11446 N N   . PRO H 2 14  ? 76.909  63.148  11.454  1.000 48.426  ? 14  PRO FFF N   1 
ATOM   11447 C CA  . PRO H 2 14  ? 77.747  64.090  10.722  1.000 49.750  ? 14  PRO FFF CA  1 
ATOM   11448 C C   . PRO H 2 14  ? 77.670  63.759  9.229   1.000 50.672  ? 14  PRO FFF C   1 
ATOM   11449 O O   . PRO H 2 14  ? 77.776  62.585  8.887   1.000 48.217  ? 14  PRO FFF O   1 
ATOM   11450 C CB  . PRO H 2 14  ? 79.165  63.883  11.282  1.000 48.814  ? 14  PRO FFF CB  1 
ATOM   11451 C CG  . PRO H 2 14  ? 78.938  63.248  12.638  1.000 51.486  ? 14  PRO FFF CG  1 
ATOM   11452 C CD  . PRO H 2 14  ? 77.644  62.462  12.519  1.000 52.536  ? 14  PRO FFF CD  1 
ATOM   11453 N N   . GLY H 2 15  ? 77.425  64.784  8.406   1.000 52.180  ? 15  GLY FFF N   1 
ATOM   11454 C CA  . GLY H 2 15  ? 77.410  64.682  6.940   1.000 54.881  ? 15  GLY FFF CA  1 
ATOM   11455 C C   . GLY H 2 15  ? 76.002  64.666  6.375   1.000 56.739  ? 15  GLY FFF C   1 
ATOM   11456 O O   . GLY H 2 15  ? 75.864  64.858  5.151   1.000 59.630  ? 15  GLY FFF O   1 
ATOM   11457 N N   . GLU H 2 16  ? 74.990  64.393  7.204   1.000 56.520  ? 16  GLU FFF N   1 
ATOM   11458 C CA  . GLU H 2 16  ? 73.571  64.417  6.770   1.000 64.587  ? 16  GLU FFF CA  1 
ATOM   11459 C C   . GLU H 2 16  ? 73.186  65.887  6.528   1.000 64.692  ? 16  GLU FFF C   1 
ATOM   11460 O O   . GLU H 2 16  ? 73.684  66.786  7.258   1.000 55.635  ? 16  GLU FFF O   1 
ATOM   11461 C CB  . GLU H 2 16  ? 72.667  63.717  7.796   1.000 67.315  ? 16  GLU FFF CB  1 
ATOM   11462 C CG  . GLU H 2 16  ? 72.868  62.206  7.892   1.000 65.691  ? 16  GLU FFF CG  1 
ATOM   11463 C CD  . GLU H 2 16  ? 71.949  61.429  8.836   1.000 65.072  ? 16  GLU FFF CD  1 
ATOM   11464 O OE1 . GLU H 2 16  ? 70.903  61.944  9.242   1.000 70.130  ? 16  GLU FFF OE1 1 
ATOM   11465 O OE2 . GLU H 2 16  ? 72.279  60.295  9.178   1.000 64.622  ? 16  GLU FFF OE2 1 
ATOM   11466 N N   . SER H 2 17  ? 72.369  66.126  5.501   1.000 62.787  ? 17  SER FFF N   1 
ATOM   11467 C CA  . SER H 2 17  ? 71.681  67.415  5.268   1.000 59.802  ? 17  SER FFF CA  1 
ATOM   11468 C C   . SER H 2 17  ? 70.593  67.548  6.330   1.000 59.932  ? 17  SER FFF C   1 
ATOM   11469 O O   . SER H 2 17  ? 70.184  66.520  6.884   1.000 63.826  ? 17  SER FFF O   1 
ATOM   11470 C CB  . SER H 2 17  ? 71.105  67.472  3.885   1.000 59.352  ? 17  SER FFF CB  1 
ATOM   11471 O OG  . SER H 2 17  ? 70.176  66.419  3.700   1.000 58.328  ? 17  SER FFF OG  1 
ATOM   11472 N N   . LEU H 2 18  ? 70.151  68.768  6.612   1.000 54.472  ? 18  LEU FFF N   1 
ATOM   11473 C CA  . LEU H 2 18  ? 68.977  69.005  7.480   1.000 50.981  ? 18  LEU FFF CA  1 
ATOM   11474 C C   . LEU H 2 18  ? 68.322  70.324  7.081   1.000 49.855  ? 18  LEU FFF C   1 
ATOM   11475 O O   . LEU H 2 18  ? 69.050  71.232  6.673   1.000 50.295  ? 18  LEU FFF O   1 
ATOM   11476 C CB  . LEU H 2 18  ? 69.437  69.019  8.937   1.000 47.632  ? 18  LEU FFF CB  1 
ATOM   11477 C CG  . LEU H 2 18  ? 68.374  69.442  9.956   1.000 45.997  ? 18  LEU FFF CG  1 
ATOM   11478 C CD1 . LEU H 2 18  ? 67.149  68.542  9.894   1.000 47.125  ? 18  LEU FFF CD1 1 
ATOM   11479 C CD2 . LEU H 2 18  ? 68.957  69.443  11.356  1.000 45.809  ? 18  LEU FFF CD2 1 
ATOM   11480 N N   . LYS H 2 19  ? 66.996  70.389  7.165   1.000 48.324  ? 19  LYS FFF N   1 
ATOM   11481 C CA  . LYS H 2 19  ? 66.207  71.623  6.966   1.000 49.020  ? 19  LYS FFF CA  1 
ATOM   11482 C C   . LYS H 2 19  ? 65.123  71.645  8.040   1.000 47.730  ? 19  LYS FFF C   1 
ATOM   11483 O O   . LYS H 2 19  ? 64.180  70.850  7.928   1.000 44.204  ? 19  LYS FFF O   1 
ATOM   11484 C CB  . LYS H 2 19  ? 65.614  71.639  5.556   1.000 53.527  ? 19  LYS FFF CB  1 
ATOM   11485 C CG  . LYS H 2 19  ? 64.538  72.690  5.298   1.000 58.202  ? 19  LYS FFF CG  1 
ATOM   11486 C CD  . LYS H 2 19  ? 64.617  73.328  3.928   1.000 61.992  ? 19  LYS FFF CD  1 
ATOM   11487 C CE  . LYS H 2 19  ? 63.546  72.832  2.979   1.000 64.490  ? 19  LYS FFF CE  1 
ATOM   11488 N NZ  . LYS H 2 19  ? 63.731  73.451  1.647   1.000 74.870  ? 19  LYS FFF NZ  1 
ATOM   11489 N N   . ILE H 2 20  ? 65.262  72.517  9.040   1.000 46.077  ? 20  ILE FFF N   1 
ATOM   11490 C CA  . ILE H 2 20  ? 64.221  72.736  10.083  1.000 43.359  ? 20  ILE FFF CA  1 
ATOM   11491 C C   . ILE H 2 20  ? 63.335  73.886  9.634   1.000 41.553  ? 20  ILE FFF C   1 
ATOM   11492 O O   . ILE H 2 20  ? 63.771  74.654  8.772   1.000 41.650  ? 20  ILE FFF O   1 
ATOM   11493 C CB  . ILE H 2 20  ? 64.847  72.988  11.461  1.000 45.216  ? 20  ILE FFF CB  1 
ATOM   11494 C CG1 . ILE H 2 20  ? 65.337  74.417  11.647  1.000 45.206  ? 20  ILE FFF CG1 1 
ATOM   11495 C CG2 . ILE H 2 20  ? 65.956  71.999  11.722  1.000 49.818  ? 20  ILE FFF CG2 1 
ATOM   11496 C CD1 . ILE H 2 20  ? 65.849  74.670  13.044  1.000 45.885  ? 20  ILE FFF CD1 1 
ATOM   11497 N N   . SER H 2 21  ? 62.156  74.002  10.232  1.000 42.908  ? 21  SER FFF N   1 
ATOM   11498 C CA  . SER H 2 21  ? 61.119  74.964  9.806   1.000 44.519  ? 21  SER FFF CA  1 
ATOM   11499 C C   . SER H 2 21  ? 60.588  75.739  11.013  1.000 44.528  ? 21  SER FFF C   1 
ATOM   11500 O O   . SER H 2 21  ? 60.955  75.381  12.174  1.000 42.679  ? 21  SER FFF O   1 
ATOM   11501 C CB  . SER H 2 21  ? 60.019  74.265  9.063   1.000 45.545  ? 21  SER FFF CB  1 
ATOM   11502 O OG  . SER H 2 21  ? 59.294  73.399  9.920   1.000 42.881  ? 21  SER FFF OG  1 
ATOM   11503 N N   . CYS H 2 22  ? 59.796  76.768  10.687  1.000 43.948  ? 22  CYS FFF N   1 
ATOM   11504 C CA  . CYS H 2 22  ? 59.213  77.823  11.548  1.000 45.009  ? 22  CYS FFF CA  1 
ATOM   11505 C C   . CYS H 2 22  ? 58.045  78.435  10.769  1.000 46.736  ? 22  CYS FFF C   1 
ATOM   11506 O O   . CYS H 2 22  ? 58.268  79.166  9.777   1.000 45.877  ? 22  CYS FFF O   1 
ATOM   11507 C CB  . CYS H 2 22  ? 60.234  78.904  11.882  1.000 47.147  ? 22  CYS FFF CB  1 
ATOM   11508 S SG  . CYS H 2 22  ? 59.593  80.224  12.939  1.000 54.094  ? 22  CYS FFF SG  1 
ATOM   11509 N N   . LYS H 2 23  ? 56.836  78.075  11.170  1.000 50.365  ? 23  LYS FFF N   1 
ATOM   11510 C CA  . LYS H 2 23  ? 55.582  78.495  10.514  1.000 51.475  ? 23  LYS FFF CA  1 
ATOM   11511 C C   . LYS H 2 23  ? 54.863  79.442  11.482  1.000 54.351  ? 23  LYS FFF C   1 
ATOM   11512 O O   . LYS H 2 23  ? 54.814  79.156  12.711  1.000 48.637  ? 23  LYS FFF O   1 
ATOM   11513 C CB  . LYS H 2 23  ? 54.737  77.277  10.134  1.000 53.000  ? 23  LYS FFF CB  1 
ATOM   11514 C CG  . LYS H 2 23  ? 53.331  77.626  9.679   1.000 58.423  ? 23  LYS FFF CG  1 
ATOM   11515 C CD  . LYS H 2 23  ? 52.488  76.487  9.185   1.000 60.395  ? 23  LYS FFF CD  1 
ATOM   11516 C CE  . LYS H 2 23  ? 51.040  76.917  9.114   1.000 64.376  ? 23  LYS FFF CE  1 
ATOM   11517 N NZ  . LYS H 2 23  ? 50.342  76.231  8.010   1.000 75.372  ? 23  LYS FFF NZ  1 
ATOM   11518 N N   . GLY H 2 24  ? 54.352  80.543  10.932  1.000 57.700  ? 24  GLY FFF N   1 
ATOM   11519 C CA  . GLY H 2 24  ? 53.623  81.575  11.680  1.000 55.509  ? 24  GLY FFF CA  1 
ATOM   11520 C C   . GLY H 2 24  ? 52.146  81.503  11.377  1.000 53.388  ? 24  GLY FFF C   1 
ATOM   11521 O O   . GLY H 2 24  ? 51.769  81.325  10.204  1.000 48.789  ? 24  GLY FFF O   1 
ATOM   11522 N N   . SER H 2 25  ? 51.348  81.597  12.428  1.000 58.853  ? 25  SER FFF N   1 
ATOM   11523 C CA  . SER H 2 25  ? 49.872  81.593  12.382  1.000 68.200  ? 25  SER FFF CA  1 
ATOM   11524 C C   . SER H 2 25  ? 49.386  82.789  13.198  1.000 71.039  ? 25  SER FFF C   1 
ATOM   11525 O O   . SER H 2 25  ? 49.969  83.065  14.263  1.000 67.296  ? 25  SER FFF O   1 
ATOM   11526 C CB  . SER H 2 25  ? 49.309  80.273  12.878  1.000 79.025  ? 25  SER FFF CB  1 
ATOM   11527 O OG  . SER H 2 25  ? 49.669  80.027  14.235  1.000 84.515  ? 25  SER FFF OG  1 
ATOM   11528 N N   . GLY H 2 26  ? 48.361  83.466  12.687  1.000 83.270  ? 26  GLY FFF N   1 
ATOM   11529 C CA  . GLY H 2 26  ? 47.823  84.727  13.224  1.000 85.967  ? 26  GLY FFF CA  1 
ATOM   11530 C C   . GLY H 2 26  ? 47.809  85.794  12.153  1.000 88.365  ? 26  GLY FFF C   1 
ATOM   11531 O O   . GLY H 2 26  ? 48.642  85.743  11.247  1.000 98.790  ? 26  GLY FFF O   1 
ATOM   11532 N N   . TYR H 2 27  ? 46.867  86.722  12.219  1.000 98.131  ? 27  TYR FFF N   1 
ATOM   11533 C CA  . TYR H 2 27  ? 46.838  87.876  11.288  1.000 102.560 ? 27  TYR FFF CA  1 
ATOM   11534 C C   . TYR H 2 27  ? 47.907  88.854  11.764  1.000 84.977  ? 27  TYR FFF C   1 
ATOM   11535 O O   . TYR H 2 27  ? 48.297  88.855  12.959  1.000 65.721  ? 27  TYR FFF O   1 
ATOM   11536 C CB  . TYR H 2 27  ? 45.448  88.511  11.138  1.000 118.403 ? 27  TYR FFF CB  1 
ATOM   11537 C CG  . TYR H 2 27  ? 44.563  88.426  12.355  1.000 120.099 ? 27  TYR FFF CG  1 
ATOM   11538 C CD1 . TYR H 2 27  ? 44.895  89.113  13.516  1.000 115.233 ? 27  TYR FFF CD1 1 
ATOM   11539 C CD2 . TYR H 2 27  ? 43.418  87.638  12.352  1.000 109.708 ? 27  TYR FFF CD2 1 
ATOM   11540 C CE1 . TYR H 2 27  ? 44.110  89.018  14.650  1.000 117.110 ? 27  TYR FFF CE1 1 
ATOM   11541 C CE2 . TYR H 2 27  ? 42.622  87.535  13.478  1.000 111.454 ? 27  TYR FFF CE2 1 
ATOM   11542 C CZ  . TYR H 2 27  ? 42.966  88.233  14.625  1.000 121.900 ? 27  TYR FFF CZ  1 
ATOM   11543 O OH  . TYR H 2 27  ? 42.173  88.140  15.731  1.000 128.403 ? 27  TYR FFF OH  1 
ATOM   11544 N N   . GLY H 2 28  ? 48.367  89.642  10.799  1.000 79.506  ? 28  GLY FFF N   1 
ATOM   11545 C CA  . GLY H 2 28  ? 49.524  90.532  10.914  1.000 73.206  ? 28  GLY FFF CA  1 
ATOM   11546 C C   . GLY H 2 28  ? 50.776  89.816  10.473  1.000 70.242  ? 28  GLY FFF C   1 
ATOM   11547 O O   . GLY H 2 28  ? 51.809  90.187  10.977  1.000 75.625  ? 28  GLY FFF O   1 
ATOM   11548 N N   . PHE H 2 29  ? 50.716  88.861  9.542   1.000 63.824  ? 29  PHE FFF N   1 
ATOM   11549 C CA  . PHE H 2 29  ? 51.919  88.069  9.190   1.000 58.310  ? 29  PHE FFF CA  1 
ATOM   11550 C C   . PHE H 2 29  ? 52.696  88.701  8.035   1.000 55.771  ? 29  PHE FFF C   1 
ATOM   11551 O O   . PHE H 2 29  ? 53.932  88.524  8.043   1.000 52.666  ? 29  PHE FFF O   1 
ATOM   11552 C CB  . PHE H 2 29  ? 51.615  86.618  8.829   1.000 56.769  ? 29  PHE FFF CB  1 
ATOM   11553 C CG  . PHE H 2 29  ? 52.883  85.825  8.615   1.000 55.141  ? 29  PHE FFF CG  1 
ATOM   11554 C CD1 . PHE H 2 29  ? 53.697  85.477  9.689   1.000 51.716  ? 29  PHE FFF CD1 1 
ATOM   11555 C CD2 . PHE H 2 29  ? 53.315  85.511  7.337   1.000 53.757  ? 29  PHE FFF CD2 1 
ATOM   11556 C CE1 . PHE H 2 29  ? 54.883  84.787  9.500   1.000 46.198  ? 29  PHE FFF CE1 1 
ATOM   11557 C CE2 . PHE H 2 29  ? 54.500  84.816  7.146   1.000 54.244  ? 29  PHE FFF CE2 1 
ATOM   11558 C CZ  . PHE H 2 29  ? 55.280  84.453  8.227   1.000 49.380  ? 29  PHE FFF CZ  1 
ATOM   11559 N N   . ILE H 2 30  ? 52.031  89.363  7.078   1.000 56.993  ? 30  ILE FFF N   1 
ATOM   11560 C CA  . ILE H 2 30  ? 52.699  89.917  5.854   1.000 57.619  ? 30  ILE FFF CA  1 
ATOM   11561 C C   . ILE H 2 30  ? 53.847  90.826  6.303   1.000 53.498  ? 30  ILE FFF C   1 
ATOM   11562 O O   . ILE H 2 30  ? 54.841  90.909  5.560   1.000 51.167  ? 30  ILE FFF O   1 
ATOM   11563 C CB  . ILE H 2 30  ? 51.722  90.658  4.914   1.000 62.162  ? 30  ILE FFF CB  1 
ATOM   11564 C CG1 . ILE H 2 30  ? 50.475  89.823  4.574   1.000 80.163  ? 30  ILE FFF CG1 1 
ATOM   11565 C CG2 . ILE H 2 30  ? 52.452  91.087  3.655   1.000 56.081  ? 30  ILE FFF CG2 1 
ATOM   11566 C CD1 . ILE H 2 30  ? 49.377  90.567  3.797   1.000 81.773  ? 30  ILE FFF CD1 1 
ATOM   11567 N N   . THR H 2 31  ? 53.735  91.394  7.512   1.000 49.558  ? 31  THR FFF N   1 
ATOM   11568 C CA  . THR H 2 31  ? 54.645  92.404  8.121   1.000 51.388  ? 31  THR FFF CA  1 
ATOM   11569 C C   . THR H 2 31  ? 55.916  91.784  8.743   1.000 52.691  ? 31  THR FFF C   1 
ATOM   11570 O O   . THR H 2 31  ? 56.949  92.509  8.803   1.000 60.463  ? 31  THR FFF O   1 
ATOM   11571 C CB  . THR H 2 31  ? 53.890  93.244  9.160   1.000 50.968  ? 31  THR FFF CB  1 
ATOM   11572 O OG1 . THR H 2 31  ? 54.826  93.938  9.971   1.000 54.533  ? 31  THR FFF OG1 1 
ATOM   11573 C CG2 . THR H 2 31  ? 53.068  92.448  10.139  1.000 52.926  ? 31  THR FFF CG2 1 
ATOM   11574 N N   . TYR H 2 32  ? 55.880  90.517  9.177   1.000 50.211  ? 32  TYR FFF N   1 
ATOM   11575 C CA  . TYR H 2 32  ? 56.903  89.912  10.076  1.000 45.727  ? 32  TYR FFF CA  1 
ATOM   11576 C C   . TYR H 2 32  ? 58.145  89.502  9.293   1.000 42.224  ? 32  TYR FFF C   1 
ATOM   11577 O O   . TYR H 2 32  ? 58.044  88.811  8.257   1.000 39.499  ? 32  TYR FFF O   1 
ATOM   11578 C CB  . TYR H 2 32  ? 56.351  88.716  10.858  1.000 47.941  ? 32  TYR FFF CB  1 
ATOM   11579 C CG  . TYR H 2 32  ? 55.767  89.120  12.188  1.000 48.369  ? 32  TYR FFF CG  1 
ATOM   11580 C CD1 . TYR H 2 32  ? 56.573  89.375  13.284  1.000 47.994  ? 32  TYR FFF CD1 1 
ATOM   11581 C CD2 . TYR H 2 32  ? 54.412  89.327  12.329  1.000 48.529  ? 32  TYR FFF CD2 1 
ATOM   11582 C CE1 . TYR H 2 32  ? 56.042  89.802  14.491  1.000 49.073  ? 32  TYR FFF CE1 1 
ATOM   11583 C CE2 . TYR H 2 32  ? 53.861  89.754  13.527  1.000 48.545  ? 32  TYR FFF CE2 1 
ATOM   11584 C CZ  . TYR H 2 32  ? 54.679  90.001  14.611  1.000 50.245  ? 32  TYR FFF CZ  1 
ATOM   11585 O OH  . TYR H 2 32  ? 54.136  90.412  15.794  1.000 55.150  ? 32  TYR FFF OH  1 
ATOM   11586 N N   . TRP H 2 33  ? 59.288  89.939  9.811   1.000 42.170  ? 33  TRP FFF N   1 
ATOM   11587 C CA  . TRP H 2 33  ? 60.649  89.510  9.398   1.000 47.010  ? 33  TRP FFF CA  1 
ATOM   11588 C C   . TRP H 2 33  ? 61.127  88.422  10.358  1.000 47.604  ? 33  TRP FFF C   1 
ATOM   11589 O O   . TRP H 2 33  ? 61.187  88.703  11.575  1.000 52.463  ? 33  TRP FFF O   1 
ATOM   11590 C CB  . TRP H 2 33  ? 61.629  90.688  9.449   1.000 51.475  ? 33  TRP FFF CB  1 
ATOM   11591 C CG  . TRP H 2 33  ? 61.413  91.748  8.421   1.000 50.982  ? 33  TRP FFF CG  1 
ATOM   11592 C CD1 . TRP H 2 33  ? 60.370  92.620  8.324   1.000 53.376  ? 33  TRP FFF CD1 1 
ATOM   11593 C CD2 . TRP H 2 33  ? 62.314  92.061  7.355   1.000 51.181  ? 33  TRP FFF CD2 1 
ATOM   11594 N NE1 . TRP H 2 33  ? 60.541  93.433  7.241   1.000 54.596  ? 33  TRP FFF NE1 1 
ATOM   11595 C CE2 . TRP H 2 33  ? 61.732  93.117  6.634   1.000 53.280  ? 33  TRP FFF CE2 1 
ATOM   11596 C CE3 . TRP H 2 33  ? 63.539  91.537  6.935   1.000 53.601  ? 33  TRP FFF CE3 1 
ATOM   11597 C CZ2 . TRP H 2 33  ? 62.349  93.659  5.509   1.000 53.012  ? 33  TRP FFF CZ2 1 
ATOM   11598 C CZ3 . TRP H 2 33  ? 64.149  92.079  5.829   1.000 53.623  ? 33  TRP FFF CZ3 1 
ATOM   11599 C CH2 . TRP H 2 33  ? 63.559  93.131  5.131   1.000 52.675  ? 33  TRP FFF CH2 1 
ATOM   11600 N N   . ILE H 2 34  ? 61.537  87.267  9.835   1.000 48.025  ? 34  ILE FFF N   1 
ATOM   11601 C CA  . ILE H 2 34  ? 61.802  86.046  10.652  1.000 44.424  ? 34  ILE FFF CA  1 
ATOM   11602 C C   . ILE H 2 34  ? 63.297  85.736  10.698  1.000 41.836  ? 34  ILE FFF C   1 
ATOM   11603 O O   . ILE H 2 34  ? 63.884  85.423  9.650   1.000 42.395  ? 34  ILE FFF O   1 
ATOM   11604 C CB  . ILE H 2 34  ? 60.979  84.883  10.098  1.000 43.262  ? 34  ILE FFF CB  1 
ATOM   11605 C CG1 . ILE H 2 34  ? 59.503  85.107  10.410  1.000 44.689  ? 34  ILE FFF CG1 1 
ATOM   11606 C CG2 . ILE H 2 34  ? 61.488  83.560  10.636  1.000 43.294  ? 34  ILE FFF CG2 1 
ATOM   11607 C CD1 . ILE H 2 34  ? 58.592  84.268  9.579   1.000 47.690  ? 34  ILE FFF CD1 1 
ATOM   11608 N N   . GLY H 2 35  ? 63.865  85.811  11.899  1.000 43.151  ? 35  GLY FFF N   1 
ATOM   11609 C CA  . GLY H 2 35  ? 65.298  85.607  12.162  1.000 45.208  ? 35  GLY FFF CA  1 
ATOM   11610 C C   . GLY H 2 35  ? 65.546  84.281  12.863  1.000 44.536  ? 35  GLY FFF C   1 
ATOM   11611 O O   . GLY H 2 35  ? 64.607  83.700  13.420  1.000 47.723  ? 35  GLY FFF O   1 
ATOM   11612 N N   . TRP H 2 36  ? 66.775  83.794  12.788  1.000 40.636  ? 36  TRP FFF N   1 
ATOM   11613 C CA  . TRP H 2 36  ? 67.203  82.492  13.342  1.000 38.282  ? 36  TRP FFF CA  1 
ATOM   11614 C C   . TRP H 2 36  ? 68.301  82.781  14.353  1.000 36.230  ? 36  TRP FFF C   1 
ATOM   11615 O O   . TRP H 2 36  ? 69.227  83.520  14.023  1.000 38.081  ? 36  TRP FFF O   1 
ATOM   11616 C CB  . TRP H 2 36  ? 67.675  81.562  12.225  1.000 38.845  ? 36  TRP FFF CB  1 
ATOM   11617 C CG  . TRP H 2 36  ? 66.552  81.025  11.393  1.000 40.412  ? 36  TRP FFF CG  1 
ATOM   11618 C CD1 . TRP H 2 36  ? 66.140  81.435  10.159  1.000 41.219  ? 36  TRP FFF CD1 1 
ATOM   11619 C CD2 . TRP H 2 36  ? 65.684  79.947  11.758  1.000 42.564  ? 36  TRP FFF CD2 1 
ATOM   11620 N NE1 . TRP H 2 36  ? 65.081  80.678  9.734   1.000 42.697  ? 36  TRP FFF NE1 1 
ATOM   11621 C CE2 . TRP H 2 36  ? 64.780  79.757  10.694  1.000 42.552  ? 36  TRP FFF CE2 1 
ATOM   11622 C CE3 . TRP H 2 36  ? 65.593  79.127  12.884  1.000 42.420  ? 36  TRP FFF CE3 1 
ATOM   11623 C CZ2 . TRP H 2 36  ? 63.795  78.779  10.723  1.000 43.311  ? 36  TRP FFF CZ2 1 
ATOM   11624 C CZ3 . TRP H 2 36  ? 64.612  78.168  12.922  1.000 44.428  ? 36  TRP FFF CZ3 1 
ATOM   11625 C CH2 . TRP H 2 36  ? 63.735  77.994  11.851  1.000 45.471  ? 36  TRP FFF CH2 1 
ATOM   11626 N N   . VAL H 2 37  ? 68.160  82.252  15.555  1.000 35.773  ? 37  VAL FFF N   1 
ATOM   11627 C CA  . VAL H 2 37  ? 69.157  82.413  16.639  1.000 36.886  ? 37  VAL FFF CA  1 
ATOM   11628 C C   . VAL H 2 37  ? 69.656  81.024  17.020  1.000 36.207  ? 37  VAL FFF C   1 
ATOM   11629 O O   . VAL H 2 37  ? 68.837  80.111  17.115  1.000 34.645  ? 37  VAL FFF O   1 
ATOM   11630 C CB  . VAL H 2 37  ? 68.524  83.143  17.828  1.000 39.112  ? 37  VAL FFF CB  1 
ATOM   11631 C CG1 . VAL H 2 37  ? 69.488  83.255  18.998  1.000 40.587  ? 37  VAL FFF CG1 1 
ATOM   11632 C CG2 . VAL H 2 37  ? 68.023  84.513  17.406  1.000 40.359  ? 37  VAL FFF CG2 1 
ATOM   11633 N N   . ARG H 2 38  ? 70.957  80.878  17.228  1.000 36.588  ? 38  ARG FFF N   1 
ATOM   11634 C CA  . ARG H 2 38  ? 71.532  79.600  17.690  1.000 40.192  ? 38  ARG FFF CA  1 
ATOM   11635 C C   . ARG H 2 38  ? 71.953  79.731  19.147  1.000 40.655  ? 38  ARG FFF C   1 
ATOM   11636 O O   . ARG H 2 38  ? 72.578  80.742  19.492  1.000 41.132  ? 38  ARG FFF O   1 
ATOM   11637 C CB  . ARG H 2 38  ? 72.747  79.191  16.865  1.000 43.725  ? 38  ARG FFF CB  1 
ATOM   11638 C CG  . ARG H 2 38  ? 73.372  77.909  17.388  1.000 47.181  ? 38  ARG FFF CG  1 
ATOM   11639 C CD  . ARG H 2 38  ? 74.502  77.447  16.511  1.000 48.191  ? 38  ARG FFF CD  1 
ATOM   11640 N NE  . ARG H 2 38  ? 75.670  78.259  16.745  1.000 46.824  ? 38  ARG FFF NE  1 
ATOM   11641 C CZ  . ARG H 2 38  ? 76.802  78.124  16.089  1.000 46.758  ? 38  ARG FFF CZ  1 
ATOM   11642 N NH1 . ARG H 2 38  ? 76.908  77.205  15.144  1.000 47.997  ? 38  ARG FFF NH1 1 
ATOM   11643 N NH2 . ARG H 2 38  ? 77.826  78.895  16.397  1.000 48.747  ? 38  ARG FFF NH2 1 
ATOM   11644 N N   . GLN H 2 39  ? 71.627  78.724  19.957  1.000 40.463  ? 39  GLN FFF N   1 
ATOM   11645 C CA  . GLN H 2 39  ? 72.073  78.648  21.367  1.000 42.630  ? 39  GLN FFF CA  1 
ATOM   11646 C C   . GLN H 2 39  ? 72.694  77.278  21.603  1.000 45.990  ? 39  GLN FFF C   1 
ATOM   11647 O O   . GLN H 2 39  ? 71.956  76.285  21.723  1.000 46.809  ? 39  GLN FFF O   1 
ATOM   11648 C CB  . GLN H 2 39  ? 70.930  78.903  22.344  1.000 39.151  ? 39  GLN FFF CB  1 
ATOM   11649 C CG  . GLN H 2 39  ? 71.404  78.914  23.782  1.000 36.513  ? 39  GLN FFF CG  1 
ATOM   11650 C CD  . GLN H 2 39  ? 70.314  79.414  24.685  1.000 37.539  ? 39  GLN FFF CD  1 
ATOM   11651 O OE1 . GLN H 2 39  ? 70.566  80.257  25.545  1.000 38.289  ? 39  GLN FFF OE1 1 
ATOM   11652 N NE2 . GLN H 2 39  ? 69.102  78.904  24.480  1.000 35.429  ? 39  GLN FFF NE2 1 
ATOM   11653 N N   . MET H 2 40  ? 74.017  77.236  21.679  1.000 51.405  ? 40  MET FFF N   1 
ATOM   11654 C CA  . MET H 2 40  ? 74.749  75.976  21.914  1.000 52.194  ? 40  MET FFF CA  1 
ATOM   11655 C C   . MET H 2 40  ? 74.581  75.601  23.374  1.000 52.377  ? 40  MET FFF C   1 
ATOM   11656 O O   . MET H 2 40  ? 74.262  76.440  24.210  1.000 54.673  ? 40  MET FFF O   1 
ATOM   11657 C CB  . MET H 2 40  ? 76.221  76.136  21.547  1.000 57.092  ? 40  MET FFF CB  1 
ATOM   11658 C CG  . MET H 2 40  ? 76.401  76.290  20.053  1.000 59.261  ? 40  MET FFF CG  1 
ATOM   11659 S SD  . MET H 2 40  ? 78.112  76.418  19.564  1.000 60.071  ? 40  MET FFF SD  1 
ATOM   11660 C CE  . MET H 2 40  ? 78.022  75.748  17.905  1.000 60.909  ? 40  MET FFF CE  1 
ATOM   11661 N N   . PRO H 2 41  ? 74.743  74.308  23.707  1.000 52.607  ? 41  PRO FFF N   1 
ATOM   11662 C CA  . PRO H 2 41  ? 74.522  73.845  25.070  1.000 51.954  ? 41  PRO FFF CA  1 
ATOM   11663 C C   . PRO H 2 41  ? 75.409  74.602  26.064  1.000 50.782  ? 41  PRO FFF C   1 
ATOM   11664 O O   . PRO H 2 41  ? 76.628  74.503  25.957  1.000 48.121  ? 41  PRO FFF O   1 
ATOM   11665 C CB  . PRO H 2 41  ? 74.902  72.365  24.996  1.000 51.159  ? 41  PRO FFF CB  1 
ATOM   11666 C CG  . PRO H 2 41  ? 74.662  72.008  23.550  1.000 49.577  ? 41  PRO FFF CG  1 
ATOM   11667 C CD  . PRO H 2 41  ? 75.126  73.227  22.790  1.000 49.928  ? 41  PRO FFF CD  1 
ATOM   11668 N N   . GLY H 2 42  ? 74.763  75.322  26.987  1.000 50.488  ? 42  GLY FFF N   1 
ATOM   11669 C CA  . GLY H 2 42  ? 75.400  76.054  28.094  1.000 49.908  ? 42  GLY FFF CA  1 
ATOM   11670 C C   . GLY H 2 42  ? 75.877  77.424  27.660  1.000 51.513  ? 42  GLY FFF C   1 
ATOM   11671 O O   . GLY H 2 42  ? 76.405  78.132  28.505  1.000 59.365  ? 42  GLY FFF O   1 
ATOM   11672 N N   . LYS H 2 43  ? 75.703  77.791  26.391  1.000 51.801  ? 43  LYS FFF N   1 
ATOM   11673 C CA  . LYS H 2 43  ? 76.212  79.071  25.839  1.000 55.213  ? 43  LYS FFF CA  1 
ATOM   11674 C C   . LYS H 2 43  ? 75.066  80.075  25.735  1.000 54.844  ? 43  LYS FFF C   1 
ATOM   11675 O O   . LYS H 2 43  ? 73.900  79.695  25.993  1.000 54.437  ? 43  LYS FFF O   1 
ATOM   11676 C CB  . LYS H 2 43  ? 76.816  78.870  24.449  1.000 59.733  ? 43  LYS FFF CB  1 
ATOM   11677 C CG  . LYS H 2 43  ? 77.803  77.720  24.356  1.000 63.095  ? 43  LYS FFF CG  1 
ATOM   11678 C CD  . LYS H 2 43  ? 78.903  77.746  25.375  1.000 63.016  ? 43  LYS FFF CD  1 
ATOM   11679 C CE  . LYS H 2 43  ? 79.793  76.541  25.195  1.000 67.549  ? 43  LYS FFF CE  1 
ATOM   11680 N NZ  . LYS H 2 43  ? 81.150  76.818  25.690  1.000 77.411  ? 43  LYS FFF NZ  1 
ATOM   11681 N N   . GLY H 2 44  ? 75.409  81.298  25.336  1.000 50.490  ? 44  GLY FFF N   1 
ATOM   11682 C CA  . GLY H 2 44  ? 74.441  82.359  25.040  1.000 48.705  ? 44  GLY FFF CA  1 
ATOM   11683 C C   . GLY H 2 44  ? 73.897  82.248  23.626  1.000 49.336  ? 44  GLY FFF C   1 
ATOM   11684 O O   . GLY H 2 44  ? 74.261  81.272  22.880  1.000 43.790  ? 44  GLY FFF O   1 
ATOM   11685 N N   . LEU H 2 45  ? 73.085  83.255  23.281  1.000 45.270  ? 45  LEU FFF N   1 
ATOM   11686 C CA  . LEU H 2 45  ? 72.369  83.437  21.996  1.000 42.123  ? 45  LEU FFF CA  1 
ATOM   11687 C C   . LEU H 2 45  ? 73.340  84.009  20.958  1.000 41.709  ? 45  LEU FFF C   1 
ATOM   11688 O O   . LEU H 2 45  ? 74.217  84.795  21.344  1.000 37.417  ? 45  LEU FFF O   1 
ATOM   11689 C CB  . LEU H 2 45  ? 71.208  84.404  22.238  1.000 41.459  ? 45  LEU FFF CB  1 
ATOM   11690 C CG  . LEU H 2 45  ? 70.299  84.049  23.410  1.000 40.789  ? 45  LEU FFF CG  1 
ATOM   11691 C CD1 . LEU H 2 45  ? 69.263  85.133  23.693  1.000 38.445  ? 45  LEU FFF CD1 1 
ATOM   11692 C CD2 . LEU H 2 45  ? 69.620  82.724  23.126  1.000 43.324  ? 45  LEU FFF CD2 1 
ATOM   11693 N N   . GLU H 2 46  ? 73.189  83.599  19.700  1.000 44.148  ? 46  GLU FFF N   1 
ATOM   11694 C CA  . GLU H 2 46  ? 73.994  84.049  18.537  1.000 48.398  ? 46  GLU FFF CA  1 
ATOM   11695 C C   . GLU H 2 46  ? 73.023  84.293  17.380  1.000 47.405  ? 46  GLU FFF C   1 
ATOM   11696 O O   . GLU H 2 46  ? 72.345  83.326  16.982  1.000 46.955  ? 46  GLU FFF O   1 
ATOM   11697 C CB  . GLU H 2 46  ? 75.036  82.990  18.149  1.000 55.408  ? 46  GLU FFF CB  1 
ATOM   11698 C CG  . GLU H 2 46  ? 75.813  82.400  19.320  1.000 60.867  ? 46  GLU FFF CG  1 
ATOM   11699 C CD  . GLU H 2 46  ? 76.448  81.041  19.054  1.000 61.063  ? 46  GLU FFF CD  1 
ATOM   11700 O OE1 . GLU H 2 46  ? 77.115  80.931  17.996  1.000 53.870  ? 46  GLU FFF OE1 1 
ATOM   11701 O OE2 . GLU H 2 46  ? 76.261  80.092  19.901  1.000 60.109  ? 46  GLU FFF OE2 1 
ATOM   11702 N N   . TRP H 2 47  ? 72.935  85.527  16.875  1.000 47.219  ? 47  TRP FFF N   1 
ATOM   11703 C CA  . TRP H 2 47  ? 72.028  85.857  15.743  1.000 45.698  ? 47  TRP FFF CA  1 
ATOM   11704 C C   . TRP H 2 47  ? 72.653  85.324  14.457  1.000 42.071  ? 47  TRP FFF C   1 
ATOM   11705 O O   . TRP H 2 47  ? 73.822  85.634  14.202  1.000 42.952  ? 47  TRP FFF O   1 
ATOM   11706 C CB  . TRP H 2 47  ? 71.757  87.362  15.676  1.000 49.754  ? 47  TRP FFF CB  1 
ATOM   11707 C CG  . TRP H 2 47  ? 70.778  87.781  14.621  1.000 54.051  ? 47  TRP FFF CG  1 
ATOM   11708 C CD1 . TRP H 2 47  ? 69.417  87.862  14.729  1.000 54.709  ? 47  TRP FFF CD1 1 
ATOM   11709 C CD2 . TRP H 2 47  ? 71.094  88.233  13.293  1.000 60.165  ? 47  TRP FFF CD2 1 
ATOM   11710 N NE1 . TRP H 2 47  ? 68.862  88.306  13.555  1.000 53.967  ? 47  TRP FFF NE1 1 
ATOM   11711 C CE2 . TRP H 2 47  ? 69.868  88.550  12.657  1.000 57.656  ? 47  TRP FFF CE2 1 
ATOM   11712 C CE3 . TRP H 2 47  ? 72.294  88.407  12.587  1.000 64.039  ? 47  TRP FFF CE3 1 
ATOM   11713 C CZ2 . TRP H 2 47  ? 69.814  89.029  11.348  1.000 57.424  ? 47  TRP FFF CZ2 1 
ATOM   11714 C CZ3 . TRP H 2 47  ? 72.240  88.874  11.289  1.000 63.220  ? 47  TRP FFF CZ3 1 
ATOM   11715 C CH2 . TRP H 2 47  ? 71.015  89.190  10.687  1.000 61.292  ? 47  TRP FFF CH2 1 
ATOM   11716 N N   . MET H 2 48  ? 71.913  84.519  13.702  1.000 41.006  ? 48  MET FFF N   1 
ATOM   11717 C CA  . MET H 2 48  ? 72.445  83.794  12.520  1.000 42.848  ? 48  MET FFF CA  1 
ATOM   11718 C C   . MET H 2 48  ? 72.091  84.573  11.259  1.000 41.747  ? 48  MET FFF C   1 
ATOM   11719 O O   . MET H 2 48  ? 72.951  84.683  10.383  1.000 49.785  ? 48  MET FFF O   1 
ATOM   11720 C CB  . MET H 2 48  ? 71.860  82.383  12.395  1.000 43.471  ? 48  MET FFF CB  1 
ATOM   11721 C CG  . MET H 2 48  ? 72.035  81.537  13.637  1.000 43.438  ? 48  MET FFF CG  1 
ATOM   11722 S SD  . MET H 2 48  ? 71.307  79.923  13.387  1.000 47.064  ? 48  MET FFF SD  1 
ATOM   11723 C CE  . MET H 2 48  ? 72.514  79.220  12.270  1.000 50.113  ? 48  MET FFF CE  1 
ATOM   11724 N N   . GLY H 2 49  ? 70.859  85.059  11.166  1.000 41.403  ? 49  GLY FFF N   1 
ATOM   11725 C CA  . GLY H 2 49  ? 70.358  85.753  9.970   1.000 41.934  ? 49  GLY FFF CA  1 
ATOM   11726 C C   . GLY H 2 49  ? 68.881  86.045  10.085  1.000 43.660  ? 49  GLY FFF C   1 
ATOM   11727 O O   . GLY H 2 49  ? 68.249  85.612  11.050  1.000 44.922  ? 49  GLY FFF O   1 
ATOM   11728 N N   . ILE H 2 50  ? 68.343  86.775  9.128   1.000 45.869  ? 50  ILE FFF N   1 
ATOM   11729 C CA  . ILE H 2 50  ? 66.908  87.154  9.110   1.000 47.565  ? 50  ILE FFF CA  1 
ATOM   11730 C C   . ILE H 2 50  ? 66.450  87.025  7.661   1.000 46.285  ? 50  ILE FFF C   1 
ATOM   11731 O O   . ILE H 2 50  ? 67.294  87.168  6.761   1.000 41.105  ? 50  ILE FFF O   1 
ATOM   11732 C CB  . ILE H 2 50  ? 66.727  88.571  9.694   1.000 48.147  ? 50  ILE FFF CB  1 
ATOM   11733 C CG1 . ILE H 2 50  ? 65.260  88.969  9.861   1.000 47.202  ? 50  ILE FFF CG1 1 
ATOM   11734 C CG2 . ILE H 2 50  ? 67.478  89.583  8.856   1.000 49.440  ? 50  ILE FFF CG2 1 
ATOM   11735 C CD1 . ILE H 2 50  ? 65.063  90.178  10.746  1.000 48.244  ? 50  ILE FFF CD1 1 
ATOM   11736 N N   . ILE H 2 51  ? 65.182  86.703  7.453   1.000 44.766  ? 51  ILE FFF N   1 
ATOM   11737 C CA  . ILE H 2 51  ? 64.585  86.710  6.096   1.000 45.713  ? 51  ILE FFF CA  1 
ATOM   11738 C C   . ILE H 2 51  ? 63.262  87.458  6.163   1.000 45.954  ? 51  ILE FFF C   1 
ATOM   11739 O O   . ILE H 2 51  ? 62.650  87.482  7.247   1.000 49.890  ? 51  ILE FFF O   1 
ATOM   11740 C CB  . ILE H 2 51  ? 64.413  85.291  5.534   1.000 48.261  ? 51  ILE FFF CB  1 
ATOM   11741 C CG1 . ILE H 2 51  ? 64.434  85.308  3.999   1.000 51.750  ? 51  ILE FFF CG1 1 
ATOM   11742 C CG2 . ILE H 2 51  ? 63.160  84.631  6.082   1.000 47.580  ? 51  ILE FFF CG2 1 
ATOM   11743 C CD1 . ILE H 2 51  ? 64.491  83.943  3.356   1.000 51.519  ? 51  ILE FFF CD1 1 
ATOM   11744 N N   . TYR H 2 52  ? 62.877  88.077  5.045   1.000 43.692  ? 52  TYR FFF N   1 
ATOM   11745 C CA  . TYR H 2 52  ? 61.513  88.598  4.819   1.000 41.707  ? 52  TYR FFF CA  1 
ATOM   11746 C C   . TYR H 2 52  ? 60.811  87.599  3.916   1.000 43.151  ? 52  TYR FFF C   1 
ATOM   11747 O O   . TYR H 2 52  ? 61.264  87.334  2.812   1.000 46.074  ? 52  TYR FFF O   1 
ATOM   11748 C CB  . TYR H 2 52  ? 61.517  90.013  4.244   1.000 39.152  ? 52  TYR FFF CB  1 
ATOM   11749 C CG  . TYR H 2 52  ? 60.125  90.574  4.115   1.000 38.893  ? 52  TYR FFF CG  1 
ATOM   11750 C CD1 . TYR H 2 52  ? 59.442  91.064  5.213   1.000 39.526  ? 52  TYR FFF CD1 1 
ATOM   11751 C CD2 . TYR H 2 52  ? 59.450  90.535  2.909   1.000 38.970  ? 52  TYR FFF CD2 1 
ATOM   11752 C CE1 . TYR H 2 52  ? 58.142  91.540  5.107   1.000 40.199  ? 52  TYR FFF CE1 1 
ATOM   11753 C CE2 . TYR H 2 52  ? 58.152  91.000  2.783   1.000 40.973  ? 52  TYR FFF CE2 1 
ATOM   11754 C CZ  . TYR H 2 52  ? 57.486  91.494  3.887   1.000 40.949  ? 52  TYR FFF CZ  1 
ATOM   11755 O OH  . TYR H 2 52  ? 56.218  91.972  3.715   1.000 39.481  ? 52  TYR FFF OH  1 
ATOM   11756 N N   . PRO H 2 53  ? 59.711  86.979  4.377   1.000 45.239  ? 53  PRO FFF N   1 
ATOM   11757 C CA  . PRO H 2 53  ? 59.029  85.968  3.578   1.000 47.211  ? 53  PRO FFF CA  1 
ATOM   11758 C C   . PRO H 2 53  ? 58.494  86.508  2.245   1.000 47.531  ? 53  PRO FFF C   1 
ATOM   11759 O O   . PRO H 2 53  ? 58.621  85.817  1.268   1.000 50.217  ? 53  PRO FFF O   1 
ATOM   11760 C CB  . PRO H 2 53  ? 57.863  85.526  4.468   1.000 49.685  ? 53  PRO FFF CB  1 
ATOM   11761 C CG  . PRO H 2 53  ? 58.266  85.952  5.865   1.000 49.565  ? 53  PRO FFF CG  1 
ATOM   11762 C CD  . PRO H 2 53  ? 59.073  87.213  5.681   1.000 47.239  ? 53  PRO FFF CD  1 
ATOM   11763 N N   . GLY H 2 54  ? 57.885  87.694  2.256   1.000 53.096  ? 54  GLY FFF N   1 
ATOM   11764 C CA  . GLY H 2 54  ? 57.172  88.283  1.104   1.000 55.388  ? 54  GLY FFF CA  1 
ATOM   11765 C C   . GLY H 2 54  ? 57.995  88.292  -0.182  1.000 57.745  ? 54  GLY FFF C   1 
ATOM   11766 O O   . GLY H 2 54  ? 57.387  88.037  -1.228  1.000 58.341  ? 54  GLY FFF O   1 
ATOM   11767 N N   . ASP H 2 55  ? 59.308  88.560  -0.135  1.000 59.925  ? 55  ASP FFF N   1 
ATOM   11768 C CA  . ASP H 2 55  ? 60.176  88.658  -1.345  1.000 64.607  ? 55  ASP FFF CA  1 
ATOM   11769 C C   . ASP H 2 55  ? 61.515  87.927  -1.142  1.000 62.848  ? 55  ASP FFF C   1 
ATOM   11770 O O   . ASP H 2 55  ? 62.408  88.098  -1.985  1.000 62.164  ? 55  ASP FFF O   1 
ATOM   11771 C CB  . ASP H 2 55  ? 60.404  90.127  -1.735  1.000 70.548  ? 55  ASP FFF CB  1 
ATOM   11772 C CG  . ASP H 2 55  ? 61.231  90.948  -0.752  1.000 70.262  ? 55  ASP FFF CG  1 
ATOM   11773 O OD1 . ASP H 2 55  ? 61.461  90.480  0.369   1.000 66.210  ? 55  ASP FFF OD1 1 
ATOM   11774 O OD2 . ASP H 2 55  ? 61.608  92.073  -1.104  1.000 77.300  ? 55  ASP FFF OD2 1 
ATOM   11775 N N   . SER H 2 56  ? 61.661  87.140  -0.074  1.000 60.881  ? 56  SER FFF N   1 
ATOM   11776 C CA  . SER H 2 56  ? 62.862  86.310  0.221   1.000 56.434  ? 56  SER FFF CA  1 
ATOM   11777 C C   . SER H 2 56  ? 64.127  87.164  0.371   1.000 52.371  ? 56  SER FFF C   1 
ATOM   11778 O O   . SER H 2 56  ? 65.190  86.689  -0.041  1.000 49.490  ? 56  SER FFF O   1 
ATOM   11779 C CB  . SER H 2 56  ? 63.055  85.252  -0.838  1.000 54.459  ? 56  SER FFF CB  1 
ATOM   11780 O OG  . SER H 2 56  ? 61.936  84.387  -0.878  1.000 57.668  ? 56  SER FFF OG  1 
ATOM   11781 N N   . GLU H 2 57  ? 64.033  88.376  0.920   1.000 55.820  ? 57  GLU FFF N   1 
ATOM   11782 C CA  . GLU H 2 57  ? 65.240  89.208  1.194   1.000 59.528  ? 57  GLU FFF CA  1 
ATOM   11783 C C   . GLU H 2 57  ? 65.948  88.586  2.394   1.000 52.154  ? 57  GLU FFF C   1 
ATOM   11784 O O   . GLU H 2 57  ? 65.314  88.491  3.454   1.000 59.243  ? 57  GLU FFF O   1 
ATOM   11785 C CB  . GLU H 2 57  ? 64.911  90.677  1.491   1.000 64.912  ? 57  GLU FFF CB  1 
ATOM   11786 C CG  . GLU H 2 57  ? 66.159  91.551  1.632   1.000 67.432  ? 57  GLU FFF CG  1 
ATOM   11787 C CD  . GLU H 2 57  ? 66.031  92.881  2.366   1.000 66.743  ? 57  GLU FFF CD  1 
ATOM   11788 O OE1 . GLU H 2 57  ? 65.035  93.609  2.148   1.000 68.625  ? 57  GLU FFF OE1 1 
ATOM   11789 O OE2 . GLU H 2 57  ? 66.940  93.193  3.150   1.000 65.128  ? 57  GLU FFF OE2 1 
ATOM   11790 N N   . THR H 2 58  ? 67.204  88.184  2.235   1.000 44.436  ? 58  THR FFF N   1 
ATOM   11791 C CA  . THR H 2 58  ? 67.913  87.357  3.239   1.000 45.656  ? 58  THR FFF CA  1 
ATOM   11792 C C   . THR H 2 58  ? 69.191  88.066  3.664   1.000 42.041  ? 58  THR FFF C   1 
ATOM   11793 O O   . THR H 2 58  ? 70.010  88.321  2.787   1.000 44.704  ? 58  THR FFF O   1 
ATOM   11794 C CB  . THR H 2 58  ? 68.211  85.960  2.682   1.000 49.397  ? 58  THR FFF CB  1 
ATOM   11795 O OG1 . THR H 2 58  ? 67.153  85.538  1.822   1.000 52.103  ? 58  THR FFF OG1 1 
ATOM   11796 C CG2 . THR H 2 58  ? 68.351  84.930  3.771   1.000 49.847  ? 58  THR FFF CG2 1 
ATOM   11797 N N   . ARG H 2 59  ? 69.340  88.355  4.955   1.000 43.332  ? 59  ARG FFF N   1 
ATOM   11798 C CA  . ARG H 2 59  ? 70.571  88.945  5.548   1.000 47.144  ? 59  ARG FFF CA  1 
ATOM   11799 C C   . ARG H 2 59  ? 71.194  87.923  6.497   1.000 46.549  ? 59  ARG FFF C   1 
ATOM   11800 O O   . ARG H 2 59  ? 70.457  87.398  7.346   1.000 51.083  ? 59  ARG FFF O   1 
ATOM   11801 C CB  . ARG H 2 59  ? 70.252  90.224  6.320   1.000 52.370  ? 59  ARG FFF CB  1 
ATOM   11802 C CG  . ARG H 2 59  ? 69.426  91.226  5.536   1.000 57.297  ? 59  ARG FFF CG  1 
ATOM   11803 C CD  . ARG H 2 59  ? 70.192  92.504  5.269   1.000 63.631  ? 59  ARG FFF CD  1 
ATOM   11804 N NE  . ARG H 2 59  ? 69.795  93.614  6.132   1.000 64.307  ? 59  ARG FFF NE  1 
ATOM   11805 C CZ  . ARG H 2 59  ? 68.684  94.347  5.985   1.000 58.488  ? 59  ARG FFF CZ  1 
ATOM   11806 N NH1 . ARG H 2 59  ? 67.788  94.070  5.048   1.000 51.089  ? 59  ARG FFF NH1 1 
ATOM   11807 N NH2 . ARG H 2 59  ? 68.463  95.351  6.810   1.000 61.169  ? 59  ARG FFF NH2 1 
ATOM   11808 N N   . TYR H 2 60  ? 72.487  87.646  6.347   1.000 45.335  ? 60  TYR FFF N   1 
ATOM   11809 C CA  . TYR H 2 60  ? 73.241  86.669  7.168   1.000 48.954  ? 60  TYR FFF CA  1 
ATOM   11810 C C   . TYR H 2 60  ? 74.112  87.436  8.166   1.000 50.387  ? 60  TYR FFF C   1 
ATOM   11811 O O   . TYR H 2 60  ? 74.401  88.607  7.943   1.000 54.341  ? 60  TYR FFF O   1 
ATOM   11812 C CB  . TYR H 2 60  ? 74.077  85.759  6.267   1.000 52.163  ? 60  TYR FFF CB  1 
ATOM   11813 C CG  . TYR H 2 60  ? 73.306  84.706  5.508   1.000 56.575  ? 60  TYR FFF CG  1 
ATOM   11814 C CD1 . TYR H 2 60  ? 73.955  83.660  4.865   1.000 68.961  ? 60  TYR FFF CD1 1 
ATOM   11815 C CD2 . TYR H 2 60  ? 71.931  84.738  5.430   1.000 54.443  ? 60  TYR FFF CD2 1 
ATOM   11816 C CE1 . TYR H 2 60  ? 73.257  82.687  4.167   1.000 66.019  ? 60  TYR FFF CE1 1 
ATOM   11817 C CE2 . TYR H 2 60  ? 71.221  83.776  4.742   1.000 56.136  ? 60  TYR FFF CE2 1 
ATOM   11818 C CZ  . TYR H 2 60  ? 71.880  82.754  4.113   1.000 59.569  ? 60  TYR FFF CZ  1 
ATOM   11819 O OH  . TYR H 2 60  ? 71.126  81.851  3.446   1.000 65.355  ? 60  TYR FFF OH  1 
ATOM   11820 N N   . SER H 2 61  ? 74.478  86.795  9.269   1.000 51.965  ? 61  SER FFF N   1 
ATOM   11821 C CA  . SER H 2 61  ? 75.588  87.233  10.143  1.000 55.515  ? 61  SER FFF CA  1 
ATOM   11822 C C   . SER H 2 61  ? 76.889  86.748  9.515   1.000 57.832  ? 61  SER FFF C   1 
ATOM   11823 O O   . SER H 2 61  ? 76.925  85.674  8.908   1.000 57.350  ? 61  SER FFF O   1 
ATOM   11824 C CB  . SER H 2 61  ? 75.438  86.718  11.545  1.000 61.157  ? 61  SER FFF CB  1 
ATOM   11825 O OG  . SER H 2 61  ? 76.712  86.590  12.161  1.000 65.497  ? 61  SER FFF OG  1 
ATOM   11826 N N   . PRO H 2 62  ? 77.983  87.533  9.648   1.000 59.670  ? 62  PRO FFF N   1 
ATOM   11827 C CA  . PRO H 2 62  ? 79.298  87.138  9.149   1.000 58.811  ? 62  PRO FFF CA  1 
ATOM   11828 C C   . PRO H 2 62  ? 79.674  85.687  9.482   1.000 60.512  ? 62  PRO FFF C   1 
ATOM   11829 O O   . PRO H 2 62  ? 80.281  85.039  8.659   1.000 63.565  ? 62  PRO FFF O   1 
ATOM   11830 C CB  . PRO H 2 62  ? 80.262  88.069  9.898   1.000 57.660  ? 62  PRO FFF CB  1 
ATOM   11831 C CG  . PRO H 2 62  ? 79.444  89.311  10.183  1.000 58.859  ? 62  PRO FFF CG  1 
ATOM   11832 C CD  . PRO H 2 62  ? 78.010  88.845  10.311  1.000 57.775  ? 62  PRO FFF CD  1 
ATOM   11833 N N   . SER H 2 63  ? 79.326  85.220  10.685  1.000 56.426  ? 63  SER FFF N   1 
ATOM   11834 C CA  . SER H 2 63  ? 79.785  83.921  11.241  1.000 56.577  ? 63  SER FFF CA  1 
ATOM   11835 C C   . SER H 2 63  ? 79.060  82.757  10.555  1.000 60.592  ? 63  SER FFF C   1 
ATOM   11836 O O   . SER H 2 63  ? 79.557  81.616  10.655  1.000 67.323  ? 63  SER FFF O   1 
ATOM   11837 C CB  . SER H 2 63  ? 79.594  83.872  12.731  1.000 56.875  ? 63  SER FFF CB  1 
ATOM   11838 O OG  . SER H 2 63  ? 79.911  85.126  13.322  1.000 57.973  ? 63  SER FFF OG  1 
ATOM   11839 N N   . PHE H 2 64  ? 77.920  83.022  9.908   1.000 58.320  ? 64  PHE FFF N   1 
ATOM   11840 C CA  . PHE H 2 64  ? 77.039  81.982  9.315   1.000 57.805  ? 64  PHE FFF CA  1 
ATOM   11841 C C   . PHE H 2 64  ? 76.884  82.192  7.808   1.000 58.045  ? 64  PHE FFF C   1 
ATOM   11842 O O   . PHE H 2 64  ? 76.136  81.427  7.201   1.000 59.667  ? 64  PHE FFF O   1 
ATOM   11843 C CB  . PHE H 2 64  ? 75.681  81.967  10.024  1.000 55.303  ? 64  PHE FFF CB  1 
ATOM   11844 C CG  . PHE H 2 64  ? 75.773  81.689  11.504  1.000 53.909  ? 64  PHE FFF CG  1 
ATOM   11845 C CD1 . PHE H 2 64  ? 75.909  80.394  11.983  1.000 54.180  ? 64  PHE FFF CD1 1 
ATOM   11846 C CD2 . PHE H 2 64  ? 75.779  82.729  12.416  1.000 55.646  ? 64  PHE FFF CD2 1 
ATOM   11847 C CE1 . PHE H 2 64  ? 76.030  80.144  13.340  1.000 53.894  ? 64  PHE FFF CE1 1 
ATOM   11848 C CE2 . PHE H 2 64  ? 75.893  82.480  13.776  1.000 57.357  ? 64  PHE FFF CE2 1 
ATOM   11849 C CZ  . PHE H 2 64  ? 76.020  81.187  14.234  1.000 56.680  ? 64  PHE FFF CZ  1 
ATOM   11850 N N   . GLN H 2 65  ? 77.573  83.167  7.218   1.000 60.285  ? 65  GLN FFF N   1 
ATOM   11851 C CA  . GLN H 2 65  ? 77.571  83.357  5.745   1.000 63.821  ? 65  GLN FFF CA  1 
ATOM   11852 C C   . GLN H 2 65  ? 78.001  82.033  5.100   1.000 55.971  ? 65  GLN FFF C   1 
ATOM   11853 O O   . GLN H 2 65  ? 79.066  81.519  5.478   1.000 44.014  ? 65  GLN FFF O   1 
ATOM   11854 C CB  . GLN H 2 65  ? 78.471  84.530  5.342   1.000 76.030  ? 65  GLN FFF CB  1 
ATOM   11855 C CG  . GLN H 2 65  ? 78.480  84.826  3.844   1.000 85.051  ? 65  GLN FFF CG  1 
ATOM   11856 C CD  . GLN H 2 65  ? 77.148  85.328  3.333   1.000 90.869  ? 65  GLN FFF CD  1 
ATOM   11857 O OE1 . GLN H 2 65  ? 76.528  86.219  3.920   1.000 79.714  ? 65  GLN FFF OE1 1 
ATOM   11858 N NE2 . GLN H 2 65  ? 76.701  84.763  2.218   1.000 99.586  ? 65  GLN FFF NE2 1 
ATOM   11859 N N   . GLY H 2 66  ? 77.165  81.475  4.218   1.000 57.537  ? 66  GLY FFF N   1 
ATOM   11860 C CA  . GLY H 2 66  ? 77.484  80.275  3.412   1.000 62.825  ? 66  GLY FFF CA  1 
ATOM   11861 C C   . GLY H 2 66  ? 77.784  79.022  4.235   1.000 64.443  ? 66  GLY FFF C   1 
ATOM   11862 O O   . GLY H 2 66  ? 78.135  78.002  3.609   1.000 60.597  ? 66  GLY FFF O   1 
ATOM   11863 N N   . GLN H 2 67  ? 77.610  79.071  5.567   1.000 67.365  ? 67  GLN FFF N   1 
ATOM   11864 C CA  . GLN H 2 67  ? 77.621  77.902  6.495   1.000 59.844  ? 67  GLN FFF CA  1 
ATOM   11865 C C   . GLN H 2 67  ? 76.217  77.293  6.602   1.000 53.427  ? 67  GLN FFF C   1 
ATOM   11866 O O   . GLN H 2 67  ? 76.141  76.080  6.806   1.000 55.393  ? 67  GLN FFF O   1 
ATOM   11867 C CB  . GLN H 2 67  ? 78.118  78.313  7.883   1.000 62.201  ? 67  GLN FFF CB  1 
ATOM   11868 C CG  . GLN H 2 67  ? 79.565  78.789  7.893   1.000 67.655  ? 67  GLN FFF CG  1 
ATOM   11869 C CD  . GLN H 2 67  ? 80.539  77.771  7.348   1.000 73.807  ? 67  GLN FFF CD  1 
ATOM   11870 O OE1 . GLN H 2 67  ? 80.320  76.563  7.430   1.000 89.402  ? 67  GLN FFF OE1 1 
ATOM   11871 N NE2 . GLN H 2 67  ? 81.632  78.255  6.779   1.000 79.848  ? 67  GLN FFF NE2 1 
ATOM   11872 N N   . VAL H 2 68  ? 75.169  78.110  6.468   1.000 47.921  ? 68  VAL FFF N   1 
ATOM   11873 C CA  . VAL H 2 68  ? 73.740  77.685  6.427   1.000 48.598  ? 68  VAL FFF CA  1 
ATOM   11874 C C   . VAL H 2 68  ? 73.042  78.428  5.289   1.000 47.840  ? 68  VAL FFF C   1 
ATOM   11875 O O   . VAL H 2 68  ? 73.668  79.289  4.673   1.000 47.211  ? 68  VAL FFF O   1 
ATOM   11876 C CB  . VAL H 2 68  ? 73.011  77.975  7.752   1.000 50.286  ? 68  VAL FFF CB  1 
ATOM   11877 C CG1 . VAL H 2 68  ? 73.773  77.448  8.945   1.000 51.783  ? 68  VAL FFF CG1 1 
ATOM   11878 C CG2 . VAL H 2 68  ? 72.734  79.458  7.929   1.000 52.470  ? 68  VAL FFF CG2 1 
ATOM   11879 N N   . THR H 2 69  ? 71.768  78.107  5.069   1.000 47.295  ? 69  THR FFF N   1 
ATOM   11880 C CA  . THR H 2 69  ? 70.878  78.718  4.047   1.000 48.130  ? 69  THR FFF CA  1 
ATOM   11881 C C   . THR H 2 69  ? 69.499  78.963  4.660   1.000 51.280  ? 69  THR FFF C   1 
ATOM   11882 O O   . THR H 2 69  ? 68.746  77.978  4.912   1.000 50.390  ? 69  THR FFF O   1 
ATOM   11883 C CB  . THR H 2 69  ? 70.715  77.850  2.793   1.000 49.802  ? 69  THR FFF CB  1 
ATOM   11884 O OG1 . THR H 2 69  ? 71.992  77.673  2.188   1.000 47.132  ? 69  THR FFF OG1 1 
ATOM   11885 C CG2 . THR H 2 69  ? 69.738  78.431  1.791   1.000 49.977  ? 69  THR FFF CG2 1 
ATOM   11886 N N   . ILE H 2 70  ? 69.170  80.237  4.865   1.000 50.224  ? 70  ILE FFF N   1 
ATOM   11887 C CA  . ILE H 2 70  ? 67.816  80.683  5.291   1.000 46.211  ? 70  ILE FFF CA  1 
ATOM   11888 C C   . ILE H 2 70  ? 66.986  80.885  4.029   1.000 44.588  ? 70  ILE FFF C   1 
ATOM   11889 O O   . ILE H 2 70  ? 67.480  81.538  3.116   1.000 55.471  ? 70  ILE FFF O   1 
ATOM   11890 C CB  . ILE H 2 70  ? 67.926  81.955  6.135   1.000 45.224  ? 70  ILE FFF CB  1 
ATOM   11891 C CG1 . ILE H 2 70  ? 68.869  81.732  7.323   1.000 45.070  ? 70  ILE FFF CG1 1 
ATOM   11892 C CG2 . ILE H 2 70  ? 66.536  82.421  6.542   1.000 45.744  ? 70  ILE FFF CG2 1 
ATOM   11893 C CD1 . ILE H 2 70  ? 69.224  82.985  8.100   1.000 44.818  ? 70  ILE FFF CD1 1 
ATOM   11894 N N   . SER H 2 71  ? 65.794  80.309  3.986   1.000 44.190  ? 71  SER FFF N   1 
ATOM   11895 C CA  . SER H 2 71  ? 64.884  80.289  2.816   1.000 47.148  ? 71  SER FFF CA  1 
ATOM   11896 C C   . SER H 2 71  ? 63.481  80.579  3.329   1.000 46.105  ? 71  SER FFF C   1 
ATOM   11897 O O   . SER H 2 71  ? 63.318  80.648  4.557   1.000 46.710  ? 71  SER FFF O   1 
ATOM   11898 C CB  . SER H 2 71  ? 64.956  78.970  2.064   1.000 55.168  ? 71  SER FFF CB  1 
ATOM   11899 O OG  . SER H 2 71  ? 65.196  77.864  2.929   1.000 62.878  ? 71  SER FFF OG  1 
ATOM   11900 N N   . ALA H 2 72  ? 62.510  80.765  2.444   1.000 48.015  ? 72  ALA FFF N   1 
ATOM   11901 C CA  . ALA H 2 72  ? 61.126  81.072  2.857   1.000 51.128  ? 72  ALA FFF CA  1 
ATOM   11902 C C   . ALA H 2 72  ? 60.134  80.489  1.857   1.000 52.252  ? 72  ALA FFF C   1 
ATOM   11903 O O   . ALA H 2 72  ? 60.526  80.165  0.733   1.000 57.289  ? 72  ALA FFF O   1 
ATOM   11904 C CB  . ALA H 2 72  ? 60.971  82.559  2.992   1.000 53.624  ? 72  ALA FFF CB  1 
ATOM   11905 N N   . ASP H 2 73  ? 58.888  80.359  2.291   1.000 55.117  ? 73  ASP FFF N   1 
ATOM   11906 C CA  . ASP H 2 73  ? 57.736  79.982  1.438   1.000 60.715  ? 73  ASP FFF CA  1 
ATOM   11907 C C   . ASP H 2 73  ? 56.534  80.771  1.959   1.000 62.383  ? 73  ASP FFF C   1 
ATOM   11908 O O   . ASP H 2 73  ? 55.909  80.335  2.967   1.000 50.915  ? 73  ASP FFF O   1 
ATOM   11909 C CB  . ASP H 2 73  ? 57.540  78.468  1.422   1.000 62.159  ? 73  ASP FFF CB  1 
ATOM   11910 C CG  . ASP H 2 73  ? 56.496  77.978  0.430   1.000 63.432  ? 73  ASP FFF CG  1 
ATOM   11911 O OD1 . ASP H 2 73  ? 55.564  78.742  0.129   1.000 70.131  ? 73  ASP FFF OD1 1 
ATOM   11912 O OD2 . ASP H 2 73  ? 56.624  76.826  -0.032  1.000 69.220  ? 73  ASP FFF OD2 1 
ATOM   11913 N N   . LYS H 2 74  ? 56.282  81.921  1.321   1.000 63.923  ? 74  LYS FFF N   1 
ATOM   11914 C CA  . LYS H 2 74  ? 55.263  82.915  1.740   1.000 63.976  ? 74  LYS FFF CA  1 
ATOM   11915 C C   . LYS H 2 74  ? 53.869  82.291  1.618   1.000 60.178  ? 74  LYS FFF C   1 
ATOM   11916 O O   . LYS H 2 74  ? 52.975  82.787  2.315   1.000 60.735  ? 74  LYS FFF O   1 
ATOM   11917 C CB  . LYS H 2 74  ? 55.389  84.209  0.928   1.000 69.905  ? 74  LYS FFF CB  1 
ATOM   11918 C CG  . LYS H 2 74  ? 55.480  84.016  -0.576  1.000 75.557  ? 74  LYS FFF CG  1 
ATOM   11919 C CD  . LYS H 2 74  ? 55.653  85.289  -1.389  1.000 76.949  ? 74  LYS FFF CD  1 
ATOM   11920 C CE  . LYS H 2 74  ? 56.010  84.982  -2.834  1.000 79.648  ? 74  LYS FFF CE  1 
ATOM   11921 N NZ  . LYS H 2 74  ? 57.030  85.897  -3.414  1.000 86.389  ? 74  LYS FFF NZ  1 
ATOM   11922 N N   . SER H 2 75  ? 53.698  81.247  0.791   1.000 58.461  ? 75  SER FFF N   1 
ATOM   11923 C CA  . SER H 2 75  ? 52.386  80.601  0.503   1.000 59.359  ? 75  SER FFF CA  1 
ATOM   11924 C C   . SER H 2 75  ? 51.861  79.853  1.735   1.000 56.867  ? 75  SER FFF C   1 
ATOM   11925 O O   . SER H 2 75  ? 50.635  79.712  1.839   1.000 53.213  ? 75  SER FFF O   1 
ATOM   11926 C CB  . SER H 2 75  ? 52.448  79.691  -0.715  1.000 61.571  ? 75  SER FFF CB  1 
ATOM   11927 O OG  . SER H 2 75  ? 53.324  78.591  -0.522  1.000 63.440  ? 75  SER FFF OG  1 
ATOM   11928 N N   . ILE H 2 76  ? 52.747  79.419  2.638   1.000 61.154  ? 76  ILE FFF N   1 
ATOM   11929 C CA  . ILE H 2 76  ? 52.395  78.645  3.872   1.000 59.713  ? 76  ILE FFF CA  1 
ATOM   11930 C C   . ILE H 2 76  ? 52.914  79.357  5.136   1.000 60.120  ? 76  ILE FFF C   1 
ATOM   11931 O O   . ILE H 2 76  ? 52.801  78.757  6.228   1.000 60.349  ? 76  ILE FFF O   1 
ATOM   11932 C CB  . ILE H 2 76  ? 52.915  77.196  3.759   1.000 55.960  ? 76  ILE FFF CB  1 
ATOM   11933 C CG1 . ILE H 2 76  ? 54.333  77.137  3.181   1.000 58.673  ? 76  ILE FFF CG1 1 
ATOM   11934 C CG2 . ILE H 2 76  ? 51.938  76.368  2.943   1.000 57.570  ? 76  ILE FFF CG2 1 
ATOM   11935 C CD1 . ILE H 2 76  ? 54.965  75.755  3.151   1.000 57.672  ? 76  ILE FFF CD1 1 
ATOM   11936 N N   . ASN H 2 77  ? 53.443  80.579  5.007   1.000 60.577  ? 77  ASN FFF N   1 
ATOM   11937 C CA  . ASN H 2 77  ? 53.896  81.436  6.138   1.000 58.903  ? 77  ASN FFF CA  1 
ATOM   11938 C C   . ASN H 2 77  ? 55.046  80.752  6.884   1.000 57.500  ? 77  ASN FFF C   1 
ATOM   11939 O O   . ASN H 2 77  ? 55.044  80.774  8.133   1.000 54.219  ? 77  ASN FFF O   1 
ATOM   11940 C CB  . ASN H 2 77  ? 52.731  81.781  7.074   1.000 54.406  ? 77  ASN FFF CB  1 
ATOM   11941 C CG  . ASN H 2 77  ? 51.735  82.690  6.402   1.000 51.755  ? 77  ASN FFF CG  1 
ATOM   11942 O OD1 . ASN H 2 77  ? 51.926  83.071  5.255   1.000 58.536  ? 77  ASN FFF OD1 1 
ATOM   11943 N ND2 . ASN H 2 77  ? 50.697  83.070  7.113   1.000 50.034  ? 77  ASN FFF ND2 1 
ATOM   11944 N N   . THR H 2 78  ? 56.008  80.196  6.148   1.000 56.182  ? 78  THR FFF N   1 
ATOM   11945 C CA  . THR H 2 78  ? 57.037  79.304  6.735   1.000 57.379  ? 78  THR FFF CA  1 
ATOM   11946 C C   . THR H 2 78  ? 58.424  79.768  6.315   1.000 50.335  ? 78  THR FFF C   1 
ATOM   11947 O O   . THR H 2 78  ? 58.683  79.867  5.105   1.000 49.713  ? 78  THR FFF O   1 
ATOM   11948 C CB  . THR H 2 78  ? 56.808  77.841  6.340   1.000 62.848  ? 78  THR FFF CB  1 
ATOM   11949 O OG1 . THR H 2 78  ? 55.419  77.543  6.517   1.000 63.887  ? 78  THR FFF OG1 1 
ATOM   11950 C CG2 . THR H 2 78  ? 57.655  76.885  7.152   1.000 65.428  ? 78  THR FFF CG2 1 
ATOM   11951 N N   . ALA H 2 79  ? 59.273  80.023  7.303   1.000 46.904  ? 79  ALA FFF N   1 
ATOM   11952 C CA  . ALA H 2 79  ? 60.722  80.253  7.131   1.000 47.266  ? 79  ALA FFF CA  1 
ATOM   11953 C C   . ALA H 2 79  ? 61.479  78.944  7.407   1.000 45.813  ? 79  ALA FFF C   1 
ATOM   11954 O O   . ALA H 2 79  ? 61.034  78.157  8.269   1.000 46.584  ? 79  ALA FFF O   1 
ATOM   11955 C CB  . ALA H 2 79  ? 61.156  81.349  8.064   1.000 48.095  ? 79  ALA FFF CB  1 
ATOM   11956 N N   . TYR H 2 80  ? 62.597  78.732  6.717   1.000 40.932  ? 80  TYR FFF N   1 
ATOM   11957 C CA  . TYR H 2 80  ? 63.406  77.493  6.782   1.000 40.681  ? 80  TYR FFF CA  1 
ATOM   11958 C C   . TYR H 2 80  ? 64.850  77.881  7.063   1.000 42.117  ? 80  TYR FFF C   1 
ATOM   11959 O O   . TYR H 2 80  ? 65.300  78.920  6.596   1.000 42.716  ? 80  TYR FFF O   1 
ATOM   11960 C CB  . TYR H 2 80  ? 63.307  76.683  5.484   1.000 40.079  ? 80  TYR FFF CB  1 
ATOM   11961 C CG  . TYR H 2 80  ? 61.933  76.155  5.144   1.000 40.869  ? 80  TYR FFF CG  1 
ATOM   11962 C CD1 . TYR H 2 80  ? 61.532  74.881  5.502   1.000 41.461  ? 80  TYR FFF CD1 1 
ATOM   11963 C CD2 . TYR H 2 80  ? 61.019  76.939  4.466   1.000 42.101  ? 80  TYR FFF CD2 1 
ATOM   11964 C CE1 . TYR H 2 80  ? 60.276  74.392  5.178   1.000 44.355  ? 80  TYR FFF CE1 1 
ATOM   11965 C CE2 . TYR H 2 80  ? 59.750  76.475  4.154   1.000 44.221  ? 80  TYR FFF CE2 1 
ATOM   11966 C CZ  . TYR H 2 80  ? 59.374  75.193  4.505   1.000 44.488  ? 80  TYR FFF CZ  1 
ATOM   11967 O OH  . TYR H 2 80  ? 58.120  74.743  4.195   1.000 45.492  ? 80  TYR FFF OH  1 
ATOM   11968 N N   . LEU H 2 81  ? 65.548  77.049  7.822   1.000 47.456  ? 81  LEU FFF N   1 
ATOM   11969 C CA  . LEU H 2 81  ? 67.012  77.142  8.043   1.000 49.252  ? 81  LEU FFF CA  1 
ATOM   11970 C C   . LEU H 2 81  ? 67.604  75.756  7.736   1.000 53.432  ? 81  LEU FFF C   1 
ATOM   11971 O O   . LEU H 2 81  ? 67.142  74.804  8.389   1.000 57.818  ? 81  LEU FFF O   1 
ATOM   11972 C CB  . LEU H 2 81  ? 67.229  77.612  9.489   1.000 44.270  ? 81  LEU FFF CB  1 
ATOM   11973 C CG  . LEU H 2 81  ? 68.616  77.361  10.072  1.000 43.442  ? 81  LEU FFF CG  1 
ATOM   11974 C CD1 . LEU H 2 81  ? 69.661  78.112  9.271   1.000 45.440  ? 81  LEU FFF CD1 1 
ATOM   11975 C CD2 . LEU H 2 81  ? 68.682  77.786  11.526  1.000 42.767  ? 81  LEU FFF CD2 1 
ATOM   11976 N N   . GLN H 2 82  ? 68.510  75.626  6.745   1.000 56.947  ? 82  GLN FFF N   1 
ATOM   11977 C CA  . GLN H 2 82  ? 69.016  74.309  6.243   1.000 56.993  ? 82  GLN FFF CA  1 
ATOM   11978 C C   . GLN H 2 82  ? 70.545  74.272  6.144   1.000 53.531  ? 82  GLN FFF C   1 
ATOM   11979 O O   . GLN H 2 82  ? 71.160  75.282  5.850   1.000 54.580  ? 82  GLN FFF O   1 
ATOM   11980 C CB  . GLN H 2 82  ? 68.396  73.909  4.895   1.000 63.750  ? 82  GLN FFF CB  1 
ATOM   11981 C CG  . GLN H 2 82  ? 68.903  74.681  3.681   1.000 67.781  ? 82  GLN FFF CG  1 
ATOM   11982 C CD  . GLN H 2 82  ? 68.010  74.489  2.474   1.000 75.776  ? 82  GLN FFF CD  1 
ATOM   11983 O OE1 . GLN H 2 82  ? 67.662  73.371  2.104   1.000 77.196  ? 82  GLN FFF OE1 1 
ATOM   11984 N NE2 . GLN H 2 82  ? 67.627  75.583  1.832   1.000 76.996  ? 82  GLN FFF NE2 1 
ATOM   11985 N N   . TRP H 2 83  ? 71.108  73.094  6.398   1.000 56.560  ? 83  TRP FFF N   1 
ATOM   11986 C CA  . TRP H 2 83  ? 72.532  72.725  6.197   1.000 54.204  ? 83  TRP FFF CA  1 
ATOM   11987 C C   . TRP H 2 83  ? 72.619  71.721  5.035   1.000 60.836  ? 83  TRP FFF C   1 
ATOM   11988 O O   . TRP H 2 83  ? 71.704  70.872  4.895   1.000 55.745  ? 83  TRP FFF O   1 
ATOM   11989 C CB  . TRP H 2 83  ? 73.103  72.118  7.481   1.000 49.319  ? 83  TRP FFF CB  1 
ATOM   11990 C CG  . TRP H 2 83  ? 73.152  73.021  8.675   1.000 46.849  ? 83  TRP FFF CG  1 
ATOM   11991 C CD1 . TRP H 2 83  ? 74.268  73.630  9.170   1.000 47.255  ? 83  TRP FFF CD1 1 
ATOM   11992 C CD2 . TRP H 2 83  ? 72.086  73.346  9.586   1.000 42.619  ? 83  TRP FFF CD2 1 
ATOM   11993 N NE1 . TRP H 2 83  ? 73.965  74.343  10.298  1.000 45.063  ? 83  TRP FFF NE1 1 
ATOM   11994 C CE2 . TRP H 2 83  ? 72.636  74.183  10.580  1.000 42.301  ? 83  TRP FFF CE2 1 
ATOM   11995 C CE3 . TRP H 2 83  ? 70.729  73.021  9.669   1.000 42.621  ? 83  TRP FFF CE3 1 
ATOM   11996 C CZ2 . TRP H 2 83  ? 71.876  74.710  11.618  1.000 41.008  ? 83  TRP FFF CZ2 1 
ATOM   11997 C CZ3 . TRP H 2 83  ? 69.971  73.554  10.690  1.000 42.032  ? 83  TRP FFF CZ3 1 
ATOM   11998 C CH2 . TRP H 2 83  ? 70.539  74.388  11.651  1.000 43.199  ? 83  TRP FFF CH2 1 
ATOM   11999 N N   . SER H 2 84  ? 73.669  71.808  4.217   1.000 67.468  ? 84  SER FFF N   1 
ATOM   12000 C CA  . SER H 2 84  ? 73.966  70.807  3.161   1.000 67.646  ? 84  SER FFF CA  1 
ATOM   12001 C C   . SER H 2 84  ? 74.602  69.589  3.830   1.000 65.791  ? 84  SER FFF C   1 
ATOM   12002 O O   . SER H 2 84  ? 74.160  68.471  3.528   1.000 60.918  ? 84  SER FFF O   1 
ATOM   12003 C CB  . SER H 2 84  ? 74.849  71.377  2.089   1.000 70.869  ? 84  SER FFF CB  1 
ATOM   12004 O OG  . SER H 2 84  ? 75.971  72.027  2.663   1.000 74.850  ? 84  SER FFF OG  1 
ATOM   12005 N N   . SER H 2 85  ? 75.551  69.820  4.749   1.000 62.936  ? 85  SER FFF N   1 
ATOM   12006 C CA  . SER H 2 85  ? 76.343  68.768  5.442   1.000 64.439  ? 85  SER FFF CA  1 
ATOM   12007 C C   . SER H 2 85  ? 76.653  69.142  6.906   1.000 63.610  ? 85  SER FFF C   1 
ATOM   12008 O O   . SER H 2 85  ? 77.544  69.999  7.149   1.000 58.808  ? 85  SER FFF O   1 
ATOM   12009 C CB  . SER H 2 85  ? 77.598  68.488  4.667   1.000 65.910  ? 85  SER FFF CB  1 
ATOM   12010 O OG  . SER H 2 85  ? 78.405  67.530  5.334   1.000 66.327  ? 85  SER FFF OG  1 
ATOM   12011 N N   . LEU H 2 86  ? 75.996  68.461  7.856   1.000 59.289  ? 86  LEU FFF N   1 
ATOM   12012 C CA  . LEU H 2 86  ? 76.059  68.785  9.311   1.000 53.347  ? 86  LEU FFF CA  1 
ATOM   12013 C C   . LEU H 2 86  ? 77.407  68.363  9.905   1.000 47.555  ? 86  LEU FFF C   1 
ATOM   12014 O O   . LEU H 2 86  ? 77.884  67.261  9.618   1.000 41.792  ? 86  LEU FFF O   1 
ATOM   12015 C CB  . LEU H 2 86  ? 74.906  68.096  10.043  1.000 53.098  ? 86  LEU FFF CB  1 
ATOM   12016 C CG  . LEU H 2 86  ? 73.572  68.835  9.997   1.000 53.722  ? 86  LEU FFF CG  1 
ATOM   12017 C CD1 . LEU H 2 86  ? 72.440  67.979  10.555  1.000 52.682  ? 86  LEU FFF CD1 1 
ATOM   12018 C CD2 . LEU H 2 86  ? 73.668  70.153  10.750  1.000 53.281  ? 86  LEU FFF CD2 1 
ATOM   12019 N N   . LYS H 2 87  ? 77.990  69.231  10.717  1.000 51.089  ? 87  LYS FFF N   1 
ATOM   12020 C CA  . LYS H 2 87  ? 79.161  68.915  11.576  1.000 55.767  ? 87  LYS FFF CA  1 
ATOM   12021 C C   . LYS H 2 87  ? 78.617  68.662  12.982  1.000 58.230  ? 87  LYS FFF C   1 
ATOM   12022 O O   . LYS H 2 87  ? 77.497  69.120  13.280  1.000 55.654  ? 87  LYS FFF O   1 
ATOM   12023 C CB  . LYS H 2 87  ? 80.208  70.043  11.565  1.000 57.740  ? 87  LYS FFF CB  1 
ATOM   12024 C CG  . LYS H 2 87  ? 80.603  70.560  10.187  1.000 65.279  ? 87  LYS FFF CG  1 
ATOM   12025 C CD  . LYS H 2 87  ? 81.181  71.973  10.133  1.000 65.367  ? 87  LYS FFF CD  1 
ATOM   12026 C CE  . LYS H 2 87  ? 81.383  72.455  8.705   1.000 71.657  ? 87  LYS FFF CE  1 
ATOM   12027 N NZ  . LYS H 2 87  ? 81.042  73.891  8.520   1.000 78.430  ? 87  LYS FFF NZ  1 
ATOM   12028 N N   . ALA H 2 88  ? 79.381  67.943  13.804  1.000 66.386  ? 88  ALA FFF N   1 
ATOM   12029 C CA  . ALA H 2 88  ? 79.045  67.632  15.213  1.000 67.026  ? 88  ALA FFF CA  1 
ATOM   12030 C C   . ALA H 2 88  ? 78.902  68.934  16.010  1.000 66.579  ? 88  ALA FFF C   1 
ATOM   12031 O O   . ALA H 2 88  ? 78.091  68.978  16.925  1.000 62.059  ? 88  ALA FFF O   1 
ATOM   12032 C CB  . ALA H 2 88  ? 80.110  66.737  15.802  1.000 68.982  ? 88  ALA FFF CB  1 
ATOM   12033 N N   . SER H 2 89  ? 79.685  69.959  15.660  1.000 69.728  ? 89  SER FFF N   1 
ATOM   12034 C CA  . SER H 2 89  ? 79.725  71.295  16.310  1.000 64.833  ? 89  SER FFF CA  1 
ATOM   12035 C C   . SER H 2 89  ? 78.400  72.046  16.109  1.000 58.395  ? 89  SER FFF C   1 
ATOM   12036 O O   . SER H 2 89  ? 78.169  73.000  16.856  1.000 50.904  ? 89  SER FFF O   1 
ATOM   12037 C CB  . SER H 2 89  ? 80.893  72.093  15.792  1.000 68.258  ? 89  SER FFF CB  1 
ATOM   12038 O OG  . SER H 2 89  ? 80.894  72.128  14.373  1.000 73.627  ? 89  SER FFF OG  1 
ATOM   12039 N N   . ASP H 2 90  ? 77.564  71.624  15.154  1.000 53.245  ? 90  ASP FFF N   1 
ATOM   12040 C CA  . ASP H 2 90  ? 76.249  72.251  14.835  1.000 52.289  ? 90  ASP FFF CA  1 
ATOM   12041 C C   . ASP H 2 90  ? 75.174  71.830  15.850  1.000 50.935  ? 90  ASP FFF C   1 
ATOM   12042 O O   . ASP H 2 90  ? 74.016  72.292  15.720  1.000 50.812  ? 90  ASP FFF O   1 
ATOM   12043 C CB  . ASP H 2 90  ? 75.801  71.903  13.414  1.000 53.534  ? 90  ASP FFF CB  1 
ATOM   12044 C CG  . ASP H 2 90  ? 76.456  72.758  12.343  1.000 54.960  ? 90  ASP FFF CG  1 
ATOM   12045 O OD1 . ASP H 2 90  ? 76.470  73.996  12.519  1.000 55.015  ? 90  ASP FFF OD1 1 
ATOM   12046 O OD2 . ASP H 2 90  ? 76.939  72.180  11.339  1.000 57.603  ? 90  ASP FFF OD2 1 
ATOM   12047 N N   . THR H 2 91  ? 75.531  70.975  16.815  1.000 49.201  ? 91  THR FFF N   1 
ATOM   12048 C CA  . THR H 2 91  ? 74.644  70.515  17.913  1.000 44.829  ? 91  THR FFF CA  1 
ATOM   12049 C C   . THR H 2 91  ? 74.275  71.708  18.777  1.000 47.492  ? 91  THR FFF C   1 
ATOM   12050 O O   . THR H 2 91  ? 75.168  72.222  19.469  1.000 48.013  ? 91  THR FFF O   1 
ATOM   12051 C CB  . THR H 2 91  ? 75.300  69.470  18.817  1.000 38.723  ? 91  THR FFF CB  1 
ATOM   12052 O OG1 . THR H 2 91  ? 75.546  68.327  17.997  1.000 35.748  ? 91  THR FFF OG1 1 
ATOM   12053 C CG2 . THR H 2 91  ? 74.420  69.110  19.995  1.000 40.102  ? 91  THR FFF CG2 1 
ATOM   12054 N N   . ALA H 2 92  ? 73.007  72.105  18.748  1.000 49.089  ? 92  ALA FFF N   1 
ATOM   12055 C CA  . ALA H 2 92  ? 72.501  73.234  19.553  1.000 51.386  ? 92  ALA FFF CA  1 
ATOM   12056 C C   . ALA H 2 92  ? 70.979  73.174  19.636  1.000 50.157  ? 92  ALA FFF C   1 
ATOM   12057 O O   . ALA H 2 92  ? 70.415  72.142  19.261  1.000 51.364  ? 92  ALA FFF O   1 
ATOM   12058 C CB  . ALA H 2 92  ? 72.976  74.525  18.936  1.000 53.475  ? 92  ALA FFF CB  1 
ATOM   12059 N N   . ILE H 2 93  ? 70.370  74.245  20.138  1.000 46.222  ? 93  ILE FFF N   1 
ATOM   12060 C CA  . ILE H 2 93  ? 68.925  74.533  19.961  1.000 44.449  ? 93  ILE FFF CA  1 
ATOM   12061 C C   . ILE H 2 93  ? 68.830  75.811  19.125  1.000 40.884  ? 93  ILE FFF C   1 
ATOM   12062 O O   . ILE H 2 93  ? 69.520  76.791  19.439  1.000 39.136  ? 93  ILE FFF O   1 
ATOM   12063 C CB  . ILE H 2 93  ? 68.186  74.621  21.308  1.000 46.260  ? 93  ILE FFF CB  1 
ATOM   12064 C CG1 . ILE H 2 93  ? 66.772  75.165  21.123  1.000 51.922  ? 93  ILE FFF CG1 1 
ATOM   12065 C CG2 . ILE H 2 93  ? 68.956  75.428  22.328  1.000 47.157  ? 93  ILE FFF CG2 1 
ATOM   12066 C CD1 . ILE H 2 93  ? 65.924  75.084  22.370  1.000 58.514  ? 93  ILE FFF CD1 1 
ATOM   12067 N N   . TYR H 2 94  ? 68.010  75.772  18.080  1.000 36.867  ? 94  TYR FFF N   1 
ATOM   12068 C CA  . TYR H 2 94  ? 67.817  76.852  17.090  1.000 33.232  ? 94  TYR FFF CA  1 
ATOM   12069 C C   . TYR H 2 94  ? 66.416  77.443  17.263  1.000 29.985  ? 94  TYR FFF C   1 
ATOM   12070 O O   . TYR H 2 94  ? 65.424  76.772  16.970  1.000 27.699  ? 94  TYR FFF O   1 
ATOM   12071 C CB  . TYR H 2 94  ? 68.060  76.285  15.690  1.000 35.158  ? 94  TYR FFF CB  1 
ATOM   12072 C CG  . TYR H 2 94  ? 69.477  75.838  15.434  1.000 35.815  ? 94  TYR FFF CG  1 
ATOM   12073 C CD1 . TYR H 2 94  ? 70.415  76.693  14.885  1.000 37.551  ? 94  TYR FFF CD1 1 
ATOM   12074 C CD2 . TYR H 2 94  ? 69.892  74.566  15.763  1.000 37.263  ? 94  TYR FFF CD2 1 
ATOM   12075 C CE1 . TYR H 2 94  ? 71.720  76.293  14.659  1.000 37.580  ? 94  TYR FFF CE1 1 
ATOM   12076 C CE2 . TYR H 2 94  ? 71.194  74.148  15.538  1.000 38.406  ? 94  TYR FFF CE2 1 
ATOM   12077 C CZ  . TYR H 2 94  ? 72.120  75.011  14.983  1.000 37.340  ? 94  TYR FFF CZ  1 
ATOM   12078 O OH  . TYR H 2 94  ? 73.416  74.625  14.761  1.000 36.360  ? 94  TYR FFF OH  1 
ATOM   12079 N N   . TYR H 2 95  ? 66.357  78.679  17.743  1.000 30.565  ? 95  TYR FFF N   1 
ATOM   12080 C CA  . TYR H 2 95  ? 65.131  79.513  17.812  1.000 32.002  ? 95  TYR FFF CA  1 
ATOM   12081 C C   . TYR H 2 95  ? 64.935  80.292  16.503  1.000 31.407  ? 95  TYR FFF C   1 
ATOM   12082 O O   . TYR H 2 95  ? 65.904  80.757  15.922  1.000 28.508  ? 95  TYR FFF O   1 
ATOM   12083 C CB  . TYR H 2 95  ? 65.231  80.479  18.993  1.000 31.990  ? 95  TYR FFF CB  1 
ATOM   12084 C CG  . TYR H 2 95  ? 65.383  79.802  20.329  1.000 31.833  ? 95  TYR FFF CG  1 
ATOM   12085 C CD1 . TYR H 2 95  ? 64.290  79.281  20.996  1.000 33.679  ? 95  TYR FFF CD1 1 
ATOM   12086 C CD2 . TYR H 2 95  ? 66.618  79.693  20.934  1.000 34.476  ? 95  TYR FFF CD2 1 
ATOM   12087 C CE1 . TYR H 2 95  ? 64.416  78.671  22.234  1.000 36.172  ? 95  TYR FFF CE1 1 
ATOM   12088 C CE2 . TYR H 2 95  ? 66.766  79.093  22.176  1.000 36.433  ? 95  TYR FFF CE2 1 
ATOM   12089 C CZ  . TYR H 2 95  ? 65.660  78.580  22.831  1.000 36.371  ? 95  TYR FFF CZ  1 
ATOM   12090 O OH  . TYR H 2 95  ? 65.791  77.960  24.038  1.000 36.946  ? 95  TYR FFF OH  1 
ATOM   12091 N N   . CYS H 2 96  ? 63.699  80.410  16.040  1.000 34.595  ? 96  CYS FFF N   1 
ATOM   12092 C CA  . CYS H 2 96  ? 63.287  81.470  15.097  1.000 38.738  ? 96  CYS FFF CA  1 
ATOM   12093 C C   . CYS H 2 96  ? 62.556  82.515  15.939  1.000 40.942  ? 96  CYS FFF C   1 
ATOM   12094 O O   . CYS H 2 96  ? 61.803  82.133  16.836  1.000 39.219  ? 96  CYS FFF O   1 
ATOM   12095 C CB  . CYS H 2 96  ? 62.430  80.939  13.953  1.000 40.129  ? 96  CYS FFF CB  1 
ATOM   12096 S SG  . CYS H 2 96  ? 60.868  80.244  14.526  1.000 44.318  ? 96  CYS FFF SG  1 
ATOM   12097 N N   . ALA H 2 97  ? 62.837  83.790  15.696  1.000 47.178  ? 97  ALA FFF N   1 
ATOM   12098 C CA  . ALA H 2 97  ? 62.157  84.949  16.307  1.000 51.587  ? 97  ALA FFF CA  1 
ATOM   12099 C C   . ALA H 2 97  ? 61.557  85.816  15.198  1.000 51.550  ? 97  ALA FFF C   1 
ATOM   12100 O O   . ALA H 2 97  ? 62.008  85.706  14.043  1.000 53.527  ? 97  ALA FFF O   1 
ATOM   12101 C CB  . ALA H 2 97  ? 63.147  85.728  17.123  1.000 59.881  ? 97  ALA FFF CB  1 
ATOM   12102 N N   . GLY H 2 98  ? 60.589  86.656  15.557  1.000 53.409  ? 98  GLY FFF N   1 
ATOM   12103 C CA  . GLY H 2 98  ? 59.847  87.503  14.612  1.000 57.096  ? 98  GLY FFF CA  1 
ATOM   12104 C C   . GLY H 2 98  ? 59.821  88.946  15.064  1.000 60.454  ? 98  GLY FFF C   1 
ATOM   12105 O O   . GLY H 2 98  ? 59.383  89.195  16.206  1.000 53.982  ? 98  GLY FFF O   1 
ATOM   12106 N N   . GLY H 2 99  ? 60.297  89.847  14.198  1.000 71.013  ? 99  GLY FFF N   1 
ATOM   12107 C CA  . GLY H 2 99  ? 60.029  91.295  14.258  1.000 76.036  ? 99  GLY FFF CA  1 
ATOM   12108 C C   . GLY H 2 99  ? 59.076  91.737  13.153  1.000 78.291  ? 99  GLY FFF C   1 
ATOM   12109 O O   . GLY H 2 99  ? 59.246  91.279  11.987  1.000 68.832  ? 99  GLY FFF O   1 
ATOM   12110 N N   . SER H 2 100 ? 58.116  92.608  13.488  1.000 83.651  ? 100 SER FFF N   1 
ATOM   12111 C CA  . SER H 2 100 ? 57.123  93.161  12.526  1.000 83.705  ? 100 SER FFF CA  1 
ATOM   12112 C C   . SER H 2 100 ? 57.800  94.159  11.568  1.000 76.242  ? 100 SER FFF C   1 
ATOM   12113 O O   . SER H 2 100 ? 57.145  94.618  10.632  1.000 91.157  ? 100 SER FFF O   1 
ATOM   12114 C CB  . SER H 2 100 ? 55.938  93.747  13.255  1.000 79.800  ? 100 SER FFF CB  1 
ATOM   12115 O OG  . SER H 2 100 ? 56.360  94.387  14.438  1.000 76.838  ? 100 SER FFF OG  1 
ATOM   12116 N N   . GLY H 2 101 ? 59.086  94.440  11.748  1.000 59.684  ? 101 GLY FFF N   1 
ATOM   12117 C CA  . GLY H 2 101 ? 59.884  95.202  10.779  1.000 57.536  ? 101 GLY FFF CA  1 
ATOM   12118 C C   . GLY H 2 101 ? 61.332  94.748  10.742  1.000 54.820  ? 101 GLY FFF C   1 
ATOM   12119 O O   . GLY H 2 101 ? 61.747  93.911  11.539  1.000 55.741  ? 101 GLY FFF O   1 
ATOM   12120 N N   . ILE H 2 102 ? 62.070  95.262  9.781   1.000 52.897  ? 102 ILE FFF N   1 
ATOM   12121 C CA  . ILE H 2 102 ? 63.526  95.052  9.675   1.000 54.644  ? 102 ILE FFF CA  1 
ATOM   12122 C C   . ILE H 2 102 ? 63.969  96.236  10.490  1.000 54.271  ? 102 ILE FFF C   1 
ATOM   12123 O O   . ILE H 2 102 ? 63.470  97.293  10.157  1.000 62.609  ? 102 ILE FFF O   1 
ATOM   12124 C CB  . ILE H 2 102 ? 64.152  95.282  8.301   1.000 59.462  ? 102 ILE FFF CB  1 
ATOM   12125 C CG1 . ILE H 2 102 ? 65.638  94.961  8.292   1.000 57.733  ? 102 ILE FFF CG1 1 
ATOM   12126 C CG2 . ILE H 2 102 ? 63.978  96.719  7.869   1.000 71.542  ? 102 ILE FFF CG2 1 
ATOM   12127 C CD1 . ILE H 2 102 ? 65.962  93.547  8.599   1.000 61.053  ? 102 ILE FFF CD1 1 
ATOM   12128 N N   . SER H 2 103 ? 64.839  96.063  11.456  1.000 57.767  ? 103 SER FFF N   1 
ATOM   12129 C CA  . SER H 2 103 ? 65.323  97.069  12.457  1.000 57.244  ? 103 SER FFF CA  1 
ATOM   12130 C C   . SER H 2 103 ? 64.204  97.331  13.469  1.000 60.487  ? 103 SER FFF C   1 
ATOM   12131 O O   . SER H 2 103 ? 63.810  98.494  13.806  1.000 51.174  ? 103 SER FFF O   1 
ATOM   12132 C CB  . SER H 2 103 ? 65.916  98.304  11.873  1.000 56.810  ? 103 SER FFF CB  1 
ATOM   12133 O OG  . SER H 2 103 ? 67.026  98.704  12.666  1.000 56.931  ? 103 SER FFF OG  1 
ATOM   12134 N N   . THR H 2 104 ? 63.787  96.186  13.988  1.000 71.722  ? 104 THR FFF N   1 
ATOM   12135 C CA  . THR H 2 104 ? 62.682  95.977  14.929  1.000 69.398  ? 104 THR FFF CA  1 
ATOM   12136 C C   . THR H 2 104 ? 63.136  94.906  15.914  1.000 68.919  ? 104 THR FFF C   1 
ATOM   12137 O O   . THR H 2 104 ? 63.856  93.959  15.550  1.000 67.885  ? 104 THR FFF O   1 
ATOM   12138 C CB  . THR H 2 104 ? 61.420  95.599  14.152  1.000 70.884  ? 104 THR FFF CB  1 
ATOM   12139 O OG1 . THR H 2 104 ? 61.026  96.788  13.471  1.000 68.102  ? 104 THR FFF OG1 1 
ATOM   12140 C CG2 . THR H 2 104 ? 60.302  95.052  15.015  1.000 73.351  ? 104 THR FFF CG2 1 
ATOM   12141 N N   . PRO H 2 105 ? 62.709  95.027  17.193  1.000 70.799  ? 105 PRO FFF N   1 
ATOM   12142 C CA  . PRO H 2 105 ? 63.011  94.008  18.191  1.000 67.077  ? 105 PRO FFF CA  1 
ATOM   12143 C C   . PRO H 2 105 ? 62.274  92.722  17.807  1.000 60.471  ? 105 PRO FFF C   1 
ATOM   12144 O O   . PRO H 2 105 ? 61.221  92.808  17.177  1.000 58.479  ? 105 PRO FFF O   1 
ATOM   12145 C CB  . PRO H 2 105 ? 62.461  94.612  19.492  1.000 67.862  ? 105 PRO FFF CB  1 
ATOM   12146 C CG  . PRO H 2 105 ? 61.318  95.494  19.018  1.000 73.987  ? 105 PRO FFF CG  1 
ATOM   12147 C CD  . PRO H 2 105 ? 61.856  96.101  17.739  1.000 75.821  ? 105 PRO FFF CD  1 
ATOM   12148 N N   . MET H 2 106 ? 62.805  91.578  18.232  1.000 55.311  ? 106 MET FFF N   1 
ATOM   12149 C CA  . MET H 2 106 ? 62.135  90.266  18.077  1.000 54.105  ? 106 MET FFF CA  1 
ATOM   12150 C C   . MET H 2 106 ? 61.055  90.093  19.162  1.000 54.267  ? 106 MET FFF C   1 
ATOM   12151 O O   . MET H 2 106 ? 61.411  89.645  20.275  1.000 44.538  ? 106 MET FFF O   1 
ATOM   12152 C CB  . MET H 2 106 ? 63.200  89.179  18.133  1.000 54.009  ? 106 MET FFF CB  1 
ATOM   12153 C CG  . MET H 2 106 ? 64.150  89.293  16.963  1.000 59.257  ? 106 MET FFF CG  1 
ATOM   12154 S SD  . MET H 2 106 ? 65.791  88.560  17.245  1.000 60.863  ? 106 MET FFF SD  1 
ATOM   12155 C CE  . MET H 2 106 ? 66.183  88.170  15.542  1.000 62.353  ? 106 MET FFF CE  1 
ATOM   12156 N N   . ASP H 2 107 ? 59.798  90.486  18.834  1.000 60.760  ? 107 ASP FFF N   1 
ATOM   12157 C CA  . ASP H 2 107 ? 58.586  90.509  19.711  1.000 60.440  ? 107 ASP FFF CA  1 
ATOM   12158 C C   . ASP H 2 107 ? 58.244  89.075  20.103  1.000 52.422  ? 107 ASP FFF C   1 
ATOM   12159 O O   . ASP H 2 107 ? 58.021  88.841  21.301  1.000 43.937  ? 107 ASP FFF O   1 
ATOM   12160 C CB  . ASP H 2 107 ? 57.289  91.010  19.044  1.000 69.793  ? 107 ASP FFF CB  1 
ATOM   12161 C CG  . ASP H 2 107 ? 57.337  92.294  18.231  1.000 86.806  ? 107 ASP FFF CG  1 
ATOM   12162 O OD1 . ASP H 2 107 ? 57.881  93.307  18.733  1.000 107.661 ? 107 ASP FFF OD1 1 
ATOM   12163 O OD2 . ASP H 2 107 ? 56.802  92.276  17.101  1.000 91.544  ? 107 ASP FFF OD2 1 
ATOM   12164 N N   . VAL H 2 108 ? 58.213  88.200  19.086  1.000 47.892  ? 108 VAL FFF N   1 
ATOM   12165 C CA  . VAL H 2 108 ? 57.633  86.827  19.080  1.000 45.144  ? 108 VAL FFF CA  1 
ATOM   12166 C C   . VAL H 2 108 ? 58.744  85.805  18.823  1.000 43.852  ? 108 VAL FFF C   1 
ATOM   12167 O O   . VAL H 2 108 ? 59.558  86.039  17.918  1.000 42.165  ? 108 VAL FFF O   1 
ATOM   12168 C CB  . VAL H 2 108 ? 56.541  86.730  18.000  1.000 45.355  ? 108 VAL FFF CB  1 
ATOM   12169 C CG1 . VAL H 2 108 ? 56.078  85.296  17.775  1.000 48.682  ? 108 VAL FFF CG1 1 
ATOM   12170 C CG2 . VAL H 2 108 ? 55.356  87.626  18.335  1.000 48.088  ? 108 VAL FFF CG2 1 
ATOM   12171 N N   . TRP H 2 109 ? 58.747  84.698  19.574  1.000 42.062  ? 109 TRP FFF N   1 
ATOM   12172 C CA  . TRP H 2 109 ? 59.747  83.595  19.496  1.000 38.459  ? 109 TRP FFF CA  1 
ATOM   12173 C C   . TRP H 2 109 ? 59.069  82.232  19.298  1.000 38.489  ? 109 TRP FFF C   1 
ATOM   12174 O O   . TRP H 2 109 ? 57.956  82.009  19.839  1.000 37.518  ? 109 TRP FFF O   1 
ATOM   12175 C CB  . TRP H 2 109 ? 60.595  83.573  20.767  1.000 36.576  ? 109 TRP FFF CB  1 
ATOM   12176 C CG  . TRP H 2 109 ? 61.545  84.720  20.890  1.000 35.577  ? 109 TRP FFF CG  1 
ATOM   12177 C CD1 . TRP H 2 109 ? 61.267  85.979  21.334  1.000 35.027  ? 109 TRP FFF CD1 1 
ATOM   12178 C CD2 . TRP H 2 109 ? 62.953  84.695  20.600  1.000 32.602  ? 109 TRP FFF CD2 1 
ATOM   12179 N NE1 . TRP H 2 109 ? 62.404  86.742  21.308  1.000 36.368  ? 109 TRP FFF NE1 1 
ATOM   12180 C CE2 . TRP H 2 109 ? 63.455  85.978  20.876  1.000 32.269  ? 109 TRP FFF CE2 1 
ATOM   12181 C CE3 . TRP H 2 109 ? 63.832  83.718  20.136  1.000 31.905  ? 109 TRP FFF CE3 1 
ATOM   12182 C CZ2 . TRP H 2 109 ? 64.793  86.305  20.699  1.000 31.354  ? 109 TRP FFF CZ2 1 
ATOM   12183 C CZ3 . TRP H 2 109 ? 65.158  84.034  19.979  1.000 31.631  ? 109 TRP FFF CZ3 1 
ATOM   12184 C CH2 . TRP H 2 109 ? 65.627  85.314  20.245  1.000 31.360  ? 109 TRP FFF CH2 1 
ATOM   12185 N N   . GLY H 2 110 ? 59.738  81.336  18.568  1.000 41.205  ? 110 GLY FFF N   1 
ATOM   12186 C CA  . GLY H 2 110 ? 59.390  79.902  18.483  1.000 43.255  ? 110 GLY FFF CA  1 
ATOM   12187 C C   . GLY H 2 110 ? 59.768  79.186  19.763  1.000 42.920  ? 110 GLY FFF C   1 
ATOM   12188 O O   . GLY H 2 110 ? 60.464  79.803  20.581  1.000 46.006  ? 110 GLY FFF O   1 
ATOM   12189 N N   . GLN H 2 111 ? 59.322  77.942  19.944  1.000 43.934  ? 111 GLN FFF N   1 
ATOM   12190 C CA  . GLN H 2 111 ? 59.605  77.133  21.164  1.000 43.102  ? 111 GLN FFF CA  1 
ATOM   12191 C C   . GLN H 2 111 ? 61.053  76.612  21.110  1.000 41.896  ? 111 GLN FFF C   1 
ATOM   12192 O O   . GLN H 2 111 ? 61.584  76.197  22.141  1.000 43.155  ? 111 GLN FFF O   1 
ATOM   12193 C CB  . GLN H 2 111 ? 58.595  75.991  21.306  1.000 42.412  ? 111 GLN FFF CB  1 
ATOM   12194 C CG  . GLN H 2 111 ? 58.748  74.872  20.275  1.000 42.766  ? 111 GLN FFF CG  1 
ATOM   12195 C CD  . GLN H 2 111 ? 57.960  75.081  19.003  1.000 44.108  ? 111 GLN FFF CD  1 
ATOM   12196 O OE1 . GLN H 2 111 ? 57.109  75.958  18.904  1.000 58.969  ? 111 GLN FFF OE1 1 
ATOM   12197 N NE2 . GLN H 2 111 ? 58.223  74.266  18.003  1.000 43.906  ? 111 GLN FFF NE2 1 
ATOM   12198 N N   . GLY H 2 112 ? 61.671  76.628  19.936  1.000 42.079  ? 112 GLY FFF N   1 
ATOM   12199 C CA  . GLY H 2 112 ? 63.040  76.134  19.721  1.000 39.953  ? 112 GLY FFF CA  1 
ATOM   12200 C C   . GLY H 2 112 ? 62.997  74.767  19.096  1.000 39.464  ? 112 GLY FFF C   1 
ATOM   12201 O O   . GLY H 2 112 ? 62.056  74.034  19.405  1.000 44.126  ? 112 GLY FFF O   1 
ATOM   12202 N N   . THR H 2 113 ? 63.935  74.467  18.198  1.000 38.639  ? 113 THR FFF N   1 
ATOM   12203 C CA  . THR H 2 113 ? 64.147  73.111  17.639  1.000 38.304  ? 113 THR FFF CA  1 
ATOM   12204 C C   . THR H 2 113 ? 65.498  72.622  18.142  1.000 39.751  ? 113 THR FFF C   1 
ATOM   12205 O O   . THR H 2 113 ? 66.486  73.232  17.761  1.000 37.816  ? 113 THR FFF O   1 
ATOM   12206 C CB  . THR H 2 113 ? 64.147  73.102  16.113  1.000 36.582  ? 113 THR FFF CB  1 
ATOM   12207 O OG1 . THR H 2 113 ? 62.888  73.564  15.634  1.000 38.309  ? 113 THR FFF OG1 1 
ATOM   12208 C CG2 . THR H 2 113 ? 64.412  71.720  15.568  1.000 38.080  ? 113 THR FFF CG2 1 
ATOM   12209 N N   . THR H 2 114 ? 65.528  71.571  18.963  1.000 45.556  ? 114 THR FFF N   1 
ATOM   12210 C CA  . THR H 2 114 ? 66.790  70.942  19.440  1.000 45.087  ? 114 THR FFF CA  1 
ATOM   12211 C C   . THR H 2 114 ? 67.374  70.039  18.339  1.000 43.939  ? 114 THR FFF C   1 
ATOM   12212 O O   . THR H 2 114 ? 66.703  69.102  17.904  1.000 44.114  ? 114 THR FFF O   1 
ATOM   12213 C CB  . THR H 2 114 ? 66.570  70.208  20.765  1.000 43.896  ? 114 THR FFF CB  1 
ATOM   12214 O OG1 . THR H 2 114 ? 66.157  71.196  21.710  1.000 39.700  ? 114 THR FFF OG1 1 
ATOM   12215 C CG2 . THR H 2 114 ? 67.810  69.483  21.244  1.000 43.396  ? 114 THR FFF CG2 1 
ATOM   12216 N N   . VAL H 2 115 ? 68.586  70.345  17.895  1.000 44.846  ? 115 VAL FFF N   1 
ATOM   12217 C CA  . VAL H 2 115 ? 69.332  69.558  16.874  1.000 45.505  ? 115 VAL FFF CA  1 
ATOM   12218 C C   . VAL H 2 115 ? 70.536  68.920  17.564  1.000 47.523  ? 115 VAL FFF C   1 
ATOM   12219 O O   . VAL H 2 115 ? 71.343  69.654  18.162  1.000 44.984  ? 115 VAL FFF O   1 
ATOM   12220 C CB  . VAL H 2 115 ? 69.766  70.435  15.689  1.000 44.018  ? 115 VAL FFF CB  1 
ATOM   12221 C CG1 . VAL H 2 115 ? 70.597  69.659  14.682  1.000 43.027  ? 115 VAL FFF CG1 1 
ATOM   12222 C CG2 . VAL H 2 115 ? 68.567  71.074  15.008  1.000 44.954  ? 115 VAL FFF CG2 1 
ATOM   12223 N N   . THR H 2 116 ? 70.625  67.594  17.506  1.000 47.254  ? 116 THR FFF N   1 
ATOM   12224 C CA  . THR H 2 116 ? 71.765  66.826  18.050  1.000 43.651  ? 116 THR FFF CA  1 
ATOM   12225 C C   . THR H 2 116 ? 72.485  66.170  16.881  1.000 41.874  ? 116 THR FFF C   1 
ATOM   12226 O O   . THR H 2 116 ? 71.845  65.370  16.202  1.000 42.026  ? 116 THR FFF O   1 
ATOM   12227 C CB  . THR H 2 116 ? 71.277  65.771  19.037  1.000 46.195  ? 116 THR FFF CB  1 
ATOM   12228 O OG1 . THR H 2 116 ? 70.267  66.342  19.877  1.000 54.001  ? 116 THR FFF OG1 1 
ATOM   12229 C CG2 . THR H 2 116 ? 72.421  65.221  19.851  1.000 46.323  ? 116 THR FFF CG2 1 
ATOM   12230 N N   . VAL H 2 117 ? 73.733  66.551  16.623  1.000 44.641  ? 117 VAL FFF N   1 
ATOM   12231 C CA  . VAL H 2 117 ? 74.583  65.922  15.569  1.000 48.660  ? 117 VAL FFF CA  1 
ATOM   12232 C C   . VAL H 2 117 ? 75.670  65.114  16.286  1.000 49.419  ? 117 VAL FFF C   1 
ATOM   12233 O O   . VAL H 2 117 ? 76.439  65.708  17.073  1.000 46.925  ? 117 VAL FFF O   1 
ATOM   12234 C CB  . VAL H 2 117 ? 75.163  66.961  14.588  1.000 54.299  ? 117 VAL FFF CB  1 
ATOM   12235 C CG1 . VAL H 2 117 ? 75.939  66.292  13.450  1.000 55.439  ? 117 VAL FFF CG1 1 
ATOM   12236 C CG2 . VAL H 2 117 ? 74.068  67.873  14.029  1.000 55.554  ? 117 VAL FFF CG2 1 
ATOM   12237 N N   . SER H 2 118 ? 75.684  63.797  16.069  1.000 50.218  ? 118 SER FFF N   1 
ATOM   12238 C CA  . SER H 2 118 ? 76.564  62.825  16.774  1.000 52.047  ? 118 SER FFF CA  1 
ATOM   12239 C C   . SER H 2 118 ? 76.585  61.527  15.968  1.000 55.744  ? 118 SER FFF C   1 
ATOM   12240 O O   . SER H 2 118 ? 75.521  61.116  15.443  1.000 54.167  ? 118 SER FFF O   1 
ATOM   12241 C CB  . SER H 2 118 ? 76.125  62.575  18.217  1.000 51.687  ? 118 SER FFF CB  1 
ATOM   12242 O OG  . SER H 2 118 ? 76.876  61.536  18.843  1.000 43.936  ? 118 SER FFF OG  1 
ATOM   12243 N N   . SER H 2 119 ? 77.772  60.931  15.855  1.000 57.640  ? 119 SER FFF N   1 
ATOM   12244 C CA  . SER H 2 119 ? 77.990  59.629  15.182  1.000 54.691  ? 119 SER FFF CA  1 
ATOM   12245 C C   . SER H 2 119 ? 77.410  58.494  16.045  1.000 50.415  ? 119 SER FFF C   1 
ATOM   12246 O O   . SER H 2 119 ? 77.346  57.367  15.541  1.000 52.284  ? 119 SER FFF O   1 
ATOM   12247 C CB  . SER H 2 119 ? 79.446  59.431  14.888  1.000 54.665  ? 119 SER FFF CB  1 
ATOM   12248 O OG  . SER H 2 119 ? 80.188  59.382  16.092  1.000 56.113  ? 119 SER FFF OG  1 
ATOM   12249 N N   . ALA H 2 120 ? 76.978  58.782  17.278  1.000 46.235  ? 120 ALA FFF N   1 
ATOM   12250 C CA  . ALA H 2 120 ? 76.317  57.811  18.184  1.000 43.907  ? 120 ALA FFF CA  1 
ATOM   12251 C C   . ALA H 2 120 ? 75.001  57.325  17.579  1.000 43.773  ? 120 ALA FFF C   1 
ATOM   12252 O O   . ALA H 2 120 ? 74.303  58.150  16.943  1.000 40.441  ? 120 ALA FFF O   1 
ATOM   12253 C CB  . ALA H 2 120 ? 76.066  58.424  19.528  1.000 44.452  ? 120 ALA FFF CB  1 
ATOM   12254 N N   . SER H 2 121 ? 74.695  56.039  17.779  1.000 45.717  ? 121 SER FFF N   1 
ATOM   12255 C CA  . SER H 2 121 ? 73.428  55.373  17.367  1.000 46.237  ? 121 SER FFF CA  1 
ATOM   12256 C C   . SER H 2 121 ? 72.453  55.322  18.540  1.000 44.473  ? 121 SER FFF C   1 
ATOM   12257 O O   . SER H 2 121 ? 72.903  55.287  19.696  1.000 40.980  ? 121 SER FFF O   1 
ATOM   12258 C CB  . SER H 2 121 ? 73.679  53.994  16.843  1.000 48.737  ? 121 SER FFF CB  1 
ATOM   12259 O OG  . SER H 2 121 ? 74.680  54.028  15.840  1.000 51.525  ? 121 SER FFF OG  1 
ATOM   12260 N N   . THR H 2 122 ? 71.157  55.293  18.237  1.000 47.583  ? 122 THR FFF N   1 
ATOM   12261 C CA  . THR H 2 122 ? 70.074  55.215  19.251  1.000 48.423  ? 122 THR FFF CA  1 
ATOM   12262 C C   . THR H 2 122 ? 70.400  54.071  20.203  1.000 45.789  ? 122 THR FFF C   1 
ATOM   12263 O O   . THR H 2 122 ? 70.603  52.946  19.720  1.000 44.494  ? 122 THR FFF O   1 
ATOM   12264 C CB  . THR H 2 122 ? 68.693  54.972  18.630  1.000 49.883  ? 122 THR FFF CB  1 
ATOM   12265 O OG1 . THR H 2 122 ? 68.478  56.058  17.735  1.000 54.866  ? 122 THR FFF OG1 1 
ATOM   12266 C CG2 . THR H 2 122 ? 67.572  54.887  19.651  1.000 51.238  ? 122 THR FFF CG2 1 
ATOM   12267 N N   . LYS H 2 123 ? 70.454  54.357  21.496  1.000 44.666  ? 123 LYS FFF N   1 
ATOM   12268 C CA  . LYS H 2 123 ? 70.625  53.318  22.533  1.000 45.898  ? 123 LYS FFF CA  1 
ATOM   12269 C C   . LYS H 2 123 ? 69.791  53.655  23.771  1.000 41.339  ? 123 LYS FFF C   1 
ATOM   12270 O O   . LYS H 2 123 ? 69.931  54.760  24.297  1.000 38.443  ? 123 LYS FFF O   1 
ATOM   12271 C CB  . LYS H 2 123 ? 72.095  53.141  22.928  1.000 49.091  ? 123 LYS FFF CB  1 
ATOM   12272 C CG  . LYS H 2 123 ? 72.270  51.909  23.791  1.000 52.416  ? 123 LYS FFF CG  1 
ATOM   12273 C CD  . LYS H 2 123 ? 73.510  51.798  24.596  1.000 55.304  ? 123 LYS FFF CD  1 
ATOM   12274 C CE  . LYS H 2 123 ? 73.251  50.778  25.683  1.000 64.995  ? 123 LYS FFF CE  1 
ATOM   12275 N NZ  . LYS H 2 123 ? 74.479  50.463  26.437  1.000 80.602  ? 123 LYS FFF NZ  1 
ATOM   12276 N N   . GLY H 2 124 ? 69.011  52.688  24.250  1.000 40.473  ? 124 GLY FFF N   1 
ATOM   12277 C CA  . GLY H 2 124 ? 68.180  52.804  25.463  1.000 37.938  ? 124 GLY FFF CA  1 
ATOM   12278 C C   . GLY H 2 124 ? 69.035  52.788  26.720  1.000 36.252  ? 124 GLY FFF C   1 
ATOM   12279 O O   . GLY H 2 124 ? 70.079  52.145  26.772  1.000 39.128  ? 124 GLY FFF O   1 
ATOM   12280 N N   . PRO H 2 125 ? 68.602  53.482  27.785  1.000 35.924  ? 125 PRO FFF N   1 
ATOM   12281 C CA  . PRO H 2 125 ? 69.387  53.577  29.010  1.000 36.683  ? 125 PRO FFF CA  1 
ATOM   12282 C C   . PRO H 2 125 ? 69.367  52.277  29.810  1.000 36.189  ? 125 PRO FFF C   1 
ATOM   12283 O O   . PRO H 2 125 ? 68.442  51.521  29.687  1.000 39.255  ? 125 PRO FFF O   1 
ATOM   12284 C CB  . PRO H 2 125 ? 68.652  54.638  29.842  1.000 39.055  ? 125 PRO FFF CB  1 
ATOM   12285 C CG  . PRO H 2 125 ? 67.205  54.548  29.352  1.000 40.073  ? 125 PRO FFF CG  1 
ATOM   12286 C CD  . PRO H 2 125 ? 67.312  54.175  27.881  1.000 38.071  ? 125 PRO FFF CD  1 
ATOM   12287 N N   . SER H 2 126 ? 70.360  52.104  30.661  1.000 37.562  ? 126 SER FFF N   1 
ATOM   12288 C CA  . SER H 2 126 ? 70.367  51.080  31.735  1.000 38.454  ? 126 SER FFF CA  1 
ATOM   12289 C C   . SER H 2 126 ? 70.071  51.794  33.059  1.000 35.748  ? 126 SER FFF C   1 
ATOM   12290 O O   . SER H 2 126 ? 70.743  52.827  33.305  1.000 35.607  ? 126 SER FFF O   1 
ATOM   12291 C CB  . SER H 2 126 ? 71.689  50.343  31.774  1.000 40.351  ? 126 SER FFF CB  1 
ATOM   12292 O OG  . SER H 2 126 ? 72.146  50.019  30.472  1.000 43.846  ? 126 SER FFF OG  1 
ATOM   12293 N N   . VAL H 2 127 ? 69.112  51.302  33.848  1.000 30.728  ? 127 VAL FFF N   1 
ATOM   12294 C CA  . VAL H 2 127 ? 68.750  51.976  35.121  1.000 31.412  ? 127 VAL FFF CA  1 
ATOM   12295 C C   . VAL H 2 127 ? 69.252  51.154  36.296  1.000 31.567  ? 127 VAL FFF C   1 
ATOM   12296 O O   . VAL H 2 127 ? 68.902  49.988  36.358  1.000 32.989  ? 127 VAL FFF O   1 
ATOM   12297 C CB  . VAL H 2 127 ? 67.242  52.199  35.224  1.000 32.797  ? 127 VAL FFF CB  1 
ATOM   12298 C CG1 . VAL H 2 127 ? 66.880  53.022  36.461  1.000 34.153  ? 127 VAL FFF CG1 1 
ATOM   12299 C CG2 . VAL H 2 127 ? 66.712  52.851  33.960  1.000 33.875  ? 127 VAL FFF CG2 1 
ATOM   12300 N N   . PHE H 2 128 ? 70.022  51.776  37.194  1.000 32.714  ? 128 PHE FFF N   1 
ATOM   12301 C CA  . PHE H 2 128 ? 70.640  51.134  38.380  1.000 31.537  ? 128 PHE FFF CA  1 
ATOM   12302 C C   . PHE H 2 128 ? 70.246  51.897  39.634  1.000 33.100  ? 128 PHE FFF C   1 
ATOM   12303 O O   . PHE H 2 128 ? 70.180  53.123  39.604  1.000 34.098  ? 128 PHE FFF O   1 
ATOM   12304 C CB  . PHE H 2 128 ? 72.159  51.167  38.256  1.000 31.560  ? 128 PHE FFF CB  1 
ATOM   12305 C CG  . PHE H 2 128 ? 72.716  50.548  37.003  1.000 29.279  ? 128 PHE FFF CG  1 
ATOM   12306 C CD1 . PHE H 2 128 ? 72.417  49.245  36.644  1.000 27.529  ? 128 PHE FFF CD1 1 
ATOM   12307 C CD2 . PHE H 2 128 ? 73.585  51.271  36.211  1.000 28.674  ? 128 PHE FFF CD2 1 
ATOM   12308 C CE1 . PHE H 2 128 ? 72.946  48.698  35.491  1.000 27.523  ? 128 PHE FFF CE1 1 
ATOM   12309 C CE2 . PHE H 2 128 ? 74.129  50.715  35.066  1.000 27.841  ? 128 PHE FFF CE2 1 
ATOM   12310 C CZ  . PHE H 2 128 ? 73.814  49.426  34.714  1.000 27.520  ? 128 PHE FFF CZ  1 
ATOM   12311 N N   . PRO H 2 129 ? 70.000  51.214  40.770  1.000 35.652  ? 129 PRO FFF N   1 
ATOM   12312 C CA  . PRO H 2 129 ? 69.579  51.895  41.993  1.000 38.269  ? 129 PRO FFF CA  1 
ATOM   12313 C C   . PRO H 2 129 ? 70.764  52.539  42.712  1.000 38.147  ? 129 PRO FFF C   1 
ATOM   12314 O O   . PRO H 2 129 ? 71.769  51.897  42.835  1.000 39.203  ? 129 PRO FFF O   1 
ATOM   12315 C CB  . PRO H 2 129 ? 68.995  50.768  42.859  1.000 38.926  ? 129 PRO FFF CB  1 
ATOM   12316 C CG  . PRO H 2 129 ? 69.776  49.540  42.431  1.000 38.221  ? 129 PRO FFF CG  1 
ATOM   12317 C CD  . PRO H 2 129 ? 70.111  49.763  40.961  1.000 37.070  ? 129 PRO FFF CD  1 
ATOM   12318 N N   . LEU H 2 130 ? 70.607  53.793  43.125  1.000 39.717  ? 130 LEU FFF N   1 
ATOM   12319 C CA  . LEU H 2 130 ? 71.421  54.434  44.193  1.000 39.355  ? 130 LEU FFF CA  1 
ATOM   12320 C C   . LEU H 2 130 ? 70.729  54.116  45.522  1.000 39.033  ? 130 LEU FFF C   1 
ATOM   12321 O O   . LEU H 2 130 ? 69.903  54.894  45.970  1.000 38.096  ? 130 LEU FFF O   1 
ATOM   12322 C CB  . LEU H 2 130 ? 71.580  55.932  43.914  1.000 37.501  ? 130 LEU FFF CB  1 
ATOM   12323 C CG  . LEU H 2 130 ? 72.101  56.249  42.510  1.000 38.399  ? 130 LEU FFF CG  1 
ATOM   12324 C CD1 . LEU H 2 130 ? 72.316  57.735  42.315  1.000 41.165  ? 130 LEU FFF CD1 1 
ATOM   12325 C CD2 . LEU H 2 130 ? 73.399  55.510  42.221  1.000 37.831  ? 130 LEU FFF CD2 1 
ATOM   12326 N N   . ALA H 2 131 ? 71.043  52.946  46.074  1.000 39.651  ? 131 ALA FFF N   1 
ATOM   12327 C CA  . ALA H 2 131 ? 70.447  52.378  47.304  1.000 39.360  ? 131 ALA FFF CA  1 
ATOM   12328 C C   . ALA H 2 131 ? 70.791  53.248  48.503  1.000 40.117  ? 131 ALA FFF C   1 
ATOM   12329 O O   . ALA H 2 131 ? 71.936  53.661  48.667  1.000 39.613  ? 131 ALA FFF O   1 
ATOM   12330 C CB  . ALA H 2 131 ? 70.956  50.975  47.509  1.000 41.732  ? 131 ALA FFF CB  1 
ATOM   12331 N N   . PRO H 2 132 ? 69.813  53.525  49.387  1.000 44.371  ? 132 PRO FFF N   1 
ATOM   12332 C CA  . PRO H 2 132 ? 70.054  54.343  50.573  1.000 50.238  ? 132 PRO FFF CA  1 
ATOM   12333 C C   . PRO H 2 132 ? 70.927  53.578  51.573  1.000 59.453  ? 132 PRO FFF C   1 
ATOM   12334 O O   . PRO H 2 132 ? 70.656  52.419  51.762  1.000 64.135  ? 132 PRO FFF O   1 
ATOM   12335 C CB  . PRO H 2 132 ? 68.651  54.560  51.167  1.000 46.092  ? 132 PRO FFF CB  1 
ATOM   12336 C CG  . PRO H 2 132 ? 67.854  53.366  50.686  1.000 43.471  ? 132 PRO FFF CG  1 
ATOM   12337 C CD  . PRO H 2 132 ? 68.433  53.025  49.328  1.000 43.516  ? 132 PRO FFF CD  1 
ATOM   12338 N N   . SER H 2 133 ? 71.935  54.217  52.171  1.000 67.035  ? 133 SER FFF N   1 
ATOM   12339 C CA  . SER H 2 133 ? 72.741  53.589  53.247  1.000 72.683  ? 133 SER FFF CA  1 
ATOM   12340 C C   . SER H 2 133 ? 71.799  53.271  54.411  1.000 82.600  ? 133 SER FFF C   1 
ATOM   12341 O O   . SER H 2 133 ? 70.975  54.146  54.786  1.000 78.829  ? 133 SER FFF O   1 
ATOM   12342 C CB  . SER H 2 133 ? 73.892  54.439  53.694  1.000 73.804  ? 133 SER FFF CB  1 
ATOM   12343 O OG  . SER H 2 133 ? 73.409  55.593  54.353  1.000 85.210  ? 133 SER FFF OG  1 
ATOM   12344 N N   . SER H 2 134 ? 71.899  52.032  54.902  1.000 94.924  ? 134 SER FFF N   1 
ATOM   12345 C CA  . SER H 2 134 ? 71.230  51.497  56.113  1.000 96.033  ? 134 SER FFF CA  1 
ATOM   12346 C C   . SER H 2 134 ? 71.715  52.297  57.324  1.000 100.419 ? 134 SER FFF C   1 
ATOM   12347 O O   . SER H 2 134 ? 70.855  52.739  58.117  1.000 97.850  ? 134 SER FFF O   1 
ATOM   12348 C CB  . SER H 2 134 ? 71.538  50.036  56.261  1.000 87.826  ? 134 SER FFF CB  1 
ATOM   12349 O OG  . SER H 2 134 ? 72.946  49.854  56.358  1.000 76.957  ? 134 SER FFF OG  1 
ATOM   12350 N N   . LYS H 2 135 ? 73.036  52.484  57.436  1.000 99.198  ? 135 LYS FFF N   1 
ATOM   12351 C CA  . LYS H 2 135 ? 73.680  53.348  58.462  1.000 107.978 ? 135 LYS FFF CA  1 
ATOM   12352 C C   . LYS H 2 135 ? 73.554  54.811  58.027  1.000 98.759  ? 135 LYS FFF C   1 
ATOM   12353 O O   . LYS H 2 135 ? 74.459  55.270  57.321  1.000 96.790  ? 135 LYS FFF O   1 
ATOM   12354 C CB  . LYS H 2 135 ? 75.160  52.988  58.649  1.000 120.272 ? 135 LYS FFF CB  1 
ATOM   12355 C CG  . LYS H 2 135 ? 75.438  51.664  59.359  1.000 128.032 ? 135 LYS FFF CG  1 
ATOM   12356 C CD  . LYS H 2 135 ? 76.516  51.754  60.425  1.000 125.005 ? 135 LYS FFF CD  1 
ATOM   12357 C CE  . LYS H 2 135 ? 76.008  52.391  61.703  1.000 128.359 ? 135 LYS FFF CE  1 
ATOM   12358 N NZ  . LYS H 2 135 ? 76.970  53.378  62.245  1.000 135.554 ? 135 LYS FFF NZ  1 
ATOM   12359 N N   . SER H 2 136 ? 72.466  55.494  58.414  1.000 100.776 ? 136 SER FFF N   1 
ATOM   12360 C CA  . SER H 2 136 ? 72.204  56.946  58.186  1.000 112.101 ? 136 SER FFF CA  1 
ATOM   12361 C C   . SER H 2 136 ? 71.655  57.558  59.482  1.000 119.643 ? 136 SER FFF C   1 
ATOM   12362 O O   . SER H 2 136 ? 71.325  56.773  60.401  1.000 117.947 ? 136 SER FFF O   1 
ATOM   12363 C CB  . SER H 2 136 ? 71.281  57.187  56.991  1.000 105.934 ? 136 SER FFF CB  1 
ATOM   12364 O OG  . SER H 2 136 ? 70.001  56.590  57.160  1.000 84.807  ? 136 SER FFF OG  1 
ATOM   12365 N N   . THR H 2 137 ? 71.572  58.895  59.572  1.000 128.569 ? 137 THR FFF N   1 
ATOM   12366 C CA  . THR H 2 137 ? 71.037  59.616  60.768  1.000 127.010 ? 137 THR FFF CA  1 
ATOM   12367 C C   . THR H 2 137 ? 69.572  59.163  60.960  1.000 123.737 ? 137 THR FFF C   1 
ATOM   12368 O O   . THR H 2 137 ? 68.706  59.536  60.133  1.000 135.658 ? 137 THR FFF O   1 
ATOM   12369 C CB  . THR H 2 137 ? 71.276  61.139  60.710  1.000 121.571 ? 137 THR FFF CB  1 
ATOM   12370 O OG1 . THR H 2 137 ? 70.534  61.718  59.633  1.000 130.652 ? 137 THR FFF OG1 1 
ATOM   12371 C CG2 . THR H 2 137 ? 72.741  61.507  60.576  1.000 111.823 ? 137 THR FFF CG2 1 
ATOM   12372 N N   . SER H 2 138 ? 69.337  58.369  62.016  1.000 113.140 ? 138 SER FFF N   1 
ATOM   12373 C CA  . SER H 2 138 ? 68.115  57.569  62.320  1.000 102.881 ? 138 SER FFF CA  1 
ATOM   12374 C C   . SER H 2 138 ? 66.849  58.438  62.489  1.000 103.421 ? 138 SER FFF C   1 
ATOM   12375 O O   . SER H 2 138 ? 65.778  57.998  62.048  1.000 100.724 ? 138 SER FFF O   1 
ATOM   12376 C CB  . SER H 2 138 ? 68.368  56.721  63.540  1.000 96.798  ? 138 SER FFF CB  1 
ATOM   12377 O OG  . SER H 2 138 ? 67.264  55.875  63.794  1.000 97.005  ? 138 SER FFF OG  1 
ATOM   12378 N N   . GLY H 2 139 ? 66.942  59.613  63.119  1.000 107.222 ? 139 GLY FFF N   1 
ATOM   12379 C CA  . GLY H 2 139 ? 65.831  60.582  63.272  1.000 99.298  ? 139 GLY FFF CA  1 
ATOM   12380 C C   . GLY H 2 139 ? 65.707  61.564  62.103  1.000 101.890 ? 139 GLY FFF C   1 
ATOM   12381 O O   . GLY H 2 139 ? 64.597  62.095  61.907  1.000 99.801  ? 139 GLY FFF O   1 
ATOM   12382 N N   . GLY H 2 140 ? 66.805  61.831  61.376  1.000 103.838 ? 140 GLY FFF N   1 
ATOM   12383 C CA  . GLY H 2 140 ? 66.890  62.780  60.238  1.000 87.660  ? 140 GLY FFF CA  1 
ATOM   12384 C C   . GLY H 2 140 ? 66.537  62.136  58.901  1.000 73.267  ? 140 GLY FFF C   1 
ATOM   12385 O O   . GLY H 2 140 ? 65.705  61.233  58.894  1.000 53.870  ? 140 GLY FFF O   1 
ATOM   12386 N N   . THR H 2 141 ? 67.153  62.576  57.801  1.000 69.261  ? 141 THR FFF N   1 
ATOM   12387 C CA  . THR H 2 141 ? 66.729  62.230  56.419  1.000 64.575  ? 141 THR FFF CA  1 
ATOM   12388 C C   . THR H 2 141 ? 67.754  61.296  55.751  1.000 51.246  ? 141 THR FFF C   1 
ATOM   12389 O O   . THR H 2 141 ? 68.939  61.352  56.111  1.000 52.339  ? 141 THR FFF O   1 
ATOM   12390 C CB  . THR H 2 141 ? 66.432  63.507  55.615  1.000 70.276  ? 141 THR FFF CB  1 
ATOM   12391 O OG1 . THR H 2 141 ? 65.935  63.074  54.341  1.000 94.032  ? 141 THR FFF OG1 1 
ATOM   12392 C CG2 . THR H 2 141 ? 67.625  64.433  55.464  1.000 69.254  ? 141 THR FFF CG2 1 
ATOM   12393 N N   . ALA H 2 142 ? 67.286  60.450  54.833  1.000 43.510  ? 142 ALA FFF N   1 
ATOM   12394 C CA  . ALA H 2 142 ? 68.090  59.528  53.998  1.000 41.991  ? 142 ALA FFF CA  1 
ATOM   12395 C C   . ALA H 2 142 ? 67.916  59.889  52.528  1.000 37.633  ? 142 ALA FFF C   1 
ATOM   12396 O O   . ALA H 2 142 ? 66.896  60.461  52.170  1.000 38.009  ? 142 ALA FFF O   1 
ATOM   12397 C CB  . ALA H 2 142 ? 67.674  58.096  54.219  1.000 42.892  ? 142 ALA FFF CB  1 
ATOM   12398 N N   . ALA H 2 143 ? 68.887  59.527  51.703  1.000 35.449  ? 143 ALA FFF N   1 
ATOM   12399 C CA  . ALA H 2 143 ? 68.895  59.825  50.260  1.000 33.958  ? 143 ALA FFF CA  1 
ATOM   12400 C C   . ALA H 2 143 ? 69.045  58.520  49.494  1.000 30.516  ? 143 ALA FFF C   1 
ATOM   12401 O O   . ALA H 2 143 ? 69.798  57.647  49.928  1.000 31.606  ? 143 ALA FFF O   1 
ATOM   12402 C CB  . ALA H 2 143 ? 70.008  60.785  49.919  1.000 37.296  ? 143 ALA FFF CB  1 
ATOM   12403 N N   . LEU H 2 144 ? 68.343  58.438  48.378  1.000 29.134  ? 144 LEU FFF N   1 
ATOM   12404 C CA  . LEU H 2 144 ? 68.301  57.280  47.460  1.000 28.320  ? 144 LEU FFF CA  1 
ATOM   12405 C C   . LEU H 2 144 ? 68.045  57.835  46.062  1.000 26.744  ? 144 LEU FFF C   1 
ATOM   12406 O O   . LEU H 2 144 ? 67.723  59.033  45.954  1.000 27.231  ? 144 LEU FFF O   1 
ATOM   12407 C CB  . LEU H 2 144 ? 67.192  56.326  47.925  1.000 28.807  ? 144 LEU FFF CB  1 
ATOM   12408 C CG  . LEU H 2 144 ? 65.771  56.884  47.894  1.000 28.852  ? 144 LEU FFF CG  1 
ATOM   12409 C CD1 . LEU H 2 144 ? 64.989  56.295  46.738  1.000 29.573  ? 144 LEU FFF CD1 1 
ATOM   12410 C CD2 . LEU H 2 144 ? 65.038  56.606  49.187  1.000 29.457  ? 144 LEU FFF CD2 1 
ATOM   12411 N N   . GLY H 2 145 ? 68.172  57.013  45.032  1.000 26.271  ? 145 GLY FFF N   1 
ATOM   12412 C CA  . GLY H 2 145 ? 68.025  57.504  43.657  1.000 28.675  ? 145 GLY FFF CA  1 
ATOM   12413 C C   . GLY H 2 145 ? 68.180  56.417  42.623  1.000 30.362  ? 145 GLY FFF C   1 
ATOM   12414 O O   . GLY H 2 145 ? 68.290  55.252  43.007  1.000 31.489  ? 145 GLY FFF O   1 
ATOM   12415 N N   . CYS H 2 146 ? 68.201  56.827  41.359  1.000 34.288  ? 146 CYS FFF N   1 
ATOM   12416 C CA  . CYS H 2 146 ? 68.476  55.996  40.170  1.000 38.110  ? 146 CYS FFF CA  1 
ATOM   12417 C C   . CYS H 2 146 ? 69.615  56.608  39.380  1.000 35.282  ? 146 CYS FFF C   1 
ATOM   12418 O O   . CYS H 2 146 ? 69.717  57.830  39.358  1.000 36.086  ? 146 CYS FFF O   1 
ATOM   12419 C CB  . CYS H 2 146 ? 67.260  55.933  39.269  1.000 44.489  ? 146 CYS FFF CB  1 
ATOM   12420 S SG  . CYS H 2 146 ? 66.034  54.827  39.991  1.000 56.970  ? 146 CYS FFF SG  1 
ATOM   12421 N N   . LEU H 2 147 ? 70.414  55.762  38.757  1.000 33.821  ? 147 LEU FFF N   1 
ATOM   12422 C CA  . LEU H 2 147 ? 71.452  56.166  37.787  1.000 33.093  ? 147 LEU FFF CA  1 
ATOM   12423 C C   . LEU H 2 147 ? 70.953  55.723  36.419  1.000 30.060  ? 147 LEU FFF C   1 
ATOM   12424 O O   . LEU H 2 147 ? 70.743  54.528  36.234  1.000 27.487  ? 147 LEU FFF O   1 
ATOM   12425 C CB  . LEU H 2 147 ? 72.771  55.487  38.165  1.000 36.865  ? 147 LEU FFF CB  1 
ATOM   12426 C CG  . LEU H 2 147 ? 73.970  55.871  37.297  1.000 37.448  ? 147 LEU FFF CG  1 
ATOM   12427 C CD1 . LEU H 2 147 ? 74.295  57.347  37.444  1.000 38.849  ? 147 LEU FFF CD1 1 
ATOM   12428 C CD2 . LEU H 2 147 ? 75.183  55.034  37.638  1.000 36.636  ? 147 LEU FFF CD2 1 
ATOM   12429 N N   . VAL H 2 148 ? 70.658  56.674  35.550  1.000 30.644  ? 148 VAL FFF N   1 
ATOM   12430 C CA  . VAL H 2 148 ? 70.200  56.409  34.164  1.000 32.829  ? 148 VAL FFF CA  1 
ATOM   12431 C C   . VAL H 2 148 ? 71.429  56.583  33.277  1.000 33.464  ? 148 VAL FFF C   1 
ATOM   12432 O O   . VAL H 2 148 ? 71.787  57.746  33.004  1.000 33.962  ? 148 VAL FFF O   1 
ATOM   12433 C CB  . VAL H 2 148 ? 69.038  57.345  33.783  1.000 35.120  ? 148 VAL FFF CB  1 
ATOM   12434 C CG1 . VAL H 2 148 ? 68.448  56.968  32.434  1.000 37.984  ? 148 VAL FFF CG1 1 
ATOM   12435 C CG2 . VAL H 2 148 ? 67.947  57.351  34.850  1.000 35.969  ? 148 VAL FFF CG2 1 
ATOM   12436 N N   . LYS H 2 149 ? 72.062  55.473  32.893  1.000 35.428  ? 149 LYS FFF N   1 
ATOM   12437 C CA  . LYS H 2 149 ? 73.430  55.467  32.305  1.000 39.188  ? 149 LYS FFF CA  1 
ATOM   12438 C C   . LYS H 2 149 ? 73.421  54.933  30.863  1.000 37.674  ? 149 LYS FFF C   1 
ATOM   12439 O O   . LYS H 2 149 ? 72.728  53.939  30.585  1.000 31.160  ? 149 LYS FFF O   1 
ATOM   12440 C CB  . LYS H 2 149 ? 74.386  54.646  33.183  1.000 42.976  ? 149 LYS FFF CB  1 
ATOM   12441 C CG  . LYS H 2 149 ? 75.874  54.936  32.983  1.000 44.423  ? 149 LYS FFF CG  1 
ATOM   12442 C CD  . LYS H 2 149 ? 76.781  53.973  33.721  1.000 48.564  ? 149 LYS FFF CD  1 
ATOM   12443 C CE  . LYS H 2 149 ? 78.127  53.775  33.048  1.000 52.259  ? 149 LYS FFF CE  1 
ATOM   12444 N NZ  . LYS H 2 149 ? 78.812  55.069  32.804  1.000 56.048  ? 149 LYS FFF NZ  1 
ATOM   12445 N N   . ASP H 2 150 ? 74.186  55.595  29.988  1.000 42.100  ? 150 ASP FFF N   1 
ATOM   12446 C CA  . ASP H 2 150 ? 74.583  55.086  28.650  1.000 44.436  ? 150 ASP FFF CA  1 
ATOM   12447 C C   . ASP H 2 150 ? 73.357  55.040  27.750  1.000 41.741  ? 150 ASP FFF C   1 
ATOM   12448 O O   . ASP H 2 150 ? 72.932  53.925  27.408  1.000 55.344  ? 150 ASP FFF O   1 
ATOM   12449 C CB  . ASP H 2 150 ? 75.246  53.705  28.751  1.000 47.677  ? 150 ASP FFF CB  1 
ATOM   12450 C CG  . ASP H 2 150 ? 76.543  53.679  29.542  1.000 48.520  ? 150 ASP FFF CG  1 
ATOM   12451 O OD1 . ASP H 2 150 ? 77.230  54.731  29.592  1.000 50.591  ? 150 ASP FFF OD1 1 
ATOM   12452 O OD2 . ASP H 2 150 ? 76.867  52.602  30.091  1.000 45.131  ? 150 ASP FFF OD2 1 
ATOM   12453 N N   . TYR H 2 151 ? 72.823  56.201  27.376  1.000 37.614  ? 151 TYR FFF N   1 
ATOM   12454 C CA  . TYR H 2 151 ? 71.677  56.325  26.435  1.000 36.791  ? 151 TYR FFF CA  1 
ATOM   12455 C C   . TYR H 2 151 ? 71.974  57.391  25.381  1.000 36.659  ? 151 TYR FFF C   1 
ATOM   12456 O O   . TYR H 2 151 ? 72.831  58.246  25.605  1.000 34.119  ? 151 TYR FFF O   1 
ATOM   12457 C CB  . TYR H 2 151 ? 70.368  56.615  27.183  1.000 35.704  ? 151 TYR FFF CB  1 
ATOM   12458 C CG  . TYR H 2 151 ? 70.260  57.959  27.857  1.000 32.115  ? 151 TYR FFF CG  1 
ATOM   12459 C CD1 . TYR H 2 151 ? 70.680  58.144  29.157  1.000 30.497  ? 151 TYR FFF CD1 1 
ATOM   12460 C CD2 . TYR H 2 151 ? 69.694  59.034  27.208  1.000 32.218  ? 151 TYR FFF CD2 1 
ATOM   12461 C CE1 . TYR H 2 151 ? 70.563  59.367  29.790  1.000 31.661  ? 151 TYR FFF CE1 1 
ATOM   12462 C CE2 . TYR H 2 151 ? 69.578  60.271  27.821  1.000 33.784  ? 151 TYR FFF CE2 1 
ATOM   12463 C CZ  . TYR H 2 151 ? 70.012  60.442  29.122  1.000 33.209  ? 151 TYR FFF CZ  1 
ATOM   12464 O OH  . TYR H 2 151 ? 69.883  61.657  29.739  1.000 32.526  ? 151 TYR FFF OH  1 
ATOM   12465 N N   . PHE H 2 152 ? 71.244  57.326  24.267  1.000 36.988  ? 152 PHE FFF N   1 
ATOM   12466 C CA  . PHE H 2 152 ? 71.296  58.282  23.135  1.000 36.303  ? 152 PHE FFF CA  1 
ATOM   12467 C C   . PHE H 2 152 ? 70.030  58.125  22.307  1.000 36.563  ? 152 PHE FFF C   1 
ATOM   12468 O O   . PHE H 2 152 ? 69.566  57.016  22.105  1.000 38.148  ? 152 PHE FFF O   1 
ATOM   12469 C CB  . PHE H 2 152 ? 72.519  58.036  22.249  1.000 37.202  ? 152 PHE FFF CB  1 
ATOM   12470 C CG  . PHE H 2 152 ? 72.691  59.070  21.164  1.000 37.019  ? 152 PHE FFF CG  1 
ATOM   12471 C CD1 . PHE H 2 152 ? 73.406  60.234  21.408  1.000 37.075  ? 152 PHE FFF CD1 1 
ATOM   12472 C CD2 . PHE H 2 152 ? 72.100  58.909  19.924  1.000 35.785  ? 152 PHE FFF CD2 1 
ATOM   12473 C CE1 . PHE H 2 152 ? 73.545  61.204  20.431  1.000 37.752  ? 152 PHE FFF CE1 1 
ATOM   12474 C CE2 . PHE H 2 152 ? 72.232  59.883  18.948  1.000 36.396  ? 152 PHE FFF CE2 1 
ATOM   12475 C CZ  . PHE H 2 152 ? 72.944  61.030  19.207  1.000 37.947  ? 152 PHE FFF CZ  1 
ATOM   12476 N N   . PRO H 2 153 ? 69.426  59.212  21.789  1.000 37.924  ? 153 PRO FFF N   1 
ATOM   12477 C CA  . PRO H 2 153 ? 69.842  60.568  22.126  1.000 38.895  ? 153 PRO FFF CA  1 
ATOM   12478 C C   . PRO H 2 153 ? 69.227  61.043  23.443  1.000 41.025  ? 153 PRO FFF C   1 
ATOM   12479 O O   . PRO H 2 153 ? 68.681  60.230  24.159  1.000 43.042  ? 153 PRO FFF O   1 
ATOM   12480 C CB  . PRO H 2 153 ? 69.303  61.344  20.925  1.000 38.271  ? 153 PRO FFF CB  1 
ATOM   12481 C CG  . PRO H 2 153 ? 68.026  60.623  20.550  1.000 36.343  ? 153 PRO FFF CG  1 
ATOM   12482 C CD  . PRO H 2 153 ? 68.340  59.171  20.796  1.000 36.826  ? 153 PRO FFF CD  1 
ATOM   12483 N N   . GLU H 2 154 ? 69.331  62.340  23.729  1.000 40.828  ? 154 GLU FFF N   1 
ATOM   12484 C CA  . GLU H 2 154 ? 68.453  63.012  24.713  1.000 40.084  ? 154 GLU FFF CA  1 
ATOM   12485 C C   . GLU H 2 154 ? 67.040  63.055  24.132  1.000 35.664  ? 154 GLU FFF C   1 
ATOM   12486 O O   . GLU H 2 154 ? 66.872  63.032  22.918  1.000 35.824  ? 154 GLU FFF O   1 
ATOM   12487 C CB  . GLU H 2 154 ? 69.018  64.398  24.986  1.000 44.428  ? 154 GLU FFF CB  1 
ATOM   12488 C CG  . GLU H 2 154 ? 70.143  64.382  25.992  1.000 46.095  ? 154 GLU FFF CG  1 
ATOM   12489 C CD  . GLU H 2 154 ? 69.681  64.808  27.373  1.000 51.235  ? 154 GLU FFF CD  1 
ATOM   12490 O OE1 . GLU H 2 154 ? 68.812  64.114  27.945  1.000 56.218  ? 154 GLU FFF OE1 1 
ATOM   12491 O OE2 . GLU H 2 154 ? 70.173  65.844  27.877  1.000 53.264  ? 154 GLU FFF OE2 1 
ATOM   12492 N N   . PRO H 2 155 ? 65.964  63.151  24.943  1.000 32.402  ? 155 PRO FFF N   1 
ATOM   12493 C CA  . PRO H 2 155 ? 66.025  63.098  26.402  1.000 32.047  ? 155 PRO FFF CA  1 
ATOM   12494 C C   . PRO H 2 155 ? 65.452  61.840  27.066  1.000 32.508  ? 155 PRO FFF C   1 
ATOM   12495 O O   . PRO H 2 155 ? 64.887  61.000  26.384  1.000 35.182  ? 155 PRO FFF O   1 
ATOM   12496 C CB  . PRO H 2 155 ? 65.078  64.254  26.727  1.000 33.375  ? 155 PRO FFF CB  1 
ATOM   12497 C CG  . PRO H 2 155 ? 63.965  64.128  25.685  1.000 33.537  ? 155 PRO FFF CG  1 
ATOM   12498 C CD  . PRO H 2 155 ? 64.601  63.459  24.477  1.000 33.299  ? 155 PRO FFF CD  1 
ATOM   12499 N N   . VAL H 2 156 ? 65.576  61.753  28.390  1.000 33.282  ? 156 VAL FFF N   1 
ATOM   12500 C CA  . VAL H 2 156 ? 64.814  60.771  29.212  1.000 34.299  ? 156 VAL FFF CA  1 
ATOM   12501 C C   . VAL H 2 156 ? 63.958  61.572  30.168  1.000 34.640  ? 156 VAL FFF C   1 
ATOM   12502 O O   . VAL H 2 156 ? 64.363  62.685  30.489  1.000 37.797  ? 156 VAL FFF O   1 
ATOM   12503 C CB  . VAL H 2 156 ? 65.702  59.781  29.985  1.000 35.092  ? 156 VAL FFF CB  1 
ATOM   12504 C CG1 . VAL H 2 156 ? 66.416  58.843  29.034  1.000 36.631  ? 156 VAL FFF CG1 1 
ATOM   12505 C CG2 . VAL H 2 156 ? 66.701  60.460  30.907  1.000 35.196  ? 156 VAL FFF CG2 1 
ATOM   12506 N N   . THR H 2 157 ? 62.804  61.032  30.541  1.000 36.247  ? 157 THR FFF N   1 
ATOM   12507 C CA  . THR H 2 157 ? 61.940  61.578  31.614  1.000 38.067  ? 157 THR FFF CA  1 
ATOM   12508 C C   . THR H 2 157 ? 62.095  60.648  32.817  1.000 35.791  ? 157 THR FFF C   1 
ATOM   12509 O O   . THR H 2 157 ? 62.080  59.427  32.624  1.000 36.892  ? 157 THR FFF O   1 
ATOM   12510 C CB  . THR H 2 157 ? 60.475  61.707  31.180  1.000 43.100  ? 157 THR FFF CB  1 
ATOM   12511 O OG1 . THR H 2 157 ? 59.912  60.397  31.228  1.000 50.742  ? 157 THR FFF OG1 1 
ATOM   12512 C CG2 . THR H 2 157 ? 60.270  62.282  29.791  1.000 46.229  ? 157 THR FFF CG2 1 
ATOM   12513 N N   . VAL H 2 158 ? 62.290  61.224  33.993  1.000 34.219  ? 158 VAL FFF N   1 
ATOM   12514 C CA  . VAL H 2 158 ? 62.370  60.504  35.287  1.000 33.427  ? 158 VAL FFF CA  1 
ATOM   12515 C C   . VAL H 2 158 ? 61.316  61.102  36.230  1.000 35.010  ? 158 VAL FFF C   1 
ATOM   12516 O O   . VAL H 2 158 ? 61.412  62.312  36.546  1.000 35.687  ? 158 VAL FFF O   1 
ATOM   12517 C CB  . VAL H 2 158 ? 63.778  60.617  35.888  1.000 33.430  ? 158 VAL FFF CB  1 
ATOM   12518 C CG1 . VAL H 2 158 ? 63.871  59.863  37.197  1.000 36.260  ? 158 VAL FFF CG1 1 
ATOM   12519 C CG2 . VAL H 2 158 ? 64.846  60.139  34.924  1.000 33.045  ? 158 VAL FFF CG2 1 
ATOM   12520 N N   . SER H 2 159 ? 60.348  60.294  36.658  1.000 36.094  ? 159 SER FFF N   1 
ATOM   12521 C CA  . SER H 2 159 ? 59.428  60.586  37.782  1.000 34.946  ? 159 SER FFF CA  1 
ATOM   12522 C C   . SER H 2 159 ? 59.706  59.569  38.886  1.000 31.014  ? 159 SER FFF C   1 
ATOM   12523 O O   . SER H 2 159 ? 60.475  58.637  38.622  1.000 30.248  ? 159 SER FFF O   1 
ATOM   12524 C CB  . SER H 2 159 ? 58.001  60.519  37.312  1.000 39.684  ? 159 SER FFF CB  1 
ATOM   12525 O OG  . SER H 2 159 ? 57.736  59.214  36.804  1.000 44.955  ? 159 SER FFF OG  1 
ATOM   12526 N N   . TRP H 2 160 ? 59.030  59.719  40.023  1.000 30.997  ? 160 TRP FFF N   1 
ATOM   12527 C CA  . TRP H 2 160 ? 59.116  58.831  41.212  1.000 32.559  ? 160 TRP FFF CA  1 
ATOM   12528 C C   . TRP H 2 160 ? 57.710  58.412  41.674  1.000 33.927  ? 160 TRP FFF C   1 
ATOM   12529 O O   . TRP H 2 160 ? 56.841  59.302  41.838  1.000 35.398  ? 160 TRP FFF O   1 
ATOM   12530 C CB  . TRP H 2 160 ? 59.872  59.541  42.339  1.000 32.036  ? 160 TRP FFF CB  1 
ATOM   12531 C CG  . TRP H 2 160 ? 61.354  59.552  42.152  1.000 34.213  ? 160 TRP FFF CG  1 
ATOM   12532 C CD1 . TRP H 2 160 ? 62.099  60.532  41.580  1.000 34.892  ? 160 TRP FFF CD1 1 
ATOM   12533 C CD2 . TRP H 2 160 ? 62.284  58.530  42.537  1.000 37.303  ? 160 TRP FFF CD2 1 
ATOM   12534 N NE1 . TRP H 2 160 ? 63.420  60.192  41.579  1.000 36.058  ? 160 TRP FFF NE1 1 
ATOM   12535 C CE2 . TRP H 2 160 ? 63.563  58.965  42.156  1.000 36.452  ? 160 TRP FFF CE2 1 
ATOM   12536 C CE3 . TRP H 2 160 ? 62.162  57.292  43.167  1.000 38.271  ? 160 TRP FFF CE3 1 
ATOM   12537 C CZ2 . TRP H 2 160 ? 64.702  58.205  42.385  1.000 37.662  ? 160 TRP FFF CZ2 1 
ATOM   12538 C CZ3 . TRP H 2 160 ? 63.290  56.533  43.390  1.000 35.533  ? 160 TRP FFF CZ3 1 
ATOM   12539 C CH2 . TRP H 2 160 ? 64.542  56.985  43.000  1.000 35.688  ? 160 TRP FFF CH2 1 
ATOM   12540 N N   . ASN H 2 161 ? 57.511  57.116  41.935  1.000 35.520  ? 161 ASN FFF N   1 
ATOM   12541 C CA  . ASN H 2 161 ? 56.227  56.556  42.427  1.000 36.861  ? 161 ASN FFF CA  1 
ATOM   12542 C C   . ASN H 2 161 ? 55.126  57.008  41.451  1.000 43.696  ? 161 ASN FFF C   1 
ATOM   12543 O O   . ASN H 2 161 ? 54.098  57.583  41.891  1.000 40.891  ? 161 ASN FFF O   1 
ATOM   12544 C CB  . ASN H 2 161 ? 55.997  56.953  43.885  1.000 34.714  ? 161 ASN FFF CB  1 
ATOM   12545 C CG  . ASN H 2 161 ? 56.937  56.269  44.857  1.000 35.601  ? 161 ASN FFF CG  1 
ATOM   12546 O OD1 . ASN H 2 161 ? 57.560  55.258  44.535  1.000 36.451  ? 161 ASN FFF OD1 1 
ATOM   12547 N ND2 . ASN H 2 161 ? 57.047  56.810  46.068  1.000 36.143  ? 161 ASN FFF ND2 1 
ATOM   12548 N N   . SER H 2 162 ? 55.411  56.858  40.151  1.000 50.072  ? 162 SER FFF N   1 
ATOM   12549 C CA  . SER H 2 162 ? 54.533  57.185  38.998  1.000 51.362  ? 162 SER FFF CA  1 
ATOM   12550 C C   . SER H 2 162 ? 54.018  58.624  39.086  1.000 48.146  ? 162 SER FFF C   1 
ATOM   12551 O O   . SER H 2 162 ? 52.899  58.849  38.648  1.000 48.015  ? 162 SER FFF O   1 
ATOM   12552 C CB  . SER H 2 162 ? 53.399  56.219  38.894  1.000 53.256  ? 162 SER FFF CB  1 
ATOM   12553 O OG  . SER H 2 162 ? 53.885  54.888  38.959  1.000 67.938  ? 162 SER FFF OG  1 
ATOM   12554 N N   . GLY H 2 163 ? 54.810  59.546  39.633  1.000 44.349  ? 163 GLY FFF N   1 
ATOM   12555 C CA  . GLY H 2 163 ? 54.482  60.980  39.665  1.000 40.020  ? 163 GLY FFF CA  1 
ATOM   12556 C C   . GLY H 2 163 ? 53.991  61.470  41.022  1.000 37.107  ? 163 GLY FFF C   1 
ATOM   12557 O O   . GLY H 2 163 ? 53.889  62.719  41.198  1.000 34.628  ? 163 GLY FFF O   1 
ATOM   12558 N N   . ALA H 2 164 ? 53.687  60.569  41.959  1.000 33.304  ? 164 ALA FFF N   1 
ATOM   12559 C CA  . ALA H 2 164 ? 53.176  60.898  43.317  1.000 29.911  ? 164 ALA FFF CA  1 
ATOM   12560 C C   . ALA H 2 164 ? 54.209  61.738  44.069  1.000 28.612  ? 164 ALA FFF C   1 
ATOM   12561 O O   . ALA H 2 164 ? 53.813  62.736  44.676  1.000 30.151  ? 164 ALA FFF O   1 
ATOM   12562 C CB  . ALA H 2 164 ? 52.865  59.631  44.081  1.000 29.602  ? 164 ALA FFF CB  1 
ATOM   12563 N N   . LEU H 2 165 ? 55.479  61.332  44.008  1.000 27.757  ? 165 LEU FFF N   1 
ATOM   12564 C CA  . LEU H 2 165 ? 56.613  61.905  44.788  1.000 29.630  ? 165 LEU FFF CA  1 
ATOM   12565 C C   . LEU H 2 165 ? 57.412  62.858  43.897  1.000 29.370  ? 165 LEU FFF C   1 
ATOM   12566 O O   . LEU H 2 165 ? 57.991  62.404  42.883  1.000 28.249  ? 165 LEU FFF O   1 
ATOM   12567 C CB  . LEU H 2 165 ? 57.506  60.766  45.305  1.000 32.251  ? 165 LEU FFF CB  1 
ATOM   12568 C CG  . LEU H 2 165 ? 58.809  61.180  46.001  1.000 31.260  ? 165 LEU FFF CG  1 
ATOM   12569 C CD1 . LEU H 2 165 ? 58.509  62.002  47.240  1.000 32.397  ? 165 LEU FFF CD1 1 
ATOM   12570 C CD2 . LEU H 2 165 ? 59.668  59.985  46.342  1.000 30.002  ? 165 LEU FFF CD2 1 
ATOM   12571 N N   . THR H 2 166 ? 57.411  64.143  44.251  1.000 29.515  ? 166 THR FFF N   1 
ATOM   12572 C CA  . THR H 2 166 ? 58.136  65.227  43.533  1.000 29.695  ? 166 THR FFF CA  1 
ATOM   12573 C C   . THR H 2 166 ? 58.900  66.086  44.543  1.000 31.603  ? 166 THR FFF C   1 
ATOM   12574 O O   . THR H 2 166 ? 59.890  66.729  44.137  1.000 30.385  ? 166 THR FFF O   1 
ATOM   12575 C CB  . THR H 2 166 ? 57.192  66.132  42.740  1.000 27.735  ? 166 THR FFF CB  1 
ATOM   12576 O OG1 . THR H 2 166 ? 56.396  66.776  43.730  1.000 29.277  ? 166 THR FFF OG1 1 
ATOM   12577 C CG2 . THR H 2 166 ? 56.308  65.398  41.762  1.000 28.396  ? 166 THR FFF CG2 1 
ATOM   12578 N N   . SER H 2 167 ? 58.443  66.122  45.799  1.000 33.098  ? 167 SER FFF N   1 
ATOM   12579 C CA  . SER H 2 167 ? 59.081  66.903  46.882  1.000 34.320  ? 167 SER FFF CA  1 
ATOM   12580 C C   . SER H 2 167 ? 60.435  66.271  47.217  1.000 36.602  ? 167 SER FFF C   1 
ATOM   12581 O O   . SER H 2 167 ? 60.518  65.034  47.448  1.000 34.466  ? 167 SER FFF O   1 
ATOM   12582 C CB  . SER H 2 167 ? 58.202  67.011  48.082  1.000 36.470  ? 167 SER FFF CB  1 
ATOM   12583 O OG  . SER H 2 167 ? 58.833  67.795  49.077  1.000 37.371  ? 167 SER FFF OG  1 
ATOM   12584 N N   . GLY H 2 168 ? 61.479  67.102  47.201  1.000 38.547  ? 168 GLY FFF N   1 
ATOM   12585 C CA  . GLY H 2 168 ? 62.843  66.703  47.575  1.000 38.060  ? 168 GLY FFF CA  1 
ATOM   12586 C C   . GLY H 2 168 ? 63.510  65.881  46.489  1.000 37.436  ? 168 GLY FFF C   1 
ATOM   12587 O O   . GLY H 2 168 ? 64.585  65.315  46.776  1.000 39.071  ? 168 GLY FFF O   1 
ATOM   12588 N N   . VAL H 2 169 ? 62.941  65.853  45.275  1.000 32.690  ? 169 VAL FFF N   1 
ATOM   12589 C CA  . VAL H 2 169 ? 63.559  65.184  44.093  1.000 31.611  ? 169 VAL FFF CA  1 
ATOM   12590 C C   . VAL H 2 169 ? 64.516  66.161  43.413  1.000 31.266  ? 169 VAL FFF C   1 
ATOM   12591 O O   . VAL H 2 169 ? 64.161  67.327  43.249  1.000 35.464  ? 169 VAL FFF O   1 
ATOM   12592 C CB  . VAL H 2 169 ? 62.515  64.685  43.081  1.000 29.179  ? 169 VAL FFF CB  1 
ATOM   12593 C CG1 . VAL H 2 169 ? 63.164  64.067  41.848  1.000 26.775  ? 169 VAL FFF CG1 1 
ATOM   12594 C CG2 . VAL H 2 169 ? 61.577  63.701  43.736  1.000 30.284  ? 169 VAL FFF CG2 1 
ATOM   12595 N N   . HIS H 2 170 ? 65.681  65.667  43.015  1.000 28.994  ? 170 HIS FFF N   1 
ATOM   12596 C CA  . HIS H 2 170 ? 66.615  66.339  42.090  1.000 28.061  ? 170 HIS FFF CA  1 
ATOM   12597 C C   . HIS H 2 170 ? 66.918  65.377  40.939  1.000 28.561  ? 170 HIS FFF C   1 
ATOM   12598 O O   . HIS H 2 170 ? 67.589  64.361  41.192  1.000 27.829  ? 170 HIS FFF O   1 
ATOM   12599 C CB  . HIS H 2 170 ? 67.871  66.754  42.850  1.000 27.957  ? 170 HIS FFF CB  1 
ATOM   12600 C CG  . HIS H 2 170 ? 67.644  67.819  43.866  1.000 27.685  ? 170 HIS FFF CG  1 
ATOM   12601 N ND1 . HIS H 2 170 ? 67.239  69.095  43.513  1.000 28.618  ? 170 HIS FFF ND1 1 
ATOM   12602 C CD2 . HIS H 2 170 ? 67.818  67.818  45.205  1.000 28.765  ? 170 HIS FFF CD2 1 
ATOM   12603 C CE1 . HIS H 2 170 ? 67.164  69.837  44.598  1.000 30.858  ? 170 HIS FFF CE1 1 
ATOM   12604 N NE2 . HIS H 2 170 ? 67.513  69.071  45.652  1.000 30.398  ? 170 HIS FFF NE2 1 
ATOM   12605 N N   . THR H 2 171 ? 66.411  65.655  39.736  1.000 29.499  ? 171 THR FFF N   1 
ATOM   12606 C CA  . THR H 2 171 ? 66.867  64.988  38.486  1.000 29.206  ? 171 THR FFF CA  1 
ATOM   12607 C C   . THR H 2 171 ? 67.927  65.882  37.865  1.000 29.772  ? 171 THR FFF C   1 
ATOM   12608 O O   . THR H 2 171 ? 67.565  66.955  37.374  1.000 33.335  ? 171 THR FFF O   1 
ATOM   12609 C CB  . THR H 2 171 ? 65.731  64.693  37.497  1.000 29.479  ? 171 THR FFF CB  1 
ATOM   12610 O OG1 . THR H 2 171 ? 64.721  63.892  38.125  1.000 30.967  ? 171 THR FFF OG1 1 
ATOM   12611 C CG2 . THR H 2 171 ? 66.239  63.988  36.255  1.000 28.820  ? 171 THR FFF CG2 1 
ATOM   12612 N N   . PHE H 2 172 ? 69.183  65.447  37.894  1.000 29.763  ? 172 PHE FFF N   1 
ATOM   12613 C CA  . PHE H 2 172 ? 70.336  66.229  37.391  1.000 29.576  ? 172 PHE FFF CA  1 
ATOM   12614 C C   . PHE H 2 172 ? 70.276  66.303  35.874  1.000 29.596  ? 172 PHE FFF C   1 
ATOM   12615 O O   . PHE H 2 172 ? 69.683  65.453  35.214  1.000 30.943  ? 172 PHE FFF O   1 
ATOM   12616 C CB  . PHE H 2 172 ? 71.660  65.642  37.899  1.000 29.904  ? 172 PHE FFF CB  1 
ATOM   12617 C CG  . PHE H 2 172 ? 71.834  65.832  39.382  1.000 27.659  ? 172 PHE FFF CG  1 
ATOM   12618 C CD1 . PHE H 2 172 ? 71.509  64.821  40.267  1.000 27.563  ? 172 PHE FFF CD1 1 
ATOM   12619 C CD2 . PHE H 2 172 ? 72.236  67.054  39.889  1.000 26.857  ? 172 PHE FFF CD2 1 
ATOM   12620 C CE1 . PHE H 2 172 ? 71.613  65.023  41.633  1.000 28.572  ? 172 PHE FFF CE1 1 
ATOM   12621 C CE2 . PHE H 2 172 ? 72.321  67.257  41.255  1.000 27.925  ? 172 PHE FFF CE2 1 
ATOM   12622 C CZ  . PHE H 2 172 ? 72.012  66.243  42.126  1.000 28.537  ? 172 PHE FFF CZ  1 
ATOM   12623 N N   . PRO H 2 173 ? 70.884  67.354  35.292  1.000 30.815  ? 173 PRO FFF N   1 
ATOM   12624 C CA  . PRO H 2 173 ? 71.105  67.429  33.855  1.000 30.825  ? 173 PRO FFF CA  1 
ATOM   12625 C C   . PRO H 2 173 ? 71.965  66.270  33.370  1.000 32.013  ? 173 PRO FFF C   1 
ATOM   12626 O O   . PRO H 2 173 ? 72.915  65.909  34.049  1.000 34.462  ? 173 PRO FFF O   1 
ATOM   12627 C CB  . PRO H 2 173 ? 71.924  68.700  33.663  1.000 30.749  ? 173 PRO FFF CB  1 
ATOM   12628 C CG  . PRO H 2 173 ? 71.610  69.534  34.884  1.000 32.576  ? 173 PRO FFF CG  1 
ATOM   12629 C CD  . PRO H 2 173 ? 71.383  68.539  35.999  1.000 32.583  ? 173 PRO FFF CD  1 
ATOM   12630 N N   . ALA H 2 174 ? 71.626  65.714  32.218  1.000 34.348  ? 174 ALA FFF N   1 
ATOM   12631 C CA  . ALA H 2 174 ? 72.464  64.668  31.604  1.000 37.449  ? 174 ALA FFF CA  1 
ATOM   12632 C C   . ALA H 2 174 ? 73.841  65.274  31.363  1.000 37.912  ? 174 ALA FFF C   1 
ATOM   12633 O O   . ALA H 2 174 ? 73.895  66.490  31.128  1.000 40.751  ? 174 ALA FFF O   1 
ATOM   12634 C CB  . ALA H 2 174 ? 71.844  64.194  30.324  1.000 38.138  ? 174 ALA FFF CB  1 
ATOM   12635 N N   . VAL H 2 175 ? 74.892  64.464  31.451  1.000 40.966  ? 175 VAL FFF N   1 
ATOM   12636 C CA  . VAL H 2 175 ? 76.248  64.801  30.930  1.000 41.145  ? 175 VAL FFF CA  1 
ATOM   12637 C C   . VAL H 2 175 ? 76.491  63.898  29.731  1.000 40.553  ? 175 VAL FFF C   1 
ATOM   12638 O O   . VAL H 2 175 ? 76.026  62.749  29.743  1.000 42.343  ? 175 VAL FFF O   1 
ATOM   12639 C CB  . VAL H 2 175 ? 77.340  64.632  31.998  1.000 42.932  ? 175 VAL FFF CB  1 
ATOM   12640 C CG1 . VAL H 2 175 ? 76.941  65.334  33.287  1.000 45.597  ? 175 VAL FFF CG1 1 
ATOM   12641 C CG2 . VAL H 2 175 ? 77.667  63.168  32.266  1.000 44.368  ? 175 VAL FFF CG2 1 
ATOM   12642 N N   . LEU H 2 176 ? 77.159  64.422  28.720  1.000 41.714  ? 176 LEU FFF N   1 
ATOM   12643 C CA  . LEU H 2 176 ? 77.627  63.632  27.558  1.000 41.221  ? 176 LEU FFF CA  1 
ATOM   12644 C C   . LEU H 2 176 ? 78.953  62.998  27.964  1.000 41.551  ? 176 LEU FFF C   1 
ATOM   12645 O O   . LEU H 2 176 ? 79.892  63.747  28.216  1.000 44.680  ? 176 LEU FFF O   1 
ATOM   12646 C CB  . LEU H 2 176 ? 77.759  64.610  26.394  1.000 42.407  ? 176 LEU FFF CB  1 
ATOM   12647 C CG  . LEU H 2 176 ? 78.023  64.038  25.009  1.000 44.897  ? 176 LEU FFF CG  1 
ATOM   12648 C CD1 . LEU H 2 176 ? 77.208  62.810  24.728  1.000 48.070  ? 176 LEU FFF CD1 1 
ATOM   12649 C CD2 . LEU H 2 176 ? 77.684  65.075  23.953  1.000 46.971  ? 176 LEU FFF CD2 1 
ATOM   12650 N N   . GLN H 2 177 ? 78.992  61.681  28.131  1.000 45.163  ? 177 GLN FFF N   1 
ATOM   12651 C CA  . GLN H 2 177 ? 80.235  60.943  28.481  1.000 49.398  ? 177 GLN FFF CA  1 
ATOM   12652 C C   . GLN H 2 177 ? 81.108  60.885  27.224  1.000 49.687  ? 177 GLN FFF C   1 
ATOM   12653 O O   . GLN H 2 177 ? 80.597  61.143  26.125  1.000 46.174  ? 177 GLN FFF O   1 
ATOM   12654 C CB  . GLN H 2 177 ? 79.937  59.529  28.988  1.000 51.875  ? 177 GLN FFF CB  1 
ATOM   12655 C CG  . GLN H 2 177 ? 79.069  59.487  30.232  1.000 54.410  ? 177 GLN FFF CG  1 
ATOM   12656 C CD  . GLN H 2 177 ? 78.506  58.106  30.474  1.000 59.880  ? 177 GLN FFF CD  1 
ATOM   12657 O OE1 . GLN H 2 177 ? 78.578  57.578  31.584  1.000 66.623  ? 177 GLN FFF OE1 1 
ATOM   12658 N NE2 . GLN H 2 177 ? 77.939  57.504  29.435  1.000 59.673  ? 177 GLN FFF NE2 1 
ATOM   12659 N N   . SER H 2 178 ? 82.386  60.546  27.384  1.000 54.180  ? 178 SER FFF N   1 
ATOM   12660 C CA  . SER H 2 178 ? 83.377  60.504  26.280  1.000 57.833  ? 178 SER FFF CA  1 
ATOM   12661 C C   . SER H 2 178 ? 83.026  59.370  25.299  1.000 56.471  ? 178 SER FFF C   1 
ATOM   12662 O O   . SER H 2 178 ? 83.523  59.425  24.169  1.000 65.246  ? 178 SER FFF O   1 
ATOM   12663 C CB  . SER H 2 178 ? 84.778  60.393  26.827  1.000 60.445  ? 178 SER FFF CB  1 
ATOM   12664 O OG  . SER H 2 178 ? 84.862  59.319  27.749  1.000 64.997  ? 178 SER FFF OG  1 
ATOM   12665 N N   . SER H 2 179 ? 82.169  58.415  25.682  1.000 49.965  ? 179 SER FFF N   1 
ATOM   12666 C CA  . SER H 2 179 ? 81.641  57.343  24.790  1.000 46.254  ? 179 SER FFF CA  1 
ATOM   12667 C C   . SER H 2 179 ? 80.606  57.895  23.806  1.000 44.016  ? 179 SER FFF C   1 
ATOM   12668 O O   . SER H 2 179 ? 80.141  57.126  22.942  1.000 41.195  ? 179 SER FFF O   1 
ATOM   12669 C CB  . SER H 2 179 ? 81.055  56.189  25.583  1.000 47.742  ? 179 SER FFF CB  1 
ATOM   12670 O OG  . SER H 2 179 ? 79.976  56.606  26.405  1.000 45.622  ? 179 SER FFF OG  1 
ATOM   12671 N N   . GLY H 2 180 ? 80.204  59.157  23.958  1.000 45.953  ? 180 GLY FFF N   1 
ATOM   12672 C CA  . GLY H 2 180 ? 79.183  59.797  23.101  1.000 47.404  ? 180 GLY FFF CA  1 
ATOM   12673 C C   . GLY H 2 180 ? 77.773  59.481  23.563  1.000 46.082  ? 180 GLY FFF C   1 
ATOM   12674 O O   . GLY H 2 180 ? 76.829  60.008  22.940  1.000 51.214  ? 180 GLY FFF O   1 
ATOM   12675 N N   . LEU H 2 181 ? 77.654  58.669  24.621  1.000 41.712  ? 181 LEU FFF N   1 
ATOM   12676 C CA  . LEU H 2 181 ? 76.390  58.302  25.300  1.000 39.026  ? 181 LEU FFF CA  1 
ATOM   12677 C C   . LEU H 2 181 ? 76.176  59.228  26.494  1.000 37.219  ? 181 LEU FFF C   1 
ATOM   12678 O O   . LEU H 2 181 ? 77.169  59.566  27.152  1.000 37.279  ? 181 LEU FFF O   1 
ATOM   12679 C CB  . LEU H 2 181 ? 76.500  56.856  25.787  1.000 41.781  ? 181 LEU FFF CB  1 
ATOM   12680 C CG  . LEU H 2 181 ? 76.662  55.791  24.708  1.000 43.149  ? 181 LEU FFF CG  1 
ATOM   12681 C CD1 . LEU H 2 181 ? 76.638  54.419  25.349  1.000 45.339  ? 181 LEU FFF CD1 1 
ATOM   12682 C CD2 . LEU H 2 181 ? 75.578  55.894  23.647  1.000 43.923  ? 181 LEU FFF CD2 1 
ATOM   12683 N N   . TYR H 2 182 ? 74.926  59.605  26.760  1.000 36.465  ? 182 TYR FFF N   1 
ATOM   12684 C CA  . TYR H 2 182 ? 74.521  60.474  27.892  1.000 37.619  ? 182 TYR FFF CA  1 
ATOM   12685 C C   . TYR H 2 182 ? 74.304  59.639  29.156  1.000 39.791  ? 182 TYR FFF C   1 
ATOM   12686 O O   . TYR H 2 182 ? 74.128  58.410  29.087  1.000 43.304  ? 182 TYR FFF O   1 
ATOM   12687 C CB  . TYR H 2 182 ? 73.240  61.228  27.553  1.000 37.850  ? 182 TYR FFF CB  1 
ATOM   12688 C CG  . TYR H 2 182 ? 73.378  62.211  26.423  1.000 37.912  ? 182 TYR FFF CG  1 
ATOM   12689 C CD1 . TYR H 2 182 ? 73.094  61.842  25.123  1.000 40.732  ? 182 TYR FFF CD1 1 
ATOM   12690 C CD2 . TYR H 2 182 ? 73.745  63.521  26.655  1.000 37.236  ? 182 TYR FFF CD2 1 
ATOM   12691 C CE1 . TYR H 2 182 ? 73.177  62.745  24.076  1.000 41.274  ? 182 TYR FFF CE1 1 
ATOM   12692 C CE2 . TYR H 2 182 ? 73.860  64.429  25.615  1.000 37.703  ? 182 TYR FFF CE2 1 
ATOM   12693 C CZ  . TYR H 2 182 ? 73.575  64.039  24.323  1.000 38.355  ? 182 TYR FFF CZ  1 
ATOM   12694 O OH  . TYR H 2 182 ? 73.663  64.910  23.291  1.000 39.236  ? 182 TYR FFF OH  1 
ATOM   12695 N N   . SER H 2 183 ? 74.285  60.316  30.298  1.000 40.905  ? 183 SER FFF N   1 
ATOM   12696 C CA  . SER H 2 183 ? 74.190  59.693  31.635  1.000 42.426  ? 183 SER FFF CA  1 
ATOM   12697 C C   . SER H 2 183 ? 73.752  60.747  32.645  1.000 40.571  ? 183 SER FFF C   1 
ATOM   12698 O O   . SER H 2 183 ? 74.248  61.883  32.601  1.000 44.659  ? 183 SER FFF O   1 
ATOM   12699 C CB  . SER H 2 183 ? 75.494  59.061  32.020  1.000 49.085  ? 183 SER FFF CB  1 
ATOM   12700 O OG  . SER H 2 183 ? 75.451  58.602  33.363  1.000 53.866  ? 183 SER FFF OG  1 
ATOM   12701 N N   . LEU H 2 184 ? 72.908  60.333  33.569  1.000 37.154  ? 184 LEU FFF N   1 
ATOM   12702 C CA  . LEU H 2 184 ? 72.060  61.227  34.380  1.000 34.634  ? 184 LEU FFF CA  1 
ATOM   12703 C C   . LEU H 2 184 ? 71.763  60.468  35.659  1.000 31.788  ? 184 LEU FFF C   1 
ATOM   12704 O O   . LEU H 2 184 ? 71.698  59.240  35.588  1.000 33.407  ? 184 LEU FFF O   1 
ATOM   12705 C CB  . LEU H 2 184 ? 70.820  61.472  33.523  1.000 36.064  ? 184 LEU FFF CB  1 
ATOM   12706 C CG  . LEU H 2 184 ? 69.621  62.148  34.171  1.000 37.322  ? 184 LEU FFF CG  1 
ATOM   12707 C CD1 . LEU H 2 184 ? 68.784  62.820  33.101  1.000 39.357  ? 184 LEU FFF CD1 1 
ATOM   12708 C CD2 . LEU H 2 184 ? 68.764  61.156  34.938  1.000 37.313  ? 184 LEU FFF CD2 1 
ATOM   12709 N N   . SER H 2 185 ? 71.671  61.133  36.795  1.000 30.275  ? 185 SER FFF N   1 
ATOM   12710 C CA  . SER H 2 185 ? 71.180  60.463  38.026  1.000 31.731  ? 185 SER FFF CA  1 
ATOM   12711 C C   . SER H 2 185 ? 70.071  61.315  38.644  1.000 29.634  ? 185 SER FFF C   1 
ATOM   12712 O O   . SER H 2 185 ? 70.158  62.534  38.555  1.000 29.337  ? 185 SER FFF O   1 
ATOM   12713 C CB  . SER H 2 185 ? 72.294  60.104  39.001  1.000 33.902  ? 185 SER FFF CB  1 
ATOM   12714 O OG  . SER H 2 185 ? 73.278  61.118  39.072  1.000 38.250  ? 185 SER FFF OG  1 
ATOM   12715 N N   . SER H 2 186 ? 69.006  60.662  39.115  1.000 28.501  ? 186 SER FFF N   1 
ATOM   12716 C CA  . SER H 2 186 ? 67.845  61.286  39.801  1.000 27.888  ? 186 SER FFF CA  1 
ATOM   12717 C C   . SER H 2 186 ? 67.871  60.842  41.260  1.000 29.229  ? 186 SER FFF C   1 
ATOM   12718 O O   . SER H 2 186 ? 67.973  59.645  41.509  1.000 31.542  ? 186 SER FFF O   1 
ATOM   12719 C CB  . SER H 2 186 ? 66.553  60.916  39.132  1.000 25.407  ? 186 SER FFF CB  1 
ATOM   12720 O OG  . SER H 2 186 ? 65.470  61.623  39.694  1.000 22.461  ? 186 SER FFF OG  1 
ATOM   12721 N N   . VAL H 2 187 ? 67.832  61.780  42.184  1.000 29.090  ? 187 VAL FFF N   1 
ATOM   12722 C CA  . VAL H 2 187 ? 67.975  61.458  43.623  1.000 31.733  ? 187 VAL FFF CA  1 
ATOM   12723 C C   . VAL H 2 187 ? 66.767  62.064  44.310  1.000 32.200  ? 187 VAL FFF C   1 
ATOM   12724 O O   . VAL H 2 187 ? 66.161  62.964  43.721  1.000 30.939  ? 187 VAL FFF O   1 
ATOM   12725 C CB  . VAL H 2 187 ? 69.296  62.002  44.199  1.000 34.775  ? 187 VAL FFF CB  1 
ATOM   12726 C CG1 . VAL H 2 187 ? 70.500  61.374  43.525  1.000 36.047  ? 187 VAL FFF CG1 1 
ATOM   12727 C CG2 . VAL H 2 187 ? 69.377  63.519  44.117  1.000 35.566  ? 187 VAL FFF CG2 1 
ATOM   12728 N N   . VAL H 2 188 ? 66.473  61.606  45.524  1.000 33.822  ? 188 VAL FFF N   1 
ATOM   12729 C CA  . VAL H 2 188 ? 65.394  62.178  46.374  1.000 33.604  ? 188 VAL FFF CA  1 
ATOM   12730 C C   . VAL H 2 188 ? 65.796  61.986  47.835  1.000 34.885  ? 188 VAL FFF C   1 
ATOM   12731 O O   . VAL H 2 188 ? 66.466  60.985  48.117  1.000 36.348  ? 188 VAL FFF O   1 
ATOM   12732 C CB  . VAL H 2 188 ? 64.047  61.525  46.035  1.000 33.274  ? 188 VAL FFF CB  1 
ATOM   12733 C CG1 . VAL H 2 188 ? 64.126  60.003  46.070  1.000 32.532  ? 188 VAL FFF CG1 1 
ATOM   12734 C CG2 . VAL H 2 188 ? 62.933  62.080  46.907  1.000 32.389  ? 188 VAL FFF CG2 1 
ATOM   12735 N N   . THR H 2 189 ? 65.460  62.952  48.696  1.000 34.864  ? 189 THR FFF N   1 
ATOM   12736 C CA  . THR H 2 189 ? 65.579  62.849  50.170  1.000 35.840  ? 189 THR FFF CA  1 
ATOM   12737 C C   . THR H 2 189 ? 64.194  62.561  50.750  1.000 35.761  ? 189 THR FFF C   1 
ATOM   12738 O O   . THR H 2 189 ? 63.227  63.240  50.364  1.000 37.707  ? 189 THR FFF O   1 
ATOM   12739 C CB  . THR H 2 189 ? 66.213  64.100  50.780  1.000 39.354  ? 189 THR FFF CB  1 
ATOM   12740 O OG1 . THR H 2 189 ? 65.632  65.270  50.208  1.000 42.020  ? 189 THR FFF OG1 1 
ATOM   12741 C CG2 . THR H 2 189 ? 67.706  64.138  50.561  1.000 44.117  ? 189 THR FFF CG2 1 
ATOM   12742 N N   . VAL H 2 190 ? 64.113  61.544  51.606  1.000 36.479  ? 190 VAL FFF N   1 
ATOM   12743 C CA  . VAL H 2 190 ? 62.878  61.090  52.300  1.000 38.232  ? 190 VAL FFF CA  1 
ATOM   12744 C C   . VAL H 2 190 ? 63.226  60.844  53.760  1.000 38.055  ? 190 VAL FFF C   1 
ATOM   12745 O O   . VAL H 2 190 ? 64.381  60.582  54.081  1.000 38.846  ? 190 VAL FFF O   1 
ATOM   12746 C CB  . VAL H 2 190 ? 62.326  59.822  51.623  1.000 41.859  ? 190 VAL FFF CB  1 
ATOM   12747 C CG1 . VAL H 2 190 ? 62.106  60.046  50.142  1.000 43.295  ? 190 VAL FFF CG1 1 
ATOM   12748 C CG2 . VAL H 2 190 ? 63.230  58.615  51.792  1.000 43.619  ? 190 VAL FFF CG2 1 
ATOM   12749 N N   . PRO H 2 191 ? 62.256  60.914  54.693  1.000 40.388  ? 191 PRO FFF N   1 
ATOM   12750 C CA  . PRO H 2 191 ? 62.518  60.537  56.083  1.000 44.578  ? 191 PRO FFF CA  1 
ATOM   12751 C C   . PRO H 2 191 ? 63.099  59.117  56.186  1.000 47.184  ? 191 PRO FFF C   1 
ATOM   12752 O O   . PRO H 2 191 ? 62.597  58.240  55.527  1.000 54.255  ? 191 PRO FFF O   1 
ATOM   12753 C CB  . PRO H 2 191 ? 61.126  60.614  56.724  1.000 44.855  ? 191 PRO FFF CB  1 
ATOM   12754 C CG  . PRO H 2 191 ? 60.371  61.618  55.875  1.000 43.199  ? 191 PRO FFF CG  1 
ATOM   12755 C CD  . PRO H 2 191 ? 60.879  61.379  54.469  1.000 41.343  ? 191 PRO FFF CD  1 
ATOM   12756 N N   . SER H 2 192 ? 64.125  58.906  57.011  1.000 48.544  ? 192 SER FFF N   1 
ATOM   12757 C CA  . SER H 2 192 ? 64.785  57.588  57.170  1.000 50.568  ? 192 SER FFF CA  1 
ATOM   12758 C C   . SER H 2 192 ? 63.798  56.572  57.759  1.000 50.535  ? 192 SER FFF C   1 
ATOM   12759 O O   . SER H 2 192 ? 63.917  55.402  57.372  1.000 54.835  ? 192 SER FFF O   1 
ATOM   12760 C CB  . SER H 2 192 ? 66.058  57.679  57.977  1.000 55.327  ? 192 SER FFF CB  1 
ATOM   12761 O OG  . SER H 2 192 ? 65.921  58.573  59.061  1.000 56.678  ? 192 SER FFF OG  1 
ATOM   12762 N N   . SER H 2 193 ? 62.852  56.988  58.613  1.000 49.786  ? 193 SER FFF N   1 
ATOM   12763 C CA  . SER H 2 193 ? 61.803  56.100  59.186  1.000 52.977  ? 193 SER FFF CA  1 
ATOM   12764 C C   . SER H 2 193 ? 60.922  55.502  58.075  1.000 48.930  ? 193 SER FFF C   1 
ATOM   12765 O O   . SER H 2 193 ? 60.391  54.398  58.263  1.000 51.518  ? 193 SER FFF O   1 
ATOM   12766 C CB  . SER H 2 193 ? 60.967  56.821  60.206  1.000 58.996  ? 193 SER FFF CB  1 
ATOM   12767 O OG  . SER H 2 193 ? 60.174  57.829  59.593  1.000 65.815  ? 193 SER FFF OG  1 
ATOM   12768 N N   . SER H 2 194 ? 60.766  56.200  56.956  1.000 46.578  ? 194 SER FFF N   1 
ATOM   12769 C CA  . SER H 2 194 ? 59.902  55.774  55.826  1.000 47.559  ? 194 SER FFF CA  1 
ATOM   12770 C C   . SER H 2 194 ? 60.620  54.773  54.918  1.000 45.887  ? 194 SER FFF C   1 
ATOM   12771 O O   . SER H 2 194 ? 60.032  54.405  53.916  1.000 53.462  ? 194 SER FFF O   1 
ATOM   12772 C CB  . SER H 2 194 ? 59.405  56.957  55.030  1.000 47.165  ? 194 SER FFF CB  1 
ATOM   12773 O OG  . SER H 2 194 ? 60.449  57.497  54.237  1.000 46.320  ? 194 SER FFF OG  1 
ATOM   12774 N N   . LEU H 2 195 ? 61.840  54.343  55.223  1.000 46.069  ? 195 LEU FFF N   1 
ATOM   12775 C CA  . LEU H 2 195 ? 62.584  53.404  54.335  1.000 48.886  ? 195 LEU FFF CA  1 
ATOM   12776 C C   . LEU H 2 195 ? 61.978  52.003  54.460  1.000 50.869  ? 195 LEU FFF C   1 
ATOM   12777 O O   . LEU H 2 195 ? 62.104  51.221  53.502  1.000 53.973  ? 195 LEU FFF O   1 
ATOM   12778 C CB  . LEU H 2 195 ? 64.074  53.398  54.692  1.000 49.560  ? 195 LEU FFF CB  1 
ATOM   12779 C CG  . LEU H 2 195 ? 64.890  54.555  54.115  1.000 48.566  ? 195 LEU FFF CG  1 
ATOM   12780 C CD1 . LEU H 2 195 ? 66.354  54.426  54.497  1.000 48.863  ? 195 LEU FFF CD1 1 
ATOM   12781 C CD2 . LEU H 2 195 ? 64.759  54.615  52.598  1.000 48.774  ? 195 LEU FFF CD2 1 
ATOM   12782 N N   . GLY H 2 196 ? 61.330  51.714  55.591  1.000 50.511  ? 196 GLY FFF N   1 
ATOM   12783 C CA  . GLY H 2 196 ? 60.728  50.403  55.885  1.000 51.260  ? 196 GLY FFF CA  1 
ATOM   12784 C C   . GLY H 2 196 ? 59.278  50.341  55.465  1.000 46.834  ? 196 GLY FFF C   1 
ATOM   12785 O O   . GLY H 2 196 ? 58.770  49.232  55.245  1.000 51.155  ? 196 GLY FFF O   1 
ATOM   12786 N N   . THR H 2 197 ? 58.642  51.498  55.328  1.000 44.003  ? 197 THR FFF N   1 
ATOM   12787 C CA  . THR H 2 197 ? 57.166  51.658  55.311  1.000 45.441  ? 197 THR FFF CA  1 
ATOM   12788 C C   . THR H 2 197 ? 56.666  52.121  53.937  1.000 47.726  ? 197 THR FFF C   1 
ATOM   12789 O O   . THR H 2 197 ? 55.438  52.185  53.759  1.000 45.222  ? 197 THR FFF O   1 
ATOM   12790 C CB  . THR H 2 197 ? 56.726  52.667  56.379  1.000 44.139  ? 197 THR FFF CB  1 
ATOM   12791 O OG1 . THR H 2 197 ? 56.628  53.959  55.780  1.000 39.537  ? 197 THR FFF OG1 1 
ATOM   12792 C CG2 . THR H 2 197 ? 57.655  52.701  57.576  1.000 47.528  ? 197 THR FFF CG2 1 
ATOM   12793 N N   . GLN H 2 198 ? 57.558  52.610  53.088  1.000 51.513  ? 198 GLN FFF N   1 
ATOM   12794 C CA  . GLN H 2 198 ? 57.183  53.228  51.803  1.000 51.530  ? 198 GLN FFF CA  1 
ATOM   12795 C C   . GLN H 2 198 ? 58.010  52.585  50.703  1.000 39.995  ? 198 GLN FFF C   1 
ATOM   12796 O O   . GLN H 2 198 ? 59.212  52.454  50.866  1.000 38.597  ? 198 GLN FFF O   1 
ATOM   12797 C CB  . GLN H 2 198 ? 57.374  54.751  51.878  1.000 63.614  ? 198 GLN FFF CB  1 
ATOM   12798 C CG  . GLN H 2 198 ? 56.871  55.481  50.647  1.000 74.784  ? 198 GLN FFF CG  1 
ATOM   12799 C CD  . GLN H 2 198 ? 55.393  55.217  50.498  1.000 78.465  ? 198 GLN FFF CD  1 
ATOM   12800 O OE1 . GLN H 2 198 ? 54.968  54.287  49.787  1.000 76.867  ? 198 GLN FFF OE1 1 
ATOM   12801 N NE2 . GLN H 2 198 ? 54.627  55.969  51.285  1.000 65.903  ? 198 GLN FFF NE2 1 
ATOM   12802 N N   . THR H 2 199 ? 57.365  52.186  49.612  1.000 35.028  ? 199 THR FFF N   1 
ATOM   12803 C CA  . THR H 2 199 ? 58.053  51.756  48.365  1.000 31.372  ? 199 THR FFF CA  1 
ATOM   12804 C C   . THR H 2 199 ? 58.467  52.989  47.549  1.000 30.194  ? 199 THR FFF C   1 
ATOM   12805 O O   . THR H 2 199 ? 57.630  53.898  47.367  1.000 28.539  ? 199 THR FFF O   1 
ATOM   12806 C CB  . THR H 2 199 ? 57.179  50.782  47.581  1.000 29.305  ? 199 THR FFF CB  1 
ATOM   12807 O OG1 . THR H 2 199 ? 57.291  49.542  48.278  1.000 32.408  ? 199 THR FFF OG1 1 
ATOM   12808 C CG2 . THR H 2 199 ? 57.610  50.602  46.149  1.000 28.911  ? 199 THR FFF CG2 1 
ATOM   12809 N N   . TYR H 2 200 ? 59.728  53.008  47.106  1.000 31.582  ? 200 TYR FFF N   1 
ATOM   12810 C CA  . TYR H 2 200 ? 60.328  54.018  46.192  1.000 29.123  ? 200 TYR FFF CA  1 
ATOM   12811 C C   . TYR H 2 200 ? 60.669  53.339  44.873  1.000 27.761  ? 200 TYR FFF C   1 
ATOM   12812 O O   . TYR H 2 200 ? 61.453  52.364  44.855  1.000 27.553  ? 200 TYR FFF O   1 
ATOM   12813 C CB  . TYR H 2 200 ? 61.551  54.669  46.844  1.000 28.406  ? 200 TYR FFF CB  1 
ATOM   12814 C CG  . TYR H 2 200 ? 61.140  55.500  48.029  1.000 28.446  ? 200 TYR FFF CG  1 
ATOM   12815 C CD1 . TYR H 2 200 ? 60.353  56.623  47.857  1.000 29.479  ? 200 TYR FFF CD1 1 
ATOM   12816 C CD2 . TYR H 2 200 ? 61.406  55.097  49.322  1.000 28.588  ? 200 TYR FFF CD2 1 
ATOM   12817 C CE1 . TYR H 2 200 ? 59.888  57.359  48.934  1.000 29.193  ? 200 TYR FFF CE1 1 
ATOM   12818 C CE2 . TYR H 2 200 ? 60.945  55.812  50.411  1.000 29.147  ? 200 TYR FFF CE2 1 
ATOM   12819 C CZ  . TYR H 2 200 ? 60.198  56.958  50.217  1.000 29.380  ? 200 TYR FFF CZ  1 
ATOM   12820 O OH  . TYR H 2 200 ? 59.775  57.715  51.269  1.000 30.117  ? 200 TYR FFF OH  1 
ATOM   12821 N N   . ILE H 2 201 ? 60.040  53.831  43.810  1.000 28.725  ? 201 ILE FFF N   1 
ATOM   12822 C CA  . ILE H 2 201 ? 60.259  53.390  42.406  1.000 30.539  ? 201 ILE FFF CA  1 
ATOM   12823 C C   . ILE H 2 201 ? 60.556  54.622  41.558  1.000 31.054  ? 201 ILE FFF C   1 
ATOM   12824 O O   . ILE H 2 201 ? 59.783  55.579  41.668  1.000 28.239  ? 201 ILE FFF O   1 
ATOM   12825 C CB  . ILE H 2 201 ? 59.023  52.661  41.860  1.000 29.967  ? 201 ILE FFF CB  1 
ATOM   12826 C CG1 . ILE H 2 201 ? 58.725  51.399  42.667  1.000 29.990  ? 201 ILE FFF CG1 1 
ATOM   12827 C CG2 . ILE H 2 201 ? 59.210  52.382  40.376  1.000 32.251  ? 201 ILE FFF CG2 1 
ATOM   12828 C CD1 . ILE H 2 201 ? 57.812  50.399  41.979  1.000 32.048  ? 201 ILE FFF CD1 1 
ATOM   12829 N N   . CYS H 2 202 ? 61.606  54.582  40.736  1.000 34.203  ? 202 CYS FFF N   1 
ATOM   12830 C CA  . CYS H 2 202 ? 61.846  55.618  39.707  1.000 40.240  ? 202 CYS FFF CA  1 
ATOM   12831 C C   . CYS H 2 202 ? 61.369  55.090  38.354  1.000 38.761  ? 202 CYS FFF C   1 
ATOM   12832 O O   . CYS H 2 202 ? 61.673  53.944  38.031  1.000 37.618  ? 202 CYS FFF O   1 
ATOM   12833 C CB  . CYS H 2 202 ? 63.297  56.086  39.670  1.000 48.398  ? 202 CYS FFF CB  1 
ATOM   12834 S SG  . CYS H 2 202 ? 64.420  55.022  38.730  1.000 60.749  ? 202 CYS FFF SG  1 
ATOM   12835 N N   . ASN H 2 203 ? 60.644  55.921  37.607  1.000 38.346  ? 203 ASN FFF N   1 
ATOM   12836 C CA  . ASN H 2 203 ? 60.092  55.570  36.286  1.000 35.035  ? 203 ASN FFF CA  1 
ATOM   12837 C C   . ASN H 2 203 ? 60.938  56.315  35.281  1.000 34.537  ? 203 ASN FFF C   1 
ATOM   12838 O O   . ASN H 2 203 ? 61.015  57.537  35.394  1.000 35.616  ? 203 ASN FFF O   1 
ATOM   12839 C CB  . ASN H 2 203 ? 58.614  55.913  36.220  1.000 37.724  ? 203 ASN FFF CB  1 
ATOM   12840 C CG  . ASN H 2 203 ? 57.936  55.689  37.554  1.000 39.661  ? 203 ASN FFF CG  1 
ATOM   12841 O OD1 . ASN H 2 203 ? 57.920  56.598  38.406  1.000 37.700  ? 203 ASN FFF OD1 1 
ATOM   12842 N ND2 . ASN H 2 203 ? 57.401  54.489  37.744  1.000 36.917  ? 203 ASN FFF ND2 1 
ATOM   12843 N N   . VAL H 2 204 ? 61.607  55.573  34.413  1.000 34.899  ? 204 VAL FFF N   1 
ATOM   12844 C CA  . VAL H 2 204 ? 62.462  56.133  33.340  1.000 35.309  ? 204 VAL FFF CA  1 
ATOM   12845 C C   . VAL H 2 204 ? 61.749  55.866  32.023  1.000 34.519  ? 204 VAL FFF C   1 
ATOM   12846 O O   . VAL H 2 204 ? 61.281  54.738  31.814  1.000 37.913  ? 204 VAL FFF O   1 
ATOM   12847 C CB  . VAL H 2 204 ? 63.855  55.490  33.401  1.000 40.776  ? 204 VAL FFF CB  1 
ATOM   12848 C CG1 . VAL H 2 204 ? 64.801  56.009  32.311  1.000 44.108  ? 204 VAL FFF CG1 1 
ATOM   12849 C CG2 . VAL H 2 204 ? 64.457  55.662  34.792  1.000 42.787  ? 204 VAL FFF CG2 1 
ATOM   12850 N N   . ASN H 2 205 ? 61.599  56.891  31.203  1.000 34.414  ? 205 ASN FFF N   1 
ATOM   12851 C CA  . ASN H 2 205 ? 61.048  56.739  29.836  1.000 35.857  ? 205 ASN FFF CA  1 
ATOM   12852 C C   . ASN H 2 205 ? 62.077  57.307  28.860  1.000 33.852  ? 205 ASN FFF C   1 
ATOM   12853 O O   . ASN H 2 205 ? 62.489  58.438  29.053  1.000 32.375  ? 205 ASN FFF O   1 
ATOM   12854 C CB  . ASN H 2 205 ? 59.656  57.360  29.717  1.000 37.314  ? 205 ASN FFF CB  1 
ATOM   12855 C CG  . ASN H 2 205 ? 58.940  56.878  28.475  1.000 40.206  ? 205 ASN FFF CG  1 
ATOM   12856 O OD1 . ASN H 2 205 ? 59.329  55.891  27.852  1.000 40.333  ? 205 ASN FFF OD1 1 
ATOM   12857 N ND2 . ASN H 2 205 ? 57.880  57.575  28.100  1.000 40.253  ? 205 ASN FFF ND2 1 
ATOM   12858 N N   . HIS H 2 206 ? 62.525  56.510  27.895  1.000 35.467  ? 206 HIS FFF N   1 
ATOM   12859 C CA  . HIS H 2 206 ? 63.380  56.949  26.761  1.000 37.663  ? 206 HIS FFF CA  1 
ATOM   12860 C C   . HIS H 2 206 ? 62.605  56.697  25.460  1.000 42.747  ? 206 HIS FFF C   1 
ATOM   12861 O O   . HIS H 2 206 ? 62.768  55.624  24.842  1.000 41.089  ? 206 HIS FFF O   1 
ATOM   12862 C CB  . HIS H 2 206 ? 64.740  56.246  26.795  1.000 34.796  ? 206 HIS FFF CB  1 
ATOM   12863 C CG  . HIS H 2 206 ? 65.713  56.788  25.803  1.000 34.535  ? 206 HIS FFF CG  1 
ATOM   12864 N ND1 . HIS H 2 206 ? 66.505  55.988  24.995  1.000 34.803  ? 206 HIS FFF ND1 1 
ATOM   12865 C CD2 . HIS H 2 206 ? 66.032  58.055  25.491  1.000 35.766  ? 206 HIS FFF CD2 1 
ATOM   12866 C CE1 . HIS H 2 206 ? 67.271  56.741  24.240  1.000 34.054  ? 206 HIS FFF CE1 1 
ATOM   12867 N NE2 . HIS H 2 206 ? 66.997  58.010  24.527  1.000 35.944  ? 206 HIS FFF NE2 1 
ATOM   12868 N N   . LYS H 2 207 ? 61.761  57.656  25.074  1.000 48.045  ? 207 LYS FFF N   1 
ATOM   12869 C CA  . LYS H 2 207 ? 60.842  57.501  23.925  1.000 50.101  ? 207 LYS FFF CA  1 
ATOM   12870 C C   . LYS H 2 207 ? 61.631  57.143  22.669  1.000 47.797  ? 207 LYS FFF C   1 
ATOM   12871 O O   . LYS H 2 207 ? 61.197  56.279  21.917  1.000 48.632  ? 207 LYS FFF O   1 
ATOM   12872 C CB  . LYS H 2 207 ? 59.990  58.762  23.766  1.000 57.922  ? 207 LYS FFF CB  1 
ATOM   12873 C CG  . LYS H 2 207 ? 58.775  58.844  24.686  1.000 65.378  ? 207 LYS FFF CG  1 
ATOM   12874 C CD  . LYS H 2 207 ? 57.470  59.116  23.916  1.000 78.933  ? 207 LYS FFF CD  1 
ATOM   12875 C CE  . LYS H 2 207 ? 56.243  59.220  24.793  1.000 90.074  ? 207 LYS FFF CE  1 
ATOM   12876 N NZ  . LYS H 2 207 ? 56.315  60.410  25.674  1.000 90.984  ? 207 LYS FFF NZ  1 
ATOM   12877 N N   . PRO H 2 208 ? 62.786  57.787  22.378  1.000 48.982  ? 208 PRO FFF N   1 
ATOM   12878 C CA  . PRO H 2 208 ? 63.551  57.492  21.164  1.000 48.976  ? 208 PRO FFF CA  1 
ATOM   12879 C C   . PRO H 2 208 ? 63.874  56.010  20.934  1.000 47.225  ? 208 PRO FFF C   1 
ATOM   12880 O O   . PRO H 2 208 ? 63.806  55.568  19.810  1.000 42.038  ? 208 PRO FFF O   1 
ATOM   12881 C CB  . PRO H 2 208 ? 64.857  58.251  21.386  1.000 49.581  ? 208 PRO FFF CB  1 
ATOM   12882 C CG  . PRO H 2 208 ? 64.434  59.437  22.215  1.000 52.398  ? 208 PRO FFF CG  1 
ATOM   12883 C CD  . PRO H 2 208 ? 63.388  58.886  23.153  1.000 50.586  ? 208 PRO FFF CD  1 
ATOM   12884 N N   . SER H 2 209 ? 64.204  55.290  22.007  1.000 50.402  ? 209 SER FFF N   1 
ATOM   12885 C CA  . SER H 2 209 ? 64.577  53.848  21.997  1.000 49.189  ? 209 SER FFF CA  1 
ATOM   12886 C C   . SER H 2 209 ? 63.374  52.993  22.402  1.000 47.332  ? 209 SER FFF C   1 
ATOM   12887 O O   . SER H 2 209 ? 63.508  51.770  22.495  1.000 46.936  ? 209 SER FFF O   1 
ATOM   12888 C CB  . SER H 2 209 ? 65.741  53.605  22.914  1.000 49.339  ? 209 SER FFF CB  1 
ATOM   12889 O OG  . SER H 2 209 ? 65.314  53.589  24.269  1.000 49.011  ? 209 SER FFF OG  1 
ATOM   12890 N N   . ASN H 2 210 ? 62.247  53.647  22.650  1.000 54.614  ? 210 ASN FFF N   1 
ATOM   12891 C CA  . ASN H 2 210 ? 60.961  53.031  23.059  1.000 56.858  ? 210 ASN FFF CA  1 
ATOM   12892 C C   . ASN H 2 210 ? 61.209  52.127  24.268  1.000 49.324  ? 210 ASN FFF C   1 
ATOM   12893 O O   . ASN H 2 210 ? 60.820  50.973  24.222  1.000 49.624  ? 210 ASN FFF O   1 
ATOM   12894 C CB  . ASN H 2 210 ? 60.294  52.328  21.882  1.000 63.873  ? 210 ASN FFF CB  1 
ATOM   12895 C CG  . ASN H 2 210 ? 58.800  52.269  22.084  1.000 82.610  ? 210 ASN FFF CG  1 
ATOM   12896 O OD1 . ASN H 2 210 ? 58.302  52.546  23.180  1.000 91.674  ? 210 ASN FFF OD1 1 
ATOM   12897 N ND2 . ASN H 2 210 ? 58.081  51.980  21.011  1.000 97.507  ? 210 ASN FFF ND2 1 
ATOM   12898 N N   . THR H 2 211 ? 61.839  52.677  25.302  1.000 45.624  ? 211 THR FFF N   1 
ATOM   12899 C CA  . THR H 2 211 ? 62.325  51.976  26.511  1.000 42.882  ? 211 THR FFF CA  1 
ATOM   12900 C C   . THR H 2 211 ? 61.615  52.573  27.714  1.000 45.082  ? 211 THR FFF C   1 
ATOM   12901 O O   . THR H 2 211 ? 61.910  53.724  28.048  1.000 46.501  ? 211 THR FFF O   1 
ATOM   12902 C CB  . THR H 2 211 ? 63.827  52.212  26.697  1.000 41.450  ? 211 THR FFF CB  1 
ATOM   12903 O OG1 . THR H 2 211 ? 64.449  51.531  25.610  1.000 41.553  ? 211 THR FFF OG1 1 
ATOM   12904 C CG2 . THR H 2 211 ? 64.375  51.771  28.044  1.000 40.403  ? 211 THR FFF CG2 1 
ATOM   12905 N N   . LYS H 2 212 ? 60.706  51.828  28.333  1.000 49.201  ? 212 LYS FFF N   1 
ATOM   12906 C CA  . LYS H 2 212 ? 60.094  52.211  29.633  1.000 49.249  ? 212 LYS FFF CA  1 
ATOM   12907 C C   . LYS H 2 212 ? 60.681  51.276  30.701  1.000 45.505  ? 212 LYS FFF C   1 
ATOM   12908 O O   . LYS H 2 212 ? 60.727  50.043  30.472  1.000 48.375  ? 212 LYS FFF O   1 
ATOM   12909 C CB  . LYS H 2 212 ? 58.563  52.206  29.538  1.000 50.132  ? 212 LYS FFF CB  1 
ATOM   12910 C CG  . LYS H 2 212 ? 57.886  53.297  30.358  1.000 59.116  ? 212 LYS FFF CG  1 
ATOM   12911 C CD  . LYS H 2 212 ? 56.376  53.361  30.198  1.000 65.190  ? 212 LYS FFF CD  1 
ATOM   12912 C CE  . LYS H 2 212 ? 55.932  54.195  29.011  1.000 70.453  ? 212 LYS FFF CE  1 
ATOM   12913 N NZ  . LYS H 2 212 ? 55.008  53.453  28.111  1.000 75.489  ? 212 LYS FFF NZ  1 
ATOM   12914 N N   . VAL H 2 213 ? 61.197  51.845  31.784  1.000 40.081  ? 213 VAL FFF N   1 
ATOM   12915 C CA  . VAL H 2 213 ? 61.772  51.066  32.909  1.000 39.597  ? 213 VAL FFF CA  1 
ATOM   12916 C C   . VAL H 2 213 ? 61.251  51.652  34.212  1.000 41.417  ? 213 VAL FFF C   1 
ATOM   12917 O O   . VAL H 2 213 ? 61.341  52.877  34.368  1.000 40.022  ? 213 VAL FFF O   1 
ATOM   12918 C CB  . VAL H 2 213 ? 63.305  51.078  32.893  1.000 38.682  ? 213 VAL FFF CB  1 
ATOM   12919 C CG1 . VAL H 2 213 ? 63.863  50.459  34.155  1.000 38.219  ? 213 VAL FFF CG1 1 
ATOM   12920 C CG2 . VAL H 2 213 ? 63.869  50.386  31.665  1.000 40.867  ? 213 VAL FFF CG2 1 
ATOM   12921 N N   . ASP H 2 214 ? 60.733  50.796  35.096  1.000 45.108  ? 214 ASP FFF N   1 
ATOM   12922 C CA  . ASP H 2 214 ? 60.366  51.131  36.498  1.000 47.392  ? 214 ASP FFF CA  1 
ATOM   12923 C C   . ASP H 2 214 ? 61.314  50.349  37.400  1.000 44.428  ? 214 ASP FFF C   1 
ATOM   12924 O O   . ASP H 2 214 ? 61.312  49.127  37.314  1.000 53.066  ? 214 ASP FFF O   1 
ATOM   12925 C CB  . ASP H 2 214 ? 58.901  50.823  36.810  1.000 50.031  ? 214 ASP FFF CB  1 
ATOM   12926 C CG  . ASP H 2 214 ? 57.885  51.615  35.992  1.000 56.155  ? 214 ASP FFF CG  1 
ATOM   12927 O OD1 . ASP H 2 214 ? 58.174  52.766  35.597  1.000 56.457  ? 214 ASP FFF OD1 1 
ATOM   12928 O OD2 . ASP H 2 214 ? 56.805  51.060  35.739  1.000 76.229  ? 214 ASP FFF OD2 1 
ATOM   12929 N N   . LYS H 2 215 ? 62.166  51.041  38.148  1.000 44.444  ? 215 LYS FFF N   1 
ATOM   12930 C CA  . LYS H 2 215 ? 63.235  50.415  38.957  1.000 47.686  ? 215 LYS FFF CA  1 
ATOM   12931 C C   . LYS H 2 215 ? 62.932  50.676  40.426  1.000 45.241  ? 215 LYS FFF C   1 
ATOM   12932 O O   . LYS H 2 215 ? 62.783  51.852  40.794  1.000 41.313  ? 215 LYS FFF O   1 
ATOM   12933 C CB  . LYS H 2 215 ? 64.615  50.958  38.582  1.000 51.969  ? 215 LYS FFF CB  1 
ATOM   12934 C CG  . LYS H 2 215 ? 65.782  50.240  39.244  1.000 56.211  ? 215 LYS FFF CG  1 
ATOM   12935 C CD  . LYS H 2 215 ? 65.817  48.788  38.879  1.000 63.119  ? 215 LYS FFF CD  1 
ATOM   12936 C CE  . LYS H 2 215 ? 67.004  48.066  39.470  1.000 71.350  ? 215 LYS FFF CE  1 
ATOM   12937 N NZ  . LYS H 2 215 ? 67.443  46.942  38.608  1.000 76.315  ? 215 LYS FFF NZ  1 
ATOM   12938 N N   . LYS H 2 216 ? 62.830  49.604  41.207  1.000 44.364  ? 216 LYS FFF N   1 
ATOM   12939 C CA  . LYS H 2 216 ? 62.566  49.711  42.655  1.000 46.145  ? 216 LYS FFF CA  1 
ATOM   12940 C C   . LYS H 2 216 ? 63.897  49.896  43.381  1.000 44.885  ? 216 LYS FFF C   1 
ATOM   12941 O O   . LYS H 2 216 ? 64.839  49.120  43.152  1.000 46.451  ? 216 LYS FFF O   1 
ATOM   12942 C CB  . LYS H 2 216 ? 61.823  48.480  43.157  1.000 49.505  ? 216 LYS FFF CB  1 
ATOM   12943 C CG  . LYS H 2 216 ? 61.526  48.523  44.642  1.000 53.651  ? 216 LYS FFF CG  1 
ATOM   12944 C CD  . LYS H 2 216 ? 60.356  47.633  45.004  1.000 59.675  ? 216 LYS FFF CD  1 
ATOM   12945 C CE  . LYS H 2 216 ? 60.205  47.472  46.498  1.000 66.872  ? 216 LYS FFF CE  1 
ATOM   12946 N NZ  . LYS H 2 216 ? 59.418  46.261  46.811  1.000 69.786  ? 216 LYS FFF NZ  1 
ATOM   12947 N N   . VAL H 2 217 ? 63.975  50.932  44.195  1.000 40.858  ? 217 VAL FFF N   1 
ATOM   12948 C CA  . VAL H 2 217 ? 65.184  51.267  44.980  1.000 39.089  ? 217 VAL FFF CA  1 
ATOM   12949 C C   . VAL H 2 217 ? 64.859  50.906  46.423  1.000 42.862  ? 217 VAL FFF C   1 
ATOM   12950 O O   . VAL H 2 217 ? 63.857  51.461  46.952  1.000 39.791  ? 217 VAL FFF O   1 
ATOM   12951 C CB  . VAL H 2 217 ? 65.519  52.758  44.812  1.000 38.534  ? 217 VAL FFF CB  1 
ATOM   12952 C CG1 . VAL H 2 217 ? 66.739  53.173  45.616  1.000 40.898  ? 217 VAL FFF CG1 1 
ATOM   12953 C CG2 . VAL H 2 217 ? 65.693  53.130  43.346  1.000 37.008  ? 217 VAL FFF CG2 1 
ATOM   12954 N N   . GLU H 2 218 ? 65.621  49.972  47.005  1.000 49.805  ? 218 GLU FFF N   1 
ATOM   12955 C CA  . GLU H 2 218 ? 65.471  49.574  48.435  1.000 54.649  ? 218 GLU FFF CA  1 
ATOM   12956 C C   . GLU H 2 218 ? 66.840  49.355  49.067  1.000 56.123  ? 218 GLU FFF C   1 
ATOM   12957 O O   . GLU H 2 218 ? 67.817  49.147  48.352  1.000 52.926  ? 218 GLU FFF O   1 
ATOM   12958 C CB  . GLU H 2 218 ? 64.575  48.337  48.572  1.000 59.625  ? 218 GLU FFF CB  1 
ATOM   12959 C CG  . GLU H 2 218 ? 65.072  47.090  47.862  1.000 63.438  ? 218 GLU FFF CG  1 
ATOM   12960 C CD  . GLU H 2 218 ? 64.021  45.993  47.727  1.000 70.509  ? 218 GLU FFF CD  1 
ATOM   12961 O OE1 . GLU H 2 218 ? 62.870  46.162  48.241  1.000 64.224  ? 218 GLU FFF OE1 1 
ATOM   12962 O OE2 . GLU H 2 218 ? 64.351  44.963  47.107  1.000 78.889  ? 218 GLU FFF OE2 1 
ATOM   12963 N N   . PRO H 2 219 ? 66.929  49.418  50.417  1.000 63.963  ? 219 PRO FFF N   1 
ATOM   12964 C CA  . PRO H 2 219 ? 68.209  49.358  51.121  1.000 73.165  ? 219 PRO FFF CA  1 
ATOM   12965 C C   . PRO H 2 219 ? 68.942  48.051  50.810  1.000 80.345  ? 219 PRO FFF C   1 
ATOM   12966 O O   . PRO H 2 219 ? 68.323  47.026  50.874  1.000 74.611  ? 219 PRO FFF O   1 
ATOM   12967 C CB  . PRO H 2 219 ? 67.861  49.468  52.615  1.000 70.771  ? 219 PRO FFF CB  1 
ATOM   12968 C CG  . PRO H 2 219 ? 66.444  50.006  52.638  1.000 66.649  ? 219 PRO FFF CG  1 
ATOM   12969 C CD  . PRO H 2 219 ? 65.799  49.544  51.350  1.000 62.873  ? 219 PRO FFF CD  1 
ATOM   12970 N N   . LYS H 2 220 ? 70.229  48.140  50.471  1.000 95.079  ? 220 LYS FFF N   1 
ATOM   12971 C CA  . LYS H 2 220 ? 71.051  46.978  50.035  1.000 104.824 ? 220 LYS FFF CA  1 
ATOM   12972 C C   . LYS H 2 220 ? 71.148  45.983  51.201  1.000 112.775 ? 220 LYS FFF C   1 
ATOM   12973 O O   . LYS H 2 220 ? 71.287  46.442  52.340  1.000 118.942 ? 220 LYS FFF O   1 
ATOM   12974 C CB  . LYS H 2 220 ? 72.430  47.444  49.550  1.000 107.737 ? 220 LYS FFF CB  1 
ATOM   12975 C CG  . LYS H 2 220 ? 73.129  46.495  48.582  1.000 108.475 ? 220 LYS FFF CG  1 
ATOM   12976 C CD  . LYS H 2 220 ? 74.645  46.668  48.539  1.000 112.259 ? 220 LYS FFF CD  1 
ATOM   12977 C CE  . LYS H 2 220 ? 75.338  45.690  47.614  1.000 104.009 ? 220 LYS FFF CE  1 
ATOM   12978 N NZ  . LYS H 2 220 ? 75.196  46.108  46.200  1.000 106.863 ? 220 LYS FFF NZ  1 
ATOM   12979 N N   . SER H 2 221 ? 71.024  44.678  50.933  1.000 121.229 ? 221 SER FFF N   1 
ATOM   12980 C CA  . SER H 2 221 ? 71.360  43.573  51.878  1.000 127.392 ? 221 SER FFF CA  1 
ATOM   12981 C C   . SER H 2 221 ? 72.804  43.762  52.364  1.000 167.455 ? 221 SER FFF C   1 
ATOM   12982 O O   . SER H 2 221 ? 73.004  43.946  53.575  1.000 176.637 ? 221 SER FFF O   1 
ATOM   12983 C CB  . SER H 2 221 ? 71.182  42.214  51.239  1.000 109.896 ? 221 SER FFF CB  1 
ATOM   12984 O OG  . SER H 2 221 ? 69.812  41.889  51.115  1.000 101.908 ? 221 SER FFF OG  1 
ATOM   12985 N N   . CYS H 2 222 ? 73.751  43.710  51.417  1.000 204.651 ? 222 CYS FFF N   1 
ATOM   12986 C CA  . CYS H 2 222 ? 75.237  43.823  51.557  1.000 206.959 ? 222 CYS FFF CA  1 
ATOM   12987 C C   . CYS H 2 222 ? 75.776  42.734  52.490  1.000 204.519 ? 222 CYS FFF C   1 
ATOM   12988 O O   . CYS H 2 222 ? 75.063  41.819  52.900  1.000 200.071 ? 222 CYS FFF O   1 
ATOM   12989 C CB  . CYS H 2 222 ? 75.677  45.223  51.991  1.000 208.963 ? 222 CYS FFF CB  1 
ATOM   12990 S SG  . CYS H 2 222 ? 75.967  45.447  53.768  1.000 197.630 ? 222 CYS FFF SG  1 
ATOM   12991 O OXT . CYS H 2 222 ? 76.958  42.764  52.820  1.000 195.247 ? 222 CYS FFF OXT 1 
ATOM   12992 N N   . ASP I 3 1   ? 79.076  96.816  11.673  1.000 99.207  ? 1   ASP GGG N   1 
ATOM   12993 C CA  . ASP I 3 1   ? 79.147  95.544  12.454  1.000 95.631  ? 1   ASP GGG CA  1 
ATOM   12994 C C   . ASP I 3 1   ? 79.401  95.899  13.925  1.000 85.017  ? 1   ASP GGG C   1 
ATOM   12995 O O   . ASP I 3 1   ? 80.587  96.041  14.331  1.000 77.201  ? 1   ASP GGG O   1 
ATOM   12996 C CB  . ASP I 3 1   ? 80.190  94.596  11.856  1.000 103.530 ? 1   ASP GGG CB  1 
ATOM   12997 C CG  . ASP I 3 1   ? 79.701  93.168  11.720  1.000 108.406 ? 1   ASP GGG CG  1 
ATOM   12998 O OD1 . ASP I 3 1   ? 79.384  92.776  10.579  1.000 109.326 ? 1   ASP GGG OD1 1 
ATOM   12999 O OD2 . ASP I 3 1   ? 79.627  92.469  12.757  1.000 113.779 ? 1   ASP GGG OD2 1 
ATOM   13000 N N   . ILE I 3 2   ? 78.309  96.093  14.669  1.000 74.200  ? 2   ILE GGG N   1 
ATOM   13001 C CA  . ILE I 3 2   ? 78.301  96.547  16.088  1.000 73.397  ? 2   ILE GGG CA  1 
ATOM   13002 C C   . ILE I 3 2   ? 78.521  95.336  16.980  1.000 76.234  ? 2   ILE GGG C   1 
ATOM   13003 O O   . ILE I 3 2   ? 78.028  94.255  16.650  1.000 100.905 ? 2   ILE GGG O   1 
ATOM   13004 C CB  . ILE I 3 2   ? 76.975  97.247  16.434  1.000 71.466  ? 2   ILE GGG CB  1 
ATOM   13005 C CG1 . ILE I 3 2   ? 76.748  98.438  15.500  1.000 69.323  ? 2   ILE GGG CG1 1 
ATOM   13006 C CG2 . ILE I 3 2   ? 76.940  97.649  17.906  1.000 71.801  ? 2   ILE GGG CG2 1 
ATOM   13007 C CD1 . ILE I 3 2   ? 75.389  99.093  15.636  1.000 66.757  ? 2   ILE GGG CD1 1 
ATOM   13008 N N   . GLN I 3 3   ? 79.196  95.546  18.093  1.000 72.153  ? 3   GLN GGG N   1 
ATOM   13009 C CA  . GLN I 3 3   ? 79.509  94.479  19.059  1.000 78.936  ? 3   GLN GGG CA  1 
ATOM   13010 C C   . GLN I 3 3   ? 79.046  94.988  20.425  1.000 73.012  ? 3   GLN GGG C   1 
ATOM   13011 O O   . GLN I 3 3   ? 79.173  96.177  20.672  1.000 70.121  ? 3   GLN GGG O   1 
ATOM   13012 C CB  . GLN I 3 3   ? 80.993  94.153  18.917  1.000 86.804  ? 3   GLN GGG CB  1 
ATOM   13013 C CG  . GLN I 3 3   ? 81.423  93.000  19.794  1.000 100.463 ? 3   GLN GGG CG  1 
ATOM   13014 C CD  . GLN I 3 3   ? 82.879  92.682  19.587  1.000 112.896 ? 3   GLN GGG CD  1 
ATOM   13015 O OE1 . GLN I 3 3   ? 83.723  93.563  19.409  1.000 120.306 ? 3   GLN GGG OE1 1 
ATOM   13016 N NE2 . GLN I 3 3   ? 83.177  91.399  19.612  1.000 115.235 ? 3   GLN GGG NE2 1 
ATOM   13017 N N   . LEU I 3 4   ? 78.448  94.132  21.251  1.000 67.197  ? 4   LEU GGG N   1 
ATOM   13018 C CA  . LEU I 3 4   ? 78.004  94.508  22.613  1.000 64.776  ? 4   LEU GGG CA  1 
ATOM   13019 C C   . LEU I 3 4   ? 78.880  93.768  23.631  1.000 65.032  ? 4   LEU GGG C   1 
ATOM   13020 O O   . LEU I 3 4   ? 79.260  92.622  23.364  1.000 60.422  ? 4   LEU GGG O   1 
ATOM   13021 C CB  . LEU I 3 4   ? 76.526  94.156  22.787  1.000 62.910  ? 4   LEU GGG CB  1 
ATOM   13022 C CG  . LEU I 3 4   ? 75.569  94.724  21.737  1.000 62.498  ? 4   LEU GGG CG  1 
ATOM   13023 C CD1 . LEU I 3 4   ? 74.118  94.324  22.003  1.000 62.255  ? 4   LEU GGG CD1 1 
ATOM   13024 C CD2 . LEU I 3 4   ? 75.660  96.230  21.679  1.000 64.917  ? 4   LEU GGG CD2 1 
ATOM   13025 N N   . THR I 3 5   ? 79.201  94.417  24.748  1.000 65.291  ? 5   THR GGG N   1 
ATOM   13026 C CA  . THR I 3 5   ? 79.777  93.770  25.952  1.000 68.351  ? 5   THR GGG CA  1 
ATOM   13027 C C   . THR I 3 5   ? 78.832  94.021  27.125  1.000 70.180  ? 5   THR GGG C   1 
ATOM   13028 O O   . THR I 3 5   ? 78.613  95.196  27.470  1.000 62.106  ? 5   THR GGG O   1 
ATOM   13029 C CB  . THR I 3 5   ? 81.188  94.284  26.265  1.000 69.538  ? 5   THR GGG CB  1 
ATOM   13030 O OG1 . THR I 3 5   ? 81.835  94.554  25.021  1.000 78.557  ? 5   THR GGG OG1 1 
ATOM   13031 C CG2 . THR I 3 5   ? 82.002  93.306  27.087  1.000 68.100  ? 5   THR GGG CG2 1 
ATOM   13032 N N   . GLN I 3 6   ? 78.282  92.953  27.702  1.000 73.825  ? 6   GLN GGG N   1 
ATOM   13033 C CA  . GLN I 3 6   ? 77.510  93.019  28.971  1.000 69.001  ? 6   GLN GGG CA  1 
ATOM   13034 C C   . GLN I 3 6   ? 78.478  92.882  30.141  1.000 67.790  ? 6   GLN GGG C   1 
ATOM   13035 O O   . GLN I 3 6   ? 79.577  92.350  29.938  1.000 68.872  ? 6   GLN GGG O   1 
ATOM   13036 C CB  . GLN I 3 6   ? 76.473  91.906  29.079  1.000 69.084  ? 6   GLN GGG CB  1 
ATOM   13037 C CG  . GLN I 3 6   ? 75.163  92.222  28.387  1.000 65.540  ? 6   GLN GGG CG  1 
ATOM   13038 C CD  . GLN I 3 6   ? 74.233  91.054  28.567  1.000 65.149  ? 6   GLN GGG CD  1 
ATOM   13039 O OE1 . GLN I 3 6   ? 74.099  90.221  27.674  1.000 70.193  ? 6   GLN GGG OE1 1 
ATOM   13040 N NE2 . GLN I 3 6   ? 73.663  90.944  29.757  1.000 58.979  ? 6   GLN GGG NE2 1 
ATOM   13041 N N   . SER I 3 7   ? 78.051  93.327  31.320  1.000 67.120  ? 7   SER GGG N   1 
ATOM   13042 C CA  . SER I 3 7   ? 78.763  93.134  32.607  1.000 69.734  ? 7   SER GGG CA  1 
ATOM   13043 C C   . SER I 3 7   ? 77.784  93.359  33.756  1.000 69.820  ? 7   SER GGG C   1 
ATOM   13044 O O   . SER I 3 7   ? 76.885  94.189  33.644  1.000 65.904  ? 7   SER GGG O   1 
ATOM   13045 C CB  . SER I 3 7   ? 79.948  94.052  32.708  1.000 65.500  ? 7   SER GGG CB  1 
ATOM   13046 O OG  . SER I 3 7   ? 79.503  95.397  32.676  1.000 66.451  ? 7   SER GGG OG  1 
ATOM   13047 N N   . PRO I 3 8   ? 77.912  92.618  34.878  1.000 70.442  ? 8   PRO GGG N   1 
ATOM   13048 C CA  . PRO I 3 8   ? 78.830  91.475  34.959  1.000 71.024  ? 8   PRO GGG CA  1 
ATOM   13049 C C   . PRO I 3 8   ? 78.330  90.214  34.228  1.000 70.550  ? 8   PRO GGG C   1 
ATOM   13050 O O   . PRO I 3 8   ? 77.240  90.227  33.703  1.000 69.945  ? 8   PRO GGG O   1 
ATOM   13051 C CB  . PRO I 3 8   ? 78.927  91.229  36.472  1.000 71.332  ? 8   PRO GGG CB  1 
ATOM   13052 C CG  . PRO I 3 8   ? 77.597  91.717  37.021  1.000 72.192  ? 8   PRO GGG CG  1 
ATOM   13053 C CD  . PRO I 3 8   ? 77.215  92.891  36.143  1.000 67.231  ? 8   PRO GGG CD  1 
ATOM   13054 N N   . ASP I 3 9   ? 79.139  89.155  34.202  1.000 71.058  ? 9   ASP GGG N   1 
ATOM   13055 C CA  . ASP I 3 9   ? 78.751  87.839  33.625  1.000 72.731  ? 9   ASP GGG CA  1 
ATOM   13056 C C   . ASP I 3 9   ? 77.738  87.176  34.564  1.000 66.670  ? 9   ASP GGG C   1 
ATOM   13057 O O   . ASP I 3 9   ? 76.716  86.644  34.099  1.000 64.260  ? 9   ASP GGG O   1 
ATOM   13058 C CB  . ASP I 3 9   ? 79.970  86.934  33.431  1.000 78.513  ? 9   ASP GGG CB  1 
ATOM   13059 C CG  . ASP I 3 9   ? 81.055  87.528  32.540  1.000 82.390  ? 9   ASP GGG CG  1 
ATOM   13060 O OD1 . ASP I 3 9   ? 82.189  87.704  33.046  1.000 86.167  ? 9   ASP GGG OD1 1 
ATOM   13061 O OD2 . ASP I 3 9   ? 80.763  87.807  31.345  1.000 72.627  ? 9   ASP GGG OD2 1 
ATOM   13062 N N   . SER I 3 10  ? 78.039  87.230  35.856  1.000 63.748  ? 10  SER GGG N   1 
ATOM   13063 C CA  . SER I 3 10  ? 77.318  86.553  36.957  1.000 63.099  ? 10  SER GGG CA  1 
ATOM   13064 C C   . SER I 3 10  ? 76.923  87.611  37.987  1.000 63.103  ? 10  SER GGG C   1 
ATOM   13065 O O   . SER I 3 10  ? 77.674  88.579  38.147  1.000 69.828  ? 10  SER GGG O   1 
ATOM   13066 C CB  . SER I 3 10  ? 78.192  85.486  37.560  1.000 64.077  ? 10  SER GGG CB  1 
ATOM   13067 O OG  . SER I 3 10  ? 77.449  84.749  38.511  1.000 78.401  ? 10  SER GGG OG  1 
ATOM   13068 N N   . LEU I 3 11  ? 75.801  87.448  38.680  1.000 60.914  ? 11  LEU GGG N   1 
ATOM   13069 C CA  . LEU I 3 11  ? 75.308  88.480  39.620  1.000 60.645  ? 11  LEU GGG CA  1 
ATOM   13070 C C   . LEU I 3 11  ? 74.343  87.842  40.615  1.000 65.953  ? 11  LEU GGG C   1 
ATOM   13071 O O   . LEU I 3 11  ? 73.296  87.336  40.167  1.000 79.462  ? 11  LEU GGG O   1 
ATOM   13072 C CB  . LEU I 3 11  ? 74.596  89.540  38.787  1.000 62.711  ? 11  LEU GGG CB  1 
ATOM   13073 C CG  . LEU I 3 11  ? 73.898  90.640  39.571  1.000 65.374  ? 11  LEU GGG CG  1 
ATOM   13074 C CD1 . LEU I 3 11  ? 74.904  91.414  40.404  1.000 68.920  ? 11  LEU GGG CD1 1 
ATOM   13075 C CD2 . LEU I 3 11  ? 73.149  91.564  38.621  1.000 64.947  ? 11  LEU GGG CD2 1 
ATOM   13076 N N   . ALA I 3 12  ? 74.663  87.873  41.908  1.000 64.654  ? 12  ALA GGG N   1 
ATOM   13077 C CA  . ALA I 3 12  ? 73.825  87.266  42.972  1.000 63.780  ? 12  ALA GGG CA  1 
ATOM   13078 C C   . ALA I 3 12  ? 73.303  88.362  43.898  1.000 56.590  ? 12  ALA GGG C   1 
ATOM   13079 O O   . ALA I 3 12  ? 74.090  89.202  44.306  1.000 53.127  ? 12  ALA GGG O   1 
ATOM   13080 C CB  . ALA I 3 12  ? 74.598  86.221  43.740  1.000 70.536  ? 12  ALA GGG CB  1 
ATOM   13081 N N   . VAL I 3 13  ? 72.012  88.332  44.206  1.000 54.322  ? 13  VAL GGG N   1 
ATOM   13082 C CA  . VAL I 3 13  ? 71.271  89.463  44.825  1.000 56.645  ? 13  VAL GGG CA  1 
ATOM   13083 C C   . VAL I 3 13  ? 70.184  88.912  45.741  1.000 57.383  ? 13  VAL GGG C   1 
ATOM   13084 O O   . VAL I 3 13  ? 69.432  88.048  45.282  1.000 59.063  ? 13  VAL GGG O   1 
ATOM   13085 C CB  . VAL I 3 13  ? 70.643  90.320  43.719  1.000 59.119  ? 13  VAL GGG CB  1 
ATOM   13086 C CG1 . VAL I 3 13  ? 69.657  91.326  44.296  1.000 64.555  ? 13  VAL GGG CG1 1 
ATOM   13087 C CG2 . VAL I 3 13  ? 71.704  90.997  42.863  1.000 59.477  ? 13  VAL GGG CG2 1 
ATOM   13088 N N   . SER I 3 14  ? 70.083  89.419  46.969  1.000 60.644  ? 14  SER GGG N   1 
ATOM   13089 C CA  . SER I 3 14  ? 69.096  88.963  47.985  1.000 64.789  ? 14  SER GGG CA  1 
ATOM   13090 C C   . SER I 3 14  ? 67.676  89.263  47.491  1.000 61.661  ? 14  SER GGG C   1 
ATOM   13091 O O   . SER I 3 14  ? 67.531  90.092  46.590  1.000 57.818  ? 14  SER GGG O   1 
ATOM   13092 C CB  . SER I 3 14  ? 69.379  89.592  49.319  1.000 70.191  ? 14  SER GGG CB  1 
ATOM   13093 O OG  . SER I 3 14  ? 70.750  89.425  49.660  1.000 75.852  ? 14  SER GGG OG  1 
ATOM   13094 N N   . LEU I 3 15  ? 66.671  88.572  48.021  1.000 62.045  ? 15  LEU GGG N   1 
ATOM   13095 C CA  . LEU I 3 15  ? 65.257  88.800  47.633  1.000 64.666  ? 15  LEU GGG CA  1 
ATOM   13096 C C   . LEU I 3 15  ? 64.883  90.231  48.007  1.000 69.887  ? 15  LEU GGG C   1 
ATOM   13097 O O   . LEU I 3 15  ? 65.185  90.657  49.128  1.000 70.962  ? 15  LEU GGG O   1 
ATOM   13098 C CB  . LEU I 3 15  ? 64.345  87.791  48.336  1.000 67.108  ? 15  LEU GGG CB  1 
ATOM   13099 C CG  . LEU I 3 15  ? 64.202  86.443  47.638  1.000 70.762  ? 15  LEU GGG CG  1 
ATOM   13100 C CD1 . LEU I 3 15  ? 63.614  85.400  48.585  1.000 68.973  ? 15  LEU GGG CD1 1 
ATOM   13101 C CD2 . LEU I 3 15  ? 63.346  86.596  46.390  1.000 72.502  ? 15  LEU GGG CD2 1 
ATOM   13102 N N   . GLY I 3 16  ? 64.275  90.952  47.073  1.000 80.591  ? 16  GLY GGG N   1 
ATOM   13103 C CA  . GLY I 3 16  ? 63.776  92.322  47.286  1.000 82.488  ? 16  GLY GGG CA  1 
ATOM   13104 C C   . GLY I 3 16  ? 64.864  93.377  47.128  1.000 82.401  ? 16  GLY GGG C   1 
ATOM   13105 O O   . GLY I 3 16  ? 64.557  94.546  47.415  1.000 96.650  ? 16  GLY GGG O   1 
ATOM   13106 N N   . GLU I 3 17  ? 66.078  93.010  46.695  1.000 72.188  ? 17  GLU GGG N   1 
ATOM   13107 C CA  . GLU I 3 17  ? 67.203  93.967  46.480  1.000 71.616  ? 17  GLU GGG CA  1 
ATOM   13108 C C   . GLU I 3 17  ? 67.259  94.359  44.999  1.000 69.466  ? 17  GLU GGG C   1 
ATOM   13109 O O   . GLU I 3 17  ? 66.460  93.820  44.217  1.000 63.731  ? 17  GLU GGG O   1 
ATOM   13110 C CB  . GLU I 3 17  ? 68.554  93.382  46.907  1.000 75.343  ? 17  GLU GGG CB  1 
ATOM   13111 C CG  . GLU I 3 17  ? 68.706  93.167  48.402  1.000 83.026  ? 17  GLU GGG CG  1 
ATOM   13112 C CD  . GLU I 3 17  ? 68.434  94.371  49.286  1.000 85.332  ? 17  GLU GGG CD  1 
ATOM   13113 O OE1 . GLU I 3 17  ? 69.372  95.160  49.514  1.000 89.139  ? 17  GLU GGG OE1 1 
ATOM   13114 O OE2 . GLU I 3 17  ? 67.283  94.509  49.749  1.000 88.054  ? 17  GLU GGG OE2 1 
ATOM   13115 N N   . ARG I 3 18  ? 68.170  95.272  44.656  1.000 69.280  ? 18  ARG GGG N   1 
ATOM   13116 C CA  . ARG I 3 18  ? 68.338  95.849  43.297  1.000 74.164  ? 18  ARG GGG CA  1 
ATOM   13117 C C   . ARG I 3 18  ? 69.402  95.041  42.550  1.000 71.219  ? 18  ARG GGG C   1 
ATOM   13118 O O   . ARG I 3 18  ? 70.477  94.782  43.132  1.000 68.496  ? 18  ARG GGG O   1 
ATOM   13119 C CB  . ARG I 3 18  ? 68.673  97.341  43.414  1.000 85.191  ? 18  ARG GGG CB  1 
ATOM   13120 C CG  . ARG I 3 18  ? 69.896  97.843  42.643  1.000 96.104  ? 18  ARG GGG CG  1 
ATOM   13121 C CD  . ARG I 3 18  ? 70.173  99.311  42.936  1.000 101.498 ? 18  ARG GGG CD  1 
ATOM   13122 N NE  . ARG I 3 18  ? 68.890  99.993  43.086  1.000 108.787 ? 18  ARG GGG NE  1 
ATOM   13123 C CZ  . ARG I 3 18  ? 68.209  100.593 42.110  1.000 109.206 ? 18  ARG GGG CZ  1 
ATOM   13124 N NH1 . ARG I 3 18  ? 68.700  100.680 40.885  1.000 117.313 ? 18  ARG GGG NH1 1 
ATOM   13125 N NH2 . ARG I 3 18  ? 67.038  101.138 42.381  1.000 103.604 ? 18  ARG GGG NH2 1 
ATOM   13126 N N   . ALA I 3 19  ? 69.106  94.650  41.310  1.000 67.269  ? 19  ALA GGG N   1 
ATOM   13127 C CA  . ALA I 3 19  ? 70.064  94.037  40.364  1.000 62.425  ? 19  ALA GGG CA  1 
ATOM   13128 C C   . ALA I 3 19  ? 70.209  94.960  39.156  1.000 59.261  ? 19  ALA GGG C   1 
ATOM   13129 O O   . ALA I 3 19  ? 69.170  95.332  38.563  1.000 46.751  ? 19  ALA GGG O   1 
ATOM   13130 C CB  . ALA I 3 19  ? 69.592  92.668  39.947  1.000 66.787  ? 19  ALA GGG CB  1 
ATOM   13131 N N   . THR I 3 20  ? 71.450  95.309  38.820  1.000 60.485  ? 20  THR GGG N   1 
ATOM   13132 C CA  . THR I 3 20  ? 71.793  96.251  37.724  1.000 64.250  ? 20  THR GGG CA  1 
ATOM   13133 C C   . THR I 3 20  ? 72.756  95.531  36.777  1.000 58.161  ? 20  THR GGG C   1 
ATOM   13134 O O   . THR I 3 20  ? 73.732  94.931  37.266  1.000 51.501  ? 20  THR GGG O   1 
ATOM   13135 C CB  . THR I 3 20  ? 72.339  97.573  38.291  1.000 65.127  ? 20  THR GGG CB  1 
ATOM   13136 O OG1 . THR I 3 20  ? 73.128  97.246  39.431  1.000 64.700  ? 20  THR GGG OG1 1 
ATOM   13137 C CG2 . THR I 3 20  ? 71.270  98.549  38.735  1.000 63.574  ? 20  THR GGG CG2 1 
ATOM   13138 N N   . ILE I 3 21  ? 72.438  95.561  35.483  1.000 55.839  ? 21  ILE GGG N   1 
ATOM   13139 C CA  . ILE I 3 21  ? 73.196  94.892  34.391  1.000 56.948  ? 21  ILE GGG CA  1 
ATOM   13140 C C   . ILE I 3 21  ? 73.561  95.975  33.373  1.000 54.518  ? 21  ILE GGG C   1 
ATOM   13141 O O   . ILE I 3 21  ? 72.666  96.752  33.019  1.000 50.061  ? 21  ILE GGG O   1 
ATOM   13142 C CB  . ILE I 3 21  ? 72.363  93.748  33.772  1.000 59.493  ? 21  ILE GGG CB  1 
ATOM   13143 C CG1 . ILE I 3 21  ? 71.832  92.790  34.846  1.000 60.872  ? 21  ILE GGG CG1 1 
ATOM   13144 C CG2 . ILE I 3 21  ? 73.155  93.016  32.699  1.000 59.809  ? 21  ILE GGG CG2 1 
ATOM   13145 C CD1 . ILE I 3 21  ? 70.840  91.753  34.327  1.000 61.247  ? 21  ILE GGG CD1 1 
ATOM   13146 N N   . ASN I 3 22  ? 74.816  96.002  32.918  1.000 59.621  ? 22  ASN GGG N   1 
ATOM   13147 C CA  . ASN I 3 22  ? 75.365  97.043  32.006  1.000 63.572  ? 22  ASN GGG CA  1 
ATOM   13148 C C   . ASN I 3 22  ? 75.646  96.455  30.616  1.000 68.030  ? 22  ASN GGG C   1 
ATOM   13149 O O   . ASN I 3 22  ? 76.262  95.367  30.557  1.000 73.670  ? 22  ASN GGG O   1 
ATOM   13150 C CB  . ASN I 3 22  ? 76.636  97.668  32.585  1.000 66.375  ? 22  ASN GGG CB  1 
ATOM   13151 C CG  . ASN I 3 22  ? 76.354  98.553  33.778  1.000 68.842  ? 22  ASN GGG CG  1 
ATOM   13152 O OD1 . ASN I 3 22  ? 75.368  99.293  33.802  1.000 73.970  ? 22  ASN GGG OD1 1 
ATOM   13153 N ND2 . ASN I 3 22  ? 77.228  98.488  34.766  1.000 67.890  ? 22  ASN GGG ND2 1 
ATOM   13154 N N   . CYS I 3 23  ? 75.218  97.167  29.559  1.000 68.141  ? 23  CYS GGG N   1 
ATOM   13155 C CA  . CYS I 3 23  ? 75.503  96.891  28.121  1.000 75.263  ? 23  CYS GGG CA  1 
ATOM   13156 C C   . CYS I 3 23  ? 76.323  98.053  27.547  1.000 73.756  ? 23  CYS GGG C   1 
ATOM   13157 O O   . CYS I 3 23  ? 75.875  99.192  27.628  1.000 69.989  ? 23  CYS GGG O   1 
ATOM   13158 C CB  . CYS I 3 23  ? 74.214  96.687  27.325  1.000 81.975  ? 23  CYS GGG CB  1 
ATOM   13159 S SG  . CYS I 3 23  ? 74.423  95.908  25.693  1.000 104.575 ? 23  CYS GGG SG  1 
ATOM   13160 N N   . LYS I 3 24  ? 77.512  97.758  27.033  1.000 81.090  ? 24  LYS GGG N   1 
ATOM   13161 C CA  . LYS I 3 24  ? 78.410  98.717  26.343  1.000 83.218  ? 24  LYS GGG CA  1 
ATOM   13162 C C   . LYS I 3 24  ? 78.401  98.350  24.858  1.000 83.834  ? 24  LYS GGG C   1 
ATOM   13163 O O   . LYS I 3 24  ? 78.799  97.213  24.545  1.000 92.247  ? 24  LYS GGG O   1 
ATOM   13164 C CB  . LYS I 3 24  ? 79.824  98.607  26.922  1.000 95.418  ? 24  LYS GGG CB  1 
ATOM   13165 C CG  . LYS I 3 24  ? 80.565  99.920  27.125  1.000 100.732 ? 24  LYS GGG CG  1 
ATOM   13166 C CD  . LYS I 3 24  ? 81.913  99.757  27.823  1.000 104.652 ? 24  LYS GGG CD  1 
ATOM   13167 C CE  . LYS I 3 24  ? 82.081  100.647 29.040  1.000 102.584 ? 24  LYS GGG CE  1 
ATOM   13168 N NZ  . LYS I 3 24  ? 82.020  102.089 28.700  1.000 99.348  ? 24  LYS GGG NZ  1 
ATOM   13169 N N   . SER I 3 25  ? 77.937  99.247  23.987  1.000 78.093  ? 25  SER GGG N   1 
ATOM   13170 C CA  . SER I 3 25  ? 77.963  99.053  22.513  1.000 78.961  ? 25  SER GGG CA  1 
ATOM   13171 C C   . SER I 3 25  ? 79.240  99.664  21.947  1.000 79.016  ? 25  SER GGG C   1 
ATOM   13172 O O   . SER I 3 25  ? 79.608  100.749 22.393  1.000 87.505  ? 25  SER GGG O   1 
ATOM   13173 C CB  . SER I 3 25  ? 76.734  99.608  21.838  1.000 77.257  ? 25  SER GGG CB  1 
ATOM   13174 O OG  . SER I 3 25  ? 76.552  100.976 22.133  1.000 69.773  ? 25  SER GGG OG  1 
ATOM   13175 N N   . SER I 3 26  ? 79.879  98.982  20.996  1.000 86.230  ? 26  SER GGG N   1 
ATOM   13176 C CA  . SER I 3 26  ? 81.130  99.424  20.327  1.000 87.898  ? 26  SER GGG CA  1 
ATOM   13177 C C   . SER I 3 26  ? 80.858  100.685 19.500  1.000 84.504  ? 26  SER GGG C   1 
ATOM   13178 O O   . SER I 3 26  ? 81.824  101.265 18.998  1.000 87.101  ? 26  SER GGG O   1 
ATOM   13179 C CB  . SER I 3 26  ? 81.712  98.331  19.463  1.000 91.654  ? 26  SER GGG CB  1 
ATOM   13180 O OG  . SER I 3 26  ? 80.863  98.063  18.350  1.000 101.801 ? 26  SER GGG OG  1 
ATOM   13181 N N   . GLN I 3 27  ? 79.599  101.104 19.372  1.000 76.470  ? 27  GLN GGG N   1 
ATOM   13182 C CA  . GLN I 3 27  ? 79.211  102.206 18.463  1.000 76.681  ? 27  GLN GGG CA  1 
ATOM   13183 C C   . GLN I 3 27  ? 77.782  102.640 18.808  1.000 74.042  ? 27  GLN GGG C   1 
ATOM   13184 O O   . GLN I 3 27  ? 77.068  101.846 19.426  1.000 83.595  ? 27  GLN GGG O   1 
ATOM   13185 C CB  . GLN I 3 27  ? 79.411  101.698 17.035  1.000 80.654  ? 27  GLN GGG CB  1 
ATOM   13186 C CG  . GLN I 3 27  ? 78.762  102.544 15.954  1.000 84.785  ? 27  GLN GGG CG  1 
ATOM   13187 C CD  . GLN I 3 27  ? 78.784  101.788 14.649  1.000 89.989  ? 27  GLN GGG CD  1 
ATOM   13188 O OE1 . GLN I 3 27  ? 79.708  101.016 14.382  1.000 77.374  ? 27  GLN GGG OE1 1 
ATOM   13189 N NE2 . GLN I 3 27  ? 77.749  101.994 13.843  1.000 92.609  ? 27  GLN GGG NE2 1 
ATOM   13190 N N   . SER I 3 28  ? 77.396  103.868 18.460  1.000 73.718  ? 28  SER GGG N   1 
ATOM   13191 C CA  . SER I 3 28  ? 76.068  104.443 18.790  1.000 77.900  ? 28  SER GGG CA  1 
ATOM   13192 C C   . SER I 3 28  ? 74.989  103.721 17.982  1.000 86.663  ? 28  SER GGG C   1 
ATOM   13193 O O   . SER I 3 28  ? 75.305  103.207 16.873  1.000 84.021  ? 28  SER GGG O   1 
ATOM   13194 C CB  . SER I 3 28  ? 76.007  105.930 18.558  1.000 78.990  ? 28  SER GGG CB  1 
ATOM   13195 O OG  . SER I 3 28  ? 74.690  106.420 18.798  1.000 73.976  ? 28  SER GGG OG  1 
ATOM   13196 N N   . VAL I 3 29  ? 73.768  103.717 18.531  1.000 96.002  ? 29  VAL GGG N   1 
ATOM   13197 C CA  . VAL I 3 29  ? 72.584  102.947 18.047  1.000 91.434  ? 29  VAL GGG CA  1 
ATOM   13198 C C   . VAL I 3 29  ? 71.365  103.873 18.074  1.000 93.714  ? 29  VAL GGG C   1 
ATOM   13199 O O   . VAL I 3 29  ? 70.232  103.387 18.302  1.000 84.399  ? 29  VAL GGG O   1 
ATOM   13200 C CB  . VAL I 3 29  ? 72.363  101.698 18.918  1.000 87.929  ? 29  VAL GGG CB  1 
ATOM   13201 C CG1 . VAL I 3 29  ? 73.494  100.698 18.736  1.000 90.708  ? 29  VAL GGG CG1 1 
ATOM   13202 C CG2 . VAL I 3 29  ? 72.177  102.051 20.393  1.000 84.648  ? 29  VAL GGG CG2 1 
ATOM   13203 N N   . LEU I 3 30  ? 71.609  105.169 17.875  1.000 102.070 ? 30  LEU GGG N   1 
ATOM   13204 C CA  . LEU I 3 30  ? 70.595  106.250 17.948  1.000 98.682  ? 30  LEU GGG CA  1 
ATOM   13205 C C   . LEU I 3 30  ? 70.044  106.527 16.539  1.000 89.249  ? 30  LEU GGG C   1 
ATOM   13206 O O   . LEU I 3 30  ? 70.830  106.932 15.666  1.000 84.348  ? 30  LEU GGG O   1 
ATOM   13207 C CB  . LEU I 3 30  ? 71.284  107.478 18.559  1.000 103.026 ? 30  LEU GGG CB  1 
ATOM   13208 C CG  . LEU I 3 30  ? 70.368  108.575 19.106  1.000 114.387 ? 30  LEU GGG CG  1 
ATOM   13209 C CD1 . LEU I 3 30  ? 69.849  109.482 17.993  1.000 116.079 ? 30  LEU GGG CD1 1 
ATOM   13210 C CD2 . LEU I 3 30  ? 69.208  107.993 19.907  1.000 118.705 ? 30  LEU GGG CD2 1 
ATOM   13211 N N   . TYR I 3 31  ? 68.753  106.273 16.305  1.000 88.976  ? 31  TYR GGG N   1 
ATOM   13212 C CA  . TYR I 3 31  ? 68.022  106.729 15.090  1.000 92.948  ? 31  TYR GGG CA  1 
ATOM   13213 C C   . TYR I 3 31  ? 67.728  108.217 15.276  1.000 101.712 ? 31  TYR GGG C   1 
ATOM   13214 O O   . TYR I 3 31  ? 67.126  108.628 16.297  1.000 104.857 ? 31  TYR GGG O   1 
ATOM   13215 C CB  . TYR I 3 31  ? 66.736  105.933 14.814  1.000 88.142  ? 31  TYR GGG CB  1 
ATOM   13216 C CG  . TYR I 3 31  ? 66.877  104.826 13.800  1.000 84.804  ? 31  TYR GGG CG  1 
ATOM   13217 C CD1 . TYR I 3 31  ? 67.772  103.793 14.008  1.000 89.196  ? 31  TYR GGG CD1 1 
ATOM   13218 C CD2 . TYR I 3 31  ? 66.128  104.803 12.634  1.000 77.529  ? 31  TYR GGG CD2 1 
ATOM   13219 C CE1 . TYR I 3 31  ? 67.939  102.783 13.077  1.000 89.201  ? 31  TYR GGG CE1 1 
ATOM   13220 C CE2 . TYR I 3 31  ? 66.274  103.798 11.693  1.000 73.649  ? 31  TYR GGG CE2 1 
ATOM   13221 C CZ  . TYR I 3 31  ? 67.187  102.784 11.917  1.000 81.880  ? 31  TYR GGG CZ  1 
ATOM   13222 O OH  . TYR I 3 31  ? 67.363  101.771 11.022  1.000 85.025  ? 31  TYR GGG OH  1 
ATOM   13223 N N   . SER I 3 32  ? 68.178  109.018 14.318  1.000 109.364 ? 32  SER GGG N   1 
ATOM   13224 C CA  . SER I 3 32  ? 68.061  110.494 14.359  1.000 95.878  ? 32  SER GGG CA  1 
ATOM   13225 C C   . SER I 3 32  ? 66.588  110.881 14.198  1.000 89.302  ? 32  SER GGG C   1 
ATOM   13226 O O   . SER I 3 32  ? 66.109  111.707 14.994  1.000 70.971  ? 32  SER GGG O   1 
ATOM   13227 C CB  . SER I 3 32  ? 68.930  111.121 13.323  1.000 88.935  ? 32  SER GGG CB  1 
ATOM   13228 O OG  . SER I 3 32  ? 69.578  112.237 13.892  1.000 89.015  ? 32  SER GGG OG  1 
ATOM   13229 N N   . SER I 3 33  ? 65.894  110.226 13.254  1.000 90.564  ? 33  SER GGG N   1 
ATOM   13230 C CA  . SER I 3 33  ? 64.503  110.515 12.799  1.000 94.623  ? 33  SER GGG CA  1 
ATOM   13231 C C   . SER I 3 33  ? 63.501  110.502 13.960  1.000 91.355  ? 33  SER GGG C   1 
ATOM   13232 O O   . SER I 3 33  ? 62.691  111.432 14.034  1.000 94.022  ? 33  SER GGG O   1 
ATOM   13233 C CB  . SER I 3 33  ? 64.079  109.561 11.714  1.000 88.272  ? 33  SER GGG CB  1 
ATOM   13234 O OG  . SER I 3 33  ? 64.752  108.334 11.871  1.000 85.193  ? 33  SER GGG OG  1 
ATOM   13235 N N   . ILE I 3 34  ? 63.522  109.470 14.801  1.000 91.725  ? 34  ILE GGG N   1 
ATOM   13236 C CA  . ILE I 3 34  ? 62.815  109.455 16.119  1.000 88.040  ? 34  ILE GGG CA  1 
ATOM   13237 C C   . ILE I 3 34  ? 63.899  109.327 17.187  1.000 79.495  ? 34  ILE GGG C   1 
ATOM   13238 O O   . ILE I 3 34  ? 64.685  108.398 17.092  1.000 100.220 ? 34  ILE GGG O   1 
ATOM   13239 C CB  . ILE I 3 34  ? 61.766  108.323 16.216  1.000 93.743  ? 34  ILE GGG CB  1 
ATOM   13240 C CG1 . ILE I 3 34  ? 62.302  106.986 15.706  1.000 101.964 ? 34  ILE GGG CG1 1 
ATOM   13241 C CG2 . ILE I 3 34  ? 60.483  108.689 15.494  1.000 95.576  ? 34  ILE GGG CG2 1 
ATOM   13242 C CD1 . ILE I 3 34  ? 61.529  105.790 16.221  1.000 105.570 ? 34  ILE GGG CD1 1 
ATOM   13243 N N   . ASN I 3 35  ? 63.954  110.232 18.154  1.000 76.294  ? 35  ASN GGG N   1 
ATOM   13244 C CA  . ASN I 3 35  ? 65.043  110.282 19.165  1.000 83.936  ? 35  ASN GGG CA  1 
ATOM   13245 C C   . ASN I 3 35  ? 64.926  109.067 20.101  1.000 84.547  ? 35  ASN GGG C   1 
ATOM   13246 O O   . ASN I 3 35  ? 64.393  109.241 21.206  1.000 90.305  ? 35  ASN GGG O   1 
ATOM   13247 C CB  . ASN I 3 35  ? 65.027  111.614 19.927  1.000 90.426  ? 35  ASN GGG CB  1 
ATOM   13248 C CG  . ASN I 3 35  ? 66.261  111.818 20.779  1.000 101.292 ? 35  ASN GGG CG  1 
ATOM   13249 O OD1 . ASN I 3 35  ? 67.383  111.624 20.304  1.000 111.949 ? 35  ASN GGG OD1 1 
ATOM   13250 N ND2 . ASN I 3 35  ? 66.066  112.199 22.032  1.000 101.847 ? 35  ASN GGG ND2 1 
ATOM   13251 N N   . LYS I 3 36  ? 65.423  107.893 19.671  1.000 86.016  ? 36  LYS GGG N   1 
ATOM   13252 C CA  . LYS I 3 36  ? 65.254  106.565 20.343  1.000 73.898  ? 36  LYS GGG CA  1 
ATOM   13253 C C   . LYS I 3 36  ? 66.487  105.682 20.099  1.000 72.839  ? 36  LYS GGG C   1 
ATOM   13254 O O   . LYS I 3 36  ? 66.909  105.573 18.922  1.000 65.757  ? 36  LYS GGG O   1 
ATOM   13255 C CB  . LYS I 3 36  ? 64.026  105.826 19.800  1.000 70.404  ? 36  LYS GGG CB  1 
ATOM   13256 C CG  . LYS I 3 36  ? 62.810  105.775 20.718  1.000 77.816  ? 36  LYS GGG CG  1 
ATOM   13257 C CD  . LYS I 3 36  ? 61.885  106.969 20.588  1.000 82.620  ? 36  LYS GGG CD  1 
ATOM   13258 C CE  . LYS I 3 36  ? 60.455  106.672 20.996  1.000 82.923  ? 36  LYS GGG CE  1 
ATOM   13259 N NZ  . LYS I 3 36  ? 60.319  106.577 22.466  1.000 80.436  ? 36  LYS GGG NZ  1 
ATOM   13260 N N   . ASN I 3 37  ? 67.035  105.044 21.145  1.000 70.860  ? 37  ASN GGG N   1 
ATOM   13261 C CA  . ASN I 3 37  ? 68.165  104.082 21.001  1.000 69.248  ? 37  ASN GGG CA  1 
ATOM   13262 C C   . ASN I 3 37  ? 67.595  102.694 20.659  1.000 62.604  ? 37  ASN GGG C   1 
ATOM   13263 O O   . ASN I 3 37  ? 66.613  102.271 21.332  1.000 60.831  ? 37  ASN GGG O   1 
ATOM   13264 C CB  . ASN I 3 37  ? 69.050  104.032 22.249  1.000 76.128  ? 37  ASN GGG CB  1 
ATOM   13265 C CG  . ASN I 3 37  ? 69.940  105.245 22.430  1.000 77.427  ? 37  ASN GGG CG  1 
ATOM   13266 O OD1 . ASN I 3 37  ? 70.994  105.372 21.787  1.000 82.319  ? 37  ASN GGG OD1 1 
ATOM   13267 N ND2 . ASN I 3 37  ? 69.548  106.103 23.358  1.000 67.688  ? 37  ASN GGG ND2 1 
ATOM   13268 N N   . TYR I 3 38  ? 68.177  102.018 19.652  1.000 57.652  ? 38  TYR GGG N   1 
ATOM   13269 C CA  . TYR I 3 38  ? 67.693  100.722 19.082  1.000 55.825  ? 38  TYR GGG CA  1 
ATOM   13270 C C   . TYR I 3 38  ? 68.392  99.562  19.802  1.000 57.510  ? 38  TYR GGG C   1 
ATOM   13271 O O   . TYR I 3 38  ? 69.241  98.880  19.201  1.000 61.053  ? 38  TYR GGG O   1 
ATOM   13272 C CB  . TYR I 3 38  ? 67.855  100.714 17.557  1.000 52.716  ? 38  TYR GGG CB  1 
ATOM   13273 C CG  . TYR I 3 38  ? 66.706  101.391 16.855  1.000 50.466  ? 38  TYR GGG CG  1 
ATOM   13274 C CD1 . TYR I 3 38  ? 65.942  100.738 15.906  1.000 51.123  ? 38  TYR GGG CD1 1 
ATOM   13275 C CD2 . TYR I 3 38  ? 66.328  102.669 17.216  1.000 52.069  ? 38  TYR GGG CD2 1 
ATOM   13276 C CE1 . TYR I 3 38  ? 64.859  101.356 15.304  1.000 51.910  ? 38  TYR GGG CE1 1 
ATOM   13277 C CE2 . TYR I 3 38  ? 65.247  103.301 16.630  1.000 54.347  ? 38  TYR GGG CE2 1 
ATOM   13278 C CZ  . TYR I 3 38  ? 64.515  102.646 15.663  1.000 53.615  ? 38  TYR GGG CZ  1 
ATOM   13279 O OH  . TYR I 3 38  ? 63.447  103.273 15.101  1.000 55.857  ? 38  TYR GGG OH  1 
ATOM   13280 N N   . LEU I 3 39  ? 68.025  99.374  21.076  1.000 57.845  ? 39  LEU GGG N   1 
ATOM   13281 C CA  . LEU I 3 39  ? 68.665  98.468  22.069  1.000 54.129  ? 39  LEU GGG CA  1 
ATOM   13282 C C   . LEU I 3 39  ? 67.531  97.776  22.812  1.000 54.694  ? 39  LEU GGG C   1 
ATOM   13283 O O   . LEU I 3 39  ? 66.604  98.490  23.236  1.000 54.400  ? 39  LEU GGG O   1 
ATOM   13284 C CB  . LEU I 3 39  ? 69.521  99.310  23.023  1.000 53.247  ? 39  LEU GGG CB  1 
ATOM   13285 C CG  . LEU I 3 39  ? 70.554  98.598  23.902  1.000 50.696  ? 39  LEU GGG CG  1 
ATOM   13286 C CD1 . LEU I 3 39  ? 69.891  97.903  25.077  1.000 51.279  ? 39  LEU GGG CD1 1 
ATOM   13287 C CD2 . LEU I 3 39  ? 71.449  97.659  23.110  1.000 49.384  ? 39  LEU GGG CD2 1 
ATOM   13288 N N   . ALA I 3 40  ? 67.583  96.446  22.909  1.000 54.182  ? 40  ALA GGG N   1 
ATOM   13289 C CA  . ALA I 3 40  ? 66.539  95.610  23.537  1.000 50.686  ? 40  ALA GGG CA  1 
ATOM   13290 C C   . ALA I 3 40  ? 67.161  94.765  24.649  1.000 52.650  ? 40  ALA GGG C   1 
ATOM   13291 O O   . ALA I 3 40  ? 68.379  94.494  24.589  1.000 51.648  ? 40  ALA GGG O   1 
ATOM   13292 C CB  . ALA I 3 40  ? 65.870  94.758  22.496  1.000 49.206  ? 40  ALA GGG CB  1 
ATOM   13293 N N   . TRP I 3 41  ? 66.325  94.362  25.608  1.000 57.586  ? 41  TRP GGG N   1 
ATOM   13294 C CA  . TRP I 3 41  ? 66.676  93.435  26.715  1.000 57.661  ? 41  TRP GGG CA  1 
ATOM   13295 C C   . TRP I 3 41  ? 65.760  92.210  26.673  1.000 54.952  ? 41  TRP GGG C   1 
ATOM   13296 O O   . TRP I 3 41  ? 64.526  92.377  26.601  1.000 60.820  ? 41  TRP GGG O   1 
ATOM   13297 C CB  . TRP I 3 41  ? 66.593  94.149  28.063  1.000 60.202  ? 41  TRP GGG CB  1 
ATOM   13298 C CG  . TRP I 3 41  ? 67.672  95.164  28.264  1.000 63.154  ? 41  TRP GGG CG  1 
ATOM   13299 C CD1 . TRP I 3 41  ? 67.589  96.506  28.043  1.000 66.612  ? 41  TRP GGG CD1 1 
ATOM   13300 C CD2 . TRP I 3 41  ? 69.005  94.921  28.737  1.000 64.340  ? 41  TRP GGG CD2 1 
ATOM   13301 N NE1 . TRP I 3 41  ? 68.773  97.116  28.355  1.000 68.568  ? 41  TRP GGG NE1 1 
ATOM   13302 C CE2 . TRP I 3 41  ? 69.663  96.167  28.777  1.000 62.821  ? 41  TRP GGG CE2 1 
ATOM   13303 C CE3 . TRP I 3 41  ? 69.703  93.780  29.136  1.000 68.053  ? 41  TRP GGG CE3 1 
ATOM   13304 C CZ2 . TRP I 3 41  ? 70.984  96.299  29.198  1.000 63.360  ? 41  TRP GGG CZ2 1 
ATOM   13305 C CZ3 . TRP I 3 41  ? 71.008  93.913  29.557  1.000 67.756  ? 41  TRP GGG CZ3 1 
ATOM   13306 C CH2 . TRP I 3 41  ? 71.640  95.156  29.587  1.000 64.591  ? 41  TRP GGG CH2 1 
ATOM   13307 N N   . TYR I 3 42  ? 66.363  91.024  26.716  1.000 51.955  ? 42  TYR GGG N   1 
ATOM   13308 C CA  . TYR I 3 42  ? 65.671  89.716  26.771  1.000 45.713  ? 42  TYR GGG CA  1 
ATOM   13309 C C   . TYR I 3 42  ? 65.975  89.028  28.106  1.000 41.530  ? 42  TYR GGG C   1 
ATOM   13310 O O   . TYR I 3 42  ? 67.091  89.165  28.670  1.000 36.821  ? 42  TYR GGG O   1 
ATOM   13311 C CB  . TYR I 3 42  ? 66.084  88.876  25.565  1.000 46.873  ? 42  TYR GGG CB  1 
ATOM   13312 C CG  . TYR I 3 42  ? 65.675  89.478  24.244  1.000 45.314  ? 42  TYR GGG CG  1 
ATOM   13313 C CD1 . TYR I 3 42  ? 66.519  90.335  23.571  1.000 42.628  ? 42  TYR GGG CD1 1 
ATOM   13314 C CD2 . TYR I 3 42  ? 64.438  89.210  23.679  1.000 44.803  ? 42  TYR GGG CD2 1 
ATOM   13315 C CE1 . TYR I 3 42  ? 66.164  90.879  22.350  1.000 43.350  ? 42  TYR GGG CE1 1 
ATOM   13316 C CE2 . TYR I 3 42  ? 64.058  89.765  22.469  1.000 45.668  ? 42  TYR GGG CE2 1 
ATOM   13317 C CZ  . TYR I 3 42  ? 64.925  90.612  21.803  1.000 45.648  ? 42  TYR GGG CZ  1 
ATOM   13318 O OH  . TYR I 3 42  ? 64.582  91.175  20.607  1.000 48.341  ? 42  TYR GGG OH  1 
ATOM   13319 N N   . GLN I 3 43  ? 64.960  88.326  28.603  1.000 39.704  ? 43  GLN GGG N   1 
ATOM   13320 C CA  . GLN I 3 43  ? 65.047  87.342  29.711  1.000 38.082  ? 43  GLN GGG CA  1 
ATOM   13321 C C   . GLN I 3 43  ? 64.966  85.943  29.092  1.000 36.975  ? 43  GLN GGG C   1 
ATOM   13322 O O   . GLN I 3 43  ? 64.095  85.730  28.223  1.000 34.497  ? 43  GLN GGG O   1 
ATOM   13323 C CB  . GLN I 3 43  ? 63.911  87.607  30.696  1.000 36.009  ? 43  GLN GGG CB  1 
ATOM   13324 C CG  . GLN I 3 43  ? 63.769  86.590  31.802  1.000 34.791  ? 43  GLN GGG CG  1 
ATOM   13325 C CD  . GLN I 3 43  ? 62.579  86.917  32.662  1.000 34.701  ? 43  GLN GGG CD  1 
ATOM   13326 O OE1 . GLN I 3 43  ? 61.443  86.613  32.309  1.000 36.826  ? 43  GLN GGG OE1 1 
ATOM   13327 N NE2 . GLN I 3 43  ? 62.838  87.554  33.794  1.000 33.315  ? 43  GLN GGG NE2 1 
ATOM   13328 N N   . GLN I 3 44  ? 65.855  85.032  29.497  1.000 36.765  ? 44  GLN GGG N   1 
ATOM   13329 C CA  . GLN I 3 44  ? 65.744  83.588  29.150  1.000 36.001  ? 44  GLN GGG CA  1 
ATOM   13330 C C   . GLN I 3 44  ? 65.906  82.760  30.418  1.000 37.341  ? 44  GLN GGG C   1 
ATOM   13331 O O   . GLN I 3 44  ? 66.936  82.909  31.098  1.000 39.238  ? 44  GLN GGG O   1 
ATOM   13332 C CB  . GLN I 3 44  ? 66.787  83.185  28.121  1.000 33.258  ? 44  GLN GGG CB  1 
ATOM   13333 C CG  . GLN I 3 44  ? 66.442  81.915  27.376  1.000 30.342  ? 44  GLN GGG CG  1 
ATOM   13334 C CD  . GLN I 3 44  ? 67.651  81.390  26.641  1.000 30.337  ? 44  GLN GGG CD  1 
ATOM   13335 O OE1 . GLN I 3 44  ? 68.781  81.838  26.848  1.000 28.219  ? 44  GLN GGG OE1 1 
ATOM   13336 N NE2 . GLN I 3 44  ? 67.427  80.388  25.805  1.000 30.783  ? 44  GLN GGG NE2 1 
ATOM   13337 N N   . LYS I 3 45  ? 64.901  81.949  30.724  1.000 41.054  ? 45  LYS GGG N   1 
ATOM   13338 C CA  . LYS I 3 45  ? 64.936  80.996  31.855  1.000 45.414  ? 45  LYS GGG CA  1 
ATOM   13339 C C   . LYS I 3 45  ? 65.204  79.618  31.286  1.000 53.890  ? 45  LYS GGG C   1 
ATOM   13340 O O   . LYS I 3 45  ? 64.973  79.370  30.101  1.000 63.193  ? 45  LYS GGG O   1 
ATOM   13341 C CB  . LYS I 3 45  ? 63.614  80.995  32.608  1.000 44.814  ? 45  LYS GGG CB  1 
ATOM   13342 C CG  . LYS I 3 45  ? 63.162  82.365  33.077  1.000 45.760  ? 45  LYS GGG CG  1 
ATOM   13343 C CD  . LYS I 3 45  ? 61.779  82.353  33.655  1.000 49.533  ? 45  LYS GGG CD  1 
ATOM   13344 C CE  . LYS I 3 45  ? 61.587  83.538  34.574  1.000 55.676  ? 45  LYS GGG CE  1 
ATOM   13345 N NZ  . LYS I 3 45  ? 60.253  83.550  35.216  1.000 63.202  ? 45  LYS GGG NZ  1 
ATOM   13346 N N   . PRO I 3 46  ? 65.732  78.706  32.119  1.000 60.846  ? 46  PRO GGG N   1 
ATOM   13347 C CA  . PRO I 3 46  ? 66.056  77.351  31.672  1.000 61.755  ? 46  PRO GGG CA  1 
ATOM   13348 C C   . PRO I 3 46  ? 64.983  76.681  30.796  1.000 58.589  ? 46  PRO GGG C   1 
ATOM   13349 O O   . PRO I 3 46  ? 63.805  76.738  31.142  1.000 59.377  ? 46  PRO GGG O   1 
ATOM   13350 C CB  . PRO I 3 46  ? 66.187  76.613  33.005  1.000 67.845  ? 46  PRO GGG CB  1 
ATOM   13351 C CG  . PRO I 3 46  ? 66.705  77.672  33.963  1.000 66.222  ? 46  PRO GGG CG  1 
ATOM   13352 C CD  . PRO I 3 46  ? 66.071  78.967  33.524  1.000 60.392  ? 46  PRO GGG CD  1 
ATOM   13353 N N   . GLY I 3 47  ? 65.432  76.089  29.680  1.000 58.109  ? 47  GLY GGG N   1 
ATOM   13354 C CA  . GLY I 3 47  ? 64.651  75.274  28.720  1.000 59.878  ? 47  GLY GGG CA  1 
ATOM   13355 C C   . GLY I 3 47  ? 63.495  76.029  28.087  1.000 59.121  ? 47  GLY GGG C   1 
ATOM   13356 O O   . GLY I 3 47  ? 62.513  75.387  27.705  1.000 60.222  ? 47  GLY GGG O   1 
ATOM   13357 N N   . GLN I 3 48  ? 63.611  77.352  27.960  1.000 58.717  ? 48  GLN GGG N   1 
ATOM   13358 C CA  . GLN I 3 48  ? 62.536  78.240  27.444  1.000 55.127  ? 48  GLN GGG CA  1 
ATOM   13359 C C   . GLN I 3 48  ? 63.116  79.174  26.395  1.000 52.029  ? 48  GLN GGG C   1 
ATOM   13360 O O   . GLN I 3 48  ? 64.291  79.500  26.437  1.000 46.919  ? 48  GLN GGG O   1 
ATOM   13361 C CB  . GLN I 3 48  ? 61.905  79.041  28.584  1.000 56.730  ? 48  GLN GGG CB  1 
ATOM   13362 C CG  . GLN I 3 48  ? 61.103  78.178  29.549  1.000 59.856  ? 48  GLN GGG CG  1 
ATOM   13363 C CD  . GLN I 3 48  ? 60.122  78.967  30.376  1.000 59.908  ? 48  GLN GGG CD  1 
ATOM   13364 O OE1 . GLN I 3 48  ? 60.314  80.147  30.690  1.000 53.906  ? 48  GLN GGG OE1 1 
ATOM   13365 N NE2 . GLN I 3 48  ? 59.052  78.288  30.748  1.000 67.572  ? 48  GLN GGG NE2 1 
ATOM   13366 N N   . PRO I 3 49  ? 62.308  79.641  25.424  1.000 52.472  ? 49  PRO GGG N   1 
ATOM   13367 C CA  . PRO I 3 49  ? 62.749  80.693  24.523  1.000 50.815  ? 49  PRO GGG CA  1 
ATOM   13368 C C   . PRO I 3 49  ? 63.000  81.987  25.290  1.000 52.437  ? 49  PRO GGG C   1 
ATOM   13369 O O   . PRO I 3 49  ? 62.442  82.202  26.371  1.000 50.838  ? 49  PRO GGG O   1 
ATOM   13370 C CB  . PRO I 3 49  ? 61.588  80.854  23.534  1.000 51.261  ? 49  PRO GGG CB  1 
ATOM   13371 C CG  . PRO I 3 49  ? 60.386  80.331  24.277  1.000 55.484  ? 49  PRO GGG CG  1 
ATOM   13372 C CD  . PRO I 3 49  ? 60.931  79.214  25.145  1.000 56.105  ? 49  PRO GGG CD  1 
ATOM   13373 N N   . PRO I 3 50  ? 63.870  82.870  24.749  1.000 49.627  ? 50  PRO GGG N   1 
ATOM   13374 C CA  . PRO I 3 50  ? 64.016  84.225  25.258  1.000 47.173  ? 50  PRO GGG CA  1 
ATOM   13375 C C   . PRO I 3 50  ? 62.686  84.980  25.180  1.000 49.520  ? 50  PRO GGG C   1 
ATOM   13376 O O   . PRO I 3 50  ? 61.914  84.731  24.268  1.000 54.666  ? 50  PRO GGG O   1 
ATOM   13377 C CB  . PRO I 3 50  ? 65.019  84.876  24.304  1.000 48.043  ? 50  PRO GGG CB  1 
ATOM   13378 C CG  . PRO I 3 50  ? 65.760  83.732  23.676  1.000 48.201  ? 50  PRO GGG CG  1 
ATOM   13379 C CD  . PRO I 3 50  ? 64.754  82.609  23.606  1.000 49.045  ? 50  PRO GGG CD  1 
ATOM   13380 N N   . LYS I 3 51  ? 62.472  85.886  26.133  1.000 49.368  ? 51  LYS GGG N   1 
ATOM   13381 C CA  . LYS I 3 51  ? 61.276  86.754  26.257  1.000 48.242  ? 51  LYS GGG CA  1 
ATOM   13382 C C   . LYS I 3 51  ? 61.753  88.203  26.131  1.000 44.638  ? 51  LYS GGG C   1 
ATOM   13383 O O   . LYS I 3 51  ? 62.711  88.568  26.834  1.000 39.388  ? 51  LYS GGG O   1 
ATOM   13384 C CB  . LYS I 3 51  ? 60.616  86.462  27.604  1.000 55.221  ? 51  LYS GGG CB  1 
ATOM   13385 C CG  . LYS I 3 51  ? 59.313  87.194  27.927  1.000 62.912  ? 51  LYS GGG CG  1 
ATOM   13386 C CD  . LYS I 3 51  ? 59.027  87.262  29.426  1.000 73.336  ? 51  LYS GGG CD  1 
ATOM   13387 C CE  . LYS I 3 51  ? 58.047  86.219  29.949  1.000 80.413  ? 51  LYS GGG CE  1 
ATOM   13388 N NZ  . LYS I 3 51  ? 56.656  86.698  29.828  1.000 88.758  ? 51  LYS GGG NZ  1 
ATOM   13389 N N   . LEU I 3 52  ? 61.113  88.996  25.271  1.000 44.580  ? 52  LEU GGG N   1 
ATOM   13390 C CA  . LEU I 3 52  ? 61.367  90.456  25.174  1.000 41.684  ? 52  LEU GGG CA  1 
ATOM   13391 C C   . LEU I 3 52  ? 60.769  91.169  26.395  1.000 42.889  ? 52  LEU GGG C   1 
ATOM   13392 O O   . LEU I 3 52  ? 59.511  91.148  26.541  1.000 41.859  ? 52  LEU GGG O   1 
ATOM   13393 C CB  . LEU I 3 52  ? 60.749  90.993  23.885  1.000 40.688  ? 52  LEU GGG CB  1 
ATOM   13394 C CG  . LEU I 3 52  ? 61.019  92.476  23.646  1.000 39.265  ? 52  LEU GGG CG  1 
ATOM   13395 C CD1 . LEU I 3 52  ? 62.473  92.701  23.232  1.000 37.676  ? 52  LEU GGG CD1 1 
ATOM   13396 C CD2 . LEU I 3 52  ? 60.030  93.045  22.642  1.000 39.241  ? 52  LEU GGG CD2 1 
ATOM   13397 N N   . LEU I 3 53  ? 61.641  91.779  27.212  1.000 44.556  ? 53  LEU GGG N   1 
ATOM   13398 C CA  . LEU I 3 53  ? 61.297  92.614  28.398  1.000 47.315  ? 53  LEU GGG CA  1 
ATOM   13399 C C   . LEU I 3 53  ? 61.178  94.075  27.977  1.000 48.315  ? 53  LEU GGG C   1 
ATOM   13400 O O   . LEU I 3 53  ? 60.147  94.700  28.287  1.000 51.781  ? 53  LEU GGG O   1 
ATOM   13401 C CB  . LEU I 3 53  ? 62.403  92.533  29.455  1.000 48.776  ? 53  LEU GGG CB  1 
ATOM   13402 C CG  . LEU I 3 53  ? 62.567  91.202  30.171  1.000 48.702  ? 53  LEU GGG CG  1 
ATOM   13403 C CD1 . LEU I 3 53  ? 63.668  91.317  31.204  1.000 49.908  ? 53  LEU GGG CD1 1 
ATOM   13404 C CD2 . LEU I 3 53  ? 61.276  90.745  30.827  1.000 49.218  ? 53  LEU GGG CD2 1 
ATOM   13405 N N   . ILE I 3 54  ? 62.241  94.599  27.366  1.000 46.222  ? 54  ILE GGG N   1 
ATOM   13406 C CA  . ILE I 3 54  ? 62.419  96.056  27.144  1.000 47.679  ? 54  ILE GGG CA  1 
ATOM   13407 C C   . ILE I 3 54  ? 62.996  96.294  25.750  1.000 47.871  ? 54  ILE GGG C   1 
ATOM   13408 O O   . ILE I 3 54  ? 63.942  95.577  25.378  1.000 46.225  ? 54  ILE GGG O   1 
ATOM   13409 C CB  . ILE I 3 54  ? 63.285  96.646  28.265  1.000 50.663  ? 54  ILE GGG CB  1 
ATOM   13410 C CG1 . ILE I 3 54  ? 62.460  96.770  29.553  1.000 56.621  ? 54  ILE GGG CG1 1 
ATOM   13411 C CG2 . ILE I 3 54  ? 63.898  97.970  27.817  1.000 51.297  ? 54  ILE GGG CG2 1 
ATOM   13412 C CD1 . ILE I 3 54  ? 63.254  97.164  30.793  1.000 63.076  ? 54  ILE GGG CD1 1 
ATOM   13413 N N   . TYR I 3 55  ? 62.424  97.261  25.016  1.000 49.339  ? 55  TYR GGG N   1 
ATOM   13414 C CA  . TYR I 3 55  ? 62.894  97.718  23.681  1.000 51.599  ? 55  TYR GGG CA  1 
ATOM   13415 C C   . TYR I 3 55  ? 62.971  99.243  23.667  1.000 52.504  ? 55  TYR GGG C   1 
ATOM   13416 O O   . TYR I 3 55  ? 62.442  99.863  24.598  1.000 56.055  ? 55  TYR GGG O   1 
ATOM   13417 C CB  . TYR I 3 55  ? 62.005  97.186  22.553  1.000 52.436  ? 55  TYR GGG CB  1 
ATOM   13418 C CG  . TYR I 3 55  ? 60.613  97.739  22.551  1.000 52.736  ? 55  TYR GGG CG  1 
ATOM   13419 C CD1 . TYR I 3 55  ? 59.608  97.108  23.256  1.000 54.598  ? 55  TYR GGG CD1 1 
ATOM   13420 C CD2 . TYR I 3 55  ? 60.304  98.885  21.844  1.000 59.489  ? 55  TYR GGG CD2 1 
ATOM   13421 C CE1 . TYR I 3 55  ? 58.318  97.605  23.272  1.000 59.379  ? 55  TYR GGG CE1 1 
ATOM   13422 C CE2 . TYR I 3 55  ? 59.014  99.391  21.838  1.000 64.330  ? 55  TYR GGG CE2 1 
ATOM   13423 C CZ  . TYR I 3 55  ? 58.022  98.755  22.565  1.000 61.362  ? 55  TYR GGG CZ  1 
ATOM   13424 O OH  . TYR I 3 55  ? 56.756  99.253  22.582  1.000 58.510  ? 55  TYR GGG OH  1 
ATOM   13425 N N   . TRP I 3 56  ? 63.634  99.802  22.644  1.000 54.634  ? 56  TRP GGG N   1 
ATOM   13426 C CA  . TRP I 3 56  ? 64.055  101.228 22.550  1.000 51.953  ? 56  TRP GGG CA  1 
ATOM   13427 C C   . TRP I 3 56  ? 64.722  101.631 23.869  1.000 49.424  ? 56  TRP GGG C   1 
ATOM   13428 O O   . TRP I 3 56  ? 64.329  102.613 24.479  1.000 42.147  ? 56  TRP GGG O   1 
ATOM   13429 C CB  . TRP I 3 56  ? 62.876  102.128 22.163  1.000 53.669  ? 56  TRP GGG CB  1 
ATOM   13430 C CG  . TRP I 3 56  ? 62.560  102.129 20.696  1.000 57.461  ? 56  TRP GGG CG  1 
ATOM   13431 C CD1 . TRP I 3 56  ? 63.407  101.850 19.657  1.000 60.161  ? 56  TRP GGG CD1 1 
ATOM   13432 C CD2 . TRP I 3 56  ? 61.298  102.473 20.095  1.000 59.634  ? 56  TRP GGG CD2 1 
ATOM   13433 N NE1 . TRP I 3 56  ? 62.756  101.983 18.456  1.000 62.223  ? 56  TRP GGG NE1 1 
ATOM   13434 C CE2 . TRP I 3 56  ? 61.458  102.350 18.695  1.000 61.647  ? 56  TRP GGG CE2 1 
ATOM   13435 C CE3 . TRP I 3 56  ? 60.054  102.862 20.605  1.000 59.617  ? 56  TRP GGG CE3 1 
ATOM   13436 C CZ2 . TRP I 3 56  ? 60.417  102.594 17.803  1.000 61.588  ? 56  TRP GGG CZ2 1 
ATOM   13437 C CZ3 . TRP I 3 56  ? 59.021  103.086 19.725  1.000 58.981  ? 56  TRP GGG CZ3 1 
ATOM   13438 C CH2 . TRP I 3 56  ? 59.204  102.954 18.346  1.000 59.815  ? 56  TRP GGG CH2 1 
ATOM   13439 N N   . ALA I 3 57  ? 65.666  100.801 24.302  1.000 55.296  ? 57  ALA GGG N   1 
ATOM   13440 C CA  . ALA I 3 57  ? 66.600  101.008 25.430  1.000 57.471  ? 57  ALA GGG CA  1 
ATOM   13441 C C   . ALA I 3 57  ? 65.858  101.097 26.766  1.000 53.914  ? 57  ALA GGG C   1 
ATOM   13442 O O   . ALA I 3 57  ? 66.532  100.791 27.785  1.000 60.272  ? 57  ALA GGG O   1 
ATOM   13443 C CB  . ALA I 3 57  ? 67.443  102.229 25.185  1.000 61.799  ? 57  ALA GGG CB  1 
ATOM   13444 N N   . SER I 3 58  ? 64.572  101.487 26.774  1.000 48.850  ? 58  SER GGG N   1 
ATOM   13445 C CA  . SER I 3 58  ? 63.836  101.844 28.015  1.000 54.283  ? 58  SER GGG CA  1 
ATOM   13446 C C   . SER I 3 58  ? 62.303  101.685 27.957  1.000 53.210  ? 58  SER GGG C   1 
ATOM   13447 O O   . SER I 3 58  ? 61.705  101.965 28.998  1.000 50.800  ? 58  SER GGG O   1 
ATOM   13448 C CB  . SER I 3 58  ? 64.159  103.259 28.372  1.000 61.037  ? 58  SER GGG CB  1 
ATOM   13449 O OG  . SER I 3 58  ? 63.470  104.149 27.496  1.000 63.703  ? 58  SER GGG OG  1 
ATOM   13450 N N   . THR I 3 59  ? 61.676  101.259 26.854  1.000 52.001  ? 59  THR GGG N   1 
ATOM   13451 C CA  . THR I 3 59  ? 60.204  101.012 26.792  1.000 53.052  ? 59  THR GGG CA  1 
ATOM   13452 C C   . THR I 3 59  ? 59.911  99.566  27.211  1.000 55.376  ? 59  THR GGG C   1 
ATOM   13453 O O   . THR I 3 59  ? 60.546  98.647  26.653  1.000 55.017  ? 59  THR GGG O   1 
ATOM   13454 C CB  . THR I 3 59  ? 59.636  101.298 25.392  1.000 54.544  ? 59  THR GGG CB  1 
ATOM   13455 O OG1 . THR I 3 59  ? 60.061  102.608 25.025  1.000 59.290  ? 59  THR GGG OG1 1 
ATOM   13456 C CG2 . THR I 3 59  ? 58.129  101.214 25.296  1.000 50.042  ? 59  THR GGG CG2 1 
ATOM   13457 N N   . ARG I 3 60  ? 58.983  99.376  28.151  1.000 58.558  ? 60  ARG GGG N   1 
ATOM   13458 C CA  . ARG I 3 60  ? 58.555  98.040  28.644  1.000 59.316  ? 60  ARG GGG CA  1 
ATOM   13459 C C   . ARG I 3 60  ? 57.589  97.399  27.646  1.000 55.413  ? 60  ARG GGG C   1 
ATOM   13460 O O   . ARG I 3 60  ? 56.593  98.045  27.284  1.000 49.948  ? 60  ARG GGG O   1 
ATOM   13461 C CB  . ARG I 3 60  ? 57.852  98.143  29.994  1.000 64.856  ? 60  ARG GGG CB  1 
ATOM   13462 C CG  . ARG I 3 60  ? 58.721  97.741  31.171  1.000 70.568  ? 60  ARG GGG CG  1 
ATOM   13463 C CD  . ARG I 3 60  ? 57.879  97.685  32.428  1.000 75.702  ? 60  ARG GGG CD  1 
ATOM   13464 N NE  . ARG I 3 60  ? 57.353  98.996  32.781  1.000 78.885  ? 60  ARG GGG NE  1 
ATOM   13465 C CZ  . ARG I 3 60  ? 58.054  99.983  33.344  1.000 80.921  ? 60  ARG GGG CZ  1 
ATOM   13466 N NH1 . ARG I 3 60  ? 59.333  99.833  33.648  1.000 76.729  ? 60  ARG GGG NH1 1 
ATOM   13467 N NH2 . ARG I 3 60  ? 57.465  101.138 33.584  1.000 92.258  ? 60  ARG GGG NH2 1 
ATOM   13468 N N   . GLU I 3 61  ? 57.876  96.168  27.228  1.000 54.693  ? 61  GLU GGG N   1 
ATOM   13469 C CA  . GLU I 3 61  ? 56.943  95.344  26.415  1.000 60.358  ? 61  GLU GGG CA  1 
ATOM   13470 C C   . GLU I 3 61  ? 55.702  95.093  27.282  1.000 63.568  ? 61  GLU GGG C   1 
ATOM   13471 O O   . GLU I 3 61  ? 55.868  95.028  28.515  1.000 73.540  ? 61  GLU GGG O   1 
ATOM   13472 C CB  . GLU I 3 61  ? 57.653  94.072  25.938  1.000 60.178  ? 61  GLU GGG CB  1 
ATOM   13473 C CG  . GLU I 3 61  ? 56.770  93.113  25.150  1.000 63.489  ? 61  GLU GGG CG  1 
ATOM   13474 C CD  . GLU I 3 61  ? 56.296  93.613  23.786  1.000 62.606  ? 61  GLU GGG CD  1 
ATOM   13475 O OE1 . GLU I 3 61  ? 56.642  93.007  22.741  1.000 60.975  ? 61  GLU GGG OE1 1 
ATOM   13476 O OE2 . GLU I 3 61  ? 55.539  94.594  23.769  1.000 66.328  ? 61  GLU GGG OE2 1 
ATOM   13477 N N   . SER I 3 62  ? 54.499  95.005  26.703  1.000 63.499  ? 62  SER GGG N   1 
ATOM   13478 C CA  . SER I 3 62  ? 53.263  94.931  27.530  1.000 67.452  ? 62  SER GGG CA  1 
ATOM   13479 C C   . SER I 3 62  ? 53.306  93.629  28.332  1.000 60.430  ? 62  SER GGG C   1 
ATOM   13480 O O   . SER I 3 62  ? 53.978  92.688  27.885  1.000 54.352  ? 62  SER GGG O   1 
ATOM   13481 C CB  . SER I 3 62  ? 51.973  95.099  26.743  1.000 74.392  ? 62  SER GGG CB  1 
ATOM   13482 O OG  . SER I 3 62  ? 51.899  94.193  25.653  1.000 86.838  ? 62  SER GGG OG  1 
ATOM   13483 N N   . GLY I 3 63  ? 52.678  93.633  29.506  1.000 63.226  ? 63  GLY GGG N   1 
ATOM   13484 C CA  . GLY I 3 63  ? 52.688  92.518  30.471  1.000 62.630  ? 63  GLY GGG CA  1 
ATOM   13485 C C   . GLY I 3 63  ? 54.059  92.295  31.090  1.000 60.300  ? 63  GLY GGG C   1 
ATOM   13486 O O   . GLY I 3 63  ? 54.322  91.170  31.484  1.000 68.104  ? 63  GLY GGG O   1 
ATOM   13487 N N   . VAL I 3 64  ? 54.909  93.313  31.181  1.000 55.276  ? 64  VAL GGG N   1 
ATOM   13488 C CA  . VAL I 3 64  ? 56.180  93.245  31.954  1.000 54.136  ? 64  VAL GGG CA  1 
ATOM   13489 C C   . VAL I 3 64  ? 56.010  94.110  33.195  1.000 57.642  ? 64  VAL GGG C   1 
ATOM   13490 O O   . VAL I 3 64  ? 55.639  95.275  33.096  1.000 59.941  ? 64  VAL GGG O   1 
ATOM   13491 C CB  . VAL I 3 64  ? 57.385  93.709  31.122  1.000 55.407  ? 64  VAL GGG CB  1 
ATOM   13492 C CG1 . VAL I 3 64  ? 58.662  93.801  31.962  1.000 57.828  ? 64  VAL GGG CG1 1 
ATOM   13493 C CG2 . VAL I 3 64  ? 57.582  92.819  29.909  1.000 55.281  ? 64  VAL GGG CG2 1 
ATOM   13494 N N   . PRO I 3 65  ? 56.297  93.580  34.401  1.000 63.000  ? 65  PRO GGG N   1 
ATOM   13495 C CA  . PRO I 3 65  ? 56.044  94.309  35.640  1.000 71.595  ? 65  PRO GGG CA  1 
ATOM   13496 C C   . PRO I 3 65  ? 56.884  95.582  35.740  1.000 74.539  ? 65  PRO GGG C   1 
ATOM   13497 O O   . PRO I 3 65  ? 57.873  95.680  35.046  1.000 67.516  ? 65  PRO GGG O   1 
ATOM   13498 C CB  . PRO I 3 65  ? 56.480  93.367  36.769  1.000 73.168  ? 65  PRO GGG CB  1 
ATOM   13499 C CG  . PRO I 3 65  ? 56.635  92.018  36.109  1.000 69.742  ? 65  PRO GGG CG  1 
ATOM   13500 C CD  . PRO I 3 65  ? 56.897  92.267  34.640  1.000 64.464  ? 65  PRO GGG CD  1 
ATOM   13501 N N   . ASP I 3 66  ? 56.487  96.495  36.630  1.000 81.291  ? 66  ASP GGG N   1 
ATOM   13502 C CA  . ASP I 3 66  ? 57.117  97.832  36.773  1.000 83.133  ? 66  ASP GGG CA  1 
ATOM   13503 C C   . ASP I 3 66  ? 58.577  97.692  37.202  1.000 75.249  ? 66  ASP GGG C   1 
ATOM   13504 O O   . ASP I 3 66  ? 59.360  98.588  36.887  1.000 75.153  ? 66  ASP GGG O   1 
ATOM   13505 C CB  . ASP I 3 66  ? 56.335  98.690  37.767  1.000 90.472  ? 66  ASP GGG CB  1 
ATOM   13506 C CG  . ASP I 3 66  ? 54.942  99.005  37.273  1.000 101.704 ? 66  ASP GGG CG  1 
ATOM   13507 O OD1 . ASP I 3 66  ? 54.795  99.228  36.058  1.000 121.580 ? 66  ASP GGG OD1 1 
ATOM   13508 O OD2 . ASP I 3 66  ? 54.022  99.001  38.099  1.000 120.748 ? 66  ASP GGG OD2 1 
ATOM   13509 N N   . ARG I 3 67  ? 58.929  96.611  37.890  1.000 70.654  ? 67  ARG GGG N   1 
ATOM   13510 C CA  . ARG I 3 67  ? 60.225  96.507  38.605  1.000 72.907  ? 67  ARG GGG CA  1 
ATOM   13511 C C   . ARG I 3 67  ? 61.382  96.350  37.607  1.000 70.545  ? 67  ARG GGG C   1 
ATOM   13512 O O   . ARG I 3 67  ? 62.538  96.526  38.012  1.000 61.238  ? 67  ARG GGG O   1 
ATOM   13513 C CB  . ARG I 3 67  ? 60.150  95.375  39.634  1.000 77.398  ? 67  ARG GGG CB  1 
ATOM   13514 C CG  . ARG I 3 67  ? 59.850  93.993  39.068  1.000 76.033  ? 67  ARG GGG CG  1 
ATOM   13515 C CD  . ARG I 3 67  ? 60.218  92.904  40.054  1.000 73.727  ? 67  ARG GGG CD  1 
ATOM   13516 N NE  . ARG I 3 67  ? 60.121  91.595  39.433  1.000 73.246  ? 67  ARG GGG NE  1 
ATOM   13517 C CZ  . ARG I 3 67  ? 58.981  90.953  39.212  1.000 74.500  ? 67  ARG GGG CZ  1 
ATOM   13518 N NH1 . ARG I 3 67  ? 57.822  91.484  39.569  1.000 70.509  ? 67  ARG GGG NH1 1 
ATOM   13519 N NH2 . ARG I 3 67  ? 58.999  89.772  38.625  1.000 83.568  ? 67  ARG GGG NH2 1 
ATOM   13520 N N   . PHE I 3 68  ? 61.085  96.047  36.344  1.000 72.681  ? 68  PHE GGG N   1 
ATOM   13521 C CA  . PHE I 3 68  ? 62.057  96.079  35.221  1.000 71.617  ? 68  PHE GGG CA  1 
ATOM   13522 C C   . PHE I 3 68  ? 62.055  97.482  34.619  1.000 72.750  ? 68  PHE GGG C   1 
ATOM   13523 O O   . PHE I 3 68  ? 60.981  97.941  34.220  1.000 85.199  ? 68  PHE GGG O   1 
ATOM   13524 C CB  . PHE I 3 68  ? 61.680  95.059  34.142  1.000 74.347  ? 68  PHE GGG CB  1 
ATOM   13525 C CG  . PHE I 3 68  ? 61.806  93.634  34.601  1.000 73.344  ? 68  PHE GGG CG  1 
ATOM   13526 C CD1 . PHE I 3 68  ? 60.740  92.972  35.182  1.000 76.314  ? 68  PHE GGG CD1 1 
ATOM   13527 C CD2 . PHE I 3 68  ? 63.015  92.977  34.499  1.000 70.442  ? 68  PHE GGG CD2 1 
ATOM   13528 C CE1 . PHE I 3 68  ? 60.877  91.670  35.632  1.000 77.843  ? 68  PHE GGG CE1 1 
ATOM   13529 C CE2 . PHE I 3 68  ? 63.152  91.678  34.950  1.000 68.010  ? 68  PHE GGG CE2 1 
ATOM   13530 C CZ  . PHE I 3 68  ? 62.085  91.021  35.510  1.000 70.807  ? 68  PHE GGG CZ  1 
ATOM   13531 N N   . SER I 3 69  ? 63.206  98.134  34.538  1.000 74.040  ? 69  SER GGG N   1 
ATOM   13532 C CA  . SER I 3 69  ? 63.347  99.445  33.858  1.000 74.088  ? 69  SER GGG CA  1 
ATOM   13533 C C   . SER I 3 69  ? 64.687  99.474  33.136  1.000 70.736  ? 69  SER GGG C   1 
ATOM   13534 O O   . SER I 3 69  ? 65.671  98.943  33.686  1.000 71.521  ? 69  SER GGG O   1 
ATOM   13535 C CB  . SER I 3 69  ? 63.212  100.581 34.826  1.000 75.210  ? 69  SER GGG CB  1 
ATOM   13536 O OG  . SER I 3 69  ? 64.310  100.583 35.727  1.000 76.296  ? 69  SER GGG OG  1 
ATOM   13537 N N   . GLY I 3 70  ? 64.687  100.053 31.943  1.000 68.878  ? 70  GLY GGG N   1 
ATOM   13538 C CA  . GLY I 3 70  ? 65.874  100.155 31.081  1.000 72.673  ? 70  GLY GGG CA  1 
ATOM   13539 C C   . GLY I 3 70  ? 66.252  101.605 30.916  1.000 69.590  ? 70  GLY GGG C   1 
ATOM   13540 O O   . GLY I 3 70  ? 65.359  102.452 31.001  1.000 65.217  ? 70  GLY GGG O   1 
ATOM   13541 N N   . SER I 3 71  ? 67.534  101.888 30.715  1.000 68.844  ? 71  SER GGG N   1 
ATOM   13542 C CA  . SER I 3 71  ? 68.036  103.277 30.624  1.000 70.314  ? 71  SER GGG CA  1 
ATOM   13543 C C   . SER I 3 71  ? 69.361  103.297 29.873  1.000 75.278  ? 71  SER GGG C   1 
ATOM   13544 O O   . SER I 3 71  ? 69.820  102.206 29.427  1.000 81.815  ? 71  SER GGG O   1 
ATOM   13545 C CB  . SER I 3 71  ? 68.161  103.868 31.998  1.000 70.917  ? 71  SER GGG CB  1 
ATOM   13546 O OG  . SER I 3 71  ? 68.979  103.042 32.814  1.000 74.336  ? 71  SER GGG OG  1 
ATOM   13547 N N   . GLY I 3 72  ? 69.920  104.503 29.741  1.000 73.304  ? 72  GLY GGG N   1 
ATOM   13548 C CA  . GLY I 3 72  ? 71.213  104.768 29.097  1.000 71.948  ? 72  GLY GGG CA  1 
ATOM   13549 C C   . GLY I 3 72  ? 71.010  105.527 27.806  1.000 72.791  ? 72  GLY GGG C   1 
ATOM   13550 O O   . GLY I 3 72  ? 69.829  105.761 27.425  1.000 58.616  ? 72  GLY GGG O   1 
ATOM   13551 N N   . SER I 3 73  ? 72.123  105.900 27.167  1.000 75.616  ? 73  SER GGG N   1 
ATOM   13552 C CA  . SER I 3 73  ? 72.149  106.650 25.891  1.000 71.181  ? 73  SER GGG CA  1 
ATOM   13553 C C   . SER I 3 73  ? 73.495  106.483 25.186  1.000 69.239  ? 73  SER GGG C   1 
ATOM   13554 O O   . SER I 3 73  ? 74.488  106.170 25.854  1.000 67.616  ? 73  SER GGG O   1 
ATOM   13555 C CB  . SER I 3 73  ? 71.854  108.084 26.142  1.000 71.424  ? 73  SER GGG CB  1 
ATOM   13556 O OG  . SER I 3 73  ? 71.284  108.642 24.980  1.000 83.943  ? 73  SER GGG OG  1 
ATOM   13557 N N   . GLY I 3 74  ? 73.524  106.709 23.876  1.000 68.623  ? 74  GLY GGG N   1 
ATOM   13558 C CA  . GLY I 3 74  ? 74.762  106.619 23.087  1.000 70.894  ? 74  GLY GGG CA  1 
ATOM   13559 C C   . GLY I 3 74  ? 75.272  105.199 23.072  1.000 69.795  ? 74  GLY GGG C   1 
ATOM   13560 O O   . GLY I 3 74  ? 74.777  104.440 22.239  1.000 80.752  ? 74  GLY GGG O   1 
ATOM   13561 N N   . THR I 3 75  ? 76.197  104.847 23.971  1.000 66.428  ? 75  THR GGG N   1 
ATOM   13562 C CA  . THR I 3 75  ? 76.860  103.515 23.985  1.000 75.234  ? 75  THR GGG CA  1 
ATOM   13563 C C   . THR I 3 75  ? 76.760  102.813 25.347  1.000 84.925  ? 75  THR GGG C   1 
ATOM   13564 O O   . THR I 3 75  ? 77.132  101.621 25.388  1.000 103.559 ? 75  THR GGG O   1 
ATOM   13565 C CB  . THR I 3 75  ? 78.336  103.589 23.567  1.000 75.767  ? 75  THR GGG CB  1 
ATOM   13566 O OG1 . THR I 3 75  ? 79.105  104.169 24.619  1.000 71.591  ? 75  THR GGG OG1 1 
ATOM   13567 C CG2 . THR I 3 75  ? 78.550  104.350 22.277  1.000 74.529  ? 75  THR GGG CG2 1 
ATOM   13568 N N   . ASP I 3 76  ? 76.304  103.481 26.413  1.000 83.032  ? 76  ASP GGG N   1 
ATOM   13569 C CA  . ASP I 3 76  ? 76.237  102.876 27.774  1.000 79.926  ? 76  ASP GGG CA  1 
ATOM   13570 C C   . ASP I 3 76  ? 74.763  102.747 28.171  1.000 70.901  ? 76  ASP GGG C   1 
ATOM   13571 O O   . ASP I 3 76  ? 74.074  103.774 28.225  1.000 67.311  ? 76  ASP GGG O   1 
ATOM   13572 C CB  . ASP I 3 76  ? 77.100  103.638 28.785  1.000 82.248  ? 76  ASP GGG CB  1 
ATOM   13573 C CG  . ASP I 3 76  ? 78.583  103.652 28.420  1.000 89.163  ? 76  ASP GGG CG  1 
ATOM   13574 O OD1 . ASP I 3 76  ? 79.146  104.759 28.324  1.000 93.068  ? 76  ASP GGG OD1 1 
ATOM   13575 O OD2 . ASP I 3 76  ? 79.171  102.558 28.221  1.000 87.789  ? 76  ASP GGG OD2 1 
ATOM   13576 N N   . PHE I 3 77  ? 74.307  101.510 28.391  1.000 66.238  ? 77  PHE GGG N   1 
ATOM   13577 C CA  . PHE I 3 77  ? 72.897  101.137 28.683  1.000 60.124  ? 77  PHE GGG CA  1 
ATOM   13578 C C   . PHE I 3 77  ? 72.832  100.253 29.927  1.000 59.938  ? 77  PHE GGG C   1 
ATOM   13579 O O   . PHE I 3 77  ? 73.824  99.570  30.250  1.000 59.966  ? 77  PHE GGG O   1 
ATOM   13580 C CB  . PHE I 3 77  ? 72.267  100.422 27.491  1.000 55.845  ? 77  PHE GGG CB  1 
ATOM   13581 C CG  . PHE I 3 77  ? 72.182  101.283 26.262  1.000 59.423  ? 77  PHE GGG CG  1 
ATOM   13582 C CD1 . PHE I 3 77  ? 71.117  102.154 26.079  1.000 56.624  ? 77  PHE GGG CD1 1 
ATOM   13583 C CD2 . PHE I 3 77  ? 73.173  101.224 25.289  1.000 63.387  ? 77  PHE GGG CD2 1 
ATOM   13584 C CE1 . PHE I 3 77  ? 71.046  102.950 24.944  1.000 55.591  ? 77  PHE GGG CE1 1 
ATOM   13585 C CE2 . PHE I 3 77  ? 73.100  102.016 24.151  1.000 61.498  ? 77  PHE GGG CE2 1 
ATOM   13586 C CZ  . PHE I 3 77  ? 72.036  102.877 23.981  1.000 57.797  ? 77  PHE GGG CZ  1 
ATOM   13587 N N   . THR I 3 78  ? 71.679  100.270 30.594  1.000 60.976  ? 78  THR GGG N   1 
ATOM   13588 C CA  . THR I 3 78  ? 71.458  99.596  31.893  1.000 60.881  ? 78  THR GGG CA  1 
ATOM   13589 C C   . THR I 3 78  ? 70.061  98.990  31.936  1.000 60.691  ? 78  THR GGG C   1 
ATOM   13590 O O   . THR I 3 78  ? 69.091  99.712  31.632  1.000 57.137  ? 78  THR GGG O   1 
ATOM   13591 C CB  . THR I 3 78  ? 71.694  100.566 33.054  1.000 65.905  ? 78  THR GGG CB  1 
ATOM   13592 O OG1 . THR I 3 78  ? 73.113  100.696 33.162  1.000 65.395  ? 78  THR GGG OG1 1 
ATOM   13593 C CG2 . THR I 3 78  ? 71.117  100.105 34.377  1.000 70.235  ? 78  THR GGG CG2 1 
ATOM   13594 N N   . LEU I 3 79  ? 70.000  97.703  32.290  1.000 60.536  ? 79  LEU GGG N   1 
ATOM   13595 C CA  . LEU I 3 79  ? 68.775  97.025  32.780  1.000 60.451  ? 79  LEU GGG CA  1 
ATOM   13596 C C   . LEU I 3 79  ? 68.837  96.958  34.308  1.000 57.805  ? 79  LEU GGG C   1 
ATOM   13597 O O   . LEU I 3 79  ? 69.886  96.566  34.865  1.000 48.340  ? 79  LEU GGG O   1 
ATOM   13598 C CB  . LEU I 3 79  ? 68.654  95.626  32.168  1.000 58.470  ? 79  LEU GGG CB  1 
ATOM   13599 C CG  . LEU I 3 79  ? 67.380  94.874  32.534  1.000 54.265  ? 79  LEU GGG CG  1 
ATOM   13600 C CD1 . LEU I 3 79  ? 66.162  95.564  31.955  1.000 53.270  ? 79  LEU GGG CD1 1 
ATOM   13601 C CD2 . LEU I 3 79  ? 67.448  93.450  32.042  1.000 55.461  ? 79  LEU GGG CD2 1 
ATOM   13602 N N   . THR I 3 80  ? 67.742  97.342  34.956  1.000 60.529  ? 80  THR GGG N   1 
ATOM   13603 C CA  . THR I 3 80  ? 67.621  97.391  36.430  1.000 62.412  ? 80  THR GGG CA  1 
ATOM   13604 C C   . THR I 3 80  ? 66.372  96.633  36.860  1.000 62.051  ? 80  THR GGG C   1 
ATOM   13605 O O   . THR I 3 80  ? 65.275  96.959  36.364  1.000 59.750  ? 80  THR GGG O   1 
ATOM   13606 C CB  . THR I 3 80  ? 67.546  98.826  36.956  1.000 62.066  ? 80  THR GGG CB  1 
ATOM   13607 O OG1 . THR I 3 80  ? 68.696  99.538  36.497  1.000 64.630  ? 80  THR GGG OG1 1 
ATOM   13608 C CG2 . THR I 3 80  ? 67.483  98.872  38.468  1.000 63.832  ? 80  THR GGG CG2 1 
ATOM   13609 N N   . ILE I 3 81  ? 66.560  95.671  37.759  1.000 62.622  ? 81  ILE GGG N   1 
ATOM   13610 C CA  . ILE I 3 81  ? 65.459  95.015  38.514  1.000 66.235  ? 81  ILE GGG CA  1 
ATOM   13611 C C   . ILE I 3 81  ? 65.550  95.535  39.944  1.000 70.840  ? 81  ILE GGG C   1 
ATOM   13612 O O   . ILE I 3 81  ? 66.497  95.151  40.627  1.000 70.264  ? 81  ILE GGG O   1 
ATOM   13613 C CB  . ILE I 3 81  ? 65.562  93.479  38.444  1.000 67.641  ? 81  ILE GGG CB  1 
ATOM   13614 C CG1 . ILE I 3 81  ? 65.812  92.972  37.021  1.000 65.705  ? 81  ILE GGG CG1 1 
ATOM   13615 C CG2 . ILE I 3 81  ? 64.320  92.851  39.063  1.000 71.706  ? 81  ILE GGG CG2 1 
ATOM   13616 C CD1 . ILE I 3 81  ? 66.003  91.477  36.932  1.000 68.698  ? 81  ILE GGG CD1 1 
ATOM   13617 N N   . SER I 3 82  ? 64.663  96.446  40.336  1.000 79.159  ? 82  SER GGG N   1 
ATOM   13618 C CA  . SER I 3 82  ? 64.373  96.756  41.754  1.000 82.925  ? 82  SER GGG CA  1 
ATOM   13619 C C   . SER I 3 82  ? 63.521  95.606  42.300  1.000 81.538  ? 82  SER GGG C   1 
ATOM   13620 O O   . SER I 3 82  ? 62.726  95.079  41.526  1.000 76.154  ? 82  SER GGG O   1 
ATOM   13621 C CB  . SER I 3 82  ? 63.653  98.057  41.851  1.000 85.205  ? 82  SER GGG CB  1 
ATOM   13622 O OG  . SER I 3 82  ? 62.484  98.011  41.047  1.000 85.931  ? 82  SER GGG OG  1 
ATOM   13623 N N   . SER I 3 83  ? 63.686  95.220  43.572  1.000 82.617  ? 83  SER GGG N   1 
ATOM   13624 C CA  . SER I 3 83  ? 62.909  94.136  44.246  1.000 80.283  ? 83  SER GGG CA  1 
ATOM   13625 C C   . SER I 3 83  ? 63.003  92.835  43.450  1.000 76.582  ? 83  SER GGG C   1 
ATOM   13626 O O   . SER I 3 83  ? 62.006  92.454  42.800  1.000 70.497  ? 83  SER GGG O   1 
ATOM   13627 C CB  . SER I 3 83  ? 61.457  94.510  44.439  1.000 82.835  ? 83  SER GGG CB  1 
ATOM   13628 O OG  . SER I 3 83  ? 61.270  95.190  45.673  1.000 90.631  ? 83  SER GGG OG  1 
ATOM   13629 N N   . LEU I 3 84  ? 64.157  92.173  43.498  1.000 74.441  ? 84  LEU GGG N   1 
ATOM   13630 C CA  . LEU I 3 84  ? 64.328  90.871  42.827  1.000 66.004  ? 84  LEU GGG CA  1 
ATOM   13631 C C   . LEU I 3 84  ? 63.308  89.908  43.427  1.000 66.438  ? 84  LEU GGG C   1 
ATOM   13632 O O   . LEU I 3 84  ? 63.148  89.887  44.660  1.000 59.810  ? 84  LEU GGG O   1 
ATOM   13633 C CB  . LEU I 3 84  ? 65.758  90.381  43.016  1.000 61.597  ? 84  LEU GGG CB  1 
ATOM   13634 C CG  . LEU I 3 84  ? 66.179  89.272  42.066  1.000 64.603  ? 84  LEU GGG CG  1 
ATOM   13635 C CD1 . LEU I 3 84  ? 66.177  89.740  40.617  1.000 64.316  ? 84  LEU GGG CD1 1 
ATOM   13636 C CD2 . LEU I 3 84  ? 67.563  88.757  42.445  1.000 67.865  ? 84  LEU GGG CD2 1 
ATOM   13637 N N   . GLN I 3 85  ? 62.604  89.189  42.564  1.000 72.915  ? 85  GLN GGG N   1 
ATOM   13638 C CA  . GLN I 3 85  ? 61.592  88.169  42.947  1.000 78.662  ? 85  GLN GGG CA  1 
ATOM   13639 C C   . GLN I 3 85  ? 62.189  86.791  42.654  1.000 80.146  ? 85  GLN GGG C   1 
ATOM   13640 O O   . GLN I 3 85  ? 63.144  86.725  41.860  1.000 81.560  ? 85  GLN GGG O   1 
ATOM   13641 C CB  . GLN I 3 85  ? 60.305  88.401  42.157  1.000 80.131  ? 85  GLN GGG CB  1 
ATOM   13642 C CG  . GLN I 3 85  ? 59.729  89.791  42.372  1.000 79.747  ? 85  GLN GGG CG  1 
ATOM   13643 C CD  . GLN I 3 85  ? 59.326  90.015  43.798  1.000 78.472  ? 85  GLN GGG CD  1 
ATOM   13644 O OE1 . GLN I 3 85  ? 58.711  89.156  44.415  1.000 78.823  ? 85  GLN GGG OE1 1 
ATOM   13645 N NE2 . GLN I 3 85  ? 59.627  91.196  44.311  1.000 83.567  ? 85  GLN GGG NE2 1 
ATOM   13646 N N   . ALA I 3 86  ? 61.654  85.733  43.270  1.000 82.904  ? 86  ALA GGG N   1 
ATOM   13647 C CA  . ALA I 3 86  ? 62.125  84.335  43.108  1.000 79.954  ? 86  ALA GGG CA  1 
ATOM   13648 C C   . ALA I 3 86  ? 62.218  83.983  41.613  1.000 68.781  ? 86  ALA GGG C   1 
ATOM   13649 O O   . ALA I 3 86  ? 63.222  83.378  41.157  1.000 52.758  ? 86  ALA GGG O   1 
ATOM   13650 C CB  . ALA I 3 86  ? 61.157  83.423  43.828  1.000 85.248  ? 86  ALA GGG CB  1 
ATOM   13651 N N   . GLU I 3 87  ? 61.210  84.456  40.891  1.000 67.324  ? 87  GLU GGG N   1 
ATOM   13652 C CA  . GLU I 3 87  ? 60.866  84.128  39.491  1.000 67.469  ? 87  GLU GGG CA  1 
ATOM   13653 C C   . GLU I 3 87  ? 61.696  84.974  38.529  1.000 57.537  ? 87  GLU GGG C   1 
ATOM   13654 O O   . GLU I 3 87  ? 61.417  84.916  37.331  1.000 58.916  ? 87  GLU GGG O   1 
ATOM   13655 C CB  . GLU I 3 87  ? 59.375  84.406  39.327  1.000 78.573  ? 87  GLU GGG CB  1 
ATOM   13656 C CG  . GLU I 3 87  ? 58.824  85.307  40.434  1.000 88.162  ? 87  GLU GGG CG  1 
ATOM   13657 C CD  . GLU I 3 87  ? 57.467  85.926  40.149  1.000 94.360  ? 87  GLU GGG CD  1 
ATOM   13658 O OE1 . GLU I 3 87  ? 56.680  85.312  39.388  1.000 93.887  ? 87  GLU GGG OE1 1 
ATOM   13659 O OE2 . GLU I 3 87  ? 57.189  87.030  40.692  1.000 94.365  ? 87  GLU GGG OE2 1 
ATOM   13660 N N   . ASP I 3 88  ? 62.641  85.764  39.033  1.000 52.498  ? 88  ASP GGG N   1 
ATOM   13661 C CA  . ASP I 3 88  ? 63.494  86.640  38.186  1.000 53.020  ? 88  ASP GGG CA  1 
ATOM   13662 C C   . ASP I 3 88  ? 64.830  85.952  37.907  1.000 47.091  ? 88  ASP GGG C   1 
ATOM   13663 O O   . ASP I 3 88  ? 65.588  86.445  37.046  1.000 42.313  ? 88  ASP GGG O   1 
ATOM   13664 C CB  . ASP I 3 88  ? 63.654  88.022  38.816  1.000 53.976  ? 88  ASP GGG CB  1 
ATOM   13665 C CG  . ASP I 3 88  ? 62.371  88.831  38.711  1.000 57.090  ? 88  ASP GGG CG  1 
ATOM   13666 O OD1 . ASP I 3 88  ? 61.604  88.592  37.737  1.000 51.592  ? 88  ASP GGG OD1 1 
ATOM   13667 O OD2 . ASP I 3 88  ? 62.166  89.707  39.582  1.000 60.752  ? 88  ASP GGG OD2 1 
ATOM   13668 N N   . VAL I 3 89  ? 65.106  84.852  38.599  1.000 45.353  ? 89  VAL GGG N   1 
ATOM   13669 C CA  . VAL I 3 89  ? 66.329  84.045  38.348  1.000 48.161  ? 89  VAL GGG CA  1 
ATOM   13670 C C   . VAL I 3 89  ? 66.325  83.648  36.874  1.000 46.215  ? 89  VAL GGG C   1 
ATOM   13671 O O   . VAL I 3 89  ? 65.506  82.800  36.493  1.000 44.020  ? 89  VAL GGG O   1 
ATOM   13672 C CB  . VAL I 3 89  ? 66.380  82.781  39.221  1.000 57.031  ? 89  VAL GGG CB  1 
ATOM   13673 C CG1 . VAL I 3 89  ? 67.541  81.880  38.810  1.000 59.683  ? 89  VAL GGG CG1 1 
ATOM   13674 C CG2 . VAL I 3 89  ? 66.424  83.108  40.705  1.000 62.320  ? 89  VAL GGG CG2 1 
ATOM   13675 N N   . ALA I 3 90  ? 67.217  84.225  36.076  1.000 45.902  ? 90  ALA GGG N   1 
ATOM   13676 C CA  . ALA I 3 90  ? 67.315  83.940  34.626  1.000 43.019  ? 90  ALA GGG CA  1 
ATOM   13677 C C   . ALA I 3 90  ? 68.620  84.479  34.073  1.000 39.880  ? 90  ALA GGG C   1 
ATOM   13678 O O   . ALA I 3 90  ? 69.375  85.088  34.830  1.000 46.772  ? 90  ALA GGG O   1 
ATOM   13679 C CB  . ALA I 3 90  ? 66.160  84.566  33.908  1.000 45.300  ? 90  ALA GGG CB  1 
ATOM   13680 N N   . VAL I 3 91  ? 68.860  84.258  32.794  1.000 35.772  ? 91  VAL GGG N   1 
ATOM   13681 C CA  . VAL I 3 91  ? 69.937  84.974  32.070  1.000 38.128  ? 91  VAL GGG CA  1 
ATOM   13682 C C   . VAL I 3 91  ? 69.290  86.136  31.321  1.000 39.342  ? 91  VAL GGG C   1 
ATOM   13683 O O   . VAL I 3 91  ? 68.179  85.956  30.795  1.000 41.258  ? 91  VAL GGG O   1 
ATOM   13684 C CB  . VAL I 3 91  ? 70.709  84.029  31.139  1.000 38.308  ? 91  VAL GGG CB  1 
ATOM   13685 C CG1 . VAL I 3 91  ? 71.742  84.778  30.327  1.000 39.803  ? 91  VAL GGG CG1 1 
ATOM   13686 C CG2 . VAL I 3 91  ? 71.367  82.920  31.925  1.000 38.482  ? 91  VAL GGG CG2 1 
ATOM   13687 N N   . TYR I 3 92  ? 69.955  87.287  31.303  1.000 39.321  ? 92  TYR GGG N   1 
ATOM   13688 C CA  . TYR I 3 92  ? 69.486  88.510  30.614  1.000 39.725  ? 92  TYR GGG CA  1 
ATOM   13689 C C   . TYR I 3 92  ? 70.517  88.873  29.548  1.000 43.008  ? 92  TYR GGG C   1 
ATOM   13690 O O   . TYR I 3 92  ? 71.713  89.009  29.885  1.000 40.382  ? 92  TYR GGG O   1 
ATOM   13691 C CB  . TYR I 3 92  ? 69.241  89.623  31.629  1.000 38.344  ? 92  TYR GGG CB  1 
ATOM   13692 C CG  . TYR I 3 92  ? 68.146  89.314  32.612  1.000 39.883  ? 92  TYR GGG CG  1 
ATOM   13693 C CD1 . TYR I 3 92  ? 68.411  88.618  33.783  1.000 41.740  ? 92  TYR GGG CD1 1 
ATOM   13694 C CD2 . TYR I 3 92  ? 66.838  89.696  32.368  1.000 39.109  ? 92  TYR GGG CD2 1 
ATOM   13695 C CE1 . TYR I 3 92  ? 67.407  88.315  34.693  1.000 43.062  ? 92  TYR GGG CE1 1 
ATOM   13696 C CE2 . TYR I 3 92  ? 65.828  89.408  33.267  1.000 40.076  ? 92  TYR GGG CE2 1 
ATOM   13697 C CZ  . TYR I 3 92  ? 66.107  88.703  34.426  1.000 43.129  ? 92  TYR GGG CZ  1 
ATOM   13698 O OH  . TYR I 3 92  ? 65.113  88.388  35.312  1.000 43.788  ? 92  TYR GGG OH  1 
ATOM   13699 N N   . TYR I 3 93  ? 70.060  88.977  28.297  1.000 45.288  ? 93  TYR GGG N   1 
ATOM   13700 C CA  . TYR I 3 93  ? 70.868  89.423  27.136  1.000 46.077  ? 93  TYR GGG CA  1 
ATOM   13701 C C   . TYR I 3 93  ? 70.372  90.801  26.679  1.000 50.455  ? 93  TYR GGG C   1 
ATOM   13702 O O   . TYR I 3 93  ? 69.157  91.012  26.616  1.000 49.592  ? 93  TYR GGG O   1 
ATOM   13703 C CB  . TYR I 3 93  ? 70.780  88.421  25.983  1.000 43.569  ? 93  TYR GGG CB  1 
ATOM   13704 C CG  . TYR I 3 93  ? 71.125  86.992  26.320  1.000 42.107  ? 93  TYR GGG CG  1 
ATOM   13705 C CD1 . TYR I 3 93  ? 72.387  86.464  26.090  1.000 40.668  ? 93  TYR GGG CD1 1 
ATOM   13706 C CD2 . TYR I 3 93  ? 70.161  86.150  26.833  1.000 42.822  ? 93  TYR GGG CD2 1 
ATOM   13707 C CE1 . TYR I 3 93  ? 72.689  85.142  26.379  1.000 39.899  ? 93  TYR GGG CE1 1 
ATOM   13708 C CE2 . TYR I 3 93  ? 70.447  84.831  27.135  1.000 45.133  ? 93  TYR GGG CE2 1 
ATOM   13709 C CZ  . TYR I 3 93  ? 71.711  84.318  26.906  1.000 42.719  ? 93  TYR GGG CZ  1 
ATOM   13710 O OH  . TYR I 3 93  ? 71.926  83.000  27.214  1.000 41.110  ? 93  TYR GGG OH  1 
ATOM   13711 N N   . CYS I 3 94  ? 71.299  91.717  26.392  1.000 56.424  ? 94  CYS GGG N   1 
ATOM   13712 C CA  . CYS I 3 94  ? 71.043  92.945  25.606  1.000 56.414  ? 94  CYS GGG CA  1 
ATOM   13713 C C   . CYS I 3 94  ? 71.263  92.602  24.135  1.000 51.496  ? 94  CYS GGG C   1 
ATOM   13714 O O   . CYS I 3 94  ? 72.092  91.734  23.842  1.000 49.780  ? 94  CYS GGG O   1 
ATOM   13715 C CB  . CYS I 3 94  ? 71.903  94.125  26.051  1.000 67.163  ? 94  CYS GGG CB  1 
ATOM   13716 S SG  . CYS I 3 94  ? 73.697  93.932  25.851  1.000 84.420  ? 94  CYS GGG SG  1 
ATOM   13717 N N   . GLN I 3 95  ? 70.489  93.225  23.259  1.000 49.599  ? 95  GLN GGG N   1 
ATOM   13718 C CA  . GLN I 3 95  ? 70.590  93.048  21.793  1.000 49.233  ? 95  GLN GGG CA  1 
ATOM   13719 C C   . GLN I 3 95  ? 70.411  94.430  21.174  1.000 50.558  ? 95  GLN GGG C   1 
ATOM   13720 O O   . GLN I 3 95  ? 69.472  95.129  21.610  1.000 51.048  ? 95  GLN GGG O   1 
ATOM   13721 C CB  . GLN I 3 95  ? 69.519  92.079  21.285  1.000 46.580  ? 95  GLN GGG CB  1 
ATOM   13722 C CG  . GLN I 3 95  ? 69.501  91.858  19.776  1.000 45.031  ? 95  GLN GGG CG  1 
ATOM   13723 C CD  . GLN I 3 95  ? 68.119  91.990  19.173  1.000 47.397  ? 95  GLN GGG CD  1 
ATOM   13724 O OE1 . GLN I 3 95  ? 67.134  92.263  19.852  1.000 49.101  ? 95  GLN GGG OE1 1 
ATOM   13725 N NE2 . GLN I 3 95  ? 68.016  91.811  17.870  1.000 49.528  ? 95  GLN GGG NE2 1 
ATOM   13726 N N   . GLN I 3 96  ? 71.272  94.790  20.216  1.000 49.013  ? 96  GLN GGG N   1 
ATOM   13727 C CA  . GLN I 3 96  ? 71.092  95.961  19.319  1.000 46.655  ? 96  GLN GGG CA  1 
ATOM   13728 C C   . GLN I 3 96  ? 70.328  95.506  18.072  1.000 50.784  ? 96  GLN GGG C   1 
ATOM   13729 O O   . GLN I 3 96  ? 70.636  94.433  17.531  1.000 57.532  ? 96  GLN GGG O   1 
ATOM   13730 C CB  . GLN I 3 96  ? 72.440  96.593  18.976  1.000 45.401  ? 96  GLN GGG CB  1 
ATOM   13731 C CG  . GLN I 3 96  ? 73.326  95.760  18.058  1.000 48.150  ? 96  GLN GGG CG  1 
ATOM   13732 C CD  . GLN I 3 96  ? 73.050  95.936  16.581  1.000 48.221  ? 96  GLN GGG CD  1 
ATOM   13733 O OE1 . GLN I 3 96  ? 72.223  96.743  16.164  1.000 45.919  ? 96  GLN GGG OE1 1 
ATOM   13734 N NE2 . GLN I 3 96  ? 73.739  95.146  15.772  1.000 46.984  ? 96  GLN GGG NE2 1 
ATOM   13735 N N   . TYR I 3 97  ? 69.347  96.293  17.646  1.000 55.682  ? 97  TYR GGG N   1 
ATOM   13736 C CA  . TYR I 3 97  ? 68.620  96.111  16.366  1.000 61.020  ? 97  TYR GGG CA  1 
ATOM   13737 C C   . TYR I 3 97  ? 68.691  97.414  15.567  1.000 66.647  ? 97  TYR GGG C   1 
ATOM   13738 O O   . TYR I 3 97  ? 67.708  97.761  14.887  1.000 66.595  ? 97  TYR GGG O   1 
ATOM   13739 C CB  . TYR I 3 97  ? 67.188  95.642  16.628  1.000 64.095  ? 97  TYR GGG CB  1 
ATOM   13740 C CG  . TYR I 3 97  ? 66.349  96.488  17.557  1.000 60.818  ? 97  TYR GGG CG  1 
ATOM   13741 C CD1 . TYR I 3 97  ? 66.477  96.408  18.938  1.000 59.278  ? 97  TYR GGG CD1 1 
ATOM   13742 C CD2 . TYR I 3 97  ? 65.359  97.315  17.053  1.000 60.285  ? 97  TYR GGG CD2 1 
ATOM   13743 C CE1 . TYR I 3 97  ? 65.673  97.153  19.786  1.000 55.512  ? 97  TYR GGG CE1 1 
ATOM   13744 C CE2 . TYR I 3 97  ? 64.552  98.072  17.885  1.000 61.090  ? 97  TYR GGG CE2 1 
ATOM   13745 C CZ  . TYR I 3 97  ? 64.700  97.980  19.257  1.000 58.893  ? 97  TYR GGG CZ  1 
ATOM   13746 O OH  . TYR I 3 97  ? 63.885  98.722  20.061  1.000 64.042  ? 97  TYR GGG OH  1 
ATOM   13747 N N   . TYR I 3 98  ? 69.831  98.107  15.658  1.000 71.531  ? 98  TYR GGG N   1 
ATOM   13748 C CA  . TYR I 3 98  ? 70.116  99.368  14.928  1.000 69.860  ? 98  TYR GGG CA  1 
ATOM   13749 C C   . TYR I 3 98  ? 70.358  99.017  13.458  1.000 65.877  ? 98  TYR GGG C   1 
ATOM   13750 O O   . TYR I 3 98  ? 69.719  99.627  12.577  1.000 75.080  ? 98  TYR GGG O   1 
ATOM   13751 C CB  . TYR I 3 98  ? 71.297  100.122 15.553  1.000 79.656  ? 98  TYR GGG CB  1 
ATOM   13752 C CG  . TYR I 3 98  ? 71.725  101.333 14.763  1.000 85.745  ? 98  TYR GGG CG  1 
ATOM   13753 C CD1 . TYR I 3 98  ? 70.957  102.485 14.740  1.000 85.302  ? 98  TYR GGG CD1 1 
ATOM   13754 C CD2 . TYR I 3 98  ? 72.878  101.310 13.999  1.000 93.771  ? 98  TYR GGG CD2 1 
ATOM   13755 C CE1 . TYR I 3 98  ? 71.312  103.574 13.962  1.000 85.748  ? 98  TYR GGG CE1 1 
ATOM   13756 C CE2 . TYR I 3 98  ? 73.256  102.393 13.223  1.000 93.969  ? 98  TYR GGG CE2 1 
ATOM   13757 C CZ  . TYR I 3 98  ? 72.470  103.530 13.209  1.000 89.208  ? 98  TYR GGG CZ  1 
ATOM   13758 O OH  . TYR I 3 98  ? 72.845  104.602 12.461  1.000 95.888  ? 98  TYR GGG OH  1 
ATOM   13759 N N   . SER I 3 99  ? 71.240  98.049  13.210  1.000 59.434  ? 99  SER GGG N   1 
ATOM   13760 C CA  . SER I 3 99  ? 71.625  97.594  11.851  1.000 64.729  ? 99  SER GGG CA  1 
ATOM   13761 C C   . SER I 3 99  ? 71.898  96.087  11.859  1.000 65.365  ? 99  SER GGG C   1 
ATOM   13762 O O   . SER I 3 99  ? 72.490  95.599  12.850  1.000 66.667  ? 99  SER GGG O   1 
ATOM   13763 C CB  . SER I 3 99  ? 72.833  98.355  11.367  1.000 71.164  ? 99  SER GGG CB  1 
ATOM   13764 O OG  . SER I 3 99  ? 73.961  98.069  12.186  1.000 74.536  ? 99  SER GGG OG  1 
ATOM   13765 N N   . THR I 3 100 ? 71.514  95.391  10.783  1.000 58.264  ? 100 THR GGG N   1 
ATOM   13766 C CA  . THR I 3 100 ? 71.925  93.993  10.511  1.000 54.082  ? 100 THR GGG CA  1 
ATOM   13767 C C   . THR I 3 100 ? 73.418  94.024  10.235  1.000 57.213  ? 100 THR GGG C   1 
ATOM   13768 O O   . THR I 3 100 ? 73.871  94.923  9.544   1.000 64.337  ? 100 THR GGG O   1 
ATOM   13769 C CB  . THR I 3 100 ? 71.162  93.375  9.334   1.000 51.402  ? 100 THR GGG CB  1 
ATOM   13770 O OG1 . THR I 3 100 ? 71.664  93.936  8.125   1.000 49.009  ? 100 THR GGG OG1 1 
ATOM   13771 C CG2 . THR I 3 100 ? 69.670  93.590  9.410   1.000 49.201  ? 100 THR GGG CG2 1 
ATOM   13772 N N   . PRO I 3 101 ? 74.242  93.103  10.779  1.000 65.498  ? 101 PRO GGG N   1 
ATOM   13773 C CA  . PRO I 3 101 ? 73.776  91.989  11.605  1.000 68.204  ? 101 PRO GGG CA  1 
ATOM   13774 C C   . PRO I 3 101 ? 73.449  92.367  13.059  1.000 63.364  ? 101 PRO GGG C   1 
ATOM   13775 O O   . PRO I 3 101 ? 74.306  92.938  13.718  1.000 58.514  ? 101 PRO GGG O   1 
ATOM   13776 C CB  . PRO I 3 101 ? 74.994  91.055  11.606  1.000 75.892  ? 101 PRO GGG CB  1 
ATOM   13777 C CG  . PRO I 3 101 ? 76.182  92.003  11.543  1.000 75.354  ? 101 PRO GGG CG  1 
ATOM   13778 C CD  . PRO I 3 101 ? 75.707  93.133  10.656  1.000 72.342  ? 101 PRO GGG CD  1 
ATOM   13779 N N   . TYR I 3 102 ? 72.243  92.025  13.533  1.000 57.647  ? 102 TYR GGG N   1 
ATOM   13780 C CA  . TYR I 3 102 ? 71.842  92.214  14.950  1.000 53.395  ? 102 TYR GGG CA  1 
ATOM   13781 C C   . TYR I 3 102 ? 72.856  91.465  15.801  1.000 47.753  ? 102 TYR GGG C   1 
ATOM   13782 O O   . TYR I 3 102 ? 73.441  90.502  15.285  1.000 49.928  ? 102 TYR GGG O   1 
ATOM   13783 C CB  . TYR I 3 102 ? 70.454  91.660  15.256  1.000 56.286  ? 102 TYR GGG CB  1 
ATOM   13784 C CG  . TYR I 3 102 ? 69.272  92.234  14.510  1.000 61.330  ? 102 TYR GGG CG  1 
ATOM   13785 C CD1 . TYR I 3 102 ? 68.029  91.635  14.652  1.000 68.802  ? 102 TYR GGG CD1 1 
ATOM   13786 C CD2 . TYR I 3 102 ? 69.351  93.344  13.683  1.000 60.843  ? 102 TYR GGG CD2 1 
ATOM   13787 C CE1 . TYR I 3 102 ? 66.902  92.113  14.007  1.000 68.671  ? 102 TYR GGG CE1 1 
ATOM   13788 C CE2 . TYR I 3 102 ? 68.234  93.830  13.016  1.000 59.658  ? 102 TYR GGG CE2 1 
ATOM   13789 C CZ  . TYR I 3 102 ? 67.006  93.206  13.169  1.000 64.439  ? 102 TYR GGG CZ  1 
ATOM   13790 O OH  . TYR I 3 102 ? 65.874  93.636  12.535  1.000 67.657  ? 102 TYR GGG OH  1 
ATOM   13791 N N   . THR I 3 103 ? 73.075  91.890  17.040  1.000 45.922  ? 103 THR GGG N   1 
ATOM   13792 C CA  . THR I 3 103 ? 74.069  91.240  17.934  1.000 54.651  ? 103 THR GGG CA  1 
ATOM   13793 C C   . THR I 3 103 ? 73.605  91.281  19.393  1.000 50.418  ? 103 THR GGG C   1 
ATOM   13794 O O   . THR I 3 103 ? 72.976  92.260  19.779  1.000 45.843  ? 103 THR GGG O   1 
ATOM   13795 C CB  . THR I 3 103 ? 75.472  91.833  17.742  1.000 58.605  ? 103 THR GGG CB  1 
ATOM   13796 O OG1 . THR I 3 103 ? 75.366  93.258  17.735  1.000 58.518  ? 103 THR GGG OG1 1 
ATOM   13797 C CG2 . THR I 3 103 ? 76.139  91.340  16.473  1.000 58.469  ? 103 THR GGG CG2 1 
ATOM   13798 N N   . PHE I 3 104 ? 73.897  90.214  20.135  1.000 46.576  ? 104 PHE GGG N   1 
ATOM   13799 C CA  . PHE I 3 104 ? 73.519  90.014  21.550  1.000 41.358  ? 104 PHE GGG CA  1 
ATOM   13800 C C   . PHE I 3 104 ? 74.771  90.195  22.392  1.000 40.158  ? 104 PHE GGG C   1 
ATOM   13801 O O   . PHE I 3 104 ? 75.855  89.933  21.876  1.000 39.391  ? 104 PHE GGG O   1 
ATOM   13802 C CB  . PHE I 3 104 ? 72.994  88.594  21.784  1.000 42.704  ? 104 PHE GGG CB  1 
ATOM   13803 C CG  . PHE I 3 104 ? 71.656  88.264  21.171  1.000 41.386  ? 104 PHE GGG CG  1 
ATOM   13804 C CD1 . PHE I 3 104 ? 71.575  87.493  20.025  1.000 38.280  ? 104 PHE GGG CD1 1 
ATOM   13805 C CD2 . PHE I 3 104 ? 70.480  88.692  21.773  1.000 41.730  ? 104 PHE GGG CD2 1 
ATOM   13806 C CE1 . PHE I 3 104 ? 70.342  87.188  19.478  1.000 40.375  ? 104 PHE GGG CE1 1 
ATOM   13807 C CE2 . PHE I 3 104 ? 69.247  88.384  21.224  1.000 42.207  ? 104 PHE GGG CE2 1 
ATOM   13808 C CZ  . PHE I 3 104 ? 69.181  87.630  20.077  1.000 42.593  ? 104 PHE GGG CZ  1 
ATOM   13809 N N   . GLY I 3 105 ? 74.604  90.571  23.656  1.000 44.728  ? 105 GLY GGG N   1 
ATOM   13810 C CA  . GLY I 3 105 ? 75.644  90.460  24.698  1.000 47.223  ? 105 GLY GGG CA  1 
ATOM   13811 C C   . GLY I 3 105 ? 75.940  89.001  24.994  1.000 51.409  ? 105 GLY GGG C   1 
ATOM   13812 O O   . GLY I 3 105 ? 75.180  88.125  24.519  1.000 52.103  ? 105 GLY GGG O   1 
ATOM   13813 N N   . GLN I 3 106 ? 77.002  88.733  25.750  1.000 57.498  ? 106 GLN GGG N   1 
ATOM   13814 C CA  . GLN I 3 106 ? 77.406  87.354  26.139  1.000 59.949  ? 106 GLN GGG CA  1 
ATOM   13815 C C   . GLN I 3 106 ? 76.391  86.807  27.154  1.000 55.347  ? 106 GLN GGG C   1 
ATOM   13816 O O   . GLN I 3 106 ? 76.315  85.580  27.306  1.000 60.872  ? 106 GLN GGG O   1 
ATOM   13817 C CB  . GLN I 3 106 ? 78.854  87.330  26.649  1.000 66.831  ? 106 GLN GGG CB  1 
ATOM   13818 C CG  . GLN I 3 106 ? 79.058  87.873  28.062  1.000 72.425  ? 106 GLN GGG CG  1 
ATOM   13819 C CD  . GLN I 3 106 ? 79.151  89.380  28.120  1.000 80.406  ? 106 GLN GGG CD  1 
ATOM   13820 O OE1 . GLN I 3 106 ? 79.057  90.075  27.102  1.000 87.409  ? 106 GLN GGG OE1 1 
ATOM   13821 N NE2 . GLN I 3 106 ? 79.296  89.893  29.329  1.000 83.221  ? 106 GLN GGG NE2 1 
ATOM   13822 N N   . GLY I 3 107 ? 75.623  87.682  27.806  1.000 52.055  ? 107 GLY GGG N   1 
ATOM   13823 C CA  . GLY I 3 107 ? 74.565  87.295  28.760  1.000 51.887  ? 107 GLY GGG CA  1 
ATOM   13824 C C   . GLY I 3 107 ? 74.983  87.569  30.193  1.000 49.199  ? 107 GLY GGG C   1 
ATOM   13825 O O   . GLY I 3 107 ? 76.187  87.617  30.447  1.000 50.987  ? 107 GLY GGG O   1 
ATOM   13826 N N   . THR I 3 108 ? 74.016  87.775  31.085  1.000 47.104  ? 108 THR GGG N   1 
ATOM   13827 C CA  . THR I 3 108 ? 74.251  87.995  32.529  1.000 49.136  ? 108 THR GGG CA  1 
ATOM   13828 C C   . THR I 3 108 ? 73.376  87.047  33.347  1.000 48.763  ? 108 THR GGG C   1 
ATOM   13829 O O   . THR I 3 108 ? 72.168  87.263  33.398  1.000 47.048  ? 108 THR GGG O   1 
ATOM   13830 C CB  . THR I 3 108 ? 74.019  89.462  32.884  1.000 51.810  ? 108 THR GGG CB  1 
ATOM   13831 O OG1 . THR I 3 108 ? 75.016  90.186  32.159  1.000 55.311  ? 108 THR GGG OG1 1 
ATOM   13832 C CG2 . THR I 3 108 ? 74.118  89.733  34.368  1.000 50.076  ? 108 THR GGG CG2 1 
ATOM   13833 N N   . LYS I 3 109 ? 73.998  86.037  33.953  1.000 54.925  ? 109 LYS GGG N   1 
ATOM   13834 C CA  . LYS I 3 109 ? 73.390  85.059  34.893  1.000 60.565  ? 109 LYS GGG CA  1 
ATOM   13835 C C   . LYS I 3 109 ? 72.967  85.821  36.159  1.000 53.190  ? 109 LYS GGG C   1 
ATOM   13836 O O   . LYS I 3 109 ? 73.819  86.518  36.739  1.000 53.406  ? 109 LYS GGG O   1 
ATOM   13837 C CB  . LYS I 3 109 ? 74.415  83.935  35.135  1.000 74.662  ? 109 LYS GGG CB  1 
ATOM   13838 C CG  . LYS I 3 109 ? 74.146  82.962  36.283  1.000 83.283  ? 109 LYS GGG CG  1 
ATOM   13839 C CD  . LYS I 3 109 ? 72.962  82.040  36.078  1.000 89.122  ? 109 LYS GGG CD  1 
ATOM   13840 C CE  . LYS I 3 109 ? 72.362  81.589  37.394  1.000 96.355  ? 109 LYS GGG CE  1 
ATOM   13841 N NZ  . LYS I 3 109 ? 70.922  81.279  37.264  1.000 101.538 ? 109 LYS GGG NZ  1 
ATOM   13842 N N   . VAL I 3 110 ? 71.700  85.717  36.561  1.000 47.485  ? 110 VAL GGG N   1 
ATOM   13843 C CA  . VAL I 3 110 ? 71.181  86.318  37.824  1.000 49.125  ? 110 VAL GGG CA  1 
ATOM   13844 C C   . VAL I 3 110 ? 70.722  85.199  38.771  1.000 52.313  ? 110 VAL GGG C   1 
ATOM   13845 O O   . VAL I 3 110 ? 69.788  84.465  38.385  1.000 54.508  ? 110 VAL GGG O   1 
ATOM   13846 C CB  . VAL I 3 110 ? 70.048  87.316  37.526  1.000 49.340  ? 110 VAL GGG CB  1 
ATOM   13847 C CG1 . VAL I 3 110 ? 69.345  87.799  38.788  1.000 49.314  ? 110 VAL GGG CG1 1 
ATOM   13848 C CG2 . VAL I 3 110 ? 70.564  88.501  36.724  1.000 52.637  ? 110 VAL GGG CG2 1 
ATOM   13849 N N   . GLU I 3 111 ? 71.339  85.095  39.960  1.000 53.289  ? 111 GLU GGG N   1 
ATOM   13850 C CA  . GLU I 3 111 ? 70.944  84.151  41.041  1.000 57.295  ? 111 GLU GGG CA  1 
ATOM   13851 C C   . GLU I 3 111 ? 70.264  84.938  42.165  1.000 54.500  ? 111 GLU GGG C   1 
ATOM   13852 O O   . GLU I 3 111 ? 70.501  86.135  42.260  1.000 49.982  ? 111 GLU GGG O   1 
ATOM   13853 C CB  . GLU I 3 111 ? 72.121  83.413  41.697  1.000 66.626  ? 111 GLU GGG CB  1 
ATOM   13854 C CG  . GLU I 3 111 ? 73.401  83.319  40.885  1.000 80.138  ? 111 GLU GGG CG  1 
ATOM   13855 C CD  . GLU I 3 111 ? 74.497  82.422  41.478  1.000 86.272  ? 111 GLU GGG CD  1 
ATOM   13856 O OE1 . GLU I 3 111 ? 74.429  82.110  42.696  1.000 69.813  ? 111 GLU GGG OE1 1 
ATOM   13857 O OE2 . GLU I 3 111 ? 75.420  82.012  40.709  1.000 91.224  ? 111 GLU GGG OE2 1 
ATOM   13858 N N   . ILE I 3 112 ? 69.486  84.261  43.008  1.000 54.071  ? 112 ILE GGG N   1 
ATOM   13859 C CA  . ILE I 3 112 ? 69.102  84.728  44.372  1.000 53.600  ? 112 ILE GGG CA  1 
ATOM   13860 C C   . ILE I 3 112 ? 70.292  84.520  45.311  1.000 54.903  ? 112 ILE GGG C   1 
ATOM   13861 O O   . ILE I 3 112 ? 70.803  83.400  45.369  1.000 59.719  ? 112 ILE GGG O   1 
ATOM   13862 C CB  . ILE I 3 112 ? 67.883  83.952  44.898  1.000 57.430  ? 112 ILE GGG CB  1 
ATOM   13863 C CG1 . ILE I 3 112 ? 66.665  84.141  43.993  1.000 62.125  ? 112 ILE GGG CG1 1 
ATOM   13864 C CG2 . ILE I 3 112 ? 67.573  84.337  46.340  1.000 57.101  ? 112 ILE GGG CG2 1 
ATOM   13865 C CD1 . ILE I 3 112 ? 66.272  85.588  43.783  1.000 62.457  ? 112 ILE GGG CD1 1 
ATOM   13866 N N   . LYS I 3 113 ? 70.697  85.550  46.048  1.000 56.803  ? 113 LYS GGG N   1 
ATOM   13867 C CA  . LYS I 3 113 ? 71.651  85.411  47.178  1.000 56.418  ? 113 LYS GGG CA  1 
ATOM   13868 C C   . LYS I 3 113 ? 70.858  85.187  48.462  1.000 46.850  ? 113 LYS GGG C   1 
ATOM   13869 O O   . LYS I 3 113 ? 69.961  85.975  48.741  1.000 46.553  ? 113 LYS GGG O   1 
ATOM   13870 C CB  . LYS I 3 113 ? 72.543  86.642  47.348  1.000 68.634  ? 113 LYS GGG CB  1 
ATOM   13871 C CG  . LYS I 3 113 ? 73.650  86.440  48.381  1.000 79.302  ? 113 LYS GGG CG  1 
ATOM   13872 C CD  . LYS I 3 113 ? 74.646  87.581  48.468  1.000 82.595  ? 113 LYS GGG CD  1 
ATOM   13873 C CE  . LYS I 3 113 ? 74.279  88.567  49.558  1.000 88.567  ? 113 LYS GGG CE  1 
ATOM   13874 N NZ  . LYS I 3 113 ? 75.080  89.807  49.475  1.000 93.830  ? 113 LYS GGG NZ  1 
ATOM   13875 N N   . ARG I 3 114 ? 71.209  84.149  49.207  1.000 43.022  ? 114 ARG GGG N   1 
ATOM   13876 C CA  . ARG I 3 114 ? 70.634  83.842  50.542  1.000 44.971  ? 114 ARG GGG CA  1 
ATOM   13877 C C   . ARG I 3 114 ? 71.793  83.555  51.496  1.000 47.031  ? 114 ARG GGG C   1 
ATOM   13878 O O   . ARG I 3 114 ? 72.965  83.637  51.038  1.000 45.139  ? 114 ARG GGG O   1 
ATOM   13879 C CB  . ARG I 3 114 ? 69.706  82.631  50.463  1.000 46.945  ? 114 ARG GGG CB  1 
ATOM   13880 C CG  . ARG I 3 114 ? 70.324  81.449  49.721  1.000 48.788  ? 114 ARG GGG CG  1 
ATOM   13881 C CD  . ARG I 3 114 ? 69.807  80.103  50.180  1.000 46.931  ? 114 ARG GGG CD  1 
ATOM   13882 N NE  . ARG I 3 114 ? 70.174  79.903  51.568  1.000 46.487  ? 114 ARG GGG NE  1 
ATOM   13883 C CZ  . ARG I 3 114 ? 69.586  79.059  52.405  1.000 45.919  ? 114 ARG GGG CZ  1 
ATOM   13884 N NH1 . ARG I 3 114 ? 68.582  78.292  52.021  1.000 46.208  ? 114 ARG GGG NH1 1 
ATOM   13885 N NH2 . ARG I 3 114 ? 70.014  78.986  53.647  1.000 49.039  ? 114 ARG GGG NH2 1 
ATOM   13886 N N   . THR I 3 115 ? 71.490  83.229  52.760  1.000 49.293  ? 115 THR GGG N   1 
ATOM   13887 C CA  . THR I 3 115 ? 72.510  82.851  53.775  1.000 50.638  ? 115 THR GGG CA  1 
ATOM   13888 C C   . THR I 3 115 ? 73.218  81.582  53.303  1.000 48.162  ? 115 THR GGG C   1 
ATOM   13889 O O   . THR I 3 115 ? 72.566  80.741  52.641  1.000 44.767  ? 115 THR GGG O   1 
ATOM   13890 C CB  . THR I 3 115 ? 71.929  82.616  55.177  1.000 51.319  ? 115 THR GGG CB  1 
ATOM   13891 O OG1 . THR I 3 115 ? 70.712  81.898  55.007  1.000 51.397  ? 115 THR GGG OG1 1 
ATOM   13892 C CG2 . THR I 3 115 ? 71.673  83.884  55.960  1.000 53.515  ? 115 THR GGG CG2 1 
ATOM   13893 N N   . VAL I 3 116 ? 74.503  81.464  53.640  1.000 46.530  ? 116 VAL GGG N   1 
ATOM   13894 C CA  . VAL I 3 116 ? 75.314  80.240  53.394  1.000 44.373  ? 116 VAL GGG CA  1 
ATOM   13895 C C   . VAL I 3 116 ? 74.548  79.061  53.979  1.000 41.804  ? 116 VAL GGG C   1 
ATOM   13896 O O   . VAL I 3 116 ? 73.971  79.210  55.060  1.000 43.119  ? 116 VAL GGG O   1 
ATOM   13897 C CB  . VAL I 3 116 ? 76.716  80.351  54.013  1.000 47.638  ? 116 VAL GGG CB  1 
ATOM   13898 C CG1 . VAL I 3 116 ? 77.546  79.081  53.835  1.000 48.954  ? 116 VAL GGG CG1 1 
ATOM   13899 C CG2 . VAL I 3 116 ? 77.447  81.557  53.452  1.000 51.637  ? 116 VAL GGG CG2 1 
ATOM   13900 N N   . ALA I 3 117 ? 74.522  77.951  53.251  1.000 40.064  ? 117 ALA GGG N   1 
ATOM   13901 C CA  . ALA I 3 117 ? 73.963  76.663  53.704  1.000 41.642  ? 117 ALA GGG CA  1 
ATOM   13902 C C   . ALA I 3 117 ? 74.923  75.565  53.268  1.000 43.008  ? 117 ALA GGG C   1 
ATOM   13903 O O   . ALA I 3 117 ? 75.226  75.488  52.065  1.000 41.634  ? 117 ALA GGG O   1 
ATOM   13904 C CB  . ALA I 3 117 ? 72.588  76.456  53.130  1.000 44.893  ? 117 ALA GGG CB  1 
ATOM   13905 N N   . ALA I 3 118 ? 75.423  74.789  54.227  1.000 43.567  ? 118 ALA GGG N   1 
ATOM   13906 C CA  . ALA I 3 118 ? 76.365  73.681  53.992  1.000 42.083  ? 118 ALA GGG CA  1 
ATOM   13907 C C   . ALA I 3 118 ? 75.631  72.547  53.296  1.000 41.289  ? 118 ALA GGG C   1 
ATOM   13908 O O   . ALA I 3 118 ? 74.438  72.368  53.508  1.000 43.782  ? 118 ALA GGG O   1 
ATOM   13909 C CB  . ALA I 3 118 ? 76.916  73.232  55.304  1.000 46.601  ? 118 ALA GGG CB  1 
ATOM   13910 N N   . PRO I 3 119 ? 76.315  71.770  52.436  1.000 40.616  ? 119 PRO GGG N   1 
ATOM   13911 C CA  . PRO I 3 119 ? 75.693  70.626  51.781  1.000 42.055  ? 119 PRO GGG CA  1 
ATOM   13912 C C   . PRO I 3 119 ? 75.581  69.419  52.723  1.000 42.875  ? 119 PRO GGG C   1 
ATOM   13913 O O   . PRO I 3 119 ? 76.504  69.178  53.485  1.000 40.881  ? 119 PRO GGG O   1 
ATOM   13914 C CB  . PRO I 3 119 ? 76.636  70.339  50.599  1.000 42.191  ? 119 PRO GGG CB  1 
ATOM   13915 C CG  . PRO I 3 119 ? 77.982  70.802  51.091  1.000 42.532  ? 119 PRO GGG CG  1 
ATOM   13916 C CD  . PRO I 3 119 ? 77.698  71.981  52.002  1.000 41.714  ? 119 PRO GGG CD  1 
ATOM   13917 N N   . SER I 3 120 ? 74.442  68.724  52.657  1.000 43.776  ? 120 SER GGG N   1 
ATOM   13918 C CA  . SER I 3 120 ? 74.272  67.329  53.131  1.000 47.539  ? 120 SER GGG CA  1 
ATOM   13919 C C   . SER I 3 120 ? 74.972  66.415  52.128  1.000 46.755  ? 120 SER GGG C   1 
ATOM   13920 O O   . SER I 3 120 ? 74.624  66.496  50.925  1.000 42.963  ? 120 SER GGG O   1 
ATOM   13921 C CB  . SER I 3 120 ? 72.814  66.955  53.291  1.000 53.693  ? 120 SER GGG CB  1 
ATOM   13922 O OG  . SER I 3 120 ? 72.262  67.533  54.472  1.000 62.373  ? 120 SER GGG OG  1 
ATOM   13923 N N   . VAL I 3 121 ? 75.921  65.594  52.594  1.000 45.342  ? 121 VAL GGG N   1 
ATOM   13924 C CA  . VAL I 3 121 ? 76.722  64.695  51.706  1.000 42.861  ? 121 VAL GGG CA  1 
ATOM   13925 C C   . VAL I 3 121 ? 76.242  63.242  51.826  1.000 39.634  ? 121 VAL GGG C   1 
ATOM   13926 O O   . VAL I 3 121 ? 75.983  62.772  52.941  1.000 40.156  ? 121 VAL GGG O   1 
ATOM   13927 C CB  . VAL I 3 121 ? 78.220  64.830  51.995  1.000 41.671  ? 121 VAL GGG CB  1 
ATOM   13928 C CG1 . VAL I 3 121 ? 79.045  64.121  50.938  1.000 42.315  ? 121 VAL GGG CG1 1 
ATOM   13929 C CG2 . VAL I 3 121 ? 78.622  66.291  52.126  1.000 41.171  ? 121 VAL GGG CG2 1 
ATOM   13930 N N   . PHE I 3 122 ? 76.096  62.576  50.686  1.000 37.938  ? 122 PHE GGG N   1 
ATOM   13931 C CA  . PHE I 3 122 ? 75.674  61.161  50.573  1.000 39.587  ? 122 PHE GGG CA  1 
ATOM   13932 C C   . PHE I 3 122 ? 76.524  60.507  49.497  1.000 39.292  ? 122 PHE GGG C   1 
ATOM   13933 O O   . PHE I 3 122 ? 76.753  61.145  48.461  1.000 37.457  ? 122 PHE GGG O   1 
ATOM   13934 C CB  . PHE I 3 122 ? 74.199  61.033  50.184  1.000 38.002  ? 122 PHE GGG CB  1 
ATOM   13935 C CG  . PHE I 3 122 ? 73.258  61.720  51.127  1.000 37.993  ? 122 PHE GGG CG  1 
ATOM   13936 C CD1 . PHE I 3 122 ? 72.870  63.028  50.898  1.000 39.558  ? 122 PHE GGG CD1 1 
ATOM   13937 C CD2 . PHE I 3 122 ? 72.778  61.066  52.247  1.000 38.144  ? 122 PHE GGG CD2 1 
ATOM   13938 C CE1 . PHE I 3 122 ? 72.006  63.668  51.772  1.000 40.854  ? 122 PHE GGG CE1 1 
ATOM   13939 C CE2 . PHE I 3 122 ? 71.908  61.706  53.114  1.000 40.137  ? 122 PHE GGG CE2 1 
ATOM   13940 C CZ  . PHE I 3 122 ? 71.528  63.009  52.881  1.000 40.226  ? 122 PHE GGG CZ  1 
ATOM   13941 N N   . ILE I 3 123 ? 76.927  59.262  49.725  1.000 39.585  ? 123 ILE GGG N   1 
ATOM   13942 C CA  . ILE I 3 123 ? 77.790  58.516  48.770  1.000 39.773  ? 123 ILE GGG CA  1 
ATOM   13943 C C   . ILE I 3 123 ? 77.105  57.189  48.470  1.000 34.721  ? 123 ILE GGG C   1 
ATOM   13944 O O   . ILE I 3 123 ? 76.664  56.551  49.394  1.000 36.350  ? 123 ILE GGG O   1 
ATOM   13945 C CB  . ILE I 3 123 ? 79.215  58.337  49.329  1.000 43.049  ? 123 ILE GGG CB  1 
ATOM   13946 C CG1 . ILE I 3 123 ? 80.148  57.709  48.295  1.000 46.169  ? 123 ILE GGG CG1 1 
ATOM   13947 C CG2 . ILE I 3 123 ? 79.201  57.534  50.610  1.000 42.598  ? 123 ILE GGG CG2 1 
ATOM   13948 C CD1 . ILE I 3 123 ? 81.592  57.611  48.742  1.000 47.307  ? 123 ILE GGG CD1 1 
ATOM   13949 N N   . PHE I 3 124 ? 77.023  56.820  47.205  1.000 32.533  ? 124 PHE GGG N   1 
ATOM   13950 C CA  . PHE I 3 124 ? 76.359  55.586  46.754  1.000 34.344  ? 124 PHE GGG CA  1 
ATOM   13951 C C   . PHE I 3 124 ? 77.404  54.703  46.107  1.000 34.677  ? 124 PHE GGG C   1 
ATOM   13952 O O   . PHE I 3 124 ? 78.070  55.106  45.152  1.000 33.640  ? 124 PHE GGG O   1 
ATOM   13953 C CB  . PHE I 3 124 ? 75.224  55.915  45.786  1.000 40.235  ? 124 PHE GGG CB  1 
ATOM   13954 C CG  . PHE I 3 124 ? 74.204  56.846  46.380  1.000 43.479  ? 124 PHE GGG CG  1 
ATOM   13955 C CD1 . PHE I 3 124 ? 73.369  56.410  47.396  1.000 44.737  ? 124 PHE GGG CD1 1 
ATOM   13956 C CD2 . PHE I 3 124 ? 74.131  58.166  45.965  1.000 45.058  ? 124 PHE GGG CD2 1 
ATOM   13957 C CE1 . PHE I 3 124 ? 72.466  57.276  47.982  1.000 48.061  ? 124 PHE GGG CE1 1 
ATOM   13958 C CE2 . PHE I 3 124 ? 73.214  59.027  46.541  1.000 46.639  ? 124 PHE GGG CE2 1 
ATOM   13959 C CZ  . PHE I 3 124 ? 72.392  58.585  47.555  1.000 49.442  ? 124 PHE GGG CZ  1 
ATOM   13960 N N   . PRO I 3 125 ? 77.567  53.462  46.603  1.000 36.259  ? 125 PRO GGG N   1 
ATOM   13961 C CA  . PRO I 3 125 ? 78.429  52.496  45.939  1.000 35.149  ? 125 PRO GGG CA  1 
ATOM   13962 C C   . PRO I 3 125 ? 77.743  52.049  44.661  1.000 34.085  ? 125 PRO GGG C   1 
ATOM   13963 O O   . PRO I 3 125 ? 76.557  52.283  44.476  1.000 29.096  ? 125 PRO GGG O   1 
ATOM   13964 C CB  . PRO I 3 125 ? 78.510  51.357  46.950  1.000 36.346  ? 125 PRO GGG CB  1 
ATOM   13965 C CG  . PRO I 3 125 ? 77.171  51.416  47.646  1.000 37.898  ? 125 PRO GGG CG  1 
ATOM   13966 C CD  . PRO I 3 125 ? 76.881  52.899  47.774  1.000 37.882  ? 125 PRO GGG CD  1 
ATOM   13967 N N   . PRO I 3 126 ? 78.469  51.404  43.737  1.000 38.086  ? 126 PRO GGG N   1 
ATOM   13968 C CA  . PRO I 3 126 ? 77.833  50.852  42.550  1.000 41.778  ? 126 PRO GGG CA  1 
ATOM   13969 C C   . PRO I 3 126 ? 76.940  49.658  42.915  1.000 40.999  ? 126 PRO GGG C   1 
ATOM   13970 O O   . PRO I 3 126 ? 77.191  48.987  43.889  1.000 35.181  ? 126 PRO GGG O   1 
ATOM   13971 C CB  . PRO I 3 126 ? 79.015  50.475  41.647  1.000 42.968  ? 126 PRO GGG CB  1 
ATOM   13972 C CG  . PRO I 3 126 ? 80.175  50.269  42.602  1.000 42.801  ? 126 PRO GGG CG  1 
ATOM   13973 C CD  . PRO I 3 126 ? 79.924  51.207  43.763  1.000 40.206  ? 126 PRO GGG CD  1 
ATOM   13974 N N   . SER I 3 127 ? 75.878  49.494  42.133  1.000 46.678  ? 127 SER GGG N   1 
ATOM   13975 C CA  . SER I 3 127 ? 74.896  48.383  42.202  1.000 55.447  ? 127 SER GGG CA  1 
ATOM   13976 C C   . SER I 3 127 ? 75.591  47.075  41.838  1.000 60.029  ? 127 SER GGG C   1 
ATOM   13977 O O   . SER I 3 127 ? 76.534  47.122  41.020  1.000 64.277  ? 127 SER GGG O   1 
ATOM   13978 C CB  . SER I 3 127 ? 73.772  48.646  41.252  1.000 58.238  ? 127 SER GGG CB  1 
ATOM   13979 O OG  . SER I 3 127 ? 74.303  49.120  40.016  1.000 66.119  ? 127 SER GGG OG  1 
ATOM   13980 N N   . ASP I 3 128 ? 75.119  45.954  42.379  1.000 61.795  ? 128 ASP GGG N   1 
ATOM   13981 C CA  . ASP I 3 128 ? 75.630  44.612  42.000  1.000 67.843  ? 128 ASP GGG CA  1 
ATOM   13982 C C   . ASP I 3 128 ? 75.344  44.401  40.511  1.000 65.380  ? 128 ASP GGG C   1 
ATOM   13983 O O   . ASP I 3 128 ? 76.212  43.821  39.807  1.000 60.056  ? 128 ASP GGG O   1 
ATOM   13984 C CB  . ASP I 3 128 ? 75.025  43.514  42.881  1.000 76.559  ? 128 ASP GGG CB  1 
ATOM   13985 C CG  . ASP I 3 128 ? 75.570  43.460  44.307  1.000 80.368  ? 128 ASP GGG CG  1 
ATOM   13986 O OD1 . ASP I 3 128 ? 76.659  44.025  44.564  1.000 84.788  ? 128 ASP GGG OD1 1 
ATOM   13987 O OD2 . ASP I 3 128 ? 74.900  42.854  45.159  1.000 79.225  ? 128 ASP GGG OD2 1 
ATOM   13988 N N   . GLU I 3 129 ? 74.185  44.895  40.061  1.000 68.189  ? 129 GLU GGG N   1 
ATOM   13989 C CA  . GLU I 3 129 ? 73.676  44.771  38.667  1.000 70.795  ? 129 GLU GGG CA  1 
ATOM   13990 C C   . GLU I 3 129 ? 74.656  45.466  37.702  1.000 62.021  ? 129 GLU GGG C   1 
ATOM   13991 O O   . GLU I 3 129 ? 74.973  44.880  36.661  1.000 61.098  ? 129 GLU GGG O   1 
ATOM   13992 C CB  . GLU I 3 129 ? 72.254  45.337  38.605  1.000 79.223  ? 129 GLU GGG CB  1 
ATOM   13993 C CG  . GLU I 3 129 ? 71.444  44.883  37.397  1.000 87.642  ? 129 GLU GGG CG  1 
ATOM   13994 C CD  . GLU I 3 129 ? 70.351  45.855  36.954  1.000 95.949  ? 129 GLU GGG CD  1 
ATOM   13995 O OE1 . GLU I 3 129 ? 69.805  46.584  37.816  1.000 84.356  ? 129 GLU GGG OE1 1 
ATOM   13996 O OE2 . GLU I 3 129 ? 70.036  45.893  35.737  1.000 99.839  ? 129 GLU GGG OE2 1 
ATOM   13997 N N   . GLN I 3 130 ? 75.155  46.658  38.035  1.000 54.209  ? 130 GLN GGG N   1 
ATOM   13998 C CA  . GLN I 3 130 ? 76.092  47.402  37.153  1.000 51.926  ? 130 GLN GGG CA  1 
ATOM   13999 C C   . GLN I 3 130 ? 77.413  46.633  37.053  1.000 53.059  ? 130 GLN GGG C   1 
ATOM   14000 O O   . GLN I 3 130 ? 78.037  46.651  35.979  1.000 53.216  ? 130 GLN GGG O   1 
ATOM   14001 C CB  . GLN I 3 130 ? 76.350  48.831  37.645  1.000 48.455  ? 130 GLN GGG CB  1 
ATOM   14002 C CG  . GLN I 3 130 ? 77.204  49.648  36.672  1.000 46.172  ? 130 GLN GGG CG  1 
ATOM   14003 C CD  . GLN I 3 130 ? 77.513  51.027  37.178  1.000 43.300  ? 130 GLN GGG CD  1 
ATOM   14004 O OE1 . GLN I 3 130 ? 77.344  51.317  38.359  1.000 44.249  ? 130 GLN GGG OE1 1 
ATOM   14005 N NE2 . GLN I 3 130 ? 77.965  51.878  36.274  1.000 39.168  ? 130 GLN GGG NE2 1 
ATOM   14006 N N   . LEU I 3 131 ? 77.847  46.017  38.148  1.000 52.947  ? 131 LEU GGG N   1 
ATOM   14007 C CA  . LEU I 3 131 ? 79.169  45.345  38.219  1.000 51.484  ? 131 LEU GGG CA  1 
ATOM   14008 C C   . LEU I 3 131 ? 79.177  44.150  37.265  1.000 49.747  ? 131 LEU GGG C   1 
ATOM   14009 O O   . LEU I 3 131 ? 80.240  43.894  36.667  1.000 47.450  ? 131 LEU GGG O   1 
ATOM   14010 C CB  . LEU I 3 131 ? 79.456  44.939  39.667  1.000 52.419  ? 131 LEU GGG CB  1 
ATOM   14011 C CG  . LEU I 3 131 ? 79.889  46.095  40.576  1.000 51.552  ? 131 LEU GGG CG  1 
ATOM   14012 C CD1 . LEU I 3 131 ? 79.839  45.715  42.045  1.000 53.949  ? 131 LEU GGG CD1 1 
ATOM   14013 C CD2 . LEU I 3 131 ? 81.283  46.577  40.227  1.000 48.497  ? 131 LEU GGG CD2 1 
ATOM   14014 N N   . LYS I 3 132 ? 78.037  43.479  37.103  1.000 51.065  ? 132 LYS GGG N   1 
ATOM   14015 C CA  . LYS I 3 132 ? 77.874  42.401  36.094  1.000 60.083  ? 132 LYS GGG CA  1 
ATOM   14016 C C   . LYS I 3 132 ? 78.183  42.936  34.690  1.000 63.837  ? 132 LYS GGG C   1 
ATOM   14017 O O   . LYS I 3 132 ? 78.808  42.204  33.915  1.000 65.280  ? 132 LYS GGG O   1 
ATOM   14018 C CB  . LYS I 3 132 ? 76.469  41.800  36.152  1.000 67.265  ? 132 LYS GGG CB  1 
ATOM   14019 C CG  . LYS I 3 132 ? 76.264  40.834  37.312  1.000 79.148  ? 132 LYS GGG CG  1 
ATOM   14020 C CD  . LYS I 3 132 ? 74.993  40.012  37.232  1.000 84.814  ? 132 LYS GGG CD  1 
ATOM   14021 C CE  . LYS I 3 132 ? 73.791  40.757  37.774  1.000 91.855  ? 132 LYS GGG CE  1 
ATOM   14022 N NZ  . LYS I 3 132 ? 72.532  40.050  37.444  1.000 93.650  ? 132 LYS GGG NZ  1 
ATOM   14023 N N   . SER I 3 133 ? 77.766  44.158  34.368  1.000 66.962  ? 133 SER GGG N   1 
ATOM   14024 C CA  . SER I 3 133 ? 77.972  44.776  33.032  1.000 73.883  ? 133 SER GGG CA  1 
ATOM   14025 C C   . SER I 3 133 ? 79.455  45.118  32.817  1.000 70.107  ? 133 SER GGG C   1 
ATOM   14026 O O   . SER I 3 133 ? 79.835  45.301  31.640  1.000 78.343  ? 133 SER GGG O   1 
ATOM   14027 C CB  . SER I 3 133 ? 77.077  45.982  32.834  1.000 83.905  ? 133 SER GGG CB  1 
ATOM   14028 O OG  . SER I 3 133 ? 77.523  47.088  33.604  1.000 97.341  ? 133 SER GGG OG  1 
ATOM   14029 N N   . GLY I 3 134 ? 80.253  45.245  33.889  1.000 62.314  ? 134 GLY GGG N   1 
ATOM   14030 C CA  . GLY I 3 134 ? 81.719  45.413  33.800  1.000 60.380  ? 134 GLY GGG CA  1 
ATOM   14031 C C   . GLY I 3 134 ? 82.200  46.859  33.895  1.000 63.238  ? 134 GLY GGG C   1 
ATOM   14032 O O   . GLY I 3 134 ? 83.412  47.091  33.636  1.000 63.696  ? 134 GLY GGG O   1 
ATOM   14033 N N   . THR I 3 135 ? 81.327  47.812  34.259  1.000 64.870  ? 135 THR GGG N   1 
ATOM   14034 C CA  . THR I 3 135 ? 81.749  49.148  34.783  1.000 61.767  ? 135 THR GGG CA  1 
ATOM   14035 C C   . THR I 3 135 ? 81.199  49.328  36.200  1.000 50.250  ? 135 THR GGG C   1 
ATOM   14036 O O   . THR I 3 135 ? 80.376  48.489  36.662  1.000 43.021  ? 135 THR GGG O   1 
ATOM   14037 C CB  . THR I 3 135 ? 81.367  50.321  33.871  1.000 66.304  ? 135 THR GGG CB  1 
ATOM   14038 O OG1 . THR I 3 135 ? 79.939  50.320  33.756  1.000 80.594  ? 135 THR GGG OG1 1 
ATOM   14039 C CG2 . THR I 3 135 ? 82.053  50.255  32.523  1.000 66.888  ? 135 THR GGG CG2 1 
ATOM   14040 N N   . ALA I 3 136 ? 81.689  50.365  36.871  1.000 44.723  ? 136 ALA GGG N   1 
ATOM   14041 C CA  . ALA I 3 136 ? 81.313  50.716  38.254  1.000 47.292  ? 136 ALA GGG CA  1 
ATOM   14042 C C   . ALA I 3 136 ? 81.215  52.236  38.362  1.000 46.699  ? 136 ALA GGG C   1 
ATOM   14043 O O   . ALA I 3 136 ? 82.190  52.937  38.014  1.000 44.858  ? 136 ALA GGG O   1 
ATOM   14044 C CB  . ALA I 3 136 ? 82.322  50.163  39.227  1.000 47.210  ? 136 ALA GGG CB  1 
ATOM   14045 N N   . SER I 3 137 ? 80.063  52.722  38.807  1.000 43.430  ? 137 SER GGG N   1 
ATOM   14046 C CA  . SER I 3 137 ? 79.807  54.165  38.986  1.000 41.869  ? 137 SER GGG CA  1 
ATOM   14047 C C   . SER I 3 137 ? 79.592  54.420  40.478  1.000 39.619  ? 137 SER GGG C   1 
ATOM   14048 O O   . SER I 3 137 ? 78.698  53.805  41.084  1.000 44.731  ? 137 SER GGG O   1 
ATOM   14049 C CB  . SER I 3 137 ? 78.658  54.613  38.124  1.000 41.253  ? 137 SER GGG CB  1 
ATOM   14050 O OG  . SER I 3 137 ? 79.020  54.610  36.746  1.000 38.163  ? 137 SER GGG OG  1 
ATOM   14051 N N   . VAL I 3 138 ? 80.442  55.258  41.055  1.000 36.000  ? 138 VAL GGG N   1 
ATOM   14052 C CA  . VAL I 3 138 ? 80.340  55.711  42.465  1.000 34.273  ? 138 VAL GGG CA  1 
ATOM   14053 C C   . VAL I 3 138 ? 79.836  57.145  42.423  1.000 31.941  ? 138 VAL GGG C   1 
ATOM   14054 O O   . VAL I 3 138 ? 80.496  57.990  41.803  1.000 32.531  ? 138 VAL GGG O   1 
ATOM   14055 C CB  . VAL I 3 138 ? 81.690  55.609  43.192  1.000 34.825  ? 138 VAL GGG CB  1 
ATOM   14056 C CG1 . VAL I 3 138 ? 81.525  55.817  44.687  1.000 35.438  ? 138 VAL GGG CG1 1 
ATOM   14057 C CG2 . VAL I 3 138 ? 82.378  54.286  42.892  1.000 35.107  ? 138 VAL GGG CG2 1 
ATOM   14058 N N   . VAL I 3 139 ? 78.695  57.393  43.049  1.000 31.035  ? 139 VAL GGG N   1 
ATOM   14059 C CA  . VAL I 3 139 ? 78.026  58.715  42.993  1.000 31.948  ? 139 VAL GGG CA  1 
ATOM   14060 C C   . VAL I 3 139 ? 78.164  59.362  44.364  1.000 32.804  ? 139 VAL GGG C   1 
ATOM   14061 O O   . VAL I 3 139 ? 77.994  58.677  45.379  1.000 34.347  ? 139 VAL GGG O   1 
ATOM   14062 C CB  . VAL I 3 139 ? 76.563  58.592  42.554  1.000 33.079  ? 139 VAL GGG CB  1 
ATOM   14063 C CG1 . VAL I 3 139 ? 75.872  59.946  42.517  1.000 35.728  ? 139 VAL GGG CG1 1 
ATOM   14064 C CG2 . VAL I 3 139 ? 76.478  57.915  41.200  1.000 34.408  ? 139 VAL GGG CG2 1 
ATOM   14065 N N   . CYS I 3 140 ? 78.492  60.644  44.357  1.000 35.951  ? 140 CYS GGG N   1 
ATOM   14066 C CA  . CYS I 3 140 ? 78.489  61.507  45.546  1.000 38.372  ? 140 CYS GGG CA  1 
ATOM   14067 C C   . CYS I 3 140 ? 77.458  62.611  45.332  1.000 40.210  ? 140 CYS GGG C   1 
ATOM   14068 O O   . CYS I 3 140 ? 77.517  63.263  44.268  1.000 37.107  ? 140 CYS GGG O   1 
ATOM   14069 C CB  . CYS I 3 140 ? 79.856  62.107  45.774  1.000 42.479  ? 140 CYS GGG CB  1 
ATOM   14070 S SG  . CYS I 3 140 ? 80.028  62.699  47.463  1.000 55.850  ? 140 CYS GGG SG  1 
ATOM   14071 N N   . LEU I 3 141 ? 76.533  62.761  46.289  1.000 39.091  ? 141 LEU GGG N   1 
ATOM   14072 C CA  . LEU I 3 141 ? 75.473  63.794  46.282  1.000 36.735  ? 141 LEU GGG CA  1 
ATOM   14073 C C   . LEU I 3 141 ? 75.821  64.871  47.309  1.000 38.097  ? 141 LEU GGG C   1 
ATOM   14074 O O   . LEU I 3 141 ? 76.005  64.529  48.480  1.000 41.773  ? 141 LEU GGG O   1 
ATOM   14075 C CB  . LEU I 3 141 ? 74.127  63.151  46.603  1.000 36.487  ? 141 LEU GGG CB  1 
ATOM   14076 C CG  . LEU I 3 141 ? 72.947  64.124  46.636  1.000 38.290  ? 141 LEU GGG CG  1 
ATOM   14077 C CD1 . LEU I 3 141 ? 72.812  64.843  45.307  1.000 37.764  ? 141 LEU GGG CD1 1 
ATOM   14078 C CD2 . LEU I 3 141 ? 71.649  63.421  46.987  1.000 38.773  ? 141 LEU GGG CD2 1 
ATOM   14079 N N   . LEU I 3 142 ? 75.933  66.119  46.855  1.000 39.207  ? 142 LEU GGG N   1 
ATOM   14080 C CA  . LEU I 3 142 ? 75.910  67.331  47.710  1.000 40.301  ? 142 LEU GGG CA  1 
ATOM   14081 C C   . LEU I 3 142 ? 74.499  67.923  47.606  1.000 44.160  ? 142 LEU GGG C   1 
ATOM   14082 O O   . LEU I 3 142 ? 74.133  68.361  46.494  1.000 46.839  ? 142 LEU GGG O   1 
ATOM   14083 C CB  . LEU I 3 142 ? 76.957  68.336  47.216  1.000 40.410  ? 142 LEU GGG CB  1 
ATOM   14084 C CG  . LEU I 3 142 ? 78.414  68.033  47.565  1.000 38.308  ? 142 LEU GGG CG  1 
ATOM   14085 C CD1 . LEU I 3 142 ? 78.882  66.715  46.978  1.000 39.432  ? 142 LEU GGG CD1 1 
ATOM   14086 C CD2 . LEU I 3 142 ? 79.324  69.151  47.093  1.000 35.830  ? 142 LEU GGG CD2 1 
ATOM   14087 N N   . ASN I 3 143 ? 73.732  67.928  48.704  1.000 42.075  ? 143 ASN GGG N   1 
ATOM   14088 C CA  . ASN I 3 143 ? 72.284  68.253  48.688  1.000 40.332  ? 143 ASN GGG CA  1 
ATOM   14089 C C   . ASN I 3 143 ? 72.044  69.624  49.338  1.000 39.650  ? 143 ASN GGG C   1 
ATOM   14090 O O   . ASN I 3 143 ? 72.532  69.843  50.451  1.000 36.064  ? 143 ASN GGG O   1 
ATOM   14091 C CB  . ASN I 3 143 ? 71.491  67.136  49.366  1.000 42.021  ? 143 ASN GGG CB  1 
ATOM   14092 C CG  . ASN I 3 143 ? 70.062  67.057  48.890  1.000 42.204  ? 143 ASN GGG CG  1 
ATOM   14093 O OD1 . ASN I 3 143 ? 69.808  67.194  47.687  1.000 37.148  ? 143 ASN GGG OD1 1 
ATOM   14094 N ND2 . ASN I 3 143 ? 69.144  66.875  49.840  1.000 40.300  ? 143 ASN GGG ND2 1 
ATOM   14095 N N   . ASN I 3 144 ? 71.310  70.506  48.642  1.000 42.969  ? 144 ASN GGG N   1 
ATOM   14096 C CA  . ASN I 3 144 ? 70.733  71.790  49.138  1.000 41.811  ? 144 ASN GGG CA  1 
ATOM   14097 C C   . ASN I 3 144 ? 71.793  72.627  49.865  1.000 42.746  ? 144 ASN GGG C   1 
ATOM   14098 O O   . ASN I 3 144 ? 71.735  72.701  51.116  1.000 41.770  ? 144 ASN GGG O   1 
ATOM   14099 C CB  . ASN I 3 144 ? 69.532  71.580  50.064  1.000 41.825  ? 144 ASN GGG CB  1 
ATOM   14100 C CG  . ASN I 3 144 ? 68.538  70.585  49.507  1.000 41.106  ? 144 ASN GGG CG  1 
ATOM   14101 O OD1 . ASN I 3 144 ? 68.159  70.631  48.344  1.000 41.478  ? 144 ASN GGG OD1 1 
ATOM   14102 N ND2 . ASN I 3 144 ? 68.153  69.632  50.323  1.000 41.543  ? 144 ASN GGG ND2 1 
ATOM   14103 N N   . PHE I 3 145 ? 72.681  73.272  49.101  1.000 44.770  ? 145 PHE GGG N   1 
ATOM   14104 C CA  . PHE I 3 145 ? 73.749  74.169  49.610  1.000 42.630  ? 145 PHE GGG CA  1 
ATOM   14105 C C   . PHE I 3 145 ? 73.749  75.470  48.815  1.000 42.357  ? 145 PHE GGG C   1 
ATOM   14106 O O   . PHE I 3 145 ? 73.232  75.483  47.682  1.000 42.281  ? 145 PHE GGG O   1 
ATOM   14107 C CB  . PHE I 3 145 ? 75.114  73.492  49.520  1.000 42.702  ? 145 PHE GGG CB  1 
ATOM   14108 C CG  . PHE I 3 145 ? 75.557  73.140  48.123  1.000 39.882  ? 145 PHE GGG CG  1 
ATOM   14109 C CD1 . PHE I 3 145 ? 76.351  74.010  47.399  1.000 38.992  ? 145 PHE GGG CD1 1 
ATOM   14110 C CD2 . PHE I 3 145 ? 75.197  71.935  47.542  1.000 39.750  ? 145 PHE GGG CD2 1 
ATOM   14111 C CE1 . PHE I 3 145 ? 76.793  73.680  46.130  1.000 38.487  ? 145 PHE GGG CE1 1 
ATOM   14112 C CE2 . PHE I 3 145 ? 75.636  71.598  46.270  1.000 39.977  ? 145 PHE GGG CE2 1 
ATOM   14113 C CZ  . PHE I 3 145 ? 76.441  72.468  45.570  1.000 39.509  ? 145 PHE GGG CZ  1 
ATOM   14114 N N   . TYR I 3 146 ? 74.270  76.530  49.435  1.000 42.027  ? 146 TYR GGG N   1 
ATOM   14115 C CA  . TYR I 3 146 ? 74.490  77.868  48.832  1.000 44.262  ? 146 TYR GGG CA  1 
ATOM   14116 C C   . TYR I 3 146 ? 75.738  78.448  49.475  1.000 48.468  ? 146 TYR GGG C   1 
ATOM   14117 O O   . TYR I 3 146 ? 75.898  78.285  50.682  1.000 51.404  ? 146 TYR GGG O   1 
ATOM   14118 C CB  . TYR I 3 146 ? 73.303  78.819  49.030  1.000 44.176  ? 146 TYR GGG CB  1 
ATOM   14119 C CG  . TYR I 3 146 ? 73.488  80.083  48.232  1.000 44.228  ? 146 TYR GGG CG  1 
ATOM   14120 C CD1 . TYR I 3 146 ? 73.216  80.106  46.873  1.000 43.937  ? 146 TYR GGG CD1 1 
ATOM   14121 C CD2 . TYR I 3 146 ? 74.078  81.207  48.788  1.000 43.759  ? 146 TYR GGG CD2 1 
ATOM   14122 C CE1 . TYR I 3 146 ? 73.455  81.234  46.109  1.000 44.211  ? 146 TYR GGG CE1 1 
ATOM   14123 C CE2 . TYR I 3 146 ? 74.325  82.344  48.036  1.000 43.051  ? 146 TYR GGG CE2 1 
ATOM   14124 C CZ  . TYR I 3 146 ? 74.010  82.360  46.688  1.000 45.001  ? 146 TYR GGG CZ  1 
ATOM   14125 O OH  . TYR I 3 146 ? 74.238  83.464  45.909  1.000 48.274  ? 146 TYR GGG OH  1 
ATOM   14126 N N   . PRO I 3 147 ? 76.660  79.103  48.722  1.000 55.565  ? 147 PRO GGG N   1 
ATOM   14127 C CA  . PRO I 3 147 ? 76.582  79.267  47.263  1.000 56.776  ? 147 PRO GGG CA  1 
ATOM   14128 C C   . PRO I 3 147 ? 77.050  78.043  46.456  1.000 54.905  ? 147 PRO GGG C   1 
ATOM   14129 O O   . PRO I 3 147 ? 77.349  77.017  47.044  1.000 49.897  ? 147 PRO GGG O   1 
ATOM   14130 C CB  . PRO I 3 147 ? 77.567  80.410  46.995  1.000 57.886  ? 147 PRO GGG CB  1 
ATOM   14131 C CG  . PRO I 3 147 ? 78.642  80.154  48.028  1.000 60.768  ? 147 PRO GGG CG  1 
ATOM   14132 C CD  . PRO I 3 147 ? 77.869  79.736  49.265  1.000 59.350  ? 147 PRO GGG CD  1 
ATOM   14133 N N   . ARG I 3 148 ? 77.106  78.189  45.127  1.000 55.836  ? 148 ARG GGG N   1 
ATOM   14134 C CA  . ARG I 3 148 ? 77.274  77.066  44.166  1.000 56.153  ? 148 ARG GGG CA  1 
ATOM   14135 C C   . ARG I 3 148 ? 78.695  76.504  44.209  1.000 52.081  ? 148 ARG GGG C   1 
ATOM   14136 O O   . ARG I 3 148 ? 78.863  75.350  43.790  1.000 48.319  ? 148 ARG GGG O   1 
ATOM   14137 C CB  . ARG I 3 148 ? 76.949  77.551  42.754  1.000 61.285  ? 148 ARG GGG CB  1 
ATOM   14138 C CG  . ARG I 3 148 ? 76.898  76.436  41.733  1.000 67.960  ? 148 ARG GGG CG  1 
ATOM   14139 C CD  . ARG I 3 148 ? 76.673  76.946  40.327  1.000 72.441  ? 148 ARG GGG CD  1 
ATOM   14140 N NE  . ARG I 3 148 ? 77.202  76.148  39.208  1.000 81.885  ? 148 ARG GGG NE  1 
ATOM   14141 C CZ  . ARG I 3 148 ? 78.198  75.222  39.218  1.000 87.633  ? 148 ARG GGG CZ  1 
ATOM   14142 N NH1 . ARG I 3 148 ? 78.881  74.885  40.308  1.000 80.878  ? 148 ARG GGG NH1 1 
ATOM   14143 N NH2 . ARG I 3 148 ? 78.523  74.631  38.080  1.000 88.116  ? 148 ARG GGG NH2 1 
ATOM   14144 N N   . GLU I 3 149 ? 79.686  77.300  44.608  1.000 54.451  ? 149 GLU GGG N   1 
ATOM   14145 C CA  . GLU I 3 149 ? 81.120  76.880  44.604  1.000 58.580  ? 149 GLU GGG CA  1 
ATOM   14146 C C   . GLU I 3 149 ? 81.318  75.816  45.687  1.000 51.890  ? 149 GLU GGG C   1 
ATOM   14147 O O   . GLU I 3 149 ? 81.015  76.107  46.852  1.000 47.786  ? 149 GLU GGG O   1 
ATOM   14148 C CB  . GLU I 3 149 ? 82.103  78.039  44.823  1.000 67.770  ? 149 GLU GGG CB  1 
ATOM   14149 C CG  . GLU I 3 149 ? 82.042  79.125  43.757  1.000 78.016  ? 149 GLU GGG CG  1 
ATOM   14150 C CD  . GLU I 3 149 ? 80.917  80.145  43.930  1.000 86.004  ? 149 GLU GGG CD  1 
ATOM   14151 O OE1 . GLU I 3 149 ? 80.924  80.888  44.941  1.000 92.728  ? 149 GLU GGG OE1 1 
ATOM   14152 O OE2 . GLU I 3 149 ? 80.022  80.185  43.070  1.000 76.219  ? 149 GLU GGG OE2 1 
ATOM   14153 N N   . ALA I 3 150 ? 81.806  74.635  45.303  1.000 52.666  ? 150 ALA GGG N   1 
ATOM   14154 C CA  . ALA I 3 150 ? 82.095  73.506  46.219  1.000 56.074  ? 150 ALA GGG CA  1 
ATOM   14155 C C   . ALA I 3 150 ? 83.084  72.536  45.563  1.000 55.868  ? 150 ALA GGG C   1 
ATOM   14156 O O   . ALA I 3 150 ? 82.881  72.138  44.390  1.000 52.021  ? 150 ALA GGG O   1 
ATOM   14157 C CB  . ALA I 3 150 ? 80.818  72.803  46.609  1.000 58.536  ? 150 ALA GGG CB  1 
ATOM   14158 N N   . LYS I 3 151 ? 84.138  72.207  46.299  1.000 55.908  ? 151 LYS GGG N   1 
ATOM   14159 C CA  . LYS I 3 151 ? 85.195  71.289  45.839  1.000 60.401  ? 151 LYS GGG CA  1 
ATOM   14160 C C   . LYS I 3 151 ? 84.789  69.871  46.258  1.000 52.347  ? 151 LYS GGG C   1 
ATOM   14161 O O   . LYS I 3 151 ? 84.464  69.645  47.425  1.000 53.063  ? 151 LYS GGG O   1 
ATOM   14162 C CB  . LYS I 3 151 ? 86.548  71.770  46.386  1.000 71.215  ? 151 LYS GGG CB  1 
ATOM   14163 C CG  . LYS I 3 151 ? 87.723  70.802  46.247  1.000 82.813  ? 151 LYS GGG CG  1 
ATOM   14164 C CD  . LYS I 3 151 ? 88.790  71.163  45.222  1.000 84.049  ? 151 LYS GGG CD  1 
ATOM   14165 C CE  . LYS I 3 151 ? 89.336  69.918  44.556  1.000 86.530  ? 151 LYS GGG CE  1 
ATOM   14166 N NZ  . LYS I 3 151 ? 90.681  70.168  44.005  1.000 97.566  ? 151 LYS GGG NZ  1 
ATOM   14167 N N   . VAL I 3 152 ? 84.780  68.953  45.308  1.000 43.824  ? 152 VAL GGG N   1 
ATOM   14168 C CA  . VAL I 3 152 ? 84.613  67.499  45.564  1.000 45.593  ? 152 VAL GGG CA  1 
ATOM   14169 C C   . VAL I 3 152 ? 85.924  66.817  45.176  1.000 50.260  ? 152 VAL GGG C   1 
ATOM   14170 O O   . VAL I 3 152 ? 86.317  66.921  43.999  1.000 55.744  ? 152 VAL GGG O   1 
ATOM   14171 C CB  . VAL I 3 152 ? 83.431  66.942  44.756  1.000 47.038  ? 152 VAL GGG CB  1 
ATOM   14172 C CG1 . VAL I 3 152 ? 83.369  65.425  44.787  1.000 43.071  ? 152 VAL GGG CG1 1 
ATOM   14173 C CG2 . VAL I 3 152 ? 82.120  67.548  45.220  1.000 49.040  ? 152 VAL GGG CG2 1 
ATOM   14174 N N   . GLN I 3 153 ? 86.568  66.143  46.133  1.000 50.464  ? 153 GLN GGG N   1 
ATOM   14175 C CA  . GLN I 3 153 ? 87.751  65.281  45.897  1.000 46.311  ? 153 GLN GGG CA  1 
ATOM   14176 C C   . GLN I 3 153 ? 87.361  63.816  46.078  1.000 43.144  ? 153 GLN GGG C   1 
ATOM   14177 O O   . GLN I 3 153 ? 86.880  63.457  47.156  1.000 41.836  ? 153 GLN GGG O   1 
ATOM   14178 C CB  . GLN I 3 153 ? 88.887  65.654  46.851  1.000 50.428  ? 153 GLN GGG CB  1 
ATOM   14179 C CG  . GLN I 3 153 ? 90.260  65.119  46.441  1.000 53.501  ? 153 GLN GGG CG  1 
ATOM   14180 C CD  . GLN I 3 153 ? 90.966  66.000  45.443  1.000 56.749  ? 153 GLN GGG CD  1 
ATOM   14181 O OE1 . GLN I 3 153 ? 90.914  67.231  45.534  1.000 64.985  ? 153 GLN GGG OE1 1 
ATOM   14182 N NE2 . GLN I 3 153 ? 91.652  65.369  44.505  1.000 46.427  ? 153 GLN GGG NE2 1 
ATOM   14183 N N   . TRP I 3 154 ? 87.559  63.002  45.048  1.000 41.244  ? 154 TRP GGG N   1 
ATOM   14184 C CA  . TRP I 3 154 ? 87.409  61.537  45.156  1.000 44.927  ? 154 TRP GGG CA  1 
ATOM   14185 C C   . TRP I 3 154 ? 88.705  60.954  45.737  1.000 50.212  ? 154 TRP GGG C   1 
ATOM   14186 O O   . TRP I 3 154 ? 89.790  61.421  45.350  1.000 52.007  ? 154 TRP GGG O   1 
ATOM   14187 C CB  . TRP I 3 154 ? 87.057  60.953  43.793  1.000 47.114  ? 154 TRP GGG CB  1 
ATOM   14188 C CG  . TRP I 3 154 ? 85.607  61.076  43.440  1.000 47.162  ? 154 TRP GGG CG  1 
ATOM   14189 C CD1 . TRP I 3 154 ? 85.062  61.887  42.490  1.000 46.876  ? 154 TRP GGG CD1 1 
ATOM   14190 C CD2 . TRP I 3 154 ? 84.513  60.350  44.025  1.000 47.841  ? 154 TRP GGG CD2 1 
ATOM   14191 N NE1 . TRP I 3 154 ? 83.708  61.718  42.446  1.000 46.624  ? 154 TRP GGG NE1 1 
ATOM   14192 C CE2 . TRP I 3 154 ? 83.341  60.784  43.380  1.000 47.679  ? 154 TRP GGG CE2 1 
ATOM   14193 C CE3 . TRP I 3 154 ? 84.405  59.383  45.029  1.000 48.997  ? 154 TRP GGG CE3 1 
ATOM   14194 C CZ2 . TRP I 3 154 ? 82.085  60.270  43.705  1.000 47.671  ? 154 TRP GGG CZ2 1 
ATOM   14195 C CZ3 . TRP I 3 154 ? 83.165  58.872  45.342  1.000 47.362  ? 154 TRP GGG CZ3 1 
ATOM   14196 C CH2 . TRP I 3 154 ? 82.018  59.317  44.692  1.000 46.904  ? 154 TRP GGG CH2 1 
ATOM   14197 N N   . LYS I 3 155 ? 88.588  59.995  46.659  1.000 49.422  ? 155 LYS GGG N   1 
ATOM   14198 C CA  . LYS I 3 155 ? 89.730  59.296  47.296  1.000 47.172  ? 155 LYS GGG CA  1 
ATOM   14199 C C   . LYS I 3 155 ? 89.498  57.790  47.238  1.000 47.054  ? 155 LYS GGG C   1 
ATOM   14200 O O   . LYS I 3 155 ? 88.522  57.313  47.821  1.000 43.647  ? 155 LYS GGG O   1 
ATOM   14201 C CB  . LYS I 3 155 ? 89.914  59.749  48.744  1.000 48.646  ? 155 LYS GGG CB  1 
ATOM   14202 C CG  . LYS I 3 155 ? 90.591  61.094  48.877  1.000 50.679  ? 155 LYS GGG CG  1 
ATOM   14203 C CD  . LYS I 3 155 ? 90.561  61.657  50.254  1.000 55.302  ? 155 LYS GGG CD  1 
ATOM   14204 C CE  . LYS I 3 155 ? 91.370  62.935  50.306  1.000 64.428  ? 155 LYS GGG CE  1 
ATOM   14205 N NZ  . LYS I 3 155 ? 91.347  63.594  51.629  1.000 70.472  ? 155 LYS GGG NZ  1 
ATOM   14206 N N   . VAL I 3 156 ? 90.405  57.074  46.583  1.000 51.609  ? 156 VAL GGG N   1 
ATOM   14207 C CA  . VAL I 3 156 ? 90.358  55.593  46.454  1.000 52.034  ? 156 VAL GGG CA  1 
ATOM   14208 C C   . VAL I 3 156 ? 91.588  55.017  47.165  1.000 53.881  ? 156 VAL GGG C   1 
ATOM   14209 O O   . VAL I 3 156 ? 92.728  55.202  46.662  1.000 52.258  ? 156 VAL GGG O   1 
ATOM   14210 C CB  . VAL I 3 156 ? 90.275  55.189  44.975  1.000 51.770  ? 156 VAL GGG CB  1 
ATOM   14211 C CG1 . VAL I 3 156 ? 90.217  53.682  44.765  1.000 52.143  ? 156 VAL GGG CG1 1 
ATOM   14212 C CG2 . VAL I 3 156 ? 89.113  55.886  44.313  1.000 52.221  ? 156 VAL GGG CG2 1 
ATOM   14213 N N   . ASP I 3 157 ? 91.348  54.353  48.300  1.000 52.235  ? 157 ASP GGG N   1 
ATOM   14214 C CA  . ASP I 3 157 ? 92.399  53.884  49.238  1.000 48.072  ? 157 ASP GGG CA  1 
ATOM   14215 C C   . ASP I 3 157 ? 93.284  55.080  49.557  1.000 47.951  ? 157 ASP GGG C   1 
ATOM   14216 O O   . ASP I 3 157 ? 94.492  54.944  49.564  1.000 51.888  ? 157 ASP GGG O   1 
ATOM   14217 C CB  . ASP I 3 157 ? 93.171  52.700  48.663  1.000 45.993  ? 157 ASP GGG CB  1 
ATOM   14218 C CG  . ASP I 3 157 ? 92.420  51.393  48.807  1.000 48.247  ? 157 ASP GGG CG  1 
ATOM   14219 O OD1 . ASP I 3 157 ? 91.475  51.326  49.616  1.000 44.668  ? 157 ASP GGG OD1 1 
ATOM   14220 O OD2 . ASP I 3 157 ? 92.793  50.446  48.111  1.000 55.960  ? 157 ASP GGG OD2 1 
ATOM   14221 N N   . ASN I 3 158 ? 92.665  56.236  49.746  1.000 49.735  ? 158 ASN GGG N   1 
ATOM   14222 C CA  . ASN I 3 158 ? 93.335  57.447  50.278  1.000 49.095  ? 158 ASN GGG CA  1 
ATOM   14223 C C   . ASN I 3 158 ? 94.256  58.067  49.209  1.000 45.112  ? 158 ASN GGG C   1 
ATOM   14224 O O   . ASN I 3 158 ? 94.964  59.043  49.542  1.000 44.316  ? 158 ASN GGG O   1 
ATOM   14225 C CB  . ASN I 3 158 ? 93.998  57.105  51.612  1.000 50.499  ? 158 ASN GGG CB  1 
ATOM   14226 C CG  . ASN I 3 158 ? 93.787  58.190  52.643  1.000 54.602  ? 158 ASN GGG CG  1 
ATOM   14227 O OD1 . ASN I 3 158 ? 92.775  58.881  52.625  1.000 57.588  ? 158 ASN GGG OD1 1 
ATOM   14228 N ND2 . ASN I 3 158 ? 94.730  58.346  53.553  1.000 62.439  ? 158 ASN GGG ND2 1 
ATOM   14229 N N   . ALA I 3 159 ? 94.183  57.581  47.962  1.000 43.673  ? 159 ALA GGG N   1 
ATOM   14230 C CA  . ALA I 3 159 ? 94.771  58.211  46.751  1.000 46.268  ? 159 ALA GGG CA  1 
ATOM   14231 C C   . ALA I 3 159 ? 93.755  59.163  46.102  1.000 43.099  ? 159 ALA GGG C   1 
ATOM   14232 O O   . ALA I 3 159 ? 92.707  58.676  45.630  1.000 44.514  ? 159 ALA GGG O   1 
ATOM   14233 C CB  . ALA I 3 159 ? 95.178  57.131  45.770  1.000 47.773  ? 159 ALA GGG CB  1 
ATOM   14234 N N   . LEU I 3 160 ? 94.077  60.449  45.996  1.000 39.854  ? 160 LEU GGG N   1 
ATOM   14235 C CA  . LEU I 3 160 ? 93.234  61.431  45.266  1.000 45.174  ? 160 LEU GGG CA  1 
ATOM   14236 C C   . LEU I 3 160 ? 93.107  61.000  43.798  1.000 47.686  ? 160 LEU GGG C   1 
ATOM   14237 O O   . LEU I 3 160 ? 94.144  60.808  43.160  1.000 58.034  ? 160 LEU GGG O   1 
ATOM   14238 C CB  . LEU I 3 160 ? 93.856  62.828  45.349  1.000 46.319  ? 160 LEU GGG CB  1 
ATOM   14239 C CG  . LEU I 3 160 ? 94.379  63.288  46.712  1.000 48.144  ? 160 LEU GGG CG  1 
ATOM   14240 C CD1 . LEU I 3 160 ? 94.384  64.813  46.786  1.000 51.262  ? 160 LEU GGG CD1 1 
ATOM   14241 C CD2 . LEU I 3 160 ? 93.584  62.713  47.867  1.000 48.138  ? 160 LEU GGG CD2 1 
ATOM   14242 N N   . GLN I 3 161 ? 91.882  60.807  43.298  1.000 44.993  ? 161 GLN GGG N   1 
ATOM   14243 C CA  . GLN I 3 161 ? 91.599  60.492  41.872  1.000 41.113  ? 161 GLN GGG CA  1 
ATOM   14244 C C   . GLN I 3 161 ? 91.427  61.784  41.091  1.000 39.957  ? 161 GLN GGG C   1 
ATOM   14245 O O   . GLN I 3 161 ? 90.986  62.764  41.690  1.000 38.812  ? 161 GLN GGG O   1 
ATOM   14246 C CB  . GLN I 3 161 ? 90.313  59.702  41.729  1.000 43.764  ? 161 GLN GGG CB  1 
ATOM   14247 C CG  . GLN I 3 161 ? 90.395  58.330  42.373  1.000 50.212  ? 161 GLN GGG CG  1 
ATOM   14248 C CD  . GLN I 3 161 ? 91.528  57.507  41.813  1.000 54.123  ? 161 GLN GGG CD  1 
ATOM   14249 O OE1 . GLN I 3 161 ? 91.584  57.242  40.619  1.000 57.344  ? 161 GLN GGG OE1 1 
ATOM   14250 N NE2 . GLN I 3 161 ? 92.438  57.088  42.682  1.000 63.383  ? 161 GLN GGG NE2 1 
ATOM   14251 N N   . SER I 3 162 ? 91.731  61.765  39.795  1.000 40.054  ? 162 SER GGG N   1 
ATOM   14252 C CA  . SER I 3 162 ? 91.619  62.942  38.908  1.000 40.768  ? 162 SER GGG CA  1 
ATOM   14253 C C   . SER I 3 162 ? 91.231  62.524  37.487  1.000 42.767  ? 162 SER GGG C   1 
ATOM   14254 O O   . SER I 3 162 ? 91.799  61.537  36.981  1.000 40.137  ? 162 SER GGG O   1 
ATOM   14255 C CB  . SER I 3 162 ? 92.884  63.720  38.925  1.000 42.279  ? 162 SER GGG CB  1 
ATOM   14256 O OG  . SER I 3 162 ? 92.776  64.837  38.058  1.000 44.654  ? 162 SER GGG OG  1 
ATOM   14257 N N   . GLY I 3 163 ? 90.241  63.231  36.915  1.000 50.240  ? 163 GLY GGG N   1 
ATOM   14258 C CA  . GLY I 3 163 ? 89.801  63.163  35.499  1.000 51.556  ? 163 GLY GGG CA  1 
ATOM   14259 C C   . GLY I 3 163 ? 89.171  61.830  35.112  1.000 46.916  ? 163 GLY GGG C   1 
ATOM   14260 O O   . GLY I 3 163 ? 89.308  61.447  33.947  1.000 45.664  ? 163 GLY GGG O   1 
ATOM   14261 N N   . ASN I 3 164 ? 88.628  61.100  36.090  1.000 43.008  ? 164 ASN GGG N   1 
ATOM   14262 C CA  . ASN I 3 164 ? 87.727  59.936  35.882  1.000 41.717  ? 164 ASN GGG CA  1 
ATOM   14263 C C   . ASN I 3 164 ? 86.389  60.259  36.559  1.000 41.918  ? 164 ASN GGG C   1 
ATOM   14264 O O   . ASN I 3 164 ? 85.693  59.313  36.985  1.000 48.382  ? 164 ASN GGG O   1 
ATOM   14265 C CB  . ASN I 3 164 ? 88.336  58.618  36.391  1.000 39.857  ? 164 ASN GGG CB  1 
ATOM   14266 C CG  . ASN I 3 164 ? 88.912  58.723  37.788  1.000 38.665  ? 164 ASN GGG CG  1 
ATOM   14267 O OD1 . ASN I 3 164 ? 88.898  59.794  38.410  1.000 40.343  ? 164 ASN GGG OD1 1 
ATOM   14268 N ND2 . ASN I 3 164 ? 89.425  57.613  38.281  1.000 33.269  ? 164 ASN GGG ND2 1 
ATOM   14269 N N   . SER I 3 165 ? 86.018  61.539  36.649  1.000 38.639  ? 165 SER GGG N   1 
ATOM   14270 C CA  . SER I 3 165 ? 84.790  61.984  37.352  1.000 39.505  ? 165 SER GGG CA  1 
ATOM   14271 C C   . SER I 3 165 ? 84.130  63.142  36.594  1.000 39.757  ? 165 SER GGG C   1 
ATOM   14272 O O   . SER I 3 165 ? 84.872  63.911  36.015  1.000 40.726  ? 165 SER GGG O   1 
ATOM   14273 C CB  . SER I 3 165 ? 85.138  62.345  38.777  1.000 39.551  ? 165 SER GGG CB  1 
ATOM   14274 O OG  . SER I 3 165 ? 85.576  63.690  38.886  1.000 38.089  ? 165 SER GGG OG  1 
ATOM   14275 N N   . GLN I 3 166 ? 82.794  63.230  36.571  1.000 40.927  ? 166 GLN GGG N   1 
ATOM   14276 C CA  . GLN I 3 166 ? 82.062  64.409  36.027  1.000 43.168  ? 166 GLN GGG CA  1 
ATOM   14277 C C   . GLN I 3 166 ? 81.070  64.911  37.078  1.000 39.997  ? 166 GLN GGG C   1 
ATOM   14278 O O   . GLN I 3 166 ? 80.556  64.100  37.854  1.000 38.476  ? 166 GLN GGG O   1 
ATOM   14279 C CB  . GLN I 3 166 ? 81.328  64.092  34.722  1.000 46.573  ? 166 GLN GGG CB  1 
ATOM   14280 C CG  . GLN I 3 166 ? 81.881  62.893  33.955  1.000 48.572  ? 166 GLN GGG CG  1 
ATOM   14281 C CD  . GLN I 3 166 ? 81.511  62.945  32.489  1.000 52.131  ? 166 GLN GGG CD  1 
ATOM   14282 O OE1 . GLN I 3 166 ? 80.902  62.022  31.923  1.000 49.992  ? 166 GLN GGG OE1 1 
ATOM   14283 N NE2 . GLN I 3 166 ? 81.888  64.053  31.866  1.000 52.995  ? 166 GLN GGG NE2 1 
ATOM   14284 N N   . GLU I 3 167 ? 80.852  66.218  37.102  1.000 38.898  ? 167 GLU GGG N   1 
ATOM   14285 C CA  . GLU I 3 167 ? 79.926  66.875  38.052  1.000 42.947  ? 167 GLU GGG CA  1 
ATOM   14286 C C   . GLU I 3 167 ? 78.662  67.236  37.277  1.000 42.177  ? 167 GLU GGG C   1 
ATOM   14287 O O   . GLU I 3 167 ? 78.676  67.176  36.041  1.000 39.998  ? 167 GLU GGG O   1 
ATOM   14288 C CB  . GLU I 3 167 ? 80.575  68.106  38.697  1.000 45.532  ? 167 GLU GGG CB  1 
ATOM   14289 C CG  . GLU I 3 167 ? 81.743  67.736  39.596  1.000 50.821  ? 167 GLU GGG CG  1 
ATOM   14290 C CD  . GLU I 3 167 ? 82.255  68.825  40.526  1.000 53.598  ? 167 GLU GGG CD  1 
ATOM   14291 O OE1 . GLU I 3 167 ? 82.047  70.024  40.212  1.000 49.910  ? 167 GLU GGG OE1 1 
ATOM   14292 O OE2 . GLU I 3 167 ? 82.860  68.462  41.575  1.000 55.953  ? 167 GLU GGG OE2 1 
ATOM   14293 N N   . SER I 3 168 ? 77.614  67.599  38.004  1.000 39.658  ? 168 SER GGG N   1 
ATOM   14294 C CA  . SER I 3 168 ? 76.299  67.979  37.451  1.000 37.495  ? 168 SER GGG CA  1 
ATOM   14295 C C   . SER I 3 168 ? 75.578  68.801  38.515  1.000 34.600  ? 168 SER GGG C   1 
ATOM   14296 O O   . SER I 3 168 ? 75.643  68.375  39.684  1.000 37.328  ? 168 SER GGG O   1 
ATOM   14297 C CB  . SER I 3 168 ? 75.552  66.732  37.075  1.000 41.229  ? 168 SER GGG CB  1 
ATOM   14298 O OG  . SER I 3 168 ? 74.515  67.022  36.155  1.000 44.867  ? 168 SER GGG OG  1 
ATOM   14299 N N   . VAL I 3 169 ? 74.953  69.922  38.151  1.000 32.027  ? 169 VAL GGG N   1 
ATOM   14300 C CA  . VAL I 3 169 ? 74.323  70.827  39.155  1.000 32.965  ? 169 VAL GGG CA  1 
ATOM   14301 C C   . VAL I 3 169 ? 72.881  71.174  38.777  1.000 33.539  ? 169 VAL GGG C   1 
ATOM   14302 O O   . VAL I 3 169 ? 72.615  71.434  37.587  1.000 32.204  ? 169 VAL GGG O   1 
ATOM   14303 C CB  . VAL I 3 169 ? 75.175  72.085  39.336  1.000 32.818  ? 169 VAL GGG CB  1 
ATOM   14304 C CG1 . VAL I 3 169 ? 74.514  73.129  40.222  1.000 34.976  ? 169 VAL GGG CG1 1 
ATOM   14305 C CG2 . VAL I 3 169 ? 76.514  71.692  39.899  1.000 33.795  ? 169 VAL GGG CG2 1 
ATOM   14306 N N   . THR I 3 170 ? 72.009  71.228  39.787  1.000 34.061  ? 170 THR GGG N   1 
ATOM   14307 C CA  . THR I 3 170 ? 70.590  71.608  39.637  1.000 36.703  ? 170 THR GGG CA  1 
ATOM   14308 C C   . THR I 3 170 ? 70.494  73.124  39.424  1.000 43.329  ? 170 THR GGG C   1 
ATOM   14309 O O   . THR I 3 170 ? 71.426  73.828  39.800  1.000 38.198  ? 170 THR GGG O   1 
ATOM   14310 C CB  . THR I 3 170 ? 69.748  71.149  40.832  1.000 35.275  ? 170 THR GGG CB  1 
ATOM   14311 O OG1 . THR I 3 170 ? 70.012  71.934  41.998  1.000 33.009  ? 170 THR GGG OG1 1 
ATOM   14312 C CG2 . THR I 3 170 ? 69.969  69.687  41.134  1.000 35.336  ? 170 THR GGG CG2 1 
ATOM   14313 N N   . GLU I 3 171 ? 69.401  73.575  38.799  1.000 53.885  ? 171 GLU GGG N   1 
ATOM   14314 C CA  . GLU I 3 171 ? 68.930  74.981  38.806  1.000 59.433  ? 171 GLU GGG CA  1 
ATOM   14315 C C   . GLU I 3 171 ? 68.734  75.406  40.259  1.000 56.076  ? 171 GLU GGG C   1 
ATOM   14316 O O   . GLU I 3 171 ? 68.277  74.582  41.085  1.000 63.462  ? 171 GLU GGG O   1 
ATOM   14317 C CB  . GLU I 3 171 ? 67.580  75.153  38.092  1.000 83.149  ? 171 GLU GGG CB  1 
ATOM   14318 C CG  . GLU I 3 171 ? 67.506  74.617  36.668  1.000 98.315  ? 171 GLU GGG CG  1 
ATOM   14319 C CD  . GLU I 3 171 ? 68.627  75.046  35.733  1.000 109.555 ? 171 GLU GGG CD  1 
ATOM   14320 O OE1 . GLU I 3 171 ? 68.601  74.599  34.561  1.000 128.515 ? 171 GLU GGG OE1 1 
ATOM   14321 O OE2 . GLU I 3 171 ? 69.493  75.852  36.157  1.000 100.051 ? 171 GLU GGG OE2 1 
ATOM   14322 N N   . GLN I 3 172 ? 69.007  76.661  40.563  1.000 45.995  ? 172 GLN GGG N   1 
ATOM   14323 C CA  . GLN I 3 172 ? 68.708  77.177  41.911  1.000 46.355  ? 172 GLN GGG CA  1 
ATOM   14324 C C   . GLN I 3 172 ? 67.242  76.855  42.226  1.000 44.944  ? 172 GLN GGG C   1 
ATOM   14325 O O   . GLN I 3 172 ? 66.398  77.117  41.375  1.000 47.238  ? 172 GLN GGG O   1 
ATOM   14326 C CB  . GLN I 3 172 ? 69.018  78.663  41.959  1.000 48.393  ? 172 GLN GGG CB  1 
ATOM   14327 C CG  . GLN I 3 172 ? 69.038  79.201  43.373  1.000 50.628  ? 172 GLN GGG CG  1 
ATOM   14328 C CD  . GLN I 3 172 ? 69.508  80.628  43.383  1.000 51.819  ? 172 GLN GGG CD  1 
ATOM   14329 O OE1 . GLN I 3 172 ? 69.087  81.429  42.556  1.000 54.636  ? 172 GLN GGG OE1 1 
ATOM   14330 N NE2 . GLN I 3 172 ? 70.368  80.943  44.335  1.000 50.032  ? 172 GLN GGG NE2 1 
ATOM   14331 N N   . ASP I 3 173 ? 66.965  76.284  43.395  1.000 46.160  ? 173 ASP GGG N   1 
ATOM   14332 C CA  . ASP I 3 173 ? 65.611  75.834  43.822  1.000 53.239  ? 173 ASP GGG CA  1 
ATOM   14333 C C   . ASP I 3 173 ? 64.666  77.034  43.989  1.000 55.835  ? 173 ASP GGG C   1 
ATOM   14334 O O   . ASP I 3 173 ? 65.091  78.033  44.577  1.000 52.987  ? 173 ASP GGG O   1 
ATOM   14335 C CB  . ASP I 3 173 ? 65.684  75.057  45.138  1.000 58.389  ? 173 ASP GGG CB  1 
ATOM   14336 C CG  . ASP I 3 173 ? 64.417  74.273  45.456  1.000 57.820  ? 173 ASP GGG CG  1 
ATOM   14337 O OD1 . ASP I 3 173 ? 64.269  73.152  44.911  1.000 53.028  ? 173 ASP GGG OD1 1 
ATOM   14338 O OD2 . ASP I 3 173 ? 63.578  74.802  46.226  1.000 55.147  ? 173 ASP GGG OD2 1 
ATOM   14339 N N   . SER I 3 174 ? 63.415  76.905  43.534  1.000 61.850  ? 174 SER GGG N   1 
ATOM   14340 C CA  . SER I 3 174 ? 62.350  77.943  43.571  1.000 60.216  ? 174 SER GGG CA  1 
ATOM   14341 C C   . SER I 3 174 ? 62.092  78.391  45.010  1.000 63.384  ? 174 SER GGG C   1 
ATOM   14342 O O   . SER I 3 174 ? 61.922  79.602  45.200  1.000 65.902  ? 174 SER GGG O   1 
ATOM   14343 C CB  . SER I 3 174 ? 61.051  77.448  42.969  1.000 63.479  ? 174 SER GGG CB  1 
ATOM   14344 O OG  . SER I 3 174 ? 61.273  76.509  41.929  1.000 69.453  ? 174 SER GGG OG  1 
ATOM   14345 N N   . LYS I 3 175 ? 62.038  77.451  45.965  1.000 63.294  ? 175 LYS GGG N   1 
ATOM   14346 C CA  . LYS I 3 175 ? 61.567  77.712  47.350  1.000 66.326  ? 175 LYS GGG CA  1 
ATOM   14347 C C   . LYS I 3 175 ? 62.739  78.135  48.245  1.000 61.700  ? 175 LYS GGG C   1 
ATOM   14348 O O   . LYS I 3 175 ? 62.574  79.145  48.949  1.000 60.649  ? 175 LYS GGG O   1 
ATOM   14349 C CB  . LYS I 3 175 ? 60.870  76.499  47.975  1.000 78.138  ? 175 LYS GGG CB  1 
ATOM   14350 C CG  . LYS I 3 175 ? 59.846  75.765  47.106  1.000 88.015  ? 175 LYS GGG CG  1 
ATOM   14351 C CD  . LYS I 3 175 ? 59.659  74.288  47.525  1.000 96.355  ? 175 LYS GGG CD  1 
ATOM   14352 C CE  . LYS I 3 175 ? 59.691  73.259  46.400  1.000 98.093  ? 175 LYS GGG CE  1 
ATOM   14353 N NZ  . LYS I 3 175 ? 58.616  73.480  45.406  1.000 96.898  ? 175 LYS GGG NZ  1 
ATOM   14354 N N   . ASP I 3 176 ? 63.861  77.401  48.260  1.000 63.451  ? 176 ASP GGG N   1 
ATOM   14355 C CA  . ASP I 3 176 ? 64.950  77.603  49.269  1.000 64.733  ? 176 ASP GGG CA  1 
ATOM   14356 C C   . ASP I 3 176 ? 66.238  78.155  48.632  1.000 60.340  ? 176 ASP GGG C   1 
ATOM   14357 O O   . ASP I 3 176 ? 67.194  78.366  49.383  1.000 56.635  ? 176 ASP GGG O   1 
ATOM   14358 C CB  . ASP I 3 176 ? 65.222  76.341  50.104  1.000 68.515  ? 176 ASP GGG CB  1 
ATOM   14359 C CG  . ASP I 3 176 ? 65.799  75.141  49.360  1.000 74.598  ? 176 ASP GGG CG  1 
ATOM   14360 O OD1 . ASP I 3 176 ? 66.092  75.274  48.151  1.000 80.319  ? 176 ASP GGG OD1 1 
ATOM   14361 O OD2 . ASP I 3 176 ? 65.968  74.072  50.003  1.000 72.379  ? 176 ASP GGG OD2 1 
ATOM   14362 N N   . SER I 3 177 ? 66.274  78.408  47.318  1.000 55.591  ? 177 SER GGG N   1 
ATOM   14363 C CA  . SER I 3 177 ? 67.402  79.091  46.622  1.000 49.385  ? 177 SER GGG CA  1 
ATOM   14364 C C   . SER I 3 177 ? 68.733  78.356  46.836  1.000 44.398  ? 177 SER GGG C   1 
ATOM   14365 O O   . SER I 3 177 ? 69.769  79.017  46.930  1.000 36.652  ? 177 SER GGG O   1 
ATOM   14366 C CB  . SER I 3 177 ? 67.505  80.509  47.074  1.000 47.727  ? 177 SER GGG CB  1 
ATOM   14367 O OG  . SER I 3 177 ? 66.320  81.203  46.730  1.000 50.104  ? 177 SER GGG OG  1 
ATOM   14368 N N   . THR I 3 178 ? 68.707  77.027  46.880  1.000 43.128  ? 178 THR GGG N   1 
ATOM   14369 C CA  . THR I 3 178 ? 69.917  76.193  47.037  1.000 40.162  ? 178 THR GGG CA  1 
ATOM   14370 C C   . THR I 3 178 ? 70.184  75.455  45.729  1.000 37.001  ? 178 THR GGG C   1 
ATOM   14371 O O   . THR I 3 178 ? 69.245  75.265  44.934  1.000 38.181  ? 178 THR GGG O   1 
ATOM   14372 C CB  . THR I 3 178 ? 69.736  75.213  48.193  1.000 42.166  ? 178 THR GGG CB  1 
ATOM   14373 O OG1 . THR I 3 178 ? 68.714  74.270  47.860  1.000 46.912  ? 178 THR GGG OG1 1 
ATOM   14374 C CG2 . THR I 3 178 ? 69.376  75.921  49.474  1.000 42.798  ? 178 THR GGG CG2 1 
ATOM   14375 N N   . TYR I 3 179 ? 71.427  75.043  45.529  1.000 34.126  ? 179 TYR GGG N   1 
ATOM   14376 C CA  . TYR I 3 179 ? 71.832  74.124  44.444  1.000 34.395  ? 179 TYR GGG CA  1 
ATOM   14377 C C   . TYR I 3 179 ? 72.002  72.722  45.050  1.000 33.065  ? 179 TYR GGG C   1 
ATOM   14378 O O   . TYR I 3 179 ? 72.129  72.581  46.282  1.000 34.335  ? 179 TYR GGG O   1 
ATOM   14379 C CB  . TYR I 3 179 ? 73.098  74.665  43.767  1.000 37.134  ? 179 TYR GGG CB  1 
ATOM   14380 C CG  . TYR I 3 179 ? 73.001  76.053  43.171  1.000 37.343  ? 179 TYR GGG CG  1 
ATOM   14381 C CD1 . TYR I 3 179 ? 72.647  76.230  41.846  1.000 38.865  ? 179 TYR GGG CD1 1 
ATOM   14382 C CD2 . TYR I 3 179 ? 73.314  77.188  43.902  1.000 38.281  ? 179 TYR GGG CD2 1 
ATOM   14383 C CE1 . TYR I 3 179 ? 72.556  77.488  41.273  1.000 43.282  ? 179 TYR GGG CE1 1 
ATOM   14384 C CE2 . TYR I 3 179 ? 73.213  78.457  43.350  1.000 44.119  ? 179 TYR GGG CE2 1 
ATOM   14385 C CZ  . TYR I 3 179 ? 72.840  78.615  42.022  1.000 46.874  ? 179 TYR GGG CZ  1 
ATOM   14386 O OH  . TYR I 3 179 ? 72.727  79.853  41.436  1.000 50.356  ? 179 TYR GGG OH  1 
ATOM   14387 N N   . SER I 3 180 ? 71.945  71.703  44.198  1.000 32.438  ? 180 SER GGG N   1 
ATOM   14388 C CA  . SER I 3 180 ? 72.389  70.316  44.490  1.000 33.283  ? 180 SER GGG CA  1 
ATOM   14389 C C   . SER I 3 180 ? 73.350  69.869  43.378  1.000 32.407  ? 180 SER GGG C   1 
ATOM   14390 O O   . SER I 3 180 ? 73.223  70.355  42.235  1.000 31.646  ? 180 SER GGG O   1 
ATOM   14391 C CB  . SER I 3 180 ? 71.217  69.367  44.674  1.000 33.465  ? 180 SER GGG CB  1 
ATOM   14392 O OG  . SER I 3 180 ? 70.582  69.551  45.942  1.000 34.901  ? 180 SER GGG OG  1 
ATOM   14393 N N   . LEU I 3 181 ? 74.298  69.004  43.720  1.000 32.426  ? 181 LEU GGG N   1 
ATOM   14394 C CA  . LEU I 3 181 ? 75.422  68.612  42.844  1.000 35.635  ? 181 LEU GGG CA  1 
ATOM   14395 C C   . LEU I 3 181 ? 75.614  67.095  42.947  1.000 36.257  ? 181 LEU GGG C   1 
ATOM   14396 O O   . LEU I 3 181 ? 75.553  66.584  44.085  1.000 36.389  ? 181 LEU GGG O   1 
ATOM   14397 C CB  . LEU I 3 181 ? 76.668  69.389  43.295  1.000 38.984  ? 181 LEU GGG CB  1 
ATOM   14398 C CG  . LEU I 3 181 ? 77.935  69.144  42.459  1.000 40.197  ? 181 LEU GGG CG  1 
ATOM   14399 C CD1 . LEU I 3 181 ? 78.846  70.356  42.427  1.000 41.368  ? 181 LEU GGG CD1 1 
ATOM   14400 C CD2 . LEU I 3 181 ? 78.710  67.946  42.980  1.000 40.672  ? 181 LEU GGG CD2 1 
ATOM   14401 N N   . SER I 3 182 ? 75.844  66.425  41.811  1.000 36.589  ? 182 SER GGG N   1 
ATOM   14402 C CA  . SER I 3 182 ? 76.222  64.991  41.738  1.000 39.658  ? 182 SER GGG CA  1 
ATOM   14403 C C   . SER I 3 182 ? 77.589  64.853  41.056  1.000 41.347  ? 182 SER GGG C   1 
ATOM   14404 O O   . SER I 3 182 ? 77.716  65.213  39.855  1.000 36.757  ? 182 SER GGG O   1 
ATOM   14405 C CB  . SER I 3 182 ? 75.178  64.155  41.044  1.000 41.597  ? 182 SER GGG CB  1 
ATOM   14406 O OG  . SER I 3 182 ? 75.377  64.134  39.629  1.000 43.641  ? 182 SER GGG OG  1 
ATOM   14407 N N   . SER I 3 183 ? 78.561  64.348  41.821  1.000 42.610  ? 183 SER GGG N   1 
ATOM   14408 C CA  . SER I 3 183 ? 79.882  63.891  41.339  1.000 42.085  ? 183 SER GGG CA  1 
ATOM   14409 C C   . SER I 3 183 ? 79.784  62.388  41.123  1.000 39.776  ? 183 SER GGG C   1 
ATOM   14410 O O   . SER I 3 183 ? 79.306  61.698  42.024  1.000 41.590  ? 183 SER GGG O   1 
ATOM   14411 C CB  . SER I 3 183 ? 80.979  64.240  42.312  1.000 45.088  ? 183 SER GGG CB  1 
ATOM   14412 O OG  . SER I 3 183 ? 82.246  64.213  41.667  1.000 49.245  ? 183 SER GGG OG  1 
ATOM   14413 N N   . THR I 3 184 ? 80.189  61.918  39.953  1.000 39.600  ? 184 THR GGG N   1 
ATOM   14414 C CA  . THR I 3 184 ? 80.066  60.510  39.531  1.000 40.456  ? 184 THR GGG CA  1 
ATOM   14415 C C   . THR I 3 184 ? 81.450  60.031  39.115  1.000 41.759  ? 184 THR GGG C   1 
ATOM   14416 O O   . THR I 3 184 ? 81.943  60.481  38.073  1.000 42.607  ? 184 THR GGG O   1 
ATOM   14417 C CB  . THR I 3 184 ? 79.050  60.359  38.395  1.000 42.846  ? 184 THR GGG CB  1 
ATOM   14418 O OG1 . THR I 3 184 ? 77.826  60.934  38.859  1.000 43.283  ? 184 THR GGG OG1 1 
ATOM   14419 C CG2 . THR I 3 184 ? 78.839  58.917  37.982  1.000 41.736  ? 184 THR GGG CG2 1 
ATOM   14420 N N   . LEU I 3 185 ? 82.044  59.163  39.926  1.000 41.353  ? 185 LEU GGG N   1 
ATOM   14421 C CA  . LEU I 3 185 ? 83.367  58.549  39.676  1.000 39.612  ? 185 LEU GGG CA  1 
ATOM   14422 C C   . LEU I 3 185 ? 83.143  57.258  38.898  1.000 39.923  ? 185 LEU GGG C   1 
ATOM   14423 O O   . LEU I 3 185 ? 82.389  56.417  39.369  1.000 43.014  ? 185 LEU GGG O   1 
ATOM   14424 C CB  . LEU I 3 185 ? 84.025  58.297  41.025  1.000 41.378  ? 185 LEU GGG CB  1 
ATOM   14425 C CG  . LEU I 3 185 ? 85.342  57.538  40.988  1.000 46.461  ? 185 LEU GGG CG  1 
ATOM   14426 C CD1 . LEU I 3 185 ? 86.474  58.441  40.530  1.000 47.645  ? 185 LEU GGG CD1 1 
ATOM   14427 C CD2 . LEU I 3 185 ? 85.647  56.924  42.350  1.000 46.963  ? 185 LEU GGG CD2 1 
ATOM   14428 N N   . THR I 3 186 ? 83.747  57.136  37.722  1.000 46.556  ? 186 THR GGG N   1 
ATOM   14429 C CA  . THR I 3 186 ? 83.516  56.018  36.766  1.000 53.109  ? 186 THR GGG CA  1 
ATOM   14430 C C   . THR I 3 186 ? 84.823  55.258  36.548  1.000 50.381  ? 186 THR GGG C   1 
ATOM   14431 O O   . THR I 3 186 ? 85.824  55.909  36.194  1.000 52.467  ? 186 THR GGG O   1 
ATOM   14432 C CB  . THR I 3 186 ? 82.951  56.547  35.441  1.000 62.351  ? 186 THR GGG CB  1 
ATOM   14433 O OG1 . THR I 3 186 ? 81.892  57.443  35.781  1.000 76.777  ? 186 THR GGG OG1 1 
ATOM   14434 C CG2 . THR I 3 186 ? 82.442  55.448  34.532  1.000 62.402  ? 186 THR GGG CG2 1 
ATOM   14435 N N   . LEU I 3 187 ? 84.823  53.944  36.779  1.000 50.343  ? 187 LEU GGG N   1 
ATOM   14436 C CA  . LEU I 3 187 ? 86.014  53.089  36.550  1.000 52.362  ? 187 LEU GGG CA  1 
ATOM   14437 C C   . LEU I 3 187 ? 85.569  51.645  36.288  1.000 54.120  ? 187 LEU GGG C   1 
ATOM   14438 O O   . LEU I 3 187 ? 84.431  51.308  36.652  1.000 53.861  ? 187 LEU GGG O   1 
ATOM   14439 C CB  . LEU I 3 187 ? 86.996  53.219  37.727  1.000 51.701  ? 187 LEU GGG CB  1 
ATOM   14440 C CG  . LEU I 3 187 ? 86.451  53.006  39.139  1.000 51.440  ? 187 LEU GGG CG  1 
ATOM   14441 C CD1 . LEU I 3 187 ? 87.502  52.382  40.054  1.000 52.249  ? 187 LEU GGG CD1 1 
ATOM   14442 C CD2 . LEU I 3 187 ? 85.949  54.312  39.723  1.000 53.862  ? 187 LEU GGG CD2 1 
ATOM   14443 N N   . SER I 3 188 ? 86.428  50.870  35.608  1.000 59.166  ? 188 SER GGG N   1 
ATOM   14444 C CA  . SER I 3 188 ? 86.200  49.462  35.175  1.000 59.164  ? 188 SER GGG CA  1 
ATOM   14445 C C   . SER I 3 188 ? 85.993  48.566  36.396  1.000 56.454  ? 188 SER GGG C   1 
ATOM   14446 O O   . SER I 3 188 ? 86.527  48.910  37.482  1.000 51.491  ? 188 SER GGG O   1 
ATOM   14447 C CB  . SER I 3 188 ? 87.347  48.953  34.338  1.000 60.186  ? 188 SER GGG CB  1 
ATOM   14448 O OG  . SER I 3 188 ? 88.562  48.974  35.072  1.000 57.484  ? 188 SER GGG OG  1 
ATOM   14449 N N   . LYS I 3 189 ? 85.262  47.459  36.220  1.000 54.301  ? 189 LYS GGG N   1 
ATOM   14450 C CA  . LYS I 3 189 ? 84.959  46.510  37.322  1.000 55.462  ? 189 LYS GGG CA  1 
ATOM   14451 C C   . LYS I 3 189 ? 86.285  46.038  37.911  1.000 54.756  ? 189 LYS GGG C   1 
ATOM   14452 O O   . LYS I 3 189 ? 86.391  45.996  39.149  1.000 51.722  ? 189 LYS GGG O   1 
ATOM   14453 C CB  . LYS I 3 189 ? 84.161  45.296  36.845  1.000 60.585  ? 189 LYS GGG CB  1 
ATOM   14454 C CG  . LYS I 3 189 ? 83.814  44.295  37.936  1.000 65.343  ? 189 LYS GGG CG  1 
ATOM   14455 C CD  . LYS I 3 189 ? 83.427  42.938  37.413  1.000 71.134  ? 189 LYS GGG CD  1 
ATOM   14456 C CE  . LYS I 3 189 ? 83.170  41.950  38.529  1.000 78.428  ? 189 LYS GGG CE  1 
ATOM   14457 N NZ  . LYS I 3 189 ? 82.847  40.601  38.012  1.000 83.232  ? 189 LYS GGG NZ  1 
ATOM   14458 N N   . ALA I 3 190 ? 87.233  45.692  37.036  1.000 54.468  ? 190 ALA GGG N   1 
ATOM   14459 C CA  . ALA I 3 190 ? 88.628  45.339  37.375  1.000 54.942  ? 190 ALA GGG CA  1 
ATOM   14460 C C   . ALA I 3 190 ? 89.193  46.351  38.385  1.000 56.489  ? 190 ALA GGG C   1 
ATOM   14461 O O   . ALA I 3 190 ? 89.462  45.949  39.531  1.000 53.122  ? 190 ALA GGG O   1 
ATOM   14462 C CB  . ALA I 3 190 ? 89.446  45.290  36.109  1.000 57.476  ? 190 ALA GGG CB  1 
ATOM   14463 N N   . ASP I 3 191 ? 89.342  47.619  37.984  1.000 64.036  ? 191 ASP GGG N   1 
ATOM   14464 C CA  . ASP I 3 191 ? 89.988  48.677  38.816  1.000 65.398  ? 191 ASP GGG CA  1 
ATOM   14465 C C   . ASP I 3 191 ? 89.151  48.927  40.079  1.000 60.018  ? 191 ASP GGG C   1 
ATOM   14466 O O   . ASP I 3 191 ? 89.751  49.331  41.091  1.000 53.502  ? 191 ASP GGG O   1 
ATOM   14467 C CB  . ASP I 3 191 ? 90.252  49.962  38.024  1.000 71.157  ? 191 ASP GGG CB  1 
ATOM   14468 C CG  . ASP I 3 191 ? 91.306  49.784  36.939  1.000 80.751  ? 191 ASP GGG CG  1 
ATOM   14469 O OD1 . ASP I 3 191 ? 92.025  48.768  36.977  1.000 88.714  ? 191 ASP GGG OD1 1 
ATOM   14470 O OD2 . ASP I 3 191 ? 91.391  50.648  36.049  1.000 83.914  ? 191 ASP GGG OD2 1 
ATOM   14471 N N   . TYR I 3 192 ? 87.832  48.684  40.040  1.000 55.257  ? 192 TYR GGG N   1 
ATOM   14472 C CA  . TYR I 3 192 ? 86.946  48.877  41.218  1.000 50.816  ? 192 TYR GGG CA  1 
ATOM   14473 C C   . TYR I 3 192 ? 87.363  47.882  42.308  1.000 54.046  ? 192 TYR GGG C   1 
ATOM   14474 O O   . TYR I 3 192 ? 87.400  48.276  43.496  1.000 50.950  ? 192 TYR GGG O   1 
ATOM   14475 C CB  . TYR I 3 192 ? 85.453  48.770  40.875  1.000 43.440  ? 192 TYR GGG CB  1 
ATOM   14476 C CG  . TYR I 3 192 ? 84.543  48.902  42.074  1.000 38.211  ? 192 TYR GGG CG  1 
ATOM   14477 C CD1 . TYR I 3 192 ? 84.452  50.096  42.764  1.000 35.888  ? 192 TYR GGG CD1 1 
ATOM   14478 C CD2 . TYR I 3 192 ? 83.785  47.835  42.535  1.000 36.489  ? 192 TYR GGG CD2 1 
ATOM   14479 C CE1 . TYR I 3 192 ? 83.631  50.235  43.873  1.000 35.845  ? 192 TYR GGG CE1 1 
ATOM   14480 C CE2 . TYR I 3 192 ? 82.963  47.950  43.647  1.000 36.425  ? 192 TYR GGG CE2 1 
ATOM   14481 C CZ  . TYR I 3 192 ? 82.893  49.154  44.326  1.000 37.153  ? 192 TYR GGG CZ  1 
ATOM   14482 O OH  . TYR I 3 192 ? 82.103  49.276  45.434  1.000 37.958  ? 192 TYR GGG OH  1 
ATOM   14483 N N   . GLU I 3 193 ? 87.692  46.648  41.917  1.000 58.576  ? 193 GLU GGG N   1 
ATOM   14484 C CA  . GLU I 3 193 ? 87.860  45.506  42.858  1.000 60.225  ? 193 GLU GGG CA  1 
ATOM   14485 C C   . GLU I 3 193 ? 89.308  45.428  43.353  1.000 59.888  ? 193 GLU GGG C   1 
ATOM   14486 O O   . GLU I 3 193 ? 89.556  44.586  44.213  1.000 60.056  ? 193 GLU GGG O   1 
ATOM   14487 C CB  . GLU I 3 193 ? 87.385  44.206  42.207  1.000 62.177  ? 193 GLU GGG CB  1 
ATOM   14488 C CG  . GLU I 3 193 ? 85.872  44.055  42.220  1.000 66.520  ? 193 GLU GGG CG  1 
ATOM   14489 C CD  . GLU I 3 193 ? 85.309  42.879  41.419  1.000 73.035  ? 193 GLU GGG CD  1 
ATOM   14490 O OE1 . GLU I 3 193 ? 86.076  42.207  40.693  1.000 75.384  ? 193 GLU GGG OE1 1 
ATOM   14491 O OE2 . GLU I 3 193 ? 84.088  42.618  41.519  1.000 79.889  ? 193 GLU GGG OE2 1 
ATOM   14492 N N   . LYS I 3 194 ? 90.205  46.298  42.876  1.000 63.802  ? 194 LYS GGG N   1 
ATOM   14493 C CA  . LYS I 3 194 ? 91.610  46.385  43.354  1.000 63.512  ? 194 LYS GGG CA  1 
ATOM   14494 C C   . LYS I 3 194 ? 91.677  47.154  44.672  1.000 62.480  ? 194 LYS GGG C   1 
ATOM   14495 O O   . LYS I 3 194 ? 92.680  47.020  45.353  1.000 80.325  ? 194 LYS GGG O   1 
ATOM   14496 C CB  . LYS I 3 194 ? 92.503  47.121  42.358  1.000 66.759  ? 194 LYS GGG CB  1 
ATOM   14497 C CG  . LYS I 3 194 ? 92.453  46.595  40.933  1.000 76.113  ? 194 LYS GGG CG  1 
ATOM   14498 C CD  . LYS I 3 194 ? 93.451  47.283  40.032  1.000 80.671  ? 194 LYS GGG CD  1 
ATOM   14499 C CE  . LYS I 3 194 ? 94.891  47.075  40.437  1.000 83.139  ? 194 LYS GGG CE  1 
ATOM   14500 N NZ  . LYS I 3 194 ? 95.762  47.291  39.270  1.000 90.763  ? 194 LYS GGG NZ  1 
ATOM   14501 N N   . HIS I 3 195 ? 90.664  47.946  45.007  1.000 57.278  ? 195 HIS GGG N   1 
ATOM   14502 C CA  . HIS I 3 195 ? 90.705  48.878  46.157  1.000 55.436  ? 195 HIS GGG CA  1 
ATOM   14503 C C   . HIS I 3 195 ? 89.562  48.578  47.132  1.000 52.515  ? 195 HIS GGG C   1 
ATOM   14504 O O   . HIS I 3 195 ? 88.685  47.777  46.791  1.000 45.346  ? 195 HIS GGG O   1 
ATOM   14505 C CB  . HIS I 3 195 ? 90.677  50.306  45.625  1.000 64.353  ? 195 HIS GGG CB  1 
ATOM   14506 C CG  . HIS I 3 195 ? 91.695  50.579  44.571  1.000 70.235  ? 195 HIS GGG CG  1 
ATOM   14507 N ND1 . HIS I 3 195 ? 91.333  50.970  43.298  1.000 79.235  ? 195 HIS GGG ND1 1 
ATOM   14508 C CD2 . HIS I 3 195 ? 93.046  50.542  44.599  1.000 68.272  ? 195 HIS GGG CD2 1 
ATOM   14509 C CE1 . HIS I 3 195 ? 92.420  51.156  42.578  1.000 79.038  ? 195 HIS GGG CE1 1 
ATOM   14510 N NE2 . HIS I 3 195 ? 93.484  50.893  43.358  1.000 73.944  ? 195 HIS GGG NE2 1 
ATOM   14511 N N   . LYS I 3 196 ? 89.583  49.222  48.302  1.000 51.944  ? 196 LYS GGG N   1 
ATOM   14512 C CA  . LYS I 3 196 ? 88.691  48.926  49.454  1.000 55.259  ? 196 LYS GGG CA  1 
ATOM   14513 C C   . LYS I 3 196 ? 87.881  50.178  49.801  1.000 50.542  ? 196 LYS GGG C   1 
ATOM   14514 O O   . LYS I 3 196 ? 86.640  50.104  49.773  1.000 44.544  ? 196 LYS GGG O   1 
ATOM   14515 C CB  . LYS I 3 196 ? 89.531  48.441  50.646  1.000 68.881  ? 196 LYS GGG CB  1 
ATOM   14516 C CG  . LYS I 3 196 ? 88.776  48.029  51.914  1.000 77.683  ? 196 LYS GGG CG  1 
ATOM   14517 C CD  . LYS I 3 196 ? 87.597  47.068  51.709  1.000 88.165  ? 196 LYS GGG CD  1 
ATOM   14518 C CE  . LYS I 3 196 ? 87.864  45.886  50.794  1.000 97.101  ? 196 LYS GGG CE  1 
ATOM   14519 N NZ  . LYS I 3 196 ? 88.721  44.875  51.450  1.000 105.765 ? 196 LYS GGG NZ  1 
ATOM   14520 N N   . VAL I 3 197 ? 88.556  51.279  50.133  1.000 49.192  ? 197 VAL GGG N   1 
ATOM   14521 C CA  . VAL I 3 197 ? 87.928  52.529  50.655  1.000 47.634  ? 197 VAL GGG CA  1 
ATOM   14522 C C   . VAL I 3 197 ? 87.698  53.502  49.502  1.000 46.939  ? 197 VAL GGG C   1 
ATOM   14523 O O   . VAL I 3 197 ? 88.682  54.057  48.975  1.000 45.957  ? 197 VAL GGG O   1 
ATOM   14524 C CB  . VAL I 3 197 ? 88.798  53.186  51.735  1.000 48.766  ? 197 VAL GGG CB  1 
ATOM   14525 C CG1 . VAL I 3 197 ? 88.248  54.533  52.185  1.000 49.289  ? 197 VAL GGG CG1 1 
ATOM   14526 C CG2 . VAL I 3 197 ? 88.980  52.251  52.912  1.000 51.621  ? 197 VAL GGG CG2 1 
ATOM   14527 N N   . TYR I 3 198 ? 86.430  53.733  49.177  1.000 44.716  ? 198 TYR GGG N   1 
ATOM   14528 C CA  . TYR I 3 198 ? 85.968  54.785  48.241  1.000 38.680  ? 198 TYR GGG CA  1 
ATOM   14529 C C   . TYR I 3 198 ? 85.413  55.930  49.071  1.000 34.378  ? 198 TYR GGG C   1 
ATOM   14530 O O   . TYR I 3 198 ? 84.529  55.664  49.871  1.000 33.476  ? 198 TYR GGG O   1 
ATOM   14531 C CB  . TYR I 3 198 ? 84.950  54.178  47.283  1.000 36.483  ? 198 TYR GGG CB  1 
ATOM   14532 C CG  . TYR I 3 198 ? 85.597  53.237  46.313  1.000 36.238  ? 198 TYR GGG CG  1 
ATOM   14533 C CD1 . TYR I 3 198 ? 86.068  53.690  45.089  1.000 37.812  ? 198 TYR GGG CD1 1 
ATOM   14534 C CD2 . TYR I 3 198 ? 85.830  51.924  46.663  1.000 34.587  ? 198 TYR GGG CD2 1 
ATOM   14535 C CE1 . TYR I 3 198 ? 86.709  52.841  44.207  1.000 39.011  ? 198 TYR GGG CE1 1 
ATOM   14536 C CE2 . TYR I 3 198 ? 86.459  51.058  45.787  1.000 36.036  ? 198 TYR GGG CE2 1 
ATOM   14537 C CZ  . TYR I 3 198 ? 86.900  51.517  44.559  1.000 38.769  ? 198 TYR GGG CZ  1 
ATOM   14538 O OH  . TYR I 3 198 ? 87.532  50.679  43.686  1.000 41.042  ? 198 TYR GGG OH  1 
ATOM   14539 N N   . ALA I 3 199 ? 85.941  57.135  48.904  1.000 34.067  ? 199 ALA GGG N   1 
ATOM   14540 C CA  . ALA I 3 199 ? 85.594  58.294  49.755  1.000 38.328  ? 199 ALA GGG CA  1 
ATOM   14541 C C   . ALA I 3 199 ? 85.366  59.538  48.908  1.000 40.377  ? 199 ALA GGG C   1 
ATOM   14542 O O   . ALA I 3 199 ? 85.942  59.695  47.827  1.000 40.240  ? 199 ALA GGG O   1 
ATOM   14543 C CB  . ALA I 3 199 ? 86.662  58.567  50.788  1.000 39.141  ? 199 ALA GGG CB  1 
ATOM   14544 N N   . CYS I 3 200 ? 84.550  60.416  49.450  1.000 42.404  ? 200 CYS GGG N   1 
ATOM   14545 C CA  . CYS I 3 200 ? 84.099  61.647  48.796  1.000 44.139  ? 200 CYS GGG CA  1 
ATOM   14546 C C   . CYS I 3 200 ? 84.326  62.765  49.801  1.000 44.337  ? 200 CYS GGG C   1 
ATOM   14547 O O   . CYS I 3 200 ? 83.639  62.749  50.830  1.000 48.378  ? 200 CYS GGG O   1 
ATOM   14548 C CB  . CYS I 3 200 ? 82.638  61.484  48.417  1.000 48.094  ? 200 CYS GGG CB  1 
ATOM   14549 S SG  . CYS I 3 200 ? 82.019  62.962  47.605  1.000 57.883  ? 200 CYS GGG SG  1 
ATOM   14550 N N   . GLU I 3 201 ? 85.303  63.634  49.552  1.000 45.151  ? 201 GLU GGG N   1 
ATOM   14551 C CA  . GLU I 3 201 ? 85.703  64.716  50.489  1.000 50.240  ? 201 GLU GGG CA  1 
ATOM   14552 C C   . GLU I 3 201 ? 85.200  66.045  49.930  1.000 48.647  ? 201 GLU GGG C   1 
ATOM   14553 O O   . GLU I 3 201 ? 85.712  66.497  48.878  1.000 49.656  ? 201 GLU GGG O   1 
ATOM   14554 C CB  . GLU I 3 201 ? 87.217  64.738  50.712  1.000 61.404  ? 201 GLU GGG CB  1 
ATOM   14555 C CG  . GLU I 3 201 ? 87.674  65.830  51.667  1.000 67.279  ? 201 GLU GGG CG  1 
ATOM   14556 C CD  . GLU I 3 201 ? 89.169  66.118  51.658  1.000 72.717  ? 201 GLU GGG CD  1 
ATOM   14557 O OE1 . GLU I 3 201 ? 89.780  66.007  52.743  1.000 75.247  ? 201 GLU GGG OE1 1 
ATOM   14558 O OE2 . GLU I 3 201 ? 89.721  66.471  50.573  1.000 74.435  ? 201 GLU GGG OE2 1 
ATOM   14559 N N   . VAL I 3 202 ? 84.254  66.657  50.641  1.000 49.088  ? 202 VAL GGG N   1 
ATOM   14560 C CA  . VAL I 3 202 ? 83.511  67.865  50.191  1.000 49.055  ? 202 VAL GGG CA  1 
ATOM   14561 C C   . VAL I 3 202 ? 84.003  69.077  50.977  1.000 51.219  ? 202 VAL GGG C   1 
ATOM   14562 O O   . VAL I 3 202 ? 83.931  69.053  52.217  1.000 55.110  ? 202 VAL GGG O   1 
ATOM   14563 C CB  . VAL I 3 202 ? 82.000  67.687  50.379  1.000 46.380  ? 202 VAL GGG CB  1 
ATOM   14564 C CG1 . VAL I 3 202 ? 81.249  68.980  50.111  1.000 47.520  ? 202 VAL GGG CG1 1 
ATOM   14565 C CG2 . VAL I 3 202 ? 81.470  66.558  49.518  1.000 46.757  ? 202 VAL GGG CG2 1 
ATOM   14566 N N   . THR I 3 203 ? 84.457  70.101  50.257  1.000 51.305  ? 203 THR GGG N   1 
ATOM   14567 C CA  . THR I 3 203 ? 84.830  71.419  50.813  1.000 48.496  ? 203 THR GGG CA  1 
ATOM   14568 C C   . THR I 3 203 ? 83.812  72.441  50.332  1.000 47.986  ? 203 THR GGG C   1 
ATOM   14569 O O   . THR I 3 203 ? 83.572  72.527  49.098  1.000 46.645  ? 203 THR GGG O   1 
ATOM   14570 C CB  . THR I 3 203 ? 86.232  71.832  50.379  1.000 48.055  ? 203 THR GGG CB  1 
ATOM   14571 O OG1 . THR I 3 203 ? 86.994  70.626  50.341  1.000 52.555  ? 203 THR GGG OG1 1 
ATOM   14572 C CG2 . THR I 3 203 ? 86.838  72.854  51.310  1.000 50.436  ? 203 THR GGG CG2 1 
ATOM   14573 N N   . HIS I 3 204 ? 83.231  73.169  51.280  1.000 46.617  ? 204 HIS GGG N   1 
ATOM   14574 C CA  . HIS I 3 204 ? 82.228  74.220  51.002  1.000 46.978  ? 204 HIS GGG CA  1 
ATOM   14575 C C   . HIS I 3 204 ? 82.383  75.329  52.024  1.000 46.252  ? 204 HIS GGG C   1 
ATOM   14576 O O   . HIS I 3 204 ? 82.824  75.037  53.148  1.000 48.777  ? 204 HIS GGG O   1 
ATOM   14577 C CB  . HIS I 3 204 ? 80.810  73.652  51.034  1.000 46.384  ? 204 HIS GGG CB  1 
ATOM   14578 C CG  . HIS I 3 204 ? 79.796  74.640  50.582  1.000 44.910  ? 204 HIS GGG CG  1 
ATOM   14579 N ND1 . HIS I 3 204 ? 78.931  75.234  51.450  1.000 47.530  ? 204 HIS GGG ND1 1 
ATOM   14580 C CD2 . HIS I 3 204 ? 79.556  75.194  49.382  1.000 44.165  ? 204 HIS GGG CD2 1 
ATOM   14581 C CE1 . HIS I 3 204 ? 78.173  76.093  50.808  1.000 46.283  ? 204 HIS GGG CE1 1 
ATOM   14582 N NE2 . HIS I 3 204 ? 78.527  76.082  49.534  1.000 44.821  ? 204 HIS GGG NE2 1 
ATOM   14583 N N   . GLN I 3 205 ? 82.001  76.539  51.643  1.000 47.848  ? 205 GLN GGG N   1 
ATOM   14584 C CA  . GLN I 3 205 ? 82.159  77.731  52.506  1.000 51.241  ? 205 GLN GGG CA  1 
ATOM   14585 C C   . GLN I 3 205 ? 81.354  77.549  53.807  1.000 51.434  ? 205 GLN GGG C   1 
ATOM   14586 O O   . GLN I 3 205 ? 81.745  78.144  54.806  1.000 59.720  ? 205 GLN GGG O   1 
ATOM   14587 C CB  . GLN I 3 205 ? 81.775  78.974  51.710  1.000 53.248  ? 205 GLN GGG CB  1 
ATOM   14588 C CG  . GLN I 3 205 ? 81.839  80.249  52.527  1.000 57.695  ? 205 GLN GGG CG  1 
ATOM   14589 C CD  . GLN I 3 205 ? 81.079  81.358  51.854  1.000 62.531  ? 205 GLN GGG CD  1 
ATOM   14590 O OE1 . GLN I 3 205 ? 80.987  81.397  50.626  1.000 66.216  ? 205 GLN GGG OE1 1 
ATOM   14591 N NE2 . GLN I 3 205 ? 80.517  82.244  52.665  1.000 61.355  ? 205 GLN GGG NE2 1 
ATOM   14592 N N   . GLY I 3 206 ? 80.297  76.738  53.829  1.000 51.414  ? 206 GLY GGG N   1 
ATOM   14593 C CA  . GLY I 3 206 ? 79.459  76.534  55.029  1.000 51.418  ? 206 GLY GGG CA  1 
ATOM   14594 C C   . GLY I 3 206 ? 79.959  75.411  55.926  1.000 52.360  ? 206 GLY GGG C   1 
ATOM   14595 O O   . GLY I 3 206 ? 79.277  75.102  56.916  1.000 55.778  ? 206 GLY GGG O   1 
ATOM   14596 N N   . LEU I 3 207 ? 81.081  74.784  55.577  1.000 52.243  ? 207 LEU GGG N   1 
ATOM   14597 C CA  . LEU I 3 207 ? 81.689  73.680  56.361  1.000 52.473  ? 207 LEU GGG CA  1 
ATOM   14598 C C   . LEU I 3 207 ? 83.005  74.176  56.950  1.000 62.227  ? 207 LEU GGG C   1 
ATOM   14599 O O   . LEU I 3 207 ? 83.931  74.438  56.155  1.000 65.565  ? 207 LEU GGG O   1 
ATOM   14600 C CB  . LEU I 3 207 ? 81.955  72.489  55.441  1.000 49.736  ? 207 LEU GGG CB  1 
ATOM   14601 C CG  . LEU I 3 207 ? 80.729  71.771  54.899  1.000 46.242  ? 207 LEU GGG CG  1 
ATOM   14602 C CD1 . LEU I 3 207 ? 81.138  70.732  53.877  1.000 45.993  ? 207 LEU GGG CD1 1 
ATOM   14603 C CD2 . LEU I 3 207 ? 79.940  71.139  56.027  1.000 47.873  ? 207 LEU GGG CD2 1 
ATOM   14604 N N   . SER I 3 208 ? 83.073  74.292  58.282  1.000 71.611  ? 208 SER GGG N   1 
ATOM   14605 C CA  . SER I 3 208 ? 84.273  74.715  59.055  1.000 74.016  ? 208 SER GGG CA  1 
ATOM   14606 C C   . SER I 3 208 ? 85.473  73.834  58.674  1.000 70.705  ? 208 SER GGG C   1 
ATOM   14607 O O   . SER I 3 208 ? 86.609  74.347  58.595  1.000 71.193  ? 208 SER GGG O   1 
ATOM   14608 C CB  . SER I 3 208 ? 83.993  74.654  60.536  1.000 79.026  ? 208 SER GGG CB  1 
ATOM   14609 O OG  . SER I 3 208 ? 83.786  73.310  60.955  1.000 83.106  ? 208 SER GGG OG  1 
ATOM   14610 N N   . SER I 3 209 ? 85.210  72.552  58.438  1.000 65.627  ? 209 SER GGG N   1 
ATOM   14611 C CA  . SER I 3 209 ? 86.208  71.527  58.061  1.000 64.823  ? 209 SER GGG CA  1 
ATOM   14612 C C   . SER I 3 209 ? 85.617  70.644  56.957  1.000 63.396  ? 209 SER GGG C   1 
ATOM   14613 O O   . SER I 3 209 ? 84.426  70.331  56.975  1.000 63.593  ? 209 SER GGG O   1 
ATOM   14614 C CB  . SER I 3 209 ? 86.595  70.754  59.294  1.000 64.822  ? 209 SER GGG CB  1 
ATOM   14615 O OG  . SER I 3 209 ? 87.072  69.465  58.954  1.000 66.802  ? 209 SER GGG OG  1 
ATOM   14616 N N   . PRO I 3 210 ? 86.408  70.252  55.931  1.000 57.172  ? 210 PRO GGG N   1 
ATOM   14617 C CA  . PRO I 3 210 ? 85.937  69.339  54.888  1.000 54.625  ? 210 PRO GGG CA  1 
ATOM   14618 C C   . PRO I 3 210 ? 85.292  68.045  55.405  1.000 50.462  ? 210 PRO GGG C   1 
ATOM   14619 O O   . PRO I 3 210 ? 85.911  67.338  56.144  1.000 47.651  ? 210 PRO GGG O   1 
ATOM   14620 C CB  . PRO I 3 210 ? 87.218  69.004  54.111  1.000 52.568  ? 210 PRO GGG CB  1 
ATOM   14621 C CG  . PRO I 3 210 ? 88.045  70.250  54.259  1.000 54.210  ? 210 PRO GGG CG  1 
ATOM   14622 C CD  . PRO I 3 210 ? 87.773  70.725  55.673  1.000 55.031  ? 210 PRO GGG CD  1 
ATOM   14623 N N   . VAL I 3 211 ? 84.065  67.768  54.962  1.000 51.428  ? 211 VAL GGG N   1 
ATOM   14624 C CA  . VAL I 3 211 ? 83.284  66.540  55.298  1.000 51.425  ? 211 VAL GGG CA  1 
ATOM   14625 C C   . VAL I 3 211 ? 83.604  65.438  54.286  1.000 48.153  ? 211 VAL GGG C   1 
ATOM   14626 O O   . VAL I 3 211 ? 83.570  65.707  53.076  1.000 47.022  ? 211 VAL GGG O   1 
ATOM   14627 C CB  . VAL I 3 211 ? 81.769  66.823  55.313  1.000 52.893  ? 211 VAL GGG CB  1 
ATOM   14628 C CG1 . VAL I 3 211 ? 80.959  65.534  55.419  1.000 52.582  ? 211 VAL GGG CG1 1 
ATOM   14629 C CG2 . VAL I 3 211 ? 81.397  67.800  56.424  1.000 55.150  ? 211 VAL GGG CG2 1 
ATOM   14630 N N   . THR I 3 212 ? 83.837  64.228  54.788  1.000 47.636  ? 212 THR GGG N   1 
ATOM   14631 C CA  . THR I 3 212 ? 84.100  62.999  53.998  1.000 48.301  ? 212 THR GGG CA  1 
ATOM   14632 C C   . THR I 3 212 ? 83.004  61.979  54.303  1.000 46.000  ? 212 THR GGG C   1 
ATOM   14633 O O   . THR I 3 212 ? 82.740  61.741  55.485  1.000 48.844  ? 212 THR GGG O   1 
ATOM   14634 C CB  . THR I 3 212 ? 85.478  62.400  54.324  1.000 53.641  ? 212 THR GGG CB  1 
ATOM   14635 O OG1 . THR I 3 212 ? 86.468  63.425  54.192  1.000 57.086  ? 212 THR GGG OG1 1 
ATOM   14636 C CG2 . THR I 3 212 ? 85.845  61.231  53.432  1.000 57.743  ? 212 THR GGG CG2 1 
ATOM   14637 N N   . LYS I 3 213 ? 82.378  61.422  53.273  1.000 43.891  ? 213 LYS GGG N   1 
ATOM   14638 C CA  . LYS I 3 213 ? 81.547  60.204  53.388  1.000 42.146  ? 213 LYS GGG CA  1 
ATOM   14639 C C   . LYS I 3 213 ? 82.227  59.153  52.536  1.000 39.042  ? 213 LYS GGG C   1 
ATOM   14640 O O   . LYS I 3 213 ? 82.675  59.498  51.447  1.000 36.967  ? 213 LYS GGG O   1 
ATOM   14641 C CB  . LYS I 3 213 ? 80.123  60.449  52.899  1.000 45.448  ? 213 LYS GGG CB  1 
ATOM   14642 C CG  . LYS I 3 213 ? 79.488  61.723  53.423  1.000 50.252  ? 213 LYS GGG CG  1 
ATOM   14643 C CD  . LYS I 3 213 ? 79.209  61.735  54.908  1.000 51.555  ? 213 LYS GGG CD  1 
ATOM   14644 C CE  . LYS I 3 213 ? 77.930  60.987  55.238  1.000 55.992  ? 213 LYS GGG CE  1 
ATOM   14645 N NZ  . LYS I 3 213 ? 77.354  61.419  56.533  1.000 56.178  ? 213 LYS GGG NZ  1 
ATOM   14646 N N   . SER I 3 214 ? 82.320  57.933  53.033  1.000 39.830  ? 214 SER GGG N   1 
ATOM   14647 C CA  . SER I 3 214 ? 83.039  56.847  52.332  1.000 43.475  ? 214 SER GGG CA  1 
ATOM   14648 C C   . SER I 3 214 ? 82.346  55.515  52.585  1.000 38.991  ? 214 SER GGG C   1 
ATOM   14649 O O   . SER I 3 214 ? 81.422  55.481  53.376  1.000 42.907  ? 214 SER GGG O   1 
ATOM   14650 C CB  . SER I 3 214 ? 84.478  56.815  52.762  1.000 49.984  ? 214 SER GGG CB  1 
ATOM   14651 O OG  . SER I 3 214 ? 84.610  56.186  54.029  1.000 54.452  ? 214 SER GGG OG  1 
ATOM   14652 N N   . PHE I 3 215 ? 82.801  54.468  51.924  1.000 38.338  ? 215 PHE GGG N   1 
ATOM   14653 C CA  . PHE I 3 215 ? 82.328  53.085  52.144  1.000 44.617  ? 215 PHE GGG CA  1 
ATOM   14654 C C   . PHE I 3 215 ? 83.439  52.113  51.753  1.000 50.557  ? 215 PHE GGG C   1 
ATOM   14655 O O   . PHE I 3 215 ? 84.282  52.464  50.906  1.000 63.397  ? 215 PHE GGG O   1 
ATOM   14656 C CB  . PHE I 3 215 ? 81.061  52.812  51.336  1.000 43.856  ? 215 PHE GGG CB  1 
ATOM   14657 C CG  . PHE I 3 215 ? 81.298  52.765  49.854  1.000 41.748  ? 215 PHE GGG CG  1 
ATOM   14658 C CD1 . PHE I 3 215 ? 81.241  53.923  49.106  1.000 43.063  ? 215 PHE GGG CD1 1 
ATOM   14659 C CD2 . PHE I 3 215 ? 81.625  51.580  49.226  1.000 40.630  ? 215 PHE GGG CD2 1 
ATOM   14660 C CE1 . PHE I 3 215 ? 81.470  53.889  47.744  1.000 43.783  ? 215 PHE GGG CE1 1 
ATOM   14661 C CE2 . PHE I 3 215 ? 81.861  51.545  47.863  1.000 41.736  ? 215 PHE GGG CE2 1 
ATOM   14662 C CZ  . PHE I 3 215 ? 81.779  52.699  47.124  1.000 43.227  ? 215 PHE GGG CZ  1 
ATOM   14663 N N   . ASN I 3 216 ? 83.415  50.930  52.364  1.000 48.733  ? 216 ASN GGG N   1 
ATOM   14664 C CA  . ASN I 3 216 ? 84.390  49.838  52.149  1.000 49.271  ? 216 ASN GGG CA  1 
ATOM   14665 C C   . ASN I 3 216 ? 83.737  48.854  51.180  1.000 45.766  ? 216 ASN GGG C   1 
ATOM   14666 O O   . ASN I 3 216 ? 82.608  48.482  51.438  1.000 42.204  ? 216 ASN GGG O   1 
ATOM   14667 C CB  . ASN I 3 216 ? 84.805  49.227  53.494  1.000 50.755  ? 216 ASN GGG CB  1 
ATOM   14668 C CG  . ASN I 3 216 ? 85.615  50.183  54.351  1.000 51.544  ? 216 ASN GGG CG  1 
ATOM   14669 O OD1 . ASN I 3 216 ? 85.553  51.398  54.187  1.000 53.714  ? 216 ASN GGG OD1 1 
ATOM   14670 N ND2 . ASN I 3 216 ? 86.407  49.649  55.260  1.000 62.432  ? 216 ASN GGG ND2 1 
ATOM   14671 N N   . ARG I 3 217 ? 84.402  48.495  50.084  1.000 46.190  ? 217 ARG GGG N   1 
ATOM   14672 C CA  . ARG I 3 217 ? 83.806  47.652  49.020  1.000 52.140  ? 217 ARG GGG CA  1 
ATOM   14673 C C   . ARG I 3 217 ? 83.277  46.353  49.633  1.000 53.905  ? 217 ARG GGG C   1 
ATOM   14674 O O   . ARG I 3 217 ? 84.045  45.700  50.353  1.000 52.355  ? 217 ARG GGG O   1 
ATOM   14675 C CB  . ARG I 3 217 ? 84.828  47.360  47.926  1.000 57.839  ? 217 ARG GGG CB  1 
ATOM   14676 C CG  . ARG I 3 217 ? 84.260  46.547  46.772  1.000 65.586  ? 217 ARG GGG CG  1 
ATOM   14677 C CD  . ARG I 3 217 ? 85.253  46.512  45.636  1.000 72.939  ? 217 ARG GGG CD  1 
ATOM   14678 N NE  . ARG I 3 217 ? 86.564  46.160  46.156  1.000 74.668  ? 217 ARG GGG NE  1 
ATOM   14679 C CZ  . ARG I 3 217 ? 86.941  44.931  46.478  1.000 72.915  ? 217 ARG GGG CZ  1 
ATOM   14680 N NH1 . ARG I 3 217 ? 86.114  43.910  46.311  1.000 70.528  ? 217 ARG GGG NH1 1 
ATOM   14681 N NH2 . ARG I 3 217 ? 88.157  44.735  46.957  1.000 74.975  ? 217 ARG GGG NH2 1 
ATOM   14682 N N   . GLY I 3 218 ? 82.003  46.030  49.365  1.000 61.120  ? 218 GLY GGG N   1 
ATOM   14683 C CA  . GLY I 3 218 ? 81.291  44.825  49.839  1.000 64.795  ? 218 GLY GGG CA  1 
ATOM   14684 C C   . GLY I 3 218 ? 80.908  44.884  51.314  1.000 66.982  ? 218 GLY GGG C   1 
ATOM   14685 O O   . GLY I 3 218 ? 81.457  44.067  52.065  1.000 65.090  ? 218 GLY GGG O   1 
ATOM   14686 N N   . GLU I 3 219 ? 80.010  45.804  51.707  1.000 68.841  ? 219 GLU GGG N   1 
ATOM   14687 C CA  . GLU I 3 219 ? 79.481  46.009  53.086  1.000 68.772  ? 219 GLU GGG CA  1 
ATOM   14688 C C   . GLU I 3 219 ? 78.270  46.948  53.000  1.000 68.960  ? 219 GLU GGG C   1 
ATOM   14689 O O   . GLU I 3 219 ? 77.858  47.618  53.953  1.000 70.566  ? 219 GLU GGG O   1 
ATOM   14690 C CB  . GLU I 3 219 ? 80.532  46.615  54.023  1.000 73.841  ? 219 GLU GGG CB  1 
ATOM   14691 C CG  . GLU I 3 219 ? 81.826  45.816  54.135  1.000 81.926  ? 219 GLU GGG CG  1 
ATOM   14692 C CD  . GLU I 3 219 ? 82.923  46.425  55.001  1.000 94.838  ? 219 GLU GGG CD  1 
ATOM   14693 O OE1 . GLU I 3 219 ? 82.646  47.402  55.735  1.000 108.131 ? 219 GLU GGG OE1 1 
ATOM   14694 O OE2 . GLU I 3 219 ? 84.073  45.940  54.922  1.000 95.757  ? 219 GLU GGG OE2 1 
HETATM 14695 C C1  . NAG J 4 .   ? 6.092   38.957  24.324  1.000 128.544 ? 601 NAG EEE C1  1 
HETATM 14696 C C2  . NAG J 4 .   ? 7.545   38.635  24.068  1.000 138.497 ? 601 NAG EEE C2  1 
HETATM 14697 C C3  . NAG J 4 .   ? 8.033   38.066  25.394  1.000 129.458 ? 601 NAG EEE C3  1 
HETATM 14698 C C4  . NAG J 4 .   ? 7.609   38.972  26.575  1.000 118.836 ? 601 NAG EEE C4  1 
HETATM 14699 C C5  . NAG J 4 .   ? 6.173   39.567  26.489  1.000 108.167 ? 601 NAG EEE C5  1 
HETATM 14700 C C6  . NAG J 4 .   ? 5.990   40.818  27.316  1.000 97.207  ? 601 NAG EEE C6  1 
HETATM 14701 C C7  . NAG J 4 .   ? 8.720   37.704  22.090  1.000 145.851 ? 601 NAG EEE C7  1 
HETATM 14702 C C8  . NAG J 4 .   ? 9.813   38.737  22.211  1.000 129.886 ? 601 NAG EEE C8  1 
HETATM 14703 N N2  . NAG J 4 .   ? 7.719   37.680  22.982  1.000 155.109 ? 601 NAG EEE N2  1 
HETATM 14704 O O3  . NAG J 4 .   ? 9.461   37.914  25.366  1.000 129.781 ? 601 NAG EEE O3  1 
HETATM 14705 O O4  . NAG J 4 .   ? 7.781   38.251  27.816  1.000 107.489 ? 601 NAG EEE O4  1 
HETATM 14706 O O5  . NAG J 4 .   ? 5.849   40.027  25.203  1.000 112.557 ? 601 NAG EEE O5  1 
HETATM 14707 O O6  . NAG J 4 .   ? 4.644   40.888  27.772  1.000 77.912  ? 601 NAG EEE O6  1 
HETATM 14708 O O7  . NAG J 4 .   ? 8.768   36.898  21.161  1.000 143.587 ? 601 NAG EEE O7  1 
HETATM 14709 C C1  . NAG K 4 .   ? 8.296   66.375  103.673 1.000 124.881 ? 601 NAG AAA C1  1 
HETATM 14710 C C2  . NAG K 4 .   ? 9.667   66.916  104.031 1.000 122.558 ? 601 NAG AAA C2  1 
HETATM 14711 C C3  . NAG K 4 .   ? 10.502  67.052  102.745 1.000 124.373 ? 601 NAG AAA C3  1 
HETATM 14712 C C4  . NAG K 4 .   ? 10.505  65.744  101.924 1.000 121.784 ? 601 NAG AAA C4  1 
HETATM 14713 C C5  . NAG K 4 .   ? 9.062   65.167  101.776 1.000 115.069 ? 601 NAG AAA C5  1 
HETATM 14714 C C6  . NAG K 4 .   ? 8.962   63.787  101.118 1.000 98.961  ? 601 NAG AAA C6  1 
HETATM 14715 C C7  . NAG K 4 .   ? 10.278  68.641  105.699 1.000 96.821  ? 601 NAG AAA C7  1 
HETATM 14716 C C8  . NAG K 4 .   ? 11.375  67.754  106.236 1.000 88.833  ? 601 NAG AAA C8  1 
HETATM 14717 N N2  . NAG K 4 .   ? 9.517   68.206  104.691 1.000 110.126 ? 601 NAG AAA N2  1 
HETATM 14718 O O3  . NAG K 4 .   ? 11.845  67.475  103.024 1.000 117.427 ? 601 NAG AAA O3  1 
HETATM 14719 O O4  . NAG K 4 .   ? 11.156  66.036  100.667 1.000 110.789 ? 601 NAG AAA O4  1 
HETATM 14720 O O5  . NAG K 4 .   ? 8.431   65.080  103.057 1.000 120.554 ? 601 NAG AAA O5  1 
HETATM 14721 O O6  . NAG K 4 .   ? 7.578   63.456  100.874 1.000 80.141  ? 601 NAG AAA O6  1 
HETATM 14722 O O7  . NAG K 4 .   ? 10.053  69.743  106.168 1.000 83.569  ? 601 NAG AAA O7  1 
HETATM 14723 C C1  . NAG L 4 .   ? 38.961  100.167 0.963   1.000 108.573 ? 601 NAG DDD C1  1 
HETATM 14724 C C2  . NAG L 4 .   ? 38.335  98.792  0.752   1.000 110.519 ? 601 NAG DDD C2  1 
HETATM 14725 C C3  . NAG L 4 .   ? 38.200  98.143  2.130   1.000 112.105 ? 601 NAG DDD C3  1 
HETATM 14726 C C4  . NAG L 4 .   ? 39.474  98.239  2.970   1.000 112.501 ? 601 NAG DDD C4  1 
HETATM 14727 C C5  . NAG L 4 .   ? 40.080  99.641  3.046   1.000 109.019 ? 601 NAG DDD C5  1 
HETATM 14728 C C6  . NAG L 4 .   ? 41.539  99.615  3.493   1.000 101.893 ? 601 NAG DDD C6  1 
HETATM 14729 C C7  . NAG L 4 .   ? 36.372  98.026  -0.589  1.000 97.797  ? 601 NAG DDD C7  1 
HETATM 14730 C C8  . NAG L 4 .   ? 37.286  97.002  -1.223  1.000 90.375  ? 601 NAG DDD C8  1 
HETATM 14731 N N2  . NAG L 4 .   ? 36.960  98.880  0.259   1.000 110.501 ? 601 NAG DDD N2  1 
HETATM 14732 O O3  . NAG L 4 .   ? 37.789  96.766  2.041   1.000 107.123 ? 601 NAG DDD O3  1 
HETATM 14733 O O4  . NAG L 4 .   ? 39.136  97.787  4.297   1.000 106.651 ? 601 NAG DDD O4  1 
HETATM 14734 O O5  . NAG L 4 .   ? 40.111  100.243 1.782   1.000 111.967 ? 601 NAG DDD O5  1 
HETATM 14735 O O6  . NAG L 4 .   ? 42.081  100.944 3.638   1.000 86.330  ? 601 NAG DDD O6  1 
HETATM 14736 O O7  . NAG L 4 .   ? 35.149  98.084  -0.788  1.000 76.932  ? 601 NAG DDD O7  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   ARG 1   319 ?    ?   ?   EEE . n 
A 1 2   VAL 2   320 ?    ?   ?   EEE . n 
A 1 3   GLN 3   321 ?    ?   ?   EEE . n 
A 1 4   PRO 4   322 ?    ?   ?   EEE . n 
A 1 5   THR 5   323 ?    ?   ?   EEE . n 
A 1 6   GLU 6   324 ?    ?   ?   EEE . n 
A 1 7   SER 7   325 ?    ?   ?   EEE . n 
A 1 8   ILE 8   326 ?    ?   ?   EEE . n 
A 1 9   VAL 9   327 ?    ?   ?   EEE . n 
A 1 10  ARG 10  328 ?    ?   ?   EEE . n 
A 1 11  PHE 11  329 ?    ?   ?   EEE . n 
A 1 12  PRO 12  330 ?    ?   ?   EEE . n 
A 1 13  ASN 13  331 ?    ?   ?   EEE . n 
A 1 14  ILE 14  332 ?    ?   ?   EEE . n 
A 1 15  THR 15  333 333  THR THR EEE . n 
A 1 16  ASN 16  334 334  ASN ASN EEE . n 
A 1 17  LEU 17  335 335  LEU LEU EEE . n 
A 1 18  CYS 18  336 336  CYS CYS EEE . n 
A 1 19  PRO 19  337 337  PRO PRO EEE . n 
A 1 20  PHE 20  338 338  PHE PHE EEE . n 
A 1 21  GLY 21  339 339  GLY GLY EEE . n 
A 1 22  GLU 22  340 340  GLU GLU EEE . n 
A 1 23  VAL 23  341 341  VAL VAL EEE . n 
A 1 24  PHE 24  342 342  PHE PHE EEE . n 
A 1 25  ASN 25  343 343  ASN ASN EEE . n 
A 1 26  ALA 26  344 344  ALA ALA EEE . n 
A 1 27  THR 27  345 345  THR THR EEE . n 
A 1 28  ARG 28  346 346  ARG ARG EEE . n 
A 1 29  PHE 29  347 347  PHE PHE EEE . n 
A 1 30  ALA 30  348 348  ALA ALA EEE . n 
A 1 31  SER 31  349 349  SER SER EEE . n 
A 1 32  VAL 32  350 350  VAL VAL EEE . n 
A 1 33  TYR 33  351 351  TYR TYR EEE . n 
A 1 34  ALA 34  352 352  ALA ALA EEE . n 
A 1 35  TRP 35  353 353  TRP TRP EEE . n 
A 1 36  ASN 36  354 354  ASN ASN EEE . n 
A 1 37  ARG 37  355 355  ARG ARG EEE . n 
A 1 38  LYS 38  356 356  LYS LYS EEE . n 
A 1 39  ARG 39  357 357  ARG ARG EEE . n 
A 1 40  ILE 40  358 358  ILE ILE EEE . n 
A 1 41  SER 41  359 359  SER SER EEE . n 
A 1 42  ASN 42  360 360  ASN ASN EEE . n 
A 1 43  CYS 43  361 361  CYS CYS EEE . n 
A 1 44  VAL 44  362 362  VAL VAL EEE . n 
A 1 45  ALA 45  363 363  ALA ALA EEE . n 
A 1 46  ASP 46  364 364  ASP ASP EEE . n 
A 1 47  TYR 47  365 365  TYR TYR EEE . n 
A 1 48  SER 48  366 366  SER SER EEE . n 
A 1 49  VAL 49  367 367  VAL VAL EEE . n 
A 1 50  LEU 50  368 368  LEU LEU EEE . n 
A 1 51  TYR 51  369 369  TYR TYR EEE . n 
A 1 52  ASN 52  370 370  ASN ASN EEE . n 
A 1 53  SER 53  371 371  SER SER EEE . n 
A 1 54  ALA 54  372 372  ALA ALA EEE . n 
A 1 55  SER 55  373 373  SER SER EEE . n 
A 1 56  PHE 56  374 374  PHE PHE EEE . n 
A 1 57  SER 57  375 375  SER SER EEE . n 
A 1 58  THR 58  376 376  THR THR EEE . n 
A 1 59  PHE 59  377 377  PHE PHE EEE . n 
A 1 60  LYS 60  378 378  LYS LYS EEE . n 
A 1 61  CYS 61  379 379  CYS CYS EEE . n 
A 1 62  TYR 62  380 380  TYR TYR EEE . n 
A 1 63  GLY 63  381 381  GLY GLY EEE . n 
A 1 64  VAL 64  382 382  VAL VAL EEE . n 
A 1 65  SER 65  383 383  SER SER EEE . n 
A 1 66  PRO 66  384 384  PRO PRO EEE . n 
A 1 67  THR 67  385 385  THR THR EEE . n 
A 1 68  LYS 68  386 386  LYS LYS EEE . n 
A 1 69  LEU 69  387 387  LEU LEU EEE . n 
A 1 70  ASN 70  388 388  ASN ASN EEE . n 
A 1 71  ASP 71  389 389  ASP ASP EEE . n 
A 1 72  LEU 72  390 390  LEU LEU EEE . n 
A 1 73  CYS 73  391 391  CYS CYS EEE . n 
A 1 74  PHE 74  392 392  PHE PHE EEE . n 
A 1 75  THR 75  393 393  THR THR EEE . n 
A 1 76  ASN 76  394 394  ASN ASN EEE . n 
A 1 77  VAL 77  395 395  VAL VAL EEE . n 
A 1 78  TYR 78  396 396  TYR TYR EEE . n 
A 1 79  ALA 79  397 397  ALA ALA EEE . n 
A 1 80  ASP 80  398 398  ASP ASP EEE . n 
A 1 81  SER 81  399 399  SER SER EEE . n 
A 1 82  PHE 82  400 400  PHE PHE EEE . n 
A 1 83  VAL 83  401 401  VAL VAL EEE . n 
A 1 84  ILE 84  402 402  ILE ILE EEE . n 
A 1 85  ARG 85  403 403  ARG ARG EEE . n 
A 1 86  GLY 86  404 404  GLY GLY EEE . n 
A 1 87  ASP 87  405 405  ASP ASP EEE . n 
A 1 88  GLU 88  406 406  GLU GLU EEE . n 
A 1 89  VAL 89  407 407  VAL VAL EEE . n 
A 1 90  ARG 90  408 408  ARG ARG EEE . n 
A 1 91  GLN 91  409 409  GLN GLN EEE . n 
A 1 92  ILE 92  410 410  ILE ILE EEE . n 
A 1 93  ALA 93  411 411  ALA ALA EEE . n 
A 1 94  PRO 94  412 412  PRO PRO EEE . n 
A 1 95  GLY 95  413 413  GLY GLY EEE . n 
A 1 96  GLN 96  414 414  GLN GLN EEE . n 
A 1 97  THR 97  415 415  THR THR EEE . n 
A 1 98  GLY 98  416 416  GLY GLY EEE . n 
A 1 99  LYS 99  417 417  LYS LYS EEE . n 
A 1 100 ILE 100 418 418  ILE ILE EEE . n 
A 1 101 ALA 101 419 419  ALA ALA EEE . n 
A 1 102 ASP 102 420 420  ASP ASP EEE . n 
A 1 103 TYR 103 421 421  TYR TYR EEE . n 
A 1 104 ASN 104 422 422  ASN ASN EEE . n 
A 1 105 TYR 105 423 423  TYR TYR EEE . n 
A 1 106 LYS 106 424 424  LYS LYS EEE . n 
A 1 107 LEU 107 425 425  LEU LEU EEE . n 
A 1 108 PRO 108 426 426  PRO PRO EEE . n 
A 1 109 ASP 109 427 427  ASP ASP EEE . n 
A 1 110 ASP 110 428 428  ASP ASP EEE . n 
A 1 111 PHE 111 429 429  PHE PHE EEE . n 
A 1 112 THR 112 430 430  THR THR EEE . n 
A 1 113 GLY 113 431 431  GLY GLY EEE . n 
A 1 114 CYS 114 432 432  CYS CYS EEE . n 
A 1 115 VAL 115 433 433  VAL VAL EEE . n 
A 1 116 ILE 116 434 434  ILE ILE EEE . n 
A 1 117 ALA 117 435 435  ALA ALA EEE . n 
A 1 118 TRP 118 436 436  TRP TRP EEE . n 
A 1 119 ASN 119 437 437  ASN ASN EEE . n 
A 1 120 SER 120 438 438  SER SER EEE . n 
A 1 121 ASN 121 439 439  ASN ASN EEE . n 
A 1 122 ASN 122 440 440  ASN ASN EEE . n 
A 1 123 LEU 123 441 441  LEU LEU EEE . n 
A 1 124 ASP 124 442 442  ASP ASP EEE . n 
A 1 125 SER 125 443 443  SER SER EEE . n 
A 1 126 LYS 126 444 444  LYS LYS EEE . n 
A 1 127 VAL 127 445 445  VAL VAL EEE . n 
A 1 128 GLY 128 446 446  GLY GLY EEE . n 
A 1 129 GLY 129 447 447  GLY GLY EEE . n 
A 1 130 ASN 130 448 448  ASN ASN EEE . n 
A 1 131 TYR 131 449 449  TYR TYR EEE . n 
A 1 132 ASN 132 450 450  ASN ASN EEE . n 
A 1 133 TYR 133 451 451  TYR TYR EEE . n 
A 1 134 LEU 134 452 452  LEU LEU EEE . n 
A 1 135 TYR 135 453 453  TYR TYR EEE . n 
A 1 136 ARG 136 454 454  ARG ARG EEE . n 
A 1 137 LEU 137 455 455  LEU LEU EEE . n 
A 1 138 PHE 138 456 456  PHE PHE EEE . n 
A 1 139 ARG 139 457 457  ARG ARG EEE . n 
A 1 140 LYS 140 458 458  LYS LYS EEE . n 
A 1 141 SER 141 459 459  SER SER EEE . n 
A 1 142 ASN 142 460 460  ASN ASN EEE . n 
A 1 143 LEU 143 461 461  LEU LEU EEE . n 
A 1 144 LYS 144 462 462  LYS LYS EEE . n 
A 1 145 PRO 145 463 463  PRO PRO EEE . n 
A 1 146 PHE 146 464 464  PHE PHE EEE . n 
A 1 147 GLU 147 465 465  GLU GLU EEE . n 
A 1 148 ARG 148 466 466  ARG ARG EEE . n 
A 1 149 ASP 149 467 467  ASP ASP EEE . n 
A 1 150 ILE 150 468 468  ILE ILE EEE . n 
A 1 151 SER 151 469 469  SER SER EEE . n 
A 1 152 THR 152 470 470  THR THR EEE . n 
A 1 153 GLU 153 471 471  GLU GLU EEE . n 
A 1 154 ILE 154 472 472  ILE ILE EEE . n 
A 1 155 TYR 155 473 473  TYR TYR EEE . n 
A 1 156 GLN 156 474 474  GLN GLN EEE . n 
A 1 157 ALA 157 475 475  ALA ALA EEE . n 
A 1 158 GLY 158 476 476  GLY GLY EEE . n 
A 1 159 SER 159 477 477  SER SER EEE . n 
A 1 160 THR 160 478 478  THR THR EEE . n 
A 1 161 PRO 161 479 479  PRO PRO EEE . n 
A 1 162 CYS 162 480 480  CYS CYS EEE . n 
A 1 163 ASN 163 481 481  ASN ASN EEE . n 
A 1 164 GLY 164 482 482  GLY GLY EEE . n 
A 1 165 VAL 165 483 483  VAL VAL EEE . n 
A 1 166 GLU 166 484 484  GLU GLU EEE . n 
A 1 167 GLY 167 485 485  GLY GLY EEE . n 
A 1 168 PHE 168 486 486  PHE PHE EEE . n 
A 1 169 ASN 169 487 487  ASN ASN EEE . n 
A 1 170 CYS 170 488 488  CYS CYS EEE . n 
A 1 171 TYR 171 489 489  TYR TYR EEE . n 
A 1 172 PHE 172 490 490  PHE PHE EEE . n 
A 1 173 PRO 173 491 491  PRO PRO EEE . n 
A 1 174 LEU 174 492 492  LEU LEU EEE . n 
A 1 175 GLN 175 493 493  GLN GLN EEE . n 
A 1 176 SER 176 494 494  SER SER EEE . n 
A 1 177 TYR 177 495 495  TYR TYR EEE . n 
A 1 178 GLY 178 496 496  GLY GLY EEE . n 
A 1 179 PHE 179 497 497  PHE PHE EEE . n 
A 1 180 GLN 180 498 498  GLN GLN EEE . n 
A 1 181 PRO 181 499 499  PRO PRO EEE . n 
A 1 182 THR 182 500 500  THR THR EEE . n 
A 1 183 ASN 183 501 501  ASN ASN EEE . n 
A 1 184 GLY 184 502 502  GLY GLY EEE . n 
A 1 185 VAL 185 503 503  VAL VAL EEE . n 
A 1 186 GLY 186 504 504  GLY GLY EEE . n 
A 1 187 TYR 187 505 505  TYR TYR EEE . n 
A 1 188 GLN 188 506 506  GLN GLN EEE . n 
A 1 189 PRO 189 507 507  PRO PRO EEE . n 
A 1 190 TYR 190 508 508  TYR TYR EEE . n 
A 1 191 ARG 191 509 509  ARG ARG EEE . n 
A 1 192 VAL 192 510 510  VAL VAL EEE . n 
A 1 193 VAL 193 511 511  VAL VAL EEE . n 
A 1 194 VAL 194 512 512  VAL VAL EEE . n 
A 1 195 LEU 195 513 513  LEU LEU EEE . n 
A 1 196 SER 196 514 514  SER SER EEE . n 
A 1 197 PHE 197 515 515  PHE PHE EEE . n 
A 1 198 GLU 198 516 516  GLU GLU EEE . n 
A 1 199 LEU 199 517 517  LEU LEU EEE . n 
A 1 200 LEU 200 518 518  LEU LEU EEE . n 
A 1 201 HIS 201 519 519  HIS HIS EEE . n 
A 1 202 ALA 202 520 520  ALA ALA EEE . n 
A 1 203 PRO 203 521 521  PRO PRO EEE . n 
A 1 204 ALA 204 522 522  ALA ALA EEE . n 
A 1 205 THR 205 523 523  THR THR EEE . n 
A 1 206 VAL 206 524 524  VAL VAL EEE . n 
A 1 207 CYS 207 525 525  CYS CYS EEE . n 
A 1 208 GLY 208 526 526  GLY GLY EEE . n 
A 1 209 PRO 209 527 527  PRO PRO EEE . n 
A 1 210 LYS 210 528 528  LYS LYS EEE . n 
A 1 211 LYS 211 529 ?    ?   ?   EEE . n 
A 1 212 SER 212 530 ?    ?   ?   EEE . n 
A 1 213 THR 213 531 ?    ?   ?   EEE . n 
A 1 214 ASN 214 532 ?    ?   ?   EEE . n 
A 1 215 LEU 215 533 ?    ?   ?   EEE . n 
A 1 216 VAL 216 534 ?    ?   ?   EEE . n 
A 1 217 LYS 217 535 ?    ?   ?   EEE . n 
A 1 218 ASN 218 536 ?    ?   ?   EEE . n 
A 1 219 LYS 219 537 ?    ?   ?   EEE . n 
A 1 220 CYS 220 538 ?    ?   ?   EEE . n 
A 1 221 VAL 221 539 ?    ?   ?   EEE . n 
A 1 222 ASN 222 540 ?    ?   ?   EEE . n 
A 1 223 PHE 223 541 ?    ?   ?   EEE . n 
A 1 224 SER 224 542 ?    ?   ?   EEE . n 
A 1 225 GLY 225 543 ?    ?   ?   EEE . n 
A 1 226 HIS 226 544 ?    ?   ?   EEE . n 
A 1 227 HIS 227 545 ?    ?   ?   EEE . n 
A 1 228 HIS 228 546 ?    ?   ?   EEE . n 
A 1 229 HIS 229 547 ?    ?   ?   EEE . n 
A 1 230 HIS 230 548 ?    ?   ?   EEE . n 
A 1 231 HIS 231 549 ?    ?   ?   EEE . n 
B 2 1   GLN 1   1   1    GLN GLN HHH . n 
B 2 2   MET 2   2   2    MET MET HHH . n 
B 2 3   GLN 3   3   3    GLN GLN HHH . n 
B 2 4   LEU 4   4   4    LEU LEU HHH . n 
B 2 5   VAL 5   5   5    VAL VAL HHH . n 
B 2 6   GLN 6   6   6    GLN GLN HHH . n 
B 2 7   SER 7   7   7    SER SER HHH . n 
B 2 8   GLY 8   8   8    GLY GLY HHH . n 
B 2 9   THR 9   9   9    THR THR HHH . n 
B 2 10  GLU 10  10  10   GLU GLU HHH . n 
B 2 11  VAL 11  11  11   VAL VAL HHH . n 
B 2 12  LYS 12  12  12   LYS LYS HHH . n 
B 2 13  LYS 13  13  13   LYS LYS HHH . n 
B 2 14  PRO 14  14  14   PRO PRO HHH . n 
B 2 15  GLY 15  15  15   GLY GLY HHH . n 
B 2 16  GLU 16  16  16   GLU GLU HHH . n 
B 2 17  SER 17  17  17   SER SER HHH . n 
B 2 18  LEU 18  18  18   LEU LEU HHH . n 
B 2 19  LYS 19  19  19   LYS LYS HHH . n 
B 2 20  ILE 20  20  20   ILE ILE HHH . n 
B 2 21  SER 21  21  21   SER SER HHH . n 
B 2 22  CYS 22  22  22   CYS CYS HHH . n 
B 2 23  LYS 23  23  23   LYS LYS HHH . n 
B 2 24  GLY 24  24  24   GLY GLY HHH . n 
B 2 25  SER 25  25  25   SER SER HHH . n 
B 2 26  GLY 26  26  26   GLY GLY HHH . n 
B 2 27  TYR 27  27  27   TYR TYR HHH . n 
B 2 28  GLY 28  28  28   GLY GLY HHH . n 
B 2 29  PHE 29  29  29   PHE PHE HHH . n 
B 2 30  ILE 30  30  30   ILE ILE HHH . n 
B 2 31  THR 31  31  31   THR THR HHH . n 
B 2 32  TYR 32  32  32   TYR TYR HHH . n 
B 2 33  TRP 33  33  33   TRP TRP HHH . n 
B 2 34  ILE 34  34  34   ILE ILE HHH . n 
B 2 35  GLY 35  35  35   GLY GLY HHH . n 
B 2 36  TRP 36  36  36   TRP TRP HHH . n 
B 2 37  VAL 37  37  37   VAL VAL HHH . n 
B 2 38  ARG 38  38  38   ARG ARG HHH . n 
B 2 39  GLN 39  39  39   GLN GLN HHH . n 
B 2 40  MET 40  40  40   MET MET HHH . n 
B 2 41  PRO 41  41  41   PRO PRO HHH . n 
B 2 42  GLY 42  42  42   GLY GLY HHH . n 
B 2 43  LYS 43  43  43   LYS LYS HHH . n 
B 2 44  GLY 44  44  44   GLY GLY HHH . n 
B 2 45  LEU 45  45  45   LEU LEU HHH . n 
B 2 46  GLU 46  46  46   GLU GLU HHH . n 
B 2 47  TRP 47  47  47   TRP TRP HHH . n 
B 2 48  MET 48  48  48   MET MET HHH . n 
B 2 49  GLY 49  49  49   GLY GLY HHH . n 
B 2 50  ILE 50  50  50   ILE ILE HHH . n 
B 2 51  ILE 51  51  51   ILE ILE HHH . n 
B 2 52  TYR 52  52  52   TYR TYR HHH . n 
B 2 53  PRO 53  53  52A  PRO PRO HHH . n 
B 2 54  GLY 54  54  53   GLY GLY HHH . n 
B 2 55  ASP 55  55  54   ASP ASP HHH . n 
B 2 56  SER 56  56  55   SER SER HHH . n 
B 2 57  GLU 57  57  56   GLU GLU HHH . n 
B 2 58  THR 58  58  57   THR THR HHH . n 
B 2 59  ARG 59  59  58   ARG ARG HHH . n 
B 2 60  TYR 60  60  59   TYR TYR HHH . n 
B 2 61  SER 61  61  60   SER SER HHH . n 
B 2 62  PRO 62  62  61   PRO PRO HHH . n 
B 2 63  SER 63  63  62   SER SER HHH . n 
B 2 64  PHE 64  64  63   PHE PHE HHH . n 
B 2 65  GLN 65  65  64   GLN GLN HHH . n 
B 2 66  GLY 66  66  65   GLY GLY HHH . n 
B 2 67  GLN 67  67  66   GLN GLN HHH . n 
B 2 68  VAL 68  68  67   VAL VAL HHH . n 
B 2 69  THR 69  69  68   THR THR HHH . n 
B 2 70  ILE 70  70  69   ILE ILE HHH . n 
B 2 71  SER 71  71  70   SER SER HHH . n 
B 2 72  ALA 72  72  71   ALA ALA HHH . n 
B 2 73  ASP 73  73  72   ASP ASP HHH . n 
B 2 74  LYS 74  74  73   LYS LYS HHH . n 
B 2 75  SER 75  75  74   SER SER HHH . n 
B 2 76  ILE 76  76  75   ILE ILE HHH . n 
B 2 77  ASN 77  77  76   ASN ASN HHH . n 
B 2 78  THR 78  78  77   THR THR HHH . n 
B 2 79  ALA 79  79  78   ALA ALA HHH . n 
B 2 80  TYR 80  80  79   TYR TYR HHH . n 
B 2 81  LEU 81  81  80   LEU LEU HHH . n 
B 2 82  GLN 82  82  81   GLN GLN HHH . n 
B 2 83  TRP 83  83  82   TRP TRP HHH . n 
B 2 84  SER 84  84  82A  SER SER HHH . n 
B 2 85  SER 85  85  82B  SER SER HHH . n 
B 2 86  LEU 86  86  82C  LEU LEU HHH . n 
B 2 87  LYS 87  87  83   LYS LYS HHH . n 
B 2 88  ALA 88  88  84   ALA ALA HHH . n 
B 2 89  SER 89  89  85   SER SER HHH . n 
B 2 90  ASP 90  90  86   ASP ASP HHH . n 
B 2 91  THR 91  91  87   THR THR HHH . n 
B 2 92  ALA 92  92  88   ALA ALA HHH . n 
B 2 93  ILE 93  93  89   ILE ILE HHH . n 
B 2 94  TYR 94  94  90   TYR TYR HHH . n 
B 2 95  TYR 95  95  91   TYR TYR HHH . n 
B 2 96  CYS 96  96  92   CYS CYS HHH . n 
B 2 97  ALA 97  97  93   ALA ALA HHH . n 
B 2 98  GLY 98  98  94   GLY GLY HHH . n 
B 2 99  GLY 99  99  95   GLY GLY HHH . n 
B 2 100 SER 100 100 96   SER SER HHH . n 
B 2 101 GLY 101 101 97   GLY GLY HHH . n 
B 2 102 ILE 102 102 98   ILE ILE HHH . n 
B 2 103 SER 103 103 99   SER SER HHH . n 
B 2 104 THR 104 104 100  THR THR HHH . n 
B 2 105 PRO 105 105 100A PRO PRO HHH . n 
B 2 106 MET 106 106 100B MET MET HHH . n 
B 2 107 ASP 107 107 101  ASP ASP HHH . n 
B 2 108 VAL 108 108 102  VAL VAL HHH . n 
B 2 109 TRP 109 109 103  TRP TRP HHH . n 
B 2 110 GLY 110 110 104  GLY GLY HHH . n 
B 2 111 GLN 111 111 105  GLN GLN HHH . n 
B 2 112 GLY 112 112 106  GLY GLY HHH . n 
B 2 113 THR 113 113 107  THR THR HHH . n 
B 2 114 THR 114 114 108  THR THR HHH . n 
B 2 115 VAL 115 115 109  VAL VAL HHH . n 
B 2 116 THR 116 116 110  THR THR HHH . n 
B 2 117 VAL 117 117 111  VAL VAL HHH . n 
B 2 118 SER 118 118 112  SER SER HHH . n 
B 2 119 SER 119 119 113  SER SER HHH . n 
B 2 120 ALA 120 120 114  ALA ALA HHH . n 
B 2 121 SER 121 121 115  SER SER HHH . n 
B 2 122 THR 122 122 116  THR THR HHH . n 
B 2 123 LYS 123 123 117  LYS LYS HHH . n 
B 2 124 GLY 124 124 118  GLY GLY HHH . n 
B 2 125 PRO 125 125 119  PRO PRO HHH . n 
B 2 126 SER 126 126 120  SER SER HHH . n 
B 2 127 VAL 127 127 121  VAL VAL HHH . n 
B 2 128 PHE 128 128 122  PHE PHE HHH . n 
B 2 129 PRO 129 129 123  PRO PRO HHH . n 
B 2 130 LEU 130 130 124  LEU LEU HHH . n 
B 2 131 ALA 131 131 125  ALA ALA HHH . n 
B 2 132 PRO 132 132 126  PRO PRO HHH . n 
B 2 133 SER 133 133 127  SER SER HHH . n 
B 2 134 SER 134 134 128  SER SER HHH . n 
B 2 135 LYS 135 135 129  LYS LYS HHH . n 
B 2 136 SER 136 136 130  SER SER HHH . n 
B 2 137 THR 137 137 131  THR THR HHH . n 
B 2 138 SER 138 138 132  SER SER HHH . n 
B 2 139 GLY 139 139 133  GLY GLY HHH . n 
B 2 140 GLY 140 140 134  GLY GLY HHH . n 
B 2 141 THR 141 141 135  THR THR HHH . n 
B 2 142 ALA 142 142 136  ALA ALA HHH . n 
B 2 143 ALA 143 143 137  ALA ALA HHH . n 
B 2 144 LEU 144 144 138  LEU LEU HHH . n 
B 2 145 GLY 145 145 139  GLY GLY HHH . n 
B 2 146 CYS 146 146 140  CYS CYS HHH . n 
B 2 147 LEU 147 147 141  LEU LEU HHH . n 
B 2 148 VAL 148 148 142  VAL VAL HHH . n 
B 2 149 LYS 149 149 143  LYS LYS HHH . n 
B 2 150 ASP 150 150 144  ASP ASP HHH . n 
B 2 151 TYR 151 151 145  TYR TYR HHH . n 
B 2 152 PHE 152 152 146  PHE PHE HHH . n 
B 2 153 PRO 153 153 147  PRO PRO HHH . n 
B 2 154 GLU 154 154 148  GLU GLU HHH . n 
B 2 155 PRO 155 155 149  PRO PRO HHH . n 
B 2 156 VAL 156 156 150  VAL VAL HHH . n 
B 2 157 THR 157 157 151  THR THR HHH . n 
B 2 158 VAL 158 158 152  VAL VAL HHH . n 
B 2 159 SER 159 159 153  SER SER HHH . n 
B 2 160 TRP 160 160 154  TRP TRP HHH . n 
B 2 161 ASN 161 161 155  ASN ASN HHH . n 
B 2 162 SER 162 162 156  SER SER HHH . n 
B 2 163 GLY 163 163 157  GLY GLY HHH . n 
B 2 164 ALA 164 164 158  ALA ALA HHH . n 
B 2 165 LEU 165 165 159  LEU LEU HHH . n 
B 2 166 THR 166 166 160  THR THR HHH . n 
B 2 167 SER 167 167 161  SER SER HHH . n 
B 2 168 GLY 168 168 162  GLY GLY HHH . n 
B 2 169 VAL 169 169 163  VAL VAL HHH . n 
B 2 170 HIS 170 170 164  HIS HIS HHH . n 
B 2 171 THR 171 171 165  THR THR HHH . n 
B 2 172 PHE 172 172 166  PHE PHE HHH . n 
B 2 173 PRO 173 173 167  PRO PRO HHH . n 
B 2 174 ALA 174 174 168  ALA ALA HHH . n 
B 2 175 VAL 175 175 169  VAL VAL HHH . n 
B 2 176 LEU 176 176 170  LEU LEU HHH . n 
B 2 177 GLN 177 177 171  GLN GLN HHH . n 
B 2 178 SER 178 178 172  SER SER HHH . n 
B 2 179 SER 179 179 173  SER SER HHH . n 
B 2 180 GLY 180 180 174  GLY GLY HHH . n 
B 2 181 LEU 181 181 175  LEU LEU HHH . n 
B 2 182 TYR 182 182 176  TYR TYR HHH . n 
B 2 183 SER 183 183 177  SER SER HHH . n 
B 2 184 LEU 184 184 178  LEU LEU HHH . n 
B 2 185 SER 185 185 179  SER SER HHH . n 
B 2 186 SER 186 186 180  SER SER HHH . n 
B 2 187 VAL 187 187 181  VAL VAL HHH . n 
B 2 188 VAL 188 188 182  VAL VAL HHH . n 
B 2 189 THR 189 189 183  THR THR HHH . n 
B 2 190 VAL 190 190 184  VAL VAL HHH . n 
B 2 191 PRO 191 191 185  PRO PRO HHH . n 
B 2 192 SER 192 192 186  SER SER HHH . n 
B 2 193 SER 193 193 187  SER SER HHH . n 
B 2 194 SER 194 194 188  SER SER HHH . n 
B 2 195 LEU 195 195 189  LEU LEU HHH . n 
B 2 196 GLY 196 196 190  GLY GLY HHH . n 
B 2 197 THR 197 197 191  THR THR HHH . n 
B 2 198 GLN 198 198 192  GLN GLN HHH . n 
B 2 199 THR 199 199 193  THR THR HHH . n 
B 2 200 TYR 200 200 194  TYR TYR HHH . n 
B 2 201 ILE 201 201 195  ILE ILE HHH . n 
B 2 202 CYS 202 202 196  CYS CYS HHH . n 
B 2 203 ASN 203 203 197  ASN ASN HHH . n 
B 2 204 VAL 204 204 198  VAL VAL HHH . n 
B 2 205 ASN 205 205 199  ASN ASN HHH . n 
B 2 206 HIS 206 206 200  HIS HIS HHH . n 
B 2 207 LYS 207 207 201  LYS LYS HHH . n 
B 2 208 PRO 208 208 202  PRO PRO HHH . n 
B 2 209 SER 209 209 203  SER SER HHH . n 
B 2 210 ASN 210 210 204  ASN ASN HHH . n 
B 2 211 THR 211 211 205  THR THR HHH . n 
B 2 212 LYS 212 212 206  LYS LYS HHH . n 
B 2 213 VAL 213 213 207  VAL VAL HHH . n 
B 2 214 ASP 214 214 208  ASP ASP HHH . n 
B 2 215 LYS 215 215 209  LYS LYS HHH . n 
B 2 216 LYS 216 216 210  LYS LYS HHH . n 
B 2 217 VAL 217 217 211  VAL VAL HHH . n 
B 2 218 GLU 218 218 212  GLU GLU HHH . n 
B 2 219 PRO 219 219 213  PRO PRO HHH . n 
B 2 220 LYS 220 220 214  LYS LYS HHH . n 
B 2 221 SER 221 221 215  SER SER HHH . n 
B 2 222 CYS 222 222 216  CYS CYS HHH . n 
C 3 1   ASP 1   1   1    ASP ASP LLL . n 
C 3 2   ILE 2   2   2    ILE ILE LLL . n 
C 3 3   GLN 3   3   3    GLN GLN LLL . n 
C 3 4   LEU 4   4   4    LEU LEU LLL . n 
C 3 5   THR 5   5   5    THR THR LLL . n 
C 3 6   GLN 6   6   6    GLN GLN LLL . n 
C 3 7   SER 7   7   7    SER SER LLL . n 
C 3 8   PRO 8   8   8    PRO PRO LLL . n 
C 3 9   ASP 9   9   9    ASP ASP LLL . n 
C 3 10  SER 10  10  10   SER SER LLL . n 
C 3 11  LEU 11  11  11   LEU LEU LLL . n 
C 3 12  ALA 12  12  12   ALA ALA LLL . n 
C 3 13  VAL 13  13  13   VAL VAL LLL . n 
C 3 14  SER 14  14  14   SER SER LLL . n 
C 3 15  LEU 15  15  15   LEU LEU LLL . n 
C 3 16  GLY 16  16  16   GLY GLY LLL . n 
C 3 17  GLU 17  17  17   GLU GLU LLL . n 
C 3 18  ARG 18  18  18   ARG ARG LLL . n 
C 3 19  ALA 19  19  19   ALA ALA LLL . n 
C 3 20  THR 20  20  20   THR THR LLL . n 
C 3 21  ILE 21  21  21   ILE ILE LLL . n 
C 3 22  ASN 22  22  22   ASN ASN LLL . n 
C 3 23  CYS 23  23  23   CYS CYS LLL . n 
C 3 24  LYS 24  24  24   LYS LYS LLL . n 
C 3 25  SER 25  25  25   SER SER LLL . n 
C 3 26  SER 26  26  26   SER SER LLL . n 
C 3 27  GLN 27  27  27   GLN GLN LLL . n 
C 3 28  SER 28  28  28   SER SER LLL . n 
C 3 29  VAL 29  29  29   VAL VAL LLL . n 
C 3 30  LEU 30  30  30   LEU LEU LLL . n 
C 3 31  TYR 31  31  31   TYR TYR LLL . n 
C 3 32  SER 32  32  32   SER SER LLL . n 
C 3 33  SER 33  33  33   SER SER LLL . n 
C 3 34  ILE 34  34  34   ILE ILE LLL . n 
C 3 35  ASN 35  35  35   ASN ASN LLL . n 
C 3 36  LYS 36  36  36   LYS LYS LLL . n 
C 3 37  ASN 37  37  37   ASN ASN LLL . n 
C 3 38  TYR 38  38  38   TYR TYR LLL . n 
C 3 39  LEU 39  39  39   LEU LEU LLL . n 
C 3 40  ALA 40  40  40   ALA ALA LLL . n 
C 3 41  TRP 41  41  41   TRP TRP LLL . n 
C 3 42  TYR 42  42  42   TYR TYR LLL . n 
C 3 43  GLN 43  43  43   GLN GLN LLL . n 
C 3 44  GLN 44  44  44   GLN GLN LLL . n 
C 3 45  LYS 45  45  45   LYS LYS LLL . n 
C 3 46  PRO 46  46  46   PRO PRO LLL . n 
C 3 47  GLY 47  47  47   GLY GLY LLL . n 
C 3 48  GLN 48  48  48   GLN GLN LLL . n 
C 3 49  PRO 49  49  49   PRO PRO LLL . n 
C 3 50  PRO 50  50  50   PRO PRO LLL . n 
C 3 51  LYS 51  51  51   LYS LYS LLL . n 
C 3 52  LEU 52  52  52   LEU LEU LLL . n 
C 3 53  LEU 53  53  53   LEU LEU LLL . n 
C 3 54  ILE 54  54  54   ILE ILE LLL . n 
C 3 55  TYR 55  55  55   TYR TYR LLL . n 
C 3 56  TRP 56  56  56   TRP TRP LLL . n 
C 3 57  ALA 57  57  57   ALA ALA LLL . n 
C 3 58  SER 58  58  58   SER SER LLL . n 
C 3 59  THR 59  59  59   THR THR LLL . n 
C 3 60  ARG 60  60  60   ARG ARG LLL . n 
C 3 61  GLU 61  61  61   GLU GLU LLL . n 
C 3 62  SER 62  62  62   SER SER LLL . n 
C 3 63  GLY 63  63  63   GLY GLY LLL . n 
C 3 64  VAL 64  64  64   VAL VAL LLL . n 
C 3 65  PRO 65  65  65   PRO PRO LLL . n 
C 3 66  ASP 66  66  66   ASP ASP LLL . n 
C 3 67  ARG 67  67  67   ARG ARG LLL . n 
C 3 68  PHE 68  68  68   PHE PHE LLL . n 
C 3 69  SER 69  69  69   SER SER LLL . n 
C 3 70  GLY 70  70  70   GLY GLY LLL . n 
C 3 71  SER 71  71  71   SER SER LLL . n 
C 3 72  GLY 72  72  72   GLY GLY LLL . n 
C 3 73  SER 73  73  73   SER SER LLL . n 
C 3 74  GLY 74  74  74   GLY GLY LLL . n 
C 3 75  THR 75  75  75   THR THR LLL . n 
C 3 76  ASP 76  76  76   ASP ASP LLL . n 
C 3 77  PHE 77  77  77   PHE PHE LLL . n 
C 3 78  THR 78  78  78   THR THR LLL . n 
C 3 79  LEU 79  79  79   LEU LEU LLL . n 
C 3 80  THR 80  80  80   THR THR LLL . n 
C 3 81  ILE 81  81  81   ILE ILE LLL . n 
C 3 82  SER 82  82  82   SER SER LLL . n 
C 3 83  SER 83  83  83   SER SER LLL . n 
C 3 84  LEU 84  84  84   LEU LEU LLL . n 
C 3 85  GLN 85  85  85   GLN GLN LLL . n 
C 3 86  ALA 86  86  86   ALA ALA LLL . n 
C 3 87  GLU 87  87  87   GLU GLU LLL . n 
C 3 88  ASP 88  88  88   ASP ASP LLL . n 
C 3 89  VAL 89  89  89   VAL VAL LLL . n 
C 3 90  ALA 90  90  90   ALA ALA LLL . n 
C 3 91  VAL 91  91  91   VAL VAL LLL . n 
C 3 92  TYR 92  92  92   TYR TYR LLL . n 
C 3 93  TYR 93  93  93   TYR TYR LLL . n 
C 3 94  CYS 94  94  94   CYS CYS LLL . n 
C 3 95  GLN 95  95  95   GLN GLN LLL . n 
C 3 96  GLN 96  96  96   GLN GLN LLL . n 
C 3 97  TYR 97  97  97   TYR TYR LLL . n 
C 3 98  TYR 98  98  98   TYR TYR LLL . n 
C 3 99  SER 99  99  99   SER SER LLL . n 
C 3 100 THR 100 100 100  THR THR LLL . n 
C 3 101 PRO 101 101 101  PRO PRO LLL . n 
C 3 102 TYR 102 102 102  TYR TYR LLL . n 
C 3 103 THR 103 103 103  THR THR LLL . n 
C 3 104 PHE 104 104 104  PHE PHE LLL . n 
C 3 105 GLY 105 105 105  GLY GLY LLL . n 
C 3 106 GLN 106 106 106  GLN GLN LLL . n 
C 3 107 GLY 107 107 107  GLY GLY LLL . n 
C 3 108 THR 108 108 108  THR THR LLL . n 
C 3 109 LYS 109 109 109  LYS LYS LLL . n 
C 3 110 VAL 110 110 110  VAL VAL LLL . n 
C 3 111 GLU 111 111 111  GLU GLU LLL . n 
C 3 112 ILE 112 112 112  ILE ILE LLL . n 
C 3 113 LYS 113 113 113  LYS LYS LLL . n 
C 3 114 ARG 114 114 114  ARG ARG LLL . n 
C 3 115 THR 115 115 115  THR THR LLL . n 
C 3 116 VAL 116 116 116  VAL VAL LLL . n 
C 3 117 ALA 117 117 117  ALA ALA LLL . n 
C 3 118 ALA 118 118 118  ALA ALA LLL . n 
C 3 119 PRO 119 119 119  PRO PRO LLL . n 
C 3 120 SER 120 120 120  SER SER LLL . n 
C 3 121 VAL 121 121 121  VAL VAL LLL . n 
C 3 122 PHE 122 122 122  PHE PHE LLL . n 
C 3 123 ILE 123 123 123  ILE ILE LLL . n 
C 3 124 PHE 124 124 124  PHE PHE LLL . n 
C 3 125 PRO 125 125 125  PRO PRO LLL . n 
C 3 126 PRO 126 126 126  PRO PRO LLL . n 
C 3 127 SER 127 127 127  SER SER LLL . n 
C 3 128 ASP 128 128 128  ASP ASP LLL . n 
C 3 129 GLU 129 129 129  GLU GLU LLL . n 
C 3 130 GLN 130 130 130  GLN GLN LLL . n 
C 3 131 LEU 131 131 131  LEU LEU LLL . n 
C 3 132 LYS 132 132 132  LYS LYS LLL . n 
C 3 133 SER 133 133 133  SER SER LLL . n 
C 3 134 GLY 134 134 134  GLY GLY LLL . n 
C 3 135 THR 135 135 135  THR THR LLL . n 
C 3 136 ALA 136 136 136  ALA ALA LLL . n 
C 3 137 SER 137 137 137  SER SER LLL . n 
C 3 138 VAL 138 138 138  VAL VAL LLL . n 
C 3 139 VAL 139 139 139  VAL VAL LLL . n 
C 3 140 CYS 140 140 140  CYS CYS LLL . n 
C 3 141 LEU 141 141 141  LEU LEU LLL . n 
C 3 142 LEU 142 142 142  LEU LEU LLL . n 
C 3 143 ASN 143 143 143  ASN ASN LLL . n 
C 3 144 ASN 144 144 144  ASN ASN LLL . n 
C 3 145 PHE 145 145 145  PHE PHE LLL . n 
C 3 146 TYR 146 146 146  TYR TYR LLL . n 
C 3 147 PRO 147 147 147  PRO PRO LLL . n 
C 3 148 ARG 148 148 148  ARG ARG LLL . n 
C 3 149 GLU 149 149 149  GLU GLU LLL . n 
C 3 150 ALA 150 150 150  ALA ALA LLL . n 
C 3 151 LYS 151 151 151  LYS LYS LLL . n 
C 3 152 VAL 152 152 152  VAL VAL LLL . n 
C 3 153 GLN 153 153 153  GLN GLN LLL . n 
C 3 154 TRP 154 154 154  TRP TRP LLL . n 
C 3 155 LYS 155 155 155  LYS LYS LLL . n 
C 3 156 VAL 156 156 156  VAL VAL LLL . n 
C 3 157 ASP 157 157 157  ASP ASP LLL . n 
C 3 158 ASN 158 158 158  ASN ASN LLL . n 
C 3 159 ALA 159 159 159  ALA ALA LLL . n 
C 3 160 LEU 160 160 160  LEU LEU LLL . n 
C 3 161 GLN 161 161 161  GLN GLN LLL . n 
C 3 162 SER 162 162 162  SER SER LLL . n 
C 3 163 GLY 163 163 163  GLY GLY LLL . n 
C 3 164 ASN 164 164 164  ASN ASN LLL . n 
C 3 165 SER 165 165 165  SER SER LLL . n 
C 3 166 GLN 166 166 166  GLN GLN LLL . n 
C 3 167 GLU 167 167 167  GLU GLU LLL . n 
C 3 168 SER 168 168 168  SER SER LLL . n 
C 3 169 VAL 169 169 169  VAL VAL LLL . n 
C 3 170 THR 170 170 170  THR THR LLL . n 
C 3 171 GLU 171 171 171  GLU GLU LLL . n 
C 3 172 GLN 172 172 172  GLN GLN LLL . n 
C 3 173 ASP 173 173 173  ASP ASP LLL . n 
C 3 174 SER 174 174 174  SER SER LLL . n 
C 3 175 LYS 175 175 175  LYS LYS LLL . n 
C 3 176 ASP 176 176 176  ASP ASP LLL . n 
C 3 177 SER 177 177 177  SER SER LLL . n 
C 3 178 THR 178 178 178  THR THR LLL . n 
C 3 179 TYR 179 179 179  TYR TYR LLL . n 
C 3 180 SER 180 180 180  SER SER LLL . n 
C 3 181 LEU 181 181 181  LEU LEU LLL . n 
C 3 182 SER 182 182 182  SER SER LLL . n 
C 3 183 SER 183 183 183  SER SER LLL . n 
C 3 184 THR 184 184 184  THR THR LLL . n 
C 3 185 LEU 185 185 185  LEU LEU LLL . n 
C 3 186 THR 186 186 186  THR THR LLL . n 
C 3 187 LEU 187 187 187  LEU LEU LLL . n 
C 3 188 SER 188 188 188  SER SER LLL . n 
C 3 189 LYS 189 189 189  LYS LYS LLL . n 
C 3 190 ALA 190 190 190  ALA ALA LLL . n 
C 3 191 ASP 191 191 191  ASP ASP LLL . n 
C 3 192 TYR 192 192 192  TYR TYR LLL . n 
C 3 193 GLU 193 193 193  GLU GLU LLL . n 
C 3 194 LYS 194 194 194  LYS LYS LLL . n 
C 3 195 HIS 195 195 195  HIS HIS LLL . n 
C 3 196 LYS 196 196 196  LYS LYS LLL . n 
C 3 197 VAL 197 197 197  VAL VAL LLL . n 
C 3 198 TYR 198 198 198  TYR TYR LLL . n 
C 3 199 ALA 199 199 199  ALA ALA LLL . n 
C 3 200 CYS 200 200 200  CYS CYS LLL . n 
C 3 201 GLU 201 201 201  GLU GLU LLL . n 
C 3 202 VAL 202 202 202  VAL VAL LLL . n 
C 3 203 THR 203 203 203  THR THR LLL . n 
C 3 204 HIS 204 204 204  HIS HIS LLL . n 
C 3 205 GLN 205 205 205  GLN GLN LLL . n 
C 3 206 GLY 206 206 206  GLY GLY LLL . n 
C 3 207 LEU 207 207 207  LEU LEU LLL . n 
C 3 208 SER 208 208 208  SER SER LLL . n 
C 3 209 SER 209 209 209  SER SER LLL . n 
C 3 210 PRO 210 210 210  PRO PRO LLL . n 
C 3 211 VAL 211 211 211  VAL VAL LLL . n 
C 3 212 THR 212 212 212  THR THR LLL . n 
C 3 213 LYS 213 213 213  LYS LYS LLL . n 
C 3 214 SER 214 214 214  SER SER LLL . n 
C 3 215 PHE 215 215 215  PHE PHE LLL . n 
C 3 216 ASN 216 216 216  ASN ASN LLL . n 
C 3 217 ARG 217 217 217  ARG ARG LLL . n 
C 3 218 GLY 218 218 218  GLY GLY LLL . n 
C 3 219 GLU 219 219 219  GLU GLU LLL . n 
C 3 220 CYS 220 220 ?    ?   ?   LLL . n 
C 3 221 SER 221 221 ?    ?   ?   LLL . n 
D 1 1   ARG 1   319 ?    ?   ?   AAA . n 
D 1 2   VAL 2   320 ?    ?   ?   AAA . n 
D 1 3   GLN 3   321 ?    ?   ?   AAA . n 
D 1 4   PRO 4   322 ?    ?   ?   AAA . n 
D 1 5   THR 5   323 ?    ?   ?   AAA . n 
D 1 6   GLU 6   324 ?    ?   ?   AAA . n 
D 1 7   SER 7   325 ?    ?   ?   AAA . n 
D 1 8   ILE 8   326 ?    ?   ?   AAA . n 
D 1 9   VAL 9   327 ?    ?   ?   AAA . n 
D 1 10  ARG 10  328 ?    ?   ?   AAA . n 
D 1 11  PHE 11  329 ?    ?   ?   AAA . n 
D 1 12  PRO 12  330 ?    ?   ?   AAA . n 
D 1 13  ASN 13  331 ?    ?   ?   AAA . n 
D 1 14  ILE 14  332 ?    ?   ?   AAA . n 
D 1 15  THR 15  333 333  THR THR AAA . n 
D 1 16  ASN 16  334 334  ASN ASN AAA . n 
D 1 17  LEU 17  335 335  LEU LEU AAA . n 
D 1 18  CYS 18  336 336  CYS CYS AAA . n 
D 1 19  PRO 19  337 337  PRO PRO AAA . n 
D 1 20  PHE 20  338 338  PHE PHE AAA . n 
D 1 21  GLY 21  339 339  GLY GLY AAA . n 
D 1 22  GLU 22  340 340  GLU GLU AAA . n 
D 1 23  VAL 23  341 341  VAL VAL AAA . n 
D 1 24  PHE 24  342 342  PHE PHE AAA . n 
D 1 25  ASN 25  343 343  ASN ASN AAA . n 
D 1 26  ALA 26  344 344  ALA ALA AAA . n 
D 1 27  THR 27  345 345  THR THR AAA . n 
D 1 28  ARG 28  346 346  ARG ARG AAA . n 
D 1 29  PHE 29  347 347  PHE PHE AAA . n 
D 1 30  ALA 30  348 348  ALA ALA AAA . n 
D 1 31  SER 31  349 349  SER SER AAA . n 
D 1 32  VAL 32  350 350  VAL VAL AAA . n 
D 1 33  TYR 33  351 351  TYR TYR AAA . n 
D 1 34  ALA 34  352 352  ALA ALA AAA . n 
D 1 35  TRP 35  353 353  TRP TRP AAA . n 
D 1 36  ASN 36  354 354  ASN ASN AAA . n 
D 1 37  ARG 37  355 355  ARG ARG AAA . n 
D 1 38  LYS 38  356 356  LYS LYS AAA . n 
D 1 39  ARG 39  357 357  ARG ARG AAA . n 
D 1 40  ILE 40  358 358  ILE ILE AAA . n 
D 1 41  SER 41  359 359  SER SER AAA . n 
D 1 42  ASN 42  360 360  ASN ASN AAA . n 
D 1 43  CYS 43  361 361  CYS CYS AAA . n 
D 1 44  VAL 44  362 362  VAL VAL AAA . n 
D 1 45  ALA 45  363 363  ALA ALA AAA . n 
D 1 46  ASP 46  364 364  ASP ASP AAA . n 
D 1 47  TYR 47  365 365  TYR TYR AAA . n 
D 1 48  SER 48  366 366  SER SER AAA . n 
D 1 49  VAL 49  367 367  VAL VAL AAA . n 
D 1 50  LEU 50  368 368  LEU LEU AAA . n 
D 1 51  TYR 51  369 369  TYR TYR AAA . n 
D 1 52  ASN 52  370 370  ASN ASN AAA . n 
D 1 53  SER 53  371 371  SER SER AAA . n 
D 1 54  ALA 54  372 372  ALA ALA AAA . n 
D 1 55  SER 55  373 373  SER SER AAA . n 
D 1 56  PHE 56  374 374  PHE PHE AAA . n 
D 1 57  SER 57  375 375  SER SER AAA . n 
D 1 58  THR 58  376 376  THR THR AAA . n 
D 1 59  PHE 59  377 377  PHE PHE AAA . n 
D 1 60  LYS 60  378 378  LYS LYS AAA . n 
D 1 61  CYS 61  379 379  CYS CYS AAA . n 
D 1 62  TYR 62  380 380  TYR TYR AAA . n 
D 1 63  GLY 63  381 381  GLY GLY AAA . n 
D 1 64  VAL 64  382 382  VAL VAL AAA . n 
D 1 65  SER 65  383 383  SER SER AAA . n 
D 1 66  PRO 66  384 384  PRO PRO AAA . n 
D 1 67  THR 67  385 385  THR THR AAA . n 
D 1 68  LYS 68  386 386  LYS LYS AAA . n 
D 1 69  LEU 69  387 387  LEU LEU AAA . n 
D 1 70  ASN 70  388 388  ASN ASN AAA . n 
D 1 71  ASP 71  389 389  ASP ASP AAA . n 
D 1 72  LEU 72  390 390  LEU LEU AAA . n 
D 1 73  CYS 73  391 391  CYS CYS AAA . n 
D 1 74  PHE 74  392 392  PHE PHE AAA . n 
D 1 75  THR 75  393 393  THR THR AAA . n 
D 1 76  ASN 76  394 394  ASN ASN AAA . n 
D 1 77  VAL 77  395 395  VAL VAL AAA . n 
D 1 78  TYR 78  396 396  TYR TYR AAA . n 
D 1 79  ALA 79  397 397  ALA ALA AAA . n 
D 1 80  ASP 80  398 398  ASP ASP AAA . n 
D 1 81  SER 81  399 399  SER SER AAA . n 
D 1 82  PHE 82  400 400  PHE PHE AAA . n 
D 1 83  VAL 83  401 401  VAL VAL AAA . n 
D 1 84  ILE 84  402 402  ILE ILE AAA . n 
D 1 85  ARG 85  403 403  ARG ARG AAA . n 
D 1 86  GLY 86  404 404  GLY GLY AAA . n 
D 1 87  ASP 87  405 405  ASP ASP AAA . n 
D 1 88  GLU 88  406 406  GLU GLU AAA . n 
D 1 89  VAL 89  407 407  VAL VAL AAA . n 
D 1 90  ARG 90  408 408  ARG ARG AAA . n 
D 1 91  GLN 91  409 409  GLN GLN AAA . n 
D 1 92  ILE 92  410 410  ILE ILE AAA . n 
D 1 93  ALA 93  411 411  ALA ALA AAA . n 
D 1 94  PRO 94  412 412  PRO PRO AAA . n 
D 1 95  GLY 95  413 413  GLY GLY AAA . n 
D 1 96  GLN 96  414 414  GLN GLN AAA . n 
D 1 97  THR 97  415 415  THR THR AAA . n 
D 1 98  GLY 98  416 416  GLY GLY AAA . n 
D 1 99  LYS 99  417 417  LYS LYS AAA . n 
D 1 100 ILE 100 418 418  ILE ILE AAA . n 
D 1 101 ALA 101 419 419  ALA ALA AAA . n 
D 1 102 ASP 102 420 420  ASP ASP AAA . n 
D 1 103 TYR 103 421 421  TYR TYR AAA . n 
D 1 104 ASN 104 422 422  ASN ASN AAA . n 
D 1 105 TYR 105 423 423  TYR TYR AAA . n 
D 1 106 LYS 106 424 424  LYS LYS AAA . n 
D 1 107 LEU 107 425 425  LEU LEU AAA . n 
D 1 108 PRO 108 426 426  PRO PRO AAA . n 
D 1 109 ASP 109 427 427  ASP ASP AAA . n 
D 1 110 ASP 110 428 428  ASP ASP AAA . n 
D 1 111 PHE 111 429 429  PHE PHE AAA . n 
D 1 112 THR 112 430 430  THR THR AAA . n 
D 1 113 GLY 113 431 431  GLY GLY AAA . n 
D 1 114 CYS 114 432 432  CYS CYS AAA . n 
D 1 115 VAL 115 433 433  VAL VAL AAA . n 
D 1 116 ILE 116 434 434  ILE ILE AAA . n 
D 1 117 ALA 117 435 435  ALA ALA AAA . n 
D 1 118 TRP 118 436 436  TRP TRP AAA . n 
D 1 119 ASN 119 437 437  ASN ASN AAA . n 
D 1 120 SER 120 438 438  SER SER AAA . n 
D 1 121 ASN 121 439 439  ASN ASN AAA . n 
D 1 122 ASN 122 440 440  ASN ASN AAA . n 
D 1 123 LEU 123 441 441  LEU LEU AAA . n 
D 1 124 ASP 124 442 442  ASP ASP AAA . n 
D 1 125 SER 125 443 443  SER SER AAA . n 
D 1 126 LYS 126 444 444  LYS LYS AAA . n 
D 1 127 VAL 127 445 445  VAL VAL AAA . n 
D 1 128 GLY 128 446 446  GLY GLY AAA . n 
D 1 129 GLY 129 447 447  GLY GLY AAA . n 
D 1 130 ASN 130 448 448  ASN ASN AAA . n 
D 1 131 TYR 131 449 449  TYR TYR AAA . n 
D 1 132 ASN 132 450 450  ASN ASN AAA . n 
D 1 133 TYR 133 451 451  TYR TYR AAA . n 
D 1 134 LEU 134 452 452  LEU LEU AAA . n 
D 1 135 TYR 135 453 453  TYR TYR AAA . n 
D 1 136 ARG 136 454 454  ARG ARG AAA . n 
D 1 137 LEU 137 455 455  LEU LEU AAA . n 
D 1 138 PHE 138 456 456  PHE PHE AAA . n 
D 1 139 ARG 139 457 457  ARG ARG AAA . n 
D 1 140 LYS 140 458 458  LYS LYS AAA . n 
D 1 141 SER 141 459 459  SER SER AAA . n 
D 1 142 ASN 142 460 460  ASN ASN AAA . n 
D 1 143 LEU 143 461 461  LEU LEU AAA . n 
D 1 144 LYS 144 462 462  LYS LYS AAA . n 
D 1 145 PRO 145 463 463  PRO PRO AAA . n 
D 1 146 PHE 146 464 464  PHE PHE AAA . n 
D 1 147 GLU 147 465 465  GLU GLU AAA . n 
D 1 148 ARG 148 466 466  ARG ARG AAA . n 
D 1 149 ASP 149 467 467  ASP ASP AAA . n 
D 1 150 ILE 150 468 468  ILE ILE AAA . n 
D 1 151 SER 151 469 469  SER SER AAA . n 
D 1 152 THR 152 470 470  THR THR AAA . n 
D 1 153 GLU 153 471 471  GLU GLU AAA . n 
D 1 154 ILE 154 472 472  ILE ILE AAA . n 
D 1 155 TYR 155 473 473  TYR TYR AAA . n 
D 1 156 GLN 156 474 474  GLN GLN AAA . n 
D 1 157 ALA 157 475 475  ALA ALA AAA . n 
D 1 158 GLY 158 476 476  GLY GLY AAA . n 
D 1 159 SER 159 477 477  SER SER AAA . n 
D 1 160 THR 160 478 478  THR THR AAA . n 
D 1 161 PRO 161 479 479  PRO PRO AAA . n 
D 1 162 CYS 162 480 480  CYS CYS AAA . n 
D 1 163 ASN 163 481 481  ASN ASN AAA . n 
D 1 164 GLY 164 482 482  GLY GLY AAA . n 
D 1 165 VAL 165 483 483  VAL VAL AAA . n 
D 1 166 GLU 166 484 484  GLU GLU AAA . n 
D 1 167 GLY 167 485 485  GLY GLY AAA . n 
D 1 168 PHE 168 486 486  PHE PHE AAA . n 
D 1 169 ASN 169 487 487  ASN ASN AAA . n 
D 1 170 CYS 170 488 488  CYS CYS AAA . n 
D 1 171 TYR 171 489 489  TYR TYR AAA . n 
D 1 172 PHE 172 490 490  PHE PHE AAA . n 
D 1 173 PRO 173 491 491  PRO PRO AAA . n 
D 1 174 LEU 174 492 492  LEU LEU AAA . n 
D 1 175 GLN 175 493 493  GLN GLN AAA . n 
D 1 176 SER 176 494 494  SER SER AAA . n 
D 1 177 TYR 177 495 495  TYR TYR AAA . n 
D 1 178 GLY 178 496 496  GLY GLY AAA . n 
D 1 179 PHE 179 497 497  PHE PHE AAA . n 
D 1 180 GLN 180 498 498  GLN GLN AAA . n 
D 1 181 PRO 181 499 499  PRO PRO AAA . n 
D 1 182 THR 182 500 500  THR THR AAA . n 
D 1 183 ASN 183 501 501  ASN ASN AAA . n 
D 1 184 GLY 184 502 502  GLY GLY AAA . n 
D 1 185 VAL 185 503 503  VAL VAL AAA . n 
D 1 186 GLY 186 504 504  GLY GLY AAA . n 
D 1 187 TYR 187 505 505  TYR TYR AAA . n 
D 1 188 GLN 188 506 506  GLN GLN AAA . n 
D 1 189 PRO 189 507 507  PRO PRO AAA . n 
D 1 190 TYR 190 508 508  TYR TYR AAA . n 
D 1 191 ARG 191 509 509  ARG ARG AAA . n 
D 1 192 VAL 192 510 510  VAL VAL AAA . n 
D 1 193 VAL 193 511 511  VAL VAL AAA . n 
D 1 194 VAL 194 512 512  VAL VAL AAA . n 
D 1 195 LEU 195 513 513  LEU LEU AAA . n 
D 1 196 SER 196 514 514  SER SER AAA . n 
D 1 197 PHE 197 515 515  PHE PHE AAA . n 
D 1 198 GLU 198 516 516  GLU GLU AAA . n 
D 1 199 LEU 199 517 517  LEU LEU AAA . n 
D 1 200 LEU 200 518 518  LEU LEU AAA . n 
D 1 201 HIS 201 519 519  HIS HIS AAA . n 
D 1 202 ALA 202 520 520  ALA ALA AAA . n 
D 1 203 PRO 203 521 521  PRO PRO AAA . n 
D 1 204 ALA 204 522 522  ALA ALA AAA . n 
D 1 205 THR 205 523 523  THR THR AAA . n 
D 1 206 VAL 206 524 524  VAL VAL AAA . n 
D 1 207 CYS 207 525 525  CYS CYS AAA . n 
D 1 208 GLY 208 526 526  GLY GLY AAA . n 
D 1 209 PRO 209 527 527  PRO PRO AAA . n 
D 1 210 LYS 210 528 528  LYS LYS AAA . n 
D 1 211 LYS 211 529 ?    ?   ?   AAA . n 
D 1 212 SER 212 530 ?    ?   ?   AAA . n 
D 1 213 THR 213 531 ?    ?   ?   AAA . n 
D 1 214 ASN 214 532 ?    ?   ?   AAA . n 
D 1 215 LEU 215 533 ?    ?   ?   AAA . n 
D 1 216 VAL 216 534 ?    ?   ?   AAA . n 
D 1 217 LYS 217 535 ?    ?   ?   AAA . n 
D 1 218 ASN 218 536 ?    ?   ?   AAA . n 
D 1 219 LYS 219 537 ?    ?   ?   AAA . n 
D 1 220 CYS 220 538 ?    ?   ?   AAA . n 
D 1 221 VAL 221 539 ?    ?   ?   AAA . n 
D 1 222 ASN 222 540 ?    ?   ?   AAA . n 
D 1 223 PHE 223 541 ?    ?   ?   AAA . n 
D 1 224 SER 224 542 ?    ?   ?   AAA . n 
D 1 225 GLY 225 543 ?    ?   ?   AAA . n 
D 1 226 HIS 226 544 ?    ?   ?   AAA . n 
D 1 227 HIS 227 545 ?    ?   ?   AAA . n 
D 1 228 HIS 228 546 ?    ?   ?   AAA . n 
D 1 229 HIS 229 547 ?    ?   ?   AAA . n 
D 1 230 HIS 230 548 ?    ?   ?   AAA . n 
D 1 231 HIS 231 549 ?    ?   ?   AAA . n 
E 2 1   GLN 1   1   1    GLN GLN BBB . n 
E 2 2   MET 2   2   2    MET MET BBB . n 
E 2 3   GLN 3   3   3    GLN GLN BBB . n 
E 2 4   LEU 4   4   4    LEU LEU BBB . n 
E 2 5   VAL 5   5   5    VAL VAL BBB . n 
E 2 6   GLN 6   6   6    GLN GLN BBB . n 
E 2 7   SER 7   7   7    SER SER BBB . n 
E 2 8   GLY 8   8   8    GLY GLY BBB . n 
E 2 9   THR 9   9   9    THR THR BBB . n 
E 2 10  GLU 10  10  10   GLU GLU BBB . n 
E 2 11  VAL 11  11  11   VAL VAL BBB . n 
E 2 12  LYS 12  12  12   LYS LYS BBB . n 
E 2 13  LYS 13  13  13   LYS LYS BBB . n 
E 2 14  PRO 14  14  14   PRO PRO BBB . n 
E 2 15  GLY 15  15  15   GLY GLY BBB . n 
E 2 16  GLU 16  16  16   GLU GLU BBB . n 
E 2 17  SER 17  17  17   SER SER BBB . n 
E 2 18  LEU 18  18  18   LEU LEU BBB . n 
E 2 19  LYS 19  19  19   LYS LYS BBB . n 
E 2 20  ILE 20  20  20   ILE ILE BBB . n 
E 2 21  SER 21  21  21   SER SER BBB . n 
E 2 22  CYS 22  22  22   CYS CYS BBB . n 
E 2 23  LYS 23  23  23   LYS LYS BBB . n 
E 2 24  GLY 24  24  24   GLY GLY BBB . n 
E 2 25  SER 25  25  25   SER SER BBB . n 
E 2 26  GLY 26  26  26   GLY GLY BBB . n 
E 2 27  TYR 27  27  27   TYR TYR BBB . n 
E 2 28  GLY 28  28  28   GLY GLY BBB . n 
E 2 29  PHE 29  29  29   PHE PHE BBB . n 
E 2 30  ILE 30  30  30   ILE ILE BBB . n 
E 2 31  THR 31  31  31   THR THR BBB . n 
E 2 32  TYR 32  32  32   TYR TYR BBB . n 
E 2 33  TRP 33  33  33   TRP TRP BBB . n 
E 2 34  ILE 34  34  34   ILE ILE BBB . n 
E 2 35  GLY 35  35  35   GLY GLY BBB . n 
E 2 36  TRP 36  36  36   TRP TRP BBB . n 
E 2 37  VAL 37  37  37   VAL VAL BBB . n 
E 2 38  ARG 38  38  38   ARG ARG BBB . n 
E 2 39  GLN 39  39  39   GLN GLN BBB . n 
E 2 40  MET 40  40  40   MET MET BBB . n 
E 2 41  PRO 41  41  41   PRO PRO BBB . n 
E 2 42  GLY 42  42  42   GLY GLY BBB . n 
E 2 43  LYS 43  43  43   LYS LYS BBB . n 
E 2 44  GLY 44  44  44   GLY GLY BBB . n 
E 2 45  LEU 45  45  45   LEU LEU BBB . n 
E 2 46  GLU 46  46  46   GLU GLU BBB . n 
E 2 47  TRP 47  47  47   TRP TRP BBB . n 
E 2 48  MET 48  48  48   MET MET BBB . n 
E 2 49  GLY 49  49  49   GLY GLY BBB . n 
E 2 50  ILE 50  50  50   ILE ILE BBB . n 
E 2 51  ILE 51  51  51   ILE ILE BBB . n 
E 2 52  TYR 52  52  52   TYR TYR BBB . n 
E 2 53  PRO 53  53  52A  PRO PRO BBB . n 
E 2 54  GLY 54  54  53   GLY GLY BBB . n 
E 2 55  ASP 55  55  54   ASP ASP BBB . n 
E 2 56  SER 56  56  55   SER SER BBB . n 
E 2 57  GLU 57  57  56   GLU GLU BBB . n 
E 2 58  THR 58  58  57   THR THR BBB . n 
E 2 59  ARG 59  59  58   ARG ARG BBB . n 
E 2 60  TYR 60  60  59   TYR TYR BBB . n 
E 2 61  SER 61  61  60   SER SER BBB . n 
E 2 62  PRO 62  62  61   PRO PRO BBB . n 
E 2 63  SER 63  63  62   SER SER BBB . n 
E 2 64  PHE 64  64  63   PHE PHE BBB . n 
E 2 65  GLN 65  65  64   GLN GLN BBB . n 
E 2 66  GLY 66  66  65   GLY GLY BBB . n 
E 2 67  GLN 67  67  66   GLN GLN BBB . n 
E 2 68  VAL 68  68  67   VAL VAL BBB . n 
E 2 69  THR 69  69  68   THR THR BBB . n 
E 2 70  ILE 70  70  69   ILE ILE BBB . n 
E 2 71  SER 71  71  70   SER SER BBB . n 
E 2 72  ALA 72  72  71   ALA ALA BBB . n 
E 2 73  ASP 73  73  72   ASP ASP BBB . n 
E 2 74  LYS 74  74  73   LYS LYS BBB . n 
E 2 75  SER 75  75  74   SER SER BBB . n 
E 2 76  ILE 76  76  75   ILE ILE BBB . n 
E 2 77  ASN 77  77  76   ASN ASN BBB . n 
E 2 78  THR 78  78  77   THR THR BBB . n 
E 2 79  ALA 79  79  78   ALA ALA BBB . n 
E 2 80  TYR 80  80  79   TYR TYR BBB . n 
E 2 81  LEU 81  81  80   LEU LEU BBB . n 
E 2 82  GLN 82  82  81   GLN GLN BBB . n 
E 2 83  TRP 83  83  82   TRP TRP BBB . n 
E 2 84  SER 84  84  82A  SER SER BBB . n 
E 2 85  SER 85  85  82B  SER SER BBB . n 
E 2 86  LEU 86  86  82C  LEU LEU BBB . n 
E 2 87  LYS 87  87  83   LYS LYS BBB . n 
E 2 88  ALA 88  88  84   ALA ALA BBB . n 
E 2 89  SER 89  89  85   SER SER BBB . n 
E 2 90  ASP 90  90  86   ASP ASP BBB . n 
E 2 91  THR 91  91  87   THR THR BBB . n 
E 2 92  ALA 92  92  88   ALA ALA BBB . n 
E 2 93  ILE 93  93  89   ILE ILE BBB . n 
E 2 94  TYR 94  94  90   TYR TYR BBB . n 
E 2 95  TYR 95  95  91   TYR TYR BBB . n 
E 2 96  CYS 96  96  92   CYS CYS BBB . n 
E 2 97  ALA 97  97  93   ALA ALA BBB . n 
E 2 98  GLY 98  98  94   GLY GLY BBB . n 
E 2 99  GLY 99  99  95   GLY GLY BBB . n 
E 2 100 SER 100 100 96   SER SER BBB . n 
E 2 101 GLY 101 101 97   GLY GLY BBB . n 
E 2 102 ILE 102 102 98   ILE ILE BBB . n 
E 2 103 SER 103 103 99   SER SER BBB . n 
E 2 104 THR 104 104 100  THR THR BBB . n 
E 2 105 PRO 105 105 100A PRO PRO BBB . n 
E 2 106 MET 106 106 100B MET MET BBB . n 
E 2 107 ASP 107 107 101  ASP ASP BBB . n 
E 2 108 VAL 108 108 102  VAL VAL BBB . n 
E 2 109 TRP 109 109 103  TRP TRP BBB . n 
E 2 110 GLY 110 110 104  GLY GLY BBB . n 
E 2 111 GLN 111 111 105  GLN GLN BBB . n 
E 2 112 GLY 112 112 106  GLY GLY BBB . n 
E 2 113 THR 113 113 107  THR THR BBB . n 
E 2 114 THR 114 114 108  THR THR BBB . n 
E 2 115 VAL 115 115 109  VAL VAL BBB . n 
E 2 116 THR 116 116 110  THR THR BBB . n 
E 2 117 VAL 117 117 111  VAL VAL BBB . n 
E 2 118 SER 118 118 112  SER SER BBB . n 
E 2 119 SER 119 119 113  SER SER BBB . n 
E 2 120 ALA 120 120 114  ALA ALA BBB . n 
E 2 121 SER 121 121 115  SER SER BBB . n 
E 2 122 THR 122 122 116  THR THR BBB . n 
E 2 123 LYS 123 123 117  LYS LYS BBB . n 
E 2 124 GLY 124 124 118  GLY GLY BBB . n 
E 2 125 PRO 125 125 119  PRO PRO BBB . n 
E 2 126 SER 126 126 120  SER SER BBB . n 
E 2 127 VAL 127 127 121  VAL VAL BBB . n 
E 2 128 PHE 128 128 122  PHE PHE BBB . n 
E 2 129 PRO 129 129 123  PRO PRO BBB . n 
E 2 130 LEU 130 130 124  LEU LEU BBB . n 
E 2 131 ALA 131 131 125  ALA ALA BBB . n 
E 2 132 PRO 132 132 126  PRO PRO BBB . n 
E 2 133 SER 133 133 127  SER SER BBB . n 
E 2 134 SER 134 134 128  SER SER BBB . n 
E 2 135 LYS 135 135 129  LYS LYS BBB . n 
E 2 136 SER 136 136 130  SER SER BBB . n 
E 2 137 THR 137 137 131  THR THR BBB . n 
E 2 138 SER 138 138 132  SER SER BBB . n 
E 2 139 GLY 139 139 133  GLY GLY BBB . n 
E 2 140 GLY 140 140 134  GLY GLY BBB . n 
E 2 141 THR 141 141 135  THR THR BBB . n 
E 2 142 ALA 142 142 136  ALA ALA BBB . n 
E 2 143 ALA 143 143 137  ALA ALA BBB . n 
E 2 144 LEU 144 144 138  LEU LEU BBB . n 
E 2 145 GLY 145 145 139  GLY GLY BBB . n 
E 2 146 CYS 146 146 140  CYS CYS BBB . n 
E 2 147 LEU 147 147 141  LEU LEU BBB . n 
E 2 148 VAL 148 148 142  VAL VAL BBB . n 
E 2 149 LYS 149 149 143  LYS LYS BBB . n 
E 2 150 ASP 150 150 144  ASP ASP BBB . n 
E 2 151 TYR 151 151 145  TYR TYR BBB . n 
E 2 152 PHE 152 152 146  PHE PHE BBB . n 
E 2 153 PRO 153 153 147  PRO PRO BBB . n 
E 2 154 GLU 154 154 148  GLU GLU BBB . n 
E 2 155 PRO 155 155 149  PRO PRO BBB . n 
E 2 156 VAL 156 156 150  VAL VAL BBB . n 
E 2 157 THR 157 157 151  THR THR BBB . n 
E 2 158 VAL 158 158 152  VAL VAL BBB . n 
E 2 159 SER 159 159 153  SER SER BBB . n 
E 2 160 TRP 160 160 154  TRP TRP BBB . n 
E 2 161 ASN 161 161 155  ASN ASN BBB . n 
E 2 162 SER 162 162 156  SER SER BBB . n 
E 2 163 GLY 163 163 157  GLY GLY BBB . n 
E 2 164 ALA 164 164 158  ALA ALA BBB . n 
E 2 165 LEU 165 165 159  LEU LEU BBB . n 
E 2 166 THR 166 166 160  THR THR BBB . n 
E 2 167 SER 167 167 161  SER SER BBB . n 
E 2 168 GLY 168 168 162  GLY GLY BBB . n 
E 2 169 VAL 169 169 163  VAL VAL BBB . n 
E 2 170 HIS 170 170 164  HIS HIS BBB . n 
E 2 171 THR 171 171 165  THR THR BBB . n 
E 2 172 PHE 172 172 166  PHE PHE BBB . n 
E 2 173 PRO 173 173 167  PRO PRO BBB . n 
E 2 174 ALA 174 174 168  ALA ALA BBB . n 
E 2 175 VAL 175 175 169  VAL VAL BBB . n 
E 2 176 LEU 176 176 170  LEU LEU BBB . n 
E 2 177 GLN 177 177 171  GLN GLN BBB . n 
E 2 178 SER 178 178 172  SER SER BBB . n 
E 2 179 SER 179 179 173  SER SER BBB . n 
E 2 180 GLY 180 180 174  GLY GLY BBB . n 
E 2 181 LEU 181 181 175  LEU LEU BBB . n 
E 2 182 TYR 182 182 176  TYR TYR BBB . n 
E 2 183 SER 183 183 177  SER SER BBB . n 
E 2 184 LEU 184 184 178  LEU LEU BBB . n 
E 2 185 SER 185 185 179  SER SER BBB . n 
E 2 186 SER 186 186 180  SER SER BBB . n 
E 2 187 VAL 187 187 181  VAL VAL BBB . n 
E 2 188 VAL 188 188 182  VAL VAL BBB . n 
E 2 189 THR 189 189 183  THR THR BBB . n 
E 2 190 VAL 190 190 184  VAL VAL BBB . n 
E 2 191 PRO 191 191 185  PRO PRO BBB . n 
E 2 192 SER 192 192 186  SER SER BBB . n 
E 2 193 SER 193 193 187  SER SER BBB . n 
E 2 194 SER 194 194 188  SER SER BBB . n 
E 2 195 LEU 195 195 189  LEU LEU BBB . n 
E 2 196 GLY 196 196 190  GLY GLY BBB . n 
E 2 197 THR 197 197 191  THR THR BBB . n 
E 2 198 GLN 198 198 192  GLN GLN BBB . n 
E 2 199 THR 199 199 193  THR THR BBB . n 
E 2 200 TYR 200 200 194  TYR TYR BBB . n 
E 2 201 ILE 201 201 195  ILE ILE BBB . n 
E 2 202 CYS 202 202 196  CYS CYS BBB . n 
E 2 203 ASN 203 203 197  ASN ASN BBB . n 
E 2 204 VAL 204 204 198  VAL VAL BBB . n 
E 2 205 ASN 205 205 199  ASN ASN BBB . n 
E 2 206 HIS 206 206 200  HIS HIS BBB . n 
E 2 207 LYS 207 207 201  LYS LYS BBB . n 
E 2 208 PRO 208 208 202  PRO PRO BBB . n 
E 2 209 SER 209 209 203  SER SER BBB . n 
E 2 210 ASN 210 210 204  ASN ASN BBB . n 
E 2 211 THR 211 211 205  THR THR BBB . n 
E 2 212 LYS 212 212 206  LYS LYS BBB . n 
E 2 213 VAL 213 213 207  VAL VAL BBB . n 
E 2 214 ASP 214 214 208  ASP ASP BBB . n 
E 2 215 LYS 215 215 209  LYS LYS BBB . n 
E 2 216 LYS 216 216 210  LYS LYS BBB . n 
E 2 217 VAL 217 217 211  VAL VAL BBB . n 
E 2 218 GLU 218 218 212  GLU GLU BBB . n 
E 2 219 PRO 219 219 213  PRO PRO BBB . n 
E 2 220 LYS 220 220 214  LYS LYS BBB . n 
E 2 221 SER 221 221 215  SER SER BBB . n 
E 2 222 CYS 222 222 216  CYS CYS BBB . n 
F 3 1   ASP 1   1   1    ASP ASP CCC . n 
F 3 2   ILE 2   2   2    ILE ILE CCC . n 
F 3 3   GLN 3   3   3    GLN GLN CCC . n 
F 3 4   LEU 4   4   4    LEU LEU CCC . n 
F 3 5   THR 5   5   5    THR THR CCC . n 
F 3 6   GLN 6   6   6    GLN GLN CCC . n 
F 3 7   SER 7   7   7    SER SER CCC . n 
F 3 8   PRO 8   8   8    PRO PRO CCC . n 
F 3 9   ASP 9   9   9    ASP ASP CCC . n 
F 3 10  SER 10  10  10   SER SER CCC . n 
F 3 11  LEU 11  11  11   LEU LEU CCC . n 
F 3 12  ALA 12  12  12   ALA ALA CCC . n 
F 3 13  VAL 13  13  13   VAL VAL CCC . n 
F 3 14  SER 14  14  14   SER SER CCC . n 
F 3 15  LEU 15  15  15   LEU LEU CCC . n 
F 3 16  GLY 16  16  16   GLY GLY CCC . n 
F 3 17  GLU 17  17  17   GLU GLU CCC . n 
F 3 18  ARG 18  18  18   ARG ARG CCC . n 
F 3 19  ALA 19  19  19   ALA ALA CCC . n 
F 3 20  THR 20  20  20   THR THR CCC . n 
F 3 21  ILE 21  21  21   ILE ILE CCC . n 
F 3 22  ASN 22  22  22   ASN ASN CCC . n 
F 3 23  CYS 23  23  23   CYS CYS CCC . n 
F 3 24  LYS 24  24  24   LYS LYS CCC . n 
F 3 25  SER 25  25  25   SER SER CCC . n 
F 3 26  SER 26  26  26   SER SER CCC . n 
F 3 27  GLN 27  27  27   GLN GLN CCC . n 
F 3 28  SER 28  28  28   SER SER CCC . n 
F 3 29  VAL 29  29  29   VAL VAL CCC . n 
F 3 30  LEU 30  30  30   LEU LEU CCC . n 
F 3 31  TYR 31  31  31   TYR TYR CCC . n 
F 3 32  SER 32  32  32   SER SER CCC . n 
F 3 33  SER 33  33  33   SER SER CCC . n 
F 3 34  ILE 34  34  34   ILE ILE CCC . n 
F 3 35  ASN 35  35  35   ASN ASN CCC . n 
F 3 36  LYS 36  36  36   LYS LYS CCC . n 
F 3 37  ASN 37  37  37   ASN ASN CCC . n 
F 3 38  TYR 38  38  38   TYR TYR CCC . n 
F 3 39  LEU 39  39  39   LEU LEU CCC . n 
F 3 40  ALA 40  40  40   ALA ALA CCC . n 
F 3 41  TRP 41  41  41   TRP TRP CCC . n 
F 3 42  TYR 42  42  42   TYR TYR CCC . n 
F 3 43  GLN 43  43  43   GLN GLN CCC . n 
F 3 44  GLN 44  44  44   GLN GLN CCC . n 
F 3 45  LYS 45  45  45   LYS LYS CCC . n 
F 3 46  PRO 46  46  46   PRO PRO CCC . n 
F 3 47  GLY 47  47  47   GLY GLY CCC . n 
F 3 48  GLN 48  48  48   GLN GLN CCC . n 
F 3 49  PRO 49  49  49   PRO PRO CCC . n 
F 3 50  PRO 50  50  50   PRO PRO CCC . n 
F 3 51  LYS 51  51  51   LYS LYS CCC . n 
F 3 52  LEU 52  52  52   LEU LEU CCC . n 
F 3 53  LEU 53  53  53   LEU LEU CCC . n 
F 3 54  ILE 54  54  54   ILE ILE CCC . n 
F 3 55  TYR 55  55  55   TYR TYR CCC . n 
F 3 56  TRP 56  56  56   TRP TRP CCC . n 
F 3 57  ALA 57  57  57   ALA ALA CCC . n 
F 3 58  SER 58  58  58   SER SER CCC . n 
F 3 59  THR 59  59  59   THR THR CCC . n 
F 3 60  ARG 60  60  60   ARG ARG CCC . n 
F 3 61  GLU 61  61  61   GLU GLU CCC . n 
F 3 62  SER 62  62  62   SER SER CCC . n 
F 3 63  GLY 63  63  63   GLY GLY CCC . n 
F 3 64  VAL 64  64  64   VAL VAL CCC . n 
F 3 65  PRO 65  65  65   PRO PRO CCC . n 
F 3 66  ASP 66  66  66   ASP ASP CCC . n 
F 3 67  ARG 67  67  67   ARG ARG CCC . n 
F 3 68  PHE 68  68  68   PHE PHE CCC . n 
F 3 69  SER 69  69  69   SER SER CCC . n 
F 3 70  GLY 70  70  70   GLY GLY CCC . n 
F 3 71  SER 71  71  71   SER SER CCC . n 
F 3 72  GLY 72  72  72   GLY GLY CCC . n 
F 3 73  SER 73  73  73   SER SER CCC . n 
F 3 74  GLY 74  74  74   GLY GLY CCC . n 
F 3 75  THR 75  75  75   THR THR CCC . n 
F 3 76  ASP 76  76  76   ASP ASP CCC . n 
F 3 77  PHE 77  77  77   PHE PHE CCC . n 
F 3 78  THR 78  78  78   THR THR CCC . n 
F 3 79  LEU 79  79  79   LEU LEU CCC . n 
F 3 80  THR 80  80  80   THR THR CCC . n 
F 3 81  ILE 81  81  81   ILE ILE CCC . n 
F 3 82  SER 82  82  82   SER SER CCC . n 
F 3 83  SER 83  83  83   SER SER CCC . n 
F 3 84  LEU 84  84  84   LEU LEU CCC . n 
F 3 85  GLN 85  85  85   GLN GLN CCC . n 
F 3 86  ALA 86  86  86   ALA ALA CCC . n 
F 3 87  GLU 87  87  87   GLU GLU CCC . n 
F 3 88  ASP 88  88  88   ASP ASP CCC . n 
F 3 89  VAL 89  89  89   VAL VAL CCC . n 
F 3 90  ALA 90  90  90   ALA ALA CCC . n 
F 3 91  VAL 91  91  91   VAL VAL CCC . n 
F 3 92  TYR 92  92  92   TYR TYR CCC . n 
F 3 93  TYR 93  93  93   TYR TYR CCC . n 
F 3 94  CYS 94  94  94   CYS CYS CCC . n 
F 3 95  GLN 95  95  95   GLN GLN CCC . n 
F 3 96  GLN 96  96  96   GLN GLN CCC . n 
F 3 97  TYR 97  97  97   TYR TYR CCC . n 
F 3 98  TYR 98  98  98   TYR TYR CCC . n 
F 3 99  SER 99  99  99   SER SER CCC . n 
F 3 100 THR 100 100 100  THR THR CCC . n 
F 3 101 PRO 101 101 101  PRO PRO CCC . n 
F 3 102 TYR 102 102 102  TYR TYR CCC . n 
F 3 103 THR 103 103 103  THR THR CCC . n 
F 3 104 PHE 104 104 104  PHE PHE CCC . n 
F 3 105 GLY 105 105 105  GLY GLY CCC . n 
F 3 106 GLN 106 106 106  GLN GLN CCC . n 
F 3 107 GLY 107 107 107  GLY GLY CCC . n 
F 3 108 THR 108 108 108  THR THR CCC . n 
F 3 109 LYS 109 109 109  LYS LYS CCC . n 
F 3 110 VAL 110 110 110  VAL VAL CCC . n 
F 3 111 GLU 111 111 111  GLU GLU CCC . n 
F 3 112 ILE 112 112 112  ILE ILE CCC . n 
F 3 113 LYS 113 113 113  LYS LYS CCC . n 
F 3 114 ARG 114 114 114  ARG ARG CCC . n 
F 3 115 THR 115 115 115  THR THR CCC . n 
F 3 116 VAL 116 116 116  VAL VAL CCC . n 
F 3 117 ALA 117 117 117  ALA ALA CCC . n 
F 3 118 ALA 118 118 118  ALA ALA CCC . n 
F 3 119 PRO 119 119 119  PRO PRO CCC . n 
F 3 120 SER 120 120 120  SER SER CCC . n 
F 3 121 VAL 121 121 121  VAL VAL CCC . n 
F 3 122 PHE 122 122 122  PHE PHE CCC . n 
F 3 123 ILE 123 123 123  ILE ILE CCC . n 
F 3 124 PHE 124 124 124  PHE PHE CCC . n 
F 3 125 PRO 125 125 125  PRO PRO CCC . n 
F 3 126 PRO 126 126 126  PRO PRO CCC . n 
F 3 127 SER 127 127 127  SER SER CCC . n 
F 3 128 ASP 128 128 128  ASP ASP CCC . n 
F 3 129 GLU 129 129 129  GLU GLU CCC . n 
F 3 130 GLN 130 130 130  GLN GLN CCC . n 
F 3 131 LEU 131 131 131  LEU LEU CCC . n 
F 3 132 LYS 132 132 132  LYS LYS CCC . n 
F 3 133 SER 133 133 133  SER SER CCC . n 
F 3 134 GLY 134 134 134  GLY GLY CCC . n 
F 3 135 THR 135 135 135  THR THR CCC . n 
F 3 136 ALA 136 136 136  ALA ALA CCC . n 
F 3 137 SER 137 137 137  SER SER CCC . n 
F 3 138 VAL 138 138 138  VAL VAL CCC . n 
F 3 139 VAL 139 139 139  VAL VAL CCC . n 
F 3 140 CYS 140 140 140  CYS CYS CCC . n 
F 3 141 LEU 141 141 141  LEU LEU CCC . n 
F 3 142 LEU 142 142 142  LEU LEU CCC . n 
F 3 143 ASN 143 143 143  ASN ASN CCC . n 
F 3 144 ASN 144 144 144  ASN ASN CCC . n 
F 3 145 PHE 145 145 145  PHE PHE CCC . n 
F 3 146 TYR 146 146 146  TYR TYR CCC . n 
F 3 147 PRO 147 147 147  PRO PRO CCC . n 
F 3 148 ARG 148 148 148  ARG ARG CCC . n 
F 3 149 GLU 149 149 149  GLU GLU CCC . n 
F 3 150 ALA 150 150 150  ALA ALA CCC . n 
F 3 151 LYS 151 151 151  LYS LYS CCC . n 
F 3 152 VAL 152 152 152  VAL VAL CCC . n 
F 3 153 GLN 153 153 153  GLN GLN CCC . n 
F 3 154 TRP 154 154 154  TRP TRP CCC . n 
F 3 155 LYS 155 155 155  LYS LYS CCC . n 
F 3 156 VAL 156 156 156  VAL VAL CCC . n 
F 3 157 ASP 157 157 157  ASP ASP CCC . n 
F 3 158 ASN 158 158 158  ASN ASN CCC . n 
F 3 159 ALA 159 159 159  ALA ALA CCC . n 
F 3 160 LEU 160 160 160  LEU LEU CCC . n 
F 3 161 GLN 161 161 161  GLN GLN CCC . n 
F 3 162 SER 162 162 162  SER SER CCC . n 
F 3 163 GLY 163 163 163  GLY GLY CCC . n 
F 3 164 ASN 164 164 164  ASN ASN CCC . n 
F 3 165 SER 165 165 165  SER SER CCC . n 
F 3 166 GLN 166 166 166  GLN GLN CCC . n 
F 3 167 GLU 167 167 167  GLU GLU CCC . n 
F 3 168 SER 168 168 168  SER SER CCC . n 
F 3 169 VAL 169 169 169  VAL VAL CCC . n 
F 3 170 THR 170 170 170  THR THR CCC . n 
F 3 171 GLU 171 171 171  GLU GLU CCC . n 
F 3 172 GLN 172 172 172  GLN GLN CCC . n 
F 3 173 ASP 173 173 173  ASP ASP CCC . n 
F 3 174 SER 174 174 174  SER SER CCC . n 
F 3 175 LYS 175 175 175  LYS LYS CCC . n 
F 3 176 ASP 176 176 176  ASP ASP CCC . n 
F 3 177 SER 177 177 177  SER SER CCC . n 
F 3 178 THR 178 178 178  THR THR CCC . n 
F 3 179 TYR 179 179 179  TYR TYR CCC . n 
F 3 180 SER 180 180 180  SER SER CCC . n 
F 3 181 LEU 181 181 181  LEU LEU CCC . n 
F 3 182 SER 182 182 182  SER SER CCC . n 
F 3 183 SER 183 183 183  SER SER CCC . n 
F 3 184 THR 184 184 184  THR THR CCC . n 
F 3 185 LEU 185 185 185  LEU LEU CCC . n 
F 3 186 THR 186 186 186  THR THR CCC . n 
F 3 187 LEU 187 187 187  LEU LEU CCC . n 
F 3 188 SER 188 188 188  SER SER CCC . n 
F 3 189 LYS 189 189 189  LYS LYS CCC . n 
F 3 190 ALA 190 190 190  ALA ALA CCC . n 
F 3 191 ASP 191 191 191  ASP ASP CCC . n 
F 3 192 TYR 192 192 192  TYR TYR CCC . n 
F 3 193 GLU 193 193 193  GLU GLU CCC . n 
F 3 194 LYS 194 194 194  LYS LYS CCC . n 
F 3 195 HIS 195 195 195  HIS HIS CCC . n 
F 3 196 LYS 196 196 196  LYS LYS CCC . n 
F 3 197 VAL 197 197 197  VAL VAL CCC . n 
F 3 198 TYR 198 198 198  TYR TYR CCC . n 
F 3 199 ALA 199 199 199  ALA ALA CCC . n 
F 3 200 CYS 200 200 200  CYS CYS CCC . n 
F 3 201 GLU 201 201 201  GLU GLU CCC . n 
F 3 202 VAL 202 202 202  VAL VAL CCC . n 
F 3 203 THR 203 203 203  THR THR CCC . n 
F 3 204 HIS 204 204 204  HIS HIS CCC . n 
F 3 205 GLN 205 205 205  GLN GLN CCC . n 
F 3 206 GLY 206 206 206  GLY GLY CCC . n 
F 3 207 LEU 207 207 207  LEU LEU CCC . n 
F 3 208 SER 208 208 208  SER SER CCC . n 
F 3 209 SER 209 209 209  SER SER CCC . n 
F 3 210 PRO 210 210 210  PRO PRO CCC . n 
F 3 211 VAL 211 211 211  VAL VAL CCC . n 
F 3 212 THR 212 212 212  THR THR CCC . n 
F 3 213 LYS 213 213 213  LYS LYS CCC . n 
F 3 214 SER 214 214 214  SER SER CCC . n 
F 3 215 PHE 215 215 215  PHE PHE CCC . n 
F 3 216 ASN 216 216 216  ASN ASN CCC . n 
F 3 217 ARG 217 217 217  ARG ARG CCC . n 
F 3 218 GLY 218 218 218  GLY GLY CCC . n 
F 3 219 GLU 219 219 219  GLU GLU CCC . n 
F 3 220 CYS 220 220 ?    ?   ?   CCC . n 
F 3 221 SER 221 221 ?    ?   ?   CCC . n 
G 1 1   ARG 1   319 ?    ?   ?   DDD . n 
G 1 2   VAL 2   320 ?    ?   ?   DDD . n 
G 1 3   GLN 3   321 ?    ?   ?   DDD . n 
G 1 4   PRO 4   322 ?    ?   ?   DDD . n 
G 1 5   THR 5   323 ?    ?   ?   DDD . n 
G 1 6   GLU 6   324 ?    ?   ?   DDD . n 
G 1 7   SER 7   325 ?    ?   ?   DDD . n 
G 1 8   ILE 8   326 ?    ?   ?   DDD . n 
G 1 9   VAL 9   327 ?    ?   ?   DDD . n 
G 1 10  ARG 10  328 ?    ?   ?   DDD . n 
G 1 11  PHE 11  329 ?    ?   ?   DDD . n 
G 1 12  PRO 12  330 ?    ?   ?   DDD . n 
G 1 13  ASN 13  331 ?    ?   ?   DDD . n 
G 1 14  ILE 14  332 ?    ?   ?   DDD . n 
G 1 15  THR 15  333 333  THR THR DDD . n 
G 1 16  ASN 16  334 334  ASN ASN DDD . n 
G 1 17  LEU 17  335 335  LEU LEU DDD . n 
G 1 18  CYS 18  336 336  CYS CYS DDD . n 
G 1 19  PRO 19  337 337  PRO PRO DDD . n 
G 1 20  PHE 20  338 338  PHE PHE DDD . n 
G 1 21  GLY 21  339 339  GLY GLY DDD . n 
G 1 22  GLU 22  340 340  GLU GLU DDD . n 
G 1 23  VAL 23  341 341  VAL VAL DDD . n 
G 1 24  PHE 24  342 342  PHE PHE DDD . n 
G 1 25  ASN 25  343 343  ASN ASN DDD . n 
G 1 26  ALA 26  344 344  ALA ALA DDD . n 
G 1 27  THR 27  345 345  THR THR DDD . n 
G 1 28  ARG 28  346 346  ARG ARG DDD . n 
G 1 29  PHE 29  347 347  PHE PHE DDD . n 
G 1 30  ALA 30  348 348  ALA ALA DDD . n 
G 1 31  SER 31  349 349  SER SER DDD . n 
G 1 32  VAL 32  350 350  VAL VAL DDD . n 
G 1 33  TYR 33  351 351  TYR TYR DDD . n 
G 1 34  ALA 34  352 352  ALA ALA DDD . n 
G 1 35  TRP 35  353 353  TRP TRP DDD . n 
G 1 36  ASN 36  354 354  ASN ASN DDD . n 
G 1 37  ARG 37  355 355  ARG ARG DDD . n 
G 1 38  LYS 38  356 356  LYS LYS DDD . n 
G 1 39  ARG 39  357 357  ARG ARG DDD . n 
G 1 40  ILE 40  358 358  ILE ILE DDD . n 
G 1 41  SER 41  359 359  SER SER DDD . n 
G 1 42  ASN 42  360 360  ASN ASN DDD . n 
G 1 43  CYS 43  361 361  CYS CYS DDD . n 
G 1 44  VAL 44  362 362  VAL VAL DDD . n 
G 1 45  ALA 45  363 363  ALA ALA DDD . n 
G 1 46  ASP 46  364 364  ASP ASP DDD . n 
G 1 47  TYR 47  365 365  TYR TYR DDD . n 
G 1 48  SER 48  366 366  SER SER DDD . n 
G 1 49  VAL 49  367 367  VAL VAL DDD . n 
G 1 50  LEU 50  368 368  LEU LEU DDD . n 
G 1 51  TYR 51  369 369  TYR TYR DDD . n 
G 1 52  ASN 52  370 370  ASN ASN DDD . n 
G 1 53  SER 53  371 371  SER SER DDD . n 
G 1 54  ALA 54  372 372  ALA ALA DDD . n 
G 1 55  SER 55  373 373  SER SER DDD . n 
G 1 56  PHE 56  374 374  PHE PHE DDD . n 
G 1 57  SER 57  375 375  SER SER DDD . n 
G 1 58  THR 58  376 376  THR THR DDD . n 
G 1 59  PHE 59  377 377  PHE PHE DDD . n 
G 1 60  LYS 60  378 378  LYS LYS DDD . n 
G 1 61  CYS 61  379 379  CYS CYS DDD . n 
G 1 62  TYR 62  380 380  TYR TYR DDD . n 
G 1 63  GLY 63  381 381  GLY GLY DDD . n 
G 1 64  VAL 64  382 382  VAL VAL DDD . n 
G 1 65  SER 65  383 383  SER SER DDD . n 
G 1 66  PRO 66  384 384  PRO PRO DDD . n 
G 1 67  THR 67  385 385  THR THR DDD . n 
G 1 68  LYS 68  386 386  LYS LYS DDD . n 
G 1 69  LEU 69  387 387  LEU LEU DDD . n 
G 1 70  ASN 70  388 388  ASN ASN DDD . n 
G 1 71  ASP 71  389 389  ASP ASP DDD . n 
G 1 72  LEU 72  390 390  LEU LEU DDD . n 
G 1 73  CYS 73  391 391  CYS CYS DDD . n 
G 1 74  PHE 74  392 392  PHE PHE DDD . n 
G 1 75  THR 75  393 393  THR THR DDD . n 
G 1 76  ASN 76  394 394  ASN ASN DDD . n 
G 1 77  VAL 77  395 395  VAL VAL DDD . n 
G 1 78  TYR 78  396 396  TYR TYR DDD . n 
G 1 79  ALA 79  397 397  ALA ALA DDD . n 
G 1 80  ASP 80  398 398  ASP ASP DDD . n 
G 1 81  SER 81  399 399  SER SER DDD . n 
G 1 82  PHE 82  400 400  PHE PHE DDD . n 
G 1 83  VAL 83  401 401  VAL VAL DDD . n 
G 1 84  ILE 84  402 402  ILE ILE DDD . n 
G 1 85  ARG 85  403 403  ARG ARG DDD . n 
G 1 86  GLY 86  404 404  GLY GLY DDD . n 
G 1 87  ASP 87  405 405  ASP ASP DDD . n 
G 1 88  GLU 88  406 406  GLU GLU DDD . n 
G 1 89  VAL 89  407 407  VAL VAL DDD . n 
G 1 90  ARG 90  408 408  ARG ARG DDD . n 
G 1 91  GLN 91  409 409  GLN GLN DDD . n 
G 1 92  ILE 92  410 410  ILE ILE DDD . n 
G 1 93  ALA 93  411 411  ALA ALA DDD . n 
G 1 94  PRO 94  412 412  PRO PRO DDD . n 
G 1 95  GLY 95  413 413  GLY GLY DDD . n 
G 1 96  GLN 96  414 414  GLN GLN DDD . n 
G 1 97  THR 97  415 415  THR THR DDD . n 
G 1 98  GLY 98  416 416  GLY GLY DDD . n 
G 1 99  LYS 99  417 417  LYS LYS DDD . n 
G 1 100 ILE 100 418 418  ILE ILE DDD . n 
G 1 101 ALA 101 419 419  ALA ALA DDD . n 
G 1 102 ASP 102 420 420  ASP ASP DDD . n 
G 1 103 TYR 103 421 421  TYR TYR DDD . n 
G 1 104 ASN 104 422 422  ASN ASN DDD . n 
G 1 105 TYR 105 423 423  TYR TYR DDD . n 
G 1 106 LYS 106 424 424  LYS LYS DDD . n 
G 1 107 LEU 107 425 425  LEU LEU DDD . n 
G 1 108 PRO 108 426 426  PRO PRO DDD . n 
G 1 109 ASP 109 427 427  ASP ASP DDD . n 
G 1 110 ASP 110 428 428  ASP ASP DDD . n 
G 1 111 PHE 111 429 429  PHE PHE DDD . n 
G 1 112 THR 112 430 430  THR THR DDD . n 
G 1 113 GLY 113 431 431  GLY GLY DDD . n 
G 1 114 CYS 114 432 432  CYS CYS DDD . n 
G 1 115 VAL 115 433 433  VAL VAL DDD . n 
G 1 116 ILE 116 434 434  ILE ILE DDD . n 
G 1 117 ALA 117 435 435  ALA ALA DDD . n 
G 1 118 TRP 118 436 436  TRP TRP DDD . n 
G 1 119 ASN 119 437 437  ASN ASN DDD . n 
G 1 120 SER 120 438 438  SER SER DDD . n 
G 1 121 ASN 121 439 439  ASN ASN DDD . n 
G 1 122 ASN 122 440 440  ASN ASN DDD . n 
G 1 123 LEU 123 441 441  LEU LEU DDD . n 
G 1 124 ASP 124 442 442  ASP ASP DDD . n 
G 1 125 SER 125 443 443  SER SER DDD . n 
G 1 126 LYS 126 444 444  LYS LYS DDD . n 
G 1 127 VAL 127 445 445  VAL VAL DDD . n 
G 1 128 GLY 128 446 446  GLY GLY DDD . n 
G 1 129 GLY 129 447 447  GLY GLY DDD . n 
G 1 130 ASN 130 448 448  ASN ASN DDD . n 
G 1 131 TYR 131 449 449  TYR TYR DDD . n 
G 1 132 ASN 132 450 450  ASN ASN DDD . n 
G 1 133 TYR 133 451 451  TYR TYR DDD . n 
G 1 134 LEU 134 452 452  LEU LEU DDD . n 
G 1 135 TYR 135 453 453  TYR TYR DDD . n 
G 1 136 ARG 136 454 454  ARG ARG DDD . n 
G 1 137 LEU 137 455 455  LEU LEU DDD . n 
G 1 138 PHE 138 456 456  PHE PHE DDD . n 
G 1 139 ARG 139 457 457  ARG ARG DDD . n 
G 1 140 LYS 140 458 458  LYS LYS DDD . n 
G 1 141 SER 141 459 459  SER SER DDD . n 
G 1 142 ASN 142 460 460  ASN ASN DDD . n 
G 1 143 LEU 143 461 461  LEU LEU DDD . n 
G 1 144 LYS 144 462 462  LYS LYS DDD . n 
G 1 145 PRO 145 463 463  PRO PRO DDD . n 
G 1 146 PHE 146 464 464  PHE PHE DDD . n 
G 1 147 GLU 147 465 465  GLU GLU DDD . n 
G 1 148 ARG 148 466 466  ARG ARG DDD . n 
G 1 149 ASP 149 467 467  ASP ASP DDD . n 
G 1 150 ILE 150 468 468  ILE ILE DDD . n 
G 1 151 SER 151 469 469  SER SER DDD . n 
G 1 152 THR 152 470 470  THR THR DDD . n 
G 1 153 GLU 153 471 471  GLU GLU DDD . n 
G 1 154 ILE 154 472 472  ILE ILE DDD . n 
G 1 155 TYR 155 473 473  TYR TYR DDD . n 
G 1 156 GLN 156 474 474  GLN GLN DDD . n 
G 1 157 ALA 157 475 475  ALA ALA DDD . n 
G 1 158 GLY 158 476 476  GLY GLY DDD . n 
G 1 159 SER 159 477 477  SER SER DDD . n 
G 1 160 THR 160 478 478  THR THR DDD . n 
G 1 161 PRO 161 479 479  PRO PRO DDD . n 
G 1 162 CYS 162 480 480  CYS CYS DDD . n 
G 1 163 ASN 163 481 481  ASN ASN DDD . n 
G 1 164 GLY 164 482 482  GLY GLY DDD . n 
G 1 165 VAL 165 483 483  VAL VAL DDD . n 
G 1 166 GLU 166 484 484  GLU GLU DDD . n 
G 1 167 GLY 167 485 485  GLY GLY DDD . n 
G 1 168 PHE 168 486 486  PHE PHE DDD . n 
G 1 169 ASN 169 487 487  ASN ASN DDD . n 
G 1 170 CYS 170 488 488  CYS CYS DDD . n 
G 1 171 TYR 171 489 489  TYR TYR DDD . n 
G 1 172 PHE 172 490 490  PHE PHE DDD . n 
G 1 173 PRO 173 491 491  PRO PRO DDD . n 
G 1 174 LEU 174 492 492  LEU LEU DDD . n 
G 1 175 GLN 175 493 493  GLN GLN DDD . n 
G 1 176 SER 176 494 494  SER SER DDD . n 
G 1 177 TYR 177 495 495  TYR TYR DDD . n 
G 1 178 GLY 178 496 496  GLY GLY DDD . n 
G 1 179 PHE 179 497 497  PHE PHE DDD . n 
G 1 180 GLN 180 498 498  GLN GLN DDD . n 
G 1 181 PRO 181 499 499  PRO PRO DDD . n 
G 1 182 THR 182 500 500  THR THR DDD . n 
G 1 183 ASN 183 501 501  ASN ASN DDD . n 
G 1 184 GLY 184 502 502  GLY GLY DDD . n 
G 1 185 VAL 185 503 503  VAL VAL DDD . n 
G 1 186 GLY 186 504 504  GLY GLY DDD . n 
G 1 187 TYR 187 505 505  TYR TYR DDD . n 
G 1 188 GLN 188 506 506  GLN GLN DDD . n 
G 1 189 PRO 189 507 507  PRO PRO DDD . n 
G 1 190 TYR 190 508 508  TYR TYR DDD . n 
G 1 191 ARG 191 509 509  ARG ARG DDD . n 
G 1 192 VAL 192 510 510  VAL VAL DDD . n 
G 1 193 VAL 193 511 511  VAL VAL DDD . n 
G 1 194 VAL 194 512 512  VAL VAL DDD . n 
G 1 195 LEU 195 513 513  LEU LEU DDD . n 
G 1 196 SER 196 514 514  SER SER DDD . n 
G 1 197 PHE 197 515 515  PHE PHE DDD . n 
G 1 198 GLU 198 516 516  GLU GLU DDD . n 
G 1 199 LEU 199 517 517  LEU LEU DDD . n 
G 1 200 LEU 200 518 518  LEU LEU DDD . n 
G 1 201 HIS 201 519 519  HIS HIS DDD . n 
G 1 202 ALA 202 520 520  ALA ALA DDD . n 
G 1 203 PRO 203 521 521  PRO PRO DDD . n 
G 1 204 ALA 204 522 522  ALA ALA DDD . n 
G 1 205 THR 205 523 523  THR THR DDD . n 
G 1 206 VAL 206 524 524  VAL VAL DDD . n 
G 1 207 CYS 207 525 525  CYS CYS DDD . n 
G 1 208 GLY 208 526 526  GLY GLY DDD . n 
G 1 209 PRO 209 527 527  PRO PRO DDD . n 
G 1 210 LYS 210 528 528  LYS LYS DDD . n 
G 1 211 LYS 211 529 ?    ?   ?   DDD . n 
G 1 212 SER 212 530 ?    ?   ?   DDD . n 
G 1 213 THR 213 531 ?    ?   ?   DDD . n 
G 1 214 ASN 214 532 ?    ?   ?   DDD . n 
G 1 215 LEU 215 533 ?    ?   ?   DDD . n 
G 1 216 VAL 216 534 ?    ?   ?   DDD . n 
G 1 217 LYS 217 535 ?    ?   ?   DDD . n 
G 1 218 ASN 218 536 ?    ?   ?   DDD . n 
G 1 219 LYS 219 537 ?    ?   ?   DDD . n 
G 1 220 CYS 220 538 ?    ?   ?   DDD . n 
G 1 221 VAL 221 539 ?    ?   ?   DDD . n 
G 1 222 ASN 222 540 ?    ?   ?   DDD . n 
G 1 223 PHE 223 541 ?    ?   ?   DDD . n 
G 1 224 SER 224 542 ?    ?   ?   DDD . n 
G 1 225 GLY 225 543 ?    ?   ?   DDD . n 
G 1 226 HIS 226 544 ?    ?   ?   DDD . n 
G 1 227 HIS 227 545 ?    ?   ?   DDD . n 
G 1 228 HIS 228 546 ?    ?   ?   DDD . n 
G 1 229 HIS 229 547 ?    ?   ?   DDD . n 
G 1 230 HIS 230 548 ?    ?   ?   DDD . n 
G 1 231 HIS 231 549 ?    ?   ?   DDD . n 
H 2 1   GLN 1   1   1    GLN GLN FFF . n 
H 2 2   MET 2   2   2    MET MET FFF . n 
H 2 3   GLN 3   3   3    GLN GLN FFF . n 
H 2 4   LEU 4   4   4    LEU LEU FFF . n 
H 2 5   VAL 5   5   5    VAL VAL FFF . n 
H 2 6   GLN 6   6   6    GLN GLN FFF . n 
H 2 7   SER 7   7   7    SER SER FFF . n 
H 2 8   GLY 8   8   8    GLY GLY FFF . n 
H 2 9   THR 9   9   9    THR THR FFF . n 
H 2 10  GLU 10  10  10   GLU GLU FFF . n 
H 2 11  VAL 11  11  11   VAL VAL FFF . n 
H 2 12  LYS 12  12  12   LYS LYS FFF . n 
H 2 13  LYS 13  13  13   LYS LYS FFF . n 
H 2 14  PRO 14  14  14   PRO PRO FFF . n 
H 2 15  GLY 15  15  15   GLY GLY FFF . n 
H 2 16  GLU 16  16  16   GLU GLU FFF . n 
H 2 17  SER 17  17  17   SER SER FFF . n 
H 2 18  LEU 18  18  18   LEU LEU FFF . n 
H 2 19  LYS 19  19  19   LYS LYS FFF . n 
H 2 20  ILE 20  20  20   ILE ILE FFF . n 
H 2 21  SER 21  21  21   SER SER FFF . n 
H 2 22  CYS 22  22  22   CYS CYS FFF . n 
H 2 23  LYS 23  23  23   LYS LYS FFF . n 
H 2 24  GLY 24  24  24   GLY GLY FFF . n 
H 2 25  SER 25  25  25   SER SER FFF . n 
H 2 26  GLY 26  26  26   GLY GLY FFF . n 
H 2 27  TYR 27  27  27   TYR TYR FFF . n 
H 2 28  GLY 28  28  28   GLY GLY FFF . n 
H 2 29  PHE 29  29  29   PHE PHE FFF . n 
H 2 30  ILE 30  30  30   ILE ILE FFF . n 
H 2 31  THR 31  31  31   THR THR FFF . n 
H 2 32  TYR 32  32  32   TYR TYR FFF . n 
H 2 33  TRP 33  33  33   TRP TRP FFF . n 
H 2 34  ILE 34  34  34   ILE ILE FFF . n 
H 2 35  GLY 35  35  35   GLY GLY FFF . n 
H 2 36  TRP 36  36  36   TRP TRP FFF . n 
H 2 37  VAL 37  37  37   VAL VAL FFF . n 
H 2 38  ARG 38  38  38   ARG ARG FFF . n 
H 2 39  GLN 39  39  39   GLN GLN FFF . n 
H 2 40  MET 40  40  40   MET MET FFF . n 
H 2 41  PRO 41  41  41   PRO PRO FFF . n 
H 2 42  GLY 42  42  42   GLY GLY FFF . n 
H 2 43  LYS 43  43  43   LYS LYS FFF . n 
H 2 44  GLY 44  44  44   GLY GLY FFF . n 
H 2 45  LEU 45  45  45   LEU LEU FFF . n 
H 2 46  GLU 46  46  46   GLU GLU FFF . n 
H 2 47  TRP 47  47  47   TRP TRP FFF . n 
H 2 48  MET 48  48  48   MET MET FFF . n 
H 2 49  GLY 49  49  49   GLY GLY FFF . n 
H 2 50  ILE 50  50  50   ILE ILE FFF . n 
H 2 51  ILE 51  51  51   ILE ILE FFF . n 
H 2 52  TYR 52  52  52   TYR TYR FFF . n 
H 2 53  PRO 53  53  52A  PRO PRO FFF . n 
H 2 54  GLY 54  54  53   GLY GLY FFF . n 
H 2 55  ASP 55  55  54   ASP ASP FFF . n 
H 2 56  SER 56  56  55   SER SER FFF . n 
H 2 57  GLU 57  57  56   GLU GLU FFF . n 
H 2 58  THR 58  58  57   THR THR FFF . n 
H 2 59  ARG 59  59  58   ARG ARG FFF . n 
H 2 60  TYR 60  60  59   TYR TYR FFF . n 
H 2 61  SER 61  61  60   SER SER FFF . n 
H 2 62  PRO 62  62  61   PRO PRO FFF . n 
H 2 63  SER 63  63  62   SER SER FFF . n 
H 2 64  PHE 64  64  63   PHE PHE FFF . n 
H 2 65  GLN 65  65  64   GLN GLN FFF . n 
H 2 66  GLY 66  66  65   GLY GLY FFF . n 
H 2 67  GLN 67  67  66   GLN GLN FFF . n 
H 2 68  VAL 68  68  67   VAL VAL FFF . n 
H 2 69  THR 69  69  68   THR THR FFF . n 
H 2 70  ILE 70  70  69   ILE ILE FFF . n 
H 2 71  SER 71  71  70   SER SER FFF . n 
H 2 72  ALA 72  72  71   ALA ALA FFF . n 
H 2 73  ASP 73  73  72   ASP ASP FFF . n 
H 2 74  LYS 74  74  73   LYS LYS FFF . n 
H 2 75  SER 75  75  74   SER SER FFF . n 
H 2 76  ILE 76  76  75   ILE ILE FFF . n 
H 2 77  ASN 77  77  76   ASN ASN FFF . n 
H 2 78  THR 78  78  77   THR THR FFF . n 
H 2 79  ALA 79  79  78   ALA ALA FFF . n 
H 2 80  TYR 80  80  79   TYR TYR FFF . n 
H 2 81  LEU 81  81  80   LEU LEU FFF . n 
H 2 82  GLN 82  82  81   GLN GLN FFF . n 
H 2 83  TRP 83  83  82   TRP TRP FFF . n 
H 2 84  SER 84  84  82A  SER SER FFF . n 
H 2 85  SER 85  85  82B  SER SER FFF . n 
H 2 86  LEU 86  86  82C  LEU LEU FFF . n 
H 2 87  LYS 87  87  83   LYS LYS FFF . n 
H 2 88  ALA 88  88  84   ALA ALA FFF . n 
H 2 89  SER 89  89  85   SER SER FFF . n 
H 2 90  ASP 90  90  86   ASP ASP FFF . n 
H 2 91  THR 91  91  87   THR THR FFF . n 
H 2 92  ALA 92  92  88   ALA ALA FFF . n 
H 2 93  ILE 93  93  89   ILE ILE FFF . n 
H 2 94  TYR 94  94  90   TYR TYR FFF . n 
H 2 95  TYR 95  95  91   TYR TYR FFF . n 
H 2 96  CYS 96  96  92   CYS CYS FFF . n 
H 2 97  ALA 97  97  93   ALA ALA FFF . n 
H 2 98  GLY 98  98  94   GLY GLY FFF . n 
H 2 99  GLY 99  99  95   GLY GLY FFF . n 
H 2 100 SER 100 100 96   SER SER FFF . n 
H 2 101 GLY 101 101 97   GLY GLY FFF . n 
H 2 102 ILE 102 102 98   ILE ILE FFF . n 
H 2 103 SER 103 103 99   SER SER FFF . n 
H 2 104 THR 104 104 100  THR THR FFF . n 
H 2 105 PRO 105 105 100A PRO PRO FFF . n 
H 2 106 MET 106 106 100B MET MET FFF . n 
H 2 107 ASP 107 107 101  ASP ASP FFF . n 
H 2 108 VAL 108 108 102  VAL VAL FFF . n 
H 2 109 TRP 109 109 103  TRP TRP FFF . n 
H 2 110 GLY 110 110 104  GLY GLY FFF . n 
H 2 111 GLN 111 111 105  GLN GLN FFF . n 
H 2 112 GLY 112 112 106  GLY GLY FFF . n 
H 2 113 THR 113 113 107  THR THR FFF . n 
H 2 114 THR 114 114 108  THR THR FFF . n 
H 2 115 VAL 115 115 109  VAL VAL FFF . n 
H 2 116 THR 116 116 110  THR THR FFF . n 
H 2 117 VAL 117 117 111  VAL VAL FFF . n 
H 2 118 SER 118 118 112  SER SER FFF . n 
H 2 119 SER 119 119 113  SER SER FFF . n 
H 2 120 ALA 120 120 114  ALA ALA FFF . n 
H 2 121 SER 121 121 115  SER SER FFF . n 
H 2 122 THR 122 122 116  THR THR FFF . n 
H 2 123 LYS 123 123 117  LYS LYS FFF . n 
H 2 124 GLY 124 124 118  GLY GLY FFF . n 
H 2 125 PRO 125 125 119  PRO PRO FFF . n 
H 2 126 SER 126 126 120  SER SER FFF . n 
H 2 127 VAL 127 127 121  VAL VAL FFF . n 
H 2 128 PHE 128 128 122  PHE PHE FFF . n 
H 2 129 PRO 129 129 123  PRO PRO FFF . n 
H 2 130 LEU 130 130 124  LEU LEU FFF . n 
H 2 131 ALA 131 131 125  ALA ALA FFF . n 
H 2 132 PRO 132 132 126  PRO PRO FFF . n 
H 2 133 SER 133 133 127  SER SER FFF . n 
H 2 134 SER 134 134 128  SER SER FFF . n 
H 2 135 LYS 135 135 129  LYS LYS FFF . n 
H 2 136 SER 136 136 130  SER SER FFF . n 
H 2 137 THR 137 137 131  THR THR FFF . n 
H 2 138 SER 138 138 132  SER SER FFF . n 
H 2 139 GLY 139 139 133  GLY GLY FFF . n 
H 2 140 GLY 140 140 134  GLY GLY FFF . n 
H 2 141 THR 141 141 135  THR THR FFF . n 
H 2 142 ALA 142 142 136  ALA ALA FFF . n 
H 2 143 ALA 143 143 137  ALA ALA FFF . n 
H 2 144 LEU 144 144 138  LEU LEU FFF . n 
H 2 145 GLY 145 145 139  GLY GLY FFF . n 
H 2 146 CYS 146 146 140  CYS CYS FFF . n 
H 2 147 LEU 147 147 141  LEU LEU FFF . n 
H 2 148 VAL 148 148 142  VAL VAL FFF . n 
H 2 149 LYS 149 149 143  LYS LYS FFF . n 
H 2 150 ASP 150 150 144  ASP ASP FFF . n 
H 2 151 TYR 151 151 145  TYR TYR FFF . n 
H 2 152 PHE 152 152 146  PHE PHE FFF . n 
H 2 153 PRO 153 153 147  PRO PRO FFF . n 
H 2 154 GLU 154 154 148  GLU GLU FFF . n 
H 2 155 PRO 155 155 149  PRO PRO FFF . n 
H 2 156 VAL 156 156 150  VAL VAL FFF . n 
H 2 157 THR 157 157 151  THR THR FFF . n 
H 2 158 VAL 158 158 152  VAL VAL FFF . n 
H 2 159 SER 159 159 153  SER SER FFF . n 
H 2 160 TRP 160 160 154  TRP TRP FFF . n 
H 2 161 ASN 161 161 155  ASN ASN FFF . n 
H 2 162 SER 162 162 156  SER SER FFF . n 
H 2 163 GLY 163 163 157  GLY GLY FFF . n 
H 2 164 ALA 164 164 158  ALA ALA FFF . n 
H 2 165 LEU 165 165 159  LEU LEU FFF . n 
H 2 166 THR 166 166 160  THR THR FFF . n 
H 2 167 SER 167 167 161  SER SER FFF . n 
H 2 168 GLY 168 168 162  GLY GLY FFF . n 
H 2 169 VAL 169 169 163  VAL VAL FFF . n 
H 2 170 HIS 170 170 164  HIS HIS FFF . n 
H 2 171 THR 171 171 165  THR THR FFF . n 
H 2 172 PHE 172 172 166  PHE PHE FFF . n 
H 2 173 PRO 173 173 167  PRO PRO FFF . n 
H 2 174 ALA 174 174 168  ALA ALA FFF . n 
H 2 175 VAL 175 175 169  VAL VAL FFF . n 
H 2 176 LEU 176 176 170  LEU LEU FFF . n 
H 2 177 GLN 177 177 171  GLN GLN FFF . n 
H 2 178 SER 178 178 172  SER SER FFF . n 
H 2 179 SER 179 179 173  SER SER FFF . n 
H 2 180 GLY 180 180 174  GLY GLY FFF . n 
H 2 181 LEU 181 181 175  LEU LEU FFF . n 
H 2 182 TYR 182 182 176  TYR TYR FFF . n 
H 2 183 SER 183 183 177  SER SER FFF . n 
H 2 184 LEU 184 184 178  LEU LEU FFF . n 
H 2 185 SER 185 185 179  SER SER FFF . n 
H 2 186 SER 186 186 180  SER SER FFF . n 
H 2 187 VAL 187 187 181  VAL VAL FFF . n 
H 2 188 VAL 188 188 182  VAL VAL FFF . n 
H 2 189 THR 189 189 183  THR THR FFF . n 
H 2 190 VAL 190 190 184  VAL VAL FFF . n 
H 2 191 PRO 191 191 185  PRO PRO FFF . n 
H 2 192 SER 192 192 186  SER SER FFF . n 
H 2 193 SER 193 193 187  SER SER FFF . n 
H 2 194 SER 194 194 188  SER SER FFF . n 
H 2 195 LEU 195 195 189  LEU LEU FFF . n 
H 2 196 GLY 196 196 190  GLY GLY FFF . n 
H 2 197 THR 197 197 191  THR THR FFF . n 
H 2 198 GLN 198 198 192  GLN GLN FFF . n 
H 2 199 THR 199 199 193  THR THR FFF . n 
H 2 200 TYR 200 200 194  TYR TYR FFF . n 
H 2 201 ILE 201 201 195  ILE ILE FFF . n 
H 2 202 CYS 202 202 196  CYS CYS FFF . n 
H 2 203 ASN 203 203 197  ASN ASN FFF . n 
H 2 204 VAL 204 204 198  VAL VAL FFF . n 
H 2 205 ASN 205 205 199  ASN ASN FFF . n 
H 2 206 HIS 206 206 200  HIS HIS FFF . n 
H 2 207 LYS 207 207 201  LYS LYS FFF . n 
H 2 208 PRO 208 208 202  PRO PRO FFF . n 
H 2 209 SER 209 209 203  SER SER FFF . n 
H 2 210 ASN 210 210 204  ASN ASN FFF . n 
H 2 211 THR 211 211 205  THR THR FFF . n 
H 2 212 LYS 212 212 206  LYS LYS FFF . n 
H 2 213 VAL 213 213 207  VAL VAL FFF . n 
H 2 214 ASP 214 214 208  ASP ASP FFF . n 
H 2 215 LYS 215 215 209  LYS LYS FFF . n 
H 2 216 LYS 216 216 210  LYS LYS FFF . n 
H 2 217 VAL 217 217 211  VAL VAL FFF . n 
H 2 218 GLU 218 218 212  GLU GLU FFF . n 
H 2 219 PRO 219 219 213  PRO PRO FFF . n 
H 2 220 LYS 220 220 214  LYS LYS FFF . n 
H 2 221 SER 221 221 215  SER SER FFF . n 
H 2 222 CYS 222 222 216  CYS CYS FFF . n 
I 3 1   ASP 1   1   1    ASP ASP GGG . n 
I 3 2   ILE 2   2   2    ILE ILE GGG . n 
I 3 3   GLN 3   3   3    GLN GLN GGG . n 
I 3 4   LEU 4   4   4    LEU LEU GGG . n 
I 3 5   THR 5   5   5    THR THR GGG . n 
I 3 6   GLN 6   6   6    GLN GLN GGG . n 
I 3 7   SER 7   7   7    SER SER GGG . n 
I 3 8   PRO 8   8   8    PRO PRO GGG . n 
I 3 9   ASP 9   9   9    ASP ASP GGG . n 
I 3 10  SER 10  10  10   SER SER GGG . n 
I 3 11  LEU 11  11  11   LEU LEU GGG . n 
I 3 12  ALA 12  12  12   ALA ALA GGG . n 
I 3 13  VAL 13  13  13   VAL VAL GGG . n 
I 3 14  SER 14  14  14   SER SER GGG . n 
I 3 15  LEU 15  15  15   LEU LEU GGG . n 
I 3 16  GLY 16  16  16   GLY GLY GGG . n 
I 3 17  GLU 17  17  17   GLU GLU GGG . n 
I 3 18  ARG 18  18  18   ARG ARG GGG . n 
I 3 19  ALA 19  19  19   ALA ALA GGG . n 
I 3 20  THR 20  20  20   THR THR GGG . n 
I 3 21  ILE 21  21  21   ILE ILE GGG . n 
I 3 22  ASN 22  22  22   ASN ASN GGG . n 
I 3 23  CYS 23  23  23   CYS CYS GGG . n 
I 3 24  LYS 24  24  24   LYS LYS GGG . n 
I 3 25  SER 25  25  25   SER SER GGG . n 
I 3 26  SER 26  26  26   SER SER GGG . n 
I 3 27  GLN 27  27  27   GLN GLN GGG . n 
I 3 28  SER 28  28  28   SER SER GGG . n 
I 3 29  VAL 29  29  29   VAL VAL GGG . n 
I 3 30  LEU 30  30  30   LEU LEU GGG . n 
I 3 31  TYR 31  31  31   TYR TYR GGG . n 
I 3 32  SER 32  32  32   SER SER GGG . n 
I 3 33  SER 33  33  33   SER SER GGG . n 
I 3 34  ILE 34  34  34   ILE ILE GGG . n 
I 3 35  ASN 35  35  35   ASN ASN GGG . n 
I 3 36  LYS 36  36  36   LYS LYS GGG . n 
I 3 37  ASN 37  37  37   ASN ASN GGG . n 
I 3 38  TYR 38  38  38   TYR TYR GGG . n 
I 3 39  LEU 39  39  39   LEU LEU GGG . n 
I 3 40  ALA 40  40  40   ALA ALA GGG . n 
I 3 41  TRP 41  41  41   TRP TRP GGG . n 
I 3 42  TYR 42  42  42   TYR TYR GGG . n 
I 3 43  GLN 43  43  43   GLN GLN GGG . n 
I 3 44  GLN 44  44  44   GLN GLN GGG . n 
I 3 45  LYS 45  45  45   LYS LYS GGG . n 
I 3 46  PRO 46  46  46   PRO PRO GGG . n 
I 3 47  GLY 47  47  47   GLY GLY GGG . n 
I 3 48  GLN 48  48  48   GLN GLN GGG . n 
I 3 49  PRO 49  49  49   PRO PRO GGG . n 
I 3 50  PRO 50  50  50   PRO PRO GGG . n 
I 3 51  LYS 51  51  51   LYS LYS GGG . n 
I 3 52  LEU 52  52  52   LEU LEU GGG . n 
I 3 53  LEU 53  53  53   LEU LEU GGG . n 
I 3 54  ILE 54  54  54   ILE ILE GGG . n 
I 3 55  TYR 55  55  55   TYR TYR GGG . n 
I 3 56  TRP 56  56  56   TRP TRP GGG . n 
I 3 57  ALA 57  57  57   ALA ALA GGG . n 
I 3 58  SER 58  58  58   SER SER GGG . n 
I 3 59  THR 59  59  59   THR THR GGG . n 
I 3 60  ARG 60  60  60   ARG ARG GGG . n 
I 3 61  GLU 61  61  61   GLU GLU GGG . n 
I 3 62  SER 62  62  62   SER SER GGG . n 
I 3 63  GLY 63  63  63   GLY GLY GGG . n 
I 3 64  VAL 64  64  64   VAL VAL GGG . n 
I 3 65  PRO 65  65  65   PRO PRO GGG . n 
I 3 66  ASP 66  66  66   ASP ASP GGG . n 
I 3 67  ARG 67  67  67   ARG ARG GGG . n 
I 3 68  PHE 68  68  68   PHE PHE GGG . n 
I 3 69  SER 69  69  69   SER SER GGG . n 
I 3 70  GLY 70  70  70   GLY GLY GGG . n 
I 3 71  SER 71  71  71   SER SER GGG . n 
I 3 72  GLY 72  72  72   GLY GLY GGG . n 
I 3 73  SER 73  73  73   SER SER GGG . n 
I 3 74  GLY 74  74  74   GLY GLY GGG . n 
I 3 75  THR 75  75  75   THR THR GGG . n 
I 3 76  ASP 76  76  76   ASP ASP GGG . n 
I 3 77  PHE 77  77  77   PHE PHE GGG . n 
I 3 78  THR 78  78  78   THR THR GGG . n 
I 3 79  LEU 79  79  79   LEU LEU GGG . n 
I 3 80  THR 80  80  80   THR THR GGG . n 
I 3 81  ILE 81  81  81   ILE ILE GGG . n 
I 3 82  SER 82  82  82   SER SER GGG . n 
I 3 83  SER 83  83  83   SER SER GGG . n 
I 3 84  LEU 84  84  84   LEU LEU GGG . n 
I 3 85  GLN 85  85  85   GLN GLN GGG . n 
I 3 86  ALA 86  86  86   ALA ALA GGG . n 
I 3 87  GLU 87  87  87   GLU GLU GGG . n 
I 3 88  ASP 88  88  88   ASP ASP GGG . n 
I 3 89  VAL 89  89  89   VAL VAL GGG . n 
I 3 90  ALA 90  90  90   ALA ALA GGG . n 
I 3 91  VAL 91  91  91   VAL VAL GGG . n 
I 3 92  TYR 92  92  92   TYR TYR GGG . n 
I 3 93  TYR 93  93  93   TYR TYR GGG . n 
I 3 94  CYS 94  94  94   CYS CYS GGG . n 
I 3 95  GLN 95  95  95   GLN GLN GGG . n 
I 3 96  GLN 96  96  96   GLN GLN GGG . n 
I 3 97  TYR 97  97  97   TYR TYR GGG . n 
I 3 98  TYR 98  98  98   TYR TYR GGG . n 
I 3 99  SER 99  99  99   SER SER GGG . n 
I 3 100 THR 100 100 100  THR THR GGG . n 
I 3 101 PRO 101 101 101  PRO PRO GGG . n 
I 3 102 TYR 102 102 102  TYR TYR GGG . n 
I 3 103 THR 103 103 103  THR THR GGG . n 
I 3 104 PHE 104 104 104  PHE PHE GGG . n 
I 3 105 GLY 105 105 105  GLY GLY GGG . n 
I 3 106 GLN 106 106 106  GLN GLN GGG . n 
I 3 107 GLY 107 107 107  GLY GLY GGG . n 
I 3 108 THR 108 108 108  THR THR GGG . n 
I 3 109 LYS 109 109 109  LYS LYS GGG . n 
I 3 110 VAL 110 110 110  VAL VAL GGG . n 
I 3 111 GLU 111 111 111  GLU GLU GGG . n 
I 3 112 ILE 112 112 112  ILE ILE GGG . n 
I 3 113 LYS 113 113 113  LYS LYS GGG . n 
I 3 114 ARG 114 114 114  ARG ARG GGG . n 
I 3 115 THR 115 115 115  THR THR GGG . n 
I 3 116 VAL 116 116 116  VAL VAL GGG . n 
I 3 117 ALA 117 117 117  ALA ALA GGG . n 
I 3 118 ALA 118 118 118  ALA ALA GGG . n 
I 3 119 PRO 119 119 119  PRO PRO GGG . n 
I 3 120 SER 120 120 120  SER SER GGG . n 
I 3 121 VAL 121 121 121  VAL VAL GGG . n 
I 3 122 PHE 122 122 122  PHE PHE GGG . n 
I 3 123 ILE 123 123 123  ILE ILE GGG . n 
I 3 124 PHE 124 124 124  PHE PHE GGG . n 
I 3 125 PRO 125 125 125  PRO PRO GGG . n 
I 3 126 PRO 126 126 126  PRO PRO GGG . n 
I 3 127 SER 127 127 127  SER SER GGG . n 
I 3 128 ASP 128 128 128  ASP ASP GGG . n 
I 3 129 GLU 129 129 129  GLU GLU GGG . n 
I 3 130 GLN 130 130 130  GLN GLN GGG . n 
I 3 131 LEU 131 131 131  LEU LEU GGG . n 
I 3 132 LYS 132 132 132  LYS LYS GGG . n 
I 3 133 SER 133 133 133  SER SER GGG . n 
I 3 134 GLY 134 134 134  GLY GLY GGG . n 
I 3 135 THR 135 135 135  THR THR GGG . n 
I 3 136 ALA 136 136 136  ALA ALA GGG . n 
I 3 137 SER 137 137 137  SER SER GGG . n 
I 3 138 VAL 138 138 138  VAL VAL GGG . n 
I 3 139 VAL 139 139 139  VAL VAL GGG . n 
I 3 140 CYS 140 140 140  CYS CYS GGG . n 
I 3 141 LEU 141 141 141  LEU LEU GGG . n 
I 3 142 LEU 142 142 142  LEU LEU GGG . n 
I 3 143 ASN 143 143 143  ASN ASN GGG . n 
I 3 144 ASN 144 144 144  ASN ASN GGG . n 
I 3 145 PHE 145 145 145  PHE PHE GGG . n 
I 3 146 TYR 146 146 146  TYR TYR GGG . n 
I 3 147 PRO 147 147 147  PRO PRO GGG . n 
I 3 148 ARG 148 148 148  ARG ARG GGG . n 
I 3 149 GLU 149 149 149  GLU GLU GGG . n 
I 3 150 ALA 150 150 150  ALA ALA GGG . n 
I 3 151 LYS 151 151 151  LYS LYS GGG . n 
I 3 152 VAL 152 152 152  VAL VAL GGG . n 
I 3 153 GLN 153 153 153  GLN GLN GGG . n 
I 3 154 TRP 154 154 154  TRP TRP GGG . n 
I 3 155 LYS 155 155 155  LYS LYS GGG . n 
I 3 156 VAL 156 156 156  VAL VAL GGG . n 
I 3 157 ASP 157 157 157  ASP ASP GGG . n 
I 3 158 ASN 158 158 158  ASN ASN GGG . n 
I 3 159 ALA 159 159 159  ALA ALA GGG . n 
I 3 160 LEU 160 160 160  LEU LEU GGG . n 
I 3 161 GLN 161 161 161  GLN GLN GGG . n 
I 3 162 SER 162 162 162  SER SER GGG . n 
I 3 163 GLY 163 163 163  GLY GLY GGG . n 
I 3 164 ASN 164 164 164  ASN ASN GGG . n 
I 3 165 SER 165 165 165  SER SER GGG . n 
I 3 166 GLN 166 166 166  GLN GLN GGG . n 
I 3 167 GLU 167 167 167  GLU GLU GGG . n 
I 3 168 SER 168 168 168  SER SER GGG . n 
I 3 169 VAL 169 169 169  VAL VAL GGG . n 
I 3 170 THR 170 170 170  THR THR GGG . n 
I 3 171 GLU 171 171 171  GLU GLU GGG . n 
I 3 172 GLN 172 172 172  GLN GLN GGG . n 
I 3 173 ASP 173 173 173  ASP ASP GGG . n 
I 3 174 SER 174 174 174  SER SER GGG . n 
I 3 175 LYS 175 175 175  LYS LYS GGG . n 
I 3 176 ASP 176 176 176  ASP ASP GGG . n 
I 3 177 SER 177 177 177  SER SER GGG . n 
I 3 178 THR 178 178 178  THR THR GGG . n 
I 3 179 TYR 179 179 179  TYR TYR GGG . n 
I 3 180 SER 180 180 180  SER SER GGG . n 
I 3 181 LEU 181 181 181  LEU LEU GGG . n 
I 3 182 SER 182 182 182  SER SER GGG . n 
I 3 183 SER 183 183 183  SER SER GGG . n 
I 3 184 THR 184 184 184  THR THR GGG . n 
I 3 185 LEU 185 185 185  LEU LEU GGG . n 
I 3 186 THR 186 186 186  THR THR GGG . n 
I 3 187 LEU 187 187 187  LEU LEU GGG . n 
I 3 188 SER 188 188 188  SER SER GGG . n 
I 3 189 LYS 189 189 189  LYS LYS GGG . n 
I 3 190 ALA 190 190 190  ALA ALA GGG . n 
I 3 191 ASP 191 191 191  ASP ASP GGG . n 
I 3 192 TYR 192 192 192  TYR TYR GGG . n 
I 3 193 GLU 193 193 193  GLU GLU GGG . n 
I 3 194 LYS 194 194 194  LYS LYS GGG . n 
I 3 195 HIS 195 195 195  HIS HIS GGG . n 
I 3 196 LYS 196 196 196  LYS LYS GGG . n 
I 3 197 VAL 197 197 197  VAL VAL GGG . n 
I 3 198 TYR 198 198 198  TYR TYR GGG . n 
I 3 199 ALA 199 199 199  ALA ALA GGG . n 
I 3 200 CYS 200 200 200  CYS CYS GGG . n 
I 3 201 GLU 201 201 201  GLU GLU GGG . n 
I 3 202 VAL 202 202 202  VAL VAL GGG . n 
I 3 203 THR 203 203 203  THR THR GGG . n 
I 3 204 HIS 204 204 204  HIS HIS GGG . n 
I 3 205 GLN 205 205 205  GLN GLN GGG . n 
I 3 206 GLY 206 206 206  GLY GLY GGG . n 
I 3 207 LEU 207 207 207  LEU LEU GGG . n 
I 3 208 SER 208 208 208  SER SER GGG . n 
I 3 209 SER 209 209 209  SER SER GGG . n 
I 3 210 PRO 210 210 210  PRO PRO GGG . n 
I 3 211 VAL 211 211 211  VAL VAL GGG . n 
I 3 212 THR 212 212 212  THR THR GGG . n 
I 3 213 LYS 213 213 213  LYS LYS GGG . n 
I 3 214 SER 214 214 214  SER SER GGG . n 
I 3 215 PHE 215 215 215  PHE PHE GGG . n 
I 3 216 ASN 216 216 216  ASN ASN GGG . n 
I 3 217 ARG 217 217 217  ARG ARG GGG . n 
I 3 218 GLY 218 218 218  GLY GLY GGG . n 
I 3 219 GLU 219 219 219  GLU GLU GGG . n 
I 3 220 CYS 220 220 ?    ?   ?   GGG . n 
I 3 221 SER 221 221 ?    ?   ?   GGG . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
J 4 NAG 1 601 907 NAG NAG EEE . 
K 4 NAG 1 601 907 NAG NAG AAA . 
L 4 NAG 1 601 907 NAG NAG DDD . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
3 author_and_software_defined_assembly PISA trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,J 
2 1 D,E,F,K 
3 1 G,H,I,L 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5840  ? 
1 MORE         -32   ? 
1 'SSA (A^2)'  28560 ? 
2 'ABSA (A^2)' 5860  ? 
2 MORE         -33   ? 
2 'SSA (A^2)'  28460 ? 
3 'ABSA (A^2)' 5800  ? 
3 MORE         -31   ? 
3 'SSA (A^2)'  28640 ? 
# 
_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 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2020-12-23 
2 'Structure model' 1 1 2021-01-13 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
5 2 'Structure model' '_citation_author.identifier_ORCID' 
6 2 'Structure model' '_citation_author.name'             
# 
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  ? ? ? 5.8.0253 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_pdbx_entry_details.entry_id                 6ZLR 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 AAA ASN 343 ? ? C1 AAA NAG 601 ? ? 1.93 
2 1 ND2 DDD ASN 343 ? ? O5 DDD NAG 601 ? ? 2.11 
3 1 ND2 AAA ASN 343 ? ? O5 AAA NAG 601 ? ? 2.17 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             GGG 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             GGG 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             GGG 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.69 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.39 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 ASN EEE 334 ? ? -103.57 47.46   
2  1 ALA EEE 352 ? ? -103.74 48.52   
3  1 PHE EEE 377 ? ? -159.52 59.65   
4  1 ASN EEE 422 ? ? -134.90 -57.45  
5  1 ASP EEE 428 ? ? -99.38  31.82   
6  1 ASN EEE 481 ? ? -103.83 60.19   
7  1 SER HHH 103 ? ? 74.91   52.47   
8  1 ASP HHH 150 ? ? 68.19   67.95   
9  1 ASN LLL 35  ? ? -69.81  79.82   
10 1 ALA LLL 57  ? ? 64.76   -24.87  
11 1 SER LLL 58  ? ? -155.62 0.35    
12 1 SER LLL 83  ? ? 54.90   74.84   
13 1 ASN LLL 144 ? ? 50.72   76.24   
14 1 ASN AAA 334 ? ? -106.28 49.80   
15 1 ALA AAA 352 ? ? -104.68 49.03   
16 1 PHE AAA 377 ? ? -159.64 62.22   
17 1 ASN AAA 422 ? ? -134.97 -57.76  
18 1 ASN AAA 481 ? ? -103.33 54.67   
19 1 SER BBB 103 ? ? 73.44   52.57   
20 1 ASP BBB 150 ? ? 69.27   66.29   
21 1 ALA CCC 57  ? ? 63.35   -24.07  
22 1 SER CCC 58  ? ? -155.62 0.66    
23 1 SER CCC 83  ? ? 53.96   74.62   
24 1 VAL CCC 89  ? ? -58.90  107.29  
25 1 ASN CCC 144 ? ? 49.54   76.56   
26 1 ASN DDD 334 ? ? -101.13 49.58   
27 1 ALA DDD 352 ? ? -103.64 49.68   
28 1 PHE DDD 377 ? ? -159.29 61.24   
29 1 ASN DDD 422 ? ? -134.64 -57.01  
30 1 ASP DDD 428 ? ? -99.01  30.54   
31 1 ASN DDD 481 ? ? -103.14 56.35   
32 1 CYS FFF 22  ? ? -161.25 104.53  
33 1 ALA FFF 92  ? ? -162.74 -169.12 
34 1 SER FFF 103 ? ? 72.98   53.54   
35 1 ASP FFF 150 ? ? 69.09   68.67   
36 1 ASN GGG 35  ? ? -69.14  80.98   
37 1 ALA GGG 57  ? ? 64.26   -24.81  
38 1 SER GGG 58  ? ? -154.98 -0.36   
39 1 SER GGG 83  ? ? 54.76   73.65   
40 1 VAL GGG 89  ? ? -56.19  109.19  
41 1 ASN GGG 144 ? ? 49.51   76.52   
42 1 LYS GGG 196 ? ? -120.73 -59.19  
# 
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 EEE LYS 528 ? CG ? A LYS 210 CG 
2  1 Y 1 EEE LYS 528 ? CD ? A LYS 210 CD 
3  1 Y 1 EEE LYS 528 ? CE ? A LYS 210 CE 
4  1 Y 1 EEE LYS 528 ? NZ ? A LYS 210 NZ 
5  1 Y 1 AAA LYS 528 ? CG ? D LYS 210 CG 
6  1 Y 1 AAA LYS 528 ? CD ? D LYS 210 CD 
7  1 Y 1 AAA LYS 528 ? CE ? D LYS 210 CE 
8  1 Y 1 AAA LYS 528 ? NZ ? D LYS 210 NZ 
9  1 Y 1 DDD LYS 528 ? CG ? G LYS 210 CG 
10 1 Y 1 DDD LYS 528 ? CD ? G LYS 210 CD 
11 1 Y 1 DDD LYS 528 ? CE ? G LYS 210 CE 
12 1 Y 1 DDD LYS 528 ? NZ ? G LYS 210 NZ 
13 1 N 1 AAA NAG 601 ? O1 ? K NAG 1   O1 
# 
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 EEE ARG 319 ? A ARG 1   
2   1 Y 1 EEE VAL 320 ? A VAL 2   
3   1 Y 1 EEE GLN 321 ? A GLN 3   
4   1 Y 1 EEE PRO 322 ? A PRO 4   
5   1 Y 1 EEE THR 323 ? A THR 5   
6   1 Y 1 EEE GLU 324 ? A GLU 6   
7   1 Y 1 EEE SER 325 ? A SER 7   
8   1 Y 1 EEE ILE 326 ? A ILE 8   
9   1 Y 1 EEE VAL 327 ? A VAL 9   
10  1 Y 1 EEE ARG 328 ? A ARG 10  
11  1 Y 1 EEE PHE 329 ? A PHE 11  
12  1 Y 1 EEE PRO 330 ? A PRO 12  
13  1 Y 1 EEE ASN 331 ? A ASN 13  
14  1 Y 1 EEE ILE 332 ? A ILE 14  
15  1 Y 1 EEE LYS 529 ? A LYS 211 
16  1 Y 1 EEE SER 530 ? A SER 212 
17  1 Y 1 EEE THR 531 ? A THR 213 
18  1 Y 1 EEE ASN 532 ? A ASN 214 
19  1 Y 1 EEE LEU 533 ? A LEU 215 
20  1 Y 1 EEE VAL 534 ? A VAL 216 
21  1 Y 1 EEE LYS 535 ? A LYS 217 
22  1 Y 1 EEE ASN 536 ? A ASN 218 
23  1 Y 1 EEE LYS 537 ? A LYS 219 
24  1 Y 1 EEE CYS 538 ? A CYS 220 
25  1 Y 1 EEE VAL 539 ? A VAL 221 
26  1 Y 1 EEE ASN 540 ? A ASN 222 
27  1 Y 1 EEE PHE 541 ? A PHE 223 
28  1 Y 1 EEE SER 542 ? A SER 224 
29  1 Y 1 EEE GLY 543 ? A GLY 225 
30  1 Y 1 EEE HIS 544 ? A HIS 226 
31  1 Y 1 EEE HIS 545 ? A HIS 227 
32  1 Y 1 EEE HIS 546 ? A HIS 228 
33  1 Y 1 EEE HIS 547 ? A HIS 229 
34  1 Y 1 EEE HIS 548 ? A HIS 230 
35  1 Y 1 EEE HIS 549 ? A HIS 231 
36  1 Y 1 LLL CYS 220 ? C CYS 220 
37  1 Y 1 LLL SER 221 ? C SER 221 
38  1 Y 1 AAA ARG 319 ? D ARG 1   
39  1 Y 1 AAA VAL 320 ? D VAL 2   
40  1 Y 1 AAA GLN 321 ? D GLN 3   
41  1 Y 1 AAA PRO 322 ? D PRO 4   
42  1 Y 1 AAA THR 323 ? D THR 5   
43  1 Y 1 AAA GLU 324 ? D GLU 6   
44  1 Y 1 AAA SER 325 ? D SER 7   
45  1 Y 1 AAA ILE 326 ? D ILE 8   
46  1 Y 1 AAA VAL 327 ? D VAL 9   
47  1 Y 1 AAA ARG 328 ? D ARG 10  
48  1 Y 1 AAA PHE 329 ? D PHE 11  
49  1 Y 1 AAA PRO 330 ? D PRO 12  
50  1 Y 1 AAA ASN 331 ? D ASN 13  
51  1 Y 1 AAA ILE 332 ? D ILE 14  
52  1 Y 1 AAA LYS 529 ? D LYS 211 
53  1 Y 1 AAA SER 530 ? D SER 212 
54  1 Y 1 AAA THR 531 ? D THR 213 
55  1 Y 1 AAA ASN 532 ? D ASN 214 
56  1 Y 1 AAA LEU 533 ? D LEU 215 
57  1 Y 1 AAA VAL 534 ? D VAL 216 
58  1 Y 1 AAA LYS 535 ? D LYS 217 
59  1 Y 1 AAA ASN 536 ? D ASN 218 
60  1 Y 1 AAA LYS 537 ? D LYS 219 
61  1 Y 1 AAA CYS 538 ? D CYS 220 
62  1 Y 1 AAA VAL 539 ? D VAL 221 
63  1 Y 1 AAA ASN 540 ? D ASN 222 
64  1 Y 1 AAA PHE 541 ? D PHE 223 
65  1 Y 1 AAA SER 542 ? D SER 224 
66  1 Y 1 AAA GLY 543 ? D GLY 225 
67  1 Y 1 AAA HIS 544 ? D HIS 226 
68  1 Y 1 AAA HIS 545 ? D HIS 227 
69  1 Y 1 AAA HIS 546 ? D HIS 228 
70  1 Y 1 AAA HIS 547 ? D HIS 229 
71  1 Y 1 AAA HIS 548 ? D HIS 230 
72  1 Y 1 AAA HIS 549 ? D HIS 231 
73  1 Y 1 CCC CYS 220 ? F CYS 220 
74  1 Y 1 CCC SER 221 ? F SER 221 
75  1 Y 1 DDD ARG 319 ? G ARG 1   
76  1 Y 1 DDD VAL 320 ? G VAL 2   
77  1 Y 1 DDD GLN 321 ? G GLN 3   
78  1 Y 1 DDD PRO 322 ? G PRO 4   
79  1 Y 1 DDD THR 323 ? G THR 5   
80  1 Y 1 DDD GLU 324 ? G GLU 6   
81  1 Y 1 DDD SER 325 ? G SER 7   
82  1 Y 1 DDD ILE 326 ? G ILE 8   
83  1 Y 1 DDD VAL 327 ? G VAL 9   
84  1 Y 1 DDD ARG 328 ? G ARG 10  
85  1 Y 1 DDD PHE 329 ? G PHE 11  
86  1 Y 1 DDD PRO 330 ? G PRO 12  
87  1 Y 1 DDD ASN 331 ? G ASN 13  
88  1 Y 1 DDD ILE 332 ? G ILE 14  
89  1 Y 1 DDD LYS 529 ? G LYS 211 
90  1 Y 1 DDD SER 530 ? G SER 212 
91  1 Y 1 DDD THR 531 ? G THR 213 
92  1 Y 1 DDD ASN 532 ? G ASN 214 
93  1 Y 1 DDD LEU 533 ? G LEU 215 
94  1 Y 1 DDD VAL 534 ? G VAL 216 
95  1 Y 1 DDD LYS 535 ? G LYS 217 
96  1 Y 1 DDD ASN 536 ? G ASN 218 
97  1 Y 1 DDD LYS 537 ? G LYS 219 
98  1 Y 1 DDD CYS 538 ? G CYS 220 
99  1 Y 1 DDD VAL 539 ? G VAL 221 
100 1 Y 1 DDD ASN 540 ? G ASN 222 
101 1 Y 1 DDD PHE 541 ? G PHE 223 
102 1 Y 1 DDD SER 542 ? G SER 224 
103 1 Y 1 DDD GLY 543 ? G GLY 225 
104 1 Y 1 DDD HIS 544 ? G HIS 226 
105 1 Y 1 DDD HIS 545 ? G HIS 227 
106 1 Y 1 DDD HIS 546 ? G HIS 228 
107 1 Y 1 DDD HIS 547 ? G HIS 229 
108 1 Y 1 DDD HIS 548 ? G HIS 230 
109 1 Y 1 DDD HIS 549 ? G HIS 231 
110 1 Y 1 GGG CYS 220 ? I CYS 220 
111 1 Y 1 GGG SER 221 ? I SER 221 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none ? 
2 2 none ? 
3 3 none ? 
# 
