data_6ZH9
# 
_entry.id   6ZH9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.333 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6ZH9         
WWPDB D_1292109531 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6ZH9 
_pdbx_database_status.recvd_initial_deposition_date   2020-06-21 
_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 
'Naismith, J.H.' 1 0000-0001-6744-5061 
'Mikolajek, H.'  2 0000-0003-0776-9974 
'Le Bas, A.'     3 0000-0002-1100-6833 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            27 
_citation.language                  ? 
_citation.page_first                846 
_citation.page_last                 854 
_citation.title                     'Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-020-0469-6 
_citation.pdbx_database_id_PubMed   32661423 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Huo, J.'               1  ? 
primary 'Le Bas, A.'            2  ? 
primary 'Ruza, R.R.'            3  ? 
primary 'Duyvesteyn, H.M.E.'    4  ? 
primary 'Mikolajek, H.'         5  ? 
primary 'Malinauskas, T.'       6  ? 
primary 'Tan, T.K.'             7  ? 
primary 'Rijal, P.'             8  ? 
primary 'Dumoux, M.'            9  ? 
primary 'Ward, P.N.'            10 ? 
primary 'Ren, J.'               11 ? 
primary 'Zhou, D.'              12 ? 
primary 'Harrison, P.J.'        13 ? 
primary 'Weckener, M.'          14 ? 
primary 'Clare, D.K.'           15 ? 
primary 'Vogirala, V.K.'        16 ? 
primary 'Radecke, J.'           17 ? 
primary 'Moynie, L.'            18 ? 
primary 'Zhao, Y.'              19 ? 
primary 'Gilbert-Jaramillo, J.' 20 ? 
primary 'Knight, M.L.'          21 ? 
primary 'Tree, J.A.'            22 ? 
primary 'Buttigieg, K.R.'       23 ? 
primary 'Coombes, N.'           24 ? 
primary 'Elmore, M.J.'          25 ? 
primary 'Carroll, M.W.'         26 ? 
primary 'Carrique, L.'          27 ? 
primary 'Shah, P.N.M.'          28 ? 
primary 'James, W.'             29 ? 
primary 'Townsend, A.R.'        30 ? 
primary 'Stuart, D.I.'          31 ? 
primary 'Owens, R.J.'           32 ? 
primary 'Naismith, J.H.'        33 ? 
# 
_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                     6ZH9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     156.411 
_cell.length_a_esd                 ? 
_cell.length_b                     156.411 
_cell.length_b_esd                 ? 
_cell.length_c                     116.205 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         6ZH9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 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 'CR3022 heavy'       22874.785 1 ? ? ? ? 
2 polymer man 'CR3022 Light chain' 24186.740 1 ? ? ? ? 
3 polymer man 'Spike glycoprotein' 22115.834 1 ? ? ? ? 
4 polymer man 'Nanobody H11-H4'    15045.752 1 ? ? ? ? 
# 
_entity_name_com.entity_id   3 
_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 
;TQMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTA
YLQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVASTKGPSVFPLAPSSGGTAALGCLVKDYFPEPVTVSWNSGAL
TSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKS
;
;TQMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTA
YLQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVASTKGPSVFPLAPSSGGTAALGCLVKDYFPEPVTVSWNSGAL
TSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKS
;
HHH ? 
2 'polypeptide(L)' no no 
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
;
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
;
LLL ? 
3 'polypeptide(L)' no no 
;ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
;ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
EEE ? 
4 'polypeptide(L)' no no 
;QVQLVESGGGLMQAGGSLRLSCAVSGRTFSTAAMGWFRQAPGKEREFVAAIRWSGGSAYYADSVKGRFTISRDKAKNTVY
LQMNSLKYEDTAVYYCAQTHYVSYLLSDYATWPYDYWGQGTQVTVSSKHHHHHH
;
;QVQLVESGGGLMQAGGSLRLSCAVSGRTFSTAAMGWFRQAPGKEREFVAAIRWSGGSAYYADSVKGRFTISRDKAKNTVY
LQMNSLKYEDTAVYYCAQTHYVSYLLSDYATWPYDYWGQGTQVTVSSKHHHHHH
;
FFF ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   GLN n 
1 3   MET n 
1 4   GLN n 
1 5   LEU n 
1 6   VAL n 
1 7   GLN n 
1 8   SER n 
1 9   GLY n 
1 10  THR n 
1 11  GLU n 
1 12  VAL n 
1 13  LYS n 
1 14  LYS n 
1 15  PRO n 
1 16  GLY n 
1 17  GLU n 
1 18  SER n 
1 19  LEU n 
1 20  LYS n 
1 21  ILE n 
1 22  SER n 
1 23  CYS n 
1 24  LYS n 
1 25  GLY n 
1 26  SER n 
1 27  GLY n 
1 28  TYR n 
1 29  GLY n 
1 30  PHE n 
1 31  ILE n 
1 32  THR n 
1 33  TYR n 
1 34  TRP n 
1 35  ILE n 
1 36  GLY n 
1 37  TRP n 
1 38  VAL n 
1 39  ARG n 
1 40  GLN n 
1 41  MET n 
1 42  PRO n 
1 43  GLY n 
1 44  LYS n 
1 45  GLY n 
1 46  LEU n 
1 47  GLU n 
1 48  TRP n 
1 49  MET n 
1 50  GLY n 
1 51  ILE n 
1 52  ILE n 
1 53  TYR n 
1 54  PRO n 
1 55  GLY n 
1 56  ASP n 
1 57  SER n 
1 58  GLU n 
1 59  THR n 
1 60  ARG n 
1 61  TYR n 
1 62  SER n 
1 63  PRO n 
1 64  SER n 
1 65  PHE n 
1 66  GLN n 
1 67  GLY n 
1 68  GLN n 
1 69  VAL n 
1 70  THR n 
1 71  ILE n 
1 72  SER n 
1 73  ALA n 
1 74  ASP n 
1 75  LYS n 
1 76  SER n 
1 77  ILE n 
1 78  ASN n 
1 79  THR n 
1 80  ALA n 
1 81  TYR n 
1 82  LEU n 
1 83  GLN n 
1 84  TRP n 
1 85  SER n 
1 86  SER n 
1 87  LEU n 
1 88  LYS n 
1 89  ALA n 
1 90  SER n 
1 91  ASP n 
1 92  THR n 
1 93  ALA n 
1 94  ILE n 
1 95  TYR n 
1 96  TYR n 
1 97  CYS n 
1 98  ALA n 
1 99  GLY n 
1 100 GLY n 
1 101 SER n 
1 102 GLY n 
1 103 ILE n 
1 104 SER n 
1 105 THR n 
1 106 PRO n 
1 107 MET n 
1 108 ASP n 
1 109 VAL n 
1 110 TRP n 
1 111 GLY n 
1 112 GLN n 
1 113 GLY n 
1 114 THR n 
1 115 THR n 
1 116 VAL n 
1 117 THR n 
1 118 VAL n 
1 119 ALA n 
1 120 SER n 
1 121 THR n 
1 122 LYS n 
1 123 GLY n 
1 124 PRO n 
1 125 SER n 
1 126 VAL n 
1 127 PHE n 
1 128 PRO n 
1 129 LEU n 
1 130 ALA n 
1 131 PRO n 
1 132 SER n 
1 133 SER n 
1 134 GLY n 
1 135 GLY n 
1 136 THR n 
1 137 ALA n 
1 138 ALA n 
1 139 LEU n 
1 140 GLY n 
1 141 CYS n 
1 142 LEU n 
1 143 VAL n 
1 144 LYS n 
1 145 ASP n 
1 146 TYR n 
1 147 PHE n 
1 148 PRO n 
1 149 GLU n 
1 150 PRO n 
1 151 VAL n 
1 152 THR n 
1 153 VAL n 
1 154 SER n 
1 155 TRP n 
1 156 ASN n 
1 157 SER n 
1 158 GLY n 
1 159 ALA n 
1 160 LEU n 
1 161 THR n 
1 162 SER n 
1 163 GLY n 
1 164 VAL n 
1 165 HIS n 
1 166 THR n 
1 167 PHE n 
1 168 PRO n 
1 169 ALA n 
1 170 VAL n 
1 171 LEU n 
1 172 GLN n 
1 173 SER n 
1 174 SER n 
1 175 GLY n 
1 176 LEU n 
1 177 TYR n 
1 178 SER n 
1 179 LEU n 
1 180 SER n 
1 181 SER n 
1 182 VAL n 
1 183 VAL n 
1 184 THR n 
1 185 VAL n 
1 186 PRO n 
1 187 SER n 
1 188 SER n 
1 189 SER n 
1 190 LEU n 
1 191 GLY n 
1 192 THR n 
1 193 GLN n 
1 194 THR n 
1 195 TYR n 
1 196 ILE n 
1 197 CYS n 
1 198 ASN n 
1 199 VAL n 
1 200 ASN n 
1 201 HIS n 
1 202 LYS n 
1 203 PRO n 
1 204 SER n 
1 205 ASN n 
1 206 THR n 
1 207 LYS n 
1 208 VAL n 
1 209 ASP n 
1 210 LYS n 
1 211 LYS n 
1 212 VAL n 
1 213 GLU n 
1 214 PRO n 
1 215 LYS n 
1 216 SER n 
2 1   ASP n 
2 2   ILE n 
2 3   GLN n 
2 4   LEU n 
2 5   THR n 
2 6   GLN n 
2 7   SER n 
2 8   PRO n 
2 9   ASP n 
2 10  SER n 
2 11  LEU n 
2 12  ALA n 
2 13  VAL n 
2 14  SER n 
2 15  LEU n 
2 16  GLY n 
2 17  GLU n 
2 18  ARG n 
2 19  ALA n 
2 20  THR n 
2 21  ILE n 
2 22  ASN n 
2 23  CYS n 
2 24  LYS n 
2 25  SER n 
2 26  SER n 
2 27  GLN n 
2 28  SER n 
2 29  VAL n 
2 30  LEU n 
2 31  TYR n 
2 32  SER n 
2 33  SER n 
2 34  ILE n 
2 35  ASN n 
2 36  LYS n 
2 37  ASN n 
2 38  TYR n 
2 39  LEU n 
2 40  ALA n 
2 41  TRP n 
2 42  TYR n 
2 43  GLN n 
2 44  GLN n 
2 45  LYS n 
2 46  PRO n 
2 47  GLY n 
2 48  GLN n 
2 49  PRO n 
2 50  PRO n 
2 51  LYS n 
2 52  LEU n 
2 53  LEU n 
2 54  ILE n 
2 55  TYR n 
2 56  TRP n 
2 57  ALA n 
2 58  SER n 
2 59  THR n 
2 60  ARG n 
2 61  GLU n 
2 62  SER n 
2 63  GLY n 
2 64  VAL n 
2 65  PRO n 
2 66  ASP n 
2 67  ARG n 
2 68  PHE n 
2 69  SER n 
2 70  GLY n 
2 71  SER n 
2 72  GLY n 
2 73  SER n 
2 74  GLY n 
2 75  THR n 
2 76  ASP n 
2 77  PHE n 
2 78  THR n 
2 79  LEU n 
2 80  THR n 
2 81  ILE n 
2 82  SER n 
2 83  SER n 
2 84  LEU n 
2 85  GLN n 
2 86  ALA n 
2 87  GLU n 
2 88  ASP n 
2 89  VAL n 
2 90  ALA n 
2 91  VAL n 
2 92  TYR n 
2 93  TYR n 
2 94  CYS n 
2 95  GLN n 
2 96  GLN n 
2 97  TYR n 
2 98  TYR n 
2 99  SER n 
2 100 THR n 
2 101 PRO n 
2 102 TYR n 
2 103 THR n 
2 104 PHE n 
2 105 GLY n 
2 106 GLN n 
2 107 GLY n 
2 108 THR n 
2 109 LYS n 
2 110 VAL n 
2 111 GLU n 
2 112 ILE n 
2 113 LYS n 
2 114 ARG n 
2 115 THR n 
2 116 VAL n 
2 117 ALA n 
2 118 ALA n 
2 119 PRO n 
2 120 SER n 
2 121 VAL n 
2 122 PHE n 
2 123 ILE n 
2 124 PHE n 
2 125 PRO n 
2 126 PRO n 
2 127 SER n 
2 128 ASP n 
2 129 GLU n 
2 130 GLN n 
2 131 LEU n 
2 132 LYS n 
2 133 SER n 
2 134 GLY n 
2 135 THR n 
2 136 ALA n 
2 137 SER n 
2 138 VAL n 
2 139 VAL n 
2 140 CYS n 
2 141 LEU n 
2 142 LEU n 
2 143 ASN n 
2 144 ASN n 
2 145 PHE n 
2 146 TYR n 
2 147 PRO n 
2 148 ARG n 
2 149 GLU n 
2 150 ALA n 
2 151 LYS n 
2 152 VAL n 
2 153 GLN n 
2 154 TRP n 
2 155 LYS n 
2 156 VAL n 
2 157 ASP n 
2 158 ASN n 
2 159 ALA n 
2 160 LEU n 
2 161 GLN n 
2 162 SER n 
2 163 GLY n 
2 164 ASN n 
2 165 SER n 
2 166 GLN n 
2 167 GLU n 
2 168 SER n 
2 169 VAL n 
2 170 THR n 
2 171 GLU n 
2 172 GLN n 
2 173 ASP n 
2 174 SER n 
2 175 LYS n 
2 176 ASP n 
2 177 SER n 
2 178 THR n 
2 179 TYR n 
2 180 SER n 
2 181 LEU n 
2 182 SER n 
2 183 SER n 
2 184 THR n 
2 185 LEU n 
2 186 THR n 
2 187 LEU n 
2 188 SER n 
2 189 LYS n 
2 190 ALA n 
2 191 ASP n 
2 192 TYR n 
2 193 GLU n 
2 194 LYS n 
2 195 HIS n 
2 196 LYS n 
2 197 VAL n 
2 198 TYR n 
2 199 ALA n 
2 200 CYS n 
2 201 GLU n 
2 202 VAL n 
2 203 THR n 
2 204 HIS n 
2 205 GLN n 
2 206 GLY n 
2 207 LEU n 
2 208 SER n 
2 209 SER n 
2 210 PRO n 
2 211 VAL n 
2 212 THR n 
2 213 LYS n 
2 214 SER n 
2 215 PHE n 
2 216 ASN n 
2 217 ARG n 
2 218 GLY n 
2 219 GLU n 
3 1   ILE n 
3 2   THR n 
3 3   ASN n 
3 4   LEU n 
3 5   CYS n 
3 6   PRO n 
3 7   PHE n 
3 8   GLY n 
3 9   GLU n 
3 10  VAL n 
3 11  PHE n 
3 12  ASN n 
3 13  ALA n 
3 14  THR n 
3 15  ARG n 
3 16  PHE n 
3 17  ALA n 
3 18  SER n 
3 19  VAL n 
3 20  TYR n 
3 21  ALA n 
3 22  TRP n 
3 23  ASN n 
3 24  ARG n 
3 25  LYS n 
3 26  ARG n 
3 27  ILE n 
3 28  SER n 
3 29  ASN n 
3 30  CYS n 
3 31  VAL n 
3 32  ALA n 
3 33  ASP n 
3 34  TYR n 
3 35  SER n 
3 36  VAL n 
3 37  LEU n 
3 38  TYR n 
3 39  ASN n 
3 40  SER n 
3 41  ALA n 
3 42  SER n 
3 43  PHE n 
3 44  SER n 
3 45  THR n 
3 46  PHE n 
3 47  LYS n 
3 48  CYS n 
3 49  TYR n 
3 50  GLY n 
3 51  VAL n 
3 52  SER n 
3 53  PRO n 
3 54  THR n 
3 55  LYS n 
3 56  LEU n 
3 57  ASN n 
3 58  ASP n 
3 59  LEU n 
3 60  CYS n 
3 61  PHE n 
3 62  THR n 
3 63  ASN n 
3 64  VAL n 
3 65  TYR n 
3 66  ALA n 
3 67  ASP n 
3 68  SER n 
3 69  PHE n 
3 70  VAL n 
3 71  ILE n 
3 72  ARG n 
3 73  GLY n 
3 74  ASP n 
3 75  GLU n 
3 76  VAL n 
3 77  ARG n 
3 78  GLN n 
3 79  ILE n 
3 80  ALA n 
3 81  PRO n 
3 82  GLY n 
3 83  GLN n 
3 84  THR n 
3 85  GLY n 
3 86  LYS n 
3 87  ILE n 
3 88  ALA n 
3 89  ASP n 
3 90  TYR n 
3 91  ASN n 
3 92  TYR n 
3 93  LYS n 
3 94  LEU n 
3 95  PRO n 
3 96  ASP n 
3 97  ASP n 
3 98  PHE n 
3 99  THR n 
3 100 GLY n 
3 101 CYS n 
3 102 VAL n 
3 103 ILE n 
3 104 ALA n 
3 105 TRP n 
3 106 ASN n 
3 107 SER n 
3 108 ASN n 
3 109 ASN n 
3 110 LEU n 
3 111 ASP n 
3 112 SER n 
3 113 LYS n 
3 114 VAL n 
3 115 GLY n 
3 116 GLY n 
3 117 ASN n 
3 118 TYR n 
3 119 ASN n 
3 120 TYR n 
3 121 LEU n 
3 122 TYR n 
3 123 ARG n 
3 124 LEU n 
3 125 PHE n 
3 126 ARG n 
3 127 LYS n 
3 128 SER n 
3 129 ASN n 
3 130 LEU n 
3 131 LYS n 
3 132 PRO n 
3 133 PHE n 
3 134 GLU n 
3 135 ARG n 
3 136 ASP n 
3 137 ILE n 
3 138 SER n 
3 139 THR n 
3 140 GLU n 
3 141 ILE n 
3 142 TYR n 
3 143 GLN n 
3 144 ALA n 
3 145 GLY n 
3 146 SER n 
3 147 THR n 
3 148 PRO n 
3 149 CYS n 
3 150 ASN n 
3 151 GLY n 
3 152 VAL n 
3 153 GLU n 
3 154 GLY n 
3 155 PHE n 
3 156 ASN n 
3 157 CYS n 
3 158 TYR n 
3 159 PHE n 
3 160 PRO n 
3 161 LEU n 
3 162 GLN n 
3 163 SER n 
3 164 TYR n 
3 165 GLY n 
3 166 PHE n 
3 167 GLN n 
3 168 PRO n 
3 169 THR n 
3 170 ASN n 
3 171 GLY n 
3 172 VAL n 
3 173 GLY n 
3 174 TYR n 
3 175 GLN n 
3 176 PRO n 
3 177 TYR n 
3 178 ARG n 
3 179 VAL n 
3 180 VAL n 
3 181 VAL n 
3 182 LEU n 
3 183 SER n 
3 184 PHE n 
3 185 GLU n 
3 186 LEU n 
3 187 LEU n 
3 188 HIS n 
3 189 ALA n 
3 190 PRO n 
3 191 ALA n 
3 192 THR n 
3 193 VAL n 
3 194 CYS n 
3 195 GLY n 
3 196 PRO n 
3 197 LYS n 
4 1   GLN n 
4 2   VAL n 
4 3   GLN n 
4 4   LEU n 
4 5   VAL n 
4 6   GLU n 
4 7   SER n 
4 8   GLY n 
4 9   GLY n 
4 10  GLY n 
4 11  LEU n 
4 12  MET n 
4 13  GLN n 
4 14  ALA n 
4 15  GLY n 
4 16  GLY n 
4 17  SER n 
4 18  LEU n 
4 19  ARG n 
4 20  LEU n 
4 21  SER n 
4 22  CYS n 
4 23  ALA n 
4 24  VAL n 
4 25  SER n 
4 26  GLY n 
4 27  ARG n 
4 28  THR n 
4 29  PHE n 
4 30  SER n 
4 31  THR n 
4 32  ALA n 
4 33  ALA n 
4 34  MET n 
4 35  GLY n 
4 36  TRP n 
4 37  PHE n 
4 38  ARG n 
4 39  GLN n 
4 40  ALA n 
4 41  PRO n 
4 42  GLY n 
4 43  LYS n 
4 44  GLU n 
4 45  ARG n 
4 46  GLU n 
4 47  PHE n 
4 48  VAL n 
4 49  ALA n 
4 50  ALA n 
4 51  ILE n 
4 52  ARG n 
4 53  TRP n 
4 54  SER n 
4 55  GLY n 
4 56  GLY n 
4 57  SER n 
4 58  ALA n 
4 59  TYR n 
4 60  TYR n 
4 61  ALA n 
4 62  ASP n 
4 63  SER n 
4 64  VAL n 
4 65  LYS n 
4 66  GLY n 
4 67  ARG n 
4 68  PHE n 
4 69  THR n 
4 70  ILE n 
4 71  SER n 
4 72  ARG n 
4 73  ASP n 
4 74  LYS n 
4 75  ALA n 
4 76  LYS n 
4 77  ASN n 
4 78  THR n 
4 79  VAL n 
4 80  TYR n 
4 81  LEU n 
4 82  GLN n 
4 83  MET n 
4 84  ASN n 
4 85  SER n 
4 86  LEU n 
4 87  LYS n 
4 88  TYR n 
4 89  GLU n 
4 90  ASP n 
4 91  THR n 
4 92  ALA n 
4 93  VAL n 
4 94  TYR n 
4 95  TYR n 
4 96  CYS n 
4 97  ALA n 
4 98  GLN n 
4 99  THR n 
4 100 HIS n 
4 101 TYR n 
4 102 VAL n 
4 103 SER n 
4 104 TYR n 
4 105 LEU n 
4 106 LEU n 
4 107 SER n 
4 108 ASP n 
4 109 TYR n 
4 110 ALA n 
4 111 THR n 
4 112 TRP n 
4 113 PRO n 
4 114 TYR n 
4 115 ASP n 
4 116 TYR n 
4 117 TRP n 
4 118 GLY n 
4 119 GLN n 
4 120 GLY n 
4 121 THR n 
4 122 GLN n 
4 123 VAL n 
4 124 THR n 
4 125 VAL n 
4 126 SER n 
4 127 SER n 
4 128 LYS n 
4 129 HIS n 
4 130 HIS n 
4 131 HIS n 
4 132 HIS n 
4 133 HIS n 
4 134 HIS 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' 1 216 ?         ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 219 ?         ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 197 2019-nCoV ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? 
? ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 134 ?         ? ?      ? ? ? ? ? ? 'Lama glama'                                      9844    ? 
? ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 6ZH9        6ZH9   ? 1 ? 1   
2 PDB 6ZH9        6ZH9   ? 2 ? 1   
3 UNP SPIKE_SARS2 P0DTC2 ? 3 
;ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
332 
4 PDB 6ZH9        6ZH9   ? 4 ? 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 6ZH9 HHH 1 ? 216 ? 6ZH9   0   ? 219 ? 0   219 
2 2 6ZH9 LLL 1 ? 219 ? 6ZH9   1   ? 219 ? 1   219 
3 3 6ZH9 EEE 1 ? 197 ? P0DTC2 332 ? 528 ? 332 528 
4 4 6ZH9 FFF 1 ? 134 ? 6ZH9   1   ? 134 ? 1   134 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6ZH9 
_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            4.22 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         70.85 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;mixing 0.2 uL of the 18 mg/mL complex with 0.1 uL of the crystallization buffer containing 0.2 M Sodium acetate trihydrate, 0.1 M MES pH 6.0, 20 % w/v PEG 8000.
;
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-06-18 
_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   0.98 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6ZH9 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.31 
_reflns.d_resolution_low                 80.253 
_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                       22105 
_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             100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  25.6 
_reflns.pdbx_Rmerge_I_obs                0.091 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         21.9 
_reflns.pdbx_netI_over_sigmaI            0.018 
_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                     1 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.31 
_reflns_shell.d_res_low                   3.4 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         0.5 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           1538 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                3.9 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             0.77 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.3 
_reflns_shell.pdbx_CC_star                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -1.696 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -1.696 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            3.392 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               134 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.830 
_refine.correlation_coeff_Fo_to_Fc_free          0.900 
_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                                 6ZH9 
_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                            3.310 
_refine.ls_d_res_low                             80.243 
_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                     22065 
_refine.ls_number_reflns_R_free                  1088 
_refine.ls_number_reflns_R_work                  20977 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.964 
_refine.ls_percent_reflns_R_free                 4.931 
_refine.ls_R_factor_all                          0.263 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.3052 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2609 
_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                      6ZBY 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.545 
_refine.pdbx_solvent_vdw_probe_radii             1.000 
_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                             109.814 
_refine.overall_SU_ML                            0.696 
_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.pdbx_number_atoms_protein        5856 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               5856 
_refine_hist.d_res_high                       3.310 
_refine_hist.d_res_low                        80.243 
# 
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   6072  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017   5372  ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.626  1.646   8275  ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.228  1.571   12533 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 21.543 5.351   797   ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 35.970 22.982  275   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 17.099 15.000  939   ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 20.671 15.000  2     ? r_dihedral_angle_other_3_deg   ? ? 
'X-RAY DIFFRACTION' ? 17.991 15.000  24    ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.059  0.200   788   ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020   7576  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020   1299  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200   920   ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.188  0.200   5024  ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200   2807  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200   2885  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.143  0.200   120   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.179  0.200   19    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.254  0.200   55    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.266  0.200   5     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 0.074  0.200   1     ? r_xyhbond_nbd_other            ? ? 
'X-RAY DIFFRACTION' ? 7.791  11.681  3051  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 7.787  11.682  3050  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 12.289 17.510  3812  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 12.288 17.509  3813  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 7.250  11.932  3020  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 7.249  11.931  3021  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 11.809 17.759  4455  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 11.808 17.759  4456  ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 19.804 221.692 24022 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 19.804 221.688 24023 ? r_lrange_other                 ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 3.310  3.396  . . 89 1494 99.6224  . . . 0.416 . 0.405 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.396  3.489  . . 87 1470 100.0000 . . . 0.395 . 0.378 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.489  3.590  . . 86 1437 100.0000 . . . 0.321 . 0.339 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.590  3.700  . . 73 1389 100.0000 . . . 0.374 . 0.319 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.700  3.822  . . 70 1386 100.0000 . . . 0.356 . 0.317 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.822  3.956  . . 82 1305 100.0000 . . . 0.355 . 0.297 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.956  4.105  . . 57 1270 100.0000 . . . 0.353 . 0.298 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.105  4.272  . . 57 1246 100.0000 . . . 0.343 . 0.300 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.272  4.462  . . 63 1187 100.0000 . . . 0.319 . 0.260 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.462  4.679  . . 47 1130 100.0000 . . . 0.240 . 0.234 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.679  4.932  . . 51 1093 100.0000 . . . 0.315 . 0.229 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.932  5.230  . . 54 1023 100.0000 . . . 0.358 . 0.246 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.230  5.591  . . 49 983  100.0000 . . . 0.296 . 0.246 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.591  6.037  . . 52 892  100.0000 . . . 0.303 . 0.244 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.037  6.612  . . 35 843  100.0000 . . . 0.362 . 0.259 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.612  7.389  . . 36 785  100.0000 . . . 0.290 . 0.229 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 7.389  8.527  . . 27 689  100.0000 . . . 0.232 . 0.211 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 8.527  10.429 . . 30 596  100.0000 . . . 0.251 . 0.181 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 10.429 14.690 . . 22 474  100.0000 . . . 0.284 . 0.198 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 14.690 80.243 . . 21 285  99.3506  . . . 0.277 . 0.504 . . . . . . . . . . . 
# 
_struct.entry_id                     6ZH9 
_struct.title                        'Ternary complex CR3022 H11-H4 and RBD (SARS-CoV-2)' 
_struct.pdbx_descriptor              'CR3022 heavy, CR3022 Light chain, Spike glycoprotein, Nanobody H11-H4' 
_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        6ZH9 
_struct_keywords.text            'Covid19, nanobody, SARS-CoV-2, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL 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 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 GLY A 29  ? TYR A 33  ? GLY HHH 28  TYR HHH 32  5 ? 5 
HELX_P HELX_P2  AA2 LYS A 75  ? ILE A 77  ? LYS HHH 74  ILE HHH 76  5 ? 3 
HELX_P HELX_P3  AA3 LYS A 88  ? THR A 92  ? LYS HHH 87  THR HHH 91  5 ? 5 
HELX_P HELX_P4  AA4 SER A 157 ? ALA A 159 ? SER HHH 160 ALA HHH 162 5 ? 3 
HELX_P HELX_P5  AA5 SER A 188 ? THR A 192 ? SER HHH 191 THR HHH 195 5 ? 5 
HELX_P HELX_P6  AA6 LYS A 202 ? ASN A 205 ? LYS HHH 205 ASN HHH 208 5 ? 4 
HELX_P HELX_P7  AA7 GLN B 85  ? VAL B 89  ? GLN LLL 85  VAL LLL 89  5 ? 5 
HELX_P HELX_P8  AA8 GLU B 129 ? SER B 133 ? GLU LLL 129 SER LLL 133 5 ? 5 
HELX_P HELX_P9  AA9 LYS B 189 ? GLU B 193 ? LYS LLL 189 GLU LLL 193 1 ? 5 
HELX_P HELX_P10 AB1 PRO C 6   ? ASN C 12  ? PRO EEE 337 ASN EEE 343 1 ? 7 
HELX_P HELX_P11 AB2 SER C 18  ? TRP C 22  ? SER EEE 349 TRP EEE 353 5 ? 5 
HELX_P HELX_P12 AB3 TYR C 34  ? ASN C 39  ? TYR EEE 365 ASN EEE 370 1 ? 6 
HELX_P HELX_P13 AB4 LYS C 55  ? ASP C 58  ? LYS EEE 386 ASP EEE 389 5 ? 4 
HELX_P HELX_P14 AB5 ASP C 74  ? ILE C 79  ? ASP EEE 405 ILE EEE 410 5 ? 6 
HELX_P HELX_P15 AB6 GLY C 85  ? ASN C 91  ? GLY EEE 416 ASN EEE 422 1 ? 7 
HELX_P HELX_P16 AB7 SER C 107 ? SER C 112 ? SER EEE 438 SER EEE 443 1 ? 6 
HELX_P HELX_P17 AB8 GLY C 171 ? TYR C 174 ? GLY EEE 502 TYR EEE 505 5 ? 4 
HELX_P HELX_P18 AB9 THR D 28  ? THR D 31  ? THR FFF 28  THR FFF 31  5 ? 4 
HELX_P HELX_P19 AC1 LYS D 87  ? THR D 91  ? LYS FFF 87  THR FFF 91  5 ? 5 
HELX_P HELX_P20 AC2 LEU D 105 ? THR D 111 ? LEU FFF 105 THR FFF 111 5 ? 7 
# 
_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 23  SG ? ? ? 1_555 A CYS 97  SG ? ? HHH CYS 22  HHH CYS 96  1_555 ? ? ? ? ? ? ? 2.018 ? ? 
disulf2 disulf ? ? A CYS 141 SG ? ? ? 1_555 A CYS 197 SG ? ? HHH CYS 144 HHH CYS 200 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf3 disulf ? ? B CYS 23  SG ? ? ? 1_555 B CYS 94  SG ? ? LLL CYS 23  LLL CYS 94  1_555 ? ? ? ? ? ? ? 2.086 ? ? 
disulf4 disulf ? ? B CYS 140 SG ? ? ? 1_555 B CYS 200 SG ? ? LLL CYS 140 LLL CYS 200 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf5 disulf ? ? C CYS 5   SG ? ? ? 1_555 C CYS 30  SG ? ? EEE CYS 336 EEE CYS 361 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
disulf6 disulf ? ? C CYS 48  SG ? ? ? 1_555 C CYS 101 SG ? ? EEE CYS 379 EEE CYS 432 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf7 disulf ? ? C CYS 60  SG ? ? ? 1_555 C CYS 194 SG ? ? EEE CYS 391 EEE CYS 525 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
disulf8 disulf ? ? C CYS 149 SG ? ? ? 1_555 C CYS 157 SG ? ? EEE CYS 480 EEE CYS 488 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf9 disulf ? ? D CYS 22  SG A ? ? 1_555 D CYS 96  SG A ? FFF CYS 22  FFF CYS 96  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 147 A . ? PHE 150 HHH PRO 148 A ? PRO 151 HHH 1 -16.96 
2 GLU 149 A . ? GLU 152 HHH PRO 150 A ? PRO 153 HHH 1 4.55   
3 SER 7   B . ? SER 7   LLL PRO 8   B ? PRO 8   LLL 1 -1.57  
4 THR 100 B . ? THR 100 LLL PRO 101 B ? PRO 101 LLL 1 2.95   
5 TYR 146 B . ? TYR 146 LLL PRO 147 B ? PRO 147 LLL 1 -9.13  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 6 ? 
AA9 ? 4 ? 
AB1 ? 2 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 2 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 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 GLN A 4   ? GLN A 7   ? GLN HHH 3   GLN HHH 6   
AA1 2 LEU A 19  ? SER A 26  ? LEU HHH 18  SER HHH 25  
AA1 3 THR A 79  ? TRP A 84  ? THR HHH 78  TRP HHH 83  
AA1 4 THR A 70  ? ASP A 74  ? THR HHH 69  ASP HHH 73  
AA2 1 GLU A 11  ? LYS A 13  ? GLU HHH 10  LYS HHH 12  
AA2 2 THR A 114 ? VAL A 118 ? THR HHH 113 VAL HHH 117 
AA2 3 ALA A 93  ? GLY A 100 ? ALA HHH 92  GLY HHH 99  
AA2 4 TRP A 34  ? GLN A 40  ? TRP HHH 33  GLN HHH 39  
AA2 5 GLU A 47  ? TYR A 53  ? GLU HHH 46  TYR HHH 52  
AA2 6 GLU A 58  ? TYR A 61  ? GLU HHH 57  TYR HHH 60  
AA3 1 GLU A 11  ? LYS A 13  ? GLU HHH 10  LYS HHH 12  
AA3 2 THR A 114 ? VAL A 118 ? THR HHH 113 VAL HHH 117 
AA3 3 ALA A 93  ? GLY A 100 ? ALA HHH 92  GLY HHH 99  
AA3 4 VAL A 109 ? TRP A 110 ? VAL HHH 108 TRP HHH 109 
AA4 1 SER A 125 ? LEU A 129 ? SER HHH 124 LEU HHH 128 
AA4 2 THR A 136 ? TYR A 146 ? THR HHH 139 TYR HHH 149 
AA4 3 TYR A 177 ? PRO A 186 ? TYR HHH 180 PRO HHH 189 
AA4 4 VAL A 164 ? THR A 166 ? VAL HHH 167 THR HHH 169 
AA5 1 SER A 125 ? LEU A 129 ? SER HHH 124 LEU HHH 128 
AA5 2 THR A 136 ? TYR A 146 ? THR HHH 139 TYR HHH 149 
AA5 3 TYR A 177 ? PRO A 186 ? TYR HHH 180 PRO HHH 189 
AA5 4 VAL A 170 ? LEU A 171 ? VAL HHH 173 LEU HHH 174 
AA6 1 THR A 152 ? TRP A 155 ? THR HHH 155 TRP HHH 158 
AA6 2 TYR A 195 ? HIS A 201 ? TYR HHH 198 HIS HHH 204 
AA6 3 THR A 206 ? VAL A 212 ? THR HHH 209 VAL HHH 215 
AA7 1 LEU B 4   ? SER B 7   ? LEU LLL 4   SER LLL 7   
AA7 2 ALA B 19  ? SER B 25  ? ALA LLL 19  SER LLL 25  
AA7 3 ASP B 76  ? ILE B 81  ? ASP LLL 76  ILE LLL 81  
AA7 4 PHE B 68  ? SER B 73  ? PHE LLL 68  SER LLL 73  
AA8 1 SER B 10  ? VAL B 13  ? SER LLL 10  VAL LLL 13  
AA8 2 THR B 108 ? ILE B 112 ? THR LLL 108 ILE LLL 112 
AA8 3 ALA B 90  ? GLN B 96  ? ALA LLL 90  GLN LLL 96  
AA8 4 LEU B 39  ? GLN B 44  ? LEU LLL 39  GLN LLL 44  
AA8 5 LYS B 51  ? TYR B 55  ? LYS LLL 51  TYR LLL 55  
AA8 6 THR B 59  ? ARG B 60  ? THR LLL 59  ARG LLL 60  
AA9 1 SER B 10  ? VAL B 13  ? SER LLL 10  VAL LLL 13  
AA9 2 THR B 108 ? ILE B 112 ? THR LLL 108 ILE LLL 112 
AA9 3 ALA B 90  ? GLN B 96  ? ALA LLL 90  GLN LLL 96  
AA9 4 THR B 103 ? PHE B 104 ? THR LLL 103 PHE LLL 104 
AB1 1 LEU B 30  ? TYR B 31  ? LEU LLL 30  TYR LLL 31  
AB1 2 LYS B 36  ? ASN B 37  ? LYS LLL 36  ASN LLL 37  
AB2 1 SER B 120 ? PHE B 124 ? SER LLL 120 PHE LLL 124 
AB2 2 THR B 135 ? PHE B 145 ? THR LLL 135 PHE LLL 145 
AB2 3 TYR B 179 ? SER B 188 ? TYR LLL 179 SER LLL 188 
AB2 4 SER B 165 ? VAL B 169 ? SER LLL 165 VAL LLL 169 
AB3 1 LEU B 160 ? GLN B 161 ? LEU LLL 160 GLN LLL 161 
AB3 2 ALA B 150 ? LYS B 155 ? ALA LLL 150 LYS LLL 155 
AB3 3 VAL B 197 ? HIS B 204 ? VAL LLL 197 HIS LLL 204 
AB3 4 VAL B 211 ? ASN B 216 ? VAL LLL 211 ASN LLL 216 
AB4 1 ASN C 23  ? ILE C 27  ? ASN EEE 354 ILE EEE 358 
AB4 2 ASN C 63  ? ARG C 72  ? ASN EEE 394 ARG EEE 403 
AB4 3 PRO C 176 ? GLU C 185 ? PRO EEE 507 GLU EEE 516 
AB4 4 GLY C 100 ? ASN C 106 ? GLY EEE 431 ASN EEE 437 
AB4 5 THR C 45  ? TYR C 49  ? THR EEE 376 TYR EEE 380 
AB5 1 CYS C 30  ? VAL C 31  ? CYS EEE 361 VAL EEE 362 
AB5 2 VAL C 193 ? CYS C 194 ? VAL EEE 524 CYS EEE 525 
AB5 3 CYS C 60  ? PHE C 61  ? CYS EEE 391 PHE EEE 392 
AB6 1 LEU C 121 ? ARG C 123 ? LEU EEE 452 ARG EEE 454 
AB6 2 LEU C 161 ? SER C 163 ? LEU EEE 492 SER EEE 494 
AB7 1 TYR C 142 ? GLN C 143 ? TYR EEE 473 GLN EEE 474 
AB7 2 CYS C 157 ? TYR C 158 ? CYS EEE 488 TYR EEE 489 
AB8 1 VAL D 2   ? SER D 7   ? VAL FFF 2   SER FFF 7   
AB8 2 LEU D 18  ? GLY D 26  ? LEU FFF 18  GLY FFF 26  
AB8 3 THR D 78  ? MET D 83  ? THR FFF 78  MET FFF 83  
AB8 4 PHE D 68  ? ASP D 73  ? PHE FFF 68  ASP FFF 73  
AB9 1 LEU D 11  ? GLN D 13  ? LEU FFF 11  GLN FFF 13  
AB9 2 THR D 121 ? SER D 126 ? THR FFF 121 SER FFF 126 
AB9 3 ALA D 92  ? THR D 99  ? ALA FFF 92  THR FFF 99  
AB9 4 ALA D 33  ? GLN D 39  ? ALA FFF 33  GLN FFF 39  
AB9 5 GLU D 46  ? ARG D 52  ? GLU FFF 46  ARG FFF 52  
AB9 6 ALA D 58  ? TYR D 60  ? ALA FFF 58  TYR FFF 60  
AC1 1 LEU D 11  ? GLN D 13  ? LEU FFF 11  GLN FFF 13  
AC1 2 THR D 121 ? SER D 126 ? THR FFF 121 SER FFF 126 
AC1 3 ALA D 92  ? THR D 99  ? ALA FFF 92  THR FFF 99  
AC1 4 TYR D 116 ? TRP D 117 ? TYR FFF 116 TRP FFF 117 
# 
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 GLN A 4   ? N GLN HHH 3   O SER A 26  ? O SER HHH 25  
AA1 2 3 N LEU A 19  ? N LEU HHH 18  O TRP A 84  ? O TRP HHH 83  
AA1 3 4 O TYR A 81  ? O TYR HHH 80  N SER A 72  ? N SER HHH 71  
AA2 1 2 N LYS A 13  ? N LYS HHH 12  O THR A 117 ? O THR HHH 116 
AA2 2 3 O THR A 114 ? O THR HHH 113 N TYR A 95  ? N TYR HHH 94  
AA2 3 4 O ALA A 98  ? O ALA HHH 97  N GLY A 36  ? N GLY HHH 35  
AA2 4 5 N ARG A 39  ? N ARG HHH 38  O GLU A 47  ? O GLU HHH 46  
AA2 5 6 N ILE A 51  ? N ILE HHH 50  O ARG A 60  ? O ARG HHH 59  
AA3 1 2 N LYS A 13  ? N LYS HHH 12  O THR A 117 ? O THR HHH 116 
AA3 2 3 O THR A 114 ? O THR HHH 113 N TYR A 95  ? N TYR HHH 94  
AA3 3 4 N GLY A 99  ? N GLY HHH 98  O VAL A 109 ? O VAL HHH 108 
AA4 1 2 N PHE A 127 ? N PHE HHH 126 O LEU A 142 ? O LEU HHH 145 
AA4 2 3 N TYR A 146 ? N TYR HHH 149 O TYR A 177 ? O TYR HHH 180 
AA4 3 4 O VAL A 182 ? O VAL HHH 185 N HIS A 165 ? N HIS HHH 168 
AA5 1 2 N PHE A 127 ? N PHE HHH 126 O LEU A 142 ? O LEU HHH 145 
AA5 2 3 N TYR A 146 ? N TYR HHH 149 O TYR A 177 ? O TYR HHH 180 
AA5 3 4 O SER A 178 ? O SER HHH 181 N VAL A 170 ? N VAL HHH 173 
AA6 1 2 N SER A 154 ? N SER HHH 157 O ASN A 198 ? O ASN HHH 201 
AA6 2 3 N VAL A 199 ? N VAL HHH 202 O VAL A 208 ? O VAL HHH 211 
AA7 1 2 N SER B 7   ? N SER LLL 7   O ASN B 22  ? O ASN LLL 22  
AA7 2 3 N ALA B 19  ? N ALA LLL 19  O ILE B 81  ? O ILE LLL 81  
AA7 3 4 O THR B 78  ? O THR LLL 78  N SER B 71  ? N SER LLL 71  
AA8 1 2 N VAL B 13  ? N VAL LLL 13  O GLU B 111 ? O GLU LLL 111 
AA8 2 3 O THR B 108 ? O THR LLL 108 N TYR B 92  ? N TYR LLL 92  
AA8 3 4 O TYR B 93  ? O TYR LLL 93  N TYR B 42  ? N TYR LLL 42  
AA8 4 5 N GLN B 43  ? N GLN LLL 43  O LYS B 51  ? O LYS LLL 51  
AA8 5 6 N TYR B 55  ? N TYR LLL 55  O THR B 59  ? O THR LLL 59  
AA9 1 2 N VAL B 13  ? N VAL LLL 13  O GLU B 111 ? O GLU LLL 111 
AA9 2 3 O THR B 108 ? O THR LLL 108 N TYR B 92  ? N TYR LLL 92  
AA9 3 4 N GLN B 96  ? N GLN LLL 96  O THR B 103 ? O THR LLL 103 
AB1 1 2 N TYR B 31  ? N TYR LLL 31  O LYS B 36  ? O LYS LLL 36  
AB2 1 2 N PHE B 122 ? N PHE LLL 122 O LEU B 141 ? O LEU LLL 141 
AB2 2 3 N VAL B 138 ? N VAL LLL 138 O LEU B 185 ? O LEU LLL 185 
AB2 3 4 O THR B 184 ? O THR LLL 184 N GLN B 166 ? N GLN LLL 166 
AB3 1 2 O GLN B 161 ? O GLN LLL 161 N TRP B 154 ? N TRP LLL 154 
AB3 2 3 N GLN B 153 ? N GLN LLL 153 O GLU B 201 ? O GLU LLL 201 
AB3 3 4 N TYR B 198 ? N TYR LLL 198 O PHE B 215 ? O PHE LLL 215 
AB4 1 2 N ILE C 27  ? N ILE EEE 358 O VAL C 64  ? O VAL EEE 395 
AB4 2 3 N ILE C 71  ? N ILE EEE 402 O TYR C 177 ? O TYR EEE 508 
AB4 3 4 O VAL C 180 ? O VAL EEE 511 N ILE C 103 ? N ILE EEE 434 
AB4 4 5 O VAL C 102 ? O VAL EEE 433 N LYS C 47  ? N LYS EEE 378 
AB5 1 2 N CYS C 30  ? N CYS EEE 361 O CYS C 194 ? O CYS EEE 525 
AB5 2 3 O VAL C 193 ? O VAL EEE 524 N PHE C 61  ? N PHE EEE 392 
AB6 1 2 N TYR C 122 ? N TYR EEE 453 O GLN C 162 ? O GLN EEE 493 
AB7 1 2 N TYR C 142 ? N TYR EEE 473 O TYR C 158 ? O TYR EEE 489 
AB8 1 2 N VAL D 5   ? N VAL FFF 5   O ALA D 23  ? O ALA FFF 23  
AB8 2 3 N LEU D 18  ? N LEU FFF 18  O MET D 83  ? O MET FFF 83  
AB8 3 4 O GLN D 82  ? O GLN FFF 82  N THR D 69  ? N THR FFF 69  
AB9 1 2 N MET D 12  ? N MET FFF 12  O SER D 126 ? O SER FFF 126 
AB9 2 3 O THR D 121 ? O THR FFF 121 N TYR D 94  ? N TYR FFF 94  
AB9 3 4 O TYR D 95  ? O TYR FFF 95  N PHE D 37  ? N PHE FFF 37  
AB9 4 5 N TRP D 36  ? N TRP FFF 36  O ALA D 49  ? O ALA FFF 49  
AB9 5 6 N ALA D 50  ? N ALA FFF 50  O TYR D 59  ? O TYR FFF 59  
AC1 1 2 N MET D 12  ? N MET FFF 12  O SER D 126 ? O SER FFF 126 
AC1 2 3 O THR D 121 ? O THR FFF 121 N TYR D 94  ? N TYR FFF 94  
AC1 3 4 N GLN D 98  ? N GLN FFF 98  O TYR D 116 ? O TYR FFF 116 
# 
_atom_sites.entry_id                    6ZH9 
_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]   0.006393 
_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]   0.006393 
_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]   0.008605 
_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 1.049   
# 
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 1   ? 46.107  -39.565 -60.745  1.000 199.006 ? 0   THR HHH N   1 
ATOM 2    C CA  . THR A 1 1   ? 44.895  -40.406 -61.019  1.000 188.018 ? 0   THR HHH CA  1 
ATOM 3    C C   . THR A 1 1   ? 44.775  -40.683 -62.528  1.000 173.536 ? 0   THR HHH C   1 
ATOM 4    O O   . THR A 1 1   ? 45.089  -39.779 -63.298  1.000 167.833 ? 0   THR HHH O   1 
ATOM 5    C CB  . THR A 1 1   ? 43.649  -39.704 -60.474  1.000 185.325 ? 0   THR HHH CB  1 
ATOM 6    O OG1 . THR A 1 1   ? 42.532  -40.493 -60.879  1.000 195.981 ? 0   THR HHH OG1 1 
ATOM 7    C CG2 . THR A 1 1   ? 43.514  -38.276 -60.959  1.000 181.274 ? 0   THR HHH CG2 1 
ATOM 8    N N   . GLN A 1 2   ? 44.336  -41.877 -62.940  1.000 160.002 ? 1   GLN HHH N   1 
ATOM 9    C CA  . GLN A 1 2   ? 44.088  -42.189 -64.374  1.000 161.664 ? 1   GLN HHH CA  1 
ATOM 10   C C   . GLN A 1 2   ? 42.941  -41.317 -64.893  1.000 167.543 ? 1   GLN HHH C   1 
ATOM 11   O O   . GLN A 1 2   ? 43.158  -40.656 -65.972  1.000 182.170 ? 1   GLN HHH O   1 
ATOM 12   C CB  . GLN A 1 2   ? 43.741  -43.664 -64.615  1.000 164.325 ? 1   GLN HHH CB  1 
ATOM 13   C CG  . GLN A 1 2   ? 43.301  -43.990 -66.050  1.000 163.638 ? 1   GLN HHH CG  1 
ATOM 14   C CD  . GLN A 1 2   ? 44.406  -43.895 -67.079  1.000 166.378 ? 1   GLN HHH CD  1 
ATOM 15   O OE1 . GLN A 1 2   ? 45.122  -44.862 -67.294  1.000 168.559 ? 1   GLN HHH OE1 1 
ATOM 16   N NE2 . GLN A 1 2   ? 44.549  -42.748 -67.744  1.000 168.770 ? 1   GLN HHH NE2 1 
ATOM 17   N N   . MET A 1 3   ? 41.785  -41.358 -64.202  1.000 148.357 ? 2   MET HHH N   1 
ATOM 18   C CA  . MET A 1 3   ? 40.478  -40.829 -64.692  1.000 145.935 ? 2   MET HHH CA  1 
ATOM 19   C C   . MET A 1 3   ? 39.675  -40.268 -63.529  1.000 140.822 ? 2   MET HHH C   1 
ATOM 20   O O   . MET A 1 3   ? 39.510  -41.014 -62.553  1.000 149.804 ? 2   MET HHH O   1 
ATOM 21   C CB  . MET A 1 3   ? 39.639  -41.923 -65.367  1.000 146.638 ? 2   MET HHH CB  1 
ATOM 22   C CG  . MET A 1 3   ? 38.317  -41.442 -65.979  1.000 148.919 ? 2   MET HHH CG  1 
ATOM 23   S SD  . MET A 1 3   ? 38.518  -40.134 -67.197  1.000 161.849 ? 2   MET HHH SD  1 
ATOM 24   C CE  . MET A 1 3   ? 39.666  -40.899 -68.354  1.000 159.400 ? 2   MET HHH CE  1 
ATOM 25   N N   . GLN A 1 4   ? 39.168  -39.037 -63.661  1.000 144.047 ? 3   GLN HHH N   1 
ATOM 26   C CA  . GLN A 1 4   ? 38.099  -38.497 -62.768  1.000 160.173 ? 3   GLN HHH CA  1 
ATOM 27   C C   . GLN A 1 4   ? 36.963  -37.922 -63.626  1.000 165.125 ? 3   GLN HHH C   1 
ATOM 28   O O   . GLN A 1 4   ? 37.258  -37.342 -64.654  1.000 172.040 ? 3   GLN HHH O   1 
ATOM 29   C CB  . GLN A 1 4   ? 38.659  -37.457 -61.786  1.000 161.855 ? 3   GLN HHH CB  1 
ATOM 30   C CG  . GLN A 1 4   ? 38.778  -36.028 -62.319  1.000 162.859 ? 3   GLN HHH CG  1 
ATOM 31   C CD  . GLN A 1 4   ? 38.824  -35.078 -61.132  1.000 155.464 ? 3   GLN HHH CD  1 
ATOM 32   O OE1 . GLN A 1 4   ? 37.969  -35.123 -60.231  1.000 138.823 ? 3   GLN HHH OE1 1 
ATOM 33   N NE2 . GLN A 1 4   ? 39.868  -34.263 -61.067  1.000 159.830 ? 3   GLN HHH NE2 1 
ATOM 34   N N   . LEU A 1 5   ? 35.706  -38.092 -63.216  1.000 157.311 ? 4   LEU HHH N   1 
ATOM 35   C CA  . LEU A 1 5   ? 34.540  -37.589 -63.985  1.000 147.704 ? 4   LEU HHH CA  1 
ATOM 36   C C   . LEU A 1 5   ? 34.024  -36.374 -63.243  1.000 153.041 ? 4   LEU HHH C   1 
ATOM 37   O O   . LEU A 1 5   ? 34.037  -36.409 -61.999  1.000 173.608 ? 4   LEU HHH O   1 
ATOM 38   C CB  . LEU A 1 5   ? 33.470  -38.684 -64.037  1.000 144.050 ? 4   LEU HHH CB  1 
ATOM 39   C CG  . LEU A 1 5   ? 33.987  -40.111 -64.258  1.000 143.402 ? 4   LEU HHH CG  1 
ATOM 40   C CD1 . LEU A 1 5   ? 32.942  -41.133 -63.859  1.000 130.751 ? 4   LEU HHH CD1 1 
ATOM 41   C CD2 . LEU A 1 5   ? 34.449  -40.348 -65.709  1.000 151.944 ? 4   LEU HHH CD2 1 
ATOM 42   N N   . VAL A 1 6   ? 33.604  -35.351 -63.963  1.000 150.601 ? 5   VAL HHH N   1 
ATOM 43   C CA  . VAL A 1 6   ? 33.013  -34.118 -63.369  1.000 161.910 ? 5   VAL HHH CA  1 
ATOM 44   C C   . VAL A 1 6   ? 31.583  -33.947 -63.885  1.000 165.233 ? 5   VAL HHH C   1 
ATOM 45   O O   . VAL A 1 6   ? 31.392  -34.091 -65.106  1.000 186.503 ? 5   VAL HHH O   1 
ATOM 46   C CB  . VAL A 1 6   ? 33.875  -32.897 -63.720  1.000 164.963 ? 5   VAL HHH CB  1 
ATOM 47   C CG1 . VAL A 1 6   ? 33.335  -31.638 -63.044  1.000 174.828 ? 5   VAL HHH CG1 1 
ATOM 48   C CG2 . VAL A 1 6   ? 35.347  -33.172 -63.411  1.000 156.327 ? 5   VAL HHH CG2 1 
ATOM 49   N N   . GLN A 1 7   ? 30.634  -33.614 -63.004  1.000 163.044 ? 6   GLN HHH N   1 
ATOM 50   C CA  . GLN A 1 7   ? 29.188  -33.549 -63.348  1.000 164.676 ? 6   GLN HHH CA  1 
ATOM 51   C C   . GLN A 1 7   ? 28.711  -32.107 -63.244  1.000 167.720 ? 6   GLN HHH C   1 
ATOM 52   O O   . GLN A 1 7   ? 29.392  -31.317 -62.545  1.000 157.235 ? 6   GLN HHH O   1 
ATOM 53   C CB  . GLN A 1 7   ? 28.326  -34.452 -62.468  1.000 161.214 ? 6   GLN HHH CB  1 
ATOM 54   C CG  . GLN A 1 7   ? 28.773  -35.908 -62.504  1.000 165.073 ? 6   GLN HHH CG  1 
ATOM 55   C CD  . GLN A 1 7   ? 27.785  -36.858 -61.868  1.000 156.938 ? 6   GLN HHH CD  1 
ATOM 56   O OE1 . GLN A 1 7   ? 28.157  -37.728 -61.081  1.000 132.950 ? 6   GLN HHH OE1 1 
ATOM 57   N NE2 . GLN A 1 7   ? 26.511  -36.681 -62.197  1.000 166.383 ? 6   GLN HHH NE2 1 
ATOM 58   N N   . SER A 1 8   ? 27.601  -31.828 -63.950  1.000 166.303 ? 7   SER HHH N   1 
ATOM 59   C CA  . SER A 1 8   ? 26.944  -30.508 -64.129  1.000 162.862 ? 7   SER HHH CA  1 
ATOM 60   C C   . SER A 1 8   ? 26.404  -30.010 -62.788  1.000 173.100 ? 7   SER HHH C   1 
ATOM 61   O O   . SER A 1 8   ? 26.137  -30.873 -61.923  1.000 202.319 ? 7   SER HHH O   1 
ATOM 62   C CB  . SER A 1 8   ? 25.845  -30.618 -65.141  1.000 162.414 ? 7   SER HHH CB  1 
ATOM 63   O OG  . SER A 1 8   ? 24.816  -31.493 -64.702  1.000 160.230 ? 7   SER HHH OG  1 
ATOM 64   N N   . GLY A 1 9   ? 26.231  -28.690 -62.628  1.000 173.595 ? 8   GLY HHH N   1 
ATOM 65   C CA  . GLY A 1 9   ? 25.735  -28.041 -61.386  1.000 177.702 ? 8   GLY HHH CA  1 
ATOM 66   C C   . GLY A 1 9   ? 24.363  -28.542 -60.962  1.000 174.456 ? 8   GLY HHH C   1 
ATOM 67   O O   . GLY A 1 9   ? 23.691  -29.154 -61.817  1.000 176.396 ? 8   GLY HHH O   1 
ATOM 68   N N   . THR A 1 10  ? 23.955  -28.338 -59.701  1.000 182.235 ? 9   THR HHH N   1 
ATOM 69   C CA  . THR A 1 10  ? 22.646  -28.866 -59.196  1.000 204.683 ? 9   THR HHH CA  1 
ATOM 70   C C   . THR A 1 10  ? 21.511  -28.034 -59.822  1.000 208.907 ? 9   THR HHH C   1 
ATOM 71   O O   . THR A 1 10  ? 21.688  -26.811 -59.978  1.000 208.918 ? 9   THR HHH O   1 
ATOM 72   C CB  . THR A 1 10  ? 22.531  -28.954 -57.662  1.000 203.660 ? 9   THR HHH CB  1 
ATOM 73   O OG1 . THR A 1 10  ? 22.439  -27.634 -57.130  1.000 214.774 ? 9   THR HHH OG1 1 
ATOM 74   C CG2 . THR A 1 10  ? 23.672  -29.703 -57.009  1.000 198.834 ? 9   THR HHH CG2 1 
ATOM 75   N N   . GLU A 1 11  ? 20.402  -28.684 -60.188  1.000 200.949 ? 10  GLU HHH N   1 
ATOM 76   C CA  . GLU A 1 11  ? 19.376  -28.113 -61.092  1.000 195.031 ? 10  GLU HHH CA  1 
ATOM 77   C C   . GLU A 1 11  ? 18.085  -27.927 -60.305  1.000 196.821 ? 10  GLU HHH C   1 
ATOM 78   O O   . GLU A 1 11  ? 17.673  -28.899 -59.654  1.000 187.778 ? 10  GLU HHH O   1 
ATOM 79   C CB  . GLU A 1 11  ? 19.200  -29.005 -62.320  1.000 192.968 ? 10  GLU HHH CB  1 
ATOM 80   C CG  . GLU A 1 11  ? 20.427  -29.025 -63.223  1.000 204.361 ? 10  GLU HHH CG  1 
ATOM 81   C CD  . GLU A 1 11  ? 20.531  -27.917 -64.265  1.000 228.744 ? 10  GLU HHH CD  1 
ATOM 82   O OE1 . GLU A 1 11  ? 19.507  -27.249 -64.518  1.000 242.879 ? 10  GLU HHH OE1 1 
ATOM 83   O OE2 . GLU A 1 11  ? 21.646  -27.717 -64.822  1.000 242.034 ? 10  GLU HHH OE2 1 
ATOM 84   N N   . VAL A 1 12  ? 17.520  -26.713 -60.385  1.000 202.351 ? 11  VAL HHH N   1 
ATOM 85   C CA  . VAL A 1 12  ? 16.200  -26.280 -59.834  1.000 198.018 ? 11  VAL HHH CA  1 
ATOM 86   C C   . VAL A 1 12  ? 15.212  -26.097 -61.002  1.000 201.367 ? 11  VAL HHH C   1 
ATOM 87   O O   . VAL A 1 12  ? 15.150  -24.986 -61.608  1.000 192.501 ? 11  VAL HHH O   1 
ATOM 88   C CB  . VAL A 1 12  ? 16.387  -25.004 -58.993  1.000 201.021 ? 11  VAL HHH CB  1 
ATOM 89   C CG1 . VAL A 1 12  ? 15.070  -24.406 -58.524  1.000 203.474 ? 11  VAL HHH CG1 1 
ATOM 90   C CG2 . VAL A 1 12  ? 17.304  -25.277 -57.810  1.000 198.505 ? 11  VAL HHH CG2 1 
ATOM 91   N N   . LYS A 1 13  ? 14.472  -27.170 -61.311  1.000 201.786 ? 12  LYS HHH N   1 
ATOM 92   C CA  . LYS A 1 13  ? 13.560  -27.285 -62.480  1.000 201.781 ? 12  LYS HHH CA  1 
ATOM 93   C C   . LYS A 1 13  ? 12.124  -27.384 -61.971  1.000 210.283 ? 12  LYS HHH C   1 
ATOM 94   O O   . LYS A 1 13  ? 11.942  -27.557 -60.757  1.000 224.335 ? 12  LYS HHH O   1 
ATOM 95   C CB  . LYS A 1 13  ? 13.945  -28.497 -63.334  1.000 191.453 ? 12  LYS HHH CB  1 
ATOM 96   C CG  . LYS A 1 13  ? 15.352  -28.442 -63.927  1.000 191.318 ? 12  LYS HHH CG  1 
ATOM 97   C CD  . LYS A 1 13  ? 15.460  -27.823 -65.317  1.000 190.849 ? 12  LYS HHH CD  1 
ATOM 98   C CE  . LYS A 1 13  ? 15.607  -26.317 -65.305  1.000 191.788 ? 12  LYS HHH CE  1 
ATOM 99   N NZ  . LYS A 1 13  ? 15.485  -25.782 -66.677  1.000 199.780 ? 12  LYS HHH NZ  1 
ATOM 100  N N   . LYS A 1 14  ? 11.142  -27.226 -62.857  1.000 210.670 ? 13  LYS HHH N   1 
ATOM 101  C CA  . LYS A 1 14  ? 9.706   -27.287 -62.488  1.000 207.805 ? 13  LYS HHH CA  1 
ATOM 102  C C   . LYS A 1 14  ? 9.007   -28.209 -63.471  1.000 198.438 ? 13  LYS HHH C   1 
ATOM 103  O O   . LYS A 1 14  ? 9.422   -28.348 -64.618  1.000 193.251 ? 13  LYS HHH O   1 
ATOM 104  C CB  . LYS A 1 14  ? 9.082   -25.893 -62.446  1.000 210.193 ? 13  LYS HHH CB  1 
ATOM 105  C CG  . LYS A 1 14  ? 9.086   -25.177 -63.781  1.000 221.331 ? 13  LYS HHH CG  1 
ATOM 106  C CD  . LYS A 1 14  ? 8.011   -24.156 -63.901  1.000 241.193 ? 13  LYS HHH CD  1 
ATOM 107  C CE  . LYS A 1 14  ? 8.083   -23.110 -62.813  1.000 252.146 ? 13  LYS HHH CE  1 
ATOM 108  N NZ  . LYS A 1 14  ? 7.096   -22.034 -63.065  1.000 267.557 ? 13  LYS HHH NZ  1 
ATOM 109  N N   . PRO A 1 15  ? 7.920   -28.864 -63.028  1.000 197.698 ? 14  PRO HHH N   1 
ATOM 110  C CA  . PRO A 1 15  ? 7.332   -29.962 -63.786  1.000 196.118 ? 14  PRO HHH CA  1 
ATOM 111  C C   . PRO A 1 15  ? 7.030   -29.543 -65.227  1.000 196.748 ? 14  PRO HHH C   1 
ATOM 112  O O   . PRO A 1 15  ? 6.480   -28.484 -65.409  1.000 199.328 ? 14  PRO HHH O   1 
ATOM 113  C CB  . PRO A 1 15  ? 6.037   -30.281 -63.019  1.000 203.082 ? 14  PRO HHH CB  1 
ATOM 114  C CG  . PRO A 1 15  ? 6.276   -29.762 -61.610  1.000 203.177 ? 14  PRO HHH CG  1 
ATOM 115  C CD  . PRO A 1 15  ? 7.195   -28.572 -61.778  1.000 202.526 ? 14  PRO HHH CD  1 
ATOM 116  N N   . GLY A 1 16  ? 7.399   -30.374 -66.203  1.000 202.424 ? 15  GLY HHH N   1 
ATOM 117  C CA  . GLY A 1 16  ? 7.114   -30.124 -67.631  1.000 215.705 ? 15  GLY HHH CA  1 
ATOM 118  C C   . GLY A 1 16  ? 8.345   -29.678 -68.409  1.000 217.114 ? 15  GLY HHH C   1 
ATOM 119  O O   . GLY A 1 16  ? 8.437   -30.029 -69.612  1.000 219.281 ? 15  GLY HHH O   1 
ATOM 120  N N   . GLU A 1 17  ? 9.242   -28.919 -67.762  1.000 213.506 ? 16  GLU HHH N   1 
ATOM 121  C CA  . GLU A 1 17  ? 10.543  -28.484 -68.337  1.000 205.783 ? 16  GLU HHH CA  1 
ATOM 122  C C   . GLU A 1 17  ? 11.320  -29.735 -68.710  1.000 192.963 ? 16  GLU HHH C   1 
ATOM 123  O O   . GLU A 1 17  ? 11.091  -30.785 -68.082  1.000 203.907 ? 16  GLU HHH O   1 
ATOM 124  C CB  . GLU A 1 17  ? 11.387  -27.664 -67.358  1.000 208.198 ? 16  GLU HHH CB  1 
ATOM 125  C CG  . GLU A 1 17  ? 10.752  -26.345 -66.949  1.000 226.685 ? 16  GLU HHH CG  1 
ATOM 126  C CD  . GLU A 1 17  ? 11.603  -25.453 -66.054  1.000 234.458 ? 16  GLU HHH CD  1 
ATOM 127  O OE1 . GLU A 1 17  ? 11.935  -24.322 -66.481  1.000 241.980 ? 16  GLU HHH OE1 1 
ATOM 128  O OE2 . GLU A 1 17  ? 11.913  -25.876 -64.920  1.000 251.222 ? 16  GLU HHH OE2 1 
ATOM 129  N N   . SER A 1 18  ? 12.208  -29.628 -69.683  1.000 190.611 ? 17  SER HHH N   1 
ATOM 130  C CA  . SER A 1 18  ? 13.201  -30.689 -69.952  1.000 201.908 ? 17  SER HHH CA  1 
ATOM 131  C C   . SER A 1 18  ? 14.554  -30.253 -69.381  1.000 210.729 ? 17  SER HHH C   1 
ATOM 132  O O   . SER A 1 18  ? 14.715  -29.048 -69.021  1.000 209.787 ? 17  SER HHH O   1 
ATOM 133  C CB  . SER A 1 18  ? 13.282  -31.033 -71.406  1.000 207.430 ? 17  SER HHH CB  1 
ATOM 134  O OG  . SER A 1 18  ? 13.787  -29.924 -72.134  1.000 218.285 ? 17  SER HHH OG  1 
ATOM 135  N N   . LEU A 1 19  ? 15.459  -31.232 -69.281  1.000 218.026 ? 18  LEU HHH N   1 
ATOM 136  C CA  . LEU A 1 19  ? 16.785  -31.149 -68.624  1.000 210.920 ? 18  LEU HHH CA  1 
ATOM 137  C C   . LEU A 1 19  ? 17.736  -32.185 -69.242  1.000 203.851 ? 18  LEU HHH C   1 
ATOM 138  O O   . LEU A 1 19  ? 17.337  -33.355 -69.442  1.000 193.126 ? 18  LEU HHH O   1 
ATOM 139  C CB  . LEU A 1 19  ? 16.591  -31.418 -67.134  1.000 206.698 ? 18  LEU HHH CB  1 
ATOM 140  C CG  . LEU A 1 19  ? 17.877  -31.555 -66.332  1.000 211.789 ? 18  LEU HHH CG  1 
ATOM 141  C CD1 . LEU A 1 19  ? 18.558  -30.198 -66.175  1.000 225.674 ? 18  LEU HHH CD1 1 
ATOM 142  C CD2 . LEU A 1 19  ? 17.594  -32.186 -64.980  1.000 213.851 ? 18  LEU HHH CD2 1 
ATOM 143  N N   . LYS A 1 20  ? 18.959  -31.761 -69.544  1.000 194.848 ? 19  LYS HHH N   1 
ATOM 144  C CA  . LYS A 1 20  ? 20.031  -32.658 -70.032  1.000 190.240 ? 19  LYS HHH CA  1 
ATOM 145  C C   . LYS A 1 20  ? 21.272  -32.367 -69.191  1.000 183.524 ? 19  LYS HHH C   1 
ATOM 146  O O   . LYS A 1 20  ? 21.928  -31.345 -69.454  1.000 185.973 ? 19  LYS HHH O   1 
ATOM 147  C CB  . LYS A 1 20  ? 20.244  -32.453 -71.535  1.000 199.995 ? 19  LYS HHH CB  1 
ATOM 148  C CG  . LYS A 1 20  ? 21.455  -33.166 -72.135  1.000 204.632 ? 19  LYS HHH CG  1 
ATOM 149  C CD  . LYS A 1 20  ? 21.550  -33.077 -73.650  1.000 213.053 ? 19  LYS HHH CD  1 
ATOM 150  C CE  . LYS A 1 20  ? 22.917  -32.592 -74.105  1.000 222.456 ? 19  LYS HHH CE  1 
ATOM 151  N NZ  . LYS A 1 20  ? 23.038  -32.427 -75.575  1.000 229.729 ? 19  LYS HHH NZ  1 
ATOM 152  N N   . ILE A 1 21  ? 21.526  -33.188 -68.172  1.000 173.741 ? 20  ILE HHH N   1 
ATOM 153  C CA  . ILE A 1 21  ? 22.720  -33.045 -67.291  1.000 166.897 ? 20  ILE HHH CA  1 
ATOM 154  C C   . ILE A 1 21  ? 23.873  -33.775 -67.975  1.000 154.420 ? 20  ILE HHH C   1 
ATOM 155  O O   . ILE A 1 21  ? 23.608  -34.670 -68.805  1.000 139.625 ? 20  ILE HHH O   1 
ATOM 156  C CB  . ILE A 1 21  ? 22.473  -33.560 -65.856  1.000 178.493 ? 20  ILE HHH CB  1 
ATOM 157  C CG1 . ILE A 1 21  ? 22.083  -35.044 -65.831  1.000 181.476 ? 20  ILE HHH CG1 1 
ATOM 158  C CG2 . ILE A 1 21  ? 21.463  -32.683 -65.124  1.000 174.566 ? 20  ILE HHH CG2 1 
ATOM 159  C CD1 . ILE A 1 21  ? 21.953  -35.604 -64.438  1.000 180.918 ? 20  ILE HHH CD1 1 
ATOM 160  N N   . SER A 1 22  ? 25.092  -33.427 -67.575  1.000 153.663 ? 21  SER HHH N   1 
ATOM 161  C CA  . SER A 1 22  ? 26.353  -33.906 -68.178  1.000 154.662 ? 21  SER HHH CA  1 
ATOM 162  C C   . SER A 1 22  ? 27.295  -34.458 -67.107  1.000 177.124 ? 21  SER HHH C   1 
ATOM 163  O O   . SER A 1 22  ? 27.015  -34.298 -65.837  1.000 184.175 ? 21  SER HHH O   1 
ATOM 164  C CB  . SER A 1 22  ? 27.012  -32.813 -68.894  1.000 153.393 ? 21  SER HHH CB  1 
ATOM 165  O OG  . SER A 1 22  ? 27.459  -31.841 -67.966  1.000 149.397 ? 21  SER HHH OG  1 
ATOM 166  N N   . CYS A 1 23  ? 28.351  -35.103 -67.629  1.000 180.767 ? 22  CYS HHH N   1 
ATOM 167  C CA  . CYS A 1 23  ? 29.420  -35.842 -66.897  1.000 169.684 ? 22  CYS HHH CA  1 
ATOM 168  C C   . CYS A 1 23  ? 30.615  -35.957 -67.848  1.000 162.076 ? 22  CYS HHH C   1 
ATOM 169  O O   . CYS A 1 23  ? 30.529  -36.748 -68.788  1.000 153.869 ? 22  CYS HHH O   1 
ATOM 170  C CB  . CYS A 1 23  ? 28.946  -37.215 -66.442  1.000 155.416 ? 22  CYS HHH CB  1 
ATOM 171  S SG  . CYS A 1 23  ? 30.312  -38.285 -65.959  1.000 155.847 ? 22  CYS HHH SG  1 
ATOM 172  N N   . LYS A 1 24  ? 31.647  -35.136 -67.638  1.000 163.524 ? 23  LYS HHH N   1 
ATOM 173  C CA  . LYS A 1 24  ? 32.841  -35.015 -68.517  1.000 163.402 ? 23  LYS HHH CA  1 
ATOM 174  C C   . LYS A 1 24  ? 34.005  -35.789 -67.908  1.000 154.164 ? 23  LYS HHH C   1 
ATOM 175  O O   . LYS A 1 24  ? 34.404  -35.417 -66.808  1.000 163.341 ? 23  LYS HHH O   1 
ATOM 176  C CB  . LYS A 1 24  ? 33.213  -33.541 -68.636  1.000 159.071 ? 23  LYS HHH CB  1 
ATOM 177  C CG  . LYS A 1 24  ? 34.305  -33.193 -69.643  1.000 159.448 ? 23  LYS HHH CG  1 
ATOM 178  C CD  . LYS A 1 24  ? 34.256  -31.696 -69.953  1.000 162.529 ? 23  LYS HHH CD  1 
ATOM 179  C CE  . LYS A 1 24  ? 35.539  -31.110 -70.481  1.000 155.692 ? 23  LYS HHH CE  1 
ATOM 180  N NZ  . LYS A 1 24  ? 35.657  -31.384 -71.925  1.000 162.862 ? 23  LYS HHH NZ  1 
ATOM 181  N N   . GLY A 1 25  ? 34.517  -36.817 -68.587  1.000 151.614 ? 24  GLY HHH N   1 
ATOM 182  C CA  . GLY A 1 25  ? 35.666  -37.621 -68.122  1.000 152.701 ? 24  GLY HHH CA  1 
ATOM 183  C C   . GLY A 1 25  ? 36.988  -36.885 -68.355  1.000 156.055 ? 24  GLY HHH C   1 
ATOM 184  O O   . GLY A 1 25  ? 37.268  -36.522 -69.521  1.000 161.179 ? 24  GLY HHH O   1 
ATOM 185  N N   . SER A 1 26  ? 37.778  -36.655 -67.291  1.000 154.431 ? 25  SER HHH N   1 
ATOM 186  C CA  . SER A 1 26  ? 39.091  -35.950 -67.323  1.000 151.754 ? 25  SER HHH CA  1 
ATOM 187  C C   . SER A 1 26  ? 40.189  -36.978 -67.159  1.000 149.660 ? 25  SER HHH C   1 
ATOM 188  O O   . SER A 1 26  ? 40.346  -37.493 -66.041  1.000 145.011 ? 25  SER HHH O   1 
ATOM 189  C CB  . SER A 1 26  ? 39.244  -34.911 -66.260  1.000 146.965 ? 25  SER HHH CB  1 
ATOM 190  O OG  . SER A 1 26  ? 38.476  -33.780 -66.594  1.000 152.963 ? 25  SER HHH OG  1 
ATOM 191  N N   . GLY A 1 27  ? 40.926  -37.221 -68.231  1.000 161.677 ? 26  GLY HHH N   1 
ATOM 192  C CA  . GLY A 1 27  ? 42.087  -38.110 -68.170  1.000 167.333 ? 26  GLY HHH CA  1 
ATOM 193  C C   . GLY A 1 27  ? 42.385  -38.738 -69.504  1.000 169.561 ? 26  GLY HHH C   1 
ATOM 194  O O   . GLY A 1 27  ? 41.524  -38.751 -70.399  1.000 163.770 ? 26  GLY HHH O   1 
ATOM 195  N N   . TYR A 1 28  ? 43.608  -39.229 -69.619  1.000 170.810 ? 27  TYR HHH N   1 
ATOM 196  C CA  . TYR A 1 28  ? 44.056  -40.054 -70.754  1.000 164.445 ? 27  TYR HHH CA  1 
ATOM 197  C C   . TYR A 1 28  ? 43.348  -41.399 -70.607  1.000 166.499 ? 27  TYR HHH C   1 
ATOM 198  O O   . TYR A 1 28  ? 42.978  -41.800 -69.499  1.000 164.093 ? 27  TYR HHH O   1 
ATOM 199  C CB  . TYR A 1 28  ? 45.580  -40.154 -70.750  1.000 154.825 ? 27  TYR HHH CB  1 
ATOM 200  C CG  . TYR A 1 28  ? 46.283  -38.845 -70.992  1.000 143.480 ? 27  TYR HHH CG  1 
ATOM 201  C CD1 . TYR A 1 28  ? 46.490  -38.418 -72.278  1.000 144.165 ? 27  TYR HHH CD1 1 
ATOM 202  C CD2 . TYR A 1 28  ? 46.743  -38.042 -69.963  1.000 140.845 ? 27  TYR HHH CD2 1 
ATOM 203  C CE1 . TYR A 1 28  ? 47.168  -37.242 -72.552  1.000 149.411 ? 27  TYR HHH CE1 1 
ATOM 204  C CE2 . TYR A 1 28  ? 47.413  -36.859 -70.208  1.000 144.437 ? 27  TYR HHH CE2 1 
ATOM 205  C CZ  . TYR A 1 28  ? 47.643  -36.460 -71.521  1.000 151.048 ? 27  TYR HHH CZ  1 
ATOM 206  O OH  . TYR A 1 28  ? 48.275  -35.302 -71.916  1.000 150.120 ? 27  TYR HHH OH  1 
ATOM 207  N N   . GLY A 1 29  ? 43.137  -42.084 -71.719  1.000 172.526 ? 28  GLY HHH N   1 
ATOM 208  C CA  . GLY A 1 29  ? 42.612  -43.455 -71.690  1.000 162.792 ? 28  GLY HHH CA  1 
ATOM 209  C C   . GLY A 1 29  ? 41.100  -43.474 -71.673  1.000 155.201 ? 28  GLY HHH C   1 
ATOM 210  O O   . GLY A 1 29  ? 40.570  -44.575 -71.496  1.000 137.264 ? 28  GLY HHH O   1 
ATOM 211  N N   . PHE A 1 30  ? 40.439  -42.331 -71.927  1.000 156.298 ? 29  PHE HHH N   1 
ATOM 212  C CA  . PHE A 1 30  ? 38.957  -42.207 -71.876  1.000 154.585 ? 29  PHE HHH CA  1 
ATOM 213  C C   . PHE A 1 30  ? 38.325  -43.209 -72.854  1.000 149.158 ? 29  PHE HHH C   1 
ATOM 214  O O   . PHE A 1 30  ? 37.197  -43.658 -72.577  1.000 152.485 ? 29  PHE HHH O   1 
ATOM 215  C CB  . PHE A 1 30  ? 38.452  -40.773 -72.108  1.000 153.737 ? 29  PHE HHH CB  1 
ATOM 216  C CG  . PHE A 1 30  ? 36.956  -40.634 -71.905  1.000 163.719 ? 29  PHE HHH CG  1 
ATOM 217  C CD1 . PHE A 1 30  ? 36.398  -40.452 -70.645  1.000 178.649 ? 29  PHE HHH CD1 1 
ATOM 218  C CD2 . PHE A 1 30  ? 36.075  -40.760 -72.965  1.000 172.547 ? 29  PHE HHH CD2 1 
ATOM 219  C CE1 . PHE A 1 30  ? 35.017  -40.375 -70.465  1.000 182.004 ? 29  PHE HHH CE1 1 
ATOM 220  C CE2 . PHE A 1 30  ? 34.699  -40.674 -72.787  1.000 176.718 ? 29  PHE HHH CE2 1 
ATOM 221  C CZ  . PHE A 1 30  ? 34.165  -40.475 -71.540  1.000 173.697 ? 29  PHE HHH CZ  1 
ATOM 222  N N   . ILE A 1 31  ? 39.016  -43.574 -73.939  1.000 148.479 ? 30  ILE HHH N   1 
ATOM 223  C CA  . ILE A 1 31  ? 38.438  -44.440 -75.016  1.000 161.422 ? 30  ILE HHH CA  1 
ATOM 224  C C   . ILE A 1 31  ? 38.042  -45.807 -74.433  1.000 152.321 ? 30  ILE HHH C   1 
ATOM 225  O O   . ILE A 1 31  ? 37.185  -46.504 -75.027  1.000 151.383 ? 30  ILE HHH O   1 
ATOM 226  C CB  . ILE A 1 31  ? 39.396  -44.569 -76.226  1.000 173.182 ? 30  ILE HHH CB  1 
ATOM 227  C CG1 . ILE A 1 31  ? 38.804  -45.396 -77.375  1.000 178.416 ? 30  ILE HHH CG1 1 
ATOM 228  C CG2 . ILE A 1 31  ? 40.739  -45.131 -75.806  1.000 179.730 ? 30  ILE HHH CG2 1 
ATOM 229  C CD1 . ILE A 1 31  ? 37.421  -44.949 -77.827  1.000 185.852 ? 30  ILE HHH CD1 1 
ATOM 230  N N   . THR A 1 32  ? 38.633  -46.192 -73.310  1.000 142.231 ? 31  THR HHH N   1 
ATOM 231  C CA  . THR A 1 32  ? 38.422  -47.537 -72.738  1.000 140.774 ? 31  THR HHH CA  1 
ATOM 232  C C   . THR A 1 32  ? 37.110  -47.566 -71.966  1.000 136.875 ? 31  THR HHH C   1 
ATOM 233  O O   . THR A 1 32  ? 36.462  -48.642 -71.970  1.000 126.005 ? 31  THR HHH O   1 
ATOM 234  C CB  . THR A 1 32  ? 39.592  -47.915 -71.837  1.000 143.741 ? 31  THR HHH CB  1 
ATOM 235  O OG1 . THR A 1 32  ? 40.850  -47.624 -72.445  1.000 146.227 ? 31  THR HHH OG1 1 
ATOM 236  C CG2 . THR A 1 32  ? 39.569  -49.385 -71.542  1.000 151.758 ? 31  THR HHH CG2 1 
ATOM 237  N N   . TYR A 1 33  ? 36.792  -46.416 -71.343  1.000 145.504 ? 32  TYR HHH N   1 
ATOM 238  C CA  . TYR A 1 33  ? 35.737  -46.192 -70.311  1.000 149.980 ? 32  TYR HHH CA  1 
ATOM 239  C C   . TYR A 1 33  ? 34.357  -46.252 -70.953  1.000 138.826 ? 32  TYR HHH C   1 
ATOM 240  O O   . TYR A 1 33  ? 34.163  -45.756 -72.052  1.000 135.580 ? 32  TYR HHH O   1 
ATOM 241  C CB  . TYR A 1 33  ? 35.916  -44.879 -69.523  1.000 155.170 ? 32  TYR HHH CB  1 
ATOM 242  C CG  . TYR A 1 33  ? 36.892  -44.999 -68.378  1.000 157.628 ? 32  TYR HHH CG  1 
ATOM 243  C CD1 . TYR A 1 33  ? 38.223  -44.667 -68.563  1.000 154.538 ? 32  TYR HHH CD1 1 
ATOM 244  C CD2 . TYR A 1 33  ? 36.511  -45.526 -67.148  1.000 158.234 ? 32  TYR HHH CD2 1 
ATOM 245  C CE1 . TYR A 1 33  ? 39.160  -44.832 -67.560  1.000 158.221 ? 32  TYR HHH CE1 1 
ATOM 246  C CE2 . TYR A 1 33  ? 37.436  -45.693 -66.127  1.000 166.016 ? 32  TYR HHH CE2 1 
ATOM 247  C CZ  . TYR A 1 33  ? 38.766  -45.348 -66.337  1.000 172.543 ? 32  TYR HHH CZ  1 
ATOM 248  O OH  . TYR A 1 33  ? 39.701  -45.502 -65.350  1.000 186.279 ? 32  TYR HHH OH  1 
ATOM 249  N N   . TRP A 1 34  ? 33.445  -46.892 -70.235  1.000 140.814 ? 33  TRP HHH N   1 
ATOM 250  C CA  . TRP A 1 34  ? 31.977  -46.850 -70.436  1.000 145.269 ? 33  TRP HHH CA  1 
ATOM 251  C C   . TRP A 1 34  ? 31.383  -46.048 -69.268  1.000 141.329 ? 33  TRP HHH C   1 
ATOM 252  O O   . TRP A 1 34  ? 31.674  -46.389 -68.108  1.000 177.437 ? 33  TRP HHH O   1 
ATOM 253  C CB  . TRP A 1 34  ? 31.396  -48.274 -70.483  1.000 151.926 ? 33  TRP HHH CB  1 
ATOM 254  C CG  . TRP A 1 34  ? 31.887  -49.200 -71.561  1.000 157.307 ? 33  TRP HHH CG  1 
ATOM 255  C CD1 . TRP A 1 34  ? 33.177  -49.506 -71.920  1.000 155.523 ? 33  TRP HHH CD1 1 
ATOM 256  C CD2 . TRP A 1 34  ? 31.045  -50.039 -72.371  1.000 153.383 ? 33  TRP HHH CD2 1 
ATOM 257  N NE1 . TRP A 1 34  ? 33.190  -50.433 -72.934  1.000 153.024 ? 33  TRP HHH NE1 1 
ATOM 258  C CE2 . TRP A 1 34  ? 31.893  -50.774 -73.228  1.000 151.418 ? 33  TRP HHH CE2 1 
ATOM 259  C CE3 . TRP A 1 34  ? 29.661  -50.203 -72.474  1.000 155.924 ? 33  TRP HHH CE3 1 
ATOM 260  C CZ2 . TRP A 1 34  ? 31.386  -51.660 -74.171  1.000 150.744 ? 33  TRP HHH CZ2 1 
ATOM 261  C CZ3 . TRP A 1 34  ? 29.162  -51.080 -73.410  1.000 151.631 ? 33  TRP HHH CZ3 1 
ATOM 262  C CH2 . TRP A 1 34  ? 30.018  -51.798 -74.237  1.000 150.034 ? 33  TRP HHH CH2 1 
ATOM 263  N N   . ILE A 1 35  ? 30.626  -44.994 -69.544  1.000 140.149 ? 34  ILE HHH N   1 
ATOM 264  C CA  . ILE A 1 35  ? 29.957  -44.148 -68.515  1.000 136.710 ? 34  ILE HHH CA  1 
ATOM 265  C C   . ILE A 1 35  ? 28.563  -44.720 -68.224  1.000 141.108 ? 34  ILE HHH C   1 
ATOM 266  O O   . ILE A 1 35  ? 27.787  -44.966 -69.172  1.000 145.784 ? 34  ILE HHH O   1 
ATOM 267  C CB  . ILE A 1 35  ? 29.868  -42.677 -68.958  1.000 135.484 ? 34  ILE HHH CB  1 
ATOM 268  C CG1 . ILE A 1 35  ? 31.167  -41.890 -68.753  1.000 131.888 ? 34  ILE HHH CG1 1 
ATOM 269  C CG2 . ILE A 1 35  ? 28.727  -42.028 -68.196  1.000 140.033 ? 34  ILE HHH CG2 1 
ATOM 270  C CD1 . ILE A 1 35  ? 32.434  -42.615 -69.119  1.000 131.784 ? 34  ILE HHH CD1 1 
ATOM 271  N N   . GLY A 1 36  ? 28.260  -44.904 -66.938  1.000 147.494 ? 35  GLY HHH N   1 
ATOM 272  C CA  . GLY A 1 36  ? 26.968  -45.402 -66.436  1.000 151.947 ? 35  GLY HHH CA  1 
ATOM 273  C C   . GLY A 1 36  ? 26.303  -44.311 -65.622  1.000 155.151 ? 35  GLY HHH C   1 
ATOM 274  O O   . GLY A 1 36  ? 27.027  -43.484 -65.026  1.000 147.830 ? 35  GLY HHH O   1 
ATOM 275  N N   . TRP A 1 37  ? 24.978  -44.276 -65.644  1.000 156.389 ? 36  TRP HHH N   1 
ATOM 276  C CA  . TRP A 1 37  ? 24.172  -43.359 -64.814  1.000 159.116 ? 36  TRP HHH CA  1 
ATOM 277  C C   . TRP A 1 37  ? 23.472  -44.170 -63.714  1.000 169.143 ? 36  TRP HHH C   1 
ATOM 278  O O   . TRP A 1 37  ? 22.908  -45.260 -63.986  1.000 171.142 ? 36  TRP HHH O   1 
ATOM 279  C CB  . TRP A 1 37  ? 23.209  -42.578 -65.699  1.000 162.560 ? 36  TRP HHH CB  1 
ATOM 280  C CG  . TRP A 1 37  ? 23.909  -41.568 -66.549  1.000 173.471 ? 36  TRP HHH CG  1 
ATOM 281  C CD1 . TRP A 1 37  ? 24.348  -41.724 -67.835  1.000 184.829 ? 36  TRP HHH CD1 1 
ATOM 282  C CD2 . TRP A 1 37  ? 24.257  -40.229 -66.171  1.000 175.767 ? 36  TRP HHH CD2 1 
ATOM 283  N NE1 . TRP A 1 37  ? 24.935  -40.569 -68.284  1.000 180.219 ? 36  TRP HHH NE1 1 
ATOM 284  C CE2 . TRP A 1 37  ? 24.900  -39.640 -67.281  1.000 180.999 ? 36  TRP HHH CE2 1 
ATOM 285  C CE3 . TRP A 1 37  ? 24.071  -39.468 -65.015  1.000 174.163 ? 36  TRP HHH CE3 1 
ATOM 286  C CZ2 . TRP A 1 37  ? 25.363  -38.326 -67.255  1.000 186.582 ? 36  TRP HHH CZ2 1 
ATOM 287  C CZ3 . TRP A 1 37  ? 24.533  -38.169 -64.985  1.000 175.711 ? 36  TRP HHH CZ3 1 
ATOM 288  C CH2 . TRP A 1 37  ? 25.172  -37.611 -66.089  1.000 181.996 ? 36  TRP HHH CH2 1 
ATOM 289  N N   . VAL A 1 38  ? 23.538  -43.658 -62.491  1.000 166.138 ? 37  VAL HHH N   1 
ATOM 290  C CA  . VAL A 1 38  ? 22.865  -44.254 -61.315  1.000 158.888 ? 37  VAL HHH CA  1 
ATOM 291  C C   . VAL A 1 38  ? 21.964  -43.182 -60.724  1.000 149.185 ? 37  VAL HHH C   1 
ATOM 292  O O   . VAL A 1 38  ? 22.449  -42.052 -60.563  1.000 137.694 ? 37  VAL HHH O   1 
ATOM 293  C CB  . VAL A 1 38  ? 23.898  -44.738 -60.290  1.000 179.868 ? 37  VAL HHH CB  1 
ATOM 294  C CG1 . VAL A 1 38  ? 23.210  -45.193 -59.009  1.000 193.654 ? 37  VAL HHH CG1 1 
ATOM 295  C CG2 . VAL A 1 38  ? 24.795  -45.830 -60.861  1.000 183.190 ? 37  VAL HHH CG2 1 
ATOM 296  N N   . ARG A 1 39  ? 20.718  -43.547 -60.423  1.000 155.442 ? 38  ARG HHH N   1 
ATOM 297  C CA  . ARG A 1 39  ? 19.713  -42.673 -59.764  1.000 162.302 ? 38  ARG HHH CA  1 
ATOM 298  C C   . ARG A 1 39  ? 19.556  -43.114 -58.308  1.000 163.659 ? 38  ARG HHH C   1 
ATOM 299  O O   . ARG A 1 39  ? 19.410  -44.306 -58.076  1.000 160.014 ? 38  ARG HHH O   1 
ATOM 300  C CB  . ARG A 1 39  ? 18.394  -42.755 -60.533  1.000 169.162 ? 38  ARG HHH CB  1 
ATOM 301  C CG  . ARG A 1 39  ? 17.338  -41.770 -60.060  1.000 176.473 ? 38  ARG HHH CG  1 
ATOM 302  C CD  . ARG A 1 39  ? 16.252  -42.457 -59.271  1.000 188.949 ? 38  ARG HHH CD  1 
ATOM 303  N NE  . ARG A 1 39  ? 15.305  -43.167 -60.123  1.000 194.339 ? 38  ARG HHH NE  1 
ATOM 304  C CZ  . ARG A 1 39  ? 14.050  -42.795 -60.354  1.000 190.976 ? 38  ARG HHH CZ  1 
ATOM 305  N NH1 . ARG A 1 39  ? 13.575  -41.681 -59.816  1.000 187.673 ? 38  ARG HHH NH1 1 
ATOM 306  N NH2 . ARG A 1 39  ? 13.278  -43.534 -61.136  1.000 194.148 ? 38  ARG HHH NH2 1 
ATOM 307  N N   . GLN A 1 40  ? 19.593  -42.187 -57.355  1.000 164.502 ? 39  GLN HHH N   1 
ATOM 308  C CA  . GLN A 1 40  ? 19.386  -42.491 -55.914  1.000 161.116 ? 39  GLN HHH CA  1 
ATOM 309  C C   . GLN A 1 40  ? 18.453  -41.458 -55.294  1.000 163.872 ? 39  GLN HHH C   1 
ATOM 310  O O   . GLN A 1 40  ? 18.918  -40.313 -55.113  1.000 168.082 ? 39  GLN HHH O   1 
ATOM 311  C CB  . GLN A 1 40  ? 20.712  -42.410 -55.175  1.000 160.077 ? 39  GLN HHH CB  1 
ATOM 312  C CG  . GLN A 1 40  ? 20.554  -42.526 -53.673  1.000 155.120 ? 39  GLN HHH CG  1 
ATOM 313  C CD  . GLN A 1 40  ? 21.876  -42.801 -53.017  1.000 154.910 ? 39  GLN HHH CD  1 
ATOM 314  O OE1 . GLN A 1 40  ? 22.131  -43.928 -52.586  1.000 148.726 ? 39  GLN HHH OE1 1 
ATOM 315  N NE2 . GLN A 1 40  ? 22.724  -41.777 -52.996  1.000 154.328 ? 39  GLN HHH NE2 1 
ATOM 316  N N   . MET A 1 41  ? 17.210  -41.822 -54.975  1.000 164.404 ? 40  MET HHH N   1 
ATOM 317  C CA  . MET A 1 41  ? 16.213  -40.807 -54.536  1.000 183.616 ? 40  MET HHH CA  1 
ATOM 318  C C   . MET A 1 41  ? 16.371  -40.583 -53.037  1.000 189.428 ? 40  MET HHH C   1 
ATOM 319  O O   . MET A 1 41  ? 16.831  -41.490 -52.355  1.000 213.449 ? 40  MET HHH O   1 
ATOM 320  C CB  . MET A 1 41  ? 14.797  -41.253 -54.889  1.000 188.226 ? 40  MET HHH CB  1 
ATOM 321  C CG  . MET A 1 41  ? 14.676  -41.584 -56.354  1.000 191.625 ? 40  MET HHH CG  1 
ATOM 322  S SD  . MET A 1 41  ? 13.063  -42.199 -56.829  1.000 208.144 ? 40  MET HHH SD  1 
ATOM 323  C CE  . MET A 1 41  ? 12.035  -40.757 -56.541  1.000 213.245 ? 40  MET HHH CE  1 
ATOM 324  N N   . PRO A 1 42  ? 16.017  -39.406 -52.464  1.000 191.740 ? 41  PRO HHH N   1 
ATOM 325  C CA  . PRO A 1 42  ? 16.323  -39.123 -51.055  1.000 192.896 ? 41  PRO HHH CA  1 
ATOM 326  C C   . PRO A 1 42  ? 15.882  -40.240 -50.082  1.000 194.109 ? 41  PRO HHH C   1 
ATOM 327  O O   . PRO A 1 42  ? 14.695  -40.537 -50.004  1.000 190.362 ? 41  PRO HHH O   1 
ATOM 328  C CB  . PRO A 1 42  ? 15.590  -37.801 -50.781  1.000 191.789 ? 41  PRO HHH CB  1 
ATOM 329  C CG  . PRO A 1 42  ? 15.474  -37.155 -52.141  1.000 195.245 ? 41  PRO HHH CG  1 
ATOM 330  C CD  . PRO A 1 42  ? 15.304  -38.300 -53.121  1.000 196.165 ? 41  PRO HHH CD  1 
ATOM 331  N N   . GLY A 1 43  ? 16.857  -40.865 -49.402  1.000 190.277 ? 42  GLY HHH N   1 
ATOM 332  C CA  . GLY A 1 43  ? 16.658  -41.944 -48.412  1.000 191.484 ? 42  GLY HHH CA  1 
ATOM 333  C C   . GLY A 1 43  ? 16.641  -43.348 -49.013  1.000 188.131 ? 42  GLY HHH C   1 
ATOM 334  O O   . GLY A 1 43  ? 16.645  -44.321 -48.229  1.000 201.470 ? 42  GLY HHH O   1 
ATOM 335  N N   . LYS A 1 44  ? 16.638  -43.483 -50.341  1.000 182.905 ? 43  LYS HHH N   1 
ATOM 336  C CA  . LYS A 1 44  ? 16.362  -44.772 -51.037  1.000 180.003 ? 43  LYS HHH CA  1 
ATOM 337  C C   . LYS A 1 44  ? 17.670  -45.294 -51.635  1.000 164.344 ? 43  LYS HHH C   1 
ATOM 338  O O   . LYS A 1 44  ? 18.706  -44.601 -51.484  1.000 159.292 ? 43  LYS HHH O   1 
ATOM 339  C CB  . LYS A 1 44  ? 15.311  -44.570 -52.135  1.000 191.724 ? 43  LYS HHH CB  1 
ATOM 340  C CG  . LYS A 1 44  ? 14.128  -43.672 -51.773  1.000 199.417 ? 43  LYS HHH CG  1 
ATOM 341  C CD  . LYS A 1 44  ? 13.382  -44.058 -50.529  1.000 210.728 ? 43  LYS HHH CD  1 
ATOM 342  C CE  . LYS A 1 44  ? 12.440  -45.215 -50.771  1.000 219.478 ? 43  LYS HHH CE  1 
ATOM 343  N NZ  . LYS A 1 44  ? 11.725  -45.604 -49.530  1.000 225.954 ? 43  LYS HHH NZ  1 
ATOM 344  N N   . GLY A 1 45  ? 17.611  -46.427 -52.337  1.000 152.566 ? 44  GLY HHH N   1 
ATOM 345  C CA  . GLY A 1 45  ? 18.808  -47.161 -52.794  1.000 158.935 ? 44  GLY HHH CA  1 
ATOM 346  C C   . GLY A 1 45  ? 19.506  -46.532 -53.989  1.000 159.498 ? 44  GLY HHH C   1 
ATOM 347  O O   . GLY A 1 45  ? 19.137  -45.450 -54.395  1.000 174.657 ? 44  GLY HHH O   1 
ATOM 348  N N   . LEU A 1 46  ? 20.487  -47.223 -54.551  1.000 154.629 ? 45  LEU HHH N   1 
ATOM 349  C CA  . LEU A 1 46  ? 21.033  -46.940 -55.897  1.000 152.647 ? 45  LEU HHH CA  1 
ATOM 350  C C   . LEU A 1 46  ? 20.140  -47.666 -56.922  1.000 157.925 ? 45  LEU HHH C   1 
ATOM 351  O O   . LEU A 1 46  ? 19.779  -48.837 -56.678  1.000 154.814 ? 45  LEU HHH O   1 
ATOM 352  C CB  . LEU A 1 46  ? 22.490  -47.432 -55.942  1.000 158.836 ? 45  LEU HHH CB  1 
ATOM 353  C CG  . LEU A 1 46  ? 23.494  -46.781 -54.968  1.000 158.939 ? 45  LEU HHH CG  1 
ATOM 354  C CD1 . LEU A 1 46  ? 24.859  -47.458 -55.039  1.000 144.553 ? 45  LEU HHH CD1 1 
ATOM 355  C CD2 . LEU A 1 46  ? 23.668  -45.284 -55.219  1.000 164.742 ? 45  LEU HHH CD2 1 
ATOM 356  N N   . GLU A 1 47  ? 19.755  -46.974 -58.002  1.000 171.536 ? 46  GLU HHH N   1 
ATOM 357  C CA  . GLU A 1 47  ? 19.063  -47.533 -59.206  1.000 175.680 ? 46  GLU HHH CA  1 
ATOM 358  C C   . GLU A 1 47  ? 19.944  -47.304 -60.440  1.000 173.819 ? 46  GLU HHH C   1 
ATOM 359  O O   . GLU A 1 47  ? 20.192  -46.126 -60.796  1.000 162.900 ? 46  GLU HHH O   1 
ATOM 360  C CB  . GLU A 1 47  ? 17.713  -46.858 -59.465  1.000 181.578 ? 46  GLU HHH CB  1 
ATOM 361  C CG  . GLU A 1 47  ? 16.630  -47.199 -58.457  1.000 187.610 ? 46  GLU HHH CG  1 
ATOM 362  C CD  . GLU A 1 47  ? 15.322  -46.444 -58.652  1.000 190.690 ? 46  GLU HHH CD  1 
ATOM 363  O OE1 . GLU A 1 47  ? 15.201  -45.318 -58.105  1.000 192.350 ? 46  GLU HHH OE1 1 
ATOM 364  O OE2 . GLU A 1 47  ? 14.431  -46.971 -59.369  1.000 189.484 ? 46  GLU HHH OE2 1 
ATOM 365  N N   . TRP A 1 48  ? 20.397  -48.385 -61.074  1.000 176.837 ? 47  TRP HHH N   1 
ATOM 366  C CA  . TRP A 1 48  ? 21.184  -48.335 -62.332  1.000 177.782 ? 47  TRP HHH CA  1 
ATOM 367  C C   . TRP A 1 48  ? 20.234  -47.979 -63.484  1.000 179.424 ? 47  TRP HHH C   1 
ATOM 368  O O   . TRP A 1 48  ? 19.214  -48.681 -63.677  1.000 186.154 ? 47  TRP HHH O   1 
ATOM 369  C CB  . TRP A 1 48  ? 21.913  -49.664 -62.562  1.000 180.219 ? 47  TRP HHH CB  1 
ATOM 370  C CG  . TRP A 1 48  ? 22.871  -49.636 -63.711  1.000 187.639 ? 47  TRP HHH CG  1 
ATOM 371  C CD1 . TRP A 1 48  ? 24.179  -49.237 -63.694  1.000 195.908 ? 47  TRP HHH CD1 1 
ATOM 372  C CD2 . TRP A 1 48  ? 22.592  -50.026 -65.065  1.000 192.633 ? 47  TRP HHH CD2 1 
ATOM 373  N NE1 . TRP A 1 48  ? 24.734  -49.349 -64.942  1.000 196.300 ? 47  TRP HHH NE1 1 
ATOM 374  C CE2 . TRP A 1 48  ? 23.780  -49.828 -65.804  1.000 197.455 ? 47  TRP HHH CE2 1 
ATOM 375  C CE3 . TRP A 1 48  ? 21.460  -50.516 -65.724  1.000 194.128 ? 47  TRP HHH CE3 1 
ATOM 376  C CZ2 . TRP A 1 48  ? 23.860  -50.119 -67.166  1.000 195.498 ? 47  TRP HHH CZ2 1 
ATOM 377  C CZ3 . TRP A 1 48  ? 21.542  -50.798 -67.070  1.000 195.803 ? 47  TRP HHH CZ3 1 
ATOM 378  C CH2 . TRP A 1 48  ? 22.729  -50.605 -67.779  1.000 195.025 ? 47  TRP HHH CH2 1 
ATOM 379  N N   . MET A 1 49  ? 20.524  -46.894 -64.197  1.000 169.013 ? 48  MET HHH N   1 
ATOM 380  C CA  . MET A 1 49  ? 19.635  -46.361 -65.265  1.000 163.979 ? 48  MET HHH CA  1 
ATOM 381  C C   . MET A 1 49  ? 20.031  -46.984 -66.607  1.000 169.244 ? 48  MET HHH C   1 
ATOM 382  O O   . MET A 1 49  ? 19.201  -47.704 -67.204  1.000 178.977 ? 48  MET HHH O   1 
ATOM 383  C CB  . MET A 1 49  ? 19.748  -44.837 -65.337  1.000 158.809 ? 48  MET HHH CB  1 
ATOM 384  C CG  . MET A 1 49  ? 19.144  -44.150 -64.130  1.000 162.268 ? 48  MET HHH CG  1 
ATOM 385  S SD  . MET A 1 49  ? 19.235  -42.342 -64.205  1.000 156.440 ? 48  MET HHH SD  1 
ATOM 386  C CE  . MET A 1 49  ? 17.905  -41.990 -65.348  1.000 169.713 ? 48  MET HHH CE  1 
ATOM 387  N N   . GLY A 1 50  ? 21.268  -46.720 -67.039  1.000 172.316 ? 49  GLY HHH N   1 
ATOM 388  C CA  . GLY A 1 50  ? 21.858  -47.194 -68.305  1.000 169.106 ? 49  GLY HHH CA  1 
ATOM 389  C C   . GLY A 1 50  ? 23.374  -47.013 -68.350  1.000 168.331 ? 49  GLY HHH C   1 
ATOM 390  O O   . GLY A 1 50  ? 23.981  -46.483 -67.395  1.000 179.179 ? 49  GLY HHH O   1 
ATOM 391  N N   . ILE A 1 51  ? 23.989  -47.442 -69.441  1.000 168.540 ? 50  ILE HHH N   1 
ATOM 392  C CA  . ILE A 1 51  ? 25.451  -47.305 -69.665  1.000 174.154 ? 50  ILE HHH CA  1 
ATOM 393  C C   . ILE A 1 51  ? 25.660  -47.020 -71.140  1.000 181.258 ? 50  ILE HHH C   1 
ATOM 394  O O   . ILE A 1 51  ? 24.873  -47.548 -71.934  1.000 188.856 ? 50  ILE HHH O   1 
ATOM 395  C CB  . ILE A 1 51  ? 26.190  -48.590 -69.274  1.000 180.179 ? 50  ILE HHH CB  1 
ATOM 396  C CG1 . ILE A 1 51  ? 27.705  -48.386 -69.242  1.000 181.991 ? 50  ILE HHH CG1 1 
ATOM 397  C CG2 . ILE A 1 51  ? 25.790  -49.733 -70.198  1.000 179.393 ? 50  ILE HHH CG2 1 
ATOM 398  C CD1 . ILE A 1 51  ? 28.442  -49.498 -68.538  1.000 187.716 ? 50  ILE HHH CD1 1 
ATOM 399  N N   . ILE A 1 52  ? 26.712  -46.281 -71.469  1.000 185.197 ? 51  ILE HHH N   1 
ATOM 400  C CA  . ILE A 1 52  ? 27.034  -45.869 -72.862  1.000 181.724 ? 51  ILE HHH CA  1 
ATOM 401  C C   . ILE A 1 52  ? 28.539  -45.928 -73.058  1.000 175.191 ? 51  ILE HHH C   1 
ATOM 402  O O   . ILE A 1 52  ? 29.261  -45.465 -72.190  1.000 186.460 ? 51  ILE HHH O   1 
ATOM 403  C CB  . ILE A 1 52  ? 26.508  -44.461 -73.169  1.000 187.944 ? 51  ILE HHH CB  1 
ATOM 404  C CG1 . ILE A 1 52  ? 26.789  -44.074 -74.619  1.000 193.105 ? 51  ILE HHH CG1 1 
ATOM 405  C CG2 . ILE A 1 52  ? 27.082  -43.440 -72.201  1.000 186.418 ? 51  ILE HHH CG2 1 
ATOM 406  C CD1 . ILE A 1 52  ? 25.988  -42.874 -75.069  1.000 202.456 ? 51  ILE HHH CD1 1 
ATOM 407  N N   . TYR A 1 53  ? 28.961  -46.475 -74.185  1.000 170.597 ? 52  TYR HHH N   1 
ATOM 408  C CA  . TYR A 1 53  ? 30.363  -46.508 -74.646  1.000 159.622 ? 52  TYR HHH CA  1 
ATOM 409  C C   . TYR A 1 53  ? 30.524  -45.380 -75.641  1.000 149.242 ? 52  TYR HHH C   1 
ATOM 410  O O   . TYR A 1 53  ? 30.102  -45.523 -76.776  1.000 153.854 ? 52  TYR HHH O   1 
ATOM 411  C CB  . TYR A 1 53  ? 30.664  -47.830 -75.339  1.000 155.381 ? 52  TYR HHH CB  1 
ATOM 412  C CG  . TYR A 1 53  ? 32.071  -47.907 -75.842  1.000 150.894 ? 52  TYR HHH CG  1 
ATOM 413  C CD1 . TYR A 1 53  ? 33.137  -47.764 -74.977  1.000 159.812 ? 52  TYR HHH CD1 1 
ATOM 414  C CD2 . TYR A 1 53  ? 32.342  -48.084 -77.170  1.000 146.857 ? 52  TYR HHH CD2 1 
ATOM 415  C CE1 . TYR A 1 53  ? 34.446  -47.821 -75.414  1.000 160.107 ? 52  TYR HHH CE1 1 
ATOM 416  C CE2 . TYR A 1 53  ? 33.648  -48.166 -77.620  1.000 153.909 ? 52  TYR HHH CE2 1 
ATOM 417  C CZ  . TYR A 1 53  ? 34.710  -48.028 -76.749  1.000 153.296 ? 52  TYR HHH CZ  1 
ATOM 418  O OH  . TYR A 1 53  ? 36.000  -48.084 -77.196  1.000 148.211 ? 52  TYR HHH OH  1 
ATOM 419  N N   . PRO A 1 54  ? 31.103  -44.235 -75.248  1.000 150.380 ? 53  PRO HHH N   1 
ATOM 420  C CA  . PRO A 1 54  ? 31.151  -43.072 -76.133  1.000 164.040 ? 53  PRO HHH CA  1 
ATOM 421  C C   . PRO A 1 54  ? 31.896  -43.325 -77.466  1.000 166.805 ? 53  PRO HHH C   1 
ATOM 422  O O   . PRO A 1 54  ? 31.714  -42.521 -78.439  1.000 137.032 ? 53  PRO HHH O   1 
ATOM 423  C CB  . PRO A 1 54  ? 31.830  -42.000 -75.262  1.000 169.223 ? 53  PRO HHH CB  1 
ATOM 424  C CG  . PRO A 1 54  ? 31.638  -42.491 -73.834  1.000 165.702 ? 53  PRO HHH CG  1 
ATOM 425  C CD  . PRO A 1 54  ? 31.726  -43.994 -73.943  1.000 154.933 ? 53  PRO HHH CD  1 
ATOM 426  N N   . GLY A 1 55  ? 32.688  -44.415 -77.531  1.000 164.990 ? 54  GLY HHH N   1 
ATOM 427  C CA  . GLY A 1 55  ? 33.390  -44.814 -78.771  1.000 169.679 ? 54  GLY HHH CA  1 
ATOM 428  C C   . GLY A 1 55  ? 32.493  -44.751 -80.015  1.000 159.271 ? 54  GLY HHH C   1 
ATOM 429  O O   . GLY A 1 55  ? 32.976  -44.298 -81.078  1.000 146.063 ? 54  GLY HHH O   1 
ATOM 430  N N   . ASP A 1 56  ? 31.268  -45.266 -79.885  1.000 157.003 ? 55  ASP HHH N   1 
ATOM 431  C CA  . ASP A 1 56  ? 30.252  -45.416 -80.957  1.000 163.670 ? 55  ASP HHH CA  1 
ATOM 432  C C   . ASP A 1 56  ? 28.857  -45.238 -80.355  1.000 160.922 ? 55  ASP HHH C   1 
ATOM 433  O O   . ASP A 1 56  ? 27.864  -45.660 -80.965  1.000 155.577 ? 55  ASP HHH O   1 
ATOM 434  C CB  . ASP A 1 56  ? 30.384  -46.780 -81.640  1.000 171.410 ? 55  ASP HHH CB  1 
ATOM 435  C CG  . ASP A 1 56  ? 30.324  -47.983 -80.711  1.000 174.915 ? 55  ASP HHH CG  1 
ATOM 436  O OD1 . ASP A 1 56  ? 29.745  -47.872 -79.612  1.000 183.775 ? 55  ASP HHH OD1 1 
ATOM 437  O OD2 . ASP A 1 56  ? 30.869  -49.030 -81.095  1.000 183.326 ? 55  ASP HHH OD2 1 
ATOM 438  N N   . SER A 1 57  ? 28.806  -44.670 -79.160  1.000 170.694 ? 56  SER HHH N   1 
ATOM 439  C CA  . SER A 1 57  ? 27.564  -44.328 -78.429  1.000 177.018 ? 56  SER HHH CA  1 
ATOM 440  C C   . SER A 1 57  ? 26.650  -45.555 -78.294  1.000 182.362 ? 56  SER HHH C   1 
ATOM 441  O O   . SER A 1 57  ? 25.424  -45.361 -78.352  1.000 203.218 ? 56  SER HHH O   1 
ATOM 442  C CB  . SER A 1 57  ? 26.897  -43.163 -79.123  1.000 165.003 ? 56  SER HHH CB  1 
ATOM 443  O OG  . SER A 1 57  ? 27.852  -42.137 -79.347  1.000 148.180 ? 56  SER HHH OG  1 
ATOM 444  N N   . GLU A 1 58  ? 27.214  -46.760 -78.138  1.000 172.057 ? 57  GLU HHH N   1 
ATOM 445  C CA  . GLU A 1 58  ? 26.426  -47.974 -77.812  1.000 174.591 ? 57  GLU HHH CA  1 
ATOM 446  C C   . GLU A 1 58  ? 25.874  -47.773 -76.407  1.000 175.853 ? 57  GLU HHH C   1 
ATOM 447  O O   . GLU A 1 58  ? 26.682  -47.742 -75.485  1.000 185.145 ? 57  GLU HHH O   1 
ATOM 448  C CB  . GLU A 1 58  ? 27.270  -49.249 -77.865  1.000 171.677 ? 57  GLU HHH CB  1 
ATOM 449  C CG  . GLU A 1 58  ? 26.565  -50.458 -77.258  1.000 172.305 ? 57  GLU HHH CG  1 
ATOM 450  C CD  . GLU A 1 58  ? 27.375  -51.748 -77.258  1.000 174.323 ? 57  GLU HHH CD  1 
ATOM 451  O OE1 . GLU A 1 58  ? 27.007  -52.690 -76.524  1.000 178.856 ? 57  GLU HHH OE1 1 
ATOM 452  O OE2 . GLU A 1 58  ? 28.384  -51.815 -77.982  1.000 178.584 ? 57  GLU HHH OE2 1 
ATOM 453  N N   . THR A 1 59  ? 24.561  -47.657 -76.244  1.000 182.051 ? 58  THR HHH N   1 
ATOM 454  C CA  . THR A 1 59  ? 23.956  -47.439 -74.909  1.000 190.977 ? 58  THR HHH CA  1 
ATOM 455  C C   . THR A 1 59  ? 23.018  -48.608 -74.597  1.000 188.596 ? 58  THR HHH C   1 
ATOM 456  O O   . THR A 1 59  ? 22.451  -49.177 -75.547  1.000 187.310 ? 58  THR HHH O   1 
ATOM 457  C CB  . THR A 1 59  ? 23.302  -46.057 -74.815  1.000 196.718 ? 58  THR HHH CB  1 
ATOM 458  O OG1 . THR A 1 59  ? 21.901  -46.278 -74.687  1.000 208.836 ? 58  THR HHH OG1 1 
ATOM 459  C CG2 . THR A 1 59  ? 23.670  -45.160 -75.981  1.000 191.056 ? 58  THR HHH CG2 1 
ATOM 460  N N   . ARG A 1 60  ? 22.927  -48.974 -73.318  1.000 181.904 ? 59  ARG HHH N   1 
ATOM 461  C CA  . ARG A 1 60  ? 21.961  -49.971 -72.799  1.000 187.205 ? 59  ARG HHH CA  1 
ATOM 462  C C   . ARG A 1 60  ? 21.160  -49.310 -71.688  1.000 190.917 ? 59  ARG HHH C   1 
ATOM 463  O O   . ARG A 1 60  ? 21.776  -48.667 -70.819  1.000 205.609 ? 59  ARG HHH O   1 
ATOM 464  C CB  . ARG A 1 60  ? 22.672  -51.217 -72.273  1.000 178.427 ? 59  ARG HHH CB  1 
ATOM 465  C CG  . ARG A 1 60  ? 23.839  -51.642 -73.144  1.000 171.742 ? 59  ARG HHH CG  1 
ATOM 466  C CD  . ARG A 1 60  ? 23.900  -53.138 -73.334  1.000 169.006 ? 59  ARG HHH CD  1 
ATOM 467  N NE  . ARG A 1 60  ? 25.194  -53.454 -73.925  1.000 170.627 ? 59  ARG HHH NE  1 
ATOM 468  C CZ  . ARG A 1 60  ? 25.944  -54.510 -73.636  1.000 169.962 ? 59  ARG HHH CZ  1 
ATOM 469  N NH1 . ARG A 1 60  ? 27.099  -54.661 -74.253  1.000 166.356 ? 59  ARG HHH NH1 1 
ATOM 470  N NH2 . ARG A 1 60  ? 25.565  -55.399 -72.733  1.000 180.258 ? 59  ARG HHH NH2 1 
ATOM 471  N N   . TYR A 1 61  ? 19.842  -49.451 -71.747  1.000 187.696 ? 60  TYR HHH N   1 
ATOM 472  C CA  . TYR A 1 61  ? 18.922  -48.975 -70.694  1.000 191.080 ? 60  TYR HHH CA  1 
ATOM 473  C C   . TYR A 1 61  ? 18.495  -50.168 -69.839  1.000 181.029 ? 60  TYR HHH C   1 
ATOM 474  O O   . TYR A 1 61  ? 18.385  -51.308 -70.338  1.000 171.041 ? 60  TYR HHH O   1 
ATOM 475  C CB  . TYR A 1 61  ? 17.745  -48.248 -71.339  1.000 202.203 ? 60  TYR HHH CB  1 
ATOM 476  C CG  . TYR A 1 61  ? 18.132  -47.013 -72.112  1.000 208.987 ? 60  TYR HHH CG  1 
ATOM 477  C CD1 . TYR A 1 61  ? 18.276  -45.780 -71.487  1.000 210.671 ? 60  TYR HHH CD1 1 
ATOM 478  C CD2 . TYR A 1 61  ? 18.342  -47.076 -73.478  1.000 207.803 ? 60  TYR HHH CD2 1 
ATOM 479  C CE1 . TYR A 1 61  ? 18.617  -44.639 -72.200  1.000 207.302 ? 60  TYR HHH CE1 1 
ATOM 480  C CE2 . TYR A 1 61  ? 18.697  -45.951 -74.202  1.000 208.890 ? 60  TYR HHH CE2 1 
ATOM 481  C CZ  . TYR A 1 61  ? 18.827  -44.731 -73.564  1.000 208.443 ? 60  TYR HHH CZ  1 
ATOM 482  O OH  . TYR A 1 61  ? 19.166  -43.638 -74.302  1.000 209.200 ? 60  TYR HHH OH  1 
ATOM 483  N N   . SER A 1 62  ? 18.286  -49.905 -68.558  1.000 173.393 ? 61  SER HHH N   1 
ATOM 484  C CA  . SER A 1 62  ? 17.535  -50.816 -67.677  1.000 177.733 ? 61  SER HHH CA  1 
ATOM 485  C C   . SER A 1 62  ? 16.067  -50.686 -68.040  1.000 180.879 ? 61  SER HHH C   1 
ATOM 486  O O   . SER A 1 62  ? 15.576  -49.575 -68.225  1.000 174.856 ? 61  SER HHH O   1 
ATOM 487  C CB  . SER A 1 62  ? 17.757  -50.512 -66.226  1.000 184.021 ? 61  SER HHH CB  1 
ATOM 488  O OG  . SER A 1 62  ? 16.895  -51.300 -65.409  1.000 195.039 ? 61  SER HHH OG  1 
ATOM 489  N N   . PRO A 1 63  ? 15.338  -51.820 -68.137  1.000 189.998 ? 62  PRO HHH N   1 
ATOM 490  C CA  . PRO A 1 63  ? 13.879  -51.815 -68.282  1.000 194.892 ? 62  PRO HHH CA  1 
ATOM 491  C C   . PRO A 1 63  ? 13.109  -50.763 -67.465  1.000 187.075 ? 62  PRO HHH C   1 
ATOM 492  O O   . PRO A 1 63  ? 12.070  -50.348 -67.936  1.000 187.511 ? 62  PRO HHH O   1 
ATOM 493  C CB  . PRO A 1 63  ? 13.500  -53.230 -67.819  1.000 193.439 ? 62  PRO HHH CB  1 
ATOM 494  C CG  . PRO A 1 63  ? 14.681  -54.080 -68.271  1.000 191.152 ? 62  PRO HHH CG  1 
ATOM 495  C CD  . PRO A 1 63  ? 15.892  -53.184 -68.117  1.000 187.423 ? 62  PRO HHH CD  1 
ATOM 496  N N   . SER A 1 64  ? 13.631  -50.337 -66.310  1.000 183.114 ? 63  SER HHH N   1 
ATOM 497  C CA  . SER A 1 64  ? 13.007  -49.308 -65.430  1.000 195.591 ? 63  SER HHH CA  1 
ATOM 498  C C   . SER A 1 64  ? 13.108  -47.905 -66.045  1.000 192.426 ? 63  SER HHH C   1 
ATOM 499  O O   . SER A 1 64  ? 12.362  -47.018 -65.571  1.000 184.853 ? 63  SER HHH O   1 
ATOM 500  C CB  . SER A 1 64  ? 13.593  -49.324 -64.036  1.000 204.075 ? 63  SER HHH CB  1 
ATOM 501  O OG  . SER A 1 64  ? 13.335  -50.570 -63.393  1.000 210.824 ? 63  SER HHH OG  1 
ATOM 502  N N   . PHE A 1 65  ? 13.988  -47.696 -67.031  1.000 191.655 ? 64  PHE HHH N   1 
ATOM 503  C CA  . PHE A 1 65  ? 14.230  -46.358 -67.631  1.000 193.469 ? 64  PHE HHH CA  1 
ATOM 504  C C   . PHE A 1 65  ? 14.244  -46.380 -69.164  1.000 198.838 ? 64  PHE HHH C   1 
ATOM 505  O O   . PHE A 1 65  ? 14.473  -45.292 -69.707  1.000 202.167 ? 64  PHE HHH O   1 
ATOM 506  C CB  . PHE A 1 65  ? 15.560  -45.779 -67.149  1.000 188.976 ? 64  PHE HHH CB  1 
ATOM 507  C CG  . PHE A 1 65  ? 15.669  -45.614 -65.658  1.000 180.986 ? 64  PHE HHH CG  1 
ATOM 508  C CD1 . PHE A 1 65  ? 16.044  -46.687 -64.874  1.000 175.475 ? 64  PHE HHH CD1 1 
ATOM 509  C CD2 . PHE A 1 65  ? 15.382  -44.399 -65.046  1.000 175.430 ? 64  PHE HHH CD2 1 
ATOM 510  C CE1 . PHE A 1 65  ? 16.138  -46.542 -63.502  1.000 180.679 ? 64  PHE HHH CE1 1 
ATOM 511  C CE2 . PHE A 1 65  ? 15.476  -44.259 -63.671  1.000 173.205 ? 64  PHE HHH CE2 1 
ATOM 512  C CZ  . PHE A 1 65  ? 15.856  -45.332 -62.905  1.000 175.193 ? 64  PHE HHH CZ  1 
ATOM 513  N N   . GLN A 1 66  ? 14.014  -47.509 -69.847  1.000 201.429 ? 65  GLN HHH N   1 
ATOM 514  C CA  . GLN A 1 66  ? 13.929  -47.511 -71.339  1.000 209.442 ? 65  GLN HHH CA  1 
ATOM 515  C C   . GLN A 1 66  ? 12.747  -46.628 -71.757  1.000 207.437 ? 65  GLN HHH C   1 
ATOM 516  O O   . GLN A 1 66  ? 11.661  -46.790 -71.196  1.000 205.994 ? 65  GLN HHH O   1 
ATOM 517  C CB  . GLN A 1 66  ? 13.797  -48.916 -71.937  1.000 215.638 ? 65  GLN HHH CB  1 
ATOM 518  C CG  . GLN A 1 66  ? 13.914  -48.936 -73.463  1.000 219.247 ? 65  GLN HHH CG  1 
ATOM 519  C CD  . GLN A 1 66  ? 14.989  -49.855 -74.001  1.000 222.564 ? 65  GLN HHH CD  1 
ATOM 520  O OE1 . GLN A 1 66  ? 15.365  -50.848 -73.386  1.000 246.657 ? 65  GLN HHH OE1 1 
ATOM 521  N NE2 . GLN A 1 66  ? 15.513  -49.529 -75.169  1.000 215.550 ? 65  GLN HHH NE2 1 
ATOM 522  N N   . GLY A 1 67  ? 12.977  -45.679 -72.663  1.000 209.722 ? 66  GLY HHH N   1 
ATOM 523  C CA  . GLY A 1 67  ? 11.923  -44.795 -73.192  1.000 221.957 ? 66  GLY HHH CA  1 
ATOM 524  C C   . GLY A 1 67  ? 11.555  -43.660 -72.245  1.000 224.923 ? 66  GLY HHH C   1 
ATOM 525  O O   . GLY A 1 67  ? 10.769  -42.793 -72.677  1.000 252.296 ? 66  GLY HHH O   1 
ATOM 526  N N   . GLN A 1 68  ? 12.065  -43.648 -71.007  1.000 208.013 ? 67  GLN HHH N   1 
ATOM 527  C CA  . GLN A 1 68  ? 11.746  -42.598 -69.999  1.000 204.318 ? 67  GLN HHH CA  1 
ATOM 528  C C   . GLN A 1 68  ? 12.902  -41.594 -69.935  1.000 193.118 ? 67  GLN HHH C   1 
ATOM 529  O O   . GLN A 1 68  ? 12.679  -40.433 -69.529  1.000 186.687 ? 67  GLN HHH O   1 
ATOM 530  C CB  . GLN A 1 68  ? 11.426  -43.261 -68.662  1.000 208.610 ? 67  GLN HHH CB  1 
ATOM 531  C CG  . GLN A 1 68  ? 10.443  -44.410 -68.827  1.000 220.102 ? 67  GLN HHH CG  1 
ATOM 532  C CD  . GLN A 1 68  ? 9.596   -44.667 -67.610  1.000 234.925 ? 67  GLN HHH CD  1 
ATOM 533  O OE1 . GLN A 1 68  ? 9.741   -44.018 -66.579  1.000 252.318 ? 67  GLN HHH OE1 1 
ATOM 534  N NE2 . GLN A 1 68  ? 8.703   -45.638 -67.721  1.000 249.729 ? 67  GLN HHH NE2 1 
ATOM 535  N N   . VAL A 1 69  ? 14.101  -42.025 -70.320  1.000 192.286 ? 68  VAL HHH N   1 
ATOM 536  C CA  . VAL A 1 69  ? 15.279  -41.128 -70.518  1.000 198.194 ? 68  VAL HHH CA  1 
ATOM 537  C C   . VAL A 1 69  ? 16.051  -41.596 -71.750  1.000 200.088 ? 68  VAL HHH C   1 
ATOM 538  O O   . VAL A 1 69  ? 15.897  -42.769 -72.163  1.000 188.921 ? 68  VAL HHH O   1 
ATOM 539  C CB  . VAL A 1 69  ? 16.237  -41.073 -69.311  1.000 192.436 ? 68  VAL HHH CB  1 
ATOM 540  C CG1 . VAL A 1 69  ? 15.568  -40.538 -68.063  1.000 187.767 ? 68  VAL HHH CG1 1 
ATOM 541  C CG2 . VAL A 1 69  ? 16.908  -42.415 -69.049  1.000 187.281 ? 68  VAL HHH CG2 1 
ATOM 542  N N   . THR A 1 70  ? 16.895  -40.700 -72.257  1.000 207.648 ? 69  THR HHH N   1 
ATOM 543  C CA  . THR A 1 70  ? 17.846  -40.941 -73.366  1.000 211.520 ? 69  THR HHH CA  1 
ATOM 544  C C   . THR A 1 70  ? 19.254  -40.611 -72.849  1.000 196.935 ? 69  THR HHH C   1 
ATOM 545  O O   . THR A 1 70  ? 19.413  -39.639 -72.067  1.000 189.552 ? 69  THR HHH O   1 
ATOM 546  C CB  . THR A 1 70  ? 17.419  -40.174 -74.632  1.000 225.853 ? 69  THR HHH CB  1 
ATOM 547  O OG1 . THR A 1 70  ? 17.801  -38.805 -74.491  1.000 231.598 ? 69  THR HHH OG1 1 
ATOM 548  C CG2 . THR A 1 70  ? 15.931  -40.242 -74.924  1.000 226.517 ? 69  THR HHH CG2 1 
ATOM 549  N N   . ILE A 1 71  ? 20.232  -41.416 -73.257  1.000 187.014 ? 70  ILE HHH N   1 
ATOM 550  C CA  . ILE A 1 71  ? 21.658  -41.293 -72.844  1.000 190.168 ? 70  ILE HHH CA  1 
ATOM 551  C C   . ILE A 1 71  ? 22.465  -41.062 -74.112  1.000 180.615 ? 70  ILE HHH C   1 
ATOM 552  O O   . ILE A 1 71  ? 22.644  -42.003 -74.891  1.000 181.834 ? 70  ILE HHH O   1 
ATOM 553  C CB  . ILE A 1 71  ? 22.145  -42.537 -72.072  1.000 199.039 ? 70  ILE HHH CB  1 
ATOM 554  C CG1 . ILE A 1 71  ? 21.420  -42.668 -70.732  1.000 211.054 ? 70  ILE HHH CG1 1 
ATOM 555  C CG2 . ILE A 1 71  ? 23.659  -42.534 -71.887  1.000 191.729 ? 70  ILE HHH CG2 1 
ATOM 556  C CD1 . ILE A 1 71  ? 21.722  -43.956 -70.005  1.000 215.940 ? 70  ILE HHH CD1 1 
ATOM 557  N N   . SER A 1 72  ? 22.906  -39.832 -74.307  1.000 175.412 ? 71  SER HHH N   1 
ATOM 558  C CA  . SER A 1 72  ? 23.850  -39.468 -75.379  1.000 174.841 ? 71  SER HHH CA  1 
ATOM 559  C C   . SER A 1 72  ? 25.260  -39.503 -74.805  1.000 165.321 ? 71  SER HHH C   1 
ATOM 560  O O   . SER A 1 72  ? 25.445  -39.663 -73.596  1.000 159.691 ? 71  SER HHH O   1 
ATOM 561  C CB  . SER A 1 72  ? 23.512  -38.122 -75.949  1.000 191.855 ? 71  SER HHH CB  1 
ATOM 562  O OG  . SER A 1 72  ? 23.000  -37.264 -74.932  1.000 205.361 ? 71  SER HHH OG  1 
ATOM 563  N N   . ALA A 1 73  ? 26.232  -39.352 -75.672  1.000 166.196 ? 72  ALA HHH N   1 
ATOM 564  C CA  . ALA A 1 73  ? 27.626  -39.093 -75.289  1.000 166.301 ? 72  ALA HHH CA  1 
ATOM 565  C C   . ALA A 1 73  ? 28.271  -38.372 -76.463  1.000 172.846 ? 72  ALA HHH C   1 
ATOM 566  O O   . ALA A 1 73  ? 27.940  -38.759 -77.603  1.000 169.948 ? 72  ALA HHH O   1 
ATOM 567  C CB  . ALA A 1 73  ? 28.310  -40.392 -74.973  1.000 161.365 ? 72  ALA HHH CB  1 
ATOM 568  N N   . ASP A 1 74  ? 29.114  -37.368 -76.193  1.000 174.624 ? 73  ASP HHH N   1 
ATOM 569  C CA  . ASP A 1 74  ? 29.958  -36.703 -77.221  1.000 170.116 ? 73  ASP HHH CA  1 
ATOM 570  C C   . ASP A 1 74  ? 31.423  -37.110 -77.023  1.000 157.737 ? 73  ASP HHH C   1 
ATOM 571  O O   . ASP A 1 74  ? 32.067  -36.599 -76.107  1.000 159.186 ? 73  ASP HHH O   1 
ATOM 572  C CB  . ASP A 1 74  ? 29.734  -35.197 -77.217  1.000 183.239 ? 73  ASP HHH CB  1 
ATOM 573  C CG  . ASP A 1 74  ? 30.379  -34.510 -78.409  1.000 197.668 ? 73  ASP HHH CG  1 
ATOM 574  O OD1 . ASP A 1 74  ? 31.223  -35.167 -79.046  1.000 202.532 ? 73  ASP HHH OD1 1 
ATOM 575  O OD2 . ASP A 1 74  ? 30.030  -33.324 -78.690  1.000 198.043 ? 73  ASP HHH OD2 1 
ATOM 576  N N   . LYS A 1 75  ? 31.890  -38.063 -77.815  1.000 154.432 ? 74  LYS HHH N   1 
ATOM 577  C CA  . LYS A 1 75  ? 33.206  -38.691 -77.628  1.000 160.242 ? 74  LYS HHH CA  1 
ATOM 578  C C   . LYS A 1 75  ? 34.267  -37.608 -77.729  1.000 164.016 ? 74  LYS HHH C   1 
ATOM 579  O O   . LYS A 1 75  ? 35.340  -37.778 -77.123  1.000 175.672 ? 74  LYS HHH O   1 
ATOM 580  C CB  . LYS A 1 75  ? 33.435  -39.733 -78.713  1.000 172.065 ? 74  LYS HHH CB  1 
ATOM 581  C CG  . LYS A 1 75  ? 33.278  -39.233 -80.149  1.000 187.622 ? 74  LYS HHH CG  1 
ATOM 582  C CD  . LYS A 1 75  ? 33.551  -40.297 -81.190  1.000 196.284 ? 74  LYS HHH CD  1 
ATOM 583  C CE  . LYS A 1 75  ? 34.590  -41.311 -80.746  1.000 201.284 ? 74  LYS HHH CE  1 
ATOM 584  N NZ  . LYS A 1 75  ? 34.763  -42.409 -81.720  1.000 203.208 ? 74  LYS HHH NZ  1 
ATOM 585  N N   . SER A 1 76  ? 33.993  -36.559 -78.498  1.000 163.501 ? 75  SER HHH N   1 
ATOM 586  C CA  . SER A 1 76  ? 35.024  -35.573 -78.892  1.000 170.739 ? 75  SER HHH CA  1 
ATOM 587  C C   . SER A 1 76  ? 35.345  -34.683 -77.703  1.000 164.553 ? 75  SER HHH C   1 
ATOM 588  O O   . SER A 1 76  ? 36.346  -33.971 -77.824  1.000 167.220 ? 75  SER HHH O   1 
ATOM 589  C CB  . SER A 1 76  ? 34.585  -34.761 -80.066  1.000 186.918 ? 75  SER HHH CB  1 
ATOM 590  O OG  . SER A 1 76  ? 33.260  -34.302 -79.871  1.000 197.691 ? 75  SER HHH OG  1 
ATOM 591  N N   . ILE A 1 77  ? 34.543  -34.733 -76.629  1.000 157.836 ? 76  ILE HHH N   1 
ATOM 592  C CA  . ILE A 1 77  ? 34.775  -33.939 -75.381  1.000 157.455 ? 76  ILE HHH CA  1 
ATOM 593  C C   . ILE A 1 77  ? 34.695  -34.811 -74.123  1.000 157.021 ? 76  ILE HHH C   1 
ATOM 594  O O   . ILE A 1 77  ? 34.563  -34.267 -72.988  1.000 171.338 ? 76  ILE HHH O   1 
ATOM 595  C CB  . ILE A 1 77  ? 33.767  -32.787 -75.362  1.000 163.626 ? 76  ILE HHH CB  1 
ATOM 596  C CG1 . ILE A 1 77  ? 32.316  -33.268 -75.334  1.000 159.749 ? 76  ILE HHH CG1 1 
ATOM 597  C CG2 . ILE A 1 77  ? 34.020  -31.895 -76.563  1.000 178.562 ? 76  ILE HHH CG2 1 
ATOM 598  C CD1 . ILE A 1 77  ? 31.330  -32.183 -74.968  1.000 166.233 ? 76  ILE HHH CD1 1 
ATOM 599  N N   . ASN A 1 78  ? 34.772  -36.130 -74.302  1.000 152.792 ? 77  ASN HHH N   1 
ATOM 600  C CA  . ASN A 1 78  ? 34.749  -37.144 -73.214  1.000 144.437 ? 77  ASN HHH CA  1 
ATOM 601  C C   . ASN A 1 78  ? 33.536  -36.943 -72.306  1.000 132.661 ? 77  ASN HHH C   1 
ATOM 602  O O   . ASN A 1 78  ? 33.634  -37.160 -71.124  1.000 134.571 ? 77  ASN HHH O   1 
ATOM 603  C CB  . ASN A 1 78  ? 36.029  -37.084 -72.387  1.000 146.132 ? 77  ASN HHH CB  1 
ATOM 604  C CG  . ASN A 1 78  ? 37.258  -37.372 -73.210  1.000 150.108 ? 77  ASN HHH CG  1 
ATOM 605  O OD1 . ASN A 1 78  ? 37.152  -37.761 -74.369  1.000 153.292 ? 77  ASN HHH OD1 1 
ATOM 606  N ND2 . ASN A 1 78  ? 38.416  -37.169 -72.609  1.000 161.338 ? 77  ASN HHH ND2 1 
ATOM 607  N N   . THR A 1 79  ? 32.423  -36.545 -72.867  1.000 135.085 ? 78  THR HHH N   1 
ATOM 608  C CA  . THR A 1 79  ? 31.223  -36.161 -72.112  1.000 138.045 ? 78  THR HHH CA  1 
ATOM 609  C C   . THR A 1 79  ? 30.170  -37.219 -72.399  1.000 133.393 ? 78  THR HHH C   1 
ATOM 610  O O   . THR A 1 79  ? 30.114  -37.688 -73.535  1.000 142.010 ? 78  THR HHH O   1 
ATOM 611  C CB  . THR A 1 79  ? 30.783  -34.727 -72.471  1.000 148.778 ? 78  THR HHH CB  1 
ATOM 612  O OG1 . THR A 1 79  ? 31.816  -33.804 -72.083  1.000 144.335 ? 78  THR HHH OG1 1 
ATOM 613  C CG2 . THR A 1 79  ? 29.471  -34.335 -71.828  1.000 149.211 ? 78  THR HHH CG2 1 
ATOM 614  N N   . ALA A 1 80  ? 29.415  -37.600 -71.382  1.000 135.280 ? 79  ALA HHH N   1 
ATOM 615  C CA  . ALA A 1 80  ? 28.163  -38.367 -71.513  1.000 146.551 ? 79  ALA HHH CA  1 
ATOM 616  C C   . ALA A 1 80  ? 27.030  -37.529 -70.942  1.000 156.517 ? 79  ALA HHH C   1 
ATOM 617  O O   . ALA A 1 80  ? 27.278  -36.720 -70.027  1.000 152.922 ? 79  ALA HHH O   1 
ATOM 618  C CB  . ALA A 1 80  ? 28.267  -39.704 -70.827  1.000 145.710 ? 79  ALA HHH CB  1 
ATOM 619  N N   . TYR A 1 81  ? 25.841  -37.710 -71.508  1.000 172.279 ? 80  TYR HHH N   1 
ATOM 620  C CA  . TYR A 1 81  ? 24.637  -36.898 -71.223  1.000 178.023 ? 80  TYR HHH CA  1 
ATOM 621  C C   . TYR A 1 81  ? 23.493  -37.802 -70.752  1.000 187.723 ? 80  TYR HHH C   1 
ATOM 622  O O   . TYR A 1 81  ? 23.341  -38.961 -71.184  1.000 197.616 ? 80  TYR HHH O   1 
ATOM 623  C CB  . TYR A 1 81  ? 24.260  -36.095 -72.464  1.000 172.619 ? 80  TYR HHH CB  1 
ATOM 624  C CG  . TYR A 1 81  ? 25.226  -34.985 -72.786  1.000 181.028 ? 80  TYR HHH CG  1 
ATOM 625  C CD1 . TYR A 1 81  ? 25.376  -33.898 -71.937  1.000 187.247 ? 80  TYR HHH CD1 1 
ATOM 626  C CD2 . TYR A 1 81  ? 25.981  -34.994 -73.951  1.000 188.189 ? 80  TYR HHH CD2 1 
ATOM 627  C CE1 . TYR A 1 81  ? 26.252  -32.861 -72.233  1.000 186.716 ? 80  TYR HHH CE1 1 
ATOM 628  C CE2 . TYR A 1 81  ? 26.859  -33.961 -74.261  1.000 188.844 ? 80  TYR HHH CE2 1 
ATOM 629  C CZ  . TYR A 1 81  ? 26.998  -32.889 -73.395  1.000 182.238 ? 80  TYR HHH CZ  1 
ATOM 630  O OH  . TYR A 1 81  ? 27.865  -31.859 -73.626  1.000 157.296 ? 80  TYR HHH OH  1 
ATOM 631  N N   . LEU A 1 82  ? 22.689  -37.262 -69.849  1.000 182.612 ? 81  LEU HHH N   1 
ATOM 632  C CA  . LEU A 1 82  ? 21.410  -37.861 -69.427  1.000 177.306 ? 81  LEU HHH CA  1 
ATOM 633  C C   . LEU A 1 82  ? 20.367  -36.778 -69.639  1.000 175.688 ? 81  LEU HHH C   1 
ATOM 634  O O   . LEU A 1 82  ? 20.537  -35.706 -69.028  1.000 176.169 ? 81  LEU HHH O   1 
ATOM 635  C CB  . LEU A 1 82  ? 21.528  -38.252 -67.958  1.000 175.720 ? 81  LEU HHH CB  1 
ATOM 636  C CG  . LEU A 1 82  ? 20.279  -38.864 -67.344  1.000 176.342 ? 81  LEU HHH CG  1 
ATOM 637  C CD1 . LEU A 1 82  ? 19.961  -40.204 -67.982  1.000 175.985 ? 81  LEU HHH CD1 1 
ATOM 638  C CD2 . LEU A 1 82  ? 20.487  -39.015 -65.856  1.000 184.762 ? 81  LEU HHH CD2 1 
ATOM 639  N N   . GLN A 1 83  ? 19.397  -37.029 -70.515  1.000 168.948 ? 82  GLN HHH N   1 
ATOM 640  C CA  . GLN A 1 83  ? 18.401  -36.020 -70.934  1.000 174.979 ? 82  GLN HHH CA  1 
ATOM 641  C C   . GLN A 1 83  ? 17.007  -36.555 -70.647  1.000 166.549 ? 82  GLN HHH C   1 
ATOM 642  O O   . GLN A 1 83  ? 16.805  -37.754 -70.894  1.000 151.289 ? 82  GLN HHH O   1 
ATOM 643  C CB  . GLN A 1 83  ? 18.551  -35.716 -72.427  1.000 202.996 ? 82  GLN HHH CB  1 
ATOM 644  C CG  . GLN A 1 83  ? 17.306  -35.090 -73.056  1.000 219.610 ? 82  GLN HHH CG  1 
ATOM 645  C CD  . GLN A 1 83  ? 17.395  -34.913 -74.553  1.000 223.936 ? 82  GLN HHH CD  1 
ATOM 646  O OE1 . GLN A 1 83  ? 18.484  -34.815 -75.117  1.000 230.830 ? 82  GLN HHH OE1 1 
ATOM 647  N NE2 . GLN A 1 83  ? 16.240  -34.865 -75.205  1.000 225.420 ? 82  GLN HHH NE2 1 
ATOM 648  N N   . TRP A 1 84  ? 16.121  -35.672 -70.167  1.000 179.847 ? 83  TRP HHH N   1 
ATOM 649  C CA  . TRP A 1 84  ? 14.634  -35.814 -70.146  1.000 195.810 ? 83  TRP HHH CA  1 
ATOM 650  C C   . TRP A 1 84  ? 14.001  -34.910 -71.215  1.000 202.777 ? 83  TRP HHH C   1 
ATOM 651  O O   . TRP A 1 84  ? 14.677  -33.977 -71.711  1.000 214.851 ? 83  TRP HHH O   1 
ATOM 652  C CB  . TRP A 1 84  ? 14.061  -35.471 -68.765  1.000 196.995 ? 83  TRP HHH CB  1 
ATOM 653  C CG  . TRP A 1 84  ? 14.478  -36.415 -67.685  1.000 191.765 ? 83  TRP HHH CG  1 
ATOM 654  C CD1 . TRP A 1 84  ? 13.784  -37.502 -67.253  1.000 189.192 ? 83  TRP HHH CD1 1 
ATOM 655  C CD2 . TRP A 1 84  ? 15.689  -36.374 -66.909  1.000 187.553 ? 83  TRP HHH CD2 1 
ATOM 656  N NE1 . TRP A 1 84  ? 14.478  -38.137 -66.264  1.000 185.486 ? 83  TRP HHH NE1 1 
ATOM 657  C CE2 . TRP A 1 84  ? 15.644  -37.467 -66.027  1.000 180.902 ? 83  TRP HHH CE2 1 
ATOM 658  C CE3 . TRP A 1 84  ? 16.806  -35.533 -66.869  1.000 193.153 ? 83  TRP HHH CE3 1 
ATOM 659  C CZ2 . TRP A 1 84  ? 16.660  -37.733 -65.116  1.000 181.317 ? 83  TRP HHH CZ2 1 
ATOM 660  C CZ3 . TRP A 1 84  ? 17.817  -35.796 -65.969  1.000 182.058 ? 83  TRP HHH CZ3 1 
ATOM 661  C CH2 . TRP A 1 84  ? 17.738  -36.880 -65.102  1.000 176.526 ? 83  TRP HHH CH2 1 
ATOM 662  N N   . SER A 1 85  ? 12.744  -35.181 -71.557  1.000 195.995 ? 84  SER HHH N   1 
ATOM 663  C CA  . SER A 1 85  ? 11.927  -34.339 -72.463  1.000 201.224 ? 84  SER HHH CA  1 
ATOM 664  C C   . SER A 1 85  ? 10.909  -33.576 -71.626  1.000 194.780 ? 84  SER HHH C   1 
ATOM 665  O O   . SER A 1 85  ? 10.507  -32.504 -72.011  1.000 193.369 ? 84  SER HHH O   1 
ATOM 666  C CB  . SER A 1 85  ? 11.260  -35.181 -73.506  1.000 211.065 ? 84  SER HHH CB  1 
ATOM 667  O OG  . SER A 1 85  ? 10.981  -36.465 -72.977  1.000 222.165 ? 84  SER HHH OG  1 
ATOM 668  N N   . SER A 1 86  ? 10.502  -34.143 -70.506  1.000 200.166 ? 85  SER HHH N   1 
ATOM 669  C CA  . SER A 1 86  ? 9.528   -33.508 -69.594  1.000 208.928 ? 85  SER HHH CA  1 
ATOM 670  C C   . SER A 1 86  ? 9.699   -34.108 -68.198  1.000 203.504 ? 85  SER HHH C   1 
ATOM 671  O O   . SER A 1 86  ? 9.263   -35.262 -67.982  1.000 201.657 ? 85  SER HHH O   1 
ATOM 672  C CB  . SER A 1 86  ? 8.143   -33.665 -70.127  1.000 214.971 ? 85  SER HHH CB  1 
ATOM 673  O OG  . SER A 1 86  ? 7.364   -32.540 -69.769  1.000 234.513 ? 85  SER HHH OG  1 
ATOM 674  N N   . LEU A 1 87  ? 10.370  -33.362 -67.320  1.000 197.866 ? 86  LEU HHH N   1 
ATOM 675  C CA  . LEU A 1 87  ? 10.673  -33.770 -65.932  1.000 197.627 ? 86  LEU HHH CA  1 
ATOM 676  C C   . LEU A 1 87  ? 9.374   -33.946 -65.173  1.000 198.154 ? 86  LEU HHH C   1 
ATOM 677  O O   . LEU A 1 87  ? 8.613   -32.967 -65.176  1.000 210.849 ? 86  LEU HHH O   1 
ATOM 678  C CB  . LEU A 1 87  ? 11.484  -32.668 -65.256  1.000 204.092 ? 86  LEU HHH CB  1 
ATOM 679  C CG  . LEU A 1 87  ? 12.960  -32.636 -65.627  1.000 207.925 ? 86  LEU HHH CG  1 
ATOM 680  C CD1 . LEU A 1 87  ? 13.626  -31.475 -64.916  1.000 204.547 ? 86  LEU HHH CD1 1 
ATOM 681  C CD2 . LEU A 1 87  ? 13.652  -33.956 -65.277  1.000 210.386 ? 86  LEU HHH CD2 1 
ATOM 682  N N   . LYS A 1 88  ? 9.185   -35.111 -64.539  1.000 198.035 ? 87  LYS HHH N   1 
ATOM 683  C CA  . LYS A 1 88  ? 8.065   -35.401 -63.607  1.000 209.039 ? 87  LYS HHH CA  1 
ATOM 684  C C   . LYS A 1 88  ? 8.535   -35.095 -62.183  1.000 211.320 ? 87  LYS HHH C   1 
ATOM 685  O O   . LYS A 1 88  ? 9.759   -35.023 -61.968  1.000 215.592 ? 87  LYS HHH O   1 
ATOM 686  C CB  . LYS A 1 88  ? 7.585   -36.849 -63.759  1.000 209.434 ? 87  LYS HHH CB  1 
ATOM 687  C CG  . LYS A 1 88  ? 6.470   -37.057 -64.776  1.000 214.048 ? 87  LYS HHH CG  1 
ATOM 688  C CD  . LYS A 1 88  ? 6.028   -38.502 -65.008  1.000 208.969 ? 87  LYS HHH CD  1 
ATOM 689  C CE  . LYS A 1 88  ? 7.020   -39.349 -65.783  1.000 198.318 ? 87  LYS HHH CE  1 
ATOM 690  N NZ  . LYS A 1 88  ? 7.576   -38.639 -66.960  1.000 194.154 ? 87  LYS HHH NZ  1 
ATOM 691  N N   . ALA A 1 89  ? 7.598   -34.892 -61.257  1.000 213.205 ? 88  ALA HHH N   1 
ATOM 692  C CA  . ALA A 1 89  ? 7.902   -34.790 -59.815  1.000 212.575 ? 88  ALA HHH CA  1 
ATOM 693  C C   . ALA A 1 89  ? 8.616   -36.084 -59.389  1.000 203.552 ? 88  ALA HHH C   1 
ATOM 694  O O   . ALA A 1 89  ? 9.502   -36.016 -58.502  1.000 185.919 ? 88  ALA HHH O   1 
ATOM 695  C CB  . ALA A 1 89  ? 6.629   -34.523 -59.052  1.000 221.084 ? 88  ALA HHH CB  1 
ATOM 696  N N   . SER A 1 90  ? 8.277   -37.205 -60.047  1.000 198.037 ? 89  SER HHH N   1 
ATOM 697  C CA  . SER A 1 90  ? 8.911   -38.540 -59.890  1.000 192.833 ? 89  SER HHH CA  1 
ATOM 698  C C   . SER A 1 90  ? 10.424  -38.397 -59.830  1.000 193.620 ? 89  SER HHH C   1 
ATOM 699  O O   . SER A 1 90  ? 11.039  -39.184 -59.087  1.000 201.214 ? 89  SER HHH O   1 
ATOM 700  C CB  . SER A 1 90  ? 8.559   -39.472 -61.018  1.000 185.440 ? 89  SER HHH CB  1 
ATOM 701  O OG  . SER A 1 90  ? 7.163   -39.554 -61.185  1.000 191.954 ? 89  SER HHH OG  1 
ATOM 702  N N   . ASP A 1 91  ? 10.971  -37.445 -60.596  1.000 204.958 ? 90  ASP HHH N   1 
ATOM 703  C CA  . ASP A 1 91  ? 12.368  -37.462 -61.110  1.000 212.340 ? 90  ASP HHH CA  1 
ATOM 704  C C   . ASP A 1 91  ? 13.314  -36.726 -60.156  1.000 208.024 ? 90  ASP HHH C   1 
ATOM 705  O O   . ASP A 1 91  ? 14.506  -36.696 -60.473  1.000 201.853 ? 90  ASP HHH O   1 
ATOM 706  C CB  . ASP A 1 91  ? 12.447  -36.896 -62.536  1.000 216.377 ? 90  ASP HHH CB  1 
ATOM 707  C CG  . ASP A 1 91  ? 11.880  -37.833 -63.595  1.000 215.964 ? 90  ASP HHH CG  1 
ATOM 708  O OD1 . ASP A 1 91  ? 11.947  -39.058 -63.390  1.000 221.387 ? 90  ASP HHH OD1 1 
ATOM 709  O OD2 . ASP A 1 91  ? 11.384  -37.333 -64.625  1.000 209.590 ? 90  ASP HHH OD2 1 
ATOM 710  N N   . THR A 1 92  ? 12.818  -36.202 -59.029  1.000 211.042 ? 91  THR HHH N   1 
ATOM 711  C CA  . THR A 1 92  ? 13.644  -35.491 -58.016  1.000 215.468 ? 91  THR HHH CA  1 
ATOM 712  C C   . THR A 1 92  ? 14.510  -36.517 -57.266  1.000 200.841 ? 91  THR HHH C   1 
ATOM 713  O O   . THR A 1 92  ? 13.979  -37.414 -56.581  1.000 189.991 ? 91  THR HHH O   1 
ATOM 714  C CB  . THR A 1 92  ? 12.814  -34.613 -57.067  1.000 227.798 ? 91  THR HHH CB  1 
ATOM 715  O OG1 . THR A 1 92  ? 12.499  -35.377 -55.903  1.000 238.216 ? 91  THR HHH OG1 1 
ATOM 716  C CG2 . THR A 1 92  ? 11.540  -34.072 -57.681  1.000 229.473 ? 91  THR HHH CG2 1 
ATOM 717  N N   . ALA A 1 93  ? 15.822  -36.382 -57.403  1.000 185.852 ? 92  ALA HHH N   1 
ATOM 718  C CA  . ALA A 1 93  ? 16.811  -37.356 -56.910  1.000 176.180 ? 92  ALA HHH CA  1 
ATOM 719  C C   . ALA A 1 93  ? 18.210  -36.810 -57.175  1.000 175.542 ? 92  ALA HHH C   1 
ATOM 720  O O   . ALA A 1 93  ? 18.333  -35.731 -57.796  1.000 182.299 ? 92  ALA HHH O   1 
ATOM 721  C CB  . ALA A 1 93  ? 16.617  -38.699 -57.573  1.000 165.838 ? 92  ALA HHH CB  1 
ATOM 722  N N   . ILE A 1 94  ? 19.217  -37.525 -56.681  1.000 169.766 ? 93  ILE HHH N   1 
ATOM 723  C CA  . ILE A 1 94  ? 20.635  -37.311 -57.059  1.000 166.886 ? 93  ILE HHH CA  1 
ATOM 724  C C   . ILE A 1 94  ? 20.961  -38.323 -58.161  1.000 173.445 ? 93  ILE HHH C   1 
ATOM 725  O O   . ILE A 1 94  ? 20.513  -39.501 -58.067  1.000 157.740 ? 93  ILE HHH O   1 
ATOM 726  C CB  . ILE A 1 94  ? 21.583  -37.400 -55.853  1.000 169.633 ? 93  ILE HHH CB  1 
ATOM 727  C CG1 . ILE A 1 94  ? 22.939  -36.807 -56.234  1.000 181.732 ? 93  ILE HHH CG1 1 
ATOM 728  C CG2 . ILE A 1 94  ? 21.709  -38.835 -55.327  1.000 172.115 ? 93  ILE HHH CG2 1 
ATOM 729  C CD1 . ILE A 1 94  ? 23.815  -36.426 -55.070  1.000 191.832 ? 93  ILE HHH CD1 1 
ATOM 730  N N   . TYR A 1 95  ? 21.665  -37.849 -59.198  1.000 178.964 ? 94  TYR HHH N   1 
ATOM 731  C CA  . TYR A 1 95  ? 22.111  -38.654 -60.362  1.000 160.772 ? 94  TYR HHH CA  1 
ATOM 732  C C   . TYR A 1 95  ? 23.635  -38.678 -60.364  1.000 152.478 ? 94  TYR HHH C   1 
ATOM 733  O O   . TYR A 1 95  ? 24.280  -37.612 -60.374  1.000 139.607 ? 94  TYR HHH O   1 
ATOM 734  C CB  . TYR A 1 95  ? 21.500  -38.124 -61.654  1.000 149.722 ? 94  TYR HHH CB  1 
ATOM 735  C CG  . TYR A 1 95  ? 20.011  -38.333 -61.748  1.000 151.216 ? 94  TYR HHH CG  1 
ATOM 736  C CD1 . TYR A 1 95  ? 19.130  -37.429 -61.188  1.000 167.955 ? 94  TYR HHH CD1 1 
ATOM 737  C CD2 . TYR A 1 95  ? 19.474  -39.428 -62.392  1.000 148.463 ? 94  TYR HHH CD2 1 
ATOM 738  C CE1 . TYR A 1 95  ? 17.757  -37.596 -61.273  1.000 172.525 ? 94  TYR HHH CE1 1 
ATOM 739  C CE2 . TYR A 1 95  ? 18.103  -39.613 -62.483  1.000 156.931 ? 94  TYR HHH CE2 1 
ATOM 740  C CZ  . TYR A 1 95  ? 17.235  -38.698 -61.922  1.000 166.145 ? 94  TYR HHH CZ  1 
ATOM 741  O OH  . TYR A 1 95  ? 15.882  -38.871 -62.020  1.000 161.561 ? 94  TYR HHH OH  1 
ATOM 742  N N   . TYR A 1 96  ? 24.163  -39.892 -60.273  1.000 155.740 ? 95  TYR HHH N   1 
ATOM 743  C CA  . TYR A 1 96  ? 25.607  -40.191 -60.329  1.000 161.474 ? 95  TYR HHH CA  1 
ATOM 744  C C   . TYR A 1 96  ? 25.896  -40.652 -61.752  1.000 162.863 ? 95  TYR HHH C   1 
ATOM 745  O O   . TYR A 1 96  ? 25.099  -41.432 -62.289  1.000 170.524 ? 95  TYR HHH O   1 
ATOM 746  C CB  . TYR A 1 96  ? 25.981  -41.227 -59.261  1.000 157.605 ? 95  TYR HHH CB  1 
ATOM 747  C CG  . TYR A 1 96  ? 25.930  -40.720 -57.835  1.000 155.747 ? 95  TYR HHH CG  1 
ATOM 748  C CD1 . TYR A 1 96  ? 26.781  -39.711 -57.410  1.000 152.483 ? 95  TYR HHH CD1 1 
ATOM 749  C CD2 . TYR A 1 96  ? 25.058  -41.263 -56.899  1.000 152.331 ? 95  TYR HHH CD2 1 
ATOM 750  C CE1 . TYR A 1 96  ? 26.759  -39.239 -56.110  1.000 154.339 ? 95  TYR HHH CE1 1 
ATOM 751  C CE2 . TYR A 1 96  ? 25.028  -40.803 -55.592  1.000 159.058 ? 95  TYR HHH CE2 1 
ATOM 752  C CZ  . TYR A 1 96  ? 25.883  -39.784 -55.200  1.000 162.595 ? 95  TYR HHH CZ  1 
ATOM 753  O OH  . TYR A 1 96  ? 25.906  -39.284 -53.930  1.000 179.438 ? 95  TYR HHH OH  1 
ATOM 754  N N   . CYS A 1 97  ? 26.962  -40.134 -62.355  1.000 153.698 ? 96  CYS HHH N   1 
ATOM 755  C CA  . CYS A 1 97  ? 27.664  -40.811 -63.469  1.000 157.497 ? 96  CYS HHH CA  1 
ATOM 756  C C   . CYS A 1 97  ? 28.830  -41.620 -62.857  1.000 166.293 ? 96  CYS HHH C   1 
ATOM 757  O O   . CYS A 1 97  ? 29.489  -41.158 -61.865  1.000 143.472 ? 96  CYS HHH O   1 
ATOM 758  C CB  . CYS A 1 97  ? 28.098  -39.833 -64.548  1.000 158.389 ? 96  CYS HHH CB  1 
ATOM 759  S SG  . CYS A 1 97  ? 29.692  -39.047 -64.196  1.000 170.849 ? 96  CYS HHH SG  1 
ATOM 760  N N   . ALA A 1 98  ? 29.027  -42.838 -63.369  1.000 175.796 ? 97  ALA HHH N   1 
ATOM 761  C CA  . ALA A 1 98  ? 29.967  -43.850 -62.827  1.000 171.945 ? 97  ALA HHH CA  1 
ATOM 762  C C   . ALA A 1 98  ? 30.689  -44.527 -64.005  1.000 167.161 ? 97  ALA HHH C   1 
ATOM 763  O O   . ALA A 1 98  ? 30.019  -44.944 -64.978  1.000 154.689 ? 97  ALA HHH O   1 
ATOM 764  C CB  . ALA A 1 98  ? 29.237  -44.836 -61.917  1.000 170.696 ? 97  ALA HHH CB  1 
ATOM 765  N N   . GLY A 1 99  ? 32.018  -44.617 -63.923  1.000 164.134 ? 98  GLY HHH N   1 
ATOM 766  C CA  . GLY A 1 99  ? 32.881  -45.135 -64.997  1.000 161.109 ? 98  GLY HHH CA  1 
ATOM 767  C C   . GLY A 1 99  ? 33.532  -46.439 -64.610  1.000 155.784 ? 98  GLY HHH C   1 
ATOM 768  O O   . GLY A 1 99  ? 34.000  -46.541 -63.464  1.000 183.849 ? 98  GLY HHH O   1 
ATOM 769  N N   . GLY A 1 100 ? 33.550  -47.397 -65.534  1.000 155.902 ? 99  GLY HHH N   1 
ATOM 770  C CA  . GLY A 1 100 ? 34.477  -48.548 -65.525  1.000 166.222 ? 99  GLY HHH CA  1 
ATOM 771  C C   . GLY A 1 100 ? 35.053  -48.787 -66.915  1.000 162.745 ? 99  GLY HHH C   1 
ATOM 772  O O   . GLY A 1 100 ? 34.282  -48.743 -67.886  1.000 156.718 ? 99  GLY HHH O   1 
ATOM 773  N N   . SER A 1 101 ? 36.362  -49.014 -67.044  1.000 167.409 ? 100 SER HHH N   1 
ATOM 774  C CA  . SER A 1 101 ? 37.016  -49.136 -68.374  1.000 161.921 ? 100 SER HHH CA  1 
ATOM 775  C C   . SER A 1 101 ? 36.643  -50.495 -68.956  1.000 149.270 ? 100 SER HHH C   1 
ATOM 776  O O   . SER A 1 101 ? 37.495  -51.361 -69.087  1.000 163.543 ? 100 SER HHH O   1 
ATOM 777  C CB  . SER A 1 101 ? 38.519  -48.857 -68.352  1.000 171.062 ? 100 SER HHH CB  1 
ATOM 778  O OG  . SER A 1 101 ? 39.225  -49.585 -67.355  1.000 188.200 ? 100 SER HHH OG  1 
ATOM 779  N N   . GLY A 1 102 ? 35.370  -50.674 -69.262  1.000 139.355 ? 101 GLY HHH N   1 
ATOM 780  C CA  . GLY A 1 102 ? 34.884  -51.920 -69.867  1.000 144.155 ? 101 GLY HHH CA  1 
ATOM 781  C C   . GLY A 1 102 ? 33.389  -52.039 -69.731  1.000 143.835 ? 101 GLY HHH C   1 
ATOM 782  O O   . GLY A 1 102 ? 32.785  -51.143 -69.158  1.000 157.491 ? 101 GLY HHH O   1 
ATOM 783  N N   . ILE A 1 103 ? 32.821  -53.109 -70.259  1.000 145.061 ? 102 ILE HHH N   1 
ATOM 784  C CA  . ILE A 1 103 ? 31.437  -53.570 -69.967  1.000 159.640 ? 102 ILE HHH CA  1 
ATOM 785  C C   . ILE A 1 103 ? 31.624  -54.807 -69.091  1.000 162.745 ? 102 ILE HHH C   1 
ATOM 786  O O   . ILE A 1 103 ? 32.713  -55.387 -69.197  1.000 162.455 ? 102 ILE HHH O   1 
ATOM 787  C CB  . ILE A 1 103 ? 30.671  -53.865 -71.271  1.000 170.558 ? 102 ILE HHH CB  1 
ATOM 788  C CG1 . ILE A 1 103 ? 29.215  -54.248 -71.020  1.000 177.266 ? 102 ILE HHH CG1 1 
ATOM 789  C CG2 . ILE A 1 103 ? 31.366  -54.945 -72.082  1.000 183.530 ? 102 ILE HHH CG2 1 
ATOM 790  C CD1 . ILE A 1 103 ? 28.413  -53.162 -70.384  1.000 185.424 ? 102 ILE HHH CD1 1 
ATOM 791  N N   . SER A 1 104 ? 30.648  -55.196 -68.265  1.000 166.708 ? 103 SER HHH N   1 
ATOM 792  C CA  . SER A 1 104 ? 30.845  -56.257 -67.241  1.000 178.299 ? 103 SER HHH CA  1 
ATOM 793  C C   . SER A 1 104 ? 32.125  -55.940 -66.451  1.000 177.200 ? 103 SER HHH C   1 
ATOM 794  O O   . SER A 1 104 ? 33.052  -56.797 -66.352  1.000 174.390 ? 103 SER HHH O   1 
ATOM 795  C CB  . SER A 1 104 ? 30.904  -57.641 -67.862  1.000 182.860 ? 103 SER HHH CB  1 
ATOM 796  O OG  . SER A 1 104 ? 29.611  -58.119 -68.185  1.000 185.595 ? 103 SER HHH OG  1 
ATOM 797  N N   . THR A 1 105 ? 32.202  -54.718 -65.938  1.000 167.252 ? 104 THR HHH N   1 
ATOM 798  C CA  . THR A 1 105 ? 33.364  -54.236 -65.163  1.000 164.528 ? 104 THR HHH CA  1 
ATOM 799  C C   . THR A 1 105 ? 32.791  -53.542 -63.937  1.000 169.034 ? 104 THR HHH C   1 
ATOM 800  O O   . THR A 1 105 ? 31.721  -52.955 -64.001  1.000 180.335 ? 104 THR HHH O   1 
ATOM 801  C CB  . THR A 1 105 ? 34.277  -53.393 -66.060  1.000 153.258 ? 104 THR HHH CB  1 
ATOM 802  O OG1 . THR A 1 105 ? 35.414  -52.826 -65.412  1.000 142.546 ? 104 THR HHH OG1 1 
ATOM 803  C CG2 . THR A 1 105 ? 33.491  -52.263 -66.667  1.000 155.486 ? 104 THR HHH CG2 1 
ATOM 804  N N   . PRO A 1 106 ? 33.482  -53.611 -62.786  1.000 163.087 ? 105 PRO HHH N   1 
ATOM 805  C CA  . PRO A 1 106 ? 33.110  -52.786 -61.634  1.000 150.729 ? 105 PRO HHH CA  1 
ATOM 806  C C   . PRO A 1 106 ? 33.226  -51.276 -61.928  1.000 140.727 ? 105 PRO HHH C   1 
ATOM 807  O O   . PRO A 1 106 ? 34.117  -50.891 -62.657  1.000 155.190 ? 105 PRO HHH O   1 
ATOM 808  C CB  . PRO A 1 106 ? 34.148  -53.232 -60.593  1.000 164.073 ? 105 PRO HHH CB  1 
ATOM 809  C CG  . PRO A 1 106 ? 34.660  -54.597 -61.057  1.000 160.564 ? 105 PRO HHH CG  1 
ATOM 810  C CD  . PRO A 1 106 ? 34.647  -54.489 -62.556  1.000 162.899 ? 105 PRO HHH CD  1 
ATOM 811  N N   . MET A 1 107 ? 32.338  -50.433 -61.416  1.000 134.580 ? 106 MET HHH N   1 
ATOM 812  C CA  . MET A 1 107 ? 32.414  -48.975 -61.723  1.000 138.372 ? 106 MET HHH CA  1 
ATOM 813  C C   . MET A 1 107 ? 33.319  -48.338 -60.673  1.000 136.044 ? 106 MET HHH C   1 
ATOM 814  O O   . MET A 1 107 ? 32.853  -48.143 -59.560  1.000 134.420 ? 106 MET HHH O   1 
ATOM 815  C CB  . MET A 1 107 ? 31.050  -48.270 -61.774  1.000 141.469 ? 106 MET HHH CB  1 
ATOM 816  C CG  . MET A 1 107 ? 29.893  -49.145 -61.345  1.000 147.522 ? 106 MET HHH CG  1 
ATOM 817  S SD  . MET A 1 107 ? 28.268  -48.490 -61.748  1.000 160.248 ? 106 MET HHH SD  1 
ATOM 818  C CE  . MET A 1 107 ? 28.107  -48.965 -63.472  1.000 165.954 ? 106 MET HHH CE  1 
ATOM 819  N N   . ASP A 1 108 ? 34.584  -48.114 -61.047  1.000 139.478 ? 107 ASP HHH N   1 
ATOM 820  C CA  . ASP A 1 108 ? 35.711  -47.734 -60.155  1.000 147.273 ? 107 ASP HHH CA  1 
ATOM 821  C C   . ASP A 1 108 ? 35.856  -46.210 -60.069  1.000 142.935 ? 107 ASP HHH C   1 
ATOM 822  O O   . ASP A 1 108 ? 36.680  -45.738 -59.279  1.000 147.224 ? 107 ASP HHH O   1 
ATOM 823  C CB  . ASP A 1 108 ? 37.032  -48.349 -60.628  1.000 162.438 ? 107 ASP HHH CB  1 
ATOM 824  C CG  . ASP A 1 108 ? 37.456  -47.984 -62.047  1.000 185.365 ? 107 ASP HHH CG  1 
ATOM 825  O OD1 . ASP A 1 108 ? 38.309  -47.073 -62.205  1.000 205.443 ? 107 ASP HHH OD1 1 
ATOM 826  O OD2 . ASP A 1 108 ? 36.958  -48.637 -62.989  1.000 199.082 ? 107 ASP HHH OD2 1 
ATOM 827  N N   . VAL A 1 109 ? 35.117  -45.456 -60.872  1.000 137.021 ? 108 VAL HHH N   1 
ATOM 828  C CA  . VAL A 1 109 ? 35.165  -43.973 -60.847  1.000 137.026 ? 108 VAL HHH CA  1 
ATOM 829  C C   . VAL A 1 109 ? 33.734  -43.483 -60.668  1.000 141.394 ? 108 VAL HHH C   1 
ATOM 830  O O   . VAL A 1 109 ? 32.878  -43.977 -61.411  1.000 146.444 ? 108 VAL HHH O   1 
ATOM 831  C CB  . VAL A 1 109 ? 35.793  -43.401 -62.129  1.000 140.153 ? 108 VAL HHH CB  1 
ATOM 832  C CG1 . VAL A 1 109 ? 36.285  -41.979 -61.888  1.000 147.527 ? 108 VAL HHH CG1 1 
ATOM 833  C CG2 . VAL A 1 109 ? 36.912  -44.279 -62.678  1.000 136.871 ? 108 VAL HHH CG2 1 
ATOM 834  N N   . TRP A 1 110 ? 33.508  -42.542 -59.747  1.000 141.584 ? 109 TRP HHH N   1 
ATOM 835  C CA  . TRP A 1 110 ? 32.178  -41.937 -59.440  1.000 133.892 ? 109 TRP HHH CA  1 
ATOM 836  C C   . TRP A 1 110 ? 32.335  -40.436 -59.408  1.000 133.663 ? 109 TRP HHH C   1 
ATOM 837  O O   . TRP A 1 110 ? 33.153  -39.989 -58.587  1.000 132.328 ? 109 TRP HHH O   1 
ATOM 838  C CB  . TRP A 1 110 ? 31.633  -42.420 -58.087  1.000 133.337 ? 109 TRP HHH CB  1 
ATOM 839  C CG  . TRP A 1 110 ? 31.317  -43.882 -58.094  1.000 136.647 ? 109 TRP HHH CG  1 
ATOM 840  C CD1 . TRP A 1 110 ? 32.221  -44.913 -58.109  1.000 140.653 ? 109 TRP HHH CD1 1 
ATOM 841  C CD2 . TRP A 1 110 ? 30.012  -44.478 -58.204  1.000 132.096 ? 109 TRP HHH CD2 1 
ATOM 842  N NE1 . TRP A 1 110 ? 31.564  -46.113 -58.205  1.000 142.417 ? 109 TRP HHH NE1 1 
ATOM 843  C CE2 . TRP A 1 110 ? 30.205  -45.877 -58.264  1.000 143.573 ? 109 TRP HHH CE2 1 
ATOM 844  C CE3 . TRP A 1 110 ? 28.716  -43.983 -58.310  1.000 127.479 ? 109 TRP HHH CE3 1 
ATOM 845  C CZ2 . TRP A 1 110 ? 29.136  -46.772 -58.393  1.000 140.983 ? 109 TRP HHH CZ2 1 
ATOM 846  C CZ3 . TRP A 1 110 ? 27.667  -44.872 -58.437  1.000 131.069 ? 109 TRP HHH CZ3 1 
ATOM 847  C CH2 . TRP A 1 110 ? 27.867  -46.245 -58.464  1.000 127.835 ? 109 TRP HHH CH2 1 
ATOM 848  N N   . GLY A 1 111 ? 31.513  -39.711 -60.167  1.000 140.320 ? 110 GLY HHH N   1 
ATOM 849  C CA  . GLY A 1 111 ? 31.402  -38.245 -60.017  1.000 146.512 ? 110 GLY HHH CA  1 
ATOM 850  C C   . GLY A 1 111 ? 30.780  -37.842 -58.679  1.000 142.447 ? 110 GLY HHH C   1 
ATOM 851  O O   . GLY A 1 111 ? 30.186  -38.699 -58.001  1.000 136.807 ? 110 GLY HHH O   1 
ATOM 852  N N   . GLN A 1 112 ? 30.880  -36.555 -58.347  1.000 139.378 ? 111 GLN HHH N   1 
ATOM 853  C CA  . GLN A 1 112 ? 30.266  -35.901 -57.169  1.000 138.292 ? 111 GLN HHH CA  1 
ATOM 854  C C   . GLN A 1 112 ? 28.730  -36.072 -57.205  1.000 140.306 ? 111 GLN HHH C   1 
ATOM 855  O O   . GLN A 1 112 ? 28.127  -35.919 -56.148  1.000 151.520 ? 111 GLN HHH O   1 
ATOM 856  C CB  . GLN A 1 112 ? 30.774  -34.452 -57.106  1.000 145.204 ? 111 GLN HHH CB  1 
ATOM 857  C CG  . GLN A 1 112 ? 30.176  -33.507 -58.166  1.000 176.460 ? 111 GLN HHH CG  1 
ATOM 858  C CD  . GLN A 1 112 ? 31.002  -33.156 -59.405  1.000 198.487 ? 111 GLN HHH CD  1 
ATOM 859  O OE1 . GLN A 1 112 ? 31.151  -33.940 -60.344  1.000 210.527 ? 111 GLN HHH OE1 1 
ATOM 860  N NE2 . GLN A 1 112 ? 31.478  -31.921 -59.494  1.000 203.339 ? 111 GLN HHH NE2 1 
ATOM 861  N N   . GLY A 1 113 ? 28.104  -36.378 -58.352  1.000 148.900 ? 112 GLY HHH N   1 
ATOM 862  C CA  . GLY A 1 113 ? 26.629  -36.438 -58.538  1.000 156.436 ? 112 GLY HHH CA  1 
ATOM 863  C C   . GLY A 1 113 ? 25.981  -35.069 -58.746  1.000 158.899 ? 112 GLY HHH C   1 
ATOM 864  O O   . GLY A 1 113 ? 26.559  -34.054 -58.300  1.000 163.456 ? 112 GLY HHH O   1 
ATOM 865  N N   . THR A 1 114 ? 24.825  -35.021 -59.414  1.000 159.871 ? 113 THR HHH N   1 
ATOM 866  C CA  . THR A 1 114 ? 24.041  -33.776 -59.635  1.000 172.586 ? 113 THR HHH CA  1 
ATOM 867  C C   . THR A 1 114 ? 22.650  -34.003 -59.049  1.000 169.580 ? 113 THR HHH C   1 
ATOM 868  O O   . THR A 1 114 ? 22.011  -35.002 -59.425  1.000 163.527 ? 113 THR HHH O   1 
ATOM 869  C CB  . THR A 1 114 ? 23.944  -33.379 -61.118  1.000 176.428 ? 113 THR HHH CB  1 
ATOM 870  O OG1 . THR A 1 114 ? 22.758  -33.945 -61.675  1.000 183.712 ? 113 THR HHH OG1 1 
ATOM 871  C CG2 . THR A 1 114 ? 25.136  -33.820 -61.939  1.000 171.894 ? 113 THR HHH CG2 1 
ATOM 872  N N   . THR A 1 115 ? 22.205  -33.122 -58.160  1.000 170.102 ? 114 THR HHH N   1 
ATOM 873  C CA  . THR A 1 115 ? 20.856  -33.225 -57.559  1.000 183.586 ? 114 THR HHH CA  1 
ATOM 874  C C   . THR A 1 115 ? 19.891  -32.408 -58.416  1.000 180.049 ? 114 THR HHH C   1 
ATOM 875  O O   . THR A 1 115 ? 20.151  -31.201 -58.549  1.000 183.102 ? 114 THR HHH O   1 
ATOM 876  C CB  . THR A 1 115 ? 20.866  -32.793 -56.088  1.000 197.788 ? 114 THR HHH CB  1 
ATOM 877  O OG1 . THR A 1 115 ? 22.102  -33.209 -55.506  1.000 205.233 ? 114 THR HHH OG1 1 
ATOM 878  C CG2 . THR A 1 115 ? 19.699  -33.367 -55.306  1.000 198.224 ? 114 THR HHH CG2 1 
ATOM 879  N N   . VAL A 1 116 ? 18.837  -33.037 -58.959  1.000 180.043 ? 115 VAL HHH N   1 
ATOM 880  C CA  . VAL A 1 116 ? 17.751  -32.344 -59.721  1.000 192.488 ? 115 VAL HHH CA  1 
ATOM 881  C C   . VAL A 1 116 ? 16.454  -32.373 -58.897  1.000 188.974 ? 115 VAL HHH C   1 
ATOM 882  O O   . VAL A 1 116 ? 16.132  -33.430 -58.358  1.000 191.831 ? 115 VAL HHH O   1 
ATOM 883  C CB  . VAL A 1 116 ? 17.567  -32.978 -61.112  1.000 204.764 ? 115 VAL HHH CB  1 
ATOM 884  C CG1 . VAL A 1 116 ? 18.904  -33.371 -61.719  1.000 208.571 ? 115 VAL HHH CG1 1 
ATOM 885  C CG2 . VAL A 1 116 ? 16.640  -34.179 -61.095  1.000 210.335 ? 115 VAL HHH CG2 1 
ATOM 886  N N   . THR A 1 117 ? 15.751  -31.244 -58.791  1.000 184.234 ? 116 THR HHH N   1 
ATOM 887  C CA  . THR A 1 117 ? 14.549  -31.067 -57.930  1.000 182.249 ? 116 THR HHH CA  1 
ATOM 888  C C   . THR A 1 117 ? 13.449  -30.381 -58.754  1.000 193.916 ? 116 THR HHH C   1 
ATOM 889  O O   . THR A 1 117 ? 13.711  -29.289 -59.310  1.000 201.690 ? 116 THR HHH O   1 
ATOM 890  C CB  . THR A 1 117 ? 14.900  -30.313 -56.638  1.000 175.988 ? 116 THR HHH CB  1 
ATOM 891  O OG1 . THR A 1 117 ? 15.183  -28.934 -56.888  1.000 180.150 ? 116 THR HHH OG1 1 
ATOM 892  C CG2 . THR A 1 117 ? 16.094  -30.900 -55.928  1.000 171.329 ? 116 THR HHH CG2 1 
ATOM 893  N N   . VAL A 1 118 ? 12.264  -30.995 -58.824  1.000 192.818 ? 117 VAL HHH N   1 
ATOM 894  C CA  . VAL A 1 118 ? 11.181  -30.656 -59.796  1.000 190.155 ? 117 VAL HHH CA  1 
ATOM 895  C C   . VAL A 1 118 ? 9.994   -30.051 -59.039  1.000 201.963 ? 117 VAL HHH C   1 
ATOM 896  O O   . VAL A 1 118 ? 8.987   -30.790 -58.906  1.000 210.691 ? 117 VAL HHH O   1 
ATOM 897  C CB  . VAL A 1 118 ? 10.751  -31.900 -60.601  1.000 182.370 ? 117 VAL HHH CB  1 
ATOM 898  C CG1 . VAL A 1 118 ? 9.709   -31.558 -61.649  1.000 186.147 ? 117 VAL HHH CG1 1 
ATOM 899  C CG2 . VAL A 1 118 ? 11.933  -32.584 -61.271  1.000 186.862 ? 117 VAL HHH CG2 1 
ATOM 900  N N   . ALA A 1 119 ? 10.092  -28.781 -58.587  1.000 206.918 ? 118 ALA HHH N   1 
ATOM 901  C CA  . ALA A 1 119 ? 9.014   -28.015 -57.886  1.000 213.720 ? 118 ALA HHH CA  1 
ATOM 902  C C   . ALA A 1 119 ? 9.458   -26.580 -57.549  1.000 208.544 ? 118 ALA HHH C   1 
ATOM 903  O O   . ALA A 1 119 ? 10.669  -26.377 -57.365  1.000 204.274 ? 118 ALA HHH O   1 
ATOM 904  C CB  . ALA A 1 119 ? 8.605   -28.733 -56.615  1.000 223.600 ? 118 ALA HHH CB  1 
ATOM 905  N N   . SER A 1 120 ? 8.511   -25.642 -57.387  1.000 206.489 ? 119 SER HHH N   1 
ATOM 906  C CA  . SER A 1 120 ? 8.780   -24.200 -57.107  1.000 206.969 ? 119 SER HHH CA  1 
ATOM 907  C C   . SER A 1 120 ? 9.363   -24.015 -55.699  1.000 199.934 ? 119 SER HHH C   1 
ATOM 908  O O   . SER A 1 120 ? 9.001   -24.779 -54.803  1.000 204.758 ? 119 SER HHH O   1 
ATOM 909  C CB  . SER A 1 120 ? 7.542   -23.370 -57.303  1.000 211.284 ? 119 SER HHH CB  1 
ATOM 910  O OG  . SER A 1 120 ? 7.109   -23.438 -58.652  1.000 214.907 ? 119 SER HHH OG  1 
ATOM 911  N N   . THR A 1 121 ? 10.244  -23.030 -55.515  1.000 198.317 ? 120 THR HHH N   1 
ATOM 912  C CA  . THR A 1 121 ? 10.999  -22.802 -54.255  1.000 200.127 ? 120 THR HHH CA  1 
ATOM 913  C C   . THR A 1 121 ? 10.225  -21.850 -53.345  1.000 210.117 ? 120 THR HHH C   1 
ATOM 914  O O   . THR A 1 121 ? 9.539   -20.953 -53.873  1.000 218.573 ? 120 THR HHH O   1 
ATOM 915  C CB  . THR A 1 121 ? 12.393  -22.225 -54.514  1.000 203.634 ? 120 THR HHH CB  1 
ATOM 916  O OG1 . THR A 1 121 ? 12.248  -20.854 -54.897  1.000 212.338 ? 120 THR HHH OG1 1 
ATOM 917  C CG2 . THR A 1 121 ? 13.157  -22.998 -55.567  1.000 206.792 ? 120 THR HHH CG2 1 
ATOM 918  N N   . LYS A 1 122 ? 10.357  -22.054 -52.031  1.000 215.464 ? 121 LYS HHH N   1 
ATOM 919  C CA  . LYS A 1 122 ? 9.767   -21.202 -50.967  1.000 215.497 ? 121 LYS HHH CA  1 
ATOM 920  C C   . LYS A 1 122 ? 10.770  -21.054 -49.816  1.000 209.747 ? 121 LYS HHH C   1 
ATOM 921  O O   . LYS A 1 122 ? 11.395  -22.045 -49.436  1.000 191.142 ? 121 LYS HHH O   1 
ATOM 922  C CB  . LYS A 1 122 ? 8.450   -21.793 -50.463  1.000 217.159 ? 121 LYS HHH CB  1 
ATOM 923  C CG  . LYS A 1 122 ? 7.714   -20.885 -49.493  1.000 226.155 ? 121 LYS HHH CG  1 
ATOM 924  C CD  . LYS A 1 122 ? 6.696   -21.587 -48.633  1.000 234.471 ? 121 LYS HHH CD  1 
ATOM 925  C CE  . LYS A 1 122 ? 6.259   -20.743 -47.455  1.000 242.319 ? 121 LYS HHH CE  1 
ATOM 926  N NZ  . LYS A 1 122 ? 7.364   -20.546 -46.484  1.000 248.212 ? 121 LYS HHH NZ  1 
ATOM 927  N N   . GLY A 1 123 ? 10.916  -19.841 -49.291  1.000 221.860 ? 122 GLY HHH N   1 
ATOM 928  C CA  . GLY A 1 123 ? 11.868  -19.517 -48.215  1.000 226.257 ? 122 GLY HHH CA  1 
ATOM 929  C C   . GLY A 1 123 ? 11.385  -20.078 -46.886  1.000 235.335 ? 122 GLY HHH C   1 
ATOM 930  O O   . GLY A 1 123 ? 10.178  -20.229 -46.690  1.000 234.741 ? 122 GLY HHH O   1 
ATOM 931  N N   . PRO A 1 124 ? 12.305  -20.405 -45.946  1.000 243.603 ? 123 PRO HHH N   1 
ATOM 932  C CA  . PRO A 1 124 ? 11.915  -20.901 -44.624  1.000 239.394 ? 123 PRO HHH CA  1 
ATOM 933  C C   . PRO A 1 124 ? 11.474  -19.779 -43.666  1.000 223.796 ? 123 PRO HHH C   1 
ATOM 934  O O   . PRO A 1 124 ? 12.035  -18.704 -43.731  1.000 226.624 ? 123 PRO HHH O   1 
ATOM 935  C CB  . PRO A 1 124 ? 13.203  -21.602 -44.144  1.000 239.932 ? 123 PRO HHH CB  1 
ATOM 936  C CG  . PRO A 1 124 ? 14.323  -20.801 -44.771  1.000 240.795 ? 123 PRO HHH CG  1 
ATOM 937  C CD  . PRO A 1 124 ? 13.768  -20.325 -46.101  1.000 243.015 ? 123 PRO HHH CD  1 
ATOM 938  N N   . SER A 1 125 ? 10.475  -20.051 -42.821  1.000 208.976 ? 124 SER HHH N   1 
ATOM 939  C CA  . SER A 1 125 ? 10.134  -19.230 -41.631  1.000 213.182 ? 124 SER HHH CA  1 
ATOM 940  C C   . SER A 1 125 ? 10.917  -19.765 -40.430  1.000 218.665 ? 124 SER HHH C   1 
ATOM 941  O O   . SER A 1 125 ? 10.919  -20.997 -40.231  1.000 224.800 ? 124 SER HHH O   1 
ATOM 942  C CB  . SER A 1 125 ? 8.662   -19.240 -41.374  1.000 213.188 ? 124 SER HHH CB  1 
ATOM 943  O OG  . SER A 1 125 ? 7.964   -18.844 -42.542  1.000 216.890 ? 124 SER HHH OG  1 
ATOM 944  N N   . VAL A 1 126 ? 11.572  -18.878 -39.675  1.000 225.815 ? 125 VAL HHH N   1 
ATOM 945  C CA  . VAL A 1 126 ? 12.471  -19.251 -38.543  1.000 225.644 ? 125 VAL HHH CA  1 
ATOM 946  C C   . VAL A 1 126 ? 11.821  -18.792 -37.240  1.000 221.174 ? 125 VAL HHH C   1 
ATOM 947  O O   . VAL A 1 126 ? 11.560  -17.588 -37.104  1.000 231.757 ? 125 VAL HHH O   1 
ATOM 948  C CB  . VAL A 1 126 ? 13.877  -18.653 -38.711  1.000 236.318 ? 125 VAL HHH CB  1 
ATOM 949  C CG1 . VAL A 1 126 ? 14.865  -19.261 -37.726  1.000 242.192 ? 125 VAL HHH CG1 1 
ATOM 950  C CG2 . VAL A 1 126 ? 14.381  -18.820 -40.134  1.000 237.554 ? 125 VAL HHH CG2 1 
ATOM 951  N N   . PHE A 1 127 ? 11.578  -19.737 -36.334  1.000 211.755 ? 126 PHE HHH N   1 
ATOM 952  C CA  . PHE A 1 127 ? 10.905  -19.515 -35.033  1.000 195.322 ? 126 PHE HHH CA  1 
ATOM 953  C C   . PHE A 1 127 ? 11.819  -20.011 -33.919  1.000 191.028 ? 126 PHE HHH C   1 
ATOM 954  O O   . PHE A 1 127 ? 12.371  -21.107 -33.984  1.000 176.895 ? 126 PHE HHH O   1 
ATOM 955  C CB  . PHE A 1 127 ? 9.555   -20.224 -35.028  1.000 188.576 ? 126 PHE HHH CB  1 
ATOM 956  C CG  . PHE A 1 127 ? 8.650   -19.928 -36.198  1.000 183.964 ? 126 PHE HHH CG  1 
ATOM 957  C CD1 . PHE A 1 127 ? 8.146   -18.655 -36.402  1.000 183.649 ? 126 PHE HHH CD1 1 
ATOM 958  C CD2 . PHE A 1 127 ? 8.236   -20.940 -37.052  1.000 181.014 ? 126 PHE HHH CD2 1 
ATOM 959  C CE1 . PHE A 1 127 ? 7.262   -18.398 -37.442  1.000 185.595 ? 126 PHE HHH CE1 1 
ATOM 960  C CE2 . PHE A 1 127 ? 7.355   -20.679 -38.092  1.000 183.953 ? 126 PHE HHH CE2 1 
ATOM 961  C CZ  . PHE A 1 127 ? 6.865   -19.408 -38.285  1.000 184.438 ? 126 PHE HHH CZ  1 
ATOM 962  N N   . PRO A 1 128 ? 12.017  -19.208 -32.858  1.000 195.512 ? 127 PRO HHH N   1 
ATOM 963  C CA  . PRO A 1 128 ? 12.902  -19.587 -31.763  1.000 199.396 ? 127 PRO HHH CA  1 
ATOM 964  C C   . PRO A 1 128 ? 12.246  -20.569 -30.784  1.000 195.544 ? 127 PRO HHH C   1 
ATOM 965  O O   . PRO A 1 128 ? 11.050  -20.488 -30.570  1.000 194.605 ? 127 PRO HHH O   1 
ATOM 966  C CB  . PRO A 1 128 ? 13.168  -18.244 -31.072  1.000 204.094 ? 127 PRO HHH CB  1 
ATOM 967  C CG  . PRO A 1 128 ? 11.883  -17.479 -31.274  1.000 204.182 ? 127 PRO HHH CG  1 
ATOM 968  C CD  . PRO A 1 128 ? 11.400  -17.892 -32.651  1.000 201.467 ? 127 PRO HHH CD  1 
ATOM 969  N N   . LEU A 1 129 ? 13.048  -21.491 -30.254  1.000 193.372 ? 128 LEU HHH N   1 
ATOM 970  C CA  . LEU A 1 129 ? 12.683  -22.381 -29.125  1.000 188.937 ? 128 LEU HHH CA  1 
ATOM 971  C C   . LEU A 1 129 ? 13.489  -21.908 -27.914  1.000 188.398 ? 128 LEU HHH C   1 
ATOM 972  O O   . LEU A 1 129 ? 14.653  -22.312 -27.786  1.000 180.001 ? 128 LEU HHH O   1 
ATOM 973  C CB  . LEU A 1 129 ? 12.970  -23.836 -29.519  1.000 190.513 ? 128 LEU HHH CB  1 
ATOM 974  C CG  . LEU A 1 129 ? 12.364  -24.274 -30.855  1.000 187.314 ? 128 LEU HHH CG  1 
ATOM 975  C CD1 . LEU A 1 129 ? 12.838  -25.651 -31.293  1.000 180.148 ? 128 LEU HHH CD1 1 
ATOM 976  C CD2 . LEU A 1 129 ? 10.852  -24.216 -30.787  1.000 187.691 ? 128 LEU HHH CD2 1 
ATOM 977  N N   . ALA A 1 130 ? 12.914  -21.019 -27.105  1.000 194.177 ? 129 ALA HHH N   1 
ATOM 978  C CA  . ALA A 1 130 ? 13.589  -20.437 -25.925  1.000 195.278 ? 129 ALA HHH CA  1 
ATOM 979  C C   . ALA A 1 130 ? 13.660  -21.490 -24.825  1.000 201.861 ? 129 ALA HHH C   1 
ATOM 980  O O   . ALA A 1 130 ? 12.791  -22.355 -24.713  1.000 194.586 ? 129 ALA HHH O   1 
ATOM 981  C CB  . ALA A 1 130 ? 12.876  -19.197 -25.456  1.000 196.524 ? 129 ALA HHH CB  1 
ATOM 982  N N   . PRO A 1 131 ? 14.707  -21.451 -23.977  1.000 211.344 ? 130 PRO HHH N   1 
ATOM 983  C CA  . PRO A 1 131 ? 14.810  -22.374 -22.849  1.000 213.968 ? 130 PRO HHH CA  1 
ATOM 984  C C   . PRO A 1 131 ? 13.925  -21.999 -21.648  1.000 217.052 ? 130 PRO HHH C   1 
ATOM 985  O O   . PRO A 1 131 ? 13.248  -20.975 -21.685  1.000 204.318 ? 130 PRO HHH O   1 
ATOM 986  C CB  . PRO A 1 131 ? 16.293  -22.253 -22.463  1.000 218.733 ? 130 PRO HHH CB  1 
ATOM 987  C CG  . PRO A 1 131 ? 16.639  -20.822 -22.814  1.000 219.608 ? 130 PRO HHH CG  1 
ATOM 988  C CD  . PRO A 1 131 ? 15.840  -20.514 -24.064  1.000 213.158 ? 130 PRO HHH CD  1 
ATOM 989  N N   . SER A 1 132 ? 13.954  -22.886 -20.647  1.000 229.791 ? 131 SER HHH N   1 
ATOM 990  C CA  . SER A 1 132 ? 13.516  -22.720 -19.235  1.000 237.551 ? 131 SER HHH CA  1 
ATOM 991  C C   . SER A 1 132 ? 14.507  -23.465 -18.324  1.000 240.678 ? 131 SER HHH C   1 
ATOM 992  O O   . SER A 1 132 ? 15.391  -24.175 -18.861  1.000 238.875 ? 131 SER HHH O   1 
ATOM 993  C CB  A SER A 1 132 ? 12.080  -23.181 -19.057  0.500 237.498 ? 131 SER HHH CB  1 
ATOM 994  C CB  B SER A 1 132 ? 12.097  -23.193 -19.031  0.500 238.712 ? 131 SER HHH CB  1 
ATOM 995  O OG  A SER A 1 132 ? 11.918  -24.545 -19.427  0.500 233.906 ? 131 SER HHH OG  1 
ATOM 996  O OG  B SER A 1 132 ? 11.184  -22.277 -19.615  0.500 238.940 ? 131 SER HHH OG  1 
ATOM 997  N N   . SER A 1 133 ? 14.370  -23.276 -17.008  1.000 236.548 ? 132 SER HHH N   1 
ATOM 998  C CA  . SER A 1 133 ? 15.339  -23.654 -15.953  1.000 228.900 ? 132 SER HHH CA  1 
ATOM 999  C C   . SER A 1 133 ? 15.761  -25.122 -16.127  1.000 224.510 ? 132 SER HHH C   1 
ATOM 1000 O O   . SER A 1 133 ? 15.086  -25.967 -15.527  1.000 223.554 ? 132 SER HHH O   1 
ATOM 1001 C CB  . SER A 1 133 ? 14.717  -23.360 -14.608  1.000 227.415 ? 132 SER HHH CB  1 
ATOM 1002 O OG  . SER A 1 133 ? 14.167  -22.041 -14.579  1.000 222.500 ? 132 SER HHH OG  1 
ATOM 1003 N N   . GLY A 1 134 ? 18.344  -24.544 -13.359  1.000 281.962 ? 137 GLY HHH N   1 
ATOM 1004 C CA  . GLY A 1 134 ? 18.516  -25.983 -13.091  1.000 277.590 ? 137 GLY HHH CA  1 
ATOM 1005 C C   . GLY A 1 134 ? 19.972  -26.371 -13.245  1.000 277.265 ? 137 GLY HHH C   1 
ATOM 1006 O O   . GLY A 1 134 ? 20.824  -25.741 -12.585  1.000 278.926 ? 137 GLY HHH O   1 
ATOM 1007 N N   . GLY A 1 135 ? 20.259  -27.345 -14.110  1.000 267.964 ? 138 GLY HHH N   1 
ATOM 1008 C CA  . GLY A 1 135 ? 21.635  -27.806 -14.374  1.000 260.737 ? 138 GLY HHH CA  1 
ATOM 1009 C C   . GLY A 1 135 ? 22.201  -27.107 -15.590  1.000 253.493 ? 138 GLY HHH C   1 
ATOM 1010 O O   . GLY A 1 135 ? 22.674  -25.952 -15.476  1.000 264.918 ? 138 GLY HHH O   1 
ATOM 1011 N N   . THR A 1 136 ? 22.126  -27.786 -16.728  1.000 239.133 ? 139 THR HHH N   1 
ATOM 1012 C CA  . THR A 1 136 ? 22.430  -27.252 -18.079  1.000 225.759 ? 139 THR HHH CA  1 
ATOM 1013 C C   . THR A 1 136 ? 21.166  -27.402 -18.937  1.000 222.860 ? 139 THR HHH C   1 
ATOM 1014 O O   . THR A 1 136 ? 20.586  -28.497 -18.890  1.000 235.981 ? 139 THR HHH O   1 
ATOM 1015 C CB  . THR A 1 136 ? 23.637  -28.009 -18.637  1.000 221.640 ? 139 THR HHH CB  1 
ATOM 1016 O OG1 . THR A 1 136 ? 23.156  -29.257 -19.136  1.000 209.316 ? 139 THR HHH OG1 1 
ATOM 1017 C CG2 . THR A 1 136 ? 24.705  -28.243 -17.589  1.000 229.229 ? 139 THR HHH CG2 1 
ATOM 1018 N N   . ALA A 1 137 ? 20.760  -26.377 -19.702  1.000 215.741 ? 140 ALA HHH N   1 
ATOM 1019 C CA  . ALA A 1 137 ? 19.473  -26.335 -20.450  1.000 205.747 ? 140 ALA HHH CA  1 
ATOM 1020 C C   . ALA A 1 137 ? 19.687  -26.419 -21.972  1.000 192.395 ? 140 ALA HHH C   1 
ATOM 1021 O O   . ALA A 1 137 ? 20.801  -26.138 -22.458  1.000 182.435 ? 140 ALA HHH O   1 
ATOM 1022 C CB  . ALA A 1 137 ? 18.708  -25.091 -20.075  1.000 205.757 ? 140 ALA HHH CB  1 
ATOM 1023 N N   . ALA A 1 138 ? 18.633  -26.811 -22.689  1.000 184.057 ? 141 ALA HHH N   1 
ATOM 1024 C CA  . ALA A 1 138 ? 18.572  -26.861 -24.164  1.000 184.331 ? 141 ALA HHH CA  1 
ATOM 1025 C C   . ALA A 1 138 ? 17.778  -25.660 -24.695  1.000 193.748 ? 141 ALA HHH C   1 
ATOM 1026 O O   . ALA A 1 138 ? 16.948  -25.128 -23.951  1.000 195.024 ? 141 ALA HHH O   1 
ATOM 1027 C CB  . ALA A 1 138 ? 17.964  -28.164 -24.600  1.000 177.172 ? 141 ALA HHH CB  1 
ATOM 1028 N N   . LEU A 1 139 ? 18.067  -25.255 -25.936  1.000 214.625 ? 142 LEU HHH N   1 
ATOM 1029 C CA  . LEU A 1 139 ? 17.423  -24.148 -26.704  1.000 218.913 ? 142 LEU HHH CA  1 
ATOM 1030 C C   . LEU A 1 139 ? 17.670  -24.386 -28.198  1.000 210.291 ? 142 LEU HHH C   1 
ATOM 1031 O O   . LEU A 1 139 ? 18.557  -25.218 -28.506  1.000 200.794 ? 142 LEU HHH O   1 
ATOM 1032 C CB  . LEU A 1 139 ? 18.001  -22.800 -26.255  1.000 232.265 ? 142 LEU HHH CB  1 
ATOM 1033 C CG  . LEU A 1 139 ? 19.511  -22.609 -26.442  1.000 236.268 ? 142 LEU HHH CG  1 
ATOM 1034 C CD1 . LEU A 1 139 ? 19.859  -22.081 -27.822  1.000 230.120 ? 142 LEU HHH CD1 1 
ATOM 1035 C CD2 . LEU A 1 139 ? 20.060  -21.667 -25.389  1.000 241.230 ? 142 LEU HHH CD2 1 
ATOM 1036 N N   . GLY A 1 140 ? 16.936  -23.702 -29.089  1.000 205.937 ? 143 GLY HHH N   1 
ATOM 1037 C CA  . GLY A 1 140 ? 17.027  -23.985 -30.538  1.000 206.959 ? 143 GLY HHH CA  1 
ATOM 1038 C C   . GLY A 1 140 ? 16.221  -23.055 -31.436  1.000 203.079 ? 143 GLY HHH C   1 
ATOM 1039 O O   . GLY A 1 140 ? 15.577  -22.133 -30.920  1.000 193.356 ? 143 GLY HHH O   1 
ATOM 1040 N N   . CYS A 1 141 ? 16.269  -23.328 -32.743  1.000 206.570 ? 144 CYS HHH N   1 
ATOM 1041 C CA  . CYS A 1 141 ? 15.536  -22.646 -33.838  1.000 207.385 ? 144 CYS HHH CA  1 
ATOM 1042 C C   . CYS A 1 141 ? 14.632  -23.676 -34.514  1.000 193.766 ? 144 CYS HHH C   1 
ATOM 1043 O O   . CYS A 1 141 ? 15.087  -24.825 -34.754  1.000 187.806 ? 144 CYS HHH O   1 
ATOM 1044 C CB  . CYS A 1 141 ? 16.492  -22.082 -34.888  1.000 231.588 ? 144 CYS HHH CB  1 
ATOM 1045 S SG  . CYS A 1 141 ? 16.962  -20.351 -34.618  1.000 267.430 ? 144 CYS HHH SG  1 
ATOM 1046 N N   . LEU A 1 142 ? 13.406  -23.279 -34.835  1.000 188.025 ? 145 LEU HHH N   1 
ATOM 1047 C CA  . LEU A 1 142 ? 12.515  -24.086 -35.704  1.000 190.287 ? 145 LEU HHH CA  1 
ATOM 1048 C C   . LEU A 1 142 ? 12.546  -23.508 -37.121  1.000 193.901 ? 145 LEU HHH C   1 
ATOM 1049 O O   . LEU A 1 142 ? 12.028  -22.409 -37.333  1.000 202.736 ? 145 LEU HHH O   1 
ATOM 1050 C CB  . LEU A 1 142 ? 11.089  -24.094 -35.147  1.000 187.322 ? 145 LEU HHH CB  1 
ATOM 1051 C CG  . LEU A 1 142 ? 10.100  -24.853 -36.025  1.000 182.742 ? 145 LEU HHH CG  1 
ATOM 1052 C CD1 . LEU A 1 142 ? 10.457  -26.330 -36.068  1.000 180.284 ? 145 LEU HHH CD1 1 
ATOM 1053 C CD2 . LEU A 1 142 ? 8.675   -24.662 -35.557  1.000 182.908 ? 145 LEU HHH CD2 1 
ATOM 1054 N N   . VAL A 1 143 ? 13.131  -24.228 -38.068  1.000 192.937 ? 146 VAL HHH N   1 
ATOM 1055 C CA  . VAL A 1 143 ? 13.144  -23.804 -39.495  1.000 191.269 ? 146 VAL HHH CA  1 
ATOM 1056 C C   . VAL A 1 143 ? 11.984  -24.539 -40.178  1.000 183.020 ? 146 VAL HHH C   1 
ATOM 1057 O O   . VAL A 1 143 ? 12.018  -25.766 -40.291  1.000 175.823 ? 146 VAL HHH O   1 
ATOM 1058 C CB  . VAL A 1 143 ? 14.523  -24.062 -40.134  1.000 197.700 ? 146 VAL HHH CB  1 
ATOM 1059 C CG1 . VAL A 1 143 ? 14.696  -23.268 -41.420  1.000 203.373 ? 146 VAL HHH CG1 1 
ATOM 1060 C CG2 . VAL A 1 143 ? 15.665  -23.764 -39.159  1.000 195.079 ? 146 VAL HHH CG2 1 
ATOM 1061 N N   . LYS A 1 144 ? 10.938  -23.820 -40.546  1.000 185.842 ? 147 LYS HHH N   1 
ATOM 1062 C CA  . LYS A 1 144 ? 9.645   -24.451 -40.898  1.000 194.887 ? 147 LYS HHH CA  1 
ATOM 1063 C C   . LYS A 1 144 ? 9.156   -23.937 -42.253  1.000 205.963 ? 147 LYS HHH C   1 
ATOM 1064 O O   . LYS A 1 144 ? 9.374   -22.743 -42.561  1.000 208.633 ? 147 LYS HHH O   1 
ATOM 1065 C CB  . LYS A 1 144 ? 8.616   -24.155 -39.807  1.000 202.564 ? 147 LYS HHH CB  1 
ATOM 1066 C CG  . LYS A 1 144 ? 7.256   -24.802 -40.028  1.000 208.790 ? 147 LYS HHH CG  1 
ATOM 1067 C CD  . LYS A 1 144 ? 6.227   -24.498 -38.953  1.000 207.485 ? 147 LYS HHH CD  1 
ATOM 1068 C CE  . LYS A 1 144 ? 4.805   -24.584 -39.475  1.000 209.163 ? 147 LYS HHH CE  1 
ATOM 1069 N NZ  . LYS A 1 144 ? 4.504   -25.899 -40.094  1.000 206.658 ? 147 LYS HHH NZ  1 
ATOM 1070 N N   . ASP A 1 145 ? 8.481   -24.814 -43.004  1.000 216.334 ? 148 ASP HHH N   1 
ATOM 1071 C CA  . ASP A 1 145 ? 7.761   -24.501 -44.270  1.000 224.310 ? 148 ASP HHH CA  1 
ATOM 1072 C C   . ASP A 1 145 ? 8.713   -23.896 -45.306  1.000 228.734 ? 148 ASP HHH C   1 
ATOM 1073 O O   . ASP A 1 145 ? 8.714   -22.652 -45.437  1.000 224.445 ? 148 ASP HHH O   1 
ATOM 1074 C CB  . ASP A 1 145 ? 6.577   -23.569 -44.016  1.000 222.134 ? 148 ASP HHH CB  1 
ATOM 1075 C CG  . ASP A 1 145 ? 5.446   -24.259 -43.278  1.000 225.407 ? 148 ASP HHH CG  1 
ATOM 1076 O OD1 . ASP A 1 145 ? 5.293   -25.474 -43.458  1.000 219.083 ? 148 ASP HHH OD1 1 
ATOM 1077 O OD2 . ASP A 1 145 ? 4.739   -23.582 -42.517  1.000 244.732 ? 148 ASP HHH OD2 1 
ATOM 1078 N N   . TYR A 1 146 ? 9.451   -24.749 -46.029  1.000 230.806 ? 149 TYR HHH N   1 
ATOM 1079 C CA  . TYR A 1 146 ? 10.414  -24.365 -47.095  1.000 232.838 ? 149 TYR HHH CA  1 
ATOM 1080 C C   . TYR A 1 146 ? 10.542  -25.481 -48.136  1.000 229.312 ? 149 TYR HHH C   1 
ATOM 1081 O O   . TYR A 1 146 ? 10.228  -26.640 -47.833  1.000 222.640 ? 149 TYR HHH O   1 
ATOM 1082 C CB  . TYR A 1 146 ? 11.775  -24.005 -46.485  1.000 232.983 ? 149 TYR HHH CB  1 
ATOM 1083 C CG  . TYR A 1 146 ? 12.593  -25.138 -45.920  1.000 223.562 ? 149 TYR HHH CG  1 
ATOM 1084 C CD1 . TYR A 1 146 ? 12.398  -25.578 -44.623  1.000 224.286 ? 149 TYR HHH CD1 1 
ATOM 1085 C CD2 . TYR A 1 146 ? 13.609  -25.724 -46.657  1.000 215.791 ? 149 TYR HHH CD2 1 
ATOM 1086 C CE1 . TYR A 1 146 ? 13.164  -26.596 -44.081  1.000 223.495 ? 149 TYR HHH CE1 1 
ATOM 1087 C CE2 . TYR A 1 146 ? 14.387  -26.742 -46.129  1.000 214.376 ? 149 TYR HHH CE2 1 
ATOM 1088 C CZ  . TYR A 1 146 ? 14.158  -27.184 -44.840  1.000 213.809 ? 149 TYR HHH CZ  1 
ATOM 1089 O OH  . TYR A 1 146 ? 14.916  -28.180 -44.307  1.000 205.324 ? 149 TYR HHH OH  1 
ATOM 1090 N N   . PHE A 1 147 ? 11.006  -25.125 -49.337  1.000 223.391 ? 150 PHE HHH N   1 
ATOM 1091 C CA  . PHE A 1 147 ? 11.255  -26.065 -50.461  1.000 213.308 ? 150 PHE HHH CA  1 
ATOM 1092 C C   . PHE A 1 147 ? 12.297  -25.475 -51.413  1.000 202.731 ? 150 PHE HHH C   1 
ATOM 1093 O O   . PHE A 1 147 ? 12.269  -24.274 -51.679  1.000 188.689 ? 150 PHE HHH O   1 
ATOM 1094 C CB  . PHE A 1 147 ? 9.943   -26.399 -51.184  1.000 213.599 ? 150 PHE HHH CB  1 
ATOM 1095 C CG  . PHE A 1 147 ? 10.010  -27.682 -51.975  1.000 210.492 ? 150 PHE HHH CG  1 
ATOM 1096 C CD1 . PHE A 1 147 ? 10.670  -27.748 -53.194  1.000 204.727 ? 150 PHE HHH CD1 1 
ATOM 1097 C CD2 . PHE A 1 147 ? 9.437   -28.840 -51.480  1.000 208.227 ? 150 PHE HHH CD2 1 
ATOM 1098 C CE1 . PHE A 1 147 ? 10.763  -28.943 -53.888  1.000 197.632 ? 150 PHE HHH CE1 1 
ATOM 1099 C CE2 . PHE A 1 147 ? 9.533   -30.034 -52.176  1.000 204.572 ? 150 PHE HHH CE2 1 
ATOM 1100 C CZ  . PHE A 1 147 ? 10.191  -30.081 -53.379  1.000 201.312 ? 150 PHE HHH CZ  1 
ATOM 1101 N N   . PRO A 1 148 ? 13.248  -26.282 -51.954  1.000 202.162 ? 151 PRO HHH N   1 
ATOM 1102 C CA  . PRO A 1 148 ? 13.584  -27.609 -51.434  1.000 199.287 ? 151 PRO HHH CA  1 
ATOM 1103 C C   . PRO A 1 148 ? 14.739  -27.580 -50.420  1.000 197.464 ? 151 PRO HHH C   1 
ATOM 1104 O O   . PRO A 1 148 ? 15.151  -26.495 -49.995  1.000 192.216 ? 151 PRO HHH O   1 
ATOM 1105 C CB  . PRO A 1 148 ? 14.027  -28.339 -52.705  1.000 202.699 ? 151 PRO HHH CB  1 
ATOM 1106 C CG  . PRO A 1 148 ? 14.746  -27.254 -53.518  1.000 208.720 ? 151 PRO HHH CG  1 
ATOM 1107 C CD  . PRO A 1 148 ? 14.070  -25.951 -53.132  1.000 209.725 ? 151 PRO HHH CD  1 
ATOM 1108 N N   . GLU A 1 149 ? 15.240  -28.755 -50.031  1.000 187.233 ? 152 GLU HHH N   1 
ATOM 1109 C CA  . GLU A 1 149 ? 16.446  -28.838 -49.175  1.000 191.926 ? 152 GLU HHH CA  1 
ATOM 1110 C C   . GLU A 1 149 ? 17.635  -28.439 -50.030  1.000 203.441 ? 152 GLU HHH C   1 
ATOM 1111 O O   . GLU A 1 149 ? 17.538  -28.492 -51.249  1.000 227.434 ? 152 GLU HHH O   1 
ATOM 1112 C CB  . GLU A 1 149 ? 16.591  -30.243 -48.621  1.000 193.543 ? 152 GLU HHH CB  1 
ATOM 1113 C CG  . GLU A 1 149 ? 15.798  -30.449 -47.358  1.000 199.616 ? 152 GLU HHH CG  1 
ATOM 1114 C CD  . GLU A 1 149 ? 16.455  -31.421 -46.404  1.000 211.900 ? 152 GLU HHH CD  1 
ATOM 1115 O OE1 . GLU A 1 149 ? 17.260  -30.953 -45.576  1.000 217.533 ? 152 GLU HHH OE1 1 
ATOM 1116 O OE2 . GLU A 1 149 ? 16.183  -32.643 -46.512  1.000 229.366 ? 152 GLU HHH OE2 1 
ATOM 1117 N N   . PRO A 1 150 ? 18.785  -28.030 -49.449  1.000 214.189 ? 153 PRO HHH N   1 
ATOM 1118 C CA  . PRO A 1 150 ? 18.998  -28.035 -48.004  1.000 200.550 ? 153 PRO HHH CA  1 
ATOM 1119 C C   . PRO A 1 150 ? 18.578  -26.732 -47.330  1.000 185.701 ? 153 PRO HHH C   1 
ATOM 1120 O O   . PRO A 1 150 ? 18.355  -25.771 -48.011  1.000 185.691 ? 153 PRO HHH O   1 
ATOM 1121 C CB  . PRO A 1 150 ? 20.527  -28.171 -47.895  1.000 219.204 ? 153 PRO HHH CB  1 
ATOM 1122 C CG  . PRO A 1 150 ? 21.082  -27.499 -49.155  1.000 228.516 ? 153 PRO HHH CG  1 
ATOM 1123 C CD  . PRO A 1 150 ? 19.964  -27.531 -50.181  1.000 229.028 ? 153 PRO HHH CD  1 
ATOM 1124 N N   . VAL A 1 151 ? 18.541  -26.721 -46.007  1.000 177.742 ? 154 VAL HHH N   1 
ATOM 1125 C CA  . VAL A 1 151 ? 18.732  -25.461 -45.240  1.000 185.737 ? 154 VAL HHH CA  1 
ATOM 1126 C C   . VAL A 1 151 ? 19.883  -25.706 -44.264  1.000 189.749 ? 154 VAL HHH C   1 
ATOM 1127 O O   . VAL A 1 151 ? 19.907  -26.784 -43.648  1.000 217.993 ? 154 VAL HHH O   1 
ATOM 1128 C CB  . VAL A 1 151 ? 17.424  -25.005 -44.560  1.000 182.183 ? 154 VAL HHH CB  1 
ATOM 1129 C CG1 . VAL A 1 151 ? 17.068  -25.863 -43.369  1.000 167.445 ? 154 VAL HHH CG1 1 
ATOM 1130 C CG2 . VAL A 1 151 ? 17.454  -23.529 -44.179  1.000 189.651 ? 154 VAL HHH CG2 1 
ATOM 1131 N N   . THR A 1 152 ? 20.820  -24.767 -44.142  1.000 185.922 ? 155 THR HHH N   1 
ATOM 1132 C CA  . THR A 1 152 ? 21.931  -24.846 -43.154  1.000 189.983 ? 155 THR HHH CA  1 
ATOM 1133 C C   . THR A 1 152 ? 21.642  -23.893 -41.995  1.000 199.098 ? 155 THR HHH C   1 
ATOM 1134 O O   . THR A 1 152 ? 21.063  -22.815 -42.238  1.000 202.335 ? 155 THR HHH O   1 
ATOM 1135 C CB  . THR A 1 152 ? 23.300  -24.524 -43.760  1.000 191.600 ? 155 THR HHH CB  1 
ATOM 1136 O OG1 . THR A 1 152 ? 23.356  -23.113 -44.000  1.000 204.476 ? 155 THR HHH OG1 1 
ATOM 1137 C CG2 . THR A 1 152 ? 23.580  -25.337 -45.008  1.000 192.980 ? 155 THR HHH CG2 1 
ATOM 1138 N N   . VAL A 1 153 ? 22.058  -24.277 -40.786  1.000 201.978 ? 156 VAL HHH N   1 
ATOM 1139 C CA  . VAL A 1 153 ? 21.988  -23.418 -39.569  1.000 200.523 ? 156 VAL HHH CA  1 
ATOM 1140 C C   . VAL A 1 153 ? 23.304  -23.548 -38.794  1.000 200.606 ? 156 VAL HHH C   1 
ATOM 1141 O O   . VAL A 1 153 ? 23.774  -24.671 -38.591  1.000 199.688 ? 156 VAL HHH O   1 
ATOM 1142 C CB  . VAL A 1 153 ? 20.764  -23.788 -38.722  1.000 199.991 ? 156 VAL HHH CB  1 
ATOM 1143 C CG1 . VAL A 1 153 ? 20.573  -25.290 -38.686  1.000 199.386 ? 156 VAL HHH CG1 1 
ATOM 1144 C CG2 . VAL A 1 153 ? 20.823  -23.191 -37.327  1.000 205.482 ? 156 VAL HHH CG2 1 
ATOM 1145 N N   . SER A 1 154 ? 23.896  -22.415 -38.431  1.000 204.136 ? 157 SER HHH N   1 
ATOM 1146 C CA  . SER A 1 154 ? 25.061  -22.316 -37.522  1.000 204.844 ? 157 SER HHH CA  1 
ATOM 1147 C C   . SER A 1 154 ? 24.638  -21.442 -36.342  1.000 207.366 ? 157 SER HHH C   1 
ATOM 1148 O O   . SER A 1 154 ? 23.580  -20.800 -36.425  1.000 204.634 ? 157 SER HHH O   1 
ATOM 1149 C CB  . SER A 1 154 ? 26.275  -21.774 -38.232  1.000 205.265 ? 157 SER HHH CB  1 
ATOM 1150 O OG  . SER A 1 154 ? 26.003  -20.522 -38.852  1.000 199.412 ? 157 SER HHH OG  1 
ATOM 1151 N N   . TRP A 1 155 ? 25.415  -21.456 -35.270  1.000 207.786 ? 158 TRP HHH N   1 
ATOM 1152 C CA  . TRP A 1 155 ? 25.070  -20.774 -34.001  1.000 212.469 ? 158 TRP HHH CA  1 
ATOM 1153 C C   . TRP A 1 155 ? 26.186  -19.780 -33.673  1.000 213.128 ? 158 TRP HHH C   1 
ATOM 1154 O O   . TRP A 1 155 ? 27.337  -20.227 -33.572  1.000 228.343 ? 158 TRP HHH O   1 
ATOM 1155 C CB  . TRP A 1 155 ? 24.871  -21.843 -32.917  1.000 220.230 ? 158 TRP HHH CB  1 
ATOM 1156 C CG  . TRP A 1 155 ? 23.558  -22.563 -33.022  1.000 215.932 ? 158 TRP HHH CG  1 
ATOM 1157 C CD1 . TRP A 1 155 ? 23.304  -23.769 -33.617  1.000 209.878 ? 158 TRP HHH CD1 1 
ATOM 1158 C CD2 . TRP A 1 155 ? 22.296  -22.085 -32.533  1.000 202.305 ? 158 TRP HHH CD2 1 
ATOM 1159 N NE1 . TRP A 1 155 ? 21.973  -24.076 -33.521  1.000 202.665 ? 158 TRP HHH NE1 1 
ATOM 1160 C CE2 . TRP A 1 155 ? 21.330  -23.060 -32.866  1.000 194.416 ? 158 TRP HHH CE2 1 
ATOM 1161 C CE3 . TRP A 1 155 ? 21.906  -20.927 -31.853  1.000 198.358 ? 158 TRP HHH CE3 1 
ATOM 1162 C CZ2 . TRP A 1 155 ? 19.990  -22.915 -32.531  1.000 192.961 ? 158 TRP HHH CZ2 1 
ATOM 1163 C CZ3 . TRP A 1 155 ? 20.583  -20.787 -31.517  1.000 206.427 ? 158 TRP HHH CZ3 1 
ATOM 1164 C CH2 . TRP A 1 155 ? 19.642  -21.767 -31.856  1.000 208.726 ? 158 TRP HHH CH2 1 
ATOM 1165 N N   . ASN A 1 156 ? 25.877  -18.486 -33.551  1.000 215.686 ? 159 ASN HHH N   1 
ATOM 1166 C CA  . ASN A 1 156 ? 26.897  -17.415 -33.368  1.000 220.529 ? 159 ASN HHH CA  1 
ATOM 1167 C C   . ASN A 1 156 ? 27.937  -17.573 -34.500  1.000 215.210 ? 159 ASN HHH C   1 
ATOM 1168 O O   . ASN A 1 156 ? 29.154  -17.433 -34.244  1.000 201.254 ? 159 ASN HHH O   1 
ATOM 1169 C CB  . ASN A 1 156 ? 27.483  -17.437 -31.944  1.000 231.405 ? 159 ASN HHH CB  1 
ATOM 1170 C CG  . ASN A 1 156 ? 26.451  -17.395 -30.824  1.000 238.966 ? 159 ASN HHH CG  1 
ATOM 1171 O OD1 . ASN A 1 156 ? 25.248  -17.509 -31.060  1.000 240.658 ? 159 ASN HHH OD1 1 
ATOM 1172 N ND2 . ASN A 1 156 ? 26.902  -17.249 -29.587  1.000 235.123 ? 159 ASN HHH ND2 1 
ATOM 1173 N N   . SER A 1 157 ? 27.457  -17.906 -35.709  1.000 215.467 ? 160 SER HHH N   1 
ATOM 1174 C CA  . SER A 1 157 ? 28.227  -18.060 -36.973  1.000 217.501 ? 160 SER HHH CA  1 
ATOM 1175 C C   . SER A 1 157 ? 29.264  -19.192 -36.899  1.000 225.348 ? 160 SER HHH C   1 
ATOM 1176 O O   . SER A 1 157 ? 30.122  -19.244 -37.792  1.000 224.426 ? 160 SER HHH O   1 
ATOM 1177 C CB  . SER A 1 157 ? 28.890  -16.764 -37.347  1.000 224.139 ? 160 SER HHH CB  1 
ATOM 1178 O OG  . SER A 1 157 ? 27.942  -15.716 -37.457  1.000 227.690 ? 160 SER HHH OG  1 
ATOM 1179 N N   . GLY A 1 158 ? 29.177  -20.102 -35.926  1.000 236.807 ? 161 GLY HHH N   1 
ATOM 1180 C CA  . GLY A 1 158 ? 30.166  -21.186 -35.738  1.000 234.174 ? 161 GLY HHH CA  1 
ATOM 1181 C C   . GLY A 1 158 ? 31.004  -21.020 -34.473  1.000 241.303 ? 161 GLY HHH C   1 
ATOM 1182 O O   . GLY A 1 158 ? 31.858  -21.898 -34.224  1.000 235.744 ? 161 GLY HHH O   1 
ATOM 1183 N N   . ALA A 1 159 ? 30.775  -19.964 -33.674  1.000 245.715 ? 162 ALA HHH N   1 
ATOM 1184 C CA  . ALA A 1 159 ? 31.373  -19.780 -32.325  1.000 249.687 ? 162 ALA HHH CA  1 
ATOM 1185 C C   . ALA A 1 159 ? 30.830  -20.835 -31.342  1.000 252.507 ? 162 ALA HHH C   1 
ATOM 1186 O O   . ALA A 1 159 ? 31.370  -20.935 -30.227  1.000 263.945 ? 162 ALA HHH O   1 
ATOM 1187 C CB  . ALA A 1 159 ? 31.110  -18.381 -31.821  1.000 254.923 ? 162 ALA HHH CB  1 
ATOM 1188 N N   . LEU A 1 160 ? 29.777  -21.561 -31.730  1.000 241.904 ? 163 LEU HHH N   1 
ATOM 1189 C CA  . LEU A 1 160 ? 29.216  -22.742 -31.020  1.000 226.021 ? 163 LEU HHH CA  1 
ATOM 1190 C C   . LEU A 1 160 ? 29.214  -23.948 -31.964  1.000 206.365 ? 163 LEU HHH C   1 
ATOM 1191 O O   . LEU A 1 160 ? 28.333  -24.011 -32.835  1.000 197.286 ? 163 LEU HHH O   1 
ATOM 1192 C CB  . LEU A 1 160 ? 27.780  -22.418 -30.601  1.000 233.606 ? 163 LEU HHH CB  1 
ATOM 1193 C CG  . LEU A 1 160 ? 27.497  -22.360 -29.105  1.000 250.143 ? 163 LEU HHH CG  1 
ATOM 1194 C CD1 . LEU A 1 160 ? 25.995  -22.272 -28.865  1.000 250.822 ? 163 LEU HHH CD1 1 
ATOM 1195 C CD2 . LEU A 1 160 ? 28.086  -23.566 -28.389  1.000 253.620 ? 163 LEU HHH CD2 1 
ATOM 1196 N N   . THR A 1 161 ? 30.151  -24.878 -31.812  1.000 198.295 ? 164 THR HHH N   1 
ATOM 1197 C CA  . THR A 1 161 ? 30.034  -26.227 -32.428  1.000 203.925 ? 164 THR HHH CA  1 
ATOM 1198 C C   . THR A 1 161 ? 29.679  -27.233 -31.334  1.000 205.748 ? 164 THR HHH C   1 
ATOM 1199 O O   . THR A 1 161 ? 29.079  -28.262 -31.691  1.000 211.905 ? 164 THR HHH O   1 
ATOM 1200 C CB  . THR A 1 161 ? 31.294  -26.654 -33.196  1.000 208.706 ? 164 THR HHH CB  1 
ATOM 1201 O OG1 . THR A 1 161 ? 31.958  -25.470 -33.633  1.000 233.187 ? 164 THR HHH OG1 1 
ATOM 1202 C CG2 . THR A 1 161 ? 31.000  -27.547 -34.387  1.000 197.239 ? 164 THR HHH CG2 1 
ATOM 1203 N N   . SER A 1 162 ? 30.007  -26.919 -30.071  1.000 206.163 ? 165 SER HHH N   1 
ATOM 1204 C CA  . SER A 1 162 ? 29.798  -27.777 -28.872  1.000 207.033 ? 165 SER HHH CA  1 
ATOM 1205 C C   . SER A 1 162 ? 28.301  -28.013 -28.618  1.000 202.056 ? 165 SER HHH C   1 
ATOM 1206 O O   . SER A 1 162 ? 27.581  -27.029 -28.422  1.000 198.889 ? 165 SER HHH O   1 
ATOM 1207 C CB  . SER A 1 162 ? 30.469  -27.172 -27.655  1.000 214.666 ? 165 SER HHH CB  1 
ATOM 1208 O OG  . SER A 1 162 ? 30.142  -27.890 -26.468  1.000 219.418 ? 165 SER HHH OG  1 
ATOM 1209 N N   . GLY A 1 163 ? 27.868  -29.279 -28.621  1.000 204.158 ? 166 GLY HHH N   1 
ATOM 1210 C CA  . GLY A 1 163 ? 26.543  -29.736 -28.149  1.000 210.298 ? 166 GLY HHH CA  1 
ATOM 1211 C C   . GLY A 1 163 ? 25.408  -29.428 -29.110  1.000 207.713 ? 166 GLY HHH C   1 
ATOM 1212 O O   . GLY A 1 163 ? 24.248  -29.360 -28.636  1.000 203.891 ? 166 GLY HHH O   1 
ATOM 1213 N N   . VAL A 1 164 ? 25.706  -29.264 -30.403  1.000 207.270 ? 167 VAL HHH N   1 
ATOM 1214 C CA  . VAL A 1 164 ? 24.697  -28.850 -31.426  1.000 207.018 ? 167 VAL HHH CA  1 
ATOM 1215 C C   . VAL A 1 164 ? 24.126  -30.109 -32.083  1.000 205.379 ? 167 VAL HHH C   1 
ATOM 1216 O O   . VAL A 1 164 ? 24.926  -30.979 -32.467  1.000 222.919 ? 167 VAL HHH O   1 
ATOM 1217 C CB  . VAL A 1 164 ? 25.282  -27.887 -32.479  1.000 200.991 ? 167 VAL HHH CB  1 
ATOM 1218 C CG1 . VAL A 1 164 ? 24.177  -27.316 -33.364  1.000 197.011 ? 167 VAL HHH CG1 1 
ATOM 1219 C CG2 . VAL A 1 164 ? 26.090  -26.756 -31.846  1.000 207.089 ? 167 VAL HHH CG2 1 
ATOM 1220 N N   . HIS A 1 165 ? 22.799  -30.191 -32.198  1.000 197.888 ? 168 HIS HHH N   1 
ATOM 1221 C CA  . HIS A 1 165 ? 22.077  -31.200 -33.017  1.000 192.612 ? 168 HIS HHH CA  1 
ATOM 1222 C C   . HIS A 1 165 ? 21.072  -30.474 -33.923  1.000 192.745 ? 168 HIS HHH C   1 
ATOM 1223 O O   . HIS A 1 165 ? 20.112  -29.853 -33.429  1.000 196.492 ? 168 HIS HHH O   1 
ATOM 1224 C CB  . HIS A 1 165 ? 21.465  -32.287 -32.120  1.000 190.248 ? 168 HIS HHH CB  1 
ATOM 1225 C CG  . HIS A 1 165 ? 22.464  -33.258 -31.583  1.000 193.762 ? 168 HIS HHH CG  1 
ATOM 1226 N ND1 . HIS A 1 165 ? 23.397  -33.872 -32.395  1.000 203.505 ? 168 HIS HHH ND1 1 
ATOM 1227 C CD2 . HIS A 1 165 ? 22.677  -33.734 -30.335  1.000 198.149 ? 168 HIS HHH CD2 1 
ATOM 1228 C CE1 . HIS A 1 165 ? 24.149  -34.676 -31.672  1.000 207.688 ? 168 HIS HHH CE1 1 
ATOM 1229 N NE2 . HIS A 1 165 ? 23.725  -34.611 -30.398  1.000 204.826 ? 168 HIS HHH NE2 1 
ATOM 1230 N N   . THR A 1 166 ? 21.323  -30.471 -35.224  1.000 197.104 ? 169 THR HHH N   1 
ATOM 1231 C CA  . THR A 1 166 ? 20.347  -29.984 -36.231  1.000 199.517 ? 169 THR HHH CA  1 
ATOM 1232 C C   . THR A 1 166 ? 19.664  -31.215 -36.817  1.000 189.453 ? 169 THR HHH C   1 
ATOM 1233 O O   . THR A 1 166 ? 20.384  -32.137 -37.233  1.000 201.661 ? 169 THR HHH O   1 
ATOM 1234 C CB  . THR A 1 166 ? 21.026  -29.132 -37.307  1.000 201.690 ? 169 THR HHH CB  1 
ATOM 1235 O OG1 . THR A 1 166 ? 21.470  -27.942 -36.649  1.000 198.825 ? 169 THR HHH OG1 1 
ATOM 1236 C CG2 . THR A 1 166 ? 20.101  -28.830 -38.468  1.000 203.167 ? 169 THR HHH CG2 1 
ATOM 1237 N N   . PHE A 1 167 ? 18.338  -31.254 -36.816  1.000 171.622 ? 170 PHE HHH N   1 
ATOM 1238 C CA  . PHE A 1 167 ? 17.599  -32.494 -37.141  1.000 170.022 ? 170 PHE HHH CA  1 
ATOM 1239 C C   . PHE A 1 167 ? 17.430  -32.634 -38.641  1.000 163.244 ? 170 PHE HHH C   1 
ATOM 1240 O O   . PHE A 1 167 ? 17.288  -31.628 -39.313  1.000 158.945 ? 170 PHE HHH O   1 
ATOM 1241 C CB  . PHE A 1 167 ? 16.264  -32.529 -36.412  1.000 175.398 ? 170 PHE HHH CB  1 
ATOM 1242 C CG  . PHE A 1 167 ? 16.488  -32.945 -34.994  1.000 183.089 ? 170 PHE HHH CG  1 
ATOM 1243 C CD1 . PHE A 1 167 ? 16.742  -31.990 -34.025  1.000 196.443 ? 170 PHE HHH CD1 1 
ATOM 1244 C CD2 . PHE A 1 167 ? 16.577  -34.285 -34.666  1.000 184.762 ? 170 PHE HHH CD2 1 
ATOM 1245 C CE1 . PHE A 1 167 ? 16.987  -32.366 -32.713  1.000 203.395 ? 170 PHE HHH CE1 1 
ATOM 1246 C CE2 . PHE A 1 167 ? 16.818  -34.665 -33.354  1.000 202.226 ? 170 PHE HHH CE2 1 
ATOM 1247 C CZ  . PHE A 1 167 ? 17.017  -33.706 -32.377  1.000 207.193 ? 170 PHE HHH CZ  1 
ATOM 1248 N N   . PRO A 1 168 ? 17.454  -33.879 -39.176  1.000 164.885 ? 171 PRO HHH N   1 
ATOM 1249 C CA  . PRO A 1 168 ? 17.032  -34.184 -40.535  1.000 167.636 ? 171 PRO HHH CA  1 
ATOM 1250 C C   . PRO A 1 168 ? 15.613  -33.721 -40.781  1.000 159.562 ? 171 PRO HHH C   1 
ATOM 1251 O O   . PRO A 1 168 ? 14.780  -34.090 -40.001  1.000 144.916 ? 171 PRO HHH O   1 
ATOM 1252 C CB  . PRO A 1 168 ? 16.995  -35.710 -40.597  1.000 174.823 ? 171 PRO HHH CB  1 
ATOM 1253 C CG  . PRO A 1 168 ? 18.107  -36.076 -39.651  1.000 179.854 ? 171 PRO HHH CG  1 
ATOM 1254 C CD  . PRO A 1 168 ? 17.906  -35.102 -38.507  1.000 176.400 ? 171 PRO HHH CD  1 
ATOM 1255 N N   . ALA A 1 169 ? 15.456  -32.921 -41.835  1.000 165.098 ? 172 ALA HHH N   1 
ATOM 1256 C CA  . ALA A 1 169 ? 14.176  -32.341 -42.270  1.000 170.297 ? 172 ALA HHH CA  1 
ATOM 1257 C C   . ALA A 1 169 ? 13.234  -33.494 -42.566  1.000 170.563 ? 172 ALA HHH C   1 
ATOM 1258 O O   . ALA A 1 169 ? 13.663  -34.601 -42.939  1.000 173.745 ? 172 ALA HHH O   1 
ATOM 1259 C CB  . ALA A 1 169 ? 14.325  -31.437 -43.466  1.000 172.875 ? 172 ALA HHH CB  1 
ATOM 1260 N N   . VAL A 1 170 ? 11.981  -33.227 -42.302  1.000 173.163 ? 173 VAL HHH N   1 
ATOM 1261 C CA  . VAL A 1 170 ? 10.879  -34.177 -42.536  1.000 180.563 ? 173 VAL HHH CA  1 
ATOM 1262 C C   . VAL A 1 170 ? 9.923   -33.382 -43.405  1.000 171.938 ? 173 VAL HHH C   1 
ATOM 1263 O O   . VAL A 1 170 ? 9.554   -32.259 -43.026  1.000 174.243 ? 173 VAL HHH O   1 
ATOM 1264 C CB  . VAL A 1 170 ? 10.268  -34.683 -41.207  1.000 195.611 ? 173 VAL HHH CB  1 
ATOM 1265 C CG1 . VAL A 1 170 ? 11.136  -35.766 -40.572  1.000 196.737 ? 173 VAL HHH CG1 1 
ATOM 1266 C CG2 . VAL A 1 170 ? 10.016  -33.560 -40.199  1.000 196.693 ? 173 VAL HHH CG2 1 
ATOM 1267 N N   . LEU A 1 171 ? 9.637   -33.880 -44.590  1.000 172.323 ? 174 LEU HHH N   1 
ATOM 1268 C CA  . LEU A 1 171 ? 8.633   -33.212 -45.453  1.000 188.433 ? 174 LEU HHH CA  1 
ATOM 1269 C C   . LEU A 1 171 ? 7.249   -33.411 -44.822  1.000 181.298 ? 174 LEU HHH C   1 
ATOM 1270 O O   . LEU A 1 171 ? 6.816   -34.571 -44.670  1.000 166.787 ? 174 LEU HHH O   1 
ATOM 1271 C CB  . LEU A 1 171 ? 8.687   -33.774 -46.877  1.000 197.188 ? 174 LEU HHH CB  1 
ATOM 1272 C CG  . LEU A 1 171 ? 7.781   -33.067 -47.882  1.000 194.934 ? 174 LEU HHH CG  1 
ATOM 1273 C CD1 . LEU A 1 171 ? 8.529   -31.919 -48.538  1.000 192.495 ? 174 LEU HHH CD1 1 
ATOM 1274 C CD2 . LEU A 1 171 ? 7.256   -34.038 -48.927  1.000 197.921 ? 174 LEU HHH CD2 1 
ATOM 1275 N N   . GLN A 1 172 ? 6.587   -32.308 -44.472  1.000 181.768 ? 175 GLN HHH N   1 
ATOM 1276 C CA  . GLN A 1 172 ? 5.236   -32.320 -43.865  1.000 188.553 ? 175 GLN HHH CA  1 
ATOM 1277 C C   . GLN A 1 172 ? 4.193   -32.671 -44.927  1.000 188.711 ? 175 GLN HHH C   1 
ATOM 1278 O O   . GLN A 1 172 ? 4.543   -32.737 -46.111  1.000 204.121 ? 175 GLN HHH O   1 
ATOM 1279 C CB  . GLN A 1 172 ? 4.928   -30.958 -43.258  1.000 196.901 ? 175 GLN HHH CB  1 
ATOM 1280 C CG  . GLN A 1 172 ? 5.958   -30.524 -42.229  1.000 206.695 ? 175 GLN HHH CG  1 
ATOM 1281 C CD  . GLN A 1 172 ? 5.877   -29.044 -41.973  1.000 213.324 ? 175 GLN HHH CD  1 
ATOM 1282 O OE1 . GLN A 1 172 ? 5.669   -28.263 -42.896  1.000 222.681 ? 175 GLN HHH OE1 1 
ATOM 1283 N NE2 . GLN A 1 172 ? 6.028   -28.655 -40.715  1.000 213.061 ? 175 GLN HHH NE2 1 
ATOM 1284 N N   . SER A 1 173 ? 2.954   -32.899 -44.501  1.000 187.249 ? 176 SER HHH N   1 
ATOM 1285 C CA  . SER A 1 173 ? 1.766   -33.030 -45.377  1.000 190.989 ? 176 SER HHH CA  1 
ATOM 1286 C C   . SER A 1 173 ? 1.625   -31.737 -46.182  1.000 199.342 ? 176 SER HHH C   1 
ATOM 1287 O O   . SER A 1 173 ? 0.941   -31.770 -47.209  1.000 214.024 ? 176 SER HHH O   1 
ATOM 1288 C CB  . SER A 1 173 ? 0.531   -33.320 -44.558  1.000 197.740 ? 176 SER HHH CB  1 
ATOM 1289 O OG  . SER A 1 173 ? -0.645  -33.367 -45.358  1.000 203.842 ? 176 SER HHH OG  1 
ATOM 1290 N N   . SER A 1 174 ? 2.248   -30.643 -45.722  1.000 202.817 ? 177 SER HHH N   1 
ATOM 1291 C CA  . SER A 1 174 ? 2.259   -29.304 -46.377  1.000 203.664 ? 177 SER HHH CA  1 
ATOM 1292 C C   . SER A 1 174 ? 2.943   -29.372 -47.754  1.000 200.700 ? 177 SER HHH C   1 
ATOM 1293 O O   . SER A 1 174 ? 2.653   -28.510 -48.590  1.000 203.192 ? 177 SER HHH O   1 
ATOM 1294 C CB  . SER A 1 174 ? 2.917   -28.270 -45.487  1.000 200.820 ? 177 SER HHH CB  1 
ATOM 1295 O OG  . SER A 1 174 ? 2.935   -26.993 -46.104  1.000 193.374 ? 177 SER HHH OG  1 
ATOM 1296 N N   . GLY A 1 175 ? 3.784   -30.374 -48.004  1.000 193.105 ? 178 GLY HHH N   1 
ATOM 1297 C CA  . GLY A 1 175 ? 4.590   -30.445 -49.231  1.000 195.290 ? 178 GLY HHH CA  1 
ATOM 1298 C C   . GLY A 1 175 ? 5.743   -29.475 -49.104  1.000 210.001 ? 178 GLY HHH C   1 
ATOM 1299 O O   . GLY A 1 175 ? 6.432   -29.216 -50.113  1.000 239.102 ? 178 GLY HHH O   1 
ATOM 1300 N N   . LEU A 1 176 ? 5.929   -28.951 -47.892  1.000 214.012 ? 179 LEU HHH N   1 
ATOM 1301 C CA  . LEU A 1 176 ? 7.072   -28.097 -47.503  1.000 215.979 ? 179 LEU HHH CA  1 
ATOM 1302 C C   . LEU A 1 176 ? 7.857   -28.839 -46.429  1.000 214.365 ? 179 LEU HHH C   1 
ATOM 1303 O O   . LEU A 1 176 ? 7.251   -29.657 -45.697  1.000 205.472 ? 179 LEU HHH O   1 
ATOM 1304 C CB  . LEU A 1 176 ? 6.545   -26.757 -46.992  1.000 218.316 ? 179 LEU HHH CB  1 
ATOM 1305 C CG  . LEU A 1 176 ? 5.738   -25.961 -48.008  1.000 216.816 ? 179 LEU HHH CG  1 
ATOM 1306 C CD1 . LEU A 1 176 ? 5.234   -24.660 -47.400  1.000 215.787 ? 179 LEU HHH CD1 1 
ATOM 1307 C CD2 . LEU A 1 176 ? 6.573   -25.711 -49.257  1.000 221.258 ? 179 LEU HHH CD2 1 
ATOM 1308 N N   . TYR A 1 177 ? 9.161   -28.581 -46.385  1.000 212.598 ? 180 TYR HHH N   1 
ATOM 1309 C CA  . TYR A 1 177 ? 10.091  -29.202 -45.419  1.000 210.532 ? 180 TYR HHH CA  1 
ATOM 1310 C C   . TYR A 1 177 ? 9.934   -28.479 -44.079  1.000 204.519 ? 180 TYR HHH C   1 
ATOM 1311 O O   . TYR A 1 177 ? 9.440   -27.339 -44.036  1.000 201.397 ? 180 TYR HHH O   1 
ATOM 1312 C CB  . TYR A 1 177 ? 11.514  -29.190 -45.977  1.000 202.580 ? 180 TYR HHH CB  1 
ATOM 1313 C CG  . TYR A 1 177 ? 11.821  -30.272 -46.981  1.000 207.582 ? 180 TYR HHH CG  1 
ATOM 1314 C CD1 . TYR A 1 177 ? 12.051  -29.959 -48.307  1.000 216.481 ? 180 TYR HHH CD1 1 
ATOM 1315 C CD2 . TYR A 1 177 ? 11.914  -31.607 -46.614  1.000 214.328 ? 180 TYR HHH CD2 1 
ATOM 1316 C CE1 . TYR A 1 177 ? 12.375  -30.930 -49.243  1.000 219.488 ? 180 TYR HHH CE1 1 
ATOM 1317 C CE2 . TYR A 1 177 ? 12.229  -32.594 -47.538  1.000 212.717 ? 180 TYR HHH CE2 1 
ATOM 1318 C CZ  . TYR A 1 177 ? 12.475  -32.250 -48.856  1.000 214.694 ? 180 TYR HHH CZ  1 
ATOM 1319 O OH  . TYR A 1 177 ? 12.795  -33.180 -49.797  1.000 218.527 ? 180 TYR HHH OH  1 
ATOM 1320 N N   . SER A 1 178 ? 10.321  -29.155 -43.001  1.000 199.583 ? 181 SER HHH N   1 
ATOM 1321 C CA  . SER A 1 178 ? 10.539  -28.531 -41.675  1.000 196.697 ? 181 SER HHH CA  1 
ATOM 1322 C C   . SER A 1 178 ? 11.609  -29.312 -40.918  1.000 184.534 ? 181 SER HHH C   1 
ATOM 1323 O O   . SER A 1 178 ? 11.623  -30.542 -41.052  1.000 175.654 ? 181 SER HHH O   1 
ATOM 1324 C CB  . SER A 1 178 ? 9.261   -28.454 -40.910  1.000 198.212 ? 181 SER HHH CB  1 
ATOM 1325 O OG  . SER A 1 178 ? 9.516   -28.376 -39.519  1.000 204.400 ? 181 SER HHH OG  1 
ATOM 1326 N N   . LEU A 1 179 ? 12.443  -28.603 -40.150  1.000 183.381 ? 182 LEU HHH N   1 
ATOM 1327 C CA  . LEU A 1 179 ? 13.389  -29.207 -39.169  1.000 191.351 ? 182 LEU HHH CA  1 
ATOM 1328 C C   . LEU A 1 179 ? 13.633  -28.270 -37.970  1.000 191.614 ? 182 LEU HHH C   1 
ATOM 1329 O O   . LEU A 1 179 ? 13.380  -27.037 -38.071  1.000 193.600 ? 182 LEU HHH O   1 
ATOM 1330 C CB  . LEU A 1 179 ? 14.696  -29.559 -39.881  1.000 185.653 ? 182 LEU HHH CB  1 
ATOM 1331 C CG  . LEU A 1 179 ? 15.533  -28.393 -40.398  1.000 189.698 ? 182 LEU HHH CG  1 
ATOM 1332 C CD1 . LEU A 1 179 ? 16.437  -27.817 -39.307  1.000 190.147 ? 182 LEU HHH CD1 1 
ATOM 1333 C CD2 . LEU A 1 179 ? 16.368  -28.857 -41.581  1.000 196.303 ? 182 LEU HHH CD2 1 
ATOM 1334 N N   . SER A 1 180 ? 14.112  -28.846 -36.863  1.000 185.545 ? 183 SER HHH N   1 
ATOM 1335 C CA  . SER A 1 180 ? 14.511  -28.116 -35.636  1.000 179.604 ? 183 SER HHH CA  1 
ATOM 1336 C C   . SER A 1 180 ? 16.036  -28.119 -35.562  1.000 183.619 ? 183 SER HHH C   1 
ATOM 1337 O O   . SER A 1 180 ? 16.649  -29.083 -36.094  1.000 184.974 ? 183 SER HHH O   1 
ATOM 1338 C CB  . SER A 1 180 ? 13.887  -28.774 -34.456  1.000 176.667 ? 183 SER HHH CB  1 
ATOM 1339 O OG  . SER A 1 180 ? 12.735  -29.512 -34.863  1.000 171.629 ? 183 SER HHH OG  1 
ATOM 1340 N N   . SER A 1 181 ? 16.634  -27.077 -34.994  1.000 183.872 ? 184 SER HHH N   1 
ATOM 1341 C CA  . SER A 1 181 ? 18.083  -27.083 -34.681  1.000 187.010 ? 184 SER HHH CA  1 
ATOM 1342 C C   . SER A 1 181 ? 18.254  -26.648 -33.239  1.000 188.196 ? 184 SER HHH C   1 
ATOM 1343 O O   . SER A 1 181 ? 17.879  -25.518 -32.937  1.000 193.721 ? 184 SER HHH O   1 
ATOM 1344 C CB  . SER A 1 181 ? 18.880  -26.207 -35.585  1.000 189.949 ? 184 SER HHH CB  1 
ATOM 1345 O OG  . SER A 1 181 ? 20.248  -26.243 -35.188  1.000 197.781 ? 184 SER HHH OG  1 
ATOM 1346 N N   . VAL A 1 182 ? 18.809  -27.519 -32.407  1.000 179.994 ? 185 VAL HHH N   1 
ATOM 1347 C CA  . VAL A 1 182 ? 18.862  -27.304 -30.941  1.000 174.431 ? 185 VAL HHH CA  1 
ATOM 1348 C C   . VAL A 1 182 ? 20.329  -27.342 -30.510  1.000 177.270 ? 185 VAL HHH C   1 
ATOM 1349 O O   . VAL A 1 182 ? 21.162  -27.909 -31.251  1.000 170.349 ? 185 VAL HHH O   1 
ATOM 1350 C CB  . VAL A 1 182 ? 17.986  -28.361 -30.256  1.000 171.496 ? 185 VAL HHH CB  1 
ATOM 1351 C CG1 . VAL A 1 182 ? 16.568  -28.359 -30.818  1.000 165.745 ? 185 VAL HHH CG1 1 
ATOM 1352 C CG2 . VAL A 1 182 ? 18.590  -29.749 -30.383  1.000 173.986 ? 185 VAL HHH CG2 1 
ATOM 1353 N N   . VAL A 1 183 ? 20.633  -26.737 -29.366  1.000 185.320 ? 186 VAL HHH N   1 
ATOM 1354 C CA  . VAL A 1 183 ? 21.985  -26.791 -28.740  1.000 192.669 ? 186 VAL HHH CA  1 
ATOM 1355 C C   . VAL A 1 183 ? 21.793  -26.718 -27.228  1.000 191.385 ? 186 VAL HHH C   1 
ATOM 1356 O O   . VAL A 1 183 ? 20.872  -26.015 -26.776  1.000 187.584 ? 186 VAL HHH O   1 
ATOM 1357 C CB  . VAL A 1 183 ? 22.908  -25.671 -29.263  1.000 193.253 ? 186 VAL HHH CB  1 
ATOM 1358 C CG1 . VAL A 1 183 ? 22.260  -24.306 -29.122  1.000 203.337 ? 186 VAL HHH CG1 1 
ATOM 1359 C CG2 . VAL A 1 183 ? 24.260  -25.675 -28.575  1.000 191.777 ? 186 VAL HHH CG2 1 
ATOM 1360 N N   . THR A 1 184 ? 22.648  -27.423 -26.495  1.000 194.567 ? 187 THR HHH N   1 
ATOM 1361 C CA  . THR A 1 184 ? 22.597  -27.543 -25.021  1.000 200.463 ? 187 THR HHH CA  1 
ATOM 1362 C C   . THR A 1 184 ? 23.740  -26.705 -24.445  1.000 199.027 ? 187 THR HHH C   1 
ATOM 1363 O O   . THR A 1 184 ? 24.872  -26.865 -24.918  1.000 200.961 ? 187 THR HHH O   1 
ATOM 1364 C CB  . THR A 1 184 ? 22.630  -29.030 -24.665  1.000 207.424 ? 187 THR HHH CB  1 
ATOM 1365 O OG1 . THR A 1 184 ? 23.947  -29.496 -24.947  1.000 208.390 ? 187 THR HHH OG1 1 
ATOM 1366 C CG2 . THR A 1 184 ? 21.631  -29.843 -25.459  1.000 207.849 ? 187 THR HHH CG2 1 
ATOM 1367 N N   . VAL A 1 185 ? 23.452  -25.813 -23.505  1.000 201.003 ? 188 VAL HHH N   1 
ATOM 1368 C CA  . VAL A 1 185 ? 24.467  -24.887 -22.931  1.000 212.693 ? 188 VAL HHH CA  1 
ATOM 1369 C C   . VAL A 1 185 ? 24.265  -24.839 -21.427  1.000 223.728 ? 188 VAL HHH C   1 
ATOM 1370 O O   . VAL A 1 185 ? 23.151  -25.062 -20.967  1.000 236.435 ? 188 VAL HHH O   1 
ATOM 1371 C CB  . VAL A 1 185 ? 24.348  -23.488 -23.554  1.000 218.481 ? 188 VAL HHH CB  1 
ATOM 1372 C CG1 . VAL A 1 185 ? 24.501  -23.530 -25.064  1.000 218.817 ? 188 VAL HHH CG1 1 
ATOM 1373 C CG2 . VAL A 1 185 ? 23.042  -22.814 -23.188  1.000 219.237 ? 188 VAL HHH CG2 1 
ATOM 1374 N N   . PRO A 1 186 ? 25.322  -24.558 -20.630  1.000 233.316 ? 189 PRO HHH N   1 
ATOM 1375 C CA  . PRO A 1 186 ? 25.184  -24.435 -19.175  1.000 244.642 ? 189 PRO HHH CA  1 
ATOM 1376 C C   . PRO A 1 186 ? 24.169  -23.349 -18.788  1.000 245.313 ? 189 PRO HHH C   1 
ATOM 1377 O O   . PRO A 1 186 ? 24.264  -22.284 -19.363  1.000 240.962 ? 189 PRO HHH O   1 
ATOM 1378 C CB  . PRO A 1 186 ? 26.581  -24.024 -18.684  1.000 246.255 ? 189 PRO HHH CB  1 
ATOM 1379 C CG  . PRO A 1 186 ? 27.524  -24.366 -19.824  1.000 241.361 ? 189 PRO HHH CG  1 
ATOM 1380 C CD  . PRO A 1 186 ? 26.700  -24.351 -21.093  1.000 232.417 ? 189 PRO HHH CD  1 
ATOM 1381 N N   . SER A 1 187 ? 23.264  -23.623 -17.837  1.000 244.315 ? 190 SER HHH N   1 
ATOM 1382 C CA  . SER A 1 187 ? 22.216  -22.663 -17.391  1.000 249.189 ? 190 SER HHH CA  1 
ATOM 1383 C C   . SER A 1 187 ? 22.897  -21.352 -16.975  1.000 247.475 ? 190 SER HHH C   1 
ATOM 1384 O O   . SER A 1 187 ? 22.231  -20.299 -17.016  1.000 244.925 ? 190 SER HHH O   1 
ATOM 1385 C CB  . SER A 1 187 ? 21.342  -23.228 -16.288  1.000 256.123 ? 190 SER HHH CB  1 
ATOM 1386 O OG  . SER A 1 187 ? 20.730  -24.444 -16.703  1.000 264.769 ? 190 SER HHH OG  1 
ATOM 1387 N N   . SER A 1 188 ? 24.181  -21.435 -16.603  1.000 249.967 ? 191 SER HHH N   1 
ATOM 1388 C CA  . SER A 1 188 ? 25.089  -20.291 -16.320  1.000 255.056 ? 191 SER HHH CA  1 
ATOM 1389 C C   . SER A 1 188 ? 25.004  -19.264 -17.448  1.000 253.723 ? 191 SER HHH C   1 
ATOM 1390 O O   . SER A 1 188 ? 24.763  -18.079 -17.144  1.000 264.718 ? 191 SER HHH O   1 
ATOM 1391 C CB  . SER A 1 188 ? 26.522  -20.741 -16.158  1.000 258.308 ? 191 SER HHH CB  1 
ATOM 1392 O OG  . SER A 1 188 ? 26.617  -21.915 -15.369  1.000 262.567 ? 191 SER HHH OG  1 
ATOM 1393 N N   . SER A 1 189 ? 25.199  -19.719 -18.691  1.000 240.967 ? 192 SER HHH N   1 
ATOM 1394 C CA  . SER A 1 189 ? 25.517  -18.873 -19.872  1.000 228.686 ? 192 SER HHH CA  1 
ATOM 1395 C C   . SER A 1 189 ? 24.249  -18.295 -20.518  1.000 233.024 ? 192 SER HHH C   1 
ATOM 1396 O O   . SER A 1 189 ? 24.396  -17.333 -21.270  1.000 227.498 ? 192 SER HHH O   1 
ATOM 1397 C CB  . SER A 1 189 ? 26.320  -19.654 -20.862  1.000 215.529 ? 192 SER HHH CB  1 
ATOM 1398 O OG  . SER A 1 189 ? 25.662  -20.867 -21.174  1.000 197.812 ? 192 SER HHH OG  1 
ATOM 1399 N N   . LEU A 1 190 ? 23.059  -18.837 -20.221  1.000 244.224 ? 193 LEU HHH N   1 
ATOM 1400 C CA  . LEU A 1 190 ? 21.763  -18.446 -20.851  1.000 247.493 ? 193 LEU HHH CA  1 
ATOM 1401 C C   . LEU A 1 190 ? 21.521  -16.936 -20.732  1.000 251.347 ? 193 LEU HHH C   1 
ATOM 1402 O O   . LEU A 1 190 ? 20.846  -16.408 -21.632  1.000 252.195 ? 193 LEU HHH O   1 
ATOM 1403 C CB  . LEU A 1 190 ? 20.609  -19.199 -20.174  1.000 256.837 ? 193 LEU HHH CB  1 
ATOM 1404 C CG  . LEU A 1 190 ? 20.520  -20.706 -20.424  1.000 261.851 ? 193 LEU HHH CG  1 
ATOM 1405 C CD1 . LEU A 1 190 ? 19.231  -21.285 -19.844  1.000 269.092 ? 193 LEU HHH CD1 1 
ATOM 1406 C CD2 . LEU A 1 190 ? 20.595  -21.016 -21.907  1.000 259.956 ? 193 LEU HHH CD2 1 
ATOM 1407 N N   . GLY A 1 191 ? 21.971  -16.306 -19.632  1.000 260.060 ? 194 GLY HHH N   1 
ATOM 1408 C CA  . GLY A 1 191 ? 21.695  -14.900 -19.258  1.000 260.093 ? 194 GLY HHH CA  1 
ATOM 1409 C C   . GLY A 1 191 ? 22.911  -14.001 -19.424  1.000 259.572 ? 194 GLY HHH C   1 
ATOM 1410 O O   . GLY A 1 191 ? 22.803  -12.798 -19.087  1.000 256.945 ? 194 GLY HHH O   1 
ATOM 1411 N N   . THR A 1 192 ? 24.023  -14.550 -19.928  1.000 254.788 ? 195 THR HHH N   1 
ATOM 1412 C CA  . THR A 1 192 ? 25.304  -13.832 -20.167  1.000 257.493 ? 195 THR HHH CA  1 
ATOM 1413 C C   . THR A 1 192 ? 25.554  -13.724 -21.670  1.000 253.573 ? 195 THR HHH C   1 
ATOM 1414 O O   . THR A 1 192 ? 25.482  -12.610 -22.213  1.000 248.230 ? 195 THR HHH O   1 
ATOM 1415 C CB  . THR A 1 192 ? 26.485  -14.548 -19.503  1.000 257.114 ? 195 THR HHH CB  1 
ATOM 1416 O OG1 . THR A 1 192 ? 26.261  -14.457 -18.098  1.000 266.135 ? 195 THR HHH OG1 1 
ATOM 1417 C CG2 . THR A 1 192 ? 27.830  -13.955 -19.868  1.000 256.877 ? 195 THR HHH CG2 1 
ATOM 1418 N N   . GLN A 1 193 ? 25.857  -14.857 -22.302  1.000 251.385 ? 196 GLN HHH N   1 
ATOM 1419 C CA  . GLN A 1 193 ? 26.100  -14.951 -23.758  1.000 244.902 ? 196 GLN HHH CA  1 
ATOM 1420 C C   . GLN A 1 193 ? 24.758  -15.140 -24.477  1.000 248.890 ? 196 GLN HHH C   1 
ATOM 1421 O O   . GLN A 1 193 ? 23.931  -15.947 -24.023  1.000 243.213 ? 196 GLN HHH O   1 
ATOM 1422 C CB  . GLN A 1 193 ? 27.055  -16.100 -24.065  1.000 236.287 ? 196 GLN HHH CB  1 
ATOM 1423 C CG  . GLN A 1 193 ? 27.298  -16.260 -25.555  1.000 233.666 ? 196 GLN HHH CG  1 
ATOM 1424 C CD  . GLN A 1 193 ? 28.261  -17.371 -25.869  1.000 233.096 ? 196 GLN HHH CD  1 
ATOM 1425 O OE1 . GLN A 1 193 ? 28.888  -17.938 -24.978  1.000 227.985 ? 196 GLN HHH OE1 1 
ATOM 1426 N NE2 . GLN A 1 193 ? 28.373  -17.687 -27.151  1.000 238.480 ? 196 GLN HHH NE2 1 
ATOM 1427 N N   . THR A 1 194 ? 24.554  -14.410 -25.570  1.000 253.862 ? 197 THR HHH N   1 
ATOM 1428 C CA  . THR A 1 194 ? 23.363  -14.528 -26.446  1.000 244.352 ? 197 THR HHH CA  1 
ATOM 1429 C C   . THR A 1 194 ? 23.692  -15.560 -27.538  1.000 237.277 ? 197 THR HHH C   1 
ATOM 1430 O O   . THR A 1 194 ? 24.862  -15.619 -27.987  1.000 221.656 ? 197 THR HHH O   1 
ATOM 1431 C CB  . THR A 1 194 ? 22.934  -13.138 -26.934  1.000 246.264 ? 197 THR HHH CB  1 
ATOM 1432 O OG1 . THR A 1 194 ? 21.591  -13.262 -27.397  1.000 233.364 ? 197 THR HHH OG1 1 
ATOM 1433 C CG2 . THR A 1 194 ? 23.833  -12.573 -28.014  1.000 251.274 ? 197 THR HHH CG2 1 
ATOM 1434 N N   . TYR A 1 195 ? 22.702  -16.368 -27.918  1.000 234.840 ? 198 TYR HHH N   1 
ATOM 1435 C CA  . TYR A 1 195 ? 22.814  -17.455 -28.927  1.000 225.767 ? 198 TYR HHH CA  1 
ATOM 1436 C C   . TYR A 1 195 ? 21.912  -17.122 -30.115  1.000 217.776 ? 198 TYR HHH C   1 
ATOM 1437 O O   . TYR A 1 195 ? 20.674  -16.998 -29.986  1.000 220.065 ? 198 TYR HHH O   1 
ATOM 1438 C CB  . TYR A 1 195 ? 22.451  -18.810 -28.322  1.000 224.641 ? 198 TYR HHH CB  1 
ATOM 1439 C CG  . TYR A 1 195 ? 23.290  -19.200 -27.134  1.000 224.706 ? 198 TYR HHH CG  1 
ATOM 1440 C CD1 . TYR A 1 195 ? 24.509  -19.826 -27.312  1.000 221.606 ? 198 TYR HHH CD1 1 
ATOM 1441 C CD2 . TYR A 1 195 ? 22.871  -18.942 -25.835  1.000 225.160 ? 198 TYR HHH CD2 1 
ATOM 1442 C CE1 . TYR A 1 195 ? 25.286  -20.200 -26.229  1.000 221.643 ? 198 TYR HHH CE1 1 
ATOM 1443 C CE2 . TYR A 1 195 ? 23.642  -19.292 -24.741  1.000 221.675 ? 198 TYR HHH CE2 1 
ATOM 1444 C CZ  . TYR A 1 195 ? 24.857  -19.914 -24.945  1.000 223.337 ? 198 TYR HHH CZ  1 
ATOM 1445 O OH  . TYR A 1 195 ? 25.601  -20.273 -23.868  1.000 225.042 ? 198 TYR HHH OH  1 
ATOM 1446 N N   . ILE A 1 196 ? 22.537  -16.933 -31.264  1.000 205.251 ? 199 ILE HHH N   1 
ATOM 1447 C CA  . ILE A 1 196 ? 21.817  -16.540 -32.500  1.000 205.058 ? 199 ILE HHH CA  1 
ATOM 1448 C C   . ILE A 1 196 ? 22.063  -17.638 -33.516  1.000 212.316 ? 199 ILE HHH C   1 
ATOM 1449 O O   . ILE A 1 196 ? 23.246  -17.958 -33.739  1.000 211.294 ? 199 ILE HHH O   1 
ATOM 1450 C CB  . ILE A 1 196 ? 22.308  -15.177 -33.001  1.000 202.886 ? 199 ILE HHH CB  1 
ATOM 1451 C CG1 . ILE A 1 196 ? 22.384  -14.171 -31.846  1.000 199.932 ? 199 ILE HHH CG1 1 
ATOM 1452 C CG2 . ILE A 1 196 ? 21.430  -14.724 -34.161  1.000 205.243 ? 199 ILE HHH CG2 1 
ATOM 1453 C CD1 . ILE A 1 196 ? 23.205  -12.933 -32.104  1.000 201.325 ? 199 ILE HHH CD1 1 
ATOM 1454 N N   . CYS A 1 197 ? 20.988  -18.193 -34.075  1.000 220.062 ? 200 CYS HHH N   1 
ATOM 1455 C CA  . CYS A 1 197 ? 21.062  -19.210 -35.152  1.000 218.295 ? 200 CYS HHH CA  1 
ATOM 1456 C C   . CYS A 1 197 ? 21.018  -18.485 -36.491  1.000 206.180 ? 200 CYS HHH C   1 
ATOM 1457 O O   . CYS A 1 197 ? 20.199  -17.560 -36.641  1.000 195.524 ? 200 CYS HHH O   1 
ATOM 1458 C CB  . CYS A 1 197 ? 19.975  -20.267 -35.012  1.000 225.789 ? 200 CYS HHH CB  1 
ATOM 1459 S SG  . CYS A 1 197 ? 18.471  -19.955 -35.968  1.000 239.040 ? 200 CYS HHH SG  1 
ATOM 1460 N N   . ASN A 1 198 ? 21.919  -18.881 -37.383  1.000 202.851 ? 201 ASN HHH N   1 
ATOM 1461 C CA  . ASN A 1 198 ? 22.104  -18.281 -38.724  1.000 206.351 ? 201 ASN HHH CA  1 
ATOM 1462 C C   . ASN A 1 198 ? 21.658  -19.340 -39.730  1.000 198.797 ? 201 ASN HHH C   1 
ATOM 1463 O O   . ASN A 1 198 ? 22.393  -20.325 -39.882  1.000 193.483 ? 201 ASN HHH O   1 
ATOM 1464 C CB  . ASN A 1 198 ? 23.560  -17.844 -38.925  1.000 209.313 ? 201 ASN HHH CB  1 
ATOM 1465 C CG  . ASN A 1 198 ? 24.145  -17.216 -37.677  1.000 210.898 ? 201 ASN HHH CG  1 
ATOM 1466 O OD1 . ASN A 1 198 ? 24.836  -17.901 -36.933  1.000 204.898 ? 201 ASN HHH OD1 1 
ATOM 1467 N ND2 . ASN A 1 198 ? 23.854  -15.949 -37.410  1.000 212.218 ? 201 ASN HHH ND2 1 
ATOM 1468 N N   . VAL A 1 199 ? 20.479  -19.182 -40.338  1.000 198.177 ? 202 VAL HHH N   1 
ATOM 1469 C CA  . VAL A 1 199 ? 19.925  -20.188 -41.293  1.000 202.779 ? 202 VAL HHH CA  1 
ATOM 1470 C C   . VAL A 1 199 ? 20.055  -19.643 -42.719  1.000 197.466 ? 202 VAL HHH C   1 
ATOM 1471 O O   . VAL A 1 199 ? 19.683  -18.487 -42.940  1.000 192.273 ? 202 VAL HHH O   1 
ATOM 1472 C CB  . VAL A 1 199 ? 18.481  -20.601 -40.943  1.000 215.796 ? 202 VAL HHH CB  1 
ATOM 1473 C CG1 . VAL A 1 199 ? 18.360  -21.017 -39.483  1.000 222.114 ? 202 VAL HHH CG1 1 
ATOM 1474 C CG2 . VAL A 1 199 ? 17.451  -19.531 -41.268  1.000 221.835 ? 202 VAL HHH CG2 1 
ATOM 1475 N N   . ASN A 1 200 ? 20.610  -20.450 -43.625  1.000 194.625 ? 203 ASN HHH N   1 
ATOM 1476 C CA  . ASN A 1 200 ? 20.721  -20.142 -45.072  1.000 194.377 ? 203 ASN HHH CA  1 
ATOM 1477 C C   . ASN A 1 200 ? 19.811  -21.111 -45.819  1.000 189.019 ? 203 ASN HHH C   1 
ATOM 1478 O O   . ASN A 1 200 ? 19.979  -22.319 -45.646  1.000 178.049 ? 203 ASN HHH O   1 
ATOM 1479 C CB  . ASN A 1 200 ? 22.161  -20.249 -45.581  1.000 198.176 ? 203 ASN HHH CB  1 
ATOM 1480 C CG  . ASN A 1 200 ? 23.015  -19.049 -45.225  1.000 205.495 ? 203 ASN HHH CG  1 
ATOM 1481 O OD1 . ASN A 1 200 ? 22.745  -18.367 -44.240  1.000 210.958 ? 203 ASN HHH OD1 1 
ATOM 1482 N ND2 . ASN A 1 200 ? 24.041  -18.780 -46.021  1.000 205.920 ? 203 ASN HHH ND2 1 
ATOM 1483 N N   . HIS A 1 201 ? 18.873  -20.600 -46.607  1.000 195.910 ? 204 HIS HHH N   1 
ATOM 1484 C CA  . HIS A 1 201 ? 18.181  -21.398 -47.649  1.000 197.352 ? 204 HIS HHH CA  1 
ATOM 1485 C C   . HIS A 1 201 ? 18.570  -20.827 -49.011  1.000 214.140 ? 204 HIS HHH C   1 
ATOM 1486 O O   . HIS A 1 201 ? 17.998  -19.789 -49.382  1.000 216.621 ? 204 HIS HHH O   1 
ATOM 1487 C CB  . HIS A 1 201 ? 16.673  -21.397 -47.431  1.000 188.158 ? 204 HIS HHH CB  1 
ATOM 1488 C CG  . HIS A 1 201 ? 15.947  -22.297 -48.368  1.000 178.202 ? 204 HIS HHH CG  1 
ATOM 1489 N ND1 . HIS A 1 201 ? 14.940  -21.837 -49.202  1.000 174.215 ? 204 HIS HHH ND1 1 
ATOM 1490 C CD2 . HIS A 1 201 ? 16.051  -23.630 -48.585  1.000 169.878 ? 204 HIS HHH CD2 1 
ATOM 1491 C CE1 . HIS A 1 201 ? 14.444  -22.853 -49.891  1.000 171.976 ? 204 HIS HHH CE1 1 
ATOM 1492 N NE2 . HIS A 1 201 ? 15.118  -23.966 -49.535  1.000 170.618 ? 204 HIS HHH NE2 1 
ATOM 1493 N N   . LYS A 1 202 ? 19.532  -21.458 -49.695  1.000 221.292 ? 205 LYS HHH N   1 
ATOM 1494 C CA  . LYS A 1 202 ? 20.118  -20.930 -50.950  1.000 219.079 ? 205 LYS HHH CA  1 
ATOM 1495 C C   . LYS A 1 202 ? 19.096  -21.027 -52.088  1.000 221.743 ? 205 LYS HHH C   1 
ATOM 1496 O O   . LYS A 1 202 ? 18.978  -20.061 -52.830  1.000 240.497 ? 205 LYS HHH O   1 
ATOM 1497 C CB  . LYS A 1 202 ? 21.470  -21.579 -51.265  1.000 223.702 ? 205 LYS HHH CB  1 
ATOM 1498 C CG  . LYS A 1 202 ? 22.209  -20.932 -52.436  1.000 241.254 ? 205 LYS HHH CG  1 
ATOM 1499 C CD  . LYS A 1 202 ? 23.675  -20.562 -52.185  1.000 245.201 ? 205 LYS HHH CD  1 
ATOM 1500 C CE  . LYS A 1 202 ? 24.386  -19.989 -53.404  1.000 244.408 ? 205 LYS HHH CE  1 
ATOM 1501 N NZ  . LYS A 1 202 ? 25.237  -20.996 -54.089  1.000 242.039 ? 205 LYS HHH NZ  1 
ATOM 1502 N N   . PRO A 1 203 ? 18.320  -22.123 -52.314  1.000 211.635 ? 206 PRO HHH N   1 
ATOM 1503 C CA  . PRO A 1 203 ? 17.328  -22.126 -53.402  1.000 200.293 ? 206 PRO HHH CA  1 
ATOM 1504 C C   . PRO A 1 203 ? 16.323  -20.955 -53.440  1.000 195.257 ? 206 PRO HHH C   1 
ATOM 1505 O O   . PRO A 1 203 ? 15.916  -20.646 -54.514  1.000 193.501 ? 206 PRO HHH O   1 
ATOM 1506 C CB  . PRO A 1 203 ? 16.598  -23.471 -53.262  1.000 200.096 ? 206 PRO HHH CB  1 
ATOM 1507 C CG  . PRO A 1 203 ? 17.597  -24.367 -52.527  1.000 197.801 ? 206 PRO HHH CG  1 
ATOM 1508 C CD  . PRO A 1 203 ? 18.358  -23.419 -51.606  1.000 205.591 ? 206 PRO HHH CD  1 
ATOM 1509 N N   . SER A 1 204 ? 15.985  -20.296 -52.325  1.000 199.845 ? 207 SER HHH N   1 
ATOM 1510 C CA  . SER A 1 204 ? 15.169  -19.040 -52.289  1.000 208.308 ? 207 SER HHH CA  1 
ATOM 1511 C C   . SER A 1 204 ? 16.055  -17.823 -51.999  1.000 208.648 ? 207 SER HHH C   1 
ATOM 1512 O O   . SER A 1 204 ? 15.517  -16.700 -51.951  1.000 203.617 ? 207 SER HHH O   1 
ATOM 1513 C CB  . SER A 1 204 ? 14.082  -19.119 -51.263  1.000 209.868 ? 207 SER HHH CB  1 
ATOM 1514 O OG  . SER A 1 204 ? 14.635  -19.384 -49.981  1.000 206.265 ? 207 SER HHH OG  1 
ATOM 1515 N N   . ASN A 1 205 ? 17.346  -18.075 -51.766  1.000 213.163 ? 208 ASN HHH N   1 
ATOM 1516 C CA  . ASN A 1 205 ? 18.437  -17.097 -51.502  1.000 223.658 ? 208 ASN HHH CA  1 
ATOM 1517 C C   . ASN A 1 205 ? 18.032  -16.199 -50.326  1.000 226.601 ? 208 ASN HHH C   1 
ATOM 1518 O O   . ASN A 1 205 ? 18.273  -14.982 -50.397  1.000 232.696 ? 208 ASN HHH O   1 
ATOM 1519 C CB  . ASN A 1 205 ? 18.848  -16.363 -52.786  1.000 233.613 ? 208 ASN HHH CB  1 
ATOM 1520 C CG  . ASN A 1 205 ? 20.353  -16.202 -52.899  1.000 237.646 ? 208 ASN HHH CG  1 
ATOM 1521 O OD1 . ASN A 1 205 ? 20.984  -15.727 -51.961  1.000 249.518 ? 208 ASN HHH OD1 1 
ATOM 1522 N ND2 . ASN A 1 205 ? 20.945  -16.613 -54.015  1.000 232.800 ? 208 ASN HHH ND2 1 
ATOM 1523 N N   . THR A 1 206 ? 17.463  -16.799 -49.275  1.000 226.109 ? 209 THR HHH N   1 
ATOM 1524 C CA  . THR A 1 206 ? 17.087  -16.119 -48.009  1.000 229.725 ? 209 THR HHH CA  1 
ATOM 1525 C C   . THR A 1 206 ? 17.963  -16.668 -46.881  1.000 228.830 ? 209 THR HHH C   1 
ATOM 1526 O O   . THR A 1 206 ? 18.083  -17.899 -46.760  1.000 204.997 ? 209 THR HHH O   1 
ATOM 1527 C CB  . THR A 1 206 ? 15.593  -16.270 -47.703  1.000 228.358 ? 209 THR HHH CB  1 
ATOM 1528 O OG1 . THR A 1 206 ? 15.395  -17.507 -47.020  1.000 216.145 ? 209 THR HHH OG1 1 
ATOM 1529 C CG2 . THR A 1 206 ? 14.740  -16.201 -48.950  1.000 227.902 ? 209 THR HHH CG2 1 
ATOM 1530 N N   . LYS A 1 207 ? 18.567  -15.761 -46.114  1.000 241.723 ? 210 LYS HHH N   1 
ATOM 1531 C CA  . LYS A 1 207 ? 19.490  -16.071 -44.995  1.000 247.413 ? 210 LYS HHH CA  1 
ATOM 1532 C C   . LYS A 1 207 ? 19.014  -15.274 -43.776  1.000 251.267 ? 210 LYS HHH C   1 
ATOM 1533 O O   . LYS A 1 207 ? 19.139  -14.032 -43.797  1.000 252.404 ? 210 LYS HHH O   1 
ATOM 1534 C CB  . LYS A 1 207 ? 20.939  -15.751 -45.382  1.000 253.630 ? 210 LYS HHH CB  1 
ATOM 1535 C CG  . LYS A 1 207 ? 21.280  -15.861 -46.866  1.000 259.679 ? 210 LYS HHH CG  1 
ATOM 1536 C CD  . LYS A 1 207 ? 21.160  -14.530 -47.596  1.000 268.131 ? 210 LYS HHH CD  1 
ATOM 1537 C CE  . LYS A 1 207 ? 21.815  -14.501 -48.961  1.000 263.035 ? 210 LYS HHH CE  1 
ATOM 1538 N NZ  . LYS A 1 207 ? 21.645  -13.181 -49.618  1.000 261.370 ? 210 LYS HHH NZ  1 
ATOM 1539 N N   . VAL A 1 208 ? 18.469  -15.973 -42.774  1.000 243.820 ? 211 VAL HHH N   1 
ATOM 1540 C CA  . VAL A 1 208 ? 17.695  -15.404 -41.630  1.000 228.842 ? 211 VAL HHH CA  1 
ATOM 1541 C C   . VAL A 1 208 ? 18.477  -15.671 -40.337  1.000 224.471 ? 211 VAL HHH C   1 
ATOM 1542 O O   . VAL A 1 208 ? 19.033  -16.783 -40.221  1.000 222.139 ? 211 VAL HHH O   1 
ATOM 1543 C CB  . VAL A 1 208 ? 16.288  -16.030 -41.591  1.000 220.118 ? 211 VAL HHH CB  1 
ATOM 1544 C CG1 . VAL A 1 208 ? 15.396  -15.363 -40.556  1.000 224.530 ? 211 VAL HHH CG1 1 
ATOM 1545 C CG2 . VAL A 1 208 ? 15.624  -16.028 -42.965  1.000 216.430 ? 211 VAL HHH CG2 1 
ATOM 1546 N N   . ASP A 1 209 ? 18.528  -14.700 -39.412  1.000 227.081 ? 212 ASP HHH N   1 
ATOM 1547 C CA  . ASP A 1 209 ? 19.198  -14.847 -38.087  1.000 231.690 ? 212 ASP HHH CA  1 
ATOM 1548 C C   . ASP A 1 209 ? 18.243  -14.431 -36.954  1.000 231.611 ? 212 ASP HHH C   1 
ATOM 1549 O O   . ASP A 1 209 ? 18.082  -13.214 -36.699  1.000 223.873 ? 212 ASP HHH O   1 
ATOM 1550 C CB  . ASP A 1 209 ? 20.518  -14.071 -38.020  1.000 232.760 ? 212 ASP HHH CB  1 
ATOM 1551 C CG  . ASP A 1 209 ? 21.457  -14.281 -39.197  1.000 228.529 ? 212 ASP HHH CG  1 
ATOM 1552 O OD1 . ASP A 1 209 ? 22.257  -13.364 -39.455  1.000 231.675 ? 212 ASP HHH OD1 1 
ATOM 1553 O OD2 . ASP A 1 209 ? 21.401  -15.357 -39.833  1.000 220.641 ? 212 ASP HHH OD2 1 
ATOM 1554 N N   . LYS A 1 210 ? 17.652  -15.422 -36.282  1.000 232.878 ? 213 LYS HHH N   1 
ATOM 1555 C CA  . LYS A 1 210 ? 16.774  -15.220 -35.103  1.000 233.819 ? 213 LYS HHH CA  1 
ATOM 1556 C C   . LYS A 1 210 ? 17.583  -15.461 -33.828  1.000 234.342 ? 213 LYS HHH C   1 
ATOM 1557 O O   . LYS A 1 210 ? 18.283  -16.508 -33.729  1.000 228.402 ? 213 LYS HHH O   1 
ATOM 1558 C CB  . LYS A 1 210 ? 15.555  -16.144 -35.162  1.000 228.491 ? 213 LYS HHH CB  1 
ATOM 1559 C CG  . LYS A 1 210 ? 14.351  -15.604 -34.418  1.000 228.641 ? 213 LYS HHH CG  1 
ATOM 1560 C CD  . LYS A 1 210 ? 13.794  -14.349 -35.066  1.000 234.803 ? 213 LYS HHH CD  1 
ATOM 1561 C CE  . LYS A 1 210 ? 12.923  -14.600 -36.281  1.000 235.405 ? 213 LYS HHH CE  1 
ATOM 1562 N NZ  . LYS A 1 210 ? 11.484  -14.573 -35.923  1.000 237.303 ? 213 LYS HHH NZ  1 
ATOM 1563 N N   . LYS A 1 211 ? 17.538  -14.503 -32.902  1.000 233.064 ? 214 LYS HHH N   1 
ATOM 1564 C CA  . LYS A 1 211 ? 18.174  -14.688 -31.578  1.000 231.220 ? 214 LYS HHH CA  1 
ATOM 1565 C C   . LYS A 1 211 ? 17.148  -15.381 -30.706  1.000 228.198 ? 214 LYS HHH C   1 
ATOM 1566 O O   . LYS A 1 211 ? 15.950  -15.076 -30.836  1.000 234.037 ? 214 LYS HHH O   1 
ATOM 1567 C CB  . LYS A 1 211 ? 18.713  -13.395 -30.958  1.000 233.459 ? 214 LYS HHH CB  1 
ATOM 1568 C CG  . LYS A 1 211 ? 17.735  -12.279 -30.638  1.000 232.324 ? 214 LYS HHH CG  1 
ATOM 1569 C CD  . LYS A 1 211 ? 18.448  -11.134 -29.951  1.000 234.578 ? 214 LYS HHH CD  1 
ATOM 1570 C CE  . LYS A 1 211 ? 17.788  -9.793  -30.171  1.000 245.236 ? 214 LYS HHH CE  1 
ATOM 1571 N NZ  . LYS A 1 211 ? 16.756  -9.540  -29.140  1.000 260.396 ? 214 LYS HHH NZ  1 
ATOM 1572 N N   . VAL A 1 212 ? 17.620  -16.330 -29.914  1.000 228.258 ? 215 VAL HHH N   1 
ATOM 1573 C CA  . VAL A 1 212 ? 16.786  -17.055 -28.925  1.000 233.412 ? 215 VAL HHH CA  1 
ATOM 1574 C C   . VAL A 1 212 ? 17.195  -16.544 -27.538  1.000 232.358 ? 215 VAL HHH C   1 
ATOM 1575 O O   . VAL A 1 212 ? 18.382  -16.210 -27.354  1.000 235.278 ? 215 VAL HHH O   1 
ATOM 1576 C CB  . VAL A 1 212 ? 16.936  -18.576 -29.123  1.000 236.268 ? 215 VAL HHH CB  1 
ATOM 1577 C CG1 . VAL A 1 212 ? 16.713  -18.956 -30.581  1.000 234.879 ? 215 VAL HHH CG1 1 
ATOM 1578 C CG2 . VAL A 1 212 ? 18.282  -19.099 -28.648  1.000 234.900 ? 215 VAL HHH CG2 1 
ATOM 1579 N N   . GLU A 1 213 ? 16.220  -16.385 -26.643  1.000 227.165 ? 216 GLU HHH N   1 
ATOM 1580 C CA  . GLU A 1 213 ? 16.426  -16.010 -25.222  1.000 225.370 ? 216 GLU HHH CA  1 
ATOM 1581 C C   . GLU A 1 213 ? 15.115  -16.227 -24.481  1.000 226.465 ? 216 GLU HHH C   1 
ATOM 1582 O O   . GLU A 1 213 ? 14.046  -16.143 -25.078  1.000 227.446 ? 216 GLU HHH O   1 
ATOM 1583 C CB  . GLU A 1 213 ? 16.907  -14.566 -25.107  1.000 226.021 ? 216 GLU HHH CB  1 
ATOM 1584 C CG  . GLU A 1 213 ? 15.980  -13.546 -25.747  1.000 230.455 ? 216 GLU HHH CG  1 
ATOM 1585 C CD  . GLU A 1 213 ? 16.669  -12.257 -26.159  1.000 234.728 ? 216 GLU HHH CD  1 
ATOM 1586 O OE1 . GLU A 1 213 ? 17.907  -12.187 -26.056  1.000 233.622 ? 216 GLU HHH OE1 1 
ATOM 1587 O OE2 . GLU A 1 213 ? 15.965  -11.319 -26.578  1.000 242.421 ? 216 GLU HHH OE2 1 
ATOM 1588 N N   . PRO A 1 214 ? 15.153  -16.511 -23.164  1.000 233.663 ? 217 PRO HHH N   1 
ATOM 1589 C CA  . PRO A 1 214 ? 13.922  -16.670 -22.386  1.000 239.153 ? 217 PRO HHH CA  1 
ATOM 1590 C C   . PRO A 1 214 ? 13.057  -15.396 -22.372  1.000 236.269 ? 217 PRO HHH C   1 
ATOM 1591 O O   . PRO A 1 214 ? 13.576  -14.303 -22.509  1.000 229.924 ? 217 PRO HHH O   1 
ATOM 1592 C CB  . PRO A 1 214 ? 14.408  -17.072 -20.980  1.000 243.208 ? 217 PRO HHH CB  1 
ATOM 1593 C CG  . PRO A 1 214 ? 15.867  -16.650 -20.933  1.000 243.822 ? 217 PRO HHH CG  1 
ATOM 1594 C CD  . PRO A 1 214 ? 16.370  -16.691 -22.362  1.000 234.979 ? 217 PRO HHH CD  1 
ATOM 1595 N N   . LYS A 1 215 ? 11.745  -15.588 -22.237  1.000 239.511 ? 218 LYS HHH N   1 
ATOM 1596 C CA  . LYS A 1 215 ? 10.699  -14.534 -22.121  1.000 257.036 ? 218 LYS HHH CA  1 
ATOM 1597 C C   . LYS A 1 215 ? 10.169  -14.572 -20.672  1.000 268.909 ? 218 LYS HHH C   1 
ATOM 1598 O O   . LYS A 1 215 ? 10.499  -15.551 -19.977  1.000 296.060 ? 218 LYS HHH O   1 
ATOM 1599 C CB  . LYS A 1 215 ? 9.653   -14.838 -23.201  1.000 259.413 ? 218 LYS HHH CB  1 
ATOM 1600 C CG  . LYS A 1 215 ? 8.433   -13.930 -23.276  1.000 267.639 ? 218 LYS HHH CG  1 
ATOM 1601 C CD  . LYS A 1 215 ? 7.125   -14.702 -23.195  1.000 275.123 ? 218 LYS HHH CD  1 
ATOM 1602 C CE  . LYS A 1 215 ? 6.715   -15.048 -21.776  1.000 280.476 ? 218 LYS HHH CE  1 
ATOM 1603 N NZ  . LYS A 1 215 ? 6.106   -13.877 -21.109  1.000 287.952 ? 218 LYS HHH NZ  1 
ATOM 1604 N N   . SER A 1 216 ? 9.403   -13.575 -20.205  1.000 257.793 ? 219 SER HHH N   1 
ATOM 1605 C CA  . SER A 1 216 ? 8.845   -13.532 -18.824  1.000 250.225 ? 219 SER HHH CA  1 
ATOM 1606 C C   . SER A 1 216 ? 8.150   -14.862 -18.494  1.000 251.319 ? 219 SER HHH C   1 
ATOM 1607 O O   . SER A 1 216 ? 6.938   -15.008 -18.330  1.000 272.907 ? 219 SER HHH O   1 
ATOM 1608 C CB  . SER A 1 216 ? 7.926   -12.356 -18.652  1.000 249.155 ? 219 SER HHH CB  1 
ATOM 1609 O OG  . SER A 1 216 ? 8.380   -11.261 -19.430  1.000 249.293 ? 219 SER HHH OG  1 
ATOM 1610 N N   . ASP B 2 1   ? 17.227  -61.608 -66.378  1.000 220.435 ? 1   ASP LLL N   1 
ATOM 1611 C CA  . ASP B 2 1   ? 17.483  -60.464 -65.435  1.000 214.353 ? 1   ASP LLL CA  1 
ATOM 1612 C C   . ASP B 2 1   ? 17.782  -60.997 -64.031  1.000 214.970 ? 1   ASP LLL C   1 
ATOM 1613 O O   . ASP B 2 1   ? 16.918  -61.700 -63.483  1.000 231.260 ? 1   ASP LLL O   1 
ATOM 1614 C CB  . ASP B 2 1   ? 16.291  -59.514 -65.304  1.000 215.171 ? 1   ASP LLL CB  1 
ATOM 1615 C CG  . ASP B 2 1   ? 15.904  -58.813 -66.589  1.000 224.890 ? 1   ASP LLL CG  1 
ATOM 1616 O OD1 . ASP B 2 1   ? 15.107  -59.416 -67.335  1.000 233.096 ? 1   ASP LLL OD1 1 
ATOM 1617 O OD2 . ASP B 2 1   ? 16.405  -57.666 -66.831  1.000 239.607 ? 1   ASP LLL OD2 1 
ATOM 1618 N N   . ILE B 2 2   ? 18.928  -60.620 -63.457  1.000 208.666 ? 2   ILE LLL N   1 
ATOM 1619 C CA  . ILE B 2 2   ? 19.396  -61.044 -62.104  1.000 194.796 ? 2   ILE LLL CA  1 
ATOM 1620 C C   . ILE B 2 2   ? 18.855  -60.067 -61.062  1.000 190.922 ? 2   ILE LLL C   1 
ATOM 1621 O O   . ILE B 2 2   ? 18.796  -58.866 -61.353  1.000 191.583 ? 2   ILE LLL O   1 
ATOM 1622 C CB  . ILE B 2 2   ? 20.930  -61.106 -62.072  1.000 187.655 ? 2   ILE LLL CB  1 
ATOM 1623 C CG1 . ILE B 2 2   ? 21.460  -62.141 -63.070  1.000 195.854 ? 2   ILE LLL CG1 1 
ATOM 1624 C CG2 . ILE B 2 2   ? 21.416  -61.379 -60.666  1.000 183.956 ? 2   ILE LLL CG2 1 
ATOM 1625 C CD1 . ILE B 2 2   ? 22.908  -61.930 -63.460  1.000 193.438 ? 2   ILE LLL CD1 1 
ATOM 1626 N N   . GLN B 2 3   ? 18.451  -60.579 -59.903  1.000 196.251 ? 3   GLN LLL N   1 
ATOM 1627 C CA  . GLN B 2 3   ? 18.053  -59.746 -58.745  1.000 199.458 ? 3   GLN LLL CA  1 
ATOM 1628 C C   . GLN B 2 3   ? 18.792  -60.216 -57.502  1.000 196.439 ? 3   GLN LLL C   1 
ATOM 1629 O O   . GLN B 2 3   ? 18.915  -61.433 -57.310  1.000 197.017 ? 3   GLN LLL O   1 
ATOM 1630 C CB  . GLN B 2 3   ? 16.541  -59.731 -58.537  1.000 206.255 ? 3   GLN LLL CB  1 
ATOM 1631 C CG  . GLN B 2 3   ? 15.850  -58.727 -59.451  1.000 219.278 ? 3   GLN LLL CG  1 
ATOM 1632 C CD  . GLN B 2 3   ? 15.027  -57.695 -58.716  1.000 226.119 ? 3   GLN LLL CD  1 
ATOM 1633 O OE1 . GLN B 2 3   ? 13.873  -57.437 -59.058  1.000 243.871 ? 3   GLN LLL OE1 1 
ATOM 1634 N NE2 . GLN B 2 3   ? 15.626  -57.081 -57.706  1.000 226.978 ? 3   GLN LLL NE2 1 
ATOM 1635 N N   . LEU B 2 4   ? 19.288  -59.240 -56.745  1.000 196.495 ? 4   LEU LLL N   1 
ATOM 1636 C CA  . LEU B 2 4   ? 20.127  -59.422 -55.542  1.000 191.012 ? 4   LEU LLL CA  1 
ATOM 1637 C C   . LEU B 2 4   ? 19.361  -58.860 -54.348  1.000 189.121 ? 4   LEU LLL C   1 
ATOM 1638 O O   . LEU B 2 4   ? 18.818  -57.730 -54.442  1.000 181.080 ? 4   LEU LLL O   1 
ATOM 1639 C CB  . LEU B 2 4   ? 21.457  -58.687 -55.730  1.000 189.075 ? 4   LEU LLL CB  1 
ATOM 1640 C CG  . LEU B 2 4   ? 22.493  -59.352 -56.638  1.000 189.789 ? 4   LEU LLL CG  1 
ATOM 1641 C CD1 . LEU B 2 4   ? 22.083  -59.311 -58.098  1.000 194.949 ? 4   LEU LLL CD1 1 
ATOM 1642 C CD2 . LEU B 2 4   ? 23.839  -58.659 -56.468  1.000 185.875 ? 4   LEU LLL CD2 1 
ATOM 1643 N N   . THR B 2 5   ? 19.331  -59.636 -53.271  1.000 191.770 ? 5   THR LLL N   1 
ATOM 1644 C CA  . THR B 2 5   ? 18.766  -59.222 -51.968  1.000 193.885 ? 5   THR LLL CA  1 
ATOM 1645 C C   . THR B 2 5   ? 19.806  -59.523 -50.887  1.000 183.115 ? 5   THR LLL C   1 
ATOM 1646 O O   . THR B 2 5   ? 20.348  -60.649 -50.876  1.000 174.465 ? 5   THR LLL O   1 
ATOM 1647 C CB  . THR B 2 5   ? 17.394  -59.868 -51.772  1.000 199.544 ? 5   THR LLL CB  1 
ATOM 1648 O OG1 . THR B 2 5   ? 17.560  -61.271 -51.978  1.000 209.563 ? 5   THR LLL OG1 1 
ATOM 1649 C CG2 . THR B 2 5   ? 16.364  -59.317 -52.731  1.000 200.480 ? 5   THR LLL CG2 1 
ATOM 1650 N N   . GLN B 2 6   ? 20.107  -58.511 -50.075  1.000 171.894 ? 6   GLN LLL N   1 
ATOM 1651 C CA  . GLN B 2 6   ? 21.071  -58.585 -48.956  1.000 178.059 ? 6   GLN LLL CA  1 
ATOM 1652 C C   . GLN B 2 6   ? 20.315  -58.994 -47.688  1.000 187.473 ? 6   GLN LLL C   1 
ATOM 1653 O O   . GLN B 2 6   ? 19.109  -58.708 -47.594  1.000 195.712 ? 6   GLN LLL O   1 
ATOM 1654 C CB  . GLN B 2 6   ? 21.795  -57.245 -48.777  1.000 176.899 ? 6   GLN LLL CB  1 
ATOM 1655 C CG  . GLN B 2 6   ? 22.475  -56.719 -50.041  1.000 180.579 ? 6   GLN LLL CG  1 
ATOM 1656 C CD  . GLN B 2 6   ? 23.105  -55.348 -49.904  1.000 177.499 ? 6   GLN LLL CD  1 
ATOM 1657 O OE1 . GLN B 2 6   ? 23.329  -54.659 -50.889  1.000 177.332 ? 6   GLN LLL OE1 1 
ATOM 1658 N NE2 . GLN B 2 6   ? 23.375  -54.913 -48.686  1.000 179.184 ? 6   GLN LLL NE2 1 
ATOM 1659 N N   . SER B 2 7   ? 20.998  -59.663 -46.758  1.000 192.414 ? 7   SER LLL N   1 
ATOM 1660 C CA  . SER B 2 7   ? 20.528  -59.897 -45.369  1.000 193.450 ? 7   SER LLL CA  1 
ATOM 1661 C C   . SER B 2 7   ? 21.691  -59.647 -44.421  1.000 186.562 ? 7   SER LLL C   1 
ATOM 1662 O O   . SER B 2 7   ? 22.783  -60.132 -44.683  1.000 187.745 ? 7   SER LLL O   1 
ATOM 1663 C CB  . SER B 2 7   ? 19.990  -61.279 -45.218  1.000 204.996 ? 7   SER LLL CB  1 
ATOM 1664 O OG  . SER B 2 7   ? 19.048  -61.557 -46.243  1.000 215.057 ? 7   SER LLL OG  1 
ATOM 1665 N N   . PRO B 2 8   ? 21.521  -58.892 -43.311  1.000 178.253 ? 8   PRO LLL N   1 
ATOM 1666 C CA  . PRO B 2 8   ? 20.258  -58.250 -42.964  1.000 175.610 ? 8   PRO LLL CA  1 
ATOM 1667 C C   . PRO B 2 8   ? 20.039  -56.892 -43.642  1.000 171.141 ? 8   PRO LLL C   1 
ATOM 1668 O O   . PRO B 2 8   ? 20.914  -56.414 -44.344  1.000 169.945 ? 8   PRO LLL O   1 
ATOM 1669 C CB  . PRO B 2 8   ? 20.451  -58.011 -41.463  1.000 180.585 ? 8   PRO LLL CB  1 
ATOM 1670 C CG  . PRO B 2 8   ? 21.912  -57.646 -41.346  1.000 173.716 ? 8   PRO LLL CG  1 
ATOM 1671 C CD  . PRO B 2 8   ? 22.570  -58.604 -42.316  1.000 178.482 ? 8   PRO LLL CD  1 
ATOM 1672 N N   . ASP B 2 9   ? 18.881  -56.295 -43.380  1.000 170.027 ? 9   ASP LLL N   1 
ATOM 1673 C CA  . ASP B 2 9   ? 18.528  -54.931 -43.829  1.000 176.702 ? 9   ASP LLL CA  1 
ATOM 1674 C C   . ASP B 2 9   ? 19.371  -53.930 -43.050  1.000 169.458 ? 9   ASP LLL C   1 
ATOM 1675 O O   . ASP B 2 9   ? 20.038  -53.073 -43.668  1.000 170.333 ? 9   ASP LLL O   1 
ATOM 1676 C CB  . ASP B 2 9   ? 17.030  -54.681 -43.663  1.000 194.790 ? 9   ASP LLL CB  1 
ATOM 1677 C CG  . ASP B 2 9   ? 16.254  -55.097 -44.903  1.000 217.283 ? 9   ASP LLL CG  1 
ATOM 1678 O OD1 . ASP B 2 9   ? 16.718  -56.031 -45.600  1.000 225.283 ? 9   ASP LLL OD1 1 
ATOM 1679 O OD2 . ASP B 2 9   ? 15.218  -54.457 -45.191  1.000 241.995 ? 9   ASP LLL OD2 1 
ATOM 1680 N N   . SER B 2 10  ? 19.322  -54.019 -41.731  1.000 166.142 ? 10  SER LLL N   1 
ATOM 1681 C CA  . SER B 2 10  ? 20.069  -53.098 -40.850  1.000 165.387 ? 10  SER LLL CA  1 
ATOM 1682 C C   . SER B 2 10  ? 20.941  -53.926 -39.925  1.000 161.923 ? 10  SER LLL C   1 
ATOM 1683 O O   . SER B 2 10  ? 20.733  -55.130 -39.884  1.000 150.139 ? 10  SER LLL O   1 
ATOM 1684 C CB  . SER B 2 10  ? 19.141  -52.224 -40.095  1.000 168.394 ? 10  SER LLL CB  1 
ATOM 1685 O OG  . SER B 2 10  ? 19.868  -51.524 -39.106  1.000 171.823 ? 10  SER LLL OG  1 
ATOM 1686 N N   . LEU B 2 11  ? 21.879  -53.285 -39.236  1.000 169.860 ? 11  LEU LLL N   1 
ATOM 1687 C CA  . LEU B 2 11  ? 22.910  -53.997 -38.442  1.000 181.212 ? 11  LEU LLL CA  1 
ATOM 1688 C C   . LEU B 2 11  ? 23.603  -53.018 -37.481  1.000 183.632 ? 11  LEU LLL C   1 
ATOM 1689 O O   . LEU B 2 11  ? 23.994  -51.900 -37.920  1.000 162.166 ? 11  LEU LLL O   1 
ATOM 1690 C CB  . LEU B 2 11  ? 23.890  -54.633 -39.434  1.000 179.810 ? 11  LEU LLL CB  1 
ATOM 1691 C CG  . LEU B 2 11  ? 24.940  -55.574 -38.854  1.000 177.758 ? 11  LEU LLL CG  1 
ATOM 1692 C CD1 . LEU B 2 11  ? 25.193  -56.741 -39.801  1.000 173.352 ? 11  LEU LLL CD1 1 
ATOM 1693 C CD2 . LEU B 2 11  ? 26.228  -54.812 -38.587  1.000 176.178 ? 11  LEU LLL CD2 1 
ATOM 1694 N N   . ALA B 2 12  ? 23.705  -53.422 -36.203  1.000 186.126 ? 12  ALA LLL N   1 
ATOM 1695 C CA  . ALA B 2 12  ? 24.449  -52.721 -35.127  1.000 173.248 ? 12  ALA LLL CA  1 
ATOM 1696 C C   . ALA B 2 12  ? 25.441  -53.713 -34.507  1.000 160.562 ? 12  ALA LLL C   1 
ATOM 1697 O O   . ALA B 2 12  ? 25.046  -54.855 -34.170  1.000 153.248 ? 12  ALA LLL O   1 
ATOM 1698 C CB  . ALA B 2 12  ? 23.506  -52.102 -34.108  1.000 171.232 ? 12  ALA LLL CB  1 
ATOM 1699 N N   . VAL B 2 13  ? 26.698  -53.289 -34.429  1.000 150.379 ? 13  VAL LLL N   1 
ATOM 1700 C CA  . VAL B 2 13  ? 27.846  -54.075 -33.911  1.000 152.405 ? 13  VAL LLL CA  1 
ATOM 1701 C C   . VAL B 2 13  ? 28.701  -53.112 -33.105  1.000 147.166 ? 13  VAL LLL C   1 
ATOM 1702 O O   . VAL B 2 13  ? 28.864  -51.972 -33.550  1.000 132.843 ? 13  VAL LLL O   1 
ATOM 1703 C CB  . VAL B 2 13  ? 28.650  -54.683 -35.075  1.000 165.623 ? 13  VAL LLL CB  1 
ATOM 1704 C CG1 . VAL B 2 13  ? 30.085  -54.989 -34.699  1.000 168.536 ? 13  VAL LLL CG1 1 
ATOM 1705 C CG2 . VAL B 2 13  ? 27.974  -55.915 -35.644  1.000 172.114 ? 13  VAL LLL CG2 1 
ATOM 1706 N N   . SER B 2 14  ? 29.226  -53.552 -31.967  1.000 152.031 ? 14  SER LLL N   1 
ATOM 1707 C CA  . SER B 2 14  ? 30.076  -52.715 -31.088  1.000 156.802 ? 14  SER LLL CA  1 
ATOM 1708 C C   . SER B 2 14  ? 31.449  -52.559 -31.750  1.000 151.722 ? 14  SER LLL C   1 
ATOM 1709 O O   . SER B 2 14  ? 31.803  -53.477 -32.518  1.000 144.313 ? 14  SER LLL O   1 
ATOM 1710 C CB  . SER B 2 14  ? 30.156  -53.348 -29.741  1.000 168.170 ? 14  SER LLL CB  1 
ATOM 1711 O OG  . SER B 2 14  ? 29.961  -54.751 -29.873  1.000 183.195 ? 14  SER LLL OG  1 
ATOM 1712 N N   . LEU B 2 15  ? 32.157  -51.437 -31.510  1.000 150.101 ? 15  LEU LLL N   1 
ATOM 1713 C CA  . LEU B 2 15  ? 33.591  -51.253 -31.889  1.000 150.084 ? 15  LEU LLL CA  1 
ATOM 1714 C C   . LEU B 2 15  ? 34.327  -52.582 -31.759  1.000 144.716 ? 15  LEU LLL C   1 
ATOM 1715 O O   . LEU B 2 15  ? 34.134  -53.265 -30.764  1.000 163.200 ? 15  LEU LLL O   1 
ATOM 1716 C CB  . LEU B 2 15  ? 34.307  -50.288 -30.937  1.000 156.543 ? 15  LEU LLL CB  1 
ATOM 1717 C CG  . LEU B 2 15  ? 34.597  -48.867 -31.402  1.000 161.666 ? 15  LEU LLL CG  1 
ATOM 1718 C CD1 . LEU B 2 15  ? 35.881  -48.357 -30.751  1.000 169.406 ? 15  LEU LLL CD1 1 
ATOM 1719 C CD2 . LEU B 2 15  ? 34.730  -48.761 -32.893  1.000 160.720 ? 15  LEU LLL CD2 1 
ATOM 1720 N N   . GLY B 2 16  ? 35.245  -52.863 -32.656  1.000 134.360 ? 16  GLY LLL N   1 
ATOM 1721 C CA  . GLY B 2 16  ? 36.191  -53.967 -32.465  1.000 138.289 ? 16  GLY LLL CA  1 
ATOM 1722 C C   . GLY B 2 16  ? 35.594  -55.307 -32.841  1.000 142.392 ? 16  GLY LLL C   1 
ATOM 1723 O O   . GLY B 2 16  ? 36.396  -56.235 -33.105  1.000 143.019 ? 16  GLY LLL O   1 
ATOM 1724 N N   . GLU B 2 17  ? 34.266  -55.424 -32.904  1.000 149.501 ? 17  GLU LLL N   1 
ATOM 1725 C CA  . GLU B 2 17  ? 33.606  -56.711 -33.249  1.000 168.069 ? 17  GLU LLL CA  1 
ATOM 1726 C C   . GLU B 2 17  ? 33.512  -56.792 -34.777  1.000 163.576 ? 17  GLU LLL C   1 
ATOM 1727 O O   . GLU B 2 17  ? 33.902  -55.815 -35.444  1.000 166.230 ? 17  GLU LLL O   1 
ATOM 1728 C CB  . GLU B 2 17  ? 32.236  -56.848 -32.572  1.000 181.376 ? 17  GLU LLL CB  1 
ATOM 1729 C CG  . GLU B 2 17  ? 32.230  -56.560 -31.082  1.000 195.288 ? 17  GLU LLL CG  1 
ATOM 1730 C CD  . GLU B 2 17  ? 33.250  -57.323 -30.254  1.000 210.026 ? 17  GLU LLL CD  1 
ATOM 1731 O OE1 . GLU B 2 17  ? 34.002  -56.674 -29.489  1.000 217.684 ? 17  GLU LLL OE1 1 
ATOM 1732 O OE2 . GLU B 2 17  ? 33.270  -58.567 -30.349  1.000 227.233 ? 17  GLU LLL OE2 1 
ATOM 1733 N N   . ARG B 2 18  ? 33.019  -57.916 -35.312  1.000 163.782 ? 18  ARG LLL N   1 
ATOM 1734 C CA  . ARG B 2 18  ? 32.862  -58.139 -36.776  1.000 156.793 ? 18  ARG LLL CA  1 
ATOM 1735 C C   . ARG B 2 18  ? 31.383  -58.039 -37.156  1.000 156.815 ? 18  ARG LLL C   1 
ATOM 1736 O O   . ARG B 2 18  ? 30.526  -58.574 -36.444  1.000 154.217 ? 18  ARG LLL O   1 
ATOM 1737 C CB  . ARG B 2 18  ? 33.477  -59.464 -37.242  1.000 155.875 ? 18  ARG LLL CB  1 
ATOM 1738 C CG  . ARG B 2 18  ? 32.512  -60.635 -37.402  1.000 161.290 ? 18  ARG LLL CG  1 
ATOM 1739 C CD  . ARG B 2 18  ? 33.227  -61.988 -37.366  1.000 163.720 ? 18  ARG LLL CD  1 
ATOM 1740 N NE  . ARG B 2 18  ? 34.522  -61.859 -38.022  1.000 162.900 ? 18  ARG LLL NE  1 
ATOM 1741 C CZ  . ARG B 2 18  ? 35.572  -62.673 -37.883  1.000 170.395 ? 18  ARG LLL CZ  1 
ATOM 1742 N NH1 . ARG B 2 18  ? 35.513  -63.736 -37.091  1.000 173.577 ? 18  ARG LLL NH1 1 
ATOM 1743 N NH2 . ARG B 2 18  ? 36.687  -62.412 -38.560  1.000 171.982 ? 18  ARG LLL NH2 1 
ATOM 1744 N N   . ALA B 2 19  ? 31.132  -57.365 -38.275  1.000 162.201 ? 19  ALA LLL N   1 
ATOM 1745 C CA  . ALA B 2 19  ? 29.854  -57.357 -39.010  1.000 154.022 ? 19  ALA LLL CA  1 
ATOM 1746 C C   . ALA B 2 19  ? 30.059  -58.151 -40.296  1.000 147.900 ? 19  ALA LLL C   1 
ATOM 1747 O O   . ALA B 2 19  ? 31.155  -58.132 -40.861  1.000 139.706 ? 19  ALA LLL O   1 
ATOM 1748 C CB  . ALA B 2 19  ? 29.411  -55.950 -39.281  1.000 145.933 ? 19  ALA LLL CB  1 
ATOM 1749 N N   . THR B 2 20  ? 29.037  -58.896 -40.664  1.000 150.567 ? 20  THR LLL N   1 
ATOM 1750 C CA  . THR B 2 20  ? 28.973  -59.654 -41.925  1.000 155.473 ? 20  THR LLL CA  1 
ATOM 1751 C C   . THR B 2 20  ? 27.638  -59.295 -42.573  1.000 156.167 ? 20  THR LLL C   1 
ATOM 1752 O O   . THR B 2 20  ? 26.686  -59.011 -41.819  1.000 141.965 ? 20  THR LLL O   1 
ATOM 1753 C CB  . THR B 2 20  ? 29.135  -61.156 -41.683  1.000 161.643 ? 20  THR LLL CB  1 
ATOM 1754 O OG1 . THR B 2 20  ? 27.860  -61.590 -41.207  1.000 171.044 ? 20  THR LLL OG1 1 
ATOM 1755 C CG2 . THR B 2 20  ? 30.216  -61.497 -40.686  1.000 162.829 ? 20  THR LLL CG2 1 
ATOM 1756 N N   . ILE B 2 21  ? 27.607  -59.301 -43.913  1.000 166.862 ? 21  ILE LLL N   1 
ATOM 1757 C CA  . ILE B 2 21  ? 26.443  -58.924 -44.769  1.000 160.862 ? 21  ILE LLL CA  1 
ATOM 1758 C C   . ILE B 2 21  ? 26.295  -59.967 -45.887  1.000 163.920 ? 21  ILE LLL C   1 
ATOM 1759 O O   . ILE B 2 21  ? 27.216  -60.073 -46.706  1.000 164.227 ? 21  ILE LLL O   1 
ATOM 1760 C CB  . ILE B 2 21  ? 26.621  -57.493 -45.320  1.000 150.109 ? 21  ILE LLL CB  1 
ATOM 1761 C CG1 . ILE B 2 21  ? 26.977  -56.492 -44.214  1.000 152.925 ? 21  ILE LLL CG1 1 
ATOM 1762 C CG2 . ILE B 2 21  ? 25.360  -57.091 -46.045  1.000 152.101 ? 21  ILE LLL CG2 1 
ATOM 1763 C CD1 . ILE B 2 21  ? 27.046  -55.043 -44.638  1.000 151.131 ? 21  ILE LLL CD1 1 
ATOM 1764 N N   . ASN B 2 22  ? 25.184  -60.709 -45.925  1.000 168.184 ? 22  ASN LLL N   1 
ATOM 1765 C CA  . ASN B 2 22  ? 24.851  -61.641 -47.034  1.000 186.871 ? 22  ASN LLL CA  1 
ATOM 1766 C C   . ASN B 2 22  ? 24.363  -60.862 -48.246  1.000 193.731 ? 22  ASN LLL C   1 
ATOM 1767 O O   . ASN B 2 22  ? 23.799  -59.789 -48.032  1.000 212.807 ? 22  ASN LLL O   1 
ATOM 1768 C CB  . ASN B 2 22  ? 23.721  -62.598 -46.678  1.000 201.375 ? 22  ASN LLL CB  1 
ATOM 1769 C CG  . ASN B 2 22  ? 24.153  -63.572 -45.614  1.000 220.769 ? 22  ASN LLL CG  1 
ATOM 1770 O OD1 . ASN B 2 22  ? 25.318  -63.980 -45.599  1.000 229.033 ? 22  ASN LLL OD1 1 
ATOM 1771 N ND2 . ASN B 2 22  ? 23.232  -63.919 -44.723  1.000 228.989 ? 22  ASN LLL ND2 1 
ATOM 1772 N N   . CYS B 2 23  ? 24.523  -61.429 -49.448  1.000 192.385 ? 23  CYS LLL N   1 
ATOM 1773 C CA  . CYS B 2 23  ? 23.958  -60.923 -50.729  1.000 179.397 ? 23  CYS LLL CA  1 
ATOM 1774 C C   . CYS B 2 23  ? 23.708  -62.098 -51.675  1.000 169.252 ? 23  CYS LLL C   1 
ATOM 1775 O O   . CYS B 2 23  ? 24.670  -62.647 -52.243  1.000 157.928 ? 23  CYS LLL O   1 
ATOM 1776 C CB  . CYS B 2 23  ? 24.887  -59.902 -51.365  1.000 189.059 ? 23  CYS LLL CB  1 
ATOM 1777 S SG  . CYS B 2 23  ? 24.356  -59.371 -53.015  1.000 213.916 ? 23  CYS LLL SG  1 
ATOM 1778 N N   . LYS B 2 24  ? 22.450  -62.497 -51.784  1.000 173.185 ? 24  LYS LLL N   1 
ATOM 1779 C CA  . LYS B 2 24  ? 22.045  -63.679 -52.574  1.000 187.594 ? 24  LYS LLL CA  1 
ATOM 1780 C C   . LYS B 2 24  ? 21.431  -63.158 -53.867  1.000 190.834 ? 24  LYS LLL C   1 
ATOM 1781 O O   . LYS B 2 24  ? 20.700  -62.147 -53.788  1.000 188.555 ? 24  LYS LLL O   1 
ATOM 1782 C CB  . LYS B 2 24  ? 21.081  -64.546 -51.768  1.000 201.937 ? 24  LYS LLL CB  1 
ATOM 1783 C CG  . LYS B 2 24  ? 20.506  -65.749 -52.500  1.000 213.159 ? 24  LYS LLL CG  1 
ATOM 1784 C CD  . LYS B 2 24  ? 19.750  -66.684 -51.550  1.000 219.919 ? 24  LYS LLL CD  1 
ATOM 1785 C CE  . LYS B 2 24  ? 19.370  -68.022 -52.146  1.000 225.720 ? 24  LYS LLL CE  1 
ATOM 1786 N NZ  . LYS B 2 24  ? 20.553  -68.902 -52.305  1.000 236.618 ? 24  LYS LLL NZ  1 
ATOM 1787 N N   . SER B 2 25  ? 21.756  -63.809 -54.990  1.000 192.523 ? 25  SER LLL N   1 
ATOM 1788 C CA  . SER B 2 25  ? 21.424  -63.385 -56.378  1.000 192.412 ? 25  SER LLL CA  1 
ATOM 1789 C C   . SER B 2 25  ? 20.412  -64.363 -56.962  1.000 191.651 ? 25  SER LLL C   1 
ATOM 1790 O O   . SER B 2 25  ? 20.455  -65.525 -56.557  1.000 196.470 ? 25  SER LLL O   1 
ATOM 1791 C CB  . SER B 2 25  ? 22.656  -63.326 -57.252  1.000 195.083 ? 25  SER LLL CB  1 
ATOM 1792 O OG  . SER B 2 25  ? 22.905  -64.583 -57.876  1.000 200.173 ? 25  SER LLL OG  1 
ATOM 1793 N N   . SER B 2 26  ? 19.577  -63.911 -57.900  1.000 190.772 ? 26  SER LLL N   1 
ATOM 1794 C CA  . SER B 2 26  ? 18.574  -64.747 -58.610  1.000 196.057 ? 26  SER LLL CA  1 
ATOM 1795 C C   . SER B 2 26  ? 19.287  -65.859 -59.375  1.000 186.485 ? 26  SER LLL C   1 
ATOM 1796 O O   . SER B 2 26  ? 18.786  -66.992 -59.429  1.000 191.132 ? 26  SER LLL O   1 
ATOM 1797 C CB  . SER B 2 26  ? 17.737  -63.938 -59.555  1.000 203.790 ? 26  SER LLL CB  1 
ATOM 1798 O OG  . SER B 2 26  ? 16.996  -64.802 -60.408  1.000 212.690 ? 26  SER LLL OG  1 
ATOM 1799 N N   . GLN B 2 27  ? 20.398  -65.516 -59.996  1.000 176.521 ? 27  GLN LLL N   1 
ATOM 1800 C CA  . GLN B 2 27  ? 21.125  -66.458 -60.866  1.000 187.448 ? 27  GLN LLL CA  1 
ATOM 1801 C C   . GLN B 2 27  ? 22.619  -66.249 -60.662  1.000 186.375 ? 27  GLN LLL C   1 
ATOM 1802 O O   . GLN B 2 27  ? 23.039  -65.132 -60.309  1.000 180.554 ? 27  GLN LLL O   1 
ATOM 1803 C CB  . GLN B 2 27  ? 20.713  -66.230 -62.318  1.000 197.930 ? 27  GLN LLL CB  1 
ATOM 1804 C CG  . GLN B 2 27  ? 21.300  -67.239 -63.295  1.000 205.550 ? 27  GLN LLL CG  1 
ATOM 1805 C CD  . GLN B 2 27  ? 21.423  -66.670 -64.685  1.000 206.472 ? 27  GLN LLL CD  1 
ATOM 1806 O OE1 . GLN B 2 27  ? 20.705  -65.745 -65.062  1.000 212.471 ? 27  GLN LLL OE1 1 
ATOM 1807 N NE2 . GLN B 2 27  ? 22.360  -67.210 -65.445  1.000 204.750 ? 27  GLN LLL NE2 1 
ATOM 1808 N N   . SER B 2 28  ? 23.383  -67.306 -60.902  1.000 193.926 ? 28  SER LLL N   1 
ATOM 1809 C CA  . SER B 2 28  ? 24.847  -67.347 -60.695  1.000 202.411 ? 28  SER LLL CA  1 
ATOM 1810 C C   . SER B 2 28  ? 25.551  -66.373 -61.644  1.000 195.509 ? 28  SER LLL C   1 
ATOM 1811 O O   . SER B 2 28  ? 25.147  -66.267 -62.817  1.000 201.896 ? 28  SER LLL O   1 
ATOM 1812 C CB  . SER B 2 28  ? 25.368  -68.753 -60.842  1.000 215.038 ? 28  SER LLL CB  1 
ATOM 1813 O OG  . SER B 2 28  ? 26.740  -68.751 -61.209  1.000 222.929 ? 28  SER LLL OG  1 
ATOM 1814 N N   . VAL B 2 29  ? 26.609  -65.746 -61.137  1.000 182.106 ? 29  VAL LLL N   1 
ATOM 1815 C CA  . VAL B 2 29  ? 27.380  -64.676 -61.817  1.000 178.135 ? 29  VAL LLL CA  1 
ATOM 1816 C C   . VAL B 2 29  ? 28.834  -65.124 -62.011  1.000 174.568 ? 29  VAL LLL C   1 
ATOM 1817 O O   . VAL B 2 29  ? 29.746  -64.302 -61.772  1.000 170.024 ? 29  VAL LLL O   1 
ATOM 1818 C CB  . VAL B 2 29  ? 27.276  -63.383 -60.995  1.000 183.452 ? 29  VAL LLL CB  1 
ATOM 1819 C CG1 . VAL B 2 29  ? 25.866  -62.821 -61.065  1.000 190.495 ? 29  VAL LLL CG1 1 
ATOM 1820 C CG2 . VAL B 2 29  ? 27.703  -63.583 -59.547  1.000 189.521 ? 29  VAL LLL CG2 1 
ATOM 1821 N N   . LEU B 2 30  ? 29.062  -66.354 -62.475  1.000 175.710 ? 30  LEU LLL N   1 
ATOM 1822 C CA  . LEU B 2 30  ? 30.444  -66.862 -62.692  1.000 184.807 ? 30  LEU LLL CA  1 
ATOM 1823 C C   . LEU B 2 30  ? 30.789  -66.866 -64.177  1.000 180.879 ? 30  LEU LLL C   1 
ATOM 1824 O O   . LEU B 2 30  ? 30.167  -67.630 -64.934  1.000 189.018 ? 30  LEU LLL O   1 
ATOM 1825 C CB  . LEU B 2 30  ? 30.596  -68.279 -62.140  1.000 207.069 ? 30  LEU LLL CB  1 
ATOM 1826 C CG  . LEU B 2 30  ? 30.814  -68.380 -60.633  1.000 216.923 ? 30  LEU LLL CG  1 
ATOM 1827 C CD1 . LEU B 2 30  ? 29.519  -68.765 -59.918  1.000 224.605 ? 30  LEU LLL CD1 1 
ATOM 1828 C CD2 . LEU B 2 30  ? 31.934  -69.369 -60.309  1.000 217.464 ? 30  LEU LLL CD2 1 
ATOM 1829 N N   . TYR B 2 31  ? 31.789  -66.071 -64.553  1.000 175.271 ? 31  TYR LLL N   1 
ATOM 1830 C CA  . TYR B 2 31  ? 32.533  -66.226 -65.830  1.000 173.603 ? 31  TYR LLL CA  1 
ATOM 1831 C C   . TYR B 2 31  ? 33.364  -67.495 -65.742  1.000 172.108 ? 31  TYR LLL C   1 
ATOM 1832 O O   . TYR B 2 31  ? 33.830  -67.836 -64.642  1.000 178.259 ? 31  TYR LLL O   1 
ATOM 1833 C CB  . TYR B 2 31  ? 33.391  -65.005 -66.167  1.000 166.322 ? 31  TYR LLL CB  1 
ATOM 1834 C CG  . TYR B 2 31  ? 32.651  -64.006 -67.020  1.000 165.061 ? 31  TYR LLL CG  1 
ATOM 1835 C CD1 . TYR B 2 31  ? 31.366  -63.598 -66.706  1.000 164.115 ? 31  TYR LLL CD1 1 
ATOM 1836 C CD2 . TYR B 2 31  ? 33.214  -63.510 -68.178  1.000 165.008 ? 31  TYR LLL CD2 1 
ATOM 1837 C CE1 . TYR B 2 31  ? 30.675  -62.711 -67.510  1.000 164.240 ? 31  TYR LLL CE1 1 
ATOM 1838 C CE2 . TYR B 2 31  ? 32.542  -62.619 -68.996  1.000 161.534 ? 31  TYR LLL CE2 1 
ATOM 1839 C CZ  . TYR B 2 31  ? 31.265  -62.228 -68.659  1.000 164.128 ? 31  TYR LLL CZ  1 
ATOM 1840 O OH  . TYR B 2 31  ? 30.594  -61.344 -69.439  1.000 178.683 ? 31  TYR LLL OH  1 
ATOM 1841 N N   . SER B 2 32  ? 33.445  -68.187 -66.868  1.000 175.572 ? 32  SER LLL N   1 
ATOM 1842 C CA  . SER B 2 32  ? 34.171  -69.464 -67.039  1.000 189.384 ? 32  SER LLL CA  1 
ATOM 1843 C C   . SER B 2 32  ? 35.517  -69.187 -67.687  1.000 193.137 ? 32  SER LLL C   1 
ATOM 1844 O O   . SER B 2 32  ? 36.406  -70.025 -67.541  1.000 197.460 ? 32  SER LLL O   1 
ATOM 1845 C CB  . SER B 2 32  ? 33.385  -70.436 -67.865  1.000 200.265 ? 32  SER LLL CB  1 
ATOM 1846 O OG  . SER B 2 32  ? 32.444  -71.121 -67.066  1.000 219.191 ? 32  SER LLL OG  1 
ATOM 1847 N N   . SER B 2 33  ? 35.629  -68.062 -68.393  1.000 206.009 ? 33  SER LLL N   1 
ATOM 1848 C CA  . SER B 2 33  ? 36.869  -67.622 -69.083  1.000 216.551 ? 33  SER LLL CA  1 
ATOM 1849 C C   . SER B 2 33  ? 38.013  -67.653 -68.076  1.000 201.989 ? 33  SER LLL C   1 
ATOM 1850 O O   . SER B 2 33  ? 39.131  -68.147 -68.377  1.000 184.364 ? 33  SER LLL O   1 
ATOM 1851 C CB  . SER B 2 33  ? 36.685  -66.235 -69.628  1.000 228.637 ? 33  SER LLL CB  1 
ATOM 1852 O OG  . SER B 2 33  ? 37.918  -65.670 -70.068  1.000 241.019 ? 33  SER LLL OG  1 
ATOM 1853 N N   . ILE B 2 34  ? 37.677  -67.086 -66.926  1.000 197.501 ? 34  ILE LLL N   1 
ATOM 1854 C CA  . ILE B 2 34  ? 38.528  -66.894 -65.728  1.000 192.367 ? 34  ILE LLL CA  1 
ATOM 1855 C C   . ILE B 2 34  ? 37.598  -67.229 -64.555  1.000 200.578 ? 34  ILE LLL C   1 
ATOM 1856 O O   . ILE B 2 34  ? 36.457  -66.676 -64.508  1.000 210.541 ? 34  ILE LLL O   1 
ATOM 1857 C CB  . ILE B 2 34  ? 39.099  -65.456 -65.735  1.000 175.317 ? 34  ILE LLL CB  1 
ATOM 1858 C CG1 . ILE B 2 34  ? 38.059  -64.414 -66.154  1.000 166.856 ? 34  ILE LLL CG1 1 
ATOM 1859 C CG2 . ILE B 2 34  ? 40.318  -65.349 -66.636  1.000 171.474 ? 34  ILE LLL CG2 1 
ATOM 1860 C CD1 . ILE B 2 34  ? 38.495  -62.993 -65.917  1.000 161.413 ? 34  ILE LLL CD1 1 
ATOM 1861 N N   . ASN B 2 35  ? 37.994  -68.185 -63.714  1.000 198.383 ? 35  ASN LLL N   1 
ATOM 1862 C CA  . ASN B 2 35  ? 37.121  -68.698 -62.630  1.000 199.005 ? 35  ASN LLL CA  1 
ATOM 1863 C C   . ASN B 2 35  ? 36.872  -67.536 -61.667  1.000 188.526 ? 35  ASN LLL C   1 
ATOM 1864 O O   . ASN B 2 35  ? 37.403  -67.599 -60.543  1.000 205.965 ? 35  ASN LLL O   1 
ATOM 1865 C CB  . ASN B 2 35  ? 37.736  -69.924 -61.948  1.000 204.422 ? 35  ASN LLL CB  1 
ATOM 1866 C CG  . ASN B 2 35  ? 36.780  -70.633 -61.011  1.000 214.466 ? 35  ASN LLL CG  1 
ATOM 1867 O OD1 . ASN B 2 35  ? 35.991  -70.005 -60.302  1.000 205.953 ? 35  ASN LLL OD1 1 
ATOM 1868 N ND2 . ASN B 2 35  ? 36.858  -71.953 -60.990  1.000 232.566 ? 35  ASN LLL ND2 1 
ATOM 1869 N N   . LYS B 2 36  ? 36.155  -66.489 -62.095  1.000 165.073 ? 36  LYS LLL N   1 
ATOM 1870 C CA  . LYS B 2 36  ? 35.867  -65.333 -61.208  1.000 162.576 ? 36  LYS LLL CA  1 
ATOM 1871 C C   . LYS B 2 36  ? 34.351  -65.115 -61.160  1.000 156.829 ? 36  LYS LLL C   1 
ATOM 1872 O O   . LYS B 2 36  ? 33.685  -65.430 -62.112  1.000 153.713 ? 36  LYS LLL O   1 
ATOM 1873 C CB  . LYS B 2 36  ? 36.660  -64.079 -61.604  1.000 164.165 ? 36  LYS LLL CB  1 
ATOM 1874 C CG  . LYS B 2 36  ? 38.111  -64.274 -62.060  1.000 174.902 ? 36  LYS LLL CG  1 
ATOM 1875 C CD  . LYS B 2 36  ? 39.102  -64.986 -61.147  1.000 183.187 ? 36  LYS LLL CD  1 
ATOM 1876 C CE  . LYS B 2 36  ? 39.510  -64.203 -59.920  1.000 187.937 ? 36  LYS LLL CE  1 
ATOM 1877 N NZ  . LYS B 2 36  ? 40.568  -64.915 -59.163  1.000 190.699 ? 36  LYS LLL NZ  1 
ATOM 1878 N N   . ASN B 2 37  ? 33.839  -64.697 -60.009  1.000 159.139 ? 37  ASN LLL N   1 
ATOM 1879 C CA  . ASN B 2 37  ? 32.436  -64.263 -59.802  1.000 159.003 ? 37  ASN LLL CA  1 
ATOM 1880 C C   . ASN B 2 37  ? 32.351  -62.753 -60.053  1.000 161.011 ? 37  ASN LLL C   1 
ATOM 1881 O O   . ASN B 2 37  ? 33.206  -62.006 -59.524  1.000 163.754 ? 37  ASN LLL O   1 
ATOM 1882 C CB  . ASN B 2 37  ? 31.957  -64.584 -58.384  1.000 154.431 ? 37  ASN LLL CB  1 
ATOM 1883 C CG  . ASN B 2 37  ? 31.961  -66.060 -58.085  1.000 149.780 ? 37  ASN LLL CG  1 
ATOM 1884 O OD1 . ASN B 2 37  ? 30.892  -66.655 -58.037  1.000 152.237 ? 37  ASN LLL OD1 1 
ATOM 1885 N ND2 . ASN B 2 37  ? 33.138  -66.643 -57.914  1.000 145.364 ? 37  ASN LLL ND2 1 
ATOM 1886 N N   . TYR B 2 38  ? 31.340  -62.309 -60.803  1.000 158.659 ? 38  TYR LLL N   1 
ATOM 1887 C CA  . TYR B 2 38  ? 31.144  -60.885 -61.184  1.000 149.422 ? 38  TYR LLL CA  1 
ATOM 1888 C C   . TYR B 2 38  ? 30.157  -60.241 -60.206  1.000 150.009 ? 38  TYR LLL C   1 
ATOM 1889 O O   . TYR B 2 38  ? 28.979  -60.029 -60.552  1.000 158.265 ? 38  TYR LLL O   1 
ATOM 1890 C CB  . TYR B 2 38  ? 30.758  -60.817 -62.666  1.000 148.658 ? 38  TYR LLL CB  1 
ATOM 1891 C CG  . TYR B 2 38  ? 31.945  -60.927 -63.585  1.000 141.243 ? 38  TYR LLL CG  1 
ATOM 1892 C CD1 . TYR B 2 38  ? 32.281  -59.928 -64.473  1.000 139.585 ? 38  TYR LLL CD1 1 
ATOM 1893 C CD2 . TYR B 2 38  ? 32.792  -62.005 -63.488  1.000 142.631 ? 38  TYR LLL CD2 1 
ATOM 1894 C CE1 . TYR B 2 38  ? 33.410  -60.014 -65.266  1.000 142.673 ? 38  TYR LLL CE1 1 
ATOM 1895 C CE2 . TYR B 2 38  ? 33.920  -62.112 -64.273  1.000 145.363 ? 38  TYR LLL CE2 1 
ATOM 1896 C CZ  . TYR B 2 38  ? 34.231  -61.120 -65.170  1.000 144.459 ? 38  TYR LLL CZ  1 
ATOM 1897 O OH  . TYR B 2 38  ? 35.363  -61.299 -65.908  1.000 145.872 ? 38  TYR LLL OH  1 
ATOM 1898 N N   . LEU B 2 39  ? 30.623  -59.960 -58.988  1.000 155.846 ? 39  LEU LLL N   1 
ATOM 1899 C CA  . LEU B 2 39  ? 29.826  -59.269 -57.925  1.000 153.918 ? 39  LEU LLL CA  1 
ATOM 1900 C C   . LEU B 2 39  ? 30.751  -58.336 -57.128  1.000 136.795 ? 39  LEU LLL C   1 
ATOM 1901 O O   . LEU B 2 39  ? 31.927  -58.629 -57.008  1.000 132.881 ? 39  LEU LLL O   1 
ATOM 1902 C CB  . LEU B 2 39  ? 29.154  -60.308 -57.022  1.000 154.695 ? 39  LEU LLL CB  1 
ATOM 1903 C CG  . LEU B 2 39  ? 28.206  -59.719 -55.983  1.000 161.817 ? 39  LEU LLL CG  1 
ATOM 1904 C CD1 . LEU B 2 39  ? 26.975  -60.592 -55.841  1.000 166.199 ? 39  LEU LLL CD1 1 
ATOM 1905 C CD2 . LEU B 2 39  ? 28.886  -59.533 -54.630  1.000 172.288 ? 39  LEU LLL CD2 1 
ATOM 1906 N N   . ALA B 2 40  ? 30.257  -57.226 -56.624  1.000 123.157 ? 40  ALA LLL N   1 
ATOM 1907 C CA  . ALA B 2 40  ? 31.107  -56.206 -55.993  1.000 129.878 ? 40  ALA LLL CA  1 
ATOM 1908 C C   . ALA B 2 40  ? 30.339  -55.603 -54.825  1.000 148.080 ? 40  ALA LLL C   1 
ATOM 1909 O O   . ALA B 2 40  ? 29.102  -55.822 -54.756  1.000 159.022 ? 40  ALA LLL O   1 
ATOM 1910 C CB  . ALA B 2 40  ? 31.445  -55.131 -56.989  1.000 137.823 ? 40  ALA LLL CB  1 
ATOM 1911 N N   . TRP B 2 41  ? 31.051  -54.834 -53.992  1.000 154.438 ? 41  TRP LLL N   1 
ATOM 1912 C CA  . TRP B 2 41  ? 30.575  -54.295 -52.689  1.000 153.682 ? 41  TRP LLL CA  1 
ATOM 1913 C C   . TRP B 2 41  ? 30.870  -52.792 -52.635  1.000 147.740 ? 41  TRP LLL C   1 
ATOM 1914 O O   . TRP B 2 41  ? 32.060  -52.385 -52.766  1.000 141.419 ? 41  TRP LLL O   1 
ATOM 1915 C CB  . TRP B 2 41  ? 31.225  -55.067 -51.525  1.000 152.838 ? 41  TRP LLL CB  1 
ATOM 1916 C CG  . TRP B 2 41  ? 30.679  -56.451 -51.344  1.000 143.753 ? 41  TRP LLL CG  1 
ATOM 1917 C CD1 . TRP B 2 41  ? 31.190  -57.658 -51.758  1.000 143.107 ? 41  TRP LLL CD1 1 
ATOM 1918 C CD2 . TRP B 2 41  ? 29.444  -56.740 -50.702  1.000 134.283 ? 41  TRP LLL CD2 1 
ATOM 1919 N NE1 . TRP B 2 41  ? 30.344  -58.681 -51.421  1.000 139.186 ? 41  TRP LLL NE1 1 
ATOM 1920 C CE2 . TRP B 2 41  ? 29.265  -58.140 -50.774  1.000 138.724 ? 41  TRP LLL CE2 1 
ATOM 1921 C CE3 . TRP B 2 41  ? 28.499  -55.932 -50.067  1.000 138.325 ? 41  TRP LLL CE3 1 
ATOM 1922 C CZ2 . TRP B 2 41  ? 28.160  -58.756 -50.200  1.000 148.133 ? 41  TRP LLL CZ2 1 
ATOM 1923 C CZ3 . TRP B 2 41  ? 27.395  -56.541 -49.512  1.000 148.434 ? 41  TRP LLL CZ3 1 
ATOM 1924 C CH2 . TRP B 2 41  ? 27.237  -57.935 -49.578  1.000 154.874 ? 41  TRP LLL CH2 1 
ATOM 1925 N N   . TYR B 2 42  ? 29.824  -51.997 -52.445  1.000 142.515 ? 42  TYR LLL N   1 
ATOM 1926 C CA  . TYR B 2 42  ? 29.916  -50.519 -52.396  1.000 144.111 ? 42  TYR LLL CA  1 
ATOM 1927 C C   . TYR B 2 42  ? 29.558  -50.035 -50.982  1.000 135.314 ? 42  TYR LLL C   1 
ATOM 1928 O O   . TYR B 2 42  ? 28.596  -50.551 -50.356  1.000 134.941 ? 42  TYR LLL O   1 
ATOM 1929 C CB  . TYR B 2 42  ? 29.026  -49.880 -53.477  1.000 150.564 ? 42  TYR LLL CB  1 
ATOM 1930 C CG  . TYR B 2 42  ? 29.493  -50.045 -54.907  1.000 141.247 ? 42  TYR LLL CG  1 
ATOM 1931 C CD1 . TYR B 2 42  ? 28.960  -51.037 -55.726  1.000 137.356 ? 42  TYR LLL CD1 1 
ATOM 1932 C CD2 . TYR B 2 42  ? 30.469  -49.216 -55.441  1.000 129.499 ? 42  TYR LLL CD2 1 
ATOM 1933 C CE1 . TYR B 2 42  ? 29.388  -51.212 -57.029  1.000 129.320 ? 42  TYR LLL CE1 1 
ATOM 1934 C CE2 . TYR B 2 42  ? 30.894  -49.368 -56.747  1.000 126.119 ? 42  TYR LLL CE2 1 
ATOM 1935 C CZ  . TYR B 2 42  ? 30.356  -50.369 -57.530  1.000 126.552 ? 42  TYR LLL CZ  1 
ATOM 1936 O OH  . TYR B 2 42  ? 30.806  -50.540 -58.793  1.000 137.103 ? 42  TYR LLL OH  1 
ATOM 1937 N N   . GLN B 2 43  ? 30.336  -49.059 -50.508  1.000 130.883 ? 43  GLN LLL N   1 
ATOM 1938 C CA  . GLN B 2 43  ? 30.128  -48.305 -49.249  1.000 130.269 ? 43  GLN LLL CA  1 
ATOM 1939 C C   . GLN B 2 43  ? 29.704  -46.882 -49.616  1.000 133.636 ? 43  GLN LLL C   1 
ATOM 1940 O O   . GLN B 2 43  ? 30.428  -46.246 -50.419  1.000 134.052 ? 43  GLN LLL O   1 
ATOM 1941 C CB  . GLN B 2 43  ? 31.424  -48.292 -48.434  1.000 128.716 ? 43  GLN LLL CB  1 
ATOM 1942 C CG  . GLN B 2 43  ? 31.451  -47.200 -47.371  1.000 135.136 ? 43  GLN LLL CG  1 
ATOM 1943 C CD  . GLN B 2 43  ? 32.832  -46.874 -46.865  1.000 136.687 ? 43  GLN LLL CD  1 
ATOM 1944 O OE1 . GLN B 2 43  ? 33.552  -46.002 -47.409  1.000 122.217 ? 43  GLN LLL OE1 1 
ATOM 1945 N NE2 . GLN B 2 43  ? 33.150  -47.570 -45.778  1.000 134.989 ? 43  GLN LLL NE2 1 
ATOM 1946 N N   . GLN B 2 44  ? 28.598  -46.396 -49.043  1.000 144.226 ? 44  GLN LLL N   1 
ATOM 1947 C CA  . GLN B 2 44  ? 28.114  -44.994 -49.224  1.000 149.407 ? 44  GLN LLL CA  1 
ATOM 1948 C C   . GLN B 2 44  ? 27.757  -44.363 -47.868  1.000 141.109 ? 44  GLN LLL C   1 
ATOM 1949 O O   . GLN B 2 44  ? 26.876  -44.883 -47.114  1.000 129.524 ? 44  GLN LLL O   1 
ATOM 1950 C CB  . GLN B 2 44  ? 26.925  -44.934 -50.186  1.000 162.602 ? 44  GLN LLL CB  1 
ATOM 1951 C CG  . GLN B 2 44  ? 26.565  -43.517 -50.619  1.000 163.245 ? 44  GLN LLL CG  1 
ATOM 1952 C CD  . GLN B 2 44  ? 25.233  -43.473 -51.327  1.000 161.472 ? 44  GLN LLL CD  1 
ATOM 1953 O OE1 . GLN B 2 44  ? 25.130  -42.935 -52.422  1.000 154.216 ? 44  GLN LLL OE1 1 
ATOM 1954 N NE2 . GLN B 2 44  ? 24.206  -44.036 -50.701  1.000 158.341 ? 44  GLN LLL NE2 1 
ATOM 1955 N N   . LYS B 2 45  ? 28.441  -43.266 -47.575  1.000 136.185 ? 45  LYS LLL N   1 
ATOM 1956 C CA  . LYS B 2 45  ? 28.227  -42.472 -46.355  1.000 142.357 ? 45  LYS LLL CA  1 
ATOM 1957 C C   . LYS B 2 45  ? 27.337  -41.323 -46.791  1.000 150.257 ? 45  LYS LLL C   1 
ATOM 1958 O O   . LYS B 2 45  ? 27.335  -40.955 -47.955  1.000 161.711 ? 45  LYS LLL O   1 
ATOM 1959 C CB  . LYS B 2 45  ? 29.569  -42.075 -45.728  1.000 146.219 ? 45  LYS LLL CB  1 
ATOM 1960 C CG  . LYS B 2 45  ? 30.403  -43.234 -45.155  1.000 148.688 ? 45  LYS LLL CG  1 
ATOM 1961 C CD  . LYS B 2 45  ? 31.920  -43.056 -45.197  1.000 155.853 ? 45  LYS LLL CD  1 
ATOM 1962 C CE  . LYS B 2 45  ? 32.504  -42.230 -44.061  1.000 161.734 ? 45  LYS LLL CE  1 
ATOM 1963 N NZ  . LYS B 2 45  ? 33.466  -43.020 -43.253  1.000 172.855 ? 45  LYS LLL NZ  1 
ATOM 1964 N N   . PRO B 2 46  ? 26.536  -40.748 -45.882  1.000 155.777 ? 46  PRO LLL N   1 
ATOM 1965 C CA  . PRO B 2 46  ? 25.708  -39.591 -46.211  1.000 154.456 ? 46  PRO LLL CA  1 
ATOM 1966 C C   . PRO B 2 46  ? 26.499  -38.432 -46.825  1.000 149.111 ? 46  PRO LLL C   1 
ATOM 1967 O O   . PRO B 2 46  ? 27.431  -37.984 -46.213  1.000 144.884 ? 46  PRO LLL O   1 
ATOM 1968 C CB  . PRO B 2 46  ? 25.182  -39.176 -44.840  1.000 165.445 ? 46  PRO LLL CB  1 
ATOM 1969 C CG  . PRO B 2 46  ? 25.130  -40.483 -44.069  1.000 170.748 ? 46  PRO LLL CG  1 
ATOM 1970 C CD  . PRO B 2 46  ? 26.387  -41.198 -44.492  1.000 164.141 ? 46  PRO LLL CD  1 
ATOM 1971 N N   . GLY B 2 47  ? 26.110  -38.004 -48.025  1.000 151.990 ? 47  GLY LLL N   1 
ATOM 1972 C CA  . GLY B 2 47  ? 26.682  -36.836 -48.729  1.000 153.474 ? 47  GLY LLL CA  1 
ATOM 1973 C C   . GLY B 2 47  ? 27.957  -37.188 -49.469  1.000 144.914 ? 47  GLY LLL C   1 
ATOM 1974 O O   . GLY B 2 47  ? 28.782  -36.284 -49.714  1.000 142.672 ? 47  GLY LLL O   1 
ATOM 1975 N N   . GLN B 2 48  ? 28.102  -38.461 -49.816  1.000 138.098 ? 48  GLN LLL N   1 
ATOM 1976 C CA  . GLN B 2 48  ? 29.297  -38.994 -50.495  1.000 146.045 ? 48  GLN LLL CA  1 
ATOM 1977 C C   . GLN B 2 48  ? 28.875  -39.894 -51.655  1.000 145.846 ? 48  GLN LLL C   1 
ATOM 1978 O O   . GLN B 2 48  ? 27.859  -40.589 -51.627  1.000 147.754 ? 48  GLN LLL O   1 
ATOM 1979 C CB  . GLN B 2 48  ? 30.144  -39.781 -49.493  1.000 162.321 ? 48  GLN LLL CB  1 
ATOM 1980 C CG  . GLN B 2 48  ? 30.641  -38.956 -48.310  1.000 172.695 ? 48  GLN LLL CG  1 
ATOM 1981 C CD  . GLN B 2 48  ? 31.774  -39.567 -47.494  1.000 180.302 ? 48  GLN LLL CD  1 
ATOM 1982 O OE1 . GLN B 2 48  ? 32.430  -40.572 -47.838  1.000 170.420 ? 48  GLN LLL OE1 1 
ATOM 1983 N NE2 . GLN B 2 48  ? 32.046  -38.913 -46.374  1.000 188.396 ? 48  GLN LLL NE2 1 
ATOM 1984 N N   . PRO B 2 49  ? 29.687  -39.927 -52.720  1.000 140.070 ? 49  PRO LLL N   1 
ATOM 1985 C CA  . PRO B 2 49  ? 29.492  -40.894 -53.803  1.000 135.214 ? 49  PRO LLL CA  1 
ATOM 1986 C C   . PRO B 2 49  ? 29.749  -42.316 -53.330  1.000 127.445 ? 49  PRO LLL C   1 
ATOM 1987 O O   . PRO B 2 49  ? 30.536  -42.472 -52.413  1.000 139.471 ? 49  PRO LLL O   1 
ATOM 1988 C CB  . PRO B 2 49  ? 30.629  -40.510 -54.757  1.000 146.291 ? 49  PRO LLL CB  1 
ATOM 1989 C CG  . PRO B 2 49  ? 31.682  -39.862 -53.856  1.000 142.199 ? 49  PRO LLL CG  1 
ATOM 1990 C CD  . PRO B 2 49  ? 30.856  -39.051 -52.891  1.000 139.791 ? 49  PRO LLL CD  1 
ATOM 1991 N N   . PRO B 2 50  ? 29.143  -43.387 -53.894  1.000 124.375 ? 50  PRO LLL N   1 
ATOM 1992 C CA  . PRO B 2 50  ? 29.493  -44.770 -53.537  1.000 122.205 ? 50  PRO LLL CA  1 
ATOM 1993 C C   . PRO B 2 50  ? 30.976  -45.053 -53.723  1.000 119.297 ? 50  PRO LLL C   1 
ATOM 1994 O O   . PRO B 2 50  ? 31.520  -44.526 -54.642  1.000 138.568 ? 50  PRO LLL O   1 
ATOM 1995 C CB  . PRO B 2 50  ? 28.732  -45.631 -54.534  1.000 122.004 ? 50  PRO LLL CB  1 
ATOM 1996 C CG  . PRO B 2 50  ? 27.515  -44.778 -54.811  1.000 129.591 ? 50  PRO LLL CG  1 
ATOM 1997 C CD  . PRO B 2 50  ? 28.068  -43.359 -54.883  1.000 131.100 ? 50  PRO LLL CD  1 
ATOM 1998 N N   . LYS B 2 51  ? 31.596  -45.781 -52.803  1.000 115.785 ? 51  LYS LLL N   1 
ATOM 1999 C CA  . LYS B 2 51  ? 33.023  -46.154 -52.921  1.000 118.052 ? 51  LYS LLL CA  1 
ATOM 2000 C C   . LYS B 2 51  ? 33.063  -47.666 -53.163  1.000 127.413 ? 51  LYS LLL C   1 
ATOM 2001 O O   . LYS B 2 51  ? 32.417  -48.437 -52.429  1.000 137.910 ? 51  LYS LLL O   1 
ATOM 2002 C CB  . LYS B 2 51  ? 33.844  -45.688 -51.711  1.000 113.357 ? 51  LYS LLL CB  1 
ATOM 2003 C CG  . LYS B 2 51  ? 35.145  -46.446 -51.437  1.000 109.958 ? 51  LYS LLL CG  1 
ATOM 2004 C CD  . LYS B 2 51  ? 36.127  -45.674 -50.578  1.000 112.571 ? 51  LYS LLL CD  1 
ATOM 2005 C CE  . LYS B 2 51  ? 37.561  -46.151 -50.727  1.000 120.828 ? 51  LYS LLL CE  1 
ATOM 2006 N NZ  . LYS B 2 51  ? 38.578  -45.254 -50.099  1.000 123.382 ? 51  LYS LLL NZ  1 
ATOM 2007 N N   . LEU B 2 52  ? 33.795  -48.072 -54.187  1.000 129.302 ? 52  LEU LLL N   1 
ATOM 2008 C CA  . LEU B 2 52  ? 34.077  -49.489 -54.435  1.000 129.640 ? 52  LEU LLL CA  1 
ATOM 2009 C C   . LEU B 2 52  ? 35.058  -49.950 -53.347  1.000 128.020 ? 52  LEU LLL C   1 
ATOM 2010 O O   . LEU B 2 52  ? 36.115  -49.273 -53.171  1.000 121.403 ? 52  LEU LLL O   1 
ATOM 2011 C CB  . LEU B 2 52  ? 34.653  -49.603 -55.853  1.000 134.002 ? 52  LEU LLL CB  1 
ATOM 2012 C CG  . LEU B 2 52  ? 34.851  -51.021 -56.394  1.000 134.187 ? 52  LEU LLL CG  1 
ATOM 2013 C CD1 . LEU B 2 52  ? 33.531  -51.764 -56.568  1.000 136.521 ? 52  LEU LLL CD1 1 
ATOM 2014 C CD2 . LEU B 2 52  ? 35.577  -50.962 -57.699  1.000 130.923 ? 52  LEU LLL CD2 1 
ATOM 2015 N N   . LEU B 2 53  ? 34.710  -51.033 -52.638  1.000 124.083 ? 53  LEU LLL N   1 
ATOM 2016 C CA  . LEU B 2 53  ? 35.610  -51.745 -51.684  1.000 123.224 ? 53  LEU LLL CA  1 
ATOM 2017 C C   . LEU B 2 53  ? 36.050  -53.068 -52.300  1.000 125.544 ? 53  LEU LLL C   1 
ATOM 2018 O O   . LEU B 2 53  ? 37.246  -53.310 -52.277  1.000 128.622 ? 53  LEU LLL O   1 
ATOM 2019 C CB  . LEU B 2 53  ? 34.910  -52.056 -50.361  1.000 130.092 ? 53  LEU LLL CB  1 
ATOM 2020 C CG  . LEU B 2 53  ? 34.247  -50.870 -49.684  1.000 136.689 ? 53  LEU LLL CG  1 
ATOM 2021 C CD1 . LEU B 2 53  ? 33.282  -51.366 -48.595  1.000 137.565 ? 53  LEU LLL CD1 1 
ATOM 2022 C CD2 . LEU B 2 53  ? 35.320  -49.906 -49.173  1.000 132.254 ? 53  LEU LLL CD2 1 
ATOM 2023 N N   . ILE B 2 54  ? 35.124  -53.911 -52.769  1.000 125.273 ? 54  ILE LLL N   1 
ATOM 2024 C CA  . ILE B 2 54  ? 35.445  -55.289 -53.249  1.000 129.545 ? 54  ILE LLL CA  1 
ATOM 2025 C C   . ILE B 2 54  ? 34.886  -55.449 -54.654  1.000 132.580 ? 54  ILE LLL C   1 
ATOM 2026 O O   . ILE B 2 54  ? 33.729  -55.025 -54.852  1.000 122.535 ? 54  ILE LLL O   1 
ATOM 2027 C CB  . ILE B 2 54  ? 34.851  -56.378 -52.335  1.000 129.254 ? 54  ILE LLL CB  1 
ATOM 2028 C CG1 . ILE B 2 54  ? 35.279  -56.200 -50.875  1.000 124.982 ? 54  ILE LLL CG1 1 
ATOM 2029 C CG2 . ILE B 2 54  ? 35.179  -57.762 -52.882  1.000 126.792 ? 54  ILE LLL CG2 1 
ATOM 2030 C CD1 . ILE B 2 54  ? 36.762  -56.074 -50.686  1.000 121.001 ? 54  ILE LLL CD1 1 
ATOM 2031 N N   . TYR B 2 55  ? 35.681  -56.046 -55.552  1.000 139.563 ? 55  TYR LLL N   1 
ATOM 2032 C CA  . TYR B 2 55  ? 35.258  -56.574 -56.880  1.000 137.964 ? 55  TYR LLL CA  1 
ATOM 2033 C C   . TYR B 2 55  ? 35.735  -58.011 -57.060  1.000 136.848 ? 55  TYR LLL C   1 
ATOM 2034 O O   . TYR B 2 55  ? 36.565  -58.475 -56.308  1.000 146.897 ? 55  TYR LLL O   1 
ATOM 2035 C CB  . TYR B 2 55  ? 35.758  -55.760 -58.070  1.000 124.894 ? 55  TYR LLL CB  1 
ATOM 2036 C CG  . TYR B 2 55  ? 37.237  -55.562 -58.152  1.000 115.797 ? 55  TYR LLL CG  1 
ATOM 2037 C CD1 . TYR B 2 55  ? 37.782  -54.398 -57.662  1.000 121.676 ? 55  TYR LLL CD1 1 
ATOM 2038 C CD2 . TYR B 2 55  ? 38.079  -56.481 -58.728  1.000 115.365 ? 55  TYR LLL CD2 1 
ATOM 2039 C CE1 . TYR B 2 55  ? 39.136  -54.121 -57.755  1.000 124.011 ? 55  TYR LLL CE1 1 
ATOM 2040 C CE2 . TYR B 2 55  ? 39.442  -56.233 -58.812  1.000 124.329 ? 55  TYR LLL CE2 1 
ATOM 2041 C CZ  . TYR B 2 55  ? 39.980  -55.054 -58.316  1.000 124.157 ? 55  TYR LLL CZ  1 
ATOM 2042 O OH  . TYR B 2 55  ? 41.312  -54.756 -58.374  1.000 129.164 ? 55  TYR LLL OH  1 
ATOM 2043 N N   . TRP B 2 56  ? 35.165  -58.686 -58.045  1.000 137.979 ? 56  TRP LLL N   1 
ATOM 2044 C CA  . TRP B 2 56  ? 35.287  -60.141 -58.255  1.000 140.732 ? 56  TRP LLL CA  1 
ATOM 2045 C C   . TRP B 2 56  ? 34.971  -60.885 -56.965  1.000 140.615 ? 56  TRP LLL C   1 
ATOM 2046 O O   . TRP B 2 56  ? 35.645  -61.876 -56.704  1.000 139.142 ? 56  TRP LLL O   1 
ATOM 2047 C CB  . TRP B 2 56  ? 36.679  -60.461 -58.790  1.000 148.377 ? 56  TRP LLL CB  1 
ATOM 2048 C CG  . TRP B 2 56  ? 36.738  -60.367 -60.279  1.000 150.660 ? 56  TRP LLL CG  1 
ATOM 2049 C CD1 . TRP B 2 56  ? 35.686  -60.419 -61.140  1.000 155.539 ? 56  TRP LLL CD1 1 
ATOM 2050 C CD2 . TRP B 2 56  ? 37.915  -60.250 -61.091  1.000 149.607 ? 56  TRP LLL CD2 1 
ATOM 2051 N NE1 . TRP B 2 56  ? 36.124  -60.311 -62.426  1.000 163.694 ? 56  TRP LLL NE1 1 
ATOM 2052 C CE2 . TRP B 2 56  ? 37.485  -60.216 -62.431  1.000 155.433 ? 56  TRP LLL CE2 1 
ATOM 2053 C CE3 . TRP B 2 56  ? 39.281  -60.173 -60.818  1.000 147.272 ? 56  TRP LLL CE3 1 
ATOM 2054 C CZ2 . TRP B 2 56  ? 38.370  -60.119 -63.499  1.000 152.196 ? 56  TRP LLL CZ2 1 
ATOM 2055 C CZ3 . TRP B 2 56  ? 40.158  -60.077 -61.869  1.000 149.364 ? 56  TRP LLL CZ3 1 
ATOM 2056 C CH2 . TRP B 2 56  ? 39.706  -60.045 -63.190  1.000 152.159 ? 56  TRP LLL CH2 1 
ATOM 2057 N N   . ALA B 2 57  ? 33.998  -60.387 -56.194  1.000 145.652 ? 57  ALA LLL N   1 
ATOM 2058 C CA  . ALA B 2 57  ? 33.413  -60.994 -54.964  1.000 150.990 ? 57  ALA LLL CA  1 
ATOM 2059 C C   . ALA B 2 57  ? 34.378  -60.908 -53.784  1.000 145.187 ? 57  ALA LLL C   1 
ATOM 2060 O O   . ALA B 2 57  ? 33.864  -60.754 -52.660  1.000 147.934 ? 57  ALA LLL O   1 
ATOM 2061 C CB  . ALA B 2 57  ? 33.005  -62.421 -55.207  1.000 154.098 ? 57  ALA LLL CB  1 
ATOM 2062 N N   . SER B 2 58  ? 35.687  -60.993 -54.048  1.000 139.865 ? 58  SER LLL N   1 
ATOM 2063 C CA  . SER B 2 58  ? 36.740  -61.287 -53.051  1.000 139.539 ? 58  SER LLL CA  1 
ATOM 2064 C C   . SER B 2 58  ? 38.021  -60.454 -53.236  1.000 137.272 ? 58  SER LLL C   1 
ATOM 2065 O O   . SER B 2 58  ? 38.923  -60.597 -52.428  1.000 149.157 ? 58  SER LLL O   1 
ATOM 2066 C CB  . SER B 2 58  ? 37.024  -62.785 -53.062  1.000 147.342 ? 58  SER LLL CB  1 
ATOM 2067 O OG  . SER B 2 58  ? 38.139  -63.131 -53.881  1.000 146.545 ? 58  SER LLL OG  1 
ATOM 2068 N N   . THR B 2 59  ? 38.160  -59.604 -54.246  1.000 139.644 ? 59  THR LLL N   1 
ATOM 2069 C CA  . THR B 2 59  ? 39.405  -58.801 -54.439  1.000 134.119 ? 59  THR LLL CA  1 
ATOM 2070 C C   . THR B 2 59  ? 39.164  -57.390 -53.886  1.000 131.975 ? 59  THR LLL C   1 
ATOM 2071 O O   . THR B 2 59  ? 38.125  -56.773 -54.209  1.000 129.938 ? 59  THR LLL O   1 
ATOM 2072 C CB  . THR B 2 59  ? 39.858  -58.797 -55.906  1.000 132.600 ? 59  THR LLL CB  1 
ATOM 2073 O OG1 . THR B 2 59  ? 40.127  -60.138 -56.328  1.000 128.686 ? 59  THR LLL OG1 1 
ATOM 2074 C CG2 . THR B 2 59  ? 41.073  -57.926 -56.154  1.000 132.375 ? 59  THR LLL CG2 1 
ATOM 2075 N N   . ARG B 2 60  ? 40.086  -56.904 -53.061  1.000 134.514 ? 60  ARG LLL N   1 
ATOM 2076 C CA  . ARG B 2 60  ? 39.960  -55.592 -52.374  1.000 135.706 ? 60  ARG LLL CA  1 
ATOM 2077 C C   . ARG B 2 60  ? 40.353  -54.527 -53.392  1.000 129.468 ? 60  ARG LLL C   1 
ATOM 2078 O O   . ARG B 2 60  ? 41.182  -54.820 -54.234  1.000 141.742 ? 60  ARG LLL O   1 
ATOM 2079 C CB  . ARG B 2 60  ? 40.853  -55.574 -51.128  1.000 140.336 ? 60  ARG LLL CB  1 
ATOM 2080 C CG  . ARG B 2 60  ? 40.449  -54.590 -50.035  1.000 137.647 ? 60  ARG LLL CG  1 
ATOM 2081 C CD  . ARG B 2 60  ? 41.480  -54.398 -48.920  1.000 138.239 ? 60  ARG LLL CD  1 
ATOM 2082 N NE  . ARG B 2 60  ? 42.441  -55.489 -48.790  1.000 140.156 ? 60  ARG LLL NE  1 
ATOM 2083 C CZ  . ARG B 2 60  ? 42.159  -56.703 -48.319  1.000 151.764 ? 60  ARG LLL CZ  1 
ATOM 2084 N NH1 . ARG B 2 60  ? 40.929  -57.010 -47.933  1.000 157.386 ? 60  ARG LLL NH1 1 
ATOM 2085 N NH2 . ARG B 2 60  ? 43.110  -57.617 -48.248  1.000 159.983 ? 60  ARG LLL NH2 1 
ATOM 2086 N N   . GLU B 2 61  ? 39.746  -53.353 -53.344  1.000 127.178 ? 61  GLU LLL N   1 
ATOM 2087 C CA  . GLU B 2 61  ? 40.037  -52.245 -54.286  1.000 134.209 ? 61  GLU LLL CA  1 
ATOM 2088 C C   . GLU B 2 61  ? 41.153  -51.421 -53.644  1.000 134.453 ? 61  GLU LLL C   1 
ATOM 2089 O O   . GLU B 2 61  ? 41.325  -51.510 -52.434  1.000 138.764 ? 61  GLU LLL O   1 
ATOM 2090 C CB  . GLU B 2 61  ? 38.739  -51.486 -54.582  1.000 140.179 ? 61  GLU LLL CB  1 
ATOM 2091 C CG  . GLU B 2 61  ? 38.904  -50.131 -55.238  1.000 152.991 ? 61  GLU LLL CG  1 
ATOM 2092 C CD  . GLU B 2 61  ? 39.273  -50.116 -56.714  1.000 163.001 ? 61  GLU LLL CD  1 
ATOM 2093 O OE1 . GLU B 2 61  ? 38.726  -49.237 -57.434  1.000 162.187 ? 61  GLU LLL OE1 1 
ATOM 2094 O OE2 . GLU B 2 61  ? 40.123  -50.945 -57.139  1.000 182.293 ? 61  GLU LLL OE2 1 
ATOM 2095 N N   . SER B 2 62  ? 41.921  -50.678 -54.424  1.000 139.245 ? 62  SER LLL N   1 
ATOM 2096 C CA  . SER B 2 62  ? 42.975  -49.787 -53.883  1.000 146.819 ? 62  SER LLL CA  1 
ATOM 2097 C C   . SER B 2 62  ? 42.367  -48.865 -52.809  1.000 143.116 ? 62  SER LLL C   1 
ATOM 2098 O O   . SER B 2 62  ? 41.190  -48.434 -52.982  1.000 130.442 ? 62  SER LLL O   1 
ATOM 2099 C CB  . SER B 2 62  ? 43.664  -49.025 -55.004  1.000 165.509 ? 62  SER LLL CB  1 
ATOM 2100 O OG  . SER B 2 62  ? 42.749  -48.275 -55.800  1.000 181.192 ? 62  SER LLL OG  1 
ATOM 2101 N N   . GLY B 2 63  ? 43.117  -48.624 -51.715  1.000 147.620 ? 63  GLY LLL N   1 
ATOM 2102 C CA  . GLY B 2 63  ? 42.837  -47.602 -50.668  1.000 150.033 ? 63  GLY LLL CA  1 
ATOM 2103 C C   . GLY B 2 63  ? 41.696  -47.989 -49.727  1.000 141.254 ? 63  GLY LLL C   1 
ATOM 2104 O O   . GLY B 2 63  ? 40.988  -47.061 -49.144  1.000 118.484 ? 63  GLY LLL O   1 
ATOM 2105 N N   . VAL B 2 64  ? 41.499  -49.308 -49.633  1.000 133.640 ? 64  VAL LLL N   1 
ATOM 2106 C CA  . VAL B 2 64  ? 40.463  -49.968 -48.802  1.000 135.346 ? 64  VAL LLL CA  1 
ATOM 2107 C C   . VAL B 2 64  ? 41.225  -50.684 -47.696  1.000 145.311 ? 64  VAL LLL C   1 
ATOM 2108 O O   . VAL B 2 64  ? 42.193  -51.397 -47.969  1.000 135.724 ? 64  VAL LLL O   1 
ATOM 2109 C CB  . VAL B 2 64  ? 39.594  -50.936 -49.617  1.000 129.830 ? 64  VAL LLL CB  1 
ATOM 2110 C CG1 . VAL B 2 64  ? 38.688  -51.746 -48.738  1.000 132.097 ? 64  VAL LLL CG1 1 
ATOM 2111 C CG2 . VAL B 2 64  ? 38.744  -50.191 -50.613  1.000 137.831 ? 64  VAL LLL CG2 1 
ATOM 2112 N N   . PRO B 2 65  ? 40.810  -50.494 -46.419  1.000 146.537 ? 65  PRO LLL N   1 
ATOM 2113 C CA  . PRO B 2 65  ? 41.526  -51.078 -45.295  1.000 139.854 ? 65  PRO LLL CA  1 
ATOM 2114 C C   . PRO B 2 65  ? 41.412  -52.599 -45.280  1.000 145.532 ? 65  PRO LLL C   1 
ATOM 2115 O O   . PRO B 2 65  ? 40.453  -53.112 -45.813  1.000 130.922 ? 65  PRO LLL O   1 
ATOM 2116 C CB  . PRO B 2 65  ? 40.832  -50.508 -44.075  1.000 144.148 ? 65  PRO LLL CB  1 
ATOM 2117 C CG  . PRO B 2 65  ? 40.057  -49.309 -44.609  1.000 144.160 ? 65  PRO LLL CG  1 
ATOM 2118 C CD  . PRO B 2 65  ? 39.641  -49.703 -45.996  1.000 142.367 ? 65  PRO LLL CD  1 
ATOM 2119 N N   . ASP B 2 66  ? 42.440  -53.227 -44.701  1.000 163.302 ? 66  ASP LLL N   1 
ATOM 2120 C CA  . ASP B 2 66  ? 42.696  -54.692 -44.585  1.000 166.198 ? 66  ASP LLL CA  1 
ATOM 2121 C C   . ASP B 2 66  ? 41.456  -55.431 -44.040  1.000 155.841 ? 66  ASP LLL C   1 
ATOM 2122 O O   . ASP B 2 66  ? 41.189  -56.530 -44.528  1.000 146.095 ? 66  ASP LLL O   1 
ATOM 2123 C CB  . ASP B 2 66  ? 43.920  -54.923 -43.691  1.000 189.541 ? 66  ASP LLL CB  1 
ATOM 2124 C CG  . ASP B 2 66  ? 43.896  -54.106 -42.397  1.000 222.265 ? 66  ASP LLL CG  1 
ATOM 2125 O OD1 . ASP B 2 66  ? 43.471  -54.655 -41.348  1.000 241.056 ? 66  ASP LLL OD1 1 
ATOM 2126 O OD2 . ASP B 2 66  ? 44.303  -52.916 -42.438  1.000 250.442 ? 66  ASP LLL OD2 1 
ATOM 2127 N N   . ARG B 2 67  ? 40.734  -54.844 -43.077  1.000 147.551 ? 67  ARG LLL N   1 
ATOM 2128 C CA  . ARG B 2 67  ? 39.669  -55.497 -42.268  1.000 146.533 ? 67  ARG LLL CA  1 
ATOM 2129 C C   . ARG B 2 67  ? 38.467  -55.892 -43.136  1.000 141.995 ? 67  ARG LLL C   1 
ATOM 2130 O O   . ARG B 2 67  ? 37.713  -56.810 -42.723  1.000 142.272 ? 67  ARG LLL O   1 
ATOM 2131 C CB  . ARG B 2 67  ? 39.244  -54.546 -41.140  1.000 150.215 ? 67  ARG LLL CB  1 
ATOM 2132 C CG  . ARG B 2 67  ? 38.984  -53.106 -41.560  1.000 143.112 ? 67  ARG LLL CG  1 
ATOM 2133 C CD  . ARG B 2 67  ? 38.292  -52.391 -40.422  1.000 145.749 ? 67  ARG LLL CD  1 
ATOM 2134 N NE  . ARG B 2 67  ? 38.009  -50.979 -40.638  1.000 141.708 ? 67  ARG LLL NE  1 
ATOM 2135 C CZ  . ARG B 2 67  ? 38.920  -50.007 -40.583  1.000 142.953 ? 67  ARG LLL CZ  1 
ATOM 2136 N NH1 . ARG B 2 67  ? 40.196  -50.285 -40.372  1.000 152.042 ? 67  ARG LLL NH1 1 
ATOM 2137 N NH2 . ARG B 2 67  ? 38.558  -48.751 -40.768  1.000 136.527 ? 67  ARG LLL NH2 1 
ATOM 2138 N N   . PHE B 2 68  ? 38.278  -55.184 -44.261  1.000 135.822 ? 68  PHE LLL N   1 
ATOM 2139 C CA  . PHE B 2 68  ? 37.221  -55.416 -45.271  1.000 122.345 ? 68  PHE LLL CA  1 
ATOM 2140 C C   . PHE B 2 68  ? 37.592  -56.613 -46.099  1.000 121.520 ? 68  PHE LLL C   1 
ATOM 2141 O O   . PHE B 2 68  ? 38.679  -56.699 -46.604  1.000 122.475 ? 68  PHE LLL O   1 
ATOM 2142 C CB  . PHE B 2 68  ? 37.096  -54.256 -46.233  1.000 115.214 ? 68  PHE LLL CB  1 
ATOM 2143 C CG  . PHE B 2 68  ? 36.316  -53.140 -45.628  1.000 117.398 ? 68  PHE LLL CG  1 
ATOM 2144 C CD1 . PHE B 2 68  ? 36.970  -52.072 -45.034  1.000 119.163 ? 68  PHE LLL CD1 1 
ATOM 2145 C CD2 . PHE B 2 68  ? 34.935  -53.211 -45.586  1.000 118.437 ? 68  PHE LLL CD2 1 
ATOM 2146 C CE1 . PHE B 2 68  ? 36.244  -51.050 -44.444  1.000 120.806 ? 68  PHE LLL CE1 1 
ATOM 2147 C CE2 . PHE B 2 68  ? 34.206  -52.194 -44.994  1.000 121.126 ? 68  PHE LLL CE2 1 
ATOM 2148 C CZ  . PHE B 2 68  ? 34.865  -51.116 -44.426  1.000 124.266 ? 68  PHE LLL CZ  1 
ATOM 2149 N N   . SER B 2 69  ? 36.677  -57.527 -46.216  1.000 130.865 ? 69  SER LLL N   1 
ATOM 2150 C CA  . SER B 2 69  ? 36.982  -58.798 -46.882  1.000 149.111 ? 69  SER LLL CA  1 
ATOM 2151 C C   . SER B 2 69  ? 35.698  -59.304 -47.515  1.000 158.555 ? 69  SER LLL C   1 
ATOM 2152 O O   . SER B 2 69  ? 34.674  -59.306 -46.803  1.000 189.792 ? 69  SER LLL O   1 
ATOM 2153 C CB  . SER B 2 69  ? 37.537  -59.724 -45.865  1.000 165.772 ? 69  SER LLL CB  1 
ATOM 2154 O OG  . SER B 2 69  ? 37.312  -61.062 -46.242  1.000 197.186 ? 69  SER LLL OG  1 
ATOM 2155 N N   . GLY B 2 70  ? 35.736  -59.657 -48.799  1.000 150.716 ? 70  GLY LLL N   1 
ATOM 2156 C CA  . GLY B 2 70  ? 34.555  -60.173 -49.517  1.000 148.796 ? 70  GLY LLL CA  1 
ATOM 2157 C C   . GLY B 2 70  ? 34.752  -61.638 -49.813  1.000 147.942 ? 70  GLY LLL C   1 
ATOM 2158 O O   . GLY B 2 70  ? 35.928  -62.011 -50.018  1.000 137.023 ? 70  GLY LLL O   1 
ATOM 2159 N N   . SER B 2 71  ? 33.681  -62.435 -49.830  1.000 148.497 ? 71  SER LLL N   1 
ATOM 2160 C CA  . SER B 2 71  ? 33.773  -63.891 -50.105  1.000 154.294 ? 71  SER LLL CA  1 
ATOM 2161 C C   . SER B 2 71  ? 32.449  -64.397 -50.677  1.000 149.763 ? 71  SER LLL C   1 
ATOM 2162 O O   . SER B 2 71  ? 31.601  -63.567 -50.990  1.000 142.476 ? 71  SER LLL O   1 
ATOM 2163 C CB  . SER B 2 71  ? 34.188  -64.631 -48.864  1.000 166.938 ? 71  SER LLL CB  1 
ATOM 2164 O OG  . SER B 2 71  ? 33.405  -64.212 -47.748  1.000 180.904 ? 71  SER LLL OG  1 
ATOM 2165 N N   . GLY B 2 72  ? 32.330  -65.709 -50.864  1.000 153.210 ? 72  GLY LLL N   1 
ATOM 2166 C CA  . GLY B 2 72  ? 31.156  -66.371 -51.460  1.000 157.151 ? 72  GLY LLL CA  1 
ATOM 2167 C C   . GLY B 2 72  ? 31.444  -66.878 -52.865  1.000 156.942 ? 72  GLY LLL C   1 
ATOM 2168 O O   . GLY B 2 72  ? 32.484  -66.510 -53.408  1.000 149.082 ? 72  GLY LLL O   1 
ATOM 2169 N N   . SER B 2 73  ? 30.567  -67.735 -53.398  1.000 166.137 ? 73  SER LLL N   1 
ATOM 2170 C CA  . SER B 2 73  ? 30.570  -68.250 -54.793  1.000 173.811 ? 73  SER LLL CA  1 
ATOM 2171 C C   . SER B 2 73  ? 29.147  -68.640 -55.193  1.000 184.598 ? 73  SER LLL C   1 
ATOM 2172 O O   . SER B 2 73  ? 28.321  -68.899 -54.298  1.000 191.622 ? 73  SER LLL O   1 
ATOM 2173 C CB  . SER B 2 73  ? 31.512  -69.422 -54.989  1.000 176.332 ? 73  SER LLL CB  1 
ATOM 2174 O OG  . SER B 2 73  ? 31.581  -69.813 -56.364  1.000 171.296 ? 73  SER LLL OG  1 
ATOM 2175 N N   . GLY B 2 74  ? 28.893  -68.646 -56.501  1.000 196.437 ? 74  GLY LLL N   1 
ATOM 2176 C CA  . GLY B 2 74  ? 27.617  -69.047 -57.122  1.000 201.878 ? 74  GLY LLL CA  1 
ATOM 2177 C C   . GLY B 2 74  ? 26.543  -67.986 -56.956  1.000 200.314 ? 74  GLY LLL C   1 
ATOM 2178 O O   . GLY B 2 74  ? 26.426  -67.111 -57.827  1.000 195.802 ? 74  GLY LLL O   1 
ATOM 2179 N N   . THR B 2 75  ? 25.790  -68.083 -55.865  1.000 201.604 ? 75  THR LLL N   1 
ATOM 2180 C CA  . THR B 2 75  ? 24.507  -67.383 -55.629  1.000 199.659 ? 75  THR LLL CA  1 
ATOM 2181 C C   . THR B 2 75  ? 24.572  -66.636 -54.305  1.000 191.985 ? 75  THR LLL C   1 
ATOM 2182 O O   . THR B 2 75  ? 23.875  -65.636 -54.178  1.000 184.150 ? 75  THR LLL O   1 
ATOM 2183 C CB  . THR B 2 75  ? 23.359  -68.397 -55.604  1.000 211.844 ? 75  THR LLL CB  1 
ATOM 2184 O OG1 . THR B 2 75  ? 23.525  -69.248 -56.737  1.000 224.536 ? 75  THR LLL OG1 1 
ATOM 2185 C CG2 . THR B 2 75  ? 21.983  -67.775 -55.652  1.000 212.798 ? 75  THR LLL CG2 1 
ATOM 2186 N N   . ASP B 2 76  ? 25.351  -67.136 -53.348  1.000 191.432 ? 76  ASP LLL N   1 
ATOM 2187 C CA  . ASP B 2 76  ? 25.466  -66.541 -51.996  1.000 196.289 ? 76  ASP LLL CA  1 
ATOM 2188 C C   . ASP B 2 76  ? 26.847  -65.918 -51.865  1.000 190.711 ? 76  ASP LLL C   1 
ATOM 2189 O O   . ASP B 2 76  ? 27.820  -66.609 -52.209  1.000 184.984 ? 76  ASP LLL O   1 
ATOM 2190 C CB  . ASP B 2 76  ? 25.232  -67.607 -50.935  1.000 206.192 ? 76  ASP LLL CB  1 
ATOM 2191 C CG  . ASP B 2 76  ? 23.923  -68.328 -51.166  1.000 217.971 ? 76  ASP LLL CG  1 
ATOM 2192 O OD1 . ASP B 2 76  ? 23.922  -69.305 -51.954  1.000 225.418 ? 76  ASP LLL OD1 1 
ATOM 2193 O OD2 . ASP B 2 76  ? 22.911  -67.875 -50.591  1.000 221.006 ? 76  ASP LLL OD2 1 
ATOM 2194 N N   . PHE B 2 77  ? 26.902  -64.659 -51.425  1.000 188.008 ? 77  PHE LLL N   1 
ATOM 2195 C CA  . PHE B 2 77  ? 28.154  -63.917 -51.137  1.000 188.608 ? 77  PHE LLL CA  1 
ATOM 2196 C C   . PHE B 2 77  ? 27.992  -63.197 -49.793  1.000 186.179 ? 77  PHE LLL C   1 
ATOM 2197 O O   . PHE B 2 77  ? 26.846  -62.973 -49.357  1.000 189.989 ? 77  PHE LLL O   1 
ATOM 2198 C CB  . PHE B 2 77  ? 28.498  -62.963 -52.290  1.000 195.420 ? 77  PHE LLL CB  1 
ATOM 2199 C CG  . PHE B 2 77  ? 28.510  -63.589 -53.664  1.000 197.439 ? 77  PHE LLL CG  1 
ATOM 2200 C CD1 . PHE B 2 77  ? 29.688  -64.050 -54.232  1.000 197.464 ? 77  PHE LLL CD1 1 
ATOM 2201 C CD2 . PHE B 2 77  ? 27.338  -63.729 -54.389  1.000 200.044 ? 77  PHE LLL CD2 1 
ATOM 2202 C CE1 . PHE B 2 77  ? 29.689  -64.651 -55.480  1.000 194.992 ? 77  PHE LLL CE1 1 
ATOM 2203 C CE2 . PHE B 2 77  ? 27.343  -64.316 -55.644  1.000 200.942 ? 77  PHE LLL CE2 1 
ATOM 2204 C CZ  . PHE B 2 77  ? 28.517  -64.781 -56.184  1.000 198.190 ? 77  PHE LLL CZ  1 
ATOM 2205 N N   . THR B 2 78  ? 29.116  -62.851 -49.160  1.000 182.922 ? 78  THR LLL N   1 
ATOM 2206 C CA  . THR B 2 78  ? 29.188  -62.142 -47.855  1.000 177.994 ? 78  THR LLL CA  1 
ATOM 2207 C C   . THR B 2 78  ? 30.315  -61.105 -47.905  1.000 167.966 ? 78  THR LLL C   1 
ATOM 2208 O O   . THR B 2 78  ? 31.316  -61.366 -48.610  1.000 170.237 ? 78  THR LLL O   1 
ATOM 2209 C CB  . THR B 2 78  ? 29.398  -63.146 -46.716  1.000 187.323 ? 78  THR LLL CB  1 
ATOM 2210 O OG1 . THR B 2 78  ? 30.782  -63.496 -46.733  1.000 191.193 ? 78  THR LLL OG1 1 
ATOM 2211 C CG2 . THR B 2 78  ? 28.535  -64.387 -46.841  1.000 187.644 ? 78  THR LLL CG2 1 
ATOM 2212 N N   . LEU B 2 79  ? 30.147  -59.969 -47.221  1.000 160.193 ? 79  LEU LLL N   1 
ATOM 2213 C CA  . LEU B 2 79  ? 31.228  -58.967 -46.988  1.000 157.410 ? 79  LEU LLL CA  1 
ATOM 2214 C C   . LEU B 2 79  ? 31.383  -58.788 -45.485  1.000 162.213 ? 79  LEU LLL C   1 
ATOM 2215 O O   . LEU B 2 79  ? 30.454  -58.263 -44.869  1.000 168.083 ? 79  LEU LLL O   1 
ATOM 2216 C CB  . LEU B 2 79  ? 30.912  -57.618 -47.640  1.000 145.886 ? 79  LEU LLL CB  1 
ATOM 2217 C CG  . LEU B 2 79  ? 31.687  -56.417 -47.084  1.000 140.379 ? 79  LEU LLL CG  1 
ATOM 2218 C CD1 . LEU B 2 79  ? 33.087  -56.328 -47.666  1.000 141.546 ? 79  LEU LLL CD1 1 
ATOM 2219 C CD2 . LEU B 2 79  ? 30.949  -55.123 -47.376  1.000 145.497 ? 79  LEU LLL CD2 1 
ATOM 2220 N N   . THR B 2 80  ? 32.536  -59.171 -44.945  1.000 164.417 ? 80  THR LLL N   1 
ATOM 2221 C CA  . THR B 2 80  ? 32.795  -59.202 -43.491  1.000 160.911 ? 80  THR LLL CA  1 
ATOM 2222 C C   . THR B 2 80  ? 33.825  -58.130 -43.130  1.000 148.347 ? 80  THR LLL C   1 
ATOM 2223 O O   . THR B 2 80  ? 34.946  -58.156 -43.630  1.000 133.391 ? 80  THR LLL O   1 
ATOM 2224 C CB  . THR B 2 80  ? 33.168  -60.626 -43.097  1.000 172.652 ? 80  THR LLL CB  1 
ATOM 2225 O OG1 . THR B 2 80  ? 34.554  -60.717 -43.415  1.000 173.649 ? 80  THR LLL OG1 1 
ATOM 2226 C CG2 . THR B 2 80  ? 32.332  -61.663 -43.822  1.000 181.790 ? 80  THR LLL CG2 1 
ATOM 2227 N N   . ILE B 2 81  ? 33.413  -57.208 -42.280  1.000 152.110 ? 81  ILE LLL N   1 
ATOM 2228 C CA  . ILE B 2 81  ? 34.279  -56.158 -41.701  1.000 155.830 ? 81  ILE LLL CA  1 
ATOM 2229 C C   . ILE B 2 81  ? 34.747  -56.673 -40.349  1.000 163.443 ? 81  ILE LLL C   1 
ATOM 2230 O O   . ILE B 2 81  ? 33.985  -56.466 -39.393  1.000 174.082 ? 81  ILE LLL O   1 
ATOM 2231 C CB  . ILE B 2 81  ? 33.474  -54.865 -41.505  1.000 158.689 ? 81  ILE LLL CB  1 
ATOM 2232 C CG1 . ILE B 2 81  ? 32.601  -54.516 -42.715  1.000 158.254 ? 81  ILE LLL CG1 1 
ATOM 2233 C CG2 . ILE B 2 81  ? 34.409  -53.736 -41.119  1.000 157.049 ? 81  ILE LLL CG2 1 
ATOM 2234 C CD1 . ILE B 2 81  ? 31.621  -53.376 -42.458  1.000 154.992 ? 81  ILE LLL CD1 1 
ATOM 2235 N N   . SER B 2 82  ? 35.922  -57.300 -40.247  1.000 168.788 ? 82  SER LLL N   1 
ATOM 2236 C CA  . SER B 2 82  ? 36.569  -57.574 -38.932  1.000 167.226 ? 82  SER LLL CA  1 
ATOM 2237 C C   . SER B 2 82  ? 36.915  -56.246 -38.261  1.000 169.787 ? 82  SER LLL C   1 
ATOM 2238 O O   . SER B 2 82  ? 37.235  -55.287 -38.981  1.000 175.969 ? 82  SER LLL O   1 
ATOM 2239 C CB  . SER B 2 82  ? 37.805  -58.407 -39.040  1.000 164.384 ? 82  SER LLL CB  1 
ATOM 2240 O OG  . SER B 2 82  ? 37.520  -59.597 -39.719  1.000 175.329 ? 82  SER LLL OG  1 
ATOM 2241 N N   . SER B 2 83  ? 36.868  -56.203 -36.930  1.000 176.640 ? 83  SER LLL N   1 
ATOM 2242 C CA  . SER B 2 83  ? 37.367  -55.060 -36.135  1.000 176.542 ? 83  SER LLL CA  1 
ATOM 2243 C C   . SER B 2 83  ? 36.638  -53.795 -36.585  1.000 159.684 ? 83  SER LLL C   1 
ATOM 2244 O O   . SER B 2 83  ? 37.301  -52.865 -37.087  1.000 150.290 ? 83  SER LLL O   1 
ATOM 2245 C CB  . SER B 2 83  ? 38.854  -54.914 -36.289  1.000 192.452 ? 83  SER LLL CB  1 
ATOM 2246 O OG  . SER B 2 83  ? 39.255  -53.587 -35.998  1.000 201.471 ? 83  SER LLL OG  1 
ATOM 2247 N N   . LEU B 2 84  ? 35.313  -53.773 -36.463  1.000 156.040 ? 84  LEU LLL N   1 
ATOM 2248 C CA  . LEU B 2 84  ? 34.513  -52.602 -36.903  1.000 151.115 ? 84  LEU LLL CA  1 
ATOM 2249 C C   . LEU B 2 84  ? 35.148  -51.348 -36.311  1.000 151.159 ? 84  LEU LLL C   1 
ATOM 2250 O O   . LEU B 2 84  ? 35.747  -51.431 -35.245  1.000 164.077 ? 84  LEU LLL O   1 
ATOM 2251 C CB  . LEU B 2 84  ? 33.056  -52.720 -36.455  1.000 147.452 ? 84  LEU LLL CB  1 
ATOM 2252 C CG  . LEU B 2 84  ? 32.136  -51.687 -37.086  1.000 144.178 ? 84  LEU LLL CG  1 
ATOM 2253 C CD1 . LEU B 2 84  ? 32.191  -51.774 -38.598  1.000 151.419 ? 84  LEU LLL CD1 1 
ATOM 2254 C CD2 . LEU B 2 84  ? 30.718  -51.884 -36.625  1.000 146.254 ? 84  LEU LLL CD2 1 
ATOM 2255 N N   . GLN B 2 85  ? 35.032  -50.226 -36.995  1.000 146.700 ? 85  GLN LLL N   1 
ATOM 2256 C CA  . GLN B 2 85  ? 35.653  -48.992 -36.507  1.000 150.534 ? 85  GLN LLL CA  1 
ATOM 2257 C C   . GLN B 2 85  ? 34.639  -47.871 -36.596  1.000 145.401 ? 85  GLN LLL C   1 
ATOM 2258 O O   . GLN B 2 85  ? 33.534  -48.121 -37.172  1.000 140.358 ? 85  GLN LLL O   1 
ATOM 2259 C CB  . GLN B 2 85  ? 36.893  -48.700 -37.325  1.000 156.956 ? 85  GLN LLL CB  1 
ATOM 2260 C CG  . GLN B 2 85  ? 37.972  -48.122 -36.455  1.000 174.060 ? 85  GLN LLL CG  1 
ATOM 2261 C CD  . GLN B 2 85  ? 38.660  -49.228 -35.705  1.000 187.451 ? 85  GLN LLL CD  1 
ATOM 2262 O OE1 . GLN B 2 85  ? 39.486  -49.930 -36.276  1.000 195.859 ? 85  GLN LLL OE1 1 
ATOM 2263 N NE2 . GLN B 2 85  ? 38.330  -49.383 -34.431  1.000 195.274 ? 85  GLN LLL NE2 1 
ATOM 2264 N N   . ALA B 2 86  ? 35.008  -46.720 -36.029  1.000 140.139 ? 86  ALA LLL N   1 
ATOM 2265 C CA  . ALA B 2 86  ? 34.205  -45.481 -36.092  1.000 152.201 ? 86  ALA LLL CA  1 
ATOM 2266 C C   . ALA B 2 86  ? 33.802  -45.225 -37.549  1.000 153.799 ? 86  ALA LLL C   1 
ATOM 2267 O O   . ALA B 2 86  ? 32.583  -45.368 -37.903  1.000 143.054 ? 86  ALA LLL O   1 
ATOM 2268 C CB  . ALA B 2 86  ? 35.005  -44.332 -35.529  1.000 156.809 ? 86  ALA LLL CB  1 
ATOM 2269 N N   . GLU B 2 87  ? 34.831  -44.954 -38.361  1.000 158.383 ? 87  GLU LLL N   1 
ATOM 2270 C CA  . GLU B 2 87  ? 34.736  -44.465 -39.757  1.000 160.451 ? 87  GLU LLL CA  1 
ATOM 2271 C C   . GLU B 2 87  ? 34.268  -45.589 -40.693  1.000 150.464 ? 87  GLU LLL C   1 
ATOM 2272 O O   . GLU B 2 87  ? 34.352  -45.388 -41.918  1.000 162.243 ? 87  GLU LLL O   1 
ATOM 2273 C CB  . GLU B 2 87  ? 36.073  -43.859 -40.208  1.000 176.297 ? 87  GLU LLL CB  1 
ATOM 2274 C CG  . GLU B 2 87  ? 37.140  -44.876 -40.591  1.000 192.684 ? 87  GLU LLL CG  1 
ATOM 2275 C CD  . GLU B 2 87  ? 38.537  -44.333 -40.914  1.000 206.563 ? 87  GLU LLL CD  1 
ATOM 2276 O OE1 . GLU B 2 87  ? 38.680  -43.484 -41.833  1.000 211.768 ? 87  GLU LLL OE1 1 
ATOM 2277 O OE2 . GLU B 2 87  ? 39.503  -44.783 -40.266  1.000 216.351 ? 87  GLU LLL OE2 1 
ATOM 2278 N N   . ASP B 2 88  ? 33.776  -46.714 -40.176  1.000 141.268 ? 88  ASP LLL N   1 
ATOM 2279 C CA  . ASP B 2 88  ? 33.109  -47.755 -41.006  1.000 139.809 ? 88  ASP LLL CA  1 
ATOM 2280 C C   . ASP B 2 88  ? 31.592  -47.525 -41.104  1.000 142.070 ? 88  ASP LLL C   1 
ATOM 2281 O O   . ASP B 2 88  ? 30.964  -48.171 -41.981  1.000 133.981 ? 88  ASP LLL O   1 
ATOM 2282 C CB  . ASP B 2 88  ? 33.413  -49.158 -40.486  1.000 139.583 ? 88  ASP LLL CB  1 
ATOM 2283 C CG  . ASP B 2 88  ? 34.811  -49.568 -40.876  1.000 140.058 ? 88  ASP LLL CG  1 
ATOM 2284 O OD1 . ASP B 2 88  ? 35.316  -48.974 -41.831  1.000 138.606 ? 88  ASP LLL OD1 1 
ATOM 2285 O OD2 . ASP B 2 88  ? 35.391  -50.447 -40.226  1.000 139.914 ? 88  ASP LLL OD2 1 
ATOM 2286 N N   . VAL B 2 89  ? 31.000  -46.677 -40.257  1.000 146.561 ? 89  VAL LLL N   1 
ATOM 2287 C CA  . VAL B 2 89  ? 29.506  -46.569 -40.179  1.000 160.556 ? 89  VAL LLL CA  1 
ATOM 2288 C C   . VAL B 2 89  ? 28.990  -45.993 -41.521  1.000 154.440 ? 89  VAL LLL C   1 
ATOM 2289 O O   . VAL B 2 89  ? 29.382  -44.850 -41.848  1.000 138.027 ? 89  VAL LLL O   1 
ATOM 2290 C CB  . VAL B 2 89  ? 29.025  -45.769 -38.936  1.000 175.611 ? 89  VAL LLL CB  1 
ATOM 2291 C CG1 . VAL B 2 89  ? 29.367  -46.469 -37.632  1.000 179.194 ? 89  VAL LLL CG1 1 
ATOM 2292 C CG2 . VAL B 2 89  ? 29.533  -44.329 -38.866  1.000 187.001 ? 89  VAL LLL CG2 1 
ATOM 2293 N N   . ALA B 2 90  ? 28.172  -46.753 -42.279  1.000 150.723 ? 90  ALA LLL N   1 
ATOM 2294 C CA  . ALA B 2 90  ? 27.681  -46.399 -43.643  1.000 146.052 ? 90  ALA LLL CA  1 
ATOM 2295 C C   . ALA B 2 90  ? 26.627  -47.399 -44.160  1.000 139.619 ? 90  ALA LLL C   1 
ATOM 2296 O O   . ALA B 2 90  ? 26.259  -48.297 -43.396  1.000 147.264 ? 90  ALA LLL O   1 
ATOM 2297 C CB  . ALA B 2 90  ? 28.867  -46.358 -44.577  1.000 153.924 ? 90  ALA LLL CB  1 
ATOM 2298 N N   . VAL B 2 91  ? 26.164  -47.257 -45.412  1.000 134.098 ? 91  VAL LLL N   1 
ATOM 2299 C CA  . VAL B 2 91  ? 25.320  -48.276 -46.111  1.000 134.362 ? 91  VAL LLL CA  1 
ATOM 2300 C C   . VAL B 2 91  ? 26.166  -49.047 -47.126  1.000 138.056 ? 91  VAL LLL C   1 
ATOM 2301 O O   . VAL B 2 91  ? 26.934  -48.429 -47.874  1.000 138.660 ? 91  VAL LLL O   1 
ATOM 2302 C CB  . VAL B 2 91  ? 24.141  -47.651 -46.861  1.000 136.081 ? 91  VAL LLL CB  1 
ATOM 2303 C CG1 . VAL B 2 91  ? 23.119  -48.711 -47.256  1.000 134.689 ? 91  VAL LLL CG1 1 
ATOM 2304 C CG2 . VAL B 2 91  ? 23.494  -46.536 -46.080  1.000 143.355 ? 91  VAL LLL CG2 1 
ATOM 2305 N N   . TYR B 2 92  ? 25.978  -50.356 -47.193  1.000 136.394 ? 92  TYR LLL N   1 
ATOM 2306 C CA  . TYR B 2 92  ? 26.822  -51.269 -47.996  1.000 132.875 ? 92  TYR LLL CA  1 
ATOM 2307 C C   . TYR B 2 92  ? 25.892  -51.828 -49.063  1.000 131.771 ? 92  TYR LLL C   1 
ATOM 2308 O O   . TYR B 2 92  ? 24.858  -52.402 -48.727  1.000 130.280 ? 92  TYR LLL O   1 
ATOM 2309 C CB  . TYR B 2 92  ? 27.561  -52.257 -47.073  1.000 128.748 ? 92  TYR LLL CB  1 
ATOM 2310 C CG  . TYR B 2 92  ? 28.622  -51.588 -46.222  1.000 126.364 ? 92  TYR LLL CG  1 
ATOM 2311 C CD1 . TYR B 2 92  ? 28.296  -50.761 -45.159  1.000 130.647 ? 92  TYR LLL CD1 1 
ATOM 2312 C CD2 . TYR B 2 92  ? 29.961  -51.671 -46.546  1.000 134.040 ? 92  TYR LLL CD2 1 
ATOM 2313 C CE1 . TYR B 2 92  ? 29.255  -50.070 -44.433  1.000 131.268 ? 92  TYR LLL CE1 1 
ATOM 2314 C CE2 . TYR B 2 92  ? 30.938  -50.987 -45.831  1.000 136.605 ? 92  TYR LLL CE2 1 
ATOM 2315 C CZ  . TYR B 2 92  ? 30.592  -50.183 -44.765  1.000 134.910 ? 92  TYR LLL CZ  1 
ATOM 2316 O OH  . TYR B 2 92  ? 31.573  -49.536 -44.058  1.000 141.728 ? 92  TYR LLL OH  1 
ATOM 2317 N N   . TYR B 2 93  ? 26.200  -51.590 -50.327  1.000 137.576 ? 93  TYR LLL N   1 
ATOM 2318 C CA  . TYR B 2 93  ? 25.444  -52.213 -51.441  1.000 142.719 ? 93  TYR LLL CA  1 
ATOM 2319 C C   . TYR B 2 93  ? 26.299  -53.278 -52.142  1.000 139.082 ? 93  TYR LLL C   1 
ATOM 2320 O O   . TYR B 2 93  ? 27.496  -53.046 -52.441  1.000 122.781 ? 93  TYR LLL O   1 
ATOM 2321 C CB  . TYR B 2 93  ? 24.977  -51.153 -52.434  1.000 142.968 ? 93  TYR LLL CB  1 
ATOM 2322 C CG  . TYR B 2 93  ? 24.126  -50.037 -51.871  1.000 138.007 ? 93  TYR LLL CG  1 
ATOM 2323 C CD1 . TYR B 2 93  ? 22.730  -50.053 -51.936  1.000 129.692 ? 93  TYR LLL CD1 1 
ATOM 2324 C CD2 . TYR B 2 93  ? 24.736  -48.906 -51.361  1.000 137.762 ? 93  TYR LLL CD2 1 
ATOM 2325 C CE1 . TYR B 2 93  ? 21.968  -48.996 -51.460  1.000 124.071 ? 93  TYR LLL CE1 1 
ATOM 2326 C CE2 . TYR B 2 93  ? 23.996  -47.828 -50.908  1.000 133.595 ? 93  TYR LLL CE2 1 
ATOM 2327 C CZ  . TYR B 2 93  ? 22.615  -47.874 -50.948  1.000 128.172 ? 93  TYR LLL CZ  1 
ATOM 2328 O OH  . TYR B 2 93  ? 22.012  -46.745 -50.467  1.000 120.546 ? 93  TYR LLL OH  1 
ATOM 2329 N N   . CYS B 2 94  ? 25.708  -54.444 -52.381  1.000 139.769 ? 94  CYS LLL N   1 
ATOM 2330 C CA  . CYS B 2 94  ? 26.299  -55.420 -53.316  1.000 153.657 ? 94  CYS LLL CA  1 
ATOM 2331 C C   . CYS B 2 94  ? 25.706  -55.121 -54.692  1.000 171.633 ? 94  CYS LLL C   1 
ATOM 2332 O O   . CYS B 2 94  ? 24.600  -54.537 -54.752  1.000 178.165 ? 94  CYS LLL O   1 
ATOM 2333 C CB  . CYS B 2 94  ? 26.044  -56.851 -52.898  1.000 158.607 ? 94  CYS LLL CB  1 
ATOM 2334 S SG  . CYS B 2 94  ? 24.298  -57.286 -53.009  1.000 171.197 ? 94  CYS LLL SG  1 
ATOM 2335 N N   . GLN B 2 95  ? 26.454  -55.467 -55.743  1.000 174.934 ? 95  GLN LLL N   1 
ATOM 2336 C CA  . GLN B 2 95  ? 26.156  -55.147 -57.161  1.000 159.202 ? 95  GLN LLL CA  1 
ATOM 2337 C C   . GLN B 2 95  ? 26.799  -56.224 -58.032  1.000 158.200 ? 95  GLN LLL C   1 
ATOM 2338 O O   . GLN B 2 95  ? 27.949  -56.610 -57.742  1.000 151.022 ? 95  GLN LLL O   1 
ATOM 2339 C CB  . GLN B 2 95  ? 26.732  -53.780 -57.533  1.000 160.299 ? 95  GLN LLL CB  1 
ATOM 2340 C CG  . GLN B 2 95  ? 26.352  -53.334 -58.942  1.000 165.961 ? 95  GLN LLL CG  1 
ATOM 2341 C CD  . GLN B 2 95  ? 27.514  -52.887 -59.790  1.000 158.920 ? 95  GLN LLL CD  1 
ATOM 2342 O OE1 . GLN B 2 95  ? 28.629  -53.377 -59.645  1.000 157.775 ? 95  GLN LLL OE1 1 
ATOM 2343 N NE2 . GLN B 2 95  ? 27.240  -51.973 -60.707  1.000 151.688 ? 95  GLN LLL NE2 1 
ATOM 2344 N N   . GLN B 2 96  ? 26.067  -56.718 -59.031  1.000 165.314 ? 96  GLN LLL N   1 
ATOM 2345 C CA  . GLN B 2 96  ? 26.607  -57.634 -60.073  1.000 163.208 ? 96  GLN LLL CA  1 
ATOM 2346 C C   . GLN B 2 96  ? 26.845  -56.809 -61.340  1.000 169.411 ? 96  GLN LLL C   1 
ATOM 2347 O O   . GLN B 2 96  ? 26.156  -55.765 -61.549  1.000 165.799 ? 96  GLN LLL O   1 
ATOM 2348 C CB  . GLN B 2 96  ? 25.690  -58.833 -60.335  1.000 162.104 ? 96  GLN LLL CB  1 
ATOM 2349 C CG  . GLN B 2 96  ? 24.359  -58.476 -60.986  1.000 168.430 ? 96  GLN LLL CG  1 
ATOM 2350 C CD  . GLN B 2 96  ? 24.465  -58.351 -62.486  1.000 172.500 ? 96  GLN LLL CD  1 
ATOM 2351 O OE1 . GLN B 2 96  ? 25.383  -58.891 -63.104  1.000 151.627 ? 96  GLN LLL OE1 1 
ATOM 2352 N NE2 . GLN B 2 96  ? 23.532  -57.609 -63.075  1.000 187.396 ? 96  GLN LLL NE2 1 
ATOM 2353 N N   . TYR B 2 97  ? 27.822  -57.257 -62.128  1.000 172.737 ? 97  TYR LLL N   1 
ATOM 2354 C CA  . TYR B 2 97  ? 28.247  -56.680 -63.430  1.000 168.418 ? 97  TYR LLL CA  1 
ATOM 2355 C C   . TYR B 2 97  ? 28.472  -57.840 -64.411  1.000 174.936 ? 97  TYR LLL C   1 
ATOM 2356 O O   . TYR B 2 97  ? 29.220  -57.697 -65.394  1.000 170.867 ? 97  TYR LLL O   1 
ATOM 2357 C CB  . TYR B 2 97  ? 29.470  -55.770 -63.235  1.000 160.514 ? 97  TYR LLL CB  1 
ATOM 2358 C CG  . TYR B 2 97  ? 30.620  -56.354 -62.450  1.000 157.076 ? 97  TYR LLL CG  1 
ATOM 2359 C CD1 . TYR B 2 97  ? 30.646  -56.319 -61.064  1.000 154.179 ? 97  TYR LLL CD1 1 
ATOM 2360 C CD2 . TYR B 2 97  ? 31.695  -56.934 -63.093  1.000 158.590 ? 97  TYR LLL CD2 1 
ATOM 2361 C CE1 . TYR B 2 97  ? 31.693  -56.864 -60.341  1.000 146.939 ? 97  TYR LLL CE1 1 
ATOM 2362 C CE2 . TYR B 2 97  ? 32.752  -57.481 -62.389  1.000 158.191 ? 97  TYR LLL CE2 1 
ATOM 2363 C CZ  . TYR B 2 97  ? 32.750  -57.441 -61.014  1.000 153.545 ? 97  TYR LLL CZ  1 
ATOM 2364 O OH  . TYR B 2 97  ? 33.816  -57.968 -60.358  1.000 175.860 ? 97  TYR LLL OH  1 
ATOM 2365 N N   . TYR B 2 98  ? 27.836  -58.984 -64.136  1.000 180.708 ? 98  TYR LLL N   1 
ATOM 2366 C CA  . TYR B 2 98  ? 27.955  -60.221 -64.945  1.000 185.201 ? 98  TYR LLL CA  1 
ATOM 2367 C C   . TYR B 2 98  ? 27.370  -59.883 -66.310  1.000 191.729 ? 98  TYR LLL C   1 
ATOM 2368 O O   . TYR B 2 98  ? 28.033  -60.112 -67.333  1.000 199.587 ? 98  TYR LLL O   1 
ATOM 2369 C CB  . TYR B 2 98  ? 27.261  -61.387 -64.235  1.000 185.618 ? 98  TYR LLL CB  1 
ATOM 2370 C CG  . TYR B 2 98  ? 27.121  -62.646 -65.048  1.000 194.161 ? 98  TYR LLL CG  1 
ATOM 2371 C CD1 . TYR B 2 98  ? 28.181  -63.531 -65.209  1.000 200.431 ? 98  TYR LLL CD1 1 
ATOM 2372 C CD2 . TYR B 2 98  ? 25.914  -62.964 -65.642  1.000 200.922 ? 98  TYR LLL CD2 1 
ATOM 2373 C CE1 . TYR B 2 98  ? 28.048  -64.689 -65.959  1.000 200.902 ? 98  TYR LLL CE1 1 
ATOM 2374 C CE2 . TYR B 2 98  ? 25.759  -64.124 -66.383  1.000 206.498 ? 98  TYR LLL CE2 1 
ATOM 2375 C CZ  . TYR B 2 98  ? 26.832  -64.982 -66.549  1.000 203.668 ? 98  TYR LLL CZ  1 
ATOM 2376 O OH  . TYR B 2 98  ? 26.699  -66.117 -67.284  1.000 216.800 ? 98  TYR LLL OH  1 
ATOM 2377 N N   . SER B 2 99  ? 26.190  -59.264 -66.278  1.000 195.014 ? 99  SER LLL N   1 
ATOM 2378 C CA  . SER B 2 99  ? 25.363  -58.907 -67.456  1.000 204.198 ? 99  SER LLL CA  1 
ATOM 2379 C C   . SER B 2 99  ? 24.767  -57.513 -67.272  1.000 205.068 ? 99  SER LLL C   1 
ATOM 2380 O O   . SER B 2 99  ? 24.533  -57.131 -66.120  1.000 209.771 ? 99  SER LLL O   1 
ATOM 2381 C CB  . SER B 2 99  ? 24.259  -59.901 -67.616  1.000 214.615 ? 99  SER LLL CB  1 
ATOM 2382 O OG  . SER B 2 99  ? 23.129  -59.485 -66.859  1.000 224.114 ? 99  SER LLL OG  1 
ATOM 2383 N N   . THR B 2 100 ? 24.467  -56.811 -68.365  1.000 208.826 ? 100 THR LLL N   1 
ATOM 2384 C CA  . THR B 2 100 ? 23.518  -55.667 -68.362  1.000 205.697 ? 100 THR LLL CA  1 
ATOM 2385 C C   . THR B 2 100 ? 22.104  -56.225 -68.536  1.000 201.245 ? 100 THR LLL C   1 
ATOM 2386 O O   . THR B 2 100 ? 21.874  -57.173 -69.278  1.000 211.105 ? 100 THR LLL O   1 
ATOM 2387 C CB  . THR B 2 100 ? 23.875  -54.607 -69.412  1.000 205.996 ? 100 THR LLL CB  1 
ATOM 2388 O OG1 . THR B 2 100 ? 23.591  -55.141 -70.705  1.000 214.702 ? 100 THR LLL OG1 1 
ATOM 2389 C CG2 . THR B 2 100 ? 25.317  -54.164 -69.338  1.000 196.267 ? 100 THR LLL CG2 1 
ATOM 2390 N N   . PRO B 2 101 ? 21.093  -55.659 -67.861  1.000 184.269 ? 101 PRO LLL N   1 
ATOM 2391 C CA  . PRO B 2 101 ? 21.295  -54.488 -67.016  1.000 178.295 ? 101 PRO LLL CA  1 
ATOM 2392 C C   . PRO B 2 101 ? 21.977  -54.847 -65.692  1.000 175.926 ? 101 PRO LLL C   1 
ATOM 2393 O O   . PRO B 2 101 ? 21.630  -55.852 -65.118  1.000 179.955 ? 101 PRO LLL O   1 
ATOM 2394 C CB  . PRO B 2 101 ? 19.866  -54.005 -66.786  1.000 183.431 ? 101 PRO LLL CB  1 
ATOM 2395 C CG  . PRO B 2 101 ? 19.042  -55.280 -66.836  1.000 192.086 ? 101 PRO LLL CG  1 
ATOM 2396 C CD  . PRO B 2 101 ? 19.706  -56.138 -67.889  1.000 187.179 ? 101 PRO LLL CD  1 
ATOM 2397 N N   . TYR B 2 102 ? 22.943  -54.029 -65.268  1.000 176.112 ? 102 TYR LLL N   1 
ATOM 2398 C CA  . TYR B 2 102 ? 23.536  -54.059 -63.908  1.000 172.098 ? 102 TYR LLL CA  1 
ATOM 2399 C C   . TYR B 2 102 ? 22.400  -53.892 -62.892  1.000 174.014 ? 102 TYR LLL C   1 
ATOM 2400 O O   . TYR B 2 102 ? 21.449  -53.112 -63.186  1.000 165.286 ? 102 TYR LLL O   1 
ATOM 2401 C CB  . TYR B 2 102 ? 24.559  -52.933 -63.739  1.000 169.729 ? 102 TYR LLL CB  1 
ATOM 2402 C CG  . TYR B 2 102 ? 25.819  -53.017 -64.565  1.000 164.177 ? 102 TYR LLL CG  1 
ATOM 2403 C CD1 . TYR B 2 102 ? 26.787  -52.034 -64.420  1.000 163.524 ? 102 TYR LLL CD1 1 
ATOM 2404 C CD2 . TYR B 2 102 ? 26.072  -54.046 -65.462  1.000 155.305 ? 102 TYR LLL CD2 1 
ATOM 2405 C CE1 . TYR B 2 102 ? 27.965  -52.056 -65.150  1.000 161.155 ? 102 TYR LLL CE1 1 
ATOM 2406 C CE2 . TYR B 2 102 ? 27.253  -54.082 -66.197  1.000 156.283 ? 102 TYR LLL CE2 1 
ATOM 2407 C CZ  . TYR B 2 102 ? 28.215  -53.090 -66.032  1.000 156.476 ? 102 TYR LLL CZ  1 
ATOM 2408 O OH  . TYR B 2 102 ? 29.423  -53.057 -66.686  1.000 144.858 ? 102 TYR LLL OH  1 
ATOM 2409 N N   . THR B 2 103 ? 22.496  -54.580 -61.747  1.000 167.491 ? 103 THR LLL N   1 
ATOM 2410 C CA  . THR B 2 103 ? 21.477  -54.541 -60.668  1.000 157.925 ? 103 THR LLL CA  1 
ATOM 2411 C C   . THR B 2 103 ? 22.188  -54.502 -59.304  1.000 163.520 ? 103 THR LLL C   1 
ATOM 2412 O O   . THR B 2 103 ? 23.242  -55.179 -59.175  1.000 164.272 ? 103 THR LLL O   1 
ATOM 2413 C CB  . THR B 2 103 ? 20.482  -55.685 -60.901  1.000 149.650 ? 103 THR LLL CB  1 
ATOM 2414 O OG1 . THR B 2 103 ? 19.561  -55.632 -59.812  1.000 153.976 ? 103 THR LLL OG1 1 
ATOM 2415 C CG2 . THR B 2 103 ? 21.136  -57.047 -61.032  1.000 143.661 ? 103 THR LLL CG2 1 
ATOM 2416 N N   . PHE B 2 104 ? 21.632  -53.755 -58.334  1.000 163.707 ? 104 PHE LLL N   1 
ATOM 2417 C CA  . PHE B 2 104 ? 22.132  -53.633 -56.934  1.000 164.921 ? 104 PHE LLL CA  1 
ATOM 2418 C C   . PHE B 2 104 ? 21.249  -54.425 -55.957  1.000 177.292 ? 104 PHE LLL C   1 
ATOM 2419 O O   . PHE B 2 104 ? 20.123  -54.835 -56.329  1.000 184.382 ? 104 PHE LLL O   1 
ATOM 2420 C CB  . PHE B 2 104 ? 22.118  -52.177 -56.466  1.000 159.407 ? 104 PHE LLL CB  1 
ATOM 2421 C CG  . PHE B 2 104 ? 23.099  -51.266 -57.150  1.000 158.275 ? 104 PHE LLL CG  1 
ATOM 2422 C CD1 . PHE B 2 104 ? 22.738  -50.563 -58.284  1.000 160.465 ? 104 PHE LLL CD1 1 
ATOM 2423 C CD2 . PHE B 2 104 ? 24.376  -51.089 -56.644  1.000 162.250 ? 104 PHE LLL CD2 1 
ATOM 2424 C CE1 . PHE B 2 104 ? 23.642  -49.712 -58.908  1.000 164.515 ? 104 PHE LLL CE1 1 
ATOM 2425 C CE2 . PHE B 2 104 ? 25.282  -50.251 -57.277  1.000 168.432 ? 104 PHE LLL CE2 1 
ATOM 2426 C CZ  . PHE B 2 104 ? 24.916  -49.563 -58.412  1.000 162.863 ? 104 PHE LLL CZ  1 
ATOM 2427 N N   . GLY B 2 105 ? 21.742  -54.622 -54.725  1.000 186.636 ? 105 GLY LLL N   1 
ATOM 2428 C CA  . GLY B 2 105 ? 20.945  -55.069 -53.561  1.000 177.584 ? 105 GLY LLL CA  1 
ATOM 2429 C C   . GLY B 2 105 ? 20.195  -53.895 -52.957  1.000 168.209 ? 105 GLY LLL C   1 
ATOM 2430 O O   . GLY B 2 105 ? 20.409  -52.718 -53.419  1.000 158.890 ? 105 GLY LLL O   1 
ATOM 2431 N N   . GLN B 2 106 ? 19.356  -54.170 -51.958  1.000 152.449 ? 106 GLN LLL N   1 
ATOM 2432 C CA  . GLN B 2 106 ? 18.577  -53.099 -51.287  1.000 157.526 ? 106 GLN LLL CA  1 
ATOM 2433 C C   . GLN B 2 106 ? 19.511  -52.209 -50.467  1.000 149.143 ? 106 GLN LLL C   1 
ATOM 2434 O O   . GLN B 2 106 ? 19.103  -51.092 -50.151  1.000 138.552 ? 106 GLN LLL O   1 
ATOM 2435 C CB  . GLN B 2 106 ? 17.478  -53.671 -50.397  1.000 178.253 ? 106 GLN LLL CB  1 
ATOM 2436 C CG  . GLN B 2 106 ? 17.983  -54.409 -49.162  1.000 197.572 ? 106 GLN LLL CG  1 
ATOM 2437 C CD  . GLN B 2 106 ? 18.177  -55.894 -49.377  1.000 216.347 ? 106 GLN LLL CD  1 
ATOM 2438 O OE1 . GLN B 2 106 ? 18.315  -56.381 -50.506  1.000 214.678 ? 106 GLN LLL OE1 1 
ATOM 2439 N NE2 . GLN B 2 106 ? 18.213  -56.627 -48.274  1.000 227.086 ? 106 GLN LLL NE2 1 
ATOM 2440 N N   . GLY B 2 107 ? 20.701  -52.704 -50.112  1.000 156.493 ? 107 GLY LLL N   1 
ATOM 2441 C CA  . GLY B 2 107 ? 21.662  -52.001 -49.238  1.000 159.686 ? 107 GLY LLL CA  1 
ATOM 2442 C C   . GLY B 2 107 ? 21.495  -52.410 -47.787  1.000 157.121 ? 107 GLY LLL C   1 
ATOM 2443 O O   . GLY B 2 107 ? 20.413  -52.906 -47.427  1.000 156.843 ? 107 GLY LLL O   1 
ATOM 2444 N N   . THR B 2 108 ? 22.531  -52.208 -46.977  1.000 153.624 ? 108 THR LLL N   1 
ATOM 2445 C CA  . THR B 2 108 ? 22.563  -52.626 -45.556  1.000 148.087 ? 108 THR LLL CA  1 
ATOM 2446 C C   . THR B 2 108 ? 23.193  -51.520 -44.712  1.000 150.373 ? 108 THR LLL C   1 
ATOM 2447 O O   . THR B 2 108 ? 24.312  -51.114 -45.033  1.000 143.349 ? 108 THR LLL O   1 
ATOM 2448 C CB  . THR B 2 108 ? 23.338  -53.936 -45.410  1.000 146.072 ? 108 THR LLL CB  1 
ATOM 2449 O OG1 . THR B 2 108 ? 22.570  -54.995 -45.980  1.000 142.309 ? 108 THR LLL OG1 1 
ATOM 2450 C CG2 . THR B 2 108 ? 23.642  -54.251 -43.970  1.000 154.375 ? 108 THR LLL CG2 1 
ATOM 2451 N N   . LYS B 2 109 ? 22.510  -51.051 -43.667  1.000 153.760 ? 109 LYS LLL N   1 
ATOM 2452 C CA  . LYS B 2 109 ? 23.099  -50.058 -42.735  1.000 146.442 ? 109 LYS LLL CA  1 
ATOM 2453 C C   . LYS B 2 109 ? 23.922  -50.805 -41.695  1.000 145.773 ? 109 LYS LLL C   1 
ATOM 2454 O O   . LYS B 2 109 ? 23.421  -51.818 -41.170  1.000 150.064 ? 109 LYS LLL O   1 
ATOM 2455 C CB  . LYS B 2 109 ? 22.023  -49.216 -42.052  1.000 147.056 ? 109 LYS LLL CB  1 
ATOM 2456 C CG  . LYS B 2 109 ? 21.739  -47.901 -42.756  1.000 156.575 ? 109 LYS LLL CG  1 
ATOM 2457 C CD  . LYS B 2 109 ? 21.181  -46.792 -41.883  1.000 167.377 ? 109 LYS LLL CD  1 
ATOM 2458 C CE  . LYS B 2 109 ? 19.712  -46.962 -41.545  1.000 185.989 ? 109 LYS LLL CE  1 
ATOM 2459 N NZ  . LYS B 2 109 ? 19.516  -47.799 -40.331  1.000 204.497 ? 109 LYS LLL NZ  1 
ATOM 2460 N N   . VAL B 2 110 ? 25.105  -50.286 -41.386  1.000 141.227 ? 110 VAL LLL N   1 
ATOM 2461 C CA  . VAL B 2 110 ? 25.908  -50.718 -40.205  1.000 143.815 ? 110 VAL LLL CA  1 
ATOM 2462 C C   . VAL B 2 110 ? 26.117  -49.520 -39.266  1.000 144.897 ? 110 VAL LLL C   1 
ATOM 2463 O O   . VAL B 2 110 ? 26.496  -48.414 -39.751  1.000 132.241 ? 110 VAL LLL O   1 
ATOM 2464 C CB  . VAL B 2 110 ? 27.247  -51.332 -40.643  1.000 140.833 ? 110 VAL LLL CB  1 
ATOM 2465 C CG1 . VAL B 2 110 ? 27.065  -52.351 -41.777  1.000 133.614 ? 110 VAL LLL CG1 1 
ATOM 2466 C CG2 . VAL B 2 110 ? 28.232  -50.230 -41.019  1.000 142.809 ? 110 VAL LLL CG2 1 
ATOM 2467 N N   . GLU B 2 111 ? 25.916  -49.734 -37.964  1.000 147.101 ? 111 GLU LLL N   1 
ATOM 2468 C CA  . GLU B 2 111 ? 26.121  -48.688 -36.930  1.000 156.108 ? 111 GLU LLL CA  1 
ATOM 2469 C C   . GLU B 2 111 ? 26.827  -49.274 -35.694  1.000 154.087 ? 111 GLU LLL C   1 
ATOM 2470 O O   . GLU B 2 111 ? 26.932  -50.516 -35.602  1.000 153.608 ? 111 GLU LLL O   1 
ATOM 2471 C CB  . GLU B 2 111 ? 24.757  -48.075 -36.621  1.000 170.673 ? 111 GLU LLL CB  1 
ATOM 2472 C CG  . GLU B 2 111 ? 23.862  -48.976 -35.792  1.000 191.281 ? 111 GLU LLL CG  1 
ATOM 2473 C CD  . GLU B 2 111 ? 22.423  -48.508 -35.644  1.000 206.015 ? 111 GLU LLL CD  1 
ATOM 2474 O OE1 . GLU B 2 111 ? 21.892  -48.578 -34.497  1.000 214.286 ? 111 GLU LLL OE1 1 
ATOM 2475 O OE2 . GLU B 2 111 ? 21.832  -48.074 -36.673  1.000 208.225 ? 111 GLU LLL OE2 1 
ATOM 2476 N N   . ILE B 2 112 ? 27.246  -48.417 -34.755  1.000 152.680 ? 112 ILE LLL N   1 
ATOM 2477 C CA  . ILE B 2 112 ? 27.963  -48.826 -33.508  1.000 164.044 ? 112 ILE LLL CA  1 
ATOM 2478 C C   . ILE B 2 112 ? 26.944  -49.255 -32.437  1.000 162.913 ? 112 ILE LLL C   1 
ATOM 2479 O O   . ILE B 2 112 ? 25.986  -48.522 -32.191  1.000 154.634 ? 112 ILE LLL O   1 
ATOM 2480 C CB  . ILE B 2 112 ? 28.907  -47.705 -33.016  1.000 171.836 ? 112 ILE LLL CB  1 
ATOM 2481 C CG1 . ILE B 2 112 ? 29.825  -47.211 -34.131  1.000 170.735 ? 112 ILE LLL CG1 1 
ATOM 2482 C CG2 . ILE B 2 112 ? 29.721  -48.164 -31.814  1.000 187.078 ? 112 ILE LLL CG2 1 
ATOM 2483 C CD1 . ILE B 2 112 ? 30.621  -48.331 -34.772  1.000 183.443 ? 112 ILE LLL CD1 1 
ATOM 2484 N N   . LYS B 2 113 ? 27.147  -50.430 -31.841  1.000 168.388 ? 113 LYS LLL N   1 
ATOM 2485 C CA  . LYS B 2 113 ? 26.403  -50.924 -30.655  1.000 168.274 ? 113 LYS LLL CA  1 
ATOM 2486 C C   . LYS B 2 113 ? 26.993  -50.270 -29.414  1.000 169.089 ? 113 LYS LLL C   1 
ATOM 2487 O O   . LYS B 2 113 ? 28.213  -50.090 -29.383  1.000 163.684 ? 113 LYS LLL O   1 
ATOM 2488 C CB  . LYS B 2 113 ? 26.543  -52.434 -30.517  1.000 166.607 ? 113 LYS LLL CB  1 
ATOM 2489 C CG  . LYS B 2 113 ? 25.556  -53.061 -29.566  1.000 171.314 ? 113 LYS LLL CG  1 
ATOM 2490 C CD  . LYS B 2 113 ? 25.840  -54.512 -29.350  1.000 181.922 ? 113 LYS LLL CD  1 
ATOM 2491 C CE  . LYS B 2 113 ? 25.055  -55.076 -28.186  1.000 189.174 ? 113 LYS LLL CE  1 
ATOM 2492 N NZ  . LYS B 2 113 ? 25.055  -56.555 -28.228  1.000 194.054 ? 113 LYS LLL NZ  1 
ATOM 2493 N N   . ARG B 2 114 ? 26.157  -49.933 -28.438  1.000 175.434 ? 114 ARG LLL N   1 
ATOM 2494 C CA  . ARG B 2 114 ? 26.567  -49.102 -27.279  1.000 183.709 ? 114 ARG LLL CA  1 
ATOM 2495 C C   . ARG B 2 114 ? 25.760  -49.504 -26.041  1.000 198.421 ? 114 ARG LLL C   1 
ATOM 2496 O O   . ARG B 2 114 ? 24.641  -50.038 -26.199  1.000 211.326 ? 114 ARG LLL O   1 
ATOM 2497 C CB  . ARG B 2 114 ? 26.353  -47.634 -27.649  1.000 174.856 ? 114 ARG LLL CB  1 
ATOM 2498 C CG  . ARG B 2 114 ? 26.806  -46.651 -26.586  1.000 172.963 ? 114 ARG LLL CG  1 
ATOM 2499 C CD  . ARG B 2 114 ? 25.900  -45.449 -26.583  1.000 170.890 ? 114 ARG LLL CD  1 
ATOM 2500 N NE  . ARG B 2 114 ? 25.869  -44.923 -25.248  1.000 179.578 ? 114 ARG LLL NE  1 
ATOM 2501 C CZ  . ARG B 2 114 ? 26.866  -44.255 -24.676  1.000 190.326 ? 114 ARG LLL CZ  1 
ATOM 2502 N NH1 . ARG B 2 114 ? 27.992  -43.996 -25.324  1.000 175.009 ? 114 ARG LLL NH1 1 
ATOM 2503 N NH2 . ARG B 2 114 ? 26.722  -43.832 -23.433  1.000 215.470 ? 114 ARG LLL NH2 1 
ATOM 2504 N N   . THR B 2 115 ? 26.317  -49.279 -24.850  1.000 201.286 ? 115 THR LLL N   1 
ATOM 2505 C CA  . THR B 2 115 ? 25.557  -49.296 -23.573  1.000 208.307 ? 115 THR LLL CA  1 
ATOM 2506 C C   . THR B 2 115 ? 24.326  -48.402 -23.745  1.000 201.444 ? 115 THR LLL C   1 
ATOM 2507 O O   . THR B 2 115 ? 24.467  -47.349 -24.420  1.000 195.028 ? 115 THR LLL O   1 
ATOM 2508 C CB  . THR B 2 115 ? 26.413  -48.785 -22.410  1.000 222.953 ? 115 THR LLL CB  1 
ATOM 2509 O OG1 . THR B 2 115 ? 26.978  -47.546 -22.844  1.000 233.796 ? 115 THR LLL OG1 1 
ATOM 2510 C CG2 . THR B 2 115 ? 27.500  -49.753 -21.996  1.000 231.048 ? 115 THR LLL CG2 1 
ATOM 2511 N N   . VAL B 2 116 ? 23.170  -48.791 -23.184  1.000 199.634 ? 116 VAL LLL N   1 
ATOM 2512 C CA  . VAL B 2 116 ? 21.926  -47.953 -23.254  1.000 187.360 ? 116 VAL LLL CA  1 
ATOM 2513 C C   . VAL B 2 116 ? 22.230  -46.638 -22.534  1.000 175.375 ? 116 VAL LLL C   1 
ATOM 2514 O O   . VAL B 2 116 ? 22.975  -46.637 -21.529  1.000 170.226 ? 116 VAL LLL O   1 
ATOM 2515 C CB  . VAL B 2 116 ? 20.623  -48.598 -22.718  1.000 184.346 ? 116 VAL LLL CB  1 
ATOM 2516 C CG1 . VAL B 2 116 ? 20.376  -49.996 -23.260  1.000 180.160 ? 116 VAL LLL CG1 1 
ATOM 2517 C CG2 . VAL B 2 116 ? 20.548  -48.611 -21.199  1.000 202.284 ? 116 VAL LLL CG2 1 
ATOM 2518 N N   . ALA B 2 117 ? 21.740  -45.545 -23.094  1.000 170.292 ? 117 ALA LLL N   1 
ATOM 2519 C CA  . ALA B 2 117 ? 21.789  -44.213 -22.466  1.000 177.126 ? 117 ALA LLL CA  1 
ATOM 2520 C C   . ALA B 2 117 ? 20.380  -43.651 -22.537  1.000 177.735 ? 117 ALA LLL C   1 
ATOM 2521 O O   . ALA B 2 117 ? 19.782  -43.644 -23.632  1.000 167.450 ? 117 ALA LLL O   1 
ATOM 2522 C CB  . ALA B 2 117 ? 22.794  -43.322 -23.143  1.000 181.608 ? 117 ALA LLL CB  1 
ATOM 2523 N N   . ALA B 2 118 ? 19.846  -43.276 -21.380  1.000 188.179 ? 118 ALA LLL N   1 
ATOM 2524 C CA  . ALA B 2 118 ? 18.502  -42.684 -21.270  1.000 184.487 ? 118 ALA LLL CA  1 
ATOM 2525 C C   . ALA B 2 118 ? 18.570  -41.338 -21.968  1.000 170.059 ? 118 ALA LLL C   1 
ATOM 2526 O O   . ALA B 2 118 ? 19.600  -40.675 -21.900  1.000 165.292 ? 118 ALA LLL O   1 
ATOM 2527 C CB  . ALA B 2 118 ? 18.089  -42.569 -19.825  1.000 192.473 ? 118 ALA LLL CB  1 
ATOM 2528 N N   . PRO B 2 119 ? 17.499  -40.929 -22.679  1.000 159.341 ? 119 PRO LLL N   1 
ATOM 2529 C CA  . PRO B 2 119 ? 17.408  -39.573 -23.217  1.000 159.413 ? 119 PRO LLL CA  1 
ATOM 2530 C C   . PRO B 2 119 ? 17.122  -38.509 -22.147  1.000 166.721 ? 119 PRO LLL C   1 
ATOM 2531 O O   . PRO B 2 119 ? 16.401  -38.815 -21.196  1.000 167.839 ? 119 PRO LLL O   1 
ATOM 2532 C CB  . PRO B 2 119 ? 16.229  -39.634 -24.201  1.000 153.939 ? 119 PRO LLL CB  1 
ATOM 2533 C CG  . PRO B 2 119 ? 15.413  -40.845 -23.788  1.000 151.674 ? 119 PRO LLL CG  1 
ATOM 2534 C CD  . PRO B 2 119 ? 16.340  -41.765 -23.023  1.000 153.550 ? 119 PRO LLL CD  1 
ATOM 2535 N N   . SER B 2 120 ? 17.706  -37.313 -22.316  1.000 170.778 ? 120 SER LLL N   1 
ATOM 2536 C CA  . SER B 2 120 ? 17.313  -36.072 -21.599  1.000 176.272 ? 120 SER LLL CA  1 
ATOM 2537 C C   . SER B 2 120 ? 16.228  -35.386 -22.438  1.000 177.590 ? 120 SER LLL C   1 
ATOM 2538 O O   . SER B 2 120 ? 16.509  -34.922 -23.560  1.000 166.766 ? 120 SER LLL O   1 
ATOM 2539 C CB  . SER B 2 120 ? 18.496  -35.158 -21.273  1.000 176.193 ? 120 SER LLL CB  1 
ATOM 2540 O OG  . SER B 2 120 ? 19.428  -35.046 -22.341  1.000 172.842 ? 120 SER LLL OG  1 
ATOM 2541 N N   . VAL B 2 121 ? 15.001  -35.358 -21.925  1.000 182.171 ? 121 VAL LLL N   1 
ATOM 2542 C CA  . VAL B 2 121 ? 13.818  -34.852 -22.673  1.000 176.343 ? 121 VAL LLL CA  1 
ATOM 2543 C C   . VAL B 2 121 ? 13.621  -33.375 -22.325  1.000 173.458 ? 121 VAL LLL C   1 
ATOM 2544 O O   . VAL B 2 121 ? 13.790  -32.985 -21.151  1.000 168.802 ? 121 VAL LLL O   1 
ATOM 2545 C CB  . VAL B 2 121 ? 12.568  -35.700 -22.378  1.000 180.547 ? 121 VAL LLL CB  1 
ATOM 2546 C CG1 . VAL B 2 121 ? 11.411  -35.341 -23.286  1.000 175.042 ? 121 VAL LLL CG1 1 
ATOM 2547 C CG2 . VAL B 2 121 ? 12.878  -37.185 -22.494  1.000 185.272 ? 121 VAL LLL CG2 1 
ATOM 2548 N N   . PHE B 2 122 ? 13.335  -32.571 -23.340  1.000 170.040 ? 122 PHE LLL N   1 
ATOM 2549 C CA  . PHE B 2 122 ? 12.823  -31.197 -23.170  1.000 170.394 ? 122 PHE LLL CA  1 
ATOM 2550 C C   . PHE B 2 122 ? 11.676  -30.990 -24.151  1.000 168.257 ? 122 PHE LLL C   1 
ATOM 2551 O O   . PHE B 2 122 ? 11.585  -31.643 -25.213  1.000 152.353 ? 122 PHE LLL O   1 
ATOM 2552 C CB  . PHE B 2 122 ? 13.900  -30.150 -23.410  1.000 175.928 ? 122 PHE LLL CB  1 
ATOM 2553 C CG  . PHE B 2 122 ? 15.273  -30.462 -22.875  1.000 188.853 ? 122 PHE LLL CG  1 
ATOM 2554 C CD1 . PHE B 2 122 ? 15.718  -29.873 -21.706  1.000 196.947 ? 122 PHE LLL CD1 1 
ATOM 2555 C CD2 . PHE B 2 122 ? 16.154  -31.282 -23.575  1.000 197.375 ? 122 PHE LLL CD2 1 
ATOM 2556 C CE1 . PHE B 2 122 ? 17.007  -30.108 -21.245  1.000 207.292 ? 122 PHE LLL CE1 1 
ATOM 2557 C CE2 . PHE B 2 122 ? 17.438  -31.527 -23.105  1.000 195.029 ? 122 PHE LLL CE2 1 
ATOM 2558 C CZ  . PHE B 2 122 ? 17.866  -30.930 -21.944  1.000 198.025 ? 122 PHE LLL CZ  1 
ATOM 2559 N N   . ILE B 2 123 ? 10.797  -30.079 -23.770  1.000 184.480 ? 123 ILE LLL N   1 
ATOM 2560 C CA  . ILE B 2 123 ? 9.587   -29.715 -24.551  1.000 198.005 ? 123 ILE LLL CA  1 
ATOM 2561 C C   . ILE B 2 123 ? 9.701   -28.216 -24.839  1.000 202.085 ? 123 ILE LLL C   1 
ATOM 2562 O O   . ILE B 2 123 ? 10.142  -27.467 -23.935  1.000 205.925 ? 123 ILE LLL O   1 
ATOM 2563 C CB  . ILE B 2 123 ? 8.287   -30.135 -23.809  1.000 198.427 ? 123 ILE LLL CB  1 
ATOM 2564 C CG1 . ILE B 2 123 ? 7.019   -29.569 -24.468  1.000 198.697 ? 123 ILE LLL CG1 1 
ATOM 2565 C CG2 . ILE B 2 123 ? 8.339   -29.799 -22.323  1.000 193.204 ? 123 ILE LLL CG2 1 
ATOM 2566 C CD1 . ILE B 2 123 ? 5.766   -30.414 -24.262  1.000 195.185 ? 123 ILE LLL CD1 1 
ATOM 2567 N N   . PHE B 2 124 ? 9.373   -27.816 -26.070  1.000 193.768 ? 124 PHE LLL N   1 
ATOM 2568 C CA  . PHE B 2 124 ? 9.285   -26.395 -26.489  1.000 194.333 ? 124 PHE LLL CA  1 
ATOM 2569 C C   . PHE B 2 124 ? 7.839   -26.059 -26.843  1.000 195.173 ? 124 PHE LLL C   1 
ATOM 2570 O O   . PHE B 2 124 ? 7.295   -26.614 -27.798  1.000 193.227 ? 124 PHE LLL O   1 
ATOM 2571 C CB  . PHE B 2 124 ? 10.240  -26.115 -27.648  1.000 188.187 ? 124 PHE LLL CB  1 
ATOM 2572 C CG  . PHE B 2 124 ? 11.668  -26.464 -27.334  1.000 186.677 ? 124 PHE LLL CG  1 
ATOM 2573 C CD1 . PHE B 2 124 ? 12.520  -25.523 -26.780  1.000 187.813 ? 124 PHE LLL CD1 1 
ATOM 2574 C CD2 . PHE B 2 124 ? 12.146  -27.750 -27.535  1.000 185.769 ? 124 PHE LLL CD2 1 
ATOM 2575 C CE1 . PHE B 2 124 ? 13.846  -25.839 -26.504  1.000 187.087 ? 124 PHE LLL CE1 1 
ATOM 2576 C CE2 . PHE B 2 124 ? 13.467  -28.067 -27.250  1.000 189.128 ? 124 PHE LLL CE2 1 
ATOM 2577 C CZ  . PHE B 2 124 ? 14.319  -27.113 -26.732  1.000 185.860 ? 124 PHE LLL CZ  1 
ATOM 2578 N N   . PRO B 2 125 ? 7.193   -25.135 -26.085  1.000 187.333 ? 125 PRO LLL N   1 
ATOM 2579 C CA  . PRO B 2 125 ? 5.892   -24.576 -26.462  1.000 179.218 ? 125 PRO LLL CA  1 
ATOM 2580 C C   . PRO B 2 125 ? 6.051   -23.745 -27.723  1.000 178.073 ? 125 PRO LLL C   1 
ATOM 2581 O O   . PRO B 2 125 ? 7.173   -23.412 -28.092  1.000 191.682 ? 125 PRO LLL O   1 
ATOM 2582 C CB  . PRO B 2 125 ? 5.510   -23.670 -25.291  1.000 185.977 ? 125 PRO LLL CB  1 
ATOM 2583 C CG  . PRO B 2 125 ? 6.835   -23.344 -24.624  1.000 188.682 ? 125 PRO LLL CG  1 
ATOM 2584 C CD  . PRO B 2 125 ? 7.704   -24.566 -24.828  1.000 184.182 ? 125 PRO LLL CD  1 
ATOM 2585 N N   . PRO B 2 126 ? 4.970   -23.384 -28.439  1.000 169.765 ? 126 PRO LLL N   1 
ATOM 2586 C CA  . PRO B 2 126 ? 5.125   -22.708 -29.725  1.000 178.089 ? 126 PRO LLL CA  1 
ATOM 2587 C C   . PRO B 2 126 ? 5.681   -21.288 -29.546  1.000 191.436 ? 126 PRO LLL C   1 
ATOM 2588 O O   . PRO B 2 126 ? 5.464   -20.693 -28.503  1.000 180.983 ? 126 PRO LLL O   1 
ATOM 2589 C CB  . PRO B 2 126 ? 3.733   -22.715 -30.362  1.000 166.745 ? 126 PRO LLL CB  1 
ATOM 2590 C CG  . PRO B 2 126 ? 2.814   -22.911 -29.194  1.000 170.392 ? 126 PRO LLL CG  1 
ATOM 2591 C CD  . PRO B 2 126 ? 3.577   -23.605 -28.077  1.000 164.886 ? 126 PRO LLL CD  1 
ATOM 2592 N N   . SER B 2 127 ? 6.456   -20.826 -30.538  1.000 208.232 ? 127 SER LLL N   1 
ATOM 2593 C CA  . SER B 2 127 ? 6.905   -19.420 -30.679  1.000 218.048 ? 127 SER LLL CA  1 
ATOM 2594 C C   . SER B 2 127 ? 5.682   -18.521 -30.561  1.000 221.946 ? 127 SER LLL C   1 
ATOM 2595 O O   . SER B 2 127 ? 4.587   -18.996 -30.914  1.000 235.710 ? 127 SER LLL O   1 
ATOM 2596 C CB  . SER B 2 127 ? 7.582   -19.177 -31.994  1.000 230.000 ? 127 SER LLL CB  1 
ATOM 2597 O OG  . SER B 2 127 ? 7.323   -17.844 -32.439  1.000 254.663 ? 127 SER LLL OG  1 
ATOM 2598 N N   . ASP B 2 128 ? 5.868   -17.275 -30.135  1.000 216.377 ? 128 ASP LLL N   1 
ATOM 2599 C CA  . ASP B 2 128 ? 4.778   -16.269 -30.134  1.000 221.104 ? 128 ASP LLL CA  1 
ATOM 2600 C C   . ASP B 2 128 ? 4.720   -15.599 -31.506  1.000 213.148 ? 128 ASP LLL C   1 
ATOM 2601 O O   . ASP B 2 128 ? 3.627   -15.142 -31.897  1.000 205.462 ? 128 ASP LLL O   1 
ATOM 2602 C CB  . ASP B 2 128 ? 4.942   -15.294 -28.974  1.000 239.241 ? 128 ASP LLL CB  1 
ATOM 2603 C CG  . ASP B 2 128 ? 4.528   -15.900 -27.642  1.000 249.757 ? 128 ASP LLL CG  1 
ATOM 2604 O OD1 . ASP B 2 128 ? 5.174   -15.575 -26.631  1.000 263.562 ? 128 ASP LLL OD1 1 
ATOM 2605 O OD2 . ASP B 2 128 ? 3.556   -16.690 -27.624  1.000 260.033 ? 128 ASP LLL OD2 1 
ATOM 2606 N N   . GLU B 2 129 ? 5.845   -15.572 -32.219  1.000 213.397 ? 129 GLU LLL N   1 
ATOM 2607 C CA  . GLU B 2 129 ? 5.881   -15.138 -33.640  1.000 228.823 ? 129 GLU LLL CA  1 
ATOM 2608 C C   . GLU B 2 129 ? 5.138   -16.162 -34.500  1.000 215.099 ? 129 GLU LLL C   1 
ATOM 2609 O O   . GLU B 2 129 ? 4.476   -15.758 -35.471  1.000 213.266 ? 129 GLU LLL O   1 
ATOM 2610 C CB  . GLU B 2 129 ? 7.308   -14.999 -34.179  1.000 244.756 ? 129 GLU LLL CB  1 
ATOM 2611 C CG  . GLU B 2 129 ? 8.105   -13.876 -33.549  1.000 257.258 ? 129 GLU LLL CG  1 
ATOM 2612 C CD  . GLU B 2 129 ? 9.096   -14.357 -32.508  1.000 260.932 ? 129 GLU LLL CD  1 
ATOM 2613 O OE1 . GLU B 2 129 ? 8.641   -14.875 -31.453  1.000 264.304 ? 129 GLU LLL OE1 1 
ATOM 2614 O OE2 . GLU B 2 129 ? 10.316  -14.239 -32.773  1.000 258.794 ? 129 GLU LLL OE2 1 
ATOM 2615 N N   . GLN B 2 130 ? 5.285   -17.448 -34.194  1.000 202.656 ? 130 GLN LLL N   1 
ATOM 2616 C CA  . GLN B 2 130 ? 4.691   -18.520 -35.022  1.000 198.434 ? 130 GLN LLL CA  1 
ATOM 2617 C C   . GLN B 2 130 ? 3.170   -18.379 -34.957  1.000 209.073 ? 130 GLN LLL C   1 
ATOM 2618 O O   . GLN B 2 130 ? 2.495   -18.613 -35.978  1.000 217.476 ? 130 GLN LLL O   1 
ATOM 2619 C CB  . GLN B 2 130 ? 5.151   -19.891 -34.543  1.000 180.522 ? 130 GLN LLL CB  1 
ATOM 2620 C CG  . GLN B 2 130 ? 4.702   -20.978 -35.485  1.000 171.309 ? 130 GLN LLL CG  1 
ATOM 2621 C CD  . GLN B 2 130 ? 4.986   -22.339 -34.932  1.000 163.661 ? 130 GLN LLL CD  1 
ATOM 2622 O OE1 . GLN B 2 130 ? 5.539   -22.504 -33.848  1.000 151.714 ? 130 GLN LLL OE1 1 
ATOM 2623 N NE2 . GLN B 2 130 ? 4.652   -23.323 -35.740  1.000 173.017 ? 130 GLN LLL NE2 1 
ATOM 2624 N N   . LEU B 2 131 ? 2.662   -17.969 -33.798  1.000 214.478 ? 131 LEU LLL N   1 
ATOM 2625 C CA  . LEU B 2 131 ? 1.209   -17.904 -33.521  1.000 218.591 ? 131 LEU LLL CA  1 
ATOM 2626 C C   . LEU B 2 131 ? 0.581   -16.764 -34.319  1.000 222.489 ? 131 LEU LLL C   1 
ATOM 2627 O O   . LEU B 2 131 ? -0.646  -16.715 -34.415  1.000 222.777 ? 131 LEU LLL O   1 
ATOM 2628 C CB  . LEU B 2 131 ? 1.029   -17.738 -32.015  1.000 227.116 ? 131 LEU LLL CB  1 
ATOM 2629 C CG  . LEU B 2 131 ? 1.249   -19.029 -31.231  1.000 233.771 ? 131 LEU LLL CG  1 
ATOM 2630 C CD1 . LEU B 2 131 ? 1.644   -18.747 -29.788  1.000 238.418 ? 131 LEU LLL CD1 1 
ATOM 2631 C CD2 . LEU B 2 131 ? 0.002   -19.900 -31.290  1.000 244.075 ? 131 LEU LLL CD2 1 
ATOM 2632 N N   . LYS B 2 132 ? 1.402   -15.903 -34.907  1.000 228.801 ? 132 LYS LLL N   1 
ATOM 2633 C CA  . LYS B 2 132 ? 0.929   -14.843 -35.827  1.000 245.401 ? 132 LYS LLL CA  1 
ATOM 2634 C C   . LYS B 2 132 ? 0.766   -15.425 -37.243  1.000 246.090 ? 132 LYS LLL C   1 
ATOM 2635 O O   . LYS B 2 132 ? -0.029  -14.843 -37.999  1.000 262.851 ? 132 LYS LLL O   1 
ATOM 2636 C CB  . LYS B 2 132 ? 1.880   -13.646 -35.756  1.000 256.003 ? 132 LYS LLL CB  1 
ATOM 2637 C CG  . LYS B 2 132 ? 2.162   -13.129 -34.348  1.000 253.242 ? 132 LYS LLL CG  1 
ATOM 2638 C CD  . LYS B 2 132 ? 2.893   -11.791 -34.313  1.000 257.955 ? 132 LYS LLL CD  1 
ATOM 2639 C CE  . LYS B 2 132 ? 1.974   -10.590 -34.206  1.000 264.013 ? 132 LYS LLL CE  1 
ATOM 2640 N NZ  . LYS B 2 132 ? 2.725   -9.313  -34.279  1.000 268.805 ? 132 LYS LLL NZ  1 
ATOM 2641 N N   . SER B 2 133 ? 1.454   -16.523 -37.596  1.000 234.011 ? 133 SER LLL N   1 
ATOM 2642 C CA  . SER B 2 133 ? 1.280   -17.228 -38.900  1.000 237.884 ? 133 SER LLL CA  1 
ATOM 2643 C C   . SER B 2 133 ? -0.099  -17.903 -38.936  1.000 236.561 ? 133 SER LLL C   1 
ATOM 2644 O O   . SER B 2 133 ? -0.563  -18.243 -40.042  1.000 247.625 ? 133 SER LLL O   1 
ATOM 2645 C CB  . SER B 2 133 ? 2.374   -18.246 -39.185  1.000 238.845 ? 133 SER LLL CB  1 
ATOM 2646 O OG  . SER B 2 133 ? 3.629   -17.843 -38.661  1.000 251.440 ? 133 SER LLL OG  1 
ATOM 2647 N N   . GLY B 2 134 ? -0.725  -18.094 -37.770  1.000 230.770 ? 134 GLY LLL N   1 
ATOM 2648 C CA  . GLY B 2 134 ? -1.988  -18.834 -37.605  1.000 223.653 ? 134 GLY LLL CA  1 
ATOM 2649 C C   . GLY B 2 134 ? -1.726  -20.297 -37.296  1.000 214.341 ? 134 GLY LLL C   1 
ATOM 2650 O O   . GLY B 2 134 ? -2.701  -21.069 -37.297  1.000 205.832 ? 134 GLY LLL O   1 
ATOM 2651 N N   . THR B 2 135 ? -0.462  -20.662 -37.042  1.000 214.588 ? 135 THR LLL N   1 
ATOM 2652 C CA  . THR B 2 135 ? -0.003  -22.065 -36.831  1.000 217.032 ? 135 THR LLL CA  1 
ATOM 2653 C C   . THR B 2 135 ? 0.793   -22.178 -35.529  1.000 219.713 ? 135 THR LLL C   1 
ATOM 2654 O O   . THR B 2 135 ? 1.433   -21.182 -35.150  1.000 225.801 ? 135 THR LLL O   1 
ATOM 2655 C CB  . THR B 2 135 ? 0.852   -22.581 -37.994  1.000 218.596 ? 135 THR LLL CB  1 
ATOM 2656 O OG1 . THR B 2 135 ? 1.308   -23.864 -37.567  1.000 215.881 ? 135 THR LLL OG1 1 
ATOM 2657 C CG2 . THR B 2 135 ? 2.029   -21.702 -38.366  1.000 219.854 ? 135 THR LLL CG2 1 
ATOM 2658 N N   . ALA B 2 136 ? 0.744   -23.344 -34.876  1.000 215.516 ? 136 ALA LLL N   1 
ATOM 2659 C CA  . ALA B 2 136 ? 1.413   -23.614 -33.583  1.000 209.114 ? 136 ALA LLL CA  1 
ATOM 2660 C C   . ALA B 2 136 ? 2.024   -25.010 -33.606  1.000 201.325 ? 136 ALA LLL C   1 
ATOM 2661 O O   . ALA B 2 136 ? 1.295   -25.999 -33.863  1.000 201.591 ? 136 ALA LLL O   1 
ATOM 2662 C CB  . ALA B 2 136 ? 0.430   -23.485 -32.458  1.000 205.767 ? 136 ALA LLL CB  1 
ATOM 2663 N N   . SER B 2 137 ? 3.318   -25.085 -33.335  1.000 190.942 ? 137 SER LLL N   1 
ATOM 2664 C CA  . SER B 2 137 ? 4.060   -26.361 -33.314  1.000 182.896 ? 137 SER LLL CA  1 
ATOM 2665 C C   . SER B 2 137 ? 4.604   -26.572 -31.908  1.000 182.018 ? 137 SER LLL C   1 
ATOM 2666 O O   . SER B 2 137 ? 5.207   -25.638 -31.356  1.000 176.381 ? 137 SER LLL O   1 
ATOM 2667 C CB  . SER B 2 137 ? 5.133   -26.369 -34.359  1.000 185.074 ? 137 SER LLL CB  1 
ATOM 2668 O OG  . SER B 2 137 ? 4.572   -26.621 -35.639  1.000 192.499 ? 137 SER LLL OG  1 
ATOM 2669 N N   . VAL B 2 138 ? 4.337   -27.745 -31.341  1.000 186.690 ? 138 VAL LLL N   1 
ATOM 2670 C CA  . VAL B 2 138 ? 4.951   -28.201 -30.064  1.000 190.491 ? 138 VAL LLL CA  1 
ATOM 2671 C C   . VAL B 2 138 ? 5.984   -29.256 -30.447  1.000 177.342 ? 138 VAL LLL C   1 
ATOM 2672 O O   . VAL B 2 138 ? 5.611   -30.211 -31.133  1.000 179.770 ? 138 VAL LLL O   1 
ATOM 2673 C CB  . VAL B 2 138 ? 3.899   -28.736 -29.067  1.000 197.473 ? 138 VAL LLL CB  1 
ATOM 2674 C CG1 . VAL B 2 138 ? 4.392   -28.629 -27.629  1.000 203.307 ? 138 VAL LLL CG1 1 
ATOM 2675 C CG2 . VAL B 2 138 ? 2.554   -28.036 -29.212  1.000 201.800 ? 138 VAL LLL CG2 1 
ATOM 2676 N N   . VAL B 2 139 ? 7.236   -29.085 -30.045  1.000 168.235 ? 139 VAL LLL N   1 
ATOM 2677 C CA  . VAL B 2 139 ? 8.287   -30.096 -30.346  1.000 178.570 ? 139 VAL LLL CA  1 
ATOM 2678 C C   . VAL B 2 139 ? 8.815   -30.669 -29.026  1.000 179.901 ? 139 VAL LLL C   1 
ATOM 2679 O O   . VAL B 2 139 ? 9.017   -29.902 -28.057  1.000 167.155 ? 139 VAL LLL O   1 
ATOM 2680 C CB  . VAL B 2 139 ? 9.416   -29.525 -31.222  1.000 182.952 ? 139 VAL LLL CB  1 
ATOM 2681 C CG1 . VAL B 2 139 ? 9.961   -28.232 -30.646  1.000 201.105 ? 139 VAL LLL CG1 1 
ATOM 2682 C CG2 . VAL B 2 139 ? 10.547  -30.519 -31.410  1.000 176.117 ? 139 VAL LLL CG2 1 
ATOM 2683 N N   . CYS B 2 140 ? 9.020   -31.986 -29.009  1.000 186.268 ? 140 CYS LLL N   1 
ATOM 2684 C CA  . CYS B 2 140 ? 9.681   -32.727 -27.912  1.000 188.196 ? 140 CYS LLL CA  1 
ATOM 2685 C C   . CYS B 2 140 ? 11.008  -33.291 -28.416  1.000 181.054 ? 140 CYS LLL C   1 
ATOM 2686 O O   . CYS B 2 140 ? 11.021  -33.899 -29.491  1.000 163.906 ? 140 CYS LLL O   1 
ATOM 2687 C CB  . CYS B 2 140 ? 8.797   -33.857 -27.419  1.000 196.303 ? 140 CYS LLL CB  1 
ATOM 2688 S SG  . CYS B 2 140 ? 9.026   -34.203 -25.659  1.000 204.014 ? 140 CYS LLL SG  1 
ATOM 2689 N N   . LEU B 2 141 ? 12.064  -33.112 -27.631  1.000 174.718 ? 141 LEU LLL N   1 
ATOM 2690 C CA  . LEU B 2 141 ? 13.450  -33.440 -28.025  1.000 160.426 ? 141 LEU LLL CA  1 
ATOM 2691 C C   . LEU B 2 141 ? 14.010  -34.480 -27.047  1.000 158.359 ? 141 LEU LLL C   1 
ATOM 2692 O O   . LEU B 2 141 ? 14.028  -34.194 -25.825  1.000 164.080 ? 141 LEU LLL O   1 
ATOM 2693 C CB  . LEU B 2 141 ? 14.256  -32.138 -28.026  1.000 156.452 ? 141 LEU LLL CB  1 
ATOM 2694 C CG  . LEU B 2 141 ? 15.765  -32.305 -27.889  1.000 159.053 ? 141 LEU LLL CG  1 
ATOM 2695 C CD1 . LEU B 2 141 ? 16.343  -33.064 -29.085  1.000 163.683 ? 141 LEU LLL CD1 1 
ATOM 2696 C CD2 . LEU B 2 141 ? 16.434  -30.958 -27.693  1.000 156.352 ? 141 LEU LLL CD2 1 
ATOM 2697 N N   . LEU B 2 142 ? 14.424  -35.639 -27.573  1.000 151.384 ? 142 LEU LLL N   1 
ATOM 2698 C CA  . LEU B 2 142 ? 15.165  -36.701 -26.837  1.000 158.539 ? 142 LEU LLL CA  1 
ATOM 2699 C C   . LEU B 2 142 ? 16.648  -36.617 -27.217  1.000 165.254 ? 142 LEU LLL C   1 
ATOM 2700 O O   . LEU B 2 142 ? 16.977  -36.809 -28.391  1.000 173.811 ? 142 LEU LLL O   1 
ATOM 2701 C CB  . LEU B 2 142 ? 14.603  -38.079 -27.195  1.000 158.011 ? 142 LEU LLL CB  1 
ATOM 2702 C CG  . LEU B 2 142 ? 13.257  -38.442 -26.572  1.000 159.063 ? 142 LEU LLL CG  1 
ATOM 2703 C CD1 . LEU B 2 142 ? 12.139  -37.577 -27.141  1.000 161.195 ? 142 LEU LLL CD1 1 
ATOM 2704 C CD2 . LEU B 2 142 ? 12.956  -39.915 -26.814  1.000 158.214 ? 142 LEU LLL CD2 1 
ATOM 2705 N N   . ASN B 2 143 ? 17.515  -36.346 -26.249  1.000 167.859 ? 143 ASN LLL N   1 
ATOM 2706 C CA  . ASN B 2 143 ? 18.895  -35.880 -26.501  1.000 169.057 ? 143 ASN LLL CA  1 
ATOM 2707 C C   . ASN B 2 143 ? 19.882  -36.933 -26.016  1.000 166.414 ? 143 ASN LLL C   1 
ATOM 2708 O O   . ASN B 2 143 ? 19.818  -37.298 -24.846  1.000 165.465 ? 143 ASN LLL O   1 
ATOM 2709 C CB  . ASN B 2 143 ? 19.122  -34.537 -25.816  1.000 176.233 ? 143 ASN LLL CB  1 
ATOM 2710 C CG  . ASN B 2 143 ? 20.149  -33.693 -26.525  1.000 188.138 ? 143 ASN LLL CG  1 
ATOM 2711 O OD1 . ASN B 2 143 ? 20.202  -33.677 -27.756  1.000 197.730 ? 143 ASN LLL OD1 1 
ATOM 2712 N ND2 . ASN B 2 143 ? 20.964  -33.000 -25.748  1.000 195.969 ? 143 ASN LLL ND2 1 
ATOM 2713 N N   . ASN B 2 144 ? 20.776  -37.375 -26.894  1.000 178.152 ? 144 ASN LLL N   1 
ATOM 2714 C CA  . ASN B 2 144 ? 21.957  -38.209 -26.539  1.000 184.715 ? 144 ASN LLL CA  1 
ATOM 2715 C C   . ASN B 2 144 ? 21.487  -39.500 -25.866  1.000 181.509 ? 144 ASN LLL C   1 
ATOM 2716 O O   . ASN B 2 144 ? 21.650  -39.621 -24.626  1.000 171.276 ? 144 ASN LLL O   1 
ATOM 2717 C CB  . ASN B 2 144 ? 22.940  -37.456 -25.638  1.000 188.210 ? 144 ASN LLL CB  1 
ATOM 2718 C CG  . ASN B 2 144 ? 23.395  -36.141 -26.235  1.000 200.243 ? 144 ASN LLL CG  1 
ATOM 2719 O OD1 . ASN B 2 144 ? 23.408  -35.953 -27.462  1.000 203.475 ? 144 ASN LLL OD1 1 
ATOM 2720 N ND2 . ASN B 2 144 ? 23.769  -35.224 -25.361  1.000 205.856 ? 144 ASN LLL ND2 1 
ATOM 2721 N N   . PHE B 2 145 ? 20.944  -40.425 -26.664  1.000 176.121 ? 145 PHE LLL N   1 
ATOM 2722 C CA  . PHE B 2 145 ? 20.445  -41.731 -26.178  1.000 175.556 ? 145 PHE LLL CA  1 
ATOM 2723 C C   . PHE B 2 145 ? 20.721  -42.835 -27.192  1.000 165.803 ? 145 PHE LLL C   1 
ATOM 2724 O O   . PHE B 2 145 ? 20.825  -42.568 -28.384  1.000 158.946 ? 145 PHE LLL O   1 
ATOM 2725 C CB  . PHE B 2 145 ? 18.947  -41.660 -25.892  1.000 175.518 ? 145 PHE LLL CB  1 
ATOM 2726 C CG  . PHE B 2 145 ? 18.083  -41.547 -27.111  1.000 163.345 ? 145 PHE LLL CG  1 
ATOM 2727 C CD1 . PHE B 2 145 ? 17.425  -42.665 -27.590  1.000 162.564 ? 145 PHE LLL CD1 1 
ATOM 2728 C CD2 . PHE B 2 145 ? 17.888  -40.319 -27.728  1.000 156.175 ? 145 PHE LLL CD2 1 
ATOM 2729 C CE1 . PHE B 2 145 ? 16.594  -42.564 -28.688  1.000 168.663 ? 145 PHE LLL CE1 1 
ATOM 2730 C CE2 . PHE B 2 145 ? 17.053  -40.221 -28.827  1.000 160.599 ? 145 PHE LLL CE2 1 
ATOM 2731 C CZ  . PHE B 2 145 ? 16.412  -41.344 -29.308  1.000 168.479 ? 145 PHE LLL CZ  1 
ATOM 2732 N N   . TYR B 2 146 ? 20.835  -44.050 -26.665  1.000 172.558 ? 146 TYR LLL N   1 
ATOM 2733 C CA  . TYR B 2 146 ? 20.948  -45.321 -27.423  1.000 168.210 ? 146 TYR LLL CA  1 
ATOM 2734 C C   . TYR B 2 146 ? 20.160  -46.375 -26.645  1.000 161.784 ? 146 TYR LLL C   1 
ATOM 2735 O O   . TYR B 2 146 ? 20.103  -46.344 -25.413  1.000 163.870 ? 146 TYR LLL O   1 
ATOM 2736 C CB  . TYR B 2 146 ? 22.422  -45.700 -27.647  1.000 175.870 ? 146 TYR LLL CB  1 
ATOM 2737 C CG  . TYR B 2 146 ? 22.640  -46.906 -28.534  1.000 177.406 ? 146 TYR LLL CG  1 
ATOM 2738 C CD1 . TYR B 2 146 ? 22.934  -46.768 -29.876  1.000 167.912 ? 146 TYR LLL CD1 1 
ATOM 2739 C CD2 . TYR B 2 146 ? 22.511  -48.196 -28.043  1.000 184.419 ? 146 TYR LLL CD2 1 
ATOM 2740 C CE1 . TYR B 2 146 ? 23.090  -47.870 -30.701  1.000 169.887 ? 146 TYR LLL CE1 1 
ATOM 2741 C CE2 . TYR B 2 146 ? 22.668  -49.309 -28.855  1.000 182.865 ? 146 TYR LLL CE2 1 
ATOM 2742 C CZ  . TYR B 2 146 ? 22.961  -49.147 -30.194  1.000 174.222 ? 146 TYR LLL CZ  1 
ATOM 2743 O OH  . TYR B 2 146 ? 23.120  -50.234 -31.006  1.000 177.392 ? 146 TYR LLL OH  1 
ATOM 2744 N N   . PRO B 2 147 ? 19.517  -47.342 -27.323  1.000 154.943 ? 147 PRO LLL N   1 
ATOM 2745 C CA  . PRO B 2 147 ? 19.379  -47.317 -28.771  1.000 162.929 ? 147 PRO LLL CA  1 
ATOM 2746 C C   . PRO B 2 147 ? 18.394  -46.246 -29.268  1.000 171.778 ? 147 PRO LLL C   1 
ATOM 2747 O O   . PRO B 2 147 ? 17.870  -45.513 -28.472  1.000 171.637 ? 147 PRO LLL O   1 
ATOM 2748 C CB  . PRO B 2 147 ? 18.938  -48.762 -29.067  1.000 165.658 ? 147 PRO LLL CB  1 
ATOM 2749 C CG  . PRO B 2 147 ? 18.199  -49.231 -27.840  1.000 157.995 ? 147 PRO LLL CG  1 
ATOM 2750 C CD  . PRO B 2 147 ? 18.899  -48.522 -26.710  1.000 161.391 ? 147 PRO LLL CD  1 
ATOM 2751 N N   . ARG B 2 148 ? 18.205  -46.174 -30.587  1.000 188.289 ? 148 ARG LLL N   1 
ATOM 2752 C CA  . ARG B 2 148 ? 17.201  -45.303 -31.249  1.000 194.947 ? 148 ARG LLL CA  1 
ATOM 2753 C C   . ARG B 2 148 ? 15.798  -45.758 -30.832  1.000 189.383 ? 148 ARG LLL C   1 
ATOM 2754 O O   . ARG B 2 148 ? 14.984  -44.865 -30.571  1.000 204.388 ? 148 ARG LLL O   1 
ATOM 2755 C CB  . ARG B 2 148 ? 17.349  -45.340 -32.775  1.000 213.628 ? 148 ARG LLL CB  1 
ATOM 2756 C CG  . ARG B 2 148 ? 16.285  -44.546 -33.527  1.000 231.689 ? 148 ARG LLL CG  1 
ATOM 2757 C CD  . ARG B 2 148 ? 14.984  -45.268 -33.867  1.000 246.581 ? 148 ARG LLL CD  1 
ATOM 2758 N NE  . ARG B 2 148 ? 13.939  -44.380 -34.391  1.000 257.675 ? 148 ARG LLL NE  1 
ATOM 2759 C CZ  . ARG B 2 148 ? 12.815  -44.003 -33.758  1.000 251.299 ? 148 ARG LLL CZ  1 
ATOM 2760 N NH1 . ARG B 2 148 ? 12.348  -44.686 -32.729  1.000 230.238 ? 148 ARG LLL NH1 1 
ATOM 2761 N NH2 . ARG B 2 148 ? 12.037  -43.085 -34.312  1.000 265.923 ? 148 ARG LLL NH2 1 
ATOM 2762 N N   . GLU B 2 149 ? 15.527  -47.074 -30.786  1.000 180.551 ? 149 GLU LLL N   1 
ATOM 2763 C CA  . GLU B 2 149 ? 14.205  -47.673 -30.416  1.000 193.336 ? 149 GLU LLL CA  1 
ATOM 2764 C C   . GLU B 2 149 ? 13.603  -46.893 -29.227  1.000 201.964 ? 149 GLU LLL C   1 
ATOM 2765 O O   . GLU B 2 149 ? 14.140  -47.038 -28.106  1.000 223.417 ? 149 GLU LLL O   1 
ATOM 2766 C CB  . GLU B 2 149 ? 14.393  -49.168 -30.100  1.000 210.129 ? 149 GLU LLL CB  1 
ATOM 2767 C CG  . GLU B 2 149 ? 13.209  -49.855 -29.389  1.000 232.183 ? 149 GLU LLL CG  1 
ATOM 2768 C CD  . GLU B 2 149 ? 13.499  -50.989 -28.392  1.000 240.741 ? 149 GLU LLL CD  1 
ATOM 2769 O OE1 . GLU B 2 149 ? 14.210  -51.947 -28.775  1.000 254.076 ? 149 GLU LLL OE1 1 
ATOM 2770 O OE2 . GLU B 2 149 ? 13.000  -50.933 -27.223  1.000 214.608 ? 149 GLU LLL OE2 1 
ATOM 2771 N N   . ALA B 2 150 ? 12.538  -46.096 -29.436  1.000 190.990 ? 150 ALA LLL N   1 
ATOM 2772 C CA  . ALA B 2 150 ? 11.927  -45.189 -28.422  1.000 176.281 ? 150 ALA LLL CA  1 
ATOM 2773 C C   . ALA B 2 150 ? 10.536  -44.739 -28.872  1.000 165.261 ? 150 ALA LLL C   1 
ATOM 2774 O O   . ALA B 2 150 ? 10.417  -44.353 -30.038  1.000 156.256 ? 150 ALA LLL O   1 
ATOM 2775 C CB  . ALA B 2 150 ? 12.806  -43.980 -28.185  1.000 170.868 ? 150 ALA LLL CB  1 
ATOM 2776 N N   . LYS B 2 151 ? 9.533   -44.777 -27.984  1.000 166.015 ? 151 LYS LLL N   1 
ATOM 2777 C CA  . LYS B 2 151 ? 8.141   -44.357 -28.315  1.000 175.453 ? 151 LYS LLL CA  1 
ATOM 2778 C C   . LYS B 2 151 ? 7.848   -43.037 -27.601  1.000 172.353 ? 151 LYS LLL C   1 
ATOM 2779 O O   . LYS B 2 151 ? 8.059   -42.976 -26.390  1.000 177.436 ? 151 LYS LLL O   1 
ATOM 2780 C CB  . LYS B 2 151 ? 7.106   -45.461 -28.037  1.000 181.693 ? 151 LYS LLL CB  1 
ATOM 2781 C CG  . LYS B 2 151 ? 6.592   -45.615 -26.612  1.000 193.169 ? 151 LYS LLL CG  1 
ATOM 2782 C CD  . LYS B 2 151 ? 5.305   -44.851 -26.269  1.000 198.746 ? 151 LYS LLL CD  1 
ATOM 2783 C CE  . LYS B 2 151 ? 4.838   -45.087 -24.843  1.000 199.439 ? 151 LYS LLL CE  1 
ATOM 2784 N NZ  . LYS B 2 151 ? 4.310   -43.864 -24.185  1.000 190.201 ? 151 LYS LLL NZ  1 
ATOM 2785 N N   . VAL B 2 152 ? 7.421   -42.025 -28.363  1.000 178.270 ? 152 VAL LLL N   1 
ATOM 2786 C CA  . VAL B 2 152 ? 7.011   -40.675 -27.874  1.000 179.031 ? 152 VAL LLL CA  1 
ATOM 2787 C C   . VAL B 2 152 ? 5.517   -40.481 -28.191  1.000 174.781 ? 152 VAL LLL C   1 
ATOM 2788 O O   . VAL B 2 152 ? 5.149   -40.460 -29.364  1.000 166.911 ? 152 VAL LLL O   1 
ATOM 2789 C CB  . VAL B 2 152 ? 7.902   -39.564 -28.478  1.000 174.556 ? 152 VAL LLL CB  1 
ATOM 2790 C CG1 . VAL B 2 152 ? 7.436   -38.186 -28.069  1.000 177.382 ? 152 VAL LLL CG1 1 
ATOM 2791 C CG2 . VAL B 2 152 ? 9.374   -39.726 -28.119  1.000 170.846 ? 152 VAL LLL CG2 1 
ATOM 2792 N N   . GLN B 2 153 ? 4.691   -40.302 -27.161  1.000 182.025 ? 153 GLN LLL N   1 
ATOM 2793 C CA  . GLN B 2 153 ? 3.229   -40.040 -27.277  1.000 190.476 ? 153 GLN LLL CA  1 
ATOM 2794 C C   . GLN B 2 153 ? 2.884   -38.622 -26.818  1.000 184.600 ? 153 GLN LLL C   1 
ATOM 2795 O O   . GLN B 2 153 ? 3.313   -38.234 -25.712  1.000 181.771 ? 153 GLN LLL O   1 
ATOM 2796 C CB  . GLN B 2 153 ? 2.447   -41.006 -26.395  1.000 204.821 ? 153 GLN LLL CB  1 
ATOM 2797 C CG  . GLN B 2 153 ? 2.855   -42.447 -26.622  1.000 218.237 ? 153 GLN LLL CG  1 
ATOM 2798 C CD  . GLN B 2 153 ? 1.746   -43.421 -26.312  1.000 218.061 ? 153 GLN LLL CD  1 
ATOM 2799 O OE1 . GLN B 2 153 ? 1.584   -43.892 -25.189  1.000 214.730 ? 153 GLN LLL OE1 1 
ATOM 2800 N NE2 . GLN B 2 153 ? 0.960   -43.734 -27.327  1.000 217.971 ? 153 GLN LLL NE2 1 
ATOM 2801 N N   . TRP B 2 154 ? 2.099   -37.900 -27.625  1.000 181.231 ? 154 TRP LLL N   1 
ATOM 2802 C CA  . TRP B 2 154 ? 1.551   -36.554 -27.298  1.000 180.007 ? 154 TRP LLL CA  1 
ATOM 2803 C C   . TRP B 2 154 ? 0.223   -36.721 -26.575  1.000 184.249 ? 154 TRP LLL C   1 
ATOM 2804 O O   . TRP B 2 154 ? -0.588  -37.524 -27.050  1.000 181.865 ? 154 TRP LLL O   1 
ATOM 2805 C CB  . TRP B 2 154 ? 1.357   -35.681 -28.539  1.000 176.402 ? 154 TRP LLL CB  1 
ATOM 2806 C CG  . TRP B 2 154 ? 2.640   -35.127 -29.061  1.000 170.581 ? 154 TRP LLL CG  1 
ATOM 2807 C CD1 . TRP B 2 154 ? 3.318   -35.556 -30.157  1.000 175.589 ? 154 TRP LLL CD1 1 
ATOM 2808 C CD2 . TRP B 2 154 ? 3.422   -34.069 -28.487  1.000 173.174 ? 154 TRP LLL CD2 1 
ATOM 2809 N NE1 . TRP B 2 154 ? 4.465   -34.829 -30.311  1.000 185.315 ? 154 TRP LLL NE1 1 
ATOM 2810 C CE2 . TRP B 2 154 ? 4.560   -33.914 -29.298  1.000 172.938 ? 154 TRP LLL CE2 1 
ATOM 2811 C CE3 . TRP B 2 154 ? 3.273   -33.230 -27.379  1.000 184.359 ? 154 TRP LLL CE3 1 
ATOM 2812 C CZ2 . TRP B 2 154 ? 5.544   -32.966 -29.038  1.000 174.780 ? 154 TRP LLL CZ2 1 
ATOM 2813 C CZ3 . TRP B 2 154 ? 4.252   -32.298 -27.113  1.000 181.217 ? 154 TRP LLL CZ3 1 
ATOM 2814 C CH2 . TRP B 2 154 ? 5.371   -32.167 -27.936  1.000 176.208 ? 154 TRP LLL CH2 1 
ATOM 2815 N N   . LYS B 2 155 ? 0.023   -35.957 -25.496  1.000 189.925 ? 155 LYS LLL N   1 
ATOM 2816 C CA  . LYS B 2 155 ? -1.198  -35.988 -24.642  1.000 190.512 ? 155 LYS LLL CA  1 
ATOM 2817 C C   . LYS B 2 155 ? -1.705  -34.549 -24.483  1.000 175.185 ? 155 LYS LLL C   1 
ATOM 2818 O O   . LYS B 2 155 ? -1.365  -33.885 -23.513  1.000 169.035 ? 155 LYS LLL O   1 
ATOM 2819 C CB  . LYS B 2 155 ? -0.902  -36.694 -23.311  1.000 205.735 ? 155 LYS LLL CB  1 
ATOM 2820 C CG  . LYS B 2 155 ? -0.197  -38.051 -23.412  1.000 216.008 ? 155 LYS LLL CG  1 
ATOM 2821 C CD  . LYS B 2 155 ? 0.056   -38.772 -22.069  1.000 215.917 ? 155 LYS LLL CD  1 
ATOM 2822 C CE  . LYS B 2 155 ? -1.201  -39.003 -21.249  1.000 220.404 ? 155 LYS LLL CE  1 
ATOM 2823 N NZ  . LYS B 2 155 ? -0.978  -39.920 -20.107  1.000 219.142 ? 155 LYS LLL NZ  1 
ATOM 2824 N N   . VAL B 2 156 ? -2.452  -34.058 -25.463  1.000 174.035 ? 156 VAL LLL N   1 
ATOM 2825 C CA  . VAL B 2 156 ? -2.986  -32.670 -25.445  1.000 169.465 ? 156 VAL LLL CA  1 
ATOM 2826 C C   . VAL B 2 156 ? -4.253  -32.732 -24.616  1.000 164.461 ? 156 VAL LLL C   1 
ATOM 2827 O O   . VAL B 2 156 ? -5.250  -33.321 -25.087  1.000 156.292 ? 156 VAL LLL O   1 
ATOM 2828 C CB  . VAL B 2 156 ? -3.249  -32.078 -26.844  1.000 181.457 ? 156 VAL LLL CB  1 
ATOM 2829 C CG1 . VAL B 2 156 ? -3.759  -30.647 -26.752  1.000 180.794 ? 156 VAL LLL CG1 1 
ATOM 2830 C CG2 . VAL B 2 156 ? -2.007  -32.123 -27.729  1.000 189.381 ? 156 VAL LLL CG2 1 
ATOM 2831 N N   . ASP B 2 157 ? -4.153  -32.173 -23.409  1.000 165.555 ? 157 ASP LLL N   1 
ATOM 2832 C CA  . ASP B 2 157 ? -5.258  -31.927 -22.442  1.000 152.669 ? 157 ASP LLL CA  1 
ATOM 2833 C C   . ASP B 2 157 ? -5.630  -33.238 -21.749  1.000 149.064 ? 157 ASP LLL C   1 
ATOM 2834 O O   . ASP B 2 157 ? -6.831  -33.493 -21.467  1.000 136.812 ? 157 ASP LLL O   1 
ATOM 2835 C CB  . ASP B 2 157 ? -6.406  -31.199 -23.121  1.000 150.092 ? 157 ASP LLL CB  1 
ATOM 2836 C CG  . ASP B 2 157 ? -6.741  -30.016 -22.258  1.000 158.388 ? 157 ASP LLL CG  1 
ATOM 2837 O OD1 . ASP B 2 157 ? -6.934  -28.919 -22.789  1.000 152.231 ? 157 ASP LLL OD1 1 
ATOM 2838 O OD2 . ASP B 2 157 ? -6.717  -30.193 -21.047  1.000 183.180 ? 157 ASP LLL OD2 1 
ATOM 2839 N N   . ASN B 2 158 ? -4.581  -34.017 -21.495  1.000 158.769 ? 158 ASN LLL N   1 
ATOM 2840 C CA  . ASN B 2 158 ? -4.595  -35.397 -20.955  1.000 172.464 ? 158 ASN LLL CA  1 
ATOM 2841 C C   . ASN B 2 158 ? -5.328  -36.385 -21.873  1.000 182.977 ? 158 ASN LLL C   1 
ATOM 2842 O O   . ASN B 2 158 ? -5.826  -37.389 -21.331  1.000 188.739 ? 158 ASN LLL O   1 
ATOM 2843 C CB  . ASN B 2 158 ? -5.212  -35.433 -19.566  1.000 185.562 ? 158 ASN LLL CB  1 
ATOM 2844 C CG  . ASN B 2 158 ? -4.443  -36.378 -18.672  1.000 195.926 ? 158 ASN LLL CG  1 
ATOM 2845 O OD1 . ASN B 2 158 ? -3.579  -37.123 -19.151  1.000 190.528 ? 158 ASN LLL OD1 1 
ATOM 2846 N ND2 . ASN B 2 158 ? -4.727  -36.319 -17.378  1.000 202.200 ? 158 ASN LLL ND2 1 
ATOM 2847 N N   . ALA B 2 159 ? -5.366  -36.146 -23.195  1.000 192.107 ? 159 ALA LLL N   1 
ATOM 2848 C CA  . ALA B 2 159 ? -5.937  -37.079 -24.199  1.000 177.865 ? 159 ALA LLL CA  1 
ATOM 2849 C C   . ALA B 2 159 ? -4.822  -37.471 -25.156  1.000 170.658 ? 159 ALA LLL C   1 
ATOM 2850 O O   . ALA B 2 159 ? -4.184  -36.562 -25.673  1.000 156.482 ? 159 ALA LLL O   1 
ATOM 2851 C CB  . ALA B 2 159 ? -7.095  -36.460 -24.943  1.000 173.142 ? 159 ALA LLL CB  1 
ATOM 2852 N N   . LEU B 2 160 ? -4.627  -38.767 -25.394  1.000 183.136 ? 160 LEU LLL N   1 
ATOM 2853 C CA  . LEU B 2 160 ? -3.642  -39.255 -26.397  1.000 193.620 ? 160 LEU LLL CA  1 
ATOM 2854 C C   . LEU B 2 160 ? -4.089  -38.802 -27.792  1.000 190.220 ? 160 LEU LLL C   1 
ATOM 2855 O O   . LEU B 2 160 ? -5.285  -38.983 -28.131  1.000 175.282 ? 160 LEU LLL O   1 
ATOM 2856 C CB  . LEU B 2 160 ? -3.479  -40.779 -26.330  1.000 199.657 ? 160 LEU LLL CB  1 
ATOM 2857 C CG  . LEU B 2 160 ? -2.365  -41.363 -27.209  1.000 204.455 ? 160 LEU LLL CG  1 
ATOM 2858 C CD1 . LEU B 2 160 ? -1.074  -40.556 -27.125  1.000 194.937 ? 160 LEU LLL CD1 1 
ATOM 2859 C CD2 . LEU B 2 160 ? -2.094  -42.811 -26.848  1.000 211.345 ? 160 LEU LLL CD2 1 
ATOM 2860 N N   . GLN B 2 161 ? -3.146  -38.226 -28.543  1.000 181.874 ? 161 GLN LLL N   1 
ATOM 2861 C CA  . GLN B 2 161 ? -3.350  -37.738 -29.926  1.000 185.973 ? 161 GLN LLL CA  1 
ATOM 2862 C C   . GLN B 2 161 ? -2.501  -38.585 -30.896  1.000 192.389 ? 161 GLN LLL C   1 
ATOM 2863 O O   . GLN B 2 161 ? -1.422  -39.052 -30.483  1.000 184.662 ? 161 GLN LLL O   1 
ATOM 2864 C CB  . GLN B 2 161 ? -3.072  -36.234 -29.928  1.000 177.181 ? 161 GLN LLL CB  1 
ATOM 2865 C CG  . GLN B 2 161 ? -3.967  -35.443 -28.978  1.000 178.269 ? 161 GLN LLL CG  1 
ATOM 2866 C CD  . GLN B 2 161 ? -5.348  -35.132 -29.522  1.000 181.369 ? 161 GLN LLL CD  1 
ATOM 2867 O OE1 . GLN B 2 161 ? -5.579  -35.048 -30.725  1.000 183.559 ? 161 GLN LLL OE1 1 
ATOM 2868 N NE2 . GLN B 2 161 ? -6.302  -34.980 -28.621  1.000 189.469 ? 161 GLN LLL NE2 1 
ATOM 2869 N N   . SER B 2 162 ? -2.996  -38.820 -32.125  1.000 203.189 ? 162 SER LLL N   1 
ATOM 2870 C CA  . SER B 2 162 ? -2.359  -39.690 -33.155  1.000 204.484 ? 162 SER LLL CA  1 
ATOM 2871 C C   . SER B 2 162 ? -2.169  -38.929 -34.471  1.000 210.445 ? 162 SER LLL C   1 
ATOM 2872 O O   . SER B 2 162 ? -3.104  -38.191 -34.891  1.000 204.346 ? 162 SER LLL O   1 
ATOM 2873 C CB  . SER B 2 162 ? -3.142  -40.956 -33.409  1.000 204.461 ? 162 SER LLL CB  1 
ATOM 2874 O OG  . SER B 2 162 ? -3.644  -41.516 -32.204  1.000 211.084 ? 162 SER LLL OG  1 
ATOM 2875 N N   . GLY B 2 163 ? -0.987  -39.112 -35.074  1.000 217.332 ? 163 GLY LLL N   1 
ATOM 2876 C CA  . GLY B 2 163 ? -0.718  -38.949 -36.515  1.000 224.516 ? 163 GLY LLL CA  1 
ATOM 2877 C C   . GLY B 2 163 ? -0.699  -37.503 -36.973  1.000 232.471 ? 163 GLY LLL C   1 
ATOM 2878 O O   . GLY B 2 163 ? -0.695  -37.291 -38.200  1.000 271.700 ? 163 GLY LLL O   1 
ATOM 2879 N N   . ASN B 2 164 ? -0.674  -36.541 -36.047  1.000 221.181 ? 164 ASN LLL N   1 
ATOM 2880 C CA  . ASN B 2 164 ? -0.425  -35.106 -36.349  1.000 215.912 ? 164 ASN LLL CA  1 
ATOM 2881 C C   . ASN B 2 164 ? 0.888   -34.709 -35.677  1.000 203.213 ? 164 ASN LLL C   1 
ATOM 2882 O O   . ASN B 2 164 ? 1.143   -33.517 -35.520  1.000 196.929 ? 164 ASN LLL O   1 
ATOM 2883 C CB  . ASN B 2 164 ? -1.597  -34.223 -35.928  1.000 225.544 ? 164 ASN LLL CB  1 
ATOM 2884 C CG  . ASN B 2 164 ? -1.918  -34.325 -34.452  1.000 235.642 ? 164 ASN LLL CG  1 
ATOM 2885 O OD1 . ASN B 2 164 ? -1.426  -35.216 -33.767  1.000 245.775 ? 164 ASN LLL OD1 1 
ATOM 2886 N ND2 . ASN B 2 164 ? -2.741  -33.418 -33.952  1.000 241.596 ? 164 ASN LLL ND2 1 
ATOM 2887 N N   . SER B 2 165 ? 1.668   -35.721 -35.295  1.000 194.044 ? 165 SER LLL N   1 
ATOM 2888 C CA  . SER B 2 165 ? 3.089   -35.635 -34.884  1.000 190.424 ? 165 SER LLL CA  1 
ATOM 2889 C C   . SER B 2 165 ? 3.975   -36.256 -35.972  1.000 187.383 ? 165 SER LLL C   1 
ATOM 2890 O O   . SER B 2 165 ? 3.509   -37.179 -36.666  1.000 201.965 ? 165 SER LLL O   1 
ATOM 2891 C CB  . SER B 2 165 ? 3.274   -36.322 -33.566  1.000 192.951 ? 165 SER LLL CB  1 
ATOM 2892 O OG  . SER B 2 165 ? 2.980   -37.714 -33.675  1.000 192.695 ? 165 SER LLL OG  1 
ATOM 2893 N N   . GLN B 2 166 ? 5.204   -35.763 -36.117  1.000 177.459 ? 166 GLN LLL N   1 
ATOM 2894 C CA  . GLN B 2 166 ? 6.241   -36.323 -37.020  1.000 170.188 ? 166 GLN LLL CA  1 
ATOM 2895 C C   . GLN B 2 166 ? 7.556   -36.423 -36.255  1.000 160.226 ? 166 GLN LLL C   1 
ATOM 2896 O O   . GLN B 2 166 ? 7.841   -35.477 -35.486  1.000 154.386 ? 166 GLN LLL O   1 
ATOM 2897 C CB  . GLN B 2 166 ? 6.505   -35.394 -38.203  1.000 182.428 ? 166 GLN LLL CB  1 
ATOM 2898 C CG  . GLN B 2 166 ? 5.435   -35.375 -39.288  1.000 184.413 ? 166 GLN LLL CG  1 
ATOM 2899 C CD  . GLN B 2 166 ? 6.048   -34.905 -40.591  1.000 182.628 ? 166 GLN LLL CD  1 
ATOM 2900 O OE1 . GLN B 2 166 ? 6.218   -33.714 -40.854  1.000 181.222 ? 166 GLN LLL OE1 1 
ATOM 2901 N NE2 . GLN B 2 166 ? 6.450   -35.862 -41.404  1.000 186.308 ? 166 GLN LLL NE2 1 
ATOM 2902 N N   . GLU B 2 167 ? 8.346   -37.466 -36.511  1.000 157.155 ? 167 GLU LLL N   1 
ATOM 2903 C CA  . GLU B 2 167 ? 9.678   -37.622 -35.877  1.000 165.549 ? 167 GLU LLL CA  1 
ATOM 2904 C C   . GLU B 2 167 ? 10.803  -37.503 -36.909  1.000 161.090 ? 167 GLU LLL C   1 
ATOM 2905 O O   . GLU B 2 167 ? 10.577  -37.748 -38.118  1.000 144.852 ? 167 GLU LLL O   1 
ATOM 2906 C CB  . GLU B 2 167 ? 9.776   -38.952 -35.144  1.000 175.208 ? 167 GLU LLL CB  1 
ATOM 2907 C CG  . GLU B 2 167 ? 8.751   -39.075 -34.045  1.000 191.578 ? 167 GLU LLL CG  1 
ATOM 2908 C CD  . GLU B 2 167 ? 8.955   -40.265 -33.124  1.000 206.763 ? 167 GLU LLL CD  1 
ATOM 2909 O OE1 . GLU B 2 167 ? 8.282   -40.322 -32.061  1.000 200.956 ? 167 GLU LLL OE1 1 
ATOM 2910 O OE2 . GLU B 2 167 ? 9.773   -41.152 -33.489  1.000 229.342 ? 167 GLU LLL OE2 1 
ATOM 2911 N N   . SER B 2 168 ? 11.976  -37.133 -36.395  1.000 162.255 ? 168 SER LLL N   1 
ATOM 2912 C CA  . SER B 2 168 ? 13.271  -37.061 -37.106  1.000 171.597 ? 168 SER LLL CA  1 
ATOM 2913 C C   . SER B 2 168 ? 14.380  -37.464 -36.130  1.000 169.044 ? 168 SER LLL C   1 
ATOM 2914 O O   . SER B 2 168 ? 14.330  -37.089 -34.943  1.000 161.115 ? 168 SER LLL O   1 
ATOM 2915 C CB  . SER B 2 168 ? 13.504  -35.681 -37.662  1.000 178.626 ? 168 SER LLL CB  1 
ATOM 2916 O OG  . SER B 2 168 ? 13.976  -34.801 -36.644  1.000 168.526 ? 168 SER LLL OG  1 
ATOM 2917 N N   . VAL B 2 169 ? 15.346  -38.236 -36.600  1.000 162.655 ? 169 VAL LLL N   1 
ATOM 2918 C CA  . VAL B 2 169 ? 16.425  -38.727 -35.710  1.000 162.517 ? 169 VAL LLL CA  1 
ATOM 2919 C C   . VAL B 2 169 ? 17.728  -38.325 -36.362  1.000 149.400 ? 169 VAL LLL C   1 
ATOM 2920 O O   . VAL B 2 169 ? 17.839  -38.633 -37.551  1.000 145.014 ? 169 VAL LLL O   1 
ATOM 2921 C CB  . VAL B 2 169 ? 16.347  -40.253 -35.514  1.000 176.824 ? 169 VAL LLL CB  1 
ATOM 2922 C CG1 . VAL B 2 169 ? 17.172  -40.697 -34.304  1.000 190.157 ? 169 VAL LLL CG1 1 
ATOM 2923 C CG2 . VAL B 2 169 ? 14.907  -40.757 -35.404  1.000 175.057 ? 169 VAL LLL CG2 1 
ATOM 2924 N N   . THR B 2 170 ? 18.652  -37.709 -35.611  1.000 149.540 ? 170 THR LLL N   1 
ATOM 2925 C CA  . THR B 2 170 ? 20.069  -37.530 -36.038  1.000 167.979 ? 170 THR LLL CA  1 
ATOM 2926 C C   . THR B 2 170 ? 20.653  -38.911 -36.400  1.000 179.650 ? 170 THR LLL C   1 
ATOM 2927 O O   . THR B 2 170 ? 20.229  -39.911 -35.814  1.000 192.607 ? 170 THR LLL O   1 
ATOM 2928 C CB  . THR B 2 170 ? 20.936  -36.817 -34.986  1.000 162.094 ? 170 THR LLL CB  1 
ATOM 2929 O OG1 . THR B 2 170 ? 20.838  -37.536 -33.770  1.000 147.568 ? 170 THR LLL OG1 1 
ATOM 2930 C CG2 . THR B 2 170 ? 20.539  -35.389 -34.690  1.000 168.747 ? 170 THR LLL CG2 1 
ATOM 2931 N N   . GLU B 2 171 ? 21.575  -38.987 -37.356  1.000 182.128 ? 171 GLU LLL N   1 
ATOM 2932 C CA  . GLU B 2 171 ? 22.411  -40.199 -37.528  1.000 178.116 ? 171 GLU LLL CA  1 
ATOM 2933 C C   . GLU B 2 171 ? 23.366  -40.229 -36.319  1.000 169.824 ? 171 GLU LLL C   1 
ATOM 2934 O O   . GLU B 2 171 ? 23.692  -39.163 -35.727  1.000 154.626 ? 171 GLU LLL O   1 
ATOM 2935 C CB  . GLU B 2 171 ? 23.117  -40.207 -38.884  1.000 193.864 ? 171 GLU LLL CB  1 
ATOM 2936 C CG  . GLU B 2 171 ? 23.292  -41.604 -39.475  1.000 199.704 ? 171 GLU LLL CG  1 
ATOM 2937 C CD  . GLU B 2 171 ? 22.903  -41.755 -40.940  1.000 188.460 ? 171 GLU LLL CD  1 
ATOM 2938 O OE1 . GLU B 2 171 ? 23.060  -42.865 -41.508  1.000 179.402 ? 171 GLU LLL OE1 1 
ATOM 2939 O OE2 . GLU B 2 171 ? 22.418  -40.780 -41.508  1.000 177.705 ? 171 GLU LLL OE2 1 
ATOM 2940 N N   . GLN B 2 172 ? 23.775  -41.427 -35.935  1.000 165.932 ? 172 GLN LLL N   1 
ATOM 2941 C CA  . GLN B 2 172 ? 24.599  -41.688 -34.734  1.000 162.890 ? 172 GLN LLL CA  1 
ATOM 2942 C C   . GLN B 2 172 ? 25.767  -40.698 -34.660  1.000 164.295 ? 172 GLN LLL C   1 
ATOM 2943 O O   . GLN B 2 172 ? 26.488  -40.573 -35.633  1.000 165.077 ? 172 GLN LLL O   1 
ATOM 2944 C CB  . GLN B 2 172 ? 25.068  -43.130 -34.832  1.000 157.522 ? 172 GLN LLL CB  1 
ATOM 2945 C CG  . GLN B 2 172 ? 25.815  -43.615 -33.614  1.000 158.995 ? 172 GLN LLL CG  1 
ATOM 2946 C CD  . GLN B 2 172 ? 26.021  -45.106 -33.694  1.000 159.903 ? 172 GLN LLL CD  1 
ATOM 2947 O OE1 . GLN B 2 172 ? 26.420  -45.644 -34.711  1.000 152.888 ? 172 GLN LLL OE1 1 
ATOM 2948 N NE2 . GLN B 2 172 ? 25.744  -45.801 -32.610  1.000 180.022 ? 172 GLN LLL NE2 1 
ATOM 2949 N N   . ASP B 2 173 ? 25.933  -40.012 -33.533  1.000 182.310 ? 173 ASP LLL N   1 
ATOM 2950 C CA  . ASP B 2 173 ? 27.134  -39.191 -33.214  1.000 198.214 ? 173 ASP LLL CA  1 
ATOM 2951 C C   . ASP B 2 173 ? 28.407  -40.053 -33.328  1.000 200.013 ? 173 ASP LLL C   1 
ATOM 2952 O O   . ASP B 2 173 ? 28.434  -41.159 -32.787  1.000 194.539 ? 173 ASP LLL O   1 
ATOM 2953 C CB  . ASP B 2 173 ? 26.997  -38.583 -31.816  1.000 205.212 ? 173 ASP LLL CB  1 
ATOM 2954 C CG  . ASP B 2 173 ? 28.104  -37.615 -31.463  1.000 210.448 ? 173 ASP LLL CG  1 
ATOM 2955 O OD1 . ASP B 2 173 ? 27.935  -36.422 -31.750  1.000 236.822 ? 173 ASP LLL OD1 1 
ATOM 2956 O OD2 . ASP B 2 173 ? 29.118  -38.064 -30.913  1.000 190.784 ? 173 ASP LLL OD2 1 
ATOM 2957 N N   . SER B 2 174 ? 29.452  -39.556 -33.989  1.000 215.912 ? 174 SER LLL N   1 
ATOM 2958 C CA  . SER B 2 174 ? 30.683  -40.333 -34.335  1.000 237.295 ? 174 SER LLL CA  1 
ATOM 2959 C C   . SER B 2 174 ? 31.496  -40.719 -33.076  1.000 235.874 ? 174 SER LLL C   1 
ATOM 2960 O O   . SER B 2 174 ? 32.362  -41.633 -33.187  1.000 236.051 ? 174 SER LLL O   1 
ATOM 2961 C CB  . SER B 2 174 ? 31.558  -39.578 -35.356  1.000 248.263 ? 174 SER LLL CB  1 
ATOM 2962 O OG  . SER B 2 174 ? 31.319  -39.997 -36.702  1.000 236.357 ? 174 SER LLL OG  1 
ATOM 2963 N N   . LYS B 2 175 ? 31.243  -40.074 -31.924  1.000 224.044 ? 175 LYS LLL N   1 
ATOM 2964 C CA  . LYS B 2 175 ? 32.214  -39.957 -30.795  1.000 218.331 ? 175 LYS LLL CA  1 
ATOM 2965 C C   . LYS B 2 175 ? 31.657  -40.556 -29.490  1.000 214.103 ? 175 LYS LLL C   1 
ATOM 2966 O O   . LYS B 2 175 ? 32.445  -41.098 -28.672  1.000 203.612 ? 175 LYS LLL O   1 
ATOM 2967 C CB  . LYS B 2 175 ? 32.587  -38.479 -30.627  1.000 213.056 ? 175 LYS LLL CB  1 
ATOM 2968 C CG  . LYS B 2 175 ? 32.937  -37.740 -31.919  1.000 215.030 ? 175 LYS LLL CG  1 
ATOM 2969 C CD  . LYS B 2 175 ? 34.065  -36.711 -31.796  1.000 227.877 ? 175 LYS LLL CD  1 
ATOM 2970 C CE  . LYS B 2 175 ? 33.690  -35.417 -31.095  1.000 237.233 ? 175 LYS LLL CE  1 
ATOM 2971 N NZ  . LYS B 2 175 ? 34.879  -34.717 -30.539  1.000 240.450 ? 175 LYS LLL NZ  1 
ATOM 2972 N N   . ASP B 2 176 ? 30.358  -40.420 -29.254  1.000 206.938 ? 176 ASP LLL N   1 
ATOM 2973 C CA  . ASP B 2 176 ? 29.694  -41.057 -28.092  1.000 206.655 ? 176 ASP LLL CA  1 
ATOM 2974 C C   . ASP B 2 176 ? 28.769  -42.168 -28.596  1.000 192.496 ? 176 ASP LLL C   1 
ATOM 2975 O O   . ASP B 2 176 ? 28.245  -42.899 -27.750  1.000 214.447 ? 176 ASP LLL O   1 
ATOM 2976 C CB  . ASP B 2 176 ? 28.953  -40.025 -27.238  1.000 213.015 ? 176 ASP LLL CB  1 
ATOM 2977 C CG  . ASP B 2 176 ? 27.811  -39.338 -27.964  1.000 212.115 ? 176 ASP LLL CG  1 
ATOM 2978 O OD1 . ASP B 2 176 ? 27.334  -38.312 -27.454  1.000 226.355 ? 176 ASP LLL OD1 1 
ATOM 2979 O OD2 . ASP B 2 176 ? 27.400  -39.841 -29.028  1.000 200.052 ? 176 ASP LLL OD2 1 
ATOM 2980 N N   . SER B 2 177 ? 28.538  -42.270 -29.905  1.000 172.088 ? 177 SER LLL N   1 
ATOM 2981 C CA  . SER B 2 177 ? 27.716  -43.335 -30.543  1.000 165.919 ? 177 SER LLL CA  1 
ATOM 2982 C C   . SER B 2 177 ? 26.258  -43.260 -30.081  1.000 148.194 ? 177 SER LLL C   1 
ATOM 2983 O O   . SER B 2 177 ? 25.656  -44.311 -29.810  1.000 143.399 ? 177 SER LLL O   1 
ATOM 2984 C CB  . SER B 2 177 ? 28.300  -44.704 -30.275  1.000 177.722 ? 177 SER LLL CB  1 
ATOM 2985 O OG  . SER B 2 177 ? 29.650  -44.803 -30.722  1.000 197.288 ? 177 SER LLL OG  1 
ATOM 2986 N N   . THR B 2 178 ? 25.700  -42.061 -30.003  1.000 154.368 ? 178 THR LLL N   1 
ATOM 2987 C CA  . THR B 2 178 ? 24.315  -41.827 -29.516  1.000 172.942 ? 178 THR LLL CA  1 
ATOM 2988 C C   . THR B 2 178 ? 23.477  -41.205 -30.627  1.000 159.910 ? 178 THR LLL C   1 
ATOM 2989 O O   . THR B 2 178 ? 24.048  -40.614 -31.539  1.000 168.196 ? 178 THR LLL O   1 
ATOM 2990 C CB  . THR B 2 178 ? 24.299  -40.943 -28.259  1.000 189.902 ? 178 THR LLL CB  1 
ATOM 2991 O OG1 . THR B 2 178 ? 24.736  -39.627 -28.620  1.000 187.449 ? 178 THR LLL OG1 1 
ATOM 2992 C CG2 . THR B 2 178 ? 25.143  -41.511 -27.132  1.000 197.631 ? 178 THR LLL CG2 1 
ATOM 2993 N N   . TYR B 2 179 ? 22.166  -41.341 -30.520  1.000 155.857 ? 179 TYR LLL N   1 
ATOM 2994 C CA  . TYR B 2 179 ? 21.172  -40.650 -31.368  1.000 156.233 ? 179 TYR LLL CA  1 
ATOM 2995 C C   . TYR B 2 179 ? 20.599  -39.466 -30.582  1.000 157.960 ? 179 TYR LLL C   1 
ATOM 2996 O O   . TYR B 2 179 ? 21.021  -39.214 -29.433  1.000 156.112 ? 179 TYR LLL O   1 
ATOM 2997 C CB  . TYR B 2 179 ? 20.118  -41.659 -31.823  1.000 163.805 ? 179 TYR LLL CB  1 
ATOM 2998 C CG  . TYR B 2 179 ? 20.746  -42.792 -32.593  1.000 165.792 ? 179 TYR LLL CG  1 
ATOM 2999 C CD1 . TYR B 2 179 ? 21.209  -43.939 -31.976  1.000 172.165 ? 179 TYR LLL CD1 1 
ATOM 3000 C CD2 . TYR B 2 179 ? 20.948  -42.677 -33.947  1.000 167.071 ? 179 TYR LLL CD2 1 
ATOM 3001 C CE1 . TYR B 2 179 ? 21.802  -44.957 -32.702  1.000 175.401 ? 179 TYR LLL CE1 1 
ATOM 3002 C CE2 . TYR B 2 179 ? 21.546  -43.677 -34.686  1.000 171.102 ? 179 TYR LLL CE2 1 
ATOM 3003 C CZ  . TYR B 2 179 ? 21.981  -44.825 -34.065  1.000 171.937 ? 179 TYR LLL CZ  1 
ATOM 3004 O OH  . TYR B 2 179 ? 22.579  -45.791 -34.825  1.000 169.904 ? 179 TYR LLL OH  1 
ATOM 3005 N N   . SER B 2 180 ? 19.703  -38.724 -31.234  1.000 151.644 ? 180 SER LLL N   1 
ATOM 3006 C CA  . SER B 2 180 ? 18.830  -37.665 -30.650  1.000 145.866 ? 180 SER LLL CA  1 
ATOM 3007 C C   . SER B 2 180 ? 17.577  -37.621 -31.525  1.000 144.424 ? 180 SER LLL C   1 
ATOM 3008 O O   . SER B 2 180 ? 17.718  -37.763 -32.753  1.000 163.688 ? 180 SER LLL O   1 
ATOM 3009 C CB  . SER B 2 180 ? 19.510  -36.298 -30.535  1.000 138.756 ? 180 SER LLL CB  1 
ATOM 3010 O OG  . SER B 2 180 ? 20.437  -36.255 -29.451  1.000 134.340 ? 180 SER LLL OG  1 
ATOM 3011 N N   . LEU B 2 181 ? 16.401  -37.505 -30.922  1.000 141.002 ? 181 LEU LLL N   1 
ATOM 3012 C CA  . LEU B 2 181 ? 15.099  -37.551 -31.630  1.000 146.168 ? 181 LEU LLL CA  1 
ATOM 3013 C C   . LEU B 2 181 ? 14.323  -36.263 -31.361  1.000 164.535 ? 181 LEU LLL C   1 
ATOM 3014 O O   . LEU B 2 181 ? 14.468  -35.705 -30.260  1.000 178.649 ? 181 LEU LLL O   1 
ATOM 3015 C CB  . LEU B 2 181 ? 14.312  -38.749 -31.109  1.000 140.813 ? 181 LEU LLL CB  1 
ATOM 3016 C CG  . LEU B 2 181 ? 13.060  -39.098 -31.904  1.000 138.600 ? 181 LEU LLL CG  1 
ATOM 3017 C CD1 . LEU B 2 181 ? 12.847  -40.609 -31.875  1.000 144.040 ? 181 LEU LLL CD1 1 
ATOM 3018 C CD2 . LEU B 2 181 ? 11.833  -38.362 -31.390  1.000 128.976 ? 181 LEU LLL CD2 1 
ATOM 3019 N N   . SER B 2 182 ? 13.509  -35.833 -32.324  1.000 177.425 ? 182 SER LLL N   1 
ATOM 3020 C CA  . SER B 2 182 ? 12.549  -34.710 -32.167  1.000 186.175 ? 182 SER LLL CA  1 
ATOM 3021 C C   . SER B 2 182 ? 11.174  -35.136 -32.710  1.000 177.250 ? 182 SER LLL C   1 
ATOM 3022 O O   . SER B 2 182 ? 11.020  -35.398 -33.918  1.000 158.217 ? 182 SER LLL O   1 
ATOM 3023 C CB  . SER B 2 182 ? 13.077  -33.446 -32.800  1.000 198.781 ? 182 SER LLL CB  1 
ATOM 3024 O OG  . SER B 2 182 ? 13.042  -33.541 -34.215  1.000 215.835 ? 182 SER LLL OG  1 
ATOM 3025 N N   . SER B 2 183 ? 10.210  -35.248 -31.808  1.000 175.899 ? 183 SER LLL N   1 
ATOM 3026 C CA  . SER B 2 183 ? 8.785   -35.497 -32.120  1.000 173.971 ? 183 SER LLL CA  1 
ATOM 3027 C C   . SER B 2 183 ? 8.056   -34.163 -32.163  1.000 176.194 ? 183 SER LLL C   1 
ATOM 3028 O O   . SER B 2 183 ? 7.951   -33.543 -31.109  1.000 184.520 ? 183 SER LLL O   1 
ATOM 3029 C CB  . SER B 2 183 ? 8.173   -36.376 -31.098  1.000 172.621 ? 183 SER LLL CB  1 
ATOM 3030 O OG  . SER B 2 183 ? 6.793   -36.509 -31.363  1.000 172.160 ? 183 SER LLL OG  1 
ATOM 3031 N N   . THR B 2 184 ? 7.588   -33.737 -33.332  1.000 177.523 ? 184 THR LLL N   1 
ATOM 3032 C CA  . THR B 2 184 ? 6.994   -32.393 -33.525  1.000 174.222 ? 184 THR LLL CA  1 
ATOM 3033 C C   . THR B 2 184 ? 5.492   -32.522 -33.749  1.000 167.163 ? 184 THR LLL C   1 
ATOM 3034 O O   . THR B 2 184 ? 5.111   -33.067 -34.772  1.000 153.661 ? 184 THR LLL O   1 
ATOM 3035 C CB  . THR B 2 184 ? 7.624   -31.679 -34.718  1.000 182.900 ? 184 THR LLL CB  1 
ATOM 3036 O OG1 . THR B 2 184 ? 9.044   -31.778 -34.631  1.000 190.445 ? 184 THR LLL OG1 1 
ATOM 3037 C CG2 . THR B 2 184 ? 7.193   -30.234 -34.784  1.000 186.662 ? 184 THR LLL CG2 1 
ATOM 3038 N N   . LEU B 2 185 ? 4.679   -32.018 -32.824  1.000 179.642 ? 185 LEU LLL N   1 
ATOM 3039 C CA  . LEU B 2 185 ? 3.194   -31.973 -32.963  1.000 196.220 ? 185 LEU LLL CA  1 
ATOM 3040 C C   . LEU B 2 185 ? 2.782   -30.603 -33.499  1.000 203.963 ? 185 LEU LLL C   1 
ATOM 3041 O O   . LEU B 2 185 ? 3.023   -29.598 -32.809  1.000 211.013 ? 185 LEU LLL O   1 
ATOM 3042 C CB  . LEU B 2 185 ? 2.500   -32.234 -31.618  1.000 193.850 ? 185 LEU LLL CB  1 
ATOM 3043 C CG  . LEU B 2 185 ? 0.968   -32.232 -31.670  1.000 191.577 ? 185 LEU LLL CG  1 
ATOM 3044 C CD1 . LEU B 2 185 ? 0.398   -33.409 -30.912  1.000 191.656 ? 185 LEU LLL CD1 1 
ATOM 3045 C CD2 . LEU B 2 185 ? 0.373   -30.935 -31.139  1.000 194.812 ? 185 LEU LLL CD2 1 
ATOM 3046 N N   . THR B 2 186 ? 2.129   -30.575 -34.659  1.000 206.942 ? 186 THR LLL N   1 
ATOM 3047 C CA  . THR B 2 186 ? 1.602   -29.327 -35.267  1.000 211.052 ? 186 THR LLL CA  1 
ATOM 3048 C C   . THR B 2 186 ? 0.070   -29.360 -35.217  1.000 205.236 ? 186 THR LLL C   1 
ATOM 3049 O O   . THR B 2 186 ? -0.518  -30.414 -35.530  1.000 201.187 ? 186 THR LLL O   1 
ATOM 3050 C CB  . THR B 2 186 ? 2.198   -29.093 -36.665  1.000 219.376 ? 186 THR LLL CB  1 
ATOM 3051 O OG1 . THR B 2 186 ? 1.483   -27.987 -37.218  1.000 225.327 ? 186 THR LLL OG1 1 
ATOM 3052 C CG2 . THR B 2 186 ? 2.140   -30.287 -37.599  1.000 216.705 ? 186 THR LLL CG2 1 
ATOM 3053 N N   . LEU B 2 187 ? -0.535  -28.255 -34.779  1.000 202.303 ? 187 LEU LLL N   1 
ATOM 3054 C CA  . LEU B 2 187 ? -1.976  -27.944 -34.980  1.000 202.016 ? 187 LEU LLL CA  1 
ATOM 3055 C C   . LEU B 2 187 ? -2.140  -26.430 -35.158  1.000 197.708 ? 187 LEU LLL C   1 
ATOM 3056 O O   . LEU B 2 187 ? -1.173  -25.664 -34.900  1.000 187.813 ? 187 LEU LLL O   1 
ATOM 3057 C CB  . LEU B 2 187 ? -2.809  -28.470 -33.808  1.000 208.684 ? 187 LEU LLL CB  1 
ATOM 3058 C CG  . LEU B 2 187 ? -2.224  -28.239 -32.416  1.000 205.626 ? 187 LEU LLL CG  1 
ATOM 3059 C CD1 . LEU B 2 187 ? -2.290  -26.768 -32.033  1.000 211.172 ? 187 LEU LLL CD1 1 
ATOM 3060 C CD2 . LEU B 2 187 ? -2.936  -29.107 -31.389  1.000 194.318 ? 187 LEU LLL CD2 1 
ATOM 3061 N N   . SER B 2 188 ? -3.314  -26.014 -35.627  1.000 200.936 ? 188 SER LLL N   1 
ATOM 3062 C CA  . SER B 2 188 ? -3.612  -24.600 -35.958  1.000 206.233 ? 188 SER LLL CA  1 
ATOM 3063 C C   . SER B 2 188 ? -3.590  -23.804 -34.657  1.000 210.656 ? 188 SER LLL C   1 
ATOM 3064 O O   . SER B 2 188 ? -3.652  -24.430 -33.579  1.000 214.443 ? 188 SER LLL O   1 
ATOM 3065 C CB  . SER B 2 188 ? -4.929  -24.440 -36.699  1.000 208.494 ? 188 SER LLL CB  1 
ATOM 3066 O OG  . SER B 2 188 ? -5.960  -25.232 -36.135  1.000 202.194 ? 188 SER LLL OG  1 
ATOM 3067 N N   . LYS B 2 189 ? -3.503  -22.479 -34.766  1.000 210.365 ? 189 LYS LLL N   1 
ATOM 3068 C CA  . LYS B 2 189 ? -3.632  -21.547 -33.620  1.000 205.697 ? 189 LYS LLL CA  1 
ATOM 3069 C C   . LYS B 2 189 ? -5.021  -21.718 -32.987  1.000 201.591 ? 189 LYS LLL C   1 
ATOM 3070 O O   . LYS B 2 189 ? -5.086  -21.791 -31.744  1.000 181.620 ? 189 LYS LLL O   1 
ATOM 3071 C CB  . LYS B 2 189 ? -3.381  -20.119 -34.110  1.000 206.540 ? 189 LYS LLL CB  1 
ATOM 3072 C CG  . LYS B 2 189 ? -3.388  -19.054 -33.030  1.000 207.576 ? 189 LYS LLL CG  1 
ATOM 3073 C CD  . LYS B 2 189 ? -3.598  -17.645 -33.561  1.000 208.166 ? 189 LYS LLL CD  1 
ATOM 3074 C CE  . LYS B 2 189 ? -3.664  -16.606 -32.463  1.000 205.311 ? 189 LYS LLL CE  1 
ATOM 3075 N NZ  . LYS B 2 189 ? -4.168  -15.305 -32.960  1.000 209.460 ? 189 LYS LLL NZ  1 
ATOM 3076 N N   . ALA B 2 190 ? -6.074  -21.774 -33.819  1.000 205.946 ? 190 ALA LLL N   1 
ATOM 3077 C CA  . ALA B 2 190 ? -7.493  -21.930 -33.411  1.000 205.515 ? 190 ALA LLL CA  1 
ATOM 3078 C C   . ALA B 2 190 ? -7.603  -23.146 -32.491  1.000 204.806 ? 190 ALA LLL C   1 
ATOM 3079 O O   . ALA B 2 190 ? -8.051  -22.972 -31.369  1.000 213.609 ? 190 ALA LLL O   1 
ATOM 3080 C CB  . ALA B 2 190 ? -8.404  -22.045 -34.612  1.000 199.547 ? 190 ALA LLL CB  1 
ATOM 3081 N N   . ASP B 2 191 ? -7.154  -24.315 -32.939  1.000 205.935 ? 191 ASP LLL N   1 
ATOM 3082 C CA  . ASP B 2 191 ? -7.199  -25.563 -32.137  1.000 206.661 ? 191 ASP LLL CA  1 
ATOM 3083 C C   . ASP B 2 191 ? -6.231  -25.448 -30.965  1.000 191.676 ? 191 ASP LLL C   1 
ATOM 3084 O O   . ASP B 2 191 ? -6.458  -26.148 -29.968  1.000 183.445 ? 191 ASP LLL O   1 
ATOM 3085 C CB  . ASP B 2 191 ? -6.826  -26.795 -32.963  1.000 225.506 ? 191 ASP LLL CB  1 
ATOM 3086 C CG  . ASP B 2 191 ? -7.652  -26.961 -34.223  1.000 242.396 ? 191 ASP LLL CG  1 
ATOM 3087 O OD1 . ASP B 2 191 ? -8.859  -26.618 -34.187  1.000 258.679 ? 191 ASP LLL OD1 1 
ATOM 3088 O OD2 . ASP B 2 191 ? -7.071  -27.409 -35.232  1.000 250.364 ? 191 ASP LLL OD2 1 
ATOM 3089 N N   . TYR B 2 192 ? -5.184  -24.627 -31.091  1.000 177.758 ? 192 TYR LLL N   1 
ATOM 3090 C CA  . TYR B 2 192 ? -4.113  -24.550 -30.067  1.000 177.481 ? 192 TYR LLL CA  1 
ATOM 3091 C C   . TYR B 2 192 ? -4.725  -23.986 -28.797  1.000 180.609 ? 192 TYR LLL C   1 
ATOM 3092 O O   . TYR B 2 192 ? -4.443  -24.495 -27.726  1.000 174.588 ? 192 TYR LLL O   1 
ATOM 3093 C CB  . TYR B 2 192 ? -2.916  -23.689 -30.483  1.000 183.331 ? 192 TYR LLL CB  1 
ATOM 3094 C CG  . TYR B 2 192 ? -1.877  -23.507 -29.394  1.000 181.876 ? 192 TYR LLL CG  1 
ATOM 3095 C CD1 . TYR B 2 192 ? -1.243  -24.593 -28.809  1.000 173.075 ? 192 TYR LLL CD1 1 
ATOM 3096 C CD2 . TYR B 2 192 ? -1.529  -22.245 -28.935  1.000 182.090 ? 192 TYR LLL CD2 1 
ATOM 3097 C CE1 . TYR B 2 192 ? -0.320  -24.431 -27.789  1.000 166.605 ? 192 TYR LLL CE1 1 
ATOM 3098 C CE2 . TYR B 2 192 ? -0.601  -22.061 -27.924  1.000 172.904 ? 192 TYR LLL CE2 1 
ATOM 3099 C CZ  . TYR B 2 192 ? 0.009   -23.158 -27.355  1.000 167.435 ? 192 TYR LLL CZ  1 
ATOM 3100 O OH  . TYR B 2 192 ? 0.930   -22.924 -26.380  1.000 166.039 ? 192 TYR LLL OH  1 
ATOM 3101 N N   . GLU B 2 193 ? -5.551  -22.961 -28.949  1.000 189.329 ? 193 GLU LLL N   1 
ATOM 3102 C CA  . GLU B 2 193 ? -6.141  -22.211 -27.820  1.000 196.039 ? 193 GLU LLL CA  1 
ATOM 3103 C C   . GLU B 2 193 ? -7.440  -22.882 -27.331  1.000 203.234 ? 193 GLU LLL C   1 
ATOM 3104 O O   . GLU B 2 193 ? -8.052  -22.343 -26.391  1.000 204.195 ? 193 GLU LLL O   1 
ATOM 3105 C CB  . GLU B 2 193 ? -6.346  -20.769 -28.275  1.000 201.780 ? 193 GLU LLL CB  1 
ATOM 3106 C CG  . GLU B 2 193 ? -5.120  -20.170 -28.939  1.000 200.340 ? 193 GLU LLL CG  1 
ATOM 3107 C CD  . GLU B 2 193 ? -5.357  -18.815 -29.574  1.000 210.437 ? 193 GLU LLL CD  1 
ATOM 3108 O OE1 . GLU B 2 193 ? -4.474  -17.953 -29.429  1.000 220.586 ? 193 GLU LLL OE1 1 
ATOM 3109 O OE2 . GLU B 2 193 ? -6.428  -18.625 -30.197  1.000 216.199 ? 193 GLU LLL OE2 1 
ATOM 3110 N N   . LYS B 2 194 ? -7.842  -24.028 -27.897  1.000 209.339 ? 194 LYS LLL N   1 
ATOM 3111 C CA  . LYS B 2 194 ? -9.023  -24.817 -27.431  1.000 209.298 ? 194 LYS LLL CA  1 
ATOM 3112 C C   . LYS B 2 194 ? -8.632  -25.706 -26.242  1.000 202.012 ? 194 LYS LLL C   1 
ATOM 3113 O O   . LYS B 2 194 ? -9.566  -26.116 -25.537  1.000 197.246 ? 194 LYS LLL O   1 
ATOM 3114 C CB  . LYS B 2 194 ? -9.608  -25.715 -28.529  1.000 214.641 ? 194 LYS LLL CB  1 
ATOM 3115 C CG  . LYS B 2 194 ? -10.328 -24.989 -29.662  1.000 215.851 ? 194 LYS LLL CG  1 
ATOM 3116 C CD  . LYS B 2 194 ? -11.501 -25.767 -30.249  1.000 215.234 ? 194 LYS LLL CD  1 
ATOM 3117 C CE  . LYS B 2 194 ? -11.754 -25.468 -31.714  1.000 214.201 ? 194 LYS LLL CE  1 
ATOM 3118 N NZ  . LYS B 2 194 ? -10.954 -26.342 -32.607  1.000 210.013 ? 194 LYS LLL NZ  1 
ATOM 3119 N N   . HIS B 2 195 ? -7.332  -26.013 -26.071  1.000 195.966 ? 195 HIS LLL N   1 
ATOM 3120 C CA  . HIS B 2 195 ? -6.761  -26.895 -25.012  1.000 185.441 ? 195 HIS LLL CA  1 
ATOM 3121 C C   . HIS B 2 195 ? -5.770  -26.086 -24.170  1.000 180.060 ? 195 HIS LLL C   1 
ATOM 3122 O O   . HIS B 2 195 ? -5.371  -25.025 -24.661  1.000 173.688 ? 195 HIS LLL O   1 
ATOM 3123 C CB  . HIS B 2 195 ? -6.130  -28.136 -25.662  1.000 178.116 ? 195 HIS LLL CB  1 
ATOM 3124 C CG  . HIS B 2 195 ? -7.061  -28.815 -26.605  1.000 179.788 ? 195 HIS LLL CG  1 
ATOM 3125 N ND1 . HIS B 2 195 ? -8.446  -28.806 -26.418  1.000 181.758 ? 195 HIS LLL ND1 1 
ATOM 3126 C CD2 . HIS B 2 195 ? -6.831  -29.525 -27.728  1.000 183.443 ? 195 HIS LLL CD2 1 
ATOM 3127 C CE1 . HIS B 2 195 ? -9.022  -29.467 -27.398  1.000 186.764 ? 195 HIS LLL CE1 1 
ATOM 3128 N NE2 . HIS B 2 195 ? -8.049  -29.917 -28.225  1.000 188.511 ? 195 HIS LLL NE2 1 
ATOM 3129 N N   . LYS B 2 196 ? -5.423  -26.511 -22.944  1.000 181.611 ? 196 LYS LLL N   1 
ATOM 3130 C CA  . LYS B 2 196 ? -4.436  -25.738 -22.133  1.000 188.634 ? 196 LYS LLL CA  1 
ATOM 3131 C C   . LYS B 2 196 ? -3.187  -26.545 -21.777  1.000 187.745 ? 196 LYS LLL C   1 
ATOM 3132 O O   . LYS B 2 196 ? -2.116  -25.939 -21.732  1.000 179.551 ? 196 LYS LLL O   1 
ATOM 3133 C CB  . LYS B 2 196 ? -5.014  -25.176 -20.833  1.000 191.284 ? 196 LYS LLL CB  1 
ATOM 3134 C CG  . LYS B 2 196 ? -4.374  -23.849 -20.399  1.000 195.616 ? 196 LYS LLL CG  1 
ATOM 3135 C CD  . LYS B 2 196 ? -4.137  -23.631 -18.901  1.000 195.090 ? 196 LYS LLL CD  1 
ATOM 3136 C CE  . LYS B 2 196 ? -4.260  -22.175 -18.462  1.000 193.500 ? 196 LYS LLL CE  1 
ATOM 3137 N NZ  . LYS B 2 196 ? -4.683  -22.027 -17.045  1.000 196.496 ? 196 LYS LLL NZ  1 
ATOM 3138 N N   . VAL B 2 197 ? -3.310  -27.828 -21.455  1.000 194.156 ? 197 VAL LLL N   1 
ATOM 3139 C CA  . VAL B 2 197 ? -2.128  -28.632 -21.029  1.000 197.229 ? 197 VAL LLL CA  1 
ATOM 3140 C C   . VAL B 2 197 ? -1.631  -29.480 -22.214  1.000 187.929 ? 197 VAL LLL C   1 
ATOM 3141 O O   . VAL B 2 197 ? -2.419  -30.226 -22.833  1.000 192.117 ? 197 VAL LLL O   1 
ATOM 3142 C CB  . VAL B 2 197 ? -2.434  -29.426 -19.746  1.000 198.117 ? 197 VAL LLL CB  1 
ATOM 3143 C CG1 . VAL B 2 197 ? -3.294  -28.598 -18.807  1.000 205.153 ? 197 VAL LLL CG1 1 
ATOM 3144 C CG2 . VAL B 2 197 ? -3.105  -30.764 -20.010  1.000 199.601 ? 197 VAL LLL CG2 1 
ATOM 3145 N N   . TYR B 2 198 ? -0.355  -29.305 -22.531  1.000 181.843 ? 198 TYR LLL N   1 
ATOM 3146 C CA  . TYR B 2 198 ? 0.394   -29.990 -23.612  1.000 183.609 ? 198 TYR LLL CA  1 
ATOM 3147 C C   . TYR B 2 198 ? 1.526   -30.811 -22.971  1.000 186.180 ? 198 TYR LLL C   1 
ATOM 3148 O O   . TYR B 2 198 ? 2.378   -30.275 -22.220  1.000 182.986 ? 198 TYR LLL O   1 
ATOM 3149 C CB  . TYR B 2 198 ? 0.906   -28.932 -24.596  1.000 174.889 ? 198 TYR LLL CB  1 
ATOM 3150 C CG  . TYR B 2 198 ? -0.193  -28.234 -25.346  1.000 165.371 ? 198 TYR LLL CG  1 
ATOM 3151 C CD1 . TYR B 2 198 ? -0.935  -27.224 -24.765  1.000 173.786 ? 198 TYR LLL CD1 1 
ATOM 3152 C CD2 . TYR B 2 198 ? -0.537  -28.642 -26.616  1.000 163.454 ? 198 TYR LLL CD2 1 
ATOM 3153 C CE1 . TYR B 2 198 ? -1.970  -26.613 -25.454  1.000 179.956 ? 198 TYR LLL CE1 1 
ATOM 3154 C CE2 . TYR B 2 198 ? -1.556  -28.042 -27.326  1.000 164.355 ? 198 TYR LLL CE2 1 
ATOM 3155 C CZ  . TYR B 2 198 ? -2.280  -27.020 -26.742  1.000 172.045 ? 198 TYR LLL CZ  1 
ATOM 3156 O OH  . TYR B 2 198 ? -3.306  -26.454 -27.440  1.000 170.221 ? 198 TYR LLL OH  1 
ATOM 3157 N N   . ALA B 2 199 ? 1.527   -32.114 -23.218  1.000 183.170 ? 199 ALA LLL N   1 
ATOM 3158 C CA  . ALA B 2 199 ? 2.425   -33.046 -22.510  1.000 177.844 ? 199 ALA LLL CA  1 
ATOM 3159 C C   . ALA B 2 199 ? 3.017   -34.028 -23.502  1.000 168.904 ? 199 ALA LLL C   1 
ATOM 3160 O O   . ALA B 2 199 ? 2.333   -34.412 -24.456  1.000 161.143 ? 199 ALA LLL O   1 
ATOM 3161 C CB  . ALA B 2 199 ? 1.672   -33.773 -21.431  1.000 189.300 ? 199 ALA LLL CB  1 
ATOM 3162 N N   . CYS B 2 200 ? 4.248   -34.420 -23.239  1.000 167.216 ? 200 CYS LLL N   1 
ATOM 3163 C CA  . CYS B 2 200 ? 5.053   -35.301 -24.102  1.000 175.287 ? 200 CYS LLL CA  1 
ATOM 3164 C C   . CYS B 2 200 ? 5.577   -36.429 -23.230  1.000 177.914 ? 200 CYS LLL C   1 
ATOM 3165 O O   . CYS B 2 200 ? 6.315   -36.118 -22.275  1.000 175.803 ? 200 CYS LLL O   1 
ATOM 3166 C CB  . CYS B 2 200 ? 6.201   -34.505 -24.696  1.000 183.026 ? 200 CYS LLL CB  1 
ATOM 3167 S SG  . CYS B 2 200 ? 7.532   -35.544 -25.342  1.000 199.670 ? 200 CYS LLL SG  1 
ATOM 3168 N N   . GLU B 2 201 ? 5.182   -37.668 -23.529  1.000 183.892 ? 201 GLU LLL N   1 
ATOM 3169 C CA  . GLU B 2 201 ? 5.478   -38.854 -22.677  1.000 189.968 ? 201 GLU LLL CA  1 
ATOM 3170 C C   . GLU B 2 201 ? 6.415   -39.778 -23.451  1.000 177.166 ? 201 GLU LLL C   1 
ATOM 3171 O O   . GLU B 2 201 ? 6.064   -40.163 -24.577  1.000 173.917 ? 201 GLU LLL O   1 
ATOM 3172 C CB  . GLU B 2 201 ? 4.199   -39.576 -22.248  1.000 197.273 ? 201 GLU LLL CB  1 
ATOM 3173 C CG  . GLU B 2 201 ? 4.440   -40.849 -21.461  1.000 206.711 ? 201 GLU LLL CG  1 
ATOM 3174 C CD  . GLU B 2 201 ? 3.183   -41.356 -20.758  1.000 229.417 ? 201 GLU LLL CD  1 
ATOM 3175 O OE1 . GLU B 2 201 ? 2.860   -40.841 -19.660  1.000 246.211 ? 201 GLU LLL OE1 1 
ATOM 3176 O OE2 . GLU B 2 201 ? 2.481   -42.223 -21.335  1.000 236.651 ? 201 GLU LLL OE2 1 
ATOM 3177 N N   . VAL B 2 202 ? 7.552   -40.096 -22.836  1.000 163.699 ? 202 VAL LLL N   1 
ATOM 3178 C CA  . VAL B 2 202 ? 8.669   -40.848 -23.457  1.000 154.615 ? 202 VAL LLL CA  1 
ATOM 3179 C C   . VAL B 2 202 ? 8.859   -42.175 -22.735  1.000 150.189 ? 202 VAL LLL C   1 
ATOM 3180 O O   . VAL B 2 202 ? 9.225   -42.169 -21.576  1.000 149.640 ? 202 VAL LLL O   1 
ATOM 3181 C CB  . VAL B 2 202 ? 9.979   -40.055 -23.410  1.000 156.513 ? 202 VAL LLL CB  1 
ATOM 3182 C CG1 . VAL B 2 202 ? 11.140  -40.909 -23.899  1.000 159.245 ? 202 VAL LLL CG1 1 
ATOM 3183 C CG2 . VAL B 2 202 ? 9.878   -38.750 -24.181  1.000 159.234 ? 202 VAL LLL CG2 1 
ATOM 3184 N N   . THR B 2 203 ? 8.691   -43.273 -23.453  1.000 150.907 ? 203 THR LLL N   1 
ATOM 3185 C CA  . THR B 2 203 ? 9.128   -44.621 -23.033  1.000 155.611 ? 203 THR LLL CA  1 
ATOM 3186 C C   . THR B 2 203 ? 10.371  -45.000 -23.826  1.000 162.724 ? 203 THR LLL C   1 
ATOM 3187 O O   . THR B 2 203 ? 10.328  -44.959 -25.058  1.000 170.882 ? 203 THR LLL O   1 
ATOM 3188 C CB  . THR B 2 203 ? 8.034   -45.655 -23.266  1.000 158.401 ? 203 THR LLL CB  1 
ATOM 3189 O OG1 . THR B 2 203 ? 6.998   -45.299 -22.357  1.000 177.299 ? 203 THR LLL OG1 1 
ATOM 3190 C CG2 . THR B 2 203 ? 8.502   -47.079 -23.051  1.000 161.390 ? 203 THR LLL CG2 1 
ATOM 3191 N N   . HIS B 2 204 ? 11.451  -45.312 -23.129  1.000 168.430 ? 204 HIS LLL N   1 
ATOM 3192 C CA  . HIS B 2 204 ? 12.713  -45.785 -23.736  1.000 159.770 ? 204 HIS LLL CA  1 
ATOM 3193 C C   . HIS B 2 204 ? 13.307  -46.854 -22.836  1.000 158.525 ? 204 HIS LLL C   1 
ATOM 3194 O O   . HIS B 2 204 ? 13.109  -46.798 -21.627  1.000 171.287 ? 204 HIS LLL O   1 
ATOM 3195 C CB  . HIS B 2 204 ? 13.653  -44.612 -23.957  1.000 155.076 ? 204 HIS LLL CB  1 
ATOM 3196 C CG  . HIS B 2 204 ? 14.952  -45.044 -24.519  1.000 162.625 ? 204 HIS LLL CG  1 
ATOM 3197 N ND1 . HIS B 2 204 ? 16.114  -44.959 -23.797  1.000 173.896 ? 204 HIS LLL ND1 1 
ATOM 3198 C CD2 . HIS B 2 204 ? 15.271  -45.576 -25.714  1.000 158.371 ? 204 HIS LLL CD2 1 
ATOM 3199 C CE1 . HIS B 2 204 ? 17.110  -45.410 -24.527  1.000 168.755 ? 204 HIS LLL CE1 1 
ATOM 3200 N NE2 . HIS B 2 204 ? 16.616  -45.790 -25.709  1.000 161.092 ? 204 HIS LLL NE2 1 
ATOM 3201 N N   . GLN B 2 205 ? 14.042  -47.775 -23.420  1.000 160.516 ? 205 GLN LLL N   1 
ATOM 3202 C CA  . GLN B 2 205 ? 14.711  -48.877 -22.691  1.000 172.898 ? 205 GLN LLL CA  1 
ATOM 3203 C C   . GLN B 2 205 ? 15.596  -48.358 -21.534  1.000 180.802 ? 205 GLN LLL C   1 
ATOM 3204 O O   . GLN B 2 205 ? 15.858  -49.135 -20.588  1.000 188.690 ? 205 GLN LLL O   1 
ATOM 3205 C CB  . GLN B 2 205 ? 15.497  -49.651 -23.739  1.000 172.862 ? 205 GLN LLL CB  1 
ATOM 3206 C CG  . GLN B 2 205 ? 15.963  -51.019 -23.297  1.000 173.295 ? 205 GLN LLL CG  1 
ATOM 3207 C CD  . GLN B 2 205 ? 16.818  -51.548 -24.414  1.000 173.652 ? 205 GLN LLL CD  1 
ATOM 3208 O OE1 . GLN B 2 205 ? 17.778  -52.271 -24.203  1.000 182.095 ? 205 GLN LLL OE1 1 
ATOM 3209 N NE2 . GLN B 2 205 ? 16.516  -51.119 -25.623  1.000 174.019 ? 205 GLN LLL NE2 1 
ATOM 3210 N N   . GLY B 2 206 ? 16.051  -47.100 -21.580  1.000 179.093 ? 206 GLY LLL N   1 
ATOM 3211 C CA  . GLY B 2 206 ? 16.969  -46.520 -20.577  1.000 172.361 ? 206 GLY LLL CA  1 
ATOM 3212 C C   . GLY B 2 206 ? 16.235  -45.897 -19.409  1.000 173.628 ? 206 GLY LLL C   1 
ATOM 3213 O O   . GLY B 2 206 ? 16.921  -45.369 -18.526  1.000 168.694 ? 206 GLY LLL O   1 
ATOM 3214 N N   . LEU B 2 207 ? 14.896  -45.943 -19.414  1.000 178.828 ? 207 LEU LLL N   1 
ATOM 3215 C CA  . LEU B 2 207 ? 14.016  -45.269 -18.423  1.000 181.599 ? 207 LEU LLL CA  1 
ATOM 3216 C C   . LEU B 2 207 ? 13.098  -46.306 -17.792  1.000 186.075 ? 207 LEU LLL C   1 
ATOM 3217 O O   . LEU B 2 207 ? 12.214  -46.797 -18.529  1.000 175.663 ? 207 LEU LLL O   1 
ATOM 3218 C CB  . LEU B 2 207 ? 13.176  -44.205 -19.127  1.000 179.352 ? 207 LEU LLL CB  1 
ATOM 3219 C CG  . LEU B 2 207 ? 13.969  -43.113 -19.843  1.000 185.771 ? 207 LEU LLL CG  1 
ATOM 3220 C CD1 . LEU B 2 207 ? 13.121  -42.496 -20.928  1.000 186.994 ? 207 LEU LLL CD1 1 
ATOM 3221 C CD2 . LEU B 2 207 ? 14.451  -42.028 -18.886  1.000 190.403 ? 207 LEU LLL CD2 1 
ATOM 3222 N N   . SER B 2 208 ? 13.305  -46.576 -16.491  1.000 194.210 ? 208 SER LLL N   1 
ATOM 3223 C CA  . SER B 2 208 ? 12.546  -47.529 -15.636  1.000 199.172 ? 208 SER LLL CA  1 
ATOM 3224 C C   . SER B 2 208 ? 11.039  -47.268 -15.750  1.000 191.662 ? 208 SER LLL C   1 
ATOM 3225 O O   . SER B 2 208 ? 10.268  -48.241 -15.684  1.000 184.101 ? 208 SER LLL O   1 
ATOM 3226 C CB  . SER B 2 208 ? 13.020  -47.436 -14.210  1.000 211.931 ? 208 SER LLL CB  1 
ATOM 3227 O OG  . SER B 2 208 ? 13.353  -46.091 -13.887  1.000 222.148 ? 208 SER LLL OG  1 
ATOM 3228 N N   . SER B 2 209 ? 10.646  -46.004 -15.936  1.000 188.191 ? 209 SER LLL N   1 
ATOM 3229 C CA  . SER B 2 209 ? 9.235   -45.569 -16.094  1.000 191.612 ? 209 SER LLL CA  1 
ATOM 3230 C C   . SER B 2 209 ? 9.141   -44.377 -17.041  1.000 176.038 ? 209 SER LLL C   1 
ATOM 3231 O O   . SER B 2 209 ? 10.032  -43.538 -17.036  1.000 168.893 ? 209 SER LLL O   1 
ATOM 3232 C CB  . SER B 2 209 ? 8.664   -45.210 -14.764  1.000 208.597 ? 209 SER LLL CB  1 
ATOM 3233 O OG  . SER B 2 209 ? 9.312   -44.050 -14.262  1.000 221.076 ? 209 SER LLL OG  1 
ATOM 3234 N N   . PRO B 2 210 ? 8.061   -44.271 -17.856  1.000 172.571 ? 210 PRO LLL N   1 
ATOM 3235 C CA  . PRO B 2 210 ? 7.831   -43.144 -18.759  1.000 169.677 ? 210 PRO LLL CA  1 
ATOM 3236 C C   . PRO B 2 210 ? 8.053   -41.789 -18.088  1.000 175.576 ? 210 PRO LLL C   1 
ATOM 3237 O O   . PRO B 2 210 ? 7.451   -41.533 -17.053  1.000 196.691 ? 210 PRO LLL O   1 
ATOM 3238 C CB  . PRO B 2 210 ? 6.360   -43.257 -19.200  1.000 164.687 ? 210 PRO LLL CB  1 
ATOM 3239 C CG  . PRO B 2 210 ? 6.081   -44.733 -19.088  1.000 170.939 ? 210 PRO LLL CG  1 
ATOM 3240 C CD  . PRO B 2 210 ? 6.976   -45.251 -17.973  1.000 179.324 ? 210 PRO LLL CD  1 
ATOM 3241 N N   . VAL B 2 211 ? 8.928   -40.986 -18.700  1.000 174.229 ? 211 VAL LLL N   1 
ATOM 3242 C CA  . VAL B 2 211 ? 9.196   -39.562 -18.334  1.000 170.621 ? 211 VAL LLL CA  1 
ATOM 3243 C C   . VAL B 2 211 ? 8.227   -38.702 -19.140  1.000 162.944 ? 211 VAL LLL C   1 
ATOM 3244 O O   . VAL B 2 211 ? 8.276   -38.753 -20.360  1.000 156.407 ? 211 VAL LLL O   1 
ATOM 3245 C CB  . VAL B 2 211 ? 10.673  -39.127 -18.532  1.000 171.775 ? 211 VAL LLL CB  1 
ATOM 3246 C CG1 . VAL B 2 211 ? 11.320  -39.600 -19.815  1.000 167.996 ? 211 VAL LLL CG1 1 
ATOM 3247 C CG2 . VAL B 2 211 ? 10.855  -37.626 -18.445  1.000 173.462 ? 211 VAL LLL CG2 1 
ATOM 3248 N N   . THR B 2 212 ? 7.373   -37.948 -18.459  1.000 163.393 ? 212 THR LLL N   1 
ATOM 3249 C CA  . THR B 2 212 ? 6.498   -36.938 -19.089  1.000 164.751 ? 212 THR LLL CA  1 
ATOM 3250 C C   . THR B 2 212 ? 7.065   -35.556 -18.799  1.000 162.280 ? 212 THR LLL C   1 
ATOM 3251 O O   . THR B 2 212 ? 7.473   -35.307 -17.638  1.000 164.098 ? 212 THR LLL O   1 
ATOM 3252 C CB  . THR B 2 212 ? 5.056   -37.017 -18.585  1.000 174.859 ? 212 THR LLL CB  1 
ATOM 3253 O OG1 . THR B 2 212 ? 4.690   -38.396 -18.516  1.000 196.042 ? 212 THR LLL OG1 1 
ATOM 3254 C CG2 . THR B 2 212 ? 4.108   -36.252 -19.479  1.000 170.992 ? 212 THR LLL CG2 1 
ATOM 3255 N N   . LYS B 2 213 ? 7.082   -34.712 -19.827  1.000 164.224 ? 213 LYS LLL N   1 
ATOM 3256 C CA  . LYS B 2 213 ? 7.420   -33.274 -19.713  1.000 171.451 ? 213 LYS LLL CA  1 
ATOM 3257 C C   . LYS B 2 213 ? 6.301   -32.467 -20.372  1.000 177.956 ? 213 LYS LLL C   1 
ATOM 3258 O O   . LYS B 2 213 ? 6.093   -32.613 -21.589  1.000 193.227 ? 213 LYS LLL O   1 
ATOM 3259 C CB  . LYS B 2 213 ? 8.771   -32.998 -20.369  1.000 173.495 ? 213 LYS LLL CB  1 
ATOM 3260 C CG  . LYS B 2 213 ? 9.931   -33.831 -19.844  1.000 178.366 ? 213 LYS LLL CG  1 
ATOM 3261 C CD  . LYS B 2 213 ? 10.770  -33.132 -18.785  1.000 181.233 ? 213 LYS LLL CD  1 
ATOM 3262 C CE  . LYS B 2 213 ? 12.021  -33.901 -18.413  1.000 178.880 ? 213 LYS LLL CE  1 
ATOM 3263 N NZ  . LYS B 2 213 ? 12.939  -33.062 -17.612  1.000 181.789 ? 213 LYS LLL NZ  1 
ATOM 3264 N N   . SER B 2 214 ? 5.610   -31.654 -19.575  1.000 177.117 ? 214 SER LLL N   1 
ATOM 3265 C CA  . SER B 2 214 ? 4.362   -30.944 -19.943  1.000 172.464 ? 214 SER LLL CA  1 
ATOM 3266 C C   . SER B 2 214 ? 4.567   -29.446 -19.779  1.000 172.218 ? 214 SER LLL C   1 
ATOM 3267 O O   . SER B 2 214 ? 5.607   -29.066 -19.235  1.000 179.364 ? 214 SER LLL O   1 
ATOM 3268 C CB  . SER B 2 214 ? 3.250   -31.404 -19.063  1.000 177.925 ? 214 SER LLL CB  1 
ATOM 3269 O OG  . SER B 2 214 ? 3.644   -31.318 -17.693  1.000 170.365 ? 214 SER LLL OG  1 
ATOM 3270 N N   . PHE B 2 215 ? 3.602   -28.650 -20.233  1.000 171.010 ? 215 PHE LLL N   1 
ATOM 3271 C CA  . PHE B 2 215 ? 3.479   -27.200 -19.925  1.000 180.517 ? 215 PHE LLL CA  1 
ATOM 3272 C C   . PHE B 2 215 ? 2.023   -26.778 -20.114  1.000 185.098 ? 215 PHE LLL C   1 
ATOM 3273 O O   . PHE B 2 215 ? 1.305   -27.408 -20.913  1.000 197.919 ? 215 PHE LLL O   1 
ATOM 3274 C CB  . PHE B 2 215 ? 4.393   -26.348 -20.810  1.000 181.554 ? 215 PHE LLL CB  1 
ATOM 3275 C CG  . PHE B 2 215 ? 3.947   -26.272 -22.244  1.000 184.234 ? 215 PHE LLL CG  1 
ATOM 3276 C CD1 . PHE B 2 215 ? 4.378   -27.215 -23.161  1.000 194.628 ? 215 PHE LLL CD1 1 
ATOM 3277 C CD2 . PHE B 2 215 ? 3.062   -25.296 -22.663  1.000 188.331 ? 215 PHE LLL CD2 1 
ATOM 3278 C CE1 . PHE B 2 215 ? 3.938   -27.181 -24.473  1.000 201.678 ? 215 PHE LLL CE1 1 
ATOM 3279 C CE2 . PHE B 2 215 ? 2.630   -25.255 -23.978  1.000 194.527 ? 215 PHE LLL CE2 1 
ATOM 3280 C CZ  . PHE B 2 215 ? 3.080   -26.188 -24.883  1.000 200.570 ? 215 PHE LLL CZ  1 
ATOM 3281 N N   . ASN B 2 216 ? 1.610   -25.738 -19.395  1.000 185.056 ? 216 ASN LLL N   1 
ATOM 3282 C CA  . ASN B 2 216 ? 0.263   -25.130 -19.524  1.000 189.200 ? 216 ASN LLL CA  1 
ATOM 3283 C C   . ASN B 2 216 ? 0.377   -23.924 -20.452  1.000 187.993 ? 216 ASN LLL C   1 
ATOM 3284 O O   . ASN B 2 216 ? 1.400   -23.240 -20.336  1.000 196.555 ? 216 ASN LLL O   1 
ATOM 3285 C CB  . ASN B 2 216 ? -0.280  -24.737 -18.158  1.000 195.030 ? 216 ASN LLL CB  1 
ATOM 3286 C CG  . ASN B 2 216 ? -0.455  -25.942 -17.267  1.000 190.312 ? 216 ASN LLL CG  1 
ATOM 3287 O OD1 . ASN B 2 216 ? -1.578  -26.354 -17.016  1.000 195.258 ? 216 ASN LLL OD1 1 
ATOM 3288 N ND2 . ASN B 2 216 ? 0.639   -26.529 -16.820  1.000 187.980 ? 216 ASN LLL ND2 1 
ATOM 3289 N N   . ARG B 2 217 ? -0.613  -23.701 -21.328  1.000 184.164 ? 217 ARG LLL N   1 
ATOM 3290 C CA  . ARG B 2 217 ? -0.582  -22.662 -22.392  1.000 191.762 ? 217 ARG LLL CA  1 
ATOM 3291 C C   . ARG B 2 217 ? -0.351  -21.289 -21.758  1.000 200.831 ? 217 ARG LLL C   1 
ATOM 3292 O O   . ARG B 2 217 ? -1.206  -20.879 -20.952  1.000 215.344 ? 217 ARG LLL O   1 
ATOM 3293 C CB  . ARG B 2 217 ? -1.879  -22.675 -23.202  1.000 192.737 ? 217 ARG LLL CB  1 
ATOM 3294 C CG  . ARG B 2 217 ? -1.938  -21.607 -24.282  1.000 202.924 ? 217 ARG LLL CG  1 
ATOM 3295 C CD  . ARG B 2 217 ? -2.910  -21.956 -25.387  1.000 202.501 ? 217 ARG LLL CD  1 
ATOM 3296 N NE  . ARG B 2 217 ? -4.113  -22.570 -24.849  1.000 206.360 ? 217 ARG LLL NE  1 
ATOM 3297 C CZ  . ARG B 2 217 ? -5.100  -21.924 -24.218  1.000 230.583 ? 217 ARG LLL CZ  1 
ATOM 3298 N NH1 . ARG B 2 217 ? -5.048  -20.617 -24.025  1.000 246.925 ? 217 ARG LLL NH1 1 
ATOM 3299 N NH2 . ARG B 2 217 ? -6.158  -22.583 -23.777  1.000 234.688 ? 217 ARG LLL NH2 1 
ATOM 3300 N N   . GLY B 2 218 ? 0.758   -20.627 -22.128  1.000 213.690 ? 218 GLY LLL N   1 
ATOM 3301 C CA  . GLY B 2 218 ? 1.177   -19.280 -21.679  1.000 222.661 ? 218 GLY LLL CA  1 
ATOM 3302 C C   . GLY B 2 218 ? 1.447   -19.180 -20.178  1.000 227.877 ? 218 GLY LLL C   1 
ATOM 3303 O O   . GLY B 2 218 ? 1.022   -18.170 -19.552  1.000 243.819 ? 218 GLY LLL O   1 
ATOM 3304 N N   . GLU B 2 219 ? 2.140   -20.161 -19.594  1.000 221.091 ? 219 GLU LLL N   1 
ATOM 3305 C CA  . GLU B 2 219 ? 2.599   -20.087 -18.181  1.000 217.987 ? 219 GLU LLL CA  1 
ATOM 3306 C C   . GLU B 2 219 ? 4.066   -20.522 -18.088  1.000 215.640 ? 219 GLU LLL C   1 
ATOM 3307 O O   . GLU B 2 219 ? 4.908   -19.691 -17.738  1.000 211.187 ? 219 GLU LLL O   1 
ATOM 3308 C CB  . GLU B 2 219 ? 1.679   -20.920 -17.291  1.000 221.282 ? 219 GLU LLL CB  1 
ATOM 3309 C CG  . GLU B 2 219 ? 0.196   -20.610 -17.475  1.000 225.326 ? 219 GLU LLL CG  1 
ATOM 3310 C CD  . GLU B 2 219 ? -0.679  -21.025 -16.300  1.000 228.272 ? 219 GLU LLL CD  1 
ATOM 3311 O OE1 . GLU B 2 219 ? -1.623  -20.272 -15.988  1.000 244.645 ? 219 GLU LLL OE1 1 
ATOM 3312 O OE2 . GLU B 2 219 ? -0.393  -22.078 -15.674  1.000 212.158 ? 219 GLU LLL OE2 1 
ATOM 3313 N N   . ASN C 3 3   ? 61.883  -59.339 -70.132  1.000 216.346 ? 334 ASN EEE N   1 
ATOM 3314 C CA  . ASN C 3 3   ? 60.983  -60.254 -70.929  1.000 206.677 ? 334 ASN EEE CA  1 
ATOM 3315 C C   . ASN C 3 3   ? 59.639  -59.542 -71.138  1.000 191.528 ? 334 ASN EEE C   1 
ATOM 3316 O O   . ASN C 3 3   ? 58.622  -60.033 -70.642  1.000 194.171 ? 334 ASN EEE O   1 
ATOM 3317 C CB  . ASN C 3 3   ? 60.859  -61.639 -70.277  1.000 213.602 ? 334 ASN EEE CB  1 
ATOM 3318 C CG  . ASN C 3 3   ? 60.826  -61.568 -68.764  1.000 223.314 ? 334 ASN EEE CG  1 
ATOM 3319 O OD1 . ASN C 3 3   ? 60.772  -60.474 -68.192  1.000 211.307 ? 334 ASN EEE OD1 1 
ATOM 3320 N ND2 . ASN C 3 3   ? 60.888  -62.724 -68.113  1.000 226.975 ? 334 ASN EEE ND2 1 
ATOM 3321 N N   . LEU C 3 4   ? 59.671  -58.408 -71.848  1.000 184.785 ? 335 LEU EEE N   1 
ATOM 3322 C CA  . LEU C 3 4   ? 58.511  -57.566 -72.263  1.000 186.135 ? 335 LEU EEE CA  1 
ATOM 3323 C C   . LEU C 3 4   ? 57.666  -58.312 -73.315  1.000 193.723 ? 335 LEU EEE C   1 
ATOM 3324 O O   . LEU C 3 4   ? 58.265  -58.937 -74.207  1.000 217.988 ? 335 LEU EEE O   1 
ATOM 3325 C CB  . LEU C 3 4   ? 59.096  -56.262 -72.822  1.000 187.980 ? 335 LEU EEE CB  1 
ATOM 3326 C CG  . LEU C 3 4   ? 58.108  -55.162 -73.212  1.000 187.163 ? 335 LEU EEE CG  1 
ATOM 3327 C CD1 . LEU C 3 4   ? 57.600  -54.405 -71.998  1.000 191.755 ? 335 LEU EEE CD1 1 
ATOM 3328 C CD2 . LEU C 3 4   ? 58.747  -54.206 -74.196  1.000 187.627 ? 335 LEU EEE CD2 1 
ATOM 3329 N N   . CYS C 3 5   ? 56.325  -58.259 -73.233  1.000 200.867 ? 336 CYS EEE N   1 
ATOM 3330 C CA  . CYS C 3 5   ? 55.395  -58.920 -74.200  1.000 196.409 ? 336 CYS EEE CA  1 
ATOM 3331 C C   . CYS C 3 5   ? 55.554  -58.274 -75.575  1.000 190.249 ? 336 CYS EEE C   1 
ATOM 3332 O O   . CYS C 3 5   ? 55.623  -57.058 -75.714  1.000 199.076 ? 336 CYS EEE O   1 
ATOM 3333 C CB  . CYS C 3 5   ? 53.921  -58.878 -73.784  1.000 190.447 ? 336 CYS EEE CB  1 
ATOM 3334 S SG  . CYS C 3 5   ? 53.491  -59.876 -72.325  1.000 207.764 ? 336 CYS EEE SG  1 
ATOM 3335 N N   . PRO C 3 6   ? 55.603  -59.072 -76.654  1.000 185.840 ? 337 PRO EEE N   1 
ATOM 3336 C CA  . PRO C 3 6   ? 55.793  -58.527 -77.992  1.000 181.383 ? 337 PRO EEE CA  1 
ATOM 3337 C C   . PRO C 3 6   ? 54.468  -58.045 -78.597  1.000 170.394 ? 337 PRO EEE C   1 
ATOM 3338 O O   . PRO C 3 6   ? 54.145  -58.409 -79.692  1.000 171.189 ? 337 PRO EEE O   1 
ATOM 3339 C CB  . PRO C 3 6   ? 56.347  -59.759 -78.708  1.000 196.867 ? 337 PRO EEE CB  1 
ATOM 3340 C CG  . PRO C 3 6   ? 55.538  -60.893 -78.115  1.000 197.184 ? 337 PRO EEE CG  1 
ATOM 3341 C CD  . PRO C 3 6   ? 55.457  -60.536 -76.649  1.000 190.889 ? 337 PRO EEE CD  1 
ATOM 3342 N N   . PHE C 3 7   ? 53.716  -57.233 -77.865  1.000 171.440 ? 338 PHE EEE N   1 
ATOM 3343 C CA  . PHE C 3 7   ? 52.507  -56.554 -78.397  1.000 171.956 ? 338 PHE EEE CA  1 
ATOM 3344 C C   . PHE C 3 7   ? 52.908  -55.661 -79.573  1.000 171.018 ? 338 PHE EEE C   1 
ATOM 3345 O O   . PHE C 3 7   ? 52.066  -55.463 -80.457  1.000 164.205 ? 338 PHE EEE O   1 
ATOM 3346 C CB  . PHE C 3 7   ? 51.798  -55.708 -77.335  1.000 171.979 ? 338 PHE EEE CB  1 
ATOM 3347 C CG  . PHE C 3 7   ? 50.862  -56.454 -76.422  1.000 169.308 ? 338 PHE EEE CG  1 
ATOM 3348 C CD1 . PHE C 3 7   ? 50.486  -57.770 -76.677  1.000 174.702 ? 338 PHE EEE CD1 1 
ATOM 3349 C CD2 . PHE C 3 7   ? 50.317  -55.809 -75.328  1.000 157.050 ? 338 PHE EEE CD2 1 
ATOM 3350 C CE1 . PHE C 3 7   ? 49.611  -58.434 -75.833  1.000 179.746 ? 338 PHE EEE CE1 1 
ATOM 3351 C CE2 . PHE C 3 7   ? 49.439  -56.475 -74.488  1.000 168.628 ? 338 PHE EEE CE2 1 
ATOM 3352 C CZ  . PHE C 3 7   ? 49.085  -57.782 -74.740  1.000 177.639 ? 338 PHE EEE CZ  1 
ATOM 3353 N N   . GLY C 3 8   ? 54.135  -55.126 -79.563  1.000 176.079 ? 339 GLY EEE N   1 
ATOM 3354 C CA  . GLY C 3 8   ? 54.691  -54.339 -80.682  1.000 183.504 ? 339 GLY EEE CA  1 
ATOM 3355 C C   . GLY C 3 8   ? 54.645  -55.124 -81.988  1.000 182.921 ? 339 GLY EEE C   1 
ATOM 3356 O O   . GLY C 3 8   ? 54.169  -54.563 -83.016  1.000 175.459 ? 339 GLY EEE O   1 
ATOM 3357 N N   . GLU C 3 9   ? 55.118  -56.377 -81.946  1.000 188.335 ? 340 GLU EEE N   1 
ATOM 3358 C CA  . GLU C 3 9   ? 55.064  -57.338 -83.079  1.000 191.162 ? 340 GLU EEE CA  1 
ATOM 3359 C C   . GLU C 3 9   ? 53.642  -57.393 -83.627  1.000 176.707 ? 340 GLU EEE C   1 
ATOM 3360 O O   . GLU C 3 9   ? 53.509  -57.532 -84.845  1.000 203.829 ? 340 GLU EEE O   1 
ATOM 3361 C CB  . GLU C 3 9   ? 55.416  -58.771 -82.673  1.000 201.116 ? 340 GLU EEE CB  1 
ATOM 3362 C CG  . GLU C 3 9   ? 56.898  -59.018 -82.461  1.000 214.247 ? 340 GLU EEE CG  1 
ATOM 3363 C CD  . GLU C 3 9   ? 57.241  -60.469 -82.151  1.000 214.884 ? 340 GLU EEE CD  1 
ATOM 3364 O OE1 . GLU C 3 9   ? 56.380  -61.347 -82.393  1.000 208.862 ? 340 GLU EEE OE1 1 
ATOM 3365 O OE2 . GLU C 3 9   ? 58.358  -60.719 -81.651  1.000 219.836 ? 340 GLU EEE OE2 1 
ATOM 3366 N N   . VAL C 3 10  ? 52.636  -57.346 -82.751  1.000 152.945 ? 341 VAL EEE N   1 
ATOM 3367 C CA  . VAL C 3 10  ? 51.208  -57.584 -83.113  1.000 149.650 ? 341 VAL EEE CA  1 
ATOM 3368 C C   . VAL C 3 10  ? 50.610  -56.303 -83.722  1.000 152.079 ? 341 VAL EEE C   1 
ATOM 3369 O O   . VAL C 3 10  ? 50.194  -56.354 -84.892  1.000 181.059 ? 341 VAL EEE O   1 
ATOM 3370 C CB  . VAL C 3 10  ? 50.403  -58.123 -81.908  1.000 136.866 ? 341 VAL EEE CB  1 
ATOM 3371 C CG1 . VAL C 3 10  ? 48.917  -58.244 -82.204  1.000 126.750 ? 341 VAL EEE CG1 1 
ATOM 3372 C CG2 . VAL C 3 10  ? 50.935  -59.467 -81.419  1.000 133.234 ? 341 VAL EEE CG2 1 
ATOM 3373 N N   . PHE C 3 11  ? 50.582  -55.197 -82.986  1.000 144.288 ? 342 PHE EEE N   1 
ATOM 3374 C CA  . PHE C 3 11  ? 49.819  -53.974 -83.347  1.000 142.224 ? 342 PHE EEE CA  1 
ATOM 3375 C C   . PHE C 3 11  ? 50.582  -53.137 -84.379  1.000 150.832 ? 342 PHE EEE C   1 
ATOM 3376 O O   . PHE C 3 11  ? 49.901  -52.447 -85.149  1.000 162.983 ? 342 PHE EEE O   1 
ATOM 3377 C CB  . PHE C 3 11  ? 49.557  -53.097 -82.118  1.000 148.520 ? 342 PHE EEE CB  1 
ATOM 3378 C CG  . PHE C 3 11  ? 48.534  -53.633 -81.151  1.000 143.117 ? 342 PHE EEE CG  1 
ATOM 3379 C CD1 . PHE C 3 11  ? 48.834  -54.653 -80.257  1.000 134.807 ? 342 PHE EEE CD1 1 
ATOM 3380 C CD2 . PHE C 3 11  ? 47.260  -53.097 -81.131  1.000 144.266 ? 342 PHE EEE CD2 1 
ATOM 3381 C CE1 . PHE C 3 11  ? 47.870  -55.157 -79.398  1.000 129.586 ? 342 PHE EEE CE1 1 
ATOM 3382 C CE2 . PHE C 3 11  ? 46.304  -53.576 -80.248  1.000 139.995 ? 342 PHE EEE CE2 1 
ATOM 3383 C CZ  . PHE C 3 11  ? 46.606  -54.611 -79.389  1.000 131.700 ? 342 PHE EEE CZ  1 
ATOM 3384 N N   . ASN C 3 12  ? 51.922  -53.157 -84.380  1.000 153.335 ? 343 ASN EEE N   1 
ATOM 3385 C CA  . ASN C 3 12  ? 52.750  -52.273 -85.250  1.000 160.039 ? 343 ASN EEE CA  1 
ATOM 3386 C C   . ASN C 3 12  ? 53.245  -53.070 -86.478  1.000 165.744 ? 343 ASN EEE C   1 
ATOM 3387 O O   . ASN C 3 12  ? 53.939  -52.474 -87.336  1.000 163.960 ? 343 ASN EEE O   1 
ATOM 3388 C CB  . ASN C 3 12  ? 53.847  -51.587 -84.420  1.000 167.866 ? 343 ASN EEE CB  1 
ATOM 3389 C CG  . ASN C 3 12  ? 53.391  -50.329 -83.693  1.000 173.439 ? 343 ASN EEE CG  1 
ATOM 3390 O OD1 . ASN C 3 12  ? 52.304  -49.814 -83.970  1.000 188.518 ? 343 ASN EEE OD1 1 
ATOM 3391 N ND2 . ASN C 3 12  ? 54.222  -49.786 -82.795  1.000 161.501 ? 343 ASN EEE ND2 1 
ATOM 3392 N N   . ALA C 3 13  ? 52.864  -54.353 -86.588  1.000 166.487 ? 344 ALA EEE N   1 
ATOM 3393 C CA  . ALA C 3 13  ? 53.191  -55.268 -87.711  1.000 157.924 ? 344 ALA EEE CA  1 
ATOM 3394 C C   . ALA C 3 13  ? 53.027  -54.542 -89.039  1.000 163.827 ? 344 ALA EEE C   1 
ATOM 3395 O O   . ALA C 3 13  ? 52.024  -53.829 -89.195  1.000 161.264 ? 344 ALA EEE O   1 
ATOM 3396 C CB  . ALA C 3 13  ? 52.283  -56.471 -87.696  1.000 150.364 ? 344 ALA EEE CB  1 
ATOM 3397 N N   . THR C 3 14  ? 53.939  -54.781 -89.975  1.000 176.255 ? 345 THR EEE N   1 
ATOM 3398 C CA  . THR C 3 14  ? 53.807  -54.354 -91.393  1.000 189.358 ? 345 THR EEE CA  1 
ATOM 3399 C C   . THR C 3 14  ? 52.667  -55.115 -92.099  1.000 210.085 ? 345 THR EEE C   1 
ATOM 3400 O O   . THR C 3 14  ? 51.853  -54.434 -92.767  1.000 217.196 ? 345 THR EEE O   1 
ATOM 3401 C CB  . THR C 3 14  ? 55.156  -54.510 -92.088  1.000 186.725 ? 345 THR EEE CB  1 
ATOM 3402 O OG1 . THR C 3 14  ? 55.693  -55.748 -91.621  1.000 187.162 ? 345 THR EEE OG1 1 
ATOM 3403 C CG2 . THR C 3 14  ? 56.086  -53.364 -91.766  1.000 188.991 ? 345 THR EEE CG2 1 
ATOM 3404 N N   . ARG C 3 15  ? 52.588  -56.452 -91.966  1.000 225.606 ? 346 ARG EEE N   1 
ATOM 3405 C CA  . ARG C 3 15  ? 51.566  -57.306 -92.657  1.000 224.665 ? 346 ARG EEE CA  1 
ATOM 3406 C C   . ARG C 3 15  ? 50.450  -57.724 -91.688  1.000 192.946 ? 346 ARG EEE C   1 
ATOM 3407 O O   . ARG C 3 15  ? 50.760  -58.288 -90.612  1.000 176.361 ? 346 ARG EEE O   1 
ATOM 3408 C CB  . ARG C 3 15  ? 52.181  -58.573 -93.277  1.000 252.746 ? 346 ARG EEE CB  1 
ATOM 3409 C CG  . ARG C 3 15  ? 51.158  -59.562 -93.832  1.000 264.041 ? 346 ARG EEE CG  1 
ATOM 3410 C CD  . ARG C 3 15  ? 51.751  -60.758 -94.557  1.000 265.668 ? 346 ARG EEE CD  1 
ATOM 3411 N NE  . ARG C 3 15  ? 52.461  -60.364 -95.771  1.000 268.737 ? 346 ARG EEE NE  1 
ATOM 3412 C CZ  . ARG C 3 15  ? 51.891  -60.036 -96.934  1.000 265.163 ? 346 ARG EEE CZ  1 
ATOM 3413 N NH1 . ARG C 3 15  ? 50.574  -60.050 -97.081  1.000 261.566 ? 346 ARG EEE NH1 1 
ATOM 3414 N NH2 . ARG C 3 15  ? 52.651  -59.696 -97.961  1.000 263.517 ? 346 ARG EEE NH2 1 
ATOM 3415 N N   . PHE C 3 16  ? 49.195  -57.521 -92.091  1.000 175.392 ? 347 PHE EEE N   1 
ATOM 3416 C CA  . PHE C 3 16  ? 48.003  -57.996 -91.345  1.000 173.601 ? 347 PHE EEE CA  1 
ATOM 3417 C C   . PHE C 3 16  ? 47.284  -59.044 -92.185  1.000 167.974 ? 347 PHE EEE C   1 
ATOM 3418 O O   . PHE C 3 16  ? 47.298  -58.886 -93.394  1.000 180.248 ? 347 PHE EEE O   1 
ATOM 3419 C CB  . PHE C 3 16  ? 47.099  -56.818 -90.984  1.000 174.811 ? 347 PHE EEE CB  1 
ATOM 3420 C CG  . PHE C 3 16  ? 47.254  -56.356 -89.558  1.000 165.784 ? 347 PHE EEE CG  1 
ATOM 3421 C CD1 . PHE C 3 16  ? 48.479  -55.914 -89.084  1.000 157.574 ? 347 PHE EEE CD1 1 
ATOM 3422 C CD2 . PHE C 3 16  ? 46.175  -56.379 -88.691  1.000 153.664 ? 347 PHE EEE CD2 1 
ATOM 3423 C CE1 . PHE C 3 16  ? 48.616  -55.508 -87.773  1.000 145.603 ? 347 PHE EEE CE1 1 
ATOM 3424 C CE2 . PHE C 3 16  ? 46.312  -55.965 -87.384  1.000 141.833 ? 347 PHE EEE CE2 1 
ATOM 3425 C CZ  . PHE C 3 16  ? 47.532  -55.532 -86.934  1.000 149.057 ? 347 PHE EEE CZ  1 
ATOM 3426 N N   . ALA C 3 17  ? 46.729  -60.081 -91.551  1.000 162.801 ? 348 ALA EEE N   1 
ATOM 3427 C CA  . ALA C 3 17  ? 46.048  -61.233 -92.201  1.000 154.178 ? 348 ALA EEE CA  1 
ATOM 3428 C C   . ALA C 3 17  ? 44.714  -60.798 -92.819  1.000 148.332 ? 348 ALA EEE C   1 
ATOM 3429 O O   . ALA C 3 17  ? 44.194  -59.736 -92.439  1.000 131.684 ? 348 ALA EEE O   1 
ATOM 3430 C CB  . ALA C 3 17  ? 45.811  -62.329 -91.195  1.000 157.505 ? 348 ALA EEE CB  1 
ATOM 3431 N N   . SER C 3 18  ? 44.178  -61.586 -93.758  1.000 159.581 ? 349 SER EEE N   1 
ATOM 3432 C CA  . SER C 3 18  ? 42.778  -61.437 -94.235  1.000 161.027 ? 349 SER EEE CA  1 
ATOM 3433 C C   . SER C 3 18  ? 41.884  -61.976 -93.128  1.000 150.314 ? 349 SER EEE C   1 
ATOM 3434 O O   . SER C 3 18  ? 42.298  -62.929 -92.417  1.000 132.816 ? 349 SER EEE O   1 
ATOM 3435 C CB  . SER C 3 18  ? 42.518  -62.117 -95.553  1.000 167.151 ? 349 SER EEE CB  1 
ATOM 3436 O OG  . SER C 3 18  ? 43.088  -61.363 -96.613  1.000 191.191 ? 349 SER EEE OG  1 
ATOM 3437 N N   . VAL C 3 19  ? 40.721  -61.369 -92.961  1.000 146.812 ? 350 VAL EEE N   1 
ATOM 3438 C CA  . VAL C 3 19  ? 39.851  -61.655 -91.784  1.000 141.422 ? 350 VAL EEE CA  1 
ATOM 3439 C C   . VAL C 3 19  ? 39.422  -63.128 -91.788  1.000 135.902 ? 350 VAL EEE C   1 
ATOM 3440 O O   . VAL C 3 19  ? 39.327  -63.694 -90.722  1.000 142.269 ? 350 VAL EEE O   1 
ATOM 3441 C CB  . VAL C 3 19  ? 38.665  -60.676 -91.724  1.000 143.044 ? 350 VAL EEE CB  1 
ATOM 3442 C CG1 . VAL C 3 19  ? 37.786  -60.769 -92.962  1.000 153.765 ? 350 VAL EEE CG1 1 
ATOM 3443 C CG2 . VAL C 3 19  ? 37.849  -60.850 -90.458  1.000 139.416 ? 350 VAL EEE CG2 1 
ATOM 3444 N N   . TYR C 3 20  ? 39.183  -63.728 -92.947  1.000 153.309 ? 351 TYR EEE N   1 
ATOM 3445 C CA  . TYR C 3 20  ? 38.732  -65.140 -93.085  1.000 159.817 ? 351 TYR EEE CA  1 
ATOM 3446 C C   . TYR C 3 20  ? 39.837  -66.071 -92.544  1.000 150.004 ? 351 TYR EEE C   1 
ATOM 3447 O O   . TYR C 3 20  ? 39.545  -67.164 -92.020  1.000 157.626 ? 351 TYR EEE O   1 
ATOM 3448 C CB  . TYR C 3 20  ? 38.321  -65.442 -94.542  1.000 163.258 ? 351 TYR EEE CB  1 
ATOM 3449 C CG  . TYR C 3 20  ? 39.440  -65.884 -95.457  1.000 159.321 ? 351 TYR EEE CG  1 
ATOM 3450 C CD1 . TYR C 3 20  ? 40.222  -64.966 -96.150  1.000 150.639 ? 351 TYR EEE CD1 1 
ATOM 3451 C CD2 . TYR C 3 20  ? 39.743  -67.233 -95.580  1.000 156.930 ? 351 TYR EEE CD2 1 
ATOM 3452 C CE1 . TYR C 3 20  ? 41.268  -65.389 -96.952  1.000 154.455 ? 351 TYR EEE CE1 1 
ATOM 3453 C CE2 . TYR C 3 20  ? 40.785  -67.671 -96.374  1.000 160.014 ? 351 TYR EEE CE2 1 
ATOM 3454 C CZ  . TYR C 3 20  ? 41.546  -66.745 -97.067  1.000 160.329 ? 351 TYR EEE CZ  1 
ATOM 3455 O OH  . TYR C 3 20  ? 42.570  -67.209 -97.839  1.000 166.403 ? 351 TYR EEE OH  1 
ATOM 3456 N N   . ALA C 3 21  ? 41.094  -65.681 -92.698  1.000 136.422 ? 352 ALA EEE N   1 
ATOM 3457 C CA  . ALA C 3 21  ? 42.241  -66.538 -92.345  1.000 148.263 ? 352 ALA EEE CA  1 
ATOM 3458 C C   . ALA C 3 21  ? 43.036  -65.832 -91.266  1.000 150.852 ? 352 ALA EEE C   1 
ATOM 3459 O O   . ALA C 3 21  ? 44.280  -65.741 -91.434  1.000 134.797 ? 352 ALA EEE O   1 
ATOM 3460 C CB  . ALA C 3 21  ? 43.097  -66.786 -93.547  1.000 169.185 ? 352 ALA EEE CB  1 
ATOM 3461 N N   . TRP C 3 22  ? 42.311  -65.379 -90.232  1.000 167.252 ? 353 TRP EEE N   1 
ATOM 3462 C CA  . TRP C 3 22  ? 42.763  -64.452 -89.157  1.000 163.340 ? 353 TRP EEE CA  1 
ATOM 3463 C C   . TRP C 3 22  ? 43.953  -65.051 -88.417  1.000 162.817 ? 353 TRP EEE C   1 
ATOM 3464 O O   . TRP C 3 22  ? 44.035  -66.293 -88.314  1.000 170.755 ? 353 TRP EEE O   1 
ATOM 3465 C CB  . TRP C 3 22  ? 41.624  -64.101 -88.196  1.000 165.561 ? 353 TRP EEE CB  1 
ATOM 3466 C CG  . TRP C 3 22  ? 40.812  -65.250 -87.670  1.000 168.004 ? 353 TRP EEE CG  1 
ATOM 3467 C CD1 . TRP C 3 22  ? 39.672  -65.781 -88.212  1.000 161.030 ? 353 TRP EEE CD1 1 
ATOM 3468 C CD2 . TRP C 3 22  ? 41.034  -65.956 -86.435  1.000 171.615 ? 353 TRP EEE CD2 1 
ATOM 3469 N NE1 . TRP C 3 22  ? 39.189  -66.784 -87.421  1.000 160.539 ? 353 TRP EEE NE1 1 
ATOM 3470 C CE2 . TRP C 3 22  ? 39.998  -66.908 -86.316  1.000 172.271 ? 353 TRP EEE CE2 1 
ATOM 3471 C CE3 . TRP C 3 22  ? 42.015  -65.893 -85.433  1.000 153.989 ? 353 TRP EEE CE3 1 
ATOM 3472 C CZ2 . TRP C 3 22  ? 39.915  -67.763 -85.215  1.000 160.135 ? 353 TRP EEE CZ2 1 
ATOM 3473 C CZ3 . TRP C 3 22  ? 41.938  -66.759 -84.366  1.000 140.972 ? 353 TRP EEE CZ3 1 
ATOM 3474 C CH2 . TRP C 3 22  ? 40.908  -67.687 -84.265  1.000 140.025 ? 353 TRP EEE CH2 1 
ATOM 3475 N N   . ASN C 3 23  ? 44.875  -64.188 -87.996  1.000 160.679 ? 354 ASN EEE N   1 
ATOM 3476 C CA  . ASN C 3 23  ? 46.155  -64.608 -87.374  1.000 170.083 ? 354 ASN EEE CA  1 
ATOM 3477 C C   . ASN C 3 23  ? 45.940  -64.661 -85.852  1.000 175.330 ? 354 ASN EEE C   1 
ATOM 3478 O O   . ASN C 3 23  ? 45.272  -63.751 -85.314  1.000 183.871 ? 354 ASN EEE O   1 
ATOM 3479 C CB  . ASN C 3 23  ? 47.296  -63.673 -87.790  1.000 178.163 ? 354 ASN EEE CB  1 
ATOM 3480 C CG  . ASN C 3 23  ? 48.510  -64.414 -88.315  1.000 184.012 ? 354 ASN EEE CG  1 
ATOM 3481 O OD1 . ASN C 3 23  ? 49.294  -65.005 -87.567  1.000 191.784 ? 354 ASN EEE OD1 1 
ATOM 3482 N ND2 . ASN C 3 23  ? 48.697  -64.348 -89.620  1.000 193.567 ? 354 ASN EEE ND2 1 
ATOM 3483 N N   . ARG C 3 24  ? 46.458  -65.695 -85.179  1.000 163.854 ? 355 ARG EEE N   1 
ATOM 3484 C CA  . ARG C 3 24  ? 46.459  -65.802 -83.695  1.000 146.520 ? 355 ARG EEE CA  1 
ATOM 3485 C C   . ARG C 3 24  ? 47.890  -65.887 -83.190  1.000 149.713 ? 355 ARG EEE C   1 
ATOM 3486 O O   . ARG C 3 24  ? 48.610  -66.822 -83.616  1.000 154.633 ? 355 ARG EEE O   1 
ATOM 3487 C CB  . ARG C 3 24  ? 45.779  -67.072 -83.195  1.000 146.305 ? 355 ARG EEE CB  1 
ATOM 3488 C CG  . ARG C 3 24  ? 45.929  -67.315 -81.700  1.000 143.864 ? 355 ARG EEE CG  1 
ATOM 3489 C CD  . ARG C 3 24  ? 44.798  -68.131 -81.086  1.000 138.876 ? 355 ARG EEE CD  1 
ATOM 3490 N NE  . ARG C 3 24  ? 43.576  -67.346 -80.913  1.000 127.086 ? 355 ARG EEE NE  1 
ATOM 3491 C CZ  . ARG C 3 24  ? 42.456  -67.813 -80.368  1.000 130.367 ? 355 ARG EEE CZ  1 
ATOM 3492 N NH1 . ARG C 3 24  ? 42.409  -69.071 -79.932  1.000 131.235 ? 355 ARG EEE NH1 1 
ATOM 3493 N NH2 . ARG C 3 24  ? 41.401  -67.014 -80.254  1.000 129.241 ? 355 ARG EEE NH2 1 
ATOM 3494 N N   . LYS C 3 25  ? 48.249  -64.952 -82.308  1.000 150.608 ? 356 LYS EEE N   1 
ATOM 3495 C CA  . LYS C 3 25  ? 49.457  -64.994 -81.440  1.000 145.570 ? 356 LYS EEE CA  1 
ATOM 3496 C C   . LYS C 3 25  ? 49.028  -65.470 -80.051  1.000 141.965 ? 356 LYS EEE C   1 
ATOM 3497 O O   . LYS C 3 25  ? 48.082  -64.887 -79.471  1.000 133.556 ? 356 LYS EEE O   1 
ATOM 3498 C CB  . LYS C 3 25  ? 50.117  -63.613 -81.381  1.000 142.931 ? 356 LYS EEE CB  1 
ATOM 3499 C CG  . LYS C 3 25  ? 51.329  -63.488 -80.473  1.000 138.914 ? 356 LYS EEE CG  1 
ATOM 3500 C CD  . LYS C 3 25  ? 52.353  -64.584 -80.686  1.000 143.491 ? 356 LYS EEE CD  1 
ATOM 3501 C CE  . LYS C 3 25  ? 53.720  -64.288 -80.097  1.000 148.633 ? 356 LYS EEE CE  1 
ATOM 3502 N NZ  . LYS C 3 25  ? 54.473  -63.277 -80.889  1.000 145.431 ? 356 LYS EEE NZ  1 
ATOM 3503 N N   . ARG C 3 26  ? 49.658  -66.535 -79.568  1.000 147.274 ? 357 ARG EEE N   1 
ATOM 3504 C CA  . ARG C 3 26  ? 49.585  -66.932 -78.143  1.000 158.816 ? 357 ARG EEE CA  1 
ATOM 3505 C C   . ARG C 3 26  ? 50.756  -66.247 -77.425  1.000 169.492 ? 357 ARG EEE C   1 
ATOM 3506 O O   . ARG C 3 26  ? 51.944  -66.490 -77.810  1.000 168.942 ? 357 ARG EEE O   1 
ATOM 3507 C CB  . ARG C 3 26  ? 49.580  -68.452 -77.971  1.000 161.759 ? 357 ARG EEE CB  1 
ATOM 3508 C CG  . ARG C 3 26  ? 49.437  -68.916 -76.525  1.000 167.225 ? 357 ARG EEE CG  1 
ATOM 3509 C CD  . ARG C 3 26  ? 49.851  -70.353 -76.260  1.000 168.322 ? 357 ARG EEE CD  1 
ATOM 3510 N NE  . ARG C 3 26  ? 51.268  -70.390 -76.598  1.000 179.994 ? 357 ARG EEE NE  1 
ATOM 3511 C CZ  . ARG C 3 26  ? 52.228  -71.056 -75.966  1.000 192.054 ? 357 ARG EEE CZ  1 
ATOM 3512 N NH1 . ARG C 3 26  ? 51.974  -71.818 -74.913  1.000 200.755 ? 357 ARG EEE NH1 1 
ATOM 3513 N NH2 . ARG C 3 26  ? 53.467  -70.957 -76.421  1.000 197.394 ? 357 ARG EEE NH2 1 
ATOM 3514 N N   . ILE C 3 27  ? 50.399  -65.418 -76.435  1.000 171.101 ? 358 ILE EEE N   1 
ATOM 3515 C CA  . ILE C 3 27  ? 51.303  -64.674 -75.515  1.000 156.856 ? 358 ILE EEE CA  1 
ATOM 3516 C C   . ILE C 3 27  ? 51.481  -65.553 -74.266  1.000 148.516 ? 358 ILE EEE C   1 
ATOM 3517 O O   . ILE C 3 27  ? 50.463  -66.102 -73.712  1.000 132.080 ? 358 ILE EEE O   1 
ATOM 3518 C CB  . ILE C 3 27  ? 50.714  -63.270 -75.238  1.000 161.504 ? 358 ILE EEE CB  1 
ATOM 3519 C CG1 . ILE C 3 27  ? 50.405  -62.504 -76.528  1.000 158.280 ? 358 ILE EEE CG1 1 
ATOM 3520 C CG2 . ILE C 3 27  ? 51.617  -62.441 -74.342  1.000 173.133 ? 358 ILE EEE CG2 1 
ATOM 3521 C CD1 . ILE C 3 27  ? 51.634  -61.933 -77.220  1.000 155.833 ? 358 ILE EEE CD1 1 
ATOM 3522 N N   . SER C 3 28  ? 52.741  -65.779 -73.907  1.000 148.427 ? 359 SER EEE N   1 
ATOM 3523 C CA  . SER C 3 28  ? 53.147  -66.439 -72.647  1.000 169.453 ? 359 SER EEE CA  1 
ATOM 3524 C C   . SER C 3 28  ? 54.574  -65.982 -72.282  1.000 183.974 ? 359 SER EEE C   1 
ATOM 3525 O O   . SER C 3 28  ? 55.275  -65.409 -73.152  1.000 191.628 ? 359 SER EEE O   1 
ATOM 3526 C CB  . SER C 3 28  ? 52.969  -67.939 -72.769  1.000 171.457 ? 359 SER EEE CB  1 
ATOM 3527 O OG  . SER C 3 28  ? 54.079  -68.544 -73.401  1.000 190.217 ? 359 SER EEE OG  1 
ATOM 3528 N N   . ASN C 3 29  ? 54.957  -66.149 -71.012  1.000 188.314 ? 360 ASN EEE N   1 
ATOM 3529 C CA  . ASN C 3 29  ? 56.325  -65.904 -70.487  1.000 191.568 ? 360 ASN EEE CA  1 
ATOM 3530 C C   . ASN C 3 29  ? 56.724  -64.458 -70.741  1.000 181.224 ? 360 ASN EEE C   1 
ATOM 3531 O O   . ASN C 3 29  ? 57.849  -64.237 -71.201  1.000 192.431 ? 360 ASN EEE O   1 
ATOM 3532 C CB  . ASN C 3 29  ? 57.354  -66.850 -71.107  1.000 203.390 ? 360 ASN EEE CB  1 
ATOM 3533 C CG  . ASN C 3 29  ? 57.513  -68.121 -70.310  1.000 209.236 ? 360 ASN EEE CG  1 
ATOM 3534 O OD1 . ASN C 3 29  ? 57.026  -69.168 -70.717  1.000 223.341 ? 360 ASN EEE OD1 1 
ATOM 3535 N ND2 . ASN C 3 29  ? 58.165  -68.019 -69.165  1.000 205.299 ? 360 ASN EEE ND2 1 
ATOM 3536 N N   . CYS C 3 30  ? 55.864  -63.505 -70.424  1.000 166.795 ? 361 CYS EEE N   1 
ATOM 3537 C CA  . CYS C 3 30  ? 56.273  -62.093 -70.542  1.000 181.140 ? 361 CYS EEE CA  1 
ATOM 3538 C C   . CYS C 3 30  ? 55.484  -61.191 -69.594  1.000 183.062 ? 361 CYS EEE C   1 
ATOM 3539 O O   . CYS C 3 30  ? 54.421  -61.612 -69.092  1.000 182.589 ? 361 CYS EEE O   1 
ATOM 3540 C CB  . CYS C 3 30  ? 56.085  -61.617 -71.968  1.000 182.225 ? 361 CYS EEE CB  1 
ATOM 3541 S SG  . CYS C 3 30  ? 54.351  -61.769 -72.451  1.000 207.448 ? 361 CYS EEE SG  1 
ATOM 3542 N N   . VAL C 3 31  ? 56.054  -60.005 -69.387  1.000 178.256 ? 362 VAL EEE N   1 
ATOM 3543 C CA  . VAL C 3 31  ? 55.476  -58.848 -68.665  1.000 175.672 ? 362 VAL EEE CA  1 
ATOM 3544 C C   . VAL C 3 31  ? 54.738  -57.993 -69.685  1.000 169.221 ? 362 VAL EEE C   1 
ATOM 3545 O O   . VAL C 3 31  ? 55.378  -57.590 -70.653  1.000 161.073 ? 362 VAL EEE O   1 
ATOM 3546 C CB  . VAL C 3 31  ? 56.591  -58.020 -68.014  1.000 196.040 ? 362 VAL EEE CB  1 
ATOM 3547 C CG1 . VAL C 3 31  ? 56.031  -56.798 -67.294  1.000 205.698 ? 362 VAL EEE CG1 1 
ATOM 3548 C CG2 . VAL C 3 31  ? 57.452  -58.872 -67.093  1.000 210.999 ? 362 VAL EEE CG2 1 
ATOM 3549 N N   . ALA C 3 32  ? 53.467  -57.696 -69.435  1.000 171.700 ? 363 ALA EEE N   1 
ATOM 3550 C CA  . ALA C 3 32  ? 52.562  -56.951 -70.338  1.000 174.164 ? 363 ALA EEE CA  1 
ATOM 3551 C C   . ALA C 3 32  ? 52.274  -55.569 -69.756  1.000 167.131 ? 363 ALA EEE C   1 
ATOM 3552 O O   . ALA C 3 32  ? 51.554  -55.522 -68.754  1.000 189.927 ? 363 ALA EEE O   1 
ATOM 3553 C CB  . ALA C 3 32  ? 51.281  -57.732 -70.486  1.000 181.670 ? 363 ALA EEE CB  1 
ATOM 3554 N N   . ASP C 3 33  ? 52.813  -54.489 -70.322  1.000 162.432 ? 364 ASP EEE N   1 
ATOM 3555 C CA  . ASP C 3 33  ? 52.454  -53.122 -69.854  1.000 176.896 ? 364 ASP EEE CA  1 
ATOM 3556 C C   . ASP C 3 33  ? 51.247  -52.674 -70.674  1.000 176.828 ? 364 ASP EEE C   1 
ATOM 3557 O O   . ASP C 3 33  ? 51.448  -52.117 -71.759  1.000 202.832 ? 364 ASP EEE O   1 
ATOM 3558 C CB  . ASP C 3 33  ? 53.623  -52.134 -69.937  1.000 189.353 ? 364 ASP EEE CB  1 
ATOM 3559 C CG  . ASP C 3 33  ? 53.393  -50.804 -69.223  1.000 196.926 ? 364 ASP EEE CG  1 
ATOM 3560 O OD1 . ASP C 3 33  ? 52.411  -50.695 -68.450  1.000 189.530 ? 364 ASP EEE OD1 1 
ATOM 3561 O OD2 . ASP C 3 33  ? 54.207  -49.881 -69.444  1.000 213.561 ? 364 ASP EEE OD2 1 
ATOM 3562 N N   . TYR C 3 34  ? 50.039  -52.936 -70.180  1.000 174.494 ? 365 TYR EEE N   1 
ATOM 3563 C CA  . TYR C 3 34  ? 48.769  -52.727 -70.928  1.000 170.447 ? 365 TYR EEE CA  1 
ATOM 3564 C C   . TYR C 3 34  ? 48.553  -51.208 -71.158  1.000 158.788 ? 365 TYR EEE C   1 
ATOM 3565 O O   . TYR C 3 34  ? 47.958  -50.792 -72.180  1.000 137.089 ? 365 TYR EEE O   1 
ATOM 3566 C CB  . TYR C 3 34  ? 47.621  -53.460 -70.210  1.000 172.010 ? 365 TYR EEE CB  1 
ATOM 3567 C CG  . TYR C 3 34  ? 47.728  -54.969 -70.084  1.000 163.890 ? 365 TYR EEE CG  1 
ATOM 3568 C CD1 . TYR C 3 34  ? 47.338  -55.821 -71.107  1.000 159.696 ? 365 TYR EEE CD1 1 
ATOM 3569 C CD2 . TYR C 3 34  ? 48.155  -55.563 -68.908  1.000 169.186 ? 365 TYR EEE CD2 1 
ATOM 3570 C CE1 . TYR C 3 34  ? 47.404  -57.204 -70.990  1.000 154.836 ? 365 TYR EEE CE1 1 
ATOM 3571 C CE2 . TYR C 3 34  ? 48.224  -56.941 -68.768  1.000 173.491 ? 365 TYR EEE CE2 1 
ATOM 3572 C CZ  . TYR C 3 34  ? 47.847  -57.767 -69.810  1.000 168.081 ? 365 TYR EEE CZ  1 
ATOM 3573 O OH  . TYR C 3 34  ? 47.918  -59.117 -69.627  1.000 176.072 ? 365 TYR EEE OH  1 
ATOM 3574 N N   . SER C 3 35  ? 49.064  -50.364 -70.260  1.000 160.887 ? 366 SER EEE N   1 
ATOM 3575 C CA  . SER C 3 35  ? 48.881  -48.892 -70.322  1.000 167.469 ? 366 SER EEE CA  1 
ATOM 3576 C C   . SER C 3 35  ? 49.333  -48.369 -71.682  1.000 168.267 ? 366 SER EEE C   1 
ATOM 3577 O O   . SER C 3 35  ? 48.790  -47.321 -72.107  1.000 174.336 ? 366 SER EEE O   1 
ATOM 3578 C CB  . SER C 3 35  ? 49.598  -48.164 -69.216  1.000 174.706 ? 366 SER EEE CB  1 
ATOM 3579 O OG  . SER C 3 35  ? 50.967  -47.944 -69.533  1.000 177.033 ? 366 SER EEE OG  1 
ATOM 3580 N N   . VAL C 3 36  ? 50.292  -49.047 -72.323  1.000 159.021 ? 367 VAL EEE N   1 
ATOM 3581 C CA  . VAL C 3 36  ? 50.905  -48.536 -73.583  1.000 160.029 ? 367 VAL EEE CA  1 
ATOM 3582 C C   . VAL C 3 36  ? 49.837  -48.583 -74.664  1.000 155.147 ? 367 VAL EEE C   1 
ATOM 3583 O O   . VAL C 3 36  ? 49.909  -47.743 -75.565  1.000 166.843 ? 367 VAL EEE O   1 
ATOM 3584 C CB  . VAL C 3 36  ? 52.184  -49.270 -74.024  1.000 165.045 ? 367 VAL EEE CB  1 
ATOM 3585 C CG1 . VAL C 3 36  ? 52.714  -48.673 -75.330  1.000 155.643 ? 367 VAL EEE CG1 1 
ATOM 3586 C CG2 . VAL C 3 36  ? 53.259  -49.234 -72.938  1.000 180.547 ? 367 VAL EEE CG2 1 
ATOM 3587 N N   . LEU C 3 37  ? 48.867  -49.492 -74.545  1.000 147.625 ? 368 LEU EEE N   1 
ATOM 3588 C CA  . LEU C 3 37  ? 47.699  -49.534 -75.464  1.000 143.436 ? 368 LEU EEE CA  1 
ATOM 3589 C C   . LEU C 3 37  ? 46.696  -48.444 -75.103  1.000 156.479 ? 368 LEU EEE C   1 
ATOM 3590 O O   . LEU C 3 37  ? 46.375  -47.671 -76.007  1.000 162.442 ? 368 LEU EEE O   1 
ATOM 3591 C CB  . LEU C 3 37  ? 46.982  -50.880 -75.394  1.000 135.089 ? 368 LEU EEE CB  1 
ATOM 3592 C CG  . LEU C 3 37  ? 47.816  -52.088 -75.788  1.000 132.971 ? 368 LEU EEE CG  1 
ATOM 3593 C CD1 . LEU C 3 37  ? 46.975  -53.347 -75.718  1.000 130.796 ? 368 LEU EEE CD1 1 
ATOM 3594 C CD2 . LEU C 3 37  ? 48.407  -51.903 -77.167  1.000 136.373 ? 368 LEU EEE CD2 1 
ATOM 3595 N N   . TYR C 3 38  ? 46.161  -48.453 -73.872  1.000 163.536 ? 369 TYR EEE N   1 
ATOM 3596 C CA  . TYR C 3 38  ? 44.926  -47.710 -73.496  1.000 157.464 ? 369 TYR EEE CA  1 
ATOM 3597 C C   . TYR C 3 38  ? 45.289  -46.225 -73.338  1.000 147.705 ? 369 TYR EEE C   1 
ATOM 3598 O O   . TYR C 3 38  ? 44.387  -45.420 -73.475  1.000 149.945 ? 369 TYR EEE O   1 
ATOM 3599 C CB  . TYR C 3 38  ? 44.163  -48.366 -72.319  1.000 162.860 ? 369 TYR EEE CB  1 
ATOM 3600 C CG  . TYR C 3 38  ? 44.815  -48.370 -70.951  1.000 162.092 ? 369 TYR EEE CG  1 
ATOM 3601 C CD1 . TYR C 3 38  ? 44.909  -47.199 -70.219  1.000 165.201 ? 369 TYR EEE CD1 1 
ATOM 3602 C CD2 . TYR C 3 38  ? 45.312  -49.533 -70.371  1.000 154.354 ? 369 TYR EEE CD2 1 
ATOM 3603 C CE1 . TYR C 3 38  ? 45.509  -47.178 -68.974  1.000 176.782 ? 369 TYR EEE CE1 1 
ATOM 3604 C CE2 . TYR C 3 38  ? 45.915  -49.528 -69.124  1.000 159.031 ? 369 TYR EEE CE2 1 
ATOM 3605 C CZ  . TYR C 3 38  ? 46.019  -48.341 -68.425  1.000 176.317 ? 369 TYR EEE CZ  1 
ATOM 3606 O OH  . TYR C 3 38  ? 46.606  -48.327 -67.191  1.000 188.659 ? 369 TYR EEE OH  1 
ATOM 3607 N N   . ASN C 3 39  ? 46.550  -45.857 -73.105  1.000 140.981 ? 370 ASN EEE N   1 
ATOM 3608 C CA  . ASN C 3 39  ? 46.929  -44.422 -72.981  1.000 164.087 ? 370 ASN EEE CA  1 
ATOM 3609 C C   . ASN C 3 39  ? 47.326  -43.873 -74.357  1.000 162.053 ? 370 ASN EEE C   1 
ATOM 3610 O O   . ASN C 3 39  ? 47.469  -42.640 -74.491  1.000 161.994 ? 370 ASN EEE O   1 
ATOM 3611 C CB  . ASN C 3 39  ? 48.006  -44.187 -71.914  1.000 180.288 ? 370 ASN EEE CB  1 
ATOM 3612 C CG  . ASN C 3 39  ? 47.469  -44.211 -70.493  1.000 180.168 ? 370 ASN EEE CG  1 
ATOM 3613 O OD1 . ASN C 3 39  ? 46.274  -43.999 -70.248  1.000 162.059 ? 370 ASN EEE OD1 1 
ATOM 3614 N ND2 . ASN C 3 39  ? 48.355  -44.485 -69.547  1.000 174.803 ? 370 ASN EEE ND2 1 
ATOM 3615 N N   . SER C 3 40  ? 47.475  -44.753 -75.345  1.000 168.917 ? 371 SER EEE N   1 
ATOM 3616 C CA  . SER C 3 40  ? 47.743  -44.414 -76.768  1.000 173.249 ? 371 SER EEE CA  1 
ATOM 3617 C C   . SER C 3 40  ? 46.583  -43.584 -77.325  1.000 181.191 ? 371 SER EEE C   1 
ATOM 3618 O O   . SER C 3 40  ? 45.433  -43.837 -76.926  1.000 197.036 ? 371 SER EEE O   1 
ATOM 3619 C CB  . SER C 3 40  ? 47.926  -45.683 -77.559  1.000 177.267 ? 371 SER EEE CB  1 
ATOM 3620 O OG  . SER C 3 40  ? 47.945  -45.421 -78.947  1.000 202.238 ? 371 SER EEE OG  1 
ATOM 3621 N N   . ALA C 3 41  ? 46.842  -42.655 -78.245  1.000 180.965 ? 372 ALA EEE N   1 
ATOM 3622 C CA  . ALA C 3 41  ? 45.757  -41.914 -78.936  1.000 189.184 ? 372 ALA EEE CA  1 
ATOM 3623 C C   . ALA C 3 41  ? 45.396  -42.577 -80.285  1.000 195.438 ? 372 ALA EEE C   1 
ATOM 3624 O O   . ALA C 3 41  ? 44.444  -42.090 -80.949  1.000 204.133 ? 372 ALA EEE O   1 
ATOM 3625 C CB  . ALA C 3 41  ? 46.158  -40.470 -79.078  1.000 184.166 ? 372 ALA EEE CB  1 
ATOM 3626 N N   . SER C 3 42  ? 46.063  -43.690 -80.626  1.000 188.917 ? 373 SER EEE N   1 
ATOM 3627 C CA  . SER C 3 42  ? 46.153  -44.281 -81.988  1.000 173.857 ? 373 SER EEE CA  1 
ATOM 3628 C C   . SER C 3 42  ? 44.900  -45.058 -82.348  1.000 163.949 ? 373 SER EEE C   1 
ATOM 3629 O O   . SER C 3 42  ? 44.681  -45.224 -83.555  1.000 174.690 ? 373 SER EEE O   1 
ATOM 3630 C CB  . SER C 3 42  ? 47.329  -45.190 -82.108  1.000 183.158 ? 373 SER EEE CB  1 
ATOM 3631 O OG  . SER C 3 42  ? 48.535  -44.460 -81.975  1.000 215.131 ? 373 SER EEE OG  1 
ATOM 3632 N N   . PHE C 3 43  ? 44.131  -45.514 -81.360  1.000 160.585 ? 374 PHE EEE N   1 
ATOM 3633 C CA  . PHE C 3 43  ? 42.977  -46.422 -81.577  1.000 157.977 ? 374 PHE EEE CA  1 
ATOM 3634 C C   . PHE C 3 43  ? 41.680  -45.634 -81.496  1.000 146.666 ? 374 PHE EEE C   1 
ATOM 3635 O O   . PHE C 3 43  ? 41.551  -44.672 -80.713  1.000 142.893 ? 374 PHE EEE O   1 
ATOM 3636 C CB  . PHE C 3 43  ? 42.942  -47.566 -80.569  1.000 167.893 ? 374 PHE EEE CB  1 
ATOM 3637 C CG  . PHE C 3 43  ? 44.261  -48.260 -80.364  1.000 174.929 ? 374 PHE EEE CG  1 
ATOM 3638 C CD1 . PHE C 3 43  ? 44.849  -48.942 -81.404  1.000 180.878 ? 374 PHE EEE CD1 1 
ATOM 3639 C CD2 . PHE C 3 43  ? 44.908  -48.247 -79.138  1.000 187.586 ? 374 PHE EEE CD2 1 
ATOM 3640 C CE1 . PHE C 3 43  ? 46.059  -49.595 -81.232  1.000 190.333 ? 374 PHE EEE CE1 1 
ATOM 3641 C CE2 . PHE C 3 43  ? 46.128  -48.884 -78.978  1.000 189.023 ? 374 PHE EEE CE2 1 
ATOM 3642 C CZ  . PHE C 3 43  ? 46.697  -49.568 -80.019  1.000 189.496 ? 374 PHE EEE CZ  1 
ATOM 3643 N N   . SER C 3 44  ? 40.754  -46.044 -82.341  1.000 140.757 ? 375 SER EEE N   1 
ATOM 3644 C CA  . SER C 3 44  ? 39.480  -45.334 -82.543  1.000 153.393 ? 375 SER EEE CA  1 
ATOM 3645 C C   . SER C 3 44  ? 38.388  -46.136 -81.864  1.000 148.337 ? 375 SER EEE C   1 
ATOM 3646 O O   . SER C 3 44  ? 37.422  -45.501 -81.413  1.000 156.352 ? 375 SER EEE O   1 
ATOM 3647 C CB  . SER C 3 44  ? 39.210  -45.133 -83.997  1.000 169.409 ? 375 SER EEE CB  1 
ATOM 3648 O OG  . SER C 3 44  ? 39.418  -46.340 -84.697  1.000 169.920 ? 375 SER EEE OG  1 
ATOM 3649 N N   . THR C 3 45  ? 38.552  -47.460 -81.810  1.000 147.975 ? 376 THR EEE N   1 
ATOM 3650 C CA  . THR C 3 45  ? 37.690  -48.389 -81.030  1.000 155.743 ? 376 THR EEE CA  1 
ATOM 3651 C C   . THR C 3 45  ? 38.540  -49.158 -80.019  1.000 153.804 ? 376 THR EEE C   1 
ATOM 3652 O O   . THR C 3 45  ? 39.614  -49.703 -80.399  1.000 144.612 ? 376 THR EEE O   1 
ATOM 3653 C CB  . THR C 3 45  ? 36.929  -49.356 -81.942  1.000 171.008 ? 376 THR EEE CB  1 
ATOM 3654 O OG1 . THR C 3 45  ? 35.967  -48.571 -82.649  1.000 180.916 ? 376 THR EEE OG1 1 
ATOM 3655 C CG2 . THR C 3 45  ? 36.237  -50.477 -81.197  1.000 167.632 ? 376 THR EEE CG2 1 
ATOM 3656 N N   . PHE C 3 46  ? 38.059  -49.208 -78.775  1.000 154.767 ? 377 PHE EEE N   1 
ATOM 3657 C CA  . PHE C 3 46  ? 38.704  -49.912 -77.635  1.000 145.666 ? 377 PHE EEE CA  1 
ATOM 3658 C C   . PHE C 3 46  ? 37.598  -50.328 -76.670  1.000 135.708 ? 377 PHE EEE C   1 
ATOM 3659 O O   . PHE C 3 46  ? 37.297  -49.599 -75.711  1.000 149.433 ? 377 PHE EEE O   1 
ATOM 3660 C CB  . PHE C 3 46  ? 39.781  -49.030 -76.999  1.000 142.963 ? 377 PHE EEE CB  1 
ATOM 3661 C CG  . PHE C 3 46  ? 40.910  -49.765 -76.310  1.000 139.088 ? 377 PHE EEE CG  1 
ATOM 3662 C CD1 . PHE C 3 46  ? 40.660  -50.791 -75.406  1.000 128.527 ? 377 PHE EEE CD1 1 
ATOM 3663 C CD2 . PHE C 3 46  ? 42.227  -49.379 -76.526  1.000 135.594 ? 377 PHE EEE CD2 1 
ATOM 3664 C CE1 . PHE C 3 46  ? 41.704  -51.425 -74.754  1.000 119.506 ? 377 PHE EEE CE1 1 
ATOM 3665 C CE2 . PHE C 3 46  ? 43.266  -50.035 -75.899  1.000 127.694 ? 377 PHE EEE CE2 1 
ATOM 3666 C CZ  . PHE C 3 46  ? 43.000  -51.045 -75.009  1.000 125.010 ? 377 PHE EEE CZ  1 
ATOM 3667 N N   . LYS C 3 47  ? 36.996  -51.471 -76.963  1.000 128.486 ? 378 LYS EEE N   1 
ATOM 3668 C CA  . LYS C 3 47  ? 35.847  -52.026 -76.222  1.000 142.324 ? 378 LYS EEE CA  1 
ATOM 3669 C C   . LYS C 3 47  ? 36.334  -53.230 -75.453  1.000 146.140 ? 378 LYS EEE C   1 
ATOM 3670 O O   . LYS C 3 47  ? 36.866  -54.116 -76.129  1.000 149.566 ? 378 LYS EEE O   1 
ATOM 3671 C CB  . LYS C 3 47  ? 34.760  -52.533 -77.164  1.000 144.723 ? 378 LYS EEE CB  1 
ATOM 3672 C CG  . LYS C 3 47  ? 33.744  -51.480 -77.545  1.000 149.879 ? 378 LYS EEE CG  1 
ATOM 3673 C CD  . LYS C 3 47  ? 32.506  -52.062 -78.178  1.000 154.586 ? 378 LYS EEE CD  1 
ATOM 3674 C CE  . LYS C 3 47  ? 31.509  -50.980 -78.531  1.000 167.845 ? 378 LYS EEE CE  1 
ATOM 3675 N NZ  . LYS C 3 47  ? 30.400  -51.477 -79.378  1.000 175.229 ? 378 LYS EEE NZ  1 
ATOM 3676 N N   . CYS C 3 48  ? 36.147  -53.269 -74.130  1.000 141.954 ? 379 CYS EEE N   1 
ATOM 3677 C CA  . CYS C 3 48  ? 36.596  -54.430 -73.323  1.000 147.367 ? 379 CYS EEE CA  1 
ATOM 3678 C C   . CYS C 3 48  ? 35.358  -55.057 -72.682  1.000 145.157 ? 379 CYS EEE C   1 
ATOM 3679 O O   . CYS C 3 48  ? 34.487  -54.298 -72.230  1.000 162.312 ? 379 CYS EEE O   1 
ATOM 3680 C CB  . CYS C 3 48  ? 37.712  -54.048 -72.354  1.000 153.926 ? 379 CYS EEE CB  1 
ATOM 3681 S SG  . CYS C 3 48  ? 39.167  -53.394 -73.224  1.000 164.951 ? 379 CYS EEE SG  1 
ATOM 3682 N N   . TYR C 3 49  ? 35.267  -56.386 -72.756  1.000 141.464 ? 380 TYR EEE N   1 
ATOM 3683 C CA  . TYR C 3 49  ? 34.162  -57.225 -72.232  1.000 148.054 ? 380 TYR EEE CA  1 
ATOM 3684 C C   . TYR C 3 49  ? 34.716  -58.055 -71.063  1.000 146.352 ? 380 TYR EEE C   1 
ATOM 3685 O O   . TYR C 3 49  ? 35.735  -58.725 -71.210  1.000 139.845 ? 380 TYR EEE O   1 
ATOM 3686 C CB  . TYR C 3 49  ? 33.561  -58.060 -73.374  1.000 158.398 ? 380 TYR EEE CB  1 
ATOM 3687 C CG  . TYR C 3 49  ? 33.093  -57.269 -74.584  1.000 166.773 ? 380 TYR EEE CG  1 
ATOM 3688 C CD1 . TYR C 3 49  ? 33.983  -56.763 -75.527  1.000 168.346 ? 380 TYR EEE CD1 1 
ATOM 3689 C CD2 . TYR C 3 49  ? 31.742  -57.040 -74.809  1.000 166.170 ? 380 TYR EEE CD2 1 
ATOM 3690 C CE1 . TYR C 3 49  ? 33.545  -56.014 -76.614  1.000 163.793 ? 380 TYR EEE CE1 1 
ATOM 3691 C CE2 . TYR C 3 49  ? 31.287  -56.329 -75.912  1.000 155.714 ? 380 TYR EEE CE2 1 
ATOM 3692 C CZ  . TYR C 3 49  ? 32.189  -55.796 -76.805  1.000 156.707 ? 380 TYR EEE CZ  1 
ATOM 3693 O OH  . TYR C 3 49  ? 31.698  -55.074 -77.850  1.000 156.916 ? 380 TYR EEE OH  1 
ATOM 3694 N N   . GLY C 3 50  ? 34.077  -58.007 -69.894  1.000 152.599 ? 381 GLY EEE N   1 
ATOM 3695 C CA  . GLY C 3 50  ? 34.391  -58.889 -68.747  1.000 148.575 ? 381 GLY EEE CA  1 
ATOM 3696 C C   . GLY C 3 50  ? 35.757  -58.653 -68.110  1.000 144.161 ? 381 GLY EEE C   1 
ATOM 3697 O O   . GLY C 3 50  ? 36.169  -59.489 -67.346  1.000 147.951 ? 381 GLY EEE O   1 
ATOM 3698 N N   . VAL C 3 51  ? 36.448  -57.553 -68.392  1.000 152.069 ? 382 VAL EEE N   1 
ATOM 3699 C CA  . VAL C 3 51  ? 37.801  -57.260 -67.827  1.000 155.976 ? 382 VAL EEE CA  1 
ATOM 3700 C C   . VAL C 3 51  ? 38.117  -55.780 -68.068  1.000 159.020 ? 382 VAL EEE C   1 
ATOM 3701 O O   . VAL C 3 51  ? 37.727  -55.253 -69.144  1.000 170.717 ? 382 VAL EEE O   1 
ATOM 3702 C CB  . VAL C 3 51  ? 38.868  -58.156 -68.481  1.000 151.065 ? 382 VAL EEE CB  1 
ATOM 3703 C CG1 . VAL C 3 51  ? 39.093  -57.741 -69.918  1.000 156.356 ? 382 VAL EEE CG1 1 
ATOM 3704 C CG2 . VAL C 3 51  ? 40.192  -58.158 -67.727  1.000 148.495 ? 382 VAL EEE CG2 1 
ATOM 3705 N N   . SER C 3 52  ? 38.853  -55.145 -67.162  1.000 142.766 ? 383 SER EEE N   1 
ATOM 3706 C CA  . SER C 3 52  ? 39.159  -53.708 -67.298  1.000 146.376 ? 383 SER EEE CA  1 
ATOM 3707 C C   . SER C 3 52  ? 40.659  -53.497 -67.531  1.000 145.085 ? 383 SER EEE C   1 
ATOM 3708 O O   . SER C 3 52  ? 41.471  -53.939 -66.732  1.000 153.116 ? 383 SER EEE O   1 
ATOM 3709 C CB  . SER C 3 52  ? 38.600  -53.001 -66.111  1.000 151.130 ? 383 SER EEE CB  1 
ATOM 3710 O OG  . SER C 3 52  ? 39.623  -52.636 -65.213  1.000 165.821 ? 383 SER EEE OG  1 
ATOM 3711 N N   . PRO C 3 53  ? 41.090  -52.831 -68.634  1.000 149.966 ? 384 PRO EEE N   1 
ATOM 3712 C CA  . PRO C 3 53  ? 42.511  -52.677 -68.985  1.000 158.107 ? 384 PRO EEE CA  1 
ATOM 3713 C C   . PRO C 3 53  ? 43.418  -52.029 -67.942  1.000 168.084 ? 384 PRO EEE C   1 
ATOM 3714 O O   . PRO C 3 53  ? 44.634  -52.232 -67.952  1.000 174.364 ? 384 PRO EEE O   1 
ATOM 3715 C CB  . PRO C 3 53  ? 42.474  -51.652 -70.119  1.000 158.218 ? 384 PRO EEE CB  1 
ATOM 3716 C CG  . PRO C 3 53  ? 41.200  -52.021 -70.786  1.000 156.142 ? 384 PRO EEE CG  1 
ATOM 3717 C CD  . PRO C 3 53  ? 40.234  -52.187 -69.634  1.000 151.272 ? 384 PRO EEE CD  1 
ATOM 3718 N N   . THR C 3 54  ? 42.777  -51.266 -67.072  1.000 168.229 ? 385 THR EEE N   1 
ATOM 3719 C CA  . THR C 3 54  ? 43.419  -50.486 -65.999  1.000 169.613 ? 385 THR EEE CA  1 
ATOM 3720 C C   . THR C 3 54  ? 43.821  -51.442 -64.858  1.000 176.938 ? 385 THR EEE C   1 
ATOM 3721 O O   . THR C 3 54  ? 44.868  -51.188 -64.234  1.000 194.466 ? 385 THR EEE O   1 
ATOM 3722 C CB  . THR C 3 54  ? 42.480  -49.315 -65.711  1.000 169.108 ? 385 THR EEE CB  1 
ATOM 3723 O OG1 . THR C 3 54  ? 41.235  -49.860 -65.277  1.000 180.541 ? 385 THR EEE OG1 1 
ATOM 3724 C CG2 . THR C 3 54  ? 42.243  -48.476 -66.945  1.000 167.952 ? 385 THR EEE CG2 1 
ATOM 3725 N N   . LYS C 3 55  ? 43.076  -52.532 -64.629  1.000 175.859 ? 386 LYS EEE N   1 
ATOM 3726 C CA  . LYS C 3 55  ? 43.388  -53.550 -63.582  1.000 172.164 ? 386 LYS EEE CA  1 
ATOM 3727 C C   . LYS C 3 55  ? 44.284  -54.672 -64.119  1.000 168.277 ? 386 LYS EEE C   1 
ATOM 3728 O O   . LYS C 3 55  ? 44.746  -55.456 -63.293  1.000 180.762 ? 386 LYS EEE O   1 
ATOM 3729 C CB  . LYS C 3 55  ? 42.116  -54.186 -63.015  1.000 172.294 ? 386 LYS EEE CB  1 
ATOM 3730 C CG  . LYS C 3 55  ? 41.401  -53.354 -61.959  1.000 185.922 ? 386 LYS EEE CG  1 
ATOM 3731 C CD  . LYS C 3 55  ? 39.936  -53.703 -61.827  1.000 192.330 ? 386 LYS EEE CD  1 
ATOM 3732 C CE  . LYS C 3 55  ? 39.137  -52.724 -60.994  1.000 190.613 ? 386 LYS EEE CE  1 
ATOM 3733 N NZ  . LYS C 3 55  ? 37.691  -53.031 -61.099  1.000 187.037 ? 386 LYS EEE NZ  1 
ATOM 3734 N N   . LEU C 3 56  ? 44.513  -54.783 -65.427  1.000 168.622 ? 387 LEU EEE N   1 
ATOM 3735 C CA  . LEU C 3 56  ? 45.322  -55.894 -65.994  1.000 168.620 ? 387 LEU EEE CA  1 
ATOM 3736 C C   . LEU C 3 56  ? 46.768  -55.726 -65.547  1.000 165.164 ? 387 LEU EEE C   1 
ATOM 3737 O O   . LEU C 3 56  ? 47.463  -56.746 -65.471  1.000 172.449 ? 387 LEU EEE O   1 
ATOM 3738 C CB  . LEU C 3 56  ? 45.241  -55.911 -67.522  1.000 165.070 ? 387 LEU EEE CB  1 
ATOM 3739 C CG  . LEU C 3 56  ? 43.907  -56.340 -68.115  1.000 157.811 ? 387 LEU EEE CG  1 
ATOM 3740 C CD1 . LEU C 3 56  ? 43.962  -56.240 -69.620  1.000 162.189 ? 387 LEU EEE CD1 1 
ATOM 3741 C CD2 . LEU C 3 56  ? 43.548  -57.745 -67.704  1.000 150.222 ? 387 LEU EEE CD2 1 
ATOM 3742 N N   . ASN C 3 57  ? 47.173  -54.489 -65.263  1.000 161.643 ? 388 ASN EEE N   1 
ATOM 3743 C CA  . ASN C 3 57  ? 48.570  -54.111 -64.926  1.000 176.682 ? 388 ASN EEE CA  1 
ATOM 3744 C C   . ASN C 3 57  ? 49.049  -54.824 -63.658  1.000 178.473 ? 388 ASN EEE C   1 
ATOM 3745 O O   . ASN C 3 57  ? 50.280  -54.840 -63.441  1.000 184.043 ? 388 ASN EEE O   1 
ATOM 3746 C CB  . ASN C 3 57  ? 48.699  -52.595 -64.774  1.000 193.007 ? 388 ASN EEE CB  1 
ATOM 3747 C CG  . ASN C 3 57  ? 48.749  -51.905 -66.116  1.000 198.715 ? 388 ASN EEE CG  1 
ATOM 3748 O OD1 . ASN C 3 57  ? 49.194  -52.507 -67.086  1.000 192.638 ? 388 ASN EEE OD1 1 
ATOM 3749 N ND2 . ASN C 3 57  ? 48.282  -50.667 -66.177  1.000 209.503 ? 388 ASN EEE ND2 1 
ATOM 3750 N N   . ASP C 3 58  ? 48.139  -55.340 -62.824  1.000 180.364 ? 389 ASP EEE N   1 
ATOM 3751 C CA  . ASP C 3 58  ? 48.508  -56.192 -61.660  1.000 186.439 ? 389 ASP EEE CA  1 
ATOM 3752 C C   . ASP C 3 58  ? 47.620  -57.441 -61.655  1.000 177.759 ? 389 ASP EEE C   1 
ATOM 3753 O O   . ASP C 3 58  ? 47.127  -57.825 -60.574  1.000 176.151 ? 389 ASP EEE O   1 
ATOM 3754 C CB  . ASP C 3 58  ? 48.532  -55.385 -60.357  1.000 210.957 ? 389 ASP EEE CB  1 
ATOM 3755 C CG  . ASP C 3 58  ? 47.186  -54.863 -59.856  1.000 227.611 ? 389 ASP EEE CG  1 
ATOM 3756 O OD1 . ASP C 3 58  ? 46.412  -54.302 -60.664  1.000 213.923 ? 389 ASP EEE OD1 1 
ATOM 3757 O OD2 . ASP C 3 58  ? 46.944  -54.962 -58.626  1.000 263.834 ? 389 ASP EEE OD2 1 
ATOM 3758 N N   . LEU C 3 59  ? 47.465  -58.057 -62.834  1.000 173.910 ? 390 LEU EEE N   1 
ATOM 3759 C CA  . LEU C 3 59  ? 46.863  -59.404 -63.028  1.000 168.161 ? 390 LEU EEE CA  1 
ATOM 3760 C C   . LEU C 3 59  ? 47.786  -60.280 -63.876  1.000 170.982 ? 390 LEU EEE C   1 
ATOM 3761 O O   . LEU C 3 59  ? 48.364  -59.769 -64.879  1.000 179.930 ? 390 LEU EEE O   1 
ATOM 3762 C CB  . LEU C 3 59  ? 45.496  -59.260 -63.694  1.000 161.221 ? 390 LEU EEE CB  1 
ATOM 3763 C CG  . LEU C 3 59  ? 44.402  -58.752 -62.769  1.000 171.344 ? 390 LEU EEE CG  1 
ATOM 3764 C CD1 . LEU C 3 59  ? 43.180  -58.326 -63.575  1.000 166.675 ? 390 LEU EEE CD1 1 
ATOM 3765 C CD2 . LEU C 3 59  ? 44.060  -59.801 -61.708  1.000 176.355 ? 390 LEU EEE CD2 1 
ATOM 3766 N N   . CYS C 3 60  ? 47.870  -61.559 -63.491  1.000 176.081 ? 391 CYS EEE N   1 
ATOM 3767 C CA  . CYS C 3 60  ? 48.600  -62.636 -64.205  1.000 186.929 ? 391 CYS EEE CA  1 
ATOM 3768 C C   . CYS C 3 60  ? 47.616  -63.612 -64.854  1.000 181.355 ? 391 CYS EEE C   1 
ATOM 3769 O O   . CYS C 3 60  ? 46.603  -63.954 -64.214  1.000 180.865 ? 391 CYS EEE O   1 
ATOM 3770 C CB  . CYS C 3 60  ? 49.543  -63.351 -63.252  1.000 202.125 ? 391 CYS EEE CB  1 
ATOM 3771 S SG  . CYS C 3 60  ? 50.938  -62.294 -62.773  1.000 226.589 ? 391 CYS EEE SG  1 
ATOM 3772 N N   . PHE C 3 61  ? 47.917  -64.042 -66.078  1.000 171.680 ? 392 PHE EEE N   1 
ATOM 3773 C CA  . PHE C 3 61  ? 47.091  -65.010 -66.836  1.000 170.403 ? 392 PHE EEE CA  1 
ATOM 3774 C C   . PHE C 3 61  ? 47.974  -66.152 -67.339  1.000 174.331 ? 392 PHE EEE C   1 
ATOM 3775 O O   . PHE C 3 61  ? 49.206  -65.961 -67.408  1.000 179.481 ? 392 PHE EEE O   1 
ATOM 3776 C CB  . PHE C 3 61  ? 46.392  -64.265 -67.963  1.000 161.639 ? 392 PHE EEE CB  1 
ATOM 3777 C CG  . PHE C 3 61  ? 45.439  -63.181 -67.526  1.000 141.341 ? 392 PHE EEE CG  1 
ATOM 3778 C CD1 . PHE C 3 61  ? 44.108  -63.486 -67.277  1.000 129.600 ? 392 PHE EEE CD1 1 
ATOM 3779 C CD2 . PHE C 3 61  ? 45.852  -61.860 -67.454  1.000 129.100 ? 392 PHE EEE CD2 1 
ATOM 3780 C CE1 . PHE C 3 61  ? 43.199  -62.493 -66.950  1.000 120.298 ? 392 PHE EEE CE1 1 
ATOM 3781 C CE2 . PHE C 3 61  ? 44.938  -60.869 -67.134  1.000 123.779 ? 392 PHE EEE CE2 1 
ATOM 3782 C CZ  . PHE C 3 61  ? 43.618  -61.188 -66.881  1.000 119.272 ? 392 PHE EEE CZ  1 
ATOM 3783 N N   . THR C 3 62  ? 47.372  -67.310 -67.612  1.000 172.235 ? 393 THR EEE N   1 
ATOM 3784 C CA  A THR C 3 62  ? 48.125  -68.482 -68.127  0.500 186.946 ? 393 THR EEE CA  1 
ATOM 3785 C CA  B THR C 3 62  ? 48.072  -68.505 -68.143  0.500 188.498 ? 393 THR EEE CA  1 
ATOM 3786 C C   . THR C 3 62  ? 48.441  -68.265 -69.608  1.000 193.485 ? 393 THR EEE C   1 
ATOM 3787 O O   . THR C 3 62  ? 49.593  -68.576 -69.988  1.000 195.295 ? 393 THR EEE O   1 
ATOM 3788 C CB  A THR C 3 62  ? 47.394  -69.806 -67.889  0.500 195.303 ? 393 THR EEE CB  1 
ATOM 3789 C CB  B THR C 3 62  ? 47.189  -69.744 -67.968  0.500 197.746 ? 393 THR EEE CB  1 
ATOM 3790 O OG1 A THR C 3 62  ? 46.036  -69.618 -68.265  0.500 187.595 ? 393 THR EEE OG1 1 
ATOM 3791 O OG1 B THR C 3 62  ? 46.723  -69.686 -66.618  0.500 202.102 ? 393 THR EEE OG1 1 
ATOM 3792 C CG2 A THR C 3 62  ? 47.464  -70.274 -66.453  0.500 204.123 ? 393 THR EEE CG2 1 
ATOM 3793 C CG2 B THR C 3 62  ? 47.911  -71.043 -68.264  0.500 204.055 ? 393 THR EEE CG2 1 
ATOM 3794 N N   . ASN C 3 63  ? 47.472  -67.754 -70.379  1.000 200.972 ? 394 ASN EEE N   1 
ATOM 3795 C CA  . ASN C 3 63  ? 47.636  -67.451 -71.828  1.000 186.593 ? 394 ASN EEE CA  1 
ATOM 3796 C C   . ASN C 3 63  ? 46.749  -66.262 -72.225  1.000 169.242 ? 394 ASN EEE C   1 
ATOM 3797 O O   . ASN C 3 63  ? 45.594  -66.159 -71.781  1.000 149.813 ? 394 ASN EEE O   1 
ATOM 3798 C CB  . ASN C 3 63  ? 47.415  -68.691 -72.698  1.000 188.394 ? 394 ASN EEE CB  1 
ATOM 3799 C CG  . ASN C 3 63  ? 48.592  -69.648 -72.640  1.000 207.402 ? 394 ASN EEE CG  1 
ATOM 3800 O OD1 . ASN C 3 63  ? 49.724  -69.272 -72.958  1.000 230.331 ? 394 ASN EEE OD1 1 
ATOM 3801 N ND2 . ASN C 3 63  ? 48.353  -70.866 -72.179  1.000 202.008 ? 394 ASN EEE ND2 1 
ATOM 3802 N N   . VAL C 3 64  ? 47.325  -65.355 -72.998  1.000 162.956 ? 395 VAL EEE N   1 
ATOM 3803 C CA  . VAL C 3 64  ? 46.611  -64.239 -73.661  1.000 152.971 ? 395 VAL EEE CA  1 
ATOM 3804 C C   . VAL C 3 64  ? 46.754  -64.485 -75.154  1.000 156.404 ? 395 VAL EEE C   1 
ATOM 3805 O O   . VAL C 3 64  ? 47.861  -64.836 -75.585  1.000 162.440 ? 395 VAL EEE O   1 
ATOM 3806 C CB  . VAL C 3 64  ? 47.221  -62.901 -73.237  1.000 152.363 ? 395 VAL EEE CB  1 
ATOM 3807 C CG1 . VAL C 3 64  ? 46.614  -61.726 -73.983  1.000 150.519 ? 395 VAL EEE CG1 1 
ATOM 3808 C CG2 . VAL C 3 64  ? 47.086  -62.746 -71.742  1.000 159.468 ? 395 VAL EEE CG2 1 
ATOM 3809 N N   . TYR C 3 65  ? 45.665  -64.351 -75.899  1.000 158.134 ? 396 TYR EEE N   1 
ATOM 3810 C CA  . TYR C 3 65  ? 45.614  -64.641 -77.349  1.000 142.459 ? 396 TYR EEE CA  1 
ATOM 3811 C C   . TYR C 3 65  ? 45.399  -63.310 -78.062  1.000 136.358 ? 396 TYR EEE C   1 
ATOM 3812 O O   . TYR C 3 65  ? 44.423  -62.625 -77.689  1.000 131.641 ? 396 TYR EEE O   1 
ATOM 3813 C CB  . TYR C 3 65  ? 44.529  -65.688 -77.599  1.000 141.548 ? 396 TYR EEE CB  1 
ATOM 3814 C CG  . TYR C 3 65  ? 44.806  -67.028 -76.954  1.000 150.018 ? 396 TYR EEE CG  1 
ATOM 3815 C CD1 . TYR C 3 65  ? 45.813  -67.863 -77.428  1.000 145.128 ? 396 TYR EEE CD1 1 
ATOM 3816 C CD2 . TYR C 3 65  ? 44.056  -67.482 -75.878  1.000 152.796 ? 396 TYR EEE CD2 1 
ATOM 3817 C CE1 . TYR C 3 65  ? 46.060  -69.108 -76.870  1.000 143.513 ? 396 TYR EEE CE1 1 
ATOM 3818 C CE2 . TYR C 3 65  ? 44.303  -68.723 -75.296  1.000 157.925 ? 396 TYR EEE CE2 1 
ATOM 3819 C CZ  . TYR C 3 65  ? 45.308  -69.546 -75.796  1.000 153.903 ? 396 TYR EEE CZ  1 
ATOM 3820 O OH  . TYR C 3 65  ? 45.612  -70.766 -75.246  1.000 167.007 ? 396 TYR EEE OH  1 
ATOM 3821 N N   . ALA C 3 66  ? 46.291  -62.941 -78.989  1.000 133.742 ? 397 ALA EEE N   1 
ATOM 3822 C CA  . ALA C 3 66  ? 46.122  -61.757 -79.865  1.000 143.792 ? 397 ALA EEE CA  1 
ATOM 3823 C C   . ALA C 3 66  ? 45.718  -62.180 -81.300  1.000 157.116 ? 397 ALA EEE C   1 
ATOM 3824 O O   . ALA C 3 66  ? 46.538  -62.785 -82.039  1.000 167.769 ? 397 ALA EEE O   1 
ATOM 3825 C CB  . ALA C 3 66  ? 47.382  -60.942 -79.819  1.000 143.403 ? 397 ALA EEE CB  1 
ATOM 3826 N N   . ASP C 3 67  ? 44.467  -61.905 -81.677  1.000 150.806 ? 398 ASP EEE N   1 
ATOM 3827 C CA  . ASP C 3 67  ? 43.887  -62.236 -83.000  1.000 141.408 ? 398 ASP EEE CA  1 
ATOM 3828 C C   . ASP C 3 67  ? 43.901  -60.949 -83.825  1.000 140.734 ? 398 ASP EEE C   1 
ATOM 3829 O O   . ASP C 3 67  ? 43.329  -59.949 -83.351  1.000 139.742 ? 398 ASP EEE O   1 
ATOM 3830 C CB  . ASP C 3 67  ? 42.490  -62.829 -82.806  1.000 140.487 ? 398 ASP EEE CB  1 
ATOM 3831 C CG  . ASP C 3 67  ? 42.455  -64.124 -81.989  1.000 140.300 ? 398 ASP EEE CG  1 
ATOM 3832 O OD1 . ASP C 3 67  ? 43.526  -64.791 -81.867  1.000 127.882 ? 398 ASP EEE OD1 1 
ATOM 3833 O OD2 . ASP C 3 67  ? 41.340  -64.479 -81.493  1.000 124.606 ? 398 ASP EEE OD2 1 
ATOM 3834 N N   . SER C 3 68  ? 44.573  -60.937 -84.976  1.000 146.397 ? 399 SER EEE N   1 
ATOM 3835 C CA  . SER C 3 68  ? 44.674  -59.719 -85.825  1.000 159.757 ? 399 SER EEE CA  1 
ATOM 3836 C C   . SER C 3 68  ? 44.243  -60.003 -87.279  1.000 166.296 ? 399 SER EEE C   1 
ATOM 3837 O O   . SER C 3 68  ? 44.463  -61.156 -87.776  1.000 152.096 ? 399 SER EEE O   1 
ATOM 3838 C CB  . SER C 3 68  ? 46.052  -59.134 -85.734  1.000 155.099 ? 399 SER EEE CB  1 
ATOM 3839 O OG  . SER C 3 68  ? 47.022  -60.145 -85.964  1.000 154.343 ? 399 SER EEE OG  1 
ATOM 3840 N N   . PHE C 3 69  ? 43.639  -58.983 -87.917  1.000 168.041 ? 400 PHE EEE N   1 
ATOM 3841 C CA  . PHE C 3 69  ? 43.075  -59.009 -89.295  1.000 161.952 ? 400 PHE EEE CA  1 
ATOM 3842 C C   . PHE C 3 69  ? 42.620  -57.616 -89.780  1.000 153.264 ? 400 PHE EEE C   1 
ATOM 3843 O O   . PHE C 3 69  ? 42.569  -56.679 -88.976  1.000 154.619 ? 400 PHE EEE O   1 
ATOM 3844 C CB  . PHE C 3 69  ? 41.923  -60.013 -89.346  1.000 159.619 ? 400 PHE EEE CB  1 
ATOM 3845 C CG  . PHE C 3 69  ? 40.882  -59.838 -88.278  1.000 150.252 ? 400 PHE EEE CG  1 
ATOM 3846 C CD1 . PHE C 3 69  ? 39.922  -58.842 -88.377  1.000 161.777 ? 400 PHE EEE CD1 1 
ATOM 3847 C CD2 . PHE C 3 69  ? 40.862  -60.674 -87.180  1.000 146.353 ? 400 PHE EEE CD2 1 
ATOM 3848 C CE1 . PHE C 3 69  ? 38.955  -58.684 -87.395  1.000 160.271 ? 400 PHE EEE CE1 1 
ATOM 3849 C CE2 . PHE C 3 69  ? 39.897  -60.515 -86.198  1.000 154.465 ? 400 PHE EEE CE2 1 
ATOM 3850 C CZ  . PHE C 3 69  ? 38.950  -59.517 -86.301  1.000 157.195 ? 400 PHE EEE CZ  1 
ATOM 3851 N N   . VAL C 3 70  ? 42.307  -57.501 -91.080  1.000 163.637 ? 401 VAL EEE N   1 
ATOM 3852 C CA  . VAL C 3 70  ? 41.720  -56.288 -91.735  1.000 172.796 ? 401 VAL EEE CA  1 
ATOM 3853 C C   . VAL C 3 70  ? 40.285  -56.573 -92.232  1.000 164.468 ? 401 VAL EEE C   1 
ATOM 3854 O O   . VAL C 3 70  ? 40.001  -57.644 -92.877  1.000 147.852 ? 401 VAL EEE O   1 
ATOM 3855 C CB  . VAL C 3 70  ? 42.599  -55.722 -92.875  1.000 185.434 ? 401 VAL EEE CB  1 
ATOM 3856 C CG1 . VAL C 3 70  ? 41.920  -54.552 -93.597  1.000 183.325 ? 401 VAL EEE CG1 1 
ATOM 3857 C CG2 . VAL C 3 70  ? 43.984  -55.318 -92.380  1.000 185.134 ? 401 VAL EEE CG2 1 
ATOM 3858 N N   . ILE C 3 71  ? 39.433  -55.592 -91.932  1.000 153.631 ? 402 ILE EEE N   1 
ATOM 3859 C CA  . ILE C 3 71  ? 38.007  -55.454 -92.313  1.000 143.715 ? 402 ILE EEE CA  1 
ATOM 3860 C C   . ILE C 3 71  ? 37.763  -53.961 -92.545  1.000 154.168 ? 402 ILE EEE C   1 
ATOM 3861 O O   . ILE C 3 71  ? 38.645  -53.141 -92.164  1.000 140.880 ? 402 ILE EEE O   1 
ATOM 3862 C CB  . ILE C 3 71  ? 37.129  -56.020 -91.188  1.000 139.065 ? 402 ILE EEE CB  1 
ATOM 3863 C CG1 . ILE C 3 71  ? 37.373  -55.300 -89.847  1.000 144.083 ? 402 ILE EEE CG1 1 
ATOM 3864 C CG2 . ILE C 3 71  ? 37.352  -57.512 -91.078  1.000 129.123 ? 402 ILE EEE CG2 1 
ATOM 3865 C CD1 . ILE C 3 71  ? 36.327  -55.556 -88.758  1.000 139.492 ? 402 ILE EEE CD1 1 
ATOM 3866 N N   . ARG C 3 72  ? 36.625  -53.611 -93.154  1.000 178.785 ? 403 ARG EEE N   1 
ATOM 3867 C CA  . ARG C 3 72  ? 36.265  -52.192 -93.448  1.000 191.085 ? 403 ARG EEE CA  1 
ATOM 3868 C C   . ARG C 3 72  ? 35.561  -51.587 -92.223  1.000 186.414 ? 403 ARG EEE C   1 
ATOM 3869 O O   . ARG C 3 72  ? 35.036  -52.345 -91.400  1.000 181.134 ? 403 ARG EEE O   1 
ATOM 3870 C CB  . ARG C 3 72  ? 35.478  -52.060 -94.761  1.000 191.557 ? 403 ARG EEE CB  1 
ATOM 3871 C CG  . ARG C 3 72  ? 34.079  -52.649 -94.768  1.000 193.022 ? 403 ARG EEE CG  1 
ATOM 3872 C CD  . ARG C 3 72  ? 33.552  -52.622 -96.185  1.000 210.225 ? 403 ARG EEE CD  1 
ATOM 3873 N NE  . ARG C 3 72  ? 32.166  -53.052 -96.282  1.000 227.644 ? 403 ARG EEE NE  1 
ATOM 3874 C CZ  . ARG C 3 72  ? 31.100  -52.275 -96.107  1.000 236.975 ? 403 ARG EEE CZ  1 
ATOM 3875 N NH1 . ARG C 3 72  ? 31.247  -50.992 -95.818  1.000 234.600 ? 403 ARG EEE NH1 1 
ATOM 3876 N NH2 . ARG C 3 72  ? 29.884  -52.783 -96.228  1.000 246.976 ? 403 ARG EEE NH2 1 
ATOM 3877 N N   . GLY C 3 73  ? 35.593  -50.260 -92.101  1.000 178.774 ? 404 GLY EEE N   1 
ATOM 3878 C CA  . GLY C 3 73  ? 35.114  -49.526 -90.918  1.000 166.277 ? 404 GLY EEE CA  1 
ATOM 3879 C C   . GLY C 3 73  ? 33.748  -50.011 -90.469  1.000 167.058 ? 404 GLY EEE C   1 
ATOM 3880 O O   . GLY C 3 73  ? 33.561  -50.204 -89.262  1.000 161.682 ? 404 GLY EEE O   1 
ATOM 3881 N N   . ASP C 3 74  ? 32.827  -50.209 -91.414  1.000 179.756 ? 405 ASP EEE N   1 
ATOM 3882 C CA  . ASP C 3 74  ? 31.383  -50.465 -91.159  1.000 191.531 ? 405 ASP EEE CA  1 
ATOM 3883 C C   . ASP C 3 74  ? 31.205  -51.765 -90.386  1.000 185.966 ? 405 ASP EEE C   1 
ATOM 3884 O O   . ASP C 3 74  ? 30.121  -51.946 -89.793  1.000 183.231 ? 405 ASP EEE O   1 
ATOM 3885 C CB  . ASP C 3 74  ? 30.576  -50.591 -92.457  1.000 205.130 ? 405 ASP EEE CB  1 
ATOM 3886 C CG  . ASP C 3 74  ? 30.118  -49.261 -93.022  1.000 205.565 ? 405 ASP EEE CG  1 
ATOM 3887 O OD1 . ASP C 3 74  ? 30.034  -48.299 -92.241  1.000 222.546 ? 405 ASP EEE OD1 1 
ATOM 3888 O OD2 . ASP C 3 74  ? 29.860  -49.195 -94.228  1.000 186.012 ? 405 ASP EEE OD2 1 
ATOM 3889 N N   . GLU C 3 75  ? 32.207  -52.642 -90.456  1.000 186.795 ? 406 GLU EEE N   1 
ATOM 3890 C CA  . GLU C 3 75  ? 32.133  -54.041 -89.966  1.000 197.563 ? 406 GLU EEE CA  1 
ATOM 3891 C C   . GLU C 3 75  ? 32.823  -54.184 -88.607  1.000 193.164 ? 406 GLU EEE C   1 
ATOM 3892 O O   . GLU C 3 75  ? 32.723  -55.275 -87.998  1.000 184.181 ? 406 GLU EEE O   1 
ATOM 3893 C CB  . GLU C 3 75  ? 32.833  -54.961 -90.958  1.000 201.439 ? 406 GLU EEE CB  1 
ATOM 3894 C CG  . GLU C 3 75  ? 32.235  -54.924 -92.342  1.000 203.803 ? 406 GLU EEE CG  1 
ATOM 3895 C CD  . GLU C 3 75  ? 33.025  -55.750 -93.336  1.000 206.154 ? 406 GLU EEE CD  1 
ATOM 3896 O OE1 . GLU C 3 75  ? 34.260  -55.787 -93.222  1.000 187.019 ? 406 GLU EEE OE1 1 
ATOM 3897 O OE2 . GLU C 3 75  ? 32.400  -56.353 -94.220  1.000 246.780 ? 406 GLU EEE OE2 1 
ATOM 3898 N N   . VAL C 3 76  ? 33.528  -53.144 -88.164  1.000 176.921 ? 407 VAL EEE N   1 
ATOM 3899 C CA  . VAL C 3 76  ? 34.185  -53.151 -86.837  1.000 170.283 ? 407 VAL EEE CA  1 
ATOM 3900 C C   . VAL C 3 76  ? 33.094  -53.464 -85.807  1.000 164.862 ? 407 VAL EEE C   1 
ATOM 3901 O O   . VAL C 3 76  ? 33.366  -54.258 -84.900  1.000 166.285 ? 407 VAL EEE O   1 
ATOM 3902 C CB  . VAL C 3 76  ? 34.923  -51.824 -86.586  1.000 178.352 ? 407 VAL EEE CB  1 
ATOM 3903 C CG1 . VAL C 3 76  ? 35.326  -51.623 -85.127  1.000 178.346 ? 407 VAL EEE CG1 1 
ATOM 3904 C CG2 . VAL C 3 76  ? 36.134  -51.711 -87.498  1.000 178.413 ? 407 VAL EEE CG2 1 
ATOM 3905 N N   . ARG C 3 77  ? 31.875  -52.953 -85.974  1.000 155.418 ? 408 ARG EEE N   1 
ATOM 3906 C CA  . ARG C 3 77  ? 30.829  -53.157 -84.941  1.000 166.365 ? 408 ARG EEE CA  1 
ATOM 3907 C C   . ARG C 3 77  ? 30.355  -54.620 -84.906  1.000 167.976 ? 408 ARG EEE C   1 
ATOM 3908 O O   . ARG C 3 77  ? 29.746  -55.014 -83.894  1.000 187.818 ? 408 ARG EEE O   1 
ATOM 3909 C CB  . ARG C 3 77  ? 29.702  -52.138 -85.101  1.000 176.816 ? 408 ARG EEE CB  1 
ATOM 3910 C CG  . ARG C 3 77  ? 28.870  -52.239 -86.368  1.000 192.247 ? 408 ARG EEE CG  1 
ATOM 3911 C CD  . ARG C 3 77  ? 28.083  -50.941 -86.418  1.000 209.125 ? 408 ARG EEE CD  1 
ATOM 3912 N NE  . ARG C 3 77  ? 27.111  -50.786 -87.495  1.000 229.634 ? 408 ARG EEE NE  1 
ATOM 3913 C CZ  . ARG C 3 77  ? 26.088  -49.920 -87.478  1.000 246.890 ? 408 ARG EEE CZ  1 
ATOM 3914 N NH1 . ARG C 3 77  ? 25.911  -49.111 -86.443  1.000 254.428 ? 408 ARG EEE NH1 1 
ATOM 3915 N NH2 . ARG C 3 77  ? 25.191  -49.921 -88.454  1.000 248.082 ? 408 ARG EEE NH2 1 
ATOM 3916 N N   . GLN C 3 78  ? 30.682  -55.429 -85.910  1.000 171.390 ? 409 GLN EEE N   1 
ATOM 3917 C CA  . GLN C 3 78  ? 30.352  -56.883 -85.921  1.000 172.264 ? 409 GLN EEE CA  1 
ATOM 3918 C C   . GLN C 3 78  ? 31.354  -57.719 -85.112  1.000 151.361 ? 409 GLN EEE C   1 
ATOM 3919 O O   . GLN C 3 78  ? 31.017  -58.887 -84.876  1.000 128.350 ? 409 GLN EEE O   1 
ATOM 3920 C CB  . GLN C 3 78  ? 30.338  -57.435 -87.344  1.000 194.009 ? 409 GLN EEE CB  1 
ATOM 3921 C CG  . GLN C 3 78  ? 29.196  -56.904 -88.187  1.000 194.201 ? 409 GLN EEE CG  1 
ATOM 3922 C CD  . GLN C 3 78  ? 29.187  -57.624 -89.505  1.000 193.103 ? 409 GLN EEE CD  1 
ATOM 3923 O OE1 . GLN C 3 78  ? 29.635  -58.772 -89.629  1.000 189.856 ? 409 GLN EEE OE1 1 
ATOM 3924 N NE2 . GLN C 3 78  ? 28.649  -56.933 -90.492  1.000 202.781 ? 409 GLN EEE NE2 1 
ATOM 3925 N N   . ILE C 3 79  ? 32.526  -57.170 -84.748  1.000 149.422 ? 410 ILE EEE N   1 
ATOM 3926 C CA  . ILE C 3 79  ? 33.550  -57.830 -83.876  1.000 157.945 ? 410 ILE EEE CA  1 
ATOM 3927 C C   . ILE C 3 79  ? 33.174  -57.584 -82.403  1.000 176.551 ? 410 ILE EEE C   1 
ATOM 3928 O O   . ILE C 3 79  ? 33.858  -56.833 -81.676  1.000 172.624 ? 410 ILE EEE O   1 
ATOM 3929 C CB  . ILE C 3 79  ? 34.977  -57.355 -84.212  1.000 160.001 ? 410 ILE EEE CB  1 
ATOM 3930 C CG1 . ILE C 3 79  ? 35.297  -57.589 -85.686  1.000 169.896 ? 410 ILE EEE CG1 1 
ATOM 3931 C CG2 . ILE C 3 79  ? 36.019  -58.014 -83.315  1.000 166.178 ? 410 ILE EEE CG2 1 
ATOM 3932 C CD1 . ILE C 3 79  ? 35.152  -59.027 -86.105  1.000 171.215 ? 410 ILE EEE CD1 1 
ATOM 3933 N N   . ALA C 3 80  ? 32.089  -58.218 -81.981  1.000 183.328 ? 411 ALA EEE N   1 
ATOM 3934 C CA  . ALA C 3 80  ? 31.512  -58.112 -80.633  1.000 168.919 ? 411 ALA EEE CA  1 
ATOM 3935 C C   . ALA C 3 80  ? 30.725  -59.391 -80.389  1.000 158.644 ? 411 ALA EEE C   1 
ATOM 3936 O O   . ALA C 3 80  ? 30.216  -60.020 -81.301  1.000 159.380 ? 411 ALA EEE O   1 
ATOM 3937 C CB  . ALA C 3 80  ? 30.659  -56.868 -80.536  1.000 171.339 ? 411 ALA EEE CB  1 
ATOM 3938 N N   . PRO C 3 81  ? 30.595  -59.822 -79.137  1.000 155.037 ? 412 PRO EEE N   1 
ATOM 3939 C CA  . PRO C 3 81  ? 29.747  -60.962 -78.834  1.000 152.768 ? 412 PRO EEE CA  1 
ATOM 3940 C C   . PRO C 3 81  ? 28.298  -60.688 -79.261  1.000 152.306 ? 412 PRO EEE C   1 
ATOM 3941 O O   . PRO C 3 81  ? 27.771  -59.637 -78.927  1.000 157.990 ? 412 PRO EEE O   1 
ATOM 3942 C CB  . PRO C 3 81  ? 29.806  -61.053 -77.312  1.000 160.716 ? 412 PRO EEE CB  1 
ATOM 3943 C CG  . PRO C 3 81  ? 31.003  -60.231 -76.902  1.000 159.921 ? 412 PRO EEE CG  1 
ATOM 3944 C CD  . PRO C 3 81  ? 31.229  -59.204 -77.973  1.000 157.821 ? 412 PRO EEE CD  1 
ATOM 3945 N N   . GLY C 3 82  ? 27.666  -61.647 -79.936  1.000 155.005 ? 413 GLY EEE N   1 
ATOM 3946 C CA  . GLY C 3 82  ? 26.211  -61.616 -80.189  1.000 166.254 ? 413 GLY EEE CA  1 
ATOM 3947 C C   . GLY C 3 82  ? 25.864  -60.751 -81.387  1.000 164.166 ? 413 GLY EEE C   1 
ATOM 3948 O O   . GLY C 3 82  ? 24.670  -60.490 -81.647  1.000 153.746 ? 413 GLY EEE O   1 
ATOM 3949 N N   . GLN C 3 83  ? 26.883  -60.333 -82.122  1.000 168.194 ? 414 GLN EEE N   1 
ATOM 3950 C CA  . GLN C 3 83  ? 26.698  -59.655 -83.418  1.000 176.116 ? 414 GLN EEE CA  1 
ATOM 3951 C C   . GLN C 3 83  ? 26.364  -60.706 -84.474  1.000 182.517 ? 414 GLN EEE C   1 
ATOM 3952 O O   . GLN C 3 83  ? 26.766  -61.893 -84.302  1.000 156.955 ? 414 GLN EEE O   1 
ATOM 3953 C CB  . GLN C 3 83  ? 27.960  -58.882 -83.776  1.000 176.010 ? 414 GLN EEE CB  1 
ATOM 3954 C CG  . GLN C 3 83  ? 28.063  -57.588 -83.001  1.000 179.874 ? 414 GLN EEE CG  1 
ATOM 3955 C CD  . GLN C 3 83  ? 26.927  -56.676 -83.380  1.000 195.437 ? 414 GLN EEE CD  1 
ATOM 3956 O OE1 . GLN C 3 83  ? 26.679  -56.444 -84.568  1.000 220.177 ? 414 GLN EEE OE1 1 
ATOM 3957 N NE2 . GLN C 3 83  ? 26.215  -56.192 -82.371  1.000 190.937 ? 414 GLN EEE NE2 1 
ATOM 3958 N N   . THR C 3 84  ? 25.668  -60.255 -85.524  1.000 192.953 ? 415 THR EEE N   1 
ATOM 3959 C CA  . THR C 3 84  ? 25.429  -61.006 -86.782  1.000 192.613 ? 415 THR EEE CA  1 
ATOM 3960 C C   . THR C 3 84  ? 25.863  -60.130 -87.969  1.000 194.455 ? 415 THR EEE C   1 
ATOM 3961 O O   . THR C 3 84  ? 26.095  -58.902 -87.777  1.000 193.381 ? 415 THR EEE O   1 
ATOM 3962 C CB  . THR C 3 84  ? 23.987  -61.531 -86.820  1.000 186.834 ? 415 THR EEE CB  1 
ATOM 3963 O OG1 . THR C 3 84  ? 23.092  -60.424 -86.890  1.000 191.635 ? 415 THR EEE OG1 1 
ATOM 3964 C CG2 . THR C 3 84  ? 23.642  -62.376 -85.612  1.000 178.188 ? 415 THR EEE CG2 1 
ATOM 3965 N N   . GLY C 3 85  ? 25.998  -60.761 -89.138  1.000 197.018 ? 416 GLY EEE N   1 
ATOM 3966 C CA  . GLY C 3 85  ? 26.572  -60.180 -90.367  1.000 206.118 ? 416 GLY EEE CA  1 
ATOM 3967 C C   . GLY C 3 85  ? 27.658  -61.082 -90.929  1.000 205.775 ? 416 GLY EEE C   1 
ATOM 3968 O O   . GLY C 3 85  ? 27.972  -62.080 -90.251  1.000 189.718 ? 416 GLY EEE O   1 
ATOM 3969 N N   . LYS C 3 86  ? 28.202  -60.741 -92.109  1.000 212.508 ? 417 LYS EEE N   1 
ATOM 3970 C CA  . LYS C 3 86  ? 29.176  -61.563 -92.889  1.000 211.787 ? 417 LYS EEE CA  1 
ATOM 3971 C C   . LYS C 3 86  ? 30.396  -61.880 -92.018  1.000 194.223 ? 417 LYS EEE C   1 
ATOM 3972 O O   . LYS C 3 86  ? 30.841  -63.052 -92.014  1.000 162.384 ? 417 LYS EEE O   1 
ATOM 3973 C CB  . LYS C 3 86  ? 29.582  -60.870 -94.205  1.000 221.580 ? 417 LYS EEE CB  1 
ATOM 3974 C CG  . LYS C 3 86  ? 29.051  -61.536 -95.477  1.000 228.242 ? 417 LYS EEE CG  1 
ATOM 3975 C CD  . LYS C 3 86  ? 28.590  -60.603 -96.580  1.000 236.634 ? 417 LYS EEE CD  1 
ATOM 3976 C CE  . LYS C 3 86  ? 27.293  -61.075 -97.214  1.000 251.456 ? 417 LYS EEE CE  1 
ATOM 3977 N NZ  . LYS C 3 86  ? 26.926  -60.310 -98.431  1.000 263.629 ? 417 LYS EEE NZ  1 
ATOM 3978 N N   . ILE C 3 87  ? 30.910  -60.881 -91.305  1.000 193.941 ? 418 ILE EEE N   1 
ATOM 3979 C CA  . ILE C 3 87  ? 32.202  -61.015 -90.581  1.000 187.192 ? 418 ILE EEE CA  1 
ATOM 3980 C C   . ILE C 3 87  ? 31.958  -61.905 -89.373  1.000 189.532 ? 418 ILE EEE C   1 
ATOM 3981 O O   . ILE C 3 87  ? 32.626  -62.947 -89.287  1.000 195.961 ? 418 ILE EEE O   1 
ATOM 3982 C CB  . ILE C 3 87  ? 32.773  -59.643 -90.210  1.000 185.517 ? 418 ILE EEE CB  1 
ATOM 3983 C CG1 . ILE C 3 87  ? 33.039  -58.810 -91.470  1.000 208.342 ? 418 ILE EEE CG1 1 
ATOM 3984 C CG2 . ILE C 3 87  ? 34.023  -59.815 -89.373  1.000 179.231 ? 418 ILE EEE CG2 1 
ATOM 3985 C CD1 . ILE C 3 87  ? 33.802  -59.535 -92.576  1.000 205.890 ? 418 ILE EEE CD1 1 
ATOM 3986 N N   . ALA C 3 88  ? 30.998  -61.521 -88.527  1.000 193.692 ? 419 ALA EEE N   1 
ATOM 3987 C CA  . ALA C 3 88  ? 30.573  -62.276 -87.324  1.000 193.448 ? 419 ALA EEE CA  1 
ATOM 3988 C C   . ALA C 3 88  ? 30.240  -63.730 -87.693  1.000 188.123 ? 419 ALA EEE C   1 
ATOM 3989 O O   . ALA C 3 88  ? 30.735  -64.644 -87.006  1.000 175.224 ? 419 ALA EEE O   1 
ATOM 3990 C CB  . ALA C 3 88  ? 29.393  -61.583 -86.683  1.000 198.229 ? 419 ALA EEE CB  1 
ATOM 3991 N N   . ASP C 3 89  ? 29.434  -63.941 -88.736  1.000 192.148 ? 420 ASP EEE N   1 
ATOM 3992 C CA  . ASP C 3 89  ? 28.825  -65.267 -89.032  1.000 202.042 ? 420 ASP EEE CA  1 
ATOM 3993 C C   . ASP C 3 89  ? 29.815  -66.172 -89.781  1.000 198.437 ? 420 ASP EEE C   1 
ATOM 3994 O O   . ASP C 3 89  ? 29.823  -67.377 -89.465  1.000 182.424 ? 420 ASP EEE O   1 
ATOM 3995 C CB  . ASP C 3 89  ? 27.514  -65.121 -89.811  1.000 216.855 ? 420 ASP EEE CB  1 
ATOM 3996 C CG  . ASP C 3 89  ? 26.388  -64.471 -89.019  1.000 214.307 ? 420 ASP EEE CG  1 
ATOM 3997 O OD1 . ASP C 3 89  ? 26.472  -64.468 -87.788  1.000 207.583 ? 420 ASP EEE OD1 1 
ATOM 3998 O OD2 . ASP C 3 89  ? 25.419  -63.998 -89.649  1.000 233.910 ? 420 ASP EEE OD2 1 
ATOM 3999 N N   . TYR C 3 90  ? 30.603  -65.633 -90.727  1.000 199.632 ? 421 TYR EEE N   1 
ATOM 4000 C CA  . TYR C 3 90  ? 31.362  -66.443 -91.723  1.000 202.822 ? 421 TYR EEE CA  1 
ATOM 4001 C C   . TYR C 3 90  ? 32.889  -66.248 -91.624  1.000 192.459 ? 421 TYR EEE C   1 
ATOM 4002 O O   . TYR C 3 90  ? 33.592  -67.013 -92.298  1.000 198.024 ? 421 TYR EEE O   1 
ATOM 4003 C CB  . TYR C 3 90  ? 30.934  -66.123 -93.164  1.000 215.454 ? 421 TYR EEE CB  1 
ATOM 4004 C CG  . TYR C 3 90  ? 29.512  -66.425 -93.592  1.000 210.647 ? 421 TYR EEE CG  1 
ATOM 4005 C CD1 . TYR C 3 90  ? 28.647  -67.202 -92.836  1.000 204.943 ? 421 TYR EEE CD1 1 
ATOM 4006 C CD2 . TYR C 3 90  ? 29.043  -65.966 -94.818  1.000 205.811 ? 421 TYR EEE CD2 1 
ATOM 4007 C CE1 . TYR C 3 90  ? 27.354  -67.470 -93.264  1.000 201.644 ? 421 TYR EEE CE1 1 
ATOM 4008 C CE2 . TYR C 3 90  ? 27.755  -66.224 -95.258  1.000 199.458 ? 421 TYR EEE CE2 1 
ATOM 4009 C CZ  . TYR C 3 90  ? 26.909  -66.987 -94.481  1.000 193.456 ? 421 TYR EEE CZ  1 
ATOM 4010 O OH  . TYR C 3 90  ? 25.645  -67.248 -94.907  1.000 196.599 ? 421 TYR EEE OH  1 
ATOM 4011 N N   . ASN C 3 91  ? 33.415  -65.297 -90.847  1.000 182.985 ? 422 ASN EEE N   1 
ATOM 4012 C CA  . ASN C 3 91  ? 34.875  -64.989 -90.871  1.000 183.664 ? 422 ASN EEE CA  1 
ATOM 4013 C C   . ASN C 3 91  ? 35.541  -65.102 -89.488  1.000 184.261 ? 422 ASN EEE C   1 
ATOM 4014 O O   . ASN C 3 91  ? 36.562  -65.841 -89.395  1.000 170.019 ? 422 ASN EEE O   1 
ATOM 4015 C CB  . ASN C 3 91  ? 35.111  -63.605 -91.460  1.000 182.209 ? 422 ASN EEE CB  1 
ATOM 4016 C CG  . ASN C 3 91  ? 34.844  -63.609 -92.937  1.000 173.667 ? 422 ASN EEE CG  1 
ATOM 4017 O OD1 . ASN C 3 91  ? 35.767  -63.815 -93.716  1.000 162.467 ? 422 ASN EEE OD1 1 
ATOM 4018 N ND2 . ASN C 3 91  ? 33.587  -63.435 -93.307  1.000 172.173 ? 422 ASN EEE ND2 1 
ATOM 4019 N N   . TYR C 3 92  ? 35.035  -64.364 -88.483  1.000 179.457 ? 423 TYR EEE N   1 
ATOM 4020 C CA  . TYR C 3 92  ? 35.544  -64.360 -87.084  1.000 166.430 ? 423 TYR EEE CA  1 
ATOM 4021 C C   . TYR C 3 92  ? 34.418  -64.116 -86.078  1.000 161.058 ? 423 TYR EEE C   1 
ATOM 4022 O O   . TYR C 3 92  ? 33.764  -63.056 -86.101  1.000 143.400 ? 423 TYR EEE O   1 
ATOM 4023 C CB  . TYR C 3 92  ? 36.617  -63.300 -86.914  1.000 164.919 ? 423 TYR EEE CB  1 
ATOM 4024 C CG  . TYR C 3 92  ? 37.293  -63.284 -85.570  1.000 162.698 ? 423 TYR EEE CG  1 
ATOM 4025 C CD1 . TYR C 3 92  ? 38.389  -64.091 -85.321  1.000 150.575 ? 423 TYR EEE CD1 1 
ATOM 4026 C CD2 . TYR C 3 92  ? 36.875  -62.411 -84.577  1.000 154.385 ? 423 TYR EEE CD2 1 
ATOM 4027 C CE1 . TYR C 3 92  ? 39.058  -64.030 -84.114  1.000 144.004 ? 423 TYR EEE CE1 1 
ATOM 4028 C CE2 . TYR C 3 92  ? 37.536  -62.331 -83.365  1.000 149.590 ? 423 TYR EEE CE2 1 
ATOM 4029 C CZ  . TYR C 3 92  ? 38.634  -63.144 -83.134  1.000 151.100 ? 423 TYR EEE CZ  1 
ATOM 4030 O OH  . TYR C 3 92  ? 39.280  -63.102 -81.927  1.000 138.508 ? 423 TYR EEE OH  1 
ATOM 4031 N N   . LYS C 3 93  ? 34.245  -65.094 -85.187  1.000 170.736 ? 424 LYS EEE N   1 
ATOM 4032 C CA  . LYS C 3 93  ? 33.059  -65.249 -84.310  1.000 170.560 ? 424 LYS EEE CA  1 
ATOM 4033 C C   . LYS C 3 93  ? 33.526  -65.248 -82.855  1.000 164.979 ? 424 LYS EEE C   1 
ATOM 4034 O O   . LYS C 3 93  ? 34.257  -66.185 -82.477  1.000 151.235 ? 424 LYS EEE O   1 
ATOM 4035 C CB  . LYS C 3 93  ? 32.317  -66.550 -84.638  1.000 171.376 ? 424 LYS EEE CB  1 
ATOM 4036 C CG  . LYS C 3 93  ? 31.030  -66.785 -83.858  1.000 177.818 ? 424 LYS EEE CG  1 
ATOM 4037 C CD  . LYS C 3 93  ? 30.117  -65.570 -83.849  1.000 179.119 ? 424 LYS EEE CD  1 
ATOM 4038 C CE  . LYS C 3 93  ? 28.664  -65.877 -83.549  1.000 171.654 ? 424 LYS EEE CE  1 
ATOM 4039 N NZ  . LYS C 3 93  ? 27.849  -64.641 -83.616  1.000 165.391 ? 424 LYS EEE NZ  1 
ATOM 4040 N N   . LEU C 3 94  ? 33.149  -64.208 -82.103  1.000 156.140 ? 425 LEU EEE N   1 
ATOM 4041 C CA  . LEU C 3 94  ? 33.363  -64.105 -80.639  1.000 146.769 ? 425 LEU EEE CA  1 
ATOM 4042 C C   . LEU C 3 94  ? 32.299  -64.981 -79.977  1.000 152.387 ? 425 LEU EEE C   1 
ATOM 4043 O O   . LEU C 3 94  ? 31.181  -65.117 -80.474  1.000 153.187 ? 425 LEU EEE O   1 
ATOM 4044 C CB  . LEU C 3 94  ? 33.290  -62.632 -80.186  1.000 135.512 ? 425 LEU EEE CB  1 
ATOM 4045 C CG  . LEU C 3 94  ? 34.436  -61.713 -80.633  1.000 128.593 ? 425 LEU EEE CG  1 
ATOM 4046 C CD1 . LEU C 3 94  ? 34.338  -60.329 -80.011  1.000 117.014 ? 425 LEU EEE CD1 1 
ATOM 4047 C CD2 . LEU C 3 94  ? 35.816  -62.313 -80.361  1.000 127.681 ? 425 LEU EEE CD2 1 
ATOM 4048 N N   . PRO C 3 95  ? 32.606  -65.629 -78.836  1.000 150.657 ? 426 PRO EEE N   1 
ATOM 4049 C CA  . PRO C 3 95  ? 31.566  -66.272 -78.033  1.000 149.508 ? 426 PRO EEE CA  1 
ATOM 4050 C C   . PRO C 3 95  ? 30.764  -65.220 -77.248  1.000 158.249 ? 426 PRO EEE C   1 
ATOM 4051 O O   . PRO C 3 95  ? 31.291  -64.139 -77.021  1.000 152.463 ? 426 PRO EEE O   1 
ATOM 4052 C CB  . PRO C 3 95  ? 32.365  -67.173 -77.093  1.000 151.609 ? 426 PRO EEE CB  1 
ATOM 4053 C CG  . PRO C 3 95  ? 33.687  -66.438 -76.941  1.000 150.424 ? 426 PRO EEE CG  1 
ATOM 4054 C CD  . PRO C 3 95  ? 33.956  -65.774 -78.275  1.000 142.975 ? 426 PRO EEE CD  1 
ATOM 4055 N N   . ASP C 3 96  ? 29.517  -65.551 -76.883  1.000 171.020 ? 427 ASP EEE N   1 
ATOM 4056 C CA  . ASP C 3 96  ? 28.575  -64.692 -76.108  1.000 173.527 ? 427 ASP EEE CA  1 
ATOM 4057 C C   . ASP C 3 96  ? 29.270  -64.151 -74.846  1.000 178.240 ? 427 ASP EEE C   1 
ATOM 4058 O O   . ASP C 3 96  ? 29.081  -62.954 -74.538  1.000 185.982 ? 427 ASP EEE O   1 
ATOM 4059 C CB  . ASP C 3 96  ? 27.293  -65.452 -75.736  1.000 178.205 ? 427 ASP EEE CB  1 
ATOM 4060 C CG  . ASP C 3 96  ? 26.204  -65.474 -76.799  1.000 180.314 ? 427 ASP EEE CG  1 
ATOM 4061 O OD1 . ASP C 3 96  ? 26.110  -64.494 -77.568  1.000 187.801 ? 427 ASP EEE OD1 1 
ATOM 4062 O OD2 . ASP C 3 96  ? 25.433  -66.463 -76.831  1.000 189.674 ? 427 ASP EEE OD2 1 
ATOM 4063 N N   . ASP C 3 97  ? 30.040  -64.991 -74.146  1.000 177.587 ? 428 ASP EEE N   1 
ATOM 4064 C CA  . ASP C 3 97  ? 30.565  -64.714 -72.780  1.000 180.580 ? 428 ASP EEE CA  1 
ATOM 4065 C C   . ASP C 3 97  ? 32.016  -64.253 -72.890  1.000 159.882 ? 428 ASP EEE C   1 
ATOM 4066 O O   . ASP C 3 97  ? 32.754  -64.378 -71.907  1.000 152.792 ? 428 ASP EEE O   1 
ATOM 4067 C CB  . ASP C 3 97  ? 30.439  -65.953 -71.891  1.000 195.572 ? 428 ASP EEE CB  1 
ATOM 4068 C CG  . ASP C 3 97  ? 31.256  -67.137 -72.385  1.000 199.275 ? 428 ASP EEE CG  1 
ATOM 4069 O OD1 . ASP C 3 97  ? 31.553  -67.196 -73.609  1.000 185.707 ? 428 ASP EEE OD1 1 
ATOM 4070 O OD2 . ASP C 3 97  ? 31.590  -67.985 -71.545  1.000 207.898 ? 428 ASP EEE OD2 1 
ATOM 4071 N N   . PHE C 3 98  ? 32.395  -63.780 -74.072  1.000 153.006 ? 429 PHE EEE N   1 
ATOM 4072 C CA  . PHE C 3 98  ? 33.756  -63.294 -74.394  1.000 153.300 ? 429 PHE EEE CA  1 
ATOM 4073 C C   . PHE C 3 98  ? 34.250  -62.429 -73.234  1.000 149.003 ? 429 PHE EEE C   1 
ATOM 4074 O O   . PHE C 3 98  ? 33.479  -61.578 -72.721  1.000 138.429 ? 429 PHE EEE O   1 
ATOM 4075 C CB  . PHE C 3 98  ? 33.751  -62.526 -75.724  1.000 145.889 ? 429 PHE EEE CB  1 
ATOM 4076 C CG  . PHE C 3 98  ? 35.007  -61.754 -76.059  1.000 134.808 ? 429 PHE EEE CG  1 
ATOM 4077 C CD1 . PHE C 3 98  ? 36.160  -62.432 -76.422  1.000 132.688 ? 429 PHE EEE CD1 1 
ATOM 4078 C CD2 . PHE C 3 98  ? 35.030  -60.360 -76.052  1.000 124.236 ? 429 PHE EEE CD2 1 
ATOM 4079 C CE1 . PHE C 3 98  ? 37.315  -61.737 -76.741  1.000 136.074 ? 429 PHE EEE CE1 1 
ATOM 4080 C CE2 . PHE C 3 98  ? 36.182  -59.658 -76.372  1.000 121.100 ? 429 PHE EEE CE2 1 
ATOM 4081 C CZ  . PHE C 3 98  ? 37.316  -60.352 -76.736  1.000 134.341 ? 429 PHE EEE CZ  1 
ATOM 4082 N N   . THR C 3 99  ? 35.488  -62.695 -72.825  1.000 148.872 ? 430 THR EEE N   1 
ATOM 4083 C CA  A THR C 3 99  ? 36.281  -61.840 -71.909  0.500 159.038 ? 430 THR EEE CA  1 
ATOM 4084 C CA  B THR C 3 99  ? 36.269  -61.810 -71.919  0.500 150.375 ? 430 THR EEE CA  1 
ATOM 4085 C C   . THR C 3 99  ? 37.549  -61.370 -72.632  1.000 154.492 ? 430 THR EEE C   1 
ATOM 4086 O O   . THR C 3 99  ? 38.422  -62.217 -72.835  1.000 177.309 ? 430 THR EEE O   1 
ATOM 4087 C CB  A THR C 3 99  ? 36.652  -62.622 -70.644  0.500 168.195 ? 430 THR EEE CB  1 
ATOM 4088 C CB  B THR C 3 99  ? 36.605  -62.488 -70.585  0.500 149.843 ? 430 THR EEE CB  1 
ATOM 4089 O OG1 A THR C 3 99  ? 35.470  -63.229 -70.114  0.500 174.652 ? 430 THR EEE OG1 1 
ATOM 4090 O OG1 B THR C 3 99  ? 37.899  -63.091 -70.643  0.500 134.239 ? 430 THR EEE OG1 1 
ATOM 4091 C CG2 A THR C 3 99  ? 37.314  -61.746 -69.605  0.500 173.454 ? 430 THR EEE CG2 1 
ATOM 4092 C CG2 B THR C 3 99  ? 35.574  -63.522 -70.197  0.500 150.854 ? 430 THR EEE CG2 1 
ATOM 4093 N N   . GLY C 3 100 ? 37.642  -60.089 -72.989  1.000 145.167 ? 431 GLY EEE N   1 
ATOM 4094 C CA  . GLY C 3 100 ? 38.811  -59.558 -73.719  1.000 139.020 ? 431 GLY EEE CA  1 
ATOM 4095 C C   . GLY C 3 100 ? 38.571  -58.164 -74.267  1.000 136.927 ? 431 GLY EEE C   1 
ATOM 4096 O O   . GLY C 3 100 ? 37.509  -57.573 -73.981  1.000 145.631 ? 431 GLY EEE O   1 
ATOM 4097 N N   . CYS C 3 101 ? 39.525  -57.646 -75.030  1.000 136.204 ? 432 CYS EEE N   1 
ATOM 4098 C CA  . CYS C 3 101 ? 39.414  -56.310 -75.657  1.000 151.156 ? 432 CYS EEE CA  1 
ATOM 4099 C C   . CYS C 3 101 ? 39.392  -56.408 -77.185  1.000 154.085 ? 432 CYS EEE C   1 
ATOM 4100 O O   . CYS C 3 101 ? 40.138  -57.242 -77.738  1.000 153.935 ? 432 CYS EEE O   1 
ATOM 4101 C CB  . CYS C 3 101 ? 40.551  -55.402 -75.218  1.000 156.980 ? 432 CYS EEE CB  1 
ATOM 4102 S SG  . CYS C 3 101 ? 40.477  -54.959 -73.468  1.000 155.318 ? 432 CYS EEE SG  1 
ATOM 4103 N N   . VAL C 3 102 ? 38.562  -55.554 -77.792  1.000 149.574 ? 433 VAL EEE N   1 
ATOM 4104 C CA  . VAL C 3 102 ? 38.386  -55.338 -79.253  1.000 155.296 ? 433 VAL EEE CA  1 
ATOM 4105 C C   . VAL C 3 102 ? 38.982  -53.969 -79.570  1.000 155.894 ? 433 VAL EEE C   1 
ATOM 4106 O O   . VAL C 3 102 ? 38.392  -52.972 -79.137  1.000 170.526 ? 433 VAL EEE O   1 
ATOM 4107 C CB  . VAL C 3 102 ? 36.888  -55.398 -79.612  1.000 156.868 ? 433 VAL EEE CB  1 
ATOM 4108 C CG1 . VAL C 3 102 ? 36.634  -55.056 -81.062  1.000 154.817 ? 433 VAL EEE CG1 1 
ATOM 4109 C CG2 . VAL C 3 102 ? 36.271  -56.744 -79.268  1.000 160.925 ? 433 VAL EEE CG2 1 
ATOM 4110 N N   . ILE C 3 103 ? 40.118  -53.931 -80.254  1.000 148.893 ? 434 ILE EEE N   1 
ATOM 4111 C CA  . ILE C 3 103 ? 40.885  -52.680 -80.494  1.000 151.480 ? 434 ILE EEE CA  1 
ATOM 4112 C C   . ILE C 3 103 ? 41.068  -52.559 -81.994  1.000 162.452 ? 434 ILE EEE C   1 
ATOM 4113 O O   . ILE C 3 103 ? 41.558  -53.524 -82.611  1.000 164.029 ? 434 ILE EEE O   1 
ATOM 4114 C CB  . ILE C 3 103 ? 42.247  -52.718 -79.787  1.000 158.742 ? 434 ILE EEE CB  1 
ATOM 4115 C CG1 . ILE C 3 103 ? 42.116  -53.057 -78.301  1.000 165.281 ? 434 ILE EEE CG1 1 
ATOM 4116 C CG2 . ILE C 3 103 ? 42.994  -51.411 -80.000  1.000 151.852 ? 434 ILE EEE CG2 1 
ATOM 4117 C CD1 . ILE C 3 103 ? 43.366  -53.648 -77.683  1.000 157.862 ? 434 ILE EEE CD1 1 
ATOM 4118 N N   . ALA C 3 104 ? 40.705  -51.414 -82.552  1.000 175.160 ? 435 ALA EEE N   1 
ATOM 4119 C CA  . ALA C 3 104 ? 40.736  -51.197 -84.013  1.000 181.828 ? 435 ALA EEE CA  1 
ATOM 4120 C C   . ALA C 3 104 ? 41.225  -49.780 -84.326  1.000 181.951 ? 435 ALA EEE C   1 
ATOM 4121 O O   . ALA C 3 104 ? 41.019  -48.856 -83.484  1.000 182.205 ? 435 ALA EEE O   1 
ATOM 4122 C CB  . ALA C 3 104 ? 39.369  -51.467 -84.591  1.000 181.757 ? 435 ALA EEE CB  1 
ATOM 4123 N N   . TRP C 3 105 ? 41.848  -49.621 -85.499  1.000 172.808 ? 436 TRP EEE N   1 
ATOM 4124 C CA  . TRP C 3 105 ? 42.227  -48.293 -86.036  1.000 166.783 ? 436 TRP EEE CA  1 
ATOM 4125 C C   . TRP C 3 105 ? 42.170  -48.259 -87.562  1.000 172.580 ? 436 TRP EEE C   1 
ATOM 4126 O O   . TRP C 3 105 ? 42.372  -49.318 -88.198  1.000 157.993 ? 436 TRP EEE O   1 
ATOM 4127 C CB  . TRP C 3 105 ? 43.603  -47.909 -85.537  1.000 153.803 ? 436 TRP EEE CB  1 
ATOM 4128 C CG  . TRP C 3 105 ? 44.695  -48.822 -85.980  1.000 140.380 ? 436 TRP EEE CG  1 
ATOM 4129 C CD1 . TRP C 3 105 ? 45.635  -48.553 -86.924  1.000 146.987 ? 436 TRP EEE CD1 1 
ATOM 4130 C CD2 . TRP C 3 105 ? 45.042  -50.094 -85.418  1.000 134.927 ? 436 TRP EEE CD2 1 
ATOM 4131 N NE1 . TRP C 3 105 ? 46.541  -49.575 -86.998  1.000 150.745 ? 436 TRP EEE NE1 1 
ATOM 4132 C CE2 . TRP C 3 105 ? 46.200  -50.536 -86.088  1.000 143.259 ? 436 TRP EEE CE2 1 
ATOM 4133 C CE3 . TRP C 3 105 ? 44.502  -50.891 -84.408  1.000 134.669 ? 436 TRP EEE CE3 1 
ATOM 4134 C CZ2 . TRP C 3 105 ? 46.809  -51.753 -85.799  1.000 144.994 ? 436 TRP EEE CZ2 1 
ATOM 4135 C CZ3 . TRP C 3 105 ? 45.106  -52.092 -84.113  1.000 142.063 ? 436 TRP EEE CZ3 1 
ATOM 4136 C CH2 . TRP C 3 105 ? 46.245  -52.512 -84.800  1.000 147.796 ? 436 TRP EEE CH2 1 
ATOM 4137 N N   . ASN C 3 106 ? 41.887  -47.059 -88.082  1.000 173.585 ? 437 ASN EEE N   1 
ATOM 4138 C CA  . ASN C 3 106 ? 41.815  -46.728 -89.526  1.000 171.180 ? 437 ASN EEE CA  1 
ATOM 4139 C C   . ASN C 3 106 ? 43.214  -46.960 -90.079  1.000 167.476 ? 437 ASN EEE C   1 
ATOM 4140 O O   . ASN C 3 106 ? 44.152  -46.400 -89.494  1.000 161.877 ? 437 ASN EEE O   1 
ATOM 4141 C CB  . ASN C 3 106 ? 41.327  -45.289 -89.724  1.000 182.145 ? 437 ASN EEE CB  1 
ATOM 4142 C CG  . ASN C 3 106 ? 41.014  -44.924 -91.164  1.000 186.126 ? 437 ASN EEE CG  1 
ATOM 4143 O OD1 . ASN C 3 106 ? 41.889  -44.937 -92.027  1.000 180.412 ? 437 ASN EEE OD1 1 
ATOM 4144 N ND2 . ASN C 3 106 ? 39.776  -44.534 -91.425  1.000 181.398 ? 437 ASN EEE ND2 1 
ATOM 4145 N N   . SER C 3 107 ? 43.356  -47.783 -91.117  1.000 168.815 ? 438 SER EEE N   1 
ATOM 4146 C CA  . SER C 3 107 ? 44.670  -48.102 -91.741  1.000 176.365 ? 438 SER EEE CA  1 
ATOM 4147 C C   . SER C 3 107 ? 44.706  -47.622 -93.203  1.000 193.923 ? 438 SER EEE C   1 
ATOM 4148 O O   . SER C 3 107 ? 45.495  -48.181 -94.000  1.000 209.257 ? 438 SER EEE O   1 
ATOM 4149 C CB  . SER C 3 107 ? 44.984  -49.569 -91.575  1.000 165.162 ? 438 SER EEE CB  1 
ATOM 4150 O OG  . SER C 3 107 ? 43.934  -50.366 -92.095  1.000 157.680 ? 438 SER EEE OG  1 
ATOM 4151 N N   . ASN C 3 108 ? 43.927  -46.578 -93.520  1.000 193.281 ? 439 ASN EEE N   1 
ATOM 4152 C CA  . ASN C 3 108 ? 43.792  -45.976 -94.874  1.000 184.872 ? 439 ASN EEE CA  1 
ATOM 4153 C C   . ASN C 3 108 ? 45.171  -45.553 -95.385  1.000 182.067 ? 439 ASN EEE C   1 
ATOM 4154 O O   . ASN C 3 108 ? 45.434  -45.779 -96.559  1.000 191.600 ? 439 ASN EEE O   1 
ATOM 4155 C CB  . ASN C 3 108 ? 42.819  -44.794 -94.867  1.000 188.489 ? 439 ASN EEE CB  1 
ATOM 4156 C CG  . ASN C 3 108 ? 42.226  -44.496 -96.226  1.000 191.216 ? 439 ASN EEE CG  1 
ATOM 4157 O OD1 . ASN C 3 108 ? 41.815  -45.406 -96.935  1.000 189.106 ? 439 ASN EEE OD1 1 
ATOM 4158 N ND2 . ASN C 3 108 ? 42.152  -43.227 -96.589  1.000 198.177 ? 439 ASN EEE ND2 1 
ATOM 4159 N N   . ASN C 3 109 ? 46.020  -44.983 -94.525  1.000 180.441 ? 440 ASN EEE N   1 
ATOM 4160 C CA  . ASN C 3 109 ? 47.377  -44.487 -94.893  1.000 185.971 ? 440 ASN EEE CA  1 
ATOM 4161 C C   . ASN C 3 109 ? 48.304  -45.644 -95.327  1.000 186.103 ? 440 ASN EEE C   1 
ATOM 4162 O O   . ASN C 3 109 ? 49.245  -45.359 -96.082  1.000 198.847 ? 440 ASN EEE O   1 
ATOM 4163 C CB  . ASN C 3 109 ? 47.992  -43.642 -93.774  1.000 185.154 ? 440 ASN EEE CB  1 
ATOM 4164 C CG  . ASN C 3 109 ? 48.096  -44.375 -92.452  1.000 197.090 ? 440 ASN EEE CG  1 
ATOM 4165 O OD1 . ASN C 3 109 ? 47.190  -45.118 -92.081  1.000 203.999 ? 440 ASN EEE OD1 1 
ATOM 4166 N ND2 . ASN C 3 109 ? 49.184  -44.162 -91.720  1.000 207.703 ? 440 ASN EEE ND2 1 
ATOM 4167 N N   . LEU C 3 110 ? 48.068  -46.888 -94.883  1.000 184.683 ? 441 LEU EEE N   1 
ATOM 4168 C CA  . LEU C 3 110 ? 48.915  -48.085 -95.180  1.000 182.700 ? 441 LEU EEE CA  1 
ATOM 4169 C C   . LEU C 3 110 ? 48.243  -49.006 -96.196  1.000 183.726 ? 441 LEU EEE C   1 
ATOM 4170 O O   . LEU C 3 110 ? 48.955  -49.518 -97.076  1.000 191.566 ? 441 LEU EEE O   1 
ATOM 4171 C CB  . LEU C 3 110 ? 49.127  -48.911 -93.910  1.000 183.410 ? 441 LEU EEE CB  1 
ATOM 4172 C CG  . LEU C 3 110 ? 49.658  -48.162 -92.695  1.000 186.543 ? 441 LEU EEE CG  1 
ATOM 4173 C CD1 . LEU C 3 110 ? 49.311  -48.907 -91.405  1.000 188.522 ? 441 LEU EEE CD1 1 
ATOM 4174 C CD2 . LEU C 3 110 ? 51.150  -47.944 -92.835  1.000 183.009 ? 441 LEU EEE CD2 1 
ATOM 4175 N N   . ASP C 3 111 ? 46.949  -49.284 -96.005  1.000 187.482 ? 442 ASP EEE N   1 
ATOM 4176 C CA  . ASP C 3 111 ? 46.246  -50.461 -96.591  1.000 202.800 ? 442 ASP EEE CA  1 
ATOM 4177 C C   . ASP C 3 111 ? 45.316  -50.065 -97.750  1.000 217.906 ? 442 ASP EEE C   1 
ATOM 4178 O O   . ASP C 3 111 ? 44.717  -50.988 -98.352  1.000 222.451 ? 442 ASP EEE O   1 
ATOM 4179 C CB  . ASP C 3 111 ? 45.473  -51.215 -95.510  1.000 198.086 ? 442 ASP EEE CB  1 
ATOM 4180 C CG  . ASP C 3 111 ? 46.378  -51.926 -94.527  1.000 198.348 ? 442 ASP EEE CG  1 
ATOM 4181 O OD1 . ASP C 3 111 ? 47.403  -52.463 -94.973  1.000 214.935 ? 442 ASP EEE OD1 1 
ATOM 4182 O OD2 . ASP C 3 111 ? 46.056  -51.925 -93.326  1.000 204.066 ? 442 ASP EEE OD2 1 
ATOM 4183 N N   . SER C 3 112 ? 45.184  -48.767 -98.045  1.000 218.316 ? 443 SER EEE N   1 
ATOM 4184 C CA  . SER C 3 112 ? 44.587  -48.229 -99.295  1.000 210.720 ? 443 SER EEE CA  1 
ATOM 4185 C C   . SER C 3 112 ? 45.710  -47.855 -100.269 1.000 220.522 ? 443 SER EEE C   1 
ATOM 4186 O O   . SER C 3 112 ? 46.855  -47.622 -99.826  1.000 212.426 ? 443 SER EEE O   1 
ATOM 4187 C CB  . SER C 3 112 ? 43.706  -47.048 -99.016  1.000 206.927 ? 443 SER EEE CB  1 
ATOM 4188 O OG  . SER C 3 112 ? 42.652  -47.409 -98.142  1.000 212.798 ? 443 SER EEE OG  1 
ATOM 4189 N N   . LYS C 3 113 ? 45.395  -47.832 -101.566 1.000 233.163 ? 444 LYS EEE N   1 
ATOM 4190 C CA  . LYS C 3 113 ? 46.250  -47.241 -102.633 1.000 221.616 ? 444 LYS EEE CA  1 
ATOM 4191 C C   . LYS C 3 113 ? 45.350  -46.744 -103.766 1.000 209.162 ? 444 LYS EEE C   1 
ATOM 4192 O O   . LYS C 3 113 ? 44.219  -47.264 -103.898 1.000 204.834 ? 444 LYS EEE O   1 
ATOM 4193 C CB  . LYS C 3 113 ? 47.279  -48.261 -103.123 1.000 224.624 ? 444 LYS EEE CB  1 
ATOM 4194 C CG  . LYS C 3 113 ? 46.723  -49.606 -103.574 1.000 225.531 ? 444 LYS EEE CG  1 
ATOM 4195 C CD  . LYS C 3 113 ? 47.835  -50.644 -103.636 1.000 230.007 ? 444 LYS EEE CD  1 
ATOM 4196 C CE  . LYS C 3 113 ? 47.390  -52.036 -104.029 1.000 229.676 ? 444 LYS EEE CE  1 
ATOM 4197 N NZ  . LYS C 3 113 ? 48.512  -52.787 -104.650 1.000 228.428 ? 444 LYS EEE NZ  1 
ATOM 4198 N N   . VAL C 3 114 ? 45.811  -45.745 -104.515 1.000 204.510 ? 445 VAL EEE N   1 
ATOM 4199 C CA  . VAL C 3 114 ? 45.009  -45.124 -105.614 1.000 210.612 ? 445 VAL EEE CA  1 
ATOM 4200 C C   . VAL C 3 114 ? 44.701  -46.221 -106.641 1.000 206.363 ? 445 VAL EEE C   1 
ATOM 4201 O O   . VAL C 3 114 ? 45.631  -46.965 -106.996 1.000 206.302 ? 445 VAL EEE O   1 
ATOM 4202 C CB  . VAL C 3 114 ? 45.724  -43.916 -106.251 1.000 215.882 ? 445 VAL EEE CB  1 
ATOM 4203 C CG1 . VAL C 3 114 ? 44.850  -43.261 -107.314 1.000 222.298 ? 445 VAL EEE CG1 1 
ATOM 4204 C CG2 . VAL C 3 114 ? 46.173  -42.897 -105.210 1.000 210.921 ? 445 VAL EEE CG2 1 
ATOM 4205 N N   . GLY C 3 115 ? 43.441  -46.355 -107.055 1.000 203.055 ? 446 GLY EEE N   1 
ATOM 4206 C CA  . GLY C 3 115 ? 42.995  -47.452 -107.938 1.000 217.270 ? 446 GLY EEE CA  1 
ATOM 4207 C C   . GLY C 3 115 ? 42.599  -48.713 -107.180 1.000 220.768 ? 446 GLY EEE C   1 
ATOM 4208 O O   . GLY C 3 115 ? 42.147  -49.660 -107.852 1.000 229.239 ? 446 GLY EEE O   1 
ATOM 4209 N N   . GLY C 3 116 ? 42.782  -48.731 -105.849 1.000 230.203 ? 447 GLY EEE N   1 
ATOM 4210 C CA  . GLY C 3 116 ? 42.259  -49.744 -104.900 1.000 230.689 ? 447 GLY EEE CA  1 
ATOM 4211 C C   . GLY C 3 116 ? 43.294  -50.790 -104.481 1.000 230.981 ? 447 GLY EEE C   1 
ATOM 4212 O O   . GLY C 3 116 ? 43.991  -51.289 -105.380 1.000 250.103 ? 447 GLY EEE O   1 
ATOM 4213 N N   . ASN C 3 117 ? 43.399  -51.114 -103.176 1.000 217.202 ? 448 ASN EEE N   1 
ATOM 4214 C CA  . ASN C 3 117 ? 44.071  -52.342 -102.644 1.000 214.225 ? 448 ASN EEE CA  1 
ATOM 4215 C C   . ASN C 3 117 ? 43.040  -53.472 -102.560 1.000 204.023 ? 448 ASN EEE C   1 
ATOM 4216 O O   . ASN C 3 117 ? 42.051  -53.315 -101.837 1.000 188.969 ? 448 ASN EEE O   1 
ATOM 4217 C CB  . ASN C 3 117 ? 44.744  -52.151 -101.274 1.000 206.108 ? 448 ASN EEE CB  1 
ATOM 4218 C CG  . ASN C 3 117 ? 45.458  -53.384 -100.732 1.000 191.481 ? 448 ASN EEE CG  1 
ATOM 4219 O OD1 . ASN C 3 117 ? 45.515  -54.430 -101.369 1.000 187.183 ? 448 ASN EEE OD1 1 
ATOM 4220 N ND2 . ASN C 3 117 ? 46.062  -53.269 -99.561  1.000 173.608 ? 448 ASN EEE ND2 1 
ATOM 4221 N N   . TYR C 3 118 ? 43.292  -54.579 -103.257 1.000 199.761 ? 449 TYR EEE N   1 
ATOM 4222 C CA  . TYR C 3 118 ? 42.350  -55.718 -103.380 1.000 204.697 ? 449 TYR EEE CA  1 
ATOM 4223 C C   . TYR C 3 118 ? 42.934  -56.944 -102.691 1.000 206.352 ? 449 TYR EEE C   1 
ATOM 4224 O O   . TYR C 3 118 ? 42.332  -58.018 -102.808 1.000 216.243 ? 449 TYR EEE O   1 
ATOM 4225 C CB  . TYR C 3 118 ? 42.059  -56.009 -104.851 1.000 210.910 ? 449 TYR EEE CB  1 
ATOM 4226 C CG  . TYR C 3 118 ? 41.351  -54.869 -105.534 1.000 221.908 ? 449 TYR EEE CG  1 
ATOM 4227 C CD1 . TYR C 3 118 ? 40.026  -54.601 -105.235 1.000 223.285 ? 449 TYR EEE CD1 1 
ATOM 4228 C CD2 . TYR C 3 118 ? 41.997  -54.031 -106.434 1.000 228.732 ? 449 TYR EEE CD2 1 
ATOM 4229 C CE1 . TYR C 3 118 ? 39.339  -53.563 -105.846 1.000 223.106 ? 449 TYR EEE CE1 1 
ATOM 4230 C CE2 . TYR C 3 118 ? 41.332  -52.973 -107.037 1.000 230.735 ? 449 TYR EEE CE2 1 
ATOM 4231 C CZ  . TYR C 3 118 ? 39.997  -52.738 -106.738 1.000 226.788 ? 449 TYR EEE CZ  1 
ATOM 4232 O OH  . TYR C 3 118 ? 39.305  -51.711 -107.312 1.000 230.180 ? 449 TYR EEE OH  1 
ATOM 4233 N N   . ASN C 3 119 ? 44.058  -56.793 -101.997 1.000 198.412 ? 450 ASN EEE N   1 
ATOM 4234 C CA  . ASN C 3 119 ? 44.804  -57.955 -101.457 1.000 200.595 ? 450 ASN EEE CA  1 
ATOM 4235 C C   . ASN C 3 119 ? 44.029  -58.568 -100.292 1.000 198.683 ? 450 ASN EEE C   1 
ATOM 4236 O O   . ASN C 3 119 ? 44.237  -59.774 -100.037 1.000 198.439 ? 450 ASN EEE O   1 
ATOM 4237 C CB  . ASN C 3 119 ? 46.212  -57.560 -101.029 1.000 208.133 ? 450 ASN EEE CB  1 
ATOM 4238 C CG  . ASN C 3 119 ? 47.110  -57.394 -102.227 1.000 213.796 ? 450 ASN EEE CG  1 
ATOM 4239 O OD1 . ASN C 3 119 ? 47.377  -58.362 -102.934 1.000 213.585 ? 450 ASN EEE OD1 1 
ATOM 4240 N ND2 . ASN C 3 119 ? 47.563  -56.177 -102.467 1.000 229.756 ? 450 ASN EEE ND2 1 
ATOM 4241 N N   . TYR C 3 120 ? 43.205  -57.766 -99.606  1.000 196.935 ? 451 TYR EEE N   1 
ATOM 4242 C CA  . TYR C 3 120 ? 42.501  -58.166 -98.362  1.000 199.681 ? 451 TYR EEE CA  1 
ATOM 4243 C C   . TYR C 3 120 ? 41.164  -58.809 -98.746  1.000 187.994 ? 451 TYR EEE C   1 
ATOM 4244 O O   . TYR C 3 120 ? 40.387  -58.179 -99.506  1.000 176.289 ? 451 TYR EEE O   1 
ATOM 4245 C CB  . TYR C 3 120 ? 42.369  -56.969 -97.414  1.000 207.386 ? 451 TYR EEE CB  1 
ATOM 4246 C CG  . TYR C 3 120 ? 43.650  -56.530 -96.740  1.000 197.827 ? 451 TYR EEE CG  1 
ATOM 4247 C CD1 . TYR C 3 120 ? 44.256  -57.316 -95.776  1.000 191.858 ? 451 TYR EEE CD1 1 
ATOM 4248 C CD2 . TYR C 3 120 ? 44.251  -55.318 -97.041  1.000 197.060 ? 451 TYR EEE CD2 1 
ATOM 4249 C CE1 . TYR C 3 120 ? 45.416  -56.914 -95.133  1.000 186.123 ? 451 TYR EEE CE1 1 
ATOM 4250 C CE2 . TYR C 3 120 ? 45.406  -54.897 -96.398  1.000 189.946 ? 451 TYR EEE CE2 1 
ATOM 4251 C CZ  . TYR C 3 120 ? 45.993  -55.699 -95.438  1.000 182.481 ? 451 TYR EEE CZ  1 
ATOM 4252 O OH  . TYR C 3 120 ? 47.131  -55.343 -94.775  1.000 177.767 ? 451 TYR EEE OH  1 
ATOM 4253 N N   . LEU C 3 121 ? 40.935  -60.029 -98.243  1.000 182.155 ? 452 LEU EEE N   1 
ATOM 4254 C CA  . LEU C 3 121 ? 39.750  -60.860 -98.557  1.000 186.213 ? 452 LEU EEE CA  1 
ATOM 4255 C C   . LEU C 3 121 ? 38.867  -60.990 -97.318  1.000 180.438 ? 452 LEU EEE C   1 
ATOM 4256 O O   . LEU C 3 121 ? 39.331  -60.672 -96.180  1.000 165.289 ? 452 LEU EEE O   1 
ATOM 4257 C CB  . LEU C 3 121 ? 40.158  -62.270 -99.001  1.000 190.623 ? 452 LEU EEE CB  1 
ATOM 4258 C CG  . LEU C 3 121 ? 41.134  -62.416 -100.169 1.000 191.411 ? 452 LEU EEE CG  1 
ATOM 4259 C CD1 . LEU C 3 121 ? 41.068  -63.825 -100.717 1.000 190.164 ? 452 LEU EEE CD1 1 
ATOM 4260 C CD2 . LEU C 3 121 ? 40.869  -61.434 -101.296 1.000 198.105 ? 452 LEU EEE CD2 1 
ATOM 4261 N N   . TYR C 3 122 ? 37.649  -61.473 -97.587  1.000 180.806 ? 453 TYR EEE N   1 
ATOM 4262 C CA  . TYR C 3 122 ? 36.658  -62.003 -96.623  1.000 174.596 ? 453 TYR EEE CA  1 
ATOM 4263 C C   . TYR C 3 122 ? 35.851  -63.137 -97.272  1.000 168.463 ? 453 TYR EEE C   1 
ATOM 4264 O O   . TYR C 3 122 ? 35.765  -63.185 -98.507  1.000 167.014 ? 453 TYR EEE O   1 
ATOM 4265 C CB  . TYR C 3 122 ? 35.753  -60.863 -96.163  1.000 177.198 ? 453 TYR EEE CB  1 
ATOM 4266 C CG  . TYR C 3 122 ? 34.877  -60.280 -97.240  1.000 172.086 ? 453 TYR EEE CG  1 
ATOM 4267 C CD1 . TYR C 3 122 ? 35.323  -59.243 -98.033  1.000 168.124 ? 453 TYR EEE CD1 1 
ATOM 4268 C CD2 . TYR C 3 122 ? 33.585  -60.742 -97.422  1.000 174.287 ? 453 TYR EEE CD2 1 
ATOM 4269 C CE1 . TYR C 3 122 ? 34.505  -58.685 -98.994  1.000 180.958 ? 453 TYR EEE CE1 1 
ATOM 4270 C CE2 . TYR C 3 122 ? 32.751  -60.182 -98.366  1.000 180.893 ? 453 TYR EEE CE2 1 
ATOM 4271 C CZ  . TYR C 3 122 ? 33.216  -59.155 -99.161  1.000 188.616 ? 453 TYR EEE CZ  1 
ATOM 4272 O OH  . TYR C 3 122 ? 32.408  -58.623 -100.121 1.000 216.999 ? 453 TYR EEE OH  1 
ATOM 4273 N N   . ARG C 3 123 ? 35.297  -64.033 -96.448  1.000 167.950 ? 454 ARG EEE N   1 
ATOM 4274 C CA  . ARG C 3 123 ? 34.352  -65.096 -96.870  1.000 165.984 ? 454 ARG EEE CA  1 
ATOM 4275 C C   . ARG C 3 123 ? 32.947  -64.501 -96.971  1.000 175.719 ? 454 ARG EEE C   1 
ATOM 4276 O O   . ARG C 3 123 ? 32.447  -63.956 -95.972  1.000 159.988 ? 454 ARG EEE O   1 
ATOM 4277 C CB  . ARG C 3 123 ? 34.349  -66.272 -95.900  1.000 158.780 ? 454 ARG EEE CB  1 
ATOM 4278 C CG  . ARG C 3 123 ? 33.518  -67.444 -96.391  1.000 164.313 ? 454 ARG EEE CG  1 
ATOM 4279 C CD  . ARG C 3 123 ? 33.772  -68.644 -95.507  1.000 173.629 ? 454 ARG EEE CD  1 
ATOM 4280 N NE  . ARG C 3 123 ? 35.185  -69.026 -95.396  1.000 179.251 ? 454 ARG EEE NE  1 
ATOM 4281 C CZ  . ARG C 3 123 ? 35.836  -69.830 -96.246  1.000 186.496 ? 454 ARG EEE CZ  1 
ATOM 4282 N NH1 . ARG C 3 123 ? 35.218  -70.338 -97.306  1.000 191.987 ? 454 ARG EEE NH1 1 
ATOM 4283 N NH2 . ARG C 3 123 ? 37.109  -70.130 -96.032  1.000 179.249 ? 454 ARG EEE NH2 1 
ATOM 4284 N N   . LEU C 3 124 ? 32.363  -64.621 -98.165  1.000 194.978 ? 455 LEU EEE N   1 
ATOM 4285 C CA  . LEU C 3 124 ? 31.078  -64.018 -98.601  1.000 189.619 ? 455 LEU EEE CA  1 
ATOM 4286 C C   . LEU C 3 124 ? 29.962  -65.058 -98.447  1.000 177.043 ? 455 LEU EEE C   1 
ATOM 4287 O O   . LEU C 3 124 ? 28.817  -64.636 -98.177  1.000 162.958 ? 455 LEU EEE O   1 
ATOM 4288 C CB  . LEU C 3 124 ? 31.275  -63.575 -100.055 1.000 201.855 ? 455 LEU EEE CB  1 
ATOM 4289 C CG  . LEU C 3 124 ? 30.059  -62.974 -100.753 1.000 218.025 ? 455 LEU EEE CG  1 
ATOM 4290 C CD1 . LEU C 3 124 ? 29.556  -61.756 -100.001 1.000 211.423 ? 455 LEU EEE CD1 1 
ATOM 4291 C CD2 . LEU C 3 124 ? 30.389  -62.617 -102.199 1.000 224.077 ? 455 LEU EEE CD2 1 
ATOM 4292 N N   . PHE C 3 125 ? 30.299  -66.353 -98.592  1.000 173.955 ? 456 PHE EEE N   1 
ATOM 4293 C CA  . PHE C 3 125 ? 29.347  -67.500 -98.553  1.000 184.228 ? 456 PHE EEE CA  1 
ATOM 4294 C C   . PHE C 3 125 ? 29.850  -68.650 -97.685  1.000 179.449 ? 456 PHE EEE C   1 
ATOM 4295 O O   . PHE C 3 125 ? 31.058  -68.983 -97.721  1.000 167.358 ? 456 PHE EEE O   1 
ATOM 4296 C CB  . PHE C 3 125 ? 29.122  -68.159 -99.915  1.000 190.973 ? 456 PHE EEE CB  1 
ATOM 4297 C CG  . PHE C 3 125 ? 28.617  -67.221 -100.973 1.000 188.634 ? 456 PHE EEE CG  1 
ATOM 4298 C CD1 . PHE C 3 125 ? 27.362  -66.653 -100.868 1.000 183.177 ? 456 PHE EEE CD1 1 
ATOM 4299 C CD2 . PHE C 3 125 ? 29.420  -66.882 -102.043 1.000 187.970 ? 456 PHE EEE CD2 1 
ATOM 4300 C CE1 . PHE C 3 125 ? 26.919  -65.754 -101.819 1.000 184.688 ? 456 PHE EEE CE1 1 
ATOM 4301 C CE2 . PHE C 3 125 ? 28.977  -65.979 -102.989 1.000 191.606 ? 456 PHE EEE CE2 1 
ATOM 4302 C CZ  . PHE C 3 125 ? 27.727  -65.420 -102.877 1.000 193.767 ? 456 PHE EEE CZ  1 
ATOM 4303 N N   . ARG C 3 126 ? 28.887  -69.292 -97.016  1.000 172.711 ? 457 ARG EEE N   1 
ATOM 4304 C CA  . ARG C 3 126 ? 29.095  -70.477 -96.158  1.000 168.419 ? 457 ARG EEE CA  1 
ATOM 4305 C C   . ARG C 3 126 ? 27.732  -71.051 -95.818  1.000 166.406 ? 457 ARG EEE C   1 
ATOM 4306 O O   . ARG C 3 126 ? 26.772  -70.262 -95.674  1.000 160.282 ? 457 ARG EEE O   1 
ATOM 4307 C CB  . ARG C 3 126 ? 29.794  -70.052 -94.868  1.000 179.292 ? 457 ARG EEE CB  1 
ATOM 4308 C CG  . ARG C 3 126 ? 30.653  -71.128 -94.227  1.000 181.094 ? 457 ARG EEE CG  1 
ATOM 4309 C CD  . ARG C 3 126 ? 31.349  -70.590 -92.973  1.000 169.927 ? 457 ARG EEE CD  1 
ATOM 4310 N NE  . ARG C 3 126 ? 32.225  -71.613 -92.419  1.000 163.094 ? 457 ARG EEE NE  1 
ATOM 4311 C CZ  . ARG C 3 126 ? 31.850  -72.596 -91.594  1.000 158.378 ? 457 ARG EEE CZ  1 
ATOM 4312 N NH1 . ARG C 3 126 ? 30.609  -72.696 -91.142  1.000 155.249 ? 457 ARG EEE NH1 1 
ATOM 4313 N NH2 . ARG C 3 126 ? 32.748  -73.475 -91.198  1.000 156.007 ? 457 ARG EEE NH2 1 
ATOM 4314 N N   . LYS C 3 127 ? 27.675  -72.367 -95.648  1.000 169.557 ? 458 LYS EEE N   1 
ATOM 4315 C CA  . LYS C 3 127 ? 26.404  -73.120 -95.466  1.000 183.116 ? 458 LYS EEE CA  1 
ATOM 4316 C C   . LYS C 3 127 ? 25.783  -72.839 -94.093  1.000 181.472 ? 458 LYS EEE C   1 
ATOM 4317 O O   . LYS C 3 127 ? 24.544  -72.947 -93.958  1.000 164.877 ? 458 LYS EEE O   1 
ATOM 4318 C CB  . LYS C 3 127 ? 26.698  -74.611 -95.602  1.000 192.379 ? 458 LYS EEE CB  1 
ATOM 4319 C CG  . LYS C 3 127 ? 27.494  -74.976 -96.843  1.000 200.043 ? 458 LYS EEE CG  1 
ATOM 4320 C CD  . LYS C 3 127 ? 27.281  -76.401 -97.255  1.000 211.796 ? 458 LYS EEE CD  1 
ATOM 4321 C CE  . LYS C 3 127 ? 28.085  -77.374 -96.427  1.000 212.010 ? 458 LYS EEE CE  1 
ATOM 4322 N NZ  . LYS C 3 127 ? 28.203  -78.667 -97.137  1.000 225.197 ? 458 LYS EEE NZ  1 
ATOM 4323 N N   . SER C 3 128 ? 26.643  -72.530 -93.121  1.000 196.463 ? 459 SER EEE N   1 
ATOM 4324 C CA  . SER C 3 128 ? 26.348  -72.504 -91.665  1.000 206.188 ? 459 SER EEE CA  1 
ATOM 4325 C C   . SER C 3 128 ? 27.254  -71.482 -90.971  1.000 197.705 ? 459 SER EEE C   1 
ATOM 4326 O O   . SER C 3 128 ? 28.323  -71.162 -91.525  1.000 190.783 ? 459 SER EEE O   1 
ATOM 4327 C CB  . SER C 3 128 ? 26.506  -73.889 -91.063  1.000 215.780 ? 459 SER EEE CB  1 
ATOM 4328 O OG  . SER C 3 128 ? 27.873  -74.228 -90.834  1.000 209.799 ? 459 SER EEE OG  1 
ATOM 4329 N N   . ASN C 3 129 ? 26.851  -70.999 -89.795  1.000 193.128 ? 460 ASN EEE N   1 
ATOM 4330 C CA  . ASN C 3 129 ? 27.645  -70.005 -89.031  1.000 187.896 ? 460 ASN EEE CA  1 
ATOM 4331 C C   . ASN C 3 129 ? 28.852  -70.730 -88.429  1.000 179.037 ? 460 ASN EEE C   1 
ATOM 4332 O O   . ASN C 3 129 ? 28.754  -71.955 -88.174  1.000 170.119 ? 460 ASN EEE O   1 
ATOM 4333 C CB  . ASN C 3 129 ? 26.804  -69.256 -87.992  1.000 192.033 ? 460 ASN EEE CB  1 
ATOM 4334 C CG  . ASN C 3 129 ? 25.793  -68.311 -88.612  1.000 196.903 ? 460 ASN EEE CG  1 
ATOM 4335 O OD1 . ASN C 3 129 ? 25.847  -68.014 -89.800  1.000 193.277 ? 460 ASN EEE OD1 1 
ATOM 4336 N ND2 . ASN C 3 129 ? 24.853  -67.834 -87.816  1.000 210.156 ? 460 ASN EEE ND2 1 
ATOM 4337 N N   . LEU C 3 130 ? 29.956  -69.991 -88.289  1.000 173.732 ? 461 LEU EEE N   1 
ATOM 4338 C CA  . LEU C 3 130 ? 31.168  -70.367 -87.519  1.000 164.491 ? 461 LEU EEE CA  1 
ATOM 4339 C C   . LEU C 3 130 ? 30.820  -70.601 -86.045  1.000 161.559 ? 461 LEU EEE C   1 
ATOM 4340 O O   . LEU C 3 130 ? 29.994  -69.850 -85.460  1.000 153.595 ? 461 LEU EEE O   1 
ATOM 4341 C CB  . LEU C 3 130 ? 32.198  -69.237 -87.595  1.000 163.394 ? 461 LEU EEE CB  1 
ATOM 4342 C CG  . LEU C 3 130 ? 32.885  -69.022 -88.935  1.000 161.168 ? 461 LEU EEE CG  1 
ATOM 4343 C CD1 . LEU C 3 130 ? 33.957  -67.948 -88.823  1.000 152.814 ? 461 LEU EEE CD1 1 
ATOM 4344 C CD2 . LEU C 3 130 ? 33.486  -70.320 -89.436  1.000 166.812 ? 461 LEU EEE CD2 1 
ATOM 4345 N N   . LYS C 3 131 ? 31.463  -71.608 -85.471  1.000 156.048 ? 462 LYS EEE N   1 
ATOM 4346 C CA  . LYS C 3 131 ? 31.581  -71.776 -84.015  1.000 157.903 ? 462 LYS EEE CA  1 
ATOM 4347 C C   . LYS C 3 131 ? 32.490  -70.665 -83.524  1.000 162.391 ? 462 LYS EEE C   1 
ATOM 4348 O O   . LYS C 3 131 ? 33.247  -70.096 -84.316  1.000 157.800 ? 462 LYS EEE O   1 
ATOM 4349 C CB  . LYS C 3 131 ? 32.178  -73.147 -83.689  1.000 165.048 ? 462 LYS EEE CB  1 
ATOM 4350 C CG  . LYS C 3 131 ? 31.288  -74.344 -83.985  1.000 167.421 ? 462 LYS EEE CG  1 
ATOM 4351 C CD  . LYS C 3 131 ? 30.006  -74.322 -83.193  1.000 173.142 ? 462 LYS EEE CD  1 
ATOM 4352 C CE  . LYS C 3 131 ? 29.196  -75.586 -83.342  1.000 181.712 ? 462 LYS EEE CE  1 
ATOM 4353 N NZ  . LYS C 3 131 ? 27.742  -75.290 -83.358  1.000 185.513 ? 462 LYS EEE NZ  1 
ATOM 4354 N N   . PRO C 3 132 ? 32.477  -70.327 -82.214  1.000 166.321 ? 463 PRO EEE N   1 
ATOM 4355 C CA  . PRO C 3 132 ? 33.258  -69.187 -81.757  1.000 167.022 ? 463 PRO EEE CA  1 
ATOM 4356 C C   . PRO C 3 132 ? 34.756  -69.519 -81.892  1.000 167.496 ? 463 PRO EEE C   1 
ATOM 4357 O O   . PRO C 3 132 ? 35.133  -70.656 -81.570  1.000 149.253 ? 463 PRO EEE O   1 
ATOM 4358 C CB  . PRO C 3 132 ? 32.784  -68.973 -80.315  1.000 169.098 ? 463 PRO EEE CB  1 
ATOM 4359 C CG  . PRO C 3 132 ? 31.539  -69.822 -80.174  1.000 168.031 ? 463 PRO EEE CG  1 
ATOM 4360 C CD  . PRO C 3 132 ? 31.761  -70.989 -81.111  1.000 162.321 ? 463 PRO EEE CD  1 
ATOM 4361 N N   . PHE C 3 133 ? 35.525  -68.561 -82.438  1.000 164.682 ? 464 PHE EEE N   1 
ATOM 4362 C CA  . PHE C 3 133 ? 36.999  -68.607 -82.630  1.000 163.514 ? 464 PHE EEE CA  1 
ATOM 4363 C C   . PHE C 3 133 ? 37.361  -69.703 -83.630  1.000 158.437 ? 464 PHE EEE C   1 
ATOM 4364 O O   . PHE C 3 133 ? 38.512  -70.210 -83.581  1.000 139.647 ? 464 PHE EEE O   1 
ATOM 4365 C CB  . PHE C 3 133 ? 37.720  -68.833 -81.294  1.000 167.912 ? 464 PHE EEE CB  1 
ATOM 4366 C CG  . PHE C 3 133 ? 37.689  -67.678 -80.317  1.000 158.929 ? 464 PHE EEE CG  1 
ATOM 4367 C CD1 . PHE C 3 133 ? 38.014  -66.393 -80.718  1.000 156.076 ? 464 PHE EEE CD1 1 
ATOM 4368 C CD2 . PHE C 3 133 ? 37.407  -67.886 -78.984  1.000 152.627 ? 464 PHE EEE CD2 1 
ATOM 4369 C CE1 . PHE C 3 133 ? 38.004  -65.333 -79.832  1.000 146.695 ? 464 PHE EEE CE1 1 
ATOM 4370 C CE2 . PHE C 3 133 ? 37.409  -66.827 -78.100  1.000 156.952 ? 464 PHE EEE CE2 1 
ATOM 4371 C CZ  . PHE C 3 133 ? 37.700  -65.553 -78.524  1.000 152.134 ? 464 PHE EEE CZ  1 
ATOM 4372 N N   . GLU C 3 134 ? 36.411  -70.062 -84.497  1.000 167.872 ? 465 GLU EEE N   1 
ATOM 4373 C CA  . GLU C 3 134 ? 36.651  -71.047 -85.581  1.000 163.982 ? 465 GLU EEE CA  1 
ATOM 4374 C C   . GLU C 3 134 ? 37.469  -70.290 -86.610  1.000 151.148 ? 465 GLU EEE C   1 
ATOM 4375 O O   . GLU C 3 134 ? 37.283  -69.058 -86.684  1.000 140.499 ? 465 GLU EEE O   1 
ATOM 4376 C CB  . GLU C 3 134 ? 35.345  -71.598 -86.163  1.000 175.452 ? 465 GLU EEE CB  1 
ATOM 4377 C CG  . GLU C 3 134 ? 35.549  -72.602 -87.295  1.000 181.288 ? 465 GLU EEE CG  1 
ATOM 4378 C CD  . GLU C 3 134 ? 34.338  -73.458 -87.663  1.000 190.699 ? 465 GLU EEE CD  1 
ATOM 4379 O OE1 . GLU C 3 134 ? 33.203  -73.138 -87.205  1.000 193.559 ? 465 GLU EEE OE1 1 
ATOM 4380 O OE2 . GLU C 3 134 ? 34.528  -74.464 -88.400  1.000 185.896 ? 465 GLU EEE OE2 1 
ATOM 4381 N N   . ARG C 3 135 ? 38.359  -70.984 -87.310  1.000 144.495 ? 466 ARG EEE N   1 
ATOM 4382 C CA  . ARG C 3 135 ? 39.108  -70.423 -88.456  1.000 149.385 ? 466 ARG EEE CA  1 
ATOM 4383 C C   . ARG C 3 135 ? 38.934  -71.333 -89.670  1.000 161.051 ? 466 ARG EEE C   1 
ATOM 4384 O O   . ARG C 3 135 ? 39.435  -72.450 -89.625  1.000 169.753 ? 466 ARG EEE O   1 
ATOM 4385 C CB  . ARG C 3 135 ? 40.578  -70.320 -88.093  1.000 147.769 ? 466 ARG EEE CB  1 
ATOM 4386 C CG  . ARG C 3 135 ? 41.334  -69.364 -88.987  1.000 155.826 ? 466 ARG EEE CG  1 
ATOM 4387 C CD  . ARG C 3 135 ? 42.754  -69.280 -88.484  1.000 166.060 ? 466 ARG EEE CD  1 
ATOM 4388 N NE  . ARG C 3 135 ? 43.658  -68.706 -89.467  1.000 175.590 ? 466 ARG EEE NE  1 
ATOM 4389 C CZ  . ARG C 3 135 ? 44.431  -69.381 -90.326  1.000 176.193 ? 466 ARG EEE CZ  1 
ATOM 4390 N NH1 . ARG C 3 135 ? 44.454  -70.707 -90.370  1.000 178.395 ? 466 ARG EEE NH1 1 
ATOM 4391 N NH2 . ARG C 3 135 ? 45.200  -68.695 -91.151  1.000 168.146 ? 466 ARG EEE NH2 1 
ATOM 4392 N N   . ASP C 3 136 ? 38.246  -70.856 -90.709  1.000 171.949 ? 467 ASP EEE N   1 
ATOM 4393 C CA  . ASP C 3 136 ? 37.873  -71.624 -91.930  1.000 175.670 ? 467 ASP EEE CA  1 
ATOM 4394 C C   . ASP C 3 136 ? 38.666  -71.087 -93.129  1.000 171.392 ? 467 ASP EEE C   1 
ATOM 4395 O O   . ASP C 3 136 ? 38.418  -69.934 -93.562  1.000 162.611 ? 467 ASP EEE O   1 
ATOM 4396 C CB  . ASP C 3 136 ? 36.358  -71.554 -92.165  1.000 182.152 ? 467 ASP EEE CB  1 
ATOM 4397 C CG  . ASP C 3 136 ? 35.853  -72.281 -93.397  1.000 185.158 ? 467 ASP EEE CG  1 
ATOM 4398 O OD1 . ASP C 3 136 ? 36.658  -72.969 -94.043  1.000 201.460 ? 467 ASP EEE OD1 1 
ATOM 4399 O OD2 . ASP C 3 136 ? 34.646  -72.163 -93.687  1.000 189.437 ? 467 ASP EEE OD2 1 
ATOM 4400 N N   . ILE C 3 137 ? 39.559  -71.913 -93.671  1.000 165.362 ? 468 ILE EEE N   1 
ATOM 4401 C CA  . ILE C 3 137 ? 40.389  -71.542 -94.851  1.000 173.860 ? 468 ILE EEE CA  1 
ATOM 4402 C C   . ILE C 3 137 ? 40.050  -72.458 -96.038  1.000 186.930 ? 468 ILE EEE C   1 
ATOM 4403 O O   . ILE C 3 137 ? 40.879  -72.557 -96.979  1.000 196.568 ? 468 ILE EEE O   1 
ATOM 4404 C CB  . ILE C 3 137 ? 41.881  -71.564 -94.490  1.000 168.706 ? 468 ILE EEE CB  1 
ATOM 4405 C CG1 . ILE C 3 137 ? 42.377  -72.956 -94.085  1.000 165.287 ? 468 ILE EEE CG1 1 
ATOM 4406 C CG2 . ILE C 3 137 ? 42.146  -70.504 -93.432  1.000 167.757 ? 468 ILE EEE CG2 1 
ATOM 4407 C CD1 . ILE C 3 137 ? 43.887  -73.034 -94.011  1.000 164.719 ? 468 ILE EEE CD1 1 
ATOM 4408 N N   . SER C 3 138 ? 38.863  -73.076 -96.040  1.000 187.394 ? 469 SER EEE N   1 
ATOM 4409 C CA  A SER C 3 138 ? 38.357  -73.873 -97.189  0.500 184.329 ? 469 SER EEE CA  1 
ATOM 4410 C CA  B SER C 3 138 ? 38.369  -73.873 -97.195  0.500 183.673 ? 469 SER EEE CA  1 
ATOM 4411 C C   . SER C 3 138 ? 38.042  -72.927 -98.349  1.000 183.654 ? 469 SER EEE C   1 
ATOM 4412 O O   . SER C 3 138 ? 37.673  -71.776 -98.065  1.000 159.465 ? 469 SER EEE O   1 
ATOM 4413 C CB  A SER C 3 138 ? 37.155  -74.724 -96.823  0.500 187.295 ? 469 SER EEE CB  1 
ATOM 4414 C CB  B SER C 3 138 ? 37.170  -74.725 -96.866  0.500 185.958 ? 469 SER EEE CB  1 
ATOM 4415 O OG  A SER C 3 138 ? 36.022  -73.925 -96.507  0.500 189.020 ? 469 SER EEE OG  1 
ATOM 4416 O OG  B SER C 3 138 ? 36.737  -75.434 -98.021  0.500 191.609 ? 469 SER EEE OG  1 
ATOM 4417 N N   . THR C 3 139 ? 38.185  -73.428 -99.583  1.000 197.646 ? 470 THR EEE N   1 
ATOM 4418 C CA  . THR C 3 139 ? 37.927  -72.684 -100.845 1.000 195.290 ? 470 THR EEE CA  1 
ATOM 4419 C C   . THR C 3 139 ? 37.048  -73.531 -101.758 1.000 191.136 ? 470 THR EEE C   1 
ATOM 4420 O O   . THR C 3 139 ? 37.127  -73.340 -102.984 1.000 189.928 ? 470 THR EEE O   1 
ATOM 4421 C CB  . THR C 3 139 ? 39.241  -72.313 -101.536 1.000 197.125 ? 470 THR EEE CB  1 
ATOM 4422 O OG1 . THR C 3 139 ? 39.957  -73.549 -101.608 1.000 197.308 ? 470 THR EEE OG1 1 
ATOM 4423 C CG2 . THR C 3 139 ? 40.023  -71.250 -100.792 1.000 198.175 ? 470 THR EEE CG2 1 
ATOM 4424 N N   . GLU C 3 140 ? 36.251  -74.421 -101.171 1.000 197.358 ? 471 GLU EEE N   1 
ATOM 4425 C CA  A GLU C 3 140 ? 35.258  -75.256 -101.900 0.500 215.290 ? 471 GLU EEE CA  1 
ATOM 4426 C CA  B GLU C 3 140 ? 35.283  -75.256 -101.924 0.500 208.063 ? 471 GLU EEE CA  1 
ATOM 4427 C C   . GLU C 3 140 ? 34.206  -74.349 -102.555 1.000 217.482 ? 471 GLU EEE C   1 
ATOM 4428 O O   . GLU C 3 140 ? 33.820  -73.326 -101.925 1.000 211.543 ? 471 GLU EEE O   1 
ATOM 4429 C CB  A GLU C 3 140 ? 34.570  -76.257 -100.969 0.500 218.403 ? 471 GLU EEE CB  1 
ATOM 4430 C CB  B GLU C 3 140 ? 34.779  -76.363 -100.995 0.500 201.573 ? 471 GLU EEE CB  1 
ATOM 4431 C CG  A GLU C 3 140 ? 33.373  -76.918 -101.626 0.500 227.808 ? 471 GLU EEE CG  1 
ATOM 4432 C CG  B GLU C 3 140 ? 35.852  -77.400 -100.721 0.500 196.429 ? 471 GLU EEE CG  1 
ATOM 4433 C CD  A GLU C 3 140 ? 32.860  -78.166 -100.940 0.500 230.512 ? 471 GLU EEE CD  1 
ATOM 4434 C CD  B GLU C 3 140 ? 35.552  -78.297 -99.539  0.500 193.346 ? 471 GLU EEE CD  1 
ATOM 4435 O OE1 A GLU C 3 140 ? 33.420  -78.531 -99.881  0.500 222.686 ? 471 GLU EEE OE1 1 
ATOM 4436 O OE1 B GLU C 3 140 ? 35.019  -77.771 -98.536  0.500 198.154 ? 471 GLU EEE OE1 1 
ATOM 4437 O OE2 A GLU C 3 140 ? 31.896  -78.762 -101.471 0.500 235.270 ? 471 GLU EEE OE2 1 
ATOM 4438 O OE2 B GLU C 3 140 ? 35.833  -79.521 -99.639  0.500 185.041 ? 471 GLU EEE OE2 1 
ATOM 4439 N N   . ILE C 3 141 ? 33.766  -74.700 -103.771 1.000 209.765 ? 472 ILE EEE N   1 
ATOM 4440 C CA  . ILE C 3 141 ? 32.758  -73.898 -104.518 1.000 205.446 ? 472 ILE EEE CA  1 
ATOM 4441 C C   . ILE C 3 141 ? 31.444  -73.980 -103.754 1.000 199.568 ? 472 ILE EEE C   1 
ATOM 4442 O O   . ILE C 3 141 ? 31.065  -75.094 -103.305 1.000 194.310 ? 472 ILE EEE O   1 
ATOM 4443 C CB  . ILE C 3 141 ? 32.610  -74.368 -105.975 1.000 219.428 ? 472 ILE EEE CB  1 
ATOM 4444 C CG1 . ILE C 3 141 ? 33.960  -74.291 -106.681 1.000 222.471 ? 472 ILE EEE CG1 1 
ATOM 4445 C CG2 . ILE C 3 141 ? 31.531  -73.568 -106.716 1.000 229.041 ? 472 ILE EEE CG2 1 
ATOM 4446 C CD1 . ILE C 3 141 ? 34.679  -73.000 -106.403 1.000 223.602 ? 472 ILE EEE CD1 1 
ATOM 4447 N N   . TYR C 3 142 ? 30.787  -72.834 -103.621 1.000 194.154 ? 473 TYR EEE N   1 
ATOM 4448 C CA  . TYR C 3 142 ? 29.552  -72.687 -102.821 1.000 191.568 ? 473 TYR EEE CA  1 
ATOM 4449 C C   . TYR C 3 142 ? 28.323  -72.869 -103.712 1.000 188.133 ? 473 TYR EEE C   1 
ATOM 4450 O O   . TYR C 3 142 ? 28.195  -72.096 -104.683 1.000 180.908 ? 473 TYR EEE O   1 
ATOM 4451 C CB  . TYR C 3 142 ? 29.522  -71.314 -102.154 1.000 192.007 ? 473 TYR EEE CB  1 
ATOM 4452 C CG  . TYR C 3 142 ? 28.285  -71.125 -101.330 1.000 184.652 ? 473 TYR EEE CG  1 
ATOM 4453 C CD1 . TYR C 3 142 ? 28.137  -71.805 -100.137 1.000 177.851 ? 473 TYR EEE CD1 1 
ATOM 4454 C CD2 . TYR C 3 142 ? 27.235  -70.344 -101.784 1.000 187.087 ? 473 TYR EEE CD2 1 
ATOM 4455 C CE1 . TYR C 3 142 ? 26.985  -71.677 -99.383  1.000 183.654 ? 473 TYR EEE CE1 1 
ATOM 4456 C CE2 . TYR C 3 142 ? 26.084  -70.195 -101.033 1.000 189.195 ? 473 TYR EEE CE2 1 
ATOM 4457 C CZ  . TYR C 3 142 ? 25.951  -70.869 -99.834  1.000 182.988 ? 473 TYR EEE CZ  1 
ATOM 4458 O OH  . TYR C 3 142 ? 24.799  -70.699 -99.121  1.000 179.637 ? 473 TYR EEE OH  1 
ATOM 4459 N N   . GLN C 3 143 ? 27.448  -73.817 -103.350 1.000 192.590 ? 474 GLN EEE N   1 
ATOM 4460 C CA  . GLN C 3 143 ? 26.124  -74.072 -103.996 1.000 204.043 ? 474 GLN EEE CA  1 
ATOM 4461 C C   . GLN C 3 143 ? 25.060  -73.076 -103.483 1.000 221.415 ? 474 GLN EEE C   1 
ATOM 4462 O O   . GLN C 3 143 ? 24.526  -73.302 -102.379 1.000 232.139 ? 474 GLN EEE O   1 
ATOM 4463 C CB  . GLN C 3 143 ? 25.709  -75.518 -103.723 1.000 193.245 ? 474 GLN EEE CB  1 
ATOM 4464 C CG  . GLN C 3 143 ? 24.280  -75.825 -104.138 1.000 197.140 ? 474 GLN EEE CG  1 
ATOM 4465 C CD  . GLN C 3 143 ? 23.931  -77.270 -103.901 1.000 209.928 ? 474 GLN EEE CD  1 
ATOM 4466 O OE1 . GLN C 3 143 ? 24.785  -78.073 -103.537 1.000 216.892 ? 474 GLN EEE OE1 1 
ATOM 4467 N NE2 . GLN C 3 143 ? 22.664  -77.609 -104.096 1.000 218.218 ? 474 GLN EEE NE2 1 
ATOM 4468 N N   . ALA C 3 144 ? 24.751  -72.017 -104.251 1.000 237.216 ? 475 ALA EEE N   1 
ATOM 4469 C CA  . ALA C 3 144 ? 23.806  -70.926 -103.884 1.000 244.059 ? 475 ALA EEE CA  1 
ATOM 4470 C C   . ALA C 3 144 ? 22.390  -71.217 -104.406 1.000 255.297 ? 475 ALA EEE C   1 
ATOM 4471 O O   . ALA C 3 144 ? 21.429  -70.650 -103.835 1.000 267.363 ? 475 ALA EEE O   1 
ATOM 4472 C CB  . ALA C 3 144 ? 24.306  -69.597 -104.409 1.000 246.669 ? 475 ALA EEE CB  1 
ATOM 4473 N N   . GLY C 3 145 ? 22.278  -72.035 -105.462 1.000 252.585 ? 476 GLY EEE N   1 
ATOM 4474 C CA  . GLY C 3 145 ? 21.010  -72.507 -106.055 1.000 254.296 ? 476 GLY EEE CA  1 
ATOM 4475 C C   . GLY C 3 145 ? 20.746  -73.966 -105.711 1.000 252.041 ? 476 GLY EEE C   1 
ATOM 4476 O O   . GLY C 3 145 ? 21.379  -74.489 -104.758 1.000 255.141 ? 476 GLY EEE O   1 
ATOM 4477 N N   . SER C 3 146 ? 19.845  -74.623 -106.442 1.000 239.160 ? 477 SER EEE N   1 
ATOM 4478 C CA  . SER C 3 146 ? 19.374  -75.987 -106.095 1.000 232.791 ? 477 SER EEE CA  1 
ATOM 4479 C C   . SER C 3 146 ? 20.202  -77.065 -106.807 1.000 232.493 ? 477 SER EEE C   1 
ATOM 4480 O O   . SER C 3 146 ? 19.890  -78.245 -106.567 1.000 238.922 ? 477 SER EEE O   1 
ATOM 4481 C CB  . SER C 3 146 ? 17.907  -76.134 -106.372 1.000 233.001 ? 477 SER EEE CB  1 
ATOM 4482 O OG  . SER C 3 146 ? 17.590  -75.594 -107.635 1.000 235.591 ? 477 SER EEE OG  1 
ATOM 4483 N N   . THR C 3 147 ? 21.214  -76.704 -107.613 1.000 227.567 ? 478 THR EEE N   1 
ATOM 4484 C CA  . THR C 3 147 ? 22.072  -77.678 -108.358 1.000 231.356 ? 478 THR EEE CA  1 
ATOM 4485 C C   . THR C 3 147 ? 23.421  -77.830 -107.667 1.000 217.397 ? 478 THR EEE C   1 
ATOM 4486 O O   . THR C 3 147 ? 24.025  -76.835 -107.300 1.000 211.415 ? 478 THR EEE O   1 
ATOM 4487 C CB  . THR C 3 147 ? 22.282  -77.283 -109.827 1.000 242.294 ? 478 THR EEE CB  1 
ATOM 4488 O OG1 . THR C 3 147 ? 20.984  -77.216 -110.416 1.000 259.133 ? 478 THR EEE OG1 1 
ATOM 4489 C CG2 . THR C 3 147 ? 23.121  -78.260 -110.626 1.000 243.605 ? 478 THR EEE CG2 1 
ATOM 4490 N N   . PRO C 3 148 ? 23.937  -79.069 -107.477 1.000 218.078 ? 479 PRO EEE N   1 
ATOM 4491 C CA  . PRO C 3 148 ? 25.264  -79.293 -106.906 1.000 216.764 ? 479 PRO EEE CA  1 
ATOM 4492 C C   . PRO C 3 148 ? 26.367  -78.818 -107.859 1.000 220.810 ? 479 PRO EEE C   1 
ATOM 4493 O O   . PRO C 3 148 ? 26.213  -79.004 -109.041 1.000 234.123 ? 479 PRO EEE O   1 
ATOM 4494 C CB  . PRO C 3 148 ? 25.340  -80.819 -106.713 1.000 215.018 ? 479 PRO EEE CB  1 
ATOM 4495 C CG  . PRO C 3 148 ? 23.902  -81.259 -106.755 1.000 219.883 ? 479 PRO EEE CG  1 
ATOM 4496 C CD  . PRO C 3 148 ? 23.284  -80.345 -107.795 1.000 229.584 ? 479 PRO EEE CD  1 
ATOM 4497 N N   . CYS C 3 149 ? 27.442  -78.239 -107.315 1.000 225.249 ? 480 CYS EEE N   1 
ATOM 4498 C CA  . CYS C 3 149 ? 28.545  -77.594 -108.079 1.000 237.933 ? 480 CYS EEE CA  1 
ATOM 4499 C C   . CYS C 3 149 ? 29.681  -78.592 -108.359 1.000 251.881 ? 480 CYS EEE C   1 
ATOM 4500 O O   . CYS C 3 149 ? 30.259  -78.503 -109.474 1.000 257.809 ? 480 CYS EEE O   1 
ATOM 4501 C CB  . CYS C 3 149 ? 29.091  -76.372 -107.348 1.000 231.480 ? 480 CYS EEE CB  1 
ATOM 4502 S SG  . CYS C 3 149 ? 27.829  -75.143 -106.925 1.000 232.427 ? 480 CYS EEE SG  1 
ATOM 4503 N N   . ASN C 3 150 ? 30.017  -79.462 -107.393 1.000 254.187 ? 481 ASN EEE N   1 
ATOM 4504 C CA  . ASN C 3 150 ? 31.134  -80.449 -107.484 1.000 251.657 ? 481 ASN EEE CA  1 
ATOM 4505 C C   . ASN C 3 150 ? 32.381  -79.782 -108.082 1.000 259.190 ? 481 ASN EEE C   1 
ATOM 4506 O O   . ASN C 3 150 ? 32.981  -80.329 -109.039 1.000 254.369 ? 481 ASN EEE O   1 
ATOM 4507 C CB  . ASN C 3 150 ? 30.692  -81.702 -108.232 1.000 245.040 ? 481 ASN EEE CB  1 
ATOM 4508 C CG  . ASN C 3 150 ? 29.523  -82.345 -107.525 1.000 243.802 ? 481 ASN EEE CG  1 
ATOM 4509 O OD1 . ASN C 3 150 ? 29.415  -82.248 -106.301 1.000 232.763 ? 481 ASN EEE OD1 1 
ATOM 4510 N ND2 . ASN C 3 150 ? 28.636  -82.968 -108.282 1.000 247.207 ? 481 ASN EEE ND2 1 
ATOM 4511 N N   . GLY C 3 151 ? 32.758  -78.635 -107.514 1.000 269.274 ? 482 GLY EEE N   1 
ATOM 4512 C CA  . GLY C 3 151 ? 34.040  -77.959 -107.777 1.000 271.181 ? 482 GLY EEE CA  1 
ATOM 4513 C C   . GLY C 3 151 ? 34.054  -77.211 -109.098 1.000 273.688 ? 482 GLY EEE C   1 
ATOM 4514 O O   . GLY C 3 151 ? 35.164  -76.899 -109.564 1.000 272.379 ? 482 GLY EEE O   1 
ATOM 4515 N N   . VAL C 3 152 ? 32.889  -76.913 -109.685 1.000 276.868 ? 483 VAL EEE N   1 
ATOM 4516 C CA  . VAL C 3 152 ? 32.800  -76.067 -110.915 1.000 278.235 ? 483 VAL EEE CA  1 
ATOM 4517 C C   . VAL C 3 152 ? 31.919  -74.844 -110.639 1.000 267.048 ? 483 VAL EEE C   1 
ATOM 4518 O O   . VAL C 3 152 ? 30.753  -75.007 -110.246 1.000 265.587 ? 483 VAL EEE O   1 
ATOM 4519 C CB  . VAL C 3 152 ? 32.301  -76.847 -112.146 1.000 289.867 ? 483 VAL EEE CB  1 
ATOM 4520 C CG1 . VAL C 3 152 ? 32.464  -76.025 -113.420 1.000 292.410 ? 483 VAL EEE CG1 1 
ATOM 4521 C CG2 . VAL C 3 152 ? 33.006  -78.191 -112.286 1.000 299.557 ? 483 VAL EEE CG2 1 
ATOM 4522 N N   . GLU C 3 153 ? 32.468  -73.654 -110.895 1.000 250.273 ? 484 GLU EEE N   1 
ATOM 4523 C CA  . GLU C 3 153 ? 31.760  -72.353 -110.788 1.000 237.534 ? 484 GLU EEE CA  1 
ATOM 4524 C C   . GLU C 3 153 ? 30.784  -72.235 -111.968 1.000 243.634 ? 484 GLU EEE C   1 
ATOM 4525 O O   . GLU C 3 153 ? 31.079  -72.803 -113.044 1.000 258.258 ? 484 GLU EEE O   1 
ATOM 4526 C CB  . GLU C 3 153 ? 32.797  -71.229 -110.706 1.000 233.178 ? 484 GLU EEE CB  1 
ATOM 4527 C CG  . GLU C 3 153 ? 33.725  -71.391 -109.502 1.000 231.680 ? 484 GLU EEE CG  1 
ATOM 4528 C CD  . GLU C 3 153 ? 34.959  -70.499 -109.429 1.000 224.090 ? 484 GLU EEE CD  1 
ATOM 4529 O OE1 . GLU C 3 153 ? 34.780  -69.267 -109.383 1.000 232.380 ? 484 GLU EEE OE1 1 
ATOM 4530 O OE2 . GLU C 3 153 ? 36.105  -71.028 -109.371 1.000 201.557 ? 484 GLU EEE OE2 1 
ATOM 4531 N N   . GLY C 3 154 ? 29.653  -71.550 -111.754 1.000 238.795 ? 485 GLY EEE N   1 
ATOM 4532 C CA  . GLY C 3 154 ? 28.566  -71.325 -112.740 1.000 243.719 ? 485 GLY EEE CA  1 
ATOM 4533 C C   . GLY C 3 154 ? 27.521  -70.334 -112.228 1.000 236.522 ? 485 GLY EEE C   1 
ATOM 4534 O O   . GLY C 3 154 ? 27.799  -69.690 -111.202 1.000 237.483 ? 485 GLY EEE O   1 
ATOM 4535 N N   . PHE C 3 155 ? 26.366  -70.200 -112.898 1.000 236.966 ? 486 PHE EEE N   1 
ATOM 4536 C CA  . PHE C 3 155 ? 25.194  -69.449 -112.369 1.000 233.972 ? 486 PHE EEE CA  1 
ATOM 4537 C C   . PHE C 3 155 ? 24.800  -70.120 -111.054 1.000 231.107 ? 486 PHE EEE C   1 
ATOM 4538 O O   . PHE C 3 155 ? 24.617  -71.357 -111.042 1.000 223.032 ? 486 PHE EEE O   1 
ATOM 4539 C CB  . PHE C 3 155 ? 24.007  -69.409 -113.342 1.000 242.539 ? 486 PHE EEE CB  1 
ATOM 4540 C CG  . PHE C 3 155 ? 24.221  -68.643 -114.629 1.000 246.449 ? 486 PHE EEE CG  1 
ATOM 4541 C CD1 . PHE C 3 155 ? 24.964  -67.467 -114.671 1.000 244.022 ? 486 PHE EEE CD1 1 
ATOM 4542 C CD2 . PHE C 3 155 ? 23.652  -69.090 -115.811 1.000 253.761 ? 486 PHE EEE CD2 1 
ATOM 4543 C CE1 . PHE C 3 155 ? 25.159  -66.784 -115.863 1.000 245.138 ? 486 PHE EEE CE1 1 
ATOM 4544 C CE2 . PHE C 3 155 ? 23.837  -68.401 -117.004 1.000 260.696 ? 486 PHE EEE CE2 1 
ATOM 4545 C CZ  . PHE C 3 155 ? 24.590  -67.249 -117.027 1.000 258.087 ? 486 PHE EEE CZ  1 
ATOM 4546 N N   . ASN C 3 156 ? 24.793  -69.339 -109.969 1.000 241.362 ? 487 ASN EEE N   1 
ATOM 4547 C CA  . ASN C 3 156 ? 24.448  -69.774 -108.585 1.000 239.966 ? 487 ASN EEE CA  1 
ATOM 4548 C C   . ASN C 3 156 ? 25.507  -70.730 -108.007 1.000 231.781 ? 487 ASN EEE C   1 
ATOM 4549 O O   . ASN C 3 156 ? 25.210  -71.356 -106.990 1.000 222.093 ? 487 ASN EEE O   1 
ATOM 4550 C CB  . ASN C 3 156 ? 23.035  -70.366 -108.561 1.000 246.219 ? 487 ASN EEE CB  1 
ATOM 4551 C CG  . ASN C 3 156 ? 21.987  -69.336 -108.928 1.000 249.114 ? 487 ASN EEE CG  1 
ATOM 4552 O OD1 . ASN C 3 156 ? 21.751  -68.418 -108.147 1.000 248.152 ? 487 ASN EEE OD1 1 
ATOM 4553 N ND2 . ASN C 3 156 ? 21.377  -69.457 -110.102 1.000 240.190 ? 487 ASN EEE ND2 1 
ATOM 4554 N N   . CYS C 3 157 ? 26.710  -70.817 -108.586 1.000 239.246 ? 488 CYS EEE N   1 
ATOM 4555 C CA  . CYS C 3 157 ? 27.833  -71.667 -108.084 1.000 242.220 ? 488 CYS EEE CA  1 
ATOM 4556 C C   . CYS C 3 157 ? 29.100  -70.805 -107.985 1.000 241.106 ? 488 CYS EEE C   1 
ATOM 4557 O O   . CYS C 3 157 ? 29.783  -70.639 -109.010 1.000 246.370 ? 488 CYS EEE O   1 
ATOM 4558 C CB  . CYS C 3 157 ? 28.097  -72.873 -108.987 1.000 250.734 ? 488 CYS EEE CB  1 
ATOM 4559 S SG  . CYS C 3 157 ? 27.072  -74.335 -108.649 1.000 254.846 ? 488 CYS EEE SG  1 
ATOM 4560 N N   . TYR C 3 158 ? 29.405  -70.251 -106.809 1.000 226.798 ? 489 TYR EEE N   1 
ATOM 4561 C CA  . TYR C 3 158 ? 30.342  -69.105 -106.682 1.000 211.901 ? 489 TYR EEE CA  1 
ATOM 4562 C C   . TYR C 3 158 ? 31.604  -69.519 -105.925 1.000 206.998 ? 489 TYR EEE C   1 
ATOM 4563 O O   . TYR C 3 158 ? 31.581  -70.516 -105.148 1.000 202.374 ? 489 TYR EEE O   1 
ATOM 4564 C CB  . TYR C 3 158 ? 29.649  -67.926 -105.997 1.000 204.272 ? 489 TYR EEE CB  1 
ATOM 4565 C CG  . TYR C 3 158 ? 28.347  -67.495 -106.624 1.000 205.675 ? 489 TYR EEE CG  1 
ATOM 4566 C CD1 . TYR C 3 158 ? 28.318  -66.998 -107.911 1.000 215.270 ? 489 TYR EEE CD1 1 
ATOM 4567 C CD2 . TYR C 3 158 ? 27.146  -67.569 -105.933 1.000 202.230 ? 489 TYR EEE CD2 1 
ATOM 4568 C CE1 . TYR C 3 158 ? 27.133  -66.585 -108.497 1.000 222.022 ? 489 TYR EEE CE1 1 
ATOM 4569 C CE2 . TYR C 3 158 ? 25.952  -67.167 -106.504 1.000 203.390 ? 489 TYR EEE CE2 1 
ATOM 4570 C CZ  . TYR C 3 158 ? 25.947  -66.674 -107.792 1.000 216.466 ? 489 TYR EEE CZ  1 
ATOM 4571 O OH  . TYR C 3 158 ? 24.783  -66.266 -108.369 1.000 228.641 ? 489 TYR EEE OH  1 
ATOM 4572 N N   . PHE C 3 159 ? 32.686  -68.764 -106.150 1.000 211.282 ? 490 PHE EEE N   1 
ATOM 4573 C CA  . PHE C 3 159 ? 33.877  -68.780 -105.258 1.000 209.422 ? 490 PHE EEE CA  1 
ATOM 4574 C C   . PHE C 3 159 ? 33.459  -68.179 -103.918 1.000 197.981 ? 490 PHE EEE C   1 
ATOM 4575 O O   . PHE C 3 159 ? 32.860  -67.107 -103.915 1.000 194.335 ? 490 PHE EEE O   1 
ATOM 4576 C CB  . PHE C 3 159 ? 35.093  -68.073 -105.867 1.000 206.232 ? 490 PHE EEE CB  1 
ATOM 4577 C CG  . PHE C 3 159 ? 36.372  -68.542 -105.220 1.000 204.002 ? 490 PHE EEE CG  1 
ATOM 4578 C CD1 . PHE C 3 159 ? 36.801  -69.858 -105.368 1.000 200.489 ? 490 PHE EEE CD1 1 
ATOM 4579 C CD2 . PHE C 3 159 ? 37.091  -67.703 -104.381 1.000 206.354 ? 490 PHE EEE CD2 1 
ATOM 4580 C CE1 . PHE C 3 159 ? 37.946  -70.310 -104.734 1.000 201.833 ? 490 PHE EEE CE1 1 
ATOM 4581 C CE2 . PHE C 3 159 ? 38.234  -68.154 -103.738 1.000 204.378 ? 490 PHE EEE CE2 1 
ATOM 4582 C CZ  . PHE C 3 159 ? 38.659  -69.455 -103.917 1.000 210.358 ? 490 PHE EEE CZ  1 
ATOM 4583 N N   . PRO C 3 160 ? 33.734  -68.846 -102.765 1.000 184.950 ? 491 PRO EEE N   1 
ATOM 4584 C CA  . PRO C 3 160 ? 33.299  -68.341 -101.457 1.000 178.916 ? 491 PRO EEE CA  1 
ATOM 4585 C C   . PRO C 3 160 ? 33.958  -67.052 -100.917 1.000 169.065 ? 491 PRO EEE C   1 
ATOM 4586 O O   . PRO C 3 160 ? 33.366  -66.457 -100.061 1.000 160.124 ? 491 PRO EEE O   1 
ATOM 4587 C CB  . PRO C 3 160 ? 33.596  -69.537 -100.529 1.000 176.368 ? 491 PRO EEE CB  1 
ATOM 4588 C CG  . PRO C 3 160 ? 34.743  -70.270 -101.184 1.000 174.563 ? 491 PRO EEE CG  1 
ATOM 4589 C CD  . PRO C 3 160 ? 34.465  -70.124 -102.660 1.000 178.133 ? 491 PRO EEE CD  1 
ATOM 4590 N N   . LEU C 3 161 ? 35.126  -66.636 -101.416 1.000 167.576 ? 492 LEU EEE N   1 
ATOM 4591 C CA  . LEU C 3 161 ? 35.881  -65.438 -100.938 1.000 169.679 ? 492 LEU EEE CA  1 
ATOM 4592 C C   . LEU C 3 161 ? 35.722  -64.262 -101.919 1.000 173.516 ? 492 LEU EEE C   1 
ATOM 4593 O O   . LEU C 3 161 ? 35.457  -64.523 -103.084 1.000 189.289 ? 492 LEU EEE O   1 
ATOM 4594 C CB  . LEU C 3 161 ? 37.353  -65.841 -100.795 1.000 171.556 ? 492 LEU EEE CB  1 
ATOM 4595 C CG  . LEU C 3 161 ? 37.600  -67.111 -99.980  1.000 173.553 ? 492 LEU EEE CG  1 
ATOM 4596 C CD1 . LEU C 3 161 ? 39.085  -67.399 -99.829  1.000 172.670 ? 492 LEU EEE CD1 1 
ATOM 4597 C CD2 . LEU C 3 161 ? 36.965  -67.002 -98.605  1.000 178.857 ? 492 LEU EEE CD2 1 
ATOM 4598 N N   . GLN C 3 162 ? 35.917  -63.015 -101.473 1.000 168.733 ? 493 GLN EEE N   1 
ATOM 4599 C CA  . GLN C 3 162 ? 35.858  -61.779 -102.309 1.000 168.679 ? 493 GLN EEE CA  1 
ATOM 4600 C C   . GLN C 3 162 ? 36.887  -60.770 -101.774 1.000 169.481 ? 493 GLN EEE C   1 
ATOM 4601 O O   . GLN C 3 162 ? 37.055  -60.712 -100.532 1.000 192.836 ? 493 GLN EEE O   1 
ATOM 4602 C CB  . GLN C 3 162 ? 34.433  -61.202 -102.304 1.000 166.805 ? 493 GLN EEE CB  1 
ATOM 4603 C CG  . GLN C 3 162 ? 34.297  -59.800 -102.915 1.000 173.108 ? 493 GLN EEE CG  1 
ATOM 4604 C CD  . GLN C 3 162 ? 34.479  -59.711 -104.422 1.000 183.858 ? 493 GLN EEE CD  1 
ATOM 4605 O OE1 . GLN C 3 162 ? 33.806  -60.385 -105.202 1.000 186.446 ? 493 GLN EEE OE1 1 
ATOM 4606 N NE2 . GLN C 3 162 ? 35.359  -58.827 -104.875 1.000 182.563 ? 493 GLN EEE NE2 1 
ATOM 4607 N N   . SER C 3 163 ? 37.551  -60.009 -102.656 1.000 168.693 ? 494 SER EEE N   1 
ATOM 4608 C CA  . SER C 3 163 ? 38.409  -58.841 -102.304 1.000 168.489 ? 494 SER EEE CA  1 
ATOM 4609 C C   . SER C 3 163 ? 37.574  -57.649 -101.825 1.000 173.166 ? 494 SER EEE C   1 
ATOM 4610 O O   . SER C 3 163 ? 36.628  -57.243 -102.528 1.000 162.789 ? 494 SER EEE O   1 
ATOM 4611 C CB  . SER C 3 163 ? 39.272  -58.406 -103.445 1.000 166.685 ? 494 SER EEE CB  1 
ATOM 4612 O OG  . SER C 3 163 ? 40.263  -59.380 -103.700 1.000 165.391 ? 494 SER EEE OG  1 
ATOM 4613 N N   . TYR C 3 164 ? 37.948  -57.095 -100.671 1.000 182.465 ? 495 TYR EEE N   1 
ATOM 4614 C CA  . TYR C 3 164 ? 37.693  -55.678 -100.317 1.000 190.627 ? 495 TYR EEE CA  1 
ATOM 4615 C C   . TYR C 3 164 ? 38.375  -54.791 -101.361 1.000 193.836 ? 495 TYR EEE C   1 
ATOM 4616 O O   . TYR C 3 164 ? 39.409  -55.207 -101.918 1.000 195.550 ? 495 TYR EEE O   1 
ATOM 4617 C CB  . TYR C 3 164 ? 38.292  -55.321 -98.958  1.000 194.234 ? 495 TYR EEE CB  1 
ATOM 4618 C CG  . TYR C 3 164 ? 37.590  -55.898 -97.757  1.000 195.741 ? 495 TYR EEE CG  1 
ATOM 4619 C CD1 . TYR C 3 164 ? 36.313  -55.486 -97.408  1.000 193.924 ? 495 TYR EEE CD1 1 
ATOM 4620 C CD2 . TYR C 3 164 ? 38.230  -56.818 -96.941  1.000 198.417 ? 495 TYR EEE CD2 1 
ATOM 4621 C CE1 . TYR C 3 164 ? 35.678  -55.988 -96.287  1.000 190.880 ? 495 TYR EEE CE1 1 
ATOM 4622 C CE2 . TYR C 3 164 ? 37.608  -57.333 -95.819  1.000 198.449 ? 495 TYR EEE CE2 1 
ATOM 4623 C CZ  . TYR C 3 164 ? 36.326  -56.922 -95.497  1.000 199.030 ? 495 TYR EEE CZ  1 
ATOM 4624 O OH  . TYR C 3 164 ? 35.718  -57.436 -94.387  1.000 211.140 ? 495 TYR EEE OH  1 
ATOM 4625 N N   . GLY C 3 165 ? 37.844  -53.588 -101.574 1.000 184.245 ? 496 GLY EEE N   1 
ATOM 4626 C CA  . GLY C 3 165 ? 38.430  -52.589 -102.486 1.000 181.848 ? 496 GLY EEE CA  1 
ATOM 4627 C C   . GLY C 3 165 ? 38.771  -51.312 -101.755 1.000 178.433 ? 496 GLY EEE C   1 
ATOM 4628 O O   . GLY C 3 165 ? 37.886  -50.462 -101.610 1.000 174.566 ? 496 GLY EEE O   1 
ATOM 4629 N N   . PHE C 3 166 ? 40.017  -51.175 -101.315 1.000 181.158 ? 497 PHE EEE N   1 
ATOM 4630 C CA  . PHE C 3 166 ? 40.463  -50.055 -100.446 1.000 182.725 ? 497 PHE EEE CA  1 
ATOM 4631 C C   . PHE C 3 166 ? 41.172  -48.997 -101.281 1.000 175.674 ? 497 PHE EEE C   1 
ATOM 4632 O O   . PHE C 3 166 ? 42.280  -49.258 -101.756 1.000 165.199 ? 497 PHE EEE O   1 
ATOM 4633 C CB  . PHE C 3 166 ? 41.363  -50.581 -99.329  1.000 185.596 ? 497 PHE EEE CB  1 
ATOM 4634 C CG  . PHE C 3 166 ? 40.649  -51.498 -98.370  1.000 181.321 ? 497 PHE EEE CG  1 
ATOM 4635 C CD1 . PHE C 3 166 ? 39.443  -51.115 -97.797  1.000 174.605 ? 497 PHE EEE CD1 1 
ATOM 4636 C CD2 . PHE C 3 166 ? 41.177  -52.740 -98.051  1.000 176.541 ? 497 PHE EEE CD2 1 
ATOM 4637 C CE1 . PHE C 3 166 ? 38.793  -51.946 -96.900  1.000 170.955 ? 497 PHE EEE CE1 1 
ATOM 4638 C CE2 . PHE C 3 166 ? 40.520  -53.572 -97.161  1.000 173.756 ? 497 PHE EEE CE2 1 
ATOM 4639 C CZ  . PHE C 3 166 ? 39.336  -53.170 -96.583  1.000 171.527 ? 497 PHE EEE CZ  1 
ATOM 4640 N N   . GLN C 3 167 ? 40.513  -47.857 -101.452 1.000 175.378 ? 498 GLN EEE N   1 
ATOM 4641 C CA  . GLN C 3 167 ? 41.064  -46.654 -102.113 1.000 182.253 ? 498 GLN EEE CA  1 
ATOM 4642 C C   . GLN C 3 167 ? 41.074  -45.519 -101.109 1.000 179.764 ? 498 GLN EEE C   1 
ATOM 4643 O O   . GLN C 3 167 ? 40.176  -45.424 -100.279 1.000 177.046 ? 498 GLN EEE O   1 
ATOM 4644 C CB  . GLN C 3 167 ? 40.164  -46.148 -103.230 1.000 187.671 ? 498 GLN EEE CB  1 
ATOM 4645 C CG  . GLN C 3 167 ? 40.149  -46.985 -104.487 1.000 191.127 ? 498 GLN EEE CG  1 
ATOM 4646 C CD  . GLN C 3 167 ? 39.287  -46.258 -105.485 1.000 200.404 ? 498 GLN EEE CD  1 
ATOM 4647 O OE1 . GLN C 3 167 ? 38.130  -46.606 -105.682 1.000 205.440 ? 498 GLN EEE OE1 1 
ATOM 4648 N NE2 . GLN C 3 167 ? 39.813  -45.188 -106.070 1.000 212.081 ? 498 GLN EEE NE2 1 
ATOM 4649 N N   . PRO C 3 168 ? 42.065  -44.614 -101.189 1.000 183.960 ? 499 PRO EEE N   1 
ATOM 4650 C CA  . PRO C 3 168 ? 42.176  -43.508 -100.240 1.000 190.930 ? 499 PRO EEE CA  1 
ATOM 4651 C C   . PRO C 3 168 ? 40.960  -42.563 -100.187 1.000 191.792 ? 499 PRO EEE C   1 
ATOM 4652 O O   . PRO C 3 168 ? 40.744  -41.971 -99.136  1.000 193.828 ? 499 PRO EEE O   1 
ATOM 4653 C CB  . PRO C 3 168 ? 43.427  -42.753 -100.725 1.000 197.491 ? 499 PRO EEE CB  1 
ATOM 4654 C CG  . PRO C 3 168 ? 43.602  -43.172 -102.173 1.000 196.673 ? 499 PRO EEE CG  1 
ATOM 4655 C CD  . PRO C 3 168 ? 43.126  -44.605 -102.203 1.000 188.887 ? 499 PRO EEE CD  1 
ATOM 4656 N N   . THR C 3 169 ? 40.202  -42.437 -101.281 1.000 192.197 ? 500 THR EEE N   1 
ATOM 4657 C CA  . THR C 3 169 ? 39.047  -41.498 -101.375 1.000 194.500 ? 500 THR EEE CA  1 
ATOM 4658 C C   . THR C 3 169 ? 37.796  -42.166 -100.777 1.000 191.395 ? 500 THR EEE C   1 
ATOM 4659 O O   . THR C 3 169 ? 36.819  -41.426 -100.508 1.000 178.233 ? 500 THR EEE O   1 
ATOM 4660 C CB  . THR C 3 169 ? 38.846  -40.931 -102.800 1.000 196.328 ? 500 THR EEE CB  1 
ATOM 4661 O OG1 . THR C 3 169 ? 38.494  -41.915 -103.778 1.000 193.924 ? 500 THR EEE OG1 1 
ATOM 4662 C CG2 . THR C 3 169 ? 40.072  -40.203 -103.304 1.000 194.931 ? 500 THR EEE CG2 1 
ATOM 4663 N N   . ASN C 3 170 ? 37.822  -43.489 -100.557 1.000 197.485 ? 501 ASN EEE N   1 
ATOM 4664 C CA  . ASN C 3 170 ? 36.667  -44.268 -100.028 1.000 206.909 ? 501 ASN EEE CA  1 
ATOM 4665 C C   . ASN C 3 170 ? 36.041  -43.547 -98.832  1.000 208.602 ? 501 ASN EEE C   1 
ATOM 4666 O O   . ASN C 3 170 ? 36.804  -42.953 -98.029  1.000 203.367 ? 501 ASN EEE O   1 
ATOM 4667 C CB  . ASN C 3 170 ? 37.036  -45.672 -99.536  1.000 205.333 ? 501 ASN EEE CB  1 
ATOM 4668 C CG  . ASN C 3 170 ? 37.163  -46.691 -100.641 1.000 205.680 ? 501 ASN EEE CG  1 
ATOM 4669 O OD1 . ASN C 3 170 ? 36.866  -46.403 -101.794 1.000 214.730 ? 501 ASN EEE OD1 1 
ATOM 4670 N ND2 . ASN C 3 170 ? 37.618  -47.883 -100.294 1.000 195.031 ? 501 ASN EEE ND2 1 
ATOM 4671 N N   . GLY C 3 171 ? 34.709  -43.645 -98.719  1.000 211.922 ? 502 GLY EEE N   1 
ATOM 4672 C CA  . GLY C 3 171 ? 33.941  -43.311 -97.508  1.000 203.084 ? 502 GLY EEE CA  1 
ATOM 4673 C C   . GLY C 3 171 ? 34.513  -44.075 -96.343  1.000 193.591 ? 502 GLY EEE C   1 
ATOM 4674 O O   . GLY C 3 171 ? 35.013  -45.193 -96.572  1.000 187.475 ? 502 GLY EEE O   1 
ATOM 4675 N N   . VAL C 3 172 ? 34.486  -43.494 -95.146  1.000 196.939 ? 503 VAL EEE N   1 
ATOM 4676 C CA  . VAL C 3 172 ? 35.197  -44.076 -93.971  1.000 186.954 ? 503 VAL EEE CA  1 
ATOM 4677 C C   . VAL C 3 172 ? 34.642  -45.488 -93.757  1.000 178.539 ? 503 VAL EEE C   1 
ATOM 4678 O O   . VAL C 3 172 ? 35.425  -46.374 -93.379  1.000 180.875 ? 503 VAL EEE O   1 
ATOM 4679 C CB  . VAL C 3 172 ? 35.088  -43.180 -92.721  1.000 188.465 ? 503 VAL EEE CB  1 
ATOM 4680 C CG1 . VAL C 3 172 ? 33.674  -43.124 -92.147  1.000 190.628 ? 503 VAL EEE CG1 1 
ATOM 4681 C CG2 . VAL C 3 172 ? 36.096  -43.607 -91.662  1.000 189.737 ? 503 VAL EEE CG2 1 
ATOM 4682 N N   . GLY C 3 173 ? 33.354  -45.692 -94.047  1.000 177.858 ? 504 GLY EEE N   1 
ATOM 4683 C CA  . GLY C 3 173 ? 32.668  -46.992 -93.921  1.000 179.449 ? 504 GLY EEE CA  1 
ATOM 4684 C C   . GLY C 3 173 ? 33.364  -48.097 -94.697  1.000 182.950 ? 504 GLY EEE C   1 
ATOM 4685 O O   . GLY C 3 173 ? 33.232  -49.273 -94.304  1.000 177.208 ? 504 GLY EEE O   1 
ATOM 4686 N N   . TYR C 3 174 ? 34.073  -47.725 -95.764  1.000 194.233 ? 505 TYR EEE N   1 
ATOM 4687 C CA  . TYR C 3 174 ? 34.681  -48.635 -96.766  1.000 197.205 ? 505 TYR EEE CA  1 
ATOM 4688 C C   . TYR C 3 174 ? 36.206  -48.518 -96.732  1.000 193.691 ? 505 TYR EEE C   1 
ATOM 4689 O O   . TYR C 3 174 ? 36.871  -49.099 -97.614  1.000 196.203 ? 505 TYR EEE O   1 
ATOM 4690 C CB  . TYR C 3 174 ? 34.112  -48.300 -98.146  1.000 206.223 ? 505 TYR EEE CB  1 
ATOM 4691 C CG  . TYR C 3 174 ? 32.665  -48.691 -98.317  1.000 208.620 ? 505 TYR EEE CG  1 
ATOM 4692 C CD1 . TYR C 3 174 ? 31.626  -47.819 -98.008  1.000 203.072 ? 505 TYR EEE CD1 1 
ATOM 4693 C CD2 . TYR C 3 174 ? 32.338  -49.956 -98.780  1.000 209.970 ? 505 TYR EEE CD2 1 
ATOM 4694 C CE1 . TYR C 3 174 ? 30.300  -48.193 -98.169  1.000 203.009 ? 505 TYR EEE CE1 1 
ATOM 4695 C CE2 . TYR C 3 174 ? 31.018  -50.343 -98.949  1.000 214.900 ? 505 TYR EEE CE2 1 
ATOM 4696 C CZ  . TYR C 3 174 ? 29.994  -49.465 -98.632  1.000 211.187 ? 505 TYR EEE CZ  1 
ATOM 4697 O OH  . TYR C 3 174 ? 28.698  -49.862 -98.809  1.000 213.586 ? 505 TYR EEE OH  1 
ATOM 4698 N N   . GLN C 3 175 ? 36.749  -47.787 -95.756  1.000 185.434 ? 506 GLN EEE N   1 
ATOM 4699 C CA  . GLN C 3 175 ? 38.216  -47.690 -95.543  1.000 174.797 ? 506 GLN EEE CA  1 
ATOM 4700 C C   . GLN C 3 175 ? 38.654  -48.897 -94.721  1.000 162.020 ? 506 GLN EEE C   1 
ATOM 4701 O O   . GLN C 3 175 ? 37.878  -49.484 -93.969  1.000 167.120 ? 506 GLN EEE O   1 
ATOM 4702 C CB  . GLN C 3 175 ? 38.593  -46.352 -94.909  1.000 171.227 ? 506 GLN EEE CB  1 
ATOM 4703 C CG  . GLN C 3 175 ? 38.676  -45.230 -95.924  1.000 178.084 ? 506 GLN EEE CG  1 
ATOM 4704 C CD  . GLN C 3 175 ? 38.923  -43.890 -95.284  1.000 185.235 ? 506 GLN EEE CD  1 
ATOM 4705 O OE1 . GLN C 3 175 ? 39.490  -43.786 -94.197  1.000 189.930 ? 506 GLN EEE OE1 1 
ATOM 4706 N NE2 . GLN C 3 175 ? 38.484  -42.847 -95.965  1.000 194.595 ? 506 GLN EEE NE2 1 
ATOM 4707 N N   . PRO C 3 176 ? 39.923  -49.310 -94.861  1.000 159.117 ? 507 PRO EEE N   1 
ATOM 4708 C CA  . PRO C 3 176 ? 40.452  -50.449 -94.120  1.000 165.773 ? 507 PRO EEE CA  1 
ATOM 4709 C C   . PRO C 3 176 ? 40.711  -50.100 -92.650  1.000 175.351 ? 507 PRO EEE C   1 
ATOM 4710 O O   . PRO C 3 176 ? 41.189  -48.998 -92.362  1.000 177.126 ? 507 PRO EEE O   1 
ATOM 4711 C CB  . PRO C 3 176 ? 41.779  -50.748 -94.826  1.000 171.053 ? 507 PRO EEE CB  1 
ATOM 4712 C CG  . PRO C 3 176 ? 42.199  -49.410 -95.409  1.000 172.544 ? 507 PRO EEE CG  1 
ATOM 4713 C CD  . PRO C 3 176 ? 40.912  -48.693 -95.747  1.000 170.008 ? 507 PRO EEE CD  1 
ATOM 4714 N N   . TYR C 3 177 ? 40.351  -51.027 -91.762  1.000 173.702 ? 508 TYR EEE N   1 
ATOM 4715 C CA  . TYR C 3 177 ? 40.624  -50.943 -90.307  1.000 169.182 ? 508 TYR EEE CA  1 
ATOM 4716 C C   . TYR C 3 177 ? 41.471  -52.163 -89.944  1.000 166.293 ? 508 TYR EEE C   1 
ATOM 4717 O O   . TYR C 3 177 ? 41.169  -53.266 -90.438  1.000 156.893 ? 508 TYR EEE O   1 
ATOM 4718 C CB  . TYR C 3 177 ? 39.314  -50.756 -89.531  1.000 157.418 ? 508 TYR EEE CB  1 
ATOM 4719 C CG  . TYR C 3 177 ? 38.847  -49.325 -89.539  1.000 153.401 ? 508 TYR EEE CG  1 
ATOM 4720 C CD1 . TYR C 3 177 ? 38.380  -48.729 -90.693  1.000 164.690 ? 508 TYR EEE CD1 1 
ATOM 4721 C CD2 . TYR C 3 177 ? 38.967  -48.524 -88.426  1.000 146.306 ? 508 TYR EEE CD2 1 
ATOM 4722 C CE1 . TYR C 3 177 ? 37.994  -47.396 -90.724  1.000 168.734 ? 508 TYR EEE CE1 1 
ATOM 4723 C CE2 . TYR C 3 177 ? 38.579  -47.192 -88.435  1.000 155.140 ? 508 TYR EEE CE2 1 
ATOM 4724 C CZ  . TYR C 3 177 ? 38.085  -46.616 -89.589  1.000 161.052 ? 508 TYR EEE CZ  1 
ATOM 4725 O OH  . TYR C 3 177 ? 37.711  -45.298 -89.622  1.000 155.302 ? 508 TYR EEE OH  1 
ATOM 4726 N N   . ARG C 3 178 ? 42.551  -51.946 -89.190  1.000 162.016 ? 509 ARG EEE N   1 
ATOM 4727 C CA  . ARG C 3 178 ? 43.278  -53.044 -88.514  1.000 152.234 ? 509 ARG EEE CA  1 
ATOM 4728 C C   . ARG C 3 178 ? 42.606  -53.275 -87.166  1.000 150.940 ? 509 ARG EEE C   1 
ATOM 4729 O O   . ARG C 3 178 ? 42.207  -52.302 -86.510  1.000 152.887 ? 509 ARG EEE O   1 
ATOM 4730 C CB  . ARG C 3 178 ? 44.764  -52.736 -88.395  1.000 146.937 ? 509 ARG EEE CB  1 
ATOM 4731 C CG  . ARG C 3 178 ? 45.456  -52.873 -89.734  1.000 155.096 ? 509 ARG EEE CG  1 
ATOM 4732 C CD  . ARG C 3 178 ? 46.908  -52.482 -89.714  1.000 163.124 ? 509 ARG EEE CD  1 
ATOM 4733 N NE  . ARG C 3 178 ? 47.458  -52.683 -91.044  1.000 172.220 ? 509 ARG EEE NE  1 
ATOM 4734 C CZ  . ARG C 3 178 ? 48.742  -52.864 -91.323  1.000 180.541 ? 509 ARG EEE CZ  1 
ATOM 4735 N NH1 . ARG C 3 178 ? 49.644  -52.850 -90.359  1.000 180.329 ? 509 ARG EEE NH1 1 
ATOM 4736 N NH2 . ARG C 3 178 ? 49.129  -53.057 -92.571  1.000 197.904 ? 509 ARG EEE NH2 1 
ATOM 4737 N N   . VAL C 3 179 ? 42.453  -54.542 -86.812  1.000 145.162 ? 510 VAL EEE N   1 
ATOM 4738 C CA  . VAL C 3 179 ? 41.748  -55.011 -85.596  1.000 133.546 ? 510 VAL EEE CA  1 
ATOM 4739 C C   . VAL C 3 179 ? 42.722  -55.921 -84.859  1.000 141.886 ? 510 VAL EEE C   1 
ATOM 4740 O O   . VAL C 3 179 ? 43.371  -56.792 -85.511  1.000 139.206 ? 510 VAL EEE O   1 
ATOM 4741 C CB  . VAL C 3 179 ? 40.455  -55.759 -85.962  1.000 133.941 ? 510 VAL EEE CB  1 
ATOM 4742 C CG1 . VAL C 3 179 ? 39.696  -56.236 -84.744  1.000 134.444 ? 510 VAL EEE CG1 1 
ATOM 4743 C CG2 . VAL C 3 179 ? 39.550  -54.911 -86.833  1.000 146.122 ? 510 VAL EEE CG2 1 
ATOM 4744 N N   . VAL C 3 180 ? 42.831  -55.727 -83.544  1.000 148.622 ? 511 VAL EEE N   1 
ATOM 4745 C CA  . VAL C 3 180 ? 43.366  -56.778 -82.637  1.000 141.114 ? 511 VAL EEE CA  1 
ATOM 4746 C C   . VAL C 3 180 ? 42.312  -57.113 -81.585  1.000 135.373 ? 511 VAL EEE C   1 
ATOM 4747 O O   . VAL C 3 180 ? 41.713  -56.152 -81.034  1.000 137.726 ? 511 VAL EEE O   1 
ATOM 4748 C CB  . VAL C 3 180 ? 44.689  -56.342 -82.007  1.000 143.618 ? 511 VAL EEE CB  1 
ATOM 4749 C CG1 . VAL C 3 180 ? 45.230  -57.445 -81.110  1.000 145.083 ? 511 VAL EEE CG1 1 
ATOM 4750 C CG2 . VAL C 3 180 ? 45.690  -55.959 -83.086  1.000 151.768 ? 511 VAL EEE CG2 1 
ATOM 4751 N N   . VAL C 3 181 ? 42.106  -58.418 -81.353  1.000 130.880 ? 512 VAL EEE N   1 
ATOM 4752 C CA  . VAL C 3 181 ? 41.259  -58.986 -80.262  1.000 134.252 ? 512 VAL EEE CA  1 
ATOM 4753 C C   . VAL C 3 181 ? 42.165  -59.693 -79.245  1.000 142.659 ? 512 VAL EEE C   1 
ATOM 4754 O O   . VAL C 3 181 ? 42.871  -60.631 -79.653  1.000 154.325 ? 512 VAL EEE O   1 
ATOM 4755 C CB  . VAL C 3 181 ? 40.208  -59.956 -80.820  1.000 135.862 ? 512 VAL EEE CB  1 
ATOM 4756 C CG1 . VAL C 3 181 ? 39.358  -60.542 -79.710  1.000 133.504 ? 512 VAL EEE CG1 1 
ATOM 4757 C CG2 . VAL C 3 181 ? 39.336  -59.286 -81.870  1.000 140.665 ? 512 VAL EEE CG2 1 
ATOM 4758 N N   . LEU C 3 182 ? 42.149  -59.257 -77.975  1.000 139.433 ? 513 LEU EEE N   1 
ATOM 4759 C CA  . LEU C 3 182 ? 42.875  -59.900 -76.845  1.000 130.137 ? 513 LEU EEE CA  1 
ATOM 4760 C C   . LEU C 3 182 ? 41.898  -60.768 -76.048  1.000 130.725 ? 513 LEU EEE C   1 
ATOM 4761 O O   . LEU C 3 182 ? 40.920  -60.218 -75.533  1.000 127.744 ? 513 LEU EEE O   1 
ATOM 4762 C CB  . LEU C 3 182 ? 43.453  -58.813 -75.945  1.000 131.392 ? 513 LEU EEE CB  1 
ATOM 4763 C CG  . LEU C 3 182 ? 44.387  -57.823 -76.623  1.000 138.453 ? 513 LEU EEE CG  1 
ATOM 4764 C CD1 . LEU C 3 182 ? 44.874  -56.789 -75.619  1.000 141.212 ? 513 LEU EEE CD1 1 
ATOM 4765 C CD2 . LEU C 3 182 ? 45.553  -58.553 -77.271  1.000 142.106 ? 513 LEU EEE CD2 1 
ATOM 4766 N N   . SER C 3 183 ? 42.149  -62.072 -75.955  1.000 139.512 ? 514 SER EEE N   1 
ATOM 4767 C CA  . SER C 3 183 ? 41.417  -63.026 -75.080  1.000 147.980 ? 514 SER EEE CA  1 
ATOM 4768 C C   . SER C 3 183 ? 42.292  -63.383 -73.868  1.000 160.900 ? 514 SER EEE C   1 
ATOM 4769 O O   . SER C 3 183 ? 43.537  -63.527 -74.048  1.000 172.401 ? 514 SER EEE O   1 
ATOM 4770 C CB  . SER C 3 183 ? 41.020  -64.269 -75.838  1.000 152.432 ? 514 SER EEE CB  1 
ATOM 4771 O OG  . SER C 3 183 ? 40.204  -63.940 -76.941  1.000 148.396 ? 514 SER EEE OG  1 
ATOM 4772 N N   . PHE C 3 184 ? 41.677  -63.546 -72.690  1.000 152.626 ? 515 PHE EEE N   1 
ATOM 4773 C CA  . PHE C 3 184 ? 42.390  -63.868 -71.432  1.000 146.295 ? 515 PHE EEE CA  1 
ATOM 4774 C C   . PHE C 3 184 ? 41.969  -65.244 -70.917  1.000 158.303 ? 515 PHE EEE C   1 
ATOM 4775 O O   . PHE C 3 184 ? 40.787  -65.580 -70.857  1.000 159.958 ? 515 PHE EEE O   1 
ATOM 4776 C CB  . PHE C 3 184 ? 42.179  -62.756 -70.420  1.000 134.935 ? 515 PHE EEE CB  1 
ATOM 4777 C CG  . PHE C 3 184 ? 42.680  -61.429 -70.912  1.000 120.026 ? 515 PHE EEE CG  1 
ATOM 4778 C CD1 . PHE C 3 184 ? 41.829  -60.587 -71.581  1.000 114.985 ? 515 PHE EEE CD1 1 
ATOM 4779 C CD2 . PHE C 3 184 ? 43.992  -61.032 -70.713  1.000 117.871 ? 515 PHE EEE CD2 1 
ATOM 4780 C CE1 . PHE C 3 184 ? 42.266  -59.347 -72.011  1.000 113.743 ? 515 PHE EEE CE1 1 
ATOM 4781 C CE2 . PHE C 3 184 ? 44.432  -59.792 -71.143  1.000 116.211 ? 515 PHE EEE CE2 1 
ATOM 4782 C CZ  . PHE C 3 184 ? 43.564  -58.959 -71.799  1.000 115.656 ? 515 PHE EEE CZ  1 
ATOM 4783 N N   . GLU C 3 185 ? 42.974  -66.029 -70.559  1.000 167.432 ? 516 GLU EEE N   1 
ATOM 4784 C CA  . GLU C 3 185 ? 42.843  -67.449 -70.182  1.000 175.607 ? 516 GLU EEE CA  1 
ATOM 4785 C C   . GLU C 3 185 ? 43.511  -67.580 -68.813  1.000 176.811 ? 516 GLU EEE C   1 
ATOM 4786 O O   . GLU C 3 185 ? 44.657  -67.095 -68.629  1.000 179.250 ? 516 GLU EEE O   1 
ATOM 4787 C CB  . GLU C 3 185 ? 43.431  -68.291 -71.325  1.000 192.498 ? 516 GLU EEE CB  1 
ATOM 4788 C CG  . GLU C 3 185 ? 43.577  -69.771 -71.027  1.000 207.939 ? 516 GLU EEE CG  1 
ATOM 4789 C CD  . GLU C 3 185 ? 43.651  -70.675 -72.249  1.000 219.123 ? 516 GLU EEE CD  1 
ATOM 4790 O OE1 . GLU C 3 185 ? 42.647  -70.733 -73.004  1.000 234.148 ? 516 GLU EEE OE1 1 
ATOM 4791 O OE2 . GLU C 3 185 ? 44.675  -71.362 -72.414  1.000 217.676 ? 516 GLU EEE OE2 1 
ATOM 4792 N N   . LEU C 3 186 ? 42.803  -68.174 -67.861  1.000 181.167 ? 517 LEU EEE N   1 
ATOM 4793 C CA  . LEU C 3 186 ? 43.319  -68.383 -66.485  1.000 180.545 ? 517 LEU EEE CA  1 
ATOM 4794 C C   . LEU C 3 186 ? 43.030  -69.815 -66.038  1.000 182.046 ? 517 LEU EEE C   1 
ATOM 4795 O O   . LEU C 3 186 ? 41.984  -70.050 -65.400  1.000 176.920 ? 517 LEU EEE O   1 
ATOM 4796 C CB  . LEU C 3 186 ? 42.670  -67.354 -65.556  1.000 181.393 ? 517 LEU EEE CB  1 
ATOM 4797 C CG  . LEU C 3 186 ? 43.370  -67.135 -64.218  1.000 182.467 ? 517 LEU EEE CG  1 
ATOM 4798 C CD1 . LEU C 3 186 ? 44.858  -66.909 -64.428  1.000 191.926 ? 517 LEU EEE CD1 1 
ATOM 4799 C CD2 . LEU C 3 186 ? 42.757  -65.967 -63.466  1.000 175.724 ? 517 LEU EEE CD2 1 
ATOM 4800 N N   . LEU C 3 187 ? 43.957  -70.721 -66.348  1.000 191.885 ? 518 LEU EEE N   1 
ATOM 4801 C CA  . LEU C 3 187 ? 43.868  -72.165 -66.010  1.000 208.272 ? 518 LEU EEE CA  1 
ATOM 4802 C C   . LEU C 3 187 ? 44.707  -72.458 -64.743  1.000 211.480 ? 518 LEU EEE C   1 
ATOM 4803 O O   . LEU C 3 187 ? 45.248  -71.514 -64.098  1.000 192.277 ? 518 LEU EEE O   1 
ATOM 4804 C CB  . LEU C 3 187 ? 44.326  -72.996 -67.226  1.000 208.741 ? 518 LEU EEE CB  1 
ATOM 4805 C CG  . LEU C 3 187 ? 43.763  -72.630 -68.607  1.000 188.019 ? 518 LEU EEE CG  1 
ATOM 4806 C CD1 . LEU C 3 187 ? 44.385  -73.501 -69.697  1.000 186.300 ? 518 LEU EEE CD1 1 
ATOM 4807 C CD2 . LEU C 3 187 ? 42.253  -72.766 -68.625  1.000 180.409 ? 518 LEU EEE CD2 1 
ATOM 4808 N N   . HIS C 3 188 ? 44.817  -73.741 -64.392  1.000 218.252 ? 519 HIS EEE N   1 
ATOM 4809 C CA  . HIS C 3 188 ? 45.385  -74.238 -63.111  1.000 238.574 ? 519 HIS EEE CA  1 
ATOM 4810 C C   . HIS C 3 188 ? 46.859  -74.603 -63.347  1.000 251.149 ? 519 HIS EEE C   1 
ATOM 4811 O O   . HIS C 3 188 ? 47.344  -75.628 -62.792  1.000 256.218 ? 519 HIS EEE O   1 
ATOM 4812 C CB  . HIS C 3 188 ? 44.443  -75.327 -62.575  1.000 246.867 ? 519 HIS EEE CB  1 
ATOM 4813 C CG  . HIS C 3 188 ? 43.011  -74.898 -62.633  1.000 247.269 ? 519 HIS EEE CG  1 
ATOM 4814 N ND1 . HIS C 3 188 ? 42.398  -74.203 -61.601  1.000 257.743 ? 519 HIS EEE ND1 1 
ATOM 4815 C CD2 . HIS C 3 188 ? 42.083  -75.007 -63.611  1.000 241.269 ? 519 HIS EEE CD2 1 
ATOM 4816 C CE1 . HIS C 3 188 ? 41.155  -73.924 -61.937  1.000 251.518 ? 519 HIS EEE CE1 1 
ATOM 4817 N NE2 . HIS C 3 188 ? 40.939  -74.401 -63.166  1.000 248.099 ? 519 HIS EEE NE2 1 
ATOM 4818 N N   . ALA C 3 189 ? 47.539  -73.726 -64.101  1.000 255.491 ? 520 ALA EEE N   1 
ATOM 4819 C CA  . ALA C 3 189 ? 48.889  -73.879 -64.697  1.000 251.832 ? 520 ALA EEE CA  1 
ATOM 4820 C C   . ALA C 3 189 ? 49.662  -72.583 -64.477  1.000 243.808 ? 520 ALA EEE C   1 
ATOM 4821 O O   . ALA C 3 189 ? 49.051  -71.567 -64.143  1.000 237.907 ? 520 ALA EEE O   1 
ATOM 4822 C CB  . ALA C 3 189 ? 48.748  -74.183 -66.169  1.000 248.439 ? 520 ALA EEE CB  1 
ATOM 4823 N N   . PRO C 3 190 ? 51.005  -72.559 -64.651  1.000 237.467 ? 521 PRO EEE N   1 
ATOM 4824 C CA  . PRO C 3 190 ? 51.781  -71.353 -64.349  1.000 236.115 ? 521 PRO EEE CA  1 
ATOM 4825 C C   . PRO C 3 190 ? 51.231  -70.132 -65.104  1.000 211.567 ? 521 PRO EEE C   1 
ATOM 4826 O O   . PRO C 3 190 ? 51.114  -70.227 -66.289  1.000 205.658 ? 521 PRO EEE O   1 
ATOM 4827 C CB  . PRO C 3 190 ? 53.211  -71.733 -64.784  1.000 247.438 ? 521 PRO EEE CB  1 
ATOM 4828 C CG  . PRO C 3 190 ? 53.240  -73.254 -64.692  1.000 250.268 ? 521 PRO EEE CG  1 
ATOM 4829 C CD  . PRO C 3 190 ? 51.850  -73.670 -65.128  1.000 236.740 ? 521 PRO EEE CD  1 
ATOM 4830 N N   . ALA C 3 191 ? 50.871  -69.057 -64.393  1.000 201.505 ? 522 ALA EEE N   1 
ATOM 4831 C CA  . ALA C 3 191 ? 50.345  -67.795 -64.964  1.000 191.820 ? 522 ALA EEE CA  1 
ATOM 4832 C C   . ALA C 3 191 ? 51.536  -66.939 -65.403  1.000 190.068 ? 522 ALA EEE C   1 
ATOM 4833 O O   . ALA C 3 191 ? 52.161  -66.262 -64.569  1.000 201.588 ? 522 ALA EEE O   1 
ATOM 4834 C CB  . ALA C 3 191 ? 49.451  -67.081 -63.978  1.000 196.267 ? 522 ALA EEE CB  1 
ATOM 4835 N N   . THR C 3 192 ? 51.842  -67.005 -66.690  1.000 186.501 ? 523 THR EEE N   1 
ATOM 4836 C CA  . THR C 3 192 ? 53.140  -66.605 -67.287  1.000 183.308 ? 523 THR EEE CA  1 
ATOM 4837 C C   . THR C 3 192 ? 52.987  -65.224 -67.939  1.000 171.523 ? 523 THR EEE C   1 
ATOM 4838 O O   . THR C 3 192 ? 53.986  -64.675 -68.409  1.000 159.438 ? 523 THR EEE O   1 
ATOM 4839 C CB  . THR C 3 192 ? 53.604  -67.727 -68.229  1.000 182.336 ? 523 THR EEE CB  1 
ATOM 4840 O OG1 . THR C 3 192 ? 54.870  -67.417 -68.810  1.000 179.994 ? 523 THR EEE OG1 1 
ATOM 4841 C CG2 . THR C 3 192 ? 52.604  -68.016 -69.327  1.000 178.811 ? 523 THR EEE CG2 1 
ATOM 4842 N N   . VAL C 3 193 ? 51.778  -64.679 -67.984  1.000 166.940 ? 524 VAL EEE N   1 
ATOM 4843 C CA  . VAL C 3 193 ? 51.525  -63.371 -68.656  1.000 181.968 ? 524 VAL EEE CA  1 
ATOM 4844 C C   . VAL C 3 193 ? 51.046  -62.380 -67.604  1.000 193.708 ? 524 VAL EEE C   1 
ATOM 4845 O O   . VAL C 3 193 ? 49.835  -62.406 -67.291  1.000 187.686 ? 524 VAL EEE O   1 
ATOM 4846 C CB  . VAL C 3 193 ? 50.504  -63.462 -69.805  1.000 181.886 ? 524 VAL EEE CB  1 
ATOM 4847 C CG1 . VAL C 3 193 ? 50.336  -62.110 -70.473  1.000 171.085 ? 524 VAL EEE CG1 1 
ATOM 4848 C CG2 . VAL C 3 193 ? 50.874  -64.518 -70.836  1.000 186.501 ? 524 VAL EEE CG2 1 
ATOM 4849 N N   . CYS C 3 194 ? 51.954  -61.512 -67.143  1.000 215.260 ? 525 CYS EEE N   1 
ATOM 4850 C CA  . CYS C 3 194 ? 51.798  -60.667 -65.927  1.000 220.400 ? 525 CYS EEE CA  1 
ATOM 4851 C C   . CYS C 3 194 ? 51.989  -59.188 -66.253  1.000 210.376 ? 525 CYS EEE C   1 
ATOM 4852 O O   . CYS C 3 194 ? 52.826  -58.882 -67.104  1.000 200.843 ? 525 CYS EEE O   1 
ATOM 4853 C CB  . CYS C 3 194 ? 52.796  -61.086 -64.858  1.000 223.870 ? 525 CYS EEE CB  1 
ATOM 4854 S SG  . CYS C 3 194 ? 52.407  -62.708 -64.155  1.000 246.499 ? 525 CYS EEE SG  1 
ATOM 4855 N N   . GLY C 3 195 ? 51.239  -58.314 -65.578  1.000 207.323 ? 526 GLY EEE N   1 
ATOM 4856 C CA  . GLY C 3 195 ? 51.464  -56.853 -65.597  1.000 209.579 ? 526 GLY EEE CA  1 
ATOM 4857 C C   . GLY C 3 195 ? 52.743  -56.475 -64.846  1.000 210.894 ? 526 GLY EEE C   1 
ATOM 4858 O O   . GLY C 3 195 ? 53.257  -57.300 -64.082  1.000 213.642 ? 526 GLY EEE O   1 
ATOM 4859 N N   . PRO C 3 196 ? 53.283  -55.232 -65.008  1.000 205.079 ? 527 PRO EEE N   1 
ATOM 4860 C CA  . PRO C 3 196 ? 54.591  -54.868 -64.453  1.000 200.047 ? 527 PRO EEE CA  1 
ATOM 4861 C C   . PRO C 3 196 ? 54.605  -55.038 -62.929  1.000 195.546 ? 527 PRO EEE C   1 
ATOM 4862 O O   . PRO C 3 196 ? 55.670  -55.232 -62.392  1.000 199.508 ? 527 PRO EEE O   1 
ATOM 4863 C CB  . PRO C 3 196 ? 54.801  -53.388 -64.819  1.000 193.579 ? 527 PRO EEE CB  1 
ATOM 4864 C CG  . PRO C 3 196 ? 53.826  -53.145 -65.950  1.000 191.633 ? 527 PRO EEE CG  1 
ATOM 4865 C CD  . PRO C 3 196 ? 52.661  -54.089 -65.700  1.000 197.386 ? 527 PRO EEE CD  1 
ATOM 4866 N N   . LYS C 3 197 ? 53.420  -54.986 -62.309  1.000 192.060 ? 528 LYS EEE N   1 
ATOM 4867 C CA  . LYS C 3 197 ? 53.183  -55.091 -60.847  1.000 194.307 ? 528 LYS EEE CA  1 
ATOM 4868 C C   . LYS C 3 197 ? 52.512  -56.425 -60.507  1.000 183.418 ? 528 LYS EEE C   1 
ATOM 4869 O O   . LYS C 3 197 ? 53.167  -57.457 -60.507  1.000 181.340 ? 528 LYS EEE O   1 
ATOM 4870 C CB  . LYS C 3 197 ? 52.352  -53.879 -60.420  1.000 203.600 ? 528 LYS EEE CB  1 
ATOM 4871 C CG  . LYS C 3 197 ? 53.096  -52.547 -60.553  1.000 215.959 ? 528 LYS EEE CG  1 
ATOM 4872 C CD  . LYS C 3 197 ? 54.295  -52.390 -59.610  1.000 228.280 ? 528 LYS EEE CD  1 
ATOM 4873 C CE  . LYS C 3 197 ? 55.447  -51.565 -60.157  1.000 226.061 ? 528 LYS EEE CE  1 
ATOM 4874 N NZ  . LYS C 3 197 ? 55.348  -50.134 -59.780  1.000 215.042 ? 528 LYS EEE NZ  1 
ATOM 4875 N N   . GLN D 4 1   ? 55.442  -58.002 -107.656 1.000 268.576 ? 1   GLN FFF N   1 
ATOM 4876 C CA  . GLN D 4 1   ? 55.347  -58.039 -109.136 1.000 273.346 ? 1   GLN FFF CA  1 
ATOM 4877 C C   . GLN D 4 1   ? 55.581  -59.471 -109.624 1.000 279.855 ? 1   GLN FFF C   1 
ATOM 4878 O O   . GLN D 4 1   ? 56.344  -60.198 -108.945 1.000 288.700 ? 1   GLN FFF O   1 
ATOM 4879 C CB  . GLN D 4 1   ? 56.390  -57.119 -109.771 1.000 271.576 ? 1   GLN FFF CB  1 
ATOM 4880 C CG  . GLN D 4 1   ? 56.092  -55.635 -109.627 1.000 270.027 ? 1   GLN FFF CG  1 
ATOM 4881 C CD  . GLN D 4 1   ? 56.879  -54.837 -110.643 1.000 269.155 ? 1   GLN FFF CD  1 
ATOM 4882 O OE1 . GLN D 4 1   ? 56.997  -55.230 -111.802 1.000 261.818 ? 1   GLN FFF OE1 1 
ATOM 4883 N NE2 . GLN D 4 1   ? 57.433  -53.708 -110.223 1.000 268.300 ? 1   GLN FFF NE2 1 
ATOM 4884 N N   . VAL D 4 2   ? 54.954  -59.855 -110.745 1.000 279.517 ? 2   VAL FFF N   1 
ATOM 4885 C CA  . VAL D 4 2   ? 55.216  -61.155 -111.438 1.000 275.925 ? 2   VAL FFF CA  1 
ATOM 4886 C C   . VAL D 4 2   ? 55.612  -60.855 -112.892 1.000 270.960 ? 2   VAL FFF C   1 
ATOM 4887 O O   . VAL D 4 2   ? 55.169  -59.799 -113.414 1.000 269.988 ? 2   VAL FFF O   1 
ATOM 4888 C CB  . VAL D 4 2   ? 54.022  -62.135 -111.326 1.000 278.705 ? 2   VAL FFF CB  1 
ATOM 4889 C CG1 . VAL D 4 2   ? 53.593  -62.355 -109.879 1.000 273.102 ? 2   VAL FFF CG1 1 
ATOM 4890 C CG2 . VAL D 4 2   ? 52.812  -61.735 -112.172 1.000 284.723 ? 2   VAL FFF CG2 1 
ATOM 4891 N N   . GLN D 4 3   ? 56.443  -61.721 -113.491 1.000 269.159 ? 3   GLN FFF N   1 
ATOM 4892 C CA  . GLN D 4 3   ? 56.747  -61.727 -114.950 1.000 274.143 ? 3   GLN FFF CA  1 
ATOM 4893 C C   . GLN D 4 3   ? 55.995  -62.880 -115.629 1.000 272.052 ? 3   GLN FFF C   1 
ATOM 4894 O O   . GLN D 4 3   ? 56.058  -64.022 -115.108 1.000 274.271 ? 3   GLN FFF O   1 
ATOM 4895 C CB  . GLN D 4 3   ? 58.248  -61.857 -115.227 1.000 276.899 ? 3   GLN FFF CB  1 
ATOM 4896 C CG  . GLN D 4 3   ? 58.579  -61.865 -116.717 1.000 277.811 ? 3   GLN FFF CG  1 
ATOM 4897 C CD  . GLN D 4 3   ? 60.025  -62.180 -117.002 1.000 278.555 ? 3   GLN FFF CD  1 
ATOM 4898 O OE1 . GLN D 4 3   ? 60.550  -63.208 -116.585 1.000 279.547 ? 3   GLN FFF OE1 1 
ATOM 4899 N NE2 . GLN D 4 3   ? 60.673  -61.304 -117.748 1.000 281.467 ? 3   GLN FFF NE2 1 
ATOM 4900 N N   . LEU D 4 4   ? 55.323  -62.578 -116.745 1.000 268.812 ? 4   LEU FFF N   1 
ATOM 4901 C CA  . LEU D 4 4   ? 54.597  -63.548 -117.602 1.000 271.756 ? 4   LEU FFF CA  1 
ATOM 4902 C C   . LEU D 4 4   ? 55.386  -63.717 -118.907 1.000 286.766 ? 4   LEU FFF C   1 
ATOM 4903 O O   . LEU D 4 4   ? 55.645  -62.683 -119.566 1.000 290.147 ? 4   LEU FFF O   1 
ATOM 4904 C CB  . LEU D 4 4   ? 53.207  -62.979 -117.899 1.000 265.216 ? 4   LEU FFF CB  1 
ATOM 4905 C CG  . LEU D 4 4   ? 52.302  -62.705 -116.701 1.000 259.941 ? 4   LEU FFF CG  1 
ATOM 4906 C CD1 . LEU D 4 4   ? 50.846  -62.692 -117.136 1.000 260.614 ? 4   LEU FFF CD1 1 
ATOM 4907 C CD2 . LEU D 4 4   ? 52.507  -63.717 -115.584 1.000 256.680 ? 4   LEU FFF CD2 1 
ATOM 4908 N N   . VAL D 4 5   ? 55.766  -64.951 -119.261 1.000 296.218 ? 5   VAL FFF N   1 
ATOM 4909 C CA  . VAL D 4 5   ? 56.451  -65.289 -120.550 1.000 295.728 ? 5   VAL FFF CA  1 
ATOM 4910 C C   . VAL D 4 5   ? 55.647  -66.405 -121.231 1.000 297.425 ? 5   VAL FFF C   1 
ATOM 4911 O O   . VAL D 4 5   ? 55.567  -67.523 -120.663 1.000 292.339 ? 5   VAL FFF O   1 
ATOM 4912 C CB  . VAL D 4 5   ? 57.933  -65.678 -120.346 1.000 294.594 ? 5   VAL FFF CB  1 
ATOM 4913 C CG1 . VAL D 4 5   ? 58.599  -66.106 -121.644 1.000 296.844 ? 5   VAL FFF CG1 1 
ATOM 4914 C CG2 . VAL D 4 5   ? 58.736  -64.555 -119.702 1.000 292.992 ? 5   VAL FFF CG2 1 
ATOM 4915 N N   . GLU D 4 6   ? 55.055  -66.096 -122.391 1.000 308.240 ? 6   GLU FFF N   1 
ATOM 4916 C CA  . GLU D 4 6   ? 54.260  -67.055 -123.206 1.000 320.132 ? 6   GLU FFF CA  1 
ATOM 4917 C C   . GLU D 4 6   ? 55.178  -67.805 -124.174 1.000 331.610 ? 6   GLU FFF C   1 
ATOM 4918 O O   . GLU D 4 6   ? 56.250  -67.263 -124.519 1.000 346.353 ? 6   GLU FFF O   1 
ATOM 4919 C CB  . GLU D 4 6   ? 53.178  -66.368 -124.042 1.000 322.299 ? 6   GLU FFF CB  1 
ATOM 4920 C CG  . GLU D 4 6   ? 52.223  -65.516 -123.237 1.000 318.488 ? 6   GLU FFF CG  1 
ATOM 4921 C CD  . GLU D 4 6   ? 52.465  -64.020 -123.332 1.000 316.774 ? 6   GLU FFF CD  1 
ATOM 4922 O OE1 . GLU D 4 6   ? 53.630  -63.605 -123.278 1.000 320.220 ? 6   GLU FFF OE1 1 
ATOM 4923 O OE2 . GLU D 4 6   ? 51.483  -63.270 -123.463 1.000 309.905 ? 6   GLU FFF OE2 1 
ATOM 4924 N N   . SER D 4 7   ? 54.740  -68.987 -124.613 1.000 330.329 ? 7   SER FFF N   1 
ATOM 4925 C CA  . SER D 4 7   ? 55.371  -69.807 -125.680 1.000 325.724 ? 7   SER FFF CA  1 
ATOM 4926 C C   . SER D 4 7   ? 54.285  -70.642 -126.365 1.000 320.876 ? 7   SER FFF C   1 
ATOM 4927 O O   . SER D 4 7   ? 53.152  -70.639 -125.858 1.000 301.680 ? 7   SER FFF O   1 
ATOM 4928 C CB  . SER D 4 7   ? 56.490  -70.669 -125.129 1.000 325.238 ? 7   SER FFF CB  1 
ATOM 4929 O OG  . SER D 4 7   ? 56.050  -71.477 -124.045 1.000 318.078 ? 7   SER FFF OG  1 
ATOM 4930 N N   . GLY D 4 8   ? 54.622  -71.277 -127.494 1.000 325.120 ? 8   GLY FFF N   1 
ATOM 4931 C CA  . GLY D 4 8   ? 53.785  -72.280 -128.182 1.000 318.545 ? 8   GLY FFF CA  1 
ATOM 4932 C C   . GLY D 4 8   ? 53.141  -71.758 -129.457 1.000 309.587 ? 8   GLY FFF C   1 
ATOM 4933 O O   . GLY D 4 8   ? 52.470  -72.549 -130.130 1.000 300.455 ? 8   GLY FFF O   1 
ATOM 4934 N N   . GLY D 4 9   ? 53.318  -70.475 -129.778 1.000 305.949 ? 9   GLY FFF N   1 
ATOM 4935 C CA  . GLY D 4 9   ? 52.847  -69.887 -131.046 1.000 306.725 ? 9   GLY FFF CA  1 
ATOM 4936 C C   . GLY D 4 9   ? 53.642  -70.414 -132.228 1.000 308.990 ? 9   GLY FFF C   1 
ATOM 4937 O O   . GLY D 4 9   ? 54.789  -70.840 -132.009 1.000 312.510 ? 9   GLY FFF O   1 
ATOM 4938 N N   . GLY D 4 10  ? 53.057  -70.385 -133.433 1.000 310.381 ? 10  GLY FFF N   1 
ATOM 4939 C CA  . GLY D 4 10  ? 53.682  -70.876 -134.681 1.000 314.884 ? 10  GLY FFF CA  1 
ATOM 4940 C C   . GLY D 4 10  ? 52.671  -71.001 -135.810 1.000 314.603 ? 10  GLY FFF C   1 
ATOM 4941 O O   . GLY D 4 10  ? 51.545  -70.495 -135.650 1.000 325.535 ? 10  GLY FFF O   1 
ATOM 4942 N N   . LEU D 4 11  ? 53.050  -71.660 -136.910 1.000 306.205 ? 11  LEU FFF N   1 
ATOM 4943 C CA  . LEU D 4 11  ? 52.152  -71.958 -138.057 1.000 306.169 ? 11  LEU FFF CA  1 
ATOM 4944 C C   . LEU D 4 11  ? 51.401  -73.264 -137.786 1.000 311.425 ? 11  LEU FFF C   1 
ATOM 4945 O O   . LEU D 4 11  ? 52.074  -74.271 -137.491 1.000 312.898 ? 11  LEU FFF O   1 
ATOM 4946 C CB  . LEU D 4 11  ? 52.987  -72.089 -139.333 1.000 305.535 ? 11  LEU FFF CB  1 
ATOM 4947 C CG  . LEU D 4 11  ? 52.182  -72.256 -140.619 1.000 300.769 ? 11  LEU FFF CG  1 
ATOM 4948 C CD1 . LEU D 4 11  ? 51.354  -71.006 -140.883 1.000 299.059 ? 11  LEU FFF CD1 1 
ATOM 4949 C CD2 . LEU D 4 11  ? 53.096  -72.573 -141.789 1.000 301.876 ? 11  LEU FFF CD2 1 
ATOM 4950 N N   . MET D 4 12  ? 50.070  -73.260 -137.903 1.000 319.908 ? 12  MET FFF N   1 
ATOM 4951 C CA  . MET D 4 12  ? 49.253  -74.500 -137.821 1.000 329.928 ? 12  MET FFF CA  1 
ATOM 4952 C C   . MET D 4 12  ? 48.124  -74.464 -138.853 1.000 338.754 ? 12  MET FFF C   1 
ATOM 4953 O O   . MET D 4 12  ? 47.665  -73.366 -139.193 1.000 347.581 ? 12  MET FFF O   1 
ATOM 4954 C CB  . MET D 4 12  ? 48.669  -74.709 -136.421 1.000 327.717 ? 12  MET FFF CB  1 
ATOM 4955 C CG  . MET D 4 12  ? 49.532  -75.600 -135.540 1.000 327.921 ? 12  MET FFF CG  1 
ATOM 4956 S SD  . MET D 4 12  ? 50.042  -77.155 -136.348 1.000 327.228 ? 12  MET FFF SD  1 
ATOM 4957 C CE  . MET D 4 12  ? 48.617  -78.201 -136.055 1.000 325.300 ? 12  MET FFF CE  1 
ATOM 4958 N N   . GLN D 4 13  ? 47.711  -75.644 -139.319 1.000 338.993 ? 13  GLN FFF N   1 
ATOM 4959 C CA  . GLN D 4 13  ? 46.641  -75.836 -140.326 1.000 336.980 ? 13  GLN FFF CA  1 
ATOM 4960 C C   . GLN D 4 13  ? 45.286  -75.727 -139.614 1.000 335.800 ? 13  GLN FFF C   1 
ATOM 4961 O O   . GLN D 4 13  ? 45.199  -76.187 -138.450 1.000 331.066 ? 13  GLN FFF O   1 
ATOM 4962 C CB  . GLN D 4 13  ? 46.867  -77.188 -141.003 1.000 337.075 ? 13  GLN FFF CB  1 
ATOM 4963 C CG  . GLN D 4 13  ? 48.047  -77.168 -141.965 1.000 336.883 ? 13  GLN FFF CG  1 
ATOM 4964 C CD  . GLN D 4 13  ? 48.719  -78.510 -142.099 1.000 334.180 ? 13  GLN FFF CD  1 
ATOM 4965 O OE1 . GLN D 4 13  ? 48.121  -79.555 -141.855 1.000 329.793 ? 13  GLN FFF OE1 1 
ATOM 4966 N NE2 . GLN D 4 13  ? 49.972  -78.494 -142.525 1.000 335.387 ? 13  GLN FFF NE2 1 
ATOM 4967 N N   . ALA D 4 14  ? 44.288  -75.118 -140.270 1.000 335.554 ? 14  ALA FFF N   1 
ATOM 4968 C CA  . ALA D 4 14  ? 42.878  -75.069 -139.813 1.000 331.309 ? 14  ALA FFF CA  1 
ATOM 4969 C C   . ALA D 4 14  ? 42.403  -76.502 -139.536 1.000 336.818 ? 14  ALA FFF C   1 
ATOM 4970 O O   . ALA D 4 14  ? 42.722  -77.394 -140.343 1.000 344.582 ? 14  ALA FFF O   1 
ATOM 4971 C CB  . ALA D 4 14  ? 42.006  -74.372 -140.832 1.000 325.021 ? 14  ALA FFF CB  1 
ATOM 4972 N N   . GLY D 4 15  ? 41.733  -76.726 -138.400 1.000 337.757 ? 15  GLY FFF N   1 
ATOM 4973 C CA  . GLY D 4 15  ? 41.258  -78.060 -137.975 1.000 334.675 ? 15  GLY FFF CA  1 
ATOM 4974 C C   . GLY D 4 15  ? 42.225  -78.756 -137.025 1.000 329.476 ? 15  GLY FFF C   1 
ATOM 4975 O O   . GLY D 4 15  ? 41.774  -79.655 -136.277 1.000 331.607 ? 15  GLY FFF O   1 
ATOM 4976 N N   . GLY D 4 16  ? 43.504  -78.367 -137.038 1.000 321.179 ? 16  GLY FFF N   1 
ATOM 4977 C CA  . GLY D 4 16  ? 44.533  -78.905 -136.131 1.000 307.940 ? 16  GLY FFF CA  1 
ATOM 4978 C C   . GLY D 4 16  ? 44.386  -78.336 -134.734 1.000 288.863 ? 16  GLY FFF C   1 
ATOM 4979 O O   . GLY D 4 16  ? 43.436  -77.577 -134.495 1.000 273.224 ? 16  GLY FFF O   1 
ATOM 4980 N N   . SER D 4 17  ? 45.303  -78.692 -133.840 1.000 281.359 ? 17  SER FFF N   1 
ATOM 4981 C CA  . SER D 4 17  ? 45.315  -78.205 -132.443 1.000 283.794 ? 17  SER FFF CA  1 
ATOM 4982 C C   . SER D 4 17  ? 46.710  -77.685 -132.079 1.000 287.998 ? 17  SER FFF C   1 
ATOM 4983 O O   . SER D 4 17  ? 47.684  -78.161 -132.691 1.000 285.199 ? 17  SER FFF O   1 
ATOM 4984 C CB  . SER D 4 17  ? 44.831  -79.279 -131.510 1.000 282.515 ? 17  SER FFF CB  1 
ATOM 4985 O OG  . SER D 4 17  ? 44.411  -78.719 -130.272 1.000 279.308 ? 17  SER FFF OG  1 
ATOM 4986 N N   . LEU D 4 18  ? 46.768  -76.721 -131.143 1.000 294.912 ? 18  LEU FFF N   1 
ATOM 4987 C CA  . LEU D 4 18  ? 47.986  -75.987 -130.683 1.000 292.409 ? 18  LEU FFF CA  1 
ATOM 4988 C C   . LEU D 4 18  ? 47.818  -75.518 -129.220 1.000 282.021 ? 18  LEU FFF C   1 
ATOM 4989 O O   . LEU D 4 18  ? 46.770  -74.952 -128.888 1.000 274.461 ? 18  LEU FFF O   1 
ATOM 4990 C CB  . LEU D 4 18  ? 48.194  -74.796 -131.625 1.000 294.550 ? 18  LEU FFF CB  1 
ATOM 4991 C CG  . LEU D 4 18  ? 49.446  -73.969 -131.374 1.000 294.166 ? 18  LEU FFF CG  1 
ATOM 4992 C CD1 . LEU D 4 18  ? 50.673  -74.865 -131.346 1.000 293.984 ? 18  LEU FFF CD1 1 
ATOM 4993 C CD2 . LEU D 4 18  ? 49.582  -72.890 -132.437 1.000 295.652 ? 18  LEU FFF CD2 1 
ATOM 4994 N N   A ARG D 4 19  ? 48.840  -75.721 -128.388 0.500 279.016 ? 19  ARG FFF N   1 
ATOM 4995 N N   B ARG D 4 19  ? 48.814  -75.770 -128.365 0.500 277.217 ? 19  ARG FFF N   1 
ATOM 4996 C CA  A ARG D 4 19  ? 48.800  -75.432 -126.928 0.500 274.803 ? 19  ARG FFF CA  1 
ATOM 4997 C CA  B ARG D 4 19  ? 48.766  -75.416 -126.918 0.500 271.997 ? 19  ARG FFF CA  1 
ATOM 4998 C C   A ARG D 4 19  ? 49.821  -74.341 -126.596 0.500 276.382 ? 19  ARG FFF C   1 
ATOM 4999 C C   B ARG D 4 19  ? 49.808  -74.338 -126.612 0.500 274.850 ? 19  ARG FFF C   1 
ATOM 5000 O O   A ARG D 4 19  ? 51.026  -74.623 -126.731 0.500 277.540 ? 19  ARG FFF O   1 
ATOM 5001 O O   B ARG D 4 19  ? 51.007  -74.630 -126.770 0.500 276.493 ? 19  ARG FFF O   1 
ATOM 5002 C CB  A ARG D 4 19  ? 49.106  -76.705 -126.131 0.500 270.348 ? 19  ARG FFF CB  1 
ATOM 5003 C CB  B ARG D 4 19  ? 49.021  -76.625 -126.011 0.500 265.207 ? 19  ARG FFF CB  1 
ATOM 5004 C CG  A ARG D 4 19  ? 48.954  -76.569 -124.623 0.500 263.869 ? 19  ARG FFF CG  1 
ATOM 5005 C CG  B ARG D 4 19  ? 49.142  -76.263 -124.536 0.500 257.466 ? 19  ARG FFF CG  1 
ATOM 5006 C CD  A ARG D 4 19  ? 49.415  -77.846 -123.948 0.500 261.422 ? 19  ARG FFF CD  1 
ATOM 5007 C CD  B ARG D 4 19  ? 49.125  -77.461 -123.606 0.500 252.546 ? 19  ARG FFF CD  1 
ATOM 5008 N NE  A ARG D 4 19  ? 48.963  -78.005 -122.573 0.500 258.117 ? 19  ARG FFF NE  1 
ATOM 5009 N NE  B ARG D 4 19  ? 47.819  -78.109 -123.548 0.500 249.067 ? 19  ARG FFF NE  1 
ATOM 5010 C CZ  A ARG D 4 19  ? 47.811  -78.564 -122.216 0.500 255.863 ? 19  ARG FFF CZ  1 
ATOM 5011 C CZ  B ARG D 4 19  ? 47.379  -78.820 -122.515 0.500 245.364 ? 19  ARG FFF CZ  1 
ATOM 5012 N NH1 A ARG D 4 19  ? 46.969  -79.004 -123.133 0.500 255.680 ? 19  ARG FFF NH1 1 
ATOM 5013 N NH1 B ARG D 4 19  ? 48.146  -78.981 -121.452 0.500 244.229 ? 19  ARG FFF NH1 1 
ATOM 5014 N NH2 A ARG D 4 19  ? 47.496  -78.677 -120.939 0.500 254.033 ? 19  ARG FFF NH2 1 
ATOM 5015 N NH2 B ARG D 4 19  ? 46.179  -79.372 -122.546 0.500 242.861 ? 19  ARG FFF NH2 1 
ATOM 5016 N N   . LEU D 4 20  ? 49.355  -73.163 -126.163 1.000 276.942 ? 20  LEU FFF N   1 
ATOM 5017 C CA  . LEU D 4 20  ? 50.220  -72.063 -125.648 1.000 279.110 ? 20  LEU FFF CA  1 
ATOM 5018 C C   . LEU D 4 20  ? 50.503  -72.313 -124.154 1.000 285.617 ? 20  LEU FFF C   1 
ATOM 5019 O O   . LEU D 4 20  ? 49.617  -72.868 -123.476 1.000 289.917 ? 20  LEU FFF O   1 
ATOM 5020 C CB  . LEU D 4 20  ? 49.517  -70.714 -125.846 1.000 276.318 ? 20  LEU FFF CB  1 
ATOM 5021 C CG  . LEU D 4 20  ? 48.931  -70.441 -127.229 1.000 279.449 ? 20  LEU FFF CG  1 
ATOM 5022 C CD1 . LEU D 4 20  ? 48.239  -69.091 -127.250 1.000 274.665 ? 20  LEU FFF CD1 1 
ATOM 5023 C CD2 . LEU D 4 20  ? 49.995  -70.517 -128.311 1.000 286.112 ? 20  LEU FFF CD2 1 
ATOM 5024 N N   . SER D 4 21  ? 51.692  -71.937 -123.663 1.000 285.238 ? 21  SER FFF N   1 
ATOM 5025 C CA  . SER D 4 21  ? 52.052  -71.879 -122.218 1.000 272.599 ? 21  SER FFF CA  1 
ATOM 5026 C C   . SER D 4 21  ? 52.287  -70.428 -121.808 1.000 270.641 ? 21  SER FFF C   1 
ATOM 5027 O O   . SER D 4 21  ? 52.675  -69.620 -122.666 1.000 278.395 ? 21  SER FFF O   1 
ATOM 5028 C CB  . SER D 4 21  ? 53.290  -72.670 -121.891 1.000 269.039 ? 21  SER FFF CB  1 
ATOM 5029 O OG  . SER D 4 21  ? 53.107  -74.042 -122.149 1.000 268.879 ? 21  SER FFF OG  1 
ATOM 5030 N N   . CYS D 4 22  ? 52.050  -70.127 -120.534 1.000 268.018 ? 22  CYS FFF N   1 
ATOM 5031 C CA  A CYS D 4 22  ? 52.504  -68.889 -119.843 0.700 267.230 ? 22  CYS FFF CA  1 
ATOM 5032 C CA  B CYS D 4 22  ? 52.589  -68.909 -119.872 0.300 266.583 ? 22  CYS FFF CA  1 
ATOM 5033 C C   . CYS D 4 22  ? 53.103  -69.291 -118.485 1.000 264.867 ? 22  CYS FFF C   1 
ATOM 5034 O O   . CYS D 4 22  ? 52.301  -69.765 -117.637 1.000 257.637 ? 22  CYS FFF O   1 
ATOM 5035 C CB  A CYS D 4 22  ? 51.333  -67.922 -119.685 0.700 264.302 ? 22  CYS FFF CB  1 
ATOM 5036 C CB  B CYS D 4 22  ? 51.595  -67.761 -119.759 0.300 264.367 ? 22  CYS FFF CB  1 
ATOM 5037 S SG  A CYS D 4 22  ? 51.743  -66.349 -118.884 0.700 259.125 ? 22  CYS FFF SG  1 
ATOM 5038 S SG  B CYS D 4 22  ? 52.344  -66.273 -119.039 0.300 259.414 ? 22  CYS FFF SG  1 
ATOM 5039 N N   . ALA D 4 23  ? 54.420  -69.131 -118.320 1.000 264.947 ? 23  ALA FFF N   1 
ATOM 5040 C CA  . ALA D 4 23  ? 55.177  -69.392 -117.078 1.000 263.014 ? 23  ALA FFF CA  1 
ATOM 5041 C C   . ALA D 4 23  ? 55.170  -68.106 -116.244 1.000 266.678 ? 23  ALA FFF C   1 
ATOM 5042 O O   . ALA D 4 23  ? 55.463  -67.022 -116.814 1.000 263.387 ? 23  ALA FFF O   1 
ATOM 5043 C CB  . ALA D 4 23  ? 56.577  -69.847 -117.406 1.000 264.253 ? 23  ALA FFF CB  1 
ATOM 5044 N N   . VAL D 4 24  ? 54.790  -68.219 -114.966 1.000 269.069 ? 24  VAL FFF N   1 
ATOM 5045 C CA  . VAL D 4 24  ? 54.704  -67.084 -114.000 1.000 258.513 ? 24  VAL FFF CA  1 
ATOM 5046 C C   . VAL D 4 24  ? 55.883  -67.214 -113.035 1.000 253.454 ? 24  VAL FFF C   1 
ATOM 5047 O O   . VAL D 4 24  ? 56.059  -68.317 -112.478 1.000 241.775 ? 24  VAL FFF O   1 
ATOM 5048 C CB  . VAL D 4 24  ? 53.350  -67.062 -113.264 1.000 256.835 ? 24  VAL FFF CB  1 
ATOM 5049 C CG1 . VAL D 4 24  ? 53.178  -65.797 -112.439 1.000 258.420 ? 24  VAL FFF CG1 1 
ATOM 5050 C CG2 . VAL D 4 24  ? 52.177  -67.219 -114.223 1.000 260.527 ? 24  VAL FFF CG2 1 
ATOM 5051 N N   . SER D 4 25  ? 56.668  -66.140 -112.888 1.000 257.393 ? 25  SER FFF N   1 
ATOM 5052 C CA  . SER D 4 25  ? 57.841  -66.043 -111.979 1.000 256.187 ? 25  SER FFF CA  1 
ATOM 5053 C C   . SER D 4 25  ? 57.712  -64.802 -111.091 1.000 259.737 ? 25  SER FFF C   1 
ATOM 5054 O O   . SER D 4 25  ? 57.009  -63.842 -111.487 1.000 259.617 ? 25  SER FFF O   1 
ATOM 5055 C CB  . SER D 4 25  ? 59.129  -66.020 -112.761 1.000 254.961 ? 25  SER FFF CB  1 
ATOM 5056 O OG  . SER D 4 25  ? 59.454  -64.701 -113.196 1.000 249.010 ? 25  SER FFF OG  1 
ATOM 5057 N N   . GLY D 4 26  ? 58.377  -64.837 -109.936 1.000 267.236 ? 26  GLY FFF N   1 
ATOM 5058 C CA  . GLY D 4 26  ? 58.385  -63.746 -108.945 1.000 275.338 ? 26  GLY FFF CA  1 
ATOM 5059 C C   . GLY D 4 26  ? 57.415  -64.013 -107.808 1.000 277.195 ? 26  GLY FFF C   1 
ATOM 5060 O O   . GLY D 4 26  ? 57.507  -65.089 -107.190 1.000 281.815 ? 26  GLY FFF O   1 
ATOM 5061 N N   . ARG D 4 27  ? 56.493  -63.078 -107.568 1.000 276.780 ? 27  ARG FFF N   1 
ATOM 5062 C CA  . ARG D 4 27  ? 55.582  -63.046 -106.396 1.000 269.942 ? 27  ARG FFF CA  1 
ATOM 5063 C C   . ARG D 4 27  ? 54.334  -63.882 -106.721 1.000 265.657 ? 27  ARG FFF C   1 
ATOM 5064 O O   . ARG D 4 27  ? 53.211  -63.341 -106.664 1.000 261.614 ? 27  ARG FFF O   1 
ATOM 5065 C CB  . ARG D 4 27  ? 55.322  -61.571 -106.074 1.000 271.825 ? 27  ARG FFF CB  1 
ATOM 5066 C CG  . ARG D 4 27  ? 55.289  -61.256 -104.589 1.000 272.962 ? 27  ARG FFF CG  1 
ATOM 5067 C CD  . ARG D 4 27  ? 55.538  -59.803 -104.198 1.000 273.064 ? 27  ARG FFF CD  1 
ATOM 5068 N NE  . ARG D 4 27  ? 54.367  -59.298 -103.484 1.000 272.904 ? 27  ARG FFF NE  1 
ATOM 5069 C CZ  . ARG D 4 27  ? 53.922  -58.040 -103.505 1.000 273.889 ? 27  ARG FFF CZ  1 
ATOM 5070 N NH1 . ARG D 4 27  ? 54.604  -57.082 -104.109 1.000 274.083 ? 27  ARG FFF NH1 1 
ATOM 5071 N NH2 . ARG D 4 27  ? 52.821  -57.726 -102.846 1.000 277.285 ? 27  ARG FFF NH2 1 
ATOM 5072 N N   . THR D 4 28  ? 54.545  -65.165 -107.047 1.000 266.793 ? 28  THR FFF N   1 
ATOM 5073 C CA  . THR D 4 28  ? 53.558  -66.084 -107.680 1.000 268.979 ? 28  THR FFF CA  1 
ATOM 5074 C C   . THR D 4 28  ? 52.441  -66.427 -106.693 1.000 271.083 ? 28  THR FFF C   1 
ATOM 5075 O O   . THR D 4 28  ? 51.372  -66.833 -107.160 1.000 280.056 ? 28  THR FFF O   1 
ATOM 5076 C CB  . THR D 4 28  ? 54.178  -67.416 -108.130 1.000 269.231 ? 28  THR FFF CB  1 
ATOM 5077 O OG1 . THR D 4 28  ? 54.942  -67.948 -107.047 1.000 269.955 ? 28  THR FFF OG1 1 
ATOM 5078 C CG2 . THR D 4 28  ? 55.066  -67.296 -109.344 1.000 269.171 ? 28  THR FFF CG2 1 
ATOM 5079 N N   . PHE D 4 29  ? 52.702  -66.321 -105.388 1.000 272.089 ? 29  PHE FFF N   1 
ATOM 5080 C CA  . PHE D 4 29  ? 51.744  -66.662 -104.303 1.000 272.733 ? 29  PHE FFF CA  1 
ATOM 5081 C C   . PHE D 4 29  ? 50.481  -65.795 -104.398 1.000 265.434 ? 29  PHE FFF C   1 
ATOM 5082 O O   . PHE D 4 29  ? 49.457  -66.171 -103.799 1.000 258.325 ? 29  PHE FFF O   1 
ATOM 5083 C CB  . PHE D 4 29  ? 52.409  -66.510 -102.932 1.000 280.067 ? 29  PHE FFF CB  1 
ATOM 5084 C CG  . PHE D 4 29  ? 52.990  -65.149 -102.622 1.000 286.394 ? 29  PHE FFF CG  1 
ATOM 5085 C CD1 . PHE D 4 29  ? 52.177  -64.086 -102.254 1.000 288.189 ? 29  PHE FFF CD1 1 
ATOM 5086 C CD2 . PHE D 4 29  ? 54.362  -64.943 -102.650 1.000 286.572 ? 29  PHE FFF CD2 1 
ATOM 5087 C CE1 . PHE D 4 29  ? 52.720  -62.846 -101.949 1.000 286.617 ? 29  PHE FFF CE1 1 
ATOM 5088 C CE2 . PHE D 4 29  ? 54.904  -63.709 -102.326 1.000 286.628 ? 29  PHE FFF CE2 1 
ATOM 5089 C CZ  . PHE D 4 29  ? 54.082  -62.663 -101.978 1.000 286.276 ? 29  PHE FFF CZ  1 
ATOM 5090 N N   . SER D 4 30  ? 50.568  -64.662 -105.100 1.000 263.205 ? 30  SER FFF N   1 
ATOM 5091 C CA  . SER D 4 30  ? 49.503  -63.631 -105.204 1.000 259.340 ? 30  SER FFF CA  1 
ATOM 5092 C C   . SER D 4 30  ? 48.438  -64.034 -106.231 1.000 253.656 ? 30  SER FFF C   1 
ATOM 5093 O O   . SER D 4 30  ? 47.333  -63.474 -106.159 1.000 247.735 ? 30  SER FFF O   1 
ATOM 5094 C CB  . SER D 4 30  ? 50.107  -62.292 -105.538 1.000 262.635 ? 30  SER FFF CB  1 
ATOM 5095 O OG  . SER D 4 30  ? 50.653  -62.298 -106.849 1.000 266.818 ? 30  SER FFF OG  1 
ATOM 5096 N N   . THR D 4 31  ? 48.752  -64.957 -107.147 1.000 254.887 ? 31  THR FFF N   1 
ATOM 5097 C CA  . THR D 4 31  ? 47.910  -65.307 -108.326 1.000 257.142 ? 31  THR FFF CA  1 
ATOM 5098 C C   . THR D 4 31  ? 46.528  -65.769 -107.842 1.000 256.443 ? 31  THR FFF C   1 
ATOM 5099 O O   . THR D 4 31  ? 46.470  -66.810 -107.146 1.000 254.619 ? 31  THR FFF O   1 
ATOM 5100 C CB  . THR D 4 31  ? 48.581  -66.374 -109.211 1.000 256.872 ? 31  THR FFF CB  1 
ATOM 5101 O OG1 . THR D 4 31  ? 49.865  -65.924 -109.658 1.000 249.365 ? 31  THR FFF OG1 1 
ATOM 5102 C CG2 . THR D 4 31  ? 47.746  -66.754 -110.417 1.000 257.858 ? 31  THR FFF CG2 1 
ATOM 5103 N N   . ALA D 4 32  ? 45.472  -65.026 -108.212 1.000 260.867 ? 32  ALA FFF N   1 
ATOM 5104 C CA  . ALA D 4 32  ? 44.040  -65.334 -107.954 1.000 265.599 ? 32  ALA FFF CA  1 
ATOM 5105 C C   . ALA D 4 32  ? 43.392  -65.943 -109.208 1.000 275.189 ? 32  ALA FFF C   1 
ATOM 5106 O O   . ALA D 4 32  ? 42.603  -66.907 -109.072 1.000 285.701 ? 32  ALA FFF O   1 
ATOM 5107 C CB  . ALA D 4 32  ? 43.316  -64.082 -107.529 1.000 259.596 ? 32  ALA FFF CB  1 
ATOM 5108 N N   . ALA D 4 33  ? 43.695  -65.377 -110.381 1.000 275.884 ? 33  ALA FFF N   1 
ATOM 5109 C CA  . ALA D 4 33  ? 43.220  -65.837 -111.704 1.000 271.110 ? 33  ALA FFF CA  1 
ATOM 5110 C C   . ALA D 4 33  ? 44.286  -65.528 -112.763 1.000 276.946 ? 33  ALA FFF C   1 
ATOM 5111 O O   . ALA D 4 33  ? 45.116  -64.627 -112.537 1.000 269.879 ? 33  ALA FFF O   1 
ATOM 5112 C CB  . ALA D 4 33  ? 41.896  -65.176 -112.020 1.000 266.644 ? 33  ALA FFF CB  1 
ATOM 5113 N N   . MET D 4 34  ? 44.275  -66.283 -113.861 1.000 281.961 ? 34  MET FFF N   1 
ATOM 5114 C CA  A MET D 4 34  ? 45.029  -66.001 -115.116 0.500 282.995 ? 34  MET FFF CA  1 
ATOM 5115 C CA  B MET D 4 34  ? 45.005  -65.895 -115.090 0.500 282.654 ? 34  MET FFF CA  1 
ATOM 5116 C C   . MET D 4 34  ? 44.016  -65.858 -116.255 1.000 288.015 ? 34  MET FFF C   1 
ATOM 5117 O O   . MET D 4 34  ? 42.972  -66.541 -116.182 1.000 297.077 ? 34  MET FFF O   1 
ATOM 5118 C CB  A MET D 4 34  ? 45.983  -67.144 -115.478 0.500 283.079 ? 34  MET FFF CB  1 
ATOM 5119 C CB  B MET D 4 34  ? 46.167  -66.851 -115.354 0.500 282.328 ? 34  MET FFF CB  1 
ATOM 5120 C CG  A MET D 4 34  ? 47.046  -67.407 -114.449 0.500 282.038 ? 34  MET FFF CG  1 
ATOM 5121 C CG  B MET D 4 34  ? 47.227  -66.739 -114.281 0.500 281.285 ? 34  MET FFF CG  1 
ATOM 5122 S SD  A MET D 4 34  ? 48.167  -66.020 -114.187 0.500 286.050 ? 34  MET FFF SD  1 
ATOM 5123 S SD  B MET D 4 34  ? 48.816  -67.457 -114.757 0.500 284.190 ? 34  MET FFF SD  1 
ATOM 5124 C CE  A MET D 4 34  ? 49.110  -66.041 -115.713 0.500 286.827 ? 34  MET FFF CE  1 
ATOM 5125 C CE  B MET D 4 34  ? 49.413  -66.233 -115.922 0.500 284.366 ? 34  MET FFF CE  1 
ATOM 5126 N N   . GLY D 4 35  ? 44.313  -65.022 -117.248 1.000 293.905 ? 35  GLY FFF N   1 
ATOM 5127 C CA  . GLY D 4 35  ? 43.462  -64.847 -118.439 1.000 291.785 ? 35  GLY FFF CA  1 
ATOM 5128 C C   . GLY D 4 35  ? 44.275  -64.956 -119.708 1.000 279.479 ? 35  GLY FFF C   1 
ATOM 5129 O O   . GLY D 4 35  ? 45.472  -64.631 -119.672 1.000 279.959 ? 35  GLY FFF O   1 
ATOM 5130 N N   . TRP D 4 36  ? 43.653  -65.420 -120.786 1.000 268.470 ? 36  TRP FFF N   1 
ATOM 5131 C CA  . TRP D 4 36  ? 44.209  -65.283 -122.151 1.000 260.195 ? 36  TRP FFF CA  1 
ATOM 5132 C C   . TRP D 4 36  ? 43.381  -64.240 -122.898 1.000 261.081 ? 36  TRP FFF C   1 
ATOM 5133 O O   . TRP D 4 36  ? 42.138  -64.246 -122.768 1.000 254.479 ? 36  TRP FFF O   1 
ATOM 5134 C CB  . TRP D 4 36  ? 44.262  -66.631 -122.867 1.000 251.918 ? 36  TRP FFF CB  1 
ATOM 5135 C CG  . TRP D 4 36  ? 45.352  -67.529 -122.368 1.000 246.019 ? 36  TRP FFF CG  1 
ATOM 5136 C CD1 . TRP D 4 36  ? 45.230  -68.493 -121.414 1.000 247.507 ? 36  TRP FFF CD1 1 
ATOM 5137 C CD2 . TRP D 4 36  ? 46.733  -67.546 -122.771 1.000 240.470 ? 36  TRP FFF CD2 1 
ATOM 5138 N NE1 . TRP D 4 36  ? 46.429  -69.119 -121.209 1.000 245.664 ? 36  TRP FFF NE1 1 
ATOM 5139 C CE2 . TRP D 4 36  ? 47.368  -68.567 -122.034 1.000 240.872 ? 36  TRP FFF CE2 1 
ATOM 5140 C CE3 . TRP D 4 36  ? 47.487  -66.832 -123.703 1.000 242.726 ? 36  TRP FFF CE3 1 
ATOM 5141 C CZ2 . TRP D 4 36  ? 48.716  -68.873 -122.184 1.000 239.774 ? 36  TRP FFF CZ2 1 
ATOM 5142 C CZ3 . TRP D 4 36  ? 48.821  -67.137 -123.858 1.000 245.431 ? 36  TRP FFF CZ3 1 
ATOM 5143 C CH2 . TRP D 4 36  ? 49.424  -68.142 -123.106 1.000 243.292 ? 36  TRP FFF CH2 1 
ATOM 5144 N N   . PHE D 4 37  ? 44.077  -63.335 -123.582 1.000 270.883 ? 37  PHE FFF N   1 
ATOM 5145 C CA  . PHE D 4 37  ? 43.513  -62.325 -124.511 1.000 283.555 ? 37  PHE FFF CA  1 
ATOM 5146 C C   . PHE D 4 37  ? 44.191  -62.532 -125.874 1.000 296.728 ? 37  PHE FFF C   1 
ATOM 5147 O O   . PHE D 4 37  ? 45.222  -63.232 -125.922 1.000 317.602 ? 37  PHE FFF O   1 
ATOM 5148 C CB  . PHE D 4 37  ? 43.708  -60.923 -123.926 1.000 281.370 ? 37  PHE FFF CB  1 
ATOM 5149 C CG  . PHE D 4 37  ? 42.979  -60.659 -122.627 1.000 277.969 ? 37  PHE FFF CG  1 
ATOM 5150 C CD1 . PHE D 4 37  ? 43.442  -61.170 -121.422 1.000 273.067 ? 37  PHE FFF CD1 1 
ATOM 5151 C CD2 . PHE D 4 37  ? 41.845  -59.859 -122.599 1.000 274.328 ? 37  PHE FFF CD2 1 
ATOM 5152 C CE1 . PHE D 4 37  ? 42.778  -60.906 -120.234 1.000 266.720 ? 37  PHE FFF CE1 1 
ATOM 5153 C CE2 . PHE D 4 37  ? 41.183  -59.595 -121.409 1.000 266.989 ? 37  PHE FFF CE2 1 
ATOM 5154 C CZ  . PHE D 4 37  ? 41.652  -60.118 -120.229 1.000 265.160 ? 37  PHE FFF CZ  1 
ATOM 5155 N N   . ARG D 4 38  ? 43.629  -61.998 -126.959 1.000 295.162 ? 38  ARG FFF N   1 
ATOM 5156 C CA  . ARG D 4 38  ? 44.301  -62.031 -128.285 1.000 290.635 ? 38  ARG FFF CA  1 
ATOM 5157 C C   . ARG D 4 38  ? 44.063  -60.703 -128.999 1.000 288.303 ? 38  ARG FFF C   1 
ATOM 5158 O O   . ARG D 4 38  ? 43.021  -60.082 -128.745 1.000 282.681 ? 38  ARG FFF O   1 
ATOM 5159 C CB  . ARG D 4 38  ? 43.817  -63.215 -129.124 1.000 289.782 ? 38  ARG FFF CB  1 
ATOM 5160 C CG  . ARG D 4 38  ? 42.362  -63.131 -129.556 1.000 286.002 ? 38  ARG FFF CG  1 
ATOM 5161 C CD  . ARG D 4 38  ? 41.952  -64.430 -130.201 1.000 279.453 ? 38  ARG FFF CD  1 
ATOM 5162 N NE  . ARG D 4 38  ? 40.543  -64.458 -130.522 1.000 272.740 ? 38  ARG FFF NE  1 
ATOM 5163 C CZ  . ARG D 4 38  ? 39.935  -65.497 -131.064 1.000 274.240 ? 38  ARG FFF CZ  1 
ATOM 5164 N NH1 . ARG D 4 38  ? 40.620  -66.589 -131.359 1.000 276.019 ? 38  ARG FFF NH1 1 
ATOM 5165 N NH2 . ARG D 4 38  ? 38.643  -65.427 -131.328 1.000 285.424 ? 38  ARG FFF NH2 1 
ATOM 5166 N N   . GLN D 4 39  ? 45.007  -60.310 -129.852 1.000 289.918 ? 39  GLN FFF N   1 
ATOM 5167 C CA  . GLN D 4 39  ? 44.919  -59.106 -130.711 1.000 292.740 ? 39  GLN FFF CA  1 
ATOM 5168 C C   . GLN D 4 39  ? 45.276  -59.503 -132.148 1.000 296.274 ? 39  GLN FFF C   1 
ATOM 5169 O O   . GLN D 4 39  ? 46.452  -59.864 -132.391 1.000 301.156 ? 39  GLN FFF O   1 
ATOM 5170 C CB  . GLN D 4 39  ? 45.847  -58.041 -130.144 1.000 292.431 ? 39  GLN FFF CB  1 
ATOM 5171 C CG  . GLN D 4 39  ? 45.605  -56.658 -130.710 1.000 296.083 ? 39  GLN FFF CG  1 
ATOM 5172 C CD  . GLN D 4 39  ? 46.034  -55.620 -129.704 1.000 298.645 ? 39  GLN FFF CD  1 
ATOM 5173 O OE1 . GLN D 4 39  ? 47.001  -55.804 -128.972 1.000 296.861 ? 39  GLN FFF OE1 1 
ATOM 5174 N NE2 . GLN D 4 39  ? 45.292  -54.528 -129.638 1.000 301.713 ? 39  GLN FFF NE2 1 
ATOM 5175 N N   . ALA D 4 40  ? 44.276  -59.507 -133.036 1.000 295.940 ? 40  ALA FFF N   1 
ATOM 5176 C CA  . ALA D 4 40  ? 44.438  -59.690 -134.496 1.000 299.671 ? 40  ALA FFF CA  1 
ATOM 5177 C C   . ALA D 4 40  ? 44.925  -58.365 -135.068 1.000 300.999 ? 40  ALA FFF C   1 
ATOM 5178 O O   . ALA D 4 40  ? 44.578  -57.311 -134.537 1.000 308.358 ? 40  ALA FFF O   1 
ATOM 5179 C CB  . ALA D 4 40  ? 43.139  -60.139 -135.123 1.000 299.818 ? 40  ALA FFF CB  1 
ATOM 5180 N N   . PRO D 4 41  ? 45.742  -58.377 -136.146 1.000 296.908 ? 41  PRO FFF N   1 
ATOM 5181 C CA  . PRO D 4 41  ? 46.430  -57.171 -136.609 1.000 293.856 ? 41  PRO FFF CA  1 
ATOM 5182 C C   . PRO D 4 41  ? 45.484  -55.965 -136.738 1.000 283.924 ? 41  PRO FFF C   1 
ATOM 5183 O O   . PRO D 4 41  ? 44.511  -56.095 -137.434 1.000 281.052 ? 41  PRO FFF O   1 
ATOM 5184 C CB  . PRO D 4 41  ? 47.004  -57.570 -137.985 1.000 306.443 ? 41  PRO FFF CB  1 
ATOM 5185 C CG  . PRO D 4 41  ? 46.382  -58.924 -138.320 1.000 308.584 ? 41  PRO FFF CG  1 
ATOM 5186 C CD  . PRO D 4 41  ? 46.041  -59.548 -136.982 1.000 303.091 ? 41  PRO FFF CD  1 
ATOM 5187 N N   . GLY D 4 42  ? 45.759  -54.862 -136.029 1.000 277.510 ? 42  GLY FFF N   1 
ATOM 5188 C CA  . GLY D 4 42  ? 45.034  -53.577 -136.142 1.000 275.144 ? 42  GLY FFF CA  1 
ATOM 5189 C C   . GLY D 4 42  ? 43.646  -53.566 -135.502 1.000 272.904 ? 42  GLY FFF C   1 
ATOM 5190 O O   . GLY D 4 42  ? 43.017  -52.485 -135.526 1.000 268.405 ? 42  GLY FFF O   1 
ATOM 5191 N N   . LYS D 4 43  ? 43.175  -54.694 -134.950 1.000 273.529 ? 43  LYS FFF N   1 
ATOM 5192 C CA  . LYS D 4 43  ? 41.829  -54.855 -134.329 1.000 271.400 ? 43  LYS FFF CA  1 
ATOM 5193 C C   . LYS D 4 43  ? 42.027  -54.892 -132.809 1.000 277.300 ? 43  LYS FFF C   1 
ATOM 5194 O O   . LYS D 4 43  ? 43.188  -55.102 -132.405 1.000 278.474 ? 43  LYS FFF O   1 
ATOM 5195 C CB  . LYS D 4 43  ? 41.141  -56.126 -134.851 1.000 268.132 ? 43  LYS FFF CB  1 
ATOM 5196 C CG  . LYS D 4 43  ? 40.979  -56.224 -136.369 1.000 266.282 ? 43  LYS FFF CG  1 
ATOM 5197 C CD  . LYS D 4 43  ? 40.596  -57.604 -136.901 1.000 261.843 ? 43  LYS FFF CD  1 
ATOM 5198 C CE  . LYS D 4 43  ? 39.159  -57.989 -136.620 1.000 258.904 ? 43  LYS FFF CE  1 
ATOM 5199 N NZ  . LYS D 4 43  ? 38.910  -59.420 -136.906 1.000 258.913 ? 43  LYS FFF NZ  1 
ATOM 5200 N N   . GLU D 4 44  ? 40.949  -54.683 -132.033 1.000 284.852 ? 44  GLU FFF N   1 
ATOM 5201 C CA  . GLU D 4 44  ? 40.916  -54.584 -130.539 1.000 280.241 ? 44  GLU FFF CA  1 
ATOM 5202 C C   . GLU D 4 44  ? 41.494  -55.843 -129.886 1.000 281.768 ? 44  GLU FFF C   1 
ATOM 5203 O O   . GLU D 4 44  ? 41.183  -56.935 -130.375 1.000 272.863 ? 44  GLU FFF O   1 
ATOM 5204 C CB  . GLU D 4 44  ? 39.481  -54.501 -129.995 1.000 276.421 ? 44  GLU FFF CB  1 
ATOM 5205 C CG  . GLU D 4 44  ? 38.840  -53.122 -130.045 1.000 276.348 ? 44  GLU FFF CG  1 
ATOM 5206 C CD  . GLU D 4 44  ? 37.753  -52.890 -129.004 1.000 272.693 ? 44  GLU FFF CD  1 
ATOM 5207 O OE1 . GLU D 4 44  ? 38.097  -52.787 -127.798 1.000 264.921 ? 44  GLU FFF OE1 1 
ATOM 5208 O OE2 . GLU D 4 44  ? 36.568  -52.814 -129.400 1.000 271.097 ? 44  GLU FFF OE2 1 
ATOM 5209 N N   . ARG D 4 45  ? 42.217  -55.694 -128.770 1.000 293.559 ? 45  ARG FFF N   1 
ATOM 5210 C CA  . ARG D 4 45  ? 42.541  -56.830 -127.866 1.000 298.724 ? 45  ARG FFF CA  1 
ATOM 5211 C C   . ARG D 4 45  ? 41.205  -57.349 -127.316 1.000 302.657 ? 45  ARG FFF C   1 
ATOM 5212 O O   . ARG D 4 45  ? 40.357  -56.517 -126.932 1.000 307.388 ? 45  ARG FFF O   1 
ATOM 5213 C CB  . ARG D 4 45  ? 43.524  -56.432 -126.754 1.000 293.458 ? 45  ARG FFF CB  1 
ATOM 5214 C CG  . ARG D 4 45  ? 44.304  -57.612 -126.188 1.000 290.823 ? 45  ARG FFF CG  1 
ATOM 5215 C CD  . ARG D 4 45  ? 45.550  -57.223 -125.432 1.000 288.976 ? 45  ARG FFF CD  1 
ATOM 5216 N NE  . ARG D 4 45  ? 45.350  -56.203 -124.425 1.000 290.833 ? 45  ARG FFF NE  1 
ATOM 5217 C CZ  . ARG D 4 45  ? 46.334  -55.558 -123.809 1.000 291.047 ? 45  ARG FFF CZ  1 
ATOM 5218 N NH1 . ARG D 4 45  ? 47.594  -55.809 -124.124 1.000 288.948 ? 45  ARG FFF NH1 1 
ATOM 5219 N NH2 . ARG D 4 45  ? 46.062  -54.642 -122.892 1.000 292.204 ? 45  ARG FFF NH2 1 
ATOM 5220 N N   . GLU D 4 46  ? 41.011  -58.667 -127.328 1.000 296.876 ? 46  GLU FFF N   1 
ATOM 5221 C CA  . GLU D 4 46  ? 39.702  -59.314 -127.067 1.000 286.179 ? 46  GLU FFF CA  1 
ATOM 5222 C C   . GLU D 4 46  ? 39.908  -60.414 -126.022 1.000 284.012 ? 46  GLU FFF C   1 
ATOM 5223 O O   . GLU D 4 46  ? 40.885  -61.178 -126.183 1.000 285.432 ? 46  GLU FFF O   1 
ATOM 5224 C CB  . GLU D 4 46  ? 39.159  -59.834 -128.399 1.000 280.523 ? 46  GLU FFF CB  1 
ATOM 5225 C CG  . GLU D 4 46  ? 38.026  -60.826 -128.242 1.000 275.871 ? 46  GLU FFF CG  1 
ATOM 5226 C CD  . GLU D 4 46  ? 37.824  -61.739 -129.429 1.000 272.486 ? 46  GLU FFF CD  1 
ATOM 5227 O OE1 . GLU D 4 46  ? 38.800  -61.976 -130.154 1.000 274.781 ? 46  GLU FFF OE1 1 
ATOM 5228 O OE2 . GLU D 4 46  ? 36.687  -62.196 -129.610 1.000 262.929 ? 46  GLU FFF OE2 1 
ATOM 5229 N N   . PHE D 4 47  ? 39.051  -60.467 -124.989 1.000 282.474 ? 47  PHE FFF N   1 
ATOM 5230 C CA  . PHE D 4 47  ? 39.057  -61.524 -123.938 1.000 284.564 ? 47  PHE FFF CA  1 
ATOM 5231 C C   . PHE D 4 47  ? 38.810  -62.887 -124.599 1.000 286.174 ? 47  PHE FFF C   1 
ATOM 5232 O O   . PHE D 4 47  ? 37.874  -62.958 -125.417 1.000 284.117 ? 47  PHE FFF O   1 
ATOM 5233 C CB  . PHE D 4 47  ? 38.005  -61.266 -122.851 1.000 284.043 ? 47  PHE FFF CB  1 
ATOM 5234 C CG  . PHE D 4 47  ? 37.844  -62.420 -121.890 1.000 281.315 ? 47  PHE FFF CG  1 
ATOM 5235 C CD1 . PHE D 4 47  ? 38.814  -62.683 -120.937 1.000 273.659 ? 47  PHE FFF CD1 1 
ATOM 5236 C CD2 . PHE D 4 47  ? 36.764  -63.289 -121.984 1.000 281.425 ? 47  PHE FFF CD2 1 
ATOM 5237 C CE1 . PHE D 4 47  ? 38.694  -63.768 -120.081 1.000 267.849 ? 47  PHE FFF CE1 1 
ATOM 5238 C CE2 . PHE D 4 47  ? 36.644  -64.374 -121.126 1.000 274.299 ? 47  PHE FFF CE2 1 
ATOM 5239 C CZ  . PHE D 4 47  ? 37.608  -64.608 -120.173 1.000 267.958 ? 47  PHE FFF CZ  1 
ATOM 5240 N N   . VAL D 4 48  ? 39.605  -63.914 -124.251 1.000 285.681 ? 48  VAL FFF N   1 
ATOM 5241 C CA  . VAL D 4 48  ? 39.499  -65.302 -124.807 1.000 286.024 ? 48  VAL FFF CA  1 
ATOM 5242 C C   . VAL D 4 48  ? 38.953  -66.233 -123.718 1.000 286.435 ? 48  VAL FFF C   1 
ATOM 5243 O O   . VAL D 4 48  ? 37.865  -66.821 -123.930 1.000 287.670 ? 48  VAL FFF O   1 
ATOM 5244 C CB  . VAL D 4 48  ? 40.848  -65.821 -125.354 1.000 281.445 ? 48  VAL FFF CB  1 
ATOM 5245 C CG1 . VAL D 4 48  ? 40.805  -67.305 -125.707 1.000 279.482 ? 48  VAL FFF CG1 1 
ATOM 5246 C CG2 . VAL D 4 48  ? 41.322  -65.007 -126.546 1.000 275.779 ? 48  VAL FFF CG2 1 
ATOM 5247 N N   . ALA D 4 49  ? 39.704  -66.376 -122.622 1.000 287.286 ? 49  ALA FFF N   1 
ATOM 5248 C CA  . ALA D 4 49  ? 39.459  -67.360 -121.545 1.000 284.859 ? 49  ALA FFF CA  1 
ATOM 5249 C C   . ALA D 4 49  ? 40.120  -66.889 -120.247 1.000 276.010 ? 49  ALA FFF C   1 
ATOM 5250 O O   . ALA D 4 49  ? 41.169  -66.220 -120.318 1.000 266.782 ? 49  ALA FFF O   1 
ATOM 5251 C CB  . ALA D 4 49  ? 39.979  -68.712 -121.974 1.000 287.704 ? 49  ALA FFF CB  1 
ATOM 5252 N N   . ALA D 4 50  ? 39.501  -67.220 -119.115 1.000 275.398 ? 50  ALA FFF N   1 
ATOM 5253 C CA  . ALA D 4 50  ? 40.029  -66.997 -117.749 1.000 281.579 ? 50  ALA FFF CA  1 
ATOM 5254 C C   . ALA D 4 50  ? 39.913  -68.296 -116.950 1.000 273.507 ? 50  ALA FFF C   1 
ATOM 5255 O O   . ALA D 4 50  ? 38.961  -69.079 -117.194 1.000 275.391 ? 50  ALA FFF O   1 
ATOM 5256 C CB  . ALA D 4 50  ? 39.288  -65.875 -117.061 1.000 283.945 ? 50  ALA FFF CB  1 
ATOM 5257 N N   . ILE D 4 51  ? 40.859  -68.503 -116.037 1.000 257.342 ? 51  ILE FFF N   1 
ATOM 5258 C CA  . ILE D 4 51  ? 40.885  -69.667 -115.113 1.000 247.681 ? 51  ILE FFF CA  1 
ATOM 5259 C C   . ILE D 4 51  ? 41.157  -69.116 -113.708 1.000 247.838 ? 51  ILE FFF C   1 
ATOM 5260 O O   . ILE D 4 51  ? 42.090  -68.307 -113.557 1.000 254.165 ? 51  ILE FFF O   1 
ATOM 5261 C CB  . ILE D 4 51  ? 41.912  -70.716 -115.589 1.000 241.150 ? 51  ILE FFF CB  1 
ATOM 5262 C CG1 . ILE D 4 51  ? 41.780  -72.024 -114.810 1.000 236.997 ? 51  ILE FFF CG1 1 
ATOM 5263 C CG2 . ILE D 4 51  ? 43.334  -70.173 -115.548 1.000 240.737 ? 51  ILE FFF CG2 1 
ATOM 5264 C CD1 . ILE D 4 51  ? 42.542  -73.182 -115.408 1.000 236.018 ? 51  ILE FFF CD1 1 
ATOM 5265 N N   . ARG D 4 52  ? 40.318  -69.471 -112.732 1.000 237.684 ? 52  ARG FFF N   1 
ATOM 5266 C CA  . ARG D 4 52  ? 40.608  -69.211 -111.303 1.000 224.211 ? 52  ARG FFF CA  1 
ATOM 5267 C C   . ARG D 4 52  ? 41.735  -70.163 -110.908 1.000 222.556 ? 52  ARG FFF C   1 
ATOM 5268 O O   . ARG D 4 52  ? 41.636  -71.374 -111.178 1.000 219.227 ? 52  ARG FFF O   1 
ATOM 5269 C CB  . ARG D 4 52  ? 39.379  -69.389 -110.407 1.000 218.203 ? 52  ARG FFF CB  1 
ATOM 5270 C CG  . ARG D 4 52  ? 39.615  -68.881 -108.992 1.000 209.457 ? 52  ARG FFF CG  1 
ATOM 5271 C CD  . ARG D 4 52  ? 38.452  -69.048 -108.056 1.000 209.763 ? 52  ARG FFF CD  1 
ATOM 5272 N NE  . ARG D 4 52  ? 37.233  -68.420 -108.543 1.000 210.310 ? 52  ARG FFF NE  1 
ATOM 5273 C CZ  . ARG D 4 52  ? 36.895  -67.139 -108.413 1.000 208.225 ? 52  ARG FFF CZ  1 
ATOM 5274 N NH1 . ARG D 4 52  ? 37.695  -66.277 -107.819 1.000 203.907 ? 52  ARG FFF NH1 1 
ATOM 5275 N NH2 . ARG D 4 52  ? 35.734  -66.719 -108.887 1.000 211.906 ? 52  ARG FFF NH2 1 
ATOM 5276 N N   . TRP D 4 53  ? 42.788  -69.625 -110.312 1.000 224.138 ? 53  TRP FFF N   1 
ATOM 5277 C CA  . TRP D 4 53  ? 43.962  -70.422 -109.889 1.000 222.692 ? 53  TRP FFF CA  1 
ATOM 5278 C C   . TRP D 4 53  ? 43.510  -71.528 -108.919 1.000 220.425 ? 53  TRP FFF C   1 
ATOM 5279 O O   . TRP D 4 53  ? 43.918  -72.675 -109.116 1.000 217.374 ? 53  TRP FFF O   1 
ATOM 5280 C CB  . TRP D 4 53  ? 45.037  -69.499 -109.312 1.000 221.056 ? 53  TRP FFF CB  1 
ATOM 5281 C CG  . TRP D 4 53  ? 46.403  -70.074 -109.471 1.000 219.020 ? 53  TRP FFF CG  1 
ATOM 5282 C CD1 . TRP D 4 53  ? 47.197  -70.575 -108.485 1.000 219.199 ? 53  TRP FFF CD1 1 
ATOM 5283 C CD2 . TRP D 4 53  ? 47.112  -70.276 -110.706 1.000 220.507 ? 53  TRP FFF CD2 1 
ATOM 5284 N NE1 . TRP D 4 53  ? 48.373  -71.034 -109.013 1.000 219.750 ? 53  TRP FFF NE1 1 
ATOM 5285 C CE2 . TRP D 4 53  ? 48.348  -70.874 -110.375 1.000 220.444 ? 53  TRP FFF CE2 1 
ATOM 5286 C CE3 . TRP D 4 53  ? 46.828  -70.018 -112.052 1.000 218.380 ? 53  TRP FFF CE3 1 
ATOM 5287 C CZ2 . TRP D 4 53  ? 49.296  -71.211 -111.342 1.000 218.133 ? 53  TRP FFF CZ2 1 
ATOM 5288 C CZ3 . TRP D 4 53  ? 47.767  -70.350 -113.001 1.000 216.053 ? 53  TRP FFF CZ3 1 
ATOM 5289 C CH2 . TRP D 4 53  ? 48.987  -70.926 -112.650 1.000 215.807 ? 53  TRP FFF CH2 1 
ATOM 5290 N N   . SER D 4 54  ? 42.658  -71.211 -107.939 1.000 220.553 ? 54  SER FFF N   1 
ATOM 5291 C CA  . SER D 4 54  ? 42.020  -72.217 -107.048 1.000 222.146 ? 54  SER FFF CA  1 
ATOM 5292 C C   . SER D 4 54  ? 40.867  -72.911 -107.775 1.000 224.077 ? 54  SER FFF C   1 
ATOM 5293 O O   . SER D 4 54  ? 39.929  -72.204 -108.228 1.000 221.944 ? 54  SER FFF O   1 
ATOM 5294 C CB  . SER D 4 54  ? 41.525  -71.629 -105.761 1.000 221.713 ? 54  SER FFF CB  1 
ATOM 5295 O OG  . SER D 4 54  ? 40.623  -72.535 -105.129 1.000 219.710 ? 54  SER FFF OG  1 
ATOM 5296 N N   . GLY D 4 55  ? 40.937  -74.243 -107.863 1.000 226.783 ? 55  GLY FFF N   1 
ATOM 5297 C CA  . GLY D 4 55  ? 39.848  -75.104 -108.357 1.000 231.510 ? 55  GLY FFF CA  1 
ATOM 5298 C C   . GLY D 4 55  ? 39.961  -75.307 -109.854 1.000 242.331 ? 55  GLY FFF C   1 
ATOM 5299 O O   . GLY D 4 55  ? 39.599  -76.395 -110.340 1.000 247.982 ? 55  GLY FFF O   1 
ATOM 5300 N N   . GLY D 4 56  ? 40.441  -74.288 -110.572 1.000 249.037 ? 56  GLY FFF N   1 
ATOM 5301 C CA  . GLY D 4 56  ? 40.738  -74.367 -112.013 1.000 248.451 ? 56  GLY FFF CA  1 
ATOM 5302 C C   . GLY D 4 56  ? 39.499  -74.139 -112.854 1.000 248.581 ? 56  GLY FFF C   1 
ATOM 5303 O O   . GLY D 4 56  ? 39.557  -74.467 -114.059 1.000 250.292 ? 56  GLY FFF O   1 
ATOM 5304 N N   . SER D 4 57  ? 38.442  -73.576 -112.248 1.000 247.574 ? 57  SER FFF N   1 
ATOM 5305 C CA  . SER D 4 57  ? 37.154  -73.204 -112.892 1.000 250.629 ? 57  SER FFF CA  1 
ATOM 5306 C C   . SER D 4 57  ? 37.422  -72.183 -114.004 1.000 255.500 ? 57  SER FFF C   1 
ATOM 5307 O O   . SER D 4 57  ? 38.175  -71.221 -113.741 1.000 243.227 ? 57  SER FFF O   1 
ATOM 5308 C CB  . SER D 4 57  ? 36.158  -72.683 -111.880 1.000 244.940 ? 57  SER FFF CB  1 
ATOM 5309 O OG  . SER D 4 57  ? 35.639  -73.728 -111.066 1.000 239.829 ? 57  SER FFF OG  1 
ATOM 5310 N N   . ALA D 4 58  ? 36.810  -72.396 -115.182 1.000 262.848 ? 58  ALA FFF N   1 
ATOM 5311 C CA  . ALA D 4 58  ? 37.099  -71.682 -116.447 1.000 257.110 ? 58  ALA FFF CA  1 
ATOM 5312 C C   . ALA D 4 58  ? 35.852  -70.954 -116.972 1.000 254.666 ? 58  ALA FFF C   1 
ATOM 5313 O O   . ALA D 4 58  ? 34.696  -71.485 -116.815 1.000 237.257 ? 58  ALA FFF O   1 
ATOM 5314 C CB  . ALA D 4 58  ? 37.638  -72.650 -117.470 1.000 260.600 ? 58  ALA FFF CB  1 
ATOM 5315 N N   . TYR D 4 59  ? 36.108  -69.777 -117.563 1.000 256.897 ? 59  TYR FFF N   1 
ATOM 5316 C CA  . TYR D 4 59  ? 35.135  -68.912 -118.280 1.000 262.396 ? 59  TYR FFF CA  1 
ATOM 5317 C C   . TYR D 4 59  ? 35.721  -68.509 -119.639 1.000 260.410 ? 59  TYR FFF C   1 
ATOM 5318 O O   . TYR D 4 59  ? 36.902  -68.106 -119.709 1.000 247.933 ? 59  TYR FFF O   1 
ATOM 5319 C CB  . TYR D 4 59  ? 34.792  -67.679 -117.445 1.000 265.297 ? 59  TYR FFF CB  1 
ATOM 5320 C CG  . TYR D 4 59  ? 33.635  -66.868 -117.973 1.000 265.684 ? 59  TYR FFF CG  1 
ATOM 5321 C CD1 . TYR D 4 59  ? 32.324  -67.263 -117.741 1.000 263.288 ? 59  TYR FFF CD1 1 
ATOM 5322 C CD2 . TYR D 4 59  ? 33.846  -65.708 -118.702 1.000 262.366 ? 59  TYR FFF CD2 1 
ATOM 5323 C CE1 . TYR D 4 59  ? 31.252  -66.517 -118.199 1.000 257.906 ? 59  TYR FFF CE1 1 
ATOM 5324 C CE2 . TYR D 4 59  ? 32.786  -64.957 -119.177 1.000 259.117 ? 59  TYR FFF CE2 1 
ATOM 5325 C CZ  . TYR D 4 59  ? 31.488  -65.358 -118.915 1.000 257.713 ? 59  TYR FFF CZ  1 
ATOM 5326 O OH  . TYR D 4 59  ? 30.443  -64.614 -119.366 1.000 258.866 ? 59  TYR FFF OH  1 
ATOM 5327 N N   . TYR D 4 60  ? 34.903  -68.631 -120.688 1.000 260.898 ? 60  TYR FFF N   1 
ATOM 5328 C CA  . TYR D 4 60  ? 35.301  -68.459 -122.111 1.000 258.958 ? 60  TYR FFF CA  1 
ATOM 5329 C C   . TYR D 4 60  ? 34.375  -67.431 -122.768 1.000 256.415 ? 60  TYR FFF C   1 
ATOM 5330 O O   . TYR D 4 60  ? 33.170  -67.372 -122.433 1.000 253.700 ? 60  TYR FFF O   1 
ATOM 5331 C CB  . TYR D 4 60  ? 35.230  -69.789 -122.873 1.000 256.062 ? 60  TYR FFF CB  1 
ATOM 5332 C CG  . TYR D 4 60  ? 36.083  -70.913 -122.337 1.000 258.928 ? 60  TYR FFF CG  1 
ATOM 5333 C CD1 . TYR D 4 60  ? 37.379  -71.110 -122.792 1.000 254.891 ? 60  TYR FFF CD1 1 
ATOM 5334 C CD2 . TYR D 4 60  ? 35.572  -71.820 -121.413 1.000 256.186 ? 60  TYR FFF CD2 1 
ATOM 5335 C CE1 . TYR D 4 60  ? 38.160  -72.149 -122.307 1.000 255.357 ? 60  TYR FFF CE1 1 
ATOM 5336 C CE2 . TYR D 4 60  ? 36.338  -72.862 -120.917 1.000 252.799 ? 60  TYR FFF CE2 1 
ATOM 5337 C CZ  . TYR D 4 60  ? 37.637  -73.028 -121.366 1.000 255.226 ? 60  TYR FFF CZ  1 
ATOM 5338 O OH  . TYR D 4 60  ? 38.383  -74.064 -120.876 1.000 254.006 ? 60  TYR FFF OH  1 
ATOM 5339 N N   . ALA D 4 61  ? 34.918  -66.644 -123.692 1.000 254.568 ? 61  ALA FFF N   1 
ATOM 5340 C CA  . ALA D 4 61  ? 34.115  -65.825 -124.620 1.000 256.854 ? 61  ALA FFF CA  1 
ATOM 5341 C C   . ALA D 4 61  ? 33.422  -66.774 -125.612 1.000 262.815 ? 61  ALA FFF C   1 
ATOM 5342 O O   . ALA D 4 61  ? 33.976  -67.880 -125.890 1.000 270.103 ? 61  ALA FFF O   1 
ATOM 5343 C CB  . ALA D 4 61  ? 35.001  -64.809 -125.283 1.000 257.338 ? 61  ALA FFF CB  1 
ATOM 5344 N N   . ASP D 4 62  ? 32.239  -66.390 -126.105 1.000 266.701 ? 62  ASP FFF N   1 
ATOM 5345 C CA  . ASP D 4 62  ? 31.394  -67.239 -126.993 1.000 271.207 ? 62  ASP FFF CA  1 
ATOM 5346 C C   . ASP D 4 62  ? 32.199  -67.634 -128.244 1.000 266.134 ? 62  ASP FFF C   1 
ATOM 5347 O O   . ASP D 4 62  ? 31.978  -68.752 -128.739 1.000 262.319 ? 62  ASP FFF O   1 
ATOM 5348 C CB  . ASP D 4 62  ? 30.060  -66.563 -127.348 1.000 279.428 ? 62  ASP FFF CB  1 
ATOM 5349 C CG  . ASP D 4 62  ? 28.997  -66.591 -126.247 1.000 279.858 ? 62  ASP FFF CG  1 
ATOM 5350 O OD1 . ASP D 4 62  ? 29.285  -66.090 -125.129 1.000 276.364 ? 62  ASP FFF OD1 1 
ATOM 5351 O OD2 . ASP D 4 62  ? 27.867  -67.098 -126.515 1.000 279.634 ? 62  ASP FFF OD2 1 
ATOM 5352 N N   . SER D 4 63  ? 33.135  -66.782 -128.683 1.000 260.009 ? 63  SER FFF N   1 
ATOM 5353 C CA  . SER D 4 63  ? 33.949  -66.932 -129.921 1.000 263.858 ? 63  SER FFF CA  1 
ATOM 5354 C C   . SER D 4 63  ? 34.800  -68.219 -129.951 1.000 273.690 ? 63  SER FFF C   1 
ATOM 5355 O O   . SER D 4 63  ? 35.148  -68.679 -131.082 1.000 289.626 ? 63  SER FFF O   1 
ATOM 5356 C CB  . SER D 4 63  ? 34.810  -65.715 -130.118 1.000 256.100 ? 63  SER FFF CB  1 
ATOM 5357 O OG  . SER D 4 63  ? 35.753  -65.549 -129.073 1.000 241.305 ? 63  SER FFF OG  1 
ATOM 5358 N N   . VAL D 4 64  ? 35.152  -68.781 -128.791 1.000 273.253 ? 64  VAL FFF N   1 
ATOM 5359 C CA  . VAL D 4 64  ? 36.062  -69.964 -128.707 1.000 273.174 ? 64  VAL FFF CA  1 
ATOM 5360 C C   . VAL D 4 64  ? 35.412  -71.096 -127.905 1.000 276.592 ? 64  VAL FFF C   1 
ATOM 5361 O O   . VAL D 4 64  ? 36.010  -72.200 -127.912 1.000 277.376 ? 64  VAL FFF O   1 
ATOM 5362 C CB  . VAL D 4 64  ? 37.432  -69.574 -128.120 1.000 270.224 ? 64  VAL FFF CB  1 
ATOM 5363 C CG1 . VAL D 4 64  ? 38.118  -68.546 -128.993 1.000 268.082 ? 64  VAL FFF CG1 1 
ATOM 5364 C CG2 . VAL D 4 64  ? 37.336  -69.077 -126.681 1.000 268.359 ? 64  VAL FFF CG2 1 
ATOM 5365 N N   . LYS D 4 65  ? 34.275  -70.839 -127.233 1.000 276.770 ? 65  LYS FFF N   1 
ATOM 5366 C CA  . LYS D 4 65  ? 33.573  -71.844 -126.391 1.000 270.295 ? 65  LYS FFF CA  1 
ATOM 5367 C C   . LYS D 4 65  ? 33.337  -73.084 -127.264 1.000 282.013 ? 65  LYS FFF C   1 
ATOM 5368 O O   . LYS D 4 65  ? 32.912  -72.923 -128.435 1.000 283.042 ? 65  LYS FFF O   1 
ATOM 5369 C CB  . LYS D 4 65  ? 32.272  -71.304 -125.784 1.000 258.481 ? 65  LYS FFF CB  1 
ATOM 5370 C CG  . LYS D 4 65  ? 31.678  -72.226 -124.726 1.000 253.832 ? 65  LYS FFF CG  1 
ATOM 5371 C CD  . LYS D 4 65  ? 30.654  -71.619 -123.808 1.000 255.342 ? 65  LYS FFF CD  1 
ATOM 5372 C CE  . LYS D 4 65  ? 30.858  -72.080 -122.375 1.000 256.481 ? 65  LYS FFF CE  1 
ATOM 5373 N NZ  . LYS D 4 65  ? 29.840  -71.547 -121.438 1.000 254.087 ? 65  LYS FFF NZ  1 
ATOM 5374 N N   . GLY D 4 66  ? 33.697  -74.264 -126.748 1.000 290.020 ? 66  GLY FFF N   1 
ATOM 5375 C CA  . GLY D 4 66  ? 33.520  -75.559 -127.432 1.000 294.508 ? 66  GLY FFF CA  1 
ATOM 5376 C C   . GLY D 4 66  ? 34.710  -75.919 -128.303 1.000 296.919 ? 66  GLY FFF C   1 
ATOM 5377 O O   . GLY D 4 66  ? 34.706  -77.049 -128.848 1.000 304.786 ? 66  GLY FFF O   1 
ATOM 5378 N N   . ARG D 4 67  ? 35.677  -75.002 -128.448 1.000 293.527 ? 67  ARG FFF N   1 
ATOM 5379 C CA  . ARG D 4 67  ? 36.921  -75.215 -129.235 1.000 295.572 ? 67  ARG FFF CA  1 
ATOM 5380 C C   . ARG D 4 67  ? 38.140  -75.157 -128.301 1.000 292.248 ? 67  ARG FFF C   1 
ATOM 5381 O O   . ARG D 4 67  ? 38.959  -76.086 -128.354 1.000 301.069 ? 67  ARG FFF O   1 
ATOM 5382 C CB  . ARG D 4 67  ? 37.018  -74.209 -130.388 1.000 294.066 ? 67  ARG FFF CB  1 
ATOM 5383 C CG  . ARG D 4 67  ? 35.952  -74.395 -131.462 1.000 296.338 ? 67  ARG FFF CG  1 
ATOM 5384 C CD  . ARG D 4 67  ? 36.190  -73.589 -132.727 1.000 295.868 ? 67  ARG FFF CD  1 
ATOM 5385 N NE  . ARG D 4 67  ? 36.359  -72.156 -132.491 1.000 293.011 ? 67  ARG FFF NE  1 
ATOM 5386 C CZ  . ARG D 4 67  ? 37.493  -71.470 -132.660 1.000 292.488 ? 67  ARG FFF CZ  1 
ATOM 5387 N NH1 . ARG D 4 67  ? 38.599  -72.073 -133.071 1.000 294.239 ? 67  ARG FFF NH1 1 
ATOM 5388 N NH2 . ARG D 4 67  ? 37.510  -70.168 -132.424 1.000 291.877 ? 67  ARG FFF NH2 1 
ATOM 5389 N N   . PHE D 4 68  ? 38.287  -74.107 -127.493 1.000 284.870 ? 68  PHE FFF N   1 
ATOM 5390 C CA  . PHE D 4 68  ? 39.519  -73.860 -126.694 1.000 285.591 ? 68  PHE FFF CA  1 
ATOM 5391 C C   . PHE D 4 68  ? 39.369  -74.445 -125.286 1.000 292.716 ? 68  PHE FFF C   1 
ATOM 5392 O O   . PHE D 4 68  ? 38.235  -74.483 -124.784 1.000 306.994 ? 68  PHE FFF O   1 
ATOM 5393 C CB  . PHE D 4 68  ? 39.827  -72.364 -126.646 1.000 283.871 ? 68  PHE FFF CB  1 
ATOM 5394 C CG  . PHE D 4 68  ? 40.359  -71.796 -127.936 1.000 287.641 ? 68  PHE FFF CG  1 
ATOM 5395 C CD1 . PHE D 4 68  ? 40.243  -72.485 -129.133 1.000 290.150 ? 68  PHE FFF CD1 1 
ATOM 5396 C CD2 . PHE D 4 68  ? 40.952  -70.543 -127.958 1.000 291.915 ? 68  PHE FFF CD2 1 
ATOM 5397 C CE1 . PHE D 4 68  ? 40.734  -71.943 -130.311 1.000 292.247 ? 68  PHE FFF CE1 1 
ATOM 5398 C CE2 . PHE D 4 68  ? 41.448  -70.005 -129.137 1.000 288.241 ? 68  PHE FFF CE2 1 
ATOM 5399 C CZ  . PHE D 4 68  ? 41.337  -70.705 -130.311 1.000 289.168 ? 68  PHE FFF CZ  1 
ATOM 5400 N N   . THR D 4 69  ? 40.483  -74.886 -124.689 1.000 292.078 ? 69  THR FFF N   1 
ATOM 5401 C CA  . THR D 4 69  ? 40.606  -75.355 -123.278 1.000 280.863 ? 69  THR FFF CA  1 
ATOM 5402 C C   . THR D 4 69  ? 41.700  -74.535 -122.596 1.000 266.447 ? 69  THR FFF C   1 
ATOM 5403 O O   . THR D 4 69  ? 42.799  -74.485 -123.137 1.000 262.446 ? 69  THR FFF O   1 
ATOM 5404 C CB  . THR D 4 69  ? 40.949  -76.852 -123.209 1.000 285.210 ? 69  THR FFF CB  1 
ATOM 5405 O OG1 . THR D 4 69  ? 39.825  -77.583 -123.703 1.000 292.792 ? 69  THR FFF OG1 1 
ATOM 5406 C CG2 . THR D 4 69  ? 41.319  -77.341 -121.824 1.000 282.178 ? 69  THR FFF CG2 1 
ATOM 5407 N N   . ILE D 4 70  ? 41.406  -73.910 -121.461 1.000 256.995 ? 70  ILE FFF N   1 
ATOM 5408 C CA  . ILE D 4 70  ? 42.436  -73.284 -120.579 1.000 250.545 ? 70  ILE FFF CA  1 
ATOM 5409 C C   . ILE D 4 70  ? 42.632  -74.237 -119.392 1.000 251.164 ? 70  ILE FFF C   1 
ATOM 5410 O O   . ILE D 4 70  ? 41.630  -74.812 -118.938 1.000 254.332 ? 70  ILE FFF O   1 
ATOM 5411 C CB  . ILE D 4 70  ? 42.027  -71.846 -120.189 1.000 243.472 ? 70  ILE FFF CB  1 
ATOM 5412 C CG1 . ILE D 4 70  ? 43.153  -71.089 -119.485 1.000 241.054 ? 70  ILE FFF CG1 1 
ATOM 5413 C CG2 . ILE D 4 70  ? 40.753  -71.830 -119.358 1.000 243.521 ? 70  ILE FFF CG2 1 
ATOM 5414 C CD1 . ILE D 4 70  ? 42.797  -69.655 -119.133 1.000 241.012 ? 70  ILE FFF CD1 1 
ATOM 5415 N N   . SER D 4 71  ? 43.879  -74.505 -118.997 1.000 254.298 ? 71  SER FFF N   1 
ATOM 5416 C CA  . SER D 4 71  ? 44.245  -75.411 -117.871 1.000 257.587 ? 71  SER FFF CA  1 
ATOM 5417 C C   . SER D 4 71  ? 45.486  -74.844 -117.173 1.000 261.464 ? 71  SER FFF C   1 
ATOM 5418 O O   . SER D 4 71  ? 46.064  -73.906 -117.731 1.000 265.646 ? 71  SER FFF O   1 
ATOM 5419 C CB  . SER D 4 71  ? 44.451  -76.833 -118.345 1.000 255.606 ? 71  SER FFF CB  1 
ATOM 5420 O OG  . SER D 4 71  ? 45.636  -76.949 -119.111 1.000 254.933 ? 71  SER FFF OG  1 
ATOM 5421 N N   . ARG D 4 72  ? 45.856  -75.340 -115.988 1.000 261.344 ? 72  ARG FFF N   1 
ATOM 5422 C CA  . ARG D 4 72  ? 47.050  -74.832 -115.260 1.000 262.793 ? 72  ARG FFF CA  1 
ATOM 5423 C C   . ARG D 4 72  ? 47.625  -75.936 -114.365 1.000 259.056 ? 72  ARG FFF C   1 
ATOM 5424 O O   . ARG D 4 72  ? 46.836  -76.745 -113.862 1.000 261.392 ? 72  ARG FFF O   1 
ATOM 5425 C CB  . ARG D 4 72  ? 46.679  -73.540 -114.512 1.000 269.292 ? 72  ARG FFF CB  1 
ATOM 5426 C CG  . ARG D 4 72  ? 45.541  -73.646 -113.503 1.000 268.951 ? 72  ARG FFF CG  1 
ATOM 5427 C CD  . ARG D 4 72  ? 46.079  -73.861 -112.108 1.000 267.658 ? 72  ARG FFF CD  1 
ATOM 5428 N NE  . ARG D 4 72  ? 45.061  -74.157 -111.109 1.000 270.269 ? 72  ARG FFF NE  1 
ATOM 5429 C CZ  . ARG D 4 72  ? 44.445  -75.329 -110.953 1.000 271.610 ? 72  ARG FFF CZ  1 
ATOM 5430 N NH1 . ARG D 4 72  ? 44.687  -76.344 -111.766 1.000 272.376 ? 72  ARG FFF NH1 1 
ATOM 5431 N NH2 . ARG D 4 72  ? 43.559  -75.476 -109.985 1.000 274.505 ? 72  ARG FFF NH2 1 
ATOM 5432 N N   . ASP D 4 73  ? 48.952  -75.985 -114.208 1.000 254.471 ? 73  ASP FFF N   1 
ATOM 5433 C CA  . ASP D 4 73  ? 49.627  -76.771 -113.137 1.000 252.334 ? 73  ASP FFF CA  1 
ATOM 5434 C C   . ASP D 4 73  ? 50.158  -75.784 -112.094 1.000 255.211 ? 73  ASP FFF C   1 
ATOM 5435 O O   . ASP D 4 73  ? 51.084  -75.032 -112.429 1.000 258.357 ? 73  ASP FFF O   1 
ATOM 5436 C CB  . ASP D 4 73  ? 50.731  -77.669 -113.703 1.000 251.918 ? 73  ASP FFF CB  1 
ATOM 5437 C CG  . ASP D 4 73  ? 51.478  -78.508 -112.671 1.000 245.508 ? 73  ASP FFF CG  1 
ATOM 5438 O OD1 . ASP D 4 73  ? 51.400  -78.206 -111.477 1.000 232.922 ? 73  ASP FFF OD1 1 
ATOM 5439 O OD2 . ASP D 4 73  ? 52.160  -79.460 -113.078 1.000 253.398 ? 73  ASP FFF OD2 1 
ATOM 5440 N N   . LYS D 4 74  ? 49.582  -75.793 -110.887 1.000 259.989 ? 74  LYS FFF N   1 
ATOM 5441 C CA  . LYS D 4 74  ? 49.902  -74.868 -109.757 1.000 268.478 ? 74  LYS FFF CA  1 
ATOM 5442 C C   . LYS D 4 74  ? 51.372  -75.013 -109.329 1.000 269.139 ? 74  LYS FFF C   1 
ATOM 5443 O O   . LYS D 4 74  ? 52.069  -73.978 -109.244 1.000 265.226 ? 74  LYS FFF O   1 
ATOM 5444 C CB  . LYS D 4 74  ? 48.977  -75.140 -108.562 1.000 271.327 ? 74  LYS FFF CB  1 
ATOM 5445 C CG  . LYS D 4 74  ? 47.489  -74.943 -108.838 1.000 271.974 ? 74  LYS FFF CG  1 
ATOM 5446 C CD  . LYS D 4 74  ? 46.593  -75.192 -107.646 1.000 264.502 ? 74  LYS FFF CD  1 
ATOM 5447 C CE  . LYS D 4 74  ? 46.237  -73.939 -106.880 1.000 262.606 ? 74  LYS FFF CE  1 
ATOM 5448 N NZ  . LYS D 4 74  ? 45.233  -74.262 -105.836 1.000 263.124 ? 74  LYS FFF NZ  1 
ATOM 5449 N N   . ALA D 4 75  ? 51.820  -76.246 -109.067 1.000 268.367 ? 75  ALA FFF N   1 
ATOM 5450 C CA  . ALA D 4 75  ? 53.202  -76.586 -108.653 1.000 266.119 ? 75  ALA FFF CA  1 
ATOM 5451 C C   . ALA D 4 75  ? 54.206  -75.956 -109.625 1.000 270.673 ? 75  ALA FFF C   1 
ATOM 5452 O O   . ALA D 4 75  ? 55.237  -75.461 -109.124 1.000 266.248 ? 75  ALA FFF O   1 
ATOM 5453 C CB  . ALA D 4 75  ? 53.381  -78.081 -108.595 1.000 265.749 ? 75  ALA FFF CB  1 
ATOM 5454 N N   . LYS D 4 76  ? 53.906  -75.973 -110.939 1.000 274.995 ? 76  LYS FFF N   1 
ATOM 5455 C CA  . LYS D 4 76  ? 54.791  -75.485 -112.043 1.000 273.939 ? 76  LYS FFF CA  1 
ATOM 5456 C C   . LYS D 4 76  ? 54.512  -74.006 -112.380 1.000 269.700 ? 76  LYS FFF C   1 
ATOM 5457 O O   . LYS D 4 76  ? 55.261  -73.457 -113.210 1.000 272.308 ? 76  LYS FFF O   1 
ATOM 5458 C CB  . LYS D 4 76  ? 54.619  -76.346 -113.302 1.000 279.339 ? 76  LYS FFF CB  1 
ATOM 5459 C CG  . LYS D 4 76  ? 55.425  -77.642 -113.350 1.000 286.274 ? 76  LYS FFF CG  1 
ATOM 5460 C CD  . LYS D 4 76  ? 55.182  -78.444 -114.636 1.000 294.726 ? 76  LYS FFF CD  1 
ATOM 5461 C CE  . LYS D 4 76  ? 55.474  -79.930 -114.535 1.000 294.933 ? 76  LYS FFF CE  1 
ATOM 5462 N NZ  . LYS D 4 76  ? 56.912  -80.211 -114.303 1.000 297.940 ? 76  LYS FFF NZ  1 
ATOM 5463 N N   . ASN D 4 77  ? 53.504  -73.381 -111.757 1.000 262.982 ? 77  ASN FFF N   1 
ATOM 5464 C CA  . ASN D 4 77  ? 53.067  -71.979 -112.008 1.000 256.905 ? 77  ASN FFF CA  1 
ATOM 5465 C C   . ASN D 4 77  ? 52.957  -71.727 -113.510 1.000 252.707 ? 77  ASN FFF C   1 
ATOM 5466 O O   . ASN D 4 77  ? 53.473  -70.674 -113.962 1.000 257.748 ? 77  ASN FFF O   1 
ATOM 5467 C CB  . ASN D 4 77  ? 53.998  -70.951 -111.365 1.000 255.315 ? 77  ASN FFF CB  1 
ATOM 5468 C CG  . ASN D 4 77  ? 53.713  -70.772 -109.890 1.000 251.228 ? 77  ASN FFF CG  1 
ATOM 5469 O OD1 . ASN D 4 77  ? 52.603  -70.416 -109.496 1.000 242.143 ? 77  ASN FFF OD1 1 
ATOM 5470 N ND2 . ASN D 4 77  ? 54.706  -71.048 -109.070 1.000 253.458 ? 77  ASN FFF ND2 1 
ATOM 5471 N N   . THR D 4 78  ? 52.311  -72.647 -114.232 1.000 247.094 ? 78  THR FFF N   1 
ATOM 5472 C CA  . THR D 4 78  ? 52.116  -72.563 -115.698 1.000 245.859 ? 78  THR FFF CA  1 
ATOM 5473 C C   . THR D 4 78  ? 50.653  -72.790 -116.057 1.000 244.068 ? 78  THR FFF C   1 
ATOM 5474 O O   . THR D 4 78  ? 50.093  -73.826 -115.638 1.000 228.966 ? 78  THR FFF O   1 
ATOM 5475 C CB  . THR D 4 78  ? 52.994  -73.565 -116.440 1.000 246.479 ? 78  THR FFF CB  1 
ATOM 5476 O OG1 . THR D 4 78  ? 54.327  -73.322 -115.991 1.000 243.993 ? 78  THR FFF OG1 1 
ATOM 5477 C CG2 . THR D 4 78  ? 52.880  -73.424 -117.942 1.000 251.243 ? 78  THR FFF CG2 1 
ATOM 5478 N N   . VAL D 4 79  ? 50.109  -71.838 -116.824 1.000 255.016 ? 79  VAL FFF N   1 
ATOM 5479 C CA  . VAL D 4 79  ? 48.751  -71.865 -117.446 1.000 264.390 ? 79  VAL FFF CA  1 
ATOM 5480 C C   . VAL D 4 79  ? 48.920  -72.178 -118.943 1.000 275.618 ? 79  VAL FFF C   1 
ATOM 5481 O O   . VAL D 4 79  ? 49.924  -71.745 -119.554 1.000 283.483 ? 79  VAL FFF O   1 
ATOM 5482 C CB  . VAL D 4 79  ? 47.955  -70.564 -117.170 1.000 264.798 ? 79  VAL FFF CB  1 
ATOM 5483 C CG1 . VAL D 4 79  ? 48.593  -69.317 -117.769 1.000 266.850 ? 79  VAL FFF CG1 1 
ATOM 5484 C CG2 . VAL D 4 79  ? 46.494  -70.659 -117.595 1.000 260.795 ? 79  VAL FFF CG2 1 
ATOM 5485 N N   . TYR D 4 80  ? 47.983  -72.946 -119.499 1.000 275.519 ? 80  TYR FFF N   1 
ATOM 5486 C CA  . TYR D 4 80  ? 47.990  -73.452 -120.894 1.000 267.441 ? 80  TYR FFF CA  1 
ATOM 5487 C C   . TYR D 4 80  ? 46.699  -72.981 -121.579 1.000 270.853 ? 80  TYR FFF C   1 
ATOM 5488 O O   . TYR D 4 80  ? 45.656  -72.932 -120.906 1.000 273.047 ? 80  TYR FFF O   1 
ATOM 5489 C CB  . TYR D 4 80  ? 48.128  -74.979 -120.875 1.000 258.701 ? 80  TYR FFF CB  1 
ATOM 5490 C CG  . TYR D 4 80  ? 49.361  -75.521 -120.187 1.000 250.069 ? 80  TYR FFF CG  1 
ATOM 5491 C CD1 . TYR D 4 80  ? 50.613  -75.427 -120.777 1.000 246.847 ? 80  TYR FFF CD1 1 
ATOM 5492 C CD2 . TYR D 4 80  ? 49.272  -76.167 -118.960 1.000 241.183 ? 80  TYR FFF CD2 1 
ATOM 5493 C CE1 . TYR D 4 80  ? 51.747  -75.925 -120.148 1.000 241.378 ? 80  TYR FFF CE1 1 
ATOM 5494 C CE2 . TYR D 4 80  ? 50.393  -76.666 -118.316 1.000 237.094 ? 80  TYR FFF CE2 1 
ATOM 5495 C CZ  . TYR D 4 80  ? 51.634  -76.542 -118.911 1.000 238.123 ? 80  TYR FFF CZ  1 
ATOM 5496 O OH  . TYR D 4 80  ? 52.711  -77.057 -118.251 1.000 233.190 ? 80  TYR FFF OH  1 
ATOM 5497 N N   . LEU D 4 81  ? 46.760  -72.607 -122.859 1.000 275.915 ? 81  LEU FFF N   1 
ATOM 5498 C CA  . LEU D 4 81  ? 45.558  -72.474 -123.730 1.000 279.564 ? 81  LEU FFF CA  1 
ATOM 5499 C C   . LEU D 4 81  ? 45.659  -73.510 -124.859 1.000 285.636 ? 81  LEU FFF C   1 
ATOM 5500 O O   . LEU D 4 81  ? 46.566  -73.375 -125.706 1.000 290.166 ? 81  LEU FFF O   1 
ATOM 5501 C CB  . LEU D 4 81  ? 45.441  -71.047 -124.274 1.000 277.470 ? 81  LEU FFF CB  1 
ATOM 5502 C CG  . LEU D 4 81  ? 44.145  -70.739 -125.026 1.000 273.172 ? 81  LEU FFF CG  1 
ATOM 5503 C CD1 . LEU D 4 81  ? 42.958  -70.597 -124.077 1.000 268.939 ? 81  LEU FFF CD1 1 
ATOM 5504 C CD2 . LEU D 4 81  ? 44.312  -69.485 -125.864 1.000 273.194 ? 81  LEU FFF CD2 1 
ATOM 5505 N N   . GLN D 4 82  ? 44.800  -74.538 -124.807 1.000 285.121 ? 82  GLN FFF N   1 
ATOM 5506 C CA  . GLN D 4 82  ? 44.655  -75.617 -125.822 1.000 278.091 ? 82  GLN FFF CA  1 
ATOM 5507 C C   . GLN D 4 82  ? 43.701  -75.110 -126.901 1.000 274.970 ? 82  GLN FFF C   1 
ATOM 5508 O O   . GLN D 4 82  ? 42.493  -74.995 -126.631 1.000 263.997 ? 82  GLN FFF O   1 
ATOM 5509 C CB  . GLN D 4 82  ? 44.125  -76.897 -125.169 1.000 273.625 ? 82  GLN FFF CB  1 
ATOM 5510 C CG  . GLN D 4 82  ? 44.083  -78.109 -126.084 1.000 268.514 ? 82  GLN FFF CG  1 
ATOM 5511 C CD  . GLN D 4 82  ? 45.472  -78.543 -126.466 1.000 267.187 ? 82  GLN FFF CD  1 
ATOM 5512 O OE1 . GLN D 4 82  ? 46.321  -78.768 -125.611 1.000 264.719 ? 82  GLN FFF OE1 1 
ATOM 5513 N NE2 . GLN D 4 82  ? 45.717  -78.643 -127.760 1.000 267.695 ? 82  GLN FFF NE2 1 
ATOM 5514 N N   . MET D 4 83  ? 44.244  -74.778 -128.066 1.000 281.226 ? 83  MET FFF N   1 
ATOM 5515 C CA  . MET D 4 83  ? 43.475  -74.213 -129.204 1.000 293.809 ? 83  MET FFF CA  1 
ATOM 5516 C C   . MET D 4 83  ? 43.119  -75.353 -130.188 1.000 308.778 ? 83  MET FFF C   1 
ATOM 5517 O O   . MET D 4 83  ? 43.916  -75.610 -131.128 1.000 330.419 ? 83  MET FFF O   1 
ATOM 5518 C CB  . MET D 4 83  ? 44.297  -73.097 -129.870 1.000 289.438 ? 83  MET FFF CB  1 
ATOM 5519 C CG  . MET D 4 83  ? 44.873  -72.066 -128.877 1.000 276.769 ? 83  MET FFF CG  1 
ATOM 5520 S SD  . MET D 4 83  ? 46.053  -70.882 -129.606 1.000 262.130 ? 83  MET FFF SD  1 
ATOM 5521 C CE  . MET D 4 83  ? 44.908  -70.011 -130.668 1.000 264.593 ? 83  MET FFF CE  1 
ATOM 5522 N N   . ASN D 4 84  ? 41.975  -76.030 -129.960 1.000 306.316 ? 84  ASN FFF N   1 
ATOM 5523 C CA  . ASN D 4 84  ? 41.450  -77.164 -130.781 1.000 300.731 ? 84  ASN FFF CA  1 
ATOM 5524 C C   . ASN D 4 84  ? 40.582  -76.606 -131.925 1.000 304.739 ? 84  ASN FFF C   1 
ATOM 5525 O O   . ASN D 4 84  ? 40.073  -75.469 -131.779 1.000 295.780 ? 84  ASN FFF O   1 
ATOM 5526 C CB  . ASN D 4 84  ? 40.651  -78.177 -129.946 1.000 291.784 ? 84  ASN FFF CB  1 
ATOM 5527 C CG  . ASN D 4 84  ? 41.354  -78.670 -128.697 1.000 283.786 ? 84  ASN FFF CG  1 
ATOM 5528 O OD1 . ASN D 4 84  ? 42.393  -79.317 -128.777 1.000 282.198 ? 84  ASN FFF OD1 1 
ATOM 5529 N ND2 . ASN D 4 84  ? 40.771  -78.416 -127.537 1.000 273.993 ? 84  ASN FFF ND2 1 
ATOM 5530 N N   . SER D 4 85  ? 40.450  -77.356 -133.029 1.000 307.901 ? 85  SER FFF N   1 
ATOM 5531 C CA  . SER D 4 85  ? 39.763  -76.940 -134.282 1.000 309.177 ? 85  SER FFF CA  1 
ATOM 5532 C C   . SER D 4 85  ? 40.132  -75.493 -134.638 1.000 312.649 ? 85  SER FFF C   1 
ATOM 5533 O O   . SER D 4 85  ? 39.208  -74.653 -134.777 1.000 316.619 ? 85  SER FFF O   1 
ATOM 5534 C CB  . SER D 4 85  ? 38.286  -77.167 -134.183 1.000 304.794 ? 85  SER FFF CB  1 
ATOM 5535 O OG  . SER D 4 85  ? 38.028  -78.560 -134.204 1.000 295.611 ? 85  SER FFF OG  1 
ATOM 5536 N N   . LEU D 4 86  ? 41.440  -75.228 -134.787 1.000 310.109 ? 86  LEU FFF N   1 
ATOM 5537 C CA  . LEU D 4 86  ? 42.006  -73.902 -135.168 1.000 307.919 ? 86  LEU FFF CA  1 
ATOM 5538 C C   . LEU D 4 86  ? 41.266  -73.386 -136.403 1.000 307.507 ? 86  LEU FFF C   1 
ATOM 5539 O O   . LEU D 4 86  ? 41.060  -74.190 -137.324 1.000 325.920 ? 86  LEU FFF O   1 
ATOM 5540 C CB  . LEU D 4 86  ? 43.502  -74.036 -135.464 1.000 305.805 ? 86  LEU FFF CB  1 
ATOM 5541 C CG  . LEU D 4 86  ? 44.424  -74.053 -134.248 1.000 301.360 ? 86  LEU FFF CG  1 
ATOM 5542 C CD1 . LEU D 4 86  ? 45.794  -74.544 -134.651 1.000 304.649 ? 86  LEU FFF CD1 1 
ATOM 5543 C CD2 . LEU D 4 86  ? 44.525  -72.681 -133.597 1.000 290.417 ? 86  LEU FFF CD2 1 
ATOM 5544 N N   . LYS D 4 87  ? 40.888  -72.103 -136.409 1.000 301.712 ? 87  LYS FFF N   1 
ATOM 5545 C CA  . LYS D 4 87  ? 40.177  -71.440 -137.535 1.000 306.362 ? 87  LYS FFF CA  1 
ATOM 5546 C C   . LYS D 4 87  ? 41.004  -70.257 -138.033 1.000 307.742 ? 87  LYS FFF C   1 
ATOM 5547 O O   . LYS D 4 87  ? 41.859  -69.770 -137.280 1.000 294.934 ? 87  LYS FFF O   1 
ATOM 5548 C CB  . LYS D 4 87  ? 38.785  -70.950 -137.128 1.000 307.679 ? 87  LYS FFF CB  1 
ATOM 5549 C CG  . LYS D 4 87  ? 37.753  -72.049 -136.939 1.000 315.093 ? 87  LYS FFF CG  1 
ATOM 5550 C CD  . LYS D 4 87  ? 36.317  -71.545 -136.968 1.000 317.507 ? 87  LYS FFF CD  1 
ATOM 5551 C CE  . LYS D 4 87  ? 35.964  -70.700 -135.765 1.000 310.961 ? 87  LYS FFF CE  1 
ATOM 5552 N NZ  . LYS D 4 87  ? 34.506  -70.485 -135.614 1.000 310.383 ? 87  LYS FFF NZ  1 
ATOM 5553 N N   . TYR D 4 88  ? 40.722  -69.816 -139.261 1.000 320.470 ? 88  TYR FFF N   1 
ATOM 5554 C CA  . TYR D 4 88  ? 41.370  -68.645 -139.903 1.000 320.008 ? 88  TYR FFF CA  1 
ATOM 5555 C C   . TYR D 4 88  ? 41.158  -67.419 -139.006 1.000 311.411 ? 88  TYR FFF C   1 
ATOM 5556 O O   . TYR D 4 88  ? 42.122  -66.657 -138.796 1.000 305.920 ? 88  TYR FFF O   1 
ATOM 5557 C CB  . TYR D 4 88  ? 40.842  -68.430 -141.320 1.000 320.733 ? 88  TYR FFF CB  1 
ATOM 5558 C CG  . TYR D 4 88  ? 41.936  -68.047 -142.278 1.000 323.332 ? 88  TYR FFF CG  1 
ATOM 5559 C CD1 . TYR D 4 88  ? 42.718  -66.917 -142.086 1.000 322.529 ? 88  TYR FFF CD1 1 
ATOM 5560 C CD2 . TYR D 4 88  ? 42.213  -68.851 -143.367 1.000 330.795 ? 88  TYR FFF CD2 1 
ATOM 5561 C CE1 . TYR D 4 88  ? 43.727  -66.576 -142.980 1.000 328.413 ? 88  TYR FFF CE1 1 
ATOM 5562 C CE2 . TYR D 4 88  ? 43.208  -68.519 -144.272 1.000 332.785 ? 88  TYR FFF CE2 1 
ATOM 5563 C CZ  . TYR D 4 88  ? 43.978  -67.388 -144.077 1.000 332.170 ? 88  TYR FFF CZ  1 
ATOM 5564 O OH  . TYR D 4 88  ? 44.958  -67.116 -144.992 1.000 327.050 ? 88  TYR FFF OH  1 
ATOM 5565 N N   . GLU D 4 89  ? 39.977  -67.311 -138.384 1.000 305.937 ? 89  GLU FFF N   1 
ATOM 5566 C CA  A GLU D 4 89  ? 39.602  -66.149 -137.527 0.500 314.036 ? 89  GLU FFF CA  1 
ATOM 5567 C CA  B GLU D 4 89  ? 39.582  -66.166 -137.512 0.500 302.841 ? 89  GLU FFF CA  1 
ATOM 5568 C C   . GLU D 4 89  ? 40.286  -66.234 -136.143 1.000 313.190 ? 89  GLU FFF C   1 
ATOM 5569 O O   . GLU D 4 89  ? 40.004  -65.351 -135.270 1.000 298.649 ? 89  GLU FFF O   1 
ATOM 5570 C CB  A GLU D 4 89  ? 38.075  -66.056 -137.435 0.500 315.058 ? 89  GLU FFF CB  1 
ATOM 5571 C CB  B GLU D 4 89  ? 38.065  -66.144 -137.314 0.500 289.988 ? 89  GLU FFF CB  1 
ATOM 5572 C CG  A GLU D 4 89  ? 37.446  -67.062 -136.489 0.500 313.182 ? 89  GLU FFF CG  1 
ATOM 5573 C CG  B GLU D 4 89  ? 37.298  -65.764 -138.562 0.500 279.133 ? 89  GLU FFF CG  1 
ATOM 5574 C CD  A GLU D 4 89  ? 35.929  -67.027 -136.463 0.500 310.730 ? 89  GLU FFF CD  1 
ATOM 5575 C CD  B GLU D 4 89  ? 37.081  -66.920 -139.513 0.500 271.264 ? 89  GLU FFF CD  1 
ATOM 5576 O OE1 A GLU D 4 89  ? 35.326  -67.097 -137.555 0.500 311.870 ? 89  GLU FFF OE1 1 
ATOM 5577 O OE1 B GLU D 4 89  ? 37.490  -68.042 -139.184 0.500 264.293 ? 89  GLU FFF OE1 1 
ATOM 5578 O OE2 A GLU D 4 89  ? 35.358  -66.927 -135.354 0.500 304.894 ? 89  GLU FFF OE2 1 
ATOM 5579 O OE2 B GLU D 4 89  ? 36.497  -66.689 -140.564 0.500 265.033 ? 89  GLU FFF OE2 1 
ATOM 5580 N N   . ASP D 4 90  ? 41.152  -67.232 -135.918 1.000 322.988 ? 90  ASP FFF N   1 
ATOM 5581 C CA  . ASP D 4 90  ? 41.976  -67.330 -134.677 1.000 317.177 ? 90  ASP FFF CA  1 
ATOM 5582 C C   . ASP D 4 90  ? 43.368  -66.702 -134.888 1.000 320.948 ? 90  ASP FFF C   1 
ATOM 5583 O O   . ASP D 4 90  ? 44.075  -66.569 -133.872 1.000 319.033 ? 90  ASP FFF O   1 
ATOM 5584 C CB  . ASP D 4 90  ? 42.148  -68.776 -134.197 1.000 318.715 ? 90  ASP FFF CB  1 
ATOM 5585 C CG  . ASP D 4 90  ? 40.865  -69.475 -133.770 1.000 317.009 ? 90  ASP FFF CG  1 
ATOM 5586 O OD1 . ASP D 4 90  ? 39.965  -68.807 -133.216 1.000 308.452 ? 90  ASP FFF OD1 1 
ATOM 5587 O OD2 . ASP D 4 90  ? 40.786  -70.697 -133.989 1.000 323.107 ? 90  ASP FFF OD2 1 
ATOM 5588 N N   . THR D 4 91  ? 43.776  -66.367 -136.129 1.000 332.915 ? 91  THR FFF N   1 
ATOM 5589 C CA  . THR D 4 91  ? 45.123  -65.794 -136.469 1.000 334.084 ? 91  THR FFF CA  1 
ATOM 5590 C C   . THR D 4 91  ? 45.274  -64.464 -135.706 1.000 335.486 ? 91  THR FFF C   1 
ATOM 5591 O O   . THR D 4 91  ? 44.459  -63.555 -135.955 1.000 344.939 ? 91  THR FFF O   1 
ATOM 5592 C CB  . THR D 4 91  ? 45.352  -65.646 -137.993 1.000 327.191 ? 91  THR FFF CB  1 
ATOM 5593 O OG1 . THR D 4 91  ? 45.380  -66.916 -138.650 1.000 320.894 ? 91  THR FFF OG1 1 
ATOM 5594 C CG2 . THR D 4 91  ? 46.653  -64.954 -138.352 1.000 319.915 ? 91  THR FFF CG2 1 
ATOM 5595 N N   . ALA D 4 92  ? 46.246  -64.364 -134.788 1.000 329.337 ? 92  ALA FFF N   1 
ATOM 5596 C CA  . ALA D 4 92  ? 46.407  -63.229 -133.844 1.000 325.469 ? 92  ALA FFF CA  1 
ATOM 5597 C C   . ALA D 4 92  ? 47.637  -63.442 -132.960 1.000 324.444 ? 92  ALA FFF C   1 
ATOM 5598 O O   . ALA D 4 92  ? 48.159  -64.573 -132.926 1.000 323.169 ? 92  ALA FFF O   1 
ATOM 5599 C CB  . ALA D 4 92  ? 45.171  -63.094 -132.981 1.000 323.266 ? 92  ALA FFF CB  1 
ATOM 5600 N N   . VAL D 4 93  ? 48.059  -62.380 -132.267 1.000 323.604 ? 93  VAL FFF N   1 
ATOM 5601 C CA  . VAL D 4 93  ? 49.018  -62.420 -131.122 1.000 317.485 ? 93  VAL FFF CA  1 
ATOM 5602 C C   . VAL D 4 93  ? 48.211  -62.726 -129.848 1.000 311.654 ? 93  VAL FFF C   1 
ATOM 5603 O O   . VAL D 4 93  ? 47.255  -61.981 -129.574 1.000 311.118 ? 93  VAL FFF O   1 
ATOM 5604 C CB  . VAL D 4 93  ? 49.793  -61.090 -131.003 1.000 313.364 ? 93  VAL FFF CB  1 
ATOM 5605 C CG1 . VAL D 4 93  ? 50.790  -61.115 -129.859 1.000 307.749 ? 93  VAL FFF CG1 1 
ATOM 5606 C CG2 . VAL D 4 93  ? 50.494  -60.707 -132.298 1.000 315.107 ? 93  VAL FFF CG2 1 
ATOM 5607 N N   . TYR D 4 94  ? 48.555  -63.788 -129.110 1.000 305.751 ? 94  TYR FFF N   1 
ATOM 5608 C CA  . TYR D 4 94  ? 47.855  -64.216 -127.865 1.000 298.747 ? 94  TYR FFF CA  1 
ATOM 5609 C C   . TYR D 4 94  ? 48.649  -63.760 -126.636 1.000 301.906 ? 94  TYR FFF C   1 
ATOM 5610 O O   . TYR D 4 94  ? 49.857  -64.034 -126.589 1.000 312.508 ? 94  TYR FFF O   1 
ATOM 5611 C CB  . TYR D 4 94  ? 47.627  -65.728 -127.864 1.000 292.574 ? 94  TYR FFF CB  1 
ATOM 5612 C CG  . TYR D 4 94  ? 46.519  -66.144 -128.791 1.000 294.463 ? 94  TYR FFF CG  1 
ATOM 5613 C CD1 . TYR D 4 94  ? 46.683  -66.079 -130.167 1.000 295.381 ? 94  TYR FFF CD1 1 
ATOM 5614 C CD2 . TYR D 4 94  ? 45.295  -66.561 -128.296 1.000 291.271 ? 94  TYR FFF CD2 1 
ATOM 5615 C CE1 . TYR D 4 94  ? 45.661  -66.430 -131.031 1.000 294.344 ? 94  TYR FFF CE1 1 
ATOM 5616 C CE2 . TYR D 4 94  ? 44.266  -66.927 -129.148 1.000 294.896 ? 94  TYR FFF CE2 1 
ATOM 5617 C CZ  . TYR D 4 94  ? 44.449  -66.859 -130.518 1.000 290.867 ? 94  TYR FFF CZ  1 
ATOM 5618 O OH  . TYR D 4 94  ? 43.426  -67.223 -131.341 1.000 290.811 ? 94  TYR FFF OH  1 
ATOM 5619 N N   . TYR D 4 95  ? 47.981  -63.075 -125.692 1.000 295.410 ? 95  TYR FFF N   1 
ATOM 5620 C CA  . TYR D 4 95  ? 48.551  -62.509 -124.437 1.000 278.423 ? 95  TYR FFF CA  1 
ATOM 5621 C C   . TYR D 4 95  ? 47.957  -63.228 -123.226 1.000 270.970 ? 95  TYR FFF C   1 
ATOM 5622 O O   . TYR D 4 95  ? 46.733  -63.421 -123.169 1.000 262.837 ? 95  TYR FFF O   1 
ATOM 5623 C CB  . TYR D 4 95  ? 48.247  -61.013 -124.293 1.000 273.223 ? 95  TYR FFF CB  1 
ATOM 5624 C CG  . TYR D 4 95  ? 48.815  -60.175 -125.402 1.000 273.571 ? 95  TYR FFF CG  1 
ATOM 5625 C CD1 . TYR D 4 95  ? 50.097  -59.664 -125.326 1.000 273.684 ? 95  TYR FFF CD1 1 
ATOM 5626 C CD2 . TYR D 4 95  ? 48.089  -59.950 -126.559 1.000 277.442 ? 95  TYR FFF CD2 1 
ATOM 5627 C CE1 . TYR D 4 95  ? 50.625  -58.915 -126.364 1.000 282.780 ? 95  TYR FFF CE1 1 
ATOM 5628 C CE2 . TYR D 4 95  ? 48.595  -59.194 -127.599 1.000 281.424 ? 95  TYR FFF CE2 1 
ATOM 5629 C CZ  . TYR D 4 95  ? 49.872  -58.681 -127.504 1.000 285.710 ? 95  TYR FFF CZ  1 
ATOM 5630 O OH  . TYR D 4 95  ? 50.374  -57.952 -128.540 1.000 292.154 ? 95  TYR FFF OH  1 
ATOM 5631 N N   A CYS D 4 96  ? 48.816  -63.642 -122.289 0.700 269.425 ? 96  CYS FFF N   1 
ATOM 5632 N N   B CYS D 4 96  ? 48.813  -63.586 -122.270 0.300 270.573 ? 96  CYS FFF N   1 
ATOM 5633 C CA  A CYS D 4 96  ? 48.422  -64.117 -120.933 0.700 266.634 ? 96  CYS FFF CA  1 
ATOM 5634 C CA  B CYS D 4 96  ? 48.406  -64.095 -120.938 0.300 268.549 ? 96  CYS FFF CA  1 
ATOM 5635 C C   A CYS D 4 96  ? 48.460  -62.922 -119.970 0.700 265.499 ? 96  CYS FFF C   1 
ATOM 5636 C C   B CYS D 4 96  ? 48.485  -62.937 -119.941 0.300 267.566 ? 96  CYS FFF C   1 
ATOM 5637 O O   A CYS D 4 96  ? 49.277  -62.003 -120.194 0.700 262.778 ? 96  CYS FFF O   1 
ATOM 5638 O O   B CYS D 4 96  ? 49.376  -62.076 -120.102 0.300 267.370 ? 96  CYS FFF O   1 
ATOM 5639 C CB  A CYS D 4 96  ? 49.274  -65.295 -120.453 0.700 264.900 ? 96  CYS FFF CB  1 
ATOM 5640 C CB  B CYS D 4 96  ? 49.265  -65.273 -120.498 0.300 268.004 ? 96  CYS FFF CB  1 
ATOM 5641 S SG  A CYS D 4 96  ? 51.026  -64.922 -120.157 0.700 262.184 ? 96  CYS FFF SG  1 
ATOM 5642 S SG  B CYS D 4 96  ? 48.534  -66.228 -119.143 0.300 263.410 ? 96  CYS FFF SG  1 
ATOM 5643 N N   . ALA D 4 97  ? 47.554  -62.901 -118.985 1.000 267.682 ? 97  ALA FFF N   1 
ATOM 5644 C CA  . ALA D 4 97  ? 47.463  -61.859 -117.933 1.000 265.574 ? 97  ALA FFF CA  1 
ATOM 5645 C C   . ALA D 4 97  ? 47.209  -62.519 -116.571 1.000 257.980 ? 97  ALA FFF C   1 
ATOM 5646 O O   . ALA D 4 97  ? 46.600  -63.612 -116.522 1.000 242.743 ? 97  ALA FFF O   1 
ATOM 5647 C CB  . ALA D 4 97  ? 46.387  -60.858 -118.272 1.000 266.503 ? 97  ALA FFF CB  1 
ATOM 5648 N N   . GLN D 4 98  ? 47.683  -61.860 -115.510 1.000 258.307 ? 98  GLN FFF N   1 
ATOM 5649 C CA  . GLN D 4 98  ? 47.635  -62.337 -114.104 1.000 249.976 ? 98  GLN FFF CA  1 
ATOM 5650 C C   . GLN D 4 98  ? 47.033  -61.228 -113.244 1.000 241.227 ? 98  GLN FFF C   1 
ATOM 5651 O O   . GLN D 4 98  ? 47.337  -60.045 -113.489 1.000 230.547 ? 98  GLN FFF O   1 
ATOM 5652 C CB  . GLN D 4 98  ? 49.036  -62.729 -113.623 1.000 248.576 ? 98  GLN FFF CB  1 
ATOM 5653 C CG  . GLN D 4 98  ? 49.041  -63.405 -112.260 1.000 243.480 ? 98  GLN FFF CG  1 
ATOM 5654 C CD  . GLN D 4 98  ? 49.245  -62.431 -111.130 1.000 244.188 ? 98  GLN FFF CD  1 
ATOM 5655 O OE1 . GLN D 4 98  ? 48.967  -61.242 -111.250 1.000 249.133 ? 98  GLN FFF OE1 1 
ATOM 5656 N NE2 . GLN D 4 98  ? 49.781  -62.932 -110.030 1.000 243.307 ? 98  GLN FFF NE2 1 
ATOM 5657 N N   . THR D 4 99  ? 46.176  -61.613 -112.305 1.000 241.069 ? 99  THR FFF N   1 
ATOM 5658 C CA  . THR D 4 99  ? 45.594  -60.706 -111.287 1.000 245.566 ? 99  THR FFF CA  1 
ATOM 5659 C C   . THR D 4 99  ? 45.617  -61.416 -109.932 1.000 247.578 ? 99  THR FFF C   1 
ATOM 5660 O O   . THR D 4 99  ? 45.487  -62.652 -109.898 1.000 259.226 ? 99  THR FFF O   1 
ATOM 5661 C CB  . THR D 4 99  ? 44.185  -60.235 -111.677 1.000 243.031 ? 99  THR FFF CB  1 
ATOM 5662 O OG1 . THR D 4 99  ? 43.768  -59.291 -110.689 1.000 240.225 ? 99  THR FFF OG1 1 
ATOM 5663 C CG2 . THR D 4 99  ? 43.175  -61.357 -111.791 1.000 239.057 ? 99  THR FFF CG2 1 
ATOM 5664 N N   . HIS D 4 100 ? 45.798  -60.655 -108.859 1.000 240.269 ? 100 HIS FFF N   1 
ATOM 5665 C CA  . HIS D 4 100 ? 45.659  -61.156 -107.474 1.000 230.185 ? 100 HIS FFF CA  1 
ATOM 5666 C C   . HIS D 4 100 ? 44.272  -60.782 -106.955 1.000 225.344 ? 100 HIS FFF C   1 
ATOM 5667 O O   . HIS D 4 100 ? 43.996  -61.124 -105.804 1.000 238.842 ? 100 HIS FFF O   1 
ATOM 5668 C CB  . HIS D 4 100 ? 46.819  -60.676 -106.599 1.000 229.716 ? 100 HIS FFF CB  1 
ATOM 5669 C CG  . HIS D 4 100 ? 47.059  -59.207 -106.606 1.000 229.090 ? 100 HIS FFF CG  1 
ATOM 5670 N ND1 . HIS D 4 100 ? 48.065  -58.628 -107.363 1.000 227.714 ? 100 HIS FFF ND1 1 
ATOM 5671 C CD2 . HIS D 4 100 ? 46.467  -58.207 -105.921 1.000 228.814 ? 100 HIS FFF CD2 1 
ATOM 5672 C CE1 . HIS D 4 100 ? 48.082  -57.331 -107.140 1.000 227.595 ? 100 HIS FFF CE1 1 
ATOM 5673 N NE2 . HIS D 4 100 ? 47.113  -57.048 -106.260 1.000 229.276 ? 100 HIS FFF NE2 1 
ATOM 5674 N N   . TYR D 4 101 ? 43.431  -60.158 -107.792 1.000 217.063 ? 101 TYR FFF N   1 
ATOM 5675 C CA  . TYR D 4 101 ? 41.998  -59.851 -107.509 1.000 211.076 ? 101 TYR FFF CA  1 
ATOM 5676 C C   . TYR D 4 101 ? 41.176  -61.139 -107.438 1.000 205.055 ? 101 TYR FFF C   1 
ATOM 5677 O O   . TYR D 4 101 ? 41.218  -61.912 -108.377 1.000 197.695 ? 101 TYR FFF O   1 
ATOM 5678 C CB  . TYR D 4 101 ? 41.351  -58.954 -108.572 1.000 211.980 ? 101 TYR FFF CB  1 
ATOM 5679 C CG  . TYR D 4 101 ? 39.930  -58.530 -108.259 1.000 207.260 ? 101 TYR FFF CG  1 
ATOM 5680 C CD1 . TYR D 4 101 ? 39.624  -57.891 -107.071 1.000 201.964 ? 101 TYR FFF CD1 1 
ATOM 5681 C CD2 . TYR D 4 101 ? 38.888  -58.738 -109.150 1.000 207.981 ? 101 TYR FFF CD2 1 
ATOM 5682 C CE1 . TYR D 4 101 ? 38.339  -57.483 -106.763 1.000 196.387 ? 101 TYR FFF CE1 1 
ATOM 5683 C CE2 . TYR D 4 101 ? 37.593  -58.328 -108.857 1.000 201.835 ? 101 TYR FFF CE2 1 
ATOM 5684 C CZ  . TYR D 4 101 ? 37.318  -57.706 -107.653 1.000 193.376 ? 101 TYR FFF CZ  1 
ATOM 5685 O OH  . TYR D 4 101 ? 36.082  -57.280 -107.295 1.000 186.726 ? 101 TYR FFF OH  1 
ATOM 5686 N N   . VAL D 4 102 ? 40.443  -61.330 -106.342 1.000 209.177 ? 102 VAL FFF N   1 
ATOM 5687 C CA  . VAL D 4 102 ? 39.440  -62.419 -106.156 1.000 210.605 ? 102 VAL FFF CA  1 
ATOM 5688 C C   . VAL D 4 102 ? 38.041  -61.774 -106.210 1.000 215.341 ? 102 VAL FFF C   1 
ATOM 5689 O O   . VAL D 4 102 ? 37.717  -60.973 -105.300 1.000 212.093 ? 102 VAL FFF O   1 
ATOM 5690 C CB  . VAL D 4 102 ? 39.683  -63.198 -104.843 1.000 206.411 ? 102 VAL FFF CB  1 
ATOM 5691 C CG1 . VAL D 4 102 ? 38.558  -64.181 -104.556 1.000 202.917 ? 102 VAL FFF CG1 1 
ATOM 5692 C CG2 . VAL D 4 102 ? 41.036  -63.910 -104.809 1.000 203.782 ? 102 VAL FFF CG2 1 
ATOM 5693 N N   . SER D 4 103 ? 37.265  -62.045 -107.272 1.000 222.167 ? 103 SER FFF N   1 
ATOM 5694 C CA  . SER D 4 103 ? 35.783  -61.866 -107.304 1.000 221.890 ? 103 SER FFF CA  1 
ATOM 5695 C C   . SER D 4 103 ? 35.114  -63.229 -107.095 1.000 223.568 ? 103 SER FFF C   1 
ATOM 5696 O O   . SER D 4 103 ? 35.650  -64.245 -107.588 1.000 216.770 ? 103 SER FFF O   1 
ATOM 5697 C CB  . SER D 4 103 ? 35.283  -61.196 -108.575 1.000 221.595 ? 103 SER FFF CB  1 
ATOM 5698 O OG  . SER D 4 103 ? 33.852  -61.193 -108.655 1.000 219.188 ? 103 SER FFF OG  1 
ATOM 5699 N N   . TYR D 4 104 ? 33.983  -63.254 -106.385 1.000 229.851 ? 104 TYR FFF N   1 
ATOM 5700 C CA  . TYR D 4 104 ? 33.167  -64.475 -106.151 1.000 235.083 ? 104 TYR FFF CA  1 
ATOM 5701 C C   . TYR D 4 104 ? 32.515  -64.908 -107.460 1.000 233.146 ? 104 TYR FFF C   1 
ATOM 5702 O O   . TYR D 4 104 ? 32.090  -66.079 -107.533 1.000 229.355 ? 104 TYR FFF O   1 
ATOM 5703 C CB  . TYR D 4 104 ? 32.067  -64.239 -105.112 1.000 243.336 ? 104 TYR FFF CB  1 
ATOM 5704 C CG  . TYR D 4 104 ? 30.971  -63.297 -105.545 1.000 240.641 ? 104 TYR FFF CG  1 
ATOM 5705 C CD1 . TYR D 4 104 ? 31.092  -61.935 -105.318 1.000 237.889 ? 104 TYR FFF CD1 1 
ATOM 5706 C CD2 . TYR D 4 104 ? 29.814  -63.762 -106.161 1.000 239.991 ? 104 TYR FFF CD2 1 
ATOM 5707 C CE1 . TYR D 4 104 ? 30.095  -61.050 -105.689 1.000 236.651 ? 104 TYR FFF CE1 1 
ATOM 5708 C CE2 . TYR D 4 104 ? 28.816  -62.889 -106.559 1.000 240.287 ? 104 TYR FFF CE2 1 
ATOM 5709 C CZ  . TYR D 4 104 ? 28.960  -61.529 -106.323 1.000 239.300 ? 104 TYR FFF CZ  1 
ATOM 5710 O OH  . TYR D 4 104 ? 27.985  -60.653 -106.703 1.000 239.502 ? 104 TYR FFF OH  1 
ATOM 5711 N N   . LEU D 4 105 ? 32.414  -63.976 -108.419 1.000 235.759 ? 105 LEU FFF N   1 
ATOM 5712 C CA  . LEU D 4 105 ? 31.723  -64.159 -109.725 1.000 241.056 ? 105 LEU FFF CA  1 
ATOM 5713 C C   . LEU D 4 105 ? 32.758  -64.267 -110.856 1.000 234.247 ? 105 LEU FFF C   1 
ATOM 5714 O O   . LEU D 4 105 ? 33.282  -63.218 -111.277 1.000 226.283 ? 105 LEU FFF O   1 
ATOM 5715 C CB  . LEU D 4 105 ? 30.776  -62.972 -109.931 1.000 249.398 ? 105 LEU FFF CB  1 
ATOM 5716 C CG  . LEU D 4 105 ? 29.770  -63.115 -111.074 1.000 262.228 ? 105 LEU FFF CG  1 
ATOM 5717 C CD1 . LEU D 4 105 ? 28.812  -64.284 -110.849 1.000 261.023 ? 105 LEU FFF CD1 1 
ATOM 5718 C CD2 . LEU D 4 105 ? 28.999  -61.814 -111.267 1.000 267.246 ? 105 LEU FFF CD2 1 
ATOM 5719 N N   . LEU D 4 106 ? 33.003  -65.492 -111.343 1.000 232.666 ? 106 LEU FFF N   1 
ATOM 5720 C CA  . LEU D 4 106 ? 34.066  -65.853 -112.327 1.000 238.316 ? 106 LEU FFF CA  1 
ATOM 5721 C C   . LEU D 4 106 ? 33.938  -65.006 -113.613 1.000 255.751 ? 106 LEU FFF C   1 
ATOM 5722 O O   . LEU D 4 106 ? 34.997  -64.616 -114.160 1.000 276.722 ? 106 LEU FFF O   1 
ATOM 5723 C CB  . LEU D 4 106 ? 33.979  -67.360 -112.621 1.000 230.485 ? 106 LEU FFF CB  1 
ATOM 5724 C CG  . LEU D 4 106 ? 35.134  -67.969 -113.420 1.000 225.051 ? 106 LEU FFF CG  1 
ATOM 5725 C CD1 . LEU D 4 106 ? 36.431  -67.922 -112.638 1.000 222.580 ? 106 LEU FFF CD1 1 
ATOM 5726 C CD2 . LEU D 4 106 ? 34.832  -69.397 -113.809 1.000 223.972 ? 106 LEU FFF CD2 1 
ATOM 5727 N N   . SER D 4 107 ? 32.712  -64.696 -114.071 1.000 257.548 ? 107 SER FFF N   1 
ATOM 5728 C CA  . SER D 4 107 ? 32.416  -63.907 -115.306 1.000 251.422 ? 107 SER FFF CA  1 
ATOM 5729 C C   . SER D 4 107 ? 33.059  -62.507 -115.263 1.000 254.976 ? 107 SER FFF C   1 
ATOM 5730 O O   . SER D 4 107 ? 33.323  -61.938 -116.343 1.000 253.223 ? 107 SER FFF O   1 
ATOM 5731 C CB  . SER D 4 107 ? 30.927  -63.807 -115.543 1.000 246.080 ? 107 SER FFF CB  1 
ATOM 5732 O OG  . SER D 4 107 ? 30.296  -63.018 -114.541 1.000 234.146 ? 107 SER FFF OG  1 
ATOM 5733 N N   . ASP D 4 108 ? 33.306  -61.959 -114.067 1.000 253.309 ? 108 ASP FFF N   1 
ATOM 5734 C CA  . ASP D 4 108 ? 33.913  -60.615 -113.887 1.000 251.438 ? 108 ASP FFF CA  1 
ATOM 5735 C C   . ASP D 4 108 ? 35.348  -60.597 -114.425 1.000 262.165 ? 108 ASP FFF C   1 
ATOM 5736 O O   . ASP D 4 108 ? 35.804  -59.496 -114.717 1.000 272.444 ? 108 ASP FFF O   1 
ATOM 5737 C CB  . ASP D 4 108 ? 33.873  -60.159 -112.428 1.000 245.660 ? 108 ASP FFF CB  1 
ATOM 5738 C CG  . ASP D 4 108 ? 32.485  -59.771 -111.959 1.000 246.928 ? 108 ASP FFF CG  1 
ATOM 5739 O OD1 . ASP D 4 108 ? 31.594  -59.610 -112.836 1.000 241.628 ? 108 ASP FFF OD1 1 
ATOM 5740 O OD2 . ASP D 4 108 ? 32.304  -59.628 -110.722 1.000 249.850 ? 108 ASP FFF OD2 1 
ATOM 5741 N N   . TYR D 4 109 ? 36.036  -61.741 -114.562 1.000 271.288 ? 109 TYR FFF N   1 
ATOM 5742 C CA  . TYR D 4 109 ? 37.436  -61.806 -115.074 1.000 276.652 ? 109 TYR FFF CA  1 
ATOM 5743 C C   . TYR D 4 109 ? 37.458  -61.547 -116.580 1.000 271.124 ? 109 TYR FFF C   1 
ATOM 5744 O O   . TYR D 4 109 ? 38.566  -61.317 -117.103 1.000 268.849 ? 109 TYR FFF O   1 
ATOM 5745 C CB  . TYR D 4 109 ? 38.137  -63.118 -114.701 1.000 284.406 ? 109 TYR FFF CB  1 
ATOM 5746 C CG  . TYR D 4 109 ? 38.464  -63.202 -113.231 1.000 291.846 ? 109 TYR FFF CG  1 
ATOM 5747 C CD1 . TYR D 4 109 ? 39.341  -62.307 -112.626 1.000 285.746 ? 109 TYR FFF CD1 1 
ATOM 5748 C CD2 . TYR D 4 109 ? 37.838  -64.138 -112.425 1.000 296.785 ? 109 TYR FFF CD2 1 
ATOM 5749 C CE1 . TYR D 4 109 ? 39.601  -62.356 -111.266 1.000 281.191 ? 109 TYR FFF CE1 1 
ATOM 5750 C CE2 . TYR D 4 109 ? 38.091  -64.203 -111.065 1.000 293.783 ? 109 TYR FFF CE2 1 
ATOM 5751 C CZ  . TYR D 4 109 ? 38.969  -63.308 -110.484 1.000 283.914 ? 109 TYR FFF CZ  1 
ATOM 5752 O OH  . TYR D 4 109 ? 39.177  -63.420 -109.145 1.000 270.054 ? 109 TYR FFF OH  1 
ATOM 5753 N N   . ALA D 4 110 ? 36.286  -61.538 -117.225 1.000 269.553 ? 110 ALA FFF N   1 
ATOM 5754 C CA  . ALA D 4 110 ? 36.118  -61.174 -118.650 1.000 274.835 ? 110 ALA FFF CA  1 
ATOM 5755 C C   . ALA D 4 110 ? 36.213  -59.655 -118.835 1.000 277.327 ? 110 ALA FFF C   1 
ATOM 5756 O O   . ALA D 4 110 ? 36.617  -59.257 -119.957 1.000 282.503 ? 110 ALA FFF O   1 
ATOM 5757 C CB  . ALA D 4 110 ? 34.811  -61.697 -119.183 1.000 272.411 ? 110 ALA FFF CB  1 
ATOM 5758 N N   . THR D 4 111 ? 35.856  -58.860 -117.802 1.000 267.770 ? 111 THR FFF N   1 
ATOM 5759 C CA  . THR D 4 111 ? 35.781  -57.362 -117.822 1.000 261.040 ? 111 THR FFF CA  1 
ATOM 5760 C C   . THR D 4 111 ? 36.878  -56.706 -116.950 1.000 256.210 ? 111 THR FFF C   1 
ATOM 5761 O O   . THR D 4 111 ? 37.206  -55.525 -117.207 1.000 262.227 ? 111 THR FFF O   1 
ATOM 5762 C CB  . THR D 4 111 ? 34.364  -56.893 -117.447 1.000 252.352 ? 111 THR FFF CB  1 
ATOM 5763 O OG1 . THR D 4 111 ? 34.134  -57.027 -116.045 1.000 246.822 ? 111 THR FFF OG1 1 
ATOM 5764 C CG2 . THR D 4 111 ? 33.284  -57.665 -118.174 1.000 247.566 ? 111 THR FFF CG2 1 
ATOM 5765 N N   . TRP D 4 112 ? 37.456  -57.436 -115.992 1.000 246.091 ? 112 TRP FFF N   1 
ATOM 5766 C CA  . TRP D 4 112 ? 38.496  -56.934 -115.054 1.000 239.182 ? 112 TRP FFF CA  1 
ATOM 5767 C C   . TRP D 4 112 ? 39.749  -56.524 -115.819 1.000 229.740 ? 112 TRP FFF C   1 
ATOM 5768 O O   . TRP D 4 112 ? 40.229  -57.277 -116.647 1.000 221.290 ? 112 TRP FFF O   1 
ATOM 5769 C CB  . TRP D 4 112 ? 38.841  -58.005 -114.007 1.000 240.928 ? 112 TRP FFF CB  1 
ATOM 5770 C CG  . TRP D 4 112 ? 39.682  -57.491 -112.881 1.000 233.655 ? 112 TRP FFF CG  1 
ATOM 5771 C CD1 . TRP D 4 112 ? 40.985  -57.791 -112.601 1.000 232.939 ? 112 TRP FFF CD1 1 
ATOM 5772 C CD2 . TRP D 4 112 ? 39.262  -56.547 -111.890 1.000 224.149 ? 112 TRP FFF CD2 1 
ATOM 5773 N NE1 . TRP D 4 112 ? 41.402  -57.097 -111.499 1.000 225.827 ? 112 TRP FFF NE1 1 
ATOM 5774 C CE2 . TRP D 4 112 ? 40.371  -56.321 -111.049 1.000 224.956 ? 112 TRP FFF CE2 1 
ATOM 5775 C CE3 . TRP D 4 112 ? 38.065  -55.874 -111.648 1.000 222.673 ? 112 TRP FFF CE3 1 
ATOM 5776 C CZ2 . TRP D 4 112 ? 40.314  -55.446 -109.972 1.000 230.244 ? 112 TRP FFF CZ2 1 
ATOM 5777 C CZ3 . TRP D 4 112 ? 38.008  -55.011 -110.582 1.000 228.510 ? 112 TRP FFF CZ3 1 
ATOM 5778 C CH2 . TRP D 4 112 ? 39.114  -54.811 -109.753 1.000 232.335 ? 112 TRP FFF CH2 1 
ATOM 5779 N N   . PRO D 4 113 ? 40.318  -55.328 -115.565 1.000 229.992 ? 113 PRO FFF N   1 
ATOM 5780 C CA  . PRO D 4 113 ? 41.686  -55.027 -115.983 1.000 233.947 ? 113 PRO FFF CA  1 
ATOM 5781 C C   . PRO D 4 113 ? 42.680  -55.715 -115.032 1.000 233.876 ? 113 PRO FFF C   1 
ATOM 5782 O O   . PRO D 4 113 ? 42.584  -55.481 -113.855 1.000 250.724 ? 113 PRO FFF O   1 
ATOM 5783 C CB  . PRO D 4 113 ? 41.771  -53.494 -115.906 1.000 233.930 ? 113 PRO FFF CB  1 
ATOM 5784 C CG  . PRO D 4 113 ? 40.708  -53.088 -114.899 1.000 231.813 ? 113 PRO FFF CG  1 
ATOM 5785 C CD  . PRO D 4 113 ? 39.679  -54.203 -114.865 1.000 231.479 ? 113 PRO FFF CD  1 
ATOM 5786 N N   . TYR D 4 114 ? 43.593  -56.535 -115.565 1.000 235.158 ? 114 TYR FFF N   1 
ATOM 5787 C CA  . TYR D 4 114 ? 44.526  -57.416 -114.807 1.000 232.155 ? 114 TYR FFF CA  1 
ATOM 5788 C C   . TYR D 4 114 ? 45.749  -56.616 -114.337 1.000 233.621 ? 114 TYR FFF C   1 
ATOM 5789 O O   . TYR D 4 114 ? 45.802  -55.404 -114.602 1.000 234.851 ? 114 TYR FFF O   1 
ATOM 5790 C CB  . TYR D 4 114 ? 44.920  -58.616 -115.667 1.000 228.434 ? 114 TYR FFF CB  1 
ATOM 5791 C CG  . TYR D 4 114 ? 43.857  -59.675 -115.803 1.000 223.256 ? 114 TYR FFF CG  1 
ATOM 5792 C CD1 . TYR D 4 114 ? 42.610  -59.393 -116.337 1.000 224.884 ? 114 TYR FFF CD1 1 
ATOM 5793 C CD2 . TYR D 4 114 ? 44.099  -60.979 -115.419 1.000 222.498 ? 114 TYR FFF CD2 1 
ATOM 5794 C CE1 . TYR D 4 114 ? 41.635  -60.368 -116.482 1.000 221.786 ? 114 TYR FFF CE1 1 
ATOM 5795 C CE2 . TYR D 4 114 ? 43.137  -61.968 -115.565 1.000 220.325 ? 114 TYR FFF CE2 1 
ATOM 5796 C CZ  . TYR D 4 114 ? 41.899  -61.669 -116.105 1.000 217.717 ? 114 TYR FFF CZ  1 
ATOM 5797 O OH  . TYR D 4 114 ? 40.941  -62.634 -116.248 1.000 207.850 ? 114 TYR FFF OH  1 
ATOM 5798 N N   . ASP D 4 115 ? 46.682  -57.270 -113.634 1.000 234.979 ? 115 ASP FFF N   1 
ATOM 5799 C CA  . ASP D 4 115 ? 47.823  -56.614 -112.940 1.000 244.987 ? 115 ASP FFF CA  1 
ATOM 5800 C C   . ASP D 4 115 ? 49.074  -56.678 -113.805 1.000 247.101 ? 115 ASP FFF C   1 
ATOM 5801 O O   . ASP D 4 115 ? 49.735  -55.650 -113.920 1.000 247.644 ? 115 ASP FFF O   1 
ATOM 5802 C CB  . ASP D 4 115 ? 48.126  -57.253 -111.585 1.000 253.993 ? 115 ASP FFF CB  1 
ATOM 5803 C CG  . ASP D 4 115 ? 47.019  -57.044 -110.567 1.000 259.908 ? 115 ASP FFF CG  1 
ATOM 5804 O OD1 . ASP D 4 115 ? 46.556  -55.897 -110.429 1.000 265.827 ? 115 ASP FFF OD1 1 
ATOM 5805 O OD2 . ASP D 4 115 ? 46.622  -58.029 -109.938 1.000 262.903 ? 115 ASP FFF OD2 1 
ATOM 5806 N N   . TYR D 4 116 ? 49.389  -57.847 -114.362 1.000 255.033 ? 116 TYR FFF N   1 
ATOM 5807 C CA  . TYR D 4 116 ? 50.613  -58.080 -115.174 1.000 267.638 ? 116 TYR FFF CA  1 
ATOM 5808 C C   . TYR D 4 116 ? 50.246  -58.826 -116.460 1.000 272.683 ? 116 TYR FFF C   1 
ATOM 5809 O O   . TYR D 4 116 ? 49.241  -59.562 -116.480 1.000 281.266 ? 116 TYR FFF O   1 
ATOM 5810 C CB  . TYR D 4 116 ? 51.666  -58.800 -114.330 1.000 269.089 ? 116 TYR FFF CB  1 
ATOM 5811 C CG  . TYR D 4 116 ? 51.990  -58.072 -113.052 1.000 267.798 ? 116 TYR FFF CG  1 
ATOM 5812 C CD1 . TYR D 4 116 ? 52.886  -57.020 -113.042 1.000 270.082 ? 116 TYR FFF CD1 1 
ATOM 5813 C CD2 . TYR D 4 116 ? 51.350  -58.390 -111.866 1.000 268.098 ? 116 TYR FFF CD2 1 
ATOM 5814 C CE1 . TYR D 4 116 ? 53.158  -56.323 -111.878 1.000 270.967 ? 116 TYR FFF CE1 1 
ATOM 5815 C CE2 . TYR D 4 116 ? 51.631  -57.720 -110.686 1.000 268.495 ? 116 TYR FFF CE2 1 
ATOM 5816 C CZ  . TYR D 4 116 ? 52.542  -56.681 -110.690 1.000 270.956 ? 116 TYR FFF CZ  1 
ATOM 5817 O OH  . TYR D 4 116 ? 52.813  -56.019 -109.526 1.000 272.054 ? 116 TYR FFF OH  1 
ATOM 5818 N N   . TRP D 4 117 ? 51.041  -58.616 -117.511 1.000 273.814 ? 117 TRP FFF N   1 
ATOM 5819 C CA  . TRP D 4 117 ? 50.743  -59.050 -118.900 1.000 275.851 ? 117 TRP FFF CA  1 
ATOM 5820 C C   . TRP D 4 117 ? 51.996  -59.649 -119.538 1.000 282.643 ? 117 TRP FFF C   1 
ATOM 5821 O O   . TRP D 4 117 ? 53.091  -59.123 -119.288 1.000 293.488 ? 117 TRP FFF O   1 
ATOM 5822 C CB  . TRP D 4 117 ? 50.221  -57.858 -119.702 1.000 275.036 ? 117 TRP FFF CB  1 
ATOM 5823 C CG  . TRP D 4 117 ? 48.826  -57.445 -119.338 1.000 271.285 ? 117 TRP FFF CG  1 
ATOM 5824 C CD1 . TRP D 4 117 ? 48.416  -56.612 -118.334 1.000 264.829 ? 117 TRP FFF CD1 1 
ATOM 5825 C CD2 . TRP D 4 117 ? 47.633  -57.858 -120.018 1.000 269.885 ? 117 TRP FFF CD2 1 
ATOM 5826 N NE1 . TRP D 4 117 ? 47.052  -56.477 -118.350 1.000 260.567 ? 117 TRP FFF NE1 1 
ATOM 5827 C CE2 . TRP D 4 117 ? 46.543  -57.233 -119.372 1.000 262.519 ? 117 TRP FFF CE2 1 
ATOM 5828 C CE3 . TRP D 4 117 ? 47.398  -58.696 -121.113 1.000 270.840 ? 117 TRP FFF CE3 1 
ATOM 5829 C CZ2 . TRP D 4 117 ? 45.230  -57.416 -119.797 1.000 258.417 ? 117 TRP FFF CZ2 1 
ATOM 5830 C CZ3 . TRP D 4 117 ? 46.102  -58.890 -121.520 1.000 268.163 ? 117 TRP FFF CZ3 1 
ATOM 5831 C CH2 . TRP D 4 117 ? 45.043  -58.222 -120.897 1.000 262.988 ? 117 TRP FFF CH2 1 
ATOM 5832 N N   . GLY D 4 118 ? 51.828  -60.704 -120.337 1.000 287.720 ? 118 GLY FFF N   1 
ATOM 5833 C CA  . GLY D 4 118 ? 52.904  -61.319 -121.142 1.000 293.078 ? 118 GLY FFF CA  1 
ATOM 5834 C C   . GLY D 4 118 ? 53.237  -60.503 -122.382 1.000 296.770 ? 118 GLY FFF C   1 
ATOM 5835 O O   . GLY D 4 118 ? 52.565  -59.465 -122.602 1.000 290.319 ? 118 GLY FFF O   1 
ATOM 5836 N N   . GLN D 4 119 ? 54.230  -60.963 -123.158 1.000 305.216 ? 119 GLN FFF N   1 
ATOM 5837 C CA  . GLN D 4 119 ? 54.822  -60.258 -124.333 1.000 311.068 ? 119 GLN FFF CA  1 
ATOM 5838 C C   . GLN D 4 119 ? 53.972  -60.519 -125.585 1.000 311.871 ? 119 GLN FFF C   1 
ATOM 5839 O O   . GLN D 4 119 ? 54.101  -59.743 -126.554 1.000 314.370 ? 119 GLN FFF O   1 
ATOM 5840 C CB  . GLN D 4 119 ? 56.287  -60.677 -124.533 1.000 313.320 ? 119 GLN FFF CB  1 
ATOM 5841 C CG  . GLN D 4 119 ? 56.505  -61.970 -125.320 1.000 315.029 ? 119 GLN FFF CG  1 
ATOM 5842 C CD  . GLN D 4 119 ? 56.393  -63.241 -124.509 1.000 318.327 ? 119 GLN FFF CD  1 
ATOM 5843 O OE1 . GLN D 4 119 ? 55.870  -63.261 -123.394 1.000 327.021 ? 119 GLN FFF OE1 1 
ATOM 5844 N NE2 . GLN D 4 119 ? 56.882  -64.332 -125.077 1.000 317.389 ? 119 GLN FFF NE2 1 
ATOM 5845 N N   . GLY D 4 120 ? 53.143  -61.568 -125.557 1.000 310.247 ? 120 GLY FFF N   1 
ATOM 5846 C CA  . GLY D 4 120 ? 52.327  -62.020 -126.699 1.000 314.637 ? 120 GLY FFF CA  1 
ATOM 5847 C C   . GLY D 4 120 ? 53.053  -63.059 -127.545 1.000 316.698 ? 120 GLY FFF C   1 
ATOM 5848 O O   . GLY D 4 120 ? 54.271  -62.897 -127.764 1.000 319.143 ? 120 GLY FFF O   1 
ATOM 5849 N N   . THR D 4 121 ? 52.328  -64.080 -128.019 1.000 311.672 ? 121 THR FFF N   1 
ATOM 5850 C CA  . THR D 4 121 ? 52.837  -65.181 -128.880 1.000 307.286 ? 121 THR FFF CA  1 
ATOM 5851 C C   . THR D 4 121 ? 51.963  -65.240 -130.141 1.000 308.635 ? 121 THR FFF C   1 
ATOM 5852 O O   . THR D 4 121 ? 50.728  -65.283 -129.991 1.000 310.142 ? 121 THR FFF O   1 
ATOM 5853 C CB  . THR D 4 121 ? 52.936  -66.490 -128.080 1.000 301.919 ? 121 THR FFF CB  1 
ATOM 5854 O OG1 . THR D 4 121 ? 53.435  -67.494 -128.960 1.000 309.061 ? 121 THR FFF OG1 1 
ATOM 5855 C CG2 . THR D 4 121 ? 51.635  -66.978 -127.478 1.000 295.913 ? 121 THR FFF CG2 1 
ATOM 5856 N N   . GLN D 4 122 ? 52.580  -65.178 -131.329 1.000 309.521 ? 122 GLN FFF N   1 
ATOM 5857 C CA  . GLN D 4 122 ? 51.876  -65.142 -132.641 1.000 308.205 ? 122 GLN FFF CA  1 
ATOM 5858 C C   . GLN D 4 122 ? 51.395  -66.556 -132.995 1.000 310.037 ? 122 GLN FFF C   1 
ATOM 5859 O O   . GLN D 4 122 ? 52.225  -67.481 -132.964 1.000 305.548 ? 122 GLN FFF O   1 
ATOM 5860 C CB  . GLN D 4 122 ? 52.792  -64.566 -133.728 1.000 306.652 ? 122 GLN FFF CB  1 
ATOM 5861 C CG  . GLN D 4 122 ? 52.171  -64.539 -135.121 1.000 305.694 ? 122 GLN FFF CG  1 
ATOM 5862 C CD  . GLN D 4 122 ? 51.049  -63.537 -135.244 1.000 302.145 ? 122 GLN FFF CD  1 
ATOM 5863 O OE1 . GLN D 4 122 ? 51.174  -62.386 -134.826 1.000 293.013 ? 122 GLN FFF OE1 1 
ATOM 5864 N NE2 . GLN D 4 122 ? 49.945  -63.965 -135.835 1.000 305.612 ? 122 GLN FFF NE2 1 
ATOM 5865 N N   . VAL D 4 123 ? 50.098  -66.708 -133.292 1.000 313.801 ? 123 VAL FFF N   1 
ATOM 5866 C CA  . VAL D 4 123 ? 49.488  -67.929 -133.904 1.000 318.788 ? 123 VAL FFF CA  1 
ATOM 5867 C C   . VAL D 4 123 ? 49.022  -67.539 -135.313 1.000 326.394 ? 123 VAL FFF C   1 
ATOM 5868 O O   . VAL D 4 123 ? 48.304  -66.520 -135.431 1.000 336.350 ? 123 VAL FFF O   1 
ATOM 5869 C CB  . VAL D 4 123 ? 48.337  -68.501 -133.047 1.000 318.379 ? 123 VAL FFF CB  1 
ATOM 5870 C CG1 . VAL D 4 123 ? 47.661  -69.707 -133.699 1.000 314.716 ? 123 VAL FFF CG1 1 
ATOM 5871 C CG2 . VAL D 4 123 ? 48.813  -68.854 -131.643 1.000 318.245 ? 123 VAL FFF CG2 1 
ATOM 5872 N N   . THR D 4 124 ? 49.466  -68.287 -136.332 1.000 324.939 ? 124 THR FFF N   1 
ATOM 5873 C CA  . THR D 4 124 ? 49.105  -68.123 -137.767 1.000 315.308 ? 124 THR FFF CA  1 
ATOM 5874 C C   . THR D 4 124 ? 48.466  -69.426 -138.248 1.000 316.970 ? 124 THR FFF C   1 
ATOM 5875 O O   . THR D 4 124 ? 49.177  -70.461 -138.242 1.000 306.827 ? 124 THR FFF O   1 
ATOM 5876 C CB  . THR D 4 124 ? 50.345  -67.758 -138.587 1.000 312.863 ? 124 THR FFF CB  1 
ATOM 5877 O OG1 . THR D 4 124 ? 50.839  -66.543 -138.018 1.000 302.829 ? 124 THR FFF OG1 1 
ATOM 5878 C CG2 . THR D 4 124 ? 50.057  -67.597 -140.063 1.000 318.646 ? 124 THR FFF CG2 1 
ATOM 5879 N N   . VAL D 4 125 ? 47.174  -69.380 -138.592 1.000 325.036 ? 125 VAL FFF N   1 
ATOM 5880 C CA  . VAL D 4 125 ? 46.373  -70.574 -138.996 1.000 335.065 ? 125 VAL FFF CA  1 
ATOM 5881 C C   . VAL D 4 125 ? 46.318  -70.600 -140.529 1.000 340.433 ? 125 VAL FFF C   1 
ATOM 5882 O O   . VAL D 4 125 ? 45.825  -69.614 -141.129 1.000 334.458 ? 125 VAL FFF O   1 
ATOM 5883 C CB  . VAL D 4 125 ? 44.965  -70.604 -138.357 1.000 336.422 ? 125 VAL FFF CB  1 
ATOM 5884 C CG1 . VAL D 4 125 ? 44.182  -71.841 -138.782 1.000 343.923 ? 125 VAL FFF CG1 1 
ATOM 5885 C CG2 . VAL D 4 125 ? 45.019  -70.520 -136.839 1.000 328.750 ? 125 VAL FFF CG2 1 
ATOM 5886 N N   . SER D 4 126 ? 46.835  -71.684 -141.122 1.000 345.467 ? 126 SER FFF N   1 
ATOM 5887 C CA  . SER D 4 126 ? 46.916  -71.933 -142.586 1.000 352.342 ? 126 SER FFF CA  1 
ATOM 5888 C C   . SER D 4 126 ? 45.551  -72.398 -143.118 1.000 352.101 ? 126 SER FFF C   1 
ATOM 5889 O O   . SER D 4 126 ? 44.792  -73.041 -142.352 1.000 352.369 ? 126 SER FFF O   1 
ATOM 5890 C CB  . SER D 4 126 ? 48.007  -72.933 -142.908 1.000 356.513 ? 126 SER FFF CB  1 
ATOM 5891 O OG  . SER D 4 126 ? 49.254  -72.530 -142.360 1.000 353.353 ? 126 SER FFF OG  1 
ATOM 5892 N N   . SER D 4 127 ? 45.280  -72.098 -144.394 1.000 346.754 ? 127 SER FFF N   1 
ATOM 5893 C CA  . SER D 4 127 ? 43.997  -72.333 -145.111 1.000 341.261 ? 127 SER FFF CA  1 
ATOM 5894 C C   . SER D 4 127 ? 43.601  -73.817 -145.108 1.000 335.963 ? 127 SER FFF C   1 
ATOM 5895 O O   . SER D 4 127 ? 44.501  -74.668 -145.236 1.000 339.669 ? 127 SER FFF O   1 
ATOM 5896 C CB  . SER D 4 127 ? 44.096  -71.794 -146.515 1.000 346.941 ? 127 SER FFF CB  1 
ATOM 5897 O OG  . SER D 4 127 ? 43.085  -72.347 -147.336 1.000 352.625 ? 127 SER FFF OG  1 
ATOM 5898 N N   . LYS D 4 128 ? 42.299  -74.092 -144.950 1.000 324.101 ? 128 LYS FFF N   1 
ATOM 5899 C CA  . LYS D 4 128 ? 41.632  -75.404 -145.196 1.000 316.118 ? 128 LYS FFF CA  1 
ATOM 5900 C C   . LYS D 4 128 ? 42.294  -76.506 -144.357 1.000 306.958 ? 128 LYS FFF C   1 
ATOM 5901 O O   . LYS D 4 128 ? 41.619  -77.209 -143.594 1.000 289.582 ? 128 LYS FFF O   1 
ATOM 5902 C CB  . LYS D 4 128 ? 41.630  -75.703 -146.702 1.000 314.336 ? 128 LYS FFF CB  1 
ATOM 5903 C CG  . LYS D 4 128 ? 40.718  -74.783 -147.505 1.000 311.624 ? 128 LYS FFF CG  1 
ATOM 5904 C CD  . LYS D 4 128 ? 41.056  -74.653 -148.966 1.000 319.006 ? 128 LYS FFF CD  1 
ATOM 5905 C CE  . LYS D 4 128 ? 40.268  -73.554 -149.654 1.000 321.866 ? 128 LYS FFF CE  1 
ATOM 5906 N NZ  . LYS D 4 128 ? 40.907  -73.119 -150.920 1.000 326.017 ? 128 LYS FFF NZ  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . THR A 1   ? 2.512 2.659 2.390 0.210  0.308  0.155  0   THR HHH N   
2    C CA  . THR A 1   ? 2.387 2.518 2.239 0.227  0.289  0.200  0   THR HHH CA  
3    C C   . THR A 1   ? 2.217 2.320 2.057 0.219  0.298  0.218  0   THR HHH C   
4    O O   . THR A 1   ? 2.154 2.230 1.993 0.203  0.326  0.210  0   THR HHH O   
5    C CB  . THR A 1   ? 2.367 2.475 2.200 0.235  0.296  0.226  0   THR HHH CB  
6    O OG1 . THR A 1   ? 2.513 2.608 2.325 0.248  0.280  0.264  0   THR HHH OG1 
7    C CG2 . THR A 1   ? 2.330 2.400 2.158 0.221  0.331  0.224  0   THR HHH CG2 
8    N N   . GLN A 2   ? 2.047 2.155 1.878 0.230  0.276  0.241  1   GLN HHH N   
9    C CA  . GLN A 2   ? 2.080 2.165 1.898 0.223  0.282  0.259  1   GLN HHH CA  
10   C C   . GLN A 2   ? 2.177 2.223 1.967 0.225  0.298  0.288  1   GLN HHH C   
11   O O   . GLN A 2   ? 2.376 2.392 2.154 0.213  0.321  0.289  1   GLN HHH O   
12   C CB  . GLN A 2   ? 2.110 2.209 1.925 0.234  0.257  0.275  1   GLN HHH CB  
13   C CG  . GLN A 2   ? 2.113 2.192 1.912 0.228  0.261  0.294  1   GLN HHH CG  
14   C CD  . GLN A 2   ? 2.147 2.221 1.954 0.210  0.277  0.273  1   GLN HHH CD  
15   O OE1 . GLN A 2   ? 2.162 2.257 1.986 0.208  0.266  0.258  1   GLN HHH OE1 
16   N NE2 . GLN A 2   ? 2.192 2.235 1.986 0.198  0.304  0.270  1   GLN HHH NE2 
17   N N   . MET A 3   ? 1.937 1.983 1.716 0.240  0.286  0.312  2   MET HHH N   
18   C CA  . MET A 3   ? 1.924 1.942 1.679 0.248  0.293  0.344  2   MET HHH CA  
19   C C   . MET A 3   ? 1.860 1.878 1.613 0.259  0.293  0.352  2   MET HHH C   
20   O O   . MET A 3   ? 1.962 2.005 1.724 0.267  0.273  0.351  2   MET HHH O   
21   C CB  . MET A 3   ? 1.934 1.960 1.678 0.256  0.274  0.369  2   MET HHH CB  
22   C CG  . MET A 3   ? 1.977 1.983 1.698 0.266  0.278  0.399  2   MET HHH CG  
23   S SD  . MET A 3   ? 2.163 2.127 1.860 0.261  0.308  0.405  2   MET HHH SD  
24   C CE  . MET A 3   ? 2.130 2.098 1.828 0.244  0.308  0.389  2   MET HHH CE  
25   N N   . GLN A 4   ? 1.915 1.902 1.656 0.260  0.314  0.362  3   GLN HHH N   
26   C CA  . GLN A 4   ? 2.122 2.105 1.859 0.272  0.315  0.376  3   GLN HHH CA  
27   C C   . GLN A 4   ? 2.201 2.156 1.917 0.283  0.324  0.407  3   GLN HHH C   
28   O O   . GLN A 4   ? 2.303 2.229 2.004 0.278  0.342  0.411  3   GLN HHH O   
29   C CB  . GLN A 4   ? 2.141 2.119 1.890 0.264  0.334  0.352  3   GLN HHH CB  
30   C CG  . GLN A 4   ? 2.170 2.106 1.911 0.257  0.369  0.351  3   GLN HHH CG  
31   C CD  . GLN A 4   ? 2.073 2.007 1.826 0.254  0.385  0.333  3   GLN HHH CD  
32   O OE1 . GLN A 4   ? 1.859 1.804 1.613 0.265  0.375  0.343  3   GLN HHH OE1 
33   N NE2 . GLN A 4   ? 2.128 2.051 1.893 0.236  0.412  0.302  3   GLN HHH NE2 
34   N N   . LEU A 5   ? 2.101 2.063 1.813 0.298  0.311  0.428  4   LEU HHH N   
35   C CA  . LEU A 5   ? 1.991 1.935 1.686 0.312  0.316  0.456  4   LEU HHH CA  
36   C C   . LEU A 5   ? 2.066 1.988 1.761 0.320  0.334  0.460  4   LEU HHH C   
37   O O   . LEU A 5   ? 2.316 2.254 2.027 0.317  0.331  0.447  4   LEU HHH O   
38   C CB  . LEU A 5   ? 1.934 1.908 1.631 0.323  0.290  0.473  4   LEU HHH CB  
39   C CG  . LEU A 5   ? 1.914 1.915 1.619 0.314  0.270  0.464  4   LEU HHH CG  
40   C CD1 . LEU A 5   ? 1.742 1.770 1.455 0.322  0.250  0.474  4   LEU HHH CD1 
41   C CD2 . LEU A 5   ? 2.029 2.023 1.721 0.309  0.271  0.466  4   LEU HHH CD2 
42   N N   . VAL A 6   ? 2.053 1.940 1.729 0.329  0.354  0.476  5   VAL HHH N   
43   C CA  . VAL A 6   ? 2.205 2.066 1.881 0.339  0.375  0.482  5   VAL HHH CA  
44   C C   . VAL A 6   ? 2.252 2.111 1.915 0.364  0.367  0.513  5   VAL HHH C   
45   O O   . VAL A 6   ? 2.530 2.383 2.173 0.373  0.362  0.530  5   VAL HHH O   
46   C CB  . VAL A 6   ? 2.263 2.077 1.928 0.329  0.411  0.472  5   VAL HHH CB  
47   C CG1 . VAL A 6   ? 2.397 2.182 2.064 0.338  0.436  0.476  5   VAL HHH CG1 
48   C CG2 . VAL A 6   ? 2.145 1.970 1.825 0.304  0.417  0.438  5   VAL HHH CG2 
49   N N   . GLN A 7   ? 2.217 2.084 1.893 0.375  0.366  0.519  6   GLN HHH N   
50   C CA  . GLN A 7   ? 2.236 2.113 1.908 0.400  0.355  0.544  6   GLN HHH CA  
51   C C   . GLN A 7   ? 2.291 2.127 1.955 0.416  0.382  0.556  6   GLN HHH C   
52   O O   . GLN A 7   ? 2.165 1.975 1.835 0.403  0.407  0.539  6   GLN HHH O   
53   C CB  . GLN A 7   ? 2.170 2.091 1.865 0.401  0.332  0.542  6   GLN HHH CB  
54   C CG  . GLN A 7   ? 2.205 2.160 1.907 0.387  0.308  0.531  6   GLN HHH CG  
55   C CD  . GLN A 7   ? 2.083 2.076 1.803 0.390  0.289  0.532  6   GLN HHH CD  
56   O OE1 . GLN A 7   ? 1.770 1.781 1.500 0.377  0.280  0.519  6   GLN HHH OE1 
57   N NE2 . GLN A 7   ? 2.197 2.203 1.921 0.408  0.283  0.548  6   GLN HHH NE2 
58   N N   . SER A 8   ? 2.277 2.113 1.929 0.443  0.376  0.581  7   SER HHH N   
59   C CA  . SER A 8   ? 2.250 2.047 1.890 0.467  0.398  0.600  7   SER HHH CA  
60   C C   . SER A 8   ? 2.370 2.170 2.037 0.467  0.408  0.591  7   SER HHH C   
61   O O   . SER A 8   ? 2.717 2.560 2.410 0.456  0.388  0.577  7   SER HHH O   
62   C CB  . SER A 8   ? 2.244 2.057 1.870 0.498  0.380  0.627  7   SER HHH CB  
63   O OG  . SER A 8   ? 2.188 2.058 1.841 0.503  0.351  0.624  7   SER HHH OG  
64   N N   . GLY A 9   ? 2.393 2.148 2.054 0.479  0.438  0.598  8   GLY HHH N   
65   C CA  . GLY A 9   ? 2.438 2.189 2.124 0.480  0.453  0.588  8   GLY HHH CA  
66   C C   . GLY A 9   ? 2.375 2.171 2.083 0.496  0.429  0.596  8   GLY HHH C   
67   O O   . GLY A 9   ? 2.392 2.217 2.094 0.514  0.404  0.612  8   GLY HHH O   
68   N N   . THR A 10  ? 2.461 2.268 2.195 0.490  0.436  0.582  9   THR HHH N   
69   C CA  . THR A 10  ? 2.722 2.575 2.481 0.502  0.415  0.585  9   THR HHH CA  
70   C C   . THR A 10  ? 2.779 2.621 2.537 0.539  0.420  0.609  9   THR HHH C   
71   O O   . THR A 10  ? 2.801 2.591 2.546 0.551  0.449  0.618  9   THR HHH O   
72   C CB  . THR A 10  ? 2.695 2.563 2.480 0.484  0.421  0.563  9   THR HHH CB  
73   O OG1 . THR A 10  ? 2.847 2.676 2.637 0.489  0.453  0.561  9   THR HHH OG1 
74   C CG2 . THR A 10  ? 2.631 2.510 2.413 0.453  0.416  0.540  9   THR HHH CG2 
75   N N   . GLU A 11  ? 2.659 2.547 2.429 0.557  0.393  0.619  10  GLU HHH N   
76   C CA  . GLU A 11  ? 2.585 2.475 2.350 0.597  0.388  0.643  10  GLU HHH CA  
77   C C   . GLU A 11  ? 2.586 2.505 2.387 0.611  0.386  0.639  10  GLU HHH C   
78   O O   . GLU A 11  ? 2.447 2.414 2.274 0.595  0.369  0.623  10  GLU HHH O   
79   C CB  . GLU A 11  ? 2.552 2.477 2.303 0.607  0.358  0.654  10  GLU HHH CB  
80   C CG  . GLU A 11  ? 2.721 2.611 2.433 0.597  0.363  0.660  10  GLU HHH CG  
81   C CD  . GLU A 11  ? 3.060 2.898 2.733 0.627  0.381  0.686  10  GLU HHH CD  
82   O OE1 . GLU A 11  ? 3.239 3.077 2.913 0.663  0.381  0.704  10  GLU HHH OE1 
83   O OE2 . GLU A 11  ? 3.253 3.048 2.895 0.614  0.396  0.688  10  GLU HHH OE2 
84   N N   . VAL A 12  ? 2.666 2.555 2.467 0.641  0.406  0.654  11  VAL HHH N   
85   C CA  . VAL A 12  ? 2.592 2.504 2.427 0.664  0.407  0.654  11  VAL HHH CA  
86   C C   . VAL A 12  ? 2.629 2.564 2.458 0.709  0.388  0.677  11  VAL HHH C   
87   O O   . VAL A 12  ? 2.540 2.429 2.345 0.742  0.405  0.700  11  VAL HHH O   
88   C CB  . VAL A 12  ? 2.648 2.504 2.486 0.664  0.446  0.651  11  VAL HHH CB  
89   C CG1 . VAL A 12  ? 2.662 2.535 2.534 0.691  0.451  0.653  11  VAL HHH CG1 
90   C CG2 . VAL A 12  ? 2.617 2.463 2.463 0.619  0.460  0.624  11  VAL HHH CG2 
91   N N   . LYS A 13  ? 2.604 2.609 2.454 0.712  0.354  0.670  12  LYS HHH N   
92   C CA  . LYS A 13  ? 2.591 2.638 2.438 0.751  0.327  0.686  12  LYS HHH CA  
93   C C   . LYS A 13  ? 2.663 2.768 2.559 0.768  0.316  0.674  12  LYS HHH C   
94   O O   . LYS A 13  ? 2.827 2.940 2.756 0.743  0.327  0.653  12  LYS HHH O   
95   C CB  . LYS A 13  ? 2.453 2.537 2.284 0.737  0.299  0.682  12  LYS HHH CB  
96   C CG  . LYS A 13  ? 2.485 2.516 2.269 0.720  0.310  0.692  12  LYS HHH CG  
97   C CD  . LYS A 13  ? 2.503 2.507 2.241 0.756  0.307  0.721  12  LYS HHH CD  
98   C CE  . LYS A 13  ? 2.548 2.478 2.261 0.782  0.341  0.742  12  LYS HHH CE  
99   N NZ  . LYS A 13  ? 2.672 2.581 2.338 0.824  0.336  0.773  12  LYS HHH NZ  
100  N N   . LYS A 14  ? 2.652 2.798 2.554 0.811  0.295  0.686  13  LYS HHH N   
101  C CA  . LYS A 14  ? 2.578 2.787 2.531 0.831  0.282  0.673  13  LYS HHH CA  
102  C C   . LYS A 14  ? 2.429 2.718 2.393 0.846  0.244  0.667  13  LYS HHH C   
103  O O   . LYS A 14  ? 2.377 2.664 2.302 0.860  0.229  0.683  13  LYS HHH O   
104  C CB  . LYS A 14  ? 2.617 2.796 2.574 0.876  0.300  0.691  13  LYS HHH CB  
105  C CG  . LYS A 14  ? 2.781 2.936 2.692 0.925  0.292  0.724  13  LYS HHH CG  
106  C CD  . LYS A 14  ? 3.026 3.186 2.953 0.979  0.295  0.738  13  LYS HHH CD  
107  C CE  . LYS A 14  ? 3.180 3.279 3.121 0.975  0.335  0.738  13  LYS HHH CE  
108  N NZ  . LYS A 14  ? 3.373 3.469 3.324 1.033  0.339  0.756  13  LYS HHH NZ  
109  N N   . PRO A 15  ? 2.376 2.740 2.396 0.842  0.229  0.641  14  PRO HHH N   
110  C CA  . PRO A 15  ? 2.323 2.769 2.360 0.843  0.196  0.625  14  PRO HHH CA  
111  C C   . PRO A 15  ? 2.333 2.800 2.342 0.893  0.172  0.647  14  PRO HHH C   
112  O O   . PRO A 15  ? 2.371 2.826 2.377 0.937  0.176  0.665  14  PRO HHH O   
113  C CB  . PRO A 15  ? 2.366 2.879 2.471 0.841  0.192  0.595  14  PRO HHH CB  
114  C CG  . PRO A 15  ? 2.381 2.841 2.498 0.818  0.226  0.591  14  PRO HHH CG  
115  C CD  . PRO A 15  ? 2.419 2.791 2.486 0.835  0.247  0.623  14  PRO HHH CD  
116  N N   . GLY A 16  ? 2.404 2.899 2.389 0.885  0.149  0.646  15  GLY HHH N   
117  C CA  . GLY A 16  ? 2.574 3.096 2.526 0.931  0.123  0.665  15  GLY HHH CA  
118  C C   . GLY A 16  ? 2.642 3.087 2.521 0.935  0.133  0.697  15  GLY HHH C   
119  O O   . GLY A 16  ? 2.671 3.143 2.518 0.951  0.110  0.705  15  GLY HHH O   
120  N N   . GLU A 17  ? 2.634 2.989 2.489 0.921  0.168  0.713  16  GLU HHH N   
121  C CA  . GLU A 17  ? 2.586 2.858 2.375 0.916  0.185  0.739  16  GLU HHH CA  
122  C C   . GLU A 17  ? 2.420 2.713 2.199 0.874  0.172  0.723  16  GLU HHH C   
123  O O   . GLU A 17  ? 2.527 2.870 2.350 0.839  0.162  0.694  16  GLU HHH O   
124  C CB  . GLU A 17  ? 2.649 2.833 2.428 0.894  0.226  0.745  16  GLU HHH CB  
125  C CG  . GLU A 17  ? 2.892 3.042 2.679 0.933  0.247  0.761  16  GLU HHH CG  
126  C CD  . GLU A 17  ? 3.024 3.085 2.799 0.912  0.290  0.766  16  GLU HHH CD  
127  O OE1 . GLU A 17  ? 3.157 3.147 2.891 0.940  0.314  0.794  16  GLU HHH OE1 
128  O OE2 . GLU A 17  ? 3.225 3.288 3.033 0.869  0.302  0.741  16  GLU HHH OE2 
129  N N   . SER A 18  ? 2.422 2.675 2.145 0.878  0.173  0.743  17  SER HHH N   
130  C CA  . SER A 18  ? 2.570 2.824 2.278 0.834  0.168  0.730  17  SER HHH CA  
131  C C   . SER A 18  ? 2.719 2.885 2.402 0.803  0.203  0.736  17  SER HHH C   
132  O O   . SER A 18  ? 2.734 2.836 2.401 0.820  0.231  0.754  17  SER HHH O   
133  C CB  . SER A 18  ? 2.645 2.923 2.313 0.853  0.145  0.741  17  SER HHH CB  
134  O OG  . SER A 18  ? 2.827 3.034 2.433 0.884  0.162  0.776  17  SER HHH OG  
135  N N   . LEU A 19  ? 2.811 2.979 2.494 0.760  0.202  0.720  18  LEU HHH N   
136  C CA  . LEU A 19  ? 2.746 2.850 2.417 0.722  0.229  0.715  18  LEU HHH CA  
137  C C   . LEU A 19  ? 2.660 2.772 2.313 0.692  0.219  0.706  18  LEU HHH C   
138  O O   . LEU A 19  ? 2.495 2.671 2.172 0.679  0.193  0.688  18  LEU HHH O   
139  C CB  . LEU A 19  ? 2.673 2.789 2.392 0.695  0.238  0.692  18  LEU HHH CB  
140  C CG  . LEU A 19  ? 2.754 2.824 2.469 0.655  0.260  0.681  18  LEU HHH CG  
141  C CD1 . LEU A 19  ? 2.966 2.957 2.652 0.662  0.293  0.696  18  LEU HHH CD1 
142  C CD2 . LEU A 19  ? 2.756 2.854 2.516 0.628  0.260  0.656  18  LEU HHH CD2 
143  N N   . LYS A 20  ? 2.581 2.628 2.194 0.680  0.240  0.715  19  LYS HHH N   
144  C CA  . LYS A 20  ? 2.528 2.574 2.126 0.648  0.236  0.704  19  LYS HHH CA  
145  C C   . LYS A 20  ? 2.462 2.452 2.059 0.616  0.265  0.695  19  LYS HHH C   
146  O O   . LYS A 20  ? 2.526 2.451 2.089 0.623  0.291  0.709  19  LYS HHH O   
147  C CB  . LYS A 20  ? 2.673 2.706 2.219 0.670  0.230  0.725  19  LYS HHH CB  
148  C CG  . LYS A 20  ? 2.744 2.763 2.267 0.639  0.232  0.716  19  LYS HHH CG  
149  C CD  . LYS A 20  ? 2.870 2.884 2.341 0.660  0.224  0.734  19  LYS HHH CD  
150  C CE  . LYS A 20  ? 3.028 2.969 2.455 0.645  0.253  0.742  19  LYS HHH CE  
151  N NZ  . LYS A 20  ? 3.144 3.071 2.514 0.666  0.250  0.762  19  LYS HHH NZ  
152  N N   . ILE A 21  ? 2.319 2.331 1.951 0.584  0.261  0.671  20  ILE HHH N   
153  C CA  . ILE A 21  ? 2.245 2.216 1.881 0.553  0.284  0.657  20  ILE HHH CA  
154  C C   . ILE A 21  ? 2.095 2.060 1.712 0.529  0.280  0.649  20  ILE HHH C   
155  O O   . ILE A 21  ? 1.896 1.900 1.509 0.531  0.257  0.649  20  ILE HHH O   
156  C CB  . ILE A 21  ? 2.369 2.366 2.047 0.533  0.281  0.637  20  ILE HHH CB  
157  C CG1 . ILE A 21  ? 2.379 2.436 2.081 0.519  0.254  0.622  20  ILE HHH CG1 
158  C CG2 . ILE A 21  ? 2.314 2.308 2.010 0.554  0.291  0.643  20  ILE HHH CG2 
159  C CD1 . ILE A 21  ? 2.356 2.429 2.090 0.498  0.255  0.604  20  ILE HHH CD1 
160  N N   . SER A 22  ? 2.103 2.024 1.712 0.507  0.303  0.640  21  SER HHH N   
161  C CA  . SER A 22  ? 2.126 2.033 1.717 0.485  0.307  0.630  21  SER HHH CA  
162  C C   . SER A 22  ? 2.401 2.312 2.017 0.452  0.310  0.604  21  SER HHH C   
163  O O   . SER A 22  ? 2.479 2.397 2.122 0.448  0.314  0.594  21  SER HHH O   
164  C CB  . SER A 22  ? 2.143 1.990 1.696 0.492  0.335  0.643  21  SER HHH CB  
165  O OG  . SER A 22  ? 2.103 1.909 1.664 0.484  0.364  0.635  21  SER HHH OG  
166  N N   . CYS A 23  ? 2.450 2.360 2.058 0.432  0.308  0.593  22  CYS HHH N   
167  C CA  . CYS A 23  ? 2.300 2.219 1.928 0.404  0.307  0.568  22  CYS HHH CA  
168  C C   . CYS A 23  ? 2.217 2.116 1.825 0.389  0.316  0.561  22  CYS HHH C   
169  O O   . CYS A 23  ? 2.110 2.029 1.708 0.390  0.300  0.566  22  CYS HHH O   
170  C CB  . CYS A 23  ? 2.094 2.064 1.747 0.397  0.280  0.559  22  CYS HHH CB  
171  S SG  . CYS A 23  ? 2.091 2.072 1.758 0.368  0.275  0.533  22  CYS HHH SG  
172  N N   . LYS A 24  ? 2.251 2.110 1.853 0.377  0.343  0.550  23  LYS HHH N   
173  C CA  . LYS A 24  ? 2.265 2.096 1.847 0.362  0.360  0.541  23  LYS HHH CA  
174  C C   . LYS A 24  ? 2.132 1.984 1.741 0.335  0.355  0.510  23  LYS HHH C   
175  O O   . LYS A 24  ? 2.242 2.092 1.872 0.326  0.365  0.493  23  LYS HHH O   
176  C CB  . LYS A 24  ? 2.237 2.008 1.799 0.364  0.398  0.545  23  LYS HHH CB  
177  C CG  . LYS A 24  ? 2.264 1.996 1.799 0.351  0.423  0.539  23  LYS HHH CG  
178  C CD  . LYS A 24  ? 2.335 2.001 1.840 0.362  0.462  0.554  23  LYS HHH CD  
179  C CE  . LYS A 24  ? 2.269 1.888 1.759 0.341  0.499  0.538  23  LYS HHH CE  
180  N NZ  . LYS A 24  ? 2.379 1.981 1.828 0.346  0.498  0.554  23  LYS HHH NZ  
181  N N   . GLY A 25  ? 2.093 1.966 1.702 0.325  0.341  0.503  24  GLY HHH N   
182  C CA  . GLY A 25  ? 2.092 1.985 1.725 0.303  0.335  0.475  24  GLY HHH CA  
183  C C   . GLY A 25  ? 2.146 2.007 1.776 0.285  0.364  0.454  24  GLY HHH C   
184  O O   . GLY A 25  ? 2.230 2.061 1.833 0.283  0.380  0.462  24  GLY HHH O   
185  N N   . SER A 26  ? 2.115 1.982 1.771 0.272  0.373  0.427  25  SER HHH N   
186  C CA  . SER A 26  ? 2.086 1.931 1.749 0.252  0.402  0.399  25  SER HHH CA  
187  C C   . SER A 26  ? 2.039 1.920 1.727 0.236  0.387  0.370  25  SER HHH C   
188  O O   . SER A 26  ? 1.960 1.876 1.674 0.236  0.370  0.355  25  SER HHH O   
189  C CB  . SER A 26  ? 2.025 1.857 1.702 0.248  0.423  0.383  25  SER HHH CB  
190  O OG  . SER A 26  ? 2.125 1.911 1.776 0.260  0.446  0.407  25  SER HHH OG  
191  N N   . GLY A 27  ? 2.197 2.069 1.877 0.224  0.396  0.363  26  GLY HHH N   
192  C CA  . GLY A 27  ? 2.249 2.153 1.956 0.209  0.386  0.333  26  GLY HHH CA  
193  C C   . GLY A 27  ? 2.284 2.182 1.976 0.202  0.385  0.337  26  GLY HHH C   
194  O O   . GLY A 27  ? 2.227 2.108 1.888 0.213  0.383  0.367  26  GLY HHH O   
195  N N   . TYR A 28  ? 2.286 2.203 2.001 0.185  0.387  0.306  27  TYR HHH N   
196  C CA  . TYR A 28  ? 2.206 2.127 1.916 0.177  0.383  0.304  27  TYR HHH CA  
197  C C   . TYR A 28  ? 2.218 2.175 1.934 0.190  0.346  0.320  27  TYR HHH C   
198  O O   . TYR A 28  ? 2.173 2.156 1.906 0.201  0.326  0.321  27  TYR HHH O   
199  C CB  . TYR A 28  ? 2.069 2.003 1.810 0.155  0.396  0.262  27  TYR HHH CB  
200  C CG  . TYR A 28  ? 1.940 1.836 1.675 0.138  0.438  0.243  27  TYR HHH CG  
201  C CD1 . TYR A 28  ? 1.973 1.827 1.677 0.127  0.465  0.250  27  TYR HHH CD1 
202  C CD2 . TYR A 28  ? 1.897 1.798 1.657 0.132  0.452  0.218  27  TYR HHH CD2 
203  C CE1 . TYR A 28  ? 2.056 1.868 1.753 0.109  0.509  0.232  27  TYR HHH CE1 
204  C CE2 . TYR A 28  ? 1.956 1.819 1.713 0.113  0.495  0.197  27  TYR HHH CE2 
205  C CZ  . TYR A 28  ? 2.066 1.882 1.791 0.101  0.525  0.204  27  TYR HHH CZ  
206  O OH  . TYR A 28  ? 2.073 1.842 1.789 0.081  0.573  0.187  27  TYR HHH OH  
207  N N   . GLY A 29  ? 2.300 2.256 1.999 0.189  0.340  0.332  28  GLY HHH N   
208  C CA  . GLY A 29  ? 2.162 2.152 1.871 0.197  0.310  0.341  28  GLY HHH CA  
209  C C   . GLY A 29  ? 2.073 2.063 1.761 0.215  0.296  0.373  28  GLY HHH C   
210  O O   . GLY A 29  ? 1.833 1.850 1.532 0.221  0.273  0.379  28  GLY HHH O   
211  N N   . PHE A 30  ? 2.106 2.066 1.767 0.223  0.310  0.393  29  PHE HHH N   
212  C CA  . PHE A 30  ? 2.089 2.052 1.733 0.243  0.298  0.422  29  PHE HHH CA  
213  C C   . PHE A 30  ? 2.017 2.001 1.650 0.245  0.280  0.434  29  PHE HHH C   
214  O O   . PHE A 30  ? 2.050 2.057 1.687 0.258  0.262  0.448  29  PHE HHH O   
215  C CB  . PHE A 30  ? 2.101 2.025 1.715 0.253  0.319  0.441  29  PHE HHH CB  
216  C CG  . PHE A 30  ? 2.228 2.161 1.831 0.276  0.304  0.468  29  PHE HHH CG  
217  C CD1 . PHE A 30  ? 2.407 2.351 2.030 0.284  0.297  0.469  29  PHE HHH CD1 
218  C CD2 . PHE A 30  ? 2.348 2.285 1.924 0.288  0.296  0.489  29  PHE HHH CD2 
219  C CE1 . PHE A 30  ? 2.447 2.403 2.065 0.304  0.285  0.491  29  PHE HHH CE1 
220  C CE2 . PHE A 30  ? 2.396 2.350 1.968 0.309  0.281  0.510  29  PHE HHH CE2 
221  C CZ  . PHE A 30  ? 2.348 2.310 1.942 0.316  0.276  0.511  29  PHE HHH CZ  
222  N N   . ILE A 31  ? 2.013 1.993 1.636 0.232  0.287  0.425  30  ILE HHH N   
223  C CA  . ILE A 31  ? 2.175 2.175 1.784 0.233  0.273  0.433  30  ILE HHH CA  
224  C C   . ILE A 31  ? 2.035 2.076 1.677 0.233  0.249  0.427  30  ILE HHH C   
225  O O   . ILE A 31  ? 2.017 2.081 1.653 0.237  0.235  0.436  30  ILE HHH O   
226  C CB  . ILE A 31  ? 2.334 2.320 1.927 0.216  0.287  0.421  30  ILE HHH CB  
227  C CG1 . ILE A 31  ? 2.398 2.406 1.975 0.216  0.274  0.428  30  ILE HHH CG1 
228  C CG2 . ILE A 31  ? 2.403 2.396 2.030 0.198  0.292  0.391  30  ILE HHH CG2 
229  C CD1 . ILE A 31  ? 2.501 2.514 2.047 0.238  0.265  0.456  30  ILE HHH CD1 
230  N N   . THR A 32  ? 1.895 1.943 1.567 0.229  0.245  0.412  31  THR HHH N   
231  C CA  . THR A 32  ? 1.857 1.935 1.557 0.229  0.227  0.406  31  THR HHH CA  
232  C C   . THR A 32  ? 1.803 1.893 1.505 0.244  0.215  0.423  31  THR HHH C   
233  O O   . THR A 32  ? 1.654 1.767 1.367 0.244  0.203  0.424  31  THR HHH O   
234  C CB  . THR A 32  ? 1.885 1.965 1.611 0.223  0.227  0.384  31  THR HHH CB  
235  O OG1 . THR A 32  ? 1.920 1.988 1.648 0.209  0.242  0.365  31  THR HHH OG1 
236  C CG2 . THR A 32  ? 1.972 2.074 1.720 0.223  0.213  0.378  31  THR HHH CG2 
237  N N   . TYR A 33  ? 1.921 1.994 1.613 0.254  0.222  0.433  32  TYR HHH N   
238  C CA  . TYR A 33  ? 1.973 2.054 1.672 0.268  0.215  0.446  32  TYR HHH CA  
239  C C   . TYR A 33  ? 1.831 1.926 1.517 0.278  0.207  0.463  32  TYR HHH C   
240  O O   . TYR A 33  ? 1.799 1.889 1.463 0.280  0.211  0.472  32  TYR HHH O   
241  C CB  . TYR A 33  ? 2.049 2.105 1.742 0.274  0.228  0.448  32  TYR HHH CB  
242  C CG  . TYR A 33  ? 2.073 2.130 1.786 0.269  0.229  0.429  32  TYR HHH CG  
243  C CD1 . TYR A 33  ? 2.036 2.082 1.753 0.257  0.241  0.409  32  TYR HHH CD1 
244  C CD2 . TYR A 33  ? 2.071 2.142 1.799 0.275  0.218  0.429  32  TYR HHH CD2 
245  C CE1 . TYR A 33  ? 2.073 2.128 1.811 0.254  0.240  0.389  32  TYR HHH CE1 
246  C CE2 . TYR A 33  ? 2.164 2.239 1.905 0.274  0.217  0.412  32  TYR HHH CE2 
247  C CZ  . TYR A 33  ? 2.246 2.316 1.994 0.264  0.226  0.391  32  TYR HHH CZ  
248  O OH  . TYR A 33  ? 2.410 2.492 2.175 0.264  0.223  0.370  32  TYR HHH OH  
249  N N   . TRP A 34  ? 1.844 1.960 1.546 0.283  0.195  0.467  33  TRP HHH N   
250  C CA  . TRP A 34  ? 1.894 2.031 1.595 0.294  0.187  0.480  33  TRP HHH CA  
251  C C   . TRP A 34  ? 1.845 1.974 1.551 0.307  0.190  0.489  33  TRP HHH C   
252  O O   . TRP A 34  ? 2.299 2.424 2.019 0.303  0.191  0.482  33  TRP HHH O   
253  C CB  . TRP A 34  ? 1.961 2.130 1.682 0.287  0.176  0.472  33  TRP HHH CB  
254  C CG  . TRP A 34  ? 2.025 2.206 1.746 0.273  0.174  0.461  33  TRP HHH CG  
255  C CD1 . TRP A 34  ? 2.008 2.174 1.727 0.261  0.179  0.449  33  TRP HHH CD1 
256  C CD2 . TRP A 34  ? 1.962 2.176 1.689 0.269  0.166  0.456  33  TRP HHH CD2 
257  N NE1 . TRP A 34  ? 1.969 2.154 1.691 0.250  0.176  0.440  33  TRP HHH NE1 
258  C CE2 . TRP A 34  ? 1.937 2.152 1.663 0.254  0.168  0.443  33  TRP HHH CE2 
259  C CE3 . TRP A 34  ? 1.981 2.227 1.716 0.276  0.158  0.459  33  TRP HHH CE3 
260  C CZ2 . TRP A 34  ? 1.917 2.163 1.648 0.245  0.162  0.434  33  TRP HHH CZ2 
261  C CZ3 . TRP A 34  ? 1.912 2.193 1.655 0.267  0.152  0.448  33  TRP HHH CZ3 
262  C CH2 . TRP A 34  ? 1.894 2.173 1.634 0.251  0.154  0.436  33  TRP HHH CH2 
263  N N   . ILE A 35  ? 1.836 1.961 1.528 0.322  0.193  0.503  34  ILE HHH N   
264  C CA  . ILE A 35  ? 1.794 1.910 1.490 0.334  0.198  0.512  34  ILE HHH CA  
265  C C   . ILE A 35  ? 1.832 1.983 1.546 0.341  0.186  0.515  34  ILE HHH C   
266  O O   . ILE A 35  ? 1.884 2.060 1.595 0.347  0.177  0.519  34  ILE HHH O   
267  C CB  . ILE A 35  ? 1.795 1.885 1.468 0.349  0.210  0.526  34  ILE HHH CB  
268  C CG1 . ILE A 35  ? 1.766 1.817 1.428 0.340  0.229  0.520  34  ILE HHH CG1 
269  C CG2 . ILE A 35  ? 1.848 1.943 1.530 0.365  0.210  0.537  34  ILE HHH CG2 
270  C CD1 . ILE A 35  ? 1.765 1.813 1.429 0.321  0.229  0.503  34  ILE HHH CD1 
271  N N   . GLY A 36  ? 1.908 2.058 1.638 0.340  0.188  0.512  35  GLY HHH N   
272  C CA  . GLY A 36  ? 1.948 2.127 1.698 0.344  0.182  0.512  35  GLY HHH CA  
273  C C   . GLY A 36  ? 1.991 2.161 1.743 0.358  0.189  0.521  35  GLY HHH C   
274  O O   . GLY A 36  ? 1.912 2.051 1.654 0.359  0.200  0.522  35  GLY HHH O   
275  N N   . TRP A 37  ? 1.993 2.190 1.759 0.368  0.184  0.524  36  TRP HHH N   
276  C CA  . TRP A 37  ? 2.026 2.219 1.800 0.382  0.191  0.531  36  TRP HHH CA  
277  C C   . TRP A 37  ? 2.140 2.349 1.937 0.373  0.193  0.521  36  TRP HHH C   
278  O O   . TRP A 37  ? 2.151 2.389 1.963 0.365  0.186  0.512  36  TRP HHH O   
279  C CB  . TRP A 37  ? 2.064 2.276 1.836 0.403  0.185  0.542  36  TRP HHH CB  
280  C CG  . TRP A 37  ? 2.222 2.405 1.964 0.414  0.190  0.555  36  TRP HHH CG  
281  C CD1 . TRP A 37  ? 2.372 2.557 2.094 0.415  0.184  0.558  36  TRP HHH CD1 
282  C CD2 . TRP A 37  ? 2.270 2.412 1.997 0.425  0.206  0.565  36  TRP HHH CD2 
283  N NE1 . TRP A 37  ? 2.336 2.482 2.029 0.426  0.196  0.571  36  TRP HHH NE1 
284  C CE2 . TRP A 37  ? 2.354 2.472 2.051 0.432  0.211  0.575  36  TRP HHH CE2 
285  C CE3 . TRP A 37  ? 2.253 2.375 1.989 0.428  0.220  0.566  36  TRP HHH CE3 
286  C CZ2 . TRP A 37  ? 2.447 2.519 2.124 0.441  0.230  0.586  36  TRP HHH CZ2 
287  C CZ3 . TRP A 37  ? 2.292 2.373 2.011 0.437  0.237  0.575  36  TRP HHH CZ3 
288  C CH2 . TRP A 37  ? 2.390 2.445 2.080 0.443  0.244  0.585  36  TRP HHH CH2 
289  N N   . VAL A 38  ? 2.109 2.297 1.906 0.374  0.203  0.522  37  VAL HHH N   
290  C CA  . VAL A 38  ? 2.010 2.205 1.823 0.367  0.209  0.515  37  VAL HHH CA  
291  C C   . VAL A 38  ? 1.883 2.079 1.706 0.381  0.217  0.519  37  VAL HHH C   
292  O O   . VAL A 38  ? 1.750 1.921 1.561 0.389  0.224  0.526  37  VAL HHH O   
293  C CB  . VAL A 38  ? 2.289 2.456 2.089 0.355  0.215  0.509  37  VAL HHH CB  
294  C CG1 . VAL A 38  ? 2.461 2.628 2.269 0.351  0.224  0.505  37  VAL HHH CG1 
295  C CG2 . VAL A 38  ? 2.334 2.500 2.127 0.344  0.208  0.504  37  VAL HHH CG2 
296  N N   . ARG A 39  ? 1.945 2.169 1.791 0.382  0.218  0.514  38  ARG HHH N   
297  C CA  . ARG A 39  ? 2.025 2.255 1.887 0.394  0.226  0.516  38  ARG HHH CA  
298  C C   . ARG A 39  ? 2.046 2.262 1.910 0.381  0.239  0.508  38  ARG HHH C   
299  O O   . ARG A 39  ? 1.995 2.220 1.865 0.367  0.240  0.499  38  ARG HHH O   
300  C CB  . ARG A 39  ? 2.088 2.364 1.976 0.405  0.217  0.512  38  ARG HHH CB  
301  C CG  . ARG A 39  ? 2.170 2.457 2.078 0.421  0.224  0.514  38  ARG HHH CG  
302  C CD  . ARG A 39  ? 2.310 2.623 2.247 0.411  0.231  0.498  38  ARG HHH CD  
303  N NE  . ARG A 39  ? 2.351 2.717 2.316 0.412  0.220  0.486  38  ARG HHH NE  
304  C CZ  . ARG A 39  ? 2.284 2.693 2.280 0.427  0.216  0.479  38  ARG HHH CZ  
305  N NH1 . ARG A 39  ? 2.242 2.644 2.245 0.444  0.223  0.485  38  ARG HHH NH1 
306  N NH2 . ARG A 39  ? 2.297 2.760 2.319 0.425  0.205  0.463  38  ARG HHH NH2 
307  N N   . GLN A 40  ? 2.065 2.260 1.925 0.386  0.251  0.510  39  GLN HHH N   
308  C CA  . GLN A 40  ? 2.027 2.209 1.886 0.375  0.265  0.503  39  GLN HHH CA  
309  C C   . GLN A 40  ? 2.055 2.241 1.931 0.385  0.276  0.502  39  GLN HHH C   
310  O O   . GLN A 40  ? 2.118 2.283 1.985 0.394  0.281  0.507  39  GLN HHH O   
311  C CB  . GLN A 40  ? 2.035 2.183 1.865 0.368  0.268  0.503  39  GLN HHH CB  
312  C CG  . GLN A 40  ? 1.980 2.113 1.801 0.362  0.282  0.497  39  GLN HHH CG  
313  C CD  . GLN A 40  ? 1.995 2.104 1.787 0.356  0.281  0.495  39  GLN HHH CD  
314  O OE1 . GLN A 40  ? 1.924 2.026 1.701 0.348  0.280  0.494  39  GLN HHH OE1 
315  N NE2 . GLN A 40  ? 1.995 2.091 1.778 0.360  0.281  0.494  39  GLN HHH NE2 
316  N N   . MET A 41  ? 2.045 2.255 1.946 0.384  0.282  0.494  40  MET HHH N   
317  C CA  . MET A 41  ? 2.278 2.498 2.201 0.396  0.292  0.492  40  MET HHH CA  
318  C C   . MET A 41  ? 2.365 2.557 2.276 0.386  0.310  0.487  40  MET HHH C   
319  O O   . MET A 41  ? 2.681 2.857 2.572 0.370  0.314  0.484  40  MET HHH O   
320  C CB  . MET A 41  ? 2.309 2.574 2.269 0.398  0.290  0.482  40  MET HHH CB  
321  C CG  . MET A 41  ? 2.338 2.635 2.308 0.407  0.271  0.484  40  MET HHH CG  
322  S SD  . MET A 41  ? 2.509 2.871 2.528 0.408  0.267  0.465  40  MET HHH SD  
323  C CE  . MET A 41  ? 2.560 2.937 2.605 0.434  0.272  0.467  40  MET HHH CE  
324  N N   . PRO A 42  ? 2.394 2.577 2.314 0.395  0.322  0.487  41  PRO HHH N   
325  C CA  . PRO A 42  ? 2.424 2.579 2.326 0.386  0.339  0.481  41  PRO HHH CA  
326  C C   . PRO A 42  ? 2.441 2.597 2.338 0.368  0.349  0.472  41  PRO HHH C   
327  O O   . PRO A 42  ? 2.376 2.556 2.301 0.367  0.356  0.464  41  PRO HHH O   
328  C CB  . PRO A 42  ? 2.402 2.559 2.326 0.399  0.352  0.480  41  PRO HHH CB  
329  C CG  . PRO A 42  ? 2.437 2.607 2.375 0.420  0.339  0.491  41  PRO HHH CG  
330  C CD  . PRO A 42  ? 2.437 2.636 2.381 0.417  0.321  0.492  41  PRO HHH CD  
331  N N   . GLY A 43  ? 2.412 2.543 2.274 0.357  0.350  0.473  42  GLY HHH N   
332  C CA  . GLY A 43  ? 2.438 2.557 2.281 0.343  0.362  0.467  42  GLY HHH CA  
333  C C   . GLY A 43  ? 2.394 2.519 2.235 0.335  0.355  0.469  42  GLY HHH C   
334  O O   . GLY A 43  ? 2.577 2.683 2.395 0.324  0.366  0.467  42  GLY HHH O   
335  N N   . LYS A 44  ? 2.313 2.462 2.175 0.340  0.339  0.472  43  LYS HHH N   
336  C CA  . LYS A 44  ? 2.269 2.431 2.139 0.331  0.335  0.469  43  LYS HHH CA  
337  C C   . LYS A 44  ? 2.084 2.232 1.928 0.331  0.319  0.477  43  LYS HHH C   
338  O O   . LYS A 44  ? 2.033 2.163 1.856 0.338  0.312  0.483  43  LYS HHH O   
339  C CB  . LYS A 44  ? 2.388 2.595 2.302 0.337  0.328  0.462  43  LYS HHH CB  
340  C CG  . LYS A 44  ? 2.468 2.696 2.413 0.344  0.338  0.455  43  LYS HHH CG  
341  C CD  . LYS A 44  ? 2.613 2.832 2.561 0.331  0.362  0.444  43  LYS HHH CD  
342  C CE  . LYS A 44  ? 2.707 2.951 2.681 0.316  0.372  0.428  43  LYS HHH CE  
343  N NZ  . LYS A 44  ? 2.795 3.022 2.768 0.301  0.400  0.417  43  LYS HHH NZ  
344  N N   . GLY A 45  ? 1.930 2.087 1.780 0.323  0.316  0.474  44  GLY HHH N   
345  C CA  . GLY A 45  ? 2.024 2.165 1.850 0.321  0.304  0.480  44  GLY HHH CA  
346  C C   . GLY A 45  ? 2.025 2.180 1.856 0.330  0.284  0.486  44  GLY HHH C   
347  O O   . GLY A 45  ? 2.206 2.377 2.053 0.341  0.280  0.487  44  GLY HHH O   
348  N N   . LEU A 46  ? 1.971 2.117 1.787 0.327  0.274  0.488  45  LEU HHH N   
349  C CA  . LEU A 46  ? 1.939 2.100 1.761 0.332  0.258  0.491  45  LEU HHH CA  
350  C C   . LEU A 46  ? 1.985 2.181 1.834 0.326  0.254  0.484  45  LEU HHH C   
351  O O   . LEU A 46  ? 1.945 2.139 1.798 0.314  0.264  0.477  45  LEU HHH O   
352  C CB  . LEU A 46  ? 2.033 2.172 1.830 0.330  0.251  0.494  45  LEU HHH CB  
353  C CG  . LEU A 46  ? 2.052 2.164 1.823 0.335  0.252  0.496  45  LEU HHH CG  
354  C CD1 . LEU A 46  ? 1.881 1.979 1.632 0.334  0.243  0.496  45  LEU HHH CD1 
355  C CD2 . LEU A 46  ? 2.123 2.238 1.899 0.344  0.249  0.498  45  LEU HHH CD2 
356  N N   . GLU A 47  ? 2.143 2.367 2.008 0.336  0.243  0.485  46  GLU HHH N   
357  C CA  . GLU A 47  ? 2.174 2.438 2.063 0.333  0.234  0.476  46  GLU HHH CA  
358  C C   . GLU A 47  ? 2.154 2.420 2.030 0.339  0.219  0.483  46  GLU HHH C   
359  O O   . GLU A 47  ? 2.020 2.282 1.888 0.354  0.212  0.493  46  GLU HHH O   
360  C CB  . GLU A 47  ? 2.225 2.529 2.145 0.344  0.233  0.471  46  GLU HHH CB  
361  C CG  . GLU A 47  ? 2.292 2.604 2.233 0.336  0.250  0.460  46  GLU HHH CG  
362  C CD  . GLU A 47  ? 2.306 2.660 2.280 0.349  0.248  0.453  46  GLU HHH CD  
363  O OE1 . GLU A 47  ? 2.332 2.673 2.303 0.363  0.251  0.462  46  GLU HHH OE1 
364  O OE2 . GLU A 47  ? 2.264 2.666 2.269 0.347  0.243  0.437  46  GLU HHH OE2 
365  N N   . TRP A 48  ? 2.191 2.462 2.066 0.327  0.215  0.477  47  TRP HHH N   
366  C CA  . TRP A 48  ? 2.205 2.481 2.069 0.329  0.201  0.480  47  TRP HHH CA  
367  C C   . TRP A 48  ? 2.205 2.527 2.086 0.339  0.190  0.477  47  TRP HHH C   
368  O O   . TRP A 48  ? 2.269 2.628 2.176 0.332  0.190  0.462  47  TRP HHH O   
369  C CB  . TRP A 48  ? 2.241 2.507 2.100 0.312  0.203  0.473  47  TRP HHH CB  
370  C CG  . TRP A 48  ? 2.340 2.605 2.185 0.313  0.192  0.475  47  TRP HHH CG  
371  C CD1 . TRP A 48  ? 2.462 2.697 2.285 0.315  0.189  0.482  47  TRP HHH CD1 
372  C CD2 . TRP A 48  ? 2.388 2.688 2.243 0.309  0.182  0.467  47  TRP HHH CD2 
373  N NE1 . TRP A 48  ? 2.466 2.710 2.282 0.313  0.181  0.481  47  TRP HHH NE1 
374  C CE2 . TRP A 48  ? 2.462 2.745 2.295 0.310  0.176  0.473  47  TRP HHH CE2 
375  C CE3 . TRP A 48  ? 2.384 2.730 2.263 0.305  0.178  0.454  47  TRP HHH CE3 
376  C CZ2 . TRP A 48  ? 2.430 2.737 2.262 0.306  0.166  0.467  47  TRP HHH CZ2 
377  C CZ3 . TRP A 48  ? 2.395 2.770 2.274 0.303  0.167  0.447  47  TRP HHH CZ3 
378  C CH2 . TRP A 48  ? 2.401 2.754 2.255 0.304  0.161  0.455  47  TRP HHH CH2 
379  N N   . MET A 49  ? 2.079 2.399 1.945 0.356  0.180  0.489  48  MET HHH N   
380  C CA  . MET A 49  ? 1.998 2.359 1.873 0.373  0.168  0.490  48  MET HHH CA  
381  C C   . MET A 49  ? 2.061 2.442 1.928 0.367  0.156  0.485  48  MET HHH C   
382  O O   . MET A 49  ? 2.161 2.590 2.050 0.363  0.149  0.469  48  MET HHH O   
383  C CB  . MET A 49  ? 1.945 2.286 1.802 0.397  0.167  0.509  48  MET HHH CB  
384  C CG  . MET A 49  ? 1.989 2.319 1.858 0.404  0.178  0.511  48  MET HHH CG  
385  S SD  . MET A 49  ? 1.931 2.232 1.781 0.431  0.182  0.532  48  MET HHH SD  
386  C CE  . MET A 49  ? 2.076 2.432 1.940 0.458  0.165  0.534  48  MET HHH CE  
387  N N   . GLY A 50  ? 2.121 2.468 1.958 0.366  0.155  0.495  49  GLY HHH N   
388  C CA  . GLY A 50  ? 2.081 2.439 1.905 0.361  0.146  0.492  49  GLY HHH CA  
389  C C   . GLY A 50  ? 2.096 2.407 1.893 0.354  0.152  0.499  49  GLY HHH C   
390  O O   . GLY A 50  ? 2.249 2.521 2.038 0.354  0.162  0.506  49  GLY HHH O   
391  N N   . ILE A 51  ? 2.102 2.417 1.885 0.347  0.147  0.496  50  ILE HHH N   
392  C CA  . ILE A 51  ? 2.194 2.470 1.954 0.339  0.153  0.499  50  ILE HHH CA  
393  C C   . ILE A 51  ? 2.288 2.573 2.025 0.344  0.146  0.503  50  ILE HHH C   
394  O O   . ILE A 51  ? 2.368 2.695 2.113 0.345  0.135  0.496  50  ILE HHH O   
395  C CB  . ILE A 51  ? 2.268 2.537 2.041 0.317  0.157  0.485  50  ILE HHH CB  
396  C CG1 . ILE A 51  ? 2.310 2.540 2.065 0.310  0.163  0.486  50  ILE HHH CG1 
397  C CG2 . ILE A 51  ? 2.242 2.547 2.027 0.305  0.150  0.470  50  ILE HHH CG2 
398  C CD1 . ILE A 51  ? 2.382 2.600 2.149 0.296  0.167  0.474  50  ILE HHH CD1 
399  N N   . ILE A 52  ? 2.360 2.607 2.070 0.346  0.153  0.512  51  ILE HHH N   
400  C CA  . ILE A 52  ? 2.327 2.572 2.006 0.352  0.151  0.518  51  ILE HHH CA  
401  C C   . ILE A 52  ? 2.261 2.469 1.926 0.336  0.163  0.514  51  ILE HHH C   
402  O O   . ILE A 52  ? 2.414 2.589 2.081 0.333  0.174  0.514  51  ILE HHH O   
403  C CB  . ILE A 52  ? 2.419 2.650 2.072 0.379  0.153  0.539  51  ILE HHH CB  
404  C CG1 . ILE A 52  ? 2.499 2.725 2.113 0.388  0.152  0.548  51  ILE HHH CG1 
405  C CG2 . ILE A 52  ? 2.417 2.601 2.065 0.382  0.170  0.548  51  ILE HHH CG2 
406  C CD1 . ILE A 52  ? 2.628 2.850 2.215 0.420  0.150  0.570  51  ILE HHH CD1 
407  N N   . TYR A 53  ? 2.204 2.422 1.856 0.327  0.159  0.507  52  TYR HHH N   
408  C CA  . TYR A 53  ? 2.080 2.267 1.717 0.312  0.171  0.500  52  TYR HHH CA  
409  C C   . TYR A 53  ? 1.971 2.134 1.566 0.325  0.178  0.516  52  TYR HHH C   
410  O O   . TYR A 53  ? 2.029 2.213 1.603 0.331  0.170  0.519  52  TYR HHH O   
411  C CB  . TYR A 53  ? 2.014 2.227 1.662 0.293  0.165  0.483  52  TYR HHH CB  
412  C CG  . TYR A 53  ? 1.971 2.155 1.607 0.277  0.176  0.474  52  TYR HHH CG  
413  C CD1 . TYR A 53  ? 2.090 2.245 1.738 0.269  0.187  0.467  52  TYR HHH CD1 
414  C CD2 . TYR A 53  ? 1.925 2.116 1.539 0.272  0.177  0.470  52  TYR HHH CD2 
415  C CE1 . TYR A 53  ? 2.103 2.236 1.745 0.255  0.199  0.455  52  TYR HHH CE1 
416  C CE2 . TYR A 53  ? 2.026 2.191 1.631 0.256  0.190  0.460  52  TYR HHH CE2 
417  C CZ  . TYR A 53  ? 2.022 2.159 1.643 0.247  0.201  0.452  52  TYR HHH CZ  
418  O OH  . TYR A 53  ? 1.966 2.082 1.583 0.231  0.214  0.438  52  TYR HHH OH  
419  N N   . PRO A 54  ? 2.006 2.123 1.585 0.331  0.196  0.525  53  PRO HHH N   
420  C CA  . PRO A 54  ? 2.204 2.290 1.738 0.346  0.207  0.544  53  PRO HHH CA  
421  C C   . PRO A 54  ? 2.252 2.329 1.756 0.336  0.213  0.539  53  PRO HHH C   
422  O O   . PRO A 54  ? 1.897 1.954 1.356 0.352  0.220  0.557  53  PRO HHH O   
423  C CB  . PRO A 54  ? 2.287 2.324 1.820 0.346  0.229  0.547  53  PRO HHH CB  
424  C CG  . PRO A 54  ? 2.221 2.277 1.797 0.340  0.222  0.536  53  PRO HHH CG  
425  C CD  . PRO A 54  ? 2.064 2.158 1.665 0.323  0.206  0.518  53  PRO HHH CD  
426  N N   . GLY A 55  ? 2.218 2.308 1.743 0.311  0.211  0.518  54  GLY HHH N   
427  C CA  . GLY A 55  ? 2.286 2.373 1.788 0.297  0.216  0.510  54  GLY HHH CA  
428  C C   . GLY A 55  ? 2.158 2.268 1.625 0.314  0.204  0.523  54  GLY HHH C   
429  O O   . GLY A 55  ? 2.014 2.098 1.437 0.314  0.216  0.529  54  GLY HHH O   
430  N N   . ASP A 56  ? 2.107 2.267 1.592 0.325  0.182  0.524  55  ASP HHH N   
431  C CA  . ASP A 56  ? 2.185 2.387 1.647 0.341  0.164  0.530  55  ASP HHH CA  
432  C C   . ASP A 56  ? 2.132 2.369 1.613 0.364  0.147  0.538  55  ASP HHH C   
433  O O   . ASP A 56  ? 2.046 2.337 1.528 0.374  0.127  0.534  55  ASP HHH O   
434  C CB  . ASP A 56  ? 2.264 2.507 1.742 0.319  0.154  0.506  55  ASP HHH CB  
435  C CG  . ASP A 56  ? 2.280 2.551 1.815 0.299  0.148  0.484  55  ASP HHH CG  
436  O OD1 . ASP A 56  ? 2.381 2.657 1.944 0.306  0.144  0.487  55  ASP HHH OD1 
437  O OD2 . ASP A 56  ? 2.377 2.662 1.927 0.276  0.149  0.464  55  ASP HHH OD2 
438  N N   . SER A 57  ? 2.257 2.471 1.758 0.369  0.154  0.545  56  SER HHH N   
439  C CA  . SER A 57  ? 2.322 2.561 1.843 0.390  0.143  0.553  56  SER HHH CA  
440  C C   . SER A 57  ? 2.354 2.659 1.916 0.382  0.123  0.533  56  SER HHH C   
441  O O   . SER A 57  ? 2.602 2.947 2.172 0.403  0.108  0.538  56  SER HHH O   
442  C CB  . SER A 57  ? 2.187 2.417 1.665 0.425  0.141  0.578  56  SER HHH CB  
443  O OG  . SER A 57  ? 2.010 2.173 1.447 0.428  0.164  0.595  56  SER HHH OG  
444  N N   . GLU A 58  ? 2.211 2.526 1.800 0.353  0.125  0.511  57  GLU HHH N   
445  C CA  . GLU A 58  ? 2.211 2.579 1.844 0.340  0.113  0.490  57  GLU HHH CA  
446  C C   . GLU A 58  ? 2.218 2.582 1.882 0.345  0.116  0.493  57  GLU HHH C   
447  O O   . GLU A 58  ? 2.346 2.670 2.018 0.335  0.128  0.494  57  GLU HHH O   
448  C CB  . GLU A 58  ? 2.167 2.535 1.821 0.309  0.119  0.468  57  GLU HHH CB  
449  C CG  . GLU A 58  ? 2.147 2.553 1.846 0.295  0.115  0.448  57  GLU HHH CG  
450  C CD  . GLU A 58  ? 2.168 2.568 1.887 0.266  0.123  0.428  57  GLU HHH CD  
451  O OE1 . GLU A 58  ? 2.210 2.622 1.964 0.254  0.127  0.414  57  GLU HHH OE1 
452  O OE2 . GLU A 58  ? 2.235 2.616 1.934 0.257  0.129  0.425  57  GLU HHH OE2 
453  N N   . THR A 59  ? 2.277 2.682 1.958 0.361  0.104  0.493  58  THR HHH N   
454  C CA  . THR A 59  ? 2.382 2.783 2.091 0.366  0.108  0.495  58  THR HHH CA  
455  C C   . THR A 59  ? 2.320 2.773 2.073 0.352  0.102  0.472  58  THR HHH C   
456  O O   . THR A 59  ? 2.285 2.788 2.044 0.350  0.090  0.458  58  THR HHH O   
457  C CB  . THR A 59  ? 2.463 2.857 2.155 0.398  0.105  0.517  58  THR HHH CB  
458  O OG1 . THR A 59  ? 2.588 3.038 2.309 0.408  0.092  0.508  58  THR HHH OG1 
459  C CG2 . THR A 59  ? 2.414 2.789 2.057 0.417  0.104  0.535  58  THR HHH CG2 
460  N N   . ARG A 60  ? 2.231 2.669 2.011 0.342  0.112  0.467  59  ARG HHH N   
461  C CA  . ARG A 60  ? 2.272 2.749 2.093 0.329  0.113  0.446  59  ARG HHH CA  
462  C C   . ARG A 60  ? 2.314 2.789 2.151 0.342  0.116  0.454  59  ARG HHH C   
463  O O   . ARG A 60  ? 2.521 2.947 2.344 0.346  0.126  0.469  59  ARG HHH O   
464  C CB  . ARG A 60  ? 2.163 2.618 1.999 0.301  0.126  0.433  59  ARG HHH CB  
465  C CG  . ARG A 60  ? 2.090 2.529 1.906 0.289  0.126  0.430  59  ARG HHH CG  
466  C CD  . ARG A 60  ? 2.043 2.497 1.882 0.263  0.133  0.406  59  ARG HHH CD  
467  N NE  . ARG A 60  ? 2.078 2.506 1.899 0.253  0.136  0.406  59  ARG HHH NE  
468  C CZ  . ARG A 60  ? 2.074 2.479 1.905 0.234  0.147  0.396  59  ARG HHH CZ  
469  N NH1 . ARG A 60  ? 2.040 2.425 1.856 0.226  0.149  0.395  59  ARG HHH NH1 
470  N NH2 . ARG A 60  ? 2.197 2.598 2.054 0.223  0.159  0.386  59  ARG HHH NH2 
471  N N   . TYR A 61  ? 2.247 2.774 2.111 0.349  0.109  0.441  60  TYR HHH N   
472  C CA  . TYR A 61  ? 2.280 2.813 2.167 0.359  0.114  0.443  60  TYR HHH CA  
473  C C   . TYR A 61  ? 2.138 2.680 2.060 0.333  0.128  0.421  60  TYR HHH C   
474  O O   . TYR A 61  ? 1.997 2.566 1.936 0.313  0.130  0.400  60  TYR HHH O   
475  C CB  . TYR A 61  ? 2.400 2.987 2.295 0.385  0.098  0.443  60  TYR HHH CB  
476  C CG  . TYR A 61  ? 2.506 3.075 2.360 0.414  0.087  0.468  60  TYR HHH CG  
477  C CD1 . TYR A 61  ? 2.547 3.073 2.384 0.434  0.094  0.491  60  TYR HHH CD1 
478  C CD2 . TYR A 61  ? 2.492 3.083 2.321 0.420  0.073  0.468  60  TYR HHH CD2 
479  C CE1 . TYR A 61  ? 2.526 3.028 2.323 0.460  0.089  0.515  60  TYR HHH CE1 
480  C CE2 . TYR A 61  ? 2.528 3.095 2.314 0.447  0.067  0.493  60  TYR HHH CE2 
481  C CZ  . TYR A 61  ? 2.543 3.064 2.313 0.467  0.076  0.517  60  TYR HHH CZ  
482  O OH  . TYR A 61  ? 2.577 3.070 2.302 0.493  0.075  0.542  60  TYR HHH OH  
483  N N   . SER A 62  ? 2.047 2.562 1.979 0.334  0.141  0.427  61  SER HHH N   
484  C CA  . SER A 62  ? 2.087 2.614 2.052 0.315  0.156  0.407  61  SER HHH CA  
485  C C   . SER A 62  ? 2.093 2.687 2.093 0.324  0.148  0.389  61  SER HHH C   
486  O O   . SER A 62  ? 2.011 2.624 2.009 0.350  0.136  0.401  61  SER HHH O   
487  C CB  . SER A 62  ? 2.185 2.663 2.144 0.314  0.172  0.419  61  SER HHH CB  
488  O OG  . SER A 62  ? 2.311 2.800 2.299 0.298  0.189  0.401  61  SER HHH OG  
489  N N   . PRO A 63  ? 2.183 2.817 2.219 0.302  0.156  0.360  62  PRO HHH N   
490  C CA  . PRO A 63  ? 2.208 2.911 2.286 0.306  0.153  0.336  62  PRO HHH CA  
491  C C   . PRO A 63  ? 2.104 2.810 2.194 0.327  0.153  0.345  62  PRO HHH C   
492  O O   . PRO A 63  ? 2.080 2.848 2.196 0.344  0.139  0.332  62  PRO HHH O   
493  C CB  . PRO A 63  ? 2.177 2.886 2.287 0.272  0.177  0.306  62  PRO HHH CB  
494  C CG  . PRO A 63  ? 2.168 2.841 2.254 0.255  0.181  0.310  62  PRO HHH CG  
495  C CD  . PRO A 63  ? 2.156 2.770 2.194 0.273  0.172  0.346  62  PRO HHH CD  
496  N N   . SER A 64  ? 2.082 2.725 2.151 0.328  0.167  0.365  63  SER HHH N   
497  C CA  . SER A 64  ? 2.239 2.876 2.317 0.346  0.171  0.375  63  SER HHH CA  
498  C C   . SER A 64  ? 2.204 2.846 2.261 0.381  0.150  0.398  63  SER HHH C   
499  O O   . SER A 64  ? 2.100 2.753 2.171 0.400  0.150  0.402  63  SER HHH O   
500  C CB  . SER A 64  ? 2.375 2.945 2.435 0.334  0.192  0.388  63  SER HHH CB  
501  O OG  . SER A 64  ? 2.456 3.020 2.534 0.306  0.215  0.368  63  SER HHH OG  
502  N N   . PHE A 65  ? 2.210 2.839 2.233 0.389  0.136  0.413  64  PHE HHH N   
503  C CA  . PHE A 65  ? 2.246 2.865 2.240 0.422  0.122  0.438  64  PHE HHH CA  
504  C C   . PHE A 65  ? 2.306 2.964 2.285 0.436  0.100  0.437  64  PHE HHH C   
505  O O   . PHE A 65  ? 2.363 3.007 2.311 0.464  0.090  0.460  64  PHE HHH O   
506  C CB  . PHE A 65  ? 2.229 2.771 2.181 0.421  0.132  0.464  64  PHE HHH CB  
507  C CG  . PHE A 65  ? 2.139 2.640 2.097 0.412  0.151  0.467  64  PHE HHH CG  
508  C CD1 . PHE A 65  ? 2.075 2.554 2.038 0.383  0.166  0.456  64  PHE HHH CD1 
509  C CD2 . PHE A 65  ? 2.076 2.558 2.031 0.432  0.156  0.481  64  PHE HHH CD2 
510  C CE1 . PHE A 65  ? 2.153 2.596 2.116 0.376  0.183  0.459  64  PHE HHH CE1 
511  C CE2 . PHE A 65  ? 2.058 2.505 2.017 0.422  0.174  0.482  64  PHE HHH CE2 
512  C CZ  . PHE A 65  ? 2.089 2.517 2.050 0.395  0.187  0.471  64  PHE HHH CZ  
513  N N   . GLN A 66  ? 2.317 3.022 2.315 0.417  0.094  0.412  65  GLN HHH N   
514  C CA  . GLN A 66  ? 2.408 3.159 2.391 0.431  0.072  0.409  65  GLN HHH CA  
515  C C   . GLN A 66  ? 2.359 3.167 2.356 0.468  0.053  0.409  65  GLN HHH C   
516  O O   . GLN A 66  ? 2.311 3.162 2.353 0.467  0.055  0.389  65  GLN HHH O   
517  C CB  . GLN A 66  ? 2.464 3.259 2.470 0.403  0.071  0.377  65  GLN HHH CB  
518  C CG  . GLN A 66  ? 2.503 3.340 2.488 0.415  0.049  0.375  65  GLN HHH CG  
519  C CD  . GLN A 66  ? 2.560 3.371 2.525 0.387  0.055  0.370  65  GLN HHH CD  
520  O OE1 . GLN A 66  ? 2.867 3.655 2.850 0.355  0.073  0.356  65  GLN HHH OE1 
521  N NE2 . GLN A 66  ? 2.483 3.297 2.409 0.401  0.040  0.381  65  GLN HHH NE2 
522  N N   . GLY A 67  ? 2.403 3.206 2.360 0.500  0.037  0.433  66  GLY HHH N   
523  C CA  . GLY A 67  ? 2.539 3.394 2.501 0.542  0.017  0.437  66  GLY HHH CA  
524  C C   . GLY A 67  ? 2.586 3.408 2.552 0.565  0.026  0.456  66  GLY HHH C   
525  O O   . GLY A 67  ? 2.922 3.778 2.887 0.605  0.010  0.465  66  GLY HHH O   
526  N N   . GLN A 68  ? 2.390 3.152 2.361 0.543  0.050  0.462  67  GLN HHH N   
527  C CA  . GLN A 68  ? 2.352 3.081 2.330 0.561  0.062  0.478  67  GLN HHH CA  
528  C C   . GLN A 68  ? 2.256 2.901 2.181 0.572  0.073  0.513  67  GLN HHH C   
529  O O   . GLN A 68  ? 2.186 2.803 2.104 0.598  0.080  0.531  67  GLN HHH O   
530  C CB  . GLN A 68  ? 2.394 3.119 2.413 0.530  0.082  0.457  67  GLN HHH CB  
531  C CG  . GLN A 68  ? 2.497 3.300 2.566 0.512  0.076  0.419  67  GLN HHH CG  
532  C CD  . GLN A 68  ? 2.665 3.481 2.781 0.497  0.093  0.399  67  GLN HHH CD  
533  O OE1 . GLN A 68  ? 2.903 3.670 3.014 0.500  0.109  0.413  67  GLN HHH OE1 
534  N NE2 . GLN A 68  ? 2.815 3.697 2.977 0.480  0.093  0.362  67  GLN HHH NE2 
535  N N   . VAL A 69  ? 2.269 2.875 2.161 0.551  0.077  0.519  68  VAL HHH N   
536  C CA  . VAL A 69  ? 2.386 2.918 2.226 0.560  0.088  0.548  68  VAL HHH CA  
537  C C   . VAL A 69  ? 2.421 2.954 2.227 0.554  0.078  0.551  68  VAL HHH C   
538  O O   . VAL A 69  ? 2.258 2.836 2.083 0.533  0.068  0.528  68  VAL HHH O   
539  C CB  . VAL A 69  ? 2.336 2.803 2.173 0.534  0.112  0.552  68  VAL HHH CB  
540  C CG1 . VAL A 69  ? 2.270 2.730 2.135 0.539  0.124  0.551  68  VAL HHH CG1 
541  C CG2 . VAL A 69  ? 2.268 2.733 2.115 0.496  0.116  0.534  68  VAL HHH CG2 
542  N N   . THR A 70  ? 2.552 3.029 2.309 0.568  0.085  0.577  69  THR HHH N   
543  C CA  . THR A 70  ? 2.620 3.080 2.336 0.562  0.082  0.583  69  THR HHH CA  
544  C C   . THR A 70  ? 2.470 2.851 2.162 0.542  0.105  0.594  69  THR HHH C   
545  O O   . THR A 70  ? 2.393 2.728 2.081 0.551  0.122  0.607  69  THR HHH O   
546  C CB  . THR A 70  ? 2.810 3.284 2.487 0.602  0.067  0.602  69  THR HHH CB  
547  O OG1 . THR A 70  ? 2.917 3.325 2.558 0.625  0.084  0.631  69  THR HHH OG1 
548  C CG2 . THR A 70  ? 2.782 3.336 2.488 0.629  0.044  0.591  69  THR HHH CG2 
549  N N   . ILE A 71  ? 2.352 2.722 2.032 0.515  0.107  0.585  70  ILE HHH N   
550  C CA  . ILE A 71  ? 2.419 2.725 2.081 0.493  0.128  0.588  70  ILE HHH CA  
551  C C   . ILE A 71  ? 2.321 2.604 1.937 0.497  0.129  0.599  70  ILE HHH C   
552  O O   . ILE A 71  ? 2.327 2.640 1.942 0.483  0.118  0.586  70  ILE HHH O   
553  C CB  . ILE A 71  ? 2.518 2.832 2.213 0.457  0.130  0.566  70  ILE HHH CB  
554  C CG1 . ILE A 71  ? 2.653 2.979 2.386 0.454  0.134  0.557  70  ILE HHH CG1 
555  C CG2 . ILE A 71  ? 2.450 2.710 2.125 0.437  0.146  0.566  70  ILE HHH CG2 
556  C CD1 . ILE A 71  ? 2.703 3.038 2.464 0.423  0.137  0.537  70  ILE HHH CD1 
557  N N   . SER A 72  ? 2.286 2.514 1.865 0.514  0.145  0.621  71  SER HHH N   
558  C CA  . SER A 72  ? 2.308 2.497 1.838 0.515  0.154  0.633  71  SER HHH CA  
559  C C   . SER A 72  ? 2.205 2.342 1.735 0.485  0.177  0.624  71  SER HHH C   
560  O O   . SER A 72  ? 2.124 2.256 1.687 0.469  0.183  0.613  71  SER HHH O   
561  C CB  . SER A 72  ? 2.549 2.705 2.035 0.552  0.162  0.661  71  SER HHH CB  
562  O OG  . SER A 72  ? 2.721 2.857 2.225 0.567  0.172  0.670  71  SER HHH OG  
563  N N   . ALA A 73  ? 2.239 2.343 1.733 0.477  0.188  0.628  72  ALA HHH N   
564  C CA  . ALA A 73  ? 2.260 2.310 1.748 0.453  0.213  0.621  72  ALA HHH CA  
565  C C   . ALA A 73  ? 2.377 2.381 1.810 0.461  0.230  0.636  72  ALA HHH C   
566  O O   . ALA A 73  ? 2.340 2.370 1.748 0.470  0.215  0.641  72  ALA HHH O   
567  C CB  . ALA A 73  ? 2.179 2.253 1.699 0.421  0.206  0.596  72  ALA HHH CB  
568  N N   . ASP A 74  ? 2.426 2.367 1.842 0.457  0.260  0.642  73  ASP HHH N   
569  C CA  . ASP A 74  ? 2.405 2.291 1.768 0.457  0.285  0.652  73  ASP HHH CA  
570  C C   . ASP A 74  ? 2.250 2.115 1.628 0.420  0.302  0.628  73  ASP HHH C   
571  O O   . ASP A 74  ? 2.272 2.107 1.669 0.406  0.322  0.617  73  ASP HHH O   
572  C CB  . ASP A 74  ? 2.602 2.429 1.931 0.483  0.310  0.677  73  ASP HHH CB  
573  C CG  . ASP A 74  ? 2.825 2.594 2.091 0.489  0.336  0.693  73  ASP HHH CG  
574  O OD1 . ASP A 74  ? 2.889 2.660 2.146 0.466  0.338  0.679  73  ASP HHH OD1 
575  O OD2 . ASP A 74  ? 2.861 2.579 2.085 0.518  0.356  0.720  73  ASP HHH OD2 
576  N N   . LYS A 75  ? 2.202 2.090 1.575 0.403  0.292  0.616  74  LYS HHH N   
577  C CA  . LYS A 75  ? 2.270 2.153 1.665 0.368  0.302  0.588  74  LYS HHH CA  
578  C C   . LYS A 75  ? 2.349 2.164 1.719 0.359  0.340  0.588  74  LYS HHH C   
579  O O   . LYS A 75  ? 2.490 2.296 1.889 0.333  0.353  0.563  74  LYS HHH O   
580  C CB  . LYS A 75  ? 2.414 2.326 1.798 0.357  0.288  0.580  74  LYS HHH CB  
581  C CG  . LYS A 75  ? 2.639 2.528 1.962 0.373  0.296  0.600  74  LYS HHH CG  
582  C CD  . LYS A 75  ? 2.741 2.661 2.055 0.358  0.283  0.588  74  LYS HHH CD  
583  C CE  . LYS A 75  ? 2.784 2.720 2.144 0.323  0.284  0.556  74  LYS HHH CE  
584  N NZ  . LYS A 75  ? 2.799 2.768 2.154 0.309  0.271  0.543  74  LYS HHH NZ  
585  N N   . SER A 76  ? 2.375 2.144 1.693 0.381  0.359  0.613  75  SER HHH N   
586  C CA  . SER A 76  ? 2.502 2.200 1.786 0.370  0.401  0.613  75  SER HHH CA  
587  C C   . SER A 76  ? 2.426 2.091 1.735 0.365  0.425  0.605  75  SER HHH C   
588  O O   . SER A 76  ? 2.482 2.094 1.778 0.348  0.463  0.595  75  SER HHH O   
589  C CB  . SER A 76  ? 2.744 2.399 1.959 0.398  0.415  0.645  75  SER HHH CB  
590  O OG  . SER A 76  ? 2.880 2.546 2.085 0.434  0.399  0.672  75  SER HHH OG  
591  N N   . ILE A 77  ? 2.318 2.015 1.663 0.376  0.407  0.607  76  ILE HHH N   
592  C CA  . ILE A 77  ? 2.312 1.985 1.685 0.370  0.427  0.596  76  ILE HHH CA  
593  C C   . ILE A 77  ? 2.268 1.998 1.700 0.357  0.401  0.574  76  ILE HHH C   
594  O O   . ILE A 77  ? 2.443 2.167 1.900 0.358  0.409  0.568  76  ILE HHH O   
595  C CB  . ILE A 77  ? 2.411 2.050 1.756 0.403  0.438  0.627  76  ILE HHH CB  
596  C CG1 . ILE A 77  ? 2.342 2.033 1.694 0.432  0.400  0.646  76  ILE HHH CG1 
597  C CG2 . ILE A 77  ? 2.643 2.216 1.925 0.416  0.469  0.648  76  ILE HHH CG2 
598  C CD1 . ILE A 77  ? 2.436 2.103 1.777 0.464  0.409  0.670  76  ILE HHH CD1 
599  N N   . ASN A 78  ? 2.191 1.972 1.643 0.346  0.372  0.562  77  ASN HHH N   
600  C CA  . ASN A 78  ? 2.051 1.883 1.553 0.334  0.348  0.542  77  ASN HHH CA  
601  C C   . ASN A 78  ? 1.890 1.742 1.409 0.354  0.334  0.555  77  ASN HHH C   
602  O O   . ASN A 78  ? 1.897 1.766 1.450 0.346  0.329  0.540  77  ASN HHH O   
603  C CB  . ASN A 78  ? 2.066 1.889 1.597 0.309  0.364  0.512  77  ASN HHH CB  
604  C CG  . ASN A 78  ? 2.124 1.933 1.646 0.287  0.377  0.495  77  ASN HHH CG  
605  O OD1 . ASN A 78  ? 2.173 1.983 1.669 0.290  0.372  0.505  77  ASN HHH OD1 
606  N ND2 . ASN A 78  ? 2.261 2.062 1.807 0.266  0.395  0.466  77  ASN HHH ND2 
607  N N   . THR A 79  ? 1.929 1.780 1.423 0.381  0.327  0.581  78  THR HHH N   
608  C CA  . THR A 79  ? 1.958 1.822 1.465 0.402  0.318  0.594  78  THR HHH CA  
609  C C   . THR A 79  ? 1.875 1.798 1.395 0.412  0.284  0.599  78  THR HHH C   
610  O O   . THR A 79  ? 1.987 1.923 1.485 0.415  0.274  0.604  78  THR HHH O   
611  C CB  . THR A 79  ? 2.122 1.937 1.594 0.428  0.341  0.619  78  THR HHH CB  
612  O OG1 . THR A 79  ? 2.085 1.846 1.553 0.413  0.377  0.608  78  THR HHH OG1 
613  C CG2 . THR A 79  ? 2.117 1.949 1.603 0.453  0.330  0.633  78  THR HHH CG2 
614  N N   . ALA A 80  ? 1.877 1.833 1.430 0.415  0.269  0.594  79  ALA HHH N   
615  C CA  . ALA A 80  ? 1.996 2.006 1.566 0.428  0.242  0.599  79  ALA HHH CA  
616  C C   . ALA A 80  ? 2.120 2.131 1.696 0.453  0.243  0.613  79  ALA HHH C   
617  O O   . ALA A 80  ? 2.083 2.062 1.666 0.452  0.262  0.612  79  ALA HHH O   
618  C CB  . ALA A 80  ? 1.961 2.009 1.566 0.406  0.226  0.578  79  ALA HHH CB  
619  N N   . TYR A 81  ? 2.307 2.356 1.882 0.475  0.224  0.623  80  TYR HHH N   
620  C CA  . TYR A 81  ? 2.376 2.432 1.956 0.505  0.222  0.638  80  TYR HHH CA  
621  C C   . TYR A 81  ? 2.465 2.584 2.084 0.506  0.199  0.627  80  TYR HHH C   
622  O O   . TYR A 81  ? 2.571 2.735 2.203 0.494  0.180  0.614  80  TYR HHH O   
623  C CB  . TYR A 81  ? 2.328 2.368 1.863 0.536  0.222  0.662  80  TYR HHH CB  
624  C CG  . TYR A 81  ? 2.472 2.439 1.967 0.539  0.253  0.676  80  TYR HHH CG  
625  C CD1 . TYR A 81  ? 2.566 2.485 2.064 0.543  0.279  0.681  80  TYR HHH CD1 
626  C CD2 . TYR A 81  ? 2.585 2.527 2.038 0.536  0.259  0.682  80  TYR HHH CD2 
627  C CE1 . TYR A 81  ? 2.594 2.444 2.057 0.543  0.312  0.691  80  TYR HHH CE1 
628  C CE2 . TYR A 81  ? 2.630 2.500 2.045 0.536  0.292  0.693  80  TYR HHH CE2 
629  C CZ  . TYR A 81  ? 2.560 2.383 1.981 0.539  0.319  0.697  80  TYR HHH CZ  
630  O OH  . TYR A 81  ? 2.279 2.030 1.667 0.536  0.356  0.704  80  TYR HHH OH  
631  N N   . LEU A 82  ? 2.391 2.515 2.033 0.518  0.202  0.629  81  LEU HHH N   
632  C CA  . LEU A 82  ? 2.292 2.474 1.971 0.524  0.184  0.620  81  LEU HHH CA  
633  C C   . LEU A 82  ? 2.272 2.457 1.946 0.562  0.184  0.638  81  LEU HHH C   
634  O O   . LEU A 82  ? 2.296 2.435 1.963 0.571  0.204  0.648  81  LEU HHH O   
635  C CB  . LEU A 82  ? 2.262 2.441 1.974 0.502  0.193  0.604  81  LEU HHH CB  
636  C CG  . LEU A 82  ? 2.239 2.470 1.991 0.503  0.181  0.592  81  LEU HHH CG  
637  C CD1 . LEU A 82  ? 2.213 2.495 1.979 0.491  0.161  0.577  81  LEU HHH CD1 
638  C CD2 . LEU A 82  ? 2.344 2.559 2.117 0.484  0.194  0.581  81  LEU HHH CD2 
639  N N   . GLN A 83  ? 2.170 2.405 1.844 0.584  0.162  0.641  82  GLN HHH N   
640  C CA  . GLN A 83  ? 2.247 2.490 1.912 0.627  0.157  0.659  82  GLN HHH CA  
641  C C   . GLN A 83  ? 2.100 2.418 1.811 0.637  0.137  0.644  82  GLN HHH C   
642  O O   . GLN A 83  ? 1.882 2.252 1.614 0.618  0.120  0.623  82  GLN HHH O   
643  C CB  . GLN A 83  ? 2.619 2.858 2.235 0.652  0.148  0.678  82  GLN HHH CB  
644  C CG  . GLN A 83  ? 2.820 3.094 2.430 0.699  0.132  0.692  82  GLN HHH CG  
645  C CD  . GLN A 83  ? 2.892 3.168 2.449 0.725  0.120  0.710  82  GLN HHH CD  
646  O OE1 . GLN A 83  ? 3.010 3.236 2.524 0.713  0.133  0.720  82  GLN HHH OE1 
647  N NE2 . GLN A 83  ? 2.890 3.226 2.449 0.762  0.094  0.713  82  GLN HHH NE2 
648  N N   . TRP A 84  ? 2.262 2.582 1.989 0.664  0.141  0.652  83  TRP HHH N   
649  C CA  . TRP A 84  ? 2.427 2.819 2.193 0.687  0.121  0.641  83  TRP HHH CA  
650  C C   . TRP A 84  ? 2.522 2.925 2.258 0.738  0.108  0.664  83  TRP HHH C   
651  O O   . TRP A 84  ? 2.713 3.052 2.399 0.756  0.122  0.691  83  TRP HHH O   
652  C CB  . TRP A 84  ? 2.430 2.818 2.237 0.683  0.135  0.633  83  TRP HHH CB  
653  C CG  . TRP A 84  ? 2.355 2.741 2.190 0.638  0.145  0.610  83  TRP HHH CG  
654  C CD1 . TRP A 84  ? 2.289 2.732 2.168 0.618  0.136  0.583  83  TRP HHH CD1 
655  C CD2 . TRP A 84  ? 2.328 2.651 2.147 0.609  0.167  0.611  83  TRP HHH CD2 
656  N NE1 . TRP A 84  ? 2.249 2.663 2.135 0.581  0.151  0.572  83  TRP HHH NE1 
657  C CE2 . TRP A 84  ? 2.225 2.571 2.077 0.576  0.168  0.588  83  TRP HHH CE2 
658  C CE3 . TRP A 84  ? 2.435 2.687 2.217 0.607  0.187  0.628  83  TRP HHH CE3 
659  C CZ2 . TRP A 84  ? 2.247 2.550 2.093 0.545  0.184  0.583  83  TRP HHH CZ2 
660  C CZ3 . TRP A 84  ? 2.307 2.522 2.089 0.575  0.203  0.619  83  TRP HHH CZ3 
661  C CH2 . TRP A 84  ? 2.218 2.459 2.030 0.546  0.200  0.598  83  TRP HHH CH2 
662  N N   . SER A 85  ? 2.400 2.881 2.167 0.761  0.084  0.652  84  SER HHH N   
663  C CA  . SER A 85  ? 2.465 2.970 2.211 0.817  0.067  0.672  84  SER HHH CA  
664  C C   . SER A 85  ? 2.367 2.883 2.151 0.842  0.073  0.672  84  SER HHH C   
665  O O   . SER A 85  ? 2.363 2.862 2.123 0.888  0.073  0.696  84  SER HHH O   
666  C CB  . SER A 85  ? 2.558 3.150 2.312 0.827  0.034  0.655  84  SER HHH CB  
667  O OG  . SER A 85  ? 2.661 3.311 2.469 0.786  0.027  0.617  84  SER HHH OG  
668  N N   . SER A 86  ? 2.407 2.951 2.248 0.812  0.079  0.645  85  SER HHH N   
669  C CA  . SER A 86  ? 2.499 3.056 2.383 0.830  0.086  0.640  85  SER HHH CA  
670  C C   . SER A 86  ? 2.421 2.967 2.345 0.783  0.105  0.616  85  SER HHH C   
671  O O   . SER A 86  ? 2.364 2.970 2.328 0.756  0.095  0.586  85  SER HHH O   
672  C CB  . SER A 86  ? 2.533 3.184 2.451 0.864  0.057  0.625  85  SER HHH CB  
673  O OG  . SER A 86  ? 2.778 3.423 2.710 0.905  0.063  0.638  85  SER HHH OG  
674  N N   . LEU A 87  ? 2.379 2.850 2.289 0.773  0.134  0.630  86  LEU HHH N   
675  C CA  . LEU A 87  ? 2.374 2.823 2.312 0.731  0.155  0.612  86  LEU HHH CA  
676  C C   . LEU A 87  ? 2.342 2.848 2.339 0.735  0.153  0.589  86  LEU HHH C   
677  O O   . LEU A 87  ? 2.497 3.009 2.505 0.772  0.154  0.598  86  LEU HHH O   
678  C CB  . LEU A 87  ? 2.493 2.857 2.405 0.731  0.185  0.631  86  LEU HHH CB  
679  C CG  . LEU A 87  ? 2.580 2.880 2.441 0.712  0.196  0.645  86  LEU HHH CG  
680  C CD1 . LEU A 87  ? 2.569 2.792 2.411 0.712  0.228  0.658  86  LEU HHH CD1 
681  C CD2 . LEU A 87  ? 2.605 2.916 2.473 0.666  0.193  0.624  86  LEU HHH CD2 
682  N N   . LYS A 88  ? 2.317 2.858 2.349 0.697  0.153  0.560  87  LYS HHH N   
683  C CA  . LYS A 88  ? 2.422 3.009 2.511 0.689  0.158  0.534  87  LYS HHH CA  
684  C C   . LYS A 88  ? 2.471 2.998 2.560 0.664  0.188  0.534  87  LYS HHH C   
685  O O   . LYS A 88  ? 2.559 3.024 2.609 0.645  0.200  0.547  87  LYS HHH O   
686  C CB  . LYS A 88  ? 2.394 3.047 2.516 0.661  0.145  0.502  87  LYS HHH CB  
687  C CG  . LYS A 88  ? 2.413 3.154 2.565 0.689  0.118  0.488  87  LYS HHH CG  
688  C CD  . LYS A 88  ? 2.315 3.123 2.502 0.660  0.108  0.453  87  LYS HHH CD  
689  C CE  . LYS A 88  ? 2.197 2.991 2.347 0.638  0.099  0.456  87  LYS HHH CE  
690  N NZ  . LYS A 88  ? 2.166 2.943 2.267 0.671  0.082  0.486  87  LYS HHH NZ  
691  N N   . ALA A 89  ? 2.474 3.022 2.605 0.664  0.199  0.518  88  ALA HHH N   
692  C CA  . ALA A 89  ? 2.479 2.982 2.615 0.636  0.227  0.511  88  ALA HHH CA  
693  C C   . ALA A 89  ? 2.372 2.865 2.497 0.591  0.232  0.498  88  ALA HHH C   
694  O O   . ALA A 89  ? 2.175 2.612 2.277 0.569  0.250  0.503  88  ALA HHH O   
695  C CB  . ALA A 89  ? 2.558 3.097 2.745 0.644  0.237  0.493  88  ALA HHH CB  
696  N N   . SER A 90  ? 2.279 2.825 2.420 0.581  0.215  0.482  89  SER HHH N   
697  C CA  . SER A 90  ? 2.219 2.759 2.349 0.543  0.216  0.471  89  SER HHH CA  
698  C C   . SER A 90  ? 2.269 2.741 2.347 0.531  0.222  0.491  89  SER HHH C   
699  O O   . SER A 90  ? 2.377 2.823 2.445 0.500  0.234  0.484  89  SER HHH O   
700  C CB  . SER A 90  ? 2.101 2.700 2.244 0.542  0.195  0.458  89  SER HHH CB  
701  O OG  . SER A 90  ? 2.143 2.813 2.337 0.555  0.187  0.435  89  SER HHH OG  
702  N N   . ASP A 91  ? 2.431 2.877 2.479 0.556  0.215  0.515  90  ASP HHH N   
703  C CA  . ASP A 91  ? 2.556 2.955 2.557 0.549  0.213  0.531  90  ASP HHH CA  
704  C C   . ASP A 91  ? 2.531 2.864 2.509 0.539  0.235  0.541  90  ASP HHH C   
705  O O   . ASP A 91  ? 2.478 2.772 2.420 0.531  0.236  0.551  90  ASP HHH O   
706  C CB  . ASP A 91  ? 2.612 3.019 2.591 0.579  0.196  0.549  90  ASP HHH CB  
707  C CG  . ASP A 91  ? 2.580 3.052 2.574 0.582  0.172  0.537  90  ASP HHH CG  
708  O OD1 . ASP A 91  ? 2.637 3.130 2.645 0.552  0.170  0.518  90  ASP HHH OD1 
709  O OD2 . ASP A 91  ? 2.491 2.992 2.480 0.615  0.155  0.547  90  ASP HHH OD2 
710  N N   . THR A 92  ? 2.566 2.889 2.563 0.538  0.253  0.535  91  THR HHH N   
711  C CA  . THR A 92  ? 2.648 2.913 2.625 0.527  0.275  0.540  91  THR HHH CA  
712  C C   . THR A 92  ? 2.473 2.722 2.436 0.493  0.279  0.529  91  THR HHH C   
713  O O   . THR A 92  ? 2.322 2.593 2.303 0.475  0.281  0.513  91  THR HHH O   
714  C CB  . THR A 92  ? 2.797 3.059 2.799 0.538  0.292  0.535  91  THR HHH CB  
715  O OG1 . THR A 92  ? 2.920 3.192 2.939 0.512  0.302  0.516  91  THR HHH OG1 
716  C CG2 . THR A 92  ? 2.795 3.097 2.827 0.571  0.284  0.538  91  THR HHH CG2 
717  N N   . ALA A 93  ? 2.308 2.517 2.237 0.484  0.281  0.537  92  ALA HHH N   
718  C CA  . ALA A 93  ? 2.196 2.391 2.107 0.457  0.281  0.529  92  ALA HHH CA  
719  C C   . ALA A 93  ? 2.213 2.366 2.091 0.454  0.285  0.537  92  ALA HHH C   
720  O O   . ALA A 93  ? 2.307 2.441 2.178 0.472  0.290  0.549  92  ALA HHH O   
721  C CB  . ALA A 93  ? 2.052 2.281 1.969 0.447  0.264  0.523  92  ALA HHH CB  
722  N N   . ILE A 94  ? 2.150 2.289 2.012 0.433  0.285  0.530  93  ILE HHH N   
723  C CA  . ILE A 94  ? 2.132 2.241 1.967 0.426  0.285  0.533  93  ILE HHH CA  
724  C C   . ILE A 94  ? 2.212 2.338 2.040 0.422  0.267  0.535  93  ILE HHH C   
725  O O   . ILE A 94  ? 2.001 2.153 1.839 0.413  0.258  0.529  93  ILE HHH O   
726  C CB  . ILE A 94  ? 2.179 2.266 2.001 0.409  0.295  0.521  93  ILE HHH CB  
727  C CG1 . ILE A 94  ? 2.348 2.406 2.151 0.405  0.300  0.520  93  ILE HHH CG1 
728  C CG2 . ILE A 94  ? 2.206 2.308 2.025 0.393  0.286  0.513  93  ILE HHH CG2 
729  C CD1 . ILE A 94  ? 2.485 2.525 2.279 0.393  0.313  0.505  93  ILE HHH CD1 
730  N N   . TYR A 95  ? 2.293 2.403 2.104 0.429  0.265  0.544  94  TYR HHH N   
731  C CA  . TYR A 95  ? 2.062 2.185 1.862 0.425  0.250  0.546  94  TYR HHH CA  
732  C C   . TYR A 95  ? 1.973 2.067 1.753 0.411  0.254  0.541  94  TYR HHH C   
733  O O   . TYR A 95  ? 1.825 1.887 1.592 0.414  0.269  0.544  94  TYR HHH O   
734  C CB  . TYR A 95  ? 1.919 2.053 1.716 0.447  0.243  0.560  94  TYR HHH CB  
735  C CG  . TYR A 95  ? 1.916 2.092 1.738 0.461  0.233  0.561  94  TYR HHH CG  
736  C CD1 . TYR A 95  ? 2.123 2.298 1.960 0.477  0.243  0.564  94  TYR HHH CD1 
737  C CD2 . TYR A 95  ? 1.862 2.081 1.697 0.457  0.216  0.554  94  TYR HHH CD2 
738  C CE1 . TYR A 95  ? 2.157 2.376 2.022 0.490  0.234  0.561  94  TYR HHH CE1 
739  C CE2 . TYR A 95  ? 1.945 2.209 1.808 0.469  0.208  0.549  94  TYR HHH CE2 
740  C CZ  . TYR A 95  ? 2.056 2.322 1.935 0.486  0.217  0.553  94  TYR HHH CZ  
741  O OH  . TYR A 95  ? 1.971 2.285 1.882 0.498  0.209  0.545  94  TYR HHH OH  
742  N N   . TYR A 96  ? 2.011 2.116 1.790 0.395  0.244  0.533  95  TYR HHH N   
743  C CA  . TYR A 96  ? 2.094 2.182 1.859 0.382  0.245  0.525  95  TYR HHH CA  
744  C C   . TYR A 96  ? 2.112 2.208 1.868 0.382  0.234  0.529  95  TYR HHH C   
745  O O   . TYR A 96  ? 2.196 2.321 1.962 0.384  0.222  0.532  95  TYR HHH O   
746  C CB  . TYR A 96  ? 2.043 2.136 1.809 0.368  0.241  0.513  95  TYR HHH CB  
747  C CG  . TYR A 96  ? 2.023 2.105 1.790 0.367  0.252  0.507  95  TYR HHH CG  
748  C CD1 . TYR A 96  ? 1.991 2.051 1.751 0.366  0.264  0.500  95  TYR HHH CD1 
749  C CD2 . TYR A 96  ? 1.973 2.066 1.749 0.366  0.253  0.505  95  TYR HHH CD2 
750  C CE1 . TYR A 96  ? 2.017 2.070 1.777 0.364  0.274  0.491  95  TYR HHH CE1 
751  C CE2 . TYR A 96  ? 2.062 2.146 1.835 0.365  0.264  0.499  95  TYR HHH CE2 
752  C CZ  . TYR A 96  ? 2.116 2.181 1.881 0.364  0.273  0.492  95  TYR HHH CZ  
753  O OH  . TYR A 96  ? 2.333 2.390 2.095 0.362  0.284  0.483  95  TYR HHH OH  
754  N N   . CYS A 97  ? 2.009 2.082 1.749 0.379  0.240  0.529  96  CYS HHH N   
755  C CA  . CYS A 97  ? 2.059 2.136 1.789 0.371  0.232  0.527  96  CYS HHH CA  
756  C C   . CYS A 97  ? 2.171 2.245 1.903 0.354  0.230  0.511  96  CYS HHH C   
757  O O   . CYS A 97  ? 1.886 1.946 1.619 0.350  0.239  0.501  96  CYS HHH O   
758  C CB  . CYS A 97  ? 2.086 2.138 1.795 0.378  0.242  0.536  96  CYS HHH CB  
759  S SG  . CYS A 97  ? 2.259 2.273 1.959 0.365  0.262  0.522  96  CYS HHH SG  
760  N N   . ALA A 98  ? 2.284 2.376 2.019 0.346  0.217  0.507  97  ALA HHH N   
761  C CA  . ALA A 98  ? 2.234 2.327 1.972 0.334  0.213  0.494  97  ALA HHH CA  
762  C C   . ALA A 98  ? 2.173 2.271 1.908 0.326  0.207  0.489  97  ALA HHH C   
763  O O   . ALA A 98  ? 2.009 2.123 1.745 0.327  0.200  0.496  97  ALA HHH O   
764  C CB  . ALA A 98  ? 2.209 2.318 1.959 0.333  0.207  0.493  97  ALA HHH CB  
765  N N   . GLY A 99  ? 2.139 2.226 1.872 0.317  0.209  0.476  98  GLY HHH N   
766  C CA  . GLY A 99  ? 2.101 2.189 1.831 0.308  0.206  0.469  98  GLY HHH CA  
767  C C   . GLY A 99  ? 2.027 2.125 1.767 0.301  0.198  0.458  98  GLY HHH C   
768  O O   . GLY A 99  ? 2.382 2.478 2.126 0.303  0.197  0.450  98  GLY HHH O   
769  N N   . GLY A 100 ? 2.024 2.133 1.767 0.294  0.192  0.456  99  GLY HHH N   
770  C CA  . GLY A 100 ? 2.151 2.263 1.902 0.287  0.187  0.444  99  GLY HHH CA  
771  C C   . GLY A 100 ? 2.106 2.221 1.856 0.277  0.188  0.437  99  GLY HHH C   
772  O O   . GLY A 100 ? 2.029 2.153 1.772 0.276  0.187  0.446  99  GLY HHH O   
773  N N   . SER A 101 ? 2.165 2.276 1.920 0.270  0.189  0.422  100 SER HHH N   
774  C CA  . SER A 101 ? 2.096 2.207 1.849 0.259  0.193  0.414  100 SER HHH CA  
775  C C   . SER A 101 ? 1.929 2.054 1.689 0.253  0.186  0.413  100 SER HHH C   
776  O O   . SER A 101 ? 2.105 2.232 1.877 0.247  0.185  0.400  100 SER HHH O   
777  C CB  . SER A 101 ? 2.212 2.316 1.972 0.252  0.200  0.394  100 SER HHH CB  
778  O OG  . SER A 101 ? 2.421 2.533 2.197 0.257  0.192  0.382  100 SER HHH OG  
779  N N   . GLY A 102 ? 1.801 1.937 1.557 0.256  0.183  0.425  101 GLY HHH N   
780  C CA  . GLY A 102 ? 1.853 2.006 1.618 0.248  0.179  0.422  101 GLY HHH CA  
781  C C   . GLY A 102 ? 1.843 2.012 1.610 0.253  0.175  0.432  101 GLY HHH C   
782  O O   . GLY A 102 ? 2.019 2.185 1.780 0.263  0.175  0.443  101 GLY HHH O   
783  N N   . ILE A 103 ? 1.848 2.037 1.627 0.244  0.174  0.426  102 ILE HHH N   
784  C CA  . ILE A 103 ? 2.023 2.230 1.812 0.245  0.173  0.429  102 ILE HHH CA  
785  C C   . ILE A 103 ? 2.062 2.257 1.865 0.240  0.179  0.423  102 ILE HHH C   
786  O O   . ILE A 103 ? 2.062 2.243 1.867 0.236  0.181  0.415  102 ILE HHH O   
787  C CB  . ILE A 103 ? 2.149 2.390 1.941 0.237  0.169  0.422  102 ILE HHH CB  
788  C CG1 . ILE A 103 ? 2.220 2.488 2.028 0.237  0.169  0.421  102 ILE HHH CG1 
789  C CG2 . ILE A 103 ? 2.310 2.554 2.109 0.221  0.173  0.407  102 ILE HHH CG2 
790  C CD1 . ILE A 103 ? 2.324 2.594 2.127 0.253  0.165  0.435  102 ILE HHH CD1 
791  N N   . SER A 104 ? 2.109 2.305 1.920 0.242  0.184  0.426  103 SER HHH N   
792  C CA  . SER A 104 ? 2.262 2.435 2.078 0.242  0.193  0.425  103 SER HHH CA  
793  C C   . SER A 104 ? 2.261 2.408 2.064 0.253  0.190  0.429  103 SER HHH C   
794  O O   . SER A 104 ? 2.230 2.361 2.035 0.253  0.192  0.423  103 SER HHH O   
795  C CB  . SER A 104 ? 2.314 2.490 2.144 0.228  0.201  0.412  103 SER HHH CB  
796  O OG  . SER A 104 ? 2.336 2.535 2.181 0.217  0.207  0.404  103 SER HHH OG  
797  N N   . THR A 105 ? 2.139 2.283 1.932 0.264  0.185  0.437  104 THR HHH N   
798  C CA  . THR A 105 ? 2.114 2.240 1.897 0.274  0.181  0.437  104 THR HHH CA  
799  C C   . THR A 105 ? 2.176 2.296 1.951 0.285  0.182  0.447  104 THR HHH C   
800  O O   . THR A 105 ? 2.316 2.445 2.091 0.285  0.184  0.454  104 THR HHH O   
801  C CB  . THR A 105 ? 1.970 2.102 1.751 0.270  0.177  0.431  104 THR HHH CB  
802  O OG1 . THR A 105 ? 1.839 1.961 1.616 0.278  0.175  0.425  104 THR HHH OG1 
803  C CG2 . THR A 105 ? 1.997 2.139 1.772 0.270  0.177  0.438  104 THR HHH CG2 
804  N N   . PRO A 106 ? 2.109 2.213 1.874 0.296  0.181  0.448  105 PRO HHH N   
805  C CA  . PRO A 106 ? 1.958 2.056 1.713 0.306  0.182  0.455  105 PRO HHH CA  
806  C C   . PRO A 106 ? 1.829 1.935 1.583 0.306  0.180  0.454  105 PRO HHH C   
807  O O   . PRO A 106 ? 2.010 2.119 1.767 0.301  0.178  0.445  105 PRO HHH O   
808  C CB  . PRO A 106 ? 2.135 2.220 1.879 0.318  0.178  0.451  105 PRO HHH CB  
809  C CG  . PRO A 106 ? 2.092 2.170 1.840 0.316  0.178  0.447  105 PRO HHH CG  
810  C CD  . PRO A 106 ? 2.111 2.204 1.875 0.300  0.178  0.440  105 PRO HHH CD  
811  N N   . MET A 107 ? 1.752 1.858 1.503 0.310  0.184  0.461  106 MET HHH N   
812  C CA  . MET A 107 ? 1.800 1.908 1.550 0.311  0.186  0.462  106 MET HHH CA  
813  C C   . MET A 107 ? 1.776 1.875 1.519 0.316  0.187  0.454  106 MET HHH C   
814  O O   . MET A 107 ? 1.758 1.854 1.495 0.323  0.189  0.457  106 MET HHH O   
815  C CB  . MET A 107 ? 1.837 1.950 1.588 0.314  0.191  0.473  106 MET HHH CB  
816  C CG  . MET A 107 ? 1.909 2.029 1.667 0.314  0.192  0.478  106 MET HHH CG  
817  S SD  . MET A 107 ? 2.060 2.199 1.829 0.317  0.195  0.486  106 MET HHH SD  
818  C CE  . MET A 107 ? 2.123 2.284 1.899 0.310  0.188  0.484  106 MET HHH CE  
819  N N   . ASP A 108 ? 1.818 1.918 1.564 0.313  0.185  0.440  107 ASP HHH N   
820  C CA  . ASP A 108 ? 1.917 2.018 1.661 0.317  0.184  0.425  107 ASP HHH CA  
821  C C   . ASP A 108 ? 1.863 1.960 1.608 0.314  0.194  0.419  107 ASP HHH C   
822  O O   . ASP A 108 ? 1.915 2.016 1.662 0.316  0.195  0.403  107 ASP HHH O   
823  C CB  . ASP A 108 ? 2.104 2.212 1.856 0.314  0.178  0.409  107 ASP HHH CB  
824  C CG  . ASP A 108 ? 2.392 2.499 2.152 0.302  0.183  0.404  107 ASP HHH CG  
825  O OD1 . ASP A 108 ? 2.645 2.751 2.410 0.296  0.191  0.389  107 ASP HHH OD1 
826  O OD2 . ASP A 108 ? 2.566 2.672 2.326 0.297  0.182  0.413  107 ASP HHH OD2 
827  N N   . VAL A 109 ? 1.791 1.879 1.535 0.311  0.203  0.430  108 VAL HHH N   
828  C CA  . VAL A 109 ? 1.796 1.872 1.538 0.309  0.217  0.426  108 VAL HHH CA  
829  C C   . VAL A 109 ? 1.855 1.925 1.593 0.317  0.222  0.445  108 VAL HHH C   
830  O O   . VAL A 109 ? 1.917 1.993 1.654 0.319  0.217  0.459  108 VAL HHH O   
831  C CB  . VAL A 109 ? 1.840 1.905 1.581 0.301  0.227  0.422  108 VAL HHH CB  
832  C CG1 . VAL A 109 ? 1.939 1.987 1.680 0.297  0.246  0.411  108 VAL HHH CG1 
833  C CG2 . VAL A 109 ? 1.793 1.867 1.541 0.293  0.220  0.408  108 VAL HHH CG2 
834  N N   . TRP A 110 ? 1.859 1.923 1.597 0.320  0.231  0.443  109 TRP HHH N   
835  C CA  . TRP A 110 ? 1.764 1.823 1.501 0.329  0.237  0.458  109 TRP HHH CA  
836  C C   . TRP A 110 ? 1.768 1.807 1.504 0.329  0.256  0.454  109 TRP HHH C   
837  O O   . TRP A 110 ? 1.751 1.788 1.489 0.323  0.263  0.436  109 TRP HHH O   
838  C CB  . TRP A 110 ? 1.754 1.821 1.491 0.333  0.233  0.458  109 TRP HHH CB  
839  C CG  . TRP A 110 ? 1.793 1.871 1.528 0.333  0.220  0.464  109 TRP HHH CG  
840  C CD1 . TRP A 110 ? 1.842 1.926 1.575 0.330  0.210  0.456  109 TRP HHH CD1 
841  C CD2 . TRP A 110 ? 1.731 1.817 1.471 0.336  0.218  0.477  109 TRP HHH CD2 
842  N NE1 . TRP A 110 ? 1.863 1.952 1.596 0.331  0.204  0.465  109 TRP HHH NE1 
843  C CE2 . TRP A 110 ? 1.875 1.967 1.613 0.333  0.209  0.476  109 TRP HHH CE2 
844  C CE3 . TRP A 110 ? 1.669 1.759 1.416 0.341  0.223  0.487  109 TRP HHH CE3 
845  C CZ2 . TRP A 110 ? 1.838 1.937 1.582 0.332  0.208  0.484  109 TRP HHH CZ2 
846  C CZ3 . TRP A 110 ? 1.707 1.811 1.462 0.341  0.219  0.493  109 TRP HHH CZ3 
847  C CH2 . TRP A 110 ? 1.666 1.773 1.419 0.335  0.213  0.491  109 TRP HHH CH2 
848  N N   . GLY A 111 ? 1.858 1.884 1.590 0.336  0.264  0.470  110 GLY HHH N   
849  C CA  . GLY A 111 ? 1.945 1.947 1.675 0.339  0.286  0.470  110 GLY HHH CA  
850  C C   . GLY A 111 ? 1.890 1.895 1.627 0.343  0.291  0.467  110 GLY HHH C   
851  O O   . GLY A 111 ? 1.811 1.835 1.552 0.346  0.278  0.470  110 GLY HHH O   
852  N N   . GLN A 112 ? 1.858 1.841 1.596 0.343  0.312  0.462  111 GLN HHH N   
853  C CA  . GLN A 112 ? 1.843 1.823 1.588 0.347  0.323  0.458  111 GLN HHH CA  
854  C C   . GLN A 112 ? 1.864 1.853 1.614 0.361  0.316  0.479  111 GLN HHH C   
855  O O   . GLN A 112 ? 2.002 1.997 1.759 0.363  0.320  0.476  111 GLN HHH O   
856  C CB  . GLN A 112 ? 1.940 1.890 1.686 0.342  0.351  0.447  111 GLN HHH CB  
857  C CG  . GLN A 112 ? 2.350 2.268 2.088 0.355  0.367  0.468  111 GLN HHH CG  
858  C CD  . GLN A 112 ? 2.642 2.534 2.366 0.351  0.379  0.470  111 GLN HHH CD  
859  O OE1 . GLN A 112 ? 2.794 2.696 2.509 0.352  0.363  0.478  111 GLN HHH OE1 
860  N NE2 . GLN A 112 ? 2.717 2.571 2.437 0.347  0.410  0.462  111 GLN HHH NE2 
861  N N   . GLY A 113 ? 1.973 1.966 1.719 0.372  0.307  0.498  112 GLY HHH N   
862  C CA  . GLY A 113 ? 2.061 2.067 1.816 0.387  0.301  0.514  112 GLY HHH CA  
863  C C   . GLY A 113 ? 2.100 2.083 1.855 0.403  0.319  0.526  112 GLY HHH C   
864  O O   . GLY A 113 ? 2.168 2.123 1.920 0.399  0.340  0.517  112 GLY HHH O   
865  N N   . THR A 114 ? 2.106 2.102 1.866 0.422  0.312  0.543  113 THR HHH N   
866  C CA  . THR A 114 ? 2.274 2.250 2.034 0.443  0.327  0.556  113 THR HHH CA  
867  C C   . THR A 114 ? 2.218 2.225 2.001 0.454  0.319  0.558  113 THR HHH C   
868  O O   . THR A 114 ? 2.126 2.169 1.918 0.456  0.299  0.560  113 THR HHH O   
869  C CB  . THR A 114 ? 2.333 2.297 2.074 0.462  0.325  0.575  113 THR HHH CB  
870  O OG1 . THR A 114 ? 2.409 2.412 2.160 0.478  0.304  0.586  113 THR HHH OG1 
871  C CG2 . THR A 114 ? 2.286 2.239 2.006 0.448  0.322  0.572  113 THR HHH CG2 
872  N N   . THR A 115 ? 2.225 2.218 2.020 0.458  0.337  0.555  114 THR HHH N   
873  C CA  . THR A 115 ? 2.378 2.399 2.198 0.468  0.333  0.555  114 THR HHH CA  
874  C C   . THR A 115 ? 2.332 2.353 2.157 0.499  0.335  0.574  114 THR HHH C   
875  O O   . THR A 115 ? 2.388 2.368 2.201 0.510  0.355  0.581  114 THR HHH O   
876  C CB  . THR A 115 ? 2.558 2.568 2.389 0.457  0.351  0.541  114 THR HHH CB  
877  O OG1 . THR A 115 ? 2.661 2.660 2.477 0.433  0.353  0.526  114 THR HHH OG1 
878  C CG2 . THR A 115 ? 2.545 2.588 2.399 0.456  0.346  0.535  114 THR HHH CG2 
879  N N   . VAL A 116 ? 2.312 2.376 2.152 0.513  0.315  0.579  115 VAL HHH N   
880  C CA  . VAL A 116 ? 2.464 2.539 2.311 0.547  0.311  0.594  115 VAL HHH CA  
881  C C   . VAL A 116 ? 2.395 2.505 2.280 0.553  0.311  0.585  115 VAL HHH C   
882  O O   . VAL A 116 ? 2.414 2.557 2.317 0.535  0.301  0.570  115 VAL HHH O   
883  C CB  . VAL A 116 ? 2.613 2.718 2.449 0.559  0.287  0.604  115 VAL HHH CB  
884  C CG1 . VAL A 116 ? 2.679 2.761 2.485 0.542  0.285  0.606  115 VAL HHH CG1 
885  C CG2 . VAL A 116 ? 2.653 2.821 2.518 0.554  0.265  0.591  115 VAL HHH CG2 
886  N N   . THR A 117 ? 2.336 2.433 2.231 0.579  0.324  0.594  116 THR HHH N   
887  C CA  . THR A 117 ? 2.289 2.413 2.223 0.586  0.329  0.583  116 THR HHH CA  
888  C C   . THR A 117 ? 2.426 2.570 2.372 0.627  0.322  0.598  116 THR HHH C   
889  O O   . THR A 117 ? 2.545 2.648 2.469 0.651  0.333  0.617  116 THR HHH O   
890  C CB  . THR A 117 ? 2.222 2.306 2.158 0.571  0.358  0.574  116 THR HHH CB  
891  O OG1 . THR A 117 ? 2.296 2.331 2.218 0.591  0.379  0.588  116 THR HHH OG1 
892  C CG2 . THR A 117 ? 2.176 2.240 2.093 0.536  0.363  0.561  116 THR HHH CG2 
893  N N   . VAL A 118 ? 2.380 2.585 2.361 0.636  0.304  0.588  117 VAL HHH N   
894  C CA  . VAL A 118 ? 2.328 2.573 2.324 0.677  0.287  0.598  117 VAL HHH CA  
895  C C   . VAL A 118 ? 2.457 2.722 2.495 0.694  0.298  0.589  117 VAL HHH C   
896  O O   . VAL A 118 ? 2.533 2.862 2.611 0.692  0.284  0.570  117 VAL HHH O   
897  C CB  . VAL A 118 ? 2.204 2.515 2.211 0.673  0.257  0.588  117 VAL HHH CB  
898  C CG1 . VAL A 118 ? 2.231 2.590 2.251 0.717  0.236  0.596  117 VAL HHH CG1 
899  C CG2 . VAL A 118 ? 2.280 2.572 2.249 0.653  0.248  0.594  117 VAL HHH CG2 
900  N N   . ALA A 119 ? 2.538 2.753 2.571 0.709  0.323  0.600  118 ALA HHH N   
901  C CA  . ALA A 119 ? 2.608 2.834 2.679 0.728  0.336  0.593  118 ALA HHH CA  
902  C C   . ALA A 119 ? 2.572 2.726 2.625 0.742  0.368  0.608  118 ALA HHH C   
903  O O   . ALA A 119 ? 2.548 2.647 2.567 0.720  0.384  0.613  118 ALA HHH O   
904  C CB  . ALA A 119 ? 2.712 2.965 2.819 0.694  0.344  0.564  118 ALA HHH CB  
905  N N   . SER A 120 ? 2.537 2.693 2.616 0.775  0.378  0.612  119 SER HHH N   
906  C CA  . SER A 120 ? 2.570 2.657 2.637 0.793  0.412  0.626  119 SER HHH CA  
907  C C   . SER A 120 ? 2.491 2.541 2.564 0.752  0.442  0.607  119 SER HHH C   
908  O O   . SER A 120 ? 2.530 2.619 2.631 0.724  0.439  0.583  119 SER HHH O   
909  C CB  . SER A 120 ? 2.609 2.714 2.705 0.840  0.413  0.634  119 SER HHH CB  
910  O OG  . SER A 120 ? 2.649 2.784 2.732 0.882  0.384  0.654  119 SER HHH OG  
911  N N   . THR A 121 ? 2.504 2.482 2.549 0.748  0.473  0.616  120 THR HHH N   
912  C CA  . THR A 121 ? 2.539 2.481 2.584 0.709  0.502  0.596  120 THR HHH CA  
913  C C   . THR A 121 ? 2.659 2.588 2.737 0.719  0.530  0.586  120 THR HHH C   
914  O O   . THR A 121 ? 2.768 2.683 2.854 0.761  0.537  0.603  120 THR HHH O   
915  C CB  . THR A 121 ? 2.621 2.495 2.622 0.695  0.524  0.604  120 THR HHH CB  
916  O OG1 . THR A 121 ? 2.752 2.571 2.745 0.728  0.551  0.623  120 THR HHH OG1 
917  C CG2 . THR A 121 ? 2.670 2.550 2.637 0.691  0.499  0.616  120 THR HHH CG2 
918  N N   . LYS A 122 ? 2.720 2.653 2.814 0.683  0.545  0.560  121 LYS HHH N   
919  C CA  . LYS A 122 ? 2.715 2.633 2.840 0.683  0.576  0.545  121 LYS HHH CA  
920  C C   . LYS A 122 ? 2.658 2.543 2.769 0.640  0.602  0.523  121 LYS HHH C   
921  O O   . LYS A 122 ? 2.421 2.325 2.517 0.607  0.588  0.510  121 LYS HHH O   
922  C CB  . LYS A 122 ? 2.699 2.681 2.870 0.686  0.562  0.530  121 LYS HHH CB  
923  C CG  . LYS A 122 ? 2.805 2.776 3.012 0.691  0.593  0.515  121 LYS HHH CG  
924  C CD  . LYS A 122 ? 2.878 2.905 3.126 0.677  0.587  0.491  121 LYS HHH CD  
925  C CE  . LYS A 122 ? 2.974 2.983 3.250 0.670  0.623  0.472  121 LYS HHH CE  
926  N NZ  . LYS A 122 ? 3.073 3.038 3.320 0.630  0.648  0.457  121 LYS HHH NZ  
927  N N   . GLY A 123 ? 2.826 2.662 2.942 0.641  0.640  0.518  122 GLY HHH N   
928  C CA  . GLY A 123 ? 2.896 2.700 3.001 0.603  0.667  0.494  122 GLY HHH CA  
929  C C   . GLY A 123 ? 2.990 2.833 3.118 0.575  0.668  0.466  122 GLY HHH C   
930  O O   . GLY A 123 ? 2.960 2.837 3.122 0.591  0.662  0.464  122 GLY HHH O   
931  N N   . PRO A 124 ? 3.103 2.941 3.212 0.536  0.676  0.443  123 PRO HHH N   
932  C CA  . PRO A 124 ? 3.035 2.904 3.157 0.510  0.679  0.418  123 PRO HHH CA  
933  C C   . PRO A 124 ? 2.837 2.682 2.984 0.507  0.718  0.399  123 PRO HHH C   
934  O O   . PRO A 124 ? 2.889 2.689 3.032 0.509  0.746  0.398  123 PRO HHH O   
935  C CB  . PRO A 124 ? 3.054 2.923 3.139 0.474  0.671  0.404  123 PRO HHH CB  
936  C CG  . PRO A 124 ? 3.087 2.911 3.152 0.476  0.685  0.410  123 PRO HHH CG  
937  C CD  . PRO A 124 ? 3.117 2.925 3.191 0.515  0.681  0.440  123 PRO HHH CD  
938  N N   . SER A 125 ? 2.630 2.506 2.804 0.502  0.721  0.385  124 SER HHH N   
939  C CA  . SER A 125 ? 2.681 2.543 2.876 0.489  0.758  0.360  124 SER HHH CA  
940  C C   . SER A 125 ? 2.757 2.627 2.924 0.447  0.761  0.334  124 SER HHH C   
941  O O   . SER A 125 ? 2.829 2.733 2.979 0.434  0.735  0.334  124 SER HHH O   
942  C CB  . SER A 125 ? 2.656 2.549 2.895 0.506  0.760  0.357  124 SER HHH CB  
943  O OG  . SER A 125 ? 2.695 2.589 2.957 0.548  0.751  0.382  124 SER HHH OG  
944  N N   . VAL A 126 ? 2.860 2.699 3.021 0.428  0.793  0.313  125 VAL HHH N   
945  C CA  . VAL A 126 ? 2.865 2.713 2.995 0.391  0.797  0.285  125 VAL HHH CA  
946  C C   . VAL A 126 ? 2.801 2.653 2.950 0.376  0.826  0.258  125 VAL HHH C   
947  O O   . VAL A 126 ? 2.936 2.758 3.111 0.382  0.860  0.250  125 VAL HHH O   
948  C CB  . VAL A 126 ? 3.018 2.835 3.126 0.377  0.808  0.276  125 VAL HHH CB  
949  C CG1 . VAL A 126 ? 3.098 2.934 3.170 0.344  0.801  0.251  125 VAL HHH CG1 
950  C CG2 . VAL A 126 ? 3.043 2.845 3.138 0.397  0.788  0.304  125 VAL HHH CG2 
951  N N   . PHE A 127 ? 2.677 2.560 2.809 0.356  0.815  0.246  126 PHE HHH N   
952  C CA  . PHE A 127 ? 2.462 2.353 2.606 0.339  0.840  0.220  126 PHE HHH CA  
953  C C   . PHE A 127 ? 2.419 2.321 2.518 0.306  0.838  0.197  126 PHE HHH C   
954  O O   . PHE A 127 ? 2.247 2.166 2.309 0.299  0.809  0.205  126 PHE HHH O   
955  C CB  . PHE A 127 ? 2.359 2.279 2.527 0.350  0.830  0.229  126 PHE HHH CB  
956  C CG  . PHE A 127 ? 2.285 2.208 2.497 0.386  0.823  0.252  126 PHE HHH CG  
957  C CD1 . PHE A 127 ? 2.276 2.175 2.527 0.406  0.851  0.251  126 PHE HHH CD1 
958  C CD2 . PHE A 127 ? 2.238 2.189 2.451 0.401  0.790  0.274  126 PHE HHH CD2 
959  C CE1 . PHE A 127 ? 2.287 2.191 2.574 0.443  0.842  0.273  126 PHE HHH CE1 
960  C CE2 . PHE A 127 ? 2.259 2.219 2.511 0.436  0.782  0.293  126 PHE HHH CE2 
961  C CZ  . PHE A 127 ? 2.261 2.198 2.549 0.458  0.807  0.293  126 PHE HHH CZ  
962  N N   . PRO A 128 ? 2.479 2.371 2.578 0.287  0.870  0.166  127 PRO HHH N   
963  C CA  . PRO A 128 ? 2.539 2.444 2.593 0.258  0.869  0.141  127 PRO HHH CA  
964  C C   . PRO A 128 ? 2.490 2.419 2.521 0.246  0.862  0.136  127 PRO HHH C   
965  O O   . PRO A 128 ? 2.467 2.399 2.528 0.251  0.877  0.137  127 PRO HHH O   
966  C CB  . PRO A 128 ? 2.599 2.485 2.670 0.243  0.909  0.109  127 PRO HHH CB  
967  C CG  . PRO A 128 ? 2.588 2.458 2.712 0.260  0.935  0.114  127 PRO HHH CG  
968  C CD  . PRO A 128 ? 2.548 2.417 2.690 0.292  0.909  0.153  127 PRO HHH CD  
969  N N   . LEU A 129 ? 2.474 2.420 2.452 0.231  0.841  0.132  128 LEU HHH N   
970  C CA  . LEU A 129 ? 2.425 2.387 2.366 0.216  0.840  0.124  128 LEU HHH CA  
971  C C   . LEU A 129 ? 2.428 2.395 2.335 0.193  0.856  0.089  128 LEU HHH C   
972  O O   . LEU A 129 ? 2.331 2.310 2.198 0.188  0.835  0.085  128 LEU HHH O   
973  C CB  . LEU A 129 ? 2.454 2.428 2.356 0.222  0.803  0.149  128 LEU HHH CB  
974  C CG  . LEU A 129 ? 2.403 2.377 2.337 0.244  0.785  0.180  128 LEU HHH CG  
975  C CD1 . LEU A 129 ? 2.322 2.305 2.218 0.248  0.750  0.201  128 LEU HHH CD1 
976  C CD2 . LEU A 129 ? 2.393 2.369 2.369 0.250  0.803  0.182  128 LEU HHH CD2 
977  N N   . ALA A 130 ? 2.496 2.457 2.425 0.182  0.891  0.064  129 ALA HHH N   
978  C CA  . ALA A 130 ? 2.516 2.485 2.419 0.158  0.911  0.026  129 ALA HHH CA  
979  C C   . ALA A 130 ? 2.614 2.601 2.454 0.146  0.899  0.021  129 ALA HHH C   
980  O O   . ALA A 130 ? 2.526 2.511 2.356 0.151  0.894  0.040  129 ALA HHH O   
981  C CB  . ALA A 130 ? 2.521 2.476 2.470 0.150  0.954  0.002  129 ALA HHH CB  
982  N N   . PRO A 131 ? 2.743 2.748 2.538 0.131  0.895  -0.005 130 PRO HHH N   
983  C CA  . PRO A 131 ? 2.794 2.814 2.521 0.122  0.886  -0.010 130 PRO HHH CA  
984  C C   . PRO A 131 ? 2.836 2.853 2.558 0.105  0.921  -0.033 130 PRO HHH C   
985  O O   . PRO A 131 ? 2.660 2.665 2.438 0.100  0.953  -0.047 130 PRO HHH O   
986  C CB  . PRO A 131 ? 2.859 2.904 2.547 0.115  0.869  -0.034 130 PRO HHH CB  
987  C CG  . PRO A 131 ? 2.852 2.895 2.597 0.107  0.894  -0.060 130 PRO HHH CG  
988  C CD  . PRO A 131 ? 2.760 2.773 2.566 0.123  0.900  -0.032 130 PRO HHH CD  
989  N N   . SER A 132 ? 3.017 3.042 2.672 0.099  0.914  -0.034 131 SER HHH N   
990  C CA  . SER A 132 ? 3.126 3.153 2.747 0.080  0.942  -0.061 131 SER HHH CA  
991  C C   . SER A 132 ? 3.188 3.236 2.721 0.078  0.919  -0.069 131 SER HHH C   
992  O O   . SER A 132 ? 3.171 3.228 2.677 0.093  0.883  -0.050 131 SER HHH O   
993  C CB  A SER A 132 ? 3.129 3.134 2.761 0.079  0.962  -0.046 131 SER HHH CB  
994  C CB  B SER A 132 ? 3.145 3.151 2.775 0.079  0.962  -0.046 131 SER HHH CB  
995  O OG  A SER A 132 ? 3.099 3.094 2.694 0.092  0.937  -0.010 131 SER HHH OG  
996  O OG  B SER A 132 ? 3.124 3.119 2.836 0.080  0.988  -0.049 131 SER HHH OG  
997  N N   . SER A 133 ? 3.147 3.202 2.638 0.062  0.941  -0.096 132 SER HHH N   
998  C CA  . SER A 133 ? 3.069 3.151 2.478 0.059  0.925  -0.114 132 SER HHH CA  
999  C C   . SER A 133 ? 3.037 3.114 2.380 0.080  0.887  -0.077 132 SER HHH C   
1000 O O   . SER A 133 ? 3.049 3.104 2.341 0.081  0.895  -0.060 132 SER HHH O   
1001 C CB  . SER A 133 ? 3.061 3.141 2.438 0.039  0.959  -0.141 132 SER HHH CB  
1002 O OG  . SER A 133 ? 2.975 3.054 2.424 0.021  0.996  -0.171 132 SER HHH OG  
1003 N N   . GLY A 134 ? 3.780 3.960 2.973 0.066  0.865  -0.169 137 GLY HHH N   
1004 C CA  . GLY A 134 ? 3.758 3.926 2.864 0.089  0.836  -0.133 137 GLY HHH CA  
1005 C C   . GLY A 134 ? 3.751 3.961 2.823 0.108  0.792  -0.137 137 GLY HHH C   
1006 O O   . GLY A 134 ? 3.761 4.019 2.818 0.101  0.786  -0.180 137 GLY HHH O   
1007 N N   . GLY A 135 ? 3.642 3.835 2.704 0.131  0.761  -0.098 138 GLY HHH N   
1008 C CA  . GLY A 135 ? 3.547 3.779 2.582 0.152  0.717  -0.098 138 GLY HHH CA  
1009 C C   . GLY A 135 ? 3.420 3.670 2.541 0.147  0.708  -0.109 138 GLY HHH C   
1010 O O   . GLY A 135 ? 3.539 3.823 2.704 0.129  0.720  -0.153 138 GLY HHH O   
1011 N N   . THR A 136 ? 3.240 3.463 2.384 0.162  0.691  -0.069 139 THR HHH N   
1012 C CA  . THR A 136 ? 3.043 3.267 2.268 0.160  0.686  -0.068 139 THR HHH CA  
1013 C C   . THR A 136 ? 3.008 3.180 2.280 0.158  0.705  -0.032 139 THR HHH C   
1014 O O   . THR A 136 ? 3.198 3.340 2.429 0.171  0.699  0.004  139 THR HHH O   
1015 C CB  . THR A 136 ? 2.990 3.238 2.193 0.182  0.642  -0.056 139 THR HHH CB  
1016 O OG1 . THR A 136 ? 2.856 3.065 2.032 0.201  0.628  -0.006 139 THR HHH OG1 
1017 C CG2 . THR A 136 ? 3.091 3.390 2.228 0.192  0.618  -0.084 139 THR HHH CG2 
1018 N N   . ALA A 137 ? 2.894 3.056 2.247 0.145  0.727  -0.041 140 ALA HHH N   
1019 C CA  . ALA A 137 ? 2.764 2.885 2.168 0.144  0.748  -0.013 140 ALA HHH CA  
1020 C C   . ALA A 137 ? 2.581 2.692 2.037 0.156  0.731  0.012  140 ALA HHH C   
1021 O O   . ALA A 137 ? 2.443 2.577 1.911 0.159  0.712  -0.001 140 ALA HHH O   
1022 C CB  . ALA A 137 ? 2.751 2.865 2.203 0.124  0.790  -0.041 140 ALA HHH CB  
1023 N N   . ALA A 138 ? 2.477 2.556 1.960 0.162  0.737  0.044  141 ALA HHH N   
1024 C CA  . ALA A 138 ? 2.467 2.534 2.002 0.174  0.725  0.069  141 ALA HHH CA  
1025 C C   . ALA A 138 ? 2.567 2.618 2.176 0.166  0.755  0.061  141 ALA HHH C   
1026 O O   . ALA A 138 ? 2.582 2.626 2.202 0.155  0.786  0.046  141 ALA HHH O   
1027 C CB  . ALA A 138 ? 2.390 2.437 1.905 0.187  0.710  0.108  141 ALA HHH CB  
1028 N N   . LEU A 139 ? 2.818 2.864 2.474 0.175  0.747  0.071  142 LEU HHH N   
1029 C CA  . LEU A 139 ? 2.855 2.882 2.581 0.175  0.772  0.071  142 LEU HHH CA  
1030 C C   . LEU A 139 ? 2.740 2.758 2.493 0.192  0.750  0.099  142 LEU HHH C   
1031 O O   . LEU A 139 ? 2.626 2.657 2.346 0.199  0.719  0.110  142 LEU HHH O   
1032 C CB  . LEU A 139 ? 3.015 3.048 2.762 0.159  0.798  0.031  142 LEU HHH CB  
1033 C CG  . LEU A 139 ? 3.063 3.117 2.797 0.155  0.781  0.012  142 LEU HHH CG  
1034 C CD1 . LEU A 139 ? 2.975 3.013 2.755 0.164  0.780  0.025  142 LEU HHH CD1 
1035 C CD2 . LEU A 139 ? 3.120 3.194 2.851 0.134  0.805  -0.036 142 LEU HHH CD2 
1036 N N   . GLY A 140 ? 2.673 2.671 2.481 0.201  0.766  0.111  143 GLY HHH N   
1037 C CA  . GLY A 140 ? 2.681 2.670 2.512 0.219  0.745  0.141  143 GLY HHH CA  
1038 C C   . GLY A 140 ? 2.620 2.587 2.509 0.232  0.764  0.152  143 GLY HHH C   
1039 O O   . GLY A 140 ? 2.491 2.448 2.408 0.226  0.796  0.135  143 GLY HHH O   
1040 N N   . CYS A 141 ? 2.661 2.621 2.566 0.250  0.745  0.179  144 CYS HHH N   
1041 C CA  . CYS A 141 ? 2.662 2.602 2.615 0.269  0.755  0.198  144 CYS HHH CA  
1042 C C   . CYS A 141 ? 2.484 2.435 2.443 0.286  0.732  0.227  144 CYS HHH C   
1043 O O   . CYS A 141 ? 2.415 2.379 2.342 0.286  0.703  0.240  144 CYS HHH O   
1044 C CB  . CYS A 141 ? 2.972 2.895 2.933 0.277  0.751  0.204  144 CYS HHH CB  
1045 S SG  . CYS A 141 ? 3.427 3.321 3.413 0.266  0.794  0.174  144 CYS HHH SG  
1046 N N   . LEU A 142 ? 2.399 2.346 2.400 0.300  0.745  0.236  145 LEU HHH N   
1047 C CA  . LEU A 142 ? 2.417 2.378 2.435 0.319  0.724  0.262  145 LEU HHH CA  
1048 C C   . LEU A 142 ? 2.458 2.406 2.504 0.344  0.717  0.282  145 LEU HHH C   
1049 O O   . LEU A 142 ? 2.563 2.495 2.644 0.357  0.740  0.281  145 LEU HHH O   
1050 C CB  . LEU A 142 ? 2.365 2.338 2.414 0.320  0.742  0.255  145 LEU HHH CB  
1051 C CG  . LEU A 142 ? 2.292 2.286 2.366 0.338  0.723  0.275  145 LEU HHH CG  
1052 C CD1 . LEU A 142 ? 2.269 2.277 2.304 0.328  0.696  0.285  145 LEU HHH CD1 
1053 C CD2 . LEU A 142 ? 2.276 2.283 2.391 0.340  0.743  0.265  145 LEU HHH CD2 
1054 N N   . VAL A 143 ? 2.450 2.403 2.478 0.351  0.688  0.302  146 VAL HHH N   
1055 C CA  . VAL A 143 ? 2.426 2.368 2.473 0.377  0.679  0.325  146 VAL HHH CA  
1056 C C   . VAL A 143 ? 2.305 2.274 2.375 0.395  0.660  0.343  146 VAL HHH C   
1057 O O   . VAL A 143 ? 2.212 2.203 2.265 0.389  0.636  0.349  146 VAL HHH O   
1058 C CB  . VAL A 143 ? 2.522 2.453 2.537 0.372  0.661  0.331  146 VAL HHH CB  
1059 C CG1 . VAL A 143 ? 2.597 2.504 2.626 0.395  0.663  0.350  146 VAL HHH CG1 
1060 C CG2 . VAL A 143 ? 2.501 2.423 2.488 0.347  0.674  0.306  146 VAL HHH CG2 
1061 N N   . LYS A 144 ? 2.326 2.296 2.438 0.418  0.672  0.348  147 LYS HHH N   
1062 C CA  . LYS A 144 ? 2.419 2.424 2.562 0.432  0.659  0.355  147 LYS HHH CA  
1063 C C   . LYS A 144 ? 2.549 2.557 2.720 0.469  0.649  0.376  147 LYS HHH C   
1064 O O   . LYS A 144 ? 2.591 2.566 2.769 0.485  0.666  0.382  147 LYS HHH O   
1065 C CB  . LYS A 144 ? 2.503 2.519 2.675 0.424  0.685  0.334  147 LYS HHH CB  
1066 C CG  . LYS A 144 ? 2.556 2.612 2.765 0.435  0.676  0.334  147 LYS HHH CG  
1067 C CD  . LYS A 144 ? 2.526 2.592 2.765 0.426  0.703  0.311  147 LYS HHH CD  
1068 C CE  . LYS A 144 ? 2.516 2.621 2.810 0.449  0.699  0.311  147 LYS HHH CE  
1069 N NZ  . LYS A 144 ? 2.472 2.615 2.766 0.448  0.671  0.318  147 LYS HHH NZ  
1070 N N   . ASP A 145 ? 2.663 2.709 2.848 0.482  0.623  0.387  148 ASP HHH N   
1071 C CA  . ASP A 145 ? 2.749 2.811 2.963 0.520  0.608  0.406  148 ASP HHH CA  
1072 C C   . ASP A 145 ? 2.825 2.852 3.013 0.537  0.602  0.428  148 ASP HHH C   
1073 O O   . ASP A 145 ? 2.780 2.772 2.976 0.556  0.624  0.433  148 ASP HHH O   
1074 C CB  . ASP A 145 ? 2.703 2.772 2.965 0.541  0.629  0.399  148 ASP HHH CB  
1075 C CG  . ASP A 145 ? 2.719 2.832 3.014 0.529  0.631  0.378  148 ASP HHH CG  
1076 O OD1 . ASP A 145 ? 2.629 2.776 2.919 0.517  0.610  0.376  148 ASP HHH OD1 
1077 O OD2 . ASP A 145 ? 2.954 3.066 3.279 0.531  0.657  0.362  148 ASP HHH OD2 
1078 N N   . TYR A 146 ? 2.860 2.893 3.017 0.531  0.576  0.440  149 TYR HHH N   
1079 C CA  . TYR A 146 ? 2.905 2.907 3.034 0.544  0.569  0.460  149 TYR HHH CA  
1080 C C   . TYR A 146 ? 2.855 2.887 2.970 0.549  0.534  0.474  149 TYR HHH C   
1081 O O   . TYR A 146 ? 2.757 2.826 2.876 0.532  0.518  0.464  149 TYR HHH O   
1082 C CB  . TYR A 146 ? 2.932 2.892 3.028 0.517  0.586  0.451  149 TYR HHH CB  
1083 C CG  . TYR A 146 ? 2.818 2.791 2.885 0.484  0.573  0.439  149 TYR HHH CG  
1084 C CD1 . TYR A 146 ? 2.823 2.809 2.890 0.459  0.581  0.418  149 TYR HHH CD1 
1085 C CD2 . TYR A 146 ? 2.732 2.700 2.767 0.479  0.553  0.449  149 TYR HHH CD2 
1086 C CE1 . TYR A 146 ? 2.821 2.815 2.856 0.433  0.569  0.410  149 TYR HHH CE1 
1087 C CE2 . TYR A 146 ? 2.719 2.698 2.728 0.452  0.540  0.439  149 TYR HHH CE2 
1088 C CZ  . TYR A 146 ? 2.708 2.700 2.716 0.431  0.548  0.420  149 TYR HHH CZ  
1089 O OH  . TYR A 146 ? 2.608 2.608 2.585 0.408  0.536  0.413  149 TYR HHH OH  
1090 N N   . PHE A 147 ? 2.792 2.806 2.890 0.570  0.524  0.496  150 PHE HHH N   
1091 C CA  . PHE A 147 ? 2.662 2.700 2.743 0.576  0.492  0.510  150 PHE HHH CA  
1092 C C   . PHE A 147 ? 2.554 2.548 2.601 0.586  0.494  0.529  150 PHE HHH C   
1093 O O   . PHE A 147 ? 2.389 2.345 2.435 0.608  0.514  0.540  150 PHE HHH O   
1094 C CB  . PHE A 147 ? 2.637 2.727 2.751 0.604  0.471  0.516  150 PHE HHH CB  
1095 C CG  . PHE A 147 ? 2.588 2.717 2.693 0.599  0.439  0.519  150 PHE HHH CG  
1096 C CD1 . PHE A 147 ? 2.528 2.647 2.604 0.612  0.422  0.538  150 PHE HHH CD1 
1097 C CD2 . PHE A 147 ? 2.537 2.712 2.662 0.578  0.429  0.501  150 PHE HHH CD2 
1098 C CE1 . PHE A 147 ? 2.428 2.584 2.497 0.604  0.395  0.539  150 PHE HHH CE1 
1099 C CE2 . PHE A 147 ? 2.482 2.690 2.600 0.571  0.403  0.502  150 PHE HHH CE2 
1100 C CZ  . PHE A 147 ? 2.453 2.653 2.544 0.584  0.386  0.520  150 PHE HHH CZ  
1101 N N   . PRO A 148 ? 2.557 2.552 2.573 0.571  0.476  0.533  151 PRO HHH N   
1102 C CA  . PRO A 148 ? 2.513 2.537 2.523 0.540  0.459  0.519  151 PRO HHH CA  
1103 C C   . PRO A 148 ? 2.507 2.501 2.495 0.508  0.475  0.503  151 PRO HHH C   
1104 O O   . PRO A 148 ? 2.454 2.411 2.438 0.507  0.501  0.498  151 PRO HHH O   
1105 C CB  . PRO A 148 ? 2.558 2.595 2.548 0.546  0.433  0.534  151 PRO HHH CB  
1106 C CG  . PRO A 148 ? 2.659 2.647 2.625 0.564  0.445  0.551  151 PRO HHH CG  
1107 C CD  . PRO A 148 ? 2.673 2.637 2.658 0.584  0.471  0.553  151 PRO HHH CD  
1108 N N   . GLU A 149 ? 2.376 2.389 2.349 0.484  0.460  0.494  152 GLU HHH N   
1109 C CA  . GLU A 149 ? 2.451 2.443 2.399 0.457  0.469  0.479  152 GLU HHH CA  
1110 C C   . GLU A 149 ? 2.614 2.577 2.539 0.458  0.469  0.487  152 GLU HHH C   
1111 O O   . GLU A 149 ? 2.919 2.883 2.840 0.476  0.457  0.505  152 GLU HHH O   
1112 C CB  . GLU A 149 ? 2.466 2.485 2.403 0.436  0.453  0.470  152 GLU HHH CB  
1113 C CG  . GLU A 149 ? 2.534 2.567 2.484 0.426  0.464  0.455  152 GLU HHH CG  
1114 C CD  . GLU A 149 ? 2.698 2.734 2.620 0.401  0.459  0.444  152 GLU HHH CD  
1115 O OE1 . GLU A 149 ? 2.781 2.799 2.685 0.389  0.472  0.430  152 GLU HHH OE1 
1116 O OE2 . GLU A 149 ? 2.914 2.970 2.831 0.396  0.444  0.447  152 GLU HHH OE2 
1117 N N   . PRO A 150 ? 2.764 2.702 2.672 0.439  0.484  0.472  153 PRO HHH N   
1118 C CA  . PRO A 150 ? 2.591 2.532 2.497 0.418  0.496  0.449  153 PRO HHH CA  
1119 C C   . PRO A 150 ? 2.404 2.323 2.328 0.421  0.528  0.438  153 PRO HHH C   
1120 O O   . PRO A 150 ? 2.410 2.303 2.343 0.438  0.543  0.450  153 PRO HHH O   
1121 C CB  . PRO A 150 ? 2.839 2.770 2.720 0.399  0.495  0.435  153 PRO HHH CB  
1122 C CG  . PRO A 150 ? 2.968 2.870 2.844 0.410  0.500  0.448  153 PRO HHH CG  
1123 C CD  . PRO A 150 ? 2.969 2.876 2.857 0.437  0.490  0.474  153 PRO HHH CD  
1124 N N   . VAL A 151 ? 2.301 2.227 2.226 0.403  0.540  0.417  154 VAL HHH N   
1125 C CA  . VAL A 151 ? 2.408 2.308 2.341 0.396  0.573  0.399  154 VAL HHH CA  
1126 C C   . VAL A 151 ? 2.464 2.370 2.375 0.369  0.575  0.373  154 VAL HHH C   
1127 O O   . VAL A 151 ? 2.818 2.751 2.713 0.359  0.556  0.368  154 VAL HHH O   
1128 C CB  . VAL A 151 ? 2.353 2.257 2.313 0.404  0.590  0.396  154 VAL HHH CB  
1129 C CG1 . VAL A 151 ? 2.158 2.091 2.113 0.387  0.583  0.381  154 VAL HHH CG1 
1130 C CG2 . VAL A 151 ? 2.453 2.323 2.429 0.404  0.627  0.383  154 VAL HHH CG2 
1131 N N   . THR A 152 ? 2.424 2.307 2.333 0.358  0.596  0.355  155 THR HHH N   
1132 C CA  . THR A 152 ? 2.478 2.372 2.369 0.333  0.599  0.324  155 THR HHH CA  
1133 C C   . THR A 152 ? 2.591 2.478 2.496 0.322  0.631  0.299  155 THR HHH C   
1134 O O   . THR A 152 ? 2.634 2.492 2.562 0.332  0.658  0.303  155 THR HHH O   
1135 C CB  . THR A 152 ? 2.505 2.386 2.388 0.324  0.603  0.314  155 THR HHH CB  
1136 O OG1 . THR A 152 ? 2.675 2.517 2.576 0.325  0.640  0.306  155 THR HHH OG1 
1137 C CG2 . THR A 152 ? 2.526 2.409 2.397 0.335  0.576  0.339  155 THR HHH CG2 
1138 N N   . VAL A 153 ? 2.625 2.537 2.513 0.304  0.627  0.274  156 VAL HHH N   
1139 C CA  . VAL A 153 ? 2.604 2.515 2.500 0.288  0.656  0.244  156 VAL HHH CA  
1140 C C   . VAL A 153 ? 2.604 2.539 2.478 0.267  0.652  0.210  156 VAL HHH C   
1141 O O   . VAL A 153 ? 2.593 2.556 2.439 0.266  0.621  0.213  156 VAL HHH O   
1142 C CB  . VAL A 153 ? 2.592 2.517 2.490 0.291  0.656  0.248  156 VAL HHH CB  
1143 C CG1 . VAL A 153 ? 2.585 2.535 2.456 0.296  0.622  0.266  156 VAL HHH CG1 
1144 C CG2 . VAL A 153 ? 2.660 2.592 2.555 0.273  0.680  0.215  156 VAL HHH CG2 
1145 N N   . SER A 154 ? 2.648 2.572 2.536 0.252  0.682  0.179  157 SER HHH N   
1146 C CA  . SER A 154 ? 2.652 2.605 2.526 0.230  0.683  0.138  157 SER HHH CA  
1147 C C   . SER A 154 ? 2.680 2.633 2.566 0.216  0.715  0.109  157 SER HHH C   
1148 O O   . SER A 154 ? 2.648 2.572 2.556 0.224  0.738  0.122  157 SER HHH O   
1149 C CB  . SER A 154 ? 2.657 2.600 2.542 0.220  0.693  0.121  157 SER HHH CB  
1150 O OG  . SER A 154 ? 2.589 2.485 2.503 0.221  0.732  0.123  157 SER HHH OG  
1151 N N   . TRP A 155 ? 2.679 2.667 2.549 0.197  0.714  0.071  158 TRP HHH N   
1152 C CA  . TRP A 155 ? 2.735 2.731 2.608 0.182  0.740  0.040  158 TRP HHH CA  
1153 C C   . TRP A 155 ? 2.734 2.740 2.623 0.158  0.766  -0.009 158 TRP HHH C   
1154 O O   . TRP A 155 ? 2.921 2.962 2.793 0.151  0.745  -0.029 158 TRP HHH O   
1155 C CB  . TRP A 155 ? 2.834 2.868 2.666 0.183  0.713  0.039  158 TRP HHH CB  
1156 C CG  . TRP A 155 ? 2.787 2.806 2.612 0.200  0.702  0.079  158 TRP HHH CG  
1157 C CD1 . TRP A 155 ? 2.716 2.737 2.522 0.217  0.670  0.114  158 TRP HHH CD1 
1158 C CD2 . TRP A 155 ? 2.615 2.616 2.456 0.201  0.727  0.082  158 TRP HHH CD2 
1159 N NE1 . TRP A 155 ? 2.627 2.635 2.438 0.227  0.673  0.138  158 TRP HHH NE1 
1160 C CE2 . TRP A 155 ? 2.519 2.516 2.352 0.218  0.708  0.120  158 TRP HHH CE2 
1161 C CE3 . TRP A 155 ? 2.560 2.550 2.426 0.188  0.766  0.055  158 TRP HHH CE3 
1162 C CZ2 . TRP A 155 ? 2.500 2.483 2.348 0.222  0.725  0.129  158 TRP HHH CZ2 
1163 C CZ3 . TRP A 155 ? 2.663 2.638 2.542 0.193  0.782  0.067  158 TRP HHH CZ3 
1164 C CH2 . TRP A 155 ? 2.695 2.668 2.567 0.210  0.761  0.103  158 TRP HHH CH2 
1165 N N   . ASN A 156 ? 2.766 2.742 2.687 0.147  0.810  -0.028 159 ASN HHH N   
1166 C CA  . ASN A 156 ? 2.820 2.797 2.763 0.122  0.843  -0.076 159 ASN HHH CA  
1167 C C   . ASN A 156 ? 2.753 2.724 2.700 0.124  0.833  -0.072 159 ASN HHH C   
1168 O O   . ASN A 156 ? 2.564 2.569 2.513 0.104  0.833  -0.113 159 ASN HHH O   
1169 C CB  . ASN A 156 ? 2.944 2.977 2.872 0.101  0.841  -0.126 159 ASN HHH CB  
1170 C CG  . ASN A 156 ? 3.041 3.080 2.959 0.100  0.850  -0.128 159 ASN HHH CG  
1171 O OD1 . ASN A 156 ? 3.072 3.078 2.994 0.116  0.853  -0.091 159 ASN HHH OD1 
1172 N ND2 . ASN A 156 ? 2.983 3.065 2.886 0.080  0.853  -0.173 159 ASN HHH ND2 
1173 N N   . SER A 157 ? 2.768 2.703 2.716 0.146  0.821  -0.024 160 SER HHH N   
1174 C CA  . SER A 157 ? 2.799 2.716 2.749 0.151  0.813  -0.010 160 SER HHH CA  
1175 C C   . SER A 157 ? 2.889 2.860 2.814 0.149  0.770  -0.020 160 SER HHH C   
1176 O O   . SER A 157 ? 2.877 2.842 2.808 0.147  0.767  -0.021 160 SER HHH O   
1177 C CB  . SER A 157 ? 2.885 2.768 2.864 0.133  0.861  -0.040 160 SER HHH CB  
1178 O OG  . SER A 157 ? 2.941 2.769 2.941 0.139  0.902  -0.029 160 SER HHH OG  
1179 N N   . GLY A 158 ? 3.027 3.045 2.925 0.151  0.738  -0.024 161 GLY HHH N   
1180 C CA  . GLY A 158 ? 2.985 3.055 2.857 0.152  0.697  -0.034 161 GLY HHH CA  
1181 C C   . GLY A 158 ? 3.060 3.184 2.924 0.133  0.697  -0.087 161 GLY HHH C   
1182 O O   . GLY A 158 ? 2.981 3.153 2.823 0.137  0.661  -0.098 161 GLY HHH O   
1183 N N   . ALA A 159 ? 3.111 3.232 2.993 0.115  0.733  -0.121 162 ALA HHH N   
1184 C CA  . ALA A 159 ? 3.146 3.323 3.018 0.097  0.734  -0.173 162 ALA HHH CA  
1185 C C   . ALA A 159 ? 3.187 3.395 3.012 0.113  0.699  -0.156 162 ALA HHH C   
1186 O O   . ALA A 159 ? 3.321 3.582 3.126 0.104  0.690  -0.194 162 ALA HHH O   
1187 C CB  . ALA A 159 ? 3.208 3.366 3.112 0.075  0.785  -0.209 162 ALA HHH CB  
1188 N N   . LEU A 160 ? 3.069 3.245 2.877 0.134  0.684  -0.103 163 LEU HHH N   
1189 C CA  . LEU A 160 ? 2.878 3.071 2.639 0.150  0.652  -0.078 163 LEU HHH CA  
1190 C C   . LEU A 160 ? 2.638 2.822 2.382 0.173  0.617  -0.033 163 LEU HHH C   
1191 O O   . LEU A 160 ? 2.532 2.673 2.291 0.183  0.622  0.006  163 LEU HHH O   
1192 C CB  . LEU A 160 ? 2.984 3.144 2.748 0.152  0.676  -0.060 163 LEU HHH CB  
1193 C CG  . LEU A 160 ? 3.194 3.381 2.930 0.143  0.682  -0.085 163 LEU HHH CG  
1194 C CD1 . LEU A 160 ? 3.213 3.364 2.953 0.147  0.701  -0.059 163 LEU HHH CD1 
1195 C CD2 . LEU A 160 ? 3.242 3.473 2.922 0.154  0.642  -0.086 163 LEU HHH CD2 
1196 N N   . THR A 161 ? 2.532 2.756 2.246 0.181  0.581  -0.038 164 THR HHH N   
1197 C CA  . THR A 161 ? 2.615 2.831 2.302 0.203  0.545  0.005  164 THR HHH CA  
1198 C C   . THR A 161 ? 2.650 2.885 2.283 0.216  0.524  0.016  164 THR HHH C   
1199 O O   . THR A 161 ? 2.742 2.956 2.354 0.232  0.506  0.057  164 THR HHH O   
1200 C CB  . THR A 161 ? 2.666 2.905 2.359 0.207  0.521  -0.002 164 THR HHH CB  
1201 O OG1 . THR A 161 ? 2.962 3.201 2.698 0.188  0.549  -0.036 164 THR HHH OG1 
1202 C CG2 . THR A 161 ? 2.531 2.742 2.222 0.224  0.502  0.044  164 THR HHH CG2 
1203 N N   . SER A 162 ? 2.651 2.920 2.262 0.207  0.528  -0.020 165 SER HHH N   
1204 C CA  . SER A 162 ? 2.675 2.964 2.227 0.219  0.509  -0.016 165 SER HHH CA  
1205 C C   . SER A 162 ? 2.631 2.877 2.170 0.222  0.525  0.018  165 SER HHH C   
1206 O O   . SER A 162 ? 2.587 2.815 2.155 0.207  0.559  0.006  165 SER HHH O   
1207 C CB  . SER A 162 ? 2.760 3.098 2.298 0.207  0.514  -0.067 165 SER HHH CB  
1208 O OG  . SER A 162 ? 2.837 3.187 2.312 0.219  0.502  -0.061 165 SER HHH OG  
1209 N N   . GLY A 163 ? 2.676 2.907 2.174 0.241  0.504  0.056  166 GLY HHH N   
1210 C CA  . GLY A 163 ? 2.773 2.971 2.247 0.244  0.517  0.084  166 GLY HHH CA  
1211 C C   . GLY A 163 ? 2.738 2.895 2.260 0.240  0.537  0.110  166 GLY HHH C   
1212 O O   . GLY A 163 ? 2.698 2.832 2.217 0.236  0.558  0.119  166 GLY HHH O   
1213 N N   . VAL A 164 ? 2.722 2.870 2.284 0.243  0.531  0.121  167 VAL HHH N   
1214 C CA  . VAL A 164 ? 2.715 2.827 2.324 0.243  0.549  0.144  167 VAL HHH CA  
1215 C C   . VAL A 164 ? 2.704 2.799 2.300 0.258  0.530  0.185  167 VAL HHH C   
1216 O O   . VAL A 164 ? 2.930 3.036 2.504 0.268  0.502  0.195  167 VAL HHH O   
1217 C CB  . VAL A 164 ? 2.623 2.732 2.281 0.237  0.558  0.133  167 VAL HHH CB  
1218 C CG1 . VAL A 164 ? 2.570 2.643 2.272 0.240  0.579  0.155  167 VAL HHH CG1 
1219 C CG2 . VAL A 164 ? 2.689 2.819 2.360 0.220  0.576  0.087  167 VAL HHH CG2 
1220 N N   . HIS A 165 ? 2.613 2.683 2.223 0.259  0.545  0.205  168 HIS HHH N   
1221 C CA  . HIS A 165 ? 2.551 2.604 2.164 0.270  0.533  0.241  168 HIS HHH CA  
1222 C C   . HIS A 165 ? 2.540 2.576 2.208 0.271  0.551  0.252  168 HIS HHH C   
1223 O O   . HIS A 165 ? 2.584 2.612 2.271 0.265  0.576  0.245  168 HIS HHH O   
1224 C CB  . HIS A 165 ? 2.538 2.585 2.105 0.273  0.532  0.253  168 HIS HHH CB  
1225 C CG  . HIS A 165 ? 2.598 2.656 2.108 0.281  0.507  0.254  168 HIS HHH CG  
1226 N ND1 . HIS A 165 ? 2.720 2.787 2.225 0.291  0.480  0.264  168 HIS HHH ND1 
1227 C CD2 . HIS A 165 ? 2.671 2.734 2.124 0.282  0.506  0.246  168 HIS HHH CD2 
1228 C CE1 . HIS A 165 ? 2.788 2.865 2.239 0.300  0.463  0.263  168 HIS HHH CE1 
1229 N NE2 . HIS A 165 ? 2.764 2.839 2.179 0.296  0.477  0.253  168 HIS HHH NE2 
1230 N N   . THR A 166 ? 2.588 2.619 2.282 0.279  0.539  0.267  169 THR HHH N   
1231 C CA  . THR A 166 ? 2.608 2.624 2.349 0.286  0.549  0.283  169 THR HHH CA  
1232 C C   . THR A 166 ? 2.482 2.498 2.219 0.296  0.533  0.310  169 THR HHH C   
1233 O O   . THR A 166 ? 2.642 2.664 2.356 0.300  0.509  0.321  169 THR HHH O   
1234 C CB  . THR A 166 ? 2.628 2.638 2.398 0.290  0.550  0.281  169 THR HHH CB  
1235 O OG1 . THR A 166 ? 2.589 2.598 2.367 0.278  0.573  0.252  169 THR HHH OG1 
1236 C CG2 . THR A 166 ? 2.638 2.634 2.447 0.303  0.554  0.304  169 THR HHH CG2 
1237 N N   . PHE A 167 ? 2.250 2.262 2.009 0.298  0.546  0.319  170 PHE HHH N   
1238 C CA  . PHE A 167 ? 2.231 2.245 1.985 0.302  0.535  0.339  170 PHE HHH CA  
1239 C C   . PHE A 167 ? 2.133 2.151 1.918 0.315  0.519  0.357  170 PHE HHH C   
1240 O O   . PHE A 167 ? 2.068 2.083 1.888 0.322  0.526  0.357  170 PHE HHH O   
1241 C CB  . PHE A 167 ? 2.296 2.308 2.061 0.297  0.556  0.335  170 PHE HHH CB  
1242 C CG  . PHE A 167 ? 2.411 2.418 2.128 0.285  0.565  0.323  170 PHE HHH CG  
1243 C CD1 . PHE A 167 ? 2.583 2.589 2.293 0.277  0.583  0.301  170 PHE HHH CD1 
1244 C CD2 . PHE A 167 ? 2.448 2.449 2.123 0.284  0.555  0.334  170 PHE HHH CD2 
1245 C CE1 . PHE A 167 ? 2.688 2.691 2.348 0.268  0.589  0.289  170 PHE HHH CE1 
1246 C CE2 . PHE A 167 ? 2.690 2.682 2.312 0.277  0.563  0.326  170 PHE HHH CE2 
1247 C CZ  . PHE A 167 ? 2.754 2.750 2.368 0.269  0.579  0.303  170 PHE HHH CZ  
1248 N N   . PRO A 168 ? 2.157 2.179 1.929 0.318  0.500  0.373  171 PRO HHH N   
1249 C CA  . PRO A 168 ? 2.179 2.210 1.980 0.328  0.487  0.390  171 PRO HHH CA  
1250 C C   . PRO A 168 ? 2.060 2.099 1.905 0.334  0.501  0.390  171 PRO HHH C   
1251 O O   . PRO A 168 ? 1.873 1.915 1.718 0.327  0.515  0.384  171 PRO HHH O   
1252 C CB  . PRO A 168 ? 2.278 2.310 2.054 0.325  0.474  0.400  171 PRO HHH CB  
1253 C CG  . PRO A 168 ? 2.361 2.384 2.088 0.319  0.469  0.394  171 PRO HHH CG  
1254 C CD  . PRO A 168 ? 2.320 2.338 2.044 0.312  0.491  0.376  171 PRO HHH CD  
1255 N N   . ALA A 169 ? 2.117 2.160 1.996 0.348  0.498  0.397  172 ALA HHH N   
1256 C CA  . ALA A 169 ? 2.164 2.219 2.088 0.361  0.508  0.399  172 ALA HHH CA  
1257 C C   . ALA A 169 ? 2.155 2.233 2.092 0.360  0.500  0.404  172 ALA HHH C   
1258 O O   . ALA A 169 ? 2.202 2.283 2.117 0.355  0.483  0.412  172 ALA HHH O   
1259 C CB  . ALA A 169 ? 2.190 2.242 2.137 0.380  0.502  0.410  172 ALA HHH CB  
1260 N N   . VAL A 170 ? 2.172 2.264 2.143 0.363  0.515  0.396  173 VAL HHH N   
1261 C CA  . VAL A 170 ? 2.249 2.368 2.244 0.361  0.513  0.394  173 VAL HHH CA  
1262 C C   . VAL A 170 ? 2.114 2.258 2.161 0.383  0.511  0.396  173 VAL HHH C   
1263 O O   . VAL A 170 ? 2.138 2.276 2.206 0.391  0.528  0.389  173 VAL HHH O   
1264 C CB  . VAL A 170 ? 2.444 2.558 2.429 0.341  0.536  0.379  173 VAL HHH CB  
1265 C CG1 . VAL A 170 ? 2.485 2.576 2.414 0.324  0.532  0.382  173 VAL HHH CG1 
1266 C CG2 . VAL A 170 ? 2.460 2.561 2.452 0.339  0.560  0.366  173 VAL HHH CG2 
1267 N N   . LEU A 171 ? 2.104 2.275 2.169 0.395  0.490  0.404  174 LEU HHH N   
1268 C CA  . LEU A 171 ? 2.281 2.483 2.395 0.420  0.486  0.405  174 LEU HHH CA  
1269 C C   . LEU A 171 ? 2.167 2.399 2.322 0.414  0.503  0.386  174 LEU HHH C   
1270 O O   . LEU A 171 ? 1.976 2.227 2.134 0.397  0.503  0.376  174 LEU HHH O   
1271 C CB  . LEU A 171 ? 2.381 2.610 2.502 0.433  0.458  0.417  174 LEU HHH CB  
1272 C CG  . LEU A 171 ? 2.327 2.589 2.491 0.465  0.448  0.421  174 LEU HHH CG  
1273 C CD1 . LEU A 171 ? 2.311 2.544 2.459 0.488  0.443  0.441  174 LEU HHH CD1 
1274 C CD2 . LEU A 171 ? 2.342 2.652 2.526 0.470  0.425  0.420  174 LEU HHH CD2 
1275 N N   . GLN A 172 ? 2.163 2.396 2.348 0.427  0.519  0.379  175 GLN HHH N   
1276 C CA  . GLN A 172 ? 2.224 2.486 2.454 0.424  0.537  0.358  175 GLN HHH CA  
1277 C C   . GLN A 172 ? 2.191 2.510 2.470 0.442  0.520  0.353  175 GLN HHH C   
1278 O O   . GLN A 172 ? 2.383 2.715 2.658 0.460  0.494  0.368  175 GLN HHH O   
1279 C CB  . GLN A 172 ? 2.329 2.575 2.578 0.435  0.559  0.352  175 GLN HHH CB  
1280 C CG  . GLN A 172 ? 2.485 2.681 2.688 0.417  0.576  0.353  175 GLN HHH CG  
1281 C CD  . GLN A 172 ? 2.569 2.746 2.790 0.433  0.594  0.351  175 GLN HHH CD  
1282 O OE1 . GLN A 172 ? 2.678 2.860 2.923 0.462  0.586  0.363  175 GLN HHH OE1 
1283 N NE2 . GLN A 172 ? 2.579 2.731 2.786 0.413  0.620  0.337  175 GLN HHH NE2 
1284 N N   . SER A 173 ? 2.145 2.500 2.469 0.437  0.534  0.330  176 SER HHH N   
1285 C CA  . SER A 173 ? 2.151 2.571 2.535 0.457  0.521  0.318  176 SER HHH CA  
1286 C C   . SER A 173 ? 2.247 2.675 2.652 0.499  0.508  0.333  176 SER HHH C   
1287 O O   . SER A 173 ? 2.404 2.883 2.845 0.524  0.487  0.331  176 SER HHH O   
1288 C CB  . SER A 173 ? 2.211 2.662 2.640 0.441  0.545  0.287  176 SER HHH CB  
1289 O OG  . SER A 173 ? 2.244 2.764 2.737 0.462  0.533  0.271  176 SER HHH OG  
1290 N N   . SER A 174 ? 2.315 2.694 2.697 0.506  0.522  0.345  177 SER HHH N   
1291 C CA  . SER A 174 ? 2.326 2.694 2.718 0.545  0.516  0.363  177 SER HHH CA  
1292 C C   . SER A 174 ? 2.297 2.665 2.664 0.567  0.486  0.388  177 SER HHH C   
1293 O O   . SER A 174 ? 2.321 2.696 2.703 0.606  0.476  0.402  177 SER HHH O   
1294 C CB  . SER A 174 ? 2.318 2.626 2.686 0.539  0.543  0.367  177 SER HHH CB  
1295 O OG  . SER A 174 ? 2.227 2.518 2.603 0.576  0.543  0.384  177 SER HHH OG  
1296 N N   . GLY A 175 ? 2.216 2.575 2.545 0.545  0.472  0.394  178 GLY HHH N   
1297 C CA  . GLY A 175 ? 2.257 2.608 2.555 0.561  0.447  0.418  178 GLY HHH CA  
1298 C C   . GLY A 175 ? 2.478 2.765 2.735 0.564  0.458  0.437  178 GLY HHH C   
1299 O O   . GLY A 175 ? 2.861 3.132 3.092 0.582  0.442  0.458  178 GLY HHH O   
1300 N N   . LEU A 176 ? 2.543 2.795 2.794 0.547  0.486  0.427  179 LEU HHH N   
1301 C CA  . LEU A 176 ? 2.600 2.792 2.815 0.541  0.502  0.437  179 LEU HHH CA  
1302 C C   . LEU A 176 ? 2.597 2.769 2.779 0.502  0.511  0.425  179 LEU HHH C   
1303 O O   . LEU A 176 ? 2.473 2.668 2.666 0.482  0.516  0.408  179 LEU HHH O   
1304 C CB  . LEU A 176 ? 2.627 2.800 2.868 0.558  0.528  0.433  179 LEU HHH CB  
1305 C CG  . LEU A 176 ? 2.592 2.782 2.864 0.603  0.520  0.446  179 LEU HHH CG  
1306 C CD1 . LEU A 176 ? 2.579 2.745 2.876 0.619  0.550  0.441  179 LEU HHH CD1 
1307 C CD2 . LEU A 176 ? 2.668 2.834 2.905 0.624  0.503  0.473  179 LEU HHH CD2 
1308 N N   . TYR A 177 ? 2.602 2.733 2.742 0.492  0.513  0.433  180 TYR HHH N   
1309 C CA  . TYR A 177 ? 2.595 2.706 2.698 0.459  0.518  0.423  180 TYR HHH CA  
1310 C C   . TYR A 177 ? 2.524 2.616 2.631 0.446  0.549  0.406  180 TYR HHH C   
1311 O O   . TYR A 177 ? 2.479 2.561 2.612 0.462  0.566  0.404  180 TYR HHH O   
1312 C CB  . TYR A 177 ? 2.517 2.600 2.580 0.455  0.507  0.436  180 TYR HHH CB  
1313 C CG  . TYR A 177 ? 2.578 2.681 2.628 0.456  0.478  0.448  180 TYR HHH CG  
1314 C CD1 . TYR A 177 ? 2.692 2.793 2.741 0.479  0.463  0.466  180 TYR HHH CD1 
1315 C CD2 . TYR A 177 ? 2.663 2.782 2.698 0.436  0.468  0.441  180 TYR HHH CD2 
1316 C CE1 . TYR A 177 ? 2.728 2.847 2.764 0.478  0.438  0.475  180 TYR HHH CE1 
1317 C CE2 . TYR A 177 ? 2.641 2.776 2.665 0.436  0.444  0.451  180 TYR HHH CE2 
1318 C CZ  . TYR A 177 ? 2.665 2.802 2.691 0.456  0.429  0.467  180 TYR HHH CZ  
1319 O OH  . TYR A 177 ? 2.712 2.865 2.727 0.456  0.406  0.475  180 TYR HHH OH  
1320 N N   . SER A 178 ? 2.473 2.558 2.552 0.418  0.555  0.393  181 SER HHH N   
1321 C CA  . SER A 178 ? 2.447 2.510 2.516 0.401  0.582  0.375  181 SER HHH CA  
1322 C C   . SER A 178 ? 2.314 2.365 2.333 0.376  0.577  0.369  181 SER HHH C   
1323 O O   . SER A 178 ? 2.202 2.267 2.204 0.369  0.561  0.375  181 SER HHH O   
1324 C CB  . SER A 178 ? 2.450 2.530 2.551 0.398  0.601  0.360  181 SER HHH CB  
1325 O OG  . SER A 178 ? 2.542 2.605 2.619 0.374  0.623  0.342  181 SER HHH OG  
1326 N N   . LEU A 179 ? 2.315 2.342 2.311 0.365  0.592  0.358  182 LEU HHH N   
1327 C CA  . LEU A 179 ? 2.434 2.454 2.383 0.343  0.590  0.347  182 LEU HHH CA  
1328 C C   . LEU A 179 ? 2.445 2.450 2.386 0.330  0.617  0.325  182 LEU HHH C   
1329 O O   . LEU A 179 ? 2.464 2.457 2.436 0.338  0.637  0.319  182 LEU HHH O   
1330 C CB  . LEU A 179 ? 2.373 2.387 2.294 0.344  0.568  0.357  182 LEU HHH CB  
1331 C CG  . LEU A 179 ? 2.429 2.423 2.356 0.350  0.574  0.356  182 LEU HHH CG  
1332 C CD1 . LEU A 179 ? 2.446 2.429 2.350 0.333  0.590  0.332  182 LEU HHH CD1 
1333 C CD2 . LEU A 179 ? 2.516 2.511 2.431 0.358  0.549  0.372  182 LEU HHH CD2 
1334 N N   . SER A 180 ? 2.381 2.386 2.282 0.312  0.619  0.313  183 SER HHH N   
1335 C CA  . SER A 180 ? 2.314 2.311 2.199 0.297  0.640  0.288  183 SER HHH CA  
1336 C C   . SER A 180 ? 2.378 2.372 2.227 0.290  0.627  0.281  183 SER HHH C   
1337 O O   . SER A 180 ? 2.401 2.401 2.226 0.294  0.601  0.296  183 SER HHH O   
1338 C CB  . SER A 180 ? 2.283 2.284 2.145 0.283  0.651  0.279  183 SER HHH CB  
1339 O OG  . SER A 180 ? 2.209 2.219 2.093 0.289  0.649  0.292  183 SER HHH OG  
1340 N N   . SER A 181 ? 2.383 2.371 2.232 0.281  0.645  0.259  184 SER HHH N   
1341 C CA  . SER A 181 ? 2.432 2.425 2.248 0.271  0.635  0.244  184 SER HHH CA  
1342 C C   . SER A 181 ? 2.452 2.451 2.247 0.255  0.654  0.214  184 SER HHH C   
1343 O O   . SER A 181 ? 2.516 2.505 2.339 0.249  0.682  0.197  184 SER HHH O   
1344 C CB  . SER A 181 ? 2.466 2.448 2.303 0.275  0.637  0.241  184 SER HHH CB  
1345 O OG  . SER A 181 ? 2.570 2.565 2.379 0.264  0.628  0.221  184 SER HHH OG  
1346 N N   . VAL A 182 ? 2.360 2.374 2.105 0.248  0.639  0.208  185 VAL HHH N   
1347 C CA  . VAL A 182 ? 2.296 2.319 2.012 0.234  0.655  0.181  185 VAL HHH CA  
1348 C C   . VAL A 182 ? 2.337 2.381 2.017 0.228  0.639  0.160  185 VAL HHH C   
1349 O O   . VAL A 182 ? 2.250 2.301 1.921 0.237  0.613  0.172  185 VAL HHH O   
1350 C CB  . VAL A 182 ? 2.271 2.291 1.954 0.234  0.654  0.195  185 VAL HHH CB  
1351 C CG1 . VAL A 182 ? 2.189 2.194 1.914 0.240  0.667  0.213  185 VAL HHH CG1 
1352 C CG2 . VAL A 182 ? 2.317 2.341 1.952 0.242  0.623  0.214  185 VAL HHH CG2 
1353 N N   . VAL A 183 ? 2.440 2.497 2.104 0.214  0.655  0.128  186 VAL HHH N   
1354 C CA  . VAL A 183 ? 2.535 2.623 2.163 0.209  0.640  0.101  186 VAL HHH CA  
1355 C C   . VAL A 183 ? 2.527 2.628 2.117 0.198  0.654  0.078  186 VAL HHH C   
1356 O O   . VAL A 183 ? 2.476 2.563 2.088 0.188  0.684  0.068  186 VAL HHH O   
1357 C CB  . VAL A 183 ? 2.527 2.623 2.193 0.200  0.649  0.075  186 VAL HHH CB  
1358 C CG1 . VAL A 183 ? 2.645 2.723 2.357 0.187  0.689  0.056  186 VAL HHH CG1 
1359 C CG2 . VAL A 183 ? 2.505 2.640 2.141 0.193  0.635  0.041  186 VAL HHH CG2 
1360 N N   . THR A 184 ? 2.577 2.704 2.111 0.202  0.631  0.069  187 THR HHH N   
1361 C CA  . THR A 184 ? 2.664 2.807 2.146 0.195  0.637  0.049  187 THR HHH CA  
1362 C C   . THR A 184 ? 2.632 2.816 2.114 0.184  0.638  0.002  187 THR HHH C   
1363 O O   . THR A 184 ? 2.649 2.857 2.130 0.190  0.614  -0.005 187 THR HHH O   
1364 C CB  . THR A 184 ? 2.776 2.915 2.191 0.212  0.611  0.077  187 THR HHH CB  
1365 O OG1 . THR A 184 ? 2.786 2.953 2.180 0.224  0.578  0.073  187 THR HHH OG1 
1366 C CG2 . THR A 184 ? 2.790 2.891 2.216 0.221  0.611  0.119  187 THR HHH CG2 
1367 N N   . VAL A 185 ? 2.653 2.845 2.139 0.166  0.667  -0.031 188 VAL HHH N   
1368 C CA  . VAL A 185 ? 2.785 3.019 2.278 0.150  0.673  -0.082 188 VAL HHH CA  
1369 C C   . VAL A 185 ? 2.934 3.188 2.378 0.142  0.684  -0.107 188 VAL HHH C   
1370 O O   . VAL A 185 ? 3.110 3.335 2.538 0.141  0.701  -0.090 188 VAL HHH O   
1371 C CB  . VAL A 185 ? 2.838 3.058 2.406 0.133  0.707  -0.104 188 VAL HHH CB  
1372 C CG1 . VAL A 185 ? 2.836 3.032 2.446 0.143  0.698  -0.076 188 VAL HHH CG1 
1373 C CG2 . VAL A 185 ? 2.850 3.037 2.443 0.122  0.746  -0.103 188 VAL HHH CG2 
1374 N N   . PRO A 186 ? 3.047 3.352 2.466 0.136  0.674  -0.150 189 PRO HHH N   
1375 C CA  . PRO A 186 ? 3.199 3.528 2.569 0.127  0.684  -0.178 189 PRO HHH CA  
1376 C C   . PRO A 186 ? 3.202 3.507 2.611 0.103  0.732  -0.197 189 PRO HHH C   
1377 O O   . PRO A 186 ? 3.127 3.427 2.602 0.088  0.755  -0.217 189 PRO HHH O   
1378 C CB  . PRO A 186 ? 3.200 3.595 2.561 0.121  0.668  -0.229 189 PRO HHH CB  
1379 C CG  . PRO A 186 ? 3.126 3.532 2.513 0.134  0.639  -0.218 189 PRO HHH CG  
1380 C CD  . PRO A 186 ? 3.016 3.362 2.453 0.136  0.653  -0.176 189 PRO HHH CD  
1381 N N   . SER A 187 ? 3.209 3.498 2.576 0.101  0.747  -0.190 190 SER HHH N   
1382 C CA  . SER A 187 ? 3.266 3.533 2.669 0.079  0.793  -0.207 190 SER HHH CA  
1383 C C   . SER A 187 ? 3.220 3.523 2.659 0.054  0.815  -0.266 190 SER HHH C   
1384 O O   . SER A 187 ? 3.177 3.458 2.671 0.036  0.856  -0.283 190 SER HHH O   
1385 C CB  . SER A 187 ? 3.379 3.631 2.722 0.078  0.804  -0.197 190 SER HHH CB  
1386 O OG  . SER A 187 ? 3.510 3.726 2.823 0.099  0.787  -0.145 190 SER HHH OG  
1387 N N   . SER A 188 ? 3.243 3.601 2.653 0.056  0.790  -0.298 191 SER HHH N   
1388 C CA  . SER A 188 ? 3.281 3.684 2.726 0.033  0.805  -0.360 191 SER HHH CA  
1389 C C   . SER A 188 ? 3.245 3.617 2.779 0.020  0.834  -0.364 191 SER HHH C   
1390 O O   . SER A 188 ? 3.371 3.739 2.948 -0.005 0.876  -0.401 191 SER HHH O   
1391 C CB  . SER A 188 ? 3.312 3.778 2.724 0.043  0.764  -0.383 191 SER HHH CB  
1392 O OG  . SER A 188 ? 3.389 3.874 2.713 0.065  0.731  -0.364 191 SER HHH OG  
1393 N N   . SER A 189 ? 3.084 3.432 2.640 0.037  0.813  -0.326 192 SER HHH N   
1394 C CA  . SER A 189 ? 2.911 3.238 2.540 0.029  0.831  -0.332 192 SER HHH CA  
1395 C C   . SER A 189 ? 2.971 3.233 2.650 0.028  0.867  -0.303 192 SER HHH C   
1396 O O   . SER A 189 ? 2.889 3.129 2.626 0.018  0.894  -0.314 192 SER HHH O   
1397 C CB  . SER A 189 ? 2.744 3.078 2.367 0.049  0.792  -0.306 192 SER HHH CB  
1398 O OG  . SER A 189 ? 2.540 2.848 2.127 0.074  0.765  -0.249 192 SER HHH OG  
1399 N N   . LEU A 190 ? 3.129 3.364 2.786 0.038  0.869  -0.269 193 LEU HHH N   
1400 C CA  . LEU A 190 ? 3.174 3.353 2.877 0.042  0.897  -0.239 193 LEU HHH CA  
1401 C C   . LEU A 190 ? 3.209 3.371 2.971 0.020  0.948  -0.275 193 LEU HHH C   
1402 O O   . LEU A 190 ? 3.217 3.334 3.031 0.027  0.969  -0.253 193 LEU HHH O   
1403 C CB  . LEU A 190 ? 3.309 3.474 2.975 0.049  0.897  -0.213 193 LEU HHH CB  
1404 C CG  . LEU A 190 ? 3.390 3.554 3.005 0.072  0.856  -0.168 193 LEU HHH CG  
1405 C CD1 . LEU A 190 ? 3.498 3.638 3.088 0.075  0.866  -0.145 193 LEU HHH CD1 
1406 C CD2 . LEU A 190 ? 3.363 3.503 3.011 0.090  0.837  -0.130 193 LEU HHH CD2 
1407 N N   . GLY A 191 ? 3.311 3.507 3.063 -0.004 0.967  -0.328 194 GLY HHH N   
1408 C CA  . GLY A 191 ? 3.299 3.482 3.101 -0.028 1.020  -0.369 194 GLY HHH CA  
1409 C C   . GLY A 191 ? 3.275 3.480 3.107 -0.048 1.034  -0.417 194 GLY HHH C   
1410 O O   . GLY A 191 ? 3.232 3.427 3.105 -0.071 1.081  -0.457 194 GLY HHH O   
1411 N N   . THR A 192 ? 3.210 3.445 3.026 -0.040 0.998  -0.416 195 THR HHH N   
1412 C CA  . THR A 192 ? 3.226 3.488 3.070 -0.058 1.008  -0.463 195 THR HHH CA  
1413 C C   . THR A 192 ? 3.177 3.398 3.060 -0.046 1.007  -0.431 195 THR HHH C   
1414 O O   . THR A 192 ? 3.105 3.285 3.042 -0.058 1.050  -0.444 195 THR HHH O   
1415 C CB  . THR A 192 ? 3.212 3.550 3.007 -0.060 0.967  -0.492 195 THR HHH CB  
1416 O OG1 . THR A 192 ? 3.326 3.700 3.086 -0.074 0.975  -0.527 195 THR HHH OG1 
1417 C CG2 . THR A 192 ? 3.187 3.558 3.015 -0.077 0.972  -0.539 195 THR HHH CG2 
1418 N N   . GLN A 193 ? 3.157 3.386 3.009 -0.022 0.960  -0.391 196 GLN HHH N   
1419 C CA  . GLN A 193 ? 3.078 3.270 2.957 -0.007 0.951  -0.357 196 GLN HHH CA  
1420 C C   . GLN A 193 ? 3.144 3.276 3.037 0.015  0.957  -0.298 196 GLN HHH C   
1421 O O   . GLN A 193 ? 3.082 3.217 2.942 0.029  0.938  -0.270 196 GLN HHH O   
1422 C CB  . GLN A 193 ? 2.967 3.201 2.810 0.008  0.899  -0.344 196 GLN HHH CB  
1423 C CG  . GLN A 193 ? 2.938 3.135 2.805 0.023  0.889  -0.309 196 GLN HHH CG  
1424 C CD  . GLN A 193 ? 2.929 3.166 2.762 0.036  0.839  -0.299 196 GLN HHH CD  
1425 O OE1 . GLN A 193 ? 2.858 3.152 2.652 0.035  0.812  -0.323 196 GLN HHH OE1 
1426 N NE2 . GLN A 193 ? 3.002 3.209 2.850 0.051  0.827  -0.262 196 GLN HHH NE2 
1427 N N   . THR A 194 ? 3.209 3.289 3.148 0.020  0.983  -0.282 197 THR HHH N   
1428 C CA  . THR A 194 ? 3.100 3.127 3.057 0.045  0.986  -0.227 197 THR HHH CA  
1429 C C   . THR A 194 ? 3.017 3.042 2.956 0.068  0.942  -0.184 197 THR HHH C   
1430 O O   . THR A 194 ? 2.814 2.857 2.751 0.062  0.930  -0.198 197 THR HHH O   
1431 C CB  . THR A 194 ? 3.125 3.096 3.136 0.040  1.039  -0.234 197 THR HHH CB  
1432 O OG1 . THR A 194 ? 2.970 2.902 2.994 0.064  1.041  -0.188 197 THR HHH OG1 
1433 C CG2 . THR A 194 ? 3.188 3.134 3.225 0.038  1.052  -0.238 197 THR HHH CG2 
1434 N N   . TYR A 195 ? 2.996 3.005 2.923 0.092  0.920  -0.135 198 TYR HHH N   
1435 C CA  . TYR A 195 ? 2.887 2.895 2.796 0.114  0.879  -0.091 198 TYR HHH CA  
1436 C C   . TYR A 195 ? 2.791 2.748 2.736 0.135  0.891  -0.051 198 TYR HHH C   
1437 O O   . TYR A 195 ? 2.822 2.759 2.781 0.145  0.904  -0.033 198 TYR HHH O   
1438 C CB  . TYR A 195 ? 2.879 2.916 2.740 0.124  0.842  -0.071 198 TYR HHH CB  
1439 C CG  . TYR A 195 ? 2.878 2.964 2.696 0.109  0.827  -0.107 198 TYR HHH CG  
1440 C CD1 . TYR A 195 ? 2.836 2.956 2.629 0.111  0.794  -0.114 198 TYR HHH CD1 
1441 C CD2 . TYR A 195 ? 2.883 2.986 2.686 0.095  0.845  -0.134 198 TYR HHH CD2 
1442 C CE1 . TYR A 195 ? 2.833 3.004 2.585 0.102  0.777  -0.147 198 TYR HHH CE1 
1443 C CE2 . TYR A 195 ? 2.838 2.988 2.597 0.084  0.829  -0.166 198 TYR HHH CE2 
1444 C CZ  . TYR A 195 ? 2.855 3.041 2.589 0.089  0.795  -0.173 198 TYR HHH CZ  
1445 O OH  . TYR A 195 ? 2.875 3.112 2.564 0.083  0.777  -0.205 198 TYR HHH OH  
1446 N N   . ILE A 196 ? 2.635 2.571 2.593 0.142  0.888  -0.038 199 ILE HHH N   
1447 C CA  . ILE A 196 ? 2.639 2.526 2.627 0.165  0.899  -0.000 199 ILE HHH CA  
1448 C C   . ILE A 196 ? 2.735 2.629 2.703 0.184  0.857  0.037  199 ILE HHH C   
1449 O O   . ILE A 196 ? 2.721 2.634 2.673 0.175  0.840  0.024  199 ILE HHH O   
1450 C CB  . ILE A 196 ? 2.614 2.460 2.635 0.156  0.943  -0.020 199 ILE HHH CB  
1451 C CG1 . ILE A 196 ? 2.570 2.420 2.607 0.130  0.984  -0.068 199 ILE HHH CG1 
1452 C CG2 . ILE A 196 ? 2.653 2.446 2.699 0.184  0.956  0.022  199 ILE HHH CG2 
1453 C CD1 . ILE A 196 ? 2.588 2.408 2.653 0.112  1.028  -0.101 199 ILE HHH CD1 
1454 N N   . CYS A 197 ? 2.836 2.718 2.807 0.208  0.841  0.078  200 CYS HHH N   
1455 C CA  . CYS A 197 ? 2.817 2.703 2.774 0.227  0.803  0.115  200 CYS HHH CA  
1456 C C   . CYS A 197 ? 2.670 2.512 2.651 0.243  0.818  0.137  200 CYS HHH C   
1457 O O   . CYS A 197 ? 2.536 2.346 2.547 0.253  0.848  0.143  200 CYS HHH O   
1458 C CB  . CYS A 197 ? 2.911 2.813 2.856 0.241  0.778  0.143  200 CYS HHH CB  
1459 S SG  . CYS A 197 ? 3.076 2.948 3.058 0.270  0.787  0.181  200 CYS HHH SG  
1460 N N   . ASN A 198 ? 2.632 2.474 2.601 0.246  0.798  0.147  201 ASN HHH N   
1461 C CA  . ASN A 198 ? 2.686 2.486 2.668 0.261  0.811  0.168  201 ASN HHH CA  
1462 C C   . ASN A 198 ? 2.592 2.399 2.562 0.285  0.772  0.210  201 ASN HHH C   
1463 O O   . ASN A 198 ? 2.523 2.359 2.470 0.279  0.741  0.211  201 ASN HHH O   
1464 C CB  . ASN A 198 ? 2.727 2.521 2.705 0.240  0.823  0.140  201 ASN HHH CB  
1465 C CG  . ASN A 198 ? 2.740 2.551 2.723 0.211  0.849  0.090  201 ASN HHH CG  
1466 O OD1 . ASN A 198 ? 2.655 2.512 2.618 0.196  0.826  0.067  201 ASN HHH OD1 
1467 N ND2 . ASN A 198 ? 2.759 2.535 2.769 0.204  0.895  0.072  201 ASN HHH ND2 
1468 N N   . VAL A 199 ? 2.585 2.373 2.572 0.310  0.774  0.241  202 VAL HHH N   
1469 C CA  . VAL A 199 ? 2.641 2.443 2.621 0.333  0.738  0.278  202 VAL HHH CA  
1470 C C   . VAL A 199 ? 2.586 2.348 2.569 0.354  0.745  0.303  202 VAL HHH C   
1471 O O   . VAL A 199 ? 2.527 2.249 2.529 0.365  0.778  0.306  202 VAL HHH O   
1472 C CB  . VAL A 199 ? 2.795 2.615 2.789 0.348  0.730  0.292  202 VAL HHH CB  
1473 C CG1 . VAL A 199 ? 2.868 2.718 2.853 0.326  0.730  0.267  202 VAL HHH CG1 
1474 C CG2 . VAL A 199 ? 2.871 2.660 2.897 0.370  0.757  0.304  202 VAL HHH CG2 
1475 N N   . ASN A 200 ? 2.553 2.325 2.517 0.359  0.716  0.321  203 ASN HHH N   
1476 C CA  . ASN A 200 ? 2.562 2.301 2.522 0.380  0.716  0.348  203 ASN HHH CA  
1477 C C   . ASN A 200 ? 2.487 2.250 2.445 0.405  0.680  0.381  203 ASN HHH C   
1478 O O   . ASN A 200 ? 2.339 2.142 2.284 0.396  0.649  0.381  203 ASN HHH O   
1479 C CB  . ASN A 200 ? 2.620 2.350 2.560 0.364  0.714  0.338  203 ASN HHH CB  
1480 C CG  . ASN A 200 ? 2.723 2.416 2.669 0.345  0.757  0.309  203 ASN HHH CG  
1481 O OD1 . ASN A 200 ? 2.788 2.478 2.750 0.334  0.783  0.286  203 ASN HHH OD1 
1482 N ND2 . ASN A 200 ? 2.741 2.408 2.675 0.338  0.767  0.306  203 ASN HHH ND2 
1483 N N   . HIS A 201 ? 2.576 2.320 2.547 0.435  0.686  0.407  204 HIS HHH N   
1484 C CA  . HIS A 201 ? 2.588 2.354 2.556 0.461  0.653  0.438  204 HIS HHH CA  
1485 C C   . HIS A 201 ? 2.820 2.544 2.772 0.481  0.660  0.461  204 HIS HHH C   
1486 O O   . HIS A 201 ? 2.860 2.548 2.822 0.506  0.684  0.475  204 HIS HHH O   
1487 C CB  . HIS A 201 ? 2.455 2.242 2.452 0.483  0.649  0.447  204 HIS HHH CB  
1488 C CG  . HIS A 201 ? 2.317 2.138 2.315 0.505  0.614  0.471  204 HIS HHH CG  
1489 N ND1 . HIS A 201 ? 2.263 2.080 2.276 0.542  0.613  0.494  204 HIS HHH ND1 
1490 C CD2 . HIS A 201 ? 2.202 2.063 2.189 0.496  0.580  0.474  204 HIS HHH CD2 
1491 C CE1 . HIS A 201 ? 2.220 2.079 2.234 0.554  0.578  0.508  204 HIS HHH CE1 
1492 N NE2 . HIS A 201 ? 2.200 2.084 2.199 0.525  0.559  0.496  204 HIS HHH NE2 
1493 N N   . LYS A 202 ? 2.918 2.645 2.845 0.472  0.642  0.465  205 LYS HHH N   
1494 C CA  . LYS A 202 ? 2.911 2.595 2.818 0.486  0.652  0.484  205 LYS HHH CA  
1495 C C   . LYS A 202 ? 2.945 2.632 2.849 0.525  0.634  0.519  205 LYS HHH C   
1496 O O   . LYS A 202 ? 3.201 2.841 3.096 0.549  0.656  0.538  205 LYS HHH O   
1497 C CB  . LYS A 202 ? 2.976 2.665 2.859 0.461  0.640  0.473  205 LYS HHH CB  
1498 C CG  . LYS A 202 ? 3.223 2.861 3.083 0.469  0.659  0.487  205 LYS HHH CG  
1499 C CD  . LYS A 202 ? 3.284 2.897 3.135 0.437  0.683  0.458  205 LYS HHH CD  
1500 C CE  . LYS A 202 ? 3.300 2.860 3.126 0.443  0.704  0.472  205 LYS HHH CE  
1501 N NZ  . LYS A 202 ? 3.268 2.852 3.076 0.432  0.676  0.473  205 LYS HHH NZ  
1502 N N   . PRO A 203 ? 2.796 2.537 2.708 0.535  0.596  0.530  206 PRO HHH N   
1503 C CA  . PRO A 203 ? 2.649 2.399 2.562 0.575  0.579  0.560  206 PRO HHH CA  
1504 C C   . PRO A 203 ? 2.589 2.312 2.519 0.608  0.602  0.573  206 PRO HHH C   
1505 O O   . PRO A 203 ? 2.575 2.285 2.492 0.643  0.597  0.599  206 PRO HHH O   
1506 C CB  . PRO A 203 ? 2.619 2.436 2.548 0.572  0.541  0.557  206 PRO HHH CB  
1507 C CG  . PRO A 203 ? 2.588 2.421 2.507 0.532  0.532  0.534  206 PRO HHH CG  
1508 C CD  . PRO A 203 ? 2.700 2.494 2.618 0.511  0.568  0.514  206 PRO HHH CD  
1509 N N   . SER A 204 ? 2.642 2.355 2.597 0.600  0.628  0.555  207 SER HHH N   
1510 C CA  . SER A 204 ? 2.755 2.433 2.727 0.631  0.658  0.565  207 SER HHH CA  
1511 C C   . SER A 204 ? 2.787 2.394 2.747 0.618  0.705  0.555  207 SER HHH C   
1512 O O   . SER A 204 ? 2.733 2.299 2.704 0.641  0.736  0.563  207 SER HHH O   
1513 C CB  . SER A 204 ? 2.749 2.464 2.761 0.631  0.657  0.549  207 SER HHH CB  
1514 O OG  . SER A 204 ? 2.698 2.423 2.717 0.588  0.668  0.517  207 SER HHH OG  
1515 N N   . ASN A 205 ? 2.854 2.450 2.795 0.581  0.711  0.537  208 ASN HHH N   
1516 C CA  . ASN A 205 ? 3.011 2.547 2.940 0.559  0.755  0.519  208 ASN HHH CA  
1517 C C   . ASN A 205 ? 3.043 2.564 3.003 0.551  0.791  0.497  208 ASN HHH C   
1518 O O   . ASN A 205 ? 3.142 2.600 3.099 0.556  0.835  0.496  208 ASN HHH O   
1519 C CB  . ASN A 205 ? 3.169 2.641 3.066 0.583  0.775  0.546  208 ASN HHH CB  
1520 C CG  . ASN A 205 ? 3.238 2.677 3.114 0.549  0.797  0.528  208 ASN HHH CG  
1521 O OD1 . ASN A 205 ? 3.388 2.814 3.278 0.517  0.826  0.495  208 ASN HHH OD1 
1522 N ND2 . ASN A 205 ? 3.191 2.620 3.035 0.554  0.782  0.546  208 ASN HHH ND2 
1523 N N   . THR A 206 ? 3.011 2.584 2.996 0.537  0.774  0.478  209 THR HHH N   
1524 C CA  . THR A 206 ? 3.049 2.618 3.062 0.523  0.804  0.452  209 THR HHH CA  
1525 C C   . THR A 206 ? 3.028 2.628 3.039 0.478  0.801  0.414  209 THR HHH C   
1526 O O   . THR A 206 ? 2.712 2.362 2.714 0.466  0.763  0.413  209 THR HHH O   
1527 C CB  . THR A 206 ? 3.010 2.613 3.054 0.548  0.791  0.461  209 THR HHH CB  
1528 O OG1 . THR A 206 ? 2.832 2.499 2.881 0.527  0.758  0.447  209 THR HHH OG1 
1529 C CG2 . THR A 206 ? 3.006 2.605 3.048 0.596  0.775  0.500  209 THR HHH CG2 
1530 N N   . LYS A 207 ? 3.199 2.768 3.217 0.454  0.841  0.385  210 LYS HHH N   
1531 C CA  . LYS A 207 ? 3.263 2.859 3.278 0.412  0.844  0.345  210 LYS HHH CA  
1532 C C   . LYS A 207 ? 3.305 2.896 3.347 0.400  0.877  0.318  210 LYS HHH C   
1533 O O   . LYS A 207 ? 3.333 2.871 3.386 0.401  0.922  0.310  210 LYS HHH O   
1534 C CB  . LYS A 207 ? 3.357 2.925 3.354 0.390  0.860  0.329  210 LYS HHH CB  
1535 C CG  . LYS A 207 ? 3.451 2.990 3.425 0.410  0.851  0.361  210 LYS HHH CG  
1536 C CD  . LYS A 207 ? 3.584 3.047 3.557 0.431  0.895  0.377  210 LYS HHH CD  
1537 C CE  . LYS A 207 ? 3.541 2.967 3.485 0.443  0.895  0.401  210 LYS HHH CE  
1538 N NZ  . LYS A 207 ? 3.549 2.895 3.487 0.465  0.943  0.418  210 LYS HHH NZ  
1539 N N   . VAL A 208 ? 3.191 2.832 3.241 0.389  0.858  0.304  211 VAL HHH N   
1540 C CA  . VAL A 208 ? 2.992 2.635 3.068 0.383  0.883  0.283  211 VAL HHH CA  
1541 C C   . VAL A 208 ? 2.929 2.604 2.996 0.343  0.886  0.242  211 VAL HHH C   
1542 O O   . VAL A 208 ? 2.894 2.609 2.937 0.330  0.851  0.239  211 VAL HHH O   
1543 C CB  . VAL A 208 ? 2.865 2.541 2.957 0.406  0.859  0.304  211 VAL HHH CB  
1544 C CG1 . VAL A 208 ? 2.911 2.586 3.033 0.403  0.888  0.286  211 VAL HHH CG1 
1545 C CG2 . VAL A 208 ? 2.822 2.483 2.918 0.447  0.844  0.345  211 VAL HHH CG2 
1546 N N   . ASP A 209 ? 2.962 2.620 3.046 0.325  0.926  0.209  212 ASP HHH N   
1547 C CA  . ASP A 209 ? 3.012 2.704 3.088 0.288  0.931  0.166  212 ASP HHH CA  
1548 C C   . ASP A 209 ? 3.001 2.701 3.098 0.283  0.953  0.148  212 ASP HHH C   
1549 O O   . ASP A 209 ? 2.907 2.570 3.029 0.279  0.998  0.131  212 ASP HHH O   
1550 C CB  . ASP A 209 ? 3.033 2.704 3.106 0.263  0.960  0.133  212 ASP HHH CB  
1551 C CG  . ASP A 209 ? 2.991 2.645 3.047 0.267  0.948  0.148  212 ASP HHH CG  
1552 O OD1 . ASP A 209 ? 3.041 2.658 3.104 0.254  0.983  0.129  212 ASP HHH OD1 
1553 O OD2 . ASP A 209 ? 2.889 2.567 2.927 0.282  0.905  0.177  212 ASP HHH OD2 
1554 N N   . LYS A 210 ? 3.006 2.750 3.093 0.281  0.925  0.150  213 LYS HHH N   
1555 C CA  . LYS A 210 ? 3.008 2.766 3.110 0.272  0.942  0.131  213 LYS HHH CA  
1556 C C   . LYS A 210 ? 3.012 2.803 3.089 0.237  0.943  0.090  213 LYS HHH C   
1557 O O   . LYS A 210 ? 2.937 2.762 2.979 0.229  0.907  0.090  213 LYS HHH O   
1558 C CB  . LYS A 210 ? 2.931 2.714 3.036 0.291  0.915  0.157  213 LYS HHH CB  
1559 C CG  . LYS A 210 ? 2.923 2.704 3.060 0.294  0.942  0.147  213 LYS HHH CG  
1560 C CD  . LYS A 210 ? 3.003 2.738 3.180 0.317  0.976  0.158  213 LYS HHH CD  
1561 C CE  . LYS A 210 ? 3.007 2.737 3.200 0.357  0.955  0.199  213 LYS HHH CE  
1562 N NZ  . LYS A 210 ? 3.015 2.759 3.242 0.372  0.961  0.203  213 LYS HHH NZ  
1563 N N   . LYS A 211 ? 2.993 2.775 3.087 0.218  0.982  0.055  214 LYS HHH N   
1564 C CA  . LYS A 211 ? 2.965 2.784 3.036 0.186  0.984  0.013  214 LYS HHH CA  
1565 C C   . LYS A 211 ? 2.922 2.767 2.982 0.187  0.972  0.017  214 LYS HHH C   
1566 O O   . LYS A 211 ? 2.991 2.819 3.082 0.203  0.987  0.033  214 LYS HHH O   
1567 C CB  . LYS A 211 ? 2.993 2.795 3.083 0.162  1.031  -0.032 214 LYS HHH CB  
1568 C CG  . LYS A 211 ? 2.976 2.744 3.107 0.165  1.077  -0.041 214 LYS HHH CG  
1569 C CD  . LYS A 211 ? 3.003 2.760 3.149 0.135  1.122  -0.091 214 LYS HHH CD  
1570 C CE  . LYS A 211 ? 3.142 2.843 3.333 0.143  1.175  -0.093 214 LYS HHH CE  
1571 N NZ  . LYS A 211 ? 3.326 3.035 3.533 0.137  1.195  -0.108 214 LYS HHH NZ  
1572 N N   . VAL A 212 ? 2.923 2.809 2.941 0.172  0.946  0.005  215 VAL HHH N   
1573 C CA  . VAL A 212 ? 2.987 2.897 2.985 0.168  0.938  0.004  215 VAL HHH CA  
1574 C C   . VAL A 212 ? 2.972 2.901 2.956 0.139  0.962  -0.043 215 VAL HHH C   
1575 O O   . VAL A 212 ? 3.008 2.950 2.981 0.123  0.964  -0.072 215 VAL HHH O   
1576 C CB  . VAL A 212 ? 3.028 2.964 2.985 0.177  0.891  0.031  215 VAL HHH CB  
1577 C CG1 . VAL A 212 ? 3.011 2.930 2.984 0.203  0.870  0.072  215 VAL HHH CG1 
1578 C CG2 . VAL A 212 ? 3.016 2.982 2.927 0.162  0.869  0.011  215 VAL HHH CG2 
1579 N N   . GLU A 213 ? 2.904 2.833 2.894 0.133  0.983  -0.054 216 GLU HHH N   
1580 C CA  . GLU A 213 ? 2.880 2.831 2.852 0.106  1.005  -0.098 216 GLU HHH CA  
1581 C C   . GLU A 213 ? 2.893 2.843 2.868 0.105  1.019  -0.095 216 GLU HHH C   
1582 O O   . GLU A 213 ? 2.901 2.829 2.912 0.123  1.026  -0.069 216 GLU HHH O   
1583 C CB  . GLU A 213 ? 2.882 2.816 2.890 0.089  1.047  -0.135 216 GLU HHH CB  
1584 C CG  . GLU A 213 ? 2.934 2.822 3.001 0.103  1.083  -0.123 216 GLU HHH CG  
1585 C CD  . GLU A 213 ? 2.986 2.844 3.088 0.095  1.118  -0.146 216 GLU HHH CD  
1586 O OE1 . GLU A 213 ? 2.972 2.848 3.056 0.077  1.113  -0.172 216 GLU HHH OE1 
1587 O OE2 . GLU A 213 ? 3.082 2.899 3.230 0.106  1.153  -0.140 216 GLU HHH OE2 
1588 N N   . PRO A 214 ? 2.989 2.964 2.924 0.085  1.023  -0.121 217 PRO HHH N   
1589 C CA  . PRO A 214 ? 3.059 3.032 2.996 0.081  1.042  -0.122 217 PRO HHH CA  
1590 C C   . PRO A 214 ? 3.011 2.956 3.010 0.079  1.088  -0.137 217 PRO HHH C   
1591 O O   . PRO A 214 ? 2.925 2.857 2.954 0.071  1.113  -0.161 217 PRO HHH O   
1592 C CB  . PRO A 214 ? 3.121 3.124 2.996 0.059  1.039  -0.153 217 PRO HHH CB  
1593 C CG  . PRO A 214 ? 3.127 3.151 2.987 0.048  1.032  -0.181 217 PRO HHH CG  
1594 C CD  . PRO A 214 ? 3.011 3.020 2.897 0.067  1.011  -0.153 217 PRO HHH CD  
1595 N N   . LYS A 215 ? 3.047 2.984 3.069 0.087  1.100  -0.124 218 LYS HHH N   
1596 C CA  . LYS A 215 ? 3.257 3.171 3.338 0.088  1.143  -0.136 218 LYS HHH CA  
1597 C C   . LYS A 215 ? 3.409 3.338 3.469 0.064  1.167  -0.167 218 LYS HHH C   
1598 O O   . LYS A 215 ? 3.767 3.719 3.764 0.052  1.145  -0.169 218 LYS HHH O   
1599 C CB  . LYS A 215 ? 3.278 3.178 3.401 0.119  1.131  -0.096 218 LYS HHH CB  
1600 C CG  . LYS A 215 ? 3.366 3.247 3.555 0.130  1.168  -0.101 218 LYS HHH CG  
1601 C CD  . LYS A 215 ? 3.452 3.347 3.654 0.139  1.162  -0.085 218 LYS HHH CD  
1602 C CE  . LYS A 215 ? 3.525 3.435 3.697 0.111  1.180  -0.112 218 LYS HHH CE  
1603 N NZ  . LYS A 215 ? 3.609 3.507 3.825 0.101  1.228  -0.145 218 LYS HHH NZ  
1604 N N   . SER A 216 ? 3.258 3.173 3.364 0.056  1.211  -0.191 219 SER HHH N   
1605 C CA  . SER A 216 ? 3.164 3.091 3.252 0.031  1.239  -0.223 219 SER HHH CA  
1606 C C   . SER A 216 ? 3.187 3.127 3.235 0.033  1.217  -0.202 219 SER HHH C   
1607 O O   . SER A 216 ? 3.453 3.388 3.528 0.037  1.233  -0.197 219 SER HHH O   
1608 C CB  . SER A 216 ? 3.136 3.041 3.290 0.029  1.286  -0.243 219 SER HHH CB  
1609 O OG  . SER A 216 ? 3.131 3.010 3.331 0.039  1.302  -0.246 219 SER HHH OG  
1610 N N   . ASP B 1   ? 2.368 3.291 2.717 0.088  0.310  -0.482 1   ASP LLL N   
1611 C CA  . ASP B 1   ? 2.333 3.184 2.628 0.107  0.306  -0.406 1   ASP LLL CA  
1612 C C   . ASP B 1   ? 2.393 3.098 2.678 0.074  0.330  -0.379 1   ASP LLL C   
1613 O O   . ASP B 1   ? 2.593 3.280 2.914 0.036  0.354  -0.414 1   ASP LLL O   
1614 C CB  . ASP B 1   ? 2.317 3.245 2.613 0.120  0.303  -0.403 1   ASP LLL CB  
1615 C CG  . ASP B 1   ? 2.391 3.466 2.688 0.162  0.280  -0.420 1   ASP LLL CG  
1616 O OD1 . ASP B 1   ? 2.443 3.626 2.788 0.153  0.281  -0.488 1   ASP LLL OD1 
1617 O OD2 . ASP B 1   ? 2.591 3.674 2.840 0.206  0.265  -0.364 1   ASP LLL OD2 
1618 N N   . ILE B 2   ? 2.360 2.971 2.597 0.089  0.325  -0.319 2   ILE LLL N   
1619 C CA  . ILE B 2   ? 2.237 2.710 2.454 0.067  0.345  -0.285 2   ILE LLL CA  
1620 C C   . ILE B 2   ? 2.206 2.651 2.397 0.069  0.349  -0.243 2   ILE LLL C   
1621 O O   . ILE B 2   ? 2.204 2.702 2.373 0.099  0.330  -0.216 2   ILE LLL O   
1622 C CB  . ILE B 2   ? 2.183 2.586 2.361 0.086  0.335  -0.246 2   ILE LLL CB  
1623 C CG1 . ILE B 2   ? 2.270 2.697 2.475 0.083  0.333  -0.289 2   ILE LLL CG1 
1624 C CG2 . ILE B 2   ? 2.187 2.464 2.338 0.073  0.352  -0.207 2   ILE LLL CG2 
1625 C CD1 . ILE B 2   ? 2.259 2.663 2.428 0.112  0.314  -0.257 2   ILE LLL CD1 
1626 N N   . GLN B 3   ? 2.298 2.664 2.495 0.039  0.374  -0.239 3   GLN LLL N   
1627 C CA  . GLN B 3   ? 2.361 2.686 2.531 0.039  0.379  -0.198 3   GLN LLL CA  
1628 C C   . GLN B 3   ? 2.375 2.573 2.516 0.028  0.396  -0.161 3   GLN LLL C   
1629 O O   . GLN B 3   ? 2.395 2.538 2.554 0.005  0.418  -0.182 3   GLN LLL O   
1630 C CB  . GLN B 3   ? 2.418 2.796 2.623 0.016  0.394  -0.232 3   GLN LLL CB  
1631 C CG  . GLN B 3   ? 2.539 3.041 2.752 0.042  0.372  -0.244 3   GLN LLL CG  
1632 C CD  . GLN B 3   ? 2.626 3.140 2.825 0.048  0.373  -0.219 3   GLN LLL CD  
1633 O OE1 . GLN B 3   ? 2.811 3.416 3.038 0.048  0.373  -0.251 3   GLN LLL OE1 
1634 N NE2 . GLN B 3   ? 2.679 3.108 2.836 0.056  0.374  -0.164 3   GLN LLL NE2 
1635 N N   . LEU B 4   ? 2.402 2.563 2.500 0.047  0.387  -0.108 4   LEU LLL N   
1636 C CA  . LEU B 4   ? 2.381 2.436 2.441 0.048  0.397  -0.066 4   LEU LLL CA  
1637 C C   . LEU B 4   ? 2.369 2.398 2.418 0.038  0.410  -0.044 4   LEU LLL C   
1638 O O   . LEU B 4   ? 2.250 2.335 2.296 0.049  0.397  -0.035 4   LEU LLL O   
1639 C CB  . LEU B 4   ? 2.372 2.418 2.394 0.079  0.374  -0.029 4   LEU LLL CB  
1640 C CG  . LEU B 4   ? 2.380 2.428 2.403 0.090  0.364  -0.042 4   LEU LLL CG  
1641 C CD1 . LEU B 4   ? 2.402 2.548 2.457 0.095  0.350  -0.081 4   LEU LLL CD1 
1642 C CD2 . LEU B 4   ? 2.352 2.376 2.335 0.117  0.347  -0.002 4   LEU LLL CD2 
1643 N N   . THR B 5   ? 2.432 2.380 2.474 0.020  0.435  -0.033 5   THR LLL N   
1644 C CA  . THR B 5   ? 2.477 2.387 2.503 0.011  0.449  -0.007 5   THR LLL CA  
1645 C C   . THR B 5   ? 2.386 2.203 2.368 0.023  0.457  0.034  5   THR LLL C   
1646 O O   . THR B 5   ? 2.295 2.057 2.276 0.019  0.472  0.030  5   THR LLL O   
1647 C CB  . THR B 5   ? 2.533 2.452 2.597 -0.023 0.477  -0.043 5   THR LLL CB  
1648 O OG1 . THR B 5   ? 2.668 2.541 2.754 -0.042 0.501  -0.068 5   THR LLL OG1 
1649 C CG2 . THR B 5   ? 2.496 2.523 2.598 -0.027 0.464  -0.080 5   THR LLL CG2 
1650 N N   . GLN B 6   ? 2.258 2.066 2.207 0.039  0.447  0.071  6   GLN LLL N   
1651 C CA  . GLN B 6   ? 2.374 2.113 2.279 0.054  0.451  0.110  6   GLN LLL CA  
1652 C C   . GLN B 6   ? 2.512 2.200 2.410 0.038  0.480  0.122  6   GLN LLL C   
1653 O O   . GLN B 6   ? 2.598 2.317 2.520 0.018  0.489  0.106  6   GLN LLL O   
1654 C CB  . GLN B 6   ? 2.360 2.125 2.237 0.078  0.426  0.137  6   GLN LLL CB  
1655 C CG  . GLN B 6   ? 2.387 2.204 2.271 0.094  0.400  0.127  6   GLN LLL CG  
1656 C CD  . GLN B 6   ? 2.347 2.187 2.210 0.114  0.382  0.151  6   GLN LLL CD  
1657 O OE1 . GLN B 6   ? 2.326 2.215 2.197 0.125  0.366  0.145  6   GLN LLL OE1 
1658 N NE2 . GLN B 6   ? 2.388 2.196 2.224 0.119  0.386  0.176  6   GLN LLL NE2 
1659 N N   . SER B 7   ? 2.610 2.226 2.475 0.048  0.496  0.149  7   SER LLL N   
1660 C CA  . SER B 7   ? 2.647 2.211 2.491 0.043  0.523  0.173  7   SER LLL CA  
1661 C C   . SER B 7   ? 2.588 2.119 2.381 0.075  0.514  0.213  7   SER LLL C   
1662 O O   . SER B 7   ? 2.617 2.125 2.392 0.095  0.507  0.220  7   SER LLL O   
1663 C CB  . SER B 7   ? 2.808 2.313 2.668 0.021  0.562  0.161  7   SER LLL CB  
1664 O OG  . SER B 7   ? 2.904 2.451 2.817 -0.008 0.567  0.115  7   SER LLL OG  
1665 N N   . PRO B 8   ? 2.490 2.024 2.258 0.082  0.514  0.236  8   PRO LLL N   
1666 C CA  . PRO B 8   ? 2.440 2.004 2.228 0.060  0.521  0.228  8   PRO LLL CA  
1667 C C   . PRO B 8   ? 2.353 1.991 2.159 0.060  0.492  0.214  8   PRO LLL C   
1668 O O   . PRO B 8   ? 2.330 1.994 2.133 0.077  0.468  0.213  8   PRO LLL O   
1669 C CB  . PRO B 8   ? 2.527 2.061 2.273 0.075  0.531  0.262  8   PRO LLL CB  
1670 C CG  . PRO B 8   ? 2.449 1.988 2.163 0.108  0.507  0.280  8   PRO LLL CG  
1671 C CD  . PRO B 8   ? 2.515 2.031 2.236 0.113  0.507  0.269  8   PRO LLL CD  
1672 N N   . ASP B 9   ? 2.322 1.991 2.147 0.044  0.497  0.206  9   ASP LLL N   
1673 C CA  . ASP B 9   ? 2.381 2.114 2.219 0.048  0.476  0.198  9   ASP LLL CA  
1674 C C   . ASP B 9   ? 2.300 2.033 2.106 0.069  0.462  0.224  9   ASP LLL C   
1675 O O   . ASP B 9   ? 2.301 2.065 2.106 0.084  0.440  0.224  9   ASP LLL O   
1676 C CB  . ASP B 9   ? 2.591 2.355 2.456 0.026  0.488  0.182  9   ASP LLL CB  
1677 C CG  . ASP B 9   ? 2.847 2.655 2.754 0.010  0.489  0.145  9   ASP LLL CG  
1678 O OD1 . ASP B 9   ? 2.951 2.742 2.867 0.006  0.491  0.131  9   ASP LLL OD1 
1679 O OD2 . ASP B 9   ? 3.133 2.997 3.064 0.002  0.486  0.128  9   ASP LLL OD2 
1680 N N   . SER B 10  ? 2.277 1.978 2.058 0.071  0.475  0.244  10  SER LLL N   
1681 C CA  . SER B 10  ? 2.275 1.982 2.027 0.090  0.464  0.263  10  SER LLL CA  
1682 C C   . SER B 10  ? 2.259 1.919 1.973 0.107  0.474  0.285  10  SER LLL C   
1683 O O   . SER B 10  ? 2.125 1.743 1.837 0.101  0.494  0.288  10  SER LLL O   
1684 C CB  . SER B 10  ? 2.305 2.033 2.061 0.082  0.470  0.264  10  SER LLL CB  
1685 O OG  . SER B 10  ? 2.356 2.087 2.085 0.099  0.463  0.280  10  SER LLL OG  
1686 N N   . LEU B 11  ? 2.365 2.036 2.053 0.128  0.462  0.297  11  LEU LLL N   
1687 C CA  . LEU B 11  ? 2.532 2.173 2.180 0.152  0.466  0.318  11  LEU LLL CA  
1688 C C   . LEU B 11  ? 2.559 2.234 2.185 0.170  0.454  0.324  11  LEU LLL C   
1689 O O   . LEU B 11  ? 2.268 1.984 1.910 0.169  0.435  0.309  11  LEU LLL O   
1690 C CB  . LEU B 11  ? 2.517 2.148 2.166 0.163  0.455  0.312  11  LEU LLL CB  
1691 C CG  . LEU B 11  ? 2.516 2.113 2.126 0.191  0.460  0.332  11  LEU LLL CG  
1692 C CD1 . LEU B 11  ? 2.470 2.029 2.087 0.191  0.467  0.328  11  LEU LLL CD1 
1693 C CD2 . LEU B 11  ? 2.488 2.126 2.080 0.215  0.437  0.332  11  LEU LLL CD2 
1694 N N   . ALA B 12  ? 2.607 2.266 2.198 0.187  0.467  0.344  12  ALA LLL N   
1695 C CA  . ALA B 12  ? 2.441 2.136 2.006 0.209  0.458  0.348  12  ALA LLL CA  
1696 C C   . ALA B 12  ? 2.301 1.977 1.822 0.243  0.463  0.369  12  ALA LLL C   
1697 O O   . ALA B 12  ? 2.233 1.857 1.733 0.249  0.486  0.391  12  ALA LLL O   
1698 C CB  . ALA B 12  ? 2.410 2.122 1.974 0.200  0.468  0.351  12  ALA LLL CB  
1699 N N   . VAL B 13  ? 2.163 1.879 1.672 0.265  0.443  0.361  13  VAL LLL N   
1700 C CA  . VAL B 13  ? 2.203 1.918 1.670 0.305  0.441  0.376  13  VAL LLL CA  
1701 C C   . VAL B 13  ? 2.116 1.903 1.572 0.323  0.424  0.362  13  VAL LLL C   
1702 O O   . VAL B 13  ? 1.910 1.738 1.399 0.304  0.409  0.334  13  VAL LLL O   
1703 C CB  . VAL B 13  ? 2.374 2.071 1.848 0.310  0.431  0.371  13  VAL LLL CB  
1704 C CG1 . VAL B 13  ? 2.413 2.138 1.853 0.351  0.419  0.375  13  VAL LLL CG1 
1705 C CG2 . VAL B 13  ? 2.479 2.104 1.956 0.300  0.453  0.386  13  VAL LLL CG2 
1706 N N   . SER B 14  ? 2.187 1.990 1.599 0.361  0.429  0.379  14  SER LLL N   
1707 C CA  . SER B 14  ? 2.225 2.109 1.624 0.382  0.414  0.360  14  SER LLL CA  
1708 C C   . SER B 14  ? 2.145 2.068 1.552 0.394  0.391  0.338  14  SER LLL C   
1709 O O   . SER B 14  ? 2.068 1.949 1.467 0.403  0.392  0.351  14  SER LLL O   
1710 C CB  . SER B 14  ? 2.384 2.276 1.730 0.422  0.427  0.387  14  SER LLL CB  
1711 O OG  . SER B 14  ? 2.609 2.426 1.925 0.440  0.448  0.424  14  SER LLL OG  
1712 N N   . LEU B 15  ? 2.093 2.092 1.518 0.391  0.375  0.304  15  LEU LLL N   
1713 C CA  . LEU B 15  ? 2.073 2.127 1.503 0.407  0.355  0.279  15  LEU LLL CA  
1714 C C   . LEU B 15  ? 2.026 2.063 1.409 0.452  0.356  0.305  15  LEU LLL C   
1715 O O   . LEU B 15  ? 2.278 2.307 1.616 0.485  0.368  0.332  15  LEU LLL O   
1716 C CB  . LEU B 15  ? 2.122 2.271 1.554 0.418  0.345  0.245  15  LEU LLL CB  
1717 C CG  . LEU B 15  ? 2.155 2.348 1.640 0.381  0.337  0.201  15  LEU LLL CG  
1718 C CD1 . LEU B 15  ? 2.219 2.513 1.704 0.402  0.324  0.162  15  LEU LLL CD1 
1719 C CD2 . LEU B 15  ? 2.145 2.298 1.663 0.355  0.333  0.196  15  LEU LLL CD2 
1720 N N   . GLY B 16  ? 1.891 1.932 1.282 0.458  0.343  0.295  16  GLY LLL N   
1721 C CA  . GLY B 16  ? 1.954 1.999 1.301 0.507  0.340  0.312  16  GLY LLL CA  
1722 C C   . GLY B 16  ? 2.047 1.994 1.370 0.516  0.359  0.353  16  GLY LLL C   
1723 O O   . GLY B 16  ? 2.068 2.002 1.365 0.550  0.357  0.366  16  GLY LLL O   
1724 N N   . GLU B 17  ? 2.154 2.037 1.489 0.487  0.379  0.371  17  GLU LLL N   
1725 C CA  . GLU B 17  ? 2.426 2.214 1.745 0.489  0.403  0.405  17  GLU LLL CA  
1726 C C   . GLU B 17  ? 2.367 2.120 1.728 0.456  0.396  0.389  17  GLU LLL C   
1727 O O   . GLU B 17  ? 2.372 2.174 1.769 0.433  0.375  0.357  17  GLU LLL O   
1728 C CB  . GLU B 17  ? 2.612 2.354 1.925 0.473  0.429  0.427  17  GLU LLL CB  
1729 C CG  . GLU B 17  ? 2.786 2.572 2.062 0.502  0.434  0.439  17  GLU LLL CG  
1730 C CD  . GLU B 17  ? 2.985 2.793 2.202 0.565  0.436  0.462  17  GLU LLL CD  
1731 O OE1 . GLU B 17  ? 3.057 2.954 2.260 0.591  0.418  0.445  17  GLU LLL OE1 
1732 O OE2 . GLU B 17  ? 3.237 2.974 2.423 0.591  0.457  0.495  17  GLU LLL OE2 
1733 N N   . ARG B 18  ? 2.397 2.071 1.755 0.452  0.415  0.409  18  ARG LLL N   
1734 C CA  . ARG B 18  ? 2.306 1.949 1.703 0.423  0.411  0.393  18  ARG LLL CA  
1735 C C   . ARG B 18  ? 2.308 1.910 1.740 0.378  0.427  0.391  18  ARG LLL C   
1736 O O   . ARG B 18  ? 2.296 1.852 1.711 0.378  0.454  0.413  18  ARG LLL O   
1737 C CB  . ARG B 18  ? 2.318 1.911 1.694 0.450  0.420  0.407  18  ARG LLL CB  
1738 C CG  . ARG B 18  ? 2.417 1.918 1.793 0.439  0.454  0.428  18  ARG LLL CG  
1739 C CD  . ARG B 18  ? 2.478 1.926 1.817 0.481  0.470  0.451  18  ARG LLL CD  
1740 N NE  . ARG B 18  ? 2.452 1.946 1.791 0.501  0.441  0.433  18  ARG LLL NE  
1741 C CZ  . ARG B 18  ? 2.562 2.048 1.864 0.549  0.442  0.447  18  ARG LLL CZ  
1742 N NH1 . ARG B 18  ? 2.639 2.062 1.895 0.586  0.473  0.485  18  ARG LLL NH1 
1743 N NH2 . ARG B 18  ? 2.562 2.100 1.872 0.560  0.413  0.425  18  ARG LLL NH2 
1744 N N   . ALA B 19  ? 2.355 1.977 1.831 0.344  0.413  0.365  19  ALA LLL N   
1745 C CA  . ALA B 19  ? 2.248 1.841 1.763 0.305  0.424  0.356  19  ALA LLL CA  
1746 C C   . ALA B 19  ? 2.174 1.739 1.707 0.298  0.423  0.345  19  ALA LLL C   
1747 O O   . ALA B 19  ? 2.062 1.652 1.594 0.314  0.404  0.336  19  ALA LLL O   
1748 C CB  . ALA B 19  ? 2.118 1.762 1.665 0.278  0.409  0.335  19  ALA LLL CB  
1749 N N   . THR B 20  ? 2.218 1.734 1.769 0.276  0.445  0.345  20  THR LLL N   
1750 C CA  . THR B 20  ? 2.279 1.771 1.857 0.263  0.447  0.328  20  THR LLL CA  
1751 C C   . THR B 20  ? 2.269 1.772 1.892 0.223  0.452  0.307  20  THR LLL C   
1752 O O   . THR B 20  ? 2.091 1.588 1.715 0.209  0.467  0.314  20  THR LLL O   
1753 C CB  . THR B 20  ? 2.389 1.808 1.945 0.280  0.475  0.345  20  THR LLL CB  
1754 O OG1 . THR B 20  ? 2.520 1.894 2.085 0.258  0.507  0.351  20  THR LLL OG1 
1755 C CG2 . THR B 20  ? 2.425 1.833 1.928 0.327  0.475  0.373  20  THR LLL CG2 
1756 N N   . ILE B 21  ? 2.386 1.911 2.043 0.208  0.440  0.281  21  ILE LLL N   
1757 C CA  . ILE B 21  ? 2.286 1.839 1.988 0.174  0.440  0.256  21  ILE LLL CA  
1758 C C   . ILE B 21  ? 2.321 1.857 2.050 0.163  0.448  0.233  21  ILE LLL C   
1759 O O   . ILE B 21  ? 2.319 1.871 2.049 0.176  0.431  0.224  21  ILE LLL O   
1760 C CB  . ILE B 21  ? 2.122 1.743 1.838 0.173  0.412  0.246  21  ILE LLL CB  
1761 C CG1 . ILE B 21  ? 2.161 1.798 1.851 0.185  0.405  0.265  21  ILE LLL CG1 
1762 C CG2 . ILE B 21  ? 2.124 1.777 1.878 0.146  0.414  0.225  21  ILE LLL CG2 
1763 C CD1 . ILE B 21  ? 2.114 1.808 1.820 0.181  0.386  0.256  21  ILE LLL CD1 
1764 N N   . ASN B 22  ? 2.377 1.883 2.130 0.138  0.475  0.220  22  ASN LLL N   
1765 C CA  . ASN B 22  ? 2.604 2.103 2.393 0.120  0.485  0.188  22  ASN LLL CA  
1766 C C   . ASN B 22  ? 2.652 2.230 2.480 0.105  0.462  0.156  22  ASN LLL C   
1767 O O   . ASN B 22  ? 2.878 2.498 2.709 0.099  0.452  0.160  22  ASN LLL O   
1768 C CB  . ASN B 22  ? 2.797 2.247 2.607 0.093  0.524  0.177  22  ASN LLL CB  
1769 C CG  . ASN B 22  ? 3.085 2.447 2.857 0.110  0.554  0.209  22  ASN LLL CG  
1770 O OD1 . ASN B 22  ? 3.208 2.544 2.951 0.140  0.548  0.225  22  ASN LLL OD1 
1771 N ND2 . ASN B 22  ? 3.203 2.523 2.974 0.093  0.588  0.219  22  ASN LLL ND2 
1772 N N   . CYS B 23  ? 2.619 2.216 2.474 0.100  0.457  0.127  23  CYS LLL N   
1773 C CA  . CYS B 23  ? 2.415 2.091 2.310 0.087  0.440  0.093  23  CYS LLL CA  
1774 C C   . CYS B 23  ? 2.276 1.949 2.206 0.071  0.453  0.053  23  CYS LLL C   
1775 O O   . CYS B 23  ? 2.138 1.799 2.063 0.085  0.445  0.049  23  CYS LLL O   
1776 C CB  . CYS B 23  ? 2.525 2.253 2.405 0.111  0.406  0.102  23  CYS LLL CB  
1777 S SG  . CYS B 23  ? 2.794 2.619 2.715 0.105  0.386  0.066  23  CYS LLL SG  
1778 N N   . LYS B 24  ? 2.309 1.994 2.277 0.041  0.474  0.023  24  LYS LLL N   
1779 C CA  . LYS B 24  ? 2.478 2.160 2.489 0.018  0.493  -0.022 24  LYS LLL CA  
1780 C C   . LYS B 24  ? 2.470 2.259 2.521 0.011  0.472  -0.064 24  LYS LLL C   
1781 O O   . LYS B 24  ? 2.422 2.267 2.476 0.010  0.460  -0.061 24  LYS LLL O   
1782 C CB  . LYS B 24  ? 2.674 2.296 2.703 -0.012 0.537  -0.032 24  LYS LLL CB  
1783 C CG  . LYS B 24  ? 2.800 2.418 2.881 -0.043 0.565  -0.085 24  LYS LLL CG  
1784 C CD  . LYS B 24  ? 2.910 2.445 3.002 -0.071 0.616  -0.086 24  LYS LLL CD  
1785 C CE  . LYS B 24  ? 2.975 2.483 3.118 -0.102 0.652  -0.138 24  LYS LLL CE  
1786 N NZ  . LYS B 24  ? 3.144 2.580 3.266 -0.081 0.659  -0.125 24  LYS LLL NZ  
1787 N N   . SER B 25  ? 2.474 2.291 2.551 0.010  0.467  -0.100 25  SER LLL N   
1788 C CA  . SER B 25  ? 2.425 2.352 2.534 0.012  0.443  -0.139 25  SER LLL CA  
1789 C C   . SER B 25  ? 2.385 2.343 2.554 -0.022 0.466  -0.201 25  SER LLL C   
1790 O O   . SER B 25  ? 2.468 2.348 2.649 -0.041 0.499  -0.212 25  SER LLL O   
1791 C CB  . SER B 25  ? 2.457 2.404 2.551 0.040  0.417  -0.134 25  SER LLL CB  
1792 O OG  . SER B 25  ? 2.518 2.448 2.640 0.029  0.431  -0.172 25  SER LLL OG  
1793 N N   . SER B 26  ? 2.326 2.394 2.529 -0.026 0.452  -0.241 26  SER LLL N   
1794 C CA  . SER B 26  ? 2.353 2.478 2.619 -0.058 0.470  -0.311 26  SER LLL CA  
1795 C C   . SER B 26  ? 2.230 2.337 2.518 -0.062 0.477  -0.344 26  SER LLL C   
1796 O O   . SER B 26  ? 2.283 2.365 2.615 -0.096 0.510  -0.391 26  SER LLL O   
1797 C CB  . SER B 26  ? 2.396 2.659 2.688 -0.051 0.447  -0.343 26  SER LLL CB  
1798 O OG  . SER B 26  ? 2.466 2.796 2.819 -0.077 0.460  -0.418 26  SER LLL OG  
1799 N N   . GLN B 27  ? 2.108 2.232 2.367 -0.029 0.448  -0.324 27  GLN LLL N   
1800 C CA  . GLN B 27  ? 2.241 2.363 2.519 -0.027 0.448  -0.356 27  GLN LLL CA  
1801 C C   . GLN B 27  ? 2.266 2.326 2.490 0.007  0.430  -0.303 27  GLN LLL C   
1802 O O   . GLN B 27  ? 2.204 2.271 2.385 0.032  0.407  -0.253 27  GLN LLL O   
1803 C CB  . GLN B 27  ? 2.315 2.575 2.630 -0.022 0.425  -0.410 27  GLN LLL CB  
1804 C CG  . GLN B 27  ? 2.397 2.671 2.741 -0.024 0.427  -0.455 27  GLN LLL CG  
1805 C CD  . GLN B 27  ? 2.362 2.769 2.715 0.002  0.392  -0.480 27  GLN LLL CD  
1806 O OE1 . GLN B 27  ? 2.404 2.910 2.759 0.013  0.373  -0.484 27  GLN LLL OE1 
1807 N NE2 . GLN B 27  ? 2.338 2.748 2.693 0.015  0.382  -0.495 27  GLN LLL NE2 
1808 N N   . SER B 28  ? 2.377 2.384 2.607 0.006  0.442  -0.318 28  SER LLL N   
1809 C CA  . SER B 28  ? 2.521 2.466 2.704 0.037  0.429  -0.274 28  SER LLL CA  
1810 C C   . SER B 28  ? 2.410 2.444 2.575 0.069  0.387  -0.263 28  SER LLL C   
1811 O O   . SER B 28  ? 2.446 2.581 2.644 0.068  0.373  -0.306 28  SER LLL O   
1812 C CB  . SER B 28  ? 2.698 2.575 2.898 0.030  0.454  -0.299 28  SER LLL CB  
1813 O OG  . SER B 28  ? 2.812 2.679 2.980 0.063  0.432  -0.277 28  SER LLL OG  
1814 N N   . VAL B 29  ? 2.270 2.266 2.383 0.097  0.371  -0.209 29  VAL LLL N   
1815 C CA  . VAL B 29  ? 2.206 2.268 2.294 0.127  0.336  -0.187 29  VAL LLL CA  
1816 C C   . VAL B 29  ? 2.181 2.207 2.245 0.150  0.327  -0.174 29  VAL LLL C   
1817 O O   . VAL B 29  ? 2.137 2.160 2.163 0.174  0.309  -0.133 29  VAL LLL O   
1818 C CB  . VAL B 29  ? 2.286 2.344 2.340 0.137  0.327  -0.139 29  VAL LLL CB  
1819 C CG1 . VAL B 29  ? 2.348 2.464 2.426 0.121  0.331  -0.155 29  VAL LLL CG1 
1820 C CG2 . VAL B 29  ? 2.409 2.363 2.429 0.137  0.343  -0.098 29  VAL LLL CG2 
1821 N N   . LEU B 30  ? 2.194 2.198 2.284 0.143  0.340  -0.210 30  LEU LLL N   
1822 C CA  . LEU B 30  ? 2.328 2.298 2.396 0.166  0.331  -0.201 30  LEU LLL CA  
1823 C C   . LEU B 30  ? 2.240 2.303 2.330 0.176  0.310  -0.236 30  LEU LLL C   
1824 O O   . LEU B 30  ? 2.316 2.414 2.451 0.158  0.320  -0.290 30  LEU LLL O   
1825 C CB  . LEU B 30  ? 2.640 2.512 2.715 0.157  0.363  -0.212 30  LEU LLL CB  
1826 C CG  . LEU B 30  ? 2.813 2.581 2.848 0.163  0.383  -0.163 30  LEU LLL CG  
1827 C CD1 . LEU B 30  ? 2.917 2.642 2.975 0.130  0.416  -0.174 30  LEU LLL CD1 
1828 C CD2 . LEU B 30  ? 2.855 2.542 2.866 0.185  0.394  -0.150 30  LEU LLL CD2 
1829 N N   . TYR B 31  ? 2.167 2.266 2.227 0.204  0.283  -0.209 31  TYR LLL N   
1830 C CA  . TYR B 31  ? 2.120 2.286 2.189 0.221  0.264  -0.234 31  TYR LLL CA  
1831 C C   . TYR B 31  ? 2.124 2.222 2.194 0.225  0.275  -0.248 31  TYR LLL C   
1832 O O   . TYR B 31  ? 2.242 2.247 2.284 0.230  0.289  -0.216 31  TYR LLL O   
1833 C CB  . TYR B 31  ? 2.023 2.238 2.058 0.247  0.238  -0.198 31  TYR LLL CB  
1834 C CG  . TYR B 31  ? 1.970 2.285 2.016 0.250  0.225  -0.205 31  TYR LLL CG  
1835 C CD1 . TYR B 31  ? 1.947 2.280 2.008 0.234  0.234  -0.208 31  TYR LLL CD1 
1836 C CD2 . TYR B 31  ? 1.943 2.340 1.986 0.272  0.205  -0.208 31  TYR LLL CD2 
1837 C CE1 . TYR B 31  ? 1.914 2.343 1.983 0.243  0.223  -0.214 31  TYR LLL CE1 
1838 C CE2 . TYR B 31  ? 1.866 2.357 1.915 0.282  0.196  -0.212 31  TYR LLL CE2 
1839 C CZ  . TYR B 31  ? 1.889 2.396 1.951 0.268  0.204  -0.214 31  TYR LLL CZ  
1840 O OH  . TYR B 31  ? 2.041 2.642 2.106 0.283  0.196  -0.215 31  TYR LLL OH  
1841 N N   . SER B 32  ? 2.140 2.288 2.243 0.224  0.272  -0.295 32  SER LLL N   
1842 C CA  . SER B 32  ? 2.329 2.425 2.442 0.229  0.284  -0.319 32  SER LLL CA  
1843 C C   . SER B 32  ? 2.372 2.506 2.460 0.260  0.257  -0.307 32  SER LLL C   
1844 O O   . SER B 32  ? 2.449 2.526 2.527 0.274  0.263  -0.307 32  SER LLL O   
1845 C CB  . SER B 32  ? 2.437 2.566 2.606 0.205  0.299  -0.387 32  SER LLL CB  
1846 O OG  . SER B 32  ? 2.694 2.749 2.885 0.176  0.334  -0.399 32  SER LLL OG  
1847 N N   . SER B 33  ? 2.507 2.734 2.586 0.272  0.231  -0.296 33  SER LLL N   
1848 C CA  . SER B 33  ? 2.633 2.906 2.689 0.301  0.207  -0.283 33  SER LLL CA  
1849 C C   . SER B 33  ? 2.489 2.682 2.504 0.318  0.207  -0.240 33  SER LLL C   
1850 O O   . SER B 33  ? 2.271 2.458 2.276 0.338  0.200  -0.244 33  SER LLL O   
1851 C CB  . SER B 33  ? 2.760 3.121 2.806 0.309  0.188  -0.263 33  SER LLL CB  
1852 O OG  . SER B 33  ? 2.916 3.308 2.934 0.334  0.170  -0.241 33  SER LLL OG  
1853 N N   . ILE B 34  ? 2.456 2.599 2.449 0.312  0.216  -0.203 34  ILE LLL N   
1854 C CA  . ILE B 34  ? 2.428 2.502 2.379 0.327  0.217  -0.158 34  ILE LLL CA  
1855 C C   . ILE B 34  ? 2.559 2.554 2.509 0.309  0.242  -0.147 34  ILE LLL C   
1856 O O   . ILE B 34  ? 2.672 2.690 2.638 0.288  0.247  -0.149 34  ILE LLL O   
1857 C CB  . ILE B 34  ? 2.204 2.328 2.129 0.338  0.198  -0.125 34  ILE LLL CB  
1858 C CG1 . ILE B 34  ? 2.073 2.257 2.011 0.324  0.195  -0.123 34  ILE LLL CG1 
1859 C CG2 . ILE B 34  ? 2.140 2.317 2.058 0.359  0.179  -0.131 34  ILE LLL CG2 
1860 C CD1 . ILE B 34  ? 2.004 2.214 1.916 0.332  0.185  -0.085 34  ILE LLL CD1 
1861 N N   . ASN B 35  ? 2.565 2.472 2.500 0.317  0.260  -0.137 35  ASN LLL N   
1862 C CA  . ASN B 35  ? 2.601 2.425 2.535 0.301  0.290  -0.127 35  ASN LLL CA  
1863 C C   . ASN B 35  ? 2.478 2.302 2.384 0.300  0.284  -0.086 35  ASN LLL C   
1864 O O   . ASN B 35  ? 2.730 2.495 2.600 0.317  0.291  -0.051 35  ASN LLL O   
1865 C CB  . ASN B 35  ? 2.708 2.436 2.623 0.320  0.312  -0.118 35  ASN LLL CB  
1866 C CG  . ASN B 35  ? 2.863 2.503 2.783 0.302  0.350  -0.113 35  ASN LLL CG  
1867 O OD1 . ASN B 35  ? 2.759 2.392 2.674 0.286  0.356  -0.094 35  ASN LLL OD1 
1868 N ND2 . ASN B 35  ? 3.112 2.680 3.044 0.305  0.378  -0.130 35  ASN LLL ND2 
1869 N N   . LYS B 36  ? 2.153 2.045 2.074 0.284  0.272  -0.089 36  LYS LLL N   
1870 C CA  . LYS B 36  ? 2.129 2.021 2.027 0.281  0.269  -0.052 36  LYS LLL CA  
1871 C C   . LYS B 36  ? 2.043 1.947 1.969 0.253  0.282  -0.065 36  LYS LLL C   
1872 O O   . LYS B 36  ? 1.977 1.925 1.938 0.239  0.283  -0.103 36  LYS LLL O   
1873 C CB  . LYS B 36  ? 2.133 2.090 2.014 0.296  0.243  -0.034 36  LYS LLL CB  
1874 C CG  . LYS B 36  ? 2.269 2.242 2.134 0.321  0.228  -0.034 36  LYS LLL CG  
1875 C CD  . LYS B 36  ? 2.405 2.315 2.240 0.343  0.233  -0.018 36  LYS LLL CD  
1876 C CE  . LYS B 36  ? 2.483 2.373 2.284 0.352  0.232  0.019  36  LYS LLL CE  
1877 N NZ  . LYS B 36  ? 2.543 2.389 2.313 0.381  0.234  0.033  36  LYS LLL NZ  
1878 N N   . ASN B 37  ? 2.092 1.954 2.000 0.245  0.293  -0.037 37  ASN LLL N   
1879 C CA  . ASN B 37  ? 2.078 1.956 2.007 0.220  0.304  -0.043 37  ASN LLL CA  
1880 C C   . ASN B 37  ? 2.084 2.029 2.005 0.225  0.283  -0.026 37  ASN LLL C   
1881 O O   . ASN B 37  ? 2.132 2.069 2.021 0.241  0.273  0.007  37  ASN LLL O   
1882 C CB  . ASN B 37  ? 2.053 1.849 1.966 0.211  0.328  -0.020 37  ASN LLL CB  
1883 C CG  . ASN B 37  ? 2.017 1.737 1.937 0.207  0.355  -0.034 37  ASN LLL CG  
1884 O OD1 . ASN B 37  ? 2.045 1.744 1.995 0.181  0.380  -0.057 37  ASN LLL OD1 
1885 N ND2 . ASN B 37  ? 1.984 1.662 1.877 0.233  0.354  -0.020 37  ASN LLL ND2 
1886 N N   . TYR B 38  ? 2.024 2.033 1.972 0.213  0.280  -0.047 38  TYR LLL N   
1887 C CA  . TYR B 38  ? 1.887 1.961 1.829 0.221  0.265  -0.030 38  TYR LLL CA  
1888 C C   . TYR B 38  ? 1.903 1.957 1.840 0.207  0.277  -0.012 38  TYR LLL C   
1889 O O   . TYR B 38  ? 1.985 2.082 1.947 0.195  0.281  -0.030 38  TYR LLL O   
1890 C CB  . TYR B 38  ? 1.838 2.002 1.808 0.224  0.254  -0.063 38  TYR LLL CB  
1891 C CG  . TYR B 38  ? 1.736 1.931 1.699 0.244  0.239  -0.067 38  TYR LLL CG  
1892 C CD1 . TYR B 38  ? 1.695 1.959 1.650 0.263  0.224  -0.057 38  TYR LLL CD1 
1893 C CD2 . TYR B 38  ? 1.770 1.919 1.731 0.247  0.241  -0.078 38  TYR LLL CD2 
1894 C CE1 . TYR B 38  ? 1.728 2.018 1.675 0.280  0.211  -0.059 38  TYR LLL CE1 
1895 C CE2 . TYR B 38  ? 1.798 1.974 1.751 0.266  0.226  -0.082 38  TYR LLL CE2 
1896 C CZ  . TYR B 38  ? 1.764 2.013 1.712 0.281  0.211  -0.074 38  TYR LLL CZ  
1897 O OH  . TYR B 38  ? 1.776 2.050 1.717 0.298  0.199  -0.079 38  TYR LLL OH  
1898 N N   . LEU B 39  ? 2.006 2.001 1.914 0.210  0.282  0.021  39  LEU LLL N   
1899 C CA  . LEU B 39  ? 1.992 1.964 1.891 0.200  0.292  0.043  39  LEU LLL CA  
1900 C C   . LEU B 39  ? 1.793 1.746 1.658 0.214  0.285  0.079  39  LEU LLL C   
1901 O O   . LEU B 39  ? 1.757 1.689 1.603 0.228  0.279  0.087  39  LEU LLL O   
1902 C CB  . LEU B 39  ? 2.022 1.929 1.927 0.182  0.315  0.036  39  LEU LLL CB  
1903 C CG  . LEU B 39  ? 2.120 2.009 2.020 0.169  0.326  0.053  39  LEU LLL CG  
1904 C CD1 . LEU B 39  ? 2.171 2.043 2.100 0.143  0.349  0.028  39  LEU LLL CD1 
1905 C CD2 . LEU B 39  ? 2.284 2.115 2.147 0.179  0.331  0.089  39  LEU LLL CD2 
1906 N N   . ALA B 40  ? 1.619 1.582 1.478 0.211  0.287  0.097  40  ALA LLL N   
1907 C CA  . ALA B 40  ? 1.715 1.671 1.548 0.222  0.281  0.124  40  ALA LLL CA  
1908 C C   . ALA B 40  ? 1.956 1.888 1.782 0.211  0.292  0.141  40  ALA LLL C   
1909 O O   . ALA B 40  ? 2.089 2.022 1.932 0.197  0.302  0.132  40  ALA LLL O   
1910 C CB  . ALA B 40  ? 1.796 1.808 1.633 0.232  0.272  0.128  40  ALA LLL CB  
1911 N N   . TRP B 41  ? 2.048 1.967 1.853 0.218  0.291  0.161  41  TRP LLL N   
1912 C CA  . TRP B 41  ? 2.051 1.944 1.844 0.211  0.301  0.177  41  TRP LLL CA  
1913 C C   . TRP B 41  ? 1.968 1.887 1.759 0.214  0.299  0.189  41  TRP LLL C   
1914 O O   . TRP B 41  ? 1.887 1.817 1.669 0.224  0.293  0.191  41  TRP LLL O   
1915 C CB  . TRP B 41  ? 2.064 1.910 1.833 0.218  0.305  0.187  41  TRP LLL CB  
1916 C CG  . TRP B 41  ? 1.962 1.767 1.733 0.213  0.317  0.180  41  TRP LLL CG  
1917 C CD1 . TRP B 41  ? 1.962 1.744 1.731 0.220  0.317  0.170  41  TRP LLL CD1 
1918 C CD2 . TRP B 41  ? 1.849 1.627 1.626 0.196  0.334  0.182  41  TRP LLL CD2 
1919 N NE1 . TRP B 41  ? 1.925 1.663 1.700 0.209  0.337  0.166  41  TRP LLL NE1 
1920 C CE2 . TRP B 41  ? 1.918 1.655 1.698 0.193  0.347  0.172  41  TRP LLL CE2 
1921 C CE3 . TRP B 41  ? 1.897 1.682 1.677 0.184  0.341  0.189  41  TRP LLL CE3 
1922 C CZ2 . TRP B 41  ? 2.046 1.747 1.835 0.176  0.369  0.170  41  TRP LLL CZ2 
1923 C CZ3 . TRP B 41  ? 2.033 1.787 1.820 0.169  0.359  0.187  41  TRP LLL CZ3 
1924 C CH2 . TRP B 41  ? 2.126 1.840 1.918 0.163  0.374  0.178  41  TRP LLL CH2 
1925 N N   . TYR B 42  ? 1.896 1.824 1.695 0.205  0.307  0.194  42  TYR LLL N   
1926 C CA  . TYR B 42  ? 1.910 1.856 1.710 0.207  0.311  0.205  42  TYR LLL CA  
1927 C C   . TYR B 42  ? 1.810 1.731 1.601 0.199  0.321  0.215  42  TYR LLL C   
1928 O O   . TYR B 42  ? 1.811 1.714 1.602 0.191  0.326  0.215  42  TYR LLL O   
1929 C CB  . TYR B 42  ? 1.974 1.957 1.790 0.211  0.314  0.205  42  TYR LLL CB  
1930 C CG  . TYR B 42  ? 1.841 1.861 1.665 0.223  0.306  0.198  42  TYR LLL CG  
1931 C CD1 . TYR B 42  ? 1.780 1.822 1.617 0.223  0.299  0.180  42  TYR LLL CD1 
1932 C CD2 . TYR B 42  ? 1.689 1.722 1.508 0.233  0.307  0.206  42  TYR LLL CD2 
1933 C CE1 . TYR B 42  ? 1.663 1.744 1.506 0.236  0.290  0.171  42  TYR LLL CE1 
1934 C CE2 . TYR B 42  ? 1.633 1.702 1.457 0.246  0.300  0.201  42  TYR LLL CE2 
1935 C CZ  . TYR B 42  ? 1.627 1.721 1.461 0.248  0.291  0.184  42  TYR LLL CZ  
1936 O OH  . TYR B 42  ? 1.746 1.879 1.584 0.262  0.283  0.177  42  TYR LLL OH  
1937 N N   . GLN B 43  ? 1.755 1.678 1.540 0.201  0.324  0.220  43  GLN LLL N   
1938 C CA  . GLN B 43  ? 1.753 1.664 1.533 0.195  0.333  0.226  43  GLN LLL CA  
1939 C C   . GLN B 43  ? 1.786 1.711 1.580 0.193  0.344  0.231  43  GLN LLL C   
1940 O O   . GLN B 43  ? 1.785 1.725 1.584 0.198  0.347  0.231  43  GLN LLL O   
1941 C CB  . GLN B 43  ? 1.738 1.648 1.504 0.199  0.329  0.221  43  GLN LLL CB  
1942 C CG  . GLN B 43  ? 1.819 1.731 1.585 0.192  0.339  0.221  43  GLN LLL CG  
1943 C CD  . GLN B 43  ? 1.834 1.764 1.596 0.196  0.337  0.209  43  GLN LLL CD  
1944 O OE1 . GLN B 43  ? 1.640 1.588 1.416 0.192  0.343  0.201  43  GLN LLL OE1 
1945 N NE2 . GLN B 43  ? 1.820 1.747 1.562 0.203  0.331  0.207  43  GLN LLL NE2 
1946 N N   . GLN B 44  ? 1.921 1.840 1.719 0.186  0.354  0.236  44  GLN LLL N   
1947 C CA  . GLN B 44  ? 1.981 1.906 1.790 0.187  0.368  0.243  44  GLN LLL CA  
1948 C C   . GLN B 44  ? 1.881 1.792 1.688 0.178  0.378  0.243  44  GLN LLL C   
1949 O O   . GLN B 44  ? 1.739 1.641 1.541 0.172  0.377  0.244  44  GLN LLL O   
1950 C CB  . GLN B 44  ? 2.139 2.083 1.956 0.195  0.370  0.249  44  GLN LLL CB  
1951 C CG  . GLN B 44  ? 2.142 2.093 1.967 0.204  0.387  0.261  44  GLN LLL CG  
1952 C CD  . GLN B 44  ? 2.109 2.086 1.940 0.216  0.387  0.265  44  GLN LLL CD  
1953 O OE1 . GLN B 44  ? 2.010 2.008 1.842 0.234  0.393  0.275  44  GLN LLL OE1 
1954 N NE2 . GLN B 44  ? 2.068 2.047 1.901 0.207  0.383  0.258  44  GLN LLL NE2 
1955 N N   . LYS B 45  ? 1.818 1.726 1.631 0.175  0.390  0.240  45  LYS LLL N   
1956 C CA  . LYS B 45  ? 1.898 1.798 1.713 0.166  0.402  0.235  45  LYS LLL CA  
1957 C C   . LYS B 45  ? 1.995 1.891 1.824 0.170  0.420  0.245  45  LYS LLL C   
1958 O O   . LYS B 45  ? 2.137 2.037 1.971 0.180  0.426  0.255  45  LYS LLL O   
1959 C CB  . LYS B 45  ? 1.944 1.850 1.762 0.160  0.405  0.219  45  LYS LLL CB  
1960 C CG  . LYS B 45  ? 1.978 1.894 1.778 0.163  0.387  0.211  45  LYS LLL CG  
1961 C CD  . LYS B 45  ? 2.060 1.997 1.864 0.163  0.385  0.194  45  LYS LLL CD  
1962 C CE  . LYS B 45  ? 2.126 2.081 1.939 0.154  0.395  0.173  45  LYS LLL CE  
1963 N NZ  . LYS B 45  ? 2.263 2.245 2.059 0.162  0.379  0.159  45  LYS LLL NZ  
1964 N N   . PRO B 46  ? 2.066 1.955 1.898 0.164  0.429  0.245  46  PRO LLL N   
1965 C CA  . PRO B 46  ? 2.048 1.930 1.891 0.171  0.449  0.255  46  PRO LLL CA  
1966 C C   . PRO B 46  ? 1.980 1.850 1.835 0.174  0.470  0.257  46  PRO LLL C   
1967 O O   . PRO B 46  ? 1.926 1.790 1.789 0.162  0.479  0.241  46  PRO LLL O   
1968 C CB  . PRO B 46  ? 2.189 2.064 2.034 0.161  0.455  0.246  46  PRO LLL CB  
1969 C CG  . PRO B 46  ? 2.258 2.141 2.088 0.154  0.435  0.241  46  PRO LLL CG  
1970 C CD  . PRO B 46  ? 2.175 2.063 1.999 0.155  0.423  0.236  46  PRO LLL CD  
1971 N N   . GLY B 47  ? 2.017 1.886 1.872 0.192  0.480  0.275  47  GLY LLL N   
1972 C CA  . GLY B 47  ? 2.039 1.890 1.903 0.199  0.508  0.284  47  GLY LLL CA  
1973 C C   . GLY B 47  ? 1.928 1.786 1.792 0.197  0.504  0.280  47  GLY LLL C   
1974 O O   . GLY B 47  ? 1.902 1.741 1.778 0.193  0.529  0.279  47  GLY LLL O   
1975 N N   . GLN B 48  ? 1.838 1.719 1.690 0.199  0.476  0.277  48  GLN LLL N   
1976 C CA  . GLN B 48  ? 1.935 1.828 1.786 0.198  0.467  0.272  48  GLN LLL CA  
1977 C C   . GLN B 48  ? 1.928 1.846 1.768 0.216  0.449  0.283  48  GLN LLL C   
1978 O O   . GLN B 48  ? 1.949 1.881 1.784 0.221  0.434  0.284  48  GLN LLL O   
1979 C CB  . GLN B 48  ? 2.140 2.039 1.989 0.181  0.449  0.249  48  GLN LLL CB  
1980 C CG  . GLN B 48  ? 2.270 2.160 2.132 0.164  0.465  0.231  48  GLN LLL CG  
1981 C CD  . GLN B 48  ? 2.361 2.269 2.221 0.152  0.450  0.207  48  GLN LLL CD  
1982 O OE1 . GLN B 48  ? 2.234 2.158 2.083 0.157  0.430  0.204  48  GLN LLL OE1 
1983 N NE2 . GLN B 48  ? 2.459 2.369 2.330 0.138  0.461  0.187  48  GLN LLL NE2 
1984 N N   . PRO B 49  ? 1.851 1.780 1.690 0.225  0.451  0.287  49  PRO LLL N   
1985 C CA  . PRO B 49  ? 1.782 1.742 1.613 0.240  0.431  0.291  49  PRO LLL CA  
1986 C C   . PRO B 49  ? 1.682 1.651 1.509 0.228  0.403  0.273  49  PRO LLL C   
1987 O O   . PRO B 49  ? 1.839 1.794 1.666 0.213  0.400  0.260  49  PRO LLL O   
1988 C CB  . PRO B 49  ? 1.921 1.885 1.753 0.246  0.442  0.296  49  PRO LLL CB  
1989 C CG  . PRO B 49  ? 1.874 1.812 1.717 0.224  0.458  0.283  49  PRO LLL CG  
1990 C CD  . PRO B 49  ? 1.850 1.764 1.698 0.218  0.473  0.286  49  PRO LLL CD  
1991 N N   . PRO B 50  ? 1.637 1.629 1.460 0.235  0.384  0.269  50  PRO LLL N   
1992 C CA  . PRO B 50  ? 1.610 1.603 1.430 0.226  0.363  0.253  50  PRO LLL CA  
1993 C C   . PRO B 50  ? 1.575 1.567 1.391 0.224  0.357  0.245  50  PRO LLL C   
1994 O O   . PRO B 50  ? 1.813 1.819 1.632 0.233  0.364  0.251  50  PRO LLL O   
1995 C CB  . PRO B 50  ? 1.596 1.620 1.419 0.236  0.350  0.248  50  PRO LLL CB  
1996 C CG  . PRO B 50  ? 1.686 1.725 1.513 0.247  0.362  0.259  50  PRO LLL CG  
1997 C CD  . PRO B 50  ? 1.711 1.735 1.536 0.254  0.383  0.277  50  PRO LLL CD  
1998 N N   . LYS B 51  ? 1.537 1.515 1.347 0.215  0.347  0.234  51  LYS LLL N   
1999 C CA  . LYS B 51  ? 1.565 1.550 1.371 0.216  0.339  0.224  51  LYS LLL CA  
2000 C C   . LYS B 51  ? 1.685 1.672 1.484 0.221  0.320  0.216  51  LYS LLL C   
2001 O O   . LYS B 51  ? 1.827 1.794 1.619 0.217  0.315  0.214  51  LYS LLL O   
2002 C CB  . LYS B 51  ? 1.509 1.485 1.313 0.206  0.345  0.215  51  LYS LLL CB  
2003 C CG  . LYS B 51  ? 1.465 1.452 1.261 0.210  0.331  0.201  51  LYS LLL CG  
2004 C CD  . LYS B 51  ? 1.493 1.491 1.293 0.201  0.340  0.187  51  LYS LLL CD  
2005 C CE  . LYS B 51  ? 1.590 1.614 1.387 0.208  0.329  0.171  51  LYS LLL CE  
2006 N NZ  . LYS B 51  ? 1.611 1.658 1.420 0.197  0.340  0.151  51  LYS LLL NZ  
2007 N N   . LEU B 52  ? 1.702 1.709 1.502 0.230  0.312  0.210  52  LEU LLL N   
2008 C CA  . LEU B 52  ? 1.709 1.715 1.502 0.236  0.296  0.200  52  LEU LLL CA  
2009 C C   . LEU B 52  ? 1.698 1.688 1.478 0.236  0.290  0.194  52  LEU LLL C   
2010 O O   . LEU B 52  ? 1.610 1.614 1.389 0.236  0.293  0.190  52  LEU LLL O   
2011 C CB  . LEU B 52  ? 1.751 1.789 1.551 0.246  0.290  0.195  52  LEU LLL CB  
2012 C CG  . LEU B 52  ? 1.752 1.795 1.551 0.253  0.275  0.181  52  LEU LLL CG  
2013 C CD1 . LEU B 52  ? 1.781 1.819 1.588 0.249  0.274  0.175  52  LEU LLL CD1 
2014 C CD2 . LEU B 52  ? 1.697 1.777 1.501 0.264  0.270  0.176  52  LEU LLL CD2 
2015 N N   . LEU B 53  ? 1.661 1.624 1.429 0.238  0.286  0.193  53  LEU LLL N   
2016 C CA  . LEU B 53  ? 1.661 1.611 1.410 0.247  0.280  0.190  53  LEU LLL CA  
2017 C C   . LEU B 53  ? 1.695 1.637 1.438 0.259  0.270  0.183  53  LEU LLL C   
2018 O O   . LEU B 53  ? 1.733 1.689 1.466 0.272  0.261  0.177  53  LEU LLL O   
2019 C CB  . LEU B 53  ? 1.764 1.681 1.499 0.245  0.286  0.199  53  LEU LLL CB  
2020 C CG  . LEU B 53  ? 1.844 1.764 1.585 0.232  0.297  0.204  53  LEU LLL CG  
2021 C CD1 . LEU B 53  ? 1.870 1.758 1.600 0.228  0.304  0.214  53  LEU LLL CD1 
2022 C CD2 . LEU B 53  ? 1.779 1.725 1.520 0.233  0.298  0.197  53  LEU LLL CD2 
2023 N N   . ILE B 54  ? 1.695 1.619 1.446 0.256  0.271  0.181  54  ILE LLL N   
2024 C CA  . ILE B 54  ? 1.755 1.664 1.503 0.266  0.266  0.171  54  ILE LLL CA  
2025 C C   . ILE B 54  ? 1.777 1.711 1.549 0.259  0.263  0.158  54  ILE LLL C   
2026 O O   . ILE B 54  ? 1.642 1.584 1.429 0.247  0.270  0.158  54  ILE LLL O   
2027 C CB  . ILE B 54  ? 1.773 1.629 1.509 0.266  0.277  0.177  54  ILE LLL CB  
2028 C CG1 . ILE B 54  ? 1.735 1.572 1.443 0.276  0.280  0.192  54  ILE LLL CG1 
2029 C CG2 . ILE B 54  ? 1.750 1.583 1.485 0.276  0.276  0.166  54  ILE LLL CG2 
2030 C CD1 . ILE B 54  ? 1.682 1.543 1.373 0.297  0.269  0.191  54  ILE LLL CD1 
2031 N N   . TYR B 55  ? 1.859 1.810 1.634 0.270  0.253  0.145  55  TYR LLL N   
2032 C CA  . TYR B 55  ? 1.823 1.799 1.619 0.268  0.249  0.126  55  TYR LLL CA  
2033 C C   . TYR B 55  ? 1.818 1.769 1.612 0.277  0.247  0.112  55  TYR LLL C   
2034 O O   . TYR B 55  ? 1.963 1.883 1.736 0.290  0.247  0.120  55  TYR LLL O   
2035 C CB  . TYR B 55  ? 1.636 1.668 1.441 0.274  0.241  0.123  55  TYR LLL CB  
2036 C CG  . TYR B 55  ? 1.520 1.566 1.313 0.287  0.233  0.125  55  TYR LLL CG  
2037 C CD1 . TYR B 55  ? 1.594 1.650 1.379 0.286  0.236  0.138  55  TYR LLL CD1 
2038 C CD2 . TYR B 55  ? 1.513 1.566 1.304 0.300  0.223  0.111  55  TYR LLL CD2 
2039 C CE1 . TYR B 55  ? 1.619 1.695 1.397 0.295  0.231  0.136  55  TYR LLL CE1 
2040 C CE2 . TYR B 55  ? 1.623 1.696 1.404 0.311  0.215  0.110  55  TYR LLL CE2 
2041 C CZ  . TYR B 55  ? 1.618 1.705 1.394 0.308  0.219  0.122  55  TYR LLL CZ  
2042 O OH  . TYR B 55  ? 1.675 1.788 1.445 0.316  0.214  0.117  55  TYR LLL OH  
2043 N N   . TRP B 56  ? 1.820 1.786 1.637 0.272  0.247  0.090  56  TRP LLL N   
2044 C CA  . TRP B 56  ? 1.863 1.798 1.686 0.275  0.252  0.071  56  TRP LLL CA  
2045 C C   . TRP B 56  ? 1.891 1.753 1.699 0.272  0.269  0.083  56  TRP LLL C   
2046 O O   . TRP B 56  ? 1.890 1.712 1.685 0.286  0.273  0.082  56  TRP LLL O   
2047 C CB  . TRP B 56  ? 1.958 1.909 1.771 0.295  0.238  0.066  56  TRP LLL CB  
2048 C CG  . TRP B 56  ? 1.959 1.972 1.794 0.296  0.227  0.043  56  TRP LLL CG  
2049 C CD1 . TRP B 56  ? 1.999 2.048 1.862 0.283  0.229  0.022  56  TRP LLL CD1 
2050 C CD2 . TRP B 56  ? 1.934 1.986 1.765 0.312  0.213  0.038  56  TRP LLL CD2 
2051 N NE1 . TRP B 56  ? 2.079 2.188 1.953 0.293  0.216  0.006  56  TRP LLL NE1 
2052 C CE2 . TRP B 56  ? 1.980 2.090 1.835 0.310  0.207  0.016  56  TRP LLL CE2 
2053 C CE3 . TRP B 56  ? 1.912 1.963 1.721 0.330  0.204  0.047  56  TRP LLL CE3 
2054 C CZ2 . TRP B 56  ? 1.921 2.083 1.779 0.323  0.194  0.006  56  TRP LLL CZ2 
2055 C CZ3 . TRP B 56  ? 1.920 2.021 1.734 0.341  0.192  0.036  56  TRP LLL CZ3 
2056 C CH2 . TRP B 56  ? 1.930 2.083 1.767 0.338  0.187  0.017  56  TRP LLL CH2 
2057 N N   . ALA B 57  ? 1.960 1.807 1.768 0.257  0.280  0.095  57  ALA LLL N   
2058 C CA  . ALA B 57  ? 2.053 1.834 1.849 0.251  0.301  0.108  57  ALA LLL CA  
2059 C C   . ALA B 57  ? 2.003 1.753 1.760 0.273  0.300  0.136  57  ALA LLL C   
2060 O O   . ALA B 57  ? 2.054 1.771 1.796 0.269  0.313  0.154  57  ALA LLL O   
2061 C CB  . ALA B 57  ? 2.102 1.839 1.914 0.244  0.319  0.088  57  ALA LLL CB  
2062 N N   . SER B 58  ? 1.936 1.701 1.677 0.295  0.286  0.136  58  SER LLL N   
2063 C CA  . SER B 58  ? 1.953 1.692 1.657 0.323  0.285  0.155  58  SER LLL CA  
2064 C C   . SER B 58  ? 1.909 1.703 1.603 0.339  0.264  0.155  58  SER LLL C   
2065 O O   . SER B 58  ? 2.071 1.860 1.737 0.363  0.261  0.167  58  SER LLL O   
2066 C CB  . SER B 58  ? 2.073 1.757 1.769 0.339  0.298  0.152  58  SER LLL CB  
2067 O OG  . SER B 58  ? 2.054 1.764 1.750 0.358  0.283  0.139  58  SER LLL OG  
2068 N N   . THR B 59  ? 1.914 1.763 1.629 0.327  0.251  0.143  59  THR LLL N   
2069 C CA  . THR B 59  ? 1.829 1.729 1.538 0.339  0.235  0.141  59  THR LLL CA  
2070 C C   . THR B 59  ? 1.793 1.717 1.504 0.325  0.237  0.151  59  THR LLL C   
2071 O O   . THR B 59  ? 1.760 1.688 1.489 0.305  0.243  0.152  59  THR LLL O   
2072 C CB  . THR B 59  ? 1.789 1.731 1.518 0.338  0.224  0.122  59  THR LLL CB  
2073 O OG1 . THR B 59  ? 1.748 1.666 1.476 0.352  0.223  0.111  59  THR LLL OG1 
2074 C CG2 . THR B 59  ? 1.770 1.764 1.496 0.346  0.212  0.119  59  THR LLL CG2 
2075 N N   . ARG B 60  ? 1.825 1.767 1.519 0.337  0.232  0.155  60  ARG LLL N   
2076 C CA  . ARG B 60  ? 1.832 1.795 1.529 0.324  0.237  0.160  60  ARG LLL CA  
2077 C C   . ARG B 60  ? 1.730 1.739 1.450 0.311  0.234  0.150  60  ARG LLL C   
2078 O O   . ARG B 60  ? 1.877 1.910 1.599 0.320  0.225  0.139  60  ARG LLL O   
2079 C CB  . ARG B 60  ? 1.896 1.869 1.568 0.342  0.234  0.162  60  ARG LLL CB  
2080 C CG  . ARG B 60  ? 1.860 1.839 1.530 0.331  0.242  0.167  60  ARG LLL CG  
2081 C CD  . ARG B 60  ? 1.863 1.876 1.514 0.349  0.237  0.161  60  ARG LLL CD  
2082 N NE  . ARG B 60  ? 1.894 1.911 1.520 0.382  0.227  0.160  60  ARG LLL NE  
2083 C CZ  . ARG B 60  ? 2.066 2.036 1.665 0.405  0.231  0.177  60  ARG LLL CZ  
2084 N NH1 . ARG B 60  ? 2.156 2.073 1.751 0.395  0.245  0.194  60  ARG LLL NH1 
2085 N NH2 . ARG B 60  ? 2.176 2.151 1.752 0.438  0.224  0.176  60  ARG LLL NH2 
2086 N N   . GLU B 61  ? 1.694 1.711 1.427 0.293  0.243  0.155  61  GLU LLL N   
2087 C CA  . GLU B 61  ? 1.765 1.817 1.517 0.282  0.248  0.151  61  GLU LLL CA  
2088 C C   . GLU B 61  ? 1.759 1.839 1.511 0.281  0.250  0.142  61  GLU LLL C   
2089 O O   . GLU B 61  ? 1.819 1.895 1.558 0.285  0.250  0.140  61  GLU LLL O   
2090 C CB  . GLU B 61  ? 1.840 1.881 1.605 0.268  0.260  0.163  61  GLU LLL CB  
2091 C CG  . GLU B 61  ? 1.989 2.055 1.770 0.259  0.272  0.166  61  GLU LLL CG  
2092 C CD  . GLU B 61  ? 2.103 2.198 1.893 0.265  0.270  0.164  61  GLU LLL CD  
2093 O OE1 . GLU B 61  ? 2.086 2.191 1.886 0.262  0.283  0.174  61  GLU LLL OE1 
2094 O OE2 . GLU B 61  ? 2.343 2.454 2.129 0.276  0.257  0.152  61  GLU LLL OE2 
2095 N N   . SER B 62  ? 1.803 1.917 1.570 0.276  0.255  0.133  62  SER LLL N   
2096 C CA  . SER B 62  ? 1.886 2.032 1.661 0.268  0.262  0.118  62  SER LLL CA  
2097 C C   . SER B 62  ? 1.842 1.974 1.621 0.253  0.276  0.121  62  SER LLL C   
2098 O O   . SER B 62  ? 1.689 1.793 1.474 0.244  0.287  0.137  62  SER LLL O   
2099 C CB  . SER B 62  ? 2.106 2.282 1.900 0.260  0.272  0.111  62  SER LLL CB  
2100 O OG  . SER B 62  ? 2.307 2.466 2.112 0.250  0.288  0.129  62  SER LLL OG  
2101 N N   . GLY B 63  ? 1.891 2.049 1.669 0.254  0.276  0.103  63  GLY LLL N   
2102 C CA  . GLY B 63  ? 1.918 2.077 1.705 0.238  0.291  0.097  63  GLY LLL CA  
2103 C C   . GLY B 63  ? 1.825 1.948 1.594 0.242  0.288  0.113  63  GLY LLL C   
2104 O O   . GLY B 63  ? 1.537 1.648 1.317 0.226  0.303  0.115  63  GLY LLL O   
2105 N N   . VAL B 64  ? 1.743 1.848 1.488 0.263  0.272  0.124  64  VAL LLL N   
2106 C CA  . VAL B 64  ? 1.783 1.851 1.508 0.270  0.270  0.142  64  VAL LLL CA  
2107 C C   . VAL B 64  ? 1.912 1.998 1.611 0.293  0.260  0.136  64  VAL LLL C   
2108 O O   . VAL B 64  ? 1.788 1.893 1.476 0.313  0.248  0.128  64  VAL LLL O   
2109 C CB  . VAL B 64  ? 1.729 1.756 1.448 0.274  0.266  0.159  64  VAL LLL CB  
2110 C CG1 . VAL B 64  ? 1.777 1.765 1.477 0.281  0.268  0.174  64  VAL LLL CG1 
2111 C CG2 . VAL B 64  ? 1.825 1.844 1.568 0.256  0.276  0.166  64  VAL LLL CG2 
2112 N N   . PRO B 65  ? 1.932 2.016 1.619 0.296  0.265  0.139  65  PRO LLL N   
2113 C CA  . PRO B 65  ? 1.848 1.959 1.507 0.323  0.256  0.134  65  PRO LLL CA  
2114 C C   . PRO B 65  ? 1.944 2.015 1.570 0.352  0.249  0.155  65  PRO LLL C   
2115 O O   . PRO B 65  ? 1.776 1.795 1.404 0.344  0.255  0.173  65  PRO LLL O   
2116 C CB  . PRO B 65  ? 1.904 2.014 1.558 0.317  0.265  0.137  65  PRO LLL CB  
2117 C CG  . PRO B 65  ? 1.898 1.994 1.586 0.282  0.279  0.134  65  PRO LLL CG  
2118 C CD  . PRO B 65  ? 1.884 1.944 1.581 0.275  0.278  0.147  65  PRO LLL CD  
2119 N N   . ASP B 66  ? 2.167 2.270 1.767 0.385  0.240  0.150  66  ASP LLL N   
2120 C CA  . ASP B 66  ? 2.226 2.299 1.790 0.421  0.235  0.168  66  ASP LLL CA  
2121 C C   . ASP B 66  ? 2.125 2.127 1.669 0.425  0.249  0.199  66  ASP LLL C   
2122 O O   . ASP B 66  ? 2.023 1.973 1.556 0.435  0.253  0.214  66  ASP LLL O   
2123 C CB  . ASP B 66  ? 2.510 2.644 2.048 0.459  0.225  0.156  66  ASP LLL CB  
2124 C CG  . ASP B 66  ? 2.911 3.091 2.443 0.460  0.227  0.146  66  ASP LLL CG  
2125 O OD1 . ASP B 66  ? 3.167 3.327 2.665 0.485  0.233  0.168  66  ASP LLL OD1 
2126 O OD2 . ASP B 66  ? 3.239 3.474 2.803 0.436  0.226  0.116  66  ASP LLL OD2 
2127 N N   . ARG B 67  ? 2.021 2.023 1.562 0.415  0.258  0.205  67  ARG LLL N   
2128 C CA  . ARG B 67  ? 2.035 1.981 1.552 0.422  0.273  0.233  67  ARG LLL CA  
2129 C C   . ARG B 67  ? 1.993 1.873 1.529 0.395  0.285  0.245  67  ARG LLL C   
2130 O O   . ARG B 67  ? 2.023 1.844 1.539 0.403  0.300  0.268  67  ARG LLL O   
2131 C CB  . ARG B 67  ? 2.072 2.047 1.588 0.413  0.278  0.230  67  ARG LLL CB  
2132 C CG  . ARG B 67  ? 1.958 1.963 1.516 0.374  0.277  0.207  67  ARG LLL CG  
2133 C CD  . ARG B 67  ? 1.988 2.005 1.544 0.366  0.286  0.209  67  ARG LLL CD  
2134 N NE  . ARG B 67  ? 1.916 1.958 1.510 0.332  0.289  0.188  67  ARG LLL NE  
2135 C CZ  . ARG B 67  ? 1.905 2.007 1.519 0.324  0.284  0.157  67  ARG LLL CZ  
2136 N NH1 . ARG B 67  ? 2.007 2.161 1.609 0.348  0.273  0.140  67  ARG LLL NH1 
2137 N NH2 . ARG B 67  ? 1.809 1.921 1.458 0.293  0.294  0.142  67  ARG LLL NH2 
2138 N N   . PHE B 68  ? 1.898 1.790 1.472 0.365  0.279  0.229  68  PHE LLL N   
2139 C CA  . PHE B 68  ? 1.733 1.584 1.331 0.340  0.287  0.233  68  PHE LLL CA  
2140 C C   . PHE B 68  ? 1.734 1.557 1.327 0.354  0.284  0.233  68  PHE LLL C   
2141 O O   . PHE B 68  ? 1.736 1.589 1.328 0.368  0.271  0.222  68  PHE LLL O   
2142 C CB  . PHE B 68  ? 1.620 1.503 1.254 0.313  0.281  0.216  68  PHE LLL CB  
2143 C CG  . PHE B 68  ? 1.641 1.533 1.286 0.293  0.289  0.217  68  PHE LLL CG  
2144 C CD1 . PHE B 68  ? 1.647 1.584 1.296 0.292  0.287  0.205  68  PHE LLL CD1 
2145 C CD2 . PHE B 68  ? 1.663 1.520 1.317 0.276  0.301  0.228  68  PHE LLL CD2 
2146 C CE1 . PHE B 68  ? 1.663 1.604 1.323 0.274  0.296  0.204  68  PHE LLL CE1 
2147 C CE2 . PHE B 68  ? 1.691 1.557 1.354 0.260  0.309  0.229  68  PHE LLL CE2 
2148 C CZ  . PHE B 68  ? 1.717 1.622 1.383 0.260  0.306  0.218  68  PHE LLL CZ  
2149 N N   . SER B 69  ? 1.871 1.638 1.463 0.349  0.299  0.244  69  SER LLL N   
2150 C CA  . SER B 69  ? 2.115 1.848 1.703 0.363  0.301  0.244  69  SER LLL CA  
2151 C C   . SER B 69  ? 2.241 1.931 1.853 0.336  0.316  0.241  69  SER LLL C   
2152 O O   . SER B 69  ? 2.647 2.307 2.257 0.324  0.333  0.252  69  SER LLL O   
2153 C CB  . SER B 69  ? 2.350 2.052 1.896 0.399  0.310  0.263  69  SER LLL CB  
2154 O OG  . SER B 69  ? 2.770 2.411 2.311 0.408  0.325  0.269  69  SER LLL OG  
2155 N N   . GLY B 70  ? 2.131 1.827 1.769 0.327  0.310  0.223  70  GLY LLL N   
2156 C CA  . GLY B 70  ? 2.106 1.775 1.773 0.302  0.323  0.211  70  GLY LLL CA  
2157 C C   . GLY B 70  ? 2.113 1.732 1.776 0.314  0.336  0.208  70  GLY LLL C   
2158 O O   . GLY B 70  ? 1.978 1.604 1.624 0.340  0.326  0.207  70  GLY LLL O   
2159 N N   . SER B 71  ? 2.131 1.702 1.809 0.296  0.360  0.203  71  SER LLL N   
2160 C CA  . SER B 71  ? 2.224 1.736 1.903 0.303  0.380  0.197  71  SER LLL CA  
2161 C C   . SER B 71  ? 2.160 1.651 1.879 0.268  0.400  0.173  71  SER LLL C   
2162 O O   . SER B 71  ? 2.044 1.580 1.789 0.242  0.393  0.161  71  SER LLL O   
2163 C CB  . SER B 71  ? 2.420 1.868 2.055 0.333  0.400  0.228  71  SER LLL CB  
2164 O OG  . SER B 71  ? 2.607 2.039 2.228 0.325  0.414  0.249  71  SER LLL OG  
2165 N N   . GLY B 72  ? 2.221 1.652 1.948 0.267  0.426  0.164  72  GLY LLL N   
2166 C CA  . GLY B 72  ? 2.262 1.675 2.034 0.232  0.449  0.133  72  GLY LLL CA  
2167 C C   . GLY B 72  ? 2.239 1.680 2.044 0.227  0.440  0.094  72  GLY LLL C   
2168 O O   . GLY B 72  ? 2.129 1.613 1.923 0.248  0.411  0.094  72  GLY LLL O   
2169 N N   . SER B 73  ? 2.349 1.768 2.195 0.198  0.465  0.060  73  SER LLL N   
2170 C CA  . SER B 73  ? 2.420 1.876 2.308 0.186  0.459  0.013  73  SER LLL CA  
2171 C C   . SER B 73  ? 2.536 2.001 2.477 0.144  0.483  -0.028 73  SER LLL C   
2172 O O   . SER B 73  ? 2.642 2.054 2.584 0.126  0.514  -0.017 73  SER LLL O   
2173 C CB  . SER B 73  ? 2.474 1.873 2.353 0.208  0.472  0.011  73  SER LLL CB  
2174 O OG  . SER B 73  ? 2.381 1.827 2.301 0.197  0.462  -0.037 73  SER LLL OG  
2175 N N   . GLY B 74  ? 2.647 2.185 2.632 0.129  0.469  -0.075 74  GLY LLL N   
2176 C CA  . GLY B 74  ? 2.686 2.256 2.729 0.089  0.487  -0.127 74  GLY LLL CA  
2177 C C   . GLY B 74  ? 2.642 2.274 2.695 0.071  0.477  -0.127 74  GLY LLL C   
2178 O O   . GLY B 74  ? 2.548 2.278 2.614 0.075  0.446  -0.142 74  GLY LLL O   
2179 N N   . THR B 75  ? 2.678 2.255 2.726 0.055  0.505  -0.109 75  THR LLL N   
2180 C CA  . THR B 75  ? 2.631 2.255 2.700 0.030  0.508  -0.119 75  THR LLL CA  
2181 C C   . THR B 75  ? 2.563 2.147 2.585 0.043  0.507  -0.063 75  THR LLL C   
2182 O O   . THR B 75  ? 2.444 2.083 2.469 0.036  0.494  -0.059 75  THR LLL O   
2183 C CB  . THR B 75  ? 2.778 2.374 2.897 -0.011 0.551  -0.162 75  THR LLL CB  
2184 O OG1 . THR B 75  ? 2.918 2.537 3.077 -0.020 0.555  -0.214 75  THR LLL OG1 
2185 C CG2 . THR B 75  ? 2.755 2.422 2.908 -0.039 0.551  -0.188 75  THR LLL CG2 
2186 N N   . ASP B 76  ? 2.600 2.094 2.580 0.063  0.523  -0.024 76  ASP LLL N   
2187 C CA  . ASP B 76  ? 2.690 2.145 2.623 0.078  0.525  0.028  76  ASP LLL CA  
2188 C C   . ASP B 76  ? 2.631 2.097 2.518 0.118  0.493  0.062  76  ASP LLL C   
2189 O O   . ASP B 76  ? 2.571 2.009 2.448 0.138  0.492  0.062  76  ASP LLL O   
2190 C CB  . ASP B 76  ? 2.855 2.204 2.775 0.074  0.572  0.046  76  ASP LLL CB  
2191 C CG  . ASP B 76  ? 2.991 2.328 2.963 0.030  0.609  0.004  76  ASP LLL CG  
2192 O OD1 . ASP B 76  ? 3.079 2.400 3.086 0.016  0.626  -0.034 76  ASP LLL OD1 
2193 O OD2 . ASP B 76  ? 3.022 2.372 3.003 0.009  0.620  0.007  76  ASP LLL OD2 
2194 N N   . PHE B 77  ? 2.590 2.098 2.456 0.128  0.469  0.086  77  PHE LLL N   
2195 C CA  . PHE B 77  ? 2.606 2.130 2.430 0.162  0.441  0.118  77  PHE LLL CA  
2196 C C   . PHE B 77  ? 2.591 2.100 2.383 0.169  0.444  0.154  77  PHE LLL C   
2197 O O   . PHE B 77  ? 2.635 2.142 2.441 0.146  0.459  0.151  77  PHE LLL O   
2198 C CB  . PHE B 77  ? 2.658 2.269 2.498 0.165  0.406  0.101  77  PHE LLL CB  
2199 C CG  . PHE B 77  ? 2.661 2.303 2.537 0.157  0.402  0.062  77  PHE LLL CG  
2200 C CD1 . PHE B 77  ? 2.666 2.305 2.532 0.179  0.390  0.059  77  PHE LLL CD1 
2201 C CD2 . PHE B 77  ? 2.667 2.347 2.587 0.129  0.409  0.024  77  PHE LLL CD2 
2202 C CE1 . PHE B 77  ? 2.614 2.283 2.513 0.172  0.386  0.021  77  PHE LLL CE1 
2203 C CE2 . PHE B 77  ? 2.654 2.371 2.609 0.123  0.405  -0.016 77  PHE LLL CE2 
2204 C CZ  . PHE B 77  ? 2.626 2.335 2.570 0.144  0.394  -0.017 77  PHE LLL CZ  
2205 N N   . THR B 78  ? 2.566 2.068 2.316 0.200  0.431  0.183  78  THR LLL N   
2206 C CA  . THR B 78  ? 2.517 2.013 2.233 0.212  0.430  0.215  78  THR LLL CA  
2207 C C   . THR B 78  ? 2.378 1.928 2.075 0.234  0.398  0.223  78  THR LLL C   
2208 O O   . THR B 78  ? 2.403 1.967 2.098 0.250  0.384  0.215  78  THR LLL O   
2209 C CB  . THR B 78  ? 2.673 2.092 2.353 0.231  0.459  0.243  78  THR LLL CB  
2210 O OG1 . THR B 78  ? 2.734 2.147 2.384 0.267  0.447  0.254  78  THR LLL OG1 
2211 C CG2 . THR B 78  ? 2.691 2.046 2.392 0.211  0.496  0.231  78  THR LLL CG2 
2212 N N   . LEU B 79  ? 2.273 1.853 1.960 0.232  0.390  0.235  79  LEU LLL N   
2213 C CA  . LEU B 79  ? 2.229 1.854 1.898 0.252  0.366  0.243  79  LEU LLL CA  
2214 C C   . LEU B 79  ? 2.307 1.916 1.940 0.268  0.374  0.268  79  LEU LLL C   
2215 O O   . LEU B 79  ? 2.380 1.989 2.018 0.252  0.383  0.273  79  LEU LLL O   
2216 C CB  . LEU B 79  ? 2.055 1.739 1.749 0.235  0.350  0.230  79  LEU LLL CB  
2217 C CG  . LEU B 79  ? 1.977 1.700 1.657 0.245  0.336  0.238  79  LEU LLL CG  
2218 C CD1 . LEU B 79  ? 1.984 1.736 1.659 0.263  0.318  0.230  79  LEU LLL CD1 
2219 C CD2 . LEU B 79  ? 2.022 1.781 1.726 0.226  0.333  0.232  79  LEU LLL CD2 
2220 N N   . THR B 80  ? 2.348 1.952 1.948 0.300  0.370  0.280  80  THR LLL N   
2221 C CA  . THR B 80  ? 2.321 1.913 1.880 0.324  0.378  0.304  80  THR LLL CA  
2222 C C   . THR B 80  ? 2.143 1.801 1.693 0.339  0.355  0.299  80  THR LLL C   
2223 O O   . THR B 80  ? 1.945 1.631 1.492 0.356  0.339  0.289  80  THR LLL O   
2224 C CB  . THR B 80  ? 2.500 2.032 2.028 0.353  0.397  0.323  80  THR LLL CB  
2225 O OG1 . THR B 80  ? 2.507 2.070 2.020 0.382  0.377  0.318  80  THR LLL OG1 
2226 C CG2 . THR B 80  ? 2.628 2.101 2.179 0.333  0.419  0.317  80  THR LLL CG2 
2227 N N   . ILE B 81  ? 2.183 1.866 1.730 0.331  0.355  0.302  81  ILE LLL N   
2228 C CA  . ILE B 81  ? 2.212 1.957 1.752 0.343  0.339  0.293  81  ILE LLL CA  
2229 C C   . ILE B 81  ? 2.324 2.067 1.818 0.379  0.346  0.313  81  ILE LLL C   
2230 O O   . ILE B 81  ? 2.466 2.200 1.949 0.375  0.358  0.325  81  ILE LLL O   
2231 C CB  . ILE B 81  ? 2.231 2.003 1.796 0.314  0.339  0.284  81  ILE LLL CB  
2232 C CG1 . ILE B 81  ? 2.216 1.978 1.819 0.281  0.340  0.273  81  ILE LLL CG1 
2233 C CG2 . ILE B 81  ? 2.188 2.024 1.755 0.319  0.325  0.267  81  ILE LLL CG2 
2234 C CD1 . ILE B 81  ? 2.162 1.940 1.786 0.257  0.344  0.269  81  ILE LLL CD1 
2235 N N   . SER B 82  ? 2.397 2.152 1.864 0.415  0.338  0.316  82  SER LLL N   
2236 C CA  . SER B 82  ? 2.385 2.162 1.806 0.458  0.340  0.331  82  SER LLL CA  
2237 C C   . SER B 82  ? 2.389 2.245 1.818 0.452  0.326  0.310  82  SER LLL C   
2238 O O   . SER B 82  ? 2.441 2.338 1.907 0.427  0.312  0.282  82  SER LLL O   
2239 C CB  . SER B 82  ? 2.356 2.142 1.748 0.500  0.332  0.335  82  SER LLL CB  
2240 O OG  . SER B 82  ? 2.520 2.232 1.909 0.503  0.347  0.350  82  SER LLL OG  
2241 N N   . SER B 83  ? 2.479 2.356 1.876 0.476  0.332  0.322  83  SER LLL N   
2242 C CA  . SER B 83  ? 2.448 2.410 1.850 0.478  0.320  0.298  83  SER LLL CA  
2243 C C   . SER B 83  ? 2.215 2.186 1.665 0.428  0.319  0.276  83  SER LLL C   
2244 O O   . SER B 83  ? 2.069 2.091 1.550 0.412  0.305  0.244  83  SER LLL O   
2245 C CB  . SER B 83  ? 2.627 2.659 2.025 0.502  0.300  0.273  83  SER LLL CB  
2246 O OG  . SER B 83  ? 2.706 2.817 2.132 0.484  0.289  0.237  83  SER LLL OG  
2247 N N   . LEU B 84  ? 2.183 2.105 1.641 0.405  0.334  0.292  84  LEU LLL N   
2248 C CA  . LEU B 84  ? 2.105 2.031 1.606 0.361  0.335  0.274  84  LEU LLL CA  
2249 C C   . LEU B 84  ? 2.075 2.078 1.590 0.358  0.326  0.244  84  LEU LLL C   
2250 O O   . LEU B 84  ? 2.233 2.281 1.720 0.387  0.322  0.241  84  LEU LLL O   
2251 C CB  . LEU B 84  ? 2.074 1.954 1.574 0.345  0.353  0.294  84  LEU LLL CB  
2252 C CG  . LEU B 84  ? 2.020 1.896 1.563 0.305  0.355  0.280  84  LEU LLL CG  
2253 C CD1 . LEU B 84  ? 2.108 1.965 1.680 0.288  0.349  0.273  84  LEU LLL CD1 
2254 C CD2 . LEU B 84  ? 2.060 1.896 1.601 0.291  0.373  0.298  84  LEU LLL CD2 
2255 N N   . GLN B 85  ? 2.000 2.017 1.557 0.325  0.323  0.221  85  GLN LLL N   
2256 C CA  . GLN B 85  ? 2.019 2.104 1.597 0.317  0.320  0.187  85  GLN LLL CA  
2257 C C   . GLN B 85  ? 1.947 2.019 1.558 0.282  0.331  0.180  85  GLN LLL C   
2258 O O   . GLN B 85  ? 1.900 1.916 1.517 0.267  0.338  0.202  85  GLN LLL O   
2259 C CB  . GLN B 85  ? 2.081 2.204 1.679 0.315  0.309  0.162  85  GLN LLL CB  
2260 C CG  . GLN B 85  ? 2.270 2.476 1.868 0.328  0.302  0.128  85  GLN LLL CG  
2261 C CD  . GLN B 85  ? 2.446 2.678 1.997 0.374  0.292  0.140  85  GLN LLL CD  
2262 O OE1 . GLN B 85  ? 2.556 2.791 2.095 0.393  0.283  0.142  85  GLN LLL OE1 
2263 N NE2 . GLN B 85  ? 2.548 2.801 2.071 0.395  0.296  0.148  85  GLN LLL NE2 
2264 N N   . ALA B 86  ? 1.856 1.981 1.488 0.272  0.333  0.149  86  ALA LLL N   
2265 C CA  . ALA B 86  ? 2.000 2.117 1.666 0.240  0.346  0.137  86  ALA LLL CA  
2266 C C   . ALA B 86  ? 2.027 2.097 1.719 0.219  0.351  0.146  86  ALA LLL C   
2267 O O   . ALA B 86  ? 1.906 1.929 1.600 0.209  0.357  0.169  86  ALA LLL O   
2268 C CB  . ALA B 86  ? 2.028 2.210 1.720 0.231  0.349  0.095  86  ALA LLL CB  
2269 N N   . GLU B 87  ? 2.072 2.163 1.783 0.215  0.347  0.129  87  GLU LLL N   
2270 C CA  . GLU B 87  ? 2.099 2.161 1.836 0.197  0.353  0.131  87  GLU LLL CA  
2271 C C   . GLU B 87  ? 1.992 2.011 1.714 0.205  0.345  0.160  87  GLU LLL C   
2272 O O   . GLU B 87  ? 2.140 2.145 1.879 0.197  0.347  0.162  87  GLU LLL O   
2273 C CB  . GLU B 87  ? 2.279 2.381 2.039 0.191  0.354  0.102  87  GLU LLL CB  
2274 C CG  . GLU B 87  ? 2.486 2.608 2.227 0.211  0.337  0.101  87  GLU LLL CG  
2275 C CD  . GLU B 87  ? 2.638 2.810 2.401 0.205  0.337  0.068  87  GLU LLL CD  
2276 O OE1 . GLU B 87  ? 2.697 2.858 2.491 0.184  0.351  0.059  87  GLU LLL OE1 
2277 O OE2 . GLU B 87  ? 2.749 2.973 2.498 0.224  0.325  0.050  87  GLU LLL OE2 
2278 N N   . ASP B 88  ? 1.893 1.890 1.585 0.221  0.340  0.181  88  ASP LLL N   
2279 C CA  . ASP B 88  ? 1.893 1.844 1.576 0.224  0.337  0.204  88  ASP LLL CA  
2280 C C   . ASP B 88  ? 1.928 1.847 1.622 0.208  0.348  0.217  88  ASP LLL C   
2281 O O   . ASP B 88  ? 1.834 1.724 1.532 0.204  0.348  0.229  88  ASP LLL O   
2282 C CB  . ASP B 88  ? 1.906 1.844 1.554 0.249  0.331  0.219  88  ASP LLL CB  
2283 C CG  . ASP B 88  ? 1.906 1.870 1.546 0.267  0.318  0.208  88  ASP LLL CG  
2284 O OD1 . ASP B 88  ? 1.874 1.854 1.539 0.255  0.315  0.194  88  ASP LLL OD1 
2285 O OD2 . ASP B 88  ? 1.913 1.882 1.521 0.294  0.313  0.215  88  ASP LLL OD2 
2286 N N   . VAL B 89  ? 1.980 1.908 1.680 0.199  0.357  0.213  89  VAL LLL N   
2287 C CA  . VAL B 89  ? 2.164 2.066 1.871 0.186  0.367  0.226  89  VAL LLL CA  
2288 C C   . VAL B 89  ? 2.080 1.973 1.814 0.174  0.371  0.226  89  VAL LLL C   
2289 O O   . VAL B 89  ? 1.861 1.770 1.614 0.167  0.376  0.215  89  VAL LLL O   
2290 C CB  . VAL B 89  ? 2.349 2.267 2.056 0.181  0.376  0.220  89  VAL LLL CB  
2291 C CG1 . VAL B 89  ? 2.402 2.330 2.077 0.199  0.374  0.224  89  VAL LLL CG1 
2292 C CG2 . VAL B 89  ? 2.476 2.422 2.207 0.171  0.382  0.197  89  VAL LLL CG2 
2293 N N   . ALA B 90  ? 2.040 1.911 1.776 0.172  0.370  0.238  90  ALA LLL N   
2294 C CA  . ALA B 90  ? 1.974 1.845 1.730 0.167  0.370  0.238  90  ALA LLL CA  
2295 C C   . ALA B 90  ? 1.896 1.753 1.655 0.163  0.370  0.245  90  ALA LLL C   
2296 O O   . ALA B 90  ? 2.004 1.842 1.749 0.162  0.373  0.250  90  ALA LLL O   
2297 C CB  . ALA B 90  ? 2.068 1.952 1.829 0.173  0.363  0.232  90  ALA LLL CB  
2298 N N   . VAL B 91  ? 1.817 1.685 1.593 0.162  0.369  0.243  91  VAL LLL N   
2299 C CA  . VAL B 91  ? 1.818 1.684 1.602 0.158  0.367  0.240  91  VAL LLL CA  
2300 C C   . VAL B 91  ? 1.864 1.733 1.648 0.166  0.357  0.235  91  VAL LLL C   
2301 O O   . VAL B 91  ? 1.865 1.751 1.652 0.174  0.351  0.234  91  VAL LLL O   
2302 C CB  . VAL B 91  ? 1.825 1.716 1.629 0.156  0.371  0.238  91  VAL LLL CB  
2303 C CG1 . VAL B 91  ? 1.802 1.698 1.618 0.147  0.373  0.228  91  VAL LLL CG1 
2304 C CG2 . VAL B 91  ? 1.916 1.809 1.722 0.153  0.382  0.243  91  VAL LLL CG2 
2305 N N   . TYR B 92  ? 1.850 1.701 1.631 0.163  0.357  0.230  92  TYR LLL N   
2306 C CA  . TYR B 92  ? 1.807 1.655 1.587 0.170  0.348  0.224  92  TYR LLL CA  
2307 C C   . TYR B 92  ? 1.780 1.644 1.582 0.162  0.349  0.209  92  TYR LLL C   
2308 O O   . TYR B 92  ? 1.762 1.615 1.573 0.149  0.359  0.204  92  TYR LLL O   
2309 C CB  . TYR B 92  ? 1.776 1.586 1.530 0.177  0.350  0.231  92  TYR LLL CB  
2310 C CG  . TYR B 92  ? 1.751 1.565 1.485 0.188  0.345  0.239  92  TYR LLL CG  
2311 C CD1 . TYR B 92  ? 1.806 1.623 1.535 0.184  0.352  0.245  92  TYR LLL CD1 
2312 C CD2 . TYR B 92  ? 1.847 1.672 1.573 0.202  0.334  0.235  92  TYR LLL CD2 
2313 C CE1 . TYR B 92  ? 1.813 1.645 1.530 0.193  0.348  0.244  92  TYR LLL CE1 
2314 C CE2 . TYR B 92  ? 1.878 1.720 1.592 0.210  0.330  0.235  92  TYR LLL CE2 
2315 C CZ  . TYR B 92  ? 1.856 1.703 1.566 0.205  0.337  0.238  92  TYR LLL CZ  
2316 O OH  . TYR B 92  ? 1.937 1.809 1.639 0.213  0.334  0.232  92  TYR LLL OH  
2317 N N   . TYR B 93  ? 1.838 1.736 1.653 0.170  0.339  0.201  93  TYR LLL N   
2318 C CA  . TYR B 93  ? 1.886 1.813 1.723 0.166  0.337  0.182  93  TYR LLL CA  
2319 C C   . TYR B 93  ? 1.842 1.763 1.680 0.170  0.330  0.170  93  TYR LLL C   
2320 O O   . TYR B 93  ? 1.639 1.562 1.464 0.184  0.320  0.177  93  TYR LLL O   
2321 C CB  . TYR B 93  ? 1.867 1.848 1.717 0.175  0.333  0.181  93  TYR LLL CB  
2322 C CG  . TYR B 93  ? 1.801 1.790 1.652 0.174  0.341  0.192  93  TYR LLL CG  
2323 C CD1 . TYR B 93  ? 1.682 1.697 1.549 0.167  0.347  0.181  93  TYR LLL CD1 
2324 C CD2 . TYR B 93  ? 1.807 1.783 1.644 0.181  0.344  0.211  93  TYR LLL CD2 
2325 C CE1 . TYR B 93  ? 1.607 1.632 1.475 0.170  0.354  0.192  93  TYR LLL CE1 
2326 C CE2 . TYR B 93  ? 1.752 1.733 1.591 0.182  0.353  0.220  93  TYR LLL CE2 
2327 C CZ  . TYR B 93  ? 1.671 1.675 1.523 0.178  0.358  0.213  93  TYR LLL CZ  
2328 O OH  . TYR B 93  ? 1.574 1.581 1.425 0.182  0.367  0.224  93  TYR LLL OH  
2329 N N   . CYS B 94  ? 1.848 1.761 1.702 0.159  0.336  0.150  94  CYS LLL N   
2330 C CA  . CYS B 94  ? 2.019 1.937 1.882 0.163  0.330  0.132  94  CYS LLL CA  
2331 C C   . CYS B 94  ? 2.216 2.202 2.104 0.165  0.322  0.111  94  CYS LLL C   
2332 O O   . CYS B 94  ? 2.282 2.303 2.184 0.160  0.326  0.107  94  CYS LLL O   
2333 C CB  . CYS B 94  ? 2.096 1.966 1.964 0.149  0.345  0.120  94  CYS LLL CB  
2334 S SG  . CYS B 94  ? 2.237 2.126 2.141 0.122  0.363  0.092  94  CYS LLL SG  
2335 N N   . GLN B 95  ? 2.248 2.259 2.140 0.176  0.311  0.099  95  GLN LLL N   
2336 C CA  . GLN B 95  ? 2.017 2.103 1.928 0.186  0.300  0.082  95  GLN LLL CA  
2337 C C   . GLN B 95  ? 1.998 2.093 1.920 0.189  0.294  0.058  95  GLN LLL C   
2338 O O   . GLN B 95  ? 1.927 1.980 1.831 0.195  0.291  0.068  95  GLN LLL O   
2339 C CB  . GLN B 95  ? 2.028 2.141 1.922 0.207  0.292  0.107  95  GLN LLL CB  
2340 C CG  . GLN B 95  ? 2.069 2.260 1.976 0.224  0.285  0.096  95  GLN LLL CG  
2341 C CD  . GLN B 95  ? 1.978 2.189 1.871 0.244  0.276  0.108  95  GLN LLL CD  
2342 O OE1 . GLN B 95  ? 1.977 2.156 1.861 0.243  0.271  0.109  95  GLN LLL OE1 
2343 N NE2 . GLN B 95  ? 1.868 2.135 1.760 0.265  0.274  0.116  95  GLN LLL NE2 
2344 N N   . GLN B 96  ? 2.060 2.210 2.011 0.185  0.292  0.023  96  GLN LLL N   
2345 C CA  . GLN B 96  ? 2.020 2.195 1.986 0.189  0.285  -0.005 96  GLN LLL CA  
2346 C C   . GLN B 96  ? 2.072 2.328 2.037 0.213  0.269  -0.004 96  GLN LLL C   
2347 O O   . GLN B 96  ? 2.012 2.313 1.975 0.224  0.268  0.007  96  GLN LLL O   
2348 C CB  . GLN B 96  ? 1.989 2.176 1.994 0.166  0.296  -0.051 96  GLN LLL CB  
2349 C CG  . GLN B 96  ? 2.032 2.303 2.065 0.162  0.295  -0.078 96  GLN LLL CG  
2350 C CD  . GLN B 96  ? 2.047 2.413 2.094 0.182  0.279  -0.102 96  GLN LLL CD  
2351 O OE1 . GLN B 96  ? 1.783 2.149 1.829 0.190  0.271  -0.111 96  GLN LLL OE1 
2352 N NE2 . GLN B 96  ? 2.204 2.654 2.261 0.194  0.274  -0.110 96  GLN LLL NE2 
2353 N N   . TYR B 97  ? 2.110 2.379 2.074 0.225  0.259  -0.014 97  TYR LLL N   
2354 C CA  . TYR B 97  ? 2.032 2.375 1.993 0.250  0.245  -0.014 97  TYR LLL CA  
2355 C C   . TYR B 97  ? 2.094 2.473 2.079 0.249  0.238  -0.056 97  TYR LLL C   
2356 O O   . TYR B 97  ? 2.030 2.453 2.009 0.268  0.226  -0.057 97  TYR LLL O   
2357 C CB  . TYR B 97  ? 1.951 2.268 1.880 0.266  0.241  0.026  97  TYR LLL CB  
2358 C CG  . TYR B 97  ? 1.937 2.181 1.850 0.259  0.241  0.035  97  TYR LLL CG  
2359 C CD1 . TYR B 97  ? 1.928 2.103 1.827 0.247  0.250  0.054  97  TYR LLL CD1 
2360 C CD2 . TYR B 97  ? 1.954 2.206 1.866 0.269  0.232  0.025  97  TYR LLL CD2 
2361 C CE1 . TYR B 97  ? 1.861 1.978 1.743 0.247  0.250  0.063  97  TYR LLL CE1 
2362 C CE2 . TYR B 97  ? 1.974 2.167 1.870 0.268  0.231  0.032  97  TYR LLL CE2 
2363 C CZ  . TYR B 97  ? 1.942 2.069 1.823 0.258  0.241  0.052  97  TYR LLL CZ  
2364 O OH  . TYR B 97  ? 2.247 2.326 2.109 0.263  0.239  0.060  97  TYR LLL OH  
2365 N N   . TYR B 98  ? 2.165 2.524 2.178 0.225  0.248  -0.091 98  TYR LLL N   
2366 C CA  . TYR B 98  ? 2.204 2.587 2.246 0.218  0.247  -0.137 98  TYR LLL CA  
2367 C C   . TYR B 98  ? 2.241 2.741 2.303 0.233  0.235  -0.166 98  TYR LLL C   
2368 O O   . TYR B 98  ? 2.323 2.872 2.389 0.250  0.223  -0.181 98  TYR LLL O   
2369 C CB  . TYR B 98  ? 2.218 2.546 2.288 0.186  0.268  -0.167 98  TYR LLL CB  
2370 C CG  . TYR B 98  ? 2.304 2.659 2.414 0.173  0.273  -0.223 98  TYR LLL CG  
2371 C CD1 . TYR B 98  ? 2.400 2.710 2.506 0.177  0.273  -0.230 98  TYR LLL CD1 
2372 C CD2 . TYR B 98  ? 2.351 2.779 2.504 0.158  0.279  -0.273 98  TYR LLL CD2 
2373 C CE1 . TYR B 98  ? 2.385 2.718 2.531 0.165  0.280  -0.285 98  TYR LLL CE1 
2374 C CE2 . TYR B 98  ? 2.398 2.855 2.593 0.143  0.286  -0.332 98  TYR LLL CE2 
2375 C CZ  . TYR B 98  ? 2.380 2.787 2.572 0.146  0.287  -0.337 98  TYR LLL CZ  
2376 O OH  . TYR B 98  ? 2.523 2.956 2.759 0.131  0.296  -0.397 98  TYR LLL OH  
2377 N N   . SER B 99  ? 2.263 2.812 2.335 0.232  0.238  -0.169 99  SER LLL N   
2378 C CA  . SER B 99  ? 2.332 3.004 2.423 0.250  0.229  -0.197 99  SER LLL CA  
2379 C C   . SER B 99  ? 2.341 3.042 2.409 0.270  0.228  -0.159 99  SER LLL C   
2380 O O   . SER B 99  ? 2.428 3.059 2.483 0.257  0.238  -0.131 99  SER LLL O   
2381 C CB  . SER B 99  ? 2.434 3.146 2.574 0.224  0.238  -0.258 99  SER LLL CB  
2382 O OG  . SER B 99  ? 2.553 3.262 2.700 0.210  0.248  -0.254 99  SER LLL OG  
2383 N N   . THR B 100 ? 2.356 3.159 2.420 0.304  0.217  -0.160 100 THR LLL N   
2384 C CA  . THR B 100 ? 2.304 3.156 2.355 0.325  0.219  -0.139 100 THR LLL CA  
2385 C C   . THR B 100 ? 2.208 3.137 2.301 0.311  0.221  -0.193 100 THR LLL C   
2386 O O   . THR B 100 ? 2.300 3.293 2.428 0.302  0.217  -0.248 100 THR LLL O   
2387 C CB  . THR B 100 ? 2.295 3.216 2.316 0.373  0.211  -0.108 100 THR LLL CB  
2388 O OG1 . THR B 100 ? 2.359 3.395 2.403 0.390  0.200  -0.154 100 THR LLL OG1 
2389 C CG2 . THR B 100 ? 2.205 3.059 2.193 0.382  0.212  -0.064 100 THR LLL CG2 
2390 N N   . PRO B 101 ? 1.993 2.922 2.087 0.307  0.229  -0.184 101 PRO LLL N   
2391 C CA  . PRO B 101 ? 1.953 2.813 2.008 0.318  0.236  -0.122 101 PRO LLL CA  
2392 C C   . PRO B 101 ? 1.970 2.698 2.016 0.284  0.246  -0.100 101 PRO LLL C   
2393 O O   . PRO B 101 ? 2.024 2.717 2.096 0.249  0.254  -0.132 101 PRO LLL O   
2394 C CB  . PRO B 101 ? 1.996 2.911 2.063 0.322  0.241  -0.133 101 PRO LLL CB  
2395 C CG  . PRO B 101 ? 2.075 3.031 2.193 0.287  0.244  -0.201 101 PRO LLL CG  
2396 C CD  . PRO B 101 ? 1.992 2.992 2.127 0.290  0.234  -0.236 101 PRO LLL CD  
2397 N N   . TYR B 102 ? 2.007 2.669 2.015 0.296  0.248  -0.049 102 TYR LLL N   
2398 C CA  . TYR B 102 ? 2.000 2.547 1.992 0.272  0.257  -0.021 102 TYR LLL CA  
2399 C C   . TYR B 102 ? 2.028 2.554 2.030 0.254  0.269  -0.022 102 TYR LLL C   
2400 O O   . TYR B 102 ? 1.896 2.485 1.899 0.271  0.269  -0.020 102 TYR LLL O   
2401 C CB  . TYR B 102 ? 1.996 2.502 1.951 0.293  0.258  0.030  102 TYR LLL CB  
2402 C CG  . TYR B 102 ? 1.927 2.441 1.870 0.309  0.250  0.037  102 TYR LLL CG  
2403 C CD1 . TYR B 102 ? 1.941 2.418 1.854 0.323  0.254  0.078  102 TYR LLL CD1 
2404 C CD2 . TYR B 102 ? 1.794 2.351 1.756 0.308  0.239  0.000  102 TYR LLL CD2 
2405 C CE1 . TYR B 102 ? 1.912 2.397 1.814 0.336  0.248  0.085  102 TYR LLL CE1 
2406 C CE2 . TYR B 102 ? 1.808 2.373 1.757 0.323  0.231  0.007  102 TYR LLL CE2 
2407 C CZ  . TYR B 102 ? 1.832 2.361 1.752 0.337  0.236  0.050  102 TYR LLL CZ  
2408 O OH  . TYR B 102 ? 1.688 2.222 1.594 0.350  0.231  0.059  102 TYR LLL OH  
2409 N N   . THR B 103 ? 1.971 2.416 1.977 0.222  0.279  -0.023 103 THR LLL N   
2410 C CA  . THR B 103 ? 1.857 2.273 1.871 0.201  0.292  -0.024 103 THR LLL CA  
2411 C C   . THR B 103 ? 1.971 2.282 1.960 0.187  0.301  0.010  103 THR LLL C   
2412 O O   . THR B 103 ? 2.000 2.261 1.981 0.182  0.299  0.013  103 THR LLL O   
2413 C CB  . THR B 103 ? 1.725 2.179 1.782 0.176  0.299  -0.078 103 THR LLL CB  
2414 O OG1 . THR B 103 ? 1.788 2.210 1.852 0.154  0.314  -0.076 103 THR LLL OG1 
2415 C CG2 . THR B 103 ? 1.657 2.072 1.730 0.156  0.303  -0.104 103 THR LLL CG2 
2416 N N   . PHE B 104 ? 1.986 2.270 1.964 0.183  0.309  0.032  104 PHE LLL N   
2417 C CA  . PHE B 104 ? 2.038 2.235 1.993 0.171  0.318  0.062  104 PHE LLL CA  
2418 C C   . PHE B 104 ? 2.202 2.363 2.172 0.142  0.335  0.046  104 PHE LLL C   
2419 O O   . PHE B 104 ? 2.265 2.474 2.266 0.129  0.340  0.013  104 PHE LLL O   
2420 C CB  . PHE B 104 ? 1.977 2.170 1.910 0.186  0.319  0.097  104 PHE LLL CB  
2421 C CG  . PHE B 104 ? 1.965 2.171 1.879 0.212  0.311  0.120  104 PHE LLL CG  
2422 C CD1 . PHE B 104 ? 1.968 2.243 1.885 0.237  0.306  0.120  104 PHE LLL CD1 
2423 C CD2 . PHE B 104 ? 2.040 2.192 1.932 0.213  0.310  0.141  104 PHE LLL CD2 
2424 C CE1 . PHE B 104 ? 2.024 2.305 1.922 0.261  0.304  0.144  104 PHE LLL CE1 
2425 C CE2 . PHE B 104 ? 2.119 2.283 1.997 0.233  0.307  0.160  104 PHE LLL CE2 
2426 C CZ  . PHE B 104 ? 2.027 2.252 1.909 0.256  0.305  0.162  104 PHE LLL CZ  
2427 N N   . GLY B 105 ? 2.353 2.436 2.302 0.132  0.344  0.069  105 GLY LLL N   
2428 C CA  . GLY B 105 ? 2.251 2.292 2.205 0.108  0.363  0.068  105 GLY LLL CA  
2429 C C   . GLY B 105 ? 2.129 2.186 2.076 0.112  0.364  0.085  105 GLY LLL C   
2430 O O   . GLY B 105 ? 2.003 2.095 1.939 0.134  0.353  0.101  105 GLY LLL O   
2431 N N   . GLN B 106 ? 1.936 1.967 1.889 0.092  0.381  0.083  106 GLN LLL N   
2432 C CA  . GLN B 106 ? 1.998 2.043 1.945 0.094  0.384  0.098  106 GLN LLL CA  
2433 C C   . GLN B 106 ? 1.917 1.920 1.830 0.108  0.380  0.135  106 GLN LLL C   
2434 O O   . GLN B 106 ? 1.779 1.799 1.686 0.117  0.379  0.148  106 GLN LLL O   
2435 C CB  . GLN B 106 ? 2.261 2.288 2.223 0.068  0.405  0.085  106 GLN LLL CB  
2436 C CG  . GLN B 106 ? 2.541 2.484 2.481 0.056  0.420  0.104  106 GLN LLL CG  
2437 C CD  . GLN B 106 ? 2.786 2.694 2.740 0.039  0.434  0.084  106 GLN LLL CD  
2438 O OE1 . GLN B 106 ? 2.747 2.687 2.722 0.039  0.427  0.058  106 GLN LLL OE1 
2439 N NE2 . GLN B 106 ? 2.950 2.789 2.889 0.027  0.456  0.098  106 GLN LLL NE2 
2440 N N   . GLY B 107 ? 2.034 1.986 1.926 0.111  0.378  0.148  107 GLY LLL N   
2441 C CA  . GLY B 107 ? 2.096 2.013 1.958 0.123  0.375  0.176  107 GLY LLL CA  
2442 C C   . GLY B 107 ? 2.085 1.953 1.932 0.112  0.389  0.188  107 GLY LLL C   
2443 O O   . GLY B 107 ? 2.079 1.942 1.939 0.094  0.404  0.178  107 GLY LLL O   
2444 N N   . THR B 108 ? 2.061 1.896 1.880 0.122  0.387  0.208  108 THR LLL N   
2445 C CA  . THR B 108 ? 2.013 1.804 1.809 0.119  0.400  0.222  108 THR LLL CA  
2446 C C   . THR B 108 ? 2.047 1.842 1.824 0.130  0.394  0.238  108 THR LLL C   
2447 O O   . THR B 108 ? 1.958 1.762 1.726 0.143  0.382  0.241  108 THR LLL O   
2448 C CB  . THR B 108 ? 2.007 1.755 1.788 0.124  0.405  0.226  108 THR LLL CB  
2449 O OG1 . THR B 108 ? 1.956 1.693 1.759 0.107  0.418  0.208  108 THR LLL OG1 
2450 C CG2 . THR B 108 ? 2.137 1.843 1.885 0.131  0.417  0.247  108 THR LLL CG2 
2451 N N   . LYS B 109 ? 2.093 1.885 1.864 0.124  0.404  0.245  109 LYS LLL N   
2452 C CA  . LYS B 109 ? 2.004 1.801 1.758 0.134  0.401  0.255  109 LYS LLL CA  
2453 C C   . LYS B 109 ? 2.016 1.784 1.739 0.145  0.404  0.268  109 LYS LLL C   
2454 O O   . LYS B 109 ? 2.084 1.820 1.797 0.140  0.418  0.275  109 LYS LLL O   
2455 C CB  . LYS B 109 ? 2.005 1.815 1.767 0.125  0.409  0.256  109 LYS LLL CB  
2456 C CG  . LYS B 109 ? 2.108 1.952 1.889 0.126  0.404  0.250  109 LYS LLL CG  
2457 C CD  . LYS B 109 ? 2.241 2.095 2.024 0.124  0.412  0.252  109 LYS LLL CD  
2458 C CE  . LYS B 109 ? 2.471 2.331 2.265 0.112  0.422  0.249  109 LYS LLL CE  
2459 N NZ  . LYS B 109 ? 2.720 2.554 2.495 0.105  0.432  0.256  109 LYS LLL NZ  
2460 N N   . VAL B 110 ? 1.959 1.740 1.667 0.159  0.394  0.269  110 VAL LLL N   
2461 C CA  . VAL B 110 ? 2.006 1.776 1.682 0.176  0.395  0.280  110 VAL LLL CA  
2462 C C   . VAL B 110 ? 2.011 1.812 1.683 0.178  0.394  0.276  110 VAL LLL C   
2463 O O   . VAL B 110 ? 1.835 1.664 1.526 0.174  0.386  0.263  110 VAL LLL O   
2464 C CB  . VAL B 110 ? 1.974 1.742 1.636 0.194  0.384  0.279  110 VAL LLL CB  
2465 C CG1 . VAL B 110 ? 1.887 1.630 1.560 0.189  0.385  0.277  110 VAL LLL CG1 
2466 C CG2 . VAL B 110 ? 1.982 1.790 1.654 0.197  0.370  0.266  110 VAL LLL CG2 
2467 N N   . GLU B 111 ? 2.048 1.844 1.697 0.186  0.402  0.286  111 GLU LLL N   
2468 C CA  . GLU B 111 ? 2.152 1.983 1.797 0.189  0.401  0.278  111 GLU LLL CA  
2469 C C   . GLU B 111 ? 2.136 1.975 1.743 0.214  0.403  0.288  111 GLU LLL C   
2470 O O   . GLU B 111 ? 2.150 1.956 1.731 0.228  0.408  0.306  111 GLU LLL O   
2471 C CB  . GLU B 111 ? 2.331 2.162 1.992 0.171  0.413  0.278  111 GLU LLL CB  
2472 C CG  . GLU B 111 ? 2.608 2.411 2.249 0.171  0.428  0.295  111 GLU LLL CG  
2473 C CD  . GLU B 111 ? 2.788 2.591 2.449 0.151  0.439  0.293  111 GLU LLL CD  
2474 O OE1 . GLU B 111 ? 2.898 2.702 2.543 0.153  0.451  0.301  111 GLU LLL OE1 
2475 O OE2 . GLU B 111 ? 2.804 2.612 2.495 0.137  0.437  0.283  111 GLU LLL OE2 
2476 N N   . ILE B 112 ? 2.106 1.988 1.708 0.220  0.399  0.275  112 ILE LLL N   
2477 C CA  . ILE B 112 ? 2.254 2.161 1.818 0.249  0.399  0.281  112 ILE LLL CA  
2478 C C   . ILE B 112 ? 2.253 2.143 1.795 0.253  0.415  0.301  112 ILE LLL C   
2479 O O   . ILE B 112 ? 2.140 2.035 1.701 0.233  0.422  0.295  112 ILE LLL O   
2480 C CB  . ILE B 112 ? 2.327 2.300 1.902 0.253  0.388  0.251  112 ILE LLL CB  
2481 C CG1 . ILE B 112 ? 2.299 2.287 1.901 0.245  0.377  0.230  112 ILE LLL CG1 
2482 C CG2 . ILE B 112 ? 2.520 2.534 2.055 0.288  0.385  0.253  112 ILE LLL CG2 
2483 C CD1 . ILE B 112 ? 2.473 2.442 2.056 0.263  0.368  0.242  112 ILE LLL CD1 
2484 N N   . LYS B 113 ? 2.343 2.211 1.844 0.279  0.424  0.327  113 LYS LLL N   
2485 C CA  . LYS B 113 ? 2.357 2.210 1.827 0.290  0.443  0.350  113 LYS LLL CA  
2486 C C   . LYS B 113 ? 2.351 2.273 1.801 0.313  0.436  0.339  113 LYS LLL C   
2487 O O   . LYS B 113 ? 2.270 2.236 1.713 0.333  0.420  0.324  113 LYS LLL O   
2488 C CB  . LYS B 113 ? 2.366 2.167 1.797 0.315  0.459  0.384  113 LYS LLL CB  
2489 C CG  . LYS B 113 ? 2.446 2.212 1.851 0.319  0.486  0.412  113 LYS LLL CG  
2490 C CD  . LYS B 113 ? 2.613 2.324 1.975 0.349  0.507  0.447  113 LYS LLL CD  
2491 C CE  . LYS B 113 ? 2.726 2.409 2.053 0.361  0.537  0.479  113 LYS LLL CE  
2492 N NZ  . LYS B 113 ? 2.824 2.429 2.120 0.380  0.567  0.514  113 LYS LLL NZ  
2493 N N   . ARG B 114 ? 2.429 2.364 1.873 0.310  0.448  0.344  114 ARG LLL N   
2494 C CA  . ARG B 114 ? 2.513 2.522 1.946 0.326  0.441  0.325  114 ARG LLL CA  
2495 C C   . ARG B 114 ? 2.711 2.717 2.110 0.340  0.460  0.350  114 ARG LLL C   
2496 O O   . ARG B 114 ? 2.894 2.841 2.294 0.323  0.480  0.373  114 ARG LLL O   
2497 C CB  . ARG B 114 ? 2.373 2.415 1.856 0.293  0.431  0.286  114 ARG LLL CB  
2498 C CG  . ARG B 114 ? 2.321 2.444 1.807 0.302  0.425  0.256  114 ARG LLL CG  
2499 C CD  . ARG B 114 ? 2.279 2.408 1.805 0.269  0.430  0.234  114 ARG LLL CD  
2500 N NE  . ARG B 114 ? 2.372 2.564 1.887 0.282  0.432  0.219  114 ARG LLL NE  
2501 C CZ  . ARG B 114 ? 2.481 2.749 2.001 0.294  0.422  0.183  114 ARG LLL CZ  
2502 N NH1 . ARG B 114 ? 2.274 2.563 1.812 0.293  0.409  0.158  114 ARG LLL NH1 
2503 N NH2 . ARG B 114 ? 2.783 3.111 2.293 0.305  0.424  0.168  114 ARG LLL NH2 
2504 N N   . THR B 115 ? 2.735 2.808 2.105 0.371  0.456  0.344  115 THR LLL N   
2505 C CA  . THR B 115 ? 2.827 2.918 2.170 0.383  0.473  0.359  115 THR LLL CA  
2506 C C   . THR B 115 ? 2.730 2.809 2.116 0.340  0.478  0.343  115 THR LLL C   
2507 O O   . THR B 115 ? 2.626 2.725 2.059 0.313  0.464  0.307  115 THR LLL O   
2508 C CB  . THR B 115 ? 2.987 3.176 2.308 0.418  0.461  0.338  115 THR LLL CB  
2509 O OG1 . THR B 115 ? 3.091 3.333 2.459 0.394  0.440  0.287  115 THR LLL OG1 
2510 C CG2 . THR B 115 ? 3.101 3.310 2.368 0.471  0.458  0.359  115 THR LLL CG2 
2511 N N   . VAL B 116 ? 2.722 2.769 2.094 0.335  0.500  0.368  116 VAL LLL N   
2512 C CA  . VAL B 116 ? 2.555 2.598 1.966 0.297  0.506  0.353  116 VAL LLL CA  
2513 C C   . VAL B 116 ? 2.371 2.495 1.798 0.298  0.493  0.314  116 VAL LLL C   
2514 O O   . VAL B 116 ? 2.296 2.481 1.691 0.331  0.488  0.310  116 VAL LLL O   
2515 C CB  . VAL B 116 ? 2.537 2.537 1.930 0.290  0.534  0.383  116 VAL LLL CB  
2516 C CG1 . VAL B 116 ? 2.516 2.437 1.892 0.290  0.554  0.420  116 VAL LLL CG1 
2517 C CG2 . VAL B 116 ? 2.762 2.809 2.115 0.319  0.545  0.395  116 VAL LLL CG2 
2518 N N   . ALA B 117 ? 2.289 2.417 1.765 0.264  0.487  0.285  117 ALA LLL N   
2519 C CA  . ALA B 117 ? 2.345 2.539 1.846 0.258  0.480  0.246  117 ALA LLL CA  
2520 C C   . ALA B 117 ? 2.351 2.522 1.880 0.229  0.492  0.244  117 ALA LLL C   
2521 O O   . ALA B 117 ? 2.229 2.349 1.785 0.205  0.494  0.249  117 ALA LLL O   
2522 C CB  . ALA B 117 ? 2.381 2.602 1.917 0.248  0.464  0.208  117 ALA LLL CB  
2523 N N   . ALA B 118 ? 2.473 2.685 1.992 0.235  0.499  0.238  118 ALA LLL N   
2524 C CA  . ALA B 118 ? 2.421 2.623 1.965 0.211  0.511  0.233  118 ALA LLL CA  
2525 C C   . ALA B 118 ? 2.218 2.429 1.814 0.188  0.502  0.195  118 ALA LLL C   
2526 O O   . ALA B 118 ? 2.140 2.391 1.749 0.193  0.492  0.165  118 ALA LLL O   
2527 C CB  . ALA B 118 ? 2.514 2.766 2.034 0.226  0.520  0.233  118 ALA LLL CB  
2528 N N   . PRO B 119 ? 2.084 2.259 1.711 0.164  0.509  0.196  119 PRO LLL N   
2529 C CA  . PRO B 119 ? 2.068 2.249 1.740 0.147  0.506  0.164  119 PRO LLL CA  
2530 C C   . PRO B 119 ? 2.139 2.371 1.824 0.146  0.512  0.134  119 PRO LLL C   
2531 O O   . PRO B 119 ? 2.153 2.405 1.818 0.152  0.519  0.144  119 PRO LLL O   
2532 C CB  . PRO B 119 ? 2.008 2.141 1.700 0.129  0.513  0.180  119 PRO LLL CB  
2533 C CG  . PRO B 119 ? 1.996 2.110 1.657 0.131  0.523  0.212  119 PRO LLL CG  
2534 C CD  . PRO B 119 ? 2.029 2.157 1.648 0.154  0.521  0.227  119 PRO LLL CD  
2535 N N   . SER B 120 ? 2.172 2.425 1.892 0.138  0.510  0.096  120 SER LLL N   
2536 C CA  . SER B 120 ? 2.220 2.509 1.968 0.131  0.519  0.061  120 SER LLL CA  
2537 C C   . SER B 120 ? 2.242 2.485 2.021 0.115  0.529  0.065  120 SER LLL C   
2538 O O   . SER B 120 ? 2.109 2.316 1.912 0.107  0.530  0.062  120 SER LLL O   
2539 C CB  . SER B 120 ? 2.196 2.531 1.967 0.130  0.517  0.015  120 SER LLL CB  
2540 O OG  . SER B 120 ? 2.157 2.464 1.945 0.124  0.513  0.010  120 SER LLL OG  
2541 N N   . VAL B 121 ? 2.299 2.548 2.075 0.113  0.537  0.074  121 VAL LLL N   
2542 C CA  . VAL B 121 ? 2.229 2.442 2.029 0.103  0.545  0.081  121 VAL LLL CA  
2543 C C   . VAL B 121 ? 2.175 2.406 2.010 0.099  0.557  0.045  121 VAL LLL C   
2544 O O   . VAL B 121 ? 2.100 2.379 1.934 0.101  0.559  0.019  121 VAL LLL O   
2545 C CB  . VAL B 121 ? 2.290 2.500 2.069 0.103  0.549  0.108  121 VAL LLL CB  
2546 C CG1 . VAL B 121 ? 2.222 2.404 2.025 0.095  0.555  0.116  121 VAL LLL CG1 
2547 C CG2 . VAL B 121 ? 2.368 2.560 2.111 0.107  0.543  0.140  121 VAL LLL CG2 
2548 N N   . PHE B 122 ? 2.135 2.327 1.999 0.094  0.565  0.042  122 PHE LLL N   
2549 C CA  . PHE B 122 ? 2.128 2.321 2.025 0.092  0.581  0.016  122 PHE LLL CA  
2550 C C   . PHE B 122 ? 2.110 2.266 2.017 0.096  0.587  0.038  122 PHE LLL C   
2551 O O   . PHE B 122 ? 1.921 2.048 1.819 0.098  0.580  0.066  122 PHE LLL O   
2552 C CB  . PHE B 122 ? 2.191 2.375 2.119 0.086  0.592  -0.016 122 PHE LLL CB  
2553 C CG  . PHE B 122 ? 2.345 2.564 2.266 0.083  0.583  -0.037 122 PHE LLL CG  
2554 C CD1 . PHE B 122 ? 2.426 2.699 2.359 0.080  0.588  -0.080 122 PHE LLL CD1 
2555 C CD2 . PHE B 122 ? 2.464 2.667 2.368 0.085  0.570  -0.019 122 PHE LLL CD2 
2556 C CE1 . PHE B 122 ? 2.544 2.860 2.473 0.080  0.580  -0.104 122 PHE LLL CE1 
2557 C CE2 . PHE B 122 ? 2.423 2.665 2.322 0.085  0.562  -0.041 122 PHE LLL CE2 
2558 C CZ  . PHE B 122 ? 2.437 2.738 2.348 0.083  0.567  -0.084 122 PHE LLL CZ  
2559 N N   . ILE B 123 ? 2.306 2.471 2.232 0.098  0.600  0.024  123 ILE LLL N   
2560 C CA  . ILE B 123 ? 2.482 2.624 2.418 0.107  0.608  0.040  123 ILE LLL CA  
2561 C C   . ILE B 123 ? 2.531 2.647 2.500 0.113  0.629  0.019  123 ILE LLL C   
2562 O O   . ILE B 123 ? 2.569 2.701 2.554 0.107  0.640  -0.015 123 ILE LLL O   
2563 C CB  . ILE B 123 ? 2.479 2.656 2.404 0.108  0.605  0.046  123 ILE LLL CB  
2564 C CG1 . ILE B 123 ? 2.481 2.649 2.420 0.120  0.614  0.053  123 ILE LLL CG1 
2565 C CG2 . ILE B 123 ? 2.399 2.619 2.323 0.103  0.609  0.018  123 ILE LLL CG2 
2566 C CD1 . ILE B 123 ? 2.430 2.629 2.357 0.118  0.608  0.068  123 ILE LLL CD1 
2567 N N   . PHE B 124 ? 2.436 2.512 2.414 0.126  0.637  0.037  124 PHE LLL N   
2568 C CA  . PHE B 124 ? 2.446 2.486 2.452 0.138  0.663  0.026  124 PHE LLL CA  
2569 C C   . PHE B 124 ? 2.456 2.497 2.462 0.159  0.669  0.041  124 PHE LLL C   
2570 O O   . PHE B 124 ? 2.436 2.475 2.430 0.171  0.659  0.070  124 PHE LLL O   
2571 C CB  . PHE B 124 ? 2.382 2.373 2.395 0.141  0.672  0.037  124 PHE LLL CB  
2572 C CG  . PHE B 124 ? 2.361 2.357 2.374 0.122  0.666  0.019  124 PHE LLL CG  
2573 C CD1 . PHE B 124 ? 2.369 2.358 2.409 0.110  0.686  -0.018 124 PHE LLL CD1 
2574 C CD2 . PHE B 124 ? 2.353 2.365 2.341 0.115  0.641  0.036  124 PHE LLL CD2 
2575 C CE1 . PHE B 124 ? 2.354 2.359 2.396 0.092  0.679  -0.039 124 PHE LLL CE1 
2576 C CE2 . PHE B 124 ? 2.393 2.414 2.379 0.101  0.634  0.020  124 PHE LLL CE2 
2577 C CZ  . PHE B 124 ? 2.342 2.364 2.356 0.090  0.652  -0.018 124 PHE LLL CZ  
2578 N N   . PRO B 125 ? 2.348 2.399 2.371 0.164  0.685  0.020  125 PRO LLL N   
2579 C CA  . PRO B 125 ? 2.244 2.294 2.271 0.189  0.695  0.032  125 PRO LLL CA  
2580 C C   . PRO B 125 ? 2.245 2.240 2.281 0.213  0.716  0.049  125 PRO LLL C   
2581 O O   . PRO B 125 ? 2.428 2.382 2.473 0.206  0.728  0.046  125 PRO LLL O   
2582 C CB  . PRO B 125 ? 2.318 2.384 2.364 0.187  0.711  -0.001 125 PRO LLL CB  
2583 C CG  . PRO B 125 ? 2.350 2.407 2.412 0.164  0.719  -0.032 125 PRO LLL CG  
2584 C CD  . PRO B 125 ? 2.297 2.365 2.336 0.148  0.695  -0.019 125 PRO LLL CD  
2585 N N   . PRO B 126 ? 2.141 2.135 2.174 0.244  0.722  0.070  126 PRO LLL N   
2586 C CA  . PRO B 126 ? 2.263 2.206 2.297 0.274  0.742  0.093  126 PRO LLL CA  
2587 C C   . PRO B 126 ? 2.444 2.327 2.503 0.279  0.781  0.077  126 PRO LLL C   
2588 O O   . PRO B 126 ? 2.303 2.194 2.379 0.270  0.793  0.048  126 PRO LLL O   
2589 C CB  . PRO B 126 ? 2.113 2.086 2.136 0.309  0.738  0.115  126 PRO LLL CB  
2590 C CG  . PRO B 126 ? 2.141 2.166 2.167 0.298  0.727  0.094  126 PRO LLL CG  
2591 C CD  . PRO B 126 ? 2.065 2.108 2.092 0.256  0.713  0.071  126 PRO LLL CD  
2592 N N   . SER B 127 ? 2.675 2.501 2.736 0.290  0.801  0.094  127 SER LLL N   
2593 C CA  . SER B 127 ? 2.815 2.570 2.900 0.301  0.848  0.086  127 SER LLL CA  
2594 C C   . SER B 127 ? 2.865 2.614 2.953 0.336  0.868  0.090  127 SER LLL C   
2595 O O   . SER B 127 ? 3.032 2.825 3.099 0.361  0.848  0.112  127 SER LLL O   
2596 C CB  . SER B 127 ? 2.988 2.686 3.065 0.318  0.866  0.116  127 SER LLL CB  
2597 O OG  . SER B 127 ? 3.318 2.952 3.406 0.351  0.913  0.128  127 SER LLL OG  
2598 N N   . ASP B 128 ? 2.803 2.500 2.918 0.338  0.909  0.069  128 ASP LLL N   
2599 C CA  . ASP B 128 ? 2.868 2.546 2.987 0.378  0.937  0.076  128 ASP LLL CA  
2600 C C   . ASP B 128 ? 2.794 2.407 2.898 0.424  0.969  0.120  128 ASP LLL C   
2601 O O   . ASP B 128 ? 2.700 2.316 2.791 0.472  0.978  0.143  128 ASP LLL O   
2602 C CB  . ASP B 128 ? 3.094 2.749 3.248 0.358  0.966  0.031  128 ASP LLL CB  
2603 C CG  . ASP B 128 ? 3.199 2.933 3.358 0.330  0.934  -0.004 128 ASP LLL CG  
2604 O OD1 . ASP B 128 ? 3.364 3.100 3.550 0.296  0.943  -0.049 128 ASP LLL OD1 
2605 O OD2 . ASP B 128 ? 3.316 3.113 3.451 0.342  0.900  0.012  128 ASP LLL OD2 
2606 N N   . GLU B 129 ? 2.813 2.375 2.920 0.414  0.984  0.131  129 GLU LLL N   
2607 C CA  . GLU B 129 ? 3.033 2.541 3.120 0.459  1.010  0.179  129 GLU LLL CA  
2608 C C   . GLU B 129 ? 2.850 2.424 2.899 0.488  0.969  0.215  129 GLU LLL C   
2609 O O   . GLU B 129 ? 2.838 2.400 2.865 0.543  0.984  0.254  129 GLU LLL O   
2610 C CB  . GLU B 129 ? 3.252 2.698 3.350 0.436  1.034  0.181  129 GLU LLL CB  
2611 C CG  . GLU B 129 ? 3.421 2.794 3.560 0.410  1.084  0.145  129 GLU LLL CG  
2612 C CD  . GLU B 129 ? 3.447 2.853 3.614 0.347  1.065  0.092  129 GLU LLL CD  
2613 O OE1 . GLU B 129 ? 3.465 2.941 3.636 0.327  1.031  0.063  129 GLU LLL OE1 
2614 O OE2 . GLU B 129 ? 3.427 2.794 3.612 0.320  1.084  0.081  129 GLU LLL OE2 
2615 N N   . GLN B 130 ? 2.672 2.314 2.714 0.453  0.920  0.202  130 GLN LLL N   
2616 C CA  . GLN B 130 ? 2.606 2.313 2.620 0.472  0.882  0.229  130 GLN LLL CA  
2617 C C   . GLN B 130 ? 2.727 2.486 2.730 0.511  0.874  0.236  130 GLN LLL C   
2618 O O   . GLN B 130 ? 2.830 2.623 2.810 0.553  0.864  0.267  130 GLN LLL O   
2619 C CB  . GLN B 130 ? 2.362 2.123 2.374 0.424  0.837  0.210  130 GLN LLL CB  
2620 C CG  . GLN B 130 ? 2.235 2.052 2.222 0.439  0.804  0.234  130 GLN LLL CG  
2621 C CD  . GLN B 130 ? 2.121 1.989 2.108 0.394  0.764  0.215  130 GLN LLL CD  
2622 O OE1 . GLN B 130 ? 1.967 1.831 1.967 0.355  0.760  0.187  130 GLN LLL OE1 
2623 N NE2 . GLN B 130 ? 2.230 2.145 2.199 0.403  0.737  0.232  130 GLN LLL NE2 
2624 N N   . LEU B 131 ? 2.786 2.556 2.807 0.499  0.879  0.207  131 LEU LLL N   
2625 C CA  . LEU B 131 ? 2.821 2.650 2.835 0.528  0.868  0.206  131 LEU LLL CA  
2626 C C   . LEU B 131 ? 2.886 2.678 2.889 0.593  0.904  0.236  131 LEU LLL C   
2627 O O   . LEU B 131 ? 2.875 2.722 2.867 0.630  0.896  0.243  131 LEU LLL O   
2628 C CB  . LEU B 131 ? 2.916 2.760 2.953 0.493  0.867  0.165  131 LEU LLL CB  
2629 C CG  . LEU B 131 ? 2.980 2.885 3.018 0.442  0.826  0.141  131 LEU LLL CG  
2630 C CD1 . LEU B 131 ? 3.032 2.932 3.095 0.403  0.832  0.100  131 LEU LLL CD1 
2631 C CD2 . LEU B 131 ? 3.086 3.078 3.110 0.452  0.793  0.146  131 LEU LLL CD2 
2632 N N   . LYS B 132 ? 2.995 2.699 3.000 0.609  0.945  0.255  132 LYS LLL N   
2633 C CA  . LYS B 132 ? 3.226 2.883 3.214 0.678  0.985  0.293  132 LYS LLL CA  
2634 C C   . LYS B 132 ? 3.234 2.928 3.188 0.717  0.968  0.335  132 LYS LLL C   
2635 O O   . LYS B 132 ? 3.452 3.151 3.384 0.784  0.986  0.367  132 LYS LLL O   
2636 C CB  . LYS B 132 ? 3.393 2.933 3.400 0.674  1.043  0.294  132 LYS LLL CB  
2637 C CG  . LYS B 132 ? 3.355 2.867 3.400 0.628  1.059  0.244  132 LYS LLL CG  
2638 C CD  . LYS B 132 ? 3.445 2.842 3.514 0.631  1.124  0.241  132 LYS LLL CD  
2639 C CE  . LYS B 132 ? 3.535 2.891 3.605 0.683  1.167  0.251  132 LYS LLL CE  
2640 N NZ  . LYS B 132 ? 3.628 2.862 3.723 0.685  1.237  0.250  132 LYS LLL NZ  
2641 N N   . SER B 133 ? 3.073 2.796 3.022 0.682  0.935  0.333  133 SER LLL N   
2642 C CA  . SER B 133 ? 3.115 2.888 3.035 0.714  0.913  0.365  133 SER LLL CA  
2643 C C   . SER B 133 ? 3.064 2.950 2.974 0.737  0.875  0.359  133 SER LLL C   
2644 O O   . SER B 133 ? 3.195 3.134 3.080 0.780  0.862  0.383  133 SER LLL O   
2645 C CB  . SER B 133 ? 3.126 2.902 3.048 0.668  0.888  0.360  133 SER LLL CB  
2646 O OG  . SER B 133 ? 3.305 2.999 3.249 0.625  0.912  0.345  133 SER LLL OG  
2647 N N   . GLY B 134 ? 2.972 2.896 2.900 0.708  0.859  0.324  134 GLY LLL N   
2648 C CA  . GLY B 134 ? 2.846 2.880 2.772 0.715  0.823  0.309  134 GLY LLL CA  
2649 C C   . GLY B 134 ? 2.707 2.796 2.641 0.656  0.781  0.285  134 GLY LLL C   
2650 O O   . GLY B 134 ? 2.569 2.750 2.502 0.656  0.752  0.271  134 GLY LLL O   
2651 N N   . THR B 135 ? 2.725 2.761 2.667 0.608  0.780  0.279  135 THR LLL N   
2652 C CA  . THR B 135 ? 2.743 2.815 2.688 0.555  0.744  0.261  135 THR LLL CA  
2653 C C   . THR B 135 ? 2.783 2.817 2.747 0.498  0.744  0.234  135 THR LLL C   
2654 O O   . THR B 135 ? 2.881 2.843 2.855 0.497  0.775  0.232  135 THR LLL O   
2655 C CB  . THR B 135 ? 2.772 2.830 2.704 0.558  0.737  0.284  135 THR LLL CB  
2656 O OG1 . THR B 135 ? 2.726 2.811 2.665 0.504  0.706  0.264  135 THR LLL OG1 
2657 C CG2 . THR B 135 ? 2.820 2.783 2.750 0.565  0.770  0.303  135 THR LLL CG2 
2658 N N   . ALA B 136 ? 2.713 2.794 2.682 0.454  0.714  0.213  136 ALA LLL N   
2659 C CA  . ALA B 136 ? 2.634 2.696 2.615 0.404  0.710  0.187  136 ALA LLL CA  
2660 C C   . ALA B 136 ? 2.531 2.613 2.506 0.365  0.682  0.184  136 ALA LLL C   
2661 O O   . ALA B 136 ? 2.516 2.659 2.485 0.361  0.659  0.183  136 ALA LLL O   
2662 C CB  . ALA B 136 ? 2.575 2.677 2.566 0.397  0.708  0.164  136 ALA LLL CB  
2663 N N   . SER B 137 ? 2.414 2.449 2.392 0.337  0.685  0.179  137 SER LLL N   
2664 C CA  . SER B 137 ? 2.311 2.357 2.281 0.303  0.661  0.177  137 SER LLL CA  
2665 C C   . SER B 137 ? 2.299 2.341 2.275 0.265  0.658  0.153  137 SER LLL C   
2666 O O   . SER B 137 ? 2.236 2.241 2.225 0.261  0.678  0.140  137 SER LLL O   
2667 C CB  . SER B 137 ? 2.354 2.359 2.318 0.308  0.664  0.195  137 SER LLL CB  
2668 O OG  . SER B 137 ? 2.444 2.474 2.397 0.339  0.658  0.217  137 SER LLL OG  
2669 N N   . VAL B 138 ? 2.347 2.430 2.316 0.240  0.636  0.146  138 VAL LLL N   
2670 C CA  . VAL B 138 ? 2.395 2.481 2.361 0.207  0.630  0.128  138 VAL LLL CA  
2671 C C   . VAL B 138 ? 2.237 2.311 2.190 0.189  0.615  0.137  138 VAL LLL C   
2672 O O   . VAL B 138 ? 2.264 2.358 2.209 0.188  0.601  0.151  138 VAL LLL O   
2673 C CB  . VAL B 138 ? 2.467 2.604 2.431 0.195  0.623  0.117  138 VAL LLL CB  
2674 C CG1 . VAL B 138 ? 2.540 2.681 2.504 0.174  0.626  0.096  138 VAL LLL CG1 
2675 C CG2 . VAL B 138 ? 2.510 2.674 2.484 0.220  0.632  0.115  138 VAL LLL CG2 
2676 N N   . VAL B 139 ? 2.130 2.177 2.085 0.175  0.618  0.128  139 VAL LLL N   
2677 C CA  . VAL B 139 ? 2.269 2.306 2.210 0.160  0.603  0.136  139 VAL LLL CA  
2678 C C   . VAL B 139 ? 2.283 2.339 2.214 0.137  0.595  0.121  139 VAL LLL C   
2679 O O   . VAL B 139 ? 2.116 2.178 2.058 0.133  0.606  0.098  139 VAL LLL O   
2680 C CB  . VAL B 139 ? 2.337 2.330 2.284 0.166  0.612  0.140  139 VAL LLL CB  
2681 C CG1 . VAL B 139 ? 2.568 2.538 2.536 0.165  0.635  0.118  139 VAL LLL CG1 
2682 C CG2 . VAL B 139 ? 2.256 2.244 2.191 0.151  0.596  0.145  139 VAL LLL CG2 
2683 N N   . CYS B 140 ? 2.366 2.433 2.278 0.126  0.579  0.132  140 CYS LLL N   
2684 C CA  . CYS B 140 ? 2.391 2.473 2.286 0.111  0.571  0.126  140 CYS LLL CA  
2685 C C   . CYS B 140 ? 2.311 2.372 2.196 0.107  0.562  0.132  140 CYS LLL C   
2686 O O   . CYS B 140 ? 2.101 2.145 1.981 0.110  0.555  0.150  140 CYS LLL O   
2687 C CB  . CYS B 140 ? 2.492 2.598 2.369 0.103  0.565  0.137  140 CYS LLL CB  
2688 S SG  . CYS B 140 ? 2.585 2.723 2.443 0.094  0.566  0.126  140 CYS LLL SG  
2689 N N   . LEU B 141 ? 2.229 2.298 2.111 0.102  0.562  0.115  141 LEU LLL N   
2690 C CA  . LEU B 141 ? 2.055 2.110 1.931 0.100  0.554  0.115  141 LEU LLL CA  
2691 C C   . LEU B 141 ? 2.029 2.110 1.877 0.096  0.543  0.116  141 LEU LLL C   
2692 O O   . LEU B 141 ? 2.092 2.206 1.936 0.096  0.546  0.098  141 LEU LLL O   
2693 C CB  . LEU B 141 ? 1.999 2.045 1.901 0.099  0.568  0.088  141 LEU LLL CB  
2694 C CG  . LEU B 141 ? 2.030 2.083 1.930 0.093  0.562  0.073  141 LEU LLL CG  
2695 C CD1 . LEU B 141 ? 2.101 2.127 1.990 0.096  0.552  0.096  141 LEU LLL CD1 
2696 C CD2 . LEU B 141 ? 1.986 2.037 1.918 0.087  0.581  0.038  141 LEU LLL CD2 
2697 N N   . LEU B 142 ? 1.953 2.019 1.780 0.097  0.531  0.137  142 LEU LLL N   
2698 C CA  . LEU B 142 ? 2.048 2.131 1.845 0.100  0.522  0.144  142 LEU LLL CA  
2699 C C   . LEU B 142 ? 2.134 2.214 1.931 0.103  0.515  0.133  142 LEU LLL C   
2700 O O   . LEU B 142 ? 2.250 2.300 2.054 0.103  0.510  0.144  142 LEU LLL O   
2701 C CB  . LEU B 142 ? 2.056 2.118 1.830 0.099  0.518  0.174  142 LEU LLL CB  
2702 C CG  . LEU B 142 ? 2.068 2.140 1.836 0.094  0.527  0.183  142 LEU LLL CG  
2703 C CD1 . LEU B 142 ? 2.086 2.157 1.882 0.090  0.534  0.176  142 LEU LLL CD1 
2704 C CD2 . LEU B 142 ? 2.072 2.122 1.818 0.091  0.528  0.209  142 LEU LLL CD2 
2705 N N   . ASN B 143 ? 2.156 2.274 1.949 0.107  0.513  0.110  143 ASN LLL N   
2706 C CA  . ASN B 143 ? 2.163 2.291 1.969 0.107  0.510  0.087  143 ASN LLL CA  
2707 C C   . ASN B 143 ? 2.132 2.286 1.905 0.120  0.496  0.093  143 ASN LLL C   
2708 O O   . ASN B 143 ? 2.115 2.308 1.865 0.130  0.495  0.091  143 ASN LLL O   
2709 C CB  . ASN B 143 ? 2.233 2.393 2.070 0.100  0.522  0.046  143 ASN LLL CB  
2710 C CG  . ASN B 143 ? 2.377 2.526 2.245 0.091  0.529  0.021  143 ASN LLL CG  
2711 O OD1 . ASN B 143 ? 2.511 2.615 2.387 0.088  0.531  0.038  143 ASN LLL OD1 
2712 N ND2 . ASN B 143 ? 2.455 2.650 2.341 0.086  0.535  -0.021 143 ASN LLL ND2 
2713 N N   . ASN B 144 ? 2.287 2.423 2.058 0.122  0.488  0.100  144 ASN LLL N   
2714 C CA  . ASN B 144 ? 2.370 2.535 2.114 0.137  0.475  0.100  144 ASN LLL CA  
2715 C C   . ASN B 144 ? 2.345 2.508 2.044 0.154  0.472  0.132  144 ASN LLL C   
2716 O O   . ASN B 144 ? 2.206 2.417 1.884 0.168  0.471  0.125  144 ASN LLL O   
2717 C CB  . ASN B 144 ? 2.389 2.618 2.144 0.140  0.475  0.057  144 ASN LLL CB  
2718 C CG  . ASN B 144 ? 2.527 2.752 2.330 0.121  0.486  0.022  144 ASN LLL CG  
2719 O OD1 . ASN B 144 ? 2.578 2.755 2.398 0.111  0.490  0.033  144 ASN LLL OD1 
2720 N ND2 . ASN B 144 ? 2.573 2.850 2.398 0.115  0.493  -0.021 144 ASN LLL ND2 
2721 N N   . PHE B 145 ? 2.298 2.410 1.985 0.152  0.472  0.166  145 PHE LLL N   
2722 C CA  . PHE B 145 ? 2.309 2.404 1.957 0.164  0.475  0.199  145 PHE LLL CA  
2723 C C   . PHE B 145 ? 2.205 2.254 1.841 0.167  0.471  0.224  145 PHE LLL C   
2724 O O   . PHE B 145 ? 2.118 2.142 1.779 0.155  0.466  0.220  145 PHE LLL O   
2725 C CB  . PHE B 145 ? 2.311 2.392 1.965 0.152  0.488  0.210  145 PHE LLL CB  
2726 C CG  . PHE B 145 ? 2.162 2.202 1.843 0.133  0.491  0.217  145 PHE LLL CG  
2727 C CD1 . PHE B 145 ? 2.169 2.170 1.838 0.129  0.496  0.243  145 PHE LLL CD1 
2728 C CD2 . PHE B 145 ? 2.058 2.100 1.776 0.122  0.491  0.196  145 PHE LLL CD2 
2729 C CE1 . PHE B 145 ? 2.245 2.222 1.941 0.113  0.498  0.244  145 PHE LLL CE1 
2730 C CE2 . PHE B 145 ? 2.117 2.129 1.856 0.111  0.494  0.204  145 PHE LLL CE2 
2731 C CZ  . PHE B 145 ? 2.229 2.215 1.957 0.107  0.495  0.226  145 PHE LLL CZ  
2732 N N   . TYR B 146 ? 2.307 2.345 1.904 0.184  0.474  0.251  146 TYR LLL N   
2733 C CA  . TYR B 146 ? 2.274 2.262 1.855 0.188  0.476  0.278  146 TYR LLL CA  
2734 C C   . TYR B 146 ? 2.212 2.175 1.760 0.196  0.494  0.308  146 TYR LLL C   
2735 O O   . TYR B 146 ? 2.237 2.231 1.759 0.211  0.501  0.312  146 TYR LLL O   
2736 C CB  . TYR B 146 ? 2.373 2.373 1.937 0.209  0.462  0.275  146 TYR LLL CB  
2737 C CG  . TYR B 146 ? 2.414 2.362 1.965 0.213  0.463  0.298  146 TYR LLL CG  
2738 C CD1 . TYR B 146 ? 2.291 2.219 1.870 0.200  0.453  0.289  146 TYR LLL CD1 
2739 C CD2 . TYR B 146 ? 2.526 2.442 2.039 0.231  0.477  0.330  146 TYR LLL CD2 
2740 C CE1 . TYR B 146 ? 2.333 2.217 1.904 0.202  0.454  0.307  146 TYR LLL CE1 
2741 C CE2 . TYR B 146 ? 2.526 2.390 2.031 0.232  0.481  0.348  146 TYR LLL CE2 
2742 C CZ  . TYR B 146 ? 2.411 2.262 1.947 0.217  0.468  0.335  146 TYR LLL CZ  
2743 O OH  . TYR B 146 ? 2.469 2.272 1.999 0.219  0.472  0.349  146 TYR LLL OH  
2744 N N   . PRO B 147 ? 2.144 2.052 1.692 0.184  0.506  0.328  147 PRO LLL N   
2745 C CA  . PRO B 147 ? 2.243 2.124 1.824 0.165  0.499  0.320  147 PRO LLL CA  
2746 C C   . PRO B 147 ? 2.337 2.231 1.959 0.140  0.497  0.301  147 PRO LLL C   
2747 O O   . PRO B 147 ? 2.324 2.247 1.950 0.138  0.502  0.292  147 PRO LLL O   
2748 C CB  . PRO B 147 ? 2.300 2.127 1.867 0.161  0.516  0.345  147 PRO LLL CB  
2749 C CG  . PRO B 147 ? 2.214 2.034 1.755 0.166  0.539  0.365  147 PRO LLL CG  
2750 C CD  . PRO B 147 ? 2.248 2.120 1.765 0.190  0.530  0.359  147 PRO LLL CD  
2751 N N   . ARG B 148 ? 2.542 2.420 2.192 0.127  0.491  0.294  148 ARG LLL N   
2752 C CA  . ARG B 148 ? 2.611 2.499 2.297 0.109  0.491  0.279  148 ARG LLL CA  
2753 C C   . ARG B 148 ? 2.542 2.423 2.231 0.095  0.509  0.286  148 ARG LLL C   
2754 O O   . ARG B 148 ? 2.718 2.624 2.424 0.088  0.512  0.275  148 ARG LLL O   
2755 C CB  . ARG B 148 ? 2.844 2.720 2.554 0.103  0.482  0.274  148 ARG LLL CB  
2756 C CG  . ARG B 148 ? 3.057 2.947 2.799 0.092  0.483  0.262  148 ARG LLL CG  
2757 C CD  . ARG B 148 ? 3.243 3.128 2.998 0.077  0.494  0.264  148 ARG LLL CD  
2758 N NE  . ARG B 148 ? 3.365 3.278 3.148 0.071  0.494  0.251  148 ARG LLL NE  
2759 C CZ  . ARG B 148 ? 3.275 3.207 3.066 0.064  0.504  0.246  148 ARG LLL CZ  
2760 N NH1 . ARG B 148 ? 3.015 2.940 2.792 0.056  0.518  0.253  148 ARG LLL NH1 
2761 N NH2 . ARG B 148 ? 3.443 3.403 3.258 0.067  0.503  0.235  148 ARG LLL NH2 
2762 N N   . GLU B 149 ? 2.446 2.294 2.120 0.091  0.523  0.302  149 GLU LLL N   
2763 C CA  . GLU B 149 ? 2.609 2.448 2.289 0.073  0.545  0.308  149 GLU LLL CA  
2764 C C   . GLU B 149 ? 2.710 2.579 2.384 0.074  0.551  0.305  149 GLU LLL C   
2765 O O   . GLU B 149 ? 2.992 2.864 2.633 0.091  0.555  0.318  149 GLU LLL O   
2766 C CB  . GLU B 149 ? 2.847 2.638 2.499 0.075  0.564  0.330  149 GLU LLL CB  
2767 C CG  . GLU B 149 ? 3.133 2.907 2.782 0.059  0.595  0.339  149 GLU LLL CG  
2768 C CD  . GLU B 149 ? 3.269 3.002 2.876 0.073  0.620  0.370  149 GLU LLL CD  
2769 O OE1 . GLU B 149 ? 3.457 3.148 3.049 0.081  0.625  0.383  149 GLU LLL OE1 
2770 O OE2 . GLU B 149 ? 2.942 2.683 2.529 0.076  0.637  0.382  149 GLU LLL OE2 
2771 N N   . ALA B 150 ? 2.552 2.449 2.256 0.061  0.551  0.289  150 ALA LLL N   
2772 C CA  . ALA B 150 ? 2.354 2.285 2.059 0.062  0.556  0.282  150 ALA LLL CA  
2773 C C   . ALA B 150 ? 2.196 2.148 1.934 0.045  0.561  0.266  150 ALA LLL C   
2774 O O   . ALA B 150 ? 2.072 2.030 1.835 0.042  0.550  0.255  150 ALA LLL O   
2775 C CB  . ALA B 150 ? 2.277 2.233 1.982 0.077  0.539  0.269  150 ALA LLL CB  
2776 N N   . LYS B 151 ? 2.202 2.168 1.938 0.036  0.577  0.267  151 LYS LLL N   
2777 C CA  . LYS B 151 ? 2.301 2.297 2.069 0.021  0.583  0.250  151 LYS LLL CA  
2778 C C   . LYS B 151 ? 2.248 2.280 2.021 0.030  0.578  0.239  151 LYS LLL C   
2779 O O   . LYS B 151 ? 2.318 2.356 2.068 0.037  0.584  0.246  151 LYS LLL O   
2780 C CB  . LYS B 151 ? 2.382 2.369 2.153 -0.001 0.608  0.254  151 LYS LLL CB  
2781 C CG  . LYS B 151 ? 2.532 2.525 2.283 -0.004 0.628  0.264  151 LYS LLL CG  
2782 C CD  . LYS B 151 ? 2.579 2.619 2.353 -0.013 0.633  0.246  151 LYS LLL CD  
2783 C CE  . LYS B 151 ? 2.594 2.639 2.345 -0.015 0.654  0.258  151 LYS LLL CE  
2784 N NZ  . LYS B 151 ? 2.458 2.551 2.217 -0.008 0.648  0.243  151 LYS LLL NZ  
2785 N N   . VAL B 152 ? 2.305 2.362 2.106 0.034  0.568  0.222  152 VAL LLL N   
2786 C CA  . VAL B 152 ? 2.301 2.388 2.113 0.043  0.566  0.208  152 VAL LLL CA  
2787 C C   . VAL B 152 ? 2.228 2.348 2.065 0.035  0.573  0.196  152 VAL LLL C   
2788 O O   . VAL B 152 ? 2.118 2.247 1.977 0.036  0.567  0.189  152 VAL LLL O   
2789 C CB  . VAL B 152 ? 2.243 2.325 2.064 0.060  0.552  0.201  152 VAL LLL CB  
2790 C CG1 . VAL B 152 ? 2.266 2.372 2.102 0.069  0.555  0.186  152 VAL LLL CG1 
2791 C CG2 . VAL B 152 ? 2.211 2.271 2.010 0.067  0.545  0.208  152 VAL LLL CG2 
2792 N N   . GLN B 153 ? 2.311 2.457 2.148 0.030  0.585  0.191  153 GLN LLL N   
2793 C CA  . GLN B 153 ? 2.397 2.582 2.258 0.023  0.592  0.176  153 GLN LLL CA  
2794 C C   . GLN B 153 ? 2.310 2.523 2.180 0.039  0.590  0.164  153 GLN LLL C   
2795 O O   . GLN B 153 ? 2.280 2.492 2.134 0.043  0.593  0.165  153 GLN LLL O   
2796 C CB  . GLN B 153 ? 2.578 2.771 2.432 0.002  0.612  0.180  153 GLN LLL CB  
2797 C CG  . GLN B 153 ? 2.765 2.920 2.607 -0.014 0.622  0.194  153 GLN LLL CG  
2798 C CD  . GLN B 153 ? 2.757 2.921 2.607 -0.040 0.647  0.191  153 GLN LLL CD  
2799 O OE1 . GLN B 153 ? 2.725 2.879 2.555 -0.047 0.666  0.203  153 GLN LLL OE1 
2800 N NE2 . GLN B 153 ? 2.737 2.924 2.620 -0.053 0.648  0.172  153 GLN LLL NE2 
2801 N N   . TRP B 154 ? 2.250 2.491 2.145 0.049  0.586  0.151  154 TRP LLL N   
2802 C CA  . TRP B 154 ? 2.222 2.489 2.129 0.067  0.588  0.138  154 TRP LLL CA  
2803 C C   . TRP B 154 ? 2.258 2.569 2.174 0.056  0.599  0.127  154 TRP LLL C   
2804 O O   . TRP B 154 ? 2.216 2.550 2.144 0.042  0.603  0.122  154 TRP LLL O   
2805 C CB  . TRP B 154 ? 2.167 2.442 2.093 0.090  0.581  0.134  154 TRP LLL CB  
2806 C CG  . TRP B 154 ? 2.110 2.342 2.029 0.104  0.574  0.143  154 TRP LLL CG  
2807 C CD1 . TRP B 154 ? 2.182 2.392 2.099 0.107  0.565  0.153  154 TRP LLL CD1 
2808 C CD2 . TRP B 154 ? 2.152 2.360 2.068 0.114  0.577  0.140  154 TRP LLL CD2 
2809 N NE1 . TRP B 154 ? 2.319 2.492 2.231 0.119  0.563  0.158  154 TRP LLL NE1 
2810 C CE2 . TRP B 154 ? 2.162 2.334 2.075 0.122  0.572  0.149  154 TRP LLL CE2 
2811 C CE3 . TRP B 154 ? 2.290 2.507 2.208 0.117  0.586  0.127  154 TRP LLL CE3 
2812 C CZ2 . TRP B 154 ? 2.195 2.338 2.109 0.129  0.576  0.143  154 TRP LLL CZ2 
2813 C CZ3 . TRP B 154 ? 2.258 2.449 2.178 0.124  0.590  0.120  154 TRP LLL CZ3 
2814 C CH2 . TRP B 154 ? 2.208 2.361 2.127 0.129  0.586  0.128  154 TRP LLL CH2 
2815 N N   . LYS B 155 ? 2.326 2.651 2.239 0.061  0.605  0.120  155 LYS LLL N   
2816 C CA  . LYS B 155 ? 2.317 2.686 2.236 0.052  0.617  0.109  155 LYS LLL CA  
2817 C C   . LYS B 155 ? 2.109 2.504 2.043 0.074  0.617  0.093  155 LYS LLL C   
2818 O O   . LYS B 155 ? 2.035 2.426 1.961 0.079  0.620  0.088  155 LYS LLL O   
2819 C CB  . LYS B 155 ? 2.521 2.882 2.415 0.035  0.627  0.118  155 LYS LLL CB  
2820 C CG  . LYS B 155 ? 2.670 2.994 2.544 0.019  0.631  0.138  155 LYS LLL CG  
2821 C CD  . LYS B 155 ? 2.681 2.998 2.525 0.009  0.645  0.152  155 LYS LLL CD  
2822 C CE  . LYS B 155 ? 2.724 3.078 2.572 -0.005 0.664  0.145  155 LYS LLL CE  
2823 N NZ  . LYS B 155 ? 2.723 3.065 2.538 -0.014 0.682  0.165  155 LYS LLL NZ  
2824 N N   . VAL B 156 ? 2.080 2.498 2.034 0.091  0.613  0.085  156 VAL LLL N   
2825 C CA  . VAL B 156 ? 2.011 2.449 1.979 0.118  0.616  0.073  156 VAL LLL CA  
2826 C C   . VAL B 156 ? 1.926 2.419 1.903 0.110  0.625  0.058  156 VAL LLL C   
2827 O O   . VAL B 156 ? 1.804 2.340 1.794 0.103  0.626  0.050  156 VAL LLL O   
2828 C CB  . VAL B 156 ? 2.156 2.600 2.138 0.147  0.610  0.075  156 VAL LLL CB  
2829 C CG1 . VAL B 156 ? 2.141 2.596 2.133 0.179  0.617  0.066  156 VAL LLL CG1 
2830 C CG2 . VAL B 156 ? 2.277 2.669 2.250 0.153  0.603  0.091  156 VAL LLL CG2 
2831 N N   . ASP B 157 ? 1.942 2.435 1.913 0.109  0.631  0.051  157 ASP LLL N   
2832 C CA  . ASP B 157 ? 1.760 2.303 1.738 0.106  0.641  0.035  157 ASP LLL CA  
2833 C C   . ASP B 157 ? 1.711 2.274 1.679 0.073  0.649  0.039  157 ASP LLL C   
2834 O O   . ASP B 157 ? 1.535 2.148 1.515 0.064  0.658  0.026  157 ASP LLL O   
2835 C CB  . ASP B 157 ? 1.705 2.292 1.706 0.130  0.641  0.021  157 ASP LLL CB  
2836 C CG  . ASP B 157 ? 1.804 2.405 1.810 0.147  0.648  0.006  157 ASP LLL CG  
2837 O OD1 . ASP B 157 ? 1.723 2.320 1.740 0.179  0.649  0.002  157 ASP LLL OD1 
2838 O OD2 . ASP B 157 ? 2.117 2.728 2.115 0.130  0.654  0.000  157 ASP LLL OD2 
2839 N N   . ASN B 158 ? 1.856 2.376 1.801 0.058  0.648  0.056  158 ASN LLL N   
2840 C CA  . ASN B 158 ? 2.036 2.552 1.965 0.030  0.660  0.069  158 ASN LLL CA  
2841 C C   . ASN B 158 ? 2.160 2.688 2.104 0.012  0.664  0.068  158 ASN LLL C   
2842 O O   . ASN B 158 ? 2.231 2.769 2.171 -0.014 0.682  0.071  158 ASN LLL O   
2843 C CB  . ASN B 158 ? 2.194 2.743 2.113 0.021  0.674  0.064  158 ASN LLL CB  
2844 C CG  . ASN B 158 ? 2.346 2.867 2.231 0.008  0.684  0.085  158 ASN LLL CG  
2845 O OD1 . ASN B 158 ? 2.297 2.774 2.168 0.003  0.681  0.103  158 ASN LLL OD1 
2846 N ND2 . ASN B 158 ? 2.421 2.970 2.292 0.006  0.696  0.084  158 ASN LLL ND2 
2847 N N   . ALA B 159 ? 2.269 2.799 2.232 0.024  0.652  0.062  159 ALA LLL N   
2848 C CA  . ALA B 159 ? 2.076 2.624 2.058 0.008  0.654  0.056  159 ALA LLL CA  
2849 C C   . ALA B 159 ? 2.004 2.503 1.977 0.012  0.642  0.071  159 ALA LLL C   
2850 O O   . ALA B 159 ? 1.831 2.312 1.802 0.038  0.628  0.076  159 ALA LLL O   
2851 C CB  . ALA B 159 ? 1.985 2.597 1.997 0.024  0.649  0.032  159 ALA LLL CB  
2852 N N   . LEU B 160 ? 2.170 2.647 2.141 -0.014 0.651  0.078  160 LEU LLL N   
2853 C CA  . LEU B 160 ? 2.319 2.754 2.284 -0.012 0.640  0.089  160 LEU LLL CA  
2854 C C   . LEU B 160 ? 2.254 2.728 2.246 0.006  0.626  0.074  160 LEU LLL C   
2855 O O   . LEU B 160 ? 2.036 2.570 2.054 -0.002 0.631  0.050  160 LEU LLL O   
2856 C CB  . LEU B 160 ? 2.407 2.812 2.367 -0.044 0.656  0.097  160 LEU LLL CB  
2857 C CG  . LEU B 160 ? 2.487 2.844 2.438 -0.043 0.646  0.111  160 LEU LLL CG  
2858 C CD1 . LEU B 160 ? 2.387 2.705 2.314 -0.017 0.628  0.129  160 LEU LLL CD1 
2859 C CD2 . LEU B 160 ? 2.592 2.907 2.531 -0.071 0.666  0.123  160 LEU LLL CD2 
2860 N N   . GLN B 161 ? 2.162 2.604 2.144 0.030  0.609  0.085  161 GLN LLL N   
2861 C CA  . GLN B 161 ? 2.198 2.670 2.198 0.055  0.596  0.077  161 GLN LLL CA  
2862 C C   . GLN B 161 ? 2.291 2.731 2.287 0.047  0.588  0.085  161 GLN LLL C   
2863 O O   . GLN B 161 ? 2.220 2.602 2.195 0.036  0.589  0.103  161 GLN LLL O   
2864 C CB  . GLN B 161 ? 2.092 2.555 2.085 0.091  0.589  0.084  161 GLN LLL CB  
2865 C CG  . GLN B 161 ? 2.093 2.589 2.091 0.098  0.598  0.073  161 GLN LLL CG  
2866 C CD  . GLN B 161 ? 2.099 2.671 2.121 0.114  0.598  0.052  161 GLN LLL CD  
2867 O OE1 . GLN B 161 ? 2.113 2.715 2.146 0.134  0.589  0.048  161 GLN LLL OE1 
2868 N NE2 . GLN B 161 ? 2.186 2.797 2.216 0.106  0.607  0.038  161 GLN LLL NE2 
2869 N N   . SER B 162 ? 2.406 2.891 2.423 0.054  0.581  0.070  162 SER LLL N   
2870 C CA  . SER B 162 ? 2.427 2.895 2.447 0.047  0.574  0.072  162 SER LLL CA  
2871 C C   . SER B 162 ? 2.494 2.985 2.517 0.084  0.558  0.074  162 SER LLL C   
2872 O O   . SER B 162 ? 2.392 2.944 2.428 0.110  0.555  0.061  162 SER LLL O   
2873 C CB  . SER B 162 ? 2.406 2.911 2.451 0.014  0.585  0.046  162 SER LLL CB  
2874 O OG  . SER B 162 ? 2.492 2.990 2.538 -0.018 0.606  0.043  162 SER LLL OG  
2875 N N   . GLY B 163 ? 2.602 3.045 2.611 0.089  0.550  0.091  163 GLY LLL N   
2876 C CA  . GLY B 163 ? 2.685 3.148 2.698 0.115  0.536  0.091  163 GLY LLL CA  
2877 C C   . GLY B 163 ? 2.785 3.257 2.790 0.161  0.532  0.104  163 GLY LLL C   
2878 O O   . GLY B 163 ? 3.271 3.773 3.279 0.189  0.523  0.105  163 GLY LLL O   
2879 N N   . ASN B 164 ? 2.655 3.099 2.650 0.170  0.539  0.115  164 ASN LLL N   
2880 C CA  . ASN B 164 ? 2.597 3.025 2.582 0.212  0.541  0.132  164 ASN LLL CA  
2881 C C   . ASN B 164 ? 2.469 2.816 2.436 0.204  0.545  0.150  164 ASN LLL C   
2882 O O   . ASN B 164 ? 2.401 2.720 2.362 0.228  0.554  0.160  164 ASN LLL O   
2883 C CB  . ASN B 164 ? 2.702 3.174 2.694 0.233  0.549  0.122  164 ASN LLL CB  
2884 C CG  . ASN B 164 ? 2.832 3.295 2.827 0.205  0.557  0.113  164 ASN LLL CG  
2885 O OD1 . ASN B 164 ? 2.972 3.404 2.962 0.168  0.558  0.113  164 ASN LLL OD1 
2886 N ND2 . ASN B 164 ? 2.897 3.386 2.896 0.224  0.565  0.107  164 ASN LLL ND2 
2887 N N   . SER B 165 ? 2.367 2.680 2.326 0.171  0.542  0.152  165 SER LLL N   
2888 C CA  . SER B 165 ? 2.349 2.595 2.292 0.162  0.542  0.166  165 SER LLL CA  
2889 C C   . SER B 165 ? 2.318 2.546 2.256 0.163  0.532  0.175  165 SER LLL C   
2890 O O   . SER B 165 ? 2.488 2.750 2.435 0.155  0.525  0.166  165 SER LLL O   
2891 C CB  . SER B 165 ? 2.389 2.618 2.324 0.131  0.546  0.163  165 SER LLL CB  
2892 O OG  . SER B 165 ? 2.380 2.623 2.318 0.106  0.544  0.157  165 SER LLL OG  
2893 N N   . GLN B 166 ? 2.212 2.391 2.139 0.170  0.532  0.189  166 GLN LLL N   
2894 C CA  . GLN B 166 ? 2.130 2.286 2.051 0.169  0.523  0.198  166 GLN LLL CA  
2895 C C   . GLN B 166 ? 2.026 2.130 1.932 0.153  0.523  0.204  166 GLN LLL C   
2896 O O   . GLN B 166 ? 1.959 2.043 1.864 0.157  0.533  0.203  166 GLN LLL O   
2897 C CB  . GLN B 166 ? 2.286 2.438 2.207 0.203  0.525  0.210  166 GLN LLL CB  
2898 C CG  . GLN B 166 ? 2.289 2.500 2.219 0.228  0.521  0.207  166 GLN LLL CG  
2899 C CD  . GLN B 166 ? 2.271 2.474 2.194 0.258  0.521  0.223  166 GLN LLL CD  
2900 O OE1 . GLN B 166 ? 2.262 2.443 2.180 0.287  0.534  0.238  166 GLN LLL OE1 
2901 N NE2 . GLN B 166 ? 2.314 2.528 2.237 0.251  0.508  0.221  166 GLN LLL NE2 
2902 N N   . GLU B 167 ? 1.995 2.082 1.894 0.139  0.514  0.207  167 GLU LLL N   
2903 C CA  . GLU B 167 ? 2.120 2.166 2.004 0.128  0.513  0.212  167 GLU LLL CA  
2904 C C   . GLU B 167 ? 2.072 2.095 1.953 0.138  0.507  0.220  167 GLU LLL C   
2905 O O   . GLU B 167 ? 1.860 1.898 1.746 0.149  0.501  0.224  167 GLU LLL O   
2906 C CB  . GLU B 167 ? 2.248 2.289 2.120 0.105  0.510  0.211  167 GLU LLL CB  
2907 C CG  . GLU B 167 ? 2.449 2.509 2.321 0.093  0.519  0.205  167 GLU LLL CG  
2908 C CD  . GLU B 167 ? 2.652 2.697 2.507 0.074  0.522  0.209  167 GLU LLL CD  
2909 O OE1 . GLU B 167 ? 2.575 2.633 2.427 0.065  0.531  0.206  167 GLU LLL OE1 
2910 O OE2 . GLU B 167 ? 2.949 2.971 2.794 0.069  0.516  0.217  167 GLU LLL OE2 
2911 N N   . SER B 168 ? 2.099 2.093 1.973 0.135  0.509  0.221  168 SER LLL N   
2912 C CA  . SER B 168 ? 2.227 2.196 2.097 0.139  0.505  0.226  168 SER LLL CA  
2913 C C   . SER B 168 ? 2.204 2.158 2.061 0.125  0.501  0.221  168 SER LLL C   
2914 O O   . SER B 168 ? 2.103 2.061 1.958 0.119  0.507  0.211  168 SER LLL O   
2915 C CB  . SER B 168 ? 2.317 2.272 2.198 0.157  0.518  0.229  168 SER LLL CB  
2916 O OG  . SER B 168 ? 2.193 2.133 2.078 0.151  0.530  0.217  168 SER LLL OG  
2917 N N   . VAL B 169 ? 2.130 2.072 1.978 0.122  0.491  0.225  169 VAL LLL N   
2918 C CA  . VAL B 169 ? 2.136 2.070 1.968 0.114  0.486  0.221  169 VAL LLL CA  
2919 C C   . VAL B 169 ? 1.973 1.894 1.809 0.119  0.484  0.218  169 VAL LLL C   
2920 O O   . VAL B 169 ? 1.919 1.833 1.757 0.125  0.479  0.227  169 VAL LLL O   
2921 C CB  . VAL B 169 ? 2.325 2.256 2.138 0.107  0.477  0.229  169 VAL LLL CB  
2922 C CG1 . VAL B 169 ? 2.501 2.432 2.293 0.105  0.475  0.227  169 VAL LLL CG1 
2923 C CG2 . VAL B 169 ? 2.297 2.240 2.114 0.100  0.482  0.232  169 VAL LLL CG2 
2924 N N   . THR B 170 ? 1.974 1.897 1.811 0.116  0.489  0.203  170 THR LLL N   
2925 C CA  . THR B 170 ? 2.209 2.125 2.049 0.116  0.487  0.196  170 THR LLL CA  
2926 C C   . THR B 170 ? 2.364 2.278 2.184 0.118  0.470  0.207  170 THR LLL C   
2927 O O   . THR B 170 ? 2.533 2.450 2.335 0.117  0.463  0.214  170 THR LLL O   
2928 C CB  . THR B 170 ? 2.127 2.058 1.974 0.110  0.494  0.171  170 THR LLL CB  
2929 O OG1 . THR B 170 ? 1.942 1.896 1.769 0.109  0.485  0.168  170 THR LLL OG1 
2930 C CG2 . THR B 170 ? 2.204 2.132 2.075 0.107  0.514  0.156  170 THR LLL CG2 
2931 N N   . GLU B 171 ? 2.397 2.303 2.220 0.121  0.465  0.208  171 GLU LLL N   
2932 C CA  . GLU B 171 ? 2.352 2.258 2.157 0.124  0.450  0.213  171 GLU LLL CA  
2933 C C   . GLU B 171 ? 2.244 2.170 2.038 0.124  0.447  0.197  171 GLU LLL C   
2934 O O   . GLU B 171 ? 2.042 1.983 1.850 0.119  0.457  0.177  171 GLU LLL O   
2935 C CB  . GLU B 171 ? 2.552 2.449 2.365 0.128  0.446  0.217  171 GLU LLL CB  
2936 C CG  . GLU B 171 ? 2.634 2.524 2.430 0.132  0.432  0.228  171 GLU LLL CG  
2937 C CD  . GLU B 171 ? 2.490 2.375 2.296 0.137  0.429  0.238  171 GLU LLL CD  
2938 O OE1 . GLU B 171 ? 2.379 2.260 2.177 0.139  0.419  0.243  171 GLU LLL OE1 
2939 O OE2 . GLU B 171 ? 2.348 2.234 2.170 0.140  0.439  0.240  171 GLU LLL OE2 
2940 N N   . GLN B 172 ? 2.203 2.131 1.971 0.131  0.436  0.205  172 GLN LLL N   
2941 C CA  . GLN B 172 ? 2.162 2.117 1.911 0.138  0.431  0.194  172 GLN LLL CA  
2942 C C   . GLN B 172 ? 2.164 2.147 1.931 0.135  0.433  0.166  172 GLN LLL C   
2943 O O   . GLN B 172 ? 2.172 2.149 1.951 0.134  0.431  0.163  172 GLN LLL O   
2944 C CB  . GLN B 172 ? 2.107 2.052 1.827 0.151  0.420  0.211  172 GLN LLL CB  
2945 C CG  . GLN B 172 ? 2.125 2.099 1.817 0.167  0.416  0.207  172 GLN LLL CG  
2946 C CD  . GLN B 172 ? 2.155 2.105 1.815 0.183  0.410  0.231  172 GLN LLL CD  
2947 O OE1 . GLN B 172 ? 2.072 2.002 1.735 0.184  0.404  0.237  172 GLN LLL OE1 
2948 N NE2 . GLN B 172 ? 2.420 2.371 2.049 0.196  0.415  0.245  172 GLN LLL NE2 
2949 N N   . ASP B 173 ? 2.379 2.396 2.151 0.133  0.439  0.144  173 ASP LLL N   
2950 C CA  . ASP B 173 ? 2.562 2.617 2.352 0.129  0.442  0.109  173 ASP LLL CA  
2951 C C   . ASP B 173 ? 2.583 2.662 2.355 0.143  0.427  0.106  173 ASP LLL C   
2952 O O   . ASP B 173 ? 2.523 2.609 2.260 0.161  0.415  0.123  173 ASP LLL O   
2953 C CB  . ASP B 173 ? 2.635 2.733 2.429 0.128  0.448  0.084  173 ASP LLL CB  
2954 C CG  . ASP B 173 ? 2.677 2.820 2.499 0.119  0.456  0.039  173 ASP LLL CG  
2955 O OD1 . ASP B 173 ? 3.004 3.133 2.862 0.101  0.475  0.020  173 ASP LLL OD1 
2956 O OD2 . ASP B 173 ? 2.416 2.609 2.224 0.131  0.444  0.022  173 ASP LLL OD2 
2957 N N   . SER B 174 ? 2.773 2.863 2.567 0.136  0.429  0.085  174 SER LLL N   
2958 C CA  . SER B 174 ? 3.042 3.153 2.822 0.149  0.414  0.082  174 SER LLL CA  
2959 C C   . SER B 174 ? 3.009 3.184 2.768 0.167  0.403  0.062  174 SER LLL C   
2960 O O   . SER B 174 ? 3.013 3.206 2.749 0.186  0.389  0.067  174 SER LLL O   
2961 C CB  . SER B 174 ? 3.170 3.280 2.983 0.134  0.422  0.063  174 SER LLL CB  
2962 O OG  . SER B 174 ? 3.036 3.098 2.846 0.134  0.420  0.090  174 SER LLL OG  
2963 N N   . LYS B 175 ? 2.845 3.058 2.610 0.164  0.410  0.039  175 LYS LLL N   
2964 C CA  . LYS B 175 ? 2.746 3.042 2.507 0.176  0.404  0.003  175 LYS LLL CA  
2965 C C   . LYS B 175 ? 2.697 3.019 2.420 0.200  0.398  0.017  175 LYS LLL C   
2966 O O   . LYS B 175 ? 2.552 2.936 2.248 0.227  0.386  0.006  175 LYS LLL O   
2967 C CB  . LYS B 175 ? 2.651 2.981 2.463 0.149  0.421  -0.048 175 LYS LLL CB  
2968 C CG  . LYS B 175 ? 2.677 2.967 2.527 0.124  0.436  -0.056 175 LYS LLL CG  
2969 C CD  . LYS B 175 ? 2.807 3.151 2.701 0.105  0.449  -0.114 175 LYS LLL CD  
2970 C CE  . LYS B 175 ? 2.907 3.267 2.840 0.082  0.473  -0.151 175 LYS LLL CE  
2971 N NZ  . LYS B 175 ? 2.909 3.349 2.878 0.068  0.481  -0.216 175 LYS LLL NZ  
2972 N N   . ASP B 176 ? 2.620 2.903 2.340 0.192  0.407  0.038  176 ASP LLL N   
2973 C CA  . ASP B 176 ? 2.624 2.922 2.306 0.213  0.405  0.058  176 ASP LLL CA  
2974 C C   . ASP B 176 ? 2.479 2.704 2.132 0.220  0.405  0.110  176 ASP LLL C   
2975 O O   . ASP B 176 ? 2.769 2.994 2.385 0.238  0.406  0.133  176 ASP LLL O   
2976 C CB  . ASP B 176 ? 2.690 3.011 2.393 0.199  0.417  0.035  176 ASP LLL CB  
2977 C CG  . ASP B 176 ? 2.690 2.947 2.422 0.171  0.431  0.045  176 ASP LLL CG  
2978 O OD1 . ASP B 176 ? 2.856 3.130 2.615 0.157  0.443  0.021  176 ASP LLL OD1 
2979 O OD2 . ASP B 176 ? 2.558 2.755 2.288 0.167  0.431  0.077  176 ASP LLL OD2 
2980 N N   . SER B 177 ? 2.234 2.401 1.903 0.204  0.406  0.125  177 SER LLL N   
2981 C CA  . SER B 177 ? 2.184 2.287 1.833 0.206  0.407  0.167  177 SER LLL CA  
2982 C C   . SER B 177 ? 1.968 2.046 1.616 0.197  0.419  0.183  177 SER LLL C   
2983 O O   . SER B 177 ? 1.927 1.976 1.545 0.207  0.423  0.213  177 SER LLL O   
2984 C CB  . SER B 177 ? 2.349 2.450 1.954 0.236  0.399  0.190  177 SER LLL CB  
2985 O OG  . SER B 177 ? 2.587 2.715 2.194 0.247  0.387  0.174  177 SER LLL OG  
2986 N N   . THR B 178 ? 2.033 2.120 1.713 0.177  0.427  0.163  178 THR LLL N   
2987 C CA  . THR B 178 ? 2.272 2.344 1.954 0.168  0.439  0.173  178 THR LLL CA  
2988 C C   . THR B 178 ? 2.109 2.143 1.824 0.148  0.446  0.176  178 THR LLL C   
2989 O O   . THR B 178 ? 2.209 2.235 1.947 0.140  0.445  0.164  178 THR LLL O   
2990 C CB  . THR B 178 ? 2.468 2.592 2.155 0.169  0.444  0.146  178 THR LLL CB  
2991 O OG1 . THR B 178 ? 2.418 2.558 2.146 0.153  0.448  0.111  178 THR LLL OG1 
2992 C CG2 . THR B 178 ? 2.560 2.736 2.213 0.195  0.436  0.141  178 THR LLL CG2 
2993 N N   . TYR B 179 ? 2.065 2.077 1.779 0.141  0.454  0.192  179 TYR LLL N   
2994 C CA  . TYR B 179 ? 2.068 2.057 1.811 0.126  0.461  0.193  179 TYR LLL CA  
2995 C C   . TYR B 179 ? 2.077 2.087 1.837 0.120  0.472  0.173  179 TYR LLL C   
2996 O O   . TYR B 179 ? 2.044 2.091 1.797 0.125  0.473  0.157  179 TYR LLL O   
2997 C CB  . TYR B 179 ? 2.178 2.136 1.910 0.123  0.463  0.218  179 TYR LLL CB  
2998 C CG  . TYR B 179 ? 2.215 2.150 1.934 0.129  0.454  0.233  179 TYR LLL CG  
2999 C CD1 . TYR B 179 ? 2.309 2.239 1.994 0.141  0.452  0.246  179 TYR LLL CD1 
3000 C CD2 . TYR B 179 ? 2.231 2.150 1.967 0.126  0.449  0.233  179 TYR LLL CD2 
3001 C CE1 . TYR B 179 ? 2.361 2.268 2.035 0.148  0.446  0.259  179 TYR LLL CE1 
3002 C CE2 . TYR B 179 ? 2.291 2.192 2.017 0.131  0.441  0.243  179 TYR LLL CE2 
3003 C CZ  . TYR B 179 ? 2.315 2.208 2.010 0.141  0.439  0.255  179 TYR LLL CZ  
3004 O OH  . TYR B 179 ? 2.299 2.171 1.986 0.147  0.433  0.264  179 TYR LLL OH  
3005 N N   . SER B 180 ? 1.995 1.988 1.779 0.112  0.481  0.174  180 SER LLL N   
3006 C CA  . SER B 180 ? 1.912 1.916 1.714 0.107  0.493  0.161  180 SER LLL CA  
3007 C C   . SER B 180 ? 1.897 1.879 1.711 0.105  0.498  0.177  180 SER LLL C   
3008 O O   . SER B 180 ? 2.146 2.107 1.966 0.107  0.495  0.187  180 SER LLL O   
3009 C CB  . SER B 180 ? 1.809 1.824 1.639 0.102  0.504  0.131  180 SER LLL CB  
3010 O OG  . SER B 180 ? 1.742 1.797 1.565 0.103  0.500  0.108  180 SER LLL OG  
3011 N N   . LEU B 181 ? 1.850 1.842 1.665 0.102  0.505  0.179  181 LEU LLL N   
3012 C CA  . LEU B 181 ? 1.915 1.899 1.739 0.102  0.508  0.191  181 LEU LLL CA  
3013 C C   . LEU B 181 ? 2.138 2.131 1.983 0.104  0.521  0.178  181 LEU LLL C   
3014 O O   . LEU B 181 ? 2.311 2.320 2.157 0.102  0.527  0.162  181 LEU LLL O   
3015 C CB  . LEU B 181 ? 1.852 1.841 1.657 0.096  0.507  0.204  181 LEU LLL CB  
3016 C CG  . LEU B 181 ? 1.820 1.809 1.637 0.092  0.509  0.212  181 LEU LLL CG  
3017 C CD1 . LEU B 181 ? 1.898 1.877 1.698 0.084  0.507  0.225  181 LEU LLL CD1 
3018 C CD2 . LEU B 181 ? 1.687 1.698 1.516 0.092  0.519  0.204  181 LEU LLL CD2 
3019 N N   . SER B 182 ? 2.299 2.284 2.158 0.111  0.526  0.185  182 SER LLL N   
3020 C CA  . SER B 182 ? 2.401 2.395 2.278 0.118  0.539  0.178  182 SER LLL CA  
3021 C C   . SER B 182 ? 2.282 2.292 2.161 0.123  0.537  0.188  182 SER LLL C   
3022 O O   . SER B 182 ? 2.041 2.048 1.923 0.131  0.532  0.199  182 SER LLL O   
3023 C CB  . SER B 182 ? 2.563 2.533 2.458 0.128  0.552  0.172  182 SER LLL CB  
3024 O OG  . SER B 182 ? 2.783 2.739 2.679 0.141  0.550  0.189  182 SER LLL OG  
3025 N N   . SER B 183 ? 2.257 2.291 2.135 0.117  0.540  0.183  183 SER LLL N   
3026 C CA  . SER B 183 ? 2.222 2.282 2.107 0.119  0.541  0.186  183 SER LLL CA  
3027 C C   . SER B 183 ? 2.241 2.311 2.143 0.136  0.553  0.179  183 SER LLL C   
3028 O O   . SER B 183 ? 2.344 2.418 2.248 0.134  0.561  0.167  183 SER LLL O   
3029 C CB  . SER B 183 ? 2.201 2.281 2.077 0.103  0.542  0.184  183 SER LLL CB  
3030 O OG  . SER B 183 ? 2.181 2.292 2.068 0.103  0.545  0.181  183 SER LLL OG  
3031 N N   . THR B 184 ? 2.254 2.327 2.164 0.156  0.555  0.186  184 THR LLL N   
3032 C CA  . THR B 184 ? 2.207 2.282 2.130 0.180  0.569  0.184  184 THR LLL CA  
3033 C C   . THR B 184 ? 2.100 2.222 2.030 0.191  0.568  0.182  184 THR LLL C   
3034 O O   . THR B 184 ? 1.921 2.066 1.851 0.200  0.559  0.188  184 THR LLL O   
3035 C CB  . THR B 184 ? 2.326 2.371 2.252 0.203  0.576  0.197  184 THR LLL CB  
3036 O OG1 . THR B 184 ? 2.435 2.444 2.357 0.189  0.575  0.197  184 THR LLL OG1 
3037 C CG2 . THR B 184 ? 2.375 2.406 2.311 0.229  0.597  0.198  184 THR LLL CG2 
3038 N N   . LEU B 185 ? 2.249 2.391 2.185 0.191  0.576  0.171  185 LEU LLL N   
3039 C CA  . LEU B 185 ? 2.439 2.632 2.384 0.204  0.576  0.165  185 LEU LLL CA  
3040 C C   . LEU B 185 ? 2.536 2.725 2.488 0.242  0.590  0.170  185 LEU LLL C   
3041 O O   . LEU B 185 ? 2.634 2.794 2.589 0.247  0.605  0.165  185 LEU LLL O   
3042 C CB  . LEU B 185 ? 2.400 2.619 2.347 0.184  0.579  0.150  185 LEU LLL CB  
3043 C CG  . LEU B 185 ? 2.348 2.626 2.306 0.193  0.580  0.140  185 LEU LLL CG  
3044 C CD1 . LEU B 185 ? 2.339 2.647 2.296 0.161  0.577  0.130  185 LEU LLL CD1 
3045 C CD2 . LEU B 185 ? 2.384 2.668 2.350 0.215  0.593  0.133  185 LEU LLL CD2 
3046 N N   . THR B 186 ? 2.563 2.784 2.516 0.269  0.587  0.178  186 THR LLL N   
3047 C CA  . THR B 186 ? 2.614 2.836 2.569 0.314  0.601  0.188  186 THR LLL CA  
3048 C C   . THR B 186 ? 2.514 2.808 2.476 0.330  0.598  0.176  186 THR LLL C   
3049 O O   . THR B 186 ? 2.442 2.792 2.410 0.317  0.583  0.166  186 THR LLL O   
3050 C CB  . THR B 186 ? 2.729 2.931 2.675 0.343  0.603  0.210  186 THR LLL CB  
3051 O OG1 . THR B 186 ? 2.802 3.014 2.746 0.391  0.619  0.221  186 THR LLL OG1 
3052 C CG2 . THR B 186 ? 2.682 2.926 2.626 0.336  0.583  0.210  186 THR LLL CG2 
3053 N N   . LEU B 187 ? 2.475 2.769 2.442 0.354  0.614  0.174  187 LEU LLL N   
3054 C CA  . LEU B 187 ? 2.447 2.809 2.420 0.385  0.614  0.167  187 LEU LLL CA  
3055 C C   . LEU B 187 ? 2.404 2.735 2.373 0.432  0.637  0.181  187 LEU LLL C   
3056 O O   . LEU B 187 ? 2.305 2.559 2.272 0.431  0.655  0.190  187 LEU LLL O   
3057 C CB  . LEU B 187 ? 2.513 2.919 2.497 0.354  0.608  0.142  187 LEU LLL CB  
3058 C CG  . LEU B 187 ? 2.489 2.849 2.475 0.323  0.617  0.133  187 LEU LLL CG  
3059 C CD1 . LEU B 187 ? 2.570 2.895 2.558 0.352  0.638  0.135  187 LEU LLL CD1 
3060 C CD2 . LEU B 187 ? 2.328 2.734 2.321 0.287  0.609  0.113  187 LEU LLL CD2 
3061 N N   . SER B 188 ? 2.425 2.815 2.395 0.474  0.639  0.181  188 SER LLL N   
3062 C CA  . SER B 188 ? 2.503 2.867 2.465 0.530  0.664  0.198  188 SER LLL CA  
3063 C C   . SER B 188 ? 2.570 2.891 2.543 0.516  0.682  0.185  188 SER LLL C   
3064 O O   . SER B 188 ? 2.609 2.946 2.593 0.470  0.670  0.162  188 SER LLL O   
3065 C CB  . SER B 188 ? 2.505 2.954 2.463 0.580  0.659  0.199  188 SER LLL CB  
3066 O OG  . SER B 188 ? 2.392 2.926 2.365 0.556  0.641  0.169  188 SER LLL OG  
3067 N N   . LYS B 189 ? 2.586 2.852 2.555 0.555  0.711  0.200  189 LYS LLL N   
3068 C CA  . LYS B 189 ? 2.535 2.765 2.516 0.550  0.732  0.185  189 LYS LLL CA  
3069 C C   . LYS B 189 ? 2.452 2.765 2.442 0.555  0.720  0.163  189 LYS LLL C   
3070 O O   . LYS B 189 ? 2.194 2.509 2.197 0.519  0.719  0.138  189 LYS LLL O   
3071 C CB  . LYS B 189 ? 2.571 2.729 2.548 0.599  0.770  0.208  189 LYS LLL CB  
3072 C CG  . LYS B 189 ? 2.595 2.704 2.588 0.596  0.798  0.191  189 LYS LLL CG  
3073 C CD  . LYS B 189 ? 2.624 2.675 2.610 0.655  0.838  0.214  189 LYS LLL CD  
3074 C CE  . LYS B 189 ? 2.596 2.601 2.603 0.650  0.867  0.191  189 LYS LLL CE  
3075 N NZ  . LYS B 189 ? 2.666 2.627 2.666 0.715  0.906  0.214  189 LYS LLL NZ  
3076 N N   . ALA B 190 ? 2.487 2.870 2.468 0.599  0.713  0.171  190 ALA LLL N   
3077 C CA  . ALA B 190 ? 2.448 2.923 2.438 0.609  0.702  0.149  190 ALA LLL CA  
3078 C C   . ALA B 190 ? 2.420 2.938 2.424 0.545  0.679  0.121  190 ALA LLL C   
3079 O O   . ALA B 190 ? 2.523 3.054 2.539 0.527  0.682  0.100  190 ALA LLL O   
3080 C CB  . ALA B 190 ? 2.349 2.905 2.328 0.661  0.692  0.159  190 ALA LLL CB  
3081 N N   . ASP B 191 ? 2.429 2.964 2.432 0.513  0.659  0.121  191 ASP LLL N   
3082 C CA  . ASP B 191 ? 2.424 2.991 2.437 0.454  0.642  0.098  191 ASP LLL CA  
3083 C C   . ASP B 191 ? 2.258 2.753 2.272 0.414  0.650  0.094  191 ASP LLL C   
3084 O O   . ASP B 191 ? 2.143 2.664 2.163 0.374  0.643  0.076  191 ASP LLL O   
3085 C CB  . ASP B 191 ? 2.657 3.244 2.667 0.432  0.624  0.101  191 ASP LLL CB  
3086 C CG  . ASP B 191 ? 2.845 3.510 2.856 0.470  0.614  0.102  191 ASP LLL CG  
3087 O OD1 . ASP B 191 ? 3.025 3.761 3.043 0.498  0.615  0.088  191 ASP LLL OD1 
3088 O OD2 . ASP B 191 ? 2.951 3.608 2.954 0.475  0.606  0.115  191 ASP LLL OD2 
3089 N N   . TYR B 192 ? 2.111 2.525 2.118 0.425  0.665  0.110  192 TYR LLL N   
3090 C CA  . TYR B 192 ? 2.127 2.480 2.137 0.388  0.672  0.102  192 TYR LLL CA  
3091 C C   . TYR B 192 ? 2.157 2.527 2.178 0.382  0.682  0.080  192 TYR LLL C   
3092 O O   . TYR B 192 ? 2.079 2.452 2.102 0.343  0.676  0.064  192 TYR LLL O   
3093 C CB  . TYR B 192 ? 2.230 2.498 2.237 0.400  0.691  0.118  192 TYR LLL CB  
3094 C CG  . TYR B 192 ? 2.226 2.445 2.240 0.364  0.699  0.102  192 TYR LLL CG  
3095 C CD1 . TYR B 192 ? 2.113 2.340 2.123 0.320  0.681  0.094  192 TYR LLL CD1 
3096 C CD2 . TYR B 192 ? 2.242 2.409 2.268 0.376  0.725  0.093  192 TYR LLL CD2 
3097 C CE1 . TYR B 192 ? 2.039 2.236 2.055 0.291  0.686  0.077  192 TYR LLL CE1 
3098 C CE2 . TYR B 192 ? 2.132 2.268 2.169 0.342  0.732  0.072  192 TYR LLL CE2 
3099 C CZ  . TYR B 192 ? 2.059 2.214 2.089 0.302  0.711  0.064  192 TYR LLL CZ  
3100 O OH  . TYR B 192 ? 2.045 2.179 2.085 0.275  0.718  0.041  192 TYR LLL OH  
3101 N N   . GLU B 193 ? 2.263 2.643 2.288 0.424  0.696  0.080  193 GLU LLL N   
3102 C CA  . GLU B 193 ? 2.340 2.731 2.378 0.426  0.709  0.058  193 GLU LLL CA  
3103 C C   . GLU B 193 ? 2.399 2.881 2.442 0.417  0.694  0.041  193 GLU LLL C   
3104 O O   . GLU B 193 ? 2.401 2.904 2.453 0.419  0.703  0.021  193 GLU LLL O   
3105 C CB  . GLU B 193 ? 2.425 2.776 2.465 0.479  0.736  0.068  193 GLU LLL CB  
3106 C CG  . GLU B 193 ? 2.439 2.699 2.474 0.488  0.755  0.088  193 GLU LLL CG  
3107 C CD  . GLU B 193 ? 2.582 2.796 2.617 0.545  0.787  0.105  193 GLU LLL CD  
3108 O OE1 . GLU B 193 ? 2.736 2.867 2.778 0.544  0.815  0.105  193 GLU LLL OE1 
3109 O OE2 . GLU B 193 ? 2.642 2.904 2.668 0.592  0.785  0.117  193 GLU LLL OE2 
3110 N N   . LYS B 194 ? 2.459 2.996 2.498 0.404  0.674  0.043  194 LYS LLL N   
3111 C CA  . LYS B 194 ? 2.427 3.051 2.474 0.386  0.663  0.023  194 LYS LLL CA  
3112 C C   . LYS B 194 ? 2.336 2.957 2.383 0.331  0.658  0.011  194 LYS LLL C   
3113 O O   . LYS B 194 ? 2.252 2.935 2.308 0.315  0.656  -0.007 194 LYS LLL O   
3114 C CB  . LYS B 194 ? 2.473 3.160 2.522 0.392  0.647  0.026  194 LYS LLL CB  
3115 C CG  . LYS B 194 ? 2.477 3.201 2.524 0.452  0.649  0.034  194 LYS LLL CG  
3116 C CD  . LYS B 194 ? 2.430 3.260 2.488 0.456  0.635  0.017  194 LYS LLL CD  
3117 C CE  . LYS B 194 ? 2.408 3.272 2.459 0.510  0.631  0.030  194 LYS LLL CE  
3118 N NZ  . LYS B 194 ? 2.363 3.209 2.407 0.492  0.619  0.042  194 LYS LLL NZ  
3119 N N   . HIS B 195 ? 2.283 2.842 2.321 0.306  0.656  0.022  195 HIS LLL N   
3120 C CA  . HIS B 195 ? 2.155 2.705 2.186 0.259  0.652  0.016  195 HIS LLL CA  
3121 C C   . HIS B 195 ? 2.106 2.601 2.135 0.255  0.662  0.011  195 HIS LLL C   
3122 O O   . HIS B 195 ? 2.038 2.490 2.072 0.283  0.673  0.015  195 HIS LLL O   
3123 C CB  . HIS B 195 ? 2.070 2.606 2.091 0.235  0.640  0.030  195 HIS LLL CB  
3124 C CG  . HIS B 195 ? 2.070 2.662 2.099 0.240  0.631  0.029  195 HIS LLL CG  
3125 N ND1 . HIS B 195 ? 2.066 2.732 2.108 0.247  0.633  0.011  195 HIS LLL ND1 
3126 C CD2 . HIS B 195 ? 2.116 2.710 2.143 0.239  0.622  0.040  195 HIS LLL CD2 
3127 C CE1 . HIS B 195 ? 2.111 2.824 2.161 0.250  0.625  0.008  195 HIS LLL CE1 
3128 N NE2 . HIS B 195 ? 2.151 2.820 2.192 0.246  0.618  0.026  195 HIS LLL NE2 
3129 N N   . LYS B 196 ? 2.126 2.626 2.149 0.224  0.662  -0.000 196 LYS LLL N   
3130 C CA  . LYS B 196 ? 2.228 2.687 2.252 0.220  0.671  -0.012 196 LYS LLL CA  
3131 C C   . LYS B 196 ? 2.231 2.663 2.240 0.191  0.663  -0.006 196 LYS LLL C   
3132 O O   . LYS B 196 ? 2.140 2.530 2.152 0.193  0.669  -0.011 196 LYS LLL O   
3133 C CB  . LYS B 196 ? 2.247 2.742 2.279 0.218  0.680  -0.037 196 LYS LLL CB  
3134 C CG  . LYS B 196 ? 2.309 2.766 2.357 0.231  0.696  -0.056 196 LYS LLL CG  
3135 C CD  . LYS B 196 ? 2.294 2.775 2.343 0.213  0.701  -0.084 196 LYS LLL CD  
3136 C CE  . LYS B 196 ? 2.270 2.739 2.343 0.232  0.721  -0.112 196 LYS LLL CE  
3137 N NZ  . LYS B 196 ? 2.289 2.811 2.366 0.221  0.723  -0.140 196 LYS LLL NZ  
3138 N N   . VAL B 197 ? 2.308 2.767 2.302 0.167  0.654  0.003  197 VAL LLL N   
3139 C CA  . VAL B 197 ? 2.361 2.797 2.336 0.144  0.647  0.011  197 VAL LLL CA  
3140 C C   . VAL B 197 ? 2.256 2.662 2.222 0.140  0.637  0.034  197 VAL LLL C   
3141 O O   . VAL B 197 ? 2.302 2.729 2.269 0.136  0.633  0.044  197 VAL LLL O   
3142 C CB  . VAL B 197 ? 2.364 2.840 2.323 0.123  0.648  0.008  197 VAL LLL CB  
3143 C CG1 . VAL B 197 ? 2.436 2.953 2.406 0.131  0.658  -0.015 197 VAL LLL CG1 
3144 C CG2 . VAL B 197 ? 2.380 2.875 2.328 0.106  0.646  0.025  197 VAL LLL CG2 
3145 N N   . TYR B 198 ? 2.195 2.557 2.157 0.140  0.634  0.039  198 TYR LLL N   
3146 C CA  . TYR B 198 ? 2.232 2.559 2.186 0.137  0.625  0.059  198 TYR LLL CA  
3147 C C   . TYR B 198 ? 2.276 2.589 2.209 0.118  0.619  0.064  198 TYR LLL C   
3148 O O   . TYR B 198 ? 2.238 2.545 2.170 0.117  0.622  0.050  198 TYR LLL O   
3149 C CB  . TYR B 198 ? 2.130 2.417 2.098 0.159  0.630  0.060  198 TYR LLL CB  
3150 C CG  . TYR B 198 ? 2.001 2.301 1.982 0.186  0.636  0.061  198 TYR LLL CG  
3151 C CD1 . TYR B 198 ? 2.097 2.414 2.092 0.201  0.649  0.045  198 TYR LLL CD1 
3152 C CD2 . TYR B 198 ? 1.975 2.279 1.956 0.198  0.629  0.078  198 TYR LLL CD2 
3153 C CE1 . TYR B 198 ? 2.166 2.501 2.171 0.230  0.654  0.048  198 TYR LLL CE1 
3154 C CE2 . TYR B 198 ? 1.976 2.302 1.967 0.227  0.634  0.079  198 TYR LLL CE2 
3155 C CZ  . TYR B 198 ? 2.064 2.406 2.067 0.245  0.647  0.065  198 TYR LLL CZ  
3156 O OH  . TYR B 198 ? 2.030 2.399 2.039 0.279  0.651  0.068  198 TYR LLL OH  
3157 N N   . ALA B 199 ? 2.243 2.556 2.160 0.103  0.612  0.082  199 ALA LLL N   
3158 C CA  . ALA B 199 ? 2.187 2.492 2.078 0.089  0.608  0.091  199 ALA LLL CA  
3159 C C   . ALA B 199 ? 2.088 2.360 1.969 0.083  0.600  0.111  199 ALA LLL C   
3160 O O   . ALA B 199 ? 1.986 2.260 1.877 0.082  0.598  0.118  199 ALA LLL O   
3161 C CB  . ALA B 199 ? 2.326 2.665 2.202 0.077  0.616  0.093  199 ALA LLL CB  
3162 N N   . CYS B 200 ? 2.079 2.331 1.943 0.081  0.595  0.117  200 CYS LLL N   
3163 C CA  . CYS B 200 ? 2.196 2.415 2.049 0.077  0.586  0.135  200 CYS LLL CA  
3164 C C   . CYS B 200 ? 2.241 2.458 2.062 0.069  0.587  0.148  200 CYS LLL C   
3165 O O   . CYS B 200 ? 2.214 2.444 2.022 0.074  0.587  0.140  200 CYS LLL O   
3166 C CB  . CYS B 200 ? 2.300 2.492 2.162 0.087  0.580  0.128  200 CYS LLL CB  
3167 S SG  . CYS B 200 ? 2.529 2.687 2.371 0.084  0.568  0.146  200 CYS LLL SG  
3168 N N   . GLU B 201 ? 2.324 2.529 2.134 0.057  0.591  0.167  201 GLU LLL N   
3169 C CA  . GLU B 201 ? 2.414 2.612 2.192 0.051  0.599  0.185  201 GLU LLL CA  
3170 C C   . GLU B 201 ? 2.270 2.427 2.035 0.051  0.593  0.202  201 GLU LLL C   
3171 O O   . GLU B 201 ? 2.229 2.369 2.010 0.042  0.591  0.205  201 GLU LLL O   
3172 C CB  . GLU B 201 ? 2.502 2.714 2.279 0.036  0.617  0.192  201 GLU LLL CB  
3173 C CG  . GLU B 201 ? 2.639 2.833 2.381 0.032  0.632  0.216  201 GLU LLL CG  
3174 C CD  . GLU B 201 ? 2.921 3.133 2.662 0.017  0.655  0.220  201 GLU LLL CD  
3175 O OE1 . GLU B 201 ? 3.125 3.372 2.857 0.023  0.661  0.215  201 GLU LLL OE1 
3176 O OE2 . GLU B 201 ? 3.015 3.210 2.767 -0.003 0.669  0.225  201 GLU LLL OE2 
3177 N N   . VAL B 202 ? 2.111 2.261 1.847 0.062  0.589  0.212  202 VAL LLL N   
3178 C CA  . VAL B 202 ? 2.013 2.128 1.734 0.067  0.581  0.226  202 VAL LLL CA  
3179 C C   . VAL B 202 ? 1.975 2.073 1.658 0.069  0.595  0.252  202 VAL LLL C   
3180 O O   . VAL B 202 ? 1.970 2.089 1.626 0.083  0.599  0.257  202 VAL LLL O   
3181 C CB  . VAL B 202 ? 2.034 2.158 1.754 0.081  0.566  0.212  202 VAL LLL CB  
3182 C CG1 . VAL B 202 ? 2.086 2.180 1.785 0.089  0.558  0.228  202 VAL LLL CG1 
3183 C CG2 . VAL B 202 ? 2.055 2.184 1.811 0.080  0.559  0.190  202 VAL LLL CG2 
3184 N N   . THR B 203 ? 1.998 2.057 1.679 0.058  0.603  0.269  203 THR LLL N   
3185 C CA  . THR B 203 ? 2.081 2.106 1.726 0.064  0.618  0.297  203 THR LLL CA  
3186 C C   . THR B 203 ? 2.183 2.179 1.820 0.074  0.603  0.303  203 THR LLL C   
3187 O O   . THR B 203 ? 2.283 2.263 1.947 0.063  0.594  0.294  203 THR LLL O   
3188 C CB  . THR B 203 ? 2.123 2.120 1.776 0.041  0.642  0.308  203 THR LLL CB  
3189 O OG1 . THR B 203 ? 2.351 2.380 2.006 0.034  0.657  0.303  203 THR LLL OG1 
3190 C CG2 . THR B 203 ? 2.189 2.135 1.808 0.046  0.662  0.339  203 THR LLL CG2 
3191 N N   . HIS B 204 ? 2.268 2.264 1.868 0.098  0.600  0.317  204 HIS LLL N   
3192 C CA  . HIS B 204 ? 2.171 2.142 1.758 0.112  0.588  0.325  204 HIS LLL CA  
3193 C C   . HIS B 204 ? 2.177 2.132 1.714 0.135  0.602  0.355  204 HIS LLL C   
3194 O O   . HIS B 204 ? 2.338 2.320 1.849 0.148  0.613  0.364  204 HIS LLL O   
3195 C CB  . HIS B 204 ? 2.095 2.101 1.696 0.121  0.563  0.300  204 HIS LLL CB  
3196 C CG  . HIS B 204 ? 2.200 2.190 1.789 0.135  0.550  0.305  204 HIS LLL CG  
3197 N ND1 . HIS B 204 ? 2.342 2.361 1.904 0.161  0.541  0.303  204 HIS LLL ND1 
3198 C CD2 . HIS B 204 ? 2.155 2.107 1.755 0.129  0.544  0.310  204 HIS LLL CD2 
3199 C CE1 . HIS B 204 ? 2.286 2.285 1.842 0.169  0.530  0.308  204 HIS LLL CE1 
3200 N NE2 . HIS B 204 ? 2.195 2.151 1.774 0.150  0.532  0.312  204 HIS LLL NE2 
3201 N N   . GLN B 205 ? 2.221 2.135 1.743 0.143  0.602  0.372  205 GLN LLL N   
3202 C CA  . GLN B 205 ? 2.403 2.293 1.873 0.172  0.617  0.405  205 GLN LLL CA  
3203 C C   . GLN B 205 ? 2.495 2.444 1.931 0.206  0.606  0.403  205 GLN LLL C   
3204 O O   . GLN B 205 ? 2.612 2.557 2.000 0.235  0.623  0.433  205 GLN LLL O   
3205 C CB  . GLN B 205 ? 2.418 2.263 1.888 0.175  0.612  0.413  205 GLN LLL CB  
3206 C CG  . GLN B 205 ? 2.455 2.253 1.877 0.200  0.634  0.451  205 GLN LLL CG  
3207 C CD  . GLN B 205 ? 2.468 2.232 1.897 0.203  0.623  0.450  205 GLN LLL CD  
3208 O OE1 . GLN B 205 ? 2.594 2.340 1.985 0.234  0.625  0.471  205 GLN LLL OE1 
3209 N NE2 . GLN B 205 ? 2.458 2.219 1.935 0.173  0.608  0.424  205 GLN LLL NE2 
3210 N N   . GLY B 206 ? 2.447 2.451 1.907 0.206  0.580  0.369  206 GLY LLL N   
3211 C CA  . GLY B 206 ? 2.347 2.418 1.785 0.235  0.567  0.356  206 GLY LLL CA  
3212 C C   . GLY B 206 ? 2.348 2.467 1.782 0.237  0.575  0.348  206 GLY LLL C   
3213 O O   . GLY B 206 ? 2.269 2.454 1.687 0.260  0.565  0.332  206 GLY LLL O   
3214 N N   . LEU B 207 ? 2.417 2.511 1.866 0.212  0.593  0.354  207 LEU LLL N   
3215 C CA  . LEU B 207 ? 2.436 2.575 1.889 0.207  0.601  0.343  207 LEU LLL CA  
3216 C C   . LEU B 207 ? 2.514 2.620 1.936 0.208  0.634  0.380  207 LEU LLL C   
3217 O O   . LEU B 207 ? 2.392 2.446 1.836 0.180  0.648  0.389  207 LEU LLL O   
3218 C CB  . LEU B 207 ? 2.388 2.530 1.896 0.174  0.594  0.312  207 LEU LLL CB  
3219 C CG  . LEU B 207 ? 2.451 2.614 1.994 0.170  0.568  0.277  207 LEU LLL CG  
3220 C CD1 . LEU B 207 ? 2.459 2.597 2.049 0.141  0.566  0.262  207 LEU LLL CD1 
3221 C CD2 . LEU B 207 ? 2.485 2.719 2.030 0.183  0.559  0.245  207 LEU LLL CD2 
3222 N N   . SER B 208 ? 2.620 2.762 1.997 0.239  0.645  0.398  208 SER LLL N   
3223 C CA  . SER B 208 ? 2.704 2.822 2.042 0.248  0.680  0.437  208 SER LLL CA  
3224 C C   . SER B 208 ? 2.601 2.706 1.974 0.209  0.697  0.429  208 SER LLL C   
3225 O O   . SER B 208 ? 2.527 2.580 1.888 0.198  0.729  0.458  208 SER LLL O   
3226 C CB  . SER B 208 ? 2.860 3.043 2.149 0.289  0.683  0.447  208 SER LLL CB  
3227 O OG  . SER B 208 ? 2.954 3.218 2.269 0.291  0.655  0.401  208 SER LLL OG  
3228 N N   . SER B 209 ? 2.528 2.678 1.945 0.190  0.676  0.388  209 SER LLL N   
3229 C CA  . SER B 209 ? 2.559 2.709 2.013 0.156  0.687  0.373  209 SER LLL CA  
3230 C C   . SER B 209 ? 2.338 2.505 1.846 0.136  0.660  0.333  209 SER LLL C   
3231 O O   . SER B 209 ? 2.233 2.435 1.749 0.149  0.636  0.309  209 SER LLL O   
3232 C CB  . SER B 209 ? 2.762 2.965 2.198 0.167  0.699  0.373  209 SER LLL CB  
3233 O OG  . SER B 209 ? 2.895 3.167 2.337 0.184  0.673  0.341  209 SER LLL OG  
3234 N N   . PRO B 210 ? 2.288 2.433 1.836 0.105  0.665  0.323  210 PRO LLL N   
3235 C CA  . PRO B 210 ? 2.230 2.390 1.827 0.090  0.645  0.289  210 PRO LLL CA  
3236 C C   . PRO B 210 ? 2.282 2.500 1.889 0.101  0.630  0.259  210 PRO LLL C   
3237 O O   . PRO B 210 ? 2.540 2.795 2.138 0.104  0.640  0.256  210 PRO LLL O   
3238 C CB  . PRO B 210 ? 2.160 2.311 1.786 0.062  0.659  0.284  210 PRO LLL CB  
3239 C CG  . PRO B 210 ? 2.262 2.369 1.865 0.054  0.687  0.316  210 PRO LLL CG  
3240 C CD  . PRO B 210 ? 2.385 2.493 1.935 0.083  0.695  0.342  210 PRO LLL CD  
3241 N N   . VAL B 211 ? 2.257 2.480 1.883 0.106  0.608  0.237  211 VAL LLL N   
3242 C CA  . VAL B 211 ? 2.188 2.458 1.837 0.112  0.596  0.201  211 VAL LLL CA  
3243 C C   . VAL B 211 ? 2.079 2.341 1.772 0.094  0.595  0.183  211 VAL LLL C   
3244 O O   . VAL B 211 ? 2.001 2.228 1.713 0.086  0.589  0.186  211 VAL LLL O   
3245 C CB  . VAL B 211 ? 2.200 2.479 1.849 0.125  0.579  0.185  211 VAL LLL CB  
3246 C CG1 . VAL B 211 ? 2.166 2.396 1.821 0.121  0.570  0.196  211 VAL LLL CG1 
3247 C CG2 . VAL B 211 ? 2.198 2.511 1.882 0.123  0.571  0.144  211 VAL LLL CG2 
3248 N N   . THR B 212 ? 2.068 2.366 1.774 0.091  0.602  0.166  212 THR LLL N   
3249 C CA  . THR B 212 ? 2.071 2.371 1.818 0.082  0.601  0.145  212 THR LLL CA  
3250 C C   . THR B 212 ? 2.025 2.349 1.792 0.090  0.595  0.112  212 THR LLL C   
3251 O O   . THR B 212 ? 2.038 2.405 1.792 0.099  0.596  0.098  212 THR LLL O   
3252 C CB  . THR B 212 ? 2.190 2.512 1.941 0.073  0.615  0.147  212 THR LLL CB  
3253 O OG1 . THR B 212 ? 2.473 2.776 2.200 0.064  0.628  0.176  212 THR LLL OG1 
3254 C CG2 . THR B 212 ? 2.130 2.449 1.918 0.067  0.615  0.133  212 THR LLL CG2 
3255 N N   . LYS B 213 ? 2.046 2.347 1.846 0.088  0.591  0.099  213 LYS LLL N   
3256 C CA  . LYS B 213 ? 2.124 2.438 1.953 0.093  0.592  0.065  213 LYS LLL CA  
3257 C C   . LYS B 213 ? 2.201 2.502 2.058 0.093  0.599  0.059  213 LYS LLL C   
3258 O O   . LYS B 213 ? 2.402 2.670 2.269 0.093  0.597  0.074  213 LYS LLL O   
3259 C CB  . LYS B 213 ? 2.156 2.444 1.992 0.095  0.585  0.057  213 LYS LLL CB  
3260 C CG  . LYS B 213 ? 2.223 2.526 2.028 0.100  0.576  0.063  213 LYS LLL CG  
3261 C CD  . LYS B 213 ? 2.242 2.593 2.051 0.105  0.576  0.028  213 LYS LLL CD  
3262 C CE  . LYS B 213 ? 2.215 2.587 1.995 0.115  0.565  0.032  213 LYS LLL CE  
3263 N NZ  . LYS B 213 ? 2.229 2.655 2.023 0.119  0.564  -0.012 213 LYS LLL NZ  
3264 N N   . SER B 214 ? 2.175 2.509 2.046 0.095  0.608  0.038  214 SER LLL N   
3265 C CA  . SER B 214 ? 2.108 2.443 2.002 0.099  0.616  0.033  214 SER LLL CA  
3266 C C   . SER B 214 ? 2.095 2.429 2.019 0.107  0.626  0.001  214 SER LLL C   
3267 O O   . SER B 214 ? 2.182 2.524 2.109 0.105  0.626  -0.020 214 SER LLL O   
3268 C CB  . SER B 214 ? 2.167 2.543 2.050 0.095  0.621  0.036  214 SER LLL CB  
3269 O OG  . SER B 214 ? 2.063 2.478 1.933 0.095  0.623  0.020  214 SER LLL OG  
3270 N N   . PHE B 215 ? 2.075 2.402 2.020 0.117  0.635  -0.003 215 PHE LLL N   
3271 C CA  . PHE B 215 ? 2.186 2.513 2.160 0.126  0.650  -0.034 215 PHE LLL CA  
3272 C C   . PHE B 215 ? 2.236 2.576 2.221 0.139  0.657  -0.031 215 PHE LLL C   
3273 O O   . PHE B 215 ? 2.401 2.740 2.379 0.143  0.651  -0.007 215 PHE LLL O   
3274 C CB  . PHE B 215 ? 2.210 2.484 2.204 0.132  0.659  -0.040 215 PHE LLL CB  
3275 C CG  . PHE B 215 ? 2.256 2.490 2.254 0.147  0.661  -0.014 215 PHE LLL CG  
3276 C CD1 . PHE B 215 ? 2.399 2.615 2.381 0.144  0.647  0.013  215 PHE LLL CD1 
3277 C CD2 . PHE B 215 ? 2.306 2.528 2.322 0.168  0.676  -0.016 215 PHE LLL CD2 
3278 C CE1 . PHE B 215 ? 2.496 2.686 2.480 0.159  0.648  0.036  215 PHE LLL CE1 
3279 C CE2 . PHE B 215 ? 2.393 2.589 2.409 0.187  0.677  0.010  215 PHE LLL CE2 
3280 C CZ  . PHE B 215 ? 2.479 2.662 2.479 0.182  0.662  0.034  215 PHE LLL CZ  
3281 N N   . ASN B 216 ? 2.223 2.580 2.227 0.146  0.670  -0.059 216 ASN LLL N   
3282 C CA  . ASN B 216 ? 2.267 2.638 2.284 0.163  0.679  -0.061 216 ASN LLL CA  
3283 C C   . ASN B 216 ? 2.261 2.580 2.301 0.184  0.696  -0.063 216 ASN LLL C   
3284 O O   . ASN B 216 ? 2.375 2.663 2.430 0.180  0.707  -0.082 216 ASN LLL O   
3285 C CB  . ASN B 216 ? 2.322 2.743 2.345 0.159  0.685  -0.089 216 ASN LLL CB  
3286 C CG  . ASN B 216 ? 2.255 2.725 2.251 0.142  0.673  -0.080 216 ASN LLL CG  
3287 O OD1 . ASN B 216 ? 2.308 2.813 2.298 0.142  0.672  -0.073 216 ASN LLL OD1 
3288 N ND2 . ASN B 216 ? 2.231 2.702 2.210 0.129  0.666  -0.080 216 ASN LLL ND2 
3289 N N   . ARG B 217 ? 2.213 2.528 2.257 0.207  0.699  -0.046 217 ARG LLL N   
3290 C CA  . ARG B 217 ? 2.322 2.584 2.380 0.235  0.717  -0.038 217 ARG LLL CA  
3291 C C   . ARG B 217 ? 2.437 2.674 2.520 0.242  0.743  -0.069 217 ARG LLL C   
3292 O O   . ARG B 217 ? 2.606 2.879 2.697 0.248  0.748  -0.088 217 ARG LLL O   
3293 C CB  . ARG B 217 ? 2.329 2.612 2.383 0.264  0.715  -0.019 217 ARG LLL CB  
3294 C CG  . ARG B 217 ? 2.471 2.704 2.535 0.301  0.735  -0.006 217 ARG LLL CG  
3295 C CD  . ARG B 217 ? 2.461 2.721 2.513 0.330  0.726  0.020  217 ARG LLL CD  
3296 N NE  . ARG B 217 ? 2.485 2.820 2.535 0.324  0.711  0.012  217 ARG LLL NE  
3297 C CZ  . ARG B 217 ? 2.778 3.145 2.838 0.340  0.720  -0.005 217 ARG LLL CZ  
3298 N NH1 . ARG B 217 ? 2.993 3.322 3.067 0.363  0.745  -0.016 217 ARG LLL NH1 
3299 N NH2 . ARG B 217 ? 2.807 3.245 2.865 0.331  0.708  -0.013 217 ARG LLL NH2 
3300 N N   . GLY B 218 ? 2.615 2.793 2.712 0.241  0.760  -0.076 218 GLY LLL N   
3301 C CA  . GLY B 218 ? 2.730 2.872 2.858 0.243  0.791  -0.108 218 GLY LLL CA  
3302 C C   . GLY B 218 ? 2.777 2.964 2.917 0.218  0.789  -0.152 218 GLY LLL C   
3303 O O   . GLY B 218 ? 2.971 3.158 3.135 0.226  0.811  -0.181 218 GLY LLL O   
3304 N N   . GLU B 219 ? 2.683 2.909 2.809 0.192  0.767  -0.157 219 GLU LLL N   
3305 C CA  . GLU B 219 ? 2.624 2.899 2.759 0.170  0.766  -0.200 219 GLU LLL CA  
3306 C C   . GLU B 219 ? 2.596 2.869 2.729 0.148  0.758  -0.211 219 GLU LLL C   
3307 O O   . GLU B 219 ? 2.533 2.795 2.696 0.137  0.777  -0.250 219 GLU LLL O   
3308 C CB  . GLU B 219 ? 2.650 2.997 2.761 0.167  0.745  -0.195 219 GLU LLL CB  
3309 C CG  . GLU B 219 ? 2.697 3.054 2.810 0.189  0.750  -0.182 219 GLU LLL CG  
3310 C CD  . GLU B 219 ? 2.713 3.144 2.816 0.184  0.740  -0.194 219 GLU LLL CD  
3311 O OE1 . GLU B 219 ? 2.911 3.356 3.028 0.199  0.752  -0.209 219 GLU LLL OE1 
3312 O OE2 . GLU B 219 ? 2.503 2.976 2.581 0.166  0.722  -0.188 219 GLU LLL OE2 
3313 N N   . ASN C 3   ? 2.576 2.637 3.007 0.288  -0.619 -0.619 334 ASN EEE N   
3314 C CA  . ASN C 3   ? 2.462 2.526 2.864 0.281  -0.581 -0.595 334 ASN EEE CA  
3315 C C   . ASN C 3   ? 2.310 2.362 2.606 0.261  -0.526 -0.551 334 ASN EEE C   
3316 O O   . ASN C 3   ? 2.394 2.393 2.591 0.267  -0.530 -0.512 334 ASN EEE O   
3317 C CB  . ASN C 3   ? 2.579 2.586 2.951 0.308  -0.633 -0.582 334 ASN EEE CB  
3318 C CG  . ASN C 3   ? 2.757 2.686 3.042 0.328  -0.695 -0.561 334 ASN EEE CG  
3319 O OD1 . ASN C 3   ? 2.624 2.541 2.863 0.322  -0.695 -0.555 334 ASN EEE OD1 
3320 N ND2 . ASN C 3   ? 2.831 2.702 3.091 0.351  -0.750 -0.551 334 ASN EEE ND2 
3321 N N   . LEU C 4   ? 2.201 2.298 2.521 0.237  -0.479 -0.558 335 LEU EEE N   
3322 C CA  . LEU C 4   ? 2.244 2.341 2.487 0.217  -0.424 -0.522 335 LEU EEE CA  
3323 C C   . LEU C 4   ? 2.337 2.457 2.567 0.204  -0.382 -0.504 335 LEU EEE C   
3324 O O   . LEU C 4   ? 2.602 2.767 2.913 0.197  -0.371 -0.533 335 LEU EEE O   
3325 C CB  . LEU C 4   ? 2.235 2.375 2.532 0.195  -0.393 -0.543 335 LEU EEE CB  
3326 C CG  . LEU C 4   ? 2.248 2.385 2.478 0.176  -0.344 -0.510 335 LEU EEE CG  
3327 C CD1 . LEU C 4   ? 2.353 2.433 2.500 0.188  -0.364 -0.488 335 LEU EEE CD1 
3328 C CD2 . LEU C 4   ? 2.214 2.402 2.513 0.148  -0.305 -0.533 335 LEU EEE CD2 
3329 N N   . CYS C 5   ? 2.468 2.561 2.603 0.200  -0.359 -0.460 336 CYS EEE N   
3330 C CA  . CYS C 5   ? 2.411 2.525 2.527 0.186  -0.321 -0.440 336 CYS EEE CA  
3331 C C   . CYS C 5   ? 2.296 2.471 2.461 0.158  -0.271 -0.452 336 CYS EEE C   
3332 O O   . CYS C 5   ? 2.405 2.591 2.568 0.146  -0.251 -0.449 336 CYS EEE O   
3333 C CB  . CYS C 5   ? 2.382 2.460 2.395 0.187  -0.306 -0.393 336 CYS EEE CB  
3334 S SG  . CYS C 5   ? 2.652 2.653 2.588 0.211  -0.353 -0.371 336 CYS EEE SG  
3335 N N   . PRO C 6   ? 2.214 2.427 2.420 0.145  -0.249 -0.466 337 PRO EEE N   
3336 C CA  . PRO C 6   ? 2.127 2.395 2.370 0.115  -0.202 -0.478 337 PRO EEE CA  
3337 C C   . PRO C 6   ? 2.012 2.281 2.180 0.098  -0.165 -0.436 337 PRO EEE C   
3338 O O   . PRO C 6   ? 2.011 2.311 2.182 0.077  -0.135 -0.435 337 PRO EEE O   
3339 C CB  . PRO C 6   ? 2.291 2.589 2.600 0.111  -0.200 -0.513 337 PRO EEE CB  
3340 C CG  . PRO C 6   ? 2.326 2.582 2.584 0.131  -0.226 -0.489 337 PRO EEE CG  
3341 C CD  . PRO C 6   ? 2.280 2.481 2.492 0.156  -0.267 -0.470 337 PRO EEE CD  
3342 N N   . PHE C 7   ? 2.058 2.293 2.162 0.106  -0.169 -0.402 338 PHE EEE N   
3343 C CA  . PHE C 7   ? 2.084 2.322 2.128 0.093  -0.137 -0.363 338 PHE EEE CA  
3344 C C   . PHE C 7   ? 2.050 2.325 2.123 0.064  -0.102 -0.371 338 PHE EEE C   
3345 O O   . PHE C 7   ? 1.970 2.260 2.009 0.047  -0.075 -0.346 338 PHE EEE O   
3346 C CB  . PHE C 7   ? 2.118 2.314 2.103 0.109  -0.147 -0.334 338 PHE EEE CB  
3347 C CG  . PHE C 7   ? 2.115 2.275 2.043 0.128  -0.165 -0.310 338 PHE EEE CG  
3348 C CD1 . PHE C 7   ? 2.183 2.347 2.108 0.128  -0.168 -0.308 338 PHE EEE CD1 
3349 C CD2 . PHE C 7   ? 1.991 2.110 1.866 0.143  -0.174 -0.291 338 PHE EEE CD2 
3350 C CE1 . PHE C 7   ? 2.278 2.405 2.146 0.141  -0.181 -0.285 338 PHE EEE CE1 
3351 C CE2 . PHE C 7   ? 2.168 2.253 1.986 0.156  -0.184 -0.270 338 PHE EEE CE2 
3352 C CZ  . PHE C 7   ? 2.282 2.371 2.096 0.154  -0.188 -0.266 338 PHE EEE CZ  
3353 N N   . GLY C 8   ? 2.090 2.378 2.222 0.058  -0.103 -0.404 339 GLY EEE N   
3354 C CA  . GLY C 8   ? 2.163 2.484 2.325 0.025  -0.067 -0.417 339 GLY EEE CA  
3355 C C   . GLY C 8   ? 2.138 2.499 2.312 0.000  -0.038 -0.427 339 GLY EEE C   
3356 O O   . GLY C 8   ? 2.051 2.425 2.191 -0.027 -0.006 -0.407 339 GLY EEE O   
3357 N N   . GLU C 9   ? 2.187 2.563 2.406 0.010  -0.052 -0.458 340 GLU EEE N   
3358 C CA  . GLU C 9   ? 2.206 2.618 2.439 -0.010 -0.028 -0.474 340 GLU EEE CA  
3359 C C   . GLU C 9   ? 2.053 2.457 2.205 -0.020 -0.014 -0.429 340 GLU EEE C   
3360 O O   . GLU C 9   ? 2.390 2.823 2.532 -0.049 0.018  -0.432 340 GLU EEE O   
3361 C CB  . GLU C 9   ? 2.318 2.729 2.595 0.011  -0.055 -0.502 340 GLU EEE CB  
3362 C CG  . GLU C 9   ? 2.444 2.876 2.821 0.018  -0.067 -0.557 340 GLU EEE CG  
3363 C CD  . GLU C 9   ? 2.437 2.866 2.862 0.040  -0.096 -0.585 340 GLU EEE CD  
3364 O OE1 . GLU C 9   ? 2.378 2.796 2.762 0.042  -0.095 -0.567 340 GLU EEE OE1 
3365 O OE2 . GLU C 9   ? 2.469 2.906 2.977 0.057  -0.122 -0.625 340 GLU EEE OE2 
3366 N N   . VAL C 10  ? 1.781 2.150 1.880 0.004  -0.036 -0.391 341 VAL EEE N   
3367 C CA  . VAL C 10  ? 1.763 2.127 1.796 -0.000 -0.029 -0.351 341 VAL EEE CA  
3368 C C   . VAL C 10  ? 1.807 2.173 1.798 -0.018 -0.007 -0.318 341 VAL EEE C   
3369 O O   . VAL C 10  ? 2.174 2.564 2.142 -0.044 0.015  -0.309 341 VAL EEE O   
3370 C CB  . VAL C 10  ? 1.624 1.952 1.625 0.030  -0.059 -0.329 341 VAL EEE CB  
3371 C CG1 . VAL C 10  ? 1.515 1.843 1.459 0.026  -0.050 -0.289 341 VAL EEE CG1 
3372 C CG2 . VAL C 10  ? 1.569 1.888 1.605 0.045  -0.083 -0.357 341 VAL EEE CG2 
3373 N N   . PHE C 11  ? 1.721 2.061 1.700 -0.005 -0.015 -0.302 342 PHE EEE N   
3374 C CA  . PHE C 11  ? 1.713 2.042 1.649 -0.013 -0.002 -0.264 342 PHE EEE CA  
3375 C C   . PHE C 11  ? 1.813 2.157 1.761 -0.046 0.025  -0.274 342 PHE EEE C   
3376 O O   . PHE C 11  ? 1.982 2.323 1.888 -0.062 0.039  -0.242 342 PHE EEE O   
3377 C CB  . PHE C 11  ? 1.810 2.101 1.732 0.014  -0.019 -0.248 342 PHE EEE CB  
3378 C CG  . PHE C 11  ? 1.759 2.029 1.649 0.041  -0.038 -0.228 342 PHE EEE CG  
3379 C CD1 . PHE C 11  ? 1.654 1.912 1.556 0.059  -0.060 -0.247 342 PHE EEE CD1 
3380 C CD2 . PHE C 11  ? 1.790 2.052 1.640 0.048  -0.033 -0.190 342 PHE EEE CD2 
3381 C CE1 . PHE C 11  ? 1.607 1.844 1.473 0.079  -0.072 -0.227 342 PHE EEE CE1 
3382 C CE2 . PHE C 11  ? 1.749 1.996 1.574 0.069  -0.044 -0.174 342 PHE EEE CE2 
3383 C CZ  . PHE C 11  ? 1.648 1.881 1.476 0.083  -0.062 -0.192 342 PHE EEE CZ  
3384 N N   . ASN C 12  ? 1.822 2.179 1.825 -0.056 0.031  -0.315 343 ASN EEE N   
3385 C CA  . ASN C 12  ? 1.898 2.266 1.916 -0.090 0.060  -0.328 343 ASN EEE CA  
3386 C C   . ASN C 12  ? 1.951 2.360 1.986 -0.123 0.089  -0.356 343 ASN EEE C   
3387 O O   . ASN C 12  ? 1.922 2.344 1.964 -0.158 0.120  -0.369 343 ASN EEE O   
3388 C CB  . ASN C 12  ? 1.984 2.340 2.054 -0.082 0.052  -0.355 343 ASN EEE CB  
3389 C CG  . ASN C 12  ? 2.079 2.392 2.118 -0.068 0.040  -0.324 343 ASN EEE CG  
3390 O OD1 . ASN C 12  ? 2.296 2.590 2.277 -0.067 0.044  -0.281 343 ASN EEE OD1 
3391 N ND2 . ASN C 12  ? 1.920 2.217 1.999 -0.057 0.026  -0.347 343 ASN EEE ND2 
3392 N N   . ALA C 13  ? 1.954 2.381 1.991 -0.114 0.081  -0.365 344 ALA EEE N   
3393 C CA  . ALA C 13  ? 1.829 2.293 1.878 -0.142 0.106  -0.394 344 ALA EEE CA  
3394 C C   . ALA C 13  ? 1.919 2.390 1.916 -0.186 0.141  -0.377 344 ALA EEE C   
3395 O O   . ALA C 13  ? 1.916 2.363 1.848 -0.186 0.135  -0.328 344 ALA EEE O   
3396 C CB  . ALA C 13  ? 1.740 2.207 1.766 -0.128 0.090  -0.385 344 ALA EEE CB  
3397 N N   . THR C 14  ? 2.058 2.559 2.080 -0.221 0.176  -0.416 345 THR EEE N   
3398 C CA  . THR C 14  ? 2.241 2.750 2.203 -0.269 0.213  -0.404 345 THR EEE CA  
3399 C C   . THR C 14  ? 2.524 3.038 2.421 -0.276 0.208  -0.381 345 THR EEE C   
3400 O O   . THR C 14  ? 2.646 3.142 2.465 -0.294 0.210  -0.336 345 THR EEE O   
3401 C CB  . THR C 14  ? 2.179 2.722 2.193 -0.305 0.255  -0.461 345 THR EEE CB  
3402 O OG1 . THR C 14  ? 2.149 2.720 2.242 -0.282 0.245  -0.509 345 THR EEE OG1 
3403 C CG2 . THR C 14  ? 2.199 2.732 2.250 -0.315 0.268  -0.470 345 THR EEE CG2 
3404 N N   . ARG C 15  ? 2.703 3.238 2.631 -0.261 0.199  -0.409 346 ARG EEE N   
3405 C CA  . ARG C 15  ? 2.706 3.250 2.581 -0.270 0.195  -0.394 346 ARG EEE CA  
3406 C C   . ARG C 15  ? 2.313 2.838 2.180 -0.229 0.153  -0.362 346 ARG EEE C   
3407 O O   . ARG C 15  ? 2.085 2.606 2.010 -0.195 0.132  -0.380 346 ARG EEE O   
3408 C CB  . ARG C 15  ? 3.038 3.615 2.950 -0.287 0.217  -0.450 346 ARG EEE CB  
3409 C CG  . ARG C 15  ? 3.194 3.778 3.060 -0.293 0.208  -0.441 346 ARG EEE CG  
3410 C CD  . ARG C 15  ? 3.194 3.808 3.092 -0.314 0.234  -0.498 346 ARG EEE CD  
3411 N NE  . ARG C 15  ? 3.235 3.868 3.108 -0.363 0.281  -0.524 346 ARG EEE NE  
3412 C CZ  . ARG C 15  ? 3.221 3.853 3.001 -0.404 0.299  -0.501 346 ARG EEE CZ  
3413 N NH1 . ARG C 15  ? 3.204 3.821 2.914 -0.400 0.270  -0.453 346 ARG EEE NH1 
3414 N NH2 . ARG C 15  ? 3.203 3.849 2.960 -0.452 0.345  -0.528 346 ARG EEE NH2 
3415 N N   . PHE C 16  ? 2.116 2.633 1.915 -0.233 0.141  -0.316 347 PHE EEE N   
3416 C CA  . PHE C 16  ? 2.100 2.607 1.889 -0.201 0.108  -0.286 347 PHE EEE CA  
3417 C C   . PHE C 16  ? 2.032 2.560 1.791 -0.220 0.109  -0.290 347 PHE EEE C   
3418 O O   . PHE C 16  ? 2.198 2.739 1.912 -0.257 0.129  -0.291 347 PHE EEE O   
3419 C CB  . PHE C 16  ? 2.136 2.619 1.887 -0.187 0.090  -0.232 347 PHE EEE CB  
3420 C CG  . PHE C 16  ? 2.017 2.476 1.806 -0.148 0.072  -0.227 347 PHE EEE CG  
3421 C CD1 . PHE C 16  ? 1.902 2.352 1.734 -0.145 0.081  -0.254 347 PHE EEE CD1 
3422 C CD2 . PHE C 16  ? 1.872 2.316 1.651 -0.118 0.048  -0.196 347 PHE EEE CD2 
3423 C CE1 . PHE C 16  ? 1.750 2.174 1.608 -0.111 0.062  -0.251 347 PHE EEE CE1 
3424 C CE2 . PHE C 16  ? 1.722 2.141 1.526 -0.085 0.033  -0.193 347 PHE EEE CE2 
3425 C CZ  . PHE C 16  ? 1.805 2.213 1.645 -0.082 0.039  -0.219 347 PHE EEE CZ  
3426 N N   . ALA C 17  ? 1.959 2.488 1.739 -0.197 0.089  -0.293 348 ALA EEE N   
3427 C CA  . ALA C 17  ? 1.850 2.397 1.611 -0.212 0.087  -0.301 348 ALA EEE CA  
3428 C C   . ALA C 17  ? 1.795 2.347 1.493 -0.224 0.075  -0.255 348 ALA EEE C   
3429 O O   . ALA C 17  ? 1.595 2.133 1.275 -0.210 0.062  -0.215 348 ALA EEE O   
3430 C CB  . ALA C 17  ? 1.883 2.418 1.683 -0.183 0.067  -0.312 348 ALA EEE CB  
3431 N N   . SER C 18  ? 1.941 2.513 1.609 -0.250 0.077  -0.263 349 SER EEE N   
3432 C CA  . SER C 18  ? 1.973 2.554 1.591 -0.258 0.056  -0.221 349 SER EEE CA  
3433 C C   . SER C 18  ? 1.828 2.405 1.479 -0.225 0.032  -0.205 349 SER EEE C   
3434 O O   . SER C 18  ? 1.594 2.163 1.289 -0.210 0.034  -0.234 349 SER EEE O   
3435 C CB  . SER C 18  ? 2.058 2.661 1.632 -0.298 0.064  -0.237 349 SER EEE CB  
3436 O OG  . SER C 18  ? 2.379 2.982 1.903 -0.332 0.084  -0.238 349 SER EEE OG  
3437 N N   . VAL C 19  ? 1.788 2.368 1.422 -0.213 0.011  -0.161 350 VAL EEE N   
3438 C CA  . VAL C 19  ? 1.711 2.286 1.377 -0.181 -0.006 -0.143 350 VAL EEE CA  
3439 C C   . VAL C 19  ? 1.632 2.219 1.312 -0.189 -0.010 -0.165 350 VAL EEE C   
3440 O O   . VAL C 19  ? 1.708 2.279 1.419 -0.167 -0.014 -0.169 350 VAL EEE O   
3441 C CB  . VAL C 19  ? 1.734 2.316 1.385 -0.170 -0.025 -0.096 350 VAL EEE CB  
3442 C CG1 . VAL C 19  ? 1.872 2.483 1.487 -0.198 -0.039 -0.080 350 VAL EEE CG1 
3443 C CG2 . VAL C 19  ? 1.678 2.255 1.364 -0.138 -0.036 -0.081 350 VAL EEE CG2 
3444 N N   . TYR C 20  ? 1.854 2.464 1.507 -0.222 -0.008 -0.177 351 TYR EEE N   
3445 C CA  . TYR C 20  ? 1.929 2.549 1.594 -0.234 -0.011 -0.199 351 TYR EEE CA  
3446 C C   . TYR C 20  ? 1.801 2.397 1.502 -0.225 0.003  -0.243 351 TYR EEE C   
3447 O O   . TYR C 20  ? 1.892 2.478 1.618 -0.219 -0.002 -0.255 351 TYR EEE O   
3448 C CB  . TYR C 20  ? 1.978 2.626 1.599 -0.274 -0.013 -0.206 351 TYR EEE CB  
3449 C CG  . TYR C 20  ? 1.935 2.582 1.537 -0.302 0.012  -0.251 351 TYR EEE CG  
3450 C CD1 . TYR C 20  ? 1.837 2.482 1.405 -0.318 0.028  -0.252 351 TYR EEE CD1 
3451 C CD2 . TYR C 20  ? 1.897 2.543 1.522 -0.313 0.022  -0.294 351 TYR EEE CD2 
3452 C CE1 . TYR C 20  ? 1.888 2.536 1.445 -0.346 0.057  -0.298 351 TYR EEE CE1 
3453 C CE2 . TYR C 20  ? 1.938 2.586 1.556 -0.337 0.048  -0.341 351 TYR EEE CE2 
3454 C CZ  . TYR C 20  ? 1.952 2.603 1.536 -0.355 0.067  -0.344 351 TYR EEE CZ  
3455 O OH  . TYR C 20  ? 2.028 2.684 1.610 -0.381 0.098  -0.395 351 TYR EEE OH  
3456 N N   . ALA C 21  ? 1.629 2.216 1.338 -0.227 0.021  -0.267 352 ALA EEE N   
3457 C CA  . ALA C 21  ? 1.770 2.341 1.522 -0.219 0.032  -0.313 352 ALA EEE CA  
3458 C C   . ALA C 21  ? 1.801 2.347 1.584 -0.188 0.030  -0.309 352 ALA EEE C   
3459 O O   . ALA C 21  ? 1.589 2.134 1.399 -0.191 0.046  -0.343 352 ALA EEE O   
3460 C CB  . ALA C 21  ? 2.032 2.620 1.776 -0.251 0.057  -0.354 352 ALA EEE CB  
3461 N N   . TRP C 22  ? 2.014 2.544 1.796 -0.162 0.013  -0.271 353 TRP EEE N   
3462 C CA  . TRP C 22  ? 1.968 2.474 1.764 -0.132 0.007  -0.256 353 TRP EEE CA  
3463 C C   . TRP C 22  ? 1.955 2.435 1.796 -0.114 0.005  -0.292 353 TRP EEE C   
3464 O O   . TRP C 22  ? 2.052 2.523 1.913 -0.114 -0.000 -0.315 353 TRP EEE O   
3465 C CB  . TRP C 22  ? 2.004 2.498 1.788 -0.110 -0.009 -0.215 353 TRP EEE CB  
3466 C CG  . TRP C 22  ? 2.037 2.521 1.825 -0.106 -0.019 -0.212 353 TRP EEE CG  
3467 C CD1 . TRP C 22  ? 1.945 2.453 1.720 -0.124 -0.022 -0.200 353 TRP EEE CD1 
3468 C CD2 . TRP C 22  ? 2.090 2.535 1.896 -0.084 -0.029 -0.219 353 TRP EEE CD2 
3469 N NE1 . TRP C 22  ? 1.943 2.430 1.727 -0.116 -0.029 -0.200 353 TRP EEE NE1 
3470 C CE2 . TRP C 22  ? 2.100 2.546 1.899 -0.092 -0.034 -0.209 353 TRP EEE CE2 
3471 C CE3 . TRP C 22  ? 1.873 2.281 1.697 -0.060 -0.037 -0.231 353 TRP EEE CE3 
3472 C CZ2 . TRP C 22  ? 1.959 2.363 1.762 -0.078 -0.043 -0.209 353 TRP EEE CZ2 
3473 C CZ3 . TRP C 22  ? 1.721 2.089 1.547 -0.044 -0.051 -0.231 353 TRP EEE CZ3 
3474 C CH2 . TRP C 22  ? 1.715 2.078 1.528 -0.054 -0.053 -0.220 353 TRP EEE CH2 
3475 N N   . ASN C 23  ? 1.925 2.396 1.785 -0.101 0.007  -0.298 354 ASN EEE N   
3476 C CA  . ASN C 23  ? 2.033 2.485 1.944 -0.084 0.002  -0.335 354 ASN EEE CA  
3477 C C   . ASN C 23  ? 2.113 2.524 2.025 -0.050 -0.024 -0.316 354 ASN EEE C   
3478 O O   . ASN C 23  ? 2.234 2.636 2.116 -0.040 -0.028 -0.280 354 ASN EEE O   
3479 C CB  . ASN C 23  ? 2.123 2.590 2.056 -0.093 0.019  -0.356 354 ASN EEE CB  
3480 C CG  . ASN C 23  ? 2.174 2.656 2.161 -0.103 0.033  -0.411 354 ASN EEE CG  
3481 O OD1 . ASN C 23  ? 2.261 2.726 2.301 -0.081 0.017  -0.438 354 ASN EEE OD1 
3482 N ND2 . ASN C 23  ? 2.288 2.803 2.264 -0.138 0.062  -0.429 354 ASN EEE ND2 
3483 N N   . ARG C 24  ? 1.966 2.350 1.910 -0.034 -0.041 -0.339 355 ARG EEE N   
3484 C CA  . ARG C 24  ? 1.764 2.100 1.703 -0.003 -0.068 -0.324 355 ARG EEE CA  
3485 C C   . ARG C 24  ? 1.792 2.112 1.784 0.016  -0.084 -0.359 355 ARG EEE C   
3486 O O   . ARG C 24  ? 1.838 2.162 1.875 0.013  -0.086 -0.397 355 ARG EEE O   
3487 C CB  . ARG C 24  ? 1.777 2.081 1.701 0.002  -0.083 -0.316 355 ARG EEE CB  
3488 C CG  . ARG C 24  ? 1.769 2.016 1.681 0.030  -0.112 -0.304 355 ARG EEE CG  
3489 C CD  . ARG C 24  ? 1.731 1.945 1.601 0.030  -0.119 -0.277 355 ARG EEE CD  
3490 N NE  . ARG C 24  ? 1.591 1.819 1.418 0.024  -0.104 -0.239 355 ARG EEE NE  
3491 C CZ  . ARG C 24  ? 1.652 1.860 1.442 0.020  -0.103 -0.212 355 ARG EEE CZ  
3492 N NH1 . ARG C 24  ? 1.679 1.845 1.463 0.020  -0.116 -0.216 355 ARG EEE NH1 
3493 N NH2 . ARG C 24  ? 1.640 1.868 1.403 0.016  -0.088 -0.182 355 ARG EEE NH2 
3494 N N   . LYS C 25  ? 1.811 2.113 1.798 0.034  -0.097 -0.348 356 LYS EEE N   
3495 C CA  . LYS C 25  ? 1.742 2.017 1.772 0.058  -0.124 -0.373 356 LYS EEE CA  
3496 C C   . LYS C 25  ? 1.729 1.945 1.720 0.082  -0.157 -0.349 356 LYS EEE C   
3497 O O   . LYS C 25  ? 1.647 1.847 1.580 0.085  -0.154 -0.312 356 LYS EEE O   
3498 C CB  . LYS C 25  ? 1.699 1.990 1.742 0.059  -0.117 -0.377 356 LYS EEE CB  
3499 C CG  . LYS C 25  ? 1.640 1.909 1.729 0.082  -0.147 -0.402 356 LYS EEE CG  
3500 C CD  . LYS C 25  ? 1.672 1.947 1.834 0.088  -0.162 -0.447 356 LYS EEE CD  
3501 C CE  . LYS C 25  ? 1.716 1.988 1.944 0.107  -0.188 -0.481 356 LYS EEE CE  
3502 N NZ  . LYS C 25  ? 1.643 1.966 1.917 0.087  -0.157 -0.505 356 LYS EEE NZ  
3503 N N   . ARG C 26  ? 1.797 1.981 1.818 0.098  -0.186 -0.370 357 ARG EEE N   
3504 C CA  . ARG C 26  ? 1.978 2.095 1.961 0.122  -0.224 -0.352 357 ARG EEE CA  
3505 C C   . ARG C 26  ? 2.106 2.212 2.122 0.143  -0.251 -0.370 357 ARG EEE C   
3506 O O   . ARG C 26  ? 2.066 2.193 2.160 0.148  -0.262 -0.412 357 ARG EEE O   
3507 C CB  . ARG C 26  ? 2.026 2.104 2.017 0.128  -0.246 -0.359 357 ARG EEE CB  
3508 C CG  . ARG C 26  ? 2.138 2.139 2.077 0.149  -0.286 -0.335 357 ARG EEE CG  
3509 C CD  . ARG C 26  ? 2.161 2.113 2.122 0.161  -0.320 -0.349 357 ARG EEE CD  
3510 N NE  . ARG C 26  ? 2.270 2.246 2.323 0.175  -0.338 -0.395 357 ARG EEE NE  
3511 C CZ  . ARG C 26  ? 2.424 2.357 2.517 0.201  -0.386 -0.415 357 ARG EEE CZ  
3512 N NH1 . ARG C 26  ? 2.579 2.431 2.617 0.215  -0.426 -0.389 357 ARG EEE NH1 
3513 N NH2 . ARG C 26  ? 2.446 2.417 2.636 0.212  -0.395 -0.462 357 ARG EEE NH2 
3514 N N   . ILE C 27  ? 2.156 2.231 2.114 0.152  -0.261 -0.343 358 ILE EEE N   
3515 C CA  . ILE C 27  ? 1.979 2.033 1.947 0.172  -0.290 -0.353 358 ILE EEE CA  
3516 C C   . ILE C 27  ? 1.909 1.890 1.843 0.194  -0.339 -0.345 358 ILE EEE C   
3517 O O   . ILE C 27  ? 1.741 1.678 1.600 0.192  -0.340 -0.312 358 ILE EEE O   
3518 C CB  . ILE C 27  ? 2.052 2.113 1.972 0.166  -0.269 -0.328 358 ILE EEE CB  
3519 C CG1 . ILE C 27  ? 1.983 2.106 1.925 0.143  -0.223 -0.329 358 ILE EEE CG1 
3520 C CG2 . ILE C 27  ? 2.203 2.244 2.131 0.183  -0.297 -0.341 358 ILE EEE CG2 
3521 C CD1 . ILE C 27  ? 1.912 2.078 1.931 0.137  -0.217 -0.367 358 ILE EEE CD1 
3522 N N   . SER C 28  ? 1.892 1.862 1.885 0.213  -0.380 -0.376 359 SER EEE N   
3523 C CA  . SER C 28  ? 2.193 2.090 2.156 0.237  -0.438 -0.371 359 SER EEE CA  
3524 C C   . SER C 28  ? 2.351 2.256 2.384 0.256  -0.477 -0.407 359 SER EEE C   
3525 O O   . SER C 28  ? 2.397 2.368 2.515 0.248  -0.455 -0.440 359 SER EEE O   
3526 C CB  . SER C 28  ? 2.228 2.091 2.195 0.241  -0.454 -0.369 359 SER EEE CB  
3527 O OG  . SER C 28  ? 2.421 2.312 2.495 0.251  -0.471 -0.414 359 SER EEE OG  
3528 N N   . ASN C 29  ? 2.441 2.280 2.434 0.278  -0.532 -0.399 360 ASN EEE N   
3529 C CA  . ASN C 29  ? 2.461 2.298 2.520 0.299  -0.584 -0.432 360 ASN EEE CA  
3530 C C   . ASN C 29  ? 2.301 2.192 2.393 0.289  -0.559 -0.450 360 ASN EEE C   
3531 O O   . ASN C 29  ? 2.391 2.330 2.590 0.294  -0.567 -0.492 360 ASN EEE O   
3532 C CB  . ASN C 29  ? 2.562 2.425 2.741 0.313  -0.608 -0.474 360 ASN EEE CB  
3533 C CG  . ASN C 29  ? 2.669 2.455 2.826 0.337  -0.669 -0.464 360 ASN EEE CG  
3534 O OD1 . ASN C 29  ? 2.856 2.624 3.006 0.333  -0.659 -0.455 360 ASN EEE OD1 
3535 N ND2 . ASN C 29  ? 2.643 2.377 2.780 0.359  -0.733 -0.464 360 ASN EEE ND2 
3536 N N   . CYS C 30  ? 2.149 2.031 2.158 0.277  -0.530 -0.420 361 CYS EEE N   
3537 C CA  . CYS C 30  ? 2.309 2.230 2.344 0.268  -0.511 -0.435 361 CYS EEE CA  
3538 C C   . CYS C 30  ? 2.383 2.261 2.312 0.266  -0.506 -0.403 361 CYS EEE C   
3539 O O   . CYS C 30  ? 2.424 2.255 2.258 0.265  -0.500 -0.367 361 CYS EEE O   
3540 C CB  . CYS C 30  ? 2.280 2.275 2.369 0.244  -0.450 -0.445 361 CYS EEE CB  
3541 S SG  . CYS C 30  ? 2.630 2.621 2.631 0.225  -0.397 -0.399 361 CYS EEE SG  
3542 N N   . VAL C 31  ? 2.310 2.204 2.260 0.265  -0.507 -0.420 362 VAL EEE N   
3543 C CA  . VAL C 31  ? 2.313 2.179 2.183 0.261  -0.494 -0.401 362 VAL EEE CA  
3544 C C   . VAL C 31  ? 2.212 2.128 2.090 0.240  -0.429 -0.389 362 VAL EEE C   
3545 O O   . VAL C 31  ? 2.061 2.034 2.025 0.228  -0.409 -0.414 362 VAL EEE O   
3546 C CB  . VAL C 31  ? 2.561 2.422 2.465 0.269  -0.532 -0.431 362 VAL EEE CB  
3547 C CG1 . VAL C 31  ? 2.720 2.551 2.545 0.264  -0.517 -0.416 362 VAL EEE CG1 
3548 C CG2 . VAL C 31  ? 2.763 2.580 2.673 0.291  -0.605 -0.445 362 VAL EEE CG2 
3549 N N   . ALA C 32  ? 2.279 2.172 2.073 0.234  -0.399 -0.354 363 ALA EEE N   
3550 C CA  . ALA C 32  ? 2.298 2.231 2.089 0.217  -0.342 -0.337 363 ALA EEE CA  
3551 C C   . ALA C 32  ? 2.228 2.143 1.979 0.217  -0.330 -0.330 363 ALA EEE C   
3552 O O   . ALA C 32  ? 2.561 2.427 2.229 0.224  -0.334 -0.311 363 ALA EEE O   
3553 C CB  . ALA C 32  ? 2.414 2.338 2.151 0.213  -0.319 -0.304 363 ALA EEE CB  
3554 N N   . ASP C 33  ? 2.140 2.087 1.944 0.207  -0.313 -0.347 364 ASP EEE N   
3555 C CA  . ASP C 33  ? 2.342 2.270 2.110 0.207  -0.297 -0.341 364 ASP EEE CA  
3556 C C   . ASP C 33  ? 2.338 2.290 2.090 0.196  -0.248 -0.311 364 ASP EEE C   
3557 O O   . ASP C 33  ? 2.637 2.629 2.441 0.181  -0.223 -0.314 364 ASP EEE O   
3558 C CB  . ASP C 33  ? 2.475 2.416 2.303 0.201  -0.308 -0.372 364 ASP EEE CB  
3559 C CG  . ASP C 33  ? 2.596 2.503 2.383 0.203  -0.301 -0.371 364 ASP EEE CG  
3560 O OD1 . ASP C 33  ? 2.541 2.410 2.250 0.212  -0.294 -0.350 364 ASP EEE OD1 
3561 O OD2 . ASP C 33  ? 2.785 2.706 2.623 0.194  -0.301 -0.394 364 ASP EEE OD2 
3562 N N   . TYR C 34  ? 2.340 2.267 2.023 0.202  -0.235 -0.284 365 TYR EEE N   
3563 C CA  . TYR C 34  ? 2.283 2.237 1.956 0.195  -0.193 -0.255 365 TYR EEE CA  
3564 C C   . TYR C 34  ? 2.131 2.088 1.814 0.192  -0.169 -0.251 365 TYR EEE C   
3565 O O   . TYR C 34  ? 1.838 1.828 1.543 0.183  -0.140 -0.234 365 TYR EEE O   
3566 C CB  . TYR C 34  ? 2.335 2.261 1.939 0.202  -0.187 -0.232 365 TYR EEE CB  
3567 C CG  . TYR C 34  ? 2.239 2.157 1.832 0.202  -0.209 -0.230 365 TYR EEE CG  
3568 C CD1 . TYR C 34  ? 2.163 2.119 1.786 0.191  -0.195 -0.220 365 TYR EEE CD1 
3569 C CD2 . TYR C 34  ? 2.339 2.204 1.885 0.212  -0.244 -0.237 365 TYR EEE CD2 
3570 C CE1 . TYR C 34  ? 2.109 2.052 1.722 0.191  -0.213 -0.219 365 TYR EEE CE1 
3571 C CE2 . TYR C 34  ? 2.404 2.252 1.936 0.213  -0.266 -0.233 365 TYR EEE CE2 
3572 C CZ  . TYR C 34  ? 2.311 2.197 1.879 0.202  -0.249 -0.224 365 TYR EEE CZ  
3573 O OH  . TYR C 34  ? 2.424 2.287 1.979 0.203  -0.271 -0.221 365 TYR EEE OH  
3574 N N   . SER C 35  ? 2.175 2.096 1.842 0.200  -0.183 -0.268 366 SER EEE N   
3575 C CA  . SER C 35  ? 2.259 2.173 1.932 0.199  -0.163 -0.267 366 SER EEE CA  
3576 C C   . SER C 35  ? 2.234 2.188 1.971 0.182  -0.147 -0.267 366 SER EEE C   
3577 O O   . SER C 35  ? 2.309 2.264 2.051 0.179  -0.122 -0.253 366 SER EEE O   
3578 C CB  . SER C 35  ? 2.371 2.242 2.025 0.207  -0.186 -0.292 366 SER EEE CB  
3579 O OG  . SER C 35  ? 2.376 2.261 2.089 0.197  -0.206 -0.320 366 SER EEE OG  
3580 N N   . VAL C 36  ? 2.090 2.075 1.876 0.170  -0.159 -0.284 367 VAL EEE N   
3581 C CA  . VAL C 36  ? 2.072 2.093 1.916 0.148  -0.141 -0.290 367 VAL EEE CA  
3582 C C   . VAL C 36  ? 2.004 2.052 1.839 0.139  -0.110 -0.257 367 VAL EEE C   
3583 O O   . VAL C 36  ? 2.141 2.201 1.997 0.123  -0.090 -0.249 367 VAL EEE O   
3584 C CB  . VAL C 36  ? 2.105 2.157 2.009 0.136  -0.156 -0.321 367 VAL EEE CB  
3585 C CG1 . VAL C 36  ? 1.957 2.045 1.912 0.109  -0.129 -0.327 367 VAL EEE CG1 
3586 C CG2 . VAL C 36  ? 2.304 2.332 2.224 0.147  -0.194 -0.355 367 VAL EEE CG2 
3587 N N   . LEU C 37  ? 1.918 1.971 1.720 0.148  -0.109 -0.238 368 LEU EEE N   
3588 C CA  . LEU C 37  ? 1.860 1.938 1.651 0.142  -0.084 -0.206 368 LEU EEE CA  
3589 C C   . LEU C 37  ? 2.042 2.097 1.807 0.154  -0.070 -0.184 368 LEU EEE C   
3590 O O   . LEU C 37  ? 2.109 2.176 1.887 0.145  -0.054 -0.166 368 LEU EEE O   
3591 C CB  . LEU C 37  ? 1.757 1.849 1.527 0.146  -0.088 -0.195 368 LEU EEE CB  
3592 C CG  . LEU C 37  ? 1.714 1.827 1.512 0.136  -0.101 -0.216 368 LEU EEE CG  
3593 C CD1 . LEU C 37  ? 1.692 1.812 1.466 0.140  -0.102 -0.202 368 LEU EEE CD1 
3594 C CD2 . LEU C 37  ? 1.730 1.881 1.571 0.112  -0.086 -0.223 368 LEU EEE CD2 
3595 N N   . TYR C 38  ? 2.154 2.178 1.881 0.174  -0.076 -0.184 369 TYR EEE N   
3596 C CA  . TYR C 38  ? 2.090 2.099 1.794 0.189  -0.058 -0.164 369 TYR EEE CA  
3597 C C   . TYR C 38  ? 1.972 1.952 1.688 0.192  -0.054 -0.171 369 TYR EEE C   
3598 O O   . TYR C 38  ? 2.002 1.977 1.718 0.201  -0.038 -0.153 369 TYR EEE O   
3599 C CB  . TYR C 38  ? 2.180 2.170 1.838 0.204  -0.058 -0.163 369 TYR EEE CB  
3600 C CG  . TYR C 38  ? 2.199 2.142 1.818 0.213  -0.076 -0.188 369 TYR EEE CG  
3601 C CD1 . TYR C 38  ? 2.255 2.161 1.861 0.222  -0.073 -0.200 369 TYR EEE CD1 
3602 C CD2 . TYR C 38  ? 2.114 2.044 1.707 0.212  -0.099 -0.198 369 TYR EEE CD2 
3603 C CE1 . TYR C 38  ? 2.430 2.292 1.995 0.229  -0.093 -0.223 369 TYR EEE CE1 
3604 C CE2 . TYR C 38  ? 2.203 2.086 1.754 0.219  -0.122 -0.219 369 TYR EEE CE2 
3605 C CZ  . TYR C 38  ? 2.438 2.288 1.973 0.227  -0.119 -0.232 369 TYR EEE CZ  
3606 O OH  . TYR C 38  ? 2.627 2.428 2.113 0.233  -0.144 -0.253 369 TYR EEE OH  
3607 N N   . ASN C 39  ? 1.888 1.850 1.618 0.185  -0.069 -0.197 370 ASN EEE N   
3608 C CA  . ASN C 39  ? 2.187 2.118 1.930 0.185  -0.065 -0.205 370 ASN EEE CA  
3609 C C   . ASN C 39  ? 2.141 2.093 1.923 0.163  -0.054 -0.193 370 ASN EEE C   
3610 O O   . ASN C 39  ? 2.146 2.071 1.938 0.160  -0.046 -0.191 370 ASN EEE O   
3611 C CB  . ASN C 39  ? 2.405 2.303 2.142 0.187  -0.086 -0.240 370 ASN EEE CB  
3612 C CG  . ASN C 39  ? 2.434 2.294 2.117 0.208  -0.092 -0.248 370 ASN EEE CG  
3613 O OD1 . ASN C 39  ? 2.216 2.068 1.874 0.221  -0.072 -0.231 370 ASN EEE OD1 
3614 N ND2 . ASN C 39  ? 2.381 2.216 2.045 0.210  -0.119 -0.276 370 ASN EEE ND2 
3615 N N   . SER C 40  ? 2.209 2.203 2.006 0.146  -0.052 -0.186 371 SER EEE N   
3616 C CA  . SER C 40  ? 2.249 2.264 2.070 0.121  -0.038 -0.172 371 SER EEE CA  
3617 C C   . SER C 40  ? 2.357 2.363 2.165 0.126  -0.024 -0.135 371 SER EEE C   
3618 O O   . SER C 40  ? 2.562 2.571 2.353 0.147  -0.023 -0.119 371 SER EEE O   
3619 C CB  . SER C 40  ? 2.281 2.342 2.112 0.106  -0.038 -0.173 371 SER EEE CB  
3620 O OG  . SER C 40  ? 2.588 2.669 2.426 0.080  -0.022 -0.156 371 SER EEE OG  
3621 N N   . ALA C 41  ? 2.354 2.349 2.172 0.108  -0.015 -0.121 372 ALA EEE N   
3622 C CA  . ALA C 41  ? 2.465 2.450 2.273 0.112  -0.008 -0.082 372 ALA EEE CA  
3623 C C   . ALA C 41  ? 2.534 2.559 2.333 0.092  -0.004 -0.057 372 ALA EEE C   
3624 O O   . ALA C 41  ? 2.649 2.669 2.438 0.096  -0.005 -0.022 372 ALA EEE O   
3625 C CB  . ALA C 41  ? 2.415 2.354 2.229 0.105  -0.004 -0.077 372 ALA EEE CB  
3626 N N   . SER C 42  ? 2.438 2.499 2.241 0.074  -0.003 -0.076 373 SER EEE N   
3627 C CA  . SER C 42  ? 2.239 2.334 2.033 0.044  0.005  -0.065 373 SER EEE CA  
3628 C C   . SER C 42  ? 2.108 2.234 1.887 0.054  -0.001 -0.040 373 SER EEE C   
3629 O O   . SER C 42  ? 2.244 2.388 2.006 0.031  0.003  -0.021 373 SER EEE O   
3630 C CB  . SER C 42  ? 2.341 2.463 2.155 0.024  0.009  -0.101 373 SER EEE CB  
3631 O OG  . SER C 42  ? 2.745 2.847 2.582 0.009  0.016  -0.124 373 SER EEE OG  
3632 N N   . PHE C 43  ? 2.064 2.193 1.845 0.083  -0.009 -0.042 374 PHE EEE N   
3633 C CA  . PHE C 43  ? 2.022 2.186 1.795 0.091  -0.013 -0.025 374 PHE EEE CA  
3634 C C   . PHE C 43  ? 1.881 2.036 1.656 0.113  -0.016 0.006  374 PHE EEE C   
3635 O O   . PHE C 43  ? 1.843 1.962 1.625 0.133  -0.015 0.005  374 PHE EEE O   
3636 C CB  . PHE C 43  ? 2.143 2.318 1.918 0.105  -0.016 -0.048 374 PHE EEE CB  
3637 C CG  . PHE C 43  ? 2.228 2.406 2.012 0.092  -0.018 -0.082 374 PHE EEE CG  
3638 C CD1 . PHE C 43  ? 2.292 2.499 2.082 0.065  -0.014 -0.091 374 PHE EEE CD1 
3639 C CD2 . PHE C 43  ? 2.396 2.547 2.184 0.107  -0.026 -0.108 374 PHE EEE CD2 
3640 C CE1 . PHE C 43  ? 2.403 2.615 2.213 0.056  -0.016 -0.126 374 PHE EEE CE1 
3641 C CE2 . PHE C 43  ? 2.407 2.562 2.212 0.098  -0.033 -0.140 374 PHE EEE CE2 
3642 C CZ  . PHE C 43  ? 2.397 2.584 2.219 0.073  -0.028 -0.150 374 PHE EEE CZ  
3643 N N   . SER C 44  ? 1.797 1.983 1.567 0.108  -0.021 0.031  375 SER EEE N   
3644 C CA  . SER C 44  ? 1.954 2.140 1.734 0.126  -0.030 0.063  375 SER EEE CA  
3645 C C   . SER C 44  ? 1.874 2.091 1.671 0.146  -0.029 0.061  375 SER EEE C   
3646 O O   . SER C 44  ? 1.970 2.182 1.789 0.172  -0.030 0.073  375 SER EEE O   
3647 C CB  . SER C 44  ? 2.159 2.355 1.923 0.105  -0.040 0.093  375 SER EEE CB  
3648 O OG  . SER C 44  ? 2.158 2.393 1.905 0.079  -0.039 0.085  375 SER EEE OG  
3649 N N   . THR C 45  ? 1.863 2.109 1.651 0.134  -0.026 0.045  376 THR EEE N   
3650 C CA  . THR C 45  ? 1.950 2.220 1.747 0.148  -0.022 0.038  376 THR EEE CA  
3651 C C   . THR C 45  ? 1.936 2.190 1.718 0.147  -0.015 0.007  376 THR EEE C   
3652 O O   . THR C 45  ? 1.824 2.077 1.594 0.128  -0.018 -0.009 376 THR EEE O   
3653 C CB  . THR C 45  ? 2.126 2.445 1.927 0.132  -0.028 0.052  376 THR EEE CB  
3654 O OG1 . THR C 45  ? 2.241 2.573 2.060 0.139  -0.040 0.081  376 THR EEE OG1 
3655 C CG2 . THR C 45  ? 2.074 2.415 1.881 0.138  -0.021 0.041  376 THR EEE CG2 
3656 N N   . PHE C 46  ? 1.953 2.193 1.734 0.168  -0.007 -0.002 377 PHE EEE N   
3657 C CA  . PHE C 46  ? 1.854 2.070 1.611 0.171  -0.005 -0.028 377 PHE EEE CA  
3658 C C   . PHE C 46  ? 1.729 1.948 1.479 0.185  0.008  -0.026 377 PHE EEE C   
3659 O O   . PHE C 46  ? 1.913 2.106 1.659 0.204  0.018  -0.032 377 PHE EEE O   
3660 C CB  . PHE C 46  ? 1.838 2.009 1.585 0.178  -0.008 -0.046 377 PHE EEE CB  
3661 C CG  . PHE C 46  ? 1.803 1.952 1.530 0.173  -0.017 -0.073 377 PHE EEE CG  
3662 C CD1 . PHE C 46  ? 1.680 1.821 1.382 0.177  -0.018 -0.081 377 PHE EEE CD1 
3663 C CD2 . PHE C 46  ? 1.761 1.894 1.496 0.164  -0.027 -0.090 377 PHE EEE CD2 
3664 C CE1 . PHE C 46  ? 1.581 1.696 1.264 0.175  -0.034 -0.104 377 PHE EEE CE1 
3665 C CE2 . PHE C 46  ? 1.670 1.786 1.396 0.162  -0.040 -0.116 377 PHE EEE CE2 
3666 C CZ  . PHE C 46  ? 1.649 1.753 1.348 0.169  -0.047 -0.122 377 PHE EEE CZ  
3667 N N   . LYS C 47  ? 1.626 1.878 1.378 0.174  0.009  -0.021 378 LYS EEE N   
3668 C CA  . LYS C 47  ? 1.798 2.062 1.548 0.180  0.025  -0.018 378 LYS EEE CA  
3669 C C   . LYS C 47  ? 1.867 2.107 1.578 0.171  0.024  -0.033 378 LYS EEE C   
3670 O O   . LYS C 47  ? 1.907 2.159 1.617 0.154  0.011  -0.035 378 LYS EEE O   
3671 C CB  . LYS C 47  ? 1.799 2.117 1.582 0.170  0.025  0.001  378 LYS EEE CB  
3672 C CG  . LYS C 47  ? 1.842 2.185 1.668 0.185  0.029  0.018  378 LYS EEE CG  
3673 C CD  . LYS C 47  ? 1.871 2.270 1.733 0.178  0.029  0.033  378 LYS EEE CD  
3674 C CE  . LYS C 47  ? 2.013 2.438 1.926 0.197  0.027  0.049  378 LYS EEE CE  
3675 N NZ  . LYS C 47  ? 2.073 2.557 2.028 0.188  0.018  0.065  378 LYS EEE NZ  
3676 N N   . CYS C 48  ? 1.837 2.042 1.515 0.180  0.036  -0.042 379 CYS EEE N   
3677 C CA  . CYS C 48  ? 1.932 2.105 1.563 0.172  0.031  -0.053 379 CYS EEE CA  
3678 C C   . CYS C 48  ? 1.906 2.086 1.523 0.167  0.055  -0.046 379 CYS EEE C   
3679 O O   . CYS C 48  ? 2.116 2.305 1.745 0.178  0.078  -0.044 379 CYS EEE O   
3680 C CB  . CYS C 48  ? 2.047 2.163 1.638 0.181  0.018  -0.071 379 CYS EEE CB  
3681 S SG  . CYS C 48  ? 2.177 2.293 1.797 0.181  -0.007 -0.082 379 CYS EEE SG  
3682 N N   . TYR C 49  ? 1.864 2.046 1.465 0.150  0.051  -0.043 380 TYR EEE N   
3683 C CA  . TYR C 49  ? 1.950 2.138 1.537 0.138  0.074  -0.036 380 TYR EEE CA  
3684 C C   . TYR C 49  ? 1.975 2.097 1.488 0.131  0.068  -0.043 380 TYR EEE C   
3685 O O   . TYR C 49  ? 1.908 2.003 1.403 0.127  0.040  -0.048 380 TYR EEE O   
3686 C CB  . TYR C 49  ? 2.049 2.290 1.679 0.120  0.071  -0.025 380 TYR EEE CB  
3687 C CG  . TYR C 49  ? 2.114 2.415 1.808 0.125  0.068  -0.016 380 TYR EEE CG  
3688 C CD1 . TYR C 49  ? 2.127 2.434 1.836 0.128  0.046  -0.017 380 TYR EEE CD1 
3689 C CD2 . TYR C 49  ? 2.075 2.425 1.813 0.125  0.087  -0.006 380 TYR EEE CD2 
3690 C CE1 . TYR C 49  ? 2.039 2.390 1.794 0.131  0.041  -0.005 380 TYR EEE CE1 
3691 C CE2 . TYR C 49  ? 1.908 2.307 1.701 0.131  0.078  0.005  380 TYR EEE CE2 
3692 C CZ  . TYR C 49  ? 1.920 2.317 1.717 0.133  0.054  0.007  380 TYR EEE CZ  
3693 O OH  . TYR C 49  ? 1.895 2.332 1.735 0.138  0.044  0.022  380 TYR EEE OH  
3694 N N   . GLY C 50  ? 2.079 2.172 1.547 0.131  0.094  -0.044 381 GLY EEE N   
3695 C CA  . GLY C 50  ? 2.078 2.104 1.464 0.120  0.091  -0.045 381 GLY EEE CA  
3696 C C   . GLY C 50  ? 2.059 2.024 1.395 0.132  0.058  -0.057 381 GLY EEE C   
3697 O O   . GLY C 50  ? 2.148 2.055 1.419 0.124  0.043  -0.055 381 GLY EEE O   
3698 N N   . VAL C 51  ? 2.147 2.120 1.511 0.150  0.045  -0.068 382 VAL EEE N   
3699 C CA  . VAL C 51  ? 2.226 2.146 1.554 0.161  0.011  -0.082 382 VAL EEE CA  
3700 C C   . VAL C 51  ? 2.246 2.184 1.612 0.178  0.013  -0.093 382 VAL EEE C   
3701 O O   . VAL C 51  ? 2.353 2.347 1.786 0.181  0.024  -0.087 382 VAL EEE O   
3702 C CB  . VAL C 51  ? 2.159 2.075 1.506 0.157  -0.027 -0.085 382 VAL EEE CB  
3703 C CG1 . VAL C 51  ? 2.178 2.157 1.606 0.159  -0.030 -0.087 382 VAL EEE CG1 
3704 C CG2 . VAL C 51  ? 2.159 2.018 1.466 0.167  -0.066 -0.100 382 VAL EEE CG2 
3705 N N   . SER C 52  ? 2.071 1.960 1.393 0.189  -0.000 -0.109 383 SER EEE N   
3706 C CA  . SER C 52  ? 2.103 2.001 1.458 0.203  0.002  -0.121 383 SER EEE CA  
3707 C C   . SER C 52  ? 2.087 1.969 1.457 0.208  -0.037 -0.136 383 SER EEE C   
3708 O O   . SER C 52  ? 2.221 2.055 1.542 0.208  -0.065 -0.147 383 SER EEE O   
3709 C CB  . SER C 52  ? 2.192 2.055 1.495 0.210  0.027  -0.130 383 SER EEE CB  
3710 O OG  . SER C 52  ? 2.414 2.220 1.666 0.216  0.001  -0.148 383 SER EEE OG  
3711 N N   . PRO C 53  ? 2.113 2.034 1.551 0.210  -0.041 -0.138 384 PRO EEE N   
3712 C CA  . PRO C 53  ? 2.209 2.124 1.674 0.211  -0.073 -0.154 384 PRO EEE CA  
3713 C C   . PRO C 53  ? 2.364 2.229 1.794 0.220  -0.095 -0.177 384 PRO EEE C   
3714 O O   . PRO C 53  ? 2.443 2.296 1.887 0.219  -0.128 -0.193 384 PRO EEE O   
3715 C CB  . PRO C 53  ? 2.175 2.132 1.704 0.211  -0.060 -0.150 384 PRO EEE CB  
3716 C CG  . PRO C 53  ? 2.130 2.128 1.675 0.206  -0.035 -0.127 384 PRO EEE CG  
3717 C CD  . PRO C 53  ? 2.094 2.066 1.588 0.211  -0.016 -0.124 384 PRO EEE CD  
3718 N N   . THR C 54  ? 2.388 2.226 1.778 0.227  -0.075 -0.179 385 THR EEE N   
3719 C CA  . THR C 54  ? 2.437 2.223 1.785 0.235  -0.089 -0.201 385 THR EEE CA  
3720 C C   . THR C 54  ? 2.573 2.307 1.843 0.233  -0.117 -0.207 385 THR EEE C   
3721 O O   . THR C 54  ? 2.815 2.511 2.063 0.236  -0.152 -0.227 385 THR EEE O   
3722 C CB  . THR C 54  ? 2.432 2.217 1.777 0.243  -0.053 -0.202 385 THR EEE CB  
3723 O OG1 . THR C 54  ? 2.589 2.375 1.896 0.241  -0.022 -0.188 385 THR EEE OG1 
3724 C CG2 . THR C 54  ? 2.375 2.207 1.800 0.246  -0.036 -0.193 385 THR EEE CG2 
3725 N N   . LYS C 55  ? 2.575 2.302 1.804 0.225  -0.107 -0.189 386 LYS EEE N   
3726 C CA  . LYS C 55  ? 2.576 2.244 1.721 0.221  -0.135 -0.188 386 LYS EEE CA  
3727 C C   . LYS C 55  ? 2.515 2.189 1.691 0.218  -0.176 -0.186 386 LYS EEE C   
3728 O O   . LYS C 55  ? 2.711 2.332 1.825 0.217  -0.210 -0.186 386 LYS EEE O   
3729 C CB  . LYS C 55  ? 2.605 2.256 1.685 0.210  -0.101 -0.169 386 LYS EEE CB  
3730 C CG  . LYS C 55  ? 2.810 2.429 1.825 0.211  -0.068 -0.178 386 LYS EEE CG  
3731 C CD  . LYS C 55  ? 2.892 2.528 1.888 0.200  -0.017 -0.162 386 LYS EEE CD  
3732 C CE  . LYS C 55  ? 2.889 2.508 1.845 0.202  0.025  -0.176 386 LYS EEE CE  
3733 N NZ  . LYS C 55  ? 2.828 2.483 1.796 0.192  0.078  -0.163 386 LYS EEE NZ  
3734 N N   . LEU C 56  ? 2.470 2.203 1.734 0.217  -0.174 -0.184 387 LEU EEE N   
3735 C CA  . LEU C 56  ? 2.455 2.197 1.756 0.215  -0.207 -0.186 387 LEU EEE CA  
3736 C C   . LEU C 56  ? 2.417 2.131 1.727 0.224  -0.256 -0.211 387 LEU EEE C   
3737 O O   . LEU C 56  ? 2.514 2.210 1.828 0.226  -0.294 -0.215 387 LEU EEE O   
3738 C CB  . LEU C 56  ? 2.356 2.169 1.746 0.209  -0.188 -0.183 387 LEU EEE CB  
3739 C CG  . LEU C 56  ? 2.252 2.099 1.645 0.198  -0.150 -0.159 387 LEU EEE CG  
3740 C CD1 . LEU C 56  ? 2.259 2.171 1.732 0.191  -0.138 -0.159 387 LEU EEE CD1 
3741 C CD2 . LEU C 56  ? 2.181 1.998 1.529 0.191  -0.159 -0.146 387 LEU EEE CD2 
3742 N N   . ASN C 57  ? 2.372 2.082 1.688 0.230  -0.256 -0.229 388 ASN EEE N   
3743 C CA  . ASN C 57  ? 2.559 2.253 1.900 0.237  -0.301 -0.257 388 ASN EEE CA  
3744 C C   . ASN C 57  ? 2.631 2.256 1.895 0.243  -0.348 -0.260 388 ASN EEE C   
3745 O O   . ASN C 57  ? 2.695 2.309 1.989 0.251  -0.396 -0.283 388 ASN EEE O   
3746 C CB  . ASN C 57  ? 2.762 2.458 2.114 0.239  -0.286 -0.272 388 ASN EEE CB  
3747 C CG  . ASN C 57  ? 2.783 2.542 2.225 0.233  -0.257 -0.274 388 ASN EEE CG  
3748 O OD1 . ASN C 57  ? 2.671 2.471 2.177 0.228  -0.262 -0.275 388 ASN EEE OD1 
3749 N ND2 . ASN C 57  ? 2.917 2.681 2.362 0.233  -0.227 -0.274 388 ASN EEE ND2 
3750 N N   . ASP C 58  ? 2.703 2.280 1.870 0.239  -0.337 -0.239 389 ASP EEE N   
3751 C CA  . ASP C 58  ? 2.834 2.337 1.913 0.242  -0.384 -0.235 389 ASP EEE CA  
3752 C C   . ASP C 58  ? 2.746 2.230 1.778 0.233  -0.369 -0.205 389 ASP EEE C   
3753 O O   . ASP C 58  ? 2.784 2.202 1.706 0.226  -0.372 -0.190 389 ASP EEE O   
3754 C CB  . ASP C 58  ? 3.195 2.639 2.182 0.243  -0.394 -0.245 389 ASP EEE CB  
3755 C CG  . ASP C 58  ? 3.436 2.865 2.348 0.233  -0.336 -0.232 389 ASP EEE CG  
3756 O OD1 . ASP C 58  ? 3.225 2.710 2.193 0.231  -0.285 -0.228 389 ASP EEE OD1 
3757 O OD2 . ASP C 58  ? 3.956 3.315 2.753 0.228  -0.344 -0.229 389 ASP EEE OD2 
3758 N N   . LEU C 59  ? 2.653 2.191 1.764 0.230  -0.354 -0.198 390 LEU EEE N   
3759 C CA  . LEU C 59  ? 2.591 2.117 1.681 0.221  -0.349 -0.174 390 LEU EEE CA  
3760 C C   . LEU C 59  ? 2.590 2.141 1.765 0.228  -0.385 -0.185 390 LEU EEE C   
3761 O O   . LEU C 59  ? 2.649 2.264 1.923 0.232  -0.379 -0.205 390 LEU EEE O   
3762 C CB  . LEU C 59  ? 2.483 2.057 1.586 0.207  -0.286 -0.157 390 LEU EEE CB  
3763 C CG  . LEU C 59  ? 2.650 2.194 1.666 0.199  -0.248 -0.144 390 LEU EEE CG  
3764 C CD1 . LEU C 59  ? 2.555 2.163 1.615 0.190  -0.188 -0.134 390 LEU EEE CD1 
3765 C CD2 . LEU C 59  ? 2.776 2.242 1.682 0.188  -0.261 -0.125 390 LEU EEE CD2 
3766 N N   . CYS C 60  ? 2.685 2.185 1.820 0.227  -0.416 -0.171 391 CYS EEE N   
3767 C CA  . CYS C 60  ? 2.794 2.307 2.002 0.234  -0.448 -0.179 391 CYS EEE CA  
3768 C C   . CYS C 60  ? 2.718 2.245 1.928 0.219  -0.414 -0.158 391 CYS EEE C   
3769 O O   . CYS C 60  ? 2.756 2.240 1.876 0.205  -0.393 -0.131 391 CYS EEE O   
3770 C CB  . CYS C 60  ? 3.025 2.462 2.192 0.248  -0.518 -0.182 391 CYS EEE CB  
3771 S SG  . CYS C 60  ? 3.323 2.762 2.525 0.267  -0.566 -0.217 391 CYS EEE SG  
3772 N N   . PHE C 61  ? 2.544 2.128 1.851 0.219  -0.408 -0.171 392 PHE EEE N   
3773 C CA  . PHE C 61  ? 2.516 2.120 1.838 0.204  -0.380 -0.157 392 PHE EEE CA  
3774 C C   . PHE C 61  ? 2.547 2.145 1.932 0.212  -0.418 -0.173 392 PHE EEE C   
3775 O O   . PHE C 61  ? 2.590 2.196 2.034 0.230  -0.456 -0.201 392 PHE EEE O   
3776 C CB  . PHE C 61  ? 2.359 2.047 1.736 0.191  -0.326 -0.159 392 PHE EEE CB  
3777 C CG  . PHE C 61  ? 2.116 1.812 1.442 0.185  -0.287 -0.144 392 PHE EEE CG  
3778 C CD1 . PHE C 61  ? 1.989 1.675 1.260 0.169  -0.251 -0.118 392 PHE EEE CD1 
3779 C CD2 . PHE C 61  ? 1.947 1.666 1.292 0.194  -0.283 -0.158 392 PHE EEE CD2 
3780 C CE1 . PHE C 61  ? 1.877 1.578 1.116 0.164  -0.212 -0.109 392 PHE EEE CE1 
3781 C CE2 . PHE C 61  ? 1.889 1.617 1.197 0.189  -0.245 -0.147 392 PHE EEE CE2 
3782 C CZ  . PHE C 61  ? 1.851 1.572 1.109 0.176  -0.210 -0.123 392 PHE EEE CZ  
3783 N N   . THR C 62  ? 2.531 2.110 1.903 0.201  -0.411 -0.157 393 THR EEE N   
3784 C CA  A THR C 62  ? 2.699 2.269 2.134 0.209  -0.444 -0.174 393 THR EEE CA  
3785 C CA  B THR C 62  ? 2.719 2.290 2.153 0.208  -0.442 -0.173 393 THR EEE CA  
3786 C C   . THR C 62  ? 2.715 2.376 2.261 0.206  -0.417 -0.204 393 THR EEE C   
3787 O O   . THR C 62  ? 2.707 2.381 2.332 0.221  -0.449 -0.235 393 THR EEE O   
3788 C CB  A THR C 62  ? 2.842 2.354 2.224 0.197  -0.446 -0.148 393 THR EEE CB  
3789 C CB  B THR C 62  ? 2.872 2.391 2.250 0.193  -0.436 -0.146 393 THR EEE CB  
3790 O OG1 A THR C 62  ? 2.743 2.289 2.096 0.171  -0.388 -0.128 393 THR EEE OG1 
3791 O OG1 B THR C 62  ? 2.992 2.433 2.254 0.189  -0.446 -0.116 393 THR EEE OG1 
3792 C CG2 A THR C 62  ? 3.024 2.430 2.301 0.202  -0.488 -0.124 393 THR EEE CG2 
3793 C CG2 B THR C 62  ? 2.946 2.434 2.373 0.203  -0.476 -0.159 393 THR EEE CG2 
3794 N N   . ASN C 63  ? 2.788 2.508 2.339 0.186  -0.364 -0.195 394 ASN EEE N   
3795 C CA  . ASN C 63  ? 2.549 2.353 2.188 0.178  -0.334 -0.218 394 ASN EEE CA  
3796 C C   . ASN C 63  ? 2.316 2.173 1.941 0.164  -0.287 -0.204 394 ASN EEE C   
3797 O O   . ASN C 63  ? 2.096 1.938 1.658 0.154  -0.264 -0.176 394 ASN EEE O   
3798 C CB  . ASN C 63  ? 2.556 2.371 2.231 0.166  -0.327 -0.226 394 ASN EEE CB  
3799 C CG  . ASN C 63  ? 2.790 2.574 2.517 0.184  -0.372 -0.253 394 ASN EEE CG  
3800 O OD1 . ASN C 63  ? 3.046 2.861 2.845 0.197  -0.388 -0.286 394 ASN EEE OD1 
3801 N ND2 . ASN C 63  ? 2.754 2.474 2.448 0.184  -0.395 -0.239 394 ASN EEE ND2 
3802 N N   . VAL C 64  ? 2.198 2.112 1.882 0.164  -0.275 -0.226 395 VAL EEE N   
3803 C CA  . VAL C 64  ? 2.052 2.021 1.740 0.152  -0.233 -0.215 395 VAL EEE CA  
3804 C C   . VAL C 64  ? 2.053 2.083 1.806 0.136  -0.212 -0.233 395 VAL EEE C   
3805 O O   . VAL C 64  ? 2.106 2.148 1.918 0.141  -0.229 -0.265 395 VAL EEE O   
3806 C CB  . VAL C 64  ? 2.042 2.014 1.734 0.163  -0.238 -0.224 395 VAL EEE CB  
3807 C CG1 . VAL C 64  ? 1.998 2.021 1.700 0.152  -0.200 -0.214 395 VAL EEE CG1 
3808 C CG2 . VAL C 64  ? 2.178 2.084 1.797 0.176  -0.260 -0.209 395 VAL EEE CG2 
3809 N N   . TYR C 65  ? 2.066 2.134 1.809 0.118  -0.179 -0.215 396 TYR EEE N   
3810 C CA  . TYR C 65  ? 1.834 1.957 1.622 0.099  -0.158 -0.229 396 TYR EEE CA  
3811 C C   . TYR C 65  ? 1.738 1.908 1.535 0.090  -0.133 -0.222 396 TYR EEE C   
3812 O O   . TYR C 65  ? 1.691 1.860 1.451 0.091  -0.120 -0.194 396 TYR EEE O   
3813 C CB  . TYR C 65  ? 1.830 1.951 1.596 0.084  -0.148 -0.213 396 TYR EEE CB  
3814 C CG  . TYR C 65  ? 1.959 2.026 1.716 0.091  -0.174 -0.219 396 TYR EEE CG  
3815 C CD1 . TYR C 65  ? 1.880 1.945 1.689 0.094  -0.191 -0.252 396 TYR EEE CD1 
3816 C CD2 . TYR C 65  ? 2.031 2.046 1.728 0.094  -0.181 -0.192 396 TYR EEE CD2 
3817 C CE1 . TYR C 65  ? 1.879 1.890 1.683 0.102  -0.219 -0.256 396 TYR EEE CE1 
3818 C CE2 . TYR C 65  ? 2.121 2.077 1.803 0.099  -0.208 -0.194 396 TYR EEE CE2 
3819 C CZ  . TYR C 65  ? 2.053 2.005 1.790 0.104  -0.229 -0.225 396 TYR EEE CZ  
3820 O OH  . TYR C 65  ? 2.243 2.132 1.971 0.112  -0.260 -0.228 396 TYR EEE OH  
3821 N N   . ALA C 66  ? 1.677 1.882 1.522 0.082  -0.126 -0.247 397 ALA EEE N   
3822 C CA  . ALA C 66  ? 1.789 2.035 1.639 0.068  -0.101 -0.240 397 ALA EEE CA  
3823 C C   . ALA C 66  ? 1.939 2.230 1.800 0.042  -0.079 -0.243 397 ALA EEE C   
3824 O O   . ALA C 66  ? 2.055 2.365 1.954 0.031  -0.076 -0.275 397 ALA EEE O   
3825 C CB  . ALA C 66  ? 1.771 2.020 1.657 0.073  -0.105 -0.264 397 ALA EEE CB  
3826 N N   . ASP C 67  ? 1.863 2.173 1.693 0.032  -0.066 -0.213 398 ASP EEE N   
3827 C CA  . ASP C 67  ? 1.731 2.082 1.560 0.006  -0.050 -0.210 398 ASP EEE CA  
3828 C C   . ASP C 67  ? 1.716 2.093 1.539 -0.006 -0.035 -0.199 398 ASP EEE C   
3829 O O   . ASP C 67  ? 1.712 2.080 1.517 0.006  -0.035 -0.171 398 ASP EEE O   
3830 C CB  . ASP C 67  ? 1.728 2.079 1.531 0.004  -0.050 -0.184 398 ASP EEE CB  
3831 C CG  . ASP C 67  ? 1.738 2.054 1.539 0.012  -0.064 -0.192 398 ASP EEE CG  
3832 O OD1 . ASP C 67  ? 1.579 1.876 1.404 0.017  -0.075 -0.222 398 ASP EEE OD1 
3833 O OD2 . ASP C 67  ? 1.550 1.858 1.327 0.012  -0.063 -0.169 398 ASP EEE OD2 
3834 N N   . SER C 68  ? 1.774 2.177 1.611 -0.029 -0.021 -0.220 399 SER EEE N   
3835 C CA  . SER C 68  ? 1.942 2.363 1.766 -0.045 -0.007 -0.208 399 SER EEE CA  
3836 C C   . SER C 68  ? 2.021 2.475 1.823 -0.078 0.007  -0.206 399 SER EEE C   
3837 O O   . SER C 68  ? 1.833 2.300 1.646 -0.092 0.011  -0.233 399 SER EEE O   
3838 C CB  . SER C 68  ? 1.875 2.289 1.729 -0.045 -0.000 -0.234 399 SER EEE CB  
3839 O OG  . SER C 68  ? 1.850 2.272 1.742 -0.052 0.003  -0.277 399 SER EEE OG  
3840 N N   . PHE C 69  ? 2.051 2.514 1.820 -0.089 0.011  -0.175 400 PHE EEE N   
3841 C CA  . PHE C 69  ? 1.976 2.467 1.710 -0.120 0.017  -0.163 400 PHE EEE CA  
3842 C C   . PHE C 69  ? 1.879 2.365 1.579 -0.125 0.016  -0.126 400 PHE EEE C   
3843 O O   . PHE C 69  ? 1.901 2.364 1.610 -0.102 0.010  -0.107 400 PHE EEE O   
3844 C CB  . PHE C 69  ? 1.944 2.450 1.671 -0.120 0.005  -0.154 400 PHE EEE CB  
3845 C CG  . PHE C 69  ? 1.826 2.323 1.560 -0.091 -0.010 -0.124 400 PHE EEE CG  
3846 C CD1 . PHE C 69  ? 1.976 2.478 1.694 -0.085 -0.019 -0.086 400 PHE EEE CD1 
3847 C CD2 . PHE C 69  ? 1.775 2.254 1.531 -0.072 -0.016 -0.136 400 PHE EEE CD2 
3848 C CE1 . PHE C 69  ? 1.954 2.451 1.685 -0.059 -0.028 -0.064 400 PHE EEE CE1 
3849 C CE2 . PHE C 69  ? 1.881 2.350 1.638 -0.049 -0.025 -0.111 400 PHE EEE CE2 
3850 C CZ  . PHE C 69  ? 1.914 2.396 1.662 -0.043 -0.028 -0.078 400 PHE EEE CZ  
3851 N N   . VAL C 70  ? 2.018 2.522 1.678 -0.156 0.020  -0.115 401 VAL EEE N   
3852 C CA  . VAL C 70  ? 2.150 2.647 1.769 -0.165 0.012  -0.074 401 VAL EEE CA  
3853 C C   . VAL C 70  ? 2.045 2.563 1.641 -0.168 -0.011 -0.044 401 VAL EEE C   
3854 O O   . VAL C 70  ? 1.830 2.374 1.414 -0.188 -0.011 -0.060 401 VAL EEE O   
3855 C CB  . VAL C 70  ? 2.326 2.816 1.905 -0.202 0.032  -0.081 401 VAL EEE CB  
3856 C CG1 . VAL C 70  ? 2.321 2.796 1.849 -0.213 0.018  -0.033 401 VAL EEE CG1 
3857 C CG2 . VAL C 70  ? 2.317 2.789 1.928 -0.201 0.054  -0.110 401 VAL EEE CG2 
3858 N N   . ILE C 71  ? 1.911 2.420 1.506 -0.147 -0.029 -0.005 402 ILE EEE N   
3859 C CA  . ILE C 71  ? 1.782 2.311 1.368 -0.143 -0.056 0.031  402 ILE EEE CA  
3860 C C   . ILE C 71  ? 1.930 2.432 1.496 -0.135 -0.069 0.070  402 ILE EEE C   
3861 O O   . ILE C 71  ? 1.772 2.241 1.339 -0.129 -0.055 0.066  402 ILE EEE O   
3862 C CB  . ILE C 71  ? 1.702 2.245 1.336 -0.112 -0.064 0.031  402 ILE EEE CB  
3863 C CG1 . ILE C 71  ? 1.764 2.279 1.432 -0.076 -0.058 0.033  402 ILE EEE CG1 
3864 C CG2 . ILE C 71  ? 1.566 2.127 1.213 -0.123 -0.054 -0.004 402 ILE EEE CG2 
3865 C CD1 . ILE C 71  ? 1.689 2.215 1.396 -0.047 -0.064 0.041  402 ILE EEE CD1 
3866 N N   . ARG C 72  ? 2.242 2.758 1.793 -0.135 -0.097 0.105  403 ARG EEE N   
3867 C CA  . ARG C 72  ? 2.413 2.900 1.947 -0.125 -0.117 0.146  403 ARG EEE CA  
3868 C C   . ARG C 72  ? 2.335 2.818 1.929 -0.079 -0.125 0.160  403 ARG EEE C   
3869 O O   . ARG C 72  ? 2.244 2.754 1.884 -0.061 -0.122 0.144  403 ARG EEE O   
3870 C CB  . ARG C 72  ? 2.432 2.930 1.917 -0.148 -0.148 0.177  403 ARG EEE CB  
3871 C CG  . ARG C 72  ? 2.424 2.967 1.942 -0.135 -0.177 0.189  403 ARG EEE CG  
3872 C CD  . ARG C 72  ? 2.659 3.211 2.118 -0.166 -0.208 0.213  403 ARG EEE CD  
3873 N NE  . ARG C 72  ? 2.853 3.449 2.348 -0.154 -0.243 0.227  403 ARG EEE NE  
3874 C CZ  . ARG C 72  ? 2.955 3.558 2.490 -0.124 -0.277 0.261  403 ARG EEE CZ  
3875 N NH1 . ARG C 72  ? 2.937 3.499 2.477 -0.101 -0.282 0.287  403 ARG EEE NH1 
3876 N NH2 . ARG C 72  ? 3.052 3.704 2.628 -0.117 -0.306 0.267  403 ARG EEE NH2 
3877 N N   . GLY C 73  ? 2.252 2.697 1.844 -0.064 -0.133 0.186  404 GLY EEE N   
3878 C CA  . GLY C 73  ? 2.079 2.512 1.727 -0.021 -0.135 0.193  404 GLY EEE CA  
3879 C C   . GLY C 73  ? 2.058 2.534 1.756 0.003  -0.150 0.199  404 GLY EEE C   
3880 O O   . GLY C 73  ? 1.972 2.454 1.716 0.029  -0.135 0.182  404 GLY EEE O   
3881 N N   . ASP C 74  ? 2.211 2.717 1.902 -0.007 -0.180 0.221  405 ASP EEE N   
3882 C CA  . ASP C 74  ? 2.326 2.877 2.074 0.015  -0.201 0.232  405 ASP EEE CA  
3883 C C   . ASP C 74  ? 2.232 2.820 2.013 0.015  -0.179 0.199  405 ASP EEE C   
3884 O O   . ASP C 74  ? 2.167 2.789 2.006 0.037  -0.184 0.200  405 ASP EEE O   
3885 C CB  . ASP C 74  ? 2.496 3.075 2.223 -0.004 -0.240 0.258  405 ASP EEE CB  
3886 C CG  . ASP C 74  ? 2.513 3.064 2.234 0.010  -0.275 0.300  405 ASP EEE CG  
3887 O OD1 . ASP C 74  ? 2.723 3.248 2.484 0.044  -0.271 0.308  405 ASP EEE OD1 
3888 O OD2 . ASP C 74  ? 2.281 2.832 1.955 -0.013 -0.308 0.324  405 ASP EEE OD2 
3889 N N   . GLU C 75  ? 2.257 2.838 2.002 -0.011 -0.157 0.171  406 GLU EEE N   
3890 C CA  . GLU C 75  ? 2.379 2.988 2.140 -0.019 -0.140 0.141  406 GLU EEE CA  
3891 C C   . GLU C 75  ? 2.326 2.909 2.105 -0.000 -0.111 0.116  406 GLU EEE C   
3892 O O   . GLU C 75  ? 2.203 2.799 1.996 -0.002 -0.098 0.095  406 GLU EEE O   
3893 C CB  . GLU C 75  ? 2.442 3.057 2.155 -0.058 -0.137 0.123  406 GLU EEE CB  
3894 C CG  . GLU C 75  ? 2.475 3.112 2.156 -0.082 -0.166 0.144  406 GLU EEE CG  
3895 C CD  . GLU C 75  ? 2.524 3.161 2.148 -0.123 -0.157 0.122  406 GLU EEE CD  
3896 O OE1 . GLU C 75  ? 2.298 2.907 1.900 -0.133 -0.131 0.100  406 GLU EEE OE1 
3897 O OE2 . GLU C 75  ? 3.034 3.702 2.641 -0.146 -0.177 0.125  406 GLU EEE OE2 
3898 N N   . VAL C 76  ? 2.136 2.678 1.908 0.015  -0.103 0.120  407 VAL EEE N   
3899 C CA  . VAL C 76  ? 2.058 2.570 1.842 0.034  -0.080 0.098  407 VAL EEE CA  
3900 C C   . VAL C 76  ? 1.968 2.501 1.795 0.057  -0.075 0.097  407 VAL EEE C   
3901 O O   . VAL C 76  ? 1.989 2.513 1.816 0.060  -0.058 0.075  407 VAL EEE O   
3902 C CB  . VAL C 76  ? 2.178 2.646 1.953 0.047  -0.076 0.104  407 VAL EEE CB  
3903 C CG1 . VAL C 76  ? 2.182 2.621 1.973 0.072  -0.059 0.086  407 VAL EEE CG1 
3904 C CG2 . VAL C 76  ? 2.199 2.648 1.932 0.018  -0.073 0.098  407 VAL EEE CG2 
3905 N N   . ARG C 77  ? 1.828 2.388 1.690 0.072  -0.089 0.120  408 ARG EEE N   
3906 C CA  . ARG C 77  ? 1.943 2.525 1.853 0.093  -0.077 0.116  408 ARG EEE CA  
3907 C C   . ARG C 77  ? 1.950 2.567 1.866 0.074  -0.071 0.102  408 ARG EEE C   
3908 O O   . ARG C 77  ? 2.189 2.815 2.132 0.084  -0.053 0.092  408 ARG EEE O   
3909 C CB  . ARG C 77  ? 2.052 2.655 2.011 0.116  -0.093 0.140  408 ARG EEE CB  
3910 C CG  . ARG C 77  ? 2.228 2.875 2.201 0.103  -0.126 0.162  408 ARG EEE CG  
3911 C CD  . ARG C 77  ? 2.426 3.074 2.445 0.134  -0.144 0.185  408 ARG EEE CD  
3912 N NE  . ARG C 77  ? 2.664 3.352 2.710 0.131  -0.183 0.211  408 ARG EEE NE  
3913 C CZ  . ARG C 77  ? 2.855 3.562 2.964 0.160  -0.203 0.228  408 ARG EEE CZ  
3914 N NH1 . ARG C 77  ? 2.942 3.631 3.094 0.193  -0.184 0.222  408 ARG EEE NH1 
3915 N NH2 . ARG C 77  ? 2.848 3.595 2.984 0.156  -0.243 0.250  408 ARG EEE NH2 
3916 N N   . GLN C 78  ? 1.998 2.628 1.886 0.044  -0.083 0.098  409 GLN EEE N   
3917 C CA  . GLN C 78  ? 1.999 2.656 1.890 0.023  -0.077 0.082  409 GLN EEE CA  
3918 C C   . GLN C 78  ? 1.757 2.375 1.619 0.018  -0.056 0.056  409 GLN EEE C   
3919 O O   . GLN C 78  ? 1.459 2.090 1.327 0.004  -0.049 0.044  409 GLN EEE O   
3920 C CB  . GLN C 78  ? 2.273 2.956 2.143 -0.008 -0.098 0.084  409 GLN EEE CB  
3921 C CG  . GLN C 78  ? 2.252 2.977 2.149 -0.007 -0.126 0.110  409 GLN EEE CG  
3922 C CD  . GLN C 78  ? 2.241 2.989 2.107 -0.041 -0.145 0.108  409 GLN EEE CD  
3923 O OE1 . GLN C 78  ? 2.207 2.954 2.052 -0.065 -0.134 0.084  409 GLN EEE OE1 
3924 N NE2 . GLN C 78  ? 2.358 3.125 2.221 -0.044 -0.177 0.133  409 GLN EEE NE2 
3925 N N   . ILE C 79  ? 1.755 2.330 1.592 0.027  -0.049 0.048  410 ILE EEE N   
3926 C CA  . ILE C 79  ? 1.884 2.419 1.698 0.028  -0.035 0.024  410 ILE EEE CA  
3927 C C   . ILE C 79  ? 2.124 2.637 1.947 0.052  -0.020 0.023  410 ILE EEE C   
3928 O O   . ILE C 79  ? 2.091 2.566 1.902 0.069  -0.015 0.019  410 ILE EEE O   
3929 C CB  . ILE C 79  ? 1.929 2.433 1.718 0.024  -0.037 0.012  410 ILE EEE CB  
3930 C CG1 . ILE C 79  ? 2.052 2.578 1.826 -0.003 -0.046 0.011  410 ILE EEE CG1 
3931 C CG2 . ILE C 79  ? 2.024 2.490 1.800 0.028  -0.029 -0.014 410 ILE EEE CG2 
3932 C CD1 . ILE C 79  ? 2.063 2.608 1.834 -0.026 -0.046 -0.006 410 ILE EEE CD1 
3933 N N   . ALA C 80  ? 2.196 2.731 2.039 0.050  -0.012 0.026  411 ALA EEE N   
3934 C CA  . ALA C 80  ? 2.016 2.537 1.865 0.066  0.008  0.025  411 ALA EEE CA  
3935 C C   . ALA C 80  ? 1.878 2.417 1.734 0.048  0.018  0.021  411 ALA EEE C   
3936 O O   . ALA C 80  ? 1.868 2.446 1.743 0.029  0.009  0.024  411 ALA EEE O   
3937 C CB  . ALA C 80  ? 2.027 2.570 1.913 0.088  0.011  0.040  411 ALA EEE CB  
3938 N N   . PRO C 81  ? 1.849 2.357 1.685 0.051  0.038  0.015  412 PRO EEE N   
3939 C CA  . PRO C 81  ? 1.813 2.335 1.656 0.032  0.052  0.013  412 PRO EEE CA  
3940 C C   . PRO C 81  ? 1.765 2.353 1.669 0.030  0.058  0.023  412 PRO EEE C   
3941 O O   . PRO C 81  ? 1.822 2.426 1.755 0.051  0.067  0.029  412 PRO EEE O   
3942 C CB  . PRO C 81  ? 1.943 2.415 1.748 0.040  0.075  0.008  412 PRO EEE CB  
3943 C CG  . PRO C 81  ? 1.960 2.385 1.731 0.061  0.066  0.002  412 PRO EEE CG  
3944 C CD  . PRO C 81  ? 1.913 2.368 1.716 0.071  0.049  0.009  412 PRO EEE CD  
3945 N N   . GLY C 82  ? 1.779 2.405 1.706 0.005  0.053  0.023  413 GLY EEE N   
3946 C CA  . GLY C 82  ? 1.878 2.569 1.870 -0.001 0.059  0.030  413 GLY EEE CA  
3947 C C   . GLY C 82  ? 1.820 2.562 1.855 0.008  0.031  0.042  413 GLY EEE C   
3948 O O   . GLY C 82  ? 1.648 2.447 1.747 0.010  0.029  0.048  413 GLY EEE O   
3949 N N   . GLN C 83  ? 1.890 2.609 1.891 0.012  0.008  0.045  414 GLN EEE N   
3950 C CA  . GLN C 83  ? 1.971 2.727 1.993 0.014  -0.023 0.060  414 GLN EEE CA  
3951 C C   . GLN C 83  ? 2.039 2.830 2.065 -0.018 -0.041 0.056  414 GLN EEE C   
3952 O O   . GLN C 83  ? 1.732 2.502 1.729 -0.040 -0.031 0.040  414 GLN EEE O   
3953 C CB  . GLN C 83  ? 1.999 2.712 1.976 0.023  -0.035 0.063  414 GLN EEE CB  
3954 C CG  . GLN C 83  ? 2.053 2.742 2.039 0.056  -0.025 0.070  414 GLN EEE CG  
3955 C CD  . GLN C 83  ? 2.215 2.949 2.261 0.072  -0.039 0.088  414 GLN EEE CD  
3956 O OE1 . GLN C 83  ? 2.516 3.278 2.571 0.065  -0.068 0.102  414 GLN EEE OE1 
3957 N NE2 . GLN C 83  ? 2.143 2.883 2.229 0.094  -0.017 0.085  414 GLN EEE NE2 
3958 N N   . THR C 84  ? 2.145 2.984 2.203 -0.020 -0.069 0.070  415 THR EEE N   
3959 C CA  . THR C 84  ? 2.131 3.004 2.184 -0.051 -0.095 0.069  415 THR EEE CA  
3960 C C   . THR C 84  ? 2.164 3.036 2.188 -0.049 -0.126 0.085  415 THR EEE C   
3961 O O   . THR C 84  ? 2.157 3.009 2.182 -0.023 -0.130 0.101  415 THR EEE O   
3962 C CB  . THR C 84  ? 2.014 2.950 2.134 -0.061 -0.099 0.068  415 THR EEE CB  
3963 O OG1 . THR C 84  ? 2.042 3.017 2.222 -0.036 -0.114 0.086  415 THR EEE OG1 
3964 C CG2 . THR C 84  ? 1.902 2.830 2.039 -0.067 -0.062 0.053  415 THR EEE CG2 
3965 N N   . GLY C 85  ? 2.202 3.088 2.196 -0.079 -0.147 0.081  416 GLY EEE N   
3966 C CA  . GLY C 85  ? 2.337 3.213 2.281 -0.089 -0.174 0.093  416 GLY EEE CA  
3967 C C   . GLY C 85  ? 2.363 3.211 2.245 -0.119 -0.164 0.069  416 GLY EEE C   
3968 O O   . GLY C 85  ? 2.164 2.996 2.048 -0.126 -0.140 0.046  416 GLY EEE O   
3969 N N   . LYS C 86  ? 2.469 3.308 2.298 -0.137 -0.182 0.075  417 LYS EEE N   
3970 C CA  . LYS C 86  ? 2.485 3.306 2.256 -0.170 -0.174 0.049  417 LYS EEE CA  
3971 C C   . LYS C 86  ? 2.281 3.056 2.042 -0.161 -0.140 0.025  417 LYS EEE C   
3972 O O   . LYS C 86  ? 1.883 2.651 1.636 -0.180 -0.126 -0.005 417 LYS EEE O   
3973 C CB  . LYS C 86  ? 2.632 3.445 2.342 -0.189 -0.194 0.063  417 LYS EEE CB  
3974 C CG  . LYS C 86  ? 2.716 3.561 2.395 -0.226 -0.220 0.058  417 LYS EEE CG  
3975 C CD  . LYS C 86  ? 2.831 3.686 2.473 -0.234 -0.259 0.091  417 LYS EEE CD  
3976 C CE  . LYS C 86  ? 2.995 3.901 2.658 -0.249 -0.297 0.098  417 LYS EEE CE  
3977 N NZ  . LYS C 86  ? 3.165 4.075 2.777 -0.262 -0.341 0.129  417 LYS EEE NZ  
3978 N N   . ILE C 87  ? 2.286 3.032 2.051 -0.134 -0.130 0.037  418 ILE EEE N   
3979 C CA  . ILE C 87  ? 2.220 2.921 1.971 -0.126 -0.103 0.015  418 ILE EEE CA  
3980 C C   . ILE C 87  ? 2.241 2.935 2.025 -0.114 -0.088 0.001  418 ILE EEE C   
3981 O O   . ILE C 87  ? 2.332 3.008 2.106 -0.127 -0.077 -0.027 418 ILE EEE O   
3982 C CB  . ILE C 87  ? 2.211 2.882 1.955 -0.102 -0.100 0.031  418 ILE EEE CB  
3983 C CG1 . ILE C 87  ? 2.515 3.185 2.216 -0.119 -0.115 0.047  418 ILE EEE CG1 
3984 C CG2 . ILE C 87  ? 2.147 2.777 1.886 -0.092 -0.077 0.007  418 ILE EEE CG2 
3985 C CD1 . ILE C 87  ? 2.499 3.170 2.154 -0.157 -0.109 0.024  418 ILE EEE CD1 
3986 N N   . ALA C 88  ? 2.277 2.983 2.099 -0.092 -0.088 0.018  419 ALA EEE N   
3987 C CA  . ALA C 88  ? 2.268 2.966 2.116 -0.084 -0.071 0.010  419 ALA EEE CA  
3988 C C   . ALA C 88  ? 2.195 2.908 2.045 -0.112 -0.071 -0.008 419 ALA EEE C   
3989 O O   . ALA C 88  ? 2.045 2.725 1.887 -0.115 -0.057 -0.027 419 ALA EEE O   
3990 C CB  . ALA C 88  ? 2.306 3.029 2.197 -0.063 -0.070 0.031  419 ALA EEE CB  
3991 N N   . ASP C 89  ? 2.227 2.987 2.087 -0.133 -0.090 -0.003 420 ASP EEE N   
3992 C CA  . ASP C 89  ? 2.341 3.122 2.214 -0.161 -0.092 -0.018 420 ASP EEE CA  
3993 C C   . ASP C 89  ? 2.316 3.075 2.149 -0.186 -0.090 -0.047 420 ASP EEE C   
3994 O O   . ASP C 89  ? 2.116 2.861 1.955 -0.200 -0.081 -0.067 420 ASP EEE O   
3995 C CB  . ASP C 89  ? 2.497 3.340 2.402 -0.173 -0.116 -0.004 420 ASP EEE CB  
3996 C CG  . ASP C 89  ? 2.436 3.309 2.398 -0.150 -0.114 0.017  420 ASP EEE CG  
3997 O OD1 . ASP C 89  ? 2.356 3.202 2.329 -0.133 -0.088 0.016  420 ASP EEE OD1 
3998 O OD2 . ASP C 89  ? 2.657 3.579 2.652 -0.151 -0.138 0.033  420 ASP EEE OD2 
3999 N N   . TYR C 90  ? 2.345 3.099 2.141 -0.193 -0.098 -0.050 421 TYR EEE N   
4000 C CA  . TYR C 90  ? 2.399 3.147 2.161 -0.222 -0.097 -0.080 421 TYR EEE CA  
4001 C C   . TYR C 90  ? 2.290 2.996 2.027 -0.215 -0.080 -0.099 421 TYR EEE C   
4002 O O   . TYR C 90  ? 2.370 3.068 2.087 -0.237 -0.073 -0.131 421 TYR EEE O   
4003 C CB  . TYR C 90  ? 2.557 3.341 2.289 -0.248 -0.119 -0.072 421 TYR EEE CB  
4004 C CG  . TYR C 90  ? 2.472 3.304 2.228 -0.263 -0.143 -0.060 421 TYR EEE CG  
4005 C CD1 . TYR C 90  ? 2.378 3.225 2.183 -0.261 -0.139 -0.063 421 TYR EEE CD1 
4006 C CD2 . TYR C 90  ? 2.409 3.273 2.137 -0.281 -0.171 -0.046 421 TYR EEE CD2 
4007 C CE1 . TYR C 90  ? 2.310 3.207 2.145 -0.277 -0.161 -0.054 421 TYR EEE CE1 
4008 C CE2 . TYR C 90  ? 2.304 3.216 2.058 -0.295 -0.199 -0.036 421 TYR EEE CE2 
4009 C CZ  . TYR C 90  ? 2.202 3.134 2.015 -0.292 -0.193 -0.042 421 TYR EEE CZ  
4010 O OH  . TYR C 90  ? 2.212 3.197 2.061 -0.307 -0.219 -0.035 421 TYR EEE OH  
4011 N N   . ASN C 91  ? 2.177 2.858 1.917 -0.187 -0.072 -0.086 422 ASN EEE N   
4012 C CA  . ASN C 91  ? 2.202 2.851 1.925 -0.182 -0.058 -0.105 422 ASN EEE CA  
4013 C C   . ASN C 91  ? 2.216 2.825 1.960 -0.154 -0.047 -0.113 422 ASN EEE C   
4014 O O   . ASN C 91  ? 2.043 2.627 1.790 -0.157 -0.038 -0.145 422 ASN EEE O   
4015 C CB  . ASN C 91  ? 2.191 2.845 1.888 -0.180 -0.063 -0.084 422 ASN EEE CB  
4016 C CG  . ASN C 91  ? 2.086 2.767 1.745 -0.214 -0.074 -0.083 422 ASN EEE CG  
4017 O OD1 . ASN C 91  ? 1.957 2.631 1.586 -0.236 -0.061 -0.108 422 ASN EEE OD1 
4018 N ND2 . ASN C 91  ? 2.056 2.769 1.717 -0.218 -0.096 -0.057 422 ASN EEE ND2 
4019 N N   . TYR C 92  ? 2.153 2.754 1.911 -0.128 -0.049 -0.087 423 TYR EEE N   
4020 C CA  . TYR C 92  ? 1.999 2.558 1.767 -0.101 -0.041 -0.091 423 TYR EEE CA  
4021 C C   . TYR C 92  ? 1.925 2.487 1.708 -0.084 -0.040 -0.066 423 TYR EEE C   
4022 O O   . TYR C 92  ? 1.692 2.274 1.482 -0.073 -0.043 -0.042 423 TYR EEE O   
4023 C CB  . TYR C 92  ? 1.990 2.527 1.750 -0.085 -0.037 -0.092 423 TYR EEE CB  
4024 C CG  . TYR C 92  ? 1.974 2.467 1.740 -0.060 -0.034 -0.100 423 TYR EEE CG  
4025 C CD1 . TYR C 92  ? 1.829 2.293 1.600 -0.060 -0.034 -0.130 423 TYR EEE CD1 
4026 C CD2 . TYR C 92  ? 1.873 2.353 1.640 -0.036 -0.033 -0.078 423 TYR EEE CD2 
4027 C CE1 . TYR C 92  ? 1.759 2.181 1.532 -0.037 -0.037 -0.135 423 TYR EEE CE1 
4028 C CE2 . TYR C 92  ? 1.829 2.264 1.591 -0.015 -0.032 -0.085 423 TYR EEE CE2 
4029 C CZ  . TYR C 92  ? 1.857 2.263 1.621 -0.015 -0.037 -0.113 423 TYR EEE CZ  
4030 O OH  . TYR C 92  ? 1.715 2.076 1.472 0.005  -0.042 -0.119 423 TYR EEE OH  
4031 N N   . LYS C 93  ? 2.055 2.592 1.841 -0.082 -0.035 -0.073 424 LYS EEE N   
4032 C CA  . LYS C 93  ? 2.046 2.589 1.846 -0.077 -0.028 -0.056 424 LYS EEE CA  
4033 C C   . LYS C 93  ? 1.999 2.487 1.782 -0.056 -0.019 -0.056 424 LYS EEE C   
4034 O O   . LYS C 93  ? 1.843 2.291 1.612 -0.059 -0.021 -0.073 424 LYS EEE O   
4035 C CB  . LYS C 93  ? 2.048 2.606 1.858 -0.103 -0.028 -0.063 424 LYS EEE CB  
4036 C CG  . LYS C 93  ? 2.119 2.690 1.948 -0.104 -0.016 -0.048 424 LYS EEE CG  
4037 C CD  . LYS C 93  ? 2.112 2.726 1.968 -0.090 -0.015 -0.025 424 LYS EEE CD  
4038 C CE  . LYS C 93  ? 1.992 2.645 1.885 -0.100 -0.005 -0.015 424 LYS EEE CE  
4039 N NZ  . LYS C 93  ? 1.886 2.582 1.815 -0.082 -0.008 0.003  424 LYS EEE NZ  
4040 N N   . LEU C 94  ? 1.887 2.374 1.672 -0.035 -0.011 -0.039 425 LEU EEE N   
4041 C CA  . LEU C 94  ? 1.792 2.230 1.555 -0.016 -0.002 -0.037 425 LEU EEE CA  
4042 C C   . LEU C 94  ? 1.864 2.300 1.626 -0.029 0.013  -0.030 425 LEU EEE C   
4043 O O   . LEU C 94  ? 1.848 2.332 1.641 -0.043 0.018  -0.022 425 LEU EEE O   
4044 C CB  . LEU C 94  ? 1.648 2.087 1.414 0.008  0.004  -0.025 425 LEU EEE CB  
4045 C CG  . LEU C 94  ? 1.565 1.995 1.326 0.020  -0.008 -0.031 425 LEU EEE CG  
4046 C CD1 . LEU C 94  ? 1.421 1.842 1.183 0.044  -0.001 -0.020 425 LEU EEE CD1 
4047 C CD2 . LEU C 94  ? 1.576 1.960 1.315 0.020  -0.017 -0.053 425 LEU EEE CD2 
4048 N N   . PRO C 95  ? 1.873 2.251 1.600 -0.027 0.018  -0.034 426 PRO EEE N   
4049 C CA  . PRO C 95  ? 1.865 2.234 1.582 -0.039 0.038  -0.024 426 PRO EEE CA  
4050 C C   . PRO C 95  ? 1.968 2.353 1.692 -0.025 0.060  -0.012 426 PRO EEE C   
4051 O O   . PRO C 95  ? 1.900 2.276 1.617 -0.002 0.056  -0.011 426 PRO EEE O   
4052 C CB  . PRO C 95  ? 1.934 2.226 1.600 -0.040 0.032  -0.030 426 PRO EEE CB  
4053 C CG  . PRO C 95  ? 1.935 2.196 1.584 -0.015 0.013  -0.039 426 PRO EEE CG  
4054 C CD  . PRO C 95  ? 1.808 2.125 1.500 -0.013 0.004  -0.046 426 PRO EEE CD  
4055 N N   . ASP C 96  ? 2.117 2.525 1.856 -0.040 0.083  -0.004 427 ASP EEE N   
4056 C CA  . ASP C 96  ? 2.137 2.565 1.891 -0.029 0.111  0.003  427 ASP EEE CA  
4057 C C   . ASP C 96  ? 2.238 2.601 1.934 -0.010 0.119  0.002  427 ASP EEE C   
4058 O O   . ASP C 96  ? 2.326 2.704 2.036 0.011  0.129  0.002  427 ASP EEE O   
4059 C CB  . ASP C 96  ? 2.182 2.633 1.955 -0.055 0.140  0.006  427 ASP EEE CB  
4060 C CG  . ASP C 96  ? 2.155 2.691 2.006 -0.067 0.138  0.008  427 ASP EEE CG  
4061 O OD1 . ASP C 96  ? 2.219 2.803 2.114 -0.049 0.123  0.010  427 ASP EEE OD1 
4062 O OD2 . ASP C 96  ? 2.263 2.815 2.130 -0.096 0.151  0.006  427 ASP EEE OD2 
4063 N N   . ASP C 97  ? 2.274 2.567 1.907 -0.017 0.112  -0.001 428 ASP EEE N   
4064 C CA  . ASP C 97  ? 2.358 2.581 1.922 -0.005 0.119  -0.001 428 ASP EEE CA  
4065 C C   . ASP C 97  ? 2.114 2.302 1.658 0.017  0.086  -0.009 428 ASP EEE C   
4066 O O   . ASP C 97  ? 2.068 2.188 1.550 0.024  0.077  -0.011 428 ASP EEE O   
4067 C CB  . ASP C 97  ? 2.590 2.750 2.092 -0.028 0.128  0.005  428 ASP EEE CB  
4068 C CG  . ASP C 97  ? 2.652 2.778 2.142 -0.038 0.096  0.002  428 ASP EEE CG  
4069 O OD1 . ASP C 97  ? 2.448 2.618 1.990 -0.037 0.077  -0.006 428 ASP EEE OD1 
4070 O OD2 . ASP C 97  ? 2.808 2.859 2.233 -0.048 0.091  0.007  428 ASP EEE OD2 
4071 N N   . PHE C 98  ? 1.995 2.229 1.590 0.025  0.068  -0.014 429 PHE EEE N   
4072 C CA  . PHE C 98  ? 2.006 2.221 1.598 0.043  0.040  -0.025 429 PHE EEE CA  
4073 C C   . PHE C 98  ? 1.982 2.149 1.530 0.063  0.042  -0.027 429 PHE EEE C   
4074 O O   . PHE C 98  ? 1.842 2.024 1.393 0.071  0.066  -0.022 429 PHE EEE O   
4075 C CB  . PHE C 98  ? 1.872 2.150 1.521 0.047  0.033  -0.025 429 PHE EEE CB  
4076 C CG  . PHE C 98  ? 1.735 2.001 1.386 0.062  0.014  -0.036 429 PHE EEE CG  
4077 C CD1 . PHE C 98  ? 1.717 1.961 1.364 0.058  -0.008 -0.051 429 PHE EEE CD1 
4078 C CD2 . PHE C 98  ? 1.592 1.871 1.257 0.080  0.018  -0.033 429 PHE EEE CD2 
4079 C CE1 . PHE C 98  ? 1.759 1.996 1.415 0.070  -0.023 -0.064 429 PHE EEE CE1 
4080 C CE2 . PHE C 98  ? 1.555 1.822 1.224 0.090  0.002  -0.043 429 PHE EEE CE2 
4081 C CZ  . PHE C 98  ? 1.730 1.979 1.395 0.084  -0.017 -0.059 429 PHE EEE CZ  
4082 N N   . THR C 99  ? 2.009 2.124 1.524 0.071  0.016  -0.037 430 THR EEE N   
4083 C CA  A THR C 99  ? 2.165 2.235 1.643 0.091  0.006  -0.045 430 THR EEE CA  
4084 C CA  B THR C 99  ? 2.054 2.126 1.533 0.091  0.007  -0.045 430 THR EEE CA  
4085 C C   . THR C 99  ? 2.093 2.172 1.604 0.103  -0.021 -0.060 430 THR EEE C   
4086 O O   . THR C 99  ? 2.389 2.447 1.901 0.100  -0.045 -0.070 430 THR EEE O   
4087 C CB  A THR C 99  ? 2.332 2.324 1.735 0.088  -0.005 -0.044 430 THR EEE CB  
4088 C CB  B THR C 99  ? 2.099 2.093 1.501 0.090  -0.002 -0.044 430 THR EEE CB  
4089 O OG1 A THR C 99  ? 2.426 2.411 1.799 0.070  0.024  -0.030 430 THR EEE OG1 
4090 O OG1 B THR C 99  ? 1.917 1.872 1.312 0.095  -0.041 -0.055 430 THR EEE OG1 
4091 C CG2 A THR C 99  ? 2.429 2.375 1.787 0.106  -0.014 -0.051 430 THR EEE CG2 
4092 C CG2 B THR C 99  ? 2.126 2.107 1.499 0.067  0.019  -0.030 430 THR EEE CG2 
4093 N N   . GLY C 100 ? 1.956 2.064 1.496 0.115  -0.015 -0.062 431 GLY EEE N   
4094 C CA  . GLY C 100 ? 1.863 1.982 1.437 0.121  -0.035 -0.076 431 GLY EEE CA  
4095 C C   . GLY C 100 ? 1.814 1.968 1.420 0.129  -0.023 -0.072 431 GLY EEE C   
4096 O O   . GLY C 100 ? 1.920 2.088 1.526 0.134  -0.001 -0.059 431 GLY EEE O   
4097 N N   . CYS C 101 ? 1.791 1.958 1.426 0.130  -0.035 -0.082 432 CYS EEE N   
4098 C CA  . CYS C 101 ? 1.963 2.155 1.626 0.135  -0.027 -0.076 432 CYS EEE CA  
4099 C C   . CYS C 101 ? 1.972 2.212 1.671 0.119  -0.027 -0.071 432 CYS EEE C   
4100 O O   . CYS C 101 ? 1.965 2.211 1.673 0.106  -0.037 -0.085 432 CYS EEE O   
4101 C CB  . CYS C 101 ? 2.048 2.209 1.708 0.147  -0.038 -0.092 432 CYS EEE CB  
4102 S SG  . CYS C 101 ? 2.062 2.166 1.673 0.166  -0.037 -0.098 432 CYS EEE SG  
4103 N N   . VAL C 102 ? 1.898 2.168 1.616 0.120  -0.017 -0.052 433 VAL EEE N   
4104 C CA  . VAL C 102 ? 1.949 2.260 1.691 0.105  -0.018 -0.041 433 VAL EEE CA  
4105 C C   . VAL C 102 ? 1.958 2.258 1.708 0.111  -0.019 -0.039 433 VAL EEE C   
4106 O O   . VAL C 102 ? 2.145 2.436 1.899 0.127  -0.014 -0.027 433 VAL EEE O   
4107 C CB  . VAL C 102 ? 1.951 2.300 1.709 0.104  -0.011 -0.019 433 VAL EEE CB  
4108 C CG1 . VAL C 102 ? 1.908 2.293 1.681 0.090  -0.018 -0.004 433 VAL EEE CG1 
4109 C CG2 . VAL C 102 ? 2.002 2.360 1.753 0.095  -0.007 -0.022 433 VAL EEE CG2 
4110 N N   . ILE C 103 ? 1.869 2.167 1.622 0.096  -0.025 -0.053 434 ILE EEE N   
4111 C CA  . ILE C 103 ? 1.905 2.186 1.664 0.097  -0.024 -0.054 434 ILE EEE CA  
4112 C C   . ILE C 103 ? 2.034 2.342 1.796 0.072  -0.022 -0.046 434 ILE EEE C   
4113 O O   . ILE C 103 ? 2.048 2.374 1.811 0.053  -0.022 -0.062 434 ILE EEE O   
4114 C CB  . ILE C 103 ? 2.007 2.257 1.767 0.100  -0.030 -0.084 434 ILE EEE CB  
4115 C CG1 . ILE C 103 ? 2.106 2.325 1.849 0.121  -0.035 -0.093 434 ILE EEE CG1 
4116 C CG2 . ILE C 103 ? 1.923 2.155 1.692 0.098  -0.027 -0.086 434 ILE EEE CG2 
4117 C CD1 . ILE C 103 ? 2.019 2.215 1.764 0.122  -0.050 -0.122 434 ILE EEE CD1 
4118 N N   . ALA C 104 ? 2.197 2.502 1.957 0.072  -0.022 -0.023 435 ALA EEE N   
4119 C CA  . ALA C 104 ? 2.278 2.602 2.028 0.046  -0.021 -0.009 435 ALA EEE CA  
4120 C C   . ALA C 104 ? 2.291 2.586 2.036 0.043  -0.019 0.003  435 ALA EEE C   
4121 O O   . ALA C 104 ? 2.301 2.567 2.055 0.066  -0.021 0.009  435 ALA EEE O   
4122 C CB  . ALA C 104 ? 2.268 2.623 2.015 0.046  -0.030 0.018  435 ALA EEE CB  
4123 N N   . TRP C 105 ? 2.180 2.479 1.907 0.012  -0.014 0.004  436 TRP EEE N   
4124 C CA  . TRP C 105 ? 2.118 2.387 1.832 0.002  -0.011 0.021  436 TRP EEE CA  
4125 C C   . TRP C 105 ? 2.200 2.480 1.877 -0.033 -0.010 0.040  436 TRP EEE C   
4126 O O   . TRP C 105 ? 2.008 2.320 1.675 -0.055 -0.004 0.024  436 TRP EEE O   
4127 C CB  . TRP C 105 ? 1.957 2.201 1.686 -0.004 0.001  -0.009 436 TRP EEE CB  
4128 C CG  . TRP C 105 ? 1.777 2.045 1.512 -0.030 0.014  -0.043 436 TRP EEE CG  
4129 C CD1 . TRP C 105 ? 1.864 2.131 1.590 -0.065 0.031  -0.053 436 TRP EEE CD1 
4130 C CD2 . TRP C 105 ? 1.693 1.983 1.451 -0.023 0.013  -0.075 436 TRP EEE CD2 
4131 N NE1 . TRP C 105 ? 1.895 2.189 1.644 -0.079 0.042  -0.093 436 TRP EEE NE1 
4132 C CE2 . TRP C 105 ? 1.789 2.095 1.559 -0.052 0.028  -0.106 436 TRP EEE CE2 
4133 C CE3 . TRP C 105 ? 1.684 1.979 1.454 0.003  0.001  -0.081 436 TRP EEE CE3 
4134 C CZ2 . TRP C 105 ? 1.794 2.122 1.593 -0.051 0.028  -0.142 436 TRP EEE CZ2 
4135 C CZ3 . TRP C 105 ? 1.767 2.076 1.555 0.002  -0.001 -0.113 436 TRP EEE CZ3 
4136 C CH2 . TRP C 105 ? 1.828 2.154 1.634 -0.023 0.011  -0.144 436 TRP EEE CH2 
4137 N N   . ASN C 106 ? 2.230 2.480 1.886 -0.037 -0.016 0.073  437 ASN EEE N   
4138 C CA  . ASN C 106 ? 2.217 2.463 1.824 -0.070 -0.019 0.099  437 ASN EEE CA  
4139 C C   . ASN C 106 ? 2.175 2.421 1.767 -0.109 0.008  0.070  437 ASN EEE C   
4140 O O   . ASN C 106 ? 2.105 2.326 1.719 -0.108 0.022  0.050  437 ASN EEE O   
4141 C CB  . ASN C 106 ? 2.376 2.576 1.968 -0.061 -0.034 0.140  437 ASN EEE CB  
4142 C CG  . ASN C 106 ? 2.450 2.638 1.983 -0.092 -0.045 0.177  437 ASN EEE CG  
4143 O OD1 . ASN C 106 ? 2.395 2.574 1.886 -0.133 -0.027 0.170  437 ASN EEE OD1 
4144 N ND2 . ASN C 106 ? 2.393 2.578 1.921 -0.073 -0.076 0.215  437 ASN EEE ND2 
4145 N N   . SER C 107 ? 2.194 2.467 1.753 -0.142 0.016  0.062  438 SER EEE N   
4146 C CA  . SER C 107 ? 2.290 2.571 1.840 -0.182 0.047  0.028  438 SER EEE CA  
4147 C C   . SER C 107 ? 2.542 2.806 2.019 -0.226 0.055  0.053  438 SER EEE C   
4148 O O   . SER C 107 ? 2.737 3.020 2.194 -0.266 0.081  0.026  438 SER EEE O   
4149 C CB  . SER C 107 ? 2.124 2.449 1.702 -0.183 0.056  -0.014 438 SER EEE CB  
4150 O OG  . SER C 107 ? 2.028 2.381 1.582 -0.184 0.040  0.001  438 SER EEE OG  
4151 N N   . ASN C 108 ? 2.559 2.786 1.999 -0.221 0.033  0.102  439 ASN EEE N   
4152 C CA  . ASN C 108 ? 2.489 2.687 1.848 -0.260 0.030  0.138  439 ASN EEE CA  
4153 C C   . ASN C 108 ? 2.469 2.645 1.804 -0.305 0.070  0.117  439 ASN EEE C   
4154 O O   . ASN C 108 ? 2.611 2.788 1.881 -0.351 0.086  0.118  439 ASN EEE O   
4155 C CB  . ASN C 108 ? 2.556 2.709 1.897 -0.238 -0.004 0.193  439 ASN EEE CB  
4156 C CG  . ASN C 108 ? 2.627 2.758 1.881 -0.268 -0.024 0.237  439 ASN EEE CG  
4157 O OD1 . ASN C 108 ? 2.599 2.765 1.821 -0.286 -0.031 0.234  439 ASN EEE OD1 
4158 N ND2 . ASN C 108 ? 2.749 2.818 1.963 -0.275 -0.036 0.279  439 ASN EEE ND2 
4159 N N   . ASN C 109 ? 2.437 2.595 1.823 -0.295 0.087  0.096  440 ASN EEE N   
4160 C CA  . ASN C 109 ? 2.517 2.655 1.894 -0.337 0.126  0.073  440 ASN EEE CA  
4161 C C   . ASN C 109 ? 2.496 2.686 1.889 -0.368 0.162  0.019  440 ASN EEE C   
4162 O O   . ASN C 109 ? 2.670 2.850 2.034 -0.416 0.198  0.004  440 ASN EEE O   
4163 C CB  . ASN C 109 ? 2.495 2.606 1.933 -0.314 0.130  0.060  440 ASN EEE CB  
4164 C CG  . ASN C 109 ? 2.607 2.755 2.127 -0.270 0.122  0.022  440 ASN EEE CG  
4165 O OD1 . ASN C 109 ? 2.681 2.857 2.213 -0.239 0.098  0.027  440 ASN EEE OD1 
4166 N ND2 . ASN C 109 ? 2.722 2.870 2.299 -0.269 0.139  -0.016 440 ASN EEE ND2 
4167 N N   . LEU C 110 ? 2.447 2.687 1.883 -0.344 0.154  -0.011 441 LEU EEE N   
4168 C CA  . LEU C 110 ? 2.396 2.686 1.860 -0.367 0.184  -0.067 441 LEU EEE CA  
4169 C C   . LEU C 110 ? 2.419 2.735 1.827 -0.387 0.181  -0.062 441 LEU EEE C   
4170 O O   . LEU C 110 ? 2.519 2.855 1.905 -0.430 0.215  -0.094 441 LEU EEE O   
4171 C CB  . LEU C 110 ? 2.365 2.687 1.917 -0.323 0.173  -0.105 441 LEU EEE CB  
4172 C CG  . LEU C 110 ? 2.392 2.692 2.004 -0.295 0.167  -0.113 441 LEU EEE CG  
4173 C CD1 . LEU C 110 ? 2.392 2.710 2.062 -0.244 0.140  -0.128 441 LEU EEE CD1 
4174 C CD2 . LEU C 110 ? 2.332 2.639 1.982 -0.326 0.204  -0.156 441 LEU EEE CD2 
4175 N N   . ASP C 111 ? 2.470 2.790 1.864 -0.357 0.142  -0.029 442 ASP EEE N   
4176 C CA  . ASP C 111 ? 2.661 3.016 2.029 -0.364 0.132  -0.035 442 ASP EEE CA  
4177 C C   . ASP C 111 ? 2.890 3.226 2.164 -0.389 0.113  0.013  442 ASP EEE C   
4178 O O   . ASP C 111 ? 2.947 3.312 2.193 -0.400 0.103  0.009  442 ASP EEE O   
4179 C CB  . ASP C 111 ? 2.573 2.953 2.001 -0.314 0.103  -0.039 442 ASP EEE CB  
4180 C CG  . ASP C 111 ? 2.542 2.944 2.051 -0.294 0.119  -0.090 442 ASP EEE CG  
4181 O OD1 . ASP C 111 ? 2.741 3.162 2.263 -0.322 0.150  -0.133 442 ASP EEE OD1 
4182 O OD2 . ASP C 111 ? 2.599 2.997 2.157 -0.251 0.099  -0.086 442 ASP EEE OD2 
4183 N N   . SER C 112 ? 2.927 3.213 2.155 -0.398 0.104  0.057  443 SER EEE N   
4184 C CA  . SER C 112 ? 2.876 3.130 2.000 -0.431 0.088  0.104  443 SER EEE CA  
4185 C C   . SER C 112 ? 3.029 3.259 2.090 -0.492 0.133  0.090  443 SER EEE C   
4186 O O   . SER C 112 ? 2.911 3.141 2.019 -0.499 0.170  0.056  443 SER EEE O   
4187 C CB  . SER C 112 ? 2.847 3.055 1.960 -0.402 0.048  0.163  443 SER EEE CB  
4188 O OG  . SER C 112 ? 2.892 3.127 2.066 -0.350 0.012  0.171  443 SER EEE OG  
4189 N N   . LYS C 113 ? 3.230 3.443 2.186 -0.536 0.130  0.114  444 LYS EEE N   
4190 C CA  . LYS C 113 ? 3.126 3.300 1.994 -0.599 0.169  0.117  444 LYS EEE CA  
4191 C C   . LYS C 113 ? 3.025 3.154 1.769 -0.626 0.134  0.177  444 LYS EEE C   
4192 O O   . LYS C 113 ? 2.967 3.117 1.700 -0.604 0.089  0.197  444 LYS EEE O   
4193 C CB  . LYS C 113 ? 3.148 3.367 2.020 -0.640 0.224  0.051  444 LYS EEE CB  
4194 C CG  . LYS C 113 ? 3.148 3.415 2.007 -0.643 0.215  0.026  444 LYS EEE CG  
4195 C CD  . LYS C 113 ? 3.171 3.488 2.080 -0.666 0.270  -0.050 444 LYS EEE CD  
4196 C CE  . LYS C 113 ? 3.153 3.516 2.058 -0.669 0.265  -0.082 444 LYS EEE CE  
4197 N NZ  . LYS C 113 ? 3.126 3.520 2.033 -0.714 0.326  -0.149 444 LYS EEE NZ  
4198 N N   . VAL C 114 ? 3.016 3.083 1.672 -0.671 0.151  0.207  445 VAL EEE N   
4199 C CA  . VAL C 114 ? 3.156 3.165 1.682 -0.699 0.113  0.271  445 VAL EEE CA  
4200 C C   . VAL C 114 ? 3.115 3.159 1.566 -0.735 0.114  0.253  445 VAL EEE C   
4201 O O   . VAL C 114 ? 3.104 3.182 1.552 -0.774 0.171  0.196  445 VAL EEE O   
4202 C CB  . VAL C 114 ? 3.278 3.209 1.716 -0.749 0.139  0.302  445 VAL EEE CB  
4203 C CG1 . VAL C 114 ? 3.427 3.290 1.729 -0.773 0.091  0.373  445 VAL EEE CG1 
4204 C CG2 . VAL C 114 ? 3.199 3.098 1.718 -0.717 0.145  0.309  445 VAL EEE CG2 
4205 N N   . GLY C 115 ? 3.090 3.131 1.494 -0.720 0.054  0.295  446 GLY EEE N   
4206 C CA  . GLY C 115 ? 3.279 3.356 1.620 -0.748 0.046  0.277  446 GLY EEE CA  
4207 C C   . GLY C 115 ? 3.260 3.417 1.711 -0.706 0.039  0.231  446 GLY EEE C   
4208 O O   . GLY C 115 ? 3.371 3.560 1.779 -0.725 0.028  0.215  446 GLY EEE O   
4209 N N   . GLY C 116 ? 3.327 3.512 1.908 -0.653 0.045  0.210  447 GLY EEE N   
4210 C CA  . GLY C 116 ? 3.275 3.523 1.967 -0.602 0.029  0.180  447 GLY EEE CA  
4211 C C   . GLY C 116 ? 3.239 3.536 2.001 -0.608 0.084  0.105  447 GLY EEE C   
4212 O O   . GLY C 116 ? 3.499 3.803 2.201 -0.660 0.124  0.071  447 GLY EEE O   
4213 N N   . ASN C 117 ? 3.015 3.342 1.896 -0.558 0.085  0.081  448 ASN EEE N   
4214 C CA  . ASN C 117 ? 2.933 3.312 1.894 -0.550 0.118  0.013  448 ASN EEE CA  
4215 C C   . ASN C 117 ? 2.783 3.203 1.766 -0.529 0.086  0.007  448 ASN EEE C   
4216 O O   . ASN C 117 ? 2.577 3.002 1.602 -0.485 0.045  0.038  448 ASN EEE O   
4217 C CB  . ASN C 117 ? 2.792 3.177 1.862 -0.508 0.133  -0.009 448 ASN EEE CB  
4218 C CG  . ASN C 117 ? 2.564 2.995 1.716 -0.499 0.161  -0.075 448 ASN EEE CG  
4219 O OD1 . ASN C 117 ? 2.506 2.966 1.640 -0.523 0.175  -0.109 448 ASN EEE OD1 
4220 N ND2 . ASN C 117 ? 2.307 2.742 1.548 -0.464 0.169  -0.096 448 ASN EEE ND2 
4221 N N   . TYR C 118 ? 2.727 3.177 1.686 -0.562 0.109  -0.036 449 TYR EEE N   
4222 C CA  . TYR C 118 ? 2.775 3.262 1.741 -0.553 0.081  -0.046 449 TYR EEE CA  
4223 C C   . TYR C 118 ? 2.753 3.278 1.809 -0.537 0.108  -0.108 449 TYR EEE C   
4224 O O   . TYR C 118 ? 2.865 3.419 1.932 -0.535 0.094  -0.125 449 TYR EEE O   
4225 C CB  . TYR C 118 ? 2.892 3.376 1.745 -0.607 0.079  -0.043 449 TYR EEE CB  
4226 C CG  . TYR C 118 ? 3.076 3.519 1.836 -0.621 0.042  0.023  449 TYR EEE CG  
4227 C CD1 . TYR C 118 ? 3.088 3.533 1.863 -0.585 -0.019 0.071  449 TYR EEE CD1 
4228 C CD2 . TYR C 118 ? 3.210 3.608 1.872 -0.668 0.065  0.038  449 TYR EEE CD2 
4229 C CE1 . TYR C 118 ? 3.125 3.530 1.822 -0.593 -0.060 0.133  449 TYR EEE CE1 
4230 C CE2 . TYR C 118 ? 3.281 3.631 1.855 -0.678 0.025  0.104  449 TYR EEE CE2 
4231 C CZ  . TYR C 118 ? 3.223 3.577 1.817 -0.639 -0.041 0.152  449 TYR EEE CZ  
4232 O OH  . TYR C 118 ? 3.307 3.615 1.824 -0.644 -0.087 0.216  449 TYR EEE OH  
4233 N N   . ASN C 119 ? 2.632 3.155 1.752 -0.525 0.143  -0.139 450 ASN EEE N   
4234 C CA  . ASN C 119 ? 2.621 3.176 1.824 -0.514 0.170  -0.202 450 ASN EEE CA  
4235 C C   . ASN C 119 ? 2.567 3.136 1.846 -0.462 0.135  -0.195 450 ASN EEE C   
4236 O O   . ASN C 119 ? 2.540 3.133 1.868 -0.455 0.144  -0.239 450 ASN EEE O   
4237 C CB  . ASN C 119 ? 2.701 3.250 1.957 -0.514 0.210  -0.236 450 ASN EEE CB  
4238 C CG  . ASN C 119 ? 2.795 3.341 1.988 -0.573 0.258  -0.263 450 ASN EEE CG  
4239 O OD1 . ASN C 119 ? 2.789 3.359 1.968 -0.602 0.282  -0.308 450 ASN EEE OD1 
4240 N ND2 . ASN C 119 ? 3.020 3.535 2.174 -0.592 0.272  -0.238 450 ASN EEE ND2 
4241 N N   . TYR C 120 ? 2.547 3.100 1.835 -0.427 0.100  -0.144 451 TYR EEE N   
4242 C CA  . TYR C 120 ? 2.555 3.118 1.914 -0.378 0.072  -0.135 451 TYR EEE CA  
4243 C C   . TYR C 120 ? 2.408 2.992 1.744 -0.380 0.039  -0.116 451 TYR EEE C   
4244 O O   . TYR C 120 ? 2.282 2.860 1.556 -0.395 0.016  -0.075 451 TYR EEE O   
4245 C CB  . TYR C 120 ? 2.652 3.189 2.039 -0.342 0.057  -0.097 451 TYR EEE CB  
4246 C CG  . TYR C 120 ? 2.521 3.042 1.953 -0.333 0.084  -0.123 451 TYR EEE CG  
4247 C CD1 . TYR C 120 ? 2.417 2.949 1.923 -0.309 0.093  -0.162 451 TYR EEE CD1 
4248 C CD2 . TYR C 120 ? 2.531 3.024 1.933 -0.349 0.098  -0.107 451 TYR EEE CD2 
4249 C CE1 . TYR C 120 ? 2.333 2.853 1.885 -0.299 0.113  -0.186 451 TYR EEE CE1 
4250 C CE2 . TYR C 120 ? 2.428 2.910 1.879 -0.341 0.122  -0.131 451 TYR EEE CE2 
4251 C CZ  . TYR C 120 ? 2.303 2.800 1.830 -0.315 0.128  -0.172 451 TYR EEE CZ  
4252 O OH  . TYR C 120 ? 2.228 2.718 1.809 -0.306 0.145  -0.199 451 TYR EEE OH  
4253 N N   . LEU C 121 ? 2.310 2.916 1.695 -0.365 0.037  -0.144 452 LEU EEE N   
4254 C CA  . LEU C 121 ? 2.357 2.987 1.732 -0.370 0.010  -0.137 452 LEU EEE CA  
4255 C C   . LEU C 121 ? 2.261 2.896 1.699 -0.326 -0.014 -0.116 452 LEU EEE C   
4256 O O   . LEU C 121 ? 2.058 2.677 1.546 -0.293 -0.007 -0.117 452 LEU EEE O   
4257 C CB  . LEU C 121 ? 2.405 3.052 1.786 -0.394 0.030  -0.191 452 LEU EEE CB  
4258 C CG  . LEU C 121 ? 2.432 3.079 1.761 -0.439 0.065  -0.227 452 LEU EEE CG  
4259 C CD1 . LEU C 121 ? 2.410 3.077 1.738 -0.462 0.074  -0.272 452 LEU EEE CD1 
4260 C CD2 . LEU C 121 ? 2.552 3.188 1.787 -0.473 0.058  -0.193 452 LEU EEE CD2 
4261 N N   . TYR C 122 ? 2.260 2.919 1.691 -0.329 -0.042 -0.100 453 TYR EEE N   
4262 C CA  . TYR C 122 ? 2.157 2.831 1.645 -0.300 -0.061 -0.090 453 TYR EEE CA  
4263 C C   . TYR C 122 ? 2.073 2.777 1.551 -0.324 -0.074 -0.103 453 TYR EEE C   
4264 O O   . TYR C 122 ? 2.071 2.784 1.490 -0.360 -0.080 -0.106 453 TYR EEE O   
4265 C CB  . TYR C 122 ? 2.186 2.860 1.687 -0.272 -0.087 -0.040 453 TYR EEE CB  
4266 C CG  . TYR C 122 ? 2.133 2.821 1.585 -0.290 -0.118 -0.006 453 TYR EEE CG  
4267 C CD1 . TYR C 122 ? 2.110 2.776 1.502 -0.307 -0.119 0.015  453 TYR EEE CD1 
4268 C CD2 . TYR C 122 ? 2.144 2.867 1.612 -0.291 -0.148 0.008  453 TYR EEE CD2 
4269 C CE1 . TYR C 122 ? 2.287 2.959 1.630 -0.322 -0.154 0.050  453 TYR EEE CE1 
4270 C CE2 . TYR C 122 ? 2.236 2.972 1.665 -0.305 -0.183 0.041  453 TYR EEE CE2 
4271 C CZ  . TYR C 122 ? 2.365 3.073 1.728 -0.320 -0.188 0.063  453 TYR EEE CZ  
4272 O OH  . TYR C 122 ? 2.738 3.453 2.054 -0.334 -0.229 0.098  453 TYR EEE OH  
4273 N N   . ARG C 123 ? 2.045 2.759 1.577 -0.307 -0.078 -0.113 454 ARG EEE N   
4274 C CA  . ARG C 123 ? 2.009 2.752 1.545 -0.327 -0.094 -0.122 454 ARG EEE CA  
4275 C C   . ARG C 123 ? 2.121 2.893 1.663 -0.319 -0.130 -0.079 454 ARG EEE C   
4276 O O   . ARG C 123 ? 1.906 2.678 1.494 -0.285 -0.136 -0.054 454 ARG EEE O   
4277 C CB  . ARG C 123 ? 1.902 2.638 1.492 -0.314 -0.082 -0.148 454 ARG EEE CB  
4278 C CG  . ARG C 123 ? 1.963 2.724 1.556 -0.339 -0.094 -0.164 454 ARG EEE CG  
4279 C CD  . ARG C 123 ? 2.073 2.813 1.711 -0.330 -0.079 -0.193 454 ARG EEE CD  
4280 N NE  . ARG C 123 ? 2.155 2.862 1.793 -0.328 -0.052 -0.230 454 ARG EEE NE  
4281 C CZ  . ARG C 123 ? 2.255 2.958 1.873 -0.356 -0.039 -0.273 454 ARG EEE CZ  
4282 N NH1 . ARG C 123 ? 2.326 3.055 1.913 -0.391 -0.048 -0.284 454 ARG EEE NH1 
4283 N NH2 . ARG C 123 ? 2.166 2.844 1.801 -0.349 -0.015 -0.308 454 ARG EEE NH2 
4284 N N   . LEU C 124 ? 2.371 3.167 1.870 -0.351 -0.152 -0.075 455 LEU EEE N   
4285 C CA  . LEU C 124 ? 2.294 3.120 1.790 -0.350 -0.194 -0.035 455 LEU EEE CA  
4286 C C   . LEU C 124 ? 2.106 2.971 1.649 -0.356 -0.210 -0.045 455 LEU EEE C   
4287 O O   . LEU C 124 ? 1.904 2.799 1.489 -0.339 -0.239 -0.015 455 LEU EEE O   
4288 C CB  . LEU C 124 ? 2.480 3.302 1.888 -0.385 -0.210 -0.028 455 LEU EEE CB  
4289 C CG  . LEU C 124 ? 2.681 3.530 2.073 -0.389 -0.261 0.012  455 LEU EEE CG  
4290 C CD1 . LEU C 124 ? 2.583 3.430 2.021 -0.347 -0.279 0.056  455 LEU EEE CD1 
4291 C CD2 . LEU C 124 ? 2.798 3.631 2.085 -0.429 -0.275 0.018  455 LEU EEE CD2 
4292 N N   . PHE C 125 ? 2.069 2.931 1.610 -0.379 -0.192 -0.087 456 PHE EEE N   
4293 C CA  . PHE C 125 ? 2.176 3.069 1.755 -0.394 -0.204 -0.103 456 PHE EEE CA  
4294 C C   . PHE C 125 ? 2.110 2.980 1.728 -0.389 -0.171 -0.138 456 PHE EEE C   
4295 O O   . PHE C 125 ? 1.976 2.812 1.570 -0.394 -0.144 -0.167 456 PHE EEE O   
4296 C CB  . PHE C 125 ? 2.273 3.185 1.798 -0.439 -0.221 -0.124 456 PHE EEE CB  
4297 C CG  . PHE C 125 ? 2.255 3.185 1.727 -0.453 -0.259 -0.092 456 PHE EEE CG  
4298 C CD1 . PHE C 125 ? 2.160 3.128 1.672 -0.437 -0.299 -0.055 456 PHE EEE CD1 
4299 C CD2 . PHE C 125 ? 2.284 3.192 1.666 -0.480 -0.255 -0.100 456 PHE EEE CD2 
4300 C CE1 . PHE C 125 ? 2.192 3.171 1.654 -0.446 -0.341 -0.022 456 PHE EEE CE1 
4301 C CE2 . PHE C 125 ? 2.348 3.262 1.670 -0.493 -0.292 -0.065 456 PHE EEE CE2 
4302 C CZ  . PHE C 125 ? 2.351 3.299 1.713 -0.475 -0.338 -0.026 456 PHE EEE CZ  
4303 N N   . ARG C 126 ? 1.999 2.889 1.674 -0.384 -0.177 -0.135 457 ARG EEE N   
4304 C CA  . ARG C 126 ? 1.941 2.807 1.652 -0.383 -0.153 -0.162 457 ARG EEE CA  
4305 C C   . ARG C 126 ? 1.886 2.787 1.650 -0.390 -0.168 -0.154 457 ARG EEE C   
4306 O O   . ARG C 126 ? 1.786 2.725 1.579 -0.377 -0.188 -0.122 457 ARG EEE O   
4307 C CB  . ARG C 126 ? 2.084 2.911 1.817 -0.345 -0.130 -0.153 457 ARG EEE CB  
4308 C CG  . ARG C 126 ? 2.119 2.900 1.862 -0.343 -0.105 -0.186 457 ARG EEE CG  
4309 C CD  . ARG C 126 ? 1.985 2.728 1.744 -0.306 -0.088 -0.174 457 ARG EEE CD  
4310 N NE  . ARG C 126 ? 1.912 2.607 1.678 -0.303 -0.071 -0.204 457 ARG EEE NE  
4311 C CZ  . ARG C 126 ? 1.851 2.523 1.643 -0.303 -0.066 -0.209 457 ARG EEE CZ  
4312 N NH1 . ARG C 126 ? 1.796 2.490 1.613 -0.306 -0.071 -0.187 457 ARG EEE NH1 
4313 N NH2 . ARG C 126 ? 1.837 2.459 1.632 -0.299 -0.055 -0.237 457 ARG EEE NH2 
4314 N N   . LYS C 127 ? 1.925 2.813 1.705 -0.409 -0.156 -0.184 458 LYS EEE N   
4315 C CA  . LYS C 127 ? 2.069 2.990 1.898 -0.426 -0.167 -0.184 458 LYS EEE CA  
4316 C C   . LYS C 127 ? 2.029 2.952 1.914 -0.399 -0.154 -0.158 458 LYS EEE C   
4317 O O   . LYS C 127 ? 1.788 2.756 1.721 -0.407 -0.166 -0.146 458 LYS EEE O   
4318 C CB  . LYS C 127 ? 2.198 3.089 2.022 -0.455 -0.153 -0.224 458 LYS EEE CB  
4319 C CG  . LYS C 127 ? 2.317 3.198 2.085 -0.481 -0.156 -0.258 458 LYS EEE CG  
4320 C CD  . LYS C 127 ? 2.467 3.340 2.240 -0.516 -0.154 -0.297 458 LYS EEE CD  
4321 C CE  . LYS C 127 ? 2.485 3.296 2.274 -0.507 -0.125 -0.322 458 LYS EEE CE  
4322 N NZ  . LYS C 127 ? 2.661 3.455 2.440 -0.543 -0.123 -0.368 458 LYS EEE NZ  
4323 N N   . SER C 128 ? 2.238 3.112 2.115 -0.369 -0.131 -0.152 459 SER EEE N   
4324 C CA  . SER C 128 ? 2.355 3.210 2.269 -0.346 -0.110 -0.136 459 SER EEE CA  
4325 C C   . SER C 128 ? 2.266 3.086 2.160 -0.309 -0.098 -0.120 459 SER EEE C   
4326 O O   . SER C 128 ? 2.198 2.998 2.053 -0.305 -0.100 -0.131 459 SER EEE O   
4327 C CB  . SER C 128 ? 2.490 3.300 2.409 -0.361 -0.092 -0.158 459 SER EEE CB  
4328 O OG  . SER C 128 ? 2.447 3.194 2.331 -0.351 -0.079 -0.177 459 SER EEE OG  
4329 N N   . ASN C 129 ? 2.201 3.015 2.122 -0.285 -0.085 -0.099 460 ASN EEE N   
4330 C CA  . ASN C 129 ? 2.151 2.932 2.056 -0.249 -0.074 -0.085 460 ASN EEE CA  
4331 C C   . ASN C 129 ? 2.072 2.784 1.946 -0.244 -0.059 -0.105 460 ASN EEE C   
4332 O O   . ASN C 129 ? 1.966 2.654 1.844 -0.262 -0.051 -0.121 460 ASN EEE O   
4333 C CB  . ASN C 129 ? 2.186 2.983 2.127 -0.226 -0.064 -0.059 460 ASN EEE CB  
4334 C CG  . ASN C 129 ? 2.214 3.077 2.190 -0.222 -0.084 -0.039 460 ASN EEE CG  
4335 O OD1 . ASN C 129 ? 2.165 3.053 2.126 -0.233 -0.109 -0.039 460 ASN EEE OD1 
4336 N ND2 . ASN C 129 ? 2.358 3.246 2.381 -0.207 -0.074 -0.023 460 ASN EEE ND2 
4337 N N   . LEU C 130 ? 2.023 2.706 1.872 -0.222 -0.056 -0.105 461 LEU EEE N   
4338 C CA  . LEU C 130 ? 1.933 2.553 1.763 -0.207 -0.045 -0.120 461 LEU EEE CA  
4339 C C   . LEU C 130 ? 1.906 2.490 1.742 -0.192 -0.032 -0.106 461 LEU EEE C   
4340 O O   . LEU C 130 ? 1.793 2.399 1.644 -0.180 -0.026 -0.082 461 LEU EEE O   
4341 C CB  . LEU C 130 ? 1.929 2.538 1.741 -0.184 -0.046 -0.117 461 LEU EEE CB  
4342 C CG  . LEU C 130 ? 1.901 2.529 1.694 -0.199 -0.053 -0.134 461 LEU EEE CG  
4343 C CD1 . LEU C 130 ? 1.806 2.416 1.585 -0.178 -0.049 -0.132 461 LEU EEE CD1 
4344 C CD2 . LEU C 130 ? 1.980 2.589 1.769 -0.221 -0.050 -0.170 461 LEU EEE CD2 
4345 N N   . LYS C 131 ? 1.860 2.387 1.682 -0.194 -0.028 -0.122 462 LYS EEE N   
4346 C CA  . LYS C 131 ? 1.907 2.379 1.714 -0.177 -0.018 -0.110 462 LYS EEE CA  
4347 C C   . LYS C 131 ? 1.976 2.428 1.766 -0.146 -0.020 -0.104 462 LYS EEE C   
4348 O O   . LYS C 131 ? 1.911 2.381 1.703 -0.140 -0.028 -0.115 462 LYS EEE O   
4349 C CB  . LYS C 131 ? 2.023 2.433 1.816 -0.186 -0.021 -0.129 462 LYS EEE CB  
4350 C CG  . LYS C 131 ? 2.047 2.462 1.853 -0.219 -0.018 -0.135 462 LYS EEE CG  
4351 C CD  . LYS C 131 ? 2.113 2.540 1.925 -0.229 -0.001 -0.111 462 LYS EEE CD  
4352 C CE  . LYS C 131 ? 2.219 2.642 2.044 -0.263 0.004  -0.117 462 LYS EEE CE  
4353 N NZ  . LYS C 131 ? 2.235 2.720 2.094 -0.280 0.017  -0.102 462 LYS EEE NZ  
4354 N N   . PRO C 132 ? 2.044 2.459 1.816 -0.126 -0.012 -0.088 463 PRO EEE N   
4355 C CA  . PRO C 132 ? 2.062 2.462 1.822 -0.098 -0.014 -0.084 463 PRO EEE CA  
4356 C C   . PRO C 132 ? 2.085 2.445 1.835 -0.088 -0.029 -0.107 463 PRO EEE C   
4357 O O   . PRO C 132 ? 1.872 2.186 1.613 -0.094 -0.035 -0.120 463 PRO EEE O   
4358 C CB  . PRO C 132 ? 2.108 2.473 1.844 -0.085 -0.001 -0.065 463 PRO EEE CB  
4359 C CG  . PRO C 132 ? 2.087 2.465 1.832 -0.110 0.013  -0.057 463 PRO EEE CG  
4360 C CD  . PRO C 132 ? 2.010 2.390 1.767 -0.134 0.001  -0.076 463 PRO EEE CD  
4361 N N   . PHE C 133 ? 2.040 2.420 1.797 -0.077 -0.034 -0.114 464 PHE EEE N   
4362 C CA  . PHE C 133 ? 2.033 2.387 1.793 -0.066 -0.044 -0.140 464 PHE EEE CA  
4363 C C   . PHE C 133 ? 1.960 2.322 1.737 -0.088 -0.047 -0.168 464 PHE EEE C   
4364 O O   . PHE C 133 ? 1.729 2.060 1.517 -0.080 -0.056 -0.194 464 PHE EEE O   
4365 C CB  . PHE C 133 ? 2.116 2.405 1.859 -0.044 -0.054 -0.141 464 PHE EEE CB  
4366 C CG  . PHE C 133 ? 2.014 2.289 1.736 -0.022 -0.051 -0.122 464 PHE EEE CG  
4367 C CD1 . PHE C 133 ? 1.964 2.269 1.697 -0.013 -0.048 -0.120 464 PHE EEE CD1 
4368 C CD2 . PHE C 133 ? 1.961 2.187 1.650 -0.012 -0.052 -0.107 464 PHE EEE CD2 
4369 C CE1 . PHE C 133 ? 1.856 2.146 1.572 0.008  -0.046 -0.105 464 PHE EEE CE1 
4370 C CE2 . PHE C 133 ? 2.028 2.240 1.696 0.007  -0.048 -0.094 464 PHE EEE CE2 
4371 C CZ  . PHE C 133 ? 1.950 2.195 1.635 0.018  -0.045 -0.094 464 PHE EEE CZ  
4372 N N   . GLU C 134 ? 2.064 2.467 1.847 -0.113 -0.042 -0.165 465 GLU EEE N   
4373 C CA  . GLU C 134 ? 2.007 2.422 1.802 -0.137 -0.043 -0.195 465 GLU EEE CA  
4374 C C   . GLU C 134 ? 1.833 2.279 1.631 -0.140 -0.040 -0.211 465 GLU EEE C   
4375 O O   . GLU C 134 ? 1.693 2.163 1.482 -0.132 -0.038 -0.190 465 GLU EEE O   
4376 C CB  . GLU C 134 ? 2.140 2.590 1.937 -0.165 -0.040 -0.186 465 GLU EEE CB  
4377 C CG  . GLU C 134 ? 2.207 2.669 2.012 -0.192 -0.041 -0.219 465 GLU EEE CG  
4378 C CD  . GLU C 134 ? 2.318 2.800 2.128 -0.220 -0.042 -0.216 465 GLU EEE CD  
4379 O OE1 . GLU C 134 ? 2.346 2.849 2.159 -0.221 -0.040 -0.187 465 GLU EEE OE1 
4380 O OE2 . GLU C 134 ? 2.256 2.735 2.072 -0.242 -0.042 -0.247 465 GLU EEE OE2 
4381 N N   . ARG C 135 ? 1.746 2.187 1.557 -0.151 -0.038 -0.248 466 ARG EEE N   
4382 C CA  . ARG C 135 ? 1.797 2.271 1.608 -0.163 -0.029 -0.270 466 ARG EEE CA  
4383 C C   . ARG C 135 ? 1.938 2.434 1.747 -0.195 -0.023 -0.298 466 ARG EEE C   
4384 O O   . ARG C 135 ? 2.050 2.520 1.880 -0.198 -0.023 -0.330 466 ARG EEE O   
4385 C CB  . ARG C 135 ? 1.778 2.224 1.612 -0.143 -0.028 -0.296 466 ARG EEE CB  
4386 C CG  . ARG C 135 ? 1.871 2.348 1.702 -0.153 -0.014 -0.309 466 ARG EEE CG  
4387 C CD  . ARG C 135 ? 1.997 2.449 1.863 -0.132 -0.014 -0.337 466 ARG EEE CD  
4388 N NE  . ARG C 135 ? 2.106 2.587 1.979 -0.148 0.006  -0.363 466 ARG EEE NE  
4389 C CZ  . ARG C 135 ? 2.101 2.595 1.998 -0.166 0.022  -0.409 466 ARG EEE CZ  
4390 N NH1 . ARG C 135 ? 2.127 2.605 2.046 -0.169 0.018  -0.437 466 ARG EEE NH1 
4391 N NH2 . ARG C 135 ? 1.991 2.511 1.887 -0.183 0.044  -0.429 466 ARG EEE NH2 
4392 N N   . ASP C 136 ? 2.070 2.610 1.853 -0.219 -0.021 -0.287 467 ASP EEE N   
4393 C CA  . ASP C 136 ? 2.113 2.679 1.882 -0.255 -0.018 -0.310 467 ASP EEE CA  
4394 C C   . ASP C 136 ? 2.059 2.648 1.805 -0.275 -0.004 -0.333 467 ASP EEE C   
4395 O O   . ASP C 136 ? 1.950 2.563 1.665 -0.279 -0.005 -0.306 467 ASP EEE O   
4396 C CB  . ASP C 136 ? 2.190 2.788 1.944 -0.270 -0.031 -0.278 467 ASP EEE CB  
4397 C CG  . ASP C 136 ? 2.224 2.850 1.960 -0.308 -0.033 -0.299 467 ASP EEE CG  
4398 O OD1 . ASP C 136 ? 2.435 3.051 2.168 -0.324 -0.021 -0.342 467 ASP EEE OD1 
4399 O OD2 . ASP C 136 ? 2.271 2.929 1.998 -0.322 -0.047 -0.275 467 ASP EEE OD2 
4400 N N   . ILE C 137 ? 1.981 2.562 1.740 -0.288 0.011  -0.381 468 ILE EEE N   
4401 C CA  . ILE C 137 ? 2.089 2.691 1.825 -0.313 0.032  -0.411 468 ILE EEE CA  
4402 C C   . ILE C 137 ? 2.257 2.877 1.968 -0.352 0.039  -0.443 468 ILE EEE C   
4403 O O   . ILE C 137 ? 2.381 3.010 2.078 -0.375 0.062  -0.483 468 ILE EEE O   
4404 C CB  . ILE C 137 ? 2.017 2.598 1.795 -0.295 0.049  -0.447 468 ILE EEE CB  
4405 C CG1 . ILE C 137 ? 1.966 2.518 1.796 -0.285 0.049  -0.488 468 ILE EEE CG1 
4406 C CG2 . ILE C 137 ? 2.005 2.573 1.797 -0.261 0.041  -0.413 468 ILE EEE CG2 
4407 C CD1 . ILE C 137 ? 1.945 2.488 1.825 -0.273 0.066  -0.534 468 ILE EEE CD1 
4408 N N   . SER C 138 ? 2.264 2.890 1.967 -0.362 0.021  -0.427 469 SER EEE N   
4409 C CA  A SER C 138 ? 2.229 2.874 1.901 -0.402 0.022  -0.454 469 SER EEE CA  
4410 C CA  B SER C 138 ? 2.220 2.865 1.893 -0.402 0.022  -0.454 469 SER EEE CA  
4411 C C   . SER C 138 ? 2.230 2.911 1.837 -0.431 0.021  -0.437 469 SER EEE C   
4412 O O   . SER C 138 ? 1.926 2.616 1.517 -0.416 0.008  -0.391 469 SER EEE O   
4413 C CB  A SER C 138 ? 2.262 2.905 1.949 -0.406 0.001  -0.440 469 SER EEE CB  
4414 C CB  B SER C 138 ? 2.245 2.889 1.931 -0.407 0.001  -0.441 469 SER EEE CB  
4415 O OG  A SER C 138 ? 2.280 2.947 1.955 -0.399 -0.021 -0.387 469 SER EEE OG  
4416 O OG  B SER C 138 ? 2.320 2.984 1.976 -0.447 0.001  -0.469 469 SER EEE OG  
4417 N N   . THR C 139 ? 2.417 3.110 1.983 -0.470 0.033  -0.474 470 THR EEE N   
4418 C CA  . THR C 139 ? 2.404 3.125 1.891 -0.506 0.031  -0.463 470 THR EEE CA  
4419 C C   . THR C 139 ? 2.358 3.096 1.809 -0.543 0.017  -0.480 470 THR EEE C   
4420 O O   . THR C 139 ? 2.362 3.113 1.742 -0.582 0.023  -0.494 470 THR EEE O   
4421 C CB  . THR C 139 ? 2.438 3.154 1.898 -0.522 0.068  -0.499 470 THR EEE CB  
4422 O OG1 . THR C 139 ? 2.431 3.134 1.931 -0.528 0.092  -0.561 470 THR EEE OG1 
4423 C CG2 . THR C 139 ? 2.447 3.151 1.932 -0.491 0.078  -0.477 470 THR EEE CG2 
4424 N N   . GLU C 140 ? 2.423 3.158 1.918 -0.535 -0.001 -0.479 471 GLU EEE N   
4425 C CA  A GLU C 140 ? 2.651 3.405 2.124 -0.569 -0.020 -0.491 471 GLU EEE CA  
4426 C CA  B GLU C 140 ? 2.560 3.314 2.032 -0.570 -0.019 -0.492 471 GLU EEE CA  
4427 C C   . GLU C 140 ? 2.685 3.475 2.103 -0.586 -0.053 -0.446 471 GLU EEE C   
4428 O O   . GLU C 140 ? 2.603 3.401 2.034 -0.557 -0.070 -0.395 471 GLU EEE O   
4429 C CB  A GLU C 140 ? 2.673 3.415 2.211 -0.554 -0.032 -0.491 471 GLU EEE CB  
4430 C CB  B GLU C 140 ? 2.461 3.198 2.000 -0.555 -0.027 -0.499 471 GLU EEE CB  
4431 C CG  A GLU C 140 ? 2.789 3.557 2.310 -0.589 -0.057 -0.494 471 GLU EEE CG  
4432 C CG  B GLU C 140 ? 2.395 3.093 1.975 -0.548 0.002  -0.553 471 GLU EEE CG  
4433 C CD  A GLU C 140 ? 2.810 3.559 2.389 -0.586 -0.061 -0.509 471 GLU EEE CD  
4434 C CD  B GLU C 140 ? 2.345 3.010 1.991 -0.524 -0.005 -0.550 471 GLU EEE CD  
4435 O OE1 A GLU C 140 ? 2.707 3.417 2.337 -0.556 -0.046 -0.513 471 GLU EEE OE1 
4436 O OE1 B GLU C 140 ? 2.398 3.063 2.068 -0.496 -0.020 -0.503 471 GLU EEE OE1 
4437 O OE2 A GLU C 140 ? 2.866 3.636 2.437 -0.617 -0.080 -0.516 471 GLU EEE OE2 
4438 O OE2 B GLU C 140 ? 2.240 2.879 1.912 -0.535 0.005  -0.595 471 GLU EEE OE2 
4439 N N   . ILE C 141 ? 2.602 3.410 1.958 -0.629 -0.064 -0.465 472 ILE EEE N   
4440 C CA  . ILE C 141 ? 2.555 3.396 1.854 -0.648 -0.103 -0.423 472 ILE EEE CA  
4441 C C   . ILE C 141 ? 2.452 3.318 1.812 -0.628 -0.139 -0.386 472 ILE EEE C   
4442 O O   . ILE C 141 ? 2.369 3.232 1.782 -0.630 -0.137 -0.409 472 ILE EEE O   
4443 C CB  . ILE C 141 ? 2.757 3.608 1.973 -0.702 -0.109 -0.456 472 ILE EEE CB  
4444 C CG1 . ILE C 141 ? 2.822 3.650 1.981 -0.723 -0.065 -0.498 472 ILE EEE CG1 
4445 C CG2 . ILE C 141 ? 2.888 3.770 2.045 -0.719 -0.158 -0.411 472 ILE EEE CG2 
4446 C CD1 . ILE C 141 ? 2.845 3.661 1.989 -0.700 -0.051 -0.464 472 ILE EEE CD1 
4447 N N   . TYR C 142 ? 2.379 3.265 1.733 -0.611 -0.168 -0.332 473 TYR EEE N   
4448 C CA  . TYR C 142 ? 2.314 3.229 1.736 -0.587 -0.199 -0.294 473 TYR EEE CA  
4449 C C   . TYR C 142 ? 2.264 3.221 1.664 -0.618 -0.243 -0.285 473 TYR EEE C   
4450 O O   . TYR C 142 ? 2.192 3.160 1.522 -0.635 -0.268 -0.266 473 TYR EEE O   
4451 C CB  . TYR C 142 ? 2.314 3.229 1.752 -0.548 -0.206 -0.242 473 TYR EEE CB  
4452 C CG  . TYR C 142 ? 2.186 3.133 1.697 -0.524 -0.232 -0.208 473 TYR EEE CG  
4453 C CD1 . TYR C 142 ? 2.078 3.017 1.663 -0.503 -0.213 -0.216 473 TYR EEE CD1 
4454 C CD2 . TYR C 142 ? 2.205 3.191 1.712 -0.524 -0.276 -0.170 473 TYR EEE CD2 
4455 C CE1 . TYR C 142 ? 2.119 3.089 1.770 -0.485 -0.230 -0.188 473 TYR EEE CE1 
4456 C CE2 . TYR C 142 ? 2.194 3.215 1.779 -0.502 -0.296 -0.143 473 TYR EEE CE2 
4457 C CZ  . TYR C 142 ? 2.093 3.109 1.751 -0.484 -0.270 -0.154 473 TYR EEE CZ  
4458 O OH  . TYR C 142 ? 2.013 3.066 1.746 -0.466 -0.286 -0.130 473 TYR EEE OH  
4459 N N   . GLN C 143 ? 2.293 3.272 1.753 -0.625 -0.254 -0.297 474 GLN EEE N   
4460 C CA  . GLN C 143 ? 2.420 3.447 1.885 -0.651 -0.300 -0.290 474 GLN EEE CA  
4461 C C   . GLN C 143 ? 2.609 3.676 2.127 -0.622 -0.335 -0.236 474 GLN EEE C   
4462 O O   . GLN C 143 ? 2.712 3.791 2.317 -0.598 -0.327 -0.226 474 GLN EEE O   
4463 C CB  . GLN C 143 ? 2.266 3.295 1.781 -0.671 -0.291 -0.329 474 GLN EEE CB  
4464 C CG  . GLN C 143 ? 2.287 3.371 1.832 -0.695 -0.336 -0.322 474 GLN EEE CG  
4465 C CD  . GLN C 143 ? 2.435 3.515 2.026 -0.718 -0.323 -0.362 474 GLN EEE CD  
4466 O OE1 . GLN C 143 ? 2.538 3.571 2.132 -0.719 -0.284 -0.396 474 GLN EEE OE1 
4467 N NE2 . GLN C 143 ? 2.509 3.639 2.144 -0.738 -0.359 -0.358 474 GLN EEE NE2 
4468 N N   . ALA C 144 ? 2.820 3.905 2.288 -0.623 -0.373 -0.202 475 ALA EEE N   
4469 C CA  . ALA C 144 ? 2.878 3.999 2.396 -0.592 -0.410 -0.151 475 ALA EEE CA  
4470 C C   . ALA C 144 ? 2.989 4.170 2.542 -0.612 -0.463 -0.145 475 ALA EEE C   
4471 O O   . ALA C 144 ? 3.101 4.323 2.734 -0.584 -0.488 -0.113 475 ALA EEE O   
4472 C CB  . ALA C 144 ? 2.942 4.042 2.388 -0.581 -0.424 -0.116 475 ALA EEE CB  
4473 N N   . GLY C 145 ? 2.971 4.158 2.468 -0.658 -0.480 -0.177 476 GLY EEE N   
4474 C CA  . GLY C 145 ? 2.964 4.208 2.491 -0.685 -0.532 -0.182 476 GLY EEE CA  
4475 C C   . GLY C 145 ? 2.914 4.167 2.495 -0.709 -0.508 -0.227 476 GLY EEE C   
4476 O O   . GLY C 145 ? 2.953 4.171 2.569 -0.694 -0.456 -0.245 476 GLY EEE O   
4477 N N   . SER C 146 ? 2.736 4.029 2.323 -0.746 -0.548 -0.246 477 SER EEE N   
4478 C CA  . SER C 146 ? 2.629 3.936 2.280 -0.770 -0.532 -0.286 477 SER EEE CA  
4479 C C   . SER C 146 ? 2.666 3.929 2.239 -0.812 -0.506 -0.340 477 SER EEE C   
4480 O O   . SER C 146 ? 2.731 3.996 2.351 -0.834 -0.492 -0.376 477 SER EEE O   
4481 C CB  . SER C 146 ? 2.584 3.964 2.304 -0.786 -0.586 -0.279 477 SER EEE CB  
4482 O OG  . SER C 146 ? 2.635 4.036 2.281 -0.807 -0.646 -0.267 477 SER EEE OG  
4483 N N   . THR C 147 ? 2.654 3.876 2.116 -0.823 -0.497 -0.348 478 THR EEE N   
4484 C CA  . THR C 147 ? 2.742 3.922 2.127 -0.862 -0.468 -0.405 478 THR EEE CA  
4485 C C   . THR C 147 ? 2.586 3.707 1.967 -0.839 -0.403 -0.423 478 THR EEE C   
4486 O O   . THR C 147 ? 2.521 3.625 1.888 -0.806 -0.389 -0.391 478 THR EEE O   
4487 C CB  . THR C 147 ? 2.924 4.101 2.181 -0.899 -0.498 -0.411 478 THR EEE CB  
4488 O OG1 . THR C 147 ? 3.115 4.347 2.384 -0.919 -0.564 -0.396 478 THR EEE OG1 
4489 C CG2 . THR C 147 ? 2.980 4.117 2.159 -0.942 -0.465 -0.474 478 THR EEE CG2 
4490 N N   . PRO C 148 ? 2.601 3.687 1.998 -0.855 -0.365 -0.475 479 PRO EEE N   
4491 C CA  . PRO C 148 ? 2.603 3.633 2.000 -0.834 -0.308 -0.497 479 PRO EEE CA  
4492 C C   . PRO C 148 ? 2.698 3.702 1.990 -0.848 -0.290 -0.514 479 PRO EEE C   
4493 O O   . PRO C 148 ? 2.889 3.903 2.104 -0.890 -0.309 -0.537 479 PRO EEE O   
4494 C CB  . PRO C 148 ? 2.577 3.581 2.012 -0.855 -0.284 -0.550 479 PRO EEE CB  
4495 C CG  . PRO C 148 ? 2.606 3.657 2.091 -0.876 -0.325 -0.543 479 PRO EEE CG  
4496 C CD  . PRO C 148 ? 2.734 3.832 2.157 -0.894 -0.375 -0.516 479 PRO EEE CD  
4497 N N   . CYS C 149 ? 2.766 3.737 2.056 -0.816 -0.253 -0.505 480 CYS EEE N   
4498 C CA  . CYS C 149 ? 2.964 3.912 2.164 -0.826 -0.230 -0.515 480 CYS EEE CA  
4499 C C   . CYS C 149 ? 3.159 4.068 2.343 -0.844 -0.181 -0.584 480 CYS EEE C   
4500 O O   . CYS C 149 ? 3.268 4.168 2.360 -0.879 -0.168 -0.613 480 CYS EEE O   
4501 C CB  . CYS C 149 ? 2.882 3.819 2.095 -0.782 -0.218 -0.469 480 CYS EEE CB  
4502 S SG  . CYS C 149 ? 2.869 3.849 2.113 -0.753 -0.273 -0.392 480 CYS EEE SG  
4503 N N   . ASN C 150 ? 3.169 4.052 2.437 -0.822 -0.153 -0.607 481 ASN EEE N   
4504 C CA  . ASN C 150 ? 3.148 3.990 2.424 -0.830 -0.107 -0.673 481 ASN EEE CA  
4505 C C   . ASN C 150 ? 3.270 4.097 2.481 -0.834 -0.072 -0.691 481 ASN EEE C   
4506 O O   . ASN C 150 ? 3.231 4.046 2.389 -0.870 -0.047 -0.748 481 ASN EEE O   
4507 C CB  . ASN C 150 ? 3.069 3.910 2.331 -0.874 -0.112 -0.726 481 ASN EEE CB  
4508 C CG  . ASN C 150 ? 3.025 3.878 2.361 -0.869 -0.142 -0.708 481 ASN EEE CG  
4509 O OD1 . ASN C 150 ? 2.863 3.706 2.274 -0.830 -0.139 -0.676 481 ASN EEE OD1 
4510 N ND2 . ASN C 150 ? 3.069 3.943 2.381 -0.911 -0.169 -0.728 481 ASN EEE ND2 
4511 N N   . GLY C 151 ? 3.395 4.222 2.614 -0.800 -0.069 -0.645 482 GLY EEE N   
4512 C CA  . GLY C 151 ? 3.437 4.248 2.618 -0.796 -0.030 -0.658 482 GLY EEE CA  
4513 C C   . GLY C 151 ? 3.504 4.328 2.567 -0.837 -0.036 -0.653 482 GLY EEE C   
4514 O O   . GLY C 151 ? 3.507 4.315 2.527 -0.849 0.005  -0.680 482 GLY EEE O   
4515 N N   . VAL C 152 ? 3.553 4.403 2.564 -0.860 -0.084 -0.619 483 VAL EEE N   
4516 C CA  . VAL C 152 ? 3.609 4.467 2.496 -0.898 -0.100 -0.602 483 VAL EEE CA  
4517 C C   . VAL C 152 ? 3.463 4.340 2.343 -0.875 -0.150 -0.523 483 VAL EEE C   
4518 O O   . VAL C 152 ? 3.418 4.323 2.350 -0.862 -0.194 -0.495 483 VAL EEE O   
4519 C CB  . VAL C 152 ? 3.780 4.646 2.587 -0.954 -0.115 -0.641 483 VAL EEE CB  
4520 C CG1 . VAL C 152 ? 3.862 4.722 2.526 -0.997 -0.122 -0.630 483 VAL EEE CG1 
4521 C CG2 . VAL C 152 ? 3.900 4.747 2.734 -0.972 -0.069 -0.722 483 VAL EEE CG2 
4522 N N   . GLU C 153 ? 3.275 4.139 2.095 -0.872 -0.142 -0.491 484 GLU EEE N   
4523 C CA  . GLU C 153 ? 3.117 3.991 1.917 -0.853 -0.189 -0.416 484 GLU EEE CA  
4524 C C   . GLU C 153 ? 3.220 4.111 1.926 -0.894 -0.243 -0.399 484 GLU EEE C   
4525 O O   . GLU C 153 ? 3.439 4.319 2.055 -0.944 -0.229 -0.443 484 GLU EEE O   
4526 C CB  . GLU C 153 ? 3.083 3.928 1.848 -0.841 -0.157 -0.395 484 GLU EEE CB  
4527 C CG  . GLU C 153 ? 3.035 3.867 1.901 -0.799 -0.110 -0.414 484 GLU EEE CG  
4528 C CD  . GLU C 153 ? 2.956 3.761 1.797 -0.792 -0.068 -0.410 484 GLU EEE CD  
4529 O OE1 . GLU C 153 ? 3.074 3.871 1.885 -0.779 -0.089 -0.355 484 GLU EEE OE1 
4530 O OE2 . GLU C 153 ? 2.669 3.460 1.530 -0.798 -0.014 -0.464 484 GLU EEE OE2 
4531 N N   . GLY C 154 ? 3.143 4.059 1.871 -0.873 -0.302 -0.340 485 GLY EEE N   
4532 C CA  . GLY C 154 ? 3.223 4.159 1.878 -0.903 -0.368 -0.314 485 GLY EEE CA  
4533 C C   . GLY C 154 ? 3.106 4.067 1.814 -0.864 -0.427 -0.244 485 GLY EEE C   
4534 O O   . GLY C 154 ? 3.096 4.050 1.877 -0.817 -0.409 -0.216 485 GLY EEE O   
4535 N N   . PHE C 155 ? 3.112 4.101 1.790 -0.881 -0.496 -0.218 486 PHE EEE N   
4536 C CA  . PHE C 155 ? 3.036 4.061 1.793 -0.841 -0.556 -0.159 486 PHE EEE CA  
4537 C C   . PHE C 155 ? 2.937 3.996 1.847 -0.804 -0.536 -0.174 486 PHE EEE C   
4538 O O   . PHE C 155 ? 2.818 3.895 1.761 -0.825 -0.523 -0.222 486 PHE EEE O   
4539 C CB  . PHE C 155 ? 3.150 4.206 1.860 -0.869 -0.636 -0.140 486 PHE EEE CB  
4540 C CG  . PHE C 155 ? 3.265 4.283 1.816 -0.905 -0.669 -0.114 486 PHE EEE CG  
4541 C CD1 . PHE C 155 ? 3.271 4.242 1.759 -0.892 -0.653 -0.075 486 PHE EEE CD1 
4542 C CD2 . PHE C 155 ? 3.384 4.413 1.845 -0.955 -0.717 -0.127 486 PHE EEE CD2 
4543 C CE1 . PHE C 155 ? 3.351 4.280 1.683 -0.930 -0.682 -0.049 486 PHE EEE CE1 
4544 C CE2 . PHE C 155 ? 3.539 4.527 1.840 -0.992 -0.749 -0.102 486 PHE EEE CE2 
4545 C CZ  . PHE C 155 ? 3.545 4.481 1.780 -0.980 -0.730 -0.062 486 PHE EEE CZ  
4546 N N   . ASN C 156 ? 3.039 4.100 2.032 -0.752 -0.528 -0.137 487 ASN EEE N   
4547 C CA  . ASN C 156 ? 2.967 4.052 2.099 -0.712 -0.506 -0.142 487 ASN EEE CA  
4548 C C   . ASN C 156 ? 2.866 3.922 2.019 -0.714 -0.437 -0.194 487 ASN EEE C   
4549 O O   . ASN C 156 ? 2.705 3.776 1.957 -0.692 -0.419 -0.205 487 ASN EEE O   
4550 C CB  . ASN C 156 ? 3.001 4.146 2.208 -0.718 -0.553 -0.143 487 ASN EEE CB  
4551 C CG  . ASN C 156 ? 3.025 4.203 2.238 -0.704 -0.624 -0.090 487 ASN EEE CG  
4552 O OD1 . ASN C 156 ? 2.989 4.173 2.266 -0.659 -0.629 -0.050 487 ASN EEE OD1 
4553 N ND2 . ASN C 156 ? 2.928 4.124 2.074 -0.741 -0.679 -0.089 487 ASN EEE ND2 
4554 N N   . CYS C 157 ? 3.004 4.017 2.069 -0.738 -0.397 -0.222 488 CYS EEE N   
4555 C CA  . CYS C 157 ? 3.044 4.027 2.132 -0.737 -0.333 -0.273 488 CYS EEE CA  
4556 C C   . CYS C 157 ? 3.058 4.000 2.103 -0.724 -0.294 -0.265 488 CYS EEE C   
4557 O O   . CYS C 157 ? 3.166 4.085 2.109 -0.760 -0.280 -0.282 488 CYS EEE O   
4558 C CB  . CYS C 157 ? 3.172 4.149 2.206 -0.787 -0.318 -0.334 488 CYS EEE CB  
4559 S SG  . CYS C 157 ? 3.184 4.194 2.305 -0.798 -0.334 -0.366 488 CYS EEE SG  
4560 N N   . TYR C 158 ? 2.856 3.788 1.973 -0.677 -0.275 -0.242 489 TYR EEE N   
4561 C CA  . TYR C 158 ? 2.690 3.589 1.772 -0.660 -0.253 -0.218 489 TYR EEE CA  
4562 C C   . TYR C 158 ? 2.624 3.495 1.747 -0.644 -0.194 -0.256 489 TYR EEE C   
4563 O O   . TYR C 158 ? 2.539 3.413 1.737 -0.630 -0.178 -0.284 489 TYR EEE O   
4564 C CB  . TYR C 158 ? 2.575 3.485 1.701 -0.619 -0.286 -0.156 489 TYR EEE CB  
4565 C CG  . TYR C 158 ? 2.589 3.531 1.695 -0.627 -0.349 -0.118 489 TYR EEE CG  
4566 C CD1 . TYR C 158 ? 2.751 3.682 1.746 -0.663 -0.377 -0.103 489 TYR EEE CD1 
4567 C CD2 . TYR C 158 ? 2.501 3.483 1.700 -0.600 -0.383 -0.096 489 TYR EEE CD2 
4568 C CE1 . TYR C 158 ? 2.833 3.791 1.811 -0.668 -0.443 -0.066 489 TYR EEE CE1 
4569 C CE2 . TYR C 158 ? 2.506 3.523 1.700 -0.605 -0.444 -0.063 489 TYR EEE CE2 
4570 C CZ  . TYR C 158 ? 2.713 3.716 1.796 -0.638 -0.478 -0.047 489 TYR EEE CZ  
4571 O OH  . TYR C 158 ? 2.858 3.893 1.936 -0.642 -0.545 -0.013 489 TYR EEE OH  
4572 N N   . PHE C 159 ? 2.704 3.545 1.779 -0.646 -0.164 -0.255 490 PHE EEE N   
4573 C CA  . PHE C 159 ? 2.671 3.488 1.798 -0.620 -0.116 -0.277 490 PHE EEE CA  
4574 C C   . PHE C 159 ? 2.498 3.317 1.708 -0.567 -0.130 -0.236 490 PHE EEE C   
4575 O O   . PHE C 159 ? 2.455 3.279 1.650 -0.553 -0.161 -0.185 490 PHE EEE O   
4576 C CB  . PHE C 159 ? 2.663 3.452 1.721 -0.639 -0.081 -0.287 490 PHE EEE CB  
4577 C CG  . PHE C 159 ? 2.622 3.393 1.736 -0.624 -0.030 -0.333 490 PHE EEE CG  
4578 C CD1 . PHE C 159 ? 2.569 3.342 1.707 -0.640 -0.004 -0.394 490 PHE EEE CD1 
4579 C CD2 . PHE C 159 ? 2.644 3.398 1.798 -0.591 -0.013 -0.315 490 PHE EEE CD2 
4580 C CE1 . PHE C 159 ? 2.570 3.328 1.771 -0.622 0.037  -0.436 490 PHE EEE CE1 
4581 C CE2 . PHE C 159 ? 2.603 3.345 1.817 -0.575 0.027  -0.357 490 PHE EEE CE2 
4582 C CZ  . PHE C 159 ? 2.670 3.414 1.909 -0.590 0.051  -0.417 490 PHE EEE CZ  
4583 N N   . PRO C 160 ? 2.307 3.119 1.601 -0.537 -0.110 -0.256 491 PRO EEE N   
4584 C CA  . PRO C 160 ? 2.206 3.019 1.572 -0.491 -0.121 -0.220 491 PRO EEE CA  
4585 C C   . PRO C 160 ? 2.089 2.879 1.456 -0.462 -0.110 -0.191 491 PRO EEE C   
4586 O O   . PRO C 160 ? 1.959 2.754 1.370 -0.428 -0.126 -0.155 491 PRO EEE O   
4587 C CB  . PRO C 160 ? 2.155 2.956 1.590 -0.476 -0.099 -0.256 491 PRO EEE CB  
4588 C CG  . PRO C 160 ? 2.148 2.931 1.554 -0.503 -0.065 -0.311 491 PRO EEE CG  
4589 C CD  . PRO C 160 ? 2.216 3.016 1.537 -0.548 -0.077 -0.314 491 PRO EEE CD  
4590 N N   . LEU C 161 ? 2.092 2.860 1.414 -0.477 -0.082 -0.208 492 LEU EEE N   
4591 C CA  . LEU C 161 ? 2.126 2.870 1.450 -0.454 -0.068 -0.185 492 LEU EEE CA  
4592 C C   . LEU C 161 ? 2.204 2.942 1.447 -0.475 -0.084 -0.148 492 LEU EEE C   
4593 O O   . LEU C 161 ? 2.424 3.170 1.598 -0.514 -0.094 -0.155 492 LEU EEE O   
4594 C CB  . LEU C 161 ? 2.152 2.876 1.490 -0.458 -0.022 -0.234 492 LEU EEE CB  
4595 C CG  . LEU C 161 ? 2.154 2.876 1.564 -0.442 -0.009 -0.273 492 LEU EEE CG  
4596 C CD1 . LEU C 161 ? 2.141 2.845 1.575 -0.441 0.031  -0.320 492 LEU EEE CD1 
4597 C CD2 . LEU C 161 ? 2.201 2.920 1.675 -0.398 -0.027 -0.243 492 LEU EEE CD2 
4598 N N   . GLN C 162 ? 2.149 2.867 1.395 -0.451 -0.087 -0.112 493 GLN EEE N   
4599 C CA  . GLN C 162 ? 2.180 2.880 1.349 -0.468 -0.103 -0.072 493 GLN EEE CA  
4600 C C   . GLN C 162 ? 2.198 2.865 1.377 -0.451 -0.076 -0.064 493 GLN EEE C   
4601 O O   . GLN C 162 ? 2.469 3.133 1.725 -0.411 -0.068 -0.066 493 GLN EEE O   
4602 C CB  . GLN C 162 ? 2.149 2.865 1.324 -0.450 -0.156 -0.020 493 GLN EEE CB  
4603 C CG  . GLN C 162 ? 2.260 2.948 1.369 -0.455 -0.180 0.030  493 GLN EEE CG  
4604 C CD  . GLN C 162 ? 2.440 3.113 1.433 -0.508 -0.186 0.032  493 GLN EEE CD  
4605 O OE1 . GLN C 162 ? 2.478 3.173 1.433 -0.534 -0.211 0.026  493 GLN EEE OE1 
4606 N NE2 . GLN C 162 ? 2.459 3.091 1.386 -0.527 -0.165 0.043  493 GLN EEE NE2 
4607 N N   . SER C 163 ? 2.223 2.863 1.323 -0.483 -0.062 -0.056 494 SER EEE N   
4608 C CA  . SER C 163 ? 2.232 2.838 1.332 -0.473 -0.041 -0.040 494 SER EEE CA  
4609 C C   . SER C 163 ? 2.293 2.882 1.405 -0.439 -0.080 0.020  494 SER EEE C   
4610 O O   . SER C 163 ? 2.178 2.767 1.240 -0.448 -0.121 0.059  494 SER EEE O   
4611 C CB  . SER C 163 ? 2.249 2.829 1.256 -0.522 -0.014 -0.048 494 SER EEE CB  
4612 O OG  . SER C 163 ? 2.225 2.819 1.240 -0.547 0.032  -0.110 494 SER EEE OG  
4613 N N   . TYR C 164 ? 2.393 2.969 1.571 -0.400 -0.069 0.024  495 TYR EEE N   
4614 C CA  . TYR C 164 ? 2.507 3.051 1.685 -0.376 -0.089 0.073  495 TYR EEE CA  
4615 C C   . TYR C 164 ? 2.591 3.096 1.678 -0.416 -0.077 0.089  495 TYR EEE C   
4616 O O   . TYR C 164 ? 2.625 3.128 1.677 -0.453 -0.037 0.051  495 TYR EEE O   
4617 C CB  . TYR C 164 ? 2.530 3.063 1.786 -0.337 -0.069 0.062  495 TYR EEE CB  
4618 C CG  . TYR C 164 ? 2.513 3.072 1.853 -0.294 -0.081 0.056  495 TYR EEE CG  
4619 C CD1 . TYR C 164 ? 2.477 3.047 1.844 -0.265 -0.119 0.094  495 TYR EEE CD1 
4620 C CD2 . TYR C 164 ? 2.525 3.096 1.918 -0.283 -0.055 0.013  495 TYR EEE CD2 
4621 C CE1 . TYR C 164 ? 2.406 2.999 1.847 -0.230 -0.124 0.088  495 TYR EEE CE1 
4622 C CE2 . TYR C 164 ? 2.498 3.085 1.957 -0.248 -0.065 0.010  495 TYR EEE CE2 
4623 C CZ  . TYR C 164 ? 2.494 3.093 1.975 -0.223 -0.096 0.047  495 TYR EEE CZ  
4624 O OH  . TYR C 164 ? 2.622 3.236 2.164 -0.192 -0.100 0.042  495 TYR EEE OH  
4625 N N   . GLY C 165 ? 2.492 2.964 1.545 -0.407 -0.108 0.143  496 GLY EEE N   
4626 C CA  . GLY C 165 ? 2.508 2.931 1.470 -0.444 -0.100 0.168  496 GLY EEE CA  
4627 C C   . GLY C 165 ? 2.469 2.849 1.461 -0.416 -0.097 0.194  496 GLY EEE C   
4628 O O   . GLY C 165 ? 2.425 2.785 1.422 -0.389 -0.139 0.243  496 GLY EEE O   
4629 N N   . PHE C 166 ? 2.500 2.867 1.516 -0.423 -0.050 0.162  497 PHE EEE N   
4630 C CA  . PHE C 166 ? 2.518 2.849 1.576 -0.396 -0.043 0.177  497 PHE EEE CA  
4631 C C   . PHE C 166 ? 2.475 2.749 1.450 -0.436 -0.026 0.200  497 PHE EEE C   
4632 O O   . PHE C 166 ? 2.353 2.626 1.298 -0.478 0.019  0.165  497 PHE EEE O   
4633 C CB  . PHE C 166 ? 2.517 2.871 1.663 -0.375 -0.007 0.126  497 PHE EEE CB  
4634 C CG  . PHE C 166 ? 2.422 2.820 1.647 -0.333 -0.023 0.109  497 PHE EEE CG  
4635 C CD1 . PHE C 166 ? 2.326 2.725 1.584 -0.292 -0.063 0.146  497 PHE EEE CD1 
4636 C CD2 . PHE C 166 ? 2.336 2.770 1.602 -0.335 0.001  0.057  497 PHE EEE CD2 
4637 C CE1 . PHE C 166 ? 2.244 2.681 1.570 -0.258 -0.074 0.130  497 PHE EEE CE1 
4638 C CE2 . PHE C 166 ? 2.268 2.735 1.599 -0.300 -0.014 0.046  497 PHE EEE CE2 
4639 C CZ  . PHE C 166 ? 2.230 2.698 1.589 -0.263 -0.049 0.082  497 PHE EEE CZ  
4640 N N   . GLN C 167 ? 2.498 2.726 1.440 -0.425 -0.063 0.257  498 GLN EEE N   
4641 C CA  . GLN C 167 ? 2.633 2.794 1.498 -0.458 -0.054 0.290  498 GLN EEE CA  
4642 C C   . GLN C 167 ? 2.594 2.717 1.519 -0.417 -0.064 0.312  498 GLN EEE C   
4643 O O   . GLN C 167 ? 2.532 2.669 1.526 -0.364 -0.097 0.327  498 GLN EEE O   
4644 C CB  . GLN C 167 ? 2.748 2.871 1.512 -0.477 -0.101 0.348  498 GLN EEE CB  
4645 C CG  . GLN C 167 ? 2.818 2.958 1.487 -0.530 -0.097 0.337  498 GLN EEE CG  
4646 C CD  . GLN C 167 ? 2.986 3.075 1.553 -0.545 -0.150 0.402  498 GLN EEE CD  
4647 O OE1 . GLN C 167 ? 3.040 3.155 1.611 -0.526 -0.202 0.423  498 GLN EEE OE1 
4648 N NE2 . GLN C 167 ? 3.187 3.202 1.669 -0.579 -0.142 0.436  498 GLN EEE NE2 
4649 N N   . PRO C 168 ? 2.673 2.745 1.572 -0.441 -0.033 0.315  499 PRO EEE N   
4650 C CA  . PRO C 168 ? 2.756 2.788 1.711 -0.406 -0.038 0.332  499 PRO EEE CA  
4651 C C   . PRO C 168 ? 2.783 2.773 1.732 -0.370 -0.096 0.393  499 PRO EEE C   
4652 O O   . PRO C 168 ? 2.787 2.766 1.812 -0.324 -0.106 0.397  499 PRO EEE O   
4653 C CB  . PRO C 168 ? 2.874 2.854 1.775 -0.456 0.005  0.329  499 PRO EEE CB  
4654 C CG  . PRO C 168 ? 2.903 2.878 1.691 -0.517 0.018  0.334  499 PRO EEE CG  
4655 C CD  . PRO C 168 ? 2.771 2.821 1.585 -0.507 0.012  0.300  499 PRO EEE CD  
4656 N N   . THR C 169 ? 2.823 2.792 1.688 -0.389 -0.133 0.437  500 THR EEE N   
4657 C CA  . THR C 169 ? 2.869 2.794 1.727 -0.357 -0.194 0.499  500 THR EEE CA  
4658 C C   . THR C 169 ? 2.781 2.770 1.721 -0.304 -0.233 0.495  500 THR EEE C   
4659 O O   . THR C 169 ? 2.610 2.578 1.585 -0.263 -0.279 0.534  500 THR EEE O   
4660 C CB  . THR C 169 ? 2.957 2.820 1.683 -0.402 -0.222 0.552  500 THR EEE CB  
4661 O OG1 . THR C 169 ? 2.936 2.837 1.595 -0.434 -0.234 0.548  500 THR EEE OG1 
4662 C CG2 . THR C 169 ? 2.987 2.783 1.636 -0.455 -0.179 0.556  500 THR EEE CG2 
4663 N N   . ASN C 170 ? 2.822 2.885 1.797 -0.306 -0.213 0.449  501 ASN EEE N   
4664 C CA  . ASN C 170 ? 2.894 3.022 1.945 -0.264 -0.244 0.441  501 ASN EEE CA  
4665 C C   . ASN C 170 ? 2.885 3.008 2.033 -0.203 -0.262 0.452  501 ASN EEE C   
4666 O O   . ASN C 170 ? 2.817 2.910 1.999 -0.191 -0.232 0.438  501 ASN EEE O   
4667 C CB  . ASN C 170 ? 2.836 3.033 1.933 -0.267 -0.208 0.382  501 ASN EEE CB  
4668 C CG  . ASN C 170 ? 2.855 3.080 1.879 -0.315 -0.202 0.366  501 ASN EEE CG  
4669 O OD1 . ASN C 170 ? 3.009 3.207 1.943 -0.346 -0.228 0.400  501 ASN EEE OD1 
4670 N ND2 . ASN C 170 ? 2.692 2.967 1.751 -0.321 -0.168 0.314  501 ASN EEE ND2 
4671 N N   . GLY C 171 ? 2.901 3.055 2.096 -0.168 -0.308 0.473  502 GLY EEE N   
4672 C CA  . GLY C 171 ? 2.747 2.919 2.050 -0.108 -0.320 0.472  502 GLY EEE CA  
4673 C C   . GLY C 171 ? 2.592 2.804 1.959 -0.095 -0.273 0.417  502 GLY EEE C   
4674 O O   . GLY C 171 ? 2.510 2.759 1.854 -0.124 -0.248 0.384  502 GLY EEE O   
4675 N N   . VAL C 172 ? 2.615 2.815 2.053 -0.054 -0.262 0.408  503 VAL EEE N   
4676 C CA  . VAL C 172 ? 2.464 2.688 1.951 -0.043 -0.218 0.359  503 VAL EEE CA  
4677 C C   . VAL C 172 ? 2.323 2.618 1.843 -0.041 -0.216 0.332  503 VAL EEE C   
4678 O O   . VAL C 172 ? 2.345 2.661 1.866 -0.055 -0.183 0.292  503 VAL EEE O   
4679 C CB  . VAL C 172 ? 2.470 2.667 2.024 0.001  -0.212 0.355  503 VAL EEE CB  
4680 C CG1 . VAL C 172 ? 2.462 2.692 2.090 0.047  -0.239 0.366  503 VAL EEE CG1 
4681 C CG2 . VAL C 172 ? 2.476 2.678 2.055 0.003  -0.169 0.308  503 VAL EEE CG2 
4682 N N   . GLY C 173 ? 2.294 2.624 1.839 -0.025 -0.253 0.353  504 GLY EEE N   
4683 C CA  . GLY C 173 ? 2.281 2.679 1.859 -0.024 -0.255 0.331  504 GLY EEE CA  
4684 C C   . GLY C 173 ? 2.339 2.756 1.857 -0.070 -0.238 0.308  504 GLY EEE C   
4685 O O   . GLY C 173 ? 2.241 2.704 1.788 -0.072 -0.223 0.276  504 GLY EEE O   
4686 N N   . TYR C 174 ? 2.522 2.901 1.957 -0.108 -0.238 0.322  505 TYR EEE N   
4687 C CA  . TYR C 174 ? 2.578 2.971 1.944 -0.158 -0.224 0.303  505 TYR EEE CA  
4688 C C   . TYR C 174 ? 2.556 2.916 1.888 -0.184 -0.178 0.276  505 TYR EEE C   
4689 O O   . TYR C 174 ? 2.606 2.970 1.878 -0.228 -0.160 0.259  505 TYR EEE O   
4690 C CB  . TYR C 174 ? 2.722 3.101 2.013 -0.184 -0.264 0.344  505 TYR EEE CB  
4691 C CG  . TYR C 174 ? 2.725 3.150 2.052 -0.166 -0.310 0.361  505 TYR EEE CG  
4692 C CD1 . TYR C 174 ? 2.639 3.059 2.017 -0.125 -0.350 0.397  505 TYR EEE CD1 
4693 C CD2 . TYR C 174 ? 2.729 3.204 2.045 -0.188 -0.312 0.338  505 TYR EEE CD2 
4694 C CE1 . TYR C 174 ? 2.607 3.076 2.030 -0.109 -0.392 0.410  505 TYR EEE CE1 
4695 C CE2 . TYR C 174 ? 2.763 3.285 2.118 -0.174 -0.355 0.352  505 TYR EEE CE2 
4696 C CZ  . TYR C 174 ? 2.697 3.219 2.108 -0.134 -0.394 0.387  505 TYR EEE CZ  
4697 O OH  . TYR C 174 ? 2.694 3.268 2.153 -0.121 -0.436 0.397  505 TYR EEE OH  
4698 N N   . GLN C 175 ? 2.447 2.778 1.821 -0.159 -0.160 0.270  506 GLN EEE N   
4699 C CA  . GLN C 175 ? 2.325 2.631 1.686 -0.180 -0.117 0.239  506 GLN EEE CA  
4700 C C   . GLN C 175 ? 2.132 2.480 1.545 -0.171 -0.091 0.189  506 GLN EEE C   
4701 O O   . GLN C 175 ? 2.168 2.549 1.633 -0.141 -0.102 0.182  506 GLN EEE O   
4702 C CB  . GLN C 175 ? 2.291 2.545 1.671 -0.159 -0.113 0.255  506 GLN EEE CB  
4703 C CG  . GLN C 175 ? 2.420 2.618 1.729 -0.184 -0.127 0.298  506 GLN EEE CG  
4704 C CD  . GLN C 175 ? 2.521 2.664 1.853 -0.162 -0.127 0.315  506 GLN EEE CD  
4705 O OE1 . GLN C 175 ? 2.563 2.704 1.949 -0.141 -0.104 0.286  506 GLN EEE OE1 
4706 N NE2 . GLN C 175 ? 2.672 2.764 1.958 -0.166 -0.155 0.364  506 GLN EEE NE2 
4707 N N   . PRO C 176 ? 2.099 2.446 1.500 -0.199 -0.055 0.152  507 PRO EEE N   
4708 C CA  . PRO C 176 ? 2.157 2.536 1.605 -0.192 -0.033 0.104  507 PRO EEE CA  
4709 C C   . PRO C 176 ? 2.261 2.628 1.774 -0.152 -0.028 0.091  507 PRO EEE C   
4710 O O   . PRO C 176 ? 2.296 2.624 1.810 -0.146 -0.023 0.102  507 PRO EEE O   
4711 C CB  . PRO C 176 ? 2.235 2.612 1.653 -0.234 0.002  0.070  507 PRO EEE CB  
4712 C CG  . PRO C 176 ? 2.285 2.615 1.655 -0.255 0.006  0.099  507 PRO EEE CG  
4713 C CD  . PRO C 176 ? 2.269 2.581 1.610 -0.241 -0.034 0.154  507 PRO EEE CD  
4714 N N   . TYR C 177 ? 2.216 2.610 1.774 -0.127 -0.030 0.071  508 TYR EEE N   
4715 C CA  . TYR C 177 ? 2.145 2.528 1.755 -0.092 -0.025 0.053  508 TYR EEE CA  
4716 C C   . TYR C 177 ? 2.094 2.497 1.728 -0.099 -0.008 0.008  508 TYR EEE C   
4717 O O   . TYR C 177 ? 1.967 2.400 1.594 -0.113 -0.009 -0.004 508 TYR EEE O   
4718 C CB  . TYR C 177 ? 1.984 2.374 1.623 -0.055 -0.046 0.077  508 TYR EEE CB  
4719 C CG  . TYR C 177 ? 1.945 2.303 1.581 -0.040 -0.059 0.113  508 TYR EEE CG  
4720 C CD1 . TYR C 177 ? 2.103 2.454 1.700 -0.057 -0.076 0.148  508 TYR EEE CD1 
4721 C CD2 . TYR C 177 ? 1.855 2.183 1.521 -0.010 -0.055 0.112  508 TYR EEE CD2 
4722 C CE1 . TYR C 177 ? 2.168 2.482 1.762 -0.042 -0.091 0.182  508 TYR EEE CE1 
4723 C CE2 . TYR C 177 ? 1.978 2.272 1.644 0.006  -0.067 0.142  508 TYR EEE CE2 
4724 C CZ  . TYR C 177 ? 2.067 2.353 1.700 -0.009 -0.086 0.178  508 TYR EEE CZ  
4725 O OH  . TYR C 177 ? 2.007 2.253 1.641 0.007  -0.101 0.210  508 TYR EEE OH  
4726 N N   . ARG C 178 ? 2.038 2.421 1.697 -0.091 0.006  -0.019 509 ARG EEE N   
4727 C CA  . ARG C 178 ? 1.898 2.293 1.593 -0.085 0.014  -0.060 509 ARG EEE CA  
4728 C C   . ARG C 178 ? 1.876 2.264 1.595 -0.047 -0.000 -0.056 509 ARG EEE C   
4729 O O   . ARG C 178 ? 1.907 2.272 1.630 -0.025 -0.007 -0.035 509 ARG EEE O   
4730 C CB  . ARG C 178 ? 1.829 2.211 1.544 -0.096 0.031  -0.092 509 ARG EEE CB  
4731 C CG  . ARG C 178 ? 1.934 2.332 1.627 -0.139 0.053  -0.107 509 ARG EEE CG  
4732 C CD  . ARG C 178 ? 2.030 2.419 1.749 -0.154 0.074  -0.140 509 ARG EEE CD  
4733 N NE  . ARG C 178 ? 2.148 2.555 1.841 -0.198 0.100  -0.155 509 ARG EEE NE  
4734 C CZ  . ARG C 178 ? 2.239 2.659 1.962 -0.221 0.127  -0.198 509 ARG EEE CZ  
4735 N NH1 . ARG C 178 ? 2.216 2.633 2.002 -0.202 0.126  -0.228 509 ARG EEE NH1 
4736 N NH2 . ARG C 178 ? 2.464 2.900 2.156 -0.264 0.154  -0.211 509 ARG EEE NH2 
4737 N N   . VAL C 179 ? 1.793 2.197 1.526 -0.043 -0.003 -0.074 510 VAL EEE N   
4738 C CA  . VAL C 179 ? 1.643 2.040 1.390 -0.014 -0.014 -0.070 510 VAL EEE CA  
4739 C C   . VAL C 179 ? 1.745 2.131 1.514 -0.008 -0.013 -0.107 510 VAL EEE C   
4740 O O   . VAL C 179 ? 1.703 2.106 1.480 -0.027 -0.008 -0.132 510 VAL EEE O   
4741 C CB  . VAL C 179 ? 1.641 2.067 1.381 -0.017 -0.021 -0.053 510 VAL EEE CB  
4742 C CG1 . VAL C 179 ? 1.646 2.065 1.397 0.007  -0.026 -0.049 510 VAL EEE CG1 
4743 C CG2 . VAL C 179 ? 1.797 2.237 1.519 -0.024 -0.027 -0.018 510 VAL EEE CG2 
4744 N N   . VAL C 180 ? 1.838 2.195 1.615 0.019  -0.021 -0.109 511 VAL EEE N   
4745 C CA  . VAL C 180 ? 1.744 2.085 1.533 0.030  -0.030 -0.135 511 VAL EEE CA  
4746 C C   . VAL C 180 ? 1.682 2.007 1.455 0.050  -0.036 -0.117 511 VAL EEE C   
4747 O O   . VAL C 180 ? 1.719 2.032 1.482 0.065  -0.034 -0.097 511 VAL EEE O   
4748 C CB  . VAL C 180 ? 1.777 2.093 1.587 0.039  -0.035 -0.160 511 VAL EEE CB  
4749 C CG1 . VAL C 180 ? 1.799 2.094 1.620 0.052  -0.051 -0.184 511 VAL EEE CG1 
4750 C CG2 . VAL C 180 ? 1.867 2.202 1.697 0.015  -0.022 -0.179 511 VAL EEE CG2 
4751 N N   . VAL C 181 ? 1.626 1.950 1.397 0.048  -0.041 -0.126 512 VAL EEE N   
4752 C CA  . VAL C 181 ? 1.682 1.986 1.433 0.062  -0.045 -0.114 512 VAL EEE CA  
4753 C C   . VAL C 181 ? 1.804 2.065 1.551 0.074  -0.061 -0.136 512 VAL EEE C   
4754 O O   . VAL C 181 ? 1.945 2.209 1.710 0.065  -0.069 -0.157 512 VAL EEE O   
4755 C CB  . VAL C 181 ? 1.694 2.025 1.443 0.047  -0.040 -0.103 512 VAL EEE CB  
4756 C CG1 . VAL C 181 ? 1.678 1.987 1.407 0.056  -0.040 -0.092 512 VAL EEE CG1 
4757 C CG2 . VAL C 181 ? 1.739 2.112 1.494 0.035  -0.032 -0.082 512 VAL EEE CG2 
4758 N N   . LEU C 182 ? 1.784 2.007 1.507 0.093  -0.067 -0.130 513 LEU EEE N   
4759 C CA  . LEU C 182 ? 1.688 1.862 1.394 0.106  -0.088 -0.145 513 LEU EEE CA  
4760 C C   . LEU C 182 ? 1.717 1.866 1.384 0.106  -0.086 -0.129 513 LEU EEE C   
4761 O O   . LEU C 182 ? 1.688 1.835 1.330 0.111  -0.071 -0.109 513 LEU EEE O   
4762 C CB  . LEU C 182 ? 1.718 1.862 1.412 0.123  -0.096 -0.150 513 LEU EEE CB  
4763 C CG  . LEU C 182 ? 1.788 1.953 1.520 0.120  -0.095 -0.165 513 LEU EEE CG  
4764 C CD1 . LEU C 182 ? 1.840 1.969 1.556 0.137  -0.104 -0.171 513 LEU EEE CD1 
4765 C CD2 . LEU C 182 ? 1.816 1.994 1.589 0.111  -0.107 -0.194 513 LEU EEE CD2 
4766 N N   . SER C 183 ? 1.836 1.965 1.500 0.101  -0.100 -0.137 514 SER EEE N   
4767 C CA  . SER C 183 ? 1.971 2.061 1.590 0.099  -0.102 -0.123 514 SER EEE CA  
4768 C C   . SER C 183 ? 2.168 2.192 1.753 0.115  -0.131 -0.132 514 SER EEE C   
4769 O O   . SER C 183 ? 2.306 2.322 1.923 0.123  -0.156 -0.155 514 SER EEE O   
4770 C CB  . SER C 183 ? 2.016 2.123 1.652 0.081  -0.099 -0.124 514 SER EEE CB  
4771 O OG  . SER C 183 ? 1.936 2.103 1.599 0.066  -0.077 -0.116 514 SER EEE OG  
4772 N N   . PHE C 184 ? 2.100 2.076 1.623 0.117  -0.129 -0.114 515 PHE EEE N   
4773 C CA  . PHE C 184 ? 2.061 1.965 1.533 0.130  -0.160 -0.118 515 PHE EEE CA  
4774 C C   . PHE C 184 ? 2.244 2.098 1.672 0.120  -0.169 -0.104 515 PHE EEE C   
4775 O O   . PHE C 184 ? 2.272 2.131 1.674 0.104  -0.141 -0.085 515 PHE EEE O   
4776 C CB  . PHE C 184 ? 1.940 1.821 1.365 0.140  -0.152 -0.111 515 PHE EEE CB  
4777 C CG  . PHE C 184 ? 1.723 1.644 1.193 0.150  -0.147 -0.124 515 PHE EEE CG  
4778 C CD1 . PHE C 184 ? 1.633 1.606 1.129 0.145  -0.114 -0.115 515 PHE EEE CD1 
4779 C CD2 . PHE C 184 ? 1.695 1.600 1.183 0.163  -0.178 -0.146 515 PHE EEE CD2 
4780 C CE1 . PHE C 184 ? 1.597 1.598 1.128 0.152  -0.110 -0.125 515 PHE EEE CE1 
4781 C CE2 . PHE C 184 ? 1.650 1.588 1.177 0.169  -0.171 -0.158 515 PHE EEE CE2 
4782 C CZ  . PHE C 184 ? 1.622 1.605 1.168 0.162  -0.136 -0.146 515 PHE EEE CZ  
4783 N N   . GLU C 185 ? 2.378 2.183 1.801 0.129  -0.209 -0.115 516 GLU EEE N   
4784 C CA  . GLU C 185 ? 2.511 2.260 1.901 0.121  -0.226 -0.105 516 GLU EEE CA  
4785 C C   . GLU C 185 ? 2.578 2.242 1.898 0.136  -0.266 -0.100 516 GLU EEE C   
4786 O O   . GLU C 185 ? 2.603 2.260 1.947 0.156  -0.299 -0.120 516 GLU EEE O   
4787 C CB  . GLU C 185 ? 2.690 2.468 2.155 0.120  -0.239 -0.126 516 GLU EEE CB  
4788 C CG  . GLU C 185 ? 2.913 2.629 2.359 0.117  -0.266 -0.122 516 GLU EEE CG  
4789 C CD  . GLU C 185 ? 3.020 2.771 2.534 0.106  -0.261 -0.140 516 GLU EEE CD  
4790 O OE1 . GLU C 185 ? 3.191 2.990 2.716 0.085  -0.224 -0.133 516 GLU EEE OE1 
4791 O OE2 . GLU C 185 ? 2.996 2.724 2.551 0.120  -0.295 -0.162 516 GLU EEE OE2 
4792 N N   . LEU C 186 ? 2.683 2.283 1.918 0.124  -0.263 -0.075 517 LEU EEE N   
4793 C CA  . LEU C 186 ? 2.735 2.242 1.883 0.133  -0.301 -0.064 517 LEU EEE CA  
4794 C C   . LEU C 186 ? 2.798 2.229 1.890 0.120  -0.318 -0.043 517 LEU EEE C   
4795 O O   . LEU C 186 ? 2.771 2.167 1.784 0.098  -0.288 -0.018 517 LEU EEE O   
4796 C CB  . LEU C 186 ? 2.775 2.269 1.848 0.129  -0.274 -0.052 517 LEU EEE CB  
4797 C CG  . LEU C 186 ? 2.844 2.257 1.832 0.141  -0.314 -0.050 517 LEU EEE CG  
4798 C CD1 . LEU C 186 ? 2.942 2.360 1.991 0.168  -0.368 -0.076 517 LEU EEE CD1 
4799 C CD2 . LEU C 186 ? 2.779 2.192 1.705 0.136  -0.281 -0.046 517 LEU EEE CD2 
4800 N N   . LEU C 187 ? 2.917 2.322 2.051 0.133  -0.363 -0.055 518 LEU EEE N   
4801 C CA  . LEU C 187 ? 3.165 2.491 2.257 0.124  -0.387 -0.037 518 LEU EEE CA  
4802 C C   . LEU C 187 ? 3.266 2.489 2.280 0.140  -0.448 -0.027 518 LEU EEE C   
4803 O O   . LEU C 187 ? 3.034 2.250 2.021 0.156  -0.467 -0.033 518 LEU EEE O   
4804 C CB  . LEU C 187 ? 3.124 2.487 2.320 0.129  -0.398 -0.060 518 LEU EEE CB  
4805 C CG  . LEU C 187 ? 2.798 2.268 2.078 0.116  -0.348 -0.077 518 LEU EEE CG  
4806 C CD1 . LEU C 187 ? 2.737 2.232 2.110 0.121  -0.364 -0.105 518 LEU EEE CD1 
4807 C CD2 . LEU C 187 ? 2.712 2.194 1.948 0.084  -0.297 -0.052 518 LEU EEE CD2 
4808 N N   . HIS C 188 ? 3.393 2.531 2.369 0.137  -0.482 -0.010 519 HIS EEE N   
4809 C CA  . HIS C 188 ? 3.722 2.742 2.600 0.146  -0.542 0.011  519 HIS EEE CA  
4810 C C   . HIS C 188 ? 3.858 2.867 2.818 0.182  -0.612 -0.016 519 HIS EEE C   
4811 O O   . HIS C 188 ? 3.966 2.880 2.889 0.192  -0.668 -0.002 519 HIS EEE O   
4812 C CB  . HIS C 188 ? 3.889 2.823 2.668 0.116  -0.528 0.049  519 HIS EEE CB  
4813 C CG  . HIS C 188 ? 3.892 2.870 2.633 0.081  -0.451 0.064  519 HIS EEE CG  
4814 N ND1 . HIS C 188 ? 4.072 3.019 2.702 0.065  -0.424 0.083  519 HIS EEE ND1 
4815 C CD2 . HIS C 188 ? 3.770 2.824 2.573 0.061  -0.394 0.059  519 HIS EEE CD2 
4816 C CE1 . HIS C 188 ? 3.972 2.977 2.607 0.038  -0.354 0.089  519 HIS EEE CE1 
4817 N NE2 . HIS C 188 ? 3.872 2.943 2.611 0.035  -0.337 0.075  519 HIS EEE NE2 
4818 N N   . ALA C 189 ? 3.846 2.949 2.913 0.201  -0.608 -0.053 520 ALA EEE N   
4819 C CA  . ALA C 189 ? 3.749 2.883 2.936 0.233  -0.655 -0.092 520 ALA EEE CA  
4820 C C   . ALA C 189 ? 3.623 2.802 2.838 0.251  -0.668 -0.115 520 ALA EEE C   
4821 O O   . ALA C 189 ? 3.560 2.761 2.719 0.238  -0.631 -0.105 520 ALA EEE O   
4822 C CB  . ALA C 189 ? 3.639 2.860 2.941 0.227  -0.616 -0.118 520 ALA EEE CB  
4823 N N   . PRO C 190 ? 3.507 2.702 2.814 0.281  -0.720 -0.149 521 PRO EEE N   
4824 C CA  . PRO C 190 ? 3.470 2.700 2.801 0.296  -0.738 -0.171 521 PRO EEE CA  
4825 C C   . PRO C 190 ? 3.115 2.443 2.480 0.280  -0.667 -0.183 521 PRO EEE C   
4826 O O   . PRO C 190 ? 2.988 2.388 2.438 0.273  -0.630 -0.201 521 PRO EEE O   
4827 C CB  . PRO C 190 ? 3.563 2.816 3.022 0.326  -0.792 -0.212 521 PRO EEE CB  
4828 C CG  . PRO C 190 ? 3.626 2.805 3.078 0.333  -0.830 -0.198 521 PRO EEE CG  
4829 C CD  . PRO C 190 ? 3.473 2.653 2.869 0.301  -0.765 -0.170 521 PRO EEE CD  
4830 N N   . ALA C 191 ? 3.015 2.337 2.304 0.273  -0.651 -0.171 522 ALA EEE N   
4831 C CA  . ALA C 191 ? 2.857 2.260 2.170 0.260  -0.590 -0.179 522 ALA EEE CA  
4832 C C   . ALA C 191 ? 2.781 2.245 2.196 0.277  -0.609 -0.219 522 ALA EEE C   
4833 O O   . ALA C 191 ? 2.945 2.382 2.333 0.289  -0.643 -0.227 522 ALA EEE O   
4834 C CB  . ALA C 191 ? 2.967 2.331 2.159 0.246  -0.566 -0.152 522 ALA EEE CB  
4835 N N   . THR C 192 ? 2.673 2.214 2.200 0.275  -0.585 -0.245 523 THR EEE N   
4836 C CA  . THR C 192 ? 2.573 2.171 2.220 0.290  -0.605 -0.289 523 THR EEE CA  
4837 C C   . THR C 192 ? 2.388 2.061 2.069 0.277  -0.555 -0.301 523 THR EEE C   
4838 O O   . THR C 192 ? 2.188 1.911 1.959 0.284  -0.562 -0.336 523 THR EEE O   
4839 C CB  . THR C 192 ? 2.521 2.144 2.263 0.295  -0.613 -0.312 523 THR EEE CB  
4840 O OG1 . THR C 192 ? 2.432 2.112 2.295 0.308  -0.629 -0.358 523 THR EEE OG1 
4841 C CG2 . THR C 192 ? 2.458 2.127 2.209 0.272  -0.551 -0.302 523 THR EEE CG2 
4842 N N   . VAL C 193 ? 2.349 2.030 1.964 0.259  -0.505 -0.274 524 VAL EEE N   
4843 C CA  . VAL C 193 ? 2.507 2.255 2.152 0.247  -0.457 -0.281 524 VAL EEE CA  
4844 C C   . VAL C 193 ? 2.697 2.409 2.254 0.247  -0.452 -0.263 524 VAL EEE C   
4845 O O   . VAL C 193 ? 2.654 2.344 2.133 0.236  -0.422 -0.233 524 VAL EEE O   
4846 C CB  . VAL C 193 ? 2.483 2.284 2.143 0.227  -0.399 -0.268 524 VAL EEE CB  
4847 C CG1 . VAL C 193 ? 2.317 2.177 2.006 0.217  -0.359 -0.273 524 VAL EEE CG1 
4848 C CG2 . VAL C 193 ? 2.506 2.338 2.242 0.224  -0.400 -0.286 524 VAL EEE CG2 
4849 N N   . CYS C 194 ? 2.964 2.674 2.541 0.258  -0.479 -0.285 525 CYS EEE N   
4850 C CA  . CYS C 194 ? 3.074 2.735 2.565 0.262  -0.490 -0.276 525 CYS EEE CA  
4851 C C   . CYS C 194 ? 2.920 2.625 2.448 0.257  -0.463 -0.293 525 CYS EEE C   
4852 O O   . CYS C 194 ? 2.748 2.508 2.375 0.257  -0.463 -0.320 525 CYS EEE O   
4853 C CB  . CYS C 194 ? 3.147 2.746 2.614 0.279  -0.561 -0.288 525 CYS EEE CB  
4854 S SG  . CYS C 194 ? 3.488 3.005 2.873 0.283  -0.596 -0.258 525 CYS EEE SG  
4855 N N   . GLY C 195 ? 2.915 2.595 2.367 0.253  -0.440 -0.278 526 GLY EEE N   
4856 C CA  . GLY C 195 ? 2.929 2.632 2.402 0.251  -0.423 -0.294 526 GLY EEE CA  
4857 C C   . GLY C 195 ? 2.949 2.627 2.437 0.262  -0.477 -0.323 526 GLY EEE C   
4858 O O   . GLY C 195 ? 3.011 2.640 2.466 0.273  -0.529 -0.325 526 GLY EEE O   
4859 N N   . PRO C 196 ? 2.852 2.556 2.384 0.260  -0.469 -0.346 527 PRO EEE N   
4860 C CA  . PRO C 196 ? 2.781 2.473 2.348 0.268  -0.521 -0.379 527 PRO EEE CA  
4861 C C   . PRO C 196 ? 2.786 2.397 2.246 0.278  -0.567 -0.374 527 PRO EEE C   
4862 O O   . PRO C 196 ? 2.836 2.428 2.316 0.289  -0.626 -0.396 527 PRO EEE O   
4863 C CB  . PRO C 196 ? 2.674 2.398 2.283 0.259  -0.492 -0.397 527 PRO EEE CB  
4864 C CG  . PRO C 196 ? 2.627 2.397 2.257 0.246  -0.428 -0.375 527 PRO EEE CG  
4865 C CD  . PRO C 196 ? 2.735 2.478 2.287 0.248  -0.414 -0.341 527 PRO EEE CD  
4866 N N   . LYS C 197 ? 2.793 2.361 2.144 0.273  -0.539 -0.346 528 LYS EEE N   
4867 C CA  . LYS C 197 ? 2.891 2.376 2.115 0.277  -0.568 -0.337 528 LYS EEE CA  
4868 C C   . LYS C 197 ? 2.793 2.234 1.942 0.276  -0.575 -0.305 528 LYS EEE C   
4869 O O   . LYS C 197 ? 2.764 2.190 1.936 0.285  -0.623 -0.305 528 LYS EEE O   
4870 C CB  . LYS C 197 ? 3.033 2.506 2.196 0.268  -0.522 -0.334 528 LYS EEE CB  
4871 C CG  . LYS C 197 ? 3.161 2.660 2.385 0.268  -0.524 -0.367 528 LYS EEE CG  
4872 C CD  . LYS C 197 ? 3.335 2.794 2.544 0.276  -0.593 -0.395 528 LYS EEE CD  
4873 C CE  . LYS C 197 ? 3.253 2.760 2.577 0.275  -0.609 -0.431 528 LYS EEE CE  
4874 N NZ  . LYS C 197 ? 3.124 2.620 2.427 0.268  -0.587 -0.449 528 LYS EEE NZ  
4875 N N   . GLN D 1   ? 3.325 4.249 2.631 -0.932 0.248  -0.474 1   GLN FFF N   
4876 C CA  . GLN D 1   ? 3.396 4.317 2.673 -0.920 0.276  -0.455 1   GLN FFF CA  
4877 C C   . GLN D 1   ? 3.492 4.412 2.730 -0.912 0.289  -0.458 1   GLN FFF C   
4878 O O   . GLN D 1   ? 3.595 4.519 2.855 -0.916 0.283  -0.465 1   GLN FFF O   
4879 C CB  . GLN D 1   ? 3.352 4.279 2.687 -0.916 0.297  -0.428 1   GLN FFF CB  
4880 C CG  . GLN D 1   ? 3.321 4.248 2.691 -0.921 0.289  -0.422 1   GLN FFF CG  
4881 C CD  . GLN D 1   ? 3.294 4.226 2.706 -0.914 0.316  -0.391 1   GLN FFF CD  
4882 O OE1 . GLN D 1   ? 3.211 4.143 2.594 -0.900 0.344  -0.375 1   GLN FFF OE1 
4883 N NE2 . GLN D 1   ? 3.259 4.195 2.741 -0.921 0.309  -0.381 1   GLN FFF NE2 
4884 N N   . VAL D 2   ? 3.509 4.421 2.691 -0.900 0.304  -0.453 2   VAL FFF N   
4885 C CA  . VAL D 2   ? 3.478 4.386 2.620 -0.888 0.318  -0.453 2   VAL FFF CA  
4886 C C   . VAL D 2   ? 3.419 4.324 2.552 -0.871 0.349  -0.428 2   VAL FFF C   
4887 O O   . VAL D 2   ? 3.407 4.310 2.541 -0.868 0.356  -0.416 2   VAL FFF O   
4888 C CB  . VAL D 2   ? 3.538 4.436 2.616 -0.889 0.301  -0.474 2   VAL FFF CB  
4889 C CG1 . VAL D 2   ? 3.462 4.364 2.551 -0.904 0.272  -0.495 2   VAL FFF CG1 
4890 C CG2 . VAL D 2   ? 3.633 4.522 2.663 -0.882 0.302  -0.472 2   VAL FFF CG2 
4891 N N   . GLN D 3   ? 3.400 4.304 2.524 -0.858 0.368  -0.419 3   GLN FFF N   
4892 C CA  . GLN D 3   ? 3.473 4.372 2.571 -0.835 0.399  -0.397 3   GLN FFF CA  
4893 C C   . GLN D 3   ? 3.479 4.361 2.497 -0.822 0.397  -0.411 3   GLN FFF C   
4894 O O   . GLN D 3   ? 3.513 4.393 2.515 -0.826 0.383  -0.428 3   GLN FFF O   
4895 C CB  . GLN D 3   ? 3.490 4.398 2.633 -0.827 0.424  -0.376 3   GLN FFF CB  
4896 C CG  . GLN D 3   ? 3.513 4.415 2.627 -0.800 0.458  -0.351 3   GLN FFF CG  
4897 C CD  . GLN D 3   ? 3.506 4.418 2.660 -0.789 0.484  -0.330 3   GLN FFF CD  
4898 O OE1 . GLN D 3   ? 3.518 4.432 2.672 -0.791 0.479  -0.340 3   GLN FFF OE1 
4899 N NE2 . GLN D 3   ? 3.528 4.448 2.718 -0.777 0.512  -0.298 3   GLN FFF NE2 
4900 N N   . LEU D 4   ? 3.457 4.328 2.428 -0.806 0.408  -0.403 4   LEU FFF N   
4901 C CA  . LEU D 4   ? 3.526 4.379 2.420 -0.788 0.406  -0.414 4   LEU FFF CA  
4902 C C   . LEU D 4   ? 3.725 4.572 2.599 -0.760 0.439  -0.391 4   LEU FFF C   
4903 O O   . LEU D 4   ? 3.761 4.611 2.652 -0.750 0.461  -0.368 4   LEU FFF O   
4904 C CB  . LEU D 4   ? 3.460 4.302 2.315 -0.790 0.392  -0.421 4   LEU FFF CB  
4905 C CG  . LEU D 4   ? 3.386 4.233 2.257 -0.815 0.362  -0.441 4   LEU FFF CG  
4906 C CD1 . LEU D 4   ? 3.418 4.251 2.234 -0.812 0.347  -0.453 4   LEU FFF CD1 
4907 C CD2 . LEU D 4   ? 3.338 4.191 2.223 -0.829 0.343  -0.460 4   LEU FFF CD2 
4908 N N   . VAL D 5   ? 3.860 4.697 2.698 -0.745 0.443  -0.397 5   VAL FFF N   
4909 C CA  . VAL D 5   ? 3.867 4.696 2.673 -0.713 0.473  -0.378 5   VAL FFF CA  
4910 C C   . VAL D 5   ? 3.925 4.729 2.647 -0.695 0.460  -0.397 5   VAL FFF C   
4911 O O   . VAL D 5   ? 3.866 4.666 2.576 -0.703 0.440  -0.418 5   VAL FFF O   
4912 C CB  . VAL D 5   ? 3.833 4.675 2.685 -0.710 0.493  -0.363 5   VAL FFF CB  
4913 C CG1 . VAL D 5   ? 3.878 4.710 2.691 -0.674 0.525  -0.343 5   VAL FFF CG1 
4914 C CG2 . VAL D 5   ? 3.776 4.641 2.715 -0.727 0.504  -0.343 5   VAL FFF CG2 
4915 N N   . GLU D 6   ? 4.085 4.872 2.754 -0.672 0.470  -0.390 6   GLU FFF N   
4916 C CA  . GLU D 6   ? 4.273 5.032 2.859 -0.651 0.456  -0.407 6   GLU FFF CA  
4917 C C   . GLU D 6   ? 4.433 5.182 2.985 -0.617 0.481  -0.395 6   GLU FFF C   
4918 O O   . GLU D 6   ? 4.604 5.366 3.189 -0.605 0.515  -0.367 6   GLU FFF O   
4919 C CB  . GLU D 6   ? 4.321 5.064 2.862 -0.639 0.453  -0.406 6   GLU FFF CB  
4920 C CG  . GLU D 6   ? 4.259 5.012 2.830 -0.668 0.432  -0.415 6   GLU FFF CG  
4921 C CD  . GLU D 6   ? 4.218 4.986 2.832 -0.672 0.453  -0.391 6   GLU FFF CD  
4922 O OE1 . GLU D 6   ? 4.240 5.024 2.903 -0.670 0.479  -0.369 6   GLU FFF OE1 
4923 O OE2 . GLU D 6   ? 4.137 4.900 2.738 -0.677 0.443  -0.394 6   GLU FFF OE2 
4924 N N   . SER D 7   ? 4.447 5.171 2.934 -0.601 0.464  -0.414 7   SER FFF N   
4925 C CA  . SER D 7   ? 4.412 5.118 2.846 -0.563 0.482  -0.408 7   SER FFF CA  
4926 C C   . SER D 7   ? 4.389 5.062 2.741 -0.545 0.455  -0.432 7   SER FFF C   
4927 O O   . SER D 7   ? 4.149 4.817 2.497 -0.566 0.423  -0.453 7   SER FFF O   
4928 C CB  . SER D 7   ? 4.392 5.109 2.856 -0.567 0.489  -0.407 7   SER FFF CB  
4929 O OG  . SER D 7   ? 4.296 5.016 2.774 -0.595 0.455  -0.435 7   SER FFF OG  
4930 N N   . GLY D 8   ? 4.471 5.121 2.761 -0.505 0.468  -0.428 8   GLY FFF N   
4931 C CA  . GLY D 8   ? 4.427 5.040 2.636 -0.483 0.441  -0.452 8   GLY FFF CA  
4932 C C   . GLY D 8   ? 4.343 4.932 2.488 -0.450 0.447  -0.446 8   GLY FFF C   
4933 O O   . GLY D 8   ? 4.262 4.817 2.337 -0.427 0.423  -0.466 8   GLY FFF O   
4934 N N   . GLY D 9   ? 4.285 4.888 2.452 -0.446 0.475  -0.421 9   GLY FFF N   
4935 C CA  . GLY D 9   ? 4.322 4.903 2.429 -0.411 0.487  -0.410 9   GLY FFF CA  
4936 C C   . GLY D 9   ? 4.377 4.939 2.425 -0.361 0.514  -0.397 9   GLY FFF C   
4937 O O   . GLY D 9   ? 4.408 4.984 2.483 -0.357 0.535  -0.384 9   GLY FFF O   
4938 N N   . GLY D 10  ? 4.431 4.961 2.400 -0.323 0.512  -0.399 10  GLY FFF N   
4939 C CA  . GLY D 10  ? 4.520 5.026 2.418 -0.267 0.536  -0.387 10  GLY FFF CA  
4940 C C   . GLY D 10  ? 4.561 5.026 2.367 -0.231 0.517  -0.402 10  GLY FFF C   
4941 O O   . GLY D 10  ? 4.701 5.161 2.507 -0.251 0.492  -0.415 10  GLY FFF O   
4942 N N   . LEU D 11  ? 4.491 4.925 2.219 -0.179 0.527  -0.399 11  LEU FFF N   
4943 C CA  . LEU D 11  ? 4.539 4.927 2.168 -0.138 0.505  -0.417 11  LEU FFF CA  
4944 C C   . LEU D 11  ? 4.627 4.985 2.221 -0.146 0.452  -0.459 11  LEU FFF C   
4945 O O   . LEU D 11  ? 4.645 5.003 2.241 -0.144 0.448  -0.466 11  LEU FFF O   
4946 C CB  . LEU D 11  ? 4.560 4.929 2.121 -0.075 0.542  -0.394 11  LEU FFF CB  
4947 C CG  . LEU D 11  ? 4.551 4.871 2.006 -0.025 0.526  -0.408 11  LEU FFF CG  
4948 C CD1 . LEU D 11  ? 4.526 4.851 1.986 -0.033 0.529  -0.399 11  LEU FFF CD1 
4949 C CD2 . LEU D 11  ? 4.595 4.896 1.980 0.039  0.561  -0.387 11  LEU FFF CD2 
4950 N N   . MET D 12  ? 4.752 5.087 2.316 -0.153 0.411  -0.484 12  MET FFF N   
4951 C CA  . MET D 12  ? 4.903 5.204 2.429 -0.154 0.357  -0.523 12  MET FFF CA  
4952 C C   . MET D 12  ? 5.056 5.313 2.502 -0.123 0.328  -0.541 12  MET FFF C   
4953 O O   . MET D 12  ? 5.167 5.428 2.611 -0.121 0.341  -0.527 12  MET FFF O   
4954 C CB  . MET D 12  ? 4.842 5.167 2.443 -0.215 0.324  -0.542 12  MET FFF CB  
4955 C CG  . MET D 12  ? 4.824 5.167 2.469 -0.235 0.326  -0.545 12  MET FFF CG  
4956 S SD  . MET D 12  ? 4.855 5.157 2.421 -0.187 0.312  -0.562 12  MET FFF SD  
4957 C CE  . MET D 12  ? 4.848 5.117 2.394 -0.204 0.242  -0.606 12  MET FFF CE  
4958 N N   . GLN D 13  ? 5.095 5.309 2.477 -0.098 0.289  -0.570 13  GLN FFF N   
4959 C CA  . GLN D 13  ? 5.113 5.278 2.413 -0.064 0.253  -0.592 13  GLN FFF CA  
4960 C C   . GLN D 13  ? 5.084 5.251 2.424 -0.109 0.207  -0.614 13  GLN FFF C   
4961 O O   . GLN D 13  ? 4.994 5.184 2.401 -0.155 0.189  -0.624 13  GLN FFF O   
4962 C CB  . GLN D 13  ? 5.154 5.275 2.379 -0.021 0.229  -0.613 13  GLN FFF CB  
4963 C CG  . GLN D 13  ? 5.173 5.285 2.342 0.035  0.275  -0.590 13  GLN FFF CG  
4964 C CD  . GLN D 13  ? 5.158 5.249 2.291 0.060  0.264  -0.604 13  GLN FFF CD  
4965 O OE1 . GLN D 13  ? 5.114 5.180 2.237 0.051  0.213  -0.637 13  GLN FFF OE1 
4966 N NE2 . GLN D 13  ? 5.176 5.276 2.291 0.093  0.311  -0.578 13  GLN FFF NE2 
4967 N N   . ALA D 14  ? 5.101 5.245 2.403 -0.096 0.191  -0.620 14  ALA FFF N   
4968 C CA  . ALA D 14  ? 5.042 5.179 2.367 -0.129 0.144  -0.642 14  ALA FFF CA  
4969 C C   . ALA D 14  ? 5.124 5.234 2.440 -0.135 0.091  -0.676 14  ALA FFF C   
4970 O O   . ALA D 14  ? 5.258 5.329 2.505 -0.091 0.079  -0.688 14  ALA FFF O   
4971 C CB  . ALA D 14  ? 4.992 5.099 2.258 -0.100 0.135  -0.644 14  ALA FFF CB  
4972 N N   . GLY D 15  ? 5.105 5.236 2.492 -0.186 0.062  -0.688 15  GLY FFF N   
4973 C CA  . GLY D 15  ? 5.070 5.181 2.465 -0.199 0.012  -0.717 15  GLY FFF CA  
4974 C C   . GLY D 15  ? 4.977 5.117 2.424 -0.222 0.026  -0.713 15  GLY FFF C   
4975 O O   . GLY D 15  ? 4.992 5.132 2.476 -0.250 -0.011 -0.732 15  GLY FFF O   
4976 N N   . GLY D 16  ? 4.862 5.027 2.315 -0.212 0.077  -0.688 16  GLY FFF N   
4977 C CA  . GLY D 16  ? 4.667 4.862 2.171 -0.234 0.095  -0.681 16  GLY FFF CA  
4978 C C   . GLY D 16  ? 4.377 4.621 1.977 -0.293 0.103  -0.672 16  GLY FFF C   
4979 O O   . GLY D 16  ? 4.168 4.421 1.792 -0.315 0.091  -0.672 16  GLY FFF O   
4980 N N   . SER D 17  ? 4.254 4.529 1.907 -0.315 0.121  -0.664 17  SER FFF N   
4981 C CA  . SER D 17  ? 4.239 4.561 1.982 -0.369 0.129  -0.655 17  SER FFF CA  
4982 C C   . SER D 17  ? 4.268 4.626 2.049 -0.373 0.180  -0.629 17  SER FFF C   
4983 O O   . SER D 17  ? 4.249 4.595 1.992 -0.340 0.200  -0.623 17  SER FFF O   
4984 C CB  . SER D 17  ? 4.211 4.534 1.990 -0.398 0.090  -0.677 17  SER FFF CB  
4985 O OG  . SER D 17  ? 4.132 4.492 1.988 -0.447 0.088  -0.672 17  SER FFF OG  
4986 N N   . LEU D 18  ? 4.319 4.717 2.170 -0.411 0.198  -0.613 18  LEU FFF N   
4987 C CA  . LEU D 18  ? 4.258 4.693 2.159 -0.421 0.245  -0.586 18  LEU FFF CA  
4988 C C   . LEU D 18  ? 4.085 4.559 2.071 -0.473 0.242  -0.584 18  LEU FFF C   
4989 O O   . LEU D 18  ? 3.982 4.461 1.985 -0.494 0.223  -0.589 18  LEU FFF O   
4990 C CB  . LEU D 18  ? 4.294 4.729 2.169 -0.395 0.279  -0.562 18  LEU FFF CB  
4991 C CG  . LEU D 18  ? 4.262 4.731 2.184 -0.399 0.328  -0.531 18  LEU FFF CG  
4992 C CD1 . LEU D 18  ? 4.259 4.730 2.181 -0.384 0.344  -0.527 18  LEU FFF CD1 
4993 C CD2 . LEU D 18  ? 4.293 4.757 2.184 -0.368 0.360  -0.508 18  LEU FFF CD2 
4994 N N   A ARG D 19  ? 4.021 4.523 2.058 -0.490 0.260  -0.575 19  ARG FFF N   
4995 N N   B ARG D 19  ? 3.998 4.500 2.035 -0.491 0.258  -0.576 19  ARG FFF N   
4996 C CA  A ARG D 19  ? 3.929 4.467 2.045 -0.536 0.255  -0.575 19  ARG FFF CA  
4997 C CA  B ARG D 19  ? 3.894 4.431 2.010 -0.537 0.255  -0.575 19  ARG FFF CA  
4998 C C   A ARG D 19  ? 3.922 4.492 2.088 -0.545 0.296  -0.548 19  ARG FFF C   
4999 C C   B ARG D 19  ? 3.903 4.472 2.068 -0.545 0.296  -0.548 19  ARG FFF C   
5000 O O   A ARG D 19  ? 3.932 4.509 2.104 -0.532 0.322  -0.535 19  ARG FFF O   
5001 O O   B ARG D 19  ? 3.920 4.496 2.090 -0.531 0.322  -0.536 19  ARG FFF O   
5002 C CB  A ARG D 19  ? 3.865 4.406 2.001 -0.551 0.236  -0.591 19  ARG FFF CB  
5003 C CB  B ARG D 19  ? 3.797 4.340 1.939 -0.555 0.235  -0.591 19  ARG FFF CB  
5004 C CG  A ARG D 19  ? 3.748 4.321 1.957 -0.595 0.226  -0.593 19  ARG FFF CG  
5005 C CG  B ARG D 19  ? 3.661 4.241 1.881 -0.598 0.235  -0.588 19  ARG FFF CG  
5006 C CD  A ARG D 19  ? 3.711 4.286 1.935 -0.604 0.212  -0.606 19  ARG FFF CD  
5007 C CD  B ARG D 19  ? 3.589 4.174 1.833 -0.617 0.210  -0.605 19  ARG FFF CD  
5008 N NE  A ARG D 19  ? 3.643 4.241 1.923 -0.642 0.193  -0.615 19  ARG FFF NE  
5009 N NE  B ARG D 19  ? 3.558 4.123 1.782 -0.624 0.169  -0.626 19  ARG FFF NE  
5010 C CZ  A ARG D 19  ? 3.618 4.206 1.897 -0.656 0.156  -0.632 19  ARG FFF CZ  
5011 C CZ  B ARG D 19  ? 3.496 4.071 1.755 -0.650 0.144  -0.639 19  ARG FFF CZ  
5012 N NH1 A ARG D 19  ? 3.645 4.200 1.870 -0.636 0.133  -0.645 19  ARG FFF NH1 
5013 N NH1 B ARG D 19  ? 3.456 4.058 1.766 -0.671 0.154  -0.635 19  ARG FFF NH1 
5014 N NH2 A ARG D 19  ? 3.570 4.181 1.901 -0.688 0.143  -0.637 19  ARG FFF NH2 
5015 N NH2 B ARG D 19  ? 3.475 4.032 1.720 -0.654 0.107  -0.655 19  ARG FFF NH2 
5016 N N   . LEU D 20  ? 3.910 4.499 2.114 -0.567 0.301  -0.539 20  LEU FFF N   
5017 C CA  . LEU D 20  ? 3.906 4.528 2.171 -0.582 0.334  -0.515 20  LEU FFF CA  
5018 C C   . LEU D 20  ? 3.957 4.606 2.289 -0.619 0.323  -0.521 20  LEU FFF C   
5019 O O   . LEU D 20  ? 4.011 4.657 2.347 -0.639 0.290  -0.542 20  LEU FFF O   
5020 C CB  . LEU D 20  ? 3.866 4.494 2.139 -0.588 0.339  -0.504 20  LEU FFF CB  
5021 C CG  . LEU D 20  ? 3.939 4.537 2.142 -0.554 0.342  -0.502 20  LEU FFF CG  
5022 C CD1 . LEU D 20  ? 3.870 4.477 2.089 -0.565 0.346  -0.492 20  LEU FFF CD1 
5023 C CD2 . LEU D 20  ? 4.038 4.627 2.207 -0.515 0.376  -0.483 20  LEU FFF CD2 
5024 N N   . SER D 21  ? 3.927 4.601 2.310 -0.627 0.350  -0.504 21  SER FFF N   
5025 C CA  . SER D 21  ? 3.734 4.436 2.187 -0.662 0.344  -0.507 21  SER FFF CA  
5026 C C   . SER D 21  ? 3.683 4.409 2.191 -0.678 0.362  -0.488 21  SER FFF C   
5027 O O   . SER D 21  ? 3.784 4.509 2.285 -0.659 0.389  -0.467 21  SER FFF O   
5028 C CB  . SER D 21  ? 3.679 4.390 2.154 -0.660 0.356  -0.504 21  SER FFF CB  
5029 O OG  . SER D 21  ? 3.699 4.389 2.129 -0.648 0.338  -0.522 21  SER FFF OG  
5030 N N   . CYS D 22  ? 3.627 4.371 2.185 -0.710 0.346  -0.495 22  CYS FFF N   
5031 C CA  A CYS D 22  ? 3.587 4.356 2.210 -0.729 0.360  -0.480 22  CYS FFF CA  
5032 C CA  B CYS D 22  ? 3.579 4.348 2.202 -0.728 0.362  -0.479 22  CYS FFF CA  
5033 C C   . CYS D 22  ? 3.533 4.321 2.210 -0.753 0.350  -0.488 22  CYS FFF C   
5034 O O   . CYS D 22  ? 3.441 4.230 2.118 -0.771 0.322  -0.508 22  CYS FFF O   
5035 C CB  A CYS D 22  ? 3.550 4.320 2.173 -0.741 0.346  -0.483 22  CYS FFF CB  
5036 C CB  B CYS D 22  ? 3.547 4.320 2.178 -0.739 0.353  -0.478 22  CYS FFF CB  
5037 S SG  A CYS D 22  ? 3.451 4.247 2.148 -0.762 0.358  -0.467 22  CYS FFF SG  
5038 S SG  B CYS D 22  ? 3.449 4.249 2.159 -0.757 0.371  -0.458 22  CYS FFF SG  
5039 N N   . ALA D 23  ? 3.515 4.318 2.235 -0.752 0.373  -0.472 23  ALA FFF N   
5040 C CA  . ALA D 23  ? 3.465 4.287 2.241 -0.772 0.367  -0.477 23  ALA FFF CA  
5041 C C   . ALA D 23  ? 3.486 4.326 2.321 -0.793 0.365  -0.470 23  ALA FFF C   
5042 O O   . ALA D 23  ? 3.437 4.281 2.290 -0.786 0.385  -0.450 23  ALA FFF O   
5043 C CB  . ALA D 23  ? 3.474 4.300 2.266 -0.759 0.391  -0.462 23  ALA FFF CB  
5044 N N   . VAL D 24  ? 3.505 4.353 2.365 -0.816 0.340  -0.486 24  VAL FFF N   
5045 C CA  . VAL D 24  ? 3.349 4.212 2.261 -0.836 0.332  -0.485 24  VAL FFF CA  
5046 C C   . VAL D 24  ? 3.260 4.139 2.231 -0.847 0.333  -0.483 24  VAL FFF C   
5047 O O   . VAL D 24  ? 3.115 3.993 2.079 -0.851 0.322  -0.497 24  VAL FFF O   
5048 C CB  . VAL D 24  ? 3.334 4.195 2.229 -0.851 0.303  -0.504 24  VAL FFF CB  
5049 C CG1 . VAL D 24  ? 3.335 4.208 2.275 -0.866 0.296  -0.501 24  VAL FFF CG1 
5050 C CG2 . VAL D 24  ? 3.407 4.251 2.241 -0.839 0.299  -0.508 24  VAL FFF CG2 
5051 N N   . SER D 25  ? 3.288 4.178 2.314 -0.851 0.346  -0.467 25  SER FFF N   
5052 C CA  . SER D 25  ? 3.246 4.150 2.337 -0.862 0.346  -0.463 25  SER FFF CA  
5053 C C   . SER D 25  ? 3.272 4.184 2.413 -0.878 0.332  -0.463 25  SER FFF C   
5054 O O   . SER D 25  ? 3.274 4.184 2.407 -0.877 0.333  -0.457 25  SER FFF O   
5055 C CB  . SER D 25  ? 3.221 4.129 2.338 -0.848 0.376  -0.439 25  SER FFF CB  
5056 O OG  . SER D 25  ? 3.130 4.045 2.286 -0.845 0.392  -0.417 25  SER FFF OG  
5057 N N   . GLY D 26  ? 3.348 4.269 2.537 -0.890 0.319  -0.470 26  GLY FFF N   
5058 C CA  . GLY D 26  ? 3.431 4.360 2.671 -0.904 0.302  -0.473 26  GLY FFF CA  
5059 C C   . GLY D 26  ? 3.463 4.389 2.681 -0.916 0.272  -0.498 26  GLY FFF C   
5060 O O   . GLY D 26  ? 3.525 4.452 2.731 -0.918 0.261  -0.513 26  GLY FFF O   
5061 N N   . ARG D 27  ? 3.460 4.384 2.673 -0.921 0.259  -0.502 27  ARG FFF N   
5062 C CA  . ARG D 27  ? 3.377 4.301 2.579 -0.930 0.231  -0.523 27  ARG FFF CA  
5063 C C   . ARG D 27  ? 3.347 4.264 2.483 -0.927 0.227  -0.533 27  ARG FFF C   
5064 O O   . ARG D 27  ? 3.304 4.218 2.418 -0.929 0.217  -0.537 27  ARG FFF O   
5065 C CB  . ARG D 27  ? 3.391 4.315 2.623 -0.935 0.222  -0.519 27  ARG FFF CB  
5066 C CG  . ARG D 27  ? 3.396 4.322 2.654 -0.943 0.195  -0.535 27  ARG FFF CG  
5067 C CD  . ARG D 27  ? 3.381 4.307 2.688 -0.947 0.186  -0.530 27  ARG FFF CD  
5068 N NE  . ARG D 27  ? 3.388 4.310 2.671 -0.949 0.165  -0.543 27  ARG FFF NE  
5069 C CZ  . ARG D 27  ? 3.397 4.316 2.693 -0.950 0.159  -0.539 27  ARG FFF CZ  
5070 N NH1 . ARG D 27  ? 3.385 4.305 2.725 -0.950 0.170  -0.522 27  ARG FFF NH1 
5071 N NH2 . ARG D 27  ? 3.450 4.366 2.719 -0.951 0.140  -0.552 27  ARG FFF NH2 
5072 N N   . THR D 28  ? 3.371 4.286 2.480 -0.922 0.233  -0.537 28  THR FFF N   
5073 C CA  . THR D 28  ? 3.422 4.327 2.471 -0.916 0.232  -0.543 28  THR FFF CA  
5074 C C   . THR D 28  ? 3.454 4.361 2.485 -0.924 0.207  -0.560 28  THR FFF C   
5075 O O   . THR D 28  ? 3.585 4.484 2.572 -0.921 0.203  -0.564 28  THR FFF O   
5076 C CB  . THR D 28  ? 3.432 4.334 2.463 -0.908 0.241  -0.544 28  THR FFF CB  
5077 O OG1 . THR D 28  ? 3.428 4.338 2.491 -0.916 0.232  -0.553 28  THR FFF OG1 
5078 C CG2 . THR D 28  ? 3.431 4.331 2.465 -0.895 0.268  -0.526 28  THR FFF CG2 
5079 N N   . PHE D 29  ? 3.454 4.369 2.515 -0.932 0.192  -0.569 29  PHE FFF N   
5080 C CA  . PHE D 29  ? 3.466 4.384 2.513 -0.937 0.170  -0.584 29  PHE FFF CA  
5081 C C   . PHE D 29  ? 3.381 4.296 2.409 -0.938 0.163  -0.583 29  PHE FFF C   
5082 O O   . PHE D 29  ? 3.298 4.214 2.304 -0.940 0.148  -0.591 29  PHE FFF O   
5083 C CB  . PHE D 29  ? 3.544 4.469 2.629 -0.942 0.157  -0.592 29  PHE FFF CB  
5084 C CG  . PHE D 29  ? 3.609 4.536 2.737 -0.945 0.156  -0.586 29  PHE FFF CG  
5085 C CD1 . PHE D 29  ? 3.632 4.558 2.760 -0.946 0.145  -0.588 29  PHE FFF CD1 
5086 C CD2 . PHE D 29  ? 3.596 4.525 2.768 -0.945 0.164  -0.580 29  PHE FFF CD2 
5087 C CE1 . PHE D 29  ? 3.599 4.524 2.767 -0.948 0.141  -0.584 29  PHE FFF CE1 
5088 C CE2 . PHE D 29  ? 3.581 4.511 2.799 -0.947 0.159  -0.575 29  PHE FFF CE2 
5089 C CZ  . PHE D 29  ? 3.578 4.505 2.793 -0.949 0.147  -0.578 29  PHE FFF CZ  
5090 N N   . SER D 30  ? 3.350 4.262 2.388 -0.936 0.173  -0.572 30  SER FFF N   
5091 C CA  . SER D 30  ? 3.306 4.216 2.332 -0.937 0.168  -0.570 30  SER FFF CA  
5092 C C   . SER D 30  ? 3.253 4.155 2.230 -0.933 0.172  -0.568 30  SER FFF C   
5093 O O   . SER D 30  ? 3.184 4.084 2.145 -0.934 0.163  -0.569 30  SER FFF O   
5094 C CB  . SER D 30  ? 3.336 4.246 2.396 -0.937 0.177  -0.558 30  SER FFF CB  
5095 O OG  . SER D 30  ? 3.392 4.298 2.447 -0.930 0.200  -0.544 30  SER FFF OG  
5096 N N   . THR D 31  ? 3.278 4.173 2.233 -0.926 0.183  -0.565 31  THR FFF N   
5097 C CA  . THR D 31  ? 3.326 4.209 2.235 -0.918 0.188  -0.562 31  THR FFF CA  
5098 C C   . THR D 31  ? 3.326 4.208 2.209 -0.923 0.168  -0.573 31  THR FFF C   
5099 O O   . THR D 31  ? 3.302 4.188 2.185 -0.926 0.157  -0.582 31  THR FFF O   
5100 C CB  . THR D 31  ? 3.332 4.207 2.221 -0.909 0.200  -0.560 31  THR FFF CB  
5101 O OG1 . THR D 31  ? 3.227 4.105 2.143 -0.903 0.221  -0.548 31  THR FFF OG1 
5102 C CG2 . THR D 31  ? 3.366 4.226 2.206 -0.898 0.202  -0.560 31  THR FFF CG2 
5103 N N   . ALA D 32  ? 3.389 4.268 2.255 -0.922 0.164  -0.570 32  ALA FFF N   
5104 C CA  . ALA D 32  ? 3.457 4.335 2.300 -0.925 0.147  -0.576 32  ALA FFF CA  
5105 C C   . ALA D 32  ? 3.598 4.460 2.399 -0.917 0.147  -0.575 32  ALA FFF C   
5106 O O   . ALA D 32  ? 3.738 4.596 2.521 -0.918 0.133  -0.582 32  ALA FFF O   
5107 C CB  . ALA D 32  ? 3.377 4.259 2.228 -0.929 0.142  -0.573 32  ALA FFF CB  
5108 N N   . ALA D 33  ? 3.615 4.467 2.401 -0.908 0.163  -0.567 33  ALA FFF N   
5109 C CA  . ALA D 33  ? 3.575 4.409 2.318 -0.896 0.165  -0.566 33  ALA FFF CA  
5110 C C   . ALA D 33  ? 3.653 4.480 2.390 -0.883 0.188  -0.556 33  ALA FFF C   
5111 O O   . ALA D 33  ? 3.549 4.386 2.319 -0.885 0.202  -0.547 33  ALA FFF O   
5112 C CB  . ALA D 33  ? 3.526 4.355 2.250 -0.896 0.155  -0.565 33  ALA FFF CB  
5113 N N   . MET D 34  ? 3.735 4.545 2.433 -0.868 0.192  -0.557 34  MET FFF N   
5114 C CA  A MET D 34  ? 3.758 4.557 2.437 -0.850 0.215  -0.545 34  MET FFF CA  
5115 C CA  B MET D 34  ? 3.753 4.553 2.434 -0.851 0.215  -0.545 34  MET FFF CA  
5116 C C   . MET D 34  ? 3.844 4.624 2.475 -0.837 0.210  -0.545 34  MET FFF C   
5117 O O   . MET D 34  ? 3.969 4.741 2.578 -0.839 0.188  -0.557 34  MET FFF O   
5118 C CB  A MET D 34  ? 3.765 4.558 2.433 -0.839 0.222  -0.547 34  MET FFF CB  
5119 C CB  B MET D 34  ? 3.750 4.548 2.429 -0.841 0.226  -0.544 34  MET FFF CB  
5120 C CG  A MET D 34  ? 3.731 4.541 2.444 -0.850 0.227  -0.547 34  MET FFF CG  
5121 C CG  B MET D 34  ? 3.713 4.530 2.445 -0.853 0.233  -0.541 34  MET FFF CG  
5122 S SD  A MET D 34  ? 3.759 4.586 2.524 -0.854 0.250  -0.530 34  MET FFF SD  
5123 S SD  B MET D 34  ? 3.748 4.564 2.485 -0.840 0.255  -0.534 34  MET FFF SD  
5124 C CE  A MET D 34  ? 3.780 4.596 2.522 -0.829 0.280  -0.513 34  MET FFF CE  
5125 C CE  B MET D 34  ? 3.751 4.565 2.489 -0.824 0.285  -0.511 34  MET FFF CE  
5126 N N   . GLY D 35  ? 3.925 4.699 2.543 -0.823 0.230  -0.532 35  GLY FFF N   
5127 C CA  . GLY D 35  ? 3.922 4.675 2.490 -0.807 0.228  -0.531 35  GLY FFF CA  
5128 C C   . GLY D 35  ? 3.781 4.520 2.318 -0.781 0.251  -0.521 35  GLY FFF C   
5129 O O   . GLY D 35  ? 3.774 4.524 2.339 -0.778 0.275  -0.507 35  GLY FFF O   
5130 N N   . TRP D 36  ? 3.668 4.383 2.149 -0.761 0.244  -0.526 36  TRP FFF N   
5131 C CA  . TRP D 36  ? 3.582 4.281 2.024 -0.731 0.267  -0.514 36  TRP FFF CA  
5132 C C   . TRP D 36  ? 3.604 4.294 2.022 -0.723 0.270  -0.507 36  TRP FFF C   
5133 O O   . TRP D 36  ? 3.528 4.210 1.931 -0.732 0.245  -0.519 36  TRP FFF O   
5134 C CB  . TRP D 36  ? 3.502 4.177 1.893 -0.710 0.258  -0.525 36  TRP FFF CB  
5135 C CG  . TRP D 36  ? 3.417 4.101 1.830 -0.712 0.264  -0.527 36  TRP FFF CG  
5136 C CD1 . TRP D 36  ? 3.428 4.117 1.859 -0.730 0.243  -0.542 36  TRP FFF CD1 
5137 C CD2 . TRP D 36  ? 3.343 4.031 1.762 -0.696 0.295  -0.511 36  TRP FFF CD2 
5138 N NE1 . TRP D 36  ? 3.397 4.093 1.844 -0.726 0.256  -0.539 36  TRP FFF NE1 
5139 C CE2 . TRP D 36  ? 3.339 4.035 1.779 -0.705 0.288  -0.520 36  TRP FFF CE2 
5140 C CE3 . TRP D 36  ? 3.375 4.062 1.785 -0.674 0.327  -0.490 36  TRP FFF CE3 
5141 C CZ2 . TRP D 36  ? 3.319 4.021 1.771 -0.694 0.313  -0.508 36  TRP FFF CZ2 
5142 C CZ3 . TRP D 36  ? 3.403 4.097 1.826 -0.662 0.353  -0.477 36  TRP FFF CZ3 
5143 C CH2 . TRP D 36  ? 3.366 4.067 1.811 -0.672 0.345  -0.486 36  TRP FFF CH2 
5144 N N   . PHE D 37  ? 3.726 4.419 2.147 -0.709 0.300  -0.486 37  PHE FFF N   
5145 C CA  . PHE D 37  ? 3.899 4.582 2.293 -0.695 0.309  -0.476 37  PHE FFF CA  
5146 C C   . PHE D 37  ? 4.088 4.752 2.434 -0.658 0.334  -0.463 37  PHE FFF C   
5147 O O   . PHE D 37  ? 4.350 5.017 2.700 -0.648 0.347  -0.459 37  PHE FFF O   
5148 C CB  . PHE D 37  ? 3.845 4.552 2.294 -0.713 0.323  -0.460 37  PHE FFF CB  
5149 C CG  . PHE D 37  ? 3.784 4.506 2.272 -0.745 0.299  -0.473 37  PHE FFF CG  
5150 C CD1 . PHE D 37  ? 3.702 4.441 2.232 -0.765 0.291  -0.481 37  PHE FFF CD1 
5151 C CD2 . PHE D 37  ? 3.740 4.460 2.222 -0.753 0.287  -0.476 37  PHE FFF CD2 
5152 C CE1 . PHE D 37  ? 3.607 4.359 2.169 -0.791 0.270  -0.491 37  PHE FFF CE1 
5153 C CE2 . PHE D 37  ? 3.631 4.366 2.147 -0.779 0.267  -0.485 37  PHE FFF CE2 
5154 C CZ  . PHE D 37  ? 3.590 4.340 2.145 -0.797 0.258  -0.493 37  PHE FFF CZ  
5155 N N   . ARG D 38  ? 4.089 4.736 2.390 -0.636 0.339  -0.457 38  ARG FFF N   
5156 C CA  . ARG D 38  ? 4.052 4.683 2.308 -0.598 0.367  -0.442 38  ARG FFF CA  
5157 C C   . ARG D 38  ? 4.024 4.655 2.274 -0.586 0.387  -0.422 38  ARG FFF C   
5158 O O   . ARG D 38  ? 3.952 4.583 2.206 -0.602 0.369  -0.430 38  ARG FFF O   
5159 C CB  . ARG D 38  ? 4.077 4.674 2.259 -0.571 0.347  -0.460 38  ARG FFF CB  
5160 C CG  . ARG D 38  ? 4.052 4.626 2.189 -0.568 0.318  -0.476 38  ARG FFF CG  
5161 C CD  . ARG D 38  ? 4.001 4.542 2.075 -0.545 0.293  -0.497 38  ARG FFF CD  
5162 N NE  . ARG D 38  ? 3.935 4.454 1.974 -0.545 0.261  -0.514 38  ARG FFF NE  
5163 C CZ  . ARG D 38  ? 3.982 4.469 1.969 -0.527 0.231  -0.535 38  ARG FFF CZ  
5164 N NH1 . ARG D 38  ? 4.018 4.491 1.978 -0.508 0.230  -0.541 38  ARG FFF NH1 
5165 N NH2 . ARG D 38  ? 4.138 4.606 2.100 -0.529 0.201  -0.549 38  ARG FFF NH2 
5166 N N   . GLN D 39  ? 4.047 4.679 2.289 -0.559 0.423  -0.397 39  GLN FFF N   
5167 C CA  . GLN D 39  ? 4.087 4.717 2.319 -0.542 0.447  -0.375 39  GLN FFF CA  
5168 C C   . GLN D 39  ? 4.164 4.769 2.325 -0.494 0.468  -0.364 39  GLN FFF C   
5169 O O   . GLN D 39  ? 4.221 4.832 2.389 -0.477 0.494  -0.348 39  GLN FFF O   
5170 C CB  . GLN D 39  ? 4.046 4.709 2.356 -0.559 0.475  -0.349 39  GLN FFF CB  
5171 C CG  . GLN D 39  ? 4.089 4.755 2.406 -0.552 0.495  -0.327 39  GLN FFF CG  
5172 C CD  . GLN D 39  ? 4.081 4.779 2.486 -0.584 0.502  -0.314 39  GLN FFF CD  
5173 O OE1 . GLN D 39  ? 4.034 4.751 2.494 -0.598 0.510  -0.308 39  GLN FFF OE1 
5174 N NE2 . GLN D 39  ? 4.115 4.816 2.533 -0.596 0.497  -0.311 39  GLN FFF NE2 
5175 N N   . ALA D 40  ? 4.191 4.768 2.285 -0.473 0.454  -0.375 40  ALA FFF N   
5176 C CA  . ALA D 40  ? 4.273 4.822 2.291 -0.423 0.472  -0.365 40  ALA FFF CA  
5177 C C   . ALA D 40  ? 4.279 4.842 2.316 -0.409 0.512  -0.330 40  ALA FFF C   
5178 O O   . ALA D 40  ? 4.349 4.931 2.436 -0.436 0.512  -0.323 40  ALA FFF O   
5179 C CB  . ALA D 40  ? 4.311 4.825 2.256 -0.408 0.437  -0.390 40  ALA FFF CB  
5180 N N   . PRO D 41  ? 4.242 4.796 2.243 -0.366 0.547  -0.306 41  PRO FFF N   
5181 C CA  . PRO D 41  ? 4.186 4.759 2.220 -0.354 0.591  -0.268 41  PRO FFF CA  
5182 C C   . PRO D 41  ? 4.058 4.632 2.097 -0.364 0.586  -0.264 41  PRO FFF C   
5183 O O   . PRO D 41  ? 4.054 4.600 2.025 -0.346 0.567  -0.280 41  PRO FFF O   
5184 C CB  . PRO D 41  ? 4.377 4.927 2.339 -0.296 0.620  -0.251 41  PRO FFF CB  
5185 C CG  . PRO D 41  ? 4.443 4.957 2.325 -0.278 0.584  -0.286 41  PRO FFF CG  
5186 C CD  . PRO D 41  ? 4.355 4.879 2.282 -0.326 0.547  -0.315 41  PRO FFF CD  
5187 N N   . GLY D 42  ? 3.940 4.545 2.059 -0.395 0.599  -0.246 42  GLY FFF N   
5188 C CA  . GLY D 42  ? 3.903 4.514 2.038 -0.405 0.600  -0.237 42  GLY FFF CA  
5189 C C   . GLY D 42  ? 3.880 4.483 2.007 -0.435 0.556  -0.270 42  GLY FFF C   
5190 O O   . GLY D 42  ? 3.816 4.424 1.958 -0.446 0.556  -0.263 42  GLY FFF O   
5191 N N   . LYS D 43  ? 3.898 4.490 2.005 -0.449 0.520  -0.302 43  LYS FFF N   
5192 C CA  . LYS D 43  ? 3.877 4.460 1.976 -0.477 0.477  -0.333 43  LYS FFF CA  
5193 C C   . LYS D 43  ? 3.916 4.528 2.092 -0.522 0.462  -0.342 43  LYS FFF C   
5194 O O   . LYS D 43  ? 3.911 4.540 2.130 -0.526 0.482  -0.329 43  LYS FFF O   
5195 C CB  . LYS D 43  ? 3.872 4.421 1.894 -0.457 0.447  -0.361 43  LYS FFF CB  
5196 C CG  . LYS D 43  ? 3.888 4.404 1.825 -0.407 0.458  -0.355 43  LYS FFF CG  
5197 C CD  . LYS D 43  ? 3.868 4.348 1.732 -0.383 0.430  -0.382 43  LYS FFF CD  
5198 C CE  . LYS D 43  ? 3.844 4.306 1.687 -0.400 0.382  -0.414 43  LYS FFF CE  
5199 N NZ  . LYS D 43  ? 3.873 4.304 1.661 -0.383 0.352  -0.440 43  LYS FFF NZ  
5200 N N   . GLU D 44  ? 4.006 4.620 2.197 -0.552 0.431  -0.362 44  GLU FFF N   
5201 C CA  . GLU D 44  ? 3.916 4.556 2.177 -0.595 0.413  -0.372 44  GLU FFF CA  
5202 C C   . GLU D 44  ? 3.930 4.573 2.202 -0.602 0.403  -0.385 44  GLU FFF C   
5203 O O   . GLU D 44  ? 3.844 4.463 2.060 -0.585 0.387  -0.402 44  GLU FFF O   
5204 C CB  . GLU D 44  ? 3.871 4.506 2.125 -0.617 0.377  -0.394 44  GLU FFF CB  
5205 C CG  . GLU D 44  ? 3.863 4.504 2.133 -0.626 0.381  -0.384 44  GLU FFF CG  
5206 C CD  . GLU D 44  ? 3.805 4.455 2.101 -0.659 0.349  -0.402 44  GLU FFF CD  
5207 O OE1 . GLU D 44  ? 3.680 4.353 2.034 -0.686 0.344  -0.405 44  GLU FFF OE1 
5208 O OE2 . GLU D 44  ? 3.803 4.437 2.060 -0.655 0.330  -0.414 44  GLU FFF OE2 
5209 N N   . ARG D 45  ? 4.048 4.717 2.388 -0.629 0.407  -0.381 45  ARG FFF N   
5210 C CA  . ARG D 45  ? 4.106 4.781 2.464 -0.644 0.390  -0.398 45  ARG FFF CA  
5211 C C   . ARG D 45  ? 4.165 4.831 2.504 -0.662 0.350  -0.426 45  ARG FFF C   
5212 O O   . ARG D 45  ? 4.217 4.889 2.573 -0.679 0.338  -0.428 45  ARG FFF O   
5213 C CB  . ARG D 45  ? 4.003 4.708 2.440 -0.669 0.401  -0.388 45  ARG FFF CB  
5214 C CG  . ARG D 45  ? 3.964 4.673 2.413 -0.673 0.396  -0.397 45  ARG FFF CG  
5215 C CD  . ARG D 45  ? 3.908 4.643 2.429 -0.687 0.415  -0.382 45  ARG FFF CD  
5216 N NE  . ARG D 45  ? 3.905 4.660 2.486 -0.716 0.407  -0.380 45  ARG FFF NE  
5217 C CZ  . ARG D 45  ? 3.878 4.654 2.526 -0.728 0.421  -0.365 45  ARG FFF CZ  
5218 N NH1 . ARG D 45  ? 3.843 4.625 2.511 -0.715 0.446  -0.348 45  ARG FFF NH1 
5219 N NH2 . ARG D 45  ? 3.872 4.662 2.568 -0.752 0.409  -0.367 45  ARG FFF NH2 
5220 N N   . GLU D 46  ? 4.108 4.758 2.414 -0.657 0.330  -0.445 46  GLU FFF N   
5221 C CA  . GLU D 46  ? 3.986 4.622 2.266 -0.667 0.292  -0.470 46  GLU FFF CA  
5222 C C   . GLU D 46  ? 3.947 4.592 2.253 -0.686 0.274  -0.485 46  GLU FFF C   
5223 O O   . GLU D 46  ? 3.967 4.610 2.268 -0.674 0.285  -0.483 46  GLU FFF O   
5224 C CB  . GLU D 46  ? 3.951 4.553 2.155 -0.634 0.284  -0.476 46  GLU FFF CB  
5225 C CG  . GLU D 46  ? 3.907 4.491 2.084 -0.640 0.244  -0.502 46  GLU FFF CG  
5226 C CD  . GLU D 46  ? 3.900 4.448 2.006 -0.606 0.233  -0.513 46  GLU FFF CD  
5227 O OE1 . GLU D 46  ? 3.940 4.480 2.020 -0.579 0.257  -0.503 46  GLU FFF OE1 
5228 O OE2 . GLU D 46  ? 3.795 4.323 1.872 -0.606 0.201  -0.530 46  GLU FFF OE2 
5229 N N   . PHE D 47  ? 3.915 4.570 2.248 -0.713 0.248  -0.498 47  PHE FFF N   
5230 C CA  . PHE D 47  ? 3.930 4.594 2.288 -0.731 0.227  -0.513 47  PHE FFF CA  
5231 C C   . PHE D 47  ? 3.976 4.613 2.284 -0.713 0.209  -0.528 47  PHE FFF C   
5232 O O   . PHE D 47  ? 3.973 4.587 2.236 -0.699 0.194  -0.536 47  PHE FFF O   
5233 C CB  . PHE D 47  ? 3.909 4.586 2.297 -0.759 0.203  -0.523 47  PHE FFF CB  
5234 C CG  . PHE D 47  ? 3.867 4.549 2.273 -0.774 0.181  -0.538 47  PHE FFF CG  
5235 C CD1 . PHE D 47  ? 3.749 4.451 2.197 -0.787 0.190  -0.536 47  PHE FFF CD1 
5236 C CD2 . PHE D 47  ? 3.882 4.548 2.263 -0.774 0.151  -0.553 47  PHE FFF CD2 
5237 C CE1 . PHE D 47  ? 3.669 4.376 2.132 -0.799 0.170  -0.548 47  PHE FFF CE1 
5238 C CE2 . PHE D 47  ? 3.783 4.455 2.184 -0.787 0.132  -0.564 47  PHE FFF CE2 
5239 C CZ  . PHE D 47  ? 3.683 4.376 2.123 -0.800 0.142  -0.562 47  PHE FFF CZ  
5240 N N   . VAL D 48  ? 3.966 4.606 2.282 -0.713 0.209  -0.534 48  VAL FFF N   
5241 C CA  . VAL D 48  ? 3.994 4.608 2.266 -0.695 0.191  -0.549 48  VAL FFF CA  
5242 C C   . VAL D 48  ? 3.987 4.609 2.287 -0.719 0.162  -0.565 48  VAL FFF C   
5243 O O   . VAL D 48  ? 4.017 4.621 2.293 -0.718 0.132  -0.579 48  VAL FFF O   
5244 C CB  . VAL D 48  ? 3.943 4.552 2.199 -0.673 0.215  -0.541 48  VAL FFF CB  
5245 C CG1 . VAL D 48  ? 3.938 4.524 2.157 -0.659 0.194  -0.559 48  VAL FFF CG1 
5246 C CG2 . VAL D 48  ? 3.885 4.485 2.109 -0.645 0.244  -0.524 48  VAL FFF CG2 
5247 N N   . ALA D 49  ? 3.974 4.620 2.322 -0.738 0.170  -0.562 49  ALA FFF N   
5248 C CA  . ALA D 49  ? 3.930 4.586 2.307 -0.758 0.147  -0.575 49  ALA FFF CA  
5249 C C   . ALA D 49  ? 3.788 4.476 2.223 -0.781 0.160  -0.568 49  ALA FFF C   
5250 O O   . ALA D 49  ? 3.662 4.361 2.114 -0.778 0.187  -0.555 49  ALA FFF O   
5251 C CB  . ALA D 49  ? 3.981 4.620 2.330 -0.742 0.140  -0.585 49  ALA FFF CB  
5252 N N   . ALA D 50  ? 3.765 4.466 2.232 -0.803 0.140  -0.576 50  ALA FFF N   
5253 C CA  . ALA D 50  ? 3.817 4.546 2.337 -0.824 0.145  -0.573 50  ALA FFF CA  
5254 C C   . ALA D 50  ? 3.709 4.441 2.242 -0.834 0.125  -0.585 50  ALA FFF C   
5255 O O   . ALA D 50  ? 3.744 4.462 2.257 -0.832 0.102  -0.594 50  ALA FFF O   
5256 C CB  . ALA D 50  ? 3.833 4.577 2.379 -0.840 0.142  -0.568 50  ALA FFF CB  
5257 N N   . ILE D 51  ? 3.487 4.237 2.055 -0.844 0.134  -0.583 51  ILE FFF N   
5258 C CA  . ILE D 51  ? 3.355 4.113 1.943 -0.854 0.119  -0.593 51  ILE FFF CA  
5259 C C   . ILE D 51  ? 3.333 4.116 1.968 -0.873 0.123  -0.589 51  ILE FFF C   
5260 O O   . ILE D 51  ? 3.403 4.197 2.058 -0.873 0.143  -0.581 51  ILE FFF O   
5261 C CB  . ILE D 51  ? 3.281 4.028 1.853 -0.841 0.125  -0.597 51  ILE FFF CB  
5262 C CG1 . ILE D 51  ? 3.223 3.974 1.808 -0.850 0.106  -0.607 51  ILE FFF CG1 
5263 C CG2 . ILE D 51  ? 3.266 4.024 1.857 -0.838 0.154  -0.586 51  ILE FFF CG2 
5264 C CD1 . ILE D 51  ? 3.223 3.959 1.785 -0.836 0.107  -0.613 51  ILE FFF CD1 
5265 N N   . ARG D 52  ? 3.195 3.988 1.848 -0.886 0.104  -0.594 52  ARG FFF N   
5266 C CA  . ARG D 52  ? 3.002 3.819 1.697 -0.900 0.105  -0.593 52  ARG FFF CA  
5267 C C   . ARG D 52  ? 2.976 3.797 1.684 -0.900 0.110  -0.597 52  ARG FFF C   
5268 O O   . ARG D 52  ? 2.942 3.753 1.635 -0.896 0.099  -0.604 52  ARG FFF O   
5269 C CB  . ARG D 52  ? 2.919 3.745 1.627 -0.911 0.085  -0.595 52  ARG FFF CB  
5270 C CG  . ARG D 52  ? 2.789 3.637 1.533 -0.921 0.087  -0.593 52  ARG FFF CG  
5271 C CD  . ARG D 52  ? 2.785 3.644 1.542 -0.929 0.071  -0.592 52  ARG FFF CD  
5272 N NE  . ARG D 52  ? 2.798 3.651 1.541 -0.928 0.064  -0.588 52  ARG FFF NE  
5273 C CZ  . ARG D 52  ? 2.769 3.627 1.515 -0.930 0.069  -0.583 52  ARG FFF CZ  
5274 N NH1 . ARG D 52  ? 2.705 3.573 1.469 -0.932 0.081  -0.581 52  ARG FFF NH1 
5275 N NH2 . ARG D 52  ? 2.822 3.675 1.554 -0.929 0.061  -0.580 52  ARG FFF NH2 
5276 N N   . TRP D 53  ? 2.982 3.816 1.718 -0.904 0.124  -0.593 53  TRP FFF N   
5277 C CA  . TRP D 53  ? 2.956 3.796 1.709 -0.904 0.130  -0.597 53  TRP FFF CA  
5278 C C   . TRP D 53  ? 2.922 3.769 1.685 -0.912 0.112  -0.605 53  TRP FFF C   
5279 O O   . TRP D 53  ? 2.888 3.728 1.643 -0.908 0.109  -0.610 53  TRP FFF O   
5280 C CB  . TRP D 53  ? 2.920 3.773 1.707 -0.909 0.146  -0.591 53  TRP FFF CB  
5281 C CG  . TRP D 53  ? 2.891 3.744 1.687 -0.904 0.159  -0.590 53  TRP FFF CG  
5282 C CD1 . TRP D 53  ? 2.879 3.744 1.705 -0.910 0.157  -0.594 53  TRP FFF CD1 
5283 C CD2 . TRP D 53  ? 2.921 3.762 1.696 -0.890 0.175  -0.584 53  TRP FFF CD2 
5284 N NE1 . TRP D 53  ? 2.887 3.748 1.714 -0.903 0.172  -0.591 53  TRP FFF NE1 
5285 C CE2 . TRP D 53  ? 2.911 3.758 1.707 -0.889 0.184  -0.585 53  TRP FFF CE2 
5286 C CE3 . TRP D 53  ? 2.911 3.736 1.650 -0.876 0.184  -0.579 53  TRP FFF CE3 
5287 C CZ2 . TRP D 53  ? 2.889 3.727 1.671 -0.875 0.202  -0.579 53  TRP FFF CZ2 
5288 C CZ3 . TRP D 53  ? 2.890 3.705 1.613 -0.860 0.201  -0.573 53  TRP FFF CZ3 
5289 C CH2 . TRP D 53  ? 2.877 3.700 1.623 -0.860 0.211  -0.572 53  TRP FFF CH2 
5290 N N   . SER D 54  ? 2.914 3.773 1.693 -0.922 0.100  -0.605 54  SER FFF N   
5291 C CA  . SER D 54  ? 2.928 3.794 1.718 -0.928 0.083  -0.609 54  SER FFF CA  
5292 C C   . SER D 54  ? 2.965 3.818 1.731 -0.925 0.067  -0.611 54  SER FFF C   
5293 O O   . SER D 54  ? 2.944 3.791 1.697 -0.924 0.063  -0.607 54  SER FFF O   
5294 C CB  . SER D 54  ? 2.909 3.793 1.723 -0.935 0.078  -0.606 54  SER FFF CB  
5295 O OG  . SER D 54  ? 2.880 3.769 1.699 -0.939 0.062  -0.607 54  SER FFF OG  
5296 N N   . GLY D 55  ? 3.003 3.849 1.765 -0.923 0.057  -0.616 55  GLY FFF N   
5297 C CA  . GLY D 55  ? 3.072 3.905 1.819 -0.921 0.037  -0.619 55  GLY FFF CA  
5298 C C   . GLY D 55  ? 3.230 4.038 1.940 -0.908 0.037  -0.623 55  GLY FFF C   
5299 O O   . GLY D 55  ? 3.311 4.104 2.007 -0.904 0.020  -0.630 55  GLY FFF O   
5300 N N   . GLY D 56  ? 3.322 4.125 2.015 -0.901 0.054  -0.620 56  GLY FFF N   
5301 C CA  . GLY D 56  ? 3.336 4.115 1.989 -0.885 0.059  -0.623 56  GLY FFF CA  
5302 C C   . GLY D 56  ? 3.352 4.114 1.979 -0.879 0.044  -0.623 56  GLY FFF C   
5303 O O   . GLY D 56  ? 3.394 4.132 1.983 -0.863 0.041  -0.628 56  GLY FFF O   
5304 N N   . SER D 57  ? 3.329 4.103 1.975 -0.890 0.035  -0.619 57  SER FFF N   
5305 C CA  . SER D 57  ? 3.378 4.139 2.006 -0.888 0.020  -0.618 57  SER FFF CA  
5306 C C   . SER D 57  ? 3.455 4.202 2.050 -0.875 0.036  -0.615 57  SER FFF C   
5307 O O   . SER D 57  ? 3.291 4.052 1.898 -0.877 0.058  -0.608 57  SER FFF O   
5308 C CB  . SER D 57  ? 3.290 4.069 1.948 -0.902 0.012  -0.611 57  SER FFF CB  
5309 O OG  . SER D 57  ? 3.214 4.002 1.897 -0.910 -0.005 -0.612 57  SER FFF OG  
5310 N N   . ALA D 58  ? 3.569 4.291 2.127 -0.862 0.023  -0.620 58  ALA FFF N   
5311 C CA  . ALA D 58  ? 3.516 4.219 2.034 -0.844 0.037  -0.618 58  ALA FFF CA  
5312 C C   . ALA D 58  ? 3.493 4.187 1.996 -0.843 0.026  -0.616 58  ALA FFF C   
5313 O O   . ALA D 58  ? 3.272 3.961 1.782 -0.849 -0.001 -0.620 58  ALA FFF O   
5314 C CB  . ALA D 58  ? 3.581 4.259 2.061 -0.824 0.033  -0.626 58  ALA FFF CB  
5315 N N   . TYR D 59  ? 3.527 4.220 2.014 -0.835 0.045  -0.608 59  TYR FFF N   
5316 C CA  . TYR D 59  ? 3.608 4.289 2.073 -0.830 0.040  -0.605 59  TYR FFF CA  
5317 C C   . TYR D 59  ? 3.605 4.265 2.024 -0.806 0.057  -0.603 59  TYR FFF C   
5318 O O   . TYR D 59  ? 3.443 4.112 1.866 -0.801 0.084  -0.595 59  TYR FFF O   
5319 C CB  . TYR D 59  ? 3.626 4.331 2.123 -0.846 0.050  -0.596 59  TYR FFF CB  
5320 C CG  . TYR D 59  ? 3.639 4.336 2.120 -0.844 0.042  -0.593 59  TYR FFF CG  
5321 C CD1 . TYR D 59  ? 3.607 4.301 2.096 -0.852 0.015  -0.597 59  TYR FFF CD1 
5322 C CD2 . TYR D 59  ? 3.605 4.297 2.067 -0.835 0.060  -0.586 59  TYR FFF CD2 
5323 C CE1 . TYR D 59  ? 3.545 4.232 2.022 -0.851 0.006  -0.594 59  TYR FFF CE1 
5324 C CE2 . TYR D 59  ? 3.571 4.256 2.019 -0.834 0.052  -0.583 59  TYR FFF CE2 
5325 C CZ  . TYR D 59  ? 3.552 4.234 2.006 -0.842 0.025  -0.588 59  TYR FFF CZ  
5326 O OH  . TYR D 59  ? 3.573 4.248 2.015 -0.840 0.017  -0.586 59  TYR FFF OH  
5327 N N   . TYR D 60  ? 3.633 4.267 2.012 -0.791 0.041  -0.609 60  TYR FFF N   
5328 C CA  . TYR D 60  ? 3.635 4.243 1.961 -0.763 0.052  -0.609 60  TYR FFF CA  
5329 C C   . TYR D 60  ? 3.613 4.212 1.918 -0.757 0.049  -0.604 60  TYR FFF C   
5330 O O   . TYR D 60  ? 3.574 4.173 1.892 -0.770 0.026  -0.608 60  TYR FFF O   
5331 C CB  . TYR D 60  ? 3.622 4.199 1.908 -0.744 0.030  -0.623 60  TYR FFF CB  
5332 C CG  . TYR D 60  ? 3.651 4.234 1.953 -0.747 0.029  -0.628 60  TYR FFF CG  
5333 C CD1 . TYR D 60  ? 3.608 4.187 1.890 -0.730 0.053  -0.625 60  TYR FFF CD1 
5334 C CD2 . TYR D 60  ? 3.602 4.194 1.938 -0.765 0.005  -0.636 60  TYR FFF CD2 
5335 C CE1 . TYR D 60  ? 3.607 4.191 1.904 -0.733 0.052  -0.630 60  TYR FFF CE1 
5336 C CE2 . TYR D 60  ? 3.553 4.149 1.903 -0.768 0.004  -0.641 60  TYR FFF CE2 
5337 C CZ  . TYR D 60  ? 3.592 4.184 1.922 -0.752 0.027  -0.639 60  TYR FFF CZ  
5338 O OH  . TYR D 60  ? 3.570 4.167 1.914 -0.755 0.026  -0.644 60  TYR FFF OH  
5339 N N   . ALA D 61  ? 3.603 4.193 1.876 -0.738 0.073  -0.596 61  ALA FFF N   
5340 C CA  . ALA D 61  ? 3.649 4.222 1.888 -0.726 0.071  -0.593 61  ALA FFF CA  
5341 C C   . ALA D 61  ? 3.753 4.290 1.943 -0.704 0.041  -0.609 61  ALA FFF C   
5342 O O   . ALA D 61  ? 3.857 4.379 2.027 -0.691 0.035  -0.617 61  ALA FFF O   
5343 C CB  . ALA D 61  ? 3.659 4.235 1.883 -0.710 0.106  -0.578 61  ALA FFF CB  
5344 N N   . ASP D 62  ? 3.814 4.335 1.984 -0.701 0.022  -0.612 62  ASP FFF N   
5345 C CA  . ASP D 62  ? 3.898 4.382 2.025 -0.682 -0.013 -0.628 62  ASP FFF CA  
5346 C C   . ASP D 62  ? 3.864 4.318 1.929 -0.645 -0.003 -0.632 62  ASP FFF C   
5347 O O   . ASP D 62  ? 3.836 4.261 1.871 -0.630 -0.030 -0.648 62  ASP FFF O   
5348 C CB  . ASP D 62  ? 4.008 4.482 2.127 -0.684 -0.031 -0.630 62  ASP FFF CB  
5349 C CG  . ASP D 62  ? 3.989 4.483 2.162 -0.715 -0.053 -0.630 62  ASP FFF CG  
5350 O OD1 . ASP D 62  ? 3.917 4.445 2.138 -0.739 -0.035 -0.620 62  ASP FFF OD1 
5351 O OD2 . ASP D 62  ? 3.995 4.469 2.161 -0.714 -0.088 -0.641 62  ASP FFF OD2 
5352 N N   . SER D 63  ? 3.789 4.251 1.839 -0.632 0.035  -0.617 63  SER FFF N   
5353 C CA  . SER D 63  ? 3.867 4.303 1.856 -0.593 0.052  -0.615 63  SER FFF CA  
5354 C C   . SER D 63  ? 3.999 4.425 1.975 -0.581 0.049  -0.624 63  SER FFF C   
5355 O O   . SER D 63  ? 4.232 4.626 2.146 -0.544 0.049  -0.629 63  SER FFF O   
5356 C CB  . SER D 63  ? 3.761 4.215 1.754 -0.587 0.097  -0.593 63  SER FFF CB  
5357 O OG  . SER D 63  ? 3.543 4.033 1.593 -0.610 0.120  -0.582 63  SER FFF OG  
5358 N N   . VAL D 64  ? 3.968 4.418 1.996 -0.607 0.046  -0.626 64  VAL FFF N   
5359 C CA  . VAL D 64  ? 3.971 4.415 1.993 -0.599 0.046  -0.632 64  VAL FFF CA  
5360 C C   . VAL D 64  ? 4.004 4.448 2.056 -0.619 0.009  -0.649 64  VAL FFF C   
5361 O O   . VAL D 64  ? 4.021 4.455 2.063 -0.611 0.002  -0.658 64  VAL FFF O   
5362 C CB  . VAL D 64  ? 3.911 4.387 1.968 -0.607 0.086  -0.615 64  VAL FFF CB  
5363 C CG1 . VAL D 64  ? 3.894 4.369 1.923 -0.584 0.123  -0.597 64  VAL FFF CG1 
5364 C CG2 . VAL D 64  ? 3.851 4.366 1.980 -0.647 0.091  -0.609 64  VAL FFF CG2 
5365 N N   . LYS D 65  ? 3.991 4.446 2.079 -0.645 -0.013 -0.651 65  LYS FFF N   
5366 C CA  . LYS D 65  ? 3.895 4.354 2.021 -0.667 -0.047 -0.663 65  LYS FFF CA  
5367 C C   . LYS D 65  ? 4.072 4.490 2.153 -0.642 -0.080 -0.682 65  LYS FFF C   
5368 O O   . LYS D 65  ? 4.115 4.499 2.140 -0.615 -0.091 -0.688 65  LYS FFF O   
5369 C CB  . LYS D 65  ? 3.729 4.201 1.891 -0.691 -0.066 -0.661 65  LYS FFF CB  
5370 C CG  . LYS D 65  ? 3.649 4.133 1.862 -0.716 -0.093 -0.667 65  LYS FFF CG  
5371 C CD  . LYS D 65  ? 3.644 4.152 1.906 -0.744 -0.101 -0.660 65  LYS FFF CD  
5372 C CE  . LYS D 65  ? 3.628 4.168 1.949 -0.770 -0.099 -0.655 65  LYS FFF CE  
5373 N NZ  . LYS D 65  ? 3.574 4.138 1.942 -0.795 -0.106 -0.646 65  LYS FFF NZ  
5374 N N   . GLY D 66  ? 4.167 4.586 2.266 -0.648 -0.093 -0.690 66  GLY FFF N   
5375 C CA  . GLY D 66  ? 4.249 4.629 2.312 -0.627 -0.127 -0.709 66  GLY FFF CA  
5376 C C   . GLY D 66  ? 4.304 4.665 2.312 -0.593 -0.108 -0.712 66  GLY FFF C   
5377 O O   . GLY D 66  ? 4.425 4.754 2.401 -0.573 -0.136 -0.728 66  GLY FFF O   
5378 N N   . ARG D 67  ? 4.258 4.637 2.257 -0.586 -0.064 -0.695 67  ARG FFF N   
5379 C CA  . ARG D 67  ? 4.305 4.670 2.256 -0.554 -0.038 -0.692 67  ARG FFF CA  
5380 C C   . ARG D 67  ? 4.235 4.637 2.232 -0.572 -0.004 -0.679 67  ARG FFF C   
5381 O O   . ARG D 67  ? 4.353 4.748 2.338 -0.561 -0.002 -0.684 67  ARG FFF O   
5382 C CB  . ARG D 67  ? 4.309 4.658 2.206 -0.524 -0.016 -0.683 67  ARG FFF CB  
5383 C CG  . ARG D 67  ? 4.371 4.677 2.212 -0.498 -0.051 -0.698 67  ARG FFF CG  
5384 C CD  . ARG D 67  ? 4.393 4.679 2.170 -0.461 -0.028 -0.690 67  ARG FFF CD  
5385 N NE  . ARG D 67  ? 4.338 4.654 2.141 -0.474 0.009  -0.668 67  ARG FFF NE  
5386 C CZ  . ARG D 67  ? 4.326 4.660 2.127 -0.464 0.055  -0.647 67  ARG FFF CZ  
5387 N NH1 . ARG D 67  ? 4.360 4.687 2.133 -0.439 0.073  -0.644 67  ARG FFF NH1 
5388 N NH2 . ARG D 67  ? 4.300 4.661 2.130 -0.478 0.083  -0.628 67  ARG FFF NH2 
5389 N N   . PHE D 68  ? 4.113 4.552 2.159 -0.598 0.021  -0.662 68  PHE FFF N   
5390 C CA  . PHE D 68  ? 4.097 4.570 2.184 -0.613 0.056  -0.648 68  PHE FFF CA  
5391 C C   . PHE D 68  ? 4.158 4.656 2.307 -0.648 0.041  -0.653 68  PHE FFF C   
5392 O O   . PHE D 68  ? 4.330 4.831 2.503 -0.667 0.014  -0.660 68  PHE FFF O   
5393 C CB  . PHE D 68  ? 4.062 4.558 2.167 -0.619 0.091  -0.627 68  PHE FFF CB  
5394 C CG  . PHE D 68  ? 4.133 4.611 2.185 -0.583 0.116  -0.617 68  PHE FFF CG  
5395 C CD1 . PHE D 68  ? 4.201 4.640 2.184 -0.546 0.103  -0.628 68  PHE FFF CD1 
5396 C CD2 . PHE D 68  ? 4.174 4.674 2.244 -0.584 0.153  -0.595 68  PHE FFF CD2 
5397 C CE1 . PHE D 68  ? 4.250 4.673 2.181 -0.510 0.129  -0.616 68  PHE FFF CE1 
5398 C CE2 . PHE D 68  ? 4.148 4.633 2.171 -0.550 0.180  -0.582 68  PHE FFF CE2 
5399 C CZ  . PHE D 68  ? 4.196 4.643 2.148 -0.513 0.168  -0.592 68  PHE FFF CZ  
5400 N N   . THR D 69  ? 4.136 4.652 2.310 -0.654 0.058  -0.649 69  THR FFF N   
5401 C CA  . THR D 69  ? 3.965 4.508 2.199 -0.686 0.052  -0.651 69  THR FFF CA  
5402 C C   . THR D 69  ? 3.758 4.335 2.031 -0.698 0.089  -0.634 69  THR FFF C   
5403 O O   . THR D 69  ? 3.714 4.288 1.969 -0.680 0.115  -0.626 69  THR FFF O   
5404 C CB  . THR D 69  ? 4.027 4.557 2.253 -0.680 0.033  -0.665 69  THR FFF CB  
5405 O OG1 . THR D 69  ? 4.141 4.642 2.341 -0.672 -0.006 -0.680 69  THR FFF OG1 
5406 C CG2 . THR D 69  ? 3.959 4.519 2.243 -0.708 0.033  -0.664 69  THR FFF CG2 
5407 N N   . ILE D 70  ? 3.611 4.217 1.937 -0.728 0.091  -0.628 70  ILE FFF N   
5408 C CA  . ILE D 70  ? 3.503 4.141 1.876 -0.743 0.119  -0.615 70  ILE FFF CA  
5409 C C   . ILE D 70  ? 3.493 4.146 1.904 -0.763 0.106  -0.623 70  ILE FFF C   
5410 O O   . ILE D 70  ? 3.531 4.181 1.951 -0.775 0.077  -0.633 70  ILE FFF O   
5411 C CB  . ILE D 70  ? 3.398 4.055 1.798 -0.758 0.130  -0.603 70  ILE FFF CB  
5412 C CG1 . ILE D 70  ? 3.344 4.028 1.787 -0.769 0.159  -0.590 70  ILE FFF CG1 
5413 C CG2 . ILE D 70  ? 3.388 4.053 1.812 -0.780 0.104  -0.610 70  ILE FFF CG2 
5414 C CD1 . ILE D 70  ? 3.329 4.029 1.799 -0.782 0.169  -0.579 70  ILE FFF CD1 
5415 N N   . SER D 71  ? 3.522 4.188 1.953 -0.764 0.125  -0.618 71  SER FFF N   
5416 C CA  . SER D 71  ? 3.546 4.228 2.014 -0.781 0.116  -0.625 71  SER FFF CA  
5417 C C   . SER D 71  ? 3.573 4.280 2.081 -0.790 0.144  -0.613 71  SER FFF C   
5418 O O   . SER D 71  ? 3.627 4.336 2.130 -0.780 0.168  -0.601 71  SER FFF O   
5419 C CB  . SER D 71  ? 3.538 4.198 1.976 -0.766 0.101  -0.637 71  SER FFF CB  
5420 O OG  . SER D 71  ? 3.540 4.192 1.954 -0.745 0.125  -0.632 71  SER FFF OG  
5421 N N   . ARG D 72  ? 3.552 4.278 2.100 -0.808 0.139  -0.617 72  ARG FFF N   
5422 C CA  . ARG D 72  ? 3.549 4.298 2.138 -0.817 0.162  -0.607 72  ARG FFF CA  
5423 C C   . ARG D 72  ? 3.491 4.249 2.103 -0.826 0.155  -0.615 72  ARG FFF C   
5424 O O   . ARG D 72  ? 3.521 4.277 2.134 -0.835 0.131  -0.626 72  ARG FFF O   
5425 C CB  . ARG D 72  ? 3.614 4.382 2.237 -0.834 0.166  -0.600 72  ARG FFF CB  
5426 C CG  . ARG D 72  ? 3.600 4.377 2.242 -0.852 0.142  -0.607 72  ARG FFF CG  
5427 C CD  . ARG D 72  ? 3.561 4.361 2.248 -0.869 0.141  -0.609 72  ARG FFF CD  
5428 N NE  . ARG D 72  ? 3.586 4.394 2.289 -0.883 0.119  -0.615 72  ARG FFF NE  
5429 C CZ  . ARG D 72  ? 3.608 4.410 2.302 -0.885 0.099  -0.624 72  ARG FFF CZ  
5430 N NH1 . ARG D 72  ? 3.633 4.417 2.300 -0.873 0.095  -0.630 72  ARG FFF NH1 
5431 N NH2 . ARG D 72  ? 3.634 4.447 2.349 -0.897 0.083  -0.625 72  ARG FFF NH2 
5432 N N   . ASP D 73  ? 3.424 4.191 2.054 -0.824 0.175  -0.609 73  ASP FFF N   
5433 C CA  . ASP D 73  ? 3.381 4.162 2.044 -0.836 0.171  -0.614 73  ASP FFF CA  
5434 C C   . ASP D 73  ? 3.392 4.198 2.106 -0.852 0.183  -0.606 73  ASP FFF C   
5435 O O   . ASP D 73  ? 3.426 4.237 2.153 -0.846 0.205  -0.594 73  ASP FFF O   
5436 C CB  . ASP D 73  ? 3.384 4.156 2.032 -0.820 0.183  -0.615 73  ASP FFF CB  
5437 C CG  . ASP D 73  ? 3.287 4.074 1.967 -0.832 0.180  -0.620 73  ASP FFF CG  
5438 O OD1 . ASP D 73  ? 3.108 3.914 1.828 -0.851 0.174  -0.621 73  ASP FFF OD1 
5439 O OD2 . ASP D 73  ? 3.396 4.173 2.059 -0.820 0.184  -0.624 73  ASP FFF OD2 
5440 N N   . LYS D 74  ? 3.439 4.259 2.180 -0.870 0.166  -0.612 74  LYS FFF N   
5441 C CA  . LYS D 74  ? 3.524 4.366 2.311 -0.885 0.171  -0.608 74  LYS FFF CA  
5442 C C   . LYS D 74  ? 3.519 4.370 2.337 -0.885 0.185  -0.605 74  LYS FFF C   
5443 O O   . LYS D 74  ? 3.457 4.317 2.303 -0.887 0.200  -0.595 74  LYS FFF O   
5444 C CB  . LYS D 74  ? 3.552 4.403 2.354 -0.899 0.149  -0.616 74  LYS FFF CB  
5445 C CG  . LYS D 74  ? 3.570 4.414 2.349 -0.900 0.134  -0.618 74  LYS FFF CG  
5446 C CD  . LYS D 74  ? 3.466 4.322 2.263 -0.912 0.115  -0.623 74  LYS FFF CD  
5447 C CE  . LYS D 74  ? 3.430 4.299 2.249 -0.920 0.116  -0.618 74  LYS FFF CE  
5448 N NZ  . LYS D 74  ? 3.430 4.309 2.259 -0.929 0.098  -0.621 74  LYS FFF NZ  
5449 N N   . ALA D 75  ? 3.510 4.360 2.326 -0.885 0.180  -0.612 75  ALA FFF N   
5450 C CA  . ALA D 75  ? 3.469 4.328 2.314 -0.885 0.192  -0.610 75  ALA FFF CA  
5451 C C   . ALA D 75  ? 3.527 4.383 2.374 -0.873 0.218  -0.596 75  ALA FFF C   
5452 O O   . ALA D 75  ? 3.453 4.322 2.341 -0.877 0.230  -0.589 75  ALA FFF O   
5453 C CB  . ALA D 75  ? 3.471 4.325 2.301 -0.882 0.183  -0.620 75  ALA FFF CB  
5454 N N   . LYS D 76  ? 3.601 4.441 2.406 -0.856 0.226  -0.592 76  LYS FFF N   
5455 C CA  . LYS D 76  ? 3.592 4.426 2.390 -0.839 0.253  -0.576 76  LYS FFF CA  
5456 C C   . LYS D 76  ? 3.534 4.372 2.342 -0.839 0.264  -0.563 76  LYS FFF C   
5457 O O   . LYS D 76  ? 3.566 4.403 2.377 -0.825 0.288  -0.547 76  LYS FFF O   
5458 C CB  . LYS D 76  ? 3.687 4.499 2.428 -0.817 0.255  -0.578 76  LYS FFF CB  
5459 C CG  . LYS D 76  ? 3.779 4.586 2.512 -0.809 0.257  -0.584 76  LYS FFF CG  
5460 C CD  . LYS D 76  ? 3.915 4.697 2.586 -0.784 0.257  -0.588 76  LYS FFF CD  
5461 C CE  . LYS D 76  ? 3.926 4.699 2.581 -0.779 0.245  -0.601 76  LYS FFF CE  
5462 N NZ  . LYS D 76  ? 3.951 4.735 2.634 -0.776 0.265  -0.593 76  LYS FFF NZ  
5463 N N   . ASN D 77  ? 3.444 4.287 2.261 -0.853 0.248  -0.569 77  ASN FFF N   
5464 C CA  . ASN D 77  ? 3.364 4.209 2.188 -0.855 0.254  -0.558 77  ASN FFF CA  
5465 C C   . ASN D 77  ? 3.329 4.159 2.113 -0.834 0.270  -0.548 77  ASN FFF C   
5466 O O   . ASN D 77  ? 3.385 4.220 2.188 -0.828 0.291  -0.531 77  ASN FFF O   
5467 C CB  . ASN D 77  ? 3.319 4.181 2.201 -0.864 0.266  -0.547 77  ASN FFF CB  
5468 C CG  . ASN D 77  ? 3.251 4.127 2.167 -0.883 0.246  -0.558 77  ASN FFF CG  
5469 O OD1 . ASN D 77  ? 3.140 4.015 2.046 -0.891 0.230  -0.565 77  ASN FFF OD1 
5470 N ND2 . ASN D 77  ? 3.263 4.150 2.218 -0.890 0.246  -0.560 77  ASN FFF ND2 
5471 N N   . THR D 78  ? 3.282 4.093 2.014 -0.821 0.261  -0.557 78  THR FFF N   
5472 C CA  . THR D 78  ? 3.289 4.081 1.972 -0.797 0.273  -0.550 78  THR FFF CA  
5473 C C   . THR D 78  ? 3.286 4.061 1.926 -0.796 0.250  -0.562 78  THR FFF C   
5474 O O   . THR D 78  ? 3.101 3.870 1.729 -0.802 0.226  -0.578 78  THR FFF O   
5475 C CB  . THR D 78  ? 3.309 4.090 1.966 -0.777 0.285  -0.548 78  THR FFF CB  
5476 O OG1 . THR D 78  ? 3.256 4.054 1.960 -0.781 0.306  -0.536 78  THR FFF OG1 
5477 C CG2 . THR D 78  ? 3.394 4.154 1.998 -0.748 0.299  -0.540 78  THR FFF CG2 
5478 N N   . VAL D 79  ? 3.434 4.201 2.054 -0.787 0.257  -0.554 79  VAL FFF N   
5479 C CA  . VAL D 79  ? 3.574 4.322 2.150 -0.781 0.238  -0.562 79  VAL FFF CA  
5480 C C   . VAL D 79  ? 3.743 4.467 2.263 -0.750 0.249  -0.558 79  VAL FFF C   
5481 O O   . VAL D 79  ? 3.841 4.568 2.362 -0.734 0.278  -0.542 79  VAL FFF O   
5482 C CB  . VAL D 79  ? 3.570 4.328 2.163 -0.794 0.236  -0.557 79  VAL FFF CB  
5483 C CG1 . VAL D 79  ? 3.590 4.354 2.195 -0.785 0.264  -0.537 79  VAL FFF CG1 
5484 C CG2 . VAL D 79  ? 3.537 4.279 2.093 -0.791 0.213  -0.567 79  VAL FFF CG2 
5485 N N   . TYR D 80  ? 3.765 4.466 2.238 -0.740 0.227  -0.573 80  TYR FFF N   
5486 C CA  . TYR D 80  ? 3.693 4.365 2.103 -0.708 0.229  -0.574 80  TYR FFF CA  
5487 C C   . TYR D 80  ? 3.755 4.408 2.128 -0.701 0.214  -0.579 80  TYR FFF C   
5488 O O   . TYR D 80  ? 3.775 4.434 2.165 -0.721 0.190  -0.588 80  TYR FFF O   
5489 C CB  . TYR D 80  ? 3.594 4.252 1.983 -0.701 0.211  -0.590 80  TYR FFF CB  
5490 C CG  . TYR D 80  ? 3.468 4.142 1.892 -0.708 0.225  -0.587 80  TYR FFF CG  
5491 C CD1 . TYR D 80  ? 3.428 4.104 1.847 -0.688 0.255  -0.572 80  TYR FFF CD1 
5492 C CD2 . TYR D 80  ? 3.338 4.027 1.800 -0.733 0.207  -0.598 80  TYR FFF CD2 
5493 C CE1 . TYR D 80  ? 3.343 4.034 1.795 -0.695 0.267  -0.569 80  TYR FFF CE1 
5494 C CE2 . TYR D 80  ? 3.270 3.974 1.764 -0.739 0.218  -0.596 80  TYR FFF CE2 
5495 C CZ  . TYR D 80  ? 3.284 3.989 1.774 -0.721 0.248  -0.582 80  TYR FFF CZ  
5496 O OH  . TYR D 80  ? 3.206 3.926 1.729 -0.728 0.257  -0.580 80  TYR FFF OH  
5497 N N   . LEU D 81  ? 3.841 4.475 2.167 -0.672 0.228  -0.571 81  LEU FFF N   
5498 C CA  . LEU D 81  ? 3.912 4.521 2.189 -0.658 0.209  -0.579 81  LEU FFF CA  
5499 C C   . LEU D 81  ? 4.022 4.596 2.234 -0.624 0.201  -0.588 81  LEU FFF C   
5500 O O   . LEU D 81  ? 4.091 4.658 2.276 -0.596 0.229  -0.576 81  LEU FFF O   
5501 C CB  . LEU D 81  ? 3.885 4.498 2.160 -0.651 0.231  -0.561 81  LEU FFF CB  
5502 C CG  . LEU D 81  ? 3.853 4.442 2.084 -0.641 0.212  -0.569 81  LEU FFF CG  
5503 C CD1 . LEU D 81  ? 3.785 4.385 2.048 -0.672 0.183  -0.580 81  LEU FFF CD1 
5504 C CD2 . LEU D 81  ? 3.858 4.448 2.074 -0.625 0.240  -0.550 81  LEU FFF CD2 
5505 N N   . GLN D 82  ? 4.029 4.584 2.221 -0.626 0.164  -0.609 82  GLN FFF N   
5506 C CA  . GLN D 82  ? 3.973 4.491 2.102 -0.595 0.146  -0.624 82  GLN FFF CA  
5507 C C   . GLN D 82  ? 3.960 4.450 2.037 -0.573 0.135  -0.627 82  GLN FFF C   
5508 O O   . GLN D 82  ? 3.819 4.306 1.906 -0.590 0.107  -0.637 82  GLN FFF O   
5509 C CB  . GLN D 82  ? 3.915 4.425 2.056 -0.610 0.108  -0.645 82  GLN FFF CB  
5510 C CG  . GLN D 82  ? 3.882 4.355 1.965 -0.579 0.087  -0.661 82  GLN FFF CG  
5511 C CD  . GLN D 82  ? 3.873 4.343 1.936 -0.557 0.114  -0.654 82  GLN FFF CD  
5512 O OE1 . GLN D 82  ? 3.818 4.314 1.926 -0.574 0.129  -0.648 82  GLN FFF OE1 
5513 N NE2 . GLN D 82  ? 3.911 4.351 1.908 -0.516 0.121  -0.654 82  GLN FFF NE2 
5514 N N   . MET D 83  ? 4.062 4.535 2.089 -0.538 0.158  -0.617 83  MET FFF N   
5515 C CA  . MET D 83  ? 4.249 4.694 2.220 -0.512 0.153  -0.617 83  MET FFF CA  
5516 C C   . MET D 83  ? 4.477 4.877 2.378 -0.478 0.123  -0.638 83  MET FFF C   
5517 O O   . MET D 83  ? 4.774 5.156 2.625 -0.440 0.142  -0.632 83  MET FFF O   
5518 C CB  . MET D 83  ? 4.194 4.649 2.154 -0.492 0.198  -0.592 83  MET FFF CB  
5519 C CG  . MET D 83  ? 3.994 4.493 2.029 -0.524 0.227  -0.571 83  MET FFF CG  
5520 S SD  . MET D 83  ? 3.805 4.317 1.838 -0.500 0.282  -0.538 83  MET FFF SD  
5521 C CE  . MET D 83  ? 3.861 4.349 1.843 -0.480 0.275  -0.537 83  MET FFF CE  
5522 N N   . ASN D 84  ? 4.451 4.835 2.352 -0.490 0.078  -0.659 84  ASN FFF N   
5523 C CA  . ASN D 84  ? 4.415 4.754 2.258 -0.462 0.040  -0.682 84  ASN FFF CA  
5524 C C   . ASN D 84  ? 4.496 4.803 2.280 -0.435 0.028  -0.686 84  ASN FFF C   
5525 O O   . ASN D 84  ? 4.370 4.693 2.175 -0.450 0.039  -0.675 84  ASN FFF O   
5526 C CB  . ASN D 84  ? 4.290 4.627 2.169 -0.490 -0.004 -0.702 84  ASN FFF CB  
5527 C CG  . ASN D 84  ? 4.157 4.528 2.098 -0.520 0.006  -0.698 84  ASN FFF CG  
5528 O OD1 . ASN D 84  ? 4.141 4.510 2.070 -0.507 0.020  -0.698 84  ASN FFF OD1 
5529 N ND2 . ASN D 84  ? 4.002 4.402 2.007 -0.560 -0.003 -0.696 84  ASN FFF ND2 
5530 N N   . SER D 85  ? 4.575 4.836 2.287 -0.395 0.007  -0.702 85  SER FFF N   
5531 C CA  . SER D 85  ? 4.626 4.851 2.270 -0.359 -0.005 -0.707 85  SER FFF CA  
5532 C C   . SER D 85  ? 4.665 4.909 2.305 -0.352 0.041  -0.681 85  SER FFF C   
5533 O O   . SER D 85  ? 4.715 4.958 2.357 -0.360 0.033  -0.679 85  SER FFF O   
5534 C CB  . SER D 85  ? 4.574 4.780 2.226 -0.374 -0.054 -0.726 85  SER FFF CB  
5535 O OG  . SER D 85  ? 4.472 4.649 2.111 -0.368 -0.097 -0.750 85  SER FFF OG  
5536 N N   . LEU D 86  ? 4.629 4.889 2.265 -0.337 0.086  -0.661 86  LEU FFF N   
5537 C CA  . LEU D 86  ? 4.595 4.875 2.230 -0.327 0.134  -0.632 86  LEU FFF CA  
5538 C C   . LEU D 86  ? 4.624 4.869 2.190 -0.291 0.126  -0.635 86  LEU FFF C   
5539 O O   . LEU D 86  ? 4.896 5.097 2.391 -0.253 0.103  -0.652 86  LEU FFF O   
5540 C CB  . LEU D 86  ? 4.569 4.858 2.193 -0.302 0.177  -0.613 86  LEU FFF CB  
5541 C CG  . LEU D 86  ? 4.472 4.805 2.174 -0.338 0.200  -0.601 86  LEU FFF CG  
5542 C CD1 . LEU D 86  ? 4.521 4.853 2.201 -0.309 0.231  -0.589 86  LEU FFF CD1 
5543 C CD2 . LEU D 86  ? 4.298 4.672 2.064 -0.369 0.229  -0.578 86  LEU FFF CD2 
5544 N N   . LYS D 87  ? 4.539 4.801 2.124 -0.303 0.145  -0.619 87  LYS FFF N   
5545 C CA  . LYS D 87  ? 4.628 4.861 2.152 -0.271 0.141  -0.619 87  LYS FFF CA  
5546 C C   . LYS D 87  ? 4.640 4.893 2.160 -0.253 0.195  -0.586 87  LYS FFF C   
5547 O O   . LYS D 87  ? 4.444 4.737 2.025 -0.277 0.230  -0.565 87  LYS FFF O   
5548 C CB  . LYS D 87  ? 4.634 4.870 2.186 -0.302 0.109  -0.630 87  LYS FFF CB  
5549 C CG  . LYS D 87  ? 4.740 4.948 2.284 -0.311 0.051  -0.661 87  LYS FFF CG  
5550 C CD  . LYS D 87  ? 4.772 4.970 2.321 -0.326 0.019  -0.671 87  LYS FFF CD  
5551 C CE  . LYS D 87  ? 4.646 4.890 2.279 -0.377 0.029  -0.659 87  LYS FFF CE  
5552 N NZ  . LYS D 87  ? 4.638 4.873 2.283 -0.396 -0.009 -0.672 87  LYS FFF NZ  
5553 N N   . TYR D 88  ? 4.835 5.057 2.284 -0.211 0.201  -0.582 88  TYR FFF N   
5554 C CA  . TYR D 88  ? 4.829 5.064 2.266 -0.187 0.252  -0.550 88  TYR FFF CA  
5555 C C   . TYR D 88  ? 4.679 4.958 2.196 -0.234 0.269  -0.533 88  TYR FFF C   
5556 O O   . TYR D 88  ? 4.585 4.896 2.143 -0.239 0.314  -0.504 88  TYR FFF O   
5557 C CB  . TYR D 88  ? 4.883 5.075 2.228 -0.136 0.246  -0.553 88  TYR FFF CB  
5558 C CG  . TYR D 88  ? 4.931 5.121 2.233 -0.088 0.296  -0.525 88  TYR FFF CG  
5559 C CD1 . TYR D 88  ? 4.891 5.121 2.242 -0.098 0.348  -0.489 88  TYR FFF CD1 
5560 C CD2 . TYR D 88  ? 5.070 5.217 2.282 -0.032 0.291  -0.533 88  TYR FFF CD2 
5561 C CE1 . TYR D 88  ? 4.978 5.207 2.293 -0.052 0.395  -0.459 88  TYR FFF CE1 
5562 C CE2 . TYR D 88  ? 5.110 5.255 2.279 0.016  0.339  -0.505 88  TYR FFF CE2 
5563 C CZ  . TYR D 88  ? 5.071 5.257 2.293 0.005  0.392  -0.467 88  TYR FFF CZ  
5564 O OH  . TYR D 88  ? 5.021 5.204 2.202 0.055  0.439  -0.437 88  TYR FFF OH  
5565 N N   . GLU D 89  ? 4.599 4.880 2.146 -0.269 0.232  -0.551 89  GLU FFF N   
5566 C CA  A GLU D 89  ? 4.665 4.983 2.283 -0.312 0.242  -0.538 89  GLU FFF CA  
5567 C CA  B GLU D 89  ? 4.524 4.841 2.142 -0.312 0.241  -0.539 89  GLU FFF CA  
5568 C C   . GLU D 89  ? 4.612 4.972 2.315 -0.355 0.253  -0.532 89  GLU FFF C   
5569 O O   . GLU D 89  ? 4.396 4.788 2.163 -0.393 0.258  -0.523 89  GLU FFF O   
5570 C CB  A GLU D 89  ? 4.686 4.988 2.297 -0.328 0.198  -0.560 89  GLU FFF CB  
5571 C CB  B GLU D 89  ? 4.366 4.669 1.983 -0.332 0.196  -0.561 89  GLU FFF CB  
5572 C CG  A GLU D 89  ? 4.650 4.953 2.296 -0.361 0.155  -0.585 89  GLU FFF CG  
5573 C CG  B GLU D 89  ? 4.265 4.532 1.809 -0.296 0.186  -0.566 89  GLU FFF CG  
5574 C CD  A GLU D 89  ? 4.627 4.912 2.267 -0.375 0.112  -0.604 89  GLU FFF CD  
5575 C CD  B GLU D 89  ? 4.208 4.426 1.672 -0.254 0.155  -0.588 89  GLU FFF CD  
5576 O OE1 A GLU D 89  ? 4.677 4.923 2.250 -0.341 0.094  -0.614 89  GLU FFF OE1 
5577 O OE1 B GLU D 89  ? 4.121 4.333 1.588 -0.255 0.141  -0.601 89  GLU FFF OE1 
5578 O OE2 A GLU D 89  ? 4.524 4.834 2.227 -0.418 0.095  -0.609 89  GLU FFF OE2 
5579 O OE2 B GLU D 89  ? 4.162 4.346 1.561 -0.220 0.145  -0.593 89  GLU FFF OE2 
5580 N N   . ASP D 90  ? 4.735 5.096 2.441 -0.350 0.256  -0.535 90  ASP FFF N   
5581 C CA  . ASP D 90  ? 4.623 5.023 2.406 -0.386 0.271  -0.527 90  ASP FFF CA  
5582 C C   . ASP D 90  ? 4.656 5.079 2.459 -0.372 0.323  -0.495 90  ASP FFF C   
5583 O O   . ASP D 90  ? 4.598 5.055 2.469 -0.402 0.338  -0.486 90  ASP FFF O   
5584 C CB  . ASP D 90  ? 4.645 5.036 2.428 -0.392 0.244  -0.549 90  ASP FFF CB  
5585 C CG  . ASP D 90  ? 4.629 5.004 2.412 -0.412 0.192  -0.578 90  ASP FFF CG  
5586 O OD1 . ASP D 90  ? 4.504 4.893 2.322 -0.442 0.179  -0.580 90  ASP FFF OD1 
5587 O OD2 . ASP D 90  ? 4.726 5.075 2.476 -0.398 0.166  -0.598 90  ASP FFF OD2 
5588 N N   . THR D 91  ? 4.833 5.238 2.579 -0.327 0.350  -0.479 91  THR FFF N   
5589 C CA  . THR D 91  ? 4.836 5.261 2.597 -0.307 0.403  -0.445 91  THR FFF CA  
5590 C C   . THR D 91  ? 4.813 5.278 2.655 -0.343 0.425  -0.423 91  THR FFF C   
5591 O O   . THR D 91  ? 4.936 5.398 2.772 -0.347 0.422  -0.420 91  THR FFF O   
5592 C CB  . THR D 91  ? 4.785 5.181 2.466 -0.249 0.426  -0.431 91  THR FFF CB  
5593 O OG1 . THR D 91  ? 4.742 5.101 2.350 -0.214 0.407  -0.451 91  THR FFF OG1 
5594 C CG2 . THR D 91  ? 4.678 5.096 2.381 -0.229 0.482  -0.392 91  THR FFF CG2 
5595 N N   . ALA D 92  ? 4.700 5.199 2.614 -0.369 0.445  -0.409 92  ALA FFF N   
5596 C CA  . ALA D 92  ? 4.610 5.147 2.609 -0.408 0.459  -0.393 92  ALA FFF CA  
5597 C C   . ALA D 92  ? 4.564 5.132 2.631 -0.427 0.477  -0.381 92  ALA FFF C   
5598 O O   . ALA D 92  ? 4.557 5.116 2.606 -0.417 0.472  -0.391 92  ALA FFF O   
5599 C CB  . ALA D 92  ? 4.574 5.114 2.595 -0.446 0.419  -0.417 92  ALA FFF CB  
5600 N N   . VAL D 93  ? 4.517 5.118 2.660 -0.454 0.496  -0.362 93  VAL FFF N   
5601 C CA  . VAL D 93  ? 4.403 5.035 2.626 -0.484 0.505  -0.355 93  VAL FFF CA  
5602 C C   . VAL D 93  ? 4.316 4.955 2.570 -0.526 0.465  -0.383 93  VAL FFF C   
5603 O O   . VAL D 93  ? 4.305 4.947 2.569 -0.544 0.449  -0.389 93  VAL FFF O   
5604 C CB  . VAL D 93  ? 4.319 4.979 2.608 -0.491 0.540  -0.321 93  VAL FFF CB  
5605 C CG1 . VAL D 93  ? 4.210 4.901 2.582 -0.520 0.546  -0.314 93  VAL FFF CG1 
5606 C CG2 . VAL D 93  ? 4.353 5.007 2.612 -0.448 0.581  -0.290 93  VAL FFF CG2 
5607 N N   . TYR D 94  ? 4.235 4.878 2.504 -0.539 0.449  -0.399 94  TYR FFF N   
5608 C CA  . TYR D 94  ? 4.134 4.785 2.432 -0.577 0.413  -0.425 94  TYR FFF CA  
5609 C C   . TYR D 94  ? 4.134 4.819 2.518 -0.609 0.422  -0.415 94  TYR FFF C   
5610 O O   . TYR D 94  ? 4.257 4.952 2.665 -0.602 0.444  -0.402 94  TYR FFF O   
5611 C CB  . TYR D 94  ? 4.076 4.707 2.333 -0.570 0.387  -0.449 94  TYR FFF CB  
5612 C CG  . TYR D 94  ? 4.137 4.733 2.318 -0.548 0.364  -0.466 94  TYR FFF CG  
5613 C CD1 . TYR D 94  ? 4.177 4.750 2.297 -0.506 0.382  -0.455 94  TYR FFF CD1 
5614 C CD2 . TYR D 94  ? 4.102 4.689 2.276 -0.567 0.325  -0.491 94  TYR FFF CD2 
5615 C CE1 . TYR D 94  ? 4.198 4.737 2.248 -0.484 0.359  -0.472 94  TYR FFF CE1 
5616 C CE2 . TYR D 94  ? 4.180 4.735 2.290 -0.547 0.301  -0.506 94  TYR FFF CE2 
5617 C CZ  . TYR D 94  ? 4.158 4.688 2.205 -0.506 0.317  -0.497 94  TYR FFF CZ  
5618 O OH  . TYR D 94  ? 4.191 4.686 2.173 -0.485 0.291  -0.514 94  TYR FFF OH  
5619 N N   . TYR D 95  ? 4.034 4.733 2.458 -0.640 0.404  -0.422 95  TYR FFF N   
5620 C CA  . TYR D 95  ? 3.782 4.511 2.286 -0.671 0.407  -0.417 95  TYR FFF CA  
5621 C C   . TYR D 95  ? 3.681 4.414 2.200 -0.699 0.373  -0.443 95  TYR FFF C   
5622 O O   . TYR D 95  ? 3.592 4.313 2.081 -0.705 0.346  -0.460 95  TYR FFF O   
5623 C CB  . TYR D 95  ? 3.700 4.442 2.240 -0.684 0.414  -0.403 95  TYR FFF CB  
5624 C CG  . TYR D 95  ? 3.707 4.447 2.241 -0.658 0.449  -0.374 95  TYR FFF CG  
5625 C CD1 . TYR D 95  ? 3.683 4.443 2.273 -0.657 0.479  -0.349 95  TYR FFF CD1 
5626 C CD2 . TYR D 95  ? 3.783 4.503 2.256 -0.634 0.453  -0.372 95  TYR FFF CD2 
5627 C CE1 . TYR D 95  ? 3.799 4.559 2.386 -0.632 0.513  -0.320 95  TYR FFF CE1 
5628 C CE2 . TYR D 95  ? 3.836 4.555 2.302 -0.608 0.487  -0.344 95  TYR FFF CE2 
5629 C CZ  . TYR D 95  ? 3.864 4.604 2.388 -0.607 0.517  -0.317 95  TYR FFF CZ  
5630 O OH  . TYR D 95  ? 3.948 4.687 2.466 -0.580 0.552  -0.287 95  TYR FFF OH  
5631 N N   A CYS D 96  ? 3.640 4.390 2.206 -0.715 0.373  -0.444 96  CYS FFF N   
5632 N N   B CYS D 96  ? 3.654 4.405 2.222 -0.715 0.373  -0.443 96  CYS FFF N   
5633 C CA  A CYS D 96  ? 3.592 4.352 2.187 -0.743 0.345  -0.464 96  CYS FFF CA  
5634 C CA  B CYS D 96  ? 3.616 4.377 2.211 -0.743 0.345  -0.464 96  CYS FFF CA  
5635 C C   A CYS D 96  ? 3.550 4.332 2.206 -0.767 0.345  -0.457 96  CYS FFF C   
5636 C C   B CYS D 96  ? 3.575 4.358 2.233 -0.768 0.345  -0.457 96  CYS FFF C   
5637 O O   A CYS D 96  ? 3.500 4.293 2.191 -0.764 0.369  -0.436 96  CYS FFF O   
5638 O O   B CYS D 96  ? 3.556 4.351 2.252 -0.765 0.369  -0.437 96  CYS FFF O   
5639 C CB  A CYS D 96  ? 3.565 4.329 2.171 -0.745 0.343  -0.471 96  CYS FFF CB  
5640 C CB  B CYS D 96  ? 3.605 4.369 2.209 -0.744 0.344  -0.471 96  CYS FFF CB  
5641 S SG  A CYS D 96  ? 3.502 4.288 2.171 -0.745 0.374  -0.449 96  CYS FFF SG  
5642 S SG  B CYS D 96  ? 3.542 4.310 2.157 -0.770 0.307  -0.498 96  CYS FFF SG  
5643 N N   . ALA D 97  ? 3.572 4.359 2.239 -0.789 0.318  -0.474 97  ALA FFF N   
5644 C CA  . ALA D 97  ? 3.521 4.327 2.242 -0.812 0.312  -0.472 97  ALA FFF CA  
5645 C C   . ALA D 97  ? 3.415 4.230 2.157 -0.832 0.287  -0.491 97  ALA FFF C   
5646 O O   . ALA D 97  ? 3.237 4.042 1.945 -0.831 0.270  -0.506 97  ALA FFF O   
5647 C CB  . ALA D 97  ? 3.540 4.341 2.245 -0.813 0.307  -0.470 97  ALA FFF CB  
5648 N N   . GLN D 98  ? 3.395 4.227 2.192 -0.849 0.285  -0.488 98  GLN FFF N   
5649 C CA  . GLN D 98  ? 3.277 4.120 2.100 -0.866 0.264  -0.504 98  GLN FFF CA  
5650 C C   . GLN D 98  ? 3.154 4.006 2.005 -0.881 0.251  -0.506 98  GLN FFF C   
5651 O O   . GLN D 98  ? 3.009 3.865 1.885 -0.880 0.263  -0.492 98  GLN FFF O   
5652 C CB  . GLN D 98  ? 3.243 4.096 2.106 -0.868 0.274  -0.500 98  GLN FFF CB  
5653 C CG  . GLN D 98  ? 3.169 4.031 2.052 -0.883 0.253  -0.516 98  GLN FFF CG  
5654 C CD  . GLN D 98  ? 3.157 4.032 2.090 -0.897 0.245  -0.516 98  GLN FFF CD  
5655 O OE1 . GLN D 98  ? 3.214 4.091 2.161 -0.899 0.247  -0.508 98  GLN FFF OE1 
5656 N NE2 . GLN D 98  ? 3.133 4.017 2.094 -0.906 0.234  -0.525 98  GLN FFF NE2 
5657 N N   . THR D 99  ? 3.153 4.008 1.999 -0.892 0.228  -0.521 99  THR FFF N   
5658 C CA  . THR D 99  ? 3.199 4.063 2.069 -0.905 0.214  -0.525 99  THR FFF CA  
5659 C C   . THR D 99  ? 3.216 4.089 2.102 -0.915 0.196  -0.539 99  THR FFF C   
5660 O O   . THR D 99  ? 3.371 4.241 2.237 -0.913 0.190  -0.547 99  THR FFF O   
5661 C CB  . THR D 99  ? 3.180 4.037 2.017 -0.904 0.205  -0.527 99  THR FFF CB  
5662 O OG1 . THR D 99  ? 3.133 3.999 1.996 -0.914 0.193  -0.529 99  THR FFF OG1 
5663 C CG2 . THR D 99  ? 3.146 3.995 1.943 -0.902 0.190  -0.538 99  THR FFF CG2 
5664 N N   . HIS D 100 ? 3.108 3.990 2.031 -0.923 0.187  -0.541 100 HIS FFF N   
5665 C CA  . HIS D 100 ? 2.973 3.864 1.909 -0.931 0.169  -0.554 100 HIS FFF CA  
5666 C C   . HIS D 100 ? 2.917 3.809 1.835 -0.934 0.153  -0.560 100 HIS FFF C   
5667 O O   . HIS D 100 ? 3.084 3.982 2.009 -0.938 0.138  -0.569 100 HIS FFF O   
5668 C CB  . HIS D 100 ? 2.948 3.847 1.933 -0.935 0.168  -0.554 100 HIS FFF CB  
5669 C CG  . HIS D 100 ? 2.930 3.829 1.945 -0.936 0.170  -0.546 100 HIS FFF CG  
5670 N ND1 . HIS D 100 ? 2.904 3.802 1.946 -0.934 0.188  -0.532 100 HIS FFF ND1 
5671 C CD2 . HIS D 100 ? 2.923 3.824 1.948 -0.940 0.157  -0.550 100 HIS FFF CD2 
5672 C CE1 . HIS D 100 ? 2.892 3.792 1.963 -0.936 0.185  -0.527 100 HIS FFF CE1 
5673 N NE2 . HIS D 100 ? 2.917 3.818 1.976 -0.940 0.165  -0.539 100 HIS FFF NE2 
5674 N N   . TYR D 101 ? 2.822 3.707 1.718 -0.931 0.156  -0.554 101 TYR FFF N   
5675 C CA  . TYR D 101 ? 2.754 3.639 1.628 -0.933 0.143  -0.557 101 TYR FFF CA  
5676 C C   . TYR D 101 ? 2.687 3.571 1.534 -0.933 0.132  -0.564 101 TYR FFF C   
5677 O O   . TYR D 101 ? 2.604 3.479 1.428 -0.928 0.138  -0.563 101 TYR FFF O   
5678 C CB  . TYR D 101 ? 2.774 3.651 1.629 -0.930 0.150  -0.549 101 TYR FFF CB  
5679 C CG  . TYR D 101 ? 2.720 3.597 1.558 -0.932 0.136  -0.551 101 TYR FFF CG  
5680 C CD1 . TYR D 101 ? 2.643 3.530 1.501 -0.936 0.125  -0.555 101 TYR FFF CD1 
5681 C CD2 . TYR D 101 ? 2.743 3.612 1.547 -0.928 0.135  -0.549 101 TYR FFF CD2 
5682 C CE1 . TYR D 101 ? 2.577 3.465 1.420 -0.937 0.114  -0.556 101 TYR FFF CE1 
5683 C CE2 . TYR D 101 ? 2.669 3.539 1.461 -0.931 0.123  -0.550 101 TYR FFF CE2 
5684 C CZ  . TYR D 101 ? 2.552 3.432 1.363 -0.935 0.113  -0.553 101 TYR FFF CZ  
5685 O OH  . TYR D 101 ? 2.470 3.353 1.271 -0.936 0.103  -0.552 101 TYR FFF OH  
5686 N N   . VAL D 102 ? 2.735 3.627 1.585 -0.937 0.117  -0.570 102 VAL FFF N   
5687 C CA  . VAL D 102 ? 2.760 3.652 1.590 -0.937 0.105  -0.574 102 VAL FFF CA  
5688 C C   . VAL D 102 ? 2.825 3.717 1.640 -0.938 0.097  -0.570 102 VAL FFF C   
5689 O O   . VAL D 102 ? 2.777 3.677 1.605 -0.939 0.091  -0.570 102 VAL FFF O   
5690 C CB  . VAL D 102 ? 2.697 3.601 1.544 -0.940 0.096  -0.580 102 VAL FFF CB  
5691 C CG1 . VAL D 102 ? 2.657 3.563 1.490 -0.940 0.084  -0.581 102 VAL FFF CG1 
5692 C CG2 . VAL D 102 ? 2.659 3.563 1.520 -0.940 0.103  -0.584 102 VAL FFF CG2 
5693 N N   . SER D 103 ? 2.924 3.805 1.712 -0.935 0.096  -0.568 103 SER FFF N   
5694 C CA  . SER D 103 ? 2.925 3.807 1.699 -0.936 0.085  -0.565 103 SER FFF CA  
5695 C C   . SER D 103 ? 2.948 3.830 1.716 -0.937 0.072  -0.567 103 SER FFF C   
5696 O O   . SER D 103 ? 2.867 3.742 1.628 -0.935 0.073  -0.571 103 SER FFF O   
5697 C CB  . SER D 103 ? 2.934 3.802 1.684 -0.932 0.089  -0.560 103 SER FFF CB  
5698 O OG  . SER D 103 ? 2.908 3.775 1.645 -0.933 0.077  -0.558 103 SER FFF OG  
5699 N N   . TYR D 104 ? 3.023 3.914 1.796 -0.939 0.061  -0.564 104 TYR FFF N   
5700 C CA  . TYR D 104 ? 3.088 3.982 1.862 -0.940 0.047  -0.563 104 TYR FFF CA  
5701 C C   . TYR D 104 ? 3.077 3.953 1.828 -0.938 0.041  -0.563 104 TYR FFF C   
5702 O O   . TYR D 104 ? 3.030 3.903 1.782 -0.939 0.029  -0.564 104 TYR FFF O   
5703 C CB  . TYR D 104 ? 3.183 4.092 1.971 -0.941 0.039  -0.556 104 TYR FFF CB  
5704 C CG  . TYR D 104 ? 3.154 4.059 1.931 -0.940 0.036  -0.550 104 TYR FFF CG  
5705 C CD1 . TYR D 104 ? 3.118 4.026 1.894 -0.939 0.044  -0.549 104 TYR FFF CD1 
5706 C CD2 . TYR D 104 ? 3.150 4.049 1.919 -0.941 0.025  -0.545 104 TYR FFF CD2 
5707 C CE1 . TYR D 104 ? 3.106 4.012 1.873 -0.938 0.041  -0.543 104 TYR FFF CE1 
5708 C CE2 . TYR D 104 ? 3.158 4.054 1.918 -0.941 0.022  -0.540 104 TYR FFF CE2 
5709 C CZ  . TYR D 104 ? 3.145 4.045 1.903 -0.939 0.031  -0.539 104 TYR FFF CZ  
5710 O OH  . TYR D 104 ? 3.151 4.049 1.900 -0.939 0.029  -0.533 104 TYR FFF OH  
5711 N N   . LEU D 105 ? 3.120 3.985 1.852 -0.935 0.047  -0.562 105 LEU FFF N   
5712 C CA  . LEU D 105 ? 3.202 4.049 1.908 -0.931 0.040  -0.563 105 LEU FFF CA  
5713 C C   . LEU D 105 ? 3.129 3.959 1.812 -0.923 0.051  -0.567 105 LEU FFF C   
5714 O O   . LEU D 105 ? 3.031 3.859 1.708 -0.920 0.066  -0.564 105 LEU FFF O   
5715 C CB  . LEU D 105 ? 3.310 4.157 2.009 -0.931 0.039  -0.557 105 LEU FFF CB  
5716 C CG  . LEU D 105 ? 3.487 4.315 2.161 -0.927 0.027  -0.556 105 LEU FFF CG  
5717 C CD1 . LEU D 105 ? 3.468 4.297 2.153 -0.930 0.007  -0.556 105 LEU FFF CD1 
5718 C CD2 . LEU D 105 ? 3.552 4.382 2.220 -0.927 0.030  -0.550 105 LEU FFF CD2 
5719 N N   . LEU D 106 ? 3.117 3.935 1.788 -0.919 0.044  -0.573 106 LEU FFF N   
5720 C CA  . LEU D 106 ? 3.201 4.004 1.850 -0.909 0.054  -0.578 106 LEU FFF CA  
5721 C C   . LEU D 106 ? 3.438 4.224 2.056 -0.899 0.062  -0.575 106 LEU FFF C   
5722 O O   . LEU D 106 ? 3.708 4.490 2.317 -0.891 0.081  -0.573 106 LEU FFF O   
5723 C CB  . LEU D 106 ? 3.109 3.900 1.749 -0.905 0.039  -0.585 106 LEU FFF CB  
5724 C CG  . LEU D 106 ? 3.052 3.829 1.670 -0.894 0.049  -0.590 106 LEU FFF CG  
5725 C CD1 . LEU D 106 ? 3.007 3.800 1.650 -0.899 0.066  -0.589 106 LEU FFF CD1 
5726 C CD2 . LEU D 106 ? 3.048 3.809 1.653 -0.889 0.029  -0.599 106 LEU FFF CD2 
5727 N N   . SER D 107 ? 3.468 4.246 2.072 -0.898 0.050  -0.574 107 SER FFF N   
5728 C CA  . SER D 107 ? 3.407 4.168 1.978 -0.887 0.055  -0.571 107 SER FFF CA  
5729 C C   . SER D 107 ? 3.446 4.216 2.025 -0.887 0.078  -0.563 107 SER FFF C   
5730 O O   . SER D 107 ? 3.438 4.194 1.990 -0.875 0.090  -0.559 107 SER FFF O   
5731 C CB  . SER D 107 ? 3.345 4.098 1.907 -0.888 0.035  -0.571 107 SER FFF CB  
5732 O OG  . SER D 107 ? 3.178 3.951 1.768 -0.901 0.034  -0.565 107 SER FFF OG  
5733 N N   . ASP D 108 ? 3.406 4.198 2.020 -0.899 0.083  -0.559 108 ASP FFF N   
5734 C CA  . ASP D 108 ? 3.374 4.175 2.004 -0.901 0.101  -0.552 108 ASP FFF CA  
5735 C C   . ASP D 108 ? 3.512 4.309 2.140 -0.893 0.121  -0.549 108 ASP FFF C   
5736 O O   . ASP D 108 ? 3.639 4.438 2.274 -0.891 0.137  -0.541 108 ASP FFF O   
5737 C CB  . ASP D 108 ? 3.282 4.104 1.948 -0.913 0.098  -0.551 108 ASP FFF CB  
5738 C CG  . ASP D 108 ? 3.296 4.123 1.963 -0.919 0.084  -0.550 108 ASP FFF CG  
5739 O OD1 . ASP D 108 ? 3.241 4.056 1.884 -0.914 0.078  -0.548 108 ASP FFF OD1 
5740 O OD2 . ASP D 108 ? 3.319 4.163 2.011 -0.926 0.079  -0.550 108 ASP FFF OD2 
5741 N N   . TYR D 109 ? 3.631 4.423 2.254 -0.888 0.122  -0.554 109 TYR FFF N   
5742 C CA  . TYR D 109 ? 3.700 4.489 2.323 -0.880 0.142  -0.550 109 TYR FFF CA  
5743 C C   . TYR D 109 ? 3.649 4.419 2.233 -0.862 0.153  -0.544 109 TYR FFF C   
5744 O O   . TYR D 109 ? 3.620 4.389 2.206 -0.852 0.175  -0.536 109 TYR FFF O   
5745 C CB  . TYR D 109 ? 3.795 4.586 2.425 -0.880 0.139  -0.557 109 TYR FFF CB  
5746 C CG  . TYR D 109 ? 3.869 4.680 2.539 -0.894 0.134  -0.560 109 TYR FFF CG  
5747 C CD1 . TYR D 109 ? 3.776 4.601 2.480 -0.900 0.148  -0.554 109 TYR FFF CD1 
5748 C CD2 . TYR D 109 ? 3.928 4.744 2.604 -0.902 0.116  -0.568 109 TYR FFF CD2 
5749 C CE1 . TYR D 109 ? 3.702 4.543 2.439 -0.911 0.141  -0.557 109 TYR FFF CE1 
5750 C CE2 . TYR D 109 ? 3.873 4.707 2.583 -0.913 0.112  -0.570 109 TYR FFF CE2 
5751 C CZ  . TYR D 109 ? 3.734 4.580 2.473 -0.917 0.124  -0.566 109 TYR FFF CZ  
5752 O OH  . TYR D 109 ? 3.544 4.405 2.312 -0.925 0.118  -0.569 109 TYR FFF OH  
5753 N N   . ALA D 110 ? 3.644 4.400 2.197 -0.857 0.140  -0.548 110 ALA FFF N   
5754 C CA  . ALA D 110 ? 3.732 4.467 2.243 -0.838 0.148  -0.543 110 ALA FFF CA  
5755 C C   . ALA D 110 ? 3.757 4.500 2.280 -0.839 0.166  -0.530 110 ALA FFF C   
5756 O O   . ALA D 110 ? 3.836 4.565 2.333 -0.822 0.183  -0.522 110 ALA FFF O   
5757 C CB  . ALA D 110 ? 3.719 4.435 2.196 -0.833 0.124  -0.552 110 ALA FFF CB  
5758 N N   . THR D 111 ? 3.618 4.379 2.177 -0.856 0.161  -0.529 111 THR FFF N   
5759 C CA  . THR D 111 ? 3.526 4.293 2.099 -0.859 0.173  -0.518 111 THR FFF CA  
5760 C C   . THR D 111 ? 3.442 4.229 2.064 -0.869 0.187  -0.511 111 THR FFF C   
5761 O O   . THR D 111 ? 3.512 4.303 2.149 -0.867 0.201  -0.499 111 THR FFF O   
5762 C CB  . THR D 111 ? 3.416 4.186 1.987 -0.868 0.154  -0.522 111 THR FFF CB  
5763 O OG1 . THR D 111 ? 3.329 4.116 1.933 -0.884 0.142  -0.527 111 THR FFF OG1 
5764 C CG2 . THR D 111 ? 3.375 4.126 1.906 -0.861 0.137  -0.529 111 THR FFF CG2 
5765 N N   . TRP D 112 ? 3.302 4.099 1.949 -0.877 0.181  -0.517 112 TRP FFF N   
5766 C CA  . TRP D 112 ? 3.193 4.007 1.888 -0.886 0.190  -0.513 112 TRP FFF CA  
5767 C C   . TRP D 112 ? 3.070 3.883 1.776 -0.876 0.215  -0.500 112 TRP FFF C   
5768 O O   . TRP D 112 ? 2.974 3.777 1.656 -0.863 0.225  -0.498 112 TRP FFF O   
5769 C CB  . TRP D 112 ? 3.206 4.029 1.918 -0.894 0.179  -0.524 112 TRP FFF CB  
5770 C CG  . TRP D 112 ? 3.093 3.932 1.853 -0.904 0.180  -0.523 112 TRP FFF CG  
5771 C CD1 . TRP D 112 ? 3.073 3.918 1.860 -0.904 0.190  -0.521 112 TRP FFF CD1 
5772 C CD2 . TRP D 112 ? 2.961 3.810 1.745 -0.914 0.171  -0.524 112 TRP FFF CD2 
5773 N NE1 . TRP D 112 ? 2.965 3.822 1.793 -0.914 0.186  -0.521 112 TRP FFF NE1 
5774 C CE2 . TRP D 112 ? 2.954 3.813 1.780 -0.919 0.174  -0.524 112 TRP FFF CE2 
5775 C CE3 . TRP D 112 ? 2.945 3.795 1.720 -0.918 0.159  -0.526 112 TRP FFF CE3 
5776 C CZ2 . TRP D 112 ? 3.008 3.876 1.864 -0.926 0.164  -0.526 112 TRP FFF CZ2 
5777 C CZ3 . TRP D 112 ? 3.006 3.866 1.810 -0.925 0.151  -0.527 112 TRP FFF CZ3 
5778 C CH2 . TRP D 112 ? 3.039 3.907 1.882 -0.928 0.153  -0.528 112 TRP FFF CH2 
5779 N N   . PRO D 113 ? 3.058 3.880 1.801 -0.881 0.226  -0.489 113 PRO FFF N   
5780 C CA  . PRO D 113 ? 3.098 3.924 1.868 -0.874 0.249  -0.475 113 PRO FFF CA  
5781 C C   . PRO D 113 ? 3.082 3.918 1.886 -0.881 0.246  -0.480 113 PRO FFF C   
5782 O O   . PRO D 113 ? 3.282 4.129 2.116 -0.895 0.231  -0.488 113 PRO FFF O   
5783 C CB  . PRO D 113 ? 3.084 3.917 1.888 -0.878 0.255  -0.463 113 PRO FFF CB  
5784 C CG  . PRO D 113 ? 3.054 3.892 1.862 -0.892 0.232  -0.475 113 PRO FFF CG  
5785 C CD  . PRO D 113 ? 3.067 3.897 1.831 -0.891 0.216  -0.490 113 PRO FFF CD  
5786 N N   . TYR D 114 ? 3.101 3.934 1.900 -0.872 0.260  -0.476 114 TYR FFF N   
5787 C CA  . TYR D 114 ? 3.052 3.893 1.876 -0.877 0.258  -0.482 114 TYR FFF CA  
5788 C C   . TYR D 114 ? 3.046 3.900 1.930 -0.882 0.269  -0.470 114 TYR FFF C   
5789 O O   . TYR D 114 ? 3.054 3.910 1.959 -0.882 0.278  -0.457 114 TYR FFF O   
5790 C CB  . TYR D 114 ? 3.020 3.851 1.809 -0.862 0.268  -0.482 114 TYR FFF CB  
5791 C CG  . TYR D 114 ? 2.975 3.793 1.715 -0.860 0.249  -0.498 114 TYR FFF CG  
5792 C CD1 . TYR D 114 ? 3.011 3.819 1.715 -0.857 0.240  -0.501 114 TYR FFF CD1 
5793 C CD2 . TYR D 114 ? 2.968 3.786 1.701 -0.861 0.240  -0.509 114 TYR FFF CD2 
5794 C CE1 . TYR D 114 ? 2.989 3.785 1.653 -0.855 0.221  -0.514 114 TYR FFF CE1 
5795 C CE2 . TYR D 114 ? 2.957 3.764 1.651 -0.859 0.222  -0.522 114 TYR FFF CE2 
5796 C CZ  . TYR D 114 ? 2.939 3.734 1.599 -0.856 0.212  -0.525 114 TYR FFF CZ  
5797 O OH  . TYR D 114 ? 2.829 3.612 1.456 -0.854 0.192  -0.537 114 TYR FFF OH  
5798 N N   . ASP D 115 ? 3.051 3.913 1.964 -0.887 0.268  -0.474 115 ASP FFF N   
5799 C CA  . ASP D 115 ? 3.153 4.026 2.129 -0.894 0.272  -0.466 115 ASP FFF CA  
5800 C C   . ASP D 115 ? 3.173 4.047 2.168 -0.883 0.299  -0.447 115 ASP FFF C   
5801 O O   . ASP D 115 ? 3.163 4.043 2.203 -0.883 0.311  -0.431 115 ASP FFF O   
5802 C CB  . ASP D 115 ? 3.257 4.138 2.256 -0.906 0.253  -0.482 115 ASP FFF CB  
5803 C CG  . ASP D 115 ? 3.335 4.216 2.324 -0.916 0.227  -0.499 115 ASP FFF CG  
5804 O OD1 . ASP D 115 ? 3.405 4.288 2.407 -0.919 0.223  -0.495 115 ASP FFF OD1 
5805 O OD2 . ASP D 115 ? 3.379 4.261 2.349 -0.919 0.213  -0.513 115 ASP FFF OD2 
5806 N N   . TYR D 116 ? 3.286 4.155 2.250 -0.872 0.308  -0.448 116 TYR FFF N   
5807 C CA  . TYR D 116 ? 3.440 4.311 2.418 -0.858 0.336  -0.430 116 TYR FFF CA  
5808 C C   . TYR D 116 ? 3.531 4.386 2.444 -0.838 0.349  -0.427 116 TYR FFF C   
5809 O O   . TYR D 116 ? 3.660 4.504 2.523 -0.838 0.332  -0.444 116 TYR FFF O   
5810 C CB  . TYR D 116 ? 3.443 4.323 2.458 -0.865 0.332  -0.435 116 TYR FFF CB  
5811 C CG  . TYR D 116 ? 3.403 4.294 2.478 -0.883 0.316  -0.439 116 TYR FFF CG  
5812 C CD1 . TYR D 116 ? 3.409 4.308 2.545 -0.885 0.327  -0.421 116 TYR FFF CD1 
5813 C CD2 . TYR D 116 ? 3.408 4.300 2.478 -0.897 0.288  -0.461 116 TYR FFF CD2 
5814 C CE1 . TYR D 116 ? 3.400 4.306 2.589 -0.900 0.309  -0.427 116 TYR FFF CE1 
5815 C CE2 . TYR D 116 ? 3.394 4.294 2.514 -0.910 0.272  -0.467 116 TYR FFF CE2 
5816 C CZ  . TYR D 116 ? 3.403 4.309 2.583 -0.911 0.280  -0.451 116 TYR FFF CZ  
5817 O OH  . TYR D 116 ? 3.400 4.310 2.627 -0.923 0.261  -0.458 116 TYR FFF OH  
5818 N N   . TRP D 117 ? 3.545 4.399 2.460 -0.820 0.378  -0.405 117 TRP FFF N   
5819 C CA  . TRP D 117 ? 3.597 4.435 2.449 -0.795 0.394  -0.398 117 TRP FFF CA  
5820 C C   . TRP D 117 ? 3.681 4.520 2.538 -0.777 0.420  -0.382 117 TRP FFF C   
5821 O O   . TRP D 117 ? 3.793 4.647 2.711 -0.780 0.436  -0.364 117 TRP FFF O   
5822 C CB  . TRP D 117 ? 3.591 4.425 2.434 -0.787 0.406  -0.383 117 TRP FFF CB  
5823 C CG  . TRP D 117 ? 3.553 4.381 2.374 -0.799 0.381  -0.399 117 TRP FFF CG  
5824 C CD1 . TRP D 117 ? 3.455 4.293 2.314 -0.821 0.363  -0.406 117 TRP FFF CD1 
5825 C CD2 . TRP D 117 ? 3.563 4.374 2.317 -0.789 0.370  -0.411 117 TRP FFF CD2 
5826 N NE1 . TRP D 117 ? 3.417 4.246 2.237 -0.824 0.345  -0.419 117 TRP FFF NE1 
5827 C CE2 . TRP D 117 ? 3.468 4.281 2.226 -0.806 0.348  -0.423 117 TRP FFF CE2 
5828 C CE3 . TRP D 117 ? 3.603 4.394 2.293 -0.766 0.376  -0.413 117 TRP FFF CE3 
5829 C CZ2 . TRP D 117 ? 3.439 4.237 2.143 -0.802 0.332  -0.435 117 TRP FFF CZ2 
5830 C CZ3 . TRP D 117 ? 3.592 4.367 2.229 -0.762 0.358  -0.427 117 TRP FFF CZ3 
5831 C CH2 . TRP D 117 ? 3.523 4.301 2.168 -0.780 0.338  -0.437 117 TRP FFF CH2 
5832 N N   . GLY D 118 ? 3.771 4.594 2.567 -0.757 0.424  -0.388 118 GLY FFF N   
5833 C CA  . GLY D 118 ? 3.843 4.663 2.629 -0.733 0.451  -0.372 118 GLY FFF CA  
5834 C C   . GLY D 118 ? 3.894 4.711 2.671 -0.709 0.483  -0.343 118 GLY FFF C   
5835 O O   . GLY D 118 ? 3.812 4.629 2.590 -0.712 0.483  -0.338 118 GLY FFF O   
5836 N N   . GLN D 119 ? 4.004 4.820 2.773 -0.684 0.511  -0.325 119 GLN FFF N   
5837 C CA  . GLN D 119 ? 4.078 4.895 2.846 -0.657 0.549  -0.292 119 GLN FFF CA  
5838 C C   . GLN D 119 ? 4.126 4.917 2.806 -0.627 0.552  -0.295 119 GLN FFF C   
5839 O O   . GLN D 119 ? 4.162 4.951 2.832 -0.605 0.579  -0.270 119 GLN FFF O   
5840 C CB  . GLN D 119 ? 4.092 4.920 2.893 -0.642 0.578  -0.270 119 GLN FFF CB  
5841 C CG  . GLN D 119 ? 4.143 4.952 2.875 -0.613 0.586  -0.275 119 GLN FFF CG  
5842 C CD  . GLN D 119 ? 4.191 4.995 2.909 -0.628 0.557  -0.306 119 GLN FFF CD  
5843 O OE1 . GLN D 119 ? 4.291 5.101 3.034 -0.659 0.527  -0.328 119 GLN FFF OE1 
5844 N NE2 . GLN D 119 ? 4.197 4.990 2.873 -0.604 0.567  -0.307 119 GLN FFF NE2 
5845 N N   . GLY D 120 ? 4.132 4.904 2.751 -0.626 0.525  -0.325 120 GLY FFF N   
5846 C CA  . GLY D 120 ? 4.227 4.970 2.758 -0.597 0.522  -0.333 120 GLY FFF CA  
5847 C C   . GLY D 120 ? 4.273 5.002 2.758 -0.563 0.539  -0.328 120 GLY FFF C   
5848 O O   . GLY D 120 ? 4.288 5.031 2.807 -0.551 0.571  -0.301 120 GLY FFF O   
5849 N N   . THR D 121 ? 4.243 4.945 2.654 -0.547 0.518  -0.351 121 THR FFF N   
5850 C CA  . THR D 121 ? 4.214 4.895 2.566 -0.512 0.528  -0.351 121 THR FFF CA  
5851 C C   . THR D 121 ? 4.270 4.920 2.536 -0.478 0.524  -0.357 121 THR FFF C   
5852 O O   . THR D 121 ? 4.303 4.939 2.542 -0.490 0.491  -0.380 121 THR FFF O   
5853 C CB  . THR D 121 ? 4.146 4.826 2.500 -0.527 0.502  -0.377 121 THR FFF CB  
5854 O OG1 . THR D 121 ? 4.263 4.922 2.559 -0.491 0.512  -0.377 121 THR FFF OG1 
5855 C CG2 . THR D 121 ? 4.081 4.748 2.415 -0.550 0.457  -0.410 121 THR FFF CG2 
5856 N N   . GLN D 122 ? 4.299 4.937 2.525 -0.436 0.556  -0.334 122 GLN FFF N   
5857 C CA  . GLN D 122 ? 4.321 4.928 2.462 -0.397 0.557  -0.335 122 GLN FFF CA  
5858 C C   . GLN D 122 ? 4.380 4.953 2.446 -0.378 0.527  -0.366 122 GLN FFF C   
5859 O O   . GLN D 122 ? 4.326 4.897 2.386 -0.366 0.533  -0.367 122 GLN FFF O   
5860 C CB  . GLN D 122 ? 4.305 4.914 2.432 -0.356 0.605  -0.298 122 GLN FFF CB  
5861 C CG  . GLN D 122 ? 4.335 4.910 2.370 -0.311 0.609  -0.297 122 GLN FFF CG  
5862 C CD  . GLN D 122 ? 4.293 4.864 2.323 -0.322 0.596  -0.301 122 GLN FFF CD  
5863 O OE1 . GLN D 122 ? 4.147 4.745 2.241 -0.345 0.611  -0.281 122 GLN FFF OE1 
5864 N NE2 . GLN D 122 ? 4.374 4.911 2.328 -0.306 0.566  -0.326 122 GLN FFF NE2 
5865 N N   . VAL D 123 ? 4.454 5.001 2.468 -0.376 0.493  -0.390 123 VAL FFF N   
5866 C CA  . VAL D 123 ? 4.557 5.065 2.491 -0.351 0.462  -0.418 123 VAL FFF CA  
5867 C C   . VAL D 123 ? 4.689 5.167 2.545 -0.306 0.471  -0.411 123 VAL FFF C   
5868 O O   . VAL D 123 ? 4.812 5.293 2.675 -0.315 0.470  -0.406 123 VAL FFF O   
5869 C CB  . VAL D 123 ? 4.551 5.052 2.494 -0.386 0.412  -0.452 123 VAL FFF CB  
5870 C CG1 . VAL D 123 ? 4.544 5.004 2.409 -0.360 0.377  -0.481 123 VAL FFF CG1 
5871 C CG2 . VAL D 123 ? 4.514 5.046 2.532 -0.427 0.405  -0.458 123 VAL FFF CG2 
5872 N N   . THR D 124 ? 4.704 5.154 2.489 -0.259 0.480  -0.410 124 THR FFF N   
5873 C CA  . THR D 124 ? 4.623 5.038 2.320 -0.207 0.487  -0.406 124 THR FFF CA  
5874 C C   . THR D 124 ? 4.685 5.055 2.303 -0.184 0.446  -0.441 124 THR FFF C   
5875 O O   . THR D 124 ? 4.564 4.927 2.167 -0.169 0.446  -0.447 124 THR FFF O   
5876 C CB  . THR D 124 ? 4.594 5.016 2.278 -0.166 0.541  -0.369 124 THR FFF CB  
5877 O OG1 . THR D 124 ? 4.425 4.888 2.193 -0.195 0.573  -0.339 124 THR FFF OG1 
5878 C CG2 . THR D 124 ? 4.710 5.096 2.301 -0.109 0.552  -0.362 124 THR FFF CG2 
5879 N N   . VAL D 125 ? 4.810 5.153 2.387 -0.182 0.409  -0.463 125 VAL FFF N   
5880 C CA  . VAL D 125 ? 4.974 5.274 2.483 -0.163 0.361  -0.499 125 VAL FFF CA  
5881 C C   . VAL D 125 ? 5.090 5.347 2.498 -0.100 0.370  -0.496 125 VAL FFF C   
5882 O O   . VAL D 125 ? 5.022 5.275 2.410 -0.087 0.380  -0.484 125 VAL FFF O   
5883 C CB  . VAL D 125 ? 4.986 5.280 2.516 -0.202 0.312  -0.527 125 VAL FFF CB  
5884 C CG1 . VAL D 125 ? 5.117 5.366 2.584 -0.183 0.262  -0.562 125 VAL FFF CG1 
5885 C CG2 . VAL D 125 ? 4.843 5.179 2.469 -0.261 0.307  -0.528 125 VAL FFF CG2 
5886 N N   . SER D 126 ? 5.183 5.412 2.531 -0.061 0.365  -0.505 126 SER FFF N   
5887 C CA  . SER D 126 ? 5.319 5.504 2.563 0.007  0.372  -0.504 126 SER FFF CA  
5888 C C   . SER D 126 ? 5.354 5.491 2.533 0.021  0.316  -0.540 126 SER FFF C   
5889 O O   . SER D 126 ? 5.349 5.482 2.558 -0.016 0.269  -0.569 126 SER FFF O   
5890 C CB  . SER D 126 ? 5.387 5.561 2.597 0.041  0.387  -0.501 126 SER FFF CB  
5891 O OG  . SER D 126 ? 5.310 5.529 2.587 0.026  0.436  -0.468 126 SER FFF OG  
5892 N N   . SER D 127 ? 5.327 5.428 2.420 0.074  0.321  -0.537 127 SER FFF N   
5893 C CA  . SER D 127 ? 5.297 5.349 2.320 0.096  0.272  -0.567 127 SER FFF CA  
5894 C C   . SER D 127 ? 5.256 5.269 2.241 0.104  0.218  -0.605 127 SER FFF C   
5895 O O   . SER D 127 ? 5.312 5.318 2.275 0.127  0.228  -0.605 127 SER FFF O   
5896 C CB  . SER D 127 ? 5.408 5.431 2.343 0.159  0.297  -0.551 127 SER FFF CB  
5897 O OG  . SER D 127 ? 5.527 5.493 2.378 0.193  0.247  -0.584 127 SER FFF OG  
5898 N N   . LYS D 128 ? 5.114 5.103 2.097 0.084  0.162  -0.636 128 LYS FFF N   
5899 C CA  . LYS D 128 ? 5.045 4.986 1.981 0.100  0.101  -0.676 128 LYS FFF CA  
5900 C C   . LYS D 128 ? 4.910 4.865 1.888 0.077  0.092  -0.685 128 LYS FFF C   
5901 O O   . LYS D 128 ? 4.676 4.630 1.696 0.040  0.047  -0.710 128 LYS FFF O   
5902 C CB  . LYS D 128 ? 5.081 4.965 1.898 0.175  0.093  -0.684 128 LYS FFF CB  
5903 C CG  . LYS D 128 ? 5.069 4.931 1.841 0.195  0.087  -0.684 128 LYS FFF CG  
5904 C CD  . LYS D 128 ? 5.213 5.033 1.875 0.271  0.105  -0.677 128 LYS FFF CD  
5905 C CE  . LYS D 128 ? 5.264 5.073 1.893 0.287  0.109  -0.669 128 LYS FFF CE  
5906 N NZ  . LYS D 128 ? 5.353 5.141 1.893 0.356  0.150  -0.648 128 LYS FFF NZ  
# 
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   THR 1   0   0   THR THR HHH . n 
A 1 2   GLN 2   1   1   GLN GLN HHH . n 
A 1 3   MET 3   2   2   MET MET HHH . n 
A 1 4   GLN 4   3   3   GLN GLN HHH . n 
A 1 5   LEU 5   4   4   LEU LEU HHH . n 
A 1 6   VAL 6   5   5   VAL VAL HHH . n 
A 1 7   GLN 7   6   6   GLN GLN HHH . n 
A 1 8   SER 8   7   7   SER SER HHH . n 
A 1 9   GLY 9   8   8   GLY GLY HHH . n 
A 1 10  THR 10  9   9   THR THR HHH . n 
A 1 11  GLU 11  10  10  GLU GLU HHH . n 
A 1 12  VAL 12  11  11  VAL VAL HHH . n 
A 1 13  LYS 13  12  12  LYS LYS HHH . n 
A 1 14  LYS 14  13  13  LYS LYS HHH . n 
A 1 15  PRO 15  14  14  PRO PRO HHH . n 
A 1 16  GLY 16  15  15  GLY GLY HHH . n 
A 1 17  GLU 17  16  16  GLU GLU HHH . n 
A 1 18  SER 18  17  17  SER SER HHH . n 
A 1 19  LEU 19  18  18  LEU LEU HHH . n 
A 1 20  LYS 20  19  19  LYS LYS HHH . n 
A 1 21  ILE 21  20  20  ILE ILE HHH . n 
A 1 22  SER 22  21  21  SER SER HHH . n 
A 1 23  CYS 23  22  22  CYS CYS HHH . n 
A 1 24  LYS 24  23  23  LYS LYS HHH . n 
A 1 25  GLY 25  24  24  GLY GLY HHH . n 
A 1 26  SER 26  25  25  SER SER HHH . n 
A 1 27  GLY 27  26  26  GLY GLY HHH . n 
A 1 28  TYR 28  27  27  TYR TYR HHH . n 
A 1 29  GLY 29  28  28  GLY GLY HHH . n 
A 1 30  PHE 30  29  29  PHE PHE HHH . n 
A 1 31  ILE 31  30  30  ILE ILE HHH . n 
A 1 32  THR 32  31  31  THR THR HHH . n 
A 1 33  TYR 33  32  32  TYR TYR HHH . n 
A 1 34  TRP 34  33  33  TRP TRP HHH . n 
A 1 35  ILE 35  34  34  ILE ILE HHH . n 
A 1 36  GLY 36  35  35  GLY GLY HHH . n 
A 1 37  TRP 37  36  36  TRP TRP HHH . n 
A 1 38  VAL 38  37  37  VAL VAL HHH . n 
A 1 39  ARG 39  38  38  ARG ARG HHH . n 
A 1 40  GLN 40  39  39  GLN GLN HHH . n 
A 1 41  MET 41  40  40  MET MET HHH . n 
A 1 42  PRO 42  41  41  PRO PRO HHH . n 
A 1 43  GLY 43  42  42  GLY GLY HHH . n 
A 1 44  LYS 44  43  43  LYS LYS HHH . n 
A 1 45  GLY 45  44  44  GLY GLY HHH . n 
A 1 46  LEU 46  45  45  LEU LEU HHH . n 
A 1 47  GLU 47  46  46  GLU GLU HHH . n 
A 1 48  TRP 48  47  47  TRP TRP HHH . n 
A 1 49  MET 49  48  48  MET MET HHH . n 
A 1 50  GLY 50  49  49  GLY GLY HHH . n 
A 1 51  ILE 51  50  50  ILE ILE HHH . n 
A 1 52  ILE 52  51  51  ILE ILE HHH . n 
A 1 53  TYR 53  52  52  TYR TYR HHH . n 
A 1 54  PRO 54  53  53  PRO PRO HHH . n 
A 1 55  GLY 55  54  54  GLY GLY HHH . n 
A 1 56  ASP 56  55  55  ASP ASP HHH . n 
A 1 57  SER 57  56  56  SER SER HHH . n 
A 1 58  GLU 58  57  57  GLU GLU HHH . n 
A 1 59  THR 59  58  58  THR THR HHH . n 
A 1 60  ARG 60  59  59  ARG ARG HHH . n 
A 1 61  TYR 61  60  60  TYR TYR HHH . n 
A 1 62  SER 62  61  61  SER SER HHH . n 
A 1 63  PRO 63  62  62  PRO PRO HHH . n 
A 1 64  SER 64  63  63  SER SER HHH . n 
A 1 65  PHE 65  64  64  PHE PHE HHH . n 
A 1 66  GLN 66  65  65  GLN GLN HHH . n 
A 1 67  GLY 67  66  66  GLY GLY HHH . n 
A 1 68  GLN 68  67  67  GLN GLN HHH . n 
A 1 69  VAL 69  68  68  VAL VAL HHH . n 
A 1 70  THR 70  69  69  THR THR HHH . n 
A 1 71  ILE 71  70  70  ILE ILE HHH . n 
A 1 72  SER 72  71  71  SER SER HHH . n 
A 1 73  ALA 73  72  72  ALA ALA HHH . n 
A 1 74  ASP 74  73  73  ASP ASP HHH . n 
A 1 75  LYS 75  74  74  LYS LYS HHH . n 
A 1 76  SER 76  75  75  SER SER HHH . n 
A 1 77  ILE 77  76  76  ILE ILE HHH . n 
A 1 78  ASN 78  77  77  ASN ASN HHH . n 
A 1 79  THR 79  78  78  THR THR HHH . n 
A 1 80  ALA 80  79  79  ALA ALA HHH . n 
A 1 81  TYR 81  80  80  TYR TYR HHH . n 
A 1 82  LEU 82  81  81  LEU LEU HHH . n 
A 1 83  GLN 83  82  82  GLN GLN HHH . n 
A 1 84  TRP 84  83  83  TRP TRP HHH . n 
A 1 85  SER 85  84  84  SER SER HHH . n 
A 1 86  SER 86  85  85  SER SER HHH . n 
A 1 87  LEU 87  86  86  LEU LEU HHH . n 
A 1 88  LYS 88  87  87  LYS LYS HHH . n 
A 1 89  ALA 89  88  88  ALA ALA HHH . n 
A 1 90  SER 90  89  89  SER SER HHH . n 
A 1 91  ASP 91  90  90  ASP ASP HHH . n 
A 1 92  THR 92  91  91  THR THR HHH . n 
A 1 93  ALA 93  92  92  ALA ALA HHH . n 
A 1 94  ILE 94  93  93  ILE ILE HHH . n 
A 1 95  TYR 95  94  94  TYR TYR HHH . n 
A 1 96  TYR 96  95  95  TYR TYR HHH . n 
A 1 97  CYS 97  96  96  CYS CYS HHH . n 
A 1 98  ALA 98  97  97  ALA ALA HHH . n 
A 1 99  GLY 99  98  98  GLY GLY HHH . n 
A 1 100 GLY 100 99  99  GLY GLY HHH . n 
A 1 101 SER 101 100 100 SER SER HHH . n 
A 1 102 GLY 102 101 101 GLY GLY HHH . n 
A 1 103 ILE 103 102 102 ILE ILE HHH . n 
A 1 104 SER 104 103 103 SER SER HHH . n 
A 1 105 THR 105 104 104 THR THR HHH . n 
A 1 106 PRO 106 105 105 PRO PRO HHH . n 
A 1 107 MET 107 106 106 MET MET HHH . n 
A 1 108 ASP 108 107 107 ASP ASP HHH . n 
A 1 109 VAL 109 108 108 VAL VAL HHH . n 
A 1 110 TRP 110 109 109 TRP TRP HHH . n 
A 1 111 GLY 111 110 110 GLY GLY HHH . n 
A 1 112 GLN 112 111 111 GLN GLN HHH . n 
A 1 113 GLY 113 112 112 GLY GLY HHH . n 
A 1 114 THR 114 113 113 THR THR HHH . n 
A 1 115 THR 115 114 114 THR THR HHH . n 
A 1 116 VAL 116 115 115 VAL VAL HHH . n 
A 1 117 THR 117 116 116 THR THR HHH . n 
A 1 118 VAL 118 117 117 VAL VAL HHH . n 
A 1 119 ALA 119 118 118 ALA ALA HHH . n 
A 1 120 SER 120 119 119 SER SER HHH . n 
A 1 121 THR 121 120 120 THR THR HHH . n 
A 1 122 LYS 122 121 121 LYS LYS HHH . n 
A 1 123 GLY 123 122 122 GLY GLY HHH . n 
A 1 124 PRO 124 123 123 PRO PRO HHH . n 
A 1 125 SER 125 124 124 SER SER HHH . n 
A 1 126 VAL 126 125 125 VAL VAL HHH . n 
A 1 127 PHE 127 126 126 PHE PHE HHH . n 
A 1 128 PRO 128 127 127 PRO PRO HHH . n 
A 1 129 LEU 129 128 128 LEU LEU HHH . n 
A 1 130 ALA 130 129 129 ALA ALA HHH . n 
A 1 131 PRO 131 130 130 PRO PRO HHH . n 
A 1 132 SER 132 131 131 SER SER HHH . n 
A 1 133 SER 133 132 132 SER SER HHH . n 
A 1 134 GLY 134 137 137 GLY GLY HHH . n 
A 1 135 GLY 135 138 138 GLY GLY HHH . n 
A 1 136 THR 136 139 139 THR THR HHH . n 
A 1 137 ALA 137 140 140 ALA ALA HHH . n 
A 1 138 ALA 138 141 141 ALA ALA HHH . n 
A 1 139 LEU 139 142 142 LEU LEU HHH . n 
A 1 140 GLY 140 143 143 GLY GLY HHH . n 
A 1 141 CYS 141 144 144 CYS CYS HHH . n 
A 1 142 LEU 142 145 145 LEU LEU HHH . n 
A 1 143 VAL 143 146 146 VAL VAL HHH . n 
A 1 144 LYS 144 147 147 LYS LYS HHH . n 
A 1 145 ASP 145 148 148 ASP ASP HHH . n 
A 1 146 TYR 146 149 149 TYR TYR HHH . n 
A 1 147 PHE 147 150 150 PHE PHE HHH . n 
A 1 148 PRO 148 151 151 PRO PRO HHH . n 
A 1 149 GLU 149 152 152 GLU GLU HHH . n 
A 1 150 PRO 150 153 153 PRO PRO HHH . n 
A 1 151 VAL 151 154 154 VAL VAL HHH . n 
A 1 152 THR 152 155 155 THR THR HHH . n 
A 1 153 VAL 153 156 156 VAL VAL HHH . n 
A 1 154 SER 154 157 157 SER SER HHH . n 
A 1 155 TRP 155 158 158 TRP TRP HHH . n 
A 1 156 ASN 156 159 159 ASN ASN HHH . n 
A 1 157 SER 157 160 160 SER SER HHH . n 
A 1 158 GLY 158 161 161 GLY GLY HHH . n 
A 1 159 ALA 159 162 162 ALA ALA HHH . n 
A 1 160 LEU 160 163 163 LEU LEU HHH . n 
A 1 161 THR 161 164 164 THR THR HHH . n 
A 1 162 SER 162 165 165 SER SER HHH . n 
A 1 163 GLY 163 166 166 GLY GLY HHH . n 
A 1 164 VAL 164 167 167 VAL VAL HHH . n 
A 1 165 HIS 165 168 168 HIS HIS HHH . n 
A 1 166 THR 166 169 169 THR THR HHH . n 
A 1 167 PHE 167 170 170 PHE PHE HHH . n 
A 1 168 PRO 168 171 171 PRO PRO HHH . n 
A 1 169 ALA 169 172 172 ALA ALA HHH . n 
A 1 170 VAL 170 173 173 VAL VAL HHH . n 
A 1 171 LEU 171 174 174 LEU LEU HHH . n 
A 1 172 GLN 172 175 175 GLN GLN HHH . n 
A 1 173 SER 173 176 176 SER SER HHH . n 
A 1 174 SER 174 177 177 SER SER HHH . n 
A 1 175 GLY 175 178 178 GLY GLY HHH . n 
A 1 176 LEU 176 179 179 LEU LEU HHH . n 
A 1 177 TYR 177 180 180 TYR TYR HHH . n 
A 1 178 SER 178 181 181 SER SER HHH . n 
A 1 179 LEU 179 182 182 LEU LEU HHH . n 
A 1 180 SER 180 183 183 SER SER HHH . n 
A 1 181 SER 181 184 184 SER SER HHH . n 
A 1 182 VAL 182 185 185 VAL VAL HHH . n 
A 1 183 VAL 183 186 186 VAL VAL HHH . n 
A 1 184 THR 184 187 187 THR THR HHH . n 
A 1 185 VAL 185 188 188 VAL VAL HHH . n 
A 1 186 PRO 186 189 189 PRO PRO HHH . n 
A 1 187 SER 187 190 190 SER SER HHH . n 
A 1 188 SER 188 191 191 SER SER HHH . n 
A 1 189 SER 189 192 192 SER SER HHH . n 
A 1 190 LEU 190 193 193 LEU LEU HHH . n 
A 1 191 GLY 191 194 194 GLY GLY HHH . n 
A 1 192 THR 192 195 195 THR THR HHH . n 
A 1 193 GLN 193 196 196 GLN GLN HHH . n 
A 1 194 THR 194 197 197 THR THR HHH . n 
A 1 195 TYR 195 198 198 TYR TYR HHH . n 
A 1 196 ILE 196 199 199 ILE ILE HHH . n 
A 1 197 CYS 197 200 200 CYS CYS HHH . n 
A 1 198 ASN 198 201 201 ASN ASN HHH . n 
A 1 199 VAL 199 202 202 VAL VAL HHH . n 
A 1 200 ASN 200 203 203 ASN ASN HHH . n 
A 1 201 HIS 201 204 204 HIS HIS HHH . n 
A 1 202 LYS 202 205 205 LYS LYS HHH . n 
A 1 203 PRO 203 206 206 PRO PRO HHH . n 
A 1 204 SER 204 207 207 SER SER HHH . n 
A 1 205 ASN 205 208 208 ASN ASN HHH . n 
A 1 206 THR 206 209 209 THR THR HHH . n 
A 1 207 LYS 207 210 210 LYS LYS HHH . n 
A 1 208 VAL 208 211 211 VAL VAL HHH . n 
A 1 209 ASP 209 212 212 ASP ASP HHH . n 
A 1 210 LYS 210 213 213 LYS LYS HHH . n 
A 1 211 LYS 211 214 214 LYS LYS HHH . n 
A 1 212 VAL 212 215 215 VAL VAL HHH . n 
A 1 213 GLU 213 216 216 GLU GLU HHH . n 
A 1 214 PRO 214 217 217 PRO PRO HHH . n 
A 1 215 LYS 215 218 218 LYS LYS HHH . n 
A 1 216 SER 216 219 219 SER SER HHH . n 
B 2 1   ASP 1   1   1   ASP ASP LLL . n 
B 2 2   ILE 2   2   2   ILE ILE LLL . n 
B 2 3   GLN 3   3   3   GLN GLN LLL . n 
B 2 4   LEU 4   4   4   LEU LEU LLL . n 
B 2 5   THR 5   5   5   THR THR LLL . n 
B 2 6   GLN 6   6   6   GLN GLN LLL . n 
B 2 7   SER 7   7   7   SER SER LLL . n 
B 2 8   PRO 8   8   8   PRO PRO LLL . n 
B 2 9   ASP 9   9   9   ASP ASP LLL . n 
B 2 10  SER 10  10  10  SER SER LLL . n 
B 2 11  LEU 11  11  11  LEU LEU LLL . n 
B 2 12  ALA 12  12  12  ALA ALA LLL . n 
B 2 13  VAL 13  13  13  VAL VAL LLL . n 
B 2 14  SER 14  14  14  SER SER LLL . n 
B 2 15  LEU 15  15  15  LEU LEU LLL . n 
B 2 16  GLY 16  16  16  GLY GLY LLL . n 
B 2 17  GLU 17  17  17  GLU GLU LLL . n 
B 2 18  ARG 18  18  18  ARG ARG LLL . n 
B 2 19  ALA 19  19  19  ALA ALA LLL . n 
B 2 20  THR 20  20  20  THR THR LLL . n 
B 2 21  ILE 21  21  21  ILE ILE LLL . n 
B 2 22  ASN 22  22  22  ASN ASN LLL . n 
B 2 23  CYS 23  23  23  CYS CYS LLL . n 
B 2 24  LYS 24  24  24  LYS LYS LLL . n 
B 2 25  SER 25  25  25  SER SER LLL . n 
B 2 26  SER 26  26  26  SER SER LLL . n 
B 2 27  GLN 27  27  27  GLN GLN LLL . n 
B 2 28  SER 28  28  28  SER SER LLL . n 
B 2 29  VAL 29  29  29  VAL VAL LLL . n 
B 2 30  LEU 30  30  30  LEU LEU LLL . n 
B 2 31  TYR 31  31  31  TYR TYR LLL . n 
B 2 32  SER 32  32  32  SER SER LLL . n 
B 2 33  SER 33  33  33  SER SER LLL . n 
B 2 34  ILE 34  34  34  ILE ILE LLL . n 
B 2 35  ASN 35  35  35  ASN ASN LLL . n 
B 2 36  LYS 36  36  36  LYS LYS LLL . n 
B 2 37  ASN 37  37  37  ASN ASN LLL . n 
B 2 38  TYR 38  38  38  TYR TYR LLL . n 
B 2 39  LEU 39  39  39  LEU LEU LLL . n 
B 2 40  ALA 40  40  40  ALA ALA LLL . n 
B 2 41  TRP 41  41  41  TRP TRP LLL . n 
B 2 42  TYR 42  42  42  TYR TYR LLL . n 
B 2 43  GLN 43  43  43  GLN GLN LLL . n 
B 2 44  GLN 44  44  44  GLN GLN LLL . n 
B 2 45  LYS 45  45  45  LYS LYS LLL . n 
B 2 46  PRO 46  46  46  PRO PRO LLL . n 
B 2 47  GLY 47  47  47  GLY GLY LLL . n 
B 2 48  GLN 48  48  48  GLN GLN LLL . n 
B 2 49  PRO 49  49  49  PRO PRO LLL . n 
B 2 50  PRO 50  50  50  PRO PRO LLL . n 
B 2 51  LYS 51  51  51  LYS LYS LLL . n 
B 2 52  LEU 52  52  52  LEU LEU LLL . n 
B 2 53  LEU 53  53  53  LEU LEU LLL . n 
B 2 54  ILE 54  54  54  ILE ILE LLL . n 
B 2 55  TYR 55  55  55  TYR TYR LLL . n 
B 2 56  TRP 56  56  56  TRP TRP LLL . n 
B 2 57  ALA 57  57  57  ALA ALA LLL . n 
B 2 58  SER 58  58  58  SER SER LLL . n 
B 2 59  THR 59  59  59  THR THR LLL . n 
B 2 60  ARG 60  60  60  ARG ARG LLL . n 
B 2 61  GLU 61  61  61  GLU GLU LLL . n 
B 2 62  SER 62  62  62  SER SER LLL . n 
B 2 63  GLY 63  63  63  GLY GLY LLL . n 
B 2 64  VAL 64  64  64  VAL VAL LLL . n 
B 2 65  PRO 65  65  65  PRO PRO LLL . n 
B 2 66  ASP 66  66  66  ASP ASP LLL . n 
B 2 67  ARG 67  67  67  ARG ARG LLL . n 
B 2 68  PHE 68  68  68  PHE PHE LLL . n 
B 2 69  SER 69  69  69  SER SER LLL . n 
B 2 70  GLY 70  70  70  GLY GLY LLL . n 
B 2 71  SER 71  71  71  SER SER LLL . n 
B 2 72  GLY 72  72  72  GLY GLY LLL . n 
B 2 73  SER 73  73  73  SER SER LLL . n 
B 2 74  GLY 74  74  74  GLY GLY LLL . n 
B 2 75  THR 75  75  75  THR THR LLL . n 
B 2 76  ASP 76  76  76  ASP ASP LLL . n 
B 2 77  PHE 77  77  77  PHE PHE LLL . n 
B 2 78  THR 78  78  78  THR THR LLL . n 
B 2 79  LEU 79  79  79  LEU LEU LLL . n 
B 2 80  THR 80  80  80  THR THR LLL . n 
B 2 81  ILE 81  81  81  ILE ILE LLL . n 
B 2 82  SER 82  82  82  SER SER LLL . n 
B 2 83  SER 83  83  83  SER SER LLL . n 
B 2 84  LEU 84  84  84  LEU LEU LLL . n 
B 2 85  GLN 85  85  85  GLN GLN LLL . n 
B 2 86  ALA 86  86  86  ALA ALA LLL . n 
B 2 87  GLU 87  87  87  GLU GLU LLL . n 
B 2 88  ASP 88  88  88  ASP ASP LLL . n 
B 2 89  VAL 89  89  89  VAL VAL LLL . n 
B 2 90  ALA 90  90  90  ALA ALA LLL . n 
B 2 91  VAL 91  91  91  VAL VAL LLL . n 
B 2 92  TYR 92  92  92  TYR TYR LLL . n 
B 2 93  TYR 93  93  93  TYR TYR LLL . n 
B 2 94  CYS 94  94  94  CYS CYS LLL . n 
B 2 95  GLN 95  95  95  GLN GLN LLL . n 
B 2 96  GLN 96  96  96  GLN GLN LLL . n 
B 2 97  TYR 97  97  97  TYR TYR LLL . n 
B 2 98  TYR 98  98  98  TYR TYR LLL . n 
B 2 99  SER 99  99  99  SER SER LLL . n 
B 2 100 THR 100 100 100 THR THR LLL . n 
B 2 101 PRO 101 101 101 PRO PRO LLL . n 
B 2 102 TYR 102 102 102 TYR TYR LLL . n 
B 2 103 THR 103 103 103 THR THR LLL . n 
B 2 104 PHE 104 104 104 PHE PHE LLL . n 
B 2 105 GLY 105 105 105 GLY GLY LLL . n 
B 2 106 GLN 106 106 106 GLN GLN LLL . n 
B 2 107 GLY 107 107 107 GLY GLY LLL . n 
B 2 108 THR 108 108 108 THR THR LLL . n 
B 2 109 LYS 109 109 109 LYS LYS LLL . n 
B 2 110 VAL 110 110 110 VAL VAL LLL . n 
B 2 111 GLU 111 111 111 GLU GLU LLL . n 
B 2 112 ILE 112 112 112 ILE ILE LLL . n 
B 2 113 LYS 113 113 113 LYS LYS LLL . n 
B 2 114 ARG 114 114 114 ARG ARG LLL . n 
B 2 115 THR 115 115 115 THR THR LLL . n 
B 2 116 VAL 116 116 116 VAL VAL LLL . n 
B 2 117 ALA 117 117 117 ALA ALA LLL . n 
B 2 118 ALA 118 118 118 ALA ALA LLL . n 
B 2 119 PRO 119 119 119 PRO PRO LLL . n 
B 2 120 SER 120 120 120 SER SER LLL . n 
B 2 121 VAL 121 121 121 VAL VAL LLL . n 
B 2 122 PHE 122 122 122 PHE PHE LLL . n 
B 2 123 ILE 123 123 123 ILE ILE LLL . n 
B 2 124 PHE 124 124 124 PHE PHE LLL . n 
B 2 125 PRO 125 125 125 PRO PRO LLL . n 
B 2 126 PRO 126 126 126 PRO PRO LLL . n 
B 2 127 SER 127 127 127 SER SER LLL . n 
B 2 128 ASP 128 128 128 ASP ASP LLL . n 
B 2 129 GLU 129 129 129 GLU GLU LLL . n 
B 2 130 GLN 130 130 130 GLN GLN LLL . n 
B 2 131 LEU 131 131 131 LEU LEU LLL . n 
B 2 132 LYS 132 132 132 LYS LYS LLL . n 
B 2 133 SER 133 133 133 SER SER LLL . n 
B 2 134 GLY 134 134 134 GLY GLY LLL . n 
B 2 135 THR 135 135 135 THR THR LLL . n 
B 2 136 ALA 136 136 136 ALA ALA LLL . n 
B 2 137 SER 137 137 137 SER SER LLL . n 
B 2 138 VAL 138 138 138 VAL VAL LLL . n 
B 2 139 VAL 139 139 139 VAL VAL LLL . n 
B 2 140 CYS 140 140 140 CYS CYS LLL . n 
B 2 141 LEU 141 141 141 LEU LEU LLL . n 
B 2 142 LEU 142 142 142 LEU LEU LLL . n 
B 2 143 ASN 143 143 143 ASN ASN LLL . n 
B 2 144 ASN 144 144 144 ASN ASN LLL . n 
B 2 145 PHE 145 145 145 PHE PHE LLL . n 
B 2 146 TYR 146 146 146 TYR TYR LLL . n 
B 2 147 PRO 147 147 147 PRO PRO LLL . n 
B 2 148 ARG 148 148 148 ARG ARG LLL . n 
B 2 149 GLU 149 149 149 GLU GLU LLL . n 
B 2 150 ALA 150 150 150 ALA ALA LLL . n 
B 2 151 LYS 151 151 151 LYS LYS LLL . n 
B 2 152 VAL 152 152 152 VAL VAL LLL . n 
B 2 153 GLN 153 153 153 GLN GLN LLL . n 
B 2 154 TRP 154 154 154 TRP TRP LLL . n 
B 2 155 LYS 155 155 155 LYS LYS LLL . n 
B 2 156 VAL 156 156 156 VAL VAL LLL . n 
B 2 157 ASP 157 157 157 ASP ASP LLL . n 
B 2 158 ASN 158 158 158 ASN ASN LLL . n 
B 2 159 ALA 159 159 159 ALA ALA LLL . n 
B 2 160 LEU 160 160 160 LEU LEU LLL . n 
B 2 161 GLN 161 161 161 GLN GLN LLL . n 
B 2 162 SER 162 162 162 SER SER LLL . n 
B 2 163 GLY 163 163 163 GLY GLY LLL . n 
B 2 164 ASN 164 164 164 ASN ASN LLL . n 
B 2 165 SER 165 165 165 SER SER LLL . n 
B 2 166 GLN 166 166 166 GLN GLN LLL . n 
B 2 167 GLU 167 167 167 GLU GLU LLL . n 
B 2 168 SER 168 168 168 SER SER LLL . n 
B 2 169 VAL 169 169 169 VAL VAL LLL . n 
B 2 170 THR 170 170 170 THR THR LLL . n 
B 2 171 GLU 171 171 171 GLU GLU LLL . n 
B 2 172 GLN 172 172 172 GLN GLN LLL . n 
B 2 173 ASP 173 173 173 ASP ASP LLL . n 
B 2 174 SER 174 174 174 SER SER LLL . n 
B 2 175 LYS 175 175 175 LYS LYS LLL . n 
B 2 176 ASP 176 176 176 ASP ASP LLL . n 
B 2 177 SER 177 177 177 SER SER LLL . n 
B 2 178 THR 178 178 178 THR THR LLL . n 
B 2 179 TYR 179 179 179 TYR TYR LLL . n 
B 2 180 SER 180 180 180 SER SER LLL . n 
B 2 181 LEU 181 181 181 LEU LEU LLL . n 
B 2 182 SER 182 182 182 SER SER LLL . n 
B 2 183 SER 183 183 183 SER SER LLL . n 
B 2 184 THR 184 184 184 THR THR LLL . n 
B 2 185 LEU 185 185 185 LEU LEU LLL . n 
B 2 186 THR 186 186 186 THR THR LLL . n 
B 2 187 LEU 187 187 187 LEU LEU LLL . n 
B 2 188 SER 188 188 188 SER SER LLL . n 
B 2 189 LYS 189 189 189 LYS LYS LLL . n 
B 2 190 ALA 190 190 190 ALA ALA LLL . n 
B 2 191 ASP 191 191 191 ASP ASP LLL . n 
B 2 192 TYR 192 192 192 TYR TYR LLL . n 
B 2 193 GLU 193 193 193 GLU GLU LLL . n 
B 2 194 LYS 194 194 194 LYS LYS LLL . n 
B 2 195 HIS 195 195 195 HIS HIS LLL . n 
B 2 196 LYS 196 196 196 LYS LYS LLL . n 
B 2 197 VAL 197 197 197 VAL VAL LLL . n 
B 2 198 TYR 198 198 198 TYR TYR LLL . n 
B 2 199 ALA 199 199 199 ALA ALA LLL . n 
B 2 200 CYS 200 200 200 CYS CYS LLL . n 
B 2 201 GLU 201 201 201 GLU GLU LLL . n 
B 2 202 VAL 202 202 202 VAL VAL LLL . n 
B 2 203 THR 203 203 203 THR THR LLL . n 
B 2 204 HIS 204 204 204 HIS HIS LLL . n 
B 2 205 GLN 205 205 205 GLN GLN LLL . n 
B 2 206 GLY 206 206 206 GLY GLY LLL . n 
B 2 207 LEU 207 207 207 LEU LEU LLL . n 
B 2 208 SER 208 208 208 SER SER LLL . n 
B 2 209 SER 209 209 209 SER SER LLL . n 
B 2 210 PRO 210 210 210 PRO PRO LLL . n 
B 2 211 VAL 211 211 211 VAL VAL LLL . n 
B 2 212 THR 212 212 212 THR THR LLL . n 
B 2 213 LYS 213 213 213 LYS LYS LLL . n 
B 2 214 SER 214 214 214 SER SER LLL . n 
B 2 215 PHE 215 215 215 PHE PHE LLL . n 
B 2 216 ASN 216 216 216 ASN ASN LLL . n 
B 2 217 ARG 217 217 217 ARG ARG LLL . n 
B 2 218 GLY 218 218 218 GLY GLY LLL . n 
B 2 219 GLU 219 219 219 GLU GLU LLL . n 
C 3 1   ILE 1   332 ?   ?   ?   EEE . n 
C 3 2   THR 2   333 ?   ?   ?   EEE . n 
C 3 3   ASN 3   334 334 ASN ASN EEE . n 
C 3 4   LEU 4   335 335 LEU LEU EEE . n 
C 3 5   CYS 5   336 336 CYS CYS EEE . n 
C 3 6   PRO 6   337 337 PRO PRO EEE . n 
C 3 7   PHE 7   338 338 PHE PHE EEE . n 
C 3 8   GLY 8   339 339 GLY GLY EEE . n 
C 3 9   GLU 9   340 340 GLU GLU EEE . n 
C 3 10  VAL 10  341 341 VAL VAL EEE . n 
C 3 11  PHE 11  342 342 PHE PHE EEE . n 
C 3 12  ASN 12  343 343 ASN ASN EEE . n 
C 3 13  ALA 13  344 344 ALA ALA EEE . n 
C 3 14  THR 14  345 345 THR THR EEE . n 
C 3 15  ARG 15  346 346 ARG ARG EEE . n 
C 3 16  PHE 16  347 347 PHE PHE EEE . n 
C 3 17  ALA 17  348 348 ALA ALA EEE . n 
C 3 18  SER 18  349 349 SER SER EEE . n 
C 3 19  VAL 19  350 350 VAL VAL EEE . n 
C 3 20  TYR 20  351 351 TYR TYR EEE . n 
C 3 21  ALA 21  352 352 ALA ALA EEE . n 
C 3 22  TRP 22  353 353 TRP TRP EEE . n 
C 3 23  ASN 23  354 354 ASN ASN EEE . n 
C 3 24  ARG 24  355 355 ARG ARG EEE . n 
C 3 25  LYS 25  356 356 LYS LYS EEE . n 
C 3 26  ARG 26  357 357 ARG ARG EEE . n 
C 3 27  ILE 27  358 358 ILE ILE EEE . n 
C 3 28  SER 28  359 359 SER SER EEE . n 
C 3 29  ASN 29  360 360 ASN ASN EEE . n 
C 3 30  CYS 30  361 361 CYS CYS EEE . n 
C 3 31  VAL 31  362 362 VAL VAL EEE . n 
C 3 32  ALA 32  363 363 ALA ALA EEE . n 
C 3 33  ASP 33  364 364 ASP ASP EEE . n 
C 3 34  TYR 34  365 365 TYR TYR EEE . n 
C 3 35  SER 35  366 366 SER SER EEE . n 
C 3 36  VAL 36  367 367 VAL VAL EEE . n 
C 3 37  LEU 37  368 368 LEU LEU EEE . n 
C 3 38  TYR 38  369 369 TYR TYR EEE . n 
C 3 39  ASN 39  370 370 ASN ASN EEE . n 
C 3 40  SER 40  371 371 SER SER EEE . n 
C 3 41  ALA 41  372 372 ALA ALA EEE . n 
C 3 42  SER 42  373 373 SER SER EEE . n 
C 3 43  PHE 43  374 374 PHE PHE EEE . n 
C 3 44  SER 44  375 375 SER SER EEE . n 
C 3 45  THR 45  376 376 THR THR EEE . n 
C 3 46  PHE 46  377 377 PHE PHE EEE . n 
C 3 47  LYS 47  378 378 LYS LYS EEE . n 
C 3 48  CYS 48  379 379 CYS CYS EEE . n 
C 3 49  TYR 49  380 380 TYR TYR EEE . n 
C 3 50  GLY 50  381 381 GLY GLY EEE . n 
C 3 51  VAL 51  382 382 VAL VAL EEE . n 
C 3 52  SER 52  383 383 SER SER EEE . n 
C 3 53  PRO 53  384 384 PRO PRO EEE . n 
C 3 54  THR 54  385 385 THR THR EEE . n 
C 3 55  LYS 55  386 386 LYS LYS EEE . n 
C 3 56  LEU 56  387 387 LEU LEU EEE . n 
C 3 57  ASN 57  388 388 ASN ASN EEE . n 
C 3 58  ASP 58  389 389 ASP ASP EEE . n 
C 3 59  LEU 59  390 390 LEU LEU EEE . n 
C 3 60  CYS 60  391 391 CYS CYS EEE . n 
C 3 61  PHE 61  392 392 PHE PHE EEE . n 
C 3 62  THR 62  393 393 THR THR EEE . n 
C 3 63  ASN 63  394 394 ASN ASN EEE . n 
C 3 64  VAL 64  395 395 VAL VAL EEE . n 
C 3 65  TYR 65  396 396 TYR TYR EEE . n 
C 3 66  ALA 66  397 397 ALA ALA EEE . n 
C 3 67  ASP 67  398 398 ASP ASP EEE . n 
C 3 68  SER 68  399 399 SER SER EEE . n 
C 3 69  PHE 69  400 400 PHE PHE EEE . n 
C 3 70  VAL 70  401 401 VAL VAL EEE . n 
C 3 71  ILE 71  402 402 ILE ILE EEE . n 
C 3 72  ARG 72  403 403 ARG ARG EEE . n 
C 3 73  GLY 73  404 404 GLY GLY EEE . n 
C 3 74  ASP 74  405 405 ASP ASP EEE . n 
C 3 75  GLU 75  406 406 GLU GLU EEE . n 
C 3 76  VAL 76  407 407 VAL VAL EEE . n 
C 3 77  ARG 77  408 408 ARG ARG EEE . n 
C 3 78  GLN 78  409 409 GLN GLN EEE . n 
C 3 79  ILE 79  410 410 ILE ILE EEE . n 
C 3 80  ALA 80  411 411 ALA ALA EEE . n 
C 3 81  PRO 81  412 412 PRO PRO EEE . n 
C 3 82  GLY 82  413 413 GLY GLY EEE . n 
C 3 83  GLN 83  414 414 GLN GLN EEE . n 
C 3 84  THR 84  415 415 THR THR EEE . n 
C 3 85  GLY 85  416 416 GLY GLY EEE . n 
C 3 86  LYS 86  417 417 LYS LYS EEE . n 
C 3 87  ILE 87  418 418 ILE ILE EEE . n 
C 3 88  ALA 88  419 419 ALA ALA EEE . n 
C 3 89  ASP 89  420 420 ASP ASP EEE . n 
C 3 90  TYR 90  421 421 TYR TYR EEE . n 
C 3 91  ASN 91  422 422 ASN ASN EEE . n 
C 3 92  TYR 92  423 423 TYR TYR EEE . n 
C 3 93  LYS 93  424 424 LYS LYS EEE . n 
C 3 94  LEU 94  425 425 LEU LEU EEE . n 
C 3 95  PRO 95  426 426 PRO PRO EEE . n 
C 3 96  ASP 96  427 427 ASP ASP EEE . n 
C 3 97  ASP 97  428 428 ASP ASP EEE . n 
C 3 98  PHE 98  429 429 PHE PHE EEE . n 
C 3 99  THR 99  430 430 THR THR EEE . n 
C 3 100 GLY 100 431 431 GLY GLY EEE . n 
C 3 101 CYS 101 432 432 CYS CYS EEE . n 
C 3 102 VAL 102 433 433 VAL VAL EEE . n 
C 3 103 ILE 103 434 434 ILE ILE EEE . n 
C 3 104 ALA 104 435 435 ALA ALA EEE . n 
C 3 105 TRP 105 436 436 TRP TRP EEE . n 
C 3 106 ASN 106 437 437 ASN ASN EEE . n 
C 3 107 SER 107 438 438 SER SER EEE . n 
C 3 108 ASN 108 439 439 ASN ASN EEE . n 
C 3 109 ASN 109 440 440 ASN ASN EEE . n 
C 3 110 LEU 110 441 441 LEU LEU EEE . n 
C 3 111 ASP 111 442 442 ASP ASP EEE . n 
C 3 112 SER 112 443 443 SER SER EEE . n 
C 3 113 LYS 113 444 444 LYS LYS EEE . n 
C 3 114 VAL 114 445 445 VAL VAL EEE . n 
C 3 115 GLY 115 446 446 GLY GLY EEE . n 
C 3 116 GLY 116 447 447 GLY GLY EEE . n 
C 3 117 ASN 117 448 448 ASN ASN EEE . n 
C 3 118 TYR 118 449 449 TYR TYR EEE . n 
C 3 119 ASN 119 450 450 ASN ASN EEE . n 
C 3 120 TYR 120 451 451 TYR TYR EEE . n 
C 3 121 LEU 121 452 452 LEU LEU EEE . n 
C 3 122 TYR 122 453 453 TYR TYR EEE . n 
C 3 123 ARG 123 454 454 ARG ARG EEE . n 
C 3 124 LEU 124 455 455 LEU LEU EEE . n 
C 3 125 PHE 125 456 456 PHE PHE EEE . n 
C 3 126 ARG 126 457 457 ARG ARG EEE . n 
C 3 127 LYS 127 458 458 LYS LYS EEE . n 
C 3 128 SER 128 459 459 SER SER EEE . n 
C 3 129 ASN 129 460 460 ASN ASN EEE . n 
C 3 130 LEU 130 461 461 LEU LEU EEE . n 
C 3 131 LYS 131 462 462 LYS LYS EEE . n 
C 3 132 PRO 132 463 463 PRO PRO EEE . n 
C 3 133 PHE 133 464 464 PHE PHE EEE . n 
C 3 134 GLU 134 465 465 GLU GLU EEE . n 
C 3 135 ARG 135 466 466 ARG ARG EEE . n 
C 3 136 ASP 136 467 467 ASP ASP EEE . n 
C 3 137 ILE 137 468 468 ILE ILE EEE . n 
C 3 138 SER 138 469 469 SER SER EEE . n 
C 3 139 THR 139 470 470 THR THR EEE . n 
C 3 140 GLU 140 471 471 GLU GLU EEE . n 
C 3 141 ILE 141 472 472 ILE ILE EEE . n 
C 3 142 TYR 142 473 473 TYR TYR EEE . n 
C 3 143 GLN 143 474 474 GLN GLN EEE . n 
C 3 144 ALA 144 475 475 ALA ALA EEE . n 
C 3 145 GLY 145 476 476 GLY GLY EEE . n 
C 3 146 SER 146 477 477 SER SER EEE . n 
C 3 147 THR 147 478 478 THR THR EEE . n 
C 3 148 PRO 148 479 479 PRO PRO EEE . n 
C 3 149 CYS 149 480 480 CYS CYS EEE . n 
C 3 150 ASN 150 481 481 ASN ASN EEE . n 
C 3 151 GLY 151 482 482 GLY GLY EEE . n 
C 3 152 VAL 152 483 483 VAL VAL EEE . n 
C 3 153 GLU 153 484 484 GLU GLU EEE . n 
C 3 154 GLY 154 485 485 GLY GLY EEE . n 
C 3 155 PHE 155 486 486 PHE PHE EEE . n 
C 3 156 ASN 156 487 487 ASN ASN EEE . n 
C 3 157 CYS 157 488 488 CYS CYS EEE . n 
C 3 158 TYR 158 489 489 TYR TYR EEE . n 
C 3 159 PHE 159 490 490 PHE PHE EEE . n 
C 3 160 PRO 160 491 491 PRO PRO EEE . n 
C 3 161 LEU 161 492 492 LEU LEU EEE . n 
C 3 162 GLN 162 493 493 GLN GLN EEE . n 
C 3 163 SER 163 494 494 SER SER EEE . n 
C 3 164 TYR 164 495 495 TYR TYR EEE . n 
C 3 165 GLY 165 496 496 GLY GLY EEE . n 
C 3 166 PHE 166 497 497 PHE PHE EEE . n 
C 3 167 GLN 167 498 498 GLN GLN EEE . n 
C 3 168 PRO 168 499 499 PRO PRO EEE . n 
C 3 169 THR 169 500 500 THR THR EEE . n 
C 3 170 ASN 170 501 501 ASN ASN EEE . n 
C 3 171 GLY 171 502 502 GLY GLY EEE . n 
C 3 172 VAL 172 503 503 VAL VAL EEE . n 
C 3 173 GLY 173 504 504 GLY GLY EEE . n 
C 3 174 TYR 174 505 505 TYR TYR EEE . n 
C 3 175 GLN 175 506 506 GLN GLN EEE . n 
C 3 176 PRO 176 507 507 PRO PRO EEE . n 
C 3 177 TYR 177 508 508 TYR TYR EEE . n 
C 3 178 ARG 178 509 509 ARG ARG EEE . n 
C 3 179 VAL 179 510 510 VAL VAL EEE . n 
C 3 180 VAL 180 511 511 VAL VAL EEE . n 
C 3 181 VAL 181 512 512 VAL VAL EEE . n 
C 3 182 LEU 182 513 513 LEU LEU EEE . n 
C 3 183 SER 183 514 514 SER SER EEE . n 
C 3 184 PHE 184 515 515 PHE PHE EEE . n 
C 3 185 GLU 185 516 516 GLU GLU EEE . n 
C 3 186 LEU 186 517 517 LEU LEU EEE . n 
C 3 187 LEU 187 518 518 LEU LEU EEE . n 
C 3 188 HIS 188 519 519 HIS HIS EEE . n 
C 3 189 ALA 189 520 520 ALA ALA EEE . n 
C 3 190 PRO 190 521 521 PRO PRO EEE . n 
C 3 191 ALA 191 522 522 ALA ALA EEE . n 
C 3 192 THR 192 523 523 THR THR EEE . n 
C 3 193 VAL 193 524 524 VAL VAL EEE . n 
C 3 194 CYS 194 525 525 CYS CYS EEE . n 
C 3 195 GLY 195 526 526 GLY GLY EEE . n 
C 3 196 PRO 196 527 527 PRO PRO EEE . n 
C 3 197 LYS 197 528 528 LYS LYS EEE . n 
D 4 1   GLN 1   1   1   GLN GLN FFF . n 
D 4 2   VAL 2   2   2   VAL VAL FFF . n 
D 4 3   GLN 3   3   3   GLN GLN FFF . n 
D 4 4   LEU 4   4   4   LEU LEU FFF . n 
D 4 5   VAL 5   5   5   VAL VAL FFF . n 
D 4 6   GLU 6   6   6   GLU GLU FFF . n 
D 4 7   SER 7   7   7   SER SER FFF . n 
D 4 8   GLY 8   8   8   GLY GLY FFF . n 
D 4 9   GLY 9   9   9   GLY GLY FFF . n 
D 4 10  GLY 10  10  10  GLY GLY FFF . n 
D 4 11  LEU 11  11  11  LEU LEU FFF . n 
D 4 12  MET 12  12  12  MET MET FFF . n 
D 4 13  GLN 13  13  13  GLN GLN FFF . n 
D 4 14  ALA 14  14  14  ALA ALA FFF . n 
D 4 15  GLY 15  15  15  GLY GLY FFF . n 
D 4 16  GLY 16  16  16  GLY GLY FFF . n 
D 4 17  SER 17  17  17  SER SER FFF . n 
D 4 18  LEU 18  18  18  LEU LEU FFF . n 
D 4 19  ARG 19  19  19  ARG ARG FFF . n 
D 4 20  LEU 20  20  20  LEU LEU FFF . n 
D 4 21  SER 21  21  21  SER SER FFF . n 
D 4 22  CYS 22  22  22  CYS CYS FFF . n 
D 4 23  ALA 23  23  23  ALA ALA FFF . n 
D 4 24  VAL 24  24  24  VAL VAL FFF . n 
D 4 25  SER 25  25  25  SER SER FFF . n 
D 4 26  GLY 26  26  26  GLY GLY FFF . n 
D 4 27  ARG 27  27  27  ARG ARG FFF . n 
D 4 28  THR 28  28  28  THR THR FFF . n 
D 4 29  PHE 29  29  29  PHE PHE FFF . n 
D 4 30  SER 30  30  30  SER SER FFF . n 
D 4 31  THR 31  31  31  THR THR FFF . n 
D 4 32  ALA 32  32  32  ALA ALA FFF . n 
D 4 33  ALA 33  33  33  ALA ALA FFF . n 
D 4 34  MET 34  34  34  MET MET FFF . n 
D 4 35  GLY 35  35  35  GLY GLY FFF . n 
D 4 36  TRP 36  36  36  TRP TRP FFF . n 
D 4 37  PHE 37  37  37  PHE PHE FFF . n 
D 4 38  ARG 38  38  38  ARG ARG FFF . n 
D 4 39  GLN 39  39  39  GLN GLN FFF . n 
D 4 40  ALA 40  40  40  ALA ALA FFF . n 
D 4 41  PRO 41  41  41  PRO PRO FFF . n 
D 4 42  GLY 42  42  42  GLY GLY FFF . n 
D 4 43  LYS 43  43  43  LYS LYS FFF . n 
D 4 44  GLU 44  44  44  GLU GLU FFF . n 
D 4 45  ARG 45  45  45  ARG ARG FFF . n 
D 4 46  GLU 46  46  46  GLU GLU FFF . n 
D 4 47  PHE 47  47  47  PHE PHE FFF . n 
D 4 48  VAL 48  48  48  VAL VAL FFF . n 
D 4 49  ALA 49  49  49  ALA ALA FFF . n 
D 4 50  ALA 50  50  50  ALA ALA FFF . n 
D 4 51  ILE 51  51  51  ILE ILE FFF . n 
D 4 52  ARG 52  52  52  ARG ARG FFF . n 
D 4 53  TRP 53  53  53  TRP TRP FFF . n 
D 4 54  SER 54  54  54  SER SER FFF . n 
D 4 55  GLY 55  55  55  GLY GLY FFF . n 
D 4 56  GLY 56  56  56  GLY GLY FFF . n 
D 4 57  SER 57  57  57  SER SER FFF . n 
D 4 58  ALA 58  58  58  ALA ALA FFF . n 
D 4 59  TYR 59  59  59  TYR TYR FFF . n 
D 4 60  TYR 60  60  60  TYR TYR FFF . n 
D 4 61  ALA 61  61  61  ALA ALA FFF . n 
D 4 62  ASP 62  62  62  ASP ASP FFF . n 
D 4 63  SER 63  63  63  SER SER FFF . n 
D 4 64  VAL 64  64  64  VAL VAL FFF . n 
D 4 65  LYS 65  65  65  LYS LYS FFF . n 
D 4 66  GLY 66  66  66  GLY GLY FFF . n 
D 4 67  ARG 67  67  67  ARG ARG FFF . n 
D 4 68  PHE 68  68  68  PHE PHE FFF . n 
D 4 69  THR 69  69  69  THR THR FFF . n 
D 4 70  ILE 70  70  70  ILE ILE FFF . n 
D 4 71  SER 71  71  71  SER SER FFF . n 
D 4 72  ARG 72  72  72  ARG ARG FFF . n 
D 4 73  ASP 73  73  73  ASP ASP FFF . n 
D 4 74  LYS 74  74  74  LYS LYS FFF . n 
D 4 75  ALA 75  75  75  ALA ALA FFF . n 
D 4 76  LYS 76  76  76  LYS LYS FFF . n 
D 4 77  ASN 77  77  77  ASN ASN FFF . n 
D 4 78  THR 78  78  78  THR THR FFF . n 
D 4 79  VAL 79  79  79  VAL VAL FFF . n 
D 4 80  TYR 80  80  80  TYR TYR FFF . n 
D 4 81  LEU 81  81  81  LEU LEU FFF . n 
D 4 82  GLN 82  82  82  GLN GLN FFF . n 
D 4 83  MET 83  83  83  MET MET FFF . n 
D 4 84  ASN 84  84  84  ASN ASN FFF . n 
D 4 85  SER 85  85  85  SER SER FFF . n 
D 4 86  LEU 86  86  86  LEU LEU FFF . n 
D 4 87  LYS 87  87  87  LYS LYS FFF . n 
D 4 88  TYR 88  88  88  TYR TYR FFF . n 
D 4 89  GLU 89  89  89  GLU GLU FFF . n 
D 4 90  ASP 90  90  90  ASP ASP FFF . n 
D 4 91  THR 91  91  91  THR THR FFF . n 
D 4 92  ALA 92  92  92  ALA ALA FFF . n 
D 4 93  VAL 93  93  93  VAL VAL FFF . n 
D 4 94  TYR 94  94  94  TYR TYR FFF . n 
D 4 95  TYR 95  95  95  TYR TYR FFF . n 
D 4 96  CYS 96  96  96  CYS CYS FFF . n 
D 4 97  ALA 97  97  97  ALA ALA FFF . n 
D 4 98  GLN 98  98  98  GLN GLN FFF . n 
D 4 99  THR 99  99  99  THR THR FFF . n 
D 4 100 HIS 100 100 100 HIS HIS FFF . n 
D 4 101 TYR 101 101 101 TYR TYR FFF . n 
D 4 102 VAL 102 102 102 VAL VAL FFF . n 
D 4 103 SER 103 103 103 SER SER FFF . n 
D 4 104 TYR 104 104 104 TYR TYR FFF . n 
D 4 105 LEU 105 105 105 LEU LEU FFF . n 
D 4 106 LEU 106 106 106 LEU LEU FFF . n 
D 4 107 SER 107 107 107 SER SER FFF . n 
D 4 108 ASP 108 108 108 ASP ASP FFF . n 
D 4 109 TYR 109 109 109 TYR TYR FFF . n 
D 4 110 ALA 110 110 110 ALA ALA FFF . n 
D 4 111 THR 111 111 111 THR THR FFF . n 
D 4 112 TRP 112 112 112 TRP TRP FFF . n 
D 4 113 PRO 113 113 113 PRO PRO FFF . n 
D 4 114 TYR 114 114 114 TYR TYR FFF . n 
D 4 115 ASP 115 115 115 ASP ASP FFF . n 
D 4 116 TYR 116 116 116 TYR TYR FFF . n 
D 4 117 TRP 117 117 117 TRP TRP FFF . n 
D 4 118 GLY 118 118 118 GLY GLY FFF . n 
D 4 119 GLN 119 119 119 GLN GLN FFF . n 
D 4 120 GLY 120 120 120 GLY GLY FFF . n 
D 4 121 THR 121 121 121 THR THR FFF . n 
D 4 122 GLN 122 122 122 GLN GLN FFF . n 
D 4 123 VAL 123 123 123 VAL VAL FFF . n 
D 4 124 THR 124 124 124 THR THR FFF . n 
D 4 125 VAL 125 125 125 VAL VAL FFF . n 
D 4 126 SER 126 126 126 SER SER FFF . n 
D 4 127 SER 127 127 127 SER SER FFF . n 
D 4 128 LYS 128 128 128 LYS LYS FFF . n 
D 4 129 HIS 129 129 ?   ?   ?   FFF . n 
D 4 130 HIS 130 130 ?   ?   ?   FFF . n 
D 4 131 HIS 131 131 ?   ?   ?   FFF . n 
D 4 132 HIS 132 132 ?   ?   ?   FFF . n 
D 4 133 HIS 133 133 ?   ?   ?   FFF . n 
D 4 134 HIS 134 134 ?   ?   ?   FFF . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
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)' 6510  ? 
1 MORE         -35   ? 
1 'SSA (A^2)'  33960 ? 
# 
_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 2020-09-02 
2 'Structure model' 1 1 2020-09-16 
# 
_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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 21.2400 -32.6080 -52.8360  0.8045 ? 0.4208  ? 0.3793  ? 0.8055 ? 0.5013  ? 0.6448 ? 2.6597 ? 
-0.4119 ? -2.0767 ? 2.4890 ? 1.9829  ? 2.9376 ? 0.4842  ? 0.0381  ? 0.6667  ? -0.0637 ? -0.0698 ? 0.4182  ? -0.5798 ? -0.3661 ? 
-0.4144 ? 
2 'X-RAY DIFFRACTION' ? refined 19.3860 -45.3110 -39.5160  0.7090 ? 0.1125  ? 0.4336  ? 0.5765 ? 0.2537  ? 0.4918 ? 4.8350 ? 
-1.7169 ? -2.7547 ? 1.0817 ? 1.8806  ? 4.1466 ? 0.0385  ? -0.1652 ? -0.1541 ? 0.3322  ? -0.0645 ? 0.2715  ? 0.3703  ? -0.2009 ? 
0.0260  ? 
3 'X-RAY DIFFRACTION' ? refined 40.2430 -60.0630 -86.0950  0.3471 ? -0.0450 ? -0.0231 ? 0.8091 ? -0.1115 ? 0.1049 ? 3.7665 ? 
1.6413  ? 0.4344  ? 6.1422 ? 1.7619  ? 3.2516 ? -0.3634 ? 0.8443  ? -0.0714 ? -0.2389 ? 0.7744  ? -0.1956 ? -0.0859 ? -0.3469 ? 
-0.4111 ? 
4 'X-RAY DIFFRACTION' ? refined 44.7910 -67.0160 -122.0690 2.2600 ? -0.7234 ? 0.2571  ? 2.9487 ? -0.5278 ? 0.6839 ? 1.4255 ? 
-1.7493 ? 0.6797  ? 2.2119 ? -0.8065 ? 0.3569 ? 0.6456  ? 0.6357  ? 0.2229  ? -1.1106 ? -0.5932 ? -0.4475 ? 0.2691  ? 0.2289  ? 
-0.0524 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? HHH 0   ? ? ? HHH 219 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? LLL 1   ? ? ? LLL 219 ? ALL ? 
3 'X-RAY DIFFRACTION' 3 ? ? EEE 334 ? ? ? EEE 528 ? ALL ? 
4 'X-RAY DIFFRACTION' 4 ? ? FFF 1   ? ? ? FFF 128 ? ALL ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        4 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 CYS HHH 22  ? ? -160.24 103.10  
2  1 MET HHH 48  ? ? -91.06  -62.17  
3  1 ASP HHH 55  ? ? -146.79 16.53   
4  1 PRO HHH 62  ? ? -39.04  -28.58  
5  1 VAL HHH 117 ? ? -112.07 74.94   
6  1 ASP HHH 148 ? ? 58.05   82.79   
7  1 THR HHH 195 ? ? -111.73 -70.20  
8  1 LEU LLL 15  ? ? -34.33  142.48  
9  1 ASN LLL 35  ? ? -64.15  66.87   
10 1 ALA LLL 57  ? ? 72.92   -33.22  
11 1 ALA LLL 90  ? ? -172.91 -175.49 
12 1 ASN LLL 144 ? ? 58.73   74.47   
13 1 GLU LLL 149 ? ? -40.93  108.48  
14 1 ASP LLL 157 ? ? 77.12   37.15   
15 1 PHE EEE 377 ? ? -151.98 84.32   
16 1 ASN EEE 422 ? ? -123.71 -56.27  
17 1 HIS EEE 519 ? ? -96.33  42.14   
18 1 VAL FFF 48  ? ? -108.95 -62.57  
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   HHH 
_pdbx_validate_polymer_linkage.auth_comp_id_1   SER 
_pdbx_validate_polymer_linkage.auth_seq_id_1    132 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   HHH 
_pdbx_validate_polymer_linkage.auth_comp_id_2   GLY 
_pdbx_validate_polymer_linkage.auth_seq_id_2    137 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             3.83 
# 
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 ILE 332 ? C ILE 1   
2 1 Y 1 EEE THR 333 ? C THR 2   
3 1 Y 1 FFF HIS 129 ? D HIS 129 
4 1 Y 1 FFF HIS 130 ? D HIS 130 
5 1 Y 1 FFF HIS 131 ? D HIS 131 
6 1 Y 1 FFF HIS 132 ? D HIS 132 
7 1 Y 1 FFF HIS 133 ? D HIS 133 
8 1 Y 1 FFF HIS 134 ? D HIS 134 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Wellcome Trust'                                     'United Kingdom' '100209/Z/12/Z).' 1 
'Engineering and Physical Sciences Research Council' 'United Kingdom' RFI               2 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'Purified before xtals' 
# 
