data_7N9X
# 
_entry.id   7N9X 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.359 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7N9X         pdb_00007n9x 10.2210/pdb7n9x/pdb 
WWPDB D_1000257606 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7N9X 
_pdbx_database_status.recvd_initial_deposition_date   2021-06-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
'Gerber, E.E.'        1 0000-0002-1862-3586 
'Digianantonio, K.M.' 2 0000-0001-8881-7856 
'Tripler, T.N.'       3 0000-0001-9336-7271 
'Smaga, S.S.'         4 0000-0003-3469-2642 
'Summers, B.J.'       5 0000-0002-3099-8145 
'Xiong, Y.'           6 0000-0001-9625-9313 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'CA-targeting nanobody is a tool for studying HIV-1 capsid lattice interactions' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gerber, E.E.'        1 0000-0002-1862-3586 
primary 'Digianantonio, K.M.' 2 0000-0001-8881-7856 
primary 'Tripler, T.N.'       3 0000-0001-9336-7271 
primary 'Smaga, S.S.'         4 0000-0003-3469-2642 
primary 'Summers, B.J.'       5 0000-0002-3099-8145 
primary 'Xiong, Y.'           6 0000-0001-9625-9313 
# 
_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                     7N9X 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     127.950 
_cell.length_a_esd                 ? 
_cell.length_b                     137.850 
_cell.length_b_esd                 ? 
_cell.length_c                     313.832 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7N9X 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 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 'Capsid protein'                        24542.164 3 ?       ? 'UNP residues 133-354' ? 
2 polymer man Nanobody                                12373.908 1 ?       ? ?                      ? 
3 polymer man Nanobody                                12116.620 1 ?       ? ?                      ? 
4 polymer man Nanobody                                12284.817 1 ?       ? ?                      ? 
5 polymer man 'Peptidyl-prolyl cis-trans isomerase A' 18036.504 3 5.2.1.8 ? ?                      ? 
# 
_entity_name_com.entity_id   5 
_entity_name_com.name        'PPIase A,Cyclophilin A,Cyclosporin A-binding protein,Rotamase A' 
# 
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 
;PIVQNLQGQMVHQCISPRTLNAWVKVVEEKAFSPEVIPMFSALSCGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW
DRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEP
FRDYVDRFYKTLRAEQASQEVKNAATETLLVQNANPDCKTILKALGPGATLEEMMTACQGVG
;
;PIVQNLQGQMVHQCISPRTLNAWVKVVEEKAFSPEVIPMFSALSCGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW
DRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEP
FRDYVDRFYKTLRAEQASQEVKNAATETLLVQNANPDCKTILKALGPGATLEEMMTACQGVG
;
BBB,CCC,AAA ? 
2 'polypeptide(L)' no no 
;DVQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLAL
QMNRLKPEDTAVYYCFAALDT(UNK)(UNK)AYWGQGTQVTVS
;
;DVQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLAL
QMNRLKPEDTAVYYCFAALDTXXAYWGQGTQVTVS
;
FFF         ? 
3 'polypeptide(L)' no no 
;DVQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLAL
QMNRLKPEDTAVYYCFAALDTAYWGQGTQVTV
;
;DVQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLAL
QMNRLKPEDTAVYYCFAALDTAYWGQGTQVTV
;
EEE         ? 
4 'polypeptide(L)' no no 
;VQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLALQ
RNRLKPEDTAVYYCFAALDT(UNK)(UNK)AYWGQGTQVTVS
;
;VQLQESGGGLVQAGGSLRLSCAASGSISRFNAMGWWRQAPGKEREFVARIVKGFDPVLADSVKGRFTISIDSAENTLALQ
RNRLKPEDTAVYYCFAALDTXXAYWGQGTQVTVS
;
DDD         ? 
5 'polypeptide(L)' no no 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
GGG,HHH,III ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   ILE n 
1 3   VAL n 
1 4   GLN n 
1 5   ASN n 
1 6   LEU n 
1 7   GLN n 
1 8   GLY n 
1 9   GLN n 
1 10  MET n 
1 11  VAL n 
1 12  HIS n 
1 13  GLN n 
1 14  CYS n 
1 15  ILE n 
1 16  SER n 
1 17  PRO n 
1 18  ARG n 
1 19  THR n 
1 20  LEU n 
1 21  ASN n 
1 22  ALA n 
1 23  TRP n 
1 24  VAL n 
1 25  LYS n 
1 26  VAL n 
1 27  VAL n 
1 28  GLU n 
1 29  GLU n 
1 30  LYS n 
1 31  ALA n 
1 32  PHE n 
1 33  SER n 
1 34  PRO n 
1 35  GLU n 
1 36  VAL n 
1 37  ILE n 
1 38  PRO n 
1 39  MET n 
1 40  PHE n 
1 41  SER n 
1 42  ALA n 
1 43  LEU n 
1 44  SER n 
1 45  CYS n 
1 46  GLY n 
1 47  ALA n 
1 48  THR n 
1 49  PRO n 
1 50  GLN n 
1 51  ASP n 
1 52  LEU n 
1 53  ASN n 
1 54  THR n 
1 55  MET n 
1 56  LEU n 
1 57  ASN n 
1 58  THR n 
1 59  VAL n 
1 60  GLY n 
1 61  GLY n 
1 62  HIS n 
1 63  GLN n 
1 64  ALA n 
1 65  ALA n 
1 66  MET n 
1 67  GLN n 
1 68  MET n 
1 69  LEU n 
1 70  LYS n 
1 71  GLU n 
1 72  THR n 
1 73  ILE n 
1 74  ASN n 
1 75  GLU n 
1 76  GLU n 
1 77  ALA n 
1 78  ALA n 
1 79  GLU n 
1 80  TRP n 
1 81  ASP n 
1 82  ARG n 
1 83  LEU n 
1 84  HIS n 
1 85  PRO n 
1 86  VAL n 
1 87  HIS n 
1 88  ALA n 
1 89  GLY n 
1 90  PRO n 
1 91  ILE n 
1 92  ALA n 
1 93  PRO n 
1 94  GLY n 
1 95  GLN n 
1 96  MET n 
1 97  ARG n 
1 98  GLU n 
1 99  PRO n 
1 100 ARG n 
1 101 GLY n 
1 102 SER n 
1 103 ASP n 
1 104 ILE n 
1 105 ALA n 
1 106 GLY n 
1 107 THR n 
1 108 THR n 
1 109 SER n 
1 110 THR n 
1 111 LEU n 
1 112 GLN n 
1 113 GLU n 
1 114 GLN n 
1 115 ILE n 
1 116 GLY n 
1 117 TRP n 
1 118 MET n 
1 119 THR n 
1 120 HIS n 
1 121 ASN n 
1 122 PRO n 
1 123 PRO n 
1 124 ILE n 
1 125 PRO n 
1 126 VAL n 
1 127 GLY n 
1 128 GLU n 
1 129 ILE n 
1 130 TYR n 
1 131 LYS n 
1 132 ARG n 
1 133 TRP n 
1 134 ILE n 
1 135 ILE n 
1 136 LEU n 
1 137 GLY n 
1 138 LEU n 
1 139 ASN n 
1 140 LYS n 
1 141 ILE n 
1 142 VAL n 
1 143 ARG n 
1 144 MET n 
1 145 TYR n 
1 146 SER n 
1 147 PRO n 
1 148 THR n 
1 149 SER n 
1 150 ILE n 
1 151 LEU n 
1 152 ASP n 
1 153 ILE n 
1 154 ARG n 
1 155 GLN n 
1 156 GLY n 
1 157 PRO n 
1 158 LYS n 
1 159 GLU n 
1 160 PRO n 
1 161 PHE n 
1 162 ARG n 
1 163 ASP n 
1 164 TYR n 
1 165 VAL n 
1 166 ASP n 
1 167 ARG n 
1 168 PHE n 
1 169 TYR n 
1 170 LYS n 
1 171 THR n 
1 172 LEU n 
1 173 ARG n 
1 174 ALA n 
1 175 GLU n 
1 176 GLN n 
1 177 ALA n 
1 178 SER n 
1 179 GLN n 
1 180 GLU n 
1 181 VAL n 
1 182 LYS n 
1 183 ASN n 
1 184 ALA n 
1 185 ALA n 
1 186 THR n 
1 187 GLU n 
1 188 THR n 
1 189 LEU n 
1 190 LEU n 
1 191 VAL n 
1 192 GLN n 
1 193 ASN n 
1 194 ALA n 
1 195 ASN n 
1 196 PRO n 
1 197 ASP n 
1 198 CYS n 
1 199 LYS n 
1 200 THR n 
1 201 ILE n 
1 202 LEU n 
1 203 LYS n 
1 204 ALA n 
1 205 LEU n 
1 206 GLY n 
1 207 PRO n 
1 208 GLY n 
1 209 ALA n 
1 210 THR n 
1 211 LEU n 
1 212 GLU n 
1 213 GLU n 
1 214 MET n 
1 215 MET n 
1 216 THR n 
1 217 ALA n 
1 218 CYS n 
1 219 GLN n 
1 220 GLY n 
1 221 VAL n 
1 222 GLY n 
2 1   ASP n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  SER n 
2 28  ILE n 
2 29  SER n 
2 30  ARG n 
2 31  PHE n 
2 32  ASN n 
2 33  ALA n 
2 34  MET n 
2 35  GLY n 
2 36  TRP n 
2 37  TRP n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLU n 
2 45  ARG n 
2 46  GLU n 
2 47  PHE n 
2 48  VAL n 
2 49  ALA n 
2 50  ARG n 
2 51  ILE n 
2 52  VAL n 
2 53  LYS n 
2 54  GLY n 
2 55  PHE n 
2 56  ASP n 
2 57  PRO n 
2 58  VAL n 
2 59  LEU n 
2 60  ALA n 
2 61  ASP n 
2 62  SER n 
2 63  VAL n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ILE n 
2 72  ASP n 
2 73  SER n 
2 74  ALA n 
2 75  GLU n 
2 76  ASN n 
2 77  THR n 
2 78  LEU n 
2 79  ALA n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  ARG n 
2 85  LEU n 
2 86  LYS n 
2 87  PRO n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  PHE n 
2 97  ALA n 
2 98  ALA n 
2 99  LEU n 
2 100 ASP n 
2 101 THR n 
2 102 UNK n 
2 103 UNK n 
2 104 ALA n 
2 105 TYR n 
2 106 TRP n 
2 107 GLY n 
2 108 GLN n 
2 109 GLY n 
2 110 THR n 
2 111 GLN n 
2 112 VAL n 
2 113 THR n 
2 114 VAL n 
2 115 SER n 
3 1   ASP n 
3 2   VAL n 
3 3   GLN n 
3 4   LEU n 
3 5   GLN n 
3 6   GLU n 
3 7   SER n 
3 8   GLY n 
3 9   GLY n 
3 10  GLY n 
3 11  LEU n 
3 12  VAL n 
3 13  GLN n 
3 14  ALA n 
3 15  GLY n 
3 16  GLY n 
3 17  SER n 
3 18  LEU n 
3 19  ARG n 
3 20  LEU n 
3 21  SER n 
3 22  CYS n 
3 23  ALA n 
3 24  ALA n 
3 25  SER n 
3 26  GLY n 
3 27  SER n 
3 28  ILE n 
3 29  SER n 
3 30  ARG n 
3 31  PHE n 
3 32  ASN n 
3 33  ALA n 
3 34  MET n 
3 35  GLY n 
3 36  TRP n 
3 37  TRP n 
3 38  ARG n 
3 39  GLN n 
3 40  ALA n 
3 41  PRO n 
3 42  GLY n 
3 43  LYS n 
3 44  GLU n 
3 45  ARG n 
3 46  GLU n 
3 47  PHE n 
3 48  VAL n 
3 49  ALA n 
3 50  ARG n 
3 51  ILE n 
3 52  VAL n 
3 53  LYS n 
3 54  GLY n 
3 55  PHE n 
3 56  ASP n 
3 57  PRO n 
3 58  VAL n 
3 59  LEU n 
3 60  ALA n 
3 61  ASP n 
3 62  SER n 
3 63  VAL n 
3 64  LYS n 
3 65  GLY n 
3 66  ARG n 
3 67  PHE n 
3 68  THR n 
3 69  ILE n 
3 70  SER n 
3 71  ILE n 
3 72  ASP n 
3 73  SER n 
3 74  ALA n 
3 75  GLU n 
3 76  ASN n 
3 77  THR n 
3 78  LEU n 
3 79  ALA n 
3 80  LEU n 
3 81  GLN n 
3 82  MET n 
3 83  ASN n 
3 84  ARG n 
3 85  LEU n 
3 86  LYS n 
3 87  PRO n 
3 88  GLU n 
3 89  ASP n 
3 90  THR n 
3 91  ALA n 
3 92  VAL n 
3 93  TYR n 
3 94  TYR n 
3 95  CYS n 
3 96  PHE n 
3 97  ALA n 
3 98  ALA n 
3 99  LEU n 
3 100 ASP n 
3 101 THR n 
3 102 ALA n 
3 103 TYR n 
3 104 TRP n 
3 105 GLY n 
3 106 GLN n 
3 107 GLY n 
3 108 THR n 
3 109 GLN n 
3 110 VAL n 
3 111 THR n 
3 112 VAL n 
4 1   VAL n 
4 2   GLN n 
4 3   LEU n 
4 4   GLN n 
4 5   GLU n 
4 6   SER n 
4 7   GLY n 
4 8   GLY n 
4 9   GLY n 
4 10  LEU n 
4 11  VAL n 
4 12  GLN n 
4 13  ALA n 
4 14  GLY n 
4 15  GLY n 
4 16  SER n 
4 17  LEU n 
4 18  ARG n 
4 19  LEU n 
4 20  SER n 
4 21  CYS n 
4 22  ALA n 
4 23  ALA n 
4 24  SER n 
4 25  GLY n 
4 26  SER n 
4 27  ILE n 
4 28  SER n 
4 29  ARG n 
4 30  PHE n 
4 31  ASN n 
4 32  ALA n 
4 33  MET n 
4 34  GLY n 
4 35  TRP n 
4 36  TRP n 
4 37  ARG n 
4 38  GLN n 
4 39  ALA n 
4 40  PRO n 
4 41  GLY n 
4 42  LYS n 
4 43  GLU n 
4 44  ARG n 
4 45  GLU n 
4 46  PHE n 
4 47  VAL n 
4 48  ALA n 
4 49  ARG n 
4 50  ILE n 
4 51  VAL n 
4 52  LYS n 
4 53  GLY n 
4 54  PHE n 
4 55  ASP n 
4 56  PRO n 
4 57  VAL n 
4 58  LEU n 
4 59  ALA n 
4 60  ASP n 
4 61  SER n 
4 62  VAL n 
4 63  LYS n 
4 64  GLY n 
4 65  ARG n 
4 66  PHE n 
4 67  THR n 
4 68  ILE n 
4 69  SER n 
4 70  ILE n 
4 71  ASP n 
4 72  SER n 
4 73  ALA n 
4 74  GLU n 
4 75  ASN n 
4 76  THR n 
4 77  LEU n 
4 78  ALA n 
4 79  LEU n 
4 80  GLN n 
4 81  ARG n 
4 82  ASN n 
4 83  ARG n 
4 84  LEU n 
4 85  LYS n 
4 86  PRO n 
4 87  GLU n 
4 88  ASP n 
4 89  THR n 
4 90  ALA n 
4 91  VAL n 
4 92  TYR n 
4 93  TYR n 
4 94  CYS n 
4 95  PHE n 
4 96  ALA n 
4 97  ALA n 
4 98  LEU n 
4 99  ASP n 
4 100 THR n 
4 101 UNK n 
4 102 UNK n 
4 103 ALA n 
4 104 TYR n 
4 105 TRP n 
4 106 GLY n 
4 107 GLN n 
4 108 GLY n 
4 109 THR n 
4 110 GLN n 
4 111 VAL n 
4 112 THR n 
4 113 VAL n 
4 114 SER n 
5 1   MET n 
5 2   VAL n 
5 3   ASN n 
5 4   PRO n 
5 5   THR n 
5 6   VAL n 
5 7   PHE n 
5 8   PHE n 
5 9   ASP n 
5 10  ILE n 
5 11  ALA n 
5 12  VAL n 
5 13  ASP n 
5 14  GLY n 
5 15  GLU n 
5 16  PRO n 
5 17  LEU n 
5 18  GLY n 
5 19  ARG n 
5 20  VAL n 
5 21  SER n 
5 22  PHE n 
5 23  GLU n 
5 24  LEU n 
5 25  PHE n 
5 26  ALA n 
5 27  ASP n 
5 28  LYS n 
5 29  VAL n 
5 30  PRO n 
5 31  LYS n 
5 32  THR n 
5 33  ALA n 
5 34  GLU n 
5 35  ASN n 
5 36  PHE n 
5 37  ARG n 
5 38  ALA n 
5 39  LEU n 
5 40  SER n 
5 41  THR n 
5 42  GLY n 
5 43  GLU n 
5 44  LYS n 
5 45  GLY n 
5 46  PHE n 
5 47  GLY n 
5 48  TYR n 
5 49  LYS n 
5 50  GLY n 
5 51  SER n 
5 52  CYS n 
5 53  PHE n 
5 54  HIS n 
5 55  ARG n 
5 56  ILE n 
5 57  ILE n 
5 58  PRO n 
5 59  GLY n 
5 60  PHE n 
5 61  MET n 
5 62  CYS n 
5 63  GLN n 
5 64  GLY n 
5 65  GLY n 
5 66  ASP n 
5 67  PHE n 
5 68  THR n 
5 69  ARG n 
5 70  HIS n 
5 71  ASN n 
5 72  GLY n 
5 73  THR n 
5 74  GLY n 
5 75  GLY n 
5 76  LYS n 
5 77  SER n 
5 78  ILE n 
5 79  TYR n 
5 80  GLY n 
5 81  GLU n 
5 82  LYS n 
5 83  PHE n 
5 84  GLU n 
5 85  ASP n 
5 86  GLU n 
5 87  ASN n 
5 88  PHE n 
5 89  ILE n 
5 90  LEU n 
5 91  LYS n 
5 92  HIS n 
5 93  THR n 
5 94  GLY n 
5 95  PRO n 
5 96  GLY n 
5 97  ILE n 
5 98  LEU n 
5 99  SER n 
5 100 MET n 
5 101 ALA n 
5 102 ASN n 
5 103 ALA n 
5 104 GLY n 
5 105 PRO n 
5 106 ASN n 
5 107 THR n 
5 108 ASN n 
5 109 GLY n 
5 110 SER n 
5 111 GLN n 
5 112 PHE n 
5 113 PHE n 
5 114 ILE n 
5 115 CYS n 
5 116 THR n 
5 117 ALA n 
5 118 LYS n 
5 119 THR n 
5 120 GLU n 
5 121 TRP n 
5 122 LEU n 
5 123 ASP n 
5 124 GLY n 
5 125 LYS n 
5 126 HIS n 
5 127 VAL n 
5 128 VAL n 
5 129 PHE n 
5 130 GLY n 
5 131 LYS n 
5 132 VAL n 
5 133 LYS n 
5 134 GLU n 
5 135 GLY n 
5 136 MET n 
5 137 ASN n 
5 138 ILE n 
5 139 VAL n 
5 140 GLU n 
5 141 ALA n 
5 142 MET n 
5 143 GLU n 
5 144 ARG n 
5 145 PHE n 
5 146 GLY n 
5 147 SER n 
5 148 ARG n 
5 149 ASN n 
5 150 GLY n 
5 151 LYS n 
5 152 THR n 
5 153 SER n 
5 154 LYS n 
5 155 LYS n 
5 156 ILE n 
5 157 THR n 
5 158 ILE n 
5 159 ALA n 
5 160 ASP n 
5 161 CYS n 
5 162 GLY n 
5 163 GLN n 
5 164 LEU n 
5 165 GLU 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' 1 222 HIV-1 ? gag          ? ? ? ? ? ? 'Human immunodeficiency virus 1' 11676 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 115 Llama ? ?            ? ? ? ? ? ? 'Lama glama'                     9844  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 112 Llama ? ?            ? ? ? ? ? ? 'Lama glama'                     9844  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 114 Llama ? ?            ? ? ? ? ? ? 'Lama glama'                     9844  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 165 Human ? 'PPIA, CYPA' ? ? ? ? ? ? 'Homo sapiens'                   9606  ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP B6DRA0_9HIV1 B6DRA0 ? 1 
;PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW
DRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEP
FRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVG
;
133 
2 PDB 7N9X         7N9X   ? 2 ? 1   
3 PDB 7N9X         7N9X   ? 3 ? 1   
4 PDB 7N9X         7N9X   ? 4 ? 1   
5 UNP PPIA_HUMAN   P62937 ? 5 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
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 7N9X BBB 1 ? 222 ? B6DRA0 133 ? 354 ? 1 222 
2 1 7N9X CCC 1 ? 222 ? B6DRA0 133 ? 354 ? 1 222 
3 1 7N9X AAA 1 ? 222 ? B6DRA0 133 ? 354 ? 1 222 
4 2 7N9X FFF 1 ? 115 ? 7N9X   1   ? 112 ? 1 112 
5 3 7N9X EEE 1 ? 112 ? 7N9X   1   ? 111 ? 1 111 
6 4 7N9X DDD 1 ? 114 ? 7N9X   2   ? 112 ? 2 112 
7 5 7N9X GGG 1 ? 165 ? P62937 1   ? 165 ? 1 165 
8 5 7N9X HHH 1 ? 165 ? P62937 1   ? 165 ? 1 165 
9 5 7N9X III 1 ? 165 ? P62937 1   ? 165 ? 1 165 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7N9X CYS BBB 14  ? UNP B6DRA0 ALA 146 conflict 14  1  
1 7N9X CYS BBB 45  ? UNP B6DRA0 GLU 177 conflict 45  2  
1 7N9X ALA BBB 184 ? UNP B6DRA0 TRP 316 conflict 184 3  
1 7N9X ALA BBB 185 ? UNP B6DRA0 MET 317 conflict 185 4  
2 7N9X CYS CCC 14  ? UNP B6DRA0 ALA 146 conflict 14  5  
2 7N9X CYS CCC 45  ? UNP B6DRA0 GLU 177 conflict 45  6  
2 7N9X ALA CCC 184 ? UNP B6DRA0 TRP 316 conflict 184 7  
2 7N9X ALA CCC 185 ? UNP B6DRA0 MET 317 conflict 185 8  
3 7N9X CYS AAA 14  ? UNP B6DRA0 ALA 146 conflict 14  9  
3 7N9X CYS AAA 45  ? UNP B6DRA0 GLU 177 conflict 45  10 
3 7N9X ALA AAA 184 ? UNP B6DRA0 TRP 316 conflict 184 11 
3 7N9X ALA AAA 185 ? UNP B6DRA0 MET 317 conflict 185 12 
# 
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 
UNK 'L-peptide linking' . UNKNOWN         ? 'C4 H9 N O2'     103.120 
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                   7N9X 
_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            4.23 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         70.93 
_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          MICROBATCH 
_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            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Bis-Tris propane, pH 6.8, 15% PEG3350, 200 mM sodium' 
_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         2018-10-29 
_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   1.0711 
_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                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0711 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7N9X 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.500 
_reflns.d_resolution_low                               50.000 
_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                                     33153 
_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                           95.900 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.300 
_reflns.pdbx_Rmerge_I_obs                              0.182 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.000 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.006 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.216 
_reflns.pdbx_Rpim_I_all                                0.114 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       109451 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
3.500 3.560  ? ? ? ? ? ? 1676 98.700 ? ? ? ? 1.179 ? ? ? ? ? ? ? ? 3.300 ? 1.012 ? ? 1.405 0.748 ? 1  1 0.380 ? ? ? ? ? ? ? ? ? ? 
3.560 3.630  ? ? ? ? ? ? 1682 98.400 ? ? ? ? 1.014 ? ? ? ? ? ? ? ? 3.300 ? 1.020 ? ? 1.210 0.645 ? 2  1 0.457 ? ? ? ? ? ? ? ? ? ? 
3.630 3.690  ? ? ? ? ? ? 1687 98.900 ? ? ? ? 0.916 ? ? ? ? ? ? ? ? 3.300 ? 1.058 ? ? 1.0   0.582 ? 3  1 0.404 ? ? ? ? ? ? ? ? ? ? 
3.690 3.770  ? ? ? ? ? ? 1654 98.000 ? ? ? ? 0.777 ? ? ? ? ? ? ? ? 3.300 ? 0.972 ? ? 0.926 0.491 ? 4  1 0.633 ? ? ? ? ? ? ? ? ? ? 
3.770 3.850  ? ? ? ? ? ? 1675 97.200 ? ? ? ? 0.782 ? ? ? ? ? ? ? ? 3.300 ? 0.999 ? ? 0.931 0.494 ? 5  1 0.658 ? ? ? ? ? ? ? ? ? ? 
3.850 3.940  ? ? ? ? ? ? 1647 96.300 ? ? ? ? 0.603 ? ? ? ? ? ? ? ? 3.100 ? 1.157 ? ? 0.724 0.390 ? 6  1 0.690 ? ? ? ? ? ? ? ? ? ? 
3.940 4.040  ? ? ? ? ? ? 1639 95.200 ? ? ? ? 0.513 ? ? ? ? ? ? ? ? 3.100 ? 1.005 ? ? 0.613 0.327 ? 7  1 0.778 ? ? ? ? ? ? ? ? ? ? 
4.040 4.150  ? ? ? ? ? ? 1471 86.400 ? ? ? ? 0.409 ? ? ? ? ? ? ? ? 3.100 ? 0.964 ? ? 0.485 0.252 ? 8  1 0.869 ? ? ? ? ? ? ? ? ? ? 
4.150 4.270  ? ? ? ? ? ? 1665 97.700 ? ? ? ? 0.347 ? ? ? ? ? ? ? ? 3.300 ? 0.969 ? ? 0.410 0.214 ? 9  1 0.899 ? ? ? ? ? ? ? ? ? ? 
4.270 4.410  ? ? ? ? ? ? 1683 99.100 ? ? ? ? 0.279 ? ? ? ? ? ? ? ? 3.400 ? 1.040 ? ? 0.330 0.172 ? 10 1 0.930 ? ? ? ? ? ? ? ? ? ? 
4.410 4.570  ? ? ? ? ? ? 1710 98.600 ? ? ? ? 0.223 ? ? ? ? ? ? ? ? 3.400 ? 0.996 ? ? 0.263 0.137 ? 11 1 0.955 ? ? ? ? ? ? ? ? ? ? 
4.570 4.750  ? ? ? ? ? ? 1677 97.700 ? ? ? ? 0.191 ? ? ? ? ? ? ? ? 3.400 ? 1.023 ? ? 0.226 0.118 ? 12 1 0.970 ? ? ? ? ? ? ? ? ? ? 
4.750 4.970  ? ? ? ? ? ? 1700 97.900 ? ? ? ? 0.171 ? ? ? ? ? ? ? ? 3.300 ? 0.975 ? ? 0.203 0.107 ? 13 1 0.976 ? ? ? ? ? ? ? ? ? ? 
4.970 5.230  ? ? ? ? ? ? 1651 95.900 ? ? ? ? 0.185 ? ? ? ? ? ? ? ? 3.200 ? 0.967 ? ? 0.221 0.118 ? 14 1 0.964 ? ? ? ? ? ? ? ? ? ? 
5.230 5.550  ? ? ? ? ? ? 1506 87.200 ? ? ? ? 0.167 ? ? ? ? ? ? ? ? 3.200 ? 1.002 ? ? 0.198 0.103 ? 15 1 0.968 ? ? ? ? ? ? ? ? ? ? 
5.550 5.980  ? ? ? ? ? ? 1710 97.600 ? ? ? ? 0.160 ? ? ? ? ? ? ? ? 3.500 ? 1.010 ? ? 0.189 0.098 ? 16 1 0.968 ? ? ? ? ? ? ? ? ? ? 
5.980 6.580  ? ? ? ? ? ? 1685 97.600 ? ? ? ? 0.119 ? ? ? ? ? ? ? ? 3.500 ? 1.021 ? ? 0.141 0.073 ? 17 1 0.983 ? ? ? ? ? ? ? ? ? ? 
6.580 7.530  ? ? ? ? ? ? 1686 95.600 ? ? ? ? 0.083 ? ? ? ? ? ? ? ? 3.300 ? 1.089 ? ? 0.099 0.052 ? 18 1 0.989 ? ? ? ? ? ? ? ? ? ? 
7.530 9.480  ? ? ? ? ? ? 1614 90.400 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 3.300 ? 0.899 ? ? 0.060 0.031 ? 19 1 0.995 ? ? ? ? ? ? ? ? ? ? 
9.480 50.000 ? ? ? ? ? ? 1735 93.200 ? ? ? ? 0.045 ? ? ? ? ? ? ? ? 3.300 ? 0.931 ? ? 0.053 0.027 ? 20 1 0.996 ? ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.400 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            2.014 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -2.414 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               180.204 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.915 
_refine.correlation_coeff_Fo_to_Fc_free          0.924 
_refine.details                                  'Hydrogens have not been used' 
_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                                 7N9X 
_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                            3.511 
_refine.ls_d_res_low                             49.581 
_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                     33142 
_refine.ls_number_reflns_R_free                  1668 
_refine.ls_number_reflns_R_work                  31474 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.389 
_refine.ls_percent_reflns_R_free                 5.033 
_refine.ls_R_factor_all                          0.246 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2699 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2449 
_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                      'PDB entries 5O2U & 3H47' 
_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                  0.593 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             97.604 
_refine.overall_SU_ML                            0.616 
_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        11458 
_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               11458 
_refine_hist.d_res_high                       3.511 
_refine_hist.d_res_low                        49.581 
# 
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  0.012   11689 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.094  0.010   15267 ? r_ext_dist_refined_d           ? ? 
'X-RAY DIFFRACTION' ? 1.602  1.639   15797 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.008  5.000   1475  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 31.926 22.687  588   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.578 15.000  1984  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.919 15.000  70    ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.075  0.200   1526  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020   8892  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.232  0.200   5166  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.321  0.200   8133  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.190  0.200   325   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.314  0.200   79    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.390  0.200   4     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 7.218  10.227  5938  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 11.904 15.324  7401  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 7.575  10.283  5750  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 11.721 15.292  8396  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 19.575 195.144 47452 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 0.158  0.050   6265  ? r_ncsr_local_group_1           ? ? 
'X-RAY DIFFRACTION' ? 0.158  0.050   6305  ? r_ncsr_local_group_2           ? ? 
'X-RAY DIFFRACTION' ? 0.152  0.050   6307  ? r_ncsr_local_group_3           ? ? 
'X-RAY DIFFRACTION' ? 0.194  0.050   2874  ? r_ncsr_local_group_4           ? ? 
'X-RAY DIFFRACTION' ? 0.231  0.050   2716  ? r_ncsr_local_group_5           ? ? 
'X-RAY DIFFRACTION' ? 0.220  0.050   2690  ? r_ncsr_local_group_6           ? ? 
'X-RAY DIFFRACTION' ? 0.180  0.050   4376  ? r_ncsr_local_group_7           ? ? 
'X-RAY DIFFRACTION' ? 0.196  0.050   4483  ? r_ncsr_local_group_8           ? ? 
'X-RAY DIFFRACTION' ? 0.184  0.050   4400  ? r_ncsr_local_group_9           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1  ? ? 0.15824 ? 0.05006 1  'Local ncs' ? BBB ? ? ? 1 
'X-RAY DIFFRACTION' 2  ? ? 0.15824 ? 0.05006 2  'Local ncs' ? CCC ? ? ? 1 
'X-RAY DIFFRACTION' 3  ? ? 0.15758 ? 0.05006 3  'Local ncs' ? BBB ? ? ? 2 
'X-RAY DIFFRACTION' 4  ? ? 0.15758 ? 0.05006 4  'Local ncs' ? AAA ? ? ? 2 
'X-RAY DIFFRACTION' 5  ? ? 0.15199 ? 0.05006 5  'Local ncs' ? CCC ? ? ? 3 
'X-RAY DIFFRACTION' 6  ? ? 0.15199 ? 0.05006 6  'Local ncs' ? AAA ? ? ? 3 
'X-RAY DIFFRACTION' 7  ? ? 0.19448 ? 0.05006 7  'Local ncs' ? FFF ? ? ? 4 
'X-RAY DIFFRACTION' 8  ? ? 0.19448 ? 0.05006 8  'Local ncs' ? EEE ? ? ? 4 
'X-RAY DIFFRACTION' 9  ? ? 0.23119 ? 0.05005 9  'Local ncs' ? FFF ? ? ? 5 
'X-RAY DIFFRACTION' 10 ? ? 0.23119 ? 0.05005 10 'Local ncs' ? DDD ? ? ? 5 
'X-RAY DIFFRACTION' 11 ? ? 0.22044 ? 0.05005 11 'Local ncs' ? EEE ? ? ? 6 
'X-RAY DIFFRACTION' 12 ? ? 0.22044 ? 0.05005 12 'Local ncs' ? DDD ? ? ? 6 
'X-RAY DIFFRACTION' 13 ? ? 0.17981 ? 0.05007 13 'Local ncs' ? GGG ? ? ? 7 
'X-RAY DIFFRACTION' 14 ? ? 0.17981 ? 0.05007 14 'Local ncs' ? HHH ? ? ? 7 
'X-RAY DIFFRACTION' 15 ? ? 0.19638 ? 0.05007 15 'Local ncs' ? GGG ? ? ? 8 
'X-RAY DIFFRACTION' 16 ? ? 0.19638 ? 0.05007 16 'Local ncs' ? III ? ? ? 8 
'X-RAY DIFFRACTION' 17 ? ? 0.18436 ? 0.05007 17 'Local ncs' ? HHH ? ? ? 9 
'X-RAY DIFFRACTION' 18 ? ? 0.18436 ? 0.05007 18 'Local ncs' ? III ? ? ? 9 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 3.511  3.602  2538 . 90  1911 78.8416 . 0.355 . 0.359 . 0.355 . . . . . 0.351 . 20 . 0.530 0.531 
'X-RAY DIFFRACTION' 3.602  3.700  2474 . 134 2301 98.4236 . 0.352 . 0.373 . 0.351 . . . . . 0.347 . 20 . 0.632 0.624 
'X-RAY DIFFRACTION' 3.700  3.807  2449 . 124 2282 98.2442 . 0.314 . 0.356 . 0.312 . . . . . 0.306 . 20 . 0.715 0.704 
'X-RAY DIFFRACTION' 3.807  3.923  2337 . 103 2169 97.2187 . 0.322 . 0.340 . 0.321 . . . . . 0.306 . 20 . 0.765 0.771 
'X-RAY DIFFRACTION' 3.923  4.051  2295 . 103 2092 95.6427 . 0.282 . 0.329 . 0.279 . . . . . 0.265 . 20 . 0.834 0.798 
'X-RAY DIFFRACTION' 4.051  4.192  2198 . 90  1841 87.8526 . 0.261 . 0.250 . 0.261 . . . . . 0.239 . 20 . 0.881 0.881 
'X-RAY DIFFRACTION' 4.192  4.349  2137 . 126 1974 98.2686 . 0.243 . 0.276 . 0.241 . . . . . 0.221 . 20 . 0.891 0.877 
'X-RAY DIFFRACTION' 4.349  4.525  2050 . 97  1935 99.1219 . 0.229 . 0.269 . 0.227 . . . . . 0.203 . 20 . 0.907 0.913 
'X-RAY DIFFRACTION' 4.525  4.725  1978 . 95  1844 98.0283 . 0.218 . 0.253 . 0.216 . . . . . 0.191 . 20 . 0.918 0.901 
'X-RAY DIFFRACTION' 4.725  4.953  1916 . 90  1779 97.5470 . 0.206 . 0.243 . 0.204 . . . . . 0.182 . 20 . 0.927 0.917 
'X-RAY DIFFRACTION' 4.953  5.218  1812 . 86  1669 96.8543 . 0.225 . 0.274 . 0.222 . . . . . 0.193 . 20 . 0.906 0.897 
'X-RAY DIFFRACTION' 5.218  5.531  1705 . 81  1411 87.5073 . 0.266 . 0.342 . 0.262 . . . . . 0.225 . 20 . 0.881 0.828 
'X-RAY DIFFRACTION' 5.531  5.907  1620 . 64  1502 96.6667 . 0.259 . 0.282 . 0.258 . . . . . 0.225 . 20 . 0.878 0.830 
'X-RAY DIFFRACTION' 5.907  6.373  1508 . 78  1392 97.4801 . 0.251 . 0.303 . 0.248 . . . . . 0.211 . 20 . 0.907 0.890 
'X-RAY DIFFRACTION' 6.373  6.970  1402 . 61  1300 97.0756 . 0.255 . 0.247 . 0.255 . . . . . 0.233 . 20 . 0.908 0.901 
'X-RAY DIFFRACTION' 6.970  7.773  1265 . 68  1123 94.1502 . 0.233 . 0.256 . 0.231 . . . . . 0.220 . 20 . 0.922 0.921 
'X-RAY DIFFRACTION' 7.773  8.939  1143 . 53  946  87.4016 . 0.182 . 0.229 . 0.180 . . . . . 0.187 . 20 . 0.957 0.947 
'X-RAY DIFFRACTION' 8.939  10.861 979  . 53  899  97.2421 . 0.165 . 0.195 . 0.163 . . . . . 0.178 . 20 . 0.969 0.966 
'X-RAY DIFFRACTION' 10.861 15.004 784  . 47  691  94.1327 . 0.185 . 0.209 . 0.184 . . . . . 0.203 . 20 . 0.964 0.958 
'X-RAY DIFFRACTION' 15.004 49.581 501  . 25  413  87.4251 . 0.268 . 0.197 . 0.274 . . . . . 0.326 . 20 . 0.938 0.970 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1  1 BBB 
2  1 CCC 
3  2 BBB 
4  2 AAA 
5  3 CCC 
6  3 AAA 
7  4 FFF 
8  4 EEE 
9  5 FFF 
10 5 DDD 
11 6 EEE 
12 6 DDD 
13 7 GGG 
14 7 HHH 
15 8 GGG 
16 8 III 
17 9 HHH 
18 9 III 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1  BBB 1 BBB 218 1  ? ? ? ? ? ? ? ? ? 1 ? 
2  CCC 1 CCC 218 2  ? ? ? ? ? ? ? ? ? 1 ? 
3  BBB 1 BBB 219 3  ? ? ? ? ? ? ? ? ? 2 ? 
4  AAA 1 AAA 219 4  ? ? ? ? ? ? ? ? ? 2 ? 
5  CCC 1 CCC 218 5  ? ? ? ? ? ? ? ? ? 3 ? 
6  AAA 1 AAA 218 6  ? ? ? ? ? ? ? ? ? 3 ? 
7  FFF 1 FFF 110 7  ? ? ? ? ? ? ? ? ? 4 ? 
8  EEE 1 EEE 110 8  ? ? ? ? ? ? ? ? ? 4 ? 
9  FFF 2 FFF 111 9  ? ? ? ? ? ? ? ? ? 5 ? 
10 DDD 2 DDD 111 10 ? ? ? ? ? ? ? ? ? 5 ? 
11 EEE 2 EEE 110 11 ? ? ? ? ? ? ? ? ? 6 ? 
12 DDD 2 DDD 110 12 ? ? ? ? ? ? ? ? ? 6 ? 
13 GGG 3 GGG 164 13 ? ? ? ? ? ? ? ? ? 7 ? 
14 HHH 3 HHH 164 14 ? ? ? ? ? ? ? ? ? 7 ? 
15 GGG 1 GGG 165 15 ? ? ? ? ? ? ? ? ? 8 ? 
16 III 1 III 165 16 ? ? ? ? ? ? ? ? ? 8 ? 
17 HHH 3 HHH 164 17 ? ? ? ? ? ? ? ? ? 9 ? 
18 III 3 III 164 18 ? ? ? ? ? ? ? ? ? 9 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 'Local NCS retraints between domains:       1       2' 
2 'Local NCS retraints between domains:       3       4' 
3 'Local NCS retraints between domains:       5       6' 
4 'Local NCS retraints between domains:       7       8' 
5 'Local NCS retraints between domains:       9      10' 
6 'Local NCS retraints between domains:      11      12' 
7 'Local NCS retraints between domains:      13      14' 
8 'Local NCS retraints between domains:      15      16' 
9 'Local NCS retraints between domains:      17      18' 
# 
_struct.entry_id                     7N9X 
_struct.title                        'CA-targeting nanobody is a tool for studying HIV-1 capsid lattice interactions' 
_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        7N9X 
_struct_keywords.text            'HIV-1, hexamer, nanobody, CypA, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
# 
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 SER A 16  ? ALA A 31  ? SER BBB 16  ALA BBB 31  1 ? 16 
HELX_P HELX_P2  AA2 GLU A 35  ? SER A 44  ? GLU BBB 35  SER BBB 44  1 ? 10 
HELX_P HELX_P3  AA3 THR A 48  ? THR A 58  ? THR BBB 48  THR BBB 58  1 ? 11 
HELX_P HELX_P4  AA4 HIS A 62  ? HIS A 84  ? HIS BBB 62  HIS BBB 84  1 ? 23 
HELX_P HELX_P5  AA5 ARG A 100 ? ALA A 105 ? ARG BBB 100 ALA BBB 105 1 ? 6  
HELX_P HELX_P6  AA6 THR A 110 ? THR A 119 ? THR BBB 110 THR BBB 119 1 ? 10 
HELX_P HELX_P7  AA7 PRO A 125 ? TYR A 145 ? PRO BBB 125 TYR BBB 145 1 ? 21 
HELX_P HELX_P8  AA8 SER A 149 ? ILE A 153 ? SER BBB 149 ILE BBB 153 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 160 ? GLU A 175 ? PRO BBB 160 GLU BBB 175 1 ? 16 
HELX_P HELX_P10 AB1 GLU A 180 ? ALA A 185 ? GLU BBB 180 ALA BBB 185 1 ? 6  
HELX_P HELX_P11 AB2 ALA A 185 ? ASN A 193 ? ALA BBB 185 ASN BBB 193 1 ? 9  
HELX_P HELX_P12 AB3 ASN A 195 ? GLY A 206 ? ASN BBB 195 GLY BBB 206 1 ? 12 
HELX_P HELX_P13 AB4 THR A 210 ? CYS A 218 ? THR BBB 210 CYS BBB 218 1 ? 9  
HELX_P HELX_P14 AB5 SER B 16  ? ALA B 31  ? SER CCC 16  ALA CCC 31  1 ? 16 
HELX_P HELX_P15 AB6 GLU B 35  ? SER B 44  ? GLU CCC 35  SER CCC 44  1 ? 10 
HELX_P HELX_P16 AB7 THR B 48  ? THR B 58  ? THR CCC 48  THR CCC 58  1 ? 11 
HELX_P HELX_P17 AB8 HIS B 62  ? HIS B 84  ? HIS CCC 62  HIS CCC 84  1 ? 23 
HELX_P HELX_P18 AB9 ARG B 100 ? ALA B 105 ? ARG CCC 100 ALA CCC 105 1 ? 6  
HELX_P HELX_P19 AC1 THR B 110 ? THR B 119 ? THR CCC 110 THR CCC 119 1 ? 10 
HELX_P HELX_P20 AC2 PRO B 125 ? TYR B 145 ? PRO CCC 125 TYR CCC 145 1 ? 21 
HELX_P HELX_P21 AC3 SER B 149 ? ILE B 153 ? SER CCC 149 ILE CCC 153 5 ? 5  
HELX_P HELX_P22 AC4 PRO B 160 ? GLN B 176 ? PRO CCC 160 GLN CCC 176 1 ? 17 
HELX_P HELX_P23 AC5 SER B 178 ? ASN B 193 ? SER CCC 178 ASN CCC 193 1 ? 16 
HELX_P HELX_P24 AC6 ASN B 195 ? GLY B 206 ? ASN CCC 195 GLY CCC 206 1 ? 12 
HELX_P HELX_P25 AC7 THR B 210 ? CYS B 218 ? THR CCC 210 CYS CCC 218 1 ? 9  
HELX_P HELX_P26 AC8 SER C 16  ? ALA C 31  ? SER AAA 16  ALA AAA 31  1 ? 16 
HELX_P HELX_P27 AC9 GLU C 35  ? SER C 44  ? GLU AAA 35  SER AAA 44  1 ? 10 
HELX_P HELX_P28 AD1 THR C 48  ? THR C 58  ? THR AAA 48  THR AAA 58  1 ? 11 
HELX_P HELX_P29 AD2 HIS C 62  ? HIS C 84  ? HIS AAA 62  HIS AAA 84  1 ? 23 
HELX_P HELX_P30 AD3 ARG C 100 ? ALA C 105 ? ARG AAA 100 ALA AAA 105 1 ? 6  
HELX_P HELX_P31 AD4 THR C 110 ? THR C 119 ? THR AAA 110 THR AAA 119 1 ? 10 
HELX_P HELX_P32 AD5 PRO C 125 ? TYR C 145 ? PRO AAA 125 TYR AAA 145 1 ? 21 
HELX_P HELX_P33 AD6 SER C 149 ? ILE C 153 ? SER AAA 149 ILE AAA 153 5 ? 5  
HELX_P HELX_P34 AD7 PRO C 160 ? GLU C 175 ? PRO AAA 160 GLU AAA 175 1 ? 16 
HELX_P HELX_P35 AD8 GLN C 176 ? SER C 178 ? GLN AAA 176 SER AAA 178 5 ? 3  
HELX_P HELX_P36 AD9 ALA C 185 ? ASN C 193 ? ALA AAA 185 ASN AAA 193 1 ? 9  
HELX_P HELX_P37 AE1 ASN C 195 ? LEU C 205 ? ASN AAA 195 LEU AAA 205 1 ? 11 
HELX_P HELX_P38 AE2 THR C 210 ? CYS C 218 ? THR AAA 210 CYS AAA 218 1 ? 9  
HELX_P HELX_P39 AE3 SER D 27  ? PHE D 31  ? SER FFF 27  PHE FFF 31  5 ? 5  
HELX_P HELX_P40 AE4 LYS D 86  ? THR D 90  ? LYS FFF 83  THR FFF 87  5 ? 5  
HELX_P HELX_P41 AE5 SER E 27  ? PHE E 31  ? SER EEE 27  PHE EEE 31  5 ? 5  
HELX_P HELX_P42 AE6 ALA E 60  ? GLY E 65  ? ALA EEE 60  GLY EEE 65  1 ? 6  
HELX_P HELX_P43 AE7 LYS E 86  ? THR E 90  ? LYS EEE 83  THR EEE 87  5 ? 5  
HELX_P HELX_P44 AE8 SER F 26  ? PHE F 30  ? SER DDD 27  PHE DDD 31  5 ? 5  
HELX_P HELX_P45 AE9 LYS F 85  ? THR F 89  ? LYS DDD 83  THR DDD 87  5 ? 5  
HELX_P HELX_P46 AF1 VAL G 29  ? GLY G 42  ? VAL GGG 29  GLY GGG 42  1 ? 14 
HELX_P HELX_P47 AF2 THR G 119 ? ASP G 123 ? THR GGG 119 ASP GGG 123 5 ? 5  
HELX_P HELX_P48 AF3 GLY G 135 ? ARG G 144 ? GLY GGG 135 ARG GGG 144 1 ? 10 
HELX_P HELX_P49 AF4 VAL H 29  ? GLY H 42  ? VAL HHH 29  GLY HHH 42  1 ? 14 
HELX_P HELX_P50 AF5 THR H 119 ? ASP H 123 ? THR HHH 119 ASP HHH 123 5 ? 5  
HELX_P HELX_P51 AF6 GLY H 135 ? ARG H 144 ? GLY HHH 135 ARG HHH 144 1 ? 10 
HELX_P HELX_P52 AF7 VAL I 29  ? GLY I 42  ? VAL III 29  GLY III 42  1 ? 14 
HELX_P HELX_P53 AF8 THR I 119 ? ASP I 123 ? THR III 119 ASP III 123 5 ? 5  
HELX_P HELX_P54 AF9 GLY I 135 ? ARG I 144 ? GLY III 135 ARG III 144 1 ? 10 
# 
_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 14 SG ? ? ? 1_555 C CYS 45 SG ? ? BBB CYS 14 AAA CYS 45 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf2 disulf ? ? A CYS 45 SG ? ? ? 1_555 B CYS 14 SG ? ? BBB CYS 45 CCC CYS 14 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3 disulf ? ? D CYS 22 SG ? ? ? 1_555 D CYS 95 SG ? ? FFF CYS 22 FFF CYS 92 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf4 disulf ? ? E CYS 22 SG ? ? ? 1_555 E CYS 95 SG ? ? EEE CYS 22 EEE CYS 92 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf5 disulf ? ? F CYS 21 SG ? ? ? 1_555 F CYS 94 SG ? ? DDD CYS 22 DDD CYS 92 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
# 
_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 ASN 121 A . ? ASN 121 BBB PRO 122 A ? PRO 122 BBB 1 1.80 
2 ASN 121 B . ? ASN 121 CCC PRO 122 B ? PRO 122 CCC 1 1.51 
3 ASN 121 C . ? ASN 121 AAA PRO 122 C ? PRO 122 AAA 1 1.83 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 5 ? 
AA9 ? 5 ? 
AB1 ? 2 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 3 ? 
AB5 ? 8 ? 
AB6 ? 8 ? 
AB7 ? 8 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB5 6 7 ? anti-parallel 
AB5 7 8 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB6 6 7 ? anti-parallel 
AB6 7 8 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB7 5 6 ? anti-parallel 
AB7 6 7 ? anti-parallel 
AB7 7 8 ? 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 ILE A 2   ? GLN A 4   ? ILE BBB 2   GLN BBB 4   
AA1 2 MET A 10  ? HIS A 12  ? MET BBB 10  HIS BBB 12  
AA2 1 ILE B 2   ? VAL B 3   ? ILE CCC 2   VAL CCC 3   
AA2 2 VAL B 11  ? HIS B 12  ? VAL CCC 11  HIS CCC 12  
AA3 1 ILE C 2   ? GLN C 4   ? ILE AAA 2   GLN AAA 4   
AA3 2 MET C 10  ? HIS C 12  ? MET AAA 10  HIS AAA 12  
AA4 1 LEU D 4   ? SER D 7   ? LEU FFF 4   SER FFF 7   
AA4 2 LEU D 18  ? ALA D 24  ? LEU FFF 18  ALA FFF 24  
AA4 3 THR D 77  ? MET D 82  ? THR FFF 77  MET FFF 82  
AA4 4 PHE D 67  ? ASP D 72  ? PHE FFF 67  ASP FFF 72  
AA5 1 LEU D 11  ? GLN D 13  ? LEU FFF 11  GLN FFF 13  
AA5 2 THR D 110 ? SER D 115 ? THR FFF 107 SER FFF 112 
AA5 3 ALA D 91  ? ALA D 98  ? ALA FFF 88  ALA FFF 95  
AA5 4 ALA D 33  ? GLN D 39  ? ALA FFF 33  GLN FFF 39  
AA5 5 GLU D 46  ? VAL D 52  ? GLU FFF 46  VAL FFF 52  
AA5 6 VAL D 58  ? LEU D 59  ? VAL FFF 58  LEU FFF 59  
AA6 1 LEU D 11  ? GLN D 13  ? LEU FFF 11  GLN FFF 13  
AA6 2 THR D 110 ? SER D 115 ? THR FFF 107 SER FFF 112 
AA6 3 ALA D 91  ? ALA D 98  ? ALA FFF 88  ALA FFF 95  
AA6 4 TYR D 105 ? TRP D 106 ? TYR FFF 102 TRP FFF 103 
AA7 1 LEU E 4   ? SER E 7   ? LEU EEE 4   SER EEE 7   
AA7 2 SER E 17  ? ALA E 24  ? SER EEE 17  ALA EEE 24  
AA7 3 THR E 77  ? ASN E 83  A THR EEE 77  ASN EEE 82  
AA7 4 PHE E 67  ? ASP E 72  ? PHE EEE 67  ASP EEE 72  
AA8 1 VAL E 58  ? LEU E 59  ? VAL EEE 58  LEU EEE 59  
AA8 2 GLU E 46  ? VAL E 52  ? GLU EEE 46  VAL EEE 52  
AA8 3 ALA E 33  ? GLN E 39  ? ALA EEE 33  GLN EEE 39  
AA8 4 ALA E 91  ? ALA E 98  ? ALA EEE 88  ALA EEE 95  
AA8 5 ALA E 102 ? TRP E 104 ? ALA EEE 101 TRP EEE 103 
AA9 1 VAL E 58  ? LEU E 59  ? VAL EEE 58  LEU EEE 59  
AA9 2 GLU E 46  ? VAL E 52  ? GLU EEE 46  VAL EEE 52  
AA9 3 ALA E 33  ? GLN E 39  ? ALA EEE 33  GLN EEE 39  
AA9 4 ALA E 91  ? ALA E 98  ? ALA EEE 88  ALA EEE 95  
AA9 5 THR E 108 ? VAL E 110 ? THR EEE 107 VAL EEE 109 
AB1 1 LEU F 3   ? GLN F 4   ? LEU DDD 4   GLN DDD 5   
AB1 2 ALA F 22  ? ALA F 23  ? ALA DDD 23  ALA DDD 24  
AB2 1 LEU F 10  ? VAL F 11  ? LEU DDD 11  VAL DDD 12  
AB2 2 THR F 109 ? VAL F 113 ? THR DDD 107 VAL DDD 111 
AB2 3 ALA F 90  ? ALA F 97  ? ALA DDD 88  ALA DDD 95  
AB2 4 ALA F 32  ? GLN F 38  ? ALA DDD 33  GLN DDD 39  
AB2 5 GLU F 45  ? VAL F 51  ? GLU DDD 46  VAL DDD 52  
AB2 6 VAL F 57  ? LEU F 58  ? VAL DDD 58  LEU DDD 59  
AB3 1 LEU F 10  ? VAL F 11  ? LEU DDD 11  VAL DDD 12  
AB3 2 THR F 109 ? VAL F 113 ? THR DDD 107 VAL DDD 111 
AB3 3 ALA F 90  ? ALA F 97  ? ALA DDD 88  ALA DDD 95  
AB3 4 TYR F 104 ? TRP F 105 ? TYR DDD 102 TRP DDD 103 
AB4 1 LEU F 17  ? LEU F 19  ? LEU DDD 18  LEU DDD 20  
AB4 2 THR F 76  ? ARG F 81  ? THR DDD 77  ARG DDD 82  
AB4 3 THR F 67  ? ASP F 71  ? THR DDD 68  ASP DDD 72  
AB5 1 PHE G 53  ? ILE G 57  ? PHE GGG 53  ILE GGG 57  
AB5 2 MET G 61  ? GLY G 64  ? MET GGG 61  GLY GGG 64  
AB5 3 ASN G 108 ? CYS G 115 ? ASN GGG 108 CYS GGG 115 
AB5 4 ILE G 97  ? ASN G 102 ? ILE GGG 97  ASN GGG 102 
AB5 5 VAL G 128 ? VAL G 132 ? VAL GGG 128 VAL GGG 132 
AB5 6 GLU G 15  ? LEU G 24  ? GLU GGG 15  LEU GGG 24  
AB5 7 THR G 5   ? VAL G 12  ? THR GGG 5   VAL GGG 12  
AB5 8 ILE G 156 ? LEU G 164 ? ILE GGG 156 LEU GGG 164 
AB6 1 PHE H 53  ? ILE H 57  ? PHE HHH 53  ILE HHH 57  
AB6 2 MET H 61  ? GLY H 64  ? MET HHH 61  GLY HHH 64  
AB6 3 ASN H 108 ? CYS H 115 ? ASN HHH 108 CYS HHH 115 
AB6 4 ILE H 97  ? ASN H 102 ? ILE HHH 97  ASN HHH 102 
AB6 5 VAL H 128 ? GLU H 134 ? VAL HHH 128 GLU HHH 134 
AB6 6 GLU H 15  ? LEU H 24  ? GLU HHH 15  LEU HHH 24  
AB6 7 THR H 5   ? VAL H 12  ? THR HHH 5   VAL HHH 12  
AB6 8 ILE H 156 ? GLN H 163 ? ILE HHH 156 GLN HHH 163 
AB7 1 PHE I 53  ? ILE I 57  ? PHE III 53  ILE III 57  
AB7 2 MET I 61  ? GLY I 64  ? MET III 61  GLY III 64  
AB7 3 ASN I 108 ? CYS I 115 ? ASN III 108 CYS III 115 
AB7 4 ILE I 97  ? ASN I 102 ? ILE III 97  ASN III 102 
AB7 5 VAL I 128 ? GLU I 134 ? VAL III 128 GLU III 134 
AB7 6 GLU I 15  ? LEU I 24  ? GLU III 15  LEU III 24  
AB7 7 THR I 5   ? VAL I 12  ? THR III 5   VAL III 12  
AB7 8 ILE I 156 ? LEU I 164 ? ILE III 156 LEU III 164 
# 
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 VAL A 3   ? N VAL BBB 3   O VAL A 11  ? O VAL BBB 11  
AA2 1 2 N VAL B 3   ? N VAL CCC 3   O VAL B 11  ? O VAL CCC 11  
AA3 1 2 N VAL C 3   ? N VAL AAA 3   O VAL C 11  ? O VAL AAA 11  
AA4 1 2 N SER D 7   ? N SER FFF 7   O SER D 21  ? O SER FFF 21  
AA4 2 3 N LEU D 18  ? N LEU FFF 18  O MET D 82  ? O MET FFF 82  
AA4 3 4 O ALA D 79  ? O ALA FFF 79  N SER D 70  ? N SER FFF 70  
AA5 1 2 N VAL D 12  ? N VAL FFF 12  O THR D 113 ? O THR FFF 110 
AA5 2 3 O VAL D 112 ? O VAL FFF 109 N ALA D 91  ? N ALA FFF 88  
AA5 3 4 O TYR D 94  ? O TYR FFF 91  N TRP D 37  ? N TRP FFF 37  
AA5 4 5 N MET D 34  ? N MET FFF 34  O ILE D 51  ? O ILE FFF 51  
AA5 5 6 N ARG D 50  ? N ARG FFF 50  O VAL D 58  ? O VAL FFF 58  
AA6 1 2 N VAL D 12  ? N VAL FFF 12  O THR D 113 ? O THR FFF 110 
AA6 2 3 O VAL D 112 ? O VAL FFF 109 N ALA D 91  ? N ALA FFF 88  
AA6 3 4 N ALA D 97  ? N ALA FFF 94  O TYR D 105 ? O TYR FFF 102 
AA7 1 2 N GLN E 5   ? N GLN EEE 5   O ALA E 23  ? O ALA EEE 23  
AA7 2 3 N LEU E 18  ? N LEU EEE 18  O MET E 82  ? O MET EEE 82  
AA7 3 4 O GLN E 81  ? O GLN EEE 81  N THR E 68  ? N THR EEE 68  
AA8 1 2 O VAL E 58  ? O VAL EEE 58  N ARG E 50  ? N ARG EEE 50  
AA8 2 3 O GLU E 46  ? O GLU EEE 46  N ARG E 38  ? N ARG EEE 38  
AA8 3 4 N TRP E 37  ? N TRP EEE 37  O TYR E 94  ? O TYR EEE 91  
AA8 4 5 N ALA E 97  ? N ALA EEE 94  O TYR E 103 ? O TYR EEE 102 
AA9 1 2 O VAL E 58  ? O VAL EEE 58  N ARG E 50  ? N ARG EEE 50  
AA9 2 3 O GLU E 46  ? O GLU EEE 46  N ARG E 38  ? N ARG EEE 38  
AA9 3 4 N TRP E 37  ? N TRP EEE 37  O TYR E 94  ? O TYR EEE 91  
AA9 4 5 N TYR E 93  ? N TYR EEE 90  O THR E 108 ? O THR EEE 107 
AB1 1 2 N GLN F 4   ? N GLN DDD 5   O ALA F 22  ? O ALA DDD 23  
AB2 1 2 N VAL F 11  ? N VAL DDD 12  O THR F 112 ? O THR DDD 110 
AB2 2 3 O VAL F 111 ? O VAL DDD 109 N ALA F 90  ? N ALA DDD 88  
AB2 3 4 O ALA F 97  ? O ALA DDD 95  N ALA F 32  ? N ALA DDD 33  
AB2 4 5 N TRP F 35  ? N TRP DDD 36  O VAL F 47  ? O VAL DDD 48  
AB2 5 6 N ARG F 49  ? N ARG DDD 50  O VAL F 57  ? O VAL DDD 58  
AB3 1 2 N VAL F 11  ? N VAL DDD 12  O THR F 112 ? O THR DDD 110 
AB3 2 3 O VAL F 111 ? O VAL DDD 109 N ALA F 90  ? N ALA DDD 88  
AB3 3 4 N ALA F 96  ? N ALA DDD 94  O TYR F 104 ? O TYR DDD 102 
AB4 1 2 N LEU F 17  ? N LEU DDD 18  O ARG F 81  ? O ARG DDD 82  
AB4 2 3 O GLN F 80  ? O GLN DDD 81  N THR F 67  ? N THR DDD 68  
AB5 1 2 N ARG G 55  ? N ARG GGG 55  O GLN G 63  ? O GLN GGG 63  
AB5 2 3 N CYS G 62  ? N CYS GGG 62  O ILE G 114 ? O ILE GGG 114 
AB5 3 4 O PHE G 113 ? O PHE GGG 113 N SER G 99  ? N SER GGG 99  
AB5 4 5 N LEU G 98  ? N LEU GGG 98  O GLY G 130 ? O GLY GGG 130 
AB5 5 6 O LYS G 131 ? O LYS GGG 131 N GLU G 23  ? N GLU GGG 23  
AB5 6 7 O PHE G 22  ? O PHE GGG 22  N VAL G 6   ? N VAL GGG 6   
AB5 7 8 N ASP G 9   ? N ASP GGG 9   O ASP G 160 ? O ASP GGG 160 
AB6 1 2 N ARG H 55  ? N ARG HHH 55  O GLN H 63  ? O GLN HHH 63  
AB6 2 3 N CYS H 62  ? N CYS HHH 62  O ILE H 114 ? O ILE HHH 114 
AB6 3 4 O GLN H 111 ? O GLN HHH 111 N ALA H 101 ? N ALA HHH 101 
AB6 4 5 N LEU H 98  ? N LEU HHH 98  O GLY H 130 ? O GLY HHH 130 
AB6 5 6 O LYS H 133 ? O LYS HHH 133 N SER H 21  ? N SER HHH 21  
AB6 6 7 O PHE H 22  ? O PHE HHH 22  N VAL H 6   ? N VAL HHH 6   
AB6 7 8 N ALA H 11  ? N ALA HHH 11  O THR H 157 ? O THR HHH 157 
AB7 1 2 N ARG I 55  ? N ARG III 55  O GLN I 63  ? O GLN III 63  
AB7 2 3 N CYS I 62  ? N CYS III 62  O ILE I 114 ? O ILE III 114 
AB7 3 4 O GLN I 111 ? O GLN III 111 N ALA I 101 ? N ALA III 101 
AB7 4 5 N LEU I 98  ? N LEU III 98  O GLY I 130 ? O GLY III 130 
AB7 5 6 O LYS I 131 ? O LYS III 131 N GLU I 23  ? N GLU III 23  
AB7 6 7 O VAL I 20  ? O VAL III 20  N PHE I 8   ? N PHE III 8   
AB7 7 8 N ALA I 11  ? N ALA III 11  O THR I 157 ? O THR III 157 
# 
_atom_sites.entry_id                    7N9X 
_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]   0.007816 
_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]   0.007254 
_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]   0.003186 
_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 
C 2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 
N 12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  
O 3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 
S 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 
# 
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_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM 1     N N   . PRO A 1 1   ? 50.291  60.616  37.119 1.000 95.857  0 1   PRO BBB N   1 ? 3  
ATOM 2     C CA  . PRO A 1 1   ? 49.371  61.547  36.456 1.000 94.787  0 1   PRO BBB CA  1 ? 3  
ATOM 3     C C   . PRO A 1 1   ? 49.643  61.669  34.960 1.000 97.961  0 1   PRO BBB C   1 ? 3  
ATOM 4     O O   . PRO A 1 1   ? 50.614  61.086  34.482 1.000 107.374 0 1   PRO BBB O   1 ? 3  
ATOM 5     C CB  A PRO A 1 1   ? 49.650  62.881  37.161 1.000 99.972  0 1   PRO BBB CB  1 ? 3  
ATOM 6     C CG  A PRO A 1 1   ? 50.933  62.672  37.943 1.000 99.431  0 1   PRO BBB CG  1 ? 3  
ATOM 7     C CD  A PRO A 1 1   ? 50.953  61.225  38.282 1.000 100.371 0 1   PRO BBB CD  1 ? 3  
ATOM 8     N N   . ILE A 1 2   ? 48.829  62.435  34.236 1.000 90.892  0 2   ILE BBB N   1 ? 3  
ATOM 9     C CA  . ILE A 1 2   ? 49.052  62.685  32.814 1.000 90.175  0 2   ILE BBB CA  1 ? 3  
ATOM 10    C C   . ILE A 1 2   ? 49.480  64.135  32.608 1.000 98.025  0 2   ILE BBB C   1 ? 3  
ATOM 11    O O   . ILE A 1 2   ? 48.780  65.065  33.029 1.000 102.592 0 2   ILE BBB O   1 ? 3  
ATOM 12    C CB  . ILE A 1 2   ? 47.795  62.371  31.986 1.000 84.303  0 2   ILE BBB CB  1 ? 3  
ATOM 13    C CG1 . ILE A 1 2   ? 47.303  60.948  32.252 1.000 83.727  0 2   ILE BBB CG1 1 ? 3  
ATOM 14    C CG2 . ILE A 1 2   ? 48.080  62.528  30.514 1.000 97.272  0 2   ILE BBB CG2 1 ? 3  
ATOM 15    C CD1 . ILE A 1 2   ? 48.289  59.879  31.859 0.500 88.253  0 2   ILE BBB CD1 1 ? 3  
ATOM 16    N N   . VAL A 1 3   ? 50.639  64.327  31.974 1.000 97.931  0 3   VAL BBB N   1 ? 3  
ATOM 17    C CA  . VAL A 1 3   ? 51.213  65.641  31.712 1.000 102.567 0 3   VAL BBB CA  1 ? 3  
ATOM 18    C C   . VAL A 1 3   ? 51.578  65.679  30.232 1.000 107.418 0 3   VAL BBB C   1 ? 3  
ATOM 19    O O   . VAL A 1 3   ? 51.624  64.644  29.568 1.000 110.862 0 3   VAL BBB O   1 ? 3  
ATOM 20    C CB  . VAL A 1 3   ? 52.439  65.946  32.591 1.000 112.871 0 3   VAL BBB CB  1 ? 3  
ATOM 21    C CG1 . VAL A 1 3   ? 53.683  65.283  32.015 1.000 125.886 0 3   VAL BBB CG1 1 ? 3  
ATOM 22    C CG2 . VAL A 1 3   ? 52.626  67.452  32.727 1.000 119.226 0 3   VAL BBB CG2 1 ? 3  
ATOM 23    N N   . GLN A 1 4   ? 51.870  66.868  29.704 1.000 110.150 0 4   GLN BBB N   1 ? 3  
ATOM 24    C CA  A GLN A 1 4   ? 52.450  66.870  28.367 1.000 124.424 0 4   GLN BBB CA  1 ? 3  
ATOM 25    C C   . GLN A 1 4   ? 53.961  67.070  28.412 1.000 124.618 0 4   GLN BBB C   1 ? 3  
ATOM 26    O O   . GLN A 1 4   ? 54.507  67.750  29.286 1.000 118.216 0 4   GLN BBB O   1 ? 3  
ATOM 27    C CB  . GLN A 1 4   ? 51.857  67.914  27.403 1.000 135.451 0 4   GLN BBB CB  1 ? 3  
ATOM 28    C CG  . GLN A 1 4   ? 51.655  69.351  27.878 1.000 138.405 0 4   GLN BBB CG  1 ? 3  
ATOM 29    C CD  . GLN A 1 4   ? 50.279  69.614  28.460 1.000 150.544 0 4   GLN BBB CD  1 ? 3  
ATOM 30    O OE1 . GLN A 1 4   ? 49.263  69.294  27.841 1.000 156.817 0 4   GLN BBB OE1 1 ? 3  
ATOM 31    N NE2 . GLN A 1 4   ? 50.237  70.202  29.652 1.000 155.784 0 4   GLN BBB NE2 1 ? 3  
ATOM 32    N N   . ASN A 1 5   ? 54.618  66.461  27.430 1.000 133.635 0 5   ASN BBB N   1 ? 3  
ATOM 33    C CA  . ASN A 1 5   ? 56.047  66.538  27.177 1.000 140.640 0 5   ASN BBB CA  1 ? 3  
ATOM 34    C C   . ASN A 1 5   ? 56.358  67.745  26.283 1.000 156.685 0 5   ASN BBB C   1 ? 3  
ATOM 35    O O   . ASN A 1 5   ? 55.519  68.627  26.084 1.000 163.593 0 5   ASN BBB O   1 ? 3  
ATOM 36    C CB  . ASN A 1 5   ? 56.516  65.188  26.625 1.000 142.120 0 5   ASN BBB CB  1 ? 3  
ATOM 37    C CG  . ASN A 1 5   ? 56.079  64.943  25.185 1.000 149.030 0 5   ASN BBB CG  1 ? 3  
ATOM 38    O OD1 . ASN A 1 5   ? 55.271  65.684  24.624 1.000 159.084 0 5   ASN BBB OD1 1 ? 3  
ATOM 39    N ND2 . ASN A 1 5   ? 56.593  63.871  24.592 1.000 152.355 0 5   ASN BBB ND2 1 ? 3  
ATOM 40    N N   . LEU A 1 6   ? 57.586  67.815  25.755 1.000 159.081 0 6   LEU BBB N   1 ? 3  
ATOM 41    C CA  . LEU A 1 6   ? 57.974  68.968  24.943 1.000 155.030 0 6   LEU BBB CA  1 ? 3  
ATOM 42    C C   . LEU A 1 6   ? 57.286  68.963  23.585 1.000 161.346 0 6   LEU BBB C   1 ? 3  
ATOM 43    O O   . LEU A 1 6   ? 57.091  70.027  22.988 1.000 170.580 0 6   LEU BBB O   1 ? 3  
ATOM 44    C CB  . LEU A 1 6   ? 59.493  69.019  24.747 1.000 167.870 0 6   LEU BBB CB  1 ? 3  
ATOM 45    C CG  . LEU A 1 6   ? 60.218  68.020  23.834 1.000 185.956 0 6   LEU BBB CG  1 ? 3  
ATOM 46    C CD1 . LEU A 1 6   ? 60.178  68.422  22.362 1.000 197.389 0 6   LEU BBB CD1 1 ? 3  
ATOM 47    C CD2 . LEU A 1 6   ? 61.665  67.917  24.267 1.000 200.811 0 6   LEU BBB CD2 1 ? 3  
ATOM 48    N N   . GLN A 1 7   ? 56.906  67.784  23.089 1.000 177.658 0 7   GLN BBB N   1 ? 3  
ATOM 49    C CA  . GLN A 1 7   ? 56.133  67.666  21.859 1.000 183.943 0 7   GLN BBB CA  1 ? 3  
ATOM 50    C C   . GLN A 1 7   ? 54.674  68.065  22.038 1.000 182.600 0 7   GLN BBB C   1 ? 3  
ATOM 51    O O   . GLN A 1 7   ? 53.954  68.194  21.042 1.000 190.378 0 7   GLN BBB O   1 ? 3  
ATOM 52    C CB  . GLN A 1 7   ? 56.231  66.215  21.356 1.000 183.615 0 7   GLN BBB CB  1 ? 3  
ATOM 53    C CG  . GLN A 1 7   ? 55.472  65.875  20.074 1.000 188.659 0 7   GLN BBB CG  1 ? 3  
ATOM 54    C CD  . GLN A 1 7   ? 56.158  66.401  18.836 1.000 195.905 0 7   GLN BBB CD  1 ? 3  
ATOM 55    O OE1 . GLN A 1 7   ? 57.365  66.632  18.836 1.000 205.624 0 7   GLN BBB OE1 1 ? 3  
ATOM 56    N NE2 . GLN A 1 7   ? 55.392  66.587  17.766 1.000 191.924 0 7   GLN BBB NE2 1 ? 3  
ATOM 57    N N   . GLY A 1 8   ? 54.230  68.317  23.267 1.000 166.344 0 8   GLY BBB N   1 ? 3  
ATOM 58    C CA  . GLY A 1 8   ? 52.832  68.558  23.514 1.000 159.002 0 8   GLY BBB CA  1 ? 3  
ATOM 59    C C   . GLY A 1 8   ? 52.035  67.302  23.756 1.000 159.935 0 8   GLY BBB C   1 ? 3  
ATOM 60    O O   . GLY A 1 8   ? 50.880  67.391  24.192 1.000 170.534 0 8   GLY BBB O   1 ? 3  
ATOM 61    N N   . GLN A 1 9   ? 52.614  66.137  23.479 1.000 156.077 0 9   GLN BBB N   1 ? 3  
ATOM 62    C CA  . GLN A 1 9   ? 51.867  64.895  23.561 1.000 154.497 0 9   GLN BBB CA  1 ? 3  
ATOM 63    C C   . GLN A 1 9   ? 51.584  64.570  25.020 1.000 146.538 0 9   GLN BBB C   1 ? 3  
ATOM 64    O O   . GLN A 1 9   ? 52.412  64.817  25.902 1.000 148.031 0 9   GLN BBB O   1 ? 3  
ATOM 65    C CB  . GLN A 1 9   ? 52.686  63.774  22.921 1.000 157.542 0 9   GLN BBB CB  1 ? 3  
ATOM 66    C CG  . GLN A 1 9   ? 52.065  62.389  22.944 1.000 170.402 0 9   GLN BBB CG  1 ? 3  
ATOM 67    C CD  . GLN A 1 9   ? 53.042  61.325  22.470 1.000 179.288 0 9   GLN BBB CD  1 ? 3  
ATOM 68    O OE1 . GLN A 1 9   ? 54.185  61.631  22.123 1.000 175.408 0 9   GLN BBB OE1 1 ? 3  
ATOM 69    N NE2 . GLN A 1 9   ? 52.607  60.070  22.470 1.000 183.587 0 9   GLN BBB NE2 1 ? 3  
ATOM 70    N N   . MET A 1 10  ? 50.412  64.001  25.271 1.000 126.529 0 10  MET BBB N   1 ? 3  
ATOM 71    C CA  . MET A 1 10  ? 50.007  63.647  26.622 1.000 107.557 0 10  MET BBB CA  1 ? 3  
ATOM 72    C C   . MET A 1 10  ? 50.559  62.275  26.979 1.000 109.866 0 10  MET BBB C   1 ? 3  
ATOM 73    O O   . MET A 1 10  ? 50.224  61.278  26.330 1.000 114.110 0 10  MET BBB O   1 ? 3  
ATOM 74    C CB  . MET A 1 10  ? 48.487  63.690  26.757 1.000 108.849 0 10  MET BBB CB  1 ? 3  
ATOM 75    C CG  . MET A 1 10  ? 47.917  65.063  26.457 1.000 122.662 0 10  MET BBB CG  1 ? 3  
ATOM 76    S SD  . MET A 1 10  ? 48.457  66.291  27.667 1.000 127.271 0 10  MET BBB SD  1 ? 3  
ATOM 77    C CE  . MET A 1 10  ? 47.515  65.835  29.128 1.000 122.514 0 10  MET BBB CE  1 ? 3  
ATOM 78    N N   . VAL A 1 11  ? 51.410  62.222  28.001 1.000 111.320 0 11  VAL BBB N   1 ? 3  
ATOM 79    C CA  . VAL A 1 11  ? 52.053  60.978  28.392 1.000 109.003 0 11  VAL BBB CA  1 ? 3  
ATOM 80    C C   . VAL A 1 11  ? 51.838  60.777  29.883 1.000 101.074 0 11  VAL BBB C   1 ? 3  
ATOM 81    O O   . VAL A 1 11  ? 51.642  61.725  30.647 1.000 96.175  0 11  VAL BBB O   1 ? 3  
ATOM 82    C CB  . VAL A 1 11  ? 53.562  60.941  28.051 1.000 114.028 0 11  VAL BBB CB  1 ? 3  
ATOM 83    C CG1 . VAL A 1 11  ? 53.787  61.223  26.576 1.000 127.531 0 11  VAL BBB CG1 1 ? 3  
ATOM 84    C CG2 . VAL A 1 11  ? 54.343  61.932  28.913 1.000 114.043 0 11  VAL BBB CG2 1 ? 3  
ATOM 85    N N   . HIS A 1 12  ? 51.888  59.514  30.289 1.000 98.320  0 12  HIS BBB N   1 ? 3  
ATOM 86    C CA  . HIS A 1 12  ? 51.797  59.169  31.697 1.000 91.870  0 12  HIS BBB CA  1 ? 3  
ATOM 87    C C   . HIS A 1 12  ? 53.130  59.440  32.379 1.000 93.515  0 12  HIS BBB C   1 ? 3  
ATOM 88    O O   . HIS A 1 12  ? 54.198  59.235  31.795 1.000 103.181 0 12  HIS BBB O   1 ? 3  
ATOM 89    C CB  . HIS A 1 12  ? 51.393  57.706  31.871 1.000 89.619  0 12  HIS BBB CB  1 ? 3  
ATOM 90    C CG  . HIS A 1 12  ? 51.288  57.279  33.300 1.000 89.305  0 12  HIS BBB CG  1 ? 3  
ATOM 91    N ND1 . HIS A 1 12  ? 52.318  56.660  33.975 1.000 93.115  0 12  HIS BBB ND1 1 ? 3  
ATOM 92    C CD2 . HIS A 1 12  ? 50.270  57.390  34.185 1.000 95.922  0 12  HIS BBB CD2 1 ? 3  
ATOM 93    C CE1 . HIS A 1 12  ? 51.937  56.407  35.215 1.000 104.498 0 12  HIS BBB CE1 1 ? 3  
ATOM 94    N NE2 . HIS A 1 12  ? 50.698  56.840  35.368 1.000 104.408 0 12  HIS BBB NE2 1 ? 3  
ATOM 95    N N   . GLN A 1 13  ? 53.060  59.898  33.623 1.000 89.324  0 13  GLN BBB N   1 ? 3  
ATOM 96    C CA  . GLN A 1 13  ? 54.242  60.099  34.441 1.000 95.717  0 13  GLN BBB CA  1 ? 3  
ATOM 97    C C   . GLN A 1 13  ? 53.930  59.547  35.822 1.000 95.631  0 13  GLN BBB C   1 ? 3  
ATOM 98    O O   . GLN A 1 13  ? 52.811  59.697  36.314 1.000 93.557  0 13  GLN BBB O   1 ? 3  
ATOM 99    C CB  . GLN A 1 13  ? 54.606  61.589  34.504 1.000 99.235  0 13  GLN BBB CB  1 ? 3  
ATOM 100   C CG  . GLN A 1 13  ? 55.840  61.919  35.306 1.000 116.730 0 13  GLN BBB CG  1 ? 3  
ATOM 101   C CD  . GLN A 1 13  ? 56.319  63.334  35.052 1.000 127.960 0 13  GLN BBB CD  1 ? 3  
ATOM 102   O OE1 . GLN A 1 13  ? 55.563  64.175  34.563 1.000 122.727 0 13  GLN BBB OE1 1 ? 3  
ATOM 103   N NE2 . GLN A 1 13  ? 57.577  63.606  35.383 1.000 150.275 0 13  GLN BBB NE2 1 ? 3  
ATOM 104   N N   . CYS A 1 14  ? 54.914  58.894  36.436 1.000 97.952  0 14  CYS BBB N   1 ? 3  
ATOM 105   C CA  . CYS A 1 14  ? 54.696  58.323  37.757 1.000 94.717  0 14  CYS BBB CA  1 ? 3  
ATOM 106   C C   . CYS A 1 14  ? 54.379  59.409  38.774 1.000 97.631  0 14  CYS BBB C   1 ? 3  
ATOM 107   O O   . CYS A 1 14  ? 54.913  60.521  38.722 1.000 101.887 0 14  CYS BBB O   1 ? 3  
ATOM 108   C CB  . CYS A 1 14  ? 55.892  57.474  38.197 1.000 102.466 0 14  CYS BBB CB  1 ? 3  
ATOM 109   S SG  . CYS A 1 14  ? 56.201  56.011  37.132 1.000 134.228 0 14  CYS BBB SG  1 ? 3  
ATOM 110   N N   . ILE A 1 15  ? 53.483  59.066  39.700 1.000 98.312  0 15  ILE BBB N   1 ? 3  
ATOM 111   C CA  . ILE A 1 15  ? 53.213  59.917  40.849 1.000 92.817  0 15  ILE BBB CA  1 ? 3  
ATOM 112   C C   . ILE A 1 15  ? 54.497  60.126  41.639 1.000 94.678  0 15  ILE BBB C   1 ? 3  
ATOM 113   O O   . ILE A 1 15  ? 55.284  59.193  41.855 1.000 94.784  0 15  ILE BBB O   1 ? 3  
ATOM 114   C CB  . ILE A 1 15  ? 52.095  59.296  41.701 1.000 85.706  0 15  ILE BBB CB  1 ? 3  
ATOM 115   C CG1 . ILE A 1 15  ? 51.667  60.269  42.792 1.000 84.882  0 15  ILE BBB CG1 1 ? 3  
ATOM 116   C CG2 . ILE A 1 15  ? 52.529  57.952  42.278 1.000 86.375  0 15  ILE BBB CG2 1 ? 3  
ATOM 117   C CD1 . ILE A 1 15  ? 50.332  59.934  43.409 1.000 92.998  0 15  ILE BBB CD1 1 ? 3  
ATOM 118   N N   . SER A 1 16  ? 54.726  61.384  42.068 1.000 92.536  0 16  SER BBB N   1 ? 3  
ATOM 119   C CA  . SER A 1 16  ? 56.013  61.706  42.659 1.000 95.976  0 16  SER BBB CA  1 ? 3  
ATOM 120   C C   . SER A 1 16  ? 56.053  61.363  44.144 1.000 93.204  0 16  SER BBB C   1 ? 3  
ATOM 121   O O   . SER A 1 16  ? 55.028  61.361  44.825 1.000 91.868  0 16  SER BBB O   1 ? 3  
ATOM 122   C CB  . SER A 1 16  ? 56.309  63.197  42.485 1.000 97.686  0 16  SER BBB CB  1 ? 3  
ATOM 123   O OG  . SER A 1 16  ? 57.530  63.570  43.105 1.000 112.561 0 16  SER BBB OG  1 ? 3  
ATOM 124   N N   . PRO A 1 17  ? 57.234  61.029  44.659 1.000 95.671  0 17  PRO BBB N   1 ? 3  
ATOM 125   C CA  . PRO A 1 17  ? 57.354  60.828  46.108 1.000 95.611  0 17  PRO BBB CA  1 ? 3  
ATOM 126   C C   . PRO A 1 17  ? 56.958  62.038  46.935 1.000 102.873 0 17  PRO BBB C   1 ? 3  
ATOM 127   O O   . PRO A 1 17  ? 56.382  61.884  48.019 1.000 111.618 0 17  PRO BBB O   1 ? 3  
ATOM 128   C CB  . PRO A 1 17  ? 58.841  60.485  46.280 1.000 97.278  0 17  PRO BBB CB  1 ? 3  
ATOM 129   C CG  . PRO A 1 17  ? 59.245  59.892  44.967 1.000 97.683  0 17  PRO BBB CG  1 ? 3  
ATOM 130   C CD  . PRO A 1 17  ? 58.455  60.637  43.934 1.000 102.767 0 17  PRO BBB CD  1 ? 3  
ATOM 131   N N   . ARG A 1 18  ? 57.246  63.246  46.445 1.000 102.486 0 18  ARG BBB N   1 ? 3  
ATOM 132   C CA  . ARG A 1 18  ? 56.839  64.460  47.147 1.000 99.146  0 18  ARG BBB CA  1 ? 3  
ATOM 133   C C   . ARG A 1 18  ? 55.326  64.593  47.310 1.000 97.921  0 18  ARG BBB C   1 ? 3  
ATOM 134   O O   . ARG A 1 18  ? 54.840  64.864  48.413 1.000 107.858 0 18  ARG BBB O   1 ? 3  
ATOM 135   C CB  . ARG A 1 18  ? 57.410  65.673  46.416 1.000 103.794 0 18  ARG BBB CB  1 ? 3  
ATOM 136   C CG  . ARG A 1 18  ? 57.725  66.844  47.320 1.000 115.053 0 18  ARG BBB CG  1 ? 3  
ATOM 137   C CD  . ARG A 1 18  ? 58.543  67.873  46.570 1.000 130.850 0 18  ARG BBB CD  1 ? 3  
ATOM 138   N NE  . ARG A 1 18  ? 59.648  67.253  45.843 1.000 146.026 0 18  ARG BBB NE  1 ? 3  
ATOM 139   C CZ  . ARG A 1 18  ? 60.344  67.850  44.884 1.000 151.598 0 18  ARG BBB CZ  1 ? 3  
ATOM 140   N NH1 . ARG A 1 18  ? 60.088  69.090  44.483 1.000 150.808 0 18  ARG BBB NH1 1 ? 3  
ATOM 141   N NH2 . ARG A 1 18  ? 61.324  67.182  44.280 1.000 150.587 0 18  ARG BBB NH2 1 ? 3  
ATOM 142   N N   . THR A 1 19  ? 54.557  64.375  46.242 1.000 99.581  0 19  THR BBB N   1 ? 3  
ATOM 143   C CA  . THR A 1 19  ? 53.103  64.465  46.372 1.000 98.661  0 19  THR BBB CA  1 ? 3  
ATOM 144   C C   . THR A 1 19  ? 52.543  63.418  47.342 1.000 98.047  0 19  THR BBB C   1 ? 3  
ATOM 145   O O   . THR A 1 19  ? 51.766  63.758  48.243 1.000 105.388 0 19  THR BBB O   1 ? 3  
ATOM 146   C CB  . THR A 1 19  ? 52.439  64.421  44.989 1.000 98.985  0 19  THR BBB CB  1 ? 3  
ATOM 147   O OG1 . THR A 1 19  ? 51.018  64.286  45.120 1.000 102.456 0 19  THR BBB OG1 1 ? 3  
ATOM 148   C CG2 . THR A 1 19  ? 52.981  63.308  44.149 1.000 107.496 0 19  THR BBB CG2 1 ? 3  
ATOM 149   N N   . LEU A 1 20  ? 52.951  62.148  47.203 1.000 91.332  0 20  LEU BBB N   1 ? 3  
ATOM 150   C CA  . LEU A 1 20  ? 52.428  61.101  48.086 1.000 91.108  0 20  LEU BBB CA  1 ? 3  
ATOM 151   C C   . LEU A 1 20  ? 52.684  61.432  49.546 1.000 96.524  0 20  LEU BBB C   1 ? 3  
ATOM 152   O O   . LEU A 1 20  ? 51.776  61.357  50.382 1.000 94.446  0 20  LEU BBB O   1 ? 3  
ATOM 153   C CB  . LEU A 1 20  ? 53.024  59.733  47.755 1.000 89.833  0 20  LEU BBB CB  1 ? 3  
ATOM 154   C CG  . LEU A 1 20  ? 52.621  59.083  46.441 1.000 96.332  0 20  LEU BBB CG  1 ? 3  
ATOM 155   C CD1 . LEU A 1 20  ? 53.626  58.017  46.044 1.000 96.856  0 20  LEU BBB CD1 1 ? 3  
ATOM 156   C CD2 . LEU A 1 20  ? 51.225  58.488  46.598 1.000 95.891  0 20  LEU BBB CD2 1 ? 3  
ATOM 157   N N   . ASN A 1 21  ? 53.918  61.801  49.870 1.000 101.321 0 21  ASN BBB N   1 ? 3  
ATOM 158   C CA  . ASN A 1 21  ? 54.241  62.125  51.250 1.000 102.602 0 21  ASN BBB CA  1 ? 3  
ATOM 159   C C   . ASN A 1 21  ? 53.442  63.336  51.710 1.000 100.843 0 21  ASN BBB C   1 ? 3  
ATOM 160   O O   . ASN A 1 21  ? 52.949  63.368  52.844 1.000 107.443 0 21  ASN BBB O   1 ? 3  
ATOM 161   C CB  . ASN A 1 21  ? 55.741  62.368  51.378 1.000 106.459 0 21  ASN BBB CB  1 ? 3  
ATOM 162   C CG  . ASN A 1 21  ? 56.171  62.574  52.799 1.000 117.300 0 21  ASN BBB CG  1 ? 3  
ATOM 163   O OD1 . ASN A 1 21  ? 55.583  62.016  53.725 1.000 132.983 0 21  ASN BBB OD1 1 ? 3  
ATOM 164   N ND2 . ASN A 1 21  ? 57.201  63.385  52.990 1.000 128.887 0 21  ASN BBB ND2 1 ? 3  
ATOM 165   N N   . ALA A 1 22  ? 53.304  64.342  50.843 1.000 95.460  0 22  ALA BBB N   1 ? 3  
ATOM 166   C CA  . ALA A 1 22  ? 52.534  65.533  51.190 1.000 92.536  0 22  ALA BBB CA  1 ? 3  
ATOM 167   C C   . ALA A 1 22  ? 51.099  65.182  51.563 1.000 92.269  0 22  ALA BBB C   1 ? 3  
ATOM 168   O O   . ALA A 1 22  ? 50.565  65.697  52.553 1.000 96.752  0 22  ALA BBB O   1 ? 3  
ATOM 169   C CB  . ALA A 1 22  ? 52.547  66.527  50.031 1.000 90.342  0 22  ALA BBB CB  1 ? 3  
ATOM 170   N N   . TRP A 1 23  ? 50.456  64.308  50.783 1.000 89.237  0 23  TRP BBB N   1 ? 3  
ATOM 171   C CA  . TRP A 1 23  ? 49.073  63.933  51.072 1.000 90.151  0 23  TRP BBB CA  1 ? 3  
ATOM 172   C C   . TRP A 1 23  ? 48.972  63.162  52.385 1.000 92.556  0 23  TRP BBB C   1 ? 3  
ATOM 173   O O   . TRP A 1 23  ? 48.120  63.464  53.227 1.000 94.831  0 23  TRP BBB O   1 ? 3  
ATOM 174   C CB  . TRP A 1 23  ? 48.504  63.108  49.916 1.000 85.281  0 23  TRP BBB CB  1 ? 3  
ATOM 175   C CG  . TRP A 1 23  ? 47.145  62.535  50.180 1.000 84.252  0 23  TRP BBB CG  1 ? 3  
ATOM 176   C CD1 . TRP A 1 23  ? 46.799  61.215  50.185 1.000 84.860  0 23  TRP BBB CD1 1 ? 3  
ATOM 177   C CD2 . TRP A 1 23  ? 45.940  63.265  50.440 1.000 83.641  0 23  TRP BBB CD2 1 ? 3  
ATOM 178   N NE1 . TRP A 1 23  ? 45.460  61.077  50.452 1.000 84.953  0 23  TRP BBB NE1 1 ? 3  
ATOM 179   C CE2 . TRP A 1 23  ? 44.909  62.320  50.612 1.000 84.068  0 23  TRP BBB CE2 1 ? 3  
ATOM 180   C CE3 . TRP A 1 23  ? 45.634  64.624  50.552 1.000 83.262  0 23  TRP BBB CE3 1 ? 3  
ATOM 181   C CZ2 . TRP A 1 23  ? 43.598  62.691  50.891 1.000 84.123  0 23  TRP BBB CZ2 1 ? 3  
ATOM 182   C CZ3 . TRP A 1 23  ? 44.331  64.988  50.832 1.000 83.386  0 23  TRP BBB CZ3 1 ? 3  
ATOM 183   C CH2 . TRP A 1 23  ? 43.329  64.026  50.996 1.000 83.842  0 23  TRP BBB CH2 1 ? 3  
ATOM 184   N N   . VAL A 1 24  ? 49.820  62.147  52.569 1.000 94.603  0 24  VAL BBB N   1 ? 3  
ATOM 185   C CA  . VAL A 1 24  ? 49.823  61.401  53.824 1.000 92.439  0 24  VAL BBB CA  1 ? 3  
ATOM 186   C C   . VAL A 1 24  ? 50.033  62.350  54.996 1.000 98.472  0 24  VAL BBB C   1 ? 3  
ATOM 187   O O   . VAL A 1 24  ? 49.378  62.234  56.039 1.000 106.833 0 24  VAL BBB O   1 ? 3  
ATOM 188   C CB  . VAL A 1 24  ? 50.892  60.292  53.789 1.000 92.818  0 24  VAL BBB CB  1 ? 3  
ATOM 189   C CG1 . VAL A 1 24  ? 51.192  59.786  55.191 1.000 102.469 0 24  VAL BBB CG1 1 ? 3  
ATOM 190   C CG2 . VAL A 1 24  ? 50.431  59.149  52.911 1.000 92.546  0 24  VAL BBB CG2 1 ? 3  
ATOM 191   N N   . LYS A 1 25  ? 50.937  63.318  54.829 1.000 99.266  0 25  LYS BBB N   1 ? 3  
ATOM 192   C CA  . LYS A 1 25  ? 51.276  64.230  55.915 1.000 108.634 0 25  LYS BBB CA  1 ? 3  
ATOM 193   C C   . LYS A 1 25  ? 50.134  65.195  56.222 1.000 109.982 0 25  LYS BBB C   1 ? 3  
ATOM 194   O O   . LYS A 1 25  ? 49.828  65.445  57.394 1.000 122.368 0 25  LYS BBB O   1 ? 3  
ATOM 195   C CB  . LYS A 1 25  ? 52.551  64.992  55.560 1.000 108.764 0 25  LYS BBB CB  1 ? 3  
ATOM 196   C CG  . LYS A 1 25  ? 53.747  64.650  56.434 1.000 111.596 0 25  LYS BBB CG  1 ? 3  
ATOM 197   C CD  . LYS A 1 25  ? 53.534  65.124  57.863 1.000 128.118 0 25  LYS BBB CD  1 ? 3  
ATOM 198   C CE  . LYS A 1 25  ? 54.785  64.962  58.719 1.000 134.647 0 25  LYS BBB CE  1 ? 3  
ATOM 199   N NZ  . LYS A 1 25  ? 54.608  65.575  60.069 1.000 136.145 0 25  LYS BBB NZ  1 ? 3  
ATOM 200   N N   . VAL A 1 26  ? 49.502  65.758  55.188 1.000 97.680  0 26  VAL BBB N   1 ? 3  
ATOM 201   C CA  . VAL A 1 26  ? 48.413  66.709  55.413 1.000 99.190  0 26  VAL BBB CA  1 ? 3  
ATOM 202   C C   . VAL A 1 26  ? 47.249  66.032  56.132 1.000 103.894 0 26  VAL BBB C   1 ? 3  
ATOM 203   O O   . VAL A 1 26  ? 46.592  66.636  56.988 1.000 110.652 0 26  VAL BBB O   1 ? 3  
ATOM 204   C CB  . VAL A 1 26  ? 47.978  67.375  54.092 1.000 91.322  0 26  VAL BBB CB  1 ? 3  
ATOM 205   C CG1 . VAL A 1 26  ? 47.277  66.399  53.179 1.000 92.333  0 26  VAL BBB CG1 1 ? 3  
ATOM 206   C CG2 . VAL A 1 26  ? 47.088  68.574  54.371 1.000 91.932  0 26  VAL BBB CG2 1 ? 3  
ATOM 207   N N   . VAL A 1 27  ? 46.974  64.772  55.795 1.000 99.060  0 27  VAL BBB N   1 ? 3  
ATOM 208   C CA  . VAL A 1 27  ? 45.941  64.016  56.496 1.000 99.707  0 27  VAL BBB CA  1 ? 3  
ATOM 209   C C   . VAL A 1 27  ? 46.334  63.784  57.952 1.000 110.055 0 27  VAL BBB C   1 ? 3  
ATOM 210   O O   . VAL A 1 27  ? 45.503  63.898  58.860 1.000 118.642 0 27  VAL BBB O   1 ? 3  
ATOM 211   C CB  . VAL A 1 27  ? 45.658  62.697  55.759 1.000 93.027  0 27  VAL BBB CB  1 ? 3  
ATOM 212   C CG1 . VAL A 1 27  ? 44.683  61.842  56.552 1.000 100.789 0 27  VAL BBB CG1 1 ? 3  
ATOM 213   C CG2 . VAL A 1 27  ? 45.118  62.984  54.364 1.000 91.499  0 27  VAL BBB CG2 1 ? 3  
ATOM 214   N N   . GLU A 1 28  ? 47.599  63.441  58.200 1.000 113.634 0 28  GLU BBB N   1 ? 3  
ATOM 215   C CA  . GLU A 1 28  ? 48.054  63.232  59.571 1.000 118.733 0 28  GLU BBB CA  1 ? 3  
ATOM 216   C C   . GLU A 1 28  ? 47.921  64.503  60.406 1.000 115.052 0 28  GLU BBB C   1 ? 3  
ATOM 217   O O   . GLU A 1 28  ? 47.528  64.443  61.577 1.000 119.317 0 28  GLU BBB O   1 ? 3  
ATOM 218   C CB  . GLU A 1 28  ? 49.502  62.743  59.572 1.000 126.169 0 28  GLU BBB CB  1 ? 3  
ATOM 219   C CG  . GLU A 1 28  ? 49.671  61.273  59.209 1.000 142.710 0 28  GLU BBB CG  1 ? 3  
ATOM 220   C CD  . GLU A 1 28  ? 51.127  60.839  59.196 1.000 149.512 0 28  GLU BBB CD  1 ? 3  
ATOM 221   O OE1 . GLU A 1 28  ? 52.010  61.708  59.367 1.000 138.354 0 28  GLU BBB OE1 1 ? 3  
ATOM 222   O OE2 . GLU A 1 28  ? 51.388  59.629  59.022 1.000 158.920 0 28  GLU BBB OE2 1 ? 3  
ATOM 223   N N   . GLU A 1 29  ? 48.219  65.663  59.821 1.000 117.623 0 29  GLU BBB N   1 ? 3  
ATOM 224   C CA  . GLU A 1 29  ? 48.244  66.894  60.604 1.000 123.822 0 29  GLU BBB CA  1 ? 3  
ATOM 225   C C   . GLU A 1 29  ? 46.885  67.578  60.687 1.000 124.396 0 29  GLU BBB C   1 ? 3  
ATOM 226   O O   . GLU A 1 29  ? 46.550  68.159  61.724 1.000 134.439 0 29  GLU BBB O   1 ? 3  
ATOM 227   C CB  . GLU A 1 29  ? 49.232  67.900  60.010 1.000 131.098 0 29  GLU BBB CB  1 ? 3  
ATOM 228   C CG  . GLU A 1 29  ? 50.691  67.539  60.090 1.000 143.709 0 29  GLU BBB CG  1 ? 3  
ATOM 229   C CD  . GLU A 1 29  ? 51.516  68.350  59.107 1.000 164.475 0 29  GLU BBB CD  1 ? 3  
ATOM 230   O OE1 . GLU A 1 29  ? 51.004  69.433  58.643 1.000 162.408 0 29  GLU BBB OE1 1 ? 3  
ATOM 231   O OE2 . GLU A 1 29  ? 52.647  67.933  58.783 1.000 164.576 0 29  GLU BBB OE2 1 ? 3  
ATOM 232   N N   . LYS A 1 30  ? 46.093  67.523  59.618 1.000 112.609 0 30  LYS BBB N   1 ? 3  
ATOM 233   C CA  . LYS A 1 30  ? 44.840  68.260  59.541 1.000 109.140 0 30  LYS BBB CA  1 ? 3  
ATOM 234   C C   . LYS A 1 30  ? 43.609  67.366  59.594 1.000 110.420 0 30  LYS BBB C   1 ? 3  
ATOM 235   O O   . LYS A 1 30  ? 42.491  67.885  59.692 1.000 106.459 0 30  LYS BBB O   1 ? 3  
ATOM 236   C CB  . LYS A 1 30  ? 44.813  69.087  58.248 1.000 107.587 0 30  LYS BBB CB  1 ? 3  
ATOM 237   C CG  . LYS A 1 30  ? 45.959  70.087  58.133 1.000 113.200 0 30  LYS BBB CG  1 ? 3  
ATOM 238   C CD  . LYS A 1 30  ? 45.939  71.147  59.220 1.000 122.793 0 30  LYS BBB CD  1 ? 3  
ATOM 239   C CE  . LYS A 1 30  ? 46.835  72.323  58.844 1.000 139.461 0 30  LYS BBB CE  1 ? 3  
ATOM 240   N NZ  . LYS A 1 30  ? 46.212  73.226  57.850 1.000 142.263 0 30  LYS BBB NZ  1 ? 3  
ATOM 241   N N   . ALA A 1 31  ? 43.788  66.045  59.521 1.000 113.028 0 31  ALA BBB N   1 ? 3  
ATOM 242   C CA  . ALA A 1 31  ? 42.712  65.058  59.475 1.000 112.136 0 31  ALA BBB CA  1 ? 3  
ATOM 243   C C   . ALA A 1 31  ? 41.695  65.389  58.386 1.000 113.129 0 31  ALA BBB C   1 ? 3  
ATOM 244   O O   . ALA A 1 31  ? 42.067  65.531  57.217 1.000 116.356 0 31  ALA BBB O   1 ? 3  
ATOM 245   C CB  . ALA A 1 31  ? 42.031  64.940  60.841 1.000 111.862 0 31  ALA BBB CB  1 ? 3  
ATOM 246   N N   . PHE A 1 32  ? 40.424  65.538  58.743 1.000 107.410 0 32  PHE BBB N   1 ? 3  
ATOM 247   C CA  . PHE A 1 32  ? 39.386  65.887  57.779 1.000 102.514 0 32  PHE BBB CA  1 ? 3  
ATOM 248   C C   . PHE A 1 32  ? 38.799  67.258  58.073 1.000 101.867 0 32  PHE BBB C   1 ? 3  
ATOM 249   O O   . PHE A 1 32  ? 37.591  67.480  57.976 1.000 108.707 0 32  PHE BBB O   1 ? 3  
ATOM 250   C CB  . PHE A 1 32  ? 38.313  64.804  57.714 1.000 105.333 0 32  PHE BBB CB  1 ? 3  
ATOM 251   C CG  . PHE A 1 32  ? 38.836  63.497  57.199 1.000 107.001 0 32  PHE BBB CG  1 ? 3  
ATOM 252   C CD1 . PHE A 1 32  ? 38.999  63.300  55.838 1.000 102.175 0 32  PHE BBB CD1 1 ? 3  
ATOM 253   C CD2 . PHE A 1 32  ? 39.213  62.489  58.068 1.000 112.726 0 32  PHE BBB CD2 1 ? 3  
ATOM 254   C CE1 . PHE A 1 32  ? 39.501  62.113  55.350 1.000 103.303 0 32  PHE BBB CE1 1 ? 3  
ATOM 255   C CE2 . PHE A 1 32  ? 39.716  61.298  57.585 1.000 112.111 0 32  PHE BBB CE2 1 ? 3  
ATOM 256   C CZ  . PHE A 1 32  ? 39.861  61.108  56.224 1.000 108.971 0 32  PHE BBB CZ  1 ? 3  
ATOM 257   N N   . SER A 1 33  ? 39.668  68.200  58.425 1.000 97.980  0 33  SER BBB N   1 ? 3  
ATOM 258   C CA  . SER A 1 33  ? 39.283  69.597  58.425 1.000 101.368 0 33  SER BBB CA  1 ? 3  
ATOM 259   C C   . SER A 1 33  ? 38.925  70.037  57.008 1.000 104.115 0 33  SER BBB C   1 ? 3  
ATOM 260   O O   . SER A 1 33  ? 39.496  69.537  56.034 1.000 113.530 0 33  SER BBB O   1 ? 3  
ATOM 261   C CB  . SER A 1 33  ? 40.413  70.470  58.966 1.000 104.164 0 33  SER BBB CB  1 ? 3  
ATOM 262   O OG  . SER A 1 33  ? 40.792  70.074  60.271 1.000 122.800 0 33  SER BBB OG  1 ? 3  
ATOM 263   N N   . PRO A 1 34  ? 37.965  70.959  56.868 1.000 105.325 0 34  PRO BBB N   1 ? 3  
ATOM 264   C CA  . PRO A 1 34  ? 37.442  71.307  55.536 1.000 106.445 0 34  PRO BBB CA  1 ? 3  
ATOM 265   C C   . PRO A 1 34  ? 38.528  71.715  54.567 1.000 113.378 0 34  PRO BBB C   1 ? 3  
ATOM 266   O O   . PRO A 1 34  ? 38.415  71.466  53.361 1.000 113.516 0 34  PRO BBB O   1 ? 3  
ATOM 267   C CB  . PRO A 1 34  ? 36.493  72.478  55.825 1.000 112.395 0 34  PRO BBB CB  1 ? 3  
ATOM 268   C CG  . PRO A 1 34  ? 36.938  73.003  57.143 1.000 115.241 0 34  PRO BBB CG  1 ? 3  
ATOM 269   C CD  . PRO A 1 34  ? 37.366  71.801  57.914 1.000 115.940 0 34  PRO BBB CD  1 ? 3  
ATOM 270   N N   . GLU A 1 35  ? 39.584  72.349  55.074 1.000 121.452 0 35  GLU BBB N   1 ? 3  
ATOM 271   C CA  . GLU A 1 35  ? 40.673  72.840  54.241 1.000 118.566 0 35  GLU BBB CA  1 ? 3  
ATOM 272   C C   . GLU A 1 35  ? 41.444  71.721  53.536 1.000 112.838 0 35  GLU BBB C   1 ? 3  
ATOM 273   O O   . GLU A 1 35  ? 42.214  72.015  52.618 1.000 115.049 0 35  GLU BBB O   1 ? 3  
ATOM 274   C CB  . GLU A 1 35  ? 41.635  73.633  55.133 1.000 122.882 0 35  GLU BBB CB  1 ? 3  
ATOM 275   C CG  . GLU A 1 35  ? 42.398  72.658  56.041 1.000 133.319 0 35  GLU BBB CG  1 ? 3  
ATOM 276   C CD  . GLU A 1 35  ? 42.820  73.209  57.398 1.000 141.082 0 35  GLU BBB CD  1 ? 3  
ATOM 277   O OE1 . GLU A 1 35  ? 43.936  73.757  57.568 1.000 157.393 0 35  GLU BBB OE1 1 ? 3  
ATOM 278   O OE2 . GLU A 1 35  ? 41.974  73.115  58.307 1.000 138.704 0 35  GLU BBB OE2 1 ? 3  
ATOM 279   N N   . VAL A 1 36  ? 41.273  70.454  53.940 1.000 104.475 0 36  VAL BBB N   1 ? 3  
ATOM 280   C CA  . VAL A 1 36  ? 41.998  69.357  53.289 1.000 97.341  0 36  VAL BBB CA  1 ? 3  
ATOM 281   C C   . VAL A 1 36  ? 41.463  69.092  51.883 1.000 95.806  0 36  VAL BBB C   1 ? 3  
ATOM 282   O O   . VAL A 1 36  ? 42.217  68.685  50.987 1.000 103.215 0 36  VAL BBB O   1 ? 3  
ATOM 283   C CB  A VAL A 1 36  ? 41.952  68.086  54.167 1.000 88.952  0 36  VAL BBB CB  1 ? 3  
ATOM 284   C CG1 A VAL A 1 36  ? 42.312  66.825  53.374 1.000 87.864  0 36  VAL BBB CG1 1 ? 3  
ATOM 285   C CG2 A VAL A 1 36  ? 42.901  68.227  55.329 1.000 94.317  0 36  VAL BBB CG2 1 ? 3  
ATOM 286   N N   . ILE A 1 37  ? 40.170  69.348  51.663 1.000 91.394  0 37  ILE BBB N   1 ? 3  
ATOM 287   C CA  . ILE A 1 37  ? 39.583  69.099  50.347 1.000 87.658  0 37  ILE BBB CA  1 ? 3  
ATOM 288   C C   . ILE A 1 37  ? 40.242  69.936  49.257 1.000 87.968  0 37  ILE BBB C   1 ? 3  
ATOM 289   O O   . ILE A 1 37  ? 40.563  69.375  48.193 1.000 90.122  0 37  ILE BBB O   1 ? 3  
ATOM 290   C CB  . ILE A 1 37  ? 38.043  69.293  50.423 1.000 89.160  0 37  ILE BBB CB  1 ? 3  
ATOM 291   C CG1 . ILE A 1 37  ? 37.430  68.380  51.487 1.000 87.390  0 37  ILE BBB CG1 1 ? 3  
ATOM 292   C CG2 . ILE A 1 37  ? 37.390  69.019  49.081 1.000 94.797  0 37  ILE BBB CG2 1 ? 3  
ATOM 293   C CD1 . ILE A 1 37  ? 35.896  68.424  51.520 1.000 90.260  0 37  ILE BBB CD1 1 ? 3  
ATOM 294   N N   . PRO A 1 38  ? 40.441  71.258  49.412 1.000 85.334  0 38  PRO BBB N   1 ? 3  
ATOM 295   C CA  A PRO A 1 38  ? 41.298  71.972  48.450 1.000 85.071  0 38  PRO BBB CA  1 ? 3  
ATOM 296   C C   . PRO A 1 38  ? 42.604  71.254  48.165 1.000 86.591  0 38  PRO BBB C   1 ? 3  
ATOM 297   O O   . PRO A 1 38  ? 42.960  71.033  47.001 1.000 92.330  0 38  PRO BBB O   1 ? 3  
ATOM 298   C CB  A PRO A 1 38  ? 41.553  73.307  49.158 1.000 86.099  0 38  PRO BBB CB  1 ? 3  
ATOM 299   C CG  A PRO A 1 38  ? 40.354  73.517  50.050 1.000 89.664  0 38  PRO BBB CG  1 ? 3  
ATOM 300   C CD  A PRO A 1 38  ? 39.544  72.227  50.063 1.000 92.453  0 38  PRO BBB CD  1 ? 3  
ATOM 301   N N   . MET A 1 39  ? 43.327  70.890  49.222 1.000 86.851  0 39  MET BBB N   1 ? 3  
ATOM 302   C CA  . MET A 1 39  ? 44.669  70.347  49.070 1.000 83.854  0 39  MET BBB CA  1 ? 3  
ATOM 303   C C   . MET A 1 39  ? 44.665  69.069  48.236 1.000 84.114  0 39  MET BBB C   1 ? 3  
ATOM 304   O O   . MET A 1 39  ? 45.492  68.911  47.330 1.000 87.619  0 39  MET BBB O   1 ? 3  
ATOM 305   C CB  . MET A 1 39  ? 45.273  70.090  50.450 1.000 85.697  0 39  MET BBB CB  1 ? 3  
ATOM 306   C CG  . MET A 1 39  ? 46.743  69.721  50.438 1.000 86.218  0 39  MET BBB CG  1 ? 3  
ATOM 307   S SD  . MET A 1 39  ? 47.723  71.082  49.772 1.000 96.401  0 39  MET BBB SD  1 ? 3  
ATOM 308   C CE  . MET A 1 39  ? 47.698  72.205  51.163 1.000 90.514  0 39  MET BBB CE  1 ? 3  
ATOM 309   N N   . PHE A 1 40  ? 43.720  68.168  48.508 1.000 86.413  0 40  PHE BBB N   1 ? 3  
ATOM 310   C CA  . PHE A 1 40  ? 43.564  66.946  47.722 1.000 80.969  0 40  PHE BBB CA  1 ? 3  
ATOM 311   C C   . PHE A 1 40  ? 43.385  67.252  46.239 1.000 85.910  0 40  PHE BBB C   1 ? 3  
ATOM 312   O O   . PHE A 1 40  ? 44.042  66.644  45.385 1.000 91.898  0 40  PHE BBB O   1 ? 3  
ATOM 313   C CB  . PHE A 1 40  ? 42.383  66.142  48.263 1.000 80.359  0 40  PHE BBB CB  1 ? 3  
ATOM 314   C CG  . PHE A 1 40  ? 42.064  64.906  47.479 1.000 80.082  0 40  PHE BBB CG  1 ? 3  
ATOM 315   C CD1 . PHE A 1 40  ? 42.851  63.774  47.598 1.000 80.123  0 40  PHE BBB CD1 1 ? 3  
ATOM 316   C CD2 . PHE A 1 40  ? 40.972  64.871  46.626 1.000 82.874  0 40  PHE BBB CD2 1 ? 3  
ATOM 317   C CE1 . PHE A 1 40  ? 42.556  62.630  46.880 1.000 80.580  0 40  PHE BBB CE1 1 ? 3  
ATOM 318   C CE2 . PHE A 1 40  ? 40.671  63.729  45.903 1.000 80.048  0 40  PHE BBB CE2 1 ? 3  
ATOM 319   C CZ  . PHE A 1 40  ? 41.461  62.611  46.037 1.000 80.560  0 40  PHE BBB CZ  1 ? 3  
ATOM 320   N N   . SER A 1 41  ? 42.502  68.200  45.914 1.000 92.695  0 41  SER BBB N   1 ? 3  
ATOM 321   C CA  . SER A 1 41  ? 42.244  68.526  44.513 1.000 94.227  0 41  SER BBB CA  1 ? 3  
ATOM 322   C C   . SER A 1 41  ? 43.503  69.024  43.814 1.000 93.907  0 41  SER BBB C   1 ? 3  
ATOM 323   O O   . SER A 1 41  ? 43.752  68.688  42.650 1.000 95.898  0 41  SER BBB O   1 ? 3  
ATOM 324   C CB  . SER A 1 41  ? 41.135  69.574  44.414 1.000 97.801  0 41  SER BBB CB  1 ? 3  
ATOM 325   O OG  . SER A 1 41  ? 40.785  69.830  43.065 1.000 121.504 0 41  SER BBB OG  1 ? 3  
ATOM 326   N N   . ALA A 1 42  ? 44.302  69.841  44.499 1.000 91.290  0 42  ALA BBB N   1 ? 3  
ATOM 327   C CA  . ALA A 1 42  ? 45.520  70.364  43.886 1.000 88.033  0 42  ALA BBB CA  1 ? 3  
ATOM 328   C C   . ALA A 1 42  ? 46.578  69.273  43.751 1.000 85.015  0 42  ALA BBB C   1 ? 3  
ATOM 329   O O   . ALA A 1 42  ? 47.235  69.157  42.709 1.000 84.650  0 42  ALA BBB O   1 ? 3  
ATOM 330   C CB  . ALA A 1 42  ? 46.053  71.543  44.702 1.000 82.992  0 42  ALA BBB CB  1 ? 3  
ATOM 331   N N   . LEU A 1 43  ? 46.750  68.459  44.798 1.000 82.589  0 43  LEU BBB N   1 ? 3  
ATOM 332   C CA  . LEU A 1 43  ? 47.703  67.354  44.766 1.000 81.694  0 43  LEU BBB CA  1 ? 3  
ATOM 333   C C   . LEU A 1 43  ? 47.342  66.285  43.748 1.000 85.558  0 43  LEU BBB C   1 ? 3  
ATOM 334   O O   . LEU A 1 43  ? 48.225  65.527  43.333 1.000 87.738  0 43  LEU BBB O   1 ? 3  
ATOM 335   C CB  . LEU A 1 43  ? 47.842  66.721  46.148 1.000 83.469  0 43  LEU BBB CB  1 ? 3  
ATOM 336   C CG  . LEU A 1 43  ? 48.560  67.598  47.174 1.000 82.369  0 43  LEU BBB CG  1 ? 3  
ATOM 337   C CD1 . LEU A 1 43  ? 48.523  66.962  48.554 1.000 82.599  0 43  LEU BBB CD1 1 ? 3  
ATOM 338   C CD2 . LEU A 1 43  ? 49.983  67.872  46.729 1.000 86.851  0 43  LEU BBB CD2 1 ? 3  
ATOM 339   N N   . SER A 1 44  ? 46.073  66.173  43.360 1.000 86.809  0 44  SER BBB N   1 ? 3  
ATOM 340   C CA  . SER A 1 44  ? 45.665  65.166  42.390 1.000 89.868  0 44  SER BBB CA  1 ? 3  
ATOM 341   C C   . SER A 1 44  ? 45.500  65.741  40.984 1.000 90.799  0 44  SER BBB C   1 ? 3  
ATOM 342   O O   . SER A 1 44  ? 44.764  65.173  40.170 1.000 93.535  0 44  SER BBB O   1 ? 3  
ATOM 343   C CB  . SER A 1 44  ? 44.366  64.501  42.840 1.000 88.543  0 44  SER BBB CB  1 ? 3  
ATOM 344   O OG  . SER A 1 44  ? 43.322  65.455  42.905 1.000 94.721  0 44  SER BBB OG  1 ? 3  
ATOM 345   N N   . CYS A 1 45  ? 46.151  66.866  40.695 1.000 90.154  0 45  CYS BBB N   1 ? 3  
ATOM 346   C CA  . CYS A 1 45  ? 46.094  67.456  39.366 1.000 87.040  0 45  CYS BBB CA  1 ? 3  
ATOM 347   C C   . CYS A 1 45  ? 46.624  66.485  38.322 1.000 89.913  0 45  CYS BBB C   1 ? 3  
ATOM 348   O O   . CYS A 1 45  ? 47.733  65.962  38.452 1.000 101.076 0 45  CYS BBB O   1 ? 3  
ATOM 349   C CB  . CYS A 1 45  ? 46.931  68.736  39.355 1.000 95.645  0 45  CYS BBB CB  1 ? 3  
ATOM 350   S SG  . CYS A 1 45  ? 46.939  69.690  37.829 1.000 128.616 0 45  CYS BBB SG  1 ? 3  
ATOM 351   N N   . GLY A 1 46  ? 45.823  66.229  37.287 1.000 93.554  0 46  GLY BBB N   1 ? 3  
ATOM 352   C CA  . GLY A 1 46  ? 46.229  65.331  36.218 1.000 93.450  0 46  GLY BBB CA  1 ? 3  
ATOM 353   C C   . GLY A 1 46  ? 46.243  63.863  36.567 1.000 86.434  0 46  GLY BBB C   1 ? 3  
ATOM 354   O O   . GLY A 1 46  ? 46.699  63.052  35.756 1.000 91.126  0 46  GLY BBB O   1 ? 3  
ATOM 355   N N   . ALA A 1 47  ? 45.752  63.503  37.745 1.000 83.117  0 47  ALA BBB N   1 ? 3  
ATOM 356   C CA  . ALA A 1 47  ? 45.857  62.137  38.236 1.000 91.960  0 47  ALA BBB CA  1 ? 3  
ATOM 357   C C   . ALA A 1 47  ? 45.019  61.181  37.393 1.000 83.978  0 47  ALA BBB C   1 ? 3  
ATOM 358   O O   . ALA A 1 47  ? 43.915  61.521  36.952 1.000 79.669  0 47  ALA BBB O   1 ? 3  
ATOM 359   C CB  . ALA A 1 47  ? 45.438  62.079  39.702 1.000 96.534  0 47  ALA BBB CB  1 ? 3  
ATOM 360   N N   . THR A 1 48  ? 45.550  59.974  37.170 1.000 85.812  0 48  THR BBB N   1 ? 3  
ATOM 361   C CA  . THR A 1 48  ? 44.725  58.887  36.669 1.000 83.897  0 48  THR BBB CA  1 ? 3  
ATOM 362   C C   . THR A 1 48  ? 43.864  58.327  37.797 1.000 85.109  0 48  THR BBB C   1 ? 3  
ATOM 363   O O   . THR A 1 48  ? 44.190  58.500  38.969 1.000 91.344  0 48  THR BBB O   1 ? 3  
ATOM 364   C CB  . THR A 1 48  ? 45.615  57.775  36.115 1.000 86.987  0 48  THR BBB CB  1 ? 3  
ATOM 365   O OG1 . THR A 1 48  ? 46.409  57.225  37.175 1.000 89.067  0 48  THR BBB OG1 1 ? 3  
ATOM 366   C CG2 . THR A 1 48  ? 46.549  58.316  35.040 1.000 90.640  0 48  THR BBB CG2 1 ? 3  
ATOM 367   N N   . PRO A 1 49  ? 42.821  57.552  37.472 1.000 83.872  0 49  PRO BBB N   1 ? 3  
ATOM 368   C CA  . PRO A 1 49  ? 42.087  56.836  38.532 1.000 84.968  0 49  PRO BBB CA  1 ? 3  
ATOM 369   C C   . PRO A 1 49  ? 42.966  55.968  39.407 1.000 93.960  0 49  PRO BBB C   1 ? 3  
ATOM 370   O O   . PRO A 1 49  ? 42.743  55.891  40.623 1.000 103.482 0 49  PRO BBB O   1 ? 3  
ATOM 371   C CB  . PRO A 1 49  ? 41.069  56.009  37.743 1.000 85.470  0 49  PRO BBB CB  1 ? 3  
ATOM 372   C CG  . PRO A 1 49  ? 40.778  56.848  36.556 1.000 85.118  0 49  PRO BBB CG  1 ? 3  
ATOM 373   C CD  . PRO A 1 49  ? 42.085  57.530  36.195 1.000 85.774  0 49  PRO BBB CD  1 ? 3  
ATOM 374   N N   . GLN A 1 50  ? 43.953  55.299  38.814 1.000 87.570  0 50  GLN BBB N   1 ? 3  
ATOM 375   C CA  . GLN A 1 50  ? 44.919  54.544  39.602 1.000 95.221  0 50  GLN BBB CA  1 ? 3  
ATOM 376   C C   . GLN A 1 50  ? 45.599  55.423  40.649 1.000 98.893  0 50  GLN BBB C   1 ? 3  
ATOM 377   O O   . GLN A 1 50  ? 45.706  55.043  41.822 1.000 99.564  0 50  GLN BBB O   1 ? 3  
ATOM 378   C CB  . GLN A 1 50  ? 45.950  53.912  38.672 1.000 91.437  0 50  GLN BBB CB  1 ? 3  
ATOM 379   C CG  . GLN A 1 50  ? 46.857  52.926  39.362 1.000 106.486 0 50  GLN BBB CG  1 ? 3  
ATOM 380   C CD  . GLN A 1 50  ? 48.004  52.487  38.481 1.000 115.910 0 50  GLN BBB CD  1 ? 3  
ATOM 381   O OE1 . GLN A 1 50  ? 48.782  53.313  37.997 1.000 114.667 0 50  GLN BBB OE1 1 ? 3  
ATOM 382   N NE2 . GLN A 1 50  ? 48.126  51.179  38.275 1.000 128.317 0 50  GLN BBB NE2 1 ? 3  
ATOM 383   N N   . ASP A 1 51  ? 46.051  56.613  40.243 1.000 104.907 0 51  ASP BBB N   1 ? 3  
ATOM 384   C CA  . ASP A 1 51  ? 46.727  57.523  41.167 1.000 101.616 0 51  ASP BBB CA  1 ? 3  
ATOM 385   C C   . ASP A 1 51  ? 45.818  57.966  42.309 1.000 96.788  0 51  ASP BBB C   1 ? 3  
ATOM 386   O O   . ASP A 1 51  ? 46.260  58.033  43.462 1.000 98.221  0 51  ASP BBB O   1 ? 3  
ATOM 387   C CB  . ASP A 1 51  ? 47.262  58.726  40.393 1.000 105.306 0 51  ASP BBB CB  1 ? 3  
ATOM 388   C CG  . ASP A 1 51  ? 48.387  58.348  39.433 1.000 115.665 0 51  ASP BBB CG  1 ? 3  
ATOM 389   O OD1 . ASP A 1 51  ? 49.119  57.373  39.719 1.000 122.712 0 51  ASP BBB OD1 1 ? 3  
ATOM 390   O OD2 . ASP A 1 51  ? 48.501  58.983  38.364 1.000 110.443 0 51  ASP BBB OD2 1 ? 3  
ATOM 391   N N   . LEU A 1 52  ? 44.549  58.281  42.016 1.000 89.843  0 52  LEU BBB N   1 ? 3  
ATOM 392   C CA  . LEU A 1 52  ? 43.650  58.685  43.095 1.000 88.014  0 52  LEU BBB CA  1 ? 3  
ATOM 393   C C   . LEU A 1 52  ? 43.458  57.555  44.092 1.000 90.367  0 52  LEU BBB C   1 ? 3  
ATOM 394   O O   . LEU A 1 52  ? 43.463  57.785  45.307 1.000 91.503  0 52  LEU BBB O   1 ? 3  
ATOM 395   C CB  . LEU A 1 52  ? 42.287  59.173  42.597 1.000 82.827  0 52  LEU BBB CB  1 ? 3  
ATOM 396   C CG  . LEU A 1 52  ? 42.073  60.451  41.782 1.000 81.829  0 52  LEU BBB CG  1 ? 3  
ATOM 397   C CD1 . LEU A 1 52  ? 42.541  60.340  40.390 1.000 93.174  0 52  LEU BBB CD1 1 ? 3  
ATOM 398   C CD2 . LEU A 1 52  ? 40.615  60.831  41.791 1.000 81.947  0 52  LEU BBB CD2 1 ? 3  
ATOM 399   N N   . ASN A 1 53  ? 43.286  56.324  43.607 1.000 86.012  0 53  ASN BBB N   1 ? 3  
ATOM 400   C CA  . ASN A 1 53  ? 43.165  55.203  44.531 1.000 88.744  0 53  ASN BBB CA  1 ? 3  
ATOM 401   C C   . ASN A 1 53  ? 44.437  55.018  45.346 1.000 91.800  0 53  ASN BBB C   1 ? 3  
ATOM 402   O O   . ASN A 1 53  ? 44.377  54.735  46.548 1.000 89.923  0 53  ASN BBB O   1 ? 3  
ATOM 403   C CB  . ASN A 1 53  ? 42.849  53.928  43.758 1.000 90.202  0 53  ASN BBB CB  1 ? 3  
ATOM 404   C CG  . ASN A 1 53  ? 41.441  53.906  43.259 1.000 91.222  0 53  ASN BBB CG  1 ? 3  
ATOM 405   O OD1 . ASN A 1 53  ? 40.543  54.464  43.891 1.000 97.781  0 53  ASN BBB OD1 1 ? 3  
ATOM 406   N ND2 . ASN A 1 53  ? 41.229  53.278  42.115 1.000 98.984  0 53  ASN BBB ND2 1 ? 3  
ATOM 407   N N   . THR A 1 54  ? 45.594  55.162  44.706 1.000 93.395  0 54  THR BBB N   1 ? 3  
ATOM 408   C CA  . THR A 1 54  ? 46.859  55.138  45.429 1.000 90.095  0 54  THR BBB CA  1 ? 3  
ATOM 409   C C   . THR A 1 54  ? 46.903  56.164  46.563 1.000 87.848  0 54  THR BBB C   1 ? 3  
ATOM 410   O O   . THR A 1 54  ? 47.229  55.830  47.706 1.000 93.865  0 54  THR BBB O   1 ? 3  
ATOM 411   C CB  . THR A 1 54  ? 48.004  55.362  44.449 1.000 87.963  0 54  THR BBB CB  1 ? 3  
ATOM 412   O OG1 . THR A 1 54  ? 48.070  54.249  43.545 1.000 94.828  0 54  THR BBB OG1 1 ? 3  
ATOM 413   C CG2 . THR A 1 54  ? 49.313  55.493  45.204 1.000 88.033  0 54  THR BBB CG2 1 ? 3  
ATOM 414   N N   . MET A 1 55  ? 46.558  57.420  46.270 1.000 85.379  0 55  MET BBB N   1 ? 3  
ATOM 415   C CA  . MET A 1 55  ? 46.583  58.453  47.306 1.000 85.736  0 55  MET BBB CA  1 ? 3  
ATOM 416   C C   . MET A 1 55  ? 45.674  58.103  48.482 1.000 90.262  0 55  MET BBB C   1 ? 3  
ATOM 417   O O   . MET A 1 55  ? 46.072  58.231  49.647 1.000 89.802  0 55  MET BBB O   1 ? 3  
ATOM 418   C CB  . MET A 1 55  ? 46.192  59.810  46.716 1.000 83.820  0 55  MET BBB CB  1 ? 3  
ATOM 419   C CG  . MET A 1 55  ? 47.202  60.413  45.757 1.000 84.572  0 55  MET BBB CG  1 ? 3  
ATOM 420   S SD  . MET A 1 55  ? 46.546  61.917  44.998 1.000 96.152  0 55  MET BBB SD  1 ? 3  
ATOM 421   C CE  . MET A 1 55  ? 46.706  63.090  46.336 1.000 89.540  0 55  MET BBB CE  1 ? 3  
ATOM 422   N N   . LEU A 1 56  ? 44.447  57.659  48.198 1.000 91.889  0 56  LEU BBB N   1 ? 3  
ATOM 423   C CA  . LEU A 1 56  ? 43.516  57.295  49.264 1.000 89.631  0 56  LEU BBB CA  1 ? 3  
ATOM 424   C C   . LEU A 1 56  ? 43.968  56.052  50.026 1.000 90.449  0 56  LEU BBB C   1 ? 3  
ATOM 425   O O   . LEU A 1 56  ? 43.837  55.987  51.254 1.000 91.226  0 56  LEU BBB O   1 ? 3  
ATOM 426   C CB  . LEU A 1 56  ? 42.121  57.067  48.678 1.000 89.412  0 56  LEU BBB CB  1 ? 3  
ATOM 427   C CG  . LEU A 1 56  ? 41.447  58.264  48.002 1.000 87.279  0 56  LEU BBB CG  1 ? 3  
ATOM 428   C CD1 . LEU A 1 56  ? 40.072  57.878  47.467 1.000 87.050  0 56  LEU BBB CD1 1 ? 3  
ATOM 429   C CD2 . LEU A 1 56  ? 41.370  59.475  48.925 1.000 87.240  0 56  LEU BBB CD2 1 ? 3  
ATOM 430   N N   . ASN A 1 57  ? 44.493  55.054  49.317 1.000 90.271  0 57  ASN BBB N   1 ? 3  
ATOM 431   C CA  . ASN A 1 57  ? 44.913  53.814  49.960 1.000 92.552  0 57  ASN BBB CA  1 ? 3  
ATOM 432   C C   . ASN A 1 57  ? 46.147  53.976  50.841 1.000 92.746  0 57  ASN BBB C   1 ? 3  
ATOM 433   O O   . ASN A 1 57  ? 46.341  53.166  51.753 1.000 95.619  0 57  ASN BBB O   1 ? 3  
ATOM 434   C CB  . ASN A 1 57  ? 45.134  52.734  48.909 1.000 94.212  0 57  ASN BBB CB  1 ? 3  
ATOM 435   C CG  . ASN A 1 57  ? 43.827  52.183  48.379 1.000 103.090 0 57  ASN BBB CG  1 ? 3  
ATOM 436   O OD1 . ASN A 1 57  ? 42.758  52.737  48.645 1.000 108.623 0 57  ASN BBB OD1 1 ? 3  
ATOM 437   N ND2 . ASN A 1 57  ? 43.901  51.086  47.637 1.000 109.378 0 57  ASN BBB ND2 1 ? 3  
ATOM 438   N N   . THR A 1 58  ? 46.995  54.975  50.585 1.000 91.196  0 58  THR BBB N   1 ? 3  
ATOM 439   C CA  . THR A 1 58  ? 48.195  55.159  51.397 1.000 93.279  0 58  THR BBB CA  1 ? 3  
ATOM 440   C C   . THR A 1 58  ? 47.898  55.772  52.760 1.000 98.581  0 58  THR BBB C   1 ? 3  
ATOM 441   O O   . THR A 1 58  ? 48.788  55.789  53.620 1.000 104.905 0 58  THR BBB O   1 ? 3  
ATOM 442   C CB  . THR A 1 58  ? 49.222  56.035  50.666 1.000 92.487  0 58  THR BBB CB  1 ? 3  
ATOM 443   O OG1 . THR A 1 58  ? 48.622  57.281  50.286 1.000 89.579  0 58  THR BBB OG1 1 ? 3  
ATOM 444   C CG2 . THR A 1 58  ? 49.771  55.324  49.439 1.000 93.661  0 58  THR BBB CG2 1 ? 3  
ATOM 445   N N   . VAL A 1 59  ? 46.667  56.232  52.985 1.000 97.984  0 59  VAL BBB N   1 ? 3  
ATOM 446   C CA  . VAL A 1 59  ? 46.258  56.752  54.285 1.000 95.452  0 59  VAL BBB CA  1 ? 3  
ATOM 447   C C   . VAL A 1 59  ? 46.102  55.586  55.247 1.000 98.712  0 59  VAL BBB C   1 ? 3  
ATOM 448   O O   . VAL A 1 59  ? 45.358  54.634  54.976 1.000 101.620 0 59  VAL BBB O   1 ? 3  
ATOM 449   C CB  . VAL A 1 59  ? 44.956  57.556  54.170 1.000 93.899  0 59  VAL BBB CB  1 ? 3  
ATOM 450   C CG1 . VAL A 1 59  ? 44.532  58.060  55.534 1.000 98.834  0 59  VAL BBB CG1 1 ? 3  
ATOM 451   C CG2 . VAL A 1 59  ? 45.150  58.725  53.235 1.000 93.616  0 59  VAL BBB CG2 1 ? 3  
ATOM 452   N N   . GLY A 1 60  ? 46.787  55.664  56.384 1.000 100.957 0 60  GLY BBB N   1 ? 3  
ATOM 453   C CA  . GLY A 1 60  ? 46.787  54.570  57.333 1.000 113.488 0 60  GLY BBB CA  1 ? 3  
ATOM 454   C C   . GLY A 1 60  ? 45.666  54.581  58.352 1.000 112.182 0 60  GLY BBB C   1 ? 3  
ATOM 455   O O   . GLY A 1 60  ? 45.117  53.516  58.653 1.000 111.645 0 60  GLY BBB O   1 ? 3  
ATOM 456   N N   . GLY A 1 61  ? 45.323  55.736  58.912 1.000 105.250 0 61  GLY BBB N   1 ? 3  
ATOM 457   C CA  . GLY A 1 61  ? 44.271  55.818  59.906 1.000 115.296 0 61  GLY BBB CA  1 ? 3  
ATOM 458   C C   . GLY A 1 61  ? 42.923  56.101  59.274 1.000 113.410 0 61  GLY BBB C   1 ? 3  
ATOM 459   O O   . GLY A 1 61  ? 42.724  55.924  58.070 1.000 112.915 0 61  GLY BBB O   1 ? 3  
ATOM 460   N N   . HIS A 1 62  ? 41.979  56.544  60.108 1.000 116.754 0 62  HIS BBB N   1 ? 3  
ATOM 461   C CA  . HIS A 1 62  ? 40.689  57.067  59.643 1.000 115.156 0 62  HIS BBB CA  1 ? 3  
ATOM 462   C C   . HIS A 1 62  ? 39.969  56.081  58.731 1.000 115.797 0 62  HIS BBB C   1 ? 3  
ATOM 463   O O   . HIS A 1 62  ? 39.335  56.470  57.747 1.000 123.574 0 62  HIS BBB O   1 ? 3  
ATOM 464   C CB  . HIS A 1 62  ? 40.852  58.403  58.920 1.000 115.368 0 62  HIS BBB CB  1 ? 3  
ATOM 465   C CG  . HIS A 1 62  ? 41.560  59.449  59.717 1.000 115.833 0 62  HIS BBB CG  1 ? 3  
ATOM 466   N ND1 . HIS A 1 62  ? 40.998  60.050  60.822 1.000 124.150 0 62  HIS BBB ND1 1 ? 3  
ATOM 467   C CD2 . HIS A 1 62  ? 42.776  60.020  59.554 1.000 114.225 0 62  HIS BBB CD2 1 ? 3  
ATOM 468   C CE1 . HIS A 1 62  ? 41.843  60.940  61.313 1.000 126.896 0 62  HIS BBB CE1 1 ? 3  
ATOM 469   N NE2 . HIS A 1 62  ? 42.929  60.942  60.561 1.000 117.768 0 62  HIS BBB NE2 1 ? 3  
ATOM 470   N N   . GLN A 1 63  ? 40.063  54.791  59.047 1.000 110.308 0 63  GLN BBB N   1 ? 3  
ATOM 471   C CA  . GLN A 1 63  ? 39.509  53.791  58.143 1.000 112.587 0 63  GLN BBB CA  1 ? 3  
ATOM 472   C C   . GLN A 1 63  ? 37.986  53.792  58.124 1.000 116.724 0 63  GLN BBB C   1 ? 3  
ATOM 473   O O   . GLN A 1 63  ? 37.396  53.301  57.155 1.000 120.818 0 63  GLN BBB O   1 ? 3  
ATOM 474   C CB  . GLN A 1 63  ? 40.037  52.402  58.505 1.000 116.294 0 63  GLN BBB CB  1 ? 3  
ATOM 475   C CG  . GLN A 1 63  ? 41.515  52.202  58.209 1.000 121.175 0 63  GLN BBB CG  1 ? 3  
ATOM 476   C CD  . GLN A 1 63  ? 41.840  52.371  56.729 1.000 122.519 0 63  GLN BBB CD  1 ? 3  
ATOM 477   O OE1 . GLN A 1 63  ? 41.426  51.565  55.895 1.000 125.788 0 63  GLN BBB OE1 1 ? 3  
ATOM 478   N NE2 . GLN A 1 63  ? 42.578  53.425  56.399 1.000 121.233 0 63  GLN BBB NE2 1 ? 3  
ATOM 479   N N   . ALA A 1 64  ? 37.339  54.327  59.163 1.000 114.827 0 64  ALA BBB N   1 ? 3  
ATOM 480   C CA  . ALA A 1 64  ? 35.895  54.535  59.107 1.000 114.147 0 64  ALA BBB CA  1 ? 3  
ATOM 481   C C   . ALA A 1 64  ? 35.520  55.514  58.005 1.000 112.365 0 64  ALA BBB C   1 ? 3  
ATOM 482   O O   . ALA A 1 64  ? 34.622  55.245  57.198 1.000 117.678 0 64  ALA BBB O   1 ? 3  
ATOM 483   C CB  . ALA A 1 64  ? 35.384  55.043  60.452 1.000 121.279 0 64  ALA BBB CB  1 ? 3  
ATOM 484   N N   . ALA A 1 65  ? 36.212  56.653  57.946 1.000 111.666 0 65  ALA BBB N   1 ? 3  
ATOM 485   C CA  . ALA A 1 65  ? 35.948  57.616  56.885 1.000 110.434 0 65  ALA BBB CA  1 ? 3  
ATOM 486   C C   . ALA A 1 65  ? 36.220  57.002  55.521 1.000 108.657 0 65  ALA BBB C   1 ? 3  
ATOM 487   O O   . ALA A 1 65  ? 35.447  57.199  54.577 1.000 112.479 0 65  ALA BBB O   1 ? 3  
ATOM 488   C CB  . ALA A 1 65  ? 36.785  58.876  57.096 1.000 110.192 0 65  ALA BBB CB  1 ? 3  
ATOM 489   N N   . MET A 1 66  ? 37.311  56.241  55.402 1.000 102.859 0 66  MET BBB N   1 ? 3  
ATOM 490   C CA  . MET A 1 66  ? 37.639  55.612  54.129 1.000 103.814 0 66  MET BBB CA  1 ? 3  
ATOM 491   C C   . MET A 1 66  ? 36.554  54.635  53.703 1.000 111.322 0 66  MET BBB C   1 ? 3  
ATOM 492   O O   . MET A 1 66  ? 36.217  54.551  52.516 1.000 121.993 0 66  MET BBB O   1 ? 3  
ATOM 493   C CB  . MET A 1 66  ? 38.990  54.908  54.223 1.000 108.571 0 66  MET BBB CB  1 ? 3  
ATOM 494   C CG  . MET A 1 66  ? 40.096  55.779  54.782 1.000 106.959 0 66  MET BBB CG  1 ? 3  
ATOM 495   S SD  . MET A 1 66  ? 40.607  57.040  53.601 1.000 99.737  0 66  MET BBB SD  1 ? 3  
ATOM 496   C CE  . MET A 1 66  ? 40.815  56.049  52.119 1.000 106.824 0 66  MET BBB CE  1 ? 3  
ATOM 497   N N   . GLN A 1 67  ? 35.992  53.890  54.657 1.000 108.278 0 67  GLN BBB N   1 ? 3  
ATOM 498   C CA  . GLN A 1 67  ? 34.912  52.968  54.326 1.000 110.857 0 67  GLN BBB CA  1 ? 3  
ATOM 499   C C   . GLN A 1 67  ? 33.658  53.722  53.896 1.000 112.706 0 67  GLN BBB C   1 ? 3  
ATOM 500   O O   . GLN A 1 67  ? 32.961  53.296  52.968 1.000 115.090 0 67  GLN BBB O   1 ? 3  
ATOM 501   C CB  . GLN A 1 67  ? 34.622  52.052  55.510 1.000 121.230 0 67  GLN BBB CB  1 ? 3  
ATOM 502   C CG  . GLN A 1 67  ? 33.840  50.818  55.129 1.000 132.166 0 67  GLN BBB CG  1 ? 3  
ATOM 503   C CD  . GLN A 1 67  ? 34.718  49.776  54.468 1.000 141.833 0 67  GLN BBB CD  1 ? 3  
ATOM 504   O OE1 . GLN A 1 67  ? 35.903  49.657  54.784 1.000 140.753 0 67  GLN BBB OE1 1 ? 3  
ATOM 505   N NE2 . GLN A 1 67  ? 34.141  49.013  53.547 1.000 149.572 0 67  GLN BBB NE2 1 ? 3  
ATOM 506   N N   . MET A 1 68  ? 33.358  54.846  54.553 1.000 113.652 0 68  MET BBB N   1 ? 3  
ATOM 507   C CA  . MET A 1 68  ? 32.265  55.699  54.094 1.000 114.284 0 68  MET BBB CA  1 ? 3  
ATOM 508   C C   . MET A 1 68  ? 32.520  56.209  52.690 1.000 113.184 0 68  MET BBB C   1 ? 3  
ATOM 509   O O   . MET A 1 68  ? 31.604  56.260  51.861 1.000 121.033 0 68  MET BBB O   1 ? 3  
ATOM 510   C CB  . MET A 1 68  ? 32.103  56.910  55.006 1.000 121.381 0 68  MET BBB CB  1 ? 3  
ATOM 511   C CG  . MET A 1 68  ? 31.472  56.641  56.304 1.000 124.810 0 68  MET BBB CG  1 ? 3  
ATOM 512   S SD  . MET A 1 68  ? 30.991  58.131  57.192 1.000 145.654 0 68  MET BBB SD  1 ? 3  
ATOM 513   C CE  . MET A 1 68  ? 32.582  58.741  57.736 1.000 132.976 0 68  MET BBB CE  1 ? 3  
ATOM 514   N N   . LEU A 1 69  ? 33.761  56.605  52.415 1.000 105.883 0 69  LEU BBB N   1 ? 3  
ATOM 515   C CA  . LEU A 1 69  ? 34.121  57.061  51.081 1.000 100.560 0 69  LEU BBB CA  1 ? 3  
ATOM 516   C C   . LEU A 1 69  ? 33.899  55.969  50.041 1.000 104.847 0 69  LEU BBB C   1 ? 3  
ATOM 517   O O   . LEU A 1 69  ? 33.392  56.244  48.948 1.000 113.456 0 69  LEU BBB O   1 ? 3  
ATOM 518   C CB  . LEU A 1 69  ? 35.571  57.543  51.087 1.000 96.575  0 69  LEU BBB CB  1 ? 3  
ATOM 519   C CG  . LEU A 1 69  ? 36.128  58.139  49.798 1.000 94.182  0 69  LEU BBB CG  1 ? 3  
ATOM 520   C CD1 . LEU A 1 69  ? 35.215  59.251  49.299 1.000 96.107  0 69  LEU BBB CD1 1 ? 3  
ATOM 521   C CD2 . LEU A 1 69  ? 37.547  58.652  50.008 1.000 91.755  0 69  LEU BBB CD2 1 ? 3  
ATOM 522   N N   . LYS A 1 70  ? 34.260  54.722  50.363 1.000 105.292 0 70  LYS BBB N   1 ? 3  
ATOM 523   C CA  . LYS A 1 70  ? 34.034  53.629  49.421 1.000 108.708 0 70  LYS BBB CA  1 ? 3  
ATOM 524   C C   . LYS A 1 70  ? 32.549  53.484  49.108 1.000 115.566 0 70  LYS BBB C   1 ? 3  
ATOM 525   O O   . LYS A 1 70  ? 32.163  53.270  47.953 1.000 122.407 0 70  LYS BBB O   1 ? 3  
ATOM 526   C CB  . LYS A 1 70  ? 34.593  52.314  49.974 1.000 107.341 0 70  LYS BBB CB  1 ? 3  
ATOM 527   C CG  . LYS A 1 70  ? 36.096  52.307  50.256 1.000 109.098 0 70  LYS BBB CG  1 ? 3  
ATOM 528   C CD  . LYS A 1 70  ? 36.929  52.851  49.099 1.000 119.718 0 70  LYS BBB CD  1 ? 3  
ATOM 529   C CE  . LYS A 1 70  ? 38.381  53.084  49.528 1.000 116.636 0 70  LYS BBB CE  1 ? 3  
ATOM 530   N NZ  . LYS A 1 70  ? 39.182  53.829  48.510 1.000 109.543 0 70  LYS BBB NZ  1 ? 3  
ATOM 531   N N   . GLU A 1 71  ? 31.705  53.594  50.135 1.000 120.639 0 71  GLU BBB N   1 ? 3  
ATOM 532   C CA  . GLU A 1 71  ? 30.261  53.553  49.938 1.000 123.653 0 71  GLU BBB CA  1 ? 3  
ATOM 533   C C   . GLU A 1 71  ? 29.789  54.669  49.014 1.000 122.304 0 71  GLU BBB C   1 ? 3  
ATOM 534   O O   . GLU A 1 71  ? 28.962  54.439  48.124 1.000 129.789 0 71  GLU BBB O   1 ? 3  
ATOM 535   C CB  . GLU A 1 71  ? 29.567  53.644  51.294 1.000 132.648 0 71  GLU BBB CB  1 ? 3  
ATOM 536   C CG  . GLU A 1 71  ? 29.686  52.381  52.127 1.000 143.618 0 71  GLU BBB CG  1 ? 3  
ATOM 537   C CD  . GLU A 1 71  ? 28.774  52.403  53.336 1.000 161.766 0 71  GLU BBB CD  1 ? 3  
ATOM 538   O OE1 . GLU A 1 71  ? 28.429  53.518  53.808 1.000 166.526 0 71  GLU BBB OE1 1 ? 3  
ATOM 539   O OE2 . GLU A 1 71  ? 28.368  51.320  53.811 1.000 167.790 0 71  GLU BBB OE2 1 ? 3  
ATOM 540   N N   . THR A 1 72  ? 30.291  55.889  49.219 1.000 113.212 0 72  THR BBB N   1 ? 3  
ATOM 541   C CA  . THR A 1 72  ? 29.878  57.004  48.372 1.000 110.670 0 72  THR BBB CA  1 ? 3  
ATOM 542   C C   . THR A 1 72  ? 30.319  56.800  46.926 1.000 111.073 0 72  THR BBB C   1 ? 3  
ATOM 543   O O   . THR A 1 72  ? 29.547  57.055  45.994 1.000 121.021 0 72  THR BBB O   1 ? 3  
ATOM 544   C CB  . THR A 1 72  ? 30.436  58.314  48.926 1.000 105.515 0 72  THR BBB CB  1 ? 3  
ATOM 545   O OG1 . THR A 1 72  ? 29.890  58.553  50.230 1.000 114.320 0 72  THR BBB OG1 1 ? 3  
ATOM 546   C CG2 . THR A 1 72  ? 30.078  59.471  48.013 1.000 106.842 0 72  THR BBB CG2 1 ? 3  
ATOM 547   N N   . ILE A 1 73  ? 31.558  56.348  46.722 1.000 106.067 0 73  ILE BBB N   1 ? 3  
ATOM 548   C CA  . ILE A 1 73  ? 32.043  56.055  45.375 1.000 107.115 0 73  ILE BBB CA  1 ? 3  
ATOM 549   C C   . ILE A 1 73  ? 31.167  55.002  44.707 1.000 117.255 0 73  ILE BBB C   1 ? 3  
ATOM 550   O O   . ILE A 1 73  ? 30.776  55.142  43.542 1.000 124.833 0 73  ILE BBB O   1 ? 3  
ATOM 551   C CB  . ILE A 1 73  ? 33.522  55.619  45.426 1.000 103.999 0 73  ILE BBB CB  1 ? 3  
ATOM 552   C CG1 . ILE A 1 73  ? 34.429  56.802  45.775 1.000 100.745 0 73  ILE BBB CG1 1 ? 3  
ATOM 553   C CG2 . ILE A 1 73  ? 33.959  54.991  44.116 1.000 108.169 0 73  ILE BBB CG2 1 ? 3  
ATOM 554   C CD1 . ILE A 1 73  ? 35.845  56.391  46.125 1.000 95.871  0 73  ILE BBB CD1 1 ? 3  
ATOM 555   N N   . ASN A 1 74  ? 30.832  53.942  45.443 1.000 117.623 0 74  ASN BBB N   1 ? 3  
ATOM 556   C CA  . ASN A 1 74  ? 30.002  52.878  44.889 1.000 117.502 0 74  ASN BBB CA  1 ? 3  
ATOM 557   C C   . ASN A 1 74  ? 28.609  53.380  44.533 1.000 122.730 0 74  ASN BBB C   1 ? 3  
ATOM 558   O O   . ASN A 1 74  ? 28.049  52.995  43.500 1.000 127.124 0 74  ASN BBB O   1 ? 3  
ATOM 559   C CB  . ASN A 1 74  ? 29.925  51.722  45.883 1.000 125.786 0 74  ASN BBB CB  1 ? 3  
ATOM 560   C CG  . ASN A 1 74  ? 31.236  50.976  46.002 1.000 134.031 0 74  ASN BBB CG  1 ? 3  
ATOM 561   O OD1 . ASN A 1 74  ? 32.282  51.473  45.578 1.000 139.983 0 74  ASN BBB OD1 1 ? 3  
ATOM 562   N ND2 . ASN A 1 74  ? 31.194  49.784  46.588 1.000 142.754 0 74  ASN BBB ND2 1 ? 3  
ATOM 563   N N   . GLU A 1 75  ? 28.038  54.252  45.366 1.000 135.914 0 75  GLU BBB N   1 ? 3  
ATOM 564   C CA  . GLU A 1 75  ? 26.755  54.864  45.033 1.000 142.275 0 75  GLU BBB CA  1 ? 3  
ATOM 565   C C   . GLU A 1 75  ? 26.842  55.675  43.746 1.000 138.536 0 75  GLU BBB C   1 ? 3  
ATOM 566   O O   . GLU A 1 75  ? 25.974  55.561  42.875 1.000 145.624 0 75  GLU BBB O   1 ? 3  
ATOM 567   C CB  . GLU A 1 75  ? 26.280  55.739  46.193 1.000 150.281 0 75  GLU BBB CB  1 ? 3  
ATOM 568   C CG  . GLU A 1 75  ? 25.015  56.529  45.907 1.000 170.785 0 75  GLU BBB CG  1 ? 3  
ATOM 569   C CD  . GLU A 1 75  ? 24.487  57.252  47.135 1.000 186.290 0 75  GLU BBB CD  1 ? 3  
ATOM 570   O OE1 . GLU A 1 75  ? 25.296  57.560  48.043 1.000 183.210 0 75  GLU BBB OE1 1 ? 3  
ATOM 571   O OE2 . GLU A 1 75  ? 23.268  57.527  47.188 1.000 191.594 0 75  GLU BBB OE2 1 ? 3  
ATOM 572   N N   . GLU A 1 76  ? 27.896  56.477  43.594 1.000 126.528 0 76  GLU BBB N   1 ? 3  
ATOM 573   C CA  . GLU A 1 76  ? 28.067  57.284  42.387 1.000 123.459 0 76  GLU BBB CA  1 ? 3  
ATOM 574   C C   . GLU A 1 76  ? 28.336  56.428  41.158 1.000 124.193 0 76  GLU BBB C   1 ? 3  
ATOM 575   O O   . GLU A 1 76  ? 27.907  56.780  40.053 1.000 127.475 0 76  GLU BBB O   1 ? 3  
ATOM 576   C CB  . GLU A 1 76  ? 29.183  58.306  42.584 1.000 117.081 0 76  GLU BBB CB  1 ? 3  
ATOM 577   C CG  . GLU A 1 76  ? 28.845  59.358  43.620 1.000 118.955 0 76  GLU BBB CG  1 ? 3  
ATOM 578   C CD  . GLU A 1 76  ? 27.640  60.188  43.219 1.000 125.821 0 76  GLU BBB CD  1 ? 3  
ATOM 579   O OE1 . GLU A 1 76  ? 27.511  60.506  42.016 1.000 125.883 0 76  GLU BBB OE1 1 ? 3  
ATOM 580   O OE2 . GLU A 1 76  ? 26.821  60.517  44.105 1.000 131.211 0 76  GLU BBB OE2 1 ? 3  
ATOM 581   N N   . ALA A 1 77  ? 29.054  55.318  41.327 1.000 126.774 0 77  ALA BBB N   1 ? 3  
ATOM 582   C CA  . ALA A 1 77  ? 29.295  54.406  40.213 1.000 131.798 0 77  ALA BBB CA  1 ? 3  
ATOM 583   C C   . ALA A 1 77  ? 27.994  53.828  39.665 1.000 140.553 0 77  ALA BBB C   1 ? 3  
ATOM 584   O O   . ALA A 1 77  ? 27.829  53.714  38.444 1.000 146.319 0 77  ALA BBB O   1 ? 3  
ATOM 585   C CB  . ALA A 1 77  ? 30.240  53.285  40.648 1.000 129.598 0 77  ALA BBB CB  1 ? 3  
ATOM 586   N N   . ALA A 1 78  ? 27.064  53.440  40.542 1.000 140.855 0 78  ALA BBB N   1 ? 3  
ATOM 587   C CA  . ALA A 1 78  ? 25.803  52.882  40.062 1.000 145.739 0 78  ALA BBB CA  1 ? 3  
ATOM 588   C C   . ALA A 1 78  ? 25.002  53.902  39.255 1.000 150.298 0 78  ALA BBB C   1 ? 3  
ATOM 589   O O   . ALA A 1 78  ? 24.449  53.565  38.201 1.000 166.417 0 78  ALA BBB O   1 ? 3  
ATOM 590   C CB  . ALA A 1 78  ? 24.981  52.359  41.240 1.000 152.410 0 78  ALA BBB CB  1 ? 3  
ATOM 591   N N   . GLU A 1 79  ? 24.934  55.155  39.716 1.000 146.535 0 79  GLU BBB N   1 ? 3  
ATOM 592   C CA  . GLU A 1 79  ? 24.230  56.176  38.939 1.000 149.969 0 79  GLU BBB CA  1 ? 3  
ATOM 593   C C   . GLU A 1 79  ? 24.925  56.455  37.615 1.000 148.967 0 79  GLU BBB C   1 ? 3  
ATOM 594   O O   . GLU A 1 79  ? 24.255  56.703  36.605 1.000 155.857 0 79  GLU BBB O   1 ? 3  
ATOM 595   C CB  . GLU A 1 79  ? 24.058  57.458  39.754 1.000 153.883 0 79  GLU BBB CB  1 ? 3  
ATOM 596   C CG  . GLU A 1 79  ? 22.732  57.537  40.503 1.000 168.521 0 79  GLU BBB CG  1 ? 3  
ATOM 597   C CD  . GLU A 1 79  ? 22.509  56.416  41.491 1.000 180.356 0 79  GLU BBB CD  1 ? 3  
ATOM 598   O OE1 . GLU A 1 79  ? 23.493  55.792  41.937 1.000 186.138 0 79  GLU BBB OE1 1 ? 3  
ATOM 599   O OE2 . GLU A 1 79  ? 21.330  56.163  41.821 1.000 183.530 0 79  GLU BBB OE2 1 ? 3  
ATOM 600   N N   . TRP A 1 80  ? 26.258  56.431  37.595 1.000 137.602 0 80  TRP BBB N   1 ? 3  
ATOM 601   C CA  . TRP A 1 80  ? 26.957  56.552  36.320 1.000 132.687 0 80  TRP BBB CA  1 ? 3  
ATOM 602   C C   . TRP A 1 80  ? 26.524  55.453  35.361 1.000 142.304 0 80  TRP BBB C   1 ? 3  
ATOM 603   O O   . TRP A 1 80  ? 26.194  55.725  34.201 1.000 153.871 0 80  TRP BBB O   1 ? 3  
ATOM 604   C CB  . TRP A 1 80  ? 28.473  56.520  36.528 1.000 124.798 0 80  TRP BBB CB  1 ? 3  
ATOM 605   C CG  . TRP A 1 80  ? 29.251  56.554  35.230 1.000 115.958 0 80  TRP BBB CG  1 ? 3  
ATOM 606   C CD1 . TRP A 1 80  ? 29.684  55.478  34.504 1.000 113.305 0 80  TRP BBB CD1 1 ? 3  
ATOM 607   C CD2 . TRP A 1 80  ? 29.629  57.717  34.483 1.000 109.127 0 80  TRP BBB CD2 1 ? 3  
ATOM 608   N NE1 . TRP A 1 80  ? 30.335  55.901  33.371 1.000 109.326 0 80  TRP BBB NE1 1 ? 3  
ATOM 609   C CE2 . TRP A 1 80  ? 30.312  57.270  33.332 1.000 106.677 0 80  TRP BBB CE2 1 ? 3  
ATOM 610   C CE3 . TRP A 1 80  ? 29.469  59.092  34.681 1.000 106.165 0 80  TRP BBB CE3 1 ? 3  
ATOM 611   C CZ2 . TRP A 1 80  ? 30.831  58.150  32.385 1.000 106.563 0 80  TRP BBB CZ2 1 ? 3  
ATOM 612   C CZ3 . TRP A 1 80  ? 29.986  59.964  33.738 1.000 104.830 0 80  TRP BBB CZ3 1 ? 3  
ATOM 613   C CH2 . TRP A 1 80  ? 30.659  59.490  32.605 1.000 107.156 0 80  TRP BBB CH2 1 ? 3  
ATOM 614   N N   . ASP A 1 81  ? 26.527  54.200  35.825 1.000 155.429 0 81  ASP BBB N   1 ? 3  
ATOM 615   C CA  . ASP A 1 81  ? 26.156  53.101  34.940 1.000 162.711 0 81  ASP BBB CA  1 ? 3  
ATOM 616   C C   . ASP A 1 81  ? 24.705  53.226  34.486 1.000 162.138 0 81  ASP BBB C   1 ? 3  
ATOM 617   O O   . ASP A 1 81  ? 24.378  52.933  33.331 1.000 168.862 0 81  ASP BBB O   1 ? 3  
ATOM 618   C CB  . ASP A 1 81  ? 26.352  51.762  35.662 1.000 167.640 0 81  ASP BBB CB  1 ? 3  
ATOM 619   C CG  . ASP A 1 81  ? 27.814  51.427  35.913 1.000 173.631 0 81  ASP BBB CG  1 ? 3  
ATOM 620   O OD1 . ASP A 1 81  ? 28.695  52.018  35.255 1.000 182.313 0 81  ASP BBB OD1 1 ? 3  
ATOM 621   O OD2 . ASP A 1 81  ? 28.079  50.585  36.802 1.000 175.713 0 81  ASP BBB OD2 1 ? 3  
ATOM 622   N N   . ARG A 1 82  ? 23.819  53.649  35.390 1.000 148.260 0 82  ARG BBB N   1 ? 3  
ATOM 623   C CA  . ARG A 1 82  ? 22.416  53.846  35.035 1.000 149.722 0 82  ARG BBB CA  1 ? 3  
ATOM 624   C C   . ARG A 1 82  ? 22.209  54.969  34.018 1.000 147.646 0 82  ARG BBB C   1 ? 3  
ATOM 625   O O   . ARG A 1 82  ? 21.389  54.834  33.102 1.000 152.254 0 82  ARG BBB O   1 ? 3  
ATOM 626   C CB  . ARG A 1 82  ? 21.598  54.090  36.303 1.000 156.616 0 82  ARG BBB CB  1 ? 3  
ATOM 627   C CG  . ARG A 1 82  ? 20.267  54.773  36.082 1.000 167.248 0 82  ARG BBB CG  1 ? 3  
ATOM 628   C CD  . ARG A 1 82  ? 19.585  55.059  37.406 1.000 171.157 0 82  ARG BBB CD  1 ? 3  
ATOM 629   N NE  . ARG A 1 82  ? 18.493  56.011  37.252 1.000 181.293 0 82  ARG BBB NE  1 ? 3  
ATOM 630   C CZ  . ARG A 1 82  ? 18.609  57.318  37.443 1.000 178.219 0 82  ARG BBB CZ  1 ? 3  
ATOM 631   N NH1 . ARG A 1 82  ? 19.761  57.865  37.795 1.000 169.772 0 82  ARG BBB NH1 1 ? 3  
ATOM 632   N NH2 . ARG A 1 82  ? 17.543  58.095  37.275 1.000 180.018 0 82  ARG BBB NH2 1 ? 3  
ATOM 633   N N   . LEU A 1 83  ? 22.950  56.076  34.141 1.000 142.870 0 83  LEU BBB N   1 ? 3  
ATOM 634   C CA  . LEU A 1 83  ? 22.777  57.186  33.207 1.000 142.657 0 83  LEU BBB CA  1 ? 3  
ATOM 635   C C   . LEU A 1 83  ? 23.608  57.049  31.941 1.000 140.162 0 83  LEU BBB C   1 ? 3  
ATOM 636   O O   . LEU A 1 83  ? 23.300  57.700  30.936 1.000 146.460 0 83  LEU BBB O   1 ? 3  
ATOM 637   C CB  A LEU A 1 83  ? 23.087  58.505  33.916 1.000 141.996 0 83  LEU BBB CB  1 ? 3  
ATOM 638   C CG  A LEU A 1 83  ? 22.100  58.721  35.072 1.000 159.740 0 83  LEU BBB CG  1 ? 3  
ATOM 639   C CD1 A LEU A 1 83  ? 22.518  59.869  35.977 1.000 163.516 0 83  LEU BBB CD1 1 ? 3  
ATOM 640   C CD2 A LEU A 1 83  ? 20.677  58.926  34.553 1.000 169.906 0 83  LEU BBB CD2 1 ? 3  
ATOM 641   N N   . HIS A 1 84  ? 24.652  56.232  31.975 1.000 136.493 0 84  HIS BBB N   1 ? 3  
ATOM 642   C CA  . HIS A 1 84  ? 25.550  56.016  30.841 1.000 131.125 0 84  HIS BBB CA  1 ? 3  
ATOM 643   C C   . HIS A 1 84  ? 25.826  54.523  30.848 1.000 135.242 0 84  HIS BBB C   1 ? 3  
ATOM 644   O O   . HIS A 1 84  ? 26.917  54.074  31.220 1.000 140.552 0 84  HIS BBB O   1 ? 3  
ATOM 645   C CB  . HIS A 1 84  ? 26.833  56.846  30.946 1.000 126.106 0 84  HIS BBB CB  1 ? 3  
ATOM 646   C CG  . HIS A 1 84  ? 26.604  58.317  31.129 1.000 131.019 0 84  HIS BBB CG  1 ? 3  
ATOM 647   N ND1 . HIS A 1 84  ? 26.544  58.915  32.370 1.000 136.638 0 84  HIS BBB ND1 1 ? 3  
ATOM 648   C CD2 . HIS A 1 84  ? 26.447  59.313  30.225 1.000 134.686 0 84  HIS BBB CD2 1 ? 3  
ATOM 649   C CE1 . HIS A 1 84  ? 26.346  60.213  32.223 1.000 136.151 0 84  HIS BBB CE1 1 ? 3  
ATOM 650   N NE2 . HIS A 1 84  ? 26.285  60.481  30.917 1.000 139.670 0 84  HIS BBB NE2 1 ? 3  
ATOM 651   N N   . PRO A 1 85  ? 24.854  53.716  30.428 1.000 137.216 0 85  PRO BBB N   1 ? 3  
ATOM 652   C CA  . PRO A 1 85  ? 25.082  52.272  30.377 1.000 136.482 0 85  PRO BBB CA  1 ? 3  
ATOM 653   C C   . PRO A 1 85  ? 26.057  51.927  29.274 1.000 135.687 0 85  PRO BBB C   1 ? 3  
ATOM 654   O O   . PRO A 1 85  ? 26.246  52.677  28.314 1.000 137.071 0 85  PRO BBB O   1 ? 3  
ATOM 655   C CB  . PRO A 1 85  ? 23.696  51.695  30.086 1.000 137.301 0 85  PRO BBB CB  1 ? 3  
ATOM 656   C CG  . PRO A 1 85  ? 22.727  52.823  30.273 1.000 142.728 0 85  PRO BBB CG  1 ? 3  
ATOM 657   C CD  . PRO A 1 85  ? 23.496  54.070  29.988 1.000 142.760 0 85  PRO BBB CD  1 ? 3  
ATOM 658   N N   . VAL A 1 86  ? 26.668  50.763  29.414 1.000 137.584 0 86  VAL BBB N   1 ? 3  
ATOM 659   C CA  . VAL A 1 86  ? 27.673  50.329  28.459 1.000 143.235 0 86  VAL BBB CA  1 ? 3  
ATOM 660   C C   . VAL A 1 86  ? 27.026  49.586  27.303 1.000 149.230 0 86  VAL BBB C   1 ? 3  
ATOM 661   O O   . VAL A 1 86  ? 26.246  48.647  27.506 1.000 154.006 0 86  VAL BBB O   1 ? 3  
ATOM 662   C CB  . VAL A 1 86  ? 28.720  49.446  29.153 1.000 143.402 0 86  VAL BBB CB  1 ? 3  
ATOM 663   C CG1 . VAL A 1 86  ? 29.699  48.888  28.140 1.000 148.482 0 86  VAL BBB CG1 1 ? 3  
ATOM 664   C CG2 . VAL A 1 86  ? 29.431  50.239  30.234 1.000 144.354 0 86  VAL BBB CG2 1 ? 3  
ATOM 665   N N   . HIS A 1 87  ? 27.342  50.026  26.089 1.000 153.491 0 87  HIS BBB N   1 ? 3  
ATOM 666   C CA  . HIS A 1 87  ? 26.834  49.417  24.868 1.000 152.889 0 87  HIS BBB CA  1 ? 3  
ATOM 667   C C   . HIS A 1 87  ? 27.640  48.148  24.597 1.000 158.855 0 87  HIS BBB C   1 ? 3  
ATOM 668   O O   . HIS A 1 87  ? 28.871  48.204  24.505 1.000 168.270 0 87  HIS BBB O   1 ? 3  
ATOM 669   C CB  . HIS A 1 87  ? 26.902  50.418  23.717 1.000 144.095 0 87  HIS BBB CB  1 ? 3  
ATOM 670   C CG  . HIS A 1 87  ? 26.040  51.627  23.929 1.000 141.601 0 87  HIS BBB CG  1 ? 3  
ATOM 671   N ND1 . HIS A 1 87  ? 24.689  51.634  23.653 1.000 148.524 0 87  HIS BBB ND1 1 ? 3  
ATOM 672   C CD2 . HIS A 1 87  ? 26.329  52.858  24.414 1.000 148.590 0 87  HIS BBB CD2 1 ? 3  
ATOM 673   C CE1 . HIS A 1 87  ? 24.187  52.821  23.943 1.000 155.677 0 87  HIS BBB CE1 1 ? 3  
ATOM 674   N NE2 . HIS A 1 87  ? 25.161  53.582  24.410 1.000 158.285 0 87  HIS BBB NE2 1 ? 3  
ATOM 675   N N   . ALA A 1 88  ? 26.970  47.009  24.475 1.000 161.044 0 88  ALA BBB N   1 ? 3  
ATOM 676   C CA  . ALA A 1 88  ? 27.685  45.746  24.365 1.000 167.161 0 88  ALA BBB CA  1 ? 3  
ATOM 677   C C   . ALA A 1 88  ? 27.947  45.402  22.906 1.000 172.206 0 88  ALA BBB C   1 ? 3  
ATOM 678   O O   . ALA A 1 88  ? 27.153  45.723  22.018 1.000 182.724 0 88  ALA BBB O   1 ? 3  
ATOM 679   C CB  . ALA A 1 88  ? 26.905  44.615  25.034 1.000 175.993 0 88  ALA BBB CB  1 ? 3  
ATOM 680   N N   . GLY A 1 89  ? 29.088  44.765  22.661 1.000 176.235 0 89  GLY BBB N   1 ? 3  
ATOM 681   C CA  . GLY A 1 89  ? 29.433  44.325  21.332 1.000 179.478 0 89  GLY BBB CA  1 ? 3  
ATOM 682   C C   . GLY A 1 89  ? 30.893  43.950  21.206 1.000 180.294 0 89  GLY BBB C   1 ? 3  
ATOM 683   O O   . GLY A 1 89  ? 31.702  44.194  22.107 1.000 185.653 0 89  GLY BBB O   1 ? 3  
ATOM 684   N N   . PRO A 1 90  ? 31.258  43.335  20.083 1.000 177.644 0 90  PRO BBB N   1 ? 3  
ATOM 685   C CA  . PRO A 1 90  ? 32.674  43.062  19.827 1.000 176.328 0 90  PRO BBB CA  1 ? 3  
ATOM 686   C C   . PRO A 1 90  ? 33.424  44.359  19.599 1.000 168.031 0 90  PRO BBB C   1 ? 3  
ATOM 687   O O   . PRO A 1 90  ? 32.915  45.286  18.964 1.000 163.761 0 90  PRO BBB O   1 ? 3  
ATOM 688   C CB  . PRO A 1 90  ? 32.656  42.206  18.555 1.000 180.599 0 90  PRO BBB CB  1 ? 3  
ATOM 689   C CG  . PRO A 1 90  ? 31.222  41.844  18.327 1.000 186.280 0 90  PRO BBB CG  1 ? 3  
ATOM 690   C CD  . PRO A 1 90  ? 30.415  42.930  18.951 1.000 179.444 0 90  PRO BBB CD  1 ? 3  
ATOM 691   N N   . ILE A 1 91  ? 34.644  44.423  20.110 1.000 167.179 0 91  ILE BBB N   1 ? 3  
ATOM 692   C CA  . ILE A 1 91  ? 35.429  45.639  19.986 1.000 165.270 0 91  ILE BBB CA  1 ? 3  
ATOM 693   C C   . ILE A 1 91  ? 36.148  45.602  18.646 1.000 168.234 0 91  ILE BBB C   1 ? 3  
ATOM 694   O O   . ILE A 1 91  ? 36.871  44.652  18.326 1.000 171.271 0 91  ILE BBB O   1 ? 3  
ATOM 695   C CB  . ILE A 1 91  ? 36.408  45.800  21.158 1.000 170.047 0 91  ILE BBB CB  1 ? 3  
ATOM 696   C CG1 . ILE A 1 91  ? 35.636  45.910  22.477 1.000 169.388 0 91  ILE BBB CG1 1 ? 3  
ATOM 697   C CG2 . ILE A 1 91  ? 37.255  47.042  20.957 1.000 164.980 0 91  ILE BBB CG2 1 ? 3  
ATOM 698   C CD1 . ILE A 1 91  ? 35.471  44.607  23.226 1.000 169.651 0 91  ILE BBB CD1 1 ? 3  
ATOM 699   N N   . ALA A 1 92  ? 35.953  46.659  17.893 1.000 179.537 0 92  ALA BBB N   1 ? 3  
ATOM 700   C CA  . ALA A 1 92  ? 36.598  46.887  16.611 1.000 183.455 0 92  ALA BBB CA  1 ? 3  
ATOM 701   C C   . ALA A 1 92  ? 38.088  47.188  16.734 1.000 183.249 0 92  ALA BBB C   1 ? 3  
ATOM 702   O O   . ALA A 1 92  ? 38.489  47.955  17.618 1.000 187.622 0 92  ALA BBB O   1 ? 3  
ATOM 703   C CB  . ALA A 1 92  ? 35.897  48.014  15.865 1.000 184.905 0 92  ALA BBB CB  1 ? 3  
ATOM 704   N N   . PRO A 1 93  ? 38.928  46.569  15.908 1.000 176.376 0 93  PRO BBB N   1 ? 3  
ATOM 705   C CA  . PRO A 1 93  ? 40.375  46.817  15.962 1.000 176.650 0 93  PRO BBB CA  1 ? 3  
ATOM 706   C C   . PRO A 1 93  ? 40.628  48.319  15.953 1.000 178.342 0 93  PRO BBB C   1 ? 3  
ATOM 707   O O   . PRO A 1 93  ? 40.185  49.053  15.065 1.000 179.542 0 93  PRO BBB O   1 ? 3  
ATOM 708   C CB  . PRO A 1 93  ? 40.915  46.108  14.715 1.000 183.429 0 93  PRO BBB CB  1 ? 3  
ATOM 709   C CG  . PRO A 1 93  ? 39.723  45.823  13.852 1.000 187.619 0 93  PRO BBB CG  1 ? 3  
ATOM 710   C CD  . PRO A 1 93  ? 38.555  45.695  14.783 1.000 180.190 0 93  PRO BBB CD  1 ? 3  
ATOM 711   N N   . GLY A 1 94  ? 41.359  48.755  16.975 1.000 176.891 0 94  GLY BBB N   1 ? 3  
ATOM 712   C CA  . GLY A 1 94  ? 41.776  50.110  17.263 1.000 174.738 0 94  GLY BBB CA  1 ? 3  
ATOM 713   C C   . GLY A 1 94  ? 40.715  50.994  17.881 1.000 169.947 0 94  GLY BBB C   1 ? 3  
ATOM 714   O O   . GLY A 1 94  ? 40.870  52.222  17.890 1.000 172.088 0 94  GLY BBB O   1 ? 3  
ATOM 715   N N   . GLN A 1 95  ? 39.625  50.401  18.365 1.000 164.785 0 95  GLN BBB N   1 ? 3  
ATOM 716   C CA  . GLN A 1 95  ? 38.540  51.099  19.035 1.000 154.919 0 95  GLN BBB CA  1 ? 3  
ATOM 717   C C   . GLN A 1 95  ? 38.726  50.722  20.494 1.000 147.125 0 95  GLN BBB C   1 ? 3  
ATOM 718   O O   . GLN A 1 95  ? 39.270  49.660  20.801 1.000 146.812 0 95  GLN BBB O   1 ? 3  
ATOM 719   C CB  . GLN A 1 95  ? 37.128  50.720  18.549 1.000 162.572 0 95  GLN BBB CB  1 ? 3  
ATOM 720   C CG  . GLN A 1 95  ? 36.820  51.013  17.104 1.000 175.934 0 95  GLN BBB CG  1 ? 3  
ATOM 721   C CD  . GLN A 1 95  ? 37.017  52.487  16.782 1.000 171.861 0 95  GLN BBB CD  1 ? 3  
ATOM 722   O OE1 . GLN A 1 95  ? 36.363  53.351  17.378 1.000 169.164 0 95  GLN BBB OE1 1 ? 3  
ATOM 723   N NE2 . GLN A 1 95  ? 37.911  52.785  15.849 1.000 173.942 0 95  GLN BBB NE2 1 ? 3  
ATOM 724   N N   . MET A 1 96  ? 38.294  51.582  21.389 1.000 140.419 0 96  MET BBB N   1 ? 3  
ATOM 725   C CA  . MET A 1 96  ? 38.412  51.285  22.805 1.000 135.138 0 96  MET BBB CA  1 ? 3  
ATOM 726   C C   . MET A 1 96  ? 37.028  50.963  23.364 1.000 131.131 0 96  MET BBB C   1 ? 3  
ATOM 727   O O   . MET A 1 96  ? 36.008  51.341  22.786 1.000 135.258 0 96  MET BBB O   1 ? 3  
ATOM 728   C CB  . MET A 1 96  ? 39.146  52.445  23.493 1.000 129.626 0 96  MET BBB CB  1 ? 3  
ATOM 729   C CG  . MET A 1 96  ? 39.419  52.291  24.949 1.000 131.922 0 96  MET BBB CG  1 ? 3  
ATOM 730   S SD  . MET A 1 96  ? 40.305  53.757  25.504 1.000 143.570 0 96  MET BBB SD  1 ? 3  
ATOM 731   C CE  . MET A 1 96  ? 39.897  54.950  24.219 1.000 123.923 0 96  MET BBB CE  1 ? 3  
ATOM 732   N N   . ARG A 1 97  ? 36.987  50.264  24.498 1.000 120.575 0 97  ARG BBB N   1 ? 3  
ATOM 733   C CA  . ARG A 1 97  ? 35.688  49.970  25.085 1.000 116.968 0 97  ARG BBB CA  1 ? 3  
ATOM 734   C C   . ARG A 1 97  ? 35.170  51.147  25.904 1.000 116.892 0 97  ARG BBB C   1 ? 3  
ATOM 735   O O   . ARG A 1 97  ? 35.883  52.112  26.196 1.000 112.984 0 97  ARG BBB O   1 ? 3  
ATOM 736   C CB  . ARG A 1 97  ? 35.732  48.716  25.959 1.000 123.284 0 97  ARG BBB CB  1 ? 3  
ATOM 737   C CG  . ARG A 1 97  ? 36.503  48.844  27.266 1.000 128.264 0 97  ARG BBB CG  1 ? 3  
ATOM 738   C CD  . ARG A 1 97  ? 36.772  47.467  27.870 1.000 133.171 0 97  ARG BBB CD  1 ? 3  
ATOM 739   N NE  . ARG A 1 97  ? 37.521  47.533  29.121 1.000 131.645 0 97  ARG BBB NE  1 ? 3  
ATOM 740   C CZ  . ARG A 1 97  ? 36.982  47.838  30.295 1.000 128.898 0 97  ARG BBB CZ  1 ? 3  
ATOM 741   N NH1 . ARG A 1 97  ? 35.690  48.108  30.415 1.000 129.640 0 97  ARG BBB NH1 1 ? 3  
ATOM 742   N NH2 . ARG A 1 97  ? 37.756  47.878  31.376 1.000 125.076 0 97  ARG BBB NH2 1 ? 3  
ATOM 743   N N   . GLU A 1 98  ? 33.897  51.061  26.270 1.000 127.562 0 98  GLU BBB N   1 ? 3  
ATOM 744   C CA  . GLU A 1 98  ? 33.217  52.096  27.037 1.000 127.342 0 98  GLU BBB CA  1 ? 3  
ATOM 745   C C   . GLU A 1 98  ? 33.441  51.876  28.525 1.000 127.395 0 98  GLU BBB C   1 ? 3  
ATOM 746   O O   . GLU A 1 98  ? 33.333  50.739  29.002 1.000 131.045 0 98  GLU BBB O   1 ? 3  
ATOM 747   C CB  . GLU A 1 98  ? 31.726  52.081  26.743 1.000 134.322 0 98  GLU BBB CB  1 ? 3  
ATOM 748   C CG  . GLU A 1 98  ? 31.382  52.179  25.271 1.000 139.745 0 98  GLU BBB CG  1 ? 3  
ATOM 749   C CD  . GLU A 1 98  ? 29.890  52.216  25.029 1.000 149.472 0 98  GLU BBB CD  1 ? 3  
ATOM 750   O OE1 . GLU A 1 98  ? 29.126  52.112  26.009 1.000 149.635 0 98  GLU BBB OE1 1 ? 3  
ATOM 751   O OE2 . GLU A 1 98  ? 29.481  52.355  23.858 1.000 159.840 0 98  GLU BBB OE2 1 ? 3  
ATOM 752   N N   . PRO A 1 99  ? 33.780  52.930  29.272 1.000 122.113 0 99  PRO BBB N   1 ? 3  
ATOM 753   C CA  . PRO A 1 99  ? 34.061  52.777  30.707 1.000 117.474 0 99  PRO BBB CA  1 ? 3  
ATOM 754   C C   . PRO A 1 99  ? 32.781  52.602  31.513 1.000 120.789 0 99  PRO BBB C   1 ? 3  
ATOM 755   O O   . PRO A 1 99  ? 31.796  53.318  31.313 1.000 119.760 0 99  PRO BBB O   1 ? 3  
ATOM 756   C CB  . PRO A 1 99  ? 34.776  54.084  31.069 1.000 110.197 0 99  PRO BBB CB  1 ? 3  
ATOM 757   C CG  . PRO A 1 99  ? 34.281  55.071  30.065 1.000 108.263 0 99  PRO BBB CG  1 ? 3  
ATOM 758   C CD  . PRO A 1 99  ? 33.998  54.309  28.800 1.000 118.927 0 99  PRO BBB CD  1 ? 3  
ATOM 759   N N   . ARG A 1 100 ? 32.802  51.640  32.428 1.000 121.474 0 100 ARG BBB N   1 ? 3  
ATOM 760   C CA  . ARG A 1 100 ? 31.738  51.486  33.401 1.000 121.996 0 100 ARG BBB CA  1 ? 3  
ATOM 761   C C   . ARG A 1 100 ? 32.062  52.296  34.648 1.000 120.942 0 100 ARG BBB C   1 ? 3  
ATOM 762   O O   . ARG A 1 100 ? 33.134  52.892  34.773 1.000 121.130 0 100 ARG BBB O   1 ? 3  
ATOM 763   C CB  . ARG A 1 100 ? 31.598  50.017  33.799 1.000 125.685 0 100 ARG BBB CB  1 ? 3  
ATOM 764   C CG  . ARG A 1 100 ? 31.605  49.033  32.651 1.000 133.473 0 100 ARG BBB CG  1 ? 3  
ATOM 765   C CD  . ARG A 1 100 ? 32.175  47.700  33.105 1.000 140.208 0 100 ARG BBB CD  1 ? 3  
ATOM 766   N NE  . ARG A 1 100 ? 31.807  46.600  32.223 1.000 155.433 0 100 ARG BBB NE  1 ? 3  
ATOM 767   C CZ  . ARG A 1 100 ? 30.957  45.630  32.546 1.000 170.026 0 100 ARG BBB CZ  1 ? 3  
ATOM 768   N NH1 . ARG A 1 100 ? 30.374  45.598  33.736 1.000 165.830 0 100 ARG BBB NH1 1 ? 3  
ATOM 769   N NH2 . ARG A 1 100 ? 30.694  44.675  31.665 1.000 182.949 0 100 ARG BBB NH2 1 ? 3  
ATOM 770   N N   . GLY A 1 101 ? 31.094  52.347  35.564 1.000 123.124 0 101 GLY BBB N   1 ? 3  
ATOM 771   C CA  . GLY A 1 101 ? 31.324  53.031  36.825 1.000 117.251 0 101 GLY BBB CA  1 ? 3  
ATOM 772   C C   . GLY A 1 101 ? 32.588  52.523  37.486 1.000 111.342 0 101 GLY BBB C   1 ? 3  
ATOM 773   O O   . GLY A 1 101 ? 33.437  53.298  37.935 1.000 110.285 0 101 GLY BBB O   1 ? 3  
ATOM 774   N N   . SER A 1 102 ? 32.731  51.195  37.528 1.000 106.153 0 102 SER BBB N   1 ? 3  
ATOM 775   C CA  . SER A 1 102 ? 33.881  50.520  38.102 1.000 106.358 0 102 SER BBB CA  1 ? 3  
ATOM 776   C C   . SER A 1 102 ? 35.161  50.777  37.319 1.000 105.995 0 102 SER BBB C   1 ? 3  
ATOM 777   O O   . SER A 1 102 ? 36.250  50.674  37.893 1.000 109.545 0 102 SER BBB O   1 ? 3  
ATOM 778   C CB  . SER A 1 102 ? 33.591  49.025  38.177 1.000 111.459 0 102 SER BBB CB  1 ? 3  
ATOM 779   O OG  . SER A 1 102 ? 32.365  48.813  38.847 1.000 137.757 0 102 SER BBB OG  1 ? 3  
ATOM 780   N N   . ASP A 1 103 ? 35.072  51.104  36.020 1.000 111.289 0 103 ASP BBB N   1 ? 3  
ATOM 781   C CA  . ASP A 1 103 ? 36.277  51.476  35.275 1.000 107.159 0 103 ASP BBB CA  1 ? 3  
ATOM 782   C C   . ASP A 1 103 ? 36.748  52.866  35.680 1.000 102.411 0 103 ASP BBB C   1 ? 3  
ATOM 783   O O   . ASP A 1 103 ? 37.953  53.098  35.799 1.000 103.674 0 103 ASP BBB O   1 ? 3  
ATOM 784   C CB  . ASP A 1 103 ? 36.031  51.458  33.756 1.000 109.519 0 103 ASP BBB CB  1 ? 3  
ATOM 785   C CG  . ASP A 1 103 ? 35.732  50.070  33.209 1.000 113.514 0 103 ASP BBB CG  1 ? 3  
ATOM 786   O OD1 . ASP A 1 103 ? 36.337  49.087  33.677 1.000 111.950 0 103 ASP BBB OD1 1 ? 3  
ATOM 787   O OD2 . ASP A 1 103 ? 34.794  49.956  32.385 1.000 119.961 0 103 ASP BBB OD2 1 ? 3  
ATOM 788   N N   . ILE A 1 104 ? 35.820  53.789  35.907 1.000 95.626  0 104 ILE BBB N   1 ? 3  
ATOM 789   C CA  . ILE A 1 104 ? 36.188  55.132  36.356 1.000 93.216  0 104 ILE BBB CA  1 ? 3  
ATOM 790   C C   . ILE A 1 104 ? 36.847  55.101  37.734 1.000 91.499  0 104 ILE BBB C   1 ? 3  
ATOM 791   O O   . ILE A 1 104 ? 37.829  55.813  37.986 1.000 91.790  0 104 ILE BBB O   1 ? 3  
ATOM 792   C CB  . ILE A 1 104 ? 34.945  56.040  36.337 1.000 95.320  0 104 ILE BBB CB  1 ? 3  
ATOM 793   C CG1 . ILE A 1 104 ? 34.523  56.288  34.886 1.000 94.822  0 104 ILE BBB CG1 1 ? 3  
ATOM 794   C CG2 . ILE A 1 104 ? 35.202  57.347  37.087 1.000 93.490  0 104 ILE BBB CG2 1 ? 3  
ATOM 795   C CD1 . ILE A 1 104 ? 33.751  57.556  34.674 1.000 99.234  0 104 ILE BBB CD1 1 ? 3  
ATOM 796   N N   . ALA A 1 105 ? 36.354  54.251  38.629 1.000 91.857  0 105 ALA BBB N   1 ? 3  
ATOM 797   C CA  . ALA A 1 105 ? 36.962  54.149  39.948 1.000 91.407  0 105 ALA BBB CA  1 ? 3  
ATOM 798   C C   . ALA A 1 105 ? 38.274  53.377  39.961 1.000 91.642  0 105 ALA BBB C   1 ? 3  
ATOM 799   O O   . ALA A 1 105 ? 38.855  53.210  41.039 1.000 92.643  0 105 ALA BBB O   1 ? 3  
ATOM 800   C CB  . ALA A 1 105 ? 35.984  53.499  40.926 1.000 95.969  0 105 ALA BBB CB  1 ? 3  
ATOM 801   N N   . GLY A 1 106 ? 38.734  52.869  38.822 1.000 92.253  0 106 GLY BBB N   1 ? 3  
ATOM 802   C CA  . GLY A 1 106 ? 40.020  52.205  38.769 1.000 93.598  0 106 GLY BBB CA  1 ? 3  
ATOM 803   C C   . GLY A 1 106 ? 40.063  50.817  39.356 1.000 97.054  0 106 GLY BBB C   1 ? 3  
ATOM 804   O O   . GLY A 1 106 ? 41.159  50.305  39.604 1.000 108.489 0 106 GLY BBB O   1 ? 3  
ATOM 805   N N   . THR A 1 107 ? 38.913  50.199  39.599 1.000 99.202  0 107 THR BBB N   1 ? 3  
ATOM 806   C CA  . THR A 1 107 ? 38.850  48.889  40.232 1.000 103.051 0 107 THR BBB CA  1 ? 3  
ATOM 807   C C   . THR A 1 107 ? 38.946  47.759  39.211 1.000 105.039 0 107 THR BBB C   1 ? 3  
ATOM 808   O O   . THR A 1 107 ? 39.583  46.734  39.483 1.000 106.405 0 107 THR BBB O   1 ? 3  
ATOM 809   C CB  . THR A 1 107 ? 37.568  48.763  41.056 1.000 108.509 0 107 THR BBB CB  1 ? 3  
ATOM 810   O OG1 . THR A 1 107 ? 36.435  48.975  40.206 1.000 130.243 0 107 THR BBB OG1 1 ? 3  
ATOM 811   C CG2 . THR A 1 107 ? 37.551  49.796  42.181 1.000 104.465 0 107 THR BBB CG2 1 ? 3  
ATOM 812   N N   . THR A 1 108 ? 38.321  47.930  38.040 1.000 105.327 0 108 THR BBB N   1 ? 3  
ATOM 813   C CA  . THR A 1 108 ? 38.304  46.915  36.990 1.000 110.666 0 108 THR BBB CA  1 ? 3  
ATOM 814   C C   . THR A 1 108 ? 38.982  47.375  35.705 1.000 111.131 0 108 THR BBB C   1 ? 3  
ATOM 815   O O   . THR A 1 108 ? 38.899  46.674  34.689 1.000 118.581 0 108 THR BBB O   1 ? 3  
ATOM 816   C CB  . THR A 1 108 ? 36.869  46.486  36.662 1.000 115.086 0 108 THR BBB CB  1 ? 3  
ATOM 817   O OG1 . THR A 1 108 ? 36.872  45.694  35.467 1.000 136.134 0 108 THR BBB OG1 1 ? 3  
ATOM 818   C CG2 . THR A 1 108 ? 36.021  47.688  36.402 1.000 108.957 0 108 THR BBB CG2 1 ? 3  
ATOM 819   N N   . SER A 1 109 ? 39.661  48.516  35.718 1.000 103.112 0 109 SER BBB N   1 ? 3  
ATOM 820   C CA  . SER A 1 109 ? 40.335  49.022  34.534 1.000 100.784 0 109 SER BBB CA  1 ? 3  
ATOM 821   C C   . SER A 1 109 ? 41.840  49.000  34.747 1.000 100.647 0 109 SER BBB C   1 ? 3  
ATOM 822   O O   . SER A 1 109 ? 42.328  49.127  35.874 1.000 103.378 0 109 SER BBB O   1 ? 3  
ATOM 823   C CB  . SER A 1 109 ? 39.899  50.453  34.210 1.000 99.022  0 109 SER BBB CB  1 ? 3  
ATOM 824   O OG  . SER A 1 109 ? 40.181  51.317  35.298 1.000 95.296  0 109 SER BBB OG  1 ? 3  
ATOM 825   N N   . THR A 1 110 ? 42.573  48.858  33.649 1.000 106.324 0 110 THR BBB N   1 ? 3  
ATOM 826   C CA  . THR A 1 110 ? 44.024  48.901  33.693 1.000 101.624 0 110 THR BBB CA  1 ? 3  
ATOM 827   C C   . THR A 1 110 ? 44.492  50.326  33.452 1.000 97.471  0 110 THR BBB C   1 ? 3  
ATOM 828   O O   . THR A 1 110 ? 43.758  51.165  32.929 1.000 98.227  0 110 THR BBB O   1 ? 3  
ATOM 829   C CB  . THR A 1 110 ? 44.636  47.978  32.644 1.000 107.602 0 110 THR BBB CB  1 ? 3  
ATOM 830   O OG1 . THR A 1 110 ? 44.337  48.482  31.335 1.000 107.503 0 110 THR BBB OG1 1 ? 3  
ATOM 831   C CG2 . THR A 1 110 ? 44.064  46.578  32.782 1.000 115.997 0 110 THR BBB CG2 1 ? 3  
ATOM 832   N N   . LEU A 1 111 ? 45.740  50.588  33.834 1.000 94.719  0 111 LEU BBB N   1 ? 3  
ATOM 833   C CA  . LEU A 1 111 ? 46.313  51.899  33.566 1.000 92.210  0 111 LEU BBB CA  1 ? 3  
ATOM 834   C C   . LEU A 1 111 ? 46.234  52.231  32.078 1.000 96.026  0 111 LEU BBB C   1 ? 3  
ATOM 835   O O   . LEU A 1 111 ? 45.897  53.362  31.708 1.000 96.544  0 111 LEU BBB O   1 ? 3  
ATOM 836   C CB  . LEU A 1 111 ? 47.746  51.970  34.096 1.000 91.454  0 111 LEU BBB CB  1 ? 3  
ATOM 837   C CG  . LEU A 1 111 ? 48.497  53.266  33.792 1.000 89.611  0 111 LEU BBB CG  1 ? 3  
ATOM 838   C CD1 . LEU A 1 111 ? 47.727  54.454  34.340 1.000 87.076  0 111 LEU BBB CD1 1 ? 3  
ATOM 839   C CD2 . LEU A 1 111 ? 49.892  53.236  34.392 1.000 98.158  0 111 LEU BBB CD2 1 ? 3  
ATOM 840   N N   . GLN A 1 112 ? 46.507  51.249  31.210 1.000 99.154  0 112 GLN BBB N   1 ? 3  
ATOM 841   C CA  . GLN A 1 112 ? 46.503  51.516  29.777 1.000 102.962 0 112 GLN BBB CA  1 ? 3  
ATOM 842   C C   . GLN A 1 112 ? 45.120  51.915  29.297 1.000 103.894 0 112 GLN BBB C   1 ? 3  
ATOM 843   O O   . GLN A 1 112 ? 44.976  52.832  28.476 1.000 106.271 0 112 GLN BBB O   1 ? 3  
ATOM 844   C CB  . GLN A 1 112 ? 46.983  50.294  28.996 1.000 113.212 0 112 GLN BBB CB  1 ? 3  
ATOM 845   C CG  . GLN A 1 112 ? 47.379  50.626  27.557 1.000 134.508 0 112 GLN BBB CG  1 ? 3  
ATOM 846   C CD  . GLN A 1 112 ? 47.215  49.451  26.622 1.000 148.625 0 112 GLN BBB CD  1 ? 3  
ATOM 847   O OE1 . GLN A 1 112 ? 46.169  48.803  26.612 1.000 148.761 0 112 GLN BBB OE1 1 ? 3  
ATOM 848   N NE2 . GLN A 1 112 ? 48.265  49.136  25.859 1.000 157.419 0 112 GLN BBB NE2 1 ? 3  
ATOM 849   N N   . GLU A 1 113 ? 44.084  51.242  29.805 1.000 105.880 0 113 GLU BBB N   1 ? 3  
ATOM 850   C CA  . GLU A 1 113 ? 42.714  51.635  29.487 1.000 102.745 0 113 GLU BBB CA  1 ? 3  
ATOM 851   C C   . GLU A 1 113 ? 42.415  53.039  29.990 1.000 101.303 0 113 GLU BBB C   1 ? 3  
ATOM 852   O O   . GLU A 1 113 ? 41.812  53.847  29.273 1.000 99.386  0 113 GLU BBB O   1 ? 3  
ATOM 853   C CB  . GLU A 1 113 ? 41.737  50.622  30.088 1.000 101.359 0 113 GLU BBB CB  1 ? 3  
ATOM 854   C CG  . GLU A 1 113 ? 41.791  49.258  29.402 1.000 104.970 0 113 GLU BBB CG  1 ? 3  
ATOM 855   C CD  . GLU A 1 113 ? 40.936  48.216  30.095 1.000 110.624 0 113 GLU BBB CD  1 ? 3  
ATOM 856   O OE1 . GLU A 1 113 ? 40.899  48.209  31.341 1.000 111.247 0 113 GLU BBB OE1 1 ? 3  
ATOM 857   O OE2 . GLU A 1 113 ? 40.277  47.420  29.391 1.000 123.451 0 113 GLU BBB OE2 1 ? 3  
ATOM 858   N N   . GLN A 1 114 ? 42.856  53.348  31.213 1.000 96.744  0 114 GLN BBB N   1 ? 3  
ATOM 859   C CA  . GLN A 1 114 ? 42.660  54.676  31.786 1.000 91.793  0 114 GLN BBB CA  1 ? 3  
ATOM 860   C C   . GLN A 1 114 ? 43.343  55.752  30.949 1.000 94.090  0 114 GLN BBB C   1 ? 3  
ATOM 861   O O   . GLN A 1 114 ? 42.757  56.803  30.666 1.000 99.069  0 114 GLN BBB O   1 ? 3  
ATOM 862   C CB  . GLN A 1 114 ? 43.194  54.695  33.222 1.000 90.074  0 114 GLN BBB CB  1 ? 3  
ATOM 863   C CG  . GLN A 1 114 ? 42.378  53.842  34.195 1.000 94.451  0 114 GLN BBB CG  1 ? 3  
ATOM 864   C CD  . GLN A 1 114 ? 43.064  53.589  35.541 1.000 90.916  0 114 GLN BBB CD  1 ? 3  
ATOM 865   O OE1 . GLN A 1 114 ? 43.912  54.366  35.987 1.000 93.273  0 114 GLN BBB OE1 1 ? 3  
ATOM 866   N NE2 . GLN A 1 114 ? 42.707  52.479  36.181 1.000 91.502  0 114 GLN BBB NE2 1 ? 3  
ATOM 867   N N   . ILE A 1 115 ? 44.591  55.505  30.548 1.000 96.936  0 115 ILE BBB N   1 ? 3  
ATOM 868   C CA  . ILE A 1 115 ? 45.311  56.438  29.684 1.000 96.926  0 115 ILE BBB CA  1 ? 3  
ATOM 869   C C   . ILE A 1 115 ? 44.609  56.601  28.341 1.000 99.699  0 115 ILE BBB C   1 ? 3  
ATOM 870   O O   . ILE A 1 115 ? 44.486  57.717  27.819 1.000 101.157 0 115 ILE BBB O   1 ? 3  
ATOM 871   C CB  . ILE A 1 115 ? 46.779  56.000  29.515 1.000 93.796  0 115 ILE BBB CB  1 ? 3  
ATOM 872   C CG1 . ILE A 1 115 ? 47.536  56.126  30.843 1.000 90.956  0 115 ILE BBB CG1 1 ? 3  
ATOM 873   C CG2 . ILE A 1 115 ? 47.453  56.811  28.425 1.000 97.744  0 115 ILE BBB CG2 1 ? 3  
ATOM 874   C CD1 . ILE A 1 115 ? 48.845  55.360  30.884 1.000 90.376  0 115 ILE BBB CD1 1 ? 3  
ATOM 875   N N   . GLY A 1 116 ? 44.130  55.495  27.768 1.000 104.609 0 116 GLY BBB N   1 ? 3  
ATOM 876   C CA  . GLY A 1 116 ? 43.399  55.571  26.510 1.000 108.939 0 116 GLY BBB CA  1 ? 3  
ATOM 877   C C   . GLY A 1 116 ? 42.204  56.504  26.556 1.000 106.391 0 116 GLY BBB C   1 ? 3  
ATOM 878   O O   . GLY A 1 116 ? 42.010  57.328  25.657 1.000 106.936 0 116 GLY BBB O   1 ? 3  
ATOM 879   N N   . TRP A 1 117 ? 41.389  56.395  27.604 1.000 97.699  0 117 TRP BBB N   1 ? 3  
ATOM 880   C CA  . TRP A 1 117 ? 40.221  57.261  27.716 1.000 92.614  0 117 TRP BBB CA  1 ? 3  
ATOM 881   C C   . TRP A 1 117 ? 40.628  58.715  27.916 1.000 91.544  0 117 TRP BBB C   1 ? 3  
ATOM 882   O O   . TRP A 1 117 ? 40.120  59.613  27.235 1.000 97.506  0 117 TRP BBB O   1 ? 3  
ATOM 883   C CB  . TRP A 1 117 ? 39.332  56.790  28.868 1.000 92.391  0 117 TRP BBB CB  1 ? 3  
ATOM 884   C CG  . TRP A 1 117 ? 38.685  55.468  28.631 1.000 95.476  0 117 TRP BBB CG  1 ? 3  
ATOM 885   C CD1 . TRP A 1 117 ? 38.105  55.042  27.478 1.000 107.776 0 117 TRP BBB CD1 1 ? 3  
ATOM 886   C CD2 . TRP A 1 117 ? 38.552  54.392  29.569 1.000 100.544 0 117 TRP BBB CD2 1 ? 3  
ATOM 887   N NE1 . TRP A 1 117 ? 37.616  53.767  27.634 1.000 115.563 0 117 TRP BBB NE1 1 ? 3  
ATOM 888   C CE2 . TRP A 1 117 ? 37.878  53.345  28.910 1.000 104.817 0 117 TRP BBB CE2 1 ? 3  
ATOM 889   C CE3 . TRP A 1 117 ? 38.935  54.214  30.901 1.000 104.180 0 117 TRP BBB CE3 1 ? 3  
ATOM 890   C CZ2 . TRP A 1 117 ? 37.578  52.136  29.537 1.000 104.893 0 117 TRP BBB CZ2 1 ? 3  
ATOM 891   C CZ3 . TRP A 1 117 ? 38.637  53.012  31.523 1.000 103.804 0 117 TRP BBB CZ3 1 ? 3  
ATOM 892   C CH2 . TRP A 1 117 ? 37.966  51.989  30.840 1.000 102.918 0 117 TRP BBB CH2 1 ? 3  
ATOM 893   N N   . MET A 1 118 ? 41.559  58.962  28.831 1.000 89.541  0 118 MET BBB N   1 ? 3  
ATOM 894   C CA  . MET A 1 118 ? 41.956  60.328  29.148 1.000 89.974  0 118 MET BBB CA  1 ? 3  
ATOM 895   C C   . MET A 1 118 ? 42.644  61.032  27.978 1.000 104.334 0 118 MET BBB C   1 ? 3  
ATOM 896   O O   . MET A 1 118 ? 42.550  62.259  27.868 1.000 114.679 0 118 MET BBB O   1 ? 3  
ATOM 897   C CB  . MET A 1 118 ? 42.835  60.327  30.396 1.000 91.461  0 118 MET BBB CB  1 ? 3  
ATOM 898   C CG  . MET A 1 118 ? 42.049  59.949  31.646 1.000 93.066  0 118 MET BBB CG  1 ? 3  
ATOM 899   S SD  . MET A 1 118 ? 43.057  59.653  33.114 1.000 86.096  0 118 MET BBB SD  1 ? 3  
ATOM 900   C CE  . MET A 1 118 ? 43.674  61.302  33.467 1.000 88.662  0 118 MET BBB CE  1 ? 3  
ATOM 901   N N   . THR A 1 119 ? 43.336  60.300  27.101 1.000 104.877 0 119 THR BBB N   1 ? 3  
ATOM 902   C CA  . THR A 1 119 ? 44.049  60.915  25.984 1.000 102.306 0 119 THR BBB CA  1 ? 3  
ATOM 903   C C   . THR A 1 119 ? 43.327  60.783  24.647 1.000 112.489 0 119 THR BBB C   1 ? 3  
ATOM 904   O O   . THR A 1 119 ? 43.922  61.072  23.605 1.000 124.620 0 119 THR BBB O   1 ? 3  
ATOM 905   C CB  . THR A 1 119 ? 45.451  60.324  25.861 1.000 99.093  0 119 THR BBB CB  1 ? 3  
ATOM 906   O OG1 . THR A 1 119 ? 45.349  58.926  25.568 1.000 103.859 0 119 THR BBB OG1 1 ? 3  
ATOM 907   C CG2 . THR A 1 119 ? 46.202  60.506  27.157 1.000 105.224 0 119 THR BBB CG2 1 ? 3  
ATOM 908   N N   . HIS A 1 120 ? 42.073  60.349  24.648 1.000 119.125 0 120 HIS BBB N   1 ? 3  
ATOM 909   C CA  . HIS A 1 120 ? 41.336  60.213  23.403 1.000 124.505 0 120 HIS BBB CA  1 ? 3  
ATOM 910   C C   . HIS A 1 120 ? 40.965  61.596  22.866 1.000 133.602 0 120 HIS BBB C   1 ? 3  
ATOM 911   O O   . HIS A 1 120 ? 41.044  62.604  23.572 1.000 135.267 0 120 HIS BBB O   1 ? 3  
ATOM 912   C CB  . HIS A 1 120 ? 40.077  59.378  23.625 1.000 130.876 0 120 HIS BBB CB  1 ? 3  
ATOM 913   C CG  . HIS A 1 120 ? 39.445  58.894  22.361 1.000 142.761 0 120 HIS BBB CG  1 ? 3  
ATOM 914   N ND1 . HIS A 1 120 ? 38.288  59.445  21.855 1.000 151.119 0 120 HIS BBB ND1 1 ? 3  
ATOM 915   C CD2 . HIS A 1 120 ? 39.797  57.905  21.506 1.000 150.386 0 120 HIS BBB CD2 1 ? 3  
ATOM 916   C CE1 . HIS A 1 120 ? 37.959  58.824  20.737 1.000 162.399 0 120 HIS BBB CE1 1 ? 3  
ATOM 917   N NE2 . HIS A 1 120 ? 38.858  57.884  20.504 1.000 164.522 0 120 HIS BBB NE2 1 ? 3  
ATOM 918   N N   . ASN A 1 121 ? 40.593  61.647  21.592 1.000 144.929 0 121 ASN BBB N   1 ? 3  
ATOM 919   C CA  . ASN A 1 121 ? 40.047  62.868  20.993 1.000 150.957 0 121 ASN BBB CA  1 ? 3  
ATOM 920   C C   . ASN A 1 121 ? 38.679  62.559  20.400 1.000 160.495 0 121 ASN BBB C   1 ? 3  
ATOM 921   O O   . ASN A 1 121 ? 38.603  61.925  19.330 1.000 163.895 0 121 ASN BBB O   1 ? 3  
ATOM 922   C CB  . ASN A 1 121 ? 40.977  63.437  19.921 1.000 152.205 0 121 ASN BBB CB  1 ? 3  
ATOM 923   C CG  . ASN A 1 121 ? 40.514  64.793  19.411 1.000 149.235 0 121 ASN BBB CG  1 ? 3  
ATOM 924   O OD1 . ASN A 1 121 ? 40.014  65.621  20.176 1.000 145.233 0 121 ASN BBB OD1 1 ? 3  
ATOM 925   N ND2 . ASN A 1 121 ? 40.675  65.024  18.113 1.000 155.501 0 121 ASN BBB ND2 1 ? 3  
ATOM 926   N N   . PRO A 1 122 ? 37.571  62.977  21.033 1.000 169.949 0 122 PRO BBB N   1 ? 3  
ATOM 927   C CA  . PRO A 1 122 ? 37.531  63.765  22.271 1.000 162.247 0 122 PRO BBB CA  1 ? 3  
ATOM 928   C C   . PRO A 1 122 ? 37.863  62.946  23.517 1.000 157.658 0 122 PRO BBB C   1 ? 3  
ATOM 929   O O   . PRO A 1 122 ? 37.617  61.741  23.550 1.000 162.357 0 122 PRO BBB O   1 ? 3  
ATOM 930   C CB  . PRO A 1 122 ? 36.078  64.269  22.319 1.000 171.636 0 122 PRO BBB CB  1 ? 3  
ATOM 931   C CG  . PRO A 1 122 ? 35.529  64.040  20.931 1.000 175.726 0 122 PRO BBB CG  1 ? 3  
ATOM 932   C CD  . PRO A 1 122 ? 36.229  62.817  20.452 1.000 175.171 0 122 PRO BBB CD  1 ? 3  
ATOM 933   N N   . PRO A 1 123 ? 38.427  63.600  24.531 1.000 140.561 0 123 PRO BBB N   1 ? 3  
ATOM 934   C CA  . PRO A 1 123 ? 38.832  62.873  25.738 1.000 124.627 0 123 PRO BBB CA  1 ? 3  
ATOM 935   C C   . PRO A 1 123 ? 37.644  62.462  26.592 1.000 120.063 0 123 PRO BBB C   1 ? 3  
ATOM 936   O O   . PRO A 1 123 ? 36.676  63.209  26.753 1.000 126.365 0 123 PRO BBB O   1 ? 3  
ATOM 937   C CB  . PRO A 1 123 ? 39.727  63.878  26.469 1.000 117.190 0 123 PRO BBB CB  1 ? 3  
ATOM 938   C CG  . PRO A 1 123 ? 39.209  65.207  26.046 1.000 124.401 0 123 PRO BBB CG  1 ? 3  
ATOM 939   C CD  . PRO A 1 123 ? 38.717  65.042  24.628 1.000 138.941 0 123 PRO BBB CD  1 ? 3  
ATOM 940   N N   . ILE A 1 124 ? 37.724  61.246  27.125 1.000 107.798 0 124 ILE BBB N   1 ? 3  
ATOM 941   C CA  . ILE A 1 124 ? 36.770  60.760  28.118 1.000 106.592 0 124 ILE BBB CA  1 ? 3  
ATOM 942   C C   . ILE A 1 124 ? 37.482  60.847  29.465 1.000 103.123 0 124 ILE BBB C   1 ? 3  
ATOM 943   O O   . ILE A 1 124 ? 38.278  59.960  29.806 1.000 107.618 0 124 ILE BBB O   1 ? 3  
ATOM 944   C CB  . ILE A 1 124 ? 36.311  59.329  27.795 1.000 104.822 0 124 ILE BBB CB  1 ? 3  
ATOM 945   C CG1 . ILE A 1 124 ? 35.704  59.268  26.390 1.000 111.473 0 124 ILE BBB CG1 1 ? 3  
ATOM 946   C CG2 . ILE A 1 124 ? 35.314  58.838  28.832 1.000 102.506 0 124 ILE BBB CG2 1 ? 3  
ATOM 947   C CD1 . ILE A 1 124 ? 35.585  57.862  25.828 1.000 118.801 0 124 ILE BBB CD1 1 ? 3  
ATOM 948   N N   . PRO A 1 125 ? 37.206  61.875  30.273 1.000 96.749  0 125 PRO BBB N   1 ? 3  
ATOM 949   C CA  . PRO A 1 125 ? 38.048  62.201  31.447 1.000 93.098  0 125 PRO BBB CA  1 ? 3  
ATOM 950   C C   . PRO A 1 125 ? 37.740  61.392  32.701 1.000 91.754  0 125 PRO BBB C   1 ? 3  
ATOM 951   O O   . PRO A 1 125 ? 37.197  61.894  33.693 1.000 97.977  0 125 PRO BBB O   1 ? 3  
ATOM 952   C CB  . PRO A 1 125 ? 37.762  63.693  31.638 1.000 96.721  0 125 PRO BBB CB  1 ? 3  
ATOM 953   C CG  . PRO A 1 125 ? 36.325  63.836  31.219 1.000 93.855  0 125 PRO BBB CG  1 ? 3  
ATOM 954   C CD  . PRO A 1 125 ? 36.048  62.779  30.164 1.000 95.689  0 125 PRO BBB CD  1 ? 3  
ATOM 955   N N   . VAL A 1 126 ? 38.104  60.108  32.679 1.000 87.934  0 126 VAL BBB N   1 ? 3  
ATOM 956   C CA  . VAL A 1 126 ? 37.750  59.231  33.791 1.000 87.539  0 126 VAL BBB CA  1 ? 3  
ATOM 957   C C   . VAL A 1 126 ? 38.414  59.698  35.077 1.000 88.625  0 126 VAL BBB C   1 ? 3  
ATOM 958   O O   . VAL A 1 126 ? 37.869  59.514  36.174 1.000 96.408  0 126 VAL BBB O   1 ? 3  
ATOM 959   C CB  . VAL A 1 126 ? 38.118  57.771  33.466 1.000 86.925  0 126 VAL BBB CB  1 ? 3  
ATOM 960   C CG1 . VAL A 1 126 ? 37.252  57.253  32.338 1.000 89.014  0 126 VAL BBB CG1 1 ? 3  
ATOM 961   C CG2 . VAL A 1 126 ? 39.586  57.657  33.117 1.000 85.442  0 126 VAL BBB CG2 1 ? 3  
ATOM 962   N N   . GLY A 1 127 ? 39.596  60.303  34.972 1.000 85.404  0 127 GLY BBB N   1 ? 3  
ATOM 963   C CA  . GLY A 1 127 ? 40.237  60.859  36.153 1.000 89.855  0 127 GLY BBB CA  1 ? 3  
ATOM 964   C C   . GLY A 1 127 ? 39.467  62.001  36.792 1.000 90.069  0 127 GLY BBB C   1 ? 3  
ATOM 965   O O   . GLY A 1 127 ? 39.276  62.030  38.011 1.000 89.745  0 127 GLY BBB O   1 ? 3  
ATOM 966   N N   . GLU A 1 128 ? 38.994  62.948  35.980 1.000 84.687  0 128 GLU BBB N   1 ? 3  
ATOM 967   C CA  . GLU A 1 128 ? 38.255  64.078  36.537 1.000 84.675  0 128 GLU BBB CA  1 ? 3  
ATOM 968   C C   . GLU A 1 128 ? 36.916  63.651  37.116 1.000 88.066  0 128 GLU BBB C   1 ? 3  
ATOM 969   O O   . GLU A 1 128 ? 36.478  64.187  38.140 1.000 92.495  0 128 GLU BBB O   1 ? 3  
ATOM 970   C CB  . GLU A 1 128 ? 38.056  65.147  35.467 1.000 90.847  0 128 GLU BBB CB  1 ? 3  
ATOM 971   C CG  . GLU A 1 128 ? 39.338  65.823  35.008 1.000 105.612 0 128 GLU BBB CG  1 ? 3  
ATOM 972   C CD  . GLU A 1 128 ? 40.171  66.407  36.132 1.000 112.953 0 128 GLU BBB CD  1 ? 3  
ATOM 973   O OE1 . GLU A 1 128 ? 39.599  66.709  37.202 1.000 108.147 0 128 GLU BBB OE1 1 ? 3  
ATOM 974   O OE2 . GLU A 1 128 ? 41.396  66.580  35.937 1.000 133.527 0 128 GLU BBB OE2 1 ? 3  
ATOM 975   N N   . ILE A 1 129 ? 36.252  62.694  36.470 1.000 91.531  0 129 ILE BBB N   1 ? 3  
ATOM 976   C CA  . ILE A 1 129 ? 34.971  62.195  36.965 1.000 90.063  0 129 ILE BBB CA  1 ? 3  
ATOM 977   C C   . ILE A 1 129 ? 35.145  61.496  38.307 1.000 90.788  0 129 ILE BBB C   1 ? 3  
ATOM 978   O O   . ILE A 1 129 ? 34.385  61.738  39.253 1.000 95.903  0 129 ILE BBB O   1 ? 3  
ATOM 979   C CB  . ILE A 1 129 ? 34.322  61.266  35.927 1.000 88.823  0 129 ILE BBB CB  1 ? 3  
ATOM 980   C CG1 . ILE A 1 129 ? 34.067  62.037  34.634 1.000 89.079  0 129 ILE BBB CG1 1 ? 3  
ATOM 981   C CG2 . ILE A 1 129 ? 33.032  60.692  36.480 1.000 98.772  0 129 ILE BBB CG2 1 ? 3  
ATOM 982   C CD1 . ILE A 1 129 ? 33.826  61.166  33.434 1.000 90.705  0 129 ILE BBB CD1 1 ? 3  
ATOM 983   N N   . TYR A 1 130 ? 36.144  60.615  38.408 1.000 87.800  0 130 TYR BBB N   1 ? 3  
ATOM 984   C CA  . TYR A 1 130 ? 36.392  59.930  39.673 1.000 86.447  0 130 TYR BBB CA  1 ? 3  
ATOM 985   C C   . TYR A 1 130 ? 36.740  60.924  40.771 1.000 88.361  0 130 TYR BBB C   1 ? 3  
ATOM 986   O O   . TYR A 1 130 ? 36.277  60.784  41.910 1.000 91.902  0 130 TYR BBB O   1 ? 3  
ATOM 987   C CB  . TYR A 1 130 ? 37.532  58.924  39.498 1.000 85.211  0 130 TYR BBB CB  1 ? 3  
ATOM 988   C CG  . TYR A 1 130 ? 37.702  57.968  40.653 1.000 85.895  0 130 TYR BBB CG  1 ? 3  
ATOM 989   C CD1 . TYR A 1 130 ? 36.624  57.607  41.447 1.000 87.294  0 130 TYR BBB CD1 1 ? 3  
ATOM 990   C CD2 . TYR A 1 130 ? 38.942  57.423  40.946 1.000 85.583  0 130 TYR BBB CD2 1 ? 3  
ATOM 991   C CE1 . TYR A 1 130 ? 36.778  56.726  42.497 1.000 88.108  0 130 TYR BBB CE1 1 ? 3  
ATOM 992   C CE2 . TYR A 1 130 ? 39.105  56.541  41.995 1.000 86.611  0 130 TYR BBB CE2 1 ? 3  
ATOM 993   C CZ  . TYR A 1 130 ? 38.018  56.196  42.766 1.000 87.684  0 130 TYR BBB CZ  1 ? 3  
ATOM 994   O OH  . TYR A 1 130 ? 38.170  55.314  43.811 1.000 91.412  0 130 TYR BBB OH  1 ? 3  
ATOM 995   N N   . LYS A 1 131 ? 37.545  61.938  40.447 1.000 85.941  0 131 LYS BBB N   1 ? 3  
ATOM 996   C CA  . LYS A 1 131 ? 37.900  62.941  41.445 1.000 86.780  0 131 LYS BBB CA  1 ? 3  
ATOM 997   C C   . LYS A 1 131 ? 36.656  63.663  41.955 1.000 87.723  0 131 LYS BBB C   1 ? 3  
ATOM 998   O O   . LYS A 1 131 ? 36.573  64.005  43.140 1.000 88.527  0 131 LYS BBB O   1 ? 3  
ATOM 999   C CB  . LYS A 1 131 ? 38.963  63.892  40.876 1.000 87.272  0 131 LYS BBB CB  1 ? 3  
ATOM 1000  C CG  . LYS A 1 131 ? 39.629  64.773  41.939 1.000 91.193  0 131 LYS BBB CG  1 ? 3  
ATOM 1001  C CD  . LYS A 1 131 ? 40.473  65.922  41.364 1.000 88.894  0 131 LYS BBB CD  1 ? 3  
ATOM 1002  C CE  . LYS A 1 131 ? 39.674  67.001  40.680 1.000 103.484 0 131 LYS BBB CE  1 ? 3  
ATOM 1003  N NZ  . LYS A 1 131 ? 40.572  67.837  39.826 1.000 103.485 0 131 LYS BBB NZ  1 ? 3  
ATOM 1004  N N   . ARG A 1 132 ? 35.694  63.922  41.070 1.000 96.990  0 132 ARG BBB N   1 ? 3  
ATOM 1005  C CA  . ARG A 1 132 ? 34.422  64.498  41.494 1.000 99.436  0 132 ARG BBB CA  1 ? 3  
ATOM 1006  C C   . ARG A 1 132 ? 33.754  63.642  42.563 1.000 99.062  0 132 ARG BBB C   1 ? 3  
ATOM 1007  O O   . ARG A 1 132 ? 33.300  64.149  43.598 1.000 102.025 0 132 ARG BBB O   1 ? 3  
ATOM 1008  C CB  . ARG A 1 132 ? 33.452  64.559  40.317 1.000 108.413 0 132 ARG BBB CB  1 ? 3  
ATOM 1009  C CG  . ARG A 1 132 ? 32.138  65.246  40.680 1.000 121.024 0 132 ARG BBB CG  1 ? 3  
ATOM 1010  C CD  . ARG A 1 132 ? 31.070  64.992  39.640 1.000 132.436 0 132 ARG BBB CD  1 ? 3  
ATOM 1011  N NE  . ARG A 1 132 ? 31.489  65.223  38.270 1.000 154.499 0 132 ARG BBB NE  1 ? 3  
ATOM 1012  C CZ  . ARG A 1 132 ? 30.945  64.606  37.223 1.000 154.777 0 132 ARG BBB CZ  1 ? 3  
ATOM 1013  N NH1 . ARG A 1 132 ? 29.982  63.700  37.380 1.000 152.202 0 132 ARG BBB NH1 1 ? 3  
ATOM 1014  N NH2 . ARG A 1 132 ? 31.404  64.868  36.007 1.000 148.639 0 132 ARG BBB NH2 1 ? 3  
ATOM 1015  N N   . TRP A 1 133 ? 33.682  62.325  42.327 1.000 88.727  0 133 TRP BBB N   1 ? 3  
ATOM 1016  C CA  . TRP A 1 133 ? 33.028  61.441  43.294 1.000 90.056  0 133 TRP BBB CA  1 ? 3  
ATOM 1017  C C   . TRP A 1 133 ? 33.773  61.423  44.621 1.000 89.175  0 133 TRP BBB C   1 ? 3  
ATOM 1018  O O   . TRP A 1 133 ? 33.155  61.452  45.691 1.000 93.388  0 133 TRP BBB O   1 ? 3  
ATOM 1019  C CB  . TRP A 1 133 ? 32.954  60.022  42.729 1.000 90.729  0 133 TRP BBB CB  1 ? 3  
ATOM 1020  C CG  . TRP A 1 133 ? 32.239  59.882  41.410 1.000 92.754  0 133 TRP BBB CG  1 ? 3  
ATOM 1021  C CD1 . TRP A 1 133 ? 31.463  60.815  40.782 1.000 100.037 0 133 TRP BBB CD1 1 ? 3  
ATOM 1022  C CD2 . TRP A 1 133 ? 32.247  58.729  40.557 1.000 95.324  0 133 TRP BBB CD2 1 ? 3  
ATOM 1023  N NE1 . TRP A 1 133 ? 30.990  60.313  39.591 1.000 102.951 0 133 TRP BBB NE1 1 ? 3  
ATOM 1024  C CE2 . TRP A 1 133 ? 31.457  59.034  39.432 1.000 99.735  0 133 TRP BBB CE2 1 ? 3  
ATOM 1025  C CE3 . TRP A 1 133 ? 32.846  57.468  40.638 1.000 96.442  0 133 TRP BBB CE3 1 ? 3  
ATOM 1026  C CZ2 . TRP A 1 133 ? 31.252  58.123  38.396 1.000 103.034 0 133 TRP BBB CZ2 1 ? 3  
ATOM 1027  C CZ3 . TRP A 1 133 ? 32.640  56.565  39.608 1.000 95.701  0 133 TRP BBB CZ3 1 ? 3  
ATOM 1028  C CH2 . TRP A 1 133 ? 31.852  56.897  38.504 1.000 97.580  0 133 TRP BBB CH2 1 ? 3  
ATOM 1029  N N   . ILE A 1 134 ? 35.103  61.381  44.571 1.000 85.926  0 134 ILE BBB N   1 ? 3  
ATOM 1030  C CA  . ILE A 1 134 ? 35.873  61.347  45.806 1.000 85.046  0 134 ILE BBB CA  1 ? 3  
ATOM 1031  C C   . ILE A 1 134 ? 35.675  62.628  46.604 1.000 84.941  0 134 ILE BBB C   1 ? 3  
ATOM 1032  O O   . ILE A 1 134 ? 35.436  62.588  47.818 1.000 85.514  0 134 ILE BBB O   1 ? 3  
ATOM 1033  C CB  . ILE A 1 134 ? 37.355  61.070  45.495 1.000 83.579  0 134 ILE BBB CB  1 ? 3  
ATOM 1034  C CG1 . ILE A 1 134 ? 37.490  59.641  44.982 1.000 83.453  0 134 ILE BBB CG1 1 ? 3  
ATOM 1035  C CG2 . ILE A 1 134 ? 38.226  61.279  46.723 1.000 83.914  0 134 ILE BBB CG2 1 ? 3  
ATOM 1036  C CD1 . ILE A 1 134 ? 38.785  59.346  44.313 1.000 82.095  0 134 ILE BBB CD1 1 ? 3  
ATOM 1037  N N   . ILE A 1 135 ? 35.696  63.778  45.931 1.000 85.579  0 135 ILE BBB N   1 ? 3  
ATOM 1038  C CA  . ILE A 1 135 ? 35.506  65.036  46.643 1.000 85.624  0 135 ILE BBB CA  1 ? 3  
ATOM 1039  C C   . ILE A 1 135 ? 34.104  65.124  47.231 1.000 90.272  0 135 ILE BBB C   1 ? 3  
ATOM 1040  O O   . ILE A 1 135 ? 33.928  65.572  48.369 1.000 98.316  0 135 ILE BBB O   1 ? 3  
ATOM 1041  C CB  . ILE A 1 135 ? 35.817  66.215  45.706 1.000 84.328  0 135 ILE BBB CB  1 ? 3  
ATOM 1042  C CG1 . ILE A 1 135 ? 37.326  66.302  45.482 1.000 83.473  0 135 ILE BBB CG1 1 ? 3  
ATOM 1043  C CG2 . ILE A 1 135 ? 35.295  67.516  46.276 1.000 84.507  0 135 ILE BBB CG2 1 ? 3  
ATOM 1044  C CD1 . ILE A 1 135 ? 37.728  67.206  44.345 1.000 87.658  0 135 ILE BBB CD1 1 ? 3  
ATOM 1045  N N   . LEU A 1 136 ? 33.092  64.654  46.499 1.000 93.054  0 136 LEU BBB N   1 ? 3  
ATOM 1046  C CA  . LEU A 1 136 ? 31.755  64.574  47.079 1.000 96.692  0 136 LEU BBB CA  1 ? 3  
ATOM 1047  C C   . LEU A 1 136 ? 31.760  63.753  48.366 1.000 94.807  0 136 LEU BBB C   1 ? 3  
ATOM 1048  O O   . LEU A 1 136 ? 31.135  64.138  49.362 1.000 98.566  0 136 LEU BBB O   1 ? 3  
ATOM 1049  C CB  . LEU A 1 136 ? 30.762  64.008  46.065 1.000 97.647  0 136 LEU BBB CB  1 ? 3  
ATOM 1050  C CG  . LEU A 1 136 ? 29.379  63.698  46.647 1.000 109.882 0 136 LEU BBB CG  1 ? 3  
ATOM 1051  C CD1 . LEU A 1 136 ? 28.732  64.928  47.306 1.000 109.924 0 136 LEU BBB CD1 1 ? 3  
ATOM 1052  C CD2 . LEU A 1 136 ? 28.479  63.124  45.566 1.000 112.048 0 136 LEU BBB CD2 1 ? 3  
ATOM 1053  N N   . GLY A 1 137 ? 32.462  62.616  48.357 1.000 91.735  0 137 GLY BBB N   1 ? 3  
ATOM 1054  C CA  . GLY A 1 137 ? 32.576  61.791  49.553 1.000 94.997  0 137 GLY BBB CA  1 ? 3  
ATOM 1055  C C   . GLY A 1 137 ? 33.328  62.468  50.684 1.000 97.237  0 137 GLY BBB C   1 ? 3  
ATOM 1056  O O   . GLY A 1 137 ? 32.940  62.366  51.851 1.000 100.267 0 137 GLY BBB O   1 ? 3  
ATOM 1057  N N   . LEU A 1 138 ? 34.442  63.129  50.362 1.000 97.980  0 138 LEU BBB N   1 ? 3  
ATOM 1058  C CA  . LEU A 1 138 ? 35.208  63.815  51.397 1.000 92.036  0 138 LEU BBB CA  1 ? 3  
ATOM 1059  C C   . LEU A 1 138 ? 34.386  64.929  52.028 1.000 92.552  0 138 LEU BBB C   1 ? 3  
ATOM 1060  O O   . LEU A 1 138 ? 34.459  65.150  53.242 1.000 100.252 0 138 LEU BBB O   1 ? 3  
ATOM 1061  C CB  . LEU A 1 138 ? 36.509  64.362  50.812 1.000 88.430  0 138 LEU BBB CB  1 ? 3  
ATOM 1062  C CG  . LEU A 1 138 ? 37.505  63.278  50.397 1.000 87.094  0 138 LEU BBB CG  1 ? 3  
ATOM 1063  C CD1 . LEU A 1 138 ? 38.675  63.897  49.664 1.000 84.523  0 138 LEU BBB CD1 1 ? 3  
ATOM 1064  C CD2 . LEU A 1 138 ? 37.970  62.452  51.588 1.000 88.500  0 138 LEU BBB CD2 1 ? 3  
ATOM 1065  N N   . ASN A 1 139 ? 33.602  65.646  51.220 1.000 92.093  0 139 ASN BBB N   1 ? 3  
ATOM 1066  C CA  . ASN A 1 139 ? 32.719  66.670  51.769 1.000 96.565  0 139 ASN BBB CA  1 ? 3  
ATOM 1067  C C   . ASN A 1 139 ? 31.816  66.100  52.856 1.000 105.094 0 139 ASN BBB C   1 ? 3  
ATOM 1068  O O   . ASN A 1 139 ? 31.649  66.715  53.908 1.000 115.517 0 139 ASN BBB O   1 ? 3  
ATOM 1069  C CB  . ASN A 1 139 ? 31.906  67.353  50.673 1.000 108.390 0 139 ASN BBB CB  1 ? 3  
ATOM 1070  C CG  . ASN A 1 139 ? 32.764  68.240  49.794 1.000 108.525 0 139 ASN BBB CG  1 ? 3  
ATOM 1071  O OD1 . ASN A 1 139 ? 32.955  69.420  50.090 1.000 112.624 0 139 ASN BBB OD1 1 ? 3  
ATOM 1072  N ND2 . ASN A 1 139 ? 33.257  67.692  48.697 1.000 111.249 0 139 ASN BBB ND2 1 ? 3  
ATOM 1073  N N   . LYS A 1 140 ? 31.239  64.921  52.632 1.000 104.761 0 140 LYS BBB N   1 ? 3  
ATOM 1074  C CA  . LYS A 1 140 ? 30.374  64.326  53.647 1.000 107.949 0 140 LYS BBB CA  1 ? 3  
ATOM 1075  C C   . LYS A 1 140 ? 31.141  64.046  54.934 1.000 110.810 0 140 LYS BBB C   1 ? 3  
ATOM 1076  O O   . LYS A 1 140 ? 30.630  64.284  56.032 1.000 130.676 0 140 LYS BBB O   1 ? 3  
ATOM 1077  C CB  . LYS A 1 140 ? 29.754  63.028  53.133 1.000 109.216 0 140 LYS BBB CB  1 ? 3  
ATOM 1078  C CG  . LYS A 1 140 ? 28.730  63.180  52.024 1.000 116.785 0 140 LYS BBB CG  1 ? 3  
ATOM 1079  C CD  . LYS A 1 140 ? 28.567  61.845  51.306 1.000 119.933 0 140 LYS BBB CD  1 ? 3  
ATOM 1080  C CE  . LYS A 1 140 ? 27.200  61.696  50.656 1.000 127.495 0 140 LYS BBB CE  1 ? 3  
ATOM 1081  N NZ  . LYS A 1 140 ? 26.914  62.780  49.677 1.000 125.310 0 140 LYS BBB NZ  1 ? 3  
ATOM 1082  N N   . ILE A 1 141 ? 32.379  63.570  54.817 1.000 105.285 0 141 ILE BBB N   1 ? 3  
ATOM 1083  C CA  . ILE A 1 141 ? 33.197  63.263  55.990 1.000 102.720 0 141 ILE BBB CA  1 ? 3  
ATOM 1084  C C   . ILE A 1 141 ? 33.519  64.516  56.807 1.000 107.353 0 141 ILE BBB C   1 ? 3  
ATOM 1085  O O   . ILE A 1 141 ? 33.421  64.495  58.040 1.000 121.557 0 141 ILE BBB O   1 ? 3  
ATOM 1086  C CB  . ILE A 1 141 ? 34.464  62.506  55.558 1.000 103.856 0 141 ILE BBB CB  1 ? 3  
ATOM 1087  C CG1 . ILE A 1 141 ? 34.069  61.143  54.998 1.000 103.112 0 141 ILE BBB CG1 1 ? 3  
ATOM 1088  C CG2 . ILE A 1 141 ? 35.421  62.337  56.717 1.000 106.090 0 141 ILE BBB CG2 1 ? 3  
ATOM 1089  C CD1 . ILE A 1 141 ? 35.124  60.540  54.138 1.000 109.814 0 141 ILE BBB CD1 1 ? 3  
ATOM 1090  N N   . VAL A 1 142 ? 33.910  65.619  56.155 1.000 103.175 0 142 VAL BBB N   1 ? 3  
ATOM 1091  C CA  . VAL A 1 142 ? 34.186  66.855  56.900 1.000 107.734 0 142 VAL BBB CA  1 ? 3  
ATOM 1092  C C   . VAL A 1 142 ? 32.968  67.262  57.729 1.000 123.333 0 142 VAL BBB C   1 ? 3  
ATOM 1093  O O   . VAL A 1 142 ? 33.106  67.720  58.870 1.000 132.232 0 142 VAL BBB O   1 ? 3  
ATOM 1094  C CB  . VAL A 1 142 ? 34.691  67.997  55.988 1.000 95.664  0 142 VAL BBB CB  1 ? 3  
ATOM 1095  C CG1 . VAL A 1 142 ? 35.922  67.559  55.232 1.000 92.968  0 142 VAL BBB CG1 1 ? 3  
ATOM 1096  C CG2 . VAL A 1 142 ? 33.627  68.542  55.067 1.000 105.248 0 142 VAL BBB CG2 1 ? 3  
ATOM 1097  N N   . ARG A 1 143 ? 31.763  67.120  57.171 1.000 120.572 0 143 ARG BBB N   1 ? 3  
ATOM 1098  C CA  . ARG A 1 143 ? 30.557  67.479  57.914 1.000 124.281 0 143 ARG BBB CA  1 ? 3  
ATOM 1099  C C   . ARG A 1 143 ? 30.392  66.569  59.123 1.000 127.530 0 143 ARG BBB C   1 ? 3  
ATOM 1100  O O   . ARG A 1 143 ? 30.052  67.038  60.216 1.000 139.437 0 143 ARG BBB O   1 ? 3  
ATOM 1101  C CB  . ARG A 1 143 ? 29.336  67.341  57.008 1.000 136.730 0 143 ARG BBB CB  1 ? 3  
ATOM 1102  C CG  . ARG A 1 143 ? 29.581  67.836  55.619 1.000 154.830 0 143 ARG BBB CG  1 ? 3  
ATOM 1103  C CD  . ARG A 1 143 ? 28.473  67.477  54.646 1.000 166.996 0 143 ARG BBB CD  1 ? 3  
ATOM 1104  N NE  . ARG A 1 143 ? 27.172  68.062  54.938 1.000 180.708 0 143 ARG BBB NE  1 ? 3  
ATOM 1105  C CZ  . ARG A 1 143 ? 26.102  67.874  54.178 1.000 193.274 0 143 ARG BBB CZ  1 ? 3  
ATOM 1106  N NH1 . ARG A 1 143 ? 26.156  67.136  53.081 1.000 200.140 0 143 ARG BBB NH1 1 ? 3  
ATOM 1107  N NH2 . ARG A 1 143 ? 24.952  68.448  54.519 1.000 199.152 0 143 ARG BBB NH2 1 ? 3  
ATOM 1108  N N   . MET A 1 144 ? 30.614  65.262  58.946 1.000 126.959 0 144 MET BBB N   1 ? 3  
ATOM 1109  C CA  . MET A 1 144 ? 30.444  64.329  60.056 1.000 129.367 0 144 MET BBB CA  1 ? 3  
ATOM 1110  C C   . MET A 1 144 ? 31.431  64.648  61.172 1.000 131.551 0 144 MET BBB C   1 ? 3  
ATOM 1111  O O   . MET A 1 144 ? 31.096  64.544  62.358 1.000 150.459 0 144 MET BBB O   1 ? 3  
ATOM 1112  C CB  . MET A 1 144 ? 30.603  62.881  59.581 1.000 129.486 0 144 MET BBB CB  1 ? 3  
ATOM 1113  C CG  . MET A 1 144 ? 29.801  62.521  58.329 1.000 134.010 0 144 MET BBB CG  1 ? 3  
ATOM 1114  S SD  . MET A 1 144 ? 28.321  63.547  58.132 1.000 161.783 0 144 MET BBB SD  1 ? 3  
ATOM 1115  C CE  . MET A 1 144 ? 27.498  62.789  56.728 1.000 144.614 0 144 MET BBB CE  1 ? 3  
ATOM 1116  N N   . TYR A 1 145 ? 32.650  65.040  60.811 1.000 122.422 0 145 TYR BBB N   1 ? 3  
ATOM 1117  C CA  . TYR A 1 145 ? 33.716  65.290  61.770 1.000 124.514 0 145 TYR BBB CA  1 ? 3  
ATOM 1118  C C   . TYR A 1 145 ? 33.736  66.731  62.268 1.000 127.140 0 145 TYR BBB C   1 ? 3  
ATOM 1119  O O   . TYR A 1 145 ? 34.637  67.087  63.033 1.000 133.926 0 145 TYR BBB O   1 ? 3  
ATOM 1120  C CB  . TYR A 1 145 ? 35.090  64.937  61.181 1.000 122.303 0 145 TYR BBB CB  1 ? 3  
ATOM 1121  C CG  . TYR A 1 145 ? 35.402  63.457  61.031 1.000 125.474 0 145 TYR BBB CG  1 ? 3  
ATOM 1122  C CD1 . TYR A 1 145 ? 34.441  62.536  60.619 1.000 121.537 0 145 TYR BBB CD1 1 ? 3  
ATOM 1123  C CD2 . TYR A 1 145 ? 36.680  62.985  61.310 1.000 130.624 0 145 TYR BBB CD2 1 ? 3  
ATOM 1124  C CE1 . TYR A 1 145 ? 34.756  61.183  60.493 1.000 122.841 0 145 TYR BBB CE1 1 ? 3  
ATOM 1125  C CE2 . TYR A 1 145 ? 37.002  61.648  61.186 1.000 130.916 0 145 TYR BBB CE2 1 ? 3  
ATOM 1126  C CZ  . TYR A 1 145 ? 36.042  60.749  60.778 1.000 128.276 0 145 TYR BBB CZ  1 ? 3  
ATOM 1127  O OH  . TYR A 1 145 ? 36.388  59.418  60.659 1.000 121.540 0 145 TYR BBB OH  1 ? 3  
ATOM 1128  N N   . SER A 1 146 ? 32.789  67.569  61.843 1.000 123.490 0 146 SER BBB N   1 ? 4  
ATOM 1129  C CA  . SER A 1 146 ? 32.668  68.907  62.413 1.000 125.105 0 146 SER BBB CA  1 ? 4  
ATOM 1130  C C   . SER A 1 146 ? 32.359  68.759  63.896 1.000 132.069 0 146 SER BBB C   1 ? 4  
ATOM 1131  O O   . SER A 1 146 ? 31.341  68.144  64.247 1.000 143.450 0 146 SER BBB O   1 ? 4  
ATOM 1132  C CB  . SER A 1 146 ? 31.562  69.697  61.712 1.000 128.157 0 146 SER BBB CB  1 ? 4  
ATOM 1133  O OG  . SER A 1 146 ? 31.425  71.000  62.254 1.000 127.248 0 146 SER BBB OG  1 ? 4  
ATOM 1134  N N   . PRO A 1 147 ? 33.197  69.287  64.794 1.000 132.903 0 147 PRO BBB N   1 ? 4  
ATOM 1135  C CA  . PRO A 1 147 ? 32.988  69.024  66.228 1.000 140.815 0 147 PRO BBB CA  1 ? 4  
ATOM 1136  C C   . PRO A 1 147 ? 31.872  69.814  66.893 1.000 137.216 0 147 PRO BBB C   1 ? 4  
ATOM 1137  O O   . PRO A 1 147 ? 31.398  69.390  67.955 1.000 138.155 0 147 PRO BBB O   1 ? 4  
ATOM 1138  C CB  . PRO A 1 147 ? 34.343  69.404  66.843 1.000 143.629 0 147 PRO BBB CB  1 ? 4  
ATOM 1139  C CG  . PRO A 1 147 ? 34.882  70.451  65.914 1.000 135.059 0 147 PRO BBB CG  1 ? 4  
ATOM 1140  C CD  . PRO A 1 147 ? 34.402  70.091  64.535 1.000 130.717 0 147 PRO BBB CD  1 ? 4  
ATOM 1141  N N   . THR A 1 148 ? 31.442  70.936  66.325 1.000 140.586 0 148 THR BBB N   1 ? 4  
ATOM 1142  C CA  . THR A 1 148 ? 30.497  71.822  66.990 1.000 141.253 0 148 THR BBB CA  1 ? 4  
ATOM 1143  C C   . THR A 1 148 ? 29.444  72.301  66.006 1.000 141.747 0 148 THR BBB C   1 ? 4  
ATOM 1144  O O   . THR A 1 148 ? 29.749  72.548  64.837 1.000 147.316 0 148 THR BBB O   1 ? 4  
ATOM 1145  C CB  . THR A 1 148 ? 31.183  73.033  67.648 1.000 140.893 0 148 THR BBB CB  1 ? 4  
ATOM 1146  O OG1 . THR A 1 148 ? 31.804  73.849  66.647 1.000 154.097 0 148 THR BBB OG1 1 ? 4  
ATOM 1147  C CG2 . THR A 1 148 ? 32.212  72.595  68.693 1.000 138.852 0 148 THR BBB CG2 1 ? 4  
ATOM 1148  N N   . SER A 1 149 ? 28.205  72.394  66.463 1.000 144.514 0 149 SER BBB N   1 ? 4  
ATOM 1149  C CA  . SER A 1 149 ? 27.193  73.032  65.642 1.000 145.180 0 149 SER BBB CA  1 ? 4  
ATOM 1150  C C   . SER A 1 149 ? 27.358  74.545  65.739 1.000 139.783 0 149 SER BBB C   1 ? 4  
ATOM 1151  O O   . SER A 1 149 ? 27.739  75.080  66.784 1.000 144.962 0 149 SER BBB O   1 ? 4  
ATOM 1152  C CB  . SER A 1 149 ? 25.791  72.622  66.086 1.000 149.583 0 149 SER BBB CB  1 ? 4  
ATOM 1153  O OG  . SER A 1 149 ? 24.823  73.518  65.569 1.000 148.763 0 149 SER BBB OG  1 ? 4  
ATOM 1154  N N   . ILE A 1 150 ? 27.084  75.234  64.627 1.000 125.672 0 150 ILE BBB N   1 ? 4  
ATOM 1155  C CA  A ILE A 1 150 ? 27.283  76.683  64.574 1.000 126.485 0 150 ILE BBB CA  1 ? 4  
ATOM 1156  C C   . ILE A 1 150 ? 26.467  77.392  65.649 1.000 131.549 0 150 ILE BBB C   1 ? 4  
ATOM 1157  O O   . ILE A 1 150 ? 26.869  78.447  66.159 1.000 127.241 0 150 ILE BBB O   1 ? 4  
ATOM 1158  C CB  A ILE A 1 150 ? 26.947  77.209  63.163 1.000 123.593 0 150 ILE BBB CB  1 ? 4  
ATOM 1159  C CG1 A ILE A 1 150 ? 27.322  78.687  63.031 1.000 120.362 0 150 ILE BBB CG1 1 ? 4  
ATOM 1160  C CG2 A ILE A 1 150 ? 25.481  76.981  62.834 1.000 126.604 0 150 ILE BBB CG2 1 ? 4  
ATOM 1161  C CD1 A ILE A 1 150 ? 28.790  78.960  63.224 1.000 121.838 0 150 ILE BBB CD1 1 ? 4  
ATOM 1162  N N   . LEU A 1 151 ? 25.317  76.823  66.012 1.000 130.845 0 151 LEU BBB N   1 ? 4  
ATOM 1163  C CA  . LEU A 1 151 ? 24.489  77.332  67.099 1.000 134.336 0 151 LEU BBB CA  1 ? 4  
ATOM 1164  C C   . LEU A 1 151 ? 25.201  77.340  68.445 1.000 135.508 0 151 LEU BBB C   1 ? 4  
ATOM 1165  O O   . LEU A 1 151 ? 24.790  78.087  69.340 1.000 142.299 0 151 LEU BBB O   1 ? 4  
ATOM 1166  C CB  . LEU A 1 151 ? 23.195  76.533  67.191 1.000 134.460 0 151 LEU BBB CB  1 ? 4  
ATOM 1167  C CG  . LEU A 1 151 ? 22.391  76.588  65.894 1.000 135.794 0 151 LEU BBB CG  1 ? 4  
ATOM 1168  C CD1 . LEU A 1 151 ? 21.513  75.357  65.756 1.000 150.863 0 151 LEU BBB CD1 1 ? 4  
ATOM 1169  C CD2 . LEU A 1 151 ? 21.561  77.862  65.859 1.000 139.152 0 151 LEU BBB CD2 1 ? 4  
ATOM 1170  N N   . ASP A 1 152 ? 26.244  76.531  68.621 1.000 135.135 0 152 ASP BBB N   1 ? 4  
ATOM 1171  C CA  . ASP A 1 152 ? 26.953  76.470  69.890 1.000 138.220 0 152 ASP BBB CA  1 ? 4  
ATOM 1172  C C   . ASP A 1 152 ? 28.179  77.370  69.915 1.000 135.387 0 152 ASP BBB C   1 ? 4  
ATOM 1173  O O   . ASP A 1 152 ? 28.895  77.399  70.923 1.000 135.563 0 152 ASP BBB O   1 ? 4  
ATOM 1174  C CB  . ASP A 1 152 ? 27.382  75.024  70.176 1.000 144.389 0 152 ASP BBB CB  1 ? 4  
ATOM 1175  C CG  . ASP A 1 152 ? 26.203  74.102  70.440 1.000 156.791 0 152 ASP BBB CG  1 ? 4  
ATOM 1176  O OD1 . ASP A 1 152 ? 25.047  74.572  70.387 1.000 161.913 0 152 ASP BBB OD1 1 ? 4  
ATOM 1177  O OD2 . ASP A 1 152 ? 26.437  72.899  70.680 1.000 170.876 0 152 ASP BBB OD2 1 ? 4  
ATOM 1178  N N   . ILE A 1 153 ? 28.431  78.105  68.837 1.000 136.904 0 153 ILE BBB N   1 ? 4  
ATOM 1179  C CA  . ILE A 1 153 ? 29.506  79.085  68.799 1.000 129.078 0 153 ILE BBB CA  1 ? 4  
ATOM 1180  C C   . ILE A 1 153 ? 28.922  80.396  69.301 1.000 129.315 0 153 ILE BBB C   1 ? 4  
ATOM 1181  O O   . ILE A 1 153 ? 28.171  81.068  68.589 1.000 128.571 0 153 ILE BBB O   1 ? 4  
ATOM 1182  C CB  . ILE A 1 153 ? 30.101  79.239  67.397 1.000 112.315 0 153 ILE BBB CB  1 ? 4  
ATOM 1183  C CG1 . ILE A 1 153 ? 30.560  77.878  66.874 1.000 114.202 0 153 ILE BBB CG1 1 ? 4  
ATOM 1184  C CG2 . ILE A 1 153 ? 31.242  80.242  67.425 1.000 108.117 0 153 ILE BBB CG2 1 ? 4  
ATOM 1185  C CD1 . ILE A 1 153 ? 31.686  77.265  67.680 1.000 122.804 0 153 ILE BBB CD1 1 ? 4  
ATOM 1186  N N   . ARG A 1 154 ? 29.275  80.762  70.520 1.000 126.172 0 154 ARG BBB N   1 ? 4  
ATOM 1187  C CA  . ARG A 1 154 ? 28.774  81.968  71.146 1.000 124.839 0 154 ARG BBB CA  1 ? 4  
ATOM 1188  C C   . ARG A 1 154 ? 29.976  82.750  71.629 1.000 122.006 0 154 ARG BBB C   1 ? 4  
ATOM 1189  O O   . ARG A 1 154 ? 30.917  82.173  72.182 1.000 125.947 0 154 ARG BBB O   1 ? 4  
ATOM 1190  C CB  . ARG A 1 154 ? 27.852  81.644  72.333 1.000 138.972 0 154 ARG BBB CB  1 ? 4  
ATOM 1191  C CG  . ARG A 1 154 ? 26.816  82.708  72.684 1.000 155.839 0 154 ARG BBB CG  1 ? 4  
ATOM 1192  C CD  . ARG A 1 154 ? 25.689  82.121  73.540 1.000 167.195 0 154 ARG BBB CD  1 ? 4  
ATOM 1193  N NE  . ARG A 1 154 ? 25.172  80.875  72.986 1.000 173.322 0 154 ARG BBB NE  1 ? 4  
ATOM 1194  C CZ  . ARG A 1 154 ? 24.162  80.793  72.131 1.000 178.289 0 154 ARG BBB CZ  1 ? 4  
ATOM 1195  N NH1 . ARG A 1 154 ? 23.525  81.872  71.707 1.000 176.524 0 154 ARG BBB NH1 1 ? 4  
ATOM 1196  N NH2 . ARG A 1 154 ? 23.788  79.598  71.682 1.000 184.440 0 154 ARG BBB NH2 1 ? 4  
ATOM 1197  N N   . GLN A 1 155 ? 29.943  84.061  71.424 1.000 118.719 0 155 GLN BBB N   1 ? 4  
ATOM 1198  C CA  . GLN A 1 155 ? 31.082  84.883  71.790 1.000 124.123 0 155 GLN BBB CA  1 ? 4  
ATOM 1199  C C   . GLN A 1 155 ? 31.194  84.932  73.304 1.000 133.820 0 155 GLN BBB C   1 ? 4  
ATOM 1200  O O   . GLN A 1 155 ? 30.212  85.186  74.003 1.000 150.289 0 155 GLN BBB O   1 ? 4  
ATOM 1201  C CB  . GLN A 1 155 ? 30.942  86.284  71.200 1.000 124.829 0 155 GLN BBB CB  1 ? 4  
ATOM 1202  C CG  . GLN A 1 155 ? 32.175  87.147  71.358 1.000 131.033 0 155 GLN BBB CG  1 ? 4  
ATOM 1203  C CD  . GLN A 1 155 ? 31.965  88.569  70.874 1.000 132.693 0 155 GLN BBB CD  1 ? 4  
ATOM 1204  O OE1 . GLN A 1 155 ? 30.836  89.010  70.656 1.000 137.218 0 155 GLN BBB OE1 1 ? 4  
ATOM 1205  N NE2 . GLN A 1 155 ? 33.059  89.304  70.725 1.000 132.990 0 155 GLN BBB NE2 1 ? 4  
ATOM 1206  N N   . GLY A 1 156 ? 32.400  84.686  73.805 1.000 149.525 0 156 GLY BBB N   1 ? 4  
ATOM 1207  C CA  . GLY A 1 156 ? 32.644  84.782  75.218 1.000 161.437 0 156 GLY BBB CA  1 ? 4  
ATOM 1208  C C   . GLY A 1 156 ? 32.592  86.228  75.642 1.000 167.990 0 156 GLY BBB C   1 ? 4  
ATOM 1209  O O   . GLY A 1 156 ? 32.732  87.147  74.827 1.000 170.107 0 156 GLY BBB O   1 ? 4  
ATOM 1210  N N   . PRO A 1 157 ? 32.361  86.459  76.932 1.000 163.809 0 157 PRO BBB N   1 ? 4  
ATOM 1211  C CA  A PRO A 1 157 ? 32.227  87.847  77.393 1.000 157.707 0 157 PRO BBB CA  1 ? 4  
ATOM 1212  C C   . PRO A 1 157 ? 33.502  88.641  77.198 1.000 160.833 0 157 PRO BBB C   1 ? 4  
ATOM 1213  O O   . PRO A 1 157 ? 33.450  89.834  76.877 1.000 154.826 0 157 PRO BBB O   1 ? 4  
ATOM 1214  C CB  A PRO A 1 157 ? 31.856  87.697  78.876 1.000 164.164 0 157 PRO BBB CB  1 ? 4  
ATOM 1215  C CG  A PRO A 1 157 ? 31.494  86.252  79.075 1.000 164.512 0 157 PRO BBB CG  1 ? 4  
ATOM 1216  C CD  A PRO A 1 157 ? 32.170  85.470  78.005 1.000 161.962 0 157 PRO BBB CD  1 ? 4  
ATOM 1217  N N   . LYS A 1 158 ? 34.653  88.001  77.386 1.000 177.640 0 158 LYS BBB N   1 ? 4  
ATOM 1218  C CA  . LYS A 1 158 ? 35.952  88.634  77.214 1.000 187.636 0 158 LYS BBB CA  1 ? 4  
ATOM 1219  C C   . LYS A 1 158 ? 36.634  88.274  75.896 1.000 186.500 0 158 LYS BBB C   1 ? 4  
ATOM 1220  O O   . LYS A 1 158 ? 37.796  88.639  75.700 1.000 194.983 0 158 LYS BBB O   1 ? 4  
ATOM 1221  C CB  . LYS A 1 158 ? 36.859  88.241  78.377 1.000 208.879 0 158 LYS BBB CB  1 ? 4  
ATOM 1222  C CG  . LYS A 1 158 ? 37.366  86.813  78.258 1.000 224.894 0 158 LYS BBB CG  1 ? 4  
ATOM 1223  C CD  . LYS A 1 158 ? 37.545  86.157  79.608 1.000 242.406 0 158 LYS BBB CD  1 ? 4  
ATOM 1224  C CE  . LYS A 1 158 ? 37.607  84.646  79.457 1.000 247.287 0 158 LYS BBB CE  1 ? 4  
ATOM 1225  N NZ  . LYS A 1 158 ? 36.384  84.096  78.807 1.000 245.841 0 158 LYS BBB NZ  1 ? 4  
ATOM 1226  N N   . GLU A 1 159 ? 35.946  87.594  74.984 1.000 170.671 0 159 GLU BBB N   1 ? 4  
ATOM 1227  C CA  . GLU A 1 159 ? 36.581  87.169  73.737 1.000 156.556 0 159 GLU BBB CA  1 ? 4  
ATOM 1228  C C   . GLU A 1 159 ? 36.609  88.310  72.726 1.000 145.759 0 159 GLU BBB C   1 ? 4  
ATOM 1229  O O   . GLU A 1 159 ? 35.554  88.882  72.428 1.000 143.610 0 159 GLU BBB O   1 ? 4  
ATOM 1230  C CB  . GLU A 1 159 ? 35.866  85.961  73.146 1.000 153.341 0 159 GLU BBB CB  1 ? 4  
ATOM 1231  C CG  . GLU A 1 159 ? 36.550  85.419  71.901 1.000 151.888 0 159 GLU BBB CG  1 ? 4  
ATOM 1232  C CD  . GLU A 1 159 ? 35.849  84.210  71.315 1.000 150.818 0 159 GLU BBB CD  1 ? 4  
ATOM 1233  O OE1 . GLU A 1 159 ? 34.663  83.989  71.635 1.000 150.106 0 159 GLU BBB OE1 1 ? 4  
ATOM 1234  O OE2 . GLU A 1 159 ? 36.489  83.477  70.532 1.000 149.150 0 159 GLU BBB OE2 1 ? 4  
ATOM 1235  N N   . PRO A 1 160 ? 37.776  88.679  72.194 1.000 133.386 0 160 PRO BBB N   1 ? 4  
ATOM 1236  C CA  . PRO A 1 160 ? 37.820  89.662  71.105 1.000 126.021 0 160 PRO BBB CA  1 ? 4  
ATOM 1237  C C   . PRO A 1 160 ? 36.940  89.233  69.941 1.000 128.461 0 160 PRO BBB C   1 ? 4  
ATOM 1238  O O   . PRO A 1 160 ? 36.902  88.059  69.570 1.000 140.537 0 160 PRO BBB O   1 ? 4  
ATOM 1239  C CB  . PRO A 1 160 ? 39.301  89.686  70.713 1.000 125.394 0 160 PRO BBB CB  1 ? 4  
ATOM 1240  C CG  . PRO A 1 160 ? 40.018  89.256  71.938 1.000 135.764 0 160 PRO BBB CG  1 ? 4  
ATOM 1241  C CD  . PRO A 1 160 ? 39.123  88.246  72.602 1.000 139.904 0 160 PRO BBB CD  1 ? 4  
ATOM 1242  N N   . PHE A 1 161 ? 36.221  90.204  69.369 1.000 122.800 0 161 PHE BBB N   1 ? 4  
ATOM 1243  C CA  . PHE A 1 161 ? 35.310  89.905  68.269 1.000 117.595 0 161 PHE BBB CA  1 ? 4  
ATOM 1244  C C   . PHE A 1 161 ? 36.010  89.187  67.119 1.000 114.401 0 161 PHE BBB C   1 ? 4  
ATOM 1245  O O   . PHE A 1 161 ? 35.471  88.224  66.562 1.000 111.146 0 161 PHE BBB O   1 ? 4  
ATOM 1246  C CB  . PHE A 1 161 ? 34.679  91.210  67.772 1.000 118.591 0 161 PHE BBB CB  1 ? 4  
ATOM 1247  C CG  . PHE A 1 161 ? 33.565  91.013  66.782 1.000 120.740 0 161 PHE BBB CG  1 ? 4  
ATOM 1248  C CD1 . PHE A 1 161 ? 32.705  89.933  66.880 1.000 123.610 0 161 PHE BBB CD1 1 ? 4  
ATOM 1249  C CD2 . PHE A 1 161 ? 33.408  91.893  65.721 1.000 120.480 0 161 PHE BBB CD2 1 ? 4  
ATOM 1250  C CE1 . PHE A 1 161 ? 31.682  89.754  65.958 1.000 119.723 0 161 PHE BBB CE1 1 ? 4  
ATOM 1251  C CE2 . PHE A 1 161 ? 32.397  91.715  64.793 1.000 117.953 0 161 PHE BBB CE2 1 ? 4  
ATOM 1252  C CZ  . PHE A 1 161 ? 31.534  90.645  64.910 1.000 117.234 0 161 PHE BBB CZ  1 ? 4  
ATOM 1253  N N   . ARG A 1 162 ? 37.233  89.612  66.783 1.000 114.675 0 162 ARG BBB N   1 ? 4  
ATOM 1254  C CA  . ARG A 1 162 ? 37.986  88.968  65.705 1.000 113.506 0 162 ARG BBB CA  1 ? 4  
ATOM 1255  C C   . ARG A 1 162 ? 38.185  87.474  65.950 1.000 111.163 0 162 ARG BBB C   1 ? 4  
ATOM 1256  O O   . ARG A 1 162 ? 38.076  86.672  65.016 1.000 117.800 0 162 ARG BBB O   1 ? 4  
ATOM 1257  C CB  . ARG A 1 162 ? 39.299  89.720  65.465 1.000 117.388 0 162 ARG BBB CB  1 ? 4  
ATOM 1258  C CG  . ARG A 1 162 ? 40.118  89.258  64.264 1.000 118.421 0 162 ARG BBB CG  1 ? 4  
ATOM 1259  C CD  . ARG A 1 162 ? 41.508  89.879  64.327 1.000 123.596 0 162 ARG BBB CD  1 ? 4  
ATOM 1260  N NE  . ARG A 1 162 ? 41.353  91.326  64.449 1.000 139.159 0 162 ARG BBB NE  1 ? 4  
ATOM 1261  C CZ  . ARG A 1 162 ? 42.351  92.194  64.579 1.000 146.363 0 162 ARG BBB CZ  1 ? 4  
ATOM 1262  N NH1 . ARG A 1 162 ? 43.616  91.774  64.564 1.000 135.452 0 162 ARG BBB NH1 1 ? 4  
ATOM 1263  N NH2 . ARG A 1 162 ? 42.071  93.495  64.686 1.000 143.834 0 162 ARG BBB NH2 1 ? 4  
ATOM 1264  N N   . ASP A 1 163 ? 38.494  87.082  67.187 1.000 112.033 0 163 ASP BBB N   1 ? 4  
ATOM 1265  C CA  . ASP A 1 163 ? 38.717  85.671  67.490 1.000 114.536 0 163 ASP BBB CA  1 ? 4  
ATOM 1266  C C   . ASP A 1 163 ? 37.418  84.871  67.425 1.000 116.337 0 163 ASP BBB C   1 ? 4  
ATOM 1267  O O   . ASP A 1 163 ? 37.412  83.718  66.977 1.000 120.139 0 163 ASP BBB O   1 ? 4  
ATOM 1268  C CB  . ASP A 1 163 ? 39.358  85.516  68.873 1.000 125.146 0 163 ASP BBB CB  1 ? 4  
ATOM 1269  C CG  . ASP A 1 163 ? 40.741  86.145  68.967 1.000 133.414 0 163 ASP BBB CG  1 ? 4  
ATOM 1270  O OD1 . ASP A 1 163 ? 41.435  86.246  67.931 1.000 142.398 0 163 ASP BBB OD1 1 ? 4  
ATOM 1271  O OD2 . ASP A 1 163 ? 41.125  86.554  70.085 1.000 125.508 0 163 ASP BBB OD2 1 ? 4  
ATOM 1272  N N   . TYR A 1 164 ? 36.310  85.472  67.866 1.000 112.657 0 164 TYR BBB N   1 ? 4  
ATOM 1273  C CA  . TYR A 1 164 ? 34.995  84.840  67.770 1.000 109.696 0 164 TYR BBB CA  1 ? 4  
ATOM 1274  C C   . TYR A 1 164 ? 34.581  84.607  66.316 1.000 110.357 0 164 TYR BBB C   1 ? 4  
ATOM 1275  O O   . TYR A 1 164 ? 34.103  83.519  65.968 1.000 113.242 0 164 TYR BBB O   1 ? 4  
ATOM 1276  C CB  . TYR A 1 164 ? 33.970  85.686  68.535 1.000 109.544 0 164 TYR BBB CB  1 ? 4  
ATOM 1277  C CG  . TYR A 1 164 ? 32.527  85.519  68.122 1.000 111.501 0 164 TYR BBB CG  1 ? 4  
ATOM 1278  C CD1 . TYR A 1 164 ? 31.867  84.311  68.314 1.000 114.022 0 164 TYR BBB CD1 1 ? 4  
ATOM 1279  C CD2 . TYR A 1 164 ? 31.811  86.577  67.580 1.000 109.931 0 164 TYR BBB CD2 1 ? 4  
ATOM 1280  C CE1 . TYR A 1 164 ? 30.544  84.153  67.948 1.000 108.847 0 164 TYR BBB CE1 1 ? 4  
ATOM 1281  C CE2 . TYR A 1 164 ? 30.486  86.429  67.212 1.000 106.482 0 164 TYR BBB CE2 1 ? 4  
ATOM 1282  C CZ  . TYR A 1 164 ? 29.859  85.214  67.399 1.000 106.722 0 164 TYR BBB CZ  1 ? 4  
ATOM 1283  O OH  . TYR A 1 164 ? 28.543  85.054  67.035 1.000 106.776 0 164 TYR BBB OH  1 ? 4  
ATOM 1284  N N   . VAL A 1 165 ? 34.774  85.605  65.449 1.000 106.600 0 165 VAL BBB N   1 ? 4  
ATOM 1285  C CA  . VAL A 1 165 ? 34.412  85.459  64.038 1.000 103.321 0 165 VAL BBB CA  1 ? 4  
ATOM 1286  C C   . VAL A 1 165 ? 35.221  84.349  63.375 1.000 103.243 0 165 VAL BBB C   1 ? 4  
ATOM 1287  O O   . VAL A 1 165 ? 34.685  83.563  62.584 1.000 100.561 0 165 VAL BBB O   1 ? 4  
ATOM 1288  C CB  . VAL A 1 165 ? 34.597  86.801  63.302 1.000 104.561 0 165 VAL BBB CB  1 ? 4  
ATOM 1289  C CG1 . VAL A 1 165 ? 34.266  86.658  61.827 1.000 117.205 0 165 VAL BBB CG1 1 ? 4  
ATOM 1290  C CG2 . VAL A 1 165 ? 33.724  87.865  63.917 1.000 105.749 0 165 VAL BBB CG2 1 ? 4  
ATOM 1291  N N   . ASP A 1 166 ? 36.513  84.252  63.699 1.000 116.267 0 166 ASP BBB N   1 ? 4  
ATOM 1292  C CA  . ASP A 1 166 ? 37.318  83.130  63.219 1.000 120.859 0 166 ASP BBB CA  1 ? 4  
ATOM 1293  C C   . ASP A 1 166 ? 36.693  81.789  63.598 1.000 122.237 0 166 ASP BBB C   1 ? 4  
ATOM 1294  O O   . ASP A 1 166 ? 36.568  80.893  62.754 1.000 128.361 0 166 ASP BBB O   1 ? 4  
ATOM 1295  C CB  . ASP A 1 166 ? 38.745  83.237  63.768 1.000 123.539 0 166 ASP BBB CB  1 ? 4  
ATOM 1296  C CG  . ASP A 1 166 ? 39.608  84.223  62.988 1.000 129.425 0 166 ASP BBB CG  1 ? 4  
ATOM 1297  O OD1 . ASP A 1 166 ? 39.602  84.169  61.738 1.000 132.483 0 166 ASP BBB OD1 1 ? 4  
ATOM 1298  O OD2 . ASP A 1 166 ? 40.320  85.030  63.627 1.000 130.631 0 166 ASP BBB OD2 1 ? 4  
ATOM 1299  N N   . ARG A 1 167 ? 36.277  81.635  64.859 1.000 109.781 0 167 ARG BBB N   1 ? 4  
ATOM 1300  C CA  . ARG A 1 167 ? 35.666  80.378  65.287 1.000 107.518 0 167 ARG BBB CA  1 ? 4  
ATOM 1301  C C   . ARG A 1 167 ? 34.348  80.139  64.565 1.000 104.104 0 167 ARG BBB C   1 ? 4  
ATOM 1302  O O   . ARG A 1 167 ? 34.024  79.002  64.199 1.000 104.678 0 167 ARG BBB O   1 ? 4  
ATOM 1303  C CB  . ARG A 1 167 ? 35.462  80.347  66.801 1.000 109.066 0 167 ARG BBB CB  1 ? 4  
ATOM 1304  C CG  . ARG A 1 167 ? 36.757  80.292  67.586 1.000 114.312 0 167 ARG BBB CG  1 ? 4  
ATOM 1305  C CD  . ARG A 1 167 ? 36.508  79.977  69.049 1.000 120.360 0 167 ARG BBB CD  1 ? 4  
ATOM 1306  N NE  . ARG A 1 167 ? 35.571  80.902  69.671 1.000 117.073 0 167 ARG BBB NE  1 ? 4  
ATOM 1307  C CZ  . ARG A 1 167 ? 34.361  80.562  70.093 1.000 116.181 0 167 ARG BBB CZ  1 ? 4  
ATOM 1308  N NH1 . ARG A 1 167 ? 33.911  79.322  69.977 1.000 119.840 0 167 ARG BBB NH1 1 ? 4  
ATOM 1309  N NH2 . ARG A 1 167 ? 33.581  81.489  70.640 1.000 116.196 0 167 ARG BBB NH2 1 ? 4  
ATOM 1310  N N   . PHE A 1 168 ? 33.571  81.202  64.370 1.000 101.013 0 168 PHE BBB N   1 ? 4  
ATOM 1311  C CA  . PHE A 1 168 ? 32.255  81.083  63.754 1.000 102.719 0 168 PHE BBB CA  1 ? 4  
ATOM 1312  C C   . PHE A 1 168 ? 32.361  80.518  62.341 1.000 102.681 0 168 PHE BBB C   1 ? 4  
ATOM 1313  O O   . PHE A 1 168 ? 31.732  79.504  62.017 1.000 104.874 0 168 PHE BBB O   1 ? 4  
ATOM 1314  C CB  . PHE A 1 168 ? 31.579  82.457  63.756 1.000 102.138 0 168 PHE BBB CB  1 ? 4  
ATOM 1315  C CG  . PHE A 1 168 ? 30.152  82.450  63.279 1.000 102.066 0 168 PHE BBB CG  1 ? 4  
ATOM 1316  C CD1 . PHE A 1 168 ? 29.842  82.596  61.938 1.000 102.488 0 168 PHE BBB CD1 1 ? 4  
ATOM 1317  C CD2 . PHE A 1 168 ? 29.116  82.313  64.187 1.000 108.874 0 168 PHE BBB CD2 1 ? 4  
ATOM 1318  C CE1 . PHE A 1 168 ? 28.528  82.601  61.517 1.000 101.975 0 168 PHE BBB CE1 1 ? 4  
ATOM 1319  C CE2 . PHE A 1 168 ? 27.802  82.313  63.769 1.000 106.585 0 168 PHE BBB CE2 1 ? 4  
ATOM 1320  C CZ  . PHE A 1 168 ? 27.508  82.456  62.433 1.000 102.887 0 168 PHE BBB CZ  1 ? 4  
ATOM 1321  N N   . TYR A 1 169 ? 33.200  81.125  61.504 1.000 100.095 0 169 TYR BBB N   1 ? 4  
ATOM 1322  C CA  . TYR A 1 169 ? 33.314  80.700  60.113 1.000 100.181 0 169 TYR BBB CA  1 ? 4  
ATOM 1323  C C   . TYR A 1 169 ? 34.080  79.400  59.928 1.000 99.658  0 169 TYR BBB C   1 ? 4  
ATOM 1324  O O   . TYR A 1 169 ? 33.867  78.721  58.919 1.000 101.791 0 169 TYR BBB O   1 ? 4  
ATOM 1325  C CB  . TYR A 1 169 ? 34.000  81.788  59.299 1.000 103.876 0 169 TYR BBB CB  1 ? 4  
ATOM 1326  C CG  . TYR A 1 169 ? 33.107  82.957  58.999 1.000 109.669 0 169 TYR BBB CG  1 ? 4  
ATOM 1327  C CD1 . TYR A 1 169 ? 31.776  82.772  58.649 1.000 107.984 0 169 TYR BBB CD1 1 ? 4  
ATOM 1328  C CD2 . TYR A 1 169 ? 33.591  84.249  59.079 1.000 112.969 0 169 TYR BBB CD2 1 ? 4  
ATOM 1329  C CE1 . TYR A 1 169 ? 30.960  83.852  58.372 1.000 101.390 0 169 TYR BBB CE1 1 ? 4  
ATOM 1330  C CE2 . TYR A 1 169 ? 32.788  85.327  58.810 1.000 105.795 0 169 TYR BBB CE2 1 ? 4  
ATOM 1331  C CZ  . TYR A 1 169 ? 31.478  85.129  58.457 1.000 102.619 0 169 TYR BBB CZ  1 ? 4  
ATOM 1332  O OH  . TYR A 1 169 ? 30.706  86.233  58.194 1.000 106.143 0 169 TYR BBB OH  1 ? 4  
ATOM 1333  N N   . LYS A 1 170 ? 34.950  79.030  60.870 1.000 99.231  0 170 LYS BBB N   1 ? 4  
ATOM 1334  C CA  . LYS A 1 170 ? 35.557  77.703  60.830 1.000 97.162  0 170 LYS BBB CA  1 ? 4  
ATOM 1335  C C   . LYS A 1 170 ? 34.494  76.619  60.954 1.000 114.647 0 170 LYS BBB C   1 ? 4  
ATOM 1336  O O   . LYS A 1 170 ? 34.491  75.644  60.191 1.000 121.596 0 170 LYS BBB O   1 ? 4  
ATOM 1337  C CB  . LYS A 1 170 ? 36.606  77.566  61.933 1.000 98.112  0 170 LYS BBB CB  1 ? 4  
ATOM 1338  C CG  . LYS A 1 170 ? 37.229  76.178  62.021 1.000 111.635 0 170 LYS BBB CG  1 ? 4  
ATOM 1339  C CD  . LYS A 1 170 ? 38.175  75.891  60.864 1.000 131.337 0 170 LYS BBB CD  1 ? 4  
ATOM 1340  C CE  . LYS A 1 170 ? 39.113  74.727  61.176 1.000 135.965 0 170 LYS BBB CE  1 ? 4  
ATOM 1341  N NZ  . LYS A 1 170 ? 40.255  75.095  62.062 1.000 126.931 0 170 LYS BBB NZ  1 ? 4  
ATOM 1342  N N   . THR A 1 171 ? 33.595  76.762  61.927 1.000 117.817 0 171 THR BBB N   1 ? 4  
ATOM 1343  C CA  . THR A 1 171 ? 32.498  75.813  62.077 1.000 113.737 0 171 THR BBB CA  1 ? 4  
ATOM 1344  C C   . THR A 1 171 ? 31.595  75.814  60.847 1.000 117.776 0 171 THR BBB C   1 ? 4  
ATOM 1345  O O   . THR A 1 171 ? 31.193  74.752  60.356 1.000 122.854 0 171 THR BBB O   1 ? 4  
ATOM 1346  C CB  . THR A 1 171 ? 31.711  76.156  63.337 1.000 109.798 0 171 THR BBB CB  1 ? 4  
ATOM 1347  O OG1 . THR A 1 171 ? 32.591  76.083  64.465 1.000 102.426 0 171 THR BBB OG1 1 ? 4  
ATOM 1348  C CG2 . THR A 1 171 ? 30.559  75.200  63.527 1.000 130.394 0 171 THR BBB CG2 1 ? 4  
ATOM 1349  N N   . LEU A 1 172 ? 31.249  77.002  60.349 1.000 113.905 0 172 LEU BBB N   1 ? 4  
ATOM 1350  C CA  . LEU A 1 172 ? 30.406  77.093  59.161 1.000 122.244 0 172 LEU BBB CA  1 ? 4  
ATOM 1351  C C   . LEU A 1 172 ? 31.055  76.400  57.968 1.000 129.492 0 172 LEU BBB C   1 ? 4  
ATOM 1352  O O   . LEU A 1 172 ? 30.379  75.720  57.185 1.000 144.603 0 172 LEU BBB O   1 ? 4  
ATOM 1353  C CB  . LEU A 1 172 ? 30.133  78.557  58.831 1.000 117.700 0 172 LEU BBB CB  1 ? 4  
ATOM 1354  C CG  . LEU A 1 172 ? 28.698  79.033  59.022 1.000 135.122 0 172 LEU BBB CG  1 ? 4  
ATOM 1355  C CD1 . LEU A 1 172 ? 28.631  80.519  58.745 1.000 144.457 0 172 LEU BBB CD1 1 ? 4  
ATOM 1356  C CD2 . LEU A 1 172 ? 27.738  78.264  58.140 1.000 152.065 0 172 LEU BBB CD2 1 ? 4  
ATOM 1357  N N   . ARG A 1 173 ? 32.372  76.567  57.821 1.000 115.942 0 173 ARG BBB N   1 ? 4  
ATOM 1358  C CA  . ARG A 1 173 ? 33.114  75.947  56.724 1.000 116.378 0 173 ARG BBB CA  1 ? 4  
ATOM 1359  C C   . ARG A 1 173 ? 33.039  74.426  56.798 1.000 123.156 0 173 ARG BBB C   1 ? 4  
ATOM 1360  O O   . ARG A 1 173 ? 32.939  73.755  55.769 1.000 149.785 0 173 ARG BBB O   1 ? 4  
ATOM 1361  C CB  . ARG A 1 173 ? 34.556  76.438  56.639 1.000 117.423 0 173 ARG BBB CB  1 ? 4  
ATOM 1362  C CG  . ARG A 1 173 ? 35.162  75.931  55.332 1.000 125.550 0 173 ARG BBB CG  1 ? 4  
ATOM 1363  C CD  . ARG A 1 173 ? 36.257  76.809  54.757 1.000 120.928 0 173 ARG BBB CD  1 ? 4  
ATOM 1364  N NE  . ARG A 1 173 ? 37.576  76.198  54.812 1.000 124.524 0 173 ARG BBB NE  1 ? 4  
ATOM 1365  C CZ  . ARG A 1 173 ? 38.690  76.809  54.433 1.000 125.314 0 173 ARG BBB CZ  1 ? 4  
ATOM 1366  N NH1 . ARG A 1 173 ? 38.651  78.051  53.962 1.000 121.139 0 173 ARG BBB NH1 1 ? 4  
ATOM 1367  N NH2 . ARG A 1 173 ? 39.843  76.153  54.497 1.000 124.776 0 173 ARG BBB NH2 1 ? 4  
ATOM 1368  N N   . ALA A 1 174 ? 33.134  73.856  57.998 1.000 113.072 0 174 ALA BBB N   1 ? 4  
ATOM 1369  C CA  . ALA A 1 174 ? 33.108  72.400  58.119 1.000 130.505 0 174 ALA BBB CA  1 ? 4  
ATOM 1370  C C   . ALA A 1 174 ? 31.750  71.861  57.688 1.000 145.959 0 174 ALA BBB C   1 ? 4  
ATOM 1371  O O   . ALA A 1 174 ? 31.660  70.777  57.098 1.000 163.900 0 174 ALA BBB O   1 ? 4  
ATOM 1372  C CB  . ALA A 1 174 ? 33.433  71.982  59.552 1.000 126.013 0 174 ALA BBB CB  1 ? 4  
ATOM 1373  N N   . GLU A 1 175 ? 30.687  72.595  57.982 1.000 140.112 0 175 GLU BBB N   1 ? 4  
ATOM 1374  C CA  . GLU A 1 175 ? 29.324  72.198  57.662 1.000 150.271 0 175 GLU BBB CA  1 ? 4  
ATOM 1375  C C   . GLU A 1 175 ? 29.218  72.306  56.137 1.000 164.031 0 175 GLU BBB C   1 ? 4  
ATOM 1376  O O   . GLU A 1 175 ? 28.556  73.209  55.621 1.000 154.071 0 175 GLU BBB O   1 ? 4  
ATOM 1377  C CB  . GLU A 1 175 ? 28.342  73.147  58.342 1.000 158.012 0 175 GLU BBB CB  1 ? 4  
ATOM 1378  C CG  . GLU A 1 175 ? 28.425  73.146  59.879 1.000 163.379 0 175 GLU BBB CG  1 ? 4  
ATOM 1379  C CD  . GLU A 1 175 ? 27.693  72.002  60.547 1.000 176.771 0 175 GLU BBB CD  1 ? 4  
ATOM 1380  O OE1 . GLU A 1 175 ? 26.608  71.613  60.070 1.000 193.207 0 175 GLU BBB OE1 1 ? 4  
ATOM 1381  O OE2 . GLU A 1 175 ? 28.210  71.487  61.561 1.000 164.112 0 175 GLU BBB OE2 1 ? 4  
ATOM 1382  N N   . GLN A 1 176 ? 29.841  71.357  55.421 1.000 193.021 0 176 GLN BBB N   1 ? 4  
ATOM 1383  C CA  . GLN A 1 176 ? 29.758  71.206  53.953 1.000 210.115 0 176 GLN BBB CA  1 ? 4  
ATOM 1384  C C   . GLN A 1 176 ? 30.143  72.499  53.237 1.000 217.705 0 176 GLN BBB C   1 ? 4  
ATOM 1385  O O   . GLN A 1 176 ? 29.453  72.980  52.337 1.000 246.980 0 176 GLN BBB O   1 ? 4  
ATOM 1386  C CB  . GLN A 1 176 ? 28.367  70.750  53.501 1.000 228.283 0 176 GLN BBB CB  1 ? 4  
ATOM 1387  C CG  . GLN A 1 176 ? 28.378  69.894  52.216 1.000 234.349 0 176 GLN BBB CG  1 ? 4  
ATOM 1388  C CD  . GLN A 1 176 ? 28.080  70.683  50.946 1.000 244.970 0 176 GLN BBB CD  1 ? 4  
ATOM 1389  O OE1 . GLN A 1 176 ? 27.249  71.591  50.947 1.000 256.227 0 176 GLN BBB OE1 1 ? 4  
ATOM 1390  N NE2 . GLN A 1 176 ? 28.760  70.336  49.856 1.000 240.783 0 176 GLN BBB NE2 1 ? 4  
ATOM 1391  N N   . ALA A 1 177 ? 31.298  73.032  53.636 1.000 179.489 0 177 ALA BBB N   1 ? 4  
ATOM 1392  C CA  . ALA A 1 177 ? 32.020  74.151  53.033 1.000 176.706 0 177 ALA BBB CA  1 ? 4  
ATOM 1393  C C   . ALA A 1 177 ? 31.204  75.427  52.854 1.000 193.084 0 177 ALA BBB C   1 ? 4  
ATOM 1394  O O   . ALA A 1 177 ? 29.976  75.433  52.996 1.000 225.616 0 177 ALA BBB O   1 ? 4  
ATOM 1395  C CB  . ALA A 1 177 ? 32.567  73.722  51.668 1.000 179.341 0 177 ALA BBB CB  1 ? 4  
ATOM 1396  N N   . SER A 1 178 ? 31.906  76.529  52.586 1.000 183.324 0 178 SER BBB N   1 ? 4  
ATOM 1397  C CA  . SER A 1 178 ? 31.263  77.820  52.372 1.000 204.388 0 178 SER BBB CA  1 ? 4  
ATOM 1398  C C   . SER A 1 178 ? 30.358  77.798  51.144 1.000 234.190 0 178 SER BBB C   1 ? 4  
ATOM 1399  O O   . SER A 1 178 ? 30.669  77.160  50.134 1.000 254.103 0 178 SER BBB O   1 ? 4  
ATOM 1400  C CB  . SER A 1 178 ? 32.307  78.932  52.251 1.000 186.970 0 178 SER BBB CB  1 ? 4  
ATOM 1401  O OG  . SER A 1 178 ? 32.902  79.183  53.511 1.000 167.428 0 178 SER BBB OG  1 ? 4  
ATOM 1402  N N   . GLN A 1 179 ? 29.273  78.566  51.211 1.000 249.922 0 179 GLN BBB N   1 ? 4  
ATOM 1403  C CA  . GLN A 1 179 ? 28.399  78.815  50.071 1.000 266.969 0 179 GLN BBB CA  1 ? 4  
ATOM 1404  C C   . GLN A 1 179 ? 27.659  80.125  50.316 1.000 286.737 0 179 GLN BBB C   1 ? 4  
ATOM 1405  O O   . GLN A 1 179 ? 27.865  80.804  51.325 1.000 279.150 0 179 GLN BBB O   1 ? 4  
ATOM 1406  C CB  . GLN A 1 179 ? 27.380  77.684  49.825 1.000 268.844 0 179 GLN BBB CB  1 ? 4  
ATOM 1407  C CG  . GLN A 1 179 ? 27.878  76.455  49.060 1.000 274.692 0 179 GLN BBB CG  1 ? 4  
ATOM 1408  C CD  . GLN A 1 179 ? 28.149  75.249  49.948 1.000 281.038 0 179 GLN BBB CD  1 ? 4  
ATOM 1409  O OE1 . GLN A 1 179 ? 27.745  75.210  51.110 1.000 292.300 0 179 GLN BBB OE1 1 ? 4  
ATOM 1410  N NE2 . GLN A 1 179 ? 28.843  74.258  49.398 1.000 284.330 0 179 GLN BBB NE2 1 ? 4  
ATOM 1411  N N   . GLU A 1 180 ? 26.773  80.456  49.379 1.000 308.158 0 180 GLU BBB N   1 ? 4  
ATOM 1412  C CA  . GLU A 1 180 ? 25.841  81.573  49.496 1.000 314.132 0 180 GLU BBB CA  1 ? 4  
ATOM 1413  C C   . GLU A 1 180 ? 24.779  81.251  50.535 1.000 315.285 0 180 GLU BBB C   1 ? 4  
ATOM 1414  O O   . GLU A 1 180 ? 24.221  82.165  51.156 1.000 315.184 0 180 GLU BBB O   1 ? 4  
ATOM 1415  C CB  . GLU A 1 180 ? 25.257  81.982  48.150 1.000 314.083 0 180 GLU BBB CB  1 ? 4  
ATOM 1416  C CG  . GLU A 1 180 ? 26.195  82.949  47.423 1.000 299.313 0 180 GLU BBB CG  1 ? 4  
ATOM 1417  C CD  . GLU A 1 180 ? 26.292  84.311  48.102 1.000 292.593 0 180 GLU BBB CD  1 ? 4  
ATOM 1418  O OE1 . GLU A 1 180 ? 25.319  84.730  48.762 1.000 290.208 0 180 GLU BBB OE1 1 ? 4  
ATOM 1419  O OE2 . GLU A 1 180 ? 27.352  84.963  47.971 1.000 290.574 0 180 GLU BBB OE2 1 ? 4  
ATOM 1420  N N   . VAL A 1 181 ? 24.449  79.968  50.671 1.000 301.651 0 181 VAL BBB N   1 ? 4  
ATOM 1421  C CA  . VAL A 1 181 ? 23.475  79.522  51.659 1.000 279.501 0 181 VAL BBB CA  1 ? 4  
ATOM 1422  C C   . VAL A 1 181 ? 23.976  79.887  53.052 1.000 271.737 0 181 VAL BBB C   1 ? 4  
ATOM 1423  O O   . VAL A 1 181 ? 23.207  80.363  53.897 1.000 252.026 0 181 VAL BBB O   1 ? 4  
ATOM 1424  C CB  . VAL A 1 181 ? 23.243  78.002  51.521 1.000 267.678 0 181 VAL BBB CB  1 ? 4  
ATOM 1425  C CG1 . VAL A 1 181 ? 22.395  77.474  52.669 1.000 255.915 0 181 VAL BBB CG1 1 ? 4  
ATOM 1426  C CG2 . VAL A 1 181 ? 22.626  77.666  50.172 1.000 256.021 0 181 VAL BBB CG2 1 ? 4  
ATOM 1427  N N   . LYS A 1 182 ? 25.268  79.668  53.316 1.000 275.958 0 182 LYS BBB N   1 ? 4  
ATOM 1428  C CA  . LYS A 1 182 ? 25.898  80.031  54.583 1.000 261.539 0 182 LYS BBB CA  1 ? 4  
ATOM 1429  C C   . LYS A 1 182 ? 25.829  81.528  54.880 1.000 266.047 0 182 LYS BBB C   1 ? 4  
ATOM 1430  O O   . LYS A 1 182 ? 26.288  81.960  55.940 1.000 285.828 0 182 LYS BBB O   1 ? 4  
ATOM 1431  C CB  . LYS A 1 182 ? 27.379  79.647  54.586 1.000 239.022 0 182 LYS BBB CB  1 ? 4  
ATOM 1432  C CG  . LYS A 1 182 ? 27.705  78.223  54.214 1.000 232.968 0 182 LYS BBB CG  1 ? 4  
ATOM 1433  C CD  . LYS A 1 182 ? 26.809  77.245  54.923 1.000 221.781 0 182 LYS BBB CD  1 ? 4  
ATOM 1434  C CE  . LYS A 1 182 ? 27.582  75.996  55.224 1.000 209.384 0 182 LYS BBB CE  1 ? 4  
ATOM 1435  N NZ  . LYS A 1 182 ? 27.577  75.044  54.086 1.000 235.672 0 182 LYS BBB NZ  1 ? 4  
ATOM 1436  N N   . ASN A 1 183 ? 25.245  82.327  53.988 1.000 258.527 0 183 ASN BBB N   1 ? 4  
ATOM 1437  C CA  . ASN A 1 183 ? 25.221  83.773  54.188 1.000 244.932 0 183 ASN BBB CA  1 ? 4  
ATOM 1438  C C   . ASN A 1 183 ? 23.899  84.246  54.772 1.000 234.328 0 183 ASN BBB C   1 ? 4  
ATOM 1439  O O   . ASN A 1 183 ? 23.878  85.235  55.515 1.000 238.174 0 183 ASN BBB O   1 ? 4  
ATOM 1440  C CB  . ASN A 1 183 ? 25.501  84.515  52.877 1.000 244.333 0 183 ASN BBB CB  1 ? 4  
ATOM 1441  C CG  . ASN A 1 183 ? 26.945  84.388  52.427 1.000 243.310 0 183 ASN BBB CG  1 ? 4  
ATOM 1442  O OD1 . ASN A 1 183 ? 27.267  83.590  51.548 1.000 259.312 0 183 ASN BBB OD1 1 ? 4  
ATOM 1443  N ND2 . ASN A 1 183 ? 27.821  85.192  53.018 1.000 226.293 0 183 ASN BBB ND2 1 ? 4  
ATOM 1444  N N   . ALA A 1 184 ? 22.791  83.583  54.436 1.000 241.470 0 184 ALA BBB N   1 ? 4  
ATOM 1445  C CA  . ALA A 1 184 ? 21.527  83.897  55.092 1.000 228.050 0 184 ALA BBB CA  1 ? 4  
ATOM 1446  C C   . ALA A 1 184 ? 21.630  83.642  56.592 1.000 232.091 0 184 ALA BBB C   1 ? 4  
ATOM 1447  O O   . ALA A 1 184 ? 21.176  84.452  57.408 1.000 214.896 0 184 ALA BBB O   1 ? 4  
ATOM 1448  C CB  . ALA A 1 184 ? 20.395  83.078  54.475 1.000 205.329 0 184 ALA BBB CB  1 ? 4  
ATOM 1449  N N   . ALA A 1 185 ? 22.204  82.499  56.971 1.000 221.042 0 185 ALA BBB N   1 ? 4  
ATOM 1450  C CA  . ALA A 1 185 ? 22.437  82.185  58.379 1.000 210.391 0 185 ALA BBB CA  1 ? 4  
ATOM 1451  C C   . ALA A 1 185 ? 23.461  83.124  59.020 1.000 195.403 0 185 ALA BBB C   1 ? 4  
ATOM 1452  O O   . ALA A 1 185 ? 23.415  83.358  60.232 1.000 180.727 0 185 ALA BBB O   1 ? 4  
ATOM 1453  C CB  . ALA A 1 185 ? 22.881  80.732  58.525 1.000 207.002 0 185 ALA BBB CB  1 ? 4  
ATOM 1454  N N   . THR A 1 186 ? 24.432  83.607  58.245 1.000 193.668 0 186 THR BBB N   1 ? 4  
ATOM 1455  C CA  . THR A 1 186 ? 25.515  84.422  58.795 1.000 185.922 0 186 THR BBB CA  1 ? 4  
ATOM 1456  C C   . THR A 1 186 ? 25.053  85.793  59.310 1.000 180.406 0 186 THR BBB C   1 ? 4  
ATOM 1457  O O   . THR A 1 186 ? 25.333  86.151  60.460 1.000 166.956 0 186 THR BBB O   1 ? 4  
ATOM 1458  C CB  . THR A 1 186 ? 26.614  84.583  57.742 1.000 193.686 0 186 THR BBB CB  1 ? 4  
ATOM 1459  O OG1 . THR A 1 186 ? 27.052  83.291  57.304 1.000 214.683 0 186 THR BBB OG1 1 ? 4  
ATOM 1460  C CG2 . THR A 1 186 ? 27.791  85.326  58.314 1.000 187.831 0 186 THR BBB CG2 1 ? 4  
ATOM 1461  N N   . GLU A 1 187 ? 24.335  86.570  58.481 1.000 190.849 0 187 GLU BBB N   1 ? 4  
ATOM 1462  C CA  . GLU A 1 187 ? 23.749  87.880  58.815 1.000 190.339 0 187 GLU BBB CA  1 ? 4  
ATOM 1463  C C   . GLU A 1 187 ? 22.839  87.917  60.040 1.000 187.145 0 187 GLU BBB C   1 ? 4  
ATOM 1464  O O   . GLU A 1 187 ? 22.403  88.988  60.473 1.000 196.776 0 187 GLU BBB O   1 ? 4  
ATOM 1465  C CB  . GLU A 1 187 ? 22.936  88.420  57.638 1.000 198.238 0 187 GLU BBB CB  1 ? 4  
ATOM 1466  C CG  . GLU A 1 187 ? 21.848  87.477  57.181 1.000 204.363 0 187 GLU BBB CG  1 ? 4  
ATOM 1467  C CD  . GLU A 1 187 ? 21.505  87.640  55.716 1.000 219.038 0 187 GLU BBB CD  1 ? 4  
ATOM 1468  O OE1 . GLU A 1 187 ? 22.065  88.544  55.064 1.000 225.217 0 187 GLU BBB OE1 1 ? 4  
ATOM 1469  O OE2 . GLU A 1 187 ? 20.635  86.893  55.224 1.000 233.573 0 187 GLU BBB OE2 1 ? 4  
ATOM 1470  N N   . THR A 1 188 ? 22.607  86.755  60.635 1.000 173.331 0 188 THR BBB N   1 ? 4  
ATOM 1471  C CA  . THR A 1 188 ? 21.653  86.543  61.723 1.000 168.275 0 188 THR BBB CA  1 ? 4  
ATOM 1472  C C   . THR A 1 188 ? 22.425  86.042  62.935 1.000 146.339 0 188 THR BBB C   1 ? 4  
ATOM 1473  O O   . THR A 1 188 ? 22.682  86.823  63.856 1.000 137.220 0 188 THR BBB O   1 ? 4  
ATOM 1474  C CB  . THR A 1 188 ? 20.438  85.662  61.396 1.000 174.695 0 188 THR BBB CB  1 ? 4  
ATOM 1475  O OG1 . THR A 1 188 ? 19.734  85.364  62.615 1.000 181.658 0 188 THR BBB OG1 1 ? 4  
ATOM 1476  C CG2 . THR A 1 188 ? 20.775  84.395  60.644 1.000 179.040 0 188 THR BBB CG2 1 ? 4  
ATOM 1477  N N   . LEU A 1 189 ? 22.862  84.792  62.932 1.000 134.056 0 189 LEU BBB N   1 ? 4  
ATOM 1478  C CA  . LEU A 1 189 ? 23.397  84.137  64.110 1.000 132.937 0 189 LEU BBB CA  1 ? 4  
ATOM 1479  C C   . LEU A 1 189 ? 24.703  84.780  64.566 1.000 134.148 0 189 LEU BBB C   1 ? 4  
ATOM 1480  O O   . LEU A 1 189 ? 25.001  84.749  65.764 1.000 139.803 0 189 LEU BBB O   1 ? 4  
ATOM 1481  C CB  . LEU A 1 189 ? 23.634  82.669  63.769 1.000 126.345 0 189 LEU BBB CB  1 ? 4  
ATOM 1482  C CG  . LEU A 1 189 ? 23.727  81.568  64.820 1.000 130.488 0 189 LEU BBB CG  1 ? 4  
ATOM 1483  C CD1 . LEU A 1 189 ? 22.467  81.521  65.668 1.000 141.734 0 189 LEU BBB CD1 1 ? 4  
ATOM 1484  C CD2 . LEU A 1 189 ? 24.025  80.224  64.156 1.000 123.795 0 189 LEU BBB CD2 1 ? 4  
ATOM 1485  N N   . LEU A 1 190 ? 25.524  85.315  63.658 1.000 125.974 0 190 LEU BBB N   1 ? 4  
ATOM 1486  C CA  . LEU A 1 190 ? 26.752  85.955  64.124 1.000 116.177 0 190 LEU BBB CA  1 ? 4  
ATOM 1487  C C   . LEU A 1 190 ? 26.437  87.086  65.098 1.000 118.952 0 190 LEU BBB C   1 ? 4  
ATOM 1488  O O   . LEU A 1 190 ? 27.156  87.279  66.085 1.000 129.943 0 190 LEU BBB O   1 ? 4  
ATOM 1489  C CB  . LEU A 1 190 ? 27.550  86.515  62.947 1.000 113.053 0 190 LEU BBB CB  1 ? 4  
ATOM 1490  C CG  . LEU A 1 190 ? 28.966  87.028  63.232 1.000 104.920 0 190 LEU BBB CG  1 ? 4  
ATOM 1491  C CD1 . LEU A 1 190 ? 29.937  85.907  63.548 1.000 109.835 0 190 LEU BBB CD1 1 ? 4  
ATOM 1492  C CD2 . LEU A 1 190 ? 29.457  87.867  62.064 1.000 104.944 0 190 LEU BBB CD2 1 ? 4  
ATOM 1493  N N   . VAL A 1 191 ? 25.377  87.850  64.830 1.000 115.407 0 191 VAL BBB N   1 ? 4  
ATOM 1494  C CA  . VAL A 1 191 ? 24.972  88.930  65.729 1.000 111.599 0 191 VAL BBB CA  1 ? 4  
ATOM 1495  C C   . VAL A 1 191 ? 24.295  88.374  66.983 1.000 116.852 0 191 VAL BBB C   1 ? 4  
ATOM 1496  O O   . VAL A 1 191 ? 24.573  88.814  68.106 1.000 117.621 0 191 VAL BBB O   1 ? 4  
ATOM 1497  C CB  . VAL A 1 191 ? 24.067  89.935  65.000 1.000 113.050 0 191 VAL BBB CB  1 ? 4  
ATOM 1498  C CG1 . VAL A 1 191 ? 23.638  91.035  65.959 1.000 114.305 0 191 VAL BBB CG1 1 ? 4  
ATOM 1499  C CG2 . VAL A 1 191 ? 24.791  90.515  63.803 1.000 112.071 0 191 VAL BBB CG2 1 ? 4  
ATOM 1500  N N   . GLN A 1 192 ? 23.379  87.416  66.810 1.000 118.249 0 192 GLN BBB N   1 ? 4  
ATOM 1501  C CA  . GLN A 1 192 ? 22.636  86.869  67.944 1.000 125.739 0 192 GLN BBB CA  1 ? 4  
ATOM 1502  C C   . GLN A 1 192 ? 23.549  86.201  68.967 1.000 127.052 0 192 GLN BBB C   1 ? 4  
ATOM 1503  O O   . GLN A 1 192 ? 23.288  86.259  70.174 1.000 137.804 0 192 GLN BBB O   1 ? 4  
ATOM 1504  C CB  . GLN A 1 192 ? 21.617  85.855  67.424 1.000 131.755 0 192 GLN BBB CB  1 ? 4  
ATOM 1505  C CG  . GLN A 1 192 ? 20.636  85.309  68.437 1.000 159.976 0 192 GLN BBB CG  1 ? 4  
ATOM 1506  C CD  . GLN A 1 192 ? 19.730  84.247  67.836 1.000 179.417 0 192 GLN BBB CD  1 ? 4  
ATOM 1507  O OE1 . GLN A 1 192 ? 19.105  84.438  66.791 1.000 192.130 0 192 GLN BBB OE1 1 ? 4  
ATOM 1508  N NE2 . GLN A 1 192 ? 19.642  83.103  68.502 1.000 190.652 0 192 GLN BBB NE2 1 ? 4  
ATOM 1509  N N   . ASN A 1 193 ? 24.613  85.554  68.507 1.000 123.438 0 193 ASN BBB N   1 ? 4  
ATOM 1510  C CA  . ASN A 1 193 ? 25.561  84.861  69.369 1.000 124.239 0 193 ASN BBB CA  1 ? 4  
ATOM 1511  C C   . ASN A 1 193 ? 26.705  85.748  69.855 1.000 122.646 0 193 ASN BBB C   1 ? 4  
ATOM 1512  O O   . ASN A 1 193 ? 27.573  85.267  70.589 1.000 123.723 0 193 ASN BBB O   1 ? 4  
ATOM 1513  C CB  . ASN A 1 193 ? 26.099  83.620  68.654 1.000 136.270 0 193 ASN BBB CB  1 ? 4  
ATOM 1514  C CG  . ASN A 1 193 ? 25.046  82.533  68.525 1.000 143.409 0 193 ASN BBB CG  1 ? 4  
ATOM 1515  O OD1 . ASN A 1 193 ? 23.865  82.768  68.793 1.000 137.865 0 193 ASN BBB OD1 1 ? 4  
ATOM 1516  N ND2 . ASN A 1 193 ? 25.462  81.345  68.099 1.000 148.804 0 193 ASN BBB ND2 1 ? 4  
ATOM 1517  N N   . ALA A 1 194 ? 26.732  87.018  69.465 1.000 121.252 0 194 ALA BBB N   1 ? 4  
ATOM 1518  C CA  . ALA A 1 194 ? 27.730  87.949  69.970 1.000 125.303 0 194 ALA BBB CA  1 ? 4  
ATOM 1519  C C   . ALA A 1 194 ? 27.468  88.263  71.439 1.000 139.213 0 194 ALA BBB C   1 ? 4  
ATOM 1520  O O   . ALA A 1 194 ? 26.393  87.990  71.977 1.000 143.493 0 194 ALA BBB O   1 ? 4  
ATOM 1521  C CB  . ALA A 1 194 ? 27.730  89.238  69.149 1.000 129.795 0 194 ALA BBB CB  1 ? 4  
ATOM 1522  N N   . ASN A 1 195 ? 28.475  88.830  72.098 1.000 150.946 0 195 ASN BBB N   1 ? 4  
ATOM 1523  C CA  . ASN A 1 195 ? 28.341  89.153  73.508 1.000 153.032 0 195 ASN BBB CA  1 ? 4  
ATOM 1524  C C   . ASN A 1 195 ? 27.478  90.397  73.649 1.000 151.887 0 195 ASN BBB C   1 ? 4  
ATOM 1525  O O   . ASN A 1 195 ? 27.220  91.100  72.669 1.000 145.197 0 195 ASN BBB O   1 ? 4  
ATOM 1526  C CB  . ASN A 1 195 ? 29.722  89.361  74.139 1.000 155.586 0 195 ASN BBB CB  1 ? 4  
ATOM 1527  C CG  . ASN A 1 195 ? 30.390  90.665  73.706 1.000 155.660 0 195 ASN BBB CG  1 ? 4  
ATOM 1528  O OD1 . ASN A 1 195 ? 31.028  90.735  72.662 1.000 157.983 0 195 ASN BBB OD1 1 ? 4  
ATOM 1529  N ND2 . ASN A 1 195 ? 30.262  91.701  74.534 1.000 160.543 0 195 ASN BBB ND2 1 ? 4  
ATOM 1530  N N   . PRO A 1 196 ? 27.001  90.684  74.869 1.000 149.195 0 196 PRO BBB N   1 ? 4  
ATOM 1531  C CA  A PRO A 1 196 ? 26.040  91.779  75.061 1.000 144.856 0 196 PRO BBB CA  1 ? 4  
ATOM 1532  C C   . PRO A 1 196 ? 26.445  93.093  74.420 1.000 142.952 0 196 PRO BBB C   1 ? 4  
ATOM 1533  O O   . PRO A 1 196 ? 25.742  93.599  73.545 1.000 142.949 0 196 PRO BBB O   1 ? 4  
ATOM 1534  C CB  A PRO A 1 196 ? 25.985  91.929  76.586 1.000 149.730 0 196 PRO BBB CB  1 ? 4  
ATOM 1535  C CG  A PRO A 1 196 ? 26.535  90.662  77.152 1.000 152.973 0 196 PRO BBB CG  1 ? 4  
ATOM 1536  C CD  A PRO A 1 196 ? 27.071  89.810  76.051 1.000 151.280 0 196 PRO BBB CD  1 ? 4  
ATOM 1537  N N   . ASP A 1 197 ? 27.575  93.655  74.855 1.000 139.744 0 197 ASP BBB N   1 ? 4  
ATOM 1538  C CA  . ASP A 1 197 ? 27.916  95.013  74.449 1.000 139.820 0 197 ASP BBB CA  1 ? 4  
ATOM 1539  C C   . ASP A 1 197 ? 28.194  95.101  72.955 1.000 143.487 0 197 ASP BBB C   1 ? 4  
ATOM 1540  O O   . ASP A 1 197 ? 27.821  96.090  72.314 1.000 155.083 0 197 ASP BBB O   1 ? 4  
ATOM 1541  C CB  . ASP A 1 197 ? 29.102  95.514  75.255 1.000 143.328 0 197 ASP BBB CB  1 ? 4  
ATOM 1542  C CG  . ASP A 1 197 ? 28.731  95.798  76.676 1.000 165.705 0 197 ASP BBB CG  1 ? 4  
ATOM 1543  O OD1 . ASP A 1 197 ? 28.270  96.922  76.950 1.000 177.959 0 197 ASP BBB OD1 1 ? 4  
ATOM 1544  O OD2 . ASP A 1 197 ? 28.878  94.888  77.516 1.000 180.218 0 197 ASP BBB OD2 1 ? 4  
ATOM 1545  N N   . CYS A 1 198 ? 28.851  94.087  72.384 1.000 143.236 0 198 CYS BBB N   1 ? 4  
ATOM 1546  C CA  . CYS A 1 198 ? 29.107  94.103  70.946 1.000 133.489 0 198 CYS BBB CA  1 ? 4  
ATOM 1547  C C   . CYS A 1 198 ? 27.819  93.955  70.142 1.000 127.362 0 198 CYS BBB C   1 ? 4  
ATOM 1548  O O   . CYS A 1 198 ? 27.690  94.543  69.062 1.000 123.695 0 198 CYS BBB O   1 ? 4  
ATOM 1549  C CB  . CYS A 1 198 ? 30.114  93.013  70.563 1.000 139.585 0 198 CYS BBB CB  1 ? 4  
ATOM 1550  S SG  . CYS A 1 198 ? 31.824  93.313  71.105 1.000 162.320 0 198 CYS BBB SG  1 ? 4  
ATOM 1551  N N   . LYS A 1 199 ? 26.870  93.147  70.627 1.000 127.577 0 199 LYS BBB N   1 ? 4  
ATOM 1552  C CA  . LYS A 1 199 ? 25.601  93.009  69.916 1.000 126.509 0 199 LYS BBB CA  1 ? 4  
ATOM 1553  C C   . LYS A 1 199 ? 24.930  94.368  69.743 1.000 128.098 0 199 LYS BBB C   1 ? 4  
ATOM 1554  O O   . LYS A 1 199 ? 24.409  94.682  68.666 1.000 132.558 0 199 LYS BBB O   1 ? 4  
ATOM 1555  C CB  . LYS A 1 199 ? 24.669  92.050  70.657 1.000 126.976 0 199 LYS BBB CB  1 ? 4  
ATOM 1556  C CG  . LYS A 1 199 ? 23.411  91.700  69.873 1.000 130.771 0 199 LYS BBB CG  1 ? 4  
ATOM 1557  C CD  . LYS A 1 199 ? 22.449  90.888  70.715 1.000 136.028 0 199 LYS BBB CD  1 ? 4  
ATOM 1558  C CE  . LYS A 1 199 ? 22.934  89.488  71.018 1.000 134.749 0 199 LYS BBB CE  1 ? 4  
ATOM 1559  N NZ  . LYS A 1 199 ? 21.785  88.662  71.490 1.000 132.545 0 199 LYS BBB NZ  1 ? 4  
ATOM 1560  N N   . THR A 1 200 ? 24.921  95.178  70.806 1.000 129.663 0 200 THR BBB N   1 ? 4  
ATOM 1561  C CA  . THR A 1 200 ? 24.369  96.528  70.729 1.000 132.958 0 200 THR BBB CA  1 ? 4  
ATOM 1562  C C   . THR A 1 200 ? 25.073  97.343  69.653 1.000 133.700 0 200 THR BBB C   1 ? 4  
ATOM 1563  O O   . THR A 1 200 ? 24.430  98.083  68.898 1.000 136.209 0 200 THR BBB O   1 ? 4  
ATOM 1564  C CB  . THR A 1 200 ? 24.476  97.228  72.083 1.000 132.934 0 200 THR BBB CB  1 ? 4  
ATOM 1565  O OG1 . THR A 1 200 ? 25.827  97.654  72.299 1.000 133.003 0 200 THR BBB OG1 1 ? 4  
ATOM 1566  C CG2 . THR A 1 200 ? 24.062  96.284  73.193 1.000 145.173 0 200 THR BBB CG2 1 ? 4  
ATOM 1567  N N   . ILE A 1 201 ? 26.400  97.225  69.574 1.000 133.191 0 201 ILE BBB N   1 ? 4  
ATOM 1568  C CA  . ILE A 1 201 ? 27.141  97.948  68.550 1.000 126.691 0 201 ILE BBB CA  1 ? 4  
ATOM 1569  C C   . ILE A 1 201 ? 26.766  97.444  67.165 1.000 129.662 0 201 ILE BBB C   1 ? 4  
ATOM 1570  O O   . ILE A 1 201 ? 26.531  98.240  66.248 1.000 135.475 0 201 ILE BBB O   1 ? 4  
ATOM 1571  C CB  . ILE A 1 201 ? 28.656  97.800  68.793 1.000 120.628 0 201 ILE BBB CB  1 ? 4  
ATOM 1572  C CG1 . ILE A 1 201 ? 29.094  98.511  70.069 1.000 130.368 0 201 ILE BBB CG1 1 ? 4  
ATOM 1573  C CG2 . ILE A 1 201 ? 29.453  98.322  67.608 1.000 120.794 0 201 ILE BBB CG2 1 ? 4  
ATOM 1574  C CD1 . ILE A 1 201 ? 30.479  98.097  70.509 1.000 130.682 0 201 ILE BBB CD1 1 ? 4  
ATOM 1575  N N   . LEU A 1 202 ? 26.686  96.122  66.987 1.000 130.367 0 202 LEU BBB N   1 ? 4  
ATOM 1576  C CA  . LEU A 1 202 ? 26.367  95.602  65.662 1.000 125.148 0 202 LEU BBB CA  1 ? 4  
ATOM 1577  C C   . LEU A 1 202 ? 24.950  95.963  65.235 1.000 128.438 0 202 LEU BBB C   1 ? 4  
ATOM 1578  O O   . LEU A 1 202 ? 24.717  96.306  64.069 1.000 125.204 0 202 LEU BBB O   1 ? 4  
ATOM 1579  C CB  . LEU A 1 202 ? 26.528  94.084  65.658 1.000 114.913 0 202 LEU BBB CB  1 ? 4  
ATOM 1580  C CG  . LEU A 1 202 ? 27.938  93.557  65.893 1.000 113.297 0 202 LEU BBB CG  1 ? 4  
ATOM 1581  C CD1 . LEU A 1 202 ? 27.930  92.037  65.955 1.000 114.752 0 202 LEU BBB CD1 1 ? 4  
ATOM 1582  C CD2 . LEU A 1 202 ? 28.879  94.070  64.834 1.000 112.271 0 202 LEU BBB CD2 1 ? 4  
ATOM 1583  N N   . LYS A 1 203 ? 23.990  95.888  66.164 1.000 128.452 0 203 LYS BBB N   1 ? 4  
ATOM 1584  C CA  . LYS A 1 203 ? 22.623  96.298  65.854 1.000 130.321 0 203 LYS BBB CA  1 ? 4  
ATOM 1585  C C   . LYS A 1 203 ? 22.551  97.767  65.457 1.000 132.510 0 203 LYS BBB C   1 ? 4  
ATOM 1586  O O   . LYS A 1 203 ? 21.821  98.133  64.527 1.000 136.347 0 203 LYS BBB O   1 ? 4  
ATOM 1587  C CB  . LYS A 1 203 ? 21.695  95.985  67.027 1.000 131.474 0 203 LYS BBB CB  1 ? 4  
ATOM 1588  C CG  . LYS A 1 203 ? 21.373  94.495  67.107 1.000 130.989 0 203 LYS BBB CG  1 ? 4  
ATOM 1589  C CD  . LYS A 1 203 ? 19.903  94.210  67.364 1.000 142.215 0 203 LYS BBB CD  1 ? 4  
ATOM 1590  C CE  . LYS A 1 203 ? 19.592  94.139  68.845 1.000 137.448 0 203 LYS BBB CE  1 ? 4  
ATOM 1591  N NZ  . LYS A 1 203 ? 18.381  93.314  69.078 1.000 140.238 0 203 LYS BBB NZ  1 ? 4  
ATOM 1592  N N   . ALA A 1 204 ? 23.302  98.626  66.150 1.000 128.473 0 204 ALA BBB N   1 ? 4  
ATOM 1593  C CA  . ALA A 1 204 ? 23.269  100.044 65.824 1.000 142.543 0 204 ALA BBB CA  1 ? 4  
ATOM 1594  C C   . ALA A 1 204 ? 23.924  100.333 64.485 1.000 147.466 0 204 ALA BBB C   1 ? 4  
ATOM 1595  O O   . ALA A 1 204 ? 23.624  101.359 63.869 1.000 153.296 0 204 ALA BBB O   1 ? 4  
ATOM 1596  C CB  . ALA A 1 204 ? 23.956  100.856 66.922 1.000 146.963 0 204 ALA BBB CB  1 ? 4  
ATOM 1597  N N   . LEU A 1 205 ? 24.788  99.434  64.011 1.000 146.238 0 205 LEU BBB N   1 ? 4  
ATOM 1598  C CA  . LEU A 1 205 ? 25.441  99.642  62.726 1.000 139.802 0 205 LEU BBB CA  1 ? 4  
ATOM 1599  C C   . LEU A 1 205 ? 24.441  99.614  61.578 1.000 143.323 0 205 LEU BBB C   1 ? 4  
ATOM 1600  O O   . LEU A 1 205 ? 24.662  100.260 60.549 1.000 147.391 0 205 LEU BBB O   1 ? 4  
ATOM 1601  C CB  . LEU A 1 205 ? 26.525  98.587  62.532 1.000 128.796 0 205 LEU BBB CB  1 ? 4  
ATOM 1602  C CG  . LEU A 1 205 ? 27.841  99.094  61.952 1.000 133.160 0 205 LEU BBB CG  1 ? 4  
ATOM 1603  C CD1 . LEU A 1 205 ? 28.262  100.393 62.624 1.000 135.788 0 205 LEU BBB CD1 1 ? 4  
ATOM 1604  C CD2 . LEU A 1 205 ? 28.907  98.036  62.130 1.000 133.572 0 205 LEU BBB CD2 1 ? 4  
ATOM 1605  N N   . GLY A 1 206 ? 23.334  98.898  61.745 1.000 142.768 0 206 GLY BBB N   1 ? 4  
ATOM 1606  C CA  . GLY A 1 206 ? 22.305  98.824  60.738 1.000 150.934 0 206 GLY BBB CA  1 ? 4  
ATOM 1607  C C   . GLY A 1 206 ? 22.474  97.671  59.768 1.000 162.430 0 206 GLY BBB C   1 ? 4  
ATOM 1608  O O   . GLY A 1 206 ? 23.417  96.877  59.854 1.000 169.438 0 206 GLY BBB O   1 ? 4  
ATOM 1609  N N   . PRO A 1 207 ? 21.541  97.560  58.827 1.000 166.154 0 207 PRO BBB N   1 ? 4  
ATOM 1610  C CA  . PRO A 1 207 ? 21.588  96.472  57.844 1.000 167.049 0 207 PRO BBB CA  1 ? 4  
ATOM 1611  C C   . PRO A 1 207 ? 22.643  96.693  56.772 1.000 170.660 0 207 PRO BBB C   1 ? 4  
ATOM 1612  O O   . PRO A 1 207 ? 23.022  97.823  56.457 1.000 172.574 0 207 PRO BBB O   1 ? 4  
ATOM 1613  C CB  . PRO A 1 207 ? 20.182  96.494  57.235 1.000 167.990 0 207 PRO BBB CB  1 ? 4  
ATOM 1614  C CG  . PRO A 1 207 ? 19.749  97.919  57.366 1.000 164.902 0 207 PRO BBB CG  1 ? 4  
ATOM 1615  C CD  . PRO A 1 207 ? 20.401  98.467  58.607 1.000 159.773 0 207 PRO BBB CD  1 ? 4  
ATOM 1616  N N   . GLY A 1 208 ? 23.119  95.583  56.210 1.000 172.164 0 208 GLY BBB N   1 ? 4  
ATOM 1617  C CA  . GLY A 1 208 ? 24.068  95.657  55.118 1.000 170.669 0 208 GLY BBB CA  1 ? 4  
ATOM 1618  C C   . GLY A 1 208 ? 25.488  95.974  55.516 1.000 165.183 0 208 GLY BBB C   1 ? 4  
ATOM 1619  O O   . GLY A 1 208 ? 26.299  96.307  54.644 1.000 170.133 0 208 GLY BBB O   1 ? 4  
ATOM 1620  N N   . ALA A 1 209 ? 25.822  95.874  56.797 1.000 148.687 0 209 ALA BBB N   1 ? 4  
ATOM 1621  C CA  . ALA A 1 209 ? 27.188  96.126  57.226 1.000 141.830 0 209 ALA BBB CA  1 ? 4  
ATOM 1622  C C   . ALA A 1 209 ? 28.142  95.049  56.724 1.000 138.994 0 209 ALA BBB C   1 ? 4  
ATOM 1623  O O   . ALA A 1 209 ? 27.844  93.852  56.767 1.000 145.998 0 209 ALA BBB O   1 ? 4  
ATOM 1624  C CB  . ALA A 1 209 ? 27.252  96.208  58.750 1.000 142.165 0 209 ALA BBB CB  1 ? 4  
ATOM 1625  N N   . THR A 1 210 ? 29.296  95.496  56.231 1.000 131.360 0 210 THR BBB N   1 ? 4  
ATOM 1626  C CA  . THR A 1 210 ? 30.353  94.622  55.753 1.000 123.730 0 210 THR BBB CA  1 ? 4  
ATOM 1627  C C   . THR A 1 210 ? 31.090  94.059  56.962 1.000 121.245 0 210 THR BBB C   1 ? 4  
ATOM 1628  O O   . THR A 1 210 ? 31.016  94.615  58.059 1.000 130.915 0 210 THR BBB O   1 ? 4  
ATOM 1629  C CB  . THR A 1 210 ? 31.322  95.426  54.872 1.000 129.176 0 210 THR BBB CB  1 ? 4  
ATOM 1630  O OG1 . THR A 1 210 ? 30.581  96.212  53.933 1.000 150.235 0 210 THR BBB OG1 1 ? 4  
ATOM 1631  C CG2 . THR A 1 210 ? 32.275  94.536  54.103 1.000 137.907 0 210 THR BBB CG2 1 ? 4  
ATOM 1632  N N   . LEU A 1 211 ? 31.826  92.961  56.764 1.000 115.148 0 211 LEU BBB N   1 ? 4  
ATOM 1633  C CA  . LEU A 1 211 ? 32.613  92.434  57.876 1.000 113.341 0 211 LEU BBB CA  1 ? 4  
ATOM 1634  C C   . LEU A 1 211 ? 33.624  93.460  58.354 1.000 121.946 0 211 LEU BBB C   1 ? 4  
ATOM 1635  O O   . LEU A 1 211 ? 33.824  93.628  59.562 1.000 130.663 0 211 LEU BBB O   1 ? 4  
ATOM 1636  C CB  . LEU A 1 211 ? 33.312  91.126  57.508 1.000 112.624 0 211 LEU BBB CB  1 ? 4  
ATOM 1637  C CG  . LEU A 1 211 ? 32.684  89.886  58.150 1.000 110.021 0 211 LEU BBB CG  1 ? 4  
ATOM 1638  C CD1 . LEU A 1 211 ? 31.196  89.804  57.851 1.000 111.080 0 211 LEU BBB CD1 1 ? 4  
ATOM 1639  C CD2 . LEU A 1 211 ? 33.409  88.609  57.732 1.000 113.638 0 211 LEU BBB CD2 1 ? 4  
ATOM 1640  N N   . GLU A 1 212 ? 34.274  94.152  57.420 1.000 134.226 0 212 GLU BBB N   1 ? 4  
ATOM 1641  C CA  . GLU A 1 212 ? 35.214  95.198  57.797 1.000 135.035 0 212 GLU BBB CA  1 ? 4  
ATOM 1642  C C   . GLU A 1 212 ? 34.559  96.243  58.698 1.000 136.197 0 212 GLU BBB C   1 ? 4  
ATOM 1643  O O   . GLU A 1 212 ? 35.129  96.637  59.721 1.000 140.734 0 212 GLU BBB O   1 ? 4  
ATOM 1644  C CB  . GLU A 1 212 ? 35.751  95.878  56.538 1.000 137.166 0 212 GLU BBB CB  1 ? 4  
ATOM 1645  C CG  . GLU A 1 212 ? 35.819  94.999  55.299 1.000 147.997 0 212 GLU BBB CG  1 ? 4  
ATOM 1646  C CD  . GLU A 1 212 ? 36.478  95.702  54.116 1.000 167.475 0 212 GLU BBB CD  1 ? 4  
ATOM 1647  O OE1 . GLU A 1 212 ? 37.241  96.689  54.341 1.000 161.944 0 212 GLU BBB OE1 1 ? 4  
ATOM 1648  O OE2 . GLU A 1 212 ? 36.196  95.321  52.954 1.000 174.039 0 212 GLU BBB OE2 1 ? 4  
ATOM 1649  N N   . GLU A 1 213 ? 33.362  96.715  58.330 1.000 130.649 0 213 GLU BBB N   1 ? 4  
ATOM 1650  C CA  . GLU A 1 213 ? 32.716  97.719  59.167 1.000 126.451 0 213 GLU BBB CA  1 ? 4  
ATOM 1651  C C   . GLU A 1 213 ? 32.315  97.185  60.539 1.000 116.708 0 213 GLU BBB C   1 ? 4  
ATOM 1652  O O   . GLU A 1 213 ? 32.541  97.850  61.555 1.000 118.782 0 213 GLU BBB O   1 ? 4  
ATOM 1653  C CB  . GLU A 1 213 ? 31.461  98.256  58.477 1.000 132.961 0 213 GLU BBB CB  1 ? 4  
ATOM 1654  C CG  . GLU A 1 213 ? 31.669  99.149  57.273 1.000 147.647 0 213 GLU BBB CG  1 ? 4  
ATOM 1655  C CD  . GLU A 1 213 ? 30.376  99.356  56.498 1.000 160.455 0 213 GLU BBB CD  1 ? 4  
ATOM 1656  O OE1 . GLU A 1 213 ? 29.462  98.514  56.637 1.000 153.410 0 213 GLU BBB OE1 1 ? 4  
ATOM 1657  O OE2 . GLU A 1 213 ? 30.282  100.337 55.729 1.000 173.407 0 213 GLU BBB OE2 1 ? 4  
ATOM 1658  N N   . MET A 1 214 ? 31.737  95.980  60.599 1.000 112.772 0 214 MET BBB N   1 ? 4  
ATOM 1659  C CA  . MET A 1 214 ? 31.388  95.400  61.894 1.000 114.320 0 214 MET BBB CA  1 ? 4  
ATOM 1660  C C   . MET A 1 214 ? 32.615  95.102  62.752 1.000 114.141 0 214 MET BBB C   1 ? 4  
ATOM 1661  O O   . MET A 1 214 ? 32.614  95.387  63.955 1.000 126.697 0 214 MET BBB O   1 ? 4  
ATOM 1662  C CB  A MET A 1 214 ? 30.436  94.212  61.727 1.000 115.109 0 214 MET BBB CB  1 ? 4  
ATOM 1663  C CG  A MET A 1 214 ? 30.771  93.156  60.750 1.000 124.311 0 214 MET BBB CG  1 ? 4  
ATOM 1664  S SD  A MET A 1 214 ? 29.370  92.011  60.694 1.000 129.537 0 214 MET BBB SD  1 ? 4  
ATOM 1665  C CE  A MET A 1 214 ? 29.195  91.532  62.407 1.000 123.083 0 214 MET BBB CE  1 ? 4  
ATOM 1666  N N   . MET A 1 215 ? 33.666  94.530  62.164 1.000 113.113 0 215 MET BBB N   1 ? 4  
ATOM 1667  C CA  . MET A 1 215 ? 34.854  94.205  62.951 1.000 115.258 0 215 MET BBB CA  1 ? 4  
ATOM 1668  C C   . MET A 1 215 ? 35.548  95.465  63.461 1.000 117.563 0 215 MET BBB C   1 ? 4  
ATOM 1669  O O   . MET A 1 215 ? 36.060  95.483  64.586 1.000 131.213 0 215 MET BBB O   1 ? 4  
ATOM 1670  C CB  . MET A 1 215 ? 35.821  93.371  62.113 1.000 117.363 0 215 MET BBB CB  1 ? 4  
ATOM 1671  C CG  . MET A 1 215 ? 35.320  91.976  61.781 1.000 122.704 0 215 MET BBB CG  1 ? 4  
ATOM 1672  S SD  . MET A 1 215 ? 36.561  90.691  62.022 1.000 132.711 0 215 MET BBB SD  1 ? 4  
ATOM 1673  C CE  . MET A 1 215 ? 37.887  91.395  61.005 1.000 136.975 0 215 MET BBB CE  1 ? 4  
ATOM 1674  N N   . THR A 1 216 ? 35.582  96.523  62.649 1.000 116.355 0 216 THR BBB N   1 ? 4  
ATOM 1675  C CA  . THR A 1 216 ? 36.109  97.809  63.107 1.000 118.481 0 216 THR BBB CA  1 ? 4  
ATOM 1676  C C   . THR A 1 216 ? 35.268  98.375  64.248 1.000 125.780 0 216 THR BBB C   1 ? 4  
ATOM 1677  O O   . THR A 1 216 ? 35.802  98.854  65.255 1.000 136.688 0 216 THR BBB O   1 ? 4  
ATOM 1678  C CB  . THR A 1 216 ? 36.168  98.798  61.944 1.000 118.808 0 216 THR BBB CB  1 ? 4  
ATOM 1679  O OG1 . THR A 1 216 ? 36.978  98.259  60.892 1.000 123.644 0 216 THR BBB OG1 1 ? 4  
ATOM 1680  C CG2 . THR A 1 216 ? 36.760  100.119 62.400 1.000 129.007 0 216 THR BBB CG2 1 ? 4  
ATOM 1681  N N   . ALA A 1 217 ? 33.943  98.343  64.086 1.000 127.822 0 217 ALA BBB N   1 ? 4  
ATOM 1682  C CA  . ALA A 1 217 ? 33.010  98.878  65.078 1.000 124.140 0 217 ALA BBB CA  1 ? 4  
ATOM 1683  C C   . ALA A 1 217 ? 33.194  98.227  66.450 1.000 122.536 0 217 ALA BBB C   1 ? 4  
ATOM 1684  O O   . ALA A 1 217 ? 33.166  98.916  67.475 1.000 128.515 0 217 ALA BBB O   1 ? 4  
ATOM 1685  C CB  . ALA A 1 217 ? 31.566  98.719  64.593 1.000 117.652 0 217 ALA BBB CB  1 ? 4  
ATOM 1686  N N   . CYS A 1 218 ? 33.406  96.914  66.498 1.000 119.194 0 218 CYS BBB N   1 ? 4  
ATOM 1687  C CA  . CYS A 1 218 ? 33.518  96.218  67.772 1.000 123.681 0 218 CYS BBB CA  1 ? 4  
ATOM 1688  C C   . CYS A 1 218 ? 34.947  96.120  68.283 1.000 137.724 0 218 CYS BBB C   1 ? 4  
ATOM 1689  O O   . CYS A 1 218 ? 35.202  95.357  69.217 1.000 171.543 0 218 CYS BBB O   1 ? 4  
ATOM 1690  C CB  . CYS A 1 218 ? 32.922  94.812  67.676 1.000 119.080 0 218 CYS BBB CB  1 ? 4  
ATOM 1691  S SG  . CYS A 1 218 ? 31.125  94.746  67.586 1.000 125.913 0 218 CYS BBB SG  1 ? 4  
ATOM 1692  N N   . GLN A 1 219 ? 35.898  96.774  67.638 1.000 135.091 0 219 GLN BBB N   1 ? 4  
ATOM 1693  C CA  . GLN A 1 219 ? 37.267  96.785  68.154 1.000 130.337 0 219 GLN BBB CA  1 ? 4  
ATOM 1694  C C   . GLN A 1 219 ? 37.454  97.736  69.377 1.000 131.155 0 219 GLN BBB C   1 ? 4  
ATOM 1695  O O   . GLN A 1 219 ? 36.904  97.528  70.474 1.000 130.438 0 219 GLN BBB O   1 ? 4  
ATOM 1696  C CB  . GLN A 1 219 ? 38.211  97.184  67.030 1.000 129.239 0 219 GLN BBB CB  1 ? 4  
ATOM 1697  C CG  . GLN A 1 219 ? 38.367  98.676  66.905 1.000 135.725 0 219 GLN BBB CG  1 ? 4  
ATOM 1698  C CD  . GLN A 1 219 ? 39.468  99.112  65.967 1.000 142.193 0 219 GLN BBB CD  1 ? 4  
ATOM 1699  O OE1 . GLN A 1 219 ? 40.308  98.319  65.540 1.000 149.472 0 219 GLN BBB OE1 1 ? 4  
ATOM 1700  N NE2 . GLN A 1 219 ? 39.436  100.388 65.595 1.000 145.075 0 219 GLN BBB NE2 1 ? 4  
ATOM 1701  N N   . PRO B 1 1   ? 49.802  76.870  36.979 1.000 86.031  0 1   PRO CCC N   1 ? 5  
ATOM 1702  C CA  . PRO B 1 1   ? 50.210  78.078  36.262 1.000 75.693  0 1   PRO CCC CA  1 ? 5  
ATOM 1703  C C   . PRO B 1 1   ? 50.410  77.860  34.768 1.000 81.029  0 1   PRO CCC C   1 ? 5  
ATOM 1704  O O   . PRO B 1 1   ? 50.284  76.742  34.270 1.000 88.301  0 1   PRO CCC O   1 ? 5  
ATOM 1705  C CB  A PRO B 1 1   ? 51.536  78.461  36.936 1.000 86.987  0 1   PRO CCC CB  1 ? 5  
ATOM 1706  C CG  A PRO B 1 1   ? 51.933  77.268  37.769 1.000 96.405  0 1   PRO CCC CG  1 ? 5  
ATOM 1707  C CD  A PRO B 1 1   ? 50.652  76.615  38.152 1.000 90.127  0 1   PRO CCC CD  1 ? 5  
ATOM 1708  N N   . ILE B 1 2   ? 50.727  78.947  34.071 1.000 82.892  0 2   ILE CCC N   1 ? 5  
ATOM 1709  C CA  . ILE B 1 2   ? 51.044  78.939  32.647 1.000 89.579  0 2   ILE CCC CA  1 ? 5  
ATOM 1710  C C   . ILE B 1 2   ? 52.536  79.202  32.530 1.000 90.830  0 2   ILE CCC C   1 ? 5  
ATOM 1711  O O   . ILE B 1 2   ? 53.035  80.217  33.029 1.000 88.205  0 2   ILE CCC O   1 ? 5  
ATOM 1712  C CB  . ILE B 1 2   ? 50.218  79.977  31.869 1.000 79.926  0 2   ILE CCC CB  1 ? 5  
ATOM 1713  C CG1 . ILE B 1 2   ? 48.721  79.774  32.125 1.000 74.003  0 2   ILE CCC CG1 1 ? 5  
ATOM 1714  C CG2 . ILE B 1 2   ? 50.508  79.876  30.394 1.000 97.166  0 2   ILE CCC CG2 1 ? 5  
ATOM 1715  C CD1 . ILE B 1 2   ? 48.199  78.431  31.662 0.500 75.762  0 2   ILE CCC CD1 1 ? 5  
ATOM 1716  N N   . VAL B 1 3   ? 53.244  78.301  31.850 1.000 90.956  0 3   VAL CCC N   1 ? 5  
ATOM 1717  C CA  . VAL B 1 3   ? 54.690  78.387  31.729 1.000 102.790 0 3   VAL CCC CA  1 ? 5  
ATOM 1718  C C   . VAL B 1 3   ? 55.134  78.289  30.277 1.000 112.422 0 3   VAL CCC C   1 ? 5  
ATOM 1719  O O   . VAL B 1 3   ? 54.373  77.924  29.380 1.000 118.544 0 3   VAL CCC O   1 ? 5  
ATOM 1720  C CB  . VAL B 1 3   ? 55.382  77.291  32.556 1.000 109.204 0 3   VAL CCC CB  1 ? 5  
ATOM 1721  C CG1 . VAL B 1 3   ? 55.117  77.510  34.038 1.000 115.053 0 3   VAL CCC CG1 1 ? 5  
ATOM 1722  C CG2 . VAL B 1 3   ? 54.885  75.924  32.110 1.000 104.292 0 3   VAL CCC CG2 1 ? 5  
ATOM 1723  N N   . GLN B 1 4   ? 56.411  78.628  30.077 1.000 112.919 0 4   GLN CCC N   1 ? 5  
ATOM 1724  C CA  A GLN B 1 4   ? 56.996  78.860  28.763 1.000 123.818 0 4   GLN CCC CA  1 ? 5  
ATOM 1725  C C   . GLN B 1 4   ? 57.197  77.592  27.937 1.000 135.678 0 4   GLN CCC C   1 ? 5  
ATOM 1726  O O   . GLN B 1 4   ? 57.298  77.695  26.713 1.000 153.501 0 4   GLN CCC O   1 ? 5  
ATOM 1727  C CB  . GLN B 1 4   ? 58.343  79.567  28.932 1.000 130.681 0 4   GLN CCC CB  1 ? 5  
ATOM 1728  C CG  . GLN B 1 4   ? 58.309  81.069  28.719 1.000 135.331 0 4   GLN CCC CG  1 ? 5  
ATOM 1729  C CD  . GLN B 1 4   ? 58.306  81.456  27.252 1.000 140.508 0 4   GLN CCC CD  1 ? 5  
ATOM 1730  O OE1 . GLN B 1 4   ? 58.670  80.663  26.381 1.000 127.988 0 4   GLN CCC OE1 1 ? 5  
ATOM 1731  N NE2 . GLN B 1 4   ? 57.896  82.688  26.972 1.000 150.137 0 4   GLN CCC NE2 1 ? 5  
ATOM 1732  N N   . ASN B 1 5   ? 57.284  76.417  28.567 1.000 132.485 0 5   ASN CCC N   1 ? 5  
ATOM 1733  C CA  . ASN B 1 5   ? 57.659  75.164  27.907 1.000 142.241 0 5   ASN CCC CA  1 ? 5  
ATOM 1734  C C   . ASN B 1 5   ? 59.076  75.238  27.340 1.000 157.748 0 5   ASN CCC C   1 ? 5  
ATOM 1735  O O   . ASN B 1 5   ? 59.775  76.243  27.513 1.000 165.200 0 5   ASN CCC O   1 ? 5  
ATOM 1736  C CB  . ASN B 1 5   ? 56.671  74.822  26.777 1.000 139.395 0 5   ASN CCC CB  1 ? 5  
ATOM 1737  C CG  . ASN B 1 5   ? 56.675  73.350  26.403 1.000 146.446 0 5   ASN CCC CG  1 ? 5  
ATOM 1738  O OD1 . ASN B 1 5   ? 57.523  72.581  26.856 1.000 157.053 0 5   ASN CCC OD1 1 ? 5  
ATOM 1739  N ND2 . ASN B 1 5   ? 55.743  72.960  25.540 1.000 145.273 0 5   ASN CCC ND2 1 ? 5  
ATOM 1740  N N   . LEU B 1 6   ? 59.521  74.161  26.685 1.000 169.547 0 6   LEU CCC N   1 ? 5  
ATOM 1741  C CA  . LEU B 1 6   ? 60.850  74.163  26.086 1.000 162.760 0 6   LEU CCC CA  1 ? 5  
ATOM 1742  C C   . LEU B 1 6   ? 60.814  74.823  24.717 1.000 158.737 0 6   LEU CCC C   1 ? 5  
ATOM 1743  O O   . LEU B 1 6   ? 61.761  75.512  24.322 1.000 168.206 0 6   LEU CCC O   1 ? 5  
ATOM 1744  C CB  . LEU B 1 6   ? 61.383  72.734  26.002 1.000 168.609 0 6   LEU CCC CB  1 ? 5  
ATOM 1745  C CG  . LEU B 1 6   ? 61.267  72.023  27.357 1.000 174.327 0 6   LEU CCC CG  1 ? 5  
ATOM 1746  C CD1 . LEU B 1 6   ? 61.592  70.539  27.259 1.000 176.819 0 6   LEU CCC CD1 1 ? 5  
ATOM 1747  C CD2 . LEU B 1 6   ? 62.120  72.702  28.418 1.000 164.294 0 6   LEU CCC CD2 1 ? 5  
ATOM 1748  N N   . GLN B 1 7   ? 59.726  74.613  23.984 1.000 155.485 0 7   GLN CCC N   1 ? 5  
ATOM 1749  C CA  . GLN B 1 7   ? 59.404  75.391  22.804 1.000 160.670 0 7   GLN CCC CA  1 ? 5  
ATOM 1750  C C   . GLN B 1 7   ? 58.666  76.652  23.229 1.000 161.454 0 7   GLN CCC C   1 ? 5  
ATOM 1751  O O   . GLN B 1 7   ? 58.327  76.837  24.397 1.000 163.087 0 7   GLN CCC O   1 ? 5  
ATOM 1752  C CB  . GLN B 1 7   ? 58.574  74.570  21.821 1.000 165.644 0 7   GLN CCC CB  1 ? 5  
ATOM 1753  C CG  . GLN B 1 7   ? 59.112  73.172  21.625 1.000 176.588 0 7   GLN CCC CG  1 ? 5  
ATOM 1754  C CD  . GLN B 1 7   ? 58.515  72.477  20.423 1.000 190.104 0 7   GLN CCC CD  1 ? 5  
ATOM 1755  O OE1 . GLN B 1 7   ? 57.768  73.076  19.648 1.000 188.498 0 7   GLN CCC OE1 1 ? 5  
ATOM 1756  N NE2 . GLN B 1 7   ? 58.852  71.204  20.253 1.000 198.484 0 7   GLN CCC NE2 1 ? 5  
ATOM 1757  N N   . GLY B 1 8   ? 58.395  77.519  22.261 1.000 161.619 0 8   GLY CCC N   1 ? 5  
ATOM 1758  C CA  . GLY B 1 8   ? 57.807  78.801  22.585 1.000 158.266 0 8   GLY CCC CA  1 ? 5  
ATOM 1759  C C   . GLY B 1 8   ? 56.396  78.743  23.131 1.000 155.715 0 8   GLY CCC C   1 ? 5  
ATOM 1760  O O   . GLY B 1 8   ? 55.921  79.758  23.650 1.000 154.480 0 8   GLY CCC O   1 ? 5  
ATOM 1761  N N   . GLN B 1 9   ? 55.714  77.603  23.030 1.000 158.864 0 9   GLN CCC N   1 ? 5  
ATOM 1762  C CA  . GLN B 1 9   ? 54.296  77.582  23.360 1.000 154.167 0 9   GLN CCC CA  1 ? 5  
ATOM 1763  C C   . GLN B 1 9   ? 54.045  77.646  24.863 1.000 148.138 0 9   GLN CCC C   1 ? 5  
ATOM 1764  O O   . GLN B 1 9   ? 54.782  77.066  25.666 1.000 145.471 0 9   GLN CCC O   1 ? 5  
ATOM 1765  C CB  . GLN B 1 9   ? 53.673  76.301  22.819 1.000 150.391 0 9   GLN CCC CB  1 ? 5  
ATOM 1766  C CG  . GLN B 1 9   ? 54.054  75.990  21.397 1.000 161.674 0 9   GLN CCC CG  1 ? 5  
ATOM 1767  C CD  . GLN B 1 9   ? 53.990  74.510  21.099 1.000 174.316 0 9   GLN CCC CD  1 ? 5  
ATOM 1768  O OE1 . GLN B 1 9   ? 54.847  73.972  20.400 1.000 184.951 0 9   GLN CCC OE1 1 ? 5  
ATOM 1769  N NE2 . GLN B 1 9   ? 53.051  73.833  21.745 1.000 169.841 0 9   GLN CCC NE2 1 ? 5  
ATOM 1770  N N   . MET B 1 10  ? 52.978  78.356  25.224 1.000 131.910 0 10  MET CCC N   1 ? 5  
ATOM 1771  C CA  . MET B 1 10  ? 52.538  78.546  26.602 1.000 111.751 0 10  MET CCC CA  1 ? 5  
ATOM 1772  C C   . MET B 1 10  ? 51.637  77.388  27.023 1.000 107.171 0 10  MET CCC C   1 ? 5  
ATOM 1773  O O   . MET B 1 10  ? 50.566  77.199  26.436 1.000 103.289 0 10  MET CCC O   1 ? 5  
ATOM 1774  C CB  . MET B 1 10  ? 51.848  79.895  26.778 1.000 105.320 0 10  MET CCC CB  1 ? 5  
ATOM 1775  C CG  . MET B 1 10  ? 52.781  81.027  26.418 1.000 117.416 0 10  MET CCC CG  1 ? 5  
ATOM 1776  S SD  . MET B 1 10  ? 54.175  81.101  27.569 1.000 118.351 0 10  MET CCC SD  1 ? 5  
ATOM 1777  C CE  . MET B 1 10  ? 53.420  81.721  29.073 1.000 115.223 0 10  MET CCC CE  1 ? 5  
ATOM 1778  N N   . VAL B 1 11  ? 52.035  76.633  28.047 1.000 102.070 0 11  VAL CCC N   1 ? 5  
ATOM 1779  C CA  . VAL B 1 11  ? 51.262  75.466  28.449 1.000 97.950  0 11  VAL CCC CA  1 ? 5  
ATOM 1780  C C   . VAL B 1 11  ? 50.959  75.545  29.939 1.000 97.700  0 11  VAL CCC C   1 ? 5  
ATOM 1781  O O   . VAL B 1 11  ? 51.661  76.197  30.713 1.000 101.110 0 11  VAL CCC O   1 ? 5  
ATOM 1782  C CB  . VAL B 1 11  ? 51.975  74.131  28.124 1.000 104.511 0 11  VAL CCC CB  1 ? 5  
ATOM 1783  C CG1 . VAL B 1 11  ? 52.333  74.055  26.652 1.000 118.624 0 11  VAL CCC CG1 1 ? 5  
ATOM 1784  C CG2 . VAL B 1 11  ? 53.217  73.945  28.994 1.000 106.310 0 11  VAL CCC CG2 1 ? 5  
ATOM 1785  N N   . HIS B 1 12  ? 49.878  74.863  30.321 1.000 91.118  0 12  HIS CCC N   1 ? 5  
ATOM 1786  C CA  . HIS B 1 12  ? 49.468  74.743  31.712 1.000 85.589  0 12  HIS CCC CA  1 ? 5  
ATOM 1787  C C   . HIS B 1 12  ? 50.329  73.734  32.456 1.000 95.439  0 12  HIS CCC C   1 ? 5  
ATOM 1788  O O   . HIS B 1 12  ? 50.726  72.701  31.907 1.000 98.745  0 12  HIS CCC O   1 ? 5  
ATOM 1789  C CB  . HIS B 1 12  ? 48.001  74.324  31.797 1.000 89.680  0 12  HIS CCC CB  1 ? 5  
ATOM 1790  C CG  . HIS B 1 12  ? 47.496  74.153  33.196 1.000 86.904  0 12  HIS CCC CG  1 ? 5  
ATOM 1791  N ND1 . HIS B 1 12  ? 47.077  75.215  33.969 1.000 91.529  0 12  HIS CCC ND1 1 ? 5  
ATOM 1792  C CD2 . HIS B 1 12  ? 47.342  73.046  33.962 1.000 87.208  0 12  HIS CCC CD2 1 ? 5  
ATOM 1793  C CE1 . HIS B 1 12  ? 46.684  74.769  35.150 1.000 93.609  0 12  HIS CCC CE1 1 ? 5  
ATOM 1794  N NE2 . HIS B 1 12  ? 46.837  73.457  35.172 1.000 98.498  0 12  HIS CCC NE2 1 ? 5  
ATOM 1795  N N   . GLN B 1 13  ? 50.599  74.040  33.724 1.000 99.377  0 13  GLN CCC N   1 ? 5  
ATOM 1796  C CA  . GLN B 1 13  ? 51.313  73.154  34.628 1.000 100.156 0 13  GLN CCC CA  1 ? 5  
ATOM 1797  C C   . GLN B 1 13  ? 50.618  73.137  35.977 1.000 96.982  0 13  GLN CCC C   1 ? 5  
ATOM 1798  O O   . GLN B 1 13  ? 50.098  74.158  36.431 1.000 92.346  0 13  GLN CCC O   1 ? 5  
ATOM 1799  C CB  . GLN B 1 13  ? 52.763  73.609  34.838 1.000 104.615 0 13  GLN CCC CB  1 ? 5  
ATOM 1800  C CG  . GLN B 1 13  ? 53.781  72.488  34.880 1.000 125.363 0 13  GLN CCC CG  1 ? 5  
ATOM 1801  C CD  . GLN B 1 13  ? 55.207  72.998  34.769 1.000 135.074 0 13  GLN CCC CD  1 ? 5  
ATOM 1802  O OE1 . GLN B 1 13  ? 55.475  74.178  35.004 1.000 132.874 0 13  GLN CCC OE1 1 ? 5  
ATOM 1803  N NE2 . GLN B 1 13  ? 56.131  72.110  34.416 1.000 143.214 0 13  GLN CCC NE2 1 ? 5  
ATOM 1804  N N   . CYS B 1 14  ? 50.563  71.961  36.586 1.000 109.828 0 14  CYS CCC N   1 ? 5  
ATOM 1805  C CA  . CYS B 1 14  ? 49.932  71.828  37.888 1.000 113.674 0 14  CYS CCC CA  1 ? 5  
ATOM 1806  C C   . CYS B 1 14  ? 50.683  72.667  38.915 1.000 115.987 0 14  CYS CCC C   1 ? 5  
ATOM 1807  O O   . CYS B 1 14  ? 51.912  72.775  38.875 1.000 121.706 0 14  CYS CCC O   1 ? 5  
ATOM 1808  C CB  . CYS B 1 14  ? 49.868  70.364  38.298 1.000 117.555 0 14  CYS CCC CB  1 ? 5  
ATOM 1809  S SG  . CYS B 1 14  ? 48.843  69.425  37.145 1.000 139.775 0 14  CYS CCC SG  1 ? 5  
ATOM 1810  N N   . ILE B 1 15  ? 49.934  73.251  39.849 1.000 106.607 0 15  ILE CCC N   1 ? 5  
ATOM 1811  C CA  . ILE B 1 15  ? 50.561  73.913  40.983 1.000 98.268  0 15  ILE CCC CA  1 ? 5  
ATOM 1812  C C   . ILE B 1 15  ? 51.424  72.906  41.729 1.000 94.825  0 15  ILE CCC C   1 ? 5  
ATOM 1813  O O   . ILE B 1 15  ? 51.051  71.736  41.894 1.000 88.200  0 15  ILE CCC O   1 ? 5  
ATOM 1814  C CB  . ILE B 1 15  ? 49.492  74.547  41.889 1.000 93.840  0 15  ILE CCC CB  1 ? 5  
ATOM 1815  C CG1 . ILE B 1 15  ? 50.153  75.405  42.963 1.000 91.215  0 15  ILE CCC CG1 1 ? 5  
ATOM 1816  C CG2 . ILE B 1 15  ? 48.595  73.483  42.517 1.000 96.862  0 15  ILE CCC CG2 1 ? 5  
ATOM 1817  C CD1 . ILE B 1 15  ? 49.210  76.367  43.633 1.000 95.021  0 15  ILE CCC CD1 1 ? 5  
ATOM 1818  N N   . SER B 1 16  ? 52.641  73.348  42.128 1.000 89.492  0 16  SER CCC N   1 ? 5  
ATOM 1819  C CA  . SER B 1 16  ? 53.578  72.378  42.671 1.000 95.181  0 16  SER CCC CA  1 ? 5  
ATOM 1820  C C   . SER B 1 16  ? 53.348  72.138  44.160 1.000 88.615  0 16  SER CCC C   1 ? 5  
ATOM 1821  O O   . SER B 1 16  ? 52.901  73.026  44.885 1.000 89.171  0 16  SER CCC O   1 ? 5  
ATOM 1822  C CB  . SER B 1 16  ? 55.009  72.872  42.467 1.000 101.264 0 16  SER CCC CB  1 ? 5  
ATOM 1823  O OG  . SER B 1 16  ? 55.951  71.993  43.061 1.000 118.812 0 16  SER CCC OG  1 ? 5  
ATOM 1824  N N   . PRO B 1 17  ? 53.656  70.932  44.640 1.000 93.914  0 17  PRO CCC N   1 ? 5  
ATOM 1825  C CA  . PRO B 1 17  ? 53.584  70.688  46.088 1.000 92.313  0 17  PRO CCC CA  1 ? 5  
ATOM 1826  C C   . PRO B 1 17  ? 54.462  71.598  46.926 1.000 93.241  0 17  PRO CCC C   1 ? 5  
ATOM 1827  O O   . PRO B 1 17  ? 54.073  71.971  48.039 1.000 97.637  0 17  PRO CCC O   1 ? 5  
ATOM 1828  C CB  . PRO B 1 17  ? 54.026  69.222  46.207 1.000 89.036  0 17  PRO CCC CB  1 ? 5  
ATOM 1829  C CG  . PRO B 1 17  ? 53.676  68.615  44.900 1.000 83.524  0 17  PRO CCC CG  1 ? 5  
ATOM 1830  C CD  . PRO B 1 17  ? 53.902  69.695  43.881 1.000 87.862  0 17  PRO CCC CD  1 ? 5  
ATOM 1831  N N   . ARG B 1 18  ? 55.643  71.960  46.423 1.000 95.688  0 18  ARG CCC N   1 ? 5  
ATOM 1832  C CA  . ARG B 1 18  ? 56.507  72.887  47.146 1.000 96.760  0 18  ARG CCC CA  1 ? 5  
ATOM 1833  C C   . ARG B 1 18  ? 55.866  74.253  47.371 1.000 92.513  0 18  ARG CCC C   1 ? 5  
ATOM 1834  O O   . ARG B 1 18  ? 55.877  74.771  48.493 1.000 101.492 0 18  ARG CCC O   1 ? 5  
ATOM 1835  C CB  . ARG B 1 18  ? 57.841  73.034  46.407 1.000 106.354 0 18  ARG CCC CB  1 ? 5  
ATOM 1836  C CG  . ARG B 1 18  ? 59.049  72.781  47.305 1.000 120.927 0 18  ARG CCC CG  1 ? 5  
ATOM 1837  C CD  . ARG B 1 18  ? 60.286  72.333  46.540 1.000 137.323 0 18  ARG CCC CD  1 ? 5  
ATOM 1838  N NE  . ARG B 1 18  ? 61.389  71.995  47.436 1.000 151.936 0 18  ARG CCC NE  1 ? 5  
ATOM 1839  C CZ  . ARG B 1 18  ? 61.531  70.816  48.052 1.000 160.013 0 18  ARG CCC CZ  1 ? 5  
ATOM 1840  N NH1 . ARG B 1 18  ? 60.652  69.836  47.890 1.000 154.719 0 18  ARG CCC NH1 1 ? 5  
ATOM 1841  N NH2 . ARG B 1 18  ? 62.546  70.630  48.871 1.000 165.664 0 18  ARG CCC NH2 1 ? 5  
ATOM 1842  N N   . THR B 1 19  ? 55.276  74.845  46.332 1.000 87.645  0 19  THR CCC N   1 ? 5  
ATOM 1843  C CA  . THR B 1 19  ? 54.619  76.142  46.505 1.000 90.272  0 19  THR CCC CA  1 ? 5  
ATOM 1844  C C   . THR B 1 19  ? 53.432  76.080  47.479 1.000 90.245  0 19  THR CCC C   1 ? 5  
ATOM 1845  O O   . THR B 1 19  ? 53.326  76.918  48.385 1.000 92.749  0 19  THR CCC O   1 ? 5  
ATOM 1846  C CB  . THR B 1 19  ? 54.257  76.740  45.139 1.000 91.864  0 19  THR CCC CB  1 ? 5  
ATOM 1847  O OG1 . THR B 1 19  ? 53.671  78.035  45.312 1.000 93.443  0 19  THR CCC OG1 1 ? 5  
ATOM 1848  C CG2 . THR B 1 19  ? 53.333  75.861  44.350 1.000 98.670  0 19  THR CCC CG2 1 ? 5  
ATOM 1849  N N   . LEU B 1 20  ? 52.531  75.098  47.318 1.000 88.331  0 20  LEU CCC N   1 ? 5  
ATOM 1850  C CA  . LEU B 1 20  ? 51.362  74.996  48.199 1.000 88.822  0 20  LEU CCC CA  1 ? 5  
ATOM 1851  C C   . LEU B 1 20  ? 51.775  74.889  49.656 1.000 96.556  0 20  LEU CCC C   1 ? 5  
ATOM 1852  O O   . LEU B 1 20  ? 51.259  75.614  50.517 1.000 103.533 0 20  LEU CCC O   1 ? 5  
ATOM 1853  C CB  . LEU B 1 20  ? 50.466  73.811  47.826 1.000 85.493  0 20  LEU CCC CB  1 ? 5  
ATOM 1854  C CG  . LEU B 1 20  ? 49.674  73.886  46.527 1.000 94.533  0 20  LEU CCC CG  1 ? 5  
ATOM 1855  C CD1 . LEU B 1 20  ? 49.241  72.505  46.075 1.000 90.299  0 20  LEU CCC CD1 1 ? 5  
ATOM 1856  C CD2 . LEU B 1 20  ? 48.466  74.783  46.749 1.000 93.688  0 20  LEU CCC CD2 1 ? 5  
ATOM 1857  N N   . ASN B 1 21  ? 52.713  73.992  49.951 1.000 100.887 0 21  ASN CCC N   1 ? 5  
ATOM 1858  C CA  . ASN B 1 21  ? 53.144  73.833  51.331 1.000 103.623 0 21  ASN CCC CA  1 ? 5  
ATOM 1859  C C   . ASN B 1 21  ? 53.787  75.124  51.824 1.000 103.807 0 21  ASN CCC C   1 ? 5  
ATOM 1860  O O   . ASN B 1 21  ? 53.542  75.554  52.956 1.000 109.850 0 21  ASN CCC O   1 ? 5  
ATOM 1861  C CB  . ASN B 1 21  ? 54.111  72.655  51.431 1.000 106.377 0 21  ASN CCC CB  1 ? 5  
ATOM 1862  C CG  . ASN B 1 21  ? 54.485  72.330  52.853 1.000 115.079 0 21  ASN CCC CG  1 ? 5  
ATOM 1863  O OD1 . ASN B 1 21  ? 53.753  72.644  53.794 1.000 123.025 0 21  ASN CCC OD1 1 ? 5  
ATOM 1864  N ND2 . ASN B 1 21  ? 55.638  71.702  53.024 1.000 124.001 0 21  ASN CCC ND2 1 ? 5  
ATOM 1865  N N   . ALA B 1 22  ? 54.596  75.765  50.977 1.000 93.638  0 22  ALA CCC N   1 ? 5  
ATOM 1866  C CA  . ALA B 1 22  ? 55.235  77.026  51.348 1.000 93.672  0 22  ALA CCC CA  1 ? 5  
ATOM 1867  C C   . ALA B 1 22  ? 54.208  78.094  51.722 1.000 92.122  0 22  ALA CCC C   1 ? 5  
ATOM 1868  O O   . ALA B 1 22  ? 54.385  78.816  52.710 1.000 95.746  0 22  ALA CCC O   1 ? 5  
ATOM 1869  C CB  . ALA B 1 22  ? 56.131  77.521  50.215 1.000 97.205  0 22  ALA CCC CB  1 ? 5  
ATOM 1870  N N   . TRP B 1 23  ? 53.133  78.220  50.939 1.000 84.828  0 23  TRP CCC N   1 ? 5  
ATOM 1871  C CA  . TRP B 1 23  ? 52.118  79.232  51.226 1.000 82.655  0 23  TRP CCC CA  1 ? 5  
ATOM 1872  C C   . TRP B 1 23  ? 51.404  78.934  52.542 1.000 88.445  0 23  TRP CCC C   1 ? 5  
ATOM 1873  O O   . TRP B 1 23  ? 51.224  79.829  53.376 1.000 90.182  0 23  TRP CCC O   1 ? 5  
ATOM 1874  C CB  . TRP B 1 23  ? 51.124  79.321  50.071 1.000 78.450  0 23  TRP CCC CB  1 ? 5  
ATOM 1875  C CG  . TRP B 1 23  ? 49.971  80.223  50.339 1.000 76.092  0 23  TRP CCC CG  1 ? 5  
ATOM 1876  C CD1 . TRP B 1 23  ? 48.654  79.882  50.347 1.000 79.315  0 23  TRP CCC CD1 1 ? 5  
ATOM 1877  C CD2 . TRP B 1 23  ? 50.022  81.635  50.589 1.000 76.977  0 23  TRP CCC CD2 1 ? 5  
ATOM 1878  N NE1 . TRP B 1 23  ? 47.881  80.986  50.615 1.000 80.739  0 23  TRP CCC NE1 1 ? 5  
ATOM 1879  C CE2 . TRP B 1 23  ? 48.698  82.075  50.765 1.000 74.985  0 23  TRP CCC CE2 1 ? 5  
ATOM 1880  C CE3 . TRP B 1 23  ? 51.060  82.567  50.693 1.000 85.152  0 23  TRP CCC CE3 1 ? 5  
ATOM 1881  C CZ2 . TRP B 1 23  ? 48.382  83.403  51.040 1.000 75.540  0 23  TRP CCC CZ2 1 ? 5  
ATOM 1882  C CZ3 . TRP B 1 23  ? 50.743  83.887  50.969 1.000 82.367  0 23  TRP CCC CZ3 1 ? 5  
ATOM 1883  C CH2 . TRP B 1 23  ? 49.416  84.291  51.138 1.000 77.546  0 23  TRP CCC CH2 1 ? 5  
ATOM 1884  N N   . VAL B 1 24  ? 50.966  77.687  52.737 1.000 87.852  0 24  VAL CCC N   1 ? 5  
ATOM 1885  C CA  . VAL B 1 24  ? 50.321  77.319  53.996 1.000 88.842  0 24  VAL CCC CA  1 ? 5  
ATOM 1886  C C   . VAL B 1 24  ? 51.225  77.648  55.181 1.000 93.240  0 24  VAL CCC C   1 ? 5  
ATOM 1887  O O   . VAL B 1 24  ? 50.767  78.180  56.199 1.000 99.749  0 24  VAL CCC O   1 ? 5  
ATOM 1888  C CB  . VAL B 1 24  ? 49.939  75.826  53.983 1.000 90.118  0 24  VAL CCC CB  1 ? 5  
ATOM 1889  C CG1 . VAL B 1 24  ? 49.657  75.322  55.400 1.000 99.143  0 24  VAL CCC CG1 1 ? 5  
ATOM 1890  C CG2 . VAL B 1 24  ? 48.745  75.596  53.079 1.000 95.526  0 24  VAL CCC CG2 1 ? 5  
ATOM 1891  N N   . LYS B 1 25  ? 52.525  77.365  55.059 1.000 95.173  0 25  LYS CCC N   1 ? 5  
ATOM 1892  C CA  . LYS B 1 25  ? 53.437  77.574  56.183 1.000 97.044  0 25  LYS CCC CA  1 ? 5  
ATOM 1893  C C   . LYS B 1 25  ? 53.665  79.053  56.480 1.000 98.338  0 25  LYS CCC C   1 ? 5  
ATOM 1894  O O   . LYS B 1 25  ? 53.736  79.443  57.651 1.000 107.713 0 25  LYS CCC O   1 ? 5  
ATOM 1895  C CB  . LYS B 1 25  ? 54.764  76.865  55.931 1.000 100.768 0 25  LYS CCC CB  1 ? 5  
ATOM 1896  C CG  . LYS B 1 25  ? 54.656  75.348  55.892 1.000 104.601 0 25  LYS CCC CG  1 ? 5  
ATOM 1897  C CD  . LYS B 1 25  ? 53.790  74.827  57.035 1.000 118.424 0 25  LYS CCC CD  1 ? 5  
ATOM 1898  C CE  . LYS B 1 25  ? 53.560  73.324  56.934 1.000 128.733 0 25  LYS CCC CE  1 ? 5  
ATOM 1899  N NZ  . LYS B 1 25  ? 52.653  72.818  58.006 1.000 137.886 0 25  LYS CCC NZ  1 ? 5  
ATOM 1900  N N   . VAL B 1 26  ? 53.833  79.888  55.449 1.000 93.156  0 26  VAL CCC N   1 ? 5  
ATOM 1901  C CA  . VAL B 1 26  ? 54.066  81.312  55.698 1.000 94.620  0 26  VAL CCC CA  1 ? 5  
ATOM 1902  C C   . VAL B 1 26  ? 52.873  81.927  56.415 1.000 102.707 0 26  VAL CCC C   1 ? 5  
ATOM 1903  O O   . VAL B 1 26  ? 53.028  82.800  57.277 1.000 116.058 0 26  VAL CCC O   1 ? 5  
ATOM 1904  C CB  . VAL B 1 26  ? 54.411  82.067  54.399 1.000 89.896  0 26  VAL CCC CB  1 ? 5  
ATOM 1905  C CG1 . VAL B 1 26  ? 55.629  81.452  53.754 1.000 103.808 0 26  VAL CCC CG1 1 ? 5  
ATOM 1906  C CG2 . VAL B 1 26  ? 53.241  82.105  53.435 1.000 92.962  0 26  VAL CCC CG2 1 ? 5  
ATOM 1907  N N   . VAL B 1 27  ? 51.664  81.497  56.062 1.000 98.139  0 27  VAL CCC N   1 ? 5  
ATOM 1908  C CA  . VAL B 1 27  ? 50.487  81.976  56.774 1.000 102.198 0 27  VAL CCC CA  1 ? 5  
ATOM 1909  C C   . VAL B 1 27  ? 50.497  81.500  58.224 1.000 107.546 0 27  VAL CCC C   1 ? 5  
ATOM 1910  O O   . VAL B 1 27  ? 50.193  82.268  59.144 1.000 107.937 0 27  VAL CCC O   1 ? 5  
ATOM 1911  C CB  . VAL B 1 27  ? 49.219  81.540  56.027 1.000 94.937  0 27  VAL CCC CB  1 ? 5  
ATOM 1912  C CG1 . VAL B 1 27  ? 47.997  81.912  56.826 1.000 100.416 0 27  VAL CCC CG1 1 ? 5  
ATOM 1913  C CG2 . VAL B 1 27  ? 49.186  82.208  54.664 1.000 88.114  0 27  VAL CCC CG2 1 ? 5  
ATOM 1914  N N   . GLU B 1 28  ? 50.849  80.232  58.455 1.000 108.903 0 28  GLU CCC N   1 ? 5  
ATOM 1915  C CA  . GLU B 1 28  ? 50.917  79.718  59.820 1.000 110.219 0 28  GLU CCC CA  1 ? 5  
ATOM 1916  C C   . GLU B 1 28  ? 51.960  80.464  60.641 1.000 114.443 0 28  GLU CCC C   1 ? 5  
ATOM 1917  O O   . GLU B 1 28  ? 51.740  80.750  61.824 1.000 131.933 0 28  GLU CCC O   1 ? 5  
ATOM 1918  C CB  . GLU B 1 28  ? 51.237  78.223  59.816 1.000 114.013 0 28  GLU CCC CB  1 ? 5  
ATOM 1919  C CG  . GLU B 1 28  ? 50.069  77.315  59.464 1.000 127.338 0 28  GLU CCC CG  1 ? 5  
ATOM 1920  C CD  . GLU B 1 28  ? 50.456  75.842  59.457 1.000 141.376 0 28  GLU CCC CD  1 ? 5  
ATOM 1921  O OE1 . GLU B 1 28  ? 51.656  75.535  59.630 1.000 147.512 0 28  GLU CCC OE1 1 ? 5  
ATOM 1922  O OE2 . GLU B 1 28  ? 49.556  74.991  59.288 1.000 147.190 0 28  GLU CCC OE2 1 ? 5  
ATOM 1923  N N   . GLU B 1 29  ? 53.101  80.792  60.037 1.000 114.919 0 29  GLU CCC N   1 ? 5  
ATOM 1924  C CA  . GLU B 1 29  ? 54.176  81.376  60.827 1.000 118.794 0 29  GLU CCC CA  1 ? 5  
ATOM 1925  C C   . GLU B 1 29  ? 54.074  82.890  60.929 1.000 118.301 0 29  GLU CCC C   1 ? 5  
ATOM 1926  O O   . GLU B 1 29  ? 54.387  83.463  61.977 1.000 136.047 0 29  GLU CCC O   1 ? 5  
ATOM 1927  C CB  . GLU B 1 29  ? 55.528  81.036  60.195 1.000 127.391 0 29  GLU CCC CB  1 ? 5  
ATOM 1928  C CG  . GLU B 1 29  ? 55.928  79.581  60.234 1.000 145.980 0 29  GLU CCC CG  1 ? 5  
ATOM 1929  C CD  . GLU B 1 29  ? 57.016  79.270  59.217 1.000 155.619 0 29  GLU CCC CD  1 ? 5  
ATOM 1930  O OE1 . GLU B 1 29  ? 57.735  80.225  58.781 1.000 151.317 0 29  GLU CCC OE1 1 ? 5  
ATOM 1931  O OE2 . GLU B 1 29  ? 57.170  78.086  58.847 1.000 155.654 0 29  GLU CCC OE2 1 ? 5  
ATOM 1932  N N   . LYS B 1 30  ? 53.642  83.550  59.859 1.000 106.224 0 30  LYS CCC N   1 ? 5  
ATOM 1933  C CA  . LYS B 1 30  ? 53.627  85.003  59.795 1.000 110.573 0 30  LYS CCC CA  1 ? 5  
ATOM 1934  C C   . LYS B 1 30  ? 52.233  85.611  59.806 1.000 109.934 0 30  LYS CCC C   1 ? 5  
ATOM 1935  O O   . LYS B 1 30  ? 52.116  86.836  59.913 1.000 110.524 0 30  LYS CCC O   1 ? 5  
ATOM 1936  C CB  . LYS B 1 30  ? 54.427  85.497  58.580 1.000 114.490 0 30  LYS CCC CB  1 ? 5  
ATOM 1937  C CG  . LYS B 1 30  ? 55.894  85.054  58.632 1.000 121.443 0 30  LYS CCC CG  1 ? 5  
ATOM 1938  C CD  . LYS B 1 30  ? 56.779  85.791  57.633 1.000 134.288 0 30  LYS CCC CD  1 ? 5  
ATOM 1939  C CE  . LYS B 1 30  ? 58.243  85.732  58.055 1.000 144.737 0 30  LYS CCC CE  1 ? 5  
ATOM 1940  N NZ  . LYS B 1 30  ? 59.089  86.667  57.263 1.000 148.297 0 30  LYS CCC NZ  1 ? 5  
ATOM 1941  N N   . ALA B 1 31  ? 51.185  84.797  59.697 1.000 122.413 0 31  ALA CCC N   1 ? 5  
ATOM 1942  C CA  . ALA B 1 31  ? 49.809  85.273  59.608 1.000 124.260 0 31  ALA CCC CA  1 ? 5  
ATOM 1943  C C   . ALA B 1 31  ? 49.665  86.318  58.511 1.000 125.778 0 31  ALA CCC C   1 ? 5  
ATOM 1944  O O   . ALA B 1 31  ? 50.018  86.056  57.358 1.000 129.381 0 31  ALA CCC O   1 ? 5  
ATOM 1945  C CB  . ALA B 1 31  ? 49.345  85.847  60.950 1.000 127.988 0 31  ALA CCC CB  1 ? 5  
ATOM 1946  N N   . PHE B 1 32  ? 49.183  87.509  58.852 1.000 110.922 0 32  PHE CCC N   1 ? 5  
ATOM 1947  C CA  . PHE B 1 32  ? 49.029  88.597  57.891 1.000 106.809 0 32  PHE CCC CA  1 ? 5  
ATOM 1948  C C   . PHE B 1 32  ? 49.937  89.782  58.202 1.000 106.166 0 32  PHE CCC C   1 ? 5  
ATOM 1949  O O   . PHE B 1 32  ? 49.547  90.944  58.070 1.000 109.526 0 32  PHE CCC O   1 ? 5  
ATOM 1950  C CB  . PHE B 1 32  ? 47.567  89.012  57.795 1.000 104.550 0 32  PHE CCC CB  1 ? 5  
ATOM 1951  C CG  . PHE B 1 32  ? 46.693  87.928  57.256 1.000 102.690 0 32  PHE CCC CG  1 ? 5  
ATOM 1952  C CD1 . PHE B 1 32  ? 46.639  87.681  55.894 1.000 106.178 0 32  PHE CCC CD1 1 ? 5  
ATOM 1953  C CD2 . PHE B 1 32  ? 45.973  87.114  58.110 1.000 108.238 0 32  PHE CCC CD2 1 ? 5  
ATOM 1954  C CE1 . PHE B 1 32  ? 45.850  86.664  55.390 1.000 115.593 0 32  PHE CCC CE1 1 ? 5  
ATOM 1955  C CE2 . PHE B 1 32  ? 45.186  86.098  57.615 1.000 113.685 0 32  PHE CCC CE2 1 ? 5  
ATOM 1956  C CZ  . PHE B 1 32  ? 45.123  85.871  56.252 1.000 118.967 0 32  PHE CCC CZ  1 ? 5  
ATOM 1957  N N   . SER B 1 33  ? 51.170  89.482  58.594 1.000 104.972 0 33  SER CCC N   1 ? 5  
ATOM 1958  C CA  . SER B 1 33  ? 52.222  90.482  58.619 1.000 110.303 0 33  SER CCC CA  1 ? 5  
ATOM 1959  C C   . SER B 1 33  ? 52.483  90.987  57.200 1.000 106.791 0 33  SER CCC C   1 ? 5  
ATOM 1960  O O   . SER B 1 33  ? 52.328  90.238  56.231 1.000 113.349 0 33  SER CCC O   1 ? 5  
ATOM 1961  C CB  . SER B 1 33  ? 53.500  89.900  59.217 1.000 122.221 0 33  SER CCC CB  1 ? 5  
ATOM 1962  O OG  . SER B 1 33  ? 53.305  89.514  60.566 1.000 135.753 0 33  SER CCC OG  1 ? 5  
ATOM 1963  N N   . PRO B 1 34  ? 52.854  92.261  57.048 1.000 101.670 0 34  PRO CCC N   1 ? 5  
ATOM 1964  C CA  . PRO B 1 34  ? 52.937  92.856  55.700 1.000 104.032 0 34  PRO CCC CA  1 ? 5  
ATOM 1965  C C   . PRO B 1 34  ? 53.808  92.099  54.708 1.000 101.056 0 34  PRO CCC C   1 ? 5  
ATOM 1966  O O   . PRO B 1 34  ? 53.510  92.132  53.507 1.000 103.264 0 34  PRO CCC O   1 ? 5  
ATOM 1967  C CB  . PRO B 1 34  ? 53.519  94.251  55.974 1.000 112.046 0 34  PRO CCC CB  1 ? 5  
ATOM 1968  C CG  . PRO B 1 34  ? 54.103  94.171  57.352 1.000 110.367 0 34  PRO CCC CG  1 ? 5  
ATOM 1969  C CD  . PRO B 1 34  ? 53.222  93.228  58.092 1.000 105.662 0 34  PRO CCC CD  1 ? 5  
ATOM 1970  N N   . GLU B 1 35  ? 54.895  91.463  55.150 1.000 110.113 0 35  GLU CCC N   1 ? 5  
ATOM 1971  C CA  . GLU B 1 35  ? 55.789  90.758  54.230 1.000 109.475 0 35  GLU CCC CA  1 ? 5  
ATOM 1972  C C   . GLU B 1 35  ? 55.141  89.555  53.547 1.000 103.523 0 35  GLU CCC C   1 ? 5  
ATOM 1973  O O   . GLU B 1 35  ? 55.706  89.043  52.573 1.000 105.330 0 35  GLU CCC O   1 ? 5  
ATOM 1974  C CB  . GLU B 1 35  ? 57.069  90.311  54.948 1.000 118.472 0 35  GLU CCC CB  1 ? 5  
ATOM 1975  C CG  . GLU B 1 35  ? 56.888  89.169  55.953 1.000 121.625 0 35  GLU CCC CG  1 ? 5  
ATOM 1976  C CD  . GLU B 1 35  ? 56.535  89.676  57.336 1.000 125.859 0 35  GLU CCC CD  1 ? 5  
ATOM 1977  O OE1 . GLU B 1 35  ? 56.067  90.831  57.426 1.000 126.931 0 35  GLU CCC OE1 1 ? 5  
ATOM 1978  O OE2 . GLU B 1 35  ? 56.701  88.918  58.321 1.000 126.235 0 35  GLU CCC OE2 1 ? 5  
ATOM 1979  N N   . VAL B 1 36  ? 53.983  89.093  54.025 1.000 94.573  0 36  VAL CCC N   1 ? 5  
ATOM 1980  C CA  . VAL B 1 36  ? 53.310  87.957  53.404 1.000 92.641  0 36  VAL CCC CA  1 ? 5  
ATOM 1981  C C   . VAL B 1 36  ? 52.766  88.327  52.024 1.000 92.921  0 36  VAL CCC C   1 ? 5  
ATOM 1982  O O   . VAL B 1 36  ? 52.714  87.481  51.118 1.000 92.508  0 36  VAL CCC O   1 ? 5  
ATOM 1983  C CB  A VAL B 1 36  ? 52.199  87.449  54.348 1.000 92.011  0 36  VAL CCC CB  1 ? 5  
ATOM 1984  C CG1 A VAL B 1 36  ? 51.243  86.496  53.633 1.000 98.395  0 36  VAL CCC CG1 1 ? 5  
ATOM 1985  C CG2 A VAL B 1 36  ? 52.807  86.773  55.573 1.000 94.079  0 36  VAL CCC CG2 1 ? 5  
ATOM 1986  N N   . ILE B 1 37  ? 52.386  89.590  51.825 1.000 89.832  0 37  ILE CCC N   1 ? 5  
ATOM 1987  C CA  . ILE B 1 37  ? 51.850  90.003  50.528 1.000 87.535  0 37  ILE CCC CA  1 ? 5  
ATOM 1988  C C   . ILE B 1 37  ? 52.878  89.837  49.409 1.000 88.177  0 37  ILE CCC C   1 ? 5  
ATOM 1989  O O   . ILE B 1 37  ? 52.533  89.251  48.369 1.000 87.326  0 37  ILE CCC O   1 ? 5  
ATOM 1990  C CB  . ILE B 1 37  ? 51.277  91.431  50.631 1.000 87.359  0 37  ILE CCC CB  1 ? 5  
ATOM 1991  C CG1 . ILE B 1 37  ? 50.234  91.501  51.742 1.000 87.854  0 37  ILE CCC CG1 1 ? 5  
ATOM 1992  C CG2 . ILE B 1 37  ? 50.645  91.861  49.322 1.000 90.520  0 37  ILE CCC CG2 1 ? 5  
ATOM 1993  C CD1 . ILE B 1 37  ? 49.537  92.831  51.825 1.000 96.399  0 37  ILE CCC CD1 1 ? 5  
ATOM 1994  N N   . PRO B 1 38  ? 54.131  90.308  49.538 1.000 90.119  0 38  PRO CCC N   1 ? 5  
ATOM 1995  C CA  A PRO B 1 38  ? 55.114  90.004  48.482 1.000 91.171  0 38  PRO CCC CA  1 ? 5  
ATOM 1996  C C   . PRO B 1 38  ? 55.294  88.516  48.216 1.000 91.321  0 38  PRO CCC C   1 ? 5  
ATOM 1997  O O   . PRO B 1 38  ? 55.397  88.112  47.051 1.000 94.894  0 38  PRO CCC O   1 ? 5  
ATOM 1998  C CB  A PRO B 1 38  ? 56.415  90.624  49.021 1.000 94.010  0 38  PRO CCC CB  1 ? 5  
ATOM 1999  C CG  A PRO B 1 38  ? 56.022  91.395  50.268 1.000 95.271  0 38  PRO CCC CG  1 ? 5  
ATOM 2000  C CD  A PRO B 1 38  ? 54.547  91.516  50.267 1.000 92.465  0 38  PRO CCC CD  1 ? 5  
ATOM 2001  N N   . MET B 1 39  ? 55.365  87.696  49.273 1.000 92.110  0 39  MET CCC N   1 ? 5  
ATOM 2002  C CA  . MET B 1 39  ? 55.534  86.255  49.102 1.000 93.072  0 39  MET CCC CA  1 ? 5  
ATOM 2003  C C   . MET B 1 39  ? 54.403  85.649  48.292 1.000 90.606  0 39  MET CCC C   1 ? 5  
ATOM 2004  O O   . MET B 1 39  ? 54.642  84.817  47.407 1.000 94.412  0 39  MET CCC O   1 ? 5  
ATOM 2005  C CB  . MET B 1 39  ? 55.640  85.559  50.455 1.000 95.028  0 39  MET CCC CB  1 ? 5  
ATOM 2006  C CG  . MET B 1 39  ? 55.993  84.078  50.354 1.000 97.055  0 39  MET CCC CG  1 ? 5  
ATOM 2007  S SD  . MET B 1 39  ? 57.745  83.741  50.100 1.000 101.871 0 39  MET CCC SD  1 ? 5  
ATOM 2008  C CE  . MET B 1 39  ? 58.414  84.124  51.717 1.000 125.069 0 39  MET CCC CE  1 ? 5  
ATOM 2009  N N   . PHE B 1 40  ? 53.165  86.038  48.595 1.000 87.853  0 40  PHE CCC N   1 ? 5  
ATOM 2010  C CA  . PHE B 1 40  ? 52.024  85.583  47.810 1.000 86.497  0 40  PHE CCC CA  1 ? 5  
ATOM 2011  C C   . PHE B 1 40  ? 52.204  85.914  46.333 1.000 86.541  0 40  PHE CCC C   1 ? 5  
ATOM 2012  O O   . PHE B 1 40  ? 52.025  85.052  45.467 1.000 87.679  0 40  PHE CCC O   1 ? 5  
ATOM 2013  C CB  . PHE B 1 40  ? 50.746  86.214  48.345 1.000 87.177  0 40  PHE CCC CB  1 ? 5  
ATOM 2014  C CG  . PHE B 1 40  ? 49.522  85.879  47.538 1.000 83.560  0 40  PHE CCC CG  1 ? 5  
ATOM 2015  C CD1 . PHE B 1 40  ? 48.930  84.629  47.646 1.000 83.261  0 40  PHE CCC CD1 1 ? 5  
ATOM 2016  C CD2 . PHE B 1 40  ? 48.972  86.803  46.664 1.000 82.217  0 40  PHE CCC CD2 1 ? 5  
ATOM 2017  C CE1 . PHE B 1 40  ? 47.802  84.315  46.914 1.000 82.498  0 40  PHE CCC CE1 1 ? 5  
ATOM 2018  C CE2 . PHE B 1 40  ? 47.846  86.489  45.922 1.000 81.367  0 40  PHE CCC CE2 1 ? 5  
ATOM 2019  C CZ  . PHE B 1 40  ? 47.263  85.241  46.050 1.000 81.550  0 40  PHE CCC CZ  1 ? 5  
ATOM 2020  N N   . SER B 1 41  ? 52.585  87.154  46.022 1.000 86.163  0 41  SER CCC N   1 ? 5  
ATOM 2021  C CA  . SER B 1 41  ? 52.740  87.527  44.619 1.000 86.704  0 41  SER CCC CA  1 ? 5  
ATOM 2022  C C   . SER B 1 41  ? 53.810  86.675  43.924 1.000 91.125  0 41  SER CCC C   1 ? 5  
ATOM 2023  O O   . SER B 1 41  ? 53.631  86.267  42.773 1.000 97.202  0 41  SER CCC O   1 ? 5  
ATOM 2024  C CB  . SER B 1 41  ? 53.067  89.014  44.510 1.000 87.861  0 41  SER CCC CB  1 ? 5  
ATOM 2025  O OG  . SER B 1 41  ? 53.388  89.377  43.178 1.000 105.304 0 41  SER CCC OG  1 ? 5  
ATOM 2026  N N   . ALA B 1 42  ? 54.928  86.388  44.603 1.000 90.637  0 42  ALA CCC N   1 ? 5  
ATOM 2027  C CA  . ALA B 1 42  ? 55.988  85.587  43.986 1.000 91.242  0 42  ALA CCC CA  1 ? 5  
ATOM 2028  C C   . ALA B 1 42  ? 55.572  84.122  43.849 1.000 89.521  0 42  ALA CCC C   1 ? 5  
ATOM 2029  O O   . ALA B 1 42  ? 55.804  83.492  42.808 1.000 93.623  0 42  ALA CCC O   1 ? 5  
ATOM 2030  C CB  . ALA B 1 42  ? 57.260  85.688  44.823 1.000 94.861  0 42  ALA CCC CB  1 ? 5  
ATOM 2031  N N   . LEU B 1 43  ? 54.962  83.559  44.893 1.000 87.682  0 43  LEU CCC N   1 ? 5  
ATOM 2032  C CA  . LEU B 1 43  ? 54.495  82.179  44.824 1.000 88.340  0 43  LEU CCC CA  1 ? 5  
ATOM 2033  C C   . LEU B 1 43  ? 53.384  81.977  43.800 1.000 86.976  0 43  LEU CCC C   1 ? 5  
ATOM 2034  O O   . LEU B 1 43  ? 53.208  80.856  43.314 1.000 92.677  0 43  LEU CCC O   1 ? 5  
ATOM 2035  C CB  . LEU B 1 43  ? 54.034  81.710  46.205 1.000 89.035  0 43  LEU CCC CB  1 ? 5  
ATOM 2036  C CG  . LEU B 1 43  ? 55.164  81.515  47.218 1.000 91.418  0 43  LEU CCC CG  1 ? 5  
ATOM 2037  C CD1 . LEU B 1 43  ? 54.587  81.200  48.578 1.000 91.179  0 43  LEU CCC CD1 1 ? 5  
ATOM 2038  C CD2 . LEU B 1 43  ? 56.105  80.414  46.758 1.000 93.290  0 43  LEU CCC CD2 1 ? 5  
ATOM 2039  N N   . SER B 1 44  ? 52.634  83.023  43.455 1.000 84.798  0 44  SER CCC N   1 ? 5  
ATOM 2040  C CA  . SER B 1 44  ? 51.548  82.907  42.491 1.000 83.142  0 44  SER CCC CA  1 ? 5  
ATOM 2041  C C   . SER B 1 44  ? 51.923  83.404  41.101 1.000 84.187  0 44  SER CCC C   1 ? 5  
ATOM 2042  O O   . SER B 1 44  ? 51.038  83.806  40.334 1.000 86.303  0 44  SER CCC O   1 ? 5  
ATOM 2043  C CB  . SER B 1 44  ? 50.334  83.668  43.003 1.000 81.257  0 44  SER CCC CB  1 ? 5  
ATOM 2044  O OG  . SER B 1 44  ? 50.642  85.042  43.127 1.000 81.158  0 44  SER CCC OG  1 ? 5  
ATOM 2045  N N   . CYS B 1 45  ? 53.213  83.436  40.789 1.000 88.389  0 45  CYS CCC N   1 ? 5  
ATOM 2046  C CA  . CYS B 1 45  ? 53.663  83.851  39.472 1.000 88.748  0 45  CYS CCC CA  1 ? 5  
ATOM 2047  C C   . CYS B 1 45  ? 53.075  82.933  38.407 1.000 88.369  0 45  CYS CCC C   1 ? 5  
ATOM 2048  O O   . CYS B 1 45  ? 53.181  81.709  38.510 1.000 86.159  0 45  CYS CCC O   1 ? 5  
ATOM 2049  C CB  . CYS B 1 45  ? 55.196  83.827  39.427 1.000 89.805  0 45  CYS CCC CB  1 ? 5  
ATOM 2050  S SG  . CYS B 1 45  ? 55.918  84.455  37.902 1.000 109.708 0 45  CYS CCC SG  1 ? 5  
ATOM 2051  N N   . GLY B 1 46  ? 52.421  83.524  37.401 1.000 89.975  0 46  GLY CCC N   1 ? 5  
ATOM 2052  C CA  . GLY B 1 46  ? 51.833  82.727  36.336 1.000 85.233  0 46  GLY CCC CA  1 ? 5  
ATOM 2053  C C   . GLY B 1 46  ? 50.576  81.962  36.676 1.000 83.426  0 46  GLY CCC C   1 ? 5  
ATOM 2054  O O   . GLY B 1 46  ? 50.121  81.160  35.856 1.000 83.446  0 46  GLY CCC O   1 ? 5  
ATOM 2055  N N   . ALA B 1 47  ? 50.001  82.188  37.849 1.000 87.252  0 47  ALA CCC N   1 ? 5  
ATOM 2056  C CA  . ALA B 1 47  ? 48.881  81.387  38.321 1.000 84.305  0 47  ALA CCC CA  1 ? 5  
ATOM 2057  C C   . ALA B 1 47  ? 47.640  81.596  37.465 1.000 83.499  0 47  ALA CCC C   1 ? 5  
ATOM 2058  O O   . ALA B 1 47  ? 47.382  82.698  36.968 1.000 80.831  0 47  ALA CCC O   1 ? 5  
ATOM 2059  C CB  . ALA B 1 47  ? 48.566  81.719  39.776 1.000 82.164  0 47  ALA CCC CB  1 ? 5  
ATOM 2060  N N   . THR B 1 48  ? 46.903  80.509  37.252 1.000 82.439  0 48  THR CCC N   1 ? 5  
ATOM 2061  C CA  . THR B 1 48  ? 45.552  80.640  36.748 1.000 81.693  0 48  THR CCC CA  1 ? 5  
ATOM 2062  C C   . THR B 1 48  ? 44.642  81.094  37.885 1.000 86.374  0 48  THR CCC C   1 ? 5  
ATOM 2063  O O   . THR B 1 48  ? 45.021  81.034  39.059 1.000 97.941  0 48  THR CCC O   1 ? 5  
ATOM 2064  C CB  . THR B 1 48  ? 45.067  79.306  36.186 1.000 81.777  0 48  THR CCC CB  1 ? 5  
ATOM 2065  O OG1 . THR B 1 48  ? 45.015  78.330  37.235 1.000 80.962  0 48  THR CCC OG1 1 ? 5  
ATOM 2066  C CG2 . THR B 1 48  ? 46.011  78.817  35.109 1.000 82.964  0 48  THR CCC CG2 1 ? 5  
ATOM 2067  N N   . PRO B 1 49  ? 43.437  81.569  37.565 1.000 82.568  0 49  PRO CCC N   1 ? 5  
ATOM 2068  C CA  . PRO B 1 49  ? 42.465  81.829  38.638 1.000 80.690  0 49  PRO CCC CA  1 ? 5  
ATOM 2069  C C   . PRO B 1 49  ? 42.195  80.627  39.528 1.000 82.612  0 49  PRO CCC C   1 ? 5  
ATOM 2070  O O   . PRO B 1 49  ? 42.093  80.777  40.752 1.000 87.549  0 49  PRO CCC O   1 ? 5  
ATOM 2071  C CB  . PRO B 1 49  ? 41.213  82.247  37.857 1.000 81.433  0 49  PRO CCC CB  1 ? 5  
ATOM 2072  C CG  . PRO B 1 49  ? 41.761  82.920  36.637 1.000 81.588  0 49  PRO CCC CG  1 ? 5  
ATOM 2073  C CD  . PRO B 1 49  ? 43.017  82.155  36.280 1.000 81.424  0 49  PRO CCC CD  1 ? 5  
ATOM 2074  N N   . GLN B 1 50  ? 42.109  79.431  38.943 1.000 82.844  0 50  GLN CCC N   1 ? 5  
ATOM 2075  C CA  . GLN B 1 50  ? 41.968  78.211  39.734 1.000 85.359  0 50  GLN CCC CA  1 ? 5  
ATOM 2076  C C   . GLN B 1 50  ? 43.094  78.050  40.748 1.000 86.347  0 50  GLN CCC C   1 ? 5  
ATOM 2077  O O   . GLN B 1 50  ? 42.848  77.746  41.921 1.000 89.905  0 50  GLN CCC O   1 ? 5  
ATOM 2078  C CB  . GLN B 1 50  ? 41.897  76.999  38.809 1.000 87.690  0 50  GLN CCC CB  1 ? 5  
ATOM 2079  C CG  . GLN B 1 50  ? 41.509  75.722  39.530 1.000 97.558  0 50  GLN CCC CG  1 ? 5  
ATOM 2080  C CD  . GLN B 1 50  ? 41.654  74.495  38.656 1.000 101.042 0 50  GLN CCC CD  1 ? 5  
ATOM 2081  O OE1 . GLN B 1 50  ? 42.733  74.222  38.127 1.000 102.796 0 50  GLN CCC OE1 1 ? 5  
ATOM 2082  N NE2 . GLN B 1 50  ? 40.565  73.746  38.497 1.000 112.011 0 50  GLN CCC NE2 1 ? 5  
ATOM 2083  N N   . ASP B 1 51  ? 44.339  78.248  40.310 1.000 89.582  0 51  ASP CCC N   1 ? 5  
ATOM 2084  C CA  . ASP B 1 51  ? 45.489  78.105  41.202 1.000 84.340  0 51  ASP CCC CA  1 ? 5  
ATOM 2085  C C   . ASP B 1 51  ? 45.447  79.109  42.346 1.000 82.436  0 51  ASP CCC C   1 ? 5  
ATOM 2086  O O   . ASP B 1 51  ? 45.769  78.770  43.491 1.000 85.665  0 51  ASP CCC O   1 ? 5  
ATOM 2087  C CB  . ASP B 1 51  ? 46.771  78.241  40.390 1.000 86.097  0 51  ASP CCC CB  1 ? 5  
ATOM 2088  C CG  . ASP B 1 51  ? 46.964  77.086  39.423 1.000 94.726  0 51  ASP CCC CG  1 ? 5  
ATOM 2089  O OD1 . ASP B 1 51  ? 46.487  75.962  39.708 1.000 102.304 0 51  ASP CCC OD1 1 ? 5  
ATOM 2090  O OD2 . ASP B 1 51  ? 47.533  77.323  38.342 1.000 93.287  0 51  ASP CCC OD2 1 ? 5  
ATOM 2091  N N   . LEU B 1 52  ? 45.078  80.355  42.055 1.000 80.333  0 52  LEU CCC N   1 ? 5  
ATOM 2092  C CA  . LEU B 1 52  ? 44.987  81.360  43.108 1.000 80.292  0 52  LEU CCC CA  1 ? 5  
ATOM 2093  C C   . LEU B 1 52  ? 43.931  80.986  44.136 1.000 82.341  0 52  LEU CCC C   1 ? 5  
ATOM 2094  O O   . LEU B 1 52  ? 44.155  81.120  45.345 1.000 90.496  0 52  LEU CCC O   1 ? 5  
ATOM 2095  C CB  . LEU B 1 52  ? 44.690  82.735  42.515 1.000 78.698  0 52  LEU CCC CB  1 ? 5  
ATOM 2096  C CG  . LEU B 1 52  ? 45.784  83.311  41.627 1.000 78.112  0 52  LEU CCC CG  1 ? 5  
ATOM 2097  C CD1 . LEU B 1 52  ? 45.234  84.427  40.776 1.000 82.296  0 52  LEU CCC CD1 1 ? 5  
ATOM 2098  C CD2 . LEU B 1 52  ? 46.885  83.835  42.517 1.000 78.518  0 52  LEU CCC CD2 1 ? 5  
ATOM 2099  N N   . ASN B 1 53  ? 42.777  80.502  43.674 1.000 81.992  0 53  ASN CCC N   1 ? 5  
ATOM 2100  C CA  . ASN B 1 53  ? 41.733  80.068  44.596 1.000 82.205  0 53  ASN CCC CA  1 ? 5  
ATOM 2101  C C   . ASN B 1 53  ? 42.176  78.887  45.456 1.000 83.632  0 53  ASN CCC C   1 ? 5  
ATOM 2102  O O   . ASN B 1 53  ? 41.861  78.836  46.650 1.000 85.074  0 53  ASN CCC O   1 ? 5  
ATOM 2103  C CB  . ASN B 1 53  ? 40.488  79.696  43.794 1.000 82.687  0 53  ASN CCC CB  1 ? 5  
ATOM 2104  C CG  . ASN B 1 53  ? 39.777  80.911  43.228 1.000 82.309  0 53  ASN CCC CG  1 ? 5  
ATOM 2105  O OD1 . ASN B 1 53  ? 39.787  81.984  43.828 1.000 82.286  0 53  ASN CCC OD1 1 ? 5  
ATOM 2106  N ND2 . ASN B 1 53  ? 39.143  80.741  42.072 1.000 82.294  0 53  ASN CCC ND2 1 ? 5  
ATOM 2107  N N   . THR B 1 54  ? 42.878  77.914  44.865 1.000 85.888  0 54  THR CCC N   1 ? 5  
ATOM 2108  C CA  . THR B 1 54  ? 43.461  76.813  45.638 1.000 89.072  0 54  THR CCC CA  1 ? 5  
ATOM 2109  C C   . THR B 1 54  ? 44.362  77.322  46.758 1.000 88.269  0 54  THR CCC C   1 ? 5  
ATOM 2110  O O   . THR B 1 54  ? 44.245  76.890  47.909 1.000 90.768  0 54  THR CCC O   1 ? 5  
ATOM 2111  C CB  . THR B 1 54  ? 44.229  75.843  44.739 1.000 94.591  0 54  THR CCC CB  1 ? 5  
ATOM 2112  O OG1 . THR B 1 54  ? 45.172  76.562  43.938 1.000 105.075 0 54  THR CCC OG1 1 ? 5  
ATOM 2113  C CG2 . THR B 1 54  ? 43.263  75.067  43.842 1.000 100.042 0 54  THR CCC CG2 1 ? 5  
ATOM 2114  N N   . MET B 1 55  ? 45.281  78.232  46.433 1.000 85.040  0 55  MET CCC N   1 ? 5  
ATOM 2115  C CA  . MET B 1 55  ? 46.190  78.764  47.445 1.000 85.849  0 55  MET CCC CA  1 ? 5  
ATOM 2116  C C   . MET B 1 55  ? 45.428  79.408  48.593 1.000 86.286  0 55  MET CCC C   1 ? 5  
ATOM 2117  O O   . MET B 1 55  ? 45.735  79.170  49.766 1.000 89.365  0 55  MET CCC O   1 ? 5  
ATOM 2118  C CB  . MET B 1 55  ? 47.130  79.790  46.815 1.000 85.130  0 55  MET CCC CB  1 ? 5  
ATOM 2119  C CG  . MET B 1 55  ? 48.143  79.221  45.851 1.000 87.962  0 55  MET CCC CG  1 ? 5  
ATOM 2120  S SD  . MET B 1 55  ? 49.067  80.545  45.051 1.000 96.902  0 55  MET CCC SD  1 ? 5  
ATOM 2121  C CE  . MET B 1 55  ? 50.164  81.037  46.379 1.000 90.745  0 55  MET CCC CE  1 ? 5  
ATOM 2122  N N   . LEU B 1 56  ? 44.431  80.233  48.276 1.000 84.635  0 56  LEU CCC N   1 ? 5  
ATOM 2123  C CA  . LEU B 1 56  ? 43.646  80.880  49.321 1.000 84.754  0 56  LEU CCC CA  1 ? 5  
ATOM 2124  C C   . LEU B 1 56  ? 42.801  79.875  50.100 1.000 86.896  0 56  LEU CCC C   1 ? 5  
ATOM 2125  O O   . LEU B 1 56  ? 42.674  79.980  51.326 1.000 89.252  0 56  LEU CCC O   1 ? 5  
ATOM 2126  C CB  . LEU B 1 56  ? 42.763  81.965  48.701 1.000 82.925  0 56  LEU CCC CB  1 ? 5  
ATOM 2127  C CG  . LEU B 1 56  ? 43.485  83.126  48.004 1.000 81.289  0 56  LEU CCC CG  1 ? 5  
ATOM 2128  C CD1 . LEU B 1 56  ? 42.483  84.120  47.435 1.000 81.068  0 56  LEU CCC CD1 1 ? 5  
ATOM 2129  C CD2 . LEU B 1 56  ? 44.470  83.822  48.926 1.000 81.354  0 56  LEU CCC CD2 1 ? 5  
ATOM 2130  N N   . ASN B 1 57  ? 42.211  78.901  49.404 1.000 87.341  0 57  ASN CCC N   1 ? 5  
ATOM 2131  C CA  . ASN B 1 57  ? 41.346  77.914  50.046 1.000 90.053  0 57  ASN CCC CA  1 ? 5  
ATOM 2132  C C   . ASN B 1 57  ? 42.104  76.941  50.946 1.000 91.960  0 57  ASN CCC C   1 ? 5  
ATOM 2133  O O   . ASN B 1 57  ? 41.498  76.351  51.849 1.000 94.624  0 57  ASN CCC O   1 ? 5  
ATOM 2134  C CB  . ASN B 1 57  ? 40.552  77.148  48.993 1.000 91.004  0 57  ASN CCC CB  1 ? 5  
ATOM 2135  C CG  . ASN B 1 57  ? 39.420  77.972  48.415 1.000 94.418  0 57  ASN CCC CG  1 ? 5  
ATOM 2136  O OD1 . ASN B 1 57  ? 39.286  79.159  48.718 1.000 99.969  0 57  ASN CCC OD1 1 ? 5  
ATOM 2137  N ND2 . ASN B 1 57  ? 38.602  77.350  47.574 1.000 103.331 0 57  ASN CCC ND2 1 ? 5  
ATOM 2138  N N   . THR B 1 58  ? 43.399  76.716  50.707 1.000 92.131  0 58  THR CCC N   1 ? 5  
ATOM 2139  C CA  . THR B 1 58  ? 44.116  75.768  51.559 1.000 95.280  0 58  THR CCC CA  1 ? 5  
ATOM 2140  C C   . THR B 1 58  ? 44.452  76.336  52.928 1.000 95.650  0 58  THR CCC C   1 ? 5  
ATOM 2141  O O   . THR B 1 58  ? 44.885  75.576  53.802 1.000 96.394  0 58  THR CCC O   1 ? 5  
ATOM 2142  C CB  . THR B 1 58  ? 45.417  75.280  50.910 1.000 96.530  0 58  THR CCC CB  1 ? 5  
ATOM 2143  O OG1 . THR B 1 58  ? 46.246  76.394  50.553 1.000 94.946  0 58  THR CCC OG1 1 ? 5  
ATOM 2144  C CG2 . THR B 1 58  ? 45.115  74.446  49.689 1.000 97.344  0 58  THR CCC CG2 1 ? 5  
ATOM 2145  N N   . VAL B 1 59  ? 44.244  77.635  53.139 1.000 94.973  0 59  VAL CCC N   1 ? 5  
ATOM 2146  C CA  . VAL B 1 59  ? 44.453  78.226  54.452 1.000 96.170  0 59  VAL CCC CA  1 ? 5  
ATOM 2147  C C   . VAL B 1 59  ? 43.317  77.780  55.356 1.000 104.506 0 59  VAL CCC C   1 ? 5  
ATOM 2148  O O   . VAL B 1 59  ? 42.138  77.997  55.050 1.000 112.630 0 59  VAL CCC O   1 ? 5  
ATOM 2149  C CB  . VAL B 1 59  ? 44.523  79.755  54.354 1.000 92.209  0 59  VAL CCC CB  1 ? 5  
ATOM 2150  C CG1 . VAL B 1 59  ? 44.711  80.353  55.727 1.000 93.641  0 59  VAL CCC CG1 1 ? 5  
ATOM 2151  C CG2 . VAL B 1 59  ? 45.658  80.170  53.447 1.000 90.307  0 59  VAL CCC CG2 1 ? 5  
ATOM 2152  N N   . GLY B 1 60  ? 43.666  77.188  56.491 1.000 117.144 0 60  GLY CCC N   1 ? 5  
ATOM 2153  C CA  . GLY B 1 60  ? 42.672  76.640  57.390 1.000 122.416 0 60  GLY CCC CA  1 ? 5  
ATOM 2154  C C   . GLY B 1 60  ? 42.128  77.612  58.409 1.000 122.944 0 60  GLY CCC C   1 ? 5  
ATOM 2155  O O   . GLY B 1 60  ? 40.920  77.625  58.665 1.000 123.868 0 60  GLY CCC O   1 ? 5  
ATOM 2156  N N   . GLY B 1 61  ? 42.990  78.432  58.993 1.000 118.875 0 61  GLY CCC N   1 ? 5  
ATOM 2157  C CA  . GLY B 1 61  ? 42.578  79.386  59.998 1.000 119.337 0 61  GLY CCC CA  1 ? 5  
ATOM 2158  C C   . GLY B 1 61  ? 42.219  80.722  59.384 1.000 108.781 0 61  GLY CCC C   1 ? 5  
ATOM 2159  O O   . GLY B 1 61  ? 41.976  80.836  58.180 1.000 107.774 0 61  GLY CCC O   1 ? 5  
ATOM 2160  N N   . HIS B 1 62  ? 42.181  81.747  60.235 1.000 110.079 0 62  HIS CCC N   1 ? 5  
ATOM 2161  C CA  . HIS B 1 62  ? 42.048  83.136  59.793 1.000 104.281 0 62  HIS CCC CA  1 ? 5  
ATOM 2162  C C   . HIS B 1 62  ? 40.827  83.288  58.899 1.000 101.303 0 62  HIS CCC C   1 ? 5  
ATOM 2163  O O   . HIS B 1 62  ? 40.828  84.055  57.934 1.000 104.407 0 62  HIS CCC O   1 ? 5  
ATOM 2164  C CB  . HIS B 1 62  ? 43.296  83.617  59.057 1.000 104.024 0 62  HIS CCC CB  1 ? 5  
ATOM 2165  C CG  . HIS B 1 62  ? 44.561  83.457  59.834 1.000 105.141 0 62  HIS CCC CG  1 ? 5  
ATOM 2166  N ND1 . HIS B 1 62  ? 44.843  84.206  60.955 1.000 108.932 0 62  HIS CCC ND1 1 ? 5  
ATOM 2167  C CD2 . HIS B 1 62  ? 45.626  82.644  59.644 1.000 105.755 0 62  HIS CCC CD2 1 ? 5  
ATOM 2168  C CE1 . HIS B 1 62  ? 46.026  83.856  61.427 1.000 119.917 0 62  HIS CCC CE1 1 ? 5  
ATOM 2169  N NE2 . HIS B 1 62  ? 46.522  82.910  60.650 1.000 112.193 0 62  HIS CCC NE2 1 ? 5  
ATOM 2170  N N   . GLN B 1 63  ? 39.760  82.567  59.241 1.000 100.528 0 63  GLN CCC N   1 ? 5  
ATOM 2171  C CA  . GLN B 1 63  ? 38.596  82.542  58.371 1.000 99.395  0 63  GLN CCC CA  1 ? 5  
ATOM 2172  C C   . GLN B 1 63  ? 37.846  83.861  58.378 1.000 102.099 0 63  GLN CCC C   1 ? 5  
ATOM 2173  O O   . GLN B 1 63  ? 37.100  84.139  57.434 1.000 107.880 0 63  GLN CCC O   1 ? 5  
ATOM 2174  C CB  . GLN B 1 63  ? 37.674  81.388  58.765 1.000 98.701  0 63  GLN CCC CB  1 ? 5  
ATOM 2175  C CG  . GLN B 1 63  ? 38.267  80.025  58.449 1.000 104.321 0 63  GLN CCC CG  1 ? 5  
ATOM 2176  C CD  . GLN B 1 63  ? 38.546  79.848  56.964 1.000 109.480 0 63  GLN CCC CD  1 ? 5  
ATOM 2177  O OE1 . GLN B 1 63  ? 37.626  79.787  56.148 1.000 116.662 0 63  GLN CCC OE1 1 ? 5  
ATOM 2178  N NE2 . GLN B 1 63  ? 39.824  79.786  56.607 1.000 113.541 0 63  GLN CCC NE2 1 ? 5  
ATOM 2179  N N   . ALA B 1 64  ? 38.023  84.678  59.417 1.000 103.458 0 64  ALA CCC N   1 ? 5  
ATOM 2180  C CA  . ALA B 1 64  ? 37.493  86.034  59.370 1.000 111.020 0 64  ALA CCC CA  1 ? 5  
ATOM 2181  C C   . ALA B 1 64  ? 38.148  86.826  58.250 1.000 108.938 0 64  ALA CCC C   1 ? 5  
ATOM 2182  O O   . ALA B 1 64  ? 37.465  87.454  57.430 1.000 109.559 0 64  ALA CCC O   1 ? 5  
ATOM 2183  C CB  . ALA B 1 64  ? 37.715  86.726  60.714 1.000 116.418 0 64  ALA CCC CB  1 ? 5  
ATOM 2184  N N   . ALA B 1 65  ? 39.479  86.775  58.180 1.000 102.535 0 65  ALA CCC N   1 ? 5  
ATOM 2185  C CA  . ALA B 1 65  ? 40.187  87.457  57.106 1.000 101.092 0 65  ALA CCC CA  1 ? 5  
ATOM 2186  C C   . ALA B 1 65  ? 39.785  86.898  55.748 1.000 104.253 0 65  ALA CCC C   1 ? 5  
ATOM 2187  O O   . ALA B 1 65  ? 39.552  87.656  54.800 1.000 110.482 0 65  ALA CCC O   1 ? 5  
ATOM 2188  C CB  . ALA B 1 65  ? 41.695  87.344  57.319 1.000 99.752  0 65  ALA CCC CB  1 ? 5  
ATOM 2189  N N   . MET B 1 66  ? 39.681  85.569  55.643 1.000 103.725 0 66  MET CCC N   1 ? 5  
ATOM 2190  C CA  . MET B 1 66  ? 39.335  84.950  54.368 1.000 103.084 0 66  MET CCC CA  1 ? 5  
ATOM 2191  C C   . MET B 1 66  ? 37.938  85.354  53.914 1.000 99.056  0 66  MET CCC C   1 ? 5  
ATOM 2192  O O   . MET B 1 66  ? 37.715  85.617  52.728 1.000 102.738 0 66  MET CCC O   1 ? 5  
ATOM 2193  C CB  . MET B 1 66  ? 39.443  83.429  54.478 1.000 101.399 0 66  MET CCC CB  1 ? 5  
ATOM 2194  C CG  . MET B 1 66  ? 40.815  82.931  54.916 1.000 95.223  0 66  MET CCC CG  1 ? 5  
ATOM 2195  S SD  . MET B 1 66  ? 42.170  83.560  53.905 1.000 88.540  0 66  MET CCC SD  1 ? 5  
ATOM 2196  C CE  . MET B 1 66  ? 41.664  82.993  52.284 1.000 101.622 0 66  MET CCC CE  1 ? 5  
ATOM 2197  N N   . GLN B 1 67  ? 36.984  85.403  54.843 1.000 99.994  0 67  GLN CCC N   1 ? 5  
ATOM 2198  C CA  . GLN B 1 67  ? 35.638  85.833  54.484 1.000 106.510 0 67  GLN CCC CA  1 ? 5  
ATOM 2199  C C   . GLN B 1 67  ? 35.608  87.315  54.140 1.000 107.464 0 67  GLN CCC C   1 ? 5  
ATOM 2200  O O   . GLN B 1 67  ? 34.910  87.733  53.208 1.000 111.275 0 67  GLN CCC O   1 ? 5  
ATOM 2201  C CB  . GLN B 1 67  ? 34.666  85.519  55.617 1.000 106.790 0 67  GLN CCC CB  1 ? 5  
ATOM 2202  C CG  . GLN B 1 67  ? 33.215  85.623  55.205 1.000 110.766 0 67  GLN CCC CG  1 ? 5  
ATOM 2203  C CD  . GLN B 1 67  ? 32.729  84.354  54.544 1.000 119.540 0 67  GLN CCC CD  1 ? 5  
ATOM 2204  O OE1 . GLN B 1 67  ? 33.205  83.259  54.854 1.000 113.961 0 67  GLN CCC OE1 1 ? 5  
ATOM 2205  N NE2 . GLN B 1 67  ? 31.790  84.491  53.616 1.000 135.273 0 67  GLN CCC NE2 1 ? 5  
ATOM 2206  N N   . MET B 1 68  ? 36.361  88.121  54.883 1.000 104.158 0 68  MET CCC N   1 ? 5  
ATOM 2207  C CA  . MET B 1 68  ? 36.514  89.528  54.540 1.000 106.937 0 68  MET CCC CA  1 ? 5  
ATOM 2208  C C   . MET B 1 68  ? 37.152  89.680  53.162 1.000 104.549 0 68  MET CCC C   1 ? 5  
ATOM 2209  O O   . MET B 1 68  ? 36.761  90.554  52.378 1.000 111.845 0 68  MET CCC O   1 ? 5  
ATOM 2210  C CB  . MET B 1 68  ? 37.304  90.229  55.643 1.000 109.823 0 68  MET CCC CB  1 ? 5  
ATOM 2211  C CG  . MET B 1 68  ? 37.135  91.735  55.683 1.000 121.136 0 68  MET CCC CG  1 ? 5  
ATOM 2212  S SD  . MET B 1 68  ? 38.300  92.582  56.781 1.000 121.632 0 68  MET CCC SD  1 ? 5  
ATOM 2213  C CE  . MET B 1 68  ? 38.834  91.237  57.839 1.000 114.913 0 68  MET CCC CE  1 ? 5  
ATOM 2214  N N   . LEU B 1 69  ? 38.156  88.849  52.862 1.000 101.114 0 69  LEU CCC N   1 ? 5  
ATOM 2215  C CA  . LEU B 1 69  ? 38.797  88.856  51.546 1.000 105.038 0 69  LEU CCC CA  1 ? 5  
ATOM 2216  C C   . LEU B 1 69  ? 37.802  88.541  50.430 1.000 108.074 0 69  LEU CCC C   1 ? 5  
ATOM 2217  O O   . LEU B 1 69  ? 37.852  89.150  49.354 1.000 109.813 0 69  LEU CCC O   1 ? 5  
ATOM 2218  C CB  . LEU B 1 69  ? 39.948  87.849  51.527 1.000 102.124 0 69  LEU CCC CB  1 ? 5  
ATOM 2219  C CG  . LEU B 1 69  ? 40.791  87.753  50.258 1.000 96.078  0 69  LEU CCC CG  1 ? 5  
ATOM 2220  C CD1 . LEU B 1 69  ? 41.312  89.124  49.858 1.000 97.815  0 69  LEU CCC CD1 1 ? 5  
ATOM 2221  C CD2 . LEU B 1 69  ? 41.930  86.765  50.467 1.000 93.386  0 69  LEU CCC CD2 1 ? 5  
ATOM 2222  N N   . LYS B 1 70  ? 36.907  87.575  50.659 1.000 104.675 0 70  LYS CCC N   1 ? 5  
ATOM 2223  C CA  . LYS B 1 70  ? 35.896  87.233  49.661 1.000 102.198 0 70  LYS CCC CA  1 ? 5  
ATOM 2224  C C   . LYS B 1 70  ? 35.016  88.432  49.343 1.000 104.071 0 70  LYS CCC C   1 ? 5  
ATOM 2225  O O   . LYS B 1 70  ? 34.689  88.685  48.178 1.000 110.302 0 70  LYS CCC O   1 ? 5  
ATOM 2226  C CB  . LYS B 1 70  ? 35.032  86.072  50.158 1.000 103.021 0 70  LYS CCC CB  1 ? 5  
ATOM 2227  C CG  . LYS B 1 70  ? 35.736  84.732  50.296 1.000 107.383 0 70  LYS CCC CG  1 ? 5  
ATOM 2228  C CD  . LYS B 1 70  ? 36.225  84.207  48.959 1.000 124.731 0 70  LYS CCC CD  1 ? 5  
ATOM 2229  C CE  . LYS B 1 70  ? 36.965  82.889  49.130 1.000 125.712 0 70  LYS CCC CE  1 ? 5  
ATOM 2230  N NZ  . LYS B 1 70  ? 37.490  82.374  47.834 1.000 115.354 0 70  LYS CCC NZ  1 ? 5  
ATOM 2231  N N   . GLU B 1 71  ? 34.634  89.185  50.372 1.000 106.301 0 71  GLU CCC N   1 ? 5  
ATOM 2232  C CA  . GLU B 1 71  ? 33.846  90.399  50.189 1.000 111.653 0 71  GLU CCC CA  1 ? 5  
ATOM 2233  C C   . GLU B 1 71  ? 34.560  91.417  49.301 1.000 109.520 0 71  GLU CCC C   1 ? 5  
ATOM 2234  O O   . GLU B 1 71  ? 33.934  92.033  48.431 1.000 112.254 0 71  GLU CCC O   1 ? 5  
ATOM 2235  C CB  . GLU B 1 71  ? 33.507  90.965  51.566 1.000 127.646 0 71  GLU CCC CB  1 ? 5  
ATOM 2236  C CG  . GLU B 1 71  ? 32.455  90.109  52.275 1.000 140.273 0 71  GLU CCC CG  1 ? 5  
ATOM 2237  C CD  . GLU B 1 71  ? 31.893  90.756  53.523 1.000 145.778 0 71  GLU CCC CD  1 ? 5  
ATOM 2238  O OE1 . GLU B 1 71  ? 32.581  91.635  54.113 1.000 145.148 0 71  GLU CCC OE1 1 ? 5  
ATOM 2239  O OE2 . GLU B 1 71  ? 30.738  90.448  53.898 1.000 143.531 0 71  GLU CCC OE2 1 ? 5  
ATOM 2240  N N   . THR B 1 72  ? 35.859  91.626  49.516 1.000 107.579 0 72  THR CCC N   1 ? 5  
ATOM 2241  C CA  . THR B 1 72  ? 36.601  92.583  48.696 1.000 111.781 0 72  THR CCC CA  1 ? 5  
ATOM 2242  C C   . THR B 1 72  ? 36.658  92.138  47.236 1.000 107.192 0 72  THR CCC C   1 ? 5  
ATOM 2243  O O   . THR B 1 72  ? 36.506  92.958  46.322 1.000 109.776 0 72  THR CCC O   1 ? 5  
ATOM 2244  C CB  . THR B 1 72  ? 38.007  92.787  49.262 1.000 113.387 0 72  THR CCC CB  1 ? 5  
ATOM 2245  O OG1 . THR B 1 72  ? 37.918  93.351  50.579 1.000 117.627 0 72  THR CCC OG1 1 ? 5  
ATOM 2246  C CG2 . THR B 1 72  ? 38.822  93.711  48.362 1.000 109.292 0 72  THR CCC CG2 1 ? 5  
ATOM 2247  N N   . ILE B 1 73  ? 36.899  90.846  47.001 1.000 102.505 0 73  ILE CCC N   1 ? 5  
ATOM 2248  C CA  . ILE B 1 73  ? 36.911  90.300  45.645 1.000 102.013 0 73  ILE CCC CA  1 ? 5  
ATOM 2249  C C   . ILE B 1 73  ? 35.578  90.540  44.943 1.000 107.584 0 73  ILE CCC C   1 ? 5  
ATOM 2250  O O   . ILE B 1 73  ? 35.538  90.955  43.779 1.000 110.814 0 73  ILE CCC O   1 ? 5  
ATOM 2251  C CB  . ILE B 1 73  ? 37.251  88.799  45.697 1.000 97.409  0 73  ILE CCC CB  1 ? 5  
ATOM 2252  C CG1 . ILE B 1 73  ? 38.712  88.599  46.088 1.000 94.747  0 73  ILE CCC CG1 1 ? 5  
ATOM 2253  C CG2 . ILE B 1 73  ? 36.952  88.131  44.370 1.000 96.626  0 73  ILE CCC CG2 1 ? 5  
ATOM 2254  C CD1 . ILE B 1 73  ? 39.039  87.182  46.444 1.000 92.700  0 73  ILE CCC CD1 1 ? 5  
ATOM 2255  N N   . ASN B 1 74  ? 34.468  90.293  45.640 1.000 110.920 0 74  ASN CCC N   1 ? 5  
ATOM 2256  C CA  . ASN B 1 74  ? 33.147  90.487  45.047 1.000 113.216 0 74  ASN CCC CA  1 ? 5  
ATOM 2257  C C   . ASN B 1 74  ? 32.895  91.950  44.696 1.000 119.420 0 74  ASN CCC C   1 ? 5  
ATOM 2258  O O   . ASN B 1 74  ? 32.292  92.250  43.660 1.000 126.633 0 74  ASN CCC O   1 ? 5  
ATOM 2259  C CB  . ASN B 1 74  ? 32.065  89.967  45.992 1.000 117.118 0 74  ASN CCC CB  1 ? 5  
ATOM 2260  C CG  . ASN B 1 74  ? 32.069  88.456  46.093 1.000 118.500 0 74  ASN CCC CG  1 ? 5  
ATOM 2261  O OD1 . ASN B 1 74  ? 32.601  87.770  45.219 1.000 120.045 0 74  ASN CCC OD1 1 ? 5  
ATOM 2262  N ND2 . ASN B 1 74  ? 31.493  87.929  47.168 1.000 119.248 0 74  ASN CCC ND2 1 ? 5  
ATOM 2263  N N   . GLU B 1 75  ? 33.346  92.871  45.547 1.000 137.043 0 75  GLU CCC N   1 ? 5  
ATOM 2264  C CA  . GLU B 1 75  ? 33.244  94.292  45.228 1.000 143.831 0 75  GLU CCC CA  1 ? 5  
ATOM 2265  C C   . GLU B 1 75  ? 34.014  94.629  43.953 1.000 139.676 0 75  GLU CCC C   1 ? 5  
ATOM 2266  O O   . GLU B 1 75  ? 33.516  95.357  43.086 1.000 144.356 0 75  GLU CCC O   1 ? 5  
ATOM 2267  C CB  . GLU B 1 75  ? 33.764  95.108  46.414 1.000 158.222 0 75  GLU CCC CB  1 ? 5  
ATOM 2268  C CG  . GLU B 1 75  ? 34.360  96.467  46.074 1.000 175.105 0 75  GLU CCC CG  1 ? 5  
ATOM 2269  C CD  . GLU B 1 75  ? 34.713  97.274  47.320 1.000 189.771 0 75  GLU CCC CD  1 ? 5  
ATOM 2270  O OE1 . GLU B 1 75  ? 34.131  96.996  48.392 1.000 196.006 0 75  GLU CCC OE1 1 ? 5  
ATOM 2271  O OE2 . GLU B 1 75  ? 35.567  98.186  47.229 1.000 195.700 0 75  GLU CCC OE2 1 ? 5  
ATOM 2272  N N   . GLU B 1 76  ? 35.236  94.112  43.825 1.000 124.429 0 76  GLU CCC N   1 ? 5  
ATOM 2273  C CA  . GLU B 1 76  ? 36.039  94.368  42.631 1.000 122.803 0 76  GLU CCC CA  1 ? 5  
ATOM 2274  C C   . GLU B 1 76  ? 35.451  93.691  41.395 1.000 119.299 0 76  GLU CCC C   1 ? 5  
ATOM 2275  O O   . GLU B 1 76  ? 35.537  94.231  40.285 1.000 120.452 0 76  GLU CCC O   1 ? 5  
ATOM 2276  C CB  . GLU B 1 76  ? 37.482  93.927  42.864 1.000 112.724 0 76  GLU CCC CB  1 ? 5  
ATOM 2277  C CG  . GLU B 1 76  ? 38.185  94.761  43.910 1.000 114.728 0 76  GLU CCC CG  1 ? 5  
ATOM 2278  C CD  . GLU B 1 76  ? 38.298  96.216  43.503 1.000 127.138 0 76  GLU CCC CD  1 ? 5  
ATOM 2279  O OE1 . GLU B 1 76  ? 38.554  96.472  42.308 1.000 126.688 0 76  GLU CCC OE1 1 ? 5  
ATOM 2280  O OE2 . GLU B 1 76  ? 38.138  97.098  44.375 1.000 145.682 0 76  GLU CCC OE2 1 ? 5  
ATOM 2281  N N   . ALA B 1 77  ? 34.861  92.505  41.567 1.000 114.317 0 77  ALA CCC N   1 ? 5  
ATOM 2282  C CA  . ALA B 1 77  ? 34.209  91.821  40.454 1.000 111.667 0 77  ALA CCC CA  1 ? 5  
ATOM 2283  C C   . ALA B 1 77  ? 33.049  92.638  39.899 1.000 117.813 0 77  ALA CCC C   1 ? 5  
ATOM 2284  O O   . ALA B 1 77  ? 32.868  92.722  38.678 1.000 125.624 0 77  ALA CCC O   1 ? 5  
ATOM 2285  C CB  . ALA B 1 77  ? 33.725  90.440  40.899 1.000 109.771 0 77  ALA CCC CB  1 ? 5  
ATOM 2286  N N   . ALA B 1 78  ? 32.242  93.230  40.778 1.000 121.390 0 78  ALA CCC N   1 ? 5  
ATOM 2287  C CA  . ALA B 1 78  ? 31.116  94.040  40.325 1.000 124.384 0 78  ALA CCC CA  1 ? 5  
ATOM 2288  C C   . ALA B 1 78  ? 31.597  95.253  39.540 1.000 127.151 0 78  ALA CCC C   1 ? 5  
ATOM 2289  O O   . ALA B 1 78  ? 31.023  95.598  38.500 1.000 135.746 0 78  ALA CCC O   1 ? 5  
ATOM 2290  C CB  . ALA B 1 78  ? 30.265  94.473  41.518 1.000 125.457 0 78  ALA CCC CB  1 ? 5  
ATOM 2291  N N   . GLU B 1 79  ? 32.663  95.902  40.015 1.000 125.350 0 79  GLU CCC N   1 ? 5  
ATOM 2292  C CA  . GLU B 1 79  ? 33.221  97.048  39.302 1.000 131.125 0 79  GLU CCC CA  1 ? 5  
ATOM 2293  C C   . GLU B 1 79  ? 33.785  96.643  37.943 1.000 130.869 0 79  GLU CCC C   1 ? 5  
ATOM 2294  O O   . GLU B 1 79  ? 33.679  97.403  36.972 1.000 136.129 0 79  GLU CCC O   1 ? 5  
ATOM 2295  C CB  . GLU B 1 79  ? 34.311  97.705  40.150 1.000 130.939 0 79  GLU CCC CB  1 ? 5  
ATOM 2296  C CG  . GLU B 1 79  ? 34.964  98.975  39.568 1.000 143.426 0 79  GLU CCC CG  1 ? 5  
ATOM 2297  C CD  . GLU B 1 79  ? 34.008  100.149 39.332 1.000 155.443 0 79  GLU CCC CD  1 ? 5  
ATOM 2298  O OE1 . GLU B 1 79  ? 32.769  99.976  39.353 1.000 160.054 0 79  GLU CCC OE1 1 ? 5  
ATOM 2299  O OE2 . GLU B 1 79  ? 34.516  101.274 39.128 1.000 160.007 0 79  GLU CCC OE2 1 ? 5  
ATOM 2300  N N   . TRP B 1 80  ? 34.393  95.458  37.853 1.000 126.234 0 80  TRP CCC N   1 ? 5  
ATOM 2301  C CA  . TRP B 1 80  ? 34.832  94.950  36.554 1.000 127.583 0 80  TRP CCC CA  1 ? 5  
ATOM 2302  C C   . TRP B 1 80  ? 33.670  94.857  35.576 1.000 131.342 0 80  TRP CCC C   1 ? 5  
ATOM 2303  O O   . TRP B 1 80  ? 33.779  95.286  34.421 1.000 137.329 0 80  TRP CCC O   1 ? 5  
ATOM 2304  C CB  . TRP B 1 80  ? 35.528  93.595  36.688 1.000 125.512 0 80  TRP CCC CB  1 ? 5  
ATOM 2305  C CG  . TRP B 1 80  ? 35.911  93.023  35.338 1.000 119.280 0 80  TRP CCC CG  1 ? 5  
ATOM 2306  C CD1 . TRP B 1 80  ? 35.165  92.178  34.563 1.000 116.836 0 80  TRP CCC CD1 1 ? 5  
ATOM 2307  C CD2 . TRP B 1 80  ? 37.085  93.332  34.572 1.000 118.433 0 80  TRP CCC CD2 1 ? 5  
ATOM 2308  N NE1 . TRP B 1 80  ? 35.824  91.903  33.390 1.000 114.849 0 80  TRP CCC NE1 1 ? 5  
ATOM 2309  C CE2 . TRP B 1 80  ? 37.001  92.603  33.368 1.000 116.682 0 80  TRP CCC CE2 1 ? 5  
ATOM 2310  C CE3 . TRP B 1 80  ? 38.207  94.136  34.798 1.000 117.912 0 80  TRP CCC CE3 1 ? 5  
ATOM 2311  C CZ2 . TRP B 1 80  ? 37.996  92.656  32.393 1.000 118.921 0 80  TRP CCC CZ2 1 ? 5  
ATOM 2312  C CZ3 . TRP B 1 80  ? 39.195  94.187  33.826 1.000 116.375 0 80  TRP CCC CZ3 1 ? 5  
ATOM 2313  C CH2 . TRP B 1 80  ? 39.082  93.452  32.640 1.000 118.450 0 80  TRP CCC CH2 1 ? 5  
ATOM 2314  N N   . ASP B 1 81  ? 32.557  94.268  36.011 1.000 132.085 0 81  ASP CCC N   1 ? 5  
ATOM 2315  C CA  . ASP B 1 81  ? 31.424  94.101  35.112 1.000 134.807 0 81  ASP CCC CA  1 ? 5  
ATOM 2316  C C   . ASP B 1 81  ? 30.886  95.448  34.650 1.000 138.951 0 81  ASP CCC C   1 ? 5  
ATOM 2317  O O   . ASP B 1 81  ? 30.478  95.601  33.493 1.000 146.300 0 81  ASP CCC O   1 ? 5  
ATOM 2318  C CB  . ASP B 1 81  ? 30.313  93.339  35.834 1.000 133.018 0 81  ASP CCC CB  1 ? 5  
ATOM 2319  C CG  . ASP B 1 81  ? 30.669  91.898  36.105 1.000 132.561 0 81  ASP CCC CG  1 ? 5  
ATOM 2320  O OD1 . ASP B 1 81  ? 31.599  91.375  35.457 1.000 141.669 0 81  ASP CCC OD1 1 ? 5  
ATOM 2321  O OD2 . ASP B 1 81  ? 30.037  91.303  37.004 1.000 129.504 0 81  ASP CCC OD2 1 ? 5  
ATOM 2322  N N   . ARG B 1 82  ? 30.862  96.434  35.548 1.000 134.407 0 82  ARG CCC N   1 ? 5  
ATOM 2323  C CA  . ARG B 1 82  ? 30.404  97.771  35.185 1.000 139.496 0 82  ARG CCC CA  1 ? 5  
ATOM 2324  C C   . ARG B 1 82  ? 31.296  98.475  34.156 1.000 141.395 0 82  ARG CCC C   1 ? 5  
ATOM 2325  O O   . ARG B 1 82  ? 30.783  99.112  33.229 1.000 150.699 0 82  ARG CCC O   1 ? 5  
ATOM 2326  C CB  . ARG B 1 82  ? 30.287  98.620  36.451 1.000 140.466 0 82  ARG CCC CB  1 ? 5  
ATOM 2327  C CG  . ARG B 1 82  ? 30.321  100.106 36.183 1.000 148.780 0 82  ARG CCC CG  1 ? 5  
ATOM 2328  C CD  . ARG B 1 82  ? 30.309  100.924 37.457 1.000 153.024 0 82  ARG CCC CD  1 ? 5  
ATOM 2329  N NE  . ARG B 1 82  ? 30.415  102.347 37.158 1.000 169.775 0 82  ARG CCC NE  1 ? 5  
ATOM 2330  C CZ  . ARG B 1 82  ? 31.552  103.029 37.188 1.000 167.922 0 82  ARG CCC CZ  1 ? 5  
ATOM 2331  N NH1 . ARG B 1 82  ? 32.698  102.446 37.498 1.000 158.688 0 82  ARG CCC NH1 1 ? 5  
ATOM 2332  N NH2 . ARG B 1 82  ? 31.539  104.327 36.895 1.000 172.190 0 82  ARG CCC NH2 1 ? 5  
ATOM 2333  N N   . LEU B 1 83  ? 32.626  98.341  34.262 1.000 138.114 0 83  LEU CCC N   1 ? 5  
ATOM 2334  C CA  . LEU B 1 83  ? 33.530  99.008  33.322 1.000 142.202 0 83  LEU CCC CA  1 ? 5  
ATOM 2335  C C   . LEU B 1 83  ? 33.804  98.216  32.054 1.000 144.923 0 83  LEU CCC C   1 ? 5  
ATOM 2336  O O   . LEU B 1 83  ? 34.231  98.798  31.049 1.000 148.188 0 83  LEU CCC O   1 ? 5  
ATOM 2337  C CB  A LEU B 1 83  ? 34.852  99.338  34.021 1.000 139.767 0 83  LEU CCC CB  1 ? 5  
ATOM 2338  C CG  A LEU B 1 83  ? 34.636  100.316 35.179 1.000 143.086 0 83  LEU CCC CG  1 ? 5  
ATOM 2339  C CD1 A LEU B 1 83  ? 35.873  100.456 36.053 1.000 141.389 0 83  LEU CCC CD1 1 ? 5  
ATOM 2340  C CD2 A LEU B 1 83  ? 34.188  101.672 34.647 1.000 154.480 0 83  LEU CCC CD2 1 ? 5  
ATOM 2341  N N   . HIS B 1 84  ? 33.566  96.917  32.087 1.000 145.118 0 84  HIS CCC N   1 ? 5  
ATOM 2342  C CA  . HIS B 1 84  ? 33.810  96.022  30.960 1.000 145.366 0 84  HIS CCC CA  1 ? 5  
ATOM 2343  C C   . HIS B 1 84  ? 32.608  95.100  30.959 1.000 144.134 0 84  HIS CCC C   1 ? 5  
ATOM 2344  O O   . HIS B 1 84  ? 32.694  93.931  31.359 1.000 143.350 0 84  HIS CCC O   1 ? 5  
ATOM 2345  C CB  . HIS B 1 84  ? 35.142  95.272  31.077 1.000 139.667 0 84  HIS CCC CB  1 ? 5  
ATOM 2346  C CG  . HIS B 1 84  ? 36.335  96.163  31.258 1.000 144.390 0 84  HIS CCC CG  1 ? 5  
ATOM 2347  N ND1 . HIS B 1 84  ? 36.834  96.512  32.495 1.000 141.782 0 84  HIS CCC ND1 1 ? 5  
ATOM 2348  C CD2 . HIS B 1 84  ? 37.129  96.776  30.347 1.000 157.343 0 84  HIS CCC CD2 1 ? 5  
ATOM 2349  C CE1 . HIS B 1 84  ? 37.883  97.300  32.338 1.000 148.277 0 84  HIS CCC CE1 1 ? 5  
ATOM 2350  N NE2 . HIS B 1 84  ? 38.082  97.477  31.038 1.000 164.559 0 84  HIS CCC NE2 1 ? 5  
ATOM 2351  N N   . PRO B 1 85  ? 31.455  95.593  30.509 1.000 142.513 0 85  PRO CCC N   1 ? 5  
ATOM 2352  C CA  . PRO B 1 85  ? 30.280  94.730  30.449 1.000 140.701 0 85  PRO CCC CA  1 ? 5  
ATOM 2353  C C   . PRO B 1 85  ? 30.476  93.697  29.367 1.000 143.409 0 85  PRO CCC C   1 ? 5  
ATOM 2354  O O   . PRO B 1 85  ? 31.268  93.870  28.439 1.000 142.459 0 85  PRO CCC O   1 ? 5  
ATOM 2355  C CB  . PRO B 1 85  ? 29.139  95.685  30.080 1.000 137.417 0 85  PRO CCC CB  1 ? 5  
ATOM 2356  C CG  . PRO B 1 85  ? 29.694  97.066  30.232 1.000 149.197 0 85  PRO CCC CG  1 ? 5  
ATOM 2357  C CD  . PRO B 1 85  ? 31.166  96.944  30.004 1.000 141.648 0 85  PRO CCC CD  1 ? 5  
ATOM 2358  N N   . VAL B 1 86  ? 29.732  92.612  29.495 1.000 144.446 0 86  VAL CCC N   1 ? 5  
ATOM 2359  C CA  . VAL B 1 86  ? 29.845  91.507  28.560 1.000 143.309 0 86  VAL CCC CA  1 ? 5  
ATOM 2360  C C   . VAL B 1 86  ? 28.936  91.764  27.371 1.000 153.304 0 86  VAL CCC C   1 ? 5  
ATOM 2361  O O   . VAL B 1 86  ? 27.744  92.053  27.533 1.000 156.287 0 86  VAL CCC O   1 ? 5  
ATOM 2362  C CB  . VAL B 1 86  ? 29.484  90.181  29.250 1.000 139.184 0 86  VAL CCC CB  1 ? 5  
ATOM 2363  C CG1 . VAL B 1 86  ? 29.506  89.031  28.259 1.000 137.852 0 86  VAL CCC CG1 1 ? 5  
ATOM 2364  C CG2 . VAL B 1 86  ? 30.427  89.920  30.410 1.000 147.517 0 86  VAL CCC CG2 1 ? 5  
ATOM 2365  N N   . HIS B 1 87  ? 29.507  91.674  26.175 1.000 157.042 0 87  HIS CCC N   1 ? 5  
ATOM 2366  C CA  . HIS B 1 87  ? 28.748  91.877  24.953 1.000 154.929 0 87  HIS CCC CA  1 ? 5  
ATOM 2367  C C   . HIS B 1 87  ? 27.955  90.606  24.693 1.000 158.179 0 87  HIS CCC C   1 ? 5  
ATOM 2368  O O   . HIS B 1 87  ? 28.541  89.524  24.574 1.000 165.786 0 87  HIS CCC O   1 ? 5  
ATOM 2369  C CB  . HIS B 1 87  ? 29.668  92.219  23.782 1.000 152.815 0 87  HIS CCC CB  1 ? 5  
ATOM 2370  C CG  . HIS B 1 87  ? 30.256  93.594  23.859 1.000 150.604 0 87  HIS CCC CG  1 ? 5  
ATOM 2371  N ND1 . HIS B 1 87  ? 31.065  94.117  22.873 1.000 148.712 0 87  HIS CCC ND1 1 ? 5  
ATOM 2372  C CD2 . HIS B 1 87  ? 30.129  94.564  24.795 1.000 160.552 0 87  HIS CCC CD2 1 ? 5  
ATOM 2373  C CE1 . HIS B 1 87  ? 31.423  95.345  23.205 1.000 160.523 0 87  HIS CCC CE1 1 ? 5  
ATOM 2374  N NE2 . HIS B 1 87  ? 30.868  95.641  24.367 1.000 172.517 0 87  HIS CCC NE2 1 ? 5  
ATOM 2375  N N   . ALA B 1 88  ? 26.637  90.721  24.606 1.000 166.178 0 88  ALA CCC N   1 ? 5  
ATOM 2376  C CA  . ALA B 1 88  ? 25.806  89.537  24.492 1.000 164.423 0 88  ALA CCC CA  1 ? 5  
ATOM 2377  C C   . ALA B 1 88  ? 25.594  89.203  23.027 1.000 168.266 0 88  ALA CCC C   1 ? 5  
ATOM 2378  O O   . ALA B 1 88  ? 25.501  90.088  22.174 1.000 178.510 0 88  ALA CCC O   1 ? 5  
ATOM 2379  C CB  . ALA B 1 88  ? 24.457  89.744  25.181 1.000 170.118 0 88  ALA CCC CB  1 ? 5  
ATOM 2380  N N   . GLY B 1 89  ? 25.539  87.908  22.739 1.000 168.952 0 89  GLY CCC N   1 ? 5  
ATOM 2381  C CA  . GLY B 1 89  ? 25.287  87.451  21.397 1.000 173.108 0 89  GLY CCC CA  1 ? 5  
ATOM 2382  C C   . GLY B 1 89  ? 25.624  85.989  21.217 1.000 174.199 0 89  GLY CCC C   1 ? 5  
ATOM 2383  O O   . GLY B 1 89  ? 26.236  85.352  22.081 1.000 173.972 0 89  GLY CCC O   1 ? 5  
ATOM 2384  N N   . PRO B 1 90  ? 25.223  85.427  20.080 1.000 166.618 0 90  PRO CCC N   1 ? 5  
ATOM 2385  C CA  . PRO B 1 90  ? 25.624  84.055  19.761 1.000 165.743 0 90  PRO CCC CA  1 ? 5  
ATOM 2386  C C   . PRO B 1 90  ? 27.119  83.996  19.521 1.000 160.898 0 90  PRO CCC C   1 ? 5  
ATOM 2387  O O   . PRO B 1 90  ? 27.698  84.881  18.886 1.000 155.407 0 90  PRO CCC O   1 ? 5  
ATOM 2388  C CB  . PRO B 1 90  ? 24.848  83.744  18.479 1.000 174.522 0 90  PRO CCC CB  1 ? 5  
ATOM 2389  C CG  . PRO B 1 90  ? 23.743  84.734  18.454 1.000 175.596 0 90  PRO CCC CG  1 ? 5  
ATOM 2390  C CD  . PRO B 1 90  ? 24.285  85.971  19.089 1.000 161.952 0 90  PRO CCC CD  1 ? 5  
ATOM 2391  N N   . ILE B 1 91  ? 27.744  82.941  20.017 1.000 159.611 0 91  ILE CCC N   1 ? 5  
ATOM 2392  C CA  . ILE B 1 91  ? 29.189  82.811  19.916 1.000 158.670 0 91  ILE CCC CA  1 ? 5  
ATOM 2393  C C   . ILE B 1 91  ? 29.547  82.140  18.596 1.000 162.521 0 91  ILE CCC C   1 ? 5  
ATOM 2394  O O   . ILE B 1 91  ? 29.013  81.083  18.236 1.000 169.811 0 91  ILE CCC O   1 ? 5  
ATOM 2395  C CB  . ILE B 1 91  ? 29.784  82.079  21.130 1.000 158.643 0 91  ILE CCC CB  1 ? 5  
ATOM 2396  C CG1 . ILE B 1 91  ? 31.300  82.294  21.148 1.000 159.441 0 91  ILE CCC CG1 1 ? 5  
ATOM 2397  C CG2 . ILE B 1 91  ? 29.407  80.606  21.153 1.000 163.515 0 91  ILE CCC CG2 1 ? 5  
ATOM 2398  C CD1 . ILE B 1 91  ? 31.709  83.759  21.193 1.000 154.154 0 91  ILE CCC CD1 1 ? 5  
ATOM 2399  N N   . ALA B 1 92  ? 30.433  82.791  17.876 1.000 168.352 0 92  ALA CCC N   1 ? 5  
ATOM 2400  C CA  . ALA B 1 92  ? 30.985  82.303  16.622 1.000 170.439 0 92  ALA CCC CA  1 ? 5  
ATOM 2401  C C   . ALA B 1 92  ? 31.905  81.103  16.824 1.000 170.883 0 92  ALA CCC C   1 ? 5  
ATOM 2402  O O   . ALA B 1 92  ? 32.721  81.100  17.755 1.000 178.232 0 92  ALA CCC O   1 ? 5  
ATOM 2403  C CB  . ALA B 1 92  ? 31.726  83.423  15.901 1.000 172.100 0 92  ALA CCC CB  1 ? 5  
ATOM 2404  N N   . PRO B 1 93  ? 31.768  80.049  15.996 1.000 167.379 0 93  PRO CCC N   1 ? 5  
ATOM 2405  C CA  . PRO B 1 93  ? 32.602  78.847  16.122 1.000 166.337 0 93  PRO CCC CA  1 ? 5  
ATOM 2406  C C   . PRO B 1 93  ? 34.064  79.227  16.215 1.000 166.640 0 93  PRO CCC C   1 ? 5  
ATOM 2407  O O   . PRO B 1 93  ? 34.647  79.910  15.365 1.000 169.201 0 93  PRO CCC O   1 ? 5  
ATOM 2408  C CB  . PRO B 1 93  ? 32.284  78.045  14.851 1.000 163.956 0 93  PRO CCC CB  1 ? 5  
ATOM 2409  C CG  . PRO B 1 93  ? 31.600  79.005  13.929 1.000 174.841 0 93  PRO CCC CG  1 ? 5  
ATOM 2410  C CD  . PRO B 1 93  ? 30.886  79.978  14.820 1.000 171.773 0 93  PRO CCC CD  1 ? 5  
ATOM 2411  N N   . GLY B 1 94  ? 34.640  78.739  17.306 1.000 159.588 0 94  GLY CCC N   1 ? 5  
ATOM 2412  C CA  . GLY B 1 94  ? 36.021  78.906  17.676 1.000 155.472 0 94  GLY CCC CA  1 ? 5  
ATOM 2413  C C   . GLY B 1 94  ? 36.405  80.245  18.272 1.000 152.823 0 94  GLY CCC C   1 ? 5  
ATOM 2414  O O   . GLY B 1 94  ? 37.601  80.547  18.327 1.000 152.954 0 94  GLY CCC O   1 ? 5  
ATOM 2415  N N   . GLN B 1 95  ? 35.443  81.072  18.702 1.000 153.655 0 95  GLN CCC N   1 ? 5  
ATOM 2416  C CA  . GLN B 1 95  ? 35.767  82.363  19.297 1.000 150.419 0 95  GLN CCC CA  1 ? 5  
ATOM 2417  C C   . GLN B 1 95  ? 35.532  82.205  20.796 1.000 144.080 0 95  GLN CCC C   1 ? 5  
ATOM 2418  O O   . GLN B 1 95  ? 34.686  81.417  21.223 1.000 144.596 0 95  GLN CCC O   1 ? 5  
ATOM 2419  C CB  . GLN B 1 95  ? 34.874  83.500  18.773 1.000 152.269 0 95  GLN CCC CB  1 ? 5  
ATOM 2420  C CG  . GLN B 1 95  ? 34.918  83.787  17.296 1.000 160.726 0 95  GLN CCC CG  1 ? 5  
ATOM 2421  C CD  . GLN B 1 95  ? 36.315  84.103  16.835 1.000 159.579 0 95  GLN CCC CD  1 ? 5  
ATOM 2422  O OE1 . GLN B 1 95  ? 36.902  85.089  17.279 1.000 161.657 0 95  GLN CCC OE1 1 ? 5  
ATOM 2423  N NE2 . GLN B 1 95  ? 36.859  83.281  15.947 1.000 159.534 0 95  GLN CCC NE2 1 ? 5  
ATOM 2424  N N   . MET B 1 96  ? 36.268  82.961  21.596 1.000 140.314 0 96  MET CCC N   1 ? 5  
ATOM 2425  C CA  . MET B 1 96  ? 36.111  82.922  23.045 1.000 132.621 0 96  MET CCC CA  1 ? 5  
ATOM 2426  C C   . MET B 1 96  ? 34.926  83.744  23.535 1.000 127.437 0 96  MET CCC C   1 ? 5  
ATOM 2427  O O   . MET B 1 96  ? 34.569  84.759  22.931 1.000 127.781 0 96  MET CCC O   1 ? 5  
ATOM 2428  C CB  . MET B 1 96  ? 37.403  83.370  23.706 1.000 132.859 0 96  MET CCC CB  1 ? 5  
ATOM 2429  C CG  . MET B 1 96  ? 38.503  82.361  23.438 1.000 134.046 0 96  MET CCC CG  1 ? 5  
ATOM 2430  S SD  . MET B 1 96  ? 40.032  82.752  24.265 1.000 157.115 0 96  MET CCC SD  1 ? 5  
ATOM 2431  C CE  . MET B 1 96  ? 40.075  84.516  23.972 1.000 140.771 0 96  MET CCC CE  1 ? 5  
ATOM 2432  N N   . ARG B 1 97  ? 34.338  83.330  24.656 1.000 125.259 0 97  ARG CCC N   1 ? 5  
ATOM 2433  C CA  . ARG B 1 97  ? 33.273  84.161  25.192 1.000 125.905 0 97  ARG CCC CA  1 ? 5  
ATOM 2434  C C   . ARG B 1 97  ? 33.937  85.278  26.008 1.000 125.607 0 97  ARG CCC C   1 ? 5  
ATOM 2435  O O   . ARG B 1 97  ? 35.142  85.246  26.269 1.000 126.310 0 97  ARG CCC O   1 ? 5  
ATOM 2436  C CB  . ARG B 1 97  ? 32.269  83.300  25.978 1.000 128.339 0 97  ARG CCC CB  1 ? 5  
ATOM 2437  C CG  . ARG B 1 97  ? 31.239  84.025  26.853 1.000 140.395 0 97  ARG CCC CG  1 ? 5  
ATOM 2438  C CD  . ARG B 1 97  ? 30.553  83.040  27.788 1.000 145.182 0 97  ARG CCC CD  1 ? 5  
ATOM 2439  N NE  . ARG B 1 97  ? 31.423  82.269  28.669 1.000 126.348 0 97  ARG CCC NE  1 ? 5  
ATOM 2440  C CZ  . ARG B 1 97  ? 31.947  82.716  29.800 1.000 117.561 0 97  ARG CCC CZ  1 ? 5  
ATOM 2441  N NH1 . ARG B 1 97  ? 31.709  83.943  30.235 1.000 122.872 0 97  ARG CCC NH1 1 ? 5  
ATOM 2442  N NH2 . ARG B 1 97  ? 32.691  81.897  30.536 1.000 112.813 0 97  ARG CCC NH2 1 ? 5  
ATOM 2443  N N   . GLU B 1 98  ? 33.177  86.292  26.369 1.000 135.906 0 98  GLU CCC N   1 ? 5  
ATOM 2444  C CA  . GLU B 1 98  ? 33.802  87.375  27.131 1.000 135.383 0 98  GLU CCC CA  1 ? 5  
ATOM 2445  C C   . GLU B 1 98  ? 33.773  87.074  28.624 1.000 134.824 0 98  GLU CCC C   1 ? 5  
ATOM 2446  O O   . GLU B 1 98  ? 32.738  86.634  29.139 1.000 141.517 0 98  GLU CCC O   1 ? 5  
ATOM 2447  C CB  . GLU B 1 98  ? 33.118  88.696  26.823 1.000 145.164 0 98  GLU CCC CB  1 ? 5  
ATOM 2448  C CG  . GLU B 1 98  ? 33.103  88.943  25.322 1.000 151.681 0 98  GLU CCC CG  1 ? 5  
ATOM 2449  C CD  . GLU B 1 98  ? 32.476  90.254  24.925 1.000 161.096 0 98  GLU CCC CD  1 ? 5  
ATOM 2450  O OE1 . GLU B 1 98  ? 32.124  91.046  25.822 1.000 165.528 0 98  GLU CCC OE1 1 ? 5  
ATOM 2451  O OE2 . GLU B 1 98  ? 32.351  90.496  23.707 1.000 164.992 0 98  GLU CCC OE2 1 ? 5  
ATOM 2452  N N   . PRO B 1 99  ? 34.887  87.272  29.335 1.000 130.645 0 99  PRO CCC N   1 ? 5  
ATOM 2453  C CA  . PRO B 1 99  ? 34.924  86.946  30.770 1.000 118.825 0 99  PRO CCC CA  1 ? 5  
ATOM 2454  C C   . PRO B 1 99  ? 34.178  88.002  31.573 1.000 117.529 0 99  PRO CCC C   1 ? 5  
ATOM 2455  O O   . PRO B 1 99  ? 34.375  89.204  31.379 1.000 113.312 0 99  PRO CCC O   1 ? 5  
ATOM 2456  C CB  . PRO B 1 99  ? 36.421  86.951  31.101 1.000 109.752 0 99  PRO CCC CB  1 ? 5  
ATOM 2457  C CG  . PRO B 1 99  ? 37.023  87.868  30.084 1.000 114.396 0 99  PRO CCC CG  1 ? 5  
ATOM 2458  C CD  . PRO B 1 99  ? 36.190  87.749  28.836 1.000 127.586 0 99  PRO CCC CD  1 ? 5  
ATOM 2459  N N   . ARG B 1 100 ? 33.353  87.543  32.507 1.000 121.892 0 100 ARG CCC N   1 ? 5  
ATOM 2460  C CA  . ARG B 1 100 ? 32.715  88.414  33.477 1.000 122.761 0 100 ARG CCC CA  1 ? 5  
ATOM 2461  C C   . ARG B 1 100 ? 33.594  88.546  34.713 1.000 123.596 0 100 ARG CCC C   1 ? 5  
ATOM 2462  O O   . ARG B 1 100 ? 34.639  87.903  34.831 1.000 123.408 0 100 ARG CCC O   1 ? 5  
ATOM 2463  C CB  . ARG B 1 100 ? 31.380  87.812  33.914 1.000 126.844 0 100 ARG CCC CB  1 ? 5  
ATOM 2464  C CG  . ARG B 1 100 ? 30.493  87.286  32.809 1.000 135.598 0 100 ARG CCC CG  1 ? 5  
ATOM 2465  C CD  . ARG B 1 100 ? 29.326  86.523  33.422 1.000 143.863 0 100 ARG CCC CD  1 ? 5  
ATOM 2466  N NE  . ARG B 1 100 ? 28.148  86.485  32.565 1.000 162.481 0 100 ARG CCC NE  1 ? 5  
ATOM 2467  C CZ  . ARG B 1 100 ? 27.179  87.397  32.572 1.000 172.929 0 100 ARG CCC CZ  1 ? 5  
ATOM 2468  N NH1 . ARG B 1 100 ? 27.232  88.442  33.387 1.000 170.093 0 100 ARG CCC NH1 1 ? 5  
ATOM 2469  N NH2 . ARG B 1 100 ? 26.149  87.255  31.755 1.000 177.065 0 100 ARG CCC NH2 1 ? 5  
ATOM 2470  N N   . GLY B 1 101 ? 33.182  89.436  35.620 1.000 119.679 0 101 GLY CCC N   1 ? 5  
ATOM 2471  C CA  . GLY B 1 101 ? 33.908  89.589  36.872 1.000 109.470 0 101 GLY CCC CA  1 ? 5  
ATOM 2472  C C   . GLY B 1 101 ? 34.087  88.256  37.569 1.000 102.808 0 101 GLY CCC C   1 ? 5  
ATOM 2473  O O   . GLY B 1 101 ? 35.176  87.914  38.038 1.000 100.224 0 101 GLY CCC O   1 ? 5  
ATOM 2474  N N   . SER B 1 102 ? 32.998  87.490  37.650 1.000 103.504 0 102 SER CCC N   1 ? 5  
ATOM 2475  C CA  . SER B 1 102 ? 32.982  86.171  38.263 1.000 103.339 0 102 SER CCC CA  1 ? 5  
ATOM 2476  C C   . SER B 1 102 ? 33.810  85.141  37.506 1.000 101.238 0 102 SER CCC C   1 ? 5  
ATOM 2477  O O   . SER B 1 102 ? 34.254  84.158  38.109 1.000 103.116 0 102 SER CCC O   1 ? 5  
ATOM 2478  C CB  . SER B 1 102 ? 31.543  85.685  38.371 1.000 108.378 0 102 SER CCC CB  1 ? 5  
ATOM 2479  O OG  . SER B 1 102 ? 31.499  84.285  38.210 1.000 113.417 0 102 SER CCC OG  1 ? 5  
ATOM 2480  N N   . ASP B 1 103 ? 34.023  85.331  36.204 1.000 104.635 0 103 ASP CCC N   1 ? 5  
ATOM 2481  C CA  . ASP B 1 103 ? 34.903  84.430  35.466 1.000 102.352 0 103 ASP CCC CA  1 ? 5  
ATOM 2482  C C   . ASP B 1 103 ? 36.361  84.690  35.815 1.000 99.247  0 103 ASP CCC C   1 ? 5  
ATOM 2483  O O   . ASP B 1 103 ? 37.149  83.748  35.965 1.000 100.335 0 103 ASP CCC O   1 ? 5  
ATOM 2484  C CB  . ASP B 1 103 ? 34.674  84.573  33.958 1.000 103.899 0 103 ASP CCC CB  1 ? 5  
ATOM 2485  C CG  . ASP B 1 103 ? 33.289  84.127  33.528 1.000 104.897 0 103 ASP CCC CG  1 ? 5  
ATOM 2486  O OD1 . ASP B 1 103 ? 32.854  83.033  33.950 1.000 105.062 0 103 ASP CCC OD1 1 ? 5  
ATOM 2487  O OD2 . ASP B 1 103 ? 32.631  84.872  32.773 1.000 108.009 0 103 ASP CCC OD2 1 ? 5  
ATOM 2488  N N   . ILE B 1 104 ? 36.725  85.960  35.986 1.000 92.413  0 104 ILE CCC N   1 ? 5  
ATOM 2489  C CA  . ILE B 1 104 ? 38.084  86.321  36.380 1.000 89.877  0 104 ILE CCC CA  1 ? 5  
ATOM 2490  C C   . ILE B 1 104 ? 38.415  85.770  37.761 1.000 89.964  0 104 ILE CCC C   1 ? 5  
ATOM 2491  O O   . ILE B 1 104 ? 39.538  85.310  38.008 1.000 84.683  0 104 ILE CCC O   1 ? 5  
ATOM 2492  C CB  . ILE B 1 104 ? 38.252  87.848  36.330 1.000 91.083  0 104 ILE CCC CB  1 ? 5  
ATOM 2493  C CG1 . ILE B 1 104 ? 38.211  88.321  34.878 1.000 93.217  0 104 ILE CCC CG1 1 ? 5  
ATOM 2494  C CG2 . ILE B 1 104 ? 39.555  88.266  37.014 1.000 90.509  0 104 ILE CCC CG2 1 ? 5  
ATOM 2495  C CD1 . ILE B 1 104 ? 38.594  89.760  34.691 1.000 102.042 0 104 ILE CCC CD1 1 ? 5  
ATOM 2496  N N   . ALA B 1 105 ? 37.449  85.794  38.677 1.000 88.164  0 105 ALA CCC N   1 ? 5  
ATOM 2497  C CA  . ALA B 1 105 ? 37.656  85.255  40.013 1.000 86.645  0 105 ALA CCC CA  1 ? 5  
ATOM 2498  C C   . ALA B 1 105 ? 37.632  83.732  40.065 1.000 87.477  0 105 ALA CCC C   1 ? 5  
ATOM 2499  O O   . ALA B 1 105 ? 37.770  83.170  41.156 1.000 88.108  0 105 ALA CCC O   1 ? 5  
ATOM 2500  C CB  . ALA B 1 105 ? 36.601  85.814  40.966 1.000 88.977  0 105 ALA CCC CB  1 ? 5  
ATOM 2501  N N   . GLY B 1 106 ? 37.429  83.055  38.935 1.000 92.602  0 106 GLY CCC N   1 ? 5  
ATOM 2502  C CA  . GLY B 1 106 ? 37.482  81.606  38.890 1.000 94.960  0 106 GLY CCC CA  1 ? 5  
ATOM 2503  C C   . GLY B 1 106 ? 36.291  80.873  39.459 1.000 100.433 0 106 GLY CCC C   1 ? 5  
ATOM 2504  O O   . GLY B 1 106 ? 36.393  79.664  39.701 1.000 106.778 0 106 GLY CCC O   1 ? 5  
ATOM 2505  N N   . THR B 1 107 ? 35.170  81.558  39.681 1.000 98.723  0 107 THR CCC N   1 ? 5  
ATOM 2506  C CA  . THR B 1 107 ? 33.991  80.962  40.296 1.000 99.286  0 107 THR CCC CA  1 ? 5  
ATOM 2507  C C   . THR B 1 107 ? 33.072  80.304  39.272 1.000 102.169 0 107 THR CCC C   1 ? 5  
ATOM 2508  O O   . THR B 1 107 ? 32.508  79.238  39.542 1.000 108.247 0 107 THR CCC O   1 ? 5  
ATOM 2509  C CB  . THR B 1 107 ? 33.217  82.017  41.099 1.000 103.165 0 107 THR CCC CB  1 ? 5  
ATOM 2510  O OG1 . THR B 1 107 ? 32.831  83.095  40.240 1.000 113.301 0 107 THR CCC OG1 1 ? 5  
ATOM 2511  C CG2 . THR B 1 107 ? 34.073  82.568  42.234 1.000 101.901 0 107 THR CCC CG2 1 ? 5  
ATOM 2512  N N   . THR B 1 108 ? 32.921  80.913  38.095 1.000 108.052 0 108 THR CCC N   1 ? 5  
ATOM 2513  C CA  . THR B 1 108 ? 32.040  80.415  37.043 1.000 113.198 0 108 THR CCC CA  1 ? 5  
ATOM 2514  C C   . THR B 1 108 ? 32.760  80.030  35.759 1.000 112.864 0 108 THR CCC C   1 ? 5  
ATOM 2515  O O   . THR B 1 108 ? 32.101  79.779  34.742 1.000 122.670 0 108 THR CCC O   1 ? 5  
ATOM 2516  C CB  . THR B 1 108 ? 30.959  81.447  36.731 1.000 118.548 0 108 THR CCC CB  1 ? 5  
ATOM 2517  O OG1 . THR B 1 108 ? 31.577  82.696  36.391 1.000 115.257 0 108 THR CCC OG1 1 ? 5  
ATOM 2518  C CG2 . THR B 1 108 ? 30.029  81.610  37.920 1.000 126.645 0 108 THR CCC CG2 1 ? 5  
ATOM 2519  N N   . SER B 1 109 ? 34.082  79.988  35.765 1.000 100.758 0 109 SER CCC N   1 ? 5  
ATOM 2520  C CA  . SER B 1 109 ? 34.850  79.632  34.587 1.000 96.807  0 109 SER CCC CA  1 ? 5  
ATOM 2521  C C   . SER B 1 109 ? 35.560  78.303  34.810 1.000 94.235  0 109 SER CCC C   1 ? 5  
ATOM 2522  O O   . SER B 1 109 ? 35.872  77.927  35.943 1.000 97.555  0 109 SER CCC O   1 ? 5  
ATOM 2523  C CB  . SER B 1 109 ? 35.861  80.730  34.260 1.000 93.635  0 109 SER CCC CB  1 ? 5  
ATOM 2524  O OG  . SER B 1 109 ? 36.735  80.941  35.354 1.000 93.937  0 109 SER CCC OG  1 ? 5  
ATOM 2525  N N   . THR B 1 110 ? 35.793  77.586  33.718 1.000 95.483  0 110 THR CCC N   1 ? 5  
ATOM 2526  C CA  . THR B 1 110 ? 36.532  76.335  33.767 1.000 96.751  0 110 THR CCC CA  1 ? 5  
ATOM 2527  C C   . THR B 1 110 ? 38.009  76.609  33.531 1.000 97.396  0 110 THR CCC C   1 ? 5  
ATOM 2528  O O   . THR B 1 110 ? 38.397  77.664  33.021 1.000 101.144 0 110 THR CCC O   1 ? 5  
ATOM 2529  C CB  . THR B 1 110 ? 36.018  75.344  32.723 1.000 103.378 0 110 THR CCC CB  1 ? 5  
ATOM 2530  O OG1 . THR B 1 110 ? 36.305  75.837  31.407 1.000 105.294 0 110 THR CCC OG1 1 ? 5  
ATOM 2531  C CG2 . THR B 1 110 ? 34.521  75.155  32.870 1.000 117.499 0 110 THR CCC CG2 1 ? 5  
ATOM 2532  N N   . LEU B 1 111 ? 38.839  75.638  33.915 1.000 94.531  0 111 LEU CCC N   1 ? 5  
ATOM 2533  C CA  . LEU B 1 111 ? 40.269  75.761  33.655 1.000 91.492  0 111 LEU CCC CA  1 ? 5  
ATOM 2534  C C   . LEU B 1 111 ? 40.544  75.993  32.175 1.000 98.211  0 111 LEU CCC C   1 ? 5  
ATOM 2535  O O   . LEU B 1 111 ? 41.386  76.825  31.819 1.000 100.032 0 111 LEU CCC O   1 ? 5  
ATOM 2536  C CB  . LEU B 1 111 ? 41.006  74.521  34.163 1.000 91.398  0 111 LEU CCC CB  1 ? 5  
ATOM 2537  C CG  . LEU B 1 111 ? 42.506  74.486  33.856 1.000 94.383  0 111 LEU CCC CG  1 ? 5  
ATOM 2538  C CD1 . LEU B 1 111 ? 43.205  75.714  34.428 1.000 85.967  0 111 LEU CCC CD1 1 ? 5  
ATOM 2539  C CD2 . LEU B 1 111 ? 43.146  73.213  34.390 1.000 108.705 0 111 LEU CCC CD2 1 ? 5  
ATOM 2540  N N   . GLN B 1 112 ? 39.833  75.282  31.296 1.000 100.950 0 112 GLN CCC N   1 ? 5  
ATOM 2541  C CA  . GLN B 1 112 ? 40.089  75.428  29.866 1.000 99.062  0 112 GLN CCC CA  1 ? 5  
ATOM 2542  C C   . GLN B 1 112 ? 39.764  76.837  29.381 1.000 97.069  0 112 GLN CCC C   1 ? 5  
ATOM 2543  O O   . GLN B 1 112 ? 40.521  77.420  28.596 1.000 96.328  0 112 GLN CCC O   1 ? 5  
ATOM 2544  C CB  . GLN B 1 112 ? 39.275  74.397  29.083 1.000 118.036 0 112 GLN CCC CB  1 ? 5  
ATOM 2545  C CG  . GLN B 1 112 ? 40.070  73.189  28.594 1.000 141.164 0 112 GLN CCC CG  1 ? 5  
ATOM 2546  C CD  . GLN B 1 112 ? 40.666  72.383  29.736 1.000 156.021 0 112 GLN CCC CD  1 ? 5  
ATOM 2547  O OE1 . GLN B 1 112 ? 39.956  71.980  30.660 1.000 163.524 0 112 GLN CCC OE1 1 ? 5  
ATOM 2548  N NE2 . GLN B 1 112 ? 41.968  72.116  29.663 1.000 150.030 0 112 GLN CCC NE2 1 ? 5  
ATOM 2549  N N   . GLU B 1 113 ? 38.660  77.414  29.862 1.000 96.849  0 113 GLU CCC N   1 ? 5  
ATOM 2550  C CA  . GLU B 1 113 ? 38.343  78.799  29.528 1.000 98.322  0 113 GLU CCC CA  1 ? 5  
ATOM 2551  C C   . GLU B 1 113 ? 39.403  79.763  30.048 1.000 95.573  0 113 GLU CCC C   1 ? 5  
ATOM 2552  O O   . GLU B 1 113 ? 39.786  80.709  29.349 1.000 100.395 0 113 GLU CCC O   1 ? 5  
ATOM 2553  C CB  . GLU B 1 113 ? 36.964  79.167  30.070 1.000 101.790 0 113 GLU CCC CB  1 ? 5  
ATOM 2554  C CG  . GLU B 1 113 ? 35.833  78.459  29.350 1.000 108.900 0 113 GLU CCC CG  1 ? 5  
ATOM 2555  C CD  . GLU B 1 113 ? 34.488  78.716  29.986 1.000 112.140 0 113 GLU CCC CD  1 ? 5  
ATOM 2556  O OE1 . GLU B 1 113 ? 34.216  78.140  31.060 1.000 111.887 0 113 GLU CCC OE1 1 ? 5  
ATOM 2557  O OE2 . GLU B 1 113 ? 33.698  79.490  29.405 1.000 117.099 0 113 GLU CCC OE2 1 ? 5  
ATOM 2558  N N   . GLN B 1 114 ? 39.871  79.551  31.281 1.000 93.613  0 114 GLN CCC N   1 ? 5  
ATOM 2559  C CA  . GLN B 1 114 ? 40.915  80.400  31.853 1.000 90.356  0 114 GLN CCC CA  1 ? 5  
ATOM 2560  C C   . GLN B 1 114 ? 42.191  80.339  31.021 1.000 91.162  0 114 GLN CCC C   1 ? 5  
ATOM 2561  O O   . GLN B 1 114 ? 42.827  81.366  30.755 1.000 89.912  0 114 GLN CCC O   1 ? 5  
ATOM 2562  C CB  . GLN B 1 114 ? 41.185  79.979  33.301 1.000 85.190  0 114 GLN CCC CB  1 ? 5  
ATOM 2563  C CG  . GLN B 1 114 ? 40.031  80.282  34.255 1.000 85.599  0 114 GLN CCC CG  1 ? 5  
ATOM 2564  C CD  . GLN B 1 114 ? 40.155  79.590  35.605 1.000 86.249  0 114 GLN CCC CD  1 ? 5  
ATOM 2565  O OE1 . GLN B 1 114 ? 41.252  79.253  36.051 1.000 89.795  0 114 GLN CCC OE1 1 ? 5  
ATOM 2566  N NE2 . GLN B 1 114 ? 39.017  79.361  36.256 1.000 85.264  0 114 GLN CCC NE2 1 ? 5  
ATOM 2567  N N   . ILE B 1 115 ? 42.598  79.131  30.632 1.000 93.186  0 115 ILE CCC N   1 ? 5  
ATOM 2568  C CA  . ILE B 1 115 ? 43.762  78.963  29.767 1.000 90.258  0 115 ILE CCC CA  1 ? 5  
ATOM 2569  C C   . ILE B 1 115 ? 43.542  79.644  28.422 1.000 106.224 0 115 ILE CCC C   1 ? 5  
ATOM 2570  O O   . ILE B 1 115 ? 44.441  80.305  27.887 1.000 113.702 0 115 ILE CCC O   1 ? 5  
ATOM 2571  C CB  . ILE B 1 115 ? 44.090  77.469  29.593 1.000 85.125  0 115 ILE CCC CB  1 ? 5  
ATOM 2572  C CG1 . ILE B 1 115 ? 44.564  76.864  30.919 1.000 83.541  0 115 ILE CCC CG1 1 ? 5  
ATOM 2573  C CG2 . ILE B 1 115 ? 45.140  77.293  28.516 1.000 86.609  0 115 ILE CCC CG2 1 ? 5  
ATOM 2574  C CD1 . ILE B 1 115 ? 44.529  75.342  30.967 1.000 87.440  0 115 ILE CCC CD1 1 ? 5  
ATOM 2575  N N   . GLY B 1 116 ? 42.337  79.502  27.864 1.000 122.805 0 116 GLY CCC N   1 ? 5  
ATOM 2576  C CA  . GLY B 1 116 ? 42.011  80.156  26.603 1.000 129.845 0 116 GLY CCC CA  1 ? 5  
ATOM 2577  C C   . GLY B 1 116 ? 42.211  81.660  26.612 1.000 131.550 0 116 GLY CCC C   1 ? 5  
ATOM 2578  O O   . GLY B 1 116 ? 42.809  82.221  25.690 1.000 141.079 0 116 GLY CCC O   1 ? 5  
ATOM 2579  N N   . TRP B 1 117 ? 41.730  82.335  27.656 1.000 106.332 0 117 TRP CCC N   1 ? 5  
ATOM 2580  C CA  . TRP B 1 117 ? 41.886  83.785  27.725 1.000 104.163 0 117 TRP CCC CA  1 ? 5  
ATOM 2581  C C   . TRP B 1 117 ? 43.352  84.172  27.868 1.000 107.185 0 117 TRP CCC C   1 ? 5  
ATOM 2582  O O   . TRP B 1 117 ? 43.839  85.071  27.173 1.000 113.379 0 117 TRP CCC O   1 ? 5  
ATOM 2583  C CB  . TRP B 1 117 ? 41.056  84.340  28.883 1.000 103.797 0 117 TRP CCC CB  1 ? 5  
ATOM 2584  C CG  . TRP B 1 117 ? 39.581  84.216  28.672 1.000 104.618 0 117 TRP CCC CG  1 ? 5  
ATOM 2585  C CD1 . TRP B 1 117 ? 38.895  84.472  27.522 1.000 118.462 0 117 TRP CCC CD1 1 ? 5  
ATOM 2586  C CD2 . TRP B 1 117 ? 38.608  83.791  29.632 1.000 102.388 0 117 TRP CCC CD2 1 ? 5  
ATOM 2587  N NE1 . TRP B 1 117 ? 37.554  84.245  27.709 1.000 119.824 0 117 TRP CCC NE1 1 ? 5  
ATOM 2588  C CE2 . TRP B 1 117 ? 37.351  83.824  28.997 1.000 108.670 0 117 TRP CCC CE2 1 ? 5  
ATOM 2589  C CE3 . TRP B 1 117 ? 38.678  83.390  30.968 1.000 106.076 0 117 TRP CCC CE3 1 ? 5  
ATOM 2590  C CZ2 . TRP B 1 117 ? 36.174  83.470  29.653 1.000 108.878 0 117 TRP CCC CZ2 1 ? 5  
ATOM 2591  C CZ3 . TRP B 1 117 ? 37.507  83.038  31.618 1.000 103.066 0 117 TRP CCC CZ3 1 ? 5  
ATOM 2592  C CH2 . TRP B 1 117 ? 36.273  83.080  30.960 1.000 101.546 0 117 TRP CCC CH2 1 ? 5  
ATOM 2593  N N   . MET B 1 118 ? 44.066  83.514  28.778 1.000 103.935 0 118 MET CCC N   1 ? 5  
ATOM 2594  C CA  . MET B 1 118 ? 45.461  83.845  29.047 1.000 105.395 0 118 MET CCC CA  1 ? 5  
ATOM 2595  C C   . MET B 1 118 ? 46.374  83.557  27.853 1.000 110.623 0 118 MET CCC C   1 ? 5  
ATOM 2596  O O   . MET B 1 118 ? 47.404  84.223  27.699 1.000 114.750 0 118 MET CCC O   1 ? 5  
ATOM 2597  C CB  . MET B 1 118 ? 45.948  83.139  30.312 1.000 105.065 0 118 MET CCC CB  1 ? 5  
ATOM 2598  C CG  . MET B 1 118 ? 45.282  83.689  31.575 1.000 104.413 0 118 MET CCC CG  1 ? 5  
ATOM 2599  S SD  . MET B 1 118 ? 45.612  82.729  33.071 1.000 100.207 0 118 MET CCC SD  1 ? 5  
ATOM 2600  C CE  . MET B 1 118 ? 47.365  83.049  33.303 1.000 113.187 0 118 MET CCC CE  1 ? 5  
ATOM 2601  N N   . THR B 1 119 ? 46.035  82.585  27.000 1.000 108.499 0 119 THR CCC N   1 ? 5  
ATOM 2602  C CA  . THR B 1 119 ? 46.898  82.239  25.874 1.000 110.871 0 119 THR CCC CA  1 ? 5  
ATOM 2603  C C   . THR B 1 119 ? 46.428  82.817  24.545 1.000 118.634 0 119 THR CCC C   1 ? 5  
ATOM 2604  O O   . THR B 1 119 ? 46.947  82.429  23.494 1.000 128.903 0 119 THR CCC O   1 ? 5  
ATOM 2605  C CB  . THR B 1 119 ? 47.010  80.721  25.744 1.000 111.424 0 119 THR CCC CB  1 ? 5  
ATOM 2606  O OG1 . THR B 1 119 ? 45.716  80.176  25.458 1.000 111.806 0 119 THR CCC OG1 1 ? 5  
ATOM 2607  C CG2 . THR B 1 119 ? 47.531  80.125  27.033 1.000 109.662 0 119 THR CCC CG2 1 ? 5  
ATOM 2608  N N   . HIS B 1 120 ? 45.459  83.723  24.566 1.000 126.647 0 120 HIS CCC N   1 ? 5  
ATOM 2609  C CA  . HIS B 1 120 ? 44.973  84.340  23.343 1.000 133.617 0 120 HIS CCC CA  1 ? 5  
ATOM 2610  C C   . HIS B 1 120 ? 46.015  85.328  22.823 1.000 142.320 0 120 HIS CCC C   1 ? 5  
ATOM 2611  O O   . HIS B 1 120 ? 46.951  85.711  23.530 1.000 144.947 0 120 HIS CCC O   1 ? 5  
ATOM 2612  C CB  . HIS B 1 120 ? 43.647  85.055  23.589 1.000 139.267 0 120 HIS CCC CB  1 ? 5  
ATOM 2613  C CG  . HIS B 1 120 ? 42.925  85.434  22.335 1.000 144.239 0 120 HIS CCC CG  1 ? 5  
ATOM 2614  N ND1 . HIS B 1 120 ? 42.875  86.734  21.879 1.000 151.146 0 120 HIS CCC ND1 1 ? 5  
ATOM 2615  C CD2 . HIS B 1 120 ? 42.253  84.690  21.426 1.000 151.551 0 120 HIS CCC CD2 1 ? 5  
ATOM 2616  C CE1 . HIS B 1 120 ? 42.185  86.777  20.754 1.000 165.075 0 120 HIS CCC CE1 1 ? 5  
ATOM 2617  N NE2 . HIS B 1 120 ? 41.797  85.550  20.457 1.000 170.643 0 120 HIS CCC NE2 1 ? 5  
ATOM 2618  N N   . ASN B 1 121 ? 45.869  85.718  21.562 1.000 153.891 0 121 ASN CCC N   1 ? 5  
ATOM 2619  C CA  . ASN B 1 121 ? 46.683  86.789  20.986 1.000 161.719 0 121 ASN CCC CA  1 ? 5  
ATOM 2620  C C   . ASN B 1 121 ? 45.767  87.872  20.435 1.000 172.300 0 121 ASN CCC C   1 ? 5  
ATOM 2621  O O   . ASN B 1 121 ? 45.162  87.686  19.363 1.000 182.642 0 121 ASN CCC O   1 ? 5  
ATOM 2622  C CB  . ASN B 1 121 ? 47.600  86.251  19.889 1.000 164.632 0 121 ASN CCC CB  1 ? 5  
ATOM 2623  C CG  . ASN B 1 121 ? 48.577  87.296  19.382 1.000 170.897 0 121 ASN CCC CG  1 ? 5  
ATOM 2624  O OD1 . ASN B 1 121 ? 49.091  88.111  20.150 1.000 169.916 0 121 ASN CCC OD1 1 ? 5  
ATOM 2625  N ND2 . ASN B 1 121 ? 48.839  87.276  18.078 1.000 181.569 0 121 ASN CCC ND2 1 ? 5  
ATOM 2626  N N   . PRO B 1 122 ? 45.629  89.023  21.114 1.000 174.908 0 122 PRO CCC N   1 ? 5  
ATOM 2627  C CA  . PRO B 1 122 ? 46.304  89.398  22.364 1.000 161.108 0 122 PRO CCC CA  1 ? 5  
ATOM 2628  C C   . PRO B 1 122 ? 45.741  88.696  23.603 1.000 151.999 0 122 PRO CCC C   1 ? 5  
ATOM 2629  O O   . PRO B 1 122 ? 44.561  88.353  23.640 1.000 155.240 0 122 PRO CCC O   1 ? 5  
ATOM 2630  C CB  . PRO B 1 122 ? 46.065  90.913  22.450 1.000 169.630 0 122 PRO CCC CB  1 ? 5  
ATOM 2631  C CG  . PRO B 1 122 ? 45.688  91.332  21.060 1.000 183.523 0 122 PRO CCC CG  1 ? 5  
ATOM 2632  C CD  . PRO B 1 122 ? 44.927  90.171  20.518 1.000 183.932 0 122 PRO CCC CD  1 ? 5  
ATOM 2633  N N   . PRO B 1 123 ? 46.588  88.488  24.609 1.000 138.444 0 123 PRO CCC N   1 ? 5  
ATOM 2634  C CA  . PRO B 1 123 ? 46.146  87.771  25.811 1.000 128.840 0 123 PRO CCC CA  1 ? 5  
ATOM 2635  C C   . PRO B 1 123 ? 45.232  88.614  26.687 1.000 126.481 0 123 PRO CCC C   1 ? 5  
ATOM 2636  O O   . PRO B 1 123 ? 45.429  89.822  26.847 1.000 132.686 0 123 PRO CCC O   1 ? 5  
ATOM 2637  C CB  . PRO B 1 123 ? 47.460  87.440  26.525 1.000 126.307 0 123 PRO CCC CB  1 ? 5  
ATOM 2638  C CG  . PRO B 1 123 ? 48.390  88.529  26.107 1.000 139.527 0 123 PRO CCC CG  1 ? 5  
ATOM 2639  C CD  . PRO B 1 123 ? 47.999  88.905  24.696 1.000 142.245 0 123 PRO CCC CD  1 ? 5  
ATOM 2640  N N   . ILE B 1 124 ? 44.203  87.965  27.227 1.000 117.666 0 124 ILE CCC N   1 ? 5  
ATOM 2641  C CA  . ILE B 1 124 ? 43.331  88.565  28.236 1.000 113.530 0 124 ILE CCC CA  1 ? 5  
ATOM 2642  C C   . ILE B 1 124 ? 43.741  87.983  29.588 1.000 105.335 0 124 ILE CCC C   1 ? 5  
ATOM 2643  O O   . ILE B 1 124 ? 43.369  86.845  29.909 1.000 103.124 0 124 ILE CCC O   1 ? 5  
ATOM 2644  C CB  . ILE B 1 124 ? 41.849  88.302  27.918 1.000 116.002 0 124 ILE CCC CB  1 ? 5  
ATOM 2645  C CG1 . ILE B 1 124 ? 41.500  88.826  26.520 1.000 121.615 0 124 ILE CCC CG1 1 ? 5  
ATOM 2646  C CG2 . ILE B 1 124 ? 40.953  88.950  28.962 1.000 112.263 0 124 ILE CCC CG2 1 ? 5  
ATOM 2647  C CD1 . ILE B 1 124 ? 40.199  88.275  25.957 1.000 128.191 0 124 ILE CCC CD1 1 ? 5  
ATOM 2648  N N   . PRO B 1 125 ? 44.516  88.723  30.412 1.000 101.501 0 125 PRO CCC N   1 ? 5  
ATOM 2649  C CA  . PRO B 1 125 ? 45.195  88.139  31.593 1.000 94.761  0 125 PRO CCC CA  1 ? 5  
ATOM 2650  C C   . PRO B 1 125 ? 44.315  88.032  32.831 1.000 94.841  0 125 PRO CCC C   1 ? 5  
ATOM 2651  O O   . PRO B 1 125 ? 44.471  88.764  33.817 1.000 99.753  0 125 PRO CCC O   1 ? 5  
ATOM 2652  C CB  . PRO B 1 125 ? 46.362  89.108  31.804 1.000 94.111  0 125 PRO CCC CB  1 ? 5  
ATOM 2653  C CG  . PRO B 1 125 ? 45.801  90.435  31.387 1.000 95.612  0 125 PRO CCC CG  1 ? 5  
ATOM 2654  C CD  . PRO B 1 125 ? 44.753  90.174  30.316 1.000 103.697 0 125 PRO CCC CD  1 ? 5  
ATOM 2655  N N   . VAL B 1 126 ? 43.358  87.103  32.788 1.000 93.342  0 126 VAL CCC N   1 ? 5  
ATOM 2656  C CA  . VAL B 1 126 ? 42.396  86.999  33.880 1.000 92.443  0 126 VAL CCC CA  1 ? 5  
ATOM 2657  C C   . VAL B 1 126 ? 43.097  86.630  35.181 1.000 90.496  0 126 VAL CCC C   1 ? 5  
ATOM 2658  O O   . VAL B 1 126 ? 42.667  87.033  36.269 1.000 98.769  0 126 VAL CCC O   1 ? 5  
ATOM 2659  C CB  . VAL B 1 126 ? 41.294  85.981  33.527 1.000 83.244  0 126 VAL CCC CB  1 ? 5  
ATOM 2660  C CG1 . VAL B 1 126 ? 40.450  86.495  32.374 1.000 92.399  0 126 VAL CCC CG1 1 ? 5  
ATOM 2661  C CG2 . VAL B 1 126 ? 41.895  84.621  33.199 1.000 80.608  0 126 VAL CCC CG2 1 ? 5  
ATOM 2662  N N   . GLY B 1 127 ? 44.187  85.866  35.088 1.000 91.930  0 127 GLY CCC N   1 ? 5  
ATOM 2663  C CA  . GLY B 1 127 ? 44.975  85.540  36.268 1.000 91.134  0 127 GLY CCC CA  1 ? 5  
ATOM 2664  C C   . GLY B 1 127 ? 45.629  86.741  36.924 1.000 93.160  0 127 GLY CCC C   1 ? 5  
ATOM 2665  O O   . GLY B 1 127 ? 45.563  86.912  38.144 1.000 93.149  0 127 GLY CCC O   1 ? 5  
ATOM 2666  N N   . GLU B 1 128 ? 46.244  87.607  36.120 1.000 94.882  0 128 GLU CCC N   1 ? 5  
ATOM 2667  C CA  . GLU B 1 128 ? 46.911  88.780  36.676 1.000 95.270  0 128 GLU CCC CA  1 ? 5  
ATOM 2668  C C   . GLU B 1 128 ? 45.918  89.764  37.281 1.000 99.156  0 128 GLU CCC C   1 ? 5  
ATOM 2669  O O   . GLU B 1 128 ? 46.198  90.373  38.319 1.000 106.203 0 128 GLU CCC O   1 ? 5  
ATOM 2670  C CB  . GLU B 1 128 ? 47.754  89.448  35.595 1.000 102.967 0 128 GLU CCC CB  1 ? 5  
ATOM 2671  C CG  . GLU B 1 128 ? 48.913  88.569  35.141 1.000 114.722 0 128 GLU CCC CG  1 ? 5  
ATOM 2672  C CD  . GLU B 1 128 ? 49.731  88.042  36.308 1.000 122.966 0 128 GLU CCC CD  1 ? 5  
ATOM 2673  O OE1 . GLU B 1 128 ? 50.334  88.866  37.025 1.000 133.509 0 128 GLU CCC OE1 1 ? 5  
ATOM 2674  O OE2 . GLU B 1 128 ? 49.782  86.804  36.501 1.000 114.726 0 128 GLU CCC OE2 1 ? 5  
ATOM 2675  N N   . ILE B 1 129 ? 44.748  89.916  36.660 1.000 100.564 0 129 ILE CCC N   1 ? 5  
ATOM 2676  C CA  . ILE B 1 129 ? 43.720  90.815  37.184 1.000 99.706  0 129 ILE CCC CA  1 ? 5  
ATOM 2677  C C   . ILE B 1 129 ? 43.209  90.327  38.535 1.000 94.820  0 129 ILE CCC C   1 ? 5  
ATOM 2678  O O   . ILE B 1 129 ? 43.088  91.102  39.492 1.000 101.512 0 129 ILE CCC O   1 ? 5  
ATOM 2679  C CB  . ILE B 1 129 ? 42.572  90.965  36.172 1.000 99.259  0 129 ILE CCC CB  1 ? 5  
ATOM 2680  C CG1 . ILE B 1 129 ? 43.100  91.557  34.868 1.000 104.133 0 129 ILE CCC CG1 1 ? 5  
ATOM 2681  C CG2 . ILE B 1 129 ? 41.471  91.836  36.750 1.000 104.877 0 129 ILE CCC CG2 1 ? 5  
ATOM 2682  C CD1 . ILE B 1 129 ? 42.169  91.362  33.705 1.000 105.080 0 129 ILE CCC CD1 1 ? 5  
ATOM 2683  N N   . TYR B 1 130 ? 42.904  89.034  38.635 1.000 115.306 0 130 TYR CCC N   1 ? 5  
ATOM 2684  C CA  . TYR B 1 130 ? 42.429  88.479  39.898 1.000 95.931  0 130 TYR CCC CA  1 ? 5  
ATOM 2685  C C   . TYR B 1 130 ? 43.465  88.637  41.001 1.000 98.581  0 130 TYR CCC C   1 ? 5  
ATOM 2686  O O   . TYR B 1 130 ? 43.116  88.932  42.152 1.000 115.962 0 130 TYR CCC O   1 ? 5  
ATOM 2687  C CB  . TYR B 1 130 ? 42.081  87.005  39.698 1.000 89.138  0 130 TYR CCC CB  1 ? 5  
ATOM 2688  C CG  . TYR B 1 130 ? 41.330  86.364  40.841 1.000 86.081  0 130 TYR CCC CG  1 ? 5  
ATOM 2689  C CD1 . TYR B 1 130 ? 40.505  87.116  41.665 1.000 88.445  0 130 TYR CCC CD1 1 ? 5  
ATOM 2690  C CD2 . TYR B 1 130 ? 41.435  85.000  41.084 1.000 82.389  0 130 TYR CCC CD2 1 ? 5  
ATOM 2691  C CE1 . TYR B 1 130 ? 39.814  86.527  42.703 1.000 86.706  0 130 TYR CCC CE1 1 ? 5  
ATOM 2692  C CE2 . TYR B 1 130 ? 40.747  84.404  42.120 1.000 78.634  0 130 TYR CCC CE2 1 ? 5  
ATOM 2693  C CZ  . TYR B 1 130 ? 39.938  85.171  42.925 1.000 80.373  0 130 TYR CCC CZ  1 ? 5  
ATOM 2694  O OH  . TYR B 1 130 ? 39.245  84.581  43.956 1.000 93.125  0 130 TYR CCC OH  1 ? 5  
ATOM 2695  N N   . LYS B 1 131 ? 44.738  88.428  40.677 1.000 88.690  0 131 LYS CCC N   1 ? 5  
ATOM 2696  C CA  . LYS B 1 131 ? 45.783  88.587  41.679 1.000 88.456  0 131 LYS CCC CA  1 ? 5  
ATOM 2697  C C   . LYS B 1 131 ? 45.805  90.015  42.208 1.000 98.551  0 131 LYS CCC C   1 ? 5  
ATOM 2698  O O   . LYS B 1 131 ? 46.047  90.241  43.400 1.000 102.464 0 131 LYS CCC O   1 ? 5  
ATOM 2699  C CB  . LYS B 1 131 ? 47.138  88.202  41.085 1.000 89.904  0 131 LYS CCC CB  1 ? 5  
ATOM 2700  C CG  . LYS B 1 131 ? 48.247  88.041  42.118 1.000 90.859  0 131 LYS CCC CG  1 ? 5  
ATOM 2701  C CD  . LYS B 1 131 ? 49.535  87.462  41.544 1.000 82.490  0 131 LYS CCC CD  1 ? 5  
ATOM 2702  C CE  . LYS B 1 131 ? 50.061  88.266  40.393 1.000 89.789  0 131 LYS CCC CE  1 ? 5  
ATOM 2703  N NZ  . LYS B 1 131 ? 51.015  87.465  39.592 1.000 94.900  0 131 LYS CCC NZ  1 ? 5  
ATOM 2704  N N   . ARG B 1 132 ? 45.570  90.989  41.326 1.000 97.549  0 132 ARG CCC N   1 ? 5  
ATOM 2705  C CA  . ARG B 1 132 ? 45.455  92.383  41.746 1.000 101.464 0 132 ARG CCC CA  1 ? 5  
ATOM 2706  C C   . ARG B 1 132 ? 44.371  92.543  42.803 1.000 98.844  0 132 ARG CCC C   1 ? 5  
ATOM 2707  O O   . ARG B 1 132 ? 44.579  93.217  43.819 1.000 100.351 0 132 ARG CCC O   1 ? 5  
ATOM 2708  C CB  . ARG B 1 132 ? 45.177  93.266  40.537 1.000 104.756 0 132 ARG CCC CB  1 ? 5  
ATOM 2709  C CG  . ARG B 1 132 ? 46.352  93.260  39.583 1.000 120.486 0 132 ARG CCC CG  1 ? 5  
ATOM 2710  C CD  . ARG B 1 132 ? 46.201  94.225  38.423 1.000 139.148 0 132 ARG CCC CD  1 ? 5  
ATOM 2711  N NE  . ARG B 1 132 ? 47.223  93.959  37.414 1.000 159.086 0 132 ARG CCC NE  1 ? 5  
ATOM 2712  C CZ  . ARG B 1 132 ? 47.095  94.237  36.123 1.000 160.835 0 132 ARG CCC CZ  1 ? 5  
ATOM 2713  N NH1 . ARG B 1 132 ? 45.969  94.747  35.646 1.000 159.577 0 132 ARG CCC NH1 1 ? 5  
ATOM 2714  N NH2 . ARG B 1 132 ? 48.082  93.923  35.287 1.000 168.972 0 132 ARG CCC NH2 1 ? 5  
ATOM 2715  N N   . TRP B 1 133 ? 43.187  91.958  42.568 1.000 98.367  0 133 TRP CCC N   1 ? 5  
ATOM 2716  C CA  . TRP B 1 133 ? 42.101  92.072  43.542 1.000 95.462  0 133 TRP CCC CA  1 ? 5  
ATOM 2717  C C   . TRP B 1 133 ? 42.466  91.400  44.859 1.000 92.778  0 133 TRP CCC C   1 ? 5  
ATOM 2718  O O   . TRP B 1 133 ? 42.217  91.950  45.939 1.000 93.583  0 133 TRP CCC O   1 ? 5  
ATOM 2719  C CB  . TRP B 1 133 ? 40.818  91.448  42.990 1.000 91.937  0 133 TRP CCC CB  1 ? 5  
ATOM 2720  C CG  . TRP B 1 133 ? 40.316  92.025  41.700 1.000 99.485  0 133 TRP CCC CG  1 ? 5  
ATOM 2721  C CD1 . TRP B 1 133 ? 40.722  93.181  41.092 1.000 105.396 0 133 TRP CCC CD1 1 ? 5  
ATOM 2722  C CD2 . TRP B 1 133 ? 39.329  91.446  40.839 1.000 98.710  0 133 TRP CCC CD2 1 ? 5  
ATOM 2723  N NE1 . TRP B 1 133 ? 40.032  93.364  39.913 1.000 103.911 0 133 TRP CCC NE1 1 ? 5  
ATOM 2724  C CE2 . TRP B 1 133 ? 39.174  92.310  39.735 1.000 99.760  0 133 TRP CCC CE2 1 ? 5  
ATOM 2725  C CE3 . TRP B 1 133 ? 38.558  90.280  40.898 1.000 97.853  0 133 TRP CCC CE3 1 ? 5  
ATOM 2726  C CZ2 . TRP B 1 133 ? 38.279  92.046  38.702 1.000 99.302  0 133 TRP CCC CZ2 1 ? 5  
ATOM 2727  C CZ3 . TRP B 1 133 ? 37.670  90.020  39.871 1.000 95.806  0 133 TRP CCC CZ3 1 ? 5  
ATOM 2728  C CH2 . TRP B 1 133 ? 37.537  90.898  38.789 1.000 99.324  0 133 TRP CCC CH2 1 ? 5  
ATOM 2729  N N   . ILE B 1 134 ? 43.094  90.223  44.788 1.000 135.660 0 134 ILE CCC N   1 ? 5  
ATOM 2730  C CA  . ILE B 1 134 ? 43.461  89.510  46.006 1.000 94.583  0 134 ILE CCC CA  1 ? 5  
ATOM 2731  C C   . ILE B 1 134 ? 44.464  90.322  46.805 1.000 100.376 0 134 ILE CCC C   1 ? 5  
ATOM 2732  O O   . ILE B 1 134 ? 44.353  90.444  48.031 1.000 95.340  0 134 ILE CCC O   1 ? 5  
ATOM 2733  C CB  . ILE B 1 134 ? 44.014  88.116  45.658 1.000 86.656  0 134 ILE CCC CB  1 ? 5  
ATOM 2734  C CG1 . ILE B 1 134 ? 42.907  87.236  45.090 1.000 83.400  0 134 ILE CCC CG1 1 ? 5  
ATOM 2735  C CG2 . ILE B 1 134 ? 44.602  87.442  46.889 1.000 84.561  0 134 ILE CCC CG2 1 ? 5  
ATOM 2736  C CD1 . ILE B 1 134 ? 43.420  86.005  44.391 1.000 79.049  0 134 ILE CCC CD1 1 ? 5  
ATOM 2737  N N   . ILE B 1 135 ? 45.453  90.901  46.124 1.000 94.885  0 135 ILE CCC N   1 ? 5  
ATOM 2738  C CA  . ILE B 1 135 ? 46.444  91.708  46.824 1.000 91.129  0 135 ILE CCC CA  1 ? 5  
ATOM 2739  C C   . ILE B 1 135 ? 45.800  92.958  47.420 1.000 100.045 0 135 ILE CCC C   1 ? 5  
ATOM 2740  O O   . ILE B 1 135 ? 46.114  93.351  48.548 1.000 105.907 0 135 ILE CCC O   1 ? 5  
ATOM 2741  C CB  . ILE B 1 135 ? 47.615  92.032  45.880 1.000 85.942  0 135 ILE CCC CB  1 ? 5  
ATOM 2742  C CG1 . ILE B 1 135 ? 48.471  90.781  45.646 1.000 81.096  0 135 ILE CCC CG1 1 ? 5  
ATOM 2743  C CG2 . ILE B 1 135 ? 48.488  93.131  46.427 1.000 93.121  0 135 ILE CCC CG2 1 ? 5  
ATOM 2744  C CD1 . ILE B 1 135 ? 49.451  90.919  44.488 1.000 92.179  0 135 ILE CCC CD1 1 ? 5  
ATOM 2745  N N   . LEU B 1 136 ? 44.866  93.584  46.696 1.000 96.113  0 136 LEU CCC N   1 ? 5  
ATOM 2746  C CA  . LEU B 1 136 ? 44.100  94.688  47.276 1.000 102.333 0 136 LEU CCC CA  1 ? 5  
ATOM 2747  C C   . LEU B 1 136 ? 43.405  94.264  48.560 1.000 101.602 0 136 LEU CCC C   1 ? 5  
ATOM 2748  O O   . LEU B 1 136 ? 43.420  94.996  49.560 1.000 103.708 0 136 LEU CCC O   1 ? 5  
ATOM 2749  C CB  . LEU B 1 136 ? 43.084  95.227  46.272 1.000 106.106 0 136 LEU CCC CB  1 ? 5  
ATOM 2750  C CG  . LEU B 1 136 ? 43.700  96.073  45.160 1.000 117.794 0 136 LEU CCC CG  1 ? 5  
ATOM 2751  C CD1 . LEU B 1 136 ? 42.643  96.401  44.144 1.000 119.512 0 136 LEU CCC CD1 1 ? 5  
ATOM 2752  C CD2 . LEU B 1 136 ? 44.319  97.357  45.711 1.000 122.354 0 136 LEU CCC CD2 1 ? 5  
ATOM 2753  N N   . GLY B 1 137 ? 42.798  93.078  48.550 1.000 99.276  0 137 GLY CCC N   1 ? 5  
ATOM 2754  C CA  . GLY B 1 137 ? 42.152  92.567  49.747 1.000 95.740  0 137 GLY CCC CA  1 ? 5  
ATOM 2755  C C   . GLY B 1 137 ? 43.114  92.279  50.884 1.000 94.980  0 137 GLY CCC C   1 ? 5  
ATOM 2756  O O   . GLY B 1 137 ? 42.841  92.625  52.035 1.000 107.027 0 137 GLY CCC O   1 ? 5  
ATOM 2757  N N   . LEU B 1 138 ? 44.255  91.651  50.581 1.000 98.300  0 138 LEU CCC N   1 ? 5  
ATOM 2758  C CA  . LEU B 1 138 ? 45.233  91.350  51.627 1.000 91.312  0 138 LEU CCC CA  1 ? 5  
ATOM 2759  C C   . LEU B 1 138 ? 45.792  92.622  52.261 1.000 97.893  0 138 LEU CCC C   1 ? 5  
ATOM 2760  O O   . LEU B 1 138 ? 46.026  92.661  53.475 1.000 100.722 0 138 LEU CCC O   1 ? 5  
ATOM 2761  C CB  . LEU B 1 138 ? 46.358  90.484  51.066 1.000 80.216  0 138 LEU CCC CB  1 ? 5  
ATOM 2762  C CG  . LEU B 1 138 ? 45.936  89.063  50.679 1.000 76.854  0 138 LEU CCC CG  1 ? 5  
ATOM 2763  C CD1 . LEU B 1 138 ? 47.067  88.350  49.958 1.000 76.532  0 138 LEU CCC CD1 1 ? 5  
ATOM 2764  C CD2 . LEU B 1 138 ? 45.471  88.260  51.887 1.000 76.718  0 138 LEU CCC CD2 1 ? 5  
ATOM 2765  N N   . ASN B 1 139 ? 46.032  93.664  51.457 1.000 106.706 0 139 ASN CCC N   1 ? 5  
ATOM 2766  C CA  . ASN B 1 139 ? 46.485  94.943  52.003 1.000 110.918 0 139 ASN CCC CA  1 ? 5  
ATOM 2767  C C   . ASN B 1 139 ? 45.537  95.439  53.088 1.000 118.560 0 139 ASN CCC C   1 ? 5  
ATOM 2768  O O   . ASN B 1 139 ? 45.978  95.921  54.137 1.000 130.489 0 139 ASN CCC O   1 ? 5  
ATOM 2769  C CB  . ASN B 1 139 ? 46.636  95.991  50.897 1.000 112.652 0 139 ASN CCC CB  1 ? 5  
ATOM 2770  C CG  . ASN B 1 139 ? 47.817  95.714  49.977 1.000 120.624 0 139 ASN CCC CG  1 ? 5  
ATOM 2771  O OD1 . ASN B 1 139 ? 48.203  94.568  49.765 1.000 115.516 0 139 ASN CCC OD1 1 ? 5  
ATOM 2772  N ND2 . ASN B 1 139 ? 48.403  96.777  49.434 1.000 140.174 0 139 ASN CCC ND2 1 ? 5  
ATOM 2773  N N   . LYS B 1 140 ? 44.227  95.356  52.847 1.000 114.005 0 140 LYS CCC N   1 ? 5  
ATOM 2774  C CA  . LYS B 1 140 ? 43.280  95.798  53.865 1.000 118.168 0 140 LYS CCC CA  1 ? 5  
ATOM 2775  C C   . LYS B 1 140 ? 43.403  94.960  55.133 1.000 116.037 0 140 LYS CCC C   1 ? 5  
ATOM 2776  O O   . LYS B 1 140 ? 43.418  95.503  56.241 1.000 131.487 0 140 LYS CCC O   1 ? 5  
ATOM 2777  C CB  . LYS B 1 140 ? 41.844  95.712  53.344 1.000 118.218 0 140 LYS CCC CB  1 ? 5  
ATOM 2778  C CG  . LYS B 1 140 ? 41.454  96.691  52.253 1.000 126.075 0 140 LYS CCC CG  1 ? 5  
ATOM 2779  C CD  . LYS B 1 140 ? 39.981  96.495  51.913 1.000 128.567 0 140 LYS CCC CD  1 ? 5  
ATOM 2780  C CE  . LYS B 1 140 ? 39.443  97.607  51.032 1.000 130.023 0 140 LYS CCC CE  1 ? 5  
ATOM 2781  N NZ  . LYS B 1 140 ? 38.049  97.307  50.598 1.000 136.260 0 140 LYS CCC NZ  1 ? 5  
ATOM 2782  N N   . ILE B 1 141 ? 43.576  93.644  54.986 1.000 108.264 0 141 ILE CCC N   1 ? 5  
ATOM 2783  C CA  . ILE B 1 141 ? 43.689  92.764  56.151 1.000 109.036 0 141 ILE CCC CA  1 ? 5  
ATOM 2784  C C   . ILE B 1 141 ? 44.944  93.058  56.973 1.000 119.959 0 141 ILE CCC C   1 ? 5  
ATOM 2785  O O   . ILE B 1 141 ? 44.878  93.140  58.205 1.000 124.611 0 141 ILE CCC O   1 ? 5  
ATOM 2786  C CB  . ILE B 1 141 ? 43.613  91.289  55.713 1.000 103.109 0 141 ILE CCC CB  1 ? 5  
ATOM 2787  C CG1 . ILE B 1 141 ? 42.223  90.978  55.157 1.000 99.740  0 141 ILE CCC CG1 1 ? 5  
ATOM 2788  C CG2 . ILE B 1 141 ? 43.945  90.349  56.857 1.000 107.803 0 141 ILE CCC CG2 1 ? 5  
ATOM 2789  C CD1 . ILE B 1 141 ? 42.180  89.754  54.290 1.000 109.250 0 141 ILE CCC CD1 1 ? 5  
ATOM 2790  N N   . VAL B 1 142 ? 46.101  93.215  56.324 1.000 122.249 0 142 VAL CCC N   1 ? 5  
ATOM 2791  C CA  . VAL B 1 142 ? 47.320  93.546  57.069 1.000 120.579 0 142 VAL CCC CA  1 ? 5  
ATOM 2792  C C   . VAL B 1 142 ? 47.133  94.830  57.871 1.000 118.162 0 142 VAL CCC C   1 ? 5  
ATOM 2793  O O   . VAL B 1 142 ? 47.593  94.931  59.014 1.000 126.353 0 142 VAL CCC O   1 ? 5  
ATOM 2794  C CB  . VAL B 1 142 ? 48.559  93.592  56.153 1.000 115.121 0 142 VAL CCC CB  1 ? 5  
ATOM 2795  C CG1 . VAL B 1 142 ? 48.591  92.360  55.269 1.000 112.044 0 142 VAL CCC CG1 1 ? 5  
ATOM 2796  C CG2 . VAL B 1 142 ? 48.624  94.866  55.338 1.000 119.639 0 142 VAL CCC CG2 1 ? 5  
ATOM 2797  N N   . ARG B 1 143 ? 46.478  95.837  57.288 1.000 123.464 0 143 ARG CCC N   1 ? 5  
ATOM 2798  C CA  . ARG B 1 143 ? 46.275  97.079  58.025 1.000 131.392 0 143 ARG CCC CA  1 ? 5  
ATOM 2799  C C   . ARG B 1 143 ? 45.371  96.847  59.230 1.000 134.309 0 143 ARG CCC C   1 ? 5  
ATOM 2800  O O   . ARG B 1 143 ? 45.647  97.355  60.323 1.000 143.630 0 143 ARG CCC O   1 ? 5  
ATOM 2801  C CB  . ARG B 1 143 ? 45.671  98.159  57.132 1.000 136.018 0 143 ARG CCC CB  1 ? 5  
ATOM 2802  C CG  . ARG B 1 143 ? 45.580  99.502  57.852 1.000 151.166 0 143 ARG CCC CG  1 ? 5  
ATOM 2803  C CD  . ARG B 1 143 ? 45.171  100.644 56.940 1.000 164.784 0 143 ARG CCC CD  1 ? 5  
ATOM 2804  N NE  . ARG B 1 143 ? 43.826  100.447 56.414 1.000 169.289 0 143 ARG CCC NE  1 ? 5  
ATOM 2805  C CZ  . ARG B 1 143 ? 43.535  100.075 55.171 1.000 168.996 0 143 ARG CCC CZ  1 ? 5  
ATOM 2806  N NH1 . ARG B 1 143 ? 44.493  99.870  54.279 1.000 164.772 0 143 ARG CCC NH1 1 ? 5  
ATOM 2807  N NH2 . ARG B 1 143 ? 42.270  99.899  54.826 1.000 169.309 0 143 ARG CCC NH2 1 ? 5  
ATOM 2808  N N   . MET B 1 144 ? 44.288  96.083  59.054 1.000 129.431 0 144 MET CCC N   1 ? 5  
ATOM 2809  C CA  . MET B 1 144 ? 43.359  95.850  60.157 1.000 128.527 0 144 MET CCC CA  1 ? 5  
ATOM 2810  C C   . MET B 1 144 ? 44.053  95.119  61.296 1.000 129.801 0 144 MET CCC C   1 ? 5  
ATOM 2811  O O   . MET B 1 144 ? 43.793  95.390  62.474 1.000 141.380 0 144 MET CCC O   1 ? 5  
ATOM 2812  C CB  . MET B 1 144 ? 42.156  95.028  59.688 1.000 128.670 0 144 MET CCC CB  1 ? 5  
ATOM 2813  C CG  . MET B 1 144 ? 41.432  95.560  58.468 1.000 133.873 0 144 MET CCC CG  1 ? 5  
ATOM 2814  S SD  . MET B 1 144 ? 40.062  96.657  58.779 1.000 166.068 0 144 MET CCC SD  1 ? 5  
ATOM 2815  C CE  . MET B 1 144 ? 39.849  97.399  57.156 1.000 157.795 0 144 MET CCC CE  1 ? 5  
ATOM 2816  N N   . TYR B 1 145 ? 44.938  94.188  60.961 1.000 125.902 0 145 TYR CCC N   1 ? 5  
ATOM 2817  C CA  . TYR B 1 145 ? 45.603  93.324  61.923 1.000 128.816 0 145 TYR CCC CA  1 ? 5  
ATOM 2818  C C   . TYR B 1 145 ? 46.908  93.905  62.463 1.000 129.923 0 145 TYR CCC C   1 ? 5  
ATOM 2819  O O   . TYR B 1 145 ? 47.589  93.224  63.237 1.000 134.566 0 145 TYR CCC O   1 ? 5  
ATOM 2820  C CB  . TYR B 1 145 ? 45.860  91.949  61.295 1.000 125.807 0 145 TYR CCC CB  1 ? 5  
ATOM 2821  C CG  . TYR B 1 145 ? 44.604  91.116  61.111 1.000 123.300 0 145 TYR CCC CG  1 ? 5  
ATOM 2822  C CD1 . TYR B 1 145 ? 43.338  91.675  61.275 1.000 119.219 0 145 TYR CCC CD1 1 ? 5  
ATOM 2823  C CD2 . TYR B 1 145 ? 44.684  89.766  60.796 1.000 124.687 0 145 TYR CCC CD2 1 ? 5  
ATOM 2824  C CE1 . TYR B 1 145 ? 42.191  90.919  61.108 1.000 116.425 0 145 TYR CCC CE1 1 ? 5  
ATOM 2825  C CE2 . TYR B 1 145 ? 43.541  88.998  60.634 1.000 125.256 0 145 TYR CCC CE2 1 ? 5  
ATOM 2826  C CZ  . TYR B 1 145 ? 42.295  89.579  60.795 1.000 119.630 0 145 TYR CCC CZ  1 ? 5  
ATOM 2827  O OH  . TYR B 1 145 ? 41.159  88.819  60.627 1.000 115.018 0 145 TYR CCC OH  1 ? 5  
ATOM 2828  N N   . SER B 1 146 ? 47.281  95.123  62.074 1.000 125.461 0 146 SER CCC N   1 ? 6  
ATOM 2829  C CA  . SER B 1 146 ? 48.435  95.773  62.688 1.000 127.988 0 146 SER CCC CA  1 ? 6  
ATOM 2830  C C   . SER B 1 146 ? 48.139  95.945  64.172 1.000 138.128 0 146 SER CCC C   1 ? 6  
ATOM 2831  O O   . SER B 1 146 ? 47.151  96.606  64.520 1.000 143.127 0 146 SER CCC O   1 ? 6  
ATOM 2832  C CB  . SER B 1 146 ? 48.696  97.127  62.034 1.000 127.229 0 146 SER CCC CB  1 ? 6  
ATOM 2833  O OG  . SER B 1 146 ? 49.809  97.775  62.621 1.000 135.380 0 146 SER CCC OG  1 ? 6  
ATOM 2834  N N   . PRO B 1 147 ? 48.948  95.374  65.074 1.000 141.218 0 147 PRO CCC N   1 ? 6  
ATOM 2835  C CA  . PRO B 1 147 ? 48.577  95.408  66.498 1.000 146.110 0 147 PRO CCC CA  1 ? 6  
ATOM 2836  C C   . PRO B 1 147 ? 48.798  96.726  67.221 1.000 146.656 0 147 PRO CCC C   1 ? 6  
ATOM 2837  O O   . PRO B 1 147 ? 48.139  96.953  68.246 1.000 155.000 0 147 PRO CCC O   1 ? 6  
ATOM 2838  C CB  . PRO B 1 147 ? 49.469  94.313  67.103 1.000 146.712 0 147 PRO CCC CB  1 ? 6  
ATOM 2839  C CG  . PRO B 1 147 ? 50.681  94.287  66.205 1.000 137.041 0 147 PRO CCC CG  1 ? 6  
ATOM 2840  C CD  . PRO B 1 147 ? 50.190  94.622  64.825 1.000 138.541 0 147 PRO CCC CD  1 ? 6  
ATOM 2841  N N   . THR B 1 148 ? 49.667  97.606  66.727 1.000 143.630 0 148 THR CCC N   1 ? 6  
ATOM 2842  C CA  . THR B 1 148 ? 50.020  98.813  67.459 1.000 141.999 0 148 THR CCC CA  1 ? 6  
ATOM 2843  C C   . THR B 1 148 ? 50.072  99.984  66.491 1.000 141.088 0 148 THR CCC C   1 ? 6  
ATOM 2844  O O   . THR B 1 148 ? 50.576  99.843  65.373 1.000 147.472 0 148 THR CCC O   1 ? 6  
ATOM 2845  C CB  . THR B 1 148 ? 51.364  98.667  68.206 1.000 144.250 0 148 THR CCC CB  1 ? 6  
ATOM 2846  O OG1 . THR B 1 148 ? 52.427  98.480  67.264 1.000 155.289 0 148 THR CCC OG1 1 ? 6  
ATOM 2847  C CG2 . THR B 1 148 ? 51.341  97.482  69.172 1.000 145.063 0 148 THR CCC CG2 1 ? 6  
ATOM 2848  N N   . SER B 1 149 ? 49.561  101.133 66.936 1.000 137.452 0 149 SER CCC N   1 ? 6  
ATOM 2849  C CA  . SER B 1 149 ? 49.713  102.392 66.224 1.000 141.560 0 149 SER CCC CA  1 ? 6  
ATOM 2850  C C   . SER B 1 149 ? 51.100  102.923 66.509 1.000 139.955 0 149 SER CCC C   1 ? 6  
ATOM 2851  O O   . SER B 1 149 ? 51.646  102.717 67.595 1.000 146.861 0 149 SER CCC O   1 ? 6  
ATOM 2852  C CB  . SER B 1 149 ? 48.688  103.443 66.652 1.000 150.722 0 149 SER CCC CB  1 ? 6  
ATOM 2853  O OG  . SER B 1 149 ? 49.102  104.743 66.232 1.000 151.202 0 149 SER CCC OG  1 ? 6  
ATOM 2854  N N   . ILE B 1 150 ? 51.686  103.581 65.518 1.000 132.737 0 150 ILE CCC N   1 ? 6  
ATOM 2855  C CA  A ILE B 1 150 ? 52.974  104.233 65.734 1.000 138.172 0 150 ILE CCC CA  1 ? 6  
ATOM 2856  C C   . ILE B 1 150 ? 52.954  105.158 66.943 1.000 144.612 0 150 ILE CCC C   1 ? 6  
ATOM 2857  O O   . ILE B 1 150 ? 53.970  105.316 67.636 1.000 142.025 0 150 ILE CCC O   1 ? 6  
ATOM 2858  C CB  A ILE B 1 150 ? 53.388  104.996 64.470 1.000 130.289 0 150 ILE CCC CB  1 ? 6  
ATOM 2859  C CG1 A ILE B 1 150 ? 53.311  104.111 63.248 1.000 144.284 0 150 ILE CCC CG1 1 ? 6  
ATOM 2860  C CG2 A ILE B 1 150 ? 54.704  105.694 64.641 1.000 139.264 0 150 ILE CCC CG2 1 ? 6  
ATOM 2861  C CD1 A ILE B 1 150 ? 53.363  104.942 62.065 1.000 151.678 0 150 ILE CCC CD1 1 ? 6  
ATOM 2862  N N   . LEU B 1 151 ? 51.815  105.800 67.205 1.000 146.675 0 151 LEU CCC N   1 ? 6  
ATOM 2863  C CA  . LEU B 1 151 ? 51.748  106.705 68.342 1.000 146.886 0 151 LEU CCC CA  1 ? 6  
ATOM 2864  C C   . LEU B 1 151 ? 52.062  105.972 69.641 1.000 146.904 0 151 LEU CCC C   1 ? 6  
ATOM 2865  O O   . LEU B 1 151 ? 52.486  106.602 70.618 1.000 153.153 0 151 LEU CCC O   1 ? 6  
ATOM 2866  C CB  . LEU B 1 151 ? 50.351  107.331 68.403 1.000 155.015 0 151 LEU CCC CB  1 ? 6  
ATOM 2867  C CG  . LEU B 1 151 ? 49.904  108.099 67.152 1.000 154.571 0 151 LEU CCC CG  1 ? 6  
ATOM 2868  C CD1 . LEU B 1 151 ? 48.493  108.682 67.306 1.000 164.495 0 151 LEU CCC CD1 1 ? 6  
ATOM 2869  C CD2 . LEU B 1 151 ? 50.913  109.186 66.815 1.000 152.296 0 151 LEU CCC CD2 1 ? 6  
ATOM 2870  N N   . ASP B 1 152 ? 51.858  104.655 69.666 1.000 155.299 0 152 ASP CCC N   1 ? 6  
ATOM 2871  C CA  . ASP B 1 152 ? 52.126  103.826 70.830 1.000 159.956 0 152 ASP CCC CA  1 ? 6  
ATOM 2872  C C   . ASP B 1 152 ? 53.479  103.127 70.754 1.000 152.907 0 152 ASP CCC C   1 ? 6  
ATOM 2873  O O   . ASP B 1 152 ? 53.829  102.385 71.677 1.000 157.753 0 152 ASP CCC O   1 ? 6  
ATOM 2874  C CB  . ASP B 1 152 ? 51.009  102.788 71.012 1.000 173.275 0 152 ASP CCC CB  1 ? 6  
ATOM 2875  C CG  . ASP B 1 152 ? 49.687  103.421 71.396 1.000 190.181 0 152 ASP CCC CG  1 ? 6  
ATOM 2876  O OD1 . ASP B 1 152 ? 49.641  104.664 71.499 1.000 196.777 0 152 ASP CCC OD1 1 ? 6  
ATOM 2877  O OD2 . ASP B 1 152 ? 48.696  102.681 71.585 1.000 202.562 0 152 ASP CCC OD2 1 ? 6  
ATOM 2878  N N   . ILE B 1 153 ? 54.253  103.356 69.697 1.000 145.248 0 153 ILE CCC N   1 ? 6  
ATOM 2879  C CA  . ILE B 1 153 ? 55.604  102.812 69.582 1.000 140.649 0 153 ILE CCC CA  1 ? 6  
ATOM 2880  C C   . ILE B 1 153 ? 56.594  103.786 70.209 1.000 139.896 0 153 ILE CCC C   1 ? 6  
ATOM 2881  O O   . ILE B 1 153 ? 56.903  104.833 69.634 1.000 143.298 0 153 ILE CCC O   1 ? 6  
ATOM 2882  C CB  . ILE B 1 153 ? 55.972  102.509 68.126 1.000 138.187 0 153 ILE CCC CB  1 ? 6  
ATOM 2883  C CG1 . ILE B 1 153 ? 54.936  101.575 67.502 1.000 141.736 0 153 ILE CCC CG1 1 ? 6  
ATOM 2884  C CG2 . ILE B 1 153 ? 57.354  101.887 68.051 1.000 129.732 0 153 ILE CCC CG2 1 ? 6  
ATOM 2885  C CD1 . ILE B 1 153 ? 54.896  100.210 68.155 1.000 144.972 0 153 ILE CCC CD1 1 ? 6  
ATOM 2886  N N   . ARG B 1 154 ? 57.103  103.431 71.384 1.000 130.810 0 154 ARG CCC N   1 ? 6  
ATOM 2887  C CA  . ARG B 1 154 ? 58.042  104.254 72.131 1.000 134.089 0 154 ARG CCC CA  1 ? 6  
ATOM 2888  C C   . ARG B 1 154 ? 59.217  103.389 72.562 1.000 133.924 0 154 ARG CCC C   1 ? 6  
ATOM 2889  O O   . ARG B 1 154 ? 59.036  102.218 72.913 1.000 136.038 0 154 ARG CCC O   1 ? 6  
ATOM 2890  C CB  . ARG B 1 154 ? 57.356  104.898 73.340 1.000 146.799 0 154 ARG CCC CB  1 ? 6  
ATOM 2891  C CG  . ARG B 1 154 ? 56.135  105.718 72.956 1.000 150.753 0 154 ARG CCC CG  1 ? 6  
ATOM 2892  C CD  . ARG B 1 154 ? 55.625  106.569 74.095 1.000 159.409 0 154 ARG CCC CD  1 ? 6  
ATOM 2893  N NE  . ARG B 1 154 ? 54.306  107.101 73.781 1.000 164.434 0 154 ARG CCC NE  1 ? 6  
ATOM 2894  C CZ  . ARG B 1 154 ? 53.170  106.493 74.088 1.000 170.982 0 154 ARG CCC CZ  1 ? 6  
ATOM 2895  N NH1 . ARG B 1 154 ? 53.161  105.322 74.708 1.000 172.337 0 154 ARG CCC NH1 1 ? 6  
ATOM 2896  N NH2 . ARG B 1 154 ? 52.016  107.064 73.760 1.000 182.785 0 154 ARG CCC NH2 1 ? 6  
ATOM 2897  N N   . GLN B 1 155 ? 60.420  103.960 72.518 1.000 132.791 0 155 GLN CCC N   1 ? 6  
ATOM 2898  C CA  . GLN B 1 155 ? 61.623  103.187 72.803 1.000 136.434 0 155 GLN CCC CA  1 ? 6  
ATOM 2899  C C   . GLN B 1 155 ? 61.696  102.805 74.274 1.000 139.545 0 155 GLN CCC C   1 ? 6  
ATOM 2900  O O   . GLN B 1 155 ? 61.505  103.644 75.160 1.000 140.666 0 155 GLN CCC O   1 ? 6  
ATOM 2901  C CB  . GLN B 1 155 ? 62.877  103.963 72.403 1.000 136.021 0 155 GLN CCC CB  1 ? 6  
ATOM 2902  C CG  . GLN B 1 155 ? 64.150  103.125 72.490 1.000 136.919 0 155 GLN CCC CG  1 ? 6  
ATOM 2903  C CD  . GLN B 1 155 ? 65.406  103.923 72.215 1.000 130.210 0 155 GLN CCC CD  1 ? 6  
ATOM 2904  O OE1 . GLN B 1 155 ? 65.373  105.151 72.165 1.000 137.566 0 155 GLN CCC OE1 1 ? 6  
ATOM 2905  N NE2 . GLN B 1 155 ? 66.525  103.227 72.042 1.000 122.197 0 155 GLN CCC NE2 1 ? 6  
ATOM 2906  N N   . GLY B 1 156 ? 61.964  101.526 74.526 1.000 145.680 0 156 GLY CCC N   1 ? 6  
ATOM 2907  C CA  . GLY B 1 156 ? 62.150  101.015 75.861 1.000 150.073 0 156 GLY CCC CA  1 ? 6  
ATOM 2908  C C   . GLY B 1 156 ? 63.446  101.498 76.477 1.000 152.688 0 156 GLY CCC C   1 ? 6  
ATOM 2909  O O   . GLY B 1 156 ? 64.379  101.908 75.779 1.000 154.782 0 156 GLY CCC O   1 ? 6  
ATOM 2910  N N   . PRO B 1 157 ? 63.529  101.461 77.810 1.000 154.325 0 157 PRO CCC N   1 ? 6  
ATOM 2911  C CA  A PRO B 1 157 ? 64.714  102.031 78.470 1.000 159.727 0 157 PRO CCC CA  1 ? 6  
ATOM 2912  C C   . PRO B 1 157 ? 65.996  101.276 78.165 1.000 160.269 0 157 PRO CCC C   1 ? 6  
ATOM 2913  O O   . PRO B 1 157 ? 67.037  101.902 77.932 1.000 166.684 0 157 PRO CCC O   1 ? 6  
ATOM 2914  C CB  A PRO B 1 157 ? 64.332  101.969 79.952 1.000 166.356 0 157 PRO CCC CB  1 ? 6  
ATOM 2915  C CG  A PRO B 1 157 ? 63.465  100.745 80.048 1.000 164.907 0 157 PRO CCC CG  1 ? 6  
ATOM 2916  C CD  A PRO B 1 157 ? 62.719  100.648 78.737 1.000 155.337 0 157 PRO CCC CD  1 ? 6  
ATOM 2917  N N   . LYS B 1 158 ? 65.951  99.947  78.145 1.000 161.993 0 158 LYS CCC N   1 ? 6  
ATOM 2918  C CA  . LYS B 1 158 ? 67.105  99.118  77.822 1.000 169.082 0 158 LYS CCC CA  1 ? 6  
ATOM 2919  C C   . LYS B 1 158 ? 67.090  98.641  76.375 1.000 169.173 0 158 LYS CCC C   1 ? 6  
ATOM 2920  O O   . LYS B 1 158 ? 67.905  97.788  76.004 1.000 176.751 0 158 LYS CCC O   1 ? 6  
ATOM 2921  C CB  . LYS B 1 158 ? 67.202  97.927  78.783 1.000 179.506 0 158 LYS CCC CB  1 ? 6  
ATOM 2922  C CG  . LYS B 1 158 ? 65.879  97.346  79.260 1.000 186.138 0 158 LYS CCC CG  1 ? 6  
ATOM 2923  C CD  . LYS B 1 158 ? 66.125  96.316  80.361 1.000 194.352 0 158 LYS CCC CD  1 ? 6  
ATOM 2924  C CE  . LYS B 1 158 ? 64.829  95.762  80.929 1.000 192.301 0 158 LYS CCC CE  1 ? 6  
ATOM 2925  N NZ  . LYS B 1 158 ? 65.091  94.759  82.001 1.000 194.736 0 158 LYS CCC NZ  1 ? 6  
ATOM 2926  N N   . GLU B 1 159 ? 66.187  99.168  75.554 1.000 154.717 0 159 GLU CCC N   1 ? 6  
ATOM 2927  C CA  . GLU B 1 159 ? 66.063  98.716  74.176 1.000 136.601 0 159 GLU CCC CA  1 ? 6  
ATOM 2928  C C   . GLU B 1 159 ? 67.116  99.375  73.291 1.000 131.904 0 159 GLU CCC C   1 ? 6  
ATOM 2929  O O   . GLU B 1 159 ? 67.200  100.607 73.253 1.000 128.402 0 159 GLU CCC O   1 ? 6  
ATOM 2930  C CB  . GLU B 1 159 ? 64.677  99.052  73.646 1.000 134.716 0 159 GLU CCC CB  1 ? 6  
ATOM 2931  C CG  . GLU B 1 159 ? 64.407  98.542  72.249 1.000 137.459 0 159 GLU CCC CG  1 ? 6  
ATOM 2932  C CD  . GLU B 1 159 ? 63.016  98.896  71.762 1.000 133.649 0 159 GLU CCC CD  1 ? 6  
ATOM 2933  O OE1 . GLU B 1 159 ? 62.400  99.819  72.338 1.000 127.588 0 159 GLU CCC OE1 1 ? 6  
ATOM 2934  O OE2 . GLU B 1 159 ? 62.542  98.254  70.803 1.000 137.951 0 159 GLU CCC OE2 1 ? 6  
ATOM 2935  N N   . PRO B 1 160 ? 67.933  98.597  72.585 1.000 128.740 0 160 PRO CCC N   1 ? 6  
ATOM 2936  C CA  . PRO B 1 160 ? 68.855  99.162  71.589 1.000 129.995 0 160 PRO CCC CA  1 ? 6  
ATOM 2937  C C   . PRO B 1 160 ? 68.124  100.008 70.557 1.000 127.287 0 160 PRO CCC C   1 ? 6  
ATOM 2938  O O   . PRO B 1 160 ? 67.028  99.666  70.114 1.000 137.412 0 160 PRO CCC O   1 ? 6  
ATOM 2939  C CB  . PRO B 1 160 ? 69.493  97.920  70.960 1.000 133.825 0 160 PRO CCC CB  1 ? 6  
ATOM 2940  C CG  . PRO B 1 160 ? 69.386  96.866  72.023 1.000 132.924 0 160 PRO CCC CG  1 ? 6  
ATOM 2941  C CD  . PRO B 1 160 ? 68.093  97.139  72.732 1.000 129.906 0 160 PRO CCC CD  1 ? 6  
ATOM 2942  N N   . PHE B 1 161 ? 68.739  101.135 70.193 1.000 118.333 0 161 PHE CCC N   1 ? 6  
ATOM 2943  C CA  . PHE B 1 161 ? 68.122  102.057 69.238 1.000 110.864 0 161 PHE CCC CA  1 ? 6  
ATOM 2944  C C   . PHE B 1 161 ? 67.747  101.351 67.935 1.000 115.381 0 161 PHE CCC C   1 ? 6  
ATOM 2945  O O   . PHE B 1 161 ? 66.703  101.641 67.345 1.000 112.855 0 161 PHE CCC O   1 ? 6  
ATOM 2946  C CB  . PHE B 1 161 ? 69.060  103.232 68.973 1.000 105.034 0 161 PHE CCC CB  1 ? 6  
ATOM 2947  C CG  . PHE B 1 161 ? 68.441  104.342 68.171 1.000 102.889 0 161 PHE CCC CG  1 ? 6  
ATOM 2948  C CD1 . PHE B 1 161 ? 67.291  104.994 68.606 1.000 107.001 0 161 PHE CCC CD1 1 ? 6  
ATOM 2949  C CD2 . PHE B 1 161 ? 68.999  104.717 66.963 1.000 102.794 0 161 PHE CCC CD2 1 ? 6  
ATOM 2950  C CE1 . PHE B 1 161 ? 66.732  106.022 67.854 1.000 101.531 0 161 PHE CCC CE1 1 ? 6  
ATOM 2951  C CE2 . PHE B 1 161 ? 68.443  105.732 66.207 1.000 99.341  0 161 PHE CCC CE2 1 ? 6  
ATOM 2952  C CZ  . PHE B 1 161 ? 67.307  106.385 66.656 1.000 98.881  0 161 PHE CCC CZ  1 ? 6  
ATOM 2953  N N   . ARG B 1 162 ? 68.606  100.438 67.444 1.000 121.992 0 162 ARG CCC N   1 ? 6  
ATOM 2954  C CA  . ARG B 1 162 ? 68.279  99.721  66.211 1.000 125.560 0 162 ARG CCC CA  1 ? 6  
ATOM 2955  C C   . ARG B 1 162 ? 66.944  99.001  66.328 1.000 123.220 0 162 ARG CCC C   1 ? 6  
ATOM 2956  O O   . ARG B 1 162 ? 66.141  99.018  65.389 1.000 131.585 0 162 ARG CCC O   1 ? 6  
ATOM 2957  C CB  . ARG B 1 162 ? 69.352  98.694  65.833 1.000 133.961 0 162 ARG CCC CB  1 ? 6  
ATOM 2958  C CG  . ARG B 1 162 ? 70.757  99.201  65.602 1.000 150.449 0 162 ARG CCC CG  1 ? 6  
ATOM 2959  C CD  . ARG B 1 162 ? 71.574  98.149  64.849 1.000 148.064 0 162 ARG CCC CD  1 ? 6  
ATOM 2960  N NE  . ARG B 1 162 ? 71.543  96.838  65.456 1.000 155.911 0 162 ARG CCC NE  1 ? 6  
ATOM 2961  C CZ  . ARG B 1 162 ? 70.797  95.815  65.057 1.000 159.523 0 162 ARG CCC CZ  1 ? 6  
ATOM 2962  N NH1 . ARG B 1 162 ? 69.993  95.939  64.018 1.000 155.362 0 162 ARG CCC NH1 1 ? 6  
ATOM 2963  N NH2 . ARG B 1 162 ? 70.851  94.662  65.713 1.000 166.994 0 162 ARG CCC NH2 1 ? 6  
ATOM 2964  N N   . ASP B 1 163 ? 66.682  98.373  67.478 1.000 118.508 0 163 ASP CCC N   1 ? 6  
ATOM 2965  C CA  . ASP B 1 163 ? 65.440  97.622  67.648 1.000 120.122 0 163 ASP CCC CA  1 ? 6  
ATOM 2966  C C   . ASP B 1 163 ? 64.219  98.532  67.716 1.000 120.253 0 163 ASP CCC C   1 ? 6  
ATOM 2967  O O   . ASP B 1 163 ? 63.154  98.175  67.201 1.000 125.083 0 163 ASP CCC O   1 ? 6  
ATOM 2968  C CB  . ASP B 1 163 ? 65.522  96.765  68.910 1.000 128.007 0 163 ASP CCC CB  1 ? 6  
ATOM 2969  C CG  . ASP B 1 163 ? 66.613  95.720  68.828 1.000 140.635 0 163 ASP CCC CG  1 ? 6  
ATOM 2970  O OD1 . ASP B 1 163 ? 66.959  95.319  67.698 1.000 147.278 0 163 ASP CCC OD1 1 ? 6  
ATOM 2971  O OD2 . ASP B 1 163 ? 67.118  95.300  69.892 1.000 140.271 0 163 ASP CCC OD2 1 ? 6  
ATOM 2972  N N   . TYR B 1 164 ? 64.335  99.698  68.353 1.000 115.581 0 164 TYR CCC N   1 ? 6  
ATOM 2973  C CA  . TYR B 1 164 ? 63.217  100.637 68.345 1.000 112.750 0 164 TYR CCC CA  1 ? 6  
ATOM 2974  C C   . TYR B 1 164 ? 62.929  101.116 66.926 1.000 114.780 0 164 TYR CCC C   1 ? 6  
ATOM 2975  O O   . TYR B 1 164 ? 61.771  101.165 66.492 1.000 117.981 0 164 TYR CCC O   1 ? 6  
ATOM 2976  C CB  . TYR B 1 164 ? 63.518  101.804 69.286 1.000 110.632 0 164 TYR CCC CB  1 ? 6  
ATOM 2977  C CG  . TYR B 1 164 ? 62.777  103.094 69.016 1.000 108.553 0 164 TYR CCC CG  1 ? 6  
ATOM 2978  C CD1 . TYR B 1 164 ? 61.401  103.166 69.170 1.000 115.757 0 164 TYR CCC CD1 1 ? 6  
ATOM 2979  C CD2 . TYR B 1 164 ? 63.456  104.248 68.647 1.000 111.004 0 164 TYR CCC CD2 1 ? 6  
ATOM 2980  C CE1 . TYR B 1 164 ? 60.717  104.342 68.944 1.000 117.865 0 164 TYR CCC CE1 1 ? 6  
ATOM 2981  C CE2 . TYR B 1 164 ? 62.778  105.434 68.418 1.000 111.043 0 164 TYR CCC CE2 1 ? 6  
ATOM 2982  C CZ  . TYR B 1 164 ? 61.407  105.472 68.568 1.000 113.304 0 164 TYR CCC CZ  1 ? 6  
ATOM 2983  O OH  . TYR B 1 164 ? 60.713  106.638 68.346 1.000 115.925 0 164 TYR CCC OH  1 ? 6  
ATOM 2984  N N   . VAL B 1 165 ? 63.979  101.481 66.189 1.000 110.943 0 165 VAL CCC N   1 ? 6  
ATOM 2985  C CA  . VAL B 1 165 ? 63.803  101.934 64.812 1.000 106.512 0 165 VAL CCC CA  1 ? 6  
ATOM 2986  C C   . VAL B 1 165 ? 63.239  100.813 63.935 1.000 104.398 0 165 VAL CCC C   1 ? 6  
ATOM 2987  O O   . VAL B 1 165 ? 62.369  101.051 63.089 1.000 107.876 0 165 VAL CCC O   1 ? 6  
ATOM 2988  C CB  . VAL B 1 165 ? 65.132  102.485 64.265 1.000 103.611 0 165 VAL CCC CB  1 ? 6  
ATOM 2989  C CG1 . VAL B 1 165 ? 64.974  102.914 62.813 1.000 109.109 0 165 VAL CCC CG1 1 ? 6  
ATOM 2990  C CG2 . VAL B 1 165 ? 65.629  103.637 65.132 1.000 101.719 0 165 VAL CCC CG2 1 ? 6  
ATOM 2991  N N   . ASP B 1 166 ? 63.721  99.575  64.124 1.000 103.388 0 166 ASP CCC N   1 ? 6  
ATOM 2992  C CA  . ASP B 1 166 ? 63.135  98.418  63.438 1.000 105.178 0 166 ASP CCC CA  1 ? 6  
ATOM 2993  C C   . ASP B 1 166 ? 61.636  98.307  63.704 1.000 110.218 0 166 ASP CCC C   1 ? 6  
ATOM 2994  O O   . ASP B 1 166 ? 60.844  98.099  62.777 1.000 118.103 0 166 ASP CCC O   1 ? 6  
ATOM 2995  C CB  . ASP B 1 166 ? 63.857  97.127  63.844 1.000 108.844 0 166 ASP CCC CB  1 ? 6  
ATOM 2996  C CG  . ASP B 1 166 ? 65.174  96.918  63.095 1.000 117.073 0 166 ASP CCC CG  1 ? 6  
ATOM 2997  O OD1 . ASP B 1 166 ? 65.385  97.569  62.049 1.000 120.139 0 166 ASP CCC OD1 1 ? 6  
ATOM 2998  O OD2 . ASP B 1 166 ? 66.008  96.108  63.564 1.000 122.148 0 166 ASP CCC OD2 1 ? 6  
ATOM 2999  N N   . ARG B 1 167 ? 61.228  98.436  64.969 1.000 108.518 0 167 ARG CCC N   1 ? 6  
ATOM 3000  C CA  . ARG B 1 167 ? 59.808  98.349  65.308 1.000 108.049 0 167 ARG CCC CA  1 ? 6  
ATOM 3001  C C   . ARG B 1 167 ? 59.034  99.498  64.676 1.000 108.095 0 167 ARG CCC C   1 ? 6  
ATOM 3002  O O   . ARG B 1 167 ? 57.904  99.319  64.205 1.000 106.592 0 167 ARG CCC O   1 ? 6  
ATOM 3003  C CB  . ARG B 1 167 ? 59.603  98.327  66.823 1.000 112.695 0 167 ARG CCC CB  1 ? 6  
ATOM 3004  C CG  . ARG B 1 167 ? 60.109  97.056  67.487 1.000 121.402 0 167 ARG CCC CG  1 ? 6  
ATOM 3005  C CD  . ARG B 1 167 ? 59.642  96.937  68.933 1.000 125.700 0 167 ARG CCC CD  1 ? 6  
ATOM 3006  N NE  . ARG B 1 167 ? 59.993  98.091  69.752 1.000 127.194 0 167 ARG CCC NE  1 ? 6  
ATOM 3007  C CZ  . ARG B 1 167 ? 59.107  98.940  70.256 1.000 131.014 0 167 ARG CCC CZ  1 ? 6  
ATOM 3008  N NH1 . ARG B 1 167 ? 57.809  98.791  70.044 1.000 134.429 0 167 ARG CCC NH1 1 ? 6  
ATOM 3009  N NH2 . ARG B 1 167 ? 59.532  99.957  71.000 1.000 133.798 0 167 ARG CCC NH2 1 ? 6  
ATOM 3010  N N   . PHE B 1 168 ? 59.640  100.686 64.661 1.000 102.788 0 168 PHE CCC N   1 ? 6  
ATOM 3011  C CA  . PHE B 1 168 ? 58.984  101.886 64.157 1.000 105.970 0 168 PHE CCC CA  1 ? 6  
ATOM 3012  C C   . PHE B 1 168 ? 58.595  101.721 62.691 1.000 109.058 0 168 PHE CCC C   1 ? 6  
ATOM 3013  O O   . PHE B 1 168 ? 57.432  101.909 62.320 1.000 116.398 0 168 PHE CCC O   1 ? 6  
ATOM 3014  C CB  . PHE B 1 168 ? 59.953  103.061 64.321 1.000 100.771 0 168 PHE CCC CB  1 ? 6  
ATOM 3015  C CG  . PHE B 1 168 ? 59.382  104.412 63.978 1.000 104.906 0 168 PHE CCC CG  1 ? 6  
ATOM 3016  C CD1 . PHE B 1 168 ? 58.451  105.026 64.797 1.000 110.432 0 168 PHE CCC CD1 1 ? 6  
ATOM 3017  C CD2 . PHE B 1 168 ? 59.772  105.061 62.818 1.000 110.717 0 168 PHE CCC CD2 1 ? 6  
ATOM 3018  C CE1 . PHE B 1 168 ? 57.947  106.279 64.481 1.000 114.396 0 168 PHE CCC CE1 1 ? 6  
ATOM 3019  C CE2 . PHE B 1 168 ? 59.257  106.305 62.490 1.000 115.085 0 168 PHE CCC CE2 1 ? 6  
ATOM 3020  C CZ  . PHE B 1 168 ? 58.339  106.912 63.324 1.000 113.808 0 168 PHE CCC CZ  1 ? 6  
ATOM 3021  N N   . TYR B 1 169 ? 59.553  101.351 61.840 1.000 105.317 0 169 TYR CCC N   1 ? 6  
ATOM 3022  C CA  . TYR B 1 169 ? 59.269  101.236 60.415 1.000 107.059 0 169 TYR CCC CA  1 ? 6  
ATOM 3023  C C   . TYR B 1 169 ? 58.478  99.984  60.043 1.000 108.493 0 169 TYR CCC C   1 ? 6  
ATOM 3024  O O   . TYR B 1 169 ? 57.811  99.985  59.002 1.000 107.041 0 169 TYR CCC O   1 ? 6  
ATOM 3025  C CB  . TYR B 1 169 ? 60.578  101.284 59.634 1.000 107.979 0 169 TYR CCC CB  1 ? 6  
ATOM 3026  C CG  . TYR B 1 169 ? 61.138  102.683 59.555 1.000 102.864 0 169 TYR CCC CG  1 ? 6  
ATOM 3027  C CD1 . TYR B 1 169 ? 60.592  103.626 58.694 1.000 108.233 0 169 TYR CCC CD1 1 ? 6  
ATOM 3028  C CD2 . TYR B 1 169 ? 62.191  103.070 60.367 1.000 101.828 0 169 TYR CCC CD2 1 ? 6  
ATOM 3029  C CE1 . TYR B 1 169 ? 61.097  104.907 58.628 1.000 108.423 0 169 TYR CCC CE1 1 ? 6  
ATOM 3030  C CE2 . TYR B 1 169 ? 62.701  104.349 60.311 1.000 103.301 0 169 TYR CCC CE2 1 ? 6  
ATOM 3031  C CZ  . TYR B 1 169 ? 62.152  105.263 59.441 1.000 106.117 0 169 TYR CCC CZ  1 ? 6  
ATOM 3032  O OH  . TYR B 1 169 ? 62.659  106.540 59.386 1.000 113.204 0 169 TYR CCC OH  1 ? 6  
ATOM 3033  N N   . LYS B 1 170 ? 58.536  98.922  60.854 1.000 106.079 0 170 LYS CCC N   1 ? 6  
ATOM 3034  C CA  . LYS B 1 170 ? 57.650  97.774  60.654 1.000 108.046 0 170 LYS CCC CA  1 ? 6  
ATOM 3035  C C   . LYS B 1 170 ? 56.192  98.183  60.818 1.000 116.366 0 170 LYS CCC C   1 ? 6  
ATOM 3036  O O   . LYS B 1 170 ? 55.333  97.827  60.002 1.000 120.202 0 170 LYS CCC O   1 ? 6  
ATOM 3037  C CB  . LYS B 1 170 ? 58.004  96.616  61.587 1.000 107.858 0 170 LYS CCC CB  1 ? 6  
ATOM 3038  C CG  . LYS B 1 170 ? 57.180  95.371  61.246 1.000 110.261 0 170 LYS CCC CG  1 ? 6  
ATOM 3039  C CD  . LYS B 1 170 ? 57.667  94.084  61.873 1.000 114.706 0 170 LYS CCC CD  1 ? 6  
ATOM 3040  C CE  . LYS B 1 170 ? 56.959  92.891  61.256 1.000 116.668 0 170 LYS CCC CE  1 ? 6  
ATOM 3041  N NZ  . LYS B 1 170 ? 57.223  91.608  61.957 1.000 132.001 0 170 LYS CCC NZ  1 ? 6  
ATOM 3042  N N   . THR B 1 171 ? 55.895  98.924  61.885 1.000 113.828 0 171 THR CCC N   1 ? 6  
ATOM 3043  C CA  . THR B 1 171 ? 54.541  99.421  62.093 1.000 116.830 0 171 THR CCC CA  1 ? 6  
ATOM 3044  C C   . THR B 1 171 ? 54.122  100.325 60.939 1.000 120.702 0 171 THR CCC C   1 ? 6  
ATOM 3045  O O   . THR B 1 171 ? 52.999  100.211 60.432 1.000 132.300 0 171 THR CCC O   1 ? 6  
ATOM 3046  C CB  . THR B 1 171 ? 54.458  100.145 63.433 1.000 116.721 0 171 THR CCC CB  1 ? 6  
ATOM 3047  O OG1 . THR B 1 171 ? 54.813  99.233  64.479 1.000 114.825 0 171 THR CCC OG1 1 ? 6  
ATOM 3048  C CG2 . THR B 1 171 ? 53.050  100.638 63.673 1.000 129.880 0 171 THR CCC CG2 1 ? 6  
ATOM 3049  N N   . LEU B 1 172 ? 55.013  101.217 60.499 1.000 116.307 0 172 LEU CCC N   1 ? 6  
ATOM 3050  C CA  . LEU B 1 172 ? 54.694  102.098 59.378 1.000 122.023 0 172 LEU CCC CA  1 ? 6  
ATOM 3051  C C   . LEU B 1 172 ? 54.334  101.285 58.138 1.000 128.677 0 172 LEU CCC C   1 ? 6  
ATOM 3052  O O   . LEU B 1 172 ? 53.414  101.646 57.395 1.000 143.144 0 172 LEU CCC O   1 ? 6  
ATOM 3053  C CB  . LEU B 1 172 ? 55.883  103.017 59.077 1.000 125.941 0 172 LEU CCC CB  1 ? 6  
ATOM 3054  C CG  . LEU B 1 172 ? 55.871  104.497 59.454 1.000 138.428 0 172 LEU CCC CG  1 ? 6  
ATOM 3055  C CD1 . LEU B 1 172 ? 57.186  105.130 59.055 1.000 143.590 0 172 LEU CCC CD1 1 ? 6  
ATOM 3056  C CD2 . LEU B 1 172 ? 54.731  105.195 58.731 1.000 151.551 0 172 LEU CCC CD2 1 ? 6  
ATOM 3057  N N   . ARG B 1 173 ? 55.049  100.179 57.908 1.000 123.904 0 173 ARG CCC N   1 ? 6  
ATOM 3058  C CA  . ARG B 1 173 ? 54.778  99.328  56.751 1.000 117.772 0 173 ARG CCC CA  1 ? 6  
ATOM 3059  C C   . ARG B 1 173 ? 53.370  98.745  56.796 1.000 120.815 0 173 ARG CCC C   1 ? 6  
ATOM 3060  O O   . ARG B 1 173 ? 52.684  98.703  55.769 1.000 129.200 0 173 ARG CCC O   1 ? 6  
ATOM 3061  C CB  . ARG B 1 173 ? 55.825  98.227  56.660 1.000 110.060 0 173 ARG CCC CB  1 ? 6  
ATOM 3062  C CG  . ARG B 1 173 ? 55.754  97.448  55.375 1.000 104.652 0 173 ARG CCC CG  1 ? 6  
ATOM 3063  C CD  . ARG B 1 173 ? 56.758  96.326  55.381 1.000 104.865 0 173 ARG CCC CD  1 ? 6  
ATOM 3064  N NE  . ARG B 1 173 ? 56.904  95.743  54.056 1.000 108.364 0 173 ARG CCC NE  1 ? 6  
ATOM 3065  C CZ  . ARG B 1 173 ? 57.642  94.676  53.788 1.000 110.471 0 173 ARG CCC CZ  1 ? 6  
ATOM 3066  N NH1 . ARG B 1 173 ? 58.315  94.047  54.737 1.000 109.061 0 173 ARG CCC NH1 1 ? 6  
ATOM 3067  N NH2 . ARG B 1 173 ? 57.704  94.228  52.537 1.000 113.286 0 173 ARG CCC NH2 1 ? 6  
ATOM 3068  N N   . ALA B 1 174 ? 52.923  98.271  57.964 1.000 118.168 0 174 ALA CCC N   1 ? 6  
ATOM 3069  C CA  . ALA B 1 174 ? 51.580  97.701  58.028 1.000 125.708 0 174 ALA CCC CA  1 ? 6  
ATOM 3070  C C   . ALA B 1 174 ? 50.557  98.809  57.815 1.000 137.931 0 174 ALA CCC C   1 ? 6  
ATOM 3071  O O   . ALA B 1 174 ? 49.536  98.609  57.147 1.000 148.012 0 174 ALA CCC O   1 ? 6  
ATOM 3072  C CB  . ALA B 1 174 ? 51.356  97.004  59.368 1.000 116.577 0 174 ALA CCC CB  1 ? 6  
ATOM 3073  N N   . GLU B 1 175 ? 50.839  99.989  58.371 1.000 139.107 0 175 GLU CCC N   1 ? 6  
ATOM 3074  C CA  . GLU B 1 175 ? 49.996  101.178 58.302 1.000 147.205 0 175 GLU CCC CA  1 ? 6  
ATOM 3075  C C   . GLU B 1 175 ? 50.034  101.746 56.893 1.000 149.811 0 175 GLU CCC C   1 ? 6  
ATOM 3076  O O   . GLU B 1 175 ? 49.110  102.462 56.474 1.000 159.058 0 175 GLU CCC O   1 ? 6  
ATOM 3077  C CB  . GLU B 1 175 ? 50.457  102.226 59.318 1.000 153.412 0 175 GLU CCC CB  1 ? 6  
ATOM 3078  C CG  . GLU B 1 175 ? 50.330  101.794 60.779 1.000 151.220 0 175 GLU CCC CG  1 ? 6  
ATOM 3079  C CD  . GLU B 1 175 ? 48.914  101.982 61.320 1.000 163.713 0 175 GLU CCC CD  1 ? 6  
ATOM 3080  O OE1 . GLU B 1 175 ? 48.232  102.954 60.922 1.000 177.802 0 175 GLU CCC OE1 1 ? 6  
ATOM 3081  O OE2 . GLU B 1 175 ? 48.482  101.162 62.159 1.000 163.539 0 175 GLU CCC OE2 1 ? 6  
ATOM 3082  N N   . GLN B 1 176 ? 51.098  101.401 56.173 1.000 150.977 0 176 GLN CCC N   1 ? 6  
ATOM 3083  C CA  . GLN B 1 176 ? 51.300  101.693 54.769 1.000 168.682 0 176 GLN CCC CA  1 ? 6  
ATOM 3084  C C   . GLN B 1 176 ? 51.191  103.167 54.427 1.000 195.582 0 176 GLN CCC C   1 ? 6  
ATOM 3085  O O   . GLN B 1 176 ? 52.227  103.741 54.079 1.000 199.790 0 176 GLN CCC O   1 ? 6  
ATOM 3086  C CB  . GLN B 1 176 ? 50.285  100.924 53.924 1.000 166.600 0 176 GLN CCC CB  1 ? 6  
ATOM 3087  C CG  . GLN B 1 176 ? 50.331  99.421  54.000 1.000 152.974 0 176 GLN CCC CG  1 ? 6  
ATOM 3088  C CD  . GLN B 1 176 ? 49.039  98.754  53.525 1.000 151.636 0 176 GLN CCC CD  1 ? 6  
ATOM 3089  O OE1 . GLN B 1 176 ? 48.013  99.405  53.291 1.000 162.864 0 176 GLN CCC OE1 1 ? 6  
ATOM 3090  N NE2 . GLN B 1 176 ? 49.068  97.435  53.455 1.000 149.935 0 176 GLN CCC NE2 1 ? 6  
ATOM 3091  N N   . ALA B 1 177 ? 50.021  103.802 54.547 1.000 234.767 0 177 ALA CCC N   1 ? 6  
ATOM 3092  C CA  . ALA B 1 177 ? 49.966  105.259 54.400 1.000 246.059 0 177 ALA CCC CA  1 ? 6  
ATOM 3093  C C   . ALA B 1 177 ? 50.589  105.699 53.082 1.000 259.431 0 177 ALA CCC C   1 ? 6  
ATOM 3094  O O   . ALA B 1 177 ? 50.161  105.284 52.000 1.000 285.453 0 177 ALA CCC O   1 ? 6  
ATOM 3095  C CB  . ALA B 1 177 ? 50.701  105.971 55.539 1.000 239.138 0 177 ALA CCC CB  1 ? 6  
ATOM 3096  N N   . SER B 1 178 ? 51.629  106.522 53.165 1.000 222.581 0 178 SER CCC N   1 ? 6  
ATOM 3097  C CA  . SER B 1 178 ? 52.303  106.999 51.969 1.000 214.677 0 178 SER CCC CA  1 ? 6  
ATOM 3098  C C   . SER B 1 178 ? 53.764  107.274 52.292 1.000 213.224 0 178 SER CCC C   1 ? 6  
ATOM 3099  O O   . SER B 1 178 ? 54.214  107.119 53.430 1.000 217.072 0 178 SER CCC O   1 ? 6  
ATOM 3100  C CB  . SER B 1 178 ? 51.602  108.238 51.404 1.000 204.413 0 178 SER CCC CB  1 ? 6  
ATOM 3101  O OG  . SER B 1 178 ? 52.194  109.430 51.885 1.000 193.856 0 178 SER CCC OG  1 ? 6  
ATOM 3102  N N   . GLN B 1 179 ? 54.496  107.718 51.269 1.000 212.243 0 179 GLN CCC N   1 ? 6  
ATOM 3103  C CA  . GLN B 1 179 ? 55.887  108.111 51.460 1.000 217.889 0 179 GLN CCC CA  1 ? 6  
ATOM 3104  C C   . GLN B 1 179 ? 56.001  109.481 52.109 1.000 220.081 0 179 GLN CCC C   1 ? 6  
ATOM 3105  O O   . GLN B 1 179 ? 56.907  109.707 52.915 1.000 226.253 0 179 GLN CCC O   1 ? 6  
ATOM 3106  C CB  . GLN B 1 179 ? 56.638  108.095 50.129 1.000 225.883 0 179 GLN CCC CB  1 ? 6  
ATOM 3107  C CG  . GLN B 1 179 ? 57.156  106.723 49.717 1.000 228.668 0 179 GLN CCC CG  1 ? 6  
ATOM 3108  C CD  . GLN B 1 179 ? 58.117  106.127 50.737 1.000 226.527 0 179 GLN CCC CD  1 ? 6  
ATOM 3109  O OE1 . GLN B 1 179 ? 58.953  106.825 51.316 1.000 224.532 0 179 GLN CCC OE1 1 ? 6  
ATOM 3110  N NE2 . GLN B 1 179 ? 57.989  104.826 50.968 1.000 227.496 0 179 GLN CCC NE2 1 ? 6  
ATOM 3111  N N   . GLU B 1 180 ? 55.114  110.409 51.745 1.000 212.554 0 180 GLU CCC N   1 ? 6  
ATOM 3112  C CA  . GLU B 1 180 ? 55.053  111.701 52.422 1.000 211.108 0 180 GLU CCC CA  1 ? 6  
ATOM 3113  C C   . GLU B 1 180 ? 54.777  111.511 53.908 1.000 206.681 0 180 GLU CCC C   1 ? 6  
ATOM 3114  O O   . GLU B 1 180 ? 55.415  112.139 54.762 1.000 220.173 0 180 GLU CCC O   1 ? 6  
ATOM 3115  C CB  . GLU B 1 180 ? 54.005  112.595 51.758 1.000 207.931 0 180 GLU CCC CB  1 ? 6  
ATOM 3116  C CG  . GLU B 1 180 ? 54.524  113.281 50.499 1.000 206.557 0 180 GLU CCC CG  1 ? 6  
ATOM 3117  C CD  . GLU B 1 180 ? 53.517  114.228 49.879 1.000 211.336 0 180 GLU CCC CD  1 ? 6  
ATOM 3118  O OE1 . GLU B 1 180 ? 52.337  114.224 50.294 1.000 207.739 0 180 GLU CCC OE1 1 ? 6  
ATOM 3119  O OE2 . GLU B 1 180 ? 53.910  115.014 48.989 1.000 223.554 0 180 GLU CCC OE2 1 ? 6  
ATOM 3120  N N   . VAL B 1 181 ? 53.800  110.665 54.232 1.000 211.055 0 181 VAL CCC N   1 ? 6  
ATOM 3121  C CA  . VAL B 1 181 ? 53.481  110.373 55.626 1.000 197.968 0 181 VAL CCC CA  1 ? 6  
ATOM 3122  C C   . VAL B 1 181 ? 54.660  109.694 56.322 1.000 193.076 0 181 VAL CCC C   1 ? 6  
ATOM 3123  O O   . VAL B 1 181 ? 55.014  110.054 57.451 1.000 187.410 0 181 VAL CCC O   1 ? 6  
ATOM 3124  C CB  . VAL B 1 181 ? 52.203  109.517 55.706 1.000 195.026 0 181 VAL CCC CB  1 ? 6  
ATOM 3125  C CG1 . VAL B 1 181 ? 51.988  109.009 57.121 1.000 186.906 0 181 VAL CCC CG1 1 ? 6  
ATOM 3126  C CG2 . VAL B 1 181 ? 50.999  110.316 55.229 1.000 177.114 0 181 VAL CCC CG2 1 ? 6  
ATOM 3127  N N   . LYS B 1 182 ? 55.288  108.708 55.665 1.000 176.648 0 182 LYS CCC N   1 ? 6  
ATOM 3128  C CA  . LYS B 1 182 ? 56.455  108.045 56.255 1.000 177.822 0 182 LYS CCC CA  1 ? 6  
ATOM 3129  C C   . LYS B 1 182 ? 57.621  108.993 56.512 1.000 184.146 0 182 LYS CCC C   1 ? 6  
ATOM 3130  O O   . LYS B 1 182 ? 58.418  108.746 57.425 1.000 185.499 0 182 LYS CCC O   1 ? 6  
ATOM 3131  C CB  . LYS B 1 182 ? 56.944  106.906 55.358 1.000 172.319 0 182 LYS CCC CB  1 ? 6  
ATOM 3132  C CG  . LYS B 1 182 ? 56.058  105.686 55.300 1.000 165.010 0 182 LYS CCC CG  1 ? 6  
ATOM 3133  C CD  . LYS B 1 182 ? 56.661  104.656 54.362 1.000 167.499 0 182 LYS CCC CD  1 ? 6  
ATOM 3134  C CE  . LYS B 1 182 ? 55.825  103.393 54.304 1.000 163.764 0 182 LYS CCC CE  1 ? 6  
ATOM 3135  N NZ  . LYS B 1 182 ? 56.455  102.366 53.428 1.000 154.304 0 182 LYS CCC NZ  1 ? 6  
ATOM 3136  N N   . ASN B 1 183 ? 57.714  110.107 55.786 1.000 190.376 0 183 ASN CCC N   1 ? 6  
ATOM 3137  C CA  . ASN B 1 183 ? 58.862  110.983 55.998 1.000 190.919 0 183 ASN CCC CA  1 ? 6  
ATOM 3138  C C   . ASN B 1 183 ? 58.502  112.111 56.949 1.000 188.307 0 183 ASN CCC C   1 ? 6  
ATOM 3139  O O   . ASN B 1 183 ? 59.366  112.598 57.685 1.000 185.894 0 183 ASN CCC O   1 ? 6  
ATOM 3140  C CB  . ASN B 1 183 ? 59.412  111.537 54.673 1.000 197.561 0 183 ASN CCC CB  1 ? 6  
ATOM 3141  C CG  . ASN B 1 183 ? 58.424  112.417 53.925 1.000 215.211 0 183 ASN CCC CG  1 ? 6  
ATOM 3142  O OD1 . ASN B 1 183 ? 57.863  113.367 54.474 1.000 232.513 0 183 ASN CCC OD1 1 ? 6  
ATOM 3143  N ND2 . ASN B 1 183 ? 58.241  112.126 52.644 1.000 223.092 0 183 ASN CCC ND2 1 ? 6  
ATOM 3144  N N   . ALA B 1 184 ? 57.250  112.560 56.918 1.000 195.005 0 184 ALA CCC N   1 ? 6  
ATOM 3145  C CA  . ALA B 1 184 ? 56.774  113.486 57.936 1.000 185.703 0 184 ALA CCC CA  1 ? 6  
ATOM 3146  C C   . ALA B 1 184 ? 56.779  112.828 59.312 1.000 175.664 0 184 ALA CCC C   1 ? 6  
ATOM 3147  O O   . ALA B 1 184 ? 57.209  113.433 60.301 1.000 172.009 0 184 ALA CCC O   1 ? 6  
ATOM 3148  C CB  . ALA B 1 184 ? 55.375  113.983 57.583 1.000 183.864 0 184 ALA CCC CB  1 ? 6  
ATOM 3149  N N   . ALA B 1 185 ? 56.295  111.582 59.392 1.000 166.040 0 185 ALA CCC N   1 ? 6  
ATOM 3150  C CA  . ALA B 1 185 ? 56.212  110.881 60.674 1.000 164.006 0 185 ALA CCC CA  1 ? 6  
ATOM 3151  C C   . ALA B 1 185 ? 57.584  110.643 61.293 1.000 157.996 0 185 ALA CCC C   1 ? 6  
ATOM 3152  O O   . ALA B 1 185 ? 57.736  110.713 62.518 1.000 158.466 0 185 ALA CCC O   1 ? 6  
ATOM 3153  C CB  . ALA B 1 185 ? 55.484  109.552 60.500 1.000 157.511 0 185 ALA CCC CB  1 ? 6  
ATOM 3154  N N   . THR B 1 186 ? 58.588  110.332 60.476 1.000 158.107 0 186 THR CCC N   1 ? 6  
ATOM 3155  C CA  . THR B 1 186 ? 59.919  110.094 61.026 1.000 159.690 0 186 THR CCC CA  1 ? 6  
ATOM 3156  C C   . THR B 1 186 ? 60.488  111.377 61.633 1.000 167.781 0 186 THR CCC C   1 ? 6  
ATOM 3157  O O   . THR B 1 186 ? 60.939  111.387 62.785 1.000 155.862 0 186 THR CCC O   1 ? 6  
ATOM 3158  C CB  . THR B 1 186 ? 60.853  109.469 59.982 1.000 161.401 0 186 THR CCC CB  1 ? 6  
ATOM 3159  O OG1 . THR B 1 186 ? 62.122  109.193 60.587 1.000 173.080 0 186 THR CCC OG1 1 ? 6  
ATOM 3160  C CG2 . THR B 1 186 ? 61.057  110.349 58.770 1.000 169.145 0 186 THR CCC CG2 1 ? 6  
ATOM 3161  N N   . GLU B 1 187 ? 60.469  112.475 60.868 1.000 183.371 0 187 GLU CCC N   1 ? 6  
ATOM 3162  C CA  . GLU B 1 187 ? 60.892  113.795 61.331 1.000 182.374 0 187 GLU CCC CA  1 ? 6  
ATOM 3163  C C   . GLU B 1 187 ? 60.211  114.232 62.626 1.000 176.191 0 187 GLU CCC C   1 ? 6  
ATOM 3164  O O   . GLU B 1 187 ? 60.549  115.275 63.192 1.000 178.139 0 187 GLU CCC O   1 ? 6  
ATOM 3165  C CB  . GLU B 1 187 ? 60.550  114.815 60.239 1.000 186.897 0 187 GLU CCC CB  1 ? 6  
ATOM 3166  C CG  . GLU B 1 187 ? 61.175  116.191 60.340 1.000 192.717 0 187 GLU CCC CG  1 ? 6  
ATOM 3167  C CD  . GLU B 1 187 ? 61.257  116.871 58.985 1.000 198.262 0 187 GLU CCC CD  1 ? 6  
ATOM 3168  O OE1 . GLU B 1 187 ? 60.949  116.211 57.969 1.000 198.588 0 187 GLU CCC OE1 1 ? 6  
ATOM 3169  O OE2 . GLU B 1 187 ? 61.602  118.070 58.938 1.000 200.731 0 187 GLU CCC OE2 1 ? 6  
ATOM 3170  N N   . THR B 1 188 ? 59.259  113.443 63.113 1.000 170.113 0 188 THR CCC N   1 ? 6  
ATOM 3171  C CA  . THR B 1 188 ? 58.459  113.838 64.264 1.000 166.234 0 188 THR CCC CA  1 ? 6  
ATOM 3172  C C   . THR B 1 188 ? 58.583  112.839 65.406 1.000 165.123 0 188 THR CCC C   1 ? 6  
ATOM 3173  O O   . THR B 1 188 ? 59.355  113.032 66.347 1.000 171.857 0 188 THR CCC O   1 ? 6  
ATOM 3174  C CB  . THR B 1 188 ? 56.990  114.028 63.884 1.000 166.261 0 188 THR CCC CB  1 ? 6  
ATOM 3175  O OG1 . THR B 1 188 ? 56.530  112.900 63.133 1.000 178.962 0 188 THR CCC OG1 1 ? 6  
ATOM 3176  C CG2 . THR B 1 188 ? 56.812  115.302 63.069 1.000 166.468 0 188 THR CCC CG2 1 ? 6  
ATOM 3177  N N   . LEU B 1 189 ? 57.849  111.734 65.274 1.000 157.316 0 189 LEU CCC N   1 ? 6  
ATOM 3178  C CA  . LEU B 1 189 ? 57.657  110.766 66.348 1.000 154.006 0 189 LEU CCC CA  1 ? 6  
ATOM 3179  C C   . LEU B 1 189 ? 58.907  109.960 66.676 1.000 152.262 0 189 LEU CCC C   1 ? 6  
ATOM 3180  O O   . LEU B 1 189 ? 59.091  109.577 67.836 1.000 155.839 0 189 LEU CCC O   1 ? 6  
ATOM 3181  C CB  . LEU B 1 189 ? 56.516  109.815 65.986 1.000 149.132 0 189 LEU CCC CB  1 ? 6  
ATOM 3182  C CG  . LEU B 1 189 ? 55.188  110.493 65.644 1.000 152.471 0 189 LEU CCC CG  1 ? 6  
ATOM 3183  C CD1 . LEU B 1 189 ? 54.192  109.511 65.033 1.000 150.048 0 189 LEU CCC CD1 1 ? 6  
ATOM 3184  C CD2 . LEU B 1 189 ? 54.614  111.161 66.880 1.000 152.220 0 189 LEU CCC CD2 1 ? 6  
ATOM 3185  N N   . LEU B 1 190 ? 59.760  109.665 65.694 1.000 146.524 0 190 LEU CCC N   1 ? 6  
ATOM 3186  C CA  . LEU B 1 190 ? 60.951  108.879 66.005 1.000 141.473 0 190 LEU CCC CA  1 ? 6  
ATOM 3187  C C   . LEU B 1 190 ? 61.834  109.543 67.058 1.000 141.348 0 190 LEU CCC C   1 ? 6  
ATOM 3188  O O   . LEU B 1 190 ? 62.375  108.856 67.933 1.000 144.404 0 190 LEU CCC O   1 ? 6  
ATOM 3189  C CB  . LEU B 1 190 ? 61.758  108.629 64.727 1.000 137.136 0 190 LEU CCC CB  1 ? 6  
ATOM 3190  C CG  . LEU B 1 190 ? 62.930  107.641 64.793 1.000 125.916 0 190 LEU CCC CG  1 ? 6  
ATOM 3191  C CD1 . LEU B 1 190 ? 62.451  106.207 64.947 1.000 126.340 0 190 LEU CCC CD1 1 ? 6  
ATOM 3192  C CD2 . LEU B 1 190 ? 63.818  107.777 63.563 1.000 117.283 0 190 LEU CCC CD2 1 ? 6  
ATOM 3193  N N   . VAL B 1 191 ? 62.004  110.863 67.007 1.000 141.913 0 191 VAL CCC N   1 ? 6  
ATOM 3194  C CA  . VAL B 1 191 ? 62.819  111.499 68.040 1.000 145.729 0 191 VAL CCC CA  1 ? 6  
ATOM 3195  C C   . VAL B 1 191 ? 62.069  111.613 69.369 1.000 152.747 0 191 VAL CCC C   1 ? 6  
ATOM 3196  O O   . VAL B 1 191 ? 62.613  111.287 70.430 1.000 151.914 0 191 VAL CCC O   1 ? 6  
ATOM 3197  C CB  . VAL B 1 191 ? 63.320  112.868 67.550 1.000 148.066 0 191 VAL CCC CB  1 ? 6  
ATOM 3198  C CG1 . VAL B 1 191 ? 64.151  113.531 68.632 1.000 148.711 0 191 VAL CCC CG1 1 ? 6  
ATOM 3199  C CG2 . VAL B 1 191 ? 64.124  112.697 66.273 1.000 141.651 0 191 VAL CCC CG2 1 ? 6  
ATOM 3200  N N   . GLN B 1 192 ? 60.817  112.087 69.338 1.000 159.289 0 192 GLN CCC N   1 ? 6  
ATOM 3201  C CA  . GLN B 1 192 ? 60.053  112.278 70.577 1.000 164.850 0 192 GLN CCC CA  1 ? 6  
ATOM 3202  C C   . GLN B 1 192 ? 59.793  110.977 71.335 1.000 156.022 0 192 GLN CCC C   1 ? 6  
ATOM 3203  O O   . GLN B 1 192 ? 59.792  110.967 72.573 1.000 160.300 0 192 GLN CCC O   1 ? 6  
ATOM 3204  C CB  . GLN B 1 192 ? 58.736  113.015 70.304 1.000 179.943 0 192 GLN CCC CB  1 ? 6  
ATOM 3205  C CG  . GLN B 1 192 ? 58.880  114.495 69.934 1.000 202.888 0 192 GLN CCC CG  1 ? 6  
ATOM 3206  C CD  . GLN B 1 192 ? 59.448  114.745 68.562 1.000 221.085 0 192 GLN CCC CD  1 ? 6  
ATOM 3207  O OE1 . GLN B 1 192 ? 60.663  114.852 68.391 1.000 229.398 0 192 GLN CCC OE1 1 ? 6  
ATOM 3208  N NE2 . GLN B 1 192 ? 58.572  114.877 67.573 1.000 231.367 0 192 GLN CCC NE2 1 ? 6  
ATOM 3209  N N   . ASN B 1 193 ? 59.588  109.877 70.622 1.000 146.791 0 193 ASN CCC N   1 ? 6  
ATOM 3210  C CA  . ASN B 1 193 ? 59.303  108.574 71.218 1.000 147.653 0 193 ASN CCC CA  1 ? 6  
ATOM 3211  C C   . ASN B 1 193 ? 60.561  107.779 71.544 1.000 146.989 0 193 ASN CCC C   1 ? 6  
ATOM 3212  O O   . ASN B 1 193 ? 60.457  106.646 72.029 1.000 145.322 0 193 ASN CCC O   1 ? 6  
ATOM 3213  C CB  . ASN B 1 193 ? 58.363  107.771 70.312 1.000 149.615 0 193 ASN CCC CB  1 ? 6  
ATOM 3214  C CG  . ASN B 1 193 ? 56.951  108.342 70.295 1.000 158.420 0 193 ASN CCC CG  1 ? 6  
ATOM 3215  O OD1 . ASN B 1 193 ? 56.704  109.429 70.823 1.000 160.321 0 193 ASN CCC OD1 1 ? 6  
ATOM 3216  N ND2 . ASN B 1 193 ? 56.017  107.607 69.697 1.000 167.417 0 193 ASN CCC ND2 1 ? 6  
ATOM 3217  N N   . ALA B 1 194 ? 61.734  108.345 71.277 1.000 147.857 0 194 ALA CCC N   1 ? 6  
ATOM 3218  C CA  . ALA B 1 194 ? 63.015  107.755 71.628 1.000 143.022 0 194 ALA CCC CA  1 ? 6  
ATOM 3219  C C   . ALA B 1 194 ? 63.201  107.784 73.146 1.000 145.217 0 194 ALA CCC C   1 ? 6  
ATOM 3220  O O   . ALA B 1 194 ? 62.503  108.494 73.877 1.000 154.027 0 194 ALA CCC O   1 ? 6  
ATOM 3221  C CB  . ALA B 1 194 ? 64.158  108.487 70.923 1.000 142.541 0 194 ALA CCC CB  1 ? 6  
ATOM 3222  N N   . ASN B 1 195 ? 64.172  107.002 73.616 1.000 150.927 0 195 ASN CCC N   1 ? 6  
ATOM 3223  C CA  . ASN B 1 195 ? 64.437  106.898 75.036 1.000 154.235 0 195 ASN CCC CA  1 ? 6  
ATOM 3224  C C   . ASN B 1 195 ? 65.148  108.190 75.449 1.000 153.002 0 195 ASN CCC C   1 ? 6  
ATOM 3225  O O   . ASN B 1 195 ? 65.654  108.911 74.590 1.000 148.886 0 195 ASN CCC O   1 ? 6  
ATOM 3226  C CB  . ASN B 1 195 ? 65.355  105.681 75.232 1.000 155.365 0 195 ASN CCC CB  1 ? 6  
ATOM 3227  C CG  . ASN B 1 195 ? 65.311  105.077 76.618 1.000 168.666 0 195 ASN CCC CG  1 ? 6  
ATOM 3228  O OD1 . ASN B 1 195 ? 64.283  105.110 77.290 1.000 181.412 0 195 ASN CCC OD1 1 ? 6  
ATOM 3229  N ND2 . ASN B 1 195 ? 66.442  104.538 77.065 1.000 175.207 0 195 ASN CCC ND2 1 ? 6  
ATOM 3230  N N   . PRO B 1 196 ? 65.244  108.508 76.754 1.000 151.983 0 196 PRO CCC N   1 ? 6  
ATOM 3231  C CA  A PRO B 1 196 ? 65.802  109.824 77.093 1.000 146.869 0 196 PRO CCC CA  1 ? 6  
ATOM 3232  C C   . PRO B 1 196 ? 67.308  109.851 76.941 1.000 149.901 0 196 PRO CCC C   1 ? 6  
ATOM 3233  O O   . PRO B 1 196 ? 67.883  110.898 76.631 1.000 153.815 0 196 PRO CCC O   1 ? 6  
ATOM 3234  C CB  A PRO B 1 196 ? 65.370  110.048 78.549 1.000 146.764 0 196 PRO CCC CB  1 ? 6  
ATOM 3235  C CG  A PRO B 1 196 ? 64.395  108.987 78.856 1.000 151.099 0 196 PRO CCC CG  1 ? 6  
ATOM 3236  C CD  A PRO B 1 196 ? 64.677  107.861 77.947 1.000 152.731 0 196 PRO CCC CD  1 ? 6  
ATOM 3237  N N   . ASP B 1 197 ? 67.958  108.705 77.154 1.000 150.641 0 197 ASP CCC N   1 ? 6  
ATOM 3238  C CA  . ASP B 1 197 ? 69.399  108.634 76.939 1.000 150.957 0 197 ASP CCC CA  1 ? 6  
ATOM 3239  C C   . ASP B 1 197 ? 69.732  108.817 75.462 1.000 147.167 0 197 ASP CCC C   1 ? 6  
ATOM 3240  O O   . ASP B 1 197 ? 70.677  109.533 75.112 1.000 138.937 0 197 ASP CCC O   1 ? 6  
ATOM 3241  C CB  . ASP B 1 197 ? 69.931  107.297 77.456 1.000 149.735 0 197 ASP CCC CB  1 ? 6  
ATOM 3242  C CG  . ASP B 1 197 ? 69.974  107.234 78.972 1.000 154.137 0 197 ASP CCC CG  1 ? 6  
ATOM 3243  O OD1 . ASP B 1 197 ? 69.734  108.274 79.620 1.000 158.301 0 197 ASP CCC OD1 1 ? 6  
ATOM 3244  O OD2 . ASP B 1 197 ? 70.227  106.138 79.517 1.000 152.640 0 197 ASP CCC OD2 1 ? 6  
ATOM 3245  N N   . CYS B 1 198 ? 68.953  108.182 74.581 1.000 143.103 0 198 CYS CCC N   1 ? 6  
ATOM 3246  C CA  . CYS B 1 198 ? 69.123  108.382 73.145 1.000 131.299 0 198 CYS CCC CA  1 ? 6  
ATOM 3247  C C   . CYS B 1 198 ? 68.645  109.765 72.712 1.000 132.117 0 198 CYS CCC C   1 ? 6  
ATOM 3248  O O   . CYS B 1 198 ? 69.260  110.400 71.846 1.000 131.389 0 198 CYS CCC O   1 ? 6  
ATOM 3249  C CB  . CYS B 1 198 ? 68.366  107.299 72.381 1.000 126.323 0 198 CYS CCC CB  1 ? 6  
ATOM 3250  S SG  . CYS B 1 198 ? 69.299  105.801 72.093 1.000 123.072 0 198 CYS CCC SG  1 ? 6  
ATOM 3251  N N   . LYS B 1 199 ? 67.543  110.240 73.302 1.000 136.837 0 199 LYS CCC N   1 ? 6  
ATOM 3252  C CA  . LYS B 1 199 ? 66.965  111.527 72.915 1.000 141.834 0 199 LYS CCC CA  1 ? 6  
ATOM 3253  C C   . LYS B 1 199 ? 67.976  112.658 73.072 1.000 146.782 0 199 LYS CCC C   1 ? 6  
ATOM 3254  O O   . LYS B 1 199 ? 68.096  113.520 72.191 1.000 146.205 0 199 LYS CCC O   1 ? 6  
ATOM 3255  C CB  . LYS B 1 199 ? 65.702  111.774 73.745 1.000 144.547 0 199 LYS CCC CB  1 ? 6  
ATOM 3256  C CG  . LYS B 1 199 ? 64.824  112.944 73.359 1.000 157.510 0 199 LYS CCC CG  1 ? 6  
ATOM 3257  C CD  . LYS B 1 199 ? 63.726  113.078 74.401 1.000 158.930 0 199 LYS CCC CD  1 ? 6  
ATOM 3258  C CE  . LYS B 1 199 ? 62.766  111.897 74.286 1.000 143.746 0 199 LYS CCC CE  1 ? 6  
ATOM 3259  N NZ  . LYS B 1 199 ? 61.474  112.121 74.984 1.000 142.661 0 199 LYS CCC NZ  1 ? 6  
ATOM 3260  N N   . THR B 1 200 ? 68.701  112.679 74.194 1.000 149.393 0 200 THR CCC N   1 ? 6  
ATOM 3261  C CA  . THR B 1 200 ? 69.745  113.682 74.398 1.000 144.180 0 200 THR CCC CA  1 ? 6  
ATOM 3262  C C   . THR B 1 200 ? 70.795  113.618 73.293 1.000 146.745 0 200 THR CCC C   1 ? 6  
ATOM 3263  O O   . THR B 1 200 ? 71.255  114.655 72.799 1.000 144.827 0 200 THR CCC O   1 ? 6  
ATOM 3264  C CB  . THR B 1 200 ? 70.398  113.488 75.765 1.000 140.118 0 200 THR CCC CB  1 ? 6  
ATOM 3265  O OG1 . THR B 1 200 ? 70.974  112.178 75.832 1.000 132.655 0 200 THR CCC OG1 1 ? 6  
ATOM 3266  C CG2 . THR B 1 200 ? 69.379  113.665 76.887 1.000 148.561 0 200 THR CCC CG2 1 ? 6  
ATOM 3267  N N   . ILE B 1 201 ? 71.207  112.401 72.916 1.000 146.407 0 201 ILE CCC N   1 ? 6  
ATOM 3268  C CA  . ILE B 1 201 ? 72.182  112.232 71.841 1.000 136.892 0 201 ILE CCC CA  1 ? 6  
ATOM 3269  C C   . ILE B 1 201 ? 71.601  112.683 70.507 1.000 134.001 0 201 ILE CCC C   1 ? 6  
ATOM 3270  O O   . ILE B 1 201 ? 72.259  113.396 69.740 1.000 139.505 0 201 ILE CCC O   1 ? 6  
ATOM 3271  C CB  . ILE B 1 201 ? 72.656  110.765 71.774 1.000 128.209 0 201 ILE CCC CB  1 ? 6  
ATOM 3272  C CG1 . ILE B 1 201 ? 73.476  110.383 73.006 1.000 146.035 0 201 ILE CCC CG1 1 ? 6  
ATOM 3273  C CG2 . ILE B 1 201 ? 73.469  110.501 70.511 1.000 118.789 0 201 ILE CCC CG2 1 ? 6  
ATOM 3274  C CD1 . ILE B 1 201 ? 73.669  108.883 73.147 1.000 154.339 0 201 ILE CCC CD1 1 ? 6  
ATOM 3275  N N   . LEU B 1 202 ? 70.358  112.293 70.213 1.000 134.505 0 202 LEU CCC N   1 ? 6  
ATOM 3276  C CA  . LEU B 1 202 ? 69.777  112.667 68.929 1.000 135.431 0 202 LEU CCC CA  1 ? 6  
ATOM 3277  C C   . LEU B 1 202 ? 69.573  114.172 68.832 1.000 148.335 0 202 LEU CCC C   1 ? 6  
ATOM 3278  O O   . LEU B 1 202 ? 69.810  114.772 67.776 1.000 154.983 0 202 LEU CCC O   1 ? 6  
ATOM 3279  C CB  . LEU B 1 202 ? 68.440  111.954 68.747 1.000 134.583 0 202 LEU CCC CB  1 ? 6  
ATOM 3280  C CG  . LEU B 1 202 ? 68.495  110.434 68.655 1.000 129.542 0 202 LEU CCC CG  1 ? 6  
ATOM 3281  C CD1 . LEU B 1 202 ? 67.093  109.842 68.569 1.000 132.455 0 202 LEU CCC CD1 1 ? 6  
ATOM 3282  C CD2 . LEU B 1 202 ? 69.338  110.029 67.485 1.000 131.776 0 202 LEU CCC CD2 1 ? 6  
ATOM 3283  N N   . LYS B 1 203 ? 69.127  114.792 69.926 1.000 155.019 0 203 LYS CCC N   1 ? 6  
ATOM 3284  C CA  . LYS B 1 203 ? 68.981  116.242 69.963 1.000 157.747 0 203 LYS CCC CA  1 ? 6  
ATOM 3285  C C   . LYS B 1 203 ? 70.317  116.940 69.732 1.000 158.730 0 203 LYS CCC C   1 ? 6  
ATOM 3286  O O   . LYS B 1 203 ? 70.388  117.945 69.015 1.000 162.252 0 203 LYS CCC O   1 ? 6  
ATOM 3287  C CB  . LYS B 1 203 ? 68.347  116.660 71.290 1.000 167.668 0 203 LYS CCC CB  1 ? 6  
ATOM 3288  C CG  . LYS B 1 203 ? 66.845  116.370 71.341 1.000 171.818 0 203 LYS CCC CG  1 ? 6  
ATOM 3289  C CD  . LYS B 1 203 ? 66.231  116.642 72.707 1.000 189.094 0 203 LYS CCC CD  1 ? 6  
ATOM 3290  C CE  . LYS B 1 203 ? 64.711  116.555 72.640 1.000 204.823 0 203 LYS CCC CE  1 ? 6  
ATOM 3291  N NZ  . LYS B 1 203 ? 64.122  117.394 71.564 1.000 216.275 0 203 LYS CCC NZ  1 ? 6  
ATOM 3292  N N   . ALA B 1 204 ? 71.393  116.407 70.323 1.000 153.234 0 204 ALA CCC N   1 ? 6  
ATOM 3293  C CA  . ALA B 1 204 ? 72.712  117.011 70.175 1.000 150.509 0 204 ALA CCC CA  1 ? 6  
ATOM 3294  C C   . ALA B 1 204 ? 73.270  116.865 68.770 1.000 153.848 0 204 ALA CCC C   1 ? 6  
ATOM 3295  O O   . ALA B 1 204 ? 74.165  117.629 68.393 1.000 159.433 0 204 ALA CCC O   1 ? 6  
ATOM 3296  C CB  . ALA B 1 204 ? 73.690  116.390 71.173 1.000 145.085 0 204 ALA CCC CB  1 ? 6  
ATOM 3297  N N   . LEU B 1 205 ? 72.782  115.897 67.992 1.000 151.584 0 205 LEU CCC N   1 ? 6  
ATOM 3298  C CA  . LEU B 1 205 ? 73.281  115.743 66.631 1.000 150.723 0 205 LEU CCC CA  1 ? 6  
ATOM 3299  C C   . LEU B 1 205 ? 72.920  116.933 65.754 1.000 160.074 0 205 LEU CCC C   1 ? 6  
ATOM 3300  O O   . LEU B 1 205 ? 73.646  117.234 64.800 1.000 164.757 0 205 LEU CCC O   1 ? 6  
ATOM 3301  C CB  . LEU B 1 205 ? 72.769  114.447 66.007 1.000 145.180 0 205 LEU CCC CB  1 ? 6  
ATOM 3302  C CG  . LEU B 1 205 ? 73.399  113.179 66.578 1.000 141.145 0 205 LEU CCC CG  1 ? 6  
ATOM 3303  C CD1 . LEU B 1 205 ? 72.823  111.938 65.912 1.000 139.259 0 205 LEU CCC CD1 1 ? 6  
ATOM 3304  C CD2 . LEU B 1 205 ? 74.907  113.248 66.403 1.000 138.752 0 205 LEU CCC CD2 1 ? 6  
ATOM 3305  N N   . GLY B 1 206 ? 71.827  117.629 66.064 1.000 170.934 0 206 GLY CCC N   1 ? 6  
ATOM 3306  C CA  . GLY B 1 206 ? 71.426  118.784 65.299 1.000 173.362 0 206 GLY CCC CA  1 ? 6  
ATOM 3307  C C   . GLY B 1 206 ? 70.471  118.454 64.167 1.000 178.647 0 206 GLY CCC C   1 ? 6  
ATOM 3308  O O   . GLY B 1 206 ? 70.078  117.302 63.960 1.000 185.916 0 206 GLY CCC O   1 ? 6  
ATOM 3309  N N   . PRO B 1 207 ? 70.069  119.480 63.420 1.000 173.108 0 207 PRO CCC N   1 ? 6  
ATOM 3310  C CA  . PRO B 1 207 ? 69.129  119.278 62.312 1.000 168.833 0 207 PRO CCC CA  1 ? 6  
ATOM 3311  C C   . PRO B 1 207 ? 69.804  118.628 61.115 1.000 168.247 0 207 PRO CCC C   1 ? 6  
ATOM 3312  O O   . PRO B 1 207 ? 71.014  118.750 60.912 1.000 171.446 0 207 PRO CCC O   1 ? 6  
ATOM 3313  C CB  . PRO B 1 207 ? 68.671  120.700 61.977 1.000 174.383 0 207 PRO CCC CB  1 ? 6  
ATOM 3314  C CG  . PRO B 1 207 ? 69.836  121.559 62.368 1.000 171.839 0 207 PRO CCC CG  1 ? 6  
ATOM 3315  C CD  . PRO B 1 207 ? 70.511  120.881 63.532 1.000 173.881 0 207 PRO CCC CD  1 ? 6  
ATOM 3316  N N   . GLY B 1 208 ? 69.002  117.930 60.312 1.000 163.970 0 208 GLY CCC N   1 ? 6  
ATOM 3317  C CA  . GLY B 1 208 ? 69.509  117.322 59.098 1.000 166.539 0 208 GLY CCC CA  1 ? 6  
ATOM 3318  C C   . GLY B 1 208 ? 70.281  116.038 59.292 1.000 156.373 0 208 GLY CCC C   1 ? 6  
ATOM 3319  O O   . GLY B 1 208 ? 70.958  115.591 58.359 1.000 159.194 0 208 GLY CCC O   1 ? 6  
ATOM 3320  N N   . ALA B 1 209 ? 70.190  115.426 60.468 1.000 150.595 0 209 ALA CCC N   1 ? 6  
ATOM 3321  C CA  . ALA B 1 209 ? 70.862  114.160 60.704 1.000 149.148 0 209 ALA CCC CA  1 ? 6  
ATOM 3322  C C   . ALA B 1 209 ? 70.216  113.064 59.873 1.000 144.610 0 209 ALA CCC C   1 ? 6  
ATOM 3323  O O   . ALA B 1 209 ? 68.989  112.965 59.790 1.000 147.763 0 209 ALA CCC O   1 ? 6  
ATOM 3324  C CB  . ALA B 1 209 ? 70.799  113.797 62.186 1.000 153.228 0 209 ALA CCC CB  1 ? 6  
ATOM 3325  N N   . THR B 1 210 ? 71.051  112.236 59.251 1.000 138.728 0 210 THR CCC N   1 ? 6  
ATOM 3326  C CA  . THR B 1 210 ? 70.524  111.133 58.470 1.000 134.201 0 210 THR CCC CA  1 ? 6  
ATOM 3327  C C   . THR B 1 210 ? 70.088  110.021 59.408 1.000 131.663 0 210 THR CCC C   1 ? 6  
ATOM 3328  O O   . THR B 1 210 ? 70.494  109.965 60.572 1.000 136.726 0 210 THR CCC O   1 ? 6  
ATOM 3329  C CB  . THR B 1 210 ? 71.595  110.590 57.518 1.000 135.962 0 210 THR CCC CB  1 ? 6  
ATOM 3330  O OG1 . THR B 1 210 ? 72.377  111.673 57.003 1.000 144.543 0 210 THR CCC OG1 1 ? 6  
ATOM 3331  C CG2 . THR B 1 210 ? 70.983  109.820 56.354 1.000 143.302 0 210 THR CCC CG2 1 ? 6  
ATOM 3332  N N   . LEU B 1 211 ? 69.242  109.130 58.894 1.000 130.622 0 211 LEU CCC N   1 ? 6  
ATOM 3333  C CA  . LEU B 1 211 ? 68.843  107.983 59.695 1.000 120.874 0 211 LEU CCC CA  1 ? 6  
ATOM 3334  C C   . LEU B 1 211 ? 70.086  107.172 60.038 1.000 127.292 0 211 LEU CCC C   1 ? 6  
ATOM 3335  O O   . LEU B 1 211 ? 70.228  106.667 61.156 1.000 130.537 0 211 LEU CCC O   1 ? 6  
ATOM 3336  C CB  . LEU B 1 211 ? 67.776  107.166 58.955 1.000 125.239 0 211 LEU CCC CB  1 ? 6  
ATOM 3337  C CG  . LEU B 1 211 ? 67.063  105.920 59.504 1.000 117.425 0 211 LEU CCC CG  1 ? 6  
ATOM 3338  C CD1 . LEU B 1 211 ? 67.968  104.756 59.802 1.000 121.794 0 211 LEU CCC CD1 1 ? 6  
ATOM 3339  C CD2 . LEU B 1 211 ? 66.259  106.304 60.748 1.000 111.671 0 211 LEU CCC CD2 1 ? 6  
ATOM 3340  N N   . GLU B 1 212 ? 70.976  107.021 59.058 1.000 139.693 0 212 GLU CCC N   1 ? 6  
ATOM 3341  C CA  . GLU B 1 212 ? 72.244  106.329 59.244 1.000 145.454 0 212 GLU CCC CA  1 ? 6  
ATOM 3342  C C   . GLU B 1 212 ? 73.072  106.923 60.385 1.000 146.727 0 212 GLU CCC C   1 ? 6  
ATOM 3343  O O   . GLU B 1 212 ? 73.593  106.189 61.235 1.000 148.700 0 212 GLU CCC O   1 ? 6  
ATOM 3344  C CB  . GLU B 1 212 ? 73.030  106.406 57.933 1.000 153.850 0 212 GLU CCC CB  1 ? 6  
ATOM 3345  C CG  . GLU B 1 212 ? 72.371  105.679 56.762 1.000 167.192 0 212 GLU CCC CG  1 ? 6  
ATOM 3346  C CD  . GLU B 1 212 ? 73.227  105.674 55.499 1.000 182.083 0 212 GLU CCC CD  1 ? 6  
ATOM 3347  O OE1 . GLU B 1 212 ? 74.468  105.919 55.612 1.000 174.454 0 212 GLU CCC OE1 1 ? 6  
ATOM 3348  O OE2 . GLU B 1 212 ? 72.668  105.486 54.387 1.000 198.953 0 212 GLU CCC OE2 1 ? 6  
ATOM 3349  N N   . GLU B 1 213 ? 73.197  108.259 60.432 1.000 138.939 0 213 GLU CCC N   1 ? 6  
ATOM 3350  C CA  . GLU B 1 213 ? 73.987  108.899 61.485 1.000 127.044 0 213 GLU CCC CA  1 ? 6  
ATOM 3351  C C   . GLU B 1 213 ? 73.407  108.709 62.879 1.000 120.792 0 213 GLU CCC C   1 ? 6  
ATOM 3352  O O   . GLU B 1 213 ? 74.154  108.447 63.829 1.000 128.284 0 213 GLU CCC O   1 ? 6  
ATOM 3353  C CB  . GLU B 1 213 ? 74.149  110.397 61.220 1.000 128.248 0 213 GLU CCC CB  1 ? 6  
ATOM 3354  C CG  . GLU B 1 213 ? 75.077  110.773 60.085 1.000 138.981 0 213 GLU CCC CG  1 ? 6  
ATOM 3355  C CD  . GLU B 1 213 ? 74.939  112.233 59.705 1.000 147.811 0 213 GLU CCC CD  1 ? 6  
ATOM 3356  O OE1 . GLU B 1 213 ? 73.793  112.702 59.551 1.000 150.559 0 213 GLU CCC OE1 1 ? 6  
ATOM 3357  O OE2 . GLU B 1 213 ? 75.978  112.920 59.598 1.000 153.241 0 213 GLU CCC OE2 1 ? 6  
ATOM 3358  N N   . MET B 1 214 ? 72.088  108.821 63.026 1.000 116.523 0 214 MET CCC N   1 ? 6  
ATOM 3359  C CA  . MET B 1 214 ? 71.478  108.597 64.334 1.000 116.779 0 214 MET CCC CA  1 ? 6  
ATOM 3360  C C   . MET B 1 214 ? 71.684  107.168 64.830 1.000 115.419 0 214 MET CCC C   1 ? 6  
ATOM 3361  O O   . MET B 1 214 ? 71.978  106.963 66.012 1.000 130.453 0 214 MET CCC O   1 ? 6  
ATOM 3362  C CB  A MET B 1 214 ? 70.009  109.027 64.345 1.000 119.584 0 214 MET CCC CB  1 ? 6  
ATOM 3363  C CG  A MET B 1 214 ? 69.186  108.847 63.110 1.000 133.694 0 214 MET CCC CG  1 ? 6  
ATOM 3364  S SD  A MET B 1 214 ? 67.556  109.575 63.412 1.000 142.255 0 214 MET CCC SD  1 ? 6  
ATOM 3365  C CE  A MET B 1 214 ? 68.010  111.261 63.808 1.000 127.053 0 214 MET CCC CE  1 ? 6  
ATOM 3366  N N   . MET B 1 215 ? 71.523  106.167 63.964 1.000 103.739 0 215 MET CCC N   1 ? 6  
ATOM 3367  C CA  . MET B 1 215 ? 71.694  104.794 64.434 1.000 102.368 0 215 MET CCC CA  1 ? 6  
ATOM 3368  C C   . MET B 1 215 ? 73.138  104.516 64.853 1.000 105.474 0 215 MET CCC C   1 ? 6  
ATOM 3369  O O   . MET B 1 215 ? 73.367  103.773 65.812 1.000 113.073 0 215 MET CCC O   1 ? 6  
ATOM 3370  C CB  . MET B 1 215 ? 71.269  103.814 63.343 1.000 114.623 0 215 MET CCC CB  1 ? 6  
ATOM 3371  C CG  . MET B 1 215 ? 69.782  103.799 63.031 1.000 116.900 0 215 MET CCC CG  1 ? 6  
ATOM 3372  S SD  . MET B 1 215 ? 69.342  102.466 61.889 1.000 109.270 0 215 MET CCC SD  1 ? 6  
ATOM 3373  C CE  . MET B 1 215 ? 69.633  101.025 62.894 1.000 131.607 0 215 MET CCC CE  1 ? 6  
ATOM 3374  N N   . THR B 1 216 ? 74.124  105.066 64.131 1.000 110.749 0 216 THR CCC N   1 ? 6  
ATOM 3375  C CA  . THR B 1 216 ? 75.526  104.958 64.552 1.000 114.473 0 216 THR CCC CA  1 ? 6  
ATOM 3376  C C   . THR B 1 216 ? 75.775  105.669 65.886 1.000 112.730 0 216 THR CCC C   1 ? 6  
ATOM 3377  O O   . THR B 1 216 ? 76.407  105.118 66.796 1.000 116.153 0 216 THR CCC O   1 ? 6  
ATOM 3378  C CB  . THR B 1 216 ? 76.444  105.521 63.460 1.000 115.766 0 216 THR CCC CB  1 ? 6  
ATOM 3379  O OG1 . THR B 1 216 ? 76.220  104.818 62.231 1.000 123.914 0 216 THR CCC OG1 1 ? 6  
ATOM 3380  C CG2 . THR B 1 216 ? 77.906  105.381 63.857 1.000 118.331 0 216 THR CCC CG2 1 ? 6  
ATOM 3381  N N   . ALA B 1 217 ? 75.265  106.898 66.007 1.000 111.568 0 217 ALA CCC N   1 ? 6  
ATOM 3382  C CA  . ALA B 1 217 ? 75.423  107.748 67.191 1.000 109.570 0 217 ALA CCC CA  1 ? 6  
ATOM 3383  C C   . ALA B 1 217 ? 74.900  107.090 68.463 1.000 110.139 0 217 ALA CCC C   1 ? 6  
ATOM 3384  O O   . ALA B 1 217 ? 75.513  107.198 69.531 1.000 119.916 0 217 ALA CCC O   1 ? 6  
ATOM 3385  C CB  . ALA B 1 217 ? 74.720  109.087 66.973 1.000 104.603 0 217 ALA CCC CB  1 ? 6  
ATOM 3386  N N   . CYS B 1 218 ? 73.770  106.410 68.359 1.000 101.607 0 218 CYS CCC N   1 ? 6  
ATOM 3387  C CA  . CYS B 1 218 ? 73.028  105.768 69.432 1.000 102.846 0 218 CYS CCC CA  1 ? 6  
ATOM 3388  C C   . CYS B 1 218 ? 73.423  104.311 69.674 1.000 108.630 0 218 CYS CCC C   1 ? 6  
ATOM 3389  O O   . CYS B 1 218 ? 72.732  103.618 70.428 1.000 120.259 0 218 CYS CCC O   1 ? 6  
ATOM 3390  C CB  . CYS B 1 218 ? 71.533  105.873 69.149 1.000 107.860 0 218 CYS CCC CB  1 ? 6  
ATOM 3391  S SG  . CYS B 1 218 ? 70.913  107.555 69.355 1.000 116.008 0 218 CYS CCC SG  1 ? 6  
ATOM 3392  N N   . GLN B 1 219 ? 74.496  103.828 69.050 1.000 104.280 0 219 GLN CCC N   1 ? 6  
ATOM 3393  C CA  . GLN B 1 219 ? 74.942  102.464 69.308 1.000 116.939 0 219 GLN CCC CA  1 ? 6  
ATOM 3394  C C   . GLN B 1 219 ? 75.606  102.290 70.668 1.000 138.514 0 219 GLN CCC C   1 ? 6  
ATOM 3395  O O   . GLN B 1 219 ? 75.983  101.163 71.001 1.000 143.587 0 219 GLN CCC O   1 ? 6  
ATOM 3396  C CB  . GLN B 1 219 ? 76.018  102.070 68.296 1.000 117.902 0 219 GLN CCC CB  1 ? 6  
ATOM 3397  C CG  . GLN B 1 219 ? 75.655  101.948 66.852 1.000 134.214 0 219 GLN CCC CG  1 ? 6  
ATOM 3398  C CD  . GLN B 1 219 ? 76.913  101.825 66.012 1.000 133.375 0 219 GLN CCC CD  1 ? 6  
ATOM 3399  O OE1 . GLN B 1 219 ? 78.017  102.071 66.503 1.000 120.674 0 219 GLN CCC OE1 1 ? 6  
ATOM 3400  N NE2 . GLN B 1 219 ? 76.757  101.465 64.743 1.000 137.580 0 219 GLN CCC NE2 1 ? 6  
ATOM 3401  N N   . GLY B 1 220 ? 75.736  103.343 71.473 1.000 147.266 0 220 GLY CCC N   1 ? ?  
ATOM 3402  C CA  . GLY B 1 220 ? 76.364  103.221 72.776 1.000 166.522 0 220 GLY CCC CA  1 ? ?  
ATOM 3403  C C   . GLY B 1 220 ? 75.412  102.933 73.920 1.000 188.778 0 220 GLY CCC C   1 ? ?  
ATOM 3404  O O   . GLY B 1 220 ? 75.820  102.364 74.937 1.000 218.654 0 220 GLY CCC O   1 ? ?  
ATOM 3405  N N   . VAL B 1 221 ? 74.137  103.302 73.763 1.000 173.778 0 221 VAL CCC N   1 ? ?  
ATOM 3406  C CA  . VAL B 1 221 ? 73.193  103.239 74.879 1.000 175.888 0 221 VAL CCC CA  1 ? ?  
ATOM 3407  C C   . VAL B 1 221 ? 72.954  101.797 75.322 1.000 182.665 0 221 VAL CCC C   1 ? ?  
ATOM 3408  O O   . VAL B 1 221 ? 72.820  101.520 76.520 1.000 181.441 0 221 VAL CCC O   1 ? ?  
ATOM 3409  C CB  . VAL B 1 221 ? 71.879  103.951 74.506 1.000 169.870 0 221 VAL CCC CB  1 ? ?  
ATOM 3410  C CG1 . VAL B 1 221 ? 72.151  105.408 74.156 1.000 163.324 0 221 VAL CCC CG1 1 ? ?  
ATOM 3411  C CG2 . VAL B 1 221 ? 71.185  103.238 73.352 1.000 173.225 0 221 VAL CCC CG2 1 ? ?  
ATOM 3412  N N   . GLY B 1 222 ? 72.900  100.862 74.378 1.000 199.599 0 222 GLY CCC N   1 ? ?  
ATOM 3413  C CA  . GLY B 1 222 ? 72.717  99.455  74.694 1.000 202.625 0 222 GLY CCC CA  1 ? ?  
ATOM 3414  C C   . GLY B 1 222 ? 71.467  99.117  75.490 1.000 192.013 0 222 GLY CCC C   1 ? ?  
ATOM 3415  O O   . GLY B 1 222 ? 71.366  98.040  76.083 1.000 171.835 0 222 GLY CCC O   1 ? ?  
ATOM 3416  N N   . PRO C 1 1   ? 64.403  52.705  37.080 1.000 91.986  0 1   PRO AAA N   1 ? 1  
ATOM 3417  C CA  . PRO C 1 1   ? 63.159  52.300  36.418 1.000 84.327  0 1   PRO AAA CA  1 ? 1  
ATOM 3418  C C   . PRO C 1 1   ? 63.185  52.581  34.924 1.000 89.356  0 1   PRO AAA C   1 ? 1  
ATOM 3419  O O   . PRO C 1 1   ? 64.139  53.201  34.452 1.000 99.108  0 1   PRO AAA O   1 ? 1  
ATOM 3420  C CB  A PRO C 1 1   ? 62.097  53.178  37.094 1.000 96.661  0 1   PRO AAA CB  1 ? 1  
ATOM 3421  C CG  A PRO C 1 1   ? 62.865  54.240  37.856 1.000 100.594 0 1   PRO AAA CG  1 ? 1  
ATOM 3422  C CD  A PRO C 1 1   ? 64.157  53.601  38.220 1.000 99.796  0 1   PRO AAA CD  1 ? 1  
ATOM 3423  N N   . ILE C 1 2   ? 62.138  52.196  34.199 1.000 94.998  0 2   ILE AAA N   1 ? 1  
ATOM 3424  C CA  . ILE C 1 2   ? 62.027  52.500  32.777 1.000 84.687  0 2   ILE AAA CA  1 ? 1  
ATOM 3425  C C   . ILE C 1 2   ? 60.937  53.542  32.617 1.000 82.592  0 2   ILE AAA C   1 ? 1  
ATOM 3426  O O   . ILE C 1 2   ? 59.790  53.319  33.026 1.000 79.136  0 2   ILE AAA O   1 ? 1  
ATOM 3427  C CB  . ILE C 1 2   ? 61.702  51.250  31.944 1.000 78.249  0 2   ILE AAA CB  1 ? 1  
ATOM 3428  C CG1 . ILE C 1 2   ? 62.718  50.141  32.203 1.000 77.809  0 2   ILE AAA CG1 1 ? 1  
ATOM 3429  C CG2 . ILE C 1 2   ? 61.642  51.597  30.474 1.000 87.567  0 2   ILE AAA CG2 1 ? 1  
ATOM 3430  C CD1 . ILE C 1 2   ? 64.120  50.517  31.806 0.500 79.864  0 2   ILE AAA CD1 1 ? 1  
ATOM 3431  N N   . VAL C 1 3   ? 61.287  54.672  32.008 1.000 86.078  0 3   VAL AAA N   1 ? 1  
ATOM 3432  C CA  . VAL C 1 3   ? 60.355  55.771  31.825 1.000 93.316  0 3   VAL AAA CA  1 ? 1  
ATOM 3433  C C   . VAL C 1 3   ? 60.376  56.217  30.372 1.000 101.555 0 3   VAL AAA C   1 ? 1  
ATOM 3434  O O   . VAL C 1 3   ? 61.262  55.866  29.594 1.000 109.957 0 3   VAL AAA O   1 ? 1  
ATOM 3435  C CB  . VAL C 1 3   ? 60.672  56.970  32.741 1.000 97.065  0 3   VAL AAA CB  1 ? 1  
ATOM 3436  C CG1 . VAL C 1 3   ? 60.486  56.596  34.208 1.000 102.655 0 3   VAL AAA CG1 1 ? 1  
ATOM 3437  C CG2 . VAL C 1 3   ? 62.077  57.484  32.463 1.000 95.561  0 3   VAL AAA CG2 1 ? 1  
ATOM 3438  N N   . GLN C 1 4   ? 59.373  57.010  30.027 1.000 110.542 0 4   GLN AAA N   1 ? 1  
ATOM 3439  C CA  . GLN C 1 4   ? 59.277  57.663  28.733 1.000 122.277 0 4   GLN AAA CA  1 ? 1  
ATOM 3440  C C   . GLN C 1 4   ? 60.063  58.964  28.830 1.000 125.325 0 4   GLN AAA C   1 ? 1  
ATOM 3441  O O   . GLN C 1 4   ? 59.904  59.714  29.797 1.000 125.820 0 4   GLN AAA O   1 ? 1  
ATOM 3442  C CB  . GLN C 1 4   ? 57.832  57.915  28.309 1.000 131.815 0 4   GLN AAA CB  1 ? 1  
ATOM 3443  C CG  . GLN C 1 4   ? 57.754  58.437  26.883 1.000 145.579 0 4   GLN AAA CG  1 ? 1  
ATOM 3444  C CD  . GLN C 1 4   ? 56.383  58.289  26.269 1.000 149.996 0 4   GLN AAA CD  1 ? 1  
ATOM 3445  O OE1 . GLN C 1 4   ? 55.525  57.607  26.827 1.000 152.124 0 4   GLN AAA OE1 1 ? 1  
ATOM 3446  N NE2 . GLN C 1 4   ? 56.191  58.887  25.096 1.000 163.194 0 4   GLN AAA NE2 1 ? 1  
ATOM 3447  N N   . ASN C 1 5   ? 60.907  59.235  27.848 1.000 131.960 0 5   ASN AAA N   1 ? 1  
ATOM 3448  C CA  . ASN C 1 5   ? 61.641  60.487  27.858 1.000 141.167 0 5   ASN AAA CA  1 ? 1  
ATOM 3449  C C   . ASN C 1 5   ? 60.906  61.504  26.991 1.000 154.207 0 5   ASN AAA C   1 ? 1  
ATOM 3450  O O   . ASN C 1 5   ? 59.740  61.313  26.627 1.000 163.407 0 5   ASN AAA O   1 ? 1  
ATOM 3451  C CB  . ASN C 1 5   ? 63.082  60.238  27.403 1.000 140.306 0 5   ASN AAA CB  1 ? 1  
ATOM 3452  C CG  . ASN C 1 5   ? 63.189  59.963  25.912 1.000 138.671 0 5   ASN AAA CG  1 ? 1  
ATOM 3453  O OD1 . ASN C 1 5   ? 62.955  60.843  25.082 1.000 150.276 0 5   ASN AAA OD1 1 ? 1  
ATOM 3454  N ND2 . ASN C 1 5   ? 63.527  58.727  25.565 1.000 141.226 0 5   ASN AAA ND2 1 ? 1  
ATOM 3455  N N   . LEU C 1 6   ? 61.557  62.629  26.700 1.000 158.348 0 6   LEU AAA N   1 ? 1  
ATOM 3456  C CA  . LEU C 1 6   ? 60.846  63.691  26.001 1.000 154.372 0 6   LEU AAA CA  1 ? 1  
ATOM 3457  C C   . LEU C 1 6   ? 60.532  63.300  24.565 1.000 150.246 0 6   LEU AAA C   1 ? 1  
ATOM 3458  O O   . LEU C 1 6   ? 59.515  63.737  24.017 1.000 158.550 0 6   LEU AAA O   1 ? 1  
ATOM 3459  C CB  . LEU C 1 6   ? 61.648  64.988  26.071 1.000 159.727 0 6   LEU AAA CB  1 ? 1  
ATOM 3460  C CG  . LEU C 1 6   ? 61.495  65.771  27.385 1.000 163.851 0 6   LEU AAA CG  1 ? 1  
ATOM 3461  C CD1 . LEU C 1 6   ? 60.037  65.837  27.818 1.000 163.456 0 6   LEU AAA CD1 1 ? 1  
ATOM 3462  C CD2 . LEU C 1 6   ? 62.321  65.167  28.512 1.000 163.086 0 6   LEU AAA CD2 1 ? 1  
ATOM 3463  N N   . GLN C 1 7   ? 61.375  62.488  23.939 1.000 148.143 0 7   GLN AAA N   1 ? 1  
ATOM 3464  C CA  . GLN C 1 7   ? 60.935  61.817  22.731 1.000 150.791 0 7   GLN AAA CA  1 ? 1  
ATOM 3465  C C   . GLN C 1 7   ? 60.151  60.571  23.128 1.000 159.972 0 7   GLN AAA C   1 ? 1  
ATOM 3466  O O   . GLN C 1 7   ? 60.136  60.164  24.291 1.000 162.757 0 7   GLN AAA O   1 ? 1  
ATOM 3467  C CB  . GLN C 1 7   ? 62.120  61.471  21.836 1.000 148.962 0 7   GLN AAA CB  1 ? 1  
ATOM 3468  C CG  . GLN C 1 7   ? 62.902  62.687  21.393 1.000 152.334 0 7   GLN AAA CG  1 ? 1  
ATOM 3469  C CD  . GLN C 1 7   ? 64.021  62.336  20.443 1.000 155.595 0 7   GLN AAA CD  1 ? 1  
ATOM 3470  O OE1 . GLN C 1 7   ? 64.195  61.182  20.054 1.000 159.500 0 7   GLN AAA OE1 1 ? 1  
ATOM 3471  N NE2 . GLN C 1 7   ? 64.757  63.346  19.997 1.000 153.750 0 7   GLN AAA NE2 1 ? 1  
ATOM 3472  N N   . GLY C 1 8   ? 59.488  59.954  22.154 1.000 184.756 0 8   GLY AAA N   1 ? 1  
ATOM 3473  C CA  . GLY C 1 8   ? 58.613  58.847  22.489 1.000 181.525 0 8   GLY AAA CA  1 ? 1  
ATOM 3474  C C   . GLY C 1 8   ? 59.321  57.637  23.062 1.000 174.889 0 8   GLY AAA C   1 ? 1  
ATOM 3475  O O   . GLY C 1 8   ? 58.659  56.752  23.613 1.000 176.113 0 8   GLY AAA O   1 ? 1  
ATOM 3476  N N   . GLN C 1 9   ? 60.646  57.567  22.946 1.000 157.428 0 9   GLN AAA N   1 ? 1  
ATOM 3477  C CA  . GLN C 1 9   ? 61.350  56.342  23.301 1.000 148.495 0 9   GLN AAA CA  1 ? 1  
ATOM 3478  C C   . GLN C 1 9   ? 61.486  56.144  24.814 1.000 136.883 0 9   GLN AAA C   1 ? 1  
ATOM 3479  O O   . GLN C 1 9   ? 61.669  57.099  25.578 1.000 132.738 0 9   GLN AAA O   1 ? 1  
ATOM 3480  C CB  . GLN C 1 9   ? 62.736  56.386  22.651 1.000 146.283 0 9   GLN AAA CB  1 ? 1  
ATOM 3481  C CG  . GLN C 1 9   ? 63.670  55.221  22.927 1.000 151.641 0 9   GLN AAA CG  1 ? 1  
ATOM 3482  C CD  . GLN C 1 9   ? 65.093  55.531  22.484 1.000 161.028 0 9   GLN AAA CD  1 ? 1  
ATOM 3483  O OE1 . GLN C 1 9   ? 65.351  56.571  21.866 1.000 163.941 0 9   GLN AAA OE1 1 ? 1  
ATOM 3484  N NE2 . GLN C 1 9   ? 66.026  54.631  22.783 1.000 161.994 0 9   GLN AAA NE2 1 ? 1  
ATOM 3485  N N   . MET C 1 10  ? 61.374  54.878  25.225 1.000 123.362 0 10  MET AAA N   1 ? 1  
ATOM 3486  C CA  . MET C 1 10  ? 61.478  54.427  26.614 1.000 113.426 0 10  MET AAA CA  1 ? 1  
ATOM 3487  C C   . MET C 1 10  ? 62.926  54.149  27.006 1.000 109.505 0 10  MET AAA C   1 ? 1  
ATOM 3488  O O   . MET C 1 10  ? 63.580  53.293  26.397 1.000 110.775 0 10  MET AAA O   1 ? 1  
ATOM 3489  C CB  . MET C 1 10  ? 60.571  53.238  26.903 1.000 110.984 0 10  MET AAA CB  1 ? 1  
ATOM 3490  C CG  . MET C 1 10  ? 59.118  53.592  26.668 1.000 119.725 0 10  MET AAA CG  1 ? 1  
ATOM 3491  S SD  . MET C 1 10  ? 58.008  52.582  27.657 1.000 137.560 0 10  MET AAA SD  1 ? 1  
ATOM 3492  C CE  . MET C 1 10  ? 58.150  50.986  26.834 1.000 129.503 0 10  MET AAA CE  1 ? 1  
ATOM 3493  N N   . VAL C 1 11  ? 63.434  54.861  28.008 1.000 103.310 0 11  VAL AAA N   1 ? 1  
ATOM 3494  C CA  . VAL C 1 11  ? 64.827  54.722  28.404 1.000 101.771 0 11  VAL AAA CA  1 ? 1  
ATOM 3495  C C   . VAL C 1 11  ? 64.879  54.445  29.902 1.000 101.662 0 11  VAL AAA C   1 ? 1  
ATOM 3496  O O   . VAL C 1 11  ? 63.965  54.781  30.657 1.000 104.993 0 11  VAL AAA O   1 ? 1  
ATOM 3497  C CB  . VAL C 1 11  ? 65.673  55.956  28.047 1.000 108.303 0 11  VAL AAA CB  1 ? 1  
ATOM 3498  C CG1 . VAL C 1 11  ? 65.658  56.190  26.547 1.000 120.113 0 11  VAL AAA CG1 1 ? 1  
ATOM 3499  C CG2 . VAL C 1 11  ? 65.209  57.189  28.822 1.000 110.095 0 11  VAL AAA CG2 1 ? 1  
ATOM 3500  N N   . HIS C 1 12  ? 65.979  53.822  30.319 1.000 101.163 0 12  HIS AAA N   1 ? 1  
ATOM 3501  C CA  . HIS C 1 12  ? 66.265  53.530  31.720 1.000 95.232  0 12  HIS AAA CA  1 ? 1  
ATOM 3502  C C   . HIS C 1 12  ? 66.712  54.798  32.444 1.000 101.845 0 12  HIS AAA C   1 ? 1  
ATOM 3503  O O   . HIS C 1 12  ? 67.374  55.671  31.876 1.000 116.070 0 12  HIS AAA O   1 ? 1  
ATOM 3504  C CB  . HIS C 1 12  ? 67.330  52.431  31.840 1.000 98.397  0 12  HIS AAA CB  1 ? 1  
ATOM 3505  C CG  . HIS C 1 12  ? 67.688  52.072  33.252 1.000 97.095  0 12  HIS AAA CG  1 ? 1  
ATOM 3506  N ND1 . HIS C 1 12  ? 68.762  52.622  33.919 1.000 105.395 0 12  HIS AAA ND1 1 ? 1  
ATOM 3507  C CD2 . HIS C 1 12  ? 67.127  51.185  34.111 1.000 98.174  0 12  HIS AAA CD2 1 ? 1  
ATOM 3508  C CE1 . HIS C 1 12  ? 68.837  52.105  35.132 1.000 111.771 0 12  HIS AAA CE1 1 ? 1  
ATOM 3509  N NE2 . HIS C 1 12  ? 67.857  51.229  35.274 1.000 104.794 0 12  HIS AAA NE2 1 ? 1  
ATOM 3510  N N   . GLN C 1 13  ? 66.323  54.891  33.718 1.000 93.089  0 13  GLN AAA N   1 ? 1  
ATOM 3511  C CA  . GLN C 1 13  ? 66.699  55.980  34.613 1.000 94.538  0 13  GLN AAA CA  1 ? 1  
ATOM 3512  C C   . GLN C 1 13  ? 67.127  55.430  35.960 1.000 95.661  0 13  GLN AAA C   1 ? 1  
ATOM 3513  O O   . GLN C 1 13  ? 66.592  54.426  36.438 1.000 93.482  0 13  GLN AAA O   1 ? 1  
ATOM 3514  C CB  . GLN C 1 13  ? 65.529  56.946  34.858 1.000 96.143  0 13  GLN AAA CB  1 ? 1  
ATOM 3515  C CG  . GLN C 1 13  ? 65.906  58.405  35.003 1.000 111.988 0 13  GLN AAA CG  1 ? 1  
ATOM 3516  C CD  . GLN C 1 13  ? 64.693  59.318  34.949 1.000 124.870 0 13  GLN AAA CD  1 ? 1  
ATOM 3517  O OE1 . GLN C 1 13  ? 63.559  58.875  35.153 1.000 129.448 0 13  GLN AAA OE1 1 ? 1  
ATOM 3518  N NE2 . GLN C 1 13  ? 64.927  60.600  34.702 1.000 136.662 0 13  GLN AAA NE2 1 ? 1  
ATOM 3519  N N   . CYS C 1 14  ? 68.138  56.069  36.534 1.000 102.621 0 14  CYS AAA N   1 ? 1  
ATOM 3520  C CA  . CYS C 1 14  ? 68.650  55.639  37.821 1.000 103.845 0 14  CYS AAA CA  1 ? 1  
ATOM 3521  C C   . CYS C 1 14  ? 67.538  55.750  38.848 1.000 100.851 0 14  CYS AAA C   1 ? 1  
ATOM 3522  O O   . CYS C 1 14  ? 66.732  56.683  38.816 1.000 103.853 0 14  CYS AAA O   1 ? 1  
ATOM 3523  C CB  . CYS C 1 14  ? 69.810  56.540  38.238 1.000 110.821 0 14  CYS AAA CB  1 ? 1  
ATOM 3524  S SG  . CYS C 1 14  ? 71.221  56.509  37.131 1.000 120.958 0 14  CYS AAA SG  1 ? 1  
ATOM 3525  N N   . ILE C 1 15  ? 67.508  54.792  39.773 1.000 96.282  0 15  ILE AAA N   1 ? 1  
ATOM 3526  C CA  . ILE C 1 15  ? 66.612  54.904  40.912 1.000 96.219  0 15  ILE AAA CA  1 ? 1  
ATOM 3527  C C   . ILE C 1 15  ? 66.950  56.182  41.668 1.000 96.127  0 15  ILE AAA C   1 ? 1  
ATOM 3528  O O   . ILE C 1 15  ? 68.125  56.529  41.849 1.000 98.033  0 15  ILE AAA O   1 ? 1  
ATOM 3529  C CB  . ILE C 1 15  ? 66.730  53.648  41.793 1.000 94.364  0 15  ILE AAA CB  1 ? 1  
ATOM 3530  C CG1 . ILE C 1 15  ? 65.664  53.653  42.879 1.000 88.156  0 15  ILE AAA CG1 1 ? 1  
ATOM 3531  C CG2 . ILE C 1 15  ? 68.133  53.497  42.361 1.000 98.844  0 15  ILE AAA CG2 1 ? 1  
ATOM 3532  C CD1 . ILE C 1 15  ? 64.308  53.256  42.365 1.000 96.008  0 15  ILE AAA CD1 1 ? 1  
ATOM 3533  N N   . SER C 1 16  ? 65.912  56.928  42.071 1.000 93.763  0 16  SER AAA N   1 ? 1  
ATOM 3534  C CA  . SER C 1 16  ? 66.298  58.222  42.610 1.000 96.602  0 16  SER AAA CA  1 ? 1  
ATOM 3535  C C   . SER C 1 16  ? 66.655  58.142  44.094 1.000 91.493  0 16  SER AAA C   1 ? 1  
ATOM 3536  O O   . SER C 1 16  ? 66.147  57.290  44.823 1.000 97.596  0 16  SER AAA O   1 ? 1  
ATOM 3537  C CB  . SER C 1 16  ? 65.166  59.226  42.411 1.000 96.989  0 16  SER AAA CB  1 ? 1  
ATOM 3538  O OG  . SER C 1 16  ? 65.338  60.363  43.238 1.000 105.191 0 16  SER AAA OG  1 ? 1  
ATOM 3539  N N   . PRO C 1 17  ? 67.556  59.007  44.563 1.000 87.061  0 17  PRO AAA N   1 ? 1  
ATOM 3540  C CA  . PRO C 1 17  ? 67.812  59.055  46.009 1.000 93.064  0 17  PRO AAA CA  1 ? 1  
ATOM 3541  C C   . PRO C 1 17  ? 66.581  59.371  46.842 1.000 94.996  0 17  PRO AAA C   1 ? 1  
ATOM 3542  O O   . PRO C 1 17  ? 66.410  58.802  47.927 1.000 91.711  0 17  PRO AAA O   1 ? 1  
ATOM 3543  C CB  . PRO C 1 17  ? 68.874  60.157  46.131 1.000 97.247  0 17  PRO AAA CB  1 ? 1  
ATOM 3544  C CG  . PRO C 1 17  ? 69.569  60.158  44.817 1.000 100.730 0 17  PRO AAA CG  1 ? 1  
ATOM 3545  C CD  . PRO C 1 17  ? 68.509  59.831  43.801 1.000 99.864  0 17  PRO AAA CD  1 ? 1  
ATOM 3546  N N   . ARG C 1 18  ? 65.695  60.234  46.334 1.000 94.252  0 18  ARG AAA N   1 ? 1  
ATOM 3547  C CA  . ARG C 1 18  ? 64.446  60.540  47.029 1.000 92.725  0 18  ARG AAA CA  1 ? 1  
ATOM 3548  C C   . ARG C 1 18  ? 63.557  59.317  47.223 1.000 89.978  0 18  ARG AAA C   1 ? 1  
ATOM 3549  O O   . ARG C 1 18  ? 63.055  59.075  48.326 1.000 96.337  0 18  ARG AAA O   1 ? 1  
ATOM 3550  C CB  . ARG C 1 18  ? 63.673  61.621  46.271 1.000 96.611  0 18  ARG AAA CB  1 ? 1  
ATOM 3551  C CG  . ARG C 1 18  ? 64.051  63.069  46.582 1.000 107.373 0 18  ARG AAA CG  1 ? 1  
ATOM 3552  C CD  . ARG C 1 18  ? 62.889  63.984  46.202 1.000 116.201 0 18  ARG AAA CD  1 ? 1  
ATOM 3553  N NE  . ARG C 1 18  ? 63.057  65.387  46.574 1.000 133.041 0 18  ARG AAA NE  1 ? 1  
ATOM 3554  C CZ  . ARG C 1 18  ? 62.667  65.916  47.734 1.000 141.668 0 18  ARG AAA CZ  1 ? 1  
ATOM 3555  N NH1 . ARG C 1 18  ? 62.063  65.172  48.652 1.000 139.619 0 18  ARG AAA NH1 1 ? 1  
ATOM 3556  N NH2 . ARG C 1 18  ? 62.835  67.214  47.941 1.000 142.905 0 18  ARG AAA NH2 1 ? 1  
ATOM 3557  N N   . THR C 1 19  ? 63.362  58.523  46.170 1.000 87.014  0 19  THR AAA N   1 ? 1  
ATOM 3558  C CA  . THR C 1 19  ? 62.544  57.321  46.302 1.000 87.291  0 19  THR AAA CA  1 ? 1  
ATOM 3559  C C   . THR C 1 19  ? 63.151  56.327  47.300 1.000 88.521  0 19  THR AAA C   1 ? 1  
ATOM 3560  O O   . THR C 1 19  ? 62.449  55.829  48.191 1.000 94.480  0 19  THR AAA O   1 ? 1  
ATOM 3561  C CB  . THR C 1 19  ? 62.261  56.717  44.916 1.000 91.776  0 19  THR AAA CB  1 ? 1  
ATOM 3562  O OG1 . THR C 1 19  ? 61.260  55.695  45.017 1.000 98.679  0 19  THR AAA OG1 1 ? 1  
ATOM 3563  C CG2 . THR C 1 19  ? 63.488  56.147  44.270 1.000 104.049 0 19  THR AAA CG2 1 ? 1  
ATOM 3564  N N   . LEU C 1 20  ? 64.455  56.046  47.190 1.000 84.502  0 20  LEU AAA N   1 ? 1  
ATOM 3565  C CA  . LEU C 1 20  ? 65.093  55.085  48.093 1.000 87.636  0 20  LEU AAA CA  1 ? 1  
ATOM 3566  C C   . LEU C 1 20  ? 64.911  55.488  49.548 1.000 92.056  0 20  LEU AAA C   1 ? 1  
ATOM 3567  O O   . LEU C 1 20  ? 64.518  54.667  50.385 1.000 92.682  0 20  LEU AAA O   1 ? 1  
ATOM 3568  C CB  . LEU C 1 20  ? 66.576  54.923  47.770 1.000 86.829  0 20  LEU AAA CB  1 ? 1  
ATOM 3569  C CG  . LEU C 1 20  ? 66.894  54.232  46.451 1.000 95.629  0 20  LEU AAA CG  1 ? 1  
ATOM 3570  C CD1 . LEU C 1 20  ? 68.312  54.556  46.046 1.000 95.250  0 20  LEU AAA CD1 1 ? 1  
ATOM 3571  C CD2 . LEU C 1 20  ? 66.689  52.725  46.588 1.000 94.357  0 20  LEU AAA CD2 1 ? 1  
ATOM 3572  N N   . ASN C 1 21  ? 65.193  56.750  49.869 1.000 94.546  0 21  ASN AAA N   1 ? 1  
ATOM 3573  C CA  . ASN C 1 21  ? 65.050  57.192  51.251 1.000 91.696  0 21  ASN AAA CA  1 ? 1  
ATOM 3574  C C   . ASN C 1 21  ? 63.598  57.095  51.701 1.000 90.134  0 21  ASN AAA C   1 ? 1  
ATOM 3575  O O   . ASN C 1 21  ? 63.318  56.653  52.821 1.000 96.745  0 21  ASN AAA O   1 ? 1  
ATOM 3576  C CB  . ASN C 1 21  ? 65.558  58.627  51.394 1.000 96.918  0 21  ASN AAA CB  1 ? 1  
ATOM 3577  C CG  . ASN C 1 21  ? 65.574  59.102  52.835 1.000 107.410 0 21  ASN AAA CG  1 ? 1  
ATOM 3578  O OD1 . ASN C 1 21  ? 65.461  58.305  53.767 1.000 114.745 0 21  ASN AAA OD1 1 ? 1  
ATOM 3579  N ND2 . ASN C 1 21  ? 65.703  60.409  53.025 1.000 112.253 0 21  ASN AAA ND2 1 ? 1  
ATOM 3580  N N   . ALA C 1 22  ? 62.659  57.477  50.832 1.000 88.142  0 22  ALA AAA N   1 ? 1  
ATOM 3581  C CA  . ALA C 1 22  ? 61.244  57.400  51.185 1.000 89.642  0 22  ALA AAA CA  1 ? 1  
ATOM 3582  C C   . ALA C 1 22  ? 60.827  55.980  51.558 1.000 88.398  0 22  ALA AAA C   1 ? 1  
ATOM 3583  O O   . ALA C 1 22  ? 60.127  55.776  52.557 1.000 90.868  0 22  ALA AAA O   1 ? 1  
ATOM 3584  C CB  . ALA C 1 22  ? 60.386  57.921  50.033 1.000 87.235  0 22  ALA AAA CB  1 ? 1  
ATOM 3585  N N   . TRP C 1 23  ? 61.254  54.985  50.776 1.000 83.556  0 23  TRP AAA N   1 ? 1  
ATOM 3586  C CA  . TRP C 1 23  ? 60.882  53.604  51.071 1.000 83.015  0 23  TRP AAA CA  1 ? 1  
ATOM 3587  C C   . TRP C 1 23  ? 61.506  53.135  52.379 1.000 85.623  0 23  TRP AAA C   1 ? 1  
ATOM 3588  O O   . TRP C 1 23  ? 60.833  52.522  53.214 1.000 95.219  0 23  TRP AAA O   1 ? 1  
ATOM 3589  C CB  . TRP C 1 23  ? 61.294  52.681  49.929 1.000 80.608  0 23  TRP AAA CB  1 ? 1  
ATOM 3590  C CG  . TRP C 1 23  ? 61.079  51.241  50.259 1.000 80.829  0 23  TRP AAA CG  1 ? 1  
ATOM 3591  C CD1 . TRP C 1 23  ? 62.026  50.261  50.304 1.000 84.860  0 23  TRP AAA CD1 1 ? 1  
ATOM 3592  C CD2 . TRP C 1 23  ? 59.829  50.604  50.549 1.000 81.118  0 23  TRP AAA CD2 1 ? 1  
ATOM 3593  N NE1 . TRP C 1 23  ? 61.449  49.059  50.634 1.000 86.914  0 23  TRP AAA NE1 1 ? 1  
ATOM 3594  C CE2 . TRP C 1 23  ? 60.100  49.241  50.785 1.000 84.140  0 23  TRP AAA CE2 1 ? 1  
ATOM 3595  C CE3 . TRP C 1 23  ? 58.508  51.055  50.641 1.000 84.119  0 23  TRP AAA CE3 1 ? 1  
ATOM 3596  C CZ2 . TRP C 1 23  ? 59.101  48.326  51.107 1.000 85.323  0 23  TRP AAA CZ2 1 ? 1  
ATOM 3597  C CZ3 . TRP C 1 23  ? 57.519  50.144  50.963 1.000 89.892  0 23  TRP AAA CZ3 1 ? 1  
ATOM 3598  C CH2 . TRP C 1 23  ? 57.821  48.794  51.191 1.000 88.878  0 23  TRP AAA CH2 1 ? 1  
ATOM 3599  N N   . VAL C 1 24  ? 62.807  53.371  52.554 1.000 88.021  0 24  VAL AAA N   1 ? 1  
ATOM 3600  C CA  . VAL C 1 24  ? 63.466  52.995  53.802 1.000 89.540  0 24  VAL AAA CA  1 ? 1  
ATOM 3601  C C   . VAL C 1 24  ? 62.760  53.624  54.998 1.000 93.351  0 24  VAL AAA C   1 ? 1  
ATOM 3602  O O   . VAL C 1 24  ? 62.524  52.960  56.015 1.000 103.892 0 24  VAL AAA O   1 ? 1  
ATOM 3603  C CB  . VAL C 1 24  ? 64.959  53.378  53.747 1.000 91.352  0 24  VAL AAA CB  1 ? 1  
ATOM 3604  C CG1 . VAL C 1 24  ? 65.576  53.390  55.140 1.000 104.974 0 24  VAL AAA CG1 1 ? 1  
ATOM 3605  C CG2 . VAL C 1 24  ? 65.712  52.417  52.842 1.000 90.986  0 24  VAL AAA CG2 1 ? 1  
ATOM 3606  N N   . LYS C 1 25  ? 62.376  54.898  54.886 1.000 93.630  0 25  LYS AAA N   1 ? 1  
ATOM 3607  C CA  . LYS C 1 25  ? 61.795  55.600  56.030 1.000 99.882  0 25  LYS AAA CA  1 ? 1  
ATOM 3608  C C   . LYS C 1 25  ? 60.384  55.118  56.365 1.000 102.992 0 25  LYS AAA C   1 ? 1  
ATOM 3609  O O   . LYS C 1 25  ? 60.050  54.954  57.545 1.000 110.996 0 25  LYS AAA O   1 ? 1  
ATOM 3610  C CB  . LYS C 1 25  ? 61.810  57.105  55.781 1.000 105.781 0 25  LYS AAA CB  1 ? 1  
ATOM 3611  C CG  . LYS C 1 25  ? 63.177  57.725  56.023 1.000 116.426 0 25  LYS AAA CG  1 ? 1  
ATOM 3612  C CD  . LYS C 1 25  ? 63.146  59.240  55.907 1.000 126.435 0 25  LYS AAA CD  1 ? 1  
ATOM 3613  C CE  . LYS C 1 25  ? 64.472  59.855  56.344 1.000 133.538 0 25  LYS AAA CE  1 ? 1  
ATOM 3614  N NZ  . LYS C 1 25  ? 64.547  61.318  56.065 1.000 141.064 0 25  LYS AAA NZ  1 ? 1  
ATOM 3615  N N   . VAL C 1 26  ? 59.533  54.913  55.356 1.000 99.350  0 26  VAL AAA N   1 ? 1  
ATOM 3616  C CA  . VAL C 1 26  ? 58.162  54.482  55.630 1.000 95.619  0 26  VAL AAA CA  1 ? 1  
ATOM 3617  C C   . VAL C 1 26  ? 58.156  53.129  56.330 1.000 97.216  0 26  VAL AAA C   1 ? 1  
ATOM 3618  O O   . VAL C 1 26  ? 57.321  52.869  57.204 1.000 112.929 0 26  VAL AAA O   1 ? 1  
ATOM 3619  C CB  . VAL C 1 26  ? 57.309  54.476  54.345 1.000 93.521  0 26  VAL AAA CB  1 ? 1  
ATOM 3620  C CG1 . VAL C 1 26  ? 57.232  55.882  53.759 1.000 97.808  0 26  VAL AAA CG1 1 ? 1  
ATOM 3621  C CG2 . VAL C 1 26  ? 57.823  53.470  53.324 1.000 95.126  0 26  VAL AAA CG2 1 ? 1  
ATOM 3622  N N   . VAL C 1 27  ? 59.069  52.240  55.947 1.000 93.749  0 27  VAL AAA N   1 ? 1  
ATOM 3623  C CA  . VAL C 1 27  ? 59.181  50.963  56.643 1.000 100.447 0 27  VAL AAA CA  1 ? 1  
ATOM 3624  C C   . VAL C 1 27  ? 59.641  51.166  58.085 1.000 111.675 0 27  VAL AAA C   1 ? 1  
ATOM 3625  O O   . VAL C 1 27  ? 59.142  50.510  59.006 1.000 112.445 0 27  VAL AAA O   1 ? 1  
ATOM 3626  C CB  . VAL C 1 27  ? 60.121  50.024  55.869 1.000 96.215  0 27  VAL AAA CB  1 ? 1  
ATOM 3627  C CG1 . VAL C 1 27  ? 60.362  48.747  56.660 1.000 101.673 0 27  VAL AAA CG1 1 ? 1  
ATOM 3628  C CG2 . VAL C 1 27  ? 59.534  49.715  54.497 1.000 96.106  0 27  VAL AAA CG2 1 ? 1  
ATOM 3629  N N   . GLU C 1 28  ? 60.626  52.040  58.303 1.000 115.826 0 28  GLU AAA N   1 ? 1  
ATOM 3630  C CA  . GLU C 1 28  ? 61.081  52.300  59.665 1.000 119.309 0 28  GLU AAA CA  1 ? 1  
ATOM 3631  C C   . GLU C 1 28  ? 59.970  52.896  60.525 1.000 123.058 0 28  GLU AAA C   1 ? 1  
ATOM 3632  O O   . GLU C 1 28  ? 59.816  52.526  61.694 1.000 138.726 0 28  GLU AAA O   1 ? 1  
ATOM 3633  C CB  . GLU C 1 28  ? 62.297  53.225  59.653 1.000 125.987 0 28  GLU AAA CB  1 ? 1  
ATOM 3634  C CG  . GLU C 1 28  ? 63.600  52.538  59.262 1.000 140.692 0 28  GLU AAA CG  1 ? 1  
ATOM 3635  C CD  . GLU C 1 28  ? 64.781  53.493  59.244 1.000 154.732 0 28  GLU AAA CD  1 ? 1  
ATOM 3636  O OE1 . GLU C 1 28  ? 64.562  54.713  59.514 1.000 155.374 0 28  GLU AAA OE1 1 ? 1  
ATOM 3637  O OE2 . GLU C 1 28  ? 65.923  53.021  59.036 1.000 155.037 0 28  GLU AAA OE2 1 ? 1  
ATOM 3638  N N   . GLU C 1 29  ? 59.167  53.797  59.958 1.000 124.972 0 29  GLU AAA N   1 ? 1  
ATOM 3639  C CA  . GLU C 1 29  ? 58.177  54.505  60.761 1.000 127.201 0 29  GLU AAA CA  1 ? 1  
ATOM 3640  C C   . GLU C 1 29  ? 56.853  53.755  60.849 1.000 124.220 0 29  GLU AAA C   1 ? 1  
ATOM 3641  O O   . GLU C 1 29  ? 56.189  53.800  61.887 1.000 136.452 0 29  GLU AAA O   1 ? 1  
ATOM 3642  C CB  . GLU C 1 29  ? 57.954  55.914  60.210 1.000 134.388 0 29  GLU AAA CB  1 ? 1  
ATOM 3643  C CG  . GLU C 1 29  ? 59.169  56.803  60.386 1.000 148.544 0 29  GLU AAA CG  1 ? 1  
ATOM 3644  C CD  . GLU C 1 29  ? 59.154  58.018  59.479 1.000 165.503 0 29  GLU AAA CD  1 ? 1  
ATOM 3645  O OE1 . GLU C 1 29  ? 58.257  58.114  58.612 1.000 169.158 0 29  GLU AAA OE1 1 ? 1  
ATOM 3646  O OE2 . GLU C 1 29  ? 60.052  58.873  59.626 1.000 174.143 0 29  GLU AAA OE2 1 ? 1  
ATOM 3647  N N   . LYS C 1 30  ? 56.439  53.081  59.778 1.000 110.812 0 30  LYS AAA N   1 ? 1  
ATOM 3648  C CA  . LYS C 1 30  ? 55.136  52.436  59.723 1.000 111.162 0 30  LYS AAA CA  1 ? 1  
ATOM 3649  C C   . LYS C 1 30  ? 55.214  50.914  59.738 1.000 108.593 0 30  LYS AAA C   1 ? 1  
ATOM 3650  O O   . LYS C 1 30  ? 54.171  50.260  59.850 1.000 113.936 0 30  LYS AAA O   1 ? 1  
ATOM 3651  C CB  . LYS C 1 30  ? 54.326  52.921  58.511 1.000 110.132 0 30  LYS AAA CB  1 ? 1  
ATOM 3652  C CG  . LYS C 1 30  ? 53.569  54.214  58.812 1.000 123.246 0 30  LYS AAA CG  1 ? 1  
ATOM 3653  C CD  . LYS C 1 30  ? 52.539  54.578  57.742 1.000 130.835 0 30  LYS AAA CD  1 ? 1  
ATOM 3654  C CE  . LYS C 1 30  ? 51.439  55.482  58.309 1.000 135.035 0 30  LYS AAA CE  1 ? 1  
ATOM 3655  N NZ  . LYS C 1 30  ? 51.864  56.882  58.565 1.000 143.857 0 30  LYS AAA NZ  1 ? 1  
ATOM 3656  N N   . ALA C 1 31  ? 56.413  50.338  59.623 1.000 104.882 0 31  ALA AAA N   1 ? 1  
ATOM 3657  C CA  . ALA C 1 31  ? 56.630  48.895  59.545 1.000 106.240 0 31  ALA AAA CA  1 ? 1  
ATOM 3658  C C   . ALA C 1 31  ? 55.792  48.205  58.477 1.000 105.372 0 31  ALA AAA C   1 ? 1  
ATOM 3659  O O   . ALA C 1 31  ? 55.863  48.561  57.296 1.000 109.321 0 31  ALA AAA O   1 ? 1  
ATOM 3660  C CB  . ALA C 1 31  ? 56.352  48.233  60.899 1.000 114.132 0 31  ALA AAA CB  1 ? 1  
ATOM 3661  N N   . PHE C 1 32  ? 54.993  47.223  58.884 1.000 102.537 0 32  PHE AAA N   1 ? 1  
ATOM 3662  C CA  . PHE C 1 32  ? 54.119  46.488  57.980 1.000 105.482 0 32  PHE AAA CA  1 ? 1  
ATOM 3663  C C   . PHE C 1 32  ? 52.640  46.723  58.272 1.000 106.321 0 32  PHE AAA C   1 ? 1  
ATOM 3664  O O   . PHE C 1 32  ? 51.823  45.798  58.249 1.000 115.838 0 32  PHE AAA O   1 ? 1  
ATOM 3665  C CB  . PHE C 1 32  ? 54.456  44.999  57.996 1.000 110.225 0 32  PHE AAA CB  1 ? 1  
ATOM 3666  C CG  . PHE C 1 32  ? 55.821  44.688  57.449 1.000 107.607 0 32  PHE AAA CG  1 ? 1  
ATOM 3667  C CD1 . PHE C 1 32  ? 56.024  44.635  56.082 1.000 104.163 0 32  PHE AAA CD1 1 ? 1  
ATOM 3668  C CD2 . PHE C 1 32  ? 56.894  44.437  58.291 1.000 114.188 0 32  PHE AAA CD2 1 ? 1  
ATOM 3669  C CE1 . PHE C 1 32  ? 57.270  44.354  55.560 1.000 102.408 0 32  PHE AAA CE1 1 ? 1  
ATOM 3670  C CE2 . PHE C 1 32  ? 58.145  44.151  57.771 1.000 113.416 0 32  PHE AAA CE2 1 ? 1  
ATOM 3671  C CZ  . PHE C 1 32  ? 58.331  44.109  56.404 1.000 105.873 0 32  PHE AAA CZ  1 ? 1  
ATOM 3672  N N   . SER C 1 33  ? 52.290  47.971  58.567 1.000 103.583 0 33  SER AAA N   1 ? 1  
ATOM 3673  C CA  . SER C 1 33  ? 50.896  48.372  58.540 1.000 109.339 0 33  SER AAA CA  1 ? 1  
ATOM 3674  C C   . SER C 1 33  ? 50.368  48.226  57.112 1.000 108.605 0 33  SER AAA C   1 ? 1  
ATOM 3675  O O   . SER C 1 33  ? 51.121  48.394  56.148 1.000 115.180 0 33  SER AAA O   1 ? 1  
ATOM 3676  C CB  . SER C 1 33  ? 50.733  49.814  59.020 1.000 116.874 0 33  SER AAA CB  1 ? 1  
ATOM 3677  O OG  . SER C 1 33  ? 51.219  49.986  60.339 1.000 130.019 0 33  SER AAA OG  1 ? 1  
ATOM 3678  N N   . PRO C 1 34  ? 49.089  47.882  56.945 1.000 107.960 0 34  PRO AAA N   1 ? 1  
ATOM 3679  C CA  . PRO C 1 34  ? 48.580  47.547  55.600 1.000 103.675 0 34  PRO AAA CA  1 ? 1  
ATOM 3680  C C   . PRO C 1 34  ? 48.820  48.614  54.545 1.000 99.845  0 34  PRO AAA C   1 ? 1  
ATOM 3681  O O   . PRO C 1 34  ? 49.007  48.276  53.372 1.000 99.359  0 34  PRO AAA O   1 ? 1  
ATOM 3682  C CB  . PRO C 1 34  ? 47.080  47.344  55.842 1.000 111.982 0 34  PRO AAA CB  1 ? 1  
ATOM 3683  C CG  . PRO C 1 34  ? 46.800  48.071  57.136 1.000 119.076 0 34  PRO AAA CG  1 ? 1  
ATOM 3684  C CD  . PRO C 1 34  ? 48.023  47.849  57.957 1.000 116.674 0 34  PRO AAA CD  1 ? 1  
ATOM 3685  N N   . GLU C 1 35  ? 48.790  49.889  54.918 1.000 105.669 0 35  GLU AAA N   1 ? 1  
ATOM 3686  C CA  . GLU C 1 35  ? 48.971  50.975  53.960 1.000 105.701 0 35  GLU AAA CA  1 ? 1  
ATOM 3687  C C   . GLU C 1 35  ? 50.365  51.002  53.334 1.000 103.514 0 35  GLU AAA C   1 ? 1  
ATOM 3688  O O   . GLU C 1 35  ? 50.585  51.760  52.379 1.000 103.639 0 35  GLU AAA O   1 ? 1  
ATOM 3689  C CB  . GLU C 1 35  ? 48.635  52.304  54.637 1.000 108.989 0 35  GLU AAA CB  1 ? 1  
ATOM 3690  C CG  . GLU C 1 35  ? 49.620  52.748  55.708 1.000 112.823 0 35  GLU AAA CG  1 ? 1  
ATOM 3691  C CD  . GLU C 1 35  ? 49.268  52.183  57.065 1.000 123.584 0 35  GLU AAA CD  1 ? 1  
ATOM 3692  O OE1 . GLU C 1 35  ? 48.530  51.171  57.100 1.000 129.046 0 35  GLU AAA OE1 1 ? 1  
ATOM 3693  O OE2 . GLU C 1 35  ? 49.704  52.767  58.084 1.000 132.534 0 35  GLU AAA OE2 1 ? 1  
ATOM 3694  N N   . VAL C 1 36  ? 51.320  50.232  53.859 1.000 103.846 0 36  VAL AAA N   1 ? 1  
ATOM 3695  C CA  . VAL C 1 36  ? 52.651  50.199  53.262 1.000 94.387  0 36  VAL AAA CA  1 ? 1  
ATOM 3696  C C   . VAL C 1 36  ? 52.615  49.515  51.896 1.000 89.592  0 36  VAL AAA C   1 ? 1  
ATOM 3697  O O   . VAL C 1 36  ? 53.404  49.861  51.006 1.000 100.039 0 36  VAL AAA O   1 ? 1  
ATOM 3698  C CB  A VAL C 1 36  ? 53.647  49.518  54.224 1.000 93.604  0 36  VAL AAA CB  1 ? 1  
ATOM 3699  C CG1 A VAL C 1 36  ? 54.851  48.958  53.476 1.000 94.037  0 36  VAL AAA CG1 1 ? 1  
ATOM 3700  C CG2 A VAL C 1 36  ? 54.103  50.500  55.301 1.000 100.507 0 36  VAL AAA CG2 1 ? 1  
ATOM 3701  N N   . ILE C 1 37  ? 51.700  48.560  51.684 1.000 88.143  0 37  ILE AAA N   1 ? 1  
ATOM 3702  C CA  . ILE C 1 37  ? 51.615  47.900  50.377 1.000 87.086  0 37  ILE AAA CA  1 ? 1  
ATOM 3703  C C   . ILE C 1 37  ? 51.283  48.893  49.267 1.000 90.340  0 37  ILE AAA C   1 ? 1  
ATOM 3704  O O   . ILE C 1 37  ? 51.943  48.850  48.215 1.000 94.675  0 37  ILE AAA O   1 ? 1  
ATOM 3705  C CB  . ILE C 1 37  ? 50.635  46.712  50.439 1.000 87.362  0 37  ILE AAA CB  1 ? 1  
ATOM 3706  C CG1 . ILE C 1 37  ? 51.036  45.714  51.522 1.000 92.063  0 37  ILE AAA CG1 1 ? 1  
ATOM 3707  C CG2 . ILE C 1 37  ? 50.529  46.018  49.089 1.000 85.632  0 37  ILE AAA CG2 1 ? 1  
ATOM 3708  C CD1 . ILE C 1 37  ? 49.844  45.023  52.157 1.000 101.987 0 37  ILE AAA CD1 1 ? 1  
ATOM 3709  N N   . PRO C 1 38  ? 50.267  49.763  49.397 1.000 86.652  0 38  PRO AAA N   1 ? 1  
ATOM 3710  C CA  A PRO C 1 38  ? 50.116  50.849  48.414 1.000 86.219  0 38  PRO AAA CA  1 ? 1  
ATOM 3711  C C   . PRO C 1 38  ? 51.386  51.646  48.178 1.000 84.692  0 38  PRO AAA C   1 ? 1  
ATOM 3712  O O   . PRO C 1 38  ? 51.776  51.870  47.026 1.000 89.776  0 38  PRO AAA O   1 ? 1  
ATOM 3713  C CB  A PRO C 1 38  ? 49.041  51.729  49.054 1.000 89.330  0 38  PRO AAA CB  1 ? 1  
ATOM 3714  C CG  A PRO C 1 38  ? 48.232  50.800  49.921 1.000 92.519  0 38  PRO AAA CG  1 ? 1  
ATOM 3715  C CD  A PRO C 1 38  ? 48.972  49.490  50.041 1.000 89.575  0 38  PRO AAA CD  1 ? 1  
ATOM 3716  N N   . MET C 1 39  ? 52.029  52.098  49.255 1.000 85.593  0 39  MET AAA N   1 ? 1  
ATOM 3717  C CA  . MET C 1 39  ? 53.194  52.961  49.131 1.000 84.475  0 39  MET AAA CA  1 ? 1  
ATOM 3718  C C   . MET C 1 39  ? 54.301  52.298  48.324 1.000 88.269  0 39  MET AAA C   1 ? 1  
ATOM 3719  O O   . MET C 1 39  ? 54.896  52.930  47.443 1.000 88.247  0 39  MET AAA O   1 ? 1  
ATOM 3720  C CB  . MET C 1 39  ? 53.705  53.331  50.522 1.000 88.652  0 39  MET AAA CB  1 ? 1  
ATOM 3721  C CG  . MET C 1 39  ? 54.791  54.379  50.510 1.000 88.376  0 39  MET AAA CG  1 ? 1  
ATOM 3722  S SD  . MET C 1 39  ? 54.121  55.901  49.841 1.000 92.849  0 39  MET AAA SD  1 ? 1  
ATOM 3723  C CE  . MET C 1 39  ? 53.141  56.482  51.227 1.000 100.910 0 39  MET AAA CE  1 ? 1  
ATOM 3724  N N   . PHE C 1 40  ? 54.582  51.025  48.604 1.000 84.268  0 40  PHE AAA N   1 ? 1  
ATOM 3725  C CA  . PHE C 1 40  ? 55.561  50.274  47.824 1.000 83.912  0 40  PHE AAA CA  1 ? 1  
ATOM 3726  C C   . PHE C 1 40  ? 55.211  50.276  46.342 1.000 89.332  0 40  PHE AAA C   1 ? 1  
ATOM 3727  O O   . PHE C 1 40  ? 56.071  50.521  45.485 1.000 98.922  0 40  PHE AAA O   1 ? 1  
ATOM 3728  C CB  . PHE C 1 40  ? 55.670  48.843  48.344 1.000 83.731  0 40  PHE AAA CB  1 ? 1  
ATOM 3729  C CG  . PHE C 1 40  ? 56.586  47.976  47.530 1.000 87.411  0 40  PHE AAA CG  1 ? 1  
ATOM 3730  C CD1 . PHE C 1 40  ? 57.963  48.106  47.645 1.000 85.643  0 40  PHE AAA CD1 1 ? 1  
ATOM 3731  C CD2 . PHE C 1 40  ? 56.077  47.047  46.634 1.000 88.151  0 40  PHE AAA CD2 1 ? 1  
ATOM 3732  C CE1 . PHE C 1 40  ? 58.818  47.316  46.892 1.000 85.273  0 40  PHE AAA CE1 1 ? 1  
ATOM 3733  C CE2 . PHE C 1 40  ? 56.929  46.251  45.874 1.000 89.898  0 40  PHE AAA CE2 1 ? 1  
ATOM 3734  C CZ  . PHE C 1 40  ? 58.302  46.388  46.005 1.000 89.699  0 40  PHE AAA CZ  1 ? 1  
ATOM 3735  N N   . SER C 1 41  ? 53.947  49.994  46.020 1.000 86.660  0 41  SER AAA N   1 ? 1  
ATOM 3736  C CA  . SER C 1 41  ? 53.535  49.931  44.622 1.000 91.671  0 41  SER AAA CA  1 ? 1  
ATOM 3737  C C   . SER C 1 41  ? 53.745  51.270  43.917 1.000 89.842  0 41  SER AAA C   1 ? 1  
ATOM 3738  O O   . SER C 1 41  ? 54.163  51.309  42.754 1.000 98.951  0 41  SER AAA O   1 ? 1  
ATOM 3739  C CB  . SER C 1 41  ? 52.074  49.483  44.534 1.000 91.969  0 41  SER AAA CB  1 ? 1  
ATOM 3740  O OG  . SER C 1 41  ? 51.660  49.296  43.189 1.000 105.355 0 41  SER AAA OG  1 ? 1  
ATOM 3741  N N   . ALA C 1 42  ? 53.448  52.380  44.597 1.000 87.522  0 42  ALA AAA N   1 ? 1  
ATOM 3742  C CA  . ALA C 1 42  ? 53.615  53.694  43.979 1.000 86.782  0 42  ALA AAA CA  1 ? 1  
ATOM 3743  C C   . ALA C 1 42  ? 55.090  54.058  43.837 1.000 91.144  0 42  ALA AAA C   1 ? 1  
ATOM 3744  O O   . ALA C 1 42  ? 55.515  54.574  42.796 1.000 97.107  0 42  ALA AAA O   1 ? 1  
ATOM 3745  C CB  . ALA C 1 42  ? 52.876  54.752  44.796 1.000 86.333  0 42  ALA AAA CB  1 ? 1  
ATOM 3746  N N   . LEU C 1 43  ? 55.885  53.805  44.880 1.000 87.620  0 43  LEU AAA N   1 ? 1  
ATOM 3747  C CA  . LEU C 1 43  ? 57.320  54.070  44.834 1.000 86.146  0 43  LEU AAA CA  1 ? 1  
ATOM 3748  C C   . LEU C 1 43  ? 58.051  53.202  43.816 1.000 90.628  0 43  LEU AAA C   1 ? 1  
ATOM 3749  O O   . LEU C 1 43  ? 59.138  53.581  43.366 1.000 95.431  0 43  LEU AAA O   1 ? 1  
ATOM 3750  C CB  . LEU C 1 43  ? 57.938  53.903  46.220 1.000 84.437  0 43  LEU AAA CB  1 ? 1  
ATOM 3751  C CG  . LEU C 1 43  ? 57.532  55.007  47.200 1.000 82.484  0 43  LEU AAA CG  1 ? 1  
ATOM 3752  C CD1 . LEU C 1 43  ? 58.050  54.723  48.600 1.000 84.020  0 43  LEU AAA CD1 1 ? 1  
ATOM 3753  C CD2 . LEU C 1 43  ? 58.020  56.360  46.711 1.000 82.290  0 43  LEU AAA CD2 1 ? 1  
ATOM 3754  N N   . SER C 1 44  ? 57.493  52.048  43.447 1.000 89.735  0 44  SER AAA N   1 ? 1  
ATOM 3755  C CA  . SER C 1 44  ? 58.127  51.152  42.491 1.000 87.512  0 44  SER AAA CA  1 ? 1  
ATOM 3756  C C   . SER C 1 44  ? 57.548  51.281  41.085 1.000 94.288  0 44  SER AAA C   1 ? 1  
ATOM 3757  O O   . SER C 1 44  ? 57.653  50.343  40.287 1.000 102.857 0 44  SER AAA O   1 ? 1  
ATOM 3758  C CB  . SER C 1 44  ? 58.022  49.707  42.982 1.000 85.340  0 44  SER AAA CB  1 ? 1  
ATOM 3759  O OG  . SER C 1 44  ? 56.671  49.291  43.086 1.000 85.596  0 44  SER AAA OG  1 ? 1  
ATOM 3760  N N   . CYS C 1 45  ? 56.938  52.424  40.772 1.000 92.185  0 45  CYS AAA N   1 ? 1  
ATOM 3761  C CA  . CYS C 1 45  ? 56.400  52.664  39.439 1.000 91.031  0 45  CYS AAA CA  1 ? 1  
ATOM 3762  C C   . CYS C 1 45  ? 57.492  52.572  38.381 1.000 92.955  0 45  CYS AAA C   1 ? 1  
ATOM 3763  O O   . CYS C 1 45  ? 58.517  53.248  38.472 1.000 93.240  0 45  CYS AAA O   1 ? 1  
ATOM 3764  C CB  . CYS C 1 45  ? 55.775  54.055  39.397 1.000 95.492  0 45  CYS AAA CB  1 ? 1  
ATOM 3765  S SG  . CYS C 1 45  ? 54.995  54.516  37.842 1.000 116.351 0 45  CYS AAA SG  1 ? 1  
ATOM 3766  N N   . GLY C 1 46  ? 57.262  51.739  37.365 1.000 88.500  0 46  GLY AAA N   1 ? 1  
ATOM 3767  C CA  . GLY C 1 46  ? 58.248  51.604  36.311 1.000 90.413  0 46  GLY AAA CA  1 ? 1  
ATOM 3768  C C   . GLY C 1 46  ? 59.498  50.834  36.672 1.000 90.297  0 46  GLY AAA C   1 ? 1  
ATOM 3769  O O   . GLY C 1 46  ? 60.427  50.781  35.861 1.000 94.338  0 46  GLY AAA O   1 ? 1  
ATOM 3770  N N   . ALA C 1 47  ? 59.541  50.208  37.844 1.000 89.188  0 47  ALA AAA N   1 ? 1  
ATOM 3771  C CA  . ALA C 1 47  ? 60.765  49.584  38.329 1.000 91.839  0 47  ALA AAA CA  1 ? 1  
ATOM 3772  C C   . ALA C 1 47  ? 61.182  48.394  37.473 1.000 88.403  0 47  ALA AAA C   1 ? 1  
ATOM 3773  O O   . ALA C 1 47  ? 60.343  47.627  36.991 1.000 85.254  0 47  ALA AAA O   1 ? 1  
ATOM 3774  C CB  . ALA C 1 47  ? 60.582  49.132  39.778 1.000 92.721  0 47  ALA AAA CB  1 ? 1  
ATOM 3775  N N   . THR C 1 48  ? 62.496  48.256  37.269 1.000 88.679  0 48  THR AAA N   1 ? 1  
ATOM 3776  C CA  . THR C 1 48  ? 63.039  47.005  36.768 1.000 87.270  0 48  THR AAA CA  1 ? 1  
ATOM 3777  C C   . THR C 1 48  ? 63.082  45.989  37.905 1.000 83.045  0 48  THR AAA C   1 ? 1  
ATOM 3778  O O   . THR C 1 48  ? 62.978  46.358  39.076 1.000 87.336  0 48  THR AAA O   1 ? 1  
ATOM 3779  C CB  . THR C 1 48  ? 64.445  47.217  36.214 1.000 90.667  0 48  THR AAA CB  1 ? 1  
ATOM 3780  O OG1 . THR C 1 48  ? 65.322  47.633  37.270 1.000 95.145  0 48  THR AAA OG1 1 ? 1  
ATOM 3781  C CG2 . THR C 1 48  ? 64.429  48.296  35.149 1.000 93.632  0 48  THR AAA CG2 1 ? 1  
ATOM 3782  N N   . PRO C 1 49  ? 63.251  44.700  37.595 1.000 80.503  0 49  PRO AAA N   1 ? 1  
ATOM 3783  C CA  . PRO C 1 49  ? 63.498  43.737  38.682 1.000 88.490  0 49  PRO AAA CA  1 ? 1  
ATOM 3784  C C   . PRO C 1 49  ? 64.681  44.085  39.570 1.000 95.449  0 49  PRO AAA C   1 ? 1  
ATOM 3785  O O   . PRO C 1 49  ? 64.602  43.902  40.791 1.000 108.747 0 49  PRO AAA O   1 ? 1  
ATOM 3786  C CB  . PRO C 1 49  ? 63.726  42.424  37.924 1.000 81.675  0 49  PRO AAA CB  1 ? 1  
ATOM 3787  C CG  . PRO C 1 49  ? 62.868  42.556  36.721 1.000 81.483  0 49  PRO AAA CG  1 ? 1  
ATOM 3788  C CD  . PRO C 1 49  ? 62.926  44.020  36.328 1.000 84.376  0 49  PRO AAA CD  1 ? 1  
ATOM 3789  N N   . GLN C 1 50  ? 65.778  44.580  38.992 1.000 93.003  0 50  GLN AAA N   1 ? 1  
ATOM 3790  C CA  . GLN C 1 50  ? 66.902  45.053  39.796 1.000 97.239  0 50  GLN AAA CA  1 ? 1  
ATOM 3791  C C   . GLN C 1 50  ? 66.468  46.125  40.788 1.000 94.527  0 50  GLN AAA C   1 ? 1  
ATOM 3792  O O   . GLN C 1 50  ? 66.821  46.075  41.972 1.000 101.340 0 50  GLN AAA O   1 ? 1  
ATOM 3793  C CB  . GLN C 1 50  ? 68.027  45.573  38.901 1.000 95.968  0 50  GLN AAA CB  1 ? 1  
ATOM 3794  C CG  . GLN C 1 50  ? 68.947  46.551  39.616 1.000 99.491  0 50  GLN AAA CG  1 ? 1  
ATOM 3795  C CD  . GLN C 1 50  ? 69.923  47.233  38.685 1.000 104.584 0 50  GLN AAA CD  1 ? 1  
ATOM 3796  O OE1 . GLN C 1 50  ? 70.507  46.598  37.809 1.000 105.004 0 50  GLN AAA OE1 1 ? 1  
ATOM 3797  N NE2 . GLN C 1 50  ? 70.104  48.537  38.869 1.000 110.272 0 50  GLN AAA NE2 1 ? 1  
ATOM 3798  N N   . ASP C 1 51  ? 65.687  47.100  40.317 1.000 91.900  0 51  ASP AAA N   1 ? 1  
ATOM 3799  C CA  . ASP C 1 51  ? 65.233  48.181  41.186 1.000 94.121  0 51  ASP AAA CA  1 ? 1  
ATOM 3800  C C   . ASP C 1 51  ? 64.382  47.651  42.331 1.000 95.101  0 51  ASP AAA C   1 ? 1  
ATOM 3801  O O   . ASP C 1 51  ? 64.517  48.104  43.474 1.000 93.309  0 51  ASP AAA O   1 ? 1  
ATOM 3802  C CB  . ASP C 1 51  ? 64.450  49.203  40.367 1.000 97.626  0 51  ASP AAA CB  1 ? 1  
ATOM 3803  C CG  . ASP C 1 51  ? 65.321  49.933  39.367 1.000 108.889 0 51  ASP AAA CG  1 ? 1  
ATOM 3804  O OD1 . ASP C 1 51  ? 66.535  50.091  39.626 1.000 121.806 0 51  ASP AAA OD1 1 ? 1  
ATOM 3805  O OD2 . ASP C 1 51  ? 64.793  50.309  38.301 1.000 104.829 0 51  ASP AAA OD2 1 ? 1  
ATOM 3806  N N   . LEU C 1 52  ? 63.496  46.697  42.045 1.000 90.392  0 52  LEU AAA N   1 ? 1  
ATOM 3807  C CA  . LEU C 1 52  ? 62.668  46.132  43.104 1.000 88.522  0 52  LEU AAA CA  1 ? 1  
ATOM 3808  C C   . LEU C 1 52  ? 63.532  45.440  44.147 1.000 89.389  0 52  LEU AAA C   1 ? 1  
ATOM 3809  O O   . LEU C 1 52  ? 63.308  45.598  45.354 1.000 98.433  0 52  LEU AAA O   1 ? 1  
ATOM 3810  C CB  . LEU C 1 52  ? 61.643  45.161  42.522 1.000 83.490  0 52  LEU AAA CB  1 ? 1  
ATOM 3811  C CG  . LEU C 1 52  ? 60.601  45.786  41.597 1.000 81.990  0 52  LEU AAA CG  1 ? 1  
ATOM 3812  C CD1 . LEU C 1 52  ? 59.909  44.726  40.746 1.000 83.356  0 52  LEU AAA CD1 1 ? 1  
ATOM 3813  C CD2 . LEU C 1 52  ? 59.593  46.571  42.413 1.000 84.734  0 52  LEU AAA CD2 1 ? 1  
ATOM 3814  N N   . ASN C 1 53  ? 64.535  44.681  43.700 1.000 88.651  0 53  ASN AAA N   1 ? 1  
ATOM 3815  C CA  . ASN C 1 53  ? 65.454  44.044  44.637 1.000 88.814  0 53  ASN AAA CA  1 ? 1  
ATOM 3816  C C   . ASN C 1 53  ? 66.234  45.079  45.435 1.000 87.792  0 53  ASN AAA C   1 ? 1  
ATOM 3817  O O   . ASN C 1 53  ? 66.455  44.907  46.640 1.000 88.508  0 53  ASN AAA O   1 ? 1  
ATOM 3818  C CB  . ASN C 1 53  ? 66.421  43.126  43.883 1.000 93.436  0 53  ASN AAA CB  1 ? 1  
ATOM 3819  C CG  . ASN C 1 53  ? 65.763  41.849  43.391 1.000 96.819  0 53  ASN AAA CG  1 ? 1  
ATOM 3820  O OD1 . ASN C 1 53  ? 64.848  41.322  44.023 1.000 95.915  0 53  ASN AAA OD1 1 ? 1  
ATOM 3821  N ND2 . ASN C 1 53  ? 66.233  41.343  42.255 1.000 104.887 0 53  ASN AAA ND2 1 ? 1  
ATOM 3822  N N   . THR C 1 54  ? 66.671  46.154  44.779 1.000 86.313  0 54  THR AAA N   1 ? 1  
ATOM 3823  C CA  . THR C 1 54  ? 67.314  47.253  45.490 1.000 89.865  0 54  THR AAA CA  1 ? 1  
ATOM 3824  C C   . THR C 1 54  ? 66.441  47.790  46.623 1.000 88.589  0 54  THR AAA C   1 ? 1  
ATOM 3825  O O   . THR C 1 54  ? 66.893  47.896  47.768 1.000 93.163  0 54  THR AAA O   1 ? 1  
ATOM 3826  C CB  . THR C 1 54  ? 67.678  48.364  44.505 1.000 92.978  0 54  THR AAA CB  1 ? 1  
ATOM 3827  O OG1 . THR C 1 54  ? 68.700  47.889  43.617 1.000 106.077 0 54  THR AAA OG1 1 ? 1  
ATOM 3828  C CG2 . THR C 1 54  ? 68.187  49.592  45.246 1.000 89.614  0 54  THR AAA CG2 1 ? 1  
ATOM 3829  N N   . MET C 1 55  ? 65.172  48.093  46.334 1.000 89.119  0 55  MET AAA N   1 ? 1  
ATOM 3830  C CA  . MET C 1 55  ? 64.282  48.613  47.372 1.000 89.248  0 55  MET AAA CA  1 ? 1  
ATOM 3831  C C   . MET C 1 55  ? 64.159  47.645  48.542 1.000 85.627  0 55  MET AAA C   1 ? 1  
ATOM 3832  O O   . MET C 1 55  ? 64.244  48.047  49.708 1.000 86.704  0 55  MET AAA O   1 ? 1  
ATOM 3833  C CB  . MET C 1 55  ? 62.899  48.913  46.795 1.000 86.691  0 55  MET AAA CB  1 ? 1  
ATOM 3834  C CG  . MET C 1 55  ? 62.852  50.082  45.833 1.000 92.130  0 55  MET AAA CG  1 ? 1  
ATOM 3835  S SD  . MET C 1 55  ? 61.220  50.251  45.074 1.000 97.142  0 55  MET AAA SD  1 ? 1  
ATOM 3836  C CE  . MET C 1 55  ? 60.290  50.965  46.426 1.000 91.201  0 55  MET AAA CE  1 ? 1  
ATOM 3837  N N   . LEU C 1 56  ? 63.954  46.361  48.249 1.000 84.213  0 56  LEU AAA N   1 ? 1  
ATOM 3838  C CA  . LEU C 1 56  ? 63.835  45.374  49.315 1.000 85.630  0 56  LEU AAA CA  1 ? 1  
ATOM 3839  C C   . LEU C 1 56  ? 65.153  45.173  50.063 1.000 90.930  0 56  LEU AAA C   1 ? 1  
ATOM 3840  O O   . LEU C 1 56  ? 65.156  45.036  51.293 1.000 95.398  0 56  LEU AAA O   1 ? 1  
ATOM 3841  C CB  . LEU C 1 56  ? 63.344  44.051  48.731 1.000 83.295  0 56  LEU AAA CB  1 ? 1  
ATOM 3842  C CG  . LEU C 1 56  ? 61.959  44.079  48.079 1.000 80.652  0 56  LEU AAA CG  1 ? 1  
ATOM 3843  C CD1 . LEU C 1 56  ? 61.603  42.700  47.542 1.000 79.949  0 56  LEU AAA CD1 1 ? 1  
ATOM 3844  C CD2 . LEU C 1 56  ? 60.890  44.599  49.033 1.000 83.859  0 56  LEU AAA CD2 1 ? 1  
ATOM 3845  N N   . ASN C 1 57  ? 66.279  45.147  49.342 1.000 89.821  0 57  ASN AAA N   1 ? 1  
ATOM 3846  C CA  . ASN C 1 57  ? 67.577  44.919  49.979 1.000 89.543  0 57  ASN AAA CA  1 ? 1  
ATOM 3847  C C   . ASN C 1 57  ? 68.037  46.090  50.845 1.000 87.049  0 57  ASN AAA C   1 ? 1  
ATOM 3848  O O   . ASN C 1 57  ? 68.840  45.890  51.763 1.000 88.163  0 57  ASN AAA O   1 ? 1  
ATOM 3849  C CB  . ASN C 1 57  ? 68.629  44.571  48.929 1.000 87.991  0 57  ASN AAA CB  1 ? 1  
ATOM 3850  C CG  . ASN C 1 57  ? 68.486  43.146  48.419 1.000 98.631  0 57  ASN AAA CG  1 ? 1  
ATOM 3851  O OD1 . ASN C 1 57  ? 67.524  42.450  48.751 1.000 99.271  0 57  ASN AAA OD1 1 ? 1  
ATOM 3852  N ND2 . ASN C 1 57  ? 69.444  42.705  47.611 1.000 114.525 0 57  ASN AAA ND2 1 ? 1  
ATOM 3853  N N   . THR C 1 58  ? 67.575  47.312  50.572 1.000 84.897  0 58  THR AAA N   1 ? 1  
ATOM 3854  C CA  . THR C 1 58  ? 68.012  48.447  51.380 1.000 86.841  0 58  THR AAA CA  1 ? 1  
ATOM 3855  C C   . THR C 1 58  ? 67.336  48.485  52.739 1.000 95.661  0 58  THR AAA C   1 ? 1  
ATOM 3856  O O   . THR C 1 58  ? 67.738  49.288  53.589 1.000 101.293 0 58  THR AAA O   1 ? 1  
ATOM 3857  C CB  . THR C 1 58  ? 67.770  49.780  50.663 1.000 89.604  0 58  THR AAA CB  1 ? 1  
ATOM 3858  O OG1 . THR C 1 58  ? 66.392  49.889  50.280 1.000 93.956  0 58  THR AAA OG1 1 ? 1  
ATOM 3859  C CG2 . THR C 1 58  ? 68.669  49.912  49.449 1.000 92.291  0 58  THR AAA CG2 1 ? 1  
ATOM 3860  N N   . VAL C 1 59  ? 66.334  47.635  52.963 1.000 97.419  0 59  VAL AAA N   1 ? 1  
ATOM 3861  C CA  . VAL C 1 59  ? 65.698  47.548  54.268 1.000 97.827  0 59  VAL AAA CA  1 ? 1  
ATOM 3862  C C   . VAL C 1 59  ? 66.653  46.850  55.220 1.000 108.062 0 59  VAL AAA C   1 ? 1  
ATOM 3863  O O   . VAL C 1 59  ? 67.092  45.721  54.965 1.000 112.401 0 59  VAL AAA O   1 ? 1  
ATOM 3864  C CB  . VAL C 1 59  ? 64.362  46.800  54.172 1.000 92.362  0 59  VAL AAA CB  1 ? 1  
ATOM 3865  C CG1 . VAL C 1 59  ? 63.726  46.693  55.541 1.000 103.941 0 59  VAL AAA CG1 1 ? 1  
ATOM 3866  C CG2 . VAL C 1 59  ? 63.423  47.514  53.216 1.000 96.818  0 59  VAL AAA CG2 1 ? 1  
ATOM 3867  N N   . GLY C 1 60  ? 66.949  47.503  56.341 1.000 124.570 0 60  GLY AAA N   1 ? 1  
ATOM 3868  C CA  . GLY C 1 60  ? 67.915  46.982  57.285 1.000 130.475 0 60  GLY AAA CA  1 ? 1  
ATOM 3869  C C   . GLY C 1 60  ? 67.340  46.051  58.327 1.000 133.552 0 60  GLY AAA C   1 ? 1  
ATOM 3870  O O   . GLY C 1 60  ? 67.958  45.029  58.639 1.000 145.138 0 60  GLY AAA O   1 ? 1  
ATOM 3871  N N   . GLY C 1 61  ? 66.175  46.372  58.877 1.000 114.099 0 61  GLY AAA N   1 ? 1  
ATOM 3872  C CA  . GLY C 1 61  ? 65.559  45.548  59.895 1.000 119.471 0 61  GLY AAA CA  1 ? 1  
ATOM 3873  C C   . GLY C 1 61  ? 64.620  44.524  59.291 1.000 112.527 0 61  GLY AAA C   1 ? 1  
ATOM 3874  O O   . GLY C 1 61  ? 64.670  44.227  58.096 1.000 109.679 0 61  GLY AAA O   1 ? 1  
ATOM 3875  N N   . HIS C 1 62  ? 63.751  43.977  60.143 1.000 112.466 0 62  HIS AAA N   1 ? 1  
ATOM 3876  C CA  . HIS C 1 62  ? 62.633  43.129  59.717 1.000 109.008 0 62  HIS AAA CA  1 ? 1  
ATOM 3877  C C   . HIS C 1 62  ? 63.118  41.968  58.853 1.000 108.209 0 62  HIS AAA C   1 ? 1  
ATOM 3878  O O   . HIS C 1 62  ? 62.460  41.567  57.889 1.000 107.299 0 62  HIS AAA O   1 ? 1  
ATOM 3879  C CB  . HIS C 1 62  ? 61.588  43.949  58.957 1.000 107.913 0 62  HIS AAA CB  1 ? 1  
ATOM 3880  C CG  . HIS C 1 62  ? 61.086  45.142  59.707 1.000 105.642 0 62  HIS AAA CG  1 ? 1  
ATOM 3881  N ND1 . HIS C 1 62  ? 60.282  45.040  60.822 1.000 114.100 0 62  HIS AAA ND1 1 ? 1  
ATOM 3882  C CD2 . HIS C 1 62  ? 61.284  46.466  59.505 1.000 103.849 0 62  HIS AAA CD2 1 ? 1  
ATOM 3883  C CE1 . HIS C 1 62  ? 60.000  46.251  61.269 1.000 116.423 0 62  HIS AAA CE1 1 ? 1  
ATOM 3884  N NE2 . HIS C 1 62  ? 60.597  47.134  60.488 1.000 104.029 0 62  HIS AAA NE2 1 ? 1  
ATOM 3885  N N   . GLN C 1 63  ? 64.281  41.415  59.206 1.000 106.789 0 63  GLN AAA N   1 ? 1  
ATOM 3886  C CA  . GLN C 1 63  ? 64.898  40.390  58.370 1.000 109.692 0 63  GLN AAA CA  1 ? 1  
ATOM 3887  C C   . GLN C 1 63  ? 64.148  39.066  58.416 1.000 110.051 0 63  GLN AAA C   1 ? 1  
ATOM 3888  O O   . GLN C 1 63  ? 64.314  38.245  57.507 1.000 116.327 0 63  GLN AAA O   1 ? 1  
ATOM 3889  C CB  . GLN C 1 63  ? 66.367  40.213  58.758 1.000 107.336 0 63  GLN AAA CB  1 ? 1  
ATOM 3890  C CG  . GLN C 1 63  ? 67.229  41.413  58.377 1.000 105.864 0 63  GLN AAA CG  1 ? 1  
ATOM 3891  C CD  . GLN C 1 63  ? 67.235  41.679  56.876 1.000 99.615  0 63  GLN AAA CD  1 ? 1  
ATOM 3892  O OE1 . GLN C 1 63  ? 67.097  40.759  56.070 1.000 98.489  0 63  GLN AAA OE1 1 ? 1  
ATOM 3893  N NE2 . GLN C 1 63  ? 67.380  42.943  56.497 1.000 107.053 0 63  GLN AAA NE2 1 ? 1  
ATOM 3894  N N   . ALA C 1 64  ? 63.346  38.831  59.457 1.000 108.584 0 64  ALA AAA N   1 ? 1  
ATOM 3895  C CA  . ALA C 1 64  ? 62.452  37.679  59.447 1.000 113.143 0 64  ALA AAA CA  1 ? 1  
ATOM 3896  C C   . ALA C 1 64  ? 61.443  37.789  58.312 1.000 115.935 0 64  ALA AAA C   1 ? 1  
ATOM 3897  O O   . ALA C 1 64  ? 61.251  36.844  57.537 1.000 116.345 0 64  ALA AAA O   1 ? 1  
ATOM 3898  C CB  . ALA C 1 64  ? 61.730  37.568  60.788 1.000 113.604 0 64  ALA AAA CB  1 ? 1  
ATOM 3899  N N   . ALA C 1 65  ? 60.809  38.956  58.184 1.000 111.447 0 65  ALA AAA N   1 ? 1  
ATOM 3900  C CA  . ALA C 1 65  ? 59.866  39.170  57.094 1.000 108.664 0 65  ALA AAA CA  1 ? 1  
ATOM 3901  C C   . ALA C 1 65  ? 60.550  39.041  55.742 1.000 109.348 0 65  ALA AAA C   1 ? 1  
ATOM 3902  O O   . ALA C 1 65  ? 60.008  38.418  54.821 1.000 115.820 0 65  ALA AAA O   1 ? 1  
ATOM 3903  C CB  . ALA C 1 65  ? 59.206  40.540  57.234 1.000 109.530 0 65  ALA AAA CB  1 ? 1  
ATOM 3904  N N   . MET C 1 66  ? 61.750  39.612  55.609 1.000 103.781 0 66  MET AAA N   1 ? 1  
ATOM 3905  C CA  . MET C 1 66  ? 62.457  39.549  54.334 1.000 101.656 0 66  MET AAA CA  1 ? 1  
ATOM 3906  C C   . MET C 1 66  ? 62.768  38.112  53.946 1.000 108.346 0 66  MET AAA C   1 ? 1  
ATOM 3907  O O   . MET C 1 66  ? 62.668  37.747  52.769 1.000 117.342 0 66  MET AAA O   1 ? 1  
ATOM 3908  C CB  . MET C 1 66  ? 63.737  40.377  54.399 1.000 100.257 0 66  MET AAA CB  1 ? 1  
ATOM 3909  C CG  . MET C 1 66  ? 63.510  41.805  54.847 1.000 103.159 0 66  MET AAA CG  1 ? 1  
ATOM 3910  S SD  . MET C 1 66  ? 62.323  42.664  53.795 1.000 100.583 0 66  MET AAA SD  1 ? 1  
ATOM 3911  C CE  . MET C 1 66  ? 63.086  42.498  52.181 1.000 105.941 0 66  MET AAA CE  1 ? 1  
ATOM 3912  N N   . GLN C 1 67  ? 63.144  37.281  54.920 1.000 107.638 0 67  GLN AAA N   1 ? 1  
ATOM 3913  C CA  . GLN C 1 67  ? 63.397  35.874  54.630 1.000 112.624 0 67  GLN AAA CA  1 ? 1  
ATOM 3914  C C   . GLN C 1 67  ? 62.105  35.158  54.246 1.000 114.372 0 67  GLN AAA C   1 ? 1  
ATOM 3915  O O   . GLN C 1 67  ? 62.105  34.293  53.362 1.000 116.856 0 67  GLN AAA O   1 ? 1  
ATOM 3916  C CB  . GLN C 1 67  ? 64.068  35.202  55.831 1.000 108.635 0 67  GLN AAA CB  1 ? 1  
ATOM 3917  C CG  . GLN C 1 67  ? 64.496  33.754  55.592 1.000 113.744 0 67  GLN AAA CG  1 ? 1  
ATOM 3918  C CD  . GLN C 1 67  ? 65.820  33.644  54.843 1.000 123.307 0 67  GLN AAA CD  1 ? 1  
ATOM 3919  O OE1 . GLN C 1 67  ? 66.606  34.592  54.803 1.000 126.612 0 67  GLN AAA OE1 1 ? 1  
ATOM 3920  N NE2 . GLN C 1 67  ? 66.067  32.483  54.245 1.000 129.069 0 67  GLN AAA NE2 1 ? 1  
ATOM 3921  N N   . MET C 1 68  ? 60.999  35.491  54.917 1.000 111.238 0 68  MET AAA N   1 ? 1  
ATOM 3922  C CA  . MET C 1 68  ? 59.692  34.975  54.517 1.000 116.634 0 68  MET AAA CA  1 ? 1  
ATOM 3923  C C   . MET C 1 68  ? 59.324  35.409  53.104 1.000 115.016 0 68  MET AAA C   1 ? 1  
ATOM 3924  O O   . MET C 1 68  ? 58.777  34.620  52.323 1.000 119.197 0 68  MET AAA O   1 ? 1  
ATOM 3925  C CB  . MET C 1 68  ? 58.625  35.451  55.496 1.000 118.161 0 68  MET AAA CB  1 ? 1  
ATOM 3926  C CG  . MET C 1 68  ? 58.645  34.735  56.817 1.000 117.906 0 68  MET AAA CG  1 ? 1  
ATOM 3927  S SD  . MET C 1 68  ? 57.155  35.086  57.759 1.000 128.874 0 68  MET AAA SD  1 ? 1  
ATOM 3928  C CE  . MET C 1 68  ? 57.440  36.778  58.281 1.000 132.050 0 68  MET AAA CE  1 ? 1  
ATOM 3929  N N   . LEU C 1 69  ? 59.601  36.669  52.767 1.000 108.998 0 69  LEU AAA N   1 ? 1  
ATOM 3930  C CA  . LEU C 1 69  ? 59.342  37.166  51.421 1.000 103.834 0 69  LEU AAA CA  1 ? 1  
ATOM 3931  C C   . LEU C 1 69  ? 60.126  36.383  50.374 1.000 111.680 0 69  LEU AAA C   1 ? 1  
ATOM 3932  O O   . LEU C 1 69  ? 59.596  36.070  49.301 1.000 118.451 0 69  LEU AAA O   1 ? 1  
ATOM 3933  C CB  . LEU C 1 69  ? 59.669  38.655  51.352 1.000 100.691 0 69  LEU AAA CB  1 ? 1  
ATOM 3934  C CG  . LEU C 1 69  ? 59.371  39.332  50.018 1.000 108.727 0 69  LEU AAA CG  1 ? 1  
ATOM 3935  C CD1 . LEU C 1 69  ? 57.932  39.065  49.598 1.000 112.543 0 69  LEU AAA CD1 1 ? 1  
ATOM 3936  C CD2 . LEU C 1 69  ? 59.634  40.824  50.126 1.000 105.966 0 69  LEU AAA CD2 1 ? 1  
ATOM 3937  N N   . LYS C 1 70  ? 61.391  36.058  50.666 1.000 116.716 0 70  LYS AAA N   1 ? 1  
ATOM 3938  C CA  . LYS C 1 70  ? 62.196  35.278  49.726 1.000 118.121 0 70  LYS AAA CA  1 ? 1  
ATOM 3939  C C   . LYS C 1 70  ? 61.557  33.924  49.448 1.000 119.734 0 70  LYS AAA C   1 ? 1  
ATOM 3940  O O   . LYS C 1 70  ? 61.546  33.456  48.302 1.000 126.307 0 70  LYS AAA O   1 ? 1  
ATOM 3941  C CB  . LYS C 1 70  ? 63.621  35.079  50.260 1.000 120.112 0 70  LYS AAA CB  1 ? 1  
ATOM 3942  C CG  . LYS C 1 70  ? 64.406  36.346  50.594 1.000 123.593 0 70  LYS AAA CG  1 ? 1  
ATOM 3943  C CD  . LYS C 1 70  ? 64.383  37.378  49.476 1.000 137.869 0 70  LYS AAA CD  1 ? 1  
ATOM 3944  C CE  . LYS C 1 70  ? 65.027  38.683  49.931 1.000 126.201 0 70  LYS AAA CE  1 ? 1  
ATOM 3945  N NZ  . LYS C 1 70  ? 64.875  39.762  48.918 1.000 117.969 0 70  LYS AAA NZ  1 ? 1  
ATOM 3946  N N   . GLU C 1 71  ? 61.034  33.274  50.490 1.000 122.104 0 71  GLU AAA N   1 ? 1  
ATOM 3947  C CA  . GLU C 1 71  ? 60.335  32.005  50.314 1.000 122.227 0 71  GLU AAA CA  1 ? 1  
ATOM 3948  C C   . GLU C 1 71  ? 59.142  32.154  49.377 1.000 117.677 0 71  GLU AAA C   1 ? 1  
ATOM 3949  O O   . GLU C 1 71  ? 58.924  31.312  48.499 1.000 123.791 0 71  GLU AAA O   1 ? 1  
ATOM 3950  C CB  . GLU C 1 71  ? 59.886  31.477  51.677 1.000 129.319 0 71  GLU AAA CB  1 ? 1  
ATOM 3951  C CG  . GLU C 1 71  ? 61.020  30.951  52.555 1.000 140.276 0 71  GLU AAA CG  1 ? 1  
ATOM 3952  C CD  . GLU C 1 71  ? 60.507  30.186  53.769 1.000 170.478 0 71  GLU AAA CD  1 ? 1  
ATOM 3953  O OE1 . GLU C 1 71  ? 59.329  30.401  54.202 1.000 170.512 0 71  GLU AAA OE1 1 ? 1  
ATOM 3954  O OE2 . GLU C 1 71  ? 61.250  29.318  54.288 1.000 187.256 0 71  GLU AAA OE2 1 ? 1  
ATOM 3955  N N   . THR C 1 72  ? 58.355  33.214  49.553 1.000 115.358 0 72  THR AAA N   1 ? 1  
ATOM 3956  C CA  . THR C 1 72  ? 57.197  33.413  48.689 1.000 117.739 0 72  THR AAA CA  1 ? 1  
ATOM 3957  C C   . THR C 1 72  ? 57.624  33.652  47.243 1.000 117.868 0 72  THR AAA C   1 ? 1  
ATOM 3958  O O   . THR C 1 72  ? 57.037  33.086  46.313 1.000 124.673 0 72  THR AAA O   1 ? 1  
ATOM 3959  C CB  . THR C 1 72  ? 56.356  34.579  49.210 1.000 114.420 0 72  THR AAA CB  1 ? 1  
ATOM 3960  O OG1 . THR C 1 72  ? 55.867  34.265  50.522 1.000 123.125 0 72  THR AAA OG1 1 ? 1  
ATOM 3961  C CG2 . THR C 1 72  ? 55.178  34.838  48.284 1.000 112.019 0 72  THR AAA CG2 1 ? 1  
ATOM 3962  N N   . ILE C 1 73  ? 58.657  34.476  47.039 1.000 112.381 0 73  ILE AAA N   1 ? 1  
ATOM 3963  C CA  . ILE C 1 73  ? 59.185  34.721  45.697 1.000 110.283 0 73  ILE AAA CA  1 ? 1  
ATOM 3964  C C   . ILE C 1 73  ? 59.648  33.420  45.049 1.000 115.797 0 73  ILE AAA C   1 ? 1  
ATOM 3965  O O   . ILE C 1 73  ? 59.338  33.139  43.885 1.000 124.403 0 73  ILE AAA O   1 ? 1  
ATOM 3966  C CB  . ILE C 1 73  ? 60.324  35.755  45.759 1.000 107.761 0 73  ILE AAA CB  1 ? 1  
ATOM 3967  C CG1 . ILE C 1 73  ? 59.769  37.142  46.085 1.000 105.157 0 73  ILE AAA CG1 1 ? 1  
ATOM 3968  C CG2 . ILE C 1 73  ? 61.102  35.781  44.454 1.000 108.830 0 73  ILE AAA CG2 1 ? 1  
ATOM 3969  C CD1 . ILE C 1 73  ? 60.837  38.148  46.452 1.000 104.879 0 73  ILE AAA CD1 1 ? 1  
ATOM 3970  N N   . ASN C 1 74  ? 60.374  32.592  45.802 1.000 117.201 0 74  ASN AAA N   1 ? 1  
ATOM 3971  C CA  . ASN C 1 74  ? 60.861  31.326  45.259 1.000 125.148 0 74  ASN AAA CA  1 ? 1  
ATOM 3972  C C   . ASN C 1 74  ? 59.703  30.406  44.899 1.000 126.834 0 74  ASN AAA C   1 ? 1  
ATOM 3973  O O   . ASN C 1 74  ? 59.749  29.699  43.886 1.000 128.683 0 74  ASN AAA O   1 ? 1  
ATOM 3974  C CB  . ASN C 1 74  ? 61.806  30.648  46.249 1.000 133.984 0 74  ASN AAA CB  1 ? 1  
ATOM 3975  C CG  . ASN C 1 74  ? 63.125  31.379  46.376 1.000 148.977 0 74  ASN AAA CG  1 ? 1  
ATOM 3976  O OD1 . ASN C 1 74  ? 63.510  32.146  45.490 1.000 156.635 0 74  ASN AAA OD1 1 ? 1  
ATOM 3977  N ND2 . ASN C 1 74  ? 63.824  31.153  47.484 1.000 150.395 0 74  ASN AAA ND2 1 ? 1  
ATOM 3978  N N   . GLU C 1 75  ? 58.660  30.402  45.727 1.000 136.497 0 75  GLU AAA N   1 ? 1  
ATOM 3979  C CA  . GLU C 1 75  ? 57.448  29.649  45.424 1.000 141.292 0 75  GLU AAA CA  1 ? 1  
ATOM 3980  C C   . GLU C 1 75  ? 56.802  30.127  44.126 1.000 140.057 0 75  GLU AAA C   1 ? 1  
ATOM 3981  O O   . GLU C 1 75  ? 56.383  29.315  43.292 1.000 143.112 0 75  GLU AAA O   1 ? 1  
ATOM 3982  C CB  . GLU C 1 75  ? 56.478  29.789  46.599 1.000 144.819 0 75  GLU AAA CB  1 ? 1  
ATOM 3983  C CG  . GLU C 1 75  ? 55.029  29.444  46.320 1.000 156.984 0 75  GLU AAA CG  1 ? 1  
ATOM 3984  C CD  . GLU C 1 75  ? 54.185  29.460  47.586 1.000 160.419 0 75  GLU AAA CD  1 ? 1  
ATOM 3985  O OE1 . GLU C 1 75  ? 54.771  29.608  48.688 1.000 156.397 0 75  GLU AAA OE1 1 ? 1  
ATOM 3986  O OE2 . GLU C 1 75  ? 52.947  29.313  47.485 1.000 166.539 0 75  GLU AAA OE2 1 ? 1  
ATOM 3987  N N   . GLU C 1 76  ? 56.706  31.445  43.946 1.000 128.409 0 76  GLU AAA N   1 ? 1  
ATOM 3988  C CA  . GLU C 1 76  ? 56.111  32.011  42.737 1.000 123.962 0 76  GLU AAA CA  1 ? 1  
ATOM 3989  C C   . GLU C 1 76  ? 56.963  31.753  41.497 1.000 124.004 0 76  GLU AAA C   1 ? 1  
ATOM 3990  O O   . GLU C 1 76  ? 56.425  31.546  40.403 1.000 127.612 0 76  GLU AAA O   1 ? 1  
ATOM 3991  C CB  . GLU C 1 76  ? 55.885  33.509  42.926 1.000 118.593 0 76  GLU AAA CB  1 ? 1  
ATOM 3992  C CG  . GLU C 1 76  ? 54.848  33.822  43.981 1.000 124.708 0 76  GLU AAA CG  1 ? 1  
ATOM 3993  C CD  . GLU C 1 76  ? 53.482  33.275  43.630 1.000 138.969 0 76  GLU AAA CD  1 ? 1  
ATOM 3994  O OE1 . GLU C 1 76  ? 53.112  33.326  42.438 1.000 146.202 0 76  GLU AAA OE1 1 ? 1  
ATOM 3995  O OE2 . GLU C 1 76  ? 52.781  32.792  44.548 1.000 153.774 0 76  GLU AAA OE2 1 ? 1  
ATOM 3996  N N   . ALA C 1 77  ? 58.288  31.759  41.646 1.000 120.332 0 77  ALA AAA N   1 ? 1  
ATOM 3997  C CA  . ALA C 1 77  ? 59.171  31.459  40.521 1.000 120.483 0 77  ALA AAA CA  1 ? 1  
ATOM 3998  C C   . ALA C 1 77  ? 58.951  30.049  39.987 1.000 128.031 0 77  ALA AAA C   1 ? 1  
ATOM 3999  O O   . ALA C 1 77  ? 58.928  29.838  38.769 1.000 135.171 0 77  ALA AAA O   1 ? 1  
ATOM 4000  C CB  . ALA C 1 77  ? 60.630  31.652  40.932 1.000 121.242 0 77  ALA AAA CB  1 ? 1  
ATOM 4001  N N   . ALA C 1 78  ? 58.796  29.070  40.878 1.000 128.641 0 78  ALA AAA N   1 ? 1  
ATOM 4002  C CA  . ALA C 1 78  ? 58.576  27.696  40.434 1.000 137.686 0 78  ALA AAA CA  1 ? 1  
ATOM 4003  C C   . ALA C 1 78  ? 57.270  27.566  39.659 1.000 140.905 0 78  ALA AAA C   1 ? 1  
ATOM 4004  O O   . ALA C 1 78  ? 57.215  26.875  38.635 1.000 147.062 0 78  ALA AAA O   1 ? 1  
ATOM 4005  C CB  . ALA C 1 78  ? 58.590  26.745  41.629 1.000 145.484 0 78  ALA AAA CB  1 ? 1  
ATOM 4006  N N   . GLU C 1 79  ? 56.206  28.220  40.131 1.000 142.719 0 79  GLU AAA N   1 ? 1  
ATOM 4007  C CA  . GLU C 1 79  ? 54.940  28.173  39.404 1.000 149.229 0 79  GLU AAA CA  1 ? 1  
ATOM 4008  C C   . GLU C 1 79  ? 55.055  28.849  38.040 1.000 144.590 0 79  GLU AAA C   1 ? 1  
ATOM 4009  O O   . GLU C 1 79  ? 54.450  28.390  37.063 1.000 148.343 0 79  GLU AAA O   1 ? 1  
ATOM 4010  C CB  . GLU C 1 79  ? 53.839  28.829  40.242 1.000 155.945 0 79  GLU AAA CB  1 ? 1  
ATOM 4011  C CG  . GLU C 1 79  ? 52.417  28.812  39.651 1.000 161.155 0 79  GLU AAA CG  1 ? 1  
ATOM 4012  C CD  . GLU C 1 79  ? 51.826  27.421  39.409 1.000 167.564 0 79  GLU AAA CD  1 ? 1  
ATOM 4013  O OE1 . GLU C 1 79  ? 52.567  26.416  39.344 1.000 167.404 0 79  GLU AAA OE1 1 ? 1  
ATOM 4014  O OE2 . GLU C 1 79  ? 50.585  27.339  39.287 1.000 175.082 0 79  GLU AAA OE2 1 ? 1  
ATOM 4015  N N   . TRP C 1 80  ? 55.816  29.942  37.951 1.000 133.067 0 80  TRP AAA N   1 ? 1  
ATOM 4016  C CA  . TRP C 1 80  ? 56.080  30.543  36.645 1.000 131.868 0 80  TRP AAA CA  1 ? 1  
ATOM 4017  C C   . TRP C 1 80  ? 56.738  29.551  35.697 1.000 132.694 0 80  TRP AAA C   1 ? 1  
ATOM 4018  O O   . TRP C 1 80  ? 56.317  29.406  34.543 1.000 141.130 0 80  TRP AAA O   1 ? 1  
ATOM 4019  C CB  . TRP C 1 80  ? 56.934  31.804  36.792 1.000 128.503 0 80  TRP AAA CB  1 ? 1  
ATOM 4020  C CG  . TRP C 1 80  ? 57.320  32.393  35.465 1.000 120.263 0 80  TRP AAA CG  1 ? 1  
ATOM 4021  C CD1 . TRP C 1 80  ? 58.462  32.128  34.763 1.000 121.565 0 80  TRP AAA CD1 1 ? 1  
ATOM 4022  C CD2 . TRP C 1 80  ? 56.526  33.238  34.624 1.000 118.560 0 80  TRP AAA CD2 1 ? 1  
ATOM 4023  N NE1 . TRP C 1 80  ? 58.459  32.808  33.574 1.000 123.842 0 80  TRP AAA NE1 1 ? 1  
ATOM 4024  C CE2 . TRP C 1 80  ? 57.278  33.491  33.458 1.000 122.616 0 80  TRP AAA CE2 1 ? 1  
ATOM 4025  C CE3 . TRP C 1 80  ? 55.265  33.827  34.753 1.000 120.577 0 80  TRP AAA CE3 1 ? 1  
ATOM 4026  C CZ2 . TRP C 1 80  ? 56.811  34.306  32.429 1.000 122.976 0 80  TRP AAA CZ2 1 ? 1  
ATOM 4027  C CZ3 . TRP C 1 80  ? 54.803  34.637  33.727 1.000 125.391 0 80  TRP AAA CZ3 1 ? 1  
ATOM 4028  C CH2 . TRP C 1 80  ? 55.574  34.868  32.582 1.000 121.569 0 80  TRP AAA CH2 1 ? 1  
ATOM 4029  N N   . ASP C 1 81  ? 57.792  28.877  36.157 1.000 128.838 0 81  ASP AAA N   1 ? 1  
ATOM 4030  C CA  . ASP C 1 81  ? 58.494  27.943  35.286 1.000 130.618 0 81  ASP AAA CA  1 ? 1  
ATOM 4031  C C   . ASP C 1 81  ? 57.583  26.793  34.867 1.000 134.901 0 81  ASP AAA C   1 ? 1  
ATOM 4032  O O   . ASP C 1 81  ? 57.637  26.332  33.721 1.000 142.308 0 81  ASP AAA O   1 ? 1  
ATOM 4033  C CB  . ASP C 1 81  ? 59.739  27.408  36.002 1.000 130.150 0 81  ASP AAA CB  1 ? 1  
ATOM 4034  C CG  . ASP C 1 81  ? 60.818  28.472  36.193 1.000 129.971 0 81  ASP AAA CG  1 ? 1  
ATOM 4035  O OD1 . ASP C 1 81  ? 60.773  29.507  35.495 1.000 134.740 0 81  ASP AAA OD1 1 ? 1  
ATOM 4036  O OD2 . ASP C 1 81  ? 61.701  28.282  37.062 1.000 124.592 0 81  ASP AAA OD2 1 ? 1  
ATOM 4037  N N   . ARG C 1 82  ? 56.743  26.313  35.787 1.000 128.884 0 82  ARG AAA N   1 ? 1  
ATOM 4038  C CA  . ARG C 1 82  ? 55.804  25.244  35.462 1.000 133.941 0 82  ARG AAA CA  1 ? 1  
ATOM 4039  C C   . ARG C 1 82  ? 54.750  25.649  34.429 1.000 138.536 0 82  ARG AAA C   1 ? 1  
ATOM 4040  O O   . ARG C 1 82  ? 54.433  24.861  33.529 1.000 149.422 0 82  ARG AAA O   1 ? 1  
ATOM 4041  C CB  . ARG C 1 82  ? 55.137  24.760  36.752 1.000 143.545 0 82  ARG AAA CB  1 ? 1  
ATOM 4042  C CG  . ARG C 1 82  ? 54.460  23.412  36.645 1.000 156.244 0 82  ARG AAA CG  1 ? 1  
ATOM 4043  C CD  . ARG C 1 82  ? 53.737  23.049  37.931 1.000 161.212 0 82  ARG AAA CD  1 ? 1  
ATOM 4044  N NE  . ARG C 1 82  ? 52.603  23.935  38.167 1.000 161.080 0 82  ARG AAA NE  1 ? 1  
ATOM 4045  C CZ  . ARG C 1 82  ? 51.435  23.846  37.545 1.000 166.423 0 82  ARG AAA CZ  1 ? 1  
ATOM 4046  N NH1 . ARG C 1 82  ? 51.205  22.916  36.632 1.000 171.427 0 82  ARG AAA NH1 1 ? 1  
ATOM 4047  N NH2 . ARG C 1 82  ? 50.473  24.714  37.846 1.000 167.176 0 82  ARG AAA NH2 1 ? 1  
ATOM 4048  N N   . LEU C 1 83  ? 54.210  26.873  34.506 1.000 134.082 0 83  LEU AAA N   1 ? 1  
ATOM 4049  C CA  . LEU C 1 83  ? 53.192  27.275  33.534 1.000 138.586 0 83  LEU AAA CA  1 ? 1  
ATOM 4050  C C   . LEU C 1 83  ? 53.762  27.870  32.258 1.000 138.915 0 83  LEU AAA C   1 ? 1  
ATOM 4051  O O   . LEU C 1 83  ? 53.066  27.904  31.237 1.000 146.617 0 83  LEU AAA O   1 ? 1  
ATOM 4052  C CB  A LEU C 1 83  ? 52.199  28.238  34.182 1.000 137.511 0 83  LEU AAA CB  1 ? 1  
ATOM 4053  C CG  A LEU C 1 83  ? 51.480  27.504  35.317 1.000 152.261 0 83  LEU AAA CG  1 ? 1  
ATOM 4054  C CD1 A LEU C 1 83  ? 50.673  28.455  36.176 1.000 151.604 0 83  LEU AAA CD1 1 ? 1  
ATOM 4055  C CD2 A LEU C 1 83  ? 50.610  26.367  34.768 1.000 159.446 0 83  LEU AAA CD2 1 ? 1  
ATOM 4056  N N   . HIS C 1 84  ? 55.000  28.340  32.302 1.000 137.386 0 84  HIS AAA N   1 ? 1  
ATOM 4057  C CA  . HIS C 1 84  ? 55.673  28.959  31.161 1.000 137.633 0 84  HIS AAA CA  1 ? 1  
ATOM 4058  C C   . HIS C 1 84  ? 57.092  28.432  31.198 1.000 138.598 0 84  HIS AAA C   1 ? 1  
ATOM 4059  O O   . HIS C 1 84  ? 58.032  29.140  31.581 1.000 138.097 0 84  HIS AAA O   1 ? 1  
ATOM 4060  C CB  . HIS C 1 84  ? 55.625  30.488  31.196 1.000 131.217 0 84  HIS AAA CB  1 ? 1  
ATOM 4061  C CG  . HIS C 1 84  ? 54.245  31.052  31.301 1.000 131.400 0 84  HIS AAA CG  1 ? 1  
ATOM 4062  N ND1 . HIS C 1 84  ? 53.654  31.367  32.505 1.000 133.850 0 84  HIS AAA ND1 1 ? 1  
ATOM 4063  C CD2 . HIS C 1 84  ? 53.343  31.372  30.343 1.000 139.236 0 84  HIS AAA CD2 1 ? 1  
ATOM 4064  C CE1 . HIS C 1 84  ? 52.443  31.848  32.284 1.000 141.088 0 84  HIS AAA CE1 1 ? 1  
ATOM 4065  N NE2 . HIS C 1 84  ? 52.231  31.862  30.979 1.000 148.997 0 84  HIS AAA NE2 1 ? 1  
ATOM 4066  N N   . PRO C 1 85  ? 57.285  27.176  30.814 1.000 137.635 0 85  PRO AAA N   1 ? 1  
ATOM 4067  C CA  . PRO C 1 85  ? 58.638  26.637  30.779 1.000 140.895 0 85  PRO AAA CA  1 ? 1  
ATOM 4068  C C   . PRO C 1 85  ? 59.387  27.300  29.645 1.000 149.018 0 85  PRO AAA C   1 ? 1  
ATOM 4069  O O   . PRO C 1 85  ? 58.798  27.813  28.691 1.000 146.044 0 85  PRO AAA O   1 ? 1  
ATOM 4070  C CB  . PRO C 1 85  ? 58.428  25.144  30.524 1.000 144.373 0 85  PRO AAA CB  1 ? 1  
ATOM 4071  C CG  . PRO C 1 85  ? 56.970  24.891  30.711 1.000 145.952 0 85  PRO AAA CG  1 ? 1  
ATOM 4072  C CD  . PRO C 1 85  ? 56.290  26.179  30.393 1.000 141.913 0 85  PRO AAA CD  1 ? 1  
ATOM 4073  N N   . VAL C 1 86  ? 60.701  27.266  29.746 1.000 165.533 0 86  VAL AAA N   1 ? 1  
ATOM 4074  C CA  . VAL C 1 86  ? 61.552  27.916  28.763 1.000 168.287 0 86  VAL AAA CA  1 ? 1  
ATOM 4075  C C   . VAL C 1 86  ? 61.811  26.996  27.582 1.000 170.856 0 86  VAL AAA C   1 ? 1  
ATOM 4076  O O   . VAL C 1 86  ? 62.213  25.839  27.752 1.000 175.724 0 86  VAL AAA O   1 ? 1  
ATOM 4077  C CB  . VAL C 1 86  ? 62.875  28.349  29.410 1.000 168.400 0 86  VAL AAA CB  1 ? 1  
ATOM 4078  C CG1 . VAL C 1 86  ? 63.822  28.919  28.365 1.000 164.905 0 86  VAL AAA CG1 1 ? 1  
ATOM 4079  C CG2 . VAL C 1 86  ? 62.601  29.343  30.518 1.000 165.527 0 86  VAL AAA CG2 1 ? 1  
ATOM 4080  N N   . HIS C 1 87  ? 61.564  27.513  26.383 1.000 163.927 0 87  HIS AAA N   1 ? 1  
ATOM 4081  C CA  . HIS C 1 87  ? 61.788  26.758  25.161 1.000 162.833 0 87  HIS AAA CA  1 ? 1  
ATOM 4082  C C   . HIS C 1 87  ? 63.288  26.777  24.884 1.000 160.684 0 87  HIS AAA C   1 ? 1  
ATOM 4083  O O   . HIS C 1 87  ? 63.882  27.853  24.754 1.000 158.934 0 87  HIS AAA O   1 ? 1  
ATOM 4084  C CB  . HIS C 1 87  ? 60.987  27.357  24.006 1.000 169.598 0 87  HIS AAA CB  1 ? 1  
ATOM 4085  C CG  . HIS C 1 87  ? 59.499  27.294  24.194 1.000 173.215 0 87  HIS AAA CG  1 ? 1  
ATOM 4086  N ND1 . HIS C 1 87  ? 58.718  26.323  23.605 1.000 183.115 0 87  HIS AAA ND1 1 ? 1  
ATOM 4087  C CD2 . HIS C 1 87  ? 58.650  28.085  24.892 1.000 180.151 0 87  HIS AAA CD2 1 ? 1  
ATOM 4088  C CE1 . HIS C 1 87  ? 57.453  26.515  23.928 1.000 191.820 0 87  HIS AAA CE1 1 ? 1  
ATOM 4089  N NE2 . HIS C 1 87  ? 57.384  27.579  24.717 1.000 193.278 0 87  HIS AAA NE2 1 ? 1  
ATOM 4090  N N   . ALA C 1 88  ? 63.907  25.605  24.800 1.000 159.626 0 88  ALA AAA N   1 ? 1  
ATOM 4091  C CA  . ALA C 1 88  ? 65.357  25.535  24.686 1.000 159.231 0 88  ALA AAA CA  1 ? 1  
ATOM 4092  C C   . ALA C 1 88  ? 65.784  25.496  23.227 1.000 166.996 0 88  ALA AAA C   1 ? 1  
ATOM 4093  O O   . ALA C 1 88  ? 65.097  24.937  22.369 1.000 174.971 0 88  ALA AAA O   1 ? 1  
ATOM 4094  C CB  . ALA C 1 88  ? 65.910  24.310  25.417 1.000 161.514 0 88  ALA AAA CB  1 ? 1  
ATOM 4095  N N   . GLY C 1 89  ? 66.926  26.115  22.952 1.000 163.511 0 89  GLY AAA N   1 ? 1  
ATOM 4096  C CA  . GLY C 1 89  ? 67.493  26.104  21.628 1.000 157.278 0 89  GLY AAA CA  1 ? 1  
ATOM 4097  C C   . GLY C 1 89  ? 68.569  27.155  21.480 1.000 153.488 0 89  GLY AAA C   1 ? 1  
ATOM 4098  O O   . GLY C 1 89  ? 68.750  28.020  22.342 1.000 157.644 0 89  GLY AAA O   1 ? 1  
ATOM 4099  N N   . PRO C 1 90  ? 69.311  27.096  20.379 1.000 154.971 0 90  PRO AAA N   1 ? 1  
ATOM 4100  C CA  . PRO C 1 90  ? 70.281  28.159  20.092 1.000 154.319 0 90  PRO AAA CA  1 ? 1  
ATOM 4101  C C   . PRO C 1 90  ? 69.572  29.471  19.796 1.000 154.055 0 90  PRO AAA C   1 ? 1  
ATOM 4102  O O   . PRO C 1 90  ? 68.549  29.503  19.108 1.000 156.971 0 90  PRO AAA O   1 ? 1  
ATOM 4103  C CB  . PRO C 1 90  ? 71.033  27.638  18.863 1.000 163.243 0 90  PRO AAA CB  1 ? 1  
ATOM 4104  C CG  . PRO C 1 90  ? 70.138  26.591  18.271 1.000 170.233 0 90  PRO AAA CG  1 ? 1  
ATOM 4105  C CD  . PRO C 1 90  ? 69.371  25.996  19.404 1.000 162.888 0 90  PRO AAA CD  1 ? 1  
ATOM 4106  N N   . ILE C 1 91  ? 70.137  30.562  20.302 1.000 154.461 0 91  ILE AAA N   1 ? 1  
ATOM 4107  C CA  . ILE C 1 91  ? 69.523  31.877  20.166 1.000 154.604 0 91  ILE AAA CA  1 ? 1  
ATOM 4108  C C   . ILE C 1 91  ? 69.957  32.505  18.844 1.000 162.023 0 91  ILE AAA C   1 ? 1  
ATOM 4109  O O   . ILE C 1 91  ? 71.146  32.547  18.503 1.000 169.006 0 91  ILE AAA O   1 ? 1  
ATOM 4110  C CB  . ILE C 1 91  ? 69.810  32.775  21.383 1.000 156.529 0 91  ILE AAA CB  1 ? 1  
ATOM 4111  C CG1 . ILE C 1 91  ? 68.663  33.779  21.540 1.000 148.379 0 91  ILE AAA CG1 1 ? 1  
ATOM 4112  C CG2 . ILE C 1 91  ? 71.155  33.478  21.292 1.000 164.449 0 91  ILE AAA CG2 1 ? 1  
ATOM 4113  C CD1 . ILE C 1 91  ? 67.317  33.121  21.796 1.000 147.458 0 91  ILE AAA CD1 1 ? 1  
ATOM 4114  N N   . ALA C 1 92  ? 68.967  32.940  18.093 1.000 165.788 0 92  ALA AAA N   1 ? 1  
ATOM 4115  C CA  . ALA C 1 92  ? 69.131  33.642  16.823 1.000 172.965 0 92  ALA AAA CA  1 ? 1  
ATOM 4116  C C   . ALA C 1 92  ? 69.717  35.043  16.980 1.000 176.323 0 92  ALA AAA C   1 ? 1  
ATOM 4117  O O   . ALA C 1 92  ? 69.310  35.785  17.883 1.000 181.730 0 92  ALA AAA O   1 ? 1  
ATOM 4118  C CB  . ALA C 1 92  ? 67.794  33.720  16.095 1.000 173.017 0 92  ALA AAA CB  1 ? 1  
ATOM 4119  N N   . PRO C 1 93  ? 70.692  35.415  16.146 1.000 180.479 0 93  PRO AAA N   1 ? 1  
ATOM 4120  C CA  . PRO C 1 93  ? 71.318  36.741  16.234 1.000 180.587 0 93  PRO AAA CA  1 ? 1  
ATOM 4121  C C   . PRO C 1 93  ? 70.253  37.822  16.297 1.000 176.533 0 93  PRO AAA C   1 ? 1  
ATOM 4122  O O   . PRO C 1 93  ? 69.375  37.938  15.437 1.000 178.236 0 93  PRO AAA O   1 ? 1  
ATOM 4123  C CB  . PRO C 1 93  ? 72.173  36.829  14.963 1.000 186.908 0 93  PRO AAA CB  1 ? 1  
ATOM 4124  C CG  . PRO C 1 93  ? 71.659  35.765  14.061 1.000 190.405 0 93  PRO AAA CG  1 ? 1  
ATOM 4125  C CD  . PRO C 1 93  ? 71.150  34.675  14.958 1.000 186.983 0 93  PRO AAA CD  1 ? 1  
ATOM 4126  N N   . GLY C 1 94  ? 70.368  38.615  17.350 1.000 167.212 0 94  GLY AAA N   1 ? 1  
ATOM 4127  C CA  . GLY C 1 94  ? 69.542  39.735  17.717 1.000 163.066 0 94  GLY AAA CA  1 ? 1  
ATOM 4128  C C   . GLY C 1 94  ? 68.218  39.380  18.347 1.000 160.502 0 94  GLY AAA C   1 ? 1  
ATOM 4129  O O   . GLY C 1 94  ? 67.338  40.246  18.431 1.000 161.767 0 94  GLY AAA O   1 ? 1  
ATOM 4130  N N   . GLN C 1 95  ? 68.027  38.130  18.775 1.000 156.144 0 95  GLN AAA N   1 ? 1  
ATOM 4131  C CA  . GLN C 1 95  ? 66.774  37.777  19.421 1.000 149.636 0 95  GLN AAA CA  1 ? 1  
ATOM 4132  C C   . GLN C 1 95  ? 67.111  37.635  20.895 1.000 147.288 0 95  GLN AAA C   1 ? 1  
ATOM 4133  O O   . GLN C 1 95  ? 68.223  37.236  21.260 1.000 150.324 0 95  GLN AAA O   1 ? 1  
ATOM 4134  C CB  . GLN C 1 95  ? 66.191  36.444  18.927 1.000 151.809 0 95  GLN AAA CB  1 ? 1  
ATOM 4135  C CG  . GLN C 1 95  ? 65.837  36.342  17.468 1.000 157.159 0 95  GLN AAA CG  1 ? 1  
ATOM 4136  C CD  . GLN C 1 95  ? 64.846  37.403  17.055 1.000 158.321 0 95  GLN AAA CD  1 ? 1  
ATOM 4137  O OE1 . GLN C 1 95  ? 63.898  37.687  17.787 1.000 154.187 0 95  GLN AAA OE1 1 ? 1  
ATOM 4138  N NE2 . GLN C 1 95  ? 65.021  37.949  15.856 1.000 169.366 0 95  GLN AAA NE2 1 ? 1  
ATOM 4139  N N   . MET C 1 96  ? 66.143  37.938  21.733 1.000 146.084 0 96  MET AAA N   1 ? 1  
ATOM 4140  C CA  . MET C 1 96  ? 66.277  37.816  23.174 1.000 139.132 0 96  MET AAA CA  1 ? 1  
ATOM 4141  C C   . MET C 1 96  ? 66.018  36.386  23.666 1.000 135.596 0 96  MET AAA C   1 ? 1  
ATOM 4142  O O   . MET C 1 96  ? 65.333  35.602  23.000 1.000 141.164 0 96  MET AAA O   1 ? 1  
ATOM 4143  C CB  . MET C 1 96  ? 65.422  38.876  23.839 1.000 137.396 0 96  MET AAA CB  1 ? 1  
ATOM 4144  C CG  . MET C 1 96  ? 65.505  38.882  25.309 1.000 136.298 0 96  MET AAA CG  1 ? 1  
ATOM 4145  S SD  . MET C 1 96  ? 65.401  40.612  25.763 1.000 143.095 0 96  MET AAA SD  1 ? 1  
ATOM 4146  C CE  . MET C 1 96  ? 64.203  41.175  24.550 1.000 134.114 0 96  MET AAA CE  1 ? 1  
ATOM 4147  N N   . ARG C 1 97  ? 66.582  36.037  24.824 1.000 122.571 0 97  ARG AAA N   1 ? 1  
ATOM 4148  C CA  . ARG C 1 97  ? 66.284  34.721  25.378 1.000 123.587 0 97  ARG AAA CA  1 ? 1  
ATOM 4149  C C   . ARG C 1 97  ? 64.962  34.785  26.149 1.000 124.724 0 97  ARG AAA C   1 ? 1  
ATOM 4150  O O   . ARG C 1 97  ? 64.420  35.862  26.411 1.000 126.289 0 97  ARG AAA O   1 ? 1  
ATOM 4151  C CB  . ARG C 1 97  ? 67.390  34.207  26.302 1.000 125.335 0 97  ARG AAA CB  1 ? 1  
ATOM 4152  C CG  . ARG C 1 97  ? 67.555  34.914  27.640 1.000 126.550 0 97  ARG AAA CG  1 ? 1  
ATOM 4153  C CD  . ARG C 1 97  ? 68.887  34.527  28.273 1.000 131.738 0 97  ARG AAA CD  1 ? 1  
ATOM 4154  N NE  . ARG C 1 97  ? 69.113  35.181  29.557 1.000 132.959 0 97  ARG AAA NE  1 ? 1  
ATOM 4155  C CZ  . ARG C 1 97  ? 68.574  34.794  30.707 1.000 131.574 0 97  ARG AAA CZ  1 ? 1  
ATOM 4156  N NH1 . ARG C 1 97  ? 67.765  33.748  30.777 1.000 130.159 0 97  ARG AAA NH1 1 ? 1  
ATOM 4157  N NH2 . ARG C 1 97  ? 68.851  35.478  31.814 1.000 125.732 0 97  ARG AAA NH2 1 ? 1  
ATOM 4158  N N   . GLU C 1 98  ? 64.426  33.604  26.512 1.000 130.803 0 98  GLU AAA N   1 ? 1  
ATOM 4159  C CA  . GLU C 1 98  ? 63.159  33.566  27.248 1.000 132.741 0 98  GLU AAA CA  1 ? 1  
ATOM 4160  C C   . GLU C 1 98  ? 63.423  33.688  28.748 1.000 129.656 0 98  GLU AAA C   1 ? 1  
ATOM 4161  O O   . GLU C 1 98  ? 64.326  33.019  29.266 1.000 133.255 0 98  GLU AAA O   1 ? 1  
ATOM 4162  C CB  . GLU C 1 98  ? 62.402  32.276  26.960 1.000 140.379 0 98  GLU AAA CB  1 ? 1  
ATOM 4163  C CG  . GLU C 1 98  ? 61.506  32.343  25.739 1.000 148.209 0 98  GLU AAA CG  1 ? 1  
ATOM 4164  C CD  . GLU C 1 98  ? 61.473  31.032  24.981 1.000 161.961 0 98  GLU AAA CD  1 ? 1  
ATOM 4165  O OE1 . GLU C 1 98  ? 62.545  30.582  24.524 1.000 165.374 0 98  GLU AAA OE1 1 ? 1  
ATOM 4166  O OE2 . GLU C 1 98  ? 60.378  30.453  24.840 1.000 166.191 0 98  GLU AAA OE2 1 ? 1  
ATOM 4167  N N   . PRO C 1 99  ? 62.677  34.528  29.474 1.000 124.990 0 99  PRO AAA N   1 ? 1  
ATOM 4168  C CA  . PRO C 1 99  ? 62.945  34.704  30.909 1.000 114.832 0 99  PRO AAA CA  1 ? 1  
ATOM 4169  C C   . PRO C 1 99  ? 62.440  33.523  31.725 1.000 118.430 0 99  PRO AAA C   1 ? 1  
ATOM 4170  O O   . PRO C 1 99  ? 61.308  33.065  31.550 1.000 121.206 0 99  PRO AAA O   1 ? 1  
ATOM 4171  C CB  . PRO C 1 99  ? 62.163  35.980  31.258 1.000 112.371 0 99  PRO AAA CB  1 ? 1  
ATOM 4172  C CG  . PRO C 1 99  ? 61.397  36.355  29.955 1.000 119.387 0 99  PRO AAA CG  1 ? 1  
ATOM 4173  C CD  . PRO C 1 99  ? 61.372  35.114  29.132 1.000 125.883 0 99  PRO AAA CD  1 ? 1  
ATOM 4174  N N   . ARG C 1 100 ? 63.280  33.054  32.640 1.000 118.237 0 100 ARG AAA N   1 ? 1  
ATOM 4175  C CA  . ARG C 1 100 ? 62.902  32.068  33.638 1.000 117.687 0 100 ARG AAA CA  1 ? 1  
ATOM 4176  C C   . ARG C 1 100 ? 62.398  32.752  34.905 1.000 114.481 0 100 ARG AAA C   1 ? 1  
ATOM 4177  O O   . ARG C 1 100 ? 62.420  33.978  35.026 1.000 116.503 0 100 ARG AAA O   1 ? 1  
ATOM 4178  C CB  . ARG C 1 100 ? 64.107  31.200  33.981 1.000 122.867 0 100 ARG AAA CB  1 ? 1  
ATOM 4179  C CG  . ARG C 1 100 ? 64.871  30.720  32.777 1.000 132.204 0 100 ARG AAA CG  1 ? 1  
ATOM 4180  C CD  . ARG C 1 100 ? 66.057  29.879  33.185 1.000 139.882 0 100 ARG AAA CD  1 ? 1  
ATOM 4181  N NE  . ARG C 1 100 ? 65.649  28.745  33.990 1.000 159.228 0 100 ARG AAA NE  1 ? 1  
ATOM 4182  C CZ  . ARG C 1 100 ? 65.786  27.477  33.625 1.000 171.210 0 100 ARG AAA CZ  1 ? 1  
ATOM 4183  N NH1 . ARG C 1 100 ? 66.313  27.153  32.454 1.000 174.797 0 100 ARG AAA NH1 1 ? 1  
ATOM 4184  N NH2 . ARG C 1 100 ? 65.373  26.512  34.442 1.000 169.839 0 100 ARG AAA NH2 1 ? 1  
ATOM 4185  N N   . GLY C 1 101 ? 61.891  31.938  35.837 1.000 112.951 0 101 GLY AAA N   1 ? 1  
ATOM 4186  C CA  . GLY C 1 101 ? 61.443  32.472  37.116 1.000 112.266 0 101 GLY AAA CA  1 ? 1  
ATOM 4187  C C   . GLY C 1 101 ? 62.510  33.312  37.787 1.000 109.939 0 101 GLY AAA C   1 ? 1  
ATOM 4188  O O   . GLY C 1 101 ? 62.258  34.428  38.249 1.000 103.969 0 101 GLY AAA O   1 ? 1  
ATOM 4189  N N   . SER C 1 102 ? 63.733  32.781  37.831 1.000 110.778 0 102 SER AAA N   1 ? 1  
ATOM 4190  C CA  . SER C 1 102 ? 64.875  33.467  38.422 1.000 113.211 0 102 SER AAA CA  1 ? 1  
ATOM 4191  C C   . SER C 1 102 ? 65.287  34.719  37.653 1.000 110.508 0 102 SER AAA C   1 ? 1  
ATOM 4192  O O   . SER C 1 102 ? 65.872  35.632  38.247 1.000 110.537 0 102 SER AAA O   1 ? 1  
ATOM 4193  C CB  . SER C 1 102 ? 66.041  32.488  38.528 1.000 111.720 0 102 SER AAA CB  1 ? 1  
ATOM 4194  O OG  . SER C 1 102 ? 66.404  32.042  37.239 1.000 116.378 0 102 SER AAA OG  1 ? 1  
ATOM 4195  N N   . ASP C 1 103 ? 64.976  34.800  36.359 1.000 109.406 0 103 ASP AAA N   1 ? 1  
ATOM 4196  C CA  . ASP C 1 103 ? 65.258  36.022  35.610 1.000 105.127 0 103 ASP AAA CA  1 ? 1  
ATOM 4197  C C   . ASP C 1 103 ? 64.285  37.131  35.990 1.000 102.596 0 103 ASP AAA C   1 ? 1  
ATOM 4198  O O   . ASP C 1 103 ? 64.677  38.297  36.103 1.000 106.190 0 103 ASP AAA O   1 ? 1  
ATOM 4199  C CB  . ASP C 1 103 ? 65.203  35.740  34.106 1.000 104.762 0 103 ASP AAA CB  1 ? 1  
ATOM 4200  C CG  . ASP C 1 103 ? 66.294  34.784  33.653 1.000 108.825 0 103 ASP AAA CG  1 ? 1  
ATOM 4201  O OD1 . ASP C 1 103 ? 67.461  34.981  34.048 1.000 106.267 0 103 ASP AAA OD1 1 ? 1  
ATOM 4202  O OD2 . ASP C 1 103 ? 65.984  33.814  32.930 1.000 112.874 0 103 ASP AAA OD2 1 ? 1  
ATOM 4203  N N   . ILE C 1 104 ? 63.018  36.781  36.203 1.000 100.125 0 104 ILE AAA N   1 ? 1  
ATOM 4204  C CA  . ILE C 1 104 ? 62.020  37.757  36.633 1.000 95.024  0 104 ILE AAA CA  1 ? 1  
ATOM 4205  C C   . ILE C 1 104 ? 62.363  38.315  38.011 1.000 91.257  0 104 ILE AAA C   1 ? 1  
ATOM 4206  O O   . ILE C 1 104 ? 62.218  39.518  38.264 1.000 86.553  0 104 ILE AAA O   1 ? 1  
ATOM 4207  C CB  . ILE C 1 104 ? 60.624  37.108  36.610 1.000 98.260  0 104 ILE AAA CB  1 ? 1  
ATOM 4208  C CG1 . ILE C 1 104 ? 60.193  36.837  35.165 1.000 104.608 0 104 ILE AAA CG1 1 ? 1  
ATOM 4209  C CG2 . ILE C 1 104 ? 59.605  37.988  37.319 1.000 97.716  0 104 ILE AAA CG2 1 ? 1  
ATOM 4210  C CD1 . ILE C 1 104 ? 58.724  36.508  35.010 1.000 110.990 0 104 ILE AAA CD1 1 ? 1  
ATOM 4211  N N   . ALA C 1 105 ? 62.859  37.468  38.910 1.000 94.148  0 105 ALA AAA N   1 ? 1  
ATOM 4212  C CA  . ALA C 1 105 ? 63.249  37.919  40.241 1.000 96.987  0 105 ALA AAA CA  1 ? 1  
ATOM 4213  C C   . ALA C 1 105 ? 64.572  38.674  40.267 1.000 97.648  0 105 ALA AAA C   1 ? 1  
ATOM 4214  O O   . ALA C 1 105 ? 65.008  39.081  41.348 1.000 100.588 0 105 ALA AAA O   1 ? 1  
ATOM 4215  C CB  . ALA C 1 105 ? 63.325  36.727  41.198 1.000 103.087 0 105 ALA AAA CB  1 ? 1  
ATOM 4216  N N   . GLY C 1 106 ? 65.232  38.848  39.127 1.000 97.909  0 106 GLY AAA N   1 ? 1  
ATOM 4217  C CA  . GLY C 1 106 ? 66.454  39.624  39.065 1.000 101.903 0 106 GLY AAA CA  1 ? 1  
ATOM 4218  C C   . GLY C 1 106 ? 67.688  38.942  39.606 1.000 103.344 0 106 GLY AAA C   1 ? 1  
ATOM 4219  O O   . GLY C 1 106 ? 68.691  39.620  39.863 1.000 111.164 0 106 GLY AAA O   1 ? 1  
ATOM 4220  N N   . THR C 1 107 ? 67.639  37.630  39.812 1.000 98.394  0 107 THR AAA N   1 ? 1  
ATOM 4221  C CA  . THR C 1 107 ? 68.739  36.869  40.387 1.000 101.142 0 107 THR AAA CA  1 ? 1  
ATOM 4222  C C   . THR C 1 107 ? 69.711  36.399  39.311 1.000 107.122 0 107 THR AAA C   1 ? 1  
ATOM 4223  O O   . THR C 1 107 ? 70.927  36.397  39.528 1.000 114.881 0 107 THR AAA O   1 ? 1  
ATOM 4224  C CB  . THR C 1 107 ? 68.210  35.669  41.178 1.000 104.956 0 107 THR AAA CB  1 ? 1  
ATOM 4225  O OG1 . THR C 1 107 ? 67.504  34.786  40.299 1.000 109.178 0 107 THR AAA OG1 1 ? 1  
ATOM 4226  C CG2 . THR C 1 107 ? 67.268  36.129  42.280 1.000 103.859 0 107 THR AAA CG2 1 ? 1  
ATOM 4227  N N   . THR C 1 108 ? 69.185  36.007  38.149 1.000 107.689 0 108 THR AAA N   1 ? 1  
ATOM 4228  C CA  . THR C 1 108 ? 69.977  35.487  37.039 1.000 109.592 0 108 THR AAA CA  1 ? 1  
ATOM 4229  C C   . THR C 1 108 ? 69.903  36.343  35.780 1.000 110.126 0 108 THR AAA C   1 ? 1  
ATOM 4230  O O   . THR C 1 108 ? 70.382  35.910  34.724 1.000 115.637 0 108 THR AAA O   1 ? 1  
ATOM 4231  C CB  . THR C 1 108 ? 69.537  34.061  36.700 1.000 110.955 0 108 THR AAA CB  1 ? 1  
ATOM 4232  O OG1 . THR C 1 108 ? 68.132  34.049  36.421 1.000 112.529 0 108 THR AAA OG1 1 ? 1  
ATOM 4233  C CG2 . THR C 1 108 ? 69.804  33.139  37.871 1.000 117.076 0 108 THR AAA CG2 1 ? 1  
ATOM 4234  N N   . SER C 1 109 ? 69.321  37.533  35.850 1.000 101.897 0 109 SER AAA N   1 ? 1  
ATOM 4235  C CA  . SER C 1 109 ? 69.210  38.400  34.688 1.000 105.519 0 109 SER AAA CA  1 ? 1  
ATOM 4236  C C   . SER C 1 109 ? 70.062  39.652  34.867 1.000 107.868 0 109 SER AAA C   1 ? 1  
ATOM 4237  O O   . SER C 1 109 ? 70.315  40.097  35.991 1.000 109.465 0 109 SER AAA O   1 ? 1  
ATOM 4238  C CB  . SER C 1 109 ? 67.750  38.801  34.452 1.000 105.214 0 109 SER AAA CB  1 ? 1  
ATOM 4239  O OG  . SER C 1 109 ? 67.219  39.468  35.585 1.000 99.708  0 109 SER AAA OG  1 ? 1  
ATOM 4240  N N   . THR C 1 110 ? 70.518  40.207  33.742 1.000 106.862 0 110 THR AAA N   1 ? 1  
ATOM 4241  C CA  . THR C 1 110 ? 71.274  41.451  33.748 1.000 105.752 0 110 THR AAA CA  1 ? 1  
ATOM 4242  C C   . THR C 1 110 ? 70.302  42.613  33.572 1.000 102.060 0 110 THR AAA C   1 ? 1  
ATOM 4243  O O   . THR C 1 110 ? 69.168  42.432  33.124 1.000 107.567 0 110 THR AAA O   1 ? 1  
ATOM 4244  C CB  . THR C 1 110 ? 72.305  41.446  32.611 1.000 116.893 0 110 THR AAA CB  1 ? 1  
ATOM 4245  O OG1 . THR C 1 110 ? 73.014  40.202  32.619 1.000 130.216 0 110 THR AAA OG1 1 ? 1  
ATOM 4246  C CG2 . THR C 1 110 ? 73.321  42.581  32.760 1.000 120.056 0 110 THR AAA CG2 1 ? 1  
ATOM 4247  N N   . LEU C 1 111 ? 70.750  43.816  33.941 1.000 96.285  0 111 LEU AAA N   1 ? 1  
ATOM 4248  C CA  . LEU C 1 111 ? 69.915  44.992  33.717 1.000 101.024 0 111 LEU AAA CA  1 ? 1  
ATOM 4249  C C   . LEU C 1 111 ? 69.532  45.119  32.248 1.000 114.256 0 111 LEU AAA C   1 ? 1  
ATOM 4250  O O   . LEU C 1 111 ? 68.381  45.439  31.924 1.000 118.098 0 111 LEU AAA O   1 ? 1  
ATOM 4251  C CB  . LEU C 1 111 ? 70.615  46.255  34.217 1.000 99.403  0 111 LEU AAA CB  1 ? 1  
ATOM 4252  C CG  . LEU C 1 111 ? 69.858  47.557  33.936 1.000 94.205  0 111 LEU AAA CG  1 ? 1  
ATOM 4253  C CD1 . LEU C 1 111 ? 68.464  47.508  34.542 1.000 92.374  0 111 LEU AAA CD1 1 ? 1  
ATOM 4254  C CD2 . LEU C 1 111 ? 70.620  48.750  34.482 1.000 103.720 0 111 LEU AAA CD2 1 ? 1  
ATOM 4255  N N   . GLN C 1 112 ? 70.484  44.872  31.344 1.000 123.322 0 112 GLN AAA N   1 ? 1  
ATOM 4256  C CA  . GLN C 1 112 ? 70.196  45.015  29.921 1.000 125.641 0 112 GLN AAA CA  1 ? 1  
ATOM 4257  C C   . GLN C 1 112 ? 69.146  44.007  29.465 1.000 125.980 0 112 GLN AAA C   1 ? 1  
ATOM 4258  O O   . GLN C 1 112 ? 68.256  44.342  28.674 1.000 129.282 0 112 GLN AAA O   1 ? 1  
ATOM 4259  C CB  . GLN C 1 112 ? 71.475  44.876  29.095 1.000 134.555 0 112 GLN AAA CB  1 ? 1  
ATOM 4260  C CG  . GLN C 1 112 ? 72.091  43.488  29.075 1.000 153.601 0 112 GLN AAA CG  1 ? 1  
ATOM 4261  C CD  . GLN C 1 112 ? 72.609  43.122  27.699 1.000 174.517 0 112 GLN AAA CD  1 ? 1  
ATOM 4262  O OE1 . GLN C 1 112 ? 72.874  43.997  26.873 1.000 184.707 0 112 GLN AAA OE1 1 ? 1  
ATOM 4263  N NE2 . GLN C 1 112 ? 72.759  41.826  27.445 1.000 178.518 0 112 GLN AAA NE2 1 ? 1  
ATOM 4264  N N   . GLU C 1 113 ? 69.232  42.765  29.958 1.000 115.238 0 113 GLU AAA N   1 ? 1  
ATOM 4265  C CA  . GLU C 1 113 ? 68.206  41.771  29.659 1.000 109.012 0 113 GLU AAA CA  1 ? 1  
ATOM 4266  C C   . GLU C 1 113 ? 66.849  42.192  30.203 1.000 107.142 0 113 GLU AAA C   1 ? 1  
ATOM 4267  O O   . GLU C 1 113 ? 65.826  42.044  29.522 1.000 109.761 0 113 GLU AAA O   1 ? 1  
ATOM 4268  C CB  . GLU C 1 113 ? 68.607  40.413  30.237 1.000 109.906 0 113 GLU AAA CB  1 ? 1  
ATOM 4269  C CG  . GLU C 1 113 ? 69.797  39.757  29.550 1.000 124.514 0 113 GLU AAA CG  1 ? 1  
ATOM 4270  C CD  . GLU C 1 113 ? 70.248  38.480  30.242 1.000 126.720 0 113 GLU AAA CD  1 ? 1  
ATOM 4271  O OE1 . GLU C 1 113 ? 69.619  38.085  31.248 1.000 117.564 0 113 GLU AAA OE1 1 ? 1  
ATOM 4272  O OE2 . GLU C 1 113 ? 71.229  37.865  29.768 1.000 135.774 0 113 GLU AAA OE2 1 ? 1  
ATOM 4273  N N   . GLN C 1 114 ? 66.817  42.715  31.430 1.000 107.394 0 114 GLN AAA N   1 ? 1  
ATOM 4274  C CA  . GLN C 1 114 ? 65.559  43.183  31.999 1.000 100.746 0 114 GLN AAA CA  1 ? 1  
ATOM 4275  C C   . GLN C 1 114 ? 64.973  44.299  31.147 1.000 98.927  0 114 GLN AAA C   1 ? 1  
ATOM 4276  O O   . GLN C 1 114 ? 63.778  44.302  30.834 1.000 102.915 0 114 GLN AAA O   1 ? 1  
ATOM 4277  C CB  . GLN C 1 114 ? 65.780  43.658  33.438 1.000 95.680  0 114 GLN AAA CB  1 ? 1  
ATOM 4278  C CG  . GLN C 1 114 ? 66.115  42.537  34.408 1.000 92.881  0 114 GLN AAA CG  1 ? 1  
ATOM 4279  C CD  . GLN C 1 114 ? 66.641  43.038  35.741 1.000 90.662  0 114 GLN AAA CD  1 ? 1  
ATOM 4280  O OE1 . GLN C 1 114 ? 66.360  44.164  36.159 1.000 89.162  0 114 GLN AAA OE1 1 ? 1  
ATOM 4281  N NE2 . GLN C 1 114 ? 67.426  42.201  36.411 1.000 90.456  0 114 GLN AAA NE2 1 ? 1  
ATOM 4282  N N   . ILE C 1 115 ? 65.816  45.253  30.754 1.000 99.899  0 115 ILE AAA N   1 ? 1  
ATOM 4283  C CA  . ILE C 1 115 ? 65.379  46.331  29.873 1.000 95.555  0 115 ILE AAA CA  1 ? 1  
ATOM 4284  C C   . ILE C 1 115 ? 64.910  45.788  28.530 1.000 99.998  0 115 ILE AAA C   1 ? 1  
ATOM 4285  O O   . ILE C 1 115 ? 63.896  46.240  27.983 1.000 97.995  0 115 ILE AAA O   1 ? 1  
ATOM 4286  C CB  . ILE C 1 115 ? 66.501  47.367  29.703 1.000 88.062  0 115 ILE AAA CB  1 ? 1  
ATOM 4287  C CG1 . ILE C 1 115 ? 66.750  48.084  31.031 1.000 87.304  0 115 ILE AAA CG1 1 ? 1  
ATOM 4288  C CG2 . ILE C 1 115 ? 66.141  48.341  28.600 1.000 92.346  0 115 ILE AAA CG2 1 ? 1  
ATOM 4289  C CD1 . ILE C 1 115 ? 68.058  48.818  31.098 1.000 93.609  0 115 ILE AAA CD1 1 ? 1  
ATOM 4290  N N   . GLY C 1 116 ? 65.639  44.816  27.976 1.000 101.538 0 116 GLY AAA N   1 ? 1  
ATOM 4291  C CA  . GLY C 1 116 ? 65.228  44.204  26.719 1.000 108.212 0 116 GLY AAA CA  1 ? 1  
ATOM 4292  C C   . GLY C 1 116 ? 63.826  43.623  26.753 1.000 105.400 0 116 GLY AAA C   1 ? 1  
ATOM 4293  O O   . GLY C 1 116 ? 63.025  43.859  25.845 1.000 113.844 0 116 GLY AAA O   1 ? 1  
ATOM 4294  N N   . TRP C 1 117 ? 63.506  42.863  27.801 1.000 99.722  0 117 TRP AAA N   1 ? 1  
ATOM 4295  C CA  . TRP C 1 117 ? 62.172  42.276  27.909 1.000 97.996  0 117 TRP AAA CA  1 ? 1  
ATOM 4296  C C   . TRP C 1 117 ? 61.106  43.345  28.098 1.000 101.880 0 117 TRP AAA C   1 ? 1  
ATOM 4297  O O   . TRP C 1 117 ? 60.059  43.314  27.440 1.000 105.392 0 117 TRP AAA O   1 ? 1  
ATOM 4298  C CB  . TRP C 1 117 ? 62.129  41.247  29.043 1.000 98.158  0 117 TRP AAA CB  1 ? 1  
ATOM 4299  C CG  . TRP C 1 117 ? 62.925  39.999  28.792 1.000 96.693  0 117 TRP AAA CG  1 ? 1  
ATOM 4300  C CD1 . TRP C 1 117 ? 62.966  39.292  27.630 1.000 104.475 0 117 TRP AAA CD1 1 ? 1  
ATOM 4301  C CD2 . TRP C 1 117 ? 63.809  39.327  29.701 1.000 98.730  0 117 TRP AAA CD2 1 ? 1  
ATOM 4302  N NE1 . TRP C 1 117 ? 63.791  38.203  27.765 1.000 108.387 0 117 TRP AAA NE1 1 ? 1  
ATOM 4303  C CE2 . TRP C 1 117 ? 64.332  38.208  29.021 1.000 100.405 0 117 TRP AAA CE2 1 ? 1  
ATOM 4304  C CE3 . TRP C 1 117 ? 64.205  39.558  31.021 1.000 106.433 0 117 TRP AAA CE3 1 ? 1  
ATOM 4305  C CZ2 . TRP C 1 117 ? 65.230  37.323  29.614 1.000 104.185 0 117 TRP AAA CZ2 1 ? 1  
ATOM 4306  C CZ3 . TRP C 1 117 ? 65.099  38.676  31.609 1.000 109.968 0 117 TRP AAA CZ3 1 ? 1  
ATOM 4307  C CH2 . TRP C 1 117 ? 65.601  37.573  30.904 1.000 106.928 0 117 TRP AAA CH2 1 ? 1  
ATOM 4308  N N   . MET C 1 118 ? 61.343  44.286  29.006 1.000 97.813  0 118 MET AAA N   1 ? 1  
ATOM 4309  C CA  . MET C 1 118 ? 60.342  45.303  29.303 1.000 98.864  0 118 MET AAA CA  1 ? 1  
ATOM 4310  C C   . MET C 1 118 ? 60.073  46.235  28.120 1.000 101.260 0 118 MET AAA C   1 ? 1  
ATOM 4311  O O   . MET C 1 118 ? 58.957  46.754  27.999 1.000 108.339 0 118 MET AAA O   1 ? 1  
ATOM 4312  C CB  . MET C 1 118 ? 60.764  46.087  30.546 1.000 102.500 0 118 MET AAA CB  1 ? 1  
ATOM 4313  C CG  . MET C 1 118 ? 60.709  45.259  31.830 1.000 101.638 0 118 MET AAA CG  1 ? 1  
ATOM 4314  S SD  . MET C 1 118 ? 61.471  46.099  33.223 1.000 114.586 0 118 MET AAA SD  1 ? 1  
ATOM 4315  C CE  . MET C 1 118 ? 60.325  47.451  33.474 1.000 110.706 0 118 MET AAA CE  1 ? 1  
ATOM 4316  N N   . THR C 1 119 ? 61.057  46.480  27.249 1.000 104.038 0 119 THR AAA N   1 ? 1  
ATOM 4317  C CA  . THR C 1 119 ? 60.855  47.393  26.125 1.000 109.579 0 119 THR AAA CA  1 ? 1  
ATOM 4318  C C   . THR C 1 119 ? 60.634  46.690  24.786 1.000 112.846 0 119 THR AAA C   1 ? 1  
ATOM 4319  O O   . THR C 1 119 ? 60.629  47.354  23.744 1.000 111.632 0 119 THR AAA O   1 ? 1  
ATOM 4320  C CB  . THR C 1 119 ? 62.049  48.343  26.004 1.000 103.351 0 119 THR AAA CB  1 ? 1  
ATOM 4321  O OG1 . THR C 1 119 ? 63.231  47.586  25.718 1.000 104.329 0 119 THR AAA OG1 1 ? 1  
ATOM 4322  C CG2 . THR C 1 119 ? 62.252  49.090  27.303 1.000 101.031 0 119 THR AAA CG2 1 ? 1  
ATOM 4323  N N   . HIS C 1 120 ? 60.438  45.376  24.785 1.000 122.829 0 120 HIS AAA N   1 ? 1  
ATOM 4324  C CA  . HIS C 1 120 ? 60.208  44.652  23.545 1.000 129.441 0 120 HIS AAA CA  1 ? 1  
ATOM 4325  C C   . HIS C 1 120 ? 58.802  44.946  23.023 1.000 137.828 0 120 HIS AAA C   1 ? 1  
ATOM 4326  O O   . HIS C 1 120 ? 57.953  45.500  23.726 1.000 135.312 0 120 HIS AAA O   1 ? 1  
ATOM 4327  C CB  . HIS C 1 120 ? 60.403  43.149  23.745 1.000 139.423 0 120 HIS AAA CB  1 ? 1  
ATOM 4328  C CG  . HIS C 1 120 ? 60.539  42.387  22.464 1.000 150.193 0 120 HIS AAA CG  1 ? 1  
ATOM 4329  N ND1 . HIS C 1 120 ? 59.529  41.598  21.957 1.000 159.061 0 120 HIS AAA ND1 1 ? 1  
ATOM 4330  C CD2 . HIS C 1 120 ? 61.562  42.304  21.581 1.000 157.850 0 120 HIS AAA CD2 1 ? 1  
ATOM 4331  C CE1 . HIS C 1 120 ? 59.926  41.057  20.819 1.000 171.656 0 120 HIS AAA CE1 1 ? 1  
ATOM 4332  N NE2 . HIS C 1 120 ? 61.156  41.469  20.568 1.000 177.702 0 120 HIS AAA NE2 1 ? 1  
ATOM 4333  N N   . ASN C 1 121 ? 58.578  44.621  21.756 1.000 155.957 0 121 ASN AAA N   1 ? 1  
ATOM 4334  C CA  . ASN C 1 121 ? 57.239  44.678  21.168 1.000 160.203 0 121 ASN AAA CA  1 ? 1  
ATOM 4335  C C   . ASN C 1 121 ? 56.894  43.307  20.600 1.000 168.940 0 121 ASN AAA C   1 ? 1  
ATOM 4336  O O   . ASN C 1 121 ? 57.425  42.935  19.535 1.000 168.598 0 121 ASN AAA O   1 ? 1  
ATOM 4337  C CB  . ASN C 1 121 ? 57.142  45.749  20.085 1.000 162.535 0 121 ASN AAA CB  1 ? 1  
ATOM 4338  C CG  . ASN C 1 121 ? 55.722  45.941  19.589 1.000 167.315 0 121 ASN AAA CG  1 ? 1  
ATOM 4339  O OD1 . ASN C 1 121 ? 54.767  45.875  20.366 1.000 163.933 0 121 ASN AAA OD1 1 ? 1  
ATOM 4340  N ND2 . ASN C 1 121 ? 55.575  46.177  18.291 1.000 180.720 0 121 ASN AAA ND2 1 ? 1  
ATOM 4341  N N   . PRO C 1 122 ? 56.025  42.515  21.251 1.000 175.981 0 122 PRO AAA N   1 ? 1  
ATOM 4342  C CA  . PRO C 1 122 ? 55.316  42.866  22.488 1.000 170.214 0 122 PRO AAA CA  1 ? 1  
ATOM 4343  C C   . PRO C 1 122 ? 56.193  42.817  23.734 1.000 164.808 0 122 PRO AAA C   1 ? 1  
ATOM 4344  O O   . PRO C 1 122 ? 57.149  42.044  23.790 1.000 172.007 0 122 PRO AAA O   1 ? 1  
ATOM 4345  C CB  . PRO C 1 122 ? 54.208  41.803  22.575 1.000 176.327 0 122 PRO AAA CB  1 ? 1  
ATOM 4346  C CG  . PRO C 1 122 ? 54.202  41.105  21.241 1.000 186.909 0 122 PRO AAA CG  1 ? 1  
ATOM 4347  C CD  . PRO C 1 122 ? 55.597  41.207  20.733 1.000 180.902 0 122 PRO AAA CD  1 ? 1  
ATOM 4348  N N   . PRO C 1 123 ? 55.868  43.646  24.722 1.000 146.273 0 123 PRO AAA N   1 ? 1  
ATOM 4349  C CA  . PRO C 1 123 ? 56.690  43.704  25.935 1.000 132.210 0 123 PRO AAA CA  1 ? 1  
ATOM 4350  C C   . PRO C 1 123 ? 56.488  42.491  26.826 1.000 126.720 0 123 PRO AAA C   1 ? 1  
ATOM 4351  O O   . PRO C 1 123 ? 55.371  41.994  26.989 1.000 134.873 0 123 PRO AAA O   1 ? 1  
ATOM 4352  C CB  . PRO C 1 123 ? 56.208  44.984  26.625 1.000 130.501 0 123 PRO AAA CB  1 ? 1  
ATOM 4353  C CG  . PRO C 1 123 ? 54.794  45.124  26.185 1.000 139.212 0 123 PRO AAA CG  1 ? 1  
ATOM 4354  C CD  . PRO C 1 123 ? 54.722  44.570  24.783 1.000 147.097 0 123 PRO AAA CD  1 ? 1  
ATOM 4355  N N   . ILE C 1 124 ? 57.590  42.004  27.387 1.000 115.619 0 124 ILE AAA N   1 ? 1  
ATOM 4356  C CA  . ILE C 1 124 ? 57.525  40.972  28.417 1.000 106.819 0 124 ILE AAA CA  1 ? 1  
ATOM 4357  C C   . ILE C 1 124 ? 57.773  41.689  29.740 1.000 99.772  0 124 ILE AAA C   1 ? 1  
ATOM 4358  O O   . ILE C 1 124 ? 58.930  41.976  30.079 1.000 101.384 0 124 ILE AAA O   1 ? 1  
ATOM 4359  C CB  . ILE C 1 124 ? 58.546  39.852  28.167 1.000 108.360 0 124 ILE AAA CB  1 ? 1  
ATOM 4360  C CG1 . ILE C 1 124 ? 58.334  39.230  26.785 1.000 118.118 0 124 ILE AAA CG1 1 ? 1  
ATOM 4361  C CG2 . ILE C 1 124 ? 58.428  38.780  29.231 1.000 103.799 0 124 ILE AAA CG2 1 ? 1  
ATOM 4362  C CD1 . ILE C 1 124 ? 59.279  39.753  25.723 1.000 120.499 0 124 ILE AAA CD1 1 ? 1  
ATOM 4363  N N   . PRO C 1 125 ? 56.732  41.991  30.521 1.000 98.182  0 125 PRO AAA N   1 ? 1  
ATOM 4364  C CA  . PRO C 1 125 ? 56.878  42.931  31.653 1.000 90.369  0 125 PRO AAA CA  1 ? 1  
ATOM 4365  C C   . PRO C 1 125 ? 57.418  42.273  32.918 1.000 93.377  0 125 PRO AAA C   1 ? 1  
ATOM 4366  O O   . PRO C 1 125 ? 56.709  42.057  33.907 1.000 96.675  0 125 PRO AAA O   1 ? 1  
ATOM 4367  C CB  . PRO C 1 125 ? 55.449  43.456  31.819 1.000 86.876  0 125 PRO AAA CB  1 ? 1  
ATOM 4368  C CG  . PRO C 1 125 ? 54.591  42.278  31.447 1.000 94.507  0 125 PRO AAA CG  1 ? 1  
ATOM 4369  C CD  . PRO C 1 125 ? 55.364  41.456  30.428 1.000 99.538  0 125 PRO AAA CD  1 ? 1  
ATOM 4370  N N   . VAL C 1 126 ? 58.709  41.932  32.888 1.000 91.871  0 126 VAL AAA N   1 ? 1  
ATOM 4371  C CA  . VAL C 1 126 ? 59.315  41.194  33.995 1.000 90.581  0 126 VAL AAA CA  1 ? 1  
ATOM 4372  C C   . VAL C 1 126 ? 59.268  42.012  35.277 1.000 90.701  0 126 VAL AAA C   1 ? 1  
ATOM 4373  O O   . VAL C 1 126 ? 59.193  41.454  36.376 1.000 97.026  0 126 VAL AAA O   1 ? 1  
ATOM 4374  C CB  . VAL C 1 126 ? 60.754  40.779  33.648 1.000 89.970  0 126 VAL AAA CB  1 ? 1  
ATOM 4375  C CG1 . VAL C 1 126 ? 60.740  39.759  32.532 1.000 97.219  0 126 VAL AAA CG1 1 ? 1  
ATOM 4376  C CG2 . VAL C 1 126 ? 61.582  41.993  33.248 1.000 89.351  0 126 VAL AAA CG2 1 ? 1  
ATOM 4377  N N   . GLY C 1 127 ? 59.325  43.341  35.160 1.000 89.868  0 127 GLY AAA N   1 ? 1  
ATOM 4378  C CA  . GLY C 1 127 ? 59.192  44.191  36.332 1.000 90.496  0 127 GLY AAA CA  1 ? 1  
ATOM 4379  C C   . GLY C 1 127 ? 57.834  44.090  36.998 1.000 94.619  0 127 GLY AAA C   1 ? 1  
ATOM 4380  O O   . GLY C 1 127 ? 57.737  43.928  38.219 1.000 94.125  0 127 GLY AAA O   1 ? 1  
ATOM 4381  N N   . GLU C 1 128 ? 56.760  44.139  36.199 1.000 86.237  0 128 GLU AAA N   1 ? 1  
ATOM 4382  C CA  . GLU C 1 128 ? 55.400  44.052  36.757 1.000 87.002  0 128 GLU AAA CA  1 ? 1  
ATOM 4383  C C   . GLU C 1 128 ? 55.103  42.678  37.341 1.000 91.055  0 128 GLU AAA C   1 ? 1  
ATOM 4384  O O   . GLU C 1 128 ? 54.411  42.570  38.358 1.000 98.646  0 128 GLU AAA O   1 ? 1  
ATOM 4385  C CB  . GLU C 1 128 ? 54.365  44.398  35.681 1.000 87.579  0 128 GLU AAA CB  1 ? 1  
ATOM 4386  C CG  . GLU C 1 128 ? 54.402  45.858  35.237 1.000 98.023  0 128 GLU AAA CG  1 ? 1  
ATOM 4387  C CD  . GLU C 1 128 ? 54.338  46.825  36.427 1.000 96.949  0 128 GLU AAA CD  1 ? 1  
ATOM 4388  O OE1 . GLU C 1 128 ? 53.404  46.720  37.254 1.000 91.067  0 128 GLU AAA OE1 1 ? 1  
ATOM 4389  O OE2 . GLU C 1 128 ? 55.286  47.629  36.582 1.000 104.228 0 128 GLU AAA OE2 1 ? 1  
ATOM 4390  N N   . ILE C 1 129 ? 55.606  41.615  36.710 1.000 90.615  0 129 ILE AAA N   1 ? 1  
ATOM 4391  C CA  . ILE C 1 129 ? 55.377  40.271  37.232 1.000 93.687  0 129 ILE AAA CA  1 ? 1  
ATOM 4392  C C   . ILE C 1 129 ? 56.047  40.109  38.586 1.000 91.871  0 129 ILE AAA C   1 ? 1  
ATOM 4393  O O   . ILE C 1 129 ? 55.446  39.603  39.541 1.000 97.637  0 129 ILE AAA O   1 ? 1  
ATOM 4394  C CB  . ILE C 1 129 ? 55.868  39.214  36.228 1.000 100.435 0 129 ILE AAA CB  1 ? 1  
ATOM 4395  C CG1 . ILE C 1 129 ? 55.114  39.336  34.898 1.000 100.569 0 129 ILE AAA CG1 1 ? 1  
ATOM 4396  C CG2 . ILE C 1 129 ? 55.725  37.812  36.816 1.000 104.560 0 129 ILE AAA CG2 1 ? 1  
ATOM 4397  C CD1 . ILE C 1 129 ? 55.798  38.629  33.746 1.000 101.375 0 129 ILE AAA CD1 1 ? 1  
ATOM 4398  N N   . TYR C 1 130 ? 57.305  40.532  38.684 1.000 88.922  0 130 TYR AAA N   1 ? 1  
ATOM 4399  C CA  . TYR C 1 130 ? 58.013  40.441  39.954 1.000 87.907  0 130 TYR AAA CA  1 ? 1  
ATOM 4400  C C   . TYR C 1 130 ? 57.329  41.276  41.034 1.000 89.130  0 130 TYR AAA C   1 ? 1  
ATOM 4401  O O   . TYR C 1 130 ? 57.223  40.838  42.187 1.000 97.234  0 130 TYR AAA O   1 ? 1  
ATOM 4402  C CB  . TYR C 1 130 ? 59.471  40.871  39.764 1.000 87.416  0 130 TYR AAA CB  1 ? 1  
ATOM 4403  C CG  . TYR C 1 130 ? 60.377  40.558  40.931 1.000 84.383  0 130 TYR AAA CG  1 ? 1  
ATOM 4404  C CD1 . TYR C 1 130 ? 60.113  39.485  41.768 1.000 84.770  0 130 TYR AAA CD1 1 ? 1  
ATOM 4405  C CD2 . TYR C 1 130 ? 61.505  41.324  41.186 1.000 87.508  0 130 TYR AAA CD2 1 ? 1  
ATOM 4406  C CE1 . TYR C 1 130 ? 60.936  39.189  42.832 1.000 91.679  0 130 TYR AAA CE1 1 ? 1  
ATOM 4407  C CE2 . TYR C 1 130 ? 62.336  41.036  42.249 1.000 89.233  0 130 TYR AAA CE2 1 ? 1  
ATOM 4408  C CZ  . TYR C 1 130 ? 62.047  39.966  43.071 1.000 94.332  0 130 TYR AAA CZ  1 ? 1  
ATOM 4409  O OH  . TYR C 1 130 ? 62.870  39.663  44.134 1.000 109.227 0 130 TYR AAA OH  1 ? 1  
ATOM 4410  N N   . LYS C 1 131 ? 56.847  42.476  40.686 1.000 88.085  0 131 LYS AAA N   1 ? 1  
ATOM 4411  C CA  . LYS C 1 131 ? 56.176  43.306  41.686 1.000 90.348  0 131 LYS AAA CA  1 ? 1  
ATOM 4412  C C   . LYS C 1 131 ? 54.935  42.622  42.245 1.000 86.449  0 131 LYS AAA C   1 ? 1  
ATOM 4413  O O   . LYS C 1 131 ? 54.663  42.700  43.450 1.000 87.513  0 131 LYS AAA O   1 ? 1  
ATOM 4414  C CB  . LYS C 1 131 ? 55.762  44.642  41.067 1.000 80.608  0 131 LYS AAA CB  1 ? 1  
ATOM 4415  C CG  . LYS C 1 131 ? 55.343  45.694  42.085 1.000 81.608  0 131 LYS AAA CG  1 ? 1  
ATOM 4416  C CD  . LYS C 1 131 ? 54.610  46.855  41.428 1.000 80.463  0 131 LYS AAA CD  1 ? 1  
ATOM 4417  C CE  . LYS C 1 131 ? 55.455  47.631  40.446 1.000 81.741  0 131 LYS AAA CE  1 ? 1  
ATOM 4418  N NZ  . LYS C 1 131 ? 54.836  48.969  40.213 1.000 83.503  0 131 LYS AAA NZ  1 ? 1  
ATOM 4419  N N   . ARG C 1 132 ? 54.174  41.943  41.386 1.000 91.564  0 132 ARG AAA N   1 ? 1  
ATOM 4420  C CA  . ARG C 1 132 ? 53.035  41.159  41.850 1.000 97.747  0 132 ARG AAA CA  1 ? 1  
ATOM 4421  C C   . ARG C 1 132 ? 53.455  40.117  42.876 1.000 96.829  0 132 ARG AAA C   1 ? 1  
ATOM 4422  O O   . ARG C 1 132 ? 52.853  40.019  43.947 1.000 100.231 0 132 ARG AAA O   1 ? 1  
ATOM 4423  C CB  . ARG C 1 132 ? 52.268  40.562  40.673 1.000 108.217 0 132 ARG AAA CB  1 ? 1  
ATOM 4424  C CG  . ARG C 1 132 ? 50.999  39.821  41.088 1.000 125.088 0 132 ARG AAA CG  1 ? 1  
ATOM 4425  C CD  . ARG C 1 132 ? 50.369  39.088  39.914 1.000 133.824 0 132 ARG AAA CD  1 ? 1  
ATOM 4426  N NE  . ARG C 1 132 ? 50.232  39.996  38.774 1.000 146.691 0 132 ARG AAA NE  1 ? 1  
ATOM 4427  C CZ  . ARG C 1 132 ? 50.973  39.948  37.665 1.000 154.216 0 132 ARG AAA CZ  1 ? 1  
ATOM 4428  N NH1 . ARG C 1 132 ? 51.906  39.018  37.501 1.000 142.984 0 132 ARG AAA NH1 1 ? 1  
ATOM 4429  N NH2 . ARG C 1 132 ? 50.764  40.839  36.710 1.000 155.540 0 132 ARG AAA NH2 1 ? 1  
ATOM 4430  N N   . TRP C 1 133 ? 54.528  39.372  42.598 1.000 90.713  0 133 TRP AAA N   1 ? 1  
ATOM 4431  C CA  . TRP C 1 133 ? 54.962  38.348  43.544 1.000 94.864  0 133 TRP AAA CA  1 ? 1  
ATOM 4432  C C   . TRP C 1 133 ? 55.352  38.966  44.875 1.000 92.606  0 133 TRP AAA C   1 ? 1  
ATOM 4433  O O   . TRP C 1 133 ? 55.042  38.422  45.942 1.000 98.355  0 133 TRP AAA O   1 ? 1  
ATOM 4434  C CB  . TRP C 1 133 ? 56.135  37.538  42.989 1.000 95.026  0 133 TRP AAA CB  1 ? 1  
ATOM 4435  C CG  . TRP C 1 133 ? 55.897  36.848  41.680 1.000 100.766 0 133 TRP AAA CG  1 ? 1  
ATOM 4436  C CD1 . TRP C 1 133 ? 54.700  36.660  41.049 1.000 106.553 0 133 TRP AAA CD1 1 ? 1  
ATOM 4437  C CD2 . TRP C 1 133 ? 56.883  36.194  40.873 1.000 101.252 0 133 TRP AAA CD2 1 ? 1  
ATOM 4438  N NE1 . TRP C 1 133 ? 54.888  35.957  39.880 1.000 106.818 0 133 TRP AAA NE1 1 ? 1  
ATOM 4439  C CE2 . TRP C 1 133 ? 56.219  35.656  39.752 1.000 103.871 0 133 TRP AAA CE2 1 ? 1  
ATOM 4440  C CE3 . TRP C 1 133 ? 58.267  36.022  40.984 1.000 99.783  0 133 TRP AAA CE3 1 ? 1  
ATOM 4441  C CZ2 . TRP C 1 133 ? 56.892  34.960  38.750 1.000 104.090 0 133 TRP AAA CZ2 1 ? 1  
ATOM 4442  C CZ3 . TRP C 1 133 ? 58.931  35.331  39.989 1.000 100.028 0 133 TRP AAA CZ3 1 ? 1  
ATOM 4443  C CH2 . TRP C 1 133 ? 58.244  34.809  38.887 1.000 103.966 0 133 TRP AAA CH2 1 ? 1  
ATOM 4444  N N   . ILE C 1 134 ? 56.042  40.101  44.832 1.000 90.158  0 134 ILE AAA N   1 ? 1  
ATOM 4445  C CA  . ILE C 1 134 ? 56.462  40.761  46.059 1.000 82.998  0 134 ILE AAA CA  1 ? 1  
ATOM 4446  C C   . ILE C 1 134 ? 55.245  41.193  46.868 1.000 91.014  0 134 ILE AAA C   1 ? 1  
ATOM 4447  O O   . ILE C 1 134 ? 55.202  41.022  48.093 1.000 98.032  0 134 ILE AAA O   1 ? 1  
ATOM 4448  C CB  . ILE C 1 134 ? 57.370  41.957  45.721 1.000 82.107  0 134 ILE AAA CB  1 ? 1  
ATOM 4449  C CG1 . ILE C 1 134 ? 58.698  41.466  45.144 1.000 85.293  0 134 ILE AAA CG1 1 ? 1  
ATOM 4450  C CG2 . ILE C 1 134 ? 57.603  42.822  46.951 1.000 90.651  0 134 ILE AAA CG2 1 ? 1  
ATOM 4451  C CD1 . ILE C 1 134 ? 59.499  42.548  44.445 1.000 82.493  0 134 ILE AAA CD1 1 ? 1  
ATOM 4452  N N   . ILE C 1 135 ? 54.230  41.745  46.198 1.000 94.839  0 135 ILE AAA N   1 ? 1  
ATOM 4453  C CA  . ILE C 1 135 ? 53.031  42.183  46.907 1.000 90.445  0 135 ILE AAA CA  1 ? 1  
ATOM 4454  C C   . ILE C 1 135 ? 52.274  41.007  47.531 1.000 94.974  0 135 ILE AAA C   1 ? 1  
ATOM 4455  O O   . ILE C 1 135 ? 51.768  41.121  48.653 1.000 104.323 0 135 ILE AAA O   1 ? 1  
ATOM 4456  C CB  . ILE C 1 135 ? 52.148  43.018  45.963 1.000 83.315  0 135 ILE AAA CB  1 ? 1  
ATOM 4457  C CG1 . ILE C 1 135 ? 52.798  44.394  45.735 1.000 81.683  0 135 ILE AAA CG1 1 ? 1  
ATOM 4458  C CG2 . ILE C 1 135 ? 50.749  43.161  46.524 1.000 91.257  0 135 ILE AAA CG2 1 ? 1  
ATOM 4459  C CD1 . ILE C 1 135 ? 52.214  45.205  44.578 1.000 96.848  0 135 ILE AAA CD1 1 ? 1  
ATOM 4460  N N   . LEU C 1 136 ? 52.181  39.865  46.839 1.000 95.502  0 136 LEU AAA N   1 ? 1  
ATOM 4461  C CA  . LEU C 1 136 ? 51.609  38.676  47.478 1.000 99.361  0 136 LEU AAA CA  1 ? 1  
ATOM 4462  C C   . LEU C 1 136 ? 52.349  38.323  48.760 1.000 106.456 0 136 LEU AAA C   1 ? 1  
ATOM 4463  O O   . LEU C 1 136 ? 51.725  37.992  49.776 1.000 117.362 0 136 LEU AAA O   1 ? 1  
ATOM 4464  C CB  . LEU C 1 136 ? 51.556  37.478  46.527 1.000 95.551  0 136 LEU AAA CB  1 ? 1  
ATOM 4465  C CG  . LEU C 1 136 ? 50.474  37.432  45.435 1.000 111.879 0 136 LEU AAA CG  1 ? 1  
ATOM 4466  C CD1 . LEU C 1 136 ? 49.112  37.285  46.116 1.000 124.613 0 136 LEU AAA CD1 1 ? 1  
ATOM 4467  C CD2 . LEU C 1 136 ? 50.413  38.618  44.512 1.000 112.069 0 136 LEU AAA CD2 1 ? 1  
ATOM 4468  N N   . GLY C 1 137 ? 53.680  38.380  48.726 1.000 108.711 0 137 GLY AAA N   1 ? 1  
ATOM 4469  C CA  . GLY C 1 137 ? 54.457  38.112  49.924 1.000 111.437 0 137 GLY AAA CA  1 ? 1  
ATOM 4470  C C   . GLY C 1 137 ? 54.227  39.135  51.021 1.000 112.573 0 137 GLY AAA C   1 ? 1  
ATOM 4471  O O   . GLY C 1 137 ? 54.079  38.774  52.192 1.000 117.215 0 137 GLY AAA O   1 ? 1  
ATOM 4472  N N   . LEU C 1 138 ? 54.191  40.423  50.661 1.000 109.908 0 138 LEU AAA N   1 ? 1  
ATOM 4473  C CA  . LEU C 1 138 ? 53.966  41.469  51.658 1.000 103.558 0 138 LEU AAA CA  1 ? 1  
ATOM 4474  C C   . LEU C 1 138 ? 52.592  41.353  52.316 1.000 109.563 0 138 LEU AAA C   1 ? 1  
ATOM 4475  O O   . LEU C 1 138 ? 52.455  41.594  53.521 1.000 118.051 0 138 LEU AAA O   1 ? 1  
ATOM 4476  C CB  . LEU C 1 138 ? 54.135  42.847  51.020 1.000 87.755  0 138 LEU AAA CB  1 ? 1  
ATOM 4477  C CG  . LEU C 1 138 ? 55.559  43.207  50.583 1.000 85.864  0 138 LEU AAA CG  1 ? 1  
ATOM 4478  C CD1 . LEU C 1 138 ? 55.588  44.509  49.794 1.000 83.931  0 138 LEU AAA CD1 1 ? 1  
ATOM 4479  C CD2 . LEU C 1 138 ? 56.487  43.273  51.779 1.000 96.509  0 138 LEU AAA CD2 1 ? 1  
ATOM 4480  N N   . ASN C 1 139 ? 51.561  41.005  51.543 1.000 113.269 0 139 ASN AAA N   1 ? 1  
ATOM 4481  C CA  . ASN C 1 139 ? 50.235  40.798  52.122 1.000 116.737 0 139 ASN AAA CA  1 ? 1  
ATOM 4482  C C   . ASN C 1 139 ? 50.261  39.786  53.260 1.000 123.143 0 139 ASN AAA C   1 ? 1  
ATOM 4483  O O   . ASN C 1 139 ? 49.637  40.005  54.306 1.000 136.444 0 139 ASN AAA O   1 ? 1  
ATOM 4484  C CB  . ASN C 1 139 ? 49.236  40.410  51.034 1.000 119.525 0 139 ASN AAA CB  1 ? 1  
ATOM 4485  C CG  . ASN C 1 139 ? 48.907  41.584  50.115 1.000 122.984 0 139 ASN AAA CG  1 ? 1  
ATOM 4486  O OD1 . ASN C 1 139 ? 49.727  42.479  49.917 1.000 120.293 0 139 ASN AAA OD1 1 ? 1  
ATOM 4487  N ND2 . ASN C 1 139 ? 47.700  41.584  49.553 1.000 133.712 0 139 ASN AAA ND2 1 ? 1  
ATOM 4488  N N   . LYS C 1 140 ? 50.961  38.666  53.075 1.000 112.512 0 140 LYS AAA N   1 ? 1  
ATOM 4489  C CA  . LYS C 1 140 ? 51.030  37.676  54.145 1.000 122.979 0 140 LYS AAA CA  1 ? 1  
ATOM 4490  C C   . LYS C 1 140 ? 51.709  38.249  55.379 1.000 117.886 0 140 LYS AAA C   1 ? 1  
ATOM 4491  O O   . LYS C 1 140 ? 51.276  37.997  56.510 1.000 126.713 0 140 LYS AAA O   1 ? 1  
ATOM 4492  C CB  . LYS C 1 140 ? 51.751  36.399  53.706 1.000 129.084 0 140 LYS AAA CB  1 ? 1  
ATOM 4493  C CG  . LYS C 1 140 ? 51.029  35.515  52.681 1.000 139.009 0 140 LYS AAA CG  1 ? 1  
ATOM 4494  C CD  . LYS C 1 140 ? 52.013  34.539  52.049 1.000 141.555 0 140 LYS AAA CD  1 ? 1  
ATOM 4495  C CE  . LYS C 1 140 ? 51.278  33.439  51.272 1.000 145.310 0 140 LYS AAA CE  1 ? 1  
ATOM 4496  N NZ  . LYS C 1 140 ? 52.222  32.551  50.538 1.000 150.972 0 140 LYS AAA NZ  1 ? 1  
ATOM 4497  N N   . ILE C 1 141 ? 52.766  39.030  55.176 1.000 112.394 0 141 ILE AAA N   1 ? 1  
ATOM 4498  C CA  . ILE C 1 141 ? 53.490  39.628  56.292 1.000 115.071 0 141 ILE AAA CA  1 ? 1  
ATOM 4499  C C   . ILE C 1 141 ? 52.610  40.613  57.050 1.000 121.814 0 141 ILE AAA C   1 ? 1  
ATOM 4500  O O   . ILE C 1 141 ? 52.571  40.601  58.285 1.000 138.192 0 141 ILE AAA O   1 ? 1  
ATOM 4501  C CB  . ILE C 1 141 ? 54.786  40.287  55.794 1.000 111.226 0 141 ILE AAA CB  1 ? 1  
ATOM 4502  C CG1 . ILE C 1 141 ? 55.732  39.213  55.266 1.000 108.532 0 141 ILE AAA CG1 1 ? 1  
ATOM 4503  C CG2 . ILE C 1 141 ? 55.439  41.113  56.894 1.000 112.299 0 141 ILE AAA CG2 1 ? 1  
ATOM 4504  C CD1 . ILE C 1 141 ? 56.787  39.740  54.349 1.000 109.572 0 141 ILE AAA CD1 1 ? 1  
ATOM 4505  N N   . VAL C 1 142 ? 51.893  41.477  56.331 1.000 118.935 0 142 VAL AAA N   1 ? 1  
ATOM 4506  C CA  . VAL C 1 142 ? 50.990  42.422  56.989 1.000 116.027 0 142 VAL AAA CA  1 ? 1  
ATOM 4507  C C   . VAL C 1 142 ? 49.977  41.689  57.855 1.000 122.863 0 142 VAL AAA C   1 ? 1  
ATOM 4508  O O   . VAL C 1 142 ? 49.691  42.090  58.991 1.000 128.476 0 142 VAL AAA O   1 ? 1  
ATOM 4509  C CB  . VAL C 1 142 ? 50.297  43.304  55.939 1.000 107.888 0 142 VAL AAA CB  1 ? 1  
ATOM 4510  C CG1 . VAL C 1 142 ? 49.152  44.065  56.560 1.000 111.275 0 142 VAL AAA CG1 1 ? 1  
ATOM 4511  C CG2 . VAL C 1 142 ? 51.296  44.263  55.348 1.000 110.816 0 142 VAL AAA CG2 1 ? 1  
ATOM 4512  N N   . ARG C 1 143 ? 49.444  40.591  57.341 1.000 121.511 0 143 ARG AAA N   1 ? 1  
ATOM 4513  C CA  . ARG C 1 143 ? 48.468  39.800  58.076 1.000 130.941 0 143 ARG AAA CA  1 ? 1  
ATOM 4514  C C   . ARG C 1 143 ? 49.102  39.174  59.312 1.000 135.477 0 143 ARG AAA C   1 ? 1  
ATOM 4515  O O   . ARG C 1 143 ? 48.489  39.158  60.388 1.000 146.828 0 143 ARG AAA O   1 ? 1  
ATOM 4516  C CB  . ARG C 1 143 ? 47.816  38.830  57.094 1.000 141.762 0 143 ARG AAA CB  1 ? 1  
ATOM 4517  C CG  . ARG C 1 143 ? 46.688  37.966  57.579 1.000 157.197 0 143 ARG AAA CG  1 ? 1  
ATOM 4518  C CD  . ARG C 1 143 ? 46.069  37.363  56.336 1.000 174.643 0 143 ARG AAA CD  1 ? 1  
ATOM 4519  N NE  . ARG C 1 143 ? 46.951  36.527  55.541 1.000 172.930 0 143 ARG AAA NE  1 ? 1  
ATOM 4520  C CZ  . ARG C 1 143 ? 46.585  35.918  54.424 1.000 184.399 0 143 ARG AAA CZ  1 ? 1  
ATOM 4521  N NH1 . ARG C 1 143 ? 45.353  36.034  53.949 1.000 196.948 0 143 ARG AAA NH1 1 ? 1  
ATOM 4522  N NH2 . ARG C 1 143 ? 47.475  35.196  53.756 1.000 180.676 0 143 ARG AAA NH2 1 ? 1  
ATOM 4523  N N   . MET C 1 144 ? 50.321  38.636  59.181 1.000 139.452 0 144 MET AAA N   1 ? 1  
ATOM 4524  C CA  . MET C 1 144 ? 50.983  38.009  60.323 1.000 144.857 0 144 MET AAA CA  1 ? 1  
ATOM 4525  C C   . MET C 1 144 ? 51.220  39.036  61.413 1.000 150.119 0 144 MET AAA C   1 ? 1  
ATOM 4526  O O   . MET C 1 144 ? 51.125  38.722  62.601 1.000 158.440 0 144 MET AAA O   1 ? 1  
ATOM 4527  C CB  . MET C 1 144 ? 52.282  37.332  59.913 1.000 149.377 0 144 MET AAA CB  1 ? 1  
ATOM 4528  C CG  . MET C 1 144 ? 52.014  36.065  59.164 1.000 158.656 0 144 MET AAA CG  1 ? 1  
ATOM 4529  S SD  . MET C 1 144 ? 53.455  35.281  58.465 1.000 173.123 0 144 MET AAA SD  1 ? 1  
ATOM 4530  C CE  . MET C 1 144 ? 52.573  34.047  57.531 1.000 165.356 0 144 MET AAA CE  1 ? 1  
ATOM 4531  N N   . TYR C 1 145 ? 51.535  40.267  61.022 1.000 140.617 0 145 TYR AAA N   1 ? 1  
ATOM 4532  C CA  . TYR C 1 145 ? 51.884  41.344  61.935 1.000 147.109 0 145 TYR AAA CA  1 ? 1  
ATOM 4533  C C   . TYR C 1 145 ? 50.662  42.113  62.409 1.000 150.066 0 145 TYR AAA C   1 ? 1  
ATOM 4534  O O   . TYR C 1 145 ? 50.822  43.108  63.121 1.000 150.679 0 145 TYR AAA O   1 ? 1  
ATOM 4535  C CB  . TYR C 1 145 ? 52.874  42.324  61.286 1.000 148.896 0 145 TYR AAA CB  1 ? 1  
ATOM 4536  C CG  . TYR C 1 145 ? 54.297  41.834  61.119 1.000 145.691 0 145 TYR AAA CG  1 ? 1  
ATOM 4537  C CD1 . TYR C 1 145 ? 54.589  40.521  60.773 1.000 144.532 0 145 TYR AAA CD1 1 ? 1  
ATOM 4538  C CD2 . TYR C 1 145 ? 55.359  42.710  61.317 1.000 147.178 0 145 TYR AAA CD2 1 ? 1  
ATOM 4539  C CE1 . TYR C 1 145 ? 55.901  40.097  60.638 1.000 148.436 0 145 TYR AAA CE1 1 ? 1  
ATOM 4540  C CE2 . TYR C 1 145 ? 56.668  42.300  61.179 1.000 151.893 0 145 TYR AAA CE2 1 ? 1  
ATOM 4541  C CZ  . TYR C 1 145 ? 56.944  40.984  60.858 1.000 155.544 0 145 TYR AAA CZ  1 ? 1  
ATOM 4542  O OH  . TYR C 1 145 ? 58.249  40.589  60.706 1.000 155.721 0 145 TYR AAA OH  1 ? 1  
ATOM 4543  N N   . SER C 1 146 ? 49.461  41.695  62.011 1.000 155.291 0 146 SER AAA N   1 ? 2  
ATOM 4544  C CA  . SER C 1 146 ? 48.245  42.282  62.560 1.000 156.614 0 146 SER AAA CA  1 ? 2  
ATOM 4545  C C   . SER C 1 146 ? 48.260  41.998  64.058 1.000 153.786 0 146 SER AAA C   1 ? 2  
ATOM 4546  O O   . SER C 1 146 ? 48.299  40.824  64.459 1.000 143.515 0 146 SER AAA O   1 ? 2  
ATOM 4547  C CB  . SER C 1 146 ? 47.004  41.680  61.896 1.000 148.418 0 146 SER AAA CB  1 ? 2  
ATOM 4548  O OG  . SER C 1 146 ? 45.801  42.232  62.403 1.000 142.851 0 146 SER AAA OG  1 ? 2  
ATOM 4549  N N   . PRO C 1 147 ? 48.229  43.024  64.915 1.000 151.517 0 147 PRO AAA N   1 ? 2  
ATOM 4550  C CA  . PRO C 1 147 ? 48.402  42.774  66.354 1.000 155.059 0 147 PRO AAA CA  1 ? 2  
ATOM 4551  C C   . PRO C 1 147 ? 47.190  42.189  67.045 1.000 161.506 0 147 PRO AAA C   1 ? 2  
ATOM 4552  O O   . PRO C 1 147 ? 47.342  41.606  68.127 1.000 183.190 0 147 PRO AAA O   1 ? 2  
ATOM 4553  C CB  . PRO C 1 147 ? 48.708  44.175  66.915 1.000 153.513 0 147 PRO AAA CB  1 ? 2  
ATOM 4554  C CG  . PRO C 1 147 ? 49.065  45.021  65.702 1.000 160.680 0 147 PRO AAA CG  1 ? 2  
ATOM 4555  C CD  . PRO C 1 147 ? 48.233  44.460  64.599 1.000 155.143 0 147 PRO AAA CD  1 ? 2  
ATOM 4556  N N   . THR C 1 148 ? 46.003  42.317  66.471 1.000 156.743 0 148 THR AAA N   1 ? 2  
ATOM 4557  C CA  . THR C 1 148 ? 44.794  41.918  67.168 1.000 158.388 0 148 THR AAA CA  1 ? 2  
ATOM 4558  C C   . THR C 1 148 ? 43.884  41.168  66.212 1.000 158.169 0 148 THR AAA C   1 ? 2  
ATOM 4559  O O   . THR C 1 148 ? 43.780  41.524  65.035 1.000 154.529 0 148 THR AAA O   1 ? 2  
ATOM 4560  C CB  . THR C 1 148 ? 44.051  43.118  67.768 1.000 158.084 0 148 THR AAA CB  1 ? 2  
ATOM 4561  O OG1 . THR C 1 148 ? 45.001  44.087  68.225 1.000 157.277 0 148 THR AAA OG1 1 ? 2  
ATOM 4562  C CG2 . THR C 1 148 ? 43.206  42.666  68.951 1.000 166.589 0 148 THR AAA CG2 1 ? 2  
ATOM 4563  N N   . SER C 1 149 ? 43.243  40.120  66.715 1.000 167.132 0 149 SER AAA N   1 ? 2  
ATOM 4564  C CA  . SER C 1 149 ? 42.209  39.475  65.930 1.000 166.373 0 149 SER AAA CA  1 ? 2  
ATOM 4565  C C   . SER C 1 149 ? 40.947  40.321  66.020 1.000 160.780 0 149 SER AAA C   1 ? 2  
ATOM 4566  O O   . SER C 1 149 ? 40.664  40.934  67.055 1.000 159.563 0 149 SER AAA O   1 ? 2  
ATOM 4567  C CB  . SER C 1 149 ? 41.944  38.056  66.434 1.000 166.361 0 149 SER AAA CB  1 ? 2  
ATOM 4568  O OG  . SER C 1 149 ? 40.705  37.558  65.953 1.000 160.550 0 149 SER AAA OG  1 ? 2  
ATOM 4569  N N   . ILE C 1 150 ? 40.193  40.360  64.918 1.000 149.965 0 150 ILE AAA N   1 ? 2  
ATOM 4570  C CA  A ILE C 1 150 ? 38.986  41.185  64.868 1.000 144.399 0 150 ILE AAA CA  1 ? 2  
ATOM 4571  C C   . ILE C 1 150 ? 38.056  40.857  66.026 1.000 156.482 0 150 ILE AAA C   1 ? 2  
ATOM 4572  O O   . ILE C 1 150 ? 37.380  41.739  66.572 1.000 155.386 0 150 ILE AAA O   1 ? 2  
ATOM 4573  C CB  A ILE C 1 150 ? 38.272  41.018  63.512 1.000 138.169 0 150 ILE AAA CB  1 ? 2  
ATOM 4574  C CG1 A ILE C 1 150 ? 37.049  41.936  63.451 1.000 139.505 0 150 ILE AAA CG1 1 ? 2  
ATOM 4575  C CG2 A ILE C 1 150 ? 37.896  39.557  63.265 1.000 139.414 0 150 ILE AAA CG2 1 ? 2  
ATOM 4576  C CD1 A ILE C 1 150 ? 36.271  41.821  62.189 1.000 138.547 0 150 ILE AAA CD1 1 ? 2  
ATOM 4577  N N   . LEU C 1 151 ? 38.005  39.585  66.410 1.000 157.375 0 151 LEU AAA N   1 ? 2  
ATOM 4578  C CA  . LEU C 1 151 ? 37.087  39.123  67.443 1.000 150.744 0 151 LEU AAA CA  1 ? 2  
ATOM 4579  C C   . LEU C 1 151 ? 37.337  39.802  68.785 1.000 151.179 0 151 LEU AAA C   1 ? 2  
ATOM 4580  O O   . LEU C 1 151 ? 36.416  39.873  69.613 1.000 160.504 0 151 LEU AAA O   1 ? 2  
ATOM 4581  C CB  . LEU C 1 151 ? 37.234  37.609  67.594 1.000 152.633 0 151 LEU AAA CB  1 ? 2  
ATOM 4582  C CG  . LEU C 1 151 ? 37.145  36.795  66.298 1.000 158.589 0 151 LEU AAA CG  1 ? 2  
ATOM 4583  C CD1 . LEU C 1 151 ? 37.292  35.309  66.597 1.000 169.083 0 151 LEU AAA CD1 1 ? 2  
ATOM 4584  C CD2 . LEU C 1 151 ? 35.856  37.089  65.559 1.000 159.080 0 151 LEU AAA CD2 1 ? 2  
ATOM 4585  N N   . ASP C 1 152 ? 38.551  40.310  69.010 1.000 156.139 0 152 ASP AAA N   1 ? 2  
ATOM 4586  C CA  . ASP C 1 152 ? 38.942  40.975  70.260 1.000 153.604 0 152 ASP AAA CA  1 ? 2  
ATOM 4587  C C   . ASP C 1 152 ? 38.852  42.498  70.212 1.000 144.328 0 152 ASP AAA C   1 ? 2  
ATOM 4588  O O   . ASP C 1 152 ? 39.224  43.152  71.192 1.000 142.399 0 152 ASP AAA O   1 ? 2  
ATOM 4589  C CB  . ASP C 1 152 ? 40.361  40.549  70.656 1.000 161.178 0 152 ASP AAA CB  1 ? 2  
ATOM 4590  C CG  . ASP C 1 152 ? 40.440  39.083  71.047 1.000 169.457 0 152 ASP AAA CG  1 ? 2  
ATOM 4591  O OD1 . ASP C 1 152 ? 39.472  38.568  71.640 1.000 162.492 0 152 ASP AAA OD1 1 ? 2  
ATOM 4592  O OD2 . ASP C 1 152 ? 41.465  38.440  70.735 1.000 182.233 0 152 ASP AAA OD2 1 ? 2  
ATOM 4593  N N   . ILE C 1 153 ? 38.400  43.081  69.106 1.000 142.470 0 153 ILE AAA N   1 ? 2  
ATOM 4594  C CA  . ILE C 1 153 ? 38.194  44.524  69.034 1.000 148.291 0 153 ILE AAA CA  1 ? 2  
ATOM 4595  C C   . ILE C 1 153 ? 36.778  44.813  69.521 1.000 149.298 0 153 ILE AAA C   1 ? 2  
ATOM 4596  O O   . ILE C 1 153 ? 35.808  44.573  68.799 1.000 147.564 0 153 ILE AAA O   1 ? 2  
ATOM 4597  C CB  . ILE C 1 153 ? 38.408  45.047  67.611 1.000 153.211 0 153 ILE AAA CB  1 ? 2  
ATOM 4598  C CG1 . ILE C 1 153 ? 39.784  44.641  67.092 1.000 153.520 0 153 ILE AAA CG1 1 ? 2  
ATOM 4599  C CG2 . ILE C 1 153 ? 38.240  46.559  67.565 1.000 149.959 0 153 ILE AAA CG2 1 ? 2  
ATOM 4600  C CD1 . ILE C 1 153 ? 40.924  45.255  67.861 1.000 152.165 0 153 ILE AAA CD1 1 ? 2  
ATOM 4601  N N   . ARG C 1 154 ? 36.661  45.338  70.742 1.000 152.749 0 154 ARG AAA N   1 ? 2  
ATOM 4602  C CA  . ARG C 1 154 ? 35.375  45.637  71.362 1.000 158.131 0 154 ARG AAA CA  1 ? 2  
ATOM 4603  C C   . ARG C 1 154 ? 35.402  47.054  71.915 1.000 155.245 0 154 ARG AAA C   1 ? 2  
ATOM 4604  O O   . ARG C 1 154 ? 36.414  47.491  72.471 1.000 159.150 0 154 ARG AAA O   1 ? 2  
ATOM 4605  C CB  . ARG C 1 154 ? 35.038  44.634  72.484 1.000 164.212 0 154 ARG AAA CB  1 ? 2  
ATOM 4606  C CG  . ARG C 1 154 ? 35.412  43.192  72.152 1.000 170.791 0 154 ARG AAA CG  1 ? 2  
ATOM 4607  C CD  . ARG C 1 154 ? 34.992  42.206  73.230 1.000 173.452 0 154 ARG AAA CD  1 ? 2  
ATOM 4608  N NE  . ARG C 1 154 ? 33.626  41.731  73.046 1.000 191.102 0 154 ARG AAA NE  1 ? 2  
ATOM 4609  C CZ  . ARG C 1 154 ? 32.564  42.247  73.649 1.000 201.671 0 154 ARG AAA CZ  1 ? 2  
ATOM 4610  N NH1 . ARG C 1 154 ? 32.673  43.262  74.490 1.000 207.801 0 154 ARG AAA NH1 1 ? 2  
ATOM 4611  N NH2 . ARG C 1 154 ? 31.364  41.727  73.409 1.000 204.229 0 154 ARG AAA NH2 1 ? 2  
ATOM 4612  N N   . GLN C 1 155 ? 34.290  47.770  71.757 1.000 158.666 0 155 GLN AAA N   1 ? 2  
ATOM 4613  C CA  . GLN C 1 155 ? 34.238  49.175  72.140 1.000 165.089 0 155 GLN AAA CA  1 ? 2  
ATOM 4614  C C   . GLN C 1 155 ? 34.261  49.354  73.651 1.000 176.521 0 155 GLN AAA C   1 ? 2  
ATOM 4615  O O   . GLN C 1 155 ? 33.504  48.703  74.377 1.000 188.027 0 155 GLN AAA O   1 ? 2  
ATOM 4616  C CB  . GLN C 1 155 ? 32.981  49.836  71.580 1.000 169.897 0 155 GLN AAA CB  1 ? 2  
ATOM 4617  C CG  . GLN C 1 155 ? 32.960  51.348  71.771 1.000 176.356 0 155 GLN AAA CG  1 ? 2  
ATOM 4618  C CD  . GLN C 1 155 ? 31.652  51.979  71.335 1.000 180.202 0 155 GLN AAA CD  1 ? 2  
ATOM 4619  O OE1 . GLN C 1 155 ? 30.665  51.285  71.086 1.000 180.989 0 155 GLN AAA OE1 1 ? 2  
ATOM 4620  N NE2 . GLN C 1 155 ? 31.631  53.306  71.258 1.000 172.366 0 155 GLN AAA NE2 1 ? 2  
ATOM 4621  N N   . GLY C 1 156 ? 35.134  50.242  74.119 1.000 190.977 0 156 GLY AAA N   1 ? 2  
ATOM 4622  C CA  . GLY C 1 156 ? 35.200  50.587  75.517 1.000 211.475 0 156 GLY AAA CA  1 ? 2  
ATOM 4623  C C   . GLY C 1 156 ? 33.979  51.397  75.897 1.000 220.965 0 156 GLY AAA C   1 ? 2  
ATOM 4624  O O   . GLY C 1 156 ? 33.315  51.986  75.037 1.000 234.847 0 156 GLY AAA O   1 ? 2  
ATOM 4625  N N   . PRO C 1 157 ? 33.642  51.439  77.187 1.000 222.120 0 157 PRO AAA N   1 ? 2  
ATOM 4626  C CA  A PRO C 1 157 ? 32.496  52.266  77.592 1.000 218.316 0 157 PRO AAA CA  1 ? 2  
ATOM 4627  C C   . PRO C 1 157 ? 32.715  53.741  77.334 1.000 219.281 0 157 PRO AAA C   1 ? 2  
ATOM 4628  O O   . PRO C 1 157 ? 31.754  54.459  77.036 1.000 212.596 0 157 PRO AAA O   1 ? 2  
ATOM 4629  C CB  A PRO C 1 157 ? 32.345  51.975  79.091 1.000 223.555 0 157 PRO AAA CB  1 ? 2  
ATOM 4630  C CG  A PRO C 1 157 ? 33.195  50.790  79.371 1.000 220.673 0 157 PRO AAA CG  1 ? 2  
ATOM 4631  C CD  A PRO C 1 157 ? 34.249  50.720  78.318 1.000 215.288 0 157 PRO AAA CD  1 ? 2  
ATOM 4632  N N   . LYS C 1 158 ? 33.944  54.232  77.438 1.000 221.028 0 158 LYS AAA N   1 ? 2  
ATOM 4633  C CA  . LYS C 1 158 ? 34.164  55.650  77.228 1.000 227.165 0 158 LYS AAA CA  1 ? 2  
ATOM 4634  C C   . LYS C 1 158 ? 34.703  55.943  75.838 1.000 223.999 0 158 LYS AAA C   1 ? 2  
ATOM 4635  O O   . LYS C 1 158 ? 35.093  57.082  75.565 1.000 231.070 0 158 LYS AAA O   1 ? 2  
ATOM 4636  C CB  . LYS C 1 158 ? 35.178  56.157  78.252 1.000 241.079 0 158 LYS AAA CB  1 ? 2  
ATOM 4637  C CG  . LYS C 1 158 ? 36.521  55.423  78.096 1.000 247.738 0 158 LYS AAA CG  1 ? 2  
ATOM 4638  C CD  . LYS C 1 158 ? 36.638  54.135  78.917 1.000 256.114 0 158 LYS AAA CD  1 ? 2  
ATOM 4639  C CE  . LYS C 1 158 ? 37.976  53.418  78.684 1.000 254.440 0 158 LYS AAA CE  1 ? 2  
ATOM 4640  N NZ  . LYS C 1 158 ? 38.136  52.188  79.527 1.000 263.792 0 158 LYS AAA NZ  1 ? 2  
ATOM 4641  N N   . GLU C 1 159 ? 34.765  54.940  74.967 1.000 208.338 0 159 GLU AAA N   1 ? 2  
ATOM 4642  C CA  . GLU C 1 159 ? 35.320  55.146  73.638 1.000 183.907 0 159 GLU AAA CA  1 ? 2  
ATOM 4643  C C   . GLU C 1 159 ? 34.271  55.720  72.691 1.000 173.396 0 159 GLU AAA C   1 ? 2  
ATOM 4644  O O   . GLU C 1 159 ? 33.195  55.129  72.546 1.000 169.402 0 159 GLU AAA O   1 ? 2  
ATOM 4645  C CB  . GLU C 1 159 ? 35.904  53.851  73.092 1.000 177.528 0 159 GLU AAA CB  1 ? 2  
ATOM 4646  C CG  . GLU C 1 159 ? 36.596  54.024  71.753 1.000 171.067 0 159 GLU AAA CG  1 ? 2  
ATOM 4647  C CD  . GLU C 1 159 ? 37.195  52.736  71.234 1.000 165.133 0 159 GLU AAA CD  1 ? 2  
ATOM 4648  O OE1 . GLU C 1 159 ? 36.790  51.653  71.708 1.000 171.437 0 159 GLU AAA OE1 1 ? 2  
ATOM 4649  O OE2 . GLU C 1 159 ? 38.092  52.811  70.369 1.000 156.328 0 159 GLU AAA OE2 1 ? 2  
ATOM 4650  N N   . PRO C 1 160 ? 34.525  56.860  72.055 1.000 170.127 0 160 PRO AAA N   1 ? 2  
ATOM 4651  C CA  . PRO C 1 160 ? 33.619  57.342  71.004 1.000 170.351 0 160 PRO AAA CA  1 ? 2  
ATOM 4652  C C   . PRO C 1 160 ? 33.432  56.287  69.920 1.000 167.454 0 160 PRO AAA C   1 ? 2  
ATOM 4653  O O   . PRO C 1 160 ? 34.377  55.586  69.550 1.000 172.583 0 160 PRO AAA O   1 ? 2  
ATOM 4654  C CB  . PRO C 1 160 ? 34.320  58.598  70.478 1.000 173.682 0 160 PRO AAA CB  1 ? 2  
ATOM 4655  C CG  . PRO C 1 160 ? 35.157  59.064  71.633 1.000 177.047 0 160 PRO AAA CG  1 ? 2  
ATOM 4656  C CD  . PRO C 1 160 ? 35.614  57.814  72.333 1.000 174.851 0 160 PRO AAA CD  1 ? 2  
ATOM 4657  N N   . PHE C 1 161 ? 32.192  56.152  69.434 1.000 153.576 0 161 PHE AAA N   1 ? 2  
ATOM 4658  C CA  . PHE C 1 161 ? 31.907  55.142  68.417 1.000 144.067 0 161 PHE AAA CA  1 ? 2  
ATOM 4659  C C   . PHE C 1 161 ? 32.851  55.290  67.233 1.000 137.568 0 161 PHE AAA C   1 ? 2  
ATOM 4660  O O   . PHE C 1 161 ? 33.348  54.294  66.695 1.000 134.502 0 161 PHE AAA O   1 ? 2  
ATOM 4661  C CB  . PHE C 1 161 ? 30.457  55.262  67.947 1.000 144.785 0 161 PHE AAA CB  1 ? 2  
ATOM 4662  C CG  . PHE C 1 161 ? 30.008  54.143  67.045 1.000 141.717 0 161 PHE AAA CG  1 ? 2  
ATOM 4663  C CD1 . PHE C 1 161 ? 30.412  52.836  67.268 1.000 144.310 0 161 PHE AAA CD1 1 ? 2  
ATOM 4664  C CD2 . PHE C 1 161 ? 29.207  54.411  65.948 1.000 134.980 0 161 PHE AAA CD2 1 ? 2  
ATOM 4665  C CE1 . PHE C 1 161 ? 29.990  51.814  66.432 1.000 137.784 0 161 PHE AAA CE1 1 ? 2  
ATOM 4666  C CE2 . PHE C 1 161 ? 28.791  53.397  65.106 1.000 132.420 0 161 PHE AAA CE2 1 ? 2  
ATOM 4667  C CZ  . PHE C 1 161 ? 29.185  52.098  65.349 1.000 133.227 0 161 PHE AAA CZ  1 ? 2  
ATOM 4668  N N   . ARG C 1 162 ? 33.135  56.535  66.837 1.000 138.789 0 162 ARG AAA N   1 ? 2  
ATOM 4669  C CA  . ARG C 1 162 ? 34.054  56.782  65.730 1.000 133.746 0 162 ARG AAA CA  1 ? 2  
ATOM 4670  C C   . ARG C 1 162 ? 35.418  56.146  65.967 1.000 131.073 0 162 ARG AAA C   1 ? 2  
ATOM 4671  O O   . ARG C 1 162 ? 35.996  55.556  65.048 1.000 129.718 0 162 ARG AAA O   1 ? 2  
ATOM 4672  C CB  . ARG C 1 162 ? 34.209  58.286  65.495 1.000 132.318 0 162 ARG AAA CB  1 ? 2  
ATOM 4673  C CG  . ARG C 1 162 ? 35.046  58.636  64.272 1.000 126.372 0 162 ARG AAA CG  1 ? 2  
ATOM 4674  C CD  . ARG C 1 162 ? 35.475  60.089  64.290 1.000 129.522 0 162 ARG AAA CD  1 ? 2  
ATOM 4675  N NE  . ARG C 1 162 ? 34.325  60.956  64.467 1.000 132.298 0 162 ARG AAA NE  1 ? 2  
ATOM 4676  C CZ  . ARG C 1 162 ? 34.374  62.280  64.559 1.000 138.879 0 162 ARG AAA CZ  1 ? 2  
ATOM 4677  N NH1 . ARG C 1 162 ? 35.538  62.913  64.478 1.000 140.323 0 162 ARG AAA NH1 1 ? 2  
ATOM 4678  N NH2 . ARG C 1 162 ? 33.247  62.967  64.719 1.000 145.651 0 162 ARG AAA NH2 1 ? 2  
ATOM 4679  N N   . ASP C 1 163 ? 35.945  56.239  67.194 1.000 134.968 0 163 ASP AAA N   1 ? 2  
ATOM 4680  C CA  . ASP C 1 163 ? 37.267  55.679  67.469 1.000 139.399 0 163 ASP AAA CA  1 ? 2  
ATOM 4681  C C   . ASP C 1 163 ? 37.249  54.152  67.440 1.000 135.491 0 163 ASP AAA C   1 ? 2  
ATOM 4682  O O   . ASP C 1 163 ? 38.211  53.528  66.977 1.000 138.534 0 163 ASP AAA O   1 ? 2  
ATOM 4683  C CB  . ASP C 1 163 ? 37.781  56.173  68.828 1.000 144.188 0 163 ASP AAA CB  1 ? 2  
ATOM 4684  C CG  . ASP C 1 163 ? 37.979  57.682  68.874 1.000 156.397 0 163 ASP AAA CG  1 ? 2  
ATOM 4685  O OD1 . ASP C 1 163 ? 38.178  58.303  67.810 1.000 166.599 0 163 ASP AAA OD1 1 ? 2  
ATOM 4686  O OD2 . ASP C 1 163 ? 37.901  58.252  69.985 1.000 163.858 0 163 ASP AAA OD2 1 ? 2  
ATOM 4687  N N   . TYR C 1 164 ? 36.179  53.532  67.936 1.000 131.527 0 164 TYR AAA N   1 ? 2  
ATOM 4688  C CA  . TYR C 1 164 ? 36.051  52.081  67.842 1.000 128.863 0 164 TYR AAA CA  1 ? 2  
ATOM 4689  C C   . TYR C 1 164 ? 35.960  51.623  66.387 1.000 125.638 0 164 TYR AAA C   1 ? 2  
ATOM 4690  O O   . TYR C 1 164 ? 36.636  50.671  65.972 1.000 123.481 0 164 TYR AAA O   1 ? 2  
ATOM 4691  C CB  . TYR C 1 164 ? 34.837  51.628  68.653 1.000 131.179 0 164 TYR AAA CB  1 ? 2  
ATOM 4692  C CG  . TYR C 1 164 ? 34.235  50.313  68.246 1.000 127.059 0 164 TYR AAA CG  1 ? 2  
ATOM 4693  C CD1 . TYR C 1 164 ? 34.943  49.133  68.400 1.000 132.274 0 164 TYR AAA CD1 1 ? 2  
ATOM 4694  C CD2 . TYR C 1 164 ? 32.950  50.248  67.732 1.000 125.823 0 164 TYR AAA CD2 1 ? 2  
ATOM 4695  C CE1 . TYR C 1 164 ? 34.395  47.926  68.042 1.000 138.619 0 164 TYR AAA CE1 1 ? 2  
ATOM 4696  C CE2 . TYR C 1 164 ? 32.390  49.045  67.369 1.000 124.778 0 164 TYR AAA CE2 1 ? 2  
ATOM 4697  C CZ  . TYR C 1 164 ? 33.117  47.886  67.526 1.000 134.364 0 164 TYR AAA CZ  1 ? 2  
ATOM 4698  O OH  . TYR C 1 164 ? 32.565  46.680  67.166 1.000 141.659 0 164 TYR AAA OH  1 ? 2  
ATOM 4699  N N   . VAL C 1 165 ? 35.136  52.307  65.591 1.000 122.471 0 165 VAL AAA N   1 ? 2  
ATOM 4700  C CA  . VAL C 1 165 ? 34.986  51.954  64.183 1.000 118.444 0 165 VAL AAA CA  1 ? 2  
ATOM 4701  C C   . VAL C 1 165 ? 36.297  52.132  63.425 1.000 117.103 0 165 VAL AAA C   1 ? 2  
ATOM 4702  O O   . VAL C 1 165 ? 36.656  51.295  62.587 1.000 112.959 0 165 VAL AAA O   1 ? 2  
ATOM 4703  C CB  . VAL C 1 165 ? 33.849  52.768  63.543 1.000 119.595 0 165 VAL AAA CB  1 ? 2  
ATOM 4704  C CG1 . VAL C 1 165 ? 33.740  52.426  62.079 1.000 124.213 0 165 VAL AAA CG1 1 ? 2  
ATOM 4705  C CG2 . VAL C 1 165 ? 32.545  52.453  64.226 1.000 125.547 0 165 VAL AAA CG2 1 ? 2  
ATOM 4706  N N   . ASP C 1 166 ? 37.041  53.208  63.714 1.000 115.864 0 166 ASP AAA N   1 ? 2  
ATOM 4707  C CA  . ASP C 1 166 ? 38.376  53.364  63.137 1.000 117.936 0 166 ASP AAA CA  1 ? 2  
ATOM 4708  C C   . ASP C 1 166 ? 39.243  52.145  63.439 1.000 122.231 0 166 ASP AAA C   1 ? 2  
ATOM 4709  O O   . ASP C 1 166 ? 39.928  51.617  62.555 1.000 126.889 0 166 ASP AAA O   1 ? 2  
ATOM 4710  C CB  . ASP C 1 166 ? 39.043  54.643  63.667 1.000 119.963 0 166 ASP AAA CB  1 ? 2  
ATOM 4711  C CG  . ASP C 1 166 ? 38.568  55.915  62.956 1.000 121.030 0 166 ASP AAA CG  1 ? 2  
ATOM 4712  O OD1 . ASP C 1 166 ? 37.974  55.825  61.862 1.000 117.291 0 166 ASP AAA OD1 1 ? 2  
ATOM 4713  O OD2 . ASP C 1 166 ? 38.776  57.016  63.515 1.000 125.807 0 166 ASP AAA OD2 1 ? 2  
ATOM 4714  N N   . ARG C 1 167 ? 39.245  51.701  64.696 1.000 120.626 0 167 ARG AAA N   1 ? 2  
ATOM 4715  C CA  . ARG C 1 167 ? 40.034  50.531  65.068 1.000 120.962 0 167 ARG AAA CA  1 ? 2  
ATOM 4716  C C   . ARG C 1 167 ? 39.511  49.276  64.375 1.000 117.372 0 167 ARG AAA C   1 ? 2  
ATOM 4717  O O   . ARG C 1 167 ? 40.294  48.421  63.942 1.000 121.084 0 167 ARG AAA O   1 ? 2  
ATOM 4718  C CB  . ARG C 1 167 ? 40.065  50.359  66.585 1.000 125.294 0 167 ARG AAA CB  1 ? 2  
ATOM 4719  C CG  . ARG C 1 167 ? 40.847  51.463  67.284 1.000 130.639 0 167 ARG AAA CG  1 ? 2  
ATOM 4720  C CD  . ARG C 1 167 ? 41.109  51.141  68.746 1.000 138.763 0 167 ARG AAA CD  1 ? 2  
ATOM 4721  N NE  . ARG C 1 167 ? 39.894  50.846  69.494 1.000 145.403 0 167 ARG AAA NE  1 ? 2  
ATOM 4722  C CZ  . ARG C 1 167 ? 39.599  49.651  69.988 1.000 148.889 0 167 ARG AAA CZ  1 ? 2  
ATOM 4723  N NH1 . ARG C 1 167 ? 40.413  48.619  69.832 1.000 149.933 0 167 ARG AAA NH1 1 ? 2  
ATOM 4724  N NH2 . ARG C 1 167 ? 38.466  49.489  70.666 1.000 145.789 0 167 ARG AAA NH2 1 ? 2  
ATOM 4725  N N   . PHE C 1 168 ? 38.186  49.154  64.268 1.000 110.057 0 168 PHE AAA N   1 ? 2  
ATOM 4726  C CA  . PHE C 1 168 ? 37.573  47.960  63.695 1.000 113.844 0 168 PHE AAA CA  1 ? 2  
ATOM 4727  C C   . PHE C 1 168 ? 38.004  47.728  62.252 1.000 120.372 0 168 PHE AAA C   1 ? 2  
ATOM 4728  O O   . PHE C 1 168 ? 38.492  46.644  61.911 1.000 126.199 0 168 PHE AAA O   1 ? 2  
ATOM 4729  C CB  . PHE C 1 168 ? 36.052  48.072  63.783 1.000 115.692 0 168 PHE AAA CB  1 ? 2  
ATOM 4730  C CG  . PHE C 1 168 ? 35.326  46.838  63.329 1.000 125.601 0 168 PHE AAA CG  1 ? 2  
ATOM 4731  C CD1 . PHE C 1 168 ? 34.978  46.670  61.996 1.000 127.314 0 168 PHE AAA CD1 1 ? 2  
ATOM 4732  C CD2 . PHE C 1 168 ? 35.009  45.835  64.228 1.000 129.936 0 168 PHE AAA CD2 1 ? 2  
ATOM 4733  C CE1 . PHE C 1 168 ? 34.316  45.535  61.576 1.000 129.500 0 168 PHE AAA CE1 1 ? 2  
ATOM 4734  C CE2 . PHE C 1 168 ? 34.348  44.697  63.812 1.000 132.482 0 168 PHE AAA CE2 1 ? 2  
ATOM 4735  C CZ  . PHE C 1 168 ? 34.001  44.547  62.486 1.000 130.903 0 168 PHE AAA CZ  1 ? 2  
ATOM 4736  N N   . TYR C 1 169 ? 37.853  48.729  61.388 1.000 120.358 0 169 TYR AAA N   1 ? 2  
ATOM 4737  C CA  . TYR C 1 169 ? 38.197  48.509  59.988 1.000 118.977 0 169 TYR AAA CA  1 ? 2  
ATOM 4738  C C   . TYR C 1 169 ? 39.697  48.483  59.741 1.000 122.569 0 169 TYR AAA C   1 ? 2  
ATOM 4739  O O   . TYR C 1 169 ? 40.129  47.901  58.740 1.000 123.494 0 169 TYR AAA O   1 ? 2  
ATOM 4740  C CB  . TYR C 1 169 ? 37.545  49.566  59.098 1.000 120.488 0 169 TYR AAA CB  1 ? 2  
ATOM 4741  C CG  . TYR C 1 169 ? 36.074  49.324  58.875 1.000 122.118 0 169 TYR AAA CG  1 ? 2  
ATOM 4742  C CD1 . TYR C 1 169 ? 35.647  48.339  57.993 1.000 131.132 0 169 TYR AAA CD1 1 ? 2  
ATOM 4743  C CD2 . TYR C 1 169 ? 35.114  50.078  59.532 1.000 117.274 0 169 TYR AAA CD2 1 ? 2  
ATOM 4744  C CE1 . TYR C 1 169 ? 34.308  48.107  57.773 1.000 132.420 0 169 TYR AAA CE1 1 ? 2  
ATOM 4745  C CE2 . TYR C 1 169 ? 33.768  49.852  59.319 1.000 125.217 0 169 TYR AAA CE2 1 ? 2  
ATOM 4746  C CZ  . TYR C 1 169 ? 33.372  48.866  58.438 1.000 128.989 0 169 TYR AAA CZ  1 ? 2  
ATOM 4747  O OH  . TYR C 1 169 ? 32.035  48.632  58.220 1.000 137.194 0 169 TYR AAA OH  1 ? 2  
ATOM 4748  N N   . LYS C 1 170 ? 40.496  49.106  60.608 1.000 121.462 0 170 LYS AAA N   1 ? 2  
ATOM 4749  C CA  . LYS C 1 170 ? 41.942  48.933  60.517 1.000 121.014 0 170 LYS AAA CA  1 ? 2  
ATOM 4750  C C   . LYS C 1 170 ? 42.318  47.473  60.746 1.000 128.641 0 170 LYS AAA C   1 ? 2  
ATOM 4751  O O   . LYS C 1 170 ? 43.119  46.902  59.996 1.000 131.423 0 170 LYS AAA O   1 ? 2  
ATOM 4752  C CB  . LYS C 1 170 ? 42.672  49.853  61.494 1.000 117.857 0 170 LYS AAA CB  1 ? 2  
ATOM 4753  C CG  . LYS C 1 170 ? 44.181  49.763  61.324 1.000 129.594 0 170 LYS AAA CG  1 ? 2  
ATOM 4754  C CD  . LYS C 1 170 ? 44.918  50.912  61.983 1.000 144.673 0 170 LYS AAA CD  1 ? 2  
ATOM 4755  C CE  . LYS C 1 170 ? 46.382  50.915  61.561 1.000 154.536 0 170 LYS AAA CE  1 ? 2  
ATOM 4756  N NZ  . LYS C 1 170 ? 47.110  52.140  61.983 1.000 163.606 0 170 LYS AAA NZ  1 ? 2  
ATOM 4757  N N   . THR C 1 171 ? 41.770  46.859  61.801 1.000 125.721 0 171 THR AAA N   1 ? 2  
ATOM 4758  C CA  . THR C 1 171 ? 42.022  45.440  62.042 1.000 120.224 0 171 THR AAA CA  1 ? 2  
ATOM 4759  C C   . THR C 1 171 ? 41.498  44.594  60.889 1.000 118.500 0 171 THR AAA C   1 ? 2  
ATOM 4760  O O   . THR C 1 171 ? 42.170  43.657  60.440 1.000 124.050 0 171 THR AAA O   1 ? 2  
ATOM 4761  C CB  . THR C 1 171 ? 41.387  45.017  63.361 1.000 118.742 0 171 THR AAA CB  1 ? 2  
ATOM 4762  O OG1 . THR C 1 171 ? 41.950  45.799  64.421 1.000 123.485 0 171 THR AAA OG1 1 ? 2  
ATOM 4763  C CG2 . THR C 1 171 ? 41.652  43.549  63.625 1.000 136.084 0 171 THR AAA CG2 1 ? 2  
ATOM 4764  N N   . LEU C 1 172 ? 40.283  44.887  60.421 1.000 116.310 0 172 LEU AAA N   1 ? 2  
ATOM 4765  C CA  . LEU C 1 172 ? 39.727  44.148  59.292 1.000 121.057 0 172 LEU AAA CA  1 ? 2  
ATOM 4766  C C   . LEU C 1 172 ? 40.637  44.296  58.082 1.000 131.146 0 172 LEU AAA C   1 ? 2  
ATOM 4767  O O   . LEU C 1 172 ? 40.846  43.342  57.323 1.000 141.346 0 172 LEU AAA O   1 ? 2  
ATOM 4768  C CB  . LEU C 1 172 ? 38.306  44.624  59.001 1.000 128.466 0 172 LEU AAA CB  1 ? 2  
ATOM 4769  C CG  . LEU C 1 172 ? 37.425  43.686  58.179 1.000 140.117 0 172 LEU AAA CG  1 ? 2  
ATOM 4770  C CD1 . LEU C 1 172 ? 37.110  42.422  58.937 1.000 151.318 0 172 LEU AAA CD1 1 ? 2  
ATOM 4771  C CD2 . LEU C 1 172 ? 36.135  44.414  57.880 1.000 148.346 0 172 LEU AAA CD2 1 ? 2  
ATOM 4772  N N   . ARG C 1 173 ? 41.179  45.500  57.891 1.000 127.485 0 173 ARG AAA N   1 ? 2  
ATOM 4773  C CA  . ARG C 1 173 ? 42.089  45.761  56.784 1.000 120.604 0 173 ARG AAA CA  1 ? 2  
ATOM 4774  C C   . ARG C 1 173 ? 43.332  44.891  56.897 1.000 129.040 0 173 ARG AAA C   1 ? 2  
ATOM 4775  O O   . ARG C 1 173 ? 43.808  44.350  55.894 1.000 138.248 0 173 ARG AAA O   1 ? 2  
ATOM 4776  C CB  . ARG C 1 173 ? 42.470  47.238  56.732 1.000 112.978 0 173 ARG AAA CB  1 ? 2  
ATOM 4777  C CG  . ARG C 1 173 ? 43.240  47.588  55.476 1.000 125.652 0 173 ARG AAA CG  1 ? 2  
ATOM 4778  C CD  . ARG C 1 173 ? 43.696  49.032  55.449 1.000 113.315 0 173 ARG AAA CD  1 ? 2  
ATOM 4779  N NE  . ARG C 1 173 ? 44.184  49.392  54.124 1.000 115.612 0 173 ARG AAA NE  1 ? 2  
ATOM 4780  C CZ  . ARG C 1 173 ? 44.739  50.556  53.819 1.000 119.991 0 173 ARG AAA CZ  1 ? 2  
ATOM 4781  N NH1 . ARG C 1 173 ? 44.897  51.505  54.727 1.000 119.557 0 173 ARG AAA NH1 1 ? 2  
ATOM 4782  N NH2 . ARG C 1 173 ? 45.146  50.773  52.571 1.000 127.017 0 173 ARG AAA NH2 1 ? 2  
ATOM 4783  N N   . ALA C 1 174 ? 43.879  44.750  58.110 1.000 132.060 0 174 ALA AAA N   1 ? 2  
ATOM 4784  C CA  . ALA C 1 174 ? 45.091  43.952  58.265 1.000 137.324 0 174 ALA AAA CA  1 ? 2  
ATOM 4785  C C   . ALA C 1 174 ? 44.807  42.482  57.983 1.000 149.661 0 174 ALA AAA C   1 ? 2  
ATOM 4786  O O   . ALA C 1 174 ? 45.643  41.795  57.383 1.000 167.927 0 174 ALA AAA O   1 ? 2  
ATOM 4787  C CB  . ALA C 1 174 ? 45.665  44.135  59.669 1.000 123.212 0 174 ALA AAA CB  1 ? 2  
ATOM 4788  N N   . GLU C 1 175 ? 43.650  41.970  58.402 1.000 145.169 0 175 GLU AAA N   1 ? 2  
ATOM 4789  C CA  . GLU C 1 175 ? 43.374  40.566  58.144 1.000 156.642 0 175 GLU AAA CA  1 ? 2  
ATOM 4790  C C   . GLU C 1 175 ? 43.120  40.474  56.648 1.000 172.736 0 175 GLU AAA C   1 ? 2  
ATOM 4791  O O   . GLU C 1 175 ? 42.395  41.298  56.083 1.000 170.276 0 175 GLU AAA O   1 ? 2  
ATOM 4792  C CB  . GLU C 1 175 ? 42.194  40.058  58.964 1.000 163.377 0 175 GLU AAA CB  1 ? 2  
ATOM 4793  C CG  . GLU C 1 175 ? 42.480  40.087  60.450 1.000 174.215 0 175 GLU AAA CG  1 ? 2  
ATOM 4794  C CD  . GLU C 1 175 ? 41.452  39.336  61.267 1.000 183.882 0 175 GLU AAA CD  1 ? 2  
ATOM 4795  O OE1 . GLU C 1 175 ? 40.435  38.885  60.694 1.000 187.925 0 175 GLU AAA OE1 1 ? 2  
ATOM 4796  O OE2 . GLU C 1 175 ? 41.679  39.180  62.486 1.000 177.612 0 175 GLU AAA OE2 1 ? 2  
ATOM 4797  N N   . GLN C 1 176 ? 43.688  39.454  56.009 1.000 206.931 0 176 GLN AAA N   1 ? 2  
ATOM 4798  C CA  . GLN C 1 176 ? 43.439  39.164  54.595 1.000 221.771 0 176 GLN AAA CA  1 ? 2  
ATOM 4799  C C   . GLN C 1 176 ? 43.707  40.391  53.722 1.000 229.378 0 176 GLN AAA C   1 ? 2  
ATOM 4800  O O   . GLN C 1 176 ? 43.319  40.412  52.551 1.000 251.617 0 176 GLN AAA O   1 ? 2  
ATOM 4801  C CB  . GLN C 1 176 ? 41.996  38.690  54.355 1.000 233.503 0 176 GLN AAA CB  1 ? 2  
ATOM 4802  C CG  . GLN C 1 176 ? 41.564  37.414  55.061 1.000 238.311 0 176 GLN AAA CG  1 ? 2  
ATOM 4803  C CD  . GLN C 1 176 ? 42.247  36.177  54.501 1.000 243.451 0 176 GLN AAA CD  1 ? 2  
ATOM 4804  O OE1 . GLN C 1 176 ? 42.351  36.008  53.284 1.000 252.085 0 176 GLN AAA OE1 1 ? 2  
ATOM 4805  N NE2 . GLN C 1 176 ? 42.701  35.298  55.386 1.000 240.384 0 176 GLN AAA NE2 1 ? 2  
ATOM 4806  N N   . ALA C 1 177 ? 44.446  41.377  54.253 1.000 217.867 0 177 ALA AAA N   1 ? 2  
ATOM 4807  C CA  . ALA C 1 177 ? 44.932  42.520  53.476 1.000 217.206 0 177 ALA AAA CA  1 ? 2  
ATOM 4808  C C   . ALA C 1 177 ? 43.778  43.150  52.703 1.000 240.083 0 177 ALA AAA C   1 ? 2  
ATOM 4809  O O   . ALA C 1 177 ? 43.904  43.499  51.527 1.000 253.466 0 177 ALA AAA O   1 ? 2  
ATOM 4810  C CB  . ALA C 1 177 ? 46.074  42.116  52.546 1.000 200.249 0 177 ALA AAA CB  1 ? 2  
ATOM 4811  N N   . SER C 1 178 ? 42.634  43.278  53.385 1.000 232.713 0 178 SER AAA N   1 ? 2  
ATOM 4812  C CA  . SER C 1 178 ? 41.405  43.829  52.825 1.000 232.617 0 178 SER AAA CA  1 ? 2  
ATOM 4813  C C   . SER C 1 178 ? 40.987  42.820  51.764 1.000 268.956 0 178 SER AAA C   1 ? 2  
ATOM 4814  O O   . SER C 1 178 ? 40.972  41.620  52.053 1.000 311.196 0 178 SER AAA O   1 ? 2  
ATOM 4815  C CB  . SER C 1 178 ? 41.586  45.245  52.271 1.000 212.701 0 178 SER AAA CB  1 ? 2  
ATOM 4816  O OG  . SER C 1 178 ? 40.335  45.823  51.930 1.000 199.184 0 178 SER AAA OG  1 ? 2  
ATOM 4817  N N   . GLN C 1 179 ? 40.673  43.273  50.547 1.000 283.838 0 179 GLN AAA N   1 ? 2  
ATOM 4818  C CA  . GLN C 1 179 ? 40.432  42.381  49.413 1.000 284.139 0 179 GLN AAA CA  1 ? 2  
ATOM 4819  C C   . GLN C 1 179 ? 39.631  41.133  49.779 1.000 288.748 0 179 GLN AAA C   1 ? 2  
ATOM 4820  O O   . GLN C 1 179 ? 39.945  40.037  49.300 1.000 297.632 0 179 GLN AAA O   1 ? 2  
ATOM 4821  C CB  . GLN C 1 179 ? 41.771  41.951  48.802 1.000 271.044 0 179 GLN AAA CB  1 ? 2  
ATOM 4822  C CG  . GLN C 1 179 ? 42.702  43.089  48.407 1.000 261.087 0 179 GLN AAA CG  1 ? 2  
ATOM 4823  C CD  . GLN C 1 179 ? 42.111  43.987  47.344 1.000 263.338 0 179 GLN AAA CD  1 ? 2  
ATOM 4824  O OE1 . GLN C 1 179 ? 42.173  45.212  47.444 1.000 254.680 0 179 GLN AAA OE1 1 ? 2  
ATOM 4825  N NE2 . GLN C 1 179 ? 41.540  43.380  46.310 1.000 270.828 0 179 GLN AAA NE2 1 ? 2  
ATOM 4826  N N   . GLU C 1 180 ? 38.620  41.272  50.630 1.000 276.417 0 180 GLU AAA N   1 ? 2  
ATOM 4827  C CA  . GLU C 1 180 ? 37.785  40.140  51.020 1.000 267.438 0 180 GLU AAA CA  1 ? 2  
ATOM 4828  C C   . GLU C 1 180 ? 36.311  40.496  50.840 1.000 256.003 0 180 GLU AAA C   1 ? 2  
ATOM 4829  O O   . GLU C 1 180 ? 35.952  41.454  50.145 1.000 251.944 0 180 GLU AAA O   1 ? 2  
ATOM 4830  C CB  . GLU C 1 180 ? 38.109  39.731  52.461 1.000 270.541 0 180 GLU AAA CB  1 ? 2  
ATOM 4831  C CG  . GLU C 1 180 ? 37.939  38.247  52.758 1.000 272.024 0 180 GLU AAA CG  1 ? 2  
ATOM 4832  C CD  . GLU C 1 180 ? 38.785  37.367  51.863 1.000 280.414 0 180 GLU AAA CD  1 ? 2  
ATOM 4833  O OE1 . GLU C 1 180 ? 39.962  37.714  51.633 1.000 280.499 0 180 GLU AAA OE1 1 ? 2  
ATOM 4834  O OE2 . GLU C 1 180 ? 38.279  36.323  51.400 1.000 284.473 0 180 GLU AAA OE2 1 ? 2  
ATOM 4835  N N   . VAL C 1 181 ? 35.435  39.709  51.471 1.000 251.259 0 181 VAL AAA N   1 ? 2  
ATOM 4836  C CA  . VAL C 1 181 ? 34.005  39.993  51.402 1.000 244.295 0 181 VAL AAA CA  1 ? 2  
ATOM 4837  C C   . VAL C 1 181 ? 33.709  41.329  52.065 1.000 248.435 0 181 VAL AAA C   1 ? 2  
ATOM 4838  O O   . VAL C 1 181 ? 32.959  42.154  51.531 1.000 246.999 0 181 VAL AAA O   1 ? 2  
ATOM 4839  C CB  . VAL C 1 181 ? 33.192  38.849  52.037 1.000 231.103 0 181 VAL AAA CB  1 ? 2  
ATOM 4840  C CG1 . VAL C 1 181 ? 33.045  37.703  51.061 1.000 225.498 0 181 VAL AAA CG1 1 ? 2  
ATOM 4841  C CG2 . VAL C 1 181 ? 33.864  38.360  53.315 1.000 215.372 0 181 VAL AAA CG2 1 ? 2  
ATOM 4842  N N   . LYS C 1 182 ? 34.293  41.558  53.244 1.000 242.636 0 182 LYS AAA N   1 ? 2  
ATOM 4843  C CA  . LYS C 1 182 ? 34.166  42.810  53.985 1.000 230.296 0 182 LYS AAA CA  1 ? 2  
ATOM 4844  C C   . LYS C 1 182 ? 32.706  43.125  54.313 1.000 230.186 0 182 LYS AAA C   1 ? 2  
ATOM 4845  O O   . LYS C 1 182 ? 32.358  44.286  54.554 1.000 224.258 0 182 LYS AAA O   1 ? 2  
ATOM 4846  C CB  . LYS C 1 182 ? 34.800  43.975  53.204 1.000 224.311 0 182 LYS AAA CB  1 ? 2  
ATOM 4847  C CG  . LYS C 1 182 ? 35.334  45.134  54.038 1.000 199.730 0 182 LYS AAA CG  1 ? 2  
ATOM 4848  C CD  . LYS C 1 182 ? 36.753  44.826  54.510 1.000 193.306 0 182 LYS AAA CD  1 ? 2  
ATOM 4849  C CE  . LYS C 1 182 ? 37.499  46.086  54.930 1.000 187.631 0 182 LYS AAA CE  1 ? 2  
ATOM 4850  N NZ  . LYS C 1 182 ? 37.772  46.994  53.783 1.000 174.842 0 182 LYS AAA NZ  1 ? 2  
ATOM 4851  N N   . ASN C 1 183 ? 31.830  42.115  54.292 1.000 229.238 0 183 ASN AAA N   1 ? 2  
ATOM 4852  C CA  . ASN C 1 183 ? 30.406  42.380  54.450 1.000 225.049 0 183 ASN AAA CA  1 ? 2  
ATOM 4853  C C   . ASN C 1 183 ? 29.704  41.464  55.447 1.000 211.158 0 183 ASN AAA C   1 ? 2  
ATOM 4854  O O   . ASN C 1 183 ? 28.868  41.923  56.232 1.000 208.716 0 183 ASN AAA O   1 ? 2  
ATOM 4855  C CB  . ASN C 1 183 ? 29.726  42.222  53.091 1.000 246.673 0 183 ASN AAA CB  1 ? 2  
ATOM 4856  C CG  . ASN C 1 183 ? 30.020  43.368  52.156 1.000 258.700 0 183 ASN AAA CG  1 ? 2  
ATOM 4857  O OD1 . ASN C 1 183 ? 30.131  44.517  52.577 1.000 258.579 0 183 ASN AAA OD1 1 ? 2  
ATOM 4858  N ND2 . ASN C 1 183 ? 30.171  43.056  50.874 1.000 272.034 0 183 ASN AAA ND2 1 ? 2  
ATOM 4859  N N   . ALA C 1 184 ? 30.034  40.171  55.428 1.000 211.332 0 184 ALA AAA N   1 ? 2  
ATOM 4860  C CA  . ALA C 1 184 ? 29.428  39.238  56.376 1.000 211.664 0 184 ALA AAA CA  1 ? 2  
ATOM 4861  C C   . ALA C 1 184 ? 29.837  39.541  57.813 1.000 212.939 0 184 ALA AAA C   1 ? 2  
ATOM 4862  O O   . ALA C 1 184 ? 28.988  39.596  58.709 1.000 208.730 0 184 ALA AAA O   1 ? 2  
ATOM 4863  C CB  . ALA C 1 184 ? 29.789  37.801  56.000 1.000 210.198 0 184 ALA AAA CB  1 ? 2  
ATOM 4864  N N   . ALA C 1 185 ? 31.135  39.727  58.056 1.000 214.193 0 185 ALA AAA N   1 ? 2  
ATOM 4865  C CA  . ALA C 1 185 ? 31.594  40.030  59.409 1.000 200.597 0 185 ALA AAA CA  1 ? 2  
ATOM 4866  C C   . ALA C 1 185 ? 31.059  41.377  59.882 1.000 196.398 0 185 ALA AAA C   1 ? 2  
ATOM 4867  O O   . ALA C 1 185 ? 30.778  41.563  61.072 1.000 189.628 0 185 ALA AAA O   1 ? 2  
ATOM 4868  C CB  . ALA C 1 185 ? 33.119  39.996  59.465 1.000 185.130 0 185 ALA AAA CB  1 ? 2  
ATOM 4869  N N   . THR C 1 186 ? 30.925  42.328  58.957 1.000 203.470 0 186 THR AAA N   1 ? 2  
ATOM 4870  C CA  . THR C 1 186 ? 30.481  43.677  59.293 1.000 199.591 0 186 THR AAA CA  1 ? 2  
ATOM 4871  C C   . THR C 1 186 ? 29.037  43.704  59.795 1.000 203.964 0 186 THR AAA C   1 ? 2  
ATOM 4872  O O   . THR C 1 186 ? 28.760  44.241  60.873 1.000 188.234 0 186 THR AAA O   1 ? 2  
ATOM 4873  C CB  . THR C 1 186 ? 30.643  44.589  58.073 1.000 202.171 0 186 THR AAA CB  1 ? 2  
ATOM 4874  O OG1 . THR C 1 186 ? 32.001  44.543  57.622 1.000 196.585 0 186 THR AAA OG1 1 ? 2  
ATOM 4875  C CG2 . THR C 1 186 ? 30.308  46.026  58.428 1.000 188.109 0 186 THR AAA CG2 1 ? 2  
ATOM 4876  N N   . GLU C 1 187 ? 28.103  43.112  59.036 1.000 227.243 0 187 GLU AAA N   1 ? 2  
ATOM 4877  C CA  . GLU C 1 187 ? 26.697  43.013  59.444 1.000 236.630 0 187 GLU AAA CA  1 ? 2  
ATOM 4878  C C   . GLU C 1 187 ? 26.471  42.307  60.781 1.000 228.927 0 187 GLU AAA C   1 ? 2  
ATOM 4879  O O   . GLU C 1 187 ? 25.334  42.278  61.267 1.000 229.471 0 187 GLU AAA O   1 ? 2  
ATOM 4880  C CB  . GLU C 1 187 ? 25.919  42.215  58.387 1.000 254.096 0 187 GLU AAA CB  1 ? 2  
ATOM 4881  C CG  . GLU C 1 187 ? 25.828  42.809  56.978 1.000 274.289 0 187 GLU AAA CG  1 ? 2  
ATOM 4882  C CD  . GLU C 1 187 ? 25.610  44.302  56.953 1.000 288.494 0 187 GLU AAA CD  1 ? 2  
ATOM 4883  O OE1 . GLU C 1 187 ? 24.563  44.766  57.450 1.000 299.875 0 187 GLU AAA OE1 1 ? 2  
ATOM 4884  O OE2 . GLU C 1 187 ? 26.481  45.009  56.401 1.000 290.480 0 187 GLU AAA OE2 1 ? 2  
ATOM 4885  N N   . THR C 1 188 ? 27.521  41.766  61.384 1.000 207.461 0 188 THR AAA N   1 ? 2  
ATOM 4886  C CA  . THR C 1 188 ? 27.485  40.930  62.579 1.000 200.963 0 188 THR AAA CA  1 ? 2  
ATOM 4887  C C   . THR C 1 188 ? 28.296  41.471  63.747 1.000 193.036 0 188 THR AAA C   1 ? 2  
ATOM 4888  O O   . THR C 1 188 ? 27.762  42.049  64.699 1.000 188.816 0 188 THR AAA O   1 ? 2  
ATOM 4889  C CB  . THR C 1 188 ? 27.904  39.501  62.246 1.000 206.314 0 188 THR AAA CB  1 ? 2  
ATOM 4890  O OG1 . THR C 1 188 ? 29.068  39.513  61.411 1.000 210.105 0 188 THR AAA OG1 1 ? 2  
ATOM 4891  C CG2 . THR C 1 188 ? 26.758  38.772  61.553 1.000 205.408 0 188 THR AAA CG2 1 ? 2  
ATOM 4892  N N   . LEU C 1 189 ? 29.611  41.292  63.644 1.000 183.421 0 189 LEU AAA N   1 ? 2  
ATOM 4893  C CA  . LEU C 1 189 ? 30.537  41.513  64.746 1.000 181.617 0 189 LEU AAA CA  1 ? 2  
ATOM 4894  C C   . LEU C 1 189 ? 30.670  42.979  65.132 1.000 178.404 0 189 LEU AAA C   1 ? 2  
ATOM 4895  O O   . LEU C 1 189 ? 30.910  43.272  66.309 1.000 182.950 0 189 LEU AAA O   1 ? 2  
ATOM 4896  C CB  . LEU C 1 189 ? 31.915  40.992  64.351 1.000 172.670 0 189 LEU AAA CB  1 ? 2  
ATOM 4897  C CG  . LEU C 1 189 ? 32.136  39.495  64.188 1.000 172.776 0 189 LEU AAA CG  1 ? 2  
ATOM 4898  C CD1 . LEU C 1 189 ? 33.602  39.250  63.890 1.000 163.542 0 189 LEU AAA CD1 1 ? 2  
ATOM 4899  C CD2 . LEU C 1 189 ? 31.699  38.761  65.438 1.000 177.333 0 189 LEU AAA CD2 1 ? 2  
ATOM 4900  N N   . LEU C 1 190 ? 30.560  43.912  64.186 1.000 165.666 0 190 LEU AAA N   1 ? 2  
ATOM 4901  C CA  . LEU C 1 190 ? 30.685  45.318  64.563 1.000 156.965 0 190 LEU AAA CA  1 ? 2  
ATOM 4902  C C   . LEU C 1 190 ? 29.632  45.698  65.602 1.000 161.489 0 190 LEU AAA C   1 ? 2  
ATOM 4903  O O   . LEU C 1 190 ? 29.922  46.452  66.538 1.000 169.750 0 190 LEU AAA O   1 ? 2  
ATOM 4904  C CB  . LEU C 1 190 ? 30.581  46.214  63.319 1.000 152.966 0 190 LEU AAA CB  1 ? 2  
ATOM 4905  C CG  . LEU C 1 190 ? 30.899  47.726  63.326 1.000 141.894 0 190 LEU AAA CG  1 ? 2  
ATOM 4906  C CD1 . LEU C 1 190 ? 30.857  48.284  61.899 1.000 128.213 0 190 LEU AAA CD1 1 ? 2  
ATOM 4907  C CD2 . LEU C 1 190 ? 30.042  48.579  64.253 1.000 145.593 0 190 LEU AAA CD2 1 ? 2  
ATOM 4908  N N   . VAL C 1 191 ? 28.409  45.179  65.467 1.000 172.563 0 191 VAL AAA N   1 ? 2  
ATOM 4909  C CA  . VAL C 1 191 ? 27.367  45.477  66.450 1.000 166.367 0 191 VAL AAA CA  1 ? 2  
ATOM 4910  C C   . VAL C 1 191 ? 27.601  44.706  67.756 1.000 172.427 0 191 VAL AAA C   1 ? 2  
ATOM 4911  O O   . VAL C 1 191 ? 27.501  45.276  68.849 1.000 162.302 0 191 VAL AAA O   1 ? 2  
ATOM 4912  C CB  . VAL C 1 191 ? 25.963  45.239  65.848 1.000 152.391 0 191 VAL AAA CB  1 ? 2  
ATOM 4913  C CG1 . VAL C 1 191 ? 25.796  46.047  64.561 1.000 142.061 0 191 VAL AAA CG1 1 ? 2  
ATOM 4914  C CG2 . VAL C 1 191 ? 25.653  43.770  65.604 1.000 174.151 0 191 VAL AAA CG2 1 ? 2  
ATOM 4915  N N   . GLN C 1 192 ? 27.914  43.407  67.668 1.000 177.788 0 192 GLN AAA N   1 ? 2  
ATOM 4916  C CA  . GLN C 1 192 ? 28.095  42.588  68.869 1.000 191.031 0 192 GLN AAA CA  1 ? 2  
ATOM 4917  C C   . GLN C 1 192 ? 29.246  43.075  69.747 1.000 189.466 0 192 GLN AAA C   1 ? 2  
ATOM 4918  O O   . GLN C 1 192 ? 29.178  42.977  70.979 1.000 205.599 0 192 GLN AAA O   1 ? 2  
ATOM 4919  C CB  . GLN C 1 192 ? 28.307  41.126  68.475 1.000 198.258 0 192 GLN AAA CB  1 ? 2  
ATOM 4920  C CG  . GLN C 1 192 ? 27.096  40.231  68.731 1.000 219.821 0 192 GLN AAA CG  1 ? 2  
ATOM 4921  C CD  . GLN C 1 192 ? 25.941  40.519  67.783 1.000 232.192 0 192 GLN AAA CD  1 ? 2  
ATOM 4922  O OE1 . GLN C 1 192 ? 26.091  40.469  66.562 1.000 237.285 0 192 GLN AAA OE1 1 ? 2  
ATOM 4923  N NE2 . GLN C 1 192 ? 24.777  40.831  68.350 1.000 241.614 0 192 GLN AAA NE2 1 ? 2  
ATOM 4924  N N   . ASN C 1 193 ? 30.310  43.585  69.141 1.000 178.825 0 193 ASN AAA N   1 ? 2  
ATOM 4925  C CA  . ASN C 1 193 ? 31.485  44.073  69.856 1.000 175.997 0 193 ASN AAA CA  1 ? 2  
ATOM 4926  C C   . ASN C 1 193 ? 31.372  45.539  70.252 1.000 173.901 0 193 ASN AAA C   1 ? 2  
ATOM 4927  O O   . ASN C 1 193 ? 32.295  46.075  70.874 1.000 164.899 0 193 ASN AAA O   1 ? 2  
ATOM 4928  C CB  . ASN C 1 193 ? 32.755  43.819  69.043 1.000 180.606 0 193 ASN AAA CB  1 ? 2  
ATOM 4929  C CG  . ASN C 1 193 ? 33.117  42.342  68.989 1.000 186.867 0 193 ASN AAA CG  1 ? 2  
ATOM 4930  O OD1 . ASN C 1 193 ? 33.006  41.632  69.992 1.000 186.752 0 193 ASN AAA OD1 1 ? 2  
ATOM 4931  N ND2 . ASN C 1 193 ? 33.563  41.877  67.826 1.000 183.849 0 193 ASN AAA ND2 1 ? 2  
ATOM 4932  N N   . ALA C 1 194 ? 30.255  46.181  69.930 1.000 186.225 0 194 ALA AAA N   1 ? 2  
ATOM 4933  C CA  . ALA C 1 194 ? 29.977  47.547  70.335 1.000 191.000 0 194 ALA AAA CA  1 ? 2  
ATOM 4934  C C   . ALA C 1 194 ? 29.745  47.599  71.842 1.000 204.762 0 194 ALA AAA C   1 ? 2  
ATOM 4935  O O   . ALA C 1 194 ? 29.531  46.580  72.505 1.000 213.290 0 194 ALA AAA O   1 ? 2  
ATOM 4936  C CB  . ALA C 1 194 ? 28.767  48.102  69.586 1.000 191.847 0 194 ALA AAA CB  1 ? 2  
ATOM 4937  N N   . ASN C 1 195 ? 29.785  48.810  72.387 1.000 207.862 0 195 ASN AAA N   1 ? 2  
ATOM 4938  C CA  . ASN C 1 195 ? 29.619  48.969  73.816 1.000 222.706 0 195 ASN AAA CA  1 ? 2  
ATOM 4939  C C   . ASN C 1 195 ? 28.144  48.772  74.176 1.000 232.703 0 195 ASN AAA C   1 ? 2  
ATOM 4940  O O   . ASN C 1 195 ? 27.276  48.814  73.302 1.000 233.771 0 195 ASN AAA O   1 ? 2  
ATOM 4941  C CB  . ASN C 1 195 ? 30.136  50.386  74.140 1.000 229.641 0 195 ASN AAA CB  1 ? 2  
ATOM 4942  C CG  . ASN C 1 195 ? 29.526  51.030  75.378 1.000 251.535 0 195 ASN AAA CG  1 ? 2  
ATOM 4943  O OD1 . ASN C 1 195 ? 29.813  50.657  76.512 1.000 274.047 0 195 ASN AAA OD1 1 ? 2  
ATOM 4944  N ND2 . ASN C 1 195 ? 28.674  52.024  75.150 1.000 253.912 0 195 ASN AAA ND2 1 ? 2  
ATOM 4945  N N   . PRO C 1 196 ? 27.834  48.558  75.462 1.000 235.062 0 196 PRO AAA N   1 ? 2  
ATOM 4946  C CA  A PRO C 1 196 ? 26.450  48.182  75.808 1.000 236.172 0 196 PRO AAA CA  1 ? 2  
ATOM 4947  C C   . PRO C 1 196 ? 25.417  49.250  75.512 1.000 237.864 0 196 PRO AAA C   1 ? 2  
ATOM 4948  O O   . PRO C 1 196 ? 24.353  48.933  74.966 1.000 237.533 0 196 PRO AAA O   1 ? 2  
ATOM 4949  C CB  A PRO C 1 196 ? 26.531  47.862  77.309 1.000 230.098 0 196 PRO AAA CB  1 ? 2  
ATOM 4950  C CG  A PRO C 1 196 ? 27.982  47.684  77.622 1.000 221.950 0 196 PRO AAA CG  1 ? 2  
ATOM 4951  C CD  A PRO C 1 196 ? 28.802  47.990  76.417 1.000 232.251 0 196 PRO AAA CD  1 ? 2  
ATOM 4952  N N   . ASP C 1 197 ? 25.686  50.506  75.862 1.000 241.629 0 197 ASP AAA N   1 ? 2  
ATOM 4953  C CA  . ASP C 1 197 ? 24.727  51.563  75.563 1.000 247.281 0 197 ASP AAA CA  1 ? 2  
ATOM 4954  C C   . ASP C 1 197 ? 24.592  51.767  74.057 1.000 239.058 0 197 ASP AAA C   1 ? 2  
ATOM 4955  O O   . ASP C 1 197 ? 23.487  51.994  73.550 1.000 254.385 0 197 ASP AAA O   1 ? 2  
ATOM 4956  C CB  . ASP C 1 197 ? 25.155  52.850  76.261 1.000 258.259 0 197 ASP AAA CB  1 ? 2  
ATOM 4957  C CG  . ASP C 1 197 ? 24.899  52.809  77.753 1.000 278.528 0 197 ASP AAA CG  1 ? 2  
ATOM 4958  O OD1 . ASP C 1 197 ? 25.282  51.803  78.388 1.000 287.904 0 197 ASP AAA OD1 1 ? 2  
ATOM 4959  O OD2 . ASP C 1 197 ? 24.325  53.774  78.292 1.000 290.176 0 197 ASP AAA OD2 1 ? 2  
ATOM 4960  N N   . CYS C 1 198 ? 25.709  51.691  73.327 1.000 222.300 0 198 CYS AAA N   1 ? 2  
ATOM 4961  C CA  . CYS C 1 198 ? 25.668  51.815  71.872 1.000 210.815 0 198 CYS AAA CA  1 ? 2  
ATOM 4962  C C   . CYS C 1 198 ? 25.014  50.600  71.213 1.000 202.503 0 198 CYS AAA C   1 ? 2  
ATOM 4963  O O   . CYS C 1 198 ? 24.298  50.748  70.215 1.000 190.935 0 198 CYS AAA O   1 ? 2  
ATOM 4964  C CB  . CYS C 1 198 ? 27.081  52.029  71.327 1.000 207.129 0 198 CYS AAA CB  1 ? 2  
ATOM 4965  S SG  . CYS C 1 198 ? 27.701  53.732  71.440 1.000 199.270 0 198 CYS AAA SG  1 ? 2  
ATOM 4966  N N   . LYS C 1 199 ? 25.261  49.392  71.740 1.000 197.141 0 199 LYS AAA N   1 ? 2  
ATOM 4967  C CA  . LYS C 1 199 ? 24.689  48.183  71.143 1.000 198.836 0 199 LYS AAA CA  1 ? 2  
ATOM 4968  C C   . LYS C 1 199 ? 23.170  48.269  71.071 1.000 208.221 0 199 LYS AAA C   1 ? 2  
ATOM 4969  O O   . LYS C 1 199 ? 22.566  47.917  70.050 1.000 203.078 0 199 LYS AAA O   1 ? 2  
ATOM 4970  C CB  . LYS C 1 199 ? 25.113  46.950  71.942 1.000 196.528 0 199 LYS AAA CB  1 ? 2  
ATOM 4971  C CG  . LYS C 1 199 ? 24.740  45.617  71.307 1.000 190.062 0 199 LYS AAA CG  1 ? 2  
ATOM 4972  C CD  . LYS C 1 199 ? 25.060  44.468  72.248 1.000 190.833 0 199 LYS AAA CD  1 ? 2  
ATOM 4973  C CE  . LYS C 1 199 ? 26.560  44.298  72.407 1.000 193.725 0 199 LYS AAA CE  1 ? 2  
ATOM 4974  N NZ  . LYS C 1 199 ? 26.903  42.971  72.983 1.000 194.900 0 199 LYS AAA NZ  1 ? 2  
ATOM 4975  N N   . THR C 1 200 ? 22.539  48.724  72.153 1.000 215.850 0 200 THR AAA N   1 ? 2  
ATOM 4976  C CA  . THR C 1 200 ? 21.093  48.913  72.155 1.000 209.890 0 200 THR AAA CA  1 ? 2  
ATOM 4977  C C   . THR C 1 200 ? 20.674  49.870  71.047 1.000 206.137 0 200 THR AAA C   1 ? 2  
ATOM 4978  O O   . THR C 1 200 ? 19.669  49.644  70.363 1.000 204.710 0 200 THR AAA O   1 ? 2  
ATOM 4979  C CB  . THR C 1 200 ? 20.625  49.414  73.520 1.000 218.914 0 200 THR AAA CB  1 ? 2  
ATOM 4980  O OG1 . THR C 1 200 ? 21.081  50.757  73.722 1.000 217.553 0 200 THR AAA OG1 1 ? 2  
ATOM 4981  C CG2 . THR C 1 200 ? 21.160  48.512  74.624 1.000 223.261 0 200 THR AAA CG2 1 ? 2  
ATOM 4982  N N   . ILE C 1 201 ? 21.433  50.954  70.864 1.000 208.642 0 201 ILE AAA N   1 ? 2  
ATOM 4983  C CA  . ILE C 1 201 ? 21.124  51.908  69.805 1.000 201.412 0 201 ILE AAA CA  1 ? 2  
ATOM 4984  C C   . ILE C 1 201 ? 21.300  51.262  68.434 1.000 196.118 0 201 ILE AAA C   1 ? 2  
ATOM 4985  O O   . ILE C 1 201 ? 20.451  51.417  67.548 1.000 195.534 0 201 ILE AAA O   1 ? 2  
ATOM 4986  C CB  . ILE C 1 201 ? 22.025  53.150  69.955 1.000 192.142 0 201 ILE AAA CB  1 ? 2  
ATOM 4987  C CG1 . ILE C 1 201 ? 21.692  53.929  71.230 1.000 216.785 0 201 ILE AAA CG1 1 ? 2  
ATOM 4988  C CG2 . ILE C 1 201 ? 21.897  54.055  68.744 1.000 187.273 0 201 ILE AAA CG2 1 ? 2  
ATOM 4989  C CD1 . ILE C 1 201 ? 22.752  54.954  71.611 1.000 205.715 0 201 ILE AAA CD1 1 ? 2  
ATOM 4990  N N   . LEU C 1 202 ? 22.397  50.524  68.237 1.000 191.415 0 202 LEU AAA N   1 ? 2  
ATOM 4991  C CA  . LEU C 1 202 ? 22.647  49.897  66.941 1.000 192.836 0 202 LEU AAA CA  1 ? 2  
ATOM 4992  C C   . LEU C 1 202 ? 21.617  48.811  66.634 1.000 206.327 0 202 LEU AAA C   1 ? 2  
ATOM 4993  O O   . LEU C 1 202 ? 21.173  48.673  65.488 1.000 200.599 0 202 LEU AAA O   1 ? 2  
ATOM 4994  C CB  . LEU C 1 202 ? 24.061  49.320  66.913 1.000 182.406 0 202 LEU AAA CB  1 ? 2  
ATOM 4995  C CG  . LEU C 1 202 ? 25.212  50.324  67.006 1.000 182.187 0 202 LEU AAA CG  1 ? 2  
ATOM 4996  C CD1 . LEU C 1 202 ? 26.547  49.603  67.065 1.000 181.795 0 202 LEU AAA CD1 1 ? 2  
ATOM 4997  C CD2 . LEU C 1 202 ? 25.177  51.280  65.828 1.000 175.365 0 202 LEU AAA CD2 1 ? 2  
ATOM 4998  N N   . LYS C 1 203 ? 21.237  48.030  67.653 1.000 207.786 0 203 LYS AAA N   1 ? 2  
ATOM 4999  C CA  . LYS C 1 203 ? 20.200  47.007  67.506 1.000 191.678 0 203 LYS AAA CA  1 ? 2  
ATOM 5000  C C   . LYS C 1 203 ? 18.876  47.621  67.071 1.000 198.815 0 203 LYS AAA C   1 ? 2  
ATOM 5001  O O   . LYS C 1 203 ? 18.160  47.061  66.230 1.000 202.999 0 203 LYS AAA O   1 ? 2  
ATOM 5002  C CB  . LYS C 1 203 ? 20.042  46.247  68.824 1.000 195.651 0 203 LYS AAA CB  1 ? 2  
ATOM 5003  C CG  . LYS C 1 203 ? 21.150  45.238  69.110 1.000 189.551 0 203 LYS AAA CG  1 ? 2  
ATOM 5004  C CD  . LYS C 1 203 ? 21.013  44.632  70.503 1.000 206.745 0 203 LYS AAA CD  1 ? 2  
ATOM 5005  C CE  . LYS C 1 203 ? 19.892  43.615  70.613 1.000 207.384 0 203 LYS AAA CE  1 ? 2  
ATOM 5006  N NZ  . LYS C 1 203 ? 20.094  42.491  69.666 1.000 211.251 0 203 LYS AAA NZ  1 ? 2  
ATOM 5007  N N   . ALA C 1 204 ? 18.551  48.783  67.633 1.000 199.639 0 204 ALA AAA N   1 ? 2  
ATOM 5008  C CA  . ALA C 1 204 ? 17.328  49.527  67.360 1.000 215.193 0 204 ALA AAA CA  1 ? 2  
ATOM 5009  C C   . ALA C 1 204 ? 17.294  50.110  65.956 1.000 212.534 0 204 ALA AAA C   1 ? 2  
ATOM 5010  O O   . ALA C 1 204 ? 16.209  50.428  65.462 1.000 228.116 0 204 ALA AAA O   1 ? 2  
ATOM 5011  C CB  . ALA C 1 204 ? 17.150  50.655  68.378 1.000 226.588 0 204 ALA AAA CB  1 ? 2  
ATOM 5012  N N   . LEU C 1 205 ? 18.443  50.235  65.294 1.000 207.204 0 205 LEU AAA N   1 ? 2  
ATOM 5013  C CA  . LEU C 1 205 ? 18.453  50.813  63.953 1.000 203.454 0 205 LEU AAA CA  1 ? 2  
ATOM 5014  C C   . LEU C 1 205 ? 17.682  50.003  62.915 1.000 204.930 0 205 LEU AAA C   1 ? 2  
ATOM 5015  O O   . LEU C 1 205 ? 17.220  50.588  61.930 1.000 202.931 0 205 LEU AAA O   1 ? 2  
ATOM 5016  C CB  . LEU C 1 205 ? 19.892  51.020  63.483 1.000 207.043 0 205 LEU AAA CB  1 ? 2  
ATOM 5017  C CG  . LEU C 1 205 ? 20.669  52.118  64.203 1.000 212.848 0 205 LEU AAA CG  1 ? 2  
ATOM 5018  C CD1 . LEU C 1 205 ? 22.071  52.195  63.640 1.000 219.487 0 205 LEU AAA CD1 1 ? 2  
ATOM 5019  C CD2 . LEU C 1 205 ? 19.950  53.451  64.038 1.000 211.419 0 205 LEU AAA CD2 1 ? 2  
ATOM 5020  N N   . GLY C 1 206 ? 17.529  48.693  63.065 1.000 213.265 0 206 GLY AAA N   1 ? 2  
ATOM 5021  C CA  . GLY C 1 206 ? 16.746  48.021  62.051 1.000 226.211 0 206 GLY AAA CA  1 ? 2  
ATOM 5022  C C   . GLY C 1 206 ? 17.581  47.495  60.909 1.000 232.455 0 206 GLY AAA C   1 ? 2  
ATOM 5023  O O   . GLY C 1 206 ? 18.808  47.644  60.891 1.000 230.003 0 206 GLY AAA O   1 ? 2  
ATOM 5024  N N   . PRO C 1 207 ? 16.935  46.885  59.916 1.000 244.583 0 207 PRO AAA N   1 ? 2  
ATOM 5025  C CA  . PRO C 1 207 ? 17.702  46.333  58.804 1.000 241.027 0 207 PRO AAA CA  1 ? 2  
ATOM 5026  C C   . PRO C 1 207 ? 18.195  47.449  57.905 1.000 240.635 0 207 PRO AAA C   1 ? 2  
ATOM 5027  O O   . PRO C 1 207 ? 17.604  48.528  57.827 1.000 252.335 0 207 PRO AAA O   1 ? 2  
ATOM 5028  C CB  . PRO C 1 207 ? 16.673  45.483  58.050 1.000 247.834 0 207 PRO AAA CB  1 ? 2  
ATOM 5029  C CG  . PRO C 1 207 ? 15.368  46.159  58.339 1.000 257.920 0 207 PRO AAA CG  1 ? 2  
ATOM 5030  C CD  . PRO C 1 207 ? 15.482  46.771  59.709 1.000 258.373 0 207 PRO AAA CD  1 ? 2  
ATOM 5031  N N   . GLY C 1 208 ? 19.320  47.171  57.272 1.000 239.583 0 208 GLY AAA N   1 ? 2  
ATOM 5032  C CA  . GLY C 1 208 ? 19.873  48.111  56.338 1.000 235.444 0 208 GLY AAA CA  1 ? 2  
ATOM 5033  C C   . GLY C 1 208 ? 20.549  49.224  57.094 1.000 229.717 0 208 GLY AAA C   1 ? 2  
ATOM 5034  O O   . GLY C 1 208 ? 19.872  49.930  57.845 1.000 249.349 0 208 GLY AAA O   1 ? 2  
ATOM 5035  N N   . ALA C 1 209 ? 21.867  49.323  57.091 1.000 211.908 0 209 ALA AAA N   1 ? 2  
ATOM 5036  C CA  . ALA C 1 209 ? 22.369  50.505  57.781 1.000 205.262 0 209 ALA AAA CA  1 ? 2  
ATOM 5037  C C   . ALA C 1 209 ? 23.577  51.033  57.046 1.000 205.774 0 209 ALA AAA C   1 ? 2  
ATOM 5038  O O   . ALA C 1 209 ? 24.497  50.265  56.758 1.000 217.546 0 209 ALA AAA O   1 ? 2  
ATOM 5039  C CB  . ALA C 1 209 ? 22.768  50.158  59.211 1.000 189.397 0 209 ALA AAA CB  1 ? 2  
ATOM 5040  N N   . THR C 1 210 ? 23.602  52.341  56.790 1.000 196.590 0 210 THR AAA N   1 ? 2  
ATOM 5041  C CA  . THR C 1 210 ? 24.809  52.831  56.167 1.000 184.230 0 210 THR AAA CA  1 ? 2  
ATOM 5042  C C   . THR C 1 210 ? 25.837  53.014  57.271 1.000 174.398 0 210 THR AAA C   1 ? 2  
ATOM 5043  O O   . THR C 1 210 ? 25.481  53.130  58.446 1.000 179.855 0 210 THR AAA O   1 ? 2  
ATOM 5044  C CB  . THR C 1 210 ? 24.512  54.107  55.377 1.000 184.093 0 210 THR AAA CB  1 ? 2  
ATOM 5045  O OG1 . THR C 1 210 ? 23.290  53.905  54.652 1.000 200.649 0 210 THR AAA OG1 1 ? 2  
ATOM 5046  C CG2 . THR C 1 210 ? 25.610  54.354  54.361 1.000 170.002 0 210 THR AAA CG2 1 ? 2  
ATOM 5047  N N   . LEU C 1 211 ? 27.115  53.045  56.921 1.000 160.888 0 211 LEU AAA N   1 ? 2  
ATOM 5048  C CA  . LEU C 1 211 ? 28.060  53.329  57.987 1.000 154.993 0 211 LEU AAA CA  1 ? 2  
ATOM 5049  C C   . LEU C 1 211 ? 27.790  54.732  58.534 1.000 159.339 0 211 LEU AAA C   1 ? 2  
ATOM 5050  O O   . LEU C 1 211 ? 27.803  54.962  59.749 1.000 168.209 0 211 LEU AAA O   1 ? 2  
ATOM 5051  C CB  . LEU C 1 211 ? 29.502  53.128  57.517 1.000 153.666 0 211 LEU AAA CB  1 ? 2  
ATOM 5052  C CG  . LEU C 1 211 ? 30.581  53.306  58.594 1.000 149.184 0 211 LEU AAA CG  1 ? 2  
ATOM 5053  C CD1 . LEU C 1 211 ? 31.810  52.535  58.192 1.000 131.172 0 211 LEU AAA CD1 1 ? 2  
ATOM 5054  C CD2 . LEU C 1 211 ? 30.984  54.723  58.808 1.000 153.709 0 211 LEU AAA CD2 1 ? 2  
ATOM 5055  N N   . GLU C 1 212 ? 27.530  55.678  57.619 1.000 159.545 0 212 GLU AAA N   1 ? 2  
ATOM 5056  C CA  . GLU C 1 212 ? 27.209  57.070  57.948 1.000 165.827 0 212 GLU AAA CA  1 ? 2  
ATOM 5057  C C   . GLU C 1 212 ? 26.017  57.226  58.891 1.000 177.114 0 212 GLU AAA C   1 ? 2  
ATOM 5058  O O   . GLU C 1 212 ? 26.081  57.990  59.864 1.000 183.142 0 212 GLU AAA O   1 ? 2  
ATOM 5059  C CB  . GLU C 1 212 ? 26.886  57.830  56.655 1.000 171.867 0 212 GLU AAA CB  1 ? 2  
ATOM 5060  C CG  . GLU C 1 212 ? 27.758  57.519  55.435 1.000 184.266 0 212 GLU AAA CG  1 ? 2  
ATOM 5061  C CD  . GLU C 1 212 ? 27.431  58.410  54.234 1.000 190.785 0 212 GLU AAA CD  1 ? 2  
ATOM 5062  O OE1 . GLU C 1 212 ? 26.911  59.533  54.440 1.000 190.292 0 212 GLU AAA OE1 1 ? 2  
ATOM 5063  O OE2 . GLU C 1 212 ? 27.648  57.973  53.079 1.000 191.652 0 212 GLU AAA OE2 1 ? 2  
ATOM 5064  N N   . GLU C 1 213 ? 24.914  56.523  58.616 1.000 185.491 0 213 GLU AAA N   1 ? 2  
ATOM 5065  C CA  . GLU C 1 213 ? 23.731  56.640  59.463 1.000 182.362 0 213 GLU AAA CA  1 ? 2  
ATOM 5066  C C   . GLU C 1 213 ? 23.948  56.113  60.872 1.000 179.596 0 213 GLU AAA C   1 ? 2  
ATOM 5067  O O   . GLU C 1 213 ? 23.533  56.748  61.850 1.000 190.551 0 213 GLU AAA O   1 ? 2  
ATOM 5068  C CB  . GLU C 1 213 ? 22.570  55.884  58.810 1.000 190.102 0 213 GLU AAA CB  1 ? 2  
ATOM 5069  C CG  . GLU C 1 213 ? 21.994  56.530  57.569 1.000 203.016 0 213 GLU AAA CG  1 ? 2  
ATOM 5070  C CD  . GLU C 1 213 ? 21.091  55.577  56.820 1.000 214.811 0 213 GLU AAA CD  1 ? 2  
ATOM 5071  O OE1 . GLU C 1 213 ? 20.941  54.429  57.286 1.000 214.070 0 213 GLU AAA OE1 1 ? 2  
ATOM 5072  O OE2 . GLU C 1 213 ? 20.516  55.973  55.785 1.000 225.974 0 213 GLU AAA OE2 1 ? 2  
ATOM 5073  N N   . MET C 1 214 ? 24.615  54.969  61.001 1.000 159.682 0 214 MET AAA N   1 ? 2  
ATOM 5074  C CA  . MET C 1 214 ? 24.915  54.421  62.327 1.000 159.146 0 214 MET AAA CA  1 ? 2  
ATOM 5075  C C   . MET C 1 214 ? 25.843  55.325  63.145 1.000 158.935 0 214 MET AAA C   1 ? 2  
ATOM 5076  O O   . MET C 1 214 ? 25.618  55.520  64.345 1.000 175.956 0 214 MET AAA O   1 ? 2  
ATOM 5077  C CB  A MET C 1 214 ? 25.377  52.971  62.191 1.000 151.342 0 214 MET AAA CB  1 ? 2  
ATOM 5078  C CG  A MET C 1 214 ? 26.507  52.641  61.280 1.000 159.043 0 214 MET AAA CG  1 ? 2  
ATOM 5079  S SD  A MET C 1 214 ? 26.602  50.838  61.279 1.000 159.994 0 214 MET AAA SD  1 ? 2  
ATOM 5080  C CE  A MET C 1 214 ? 27.660  50.558  62.680 1.000 168.157 0 214 MET AAA CE  1 ? 2  
ATOM 5081  N N   . MET C 1 215 ? 26.894  55.879  62.537 1.000 150.894 0 215 MET AAA N   1 ? 2  
ATOM 5082  C CA  . MET C 1 215 ? 27.803  56.733  63.311 1.000 153.780 0 215 MET AAA CA  1 ? 2  
ATOM 5083  C C   . MET C 1 215 ? 27.115  58.011  63.783 1.000 165.793 0 215 MET AAA C   1 ? 2  
ATOM 5084  O O   . MET C 1 215 ? 27.392  58.496  64.884 1.000 180.264 0 215 MET AAA O   1 ? 2  
ATOM 5085  C CB  . MET C 1 215 ? 29.046  57.089  62.502 1.000 154.387 0 215 MET AAA CB  1 ? 2  
ATOM 5086  C CG  . MET C 1 215 ? 30.016  55.966  62.211 1.000 144.947 0 215 MET AAA CG  1 ? 2  
ATOM 5087  S SD  . MET C 1 215 ? 31.489  56.664  61.453 1.000 140.634 0 215 MET AAA SD  1 ? 2  
ATOM 5088  C CE  . MET C 1 215 ? 32.064  57.736  62.763 1.000 147.688 0 215 MET AAA CE  1 ? 2  
ATOM 5089  N N   . THR C 1 216 ? 26.230  58.583  62.957 1.000 168.612 0 216 THR AAA N   1 ? 2  
ATOM 5090  C CA  . THR C 1 216 ? 25.440  59.740  63.380 1.000 183.322 0 216 THR AAA CA  1 ? 2  
ATOM 5091  C C   . THR C 1 216 ? 24.541  59.394  64.563 1.000 194.525 0 216 THR AAA C   1 ? 2  
ATOM 5092  O O   . THR C 1 216 ? 24.458  60.149  65.540 1.000 203.429 0 216 THR AAA O   1 ? 2  
ATOM 5093  C CB  . THR C 1 216 ? 24.618  60.267  62.203 1.000 184.452 0 216 THR AAA CB  1 ? 2  
ATOM 5094  O OG1 . THR C 1 216 ? 25.495  60.607  61.123 1.000 185.862 0 216 THR AAA OG1 1 ? 2  
ATOM 5095  C CG2 . THR C 1 216 ? 23.834  61.506  62.611 1.000 193.891 0 216 THR AAA CG2 1 ? 2  
ATOM 5096  N N   . ALA C 1 217 ? 23.855  58.254  64.482 1.000 193.227 0 217 ALA AAA N   1 ? 2  
ATOM 5097  C CA  . ALA C 1 217 ? 22.936  57.804  65.527 1.000 190.500 0 217 ALA AAA CA  1 ? 2  
ATOM 5098  C C   . ALA C 1 217 ? 23.637  57.693  66.878 1.000 186.269 0 217 ALA AAA C   1 ? 2  
ATOM 5099  O O   . ALA C 1 217 ? 23.079  58.076  67.913 1.000 202.362 0 217 ALA AAA O   1 ? 2  
ATOM 5100  C CB  . ALA C 1 217 ? 22.313  56.465  65.133 1.000 178.721 0 217 ALA AAA CB  1 ? 2  
ATOM 5101  N N   . CYS C 1 218 ? 24.866  57.190  66.878 1.000 175.103 0 218 CYS AAA N   1 ? 2  
ATOM 5102  C CA  . CYS C 1 218 ? 25.687  56.937  68.055 1.000 180.570 0 218 CYS AAA CA  1 ? 2  
ATOM 5103  C C   . CYS C 1 218 ? 26.576  58.121  68.426 1.000 187.104 0 218 CYS AAA C   1 ? 2  
ATOM 5104  O O   . CYS C 1 218 ? 27.437  57.985  69.302 1.000 196.925 0 218 CYS AAA O   1 ? 2  
ATOM 5105  C CB  . CYS C 1 218 ? 26.541  55.685  67.847 1.000 175.446 0 218 CYS AAA CB  1 ? 2  
ATOM 5106  S SG  . CYS C 1 218 ? 25.603  54.142  67.900 1.000 171.155 0 218 CYS AAA SG  1 ? 2  
ATOM 5107  N N   . GLN C 1 219 ? 26.389  59.267  67.781 1.000 190.243 0 219 GLN AAA N   1 ? 2  
ATOM 5108  C CA  . GLN C 1 219 ? 27.140  60.470  68.117 1.000 194.110 0 219 GLN AAA CA  1 ? 2  
ATOM 5109  C C   . GLN C 1 219 ? 26.620  61.037  69.430 1.000 205.096 0 219 GLN AAA C   1 ? 2  
ATOM 5110  O O   . GLN C 1 219 ? 27.306  60.991  70.454 1.000 218.162 0 219 GLN AAA O   1 ? 2  
ATOM 5111  C CB  . GLN C 1 219 ? 26.922  61.555  67.057 1.000 190.288 0 219 GLN AAA CB  1 ? 2  
ATOM 5112  C CG  . GLN C 1 219 ? 27.820  61.614  65.848 1.000 193.693 0 219 GLN AAA CG  1 ? 2  
ATOM 5113  C CD  . GLN C 1 219 ? 27.257  62.593  64.826 1.000 190.724 0 219 GLN AAA CD  1 ? 2  
ATOM 5114  O OE1 . GLN C 1 219 ? 26.214  63.209  65.059 1.000 190.702 0 219 GLN AAA OE1 1 ? 2  
ATOM 5115  N NE2 . GLN C 1 219 ? 27.934  62.734  63.691 1.000 178.923 0 219 GLN AAA NE2 1 ? 2  
ATOM 5116  N N   . ASP D 2 1   ? 83.413  109.009 85.188 1.000 148.881 0 1   ASP FFF N   1 ? 7  
ATOM 5117  C CA  . ASP D 2 1   ? 83.012  108.277 83.993 1.000 145.218 0 1   ASP FFF CA  1 ? 7  
ATOM 5118  C C   . ASP D 2 1   ? 83.768  108.788 82.776 1.000 135.567 0 1   ASP FFF C   1 ? 7  
ATOM 5119  O O   . ASP D 2 1   ? 84.928  108.444 82.559 1.000 137.804 0 1   ASP FFF O   1 ? 7  
ATOM 5120  C CB  . ASP D 2 1   ? 81.505  108.403 83.764 1.000 139.435 0 1   ASP FFF CB  1 ? 7  
ATOM 5121  C CG  . ASP D 2 1   ? 80.910  107.164 83.132 1.000 147.590 0 1   ASP FFF CG  1 ? 7  
ATOM 5122  O OD1 . ASP D 2 1   ? 81.635  106.155 83.008 1.000 152.542 0 1   ASP FFF OD1 1 ? 7  
ATOM 5123  O OD2 . ASP D 2 1   ? 79.717  107.199 82.764 1.000 151.824 0 1   ASP FFF OD2 1 ? 7  
ATOM 5124  N N   . VAL D 2 2   ? 83.093  109.615 81.986 1.000 128.935 0 2   VAL FFF N   1 ? 7  
ATOM 5125  C CA  . VAL D 2 2   ? 83.661  110.221 80.789 1.000 128.975 0 2   VAL FFF CA  1 ? 7  
ATOM 5126  C C   . VAL D 2 2   ? 83.694  111.722 81.004 1.000 125.043 0 2   VAL FFF C   1 ? 7  
ATOM 5127  O O   . VAL D 2 2   ? 82.655  112.335 81.281 1.000 117.481 0 2   VAL FFF O   1 ? 7  
ATOM 5128  C CB  . VAL D 2 2   ? 82.861  109.874 79.527 1.000 132.189 0 2   VAL FFF CB  1 ? 7  
ATOM 5129  C CG1 . VAL D 2 2   ? 83.479  110.557 78.318 1.000 125.260 0 2   VAL FFF CG1 1 ? 7  
ATOM 5130  C CG2 . VAL D 2 2   ? 82.806  108.367 79.337 1.000 145.234 0 2   VAL FFF CG2 1 ? 7  
ATOM 5131  N N   . GLN D 2 3   ? 84.878  112.312 80.881 1.000 129.164 0 3   GLN FFF N   1 ? 7  
ATOM 5132  C CA  . GLN D 2 3   ? 85.055  113.733 81.119 1.000 132.145 0 3   GLN FFF CA  1 ? 7  
ATOM 5133  C C   . GLN D 2 3   ? 85.515  114.433 79.849 1.000 130.018 0 3   GLN FFF C   1 ? 7  
ATOM 5134  O O   . GLN D 2 3   ? 86.399  113.942 79.140 1.000 124.692 0 3   GLN FFF O   1 ? 7  
ATOM 5135  C CB  . GLN D 2 3   ? 86.067  113.982 82.232 1.000 130.881 0 3   GLN FFF CB  1 ? 7  
ATOM 5136  C CG  . GLN D 2 3   ? 85.643  113.399 83.559 1.000 131.883 0 3   GLN FFF CG  1 ? 7  
ATOM 5137  C CD  . GLN D 2 3   ? 84.455  114.121 84.149 1.000 137.616 0 3   GLN FFF CD  1 ? 7  
ATOM 5138  O OE1 . GLN D 2 3   ? 84.342  115.344 84.050 1.000 132.734 0 3   GLN FFF OE1 1 ? 7  
ATOM 5139  N NE2 . GLN D 2 3   ? 83.567  113.367 84.788 1.000 144.549 0 3   GLN FFF NE2 1 ? 7  
ATOM 5140  N N   . LEU D 2 4   ? 84.919  115.594 79.585 1.000 128.317 0 4   LEU FFF N   1 ? 7  
ATOM 5141  C CA  . LEU D 2 4   ? 85.272  116.424 78.445 1.000 143.854 0 4   LEU FFF CA  1 ? 7  
ATOM 5142  C C   . LEU D 2 4   ? 85.611  117.811 78.957 1.000 159.160 0 4   LEU FFF C   1 ? 7  
ATOM 5143  O O   . LEU D 2 4   ? 84.979  118.301 79.899 1.000 162.723 0 4   LEU FFF O   1 ? 7  
ATOM 5144  C CB  . LEU D 2 4   ? 84.109  116.532 77.453 1.000 144.227 0 4   LEU FFF CB  1 ? 7  
ATOM 5145  C CG  . LEU D 2 4   ? 83.618  115.297 76.699 1.000 142.933 0 4   LEU FFF CG  1 ? 7  
ATOM 5146  C CD1 . LEU D 2 4   ? 82.380  115.633 75.876 1.000 139.703 0 4   LEU FFF CD1 1 ? 7  
ATOM 5147  C CD2 . LEU D 2 4   ? 84.713  114.753 75.811 1.000 143.326 0 4   LEU FFF CD2 1 ? 7  
ATOM 5148  N N   . GLN D 2 5   ? 86.595  118.451 78.329 1.000 177.782 0 5   GLN FFF N   1 ? 7  
ATOM 5149  C CA  . GLN D 2 5   ? 86.943  119.827 78.664 1.000 187.669 0 5   GLN FFF CA  1 ? 7  
ATOM 5150  C C   . GLN D 2 5   ? 87.366  120.568 77.410 1.000 187.860 0 5   GLN FFF C   1 ? 7  
ATOM 5151  O O   . GLN D 2 5   ? 88.317  120.157 76.737 1.000 183.122 0 5   GLN FFF O   1 ? 7  
ATOM 5152  C CB  . GLN D 2 5   ? 88.060  119.882 79.704 1.000 196.349 0 5   GLN FFF CB  1 ? 7  
ATOM 5153  C CG  . GLN D 2 5   ? 88.381  121.292 80.155 1.000 218.888 0 5   GLN FFF CG  1 ? 7  
ATOM 5154  C CD  . GLN D 2 5   ? 87.139  122.030 80.617 1.000 225.851 0 5   GLN FFF CD  1 ? 7  
ATOM 5155  O OE1 . GLN D 2 5   ? 86.562  121.706 81.655 1.000 232.608 0 5   GLN FFF OE1 1 ? 7  
ATOM 5156  N NE2 . GLN D 2 5   ? 86.724  123.031 79.850 1.000 223.473 0 5   GLN FFF NE2 1 ? 7  
ATOM 5157  N N   . GLU D 2 6   ? 86.676  121.658 77.098 1.000 187.254 0 6   GLU FFF N   1 ? 7  
ATOM 5158  C CA  . GLU D 2 6   ? 87.146  122.463 75.987 1.000 181.704 0 6   GLU FFF CA  1 ? 7  
ATOM 5159  C C   . GLU D 2 6   ? 88.291  123.345 76.452 1.000 182.400 0 6   GLU FFF C   1 ? 7  
ATOM 5160  O O   . GLU D 2 6   ? 88.456  123.613 77.645 1.000 185.952 0 6   GLU FFF O   1 ? 7  
ATOM 5161  C CB  . GLU D 2 6   ? 86.044  123.380 75.456 1.000 183.315 0 6   GLU FFF CB  1 ? 7  
ATOM 5162  C CG  . GLU D 2 6   ? 84.782  122.697 75.016 1.000 180.012 0 6   GLU FFF CG  1 ? 7  
ATOM 5163  C CD  . GLU D 2 6   ? 83.845  122.462 76.177 1.000 181.407 0 6   GLU FFF CD  1 ? 7  
ATOM 5164  O OE1 . GLU D 2 6   ? 84.335  122.334 77.319 1.000 189.595 0 6   GLU FFF OE1 1 ? 7  
ATOM 5165  O OE2 . GLU D 2 6   ? 82.620  122.418 75.955 1.000 180.169 0 6   GLU FFF OE2 1 ? 7  
ATOM 5166  N N   . SER D 2 7   ? 89.081  123.811 75.494 1.000 175.839 0 7   SER FFF N   1 ? 7  
ATOM 5167  C CA  . SER D 2 7   ? 90.138  124.758 75.816 1.000 181.578 0 7   SER FFF CA  1 ? 7  
ATOM 5168  C C   . SER D 2 7   ? 90.677  125.347 74.522 1.000 186.919 0 7   SER FFF C   1 ? 7  
ATOM 5169  O O   . SER D 2 7   ? 90.373  124.876 73.422 1.000 193.427 0 7   SER FFF O   1 ? 7  
ATOM 5170  C CB  . SER D 2 7   ? 91.262  124.094 76.616 1.000 187.181 0 7   SER FFF CB  1 ? 7  
ATOM 5171  O OG  . SER D 2 7   ? 91.931  123.113 75.840 1.000 181.104 0 7   SER FFF OG  1 ? 7  
ATOM 5172  N N   . GLY D 2 8   ? 91.499  126.379 74.676 1.000 192.806 0 8   GLY FFF N   1 ? 7  
ATOM 5173  C CA  . GLY D 2 8   ? 92.078  127.093 73.563 1.000 206.920 0 8   GLY FFF CA  1 ? 7  
ATOM 5174  C C   . GLY D 2 8   ? 91.291  128.311 73.140 1.000 215.300 0 8   GLY FFF C   1 ? 7  
ATOM 5175  O O   . GLY D 2 8   ? 91.698  128.999 72.195 1.000 216.382 0 8   GLY FFF O   1 ? 7  
ATOM 5176  N N   . GLY D 2 9   ? 90.167  128.588 73.808 1.000 220.074 0 9   GLY FFF N   1 ? 7  
ATOM 5177  C CA  . GLY D 2 9   ? 89.336  129.727 73.488 1.000 223.404 0 9   GLY FFF CA  1 ? 7  
ATOM 5178  C C   . GLY D 2 9   ? 89.706  131.035 74.145 1.000 233.599 0 9   GLY FFF C   1 ? 7  
ATOM 5179  O O   . GLY D 2 9   ? 90.366  131.115 75.177 1.000 240.524 0 9   GLY FFF O   1 ? 7  
ATOM 5180  N N   . GLY D 2 10  ? 89.231  132.102 73.520 1.000 236.531 0 10  GLY FFF N   1 ? 7  
ATOM 5181  C CA  . GLY D 2 10  ? 89.494  133.427 74.033 1.000 245.248 0 10  GLY FFF CA  1 ? 7  
ATOM 5182  C C   . GLY D 2 10  ? 88.944  134.452 73.072 1.000 250.484 0 10  GLY FFF C   1 ? 7  
ATOM 5183  O O   . GLY D 2 10  ? 88.080  134.153 72.248 1.000 250.388 0 10  GLY FFF O   1 ? 7  
ATOM 5184  N N   . LEU D 2 11  ? 89.466  135.658 73.192 1.000 249.889 0 11  LEU FFF N   1 ? 7  
ATOM 5185  C CA  . LEU D 2 11  ? 88.991  136.813 72.452 1.000 253.508 0 11  LEU FFF CA  1 ? 7  
ATOM 5186  C C   . LEU D 2 11  ? 90.025  137.211 71.411 1.000 260.068 0 11  LEU FFF C   1 ? 7  
ATOM 5187  O O   . LEU D 2 11  ? 91.204  137.363 71.742 1.000 268.205 0 11  LEU FFF O   1 ? 7  
ATOM 5188  C CB  . LEU D 2 11  ? 88.703  138.021 73.343 1.000 252.746 0 11  LEU FFF CB  1 ? 7  
ATOM 5189  C CG  . LEU D 2 11  ? 87.647  138.154 74.436 1.000 249.133 0 11  LEU FFF CG  1 ? 7  
ATOM 5190  C CD1 . LEU D 2 11  ? 88.101  137.632 75.806 1.000 245.492 0 11  LEU FFF CD1 1 ? 7  
ATOM 5191  C CD2 . LEU D 2 11  ? 87.200  139.602 74.463 1.000 247.798 0 11  LEU FFF CD2 1 ? 7  
ATOM 5192  N N   . VAL D 2 12  ? 89.587  137.381 70.161 1.000 263.304 0 12  VAL FFF N   1 ? 7  
ATOM 5193  C CA  . VAL D 2 12  ? 90.473  137.704 69.050 1.000 259.066 0 12  VAL FFF CA  1 ? 7  
ATOM 5194  C C   . VAL D 2 12  ? 89.676  138.719 68.238 1.000 260.284 0 12  VAL FFF C   1 ? 7  
ATOM 5195  O O   . VAL D 2 12  ? 88.447  138.769 68.306 1.000 264.516 0 12  VAL FFF O   1 ? 7  
ATOM 5196  C CB  . VAL D 2 12  ? 90.875  136.446 68.222 1.000 252.569 0 12  VAL FFF CB  1 ? 7  
ATOM 5197  C CG1 . VAL D 2 12  ? 91.610  136.795 66.925 1.000 248.895 0 12  VAL FFF CG1 1 ? 7  
ATOM 5198  C CG2 . VAL D 2 12  ? 91.725  135.486 69.057 1.000 255.030 0 12  VAL FFF CG2 1 ? 7  
ATOM 5199  N N   . GLN D 2 13  ? 90.381  139.536 67.465 1.000 262.940 0 13  GLN FFF N   1 ? 7  
ATOM 5200  C CA  . GLN D 2 13  ? 89.736  140.479 66.565 1.000 270.800 0 13  GLN FFF CA  1 ? 7  
ATOM 5201  C C   . GLN D 2 13  ? 89.276  139.856 65.249 1.000 273.663 0 13  GLN FFF C   1 ? 7  
ATOM 5202  O O   . GLN D 2 13  ? 89.681  138.758 64.857 1.000 281.313 0 13  GLN FFF O   1 ? 7  
ATOM 5203  C CB  . GLN D 2 13  ? 90.640  141.689 66.370 1.000 274.514 0 13  GLN FFF CB  1 ? 7  
ATOM 5204  C CG  . GLN D 2 13  ? 90.755  142.439 67.696 1.000 275.723 0 13  GLN FFF CG  1 ? 7  
ATOM 5205  C CD  . GLN D 2 13  ? 91.249  143.846 67.546 1.000 288.272 0 13  GLN FFF CD  1 ? 7  
ATOM 5206  O OE1 . GLN D 2 13  ? 91.731  144.237 66.485 1.000 293.513 0 13  GLN FFF OE1 1 ? 7  
ATOM 5207  N NE2 . GLN D 2 13  ? 91.107  144.637 68.605 1.000 294.935 0 13  GLN FFF NE2 1 ? 7  
ATOM 5208  N N   . ALA D 2 14  ? 88.381  140.590 64.587 1.000 274.592 0 14  ALA FFF N   1 ? 7  
ATOM 5209  C CA  . ALA D 2 14  ? 87.862  140.225 63.276 1.000 267.171 0 14  ALA FFF CA  1 ? 7  
ATOM 5210  C C   . ALA D 2 14  ? 88.967  140.036 62.245 1.000 268.963 0 14  ALA FFF C   1 ? 7  
ATOM 5211  O O   . ALA D 2 14  ? 89.991  140.726 62.252 1.000 272.579 0 14  ALA FFF O   1 ? 7  
ATOM 5212  C CB  . ALA D 2 14  ? 86.872  141.285 62.795 1.000 262.676 0 14  ALA FFF CB  1 ? 7  
ATOM 5213  N N   . GLY D 2 15  ? 88.728  139.070 61.362 1.000 261.700 0 15  GLY FFF N   1 ? 7  
ATOM 5214  C CA  . GLY D 2 15  ? 89.595  138.590 60.312 1.000 257.423 0 15  GLY FFF CA  1 ? 7  
ATOM 5215  C C   . GLY D 2 15  ? 90.652  137.620 60.776 1.000 253.952 0 15  GLY FFF C   1 ? 7  
ATOM 5216  O O   . GLY D 2 15  ? 91.423  137.125 59.946 1.000 253.679 0 15  GLY FFF O   1 ? 7  
ATOM 5217  N N   . GLY D 2 16  ? 90.717  137.338 62.075 1.000 261.021 0 16  GLY FFF N   1 ? 7  
ATOM 5218  C CA  . GLY D 2 16  ? 91.696  136.423 62.611 1.000 262.273 0 16  GLY FFF CA  1 ? 7  
ATOM 5219  C C   . GLY D 2 16  ? 91.230  134.989 62.473 1.000 261.026 0 16  GLY FFF C   1 ? 7  
ATOM 5220  O O   . GLY D 2 16  ? 90.185  134.688 61.898 1.000 253.318 0 16  GLY FFF O   1 ? 7  
ATOM 5221  N N   . SER D 2 17  ? 92.041  134.086 63.013 1.000 266.157 0 17  SER FFF N   1 ? 7  
ATOM 5222  C CA  . SER D 2 17  ? 91.750  132.664 63.010 1.000 262.926 0 17  SER FFF CA  1 ? 7  
ATOM 5223  C C   . SER D 2 17  ? 91.995  132.139 64.419 1.000 255.832 0 17  SER FFF C   1 ? 7  
ATOM 5224  O O   . SER D 2 17  ? 92.749  132.730 65.196 1.000 261.046 0 17  SER FFF O   1 ? 7  
ATOM 5225  C CB  . SER D 2 17  ? 92.590  131.902 61.972 1.000 273.203 0 17  SER FFF CB  1 ? 7  
ATOM 5226  O OG  . SER D 2 17  ? 93.971  132.191 62.102 1.000 286.783 0 17  SER FFF OG  1 ? 7  
ATOM 5227  N N   . LEU D 2 18  ? 91.358  131.021 64.751 1.000 238.583 0 18  LEU FFF N   1 ? 7  
ATOM 5228  C CA  . LEU D 2 18  ? 91.541  130.450 66.078 1.000 222.717 0 18  LEU FFF CA  1 ? 7  
ATOM 5229  C C   . LEU D 2 18  ? 91.237  128.963 65.992 1.000 215.511 0 18  LEU FFF C   1 ? 7  
ATOM 5230  O O   . LEU D 2 18  ? 90.439  128.529 65.158 1.000 218.547 0 18  LEU FFF O   1 ? 7  
ATOM 5231  C CB  . LEU D 2 18  ? 90.676  131.146 67.135 1.000 214.800 0 18  LEU FFF CB  1 ? 7  
ATOM 5232  C CG  . LEU D 2 18  ? 91.009  130.731 68.570 1.000 206.619 0 18  LEU FFF CG  1 ? 7  
ATOM 5233  C CD1 . LEU D 2 18  ? 92.480  130.999 68.857 1.000 209.545 0 18  LEU FFF CD1 1 ? 7  
ATOM 5234  C CD2 . LEU D 2 18  ? 90.139  131.472 69.566 1.000 205.412 0 18  LEU FFF CD2 1 ? 7  
ATOM 5235  N N   . ARG D 2 19  ? 91.867  128.189 66.873 1.000 206.813 0 19  ARG FFF N   1 ? 7  
ATOM 5236  C CA  . ARG D 2 19  ? 91.656  126.746 66.932 1.000 197.940 0 19  ARG FFF CA  1 ? 7  
ATOM 5237  C C   . ARG D 2 19  ? 91.295  126.330 68.350 1.000 191.014 0 19  ARG FFF C   1 ? 7  
ATOM 5238  O O   . ARG D 2 19  ? 92.126  126.417 69.259 1.000 195.874 0 19  ARG FFF O   1 ? 7  
ATOM 5239  C CB  . ARG D 2 19  ? 92.916  126.015 66.465 1.000 199.436 0 19  ARG FFF CB  1 ? 7  
ATOM 5240  C CG  . ARG D 2 19  ? 92.907  124.501 66.604 1.000 190.891 0 19  ARG FFF CG  1 ? 7  
ATOM 5241  C CD  . ARG D 2 19  ? 94.120  123.924 65.886 1.000 194.109 0 19  ARG FFF CD  1 ? 7  
ATOM 5242  N NE  . ARG D 2 19  ? 93.965  122.524 65.514 1.000 195.294 0 19  ARG FFF NE  1 ? 7  
ATOM 5243  C CZ  . ARG D 2 19  ? 93.611  122.107 64.306 1.000 194.874 0 19  ARG FFF CZ  1 ? 7  
ATOM 5244  N NH1 . ARG D 2 19  ? 93.354  122.961 63.328 1.000 199.238 0 19  ARG FFF NH1 1 ? 7  
ATOM 5245  N NH2 . ARG D 2 19  ? 93.529  120.801 64.068 1.000 184.770 0 19  ARG FFF NH2 1 ? 7  
ATOM 5246  N N   . LEU D 2 20  ? 90.061  125.873 68.529 1.000 189.175 0 20  LEU FFF N   1 ? 7  
ATOM 5247  C CA  . LEU D 2 20  ? 89.611  125.343 69.805 1.000 183.166 0 20  LEU FFF CA  1 ? 7  
ATOM 5248  C C   . LEU D 2 20  ? 89.918  123.852 69.859 1.000 184.108 0 20  LEU FFF C   1 ? 7  
ATOM 5249  O O   . LEU D 2 20  ? 89.888  123.157 68.839 1.000 188.346 0 20  LEU FFF O   1 ? 7  
ATOM 5250  C CB  . LEU D 2 20  ? 88.114  125.588 70.005 1.000 178.602 0 20  LEU FFF CB  1 ? 7  
ATOM 5251  C CG  . LEU D 2 20  ? 87.630  127.012 69.716 1.000 184.172 0 20  LEU FFF CG  1 ? 7  
ATOM 5252  C CD1 . LEU D 2 20  ? 86.122  127.135 69.919 1.000 178.705 0 20  LEU FFF CD1 1 ? 7  
ATOM 5253  C CD2 . LEU D 2 20  ? 88.390  128.029 70.546 1.000 200.691 0 20  LEU FFF CD2 1 ? 7  
ATOM 5254  N N   . SER D 2 21  ? 90.214  123.359 71.060 1.000 180.761 0 21  SER FFF N   1 ? 7  
ATOM 5255  C CA  . SER D 2 21  ? 90.538  121.950 71.236 1.000 179.878 0 21  SER FFF CA  1 ? 7  
ATOM 5256  C C   . SER D 2 21  ? 89.831  121.402 72.465 1.000 176.224 0 21  SER FFF C   1 ? 7  
ATOM 5257  O O   . SER D 2 21  ? 89.789  122.046 73.518 1.000 179.210 0 21  SER FFF O   1 ? 7  
ATOM 5258  C CB  . SER D 2 21  ? 92.051  121.729 71.356 1.000 184.525 0 21  SER FFF CB  1 ? 7  
ATOM 5259  O OG  . SER D 2 21  ? 92.727  122.224 70.214 1.000 195.589 0 21  SER FFF OG  1 ? 7  
ATOM 5260  N N   . CYS D 2 22  ? 89.288  120.197 72.315 1.000 163.801 0 22  CYS FFF N   1 ? 7  
ATOM 5261  C CA  . CYS D 2 22  ? 88.496  119.528 73.340 1.000 161.130 0 22  CYS FFF CA  1 ? 7  
ATOM 5262  C C   . CYS D 2 22  ? 89.184  118.225 73.731 1.000 152.958 0 22  CYS FFF C   1 ? 7  
ATOM 5263  O O   . CYS D 2 22  ? 89.246  117.282 72.933 1.000 154.081 0 22  CYS FFF O   1 ? 7  
ATOM 5264  C CB  . CYS D 2 22  ? 87.070  119.288 72.841 1.000 175.775 0 22  CYS FFF CB  1 ? 7  
ATOM 5265  S SG  . CYS D 2 22  ? 86.005  118.313 73.926 1.000 183.415 0 22  CYS FFF SG  1 ? 7  
ATOM 5266  N N   . ALA D 2 23  ? 89.668  118.167 74.969 1.000 152.570 0 23  ALA FFF N   1 ? 7  
ATOM 5267  C CA  . ALA D 2 23  ? 90.342  116.992 75.497 1.000 142.393 0 23  ALA FFF CA  1 ? 7  
ATOM 5268  C C   . ALA D 2 23  ? 89.306  116.060 76.107 1.000 133.707 0 23  ALA FFF C   1 ? 7  
ATOM 5269  O O   . ALA D 2 23  ? 88.423  116.489 76.854 1.000 134.222 0 23  ALA FFF O   1 ? 7  
ATOM 5270  C CB  . ALA D 2 23  ? 91.376  117.391 76.550 1.000 164.106 0 23  ALA FFF CB  1 ? 7  
ATOM 5271  N N   . ALA D 2 24  ? 89.438  114.777 75.798 1.000 130.652 0 24  ALA FFF N   1 ? 7  
ATOM 5272  C CA  . ALA D 2 24  ? 88.515  113.743 76.237 1.000 128.463 0 24  ALA FFF CA  1 ? 7  
ATOM 5273  C C   . ALA D 2 24  ? 89.252  112.682 77.037 1.000 129.683 0 24  ALA FFF C   1 ? 7  
ATOM 5274  O O   . ALA D 2 24  ? 90.408  112.357 76.749 1.000 131.925 0 24  ALA FFF O   1 ? 7  
ATOM 5275  C CB  . ALA D 2 24  ? 87.796  113.100 75.047 1.000 130.102 0 24  ALA FFF CB  1 ? 7  
ATOM 5276  N N   . SER D 2 25  ? 88.576  112.155 78.049 1.000 125.124 0 25  SER FFF N   1 ? 7  
ATOM 5277  C CA  . SER D 2 25  ? 89.130  111.028 78.770 1.000 137.746 0 25  SER FFF CA  1 ? 7  
ATOM 5278  C C   . SER D 2 25  ? 88.960  109.735 77.981 1.000 152.552 0 25  SER FFF C   1 ? 7  
ATOM 5279  O O   . SER D 2 25  ? 88.077  109.598 77.129 1.000 162.049 0 25  SER FFF O   1 ? 7  
ATOM 5280  C CB  . SER D 2 25  ? 88.451  110.889 80.130 1.000 139.008 0 25  SER FFF CB  1 ? 7  
ATOM 5281  O OG  . SER D 2 25  ? 88.365  109.526 80.503 1.000 148.510 0 25  SER FFF OG  1 ? 7  
ATOM 5282  N N   . GLY D 2 26  ? 89.833  108.777 78.282 1.000 174.864 0 26  GLY FFF N   1 ? 7  
ATOM 5283  C CA  . GLY D 2 26  ? 89.850  107.577 77.489 1.000 177.140 0 26  GLY FFF CA  1 ? 7  
ATOM 5284  C C   . GLY D 2 26  ? 90.362  107.868 76.086 1.000 174.444 0 26  GLY FFF C   1 ? 7  
ATOM 5285  O O   . GLY D 2 26  ? 91.004  108.885 75.809 1.000 180.934 0 26  GLY FFF O   1 ? 7  
ATOM 5286  N N   . SER D 2 27  ? 90.058  106.933 75.199 1.000 155.250 0 27  SER FFF N   1 ? 7  
ATOM 5287  C CA  . SER D 2 27  ? 90.418  106.999 73.791 1.000 156.529 0 27  SER FFF CA  1 ? 7  
ATOM 5288  C C   . SER D 2 27  ? 89.263  107.637 73.031 1.000 158.319 0 27  SER FFF C   1 ? 7  
ATOM 5289  O O   . SER D 2 27  ? 88.095  107.322 73.278 1.000 163.367 0 27  SER FFF O   1 ? 7  
ATOM 5290  C CB  . SER D 2 27  ? 90.737  105.616 73.227 1.000 161.471 0 27  SER FFF CB  1 ? 7  
ATOM 5291  O OG  . SER D 2 27  ? 91.128  105.706 71.866 1.000 170.365 0 27  SER FFF OG  1 ? 7  
ATOM 5292  N N   . ILE D 2 28  ? 89.591  108.547 72.111 1.000 150.986 0 28  ILE FFF N   1 ? 7  
ATOM 5293  C CA  . ILE D 2 28  ? 88.543  109.279 71.416 1.000 136.938 0 28  ILE FFF CA  1 ? 7  
ATOM 5294  C C   . ILE D 2 28  ? 87.861  108.388 70.392 1.000 136.608 0 28  ILE FFF C   1 ? 7  
ATOM 5295  O O   . ILE D 2 28  ? 86.716  108.653 70.006 1.000 142.842 0 28  ILE FFF O   1 ? 7  
ATOM 5296  C CB  . ILE D 2 28  ? 89.127  110.546 70.763 1.000 130.275 0 28  ILE FFF CB  1 ? 7  
ATOM 5297  C CG1 . ILE D 2 28  ? 88.036  111.594 70.563 1.000 125.073 0 28  ILE FFF CG1 1 ? 7  
ATOM 5298  C CG2 . ILE D 2 28  ? 89.787  110.209 69.436 1.000 144.347 0 28  ILE FFF CG2 1 ? 7  
ATOM 5299  C CD1 . ILE D 2 28  ? 88.554  112.934 70.078 1.000 136.901 0 28  ILE FFF CD1 1 ? 7  
ATOM 5300  N N   . SER D 2 29  ? 88.532  107.333 69.936 1.000 137.721 0 29  SER FFF N   1 ? 7  
ATOM 5301  C CA  . SER D 2 29  ? 87.931  106.433 68.968 1.000 141.136 0 29  SER FFF CA  1 ? 7  
ATOM 5302  C C   . SER D 2 29  ? 86.770  105.647 69.569 1.000 140.841 0 29  SER FFF C   1 ? 7  
ATOM 5303  O O   . SER D 2 29  ? 86.049  104.974 68.822 1.000 149.234 0 29  SER FFF O   1 ? 7  
ATOM 5304  C CB  . SER D 2 29  ? 88.986  105.480 68.410 1.000 141.691 0 29  SER FFF CB  1 ? 7  
ATOM 5305  O OG  . SER D 2 29  ? 89.566  104.718 69.450 1.000 149.234 0 29  SER FFF OG  1 ? 7  
ATOM 5306  N N   . ARG D 2 30  ? 86.575  105.706 70.894 1.000 137.317 0 30  ARG FFF N   1 ? 7  
ATOM 5307  C CA  . ARG D 2 30  ? 85.480  104.979 71.524 1.000 141.947 0 30  ARG FFF CA  1 ? 7  
ATOM 5308  C C   . ARG D 2 30  ? 84.145  105.691 71.389 1.000 135.425 0 30  ARG FFF C   1 ? 7  
ATOM 5309  O O   . ARG D 2 30  ? 83.096  105.040 71.458 1.000 131.607 0 30  ARG FFF O   1 ? 7  
ATOM 5310  C CB  . ARG D 2 30  ? 85.733  104.885 73.031 1.000 151.444 0 30  ARG FFF CB  1 ? 7  
ATOM 5311  C CG  . ARG D 2 30  ? 87.020  104.263 73.514 1.000 162.339 0 30  ARG FFF CG  1 ? 7  
ATOM 5312  C CD  . ARG D 2 30  ? 86.961  104.220 75.040 1.000 171.687 0 30  ARG FFF CD  1 ? 7  
ATOM 5313  N NE  . ARG D 2 30  ? 86.553  105.532 75.538 1.000 169.026 0 30  ARG FFF NE  1 ? 7  
ATOM 5314  C CZ  . ARG D 2 30  ? 86.211  105.808 76.790 1.000 162.690 0 30  ARG FFF CZ  1 ? 7  
ATOM 5315  N NH1 . ARG D 2 30  ? 86.238  104.875 77.727 1.000 172.987 0 30  ARG FFF NH1 1 ? 7  
ATOM 5316  N NH2 . ARG D 2 30  ? 85.851  107.050 77.104 1.000 147.579 0 30  ARG FFF NH2 1 ? 7  
ATOM 5317  N N   . PHE D 2 31  ? 84.164  107.006 71.197 1.000 135.022 0 31  PHE FFF N   1 ? 7  
ATOM 5318  C CA  . PHE D 2 31  ? 82.936  107.771 71.052 1.000 129.882 0 31  PHE FFF CA  1 ? 7  
ATOM 5319  C C   . PHE D 2 31  ? 82.281  107.471 69.711 1.000 126.584 0 31  PHE FFF C   1 ? 7  
ATOM 5320  O O   . PHE D 2 31  ? 82.964  107.336 68.693 1.000 129.616 0 31  PHE FFF O   1 ? 7  
ATOM 5321  C CB  . PHE D 2 31  ? 83.249  109.253 71.226 1.000 130.882 0 31  PHE FFF CB  1 ? 7  
ATOM 5322  C CG  . PHE D 2 31  ? 83.845  109.568 72.574 1.000 132.032 0 31  PHE FFF CG  1 ? 7  
ATOM 5323  C CD1 . PHE D 2 31  ? 83.228  109.136 73.737 1.000 130.301 0 31  PHE FFF CD1 1 ? 7  
ATOM 5324  C CD2 . PHE D 2 31  ? 85.054  110.237 72.675 1.000 135.043 0 31  PHE FFF CD2 1 ? 7  
ATOM 5325  C CE1 . PHE D 2 31  ? 83.786  109.398 74.976 1.000 132.411 0 31  PHE FFF CE1 1 ? 7  
ATOM 5326  C CE2 . PHE D 2 31  ? 85.617  110.502 73.911 1.000 135.248 0 31  PHE FFF CE2 1 ? 7  
ATOM 5327  C CZ  . PHE D 2 31  ? 84.982  110.082 75.063 1.000 132.578 0 31  PHE FFF CZ  1 ? 7  
ATOM 5328  N N   . ASN D 2 32  ? 80.949  107.406 69.695 1.000 123.871 0 32  ASN FFF N   1 ? 7  
ATOM 5329  C CA  . ASN D 2 32  ? 80.266  107.135 68.437 1.000 116.890 0 32  ASN FFF CA  1 ? 7  
ATOM 5330  C C   . ASN D 2 32  ? 79.935  108.398 67.656 1.000 113.821 0 32  ASN FFF C   1 ? 7  
ATOM 5331  O O   . ASN D 2 32  ? 79.643  108.310 66.458 1.000 112.879 0 32  ASN FFF O   1 ? 7  
ATOM 5332  C CB  . ASN D 2 32  ? 78.973  106.353 68.690 1.000 112.102 0 32  ASN FFF CB  1 ? 7  
ATOM 5333  C CG  . ASN D 2 32  ? 79.223  105.013 69.349 1.000 114.921 0 32  ASN FFF CG  1 ? 7  
ATOM 5334  O OD1 . ASN D 2 32  ? 80.243  104.370 69.100 1.000 115.419 0 32  ASN FFF OD1 1 ? 7  
ATOM 5335  N ND2 . ASN D 2 32  ? 78.294  104.585 70.200 1.000 118.482 0 32  ASN FFF ND2 1 ? 7  
ATOM 5336  N N   . ALA D 2 33  ? 79.990  109.560 68.298 1.000 119.765 0 33  ALA FFF N   1 ? 7  
ATOM 5337  C CA  . ALA D 2 33  ? 79.776  110.827 67.618 1.000 121.402 0 33  ALA FFF CA  1 ? 7  
ATOM 5338  C C   . ALA D 2 33  ? 80.279  111.940 68.521 1.000 123.180 0 33  ALA FFF C   1 ? 7  
ATOM 5339  O O   . ALA D 2 33  ? 80.136  111.860 69.744 1.000 128.625 0 33  ALA FFF O   1 ? 7  
ATOM 5340  C CB  . ALA D 2 33  ? 78.298  111.034 67.254 1.000 121.304 0 33  ALA FFF CB  1 ? 7  
ATOM 5341  N N   . MET D 2 34  ? 80.875  112.968 67.919 1.000 123.090 0 34  MET FFF N   1 ? 7  
ATOM 5342  C CA  . MET D 2 34  ? 81.270  114.174 68.637 1.000 123.780 0 34  MET FFF CA  1 ? 7  
ATOM 5343  C C   . MET D 2 34  ? 80.970  115.395 67.782 1.000 124.494 0 34  MET FFF C   1 ? 7  
ATOM 5344  O O   . MET D 2 34  ? 80.764  115.296 66.571 1.000 126.867 0 34  MET FFF O   1 ? 7  
ATOM 5345  C CB  . MET D 2 34  ? 82.752  114.190 69.032 1.000 126.182 0 34  MET FFF CB  1 ? 7  
ATOM 5346  C CG  . MET D 2 34  ? 83.272  112.908 69.620 1.000 136.118 0 34  MET FFF CG  1 ? 7  
ATOM 5347  S SD  . MET D 2 34  ? 84.980  113.127 70.128 1.000 148.415 0 34  MET FFF SD  1 ? 7  
ATOM 5348  C CE  . MET D 2 34  ? 84.789  114.356 71.423 1.000 147.569 0 34  MET FFF CE  1 ? 7  
ATOM 5349  N N   . GLY D 2 35  ? 80.944  116.552 68.430 1.000 124.572 0 35  GLY FFF N   1 ? 7  
ATOM 5350  C CA  . GLY D 2 35  ? 80.688  117.784 67.715 1.000 133.143 0 35  GLY FFF CA  1 ? 7  
ATOM 5351  C C   . GLY D 2 35  ? 80.782  118.989 68.625 1.000 136.714 0 35  GLY FFF C   1 ? 7  
ATOM 5352  O O   . GLY D 2 35  ? 81.212  118.893 69.776 1.000 139.862 0 35  GLY FFF O   1 ? 7  
ATOM 5353  N N   . TRP D 2 36  ? 80.354  120.131 68.084 1.000 147.456 0 36  TRP FFF N   1 ? 7  
ATOM 5354  C CA  . TRP D 2 36  ? 80.510  121.440 68.706 1.000 147.633 0 36  TRP FFF CA  1 ? 7  
ATOM 5355  C C   . TRP D 2 36  ? 79.176  122.168 68.608 1.000 158.622 0 36  TRP FFF C   1 ? 7  
ATOM 5356  O O   . TRP D 2 36  ? 78.572  122.217 67.531 1.000 165.398 0 36  TRP FFF O   1 ? 7  
ATOM 5357  C CB  . TRP D 2 36  ? 81.610  122.236 67.988 1.000 147.344 0 36  TRP FFF CB  1 ? 7  
ATOM 5358  C CG  . TRP D 2 36  ? 83.026  121.750 68.227 1.000 150.275 0 36  TRP FFF CG  1 ? 7  
ATOM 5359  C CD1 . TRP D 2 36  ? 83.772  120.979 67.381 1.000 152.787 0 36  TRP FFF CD1 1 ? 7  
ATOM 5360  C CD2 . TRP D 2 36  ? 83.892  122.087 69.322 1.000 157.224 0 36  TRP FFF CD2 1 ? 7  
ATOM 5361  N NE1 . TRP D 2 36  ? 85.024  120.767 67.907 1.000 157.808 0 36  TRP FFF NE1 1 ? 7  
ATOM 5362  C CE2 . TRP D 2 36  ? 85.126  121.442 69.094 1.000 158.642 0 36  TRP FFF CE2 1 ? 7  
ATOM 5363  C CE3 . TRP D 2 36  ? 83.737  122.853 70.482 1.000 161.882 0 36  TRP FFF CE3 1 ? 7  
ATOM 5364  C CZ2 . TRP D 2 36  ? 86.197  121.539 69.983 1.000 160.155 0 36  TRP FFF CZ2 1 ? 7  
ATOM 5365  C CZ3 . TRP D 2 36  ? 84.802  122.948 71.364 1.000 161.074 0 36  TRP FFF CZ3 1 ? 7  
ATOM 5366  C CH2 . TRP D 2 36  ? 86.015  122.294 71.109 1.000 160.832 0 36  TRP FFF CH2 1 ? 7  
ATOM 5367  N N   . TRP D 2 37  ? 78.723  122.740 69.719 1.000 167.764 0 37  TRP FFF N   1 ? 7  
ATOM 5368  C CA  . TRP D 2 37  ? 77.568  123.628 69.749 1.000 177.728 0 37  TRP FFF CA  1 ? 7  
ATOM 5369  C C   . TRP D 2 37  ? 78.009  124.949 70.365 1.000 193.677 0 37  TRP FFF C   1 ? 7  
ATOM 5370  O O   . TRP D 2 37  ? 79.065  125.023 70.999 1.000 202.396 0 37  TRP FFF O   1 ? 7  
ATOM 5371  C CB  . TRP D 2 37  ? 76.428  122.994 70.560 1.000 174.556 0 37  TRP FFF CB  1 ? 7  
ATOM 5372  C CG  . TRP D 2 37  ? 75.681  121.919 69.821 1.000 175.299 0 37  TRP FFF CG  1 ? 7  
ATOM 5373  C CD1 . TRP D 2 37  ? 76.179  120.711 69.431 1.000 178.428 0 37  TRP FFF CD1 1 ? 7  
ATOM 5374  C CD2 . TRP D 2 37  ? 74.288  121.903 69.482 1.000 177.356 0 37  TRP FFF CD2 1 ? 7  
ATOM 5375  N NE1 . TRP D 2 37  ? 75.204  119.969 68.816 1.000 185.701 0 37  TRP FFF NE1 1 ? 7  
ATOM 5376  C CE2 . TRP D 2 37  ? 74.031  120.674 68.841 1.000 186.963 0 37  TRP FFF CE2 1 ? 7  
ATOM 5377  C CE3 . TRP D 2 37  ? 73.239  122.814 69.635 1.000 177.974 0 37  TRP FFF CE3 1 ? 7  
ATOM 5378  C CZ2 . TRP D 2 37  ? 72.774  120.333 68.355 1.000 199.188 0 37  TRP FFF CZ2 1 ? 7  
ATOM 5379  C CZ3 . TRP D 2 37  ? 71.989  122.471 69.151 1.000 186.124 0 37  TRP FFF CZ3 1 ? 7  
ATOM 5380  C CH2 . TRP D 2 37  ? 71.769  121.241 68.519 1.000 201.226 0 37  TRP FFF CH2 1 ? 7  
ATOM 5381  N N   . ARG D 2 38  ? 77.210  126.005 70.178 1.000 198.807 0 38  ARG FFF N   1 ? 7  
ATOM 5382  C CA  . ARG D 2 38  ? 77.524  127.284 70.809 1.000 200.658 0 38  ARG FFF CA  1 ? 7  
ATOM 5383  C C   . ARG D 2 38  ? 76.270  128.007 71.286 1.000 204.591 0 38  ARG FFF C   1 ? 7  
ATOM 5384  O O   . ARG D 2 38  ? 75.173  127.808 70.760 1.000 209.831 0 38  ARG FFF O   1 ? 7  
ATOM 5385  C CB  . ARG D 2 38  ? 78.288  128.250 69.892 1.000 201.975 0 38  ARG FFF CB  1 ? 7  
ATOM 5386  C CG  . ARG D 2 38  ? 77.497  128.799 68.718 1.000 203.195 0 38  ARG FFF CG  1 ? 7  
ATOM 5387  C CD  . ARG D 2 38  ? 78.376  129.728 67.887 1.000 207.565 0 38  ARG FFF CD  1 ? 7  
ATOM 5388  N NE  . ARG D 2 38  ? 77.659  130.356 66.782 1.000 209.746 0 38  ARG FFF NE  1 ? 7  
ATOM 5389  C CZ  . ARG D 2 38  ? 78.243  131.008 65.785 1.000 216.254 0 38  ARG FFF CZ  1 ? 7  
ATOM 5390  N NH1 . ARG D 2 38  ? 79.559  131.134 65.718 1.000 220.743 0 38  ARG FFF NH1 1 ? 7  
ATOM 5391  N NH2 . ARG D 2 38  ? 77.488  131.557 64.838 1.000 219.189 0 38  ARG FFF NH2 1 ? 7  
ATOM 5392  N N   . GLN D 2 39  ? 76.462  128.864 72.293 1.000 206.860 0 39  GLN FFF N   1 ? 7  
ATOM 5393  C CA  . GLN D 2 39  ? 75.422  129.736 72.830 1.000 211.740 0 39  GLN FFF CA  1 ? 7  
ATOM 5394  C C   . GLN D 2 39  ? 75.983  131.118 73.128 1.000 221.229 0 39  GLN FFF C   1 ? 7  
ATOM 5395  O O   . GLN D 2 39  ? 76.978  131.247 73.845 1.000 222.701 0 39  GLN FFF O   1 ? 7  
ATOM 5396  C CB  . GLN D 2 39  ? 74.787  129.191 74.111 1.000 210.260 0 39  GLN FFF CB  1 ? 7  
ATOM 5397  C CG  . GLN D 2 39  ? 73.590  130.040 74.522 1.000 214.367 0 39  GLN FFF CG  1 ? 7  
ATOM 5398  C CD  . GLN D 2 39  ? 72.868  129.543 75.753 1.000 212.701 0 39  GLN FFF CD  1 ? 7  
ATOM 5399  O OE1 . GLN D 2 39  ? 73.148  128.460 76.263 1.000 204.536 0 39  GLN FFF OE1 1 ? 7  
ATOM 5400  N NE2 . GLN D 2 39  ? 71.933  130.348 76.248 1.000 216.976 0 39  GLN FFF NE2 1 ? 7  
ATOM 5401  N N   . ALA D 2 40  ? 75.345  132.136 72.582 1.000 241.048 0 40  ALA FFF N   1 ? 7  
ATOM 5402  C CA  . ALA D 2 40  ? 75.727  133.508 72.863 1.000 247.856 0 40  ALA FFF CA  1 ? 7  
ATOM 5403  C C   . ALA D 2 40  ? 74.828  134.064 73.961 1.000 256.272 0 40  ALA FFF C   1 ? 7  
ATOM 5404  O O   . ALA D 2 40  ? 73.695  133.603 74.129 1.000 268.312 0 40  ALA FFF O   1 ? 7  
ATOM 5405  C CB  . ALA D 2 40  ? 75.607  134.379 71.608 1.000 244.717 0 40  ALA FFF CB  1 ? 7  
ATOM 5406  N N   . PRO D 2 41  ? 75.297  135.032 74.750 1.000 248.769 0 41  PRO FFF N   1 ? 7  
ATOM 5407  C CA  . PRO D 2 41  ? 74.464  135.552 75.848 1.000 246.333 0 41  PRO FFF CA  1 ? 7  
ATOM 5408  C C   . PRO D 2 41  ? 73.137  136.102 75.344 1.000 244.959 0 41  PRO FFF C   1 ? 7  
ATOM 5409  O O   . PRO D 2 41  ? 73.091  137.009 74.511 1.000 248.239 0 41  PRO FFF O   1 ? 7  
ATOM 5410  C CB  . PRO D 2 41  ? 75.344  136.649 76.457 1.000 251.789 0 41  PRO FFF CB  1 ? 7  
ATOM 5411  C CG  . PRO D 2 41  ? 76.737  136.165 76.197 1.000 246.326 0 41  PRO FFF CG  1 ? 7  
ATOM 5412  C CD  . PRO D 2 41  ? 76.673  135.559 74.815 1.000 246.609 0 41  PRO FFF CD  1 ? 7  
ATOM 5413  N N   . GLY D 2 42  ? 72.048  135.529 75.862 1.000 252.095 0 42  GLY FFF N   1 ? 7  
ATOM 5414  C CA  . GLY D 2 42  ? 70.698  135.922 75.518 1.000 246.341 0 42  GLY FFF CA  1 ? 7  
ATOM 5415  C C   . GLY D 2 42  ? 70.130  135.239 74.294 1.000 244.557 0 42  GLY FFF C   1 ? 7  
ATOM 5416  O O   . GLY D 2 42  ? 68.911  135.303 74.077 1.000 234.244 0 42  GLY FFF O   1 ? 7  
ATOM 5417  N N   . LYS D 2 43  ? 70.969  134.589 73.493 1.000 244.548 0 43  LYS FFF N   1 ? 7  
ATOM 5418  C CA  . LYS D 2 43  ? 70.557  133.921 72.271 1.000 241.820 0 43  LYS FFF CA  1 ? 7  
ATOM 5419  C C   . LYS D 2 43  ? 70.507  132.422 72.536 1.000 231.718 0 43  LYS FFF C   1 ? 7  
ATOM 5420  O O   . LYS D 2 43  ? 71.257  131.902 73.366 1.000 236.114 0 43  LYS FFF O   1 ? 7  
ATOM 5421  C CB  . LYS D 2 43  ? 71.524  134.239 71.131 1.000 240.689 0 43  LYS FFF CB  1 ? 7  
ATOM 5422  C CG  . LYS D 2 43  ? 70.925  135.172 70.100 1.000 242.325 0 43  LYS FFF CG  1 ? 7  
ATOM 5423  C CD  . LYS D 2 43  ? 71.868  135.452 68.947 1.000 238.817 0 43  LYS FFF CD  1 ? 7  
ATOM 5424  C CE  . LYS D 2 43  ? 72.396  134.183 68.309 1.000 228.376 0 43  LYS FFF CE  1 ? 7  
ATOM 5425  N NZ  . LYS D 2 43  ? 73.487  134.476 67.348 1.000 228.212 0 43  LYS FFF NZ  1 ? 7  
ATOM 5426  N N   . GLU D 2 44  ? 69.623  131.728 71.831 1.000 217.692 0 44  GLU FFF N   1 ? 7  
ATOM 5427  C CA  . GLU D 2 44  ? 69.494  130.296 72.047 1.000 210.034 0 44  GLU FFF CA  1 ? 7  
ATOM 5428  C C   . GLU D 2 44  ? 70.653  129.528 71.405 1.000 205.980 0 44  GLU FFF C   1 ? 7  
ATOM 5429  O O   . GLU D 2 44  ? 71.241  129.964 70.411 1.000 210.388 0 44  GLU FFF O   1 ? 7  
ATOM 5430  C CB  . GLU D 2 44  ? 68.141  129.845 71.501 1.000 213.345 0 44  GLU FFF CB  1 ? 7  
ATOM 5431  C CG  . GLU D 2 44  ? 66.980  130.513 72.255 1.000 215.330 0 44  GLU FFF CG  1 ? 7  
ATOM 5432  C CD  . GLU D 2 44  ? 65.633  129.856 72.060 1.000 214.666 0 44  GLU FFF CD  1 ? 7  
ATOM 5433  O OE1 . GLU D 2 44  ? 65.604  128.662 71.677 1.000 205.947 0 44  GLU FFF OE1 1 ? 7  
ATOM 5434  O OE2 . GLU D 2 44  ? 64.606  130.508 72.319 1.000 221.549 0 44  GLU FFF OE2 1 ? 7  
ATOM 5435  N N   . ARG D 2 45  ? 70.976  128.374 71.998 1.000 206.286 0 45  ARG FFF N   1 ? 7  
ATOM 5436  C CA  . ARG D 2 45  ? 72.021  127.483 71.491 1.000 204.471 0 45  ARG FFF CA  1 ? 7  
ATOM 5437  C C   . ARG D 2 45  ? 71.867  127.125 70.019 1.000 207.946 0 45  ARG FFF C   1 ? 7  
ATOM 5438  O O   . ARG D 2 45  ? 70.812  126.651 69.591 1.000 211.831 0 45  ARG FFF O   1 ? 7  
ATOM 5439  C CB  . ARG D 2 45  ? 72.089  126.201 72.325 1.000 196.836 0 45  ARG FFF CB  1 ? 7  
ATOM 5440  C CG  . ARG D 2 45  ? 72.739  126.424 73.672 1.000 198.948 0 45  ARG FFF CG  1 ? 7  
ATOM 5441  C CD  . ARG D 2 45  ? 72.168  125.607 74.807 1.000 196.152 0 45  ARG FFF CD  1 ? 7  
ATOM 5442  N NE  . ARG D 2 45  ? 72.772  124.283 74.830 1.000 188.967 0 45  ARG FFF NE  1 ? 7  
ATOM 5443  C CZ  . ARG D 2 45  ? 73.875  123.980 75.513 1.000 187.206 0 45  ARG FFF CZ  1 ? 7  
ATOM 5444  N NH1 . ARG D 2 45  ? 74.508  124.899 76.235 1.000 193.501 0 45  ARG FFF NH1 1 ? 7  
ATOM 5445  N NH2 . ARG D 2 45  ? 74.361  122.752 75.452 1.000 180.772 0 45  ARG FFF NH2 1 ? 7  
ATOM 5446  N N   . GLU D 2 46  ? 72.934  127.341 69.251 1.000 221.545 0 46  GLU FFF N   1 ? 7  
ATOM 5447  C CA  . GLU D 2 46  ? 72.963  127.052 67.824 1.000 216.032 0 46  GLU FFF CA  1 ? 7  
ATOM 5448  C C   . GLU D 2 46  ? 73.987  125.952 67.550 1.000 203.470 0 46  GLU FFF C   1 ? 7  
ATOM 5449  O O   . GLU D 2 46  ? 75.038  125.901 68.195 1.000 201.375 0 46  GLU FFF O   1 ? 7  
ATOM 5450  C CB  . GLU D 2 46  ? 73.274  128.306 66.998 1.000 225.230 0 46  GLU FFF CB  1 ? 7  
ATOM 5451  C CG  . GLU D 2 46  ? 72.462  128.392 65.711 1.000 233.413 0 46  GLU FFF CG  1 ? 7  
ATOM 5452  C CD  . GLU D 2 46  ? 72.820  129.598 64.869 1.000 238.614 0 46  GLU FFF CD  1 ? 7  
ATOM 5453  O OE1 . GLU D 2 46  ? 73.817  130.277 65.196 1.000 239.697 0 46  GLU FFF OE1 1 ? 7  
ATOM 5454  O OE2 . GLU D 2 46  ? 72.109  129.864 63.876 1.000 237.361 0 46  GLU FFF OE2 1 ? 7  
ATOM 5455  N N   . PHE D 2 47  ? 73.668  125.061 66.609 1.000 188.511 0 47  PHE FFF N   1 ? 7  
ATOM 5456  C CA  . PHE D 2 47  ? 74.537  123.937 66.259 1.000 181.305 0 47  PHE FFF CA  1 ? 7  
ATOM 5457  C C   . PHE D 2 47  ? 75.651  124.376 65.313 1.000 177.649 0 47  PHE FFF C   1 ? 7  
ATOM 5458  O O   . PHE D 2 47  ? 75.394  125.092 64.342 1.000 188.288 0 47  PHE FFF O   1 ? 7  
ATOM 5459  C CB  . PHE D 2 47  ? 73.707  122.827 65.609 1.000 185.135 0 47  PHE FFF CB  1 ? 7  
ATOM 5460  C CG  . PHE D 2 47  ? 74.521  121.816 64.840 1.000 181.504 0 47  PHE FFF CG  1 ? 7  
ATOM 5461  C CD1 . PHE D 2 47  ? 75.161  120.771 65.483 1.000 177.417 0 47  PHE FFF CD1 1 ? 7  
ATOM 5462  C CD2 . PHE D 2 47  ? 74.630  121.914 63.460 1.000 183.551 0 47  PHE FFF CD2 1 ? 7  
ATOM 5463  C CE1 . PHE D 2 47  ? 75.900  119.848 64.764 1.000 169.018 0 47  PHE FFF CE1 1 ? 7  
ATOM 5464  C CE2 . PHE D 2 47  ? 75.367  120.998 62.739 1.000 176.238 0 47  PHE FFF CE2 1 ? 7  
ATOM 5465  C CZ  . PHE D 2 47  ? 76.002  119.963 63.390 1.000 168.535 0 47  PHE FFF CZ  1 ? 7  
ATOM 5466  N N   . VAL D 2 48  ? 76.888  123.941 65.579 1.000 166.768 0 48  VAL FFF N   1 ? 7  
ATOM 5467  C CA  . VAL D 2 48  ? 78.046  124.377 64.797 1.000 164.191 0 48  VAL FFF CA  1 ? 7  
ATOM 5468  C C   . VAL D 2 48  ? 78.623  123.242 63.952 1.000 163.093 0 48  VAL FFF C   1 ? 7  
ATOM 5469  O O   . VAL D 2 48  ? 78.685  123.344 62.725 1.000 166.919 0 48  VAL FFF O   1 ? 7  
ATOM 5470  C CB  . VAL D 2 48  ? 79.130  124.990 65.712 1.000 163.110 0 48  VAL FFF CB  1 ? 7  
ATOM 5471  C CG1 . VAL D 2 48  ? 80.326  125.442 64.892 1.000 165.163 0 48  VAL FFF CG1 1 ? 7  
ATOM 5472  C CG2 . VAL D 2 48  ? 78.557  126.147 66.490 1.000 174.340 0 48  VAL FFF CG2 1 ? 7  
ATOM 5473  N N   . ALA D 2 49  ? 79.047  122.150 64.587 1.000 157.419 0 49  ALA FFF N   1 ? 7  
ATOM 5474  C CA  . ALA D 2 49  ? 79.694  121.092 63.820 1.000 151.906 0 49  ALA FFF CA  1 ? 7  
ATOM 5475  C C   . ALA D 2 49  ? 79.410  119.723 64.421 1.000 147.446 0 49  ALA FFF C   1 ? 7  
ATOM 5476  O O   . ALA D 2 49  ? 79.117  119.595 65.612 1.000 150.286 0 49  ALA FFF O   1 ? 7  
ATOM 5477  C CB  . ALA D 2 49  ? 81.208  121.326 63.749 1.000 147.695 0 49  ALA FFF CB  1 ? 7  
ATOM 5478  N N   . ARG D 2 50  ? 79.509  118.696 63.576 1.000 146.610 0 50  ARG FFF N   1 ? 7  
ATOM 5479  C CA  . ARG D 2 50  ? 79.276  117.311 63.971 1.000 139.437 0 50  ARG FFF CA  1 ? 7  
ATOM 5480  C C   . ARG D 2 50  ? 80.217  116.411 63.180 1.000 136.983 0 50  ARG FFF C   1 ? 7  
ATOM 5481  O O   . ARG D 2 50  ? 80.456  116.648 61.995 1.000 146.485 0 50  ARG FFF O   1 ? 7  
ATOM 5482  C CB  . ARG D 2 50  ? 77.830  116.828 63.795 1.000 141.479 0 50  ARG FFF CB  1 ? 7  
ATOM 5483  C CG  . ARG D 2 50  ? 77.323  116.665 62.384 1.000 158.625 0 50  ARG FFF CG  1 ? 7  
ATOM 5484  C CD  . ARG D 2 50  ? 75.938  116.046 62.443 1.000 158.786 0 50  ARG FFF CD  1 ? 7  
ATOM 5485  N NE  . ARG D 2 50  ? 75.114  116.402 61.299 1.000 166.288 0 50  ARG FFF NE  1 ? 7  
ATOM 5486  C CZ  . ARG D 2 50  ? 73.816  116.655 61.378 1.000 175.473 0 50  ARG FFF CZ  1 ? 7  
ATOM 5487  N NH1 . ARG D 2 50  ? 73.174  116.604 62.534 1.000 182.495 0 50  ARG FFF NH1 1 ? 7  
ATOM 5488  N NH2 . ARG D 2 50  ? 73.147  116.973 60.273 1.000 184.960 0 50  ARG FFF NH2 1 ? 7  
ATOM 5489  N N   . ILE D 2 51  ? 80.750  115.386 63.839 1.000 127.530 0 51  ILE FFF N   1 ? 7  
ATOM 5490  C CA  . ILE D 2 51  ? 81.467  114.301 63.170 1.000 128.693 0 51  ILE FFF CA  1 ? 7  
ATOM 5491  C C   . ILE D 2 51  ? 80.927  113.017 63.783 1.000 127.512 0 51  ILE FFF C   1 ? 7  
ATOM 5492  O O   . ILE D 2 51  ? 81.101  112.772 64.982 1.000 140.299 0 51  ILE FFF O   1 ? 7  
ATOM 5493  C CB  . ILE D 2 51  ? 83.001  114.396 63.300 1.000 130.917 0 51  ILE FFF CB  1 ? 7  
ATOM 5494  C CG1 . ILE D 2 51  ? 83.539  115.657 62.612 1.000 144.599 0 51  ILE FFF CG1 1 ? 7  
ATOM 5495  C CG2 . ILE D 2 51  ? 83.678  113.163 62.703 1.000 127.888 0 51  ILE FFF CG2 1 ? 7  
ATOM 5496  C CD1 . ILE D 2 51  ? 85.034  115.590 62.269 1.000 156.590 0 51  ILE FFF CD1 1 ? 7  
ATOM 5497  N N   . VAL D 2 52  ? 80.317  112.181 62.948 1.000 128.137 0 52  VAL FFF N   1 ? 7  
ATOM 5498  C CA  . VAL D 2 52  ? 79.844  110.858 63.334 1.000 128.173 0 52  VAL FFF CA  1 ? 7  
ATOM 5499  C C   . VAL D 2 52  ? 80.767  109.808 62.736 1.000 131.167 0 52  VAL FFF C   1 ? 7  
ATOM 5500  O O   . VAL D 2 52  ? 81.268  109.967 61.617 1.000 137.407 0 52  VAL FFF O   1 ? 7  
ATOM 5501  C CB  . VAL D 2 52  ? 78.383  110.649 62.879 1.000 129.735 0 52  VAL FFF CB  1 ? 7  
ATOM 5502  C CG1 . VAL D 2 52  ? 77.858  109.307 63.347 1.000 130.228 0 52  VAL FFF CG1 1 ? 7  
ATOM 5503  C CG2 . VAL D 2 52  ? 77.492  111.772 63.402 1.000 127.965 0 52  VAL FFF CG2 1 ? 7  
ATOM 5504  N N   . LYS D 2 53  ? 81.027  108.757 63.515 1.000 126.685 0 53  LYS FFF N   1 ? 7  
ATOM 5505  C CA  . LYS D 2 53  ? 82.028  107.763 63.150 1.000 133.455 0 53  LYS FFF CA  1 ? 7  
ATOM 5506  C C   . LYS D 2 53  ? 81.696  107.109 61.816 1.000 144.629 0 53  LYS FFF C   1 ? 7  
ATOM 5507  O O   . LYS D 2 53  ? 80.600  106.576 61.621 1.000 148.058 0 53  LYS FFF O   1 ? 7  
ATOM 5508  C CB  . LYS D 2 53  ? 82.158  106.692 64.235 1.000 131.798 0 53  LYS FFF CB  1 ? 7  
ATOM 5509  C CG  . LYS D 2 53  ? 83.213  106.996 65.293 1.000 134.778 0 53  LYS FFF CG  1 ? 7  
ATOM 5510  C CD  . LYS D 2 53  ? 83.833  105.714 65.836 1.000 130.704 0 53  LYS FFF CD  1 ? 7  
ATOM 5511  C CE  . LYS D 2 53  ? 82.865  104.946 66.717 1.000 130.821 0 53  LYS FFF CE  1 ? 7  
ATOM 5512  N NZ  . LYS D 2 53  ? 83.496  103.724 67.290 1.000 135.581 0 53  LYS FFF NZ  1 ? 7  
ATOM 5513  N N   . GLY D 2 54  ? 82.665  107.155 60.898 1.000 158.570 0 54  GLY FFF N   1 ? 7  
ATOM 5514  C CA  . GLY D 2 54  ? 82.531  106.631 59.557 1.000 163.008 0 54  GLY FFF CA  1 ? 7  
ATOM 5515  C C   . GLY D 2 54  ? 81.978  107.599 58.538 1.000 160.737 0 54  GLY FFF C   1 ? 7  
ATOM 5516  O O   . GLY D 2 54  ? 81.940  107.263 57.346 1.000 174.264 0 54  GLY FFF O   1 ? 7  
ATOM 5517  N N   . PHE D 2 55  ? 81.541  108.777 58.958 1.000 143.362 0 55  PHE FFF N   1 ? 7  
ATOM 5518  C CA  . PHE D 2 55  ? 80.900  109.719 58.063 1.000 145.211 0 55  PHE FFF CA  1 ? 7  
ATOM 5519  C C   . PHE D 2 55  ? 81.808  110.920 57.852 1.000 143.218 0 55  PHE FFF C   1 ? 7  
ATOM 5520  O O   . PHE D 2 55  ? 82.747  111.160 58.615 1.000 140.018 0 55  PHE FFF O   1 ? 7  
ATOM 5521  C CB  . PHE D 2 55  ? 79.556  110.183 58.629 1.000 147.981 0 55  PHE FFF CB  1 ? 7  
ATOM 5522  C CG  . PHE D 2 55  ? 78.510  109.113 58.655 1.000 144.872 0 55  PHE FFF CG  1 ? 7  
ATOM 5523  C CD1 . PHE D 2 55  ? 77.747  108.854 57.534 1.000 158.786 0 55  PHE FFF CD1 1 ? 7  
ATOM 5524  C CD2 . PHE D 2 55  ? 78.283  108.375 59.805 1.000 139.917 0 55  PHE FFF CD2 1 ? 7  
ATOM 5525  C CE1 . PHE D 2 55  ? 76.781  107.870 57.554 1.000 168.127 0 55  PHE FFF CE1 1 ? 7  
ATOM 5526  C CE2 . PHE D 2 55  ? 77.317  107.393 59.833 1.000 141.927 0 55  PHE FFF CE2 1 ? 7  
ATOM 5527  C CZ  . PHE D 2 55  ? 76.587  107.124 58.699 1.000 160.483 0 55  PHE FFF CZ  1 ? 7  
ATOM 5528  N N   . ASP D 2 56  ? 81.517  111.669 56.798 1.000 151.294 0 56  ASP FFF N   1 ? 7  
ATOM 5529  C CA  . ASP D 2 56  ? 82.227  112.902 56.525 1.000 155.682 0 56  ASP FFF CA  1 ? 7  
ATOM 5530  C C   . ASP D 2 56  ? 81.812  113.951 57.556 1.000 155.085 0 56  ASP FFF C   1 ? 7  
ATOM 5531  O O   . ASP D 2 56  ? 80.731  113.858 58.145 1.000 146.223 0 56  ASP FFF O   1 ? 7  
ATOM 5532  C CB  . ASP D 2 56  ? 81.977  113.367 55.095 1.000 169.077 0 56  ASP FFF CB  1 ? 7  
ATOM 5533  C CG  . ASP D 2 56  ? 82.879  112.658 54.090 1.000 182.889 0 56  ASP FFF CG  1 ? 7  
ATOM 5534  O OD1 . ASP D 2 56  ? 83.190  111.461 54.288 1.000 187.282 0 56  ASP FFF OD1 1 ? 7  
ATOM 5535  O OD2 . ASP D 2 56  ? 83.303  113.309 53.115 1.000 190.905 0 56  ASP FFF OD2 1 ? 7  
ATOM 5536  N N   . PRO D 2 57  ? 82.646  114.962 57.793 1.000 168.973 0 57  PRO FFF N   1 ? 7  
ATOM 5537  C CA  . PRO D 2 57  ? 82.230  116.042 58.694 1.000 164.435 0 57  PRO FFF CA  1 ? 7  
ATOM 5538  C C   . PRO D 2 57  ? 81.100  116.866 58.094 1.000 166.717 0 57  PRO FFF C   1 ? 7  
ATOM 5539  O O   . PRO D 2 57  ? 81.089  117.182 56.902 1.000 174.188 0 57  PRO FFF O   1 ? 7  
ATOM 5540  C CB  . PRO D 2 57  ? 83.506  116.878 58.848 1.000 161.358 0 57  PRO FFF CB  1 ? 7  
ATOM 5541  C CG  . PRO D 2 57  ? 84.602  115.883 58.664 1.000 160.153 0 57  PRO FFF CG  1 ? 7  
ATOM 5542  C CD  . PRO D 2 57  ? 84.097  115.008 57.536 1.000 169.623 0 57  PRO FFF CD  1 ? 7  
ATOM 5543  N N   . VAL D 2 58  ? 80.140  117.201 58.953 1.000 148.488 0 58  VAL FFF N   1 ? 7  
ATOM 5544  C CA  . VAL D 2 58  ? 79.022  118.082 58.638 1.000 149.922 0 58  VAL FFF CA  1 ? 7  
ATOM 5545  C C   . VAL D 2 58  ? 79.155  119.360 59.454 1.000 152.803 0 58  VAL FFF C   1 ? 7  
ATOM 5546  O O   . VAL D 2 58  ? 79.443  119.318 60.655 1.000 158.310 0 58  VAL FFF O   1 ? 7  
ATOM 5547  C CB  . VAL D 2 58  ? 77.675  117.387 58.922 1.000 151.526 0 58  VAL FFF CB  1 ? 7  
ATOM 5548  C CG1 . VAL D 2 58  ? 76.508  118.330 58.660 1.000 158.818 0 58  VAL FFF CG1 1 ? 7  
ATOM 5549  C CG2 . VAL D 2 58  ? 77.548  116.120 58.093 1.000 171.003 0 58  VAL FFF CG2 1 ? 7  
ATOM 5550  N N   . LEU D 2 59  ? 78.939  120.494 58.795 1.000 163.363 0 59  LEU FFF N   1 ? 7  
ATOM 5551  C CA  . LEU D 2 59  ? 79.071  121.812 59.395 1.000 169.575 0 59  LEU FFF CA  1 ? 7  
ATOM 5552  C C   . LEU D 2 59  ? 77.765  122.578 59.222 1.000 180.114 0 59  LEU FFF C   1 ? 7  
ATOM 5553  O O   . LEU D 2 59  ? 76.980  122.282 58.317 1.000 188.401 0 59  LEU FFF O   1 ? 7  
ATOM 5554  C CB  . LEU D 2 59  ? 80.206  122.572 58.716 1.000 171.963 0 59  LEU FFF CB  1 ? 7  
ATOM 5555  C CG  . LEU D 2 59  ? 81.595  121.967 58.888 1.000 168.235 0 59  LEU FFF CG  1 ? 7  
ATOM 5556  C CD1 . LEU D 2 59  ? 82.541  122.627 57.916 1.000 172.557 0 59  LEU FFF CD1 1 ? 7  
ATOM 5557  C CD2 . LEU D 2 59  ? 82.085  122.140 60.311 1.000 173.266 0 59  LEU FFF CD2 1 ? 7  
ATOM 5558  N N   . ALA D 2 60  ? 77.505  123.530 60.121 1.000 180.804 0 60  ALA FFF N   1 ? 7  
ATOM 5559  C CA  . ALA D 2 60  ? 76.319  124.365 59.980 1.000 187.162 0 60  ALA FFF CA  1 ? 7  
ATOM 5560  C C   . ALA D 2 60  ? 76.453  125.280 58.760 1.000 198.194 0 60  ALA FFF C   1 ? 7  
ATOM 5561  O O   . ALA D 2 60  ? 77.552  125.558 58.279 1.000 206.643 0 60  ALA FFF O   1 ? 7  
ATOM 5562  C CB  . ALA D 2 60  ? 76.089  125.186 61.250 1.000 182.213 0 60  ALA FFF CB  1 ? 7  
ATOM 5563  N N   . ASP D 2 61  ? 75.309  125.744 58.250 1.000 203.152 0 61  ASP FFF N   1 ? 7  
ATOM 5564  C CA  . ASP D 2 61  ? 75.327  126.561 57.039 1.000 198.399 0 61  ASP FFF CA  1 ? 7  
ATOM 5565  C C   . ASP D 2 61  ? 75.936  127.948 57.264 1.000 200.290 0 61  ASP FFF C   1 ? 7  
ATOM 5566  O O   . ASP D 2 61  ? 76.588  128.489 56.363 1.000 205.700 0 61  ASP FFF O   1 ? 7  
ATOM 5567  C CB  . ASP D 2 61  ? 73.912  126.677 56.470 1.000 194.689 0 61  ASP FFF CB  1 ? 7  
ATOM 5568  C CG  . ASP D 2 61  ? 73.571  125.537 55.508 1.000 212.381 0 61  ASP FFF CG  1 ? 7  
ATOM 5569  O OD1 . ASP D 2 61  ? 74.375  124.589 55.386 1.000 213.876 0 61  ASP FFF OD1 1 ? 7  
ATOM 5570  O OD2 . ASP D 2 61  ? 72.515  125.608 54.842 1.000 219.696 0 61  ASP FFF OD2 1 ? 7  
ATOM 5571  N N   . SER D 2 62  ? 75.738  128.542 58.446 1.000 202.052 0 62  SER FFF N   1 ? 7  
ATOM 5572  C CA  . SER D 2 62  ? 76.297  129.864 58.716 1.000 207.117 0 62  SER FFF CA  1 ? 7  
ATOM 5573  C C   . SER D 2 62  ? 77.810  129.843 58.858 1.000 204.405 0 62  SER FFF C   1 ? 7  
ATOM 5574  O O   . SER D 2 62  ? 78.423  130.911 58.974 1.000 208.172 0 62  SER FFF O   1 ? 7  
ATOM 5575  C CB  . SER D 2 62  ? 75.681  130.441 59.991 1.000 204.931 0 62  SER FFF CB  1 ? 7  
ATOM 5576  O OG  . SER D 2 62  ? 74.269  130.376 59.948 1.000 221.180 0 62  SER FFF OG  1 ? 7  
ATOM 5577  N N   . VAL D 2 63  ? 78.412  128.657 58.846 1.000 201.051 0 63  VAL FFF N   1 ? 7  
ATOM 5578  C CA  . VAL D 2 63  ? 79.828  128.455 59.124 1.000 203.143 0 63  VAL FFF CA  1 ? 7  
ATOM 5579  C C   . VAL D 2 63  ? 80.438  127.551 58.062 1.000 213.017 0 63  VAL FFF C   1 ? 7  
ATOM 5580  O O   . VAL D 2 63  ? 81.655  127.339 58.047 1.000 211.695 0 63  VAL FFF O   1 ? 7  
ATOM 5581  C CB  . VAL D 2 63  ? 80.072  127.897 60.539 1.000 195.323 0 63  VAL FFF CB  1 ? 7  
ATOM 5582  C CG1 . VAL D 2 63  ? 79.518  128.848 61.590 1.000 187.230 0 63  VAL FFF CG1 1 ? 7  
ATOM 5583  C CG2 . VAL D 2 63  ? 79.477  126.502 60.696 1.000 194.967 0 63  VAL FFF CG2 1 ? 7  
ATOM 5584  N N   . LYS D 2 64  ? 79.592  127.009 57.178 1.000 223.362 0 64  LYS FFF N   1 ? 7  
ATOM 5585  C CA  . LYS D 2 64  ? 79.984  125.902 56.308 1.000 224.517 0 64  LYS FFF CA  1 ? 7  
ATOM 5586  C C   . LYS D 2 64  ? 81.241  126.256 55.527 1.000 229.318 0 64  LYS FFF C   1 ? 7  
ATOM 5587  O O   . LYS D 2 64  ? 82.148  125.429 55.377 1.000 226.068 0 64  LYS FFF O   1 ? 7  
ATOM 5588  C CB  . LYS D 2 64  ? 78.836  125.635 55.332 1.000 227.641 0 64  LYS FFF CB  1 ? 7  
ATOM 5589  C CG  . LYS D 2 64  ? 78.673  124.258 54.714 1.000 230.573 0 64  LYS FFF CG  1 ? 7  
ATOM 5590  C CD  . LYS D 2 64  ? 77.797  123.390 55.583 1.000 231.932 0 64  LYS FFF CD  1 ? 7  
ATOM 5591  C CE  . LYS D 2 64  ? 77.123  122.315 54.754 1.000 230.442 0 64  LYS FFF CE  1 ? 7  
ATOM 5592  N NZ  . LYS D 2 64  ? 76.055  121.616 55.511 1.000 228.771 0 64  LYS FFF NZ  1 ? 7  
ATOM 5593  N N   . GLY D 2 65  ? 81.305  127.483 55.011 1.000 247.478 0 65  GLY FFF N   1 ? 7  
ATOM 5594  C CA  . GLY D 2 65  ? 82.452  127.920 54.244 1.000 248.870 0 65  GLY FFF CA  1 ? 7  
ATOM 5595  C C   . GLY D 2 65  ? 83.687  128.218 55.067 1.000 249.204 0 65  GLY FFF C   1 ? 7  
ATOM 5596  O O   . GLY D 2 65  ? 84.795  128.199 54.517 1.000 261.895 0 65  GLY FFF O   1 ? 7  
ATOM 5597  N N   . ARG D 2 66  ? 83.528  128.474 56.376 1.000 227.183 0 66  ARG FFF N   1 ? 7  
ATOM 5598  C CA  . ARG D 2 66  ? 84.594  129.068 57.179 1.000 221.660 0 66  ARG FFF CA  1 ? 7  
ATOM 5599  C C   . ARG D 2 66  ? 85.199  128.193 58.266 1.000 215.085 0 66  ARG FFF C   1 ? 7  
ATOM 5600  O O   . ARG D 2 66  ? 86.381  128.356 58.565 1.000 216.554 0 66  ARG FFF O   1 ? 7  
ATOM 5601  C CB  . ARG D 2 66  ? 84.084  130.358 57.843 1.000 222.901 0 66  ARG FFF CB  1 ? 7  
ATOM 5602  C CG  . ARG D 2 66  ? 83.287  131.258 56.887 1.000 223.128 0 66  ARG FFF CG  1 ? 7  
ATOM 5603  C CD  . ARG D 2 66  ? 82.717  132.495 57.537 1.000 218.681 0 66  ARG FFF CD  1 ? 7  
ATOM 5604  N NE  . ARG D 2 66  ? 81.739  132.235 58.579 1.000 218.488 0 66  ARG FFF NE  1 ? 7  
ATOM 5605  C CZ  . ARG D 2 66  ? 81.864  132.595 59.851 1.000 222.128 0 66  ARG FFF CZ  1 ? 7  
ATOM 5606  N NH1 . ARG D 2 66  ? 82.928  133.252 60.287 1.000 225.337 0 66  ARG FFF NH1 1 ? 7  
ATOM 5607  N NH2 . ARG D 2 66  ? 80.889  132.293 60.704 1.000 219.634 0 66  ARG FFF NH2 1 ? 7  
ATOM 5608  N N   . PHE D 2 67  ? 84.447  127.268 58.851 1.000 203.086 0 67  PHE FFF N   1 ? 7  
ATOM 5609  C CA  . PHE D 2 67  ? 84.948  126.435 59.938 1.000 194.131 0 67  PHE FFF CA  1 ? 7  
ATOM 5610  C C   . PHE D 2 67  ? 85.295  125.035 59.458 1.000 188.038 0 67  PHE FFF C   1 ? 7  
ATOM 5611  O O   . PHE D 2 67  ? 84.812  124.562 58.426 1.000 194.708 0 67  PHE FFF O   1 ? 7  
ATOM 5612  C CB  . PHE D 2 67  ? 83.948  126.348 61.099 1.000 197.714 0 67  PHE FFF CB  1 ? 7  
ATOM 5613  C CG  . PHE D 2 67  ? 83.733  127.650 61.838 1.000 212.966 0 67  PHE FFF CG  1 ? 7  
ATOM 5614  C CD1 . PHE D 2 67  ? 84.343  128.817 61.418 1.000 220.875 0 67  PHE FFF CD1 1 ? 7  
ATOM 5615  C CD2 . PHE D 2 67  ? 82.938  127.692 62.978 1.000 212.665 0 67  PHE FFF CD2 1 ? 7  
ATOM 5616  C CE1 . PHE D 2 67  ? 84.152  130.000 62.091 1.000 225.353 0 67  PHE FFF CE1 1 ? 7  
ATOM 5617  C CE2 . PHE D 2 67  ? 82.745  128.880 63.661 1.000 214.379 0 67  PHE FFF CE2 1 ? 7  
ATOM 5618  C CZ  . PHE D 2 67  ? 83.354  130.034 63.214 1.000 222.651 0 67  PHE FFF CZ  1 ? 7  
ATOM 5619  N N   . THR D 2 68  ? 86.184  124.389 60.211 1.000 180.008 0 68  THR FFF N   1 ? 7  
ATOM 5620  C CA  . THR D 2 68  ? 86.530  122.991 59.989 1.000 175.900 0 68  THR FFF CA  1 ? 7  
ATOM 5621  C C   . THR D 2 68  ? 86.639  122.274 61.328 1.000 166.962 0 68  THR FFF C   1 ? 7  
ATOM 5622  O O   . THR D 2 68  ? 87.135  122.840 62.305 1.000 169.277 0 68  THR FFF O   1 ? 7  
ATOM 5623  C CB  . THR D 2 68  ? 87.858  122.866 59.229 1.000 176.419 0 68  THR FFF CB  1 ? 7  
ATOM 5624  O OG1 . THR D 2 68  ? 87.812  123.682 58.055 1.000 187.305 0 68  THR FFF OG1 1 ? 7  
ATOM 5625  C CG2 . THR D 2 68  ? 88.129  121.419 58.822 1.000 174.357 0 68  THR FFF CG2 1 ? 7  
ATOM 5626  N N   . ILE D 2 69  ? 86.184  121.023 61.359 1.000 161.011 0 69  ILE FFF N   1 ? 7  
ATOM 5627  C CA  . ILE D 2 69  ? 86.245  120.173 62.543 1.000 151.880 0 69  ILE FFF CA  1 ? 7  
ATOM 5628  C C   . ILE D 2 69  ? 87.097  118.945 62.229 1.000 152.042 0 69  ILE FFF C   1 ? 7  
ATOM 5629  O O   . ILE D 2 69  ? 86.945  118.339 61.162 1.000 155.723 0 69  ILE FFF O   1 ? 7  
ATOM 5630  C CB  . ILE D 2 69  ? 84.832  119.775 63.006 1.000 145.407 0 69  ILE FFF CB  1 ? 7  
ATOM 5631  C CG1 . ILE D 2 69  ? 84.892  118.809 64.188 1.000 148.584 0 69  ILE FFF CG1 1 ? 7  
ATOM 5632  C CG2 . ILE D 2 69  ? 84.030  119.204 61.841 1.000 150.035 0 69  ILE FFF CG2 1 ? 7  
ATOM 5633  C CD1 . ILE D 2 69  ? 83.548  118.586 64.837 1.000 147.251 0 69  ILE FFF CD1 1 ? 7  
ATOM 5634  N N   . SER D 2 70  ? 88.009  118.597 63.139 1.000 151.973 0 70  SER FFF N   1 ? 7  
ATOM 5635  C CA  . SER D 2 70  ? 88.898  117.461 62.922 1.000 156.671 0 70  SER FFF CA  1 ? 7  
ATOM 5636  C C   . SER D 2 70  ? 89.100  116.702 64.228 1.000 153.820 0 70  SER FFF C   1 ? 7  
ATOM 5637  O O   . SER D 2 70  ? 88.855  117.225 65.318 1.000 149.139 0 70  SER FFF O   1 ? 7  
ATOM 5638  C CB  . SER D 2 70  ? 90.259  117.906 62.364 1.000 166.883 0 70  SER FFF CB  1 ? 7  
ATOM 5639  O OG  . SER D 2 70  ? 90.838  118.917 63.173 1.000 178.227 0 70  SER FFF OG  1 ? 7  
ATOM 5640  N N   . ILE D 2 71  ? 89.558  115.453 64.103 1.000 157.201 0 71  ILE FFF N   1 ? 7  
ATOM 5641  C CA  . ILE D 2 71  ? 89.832  114.590 65.248 1.000 155.638 0 71  ILE FFF CA  1 ? 7  
ATOM 5642  C C   . ILE D 2 71  ? 91.250  114.044 65.140 1.000 162.823 0 71  ILE FFF C   1 ? 7  
ATOM 5643  O O   . ILE D 2 71  ? 91.641  113.520 64.091 1.000 170.798 0 71  ILE FFF O   1 ? 7  
ATOM 5644  C CB  . ILE D 2 71  ? 88.820  113.429 65.349 1.000 141.007 0 71  ILE FFF CB  1 ? 7  
ATOM 5645  C CG1 . ILE D 2 71  ? 87.429  113.957 65.711 1.000 138.419 0 71  ILE FFF CG1 1 ? 7  
ATOM 5646  C CG2 . ILE D 2 71  ? 89.290  112.384 66.351 1.000 140.493 0 71  ILE FFF CG2 1 ? 7  
ATOM 5647  C CD1 . ILE D 2 71  ? 86.411  112.869 66.007 1.000 134.503 0 71  ILE FFF CD1 1 ? 7  
ATOM 5648  N N   . ASP D 2 72  ? 92.015  114.167 66.224 1.000 157.520 0 72  ASP FFF N   1 ? 7  
ATOM 5649  C CA  . ASP D 2 72  ? 93.378  113.652 66.316 1.000 164.824 0 72  ASP FFF CA  1 ? 7  
ATOM 5650  C C   . ASP D 2 72  ? 93.345  112.546 67.367 1.000 168.335 0 72  ASP FFF C   1 ? 7  
ATOM 5651  O O   . ASP D 2 72  ? 93.272  112.833 68.567 1.000 174.268 0 72  ASP FFF O   1 ? 7  
ATOM 5652  C CB  . ASP D 2 72  ? 94.376  114.751 66.681 1.000 176.047 0 72  ASP FFF CB  1 ? 7  
ATOM 5653  C CG  . ASP D 2 72  ? 95.819  114.256 66.699 1.000 189.660 0 72  ASP FFF CG  1 ? 7  
ATOM 5654  O OD1 . ASP D 2 72  ? 96.041  113.033 66.577 1.000 190.545 0 72  ASP FFF OD1 1 ? 7  
ATOM 5655  O OD2 . ASP D 2 72  ? 96.737  115.093 66.839 1.000 198.067 0 72  ASP FFF OD2 1 ? 7  
ATOM 5656  N N   . SER D 2 73  ? 93.396  111.285 66.930 1.000 175.095 0 73  SER FFF N   1 ? 7  
ATOM 5657  C CA  . SER D 2 73  ? 93.363  110.192 67.897 1.000 179.736 0 73  SER FFF CA  1 ? 7  
ATOM 5658  C C   . SER D 2 73  ? 94.677  110.063 68.657 1.000 189.913 0 73  SER FFF C   1 ? 7  
ATOM 5659  O O   . SER D 2 73  ? 94.693  109.489 69.751 1.000 201.810 0 73  SER FFF O   1 ? 7  
ATOM 5660  C CB  . SER D 2 73  ? 93.025  108.871 67.198 1.000 176.183 0 73  SER FFF CB  1 ? 7  
ATOM 5661  O OG  . SER D 2 73  ? 92.942  107.800 68.126 1.000 169.699 0 73  SER FFF OG  1 ? 7  
ATOM 5662  N N   . ALA D 2 74  ? 95.775  110.573 68.096 1.000 194.316 0 74  ALA FFF N   1 ? 7  
ATOM 5663  C CA  . ALA D 2 74  ? 97.061  110.527 68.785 1.000 198.824 0 74  ALA FFF CA  1 ? 7  
ATOM 5664  C C   . ALA D 2 74  ? 97.024  111.341 70.075 1.000 198.822 0 74  ALA FFF C   1 ? 7  
ATOM 5665  O O   . ALA D 2 74  ? 97.396  110.850 71.146 1.000 193.874 0 74  ALA FFF O   1 ? 7  
ATOM 5666  C CB  . ALA D 2 74  ? 98.172  111.025 67.860 1.000 199.689 0 74  ALA FFF CB  1 ? 7  
ATOM 5667  N N   . GLU D 2 75  ? 96.557  112.587 69.992 1.000 201.340 0 75  GLU FFF N   1 ? 7  
ATOM 5668  C CA  . GLU D 2 75  ? 96.446  113.451 71.160 1.000 199.587 0 75  GLU FFF CA  1 ? 7  
ATOM 5669  C C   . GLU D 2 75  ? 95.098  113.344 71.860 1.000 189.300 0 75  GLU FFF C   1 ? 7  
ATOM 5670  O O   . GLU D 2 75  ? 94.880  114.042 72.855 1.000 203.503 0 75  GLU FFF O   1 ? 7  
ATOM 5671  C CB  . GLU D 2 75  ? 96.689  114.908 70.749 1.000 200.963 0 75  GLU FFF CB  1 ? 7  
ATOM 5672  C CG  . GLU D 2 75  ? 98.094  115.195 70.245 1.000 213.035 0 75  GLU FFF CG  1 ? 7  
ATOM 5673  C CD  . GLU D 2 75  ? 99.091  115.366 71.372 1.000 225.062 0 75  GLU FFF CD  1 ? 7  
ATOM 5674  O OE1 . GLU D 2 75  ? 98.667  115.732 72.488 1.000 223.951 0 75  GLU FFF OE1 1 ? 7  
ATOM 5675  O OE2 . GLU D 2 75  ? 100.297 115.137 71.143 1.000 238.707 0 75  GLU FFF OE2 1 ? 7  
ATOM 5676  N N   . ASN D 2 76  ? 94.191  112.506 71.359 1.000 173.176 0 76  ASN FFF N   1 ? 7  
ATOM 5677  C CA  . ASN D 2 76  ? 92.859  112.325 71.940 1.000 158.194 0 76  ASN FFF CA  1 ? 7  
ATOM 5678  C C   . ASN D 2 76  ? 92.080  113.638 72.021 1.000 151.244 0 76  ASN FFF C   1 ? 7  
ATOM 5679  O O   . ASN D 2 76  ? 91.467  113.953 73.042 1.000 152.660 0 76  ASN FFF O   1 ? 7  
ATOM 5680  C CB  . ASN D 2 76  ? 92.955  111.675 73.322 1.000 159.492 0 76  ASN FFF CB  1 ? 7  
ATOM 5681  C CG  . ASN D 2 76  ? 92.815  110.175 73.268 1.000 159.934 0 76  ASN FFF CG  1 ? 7  
ATOM 5682  O OD1 . ASN D 2 76  ? 92.324  109.621 72.283 1.000 157.376 0 76  ASN FFF OD1 1 ? 7  
ATOM 5683  N ND2 . ASN D 2 76  ? 93.245  109.502 74.328 1.000 174.969 0 76  ASN FFF ND2 1 ? 7  
ATOM 5684  N N   . THR D 2 77  ? 92.103  114.413 70.942 1.000 155.366 0 77  THR FFF N   1 ? 7  
ATOM 5685  C CA  . THR D 2 77  ? 91.506  115.739 70.982 1.000 157.812 0 77  THR FFF CA  1 ? 7  
ATOM 5686  C C   . THR D 2 77  ? 90.598  115.961 69.780 1.000 161.043 0 77  THR FFF C   1 ? 7  
ATOM 5687  O O   . THR D 2 77  ? 90.790  115.370 68.713 1.000 159.234 0 77  THR FFF O   1 ? 7  
ATOM 5688  C CB  . THR D 2 77  ? 92.586  116.834 71.038 1.000 158.580 0 77  THR FFF CB  1 ? 7  
ATOM 5689  O OG1 . THR D 2 77  ? 91.966  118.109 71.237 1.000 164.829 0 77  THR FFF OG1 1 ? 7  
ATOM 5690  C CG2 . THR D 2 77  ? 93.403  116.860 69.756 1.000 163.709 0 77  THR FFF CG2 1 ? 7  
ATOM 5691  N N   . LEU D 2 78  ? 89.606  116.831 69.968 1.000 158.702 0 78  LEU FFF N   1 ? 7  
ATOM 5692  C CA  . LEU D 2 78  ? 88.657  117.204 68.926 1.000 155.531 0 78  LEU FFF CA  1 ? 7  
ATOM 5693  C C   . LEU D 2 78  ? 88.855  118.680 68.621 1.000 165.425 0 78  LEU FFF C   1 ? 7  
ATOM 5694  O O   . LEU D 2 78  ? 88.640  119.529 69.494 1.000 169.204 0 78  LEU FFF O   1 ? 7  
ATOM 5695  C CB  . LEU D 2 78  ? 87.216  116.924 69.365 1.000 147.415 0 78  LEU FFF CB  1 ? 7  
ATOM 5696  C CG  . LEU D 2 78  ? 86.100  117.573 68.544 1.000 144.161 0 78  LEU FFF CG  1 ? 7  
ATOM 5697  C CD1 . LEU D 2 78  ? 85.795  116.748 67.311 1.000 145.966 0 78  LEU FFF CD1 1 ? 7  
ATOM 5698  C CD2 . LEU D 2 78  ? 84.851  117.747 69.392 1.000 142.970 0 78  LEU FFF CD2 1 ? 7  
ATOM 5699  N N   . ALA D 2 79  ? 89.254  118.988 67.391 1.000 165.433 0 79  ALA FFF N   1 ? 7  
ATOM 5700  C CA  . ALA D 2 79  ? 89.618  120.344 67.014 1.000 163.125 0 79  ALA FFF CA  1 ? 7  
ATOM 5701  C C   . ALA D 2 79  ? 88.521  120.981 66.172 1.000 163.133 0 79  ALA FFF C   1 ? 7  
ATOM 5702  O O   . ALA D 2 79  ? 87.944  120.333 65.294 1.000 167.868 0 79  ALA FFF O   1 ? 7  
ATOM 5703  C CB  . ALA D 2 79  ? 90.941  120.360 66.245 1.000 161.790 0 79  ALA FFF CB  1 ? 7  
ATOM 5704  N N   . LEU D 2 80  ? 88.235  122.250 66.445 1.000 169.267 0 80  LEU FFF N   1 ? 7  
ATOM 5705  C CA  . LEU D 2 80  ? 87.394  123.064 65.578 1.000 181.094 0 80  LEU FFF CA  1 ? 7  
ATOM 5706  C C   . LEU D 2 80  ? 88.253  124.264 65.212 1.000 199.809 0 80  LEU FFF C   1 ? 7  
ATOM 5707  O O   . LEU D 2 80  ? 88.507  125.128 66.061 1.000 206.905 0 80  LEU FFF O   1 ? 7  
ATOM 5708  C CB  . LEU D 2 80  ? 86.100  123.488 66.269 1.000 171.095 0 80  LEU FFF CB  1 ? 7  
ATOM 5709  C CG  . LEU D 2 80  ? 85.198  124.424 65.458 1.000 174.169 0 80  LEU FFF CG  1 ? 7  
ATOM 5710  C CD1 . LEU D 2 80  ? 84.416  123.640 64.393 1.000 175.551 0 80  LEU FFF CD1 1 ? 7  
ATOM 5711  C CD2 . LEU D 2 80  ? 84.243  125.167 66.375 1.000 168.352 0 80  LEU FFF CD2 1 ? 7  
ATOM 5712  N N   . GLN D 2 81  ? 88.692  124.326 63.957 1.000 210.354 0 81  GLN FFF N   1 ? 7  
ATOM 5713  C CA  . GLN D 2 81  ? 89.511  125.438 63.473 1.000 217.755 0 81  GLN FFF CA  1 ? 7  
ATOM 5714  C C   . GLN D 2 81  ? 88.599  126.525 62.918 1.000 219.980 0 81  GLN FFF C   1 ? 7  
ATOM 5715  O O   . GLN D 2 81  ? 88.244  126.538 61.736 1.000 218.604 0 81  GLN FFF O   1 ? 7  
ATOM 5716  C CB  . GLN D 2 81  ? 90.513  124.947 62.436 1.000 220.421 0 81  GLN FFF CB  1 ? 7  
ATOM 5717  C CG  . GLN D 2 81  ? 91.360  126.043 61.826 1.000 228.649 0 81  GLN FFF CG  1 ? 7  
ATOM 5718  C CD  . GLN D 2 81  ? 92.506  126.456 62.724 1.000 240.537 0 81  GLN FFF CD  1 ? 7  
ATOM 5719  O OE1 . GLN D 2 81  ? 93.528  125.773 62.801 1.000 248.614 0 81  GLN FFF OE1 1 ? 7  
ATOM 5720  N NE2 . GLN D 2 81  ? 92.341  127.579 63.413 1.000 250.791 0 81  GLN FFF NE2 1 ? 7  
ATOM 5721  N N   . MET D 2 82  ? 88.209  127.441 63.798 1.000 218.666 0 82  MET FFF N   1 ? 7  
ATOM 5722  C CA  . MET D 2 82  ? 87.435  128.610 63.405 1.000 223.925 0 82  MET FFF CA  1 ? 7  
ATOM 5723  C C   . MET D 2 82  ? 88.326  129.562 62.611 1.000 238.002 0 82  MET FFF C   1 ? 7  
ATOM 5724  O O   . MET D 2 82  ? 89.392  129.965 63.086 1.000 251.610 0 82  MET FFF O   1 ? 7  
ATOM 5725  C CB  . MET D 2 82  ? 86.885  129.293 64.659 1.000 221.735 0 82  MET FFF CB  1 ? 7  
ATOM 5726  C CG  . MET D 2 82  ? 85.938  128.400 65.460 1.000 218.294 0 82  MET FFF CG  1 ? 7  
ATOM 5727  S SD  . MET D 2 82  ? 85.368  129.063 67.044 1.000 222.934 0 82  MET FFF SD  1 ? 7  
ATOM 5728  C CE  . MET D 2 82  ? 84.850  130.707 66.591 1.000 228.268 0 82  MET FFF CE  1 ? 7  
ATOM 5729  N N   . ASN D 2 83  A 87.914  129.901 61.391 1.000 235.746 0 82  ASN FFF N   1 ? 7  
ATOM 5730  C CA  . ASN D 2 83  A 88.688  130.802 60.548 1.000 231.900 0 82  ASN FFF CA  1 ? 7  
ATOM 5731  C C   . ASN D 2 83  A 87.758  131.859 59.972 1.000 235.264 0 82  ASN FFF C   1 ? 7  
ATOM 5732  O O   . ASN D 2 83  A 86.539  131.674 59.936 1.000 236.072 0 82  ASN FFF O   1 ? 7  
ATOM 5733  C CB  . ASN D 2 83  A 89.358  130.045 59.392 1.000 224.161 0 82  ASN FFF CB  1 ? 7  
ATOM 5734  C CG  . ASN D 2 83  A 90.307  128.967 59.864 1.000 221.336 0 82  ASN FFF CG  1 ? 7  
ATOM 5735  O OD1 . ASN D 2 83  A 91.177  129.204 60.702 1.000 222.111 0 82  ASN FFF OD1 1 ? 7  
ATOM 5736  N ND2 . ASN D 2 83  A 90.139  127.766 59.326 1.000 222.200 0 82  ASN FFF ND2 1 ? 7  
ATOM 5737  N N   . ARG D 2 84  B 88.339  132.972 59.506 1.000 237.460 0 82  ARG FFF N   1 ? 7  
ATOM 5738  C CA  . ARG D 2 84  B 87.542  134.046 58.908 1.000 245.053 0 82  ARG FFF CA  1 ? 7  
ATOM 5739  C C   . ARG D 2 84  B 86.449  134.515 59.875 1.000 241.803 0 82  ARG FFF C   1 ? 7  
ATOM 5740  O O   . ARG D 2 84  B 85.271  134.593 59.527 1.000 237.893 0 82  ARG FFF O   1 ? 7  
ATOM 5741  C CB  . ARG D 2 84  B 87.000  133.654 57.527 1.000 246.663 0 82  ARG FFF CB  1 ? 7  
ATOM 5742  C CG  . ARG D 2 84  B 86.647  134.859 56.678 1.000 252.929 0 82  ARG FFF CG  1 ? 7  
ATOM 5743  C CD  . ARG D 2 84  B 85.856  134.487 55.447 1.000 255.648 0 82  ARG FFF CD  1 ? 7  
ATOM 5744  N NE  . ARG D 2 84  B 86.729  133.751 54.544 1.000 260.677 0 82  ARG FFF NE  1 ? 7  
ATOM 5745  C CZ  . ARG D 2 84  B 86.328  132.934 53.578 1.000 265.547 0 82  ARG FFF CZ  1 ? 7  
ATOM 5746  N NH1 . ARG D 2 84  B 85.041  132.742 53.342 1.000 269.472 0 82  ARG FFF NH1 1 ? 7  
ATOM 5747  N NH2 . ARG D 2 84  B 87.237  132.339 52.811 1.000 265.418 0 82  ARG FFF NH2 1 ? 7  
ATOM 5748  N N   . LEU D 2 85  C 86.852  134.797 61.114 1.000 251.293 0 82  LEU FFF N   1 ? 7  
ATOM 5749  C CA  . LEU D 2 85  C 85.921  135.068 62.202 1.000 253.328 0 82  LEU FFF CA  1 ? 7  
ATOM 5750  C C   . LEU D 2 85  C 85.132  136.361 61.972 1.000 255.977 0 82  LEU FFF C   1 ? 7  
ATOM 5751  O O   . LEU D 2 85  C 85.638  137.348 61.430 1.000 268.652 0 82  LEU FFF O   1 ? 7  
ATOM 5752  C CB  . LEU D 2 85  C 86.738  135.222 63.485 1.000 255.569 0 82  LEU FFF CB  1 ? 7  
ATOM 5753  C CG  . LEU D 2 85  C 87.337  133.993 64.166 1.000 250.378 0 82  LEU FFF CG  1 ? 7  
ATOM 5754  C CD1 . LEU D 2 85  C 88.224  134.424 65.329 1.000 255.199 0 82  LEU FFF CD1 1 ? 7  
ATOM 5755  C CD2 . LEU D 2 85  C 86.253  133.078 64.612 1.000 242.052 0 82  LEU FFF CD2 1 ? 7  
ATOM 5756  N N   . LYS D 2 86  ? 83.877  136.337 62.397 1.000 242.047 0 83  LYS FFF N   1 ? 7  
ATOM 5757  C CA  . LYS D 2 86  ? 82.886  137.392 62.296 1.000 242.385 0 83  LYS FFF CA  1 ? 7  
ATOM 5758  C C   . LYS D 2 86  ? 82.376  137.812 63.673 1.000 243.897 0 83  LYS FFF C   1 ? 7  
ATOM 5759  O O   . LYS D 2 86  ? 82.521  137.068 64.649 1.000 245.042 0 83  LYS FFF O   1 ? 7  
ATOM 5760  C CB  . LYS D 2 86  ? 81.753  136.972 61.349 1.000 237.546 0 83  LYS FFF CB  1 ? 7  
ATOM 5761  C CG  . LYS D 2 86  ? 82.303  136.697 59.956 1.000 232.973 0 83  LYS FFF CG  1 ? 7  
ATOM 5762  C CD  . LYS D 2 86  ? 81.227  136.556 58.881 1.000 224.068 0 83  LYS FFF CD  1 ? 7  
ATOM 5763  C CE  . LYS D 2 86  ? 81.826  135.868 57.649 1.000 217.483 0 83  LYS FFF CE  1 ? 7  
ATOM 5764  N NZ  . LYS D 2 86  ? 80.812  135.649 56.580 1.000 212.498 0 83  LYS FFF NZ  1 ? 7  
ATOM 5765  N N   . PRO D 2 87  ? 81.775  139.008 63.785 1.000 245.664 0 84  PRO FFF N   1 ? 7  
ATOM 5766  C CA  . PRO D 2 87  ? 81.177  139.423 65.073 1.000 245.545 0 84  PRO FFF CA  1 ? 7  
ATOM 5767  C C   . PRO D 2 87  ? 80.073  138.509 65.609 1.000 242.796 0 84  PRO FFF C   1 ? 7  
ATOM 5768  O O   . PRO D 2 87  ? 79.949  138.367 66.833 1.000 239.017 0 84  PRO FFF O   1 ? 7  
ATOM 5769  C CB  . PRO D 2 87  ? 80.602  140.806 64.735 1.000 242.073 0 84  PRO FFF CB  1 ? 7  
ATOM 5770  C CG  . PRO D 2 87  ? 81.494  141.312 63.653 1.000 243.196 0 84  PRO FFF CG  1 ? 7  
ATOM 5771  C CD  . PRO D 2 87  ? 81.797  140.117 62.810 1.000 247.111 0 84  PRO FFF CD  1 ? 7  
ATOM 5772  N N   . GLU D 2 88  ? 79.248  137.906 64.752 1.000 242.507 0 85  GLU FFF N   1 ? 7  
ATOM 5773  C CA  . GLU D 2 88  ? 78.233  136.965 65.231 1.000 243.513 0 85  GLU FFF CA  1 ? 7  
ATOM 5774  C C   . GLU D 2 88  ? 78.842  135.741 65.895 1.000 247.036 0 85  GLU FFF C   1 ? 7  
ATOM 5775  O O   . GLU D 2 88  ? 78.114  134.982 66.548 1.000 243.765 0 85  GLU FFF O   1 ? 7  
ATOM 5776  C CB  . GLU D 2 88  ? 77.273  136.526 64.120 1.000 241.205 0 85  GLU FFF CB  1 ? 7  
ATOM 5777  C CG  . GLU D 2 88  ? 76.459  137.644 63.505 1.000 240.784 0 85  GLU FFF CG  1 ? 7  
ATOM 5778  C CD  . GLU D 2 88  ? 77.246  138.481 62.526 1.000 240.866 0 85  GLU FFF CD  1 ? 7  
ATOM 5779  O OE1 . GLU D 2 88  ? 78.266  137.979 62.003 1.000 242.119 0 85  GLU FFF OE1 1 ? 7  
ATOM 5780  O OE2 . GLU D 2 88  ? 76.840  139.629 62.290 1.000 232.535 0 85  GLU FFF OE2 1 ? 7  
ATOM 5781  N N   . ASP D 2 89  ? 80.150  135.541 65.767 1.000 261.422 0 86  ASP FFF N   1 ? 7  
ATOM 5782  C CA  . ASP D 2 89  ? 80.779  134.401 66.411 1.000 256.725 0 86  ASP FFF CA  1 ? 7  
ATOM 5783  C C   . ASP D 2 89  ? 81.004  134.603 67.900 1.000 254.244 0 86  ASP FFF C   1 ? 7  
ATOM 5784  O O   . ASP D 2 89  ? 81.475  133.664 68.553 1.000 248.562 0 86  ASP FFF O   1 ? 7  
ATOM 5785  C CB  . ASP D 2 89  ? 82.124  134.083 65.748 1.000 258.694 0 86  ASP FFF CB  1 ? 7  
ATOM 5786  C CG  . ASP D 2 89  ? 81.979  133.654 64.304 1.000 253.152 0 86  ASP FFF CG  1 ? 7  
ATOM 5787  O OD1 . ASP D 2 89  ? 80.831  133.528 63.833 1.000 253.073 0 86  ASP FFF OD1 1 ? 7  
ATOM 5788  O OD2 . ASP D 2 89  ? 83.015  133.439 63.640 1.000 245.608 0 86  ASP FFF OD2 1 ? 7  
ATOM 5789  N N   . THR D 2 90  ? 80.748  135.793 68.453 1.000 253.688 0 87  THR FFF N   1 ? 7  
ATOM 5790  C CA  . THR D 2 90  ? 80.918  135.921 69.891 1.000 250.535 0 87  THR FFF CA  1 ? 7  
ATOM 5791  C C   . THR D 2 90  ? 79.932  134.963 70.543 1.000 244.541 0 87  THR FFF C   1 ? 7  
ATOM 5792  O O   . THR D 2 90  ? 78.716  135.111 70.376 1.000 243.144 0 87  THR FFF O   1 ? 7  
ATOM 5793  C CB  . THR D 2 90  ? 80.648  137.359 70.337 1.000 248.194 0 87  THR FFF CB  1 ? 7  
ATOM 5794  O OG1 . THR D 2 90  ? 81.533  138.258 69.654 1.000 239.796 0 87  THR FFF OG1 1 ? 7  
ATOM 5795  C CG2 . THR D 2 90  ? 80.809  137.499 71.840 1.000 249.564 0 87  THR FFF CG2 1 ? 7  
ATOM 5796  N N   . ALA D 2 91  ? 80.448  134.011 71.315 1.000 238.826 0 88  ALA FFF N   1 ? 7  
ATOM 5797  C CA  . ALA D 2 91  ? 79.609  133.009 71.961 1.000 231.814 0 88  ALA FFF CA  1 ? 7  
ATOM 5798  C C   . ALA D 2 91  ? 80.491  132.130 72.838 1.000 227.865 0 88  ALA FFF C   1 ? 7  
ATOM 5799  O O   . ALA D 2 91  ? 81.723  132.187 72.773 1.000 230.544 0 88  ALA FFF O   1 ? 7  
ATOM 5800  C CB  . ALA D 2 91  ? 78.855  132.143 70.951 1.000 232.116 0 88  ALA FFF CB  1 ? 7  
ATOM 5801  N N   . VAL D 2 92  ? 79.834  131.317 73.663 1.000 221.169 0 89  VAL FFF N   1 ? 7  
ATOM 5802  C CA  . VAL D 2 92  ? 80.467  130.212 74.379 1.000 212.511 0 89  VAL FFF CA  1 ? 7  
ATOM 5803  C C   . VAL D 2 92  ? 80.365  128.946 73.528 1.000 212.449 0 89  VAL FFF C   1 ? 7  
ATOM 5804  O O   . VAL D 2 92  ? 79.277  128.596 73.057 1.000 214.308 0 89  VAL FFF O   1 ? 7  
ATOM 5805  C CB  . VAL D 2 92  ? 79.805  130.007 75.752 1.000 209.065 0 89  VAL FFF CB  1 ? 7  
ATOM 5806  C CG1 . VAL D 2 92  ? 80.622  129.051 76.600 1.000 204.100 0 89  VAL FFF CG1 1 ? 7  
ATOM 5807  C CG2 . VAL D 2 92  ? 79.630  131.344 76.466 1.000 215.649 0 89  VAL FFF CG2 1 ? 7  
ATOM 5808  N N   . TYR D 2 93  ? 81.489  128.253 73.328 1.000 209.230 0 90  TYR FFF N   1 ? 7  
ATOM 5809  C CA  . TYR D 2 93  ? 81.549  127.092 72.440 1.000 201.111 0 90  TYR FFF CA  1 ? 7  
ATOM 5810  C C   . TYR D 2 93  ? 81.681  125.824 73.279 1.000 191.307 0 90  TYR FFF C   1 ? 7  
ATOM 5811  O O   . TYR D 2 93  ? 82.525  125.766 74.178 1.000 194.341 0 90  TYR FFF O   1 ? 7  
ATOM 5812  C CB  . TYR D 2 93  ? 82.711  127.217 71.445 1.000 203.346 0 90  TYR FFF CB  1 ? 7  
ATOM 5813  C CG  . TYR D 2 93  ? 82.468  128.227 70.340 1.000 209.038 0 90  TYR FFF CG  1 ? 7  
ATOM 5814  C CD1 . TYR D 2 93  ? 82.495  129.590 70.599 1.000 217.757 0 90  TYR FFF CD1 1 ? 7  
ATOM 5815  C CD2 . TYR D 2 93  ? 82.216  127.814 69.037 1.000 207.786 0 90  TYR FFF CD2 1 ? 7  
ATOM 5816  C CE1 . TYR D 2 93  ? 82.270  130.513 69.597 1.000 224.517 0 90  TYR FFF CE1 1 ? 7  
ATOM 5817  C CE2 . TYR D 2 93  ? 81.993  128.732 68.027 1.000 218.345 0 90  TYR FFF CE2 1 ? 7  
ATOM 5818  C CZ  . TYR D 2 93  ? 82.020  130.080 68.314 1.000 225.965 0 90  TYR FFF CZ  1 ? 7  
ATOM 5819  O OH  . TYR D 2 93  ? 81.798  131.000 67.315 1.000 239.803 0 90  TYR FFF OH  1 ? 7  
ATOM 5820  N N   . TYR D 2 94  ? 80.870  124.802 72.972 1.000 182.830 0 91  TYR FFF N   1 ? 7  
ATOM 5821  C CA  . TYR D 2 94  ? 80.862  123.540 73.715 1.000 175.327 0 91  TYR FFF CA  1 ? 7  
ATOM 5822  C C   . TYR D 2 94  ? 81.162  122.342 72.814 1.000 167.612 0 91  TYR FFF C   1 ? 7  
ATOM 5823  O O   . TYR D 2 94  ? 80.625  122.255 71.707 1.000 166.337 0 91  TYR FFF O   1 ? 7  
ATOM 5824  C CB  . TYR D 2 94  ? 79.483  123.306 74.362 1.000 178.054 0 91  TYR FFF CB  1 ? 7  
ATOM 5825  C CG  . TYR D 2 94  ? 78.922  124.478 75.144 1.000 191.404 0 91  TYR FFF CG  1 ? 7  
ATOM 5826  C CD1 . TYR D 2 94  ? 78.238  125.497 74.491 1.000 198.222 0 91  TYR FFF CD1 1 ? 7  
ATOM 5827  C CD2 . TYR D 2 94  ? 79.045  124.554 76.526 1.000 198.143 0 91  TYR FFF CD2 1 ? 7  
ATOM 5828  C CE1 . TYR D 2 94  ? 77.712  126.569 75.185 1.000 206.598 0 91  TYR FFF CE1 1 ? 7  
ATOM 5829  C CE2 . TYR D 2 94  ? 78.519  125.629 77.232 1.000 201.063 0 91  TYR FFF CE2 1 ? 7  
ATOM 5830  C CZ  . TYR D 2 94  ? 77.853  126.632 76.554 1.000 207.168 0 91  TYR FFF CZ  1 ? 7  
ATOM 5831  O OH  . TYR D 2 94  ? 77.328  127.703 77.243 1.000 209.872 0 91  TYR FFF OH  1 ? 7  
ATOM 5832  N N   . CYS D 2 95  ? 82.000  121.402 73.278 1.000 156.584 0 92  CYS FFF N   1 ? 7  
ATOM 5833  C CA  . CYS D 2 95  ? 82.112  120.110 72.604 1.000 153.417 0 92  CYS FFF CA  1 ? 7  
ATOM 5834  C C   . CYS D 2 95  ? 81.254  119.062 73.308 1.000 144.098 0 92  CYS FFF C   1 ? 7  
ATOM 5835  O O   . CYS D 2 95  ? 81.038  119.132 74.520 1.000 142.191 0 92  CYS FFF O   1 ? 7  
ATOM 5836  C CB  . CYS D 2 95  ? 83.555  119.589 72.578 1.000 160.473 0 92  CYS FFF CB  1 ? 7  
ATOM 5837  S SG  . CYS D 2 95  ? 84.367  119.490 74.203 1.000 198.147 0 92  CYS FFF SG  1 ? 7  
ATOM 5838  N N   . PHE D 2 96  ? 80.759  118.085 72.542 1.000 140.739 0 93  PHE FFF N   1 ? 7  
ATOM 5839  C CA  . PHE D 2 96  ? 80.044  116.955 73.123 1.000 134.450 0 93  PHE FFF CA  1 ? 7  
ATOM 5840  C C   . PHE D 2 96  ? 80.549  115.644 72.531 1.000 128.597 0 93  PHE FFF C   1 ? 7  
ATOM 5841  O O   . PHE D 2 96  ? 81.017  115.612 71.392 1.000 130.989 0 93  PHE FFF O   1 ? 7  
ATOM 5842  C CB  . PHE D 2 96  ? 78.524  117.079 72.887 1.000 136.387 0 93  PHE FFF CB  1 ? 7  
ATOM 5843  C CG  . PHE D 2 96  ? 78.106  116.881 71.449 1.000 137.367 0 93  PHE FFF CG  1 ? 7  
ATOM 5844  C CD1 . PHE D 2 96  ? 77.900  115.607 70.934 1.000 132.147 0 93  PHE FFF CD1 1 ? 7  
ATOM 5845  C CD2 . PHE D 2 96  ? 77.945  117.965 70.606 1.000 137.149 0 93  PHE FFF CD2 1 ? 7  
ATOM 5846  C CE1 . PHE D 2 96  ? 77.523  115.424 69.618 1.000 125.321 0 93  PHE FFF CE1 1 ? 7  
ATOM 5847  C CE2 . PHE D 2 96  ? 77.570  117.784 69.288 1.000 138.743 0 93  PHE FFF CE2 1 ? 7  
ATOM 5848  C CZ  . PHE D 2 96  ? 77.359  116.514 68.794 1.000 129.851 0 93  PHE FFF CZ  1 ? 7  
ATOM 5849  N N   . ALA D 2 97  ? 80.472  114.561 73.309 1.000 122.465 0 94  ALA FFF N   1 ? 7  
ATOM 5850  C CA  . ALA D 2 97  ? 80.820  113.233 72.812 1.000 118.768 0 94  ALA FFF CA  1 ? 7  
ATOM 5851  C C   . ALA D 2 97  ? 79.732  112.267 73.256 1.000 120.433 0 94  ALA FFF C   1 ? 7  
ATOM 5852  O O   . ALA D 2 97  ? 79.225  112.403 74.371 1.000 131.493 0 94  ALA FFF O   1 ? 7  
ATOM 5853  C CB  . ALA D 2 97  ? 82.176  112.767 73.343 1.000 120.843 0 94  ALA FFF CB  1 ? 7  
ATOM 5854  N N   . ALA D 2 98  ? 79.338  111.302 72.423 1.000 112.033 0 95  ALA FFF N   1 ? 7  
ATOM 5855  C CA  . ALA D 2 98  ? 78.266  110.422 72.880 1.000 117.061 0 95  ALA FFF CA  1 ? 7  
ATOM 5856  C C   . ALA D 2 98  ? 78.744  108.978 73.021 1.000 120.345 0 95  ALA FFF C   1 ? 7  
ATOM 5857  O O   . ALA D 2 98  ? 79.100  108.341 72.023 1.000 121.029 0 95  ALA FFF O   1 ? 7  
ATOM 5858  C CB  . ALA D 2 98  ? 77.066  110.507 71.939 1.000 112.615 0 95  ALA FFF CB  1 ? 7  
ATOM 5859  N N   . LEU D 2 99  ? 78.742  108.457 74.249 1.000 124.081 0 96  LEU FFF N   1 ? 7  
ATOM 5860  C CA  . LEU D 2 99  ? 78.936  107.033 74.513 1.000 128.299 0 96  LEU FFF CA  1 ? 7  
ATOM 5861  C C   . LEU D 2 99  ? 77.834  106.797 75.542 1.000 143.063 0 96  LEU FFF C   1 ? 7  
ATOM 5862  O O   . LEU D 2 99  ? 77.860  107.442 76.594 1.000 160.555 0 96  LEU FFF O   1 ? 7  
ATOM 5863  C CB  . LEU D 2 99  ? 80.364  106.721 74.994 1.000 130.279 0 96  LEU FFF CB  1 ? 7  
ATOM 5864  C CG  . LEU D 2 99  ? 80.961  105.311 74.780 1.000 143.349 0 96  LEU FFF CG  1 ? 7  
ATOM 5865  C CD1 . LEU D 2 99  ? 82.472  105.436 74.673 1.000 152.701 0 96  LEU FFF CD1 1 ? 7  
ATOM 5866  C CD2 . LEU D 2 99  ? 80.659  104.247 75.797 1.000 153.923 0 96  LEU FFF CD2 1 ? 7  
ATOM 5867  N N   . ASP D 2 100 ? 76.888  105.890 75.278 1.000 147.404 0 97  ASP FFF N   1 ? 7  
ATOM 5868  C CA  . ASP D 2 100 ? 75.834  105.498 76.231 1.000 156.782 0 97  ASP FFF CA  1 ? 7  
ATOM 5869  C C   . ASP D 2 100 ? 75.294  106.723 76.975 1.000 140.009 0 97  ASP FFF C   1 ? 7  
ATOM 5870  O O   . ASP D 2 100 ? 74.977  106.622 78.162 1.000 137.903 0 97  ASP FFF O   1 ? 7  
ATOM 5871  C CB  . ASP D 2 100 ? 76.256  104.473 77.307 1.000 174.210 0 97  ASP FFF CB  1 ? 7  
ATOM 5872  C CG  . ASP D 2 100 ? 77.524  104.851 78.063 1.000 192.689 0 97  ASP FFF CG  1 ? 7  
ATOM 5873  O OD1 . ASP D 2 100 ? 77.441  105.574 79.082 1.000 188.725 0 97  ASP FFF OD1 1 ? 7  
ATOM 5874  O OD2 . ASP D 2 100 ? 78.584  104.311 77.728 1.000 214.998 0 97  ASP FFF OD2 1 ? 7  
ATOM 5875  N N   . THR D 2 101 ? 75.281  107.879 76.303 1.000 133.920 0 98  THR FFF N   1 ? 7  
ATOM 5876  C CA  . THR D 2 101 ? 74.630  109.184 76.601 1.000 128.836 0 98  THR FFF CA  1 ? 7  
ATOM 5877  C C   . THR D 2 101 ? 75.714  110.103 77.102 1.000 121.724 0 98  THR FFF C   1 ? 7  
ATOM 5878  O O   . THR D 2 101 ? 76.785  110.181 76.519 1.000 120.692 0 98  THR FFF O   1 ? 7  
ATOM 5879  C CB  . THR D 2 101 ? 73.465  109.260 77.623 1.000 140.920 0 98  THR FFF CB  1 ? 7  
ATOM 5880  O OG1 . THR D 2 101 ? 72.912  110.581 77.510 1.000 142.664 0 98  THR FFF OG1 1 ? 7  
ATOM 5881  C CG2 . THR D 2 101 ? 73.927  109.116 79.073 1.000 144.211 0 98  THR FFF CG2 1 ? 7  
ATOM 5882  N N   . ALA D 2 104 ? 74.094  112.450 76.023 1.000 129.690 0 101 ALA FFF N   1 ? 7  
ATOM 5883  C CA  . ALA D 2 104 ? 75.443  112.844 75.628 1.000 132.816 0 101 ALA FFF CA  1 ? 7  
ATOM 5884  C C   . ALA D 2 104 ? 76.183  113.512 76.788 1.000 137.103 0 101 ALA FFF C   1 ? 7  
ATOM 5885  O O   . ALA D 2 104 ? 75.594  113.784 77.835 1.000 150.378 0 101 ALA FFF O   1 ? 7  
ATOM 5886  C CB  . ALA D 2 104 ? 75.399  113.760 74.423 1.000 140.815 0 101 ALA FFF CB  1 ? 7  
ATOM 5887  N N   . TYR D 2 105 ? 77.479  113.754 76.594 1.000 135.296 0 102 TYR FFF N   1 ? 7  
ATOM 5888  C CA  . TYR D 2 105 ? 78.336  114.412 77.572 1.000 133.572 0 102 TYR FFF CA  1 ? 7  
ATOM 5889  C C   . TYR D 2 105 ? 78.792  115.747 77.005 1.000 138.897 0 102 TYR FFF C   1 ? 7  
ATOM 5890  O O   . TYR D 2 105 ? 79.037  115.864 75.802 1.000 141.642 0 102 TYR FFF O   1 ? 7  
ATOM 5891  C CB  . TYR D 2 105 ? 79.565  113.566 77.938 1.000 124.784 0 102 TYR FFF CB  1 ? 7  
ATOM 5892  C CG  . TYR D 2 105 ? 79.276  112.180 78.481 1.000 122.646 0 102 TYR FFF CG  1 ? 7  
ATOM 5893  C CD1 . TYR D 2 105 ? 78.434  112.002 79.573 1.000 131.680 0 102 TYR FFF CD1 1 ? 7  
ATOM 5894  C CD2 . TYR D 2 105 ? 79.863  111.053 77.921 1.000 119.570 0 102 TYR FFF CD2 1 ? 7  
ATOM 5895  C CE1 . TYR D 2 105 ? 78.170  110.737 80.082 1.000 133.329 0 102 TYR FFF CE1 1 ? 7  
ATOM 5896  C CE2 . TYR D 2 105 ? 79.603  109.780 78.423 1.000 123.158 0 102 TYR FFF CE2 1 ? 7  
ATOM 5897  C CZ  . TYR D 2 105 ? 78.758  109.629 79.505 1.000 124.354 0 102 TYR FFF CZ  1 ? 7  
ATOM 5898  O OH  . TYR D 2 105 ? 78.495  108.372 80.012 1.000 116.087 0 102 TYR FFF OH  1 ? 7  
ATOM 5899  N N   . TRP D 2 106 ? 78.903  116.749 77.875 1.000 138.377 0 103 TRP FFF N   1 ? 7  
ATOM 5900  C CA  . TRP D 2 106 ? 79.278  118.098 77.482 1.000 144.561 0 103 TRP FFF CA  1 ? 7  
ATOM 5901  C C   . TRP D 2 106 ? 80.490  118.571 78.278 1.000 148.988 0 103 TRP FFF C   1 ? 7  
ATOM 5902  O O   . TRP D 2 106 ? 80.695  118.179 79.431 1.000 145.197 0 103 TRP FFF O   1 ? 7  
ATOM 5903  C CB  . TRP D 2 106 ? 78.105  119.075 77.667 1.000 147.538 0 103 TRP FFF CB  1 ? 7  
ATOM 5904  C CG  . TRP D 2 106 ? 76.932  118.759 76.784 1.000 146.310 0 103 TRP FFF CG  1 ? 7  
ATOM 5905  C CD1 . TRP D 2 106 ? 75.932  117.865 77.039 1.000 147.319 0 103 TRP FFF CD1 1 ? 7  
ATOM 5906  C CD2 . TRP D 2 106 ? 76.651  119.316 75.492 1.000 148.402 0 103 TRP FFF CD2 1 ? 7  
ATOM 5907  N NE1 . TRP D 2 106 ? 75.040  117.840 75.993 1.000 148.155 0 103 TRP FFF NE1 1 ? 7  
ATOM 5908  C CE2 . TRP D 2 106 ? 75.460  118.721 75.031 1.000 146.458 0 103 TRP FFF CE2 1 ? 7  
ATOM 5909  C CE3 . TRP D 2 106 ? 77.289  120.263 74.685 1.000 153.867 0 103 TRP FFF CE3 1 ? 7  
ATOM 5910  C CZ2 . TRP D 2 106 ? 74.893  119.043 73.798 1.000 146.740 0 103 TRP FFF CZ2 1 ? 7  
ATOM 5911  C CZ3 . TRP D 2 106 ? 76.725  120.581 73.462 1.000 154.268 0 103 TRP FFF CZ3 1 ? 7  
ATOM 5912  C CH2 . TRP D 2 106 ? 75.539  119.973 73.031 1.000 149.591 0 103 TRP FFF CH2 1 ? 7  
ATOM 5913  N N   . GLY D 2 107 ? 81.291  119.421 77.632 1.000 158.086 0 104 GLY FFF N   1 ? 7  
ATOM 5914  C CA  . GLY D 2 107 ? 82.316  120.207 78.286 1.000 159.167 0 104 GLY FFF CA  1 ? 7  
ATOM 5915  C C   . GLY D 2 107 ? 81.762  121.431 78.994 1.000 165.312 0 104 GLY FFF C   1 ? 7  
ATOM 5916  O O   . GLY D 2 107 ? 80.565  121.716 78.976 1.000 160.153 0 104 GLY FFF O   1 ? 7  
ATOM 5917  N N   . GLN D 2 108 ? 82.667  122.175 79.638 1.000 170.311 0 105 GLN FFF N   1 ? 7  
ATOM 5918  C CA  . GLN D 2 108 ? 82.238  123.381 80.335 1.000 172.592 0 105 GLN FFF CA  1 ? 7  
ATOM 5919  C C   . GLN D 2 108 ? 82.146  124.596 79.425 1.000 164.560 0 105 GLN FFF C   1 ? 7  
ATOM 5920  O O   . GLN D 2 108 ? 81.502  125.585 79.793 1.000 163.555 0 105 GLN FFF O   1 ? 7  
ATOM 5921  C CB  . GLN D 2 108 ? 83.262  123.725 81.424 1.000 177.926 0 105 GLN FFF CB  1 ? 7  
ATOM 5922  C CG  . GLN D 2 108 ? 83.452  122.747 82.588 1.000 189.825 0 105 GLN FFF CG  1 ? 7  
ATOM 5923  C CD  . GLN D 2 108 ? 82.189  122.430 83.357 1.000 202.674 0 105 GLN FFF CD  1 ? 7  
ATOM 5924  O OE1 . GLN D 2 108 ? 81.286  121.753 82.859 1.000 210.038 0 105 GLN FFF OE1 1 ? 7  
ATOM 5925  N NE2 . GLN D 2 108 ? 82.118  122.918 84.592 1.000 206.334 0 105 GLN FFF NE2 1 ? 7  
ATOM 5926  N N   . GLY D 2 109 ? 82.786  124.558 78.270 1.000 173.818 0 106 GLY FFF N   1 ? 7  
ATOM 5927  C CA  . GLY D 2 109 ? 82.663  125.595 77.274 1.000 180.919 0 106 GLY FFF CA  1 ? 7  
ATOM 5928  C C   . GLY D 2 109 ? 83.882  126.499 77.287 1.000 181.922 0 106 GLY FFF C   1 ? 7  
ATOM 5929  O O   . GLY D 2 109 ? 84.624  126.576 78.268 1.000 184.825 0 106 GLY FFF O   1 ? 7  
ATOM 5930  N N   . THR D 2 110 ? 84.110  127.185 76.171 1.000 182.705 0 107 THR FFF N   1 ? 7  
ATOM 5931  C CA  . THR D 2 110 ? 85.153  128.199 76.110 1.000 196.909 0 107 THR FFF CA  1 ? 7  
ATOM 5932  C C   . THR D 2 110 ? 84.582  129.454 75.456 1.000 210.402 0 107 THR FFF C   1 ? 7  
ATOM 5933  O O   . THR D 2 110 ? 83.845  129.363 74.470 1.000 208.895 0 107 THR FFF O   1 ? 7  
ATOM 5934  C CB  . THR D 2 110 ? 86.396  127.686 75.366 1.000 192.255 0 107 THR FFF CB  1 ? 7  
ATOM 5935  O OG1 . THR D 2 110 ? 87.427  128.674 75.437 1.000 199.032 0 107 THR FFF OG1 1 ? 7  
ATOM 5936  C CG2 . THR D 2 110 ? 86.081  127.367 73.907 1.000 197.934 0 107 THR FFF CG2 1 ? 7  
ATOM 5937  N N   . GLN D 2 111 ? 84.911  130.625 76.003 1.000 224.745 0 108 GLN FFF N   1 ? 7  
ATOM 5938  C CA  . GLN D 2 111 ? 84.322  131.865 75.509 1.000 235.817 0 108 GLN FFF CA  1 ? 7  
ATOM 5939  C C   . GLN D 2 111 ? 85.102  132.370 74.297 1.000 240.388 0 108 GLN FFF C   1 ? 7  
ATOM 5940  O O   . GLN D 2 111 ? 86.333  132.464 74.344 1.000 245.320 0 108 GLN FFF O   1 ? 7  
ATOM 5941  C CB  . GLN D 2 111 ? 84.325  132.908 76.629 1.000 245.782 0 108 GLN FFF CB  1 ? 7  
ATOM 5942  C CG  . GLN D 2 111 ? 83.926  134.312 76.225 1.000 245.768 0 108 GLN FFF CG  1 ? 7  
ATOM 5943  C CD  . GLN D 2 111 ? 82.425  134.486 76.151 1.000 241.772 0 108 GLN FFF CD  1 ? 7  
ATOM 5944  O OE1 . GLN D 2 111 ? 81.706  134.192 77.107 1.000 236.424 0 108 GLN FFF OE1 1 ? 7  
ATOM 5945  N NE2 . GLN D 2 111 ? 81.943  134.963 75.013 1.000 244.588 0 108 GLN FFF NE2 1 ? 7  
ATOM 5946  N N   . VAL D 2 112 ? 84.398  132.686 73.209 1.000 241.812 0 109 VAL FFF N   1 ? 7  
ATOM 5947  C CA  . VAL D 2 112 ? 85.005  133.280 72.018 1.000 243.286 0 109 VAL FFF CA  1 ? 7  
ATOM 5948  C C   . VAL D 2 112 ? 84.306  134.593 71.672 1.000 251.467 0 109 VAL FFF C   1 ? 7  
ATOM 5949  O O   . VAL D 2 112 ? 83.079  134.622 71.530 1.000 258.958 0 109 VAL FFF O   1 ? 7  
ATOM 5950  C CB  . VAL D 2 112 ? 84.983  132.318 70.819 1.000 235.369 0 109 VAL FFF CB  1 ? 7  
ATOM 5951  C CG1 . VAL D 2 112 ? 85.363  133.047 69.537 1.000 232.855 0 109 VAL FFF CG1 1 ? 7  
ATOM 5952  C CG2 . VAL D 2 112 ? 85.937  131.158 71.060 1.000 232.853 0 109 VAL FFF CG2 1 ? 7  
ATOM 5953  N N   . THR D 2 113 ? 85.075  135.677 71.571 1.000 255.045 0 110 THR FFF N   1 ? 7  
ATOM 5954  C CA  . THR D 2 113 ? 84.553  137.029 71.365 1.000 252.552 0 110 THR FFF CA  1 ? 7  
ATOM 5955  C C   . THR D 2 113 ? 85.348  137.622 70.211 1.000 251.751 0 110 THR FFF C   1 ? 7  
ATOM 5956  O O   . THR D 2 113 ? 86.571  137.757 70.310 1.000 253.516 0 110 THR FFF O   1 ? 7  
ATOM 5957  C CB  . THR D 2 113 ? 84.654  137.893 72.624 1.000 255.674 0 110 THR FFF CB  1 ? 7  
ATOM 5958  O OG1 . THR D 2 113 ? 84.268  137.122 73.771 1.000 262.910 0 110 THR FFF OG1 1 ? 7  
ATOM 5959  C CG2 . THR D 2 113 ? 83.793  139.155 72.510 1.000 256.221 0 110 THR FFF CG2 1 ? 7  
ATOM 5960  N N   . VAL D 2 114 ? 84.670  137.976 69.121 1.000 251.153 0 111 VAL FFF N   1 ? 7  
ATOM 5961  C CA  . VAL D 2 114 ? 85.330  138.582 67.967 1.000 253.036 0 111 VAL FFF CA  1 ? 7  
ATOM 5962  C C   . VAL D 2 114 ? 84.901  140.033 67.796 1.000 256.476 0 111 VAL FFF C   1 ? 7  
ATOM 5963  O O   . VAL D 2 114 ? 83.709  140.322 67.625 1.000 252.643 0 111 VAL FFF O   1 ? 7  
ATOM 5964  C CB  . VAL D 2 114 ? 85.053  137.781 66.687 1.000 249.585 0 111 VAL FFF CB  1 ? 7  
ATOM 5965  C CG1 . VAL D 2 114 ? 85.937  138.280 65.559 1.000 253.822 0 111 VAL FFF CG1 1 ? 7  
ATOM 5966  C CG2 . VAL D 2 114 ? 85.284  136.300 66.934 1.000 251.099 0 111 VAL FFF CG2 1 ? 7  
ATOM 5967  N N   . SER D 2 115 ? 85.888  140.932 67.839 1.000 260.228 0 112 SER FFF N   1 ? 7  
ATOM 5968  C CA  . SER D 2 115 ? 85.826  142.301 67.312 1.000 263.091 0 112 SER FFF CA  1 ? 7  
ATOM 5969  C C   . SER D 2 115 ? 87.113  143.044 67.661 1.000 268.432 0 112 SER FFF C   1 ? 7  
ATOM 5970  O O   . SER D 2 115 ? 87.774  143.610 66.790 1.000 272.750 0 112 SER FFF O   1 ? 7  
ATOM 5971  C CB  . SER D 2 115 ? 84.626  143.084 67.842 1.000 265.727 0 112 SER FFF CB  1 ? 7  
ATOM 5972  O OG  . SER D 2 115 ? 84.189  144.019 66.869 1.000 268.205 0 112 SER FFF OG  1 ? 7  
ATOM 5973  N N   . ASP E 3 1   ? 33.246  109.195 80.860 1.000 221.459 0 1   ASP EEE N   1 ? 8  
ATOM 5974  C CA  . ASP E 3 1   ? 32.138  108.602 80.123 1.000 229.439 0 1   ASP EEE CA  1 ? 8  
ATOM 5975  C C   . ASP E 3 1   ? 31.922  109.360 78.818 1.000 235.243 0 1   ASP EEE C   1 ? 8  
ATOM 5976  O O   . ASP E 3 1   ? 32.405  110.481 78.659 1.000 237.412 0 1   ASP EEE O   1 ? 8  
ATOM 5977  C CB  . ASP E 3 1   ? 30.862  108.613 80.969 1.000 226.012 0 1   ASP EEE CB  1 ? 8  
ATOM 5978  C CG  . ASP E 3 1   ? 29.783  107.710 80.409 1.000 223.193 0 1   ASP EEE CG  1 ? 8  
ATOM 5979  O OD1 . ASP E 3 1   ? 30.133  106.694 79.773 1.000 225.169 0 1   ASP EEE OD1 1 ? 8  
ATOM 5980  O OD2 . ASP E 3 1   ? 28.587  108.019 80.596 1.000 230.369 0 1   ASP EEE OD2 1 ? 8  
ATOM 5981  N N   . VAL E 3 2   ? 31.200  108.752 77.881 1.000 231.506 0 2   VAL EEE N   1 ? 8  
ATOM 5982  C CA  . VAL E 3 2   ? 30.909  109.377 76.599 1.000 222.095 0 2   VAL EEE CA  1 ? 8  
ATOM 5983  C C   . VAL E 3 2   ? 29.475  109.881 76.613 1.000 218.097 0 2   VAL EEE C   1 ? 8  
ATOM 5984  O O   . VAL E 3 2   ? 28.538  109.102 76.829 1.000 219.270 0 2   VAL EEE O   1 ? 8  
ATOM 5985  C CB  . VAL E 3 2   ? 31.110  108.381 75.446 1.000 213.043 0 2   VAL EEE CB  1 ? 8  
ATOM 5986  C CG1 . VAL E 3 2   ? 30.785  109.035 74.136 1.000 219.084 0 2   VAL EEE CG1 1 ? 8  
ATOM 5987  C CG2 . VAL E 3 2   ? 32.525  107.820 75.451 1.000 205.089 0 2   VAL EEE CG2 1 ? 8  
ATOM 5988  N N   . GLN E 3 3   ? 29.301  111.181 76.383 1.000 203.022 0 3   GLN EEE N   1 ? 8  
ATOM 5989  C CA  . GLN E 3 3   ? 27.988  111.808 76.404 1.000 205.916 0 3   GLN EEE CA  1 ? 8  
ATOM 5990  C C   . GLN E 3 3   ? 27.672  112.408 75.040 1.000 202.037 0 3   GLN EEE C   1 ? 8  
ATOM 5991  O O   . GLN E 3 3   ? 28.520  113.076 74.444 1.000 197.460 0 3   GLN EEE O   1 ? 8  
ATOM 5992  C CB  . GLN E 3 3   ? 27.963  112.873 77.495 1.000 212.803 0 3   GLN EEE CB  1 ? 8  
ATOM 5993  C CG  . GLN E 3 3   ? 28.190  112.265 78.872 1.000 216.698 0 3   GLN EEE CG  1 ? 8  
ATOM 5994  C CD  . GLN E 3 3   ? 28.983  113.170 79.773 1.000 220.811 0 3   GLN EEE CD  1 ? 8  
ATOM 5995  O OE1 . GLN E 3 3   ? 29.812  113.946 79.306 1.000 220.880 0 3   GLN EEE OE1 1 ? 8  
ATOM 5996  N NE2 . GLN E 3 3   ? 28.675  113.136 81.070 1.000 223.330 0 3   GLN EEE NE2 1 ? 8  
ATOM 5997  N N   . LEU E 3 4   ? 26.452  112.177 74.553 1.000 204.244 0 4   LEU EEE N   1 ? 8  
ATOM 5998  C CA  . LEU E 3 4   ? 26.013  112.761 73.290 1.000 210.381 0 4   LEU EEE CA  1 ? 8  
ATOM 5999  C C   . LEU E 3 4   ? 24.691  113.491 73.474 1.000 218.617 0 4   LEU EEE C   1 ? 8  
ATOM 6000  O O   . LEU E 3 4   ? 23.823  113.031 74.222 1.000 218.773 0 4   LEU EEE O   1 ? 8  
ATOM 6001  C CB  . LEU E 3 4   ? 25.885  111.695 72.185 1.000 210.110 0 4   LEU EEE CB  1 ? 8  
ATOM 6002  C CG  . LEU E 3 4   ? 27.192  111.013 71.758 1.000 202.492 0 4   LEU EEE CG  1 ? 8  
ATOM 6003  C CD1 . LEU E 3 4   ? 27.522  109.810 72.624 1.000 182.873 0 4   LEU EEE CD1 1 ? 8  
ATOM 6004  C CD2 . LEU E 3 4   ? 27.178  110.614 70.287 1.000 201.734 0 4   LEU EEE CD2 1 ? 8  
ATOM 6005  N N   . GLN E 3 5   ? 24.526  114.615 72.777 1.000 223.395 0 5   GLN EEE N   1 ? 8  
ATOM 6006  C CA  . GLN E 3 5   ? 23.244  115.317 72.782 1.000 221.059 0 5   GLN EEE CA  1 ? 8  
ATOM 6007  C C   . GLN E 3 5   ? 23.012  115.938 71.412 1.000 225.079 0 5   GLN EEE C   1 ? 8  
ATOM 6008  O O   . GLN E 3 5   ? 23.813  116.763 70.960 1.000 225.332 0 5   GLN EEE O   1 ? 8  
ATOM 6009  C CB  . GLN E 3 5   ? 23.154  116.373 73.887 1.000 220.637 0 5   GLN EEE CB  1 ? 8  
ATOM 6010  C CG  . GLN E 3 5   ? 22.118  116.013 74.969 1.000 230.903 0 5   GLN EEE CG  1 ? 8  
ATOM 6011  C CD  . GLN E 3 5   ? 20.671  116.184 74.504 1.000 234.251 0 5   GLN EEE CD  1 ? 8  
ATOM 6012  O OE1 . GLN E 3 5   ? 20.411  116.456 73.332 1.000 232.841 0 5   GLN EEE OE1 1 ? 8  
ATOM 6013  N NE2 . GLN E 3 5   ? 19.725  116.006 75.423 1.000 248.172 0 5   GLN EEE NE2 1 ? 8  
ATOM 6014  N N   . GLU E 3 6   ? 21.911  115.552 70.772 1.000 231.459 0 6   GLU EEE N   1 ? 8  
ATOM 6015  C CA  . GLU E 3 6   ? 21.437  116.112 69.513 1.000 236.823 0 6   GLU EEE CA  1 ? 8  
ATOM 6016  C C   . GLU E 3 6   ? 20.685  117.427 69.720 1.000 239.170 0 6   GLU EEE C   1 ? 8  
ATOM 6017  O O   . GLU E 3 6   ? 20.209  117.736 70.815 1.000 246.055 0 6   GLU EEE O   1 ? 8  
ATOM 6018  C CB  . GLU E 3 6   ? 20.528  115.118 68.790 1.000 240.179 0 6   GLU EEE CB  1 ? 8  
ATOM 6019  C CG  . GLU E 3 6   ? 19.640  114.318 69.713 1.000 244.164 0 6   GLU EEE CG  1 ? 8  
ATOM 6020  C CD  . GLU E 3 6   ? 20.321  113.067 70.208 1.000 240.782 0 6   GLU EEE CD  1 ? 8  
ATOM 6021  O OE1 . GLU E 3 6   ? 21.182  113.203 71.101 1.000 242.671 0 6   GLU EEE OE1 1 ? 8  
ATOM 6022  O OE2 . GLU E 3 6   ? 20.014  111.964 69.708 1.000 234.252 0 6   GLU EEE OE2 1 ? 8  
ATOM 6023  N N   . SER E 3 7   ? 20.574  118.197 68.635 1.000 237.196 0 7   SER EEE N   1 ? 8  
ATOM 6024  C CA  . SER E 3 7   ? 19.809  119.441 68.607 1.000 236.769 0 7   SER EEE CA  1 ? 8  
ATOM 6025  C C   . SER E 3 7   ? 19.645  119.877 67.156 1.000 242.648 0 7   SER EEE C   1 ? 8  
ATOM 6026  O O   . SER E 3 7   ? 20.258  119.316 66.244 1.000 244.997 0 7   SER EEE O   1 ? 8  
ATOM 6027  C CB  . SER E 3 7   ? 20.483  120.552 69.418 1.000 236.721 0 7   SER EEE CB  1 ? 8  
ATOM 6028  O OG  . SER E 3 7   ? 21.725  120.934 68.845 1.000 220.269 0 7   SER EEE OG  1 ? 8  
ATOM 6029  N N   . GLY E 3 8   ? 18.812  120.899 66.955 1.000 243.798 0 8   GLY EEE N   1 ? 8  
ATOM 6030  C CA  . GLY E 3 8   ? 18.512  121.406 65.632 1.000 240.300 0 8   GLY EEE CA  1 ? 8  
ATOM 6031  C C   . GLY E 3 8   ? 17.259  120.866 64.977 1.000 243.375 0 8   GLY EEE C   1 ? 8  
ATOM 6032  O O   . GLY E 3 8   ? 16.963  121.261 63.842 1.000 238.054 0 8   GLY EEE O   1 ? 8  
ATOM 6033  N N   . GLY E 3 9   ? 16.515  119.974 65.638 1.000 255.277 0 9   GLY EEE N   1 ? 8  
ATOM 6034  C CA  . GLY E 3 9   ? 15.307  119.466 65.033 1.000 262.506 0 9   GLY EEE CA  1 ? 8  
ATOM 6035  C C   . GLY E 3 9   ? 14.134  120.381 65.305 1.000 277.063 0 9   GLY EEE C   1 ? 8  
ATOM 6036  O O   . GLY E 3 9   ? 14.141  121.156 66.260 1.000 282.847 0 9   GLY EEE O   1 ? 8  
ATOM 6037  N N   . GLY E 3 10  ? 13.113  120.273 64.462 1.000 273.497 0 10  GLY EEE N   1 ? 8  
ATOM 6038  C CA  . GLY E 3 10  ? 11.939  121.111 64.623 1.000 285.054 0 10  GLY EEE CA  1 ? 8  
ATOM 6039  C C   . GLY E 3 10  ? 10.968  120.912 63.476 1.000 288.622 0 10  GLY EEE C   1 ? 8  
ATOM 6040  O O   . GLY E 3 10  ? 10.991  119.888 62.790 1.000 297.971 0 10  GLY EEE O   1 ? 8  
ATOM 6041  N N   . LEU E 3 11  ? 10.110  121.917 63.293 1.000 292.124 0 11  LEU EEE N   1 ? 8  
ATOM 6042  C CA  . LEU E 3 11  ? 9.022   121.895 62.324 1.000 288.431 0 11  LEU EEE CA  1 ? 8  
ATOM 6043  C C   . LEU E 3 11  ? 9.447   122.866 61.232 1.000 288.703 0 11  LEU EEE C   1 ? 8  
ATOM 6044  O O   . LEU E 3 11  ? 9.774   124.023 61.515 1.000 286.759 0 11  LEU EEE O   1 ? 8  
ATOM 6045  C CB  . LEU E 3 11  ? 7.678   122.298 62.957 1.000 287.114 0 11  LEU EEE CB  1 ? 8  
ATOM 6046  C CG  . LEU E 3 11  ? 6.359   122.363 62.155 1.000 284.221 0 11  LEU EEE CG  1 ? 8  
ATOM 6047  C CD1 . LEU E 3 11  ? 6.196   121.202 61.234 1.000 286.937 0 11  LEU EEE CD1 1 ? 8  
ATOM 6048  C CD2 . LEU E 3 11  ? 5.127   122.427 63.070 1.000 287.784 0 11  LEU EEE CD2 1 ? 8  
ATOM 6049  N N   . VAL E 3 12  ? 9.419   122.392 59.987 1.000 288.848 0 12  VAL EEE N   1 ? 8  
ATOM 6050  C CA  . VAL E 3 12  ? 9.876   123.133 58.819 1.000 297.468 0 12  VAL EEE CA  1 ? 8  
ATOM 6051  C C   . VAL E 3 12  ? 8.931   122.834 57.668 1.000 312.271 0 12  VAL EEE C   1 ? 8  
ATOM 6052  O O   . VAL E 3 12  ? 8.220   121.827 57.665 1.000 318.624 0 12  VAL EEE O   1 ? 8  
ATOM 6053  C CB  . VAL E 3 12  ? 11.331  122.795 58.423 1.000 295.748 0 12  VAL EEE CB  1 ? 8  
ATOM 6054  C CG1 . VAL E 3 12  ? 12.287  123.120 59.562 1.000 286.021 0 12  VAL EEE CG1 1 ? 8  
ATOM 6055  C CG2 . VAL E 3 12  ? 11.440  121.333 58.040 1.000 297.217 0 12  VAL EEE CG2 1 ? 8  
ATOM 6056  N N   . GLN E 3 13  ? 8.917   123.725 56.685 1.000 318.474 0 13  GLN EEE N   1 ? 8  
ATOM 6057  C CA  . GLN E 3 13  ? 8.120   123.399 55.518 1.000 317.322 0 13  GLN EEE CA  1 ? 8  
ATOM 6058  C C   . GLN E 3 13  ? 8.866   122.442 54.596 1.000 312.240 0 13  GLN EEE C   1 ? 8  
ATOM 6059  O O   . GLN E 3 13  ? 10.088  122.276 54.666 1.000 309.209 0 13  GLN EEE O   1 ? 8  
ATOM 6060  C CB  . GLN E 3 13  ? 7.780   124.673 54.744 1.000 312.394 0 13  GLN EEE CB  1 ? 8  
ATOM 6061  C CG  . GLN E 3 13  ? 8.939   125.288 53.952 1.000 309.914 0 13  GLN EEE CG  1 ? 8  
ATOM 6062  C CD  . GLN E 3 13  ? 10.160  125.591 54.792 1.000 307.412 0 13  GLN EEE CD  1 ? 8  
ATOM 6063  O OE1 . GLN E 3 13  ? 10.092  125.637 56.019 1.000 304.081 0 13  GLN EEE OE1 1 ? 8  
ATOM 6064  N NE2 . GLN E 3 13  ? 11.274  125.862 54.129 1.000 310.107 0 13  GLN EEE NE2 1 ? 8  
ATOM 6065  N N   . ALA E 3 14  ? 8.084   121.794 53.740 1.000 307.589 0 14  ALA EEE N   1 ? 8  
ATOM 6066  C CA  . ALA E 3 14  ? 8.596   120.902 52.709 1.000 300.948 0 14  ALA EEE CA  1 ? 8  
ATOM 6067  C C   . ALA E 3 14  ? 9.569   121.605 51.772 1.000 303.511 0 14  ALA EEE C   1 ? 8  
ATOM 6068  O O   . ALA E 3 14  ? 9.406   122.785 51.451 1.000 320.807 0 14  ALA EEE O   1 ? 8  
ATOM 6069  C CB  . ALA E 3 14  ? 7.430   120.321 51.912 1.000 299.837 0 14  ALA EEE CB  1 ? 8  
ATOM 6070  N N   . GLY E 3 15  ? 10.588  120.871 51.335 1.000 291.879 0 15  GLY EEE N   1 ? 8  
ATOM 6071  C CA  . GLY E 3 15  ? 11.623  121.416 50.483 1.000 289.018 0 15  GLY EEE CA  1 ? 8  
ATOM 6072  C C   . GLY E 3 15  ? 12.697  122.212 51.181 1.000 292.924 0 15  GLY EEE C   1 ? 8  
ATOM 6073  O O   . GLY E 3 15  ? 13.634  122.670 50.515 1.000 292.156 0 15  GLY EEE O   1 ? 8  
ATOM 6074  N N   . GLY E 3 16  ? 12.609  122.378 52.494 1.000 302.885 0 16  GLY EEE N   1 ? 8  
ATOM 6075  C CA  . GLY E 3 16  ? 13.590  123.144 53.224 1.000 297.740 0 16  GLY EEE CA  1 ? 8  
ATOM 6076  C C   . GLY E 3 16  ? 14.803  122.295 53.514 1.000 286.361 0 16  GLY EEE C   1 ? 8  
ATOM 6077  O O   . GLY E 3 16  ? 14.919  121.147 53.084 1.000 287.231 0 16  GLY EEE O   1 ? 8  
ATOM 6078  N N   . SER E 3 17  ? 15.732  122.871 54.265 1.000 275.322 0 17  SER EEE N   1 ? 8  
ATOM 6079  C CA  . SER E 3 17  ? 16.937  122.148 54.621 1.000 259.926 0 17  SER EEE CA  1 ? 8  
ATOM 6080  C C   . SER E 3 17  ? 17.155  122.292 56.115 1.000 257.199 0 17  SER EEE C   1 ? 8  
ATOM 6081  O O   . SER E 3 17  ? 16.684  123.236 56.755 1.000 260.764 0 17  SER EEE O   1 ? 8  
ATOM 6082  C CB  . SER E 3 17  ? 18.170  122.654 53.855 1.000 255.310 0 17  SER EEE CB  1 ? 8  
ATOM 6083  O OG  . SER E 3 17  ? 18.310  124.059 53.975 1.000 252.053 0 17  SER EEE OG  1 ? 8  
ATOM 6084  N N   . LEU E 3 18  ? 17.886  121.330 56.658 1.000 256.179 0 18  LEU EEE N   1 ? 8  
ATOM 6085  C CA  . LEU E 3 18  ? 18.185  121.302 58.076 1.000 247.492 0 18  LEU EEE CA  1 ? 8  
ATOM 6086  C C   . LEU E 3 18  ? 19.453  120.496 58.274 1.000 245.334 0 18  LEU EEE C   1 ? 8  
ATOM 6087  O O   . LEU E 3 18  ? 19.760  119.592 57.494 1.000 249.588 0 18  LEU EEE O   1 ? 8  
ATOM 6088  C CB  . LEU E 3 18  ? 17.024  120.693 58.871 1.000 243.456 0 18  LEU EEE CB  1 ? 8  
ATOM 6089  C CG  . LEU E 3 18  ? 16.920  120.965 60.373 1.000 245.633 0 18  LEU EEE CG  1 ? 8  
ATOM 6090  C CD1 . LEU E 3 18  ? 17.139  122.437 60.672 1.000 245.370 0 18  LEU EEE CD1 1 ? 8  
ATOM 6091  C CD2 . LEU E 3 18  ? 15.572  120.498 60.908 1.000 245.306 0 18  LEU EEE CD2 1 ? 8  
ATOM 6092  N N   . ARG E 3 19  ? 20.174  120.821 59.333 1.000 238.680 0 19  ARG EEE N   1 ? 8  
ATOM 6093  C CA  . ARG E 3 19  ? 21.386  120.101 59.685 1.000 230.402 0 19  ARG EEE CA  1 ? 8  
ATOM 6094  C C   . ARG E 3 19  ? 21.190  119.702 61.135 1.000 232.930 0 19  ARG EEE C   1 ? 8  
ATOM 6095  O O   . ARG E 3 19  ? 21.168  120.564 62.020 1.000 245.835 0 19  ARG EEE O   1 ? 8  
ATOM 6096  C CB  . ARG E 3 19  ? 22.622  120.990 59.528 1.000 222.965 0 19  ARG EEE CB  1 ? 8  
ATOM 6097  C CG  . ARG E 3 19  ? 23.960  120.289 59.377 1.000 220.911 0 19  ARG EEE CG  1 ? 8  
ATOM 6098  C CD  . ARG E 3 19  ? 25.018  121.320 59.002 1.000 218.254 0 19  ARG EEE CD  1 ? 8  
ATOM 6099  N NE  . ARG E 3 19  ? 26.227  120.734 58.438 1.000 223.467 0 19  ARG EEE NE  1 ? 8  
ATOM 6100  C CZ  . ARG E 3 19  ? 26.479  120.629 57.141 1.000 221.187 0 19  ARG EEE CZ  1 ? 8  
ATOM 6101  N NH1 . ARG E 3 19  ? 25.618  121.056 56.231 1.000 224.673 0 19  ARG EEE NH1 1 ? 8  
ATOM 6102  N NH2 . ARG E 3 19  ? 27.626  120.083 56.747 1.000 213.201 0 19  ARG EEE NH2 1 ? 8  
ATOM 6103  N N   . LEU E 3 20  ? 21.051  118.411 61.390 1.000 227.271 0 20  LEU EEE N   1 ? 8  
ATOM 6104  C CA  . LEU E 3 20  ? 20.973  118.000 62.773 1.000 223.490 0 20  LEU EEE CA  1 ? 8  
ATOM 6105  C C   . LEU E 3 20  ? 22.403  117.770 63.222 1.000 227.974 0 20  LEU EEE C   1 ? 8  
ATOM 6106  O O   . LEU E 3 20  ? 23.253  117.334 62.442 1.000 242.281 0 20  LEU EEE O   1 ? 8  
ATOM 6107  C CB  . LEU E 3 20  ? 20.111  116.746 62.944 1.000 218.531 0 20  LEU EEE CB  1 ? 8  
ATOM 6108  C CG  . LEU E 3 20  ? 18.753  116.779 62.234 1.000 221.268 0 20  LEU EEE CG  1 ? 8  
ATOM 6109  C CD1 . LEU E 3 20  ? 17.996  115.473 62.438 1.000 213.855 0 20  LEU EEE CD1 1 ? 8  
ATOM 6110  C CD2 . LEU E 3 20  ? 17.924  117.963 62.707 1.000 235.615 0 20  LEU EEE CD2 1 ? 8  
ATOM 6111  N N   . SER E 3 21  ? 22.672  118.059 64.483 1.000 225.908 0 21  SER EEE N   1 ? 8  
ATOM 6112  C CA  . SER E 3 21  ? 24.027  117.887 64.971 1.000 231.126 0 21  SER EEE CA  1 ? 8  
ATOM 6113  C C   . SER E 3 21  ? 24.016  117.236 66.338 1.000 240.134 0 21  SER EEE C   1 ? 8  
ATOM 6114  O O   . SER E 3 21  ? 23.211  117.586 67.205 1.000 248.901 0 21  SER EEE O   1 ? 8  
ATOM 6115  C CB  . SER E 3 21  ? 24.774  119.227 65.018 1.000 229.634 0 21  SER EEE CB  1 ? 8  
ATOM 6116  O OG  . SER E 3 21  ? 24.826  119.824 63.731 1.000 221.644 0 21  SER EEE OG  1 ? 8  
ATOM 6117  N N   . CYS E 3 22  ? 24.928  116.295 66.521 1.000 262.798 0 22  CYS EEE N   1 ? 8  
ATOM 6118  C CA  . CYS E 3 22  ? 25.023  115.514 67.742 1.000 263.171 0 22  CYS EEE CA  1 ? 8  
ATOM 6119  C C   . CYS E 3 22  ? 26.399  115.810 68.323 1.000 258.190 0 22  CYS EEE C   1 ? 8  
ATOM 6120  O O   . CYS E 3 22  ? 27.421  115.426 67.745 1.000 255.407 0 22  CYS EEE O   1 ? 8  
ATOM 6121  C CB  . CYS E 3 22  ? 24.813  114.028 67.457 1.000 270.879 0 22  CYS EEE CB  1 ? 8  
ATOM 6122  S SG  . CYS E 3 22  ? 25.071  112.936 68.855 1.000 282.333 0 22  CYS EEE SG  1 ? 8  
ATOM 6123  N N   . ALA E 3 23  ? 26.419  116.482 69.470 1.000 238.847 0 23  ALA EEE N   1 ? 8  
ATOM 6124  C CA  . ALA E 3 23  ? 27.660  116.831 70.139 1.000 226.021 0 23  ALA EEE CA  1 ? 8  
ATOM 6125  C C   . ALA E 3 23  ? 28.070  115.700 71.066 1.000 219.820 0 23  ALA EEE C   1 ? 8  
ATOM 6126  O O   . ALA E 3 23  ? 27.254  115.165 71.818 1.000 219.070 0 23  ALA EEE O   1 ? 8  
ATOM 6127  C CB  . ALA E 3 23  ? 27.506  118.129 70.933 1.000 223.668 0 23  ALA EEE CB  1 ? 8  
ATOM 6128  N N   . ALA E 3 24  ? 29.349  115.359 71.017 1.000 215.753 0 24  ALA EEE N   1 ? 8  
ATOM 6129  C CA  . ALA E 3 24  ? 29.920  114.273 71.794 1.000 207.211 0 24  ALA EEE CA  1 ? 8  
ATOM 6130  C C   . ALA E 3 24  ? 31.026  114.835 72.667 1.000 207.933 0 24  ALA EEE C   1 ? 8  
ATOM 6131  O O   . ALA E 3 24  ? 31.750  115.748 72.259 1.000 217.849 0 24  ALA EEE O   1 ? 8  
ATOM 6132  C CB  . ALA E 3 24  ? 30.459  113.161 70.890 1.000 205.411 0 24  ALA EEE CB  1 ? 8  
ATOM 6133  N N   . SER E 3 25  ? 31.154  114.293 73.870 1.000 201.548 0 25  SER EEE N   1 ? 8  
ATOM 6134  C CA  . SER E 3 25  ? 32.292  114.686 74.676 1.000 196.054 0 25  SER EEE CA  1 ? 8  
ATOM 6135  C C   . SER E 3 25  ? 33.550  113.981 74.190 1.000 194.959 0 25  SER EEE C   1 ? 8  
ATOM 6136  O O   . SER E 3 25  ? 33.507  112.911 73.576 1.000 198.658 0 25  SER EEE O   1 ? 8  
ATOM 6137  C CB  . SER E 3 25  ? 32.053  114.360 76.148 1.000 194.695 0 25  SER EEE CB  1 ? 8  
ATOM 6138  O OG  . SER E 3 25  ? 31.828  112.973 76.326 1.000 193.016 0 25  SER EEE OG  1 ? 8  
ATOM 6139  N N   . GLY E 3 26  ? 34.683  114.599 74.492 1.000 198.444 0 26  GLY EEE N   1 ? 8  
ATOM 6140  C CA  . GLY E 3 26  ? 35.931  114.123 73.960 1.000 212.864 0 26  GLY EEE CA  1 ? 8  
ATOM 6141  C C   . GLY E 3 26  ? 36.051  114.347 72.456 1.000 223.462 0 26  GLY EEE C   1 ? 8  
ATOM 6142  O O   . GLY E 3 26  ? 35.344  115.149 71.839 1.000 220.446 0 26  GLY EEE O   1 ? 8  
ATOM 6143  N N   . SER E 3 27  ? 36.985  113.603 71.880 1.000 217.125 0 27  SER EEE N   1 ? 8  
ATOM 6144  C CA  . SER E 3 27  ? 37.306  113.611 70.457 1.000 216.098 0 27  SER EEE CA  1 ? 8  
ATOM 6145  C C   . SER E 3 27  ? 36.533  112.543 69.692 1.000 211.958 0 27  SER EEE C   1 ? 8  
ATOM 6146  O O   . SER E 3 27  ? 36.401  111.406 70.154 1.000 217.530 0 27  SER EEE O   1 ? 8  
ATOM 6147  C CB  . SER E 3 27  ? 38.808  113.412 70.240 1.000 217.258 0 27  SER EEE CB  1 ? 8  
ATOM 6148  O OG  . SER E 3 27  ? 39.561  114.423 70.888 1.000 222.844 0 27  SER EEE OG  1 ? 8  
ATOM 6149  N N   . ILE E 3 28  ? 36.017  112.916 68.515 1.000 208.144 0 28  ILE EEE N   1 ? 8  
ATOM 6150  C CA  . ILE E 3 28  ? 35.188  111.985 67.756 1.000 200.868 0 28  ILE EEE CA  1 ? 8  
ATOM 6151  C C   . ILE E 3 28  ? 36.055  110.912 67.121 1.000 205.361 0 28  ILE EEE C   1 ? 8  
ATOM 6152  O O   . ILE E 3 28  ? 35.581  109.791 66.888 1.000 207.059 0 28  ILE EEE O   1 ? 8  
ATOM 6153  C CB  . ILE E 3 28  ? 34.376  112.715 66.659 1.000 192.790 0 28  ILE EEE CB  1 ? 8  
ATOM 6154  C CG1 . ILE E 3 28  ? 33.063  113.270 67.200 1.000 192.133 0 28  ILE EEE CG1 1 ? 8  
ATOM 6155  C CG2 . ILE E 3 28  ? 34.119  111.833 65.428 1.000 194.593 0 28  ILE EEE CG2 1 ? 8  
ATOM 6156  C CD1 . ILE E 3 28  ? 32.324  114.110 66.188 1.000 195.641 0 28  ILE EEE CD1 1 ? 8  
ATOM 6157  N N   . SER E 3 29  ? 37.343  111.190 66.915 1.000 207.236 0 29  SER EEE N   1 ? 8  
ATOM 6158  C CA  . SER E 3 29  ? 38.217  110.190 66.320 1.000 199.351 0 29  SER EEE CA  1 ? 8  
ATOM 6159  C C   . SER E 3 29  ? 38.434  109.009 67.253 1.000 196.615 0 29  SER EEE C   1 ? 8  
ATOM 6160  O O   . SER E 3 29  ? 39.001  107.997 66.826 1.000 189.029 0 29  SER EEE O   1 ? 8  
ATOM 6161  C CB  . SER E 3 29  ? 39.568  110.808 65.958 1.000 199.506 0 29  SER EEE CB  1 ? 8  
ATOM 6162  O OG  . SER E 3 29  ? 40.438  109.835 65.404 1.000 204.338 0 29  SER EEE OG  1 ? 8  
ATOM 6163  N N   . ARG E 3 30  ? 38.011  109.121 68.517 1.000 215.632 0 30  ARG EEE N   1 ? 8  
ATOM 6164  C CA  . ARG E 3 30  ? 38.176  108.023 69.454 1.000 216.548 0 30  ARG EEE CA  1 ? 8  
ATOM 6165  C C   . ARG E 3 30  ? 37.099  106.970 69.268 1.000 212.170 0 30  ARG EEE C   1 ? 8  
ATOM 6166  O O   . ARG E 3 30  ? 37.311  105.805 69.611 1.000 207.501 0 30  ARG EEE O   1 ? 8  
ATOM 6167  C CB  . ARG E 3 30  ? 38.025  108.573 70.876 1.000 220.449 0 30  ARG EEE CB  1 ? 8  
ATOM 6168  C CG  . ARG E 3 30  ? 38.962  109.698 71.288 1.000 224.351 0 30  ARG EEE CG  1 ? 8  
ATOM 6169  C CD  . ARG E 3 30  ? 38.734  110.058 72.762 1.000 226.128 0 30  ARG EEE CD  1 ? 8  
ATOM 6170  N NE  . ARG E 3 30  ? 37.305  110.073 73.071 1.000 226.213 0 30  ARG EEE NE  1 ? 8  
ATOM 6171  C CZ  . ARG E 3 30  ? 36.781  110.331 74.263 1.000 231.586 0 30  ARG EEE CZ  1 ? 8  
ATOM 6172  N NH1 . ARG E 3 30  ? 37.540  110.611 75.310 1.000 236.140 0 30  ARG EEE NH1 1 ? 8  
ATOM 6173  N NH2 . ARG E 3 30  ? 35.458  110.314 74.408 1.000 226.149 0 30  ARG EEE NH2 1 ? 8  
ATOM 6174  N N   . PHE E 3 31  ? 35.957  107.371 68.717 1.000 202.976 0 31  PHE EEE N   1 ? 8  
ATOM 6175  C CA  . PHE E 3 31  ? 34.843  106.468 68.471 1.000 193.176 0 31  PHE EEE CA  1 ? 8  
ATOM 6176  C C   . PHE E 3 31  ? 35.167  105.527 67.321 1.000 180.234 0 31  PHE EEE C   1 ? 8  
ATOM 6177  O O   . PHE E 3 31  ? 35.759  105.944 66.322 1.000 176.264 0 31  PHE EEE O   1 ? 8  
ATOM 6178  C CB  . PHE E 3 31  ? 33.593  107.288 68.178 1.000 201.959 0 31  PHE EEE CB  1 ? 8  
ATOM 6179  C CG  . PHE E 3 31  ? 33.230  108.211 69.299 1.000 199.816 0 31  PHE EEE CG  1 ? 8  
ATOM 6180  C CD1 . PHE E 3 31  ? 33.125  107.738 70.591 1.000 198.883 0 31  PHE EEE CD1 1 ? 8  
ATOM 6181  C CD2 . PHE E 3 31  ? 33.066  109.566 69.070 1.000 202.426 0 31  PHE EEE CD2 1 ? 8  
ATOM 6182  C CE1 . PHE E 3 31  ? 32.833  108.589 71.621 1.000 205.690 0 31  PHE EEE CE1 1 ? 8  
ATOM 6183  C CE2 . PHE E 3 31  ? 32.766  110.425 70.102 1.000 208.895 0 31  PHE EEE CE2 1 ? 8  
ATOM 6184  C CZ  . PHE E 3 31  ? 32.648  109.935 71.380 1.000 212.177 0 31  PHE EEE CZ  1 ? 8  
ATOM 6185  N N   . ASN E 3 32  ? 34.741  104.264 67.420 1.000 172.770 0 32  ASN EEE N   1 ? 8  
ATOM 6186  C CA  . ASN E 3 32  ? 35.014  103.351 66.311 1.000 157.758 0 32  ASN EEE CA  1 ? 8  
ATOM 6187  C C   . ASN E 3 32  ? 33.914  103.358 65.257 1.000 151.639 0 32  ASN EEE C   1 ? 8  
ATOM 6188  O O   . ASN E 3 32  ? 34.152  102.879 64.147 1.000 150.147 0 32  ASN EEE O   1 ? 8  
ATOM 6189  C CB  . ASN E 3 32  ? 35.215  101.903 66.798 1.000 146.686 0 32  ASN EEE CB  1 ? 8  
ATOM 6190  C CG  . ASN E 3 32  ? 36.394  101.746 67.752 1.000 146.004 0 32  ASN EEE CG  1 ? 8  
ATOM 6191  O OD1 . ASN E 3 32  ? 37.474  102.282 67.513 1.000 147.742 0 32  ASN EEE OD1 1 ? 8  
ATOM 6192  N ND2 . ASN E 3 32  ? 36.183  101.012 68.845 1.000 146.878 0 32  ASN EEE ND2 1 ? 8  
ATOM 6193  N N   . ALA E 3 33  ? 32.735  103.899 65.568 1.000 158.408 0 33  ALA EEE N   1 ? 8  
ATOM 6194  C CA  . ALA E 3 33  ? 31.647  104.025 64.602 1.000 156.352 0 33  ALA EEE CA  1 ? 8  
ATOM 6195  C C   . ALA E 3 33  ? 30.625  105.011 65.151 1.000 165.765 0 33  ALA EEE C   1 ? 8  
ATOM 6196  O O   . ALA E 3 33  ? 30.376  105.027 66.359 1.000 177.432 0 33  ALA EEE O   1 ? 8  
ATOM 6197  C CB  . ALA E 3 33  ? 30.988  102.668 64.321 1.000 147.202 0 33  ALA EEE CB  1 ? 8  
ATOM 6198  N N   . MET E 3 34  ? 30.029  105.821 64.276 1.000 171.879 0 34  MET EEE N   1 ? 8  
ATOM 6199  C CA  . MET E 3 34  ? 28.932  106.689 64.687 1.000 177.874 0 34  MET EEE CA  1 ? 8  
ATOM 6200  C C   . MET E 3 34  ? 27.855  106.711 63.608 1.000 176.593 0 34  MET EEE C   1 ? 8  
ATOM 6201  O O   . MET E 3 34  ? 28.102  106.344 62.457 1.000 179.166 0 34  MET EEE O   1 ? 8  
ATOM 6202  C CB  . MET E 3 34  ? 29.435  108.116 64.924 1.000 190.422 0 34  MET EEE CB  1 ? 8  
ATOM 6203  C CG  . MET E 3 34  ? 30.107  108.353 66.249 1.000 205.687 0 34  MET EEE CG  1 ? 8  
ATOM 6204  S SD  . MET E 3 34  ? 31.479  109.497 66.036 1.000 219.557 0 34  MET EEE SD  1 ? 8  
ATOM 6205  C CE  . MET E 3 34  ? 32.513  108.564 64.905 1.000 212.715 0 34  MET EEE CE  1 ? 8  
ATOM 6206  N N   . GLY E 3 35  ? 26.652  107.138 63.984 1.000 185.389 0 35  GLY EEE N   1 ? 8  
ATOM 6207  C CA  . GLY E 3 35  ? 25.580  107.221 63.007 1.000 191.833 0 35  GLY EEE CA  1 ? 8  
ATOM 6208  C C   . GLY E 3 35  ? 24.295  107.775 63.592 1.000 198.839 0 35  GLY EEE C   1 ? 8  
ATOM 6209  O O   . GLY E 3 35  ? 24.255  108.255 64.726 1.000 205.818 0 35  GLY EEE O   1 ? 8  
ATOM 6210  N N   . TRP E 3 36  ? 23.236  107.679 62.780 1.000 184.712 0 36  TRP EEE N   1 ? 8  
ATOM 6211  C CA  . TRP E 3 36  ? 21.920  108.266 63.033 1.000 181.836 0 36  TRP EEE CA  1 ? 8  
ATOM 6212  C C   . TRP E 3 36  ? 20.803  107.271 62.746 1.000 179.482 0 36  TRP EEE C   1 ? 8  
ATOM 6213  O O   . TRP E 3 36  ? 20.786  106.632 61.689 1.000 182.000 0 36  TRP EEE O   1 ? 8  
ATOM 6214  C CB  . TRP E 3 36  ? 21.693  109.545 62.209 1.000 181.834 0 36  TRP EEE CB  1 ? 8  
ATOM 6215  C CG  . TRP E 3 36  ? 22.429  110.767 62.668 1.000 194.978 0 36  TRP EEE CG  1 ? 8  
ATOM 6216  C CD1 . TRP E 3 36  ? 23.581  111.292 62.160 1.000 197.763 0 36  TRP EEE CD1 1 ? 8  
ATOM 6217  C CD2 . TRP E 3 36  ? 21.951  111.716 63.631 1.000 204.723 0 36  TRP EEE CD2 1 ? 8  
ATOM 6218  N NE1 . TRP E 3 36  ? 23.896  112.463 62.815 1.000 201.949 0 36  TRP EEE NE1 1 ? 8  
ATOM 6219  C CE2 . TRP E 3 36  ? 22.903  112.748 63.715 1.000 210.733 0 36  TRP EEE CE2 1 ? 8  
ATOM 6220  C CE3 . TRP E 3 36  ? 20.822  111.771 64.455 1.000 211.817 0 36  TRP EEE CE3 1 ? 8  
ATOM 6221  C CZ2 . TRP E 3 36  ? 22.762  113.825 64.593 1.000 221.677 0 36  TRP EEE CZ2 1 ? 8  
ATOM 6222  C CZ3 . TRP E 3 36  ? 20.684  112.837 65.326 1.000 219.675 0 36  TRP EEE CZ3 1 ? 8  
ATOM 6223  C CH2 . TRP E 3 36  ? 21.648  113.849 65.388 1.000 223.830 0 36  TRP EEE CH2 1 ? 8  
ATOM 6224  N N   . TRP E 3 37  ? 19.874  107.157 63.689 1.000 180.169 0 37  TRP EEE N   1 ? 8  
ATOM 6225  C CA  . TRP E 3 37  ? 18.613  106.436 63.567 1.000 182.691 0 37  TRP EEE CA  1 ? 8  
ATOM 6226  C C   . TRP E 3 37  ? 17.465  107.379 63.885 1.000 198.246 0 37  TRP EEE C   1 ? 8  
ATOM 6227  O O   . TRP E 3 37  ? 17.670  108.454 64.456 1.000 206.691 0 37  TRP EEE O   1 ? 8  
ATOM 6228  C CB  . TRP E 3 37  ? 18.533  105.249 64.533 1.000 180.490 0 37  TRP EEE CB  1 ? 8  
ATOM 6229  C CG  . TRP E 3 37  ? 19.267  104.028 64.157 1.000 168.875 0 37  TRP EEE CG  1 ? 8  
ATOM 6230  C CD1 . TRP E 3 37  ? 20.615  103.868 64.054 1.000 165.471 0 37  TRP EEE CD1 1 ? 8  
ATOM 6231  C CD2 . TRP E 3 37  ? 18.689  102.736 63.950 1.000 175.557 0 37  TRP EEE CD2 1 ? 8  
ATOM 6232  N NE1 . TRP E 3 37  ? 20.909  102.565 63.725 1.000 173.914 0 37  TRP EEE NE1 1 ? 8  
ATOM 6233  C CE2 . TRP E 3 37  ? 19.742  101.849 63.665 1.000 178.383 0 37  TRP EEE CE2 1 ? 8  
ATOM 6234  C CE3 . TRP E 3 37  ? 17.378  102.249 63.953 1.000 183.705 0 37  TRP EEE CE3 1 ? 8  
ATOM 6235  C CZ2 . TRP E 3 37  ? 19.527  100.503 63.384 1.000 181.044 0 37  TRP EEE CZ2 1 ? 8  
ATOM 6236  C CZ3 . TRP E 3 37  ? 17.166  100.914 63.675 1.000 184.004 0 37  TRP EEE CZ3 1 ? 8  
ATOM 6237  C CH2 . TRP E 3 37  ? 18.234  100.056 63.394 1.000 181.820 0 37  TRP EEE CH2 1 ? 8  
ATOM 6238  N N   . ARG E 3 38  ? 16.247  106.992 63.501 1.000 200.555 0 38  ARG EEE N   1 ? 8  
ATOM 6239  C CA  . ARG E 3 38  ? 15.102  107.801 63.887 1.000 214.341 0 38  ARG EEE CA  1 ? 8  
ATOM 6240  C C   . ARG E 3 38  ? 13.917  106.907 64.226 1.000 228.142 0 38  ARG EEE C   1 ? 8  
ATOM 6241  O O   . ARG E 3 38  ? 13.797  105.793 63.708 1.000 231.650 0 38  ARG EEE O   1 ? 8  
ATOM 6242  C CB  . ARG E 3 38  ? 14.671  108.756 62.758 1.000 211.864 0 38  ARG EEE CB  1 ? 8  
ATOM 6243  C CG  . ARG E 3 38  ? 14.087  108.021 61.548 1.000 208.721 0 38  ARG EEE CG  1 ? 8  
ATOM 6244  C CD  . ARG E 3 38  ? 13.675  108.943 60.405 1.000 207.628 0 38  ARG EEE CD  1 ? 8  
ATOM 6245  N NE  . ARG E 3 38  ? 13.056  108.192 59.316 1.000 205.543 0 38  ARG EEE NE  1 ? 8  
ATOM 6246  C CZ  . ARG E 3 38  ? 12.816  108.673 58.103 1.000 209.407 0 38  ARG EEE CZ  1 ? 8  
ATOM 6247  N NH1 . ARG E 3 38  ? 13.133  109.915 57.775 1.000 216.058 0 38  ARG EEE NH1 1 ? 8  
ATOM 6248  N NH2 . ARG E 3 38  ? 12.251  107.885 57.192 1.000 205.694 0 38  ARG EEE NH2 1 ? 8  
ATOM 6249  N N   . GLN E 3 39  ? 13.039  107.397 65.108 1.000 241.622 0 39  GLN EEE N   1 ? 8  
ATOM 6250  C CA  . GLN E 3 39  ? 11.793  106.698 65.419 1.000 242.472 0 39  GLN EEE CA  1 ? 8  
ATOM 6251  C C   . GLN E 3 39  ? 10.669  107.710 65.597 1.000 248.164 0 39  GLN EEE C   1 ? 8  
ATOM 6252  O O   . GLN E 3 39  ? 10.779  108.616 66.429 1.000 242.154 0 39  GLN EEE O   1 ? 8  
ATOM 6253  C CB  . GLN E 3 39  ? 11.945  105.807 66.656 1.000 238.954 0 39  GLN EEE CB  1 ? 8  
ATOM 6254  C CG  . GLN E 3 39  ? 10.743  104.907 66.922 1.000 242.398 0 39  GLN EEE CG  1 ? 8  
ATOM 6255  C CD  . GLN E 3 39  ? 10.953  103.988 68.110 1.000 231.408 0 39  GLN EEE CD  1 ? 8  
ATOM 6256  O OE1 . GLN E 3 39  ? 11.708  104.302 69.028 1.000 222.344 0 39  GLN EEE OE1 1 ? 8  
ATOM 6257  N NE2 . GLN E 3 39  ? 10.300  102.830 68.084 1.000 233.765 0 39  GLN EEE NE2 1 ? 8  
ATOM 6258  N N   . ALA E 3 40  ? 9.610   107.554 64.859 1.000 270.655 0 40  ALA EEE N   1 ? 8  
ATOM 6259  C CA  . ALA E 3 40  ? 8.404   108.363 64.957 1.000 283.882 0 40  ALA EEE CA  1 ? 8  
ATOM 6260  C C   . ALA E 3 40  ? 7.335   107.653 65.780 1.000 296.199 0 40  ALA EEE C   1 ? 8  
ATOM 6261  O O   . ALA E 3 40  ? 7.335   106.420 65.859 1.000 312.025 0 40  ALA EEE O   1 ? 8  
ATOM 6262  C CB  . ALA E 3 40  ? 7.840   108.668 63.567 1.000 286.287 0 40  ALA EEE CB  1 ? 8  
ATOM 6263  N N   . PRO E 3 41  ? 6.432   108.381 66.441 1.000 275.218 0 41  PRO EEE N   1 ? 8  
ATOM 6264  C CA  . PRO E 3 41  ? 5.394   107.709 67.238 1.000 275.427 0 41  PRO EEE CA  1 ? 8  
ATOM 6265  C C   . PRO E 3 41  ? 4.621   106.803 66.294 1.000 279.322 0 41  PRO EEE C   1 ? 8  
ATOM 6266  O O   . PRO E 3 41  ? 4.055   107.256 65.297 1.000 285.822 0 41  PRO EEE O   1 ? 8  
ATOM 6267  C CB  . PRO E 3 41  ? 4.549   108.864 67.783 1.000 271.675 0 41  PRO EEE CB  1 ? 8  
ATOM 6268  C CG  . PRO E 3 41  ? 5.493   110.012 67.822 1.000 267.020 0 41  PRO EEE CG  1 ? 8  
ATOM 6269  C CD  . PRO E 3 41  ? 6.385   109.842 66.618 1.000 263.990 0 41  PRO EEE CD  1 ? 8  
ATOM 6270  N N   . GLY E 3 42  ? 4.591   105.515 66.619 1.000 279.217 0 42  GLY EEE N   1 ? 8  
ATOM 6271  C CA  . GLY E 3 42  ? 3.912   104.532 65.807 1.000 276.801 0 42  GLY EEE CA  1 ? 8  
ATOM 6272  C C   . GLY E 3 42  ? 4.777   103.945 64.710 1.000 270.375 0 42  GLY EEE C   1 ? 8  
ATOM 6273  O O   . GLY E 3 42  ? 4.384   102.935 64.108 1.000 257.291 0 42  GLY EEE O   1 ? 8  
ATOM 6274  N N   . LYS E 3 43  ? 5.930   104.547 64.414 1.000 274.909 0 43  LYS EEE N   1 ? 8  
ATOM 6275  C CA  . LYS E 3 43  ? 6.797   104.039 63.367 1.000 278.981 0 43  LYS EEE CA  1 ? 8  
ATOM 6276  C C   . LYS E 3 43  ? 7.929   103.312 64.082 1.000 286.123 0 43  LYS EEE C   1 ? 8  
ATOM 6277  O O   . LYS E 3 43  ? 8.316   103.689 65.194 1.000 290.997 0 43  LYS EEE O   1 ? 8  
ATOM 6278  C CB  . LYS E 3 43  ? 7.372   105.181 62.521 1.000 269.945 0 43  LYS EEE CB  1 ? 8  
ATOM 6279  C CG  . LYS E 3 43  ? 7.198   105.095 61.010 1.000 255.074 0 43  LYS EEE CG  1 ? 8  
ATOM 6280  C CD  . LYS E 3 43  ? 5.746   105.022 60.582 1.000 252.323 0 43  LYS EEE CD  1 ? 8  
ATOM 6281  C CE  . LYS E 3 43  ? 5.648   104.853 59.074 1.000 248.706 0 43  LYS EEE CE  1 ? 8  
ATOM 6282  N NZ  . LYS E 3 43  ? 4.256   105.010 58.575 1.000 262.974 0 43  LYS EEE NZ  1 ? 8  
ATOM 6283  N N   . GLU E 3 44  ? 8.461   102.269 63.455 1.000 286.658 0 44  GLU EEE N   1 ? 8  
ATOM 6284  C CA  . GLU E 3 44  ? 9.537   101.527 64.100 1.000 277.625 0 44  GLU EEE CA  1 ? 8  
ATOM 6285  C C   . GLU E 3 44  ? 10.841  102.315 63.970 1.000 277.274 0 44  GLU EEE C   1 ? 8  
ATOM 6286  O O   . GLU E 3 44  ? 10.998  103.119 63.043 1.000 290.258 0 44  GLU EEE O   1 ? 8  
ATOM 6287  C CB  . GLU E 3 44  ? 9.629   100.121 63.492 1.000 273.182 0 44  GLU EEE CB  1 ? 8  
ATOM 6288  C CG  . GLU E 3 44  ? 10.134  99.029  64.453 1.000 271.686 0 44  GLU EEE CG  1 ? 8  
ATOM 6289  C CD  . GLU E 3 44  ? 11.605  99.120  64.775 1.000 271.084 0 44  GLU EEE CD  1 ? 8  
ATOM 6290  O OE1 . GLU E 3 44  ? 12.397  99.431  63.874 1.000 278.153 0 44  GLU EEE OE1 1 ? 8  
ATOM 6291  O OE2 . GLU E 3 44  ? 11.965  98.907  65.953 1.000 268.244 0 44  GLU EEE OE2 1 ? 8  
ATOM 6292  N N   . ARG E 3 45  ? 11.758  102.132 64.927 1.000 273.904 0 45  ARG EEE N   1 ? 8  
ATOM 6293  C CA  . ARG E 3 45  ? 13.054  102.802 64.812 1.000 265.347 0 45  ARG EEE CA  1 ? 8  
ATOM 6294  C C   . ARG E 3 45  ? 13.650  102.493 63.441 1.000 262.113 0 45  ARG EEE C   1 ? 8  
ATOM 6295  O O   . ARG E 3 45  ? 13.854  101.327 63.097 1.000 268.168 0 45  ARG EEE O   1 ? 8  
ATOM 6296  C CB  . ARG E 3 45  ? 13.979  102.292 65.924 1.000 259.959 0 45  ARG EEE CB  1 ? 8  
ATOM 6297  C CG  . ARG E 3 45  ? 14.563  103.326 66.885 1.000 247.077 0 45  ARG EEE CG  1 ? 8  
ATOM 6298  C CD  . ARG E 3 45  ? 15.330  102.592 67.992 1.000 233.800 0 45  ARG EEE CD  1 ? 8  
ATOM 6299  N NE  . ARG E 3 45  ? 15.917  103.466 69.002 1.000 217.060 0 45  ARG EEE NE  1 ? 8  
ATOM 6300  C CZ  . ARG E 3 45  ? 16.554  103.034 70.083 1.000 202.199 0 45  ARG EEE CZ  1 ? 8  
ATOM 6301  N NH1 . ARG E 3 45  ? 16.690  101.741 70.334 1.000 191.419 0 45  ARG EEE NH1 1 ? 8  
ATOM 6302  N NH2 . ARG E 3 45  ? 17.054  103.918 70.941 1.000 197.861 0 45  ARG EEE NH2 1 ? 8  
ATOM 6303  N N   . GLU E 3 46  ? 13.992  103.512 62.665 1.000 237.765 0 46  GLU EEE N   1 ? 8  
ATOM 6304  C CA  . GLU E 3 46  ? 14.551  103.254 61.344 1.000 216.362 0 46  GLU EEE CA  1 ? 8  
ATOM 6305  C C   . GLU E 3 46  ? 15.977  103.786 61.248 1.000 195.496 0 46  GLU EEE C   1 ? 8  
ATOM 6306  O O   . GLU E 3 46  ? 16.294  104.842 61.805 1.000 188.760 0 46  GLU EEE O   1 ? 8  
ATOM 6307  C CB  . GLU E 3 46  ? 13.629  103.786 60.231 1.000 220.561 0 46  GLU EEE CB  1 ? 8  
ATOM 6308  C CG  . GLU E 3 46  ? 14.219  103.750 58.828 1.000 215.314 0 46  GLU EEE CG  1 ? 8  
ATOM 6309  C CD  . GLU E 3 46  ? 13.272  104.323 57.793 1.000 211.021 0 46  GLU EEE CD  1 ? 8  
ATOM 6310  O OE1 . GLU E 3 46  ? 12.052  104.347 58.064 1.000 203.804 0 46  GLU EEE OE1 1 ? 8  
ATOM 6311  O OE2 . GLU E 3 46  ? 13.734  104.715 56.702 1.000 203.245 0 46  GLU EEE OE2 1 ? 8  
ATOM 6312  N N   . PHE E 3 47  ? 16.834  103.052 60.543 1.000 182.214 0 47  PHE EEE N   1 ? 8  
ATOM 6313  C CA  . PHE E 3 47  ? 18.229  103.441 60.399 1.000 176.755 0 47  PHE EEE CA  1 ? 8  
ATOM 6314  C C   . PHE E 3 47  ? 18.351  104.508 59.321 1.000 171.601 0 47  PHE EEE C   1 ? 8  
ATOM 6315  O O   . PHE E 3 47  ? 17.756  104.384 58.247 1.000 173.493 0 47  PHE EEE O   1 ? 8  
ATOM 6316  C CB  . PHE E 3 47  ? 19.074  102.220 60.024 1.000 180.599 0 47  PHE EEE CB  1 ? 8  
ATOM 6317  C CG  . PHE E 3 47  ? 20.428  102.559 59.449 1.000 173.355 0 47  PHE EEE CG  1 ? 8  
ATOM 6318  C CD1 . PHE E 3 47  ? 21.500  102.878 60.267 1.000 168.893 0 47  PHE EEE CD1 1 ? 8  
ATOM 6319  C CD2 . PHE E 3 47  ? 20.623  102.550 58.075 1.000 168.430 0 47  PHE EEE CD2 1 ? 8  
ATOM 6320  C CE1 . PHE E 3 47  ? 22.736  103.186 59.721 1.000 158.172 0 47  PHE EEE CE1 1 ? 8  
ATOM 6321  C CE2 . PHE E 3 47  ? 21.849  102.858 57.527 1.000 165.911 0 47  PHE EEE CE2 1 ? 8  
ATOM 6322  C CZ  . PHE E 3 47  ? 22.908  103.175 58.349 1.000 161.508 0 47  PHE EEE CZ  1 ? 8  
ATOM 6323  N N   . VAL E 3 48  ? 19.115  105.563 59.608 1.000 173.478 0 48  VAL EEE N   1 ? 8  
ATOM 6324  C CA  . VAL E 3 48  ? 19.244  106.701 58.702 1.000 173.028 0 48  VAL EEE CA  1 ? 8  
ATOM 6325  C C   . VAL E 3 48  ? 20.645  106.777 58.104 1.000 172.626 0 48  VAL EEE C   1 ? 8  
ATOM 6326  O O   . VAL E 3 48  ? 20.812  106.720 56.883 1.000 166.396 0 48  VAL EEE O   1 ? 8  
ATOM 6327  C CB  . VAL E 3 48  ? 18.874  108.017 59.423 1.000 165.257 0 48  VAL EEE CB  1 ? 8  
ATOM 6328  C CG1 . VAL E 3 48  ? 19.007  109.206 58.485 1.000 177.871 0 48  VAL EEE CG1 1 ? 8  
ATOM 6329  C CG2 . VAL E 3 48  ? 17.470  107.933 59.985 1.000 180.706 0 48  VAL EEE CG2 1 ? 8  
ATOM 6330  N N   . ALA E 3 49  ? 21.669  106.895 58.948 1.000 167.295 0 49  ALA EEE N   1 ? 8  
ATOM 6331  C CA  . ALA E 3 49  ? 23.017  107.068 58.434 1.000 153.942 0 49  ALA EEE CA  1 ? 8  
ATOM 6332  C C   . ALA E 3 49  ? 24.035  106.425 59.366 1.000 148.654 0 49  ALA EEE C   1 ? 8  
ATOM 6333  O O   . ALA E 3 49  ? 23.789  106.250 60.560 1.000 157.063 0 49  ALA EEE O   1 ? 8  
ATOM 6334  C CB  . ALA E 3 49  ? 23.336  108.553 58.255 1.000 156.669 0 49  ALA EEE CB  1 ? 8  
ATOM 6335  N N   . ARG E 3 50  ? 25.189  106.079 58.801 1.000 148.547 0 50  ARG EEE N   1 ? 8  
ATOM 6336  C CA  . ARG E 3 50  ? 26.272  105.459 59.553 1.000 146.497 0 50  ARG EEE CA  1 ? 8  
ATOM 6337  C C   . ARG E 3 50  ? 27.587  105.956 58.970 1.000 151.963 0 50  ARG EEE C   1 ? 8  
ATOM 6338  O O   . ARG E 3 50  ? 27.712  106.115 57.752 1.000 163.835 0 50  ARG EEE O   1 ? 8  
ATOM 6339  C CB  . ARG E 3 50  ? 26.272  103.926 59.602 1.000 142.714 0 50  ARG EEE CB  1 ? 8  
ATOM 6340  C CG  . ARG E 3 50  ? 26.594  103.170 58.340 1.000 149.584 0 50  ARG EEE CG  1 ? 8  
ATOM 6341  C CD  . ARG E 3 50  ? 26.694  101.705 58.730 1.000 140.047 0 50  ARG EEE CD  1 ? 8  
ATOM 6342  N NE  . ARG E 3 50  ? 26.964  100.800 57.622 1.000 131.605 0 50  ARG EEE NE  1 ? 8  
ATOM 6343  C CZ  . ARG E 3 50  ? 26.036  100.090 56.997 1.000 139.779 0 50  ARG EEE CZ  1 ? 8  
ATOM 6344  N NH1 . ARG E 3 50  ? 24.759  100.174 57.334 1.000 142.078 0 50  ARG EEE NH1 1 ? 8  
ATOM 6345  N NH2 . ARG E 3 50  ? 26.400  99.263  56.022 1.000 152.743 0 50  ARG EEE NH2 1 ? 8  
ATOM 6346  N N   . ILE E 3 51  ? 28.556  106.207 59.838 1.000 145.995 0 51  ILE EEE N   1 ? 8  
ATOM 6347  C CA  . ILE E 3 51  ? 29.931  106.463 59.429 1.000 144.344 0 51  ILE EEE CA  1 ? 8  
ATOM 6348  C C   . ILE E 3 51  ? 30.810  105.617 60.341 1.000 145.842 0 51  ILE EEE C   1 ? 8  
ATOM 6349  O O   . ILE E 3 51  ? 30.791  105.785 61.566 1.000 157.554 0 51  ILE EEE O   1 ? 8  
ATOM 6350  C CB  . ILE E 3 51  ? 30.300  107.956 59.491 1.000 146.749 0 51  ILE EEE CB  1 ? 8  
ATOM 6351  C CG1 . ILE E 3 51  ? 31.813  108.143 59.334 1.000 148.341 0 51  ILE EEE CG1 1 ? 8  
ATOM 6352  C CG2 . ILE E 3 51  ? 29.725  108.603 60.742 1.000 166.887 0 51  ILE EEE CG2 1 ? 8  
ATOM 6353  C CD1 . ILE E 3 51  ? 32.313  107.900 57.916 1.000 159.331 0 51  ILE EEE CD1 1 ? 8  
ATOM 6354  N N   . VAL E 3 52  ? 31.561  104.698 59.742 1.000 139.913 0 52  VAL EEE N   1 ? 8  
ATOM 6355  C CA  . VAL E 3 52  ? 32.546  103.875 60.433 1.000 136.299 0 52  VAL EEE CA  1 ? 8  
ATOM 6356  C C   . VAL E 3 52  ? 33.949  104.351 60.083 1.000 139.776 0 52  VAL EEE C   1 ? 8  
ATOM 6357  O O   . VAL E 3 52  ? 34.221  104.749 58.944 1.000 141.361 0 52  VAL EEE O   1 ? 8  
ATOM 6358  C CB  . VAL E 3 52  ? 32.354  102.390 60.069 1.000 127.356 0 52  VAL EEE CB  1 ? 8  
ATOM 6359  C CG1 . VAL E 3 52  ? 33.320  101.506 60.846 1.000 124.346 0 52  VAL EEE CG1 1 ? 8  
ATOM 6360  C CG2 . VAL E 3 52  ? 30.906  101.979 60.297 1.000 125.824 0 52  VAL EEE CG2 1 ? 8  
ATOM 6361  N N   . LYS E 3 53  ? 34.833  104.328 61.082 1.000 144.246 0 53  LYS EEE N   1 ? 8  
ATOM 6362  C CA  . LYS E 3 53  ? 36.156  104.922 60.951 1.000 144.143 0 53  LYS EEE CA  1 ? 8  
ATOM 6363  C C   . LYS E 3 53  ? 36.938  104.294 59.811 1.000 153.503 0 53  LYS EEE C   1 ? 8  
ATOM 6364  O O   . LYS E 3 53  ? 37.110  103.073 59.755 1.000 158.433 0 53  LYS EEE O   1 ? 8  
ATOM 6365  C CB  . LYS E 3 53  ? 36.945  104.735 62.243 1.000 142.138 0 53  LYS EEE CB  1 ? 8  
ATOM 6366  C CG  . LYS E 3 53  ? 36.979  105.915 63.181 1.000 148.024 0 53  LYS EEE CG  1 ? 8  
ATOM 6367  C CD  . LYS E 3 53  ? 38.249  105.841 64.023 1.000 153.716 0 53  LYS EEE CD  1 ? 8  
ATOM 6368  C CE  . LYS E 3 53  ? 38.205  104.713 65.050 1.000 157.630 0 53  LYS EEE CE  1 ? 8  
ATOM 6369  N NZ  . LYS E 3 53  ? 39.394  104.700 65.952 1.000 159.098 0 53  LYS EEE NZ  1 ? 8  
ATOM 6370  N N   . GLY E 3 54  ? 37.398  105.145 58.896 1.000 167.477 0 54  GLY EEE N   1 ? 8  
ATOM 6371  C CA  . GLY E 3 54  ? 38.139  104.735 57.727 1.000 173.798 0 54  GLY EEE CA  1 ? 8  
ATOM 6372  C C   . GLY E 3 54  ? 37.300  104.372 56.525 1.000 173.126 0 54  GLY EEE C   1 ? 8  
ATOM 6373  O O   . GLY E 3 54  ? 37.860  104.137 55.448 1.000 179.527 0 54  GLY EEE O   1 ? 8  
ATOM 6374  N N   . PHE E 3 55  ? 35.984  104.318 56.668 1.000 158.594 0 55  PHE EEE N   1 ? 8  
ATOM 6375  C CA  . PHE E 3 55  ? 35.109  103.869 55.602 1.000 154.264 0 55  PHE EEE CA  1 ? 8  
ATOM 6376  C C   . PHE E 3 55  ? 34.291  105.047 55.089 1.000 160.773 0 55  PHE EEE C   1 ? 8  
ATOM 6377  O O   . PHE E 3 55  ? 34.180  106.084 55.746 1.000 160.416 0 55  PHE EEE O   1 ? 8  
ATOM 6378  C CB  . PHE E 3 55  ? 34.206  102.738 56.101 1.000 144.369 0 55  PHE EEE CB  1 ? 8  
ATOM 6379  C CG  . PHE E 3 55  ? 34.951  101.464 56.393 1.000 142.746 0 55  PHE EEE CG  1 ? 8  
ATOM 6380  C CD1 . PHE E 3 55  ? 35.258  100.565 55.385 1.000 153.307 0 55  PHE EEE CD1 1 ? 8  
ATOM 6381  C CD2 . PHE E 3 55  ? 35.376  101.186 57.682 1.000 147.928 0 55  PHE EEE CD2 1 ? 8  
ATOM 6382  C CE1 . PHE E 3 55  ? 35.956  99.400  55.665 1.000 159.994 0 55  PHE EEE CE1 1 ? 8  
ATOM 6383  C CE2 . PHE E 3 55  ? 36.073  100.028 57.968 1.000 151.140 0 55  PHE EEE CE2 1 ? 8  
ATOM 6384  C CZ  . PHE E 3 55  ? 36.368  99.136  56.956 1.000 156.169 0 55  PHE EEE CZ  1 ? 8  
ATOM 6385  N N   . ASP E 3 56  ? 33.720  104.881 53.902 1.000 162.601 0 56  ASP EEE N   1 ? 8  
ATOM 6386  C CA  . ASP E 3 56  ? 32.851  105.907 53.368 1.000 162.376 0 56  ASP EEE CA  1 ? 8  
ATOM 6387  C C   . ASP E 3 56  ? 31.541  105.945 54.149 1.000 158.304 0 56  ASP EEE C   1 ? 8  
ATOM 6388  O O   . ASP E 3 56  ? 31.134  104.948 54.752 1.000 162.333 0 56  ASP EEE O   1 ? 8  
ATOM 6389  C CB  . ASP E 3 56  ? 32.601  105.677 51.883 1.000 172.522 0 56  ASP EEE CB  1 ? 8  
ATOM 6390  C CG  . ASP E 3 56  ? 33.727  106.218 51.022 1.000 183.249 0 56  ASP EEE CG  1 ? 8  
ATOM 6391  O OD1 . ASP E 3 56  ? 34.817  106.493 51.571 1.000 177.098 0 56  ASP EEE OD1 1 ? 8  
ATOM 6392  O OD2 . ASP E 3 56  ? 33.521  106.370 49.800 1.000 200.248 0 56  ASP EEE OD2 1 ? 8  
ATOM 6393  N N   . PRO E 3 57  ? 30.854  107.086 54.144 1.000 160.640 0 57  PRO EEE N   1 ? 8  
ATOM 6394  C CA  . PRO E 3 57  ? 29.530  107.139 54.777 1.000 160.421 0 57  PRO EEE CA  1 ? 8  
ATOM 6395  C C   . PRO E 3 57  ? 28.518  106.321 53.994 1.000 161.617 0 57  PRO EEE C   1 ? 8  
ATOM 6396  O O   . PRO E 3 57  ? 28.491  106.344 52.763 1.000 171.418 0 57  PRO EEE O   1 ? 8  
ATOM 6397  C CB  . PRO E 3 57  ? 29.184  108.629 54.740 1.000 162.315 0 57  PRO EEE CB  1 ? 8  
ATOM 6398  C CG  . PRO E 3 57  ? 30.498  109.322 54.706 1.000 162.217 0 57  PRO EEE CG  1 ? 8  
ATOM 6399  C CD  . PRO E 3 57  ? 31.398  108.431 53.889 1.000 159.532 0 57  PRO EEE CD  1 ? 8  
ATOM 6400  N N   . VAL E 3 58  ? 27.686  105.591 54.728 1.000 149.006 0 58  VAL EEE N   1 ? 8  
ATOM 6401  C CA  . VAL E 3 58  ? 26.571  104.842 54.166 1.000 155.106 0 58  VAL EEE CA  1 ? 8  
ATOM 6402  C C   . VAL E 3 58  ? 25.262  105.440 54.655 1.000 158.598 0 58  VAL EEE C   1 ? 8  
ATOM 6403  O O   . VAL E 3 58  ? 25.117  105.744 55.843 1.000 168.441 0 58  VAL EEE O   1 ? 8  
ATOM 6404  C CB  . VAL E 3 58  ? 26.655  103.353 54.546 1.000 155.830 0 58  VAL EEE CB  1 ? 8  
ATOM 6405  C CG1 . VAL E 3 58  ? 25.438  102.596 54.016 1.000 160.739 0 58  VAL EEE CG1 1 ? 8  
ATOM 6406  C CG2 . VAL E 3 58  ? 27.937  102.744 53.996 1.000 162.594 0 58  VAL EEE CG2 1 ? 8  
ATOM 6407  N N   . LEU E 3 59  ? 24.310  105.617 53.737 1.000 159.127 0 59  LEU EEE N   1 ? 8  
ATOM 6408  C CA  . LEU E 3 59  ? 23.019  106.208 54.065 1.000 163.422 0 59  LEU EEE CA  1 ? 8  
ATOM 6409  C C   . LEU E 3 59  ? 21.921  105.250 53.638 1.000 171.180 0 59  LEU EEE C   1 ? 8  
ATOM 6410  O O   . LEU E 3 59  ? 22.118  104.436 52.734 1.000 177.360 0 59  LEU EEE O   1 ? 8  
ATOM 6411  C CB  . LEU E 3 59  ? 22.809  107.539 53.334 1.000 165.178 0 59  LEU EEE CB  1 ? 8  
ATOM 6412  C CG  . LEU E 3 59  ? 23.715  108.727 53.642 1.000 165.639 0 59  LEU EEE CG  1 ? 8  
ATOM 6413  C CD1 . LEU E 3 59  ? 23.688  109.765 52.493 1.000 175.165 0 59  LEU EEE CD1 1 ? 8  
ATOM 6414  C CD2 . LEU E 3 59  ? 23.233  109.354 54.915 1.000 175.841 0 59  LEU EEE CD2 1 ? 8  
ATOM 6415  N N   . ALA E 3 60  ? 20.773  105.319 54.308 1.000 178.069 0 60  ALA EEE N   1 ? 8  
ATOM 6416  C CA  . ALA E 3 60  ? 19.656  104.492 53.894 1.000 187.221 0 60  ALA EEE CA  1 ? 8  
ATOM 6417  C C   . ALA E 3 60  ? 19.104  104.944 52.542 1.000 211.511 0 60  ALA EEE C   1 ? 8  
ATOM 6418  O O   . ALA E 3 60  ? 19.289  106.084 52.106 1.000 237.456 0 60  ALA EEE O   1 ? 8  
ATOM 6419  C CB  . ALA E 3 60  ? 18.540  104.526 54.942 1.000 177.796 0 60  ALA EEE CB  1 ? 8  
ATOM 6420  N N   . ASP E 3 61  ? 18.423  104.016 51.868 1.000 213.813 0 61  ASP EEE N   1 ? 8  
ATOM 6421  C CA  . ASP E 3 61  ? 17.884  104.288 50.539 1.000 220.280 0 61  ASP EEE CA  1 ? 8  
ATOM 6422  C C   . ASP E 3 61  ? 16.731  105.285 50.584 1.000 230.263 0 61  ASP EEE C   1 ? 8  
ATOM 6423  O O   . ASP E 3 61  ? 16.558  106.074 49.646 1.000 239.220 0 61  ASP EEE O   1 ? 8  
ATOM 6424  C CB  . ASP E 3 61  ? 17.481  102.993 49.839 1.000 222.151 0 61  ASP EEE CB  1 ? 8  
ATOM 6425  C CG  . ASP E 3 61  ? 18.682  102.136 49.463 1.000 224.484 0 61  ASP EEE CG  1 ? 8  
ATOM 6426  O OD1 . ASP E 3 61  ? 19.820  102.482 49.856 1.000 220.079 0 61  ASP EEE OD1 1 ? 8  
ATOM 6427  O OD2 . ASP E 3 61  ? 18.494  101.138 48.737 1.000 235.578 0 61  ASP EEE OD2 1 ? 8  
ATOM 6428  N N   . SER E 3 62  ? 15.940  105.270 51.660 1.000 233.644 0 62  SER EEE N   1 ? 8  
ATOM 6429  C CA  . SER E 3 62  ? 14.807  106.179 51.779 1.000 224.806 0 62  SER EEE CA  1 ? 8  
ATOM 6430  C C   . SER E 3 62  ? 15.216  107.635 51.963 1.000 220.428 0 62  SER EEE C   1 ? 8  
ATOM 6431  O O   . SER E 3 62  ? 14.335  108.501 51.995 1.000 232.410 0 62  SER EEE O   1 ? 8  
ATOM 6432  C CB  . SER E 3 62  ? 13.927  105.748 52.956 1.000 220.501 0 62  SER EEE CB  1 ? 8  
ATOM 6433  O OG  . SER E 3 62  ? 13.623  104.365 52.897 1.000 224.385 0 62  SER EEE OG  1 ? 8  
ATOM 6434  N N   . VAL E 3 63  ? 16.510  107.923 52.113 1.000 218.161 0 63  VAL EEE N   1 ? 8  
ATOM 6435  C CA  . VAL E 3 63  ? 16.977  109.269 52.424 1.000 216.690 0 63  VAL EEE CA  1 ? 8  
ATOM 6436  C C   . VAL E 3 63  ? 18.127  109.569 51.471 1.000 216.705 0 63  VAL EEE C   1 ? 8  
ATOM 6437  O O   . VAL E 3 63  ? 18.638  110.695 51.419 1.000 216.731 0 63  VAL EEE O   1 ? 8  
ATOM 6438  C CB  . VAL E 3 63  ? 17.424  109.394 53.892 1.000 209.882 0 63  VAL EEE CB  1 ? 8  
ATOM 6439  C CG1 . VAL E 3 63  ? 16.273  109.049 54.829 1.000 214.122 0 63  VAL EEE CG1 1 ? 8  
ATOM 6440  C CG2 . VAL E 3 63  ? 18.665  108.535 54.168 1.000 203.250 0 63  VAL EEE CG2 1 ? 8  
ATOM 6441  N N   . LYS E 3 64  ? 18.546  108.532 50.735 1.000 201.902 0 64  LYS EEE N   1 ? 8  
ATOM 6442  C CA  . LYS E 3 64  ? 19.805  108.557 49.995 1.000 199.777 0 64  LYS EEE CA  1 ? 8  
ATOM 6443  C C   . LYS E 3 64  ? 19.890  109.724 49.019 1.000 202.638 0 64  LYS EEE C   1 ? 8  
ATOM 6444  O O   . LYS E 3 64  ? 20.931  110.384 48.917 1.000 201.245 0 64  LYS EEE O   1 ? 8  
ATOM 6445  C CB  . LYS E 3 64  ? 19.984  107.229 49.256 1.000 197.490 0 64  LYS EEE CB  1 ? 8  
ATOM 6446  C CG  . LYS E 3 64  ? 21.238  107.122 48.414 1.000 189.555 0 64  LYS EEE CG  1 ? 8  
ATOM 6447  C CD  . LYS E 3 64  ? 21.211  105.862 47.559 1.000 195.495 0 64  LYS EEE CD  1 ? 8  
ATOM 6448  C CE  . LYS E 3 64  ? 19.972  105.785 46.686 1.000 203.130 0 64  LYS EEE CE  1 ? 8  
ATOM 6449  N NZ  . LYS E 3 64  ? 19.983  104.591 45.807 1.000 202.225 0 64  LYS EEE NZ  1 ? 8  
ATOM 6450  N N   . GLY E 3 65  ? 18.809  109.996 48.286 1.000 208.616 0 65  GLY EEE N   1 ? 8  
ATOM 6451  C CA  . GLY E 3 65  ? 18.869  111.087 47.330 1.000 212.887 0 65  GLY EEE CA  1 ? 8  
ATOM 6452  C C   . GLY E 3 65  ? 18.832  112.465 47.953 1.000 216.446 0 65  GLY EEE C   1 ? 8  
ATOM 6453  O O   . GLY E 3 65  ? 19.271  113.431 47.323 1.000 214.159 0 65  GLY EEE O   1 ? 8  
ATOM 6454  N N   . ARG E 3 66  ? 18.321  112.572 49.176 1.000 217.124 0 66  ARG EEE N   1 ? 8  
ATOM 6455  C CA  . ARG E 3 66  ? 17.973  113.847 49.784 1.000 219.302 0 66  ARG EEE CA  1 ? 8  
ATOM 6456  C C   . ARG E 3 66  ? 18.816  114.212 50.996 1.000 218.458 0 66  ARG EEE C   1 ? 8  
ATOM 6457  O O   . ARG E 3 66  ? 19.025  115.402 51.244 1.000 226.655 0 66  ARG EEE O   1 ? 8  
ATOM 6458  C CB  . ARG E 3 66  ? 16.484  113.867 50.141 1.000 225.213 0 66  ARG EEE CB  1 ? 8  
ATOM 6459  C CG  . ARG E 3 66  ? 15.637  113.348 48.991 1.000 226.973 0 66  ARG EEE CG  1 ? 8  
ATOM 6460  C CD  . ARG E 3 66  ? 14.202  113.117 49.397 1.000 233.946 0 66  ARG EEE CD  1 ? 8  
ATOM 6461  N NE  . ARG E 3 66  ? 14.088  112.091 50.425 1.000 230.773 0 66  ARG EEE NE  1 ? 8  
ATOM 6462  C CZ  . ARG E 3 66  ? 13.590  112.302 51.634 1.000 239.059 0 66  ARG EEE CZ  1 ? 8  
ATOM 6463  N NH1 . ARG E 3 66  ? 13.145  113.494 51.999 1.000 251.616 0 66  ARG EEE NH1 1 ? 8  
ATOM 6464  N NH2 . ARG E 3 66  ? 13.545  111.296 52.503 1.000 236.067 0 66  ARG EEE NH2 1 ? 8  
ATOM 6465  N N   . PHE E 3 67  ? 19.314  113.234 51.745 1.000 212.296 0 67  PHE EEE N   1 ? 8  
ATOM 6466  C CA  . PHE E 3 67  ? 20.089  113.508 52.943 1.000 208.553 0 67  PHE EEE CA  1 ? 8  
ATOM 6467  C C   . PHE E 3 67  ? 21.574  113.318 52.661 1.000 200.543 0 67  PHE EEE C   1 ? 8  
ATOM 6468  O O   . PHE E 3 67  ? 21.975  112.586 51.757 1.000 199.934 0 67  PHE EEE O   1 ? 8  
ATOM 6469  C CB  . PHE E 3 67  ? 19.682  112.603 54.120 1.000 206.493 0 67  PHE EEE CB  1 ? 8  
ATOM 6470  C CG  . PHE E 3 67  ? 18.288  112.845 54.653 1.000 217.276 0 67  PHE EEE CG  1 ? 8  
ATOM 6471  C CD1 . PHE E 3 67  ? 17.413  113.712 54.018 1.000 231.892 0 67  PHE EEE CD1 1 ? 8  
ATOM 6472  C CD2 . PHE E 3 67  ? 17.875  112.229 55.826 1.000 215.350 0 67  PHE EEE CD2 1 ? 8  
ATOM 6473  C CE1 . PHE E 3 67  ? 16.142  113.927 54.518 1.000 233.951 0 67  PHE EEE CE1 1 ? 8  
ATOM 6474  C CE2 . PHE E 3 67  ? 16.610  112.445 56.336 1.000 223.370 0 67  PHE EEE CE2 1 ? 8  
ATOM 6475  C CZ  . PHE E 3 67  ? 15.743  113.299 55.683 1.000 232.972 0 67  PHE EEE CZ  1 ? 8  
ATOM 6476  N N   . THR E 3 68  ? 22.389  114.002 53.462 1.000 201.655 0 68  THR EEE N   1 ? 8  
ATOM 6477  C CA  . THR E 3 68  ? 23.832  113.845 53.434 1.000 197.970 0 68  THR EEE CA  1 ? 8  
ATOM 6478  C C   . THR E 3 68  ? 24.339  113.835 54.866 1.000 202.701 0 68  THR EEE C   1 ? 8  
ATOM 6479  O O   . THR E 3 68  ? 23.833  114.575 55.714 1.000 205.713 0 68  THR EEE O   1 ? 8  
ATOM 6480  C CB  . THR E 3 68  ? 24.505  114.976 52.644 1.000 195.528 0 68  THR EEE CB  1 ? 8  
ATOM 6481  O OG1 . THR E 3 68  ? 23.805  115.189 51.411 1.000 201.923 0 68  THR EEE OG1 1 ? 8  
ATOM 6482  C CG2 . THR E 3 68  ? 25.953  114.626 52.341 1.000 191.335 0 68  THR EEE CG2 1 ? 8  
ATOM 6483  N N   . ILE E 3 69  ? 25.345  113.003 55.131 1.000 202.121 0 69  ILE EEE N   1 ? 8  
ATOM 6484  C CA  . ILE E 3 69  ? 25.965  112.906 56.447 1.000 190.383 0 69  ILE EEE CA  1 ? 8  
ATOM 6485  C C   . ILE E 3 69  ? 27.431  113.294 56.349 1.000 183.098 0 69  ILE EEE C   1 ? 8  
ATOM 6486  O O   . ILE E 3 69  ? 28.139  112.856 55.434 1.000 184.496 0 69  ILE EEE O   1 ? 8  
ATOM 6487  C CB  . ILE E 3 69  ? 25.834  111.485 57.032 1.000 181.521 0 69  ILE EEE CB  1 ? 8  
ATOM 6488  C CG1 . ILE E 3 69  ? 26.579  111.383 58.365 1.000 172.839 0 69  ILE EEE CG1 1 ? 8  
ATOM 6489  C CG2 . ILE E 3 69  ? 26.355  110.438 56.058 1.000 181.928 0 69  ILE EEE CG2 1 ? 8  
ATOM 6490  C CD1 . ILE E 3 69  ? 26.310  110.106 59.130 1.000 165.648 0 69  ILE EEE CD1 1 ? 8  
ATOM 6491  N N   . SER E 3 70  ? 27.879  114.132 57.280 1.000 177.440 0 70  SER EEE N   1 ? 8  
ATOM 6492  C CA  . SER E 3 70  ? 29.253  114.596 57.290 1.000 184.508 0 70  SER EEE CA  1 ? 8  
ATOM 6493  C C   . SER E 3 70  ? 29.712  114.661 58.737 1.000 185.409 0 70  SER EEE C   1 ? 8  
ATOM 6494  O O   . SER E 3 70  ? 28.898  114.696 59.664 1.000 191.990 0 70  SER EEE O   1 ? 8  
ATOM 6495  C CB  . SER E 3 70  ? 29.398  115.968 56.613 1.000 192.889 0 70  SER EEE CB  1 ? 8  
ATOM 6496  O OG  . SER E 3 70  ? 28.724  116.004 55.367 1.000 199.955 0 70  SER EEE OG  1 ? 8  
ATOM 6497  N N   . ILE E 3 71  ? 31.027  114.678 58.928 1.000 186.506 0 71  ILE EEE N   1 ? 8  
ATOM 6498  C CA  . ILE E 3 71  ? 31.620  114.768 60.256 1.000 192.050 0 71  ILE EEE CA  1 ? 8  
ATOM 6499  C C   . ILE E 3 71  ? 32.619  115.909 60.278 1.000 204.829 0 71  ILE EEE C   1 ? 8  
ATOM 6500  O O   . ILE E 3 71  ? 33.476  116.009 59.393 1.000 201.148 0 71  ILE EEE O   1 ? 8  
ATOM 6501  C CB  . ILE E 3 71  ? 32.293  113.458 60.707 1.000 188.884 0 71  ILE EEE CB  1 ? 8  
ATOM 6502  C CG1 . ILE E 3 71  ? 31.239  112.379 60.947 1.000 191.443 0 71  ILE EEE CG1 1 ? 8  
ATOM 6503  C CG2 . ILE E 3 71  ? 33.136  113.690 61.961 1.000 188.033 0 71  ILE EEE CG2 1 ? 8  
ATOM 6504  C CD1 . ILE E 3 71  ? 31.722  111.267 61.848 1.000 199.564 0 71  ILE EEE CD1 1 ? 8  
ATOM 6505  N N   . ASP E 3 72  ? 32.504  116.764 61.281 1.000 218.444 0 72  ASP EEE N   1 ? 8  
ATOM 6506  C CA  . ASP E 3 72  ? 33.414  117.878 61.482 1.000 219.818 0 72  ASP EEE CA  1 ? 8  
ATOM 6507  C C   . ASP E 3 72  ? 34.147  117.552 62.778 1.000 224.735 0 72  ASP EEE C   1 ? 8  
ATOM 6508  O O   . ASP E 3 72  ? 33.577  117.680 63.867 1.000 219.777 0 72  ASP EEE O   1 ? 8  
ATOM 6509  C CB  . ASP E 3 72  ? 32.680  119.215 61.557 1.000 212.807 0 72  ASP EEE CB  1 ? 8  
ATOM 6510  C CG  . ASP E 3 72  ? 33.628  120.395 61.677 1.000 217.244 0 72  ASP EEE CG  1 ? 8  
ATOM 6511  O OD1 . ASP E 3 72  ? 34.855  120.188 61.570 1.000 221.775 0 72  ASP EEE OD1 1 ? 8  
ATOM 6512  O OD2 . ASP E 3 72  ? 33.148  121.530 61.877 1.000 217.789 0 72  ASP EEE OD2 1 ? 8  
ATOM 6513  N N   . SER E 3 73  ? 35.408  117.130 62.662 1.000 224.304 0 73  SER EEE N   1 ? 8  
ATOM 6514  C CA  . SER E 3 73  ? 36.182  116.792 63.850 1.000 227.365 0 73  SER EEE CA  1 ? 8  
ATOM 6515  C C   . SER E 3 73  ? 36.567  118.048 64.609 1.000 233.296 0 73  SER EEE C   1 ? 8  
ATOM 6516  O O   . SER E 3 73  ? 36.875  117.981 65.803 1.000 237.474 0 73  SER EEE O   1 ? 8  
ATOM 6517  C CB  . SER E 3 73  ? 37.426  115.993 63.461 1.000 227.003 0 73  SER EEE CB  1 ? 8  
ATOM 6518  O OG  . SER E 3 73  ? 38.249  116.740 62.582 1.000 231.341 0 73  SER EEE OG  1 ? 8  
ATOM 6519  N N   . ALA E 3 74  ? 36.568  119.184 63.918 1.000 237.704 0 74  ALA EEE N   1 ? 8  
ATOM 6520  C CA  . ALA E 3 74  ? 36.863  120.472 64.530 1.000 242.940 0 74  ALA EEE CA  1 ? 8  
ATOM 6521  C C   . ALA E 3 74  ? 35.821  120.820 65.589 1.000 250.483 0 74  ALA EEE C   1 ? 8  
ATOM 6522  O O   . ALA E 3 74  ? 36.163  121.191 66.718 1.000 258.532 0 74  ALA EEE O   1 ? 8  
ATOM 6523  C CB  . ALA E 3 74  ? 36.944  121.561 63.460 1.000 242.704 0 74  ALA EEE CB  1 ? 8  
ATOM 6524  N N   . GLU E 3 75  ? 34.537  120.690 65.245 1.000 249.858 0 75  GLU EEE N   1 ? 8  
ATOM 6525  C CA  . GLU E 3 75  ? 33.444  120.982 66.165 1.000 251.308 0 75  GLU EEE CA  1 ? 8  
ATOM 6526  C C   . GLU E 3 75  ? 33.003  119.794 67.012 1.000 246.285 0 75  GLU EEE C   1 ? 8  
ATOM 6527  O O   . GLU E 3 75  ? 32.083  119.945 67.822 1.000 245.747 0 75  GLU EEE O   1 ? 8  
ATOM 6528  C CB  . GLU E 3 75  ? 32.229  121.415 65.325 1.000 241.863 0 75  GLU EEE CB  1 ? 8  
ATOM 6529  C CG  . GLU E 3 75  ? 32.015  122.893 65.088 1.000 237.357 0 75  GLU EEE CG  1 ? 8  
ATOM 6530  C CD  . GLU E 3 75  ? 31.679  123.641 66.350 1.000 239.455 0 75  GLU EEE CD  1 ? 8  
ATOM 6531  O OE1 . GLU E 3 75  ? 31.072  123.029 67.254 1.000 245.682 0 75  GLU EEE OE1 1 ? 8  
ATOM 6532  O OE2 . GLU E 3 75  ? 31.997  124.845 66.427 1.000 234.858 0 75  GLU EEE OE2 1 ? 8  
ATOM 6533  N N   . ASN E 3 76  ? 33.617  118.622 66.841 1.000 234.812 0 76  ASN EEE N   1 ? 8  
ATOM 6534  C CA  . ASN E 3 76  ? 33.261  117.420 67.600 1.000 226.033 0 76  ASN EEE CA  1 ? 8  
ATOM 6535  C C   . ASN E 3 76  ? 31.780  117.093 67.444 1.000 226.980 0 76  ASN EEE C   1 ? 8  
ATOM 6536  O O   . ASN E 3 76  ? 31.092  116.753 68.412 1.000 215.530 0 76  ASN EEE O   1 ? 8  
ATOM 6537  C CB  . ASN E 3 76  ? 33.637  117.553 69.076 1.000 222.380 0 76  ASN EEE CB  1 ? 8  
ATOM 6538  C CG  . ASN E 3 76  ? 35.127  117.495 69.303 1.000 225.297 0 76  ASN EEE CG  1 ? 8  
ATOM 6539  O OD1 . ASN E 3 76  ? 35.918  117.814 68.417 1.000 226.951 0 76  ASN EEE OD1 1 ? 8  
ATOM 6540  N ND2 . ASN E 3 76  ? 35.521  117.103 70.505 1.000 225.720 0 76  ASN EEE ND2 1 ? 8  
ATOM 6541  N N   . THR E 3 77  ? 31.288  117.181 66.219 1.000 239.056 0 77  THR EEE N   1 ? 8  
ATOM 6542  C CA  . THR E 3 77  ? 29.868  117.031 65.955 1.000 233.863 0 77  THR EEE CA  1 ? 8  
ATOM 6543  C C   . THR E 3 77  ? 29.644  116.084 64.787 1.000 225.032 0 77  THR EEE C   1 ? 8  
ATOM 6544  O O   . THR E 3 77  ? 30.508  115.922 63.921 1.000 207.648 0 77  THR EEE O   1 ? 8  
ATOM 6545  C CB  . THR E 3 77  ? 29.190  118.381 65.678 1.000 227.012 0 77  THR EEE CB  1 ? 8  
ATOM 6546  O OG1 . THR E 3 77  ? 27.769  118.214 65.734 1.000 216.781 0 77  THR EEE OG1 1 ? 8  
ATOM 6547  C CG2 . THR E 3 77  ? 29.571  118.906 64.305 1.000 222.119 0 77  THR EEE CG2 1 ? 8  
ATOM 6548  N N   . LEU E 3 78  ? 28.482  115.447 64.775 1.000 219.396 0 78  LEU EEE N   1 ? 8  
ATOM 6549  C CA  . LEU E 3 78  ? 28.114  114.555 63.689 1.000 211.150 0 78  LEU EEE CA  1 ? 8  
ATOM 6550  C C   . LEU E 3 78  ? 26.931  115.229 63.021 1.000 208.297 0 78  LEU EEE C   1 ? 8  
ATOM 6551  O O   . LEU E 3 78  ? 25.873  115.388 63.639 1.000 220.953 0 78  LEU EEE O   1 ? 8  
ATOM 6552  C CB  . LEU E 3 78  ? 27.727  113.158 64.175 1.000 206.710 0 78  LEU EEE CB  1 ? 8  
ATOM 6553  C CG  . LEU E 3 78  ? 27.836  112.021 63.145 1.000 199.440 0 78  LEU EEE CG  1 ? 8  
ATOM 6554  C CD1 . LEU E 3 78  ? 27.536  110.696 63.804 1.000 196.327 0 78  LEU EEE CD1 1 ? 8  
ATOM 6555  C CD2 . LEU E 3 78  ? 26.957  112.211 61.917 1.000 199.218 0 78  LEU EEE CD2 1 ? 8  
ATOM 6556  N N   . ALA E 3 79  ? 27.101  115.607 61.764 1.000 202.890 0 79  ALA EEE N   1 ? 8  
ATOM 6557  C CA  . ALA E 3 79  ? 26.095  116.389 61.071 1.000 204.881 0 79  ALA EEE CA  1 ? 8  
ATOM 6558  C C   . ALA E 3 79  ? 25.352  115.491 60.100 1.000 207.821 0 79  ALA EEE C   1 ? 8  
ATOM 6559  O O   . ALA E 3 79  ? 25.961  114.672 59.406 1.000 214.358 0 79  ALA EEE O   1 ? 8  
ATOM 6560  C CB  . ALA E 3 79  ? 26.728  117.569 60.330 1.000 203.798 0 79  ALA EEE CB  1 ? 8  
ATOM 6561  N N   . LEU E 3 80  ? 24.037  115.653 60.049 1.000 212.092 0 80  LEU EEE N   1 ? 8  
ATOM 6562  C CA  . LEU E 3 80  ? 23.222  115.044 59.008 1.000 219.294 0 80  LEU EEE CA  1 ? 8  
ATOM 6563  C C   . LEU E 3 80  ? 22.486  116.191 58.336 1.000 233.312 0 80  LEU EEE C   1 ? 8  
ATOM 6564  O O   . LEU E 3 80  ? 21.570  116.776 58.924 1.000 248.579 0 80  LEU EEE O   1 ? 8  
ATOM 6565  C CB  . LEU E 3 80  ? 22.265  114.009 59.600 1.000 217.287 0 80  LEU EEE CB  1 ? 8  
ATOM 6566  C CG  . LEU E 3 80  ? 21.251  113.310 58.695 1.000 219.587 0 80  LEU EEE CG  1 ? 8  
ATOM 6567  C CD1 . LEU E 3 80  ? 21.918  112.170 57.948 1.000 218.501 0 80  LEU EEE CD1 1 ? 8  
ATOM 6568  C CD2 . LEU E 3 80  ? 20.090  112.785 59.524 1.000 216.779 0 80  LEU EEE CD2 1 ? 8  
ATOM 6569  N N   . GLN E 3 81  ? 22.883  116.510 57.108 1.000 231.411 0 81  GLN EEE N   1 ? 8  
ATOM 6570  C CA  . GLN E 3 81  ? 22.238  117.568 56.346 1.000 232.732 0 81  GLN EEE CA  1 ? 8  
ATOM 6571  C C   . GLN E 3 81  ? 21.107  116.967 55.527 1.000 237.412 0 81  GLN EEE C   1 ? 8  
ATOM 6572  O O   . GLN E 3 81  ? 21.334  116.080 54.697 1.000 237.660 0 81  GLN EEE O   1 ? 8  
ATOM 6573  C CB  . GLN E 3 81  ? 23.235  118.300 55.450 1.000 230.948 0 81  GLN EEE CB  1 ? 8  
ATOM 6574  C CG  . GLN E 3 81  ? 22.580  119.359 54.580 1.000 230.849 0 81  GLN EEE CG  1 ? 8  
ATOM 6575  C CD  . GLN E 3 81  ? 22.319  120.648 55.339 1.000 226.636 0 81  GLN EEE CD  1 ? 8  
ATOM 6576  O OE1 . GLN E 3 81  ? 23.179  121.137 56.071 1.000 216.635 0 81  GLN EEE OE1 1 ? 8  
ATOM 6577  N NE2 . GLN E 3 81  ? 21.121  121.199 55.175 1.000 239.896 0 81  GLN EEE NE2 1 ? 8  
ATOM 6578  N N   . MET E 3 82  ? 19.894  117.455 55.760 1.000 245.863 0 82  MET EEE N   1 ? 8  
ATOM 6579  C CA  . MET E 3 82  ? 18.689  116.922 55.139 1.000 252.804 0 82  MET EEE CA  1 ? 8  
ATOM 6580  C C   . MET E 3 82  ? 18.014  118.033 54.345 1.000 264.764 0 82  MET EEE C   1 ? 8  
ATOM 6581  O O   . MET E 3 82  ? 17.498  118.994 54.927 1.000 286.040 0 82  MET EEE O   1 ? 8  
ATOM 6582  C CB  . MET E 3 82  ? 17.754  116.337 56.196 1.000 245.787 0 82  MET EEE CB  1 ? 8  
ATOM 6583  C CG  . MET E 3 82  ? 18.464  115.721 57.396 1.000 236.363 0 82  MET EEE CG  1 ? 8  
ATOM 6584  S SD  . MET E 3 82  ? 17.333  115.304 58.738 1.000 233.260 0 82  MET EEE SD  1 ? 8  
ATOM 6585  C CE  . MET E 3 82  ? 16.645  116.914 59.108 1.000 245.295 0 82  MET EEE CE  1 ? 8  
ATOM 6586  N N   . ASN E 3 83  A 18.033  117.906 53.022 1.000 254.004 0 82  ASN EEE N   1 ? 8  
ATOM 6587  C CA  . ASN E 3 83  A 17.359  118.816 52.111 1.000 251.986 0 82  ASN EEE CA  1 ? 8  
ATOM 6588  C C   . ASN E 3 83  A 16.128  118.133 51.532 1.000 255.383 0 82  ASN EEE C   1 ? 8  
ATOM 6589  O O   . ASN E 3 83  A 15.992  116.907 51.580 1.000 258.268 0 82  ASN EEE O   1 ? 8  
ATOM 6590  C CB  . ASN E 3 83  A 18.293  119.282 50.988 1.000 242.023 0 82  ASN EEE CB  1 ? 8  
ATOM 6591  C CG  . ASN E 3 83  A 19.507  120.022 51.512 1.000 234.111 0 82  ASN EEE CG  1 ? 8  
ATOM 6592  O OD1 . ASN E 3 83  A 20.136  119.596 52.478 1.000 231.852 0 82  ASN EEE OD1 1 ? 8  
ATOM 6593  N ND2 . ASN E 3 83  A 19.834  121.146 50.884 1.000 226.386 0 82  ASN EEE ND2 1 ? 8  
ATOM 6594  N N   . ARG E 3 84  B 15.228  118.949 50.983 1.000 259.691 0 82  ARG EEE N   1 ? 8  
ATOM 6595  C CA  . ARG E 3 84  B 13.989  118.465 50.378 1.000 263.362 0 82  ARG EEE CA  1 ? 8  
ATOM 6596  C C   . ARG E 3 84  B 13.184  117.637 51.377 1.000 260.205 0 82  ARG EEE C   1 ? 8  
ATOM 6597  O O   . ARG E 3 84  B 12.729  116.531 51.070 1.000 250.089 0 82  ARG EEE O   1 ? 8  
ATOM 6598  C CB  . ARG E 3 84  B 14.263  117.646 49.112 1.000 257.564 0 82  ARG EEE CB  1 ? 8  
ATOM 6599  C CG  . ARG E 3 84  B 15.065  118.340 48.033 1.000 251.318 0 82  ARG EEE CG  1 ? 8  
ATOM 6600  C CD  . ARG E 3 84  B 16.463  117.756 47.974 1.000 242.142 0 82  ARG EEE CD  1 ? 8  
ATOM 6601  N NE  . ARG E 3 84  B 17.063  117.914 46.657 1.000 240.460 0 82  ARG EEE NE  1 ? 8  
ATOM 6602  C CZ  . ARG E 3 84  B 16.975  117.015 45.682 1.000 243.548 0 82  ARG EEE CZ  1 ? 8  
ATOM 6603  N NH1 . ARG E 3 84  B 16.317  115.880 45.861 1.000 239.516 0 82  ARG EEE NH1 1 ? 8  
ATOM 6604  N NH2 . ARG E 3 84  B 17.549  117.265 44.516 1.000 249.280 0 82  ARG EEE NH2 1 ? 8  
ATOM 6605  N N   . LEU E 3 85  C 13.022  118.168 52.587 1.000 271.830 0 82  LEU EEE N   1 ? 8  
ATOM 6606  C CA  . LEU E 3 85  C 12.412  117.378 53.645 1.000 264.824 0 82  LEU EEE CA  1 ? 8  
ATOM 6607  C C   . LEU E 3 85  C 10.951  117.131 53.295 1.000 279.278 0 82  LEU EEE C   1 ? 8  
ATOM 6608  O O   . LEU E 3 85  C 10.276  117.995 52.728 1.000 297.050 0 82  LEU EEE O   1 ? 8  
ATOM 6609  C CB  . LEU E 3 85  C 12.528  118.113 54.981 1.000 253.262 0 82  LEU EEE CB  1 ? 8  
ATOM 6610  C CG  . LEU E 3 85  C 13.896  118.101 55.657 1.000 243.449 0 82  LEU EEE CG  1 ? 8  
ATOM 6611  C CD1 . LEU E 3 85  C 13.899  119.009 56.876 1.000 239.463 0 82  LEU EEE CD1 1 ? 8  
ATOM 6612  C CD2 . LEU E 3 85  C 14.235  116.685 56.047 1.000 238.725 0 82  LEU EEE CD2 1 ? 8  
ATOM 6613  N N   . LYS E 3 86  ? 10.461  115.953 53.647 1.000 267.201 0 83  LYS EEE N   1 ? 8  
ATOM 6614  C CA  . LYS E 3 86  ? 9.095   115.574 53.345 1.000 269.205 0 83  LYS EEE CA  1 ? 8  
ATOM 6615  C C   . LYS E 3 86  ? 8.322   115.258 54.614 1.000 272.758 0 83  LYS EEE C   1 ? 8  
ATOM 6616  O O   . LYS E 3 86  ? 8.917   114.985 55.664 1.000 272.527 0 83  LYS EEE O   1 ? 8  
ATOM 6617  C CB  . LYS E 3 86  ? 9.070   114.367 52.399 1.000 260.043 0 83  LYS EEE CB  1 ? 8  
ATOM 6618  C CG  . LYS E 3 86  ? 9.916   114.564 51.159 1.000 250.052 0 83  LYS EEE CG  1 ? 8  
ATOM 6619  C CD  . LYS E 3 86  ? 9.649   113.487 50.125 1.000 242.772 0 83  LYS EEE CD  1 ? 8  
ATOM 6620  C CE  . LYS E 3 86  ? 10.754  113.461 49.097 1.000 239.092 0 83  LYS EEE CE  1 ? 8  
ATOM 6621  N NZ  . LYS E 3 86  ? 10.564  112.386 48.096 1.000 245.600 0 83  LYS EEE NZ  1 ? 8  
ATOM 6622  N N   . PRO E 3 87  ? 6.988   115.300 54.559 1.000 275.661 0 84  PRO EEE N   1 ? 8  
ATOM 6623  C CA  . PRO E 3 87  ? 6.208   114.885 55.734 1.000 273.082 0 84  PRO EEE CA  1 ? 8  
ATOM 6624  C C   . PRO E 3 87  ? 6.438   113.439 56.129 1.000 266.292 0 84  PRO EEE C   1 ? 8  
ATOM 6625  O O   . PRO E 3 87  ? 6.405   113.124 57.325 1.000 270.376 0 84  PRO EEE O   1 ? 8  
ATOM 6626  C CB  . PRO E 3 87  ? 4.756   115.122 55.292 1.000 284.793 0 84  PRO EEE CB  1 ? 8  
ATOM 6627  C CG  . PRO E 3 87  ? 4.851   116.155 54.225 1.000 288.045 0 84  PRO EEE CG  1 ? 8  
ATOM 6628  C CD  . PRO E 3 87  ? 6.133   115.883 53.507 1.000 279.294 0 84  PRO EEE CD  1 ? 8  
ATOM 6629  N N   . GLU E 3 88  ? 6.653   112.531 55.167 1.000 260.612 0 85  GLU EEE N   1 ? 8  
ATOM 6630  C CA  . GLU E 3 88  ? 6.938   111.152 55.550 1.000 258.618 0 85  GLU EEE CA  1 ? 8  
ATOM 6631  C C   . GLU E 3 88  ? 8.246   111.019 56.320 1.000 258.890 0 85  GLU EEE C   1 ? 8  
ATOM 6632  O O   . GLU E 3 88  ? 8.482   109.979 56.944 1.000 256.303 0 85  GLU EEE O   1 ? 8  
ATOM 6633  C CB  . GLU E 3 88  ? 7.008   110.297 54.285 1.000 251.114 0 85  GLU EEE CB  1 ? 8  
ATOM 6634  C CG  . GLU E 3 88  ? 5.721   110.261 53.482 1.000 255.107 0 85  GLU EEE CG  1 ? 8  
ATOM 6635  C CD  . GLU E 3 88  ? 5.815   109.355 52.271 1.000 259.453 0 85  GLU EEE CD  1 ? 8  
ATOM 6636  O OE1 . GLU E 3 88  ? 6.940   109.193 51.756 1.000 255.548 0 85  GLU EEE OE1 1 ? 8  
ATOM 6637  O OE2 . GLU E 3 88  ? 4.761   108.863 51.816 1.000 270.234 0 85  GLU EEE OE2 1 ? 8  
ATOM 6638  N N   . ASP E 3 89  ? 9.096   112.047 56.286 1.000 269.910 0 86  ASP EEE N   1 ? 8  
ATOM 6639  C CA  . ASP E 3 89  ? 10.353  112.094 57.024 1.000 262.863 0 86  ASP EEE CA  1 ? 8  
ATOM 6640  C C   . ASP E 3 89  ? 10.170  112.495 58.479 1.000 259.405 0 86  ASP EEE C   1 ? 8  
ATOM 6641  O O   . ASP E 3 89  ? 11.146  112.473 59.237 1.000 253.249 0 86  ASP EEE O   1 ? 8  
ATOM 6642  C CB  . ASP E 3 89  ? 11.359  113.015 56.331 1.000 263.634 0 86  ASP EEE CB  1 ? 8  
ATOM 6643  C CG  . ASP E 3 89  ? 11.762  112.502 54.959 1.000 273.504 0 86  ASP EEE CG  1 ? 8  
ATOM 6644  O OD1 . ASP E 3 89  ? 10.872  112.326 54.102 1.000 296.831 0 86  ASP EEE OD1 1 ? 8  
ATOM 6645  O OD2 . ASP E 3 89  ? 12.966  112.246 54.747 1.000 266.269 0 86  ASP EEE OD2 1 ? 8  
ATOM 6646  N N   . THR E 3 90  ? 8.956   112.875 58.874 1.000 267.608 0 87  THR EEE N   1 ? 8  
ATOM 6647  C CA  . THR E 3 90  ? 8.678   113.261 60.250 1.000 265.167 0 87  THR EEE CA  1 ? 8  
ATOM 6648  C C   . THR E 3 90  ? 8.944   112.112 61.210 1.000 259.911 0 87  THR EEE C   1 ? 8  
ATOM 6649  O O   . THR E 3 90  ? 8.338   111.042 61.098 1.000 251.161 0 87  THR EEE O   1 ? 8  
ATOM 6650  C CB  . THR E 3 90  ? 7.222   113.721 60.362 1.000 268.908 0 87  THR EEE CB  1 ? 8  
ATOM 6651  O OG1 . THR E 3 90  ? 6.990   114.816 59.466 1.000 281.168 0 87  THR EEE OG1 1 ? 8  
ATOM 6652  C CG2 . THR E 3 90  ? 6.873   114.136 61.781 1.000 276.493 0 87  THR EEE CG2 1 ? 8  
ATOM 6653  N N   . ALA E 3 91  ? 9.840   112.355 62.166 1.000 263.444 0 88  ALA EEE N   1 ? 8  
ATOM 6654  C CA  . ALA E 3 91  ? 10.269  111.385 63.168 1.000 262.758 0 88  ALA EEE CA  1 ? 8  
ATOM 6655  C C   . ALA E 3 91  ? 11.207  112.093 64.139 1.000 262.813 0 88  ALA EEE C   1 ? 8  
ATOM 6656  O O   . ALA E 3 91  ? 11.649  113.221 63.901 1.000 270.637 0 88  ALA EEE O   1 ? 8  
ATOM 6657  C CB  . ALA E 3 91  ? 10.969  110.172 62.549 1.000 255.112 0 88  ALA EEE CB  1 ? 8  
ATOM 6658  N N   . VAL E 3 92  ? 11.503  111.408 65.241 1.000 254.004 0 89  VAL EEE N   1 ? 8  
ATOM 6659  C CA  . VAL E 3 92  ? 12.570  111.783 66.166 1.000 243.962 0 89  VAL EEE CA  1 ? 8  
ATOM 6660  C C   . VAL E 3 92  ? 13.862  111.092 65.746 1.000 237.130 0 89  VAL EEE C   1 ? 8  
ATOM 6661  O O   . VAL E 3 92  ? 13.880  109.871 65.571 1.000 236.999 0 89  VAL EEE O   1 ? 8  
ATOM 6662  C CB  . VAL E 3 92  ? 12.194  111.415 67.611 1.000 239.475 0 89  VAL EEE CB  1 ? 8  
ATOM 6663  C CG1 . VAL E 3 92  ? 13.371  111.644 68.534 1.000 239.412 0 89  VAL EEE CG1 1 ? 8  
ATOM 6664  C CG2 . VAL E 3 92  ? 10.991  112.221 68.072 1.000 247.333 0 89  VAL EEE CG2 1 ? 8  
ATOM 6665  N N   . TYR E 3 93  ? 14.955  111.853 65.642 1.000 222.889 0 90  TYR EEE N   1 ? 8  
ATOM 6666  C CA  . TYR E 3 93  ? 16.235  111.364 65.126 1.000 215.784 0 90  TYR EEE CA  1 ? 8  
ATOM 6667  C C   . TYR E 3 93  ? 17.225  111.204 66.277 1.000 214.342 0 90  TYR EEE C   1 ? 8  
ATOM 6668  O O   . TYR E 3 93  ? 17.377  112.113 67.099 1.000 218.003 0 90  TYR EEE O   1 ? 8  
ATOM 6669  C CB  . TYR E 3 93  ? 16.798  112.316 64.064 1.000 218.717 0 90  TYR EEE CB  1 ? 8  
ATOM 6670  C CG  . TYR E 3 93  ? 16.081  112.261 62.727 1.000 225.212 0 90  TYR EEE CG  1 ? 8  
ATOM 6671  C CD1 . TYR E 3 93  ? 14.802  112.781 62.577 1.000 236.447 0 90  TYR EEE CD1 1 ? 8  
ATOM 6672  C CD2 . TYR E 3 93  ? 16.691  111.700 61.610 1.000 224.561 0 90  TYR EEE CD2 1 ? 8  
ATOM 6673  C CE1 . TYR E 3 93  ? 14.145  112.732 61.359 1.000 237.504 0 90  TYR EEE CE1 1 ? 8  
ATOM 6674  C CE2 . TYR E 3 93  ? 16.042  111.648 60.386 1.000 224.560 0 90  TYR EEE CE2 1 ? 8  
ATOM 6675  C CZ  . TYR E 3 93  ? 14.769  112.167 60.267 1.000 229.509 0 90  TYR EEE CZ  1 ? 8  
ATOM 6676  O OH  . TYR E 3 93  ? 14.114  112.120 59.057 1.000 227.306 0 90  TYR EEE OH  1 ? 8  
ATOM 6677  N N   . TYR E 3 94  ? 17.920  110.058 66.314 1.000 212.238 0 91  TYR EEE N   1 ? 8  
ATOM 6678  C CA  . TYR E 3 94  ? 18.873  109.717 67.369 1.000 215.393 0 91  TYR EEE CA  1 ? 8  
ATOM 6679  C C   . TYR E 3 94  ? 20.262  109.472 66.789 1.000 211.345 0 91  TYR EEE C   1 ? 8  
ATOM 6680  O O   . TYR E 3 94  ? 20.397  108.820 65.751 1.000 209.941 0 91  TYR EEE O   1 ? 8  
ATOM 6681  C CB  . TYR E 3 94  ? 18.428  108.432 68.084 1.000 217.663 0 91  TYR EEE CB  1 ? 8  
ATOM 6682  C CG  . TYR E 3 94  ? 16.972  108.410 68.500 1.000 226.128 0 91  TYR EEE CG  1 ? 8  
ATOM 6683  C CD1 . TYR E 3 94  ? 15.986  108.038 67.589 1.000 231.290 0 91  TYR EEE CD1 1 ? 8  
ATOM 6684  C CD2 . TYR E 3 94  ? 16.578  108.741 69.789 1.000 227.353 0 91  TYR EEE CD2 1 ? 8  
ATOM 6685  C CE1 . TYR E 3 94  ? 14.653  108.007 67.942 1.000 230.744 0 91  TYR EEE CE1 1 ? 8  
ATOM 6686  C CE2 . TYR E 3 94  ? 15.237  108.712 70.153 1.000 229.943 0 91  TYR EEE CE2 1 ? 8  
ATOM 6687  C CZ  . TYR E 3 94  ? 14.281  108.343 69.221 1.000 227.644 0 91  TYR EEE CZ  1 ? 8  
ATOM 6688  O OH  . TYR E 3 94  ? 12.948  108.308 69.562 1.000 224.583 0 91  TYR EEE OH  1 ? 8  
ATOM 6689  N N   . CYS E 3 95  ? 21.300  109.987 67.452 1.000 227.948 0 92  CYS EEE N   1 ? 8  
ATOM 6690  C CA  . CYS E 3 95  ? 22.669  109.595 67.139 1.000 221.934 0 92  CYS EEE CA  1 ? 8  
ATOM 6691  C C   . CYS E 3 95  ? 23.201  108.516 68.079 1.000 213.701 0 92  CYS EEE C   1 ? 8  
ATOM 6692  O O   . CYS E 3 95  ? 22.807  108.429 69.245 1.000 218.255 0 92  CYS EEE O   1 ? 8  
ATOM 6693  C CB  . CYS E 3 95  ? 23.597  110.809 67.216 1.000 228.853 0 92  CYS EEE CB  1 ? 8  
ATOM 6694  S SG  . CYS E 3 95  ? 23.469  111.687 68.798 1.000 259.679 0 92  CYS EEE SG  1 ? 8  
ATOM 6695  N N   . PHE E 3 96  ? 24.107  107.687 67.554 1.000 192.441 0 93  PHE EEE N   1 ? 8  
ATOM 6696  C CA  . PHE E 3 96  ? 24.811  106.692 68.349 1.000 185.231 0 93  PHE EEE CA  1 ? 8  
ATOM 6697  C C   . PHE E 3 96  ? 26.303  106.749 68.046 1.000 187.077 0 93  PHE EEE C   1 ? 8  
ATOM 6698  O O   . PHE E 3 96  ? 26.706  107.116 66.939 1.000 193.806 0 93  PHE EEE O   1 ? 8  
ATOM 6699  C CB  . PHE E 3 96  ? 24.276  105.270 68.067 1.000 180.395 0 93  PHE EEE CB  1 ? 8  
ATOM 6700  C CG  . PHE E 3 96  ? 24.630  104.745 66.696 1.000 173.196 0 93  PHE EEE CG  1 ? 8  
ATOM 6701  C CD1 . PHE E 3 96  ? 25.857  104.141 66.456 1.000 169.463 0 93  PHE EEE CD1 1 ? 8  
ATOM 6702  C CD2 . PHE E 3 96  ? 23.746  104.884 65.641 1.000 171.362 0 93  PHE EEE CD2 1 ? 8  
ATOM 6703  C CE1 . PHE E 3 96  ? 26.186  103.676 65.200 1.000 165.716 0 93  PHE EEE CE1 1 ? 8  
ATOM 6704  C CE2 . PHE E 3 96  ? 24.069  104.418 64.382 1.000 173.413 0 93  PHE EEE CE2 1 ? 8  
ATOM 6705  C CZ  . PHE E 3 96  ? 25.293  103.816 64.161 1.000 169.006 0 93  PHE EEE CZ  1 ? 8  
ATOM 6706  N N   . ALA E 3 97  ? 27.125  106.386 69.033 1.000 179.608 0 94  ALA EEE N   1 ? 8  
ATOM 6707  C CA  . ALA E 3 97  ? 28.571  106.293 68.860 1.000 169.311 0 94  ALA EEE CA  1 ? 8  
ATOM 6708  C C   . ALA E 3 97  ? 29.048  104.986 69.472 1.000 164.454 0 94  ALA EEE C   1 ? 8  
ATOM 6709  O O   . ALA E 3 97  ? 28.546  104.586 70.529 1.000 166.942 0 94  ALA EEE O   1 ? 8  
ATOM 6710  C CB  . ALA E 3 97  ? 29.316  107.465 69.512 1.000 167.650 0 94  ALA EEE CB  1 ? 8  
ATOM 6711  N N   . ALA E 3 98  ? 30.026  104.319 68.850 1.000 164.918 0 95  ALA EEE N   1 ? 8  
ATOM 6712  C CA  . ALA E 3 98  ? 30.449  103.046 69.415 1.000 157.766 0 95  ALA EEE CA  1 ? 8  
ATOM 6713  C C   . ALA E 3 98  ? 31.890  103.132 69.908 1.000 162.467 0 95  ALA EEE C   1 ? 8  
ATOM 6714  O O   . ALA E 3 98  ? 32.828  103.223 69.108 1.000 159.911 0 95  ALA EEE O   1 ? 8  
ATOM 6715  C CB  . ALA E 3 98  ? 30.324  101.950 68.351 1.000 132.206 0 95  ALA EEE CB  1 ? 8  
ATOM 6716  N N   . LEU E 3 99  ? 32.054  103.023 71.223 1.000 172.706 0 96  LEU EEE N   1 ? 8  
ATOM 6717  C CA  . LEU E 3 99  ? 33.304  102.844 71.952 1.000 182.495 0 96  LEU EEE CA  1 ? 8  
ATOM 6718  C C   . LEU E 3 99  ? 32.951  101.777 72.972 1.000 200.001 0 96  LEU EEE C   1 ? 8  
ATOM 6719  O O   . LEU E 3 99  ? 31.936  101.937 73.649 1.000 213.007 0 96  LEU EEE O   1 ? 8  
ATOM 6720  C CB  . LEU E 3 99  ? 33.850  104.125 72.589 1.000 197.452 0 96  LEU EEE CB  1 ? 8  
ATOM 6721  C CG  . LEU E 3 99  ? 35.362  104.003 72.820 1.000 188.103 0 96  LEU EEE CG  1 ? 8  
ATOM 6722  C CD1 . LEU E 3 99  ? 36.074  103.687 71.519 1.000 177.883 0 96  LEU EEE CD1 1 ? 8  
ATOM 6723  C CD2 . LEU E 3 99  ? 35.933  105.273 73.432 1.000 200.957 0 96  LEU EEE CD2 1 ? 8  
ATOM 6724  N N   . ASP E 3 100 ? 33.787  100.762 73.166 1.000 205.362 0 97  ASP EEE N   1 ? 8  
ATOM 6725  C CA  . ASP E 3 100 ? 33.569  99.769  74.225 1.000 211.246 0 97  ASP EEE CA  1 ? 8  
ATOM 6726  C C   . ASP E 3 100 ? 32.135  99.223  74.192 1.000 199.926 0 97  ASP EEE C   1 ? 8  
ATOM 6727  O O   . ASP E 3 100 ? 31.936  98.087  73.747 1.000 200.516 0 97  ASP EEE O   1 ? 8  
ATOM 6728  C CB  . ASP E 3 100 ? 33.908  100.310 75.638 1.000 226.985 0 97  ASP EEE CB  1 ? 8  
ATOM 6729  C CG  . ASP E 3 100 ? 33.252  101.651 75.972 1.000 241.795 0 97  ASP EEE CG  1 ? 8  
ATOM 6730  O OD1 . ASP E 3 100 ? 32.081  101.646 76.413 1.000 239.537 0 97  ASP EEE OD1 1 ? 8  
ATOM 6731  O OD2 . ASP E 3 100 ? 33.905  102.704 75.803 1.000 266.737 0 97  ASP EEE OD2 1 ? 8  
ATOM 6732  N N   . THR E 3 101 ? 31.124  99.998  74.614 1.000 187.462 0 98  THR EEE N   1 ? 8  
ATOM 6733  C CA  . THR E 3 101 ? 29.730  99.638  74.353 1.000 177.272 0 98  THR EEE CA  1 ? 8  
ATOM 6734  C C   . THR E 3 101 ? 29.090  100.625 73.369 1.000 171.916 0 98  THR EEE C   1 ? 8  
ATOM 6735  O O   . THR E 3 101 ? 29.750  101.495 72.802 1.000 177.820 0 98  THR EEE O   1 ? 8  
ATOM 6736  C CB  . THR E 3 101 ? 28.938  99.579  75.661 1.000 183.490 0 98  THR EEE CB  1 ? 8  
ATOM 6737  O OG1 . THR E 3 101 ? 27.638  99.028  75.408 1.000 162.080 0 98  THR EEE OG1 1 ? 8  
ATOM 6738  C CG2 . THR E 3 101 ? 28.784  100.967 76.269 1.000 196.723 0 98  THR EEE CG2 1 ? 8  
ATOM 6739  N N   . ALA E 3 102 ? 27.794  100.475 73.125 1.000 142.193 0 101 ALA EEE N   1 ? 8  
ATOM 6740  C CA  . ALA E 3 102 ? 27.080  101.423 72.280 1.000 138.632 0 101 ALA EEE CA  1 ? 8  
ATOM 6741  C C   . ALA E 3 102 ? 26.379  102.487 73.113 1.000 161.051 0 101 ALA EEE C   1 ? 8  
ATOM 6742  O O   . ALA E 3 102 ? 25.675  102.166 74.076 1.000 170.750 0 101 ALA EEE O   1 ? 8  
ATOM 6743  C CB  . ALA E 3 102 ? 26.068  100.702 71.390 1.000 128.182 0 101 ALA EEE CB  1 ? 8  
ATOM 6744  N N   . TYR E 3 103 ? 26.582  103.750 72.745 1.000 162.940 0 102 TYR EEE N   1 ? 8  
ATOM 6745  C CA  . TYR E 3 103 ? 25.944  104.877 73.408 1.000 172.352 0 102 TYR EEE CA  1 ? 8  
ATOM 6746  C C   . TYR E 3 103 ? 25.012  105.595 72.438 1.000 180.220 0 102 TYR EEE C   1 ? 8  
ATOM 6747  O O   . TYR E 3 103 ? 25.314  105.721 71.247 1.000 181.303 0 102 TYR EEE O   1 ? 8  
ATOM 6748  C CB  . TYR E 3 103 ? 26.967  105.864 73.983 1.000 172.929 0 102 TYR EEE CB  1 ? 8  
ATOM 6749  C CG  . TYR E 3 103 ? 27.976  105.306 74.978 1.000 182.176 0 102 TYR EEE CG  1 ? 8  
ATOM 6750  C CD1 . TYR E 3 103 ? 27.677  105.262 76.338 1.000 194.057 0 102 TYR EEE CD1 1 ? 8  
ATOM 6751  C CD2 . TYR E 3 103 ? 29.246  104.900 74.580 1.000 173.157 0 102 TYR EEE CD2 1 ? 8  
ATOM 6752  C CE1 . TYR E 3 103 ? 28.596  104.789 77.268 1.000 200.191 0 102 TYR EEE CE1 1 ? 8  
ATOM 6753  C CE2 . TYR E 3 103 ? 30.176  104.426 75.507 1.000 181.730 0 102 TYR EEE CE2 1 ? 8  
ATOM 6754  C CZ  . TYR E 3 103 ? 29.843  104.374 76.849 1.000 196.536 0 102 TYR EEE CZ  1 ? 8  
ATOM 6755  O OH  . TYR E 3 103 ? 30.755  103.905 77.772 1.000 204.045 0 102 TYR EEE OH  1 ? 8  
ATOM 6756  N N   . TRP E 3 104 ? 23.885  106.067 72.961 1.000 188.057 0 103 TRP EEE N   1 ? 8  
ATOM 6757  C CA  . TRP E 3 104 ? 22.847  106.753 72.202 1.000 201.071 0 103 TRP EEE CA  1 ? 8  
ATOM 6758  C C   . TRP E 3 104 ? 22.544  108.110 72.827 1.000 212.309 0 103 TRP EEE C   1 ? 8  
ATOM 6759  O O   . TRP E 3 104 ? 22.662  108.289 74.043 1.000 203.096 0 103 TRP EEE O   1 ? 8  
ATOM 6760  C CB  . TRP E 3 104 ? 21.567  105.920 72.108 1.000 202.838 0 103 TRP EEE CB  1 ? 8  
ATOM 6761  C CG  . TRP E 3 104 ? 21.662  104.639 71.323 1.000 188.627 0 103 TRP EEE CG  1 ? 8  
ATOM 6762  C CD1 . TRP E 3 104 ? 22.108  103.419 71.752 1.000 185.103 0 103 TRP EEE CD1 1 ? 8  
ATOM 6763  C CD2 . TRP E 3 104 ? 21.203  104.450 69.983 1.000 188.721 0 103 TRP EEE CD2 1 ? 8  
ATOM 6764  N NE1 . TRP E 3 104 ? 21.989  102.492 70.739 1.000 182.848 0 103 TRP EEE NE1 1 ? 8  
ATOM 6765  C CE2 . TRP E 3 104 ? 21.432  103.103 69.645 1.000 188.374 0 103 TRP EEE CE2 1 ? 8  
ATOM 6766  C CE3 . TRP E 3 104 ? 20.634  105.298 69.029 1.000 191.596 0 103 TRP EEE CE3 1 ? 8  
ATOM 6767  C CZ2 . TRP E 3 104 ? 21.112  102.584 68.392 1.000 189.932 0 103 TRP EEE CZ2 1 ? 8  
ATOM 6768  C CZ3 . TRP E 3 104 ? 20.317  104.785 67.788 1.000 197.933 0 103 TRP EEE CZ3 1 ? 8  
ATOM 6769  C CH2 . TRP E 3 104 ? 20.556  103.440 67.479 1.000 188.787 0 103 TRP EEE CH2 1 ? 8  
ATOM 6770  N N   . GLY E 3 105 ? 22.154  109.069 71.981 1.000 227.031 0 104 GLY EEE N   1 ? 8  
ATOM 6771  C CA  . GLY E 3 105 ? 21.544  110.301 72.441 1.000 227.911 0 104 GLY EEE CA  1 ? 8  
ATOM 6772  C C   . GLY E 3 105 ? 20.071  110.138 72.786 1.000 238.165 0 104 GLY EEE C   1 ? 8  
ATOM 6773  O O   . GLY E 3 105 ? 19.478  109.070 72.641 1.000 231.768 0 104 GLY EEE O   1 ? 8  
ATOM 6774  N N   . GLN E 3 106 ? 19.472  111.238 73.263 1.000 257.453 0 105 GLN EEE N   1 ? 8  
ATOM 6775  C CA  . GLN E 3 106 ? 18.055  111.246 73.617 1.000 270.211 0 105 GLN EEE CA  1 ? 8  
ATOM 6776  C C   . GLN E 3 106 ? 17.108  111.533 72.453 1.000 270.431 0 105 GLN EEE C   1 ? 8  
ATOM 6777  O O   . GLN E 3 106 ? 15.913  111.236 72.564 1.000 280.040 0 105 GLN EEE O   1 ? 8  
ATOM 6778  C CB  . GLN E 3 106 ? 17.821  112.299 74.705 1.000 280.558 0 105 GLN EEE CB  1 ? 8  
ATOM 6779  C CG  . GLN E 3 106 ? 18.413  111.943 76.063 1.000 283.644 0 105 GLN EEE CG  1 ? 8  
ATOM 6780  C CD  . GLN E 3 106 ? 19.860  112.413 76.211 1.000 284.622 0 105 GLN EEE CD  1 ? 8  
ATOM 6781  O OE1 . GLN E 3 106 ? 20.389  113.119 75.348 1.000 281.275 0 105 GLN EEE OE1 1 ? 8  
ATOM 6782  N NE2 . GLN E 3 106 ? 20.505  112.012 77.301 1.000 290.374 0 105 GLN EEE NE2 1 ? 8  
ATOM 6783  N N   . GLY E 3 107 ? 17.592  112.099 71.354 1.000 260.014 0 106 GLY EEE N   1 ? 8  
ATOM 6784  C CA  . GLY E 3 107 ? 16.813  112.292 70.147 1.000 256.395 0 106 GLY EEE CA  1 ? 8  
ATOM 6785  C C   . GLY E 3 107 ? 16.355  113.736 69.961 1.000 253.854 0 106 GLY EEE C   1 ? 8  
ATOM 6786  O O   . GLY E 3 107 ? 16.267  114.524 70.906 1.000 252.207 0 106 GLY EEE O   1 ? 8  
ATOM 6787  N N   . THR E 3 108 ? 16.047  114.082 68.706 1.000 249.954 0 107 THR EEE N   1 ? 8  
ATOM 6788  C CA  . THR E 3 108 ? 15.462  115.373 68.351 1.000 247.586 0 107 THR EEE CA  1 ? 8  
ATOM 6789  C C   . THR E 3 108 ? 14.274  115.180 67.411 1.000 250.931 0 107 THR EEE C   1 ? 8  
ATOM 6790  O O   . THR E 3 108 ? 14.324  114.346 66.503 1.000 244.713 0 107 THR EEE O   1 ? 8  
ATOM 6791  C CB  . THR E 3 108 ? 16.504  116.323 67.727 1.000 243.101 0 107 THR EEE CB  1 ? 8  
ATOM 6792  O OG1 . THR E 3 108 ? 15.908  117.605 67.498 1.000 251.676 0 107 THR EEE OG1 1 ? 8  
ATOM 6793  C CG2 . THR E 3 108 ? 17.056  115.773 66.417 1.000 233.933 0 107 THR EEE CG2 1 ? 8  
ATOM 6794  N N   . GLN E 3 109 ? 13.203  115.942 67.636 1.000 259.658 0 108 GLN EEE N   1 ? 8  
ATOM 6795  C CA  . GLN E 3 109 ? 11.963  115.777 66.879 1.000 262.738 0 108 GLN EEE CA  1 ? 8  
ATOM 6796  C C   . GLN E 3 109 ? 12.036  116.528 65.550 1.000 266.717 0 108 GLN EEE C   1 ? 8  
ATOM 6797  O O   . GLN E 3 109 ? 12.420  117.702 65.514 1.000 271.306 0 108 GLN EEE O   1 ? 8  
ATOM 6798  C CB  . GLN E 3 109 ? 10.764  116.265 67.693 1.000 258.620 0 108 GLN EEE CB  1 ? 8  
ATOM 6799  C CG  . GLN E 3 109 ? 9.465   116.319 66.896 1.000 261.630 0 108 GLN EEE CG  1 ? 8  
ATOM 6800  C CD  . GLN E 3 109 ? 8.788   114.964 66.770 1.000 257.427 0 108 GLN EEE CD  1 ? 8  
ATOM 6801  O OE1 . GLN E 3 109 ? 8.526   114.291 67.767 1.000 255.548 0 108 GLN EEE OE1 1 ? 8  
ATOM 6802  N NE2 . GLN E 3 109 ? 8.518   114.552 65.537 1.000 260.244 0 108 GLN EEE NE2 1 ? 8  
ATOM 6803  N N   . VAL E 3 110 ? 11.673  115.856 64.456 1.000 265.263 0 109 VAL EEE N   1 ? 8  
ATOM 6804  C CA  . VAL E 3 110 ? 11.605  116.483 63.137 1.000 272.295 0 109 VAL EEE CA  1 ? 8  
ATOM 6805  C C   . VAL E 3 110 ? 10.196  116.326 62.583 1.000 278.963 0 109 VAL EEE C   1 ? 8  
ATOM 6806  O O   . VAL E 3 110 ? 9.680   115.207 62.484 1.000 269.380 0 109 VAL EEE O   1 ? 8  
ATOM 6807  C CB  . VAL E 3 110 ? 12.633  115.882 62.164 1.000 271.144 0 109 VAL EEE CB  1 ? 8  
ATOM 6808  C CG1 . VAL E 3 110 ? 12.354  116.340 60.730 1.000 268.603 0 109 VAL EEE CG1 1 ? 8  
ATOM 6809  C CG2 . VAL E 3 110 ? 14.039  116.265 62.585 1.000 272.519 0 109 VAL EEE CG2 1 ? 8  
ATOM 6810  N N   . THR E 3 111 ? 9.579   117.456 62.235 1.000 297.156 0 110 THR EEE N   1 ? 8  
ATOM 6811  C CA  . THR E 3 111 ? 8.184   117.550 61.817 1.000 300.433 0 110 THR EEE CA  1 ? 8  
ATOM 6812  C C   . THR E 3 111 ? 8.120   118.361 60.530 1.000 306.547 0 110 THR EEE C   1 ? 8  
ATOM 6813  O O   . THR E 3 111 ? 8.595   119.499 60.499 1.000 308.469 0 110 THR EEE O   1 ? 8  
ATOM 6814  C CB  . THR E 3 111 ? 7.311   118.191 62.900 1.000 294.656 0 110 THR EEE CB  1 ? 8  
ATOM 6815  O OG1 . THR E 3 111 ? 7.688   117.683 64.186 1.000 295.233 0 110 THR EEE OG1 1 ? 8  
ATOM 6816  C CG2 . THR E 3 111 ? 5.843   117.876 62.649 1.000 293.126 0 110 THR EEE CG2 1 ? 8  
ATOM 6817  N N   . VAL E 3 112 ? 7.617   117.769 59.453 1.000 319.716 0 111 VAL EEE N   1 ? 8  
ATOM 6818  C CA  . VAL E 3 112 ? 7.493   118.548 58.223 1.000 313.484 0 111 VAL EEE CA  1 ? 8  
ATOM 6819  C C   . VAL E 3 112 ? 6.024   118.779 57.888 1.000 314.387 0 111 VAL EEE C   1 ? 8  
ATOM 6820  O O   . VAL E 3 112 ? 5.572   119.919 57.782 1.000 315.947 0 111 VAL EEE O   1 ? 8  
ATOM 6821  C CB  . VAL E 3 112 ? 8.199   117.879 57.049 1.000 307.148 0 111 VAL EEE CB  1 ? 8  
ATOM 6822  C CG1 . VAL E 3 112 ? 7.584   118.361 55.741 1.000 306.320 0 111 VAL EEE CG1 1 ? 8  
ATOM 6823  C CG2 . VAL E 3 112 ? 9.685   118.173 57.094 1.000 300.124 0 111 VAL EEE CG2 1 ? 8  
ATOM 6824  N N   . VAL F 4 1   ? 14.271  64.468  81.698 1.000 316.872 0 2   VAL DDD N   1 ? 9  
ATOM 6825  C CA  . VAL F 4 1   ? 13.742  64.170  80.373 1.000 312.584 0 2   VAL DDD CA  1 ? 9  
ATOM 6826  C C   . VAL F 4 1   ? 13.029  62.814  80.359 1.000 321.276 0 2   VAL DDD C   1 ? 9  
ATOM 6827  O O   . VAL F 4 1   ? 13.612  61.792  80.719 1.000 348.682 0 2   VAL DDD O   1 ? 9  
ATOM 6828  C CB  . VAL F 4 1   ? 14.856  64.207  79.313 1.000 288.749 0 2   VAL DDD CB  1 ? 9  
ATOM 6829  C CG1 . VAL F 4 1   ? 14.292  63.858  77.948 1.000 288.517 0 2   VAL DDD CG1 1 ? 9  
ATOM 6830  C CG2 . VAL F 4 1   ? 15.509  65.582  79.282 1.000 272.986 0 2   VAL DDD CG2 1 ? 9  
ATOM 6831  N N   . GLN F 4 2   ? 11.761  62.830  79.956 1.000 312.650 0 3   GLN DDD N   1 ? 9  
ATOM 6832  C CA  . GLN F 4 2   ? 10.875  61.676  79.915 1.000 292.957 0 3   GLN DDD CA  1 ? 9  
ATOM 6833  C C   . GLN F 4 2   ? 10.426  61.385  78.484 1.000 287.496 0 3   GLN DDD C   1 ? 9  
ATOM 6834  O O   . GLN F 4 2   ? 10.590  62.205  77.572 1.000 293.655 0 3   GLN DDD O   1 ? 9  
ATOM 6835  C CB  . GLN F 4 2   ? 9.677   61.864  80.852 1.000 287.473 0 3   GLN DDD CB  1 ? 9  
ATOM 6836  C CG  . GLN F 4 2   ? 10.097  61.974  82.312 1.000 280.236 0 3   GLN DDD CG  1 ? 9  
ATOM 6837  C CD  . GLN F 4 2   ? 10.634  60.661  82.860 1.000 272.442 0 3   GLN DDD CD  1 ? 9  
ATOM 6838  O OE1 . GLN F 4 2   ? 10.125  59.589  82.536 1.000 274.889 0 3   GLN DDD OE1 1 ? 9  
ATOM 6839  N NE2 . GLN F 4 2   ? 11.681  60.739  83.674 1.000 266.075 0 3   GLN DDD NE2 1 ? 9  
ATOM 6840  N N   . LEU F 4 3   ? 9.876   60.185  78.291 1.000 280.126 0 4   LEU DDD N   1 ? 9  
ATOM 6841  C CA  . LEU F 4 3   ? 9.346   59.731  77.014 1.000 276.412 0 4   LEU DDD CA  1 ? 9  
ATOM 6842  C C   . LEU F 4 3   ? 7.903   59.290  77.180 1.000 288.192 0 4   LEU DDD C   1 ? 9  
ATOM 6843  O O   . LEU F 4 3   ? 7.537   58.736  78.225 1.000 296.741 0 4   LEU DDD O   1 ? 9  
ATOM 6844  C CB  . LEU F 4 3   ? 10.128  58.552  76.509 1.000 267.086 0 4   LEU DDD CB  1 ? 9  
ATOM 6845  C CG  . LEU F 4 3   ? 11.541  58.849  76.065 1.000 274.220 0 4   LEU DDD CG  1 ? 9  
ATOM 6846  C CD1 . LEU F 4 3   ? 12.073  57.508  75.751 1.000 285.382 0 4   LEU DDD CD1 1 ? 9  
ATOM 6847  C CD2 . LEU F 4 3   ? 11.613  59.771  74.855 1.000 276.229 0 4   LEU DDD CD2 1 ? 9  
ATOM 6848  N N   . GLN F 4 4   ? 7.077   59.540  76.162 1.000 289.065 0 5   GLN DDD N   1 ? 9  
ATOM 6849  C CA  . GLN F 4 4   ? 5.688   59.085  76.166 1.000 296.771 0 5   GLN DDD CA  1 ? 9  
ATOM 6850  C C   . GLN F 4 4   ? 5.210   58.683  74.774 1.000 300.293 0 5   GLN DDD C   1 ? 9  
ATOM 6851  O O   . GLN F 4 4   ? 5.266   59.496  73.844 1.000 299.454 0 5   GLN DDD O   1 ? 9  
ATOM 6852  C CB  . GLN F 4 4   ? 4.777   60.172  76.731 1.000 297.495 0 5   GLN DDD CB  1 ? 9  
ATOM 6853  C CG  . GLN F 4 4   ? 3.369   59.702  76.859 1.000 304.327 0 5   GLN DDD CG  1 ? 9  
ATOM 6854  C CD  . GLN F 4 4   ? 3.323   58.403  77.623 1.000 301.930 0 5   GLN DDD CD  1 ? 9  
ATOM 6855  O OE1 . GLN F 4 4   ? 3.012   57.355  77.060 1.000 303.873 0 5   GLN DDD OE1 1 ? 9  
ATOM 6856  N NE2 . GLN F 4 4   ? 3.662   58.454  78.907 1.000 298.413 0 5   GLN DDD NE2 1 ? 9  
ATOM 6857  N N   . GLU F 4 5   ? 4.741   57.442  74.612 1.000 304.870 0 6   GLU DDD N   1 ? 9  
ATOM 6858  C CA  . GLU F 4 5   ? 4.144   57.071  73.330 1.000 311.583 0 6   GLU DDD CA  1 ? 9  
ATOM 6859  C C   . GLU F 4 5   ? 2.707   57.613  73.265 1.000 315.099 0 6   GLU DDD C   1 ? 9  
ATOM 6860  O O   . GLU F 4 5   ? 2.091   57.898  74.295 1.000 315.845 0 6   GLU DDD O   1 ? 9  
ATOM 6861  C CB  . GLU F 4 5   ? 4.179   55.544  73.197 1.000 319.382 0 6   GLU DDD CB  1 ? 9  
ATOM 6862  C CG  . GLU F 4 5   ? 3.230   54.911  72.195 1.000 331.729 0 6   GLU DDD CG  1 ? 9  
ATOM 6863  C CD  . GLU F 4 5   ? 3.774   54.877  70.786 1.000 334.948 0 6   GLU DDD CD  1 ? 9  
ATOM 6864  O OE1 . GLU F 4 5   ? 4.905   54.382  70.599 1.000 338.770 0 6   GLU DDD OE1 1 ? 9  
ATOM 6865  O OE2 . GLU F 4 5   ? 3.058   55.324  69.865 1.000 333.824 0 6   GLU DDD OE2 1 ? 9  
ATOM 6866  N N   . SER F 4 6   ? 2.170   57.760  72.045 1.000 316.598 0 7   SER DDD N   1 ? 9  
ATOM 6867  C CA  . SER F 4 6   ? 0.782   58.200  71.847 1.000 307.205 0 7   SER DDD CA  1 ? 9  
ATOM 6868  C C   . SER F 4 6   ? 0.345   58.025  70.390 1.000 300.397 0 7   SER DDD C   1 ? 9  
ATOM 6869  O O   . SER F 4 6   ? 1.111   57.539  69.554 1.000 303.040 0 7   SER DDD O   1 ? 9  
ATOM 6870  C CB  . SER F 4 6   ? 0.614   59.668  72.262 1.000 305.078 0 7   SER DDD CB  1 ? 9  
ATOM 6871  O OG  . SER F 4 6   ? 1.360   60.534  71.419 1.000 309.648 0 7   SER DDD OG  1 ? 9  
ATOM 6872  N N   . GLY F 4 7   ? -0.952  58.261  70.134 1.000 299.482 0 8   GLY DDD N   1 ? 9  
ATOM 6873  C CA  . GLY F 4 7   ? -1.510  58.151  68.790 1.000 296.736 0 8   GLY DDD CA  1 ? 9  
ATOM 6874  C C   . GLY F 4 7   ? -2.191  56.889  68.309 1.000 303.432 0 8   GLY DDD C   1 ? 9  
ATOM 6875  O O   . GLY F 4 7   ? -2.630  56.860  67.152 1.000 298.773 0 8   GLY DDD O   1 ? 9  
ATOM 6876  N N   . GLY F 4 8   ? -2.294  55.870  69.109 1.000 308.974 0 9   GLY DDD N   1 ? 9  
ATOM 6877  C CA  . GLY F 4 8   ? -2.941  54.653  68.674 1.000 317.431 0 9   GLY DDD CA  1 ? 9  
ATOM 6878  C C   . GLY F 4 8   ? -4.444  54.598  68.827 1.000 324.772 0 9   GLY DDD C   1 ? 9  
ATOM 6879  O O   . GLY F 4 8   ? -5.052  55.345  69.590 1.000 326.419 0 9   GLY DDD O   1 ? 9  
ATOM 6880  N N   . GLY F 4 9   ? -5.028  53.684  68.064 1.000 343.121 0 10  GLY DDD N   1 ? 9  
ATOM 6881  C CA  . GLY F 4 9   ? -6.460  53.489  68.096 1.000 374.667 0 10  GLY DDD CA  1 ? 9  
ATOM 6882  C C   . GLY F 4 9   ? -6.901  52.461  67.078 1.000 393.717 0 10  GLY DDD C   1 ? 9  
ATOM 6883  O O   . GLY F 4 9   ? -6.100  51.659  66.593 1.000 420.534 0 10  GLY DDD O   1 ? 9  
ATOM 6884  N N   . LEU F 4 10  ? -8.191  52.510  66.758 1.000 378.244 0 11  LEU DDD N   1 ? 9  
ATOM 6885  C CA  . LEU F 4 10  ? -8.881  51.531  65.921 1.000 362.537 0 11  LEU DDD CA  1 ? 9  
ATOM 6886  C C   . LEU F 4 10  ? -9.299  52.063  64.552 1.000 373.865 0 11  LEU DDD C   1 ? 9  
ATOM 6887  O O   . LEU F 4 10  ? -9.926  53.124  64.469 1.000 374.542 0 11  LEU DDD O   1 ? 9  
ATOM 6888  C CB  . LEU F 4 10  ? -10.117 51.013  66.660 1.000 333.104 0 11  LEU DDD CB  1 ? 9  
ATOM 6889  C CG  . LEU F 4 10  ? -9.920  49.730  67.462 1.000 317.945 0 11  LEU DDD CG  1 ? 9  
ATOM 6890  C CD1 . LEU F 4 10  ? -9.339  48.665  66.563 1.000 319.865 0 11  LEU DDD CD1 1 ? 9  
ATOM 6891  C CD2 . LEU F 4 10  ? -9.012  49.976  68.658 1.000 315.844 0 11  LEU DDD CD2 1 ? 9  
ATOM 6892  N N   . VAL F 4 11  ? -8.959  51.333  63.480 1.000 385.777 0 12  VAL DDD N   1 ? 9  
ATOM 6893  C CA  . VAL F 4 11  ? -9.268  51.763  62.119 1.000 384.270 0 12  VAL DDD CA  1 ? 9  
ATOM 6894  C C   . VAL F 4 11  ? -9.683  50.532  61.315 1.000 380.306 0 12  VAL DDD C   1 ? 9  
ATOM 6895  O O   . VAL F 4 11  ? -9.327  49.400  61.645 1.000 390.734 0 12  VAL DDD O   1 ? 9  
ATOM 6896  C CB  . VAL F 4 11  ? -8.083  52.463  61.418 1.000 381.637 0 12  VAL DDD CB  1 ? 9  
ATOM 6897  C CG1 . VAL F 4 11  ? -7.652  53.703  62.177 1.000 380.827 0 12  VAL DDD CG1 1 ? 9  
ATOM 6898  C CG2 . VAL F 4 11  ? -6.915  51.497  61.283 1.000 376.531 0 12  VAL DDD CG2 1 ? 9  
ATOM 6899  N N   . GLN F 4 12  ? -10.455 50.764  60.249 1.000 360.829 0 13  GLN DDD N   1 ? 9  
ATOM 6900  C CA  . GLN F 4 12  ? -10.828 49.718  59.305 1.000 346.567 0 13  GLN DDD CA  1 ? 9  
ATOM 6901  C C   . GLN F 4 12  ? -9.759  49.445  58.248 1.000 343.500 0 13  GLN DDD C   1 ? 9  
ATOM 6902  O O   . GLN F 4 12  ? -8.860  50.254  58.008 1.000 347.351 0 13  GLN DDD O   1 ? 9  
ATOM 6903  C CB  . GLN F 4 12  ? -12.133 50.088  58.605 1.000 336.746 0 13  GLN DDD CB  1 ? 9  
ATOM 6904  C CG  . GLN F 4 12  ? -12.898 48.933  57.990 1.000 328.398 0 13  GLN DDD CG  1 ? 9  
ATOM 6905  C CD  . GLN F 4 12  ? -12.922 49.011  56.488 1.000 324.360 0 13  GLN DDD CD  1 ? 9  
ATOM 6906  O OE1 . GLN F 4 12  ? -12.875 50.109  55.931 1.000 326.545 0 13  GLN DDD OE1 1 ? 9  
ATOM 6907  N NE2 . GLN F 4 12  ? -13.047 47.873  55.826 1.000 319.040 0 13  GLN DDD NE2 1 ? 9  
ATOM 6908  N N   . ALA F 4 13  ? -9.865  48.265  57.628 1.000 334.513 0 14  ALA DDD N   1 ? 9  
ATOM 6909  C CA  . ALA F 4 13  ? -8.998  47.903  56.514 1.000 326.617 0 14  ALA DDD CA  1 ? 9  
ATOM 6910  C C   . ALA F 4 13  ? -9.133  48.900  55.363 1.000 329.212 0 14  ALA DDD C   1 ? 9  
ATOM 6911  O O   . ALA F 4 13  ? -10.228 49.386  55.064 1.000 328.051 0 14  ALA DDD O   1 ? 9  
ATOM 6912  C CB  . ALA F 4 13  ? -9.330  46.495  56.025 1.000 314.219 0 14  ALA DDD CB  1 ? 9  
ATOM 6913  N N   . GLY F 4 14  ? -8.017  49.185  54.701 1.000 329.391 0 15  GLY DDD N   1 ? 9  
ATOM 6914  C CA  . GLY F 4 14  ? -7.959  50.145  53.619 1.000 327.362 0 15  GLY DDD CA  1 ? 9  
ATOM 6915  C C   . GLY F 4 14  ? -7.917  51.594  54.051 1.000 330.929 0 15  GLY DDD C   1 ? 9  
ATOM 6916  O O   . GLY F 4 14  ? -7.801  52.479  53.192 1.000 329.597 0 15  GLY DDD O   1 ? 9  
ATOM 6917  N N   . GLY F 4 15  ? -7.987  51.860  55.352 1.000 336.505 0 16  GLY DDD N   1 ? 9  
ATOM 6918  C CA  . GLY F 4 15  ? -7.975  53.201  55.896 1.000 335.392 0 16  GLY DDD CA  1 ? 9  
ATOM 6919  C C   . GLY F 4 15  ? -6.570  53.748  56.032 1.000 328.125 0 16  GLY DDD C   1 ? 9  
ATOM 6920  O O   . GLY F 4 15  ? -5.592  53.151  55.586 1.000 324.818 0 16  GLY DDD O   1 ? 9  
ATOM 6921  N N   . SER F 4 16  ? -6.471  54.941  56.623 1.000 327.013 0 17  SER DDD N   1 ? 9  
ATOM 6922  C CA  . SER F 4 16  ? -5.170  55.557  56.848 1.000 316.036 0 17  SER DDD CA  1 ? 9  
ATOM 6923  C C   . SER F 4 16  ? -5.133  56.027  58.301 1.000 308.658 0 17  SER DDD C   1 ? 9  
ATOM 6924  O O   . SER F 4 16  ? -6.176  56.293  58.904 1.000 301.834 0 17  SER DDD O   1 ? 9  
ATOM 6925  C CB  . SER F 4 16  ? -4.916  56.728  55.877 1.000 311.957 0 17  SER DDD CB  1 ? 9  
ATOM 6926  O OG  . SER F 4 16  ? -4.625  56.264  54.567 1.000 312.279 0 17  SER DDD OG  1 ? 9  
ATOM 6927  N N   . LEU F 4 17  ? -3.923  56.144  58.857 1.000 306.627 0 18  LEU DDD N   1 ? 9  
ATOM 6928  C CA  . LEU F 4 17  ? -3.738  56.570  60.245 1.000 305.173 0 18  LEU DDD CA  1 ? 9  
ATOM 6929  C C   . LEU F 4 17  ? -2.330  57.145  60.424 1.000 315.352 0 18  LEU DDD C   1 ? 9  
ATOM 6930  O O   . LEU F 4 17  ? -1.434  56.836  59.641 1.000 321.566 0 18  LEU DDD O   1 ? 9  
ATOM 6931  C CB  . LEU F 4 17  ? -4.025  55.428  61.226 1.000 293.930 0 18  LEU DDD CB  1 ? 9  
ATOM 6932  C CG  . LEU F 4 17  ? -4.197  55.937  62.656 1.000 281.992 0 18  LEU DDD CG  1 ? 9  
ATOM 6933  C CD1 . LEU F 4 17  ? -5.409  56.849  62.711 1.000 278.099 0 18  LEU DDD CD1 1 ? 9  
ATOM 6934  C CD2 . LEU F 4 17  ? -4.368  54.793  63.631 1.000 280.742 0 18  LEU DDD CD2 1 ? 9  
ATOM 6935  N N   . ARG F 4 18  ? -2.161  58.042  61.400 1.000 309.893 0 19  ARG DDD N   1 ? 9  
ATOM 6936  C CA  . ARG F 4 18  ? -0.865  58.651  61.727 1.000 300.803 0 19  ARG DDD CA  1 ? 9  
ATOM 6937  C C   . ARG F 4 18  ? -0.547  58.504  63.216 1.000 301.001 0 19  ARG DDD C   1 ? 9  
ATOM 6938  O O   . ARG F 4 18  ? -1.302  59.002  64.060 1.000 302.285 0 19  ARG DDD O   1 ? 9  
ATOM 6939  C CB  . ARG F 4 18  ? -0.810  60.119  61.336 1.000 296.227 0 19  ARG DDD CB  1 ? 9  
ATOM 6940  C CG  . ARG F 4 18  ? 0.469   60.740  61.834 1.000 287.786 0 19  ARG DDD CG  1 ? 9  
ATOM 6941  C CD  . ARG F 4 18  ? 0.278   62.203  62.102 1.000 280.348 0 19  ARG DDD CD  1 ? 9  
ATOM 6942  N NE  . ARG F 4 18  ? -0.486  62.853  61.048 1.000 282.266 0 19  ARG DDD NE  1 ? 9  
ATOM 6943  C CZ  . ARG F 4 18  ? 0.042   63.637  60.121 1.000 281.562 0 19  ARG DDD CZ  1 ? 9  
ATOM 6944  N NH1 . ARG F 4 18  ? 1.338   63.897  60.098 1.000 274.775 0 19  ARG DDD NH1 1 ? 9  
ATOM 6945  N NH2 . ARG F 4 18  ? -0.747  64.168  59.191 1.000 286.321 0 19  ARG DDD NH2 1 ? 9  
ATOM 6946  N N   . LEU F 4 19  ? 0.507   57.755  63.558 1.000 303.537 0 20  LEU DDD N   1 ? 9  
ATOM 6947  C CA  . LEU F 4 19  ? 0.930   57.638  64.958 1.000 311.148 0 20  LEU DDD CA  1 ? 9  
ATOM 6948  C C   . LEU F 4 19  ? 1.923   58.744  65.380 1.000 321.842 0 20  LEU DDD C   1 ? 9  
ATOM 6949  O O   . LEU F 4 19  ? 2.766   59.180  64.587 1.000 336.371 0 20  LEU DDD O   1 ? 9  
ATOM 6950  C CB  . LEU F 4 19  ? 1.559   56.248  65.133 1.000 307.641 0 20  LEU DDD CB  1 ? 9  
ATOM 6951  C CG  . LEU F 4 19  ? 0.711   54.976  65.364 1.000 301.918 0 20  LEU DDD CG  1 ? 9  
ATOM 6952  C CD1 . LEU F 4 19  ? 1.575   53.727  65.453 1.000 307.512 0 20  LEU DDD CD1 1 ? 9  
ATOM 6953  C CD2 . LEU F 4 19  ? -0.134  55.019  66.617 1.000 292.638 0 20  LEU DDD CD2 1 ? 9  
ATOM 6954  N N   . SER F 4 20  ? 1.836   59.176  66.658 1.000 320.324 0 21  SER DDD N   1 ? 9  
ATOM 6955  C CA  . SER F 4 20  ? 2.690   60.233  67.227 1.000 320.968 0 21  SER DDD CA  1 ? 9  
ATOM 6956  C C   . SER F 4 20  ? 3.205   59.946  68.648 1.000 323.340 0 21  SER DDD C   1 ? 9  
ATOM 6957  O O   . SER F 4 20  ? 2.423   59.607  69.529 1.000 339.236 0 21  SER DDD O   1 ? 9  
ATOM 6958  C CB  . SER F 4 20  ? 1.947   61.574  67.170 1.000 319.453 0 21  SER DDD CB  1 ? 9  
ATOM 6959  O OG  . SER F 4 20  ? 1.949   62.046  65.832 1.000 310.509 0 21  SER DDD OG  1 ? 9  
ATOM 6960  N N   . CYS F 4 21  ? 4.495   60.245  68.886 1.000 317.927 0 22  CYS DDD N   1 ? 9  
ATOM 6961  C CA  . CYS F 4 21  ? 5.253   59.987  70.124 1.000 307.909 0 22  CYS DDD CA  1 ? 9  
ATOM 6962  C C   . CYS F 4 21  ? 5.801   61.221  70.814 1.000 296.316 0 22  CYS DDD C   1 ? 9  
ATOM 6963  O O   . CYS F 4 21  ? 6.657   61.915  70.255 1.000 298.250 0 22  CYS DDD O   1 ? 9  
ATOM 6964  C CB  . CYS F 4 21  ? 6.435   59.067  69.885 1.000 316.540 0 22  CYS DDD CB  1 ? 9  
ATOM 6965  S SG  . CYS F 4 21  ? 5.966   57.510  69.304 1.000 340.031 0 22  CYS DDD SG  1 ? 9  
ATOM 6966  N N   . ALA F 4 22  ? 5.298   61.510  72.007 1.000 294.530 0 23  ALA DDD N   1 ? 9  
ATOM 6967  C CA  . ALA F 4 22  ? 5.773   62.668  72.741 1.000 288.277 0 23  ALA DDD CA  1 ? 9  
ATOM 6968  C C   . ALA F 4 22  ? 6.985   62.391  73.642 1.000 284.931 0 23  ALA DDD C   1 ? 9  
ATOM 6969  O O   . ALA F 4 22  ? 7.082   61.369  74.343 1.000 283.983 0 23  ALA DDD O   1 ? 9  
ATOM 6970  C CB  . ALA F 4 22  ? 4.610   63.290  73.514 1.000 283.084 0 23  ALA DDD CB  1 ? 9  
ATOM 6971  N N   . ALA F 4 23  ? 7.918   63.335  73.543 1.000 290.811 0 24  ALA DDD N   1 ? 9  
ATOM 6972  C CA  . ALA F 4 23  ? 9.219   63.434  74.180 1.000 298.142 0 24  ALA DDD CA  1 ? 9  
ATOM 6973  C C   . ALA F 4 23  ? 9.322   64.713  74.995 1.000 320.669 0 24  ALA DDD C   1 ? 9  
ATOM 6974  O O   . ALA F 4 23  ? 8.762   65.747  74.616 1.000 318.776 0 24  ALA DDD O   1 ? 9  
ATOM 6975  C CB  . ALA F 4 23  ? 10.339  63.456  73.134 1.000 297.122 0 24  ALA DDD CB  1 ? 9  
ATOM 6976  N N   . SER F 4 24  ? 10.029  64.645  76.120 1.000 342.387 0 25  SER DDD N   1 ? 9  
ATOM 6977  C CA  . SER F 4 24  ? 10.293  65.893  76.812 1.000 346.187 0 25  SER DDD CA  1 ? 9  
ATOM 6978  C C   . SER F 4 24  ? 11.410  66.641  76.092 1.000 346.120 0 25  SER DDD C   1 ? 9  
ATOM 6979  O O   . SER F 4 24  ? 12.261  66.050  75.418 1.000 338.217 0 25  SER DDD O   1 ? 9  
ATOM 6980  C CB  . SER F 4 24  ? 10.701  65.635  78.262 1.000 343.426 0 25  SER DDD CB  1 ? 9  
ATOM 6981  O OG  . SER F 4 24  ? 11.379  66.760  78.793 1.000 342.842 0 25  SER DDD OG  1 ? 9  
ATOM 6982  N N   . GLY F 4 25  ? 11.413  67.960  76.268 1.000 341.354 0 26  GLY DDD N   1 ? 9  
ATOM 6983  C CA  . GLY F 4 25  ? 12.332  68.773  75.506 1.000 349.476 0 26  GLY DDD CA  1 ? 9  
ATOM 6984  C C   . GLY F 4 25  ? 11.943  68.771  74.031 1.000 359.737 0 26  GLY DDD C   1 ? 9  
ATOM 6985  O O   . GLY F 4 25  ? 10.830  68.409  73.644 1.000 353.852 0 26  GLY DDD O   1 ? 9  
ATOM 6986  N N   . SER F 4 26  ? 12.904  69.173  73.199 1.000 383.604 0 27  SER DDD N   1 ? 9  
ATOM 6987  C CA  . SER F 4 26  ? 12.736  69.221  71.750 1.000 413.002 0 27  SER DDD CA  1 ? 9  
ATOM 6988  C C   . SER F 4 26  ? 13.229  67.936  71.092 1.000 427.411 0 27  SER DDD C   1 ? 9  
ATOM 6989  O O   . SER F 4 26  ? 14.289  67.418  71.447 1.000 456.301 0 27  SER DDD O   1 ? 9  
ATOM 6990  C CB  . SER F 4 26  ? 13.472  70.421  71.159 1.000 422.983 0 27  SER DDD CB  1 ? 9  
ATOM 6991  O OG  . SER F 4 26  ? 13.310  70.469  69.752 1.000 435.365 0 27  SER DDD OG  1 ? 9  
ATOM 6992  N N   . ILE F 4 27  ? 12.445  67.413  70.143 1.000 415.011 0 28  ILE DDD N   1 ? 9  
ATOM 6993  C CA  . ILE F 4 27  ? 12.792  66.144  69.507 1.000 374.543 0 28  ILE DDD CA  1 ? 9  
ATOM 6994  C C   . ILE F 4 27  ? 13.923  66.302  68.492 1.000 355.848 0 28  ILE DDD C   1 ? 9  
ATOM 6995  O O   . ILE F 4 27  ? 14.621  65.322  68.203 1.000 349.346 0 28  ILE DDD O   1 ? 9  
ATOM 6996  C CB  . ILE F 4 27  ? 11.554  65.500  68.853 1.000 362.253 0 28  ILE DDD CB  1 ? 9  
ATOM 6997  C CG1 . ILE F 4 27  ? 11.725  63.983  68.702 1.000 341.017 0 28  ILE DDD CG1 1 ? 9  
ATOM 6998  C CG2 . ILE F 4 27  ? 11.236  66.142  67.524 1.000 357.148 0 28  ILE DDD CG2 1 ? 9  
ATOM 6999  C CD1 . ILE F 4 27  ? 11.906  63.231  69.988 1.000 337.521 0 28  ILE DDD CD1 1 ? 9  
ATOM 7000  N N   . SER F 4 28  ? 14.131  67.506  67.950 1.000 344.381 0 29  SER DDD N   1 ? 9  
ATOM 7001  C CA  . SER F 4 28  ? 15.193  67.753  66.977 1.000 328.275 0 29  SER DDD CA  1 ? 9  
ATOM 7002  C C   . SER F 4 28  ? 16.577  67.636  67.599 1.000 323.052 0 29  SER DDD C   1 ? 9  
ATOM 7003  O O   . SER F 4 28  ? 17.572  67.630  66.866 1.000 307.523 0 29  SER DDD O   1 ? 9  
ATOM 7004  C CB  . SER F 4 28  ? 15.033  69.127  66.329 1.000 314.470 0 29  SER DDD CB  1 ? 9  
ATOM 7005  O OG  . SER F 4 28  ? 15.063  70.161  67.295 1.000 321.930 0 29  SER DDD OG  1 ? 9  
ATOM 7006  N N   . ARG F 4 29  ? 16.654  67.533  68.927 1.000 330.067 0 30  ARG DDD N   1 ? 9  
ATOM 7007  C CA  . ARG F 4 29  ? 17.915  67.418  69.642 1.000 323.042 0 30  ARG DDD CA  1 ? 9  
ATOM 7008  C C   . ARG F 4 29  ? 18.463  66.002  69.584 1.000 314.703 0 30  ARG DDD C   1 ? 9  
ATOM 7009  O O   . ARG F 4 29  ? 19.675  65.805  69.715 1.000 299.674 0 30  ARG DDD O   1 ? 9  
ATOM 7010  C CB  . ARG F 4 29  ? 17.637  67.768  71.102 1.000 335.220 0 30  ARG DDD CB  1 ? 9  
ATOM 7011  C CG  . ARG F 4 29  ? 16.957  69.107  71.325 1.000 347.749 0 30  ARG DDD CG  1 ? 9  
ATOM 7012  C CD  . ARG F 4 29  ? 16.813  69.338  72.812 1.000 348.306 0 30  ARG DDD CD  1 ? 9  
ATOM 7013  N NE  . ARG F 4 29  ? 16.307  68.102  73.402 1.000 346.322 0 30  ARG DDD NE  1 ? 9  
ATOM 7014  C CZ  . ARG F 4 29  ? 16.100  67.892  74.694 1.000 338.293 0 30  ARG DDD CZ  1 ? 9  
ATOM 7015  N NH1 . ARG F 4 29  ? 16.341  68.833  75.591 1.000 330.485 0 30  ARG DDD NH1 1 ? 9  
ATOM 7016  N NH2 . ARG F 4 29  ? 15.627  66.713  75.092 1.000 327.212 0 30  ARG DDD NH2 1 ? 9  
ATOM 7017  N N   . PHE F 4 30  ? 17.584  65.033  69.360 1.000 326.304 0 31  PHE DDD N   1 ? 9  
ATOM 7018  C CA  . PHE F 4 30  ? 17.919  63.622  69.243 1.000 324.210 0 31  PHE DDD CA  1 ? 9  
ATOM 7019  C C   . PHE F 4 30  ? 18.671  63.375  67.939 1.000 318.439 0 31  PHE DDD C   1 ? 9  
ATOM 7020  O O   . PHE F 4 30  ? 18.402  64.004  66.913 1.000 313.733 0 31  PHE DDD O   1 ? 9  
ATOM 7021  C CB  . PHE F 4 30  ? 16.679  62.745  69.404 1.000 330.047 0 31  PHE DDD CB  1 ? 9  
ATOM 7022  C CG  . PHE F 4 30  ? 16.018  62.895  70.753 1.000 334.792 0 31  PHE DDD CG  1 ? 9  
ATOM 7023  C CD1 . PHE F 4 30  ? 15.153  63.941  71.017 1.000 349.335 0 31  PHE DDD CD1 1 ? 9  
ATOM 7024  C CD2 . PHE F 4 30  ? 16.304  61.998  71.774 1.000 335.303 0 31  PHE DDD CD2 1 ? 9  
ATOM 7025  C CE1 . PHE F 4 30  ? 14.565  64.077  72.265 1.000 356.865 0 31  PHE DDD CE1 1 ? 9  
ATOM 7026  C CE2 . PHE F 4 30  ? 15.721  62.130  73.022 1.000 343.993 0 31  PHE DDD CE2 1 ? 9  
ATOM 7027  C CZ  . PHE F 4 30  ? 14.850  63.170  73.267 1.000 350.879 0 31  PHE DDD CZ  1 ? 9  
ATOM 7028  N N   . ASN F 4 31  ? 19.618  62.442  67.983 1.000 298.079 0 32  ASN DDD N   1 ? 9  
ATOM 7029  C CA  . ASN F 4 31  ? 20.430  62.109  66.820 1.000 272.916 0 32  ASN DDD CA  1 ? 9  
ATOM 7030  C C   . ASN F 4 31  ? 19.792  61.056  65.923 1.000 265.226 0 32  ASN DDD C   1 ? 9  
ATOM 7031  O O   . ASN F 4 31  ? 20.222  60.908  64.774 1.000 252.160 0 32  ASN DDD O   1 ? 9  
ATOM 7032  C CB  . ASN F 4 31  ? 21.790  61.548  67.264 1.000 248.781 0 32  ASN DDD CB  1 ? 9  
ATOM 7033  C CG  . ASN F 4 31  ? 22.606  62.524  68.100 1.000 245.127 0 32  ASN DDD CG  1 ? 9  
ATOM 7034  O OD1 . ASN F 4 31  ? 22.270  63.699  68.214 1.000 265.180 0 32  ASN DDD OD1 1 ? 9  
ATOM 7035  N ND2 . ASN F 4 31  ? 23.693  62.027  68.695 1.000 224.607 0 32  ASN DDD ND2 1 ? 9  
ATOM 7036  N N   . ALA F 4 32  ? 18.765  60.358  66.397 1.000 273.720 0 33  ALA DDD N   1 ? 9  
ATOM 7037  C CA  . ALA F 4 32  ? 18.049  59.390  65.586 1.000 282.486 0 33  ALA DDD CA  1 ? 9  
ATOM 7038  C C   . ALA F 4 32  ? 16.724  59.103  66.271 1.000 301.480 0 33  ALA DDD C   1 ? 9  
ATOM 7039  O O   . ALA F 4 32  ? 16.651  59.061  67.500 1.000 331.591 0 33  ALA DDD O   1 ? 9  
ATOM 7040  C CB  . ALA F 4 32  ? 18.865  58.122  65.383 1.000 274.402 0 33  ALA DDD CB  1 ? 9  
ATOM 7041  N N   . MET F 4 33  ? 15.673  58.915  65.479 1.000 295.236 0 34  MET DDD N   1 ? 9  
ATOM 7042  C CA  . MET F 4 33  ? 14.398  58.486  66.040 1.000 285.093 0 34  MET DDD CA  1 ? 9  
ATOM 7043  C C   . MET F 4 33  ? 13.779  57.443  65.112 1.000 266.097 0 34  MET DDD C   1 ? 9  
ATOM 7044  O O   . MET F 4 33  ? 14.133  57.345  63.935 1.000 253.296 0 34  MET DDD O   1 ? 9  
ATOM 7045  C CB  . MET F 4 33  ? 13.431  59.692  66.277 1.000 298.474 0 34  MET DDD CB  1 ? 9  
ATOM 7046  C CG  . MET F 4 33  ? 13.989  60.948  67.017 1.000 313.040 0 34  MET DDD CG  1 ? 9  
ATOM 7047  S SD  . MET F 4 33  ? 15.276  61.928  66.226 1.000 323.609 0 34  MET DDD SD  1 ? 9  
ATOM 7048  C CE  . MET F 4 33  ? 14.389  62.879  65.017 1.000 318.129 0 34  MET DDD CE  1 ? 9  
ATOM 7049  N N   . GLY F 4 34  ? 12.831  56.677  65.639 1.000 282.424 0 35  GLY DDD N   1 ? 9  
ATOM 7050  C CA  . GLY F 4 34  ? 12.188  55.670  64.821 1.000 282.026 0 35  GLY DDD CA  1 ? 9  
ATOM 7051  C C   . GLY F 4 34  ? 11.088  54.919  65.546 1.000 299.515 0 35  GLY DDD C   1 ? 9  
ATOM 7052  O O   . GLY F 4 34  ? 10.664  55.298  66.638 1.000 309.547 0 35  GLY DDD O   1 ? 9  
ATOM 7053  N N   . TRP F 4 35  ? 10.622  53.841  64.892 1.000 302.234 0 36  TRP DDD N   1 ? 9  
ATOM 7054  C CA  . TRP F 4 35  ? 9.460   53.040  65.287 1.000 312.061 0 36  TRP DDD CA  1 ? 9  
ATOM 7055  C C   . TRP F 4 35  ? 9.695   51.532  65.246 1.000 310.305 0 36  TRP DDD C   1 ? 9  
ATOM 7056  O O   . TRP F 4 35  ? 10.257  51.006  64.278 1.000 307.782 0 36  TRP DDD O   1 ? 9  
ATOM 7057  C CB  . TRP F 4 35  ? 8.252   53.347  64.396 1.000 325.458 0 36  TRP DDD CB  1 ? 9  
ATOM 7058  C CG  . TRP F 4 35  ? 7.549   54.626  64.626 1.000 348.840 0 36  TRP DDD CG  1 ? 9  
ATOM 7059  C CD1 . TRP F 4 35  ? 7.662   55.782  63.916 1.000 358.740 0 36  TRP DDD CD1 1 ? 9  
ATOM 7060  C CD2 . TRP F 4 35  ? 6.459   54.819  65.535 1.000 366.893 0 36  TRP DDD CD2 1 ? 9  
ATOM 7061  N NE1 . TRP F 4 35  ? 6.770   56.713  64.389 1.000 373.093 0 36  TRP DDD NE1 1 ? 9  
ATOM 7062  C CE2 . TRP F 4 35  ? 6.014   56.142  65.377 1.000 379.438 0 36  TRP DDD CE2 1 ? 9  
ATOM 7063  C CE3 . TRP F 4 35  ? 5.839   54.007  66.493 1.000 375.618 0 36  TRP DDD CE3 1 ? 9  
ATOM 7064  C CZ2 . TRP F 4 35  ? 4.978   56.677  66.141 1.000 399.009 0 36  TRP DDD CZ2 1 ? 9  
ATOM 7065  C CZ3 . TRP F 4 35  ? 4.812   54.540  67.251 1.000 395.295 0 36  TRP DDD CZ3 1 ? 9  
ATOM 7066  C CH2 . TRP F 4 35  ? 4.388   55.858  67.065 1.000 404.712 0 36  TRP DDD CH2 1 ? 9  
ATOM 7067  N N   . TRP F 4 36  ? 9.302   50.851  66.327 1.000 298.465 0 37  TRP DDD N   1 ? 9  
ATOM 7068  C CA  . TRP F 4 36  ? 9.220   49.392  66.422 1.000 294.818 0 37  TRP DDD CA  1 ? 9  
ATOM 7069  C C   . TRP F 4 36  ? 7.820   48.953  66.835 1.000 307.451 0 37  TRP DDD C   1 ? 9  
ATOM 7070  O O   . TRP F 4 36  ? 6.999   49.749  67.302 1.000 321.634 0 37  TRP DDD O   1 ? 9  
ATOM 7071  C CB  . TRP F 4 36  ? 10.240  48.784  67.398 1.000 287.442 0 37  TRP DDD CB  1 ? 9  
ATOM 7072  C CG  . TRP F 4 36  ? 11.623  48.562  66.878 1.000 280.263 0 37  TRP DDD CG  1 ? 9  
ATOM 7073  C CD1 . TRP F 4 36  ? 12.548  49.489  66.498 1.000 280.797 0 37  TRP DDD CD1 1 ? 9  
ATOM 7074  C CD2 . TRP F 4 36  ? 12.262  47.284  66.755 1.000 271.261 0 37  TRP DDD CD2 1 ? 9  
ATOM 7075  N NE1 . TRP F 4 36  ? 13.707  48.858  66.098 1.000 271.948 0 37  TRP DDD NE1 1 ? 9  
ATOM 7076  C CE2 . TRP F 4 36  ? 13.556  47.507  66.258 1.000 260.814 0 37  TRP DDD CE2 1 ? 9  
ATOM 7077  C CE3 . TRP F 4 36  ? 11.853  45.967  67.007 1.000 267.193 0 37  TRP DDD CE3 1 ? 9  
ATOM 7078  C CZ2 . TRP F 4 36  ? 14.448  46.468  66.005 1.000 242.461 0 37  TRP DDD CZ2 1 ? 9  
ATOM 7079  C CZ3 . TRP F 4 36  ? 12.741  44.937  66.756 1.000 252.659 0 37  TRP DDD CZ3 1 ? 9  
ATOM 7080  C CH2 . TRP F 4 36  ? 14.022  45.193  66.260 1.000 238.640 0 37  TRP DDD CH2 1 ? 9  
ATOM 7081  N N   . ARG F 4 37  ? 7.531   47.675  66.606 1.000 307.785 0 38  ARG DDD N   1 ? 9  
ATOM 7082  C CA  . ARG F 4 37  ? 6.277   47.063  67.017 1.000 303.053 0 38  ARG DDD CA  1 ? 9  
ATOM 7083  C C   . ARG F 4 37  ? 6.494   45.624  67.464 1.000 301.614 0 38  ARG DDD C   1 ? 9  
ATOM 7084  O O   . ARG F 4 37  ? 7.452   44.969  67.046 1.000 318.283 0 38  ARG DDD O   1 ? 9  
ATOM 7085  C CB  . ARG F 4 37  ? 5.249   47.109  65.884 1.000 297.195 0 38  ARG DDD CB  1 ? 9  
ATOM 7086  C CG  . ARG F 4 37  ? 5.616   46.239  64.700 1.000 280.828 0 38  ARG DDD CG  1 ? 9  
ATOM 7087  C CD  . ARG F 4 37  ? 4.580   46.354  63.601 1.000 271.427 0 38  ARG DDD CD  1 ? 9  
ATOM 7088  N NE  . ARG F 4 37  ? 4.867   45.480  62.471 1.000 257.849 0 38  ARG DDD NE  1 ? 9  
ATOM 7089  C CZ  . ARG F 4 37  ? 4.265   45.565  61.293 1.000 256.994 0 38  ARG DDD CZ  1 ? 9  
ATOM 7090  N NH1 . ARG F 4 37  ? 3.337   46.478  61.056 1.000 267.603 0 38  ARG DDD NH1 1 ? 9  
ATOM 7091  N NH2 . ARG F 4 37  ? 4.603   44.719  60.326 1.000 244.775 0 38  ARG DDD NH2 1 ? 9  
ATOM 7092  N N   . GLN F 4 38  ? 5.598   45.133  68.321 1.000 291.088 0 39  GLN DDD N   1 ? 9  
ATOM 7093  C CA  . GLN F 4 38  ? 5.621   43.726  68.712 1.000 277.220 0 39  GLN DDD CA  1 ? 9  
ATOM 7094  C C   . GLN F 4 38  ? 4.176   43.261  68.745 1.000 284.486 0 39  GLN DDD C   1 ? 9  
ATOM 7095  O O   . GLN F 4 38  ? 3.348   43.846  69.448 1.000 287.274 0 39  GLN DDD O   1 ? 9  
ATOM 7096  C CB  . GLN F 4 38  ? 6.281   43.502  70.075 1.000 263.820 0 39  GLN DDD CB  1 ? 9  
ATOM 7097  C CG  . GLN F 4 38  ? 6.471   42.022  70.399 1.000 254.652 0 39  GLN DDD CG  1 ? 9  
ATOM 7098  C CD  . GLN F 4 38  ? 7.173   41.778  71.720 1.000 242.689 0 39  GLN DDD CD  1 ? 9  
ATOM 7099  O OE1 . GLN F 4 38  ? 7.662   42.708  72.360 1.000 239.791 0 39  GLN DDD OE1 1 ? 9  
ATOM 7100  N NE2 . GLN F 4 38  ? 7.220   40.518  72.139 1.000 239.351 0 39  GLN DDD NE2 1 ? 9  
ATOM 7101  N N   . ALA F 4 39  ? 3.876   42.190  67.975 1.000 304.936 0 40  ALA DDD N   1 ? 9  
ATOM 7102  C CA  . ALA F 4 39  ? 2.636   41.450  67.828 1.000 303.371 0 40  ALA DDD CA  1 ? 9  
ATOM 7103  C C   . ALA F 4 39  ? 2.630   40.175  68.662 1.000 299.808 0 40  ALA DDD C   1 ? 9  
ATOM 7104  O O   . ALA F 4 39  ? 3.691   39.618  68.968 1.000 321.509 0 40  ALA DDD O   1 ? 9  
ATOM 7105  C CB  . ALA F 4 39  ? 2.405   41.086  66.358 1.000 299.400 0 40  ALA DDD CB  1 ? 9  
ATOM 7106  N N   . PRO F 4 40  ? 1.446   39.725  69.077 1.000 268.388 0 41  PRO DDD N   1 ? 9  
ATOM 7107  C CA  . PRO F 4 40  ? 1.359   38.502  69.888 1.000 261.578 0 41  PRO DDD CA  1 ? 9  
ATOM 7108  C C   . PRO F 4 40  ? 1.964   37.349  69.103 1.000 257.832 0 41  PRO DDD C   1 ? 9  
ATOM 7109  O O   . PRO F 4 40  ? 1.530   37.040  67.991 1.000 258.135 0 41  PRO DDD O   1 ? 9  
ATOM 7110  C CB  . PRO F 4 40  ? -0.146  38.330  70.106 1.000 260.417 0 41  PRO DDD CB  1 ? 9  
ATOM 7111  C CG  . PRO F 4 40  ? -0.680  39.723  70.043 1.000 261.612 0 41  PRO DDD CG  1 ? 9  
ATOM 7112  C CD  . PRO F 4 40  ? 0.149   40.422  68.997 1.000 262.811 0 41  PRO DDD CD  1 ? 9  
ATOM 7113  N N   . GLY F 4 41  ? 2.976   36.713  69.678 1.000 261.168 0 42  GLY DDD N   1 ? 9  
ATOM 7114  C CA  . GLY F 4 41  ? 3.605   35.600  68.998 1.000 246.453 0 42  GLY DDD CA  1 ? 9  
ATOM 7115  C C   . GLY F 4 41  ? 4.698   36.074  68.065 1.000 260.997 0 42  GLY DDD C   1 ? 9  
ATOM 7116  O O   . GLY F 4 41  ? 5.854   35.681  68.238 1.000 258.724 0 42  GLY DDD O   1 ? 9  
ATOM 7117  N N   . LYS F 4 42  ? 4.374   36.918  67.083 1.000 256.214 0 43  LYS DDD N   1 ? 9  
ATOM 7118  C CA  . LYS F 4 42  ? 5.412   37.357  66.161 1.000 257.725 0 43  LYS DDD CA  1 ? 9  
ATOM 7119  C C   . LYS F 4 42  ? 6.477   38.128  66.924 1.000 261.608 0 43  LYS DDD C   1 ? 9  
ATOM 7120  O O   . LYS F 4 42  ? 6.210   38.777  67.940 1.000 264.642 0 43  LYS DDD O   1 ? 9  
ATOM 7121  C CB  . LYS F 4 42  ? 4.842   38.188  65.012 1.000 254.529 0 43  LYS DDD CB  1 ? 9  
ATOM 7122  C CG  . LYS F 4 42  ? 3.930   37.403  64.085 1.000 246.359 0 43  LYS DDD CG  1 ? 9  
ATOM 7123  C CD  . LYS F 4 42  ? 4.737   36.239  63.511 1.000 236.449 0 43  LYS DDD CD  1 ? 9  
ATOM 7124  C CE  . LYS F 4 42  ? 3.900   35.218  62.767 1.000 231.131 0 43  LYS DDD CE  1 ? 9  
ATOM 7125  N NZ  . LYS F 4 42  ? 2.878   35.866  61.912 1.000 232.299 0 43  LYS DDD NZ  1 ? 9  
ATOM 7126  N N   . GLU F 4 43  ? 7.694   38.049  66.414 1.000 260.897 0 44  GLU DDD N   1 ? 9  
ATOM 7127  C CA  . GLU F 4 43  ? 8.823   38.687  67.054 1.000 263.240 0 44  GLU DDD CA  1 ? 9  
ATOM 7128  C C   . GLU F 4 43  ? 8.794   40.198  66.816 1.000 272.251 0 44  GLU DDD C   1 ? 9  
ATOM 7129  O O   . GLU F 4 43  ? 8.228   40.673  65.829 1.000 281.695 0 44  GLU DDD O   1 ? 9  
ATOM 7130  C CB  . GLU F 4 43  ? 10.098  38.058  66.494 1.000 254.176 0 44  GLU DDD CB  1 ? 9  
ATOM 7131  C CG  . GLU F 4 43  ? 10.090  36.521  66.715 1.000 249.062 0 44  GLU DDD CG  1 ? 9  
ATOM 7132  C CD  . GLU F 4 43  ? 10.301  36.077  68.157 1.000 254.605 0 44  GLU DDD CD  1 ? 9  
ATOM 7133  O OE1 . GLU F 4 43  ? 11.138  36.666  68.865 1.000 267.347 0 44  GLU DDD OE1 1 ? 9  
ATOM 7134  O OE2 . GLU F 4 43  ? 9.591   35.148  68.600 1.000 246.410 0 44  GLU DDD OE2 1 ? 9  
ATOM 7135  N N   . ARG F 4 44  ? 9.373   40.957  67.756 1.000 270.527 0 45  ARG DDD N   1 ? 9  
ATOM 7136  C CA  . ARG F 4 44  ? 9.453   42.411  67.602 1.000 270.237 0 45  ARG DDD CA  1 ? 9  
ATOM 7137  C C   . ARG F 4 44  ? 10.052  42.783  66.248 1.000 274.754 0 45  ARG DDD C   1 ? 9  
ATOM 7138  O O   . ARG F 4 44  ? 11.146  42.334  65.891 1.000 278.552 0 45  ARG DDD O   1 ? 9  
ATOM 7139  C CB  . ARG F 4 44  ? 10.261  43.020  68.753 1.000 261.832 0 45  ARG DDD CB  1 ? 9  
ATOM 7140  C CG  . ARG F 4 44  ? 9.619   44.286  69.327 1.000 263.087 0 45  ARG DDD CG  1 ? 9  
ATOM 7141  C CD  . ARG F 4 44  ? 10.489  45.011  70.351 1.000 256.326 0 45  ARG DDD CD  1 ? 9  
ATOM 7142  N NE  . ARG F 4 44  ? 10.684  44.218  71.560 1.000 251.486 0 45  ARG DDD NE  1 ? 9  
ATOM 7143  C CZ  . ARG F 4 44  ? 11.452  44.570  72.582 1.000 247.429 0 45  ARG DDD CZ  1 ? 9  
ATOM 7144  N NH1 . ARG F 4 44  ? 12.122  45.711  72.567 1.000 249.584 0 45  ARG DDD NH1 1 ? 9  
ATOM 7145  N NH2 . ARG F 4 44  ? 11.540  43.768  73.638 1.000 243.256 0 45  ARG DDD NH2 1 ? 9  
ATOM 7146  N N   . GLU F 4 45  ? 9.326   43.620  65.506 1.000 292.668 0 46  GLU DDD N   1 ? 9  
ATOM 7147  C CA  . GLU F 4 45  ? 9.710   44.072  64.173 1.000 287.668 0 46  GLU DDD CA  1 ? 9  
ATOM 7148  C C   . GLU F 4 45  ? 9.960   45.580  64.114 1.000 284.475 0 46  GLU DDD C   1 ? 9  
ATOM 7149  O O   . GLU F 4 45  ? 9.262   46.362  64.767 1.000 288.779 0 46  GLU DDD O   1 ? 9  
ATOM 7150  C CB  . GLU F 4 45  ? 8.640   43.656  63.148 1.000 287.596 0 46  GLU DDD CB  1 ? 9  
ATOM 7151  C CG  . GLU F 4 45  ? 9.212   43.314  61.769 1.000 288.995 0 46  GLU DDD CG  1 ? 9  
ATOM 7152  C CD  . GLU F 4 45  ? 9.596   44.527  60.959 1.000 290.889 0 46  GLU DDD CD  1 ? 9  
ATOM 7153  O OE1 . GLU F 4 45  ? 8.734   45.414  60.812 1.000 301.264 0 46  GLU DDD OE1 1 ? 9  
ATOM 7154  O OE2 . GLU F 4 45  ? 10.756  44.597  60.488 1.000 287.315 0 46  GLU DDD OE2 1 ? 9  
ATOM 7155  N N   . PHE F 4 46  ? 10.954  45.979  63.316 1.000 272.278 0 47  PHE DDD N   1 ? 9  
ATOM 7156  C CA  . PHE F 4 46  ? 11.345  47.379  63.150 1.000 262.811 0 47  PHE DDD CA  1 ? 9  
ATOM 7157  C C   . PHE F 4 46  ? 10.382  48.048  62.168 1.000 258.795 0 47  PHE DDD C   1 ? 9  
ATOM 7158  O O   . PHE F 4 46  ? 10.036  47.459  61.142 1.000 262.954 0 47  PHE DDD O   1 ? 9  
ATOM 7159  C CB  . PHE F 4 46  ? 12.786  47.477  62.642 1.000 259.024 0 47  PHE DDD CB  1 ? 9  
ATOM 7160  C CG  . PHE F 4 46  ? 13.140  48.823  62.055 1.000 270.641 0 47  PHE DDD CG  1 ? 9  
ATOM 7161  C CD1 . PHE F 4 46  ? 13.502  49.893  62.861 1.000 292.566 0 47  PHE DDD CD1 1 ? 9  
ATOM 7162  C CD2 . PHE F 4 46  ? 13.064  49.021  60.685 1.000 275.888 0 47  PHE DDD CD2 1 ? 9  
ATOM 7163  C CE1 . PHE F 4 46  ? 13.813  51.125  62.300 1.000 303.285 0 47  PHE DDD CE1 1 ? 9  
ATOM 7164  C CE2 . PHE F 4 46  ? 13.363  50.243  60.125 1.000 286.326 0 47  PHE DDD CE2 1 ? 9  
ATOM 7165  C CZ  . PHE F 4 46  ? 13.737  51.295  60.928 1.000 299.863 0 47  PHE DDD CZ  1 ? 9  
ATOM 7166  N N   . VAL F 4 47  ? 9.920   49.263  62.485 1.000 261.031 0 48  VAL DDD N   1 ? 9  
ATOM 7167  C CA  . VAL F 4 47  ? 8.901   49.949  61.680 1.000 258.268 0 48  VAL DDD CA  1 ? 9  
ATOM 7168  C C   . VAL F 4 47  ? 9.462   51.163  60.937 1.000 252.538 0 48  VAL DDD C   1 ? 9  
ATOM 7169  O O   . VAL F 4 47  ? 9.387   51.233  59.708 1.000 244.294 0 48  VAL DDD O   1 ? 9  
ATOM 7170  C CB  . VAL F 4 47  ? 7.693   50.350  62.556 1.000 268.239 0 48  VAL DDD CB  1 ? 9  
ATOM 7171  C CG1 . VAL F 4 47  ? 6.623   51.072  61.733 1.000 270.532 0 48  VAL DDD CG1 1 ? 9  
ATOM 7172  C CG2 . VAL F 4 47  ? 7.131   49.135  63.248 1.000 271.879 0 48  VAL DDD CG2 1 ? 9  
ATOM 7173  N N   . ALA F 4 48  ? 10.024  52.131  61.657 1.000 255.626 0 49  ALA DDD N   1 ? 9  
ATOM 7174  C CA  . ALA F 4 48  ? 10.449  53.326  60.939 1.000 255.618 0 49  ALA DDD CA  1 ? 9  
ATOM 7175  C C   . ALA F 4 48  ? 11.691  53.934  61.560 1.000 254.767 0 49  ALA DDD C   1 ? 9  
ATOM 7176  O O   . ALA F 4 48  ? 12.008  53.703  62.727 1.000 265.645 0 49  ALA DDD O   1 ? 9  
ATOM 7177  C CB  . ALA F 4 48  ? 9.334   54.376  60.925 1.000 259.837 0 49  ALA DDD CB  1 ? 9  
ATOM 7178  N N   . ARG F 4 49  ? 12.417  54.679  60.729 1.000 238.707 0 50  ARG DDD N   1 ? 9  
ATOM 7179  C CA  . ARG F 4 49  ? 13.649  55.346  61.129 1.000 240.723 0 50  ARG DDD CA  1 ? 9  
ATOM 7180  C C   . ARG F 4 49  ? 13.778  56.669  60.387 1.000 235.260 0 50  ARG DDD C   1 ? 9  
ATOM 7181  O O   . ARG F 4 49  ? 13.394  56.780  59.220 1.000 228.554 0 50  ARG DDD O   1 ? 9  
ATOM 7182  C CB  . ARG F 4 49  ? 14.917  54.511  60.967 1.000 249.736 0 50  ARG DDD CB  1 ? 9  
ATOM 7183  C CG  . ARG F 4 49  ? 15.467  54.330  59.597 1.000 246.868 0 50  ARG DDD CG  1 ? 9  
ATOM 7184  C CD  . ARG F 4 49  ? 16.773  53.612  59.775 1.000 221.984 0 50  ARG DDD CD  1 ? 9  
ATOM 7185  N NE  . ARG F 4 49  ? 17.248  52.990  58.555 1.000 204.679 0 50  ARG DDD NE  1 ? 9  
ATOM 7186  C CZ  . ARG F 4 49  ? 17.859  51.818  58.532 1.000 213.196 0 50  ARG DDD CZ  1 ? 9  
ATOM 7187  N NH1 . ARG F 4 49  ? 18.063  51.123  59.645 1.000 210.497 0 50  ARG DDD NH1 1 ? 9  
ATOM 7188  N NH2 . ARG F 4 49  ? 18.256  51.318  57.367 1.000 223.098 0 50  ARG DDD NH2 1 ? 9  
ATOM 7189  N N   . ILE F 4 50  ? 14.276  57.673  61.096 1.000 234.655 0 51  ILE DDD N   1 ? 9  
ATOM 7190  C CA  . ILE F 4 50  ? 14.700  58.954  60.537 1.000 233.539 0 51  ILE DDD CA  1 ? 9  
ATOM 7191  C C   . ILE F 4 50  ? 16.056  59.276  61.158 1.000 243.914 0 51  ILE DDD C   1 ? 9  
ATOM 7192  O O   . ILE F 4 50  ? 16.176  59.390  62.385 1.000 254.320 0 51  ILE DDD O   1 ? 9  
ATOM 7193  C CB  . ILE F 4 50  ? 13.666  60.055  60.812 1.000 236.244 0 51  ILE DDD CB  1 ? 9  
ATOM 7194  C CG1 . ILE F 4 50  ? 14.020  61.378  60.115 1.000 230.364 0 51  ILE DDD CG1 1 ? 9  
ATOM 7195  C CG2 . ILE F 4 50  ? 13.489  60.204  62.280 1.000 252.749 0 51  ILE DDD CG2 1 ? 9  
ATOM 7196  C CD1 . ILE F 4 50  ? 13.960  61.370  58.610 1.000 218.601 0 51  ILE DDD CD1 1 ? 9  
ATOM 7197  N N   . VAL F 4 51  ? 17.084  59.394  60.326 1.000 243.060 0 52  VAL DDD N   1 ? 9  
ATOM 7198  C CA  . VAL F 4 51  ? 18.392  59.817  60.803 1.000 234.434 0 52  VAL DDD CA  1 ? 9  
ATOM 7199  C C   . VAL F 4 51  ? 18.696  61.244  60.372 1.000 238.296 0 52  VAL DDD C   1 ? 9  
ATOM 7200  O O   . VAL F 4 51  ? 18.368  61.659  59.253 1.000 243.064 0 52  VAL DDD O   1 ? 9  
ATOM 7201  C CB  . VAL F 4 51  ? 19.460  58.843  60.273 1.000 212.069 0 52  VAL DDD CB  1 ? 9  
ATOM 7202  C CG1 . VAL F 4 51  ? 20.829  59.190  60.822 1.000 204.893 0 52  VAL DDD CG1 1 ? 9  
ATOM 7203  C CG2 . VAL F 4 51  ? 19.053  57.402  60.572 1.000 211.435 0 52  VAL DDD CG2 1 ? 9  
ATOM 7204  N N   . LYS F 4 52  ? 19.304  61.997  61.290 1.000 241.102 0 53  LYS DDD N   1 ? 9  
ATOM 7205  C CA  . LYS F 4 52  ? 19.523  63.426  61.107 1.000 241.792 0 53  LYS DDD CA  1 ? 9  
ATOM 7206  C C   . LYS F 4 52  ? 20.390  63.714  59.891 1.000 240.888 0 53  LYS DDD C   1 ? 9  
ATOM 7207  O O   . LYS F 4 52  ? 21.501  63.190  59.767 1.000 234.307 0 53  LYS DDD O   1 ? 9  
ATOM 7208  C CB  . LYS F 4 52  ? 20.148  64.033  62.359 1.000 241.301 0 53  LYS DDD CB  1 ? 9  
ATOM 7209  C CG  . LYS F 4 52  ? 19.110  64.531  63.341 1.000 246.781 0 53  LYS DDD CG  1 ? 9  
ATOM 7210  C CD  . LYS F 4 52  ? 19.615  65.716  64.142 1.000 250.865 0 53  LYS DDD CD  1 ? 9  
ATOM 7211  C CE  . LYS F 4 52  ? 20.670  65.312  65.155 1.000 258.069 0 53  LYS DDD CE  1 ? 9  
ATOM 7212  N NZ  . LYS F 4 52  ? 20.833  66.354  66.208 1.000 270.253 0 53  LYS DDD NZ  1 ? 9  
ATOM 7213  N N   . GLY F 4 53  ? 19.865  64.538  58.994 1.000 255.417 0 54  GLY DDD N   1 ? 9  
ATOM 7214  C CA  . GLY F 4 53  ? 20.515  64.919  57.763 1.000 252.586 0 54  GLY DDD CA  1 ? 9  
ATOM 7215  C C   . GLY F 4 53  ? 20.276  63.976  56.611 1.000 252.478 0 54  GLY DDD C   1 ? 9  
ATOM 7216  O O   . GLY F 4 53  ? 20.668  64.289  55.480 1.000 257.993 0 54  GLY DDD O   1 ? 9  
ATOM 7217  N N   . PHE F 4 54  ? 19.653  62.833  56.859 1.000 239.699 0 55  PHE DDD N   1 ? 9  
ATOM 7218  C CA  . PHE F 4 54  ? 19.461  61.820  55.839 1.000 226.839 0 55  PHE DDD CA  1 ? 9  
ATOM 7219  C C   . PHE F 4 54  ? 17.974  61.742  55.525 1.000 225.097 0 55  PHE DDD C   1 ? 9  
ATOM 7220  O O   . PHE F 4 54  ? 17.136  62.215  56.298 1.000 226.831 0 55  PHE DDD O   1 ? 9  
ATOM 7221  C CB  . PHE F 4 54  ? 19.997  60.458  56.304 1.000 217.651 0 55  PHE DDD CB  1 ? 9  
ATOM 7222  C CG  . PHE F 4 54  ? 21.502  60.401  56.430 1.000 209.462 0 55  PHE DDD CG  1 ? 9  
ATOM 7223  C CD1 . PHE F 4 54  ? 22.310  60.141  55.331 1.000 210.193 0 55  PHE DDD CD1 1 ? 9  
ATOM 7224  C CD2 . PHE F 4 54  ? 22.107  60.623  57.656 1.000 208.182 0 55  PHE DDD CD2 1 ? 9  
ATOM 7225  C CE1 . PHE F 4 54  ? 23.695  60.093  55.462 1.000 201.827 0 55  PHE DDD CE1 1 ? 9  
ATOM 7226  C CE2 . PHE F 4 54  ? 23.484  60.580  57.791 1.000 202.673 0 55  PHE DDD CE2 1 ? 9  
ATOM 7227  C CZ  . PHE F 4 54  ? 24.275  60.318  56.691 1.000 203.137 0 55  PHE DDD CZ  1 ? 9  
ATOM 7228  N N   . ASP F 4 55  ? 17.644  61.148  54.384 1.000 212.147 0 56  ASP DDD N   1 ? 9  
ATOM 7229  C CA  . ASP F 4 55  ? 16.241  60.940  54.073 1.000 213.115 0 56  ASP DDD CA  1 ? 9  
ATOM 7230  C C   . ASP F 4 55  ? 15.687  59.842  54.983 1.000 209.767 0 56  ASP DDD C   1 ? 9  
ATOM 7231  O O   . ASP F 4 55  ? 16.436  58.990  55.470 1.000 210.966 0 56  ASP DDD O   1 ? 9  
ATOM 7232  C CB  . ASP F 4 55  ? 16.053  60.651  52.587 1.000 216.962 0 56  ASP DDD CB  1 ? 9  
ATOM 7233  C CG  . ASP F 4 55  ? 16.712  61.710  51.714 1.000 220.659 0 56  ASP DDD CG  1 ? 9  
ATOM 7234  O OD1 . ASP F 4 55  ? 16.701  62.890  52.129 1.000 220.679 0 56  ASP DDD OD1 1 ? 9  
ATOM 7235  O OD2 . ASP F 4 55  ? 17.243  61.376  50.634 1.000 222.202 0 56  ASP DDD OD2 1 ? 9  
ATOM 7236  N N   . PRO F 4 56  ? 14.375  59.831  55.219 1.000 214.028 0 57  PRO DDD N   1 ? 9  
ATOM 7237  C CA  . PRO F 4 56  ? 13.786  58.737  56.004 1.000 216.428 0 57  PRO DDD CA  1 ? 9  
ATOM 7238  C C   . PRO F 4 56  ? 13.780  57.381  55.312 1.000 217.402 0 57  PRO DDD C   1 ? 9  
ATOM 7239  O O   . PRO F 4 56  ? 13.481  57.250  54.122 1.000 216.880 0 57  PRO DDD O   1 ? 9  
ATOM 7240  C CB  . PRO F 4 56  ? 12.355  59.224  56.261 1.000 222.297 0 57  PRO DDD CB  1 ? 9  
ATOM 7241  C CG  . PRO F 4 56  ? 12.085  60.225  55.201 1.000 219.309 0 57  PRO DDD CG  1 ? 9  
ATOM 7242  C CD  . PRO F 4 56  ? 13.398  60.890  54.920 1.000 215.412 0 57  PRO DDD CD  1 ? 9  
ATOM 7243  N N   . VAL F 4 57  ? 14.116  56.367  56.106 1.000 218.322 0 58  VAL DDD N   1 ? 9  
ATOM 7244  C CA  . VAL F 4 57  ? 14.057  54.957  55.744 1.000 226.298 0 58  VAL DDD CA  1 ? 9  
ATOM 7245  C C   . VAL F 4 57  ? 13.009  54.273  56.615 1.000 235.943 0 58  VAL DDD C   1 ? 9  
ATOM 7246  O O   . VAL F 4 57  ? 12.933  54.516  57.824 1.000 236.270 0 58  VAL DDD O   1 ? 9  
ATOM 7247  C CB  . VAL F 4 57  ? 15.428  54.259  55.850 1.000 230.579 0 58  VAL DDD CB  1 ? 9  
ATOM 7248  C CG1 . VAL F 4 57  ? 15.294  52.772  55.534 1.000 225.870 0 58  VAL DDD CG1 1 ? 9  
ATOM 7249  C CG2 . VAL F 4 57  ? 16.410  54.902  54.886 1.000 231.817 0 58  VAL DDD CG2 1 ? 9  
ATOM 7250  N N   . LEU F 4 58  ? 12.198  53.430  55.995 1.000 247.943 0 59  LEU DDD N   1 ? 9  
ATOM 7251  C CA  . LEU F 4 58  ? 11.102  52.693  56.607 1.000 253.336 0 59  LEU DDD CA  1 ? 9  
ATOM 7252  C C   . LEU F 4 58  ? 11.382  51.225  56.329 1.000 259.986 0 59  LEU DDD C   1 ? 9  
ATOM 7253  O O   . LEU F 4 58  ? 12.096  50.890  55.379 1.000 267.593 0 59  LEU DDD O   1 ? 9  
ATOM 7254  C CB  . LEU F 4 58  ? 9.720   53.123  56.097 1.000 254.069 0 59  LEU DDD CB  1 ? 9  
ATOM 7255  C CG  . LEU F 4 58  ? 9.338   54.567  56.435 1.000 249.868 0 59  LEU DDD CG  1 ? 9  
ATOM 7256  C CD1 . LEU F 4 58  ? 9.486   55.484  55.228 1.000 246.679 0 59  LEU DDD CD1 1 ? 9  
ATOM 7257  C CD2 . LEU F 4 58  ? 7.936   54.631  57.021 1.000 274.379 0 59  LEU DDD CD2 1 ? 9  
ATOM 7258  N N   . ALA F 4 59  ? 10.836  50.338  57.160 1.000 255.641 0 60  ALA DDD N   1 ? 9  
ATOM 7259  C CA  . ALA F 4 59  ? 11.072  48.931  56.882 1.000 253.515 0 60  ALA DDD CA  1 ? 9  
ATOM 7260  C C   . ALA F 4 59  ? 10.420  48.530  55.566 1.000 261.737 0 60  ALA DDD C   1 ? 9  
ATOM 7261  O O   . ALA F 4 59  ? 9.438   49.117  55.113 1.000 269.032 0 60  ALA DDD O   1 ? 9  
ATOM 7262  C CB  . ALA F 4 59  ? 10.547  48.062  58.024 1.000 246.375 0 60  ALA DDD CB  1 ? 9  
ATOM 7263  N N   . ASP F 4 60  ? 10.946  47.439  55.008 1.000 255.403 0 61  ASP DDD N   1 ? 9  
ATOM 7264  C CA  . ASP F 4 60  ? 10.553  46.960  53.688 1.000 261.508 0 61  ASP DDD CA  1 ? 9  
ATOM 7265  C C   . ASP F 4 60  ? 9.127   46.430  53.608 1.000 274.398 0 61  ASP DDD C   1 ? 9  
ATOM 7266  O O   . ASP F 4 60  ? 8.489   46.587  52.560 1.000 293.695 0 61  ASP DDD O   1 ? 9  
ATOM 7267  C CB  . ASP F 4 60  ? 11.562  45.906  53.224 1.000 247.851 0 61  ASP DDD CB  1 ? 9  
ATOM 7268  C CG  . ASP F 4 60  ? 12.938  46.508  52.924 1.000 239.655 0 61  ASP DDD CG  1 ? 9  
ATOM 7269  O OD1 . ASP F 4 60  ? 13.142  47.712  53.190 1.000 248.077 0 61  ASP DDD OD1 1 ? 9  
ATOM 7270  O OD2 . ASP F 4 60  ? 13.809  45.783  52.398 1.000 225.624 0 61  ASP DDD OD2 1 ? 9  
ATOM 7271  N N   . SER F 4 61  ? 8.590   45.813  54.660 1.000 272.360 0 62  SER DDD N   1 ? 9  
ATOM 7272  C CA  . SER F 4 61  ? 7.221   45.357  54.466 1.000 265.194 0 62  SER DDD CA  1 ? 9  
ATOM 7273  C C   . SER F 4 61  ? 6.227   46.512  54.386 1.000 273.290 0 62  SER DDD C   1 ? 9  
ATOM 7274  O O   . SER F 4 61  ? 5.047   46.269  54.108 1.000 276.879 0 62  SER DDD O   1 ? 9  
ATOM 7275  C CB  . SER F 4 61  ? 6.823   44.398  55.588 1.000 251.441 0 62  SER DDD CB  1 ? 9  
ATOM 7276  O OG  . SER F 4 61  ? 6.961   45.016  56.855 1.000 254.478 0 62  SER DDD OG  1 ? 9  
ATOM 7277  N N   . VAL F 4 62  ? 6.675   47.751  54.632 1.000 286.188 0 63  VAL DDD N   1 ? 9  
ATOM 7278  C CA  . VAL F 4 62  ? 5.807   48.925  54.717 1.000 291.533 0 63  VAL DDD CA  1 ? 9  
ATOM 7279  C C   . VAL F 4 62  ? 6.403   50.079  53.905 1.000 301.693 0 63  VAL DDD C   1 ? 9  
ATOM 7280  O O   . VAL F 4 62  ? 5.764   51.122  53.727 1.000 300.697 0 63  VAL DDD O   1 ? 9  
ATOM 7281  C CB  . VAL F 4 62  ? 5.560   49.338  56.182 1.000 291.068 0 63  VAL DDD CB  1 ? 9  
ATOM 7282  C CG1 . VAL F 4 62  ? 4.909   48.191  56.955 1.000 291.858 0 63  VAL DDD CG1 1 ? 9  
ATOM 7283  C CG2 . VAL F 4 62  ? 6.851   49.811  56.856 1.000 280.457 0 63  VAL DDD CG2 1 ? 9  
ATOM 7284  N N   . LYS F 4 63  ? 7.640   49.889  53.423 1.000 320.366 0 64  LYS DDD N   1 ? 9  
ATOM 7285  C CA  . LYS F 4 63  ? 8.469   50.975  52.885 1.000 316.739 0 64  LYS DDD CA  1 ? 9  
ATOM 7286  C C   . LYS F 4 63  ? 7.786   51.740  51.756 1.000 323.365 0 64  LYS DDD C   1 ? 9  
ATOM 7287  O O   . LYS F 4 63  ? 7.860   52.973  51.692 1.000 347.985 0 64  LYS DDD O   1 ? 9  
ATOM 7288  C CB  . LYS F 4 63  ? 9.807   50.417  52.400 1.000 291.533 0 64  LYS DDD CB  1 ? 9  
ATOM 7289  C CG  . LYS F 4 63  ? 10.683  51.418  51.672 1.000 273.270 0 64  LYS DDD CG  1 ? 9  
ATOM 7290  C CD  . LYS F 4 63  ? 11.127  52.531  52.606 1.000 266.170 0 64  LYS DDD CD  1 ? 9  
ATOM 7291  C CE  . LYS F 4 63  ? 11.822  53.638  51.837 1.000 254.619 0 64  LYS DDD CE  1 ? 9  
ATOM 7292  N NZ  . LYS F 4 63  ? 12.162  54.801  52.699 1.000 244.131 0 64  LYS DDD NZ  1 ? 9  
ATOM 7293  N N   . GLY F 4 64  ? 7.119   51.021  50.854 1.000 306.918 0 65  GLY DDD N   1 ? 9  
ATOM 7294  C CA  . GLY F 4 64  ? 6.464   51.630  49.709 1.000 291.941 0 65  GLY DDD CA  1 ? 9  
ATOM 7295  C C   . GLY F 4 64  ? 5.205   52.410  50.021 1.000 283.882 0 65  GLY DDD C   1 ? 9  
ATOM 7296  O O   . GLY F 4 64  ? 4.795   53.244  49.206 1.000 286.081 0 65  GLY DDD O   1 ? 9  
ATOM 7297  N N   . ARG F 4 65  ? 4.585   52.163  51.172 1.000 300.296 0 66  ARG DDD N   1 ? 9  
ATOM 7298  C CA  . ARG F 4 65  ? 3.231   52.618  51.475 1.000 308.486 0 66  ARG DDD CA  1 ? 9  
ATOM 7299  C C   . ARG F 4 65  ? 3.129   53.669  52.583 1.000 327.141 0 66  ARG DDD C   1 ? 9  
ATOM 7300  O O   . ARG F 4 65  ? 2.198   54.472  52.550 1.000 328.022 0 66  ARG DDD O   1 ? 9  
ATOM 7301  C CB  . ARG F 4 65  ? 2.312   51.411  51.739 1.000 306.101 0 66  ARG DDD CB  1 ? 9  
ATOM 7302  C CG  . ARG F 4 65  ? 2.688   50.373  52.784 1.000 310.648 0 66  ARG DDD CG  1 ? 9  
ATOM 7303  C CD  . ARG F 4 65  ? 1.471   49.449  52.934 1.000 291.459 0 66  ARG DDD CD  1 ? 9  
ATOM 7304  N NE  . ARG F 4 65  ? 1.648   48.346  53.870 1.000 289.767 0 66  ARG DDD NE  1 ? 9  
ATOM 7305  C CZ  . ARG F 4 65  ? 0.919   48.162  54.962 1.000 303.962 0 66  ARG DDD CZ  1 ? 9  
ATOM 7306  N NH1 . ARG F 4 65  ? -0.057  48.991  55.290 1.000 313.748 0 66  ARG DDD NH1 1 ? 9  
ATOM 7307  N NH2 . ARG F 4 65  ? 1.168   47.110  55.736 1.000 302.113 0 66  ARG DDD NH2 1 ? 9  
ATOM 7308  N N   . PHE F 4 66  ? 4.054   53.713  53.536 1.000 342.238 0 67  PHE DDD N   1 ? 9  
ATOM 7309  C CA  . PHE F 4 66  ? 4.034   54.628  54.678 1.000 347.920 0 67  PHE DDD CA  1 ? 9  
ATOM 7310  C C   . PHE F 4 66  ? 4.981   55.812  54.476 1.000 343.473 0 67  PHE DDD C   1 ? 9  
ATOM 7311  O O   . PHE F 4 66  ? 5.929   55.754  53.689 1.000 343.033 0 67  PHE DDD O   1 ? 9  
ATOM 7312  C CB  . PHE F 4 66  ? 4.435   53.926  55.982 1.000 348.414 0 67  PHE DDD CB  1 ? 9  
ATOM 7313  C CG  . PHE F 4 66  ? 3.460   52.895  56.466 1.000 358.886 0 67  PHE DDD CG  1 ? 9  
ATOM 7314  C CD1 . PHE F 4 66  ? 2.345   52.552  55.725 1.000 365.805 0 67  PHE DDD CD1 1 ? 9  
ATOM 7315  C CD2 . PHE F 4 66  ? 3.664   52.275  57.688 1.000 359.299 0 67  PHE DDD CD2 1 ? 9  
ATOM 7316  C CE1 . PHE F 4 66  ? 1.458   51.605  56.187 1.000 369.208 0 67  PHE DDD CE1 1 ? 9  
ATOM 7317  C CE2 . PHE F 4 66  ? 2.780   51.328  58.156 1.000 367.751 0 67  PHE DDD CE2 1 ? 9  
ATOM 7318  C CZ  . PHE F 4 66  ? 1.675   50.991  57.403 1.000 370.884 0 67  PHE DDD CZ  1 ? 9  
ATOM 7319  N N   . THR F 4 67  ? 4.696   56.905  55.203 1.000 325.454 0 68  THR DDD N   1 ? 9  
ATOM 7320  C CA  . THR F 4 67  ? 5.565   58.078  55.238 1.000 315.060 0 68  THR DDD CA  1 ? 9  
ATOM 7321  C C   . THR F 4 67  ? 5.681   58.557  56.680 1.000 315.299 0 68  THR DDD C   1 ? 9  
ATOM 7322  O O   . THR F 4 67  ? 4.715   58.527  57.442 1.000 313.642 0 68  THR DDD O   1 ? 9  
ATOM 7323  C CB  . THR F 4 67  ? 4.994   59.215  54.375 1.000 306.760 0 68  THR DDD CB  1 ? 9  
ATOM 7324  O OG1 . THR F 4 67  ? 4.529   58.690  53.125 1.000 310.672 0 68  THR DDD OG1 1 ? 9  
ATOM 7325  C CG2 . THR F 4 67  ? 6.039   60.294  54.125 1.000 292.506 0 68  THR DDD CG2 1 ? 9  
ATOM 7326  N N   . ILE F 4 68  ? 6.892   58.986  57.036 1.000 306.782 0 69  ILE DDD N   1 ? 9  
ATOM 7327  C CA  . ILE F 4 68  ? 7.262   59.498  58.354 1.000 299.315 0 69  ILE DDD CA  1 ? 9  
ATOM 7328  C C   . ILE F 4 68  ? 7.781   60.938  58.339 1.000 293.880 0 69  ILE DDD C   1 ? 9  
ATOM 7329  O O   . ILE F 4 68  ? 8.595   61.289  57.478 1.000 300.696 0 69  ILE DDD O   1 ? 9  
ATOM 7330  C CB  . ILE F 4 68  ? 8.324   58.550  58.946 1.000 290.894 0 69  ILE DDD CB  1 ? 9  
ATOM 7331  C CG1 . ILE F 4 68  ? 8.868   59.029  60.272 1.000 288.504 0 69  ILE DDD CG1 1 ? 9  
ATOM 7332  C CG2 . ILE F 4 68  ? 9.450   58.281  57.954 1.000 278.632 0 69  ILE DDD CG2 1 ? 9  
ATOM 7333  C CD1 . ILE F 4 68  ? 9.713   57.962  60.925 1.000 283.024 0 69  ILE DDD CD1 1 ? 9  
ATOM 7334  N N   . SER F 4 69  ? 7.312   61.784  59.274 1.000 286.606 0 70  SER DDD N   1 ? 9  
ATOM 7335  C CA  . SER F 4 69  ? 7.810   63.161  59.284 1.000 277.654 0 70  SER DDD CA  1 ? 9  
ATOM 7336  C C   . SER F 4 69  ? 8.006   63.596  60.737 1.000 287.795 0 70  SER DDD C   1 ? 9  
ATOM 7337  O O   . SER F 4 69  ? 7.377   63.055  61.647 1.000 288.949 0 70  SER DDD O   1 ? 9  
ATOM 7338  C CB  . SER F 4 69  ? 6.828   64.128  58.588 1.000 267.584 0 70  SER DDD CB  1 ? 9  
ATOM 7339  O OG  . SER F 4 69  ? 5.505   64.032  59.108 1.000 277.197 0 70  SER DDD OG  1 ? 9  
ATOM 7340  N N   . ILE F 4 70  ? 8.861   64.607  60.955 1.000 294.705 0 71  ILE DDD N   1 ? 9  
ATOM 7341  C CA  . ILE F 4 70  ? 9.119   65.134  62.301 1.000 304.812 0 71  ILE DDD CA  1 ? 9  
ATOM 7342  C C   . ILE F 4 70  ? 9.016   66.654  62.425 1.000 311.487 0 71  ILE DDD C   1 ? 9  
ATOM 7343  O O   . ILE F 4 70  ? 9.601   67.400  61.628 1.000 317.834 0 71  ILE DDD O   1 ? 9  
ATOM 7344  C CB  . ILE F 4 70  ? 10.445  64.635  62.910 1.000 308.322 0 71  ILE DDD CB  1 ? 9  
ATOM 7345  C CG1 . ILE F 4 70  ? 10.355  63.133  63.177 1.000 307.517 0 71  ILE DDD CG1 1 ? 9  
ATOM 7346  C CG2 . ILE F 4 70  ? 10.782  65.390  64.179 1.000 309.400 0 71  ILE DDD CG2 1 ? 9  
ATOM 7347  C CD1 . ILE F 4 70  ? 11.624  62.513  63.459 1.000 306.844 0 71  ILE DDD CD1 1 ? 9  
ATOM 7348  N N   . ASP F 4 71  ? 8.268   67.092  63.430 1.000 314.368 0 72  ASP DDD N   1 ? 9  
ATOM 7349  C CA  . ASP F 4 71  ? 8.068   68.487  63.814 1.000 315.219 0 72  ASP DDD CA  1 ? 9  
ATOM 7350  C C   . ASP F 4 71  ? 8.682   68.663  65.200 1.000 321.244 0 72  ASP DDD C   1 ? 9  
ATOM 7351  O O   . ASP F 4 71  ? 8.137   68.149  66.182 1.000 327.499 0 72  ASP DDD O   1 ? 9  
ATOM 7352  C CB  . ASP F 4 71  ? 6.640   68.999  63.792 1.000 314.385 0 72  ASP DDD CB  1 ? 9  
ATOM 7353  C CG  . ASP F 4 71  ? 6.598   70.493  64.117 1.000 316.707 0 72  ASP DDD CG  1 ? 9  
ATOM 7354  O OD1 . ASP F 4 71  ? 7.593   71.182  63.808 1.000 308.822 0 72  ASP DDD OD1 1 ? 9  
ATOM 7355  O OD2 . ASP F 4 71  ? 5.611   71.006  64.644 1.000 323.487 0 72  ASP DDD OD2 1 ? 9  
ATOM 7356  N N   . SER F 4 72  ? 9.803   69.375  65.303 1.000 323.147 0 73  SER DDD N   1 ? 9  
ATOM 7357  C CA  . SER F 4 72  ? 10.413  69.538  66.619 1.000 323.099 0 73  SER DDD CA  1 ? 9  
ATOM 7358  C C   . SER F 4 72  ? 9.525   70.408  67.491 1.000 324.603 0 73  SER DDD C   1 ? 9  
ATOM 7359  O O   . SER F 4 72  ? 9.673   70.405  68.717 1.000 328.439 0 73  SER DDD O   1 ? 9  
ATOM 7360  C CB  . SER F 4 72  ? 11.798  70.176  66.517 1.000 321.256 0 73  SER DDD CB  1 ? 9  
ATOM 7361  O OG  . SER F 4 72  ? 11.729  71.520  66.068 1.000 317.759 0 73  SER DDD OG  1 ? 9  
ATOM 7362  N N   . ALA F 4 73  ? 8.637   71.176  66.868 1.000 316.076 0 74  ALA DDD N   1 ? 9  
ATOM 7363  C CA  . ALA F 4 73  ? 7.688   72.003  67.599 1.000 328.862 0 74  ALA DDD CA  1 ? 9  
ATOM 7364  C C   . ALA F 4 73  ? 6.759   71.134  68.454 1.000 342.613 0 74  ALA DDD C   1 ? 9  
ATOM 7365  O O   . ALA F 4 73  ? 6.568   71.413  69.644 1.000 358.214 0 74  ALA DDD O   1 ? 9  
ATOM 7366  C CB  . ALA F 4 73  ? 6.893   72.878  66.634 1.000 325.922 0 74  ALA DDD CB  1 ? 9  
ATOM 7367  N N   . GLU F 4 74  ? 6.169   70.067  67.882 1.000 358.069 0 75  GLU DDD N   1 ? 9  
ATOM 7368  C CA  . GLU F 4 74  ? 5.303   69.233  68.718 1.000 362.653 0 75  GLU DDD CA  1 ? 9  
ATOM 7369  C C   . GLU F 4 74  ? 6.017   68.103  69.441 1.000 357.223 0 75  GLU DDD C   1 ? 9  
ATOM 7370  O O   . GLU F 4 74  ? 5.350   67.360  70.165 1.000 375.978 0 75  GLU DDD O   1 ? 9  
ATOM 7371  C CB  . GLU F 4 74  ? 4.238   68.443  67.916 1.000 363.132 0 75  GLU DDD CB  1 ? 9  
ATOM 7372  C CG  . GLU F 4 74  ? 3.061   69.021  67.113 1.000 362.556 0 75  GLU DDD CG  1 ? 9  
ATOM 7373  C CD  . GLU F 4 74  ? 3.423   69.545  65.743 1.000 357.280 0 75  GLU DDD CD  1 ? 9  
ATOM 7374  O OE1 . GLU F 4 74  ? 3.655   68.709  64.842 1.000 354.706 0 75  GLU DDD OE1 1 ? 9  
ATOM 7375  O OE2 . GLU F 4 74  ? 3.350   70.770  65.525 1.000 357.345 0 75  GLU DDD OE2 1 ? 9  
ATOM 7376  N N   . ASN F 4 75  ? 7.327   67.936  69.268 1.000 330.522 0 76  ASN DDD N   1 ? 9  
ATOM 7377  C CA  . ASN F 4 75  ? 8.069   66.852  69.917 1.000 320.321 0 76  ASN DDD CA  1 ? 9  
ATOM 7378  C C   . ASN F 4 75  ? 7.444   65.509  69.553 1.000 306.179 0 76  ASN DDD C   1 ? 9  
ATOM 7379  O O   . ASN F 4 75  ? 7.254   64.640  70.407 1.000 294.993 0 76  ASN DDD O   1 ? 9  
ATOM 7380  C CB  . ASN F 4 75  ? 8.104   67.022  71.438 1.000 321.316 0 76  ASN DDD CB  1 ? 9  
ATOM 7381  C CG  . ASN F 4 75  ? 8.596   68.380  71.860 1.000 332.311 0 76  ASN DDD CG  1 ? 9  
ATOM 7382  O OD1 . ASN F 4 75  ? 9.219   69.095  71.079 1.000 334.745 0 76  ASN DDD OD1 1 ? 9  
ATOM 7383  N ND2 . ASN F 4 75  ? 8.335   68.742  73.111 1.000 335.845 0 76  ASN DDD ND2 1 ? 9  
ATOM 7384  N N   . THR F 4 76  ? 7.116   65.337  68.281 1.000 311.640 0 77  THR DDD N   1 ? 9  
ATOM 7385  C CA  . THR F 4 76  ? 6.385   64.161  67.846 1.000 304.169 0 77  THR DDD CA  1 ? 9  
ATOM 7386  C C   . THR F 4 76  ? 7.037   63.554  66.621 1.000 300.741 0 77  THR DDD C   1 ? 9  
ATOM 7387  O O   . THR F 4 76  ? 7.714   64.238  65.847 1.000 298.574 0 77  THR DDD O   1 ? 9  
ATOM 7388  C CB  . THR F 4 76  ? 4.909   64.459  67.512 1.000 302.273 0 77  THR DDD CB  1 ? 9  
ATOM 7389  O OG1 . THR F 4 76  ? 4.831   65.525  66.560 1.000 305.458 0 77  THR DDD OG1 1 ? 9  
ATOM 7390  C CG2 . THR F 4 76  ? 4.140   64.846  68.765 1.000 303.773 0 77  THR DDD CG2 1 ? 9  
ATOM 7391  N N   . LEU F 4 77  ? 6.828   62.256  66.466 1.000 292.531 0 78  LEU DDD N   1 ? 9  
ATOM 7392  C CA  . LEU F 4 77  ? 7.323   61.518  65.322 1.000 292.105 0 78  LEU DDD CA  1 ? 9  
ATOM 7393  C C   . LEU F 4 77  ? 6.041   61.092  64.624 1.000 301.145 0 78  LEU DDD C   1 ? 9  
ATOM 7394  O O   . LEU F 4 77  ? 5.255   60.318  65.183 1.000 320.060 0 78  LEU DDD O   1 ? 9  
ATOM 7395  C CB  . LEU F 4 77  ? 8.196   60.334  65.747 1.000 294.972 0 78  LEU DDD CB  1 ? 9  
ATOM 7396  C CG  . LEU F 4 77  ? 8.554   59.273  64.715 1.000 295.358 0 78  LEU DDD CG  1 ? 9  
ATOM 7397  C CD1 . LEU F 4 77  ? 8.830   59.979  63.434 1.000 281.654 0 78  LEU DDD CD1 1 ? 9  
ATOM 7398  C CD2 . LEU F 4 77  ? 9.788   58.499  65.144 1.000 291.064 0 78  LEU DDD CD2 1 ? 9  
ATOM 7399  N N   . ALA F 4 78  ? 5.842   61.580  63.401 1.000 299.489 0 79  ALA DDD N   1 ? 9  
ATOM 7400  C CA  . ALA F 4 78  ? 4.584   61.388  62.684 1.000 298.780 0 79  ALA DDD CA  1 ? 9  
ATOM 7401  C C   . ALA F 4 78  ? 4.778   60.333  61.604 1.000 292.726 0 79  ALA DDD C   1 ? 9  
ATOM 7402  O O   . ALA F 4 78  ? 5.022   60.629  60.434 1.000 287.034 0 79  ALA DDD O   1 ? 9  
ATOM 7403  C CB  . ALA F 4 78  ? 4.097   62.713  62.105 1.000 292.432 0 79  ALA DDD CB  1 ? 9  
ATOM 7404  N N   . LEU F 4 79  ? 4.648   59.077  62.018 1.000 295.061 0 80  LEU DDD N   1 ? 9  
ATOM 7405  C CA  . LEU F 4 79  ? 4.567   57.971  61.075 1.000 294.339 0 80  LEU DDD CA  1 ? 9  
ATOM 7406  C C   . LEU F 4 79  ? 3.189   57.940  60.432 1.000 302.648 0 80  LEU DDD C   1 ? 9  
ATOM 7407  O O   . LEU F 4 79  ? 2.198   57.593  61.083 1.000 312.529 0 80  LEU DDD O   1 ? 9  
ATOM 7408  C CB  . LEU F 4 79  ? 4.847   56.659  61.801 1.000 296.766 0 80  LEU DDD CB  1 ? 9  
ATOM 7409  C CG  . LEU F 4 79  ? 4.712   55.347  61.027 1.000 294.863 0 80  LEU DDD CG  1 ? 9  
ATOM 7410  C CD1 . LEU F 4 79  ? 5.944   55.068  60.205 1.000 297.566 0 80  LEU DDD CD1 1 ? 9  
ATOM 7411  C CD2 . LEU F 4 79  ? 4.444   54.200  61.993 1.000 298.120 0 80  LEU DDD CD2 1 ? 9  
ATOM 7412  N N   . GLN F 4 80  ? 3.122   58.300  59.155 1.000 310.568 0 81  GLN DDD N   1 ? 9  
ATOM 7413  C CA  . GLN F 4 80  ? 1.872   58.264  58.409 1.000 332.738 0 81  GLN DDD CA  1 ? 9  
ATOM 7414  C C   . GLN F 4 80  ? 1.761   56.899  57.751 1.000 353.307 0 81  GLN DDD C   1 ? 9  
ATOM 7415  O O   . GLN F 4 80  ? 2.639   56.502  56.975 1.000 360.377 0 81  GLN DDD O   1 ? 9  
ATOM 7416  C CB  . GLN F 4 80  ? 1.782   59.377  57.366 1.000 322.418 0 81  GLN DDD CB  1 ? 9  
ATOM 7417  C CG  . GLN F 4 80  ? 0.516   59.286  56.514 1.000 315.650 0 81  GLN DDD CG  1 ? 9  
ATOM 7418  C CD  . GLN F 4 80  ? -0.727  59.819  57.206 1.000 307.165 0 81  GLN DDD CD  1 ? 9  
ATOM 7419  O OE1 . GLN F 4 80  ? -0.705  60.879  57.835 1.000 301.618 0 81  GLN DDD OE1 1 ? 9  
ATOM 7420  N NE2 . GLN F 4 80  ? -1.819  59.068  57.107 1.000 306.824 0 81  GLN DDD NE2 1 ? 9  
ATOM 7421  N N   . ARG F 4 81  ? 0.694   56.190  58.061 1.000 357.820 0 82  ARG DDD N   1 ? 9  
ATOM 7422  C CA  . ARG F 4 81  ? 0.461   54.845  57.563 1.000 349.911 0 82  ARG DDD CA  1 ? 9  
ATOM 7423  C C   . ARG F 4 81  ? -0.552  54.938  56.428 1.000 357.924 0 82  ARG DDD C   1 ? 9  
ATOM 7424  O O   . ARG F 4 81  ? -1.734  55.204  56.669 1.000 361.695 0 82  ARG DDD O   1 ? 9  
ATOM 7425  C CB  . ARG F 4 81  ? -0.047  53.967  58.701 1.000 332.591 0 82  ARG DDD CB  1 ? 9  
ATOM 7426  C CG  . ARG F 4 81  ? 0.253   54.535  60.081 1.000 322.280 0 82  ARG DDD CG  1 ? 9  
ATOM 7427  C CD  . ARG F 4 81  ? 0.174   53.475  61.138 1.000 316.924 0 82  ARG DDD CD  1 ? 9  
ATOM 7428  N NE  . ARG F 4 81  ? 1.084   52.376  60.861 1.000 321.464 0 82  ARG DDD NE  1 ? 9  
ATOM 7429  C CZ  . ARG F 4 81  ? 1.141   51.263  61.575 1.000 333.888 0 82  ARG DDD CZ  1 ? 9  
ATOM 7430  N NH1 . ARG F 4 81  ? 0.370   51.084  62.635 1.000 342.353 0 82  ARG DDD NH1 1 ? 9  
ATOM 7431  N NH2 . ARG F 4 81  ? 1.978   50.299  61.205 1.000 331.616 0 82  ARG DDD NH2 1 ? 9  
ATOM 7432  N N   . ASN F 4 82  A -0.100  54.749  55.192 1.000 359.416 0 82  ASN DDD N   1 ? 9  
ATOM 7433  C CA  . ASN F 4 82  A -1.030  54.807  54.078 1.000 356.886 0 82  ASN DDD CA  1 ? 9  
ATOM 7434  C C   . ASN F 4 82  A -1.224  53.399  53.533 1.000 353.127 0 82  ASN DDD C   1 ? 9  
ATOM 7435  O O   . ASN F 4 82  A -0.395  52.513  53.759 1.000 359.053 0 82  ASN DDD O   1 ? 9  
ATOM 7436  C CB  . ASN F 4 82  A -0.477  55.710  52.968 1.000 345.993 0 82  ASN DDD CB  1 ? 9  
ATOM 7437  C CG  . ASN F 4 82  A -0.213  57.126  53.439 1.000 345.245 0 82  ASN DDD CG  1 ? 9  
ATOM 7438  O OD1 . ASN F 4 82  A 0.856   57.413  53.982 1.000 339.221 0 82  ASN DDD OD1 1 ? 9  
ATOM 7439  N ND2 . ASN F 4 82  A -1.166  58.019  53.219 1.000 347.142 0 82  ASN DDD ND2 1 ? 9  
ATOM 7440  N N   . ARG F 4 83  B -2.319  53.203  52.797 1.000 330.902 0 82  ARG DDD N   1 ? 9  
ATOM 7441  C CA  . ARG F 4 83  B -2.621  51.904  52.195 1.000 313.763 0 82  ARG DDD CA  1 ? 9  
ATOM 7442  C C   . ARG F 4 83  B -2.625  50.814  53.269 1.000 312.905 0 82  ARG DDD C   1 ? 9  
ATOM 7443  O O   . ARG F 4 83  B -2.022  49.751  53.109 1.000 314.143 0 82  ARG DDD O   1 ? 9  
ATOM 7444  C CB  . ARG F 4 83  B -1.647  51.583  51.056 1.000 303.682 0 82  ARG DDD CB  1 ? 9  
ATOM 7445  C CG  . ARG F 4 83  B -1.604  52.648  49.957 1.000 289.155 0 82  ARG DDD CG  1 ? 9  
ATOM 7446  C CD  . ARG F 4 83  B -0.371  52.511  49.070 1.000 276.523 0 82  ARG DDD CD  1 ? 9  
ATOM 7447  N NE  . ARG F 4 83  B -0.614  52.986  47.712 1.000 260.852 0 82  ARG DDD NE  1 ? 9  
ATOM 7448  C CZ  . ARG F 4 83  B -0.939  52.211  46.681 1.000 253.872 0 82  ARG DDD CZ  1 ? 9  
ATOM 7449  N NH1 . ARG F 4 83  B -1.068  50.899  46.824 1.000 257.640 0 82  ARG DDD NH1 1 ? 9  
ATOM 7450  N NH2 . ARG F 4 83  B -1.129  52.759  45.490 1.000 247.923 0 82  ARG DDD NH2 1 ? 9  
ATOM 7451  N N   . LEU F 4 84  C -3.318  51.080  54.376 1.000 314.325 0 82  LEU DDD N   1 ? 9  
ATOM 7452  C CA  . LEU F 4 84  C -3.232  50.197  55.534 1.000 315.266 0 82  LEU DDD CA  1 ? 9  
ATOM 7453  C C   . LEU F 4 84  C -3.835  48.817  55.311 1.000 313.683 0 82  LEU DDD C   1 ? 9  
ATOM 7454  O O   . LEU F 4 84  C -4.839  48.652  54.614 1.000 316.967 0 82  LEU DDD O   1 ? 9  
ATOM 7455  C CB  . LEU F 4 84  C -3.909  50.839  56.742 1.000 315.150 0 82  LEU DDD CB  1 ? 9  
ATOM 7456  C CG  . LEU F 4 84  C -3.093  51.930  57.416 1.000 318.534 0 82  LEU DDD CG  1 ? 9  
ATOM 7457  C CD1 . LEU F 4 84  C -3.899  52.629  58.492 1.000 310.319 0 82  LEU DDD CD1 1 ? 9  
ATOM 7458  C CD2 . LEU F 4 84  C -1.892  51.246  58.016 1.000 327.357 0 82  LEU DDD CD2 1 ? 9  
ATOM 7459  N N   . LYS F 4 85  ? -3.190  47.830  55.928 1.000 307.133 0 83  LYS DDD N   1 ? 9  
ATOM 7460  C CA  . LYS F 4 85  ? -3.501  46.412  55.897 1.000 295.476 0 83  LYS DDD CA  1 ? 9  
ATOM 7461  C C   . LYS F 4 85  ? -3.777  45.854  57.294 1.000 289.034 0 83  LYS DDD C   1 ? 9  
ATOM 7462  O O   . LYS F 4 85  ? -3.396  46.452  58.307 1.000 295.962 0 83  LYS DDD O   1 ? 9  
ATOM 7463  C CB  . LYS F 4 85  ? -2.358  45.625  55.236 1.000 287.017 0 83  LYS DDD CB  1 ? 9  
ATOM 7464  C CG  . LYS F 4 85  ? -2.498  45.477  53.726 1.000 279.753 0 83  LYS DDD CG  1 ? 9  
ATOM 7465  C CD  . LYS F 4 85  ? -1.595  46.410  52.945 1.000 277.759 0 83  LYS DDD CD  1 ? 9  
ATOM 7466  C CE  . LYS F 4 85  ? -2.075  46.541  51.506 1.000 271.309 0 83  LYS DDD CE  1 ? 9  
ATOM 7467  N NZ  . LYS F 4 85  ? -1.248  47.493  50.716 1.000 284.053 0 83  LYS DDD NZ  1 ? 9  
ATOM 7468  N N   . PRO F 4 86  ? -4.460  44.708  57.371 1.000 283.226 0 84  PRO DDD N   1 ? 9  
ATOM 7469  C CA  . PRO F 4 86  ? -4.681  44.022  58.661 1.000 280.363 0 84  PRO DDD CA  1 ? 9  
ATOM 7470  C C   . PRO F 4 86  ? -3.414  43.587  59.391 1.000 285.126 0 84  PRO DDD C   1 ? 9  
ATOM 7471  O O   . PRO F 4 86  ? -3.390  43.591  60.629 1.000 293.180 0 84  PRO DDD O   1 ? 9  
ATOM 7472  C CB  . PRO F 4 86  ? -5.547  42.818  58.264 1.000 262.576 0 84  PRO DDD CB  1 ? 9  
ATOM 7473  C CG  . PRO F 4 86  ? -6.246  43.270  57.027 1.000 260.844 0 84  PRO DDD CG  1 ? 9  
ATOM 7474  C CD  . PRO F 4 86  ? -5.233  44.081  56.286 1.000 269.128 0 84  PRO DDD CD  1 ? 9  
ATOM 7475  N N   . GLU F 4 87  ? -2.357  43.226  58.661 1.000 273.664 0 85  GLU DDD N   1 ? 9  
ATOM 7476  C CA  . GLU F 4 87  ? -1.072  42.814  59.232 1.000 274.366 0 85  GLU DDD CA  1 ? 9  
ATOM 7477  C C   . GLU F 4 87  ? -0.378  43.878  60.073 1.000 299.175 0 85  GLU DDD C   1 ? 9  
ATOM 7478  O O   . GLU F 4 87  ? 0.595   43.555  60.763 1.000 299.881 0 85  GLU DDD O   1 ? 9  
ATOM 7479  C CB  . GLU F 4 87  ? -0.124  42.377  58.123 1.000 258.380 0 85  GLU DDD CB  1 ? 9  
ATOM 7480  C CG  . GLU F 4 87  ? -0.527  41.095  57.429 1.000 248.776 0 85  GLU DDD CG  1 ? 9  
ATOM 7481  C CD  . GLU F 4 87  ? -1.094  41.344  56.051 1.000 245.090 0 85  GLU DDD CD  1 ? 9  
ATOM 7482  O OE1 . GLU F 4 87  ? -0.810  42.415  55.473 1.000 242.695 0 85  GLU DDD OE1 1 ? 9  
ATOM 7483  O OE2 . GLU F 4 87  ? -1.848  40.481  55.556 1.000 244.292 0 85  GLU DDD OE2 1 ? 9  
ATOM 7484  N N   . ASP F 4 88  ? -0.833  45.117  60.050 1.000 332.989 0 86  ASP DDD N   1 ? 9  
ATOM 7485  C CA  . ASP F 4 88  ? -0.193  46.110  60.896 1.000 352.086 0 86  ASP DDD CA  1 ? 9  
ATOM 7486  C C   . ASP F 4 88  ? -0.628  45.994  62.348 1.000 352.167 0 86  ASP DDD C   1 ? 9  
ATOM 7487  O O   . ASP F 4 88  ? -0.104  46.722  63.201 1.000 359.628 0 86  ASP DDD O   1 ? 9  
ATOM 7488  C CB  . ASP F 4 88  ? -0.485  47.516  60.373 1.000 379.663 0 86  ASP DDD CB  1 ? 9  
ATOM 7489  C CG  . ASP F 4 88  ? 0.126   47.772  59.012 1.000 385.582 0 86  ASP DDD CG  1 ? 9  
ATOM 7490  O OD1 . ASP F 4 88  ? 1.281   47.340  58.795 1.000 375.469 0 86  ASP DDD OD1 1 ? 9  
ATOM 7491  O OD2 . ASP F 4 88  ? -0.524  48.440  58.182 1.000 399.946 0 86  ASP DDD OD2 1 ? 9  
ATOM 7492  N N   . THR F 4 89  ? -1.591  45.120  62.645 1.000 337.497 0 87  THR DDD N   1 ? 9  
ATOM 7493  C CA  . THR F 4 89  ? -2.021  44.930  64.019 1.000 335.179 0 87  THR DDD CA  1 ? 9  
ATOM 7494  C C   . THR F 4 89  ? -0.867  44.421  64.876 1.000 335.446 0 87  THR DDD C   1 ? 9  
ATOM 7495  O O   . THR F 4 89  ? -0.315  43.344  64.622 1.000 336.366 0 87  THR DDD O   1 ? 9  
ATOM 7496  C CB  . THR F 4 89  ? -3.191  43.941  64.059 1.000 329.850 0 87  THR DDD CB  1 ? 9  
ATOM 7497  O OG1 . THR F 4 89  ? -4.272  44.428  63.251 1.000 329.487 0 87  THR DDD OG1 1 ? 9  
ATOM 7498  C CG2 . THR F 4 89  ? -3.670  43.694  65.490 1.000 324.997 0 87  THR DDD CG2 1 ? 9  
ATOM 7499  N N   . ALA F 4 90  ? -0.528  45.189  65.911 1.000 339.224 0 88  ALA DDD N   1 ? 9  
ATOM 7500  C CA  . ALA F 4 90  ? 0.567   44.904  66.836 1.000 335.510 0 88  ALA DDD CA  1 ? 9  
ATOM 7501  C C   . ALA F 4 90  ? 0.547   45.979  67.915 1.000 332.822 0 88  ALA DDD C   1 ? 9  
ATOM 7502  O O   . ALA F 4 90  ? -0.169  46.978  67.801 1.000 351.768 0 88  ALA DDD O   1 ? 9  
ATOM 7503  C CB  . ALA F 4 90  ? 1.928   44.871  66.142 1.000 334.678 0 88  ALA DDD CB  1 ? 9  
ATOM 7504  N N   . VAL F 4 91  ? 1.338   45.772  68.969 1.000 315.668 0 89  VAL DDD N   1 ? 9  
ATOM 7505  C CA  . VAL F 4 91  ? 1.609   46.859  69.902 1.000 309.537 0 89  VAL DDD CA  1 ? 9  
ATOM 7506  C C   . VAL F 4 91  ? 2.854   47.563  69.390 1.000 306.908 0 89  VAL DDD C   1 ? 9  
ATOM 7507  O O   . VAL F 4 91  ? 3.883   46.923  69.145 1.000 301.112 0 89  VAL DDD O   1 ? 9  
ATOM 7508  C CB  . VAL F 4 91  ? 1.825   46.335  71.332 1.000 295.570 0 89  VAL DDD CB  1 ? 9  
ATOM 7509  C CG1 . VAL F 4 91  ? 2.277   47.463  72.250 1.000 297.410 0 89  VAL DDD CG1 1 ? 9  
ATOM 7510  C CG2 . VAL F 4 91  ? 0.563   45.707  71.864 1.000 292.684 0 89  VAL DDD CG2 1 ? 9  
ATOM 7511  N N   . TYR F 4 92  ? 2.776   48.879  69.242 1.000 298.039 0 90  TYR DDD N   1 ? 9  
ATOM 7512  C CA  . TYR F 4 92  ? 3.856   49.646  68.638 1.000 296.277 0 90  TYR DDD CA  1 ? 9  
ATOM 7513  C C   . TYR F 4 92  ? 4.616   50.505  69.629 1.000 300.242 0 90  TYR DDD C   1 ? 9  
ATOM 7514  O O   . TYR F 4 92  ? 4.006   51.294  70.350 1.000 308.665 0 90  TYR DDD O   1 ? 9  
ATOM 7515  C CB  . TYR F 4 92  ? 3.330   50.596  67.559 1.000 303.582 0 90  TYR DDD CB  1 ? 9  
ATOM 7516  C CG  . TYR F 4 92  ? 2.912   49.977  66.261 1.000 309.350 0 90  TYR DDD CG  1 ? 9  
ATOM 7517  C CD1 . TYR F 4 92  ? 1.747   49.236  66.162 1.000 321.727 0 90  TYR DDD CD1 1 ? 9  
ATOM 7518  C CD2 . TYR F 4 92  ? 3.677   50.162  65.120 1.000 304.404 0 90  TYR DDD CD2 1 ? 9  
ATOM 7519  C CE1 . TYR F 4 92  ? 1.364   48.686  64.965 1.000 329.848 0 90  TYR DDD CE1 1 ? 9  
ATOM 7520  C CE2 . TYR F 4 92  ? 3.306   49.615  63.923 1.000 307.953 0 90  TYR DDD CE2 1 ? 9  
ATOM 7521  C CZ  . TYR F 4 92  ? 2.149   48.875  63.848 1.000 325.925 0 90  TYR DDD CZ  1 ? 9  
ATOM 7522  O OH  . TYR F 4 92  ? 1.770   48.326  62.646 1.000 345.214 0 90  TYR DDD OH  1 ? 9  
ATOM 7523  N N   . TYR F 4 93  ? 5.940   50.444  69.577 1.000 294.553 0 91  TYR DDD N   1 ? 9  
ATOM 7524  C CA  . TYR F 4 93  ? 6.768   51.250  70.456 1.000 302.870 0 91  TYR DDD CA  1 ? 9  
ATOM 7525  C C   . TYR F 4 93  ? 7.605   52.078  69.493 1.000 306.144 0 91  TYR DDD C   1 ? 9  
ATOM 7526  O O   . TYR F 4 93  ? 8.184   51.551  68.543 1.000 301.418 0 91  TYR DDD O   1 ? 9  
ATOM 7527  C CB  . TYR F 4 93  ? 7.662   50.442  71.434 1.000 294.473 0 91  TYR DDD CB  1 ? 9  
ATOM 7528  C CG  . TYR F 4 93  ? 6.983   49.370  72.271 1.000 291.839 0 91  TYR DDD CG  1 ? 9  
ATOM 7529  C CD1 . TYR F 4 93  ? 6.788   48.087  71.786 1.000 287.688 0 91  TYR DDD CD1 1 ? 9  
ATOM 7530  C CD2 . TYR F 4 93  ? 6.613   49.631  73.591 1.000 300.871 0 91  TYR DDD CD2 1 ? 9  
ATOM 7531  C CE1 . TYR F 4 93  ? 6.191   47.109  72.570 1.000 291.548 0 91  TYR DDD CE1 1 ? 9  
ATOM 7532  C CE2 . TYR F 4 93  ? 6.018   48.660  74.382 1.000 308.945 0 91  TYR DDD CE2 1 ? 9  
ATOM 7533  C CZ  . TYR F 4 93  ? 5.810   47.401  73.867 1.000 304.125 0 91  TYR DDD CZ  1 ? 9  
ATOM 7534  O OH  . TYR F 4 93  ? 5.223   46.428  74.647 1.000 307.777 0 91  TYR DDD OH  1 ? 9  
ATOM 7535  N N   . CYS F 4 94  ? 7.721   53.359  69.782 1.000 317.089 0 92  CYS DDD N   1 ? 9  
ATOM 7536  C CA  . CYS F 4 94  ? 8.666   54.233  69.119 1.000 315.574 0 92  CYS DDD CA  1 ? 9  
ATOM 7537  C C   . CYS F 4 94  ? 9.929   54.412  69.932 1.000 310.058 0 92  CYS DDD C   1 ? 9  
ATOM 7538  O O   . CYS F 4 94  ? 9.916   54.328  71.162 1.000 304.695 0 92  CYS DDD O   1 ? 9  
ATOM 7539  C CB  . CYS F 4 94  ? 8.025   55.579  68.833 1.000 324.359 0 92  CYS DDD CB  1 ? 9  
ATOM 7540  S SG  . CYS F 4 94  ? 7.317   56.346  70.249 1.000 334.395 0 92  CYS DDD SG  1 ? 9  
ATOM 7541  N N   . PHE F 4 95  ? 11.026  54.659  69.233 1.000 315.002 0 93  PHE DDD N   1 ? 9  
ATOM 7542  C CA  . PHE F 4 95  ? 12.261  54.962  69.916 1.000 306.963 0 93  PHE DDD CA  1 ? 9  
ATOM 7543  C C   . PHE F 4 95  ? 12.909  56.200  69.321 1.000 298.857 0 93  PHE DDD C   1 ? 9  
ATOM 7544  O O   . PHE F 4 95  ? 12.734  56.513  68.141 1.000 297.203 0 93  PHE DDD O   1 ? 9  
ATOM 7545  C CB  . PHE F 4 95  ? 13.242  53.776  69.810 1.000 308.698 0 93  PHE DDD CB  1 ? 9  
ATOM 7546  C CG  . PHE F 4 95  ? 13.804  53.555  68.433 1.000 321.716 0 93  PHE DDD CG  1 ? 9  
ATOM 7547  C CD1 . PHE F 4 95  ? 13.118  52.805  67.493 1.000 338.158 0 93  PHE DDD CD1 1 ? 9  
ATOM 7548  C CD2 . PHE F 4 95  ? 15.047  54.069  68.094 1.000 317.762 0 93  PHE DDD CD2 1 ? 9  
ATOM 7549  C CE1 . PHE F 4 95  ? 13.650  52.598  66.232 1.000 350.288 0 93  PHE DDD CE1 1 ? 9  
ATOM 7550  C CE2 . PHE F 4 95  ? 15.582  53.865  66.839 1.000 325.677 0 93  PHE DDD CE2 1 ? 9  
ATOM 7551  C CZ  . PHE F 4 95  ? 14.883  53.129  65.906 1.000 336.895 0 93  PHE DDD CZ  1 ? 9  
ATOM 7552  N N   . ALA F 4 96  ? 13.657  56.904  70.158 1.000 293.629 0 94  ALA DDD N   1 ? 9  
ATOM 7553  C CA  . ALA F 4 96  ? 14.428  58.056  69.727 1.000 289.362 0 94  ALA DDD CA  1 ? 9  
ATOM 7554  C C   . ALA F 4 96  ? 15.802  57.846  70.334 1.000 283.049 0 94  ALA DDD C   1 ? 9  
ATOM 7555  O O   . ALA F 4 96  ? 15.918  57.432  71.495 1.000 289.386 0 94  ALA DDD O   1 ? 9  
ATOM 7556  C CB  . ALA F 4 96  ? 13.810  59.395  70.140 1.000 292.286 0 94  ALA DDD CB  1 ? 9  
ATOM 7557  N N   . ALA F 4 97  ? 16.827  58.211  69.572 1.000 275.834 0 95  ALA DDD N   1 ? 9  
ATOM 7558  C CA  . ALA F 4 97  ? 18.214  58.003  69.953 1.000 267.609 0 95  ALA DDD CA  1 ? 9  
ATOM 7559  C C   . ALA F 4 97  ? 18.975  59.298  70.184 1.000 269.025 0 95  ALA DDD C   1 ? 9  
ATOM 7560  O O   . ALA F 4 97  ? 19.172  60.073  69.244 1.000 283.910 0 95  ALA DDD O   1 ? 9  
ATOM 7561  C CB  . ALA F 4 97  ? 18.917  57.251  68.818 1.000 287.802 0 95  ALA DDD CB  1 ? 9  
ATOM 7562  N N   . LEU F 4 98  ? 19.434  59.515  71.415 1.000 262.161 0 96  LEU DDD N   1 ? 9  
ATOM 7563  C CA  . LEU F 4 98  ? 20.381  60.583  71.732 1.000 250.367 0 96  LEU DDD CA  1 ? 9  
ATOM 7564  C C   . LEU F 4 98  ? 21.394  59.868  72.604 1.000 242.211 0 96  LEU DDD C   1 ? 9  
ATOM 7565  O O   . LEU F 4 98  ? 21.003  59.234  73.590 1.000 225.578 0 96  LEU DDD O   1 ? 9  
ATOM 7566  C CB  . LEU F 4 98  ? 19.780  61.822  72.426 1.000 252.604 0 96  LEU DDD CB  1 ? 9  
ATOM 7567  C CG  . LEU F 4 98  ? 20.635  63.108  72.201 1.000 247.945 0 96  LEU DDD CG  1 ? 9  
ATOM 7568  C CD1 . LEU F 4 98  ? 19.873  64.413  72.457 1.000 259.615 0 96  LEU DDD CD1 1 ? 9  
ATOM 7569  C CD2 . LEU F 4 98  ? 21.964  63.152  72.974 1.000 225.397 0 96  LEU DDD CD2 1 ? 9  
ATOM 7570  N N   . ASP F 4 99  ? 22.675  59.944  72.227 1.000 237.324 0 97  ASP DDD N   1 ? 9  
ATOM 7571  C CA  . ASP F 4 99  ? 23.792  59.429  73.018 1.000 224.906 0 97  ASP DDD CA  1 ? 9  
ATOM 7572  C C   . ASP F 4 99  ? 23.452  59.351  74.502 1.000 225.093 0 97  ASP DDD C   1 ? 9  
ATOM 7573  O O   . ASP F 4 99  ? 23.867  60.205  75.295 1.000 226.575 0 97  ASP DDD O   1 ? 9  
ATOM 7574  C CB  . ASP F 4 99  ? 25.048  60.273  72.793 1.000 206.366 0 97  ASP DDD CB  1 ? 9  
ATOM 7575  C CG  . ASP F 4 99  ? 26.324  59.503  73.091 1.000 181.630 0 97  ASP DDD CG  1 ? 9  
ATOM 7576  O OD1 . ASP F 4 99  ? 26.259  58.260  73.205 1.000 177.652 0 97  ASP DDD OD1 1 ? 9  
ATOM 7577  O OD2 . ASP F 4 99  ? 27.393  60.134  73.213 1.000 176.684 0 97  ASP DDD OD2 1 ? 9  
ATOM 7578  N N   . THR F 4 100 ? 22.637  58.347  74.843 1.000 220.348 0 98  THR DDD N   1 ? 9  
ATOM 7579  C CA  . THR F 4 100 ? 22.344  57.872  76.199 1.000 216.283 0 98  THR DDD CA  1 ? 9  
ATOM 7580  C C   . THR F 4 100 ? 23.250  58.439  77.286 1.000 223.866 0 98  THR DDD C   1 ? 9  
ATOM 7581  O O   . THR F 4 100 ? 22.894  59.400  77.967 1.000 217.500 0 98  THR DDD O   1 ? 9  
ATOM 7582  C CB  . THR F 4 100 ? 22.440  56.329  76.273 1.000 204.301 0 98  THR DDD CB  1 ? 9  
ATOM 7583  O OG1 . THR F 4 100 ? 21.529  55.731  75.340 1.000 185.319 0 98  THR DDD OG1 1 ? 9  
ATOM 7584  C CG2 . THR F 4 100 ? 22.103  55.851  77.674 1.000 207.365 0 98  THR DDD CG2 1 ? 9  
ATOM 7585  N N   . ALA F 4 103 ? 19.823  54.174  73.980 1.000 190.534 0 101 ALA DDD N   1 ? 9  
ATOM 7586  C CA  . ALA F 4 103 ? 18.576  53.911  73.268 1.000 208.349 0 101 ALA DDD CA  1 ? 9  
ATOM 7587  C C   . ALA F 4 103 ? 17.368  54.103  74.188 1.000 256.428 0 101 ALA DDD C   1 ? 9  
ATOM 7588  O O   . ALA F 4 103 ? 17.337  53.600  75.309 1.000 269.711 0 101 ALA DDD O   1 ? 9  
ATOM 7589  C CB  . ALA F 4 103 ? 18.584  52.514  72.682 1.000 192.373 0 101 ALA DDD CB  1 ? 9  
ATOM 7590  N N   . TYR F 4 104 ? 16.384  54.849  73.692 1.000 259.217 0 102 TYR DDD N   1 ? 9  
ATOM 7591  C CA  . TYR F 4 104 ? 15.137  55.146  74.387 1.000 257.075 0 102 TYR DDD CA  1 ? 9  
ATOM 7592  C C   . TYR F 4 104 ? 13.924  54.545  73.681 1.000 263.349 0 102 TYR DDD C   1 ? 9  
ATOM 7593  O O   . TYR F 4 104 ? 13.889  54.487  72.456 1.000 266.658 0 102 TYR DDD O   1 ? 9  
ATOM 7594  C CB  . TYR F 4 104 ? 14.959  56.656  74.512 1.000 267.453 0 102 TYR DDD CB  1 ? 9  
ATOM 7595  C CG  . TYR F 4 104 ? 16.079  57.384  75.220 1.000 286.380 0 102 TYR DDD CG  1 ? 9  
ATOM 7596  C CD1 . TYR F 4 104 ? 16.624  56.881  76.394 1.000 290.107 0 102 TYR DDD CD1 1 ? 9  
ATOM 7597  C CD2 . TYR F 4 104 ? 16.557  58.600  74.745 1.000 309.148 0 102 TYR DDD CD2 1 ? 9  
ATOM 7598  C CE1 . TYR F 4 104 ? 17.634  57.551  77.059 1.000 292.029 0 102 TYR DDD CE1 1 ? 9  
ATOM 7599  C CE2 . TYR F 4 104 ? 17.567  59.278  75.405 1.000 303.084 0 102 TYR DDD CE2 1 ? 9  
ATOM 7600  C CZ  . TYR F 4 104 ? 18.101  58.750  76.562 1.000 286.368 0 102 TYR DDD CZ  1 ? 9  
ATOM 7601  O OH  . TYR F 4 104 ? 19.106  59.418  77.224 1.000 262.392 0 102 TYR DDD OH  1 ? 9  
ATOM 7602  N N   . TRP F 4 105 ? 12.935  54.092  74.463 1.000 270.050 0 103 TRP DDD N   1 ? 9  
ATOM 7603  C CA  . TRP F 4 105 ? 11.705  53.450  73.991 1.000 278.734 0 103 TRP DDD CA  1 ? 9  
ATOM 7604  C C   . TRP F 4 105 ? 10.459  54.161  74.517 1.000 284.217 0 103 TRP DDD C   1 ? 9  
ATOM 7605  O O   . TRP F 4 105 ? 10.461  54.730  75.613 1.000 284.725 0 103 TRP DDD O   1 ? 9  
ATOM 7606  C CB  . TRP F 4 105 ? 11.631  51.953  74.366 1.000 275.537 0 103 TRP DDD CB  1 ? 9  
ATOM 7607  C CG  . TRP F 4 105 ? 12.637  51.060  73.698 1.000 275.214 0 103 TRP DDD CG  1 ? 9  
ATOM 7608  C CD1 . TRP F 4 105 ? 13.662  50.377  74.286 1.000 273.353 0 103 TRP DDD CD1 1 ? 9  
ATOM 7609  C CD2 . TRP F 4 105 ? 12.611  50.636  72.326 1.000 275.800 0 103 TRP DDD CD2 1 ? 9  
ATOM 7610  N NE1 . TRP F 4 105 ? 14.324  49.618  73.349 1.000 274.952 0 103 TRP DDD NE1 1 ? 9  
ATOM 7611  C CE2 . TRP F 4 105 ? 13.693  49.754  72.140 1.000 275.723 0 103 TRP DDD CE2 1 ? 9  
ATOM 7612  C CE3 . TRP F 4 105 ? 11.797  50.943  71.231 1.000 274.814 0 103 TRP DDD CE3 1 ? 9  
ATOM 7613  C CZ2 . TRP F 4 105 ? 13.983  49.176  70.905 1.000 272.773 0 103 TRP DDD CZ2 1 ? 9  
ATOM 7614  C CZ3 . TRP F 4 105 ? 12.087  50.368  70.003 1.000 271.425 0 103 TRP DDD CZ3 1 ? 9  
ATOM 7615  C CH2 . TRP F 4 105 ? 13.170  49.495  69.852 1.000 273.217 0 103 TRP DDD CH2 1 ? 9  
ATOM 7616  N N   . GLY F 4 106 ? 9.385   54.113  73.718 1.000 290.212 0 104 GLY DDD N   1 ? 9  
ATOM 7617  C CA  . GLY F 4 106 ? 8.054   54.473  74.177 1.000 293.328 0 104 GLY DDD CA  1 ? 9  
ATOM 7618  C C   . GLY F 4 106 ? 7.380   53.375  74.987 1.000 294.950 0 104 GLY DDD C   1 ? 9  
ATOM 7619  O O   . GLY F 4 106 ? 7.917   52.284  75.181 1.000 298.261 0 104 GLY DDD O   1 ? 9  
ATOM 7620  N N   . GLN F 4 107 ? 6.165   53.678  75.471 1.000 291.750 0 105 GLN DDD N   1 ? 9  
ATOM 7621  C CA  . GLN F 4 107 ? 5.427   52.689  76.252 1.000 299.287 0 105 GLN DDD CA  1 ? 9  
ATOM 7622  C C   . GLN F 4 107 ? 4.608   51.702  75.424 1.000 310.171 0 105 GLN DDD C   1 ? 9  
ATOM 7623  O O   . GLN F 4 107 ? 4.240   50.641  75.938 1.000 306.610 0 105 GLN DDD O   1 ? 9  
ATOM 7624  C CB  . GLN F 4 107 ? 4.448   53.437  77.164 1.000 298.492 0 105 GLN DDD CB  1 ? 9  
ATOM 7625  C CG  . GLN F 4 107 ? 5.021   53.938  78.462 1.000 293.210 0 105 GLN DDD CG  1 ? 9  
ATOM 7626  C CD  . GLN F 4 107 ? 5.525   52.824  79.329 1.000 287.692 0 105 GLN DDD CD  1 ? 9  
ATOM 7627  O OE1 . GLN F 4 107 ? 4.861   51.802  79.493 1.000 293.263 0 105 GLN DDD OE1 1 ? 9  
ATOM 7628  N NE2 . GLN F 4 107 ? 6.706   53.012  79.901 1.000 276.260 0 105 GLN DDD NE2 1 ? 9  
ATOM 7629  N N   . GLY F 4 108 ? 4.302   52.031  74.179 1.000 332.384 0 106 GLY DDD N   1 ? 9  
ATOM 7630  C CA  . GLY F 4 108 ? 3.668   51.205  73.173 1.000 348.013 0 106 GLY DDD CA  1 ? 9  
ATOM 7631  C C   . GLY F 4 108 ? 2.192   51.530  72.991 1.000 368.641 0 106 GLY DDD C   1 ? 9  
ATOM 7632  O O   . GLY F 4 108 ? 1.524   52.065  73.879 1.000 395.355 0 106 GLY DDD O   1 ? 9  
ATOM 7633  N N   . THR F 4 109 ? 1.663   51.204  71.809 1.000 371.342 0 107 THR DDD N   1 ? 9  
ATOM 7634  C CA  . THR F 4 109 ? 0.227   51.320  71.581 1.000 373.260 0 107 THR DDD CA  1 ? 9  
ATOM 7635  C C   . THR F 4 109 ? -0.357  50.111  70.858 1.000 369.402 0 107 THR DDD C   1 ? 9  
ATOM 7636  O O   . THR F 4 109 ? 0.251   49.632  69.897 1.000 383.212 0 107 THR DDD O   1 ? 9  
ATOM 7637  C CB  . THR F 4 109 ? -0.128  52.568  70.792 1.000 369.028 0 107 THR DDD CB  1 ? 9  
ATOM 7638  O OG1 . THR F 4 109 ? 0.407   53.716  71.455 1.000 366.955 0 107 THR DDD OG1 1 ? 9  
ATOM 7639  C CG2 . THR F 4 109 ? -1.612  52.699  70.817 1.000 364.322 0 107 THR DDD CG2 1 ? 9  
ATOM 7640  N N   . GLN F 4 110 ? -1.531  49.624  71.264 1.000 340.945 0 108 GLN DDD N   1 ? 9  
ATOM 7641  C CA  . GLN F 4 110 ? -2.043  48.436  70.595 1.000 321.233 0 108 GLN DDD CA  1 ? 9  
ATOM 7642  C C   . GLN F 4 110 ? -2.723  49.003  69.351 1.000 324.825 0 108 GLN DDD C   1 ? 9  
ATOM 7643  O O   . GLN F 4 110 ? -3.529  49.933  69.453 1.000 323.583 0 108 GLN DDD O   1 ? 9  
ATOM 7644  C CB  . GLN F 4 110 ? -3.018  47.642  71.463 1.000 303.649 0 108 GLN DDD CB  1 ? 9  
ATOM 7645  C CG  . GLN F 4 110 ? -3.715  46.517  70.702 1.000 301.813 0 108 GLN DDD CG  1 ? 9  
ATOM 7646  C CD  . GLN F 4 110 ? -2.860  45.271  70.566 1.000 293.431 0 108 GLN DDD CD  1 ? 9  
ATOM 7647  O OE1 . GLN F 4 110 ? -2.378  44.724  71.555 1.000 286.890 0 108 GLN DDD OE1 1 ? 9  
ATOM 7648  N NE2 . GLN F 4 110 ? -2.662  44.822  69.331 1.000 298.673 0 108 GLN DDD NE2 1 ? 9  
ATOM 7649  N N   . VAL F 4 111 ? -2.413  48.451  68.183 1.000 329.533 0 109 VAL DDD N   1 ? 9  
ATOM 7650  C CA  . VAL F 4 111 ? -3.037  48.853  66.924 1.000 335.769 0 109 VAL DDD CA  1 ? 9  
ATOM 7651  C C   . VAL F 4 111 ? -3.688  47.669  66.225 1.000 342.065 0 109 VAL DDD C   1 ? 9  
ATOM 7652  O O   . VAL F 4 111 ? -3.057  46.623  66.074 1.000 345.236 0 109 VAL DDD O   1 ? 9  
ATOM 7653  C CB  . VAL F 4 111 ? -2.020  49.535  65.989 1.000 325.574 0 109 VAL DDD CB  1 ? 9  
ATOM 7654  C CG1 . VAL F 4 111 ? -2.602  49.688  64.590 1.000 325.265 0 109 VAL DDD CG1 1 ? 9  
ATOM 7655  C CG2 . VAL F 4 111 ? -1.624  50.896  66.544 1.000 316.483 0 109 VAL DDD CG2 1 ? 9  
ATOM 7656  N N   . THR F 4 112 ? -4.973  47.805  65.895 1.000 350.284 0 110 THR DDD N   1 ? 9  
ATOM 7657  C CA  . THR F 4 112 ? -5.796  46.737  65.330 1.000 347.046 0 110 THR DDD CA  1 ? 9  
ATOM 7658  C C   . THR F 4 112 ? -6.466  47.338  64.100 1.000 354.092 0 110 THR DDD C   1 ? 9  
ATOM 7659  O O   . THR F 4 112 ? -7.207  48.319  64.219 1.000 373.306 0 110 THR DDD O   1 ? 9  
ATOM 7660  C CB  . THR F 4 112 ? -6.835  46.197  66.316 1.000 345.949 0 110 THR DDD CB  1 ? 9  
ATOM 7661  O OG1 . THR F 4 112 ? -6.246  46.063  67.615 1.000 345.533 0 110 THR DDD OG1 1 ? 9  
ATOM 7662  C CG2 . THR F 4 112 ? -7.347  44.839  65.853 1.000 338.479 0 110 THR DDD CG2 1 ? 9  
ATOM 7663  N N   . VAL F 4 113 ? -6.207  46.765  62.924 1.000 342.082 0 111 VAL DDD N   1 ? 9  
ATOM 7664  C CA  . VAL F 4 113 ? -6.807  47.227  61.672 1.000 337.215 0 111 VAL DDD CA  1 ? 9  
ATOM 7665  C C   . VAL F 4 113 ? -7.778  46.175  61.154 1.000 334.141 0 111 VAL DDD C   1 ? 9  
ATOM 7666  O O   . VAL F 4 113 ? -7.369  45.093  60.716 1.000 332.259 0 111 VAL DDD O   1 ? 9  
ATOM 7667  C CB  . VAL F 4 113 ? -5.737  47.535  60.615 1.000 326.991 0 111 VAL DDD CB  1 ? 9  
ATOM 7668  C CG1 . VAL F 4 113 ? -6.353  48.245  59.416 1.000 329.290 0 111 VAL DDD CG1 1 ? 9  
ATOM 7669  C CG2 . VAL F 4 113 ? -4.608  48.358  61.217 1.000 326.272 0 111 VAL DDD CG2 1 ? 9  
ATOM 7670  N N   . SER F 4 114 ? -9.065  46.517  61.179 1.000 330.798 0 112 SER DDD N   1 ? 9  
ATOM 7671  C CA  . SER F 4 114 ? -10.132 45.705  60.600 1.000 315.444 0 112 SER DDD CA  1 ? 9  
ATOM 7672  C C   . SER F 4 114 ? -11.419 46.517  60.532 1.000 317.267 0 112 SER DDD C   1 ? 9  
ATOM 7673  O O   . SER F 4 114 ? -11.765 47.216  61.485 1.000 319.334 0 112 SER DDD O   1 ? 9  
ATOM 7674  C CB  . SER F 4 114 ? -10.355 44.428  61.385 1.000 290.987 0 112 SER DDD CB  1 ? 9  
ATOM 7675  O OG  . SER F 4 114 ? -11.523 43.759  60.932 1.000 273.136 0 112 SER DDD OG  1 ? 9  
ATOM 7676  N N   . MET G 5 1   ? 84.529  1.965   16.095 1.000 303.744 0 1   MET GGG N   1 ? 10 
ATOM 7677  C CA  . MET G 5 1   ? 85.727  2.733   16.405 1.000 310.731 0 1   MET GGG CA  1 ? 10 
ATOM 7678  C C   . MET G 5 1   ? 85.317  3.761   17.463 1.000 319.899 0 1   MET GGG C   1 ? 10 
ATOM 7679  O O   . MET G 5 1   ? 84.125  3.918   17.723 1.000 324.242 0 1   MET GGG O   1 ? 10 
ATOM 7680  C CB  . MET G 5 1   ? 86.297  3.369   15.122 1.000 306.961 0 1   MET GGG CB  1 ? 10 
ATOM 7681  C CG  . MET G 5 1   ? 87.103  4.664   15.260 1.000 310.170 0 1   MET GGG CG  1 ? 10 
ATOM 7682  S SD  . MET G 5 1   ? 87.089  5.697   13.777 1.000 309.841 0 1   MET GGG SD  1 ? 10 
ATOM 7683  C CE  . MET G 5 1   ? 87.750  7.233   14.423 1.000 289.345 0 1   MET GGG CE  1 ? 10 
ATOM 7684  N N   . VAL G 5 2   ? 86.288  4.431   18.092 1.000 337.603 0 2   VAL GGG N   1 ? 10 
ATOM 7685  C CA  . VAL G 5 2   ? 85.973  5.426   19.117 1.000 328.128 0 2   VAL GGG CA  1 ? 10 
ATOM 7686  C C   . VAL G 5 2   ? 84.982  6.457   18.590 1.000 318.598 0 2   VAL GGG C   1 ? 10 
ATOM 7687  O O   . VAL G 5 2   ? 84.047  6.851   19.296 1.000 323.512 0 2   VAL GGG O   1 ? 10 
ATOM 7688  C CB  . VAL G 5 2   ? 87.263  6.093   19.630 1.000 326.606 0 2   VAL GGG CB  1 ? 10 
ATOM 7689  C CG1 . VAL G 5 2   ? 87.977  5.172   20.600 1.000 331.019 0 2   VAL GGG CG1 1 ? 10 
ATOM 7690  C CG2 . VAL G 5 2   ? 88.168  6.455   18.465 1.000 324.304 0 2   VAL GGG CG2 1 ? 10 
ATOM 7691  N N   . ASN G 5 3   ? 85.155  6.892   17.334 1.000 319.424 0 3   ASN GGG N   1 ? 10 
ATOM 7692  C CA  . ASN G 5 3   ? 84.271  7.862   16.695 1.000 300.343 0 3   ASN GGG CA  1 ? 10 
ATOM 7693  C C   . ASN G 5 3   ? 83.221  7.149   15.842 1.000 301.453 0 3   ASN GGG C   1 ? 10 
ATOM 7694  O O   . ASN G 5 3   ? 83.418  6.973   14.633 1.000 295.024 0 3   ASN GGG O   1 ? 10 
ATOM 7695  C CB  . ASN G 5 3   ? 85.074  8.844   15.839 1.000 285.594 0 3   ASN GGG CB  1 ? 10 
ATOM 7696  C CG  . ASN G 5 3   ? 85.716  9.945   16.660 1.000 282.416 0 3   ASN GGG CG  1 ? 10 
ATOM 7697  O OD1 . ASN G 5 3   ? 85.338  10.172  17.808 1.000 287.409 0 3   ASN GGG OD1 1 ? 10 
ATOM 7698  N ND2 . ASN G 5 3   ? 86.689  10.635  16.076 1.000 274.680 0 3   ASN GGG ND2 1 ? 10 
ATOM 7699  N N   . PRO G 5 4   ? 82.100  6.726   16.424 1.000 294.098 0 4   PRO GGG N   1 ? 10 
ATOM 7700  C CA  . PRO G 5 4   ? 81.097  5.983   15.657 1.000 288.075 0 4   PRO GGG CA  1 ? 10 
ATOM 7701  C C   . PRO G 5 4   ? 80.280  6.874   14.726 1.000 286.914 0 4   PRO GGG C   1 ? 10 
ATOM 7702  O O   . PRO G 5 4   ? 80.393  8.101   14.713 1.000 296.459 0 4   PRO GGG O   1 ? 10 
ATOM 7703  C CB  . PRO G 5 4   ? 80.224  5.371   16.754 1.000 288.033 0 4   PRO GGG CB  1 ? 10 
ATOM 7704  C CG  . PRO G 5 4   ? 80.358  6.323   17.939 1.000 296.153 0 4   PRO GGG CG  1 ? 10 
ATOM 7705  C CD  . PRO G 5 4   ? 81.490  7.296   17.635 1.000 293.186 0 4   PRO GGG CD  1 ? 10 
ATOM 7706  N N   . THR G 5 5   ? 79.446  6.208   13.928 1.000 279.736 0 5   THR GGG N   1 ? 10 
ATOM 7707  C CA  . THR G 5 5   ? 78.571  6.828   12.944 1.000 270.414 0 5   THR GGG CA  1 ? 10 
ATOM 7708  C C   . THR G 5 5   ? 77.116  6.426   13.182 1.000 261.346 0 5   THR GGG C   1 ? 10 
ATOM 7709  O O   . THR G 5 5   ? 76.828  5.326   13.664 1.000 263.811 0 5   THR GGG O   1 ? 10 
ATOM 7710  C CB  . THR G 5 5   ? 79.036  6.493   11.519 1.000 268.136 0 5   THR GGG CB  1 ? 10 
ATOM 7711  O OG1 . THR G 5 5   ? 79.022  5.077   11.327 1.000 273.511 0 5   THR GGG OG1 1 ? 10 
ATOM 7712  C CG2 . THR G 5 5   ? 80.443  7.031   11.275 1.000 271.590 0 5   THR GGG CG2 1 ? 10 
ATOM 7713  N N   . VAL G 5 6   ? 76.198  7.344   12.848 1.000 248.690 0 6   VAL GGG N   1 ? 10 
ATOM 7714  C CA  . VAL G 5 6   ? 74.776  7.228   13.168 1.000 236.152 0 6   VAL GGG CA  1 ? 10 
ATOM 7715  C C   . VAL G 5 6   ? 73.923  7.486   11.923 1.000 234.594 0 6   VAL GGG C   1 ? 10 
ATOM 7716  O O   . VAL G 5 6   ? 74.340  8.182   10.991 1.000 230.605 0 6   VAL GGG O   1 ? 10 
ATOM 7717  C CB  . VAL G 5 6   ? 74.390  8.194   14.316 1.000 226.554 0 6   VAL GGG CB  1 ? 10 
ATOM 7718  C CG1 . VAL G 5 6   ? 72.932  8.027   14.718 1.000 222.409 0 6   VAL GGG CG1 1 ? 10 
ATOM 7719  C CG2 . VAL G 5 6   ? 75.296  7.986   15.518 1.000 225.628 0 6   VAL GGG CG2 1 ? 10 
ATOM 7720  N N   . PHE G 5 7   ? 72.717  6.908   11.917 1.000 233.478 0 7   PHE GGG N   1 ? 10 
ATOM 7721  C CA  . PHE G 5 7   ? 71.807  6.870   10.776 1.000 231.500 0 7   PHE GGG CA  1 ? 10 
ATOM 7722  C C   . PHE G 5 7   ? 70.491  7.582   11.100 1.000 225.355 0 7   PHE GGG C   1 ? 10 
ATOM 7723  O O   . PHE G 5 7   ? 69.944  7.393   12.189 1.000 224.197 0 7   PHE GGG O   1 ? 10 
ATOM 7724  C CB  . PHE G 5 7   ? 71.573  5.380   10.463 1.000 234.640 0 7   PHE GGG CB  1 ? 10 
ATOM 7725  C CG  . PHE G 5 7   ? 70.318  5.059   9.695  1.000 228.667 0 7   PHE GGG CG  1 ? 10 
ATOM 7726  C CD1 . PHE G 5 7   ? 69.128  4.813   10.366 1.000 233.553 0 7   PHE GGG CD1 1 ? 10 
ATOM 7727  C CD2 . PHE G 5 7   ? 70.366  4.803   8.341  1.000 221.758 0 7   PHE GGG CD2 1 ? 10 
ATOM 7728  C CE1 . PHE G 5 7   ? 67.979  4.463   9.674  1.000 231.759 0 7   PHE GGG CE1 1 ? 10 
ATOM 7729  C CE2 . PHE G 5 7   ? 69.222  4.439   7.642  1.000 227.741 0 7   PHE GGG CE2 1 ? 10 
ATOM 7730  C CZ  . PHE G 5 7   ? 68.029  4.270   8.310  1.000 229.356 0 7   PHE GGG CZ  1 ? 10 
ATOM 7731  N N   . PHE G 5 8   ? 69.997  8.424   10.174 1.000 214.829 0 8   PHE GGG N   1 ? 10 
ATOM 7732  C CA  . PHE G 5 8   ? 68.661  9.022   10.279 1.000 205.906 0 8   PHE GGG CA  1 ? 10 
ATOM 7733  C C   . PHE G 5 8   ? 67.905  8.942   8.960  1.000 199.506 0 8   PHE GGG C   1 ? 10 
ATOM 7734  O O   . PHE G 5 8   ? 68.431  9.378   7.932  1.000 192.945 0 8   PHE GGG O   1 ? 10 
ATOM 7735  C CB  . PHE G 5 8   ? 68.721  10.517  10.647 1.000 200.898 0 8   PHE GGG CB  1 ? 10 
ATOM 7736  C CG  . PHE G 5 8   ? 68.980  10.814  12.095 1.000 206.457 0 8   PHE GGG CG  1 ? 10 
ATOM 7737  C CD1 . PHE G 5 8   ? 70.121  10.387  12.745 1.000 216.268 0 8   PHE GGG CD1 1 ? 10 
ATOM 7738  C CD2 . PHE G 5 8   ? 68.071  11.596  12.792 1.000 193.012 0 8   PHE GGG CD2 1 ? 10 
ATOM 7739  C CE1 . PHE G 5 8   ? 70.321  10.685  14.078 1.000 216.163 0 8   PHE GGG CE1 1 ? 10 
ATOM 7740  C CE2 . PHE G 5 8   ? 68.266  11.903  14.118 1.000 182.859 0 8   PHE GGG CE2 1 ? 10 
ATOM 7741  C CZ  . PHE G 5 8   ? 69.394  11.446  14.763 1.000 198.295 0 8   PHE GGG CZ  1 ? 10 
ATOM 7742  N N   . ASP G 5 9   ? 66.679  8.402   8.983  1.000 204.296 0 9   ASP GGG N   1 ? 10 
ATOM 7743  C CA  . ASP G 5 9   ? 65.696  8.530   7.903  1.000 205.347 0 9   ASP GGG CA  1 ? 10 
ATOM 7744  C C   . ASP G 5 9   ? 64.652  9.620   8.178  1.000 196.563 0 9   ASP GGG C   1 ? 10 
ATOM 7745  O O   . ASP G 5 9   ? 63.921  9.530   9.169  1.000 202.754 0 9   ASP GGG O   1 ? 10 
ATOM 7746  C CB  . ASP G 5 9   ? 65.003  7.190   7.654  1.000 217.917 0 9   ASP GGG CB  1 ? 10 
ATOM 7747  C CG  . ASP G 5 9   ? 64.269  7.141   6.323  1.000 223.182 0 9   ASP GGG CG  1 ? 10 
ATOM 7748  O OD1 . ASP G 5 9   ? 63.988  8.206   5.725  1.000 231.836 0 9   ASP GGG OD1 1 ? 10 
ATOM 7749  O OD2 . ASP G 5 9   ? 63.980  6.016   5.868  1.000 226.135 0 9   ASP GGG OD2 1 ? 10 
ATOM 7750  N N   . ILE G 5 10  ? 64.567  10.639  7.317  1.000 182.758 0 10  ILE GGG N   1 ? 10 
ATOM 7751  C CA  . ILE G 5 10  ? 63.702  11.800  7.552  1.000 161.069 0 10  ILE GGG CA  1 ? 10 
ATOM 7752  C C   . ILE G 5 10  ? 62.434  11.635  6.720  1.000 158.818 0 10  ILE GGG C   1 ? 10 
ATOM 7753  O O   . ILE G 5 10  ? 62.499  11.178  5.573  1.000 170.272 0 10  ILE GGG O   1 ? 10 
ATOM 7754  C CB  . ILE G 5 10  ? 64.412  13.128  7.243  1.000 163.523 0 10  ILE GGG CB  1 ? 10 
ATOM 7755  C CG1 . ILE G 5 10  ? 65.703  13.214  8.048  1.000 163.129 0 10  ILE GGG CG1 1 ? 10 
ATOM 7756  C CG2 . ILE G 5 10  ? 63.497  14.302  7.571  1.000 160.979 0 10  ILE GGG CG2 1 ? 10 
ATOM 7757  C CD1 . ILE G 5 10  ? 65.453  13.273  9.536  1.000 167.086 0 10  ILE GGG CD1 1 ? 10 
ATOM 7758  N N   . ALA G 5 11  ? 61.277  11.985  7.294  1.000 159.113 0 11  ALA GGG N   1 ? 10 
ATOM 7759  C CA  . ALA G 5 11  ? 59.994  11.966  6.589  1.000 163.314 0 11  ALA GGG CA  1 ? 10 
ATOM 7760  C C   . ALA G 5 11  ? 59.277  13.310  6.696  1.000 158.616 0 11  ALA GGG C   1 ? 10 
ATOM 7761  O O   . ALA G 5 11  ? 59.468  14.054  7.660  1.000 160.186 0 11  ALA GGG O   1 ? 10 
ATOM 7762  C CB  . ALA G 5 11  ? 59.075  10.860  7.122  1.000 175.448 0 11  ALA GGG CB  1 ? 10 
ATOM 7763  N N   . VAL G 5 12  ? 58.447  13.616  5.694  1.000 159.734 0 12  VAL GGG N   1 ? 10 
ATOM 7764  C CA  . VAL G 5 12  ? 57.674  14.860  5.644  1.000 162.949 0 12  VAL GGG CA  1 ? 10 
ATOM 7765  C C   . VAL G 5 12  ? 56.196  14.506  5.515  1.000 177.352 0 12  VAL GGG C   1 ? 10 
ATOM 7766  O O   . VAL G 5 12  ? 55.764  14.006  4.468  1.000 189.149 0 12  VAL GGG O   1 ? 10 
ATOM 7767  C CB  . VAL G 5 12  ? 58.106  15.757  4.478  1.000 153.553 0 12  VAL GGG CB  1 ? 10 
ATOM 7768  C CG1 . VAL G 5 12  ? 57.224  17.002  4.412  1.000 149.130 0 12  VAL GGG CG1 1 ? 10 
ATOM 7769  C CG2 . VAL G 5 12  ? 59.570  16.123  4.607  1.000 161.760 0 12  VAL GGG CG2 1 ? 10 
ATOM 7770  N N   . ASP G 5 13  ? 55.410  14.813  6.554  1.000 174.662 0 13  ASP GGG N   1 ? 10 
ATOM 7771  C CA  . ASP G 5 13  ? 54.002  14.401  6.639  1.000 179.705 0 13  ASP GGG CA  1 ? 10 
ATOM 7772  C C   . ASP G 5 13  ? 53.825  12.925  6.293  1.000 185.430 0 13  ASP GGG C   1 ? 10 
ATOM 7773  O O   . ASP G 5 13  ? 52.863  12.531  5.632  1.000 190.365 0 13  ASP GGG O   1 ? 10 
ATOM 7774  C CB  . ASP G 5 13  ? 53.098  15.271  5.760  1.000 180.590 0 13  ASP GGG CB  1 ? 10 
ATOM 7775  C CG  . ASP G 5 13  ? 52.720  16.585  6.419  1.000 183.850 0 13  ASP GGG CG  1 ? 10 
ATOM 7776  O OD1 . ASP G 5 13  ? 53.109  16.803  7.586  1.000 185.905 0 13  ASP GGG OD1 1 ? 10 
ATOM 7777  O OD2 . ASP G 5 13  ? 52.028  17.397  5.771  1.000 190.407 0 13  ASP GGG OD2 1 ? 10 
ATOM 7778  N N   . GLY G 5 14  ? 54.769  12.102  6.736  1.000 184.531 0 14  GLY GGG N   1 ? 10 
ATOM 7779  C CA  . GLY G 5 14  ? 54.704  10.691  6.433  1.000 189.775 0 14  GLY GGG CA  1 ? 10 
ATOM 7780  C C   . GLY G 5 14  ? 55.257  10.305  5.082  1.000 192.052 0 14  GLY GGG C   1 ? 10 
ATOM 7781  O O   . GLY G 5 14  ? 55.256  9.112   4.754  1.000 201.541 0 14  GLY GGG O   1 ? 10 
ATOM 7782  N N   . GLU G 5 15  ? 55.752  11.279  4.285  1.000 194.519 0 15  GLU GGG N   1 ? 10 
ATOM 7783  C CA  . GLU G 5 15  ? 56.268  10.992  2.951  1.000 190.381 0 15  GLU GGG CA  1 ? 10 
ATOM 7784  C C   . GLU G 5 15  ? 57.773  10.809  3.013  1.000 186.503 0 15  GLU GGG C   1 ? 10 
ATOM 7785  O O   . GLU G 5 15  ? 58.463  11.642  3.619  1.000 191.088 0 15  GLU GGG O   1 ? 10 
ATOM 7786  C CB  . GLU G 5 15  ? 55.935  12.120  1.982  1.000 188.368 0 15  GLU GGG CB  1 ? 10 
ATOM 7787  C CG  . GLU G 5 15  ? 54.456  12.420  1.852  1.000 200.474 0 15  GLU GGG CG  1 ? 10 
ATOM 7788  C CD  . GLU G 5 15  ? 54.089  12.783  0.440  1.000 214.328 0 15  GLU GGG CD  1 ? 10 
ATOM 7789  O OE1 . GLU G 5 15  ? 54.747  12.234  -0.465 1.000 218.975 0 15  GLU GGG OE1 1 ? 10 
ATOM 7790  O OE2 . GLU G 5 15  ? 53.178  13.616  0.235  1.000 216.454 0 15  GLU GGG OE2 1 ? 10 
ATOM 7791  N N   . PRO G 5 16  ? 58.316  9.751   2.412  1.000 183.044 0 16  PRO GGG N   1 ? 10 
ATOM 7792  C CA  . PRO G 5 16  ? 59.754  9.498   2.545  1.000 179.401 0 16  PRO GGG CA  1 ? 10 
ATOM 7793  C C   . PRO G 5 16  ? 60.563  10.640  1.953  1.000 178.663 0 16  PRO GGG C   1 ? 10 
ATOM 7794  O O   . PRO G 5 16  ? 60.244  11.161  0.883  1.000 191.011 0 16  PRO GGG O   1 ? 10 
ATOM 7795  C CB  . PRO G 5 16  ? 59.961  8.200   1.753  1.000 188.013 0 16  PRO GGG CB  1 ? 10 
ATOM 7796  C CG  . PRO G 5 16  ? 58.778  8.135   0.823  1.000 186.747 0 16  PRO GGG CG  1 ? 10 
ATOM 7797  C CD  . PRO G 5 16  ? 57.646  8.722   1.601  1.000 188.621 0 16  PRO GGG CD  1 ? 10 
ATOM 7798  N N   . LEU G 5 17  ? 61.625  11.019  2.662  1.000 177.743 0 17  LEU GGG N   1 ? 10 
ATOM 7799  C CA  . LEU G 5 17  ? 62.463  12.148  2.277  1.000 173.373 0 17  LEU GGG CA  1 ? 10 
ATOM 7800  C C   . LEU G 5 17  ? 63.917  11.764  2.060  1.000 170.359 0 17  LEU GGG C   1 ? 10 
ATOM 7801  O O   . LEU G 5 17  ? 64.510  12.165  1.058  1.000 179.001 0 17  LEU GGG O   1 ? 10 
ATOM 7802  C CB  . LEU G 5 17  ? 62.364  13.289  3.298  1.000 166.488 0 17  LEU GGG CB  1 ? 10 
ATOM 7803  C CG  . LEU G 5 17  ? 63.287  14.446  2.919  1.000 155.775 0 17  LEU GGG CG  1 ? 10 
ATOM 7804  C CD1 . LEU G 5 17  ? 62.825  15.049  1.603  1.000 151.623 0 17  LEU GGG CD1 1 ? 10 
ATOM 7805  C CD2 . LEU G 5 17  ? 63.297  15.503  3.999  1.000 154.510 0 17  LEU GGG CD2 1 ? 10 
ATOM 7806  N N   . GLY G 5 18  ? 64.570  11.140  3.022  1.000 175.389 0 18  GLY GGG N   1 ? 10 
ATOM 7807  C CA  . GLY G 5 18  ? 65.937  10.763  2.742  1.000 180.833 0 18  GLY GGG CA  1 ? 10 
ATOM 7808  C C   . GLY G 5 18  ? 66.682  10.311  3.971  1.000 191.164 0 18  GLY GGG C   1 ? 10 
ATOM 7809  O O   . GLY G 5 18  ? 66.178  10.345  5.098  1.000 193.976 0 18  GLY GGG O   1 ? 10 
ATOM 7810  N N   . ARG G 5 19  ? 67.920  9.907   3.714  1.000 194.418 0 19  ARG GGG N   1 ? 10 
ATOM 7811  C CA  . ARG G 5 19  ? 68.798  9.338   4.718  1.000 205.198 0 19  ARG GGG CA  1 ? 10 
ATOM 7812  C C   . ARG G 5 19  ? 69.994  10.256  4.913  1.000 197.334 0 19  ARG GGG C   1 ? 10 
ATOM 7813  O O   . ARG G 5 19  ? 70.642  10.659  3.941  1.000 194.289 0 19  ARG GGG O   1 ? 10 
ATOM 7814  C CB  . ARG G 5 19  ? 69.242  7.938   4.302  1.000 212.215 0 19  ARG GGG CB  1 ? 10 
ATOM 7815  C CG  . ARG G 5 19  ? 69.383  7.003   5.465  1.000 213.882 0 19  ARG GGG CG  1 ? 10 
ATOM 7816  C CD  . ARG G 5 19  ? 70.644  7.247   6.252  1.000 221.562 0 19  ARG GGG CD  1 ? 10 
ATOM 7817  N NE  . ARG G 5 19  ? 71.838  6.911   5.492  1.000 224.921 0 19  ARG GGG NE  1 ? 10 
ATOM 7818  C CZ  . ARG G 5 19  ? 73.066  6.967   5.986  1.000 232.764 0 19  ARG GGG CZ  1 ? 10 
ATOM 7819  N NH1 . ARG G 5 19  ? 73.287  7.316   7.242  1.000 237.946 0 19  ARG GGG NH1 1 ? 10 
ATOM 7820  N NH2 . ARG G 5 19  ? 74.095  6.647   5.206  1.000 241.627 0 19  ARG GGG NH2 1 ? 10 
ATOM 7821  N N   . VAL G 5 20  ? 70.277  10.580  6.169  1.000 197.633 0 20  VAL GGG N   1 ? 10 
ATOM 7822  C CA  . VAL G 5 20  ? 71.347  11.491  6.550  1.000 195.706 0 20  VAL GGG CA  1 ? 10 
ATOM 7823  C C   . VAL G 5 20  ? 72.383  10.701  7.329  1.000 205.024 0 20  VAL GGG C   1 ? 10 
ATOM 7824  O O   . VAL G 5 20  ? 72.037  9.981   8.273  1.000 205.895 0 20  VAL GGG O   1 ? 10 
ATOM 7825  C CB  . VAL G 5 20  ? 70.834  12.670  7.393  1.000 193.919 0 20  VAL GGG CB  1 ? 10 
ATOM 7826  C CG1 . VAL G 5 20  ? 71.927  13.720  7.539  1.000 198.252 0 20  VAL GGG CG1 1 ? 10 
ATOM 7827  C CG2 . VAL G 5 20  ? 69.583  13.259  6.778  1.000 187.411 0 20  VAL GGG CG2 1 ? 10 
ATOM 7828  N N   . SER G 5 21  ? 73.647  10.851  6.952  1.000 205.560 0 21  SER GGG N   1 ? 10 
ATOM 7829  C CA  . SER G 5 21  ? 74.729  10.170  7.641  1.000 211.172 0 21  SER GGG CA  1 ? 10 
ATOM 7830  C C   . SER G 5 21  ? 75.236  11.069  8.754  1.000 201.848 0 21  SER GGG C   1 ? 10 
ATOM 7831  O O   . SER G 5 21  ? 75.385  12.281  8.574  1.000 193.756 0 21  SER GGG O   1 ? 10 
ATOM 7832  C CB  . SER G 5 21  ? 75.866  9.822   6.681  1.000 223.286 0 21  SER GGG CB  1 ? 10 
ATOM 7833  O OG  . SER G 5 21  ? 75.362  9.279   5.476  1.000 235.891 0 21  SER GGG OG  1 ? 10 
ATOM 7834  N N   . PHE G 5 22  ? 75.502  10.462  9.905  1.000 216.201 0 22  PHE GGG N   1 ? 10 
ATOM 7835  C CA  . PHE G 5 22  ? 75.950  11.183  11.081 1.000 223.551 0 22  PHE GGG CA  1 ? 10 
ATOM 7836  C C   . PHE G 5 22  ? 77.213  10.520  11.604 1.000 242.778 0 22  PHE GGG C   1 ? 10 
ATOM 7837  O O   . PHE G 5 22  ? 77.282  9.291   11.670 1.000 255.404 0 22  PHE GGG O   1 ? 10 
ATOM 7838  C CB  . PHE G 5 22  ? 74.862  11.100  12.157 1.000 224.267 0 22  PHE GGG CB  1 ? 10 
ATOM 7839  C CG  . PHE G 5 22  ? 73.817  12.167  12.062 1.000 216.486 0 22  PHE GGG CG  1 ? 10 
ATOM 7840  C CD1 . PHE G 5 22  ? 72.814  12.070  11.112 1.000 209.238 0 22  PHE GGG CD1 1 ? 10 
ATOM 7841  C CD2 . PHE G 5 22  ? 73.795  13.226  12.947 1.000 208.071 0 22  PHE GGG CD2 1 ? 10 
ATOM 7842  C CE1 . PHE G 5 22  ? 71.830  13.026  11.021 1.000 203.057 0 22  PHE GGG CE1 1 ? 10 
ATOM 7843  C CE2 . PHE G 5 22  ? 72.808  14.191  12.862 1.000 201.264 0 22  PHE GGG CE2 1 ? 10 
ATOM 7844  C CZ  . PHE G 5 22  ? 71.824  14.089  11.895 1.000 201.338 0 22  PHE GGG CZ  1 ? 10 
ATOM 7845  N N   . GLU G 5 23  ? 78.216  11.323  11.965 1.000 261.890 0 23  GLU GGG N   1 ? 10 
ATOM 7846  C CA  . GLU G 5 23  ? 79.412  10.827  12.640 1.000 285.048 0 23  GLU GGG CA  1 ? 10 
ATOM 7847  C C   . GLU G 5 23  ? 79.585  11.625  13.923 1.000 292.165 0 23  GLU GGG C   1 ? 10 
ATOM 7848  O O   . GLU G 5 23  ? 79.477  12.855  13.905 1.000 303.464 0 23  GLU GGG O   1 ? 10 
ATOM 7849  C CB  . GLU G 5 23  ? 80.652  10.935  11.749 1.000 300.413 0 23  GLU GGG CB  1 ? 10 
ATOM 7850  C CG  . GLU G 5 23  ? 81.956  10.542  12.417 1.000 314.205 0 23  GLU GGG CG  1 ? 10 
ATOM 7851  C CD  . GLU G 5 23  ? 82.724  11.741  12.925 1.000 322.236 0 23  GLU GGG CD  1 ? 10 
ATOM 7852  O OE1 . GLU G 5 23  ? 82.284  12.878  12.660 1.000 321.576 0 23  GLU GGG OE1 1 ? 10 
ATOM 7853  O OE2 . GLU G 5 23  ? 83.769  11.548  13.582 1.000 334.562 0 23  GLU GGG OE2 1 ? 10 
ATOM 7854  N N   . LEU G 5 24  ? 79.852  10.937  15.028 1.000 278.585 0 24  LEU GGG N   1 ? 10 
ATOM 7855  C CA  . LEU G 5 24  ? 80.057  11.588  16.314 1.000 263.378 0 24  LEU GGG CA  1 ? 10 
ATOM 7856  C C   . LEU G 5 24  ? 81.505  11.567  16.789 1.000 263.903 0 24  LEU GGG C   1 ? 10 
ATOM 7857  O O   . LEU G 5 24  ? 82.154  10.515  16.766 1.000 288.887 0 24  LEU GGG O   1 ? 10 
ATOM 7858  C CB  . LEU G 5 24  ? 79.200  10.894  17.374 1.000 250.778 0 24  LEU GGG CB  1 ? 10 
ATOM 7859  C CG  . LEU G 5 24  ? 77.701  10.757  17.118 1.000 247.539 0 24  LEU GGG CG  1 ? 10 
ATOM 7860  C CD1 . LEU G 5 24  ? 77.035  10.052  18.286 1.000 242.981 0 24  LEU GGG CD1 1 ? 10 
ATOM 7861  C CD2 . LEU G 5 24  ? 77.073  12.118  16.889 1.000 242.233 0 24  LEU GGG CD2 1 ? 10 
ATOM 7862  N N   . PHE G 5 25  ? 82.009  12.728  17.216 1.000 257.031 0 25  PHE GGG N   1 ? 10 
ATOM 7863  C CA  . PHE G 5 25  ? 83.420  12.877  17.588 1.000 260.034 0 25  PHE GGG CA  1 ? 10 
ATOM 7864  C C   . PHE G 5 25  ? 83.564  12.507  19.064 1.000 265.248 0 25  PHE GGG C   1 ? 10 
ATOM 7865  O O   . PHE G 5 25  ? 83.860  13.326  19.936 1.000 263.407 0 25  PHE GGG O   1 ? 10 
ATOM 7866  C CB  . PHE G 5 25  ? 83.990  14.256  17.267 1.000 251.674 0 25  PHE GGG CB  1 ? 10 
ATOM 7867  C CG  . PHE G 5 25  ? 83.973  14.613  15.808 1.000 251.038 0 25  PHE GGG CG  1 ? 10 
ATOM 7868  C CD1 . PHE G 5 25  ? 85.045  14.223  15.016 1.000 261.050 0 25  PHE GGG CD1 1 ? 10 
ATOM 7869  C CD2 . PHE G 5 25  ? 82.968  15.369  15.238 1.000 235.809 0 25  PHE GGG CD2 1 ? 10 
ATOM 7870  C CE1 . PHE G 5 25  ? 85.100  14.535  13.678 1.000 258.613 0 25  PHE GGG CE1 1 ? 10 
ATOM 7871  C CE2 . PHE G 5 25  ? 83.018  15.692  13.887 1.000 236.692 0 25  PHE GGG CE2 1 ? 10 
ATOM 7872  C CZ  . PHE G 5 25  ? 84.088  15.274  13.109 1.000 244.629 0 25  PHE GGG CZ  1 ? 10 
ATOM 7873  N N   . ALA G 5 26  ? 83.329  11.219  19.321 1.000 274.176 0 26  ALA GGG N   1 ? 10 
ATOM 7874  C CA  . ALA G 5 26  ? 83.325  10.649  20.663 1.000 276.082 0 26  ALA GGG CA  1 ? 10 
ATOM 7875  C C   . ALA G 5 26  ? 84.705  10.691  21.299 1.000 282.218 0 26  ALA GGG C   1 ? 10 
ATOM 7876  O O   . ALA G 5 26  ? 84.821  10.527  22.518 1.000 274.420 0 26  ALA GGG O   1 ? 10 
ATOM 7877  C CB  . ALA G 5 26  ? 82.789  9.220   20.640 1.000 267.957 0 26  ALA GGG CB  1 ? 10 
ATOM 7878  N N   . ASP G 5 27  ? 85.752  10.873  20.495 1.000 292.728 0 27  ASP GGG N   1 ? 10 
ATOM 7879  C CA  . ASP G 5 27  ? 87.101  10.975  21.034 1.000 311.662 0 27  ASP GGG CA  1 ? 10 
ATOM 7880  C C   . ASP G 5 27  ? 87.294  12.259  21.829 1.000 317.794 0 27  ASP GGG C   1 ? 10 
ATOM 7881  O O   . ASP G 5 27  ? 88.169  12.317  22.701 1.000 335.370 0 27  ASP GGG O   1 ? 10 
ATOM 7882  C CB  . ASP G 5 27  ? 88.107  10.940  19.885 1.000 316.829 0 27  ASP GGG CB  1 ? 10 
ATOM 7883  C CG  . ASP G 5 27  ? 87.947  12.130  18.940 1.000 309.736 0 27  ASP GGG CG  1 ? 10 
ATOM 7884  O OD1 . ASP G 5 27  ? 86.799  12.587  18.745 1.000 307.103 0 27  ASP GGG OD1 1 ? 10 
ATOM 7885  O OD2 . ASP G 5 27  ? 88.964  12.616  18.400 1.000 310.431 0 27  ASP GGG OD2 1 ? 10 
ATOM 7886  N N   . LYS G 5 28  ? 86.500  13.291  21.552 1.000 318.141 0 28  LYS GGG N   1 ? 10 
ATOM 7887  C CA  . LYS G 5 28  ? 86.495  14.506  22.358 1.000 300.020 0 28  LYS GGG CA  1 ? 10 
ATOM 7888  C C   . LYS G 5 28  ? 85.323  14.579  23.327 1.000 290.450 0 28  LYS GGG C   1 ? 10 
ATOM 7889  O O   . LYS G 5 28  ? 85.482  15.081  24.444 1.000 288.761 0 28  LYS GGG O   1 ? 10 
ATOM 7890  C CB  . LYS G 5 28  ? 86.473  15.749  21.462 1.000 287.081 0 28  LYS GGG CB  1 ? 10 
ATOM 7891  C CG  . LYS G 5 28  ? 87.586  15.814  20.443 1.000 290.591 0 28  LYS GGG CG  1 ? 10 
ATOM 7892  C CD  . LYS G 5 28  ? 88.932  15.897  21.135 1.000 289.304 0 28  LYS GGG CD  1 ? 10 
ATOM 7893  C CE  . LYS G 5 28  ? 90.000  16.401  20.186 1.000 282.704 0 28  LYS GGG CE  1 ? 10 
ATOM 7894  N NZ  . LYS G 5 28  ? 90.012  15.621  18.921 1.000 281.189 0 28  LYS GGG NZ  1 ? 10 
ATOM 7895  N N   . VAL G 5 29  ? 84.153  14.086  22.936 1.000 272.231 0 29  VAL GGG N   1 ? 10 
ATOM 7896  C CA  . VAL G 5 29  ? 82.954  14.230  23.756 1.000 256.203 0 29  VAL GGG CA  1 ? 10 
ATOM 7897  C C   . VAL G 5 29  ? 82.240  12.878  23.778 1.000 255.107 0 29  VAL GGG C   1 ? 10 
ATOM 7898  O O   . VAL G 5 29  ? 81.330  12.627  22.975 1.000 254.261 0 29  VAL GGG O   1 ? 10 
ATOM 7899  C CB  . VAL G 5 29  ? 82.099  15.401  23.230 1.000 243.595 0 29  VAL GGG CB  1 ? 10 
ATOM 7900  C CG1 . VAL G 5 29  ? 80.649  15.279  23.584 1.000 233.168 0 29  VAL GGG CG1 1 ? 10 
ATOM 7901  C CG2 . VAL G 5 29  ? 82.650  16.725  23.730 1.000 241.393 0 29  VAL GGG CG2 1 ? 10 
ATOM 7902  N N   . PRO G 5 30  ? 82.711  11.928  24.592 1.000 254.053 0 30  PRO GGG N   1 ? 10 
ATOM 7903  C CA  . PRO G 5 30  ? 82.049  10.612  24.626 1.000 253.618 0 30  PRO GGG CA  1 ? 10 
ATOM 7904  C C   . PRO G 5 30  ? 80.663  10.636  25.245 1.000 250.957 0 30  PRO GGG C   1 ? 10 
ATOM 7905  O O   . PRO G 5 30  ? 79.762  9.948   24.750 1.000 253.469 0 30  PRO GGG O   1 ? 10 
ATOM 7906  C CB  . PRO G 5 30  ? 83.016  9.750   25.454 1.000 254.495 0 30  PRO GGG CB  1 ? 10 
ATOM 7907  C CG  . PRO G 5 30  ? 83.903  10.720  26.163 1.000 257.825 0 30  PRO GGG CG  1 ? 10 
ATOM 7908  C CD  . PRO G 5 30  ? 84.010  11.912  25.281 1.000 258.507 0 30  PRO GGG CD  1 ? 10 
ATOM 7909  N N   . LYS G 5 31  ? 80.470  11.395  26.330 1.000 250.254 0 31  LYS GGG N   1 ? 10 
ATOM 7910  C CA  . LYS G 5 31  ? 79.191  11.369  27.033 1.000 246.938 0 31  LYS GGG CA  1 ? 10 
ATOM 7911  C C   . LYS G 5 31  ? 78.040  11.810  26.137 1.000 246.282 0 31  LYS GGG C   1 ? 10 
ATOM 7912  O O   . LYS G 5 31  ? 76.975  11.182  26.132 1.000 247.751 0 31  LYS GGG O   1 ? 10 
ATOM 7913  C CB  . LYS G 5 31  ? 79.275  12.262  28.271 1.000 245.066 0 31  LYS GGG CB  1 ? 10 
ATOM 7914  C CG  . LYS G 5 31  ? 80.434  11.924  29.196 1.000 250.185 0 31  LYS GGG CG  1 ? 10 
ATOM 7915  C CD  . LYS G 5 31  ? 80.641  12.999  30.252 1.000 248.807 0 31  LYS GGG CD  1 ? 10 
ATOM 7916  C CE  . LYS G 5 31  ? 79.683  12.849  31.419 1.000 248.470 0 31  LYS GGG CE  1 ? 10 
ATOM 7917  N NZ  . LYS G 5 31  ? 80.026  13.787  32.523 1.000 238.983 0 31  LYS GGG NZ  1 ? 10 
ATOM 7918  N N   . THR G 5 32  ? 78.231  12.886  25.369 1.000 243.105 0 32  THR GGG N   1 ? 10 
ATOM 7919  C CA  . THR G 5 32  ? 77.149  13.369  24.516 1.000 236.057 0 32  THR GGG CA  1 ? 10 
ATOM 7920  C C   . THR G 5 32  ? 76.942  12.432  23.336 1.000 236.433 0 32  THR GGG C   1 ? 10 
ATOM 7921  O O   . THR G 5 32  ? 75.803  12.168  22.931 1.000 235.564 0 32  THR GGG O   1 ? 10 
ATOM 7922  C CB  . THR G 5 32  ? 77.419  14.787  24.030 1.000 231.686 0 32  THR GGG CB  1 ? 10 
ATOM 7923  O OG1 . THR G 5 32  ? 77.689  15.635  25.153 1.000 231.719 0 32  THR GGG OG1 1 ? 10 
ATOM 7924  C CG2 . THR G 5 32  ? 76.201  15.322  23.307 1.000 226.906 0 32  THR GGG CG2 1 ? 10 
ATOM 7925  N N   . ALA G 5 33  ? 78.041  11.929  22.765 1.000 236.723 0 33  ALA GGG N   1 ? 10 
ATOM 7926  C CA  . ALA G 5 33  ? 77.932  10.963  21.681 1.000 242.790 0 33  ALA GGG CA  1 ? 10 
ATOM 7927  C C   . ALA G 5 33  ? 77.191  9.726   22.161 1.000 253.201 0 33  ALA GGG C   1 ? 10 
ATOM 7928  O O   . ALA G 5 33  ? 76.311  9.207   21.465 1.000 248.678 0 33  ALA GGG O   1 ? 10 
ATOM 7929  C CB  . ALA G 5 33  ? 79.321  10.601  21.153 1.000 247.873 0 33  ALA GGG CB  1 ? 10 
ATOM 7930  N N   . GLU G 5 34  ? 77.546  9.228   23.349 1.000 255.789 0 34  GLU GGG N   1 ? 10 
ATOM 7931  C CA  . GLU G 5 34  ? 76.893  8.026   23.851 1.000 265.283 0 34  GLU GGG CA  1 ? 10 
ATOM 7932  C C   . GLU G 5 34  ? 75.412  8.307   24.055 1.000 263.700 0 34  GLU GGG C   1 ? 10 
ATOM 7933  O O   . GLU G 5 34  ? 74.557  7.462   23.767 1.000 270.059 0 34  GLU GGG O   1 ? 10 
ATOM 7934  C CB  . GLU G 5 34  ? 77.541  7.578   25.160 1.000 261.877 0 34  GLU GGG CB  1 ? 10 
ATOM 7935  C CG  . GLU G 5 34  ? 77.962  6.118   25.193 1.000 272.945 0 34  GLU GGG CG  1 ? 10 
ATOM 7936  C CD  . GLU G 5 34  ? 79.044  5.799   24.181 1.000 279.980 0 34  GLU GGG CD  1 ? 10 
ATOM 7937  O OE1 . GLU G 5 34  ? 79.953  6.638   24.003 1.000 284.821 0 34  GLU GGG OE1 1 ? 10 
ATOM 7938  O OE2 . GLU G 5 34  ? 78.993  4.710   23.574 1.000 280.384 0 34  GLU GGG OE2 1 ? 10 
ATOM 7939  N N   . ASN G 5 35  ? 75.104  9.500   24.571 1.000 271.229 0 35  ASN GGG N   1 ? 10 
ATOM 7940  C CA  . ASN G 5 35  ? 73.726  9.948   24.722 1.000 270.145 0 35  ASN GGG CA  1 ? 10 
ATOM 7941  C C   . ASN G 5 35  ? 72.997  9.906   23.385 1.000 264.662 0 35  ASN GGG C   1 ? 10 
ATOM 7942  O O   . ASN G 5 35  ? 71.910  9.329   23.267 1.000 264.540 0 35  ASN GGG O   1 ? 10 
ATOM 7943  C CB  . ASN G 5 35  ? 73.716  11.362  25.311 1.000 273.114 0 35  ASN GGG CB  1 ? 10 
ATOM 7944  C CG  . ASN G 5 35  ? 72.317  11.895  25.558 1.000 276.415 0 35  ASN GGG CG  1 ? 10 
ATOM 7945  O OD1 . ASN G 5 35  ? 71.322  11.231  25.279 1.000 274.652 0 35  ASN GGG OD1 1 ? 10 
ATOM 7946  N ND2 . ASN G 5 35  ? 72.238  13.109  26.090 1.000 278.614 0 35  ASN GGG ND2 1 ? 10 
ATOM 7947  N N   . PHE G 5 36  ? 73.593  10.523  22.363 1.000 256.649 0 36  PHE GGG N   1 ? 10 
ATOM 7948  C CA  . PHE G 5 36  ? 72.992  10.560  21.034 1.000 255.025 0 36  PHE GGG CA  1 ? 10 
ATOM 7949  C C   . PHE G 5 36  ? 72.873  9.160   20.441 1.000 253.295 0 36  PHE GGG C   1 ? 10 
ATOM 7950  O O   . PHE G 5 36  ? 71.857  8.827   19.818 1.000 248.320 0 36  PHE GGG O   1 ? 10 
ATOM 7951  C CB  . PHE G 5 36  ? 73.826  11.474  20.133 1.000 252.726 0 36  PHE GGG CB  1 ? 10 
ATOM 7952  C CG  . PHE G 5 36  ? 73.156  11.854  18.842 1.000 236.828 0 36  PHE GGG CG  1 ? 10 
ATOM 7953  C CD1 . PHE G 5 36  ? 72.376  12.998  18.765 1.000 222.271 0 36  PHE GGG CD1 1 ? 10 
ATOM 7954  C CD2 . PHE G 5 36  ? 73.327  11.089  17.702 1.000 239.434 0 36  PHE GGG CD2 1 ? 10 
ATOM 7955  C CE1 . PHE G 5 36  ? 71.768  13.363  17.579 1.000 217.660 0 36  PHE GGG CE1 1 ? 10 
ATOM 7956  C CE2 . PHE G 5 36  ? 72.720  11.449  16.514 1.000 232.701 0 36  PHE GGG CE2 1 ? 10 
ATOM 7957  C CZ  . PHE G 5 36  ? 71.943  12.590  16.453 1.000 220.497 0 36  PHE GGG CZ  1 ? 10 
ATOM 7958  N N   . ARG G 5 37  ? 73.903  8.328   20.616 1.000 258.928 0 37  ARG GGG N   1 ? 10 
ATOM 7959  C CA  . ARG G 5 37  ? 73.859  6.968   20.084 1.000 260.987 0 37  ARG GGG CA  1 ? 10 
ATOM 7960  C C   . ARG G 5 37  ? 72.684  6.185   20.658 1.000 260.511 0 37  ARG GGG C   1 ? 10 
ATOM 7961  O O   . ARG G 5 37  ? 71.912  5.571   19.912 1.000 249.781 0 37  ARG GGG O   1 ? 10 
ATOM 7962  C CB  . ARG G 5 37  ? 75.172  6.239   20.375 1.000 254.890 0 37  ARG GGG CB  1 ? 10 
ATOM 7963  C CG  . ARG G 5 37  ? 75.032  4.722   20.423 1.000 242.537 0 37  ARG GGG CG  1 ? 10 
ATOM 7964  C CD  . ARG G 5 37  ? 76.190  4.075   21.153 1.000 247.453 0 37  ARG GGG CD  1 ? 10 
ATOM 7965  N NE  . ARG G 5 37  ? 75.861  2.720   21.575 1.000 258.428 0 37  ARG GGG NE  1 ? 10 
ATOM 7966  C CZ  . ARG G 5 37  ? 75.389  2.404   22.773 1.000 265.032 0 37  ARG GGG CZ  1 ? 10 
ATOM 7967  N NH1 . ARG G 5 37  ? 75.125  3.333   23.678 1.000 265.241 0 37  ARG GGG NH1 1 ? 10 
ATOM 7968  N NH2 . ARG G 5 37  ? 75.161  1.127   23.066 1.000 264.872 0 37  ARG GGG NH2 1 ? 10 
ATOM 7969  N N   . ALA G 5 38  ? 72.526  6.197   21.985 1.000 269.267 0 38  ALA GGG N   1 ? 10 
ATOM 7970  C CA  . ALA G 5 38  ? 71.466  5.398   22.595 1.000 287.369 0 38  ALA GGG CA  1 ? 10 
ATOM 7971  C C   . ALA G 5 38  ? 70.088  5.944   22.244 1.000 283.823 0 38  ALA GGG C   1 ? 10 
ATOM 7972  O O   . ALA G 5 38  ? 69.141  5.173   22.049 1.000 294.884 0 38  ALA GGG O   1 ? 10 
ATOM 7973  C CB  . ALA G 5 38  ? 71.655  5.344   24.111 1.000 313.894 0 38  ALA GGG CB  1 ? 10 
ATOM 7974  N N   . LEU G 5 39  ? 69.954  7.269   22.163 1.000 261.241 0 39  LEU GGG N   1 ? 10 
ATOM 7975  C CA  . LEU G 5 39  ? 68.689  7.852   21.731 1.000 246.208 0 39  LEU GGG CA  1 ? 10 
ATOM 7976  C C   . LEU G 5 39  ? 68.401  7.520   20.272 1.000 235.781 0 39  LEU GGG C   1 ? 10 
ATOM 7977  O O   . LEU G 5 39  ? 67.236  7.443   19.870 1.000 231.878 0 39  LEU GGG O   1 ? 10 
ATOM 7978  C CB  . LEU G 5 39  ? 68.687  9.362   21.959 1.000 242.990 0 39  LEU GGG CB  1 ? 10 
ATOM 7979  C CG  . LEU G 5 39  ? 68.719  9.831   23.414 1.000 234.775 0 39  LEU GGG CG  1 ? 10 
ATOM 7980  C CD1 . LEU G 5 39  ? 68.832  11.339  23.470 1.000 223.984 0 39  LEU GGG CD1 1 ? 10 
ATOM 7981  C CD2 . LEU G 5 39  ? 67.490  9.360   24.172 1.000 237.060 0 39  LEU GGG CD2 1 ? 10 
ATOM 7982  N N   . SER G 5 40  ? 69.444  7.319   19.470 1.000 235.386 0 40  SER GGG N   1 ? 10 
ATOM 7983  C CA  . SER G 5 40  ? 69.243  6.984   18.068 1.000 235.708 0 40  SER GGG CA  1 ? 10 
ATOM 7984  C C   . SER G 5 40  ? 68.823  5.533   17.884 1.000 242.583 0 40  SER GGG C   1 ? 10 
ATOM 7985  O O   . SER G 5 40  ? 68.131  5.212   16.915 1.000 248.740 0 40  SER GGG O   1 ? 10 
ATOM 7986  C CB  . SER G 5 40  ? 70.521  7.261   17.281 1.000 237.833 0 40  SER GGG CB  1 ? 10 
ATOM 7987  O OG  . SER G 5 40  ? 70.839  8.639   17.324 1.000 241.192 0 40  SER GGG OG  1 ? 10 
ATOM 7988  N N   . THR G 5 41  ? 69.244  4.637   18.764 1.000 243.599 0 41  THR GGG N   1 ? 10 
ATOM 7989  C CA  . THR G 5 41  ? 68.830  3.251   18.613 1.000 241.977 0 41  THR GGG CA  1 ? 10 
ATOM 7990  C C   . THR G 5 41  ? 67.557  2.942   19.387 1.000 243.789 0 41  THR GGG C   1 ? 10 
ATOM 7991  O O   . THR G 5 41  ? 66.854  1.984   19.047 1.000 245.242 0 41  THR GGG O   1 ? 10 
ATOM 7992  C CB  . THR G 5 41  ? 69.945  2.309   19.080 1.000 251.915 0 41  THR GGG CB  1 ? 10 
ATOM 7993  O OG1 . THR G 5 41  ? 70.166  2.490   20.484 1.000 262.485 0 41  THR GGG OG1 1 ? 10 
ATOM 7994  C CG2 . THR G 5 41  ? 71.240  2.597   18.331 1.000 250.687 0 41  THR GGG CG2 1 ? 10 
ATOM 7995  N N   . GLY G 5 42  ? 67.242  3.750   20.397 1.000 245.217 0 42  GLY GGG N   1 ? 10 
ATOM 7996  C CA  . GLY G 5 42  ? 66.070  3.566   21.229 1.000 245.105 0 42  GLY GGG CA  1 ? 10 
ATOM 7997  C C   . GLY G 5 42  ? 66.229  2.409   22.181 1.000 243.659 0 42  GLY GGG C   1 ? 10 
ATOM 7998  O O   . GLY G 5 42  ? 65.245  1.927   22.747 1.000 247.280 0 42  GLY GGG O   1 ? 10 
ATOM 7999  N N   . GLU G 5 43  ? 67.470  1.959   22.368 1.000 244.741 0 43  GLU GGG N   1 ? 10 
ATOM 8000  C CA  . GLU G 5 43  ? 67.766  0.755   23.129 1.000 250.676 0 43  GLU GGG CA  1 ? 10 
ATOM 8001  C C   . GLU G 5 43  ? 67.501  0.891   24.621 1.000 248.547 0 43  GLU GGG C   1 ? 10 
ATOM 8002  O O   . GLU G 5 43  ? 67.332  -0.128  25.298 1.000 249.197 0 43  GLU GGG O   1 ? 10 
ATOM 8003  C CB  . GLU G 5 43  ? 69.234  0.393   22.913 1.000 256.649 0 43  GLU GGG CB  1 ? 10 
ATOM 8004  C CG  . GLU G 5 43  ? 70.172  1.377   23.598 1.000 259.249 0 43  GLU GGG CG  1 ? 10 
ATOM 8005  C CD  . GLU G 5 43  ? 71.607  1.262   23.140 1.000 264.426 0 43  GLU GGG CD  1 ? 10 
ATOM 8006  O OE1 . GLU G 5 43  ? 72.256  0.238   23.440 1.000 273.873 0 43  GLU GGG OE1 1 ? 10 
ATOM 8007  O OE2 . GLU G 5 43  ? 72.088  2.209   22.482 1.000 262.471 0 43  GLU GGG OE2 1 ? 10 
ATOM 8008  N N   . LYS G 5 44  ? 67.444  2.112   25.148 1.000 245.179 0 44  LYS GGG N   1 ? 10 
ATOM 8009  C CA  . LYS G 5 44  ? 67.098  2.324   26.546 1.000 248.482 0 44  LYS GGG CA  1 ? 10 
ATOM 8010  C C   . LYS G 5 44  ? 65.603  2.430   26.803 1.000 250.782 0 44  LYS GGG C   1 ? 10 
ATOM 8011  O O   . LYS G 5 44  ? 65.202  2.564   27.966 1.000 248.566 0 44  LYS GGG O   1 ? 10 
ATOM 8012  C CB  . LYS G 5 44  ? 67.771  3.610   27.042 1.000 243.829 0 44  LYS GGG CB  1 ? 10 
ATOM 8013  C CG  . LYS G 5 44  ? 69.287  3.629   26.896 1.000 235.950 0 44  LYS GGG CG  1 ? 10 
ATOM 8014  C CD  . LYS G 5 44  ? 69.994  2.634   27.786 1.000 238.369 0 44  LYS GGG CD  1 ? 10 
ATOM 8015  C CE  . LYS G 5 44  ? 71.451  2.532   27.365 1.000 236.113 0 44  LYS GGG CE  1 ? 10 
ATOM 8016  N NZ  . LYS G 5 44  ? 72.136  1.345   27.933 1.000 242.287 0 44  LYS GGG NZ  1 ? 10 
ATOM 8017  N N   . GLY G 5 45  ? 64.770  2.379   25.767 1.000 252.107 0 45  GLY GGG N   1 ? 10 
ATOM 8018  C CA  . GLY G 5 45  ? 63.337  2.423   25.954 1.000 255.827 0 45  GLY GGG CA  1 ? 10 
ATOM 8019  C C   . GLY G 5 45  ? 62.762  3.782   25.625 1.000 261.597 0 45  GLY GGG C   1 ? 10 
ATOM 8020  O O   . GLY G 5 45  ? 61.544  3.972   25.745 1.000 259.149 0 45  GLY GGG O   1 ? 10 
ATOM 8021  N N   . PHE G 5 46  ? 63.623  4.740   25.263 1.000 269.689 0 46  PHE GGG N   1 ? 10 
ATOM 8022  C CA  . PHE G 5 46  ? 63.265  6.092   24.856 1.000 264.489 0 46  PHE GGG CA  1 ? 10 
ATOM 8023  C C   . PHE G 5 46  ? 64.326  6.628   23.902 1.000 257.383 0 46  PHE GGG C   1 ? 10 
ATOM 8024  O O   . PHE G 5 46  ? 65.523  6.502   24.176 1.000 261.360 0 46  PHE GGG O   1 ? 10 
ATOM 8025  C CB  . PHE G 5 46  ? 63.171  6.994   26.096 1.000 261.138 0 46  PHE GGG CB  1 ? 10 
ATOM 8026  C CG  . PHE G 5 46  ? 64.432  7.004   26.949 1.000 259.370 0 46  PHE GGG CG  1 ? 10 
ATOM 8027  C CD1 . PHE G 5 46  ? 64.597  6.105   27.994 1.000 263.619 0 46  PHE GGG CD1 1 ? 10 
ATOM 8028  C CD2 . PHE G 5 46  ? 65.427  7.950   26.733 1.000 255.011 0 46  PHE GGG CD2 1 ? 10 
ATOM 8029  C CE1 . PHE G 5 46  ? 65.750  6.127   28.782 1.000 265.763 0 46  PHE GGG CE1 1 ? 10 
ATOM 8030  C CE2 . PHE G 5 46  ? 66.577  7.978   27.516 1.000 250.397 0 46  PHE GGG CE2 1 ? 10 
ATOM 8031  C CZ  . PHE G 5 46  ? 66.736  7.069   28.542 1.000 254.923 0 46  PHE GGG CZ  1 ? 10 
ATOM 8032  N N   . GLY G 5 47  ? 63.901  7.206   22.788 1.000 243.834 0 47  GLY GGG N   1 ? 10 
ATOM 8033  C CA  . GLY G 5 47  ? 64.850  7.693   21.815 1.000 242.210 0 47  GLY GGG CA  1 ? 10 
ATOM 8034  C C   . GLY G 5 47  ? 64.216  8.537   20.732 1.000 228.323 0 47  GLY GGG C   1 ? 10 
ATOM 8035  O O   . GLY G 5 47  ? 63.099  9.037   20.878 1.000 222.596 0 47  GLY GGG O   1 ? 10 
ATOM 8036  N N   . TYR G 5 48  ? 64.952  8.677   19.624 1.000 220.383 0 48  TYR GGG N   1 ? 10 
ATOM 8037  C CA  . TYR G 5 48  ? 64.603  9.651   18.599 1.000 201.728 0 48  TYR GGG CA  1 ? 10 
ATOM 8038  C C   . TYR G 5 48  ? 63.510  9.186   17.643 1.000 196.571 0 48  TYR GGG C   1 ? 10 
ATOM 8039  O O   . TYR G 5 48  ? 62.912  10.034  16.973 1.000 193.357 0 48  TYR GGG O   1 ? 10 
ATOM 8040  C CB  . TYR G 5 48  ? 65.843  10.065  17.810 1.000 197.570 0 48  TYR GGG CB  1 ? 10 
ATOM 8041  C CG  . TYR G 5 48  ? 66.856  10.822  18.634 1.000 196.859 0 48  TYR GGG CG  1 ? 10 
ATOM 8042  C CD1 . TYR G 5 48  ? 66.449  11.833  19.495 1.000 188.448 0 48  TYR GGG CD1 1 ? 10 
ATOM 8043  C CD2 . TYR G 5 48  ? 68.218  10.599  18.485 1.000 204.315 0 48  TYR GGG CD2 1 ? 10 
ATOM 8044  C CE1 . TYR G 5 48  ? 67.364  12.557  20.238 1.000 186.386 0 48  TYR GGG CE1 1 ? 10 
ATOM 8045  C CE2 . TYR G 5 48  ? 69.145  11.328  19.214 1.000 203.245 0 48  TYR GGG CE2 1 ? 10 
ATOM 8046  C CZ  . TYR G 5 48  ? 68.712  12.304  20.090 1.000 191.757 0 48  TYR GGG CZ  1 ? 10 
ATOM 8047  O OH  . TYR G 5 48  ? 69.636  13.025  20.814 1.000 198.083 0 48  TYR GGG OH  1 ? 10 
ATOM 8048  N N   . LYS G 5 49  ? 63.241  7.884   17.535 1.000 199.209 0 49  LYS GGG N   1 ? 10 
ATOM 8049  C CA  . LYS G 5 49  ? 62.266  7.427   16.550 1.000 198.306 0 49  LYS GGG CA  1 ? 10 
ATOM 8050  C C   . LYS G 5 49  ? 60.921  8.082   16.834 1.000 200.009 0 49  LYS GGG C   1 ? 10 
ATOM 8051  O O   . LYS G 5 49  ? 60.410  8.009   17.954 1.000 214.092 0 49  LYS GGG O   1 ? 10 
ATOM 8052  C CB  . LYS G 5 49  ? 62.125  5.904   16.566 1.000 203.082 0 49  LYS GGG CB  1 ? 10 
ATOM 8053  C CG  . LYS G 5 49  ? 63.426  5.140   16.650 1.000 216.151 0 49  LYS GGG CG  1 ? 10 
ATOM 8054  C CD  . LYS G 5 49  ? 63.439  4.032   15.611 1.000 227.429 0 49  LYS GGG CD  1 ? 10 
ATOM 8055  C CE  . LYS G 5 49  ? 64.747  3.266   15.617 1.000 233.521 0 49  LYS GGG CE  1 ? 10 
ATOM 8056  N NZ  . LYS G 5 49  ? 64.731  2.144   14.634 1.000 229.637 0 49  LYS GGG NZ  1 ? 10 
ATOM 8057  N N   . GLY G 5 50  ? 60.351  8.735   15.824 1.000 203.280 0 50  GLY GGG N   1 ? 10 
ATOM 8058  C CA  . GLY G 5 50  ? 59.089  9.411   16.015 1.000 201.510 0 50  GLY GGG CA  1 ? 10 
ATOM 8059  C C   . GLY G 5 50  ? 59.192  10.854  16.460 1.000 199.509 0 50  GLY GGG C   1 ? 10 
ATOM 8060  O O   . GLY G 5 50  ? 58.154  11.513  16.602 1.000 199.671 0 50  GLY GGG O   1 ? 10 
ATOM 8061  N N   . SER G 5 51  ? 60.397  11.374  16.684 1.000 211.844 0 51  SER GGG N   1 ? 10 
ATOM 8062  C CA  . SER G 5 51  ? 60.496  12.731  17.188 1.000 209.022 0 51  SER GGG CA  1 ? 10 
ATOM 8063  C C   . SER G 5 51  ? 60.446  13.702  16.017 1.000 202.734 0 51  SER GGG C   1 ? 10 
ATOM 8064  O O   . SER G 5 51  ? 60.613  13.326  14.855 1.000 205.343 0 51  SER GGG O   1 ? 10 
ATOM 8065  C CB  . SER G 5 51  ? 61.791  12.914  17.985 1.000 210.016 0 51  SER GGG CB  1 ? 10 
ATOM 8066  O OG  . SER G 5 51  ? 62.186  14.276  18.036 1.000 208.526 0 51  SER GGG OG  1 ? 10 
ATOM 8067  N N   . CYS G 5 52  ? 60.223  14.971  16.331 1.000 189.938 0 52  CYS GGG N   1 ? 10 
ATOM 8068  C CA  . CYS G 5 52  ? 60.063  15.970  15.292 1.000 180.603 0 52  CYS GGG CA  1 ? 10 
ATOM 8069  C C   . CYS G 5 52  ? 61.207  16.969  15.307 1.000 169.215 0 52  CYS GGG C   1 ? 10 
ATOM 8070  O O   . CYS G 5 52  ? 61.943  17.098  16.289 1.000 165.536 0 52  CYS GGG O   1 ? 10 
ATOM 8071  C CB  . CYS G 5 52  ? 58.738  16.720  15.473 1.000 180.620 0 52  CYS GGG CB  1 ? 10 
ATOM 8072  S SG  . CYS G 5 52  ? 57.274  15.736  15.099 1.000 217.745 0 52  CYS GGG SG  1 ? 10 
ATOM 8073  N N   . PHE G 5 53  ? 61.354  17.669  14.188 1.000 159.190 0 53  PHE GGG N   1 ? 10 
ATOM 8074  C CA  . PHE G 5 53  ? 62.161  18.876  14.141 1.000 150.066 0 53  PHE GGG CA  1 ? 10 
ATOM 8075  C C   . PHE G 5 53  ? 61.222  20.040  14.426 1.000 150.600 0 53  PHE GGG C   1 ? 10 
ATOM 8076  O O   . PHE G 5 53  ? 60.401  20.406  13.578 1.000 149.176 0 53  PHE GGG O   1 ? 10 
ATOM 8077  C CB  . PHE G 5 53  ? 62.868  19.006  12.798 1.000 145.300 0 53  PHE GGG CB  1 ? 10 
ATOM 8078  C CG  . PHE G 5 53  ? 64.084  18.136  12.680 1.000 147.704 0 53  PHE GGG CG  1 ? 10 
ATOM 8079  C CD1 . PHE G 5 53  ? 65.329  18.608  13.064 1.000 147.515 0 53  PHE GGG CD1 1 ? 10 
ATOM 8080  C CD2 . PHE G 5 53  ? 63.977  16.828  12.236 1.000 152.068 0 53  PHE GGG CD2 1 ? 10 
ATOM 8081  C CE1 . PHE G 5 53  ? 66.450  17.807  12.967 1.000 150.425 0 53  PHE GGG CE1 1 ? 10 
ATOM 8082  C CE2 . PHE G 5 53  ? 65.095  16.018  12.139 1.000 148.957 0 53  PHE GGG CE2 1 ? 10 
ATOM 8083  C CZ  . PHE G 5 53  ? 66.333  16.509  12.506 1.000 141.540 0 53  PHE GGG CZ  1 ? 10 
ATOM 8084  N N   . HIS G 5 54  ? 61.350  20.621  15.616 1.000 152.578 0 54  HIS GGG N   1 ? 10 
ATOM 8085  C CA  . HIS G 5 54  ? 60.423  21.640  16.094 1.000 147.046 0 54  HIS GGG CA  1 ? 10 
ATOM 8086  C C   . HIS G 5 54  ? 60.835  23.052  15.701 1.000 140.242 0 54  HIS GGG C   1 ? 10 
ATOM 8087  O O   . HIS G 5 54  ? 59.974  23.932  15.585 1.000 134.664 0 54  HIS GGG O   1 ? 10 
ATOM 8088  C CB  . HIS G 5 54  ? 60.263  21.515  17.616 1.000 150.495 0 54  HIS GGG CB  1 ? 10 
ATOM 8089  C CG  . HIS G 5 54  ? 61.511  21.806  18.395 1.000 154.430 0 54  HIS GGG CG  1 ? 10 
ATOM 8090  N ND1 . HIS G 5 54  ? 62.477  20.849  18.627 1.000 160.731 0 54  HIS GGG ND1 1 ? 10 
ATOM 8091  C CD2 . HIS G 5 54  ? 61.940  22.930  19.017 1.000 154.654 0 54  HIS GGG CD2 1 ? 10 
ATOM 8092  C CE1 . HIS G 5 54  ? 63.452  21.374  19.348 1.000 160.827 0 54  HIS GGG CE1 1 ? 10 
ATOM 8093  N NE2 . HIS G 5 54  ? 63.152  22.636  19.597 1.000 155.948 0 54  HIS GGG NE2 1 ? 10 
ATOM 8094  N N   . ARG G 5 55  ? 62.128  23.285  15.497 1.000 137.627 0 55  ARG GGG N   1 ? 10 
ATOM 8095  C CA  . ARG G 5 55  ? 62.641  24.577  15.057 1.000 128.279 0 55  ARG GGG CA  1 ? 10 
ATOM 8096  C C   . ARG G 5 55  ? 63.494  24.362  13.816 1.000 129.279 0 55  ARG GGG C   1 ? 10 
ATOM 8097  O O   . ARG G 5 55  ? 64.586  23.792  13.906 1.000 125.085 0 55  ARG GGG O   1 ? 10 
ATOM 8098  C CB  . ARG G 5 55  ? 63.464  25.240  16.157 1.000 119.213 0 55  ARG GGG CB  1 ? 10 
ATOM 8099  C CG  . ARG G 5 55  ? 63.251  26.727  16.298 1.000 112.695 0 55  ARG GGG CG  1 ? 10 
ATOM 8100  C CD  . ARG G 5 55  ? 64.053  27.238  17.468 1.000 110.934 0 55  ARG GGG CD  1 ? 10 
ATOM 8101  N NE  . ARG G 5 55  ? 64.635  28.548  17.211 1.000 109.459 0 55  ARG GGG NE  1 ? 10 
ATOM 8102  C CZ  . ARG G 5 55  ? 65.728  29.005  17.806 1.000 127.449 0 55  ARG GGG CZ  1 ? 10 
ATOM 8103  N NH1 . ARG G 5 55  ? 66.396  28.269  18.681 1.000 133.251 0 55  ARG GGG NH1 1 ? 10 
ATOM 8104  N NH2 . ARG G 5 55  ? 66.158  30.231  17.521 1.000 134.669 0 55  ARG GGG NH2 1 ? 10 
ATOM 8105  N N   . ILE G 5 56  ? 63.016  24.822  12.664 1.000 129.642 0 56  ILE GGG N   1 ? 10 
ATOM 8106  C CA  . ILE G 5 56  ? 63.839  24.872  11.464 1.000 126.892 0 56  ILE GGG CA  1 ? 10 
ATOM 8107  C C   . ILE G 5 56  ? 63.889  26.316  10.990 1.000 120.253 0 56  ILE GGG C   1 ? 10 
ATOM 8108  O O   . ILE G 5 56  ? 62.857  26.899  10.635 1.000 120.646 0 56  ILE GGG O   1 ? 10 
ATOM 8109  C CB  . ILE G 5 56  ? 63.297  23.951  10.361 1.000 125.008 0 56  ILE GGG CB  1 ? 10 
ATOM 8110  C CG1 . ILE G 5 56  ? 63.321  22.492  10.814 1.000 129.072 0 56  ILE GGG CG1 1 ? 10 
ATOM 8111  C CG2 . ILE G 5 56  ? 64.115  24.108  9.108  1.000 122.518 0 56  ILE GGG CG2 1 ? 10 
ATOM 8112  C CD1 . ILE G 5 56  ? 62.863  21.523  9.749  1.000 126.227 0 56  ILE GGG CD1 1 ? 10 
ATOM 8113  N N   . ILE G 5 57  ? 65.087  26.888  10.991 1.000 120.333 0 57  ILE GGG N   1 ? 10 
ATOM 8114  C CA  . ILE G 5 57  ? 65.331  28.265  10.574 1.000 122.867 0 57  ILE GGG CA  1 ? 10 
ATOM 8115  C C   . ILE G 5 57  ? 66.297  28.264  9.396  1.000 121.089 0 57  ILE GGG C   1 ? 10 
ATOM 8116  O O   . ILE G 5 57  ? 67.478  27.936  9.581  1.000 118.011 0 57  ILE GGG O   1 ? 10 
ATOM 8117  C CB  . ILE G 5 57  ? 65.849  29.124  11.738 1.000 123.822 0 57  ILE GGG CB  1 ? 10 
ATOM 8118  C CG1 . ILE G 5 57  ? 64.840  29.116  12.884 1.000 120.545 0 57  ILE GGG CG1 1 ? 10 
ATOM 8119  C CG2 . ILE G 5 57  ? 66.108  30.547  11.283 1.000 122.668 0 57  ILE GGG CG2 1 ? 10 
ATOM 8120  C CD1 . ILE G 5 57  ? 65.347  29.763  14.141 1.000 125.397 0 57  ILE GGG CD1 1 ? 10 
ATOM 8121  N N   . PRO G 5 58  ? 65.858  28.592  8.182  1.000 121.255 0 58  PRO GGG N   1 ? 10 
ATOM 8122  C CA  . PRO G 5 58  ? 66.764  28.500  7.031  1.000 120.041 0 58  PRO GGG CA  1 ? 10 
ATOM 8123  C C   . PRO G 5 58  ? 67.954  29.432  7.203  1.000 124.372 0 58  PRO GGG C   1 ? 10 
ATOM 8124  O O   . PRO G 5 58  ? 67.824  30.564  7.674  1.000 121.036 0 58  PRO GGG O   1 ? 10 
ATOM 8125  C CB  . PRO G 5 58  ? 65.879  28.917  5.851  1.000 121.966 0 58  PRO GGG CB  1 ? 10 
ATOM 8126  C CG  . PRO G 5 58  ? 64.812  29.761  6.475  1.000 127.510 0 58  PRO GGG CG  1 ? 10 
ATOM 8127  C CD  . PRO G 5 58  ? 64.532  29.099  7.791  1.000 126.447 0 58  PRO GGG CD  1 ? 10 
ATOM 8128  N N   . GLY G 5 59  ? 69.129  28.933  6.828  1.000 124.699 0 59  GLY GGG N   1 ? 10 
ATOM 8129  C CA  . GLY G 5 59  ? 70.345  29.701  6.968  1.000 124.922 0 59  GLY GGG CA  1 ? 10 
ATOM 8130  C C   . GLY G 5 59  ? 70.922  29.689  8.364  1.000 125.007 0 59  GLY GGG C   1 ? 10 
ATOM 8131  O O   . GLY G 5 59  ? 71.909  30.388  8.616  1.000 125.933 0 59  GLY GGG O   1 ? 10 
ATOM 8132  N N   . PHE G 5 60  ? 70.336  28.913  9.278  1.000 127.205 0 60  PHE GGG N   1 ? 10 
ATOM 8133  C CA  . PHE G 5 60  ? 70.766  28.859  10.670 1.000 126.983 0 60  PHE GGG CA  1 ? 10 
ATOM 8134  C C   . PHE G 5 60  ? 70.997  27.425  11.120 1.000 127.390 0 60  PHE GGG C   1 ? 10 
ATOM 8135  O O   . PHE G 5 60  ? 72.141  26.963  11.183 1.000 131.761 0 60  PHE GGG O   1 ? 10 
ATOM 8136  C CB  . PHE G 5 60  ? 69.733  29.525  11.581 1.000 133.395 0 60  PHE GGG CB  1 ? 10 
ATOM 8137  C CG  . PHE G 5 60  ? 70.215  29.749  12.989 1.000 138.243 0 60  PHE GGG CG  1 ? 10 
ATOM 8138  C CD1 . PHE G 5 60  ? 71.559  29.951  13.256 1.000 142.650 0 60  PHE GGG CD1 1 ? 10 
ATOM 8139  C CD2 . PHE G 5 60  ? 69.317  29.785  14.043 1.000 135.414 0 60  PHE GGG CD2 1 ? 10 
ATOM 8140  C CE1 . PHE G 5 60  ? 71.998  30.164  14.553 1.000 150.909 0 60  PHE GGG CE1 1 ? 10 
ATOM 8141  C CE2 . PHE G 5 60  ? 69.749  30.002  15.337 1.000 141.025 0 60  PHE GGG CE2 1 ? 10 
ATOM 8142  C CZ  . PHE G 5 60  ? 71.090  30.193  15.592 1.000 148.954 0 60  PHE GGG CZ  1 ? 10 
ATOM 8143  N N   . MET G 5 61  ? 69.920  26.715  11.437 1.000 128.045 0 61  MET GGG N   1 ? 10 
ATOM 8144  C CA  . MET G 5 61  ? 70.034  25.370  11.983 1.000 134.304 0 61  MET GGG CA  1 ? 10 
ATOM 8145  C C   . MET G 5 61  ? 68.680  24.681  11.902 1.000 136.125 0 61  MET GGG C   1 ? 10 
ATOM 8146  O O   . MET G 5 61  ? 67.649  25.311  11.650 1.000 134.902 0 61  MET GGG O   1 ? 10 
ATOM 8147  C CB  . MET G 5 61  ? 70.531  25.395  13.431 1.000 138.872 0 61  MET GGG CB  1 ? 10 
ATOM 8148  C CG  . MET G 5 61  ? 69.705  26.281  14.347 1.000 139.931 0 61  MET GGG CG  1 ? 10 
ATOM 8149  S SD  . MET G 5 61  ? 68.320  25.415  15.108 1.000 144.444 0 61  MET GGG SD  1 ? 10 
ATOM 8150  C CE  . MET G 5 61  ? 67.184  26.775  15.349 1.000 142.346 0 61  MET GGG CE  1 ? 10 
ATOM 8151  N N   . CYS G 5 62  ? 68.703  23.371  12.129 1.000 138.770 0 62  CYS GGG N   1 ? 10 
ATOM 8152  C CA  . CYS G 5 62  ? 67.506  22.560  12.294 1.000 139.749 0 62  CYS GGG CA  1 ? 10 
ATOM 8153  C C   . CYS G 5 62  ? 67.604  21.851  13.635 1.000 141.585 0 62  CYS GGG C   1 ? 10 
ATOM 8154  O O   . CYS G 5 62  ? 68.614  21.202  13.922 1.000 142.220 0 62  CYS GGG O   1 ? 10 
ATOM 8155  C CB  . CYS G 5 62  ? 67.348  21.539  11.166 1.000 140.809 0 62  CYS GGG CB  1 ? 10 
ATOM 8156  S SG  . CYS G 5 62  ? 67.281  22.240  9.505  1.000 141.831 0 62  CYS GGG SG  1 ? 10 
ATOM 8157  N N   . GLN G 5 63  ? 66.548  21.950  14.436 1.000 141.154 0 63  GLN GGG N   1 ? 10 
ATOM 8158  C CA  . GLN G 5 63  ? 66.577  21.472  15.809 1.000 141.664 0 63  GLN GGG CA  1 ? 10 
ATOM 8159  C C   . GLN G 5 63  ? 65.444  20.483  16.033 1.000 145.933 0 63  GLN GGG C   1 ? 10 
ATOM 8160  O O   . GLN G 5 63  ? 64.347  20.649  15.493 1.000 145.168 0 63  GLN GGG O   1 ? 10 
ATOM 8161  C CB  . GLN G 5 63  ? 66.454  22.646  16.799 1.000 142.560 0 63  GLN GGG CB  1 ? 10 
ATOM 8162  C CG  . GLN G 5 63  ? 66.683  22.285  18.262 1.000 141.961 0 63  GLN GGG CG  1 ? 10 
ATOM 8163  C CD  . GLN G 5 63  ? 66.466  23.464  19.201 1.000 142.702 0 63  GLN GGG CD  1 ? 10 
ATOM 8164  O OE1 . GLN G 5 63  ? 66.352  24.611  18.767 1.000 132.341 0 63  GLN GGG OE1 1 ? 10 
ATOM 8165  N NE2 . GLN G 5 63  ? 66.400  23.181  20.497 1.000 147.718 0 63  GLN GGG NE2 1 ? 10 
ATOM 8166  N N   . GLY G 5 64  ? 65.725  19.462  16.829 1.000 155.078 0 64  GLY GGG N   1 ? 10 
ATOM 8167  C CA  . GLY G 5 64  ? 64.767  18.427  17.140 1.000 163.594 0 64  GLY GGG CA  1 ? 10 
ATOM 8168  C C   . GLY G 5 64  ? 65.172  17.721  18.414 1.000 161.907 0 64  GLY GGG C   1 ? 10 
ATOM 8169  O O   . GLY G 5 64  ? 66.006  18.210  19.177 1.000 157.472 0 64  GLY GGG O   1 ? 10 
ATOM 8170  N N   . GLY G 5 65  ? 64.581  16.553  18.647 1.000 174.124 0 65  GLY GGG N   1 ? 10 
ATOM 8171  C CA  . GLY G 5 65  ? 64.988  15.764  19.789 1.000 179.058 0 65  GLY GGG CA  1 ? 10 
ATOM 8172  C C   . GLY G 5 65  ? 64.130  15.899  21.026 1.000 181.345 0 65  GLY GGG C   1 ? 10 
ATOM 8173  O O   . GLY G 5 65  ? 64.454  15.280  22.047 1.000 186.263 0 65  GLY GGG O   1 ? 10 
ATOM 8174  N N   . ASP G 5 66  ? 63.053  16.688  20.985 1.000 169.308 0 66  ASP GGG N   1 ? 10 
ATOM 8175  C CA  . ASP G 5 66  ? 62.189  16.798  22.159 1.000 176.430 0 66  ASP GGG CA  1 ? 10 
ATOM 8176  C C   . ASP G 5 66  ? 61.135  15.700  22.114 1.000 185.104 0 66  ASP GGG C   1 ? 10 
ATOM 8177  O O   . ASP G 5 66  ? 60.004  15.880  21.656 1.000 184.145 0 66  ASP GGG O   1 ? 10 
ATOM 8178  C CB  . ASP G 5 66  ? 61.544  18.177  22.218 1.000 173.963 0 66  ASP GGG CB  1 ? 10 
ATOM 8179  C CG  . ASP G 5 66  ? 60.621  18.353  23.422 1.000 178.296 0 66  ASP GGG CG  1 ? 10 
ATOM 8180  O OD1 . ASP G 5 66  ? 60.432  17.399  24.207 1.000 182.843 0 66  ASP GGG OD1 1 ? 10 
ATOM 8181  O OD2 . ASP G 5 66  ? 60.072  19.462  23.579 1.000 180.880 0 66  ASP GGG OD2 1 ? 10 
ATOM 8182  N N   . PHE G 5 67  ? 61.539  14.529  22.599 1.000 190.121 0 67  PHE GGG N   1 ? 10 
ATOM 8183  C CA  . PHE G 5 67  ? 60.696  13.348  22.574 1.000 189.848 0 67  PHE GGG CA  1 ? 10 
ATOM 8184  C C   . PHE G 5 67  ? 59.847  13.222  23.828 1.000 192.963 0 67  PHE GGG C   1 ? 10 
ATOM 8185  O O   . PHE G 5 67  ? 59.109  12.242  23.956 1.000 200.303 0 67  PHE GGG O   1 ? 10 
ATOM 8186  C CB  . PHE G 5 67  ? 61.534  12.081  22.347 1.000 191.863 0 67  PHE GGG CB  1 ? 10 
ATOM 8187  C CG  . PHE G 5 67  ? 62.648  11.883  23.331 1.000 198.480 0 67  PHE GGG CG  1 ? 10 
ATOM 8188  C CD1 . PHE G 5 67  ? 62.435  11.260  24.553 1.000 212.605 0 67  PHE GGG CD1 1 ? 10 
ATOM 8189  C CD2 . PHE G 5 67  ? 63.930  12.287  23.006 1.000 197.512 0 67  PHE GGG CD2 1 ? 10 
ATOM 8190  C CE1 . PHE G 5 67  ? 63.483  11.073  25.441 1.000 222.939 0 67  PHE GGG CE1 1 ? 10 
ATOM 8191  C CE2 . PHE G 5 67  ? 64.972  12.096  23.881 1.000 204.904 0 67  PHE GGG CE2 1 ? 10 
ATOM 8192  C CZ  . PHE G 5 67  ? 64.752  11.494  25.101 1.000 220.591 0 67  PHE GGG CZ  1 ? 10 
ATOM 8193  N N   . THR G 5 68  ? 59.909  14.192  24.747 1.000 197.962 0 68  THR GGG N   1 ? 10 
ATOM 8194  C CA  . THR G 5 68  ? 59.063  14.131  25.931 1.000 201.702 0 68  THR GGG CA  1 ? 10 
ATOM 8195  C C   . THR G 5 68  ? 57.922  15.129  25.901 1.000 195.777 0 68  THR GGG C   1 ? 10 
ATOM 8196  O O   . THR G 5 68  ? 56.862  14.845  26.462 1.000 197.654 0 68  THR GGG O   1 ? 10 
ATOM 8197  C CB  . THR G 5 68  ? 59.896  14.390  27.198 1.000 206.044 0 68  THR GGG CB  1 ? 10 
ATOM 8198  O OG1 . THR G 5 68  ? 61.193  13.792  27.067 1.000 220.641 0 68  THR GGG OG1 1 ? 10 
ATOM 8199  C CG2 . THR G 5 68  ? 59.194  13.845  28.438 1.000 211.334 0 68  THR GGG CG2 1 ? 10 
ATOM 8200  N N   . ARG G 5 69  ? 58.105  16.282  25.256 1.000 190.707 0 69  ARG GGG N   1 ? 10 
ATOM 8201  C CA  . ARG G 5 69  ? 57.063  17.295  25.195 1.000 189.014 0 69  ARG GGG CA  1 ? 10 
ATOM 8202  C C   . ARG G 5 69  ? 56.802  17.804  23.786 1.000 188.774 0 69  ARG GGG C   1 ? 10 
ATOM 8203  O O   . ARG G 5 69  ? 55.799  18.498  23.582 1.000 189.604 0 69  ARG GGG O   1 ? 10 
ATOM 8204  C CB  . ARG G 5 69  ? 57.386  18.474  26.126 1.000 190.084 0 69  ARG GGG CB  1 ? 10 
ATOM 8205  C CG  . ARG G 5 69  ? 57.440  18.062  27.593 1.000 198.878 0 69  ARG GGG CG  1 ? 10 
ATOM 8206  C CD  . ARG G 5 69  ? 56.062  17.648  28.111 1.000 207.016 0 69  ARG GGG CD  1 ? 10 
ATOM 8207  N NE  . ARG G 5 69  ? 56.125  16.494  29.004 1.000 213.300 0 69  ARG GGG NE  1 ? 10 
ATOM 8208  C CZ  . ARG G 5 69  ? 56.638  16.499  30.227 1.000 210.155 0 69  ARG GGG CZ  1 ? 10 
ATOM 8209  N NH1 . ARG G 5 69  ? 57.128  17.607  30.759 1.000 209.603 0 69  ARG GGG NH1 1 ? 10 
ATOM 8210  N NH2 . ARG G 5 69  ? 56.639  15.371  30.933 1.000 205.682 0 69  ARG GGG NH2 1 ? 10 
ATOM 8211  N N   . HIS G 5 70  ? 57.658  17.481  22.811 1.000 189.031 0 70  HIS GGG N   1 ? 10 
ATOM 8212  C CA  . HIS G 5 70  ? 57.385  17.706  21.393 1.000 181.469 0 70  HIS GGG CA  1 ? 10 
ATOM 8213  C C   . HIS G 5 70  ? 57.293  19.181  20.996 1.000 179.429 0 70  HIS GGG C   1 ? 10 
ATOM 8214  O O   . HIS G 5 70  ? 56.710  19.506  19.953 1.000 177.764 0 70  HIS GGG O   1 ? 10 
ATOM 8215  C CB  . HIS G 5 70  ? 56.195  16.869  20.913 1.000 186.086 0 70  HIS GGG CB  1 ? 10 
ATOM 8216  C CG  . HIS G 5 70  ? 56.555  15.424  20.739 1.000 191.170 0 70  HIS GGG CG  1 ? 10 
ATOM 8217  N ND1 . HIS G 5 70  ? 56.099  14.417  21.563 1.000 201.557 0 70  HIS GGG ND1 1 ? 10 
ATOM 8218  C CD2 . HIS G 5 70  ? 57.403  14.835  19.862 1.000 190.903 0 70  HIS GGG CD2 1 ? 10 
ATOM 8219  C CE1 . HIS G 5 70  ? 56.618  13.264  21.173 1.000 202.063 0 70  HIS GGG CE1 1 ? 10 
ATOM 8220  N NE2 . HIS G 5 70  ? 57.414  13.492  20.145 1.000 205.293 0 70  HIS GGG NE2 1 ? 10 
ATOM 8221  N N   . ASN G 5 71  ? 57.871  20.092  21.794 1.000 175.072 0 71  ASN GGG N   1 ? 10 
ATOM 8222  C CA  . ASN G 5 71  ? 57.730  21.524  21.560 1.000 161.778 0 71  ASN GGG CA  1 ? 10 
ATOM 8223  C C   . ASN G 5 71  ? 58.995  22.310  21.885 1.000 150.793 0 71  ASN GGG C   1 ? 10 
ATOM 8224  O O   . ASN G 5 71  ? 58.973  23.541  21.800 1.000 149.523 0 71  ASN GGG O   1 ? 10 
ATOM 8225  C CB  . ASN G 5 71  ? 56.562  22.094  22.395 1.000 166.739 0 71  ASN GGG CB  1 ? 10 
ATOM 8226  C CG  . ASN G 5 71  ? 56.796  21.980  23.905 1.000 168.474 0 71  ASN GGG CG  1 ? 10 
ATOM 8227  O OD1 . ASN G 5 71  ? 57.600  21.168  24.367 1.000 173.613 0 71  ASN GGG OD1 1 ? 10 
ATOM 8228  N ND2 . ASN G 5 71  ? 56.071  22.784  24.677 1.000 159.356 0 71  ASN GGG ND2 1 ? 10 
ATOM 8229  N N   . GLY G 5 72  ? 60.093  21.643  22.238 1.000 149.064 0 72  GLY GGG N   1 ? 10 
ATOM 8230  C CA  . GLY G 5 72  ? 61.350  22.283  22.562 1.000 149.473 0 72  GLY GGG CA  1 ? 10 
ATOM 8231  C C   . GLY G 5 72  ? 61.626  22.410  24.042 1.000 157.227 0 72  GLY GGG C   1 ? 10 
ATOM 8232  O O   . GLY G 5 72  ? 62.698  22.892  24.421 1.000 159.379 0 72  GLY GGG O   1 ? 10 
ATOM 8233  N N   . THR G 5 73  ? 60.697  21.991  24.885 1.000 160.698 0 73  THR GGG N   1 ? 10 
ATOM 8234  C CA  . THR G 5 73  ? 60.812  22.129  26.325 1.000 151.596 0 73  THR GGG CA  1 ? 10 
ATOM 8235  C C   . THR G 5 73  ? 61.147  20.836  27.048 1.000 150.720 0 73  THR GGG C   1 ? 10 
ATOM 8236  O O   . THR G 5 73  ? 61.415  20.862  28.255 1.000 153.664 0 73  THR GGG O   1 ? 10 
ATOM 8237  C CB  . THR G 5 73  ? 59.533  22.735  26.874 1.000 152.192 0 73  THR GGG CB  1 ? 10 
ATOM 8238  O OG1 . THR G 5 73  ? 59.105  23.781  25.990 1.000 159.958 0 73  THR GGG OG1 1 ? 10 
ATOM 8239  C CG2 . THR G 5 73  ? 59.824  23.341  28.209 1.000 156.014 0 73  THR GGG CG2 1 ? 10 
ATOM 8240  N N   . GLY G 5 74  ? 61.249  19.731  26.333 1.000 157.221 0 74  GLY GGG N   1 ? 10 
ATOM 8241  C CA  . GLY G 5 74  ? 61.434  18.453  26.979 1.000 170.907 0 74  GLY GGG CA  1 ? 10 
ATOM 8242  C C   . GLY G 5 74  ? 62.697  17.728  26.587 1.000 167.136 0 74  GLY GGG C   1 ? 10 
ATOM 8243  O O   . GLY G 5 74  ? 63.694  18.370  26.239 1.000 148.944 0 74  GLY GGG O   1 ? 10 
ATOM 8244  N N   . GLY G 5 75  ? 62.694  16.405  26.681 1.000 172.993 0 75  GLY GGG N   1 ? 10 
ATOM 8245  C CA  . GLY G 5 75  ? 63.916  15.664  26.473 1.000 182.206 0 75  GLY GGG CA  1 ? 10 
ATOM 8246  C C   . GLY G 5 75  ? 64.556  15.212  27.779 1.000 184.060 0 75  GLY GGG C   1 ? 10 
ATOM 8247  O O   . GLY G 5 75  ? 64.254  15.704  28.872 1.000 176.812 0 75  GLY GGG O   1 ? 10 
ATOM 8248  N N   . LYS G 5 76  ? 65.473  14.256  27.644 1.000 189.851 0 76  LYS GGG N   1 ? 10 
ATOM 8249  C CA  . LYS G 5 76  ? 66.261  13.767  28.763 1.000 193.669 0 76  LYS GGG CA  1 ? 10 
ATOM 8250  C C   . LYS G 5 76  ? 67.546  13.147  28.226 1.000 202.082 0 76  LYS GGG C   1 ? 10 
ATOM 8251  O O   . LYS G 5 76  ? 67.597  12.651  27.097 1.000 209.672 0 76  LYS GGG O   1 ? 10 
ATOM 8252  C CB  . LYS G 5 76  ? 65.432  12.737  29.555 1.000 198.391 0 76  LYS GGG CB  1 ? 10 
ATOM 8253  C CG  . LYS G 5 76  ? 66.185  11.819  30.516 1.000 218.787 0 76  LYS GGG CG  1 ? 10 
ATOM 8254  C CD  . LYS G 5 76  ? 65.216  10.885  31.227 1.000 225.034 0 76  LYS GGG CD  1 ? 10 
ATOM 8255  C CE  . LYS G 5 76  ? 64.454  10.064  30.201 1.000 230.628 0 76  LYS GGG CE  1 ? 10 
ATOM 8256  N NZ  . LYS G 5 76  ? 63.621  9.005   30.820 1.000 241.892 0 76  LYS GGG NZ  1 ? 10 
ATOM 8257  N N   . SER G 5 77  ? 68.573  13.183  29.071 1.000 211.487 0 77  SER GGG N   1 ? 10 
ATOM 8258  C CA  . SER G 5 77  ? 69.905  12.626  28.877 1.000 228.135 0 77  SER GGG CA  1 ? 10 
ATOM 8259  C C   . SER G 5 77  ? 69.925  11.164  29.309 1.000 243.335 0 77  SER GGG C   1 ? 10 
ATOM 8260  O O   . SER G 5 77  ? 68.954  10.642  29.854 1.000 262.365 0 77  SER GGG O   1 ? 10 
ATOM 8261  C CB  . SER G 5 77  ? 70.954  13.429  29.658 1.000 235.551 0 77  SER GGG CB  1 ? 10 
ATOM 8262  O OG  . SER G 5 77  ? 70.635  13.524  31.037 1.000 255.701 0 77  SER GGG OG  1 ? 10 
ATOM 8263  N N   . ILE G 5 78  ? 71.046  10.484  29.058 1.000 253.583 0 78  ILE GGG N   1 ? 10 
ATOM 8264  C CA  . ILE G 5 78  ? 71.113  9.117   29.547 1.000 241.382 0 78  ILE GGG CA  1 ? 10 
ATOM 8265  C C   . ILE G 5 78  ? 71.275  9.150   31.049 1.000 259.253 0 78  ILE GGG C   1 ? 10 
ATOM 8266  O O   . ILE G 5 78  ? 71.241  8.108   31.708 1.000 265.788 0 78  ILE GGG O   1 ? 10 
ATOM 8267  C CB  . ILE G 5 78  ? 72.267  8.347   28.879 1.000 219.069 0 78  ILE GGG CB  1 ? 10 
ATOM 8268  C CG1 . ILE G 5 78  ? 73.603  8.970   29.300 1.000 225.343 0 78  ILE GGG CG1 1 ? 10 
ATOM 8269  C CG2 . ILE G 5 78  ? 72.071  8.361   27.371 1.000 235.003 0 78  ILE GGG CG2 1 ? 10 
ATOM 8270  C CD1 . ILE G 5 78  ? 74.806  8.454   28.562 1.000 223.719 0 78  ILE GGG CD1 1 ? 10 
ATOM 8271  N N   . TYR G 5 79  ? 71.465  10.355  31.574 1.000 250.288 0 79  TYR GGG N   1 ? 10 
ATOM 8272  C CA  . TYR G 5 79  ? 71.611  10.697  32.972 1.000 251.045 0 79  TYR GGG CA  1 ? 10 
ATOM 8273  C C   . TYR G 5 79  ? 70.256  11.307  33.304 1.000 256.189 0 79  TYR GGG C   1 ? 10 
ATOM 8274  O O   . TYR G 5 79  ? 69.608  11.876  32.421 1.000 275.077 0 79  TYR GGG O   1 ? 10 
ATOM 8275  C CB  . TYR G 5 79  ? 72.716  11.729  33.199 1.000 253.324 0 79  TYR GGG CB  1 ? 10 
ATOM 8276  C CG  . TYR G 5 79  ? 74.029  11.406  32.525 1.000 263.275 0 79  TYR GGG CG  1 ? 10 
ATOM 8277  C CD1 . TYR G 5 79  ? 74.756  10.272  32.858 1.000 277.252 0 79  TYR GGG CD1 1 ? 10 
ATOM 8278  C CD2 . TYR G 5 79  ? 74.530  12.239  31.532 1.000 264.683 0 79  TYR GGG CD2 1 ? 10 
ATOM 8279  C CE1 . TYR G 5 79  ? 75.958  9.986   32.225 1.000 277.879 0 79  TYR GGG CE1 1 ? 10 
ATOM 8280  C CE2 . TYR G 5 79  ? 75.719  11.962  30.896 1.000 265.549 0 79  TYR GGG CE2 1 ? 10 
ATOM 8281  C CZ  . TYR G 5 79  ? 76.430  10.839  31.243 1.000 269.824 0 79  TYR GGG CZ  1 ? 10 
ATOM 8282  O OH  . TYR G 5 79  ? 77.613  10.585  30.589 1.000 273.526 0 79  TYR GGG OH  1 ? 10 
ATOM 8283  N N   . GLY G 5 80  ? 69.803  11.171  34.544 1.000 252.432 0 80  GLY GGG N   1 ? 10 
ATOM 8284  C CA  . GLY G 5 80  ? 68.445  11.607  34.824 1.000 238.307 0 80  GLY GGG CA  1 ? 10 
ATOM 8285  C C   . GLY G 5 80  ? 68.239  13.078  34.492 1.000 227.184 0 80  GLY GGG C   1 ? 10 
ATOM 8286  O O   . GLY G 5 80  ? 68.829  13.944  35.141 1.000 224.499 0 80  GLY GGG O   1 ? 10 
ATOM 8287  N N   . GLU G 5 81  ? 67.454  13.363  33.449 1.000 219.413 0 81  GLU GGG N   1 ? 10 
ATOM 8288  C CA  . GLU G 5 81  ? 67.190  14.713  32.942 1.000 214.228 0 81  GLU GGG CA  1 ? 10 
ATOM 8289  C C   . GLU G 5 81  ? 68.397  15.528  32.470 1.000 219.133 0 81  GLU GGG C   1 ? 10 
ATOM 8290  O O   . GLU G 5 81  ? 68.858  15.365  31.335 1.000 223.643 0 81  GLU GGG O   1 ? 10 
ATOM 8291  C CB  . GLU G 5 81  ? 66.440  15.535  34.003 1.000 213.759 0 81  GLU GGG CB  1 ? 10 
ATOM 8292  C CG  . GLU G 5 81  ? 65.194  16.265  33.485 1.000 214.550 0 81  GLU GGG CG  1 ? 10 
ATOM 8293  C CD  . GLU G 5 81  ? 64.366  16.917  34.588 1.000 213.244 0 81  GLU GGG CD  1 ? 10 
ATOM 8294  O OE1 . GLU G 5 81  ? 64.578  16.586  35.774 1.000 210.826 0 81  GLU GGG OE1 1 ? 10 
ATOM 8295  O OE2 . GLU G 5 81  ? 63.513  17.775  34.270 1.000 210.927 0 81  GLU GGG OE2 1 ? 10 
ATOM 8296  N N   . LYS G 5 82  ? 68.894  16.430  33.315 1.000 221.871 0 82  LYS GGG N   1 ? 10 
ATOM 8297  C CA  . LYS G 5 82  ? 69.986  17.315  32.927 1.000 224.770 0 82  LYS GGG CA  1 ? 10 
ATOM 8298  C C   . LYS G 5 82  ? 71.296  16.579  32.661 1.000 232.775 0 82  LYS GGG C   1 ? 10 
ATOM 8299  O O   . LYS G 5 82  ? 71.532  15.469  33.146 1.000 244.474 0 82  LYS GGG O   1 ? 10 
ATOM 8300  C CB  . LYS G 5 82  ? 70.289  18.322  34.043 1.000 223.209 0 82  LYS GGG CB  1 ? 10 
ATOM 8301  C CG  . LYS G 5 82  ? 69.325  18.327  35.222 1.000 225.483 0 82  LYS GGG CG  1 ? 10 
ATOM 8302  C CD  . LYS G 5 82  ? 68.045  19.087  34.934 1.000 222.683 0 82  LYS GGG CD  1 ? 10 
ATOM 8303  C CE  . LYS G 5 82  ? 67.111  19.058  36.139 1.000 222.155 0 82  LYS GGG CE  1 ? 10 
ATOM 8304  N NZ  . LYS G 5 82  ? 65.798  19.707  35.855 1.000 221.141 0 82  LYS GGG NZ  1 ? 10 
ATOM 8305  N N   . PHE G 5 83  ? 72.158  17.221  31.868 1.000 249.834 0 83  PHE GGG N   1 ? 10 
ATOM 8306  C CA  . PHE G 5 83  ? 73.529  16.757  31.748 1.000 257.477 0 83  PHE GGG CA  1 ? 10 
ATOM 8307  C C   . PHE G 5 83  ? 74.448  17.969  31.670 1.000 253.762 0 83  PHE GGG C   1 ? 10 
ATOM 8308  O O   . PHE G 5 83  ? 74.045  19.039  31.205 1.000 250.619 0 83  PHE GGG O   1 ? 10 
ATOM 8309  C CB  . PHE G 5 83  ? 73.598  15.890  30.460 1.000 261.775 0 83  PHE GGG CB  1 ? 10 
ATOM 8310  C CG  . PHE G 5 83  ? 74.948  15.844  29.774 1.000 268.357 0 83  PHE GGG CG  1 ? 10 
ATOM 8311  C CD1 . PHE G 5 83  ? 76.085  15.352  30.391 1.000 280.334 0 83  PHE GGG CD1 1 ? 10 
ATOM 8312  C CD2 . PHE G 5 83  ? 75.055  16.320  28.472 1.000 265.355 0 83  PHE GGG CD2 1 ? 10 
ATOM 8313  C CE1 . PHE G 5 83  ? 77.304  15.338  29.712 1.000 285.393 0 83  PHE GGG CE1 1 ? 10 
ATOM 8314  C CE2 . PHE G 5 83  ? 76.256  16.309  27.797 1.000 272.547 0 83  PHE GGG CE2 1 ? 10 
ATOM 8315  C CZ  . PHE G 5 83  ? 77.383  15.818  28.412 1.000 280.286 0 83  PHE GGG CZ  1 ? 10 
ATOM 8316  N N   . GLU G 5 84  ? 75.703  17.776  32.074 1.000 244.389 0 84  GLU GGG N   1 ? 10 
ATOM 8317  C CA  . GLU G 5 84  ? 76.624  18.901  32.177 1.000 234.278 0 84  GLU GGG CA  1 ? 10 
ATOM 8318  C C   . GLU G 5 84  ? 77.132  19.305  30.794 1.000 232.441 0 84  GLU GGG C   1 ? 10 
ATOM 8319  O O   . GLU G 5 84  ? 77.090  18.518  29.846 1.000 233.921 0 84  GLU GGG O   1 ? 10 
ATOM 8320  C CB  . GLU G 5 84  ? 77.760  18.628  33.162 1.000 231.252 0 84  GLU GGG CB  1 ? 10 
ATOM 8321  C CG  . GLU G 5 84  ? 78.805  17.643  32.755 1.000 236.314 0 84  GLU GGG CG  1 ? 10 
ATOM 8322  C CD  . GLU G 5 84  ? 79.875  17.523  33.820 1.000 235.902 0 84  GLU GGG CD  1 ? 10 
ATOM 8323  O OE1 . GLU G 5 84  ? 79.606  17.930  34.976 1.000 236.664 0 84  GLU GGG OE1 1 ? 10 
ATOM 8324  O OE2 . GLU G 5 84  ? 80.969  17.012  33.509 1.000 231.791 0 84  GLU GGG OE2 1 ? 10 
ATOM 8325  N N   . ASP G 5 85  ? 77.637  20.530  30.675 1.000 225.197 0 85  ASP GGG N   1 ? 10 
ATOM 8326  C CA  . ASP G 5 85  ? 78.408  20.876  29.481 1.000 223.473 0 85  ASP GGG CA  1 ? 10 
ATOM 8327  C C   . ASP G 5 85  ? 79.765  20.175  29.550 1.000 225.677 0 85  ASP GGG C   1 ? 10 
ATOM 8328  O O   . ASP G 5 85  ? 80.578  20.480  30.430 1.000 227.285 0 85  ASP GGG O   1 ? 10 
ATOM 8329  C CB  . ASP G 5 85  ? 78.562  22.384  29.316 1.000 225.292 0 85  ASP GGG CB  1 ? 10 
ATOM 8330  C CG  . ASP G 5 85  ? 77.240  23.082  29.066 1.000 224.369 0 85  ASP GGG CG  1 ? 10 
ATOM 8331  O OD1 . ASP G 5 85  ? 76.188  22.414  29.135 1.000 224.453 0 85  ASP GGG OD1 1 ? 10 
ATOM 8332  O OD2 . ASP G 5 85  ? 77.255  24.299  28.782 1.000 222.577 0 85  ASP GGG OD2 1 ? 10 
ATOM 8333  N N   . GLU G 5 86  ? 80.021  19.236  28.638 1.000 229.802 0 86  GLU GGG N   1 ? 10 
ATOM 8334  C CA  . GLU G 5 86  ? 81.204  18.386  28.770 1.000 232.298 0 86  GLU GGG CA  1 ? 10 
ATOM 8335  C C   . GLU G 5 86  ? 82.493  19.156  28.493 1.000 240.915 0 86  GLU GGG C   1 ? 10 
ATOM 8336  O O   . GLU G 5 86  ? 83.432  19.118  29.296 1.000 243.044 0 86  GLU GGG O   1 ? 10 
ATOM 8337  C CB  . GLU G 5 86  ? 81.114  17.162  27.860 1.000 234.573 0 86  GLU GGG CB  1 ? 10 
ATOM 8338  C CG  . GLU G 5 86  ? 82.281  16.197  28.086 1.000 234.148 0 86  GLU GGG CG  1 ? 10 
ATOM 8339  C CD  . GLU G 5 86  ? 82.115  14.867  27.385 1.000 236.092 0 86  GLU GGG CD  1 ? 10 
ATOM 8340  O OE1 . GLU G 5 86  ? 81.176  14.728  26.579 1.000 241.833 0 86  GLU GGG OE1 1 ? 10 
ATOM 8341  O OE2 . GLU G 5 86  ? 82.933  13.959  27.638 1.000 240.287 0 86  GLU GGG OE2 1 ? 10 
ATOM 8342  N N   . ASN G 5 87  ? 82.553  19.869  27.368 1.000 240.544 0 87  ASN GGG N   1 ? 10 
ATOM 8343  C CA  . ASN G 5 87  ? 83.691  20.722  27.040 1.000 239.321 0 87  ASN GGG CA  1 ? 10 
ATOM 8344  C C   . ASN G 5 87  ? 83.321  21.629  25.871 1.000 244.426 0 87  ASN GGG C   1 ? 10 
ATOM 8345  O O   . ASN G 5 87  ? 82.266  21.479  25.249 1.000 246.349 0 87  ASN GGG O   1 ? 10 
ATOM 8346  C CB  . ASN G 5 87  ? 84.947  19.889  26.732 1.000 238.925 0 87  ASN GGG CB  1 ? 10 
ATOM 8347  C CG  . ASN G 5 87  ? 84.803  19.027  25.483 1.000 243.553 0 87  ASN GGG CG  1 ? 10 
ATOM 8348  O OD1 . ASN G 5 87  ? 84.474  19.513  24.400 1.000 244.410 0 87  ASN GGG OD1 1 ? 10 
ATOM 8349  N ND2 . ASN G 5 87  ? 85.055  17.731  25.636 1.000 248.751 0 87  ASN GGG ND2 1 ? 10 
ATOM 8350  N N   . PHE G 5 88  ? 84.217  22.578  25.585 1.000 244.677 0 88  PHE GGG N   1 ? 10 
ATOM 8351  C CA  . PHE G 5 88  ? 84.087  23.516  24.474 1.000 241.796 0 88  PHE GGG CA  1 ? 10 
ATOM 8352  C C   . PHE G 5 88  ? 85.290  23.441  23.541 1.000 242.237 0 88  PHE GGG C   1 ? 10 
ATOM 8353  O O   . PHE G 5 88  ? 85.628  24.421  22.872 1.000 238.406 0 88  PHE GGG O   1 ? 10 
ATOM 8354  C CB  . PHE G 5 88  ? 83.922  24.956  24.971 1.000 240.939 0 88  PHE GGG CB  1 ? 10 
ATOM 8355  C CG  . PHE G 5 88  ? 82.691  25.191  25.801 1.000 243.765 0 88  PHE GGG CG  1 ? 10 
ATOM 8356  C CD1 . PHE G 5 88  ? 81.502  24.543  25.512 1.000 236.413 0 88  PHE GGG CD1 1 ? 10 
ATOM 8357  C CD2 . PHE G 5 88  ? 82.722  26.082  26.863 1.000 244.415 0 88  PHE GGG CD2 1 ? 10 
ATOM 8358  C CE1 . PHE G 5 88  ? 80.370  24.769  26.276 1.000 226.250 0 88  PHE GGG CE1 1 ? 10 
ATOM 8359  C CE2 . PHE G 5 88  ? 81.594  26.311  27.630 1.000 233.249 0 88  PHE GGG CE2 1 ? 10 
ATOM 8360  C CZ  . PHE G 5 88  ? 80.417  25.654  27.336 1.000 223.868 0 88  PHE GGG CZ  1 ? 10 
ATOM 8361  N N   . ILE G 5 89  ? 85.963  22.288  23.516 1.000 244.025 0 89  ILE GGG N   1 ? 10 
ATOM 8362  C CA  . ILE G 5 89  ? 87.112  22.110  22.631 1.000 243.975 0 89  ILE GGG CA  1 ? 10 
ATOM 8363  C C   . ILE G 5 89  ? 86.691  22.310  21.180 1.000 237.362 0 89  ILE GGG C   1 ? 10 
ATOM 8364  O O   . ILE G 5 89  ? 87.343  23.033  20.417 1.000 234.527 0 89  ILE GGG O   1 ? 10 
ATOM 8365  C CB  . ILE G 5 89  ? 87.740  20.718  22.839 1.000 242.281 0 89  ILE GGG CB  1 ? 10 
ATOM 8366  C CG1 . ILE G 5 89  ? 88.044  20.466  24.316 1.000 246.621 0 89  ILE GGG CG1 1 ? 10 
ATOM 8367  C CG2 . ILE G 5 89  ? 88.995  20.564  21.994 1.000 241.541 0 89  ILE GGG CG2 1 ? 10 
ATOM 8368  C CD1 . ILE G 5 89  ? 88.541  19.062  24.594 1.000 246.756 0 89  ILE GGG CD1 1 ? 10 
ATOM 8369  N N   . LEU G 5 90  ? 85.588  21.680  20.784 1.000 234.454 0 90  LEU GGG N   1 ? 10 
ATOM 8370  C CA  . LEU G 5 90  ? 85.109  21.741  19.411 1.000 223.726 0 90  LEU GGG CA  1 ? 10 
ATOM 8371  C C   . LEU G 5 90  ? 84.450  23.082  19.105 1.000 217.610 0 90  LEU GGG C   1 ? 10 
ATOM 8372  O O   . LEU G 5 90  ? 83.900  23.751  19.984 1.000 218.727 0 90  LEU GGG O   1 ? 10 
ATOM 8373  C CB  . LEU G 5 90  ? 84.131  20.599  19.135 1.000 213.567 0 90  LEU GGG CB  1 ? 10 
ATOM 8374  C CG  . LEU G 5 90  ? 84.761  19.365  18.485 1.000 209.418 0 90  LEU GGG CG  1 ? 10 
ATOM 8375  C CD1 . LEU G 5 90  ? 83.723  18.279  18.265 1.000 207.245 0 90  LEU GGG CD1 1 ? 10 
ATOM 8376  C CD2 . LEU G 5 90  ? 85.435  19.736  17.172 1.000 194.443 0 90  LEU GGG CD2 1 ? 10 
ATOM 8377  N N   . LYS G 5 91  ? 84.515  23.469  17.834 1.000 212.096 0 91  LYS GGG N   1 ? 10 
ATOM 8378  C CA  . LYS G 5 91  ? 84.000  24.743  17.363 1.000 208.182 0 91  LYS GGG CA  1 ? 10 
ATOM 8379  C C   . LYS G 5 91  ? 82.934  24.520  16.298 1.000 215.153 0 91  LYS GGG C   1 ? 10 
ATOM 8380  O O   . LYS G 5 91  ? 82.942  23.510  15.589 1.000 215.258 0 91  LYS GGG O   1 ? 10 
ATOM 8381  C CB  . LYS G 5 91  ? 85.124  25.607  16.779 1.000 207.397 0 91  LYS GGG CB  1 ? 10 
ATOM 8382  C CG  . LYS G 5 91  ? 85.001  27.099  17.036 1.000 200.092 0 91  LYS GGG CG  1 ? 10 
ATOM 8383  C CD  . LYS G 5 91  ? 85.561  27.467  18.397 1.000 195.764 0 91  LYS GGG CD  1 ? 10 
ATOM 8384  C CE  . LYS G 5 91  ? 85.753  28.967  18.520 1.000 194.712 0 91  LYS GGG CE  1 ? 10 
ATOM 8385  N NZ  . LYS G 5 91  ? 86.529  29.321  19.739 1.000 205.322 0 91  LYS GGG NZ  1 ? 10 
ATOM 8386  N N   . HIS G 5 92  ? 81.996  25.463  16.219 1.000 227.813 0 92  HIS GGG N   1 ? 10 
ATOM 8387  C CA  . HIS G 5 92  ? 80.962  25.500  15.183 1.000 227.870 0 92  HIS GGG CA  1 ? 10 
ATOM 8388  C C   . HIS G 5 92  ? 81.618  26.040  13.918 1.000 232.354 0 92  HIS GGG C   1 ? 10 
ATOM 8389  O O   . HIS G 5 92  ? 81.602  27.242  13.649 1.000 230.655 0 92  HIS GGG O   1 ? 10 
ATOM 8390  C CB  . HIS G 5 92  ? 79.782  26.362  15.611 1.000 223.887 0 92  HIS GGG CB  1 ? 10 
ATOM 8391  C CG  . HIS G 5 92  ? 79.085  25.868  16.839 1.000 224.808 0 92  HIS GGG CG  1 ? 10 
ATOM 8392  N ND1 . HIS G 5 92  ? 79.535  26.151  18.110 1.000 232.542 0 92  HIS GGG ND1 1 ? 10 
ATOM 8393  C CD2 . HIS G 5 92  ? 77.976  25.108  16.993 1.000 218.152 0 92  HIS GGG CD2 1 ? 10 
ATOM 8394  C CE1 . HIS G 5 92  ? 78.728  25.595  18.995 1.000 227.859 0 92  HIS GGG CE1 1 ? 10 
ATOM 8395  N NE2 . HIS G 5 92  ? 77.775  24.953  18.343 1.000 220.021 0 92  HIS GGG NE2 1 ? 10 
ATOM 8396  N N   . THR G 5 93  ? 82.200  25.146  13.118 1.000 227.168 0 93  THR GGG N   1 ? 10 
ATOM 8397  C CA  . THR G 5 93  ? 83.086  25.564  12.038 1.000 219.813 0 93  THR GGG CA  1 ? 10 
ATOM 8398  C C   . THR G 5 93  ? 82.403  25.751  10.690 1.000 206.825 0 93  THR GGG C   1 ? 10 
ATOM 8399  O O   . THR G 5 93  ? 83.038  26.278  9.771  1.000 203.171 0 93  THR GGG O   1 ? 10 
ATOM 8400  C CB  . THR G 5 93  ? 84.208  24.533  11.859 1.000 228.406 0 93  THR GGG CB  1 ? 10 
ATOM 8401  O OG1 . THR G 5 93  ? 83.681  23.363  11.218 1.000 230.722 0 93  THR GGG OG1 1 ? 10 
ATOM 8402  C CG2 . THR G 5 93  ? 84.827  24.156  13.198 1.000 228.475 0 93  THR GGG CG2 1 ? 10 
ATOM 8403  N N   . GLY G 5 94  ? 81.147  25.353  10.535 1.000 193.286 0 94  GLY GGG N   1 ? 10 
ATOM 8404  C CA  . GLY G 5 94  ? 80.501  25.471  9.249  1.000 186.340 0 94  GLY GGG CA  1 ? 10 
ATOM 8405  C C   . GLY G 5 94  ? 79.256  24.620  9.153  1.000 179.482 0 94  GLY GGG C   1 ? 10 
ATOM 8406  O O   . GLY G 5 94  ? 78.783  24.063  10.148 1.000 181.503 0 94  GLY GGG O   1 ? 10 
ATOM 8407  N N   . PRO G 5 95  ? 78.687  24.522  7.950  1.000 170.396 0 95  PRO GGG N   1 ? 10 
ATOM 8408  C CA  . PRO G 5 95  ? 77.517  23.655  7.770  1.000 162.524 0 95  PRO GGG CA  1 ? 10 
ATOM 8409  C C   . PRO G 5 95  ? 77.878  22.226  8.142  1.000 174.367 0 95  PRO GGG C   1 ? 10 
ATOM 8410  O O   . PRO G 5 95  ? 78.987  21.754  7.878  1.000 191.028 0 95  PRO GGG O   1 ? 10 
ATOM 8411  C CB  . PRO G 5 95  ? 77.188  23.794  6.278  1.000 154.100 0 95  PRO GGG CB  1 ? 10 
ATOM 8412  C CG  . PRO G 5 95  ? 77.878  25.043  5.837  1.000 160.783 0 95  PRO GGG CG  1 ? 10 
ATOM 8413  C CD  . PRO G 5 95  ? 79.087  25.191  6.702  1.000 170.236 0 95  PRO GGG CD  1 ? 10 
ATOM 8414  N N   . GLY G 5 96  ? 76.927  21.535  8.758  1.000 169.295 0 96  GLY GGG N   1 ? 10 
ATOM 8415  C CA  . GLY G 5 96  ? 77.081  20.136  9.073  1.000 166.489 0 96  GLY GGG CA  1 ? 10 
ATOM 8416  C C   . GLY G 5 96  ? 77.507  19.903  10.504 1.000 167.841 0 96  GLY GGG C   1 ? 10 
ATOM 8417  O O   . GLY G 5 96  ? 77.459  18.760  10.975 1.000 182.659 0 96  GLY GGG O   1 ? 10 
ATOM 8418  N N   . ILE G 5 97  ? 77.937  20.960  11.197 1.000 168.461 0 97  ILE GGG N   1 ? 10 
ATOM 8419  C CA  . ILE G 5 97  ? 78.294  20.858  12.605 1.000 171.538 0 97  ILE GGG CA  1 ? 10 
ATOM 8420  C C   . ILE G 5 97  ? 77.066  20.463  13.412 1.000 170.451 0 97  ILE GGG C   1 ? 10 
ATOM 8421  O O   . ILE G 5 97  ? 75.983  21.041  13.254 1.000 161.833 0 97  ILE GGG O   1 ? 10 
ATOM 8422  C CB  . ILE G 5 97  ? 78.892  22.189  13.089 1.000 174.999 0 97  ILE GGG CB  1 ? 10 
ATOM 8423  C CG1 . ILE G 5 97  ? 80.369  22.290  12.702 1.000 183.519 0 97  ILE GGG CG1 1 ? 10 
ATOM 8424  C CG2 . ILE G 5 97  ? 78.714  22.360  14.592 1.000 177.699 0 97  ILE GGG CG2 1 ? 10 
ATOM 8425  C CD1 . ILE G 5 97  ? 81.292  21.560  13.643 1.000 192.635 0 97  ILE GGG CD1 1 ? 10 
ATOM 8426  N N   . LEU G 5 98  ? 77.230  19.473  14.284 1.000 170.846 0 98  LEU GGG N   1 ? 10 
ATOM 8427  C CA  . LEU G 5 98  ? 76.165  18.982  15.150 1.000 174.286 0 98  LEU GGG CA  1 ? 10 
ATOM 8428  C C   . LEU G 5 98  ? 76.478  19.382  16.586 1.000 180.920 0 98  LEU GGG C   1 ? 10 
ATOM 8429  O O   . LEU G 5 98  ? 77.556  19.063  17.100 1.000 190.417 0 98  LEU GGG O   1 ? 10 
ATOM 8430  C CB  . LEU G 5 98  ? 76.031  17.465  15.031 1.000 177.891 0 98  LEU GGG CB  1 ? 10 
ATOM 8431  C CG  . LEU G 5 98  ? 74.863  16.818  15.770 1.000 178.720 0 98  LEU GGG CG  1 ? 10 
ATOM 8432  C CD1 . LEU G 5 98  ? 73.552  17.485  15.397 1.000 172.738 0 98  LEU GGG CD1 1 ? 10 
ATOM 8433  C CD2 . LEU G 5 98  ? 74.815  15.326  15.487 1.000 185.992 0 98  LEU GGG CD2 1 ? 10 
ATOM 8434  N N   . SER G 5 99  ? 75.544  20.078  17.233 1.000 178.451 0 99  SER GGG N   1 ? 10 
ATOM 8435  C CA  . SER G 5 99  ? 75.786  20.597  18.571 1.000 184.572 0 99  SER GGG CA  1 ? 10 
ATOM 8436  C C   . SER G 5 99  ? 74.523  20.530  19.419 1.000 181.545 0 99  SER GGG C   1 ? 10 
ATOM 8437  O O   . SER G 5 99  ? 73.401  20.528  18.904 1.000 169.351 0 99  SER GGG O   1 ? 10 
ATOM 8438  C CB  . SER G 5 99  ? 76.309  22.039  18.527 1.000 191.677 0 99  SER GGG CB  1 ? 10 
ATOM 8439  O OG  . SER G 5 99  ? 76.271  22.638  19.812 1.000 208.025 0 99  SER GGG OG  1 ? 10 
ATOM 8440  N N   . MET G 5 100 ? 74.730  20.464  20.732 1.000 186.760 0 100 MET GGG N   1 ? 10 
ATOM 8441  C CA  . MET G 5 100 ? 73.647  20.394  21.703 1.000 175.351 0 100 MET GGG CA  1 ? 10 
ATOM 8442  C C   . MET G 5 100 ? 73.025  21.759  21.967 1.000 172.319 0 100 MET GGG C   1 ? 10 
ATOM 8443  O O   . MET G 5 100 ? 73.698  22.791  21.938 1.000 171.419 0 100 MET GGG O   1 ? 10 
ATOM 8444  C CB  . MET G 5 100 ? 74.161  19.820  23.020 1.000 174.636 0 100 MET GGG CB  1 ? 10 
ATOM 8445  C CG  . MET G 5 100 ? 74.337  18.325  23.025 1.000 175.940 0 100 MET GGG CG  1 ? 10 
ATOM 8446  S SD  . MET G 5 100 ? 72.777  17.428  22.927 1.000 164.063 0 100 MET GGG SD  1 ? 10 
ATOM 8447  C CE  . MET G 5 100 ? 71.876  18.150  24.297 1.000 178.306 0 100 MET GGG CE  1 ? 10 
ATOM 8448  N N   . ALA G 5 101 ? 71.722  21.752  22.225 1.000 168.599 0 101 ALA GGG N   1 ? 10 
ATOM 8449  C CA  . ALA G 5 101 ? 71.015  22.934  22.700 1.000 173.457 0 101 ALA GGG CA  1 ? 10 
ATOM 8450  C C   . ALA G 5 101 ? 71.191  23.051  24.207 1.000 184.129 0 101 ALA GGG C   1 ? 10 
ATOM 8451  O O   . ALA G 5 101 ? 71.465  22.060  24.893 1.000 195.750 0 101 ALA GGG O   1 ? 10 
ATOM 8452  C CB  . ALA G 5 101 ? 69.530  22.885  22.339 1.000 166.080 0 101 ALA GGG CB  1 ? 10 
ATOM 8453  N N   . ASN G 5 102 ? 71.109  24.282  24.714 1.000 184.781 0 102 ASN GGG N   1 ? 10 
ATOM 8454  C CA  . ASN G 5 102 ? 71.188  24.477  26.156 1.000 187.484 0 102 ASN GGG CA  1 ? 10 
ATOM 8455  C C   . ASN G 5 102 ? 70.554  25.790  26.581 1.000 182.197 0 102 ASN GGG C   1 ? 10 
ATOM 8456  O O   . ASN G 5 102 ? 70.856  26.850  26.022 1.000 180.254 0 102 ASN GGG O   1 ? 10 
ATOM 8457  C CB  . ASN G 5 102 ? 72.641  24.479  26.632 1.000 203.267 0 102 ASN GGG CB  1 ? 10 
ATOM 8458  C CG  . ASN G 5 102 ? 73.404  25.694  26.150 1.000 215.001 0 102 ASN GGG CG  1 ? 10 
ATOM 8459  O OD1 . ASN G 5 102 ? 73.915  25.714  25.033 1.000 230.634 0 102 ASN GGG OD1 1 ? 10 
ATOM 8460  N ND2 . ASN G 5 102 ? 73.519  26.702  27.011 1.000 215.523 0 102 ASN GGG ND2 1 ? 10 
ATOM 8461  N N   . ALA G 5 103 ? 69.644  25.695  27.552 1.000 187.881 0 103 ALA GGG N   1 ? 10 
ATOM 8462  C CA  . ALA G 5 103 ? 68.936  26.866  28.047 1.000 187.005 0 103 ALA GGG CA  1 ? 10 
ATOM 8463  C C   . ALA G 5 103 ? 69.907  27.762  28.798 1.000 191.114 0 103 ALA GGG C   1 ? 10 
ATOM 8464  O O   . ALA G 5 103 ? 69.694  28.974  28.911 1.000 190.378 0 103 ALA GGG O   1 ? 10 
ATOM 8465  C CB  . ALA G 5 103 ? 67.786  26.438  28.952 1.000 178.281 0 103 ALA GGG CB  1 ? 10 
ATOM 8466  N N   . GLY G 5 104 ? 70.972  27.159  29.317 1.000 198.222 0 104 GLY GGG N   1 ? 10 
ATOM 8467  C CA  . GLY G 5 104 ? 71.945  27.792  30.172 1.000 203.389 0 104 GLY GGG CA  1 ? 10 
ATOM 8468  C C   . GLY G 5 104 ? 73.140  26.868  30.309 1.000 210.538 0 104 GLY GGG C   1 ? 10 
ATOM 8469  O O   . GLY G 5 104 ? 73.132  25.744  29.796 1.000 210.094 0 104 GLY GGG O   1 ? 10 
ATOM 8470  N N   . PRO G 5 105 ? 74.201  27.327  30.973 1.000 204.767 0 105 PRO GGG N   1 ? 10 
ATOM 8471  C CA  . PRO G 5 105 ? 75.342  26.440  31.236 1.000 203.061 0 105 PRO GGG CA  1 ? 10 
ATOM 8472  C C   . PRO G 5 105 ? 74.892  25.159  31.931 1.000 208.928 0 105 PRO GGG C   1 ? 10 
ATOM 8473  O O   . PRO G 5 105 ? 74.104  25.184  32.887 1.000 215.441 0 105 PRO GGG O   1 ? 10 
ATOM 8474  C CB  . PRO G 5 105 ? 76.277  27.285  32.107 1.000 204.184 0 105 PRO GGG CB  1 ? 10 
ATOM 8475  C CG  . PRO G 5 105 ? 75.700  28.641  32.169 1.000 202.701 0 105 PRO GGG CG  1 ? 10 
ATOM 8476  C CD  . PRO G 5 105 ? 74.309  28.626  31.657 1.000 205.273 0 105 PRO GGG CD  1 ? 10 
ATOM 8477  N N   . ASN G 5 106 ? 75.399  24.030  31.435 1.000 206.307 0 106 ASN GGG N   1 ? 10 
ATOM 8478  C CA  . ASN G 5 106 ? 75.191  22.698  32.012 1.000 218.544 0 106 ASN GGG CA  1 ? 10 
ATOM 8479  C C   . ASN G 5 106 ? 73.708  22.332  32.106 1.000 217.597 0 106 ASN GGG C   1 ? 10 
ATOM 8480  O O   . ASN G 5 106 ? 73.226  21.836  33.126 1.000 221.865 0 106 ASN GGG O   1 ? 10 
ATOM 8481  C CB  . ASN G 5 106 ? 75.866  22.562  33.379 1.000 223.401 0 106 ASN GGG CB  1 ? 10 
ATOM 8482  C CG  . ASN G 5 106 ? 77.334  22.918  33.347 1.000 235.325 0 106 ASN GGG CG  1 ? 10 
ATOM 8483  O OD1 . ASN G 5 106 ? 78.094  22.400  32.527 1.000 236.744 0 106 ASN GGG OD1 1 ? 10 
ATOM 8484  N ND2 . ASN G 5 106 ? 77.741  23.816  34.232 1.000 249.606 0 106 ASN GGG ND2 1 ? 10 
ATOM 8485  N N   . THR G 5 107 ? 72.977  22.584  31.015 1.000 208.456 0 107 THR GGG N   1 ? 10 
ATOM 8486  C CA  . THR G 5 107 ? 71.558  22.254  30.941 1.000 202.714 0 107 THR GGG CA  1 ? 10 
ATOM 8487  C C   . THR G 5 107 ? 71.284  21.518  29.635 1.000 202.464 0 107 THR GGG C   1 ? 10 
ATOM 8488  O O   . THR G 5 107 ? 70.215  21.652  29.041 1.000 201.977 0 107 THR GGG O   1 ? 10 
ATOM 8489  C CB  . THR G 5 107 ? 70.680  23.499  31.054 1.000 196.531 0 107 THR GGG CB  1 ? 10 
ATOM 8490  O OG1 . THR G 5 107 ? 70.975  24.399  29.977 1.000 200.994 0 107 THR GGG OG1 1 ? 10 
ATOM 8491  C CG2 . THR G 5 107 ? 70.905  24.204  32.383 1.000 196.400 0 107 THR GGG CG2 1 ? 10 
ATOM 8492  N N   . ASN G 5 108 ? 72.270  20.748  29.181 1.000 210.265 0 108 ASN GGG N   1 ? 10 
ATOM 8493  C CA  . ASN G 5 108 ? 72.127  19.915  27.996 1.000 199.117 0 108 ASN GGG CA  1 ? 10 
ATOM 8494  C C   . ASN G 5 108 ? 71.156  18.770  28.259 1.000 196.339 0 108 ASN GGG C   1 ? 10 
ATOM 8495  O O   . ASN G 5 108 ? 71.185  18.146  29.322 1.000 211.326 0 108 ASN GGG O   1 ? 10 
ATOM 8496  C CB  . ASN G 5 108 ? 73.489  19.380  27.564 1.000 200.422 0 108 ASN GGG CB  1 ? 10 
ATOM 8497  C CG  . ASN G 5 108 ? 74.468  20.497  27.201 1.000 198.306 0 108 ASN GGG CG  1 ? 10 
ATOM 8498  O OD1 . ASN G 5 108 ? 74.107  21.673  27.186 1.000 197.100 0 108 ASN GGG OD1 1 ? 10 
ATOM 8499  N ND2 . ASN G 5 108 ? 75.714  20.129  26.916 1.000 208.676 0 108 ASN GGG ND2 1 ? 10 
ATOM 8500  N N   . GLY G 5 109 ? 70.297  18.483  27.289 1.000 180.443 0 109 GLY GGG N   1 ? 10 
ATOM 8501  C CA  . GLY G 5 109 ? 69.418  17.349  27.473 1.000 176.094 0 109 GLY GGG CA  1 ? 10 
ATOM 8502  C C   . GLY G 5 109 ? 69.453  16.376  26.314 1.000 175.879 0 109 GLY GGG C   1 ? 10 
ATOM 8503  O O   . GLY G 5 109 ? 70.453  15.674  26.132 1.000 185.352 0 109 GLY GGG O   1 ? 10 
ATOM 8504  N N   . SER G 5 110 ? 68.382  16.312  25.529 1.000 167.012 0 110 SER GGG N   1 ? 10 
ATOM 8505  C CA  . SER G 5 110 ? 68.320  15.462  24.343 1.000 170.211 0 110 SER GGG CA  1 ? 10 
ATOM 8506  C C   . SER G 5 110 ? 68.011  16.246  23.066 1.000 169.751 0 110 SER GGG C   1 ? 10 
ATOM 8507  O O   . SER G 5 110 ? 67.453  15.697  22.112 1.000 171.563 0 110 SER GGG O   1 ? 10 
ATOM 8508  C CB  . SER G 5 110 ? 67.295  14.358  24.560 1.000 173.005 0 110 SER GGG CB  1 ? 10 
ATOM 8509  O OG  . SER G 5 110 ? 65.994  14.906  24.512 1.000 170.522 0 110 SER GGG OG  1 ? 10 
ATOM 8510  N N   . GLN G 5 111 ? 68.356  17.525  23.021 1.000 163.406 0 111 GLN GGG N   1 ? 10 
ATOM 8511  C CA  . GLN G 5 111 ? 68.037  18.340  21.858 1.000 156.794 0 111 GLN GGG CA  1 ? 10 
ATOM 8512  C C   . GLN G 5 111 ? 69.304  18.798  21.152 1.000 156.427 0 111 GLN GGG C   1 ? 10 
ATOM 8513  O O   . GLN G 5 111 ? 70.264  19.244  21.788 1.000 155.989 0 111 GLN GGG O   1 ? 10 
ATOM 8514  C CB  . GLN G 5 111 ? 67.178  19.532  22.266 1.000 153.402 0 111 GLN GGG CB  1 ? 10 
ATOM 8515  C CG  . GLN G 5 111 ? 65.800  19.101  22.763 1.000 160.871 0 111 GLN GGG CG  1 ? 10 
ATOM 8516  C CD  . GLN G 5 111 ? 64.887  20.266  23.075 1.000 161.080 0 111 GLN GGG CD  1 ? 10 
ATOM 8517  O OE1 . GLN G 5 111 ? 65.229  21.419  22.822 1.000 156.249 0 111 GLN GGG OE1 1 ? 10 
ATOM 8518  N NE2 . GLN G 5 111 ? 63.730  19.972  23.657 1.000 162.954 0 111 GLN GGG NE2 1 ? 10 
ATOM 8519  N N   . PHE G 5 112 ? 69.279  18.692  19.827 1.000 151.843 0 112 PHE GGG N   1 ? 10 
ATOM 8520  C CA  . PHE G 5 112 ? 70.431  18.934  18.977 1.000 151.903 0 112 PHE GGG CA  1 ? 10 
ATOM 8521  C C   . PHE G 5 112 ? 70.039  19.884  17.861 1.000 148.612 0 112 PHE GGG C   1 ? 10 
ATOM 8522  O O   . PHE G 5 112 ? 68.875  19.939  17.455 1.000 144.736 0 112 PHE GGG O   1 ? 10 
ATOM 8523  C CB  . PHE G 5 112 ? 70.943  17.638  18.346 1.000 160.239 0 112 PHE GGG CB  1 ? 10 
ATOM 8524  C CG  . PHE G 5 112 ? 69.884  16.868  17.598 1.000 161.893 0 112 PHE GGG CG  1 ? 10 
ATOM 8525  C CD1 . PHE G 5 112 ? 68.961  16.088  18.275 1.000 165.079 0 112 PHE GGG CD1 1 ? 10 
ATOM 8526  C CD2 . PHE G 5 112 ? 69.807  16.937  16.215 1.000 162.627 0 112 PHE GGG CD2 1 ? 10 
ATOM 8527  C CE1 . PHE G 5 112 ? 67.988  15.385  17.590 1.000 169.651 0 112 PHE GGG CE1 1 ? 10 
ATOM 8528  C CE2 . PHE G 5 112 ? 68.835  16.234  15.523 1.000 166.307 0 112 PHE GGG CE2 1 ? 10 
ATOM 8529  C CZ  . PHE G 5 112 ? 67.925  15.458  16.213 1.000 166.911 0 112 PHE GGG CZ  1 ? 10 
ATOM 8530  N N   . PHE G 5 113 ? 71.018  20.626  17.358 1.000 148.905 0 113 PHE GGG N   1 ? 10 
ATOM 8531  C CA  . PHE G 5 113 ? 70.800  21.458  16.187 1.000 144.719 0 113 PHE GGG CA  1 ? 10 
ATOM 8532  C C   . PHE G 5 113 ? 71.899  21.216  15.162 1.000 153.135 0 113 PHE GGG C   1 ? 10 
ATOM 8533  O O   . PHE G 5 113 ? 73.082  21.144  15.507 1.000 161.704 0 113 PHE GGG O   1 ? 10 
ATOM 8534  C CB  . PHE G 5 113 ? 70.699  22.949  16.567 1.000 138.774 0 113 PHE GGG CB  1 ? 10 
ATOM 8535  C CG  . PHE G 5 113 ? 71.979  23.560  17.071 1.000 138.403 0 113 PHE GGG CG  1 ? 10 
ATOM 8536  C CD1 . PHE G 5 113 ? 72.889  24.126  16.193 1.000 144.481 0 113 PHE GGG CD1 1 ? 10 
ATOM 8537  C CD2 . PHE G 5 113 ? 72.254  23.602  18.427 1.000 145.143 0 113 PHE GGG CD2 1 ? 10 
ATOM 8538  C CE1 . PHE G 5 113 ? 74.056  24.702  16.657 1.000 152.449 0 113 PHE GGG CE1 1 ? 10 
ATOM 8539  C CE2 . PHE G 5 113 ? 73.419  24.177  18.895 1.000 153.334 0 113 PHE GGG CE2 1 ? 10 
ATOM 8540  C CZ  . PHE G 5 113 ? 74.319  24.730  18.009 1.000 154.674 0 113 PHE GGG CZ  1 ? 10 
ATOM 8541  N N   . ILE G 5 114 ? 71.493  21.070  13.903 1.000 155.049 0 114 ILE GGG N   1 ? 10 
ATOM 8542  C CA  . ILE G 5 114 ? 72.411  20.857  12.790 1.000 147.702 0 114 ILE GGG CA  1 ? 10 
ATOM 8543  C C   . ILE G 5 114 ? 72.542  22.161  12.020 1.000 143.988 0 114 ILE GGG C   1 ? 10 
ATOM 8544  O O   . ILE G 5 114 ? 71.571  22.639  11.422 1.000 139.830 0 114 ILE GGG O   1 ? 10 
ATOM 8545  C CB  . ILE G 5 114 ? 71.932  19.729  11.868 1.000 140.639 0 114 ILE GGG CB  1 ? 10 
ATOM 8546  C CG1 . ILE G 5 114 ? 71.407  18.560  12.694 1.000 150.249 0 114 ILE GGG CG1 1 ? 10 
ATOM 8547  C CG2 . ILE G 5 114 ? 73.063  19.288  10.955 1.000 147.073 0 114 ILE GGG CG2 1 ? 10 
ATOM 8548  C CD1 . ILE G 5 114 ? 70.593  17.591  11.892 1.000 154.108 0 114 ILE GGG CD1 1 ? 10 
ATOM 8549  N N   . CYS G 5 115 ? 73.742  22.729  12.029 1.000 141.050 0 115 CYS GGG N   1 ? 10 
ATOM 8550  C CA  . CYS G 5 115 ? 73.980  24.007  11.374 1.000 140.863 0 115 CYS GGG CA  1 ? 10 
ATOM 8551  C C   . CYS G 5 115 ? 73.915  23.888  9.856  1.000 142.490 0 115 CYS GGG C   1 ? 10 
ATOM 8552  O O   . CYS G 5 115 ? 74.388  22.910  9.270  1.000 148.360 0 115 CYS GGG O   1 ? 10 
ATOM 8553  C CB  . CYS G 5 115 ? 75.354  24.557  11.767 1.000 148.249 0 115 CYS GGG CB  1 ? 10 
ATOM 8554  S SG  . CYS G 5 115 ? 75.603  24.920  13.516 1.000 156.214 0 115 CYS GGG SG  1 ? 10 
ATOM 8555  N N   . THR G 5 116 ? 73.318  24.897  9.217  1.000 141.085 0 116 THR GGG N   1 ? 10 
ATOM 8556  C CA  . THR G 5 116 ? 73.285  24.970  7.763  1.000 143.220 0 116 THR GGG CA  1 ? 10 
ATOM 8557  C C   . THR G 5 116 ? 74.061  26.195  7.310  1.000 146.960 0 116 THR GGG C   1 ? 10 
ATOM 8558  O O   . THR G 5 116 ? 74.000  26.578  6.135  1.000 151.077 0 116 THR GGG O   1 ? 10 
ATOM 8559  C CB  . THR G 5 116 ? 71.847  25.049  7.242  1.000 134.034 0 116 THR GGG CB  1 ? 10 
ATOM 8560  O OG1 . THR G 5 116 ? 71.189  26.180  7.829  1.000 127.923 0 116 THR GGG OG1 1 ? 10 
ATOM 8561  C CG2 . THR G 5 116 ? 71.081  23.788  7.602  1.000 138.883 0 116 THR GGG CG2 1 ? 10 
ATOM 8562  N N   . ALA G 5 117 ? 74.782  26.810  8.241  1.000 147.830 0 117 ALA GGG N   1 ? 10 
ATOM 8563  C CA  . ALA G 5 117 ? 75.677  27.933  8.022  1.000 153.835 0 117 ALA GGG CA  1 ? 10 
ATOM 8564  C C   . ALA G 5 117 ? 76.689  27.915  9.157  1.000 162.989 0 117 ALA GGG C   1 ? 10 
ATOM 8565  O O   . ALA G 5 117 ? 76.550  27.163  10.127 1.000 162.461 0 117 ALA GGG O   1 ? 10 
ATOM 8566  C CB  . ALA G 5 117 ? 74.926  29.265  7.960  1.000 147.239 0 117 ALA GGG CB  1 ? 10 
ATOM 8567  N N   . LYS G 5 118 ? 77.723  28.733  9.013  1.000 172.432 0 118 LYS GGG N   1 ? 10 
ATOM 8568  C CA  . LYS G 5 118 ? 78.672  28.938  10.096 1.000 181.529 0 118 LYS GGG CA  1 ? 10 
ATOM 8569  C C   . LYS G 5 118 ? 77.949  29.776  11.145 1.000 179.845 0 118 LYS GGG C   1 ? 10 
ATOM 8570  O O   . LYS G 5 118 ? 77.359  30.812  10.825 1.000 174.336 0 118 LYS GGG O   1 ? 10 
ATOM 8571  C CB  . LYS G 5 118 ? 79.967  29.581  9.610  1.000 191.579 0 118 LYS GGG CB  1 ? 10 
ATOM 8572  C CG  . LYS G 5 118 ? 80.985  29.789  10.719 1.000 195.449 0 118 LYS GGG CG  1 ? 10 
ATOM 8573  C CD  . LYS G 5 118 ? 82.287  30.353  10.171 1.000 201.442 0 118 LYS GGG CD  1 ? 10 
ATOM 8574  C CE  . LYS G 5 118 ? 83.317  30.532  11.278 1.000 211.601 0 118 LYS GGG CE  1 ? 10 
ATOM 8575  N NZ  . LYS G 5 118 ? 84.599  31.143  10.824 1.000 214.520 0 118 LYS GGG NZ  1 ? 10 
ATOM 8576  N N   . THR G 5 119 ? 77.998  29.346  12.397 1.000 182.309 0 119 THR GGG N   1 ? 10 
ATOM 8577  C CA  . THR G 5 119 ? 77.232  29.969  13.470 1.000 180.861 0 119 THR GGG CA  1 ? 10 
ATOM 8578  C C   . THR G 5 119 ? 78.184  30.339  14.605 1.000 190.171 0 119 THR GGG C   1 ? 10 
ATOM 8579  O O   . THR G 5 119 ? 78.159  29.771  15.696 1.000 195.644 0 119 THR GGG O   1 ? 10 
ATOM 8580  C CB  . THR G 5 119 ? 76.133  29.015  13.965 1.000 176.694 0 119 THR GGG CB  1 ? 10 
ATOM 8581  O OG1 . THR G 5 119 ? 76.739  27.792  14.409 1.000 177.480 0 119 THR GGG OG1 1 ? 10 
ATOM 8582  C CG2 . THR G 5 119 ? 75.117  28.700  12.866 1.000 174.773 0 119 THR GGG CG2 1 ? 10 
ATOM 8583  N N   . GLU G 5 120 ? 79.045  31.321  14.307 1.000 193.581 0 120 GLU GGG N   1 ? 10 
ATOM 8584  C CA  . GLU G 5 120 ? 80.192  31.629  15.148 1.000 203.980 0 120 GLU GGG CA  1 ? 10 
ATOM 8585  C C   . GLU G 5 120 ? 79.761  32.166  16.497 1.000 208.032 0 120 GLU GGG C   1 ? 10 
ATOM 8586  O O   . GLU G 5 120 ? 80.499  32.045  17.478 1.000 220.001 0 120 GLU GGG O   1 ? 10 
ATOM 8587  C CB  . GLU G 5 120 ? 80.969  32.744  14.458 1.000 210.910 0 120 GLU GGG CB  1 ? 10 
ATOM 8588  C CG  . GLU G 5 120 ? 81.145  32.465  12.997 1.000 223.596 0 120 GLU GGG CG  1 ? 10 
ATOM 8589  C CD  . GLU G 5 120 ? 81.073  33.716  12.128 1.000 227.794 0 120 GLU GGG CD  1 ? 10 
ATOM 8590  O OE1 . GLU G 5 120 ? 81.299  34.827  12.660 1.000 231.002 0 120 GLU GGG OE1 1 ? 10 
ATOM 8591  O OE2 . GLU G 5 120 ? 80.735  33.575  10.932 1.000 227.721 0 120 GLU GGG OE2 1 ? 10 
ATOM 8592  N N   . TRP G 5 121 ? 78.579  32.785  16.560 1.000 196.648 0 121 TRP GGG N   1 ? 10 
ATOM 8593  C CA  . TRP G 5 121 ? 78.058  33.332  17.804 1.000 189.559 0 121 TRP GGG CA  1 ? 10 
ATOM 8594  C C   . TRP G 5 121 ? 77.648  32.282  18.827 1.000 189.795 0 121 TRP GGG C   1 ? 10 
ATOM 8595  O O   . TRP G 5 121 ? 77.455  32.639  19.994 1.000 192.064 0 121 TRP GGG O   1 ? 10 
ATOM 8596  C CB  . TRP G 5 121 ? 76.929  34.307  17.483 1.000 184.681 0 121 TRP GGG CB  1 ? 10 
ATOM 8597  C CG  . TRP G 5 121 ? 75.808  33.689  16.779 1.000 181.731 0 121 TRP GGG CG  1 ? 10 
ATOM 8598  C CD1 . TRP G 5 121 ? 74.698  33.103  17.304 1.000 174.908 0 121 TRP GGG CD1 1 ? 10 
ATOM 8599  C CD2 . TRP G 5 121 ? 75.699  33.576  15.364 1.000 182.618 0 121 TRP GGG CD2 1 ? 10 
ATOM 8600  N NE1 . TRP G 5 121 ? 73.892  32.639  16.289 1.000 167.620 0 121 TRP GGG NE1 1 ? 10 
ATOM 8601  C CE2 . TRP G 5 121 ? 74.491  32.919  15.087 1.000 172.150 0 121 TRP GGG CE2 1 ? 10 
ATOM 8602  C CE3 . TRP G 5 121 ? 76.513  33.975  14.299 1.000 184.224 0 121 TRP GGG CE3 1 ? 10 
ATOM 8603  C CZ2 . TRP G 5 121 ? 74.073  32.651  13.789 1.000 169.550 0 121 TRP GGG CZ2 1 ? 10 
ATOM 8604  C CZ3 . TRP G 5 121 ? 76.102  33.710  13.016 1.000 176.081 0 121 TRP GGG CZ3 1 ? 10 
ATOM 8605  C CH2 . TRP G 5 121 ? 74.892  33.053  12.769 1.000 170.887 0 121 TRP GGG CH2 1 ? 10 
ATOM 8606  N N   . LEU G 5 122 ? 77.527  31.015  18.433 1.000 190.500 0 122 LEU GGG N   1 ? 10 
ATOM 8607  C CA  . LEU G 5 122 ? 77.226  29.927  19.352 1.000 195.137 0 122 LEU GGG CA  1 ? 10 
ATOM 8608  C C   . LEU G 5 122 ? 78.489  29.333  19.955 1.000 202.456 0 122 LEU GGG C   1 ? 10 
ATOM 8609  O O   . LEU G 5 122 ? 78.396  28.500  20.865 1.000 202.810 0 122 LEU GGG O   1 ? 10 
ATOM 8610  C CB  . LEU G 5 122 ? 76.408  28.844  18.634 1.000 190.290 0 122 LEU GGG CB  1 ? 10 
ATOM 8611  C CG  . LEU G 5 122 ? 75.093  29.371  18.040 1.000 180.318 0 122 LEU GGG CG  1 ? 10 
ATOM 8612  C CD1 . LEU G 5 122 ? 74.354  28.302  17.259 1.000 167.128 0 122 LEU GGG CD1 1 ? 10 
ATOM 8613  C CD2 . LEU G 5 122 ? 74.186  29.948  19.122 1.000 183.355 0 122 LEU GGG CD2 1 ? 10 
ATOM 8614  N N   . ASP G 5 123 ? 79.657  29.719  19.439 1.000 213.159 0 123 ASP GGG N   1 ? 10 
ATOM 8615  C CA  . ASP G 5 123 ? 80.915  29.183  19.934 1.000 221.895 0 123 ASP GGG CA  1 ? 10 
ATOM 8616  C C   . ASP G 5 123 ? 81.067  29.515  21.413 1.000 224.093 0 123 ASP GGG C   1 ? 10 
ATOM 8617  O O   . ASP G 5 123 ? 80.857  30.657  21.833 1.000 226.335 0 123 ASP GGG O   1 ? 10 
ATOM 8618  C CB  . ASP G 5 123 ? 82.091  29.747  19.124 1.000 229.245 0 123 ASP GGG CB  1 ? 10 
ATOM 8619  C CG  . ASP G 5 123 ? 82.141  29.203  17.692 1.000 233.582 0 123 ASP GGG CG  1 ? 10 
ATOM 8620  O OD1 . ASP G 5 123 ? 81.440  28.213  17.406 1.000 234.447 0 123 ASP GGG OD1 1 ? 10 
ATOM 8621  O OD2 . ASP G 5 123 ? 82.879  29.764  16.851 1.000 231.819 0 123 ASP GGG OD2 1 ? 10 
ATOM 8622  N N   . GLY G 5 124 ? 81.427  28.508  22.201 1.000 232.337 0 124 GLY GGG N   1 ? 10 
ATOM 8623  C CA  . GLY G 5 124 ? 81.661  28.682  23.617 1.000 232.612 0 124 GLY GGG CA  1 ? 10 
ATOM 8624  C C   . GLY G 5 124 ? 80.431  28.624  24.498 1.000 224.383 0 124 GLY GGG C   1 ? 10 
ATOM 8625  O O   . GLY G 5 124 ? 80.569  28.725  25.722 1.000 229.101 0 124 GLY GGG O   1 ? 10 
ATOM 8626  N N   . LYS G 5 125 ? 79.239  28.475  23.926 1.000 212.222 0 125 LYS GGG N   1 ? 10 
ATOM 8627  C CA  . LYS G 5 125 ? 77.993  28.387  24.679 1.000 198.718 0 125 LYS GGG CA  1 ? 10 
ATOM 8628  C C   . LYS G 5 125 ? 77.267  27.072  24.469 1.000 200.400 0 125 LYS GGG C   1 ? 10 
ATOM 8629  O O   . LYS G 5 125 ? 76.599  26.597  25.389 1.000 200.092 0 125 LYS GGG O   1 ? 10 
ATOM 8630  C CB  . LYS G 5 125 ? 77.042  29.563  24.382 1.000 184.993 0 125 LYS GGG CB  1 ? 10 
ATOM 8631  C CG  . LYS G 5 125 ? 77.680  30.942  24.502 1.000 180.426 0 125 LYS GGG CG  1 ? 10 
ATOM 8632  C CD  . LYS G 5 125 ? 76.646  32.044  24.292 1.000 171.300 0 125 LYS GGG CD  1 ? 10 
ATOM 8633  C CE  . LYS G 5 125 ? 77.249  33.429  24.471 1.000 168.313 0 125 LYS GGG CE  1 ? 10 
ATOM 8634  N NZ  . LYS G 5 125 ? 76.363  34.497  23.935 1.000 166.408 0 125 LYS GGG NZ  1 ? 10 
ATOM 8635  N N   . HIS G 5 126 ? 77.395  26.467  23.294 1.000 205.206 0 126 HIS GGG N   1 ? 10 
ATOM 8636  C CA  . HIS G 5 126 ? 76.747  25.206  22.979 1.000 209.656 0 126 HIS GGG CA  1 ? 10 
ATOM 8637  C C   . HIS G 5 126 ? 77.843  24.219  22.608 1.000 227.237 0 126 HIS GGG C   1 ? 10 
ATOM 8638  O O   . HIS G 5 126 ? 78.918  24.610  22.144 1.000 230.254 0 126 HIS GGG O   1 ? 10 
ATOM 8639  C CB  . HIS G 5 126 ? 75.762  25.347  21.808 1.000 197.051 0 126 HIS GGG CB  1 ? 10 
ATOM 8640  C CG  . HIS G 5 126 ? 74.605  26.256  22.082 1.000 184.017 0 126 HIS GGG CG  1 ? 10 
ATOM 8641  N ND1 . HIS G 5 126 ? 73.381  25.795  22.517 1.000 183.039 0 126 HIS GGG ND1 1 ? 10 
ATOM 8642  C CD2 . HIS G 5 126 ? 74.482  27.600  21.969 1.000 174.611 0 126 HIS GGG CD2 1 ? 10 
ATOM 8643  C CE1 . HIS G 5 126 ? 72.554  26.816  22.661 1.000 182.760 0 126 HIS GGG CE1 1 ? 10 
ATOM 8644  N NE2 . HIS G 5 126 ? 73.199  27.923  22.339 1.000 180.099 0 126 HIS GGG NE2 1 ? 10 
ATOM 8645  N N   . VAL G 5 127 ? 77.567  22.936  22.814 1.000 243.987 0 127 VAL GGG N   1 ? 10 
ATOM 8646  C CA  . VAL G 5 127 ? 78.597  21.904  22.784 1.000 249.699 0 127 VAL GGG CA  1 ? 10 
ATOM 8647  C C   . VAL G 5 127 ? 78.511  21.134  21.473 1.000 242.891 0 127 VAL GGG C   1 ? 10 
ATOM 8648  O O   . VAL G 5 127 ? 77.502  20.475  21.195 1.000 247.678 0 127 VAL GGG O   1 ? 10 
ATOM 8649  C CB  . VAL G 5 127 ? 78.470  20.956  23.986 1.000 253.856 0 127 VAL GGG CB  1 ? 10 
ATOM 8650  C CG1 . VAL G 5 127 ? 79.496  19.844  23.883 1.000 263.787 0 127 VAL GGG CG1 1 ? 10 
ATOM 8651  C CG2 . VAL G 5 127 ? 78.634  21.726  25.288 1.000 254.569 0 127 VAL GGG CG2 1 ? 10 
ATOM 8652  N N   . VAL G 5 128 ? 79.587  21.188  20.693 1.000 228.366 0 128 VAL GGG N   1 ? 10 
ATOM 8653  C CA  . VAL G 5 128 ? 79.675  20.492  19.411 1.000 217.657 0 128 VAL GGG CA  1 ? 10 
ATOM 8654  C C   . VAL G 5 128 ? 80.104  19.052  19.662 1.000 212.909 0 128 VAL GGG C   1 ? 10 
ATOM 8655  O O   . VAL G 5 128 ? 81.183  18.806  20.212 1.000 216.358 0 128 VAL GGG O   1 ? 10 
ATOM 8656  C CB  . VAL G 5 128 ? 80.662  21.196  18.470 1.000 219.079 0 128 VAL GGG CB  1 ? 10 
ATOM 8657  C CG1 . VAL G 5 128 ? 80.651  20.535  17.105 1.000 220.755 0 128 VAL GGG CG1 1 ? 10 
ATOM 8658  C CG2 . VAL G 5 128 ? 80.340  22.676  18.361 1.000 220.816 0 128 VAL GGG CG2 1 ? 10 
ATOM 8659  N N   . PHE G 5 129 ? 79.263  18.094  19.263 1.000 193.323 0 129 PHE GGG N   1 ? 10 
ATOM 8660  C CA  . PHE G 5 129 ? 79.560  16.688  19.510 1.000 194.571 0 129 PHE GGG CA  1 ? 10 
ATOM 8661  C C   . PHE G 5 129 ? 79.549  15.782  18.282 1.000 200.983 0 129 PHE GGG C   1 ? 10 
ATOM 8662  O O   . PHE G 5 129 ? 79.807  14.582  18.432 1.000 216.569 0 129 PHE GGG O   1 ? 10 
ATOM 8663  C CB  . PHE G 5 129 ? 78.562  16.127  20.532 1.000 200.856 0 129 PHE GGG CB  1 ? 10 
ATOM 8664  C CG  . PHE G 5 129 ? 77.145  16.054  20.023 1.000 196.297 0 129 PHE GGG CG  1 ? 10 
ATOM 8665  C CD1 . PHE G 5 129 ? 76.294  17.142  20.131 1.000 192.189 0 129 PHE GGG CD1 1 ? 10 
ATOM 8666  C CD2 . PHE G 5 129 ? 76.661  14.886  19.454 1.000 200.947 0 129 PHE GGG CD2 1 ? 10 
ATOM 8667  C CE1 . PHE G 5 129 ? 74.992  17.071  19.663 1.000 191.670 0 129 PHE GGG CE1 1 ? 10 
ATOM 8668  C CE2 . PHE G 5 129 ? 75.362  14.809  18.988 1.000 196.681 0 129 PHE GGG CE2 1 ? 10 
ATOM 8669  C CZ  . PHE G 5 129 ? 74.525  15.901  19.095 1.000 193.173 0 129 PHE GGG CZ  1 ? 10 
ATOM 8670  N N   . GLY G 5 130 ? 79.271  16.292  17.088 1.000 197.936 0 130 GLY GGG N   1 ? 10 
ATOM 8671  C CA  . GLY G 5 130 ? 79.280  15.429  15.919 1.000 206.800 0 130 GLY GGG CA  1 ? 10 
ATOM 8672  C C   . GLY G 5 130 ? 79.229  16.234  14.640 1.000 204.061 0 130 GLY GGG C   1 ? 10 
ATOM 8673  O O   . GLY G 5 130 ? 79.244  17.468  14.652 1.000 200.608 0 130 GLY GGG O   1 ? 10 
ATOM 8674  N N   . LYS G 5 131 ? 79.201  15.503  13.525 1.000 211.829 0 131 LYS GGG N   1 ? 10 
ATOM 8675  C CA  . LYS G 5 131 ? 79.079  16.124  12.217 1.000 202.758 0 131 LYS GGG CA  1 ? 10 
ATOM 8676  C C   . LYS G 5 131 ? 78.389  15.182  11.241 1.000 204.967 0 131 LYS GGG C   1 ? 10 
ATOM 8677  O O   . LYS G 5 131 ? 78.559  13.961  11.288 1.000 211.578 0 131 LYS GGG O   1 ? 10 
ATOM 8678  C CB  . LYS G 5 131 ? 80.440  16.485  11.599 1.000 205.159 0 131 LYS GGG CB  1 ? 10 
ATOM 8679  C CG  . LYS G 5 131 ? 81.000  17.878  11.825 1.000 202.684 0 131 LYS GGG CG  1 ? 10 
ATOM 8680  C CD  . LYS G 5 131 ? 82.203  18.062  10.888 1.000 198.905 0 131 LYS GGG CD  1 ? 10 
ATOM 8681  C CE  . LYS G 5 131 ? 82.819  19.450  10.978 1.000 191.016 0 131 LYS GGG CE  1 ? 10 
ATOM 8682  N NZ  . LYS G 5 131 ? 83.476  19.706  12.281 1.000 188.016 0 131 LYS GGG NZ  1 ? 10 
ATOM 8683  N N   . VAL G 5 132 ? 77.611  15.794  10.347 1.000 202.915 0 132 VAL GGG N   1 ? 10 
ATOM 8684  C CA  . VAL G 5 132 ? 77.066  15.129  9.172  1.000 203.559 0 132 VAL GGG CA  1 ? 10 
ATOM 8685  C C   . VAL G 5 132 ? 78.206  14.652  8.285  1.000 204.018 0 132 VAL GGG C   1 ? 10 
ATOM 8686  O O   . VAL G 5 132 ? 79.105  15.429  7.944  1.000 207.061 0 132 VAL GGG O   1 ? 10 
ATOM 8687  C CB  . VAL G 5 132 ? 76.111  16.069  8.432  1.000 198.411 0 132 VAL GGG CB  1 ? 10 
ATOM 8688  C CG1 . VAL G 5 132 ? 75.666  15.432  7.145  1.000 201.995 0 132 VAL GGG CG1 1 ? 10 
ATOM 8689  C CG2 . VAL G 5 132 ? 74.904  16.373  9.316  1.000 196.562 0 132 VAL GGG CG2 1 ? 10 
ATOM 8690  N N   . LYS G 5 133 ? 78.167  13.383  7.883  1.000 211.778 0 133 LYS GGG N   1 ? 10 
ATOM 8691  C CA  . LYS G 5 133 ? 79.196  12.804  7.023  1.000 205.456 0 133 LYS GGG CA  1 ? 10 
ATOM 8692  C C   . LYS G 5 133 ? 78.757  12.751  5.572  1.000 224.588 0 133 LYS GGG C   1 ? 10 
ATOM 8693  O O   . LYS G 5 133 ? 79.474  13.215  4.683  1.000 229.770 0 133 LYS GGG O   1 ? 10 
ATOM 8694  C CB  . LYS G 5 133 ? 79.521  11.374  7.468  1.000 221.029 0 133 LYS GGG CB  1 ? 10 
ATOM 8695  C CG  . LYS G 5 133 ? 80.690  11.218  8.389  1.000 238.046 0 133 LYS GGG CG  1 ? 10 
ATOM 8696  C CD  . LYS G 5 133 ? 81.799  12.217  8.136  1.000 230.773 0 133 LYS GGG CD  1 ? 10 
ATOM 8697  C CE  . LYS G 5 133 ? 83.011  11.837  8.972  1.000 242.181 0 133 LYS GGG CE  1 ? 10 
ATOM 8698  N NZ  . LYS G 5 133 ? 84.176  12.743  8.798  1.000 250.888 0 133 LYS GGG NZ  1 ? 10 
ATOM 8699  N N   . GLU G 5 134 ? 77.582  12.204  5.320  1.000 223.890 0 134 GLU GGG N   1 ? 10 
ATOM 8700  C CA  . GLU G 5 134 ? 76.999  12.186  3.995  1.000 235.640 0 134 GLU GGG CA  1 ? 10 
ATOM 8701  C C   . GLU G 5 134 ? 75.573  12.684  4.096  1.000 228.964 0 134 GLU GGG C   1 ? 10 
ATOM 8702  O O   . GLU G 5 134 ? 74.928  12.569  5.142  1.000 217.205 0 134 GLU GGG O   1 ? 10 
ATOM 8703  C CB  . GLU G 5 134 ? 76.991  10.788  3.386  1.000 247.441 0 134 GLU GGG CB  1 ? 10 
ATOM 8704  C CG  . GLU G 5 134 ? 76.884  10.708  1.860  1.000 259.825 0 134 GLU GGG CG  1 ? 10 
ATOM 8705  C CD  . GLU G 5 134 ? 77.862  11.599  1.097  1.000 275.694 0 134 GLU GGG CD  1 ? 10 
ATOM 8706  O OE1 . GLU G 5 134 ? 79.002  11.806  1.569  1.000 286.802 0 134 GLU GGG OE1 1 ? 10 
ATOM 8707  O OE2 . GLU G 5 134 ? 77.513  12.016  -0.029 1.000 290.977 0 134 GLU GGG OE2 1 ? 10 
ATOM 8708  N N   . GLY G 5 135 ? 75.090  13.240  2.997  1.000 222.296 0 135 GLY GGG N   1 ? 10 
ATOM 8709  C CA  . GLY G 5 135 ? 73.721  13.694  2.959  1.000 208.114 0 135 GLY GGG CA  1 ? 10 
ATOM 8710  C C   . GLY G 5 135 ? 73.447  15.057  3.533  1.000 196.112 0 135 GLY GGG C   1 ? 10 
ATOM 8711  O O   . GLY G 5 135 ? 72.333  15.306  4.006  1.000 189.488 0 135 GLY GGG O   1 ? 10 
ATOM 8712  N N   . MET G 5 136 ? 74.442  15.948  3.532  1.000 191.801 0 136 MET GGG N   1 ? 10 
ATOM 8713  C CA  . MET G 5 136 ? 74.178  17.329  3.913  1.000 175.466 0 136 MET GGG CA  1 ? 10 
ATOM 8714  C C   . MET G 5 136 ? 73.123  17.923  2.996  1.000 161.009 0 136 MET GGG C   1 ? 10 
ATOM 8715  O O   . MET G 5 136 ? 72.380  18.827  3.396  1.000 161.434 0 136 MET GGG O   1 ? 10 
ATOM 8716  C CB  . MET G 5 136 ? 75.456  18.167  3.875  1.000 179.422 0 136 MET GGG CB  1 ? 10 
ATOM 8717  C CG  . MET G 5 136 ? 75.947  18.609  5.247  1.000 187.415 0 136 MET GGG CG  1 ? 10 
ATOM 8718  S SD  . MET G 5 136 ? 74.845  19.799  6.050  1.000 181.808 0 136 MET GGG SD  1 ? 10 
ATOM 8719  C CE  . MET G 5 136 ? 74.929  21.196  4.931  1.000 180.897 0 136 MET GGG CE  1 ? 10 
ATOM 8720  N N   . ASN G 5 137 ? 73.069  17.449  1.748  1.000 160.411 0 137 ASN GGG N   1 ? 10 
ATOM 8721  C CA  . ASN G 5 137 ? 72.042  17.916  0.831  1.000 160.013 0 137 ASN GGG CA  1 ? 10 
ATOM 8722  C C   . ASN G 5 137 ? 70.661  17.558  1.358  1.000 159.220 0 137 ASN GGG C   1 ? 10 
ATOM 8723  O O   . ASN G 5 137 ? 69.683  18.256  1.072  1.000 164.706 0 137 ASN GGG O   1 ? 10 
ATOM 8724  C CB  . ASN G 5 137 ? 72.258  17.287  -0.545 1.000 166.213 0 137 ASN GGG CB  1 ? 10 
ATOM 8725  C CG  . ASN G 5 137 ? 73.652  17.528  -1.083 1.000 170.170 0 137 ASN GGG CG  1 ? 10 
ATOM 8726  O OD1 . ASN G 5 137 ? 74.129  18.663  -1.121 1.000 166.091 0 137 ASN GGG OD1 1 ? 10 
ATOM 8727  N ND2 . ASN G 5 137 ? 74.322  16.455  -1.484 1.000 174.193 0 137 ASN GGG ND2 1 ? 10 
ATOM 8728  N N   . ILE G 5 138 ? 70.565  16.460  2.111  1.000 157.404 0 138 ILE GGG N   1 ? 10 
ATOM 8729  C CA  . ILE G 5 138 ? 69.302  16.074  2.729  1.000 167.342 0 138 ILE GGG CA  1 ? 10 
ATOM 8730  C C   . ILE G 5 138 ? 68.993  16.984  3.915  1.000 172.655 0 138 ILE GGG C   1 ? 10 
ATOM 8731  O O   . ILE G 5 138 ? 67.837  17.363  4.138  1.000 173.803 0 138 ILE GGG O   1 ? 10 
ATOM 8732  C CB  . ILE G 5 138 ? 69.323  14.591  3.128  1.000 172.581 0 138 ILE GGG CB  1 ? 10 
ATOM 8733  C CG1 . ILE G 5 138 ? 69.527  13.719  1.890  1.000 182.198 0 138 ILE GGG CG1 1 ? 10 
ATOM 8734  C CG2 . ILE G 5 138 ? 67.995  14.207  3.756  1.000 169.898 0 138 ILE GGG CG2 1 ? 10 
ATOM 8735  C CD1 . ILE G 5 138 ? 68.491  13.931  0.810  1.000 175.558 0 138 ILE GGG CD1 1 ? 10 
ATOM 8736  N N   . VAL G 5 139 ? 70.020  17.336  4.702  1.000 175.975 0 139 VAL GGG N   1 ? 10 
ATOM 8737  C CA  . VAL G 5 139 ? 69.844  18.319  5.773  1.000 172.352 0 139 VAL GGG CA  1 ? 10 
ATOM 8738  C C   . VAL G 5 139 ? 69.362  19.625  5.170  1.000 167.855 0 139 VAL GGG C   1 ? 10 
ATOM 8739  O O   . VAL G 5 139 ? 68.484  20.304  5.720  1.000 165.801 0 139 VAL GGG O   1 ? 10 
ATOM 8740  C CB  . VAL G 5 139 ? 71.157  18.503  6.561  1.000 174.987 0 139 VAL GGG CB  1 ? 10 
ATOM 8741  C CG1 . VAL G 5 139 ? 71.037  19.642  7.567  1.000 165.550 0 139 VAL GGG CG1 1 ? 10 
ATOM 8742  C CG2 . VAL G 5 139 ? 71.552  17.213  7.264  1.000 184.432 0 139 VAL GGG CG2 1 ? 10 
ATOM 8743  N N   . GLU G 5 140 ? 69.923  19.986  4.018  1.000 166.532 0 140 GLU GGG N   1 ? 10 
ATOM 8744  C CA  . GLU G 5 140 ? 69.491  21.184  3.321  1.000 159.272 0 140 GLU GGG CA  1 ? 10 
ATOM 8745  C C   . GLU G 5 140 ? 68.044  21.047  2.892  1.000 150.125 0 140 GLU GGG C   1 ? 10 
ATOM 8746  O O   . GLU G 5 140 ? 67.281  22.000  3.030  1.000 145.852 0 140 GLU GGG O   1 ? 10 
ATOM 8747  C CB  . GLU G 5 140 ? 70.361  21.521  2.102  1.000 163.706 0 140 GLU GGG CB  1 ? 10 
ATOM 8748  C CG  . GLU G 5 140 ? 71.786  21.982  2.402  1.000 171.444 0 140 GLU GGG CG  1 ? 10 
ATOM 8749  C CD  . GLU G 5 140 ? 72.651  22.025  1.153  1.000 167.603 0 140 GLU GGG CD  1 ? 10 
ATOM 8750  O OE1 . GLU G 5 140 ? 72.185  21.562  0.090  1.000 154.906 0 140 GLU GGG OE1 1 ? 10 
ATOM 8751  O OE2 . GLU G 5 140 ? 73.796  22.519  1.234  1.000 171.066 0 140 GLU GGG OE2 1 ? 10 
ATOM 8752  N N   . ALA G 5 141 ? 67.607  19.839  2.515  1.000 151.072 0 141 ALA GGG N   1 ? 10 
ATOM 8753  C CA  . ALA G 5 141 ? 66.218  19.643  2.091  1.000 151.904 0 141 ALA GGG CA  1 ? 10 
ATOM 8754  C C   . ALA G 5 141 ? 65.225  19.968  3.200  1.000 153.098 0 141 ALA GGG C   1 ? 10 
ATOM 8755  O O   . ALA G 5 141 ? 64.145  20.505  2.929  1.000 152.496 0 141 ALA GGG O   1 ? 10 
ATOM 8756  C CB  . ALA G 5 141 ? 66.024  18.215  1.577  1.000 153.564 0 141 ALA GGG CB  1 ? 10 
ATOM 8757  N N   . MET G 5 142 ? 65.564  19.681  4.444  1.000 149.089 0 142 MET GGG N   1 ? 10 
ATOM 8758  C CA  . MET G 5 142 ? 64.669  20.006  5.551  1.000 144.735 0 142 MET GGG CA  1 ? 10 
ATOM 8759  C C   . MET G 5 142 ? 64.395  21.506  5.720  1.000 137.655 0 142 MET GGG C   1 ? 10 
ATOM 8760  O O   . MET G 5 142 ? 63.259  21.892  6.023  1.000 138.225 0 142 MET GGG O   1 ? 10 
ATOM 8761  C CB  . MET G 5 142 ? 65.268  19.457  6.830  1.000 143.275 0 142 MET GGG CB  1 ? 10 
ATOM 8762  C CG  . MET G 5 142 ? 65.202  17.982  6.864  1.000 148.571 0 142 MET GGG CG  1 ? 10 
ATOM 8763  S SD  . MET G 5 142 ? 66.255  17.407  8.177  1.000 152.158 0 142 MET GGG SD  1 ? 10 
ATOM 8764  C CE  . MET G 5 142 ? 65.536  18.267  9.563  1.000 154.816 0 142 MET GGG CE  1 ? 10 
ATOM 8765  N N   . GLU G 5 143 ? 65.401  22.367  5.488  1.000 130.203 0 143 GLU GGG N   1 ? 10 
ATOM 8766  C CA  . GLU G 5 143 ? 65.267  23.798  5.800  1.000 139.708 0 143 GLU GGG CA  1 ? 10 
ATOM 8767  C C   . GLU G 5 143 ? 64.068  24.495  5.146  1.000 136.155 0 143 GLU GGG C   1 ? 10 
ATOM 8768  O O   . GLU G 5 143 ? 63.564  25.469  5.718  1.000 144.900 0 143 GLU GGG O   1 ? 10 
ATOM 8769  C CB  . GLU G 5 143 ? 66.572  24.544  5.463  1.000 138.486 0 143 GLU GGG CB  1 ? 10 
ATOM 8770  C CG  . GLU G 5 143 ? 66.885  24.814  3.993  1.000 152.877 0 143 GLU GGG CG  1 ? 10 
ATOM 8771  C CD  . GLU G 5 143 ? 68.262  25.461  3.830  1.000 154.052 0 143 GLU GGG CD  1 ? 10 
ATOM 8772  O OE1 . GLU G 5 143 ? 68.887  25.747  4.875  1.000 130.803 0 143 GLU GGG OE1 1 ? 10 
ATOM 8773  O OE2 . GLU G 5 143 ? 68.730  25.674  2.685  1.000 161.724 0 143 GLU GGG OE2 1 ? 10 
ATOM 8774  N N   . ARG G 5 144 ? 63.612  24.084  3.957  1.000 126.395 0 144 ARG GGG N   1 ? 10 
ATOM 8775  C CA  . ARG G 5 144 ? 62.567  24.909  3.338  1.000 134.521 0 144 ARG GGG CA  1 ? 10 
ATOM 8776  C C   . ARG G 5 144 ? 61.233  24.713  4.013  1.000 138.732 0 144 ARG GGG C   1 ? 10 
ATOM 8777  O O   . ARG G 5 144 ? 60.335  25.533  3.817  1.000 146.253 0 144 ARG GGG O   1 ? 10 
ATOM 8778  C CB  . ARG G 5 144 ? 62.194  24.548  1.937  1.000 132.737 0 144 ARG GGG CB  1 ? 10 
ATOM 8779  C CG  . ARG G 5 144 ? 61.296  25.501  1.139  1.000 139.881 0 144 ARG GGG CG  1 ? 10 
ATOM 8780  C CD  . ARG G 5 144 ? 61.041  24.436  0.314  1.000 139.342 0 144 ARG GGG CD  1 ? 10 
ATOM 8781  N NE  . ARG G 5 144 ? 62.182  24.113  -0.502 1.000 180.175 0 144 ARG GGG NE  1 ? 10 
ATOM 8782  C CZ  . ARG G 5 144 ? 62.188  22.937  -1.075 1.000 202.964 0 144 ARG GGG CZ  1 ? 10 
ATOM 8783  N NH1 . ARG G 5 144 ? 61.180  22.125  -0.868 1.000 193.227 0 144 ARG GGG NH1 1 ? 10 
ATOM 8784  N NH2 . ARG G 5 144 ? 63.199  22.576  -1.857 1.000 202.606 0 144 ARG GGG NH2 1 ? 10 
ATOM 8785  N N   . PHE G 5 145 ? 61.097  23.702  4.856  1.000 131.572 0 145 PHE GGG N   1 ? 10 
ATOM 8786  C CA  . PHE G 5 145 ? 59.823  23.521  5.516  1.000 137.102 0 145 PHE GGG CA  1 ? 10 
ATOM 8787  C C   . PHE G 5 145 ? 59.832  24.262  6.831  1.000 137.527 0 145 PHE GGG C   1 ? 10 
ATOM 8788  O O   . PHE G 5 145 ? 58.846  24.240  7.569  1.000 138.828 0 145 PHE GGG O   1 ? 10 
ATOM 8789  C CB  . PHE G 5 145 ? 59.592  22.024  5.738  1.000 142.845 0 145 PHE GGG CB  1 ? 10 
ATOM 8790  C CG  . PHE G 5 145 ? 59.503  21.234  4.462  1.000 144.919 0 145 PHE GGG CG  1 ? 10 
ATOM 8791  C CD1 . PHE G 5 145 ? 58.379  21.288  3.654  1.000 148.984 0 145 PHE GGG CD1 1 ? 10 
ATOM 8792  C CD2 . PHE G 5 145 ? 60.587  20.475  4.045  1.000 142.744 0 145 PHE GGG CD2 1 ? 10 
ATOM 8793  C CE1 . PHE G 5 145 ? 58.326  20.565  2.471  1.000 155.724 0 145 PHE GGG CE1 1 ? 10 
ATOM 8794  C CE2 . PHE G 5 145 ? 60.540  19.755  2.866  1.000 146.149 0 145 PHE GGG CE2 1 ? 10 
ATOM 8795  C CZ  . PHE G 5 145 ? 59.410  19.800  2.079  1.000 152.164 0 145 PHE GGG CZ  1 ? 10 
ATOM 8796  N N   . GLY G 5 146 ? 60.943  24.944  7.082  1.000 136.270 0 146 GLY GGG N   1 ? 10 
ATOM 8797  C CA  . GLY G 5 146 ? 61.116  25.815  8.217  1.000 125.861 0 146 GLY GGG CA  1 ? 10 
ATOM 8798  C C   . GLY G 5 146 ? 60.678  27.212  7.823  1.000 122.462 0 146 GLY GGG C   1 ? 10 
ATOM 8799  O O   . GLY G 5 146 ? 60.120  27.444  6.749  1.000 118.691 0 146 GLY GGG O   1 ? 10 
ATOM 8800  N N   . SER G 5 147 ? 60.923  28.153  8.722  1.000 128.656 0 147 SER GGG N   1 ? 10 
ATOM 8801  C CA  . SER G 5 147 ? 60.531  29.535  8.490  1.000 129.611 0 147 SER GGG CA  1 ? 10 
ATOM 8802  C C   . SER G 5 147 ? 61.426  30.422  9.339  1.000 132.671 0 147 SER GGG C   1 ? 10 
ATOM 8803  O O   . SER G 5 147 ? 62.222  29.940  10.148 1.000 131.398 0 147 SER GGG O   1 ? 10 
ATOM 8804  C CB  . SER G 5 147 ? 59.049  29.760  8.809  1.000 135.893 0 147 SER GGG CB  1 ? 10 
ATOM 8805  O OG  . SER G 5 147 ? 58.803  29.650  10.200 1.000 137.008 0 147 SER GGG OG  1 ? 10 
ATOM 8806  N N   . ARG G 5 148 ? 61.309  31.733  9.118  1.000 137.777 0 148 ARG GGG N   1 ? 10 
ATOM 8807  C CA  . ARG G 5 148 ? 62.171  32.671  9.826  1.000 138.279 0 148 ARG GGG CA  1 ? 10 
ATOM 8808  C C   . ARG G 5 148 ? 62.011  32.528  11.335 1.000 135.910 0 148 ARG GGG C   1 ? 10 
ATOM 8809  O O   . ARG G 5 148 ? 62.991  32.633  12.081 1.000 132.907 0 148 ARG GGG O   1 ? 10 
ATOM 8810  C CB  . ARG G 5 148 ? 61.891  34.103  9.368  1.000 144.694 0 148 ARG GGG CB  1 ? 10 
ATOM 8811  C CG  . ARG G 5 148 ? 62.392  34.377  7.959  1.000 161.923 0 148 ARG GGG CG  1 ? 10 
ATOM 8812  C CD  . ARG G 5 148 ? 63.740  33.704  7.731  1.000 185.832 0 148 ARG GGG CD  1 ? 10 
ATOM 8813  N NE  . ARG G 5 148 ? 64.584  34.426  6.787  1.000 216.591 0 148 ARG GGG NE  1 ? 10 
ATOM 8814  C CZ  . ARG G 5 148 ? 65.910  34.416  6.812  1.000 217.325 0 148 ARG GGG CZ  1 ? 10 
ATOM 8815  N NH1 . ARG G 5 148 ? 66.576  33.713  7.717  1.000 204.323 0 148 ARG GGG NH1 1 ? 10 
ATOM 8816  N NH2 . ARG G 5 148 ? 66.584  35.118  5.911  1.000 220.176 0 148 ARG GGG NH2 1 ? 10 
ATOM 8817  N N   . ASN G 5 149 ? 60.797  32.249  11.800 1.000 136.059 0 149 ASN GGG N   1 ? 10 
ATOM 8818  C CA  . ASN G 5 149 ? 60.560  32.074  13.223 1.000 130.762 0 149 ASN GGG CA  1 ? 10 
ATOM 8819  C C   . ASN G 5 149 ? 60.692  30.632  13.690 1.000 127.281 0 149 ASN GGG C   1 ? 10 
ATOM 8820  O O   . ASN G 5 149 ? 60.476  30.361  14.876 1.000 134.275 0 149 ASN GGG O   1 ? 10 
ATOM 8821  C CB  . ASN G 5 149 ? 59.161  32.583  13.548 1.000 138.351 0 149 ASN GGG CB  1 ? 10 
ATOM 8822  C CG  . ASN G 5 149 ? 58.072  31.709  12.941 1.000 145.466 0 149 ASN GGG CG  1 ? 10 
ATOM 8823  O OD1 . ASN G 5 149 ? 58.106  31.403  11.746 1.000 146.596 0 149 ASN GGG OD1 1 ? 10 
ATOM 8824  N ND2 . ASN G 5 149 ? 57.075  31.360  13.737 1.000 152.098 0 149 ASN GGG ND2 1 ? 10 
ATOM 8825  N N   . GLY G 5 150 ? 61.008  29.704  12.789 1.000 121.984 0 150 GLY GGG N   1 ? 10 
ATOM 8826  C CA  . GLY G 5 150 ? 61.349  28.341  13.135 1.000 132.348 0 150 GLY GGG CA  1 ? 10 
ATOM 8827  C C   . GLY G 5 150 ? 60.216  27.343  13.049 1.000 137.790 0 150 GLY GGG C   1 ? 10 
ATOM 8828  O O   . GLY G 5 150 ? 60.469  26.133  13.130 1.000 136.278 0 150 GLY GGG O   1 ? 10 
ATOM 8829  N N   . LYS G 5 151 ? 58.982  27.812  12.916 1.000 138.592 0 151 LYS GGG N   1 ? 10 
ATOM 8830  C CA  . LYS G 5 151 ? 57.836  26.923  12.817 1.000 143.020 0 151 LYS GGG CA  1 ? 10 
ATOM 8831  C C   . LYS G 5 151 ? 57.867  26.218  11.475 1.000 139.275 0 151 LYS GGG C   1 ? 10 
ATOM 8832  O O   . LYS G 5 151 ? 58.194  26.825  10.452 1.000 137.113 0 151 LYS GGG O   1 ? 10 
ATOM 8833  C CB  . LYS G 5 151 ? 56.541  27.701  13.000 1.000 147.110 0 151 LYS GGG CB  1 ? 10 
ATOM 8834  C CG  . LYS G 5 151 ? 56.407  28.264  14.406 1.000 159.454 0 151 LYS GGG CG  1 ? 10 
ATOM 8835  C CD  . LYS G 5 151 ? 56.880  27.286  15.471 1.000 166.409 0 151 LYS GGG CD  1 ? 10 
ATOM 8836  C CE  . LYS G 5 151 ? 57.335  28.043  16.706 1.000 160.256 0 151 LYS GGG CE  1 ? 10 
ATOM 8837  N NZ  . LYS G 5 151 ? 57.789  27.124  17.778 1.000 169.792 0 151 LYS GGG NZ  1 ? 10 
ATOM 8838  N N   . THR G 5 152 ? 57.542  24.935  11.461 1.000 136.483 0 152 THR GGG N   1 ? 10 
ATOM 8839  C CA  . THR G 5 152 ? 57.621  24.211  10.208 1.000 135.608 0 152 THR GGG CA  1 ? 10 
ATOM 8840  C C   . THR G 5 152 ? 56.260  24.181  9.526  1.000 140.479 0 152 THR GGG C   1 ? 10 
ATOM 8841  O O   . THR G 5 152 ? 55.219  24.084  10.183 1.000 152.684 0 152 THR GGG O   1 ? 10 
ATOM 8842  C CB  . THR G 5 152 ? 58.121  22.780  10.434 1.000 138.764 0 152 THR GGG CB  1 ? 10 
ATOM 8843  O OG1 . THR G 5 152 ? 57.224  22.089  11.317 1.000 148.350 0 152 THR GGG OG1 1 ? 10 
ATOM 8844  C CG2 . THR G 5 152 ? 59.521  22.781  11.022 1.000 135.918 0 152 THR GGG CG2 1 ? 10 
ATOM 8845  N N   . SER G 5 153 ? 56.286  24.254  8.191  1.000 137.515 0 153 SER GGG N   1 ? 10 
ATOM 8846  C CA  . SER G 5 153 ? 55.073  24.271  7.381  1.000 139.875 0 153 SER GGG CA  1 ? 10 
ATOM 8847  C C   . SER G 5 153 ? 54.559  22.874  7.092  1.000 140.037 0 153 SER GGG C   1 ? 10 
ATOM 8848  O O   . SER G 5 153 ? 53.391  22.717  6.718  1.000 140.467 0 153 SER GGG O   1 ? 10 
ATOM 8849  C CB  . SER G 5 153 ? 55.321  25.014  6.066  1.000 144.818 0 153 SER GGG CB  1 ? 10 
ATOM 8850  O OG  . SER G 5 153 ? 56.386  24.431  5.335  1.000 146.832 0 153 SER GGG OG  1 ? 10 
ATOM 8851  N N   . LYS G 5 154 ? 55.406  21.868  7.290  1.000 138.771 0 154 LYS GGG N   1 ? 10 
ATOM 8852  C CA  . LYS G 5 154 ? 55.048  20.467  7.171  1.000 147.752 0 154 LYS GGG CA  1 ? 10 
ATOM 8853  C C   . LYS G 5 154 ? 55.717  19.750  8.336  1.000 151.452 0 154 LYS GGG C   1 ? 10 
ATOM 8854  O O   . LYS G 5 154 ? 56.675  20.259  8.922  1.000 145.346 0 154 LYS GGG O   1 ? 10 
ATOM 8855  C CB  . LYS G 5 154 ? 55.521  19.884  5.830  1.000 149.212 0 154 LYS GGG CB  1 ? 10 
ATOM 8856  C CG  . LYS G 5 154 ? 54.772  20.393  4.593  1.000 153.070 0 154 LYS GGG CG  1 ? 10 
ATOM 8857  C CD  . LYS G 5 154 ? 53.302  19.982  4.517  1.000 161.475 0 154 LYS GGG CD  1 ? 10 
ATOM 8858  C CE  . LYS G 5 154 ? 52.561  20.835  3.482  1.000 158.462 0 154 LYS GGG CE  1 ? 10 
ATOM 8859  N NZ  . LYS G 5 154 ? 52.546  22.275  3.839  1.000 160.547 0 154 LYS GGG NZ  1 ? 10 
ATOM 8860  N N   . LYS G 5 155 ? 55.225  18.562  8.676  1.000 164.019 0 155 LYS GGG N   1 ? 10 
ATOM 8861  C CA  . LYS G 5 155 ? 55.777  17.839  9.817  1.000 167.755 0 155 LYS GGG CA  1 ? 10 
ATOM 8862  C C   . LYS G 5 155 ? 57.040  17.094  9.410  1.000 163.610 0 155 LYS GGG C   1 ? 10 
ATOM 8863  O O   . LYS G 5 155 ? 57.009  16.234  8.523  1.000 167.995 0 155 LYS GGG O   1 ? 10 
ATOM 8864  C CB  . LYS G 5 155 ? 54.761  16.854  10.394 1.000 181.068 0 155 LYS GGG CB  1 ? 10 
ATOM 8865  C CG  . LYS G 5 155 ? 53.402  17.436  10.748 1.000 190.135 0 155 LYS GGG CG  1 ? 10 
ATOM 8866  C CD  . LYS G 5 155 ? 52.486  16.331  11.254 1.000 200.988 0 155 LYS GGG CD  1 ? 10 
ATOM 8867  C CE  . LYS G 5 155 ? 51.234  16.879  11.897 1.000 210.139 0 155 LYS GGG CE  1 ? 10 
ATOM 8868  N NZ  . LYS G 5 155 ? 50.267  15.792  12.189 1.000 213.328 0 155 LYS GGG NZ  1 ? 10 
ATOM 8869  N N   . ILE G 5 156 ? 58.144  17.419  10.072 1.000 157.219 0 156 ILE GGG N   1 ? 10 
ATOM 8870  C CA  . ILE G 5 156 ? 59.432  16.788  9.821  1.000 157.598 0 156 ILE GGG CA  1 ? 10 
ATOM 8871  C C   . ILE G 5 156 ? 59.649  15.766  10.926 1.000 160.718 0 156 ILE GGG C   1 ? 10 
ATOM 8872  O O   . ILE G 5 156 ? 59.782  16.123  12.101 1.000 163.439 0 156 ILE GGG O   1 ? 10 
ATOM 8873  C CB  . ILE G 5 156 ? 60.573  17.811  9.782  1.000 153.688 0 156 ILE GGG CB  1 ? 10 
ATOM 8874  C CG1 . ILE G 5 156 ? 60.276  18.901  8.752  1.000 153.779 0 156 ILE GGG CG1 1 ? 10 
ATOM 8875  C CG2 . ILE G 5 156 ? 61.888  17.114  9.458  1.000 150.129 0 156 ILE GGG CG2 1 ? 10 
ATOM 8876  C CD1 . ILE G 5 156 ? 60.063  18.379  7.358  1.000 146.601 0 156 ILE GGG CD1 1 ? 10 
ATOM 8877  N N   . THR G 5 157 ? 59.689  14.494  10.553 1.000 162.367 0 157 THR GGG N   1 ? 10 
ATOM 8878  C CA  . THR G 5 157 ? 59.747  13.397  11.504 1.000 163.133 0 157 THR GGG CA  1 ? 10 
ATOM 8879  C C   . THR G 5 157 ? 61.002  12.577  11.255 1.000 162.563 0 157 THR GGG C   1 ? 10 
ATOM 8880  O O   . THR G 5 157 ? 61.429  12.412  10.108 1.000 170.973 0 157 THR GGG O   1 ? 10 
ATOM 8881  C CB  . THR G 5 157 ? 58.516  12.490  11.393 1.000 168.405 0 157 THR GGG CB  1 ? 10 
ATOM 8882  O OG1 . THR G 5 157 ? 58.307  12.131  10.022 1.000 173.294 0 157 THR GGG OG1 1 ? 10 
ATOM 8883  C CG2 . THR G 5 157 ? 57.278  13.201  11.919 1.000 169.908 0 157 THR GGG CG2 1 ? 10 
ATOM 8884  N N   . ILE G 5 158 ? 61.595  12.073  12.333 1.000 166.545 0 158 ILE GGG N   1 ? 10 
ATOM 8885  C CA  . ILE G 5 158 ? 62.707  11.138  12.229 1.000 175.967 0 158 ILE GGG CA  1 ? 10 
ATOM 8886  C C   . ILE G 5 158 ? 62.100  9.741   12.169 1.000 193.753 0 158 ILE GGG C   1 ? 10 
ATOM 8887  O O   . ILE G 5 158 ? 61.759  9.144   13.191 1.000 205.353 0 158 ILE GGG O   1 ? 10 
ATOM 8888  C CB  . ILE G 5 158 ? 63.698  11.296  13.381 1.000 171.227 0 158 ILE GGG CB  1 ? 10 
ATOM 8889  C CG1 . ILE G 5 158 ? 64.024  12.779  13.587 1.000 174.141 0 158 ILE GGG CG1 1 ? 10 
ATOM 8890  C CG2 . ILE G 5 158 ? 64.941  10.470  13.116 1.000 168.008 0 158 ILE GGG CG2 1 ? 10 
ATOM 8891  C CD1 . ILE G 5 158 ? 64.776  13.074  14.861 1.000 184.716 0 158 ILE GGG CD1 1 ? 10 
ATOM 8892  N N   . ALA G 5 159 ? 61.988  9.217   10.947 1.000 201.351 0 159 ALA GGG N   1 ? 10 
ATOM 8893  C CA  . ALA G 5 159 ? 61.316  7.945   10.711 1.000 203.971 0 159 ALA GGG CA  1 ? 10 
ATOM 8894  C C   . ALA G 5 159 ? 62.144  6.764   11.192 1.000 213.142 0 159 ALA GGG C   1 ? 10 
ATOM 8895  O O   . ALA G 5 159 ? 61.584  5.783   11.693 1.000 214.091 0 159 ALA GGG O   1 ? 10 
ATOM 8896  C CB  . ALA G 5 159 ? 60.985  7.798   9.226  1.000 204.624 0 159 ALA GGG CB  1 ? 10 
ATOM 8897  N N   . ASP G 5 160 ? 63.468  6.847   11.089 1.000 224.039 0 160 ASP GGG N   1 ? 10 
ATOM 8898  C CA  . ASP G 5 160 ? 64.316  5.776   11.583 1.000 233.536 0 160 ASP GGG CA  1 ? 10 
ATOM 8899  C C   . ASP G 5 160 ? 65.665  6.344   11.991 1.000 232.648 0 160 ASP GGG C   1 ? 10 
ATOM 8900  O O   . ASP G 5 160 ? 66.096  7.396   11.512 1.000 225.703 0 160 ASP GGG O   1 ? 10 
ATOM 8901  C CB  . ASP G 5 160 ? 64.503  4.682   10.520 1.000 243.764 0 160 ASP GGG CB  1 ? 10 
ATOM 8902  C CG  . ASP G 5 160 ? 64.965  3.366   11.110 1.000 254.837 0 160 ASP GGG CG  1 ? 10 
ATOM 8903  O OD1 . ASP G 5 160 ? 65.006  3.259   12.352 1.000 261.385 0 160 ASP GGG OD1 1 ? 10 
ATOM 8904  O OD2 . ASP G 5 160 ? 65.294  2.442   10.335 1.000 261.783 0 160 ASP GGG OD2 1 ? 10 
ATOM 8905  N N   . CYS G 5 161 ? 66.321  5.613   12.888 1.000 242.409 0 161 CYS GGG N   1 ? 10 
ATOM 8906  C CA  . CYS G 5 161 ? 67.658  5.908   13.379 1.000 247.045 0 161 CYS GGG CA  1 ? 10 
ATOM 8907  C C   . CYS G 5 161 ? 68.264  4.632   13.958 1.000 255.104 0 161 CYS GGG C   1 ? 10 
ATOM 8908  O O   . CYS G 5 161 ? 67.556  3.659   14.227 1.000 262.207 0 161 CYS GGG O   1 ? 10 
ATOM 8909  C CB  . CYS G 5 161 ? 67.620  7.090   14.362 1.000 251.446 0 161 CYS GGG CB  1 ? 10 
ATOM 8910  S SG  . CYS G 5 161 ? 66.312  7.018   15.613 1.000 261.233 0 161 CYS GGG SG  1 ? 10 
ATOM 8911  N N   . GLY G 5 162 ? 69.584  4.632   14.111 1.000 259.448 0 162 GLY GGG N   1 ? 10 
ATOM 8912  C CA  . GLY G 5 162 ? 70.277  3.473   14.639 1.000 265.046 0 162 GLY GGG CA  1 ? 10 
ATOM 8913  C C   . GLY G 5 162 ? 71.778  3.671   14.562 1.000 269.173 0 162 GLY GGG C   1 ? 10 
ATOM 8914  O O   . GLY G 5 162 ? 72.255  4.775   14.290 1.000 258.644 0 162 GLY GGG O   1 ? 10 
ATOM 8915  N N   . GLN G 5 163 ? 72.520  2.583   14.772 1.000 272.280 0 163 GLN GGG N   1 ? 10 
ATOM 8916  C CA  . GLN G 5 163 ? 73.974  2.670   14.801 1.000 285.007 0 163 GLN GGG CA  1 ? 10 
ATOM 8917  C C   . GLN G 5 163 ? 74.676  2.084   13.584 1.000 291.430 0 163 GLN GGG C   1 ? 10 
ATOM 8918  O O   . GLN G 5 163 ? 74.444  0.931   13.205 1.000 302.687 0 163 GLN GGG O   1 ? 10 
ATOM 8919  C CB  . GLN G 5 163 ? 74.477  1.927   16.046 1.000 285.607 0 163 GLN GGG CB  1 ? 10 
ATOM 8920  C CG  . GLN G 5 163 ? 75.988  1.909   16.290 1.000 290.679 0 163 GLN GGG CG  1 ? 10 
ATOM 8921  C CD  . GLN G 5 163 ? 76.602  3.231   16.689 1.000 289.434 0 163 GLN GGG CD  1 ? 10 
ATOM 8922  O OE1 . GLN G 5 163 ? 77.819  3.323   16.851 1.000 290.948 0 163 GLN GGG OE1 1 ? 10 
ATOM 8923  N NE2 . GLN G 5 163 ? 75.774  4.248   16.883 1.000 296.481 0 163 GLN GGG NE2 1 ? 10 
ATOM 8924  N N   . LEU G 5 164 ? 75.522  2.910   12.980 1.000 283.880 0 164 LEU GGG N   1 ? 10 
ATOM 8925  C CA  . LEU G 5 164 ? 76.480  2.597   11.933 1.000 284.150 0 164 LEU GGG CA  1 ? 10 
ATOM 8926  C C   . LEU G 5 164 ? 77.844  2.353   12.582 1.000 290.540 0 164 LEU GGG C   1 ? 10 
ATOM 8927  O O   . LEU G 5 164 ? 78.060  2.682   13.751 1.000 291.285 0 164 LEU GGG O   1 ? 10 
ATOM 8928  C CB  . LEU G 5 164 ? 76.496  3.699   10.874 1.000 274.270 0 164 LEU GGG CB  1 ? 10 
ATOM 8929  C CG  . LEU G 5 164 ? 75.156  3.755   10.138 1.000 261.149 0 164 LEU GGG CG  1 ? 10 
ATOM 8930  C CD1 . LEU G 5 164 ? 75.112  4.917   9.167  1.000 244.128 0 164 LEU GGG CD1 1 ? 10 
ATOM 8931  C CD2 . LEU G 5 164 ? 74.907  2.435   9.412  1.000 262.176 0 164 LEU GGG CD2 1 ? 10 
ATOM 8932  N N   . GLU G 5 165 ? 78.775  1.783   11.827 1.000 293.065 0 165 GLU GGG N   1 ? 10 
ATOM 8933  C CA  . GLU G 5 165 ? 80.110  1.565   12.387 1.000 303.654 0 165 GLU GGG CA  1 ? 10 
ATOM 8934  C C   . GLU G 5 165 ? 81.024  2.768   12.097 1.000 308.603 0 165 GLU GGG C   1 ? 10 
ATOM 8935  O O   . GLU G 5 165 ? 81.639  3.318   13.014 1.000 310.306 0 165 GLU GGG O   1 ? 10 
ATOM 8936  C CB  . GLU G 5 165 ? 80.720  0.262   11.849 1.000 305.956 0 165 GLU GGG CB  1 ? 10 
ATOM 8937  C CG  . GLU G 5 165 ? 81.110  0.286   10.380 1.000 304.754 0 165 GLU GGG CG  1 ? 10 
ATOM 8938  C CD  . GLU G 5 165 ? 79.906  0.237   9.461  1.000 299.331 0 165 GLU GGG CD  1 ? 10 
ATOM 8939  O OE1 . GLU G 5 165 ? 78.875  -0.348  9.858  1.000 300.313 0 165 GLU GGG OE1 1 ? 10 
ATOM 8940  O OE2 . GLU G 5 165 ? 79.984  0.799   8.349  1.000 294.530 0 165 GLU GGG OE2 1 ? 10 
ATOM 8941  O OXT . GLU G 5 165 ? 81.153  3.260   10.973 1.000 318.517 0 165 GLU GGG OXT 1 ? 10 
ATOM 8942  N N   . ASN H 5 3   ? 22.006  19.497  17.641 1.000 290.328 0 3   ASN HHH N   1 ? 11 
ATOM 8943  C CA  . ASN H 5 3   ? 22.282  20.583  16.738 1.000 285.680 0 3   ASN HHH CA  1 ? 11 
ATOM 8944  C C   . ASN H 5 3   ? 21.049  20.914  15.883 1.000 291.596 0 3   ASN HHH C   1 ? 11 
ATOM 8945  O O   . ASN H 5 3   ? 20.918  20.445  14.760 1.000 295.340 0 3   ASN HHH O   1 ? 11 
ATOM 8946  C CB  . ASN H 5 3   ? 23.463  20.232  15.830 1.000 280.209 0 3   ASN HHH CB  1 ? 11 
ATOM 8947  C CG  . ASN H 5 3   ? 24.805  20.431  16.507 1.000 276.640 0 3   ASN HHH CG  1 ? 11 
ATOM 8948  O OD1 . ASN H 5 3   ? 24.891  20.523  17.729 1.000 286.589 0 3   ASN HHH OD1 1 ? 11 
ATOM 8949  N ND2 . ASN H 5 3   ? 25.864  20.485  15.708 1.000 269.991 0 3   ASN HHH ND2 1 ? 11 
ATOM 8950  N N   . PRO H 5 4   ? 20.144  21.702  16.429 1.000 286.157 0 4   PRO HHH N   1 ? 11 
ATOM 8951  C CA  . PRO H 5 4   ? 18.912  22.071  15.721 1.000 290.341 0 4   PRO HHH CA  1 ? 11 
ATOM 8952  C C   . PRO H 5 4   ? 19.183  23.109  14.638 1.000 295.627 0 4   PRO HHH C   1 ? 11 
ATOM 8953  O O   . PRO H 5 4   ? 20.303  23.575  14.461 1.000 303.200 0 4   PRO HHH O   1 ? 11 
ATOM 8954  C CB  . PRO H 5 4   ? 18.047  22.660  16.828 1.000 287.009 0 4   PRO HHH CB  1 ? 11 
ATOM 8955  C CG  . PRO H 5 4   ? 18.998  23.163  17.878 1.000 285.791 0 4   PRO HHH CG  1 ? 11 
ATOM 8956  C CD  . PRO H 5 4   ? 20.366  22.554  17.609 1.000 284.006 0 4   PRO HHH CD  1 ? 11 
ATOM 8957  N N   . THR H 5 5   ? 18.127  23.462  13.899 1.000 306.754 0 5   THR HHH N   1 ? 11 
ATOM 8958  C CA  . THR H 5 5   ? 18.203  24.459  12.841 1.000 296.775 0 5   THR HHH CA  1 ? 11 
ATOM 8959  C C   . THR H 5 5   ? 17.254  25.607  13.156 1.000 287.680 0 5   THR HHH C   1 ? 11 
ATOM 8960  O O   . THR H 5 5   ? 16.137  25.389  13.630 1.000 301.629 0 5   THR HHH O   1 ? 11 
ATOM 8961  C CB  . THR H 5 5   ? 17.832  23.852  11.480 1.000 307.755 0 5   THR HHH CB  1 ? 11 
ATOM 8962  O OG1 . THR H 5 5   ? 18.417  22.549  11.364 1.000 317.295 0 5   THR HHH OG1 1 ? 11 
ATOM 8963  C CG2 . THR H 5 5   ? 18.311  24.736  10.335 1.000 299.463 0 5   THR HHH CG2 1 ? 11 
ATOM 8964  N N   . VAL H 5 6   ? 17.697  26.839  12.883 1.000 279.462 0 6   VAL HHH N   1 ? 11 
ATOM 8965  C CA  . VAL H 5 6   ? 16.922  28.035  13.196 1.000 264.718 0 6   VAL HHH CA  1 ? 11 
ATOM 8966  C C   . VAL H 5 6   ? 16.969  28.983  12.002 1.000 258.532 0 6   VAL HHH C   1 ? 11 
ATOM 8967  O O   . VAL H 5 6   ? 18.000  29.097  11.330 1.000 252.859 0 6   VAL HHH O   1 ? 11 
ATOM 8968  C CB  . VAL H 5 6   ? 17.452  28.716  14.477 1.000 249.309 0 6   VAL HHH CB  1 ? 11 
ATOM 8969  C CG1 . VAL H 5 6   ? 16.894  30.117  14.629 1.000 246.435 0 6   VAL HHH CG1 1 ? 11 
ATOM 8970  C CG2 . VAL H 5 6   ? 17.129  27.871  15.700 1.000 248.187 0 6   VAL HHH CG2 1 ? 11 
ATOM 8971  N N   . PHE H 5 7   ? 15.859  29.678  11.751 1.000 242.496 0 7   PHE HHH N   1 ? 11 
ATOM 8972  C CA  . PHE H 5 7   ? 15.692  30.547  10.591 1.000 236.721 0 7   PHE HHH CA  1 ? 11 
ATOM 8973  C C   . PHE H 5 7   ? 15.307  31.960  11.020 1.000 231.393 0 7   PHE HHH C   1 ? 11 
ATOM 8974  O O   . PHE H 5 7   ? 14.562  32.135  11.985 1.000 237.360 0 7   PHE HHH O   1 ? 11 
ATOM 8975  C CB  . PHE H 5 7   ? 14.651  29.947  9.633  1.000 255.181 0 7   PHE HHH CB  1 ? 11 
ATOM 8976  C CG  . PHE H 5 7   ? 13.220  30.274  9.981  1.000 273.366 0 7   PHE HHH CG  1 ? 11 
ATOM 8977  C CD1 . PHE H 5 7   ? 12.620  31.443  9.538  1.000 280.902 0 7   PHE HHH CD1 1 ? 11 
ATOM 8978  C CD2 . PHE H 5 7   ? 12.470  29.395  10.748 1.000 290.060 0 7   PHE HHH CD2 1 ? 11 
ATOM 8979  C CE1 . PHE H 5 7   ? 11.302  31.727  9.857  1.000 291.235 0 7   PHE HHH CE1 1 ? 11 
ATOM 8980  C CE2 . PHE H 5 7   ? 11.152  29.675  11.068 1.000 298.169 0 7   PHE HHH CE2 1 ? 11 
ATOM 8981  C CZ  . PHE H 5 7   ? 10.569  30.842  10.623 1.000 295.651 0 7   PHE HHH CZ  1 ? 11 
ATOM 8982  N N   . PHE H 5 8   ? 15.819  32.965  10.304 1.000 213.601 0 8   PHE HHH N   1 ? 11 
ATOM 8983  C CA  . PHE H 5 8   ? 15.459  34.366  10.514 1.000 213.782 0 8   PHE HHH CA  1 ? 11 
ATOM 8984  C C   . PHE H 5 8   ? 15.004  34.962  9.190  1.000 204.324 0 8   PHE HHH C   1 ? 11 
ATOM 8985  O O   . PHE H 5 8   ? 15.714  34.849  8.188  1.000 204.841 0 8   PHE HHH O   1 ? 11 
ATOM 8986  C CB  . PHE H 5 8   ? 16.639  35.208  11.035 1.000 215.309 0 8   PHE HHH CB  1 ? 11 
ATOM 8987  C CG  . PHE H 5 8   ? 16.989  34.998  12.488 1.000 218.901 0 8   PHE HHH CG  1 ? 11 
ATOM 8988  C CD1 . PHE H 5 8   ? 16.808  33.783  13.122 1.000 237.973 0 8   PHE HHH CD1 1 ? 11 
ATOM 8989  C CD2 . PHE H 5 8   ? 17.525  36.048  13.214 1.000 203.769 0 8   PHE HHH CD2 1 ? 11 
ATOM 8990  C CE1 . PHE H 5 8   ? 17.137  33.626  14.456 1.000 245.719 0 8   PHE HHH CE1 1 ? 11 
ATOM 8991  C CE2 . PHE H 5 8   ? 17.859  35.897  14.541 1.000 207.259 0 8   PHE HHH CE2 1 ? 11 
ATOM 8992  C CZ  . PHE H 5 8   ? 17.665  34.684  15.164 1.000 226.544 0 8   PHE HHH CZ  1 ? 11 
ATOM 8993  N N   . ASP H 5 9   ? 13.831  35.603  9.187  1.000 208.972 0 9   ASP HHH N   1 ? 11 
ATOM 8994  C CA  . ASP H 5 9   ? 13.396  36.474  8.094  1.000 208.555 0 9   ASP HHH CA  1 ? 11 
ATOM 8995  C C   . ASP H 5 9   ? 13.678  37.948  8.380  1.000 199.957 0 9   ASP HHH C   1 ? 11 
ATOM 8996  O O   . ASP H 5 9   ? 13.162  38.506  9.356  1.000 198.731 0 9   ASP HHH O   1 ? 11 
ATOM 8997  C CB  . ASP H 5 9   ? 11.906  36.294  7.805  1.000 228.278 0 9   ASP HHH CB  1 ? 11 
ATOM 8998  C CG  . ASP H 5 9   ? 11.609  35.047  6.996  1.000 236.859 0 9   ASP HHH CG  1 ? 11 
ATOM 8999  O OD1 . ASP H 5 9   ? 12.377  34.074  7.097  1.000 237.663 0 9   ASP HHH OD1 1 ? 11 
ATOM 9000  O OD2 . ASP H 5 9   ? 10.608  35.043  6.248  1.000 239.466 0 9   ASP HHH OD2 1 ? 11 
ATOM 9001  N N   . ILE H 5 10  ? 14.487  38.577  7.518  1.000 189.184 0 10  ILE HHH N   1 ? 11 
ATOM 9002  C CA  . ILE H 5 10  ? 14.992  39.935  7.706  1.000 165.639 0 10  ILE HHH CA  1 ? 11 
ATOM 9003  C C   . ILE H 5 10  ? 14.164  40.892  6.860  1.000 160.896 0 10  ILE HHH C   1 ? 11 
ATOM 9004  O O   . ILE H 5 10  ? 13.827  40.575  5.714  1.000 164.618 0 10  ILE HHH O   1 ? 11 
ATOM 9005  C CB  . ILE H 5 10  ? 16.480  40.026  7.335  1.000 157.020 0 10  ILE HHH CB  1 ? 11 
ATOM 9006  C CG1 . ILE H 5 10  ? 17.250  38.991  8.137  1.000 159.430 0 10  ILE HHH CG1 1 ? 11 
ATOM 9007  C CG2 . ILE H 5 10  ? 16.991  41.421  7.595  1.000 166.005 0 10  ILE HHH CG2 1 ? 11 
ATOM 9008  C CD1 . ILE H 5 10  ? 17.210  39.266  9.605  1.000 181.743 0 10  ILE HHH CD1 1 ? 11 
ATOM 9009  N N   . ALA H 5 11  ? 13.842  42.068  7.409  1.000 158.376 0 11  ALA HHH N   1 ? 11 
ATOM 9010  C CA  . ALA H 5 11  ? 13.130  43.108  6.671  1.000 158.518 0 11  ALA HHH CA  1 ? 11 
ATOM 9011  C C   . ALA H 5 11  ? 13.887  44.429  6.735  1.000 151.544 0 11  ALA HHH C   1 ? 11 
ATOM 9012  O O   . ALA H 5 11  ? 14.607  44.702  7.698  1.000 160.607 0 11  ALA HHH O   1 ? 11 
ATOM 9013  C CB  . ALA H 5 11  ? 11.710  43.299  7.203  1.000 181.497 0 11  ALA HHH CB  1 ? 11 
ATOM 9014  N N   . VAL H 5 12  ? 13.706  45.256  5.702  1.000 154.958 0 12  VAL HHH N   1 ? 11 
ATOM 9015  C CA  . VAL H 5 12  ? 14.356  46.563  5.602  1.000 163.792 0 12  VAL HHH CA  1 ? 11 
ATOM 9016  C C   . VAL H 5 12  ? 13.316  47.663  5.424  1.000 173.686 0 12  VAL HHH C   1 ? 11 
ATOM 9017  O O   . VAL H 5 12  ? 12.656  47.738  4.379  1.000 185.909 0 12  VAL HHH O   1 ? 11 
ATOM 9018  C CB  . VAL H 5 12  ? 15.367  46.602  4.449  1.000 157.488 0 12  VAL HHH CB  1 ? 11 
ATOM 9019  C CG1 . VAL H 5 12  ? 15.968  47.996  4.317  1.000 153.171 0 12  VAL HHH CG1 1 ? 11 
ATOM 9020  C CG2 . VAL H 5 12  ? 16.445  45.556  4.660  1.000 158.487 0 12  VAL HHH CG2 1 ? 11 
ATOM 9021  N N   . ASP H 5 13  ? 13.197  48.536  6.428  1.000 177.188 0 13  ASP HHH N   1 ? 11 
ATOM 9022  C CA  . ASP H 5 13  ? 12.158  49.570  6.478  1.000 190.249 0 13  ASP HHH CA  1 ? 11 
ATOM 9023  C C   . ASP H 5 13  ? 10.779  48.993  6.156  1.000 203.949 0 13  ASP HHH C   1 ? 11 
ATOM 9024  O O   . ASP H 5 13  ? 9.974   49.600  5.445  1.000 210.709 0 13  ASP HHH O   1 ? 11 
ATOM 9025  C CB  . ASP H 5 13  ? 12.514  50.725  5.536  1.000 191.902 0 13  ASP HHH CB  1 ? 11 
ATOM 9026  C CG  . ASP H 5 13  ? 11.897  52.049  5.957  1.000 205.021 0 13  ASP HHH CG  1 ? 11 
ATOM 9027  O OD1 . ASP H 5 13  ? 10.654  52.167  5.986  1.000 224.952 0 13  ASP HHH OD1 1 ? 11 
ATOM 9028  O OD2 . ASP H 5 13  ? 12.675  52.981  6.256  1.000 197.609 0 13  ASP HHH OD2 1 ? 11 
ATOM 9029  N N   . GLY H 5 14  ? 10.510  47.795  6.671  1.000 203.677 0 14  GLY HHH N   1 ? 11 
ATOM 9030  C CA  . GLY H 5 14  ? 9.257   47.113  6.432  1.000 201.889 0 14  GLY HHH CA  1 ? 11 
ATOM 9031  C C   . GLY H 5 14  ? 9.186   46.316  5.148  1.000 201.042 0 14  GLY HHH C   1 ? 11 
ATOM 9032  O O   . GLY H 5 14  ? 8.150   45.688  4.886  1.000 209.879 0 14  GLY HHH O   1 ? 11 
ATOM 9033  N N   . GLU H 5 15  ? 10.243  46.322  4.338  1.000 192.030 0 15  GLU HHH N   1 ? 11 
ATOM 9034  C CA  . GLU H 5 15  ? 10.260  45.597  3.075  1.000 185.982 0 15  GLU HHH CA  1 ? 11 
ATOM 9035  C C   . GLU H 5 15  ? 10.994  44.275  3.239  1.000 178.100 0 15  GLU HHH C   1 ? 11 
ATOM 9036  O O   . GLU H 5 15  ? 12.111  44.254  3.778  1.000 182.786 0 15  GLU HHH O   1 ? 11 
ATOM 9037  C CB  . GLU H 5 15  ? 10.922  46.449  1.996  1.000 179.946 0 15  GLU HHH CB  1 ? 11 
ATOM 9038  C CG  . GLU H 5 15  ? 10.287  47.842  1.904  1.000 184.413 0 15  GLU HHH CG  1 ? 11 
ATOM 9039  C CD  . GLU H 5 15  ? 10.809  48.672  0.751  1.000 181.131 0 15  GLU HHH CD  1 ? 11 
ATOM 9040  O OE1 . GLU H 5 15  ? 11.194  48.071  -0.246 1.000 176.840 0 15  GLU HHH OE1 1 ? 11 
ATOM 9041  O OE2 . GLU H 5 15  ? 10.810  49.916  0.857  1.000 183.868 0 15  GLU HHH OE2 1 ? 11 
ATOM 9042  N N   . PRO H 5 16  ? 10.403  43.165  2.800  1.000 177.517 0 16  PRO HHH N   1 ? 11 
ATOM 9043  C CA  . PRO H 5 16  ? 11.026  41.851  3.012  1.000 177.652 0 16  PRO HHH CA  1 ? 11 
ATOM 9044  C C   . PRO H 5 16  ? 12.358  41.729  2.286  1.000 179.081 0 16  PRO HHH C   1 ? 11 
ATOM 9045  O O   . PRO H 5 16  ? 12.538  42.266  1.192  1.000 179.361 0 16  PRO HHH O   1 ? 11 
ATOM 9046  C CB  . PRO H 5 16  ? 9.990   40.877  2.441  1.000 185.376 0 16  PRO HHH CB  1 ? 11 
ATOM 9047  C CG  . PRO H 5 16  ? 9.231   41.695  1.433  1.000 187.337 0 16  PRO HHH CG  1 ? 11 
ATOM 9048  C CD  . PRO H 5 16  ? 9.149   43.067  2.034  1.000 191.685 0 16  PRO HHH CD  1 ? 11 
ATOM 9049  N N   . LEU H 5 17  ? 13.301  41.026  2.919  1.000 178.186 0 17  LEU HHH N   1 ? 11 
ATOM 9050  C CA  . LEU H 5 17  ? 14.646  40.865  2.371  1.000 178.350 0 17  LEU HHH CA  1 ? 11 
ATOM 9051  C C   . LEU H 5 17  ? 14.998  39.408  2.098  1.000 171.657 0 17  LEU HHH C   1 ? 11 
ATOM 9052  O O   . LEU H 5 17  ? 15.382  39.079  0.972  1.000 172.804 0 17  LEU HHH O   1 ? 11 
ATOM 9053  C CB  . LEU H 5 17  ? 15.687  41.501  3.303  1.000 178.904 0 17  LEU HHH CB  1 ? 11 
ATOM 9054  C CG  . LEU H 5 17  ? 17.125  41.345  2.809  1.000 163.062 0 17  LEU HHH CG  1 ? 11 
ATOM 9055  C CD1 . LEU H 5 17  ? 17.244  42.115  1.516  1.000 163.381 0 17  LEU HHH CD1 1 ? 11 
ATOM 9056  C CD2 . LEU H 5 17  ? 18.140  41.862  3.815  1.000 167.222 0 17  LEU HHH CD2 1 ? 11 
ATOM 9057  N N   . GLY H 5 18  ? 14.902  38.528  3.084  1.000 172.056 0 18  GLY HHH N   1 ? 11 
ATOM 9058  C CA  . GLY H 5 18  ? 15.199  37.133  2.841  1.000 175.338 0 18  GLY HHH CA  1 ? 11 
ATOM 9059  C C   . GLY H 5 18  ? 15.297  36.369  4.141  1.000 179.626 0 18  GLY HHH C   1 ? 11 
ATOM 9060  O O   . GLY H 5 18  ? 15.186  36.934  5.233  1.000 175.458 0 18  GLY HHH O   1 ? 11 
ATOM 9061  N N   . ARG H 5 19  ? 15.519  35.064  3.999  1.000 184.171 0 19  ARG HHH N   1 ? 11 
ATOM 9062  C CA  . ARG H 5 19  ? 15.550  34.148  5.129  1.000 198.784 0 19  ARG HHH CA  1 ? 11 
ATOM 9063  C C   . ARG H 5 19  ? 16.947  33.575  5.291  1.000 195.956 0 19  ARG HHH C   1 ? 11 
ATOM 9064  O O   . ARG H 5 19  ? 17.520  33.039  4.337  1.000 193.647 0 19  ARG HHH O   1 ? 11 
ATOM 9065  C CB  . ARG H 5 19  ? 14.538  33.008  4.954  1.000 212.762 0 19  ARG HHH CB  1 ? 11 
ATOM 9066  C CG  . ARG H 5 19  ? 14.423  32.082  6.172  1.000 218.027 0 19  ARG HHH CG  1 ? 11 
ATOM 9067  C CD  . ARG H 5 19  ? 14.871  30.649  5.890  1.000 220.573 0 19  ARG HHH CD  1 ? 11 
ATOM 9068  N NE  . ARG H 5 19  ? 14.039  30.000  4.886  1.000 230.750 0 19  ARG HHH NE  1 ? 11 
ATOM 9069  C CZ  . ARG H 5 19  ? 14.337  28.851  4.285  1.000 234.397 0 19  ARG HHH CZ  1 ? 11 
ATOM 9070  N NH1 . ARG H 5 19  ? 15.439  28.190  4.596  1.000 237.025 0 19  ARG HHH NH1 1 ? 11 
ATOM 9071  N NH2 . ARG H 5 19  ? 13.521  28.361  3.364  1.000 232.485 0 19  ARG HHH NH2 1 ? 11 
ATOM 9072  N N   . VAL H 5 20  ? 17.481  33.673  6.504  1.000 208.433 0 20  VAL HHH N   1 ? 11 
ATOM 9073  C CA  . VAL H 5 20  ? 18.821  33.199  6.812  1.000 208.821 0 20  VAL HHH CA  1 ? 11 
ATOM 9074  C C   . VAL H 5 20  ? 18.675  32.064  7.810  1.000 223.322 0 20  VAL HHH C   1 ? 11 
ATOM 9075  O O   . VAL H 5 20  ? 18.074  32.242  8.877  1.000 229.969 0 20  VAL HHH O   1 ? 11 
ATOM 9076  C CB  . VAL H 5 20  ? 19.708  34.316  7.382  1.000 189.884 0 20  VAL HHH CB  1 ? 11 
ATOM 9077  C CG1 . VAL H 5 20  ? 21.017  33.740  7.895  1.000 191.153 0 20  VAL HHH CG1 1 ? 11 
ATOM 9078  C CG2 . VAL H 5 20  ? 19.944  35.388  6.339  1.000 189.010 0 20  VAL HHH CG2 1 ? 11 
ATOM 9079  N N   . SER H 5 21  ? 19.220  30.906  7.471  1.000 223.117 0 21  SER HHH N   1 ? 11 
ATOM 9080  C CA  . SER H 5 21  ? 19.178  29.760  8.363  1.000 232.289 0 21  SER HHH CA  1 ? 11 
ATOM 9081  C C   . SER H 5 21  ? 20.503  29.608  9.091  1.000 228.089 0 21  SER HHH C   1 ? 11 
ATOM 9082  O O   . SER H 5 21  ? 21.576  29.792  8.505  1.000 223.450 0 21  SER HHH O   1 ? 11 
ATOM 9083  C CB  . SER H 5 21  ? 18.865  28.468  7.607  1.000 246.542 0 21  SER HHH CB  1 ? 11 
ATOM 9084  O OG  . SER H 5 21  ? 19.981  28.035  6.857  1.000 252.069 0 21  SER HHH OG  1 ? 11 
ATOM 9085  N N   . PHE H 5 22  ? 20.419  29.265  10.368 1.000 228.713 0 22  PHE HHH N   1 ? 11 
ATOM 9086  C CA  . PHE H 5 22  ? 21.589  28.920  11.154 1.000 232.166 0 22  PHE HHH CA  1 ? 11 
ATOM 9087  C C   . PHE H 5 22  ? 21.335  27.557  11.756 1.000 243.198 0 22  PHE HHH C   1 ? 11 
ATOM 9088  O O   . PHE H 5 22  ? 20.218  27.249  12.189 1.000 248.772 0 22  PHE HHH O   1 ? 11 
ATOM 9089  C CB  . PHE H 5 22  ? 21.923  29.895  12.315 1.000 231.291 0 22  PHE HHH CB  1 ? 11 
ATOM 9090  C CG  . PHE H 5 22  ? 21.830  31.353  11.966 1.000 229.398 0 22  PHE HHH CG  1 ? 11 
ATOM 9091  C CD1 . PHE H 5 22  ? 20.611  31.948  11.690 1.000 227.006 0 22  PHE HHH CD1 1 ? 11 
ATOM 9092  C CD2 . PHE H 5 22  ? 22.975  32.132  11.922 1.000 229.059 0 22  PHE HHH CD2 1 ? 11 
ATOM 9093  C CE1 . PHE H 5 22  ? 20.537  33.282  11.372 1.000 223.169 0 22  PHE HHH CE1 1 ? 11 
ATOM 9094  C CE2 . PHE H 5 22  ? 22.907  33.467  11.605 1.000 224.786 0 22  PHE HHH CE2 1 ? 11 
ATOM 9095  C CZ  . PHE H 5 22  ? 21.688  34.044  11.328 1.000 222.258 0 22  PHE HHH CZ  1 ? 11 
ATOM 9096  N N   . GLU H 5 23  ? 22.390  26.762  11.795 1.000 259.830 0 23  GLU HHH N   1 ? 11 
ATOM 9097  C CA  . GLU H 5 23  ? 22.382  25.490  12.486 1.000 275.115 0 23  GLU HHH CA  1 ? 11 
ATOM 9098  C C   . GLU H 5 23  ? 23.161  25.831  13.752 1.000 273.888 0 23  GLU HHH C   1 ? 11 
ATOM 9099  O O   . GLU H 5 23  ? 24.210  26.485  13.690 1.000 277.153 0 23  GLU HHH O   1 ? 11 
ATOM 9100  C CB  . GLU H 5 23  ? 23.011  24.383  11.651 1.000 288.450 0 23  GLU HHH CB  1 ? 11 
ATOM 9101  C CG  . GLU H 5 23  ? 22.932  23.027  12.269 1.000 308.977 0 23  GLU HHH CG  1 ? 11 
ATOM 9102  C CD  . GLU H 5 23  ? 21.629  22.388  11.849 1.000 329.044 0 23  GLU HHH CD  1 ? 11 
ATOM 9103  O OE1 . GLU H 5 23  ? 20.985  22.985  10.957 1.000 334.077 0 23  GLU HHH OE1 1 ? 11 
ATOM 9104  O OE2 . GLU H 5 23  ? 21.275  21.298  12.346 1.000 351.487 0 23  GLU HHH OE2 1 ? 11 
ATOM 9105  N N   . LEU H 5 24  ? 22.669  25.398  14.907 1.000 274.940 0 24  LEU HHH N   1 ? 11 
ATOM 9106  C CA  . LEU H 5 24  ? 23.345  25.722  16.151 1.000 267.278 0 24  LEU HHH CA  1 ? 11 
ATOM 9107  C C   . LEU H 5 24  ? 24.091  24.546  16.742 1.000 276.220 0 24  LEU HHH C   1 ? 11 
ATOM 9108  O O   . LEU H 5 24  ? 23.549  23.446  16.872 1.000 297.067 0 24  LEU HHH O   1 ? 11 
ATOM 9109  C CB  . LEU H 5 24  ? 22.318  26.221  17.170 1.000 267.774 0 24  LEU HHH CB  1 ? 11 
ATOM 9110  C CG  . LEU H 5 24  ? 21.369  27.384  16.844 1.000 261.622 0 24  LEU HHH CG  1 ? 11 
ATOM 9111  C CD1 . LEU H 5 24  ? 20.487  27.662  18.052 1.000 263.216 0 24  LEU HHH CD1 1 ? 11 
ATOM 9112  C CD2 . LEU H 5 24  ? 22.122  28.615  16.409 1.000 252.455 0 24  LEU HHH CD2 1 ? 11 
ATOM 9113  N N   . PHE H 5 25  ? 25.340  24.824  17.116 1.000 259.255 0 25  PHE HHH N   1 ? 11 
ATOM 9114  C CA  . PHE H 5 25  ? 26.319  23.833  17.559 1.000 267.241 0 25  PHE HHH CA  1 ? 11 
ATOM 9115  C C   . PHE H 5 25  ? 26.204  23.568  19.059 1.000 289.558 0 25  PHE HHH C   1 ? 11 
ATOM 9116  O O   . PHE H 5 25  ? 27.061  23.911  19.875 1.000 306.156 0 25  PHE HHH O   1 ? 11 
ATOM 9117  C CB  . PHE H 5 25  ? 27.736  24.185  17.131 1.000 253.203 0 25  PHE HHH CB  1 ? 11 
ATOM 9118  C CG  . PHE H 5 25  ? 27.942  24.142  15.646 1.000 251.610 0 25  PHE HHH CG  1 ? 11 
ATOM 9119  C CD1 . PHE H 5 25  ? 27.622  25.200  14.824 1.000 247.599 0 25  PHE HHH CD1 1 ? 11 
ATOM 9120  C CD2 . PHE H 5 25  ? 28.458  22.984  15.076 1.000 255.364 0 25  PHE HHH CD2 1 ? 11 
ATOM 9121  C CE1 . PHE H 5 25  ? 27.821  25.117  13.456 1.000 240.653 0 25  PHE HHH CE1 1 ? 11 
ATOM 9122  C CE2 . PHE H 5 25  ? 28.661  22.895  13.708 1.000 245.273 0 25  PHE HHH CE2 1 ? 11 
ATOM 9123  C CZ  . PHE H 5 25  ? 28.339  23.969  12.897 1.000 237.634 0 25  PHE HHH CZ  1 ? 11 
ATOM 9124  N N   . ALA H 5 26  ? 25.065  22.960  19.391 1.000 294.288 0 26  ALA HHH N   1 ? 11 
ATOM 9125  C CA  . ALA H 5 26  ? 24.642  22.636  20.741 1.000 287.504 0 26  ALA HHH CA  1 ? 11 
ATOM 9126  C C   . ALA H 5 26  ? 25.557  21.588  21.360 1.000 288.502 0 26  ALA HHH C   1 ? 11 
ATOM 9127  O O   . ALA H 5 26  ? 25.527  21.384  22.583 1.000 290.159 0 26  ALA HHH O   1 ? 11 
ATOM 9128  C CB  . ALA H 5 26  ? 23.191  22.153  20.736 1.000 282.087 0 26  ALA HHH CB  1 ? 11 
ATOM 9129  N N   . ASP H 5 27  ? 26.329  20.890  20.523 1.000 286.605 0 27  ASP HHH N   1 ? 11 
ATOM 9130  C CA  . ASP H 5 27  ? 27.268  19.887  20.994 1.000 289.666 0 27  ASP HHH CA  1 ? 11 
ATOM 9131  C C   . ASP H 5 27  ? 28.432  20.482  21.766 1.000 287.276 0 27  ASP HHH C   1 ? 11 
ATOM 9132  O O   . ASP H 5 27  ? 29.034  19.775  22.576 1.000 299.148 0 27  ASP HHH O   1 ? 11 
ATOM 9133  C CB  . ASP H 5 27  ? 27.839  19.131  19.796 1.000 283.142 0 27  ASP HHH CB  1 ? 11 
ATOM 9134  C CG  . ASP H 5 27  ? 28.644  20.030  18.858 1.000 273.245 0 27  ASP HHH CG  1 ? 11 
ATOM 9135  O OD1 . ASP H 5 27  ? 28.224  21.191  18.624 1.000 277.961 0 27  ASP HHH OD1 1 ? 11 
ATOM 9136  O OD2 . ASP H 5 27  ? 29.661  19.547  18.302 1.000 265.155 0 27  ASP HHH OD2 1 ? 11 
ATOM 9137  N N   . LYS H 5 28  ? 28.777  21.751  21.537 1.000 285.557 0 28  LYS HHH N   1 ? 11 
ATOM 9138  C CA  . LYS H 5 28  ? 29.787  22.392  22.370 1.000 282.271 0 28  LYS HHH CA  1 ? 11 
ATOM 9139  C C   . LYS H 5 28  ? 29.198  23.315  23.428 1.000 285.789 0 28  LYS HHH C   1 ? 11 
ATOM 9140  O O   . LYS H 5 28  ? 29.717  23.366  24.545 1.000 277.334 0 28  LYS HHH O   1 ? 11 
ATOM 9141  C CB  . LYS H 5 28  ? 30.791  23.168  21.512 1.000 271.402 0 28  LYS HHH CB  1 ? 11 
ATOM 9142  C CG  . LYS H 5 28  ? 31.557  22.301  20.529 1.000 266.225 0 28  LYS HHH CG  1 ? 11 
ATOM 9143  C CD  . LYS H 5 28  ? 32.386  21.263  21.277 1.000 267.962 0 28  LYS HHH CD  1 ? 11 
ATOM 9144  C CE  . LYS H 5 28  ? 33.289  20.479  20.340 1.000 264.872 0 28  LYS HHH CE  1 ? 11 
ATOM 9145  N NZ  . LYS H 5 28  ? 32.495  19.598  19.432 1.000 264.135 0 28  LYS HHH NZ  1 ? 11 
ATOM 9146  N N   . VAL H 5 29  ? 28.129  24.038  23.114 1.000 297.262 0 29  VAL HHH N   1 ? 11 
ATOM 9147  C CA  . VAL H 5 29  ? 27.520  24.981  24.049 1.000 293.729 0 29  VAL HHH CA  1 ? 11 
ATOM 9148  C C   . VAL H 5 29  ? 26.006  24.795  24.013 1.000 293.773 0 29  VAL HHH C   1 ? 11 
ATOM 9149  O O   . VAL H 5 29  ? 25.292  25.604  23.405 1.000 293.482 0 29  VAL HHH O   1 ? 11 
ATOM 9150  C CB  . VAL H 5 29  ? 27.944  26.427  23.739 1.000 287.705 0 29  VAL HHH CB  1 ? 11 
ATOM 9151  C CG1 . VAL H 5 29  ? 29.360  26.666  24.227 1.000 286.149 0 29  VAL HHH CG1 1 ? 11 
ATOM 9152  C CG2 . VAL H 5 29  ? 27.892  26.681  22.239 1.000 292.633 0 29  VAL HHH CG2 1 ? 11 
ATOM 9153  N N   . PRO H 5 30  ? 25.474  23.748  24.654 1.000 287.567 0 30  PRO HHH N   1 ? 11 
ATOM 9154  C CA  . PRO H 5 30  ? 24.019  23.526  24.590 1.000 286.443 0 30  PRO HHH CA  1 ? 11 
ATOM 9155  C C   . PRO H 5 30  ? 23.219  24.617  25.276 1.000 284.040 0 30  PRO HHH C   1 ? 11 
ATOM 9156  O O   . PRO H 5 30  ? 22.172  25.019  24.754 1.000 283.162 0 30  PRO HHH O   1 ? 11 
ATOM 9157  C CB  . PRO H 5 30  ? 23.838  22.166  25.280 1.000 297.831 0 30  PRO HHH CB  1 ? 11 
ATOM 9158  C CG  . PRO H 5 30  ? 25.065  21.988  26.107 1.000 297.033 0 30  PRO HHH CG  1 ? 11 
ATOM 9159  C CD  . PRO H 5 30  ? 26.170  22.660  25.361 1.000 287.270 0 30  PRO HHH CD  1 ? 11 
ATOM 9160  N N   . LYS H 5 31  ? 23.670  25.102  26.439 1.000 282.214 0 31  LYS HHH N   1 ? 11 
ATOM 9161  C CA  . LYS H 5 31  ? 22.932  26.160  27.121 1.000 278.112 0 31  LYS HHH CA  1 ? 11 
ATOM 9162  C C   . LYS H 5 31  ? 22.828  27.396  26.242 1.000 277.923 0 31  LYS HHH C   1 ? 11 
ATOM 9163  O O   . LYS H 5 31  ? 21.762  28.015  26.150 1.000 283.956 0 31  LYS HHH O   1 ? 11 
ATOM 9164  C CB  . LYS H 5 31  ? 23.593  26.522  28.449 1.000 267.407 0 31  LYS HHH CB  1 ? 11 
ATOM 9165  C CG  . LYS H 5 31  ? 23.408  25.512  29.558 1.000 270.162 0 31  LYS HHH CG  1 ? 11 
ATOM 9166  C CD  . LYS H 5 31  ? 24.314  25.859  30.721 1.000 272.129 0 31  LYS HHH CD  1 ? 11 
ATOM 9167  C CE  . LYS H 5 31  ? 23.957  27.235  31.270 1.000 266.843 0 31  LYS HHH CE  1 ? 11 
ATOM 9168  N NZ  . LYS H 5 31  ? 24.682  27.559  32.528 1.000 259.546 0 31  LYS HHH NZ  1 ? 11 
ATOM 9169  N N   . THR H 5 32  ? 23.927  27.771  25.584 1.000 275.173 0 32  THR HHH N   1 ? 11 
ATOM 9170  C CA  . THR H 5 32  ? 23.891  28.969  24.758 1.000 264.395 0 32  THR HHH CA  1 ? 11 
ATOM 9171  C C   . THR H 5 32  ? 23.070  28.729  23.498 1.000 259.600 0 32  THR HHH C   1 ? 11 
ATOM 9172  O O   . THR H 5 32  ? 22.309  29.606  23.071 1.000 255.321 0 32  THR HHH O   1 ? 11 
ATOM 9173  C CB  . THR H 5 32  ? 25.314  29.404  24.404 1.000 264.171 0 32  THR HHH CB  1 ? 11 
ATOM 9174  O OG1 . THR H 5 32  ? 26.088  29.540  25.603 1.000 266.845 0 32  THR HHH OG1 1 ? 11 
ATOM 9175  C CG2 . THR H 5 32  ? 25.297  30.730  23.660 1.000 256.677 0 32  THR HHH CG2 1 ? 11 
ATOM 9176  N N   . ALA H 5 33  ? 23.214  27.550  22.884 1.000 261.763 0 33  ALA HHH N   1 ? 11 
ATOM 9177  C CA  . ALA H 5 33  ? 22.389  27.225  21.725 1.000 264.358 0 33  ALA HHH CA  1 ? 11 
ATOM 9178  C C   . ALA H 5 33  ? 20.915  27.208  22.103 1.000 270.216 0 33  ALA HHH C   1 ? 11 
ATOM 9179  O O   . ALA H 5 33  ? 20.071  27.761  21.388 1.000 270.037 0 33  ALA HHH O   1 ? 11 
ATOM 9180  C CB  . ALA H 5 33  ? 22.810  25.876  21.143 1.000 271.047 0 33  ALA HHH CB  1 ? 11 
ATOM 9181  N N   . GLU H 5 34  ? 20.586  26.559  23.224 1.000 276.008 0 34  GLU HHH N   1 ? 11 
ATOM 9182  C CA  . GLU H 5 34  ? 19.189  26.465  23.632 1.000 280.076 0 34  GLU HHH CA  1 ? 11 
ATOM 9183  C C   . GLU H 5 34  ? 18.641  27.851  23.934 1.000 276.780 0 34  GLU HHH C   1 ? 11 
ATOM 9184  O O   . GLU H 5 34  ? 17.490  28.162  23.603 1.000 283.970 0 34  GLU HHH O   1 ? 11 
ATOM 9185  C CB  . GLU H 5 34  ? 19.029  25.535  24.830 1.000 281.122 0 34  GLU HHH CB  1 ? 11 
ATOM 9186  C CG  . GLU H 5 34  ? 17.599  25.468  25.328 1.000 282.979 0 34  GLU HHH CG  1 ? 11 
ATOM 9187  C CD  . GLU H 5 34  ? 16.661  24.886  24.282 1.000 282.522 0 34  GLU HHH CD  1 ? 11 
ATOM 9188  O OE1 . GLU H 5 34  ? 16.923  23.761  23.805 1.000 287.269 0 34  GLU HHH OE1 1 ? 11 
ATOM 9189  O OE2 . GLU H 5 34  ? 15.666  25.555  23.929 1.000 283.857 0 34  GLU HHH OE2 1 ? 11 
ATOM 9190  N N   . ASN H 5 35  ? 19.460  28.688  24.578 1.000 268.202 0 35  ASN HHH N   1 ? 11 
ATOM 9191  C CA  . ASN H 5 35  ? 19.080  30.073  24.824 1.000 265.502 0 35  ASN HHH CA  1 ? 11 
ATOM 9192  C C   . ASN H 5 35  ? 18.721  30.737  23.508 1.000 258.946 0 35  ASN HHH C   1 ? 11 
ATOM 9193  O O   . ASN H 5 35  ? 17.650  31.337  23.369 1.000 256.907 0 35  ASN HHH O   1 ? 11 
ATOM 9194  C CB  . ASN H 5 35  ? 20.214  30.823  25.524 1.000 268.511 0 35  ASN HHH CB  1 ? 11 
ATOM 9195  C CG  . ASN H 5 35  ? 19.854  32.262  25.840 1.000 271.225 0 35  ASN HHH CG  1 ? 11 
ATOM 9196  O OD1 . ASN H 5 35  ? 18.888  32.529  26.556 1.000 290.624 0 35  ASN HHH OD1 1 ? 11 
ATOM 9197  N ND2 . ASN H 5 35  ? 20.627  33.199  25.303 1.000 259.449 0 35  ASN HHH ND2 1 ? 11 
ATOM 9198  N N   . PHE H 5 36  ? 19.612  30.627  22.522 1.000 276.590 0 36  PHE HHH N   1 ? 11 
ATOM 9199  C CA  . PHE H 5 36  ? 19.335  31.222  21.224 1.000 277.499 0 36  PHE HHH CA  1 ? 11 
ATOM 9200  C C   . PHE H 5 36  ? 18.115  30.557  20.606 1.000 280.782 0 36  PHE HHH C   1 ? 11 
ATOM 9201  O O   . PHE H 5 36  ? 17.254  31.234  20.034 1.000 282.484 0 36  PHE HHH O   1 ? 11 
ATOM 9202  C CB  . PHE H 5 36  ? 20.561  31.080  20.319 1.000 277.210 0 36  PHE HHH CB  1 ? 11 
ATOM 9203  C CG  . PHE H 5 36  ? 20.503  31.912  19.069 1.000 265.517 0 36  PHE HHH CG  1 ? 11 
ATOM 9204  C CD1 . PHE H 5 36  ? 19.931  31.405  17.914 1.000 268.457 0 36  PHE HHH CD1 1 ? 11 
ATOM 9205  C CD2 . PHE H 5 36  ? 21.033  33.192  19.040 1.000 254.957 0 36  PHE HHH CD2 1 ? 11 
ATOM 9206  C CE1 . PHE H 5 36  ? 19.878  32.159  16.759 1.000 258.574 0 36  PHE HHH CE1 1 ? 11 
ATOM 9207  C CE2 . PHE H 5 36  ? 20.983  33.951  17.886 1.000 248.727 0 36  PHE HHH CE2 1 ? 11 
ATOM 9208  C CZ  . PHE H 5 36  ? 20.406  33.433  16.744 1.000 245.310 0 36  PHE HHH CZ  1 ? 11 
ATOM 9209  N N   . ARG H 5 37  ? 18.020  29.228  20.721 1.000 270.884 0 37  ARG HHH N   1 ? 11 
ATOM 9210  C CA  . ARG H 5 37  ? 16.868  28.519  20.176 1.000 273.576 0 37  ARG HHH CA  1 ? 11 
ATOM 9211  C C   . ARG H 5 37  ? 15.572  29.010  20.814 1.000 275.729 0 37  ARG HHH C   1 ? 11 
ATOM 9212  O O   . ARG H 5 37  ? 14.600  29.316  20.116 1.000 273.167 0 37  ARG HHH O   1 ? 11 
ATOM 9213  C CB  . ARG H 5 37  ? 16.997  27.013  20.379 1.000 282.688 0 37  ARG HHH CB  1 ? 11 
ATOM 9214  C CG  . ARG H 5 37  ? 15.927  26.281  19.598 1.000 292.114 0 37  ARG HHH CG  1 ? 11 
ATOM 9215  C CD  . ARG H 5 37  ? 15.662  24.885  20.099 1.000 294.667 0 37  ARG HHH CD  1 ? 11 
ATOM 9216  N NE  . ARG H 5 37  ? 14.234  24.614  20.003 1.000 298.747 0 37  ARG HHH NE  1 ? 11 
ATOM 9217  C CZ  . ARG H 5 37  ? 13.343  24.952  20.925 1.000 301.750 0 37  ARG HHH CZ  1 ? 11 
ATOM 9218  N NH1 . ARG H 5 37  ? 13.689  25.628  22.009 1.000 285.719 0 37  ARG HHH NH1 1 ? 11 
ATOM 9219  N NH2 . ARG H 5 37  ? 12.064  24.635  20.739 1.000 319.402 0 37  ARG HHH NH2 1 ? 11 
ATOM 9220  N N   . ALA H 5 38  ? 15.535  29.075  22.151 1.000 286.659 0 38  ALA HHH N   1 ? 11 
ATOM 9221  C CA  . ALA H 5 38  ? 14.296  29.460  22.819 1.000 292.038 0 38  ALA HHH CA  1 ? 11 
ATOM 9222  C C   . ALA H 5 38  ? 13.968  30.918  22.538 1.000 277.005 0 38  ALA HHH C   1 ? 11 
ATOM 9223  O O   . ALA H 5 38  ? 12.795  31.281  22.389 1.000 285.254 0 38  ALA HHH O   1 ? 11 
ATOM 9224  C CB  . ALA H 5 38  ? 14.407  29.209  24.322 1.000 306.406 0 38  ALA HHH CB  1 ? 11 
ATOM 9225  N N   . LEU H 5 39  ? 14.990  31.772  22.468 1.000 265.364 0 39  LEU HHH N   1 ? 11 
ATOM 9226  C CA  . LEU H 5 39  ? 14.749  33.154  22.084 1.000 241.358 0 39  LEU HHH CA  1 ? 11 
ATOM 9227  C C   . LEU H 5 39  ? 14.291  33.208  20.635 1.000 237.519 0 39  LEU HHH C   1 ? 11 
ATOM 9228  O O   . LEU H 5 39  ? 13.543  34.107  20.242 1.000 225.930 0 39  LEU HHH O   1 ? 11 
ATOM 9229  C CB  . LEU H 5 39  ? 15.999  34.004  22.308 1.000 236.642 0 39  LEU HHH CB  1 ? 11 
ATOM 9230  C CG  . LEU H 5 39  ? 16.405  34.209  23.770 1.000 241.010 0 39  LEU HHH CG  1 ? 11 
ATOM 9231  C CD1 . LEU H 5 39  ? 17.724  34.952  23.867 1.000 229.722 0 39  LEU HHH CD1 1 ? 11 
ATOM 9232  C CD2 . LEU H 5 39  ? 15.320  34.949  24.540 1.000 255.746 0 39  LEU HHH CD2 1 ? 11 
ATOM 9233  N N   . SER H 5 40  ? 14.726  32.234  19.835 1.000 249.456 0 40  SER HHH N   1 ? 11 
ATOM 9234  C CA  . SER H 5 40  ? 14.350  32.152  18.431 1.000 253.765 0 40  SER HHH CA  1 ? 11 
ATOM 9235  C C   . SER H 5 40  ? 12.932  31.633  18.263 1.000 270.266 0 40  SER HHH C   1 ? 11 
ATOM 9236  O O   . SER H 5 40  ? 12.262  31.985  17.286 1.000 288.641 0 40  SER HHH O   1 ? 11 
ATOM 9237  C CB  . SER H 5 40  ? 15.327  31.255  17.670 1.000 252.455 0 40  SER HHH CB  1 ? 11 
ATOM 9238  O OG  . SER H 5 40  ? 16.630  31.810  17.681 1.000 246.980 0 40  SER HHH OG  1 ? 11 
ATOM 9239  N N   . THR H 5 41  ? 12.454  30.803  19.189 1.000 274.941 0 41  THR HHH N   1 ? 11 
ATOM 9240  C CA  . THR H 5 41  ? 11.100  30.290  19.070 1.000 270.844 0 41  THR HHH CA  1 ? 11 
ATOM 9241  C C   . THR H 5 41  ? 10.086  31.177  19.781 1.000 277.177 0 41  THR HHH C   1 ? 11 
ATOM 9242  O O   . THR H 5 41  ? 8.901   31.153  19.429 1.000 287.125 0 41  THR HHH O   1 ? 11 
ATOM 9243  C CB  . THR H 5 41  ? 11.049  28.872  19.661 1.000 284.276 0 41  THR HHH CB  1 ? 11 
ATOM 9244  O OG1 . THR H 5 41  ? 12.092  28.074  19.088 1.000 273.141 0 41  THR HHH OG1 1 ? 11 
ATOM 9245  C CG2 . THR H 5 41  ? 9.718   28.197  19.378 1.000 296.955 0 41  THR HHH CG2 1 ? 11 
ATOM 9246  N N   . GLY H 5 42  ? 10.534  31.977  20.747 1.000 272.365 0 42  GLY HHH N   1 ? 11 
ATOM 9247  C CA  . GLY H 5 42  ? 9.688   32.878  21.507 1.000 273.497 0 42  GLY HHH CA  1 ? 11 
ATOM 9248  C C   . GLY H 5 42  ? 8.787   32.202  22.510 1.000 286.015 0 42  GLY HHH C   1 ? 11 
ATOM 9249  O O   . GLY H 5 42  ? 7.827   32.816  22.984 1.000 291.882 0 42  GLY HHH O   1 ? 11 
ATOM 9250  N N   . GLU H 5 43  ? 9.067   30.943  22.839 1.000 300.483 0 43  GLU HHH N   1 ? 11 
ATOM 9251  C CA  . GLU H 5 43  ? 8.174   30.153  23.675 1.000 312.336 0 43  GLU HHH CA  1 ? 11 
ATOM 9252  C C   . GLU H 5 43  ? 8.123   30.628  25.118 1.000 314.558 0 43  GLU HHH C   1 ? 11 
ATOM 9253  O O   . GLU H 5 43  ? 7.161   30.312  25.826 1.000 333.557 0 43  GLU HHH O   1 ? 11 
ATOM 9254  C CB  . GLU H 5 43  ? 8.614   28.692  23.680 1.000 318.145 0 43  GLU HHH CB  1 ? 11 
ATOM 9255  C CG  . GLU H 5 43  ? 10.122  28.542  23.740 1.000 309.605 0 43  GLU HHH CG  1 ? 11 
ATOM 9256  C CD  . GLU H 5 43  ? 10.592  27.146  23.416 1.000 316.707 0 43  GLU HHH CD  1 ? 11 
ATOM 9257  O OE1 . GLU H 5 43  ? 9.760   26.317  22.991 1.000 332.720 0 43  GLU HHH OE1 1 ? 11 
ATOM 9258  O OE2 . GLU H 5 43  ? 11.796  26.875  23.603 1.000 312.243 0 43  GLU HHH OE2 1 ? 11 
ATOM 9259  N N   . LYS H 5 44  ? 9.121   31.384  25.569 1.000 290.873 0 44  LYS HHH N   1 ? 11 
ATOM 9260  C CA  . LYS H 5 44  ? 9.099   31.931  26.914 1.000 283.865 0 44  LYS HHH CA  1 ? 11 
ATOM 9261  C C   . LYS H 5 44  ? 8.371   33.263  27.036 1.000 278.988 0 44  LYS HHH C   1 ? 11 
ATOM 9262  O O   . LYS H 5 44  ? 8.245   33.778  28.154 1.000 279.706 0 44  LYS HHH O   1 ? 11 
ATOM 9263  C CB  . LYS H 5 44  ? 10.549  32.164  27.349 1.000 277.208 0 44  LYS HHH CB  1 ? 11 
ATOM 9264  C CG  . LYS H 5 44  ? 11.449  30.935  27.265 1.000 274.847 0 44  LYS HHH CG  1 ? 11 
ATOM 9265  C CD  . LYS H 5 44  ? 11.165  29.795  28.193 1.000 282.440 0 44  LYS HHH CD  1 ? 11 
ATOM 9266  C CE  . LYS H 5 44  ? 12.004  28.619  27.703 1.000 279.650 0 44  LYS HHH CE  1 ? 11 
ATOM 9267  N NZ  . LYS H 5 44  ? 11.613  27.306  28.264 1.000 299.485 0 44  LYS HHH NZ  1 ? 11 
ATOM 9268  N N   . GLY H 5 45  ? 7.890   33.834  25.939 1.000 285.362 0 45  GLY HHH N   1 ? 11 
ATOM 9269  C CA  . GLY H 5 45  ? 7.145   35.070  26.007 1.000 285.540 0 45  GLY HHH CA  1 ? 11 
ATOM 9270  C C   . GLY H 5 45  ? 7.988   36.252  25.592 1.000 280.032 0 45  GLY HHH C   1 ? 11 
ATOM 9271  O O   . GLY H 5 45  ? 7.487   37.381  25.561 1.000 274.857 0 45  GLY HHH O   1 ? 11 
ATOM 9272  N N   . PHE H 5 46  ? 9.262   36.010  25.283 1.000 282.408 0 46  PHE HHH N   1 ? 11 
ATOM 9273  C CA  . PHE H 5 46  ? 10.206  37.009  24.814 1.000 278.301 0 46  PHE HHH CA  1 ? 11 
ATOM 9274  C C   . PHE H 5 46  ? 11.252  36.335  23.940 1.000 268.011 0 46  PHE HHH C   1 ? 11 
ATOM 9275  O O   . PHE H 5 46  ? 11.775  35.275  24.297 1.000 268.784 0 46  PHE HHH O   1 ? 11 
ATOM 9276  C CB  . PHE H 5 46  ? 10.858  37.702  26.021 1.000 275.881 0 46  PHE HHH CB  1 ? 11 
ATOM 9277  C CG  . PHE H 5 46  ? 11.509  36.748  27.002 1.000 278.966 0 46  PHE HHH CG  1 ? 11 
ATOM 9278  C CD1 . PHE H 5 46  ? 12.838  36.368  26.869 1.000 275.550 0 46  PHE HHH CD1 1 ? 11 
ATOM 9279  C CD2 . PHE H 5 46  ? 10.776  36.219  28.056 1.000 294.491 0 46  PHE HHH CD2 1 ? 11 
ATOM 9280  C CE1 . PHE H 5 46  ? 13.425  35.489  27.777 1.000 279.550 0 46  PHE HHH CE1 1 ? 11 
ATOM 9281  C CE2 . PHE H 5 46  ? 11.356  35.341  28.965 1.000 298.767 0 46  PHE HHH CE2 1 ? 11 
ATOM 9282  C CZ  . PHE H 5 46  ? 12.682  34.976  28.824 1.000 289.236 0 46  PHE HHH CZ  1 ? 11 
ATOM 9283  N N   . GLY H 5 47  ? 11.521  36.921  22.787 1.000 256.966 0 47  GLY HHH N   1 ? 11 
ATOM 9284  C CA  . GLY H 5 47  ? 12.459  36.341  21.859 1.000 244.238 0 47  GLY HHH CA  1 ? 11 
ATOM 9285  C C   . GLY H 5 47  ? 12.855  37.326  20.785 1.000 237.555 0 47  GLY HHH C   1 ? 11 
ATOM 9286  O O   . GLY H 5 47  ? 12.679  38.536  20.932 1.000 239.166 0 47  GLY HHH O   1 ? 11 
ATOM 9287  N N   . TYR H 5 48  ? 13.392  36.791  19.683 1.000 236.028 0 48  TYR HHH N   1 ? 11 
ATOM 9288  C CA  . TYR H 5 48  ? 14.037  37.655  18.701 1.000 222.946 0 48  TYR HHH CA  1 ? 11 
ATOM 9289  C C   . TYR H 5 48  ? 13.052  38.338  17.754 1.000 219.136 0 48  TYR HHH C   1 ? 11 
ATOM 9290  O O   . TYR H 5 48  ? 13.427  39.334  17.126 1.000 211.237 0 48  TYR HHH O   1 ? 11 
ATOM 9291  C CB  . TYR H 5 48  ? 15.097  36.873  17.912 1.000 216.936 0 48  TYR HHH CB  1 ? 11 
ATOM 9292  C CG  . TYR H 5 48  ? 16.268  36.415  18.766 1.000 213.227 0 48  TYR HHH CG  1 ? 11 
ATOM 9293  C CD1 . TYR H 5 48  ? 16.863  37.284  19.672 1.000 201.402 0 48  TYR HHH CD1 1 ? 11 
ATOM 9294  C CD2 . TYR H 5 48  ? 16.800  35.137  18.643 1.000 222.528 0 48  TYR HHH CD2 1 ? 11 
ATOM 9295  C CE1 . TYR H 5 48  ? 17.934  36.889  20.457 1.000 211.205 0 48  TYR HHH CE1 1 ? 11 
ATOM 9296  C CE2 . TYR H 5 48  ? 17.879  34.734  19.420 1.000 225.368 0 48  TYR HHH CE2 1 ? 11 
ATOM 9297  C CZ  . TYR H 5 48  ? 18.440  35.615  20.327 1.000 220.588 0 48  TYR HHH CZ  1 ? 11 
ATOM 9298  O OH  . TYR H 5 48  ? 19.512  35.226  21.100 1.000 231.471 0 48  TYR HHH OH  1 ? 11 
ATOM 9299  N N   . LYS H 5 49  ? 11.822  37.830  17.615 1.000 216.412 0 49  LYS HHH N   1 ? 11 
ATOM 9300  C CA  . LYS H 5 49  ? 10.891  38.406  16.644 1.000 212.827 0 49  LYS HHH CA  1 ? 11 
ATOM 9301  C C   . LYS H 5 49  ? 10.616  39.875  16.940 1.000 211.369 0 49  LYS HHH C   1 ? 11 
ATOM 9302  O O   . LYS H 5 49  ? 10.246  40.240  18.059 1.000 218.670 0 49  LYS HHH O   1 ? 11 
ATOM 9303  C CB  . LYS H 5 49  ? 9.561   37.649  16.545 1.000 221.062 0 49  LYS HHH CB  1 ? 11 
ATOM 9304  C CG  . LYS H 5 49  ? 9.637   36.293  15.862 1.000 227.716 0 49  LYS HHH CG  1 ? 11 
ATOM 9305  C CD  . LYS H 5 49  ? 8.288   35.596  15.903 1.000 249.707 0 49  LYS HHH CD  1 ? 11 
ATOM 9306  C CE  . LYS H 5 49  ? 8.316   34.264  15.178 1.000 265.660 0 49  LYS HHH CE  1 ? 11 
ATOM 9307  N NZ  . LYS H 5 49  ? 7.004   33.564  15.248 1.000 279.174 0 49  LYS HHH NZ  1 ? 11 
ATOM 9308  N N   . GLY H 5 50  ? 10.809  40.720  15.928 1.000 206.348 0 50  GLY HHH N   1 ? 11 
ATOM 9309  C CA  . GLY H 5 50  ? 10.608  42.148  16.053 1.000 201.507 0 50  GLY HHH CA  1 ? 11 
ATOM 9310  C C   . GLY H 5 50  ? 11.812  42.958  16.473 1.000 204.415 0 50  GLY HHH C   1 ? 11 
ATOM 9311  O O   . GLY H 5 50  ? 11.704  44.187  16.567 1.000 204.107 0 50  GLY HHH O   1 ? 11 
ATOM 9312  N N   . SER H 5 51  ? 12.944  42.329  16.751 1.000 211.556 0 51  SER HHH N   1 ? 11 
ATOM 9313  C CA  . SER H 5 51  ? 14.079  43.105  17.216 1.000 208.658 0 51  SER HHH CA  1 ? 11 
ATOM 9314  C C   . SER H 5 51  ? 14.838  43.631  16.002 1.000 197.938 0 51  SER HHH C   1 ? 11 
ATOM 9315  O O   . SER H 5 51  ? 14.623  43.198  14.870 1.000 199.615 0 51  SER HHH O   1 ? 11 
ATOM 9316  C CB  . SER H 5 51  ? 14.989  42.262  18.101 1.000 214.679 0 51  SER HHH CB  1 ? 11 
ATOM 9317  O OG  . SER H 5 51  ? 15.636  41.277  17.319 1.000 213.759 0 51  SER HHH OG  1 ? 11 
ATOM 9318  N N   . CYS H 5 52  ? 15.728  44.585  16.236 1.000 187.102 0 52  CYS HHH N   1 ? 11 
ATOM 9319  C CA  . CYS H 5 52  ? 16.441  45.208  15.135 1.000 173.687 0 52  CYS HHH CA  1 ? 11 
ATOM 9320  C C   . CYS H 5 52  ? 17.919  44.851  15.201 1.000 164.233 0 52  CYS HHH C   1 ? 11 
ATOM 9321  O O   . CYS H 5 52  ? 18.426  44.398  16.231 1.000 157.611 0 52  CYS HHH O   1 ? 11 
ATOM 9322  C CB  . CYS H 5 52  ? 16.249  46.728  15.151 1.000 174.565 0 52  CYS HHH CB  1 ? 11 
ATOM 9323  S SG  . CYS H 5 52  ? 17.221  47.595  16.395 1.000 176.305 0 52  CYS HHH SG  1 ? 11 
ATOM 9324  N N   . PHE H 5 53  ? 18.607  45.031  14.075 1.000 155.326 0 53  PHE HHH N   1 ? 11 
ATOM 9325  C CA  . PHE H 5 53  ? 20.063  45.034  14.067 1.000 142.384 0 53  PHE HHH CA  1 ? 11 
ATOM 9326  C C   . PHE H 5 53  ? 20.573  46.458  14.251 1.000 140.395 0 53  PHE HHH C   1 ? 11 
ATOM 9327  O O   . PHE H 5 53  ? 20.448  47.297  13.353 1.000 139.805 0 53  PHE HHH O   1 ? 11 
ATOM 9328  C CB  . PHE H 5 53  ? 20.600  44.409  12.782 1.000 143.939 0 53  PHE HHH CB  1 ? 11 
ATOM 9329  C CG  . PHE H 5 53  ? 20.570  42.906  12.786 1.000 145.698 0 53  PHE HHH CG  1 ? 11 
ATOM 9330  C CD1 . PHE H 5 53  ? 19.415  42.212  12.464 1.000 159.251 0 53  PHE HHH CD1 1 ? 11 
ATOM 9331  C CD2 . PHE H 5 53  ? 21.701  42.186  13.137 1.000 141.959 0 53  PHE HHH CD2 1 ? 11 
ATOM 9332  C CE1 . PHE H 5 53  ? 19.397  40.825  12.480 1.000 162.996 0 53  PHE HHH CE1 1 ? 11 
ATOM 9333  C CE2 . PHE H 5 53  ? 21.688  40.804  13.155 1.000 145.388 0 53  PHE HHH CE2 1 ? 11 
ATOM 9334  C CZ  . PHE H 5 53  ? 20.537  40.123  12.828 1.000 152.733 0 53  PHE HHH CZ  1 ? 11 
ATOM 9335  N N   . HIS H 5 54  ? 21.118  46.728  15.435 1.000 138.095 0 54  HIS HHH N   1 ? 11 
ATOM 9336  C CA  . HIS H 5 54  ? 21.534  48.062  15.838 1.000 129.249 0 54  HIS HHH CA  1 ? 11 
ATOM 9337  C C   . HIS H 5 54  ? 22.981  48.364  15.463 1.000 122.041 0 54  HIS HHH C   1 ? 11 
ATOM 9338  O O   . HIS H 5 54  ? 23.329  49.533  15.267 1.000 119.038 0 54  HIS HHH O   1 ? 11 
ATOM 9339  C CB  . HIS H 5 54  ? 21.283  48.252  17.337 1.000 138.825 0 54  HIS HHH CB  1 ? 11 
ATOM 9340  C CG  . HIS H 5 54  ? 22.116  47.372  18.212 1.000 145.658 0 54  HIS HHH CG  1 ? 11 
ATOM 9341  N ND1 . HIS H 5 54  ? 21.749  46.081  18.526 1.000 142.073 0 54  HIS HHH ND1 1 ? 11 
ATOM 9342  C CD2 . HIS H 5 54  ? 23.283  47.600  18.859 1.000 143.356 0 54  HIS HHH CD2 1 ? 11 
ATOM 9343  C CE1 . HIS H 5 54  ? 22.658  45.549  19.323 1.000 140.738 0 54  HIS HHH CE1 1 ? 11 
ATOM 9344  N NE2 . HIS H 5 54  ? 23.599  46.450  19.541 1.000 138.028 0 54  HIS HHH NE2 1 ? 11 
ATOM 9345  N N   . ARG H 5 55  ? 23.827  47.340  15.339 1.000 120.403 0 55  ARG HHH N   1 ? 11 
ATOM 9346  C CA  . ARG H 5 55  ? 25.224  47.502  14.937 1.000 123.773 0 55  ARG HHH CA  1 ? 11 
ATOM 9347  C C   . ARG H 5 55  ? 25.510  46.642  13.712 1.000 121.547 0 55  ARG HHH C   1 ? 11 
ATOM 9348  O O   . ARG H 5 55  ? 25.563  45.410  13.809 1.000 116.183 0 55  ARG HHH O   1 ? 11 
ATOM 9349  C CB  . ARG H 5 55  ? 26.164  47.126  16.077 1.000 119.506 0 55  ARG HHH CB  1 ? 11 
ATOM 9350  C CG  . ARG H 5 55  ? 27.384  48.013  16.221 1.000 113.421 0 55  ARG HHH CG  1 ? 11 
ATOM 9351  C CD  . ARG H 5 55  ? 28.134  47.688  17.503 1.000 120.178 0 55  ARG HHH CD  1 ? 11 
ATOM 9352  N NE  . ARG H 5 55  ? 29.318  48.518  17.681 1.000 128.136 0 55  ARG HHH NE  1 ? 11 
ATOM 9353  C CZ  . ARG H 5 55  ? 30.560  48.105  17.465 1.000 124.292 0 55  ARG HHH CZ  1 ? 11 
ATOM 9354  N NH1 . ARG H 5 55  ? 30.817  46.869  17.062 1.000 116.365 0 55  ARG HHH NH1 1 ? 11 
ATOM 9355  N NH2 . ARG H 5 55  ? 31.569  48.951  17.650 1.000 130.177 0 55  ARG HHH NH2 1 ? 11 
ATOM 9356  N N   . ILE H 5 56  ? 25.689  47.292  12.563 1.000 122.323 0 56  ILE HHH N   1 ? 11 
ATOM 9357  C CA  . ILE H 5 56  ? 26.161  46.642  11.347 1.000 124.937 0 56  ILE HHH CA  1 ? 11 
ATOM 9358  C C   . ILE H 5 56  ? 27.406  47.380  10.864 1.000 125.038 0 56  ILE HHH C   1 ? 11 
ATOM 9359  O O   . ILE H 5 56  ? 27.340  48.566  10.526 1.000 125.264 0 56  ILE HHH O   1 ? 11 
ATOM 9360  C CB  . ILE H 5 56  ? 25.081  46.620  10.252 1.000 127.315 0 56  ILE HHH CB  1 ? 11 
ATOM 9361  C CG1 . ILE H 5 56  ? 23.873  45.804  10.713 1.000 118.627 0 56  ILE HHH CG1 1 ? 11 
ATOM 9362  C CG2 . ILE H 5 56  ? 25.655  46.042  8.980  1.000 129.115 0 56  ILE HHH CG2 1 ? 11 
ATOM 9363  C CD1 . ILE H 5 56  ? 22.784  45.681  9.655  1.000 130.890 0 56  ILE HHH CD1 1 ? 11 
ATOM 9364  N N   . ILE H 5 57  ? 28.531  46.681  10.825 1.000 123.208 0 57  ILE HHH N   1 ? 11 
ATOM 9365  C CA  . ILE H 5 57  ? 29.795  47.252  10.387 1.000 124.051 0 57  ILE HHH CA  1 ? 11 
ATOM 9366  C C   . ILE H 5 57  ? 30.255  46.464  9.172  1.000 121.509 0 57  ILE HHH C   1 ? 11 
ATOM 9367  O O   . ILE H 5 57  ? 30.644  45.296  9.322  1.000 118.589 0 57  ILE HHH O   1 ? 11 
ATOM 9368  C CB  . ILE H 5 57  ? 30.854  47.229  11.497 1.000 121.006 0 57  ILE HHH CB  1 ? 11 
ATOM 9369  C CG1 . ILE H 5 57  ? 30.354  48.003  12.706 1.000 124.531 0 57  ILE HHH CG1 1 ? 11 
ATOM 9370  C CG2 . ILE H 5 57  ? 32.160  47.829  10.999 1.000 121.870 0 57  ILE HHH CG2 1 ? 11 
ATOM 9371  C CD1 . ILE H 5 57  ? 31.295  48.034  13.877 1.000 124.490 0 57  ILE HHH CD1 1 ? 11 
ATOM 9372  N N   . PRO H 5 58  ? 30.230  47.042  7.971  1.000 121.835 0 58  PRO HHH N   1 ? 11 
ATOM 9373  C CA  . PRO H 5 58  ? 30.587  46.263  6.776  1.000 118.706 0 58  PRO HHH CA  1 ? 11 
ATOM 9374  C C   . PRO H 5 58  ? 32.026  45.778  6.866  1.000 121.545 0 58  PRO HHH C   1 ? 11 
ATOM 9375  O O   . PRO H 5 58  ? 32.922  46.502  7.304  1.000 123.661 0 58  PRO HHH O   1 ? 11 
ATOM 9376  C CB  . PRO H 5 58  ? 30.400  47.263  5.630  1.000 124.479 0 58  PRO HHH CB  1 ? 11 
ATOM 9377  C CG  . PRO H 5 58  ? 30.481  48.613  6.308  1.000 122.506 0 58  PRO HHH CG  1 ? 11 
ATOM 9378  C CD  . PRO H 5 58  ? 29.833  48.418  7.630  1.000 127.030 0 58  PRO HHH CD  1 ? 11 
ATOM 9379  N N   . GLY H 5 59  ? 32.238  44.532  6.455  1.000 124.332 0 59  GLY HHH N   1 ? 11 
ATOM 9380  C CA  . GLY H 5 59  ? 33.552  43.935  6.521  1.000 126.614 0 59  GLY HHH CA  1 ? 11 
ATOM 9381  C C   . GLY H 5 59  ? 33.915  43.427  7.896  1.000 129.519 0 59  GLY HHH C   1 ? 11 
ATOM 9382  O O   . GLY H 5 59  ? 35.046  42.965  8.092  1.000 132.647 0 59  GLY HHH O   1 ? 11 
ATOM 9383  N N   . PHE H 5 60  ? 32.989  43.498  8.853  1.000 129.179 0 60  PHE HHH N   1 ? 11 
ATOM 9384  C CA  . PHE H 5 60  ? 33.252  43.110  10.233 1.000 129.174 0 60  PHE HHH CA  1 ? 11 
ATOM 9385  C C   . PHE H 5 60  ? 32.190  42.141  10.741 1.000 131.499 0 60  PHE HHH C   1 ? 11 
ATOM 9386  O O   . PHE H 5 60  ? 32.416  40.926  10.765 1.000 130.503 0 60  PHE HHH O   1 ? 11 
ATOM 9387  C CB  . PHE H 5 60  ? 33.317  44.351  11.129 1.000 131.085 0 60  PHE HHH CB  1 ? 11 
ATOM 9388  C CG  . PHE H 5 60  ? 33.721  44.061  12.548 1.000 134.903 0 60  PHE HHH CG  1 ? 11 
ATOM 9389  C CD1 . PHE H 5 60  ? 34.538  42.981  12.844 1.000 142.086 0 60  PHE HHH CD1 1 ? 11 
ATOM 9390  C CD2 . PHE H 5 60  ? 33.290  44.872  13.584 1.000 128.869 0 60  PHE HHH CD2 1 ? 11 
ATOM 9391  C CE1 . PHE H 5 60  ? 34.910  42.713  14.146 1.000 138.455 0 60  PHE HHH CE1 1 ? 11 
ATOM 9392  C CE2 . PHE H 5 60  ? 33.661  44.609  14.888 1.000 128.317 0 60  PHE HHH CE2 1 ? 11 
ATOM 9393  C CZ  . PHE H 5 60  ? 34.472  43.528  15.168 1.000 133.398 0 60  PHE HHH CZ  1 ? 11 
ATOM 9394  N N   . MET H 5 61  ? 31.029  42.664  11.136 1.000 132.408 0 61  MET HHH N   1 ? 11 
ATOM 9395  C CA  . MET H 5 61  ? 29.991  41.835  11.734 1.000 133.196 0 61  MET HHH CA  1 ? 11 
ATOM 9396  C C   . MET H 5 61  ? 28.666  42.586  11.751 1.000 130.315 0 61  MET HHH C   1 ? 11 
ATOM 9397  O O   . MET H 5 61  ? 28.610  43.805  11.571 1.000 124.924 0 61  MET HHH O   1 ? 11 
ATOM 9398  C CB  . MET H 5 61  ? 30.368  41.424  13.157 1.000 137.088 0 61  MET HHH CB  1 ? 11 
ATOM 9399  C CG  . MET H 5 61  ? 30.608  42.612  14.073 1.000 139.575 0 61  MET HHH CG  1 ? 11 
ATOM 9400  S SD  . MET H 5 61  ? 29.239  42.917  15.204 1.000 156.922 0 61  MET HHH SD  1 ? 11 
ATOM 9401  C CE  . MET H 5 61  ? 29.143  44.703  15.149 1.000 145.436 0 61  MET HHH CE  1 ? 11 
ATOM 9402  N N   . CYS H 5 62  ? 27.594  41.826  11.990 1.000 138.581 0 62  CYS HHH N   1 ? 11 
ATOM 9403  C CA  . CYS H 5 62  ? 26.256  42.355  12.230 1.000 137.755 0 62  CYS HHH CA  1 ? 11 
ATOM 9404  C C   . CYS H 5 62  ? 25.727  41.781  13.535 1.000 142.118 0 62  CYS HHH C   1 ? 11 
ATOM 9405  O O   . CYS H 5 62  ? 25.761  40.562  13.734 1.000 144.847 0 62  CYS HHH O   1 ? 11 
ATOM 9406  C CB  . CYS H 5 62  ? 25.300  42.003  11.087 1.000 134.396 0 62  CYS HHH CB  1 ? 11 
ATOM 9407  S SG  . CYS H 5 62  ? 25.913  42.393  9.440  1.000 140.367 0 62  CYS HHH SG  1 ? 11 
ATOM 9408  N N   . GLN H 5 63  ? 25.249  42.649  14.425 1.000 141.481 0 63  GLN HHH N   1 ? 11 
ATOM 9409  C CA  . GLN H 5 63  ? 24.817  42.228  15.750 1.000 138.554 0 63  GLN HHH CA  1 ? 11 
ATOM 9410  C C   . GLN H 5 63  ? 23.427  42.771  16.062 1.000 138.646 0 63  GLN HHH C   1 ? 11 
ATOM 9411  O O   . GLN H 5 63  ? 23.037  43.848  15.600 1.000 133.987 0 63  GLN HHH O   1 ? 11 
ATOM 9412  C CB  . GLN H 5 63  ? 25.829  42.628  16.835 1.000 141.849 0 63  GLN HHH CB  1 ? 11 
ATOM 9413  C CG  . GLN H 5 63  ? 25.591  43.952  17.516 1.000 146.011 0 63  GLN HHH CG  1 ? 11 
ATOM 9414  C CD  . GLN H 5 63  ? 26.427  44.089  18.775 1.000 150.705 0 63  GLN HHH CD  1 ? 11 
ATOM 9415  O OE1 . GLN H 5 63  ? 27.381  43.338  18.984 1.000 146.747 0 63  GLN HHH OE1 1 ? 11 
ATOM 9416  N NE2 . GLN H 5 63  ? 26.072  45.045  19.622 1.000 154.904 0 63  GLN HHH NE2 1 ? 11 
ATOM 9417  N N   . GLY H 5 64  ? 22.683  42.003  16.841 1.000 150.851 0 64  GLY HHH N   1 ? 11 
ATOM 9418  C CA  . GLY H 5 64  ? 21.322  42.342  17.185 1.000 160.580 0 64  GLY HHH CA  1 ? 11 
ATOM 9419  C C   . GLY H 5 64  ? 20.920  41.666  18.473 1.000 167.804 0 64  GLY HHH C   1 ? 11 
ATOM 9420  O O   . GLY H 5 64  ? 21.761  41.192  19.239 1.000 168.907 0 64  GLY HHH O   1 ? 11 
ATOM 9421  N N   . GLY H 5 65  ? 19.615  41.620  18.719 1.000 176.788 0 65  GLY HHH N   1 ? 11 
ATOM 9422  C CA  . GLY H 5 65  ? 19.131  40.908  19.879 1.000 181.810 0 65  GLY HHH CA  1 ? 11 
ATOM 9423  C C   . GLY H 5 65  ? 18.822  41.742  21.104 1.000 177.407 0 65  GLY HHH C   1 ? 11 
ATOM 9424  O O   . GLY H 5 65  ? 18.458  41.169  22.137 1.000 183.236 0 65  GLY HHH O   1 ? 11 
ATOM 9425  N N   . ASP H 5 66  ? 18.963  43.065  21.041 1.000 170.749 0 66  ASP HHH N   1 ? 11 
ATOM 9426  C CA  . ASP H 5 66  ? 18.634  43.905  22.200 1.000 179.291 0 66  ASP HHH CA  1 ? 11 
ATOM 9427  C C   . ASP H 5 66  ? 17.162  44.280  22.178 1.000 195.479 0 66  ASP HHH C   1 ? 11 
ATOM 9428  O O   . ASP H 5 66  ? 16.761  45.326  21.673 1.000 190.799 0 66  ASP HHH O   1 ? 11 
ATOM 9429  C CB  . ASP H 5 66  ? 19.506  45.151  22.247 1.000 180.487 0 66  ASP HHH CB  1 ? 11 
ATOM 9430  C CG  . ASP H 5 66  ? 19.182  46.064  23.440 1.000 188.847 0 66  ASP HHH CG  1 ? 11 
ATOM 9431  O OD1 . ASP H 5 66  ? 18.254  45.771  24.229 1.000 201.597 0 66  ASP HHH OD1 1 ? 11 
ATOM 9432  O OD2 . ASP H 5 66  ? 19.870  47.093  23.583 1.000 191.692 0 66  ASP HHH OD2 1 ? 11 
ATOM 9433  N N   . PHE H 5 67  ? 16.348  43.376  22.723 1.000 217.480 0 67  PHE HHH N   1 ? 11 
ATOM 9434  C CA  . PHE H 5 67  ? 14.898  43.493  22.737 1.000 218.500 0 67  PHE HHH CA  1 ? 11 
ATOM 9435  C C   . PHE H 5 67  ? 14.373  44.228  23.957 1.000 217.975 0 67  PHE HHH C   1 ? 11 
ATOM 9436  O O   . PHE H 5 67  ? 13.156  44.317  24.120 1.000 222.705 0 67  PHE HHH O   1 ? 11 
ATOM 9437  C CB  . PHE H 5 67  ? 14.229  42.116  22.599 1.000 219.535 0 67  PHE HHH CB  1 ? 11 
ATOM 9438  C CG  . PHE H 5 67  ? 14.734  41.065  23.540 1.000 228.587 0 67  PHE HHH CG  1 ? 11 
ATOM 9439  C CD1 . PHE H 5 67  ? 14.218  40.924  24.819 1.000 238.129 0 67  PHE HHH CD1 1 ? 11 
ATOM 9440  C CD2 . PHE H 5 67  ? 15.725  40.195  23.122 1.000 233.443 0 67  PHE HHH CD2 1 ? 11 
ATOM 9441  C CE1 . PHE H 5 67  ? 14.687  39.941  25.662 1.000 254.934 0 67  PHE HHH CE1 1 ? 11 
ATOM 9442  C CE2 . PHE H 5 67  ? 16.197  39.209  23.962 1.000 241.903 0 67  PHE HHH CE2 1 ? 11 
ATOM 9443  C CZ  . PHE H 5 67  ? 15.677  39.087  25.239 1.000 253.178 0 67  PHE HHH CZ  1 ? 11 
ATOM 9444  N N   . THR H 5 68  ? 15.239  44.755  24.834 1.000 213.241 0 68  THR HHH N   1 ? 11 
ATOM 9445  C CA  . THR H 5 68  ? 14.704  45.506  25.958 1.000 218.376 0 68  THR HHH CA  1 ? 11 
ATOM 9446  C C   . THR H 5 68  ? 14.901  47.001  25.806 1.000 215.495 0 68  THR HHH C   1 ? 11 
ATOM 9447  O O   . THR H 5 68  ? 14.081  47.772  26.322 1.000 225.886 0 68  THR HHH O   1 ? 11 
ATOM 9448  C CB  . THR H 5 68  ? 15.385  45.048  27.267 1.000 219.578 0 68  THR HHH CB  1 ? 11 
ATOM 9449  O OG1 . THR H 5 68  ? 15.625  43.635  27.234 1.000 222.659 0 68  THR HHH OG1 1 ? 11 
ATOM 9450  C CG2 . THR H 5 68  ? 14.547  45.408  28.496 1.000 222.793 0 68  THR HHH CG2 1 ? 11 
ATOM 9451  N N   . ARG H 5 69  ? 15.970  47.441  25.143 1.000 197.152 0 69  ARG HHH N   1 ? 11 
ATOM 9452  C CA  . ARG H 5 69  ? 16.200  48.863  24.964 1.000 192.775 0 69  ARG HHH CA  1 ? 11 
ATOM 9453  C C   . ARG H 5 69  ? 16.517  49.217  23.514 1.000 194.916 0 69  ARG HHH C   1 ? 11 
ATOM 9454  O O   . ARG H 5 69  ? 16.582  50.406  23.187 1.000 200.275 0 69  ARG HHH O   1 ? 11 
ATOM 9455  C CB  . ARG H 5 69  ? 17.257  49.425  25.924 1.000 193.791 0 69  ARG HHH CB  1 ? 11 
ATOM 9456  C CG  . ARG H 5 69  ? 16.829  49.275  27.393 1.000 207.761 0 69  ARG HHH CG  1 ? 11 
ATOM 9457  C CD  . ARG H 5 69  ? 17.691  50.085  28.371 1.000 210.158 0 69  ARG HHH CD  1 ? 11 
ATOM 9458  N NE  . ARG H 5 69  ? 17.470  51.508  28.128 1.000 218.903 0 69  ARG HHH NE  1 ? 11 
ATOM 9459  C CZ  . ARG H 5 69  ? 18.265  52.328  27.438 1.000 212.140 0 69  ARG HHH CZ  1 ? 11 
ATOM 9460  N NH1 . ARG H 5 69  ? 19.404  51.909  26.919 1.000 202.334 0 69  ARG HHH NH1 1 ? 11 
ATOM 9461  N NH2 . ARG H 5 69  ? 17.901  53.597  27.260 1.000 217.408 0 69  ARG HHH NH2 1 ? 11 
ATOM 9462  N N   . HIS H 5 70  ? 16.746  48.219  22.652 1.000 193.037 0 70  HIS HHH N   1 ? 11 
ATOM 9463  C CA  . HIS H 5 70  ? 16.842  48.386  21.206 1.000 186.009 0 70  HIS HHH CA  1 ? 11 
ATOM 9464  C C   . HIS H 5 70  ? 18.068  49.178  20.768 1.000 177.328 0 70  HIS HHH C   1 ? 11 
ATOM 9465  O O   . HIS H 5 70  ? 18.092  49.716  19.661 1.000 181.915 0 70  HIS HHH O   1 ? 11 
ATOM 9466  C CB  . HIS H 5 70  ? 15.564  49.001  20.629 1.000 189.179 0 70  HIS HHH CB  1 ? 11 
ATOM 9467  C CG  . HIS H 5 70  ? 14.509  47.986  20.322 1.000 194.625 0 70  HIS HHH CG  1 ? 11 
ATOM 9468  N ND1 . HIS H 5 70  ? 14.063  47.081  21.260 1.000 203.262 0 70  HIS HHH ND1 1 ? 11 
ATOM 9469  C CD2 . HIS H 5 70  ? 13.830  47.715  19.183 1.000 200.935 0 70  HIS HHH CD2 1 ? 11 
ATOM 9470  C CE1 . HIS H 5 70  ? 13.145  46.303  20.716 1.000 208.873 0 70  HIS HHH CE1 1 ? 11 
ATOM 9471  N NE2 . HIS H 5 70  ? 12.984  46.667  19.456 1.000 211.931 0 70  HIS HHH NE2 1 ? 11 
ATOM 9472  N N   . ASN H 5 71  ? 19.108  49.258  21.611 1.000 156.909 0 71  ASN HHH N   1 ? 11 
ATOM 9473  C CA  . ASN H 5 71  ? 20.253  50.108  21.312 1.000 147.086 0 71  ASN HHH CA  1 ? 11 
ATOM 9474  C C   . ASN H 5 71  ? 21.590  49.527  21.763 1.000 141.617 0 71  ASN HHH C   1 ? 11 
ATOM 9475  O O   . ASN H 5 71  ? 22.606  50.224  21.660 1.000 151.438 0 71  ASN HHH O   1 ? 11 
ATOM 9476  C CB  . ASN H 5 71  ? 20.093  51.502  21.939 1.000 158.260 0 71  ASN HHH CB  1 ? 11 
ATOM 9477  C CG  . ASN H 5 71  ? 20.051  51.469  23.466 1.000 172.571 0 71  ASN HHH CG  1 ? 11 
ATOM 9478  O OD1 . ASN H 5 71  ? 20.225  50.419  24.088 1.000 176.427 0 71  ASN HHH OD1 1 ? 11 
ATOM 9479  N ND2 . ASN H 5 71  ? 19.795  52.623  24.074 1.000 180.076 0 71  ASN HHH ND2 1 ? 11 
ATOM 9480  N N   . GLY H 5 72  ? 21.639  48.288  22.266 1.000 137.832 0 72  GLY HHH N   1 ? 11 
ATOM 9481  C CA  . GLY H 5 72  ? 22.886  47.701  22.710 1.000 139.579 0 72  GLY HHH CA  1 ? 11 
ATOM 9482  C C   . GLY H 5 72  ? 23.106  47.689  24.207 1.000 145.950 0 72  GLY HHH C   1 ? 11 
ATOM 9483  O O   . GLY H 5 72  ? 24.133  47.169  24.663 1.000 148.524 0 72  GLY HHH O   1 ? 11 
ATOM 9484  N N   . THR H 5 73  ? 22.172  48.239  24.976 1.000 153.323 0 73  THR HHH N   1 ? 11 
ATOM 9485  C CA  . THR H 5 73  ? 22.237  48.372  26.423 1.000 154.425 0 73  THR HHH CA  1 ? 11 
ATOM 9486  C C   . THR H 5 73  ? 21.359  47.336  27.113 1.000 159.517 0 73  THR HHH C   1 ? 11 
ATOM 9487  O O   . THR H 5 73  ? 21.452  47.148  28.331 1.000 171.453 0 73  THR HHH O   1 ? 11 
ATOM 9488  C CB  . THR H 5 73  ? 21.792  49.796  26.804 1.000 157.457 0 73  THR HHH CB  1 ? 11 
ATOM 9489  O OG1 . THR H 5 73  ? 22.773  50.748  26.377 1.000 154.529 0 73  THR HHH OG1 1 ? 11 
ATOM 9490  C CG2 . THR H 5 73  ? 21.528  49.958  28.288 1.000 175.743 0 73  THR HHH CG2 1 ? 11 
ATOM 9491  N N   . GLY H 5 74  ? 20.636  46.551  26.336 1.000 165.728 0 74  GLY HHH N   1 ? 11 
ATOM 9492  C CA  . GLY H 5 74  ? 19.679  45.602  26.855 1.000 172.339 0 74  GLY HHH CA  1 ? 11 
ATOM 9493  C C   . GLY H 5 74  ? 19.960  44.178  26.437 1.000 172.759 0 74  GLY HHH C   1 ? 11 
ATOM 9494  O O   . GLY H 5 74  ? 21.102  43.801  26.154 1.000 163.936 0 74  GLY HHH O   1 ? 11 
ATOM 9495  N N   . GLY H 5 75  ? 18.900  43.381  26.407 1.000 188.607 0 75  GLY HHH N   1 ? 11 
ATOM 9496  C CA  . GLY H 5 75  ? 18.934  41.955  26.174 1.000 199.245 0 75  GLY HHH CA  1 ? 11 
ATOM 9497  C C   . GLY H 5 75  ? 18.811  41.173  27.470 1.000 220.833 0 75  GLY HHH C   1 ? 11 
ATOM 9498  O O   . GLY H 5 75  ? 19.044  41.683  28.567 1.000 223.180 0 75  GLY HHH O   1 ? 11 
ATOM 9499  N N   . LYS H 5 76  ? 18.469  39.894  27.339 1.000 235.598 0 76  LYS HHH N   1 ? 11 
ATOM 9500  C CA  . LYS H 5 76  ? 18.443  39.057  28.527 1.000 244.634 0 76  LYS HHH CA  1 ? 11 
ATOM 9501  C C   . LYS H 5 76  ? 18.557  37.588  28.158 1.000 253.924 0 76  LYS HHH C   1 ? 11 
ATOM 9502  O O   . LYS H 5 76  ? 18.139  37.177  27.074 1.000 262.780 0 76  LYS HHH O   1 ? 11 
ATOM 9503  C CB  . LYS H 5 76  ? 17.107  39.322  29.215 1.000 247.404 0 76  LYS HHH CB  1 ? 11 
ATOM 9504  C CG  . LYS H 5 76  ? 16.726  38.443  30.350 1.000 257.775 0 76  LYS HHH CG  1 ? 11 
ATOM 9505  C CD  . LYS H 5 76  ? 15.383  38.874  30.892 1.000 253.367 0 76  LYS HHH CD  1 ? 11 
ATOM 9506  C CE  . LYS H 5 76  ? 14.385  38.982  29.753 1.000 245.254 0 76  LYS HHH CE  1 ? 11 
ATOM 9507  N NZ  . LYS H 5 76  ? 13.011  39.224  30.251 1.000 247.776 0 76  LYS HHH NZ  1 ? 11 
ATOM 9508  N N   . SER H 5 77  ? 19.130  36.807  29.072 1.000 265.636 0 77  SER HHH N   1 ? 11 
ATOM 9509  C CA  . SER H 5 77  ? 19.208  35.366  28.891 1.000 265.756 0 77  SER HHH CA  1 ? 11 
ATOM 9510  C C   . SER H 5 77  ? 17.948  34.740  29.470 1.000 280.335 0 77  SER HHH C   1 ? 11 
ATOM 9511  O O   . SER H 5 77  ? 17.155  35.399  30.145 1.000 311.943 0 77  SER HHH O   1 ? 11 
ATOM 9512  C CB  . SER H 5 77  ? 20.454  34.779  29.555 1.000 265.713 0 77  SER HHH CB  1 ? 11 
ATOM 9513  O OG  . SER H 5 77  ? 20.248  34.541  30.933 1.000 297.902 0 77  SER HHH OG  1 ? 11 
ATOM 9514  N N   . ILE H 5 78  ? 17.758  33.444  29.224 1.000 283.321 0 78  ILE HHH N   1 ? 11 
ATOM 9515  C CA  . ILE H 5 78  ? 16.616  32.812  29.872 1.000 285.338 0 78  ILE HHH CA  1 ? 11 
ATOM 9516  C C   . ILE H 5 78  ? 16.891  32.549  31.341 1.000 294.447 0 78  ILE HHH C   1 ? 11 
ATOM 9517  O O   . ILE H 5 78  ? 15.974  32.160  32.071 1.000 303.326 0 78  ILE HHH O   1 ? 11 
ATOM 9518  C CB  . ILE H 5 78  ? 16.222  31.537  29.110 1.000 260.288 0 78  ILE HHH CB  1 ? 11 
ATOM 9519  C CG1 . ILE H 5 78  ? 17.336  30.496  29.187 1.000 260.022 0 78  ILE HHH CG1 1 ? 11 
ATOM 9520  C CG2 . ILE H 5 78  ? 15.889  31.882  27.665 1.000 256.869 0 78  ILE HHH CG2 1 ? 11 
ATOM 9521  C CD1 . ILE H 5 78  ? 16.901  29.120  28.748 1.000 263.648 0 78  ILE HHH CD1 1 ? 11 
ATOM 9522  N N   . TYR H 5 79  ? 18.128  32.759  31.789 1.000 289.254 0 79  TYR HHH N   1 ? 11 
ATOM 9523  C CA  . TYR H 5 79  ? 18.533  32.545  33.179 1.000 290.654 0 79  TYR HHH CA  1 ? 11 
ATOM 9524  C C   . TYR H 5 79  ? 18.682  33.889  33.888 1.000 300.676 0 79  TYR HHH C   1 ? 11 
ATOM 9525  O O   . TYR H 5 79  ? 19.786  34.396  34.099 1.000 286.249 0 79  TYR HHH O   1 ? 11 
ATOM 9526  C CB  . TYR H 5 79  ? 19.803  31.710  33.251 1.000 288.886 0 79  TYR HHH CB  1 ? 11 
ATOM 9527  C CG  . TYR H 5 79  ? 19.764  30.430  32.449 1.000 294.985 0 79  TYR HHH CG  1 ? 11 
ATOM 9528  C CD1 . TYR H 5 79  ? 18.851  29.432  32.766 1.000 308.401 0 79  TYR HHH CD1 1 ? 11 
ATOM 9529  C CD2 . TYR H 5 79  ? 20.637  30.209  31.390 1.000 278.872 0 79  TYR HHH CD2 1 ? 11 
ATOM 9530  C CE1 . TYR H 5 79  ? 18.811  28.244  32.058 1.000 314.533 0 79  TYR HHH CE1 1 ? 11 
ATOM 9531  C CE2 . TYR H 5 79  ? 20.600  29.025  30.672 1.000 278.883 0 79  TYR HHH CE2 1 ? 11 
ATOM 9532  C CZ  . TYR H 5 79  ? 19.685  28.049  31.013 1.000 301.076 0 79  TYR HHH CZ  1 ? 11 
ATOM 9533  O OH  . TYR H 5 79  ? 19.647  26.875  30.301 1.000 301.581 0 79  TYR HHH OH  1 ? 11 
ATOM 9534  N N   . GLY H 5 80  ? 17.553  34.479  34.251 0.000 338.098 0 80  GLY HHH N   1 ? 11 
ATOM 9535  C CA  . GLY H 5 80  ? 17.585  35.827  34.780 0.000 316.633 0 80  GLY HHH CA  1 ? 11 
ATOM 9536  C C   . GLY H 5 80  ? 17.790  36.867  33.699 0.000 310.285 0 80  GLY HHH C   1 ? 11 
ATOM 9537  O O   . GLY H 5 80  ? 16.843  37.202  32.991 0.000 324.378 0 80  GLY HHH O   1 ? 11 
ATOM 9538  N N   . GLU H 5 81  ? 19.009  37.389  33.571 0.000 272.751 0 81  GLU HHH N   1 ? 11 
ATOM 9539  C CA  . GLU H 5 81  ? 19.427  38.446  32.645 0.000 296.438 0 81  GLU HHH CA  1 ? 11 
ATOM 9540  C C   . GLU H 5 81  ? 20.720  38.126  31.917 0.000 297.923 0 81  GLU HHH C   1 ? 11 
ATOM 9541  O O   . GLU H 5 81  ? 20.812  38.378  30.713 0.000 290.722 0 81  GLU HHH O   1 ? 11 
ATOM 9542  C CB  . GLU H 5 81  ? 19.534  39.833  33.293 1.000 242.998 0 81  GLU HHH CB  1 ? 11 
ATOM 9543  C CG  . GLU H 5 81  ? 18.194  40.349  33.782 1.000 249.511 0 81  GLU HHH CG  1 ? 11 
ATOM 9544  C CD  . GLU H 5 81  ? 18.243  41.775  34.277 1.000 250.737 0 81  GLU HHH CD  1 ? 11 
ATOM 9545  O OE1 . GLU H 5 81  ? 19.159  42.509  33.855 1.000 241.279 0 81  GLU HHH OE1 1 ? 11 
ATOM 9546  O OE2 . GLU H 5 81  ? 17.362  42.155  35.081 1.000 252.309 0 81  GLU HHH OE2 1 ? 11 
ATOM 9547  N N   . LYS H 5 82  ? 21.717  37.578  32.603 1.000 249.007 0 82  LYS HHH N   1 ? 11 
ATOM 9548  C CA  . LYS H 5 82  ? 23.000  37.317  31.975 1.000 232.384 0 82  LYS HHH CA  1 ? 11 
ATOM 9549  C C   . LYS H 5 82  ? 23.508  35.987  32.500 1.000 232.657 0 82  LYS HHH C   1 ? 11 
ATOM 9550  O O   . LYS H 5 82  ? 23.121  35.531  33.578 1.000 236.526 0 82  LYS HHH O   1 ? 11 
ATOM 9551  C CB  . LYS H 5 82  ? 24.017  38.427  32.283 1.000 222.821 0 82  LYS HHH CB  1 ? 11 
ATOM 9552  C CG  . LYS H 5 82  ? 23.862  39.687  31.451 1.000 220.706 0 82  LYS HHH CG  1 ? 11 
ATOM 9553  C CD  . LYS H 5 82  ? 25.019  40.641  31.700 1.000 212.305 0 82  LYS HHH CD  1 ? 11 
ATOM 9554  C CE  . LYS H 5 82  ? 24.888  41.911  30.877 1.000 205.103 0 82  LYS HHH CE  1 ? 11 
ATOM 9555  N NZ  . LYS H 5 82  ? 24.791  41.646  29.416 1.000 208.130 0 82  LYS HHH NZ  1 ? 11 
ATOM 9556  N N   . PHE H 5 83  ? 24.389  35.370  31.719 1.000 217.170 0 83  PHE HHH N   1 ? 11 
ATOM 9557  C CA  . PHE H 5 83  ? 25.097  34.174  32.137 1.000 220.672 0 83  PHE HHH CA  1 ? 11 
ATOM 9558  C C   . PHE H 5 83  ? 26.546  34.164  31.678 1.000 222.072 0 83  PHE HHH C   1 ? 11 
ATOM 9559  O O   . PHE H 5 83  ? 26.982  34.958  30.841 1.000 227.507 0 83  PHE HHH O   1 ? 11 
ATOM 9560  C CB  . PHE H 5 83  ? 24.393  32.918  31.601 1.000 228.626 0 83  PHE HHH CB  1 ? 11 
ATOM 9561  C CG  . PHE H 5 83  ? 24.465  32.772  30.099 1.000 227.662 0 83  PHE HHH CG  1 ? 11 
ATOM 9562  C CD1 . PHE H 5 83  ? 23.636  33.518  29.280 1.000 225.059 0 83  PHE HHH CD1 1 ? 11 
ATOM 9563  C CD2 . PHE H 5 83  ? 25.338  31.871  29.510 1.000 227.029 0 83  PHE HHH CD2 1 ? 11 
ATOM 9564  C CE1 . PHE H 5 83  ? 23.690  33.390  27.907 1.000 214.795 0 83  PHE HHH CE1 1 ? 11 
ATOM 9565  C CE2 . PHE H 5 83  ? 25.397  31.737  28.133 1.000 215.312 0 83  PHE HHH CE2 1 ? 11 
ATOM 9566  C CZ  . PHE H 5 83  ? 24.569  32.498  27.332 1.000 214.026 0 83  PHE HHH CZ  1 ? 11 
ATOM 9567  N N   . GLU H 5 84  ? 27.283  33.229  32.266 1.000 224.493 0 84  GLU HHH N   1 ? 11 
ATOM 9568  C CA  . GLU H 5 84  ? 28.722  33.099  32.140 1.000 227.438 0 84  GLU HHH CA  1 ? 11 
ATOM 9569  C C   . GLU H 5 84  ? 29.079  32.608  30.739 1.000 229.196 0 84  GLU HHH C   1 ? 11 
ATOM 9570  O O   . GLU H 5 84  ? 28.243  32.094  29.994 1.000 228.369 0 84  GLU HHH O   1 ? 11 
ATOM 9571  C CB  . GLU H 5 84  ? 29.310  32.189  33.215 1.000 233.956 0 84  GLU HHH CB  1 ? 11 
ATOM 9572  C CG  . GLU H 5 84  ? 29.268  32.816  34.599 1.000 238.318 0 84  GLU HHH CG  1 ? 11 
ATOM 9573  C CD  . GLU H 5 84  ? 30.412  32.355  35.487 1.000 247.569 0 84  GLU HHH CD  1 ? 11 
ATOM 9574  O OE1 . GLU H 5 84  ? 31.399  31.810  34.948 1.000 259.253 0 84  GLU HHH OE1 1 ? 11 
ATOM 9575  O OE2 . GLU H 5 84  ? 30.338  32.559  36.718 1.000 242.944 0 84  GLU HHH OE2 1 ? 11 
ATOM 9576  N N   . ASP H 5 85  ? 30.349  32.772  30.389 1.000 225.768 0 85  ASP HHH N   1 ? 11 
ATOM 9577  C CA  . ASP H 5 85  ? 30.880  32.164  29.177 1.000 233.170 0 85  ASP HHH CA  1 ? 11 
ATOM 9578  C C   . ASP H 5 85  ? 30.940  30.649  29.302 1.000 243.817 0 85  ASP HHH C   1 ? 11 
ATOM 9579  O O   . ASP H 5 85  ? 31.666  30.104  30.139 1.000 245.643 0 85  ASP HHH O   1 ? 11 
ATOM 9580  C CB  . ASP H 5 85  ? 32.287  32.697  28.893 1.000 232.306 0 85  ASP HHH CB  1 ? 11 
ATOM 9581  C CG  . ASP H 5 85  ? 32.315  34.195  28.639 1.000 223.478 0 85  ASP HHH CG  1 ? 11 
ATOM 9582  O OD1 . ASP H 5 85  ? 31.455  34.691  27.886 1.000 222.225 0 85  ASP HHH OD1 1 ? 11 
ATOM 9583  O OD2 . ASP H 5 85  ? 33.197  34.884  29.197 1.000 216.055 0 85  ASP HHH OD2 1 ? 11 
ATOM 9584  N N   . GLU H 5 86  ? 30.145  29.979  28.458 1.000 248.413 0 86  GLU HHH N   1 ? 11 
ATOM 9585  C CA  . GLU H 5 86  ? 29.927  28.542  28.572 1.000 257.860 0 86  GLU HHH CA  1 ? 11 
ATOM 9586  C C   . GLU H 5 86  ? 31.212  27.823  28.192 1.000 260.130 0 86  GLU HHH C   1 ? 11 
ATOM 9587  O O   . GLU H 5 86  ? 31.704  26.982  28.954 1.000 272.139 0 86  GLU HHH O   1 ? 11 
ATOM 9588  C CB  . GLU H 5 86  ? 28.737  28.088  27.723 1.000 258.291 0 86  GLU HHH CB  1 ? 11 
ATOM 9589  C CG  . GLU H 5 86  ? 28.393  26.606  27.926 1.000 263.499 0 86  GLU HHH CG  1 ? 11 
ATOM 9590  C CD  . GLU H 5 86  ? 27.075  26.186  27.296 1.000 267.759 0 86  GLU HHH CD  1 ? 11 
ATOM 9591  O OE1 . GLU H 5 86  ? 26.485  26.985  26.543 1.000 270.483 0 86  GLU HHH OE1 1 ? 11 
ATOM 9592  O OE2 . GLU H 5 86  ? 26.615  25.058  27.579 1.000 266.864 0 86  GLU HHH OE2 1 ? 11 
ATOM 9593  N N   . ASN H 5 87  ? 31.803  28.192  27.055 1.000 251.528 0 87  ASN HHH N   1 ? 11 
ATOM 9594  C CA  . ASN H 5 87  ? 33.106  27.673  26.659 1.000 253.891 0 87  ASN HHH CA  1 ? 11 
ATOM 9595  C C   . ASN H 5 87  ? 33.632  28.549  25.533 1.000 250.228 0 87  ASN HHH C   1 ? 11 
ATOM 9596  O O   . ASN H 5 87  ? 32.900  29.347  24.942 1.000 253.609 0 87  ASN HHH O   1 ? 11 
ATOM 9597  C CB  . ASN H 5 87  ? 33.016  26.243  26.096 1.000 261.987 0 87  ASN HHH CB  1 ? 11 
ATOM 9598  C CG  . ASN H 5 87  ? 32.621  25.206  27.115 1.000 278.280 0 87  ASN HHH CG  1 ? 11 
ATOM 9599  O OD1 . ASN H 5 87  ? 33.356  24.924  28.058 1.000 300.734 0 87  ASN HHH OD1 1 ? 11 
ATOM 9600  N ND2 . ASN H 5 87  ? 31.440  24.624  26.926 1.000 280.065 0 87  ASN HHH ND2 1 ? 11 
ATOM 9601  N N   . PHE H 5 88  ? 34.924  28.354  25.226 1.000 239.238 0 88  PHE HHH N   1 ? 11 
ATOM 9602  C CA  . PHE H 5 88  ? 35.658  29.004  24.143 1.000 231.473 0 88  PHE HHH CA  1 ? 11 
ATOM 9603  C C   . PHE H 5 88  ? 36.317  27.979  23.230 1.000 229.966 0 88  PHE HHH C   1 ? 11 
ATOM 9604  O O   . PHE H 5 88  ? 37.331  28.289  22.596 1.000 229.001 0 88  PHE HHH O   1 ? 11 
ATOM 9605  C CB  . PHE H 5 88  ? 36.726  29.988  24.650 1.000 228.370 0 88  PHE HHH CB  1 ? 11 
ATOM 9606  C CG  . PHE H 5 88  ? 36.185  31.206  25.375 1.000 227.957 0 88  PHE HHH CG  1 ? 11 
ATOM 9607  C CD1 . PHE H 5 88  ? 34.832  31.483  25.423 1.000 232.202 0 88  PHE HHH CD1 1 ? 11 
ATOM 9608  C CD2 . PHE H 5 88  ? 37.058  32.098  25.983 1.000 226.984 0 88  PHE HHH CD2 1 ? 11 
ATOM 9609  C CE1 . PHE H 5 88  ? 34.355  32.604  26.077 1.000 237.037 0 88  PHE HHH CE1 1 ? 11 
ATOM 9610  C CE2 . PHE H 5 88  ? 36.582  33.222  26.639 1.000 236.864 0 88  PHE HHH CE2 1 ? 11 
ATOM 9611  C CZ  . PHE H 5 88  ? 35.229  33.475  26.682 1.000 240.499 0 88  PHE HHH CZ  1 ? 11 
ATOM 9612  N N   . ILE H 5 89  ? 35.806  26.748  23.197 1.000 241.181 0 89  ILE HHH N   1 ? 11 
ATOM 9613  C CA  . ILE H 5 89  ? 36.446  25.703  22.401 1.000 252.797 0 89  ILE HHH CA  1 ? 11 
ATOM 9614  C C   . ILE H 5 89  ? 36.509  26.113  20.937 1.000 256.180 0 89  ILE HHH C   1 ? 11 
ATOM 9615  O O   . ILE H 5 89  ? 37.557  26.010  20.289 1.000 260.637 0 89  ILE HHH O   1 ? 11 
ATOM 9616  C CB  . ILE H 5 89  ? 35.707  24.366  22.578 1.000 256.144 0 89  ILE HHH CB  1 ? 11 
ATOM 9617  C CG1 . ILE H 5 89  ? 35.295  24.184  24.041 1.000 256.097 0 89  ILE HHH CG1 1 ? 11 
ATOM 9618  C CG2 . ILE H 5 89  ? 36.575  23.213  22.112 1.000 251.820 0 89  ILE HHH CG2 1 ? 11 
ATOM 9619  C CD1 . ILE H 5 89  ? 34.447  22.967  24.287 1.000 254.959 0 89  ILE HHH CD1 1 ? 11 
ATOM 9620  N N   . LEU H 5 90  ? 35.395  26.595  20.399 1.000 266.399 0 90  LEU HHH N   1 ? 11 
ATOM 9621  C CA  . LEU H 5 90  ? 35.340  26.968  18.993 1.000 264.030 0 90  LEU HHH CA  1 ? 11 
ATOM 9622  C C   . LEU H 5 90  ? 36.058  28.291  18.740 1.000 266.755 0 90  LEU HHH C   1 ? 11 
ATOM 9623  O O   . LEU H 5 90  ? 36.135  29.160  19.614 1.000 280.771 0 90  LEU HHH O   1 ? 11 
ATOM 9624  C CB  . LEU H 5 90  ? 33.891  27.054  18.520 1.000 251.354 0 90  LEU HHH CB  1 ? 11 
ATOM 9625  C CG  . LEU H 5 90  ? 33.117  25.737  18.585 1.000 249.202 0 90  LEU HHH CG  1 ? 11 
ATOM 9626  C CD1 . LEU H 5 90  ? 31.748  25.896  17.951 1.000 239.263 0 90  LEU HHH CD1 1 ? 11 
ATOM 9627  C CD2 . LEU H 5 90  ? 33.900  24.616  17.916 1.000 253.422 0 90  LEU HHH CD2 1 ? 11 
ATOM 9628  N N   . LYS H 5 91  ? 36.582  28.434  17.524 1.000 249.759 0 91  LYS HHH N   1 ? 11 
ATOM 9629  C CA  . LYS H 5 91  ? 37.350  29.603  17.120 1.000 242.978 0 91  LYS HHH CA  1 ? 11 
ATOM 9630  C C   . LYS H 5 91  ? 36.672  30.288  15.937 1.000 241.139 0 91  LYS HHH C   1 ? 11 
ATOM 9631  O O   . LYS H 5 91  ? 35.982  29.648  15.138 1.000 244.152 0 91  LYS HHH O   1 ? 11 
ATOM 9632  C CB  . LYS H 5 91  ? 38.797  29.224  16.760 1.000 238.621 0 91  LYS HHH CB  1 ? 11 
ATOM 9633  C CG  . LYS H 5 91  ? 39.851  30.086  17.447 1.000 233.949 0 91  LYS HHH CG  1 ? 11 
ATOM 9634  C CD  . LYS H 5 91  ? 41.265  29.629  17.115 1.000 231.190 0 91  LYS HHH CD  1 ? 11 
ATOM 9635  C CE  . LYS H 5 91  ? 42.303  30.425  17.896 1.000 227.817 0 91  LYS HHH CE  1 ? 11 
ATOM 9636  N NZ  . LYS H 5 91  ? 43.687  30.140  17.439 1.000 226.105 0 91  LYS HHH NZ  1 ? 11 
ATOM 9637  N N   . HIS H 5 92  ? 36.880  31.601  15.835 1.000 235.776 0 92  HIS HHH N   1 ? 11 
ATOM 9638  C CA  . HIS H 5 92  ? 36.337  32.426  14.759 1.000 224.000 0 92  HIS HHH CA  1 ? 11 
ATOM 9639  C C   . HIS H 5 92  ? 37.090  32.202  13.453 1.000 222.662 0 92  HIS HHH C   1 ? 11 
ATOM 9640  O O   . HIS H 5 92  ? 38.058  32.910  13.155 1.000 216.814 0 92  HIS HHH O   1 ? 11 
ATOM 9641  C CB  . HIS H 5 92  ? 36.367  33.905  15.156 1.000 212.067 0 92  HIS HHH CB  1 ? 11 
ATOM 9642  C CG  . HIS H 5 92  ? 35.531  34.221  16.358 1.000 205.117 0 92  HIS HHH CG  1 ? 11 
ATOM 9643  N ND1 . HIS H 5 92  ? 35.985  34.040  17.647 1.000 205.620 0 92  HIS HHH ND1 1 ? 11 
ATOM 9644  C CD2 . HIS H 5 92  ? 34.267  34.693  16.468 1.000 193.957 0 92  HIS HHH CD2 1 ? 11 
ATOM 9645  C CE1 . HIS H 5 92  ? 35.040  34.395  18.499 1.000 195.093 0 92  HIS HHH CE1 1 ? 11 
ATOM 9646  N NE2 . HIS H 5 92  ? 33.986  34.794  17.809 1.000 186.993 0 92  HIS HHH NE2 1 ? 11 
ATOM 9647  N N   . THR H 5 93  ? 36.655  31.214  12.669 1.000 225.243 0 93  THR HHH N   1 ? 11 
ATOM 9648  C CA  . THR H 5 93  ? 37.420  30.711  11.535 1.000 226.455 0 93  THR HHH CA  1 ? 11 
ATOM 9649  C C   . THR H 5 93  ? 37.079  31.377  10.206 1.000 213.951 0 93  THR HHH C   1 ? 11 
ATOM 9650  O O   . THR H 5 93  ? 37.784  31.133  9.221  1.000 216.219 0 93  THR HHH O   1 ? 11 
ATOM 9651  C CB  . THR H 5 93  ? 37.203  29.199  11.386 1.000 237.201 0 93  THR HHH CB  1 ? 11 
ATOM 9652  O OG1 . THR H 5 93  ? 35.798  28.913  11.378 1.000 245.970 0 93  THR HHH OG1 1 ? 11 
ATOM 9653  C CG2 . THR H 5 93  ? 37.855  28.455  12.542 1.000 237.360 0 93  THR HHH CG2 1 ? 11 
ATOM 9654  N N   . GLY H 5 94  ? 36.030  32.194  10.137 1.000 203.784 0 94  GLY HHH N   1 ? 11 
ATOM 9655  C CA  . GLY H 5 94  ? 35.647  32.797  8.879  1.000 193.850 0 94  GLY HHH CA  1 ? 11 
ATOM 9656  C C   . GLY H 5 94  ? 34.243  33.367  8.875  1.000 189.402 0 94  GLY HHH C   1 ? 11 
ATOM 9657  O O   . GLY H 5 94  ? 33.585  33.472  9.916  1.000 191.323 0 94  GLY HHH O   1 ? 11 
ATOM 9658  N N   . PRO H 5 95  ? 33.770  33.775  7.695  1.000 187.179 0 95  PRO HHH N   1 ? 11 
ATOM 9659  C CA  . PRO H 5 95  ? 32.396  34.282  7.583  1.000 178.044 0 95  PRO HHH CA  1 ? 11 
ATOM 9660  C C   . PRO H 5 95  ? 31.389  33.232  8.023  1.000 177.021 0 95  PRO HHH C   1 ? 11 
ATOM 9661  O O   . PRO H 5 95  ? 31.561  32.035  7.781  1.000 176.772 0 95  PRO HHH O   1 ? 11 
ATOM 9662  C CB  . PRO H 5 95  ? 32.254  34.613  6.092  1.000 174.880 0 95  PRO HHH CB  1 ? 11 
ATOM 9663  C CG  . PRO H 5 95  ? 33.654  34.704  5.570  1.000 184.845 0 95  PRO HHH CG  1 ? 11 
ATOM 9664  C CD  . PRO H 5 95  ? 34.481  33.783  6.406  1.000 191.116 0 95  PRO HHH CD  1 ? 11 
ATOM 9665  N N   . GLY H 5 96  ? 30.327  33.692  8.678  1.000 187.857 0 96  GLY HHH N   1 ? 11 
ATOM 9666  C CA  . GLY H 5 96  ? 29.227  32.838  9.058  1.000 193.130 0 96  GLY HHH CA  1 ? 11 
ATOM 9667  C C   . GLY H 5 96  ? 29.293  32.372  10.494 1.000 194.920 0 96  GLY HHH C   1 ? 11 
ATOM 9668  O O   . GLY H 5 96  ? 28.302  31.833  11.002 1.000 198.952 0 96  GLY HHH O   1 ? 11 
ATOM 9669  N N   . ILE H 5 97  ? 30.437  32.564  11.157 1.000 189.652 0 97  ILE HHH N   1 ? 11 
ATOM 9670  C CA  . ILE H 5 97  ? 30.558  32.213  12.565 1.000 191.462 0 97  ILE HHH CA  1 ? 11 
ATOM 9671  C C   . ILE H 5 97  ? 29.572  33.039  13.371 1.000 192.546 0 97  ILE HHH C   1 ? 11 
ATOM 9672  O O   . ILE H 5 97  ? 29.486  34.264  13.215 1.000 177.302 0 97  ILE HHH O   1 ? 11 
ATOM 9673  C CB  . ILE H 5 97  ? 32.000  32.434  13.050 1.000 189.978 0 97  ILE HHH CB  1 ? 11 
ATOM 9674  C CG1 . ILE H 5 97  ? 32.936  31.382  12.459 1.000 196.714 0 97  ILE HHH CG1 1 ? 11 
ATOM 9675  C CG2 . ILE H 5 97  ? 32.071  32.426  14.572 1.000 196.461 0 97  ILE HHH CG2 1 ? 11 
ATOM 9676  C CD1 . ILE H 5 97  ? 32.536  29.965  12.792 1.000 208.082 0 97  ILE HHH CD1 1 ? 11 
ATOM 9677  N N   . LEU H 5 98  ? 28.821  32.369  14.237 1.000 206.937 0 98  LEU HHH N   1 ? 11 
ATOM 9678  C CA  . LEU H 5 98  ? 27.855  33.014  15.114 1.000 204.312 0 98  LEU HHH CA  1 ? 11 
ATOM 9679  C C   . LEU H 5 98  ? 28.376  32.932  16.539 1.000 196.280 0 98  LEU HHH C   1 ? 11 
ATOM 9680  O O   . LEU H 5 98  ? 28.659  31.838  17.039 1.000 205.473 0 98  LEU HHH O   1 ? 11 
ATOM 9681  C CB  . LEU H 5 98  ? 26.480  32.355  15.008 1.000 210.935 0 98  LEU HHH CB  1 ? 11 
ATOM 9682  C CG  . LEU H 5 98  ? 25.328  33.207  15.543 1.000 210.734 0 98  LEU HHH CG  1 ? 11 
ATOM 9683  C CD1 . LEU H 5 98  ? 25.451  34.645  15.064 1.000 196.863 0 98  LEU HHH CD1 1 ? 11 
ATOM 9684  C CD2 . LEU H 5 98  ? 23.968  32.622  15.180 1.000 226.901 0 98  LEU HHH CD2 1 ? 11 
ATOM 9685  N N   . SER H 5 99  ? 28.504  34.084  17.187 1.000 188.841 0 99  SER HHH N   1 ? 11 
ATOM 9686  C CA  . SER H 5 99  ? 29.063  34.147  18.525 1.000 195.129 0 99  SER HHH CA  1 ? 11 
ATOM 9687  C C   . SER H 5 99  ? 28.321  35.207  19.323 1.000 195.496 0 99  SER HHH C   1 ? 11 
ATOM 9688  O O   . SER H 5 99  ? 27.788  36.170  18.765 1.000 185.881 0 99  SER HHH O   1 ? 11 
ATOM 9689  C CB  . SER H 5 99  ? 30.571  34.440  18.489 1.000 193.274 0 99  SER HHH CB  1 ? 11 
ATOM 9690  O OG  . SER H 5 99  ? 31.052  34.843  19.759 1.000 207.596 0 99  SER HHH OG  1 ? 11 
ATOM 9691  N N   . MET H 5 100 ? 28.292  35.023  20.639 1.000 197.981 0 100 MET HHH N   1 ? 11 
ATOM 9692  C CA  . MET H 5 100 ? 27.594  35.959  21.507 1.000 188.746 0 100 MET HHH CA  1 ? 11 
ATOM 9693  C C   . MET H 5 100 ? 28.414  37.219  21.748 1.000 183.224 0 100 MET HHH C   1 ? 11 
ATOM 9694  O O   . MET H 5 100 ? 29.642  37.181  21.819 1.000 182.463 0 100 MET HHH O   1 ? 11 
ATOM 9695  C CB  . MET H 5 100 ? 27.275  35.310  22.849 1.000 189.617 0 100 MET HHH CB  1 ? 11 
ATOM 9696  C CG  . MET H 5 100 ? 26.321  34.159  22.755 1.000 193.972 0 100 MET HHH CG  1 ? 11 
ATOM 9697  S SD  . MET H 5 100 ? 24.621  34.752  22.786 1.000 196.527 0 100 MET HHH SD  1 ? 11 
ATOM 9698  C CE  . MET H 5 100 ? 24.663  35.907  24.155 1.000 192.684 0 100 MET HHH CE  1 ? 11 
ATOM 9699  N N   . ALA H 5 101 ? 27.717  38.343  21.876 1.000 181.021 0 101 ALA HHH N   1 ? 11 
ATOM 9700  C CA  . ALA H 5 101 ? 28.347  39.574  22.320 1.000 182.069 0 101 ALA HHH CA  1 ? 11 
ATOM 9701  C C   . ALA H 5 101 ? 28.436  39.547  23.834 1.000 193.346 0 101 ALA HHH C   1 ? 11 
ATOM 9702  O O   . ALA H 5 101 ? 27.668  38.852  24.511 1.000 206.597 0 101 ALA HHH O   1 ? 11 
ATOM 9703  C CB  . ALA H 5 101 ? 27.594  40.822  21.852 1.000 172.293 0 101 ALA HHH CB  1 ? 11 
ATOM 9704  N N   . ASN H 5 102 ? 29.419  40.268  24.360 1.000 198.948 0 102 ASN HHH N   1 ? 11 
ATOM 9705  C CA  . ASN H 5 102 ? 29.553  40.373  25.803 1.000 203.635 0 102 ASN HHH CA  1 ? 11 
ATOM 9706  C C   . ASN H 5 102 ? 30.329  41.628  26.161 1.000 200.849 0 102 ASN HHH C   1 ? 11 
ATOM 9707  O O   . ASN H 5 102 ? 31.401  41.879  25.603 1.000 203.035 0 102 ASN HHH O   1 ? 11 
ATOM 9708  C CB  . ASN H 5 102 ? 30.274  39.149  26.374 1.000 217.387 0 102 ASN HHH CB  1 ? 11 
ATOM 9709  C CG  . ASN H 5 102 ? 31.476  38.714  25.527 1.000 221.648 0 102 ASN HHH CG  1 ? 11 
ATOM 9710  O OD1 . ASN H 5 102 ? 31.345  38.362  24.353 1.000 229.350 0 102 ASN HHH OD1 1 ? 11 
ATOM 9711  N ND2 . ASN H 5 102 ? 32.646  38.697  26.146 1.000 217.685 0 102 ASN HHH ND2 1 ? 11 
ATOM 9712  N N   . ALA H 5 103 ? 29.769  42.413  27.090 1.000 199.740 0 103 ALA HHH N   1 ? 11 
ATOM 9713  C CA  . ALA H 5 103 ? 30.385  43.671  27.499 1.000 204.174 0 103 ALA HHH CA  1 ? 11 
ATOM 9714  C C   . ALA H 5 103 ? 31.722  43.403  28.170 1.000 204.419 0 103 ALA HHH C   1 ? 11 
ATOM 9715  O O   . ALA H 5 103 ? 32.602  44.270  28.193 1.000 200.474 0 103 ALA HHH O   1 ? 11 
ATOM 9716  C CB  . ALA H 5 103 ? 29.453  44.431  28.442 1.000 199.251 0 103 ALA HHH CB  1 ? 11 
ATOM 9717  N N   . GLY H 5 104 ? 31.879  42.201  28.713 1.000 213.521 0 104 GLY HHH N   1 ? 11 
ATOM 9718  C CA  . GLY H 5 104 ? 33.022  41.807  29.496 1.000 209.542 0 104 GLY HHH CA  1 ? 11 
ATOM 9719  C C   . GLY H 5 104 ? 32.995  40.303  29.669 1.000 214.204 0 104 GLY HHH C   1 ? 11 
ATOM 9720  O O   . GLY H 5 104 ? 32.048  39.636  29.238 1.000 218.156 0 104 GLY HHH O   1 ? 11 
ATOM 9721  N N   . PRO H 5 105 ? 34.040  39.731  30.268 1.000 191.263 0 105 PRO HHH N   1 ? 11 
ATOM 9722  C CA  . PRO H 5 105 ? 34.013  38.293  30.565 1.000 196.463 0 105 PRO HHH CA  1 ? 11 
ATOM 9723  C C   . PRO H 5 105 ? 32.769  37.932  31.366 1.000 201.781 0 105 PRO HHH C   1 ? 11 
ATOM 9724  O O   . PRO H 5 105 ? 32.410  38.603  32.342 1.000 208.947 0 105 PRO HHH O   1 ? 11 
ATOM 9725  C CB  . PRO H 5 105 ? 35.309  38.047  31.346 1.000 195.543 0 105 PRO HHH CB  1 ? 11 
ATOM 9726  C CG  . PRO H 5 105 ? 36.073  39.318  31.322 1.000 190.627 0 105 PRO HHH CG  1 ? 11 
ATOM 9727  C CD  . PRO H 5 105 ? 35.201  40.422  30.851 1.000 184.852 0 105 PRO HHH CD  1 ? 11 
ATOM 9728  N N   . ASN H 5 106 ? 32.115  36.854  30.943 1.000 203.970 0 106 ASN HHH N   1 ? 11 
ATOM 9729  C CA  . ASN H 5 106 ? 30.965  36.265  31.625 1.000 209.533 0 106 ASN HHH CA  1 ? 11 
ATOM 9730  C C   . ASN H 5 106 ? 29.820  37.270  31.781 1.000 205.600 0 106 ASN HHH C   1 ? 11 
ATOM 9731  O O   . ASN H 5 106 ? 29.212  37.404  32.844 1.000 204.246 0 106 ASN HHH O   1 ? 11 
ATOM 9732  C CB  . ASN H 5 106 ? 31.378  35.703  32.986 1.000 213.924 0 106 ASN HHH CB  1 ? 11 
ATOM 9733  C CG  . ASN H 5 106 ? 32.544  34.744  32.892 1.000 224.055 0 106 ASN HHH CG  1 ? 11 
ATOM 9734  O OD1 . ASN H 5 106 ? 32.507  33.768  32.142 1.000 237.229 0 106 ASN HHH OD1 1 ? 11 
ATOM 9735  N ND2 . ASN H 5 106 ? 33.600  35.030  33.644 1.000 219.633 0 106 ASN HHH ND2 1 ? 11 
ATOM 9736  N N   . THR H 5 107 ? 29.522  37.981  30.691 1.000 212.479 0 107 THR HHH N   1 ? 11 
ATOM 9737  C CA  . THR H 5 107 ? 28.448  38.966  30.636 1.000 213.425 0 107 THR HHH CA  1 ? 11 
ATOM 9738  C C   . THR H 5 107 ? 27.602  38.725  29.391 1.000 209.150 0 107 THR HHH C   1 ? 11 
ATOM 9739  O O   . THR H 5 107 ? 27.086  39.669  28.790 1.000 208.147 0 107 THR HHH O   1 ? 11 
ATOM 9740  C CB  . THR H 5 107 ? 28.988  40.396  30.657 1.000 216.994 0 107 THR HHH CB  1 ? 11 
ATOM 9741  O OG1 . THR H 5 107 ? 29.839  40.614  29.521 1.000 222.491 0 107 THR HHH OG1 1 ? 11 
ATOM 9742  C CG2 . THR H 5 107 ? 29.754  40.656  31.941 1.000 221.458 0 107 THR HHH CG2 1 ? 11 
ATOM 9743  N N   . ASN H 5 108 ? 27.467  37.457  29.002 1.000 207.640 0 108 ASN HHH N   1 ? 11 
ATOM 9744  C CA  . ASN H 5 108 ? 26.624  37.080  27.879 1.000 202.204 0 108 ASN HHH CA  1 ? 11 
ATOM 9745  C C   . ASN H 5 108 ? 25.153  37.304  28.179 1.000 204.949 0 108 ASN HHH C   1 ? 11 
ATOM 9746  O O   . ASN H 5 108 ? 24.678  37.010  29.274 1.000 217.639 0 108 ASN HHH O   1 ? 11 
ATOM 9747  C CB  . ASN H 5 108 ? 26.860  35.602  27.534 1.000 205.142 0 108 ASN HHH CB  1 ? 11 
ATOM 9748  C CG  . ASN H 5 108 ? 28.315  35.302  27.218 1.000 204.918 0 108 ASN HHH CG  1 ? 11 
ATOM 9749  O OD1 . ASN H 5 108 ? 28.817  35.708  26.168 1.000 204.506 0 108 ASN HHH OD1 1 ? 11 
ATOM 9750  N ND2 . ASN H 5 108 ? 29.017  34.637  28.142 1.000 211.221 0 108 ASN HHH ND2 1 ? 11 
ATOM 9751  N N   . GLY H 5 109 ? 24.435  37.839  27.195 1.000 190.059 0 109 GLY HHH N   1 ? 11 
ATOM 9752  C CA  . GLY H 5 109 ? 23.007  37.995  27.390 1.000 202.971 0 109 GLY HHH CA  1 ? 11 
ATOM 9753  C C   . GLY H 5 109 ? 22.203  37.402  26.252 1.000 209.125 0 109 GLY HHH C   1 ? 11 
ATOM 9754  O O   . GLY H 5 109 ? 22.136  36.178  26.106 1.000 216.824 0 109 GLY HHH O   1 ? 11 
ATOM 9755  N N   . SER H 5 110 ? 21.574  38.251  25.441 1.000 205.718 0 110 SER HHH N   1 ? 11 
ATOM 9756  C CA  . SER H 5 110 ? 20.825  37.809  24.271 1.000 205.076 0 110 SER HHH CA  1 ? 11 
ATOM 9757  C C   . SER H 5 110 ? 21.334  38.465  22.994 1.000 190.804 0 110 SER HHH C   1 ? 11 
ATOM 9758  O O   . SER H 5 110 ? 20.585  38.613  22.027 1.000 189.007 0 110 SER HHH O   1 ? 11 
ATOM 9759  C CB  . SER H 5 110 ? 19.337  38.081  24.444 1.000 223.416 0 110 SER HHH CB  1 ? 11 
ATOM 9760  O OG  . SER H 5 110 ? 19.114  39.456  24.650 1.000 230.317 0 110 SER HHH OG  1 ? 11 
ATOM 9761  N N   . GLN H 5 111 ? 22.594  38.874  22.970 1.000 183.386 0 111 GLN HHH N   1 ? 11 
ATOM 9762  C CA  . GLN H 5 111 ? 23.129  39.557  21.806 1.000 172.968 0 111 GLN HHH CA  1 ? 11 
ATOM 9763  C C   . GLN H 5 111 ? 24.197  38.707  21.137 1.000 171.421 0 111 GLN HHH C   1 ? 11 
ATOM 9764  O O   . GLN H 5 111 ? 25.069  38.138  21.799 1.000 171.958 0 111 GLN HHH O   1 ? 11 
ATOM 9765  C CB  . GLN H 5 111 ? 23.685  40.935  22.190 1.000 171.424 0 111 GLN HHH CB  1 ? 11 
ATOM 9766  C CG  . GLN H 5 111 ? 22.603  41.916  22.654 1.000 173.451 0 111 GLN HHH CG  1 ? 11 
ATOM 9767  C CD  . GLN H 5 111 ? 23.138  43.310  22.927 1.000 161.690 0 111 GLN HHH CD  1 ? 11 
ATOM 9768  O OE1 . GLN H 5 111 ? 22.387  44.220  23.279 1.000 162.323 0 111 GLN HHH OE1 1 ? 11 
ATOM 9769  N NE2 . GLN H 5 111 ? 24.441  43.486  22.754 1.000 150.434 0 111 GLN HHH NE2 1 ? 11 
ATOM 9770  N N   . PHE H 5 112 ? 24.101  38.632  19.815 1.000 172.028 0 112 PHE HHH N   1 ? 11 
ATOM 9771  C CA  . PHE H 5 112 ? 24.930  37.784  18.976 1.000 165.768 0 112 PHE HHH CA  1 ? 11 
ATOM 9772  C C   . PHE H 5 112 ? 25.471  38.634  17.840 1.000 157.477 0 112 PHE HHH C   1 ? 11 
ATOM 9773  O O   . PHE H 5 112 ? 24.855  39.630  17.454 1.000 148.381 0 112 PHE HHH O   1 ? 11 
ATOM 9774  C CB  . PHE H 5 112 ? 24.133  36.611  18.398 1.000 169.831 0 112 PHE HHH CB  1 ? 11 
ATOM 9775  C CG  . PHE H 5 112 ? 22.911  37.037  17.629 1.000 174.365 0 112 PHE HHH CG  1 ? 11 
ATOM 9776  C CD1 . PHE H 5 112 ? 21.752  37.414  18.289 1.000 178.230 0 112 PHE HHH CD1 1 ? 11 
ATOM 9777  C CD2 . PHE H 5 112 ? 22.929  37.078  16.245 1.000 180.148 0 112 PHE HHH CD2 1 ? 11 
ATOM 9778  C CE1 . PHE H 5 112 ? 20.634  37.814  17.584 1.000 183.320 0 112 PHE HHH CE1 1 ? 11 
ATOM 9779  C CE2 . PHE H 5 112 ? 21.812  37.476  15.534 1.000 185.326 0 112 PHE HHH CE2 1 ? 11 
ATOM 9780  C CZ  . PHE H 5 112 ? 20.663  37.844  16.206 1.000 179.492 0 112 PHE HHH CZ  1 ? 11 
ATOM 9781  N N   . PHE H 5 113 ? 26.615  38.238  17.293 1.000 159.750 0 113 PHE HHH N   1 ? 11 
ATOM 9782  C CA  . PHE H 5 113 ? 27.152  38.911  16.120 1.000 157.597 0 113 PHE HHH CA  1 ? 11 
ATOM 9783  C C   . PHE H 5 113 ? 27.457  37.882  15.045 1.000 157.503 0 113 PHE HHH C   1 ? 11 
ATOM 9784  O O   . PHE H 5 113 ? 28.008  36.814  15.329 1.000 166.231 0 113 PHE HHH O   1 ? 11 
ATOM 9785  C CB  . PHE H 5 113 ? 28.404  39.749  16.459 1.000 160.145 0 113 PHE HHH CB  1 ? 11 
ATOM 9786  C CG  . PHE H 5 113 ? 29.566  38.960  17.015 1.000 163.181 0 113 PHE HHH CG  1 ? 11 
ATOM 9787  C CD1 . PHE H 5 113 ? 30.503  38.385  16.171 1.000 161.366 0 113 PHE HHH CD1 1 ? 11 
ATOM 9788  C CD2 . PHE H 5 113 ? 29.730  38.811  18.383 1.000 172.756 0 113 PHE HHH CD2 1 ? 11 
ATOM 9789  C CE1 . PHE H 5 113 ? 31.576  37.676  16.679 1.000 167.198 0 113 PHE HHH CE1 1 ? 11 
ATOM 9790  C CE2 . PHE H 5 113 ? 30.803  38.101  18.894 1.000 177.596 0 113 PHE HHH CE2 1 ? 11 
ATOM 9791  C CZ  . PHE H 5 113 ? 31.727  37.537  18.040 1.000 172.437 0 113 PHE HHH CZ  1 ? 11 
ATOM 9792  N N   . ILE H 5 114 ? 27.080  38.203  13.813 1.000 155.615 0 114 ILE HHH N   1 ? 11 
ATOM 9793  C CA  . ILE H 5 114 ? 27.294  37.328  12.671 1.000 156.661 0 114 ILE HHH CA  1 ? 11 
ATOM 9794  C C   . ILE H 5 114 ? 28.515  37.859  11.939 1.000 155.666 0 114 ILE HHH C   1 ? 11 
ATOM 9795  O O   . ILE H 5 114 ? 28.483  38.953  11.366 1.000 151.162 0 114 ILE HHH O   1 ? 11 
ATOM 9796  C CB  . ILE H 5 114 ? 26.070  37.288  11.749 1.000 153.579 0 114 ILE HHH CB  1 ? 11 
ATOM 9797  C CG1 . ILE H 5 114 ? 24.787  37.227  12.575 1.000 151.226 0 114 ILE HHH CG1 1 ? 11 
ATOM 9798  C CG2 . ILE H 5 114 ? 26.156  36.096  10.805 1.000 147.396 0 114 ILE HHH CG2 1 ? 11 
ATOM 9799  C CD1 . ILE H 5 114 ? 23.549  37.570  11.788 1.000 145.064 0 114 ILE HHH CD1 1 ? 11 
ATOM 9800  N N   . CYS H 5 115 ? 29.594  37.086  11.963 1.000 157.737 0 115 CYS HHH N   1 ? 11 
ATOM 9801  C CA  . CYS H 5 115 ? 30.831  37.522  11.337 1.000 156.506 0 115 CYS HHH CA  1 ? 11 
ATOM 9802  C C   . CYS H 5 115 ? 30.717  37.509  9.820  1.000 156.685 0 115 CYS HHH C   1 ? 11 
ATOM 9803  O O   . CYS H 5 115 ? 30.115  36.607  9.229  1.000 164.099 0 115 CYS HHH O   1 ? 11 
ATOM 9804  C CB  . CYS H 5 115 ? 31.994  36.621  11.759 1.000 161.338 0 115 CYS HHH CB  1 ? 11 
ATOM 9805  S SG  . CYS H 5 115 ? 32.402  36.619  13.514 1.000 163.807 0 115 CYS HHH SG  1 ? 11 
ATOM 9806  N N   . THR H 5 116 ? 31.288  38.531  9.187  1.000 150.294 0 116 THR HHH N   1 ? 11 
ATOM 9807  C CA  . THR H 5 116 ? 31.353  38.588  7.736  1.000 150.529 0 116 THR HHH CA  1 ? 11 
ATOM 9808  C C   . THR H 5 116 ? 32.808  38.549  7.299  1.000 152.870 0 116 THR HHH C   1 ? 11 
ATOM 9809  O O   . THR H 5 116 ? 33.114  38.786  6.124  1.000 152.322 0 116 THR HHH O   1 ? 11 
ATOM 9810  C CB  . THR H 5 116 ? 30.673  39.855  7.210  1.000 145.267 0 116 THR HHH CB  1 ? 11 
ATOM 9811  O OG1 . THR H 5 116 ? 31.284  41.005  7.807  1.000 134.604 0 116 THR HHH OG1 1 ? 11 
ATOM 9812  C CG2 . THR H 5 116 ? 29.195  39.847  7.570  1.000 148.031 0 116 THR HHH CG2 1 ? 11 
ATOM 9813  N N   . ALA H 5 117 ? 33.703  38.252  8.235  1.000 164.579 0 117 ALA HHH N   1 ? 11 
ATOM 9814  C CA  . ALA H 5 117 ? 35.124  38.078  7.989  1.000 171.896 0 117 ALA HHH CA  1 ? 11 
ATOM 9815  C C   . ALA H 5 117 ? 35.697  37.200  9.094  1.000 182.276 0 117 ALA HHH C   1 ? 11 
ATOM 9816  O O   . ALA H 5 117 ? 35.037  36.907  10.093 1.000 185.766 0 117 ALA HHH O   1 ? 11 
ATOM 9817  C CB  . ALA H 5 117 ? 35.847  39.426  7.918  1.000 172.133 0 117 ALA HHH CB  1 ? 11 
ATOM 9818  N N   . LYS H 5 118 ? 36.938  36.777  8.889  1.000 180.991 0 118 LYS HHH N   1 ? 11 
ATOM 9819  C CA  . LYS H 5 118 ? 37.683  36.077  9.926  1.000 185.160 0 118 LYS HHH CA  1 ? 11 
ATOM 9820  C C   . LYS H 5 118 ? 38.041  37.122  10.980 1.000 190.961 0 118 LYS HHH C   1 ? 11 
ATOM 9821  O O   . LYS H 5 118 ? 38.559  38.192  10.648 1.000 188.217 0 118 LYS HHH O   1 ? 11 
ATOM 9822  C CB  . LYS H 5 118 ? 38.919  35.392  9.350  1.000 186.204 0 118 LYS HHH CB  1 ? 11 
ATOM 9823  C CG  . LYS H 5 118 ? 39.752  34.649  10.376 1.000 190.576 0 118 LYS HHH CG  1 ? 11 
ATOM 9824  C CD  . LYS H 5 118 ? 40.917  33.937  9.711  1.000 190.007 0 118 LYS HHH CD  1 ? 11 
ATOM 9825  C CE  . LYS H 5 118 ? 41.753  33.171  10.721 1.000 200.156 0 118 LYS HHH CE  1 ? 11 
ATOM 9826  N NZ  . LYS H 5 118 ? 42.904  32.476  10.082 1.000 200.016 0 118 LYS HHH NZ  1 ? 11 
ATOM 9827  N N   . THR H 5 119 ? 37.760  36.826  12.254 1.000 196.059 0 119 THR HHH N   1 ? 11 
ATOM 9828  C CA  . THR H 5 119 ? 37.923  37.801  13.336 1.000 193.485 0 119 THR HHH CA  1 ? 11 
ATOM 9829  C C   . THR H 5 119 ? 38.778  37.242  14.475 1.000 201.587 0 119 THR HHH C   1 ? 11 
ATOM 9830  O O   . THR H 5 119 ? 38.289  36.983  15.577 1.000 206.234 0 119 THR HHH O   1 ? 11 
ATOM 9831  C CB  . THR H 5 119 ? 36.553  38.232  13.873 1.000 184.770 0 119 THR HHH CB  1 ? 11 
ATOM 9832  O OG1 . THR H 5 119 ? 35.839  37.076  14.332 1.000 178.592 0 119 THR HHH OG1 1 ? 11 
ATOM 9833  C CG2 . THR H 5 119 ? 35.732  38.916  12.792 1.000 180.192 0 119 THR HHH CG2 1 ? 11 
ATOM 9834  N N   . GLU H 5 120 ? 40.068  37.036  14.187 1.000 211.326 0 120 GLU HHH N   1 ? 11 
ATOM 9835  C CA  . GLU H 5 120 ? 40.914  36.276  15.095 1.000 215.716 0 120 GLU HHH CA  1 ? 11 
ATOM 9836  C C   . GLU H 5 120 ? 41.109  37.021  16.409 1.000 209.721 0 120 GLU HHH C   1 ? 11 
ATOM 9837  O O   . GLU H 5 120 ? 41.392  36.399  17.437 1.000 216.404 0 120 GLU HHH O   1 ? 11 
ATOM 9838  C CB  . GLU H 5 120 ? 42.283  36.045  14.458 1.000 227.336 0 120 GLU HHH CB  1 ? 11 
ATOM 9839  C CG  . GLU H 5 120 ? 42.250  35.780  12.965 1.000 238.357 0 120 GLU HHH CG  1 ? 11 
ATOM 9840  C CD  . GLU H 5 120 ? 42.254  37.067  12.148 1.000 237.860 0 120 GLU HHH CD  1 ? 11 
ATOM 9841  O OE1 . GLU H 5 120 ? 42.726  38.099  12.671 1.000 236.199 0 120 GLU HHH OE1 1 ? 11 
ATOM 9842  O OE2 . GLU H 5 120 ? 41.789  37.049  10.989 1.000 238.486 0 120 GLU HHH OE2 1 ? 11 
ATOM 9843  N N   . TRP H 5 121 ? 40.990  38.354  16.393 1.000 190.474 0 121 TRP HHH N   1 ? 11 
ATOM 9844  C CA  . TRP H 5 121 ? 41.151  39.126  17.618 1.000 183.742 0 121 TRP HHH CA  1 ? 11 
ATOM 9845  C C   . TRP H 5 121 ? 40.022  38.899  18.613 1.000 182.978 0 121 TRP HHH C   1 ? 11 
ATOM 9846  O O   . TRP H 5 121 ? 40.159  39.291  19.777 1.000 184.160 0 121 TRP HHH O   1 ? 11 
ATOM 9847  C CB  . TRP H 5 121 ? 41.324  40.608  17.269 1.000 179.660 0 121 TRP HHH CB  1 ? 11 
ATOM 9848  C CG  . TRP H 5 121 ? 40.161  41.204  16.557 1.000 176.065 0 121 TRP HHH CG  1 ? 11 
ATOM 9849  C CD1 . TRP H 5 121 ? 39.067  41.809  17.101 1.000 170.448 0 121 TRP HHH CD1 1 ? 11 
ATOM 9850  C CD2 . TRP H 5 121 ? 39.988  41.257  15.137 1.000 183.555 0 121 TRP HHH CD2 1 ? 11 
ATOM 9851  N NE1 . TRP H 5 121 ? 38.217  42.229  16.102 1.000 169.946 0 121 TRP HHH NE1 1 ? 11 
ATOM 9852  C CE2 . TRP H 5 121 ? 38.762  41.901  14.888 1.000 176.095 0 121 TRP HHH CE2 1 ? 11 
ATOM 9853  C CE3 . TRP H 5 121 ? 40.753  40.816  14.051 1.000 195.162 0 121 TRP HHH CE3 1 ? 11 
ATOM 9854  C CZ2 . TRP H 5 121 ? 38.282  42.116  13.596 1.000 175.233 0 121 TRP HHH CZ2 1 ? 11 
ATOM 9855  C CZ3 . TRP H 5 121 ? 40.277  41.031  12.772 1.000 196.872 0 121 TRP HHH CZ3 1 ? 11 
ATOM 9856  C CH2 . TRP H 5 121 ? 39.053  41.675  12.555 1.000 184.733 0 121 TRP HHH CH2 1 ? 11 
ATOM 9857  N N   . LEU H 5 122 ? 38.913  38.287  18.190 1.000 196.593 0 122 LEU HHH N   1 ? 11 
ATOM 9858  C CA  . LEU H 5 122 ? 37.834  37.943  19.104 1.000 197.680 0 122 LEU HHH CA  1 ? 11 
ATOM 9859  C C   . LEU H 5 122 ? 38.040  36.567  19.719 1.000 209.418 0 122 LEU HHH C   1 ? 11 
ATOM 9860  O O   . LEU H 5 122 ? 37.305  36.198  20.641 1.000 212.353 0 122 LEU HHH O   1 ? 11 
ATOM 9861  C CB  . LEU H 5 122 ? 36.475  38.005  18.397 1.000 193.189 0 122 LEU HHH CB  1 ? 11 
ATOM 9862  C CG  . LEU H 5 122 ? 36.113  39.356  17.776 1.000 184.366 0 122 LEU HHH CG  1 ? 11 
ATOM 9863  C CD1 . LEU H 5 122 ? 34.791  39.276  17.034 1.000 175.579 0 122 LEU HHH CD1 1 ? 11 
ATOM 9864  C CD2 . LEU H 5 122 ? 36.065  40.436  18.848 1.000 183.182 0 122 LEU HHH CD2 1 ? 11 
ATOM 9865  N N   . ASP H 5 123 ? 39.008  35.807  19.206 1.000 217.339 0 123 ASP HHH N   1 ? 11 
ATOM 9866  C CA  . ASP H 5 123 ? 39.277  34.465  19.701 1.000 230.824 0 123 ASP HHH CA  1 ? 11 
ATOM 9867  C C   . ASP H 5 123 ? 39.652  34.540  21.172 1.000 231.687 0 123 ASP HHH C   1 ? 11 
ATOM 9868  O O   . ASP H 5 123 ? 40.481  35.363  21.571 1.000 234.782 0 123 ASP HHH O   1 ? 11 
ATOM 9869  C CB  . ASP H 5 123 ? 40.402  33.821  18.890 1.000 247.028 0 123 ASP HHH CB  1 ? 11 
ATOM 9870  C CG  . ASP H 5 123 ? 39.977  33.484  17.470 1.000 255.784 0 123 ASP HHH CG  1 ? 11 
ATOM 9871  O OD1 . ASP H 5 123 ? 38.760  33.503  17.193 1.000 257.652 0 123 ASP HHH OD1 1 ? 11 
ATOM 9872  O OD2 . ASP H 5 123 ? 40.859  33.217  16.624 1.000 260.955 0 123 ASP HHH OD2 1 ? 11 
ATOM 9873  N N   . GLY H 5 124 ? 39.040  33.684  21.981 1.000 232.510 0 124 GLY HHH N   1 ? 11 
ATOM 9874  C CA  . GLY H 5 124 ? 39.367  33.649  23.387 1.000 232.745 0 124 GLY HHH CA  1 ? 11 
ATOM 9875  C C   . GLY H 5 124 ? 38.629  34.668  24.223 1.000 226.851 0 124 GLY HHH C   1 ? 11 
ATOM 9876  O O   . GLY H 5 124 ? 38.845  34.718  25.440 1.000 234.743 0 124 GLY HHH O   1 ? 11 
ATOM 9877  N N   . LYS H 5 125 ? 37.804  35.511  23.602 1.000 219.909 0 125 LYS HHH N   1 ? 11 
ATOM 9878  C CA  . LYS H 5 125 ? 37.022  36.536  24.281 1.000 212.902 0 125 LYS HHH CA  1 ? 11 
ATOM 9879  C C   . LYS H 5 125 ? 35.516  36.374  24.120 1.000 215.277 0 125 LYS HHH C   1 ? 11 
ATOM 9880  O O   . LYS H 5 125 ? 34.773  36.746  25.032 1.000 211.728 0 125 LYS HHH O   1 ? 11 
ATOM 9881  C CB  . LYS H 5 125 ? 37.440  37.940  23.810 1.000 203.255 0 125 LYS HHH CB  1 ? 11 
ATOM 9882  C CG  . LYS H 5 125 ? 38.947  38.182  23.847 1.000 196.862 0 125 LYS HHH CG  1 ? 11 
ATOM 9883  C CD  . LYS H 5 125 ? 39.304  39.605  23.446 1.000 188.149 0 125 LYS HHH CD  1 ? 11 
ATOM 9884  C CE  . LYS H 5 125 ? 40.810  39.785  23.334 1.000 180.571 0 125 LYS HHH CE  1 ? 11 
ATOM 9885  N NZ  . LYS H 5 125 ? 41.164  41.043  22.623 1.000 183.627 0 125 LYS HHH NZ  1 ? 11 
ATOM 9886  N N   . HIS H 5 126 ? 35.046  35.837  22.995 1.000 221.798 0 126 HIS HHH N   1 ? 11 
ATOM 9887  C CA  . HIS H 5 126 ? 33.628  35.645  22.724 1.000 219.951 0 126 HIS HHH CA  1 ? 11 
ATOM 9888  C C   . HIS H 5 126 ? 33.335  34.173  22.450 1.000 220.731 0 126 HIS HHH C   1 ? 11 
ATOM 9889  O O   . HIS H 5 126 ? 34.224  33.397  22.087 1.000 221.654 0 126 HIS HHH O   1 ? 11 
ATOM 9890  C CB  . HIS H 5 126 ? 33.174  36.489  21.521 1.000 216.212 0 126 HIS HHH CB  1 ? 11 
ATOM 9891  C CG  . HIS H 5 126 ? 33.280  37.969  21.735 1.000 213.765 0 126 HIS HHH CG  1 ? 11 
ATOM 9892  N ND1 . HIS H 5 126 ? 32.218  38.741  22.157 1.000 207.383 0 126 HIS HHH ND1 1 ? 11 
ATOM 9893  C CD2 . HIS H 5 126 ? 34.322  38.819  21.576 1.000 211.776 0 126 HIS HHH CD2 1 ? 11 
ATOM 9894  C CE1 . HIS H 5 126 ? 32.602  40.002  22.250 1.000 201.852 0 126 HIS HHH CE1 1 ? 11 
ATOM 9895  N NE2 . HIS H 5 126 ? 33.875  40.076  21.905 1.000 203.350 0 126 HIS HHH NE2 1 ? 11 
ATOM 9896  N N   . VAL H 5 127 ? 32.067  33.798  22.629 1.000 210.172 0 127 VAL HHH N   1 ? 11 
ATOM 9897  C CA  . VAL H 5 127 ? 31.635  32.402  22.645 1.000 213.820 0 127 VAL HHH CA  1 ? 11 
ATOM 9898  C C   . VAL H 5 127 ? 31.013  32.064  21.298 1.000 209.616 0 127 VAL HHH C   1 ? 11 
ATOM 9899  O O   . VAL H 5 127 ? 29.946  32.584  20.955 1.000 206.141 0 127 VAL HHH O   1 ? 11 
ATOM 9900  C CB  . VAL H 5 127 ? 30.618  32.150  23.770 1.000 217.543 0 127 VAL HHH CB  1 ? 11 
ATOM 9901  C CG1 . VAL H 5 127 ? 30.283  30.668  23.880 1.000 228.398 0 127 VAL HHH CG1 1 ? 11 
ATOM 9902  C CG2 . VAL H 5 127 ? 31.122  32.706  25.085 1.000 221.341 0 127 VAL HHH CG2 1 ? 11 
ATOM 9903  N N   . VAL H 5 128 ? 31.639  31.145  20.568 1.000 224.048 0 128 VAL HHH N   1 ? 11 
ATOM 9904  C CA  . VAL H 5 128 ? 31.157  30.715  19.259 1.000 223.005 0 128 VAL HHH CA  1 ? 11 
ATOM 9905  C C   . VAL H 5 128 ? 30.126  29.609  19.452 1.000 227.967 0 128 VAL HHH C   1 ? 11 
ATOM 9906  O O   . VAL H 5 128 ? 30.439  28.549  20.004 1.000 226.143 0 128 VAL HHH O   1 ? 11 
ATOM 9907  C CB  . VAL H 5 128 ? 32.319  30.241  18.375 1.000 223.400 0 128 VAL HHH CB  1 ? 11 
ATOM 9908  C CG1 . VAL H 5 128 ? 31.801  29.798  17.024 1.000 223.737 0 128 VAL HHH CG1 1 ? 11 
ATOM 9909  C CG2 . VAL H 5 128 ? 33.348  31.350  18.221 1.000 215.572 0 128 VAL HHH CG2 1 ? 11 
ATOM 9910  N N   . PHE H 5 129 ? 28.891  29.851  19.001 1.000 221.552 0 129 PHE HHH N   1 ? 11 
ATOM 9911  C CA  . PHE H 5 129 ? 27.817  28.885  19.195 1.000 224.361 0 129 PHE HHH CA  1 ? 11 
ATOM 9912  C C   . PHE H 5 129 ? 27.072  28.451  17.935 1.000 233.071 0 129 PHE HHH C   1 ? 11 
ATOM 9913  O O   . PHE H 5 129 ? 26.136  27.652  18.049 1.000 241.466 0 129 PHE HHH O   1 ? 11 
ATOM 9914  C CB  . PHE H 5 129 ? 26.788  29.417  20.208 1.000 223.899 0 129 PHE HHH CB  1 ? 11 
ATOM 9915  C CG  . PHE H 5 129 ? 26.000  30.608  19.729 1.000 216.505 0 129 PHE HHH CG  1 ? 11 
ATOM 9916  C CD1 . PHE H 5 129 ? 26.482  31.893  19.901 1.000 211.363 0 129 PHE HHH CD1 1 ? 11 
ATOM 9917  C CD2 . PHE H 5 129 ? 24.758  30.438  19.135 1.000 217.318 0 129 PHE HHH CD2 1 ? 11 
ATOM 9918  C CE1 . PHE H 5 129 ? 25.749  32.986  19.472 1.000 208.421 0 129 PHE HHH CE1 1 ? 11 
ATOM 9919  C CE2 . PHE H 5 129 ? 24.022  31.525  18.704 1.000 214.696 0 129 PHE HHH CE2 1 ? 11 
ATOM 9920  C CZ  . PHE H 5 129 ? 24.517  32.801  18.876 1.000 211.327 0 129 PHE HHH CZ  1 ? 11 
ATOM 9921  N N   . GLY H 5 130 ? 27.428  28.948  16.755 1.000 244.199 0 130 GLY HHH N   1 ? 11 
ATOM 9922  C CA  . GLY H 5 130 ? 26.702  28.521  15.572 1.000 242.406 0 130 GLY HHH CA  1 ? 11 
ATOM 9923  C C   . GLY H 5 130 ? 27.386  28.918  14.282 1.000 234.896 0 130 GLY HHH C   1 ? 11 
ATOM 9924  O O   . GLY H 5 130 ? 28.471  29.507  14.274 1.000 231.778 0 130 GLY HHH O   1 ? 11 
ATOM 9925  N N   . LYS H 5 131 ? 26.713  28.583  13.180 1.000 227.902 0 131 LYS HHH N   1 ? 11 
ATOM 9926  C CA  . LYS H 5 131 ? 27.167  28.927  11.843 1.000 217.961 0 131 LYS HHH CA  1 ? 11 
ATOM 9927  C C   . LYS H 5 131 ? 25.945  29.093  10.952 1.000 217.855 0 131 LYS HHH C   1 ? 11 
ATOM 9928  O O   . LYS H 5 131 ? 24.937  28.396  11.111 1.000 218.901 0 131 LYS HHH O   1 ? 11 
ATOM 9929  C CB  . LYS H 5 131 ? 28.086  27.815  11.306 1.000 218.174 0 131 LYS HHH CB  1 ? 11 
ATOM 9930  C CG  . LYS H 5 131 ? 28.505  27.882  9.839  1.000 207.907 0 131 LYS HHH CG  1 ? 11 
ATOM 9931  C CD  . LYS H 5 131 ? 29.317  29.104  9.490  1.000 201.787 0 131 LYS HHH CD  1 ? 11 
ATOM 9932  C CE  . LYS H 5 131 ? 29.740  29.051  8.030  1.000 198.246 0 131 LYS HHH CE  1 ? 11 
ATOM 9933  N NZ  . LYS H 5 131 ? 28.577  28.876  7.117  1.000 190.186 0 131 LYS HHH NZ  1 ? 11 
ATOM 9934  N N   . VAL H 5 132 ? 26.061  30.043  10.017 1.000 217.064 0 132 VAL HHH N   1 ? 11 
ATOM 9935  C CA  . VAL H 5 132 ? 25.109  30.221  8.926  1.000 212.251 0 132 VAL HHH CA  1 ? 11 
ATOM 9936  C C   . VAL H 5 132 ? 25.043  29.003  8.021  1.000 221.838 0 132 VAL HHH C   1 ? 11 
ATOM 9937  O O   . VAL H 5 132 ? 26.070  28.512  7.535  1.000 223.600 0 132 VAL HHH O   1 ? 11 
ATOM 9938  C CB  . VAL H 5 132 ? 25.458  31.477  8.111  1.000 194.069 0 132 VAL HHH CB  1 ? 11 
ATOM 9939  C CG1 . VAL H 5 132 ? 24.529  31.601  6.915  1.000 201.935 0 132 VAL HHH CG1 1 ? 11 
ATOM 9940  C CG2 . VAL H 5 132 ? 25.362  32.726  8.966  1.000 190.156 0 132 VAL HHH CG2 1 ? 11 
ATOM 9941  N N   . LYS H 5 133 ? 23.825  28.517  7.782  1.000 218.738 0 133 LYS HHH N   1 ? 11 
ATOM 9942  C CA  . LYS H 5 133 ? 23.575  27.384  6.901  1.000 219.977 0 133 LYS HHH CA  1 ? 11 
ATOM 9943  C C   . LYS H 5 133 ? 23.076  27.877  5.550  1.000 216.741 0 133 LYS HHH C   1 ? 11 
ATOM 9944  O O   . LYS H 5 133 ? 23.603  27.485  4.505  1.000 210.864 0 133 LYS HHH O   1 ? 11 
ATOM 9945  C CB  . LYS H 5 133 ? 22.582  26.377  7.493  1.000 231.495 0 133 LYS HHH CB  1 ? 11 
ATOM 9946  C CG  . LYS H 5 133 ? 22.451  25.148  6.589  1.000 240.423 0 133 LYS HHH CG  1 ? 11 
ATOM 9947  C CD  . LYS H 5 133 ? 21.496  24.092  7.105  1.000 243.923 0 133 LYS HHH CD  1 ? 11 
ATOM 9948  C CE  . LYS H 5 133 ? 21.613  22.838  6.242  1.000 257.114 0 133 LYS HHH CE  1 ? 11 
ATOM 9949  N NZ  . LYS H 5 133 ? 20.731  21.729  6.696  1.000 266.492 0 133 LYS HHH NZ  1 ? 11 
ATOM 9950  N N   . GLU H 5 134 ? 22.060  28.740  5.557  1.000 229.076 0 134 GLU HHH N   1 ? 11 
ATOM 9951  C CA  . GLU H 5 134 ? 21.567  29.374  4.347  1.000 231.476 0 134 GLU HHH CA  1 ? 11 
ATOM 9952  C C   . GLU H 5 134 ? 21.452  30.879  4.539  1.000 220.597 0 134 GLU HHH C   1 ? 11 
ATOM 9953  O O   . GLU H 5 134 ? 21.243  31.376  5.649  1.000 215.348 0 134 GLU HHH O   1 ? 11 
ATOM 9954  C CB  . GLU H 5 134 ? 20.182  28.807  3.970  1.000 251.828 0 134 GLU HHH CB  1 ? 11 
ATOM 9955  C CG  . GLU H 5 134 ? 19.859  28.702  2.496  1.000 276.761 0 134 GLU HHH CG  1 ? 11 
ATOM 9956  C CD  . GLU H 5 134 ? 19.571  30.053  1.877  1.000 285.159 0 134 GLU HHH CD  1 ? 11 
ATOM 9957  O OE1 . GLU H 5 134 ? 18.590  30.711  2.286  1.000 294.162 0 134 GLU HHH OE1 1 ? 11 
ATOM 9958  O OE2 . GLU H 5 134 ? 20.331  30.460  0.985  1.000 290.953 0 134 GLU HHH OE2 1 ? 11 
ATOM 9959  N N   . GLY H 5 135 ? 21.596  31.588  3.423  1.000 210.387 0 135 GLY HHH N   1 ? 11 
ATOM 9960  C CA  . GLY H 5 135 ? 21.453  33.026  3.366  1.000 200.714 0 135 GLY HHH CA  1 ? 11 
ATOM 9961  C C   . GLY H 5 135 ? 22.645  33.854  3.787  1.000 191.889 0 135 GLY HHH C   1 ? 11 
ATOM 9962  O O   . GLY H 5 135 ? 22.454  34.994  4.221  1.000 187.308 0 135 GLY HHH O   1 ? 11 
ATOM 9963  N N   . MET H 5 136 ? 23.876  33.330  3.695  1.000 186.374 0 136 MET HHH N   1 ? 11 
ATOM 9964  C CA  . MET H 5 136 ? 25.012  34.212  3.955  1.000 171.391 0 136 MET HHH CA  1 ? 11 
ATOM 9965  C C   . MET H 5 136 ? 25.015  35.378  2.975  1.000 170.761 0 136 MET HHH C   1 ? 11 
ATOM 9966  O O   . MET H 5 136 ? 25.449  36.483  3.318  1.000 177.593 0 136 MET HHH O   1 ? 11 
ATOM 9967  C CB  . MET H 5 136 ? 26.327  33.432  3.878  1.000 166.410 0 136 MET HHH CB  1 ? 11 
ATOM 9968  C CG  . MET H 5 136 ? 27.078  33.312  5.209  1.000 166.119 0 136 MET HHH CG  1 ? 11 
ATOM 9969  S SD  . MET H 5 136 ? 27.615  34.868  5.951  1.000 155.347 0 136 MET HHH SD  1 ? 11 
ATOM 9970  C CE  . MET H 5 136 ? 28.749  35.460  4.700  1.000 173.620 0 136 MET HHH CE  1 ? 11 
ATOM 9971  N N   . ASN H 5 137 ? 24.536  35.139  1.749  1.000 170.680 0 137 ASN HHH N   1 ? 11 
ATOM 9972  C CA  . ASN H 5 137 ? 24.409  36.194  0.749  1.000 172.216 0 137 ASN HHH CA  1 ? 11 
ATOM 9973  C C   . ASN H 5 137 ? 23.412  37.260  1.185  1.000 167.503 0 137 ASN HHH C   1 ? 11 
ATOM 9974  O O   . ASN H 5 137 ? 23.541  38.431  0.810  1.000 163.875 0 137 ASN HHH O   1 ? 11 
ATOM 9975  C CB  . ASN H 5 137 ? 24.039  35.583  -0.602 1.000 178.335 0 137 ASN HHH CB  1 ? 11 
ATOM 9976  C CG  . ASN H 5 137 ? 24.736  34.259  -0.839 1.000 183.576 0 137 ASN HHH CG  1 ? 11 
ATOM 9977  O OD1 . ASN H 5 137 ? 24.103  33.214  -0.933 1.000 199.434 0 137 ASN HHH OD1 1 ? 11 
ATOM 9978  N ND2 . ASN H 5 137 ? 26.059  34.302  -0.943 1.000 178.877 0 137 ASN HHH ND2 1 ? 11 
ATOM 9979  N N   . ILE H 5 138 ? 22.420  36.867  1.985  1.000 164.043 0 138 ILE HHH N   1 ? 11 
ATOM 9980  C CA  . ILE H 5 138 ? 21.438  37.806  2.517  1.000 164.669 0 138 ILE HHH CA  1 ? 11 
ATOM 9981  C C   . ILE H 5 138 ? 22.072  38.666  3.606  1.000 168.586 0 138 ILE HHH C   1 ? 11 
ATOM 9982  O O   . ILE H 5 138 ? 21.801  39.869  3.708  1.000 165.967 0 138 ILE HHH O   1 ? 11 
ATOM 9983  C CB  . ILE H 5 138 ? 20.203  37.040  3.023  1.000 165.438 0 138 ILE HHH CB  1 ? 11 
ATOM 9984  C CG1 . ILE H 5 138 ? 19.555  36.272  1.869  1.000 177.610 0 138 ILE HHH CG1 1 ? 11 
ATOM 9985  C CG2 . ILE H 5 138 ? 19.190  37.986  3.641  1.000 163.942 0 138 ILE HHH CG2 1 ? 11 
ATOM 9986  C CD1 . ILE H 5 138 ? 18.501  35.284  2.312  1.000 184.789 0 138 ILE HHH CD1 1 ? 11 
ATOM 9987  N N   . VAL H 5 139 ? 22.921  38.057  4.437  1.000 167.360 0 139 VAL HHH N   1 ? 11 
ATOM 9988  C CA  . VAL H 5 139 ? 23.699  38.798  5.428  1.000 160.844 0 139 VAL HHH CA  1 ? 11 
ATOM 9989  C C   . VAL H 5 139 ? 24.580  39.840  4.745  1.000 162.406 0 139 VAL HHH C   1 ? 11 
ATOM 9990  O O   . VAL H 5 139 ? 24.715  40.972  5.225  1.000 165.957 0 139 VAL HHH O   1 ? 11 
ATOM 9991  C CB  . VAL H 5 139 ? 24.532  37.823  6.283  1.000 156.357 0 139 VAL HHH CB  1 ? 11 
ATOM 9992  C CG1 . VAL H 5 139 ? 25.476  38.578  7.213  1.000 157.355 0 139 VAL HHH CG1 1 ? 11 
ATOM 9993  C CG2 . VAL H 5 139 ? 23.623  36.890  7.072  1.000 166.635 0 139 VAL HHH CG2 1 ? 11 
ATOM 9994  N N   . GLU H 5 140 ? 25.173  39.482  3.602  1.000 155.028 0 140 GLU HHH N   1 ? 11 
ATOM 9995  C CA  . GLU H 5 140 ? 26.009  40.424  2.859  1.000 155.030 0 140 GLU HHH CA  1 ? 11 
ATOM 9996  C C   . GLU H 5 140 ? 25.210  41.626  2.369  1.000 155.136 0 140 GLU HHH C   1 ? 11 
ATOM 9997  O O   . GLU H 5 140 ? 25.717  42.754  2.367  1.000 162.707 0 140 GLU HHH O   1 ? 11 
ATOM 9998  C CB  . GLU H 5 140 ? 26.685  39.719  1.681  1.000 162.016 0 140 GLU HHH CB  1 ? 11 
ATOM 9999  C CG  . GLU H 5 140 ? 27.319  40.686  0.680  1.000 165.719 0 140 GLU HHH CG  1 ? 11 
ATOM 10000 C CD  . GLU H 5 140 ? 28.819  40.816  0.816  1.000 164.429 0 140 GLU HHH CD  1 ? 11 
ATOM 10001 O OE1 . GLU H 5 140 ? 29.462  39.862  1.301  1.000 192.777 0 140 GLU HHH OE1 1 ? 11 
ATOM 10002 O OE2 . GLU H 5 140 ? 29.352  41.877  0.421  1.000 137.143 0 140 GLU HHH OE2 1 ? 11 
ATOM 10003 N N   . ALA H 5 141 ? 23.958  41.410  1.963  1.000 150.703 0 141 ALA HHH N   1 ? 11 
ATOM 10004 C CA  . ALA H 5 141 ? 23.119  42.526  1.536  1.000 153.830 0 141 ALA HHH CA  1 ? 11 
ATOM 10005 C C   . ALA H 5 141 ? 22.850  43.475  2.692  1.000 161.897 0 141 ALA HHH C   1 ? 11 
ATOM 10006 O O   . ALA H 5 141 ? 22.804  44.698  2.512  1.000 169.257 0 141 ALA HHH O   1 ? 11 
ATOM 10007 C CB  . ALA H 5 141 ? 21.798  42.003  0.972  1.000 147.619 0 141 ALA HHH CB  1 ? 11 
ATOM 10008 N N   . MET H 5 142 ? 22.686  42.929  3.890  1.000 159.443 0 142 MET HHH N   1 ? 11 
ATOM 10009 C CA  . MET H 5 142 ? 22.462  43.764  5.060  1.000 152.891 0 142 MET HHH CA  1 ? 11 
ATOM 10010 C C   . MET H 5 142 ? 23.639  44.687  5.352  1.000 146.642 0 142 MET HHH C   1 ? 11 
ATOM 10011 O O   . MET H 5 142 ? 23.435  45.837  5.755  1.000 145.581 0 142 MET HHH O   1 ? 11 
ATOM 10012 C CB  . MET H 5 142 ? 22.195  42.895  6.286  1.000 152.684 0 142 MET HHH CB  1 ? 11 
ATOM 10013 C CG  . MET H 5 142 ? 20.878  42.177  6.295  1.000 168.559 0 142 MET HHH CG  1 ? 11 
ATOM 10014 S SD  . MET H 5 142 ? 20.914  40.931  7.597  1.000 175.397 0 142 MET HHH SD  1 ? 11 
ATOM 10015 C CE  . MET H 5 142 ? 21.253  41.903  9.067  1.000 148.959 0 142 MET HHH CE  1 ? 11 
ATOM 10016 N N   . GLU H 5 143 ? 24.875  44.220  5.147  1.000 150.257 0 143 GLU HHH N   1 ? 11 
ATOM 10017 C CA  . GLU H 5 143 ? 26.024  45.021  5.575  1.000 158.804 0 143 GLU HHH CA  1 ? 11 
ATOM 10018 C C   . GLU H 5 143 ? 26.057  46.437  4.988  1.000 159.287 0 143 GLU HHH C   1 ? 11 
ATOM 10019 O O   . GLU H 5 143 ? 26.579  47.347  5.640  1.000 170.189 0 143 GLU HHH O   1 ? 11 
ATOM 10020 C CB  . GLU H 5 143 ? 27.322  44.253  5.323  1.000 159.076 0 143 GLU HHH CB  1 ? 11 
ATOM 10021 C CG  . GLU H 5 143 ? 27.922  44.323  3.967  1.000 173.318 0 143 GLU HHH CG  1 ? 11 
ATOM 10022 C CD  . GLU H 5 143 ? 29.146  43.434  3.877  1.000 179.384 0 143 GLU HHH CD  1 ? 11 
ATOM 10023 O OE1 . GLU H 5 143 ? 29.533  42.840  4.911  1.000 160.929 0 143 GLU HHH OE1 1 ? 11 
ATOM 10024 O OE2 . GLU H 5 143 ? 29.730  43.344  2.779  1.000 191.820 0 143 GLU HHH OE2 1 ? 11 
ATOM 10025 N N   . ARG H 5 144 ? 25.539  46.663  3.781  1.000 140.320 0 144 ARG HHH N   1 ? 11 
ATOM 10026 C CA  . ARG H 5 144 ? 25.699  47.984  3.170  1.000 150.066 0 144 ARG HHH CA  1 ? 11 
ATOM 10027 C C   . ARG H 5 144 ? 24.789  49.005  3.817  1.000 147.672 0 144 ARG HHH C   1 ? 11 
ATOM 10028 O O   . ARG H 5 144 ? 24.932  50.207  3.564  1.000 151.839 0 144 ARG HHH O   1 ? 11 
ATOM 10029 C CB  . ARG H 5 144 ? 25.378  48.005  1.716  1.000 155.108 0 144 ARG HHH CB  1 ? 11 
ATOM 10030 C CG  . ARG H 5 144 ? 25.897  49.159  0.877  1.000 169.823 0 144 ARG HHH CG  1 ? 11 
ATOM 10031 C CD  . ARG H 5 144 ? 27.377  49.450  0.976  1.000 179.147 0 144 ARG HHH CD  1 ? 11 
ATOM 10032 N NE  . ARG H 5 144 ? 28.116  48.354  0.356  1.000 179.781 0 144 ARG HHH NE  1 ? 11 
ATOM 10033 C CZ  . ARG H 5 144 ? 29.348  47.980  0.677  1.000 188.236 0 144 ARG HHH CZ  1 ? 11 
ATOM 10034 N NH1 . ARG H 5 144 ? 30.003  48.591  1.650  1.000 189.242 0 144 ARG HHH NH1 1 ? 11 
ATOM 10035 N NH2 . ARG H 5 144 ? 29.920  46.981  0.006  1.000 185.005 0 144 ARG HHH NH2 1 ? 11 
ATOM 10036 N N   . PHE H 5 145 ? 23.854  48.557  4.636  1.000 146.301 0 145 PHE HHH N   1 ? 11 
ATOM 10037 C CA  . PHE H 5 145 ? 23.007  49.521  5.294  1.000 143.116 0 145 PHE HHH CA  1 ? 11 
ATOM 10038 C C   . PHE H 5 145 ? 23.628  49.882  6.616  1.000 145.537 0 145 PHE HHH C   1 ? 11 
ATOM 10039 O O   . PHE H 5 145 ? 23.083  50.708  7.346  1.000 154.006 0 145 PHE HHH O   1 ? 11 
ATOM 10040 C CB  . PHE H 5 145 ? 21.637  48.904  5.589  1.000 142.122 0 145 PHE HHH CB  1 ? 11 
ATOM 10041 C CG  . PHE H 5 145 ? 20.847  48.506  4.384  1.000 137.076 0 145 PHE HHH CG  1 ? 11 
ATOM 10042 C CD1 . PHE H 5 145 ? 20.229  49.458  3.598  1.000 138.673 0 145 PHE HHH CD1 1 ? 11 
ATOM 10043 C CD2 . PHE H 5 145 ? 20.692  47.166  4.061  1.000 139.096 0 145 PHE HHH CD2 1 ? 11 
ATOM 10044 C CE1 . PHE H 5 145 ? 19.477  49.086  2.507  1.000 141.740 0 145 PHE HHH CE1 1 ? 11 
ATOM 10045 C CE2 . PHE H 5 145 ? 19.947  46.786  2.965  1.000 138.826 0 145 PHE HHH CE2 1 ? 11 
ATOM 10046 C CZ  . PHE H 5 145 ? 19.340  47.747  2.185  1.000 141.893 0 145 PHE HHH CZ  1 ? 11 
ATOM 10047 N N   . GLY H 5 146 ? 24.792  49.297  6.888  1.000 137.844 0 146 GLY HHH N   1 ? 11 
ATOM 10048 C CA  . GLY H 5 146 ? 25.585  49.608  8.051  1.000 126.295 0 146 GLY HHH CA  1 ? 11 
ATOM 10049 C C   . GLY H 5 146 ? 26.564  50.717  7.727  1.000 123.246 0 146 GLY HHH C   1 ? 11 
ATOM 10050 O O   . GLY H 5 146 ? 26.549  51.310  6.647  1.000 121.658 0 146 GLY HHH O   1 ? 11 
ATOM 10051 N N   . SER H 5 147 ? 27.438  50.995  8.683  1.000 138.299 0 147 SER HHH N   1 ? 11 
ATOM 10052 C CA  . SER H 5 147 ? 28.413  52.056  8.489  1.000 143.574 0 147 SER HHH CA  1 ? 11 
ATOM 10053 C C   . SER H 5 147 ? 29.600  51.804  9.404  1.000 147.198 0 147 SER HHH C   1 ? 11 
ATOM 10054 O O   . SER H 5 147 ? 29.587  50.900  10.243 1.000 148.596 0 147 SER HHH O   1 ? 11 
ATOM 10055 C CB  . SER H 5 147 ? 27.805  53.441  8.744  1.000 153.126 0 147 SER HHH CB  1 ? 11 
ATOM 10056 O OG  . SER H 5 147 ? 27.503  53.636  10.115 1.000 154.342 0 147 SER HHH OG  1 ? 11 
ATOM 10057 N N   . ARG H 5 148 ? 30.644  52.608  9.205  1.000 135.166 0 148 ARG HHH N   1 ? 11 
ATOM 10058 C CA  . ARG H 5 148 ? 31.869  52.441  9.977  1.000 131.149 0 148 ARG HHH CA  1 ? 11 
ATOM 10059 C C   . ARG H 5 148 ? 31.595  52.565  11.468 1.000 138.211 0 148 ARG HHH C   1 ? 11 
ATOM 10060 O O   . ARG H 5 148 ? 32.237  51.880  12.273 1.000 139.414 0 148 ARG HHH O   1 ? 11 
ATOM 10061 C CB  . ARG H 5 148 ? 32.979  53.394  9.521  1.000 145.501 0 148 ARG HHH CB  1 ? 11 
ATOM 10062 C CG  . ARG H 5 148 ? 33.565  52.987  8.167  1.000 163.177 0 148 ARG HHH CG  1 ? 11 
ATOM 10063 C CD  . ARG H 5 148 ? 34.771  53.807  7.736  1.000 178.617 0 148 ARG HHH CD  1 ? 11 
ATOM 10064 N NE  . ARG H 5 148 ? 34.550  55.238  7.766  1.000 199.590 0 148 ARG HHH NE  1 ? 11 
ATOM 10065 C CZ  . ARG H 5 148 ? 33.987  55.925  6.777  1.000 211.974 0 148 ARG HHH CZ  1 ? 11 
ATOM 10066 N NH1 . ARG H 5 148 ? 33.597  55.327  5.664  1.000 214.213 0 148 ARG HHH NH1 1 ? 11 
ATOM 10067 N NH2 . ARG H 5 148 ? 33.844  57.241  6.895  1.000 208.470 0 148 ARG HHH NH2 1 ? 11 
ATOM 10068 N N   . ASN H 5 149 ? 30.644  53.415  11.858 1.000 141.420 0 149 ASN HHH N   1 ? 11 
ATOM 10069 C CA  . ASN H 5 149 ? 30.317  53.596  13.264 1.000 129.839 0 149 ASN HHH CA  1 ? 11 
ATOM 10070 C C   . ASN H 5 149 ? 29.240  52.643  13.746 1.000 122.277 0 149 ASN HHH C   1 ? 11 
ATOM 10071 O O   . ASN H 5 149 ? 28.852  52.717  14.915 1.000 128.976 0 149 ASN HHH O   1 ? 11 
ATOM 10072 C CB  . ASN H 5 149 ? 29.754  55.002  13.501 1.000 139.730 0 149 ASN HHH CB  1 ? 11 
ATOM 10073 C CG  . ASN H 5 149 ? 30.422  56.058  12.658 1.000 173.683 0 149 ASN HHH CG  1 ? 11 
ATOM 10074 O OD1 . ASN H 5 149 ? 30.285  56.055  11.434 1.000 186.802 0 149 ASN HHH OD1 1 ? 11 
ATOM 10075 N ND2 . ASN H 5 149 ? 31.114  56.994  13.303 1.000 191.138 0 149 ASN HHH ND2 1 ? 11 
ATOM 10076 N N   . GLY H 5 150 ? 28.742  51.760  12.888 1.000 125.822 0 150 GLY HHH N   1 ? 11 
ATOM 10077 C CA  . GLY H 5 150 ? 27.844  50.714  13.311 1.000 128.758 0 150 GLY HHH CA  1 ? 11 
ATOM 10078 C C   . GLY H 5 150 ? 26.396  51.075  13.092 1.000 131.353 0 150 GLY HHH C   1 ? 11 
ATOM 10079 O O   . GLY H 5 150 ? 25.526  50.198  13.168 1.000 124.221 0 150 GLY HHH O   1 ? 11 
ATOM 10080 N N   . LYS H 5 151 ? 26.134  52.341  12.780 1.000 132.036 0 151 LYS HHH N   1 ? 11 
ATOM 10081 C CA  . LYS H 5 151 ? 24.782  52.815  12.549 1.000 136.218 0 151 LYS HHH CA  1 ? 11 
ATOM 10082 C C   . LYS H 5 151 ? 24.211  52.252  11.263 1.000 139.861 0 151 LYS HHH C   1 ? 11 
ATOM 10083 O O   . LYS H 5 151 ? 24.900  52.172  10.243 1.000 151.567 0 151 LYS HHH O   1 ? 11 
ATOM 10084 C CB  . LYS H 5 151 ? 24.763  54.337  12.417 1.000 139.840 0 151 LYS HHH CB  1 ? 11 
ATOM 10085 C CG  . LYS H 5 151 ? 24.127  55.121  13.533 1.000 158.112 0 151 LYS HHH CG  1 ? 11 
ATOM 10086 C CD  . LYS H 5 151 ? 24.229  56.589  13.156 1.000 166.290 0 151 LYS HHH CD  1 ? 11 
ATOM 10087 C CE  . LYS H 5 151 ? 23.602  57.505  14.182 1.000 180.612 0 151 LYS HHH CE  1 ? 11 
ATOM 10088 N NZ  . LYS H 5 151 ? 23.736  58.931  13.769 1.000 186.390 0 151 LYS HHH NZ  1 ? 11 
ATOM 10089 N N   . THR H 5 152 ? 22.943  51.859  11.309 1.000 147.532 0 152 THR HHH N   1 ? 11 
ATOM 10090 C CA  . THR H 5 152 ? 22.316  51.278  10.138 1.000 148.071 0 152 THR HHH CA  1 ? 11 
ATOM 10091 C C   . THR H 5 152 ? 21.581  52.421  9.453  1.000 152.789 0 152 THR HHH C   1 ? 11 
ATOM 10092 O O   . THR H 5 152 ? 21.038  53.306  10.121 1.000 165.210 0 152 THR HHH O   1 ? 11 
ATOM 10093 C CB  . THR H 5 152 ? 21.354  50.138  10.498 1.000 147.554 0 152 THR HHH CB  1 ? 11 
ATOM 10094 O OG1 . THR H 5 152 ? 20.320  50.622  11.367 1.000 158.654 0 152 THR HHH OG1 1 ? 11 
ATOM 10095 C CG2 . THR H 5 152 ? 22.100  48.999  11.180 1.000 139.221 0 152 THR HHH CG2 1 ? 11 
ATOM 10096 N N   . SER H 5 153 ? 21.561  52.402  8.120  1.000 154.694 0 153 SER HHH N   1 ? 11 
ATOM 10097 C CA  . SER H 5 153 ? 20.914  53.479  7.383  1.000 155.395 0 153 SER HHH CA  1 ? 11 
ATOM 10098 C C   . SER H 5 153 ? 19.422  53.256  7.231  1.000 173.354 0 153 SER HHH C   1 ? 11 
ATOM 10099 O O   . SER H 5 153 ? 18.689  54.204  6.934  1.000 174.359 0 153 SER HHH O   1 ? 11 
ATOM 10100 C CB  . SER H 5 153 ? 21.558  53.645  6.001  1.000 152.899 0 153 SER HHH CB  1 ? 11 
ATOM 10101 O OG  . SER H 5 153 ? 21.503  52.447  5.244  1.000 147.847 0 153 SER HHH OG  1 ? 11 
ATOM 10102 N N   . LYS H 5 154 ? 18.967  52.026  7.453  1.000 177.774 0 154 LYS HHH N   1 ? 11 
ATOM 10103 C CA  . LYS H 5 154 ? 17.563  51.662  7.456  1.000 179.477 0 154 LYS HHH CA  1 ? 11 
ATOM 10104 C C   . LYS H 5 154 ? 17.349  50.703  8.616  1.000 180.383 0 154 LYS HHH C   1 ? 11 
ATOM 10105 O O   . LYS H 5 154 ? 18.298  50.098  9.118  1.000 178.445 0 154 LYS HHH O   1 ? 11 
ATOM 10106 C CB  . LYS H 5 154 ? 17.168  50.993  6.127  1.000 182.604 0 154 LYS HHH CB  1 ? 11 
ATOM 10107 C CG  . LYS H 5 154 ? 17.631  51.757  4.888  1.000 176.595 0 154 LYS HHH CG  1 ? 11 
ATOM 10108 C CD  . LYS H 5 154 ? 16.852  53.023  4.615  1.000 180.998 0 154 LYS HHH CD  1 ? 11 
ATOM 10109 C CE  . LYS H 5 154 ? 17.092  53.483  3.184  1.000 182.684 0 154 LYS HHH CE  1 ? 11 
ATOM 10110 N NZ  . LYS H 5 154 ? 18.554  53.519  2.858  1.000 180.353 0 154 LYS HHH NZ  1 ? 11 
ATOM 10111 N N   . LYS H 5 155 ? 16.102  50.555  9.048  1.000 166.936 0 155 LYS HHH N   1 ? 11 
ATOM 10112 C CA  . LYS H 5 155 ? 15.845  49.681  10.183 1.000 167.623 0 155 LYS HHH CA  1 ? 11 
ATOM 10113 C C   . LYS H 5 155 ? 15.789  48.252  9.664  1.000 166.381 0 155 LYS HHH C   1 ? 11 
ATOM 10114 O O   . LYS H 5 155 ? 14.926  47.910  8.848  1.000 174.361 0 155 LYS HHH O   1 ? 11 
ATOM 10115 C CB  . LYS H 5 155 ? 14.539  50.055  10.880 1.000 169.261 0 155 LYS HHH CB  1 ? 11 
ATOM 10116 C CG  . LYS H 5 155 ? 14.501  51.466  11.435 0.000 171.231 0 155 LYS HHH CG  1 ? 11 
ATOM 10117 C CD  . LYS H 5 155 ? 15.519  51.641  12.550 0.000 153.458 0 155 LYS HHH CD  1 ? 11 
ATOM 10118 C CE  . LYS H 5 155 ? 15.200  50.730  13.730 0.000 149.221 0 155 LYS HHH CE  1 ? 11 
ATOM 10119 N NZ  . LYS H 5 155 ? 16.215  50.838  14.814 0.000 150.850 0 155 LYS HHH NZ  1 ? 11 
ATOM 10120 N N   . ILE H 5 156 ? 16.710  47.423  10.140 1.000 162.023 0 156 ILE HHH N   1 ? 11 
ATOM 10121 C CA  . ILE H 5 156 ? 16.814  46.028  9.738  1.000 160.072 0 156 ILE HHH CA  1 ? 11 
ATOM 10122 C C   . ILE H 5 156 ? 16.189  45.211  10.858 1.000 166.838 0 156 ILE HHH C   1 ? 11 
ATOM 10123 O O   . ILE H 5 156 ? 16.728  45.145  11.968 1.000 174.682 0 156 ILE HHH O   1 ? 11 
ATOM 10124 C CB  . ILE H 5 156 ? 18.274  45.629  9.479  1.000 149.589 0 156 ILE HHH CB  1 ? 11 
ATOM 10125 C CG1 . ILE H 5 156 ? 19.018  46.756  8.754  1.000 148.124 0 156 ILE HHH CG1 1 ? 11 
ATOM 10126 C CG2 . ILE H 5 156 ? 18.355  44.374  8.655  1.000 146.108 0 156 ILE HHH CG2 1 ? 11 
ATOM 10127 C CD1 . ILE H 5 156 ? 18.448  47.092  7.393  1.000 143.032 0 156 ILE HHH CD1 1 ? 11 
ATOM 10128 N N   . THR H 5 157 ? 15.054  44.582  10.569 1.000 169.867 0 157 THR HHH N   1 ? 11 
ATOM 10129 C CA  . THR H 5 157 ? 14.237  43.933  11.583 1.000 175.499 0 157 THR HHH CA  1 ? 11 
ATOM 10130 C C   . THR H 5 157 ? 14.042  42.458  11.253 1.000 177.517 0 157 THR HHH C   1 ? 11 
ATOM 10131 O O   . THR H 5 157 ? 13.913  42.084  10.082 1.000 177.148 0 157 THR HHH O   1 ? 11 
ATOM 10132 C CB  . THR H 5 157 ? 12.879  44.643  11.701 1.000 184.268 0 157 THR HHH CB  1 ? 11 
ATOM 10133 O OG1 . THR H 5 157 ? 13.094  46.029  11.998 1.000 182.778 0 157 THR HHH OG1 1 ? 11 
ATOM 10134 C CG2 . THR H 5 157 ? 12.036  44.033  12.812 1.000 202.527 0 157 THR HHH CG2 1 ? 11 
ATOM 10135 N N   . ILE H 5 158 ? 14.026  41.625  12.292 1.000 180.864 0 158 ILE HHH N   1 ? 11 
ATOM 10136 C CA  . ILE H 5 158 ? 13.713  40.204  12.167 1.000 185.715 0 158 ILE HHH CA  1 ? 11 
ATOM 10137 C C   . ILE H 5 158 ? 12.202  40.057  12.339 1.000 197.494 0 158 ILE HHH C   1 ? 11 
ATOM 10138 O O   . ILE H 5 158 ? 11.685  40.089  13.456 1.000 207.361 0 158 ILE HHH O   1 ? 11 
ATOM 10139 C CB  . ILE H 5 158 ? 14.488  39.360  13.182 1.000 179.005 0 158 ILE HHH CB  1 ? 11 
ATOM 10140 C CG1 . ILE H 5 158 ? 15.908  39.907  13.366 1.000 175.409 0 158 ILE HHH CG1 1 ? 11 
ATOM 10141 C CG2 . ILE H 5 158 ? 14.525  37.900  12.749 1.000 186.781 0 158 ILE HHH CG2 1 ? 11 
ATOM 10142 C CD1 . ILE H 5 158 ? 16.644  39.351  14.578 1.000 181.717 0 158 ILE HHH CD1 1 ? 11 
ATOM 10143 N N   . ALA H 5 159 ? 11.489  39.906  11.217 1.000 196.974 0 159 ALA HHH N   1 ? 11 
ATOM 10144 C CA  . ALA H 5 159 ? 10.030  39.842  11.257 1.000 199.761 0 159 ALA HHH CA  1 ? 11 
ATOM 10145 C C   . ALA H 5 159 ? 9.540   38.521  11.834 1.000 216.474 0 159 ALA HHH C   1 ? 11 
ATOM 10146 O O   . ALA H 5 159 ? 8.504   38.485  12.509 1.000 239.073 0 159 ALA HHH O   1 ? 11 
ATOM 10147 C CB  . ALA H 5 159 ? 9.452   40.049  9.860  1.000 200.520 0 159 ALA HHH CB  1 ? 11 
ATOM 10148 N N   . ASP H 5 160 ? 10.258  37.433  11.573 1.000 230.259 0 160 ASP HHH N   1 ? 11 
ATOM 10149 C CA  . ASP H 5 160 ? 9.920   36.129  12.123 1.000 243.083 0 160 ASP HHH CA  1 ? 11 
ATOM 10150 C C   . ASP H 5 160 ? 11.186  35.292  12.241 1.000 238.287 0 160 ASP HHH C   1 ? 11 
ATOM 10151 O O   . ASP H 5 160 ? 12.187  35.526  11.557 1.000 226.596 0 160 ASP HHH O   1 ? 11 
ATOM 10152 C CB  . ASP H 5 160 ? 8.825   35.419  11.314 1.000 259.556 0 160 ASP HHH CB  1 ? 11 
ATOM 10153 C CG  . ASP H 5 160 ? 9.177   35.269  9.859  1.000 277.350 0 160 ASP HHH CG  1 ? 11 
ATOM 10154 O OD1 . ASP H 5 160 ? 9.235   36.308  9.176  1.000 296.431 0 160 ASP HHH OD1 1 ? 11 
ATOM 10155 O OD2 . ASP H 5 160 ? 9.389   34.127  9.399  1.000 288.717 0 160 ASP HHH OD2 1 ? 11 
ATOM 10156 N N   . CYS H 5 161 ? 11.115  34.308  13.134 1.000 246.368 0 161 CYS HHH N   1 ? 11 
ATOM 10157 C CA  . CYS H 5 161 ? 12.180  33.345  13.370 1.000 245.591 0 161 CYS HHH CA  1 ? 11 
ATOM 10158 C C   . CYS H 5 161 ? 11.569  32.108  14.006 1.000 255.826 0 161 CYS HHH C   1 ? 11 
ATOM 10159 O O   . CYS H 5 161 ? 10.451  32.147  14.524 1.000 268.087 0 161 CYS HHH O   1 ? 11 
ATOM 10160 C CB  . CYS H 5 161 ? 13.288  33.922  14.259 1.000 242.902 0 161 CYS HHH CB  1 ? 11 
ATOM 10161 S SG  . CYS H 5 161 ? 12.734  34.776  15.755 1.000 270.566 0 161 CYS HHH SG  1 ? 11 
ATOM 10162 N N   . GLY H 5 162 ? 12.311  31.007  13.967 1.000 252.458 0 162 GLY HHH N   1 ? 11 
ATOM 10163 C CA  . GLY H 5 162 ? 11.787  29.781  14.528 1.000 264.394 0 162 GLY HHH CA  1 ? 11 
ATOM 10164 C C   . GLY H 5 162 ? 12.692  28.593  14.270 1.000 266.821 0 162 GLY HHH C   1 ? 11 
ATOM 10165 O O   . GLY H 5 162 ? 13.859  28.735  13.894 1.000 255.642 0 162 GLY HHH O   1 ? 11 
ATOM 10166 N N   . GLN H 5 163 ? 12.117  27.417  14.508 1.000 279.017 0 163 GLN HHH N   1 ? 11 
ATOM 10167 C CA  . GLN H 5 163 ? 12.789  26.129  14.412 1.000 292.689 0 163 GLN HHH CA  1 ? 11 
ATOM 10168 C C   . GLN H 5 163 ? 12.327  25.406  13.158 1.000 304.962 0 163 GLN HHH C   1 ? 11 
ATOM 10169 O O   . GLN H 5 163 ? 11.121  25.301  12.908 1.000 315.182 0 163 GLN HHH O   1 ? 11 
ATOM 10170 C CB  . GLN H 5 163 ? 12.454  25.278  15.644 1.000 295.521 0 163 GLN HHH CB  1 ? 11 
ATOM 10171 C CG  . GLN H 5 163 ? 13.112  23.899  15.753 1.000 299.579 0 163 GLN HHH CG  1 ? 11 
ATOM 10172 C CD  . GLN H 5 163 ? 14.623  23.938  15.733 1.000 295.825 0 163 GLN HHH CD  1 ? 11 
ATOM 10173 O OE1 . GLN H 5 163 ? 15.270  23.148  15.043 1.000 296.776 0 163 GLN HHH OE1 1 ? 11 
ATOM 10174 N NE2 . GLN H 5 163 ? 15.199  24.852  16.504 1.000 290.023 0 163 GLN HHH NE2 1 ? 11 
ATOM 10175 N N   . LEU H 5 164 ? 13.306  24.953  12.366 1.000 312.447 0 164 LEU HHH N   1 ? 11 
ATOM 10176 C CA  . LEU H 5 164 ? 13.152  24.097  11.192 1.000 333.959 0 164 LEU HHH CA  1 ? 11 
ATOM 10177 C C   . LEU H 5 164 ? 11.801  23.401  11.126 1.000 357.673 0 164 LEU HHH C   1 ? 11 
ATOM 10178 O O   . LEU H 5 164 ? 11.505  22.510  11.929 1.000 375.789 0 164 LEU HHH O   1 ? 11 
ATOM 10179 C CB  . LEU H 5 164 ? 14.269  23.050  11.152 1.000 334.732 0 164 LEU HHH CB  1 ? 11 
ATOM 10180 C CG  . LEU H 5 164 ? 14.105  21.970  10.078 1.000 347.792 0 164 LEU HHH CG  1 ? 11 
ATOM 10181 C CD1 . LEU H 5 164 ? 14.305  22.555  8.687  1.000 337.738 0 164 LEU HHH CD1 1 ? 11 
ATOM 10182 C CD2 . LEU H 5 164 ? 15.043  20.795  10.313 1.000 352.149 0 164 LEU HHH CD2 1 ? 11 
ATOM 10183 N N   . GLU H 5 165 ? 10.977  23.817  10.174 1.000 373.162 0 165 GLU HHH N   1 ? 11 
ATOM 10184 C CA  . GLU H 5 165 ? 9.656   23.245  9.984  1.000 387.297 0 165 GLU HHH CA  1 ? 11 
ATOM 10185 C C   . GLU H 5 165 ? 9.689   22.123  8.954  1.000 397.556 0 165 GLU HHH C   1 ? 11 
ATOM 10186 O O   . GLU H 5 165 ? 8.646   21.651  8.502  1.000 406.078 0 165 GLU HHH O   1 ? 11 
ATOM 10187 C CB  . GLU H 5 165 ? 8.673   24.339  9.562  1.000 387.137 0 165 GLU HHH CB  1 ? 11 
ATOM 10188 C CG  . GLU H 5 165 ? 9.227   25.325  8.532  1.000 379.961 0 165 GLU HHH CG  1 ? 11 
ATOM 10189 C CD  . GLU H 5 165 ? 9.363   24.732  7.142  1.000 383.672 0 165 GLU HHH CD  1 ? 11 
ATOM 10190 O OE1 . GLU H 5 165 ? 8.482   23.942  6.744  1.000 392.577 0 165 GLU HHH OE1 1 ? 11 
ATOM 10191 O OE2 . GLU H 5 165 ? 10.348  25.058  6.448  1.000 378.963 0 165 GLU HHH OE2 1 ? 11 
ATOM 10192 O OXT . GLU H 5 165 ? 10.761  21.666  8.551  1.000 404.991 0 165 GLU HHH OXT 1 ? 11 
ATOM 10193 N N   . MET I 5 1   ? -1.932  77.441  20.938 1.000 362.401 0 1   MET III N   1 ? 12 
ATOM 10194 C CA  . MET I 5 1   ? -2.882  77.379  19.834 1.000 371.400 0 1   MET III CA  1 ? 12 
ATOM 10195 C C   . MET I 5 1   ? -2.834  78.653  18.991 1.000 378.219 0 1   MET III C   1 ? 12 
ATOM 10196 O O   . MET I 5 1   ? -3.590  78.800  18.032 1.000 374.280 0 1   MET III O   1 ? 12 
ATOM 10197 C CB  . MET I 5 1   ? -4.301  77.153  20.363 1.000 373.366 0 1   MET III CB  1 ? 12 
ATOM 10198 C CG  . MET I 5 1   ? -5.220  76.428  19.393 1.000 375.907 0 1   MET III CG  1 ? 12 
ATOM 10199 S SD  . MET I 5 1   ? -6.967  76.663  19.790 1.000 383.156 0 1   MET III SD  1 ? 12 
ATOM 10200 C CE  . MET I 5 1   ? -7.060  75.889  21.403 1.000 371.504 0 1   MET III CE  1 ? 12 
ATOM 10201 N N   . VAL I 5 2   ? -1.936  79.568  19.348 1.000 396.940 0 2   VAL III N   1 ? 12 
ATOM 10202 C CA  . VAL I 5 2   ? -1.828  80.872  18.704 1.000 392.452 0 2   VAL III CA  1 ? 12 
ATOM 10203 C C   . VAL I 5 2   ? -0.417  81.035  18.153 1.000 381.096 0 2   VAL III C   1 ? 12 
ATOM 10204 O O   . VAL I 5 2   ? 0.562   80.710  18.834 1.000 396.837 0 2   VAL III O   1 ? 12 
ATOM 10205 C CB  . VAL I 5 2   ? -2.180  82.010  19.683 1.000 394.160 0 2   VAL III CB  1 ? 12 
ATOM 10206 C CG1 . VAL I 5 2   ? -1.389  81.873  20.983 1.000 393.840 0 2   VAL III CG1 1 ? 12 
ATOM 10207 C CG2 . VAL I 5 2   ? -1.941  83.367  19.043 1.000 384.234 0 2   VAL III CG2 1 ? 12 
ATOM 10208 N N   . ASN I 5 3   ? -0.318  81.530  16.917 1.000 349.011 0 3   ASN III N   1 ? 12 
ATOM 10209 C CA  . ASN I 5 3   ? 0.965   81.797  16.265 1.000 310.875 0 3   ASN III CA  1 ? 12 
ATOM 10210 C C   . ASN I 5 3   ? 0.884   83.135  15.539 1.000 304.340 0 3   ASN III C   1 ? 12 
ATOM 10211 O O   . ASN I 5 3   ? 0.634   83.193  14.330 1.000 296.993 0 3   ASN III O   1 ? 12 
ATOM 10212 C CB  . ASN I 5 3   ? 1.335   80.672  15.290 1.000 281.373 0 3   ASN III CB  1 ? 12 
ATOM 10213 C CG  . ASN I 5 3   ? 1.952   79.467  15.982 1.000 276.537 0 3   ASN III CG  1 ? 12 
ATOM 10214 O OD1 . ASN I 5 3   ? 2.393   79.556  17.124 1.000 292.571 0 3   ASN III OD1 1 ? 12 
ATOM 10215 N ND2 . ASN I 5 3   ? 1.984   78.334  15.288 1.000 265.027 0 3   ASN III ND2 1 ? 12 
ATOM 10216 N N   . PRO I 5 4   ? 1.082   84.238  16.252 1.000 296.460 0 4   PRO III N   1 ? 12 
ATOM 10217 C CA  . PRO I 5 4   ? 0.966   85.561  15.632 1.000 295.360 0 4   PRO III CA  1 ? 12 
ATOM 10218 C C   . PRO I 5 4   ? 2.177   85.895  14.762 1.000 303.005 0 4   PRO III C   1 ? 12 
ATOM 10219 O O   . PRO I 5 4   ? 3.185   85.187  14.751 1.000 302.165 0 4   PRO III O   1 ? 12 
ATOM 10220 C CB  . PRO I 5 4   ? 0.861   86.513  16.834 1.000 290.301 0 4   PRO III CB  1 ? 12 
ATOM 10221 C CG  . PRO I 5 4   ? 1.544   85.816  17.944 1.000 293.463 0 4   PRO III CG  1 ? 12 
ATOM 10222 C CD  . PRO I 5 4   ? 1.386   84.328  17.689 1.000 300.538 0 4   PRO III CD  1 ? 12 
ATOM 10223 N N   . THR I 5 5   ? 2.059   87.006  14.027 1.000 316.009 0 5   THR III N   1 ? 12 
ATOM 10224 C CA  . THR I 5 5   ? 3.096   87.470  13.111 1.000 309.249 0 5   THR III CA  1 ? 12 
ATOM 10225 C C   . THR I 5 5   ? 3.482   88.921  13.390 1.000 299.168 0 5   THR III C   1 ? 12 
ATOM 10226 O O   . THR I 5 5   ? 2.644   89.737  13.779 1.000 312.056 0 5   THR III O   1 ? 12 
ATOM 10227 C CB  . THR I 5 5   ? 2.639   87.334  11.649 1.000 321.072 0 5   THR III CB  1 ? 12 
ATOM 10228 O OG1 . THR I 5 5   ? 1.262   87.719  11.544 1.000 347.456 0 5   THR III OG1 1 ? 12 
ATOM 10229 C CG2 . THR I 5 5   ? 2.797   85.899  11.167 1.000 320.601 0 5   THR III CG2 1 ? 12 
ATOM 10230 N N   . VAL I 5 6   ? 4.767   89.237  13.193 1.000 277.112 0 6   VAL III N   1 ? 12 
ATOM 10231 C CA  . VAL I 5 6   ? 5.301   90.576  13.431 1.000 265.901 0 6   VAL III CA  1 ? 12 
ATOM 10232 C C   . VAL I 5 6   ? 6.188   90.964  12.246 1.000 260.742 0 6   VAL III C   1 ? 12 
ATOM 10233 O O   . VAL I 5 6   ? 6.856   90.108  11.656 1.000 245.001 0 6   VAL III O   1 ? 12 
ATOM 10234 C CB  . VAL I 5 6   ? 6.079   90.635  14.768 1.000 257.080 0 6   VAL III CB  1 ? 12 
ATOM 10235 C CG1 . VAL I 5 6   ? 7.010   91.846  14.836 1.000 262.227 0 6   VAL III CG1 1 ? 12 
ATOM 10236 C CG2 . VAL I 5 6   ? 5.120   90.605  15.954 1.000 270.769 0 6   VAL III CG2 1 ? 12 
ATOM 10237 N N   . PHE I 5 7   ? 6.181   92.255  11.886 1.000 259.050 0 7   PHE III N   1 ? 12 
ATOM 10238 C CA  . PHE I 5 7   ? 6.891   92.776  10.719 1.000 250.714 0 7   PHE III CA  1 ? 12 
ATOM 10239 C C   . PHE I 5 7   ? 7.859   93.901  11.095 1.000 244.790 0 7   PHE III C   1 ? 12 
ATOM 10240 O O   . PHE I 5 7   ? 7.562   94.718  11.970 1.000 253.676 0 7   PHE III O   1 ? 12 
ATOM 10241 C CB  . PHE I 5 7   ? 5.892   93.239  9.638  1.000 274.919 0 7   PHE III CB  1 ? 12 
ATOM 10242 C CG  . PHE I 5 7   ? 5.000   94.384  10.055 1.000 301.836 0 7   PHE III CG  1 ? 12 
ATOM 10243 C CD1 . PHE I 5 7   ? 5.421   95.699  9.940  1.000 304.399 0 7   PHE III CD1 1 ? 12 
ATOM 10244 C CD2 . PHE I 5 7   ? 3.723   94.138  10.538 1.000 325.793 0 7   PHE III CD2 1 ? 12 
ATOM 10245 C CE1 . PHE I 5 7   ? 4.591   96.746  10.311 1.000 323.593 0 7   PHE III CE1 1 ? 12 
ATOM 10246 C CE2 . PHE I 5 7   ? 2.889   95.181  10.912 1.000 342.053 0 7   PHE III CE2 1 ? 12 
ATOM 10247 C CZ  . PHE I 5 7   ? 3.324   96.485  10.798 1.000 342.544 0 7   PHE III CZ  1 ? 12 
ATOM 10248 N N   . PHE I 5 8   ? 9.009   93.947  10.405 1.000 230.719 0 8   PHE III N   1 ? 12 
ATOM 10249 C CA  . PHE I 5 8   ? 10.040  94.977  10.557 1.000 230.412 0 8   PHE III CA  1 ? 12 
ATOM 10250 C C   . PHE I 5 8   ? 10.344  95.621  9.211  1.000 213.047 0 8   PHE III C   1 ? 12 
ATOM 10251 O O   . PHE I 5 8   ? 10.590  94.912  8.232  1.000 211.557 0 8   PHE III O   1 ? 12 
ATOM 10252 C CB  . PHE I 5 8   ? 11.372  94.430  11.102 1.000 230.409 0 8   PHE III CB  1 ? 12 
ATOM 10253 C CG  . PHE I 5 8   ? 11.374  94.091  12.561 1.000 227.713 0 8   PHE III CG  1 ? 12 
ATOM 10254 C CD1 . PHE I 5 8   ? 10.264  94.302  13.354 1.000 270.717 0 8   PHE III CD1 1 ? 12 
ATOM 10255 C CD2 . PHE I 5 8   ? 12.534  93.617  13.152 1.000 202.260 0 8   PHE III CD2 1 ? 12 
ATOM 10256 C CE1 . PHE I 5 8   ? 10.296  93.995  14.702 1.000 297.361 0 8   PHE III CE1 1 ? 12 
ATOM 10257 C CE2 . PHE I 5 8   ? 12.576  93.319  14.493 1.000 212.418 0 8   PHE III CE2 1 ? 12 
ATOM 10258 C CZ  . PHE I 5 8   ? 11.456  93.511  15.272 1.000 254.980 0 8   PHE III CZ  1 ? 12 
ATOM 10259 N N   . ASP I 5 9   ? 10.328  96.957  9.158  1.000 214.101 0 9   ASP III N   1 ? 12 
ATOM 10260 C CA  . ASP I 5 9   ? 10.887  97.706  8.033  1.000 211.705 0 9   ASP III CA  1 ? 12 
ATOM 10261 C C   . ASP I 5 9   ? 12.316  98.168  8.326  1.000 200.155 0 9   ASP III C   1 ? 12 
ATOM 10262 O O   . ASP I 5 9   ? 12.545  98.927  9.275  1.000 200.534 0 9   ASP III O   1 ? 12 
ATOM 10263 C CB  . ASP I 5 9   ? 10.020  98.923  7.705  1.000 225.610 0 9   ASP III CB  1 ? 12 
ATOM 10264 C CG  . ASP I 5 9   ? 8.769   98.565  6.927  1.000 221.666 0 9   ASP III CG  1 ? 12 
ATOM 10265 O OD1 . ASP I 5 9   ? 7.954   97.765  7.433  1.000 227.007 0 9   ASP III OD1 1 ? 12 
ATOM 10266 O OD2 . ASP I 5 9   ? 8.602   99.086  5.805  1.000 220.590 0 9   ASP III OD2 1 ? 12 
ATOM 10267 N N   . ILE I 5 10  ? 13.272  97.715  7.500  1.000 188.572 0 10  ILE III N   1 ? 12 
ATOM 10268 C CA  . ILE I 5 10  ? 14.706  97.921  7.716  1.000 178.293 0 10  ILE III CA  1 ? 12 
ATOM 10269 C C   . ILE I 5 10  ? 15.195  99.067  6.836  1.000 176.108 0 10  ILE III C   1 ? 12 
ATOM 10270 O O   . ILE I 5 10  ? 14.793  99.180  5.670  1.000 196.194 0 10  ILE III O   1 ? 12 
ATOM 10271 C CB  . ILE I 5 10  ? 15.498  96.628  7.442  1.000 170.905 0 10  ILE III CB  1 ? 12 
ATOM 10272 C CG1 . ILE I 5 10  ? 14.945  95.479  8.287  1.000 176.870 0 10  ILE III CG1 1 ? 12 
ATOM 10273 C CG2 . ILE I 5 10  ? 16.977  96.832  7.731  1.000 166.126 0 10  ILE III CG2 1 ? 12 
ATOM 10274 C CD1 . ILE I 5 10  ? 15.130  95.679  9.785  1.000 190.478 0 10  ILE III CD1 1 ? 12 
ATOM 10275 N N   . ALA I 5 11  ? 16.069  99.919  7.383  1.000 170.192 0 11  ALA III N   1 ? 12 
ATOM 10276 C CA  . ALA I 5 11  ? 16.685  100.998 6.619  1.000 171.485 0 11  ALA III CA  1 ? 12 
ATOM 10277 C C   . ALA I 5 11  ? 18.202  100.939 6.739  1.000 169.320 0 11  ALA III C   1 ? 12 
ATOM 10278 O O   . ALA I 5 11  ? 18.743  100.480 7.749  1.000 163.708 0 11  ALA III O   1 ? 12 
ATOM 10279 C CB  . ALA I 5 11  ? 16.191  102.374 7.081  1.000 190.009 0 11  ALA III CB  1 ? 12 
ATOM 10280 N N   . VAL I 5 12  ? 18.881  101.431 5.703  1.000 181.247 0 12  VAL III N   1 ? 12 
ATOM 10281 C CA  . VAL I 5 12  ? 20.342  101.464 5.642  1.000 190.118 0 12  VAL III CA  1 ? 12 
ATOM 10282 C C   . VAL I 5 12  ? 20.788  102.901 5.402  1.000 210.221 0 12  VAL III C   1 ? 12 
ATOM 10283 O O   . VAL I 5 12  ? 20.554  103.456 4.320  1.000 230.518 0 12  VAL III O   1 ? 12 
ATOM 10284 C CB  . VAL I 5 12  ? 20.890  100.540 4.546  1.000 175.912 0 12  VAL III CB  1 ? 12 
ATOM 10285 C CG1 . VAL I 5 12  ? 22.407  100.660 4.460  1.000 176.629 0 12  VAL III CG1 1 ? 12 
ATOM 10286 C CG2 . VAL I 5 12  ? 20.469  99.103  4.798  1.000 167.552 0 12  VAL III CG2 1 ? 12 
ATOM 10287 N N   . ASP I 5 13  ? 21.460  103.489 6.396  1.000 222.266 0 13  ASP III N   1 ? 12 
ATOM 10288 C CA  . ASP I 5 13  ? 21.835  104.907 6.387  1.000 228.378 0 13  ASP III CA  1 ? 12 
ATOM 10289 C C   . ASP I 5 13  ? 20.663  105.803 5.993  1.000 238.451 0 13  ASP III C   1 ? 12 
ATOM 10290 O O   . ASP I 5 13  ? 20.817  106.779 5.254  1.000 251.373 0 13  ASP III O   1 ? 12 
ATOM 10291 C CB  . ASP I 5 13  ? 23.040  105.153 5.474  1.000 224.013 0 13  ASP III CB  1 ? 12 
ATOM 10292 C CG  . ASP I 5 13  ? 24.358  104.811 6.144  1.000 221.510 0 13  ASP III CG  1 ? 12 
ATOM 10293 O OD1 . ASP I 5 13  ? 24.373  103.905 7.003  1.000 223.242 0 13  ASP III OD1 1 ? 12 
ATOM 10294 O OD2 . ASP I 5 13  ? 25.378  105.456 5.822  1.000 224.255 0 13  ASP III OD2 1 ? 12 
ATOM 10295 N N   . GLY I 5 14  ? 19.474  105.461 6.483  1.000 228.414 0 14  GLY III N   1 ? 12 
ATOM 10296 C CA  . GLY I 5 14  ? 18.278  106.211 6.171  1.000 225.329 0 14  GLY III CA  1 ? 12 
ATOM 10297 C C   . GLY I 5 14  ? 17.619  105.843 4.863  1.000 232.653 0 14  GLY III C   1 ? 12 
ATOM 10298 O O   . GLY I 5 14  ? 16.567  106.409 4.538  1.000 244.129 0 14  GLY III O   1 ? 12 
ATOM 10299 N N   . GLU I 5 15  ? 18.197  104.924 4.103  1.000 222.548 0 15  GLU III N   1 ? 12 
ATOM 10300 C CA  . GLU I 5 15  ? 17.607  104.511 2.841  1.000 210.341 0 15  GLU III CA  1 ? 12 
ATOM 10301 C C   . GLU I 5 15  ? 16.828  103.229 3.042  1.000 202.013 0 15  GLU III C   1 ? 12 
ATOM 10302 O O   . GLU I 5 15  ? 17.366  102.269 3.615  1.000 206.656 0 15  GLU III O   1 ? 12 
ATOM 10303 C CB  . GLU I 5 15  ? 18.687  104.298 1.787  1.000 209.668 0 15  GLU III CB  1 ? 12 
ATOM 10304 C CG  . GLU I 5 15  ? 19.753  105.368 1.795  1.000 217.837 0 15  GLU III CG  1 ? 12 
ATOM 10305 C CD  . GLU I 5 15  ? 20.761  105.187 0.689  1.000 222.852 0 15  GLU III CD  1 ? 12 
ATOM 10306 O OE1 . GLU I 5 15  ? 20.478  104.426 -0.264 1.000 226.850 0 15  GLU III OE1 1 ? 12 
ATOM 10307 O OE2 . GLU I 5 15  ? 21.817  105.846 0.746  1.000 228.517 0 15  GLU III OE2 1 ? 12 
ATOM 10308 N N   . PRO I 5 16  ? 15.573  103.172 2.604  1.000 197.671 0 16  PRO III N   1 ? 12 
ATOM 10309 C CA  . PRO I 5 16  ? 14.780  101.961 2.824  1.000 195.655 0 16  PRO III CA  1 ? 12 
ATOM 10310 C C   . PRO I 5 16  ? 15.394  100.783 2.089  1.000 192.272 0 16  PRO III C   1 ? 12 
ATOM 10311 O O   . PRO I 5 16  ? 15.914  100.916 0.980  1.000 200.537 0 16  PRO III O   1 ? 12 
ATOM 10312 C CB  . PRO I 5 16  ? 13.401  102.324 2.263  1.000 208.939 0 16  PRO III CB  1 ? 12 
ATOM 10313 C CG  . PRO I 5 16  ? 13.655  103.453 1.325  1.000 219.363 0 16  PRO III CG  1 ? 12 
ATOM 10314 C CD  . PRO I 5 16  ? 14.816  104.212 1.891  1.000 206.878 0 16  PRO III CD  1 ? 12 
ATOM 10315 N N   . LEU I 5 17  ? 15.319  99.623  2.726  1.000 184.233 0 17  LEU III N   1 ? 12 
ATOM 10316 C CA  . LEU I 5 17  ? 15.898  98.382  2.239  1.000 178.801 0 17  LEU III CA  1 ? 12 
ATOM 10317 C C   . LEU I 5 17  ? 14.805  97.369  1.944  1.000 180.265 0 17  LEU III C   1 ? 12 
ATOM 10318 O O   . LEU I 5 17  ? 14.746  96.812  0.844  1.000 186.624 0 17  LEU III O   1 ? 12 
ATOM 10319 C CB  . LEU I 5 17  ? 16.911  97.821  3.249  1.000 174.234 0 17  LEU III CB  1 ? 12 
ATOM 10320 C CG  . LEU I 5 17  ? 17.563  96.487  2.877  1.000 167.152 0 17  LEU III CG  1 ? 12 
ATOM 10321 C CD1 . LEU I 5 17  ? 18.410  96.662  1.631  1.000 161.737 0 17  LEU III CD1 1 ? 12 
ATOM 10322 C CD2 . LEU I 5 17  ? 18.413  95.931  4.009  1.000 167.230 0 17  LEU III CD2 1 ? 12 
ATOM 10323 N N   . GLY I 5 18  ? 13.950  97.100  2.918  1.000 180.312 0 18  GLY III N   1 ? 12 
ATOM 10324 C CA  . GLY I 5 18  ? 12.851  96.183  2.723  1.000 183.804 0 18  GLY III CA  1 ? 12 
ATOM 10325 C C   . GLY I 5 18  ? 12.202  95.864  4.048  1.000 186.583 0 18  GLY III C   1 ? 12 
ATOM 10326 O O   . GLY I 5 18  ? 12.655  96.290  5.115  1.000 184.954 0 18  GLY III O   1 ? 12 
ATOM 10327 N N   . ARG I 5 19  ? 11.121  95.103  3.956  1.000 192.381 0 19  ARG III N   1 ? 12 
ATOM 10328 C CA  . ARG I 5 19  ? 10.297  94.771  5.105  1.000 201.404 0 19  ARG III CA  1 ? 12 
ATOM 10329 C C   . ARG I 5 19  ? 10.397  93.274  5.341  1.000 204.489 0 19  ARG III C   1 ? 12 
ATOM 10330 O O   . ARG I 5 19  ? 10.237  92.484  4.404  1.000 193.902 0 19  ARG III O   1 ? 12 
ATOM 10331 C CB  . ARG I 5 19  ? 8.843   95.193  4.882  1.000 209.772 0 19  ARG III CB  1 ? 12 
ATOM 10332 C CG  . ARG I 5 19  ? 7.929   94.953  6.078  1.000 215.504 0 19  ARG III CG  1 ? 12 
ATOM 10333 C CD  . ARG I 5 19  ? 7.068   93.708  5.922  1.000 221.709 0 19  ARG III CD  1 ? 12 
ATOM 10334 N NE  . ARG I 5 19  ? 6.138   93.814  4.813  1.000 235.298 0 19  ARG III NE  1 ? 12 
ATOM 10335 C CZ  . ARG I 5 19  ? 5.326   92.847  4.409  1.000 240.873 0 19  ARG III CZ  1 ? 12 
ATOM 10336 N NH1 . ARG I 5 19  ? 5.292   91.679  5.030  1.000 242.538 0 19  ARG III NH1 1 ? 12 
ATOM 10337 N NH2 . ARG I 5 19  ? 4.528   93.053  3.365  1.000 246.039 0 19  ARG III NH2 1 ? 12 
ATOM 10338 N N   . VAL I 5 20  ? 10.669  92.887  6.583  1.000 217.329 0 20  VAL III N   1 ? 12 
ATOM 10339 C CA  . VAL I 5 20  ? 10.882  91.489  6.935  1.000 215.550 0 20  VAL III CA  1 ? 12 
ATOM 10340 C C   . VAL I 5 20  ? 9.746   91.041  7.838  1.000 215.611 0 20  VAL III C   1 ? 12 
ATOM 10341 O O   . VAL I 5 20  ? 9.533   91.609  8.916  1.000 202.467 0 20  VAL III O   1 ? 12 
ATOM 10342 C CB  . VAL I 5 20  ? 12.235  91.285  7.633  1.000 211.438 0 20  VAL III CB  1 ? 12 
ATOM 10343 C CG1 . VAL I 5 20  ? 12.557  89.801  7.750  1.000 213.841 0 20  VAL III CG1 1 ? 12 
ATOM 10344 C CG2 . VAL I 5 20  ? 13.334  92.029  6.893  1.000 203.626 0 20  VAL III CG2 1 ? 12 
ATOM 10345 N N   . SER I 5 21  ? 9.028   90.015  7.401  1.000 216.266 0 21  SER III N   1 ? 12 
ATOM 10346 C CA  . SER I 5 21  ? 7.959   89.425  8.185  1.000 227.129 0 21  SER III CA  1 ? 12 
ATOM 10347 C C   . SER I 5 21  ? 8.439   88.124  8.810  1.000 217.325 0 21  SER III C   1 ? 12 
ATOM 10348 O O   . SER I 5 21  ? 9.086   87.304  8.151  1.000 208.542 0 21  SER III O   1 ? 12 
ATOM 10349 C CB  . SER I 5 21  ? 6.723   89.173  7.319  1.000 247.032 0 21  SER III CB  1 ? 12 
ATOM 10350 O OG  . SER I 5 21  ? 7.049   88.424  6.160  1.000 241.486 0 21  SER III OG  1 ? 12 
ATOM 10351 N N   . PHE I 5 22  ? 8.141   87.949  10.088 1.000 227.370 0 22  PHE III N   1 ? 12 
ATOM 10352 C CA  . PHE I 5 22  ? 8.414   86.695  10.763 1.000 236.957 0 22  PHE III CA  1 ? 12 
ATOM 10353 C C   . PHE I 5 22  ? 7.197   86.306  11.590 1.000 248.508 0 22  PHE III C   1 ? 12 
ATOM 10354 O O   . PHE I 5 22  ? 6.472   87.160  12.108 1.000 250.924 0 22  PHE III O   1 ? 12 
ATOM 10355 C CB  . PHE I 5 22  ? 9.710   86.748  11.582 1.000 238.771 0 22  PHE III CB  1 ? 12 
ATOM 10356 C CG  . PHE I 5 22  ? 9.892   88.005  12.337 1.000 263.409 0 22  PHE III CG  1 ? 12 
ATOM 10357 C CD1 . PHE I 5 22  ? 9.111   88.276  13.439 1.000 314.875 0 22  PHE III CD1 1 ? 12 
ATOM 10358 C CD2 . PHE I 5 22  ? 10.851  88.923  11.947 1.000 235.031 0 22  PHE III CD2 1 ? 12 
ATOM 10359 C CE1 . PHE I 5 22  ? 9.277   89.434  14.136 1.000 326.875 0 22  PHE III CE1 1 ? 12 
ATOM 10360 C CE2 . PHE I 5 22  ? 11.023  90.091  12.645 1.000 254.814 0 22  PHE III CE2 1 ? 12 
ATOM 10361 C CZ  . PHE I 5 22  ? 10.232  90.349  13.741 1.000 315.344 0 22  PHE III CZ  1 ? 12 
ATOM 10362 N N   . GLU I 5 23  ? 6.979   85.003  11.686 1.000 252.547 0 23  GLU III N   1 ? 12 
ATOM 10363 C CA  . GLU I 5 23  ? 5.909   84.413  12.473 1.000 264.883 0 23  GLU III CA  1 ? 12 
ATOM 10364 C C   . GLU I 5 23  ? 6.510   83.954  13.791 1.000 262.619 0 23  GLU III C   1 ? 12 
ATOM 10365 O O   . GLU I 5 23  ? 7.579   83.339  13.812 1.000 266.618 0 23  GLU III O   1 ? 12 
ATOM 10366 C CB  . GLU I 5 23  ? 5.241   83.244  11.743 1.000 276.209 0 23  GLU III CB  1 ? 12 
ATOM 10367 C CG  . GLU I 5 23  ? 4.188   82.508  12.570 1.000 290.868 0 23  GLU III CG  1 ? 12 
ATOM 10368 C CD  . GLU I 5 23  ? 3.530   81.369  11.810 1.000 297.689 0 23  GLU III CD  1 ? 12 
ATOM 10369 O OE1 . GLU I 5 23  ? 4.182   80.802  10.910 1.000 289.251 0 23  GLU III OE1 1 ? 12 
ATOM 10370 O OE2 . GLU I 5 23  ? 2.361   81.042  12.110 1.000 317.829 0 23  GLU III OE2 1 ? 12 
ATOM 10371 N N   . LEU I 5 24  ? 5.819   84.246  14.889 1.000 271.204 0 24  LEU III N   1 ? 12 
ATOM 10372 C CA  . LEU I 5 24  ? 6.289   83.857  16.209 1.000 257.936 0 24  LEU III CA  1 ? 12 
ATOM 10373 C C   . LEU I 5 24  ? 5.468   82.689  16.732 1.000 275.115 0 24  LEU III C   1 ? 12 
ATOM 10374 O O   . LEU I 5 24  ? 4.233   82.710  16.695 1.000 290.908 0 24  LEU III O   1 ? 12 
ATOM 10375 C CB  . LEU I 5 24  ? 6.166   85.031  17.185 1.000 237.300 0 24  LEU III CB  1 ? 12 
ATOM 10376 C CG  . LEU I 5 24  ? 6.803   86.387  16.869 1.000 223.151 0 24  LEU III CG  1 ? 12 
ATOM 10377 C CD1 . LEU I 5 24  ? 6.548   87.374  18.001 1.000 226.960 0 24  LEU III CD1 1 ? 12 
ATOM 10378 C CD2 . LEU I 5 24  ? 8.290   86.250  16.610 1.000 229.191 0 24  LEU III CD2 1 ? 12 
ATOM 10379 N N   . PHE I 5 25  ? 6.183   81.678  17.224 1.000 257.840 0 25  PHE III N   1 ? 12 
ATOM 10380 C CA  . PHE I 5 25  ? 5.624   80.385  17.616 1.000 272.636 0 25  PHE III CA  1 ? 12 
ATOM 10381 C C   . PHE I 5 25  ? 5.150   80.424  19.070 1.000 286.274 0 25  PHE III C   1 ? 12 
ATOM 10382 O O   . PHE I 5 25  ? 5.691   79.772  19.964 1.000 301.164 0 25  PHE III O   1 ? 12 
ATOM 10383 C CB  . PHE I 5 25  ? 6.635   79.276  17.354 1.000 263.645 0 25  PHE III CB  1 ? 12 
ATOM 10384 C CG  . PHE I 5 25  ? 7.055   79.188  15.914 1.000 254.352 0 25  PHE III CG  1 ? 12 
ATOM 10385 C CD1 . PHE I 5 25  ? 6.110   79.302  14.907 1.000 259.017 0 25  PHE III CD1 1 ? 12 
ATOM 10386 C CD2 . PHE I 5 25  ? 8.382   79.001  15.563 1.000 243.736 0 25  PHE III CD2 1 ? 12 
ATOM 10387 C CE1 . PHE I 5 25  ? 6.475   79.232  13.579 1.000 253.396 0 25  PHE III CE1 1 ? 12 
ATOM 10388 C CE2 . PHE I 5 25  ? 8.754   78.929  14.231 1.000 240.082 0 25  PHE III CE2 1 ? 12 
ATOM 10389 C CZ  . PHE I 5 25  ? 7.797   79.044  13.239 1.000 248.646 0 25  PHE III CZ  1 ? 12 
ATOM 10390 N N   . ALA I 5 26  ? 4.108   81.228  19.288 1.000 294.842 0 26  ALA III N   1 ? 12 
ATOM 10391 C CA  . ALA I 5 26  ? 3.572   81.451  20.625 1.000 289.364 0 26  ALA III CA  1 ? 12 
ATOM 10392 C C   . ALA I 5 26  ? 2.953   80.185  21.201 1.000 301.482 0 26  ALA III C   1 ? 12 
ATOM 10393 O O   . ALA I 5 26  ? 2.749   80.106  22.416 1.000 290.162 0 26  ALA III O   1 ? 12 
ATOM 10394 C CB  . ALA I 5 26  ? 2.544   82.582  20.610 1.000 290.944 0 26  ALA III CB  1 ? 12 
ATOM 10395 N N   . ASP I 5 27  ? 2.631   79.206  20.351 1.000 320.064 0 27  ASP III N   1 ? 12 
ATOM 10396 C CA  . ASP I 5 27  ? 2.082   77.944  20.834 1.000 325.035 0 27  ASP III CA  1 ? 12 
ATOM 10397 C C   . ASP I 5 27  ? 3.117   77.126  21.594 1.000 315.454 0 27  ASP III C   1 ? 12 
ATOM 10398 O O   . ASP I 5 27  ? 2.750   76.314  22.451 1.000 332.465 0 27  ASP III O   1 ? 12 
ATOM 10399 C CB  . ASP I 5 27  ? 1.567   77.118  19.655 1.000 340.327 0 27  ASP III CB  1 ? 12 
ATOM 10400 C CG  . ASP I 5 27  ? 2.683   76.723  18.686 1.000 334.463 0 27  ASP III CG  1 ? 12 
ATOM 10401 O OD1 . ASP I 5 27  ? 3.633   77.516  18.515 1.000 327.462 0 27  ASP III OD1 1 ? 12 
ATOM 10402 O OD2 . ASP I 5 27  ? 2.622   75.616  18.108 1.000 337.892 0 27  ASP III OD2 1 ? 12 
ATOM 10403 N N   . LYS I 5 28  ? 4.402   77.314  21.303 1.000 297.745 0 28  LYS III N   1 ? 12 
ATOM 10404 C CA  . LYS I 5 28  ? 5.457   76.654  22.061 1.000 291.915 0 28  LYS III CA  1 ? 12 
ATOM 10405 C C   . LYS I 5 28  ? 6.141   77.572  23.068 1.000 284.447 0 28  LYS III C   1 ? 12 
ATOM 10406 O O   . LYS I 5 28  ? 6.498   77.123  24.161 1.000 278.051 0 28  LYS III O   1 ? 12 
ATOM 10407 C CB  . LYS I 5 28  ? 6.494   76.057  21.106 1.000 280.774 0 28  LYS III CB  1 ? 12 
ATOM 10408 C CG  . LYS I 5 28  ? 5.911   74.997  20.181 1.000 270.473 0 28  LYS III CG  1 ? 12 
ATOM 10409 C CD  . LYS I 5 28  ? 5.184   73.925  20.983 1.000 261.005 0 28  LYS III CD  1 ? 12 
ATOM 10410 C CE  . LYS I 5 28  ? 4.345   73.019  20.096 1.000 265.198 0 28  LYS III CE  1 ? 12 
ATOM 10411 N NZ  . LYS I 5 28  ? 5.139   72.350  19.040 1.000 261.526 0 28  LYS III NZ  1 ? 12 
ATOM 10412 N N   . VAL I 5 29  ? 6.331   78.845  22.734 1.000 272.342 0 29  VAL III N   1 ? 12 
ATOM 10413 C CA  . VAL I 5 29  ? 7.007   79.783  23.630 1.000 261.852 0 29  VAL III CA  1 ? 12 
ATOM 10414 C C   . VAL I 5 29  ? 6.225   81.094  23.677 1.000 263.634 0 29  VAL III C   1 ? 12 
ATOM 10415 O O   . VAL I 5 29  ? 6.655   82.099  23.092 1.000 256.293 0 29  VAL III O   1 ? 12 
ATOM 10416 C CB  . VAL I 5 29  ? 8.475   79.995  23.214 1.000 245.120 0 29  VAL III CB  1 ? 12 
ATOM 10417 C CG1 . VAL I 5 29  ? 9.322   78.804  23.640 1.000 237.978 0 29  VAL III CG1 1 ? 12 
ATOM 10418 C CG2 . VAL I 5 29  ? 8.592   80.181  21.704 1.000 253.331 0 29  VAL III CG2 1 ? 12 
ATOM 10419 N N   . PRO I 5 30  ? 5.082   81.137  24.372 1.000 272.569 0 30  PRO III N   1 ? 12 
ATOM 10420 C CA  . PRO I 5 30  ? 4.313   82.393  24.412 1.000 275.810 0 30  PRO III CA  1 ? 12 
ATOM 10421 C C   . PRO I 5 30  ? 5.011   83.496  25.184 1.000 268.598 0 30  PRO III C   1 ? 12 
ATOM 10422 O O   . PRO I 5 30  ? 4.975   84.658  24.758 1.000 263.290 0 30  PRO III O   1 ? 12 
ATOM 10423 C CB  . PRO I 5 30  ? 2.991   81.980  25.076 1.000 289.392 0 30  PRO III CB  1 ? 12 
ATOM 10424 C CG  . PRO I 5 30  ? 3.308   80.742  25.836 1.000 292.301 0 30  PRO III CG  1 ? 12 
ATOM 10425 C CD  . PRO I 5 30  ? 4.404   80.042  25.086 1.000 283.100 0 30  PRO III CD  1 ? 12 
ATOM 10426 N N   . LYS I 5 31  ? 5.638   83.167  26.319 1.000 265.706 0 31  LYS III N   1 ? 12 
ATOM 10427 C CA  . LYS I 5 31  ? 6.296   84.188  27.127 1.000 256.060 0 31  LYS III CA  1 ? 12 
ATOM 10428 C C   . LYS I 5 31  ? 7.389   84.890  26.334 1.000 251.355 0 31  LYS III C   1 ? 12 
ATOM 10429 O O   . LYS I 5 31  ? 7.511   86.120  26.386 1.000 256.911 0 31  LYS III O   1 ? 12 
ATOM 10430 C CB  . LYS I 5 31  ? 6.865   83.557  28.397 1.000 252.568 0 31  LYS III CB  1 ? 12 
ATOM 10431 C CG  . LYS I 5 31  ? 7.469   84.543  29.374 1.000 251.408 0 31  LYS III CG  1 ? 12 
ATOM 10432 C CD  . LYS I 5 31  ? 7.753   83.868  30.703 1.000 256.738 0 31  LYS III CD  1 ? 12 
ATOM 10433 C CE  . LYS I 5 31  ? 8.330   84.845  31.703 1.000 257.123 0 31  LYS III CE  1 ? 12 
ATOM 10434 N NZ  . LYS I 5 31  ? 9.731   85.189  31.365 1.000 270.209 0 31  LYS III NZ  1 ? 12 
ATOM 10435 N N   . THR I 5 32  ? 8.192   84.126  25.589 1.000 253.858 0 32  THR III N   1 ? 12 
ATOM 10436 C CA  . THR I 5 32  ? 9.278   84.733  24.828 1.000 236.333 0 32  THR III CA  1 ? 12 
ATOM 10437 C C   . THR I 5 32  ? 8.713   85.511  23.648 1.000 239.018 0 32  THR III C   1 ? 12 
ATOM 10438 O O   . THR I 5 32  ? 9.192   86.604  23.322 1.000 235.994 0 32  THR III O   1 ? 12 
ATOM 10439 C CB  . THR I 5 32  ? 10.260  83.659  24.357 1.000 224.937 0 32  THR III CB  1 ? 12 
ATOM 10440 O OG1 . THR I 5 32  ? 10.694  82.880  25.479 1.000 228.830 0 32  THR III OG1 1 ? 12 
ATOM 10441 C CG2 . THR I 5 32  ? 11.471  84.295  23.694 1.000 218.543 0 32  THR III CG2 1 ? 12 
ATOM 10442 N N   . ALA I 5 33  ? 7.692   84.949  22.997 1.000 240.692 0 33  ALA III N   1 ? 12 
ATOM 10443 C CA  . ALA I 5 33  ? 7.008   85.638  21.909 1.000 244.554 0 33  ALA III CA  1 ? 12 
ATOM 10444 C C   . ALA I 5 33  ? 6.373   86.936  22.392 1.000 256.790 0 33  ALA III C   1 ? 12 
ATOM 10445 O O   . ALA I 5 33  ? 6.469   87.970  21.721 1.000 257.213 0 33  ALA III O   1 ? 12 
ATOM 10446 C CB  . ALA I 5 33  ? 5.952   84.727  21.285 1.000 251.056 0 33  ALA III CB  1 ? 12 
ATOM 10447 N N   . GLU I 5 34  ? 5.705   86.896  23.549 1.000 265.925 0 34  GLU III N   1 ? 12 
ATOM 10448 C CA  . GLU I 5 34  ? 5.009   88.081  24.041 1.000 276.652 0 34  GLU III CA  1 ? 12 
ATOM 10449 C C   . GLU I 5 34  ? 5.962   89.238  24.321 1.000 278.349 0 34  GLU III C   1 ? 12 
ATOM 10450 O O   . GLU I 5 34  ? 5.626   90.396  24.047 1.000 299.823 0 34  GLU III O   1 ? 12 
ATOM 10451 C CB  . GLU I 5 34  ? 4.211   87.727  25.296 1.000 282.188 0 34  GLU III CB  1 ? 12 
ATOM 10452 C CG  . GLU I 5 34  ? 3.522   88.911  25.951 1.000 296.184 0 34  GLU III CG  1 ? 12 
ATOM 10453 C CD  . GLU I 5 34  ? 2.471   89.543  25.059 1.000 312.876 0 34  GLU III CD  1 ? 12 
ATOM 10454 O OE1 . GLU I 5 34  ? 1.557   88.826  24.603 1.000 327.562 0 34  GLU III OE1 1 ? 12 
ATOM 10455 O OE2 . GLU I 5 34  ? 2.555   90.767  24.824 1.000 318.833 0 34  GLU III OE2 1 ? 12 
ATOM 10456 N N   . ASN I 5 35  ? 7.137   88.961  24.892 1.000 268.061 0 35  ASN III N   1 ? 12 
ATOM 10457 C CA  . ASN I 5 35  ? 8.123   90.024  25.084 1.000 261.811 0 35  ASN III CA  1 ? 12 
ATOM 10458 C C   . ASN I 5 35  ? 8.460   90.708  23.769 1.000 255.357 0 35  ASN III C   1 ? 12 
ATOM 10459 O O   . ASN I 5 35  ? 8.409   91.938  23.654 1.000 252.981 0 35  ASN III O   1 ? 12 
ATOM 10460 C CB  . ASN I 5 35  ? 9.415   89.516  25.707 1.000 257.812 0 35  ASN III CB  1 ? 12 
ATOM 10461 C CG  . ASN I 5 35  ? 10.395  90.655  25.938 1.000 253.967 0 35  ASN III CG  1 ? 12 
ATOM 10462 O OD1 . ASN I 5 35  ? 9.984   91.805  26.042 1.000 254.641 0 35  ASN III OD1 1 ? 12 
ATOM 10463 N ND2 . ASN I 5 35  ? 11.681  90.365  25.908 1.000 256.361 0 35  ASN III ND2 1 ? 12 
ATOM 10464 N N   . PHE I 5 36  ? 8.803   89.910  22.758 1.000 256.978 0 36  PHE III N   1 ? 12 
ATOM 10465 C CA  . PHE I 5 36  ? 9.170   90.456  21.462 1.000 252.686 0 36  PHE III CA  1 ? 12 
ATOM 10466 C C   . PHE I 5 36  ? 8.002   91.213  20.848 1.000 257.007 0 36  PHE III C   1 ? 12 
ATOM 10467 O O   . PHE I 5 36  ? 8.193   92.286  20.265 1.000 255.295 0 36  PHE III O   1 ? 12 
ATOM 10468 C CB  . PHE I 5 36  ? 9.631   89.319  20.555 1.000 246.865 0 36  PHE III CB  1 ? 12 
ATOM 10469 C CG  . PHE I 5 36  ? 10.323  89.777  19.319 1.000 241.040 0 36  PHE III CG  1 ? 12 
ATOM 10470 C CD1 . PHE I 5 36  ? 11.699  89.938  19.298 1.000 224.814 0 36  PHE III CD1 1 ? 12 
ATOM 10471 C CD2 . PHE I 5 36  ? 9.596   90.104  18.196 1.000 253.532 0 36  PHE III CD2 1 ? 12 
ATOM 10472 C CE1 . PHE I 5 36  ? 12.337  90.367  18.156 1.000 224.108 0 36  PHE III CE1 1 ? 12 
ATOM 10473 C CE2 . PHE I 5 36  ? 10.223  90.546  17.065 1.000 252.233 0 36  PHE III CE2 1 ? 12 
ATOM 10474 C CZ  . PHE I 5 36  ? 11.595  90.676  17.038 1.000 234.721 0 36  PHE III CZ  1 ? 12 
ATOM 10475 N N   . ARG I 5 37  ? 6.785   90.675  20.963 1.000 258.269 0 37  ARG III N   1 ? 12 
ATOM 10476 C CA  . ARG I 5 37  ? 5.634   91.380  20.413 1.000 262.118 0 37  ARG III CA  1 ? 12 
ATOM 10477 C C   . ARG I 5 37  ? 5.506   92.756  21.052 1.000 268.412 0 37  ARG III C   1 ? 12 
ATOM 10478 O O   . ARG I 5 37  ? 5.374   93.766  20.352 1.000 260.936 0 37  ARG III O   1 ? 12 
ATOM 10479 C CB  . ARG I 5 37  ? 4.359   90.568  20.625 1.000 267.610 0 37  ARG III CB  1 ? 12 
ATOM 10480 C CG  . ARG I 5 37  ? 3.161   91.126  19.892 1.000 263.938 0 37  ARG III CG  1 ? 12 
ATOM 10481 C CD  . ARG I 5 37  ? 2.230   91.805  20.871 1.000 270.163 0 37  ARG III CD  1 ? 12 
ATOM 10482 N NE  . ARG I 5 37  ? 1.432   90.828  21.599 1.000 274.460 0 37  ARG III NE  1 ? 12 
ATOM 10483 C CZ  . ARG I 5 37  ? 0.579   91.135  22.564 1.000 280.953 0 37  ARG III CZ  1 ? 12 
ATOM 10484 N NH1 . ARG I 5 37  ? 0.348   92.392  22.905 1.000 288.924 0 37  ARG III NH1 1 ? 12 
ATOM 10485 N NH2 . ARG I 5 37  ? -0.067  90.159  23.194 1.000 288.044 0 37  ARG III NH2 1 ? 12 
ATOM 10486 N N   . ALA I 5 38  ? 5.549   92.818  22.389 1.000 282.419 0 38  ALA III N   1 ? 12 
ATOM 10487 C CA  . ALA I 5 38  ? 5.366   94.105  23.052 1.000 289.263 0 38  ALA III CA  1 ? 12 
ATOM 10488 C C   . ALA I 5 38  ? 6.550   95.027  22.782 1.000 279.610 0 38  ALA III C   1 ? 12 
ATOM 10489 O O   . ALA I 5 38  ? 6.374   96.243  22.640 1.000 296.005 0 38  ALA III O   1 ? 12 
ATOM 10490 C CB  . ALA I 5 38  ? 5.167   93.906  24.555 1.000 302.457 0 38  ALA III CB  1 ? 12 
ATOM 10491 N N   . LEU I 5 39  ? 7.766   94.474  22.726 1.000 265.313 0 39  LEU III N   1 ? 12 
ATOM 10492 C CA  . LEU I 5 39  ? 8.913   95.301  22.367 1.000 244.468 0 39  LEU III CA  1 ? 12 
ATOM 10493 C C   . LEU I 5 39  ? 8.833   95.771  20.918 1.000 247.572 0 39  LEU III C   1 ? 12 
ATOM 10494 O O   . LEU I 5 39  ? 9.350   96.841  20.584 1.000 238.441 0 39  LEU III O   1 ? 12 
ATOM 10495 C CB  . LEU I 5 39  ? 10.215  94.533  22.594 1.000 225.066 0 39  LEU III CB  1 ? 12 
ATOM 10496 C CG  . LEU I 5 39  ? 10.625  94.162  24.017 1.000 221.503 0 39  LEU III CG  1 ? 12 
ATOM 10497 C CD1 . LEU I 5 39  ? 11.867  93.295  23.972 1.000 214.840 0 39  LEU III CD1 1 ? 12 
ATOM 10498 C CD2 . LEU I 5 39  ? 10.875  95.402  24.855 1.000 223.419 0 39  LEU III CD2 1 ? 12 
ATOM 10499 N N   . SER I 5 40  ? 8.202   94.985  20.044 1.000 251.690 0 40  SER III N   1 ? 12 
ATOM 10500 C CA  . SER I 5 40  ? 8.062   95.362  18.641 1.000 247.653 0 40  SER III CA  1 ? 12 
ATOM 10501 C C   . SER I 5 40  ? 6.972   96.402  18.415 1.000 261.245 0 40  SER III C   1 ? 12 
ATOM 10502 O O   . SER I 5 40  ? 7.084   97.227  17.503 1.000 262.031 0 40  SER III O   1 ? 12 
ATOM 10503 C CB  . SER I 5 40  ? 7.777   94.127  17.792 1.000 240.207 0 40  SER III CB  1 ? 12 
ATOM 10504 O OG  . SER I 5 40  ? 8.871   93.231  17.846 1.000 243.152 0 40  SER III OG  1 ? 12 
ATOM 10505 N N   . THR I 5 41  ? 5.934   96.400  19.243 1.000 270.423 0 41  THR III N   1 ? 12 
ATOM 10506 C CA  . THR I 5 41  ? 4.844   97.354  19.110 1.000 266.050 0 41  THR III CA  1 ? 12 
ATOM 10507 C C   . THR I 5 41  ? 5.064   98.616  19.925 1.000 278.663 0 41  THR III C   1 ? 12 
ATOM 10508 O O   . THR I 5 41  ? 4.450   99.647  19.628 1.000 285.788 0 41  THR III O   1 ? 12 
ATOM 10509 C CB  . THR I 5 41  ? 3.514   96.709  19.528 1.000 271.233 0 41  THR III CB  1 ? 12 
ATOM 10510 O OG1 . THR I 5 41  ? 3.558   96.365  20.918 1.000 278.371 0 41  THR III OG1 1 ? 12 
ATOM 10511 C CG2 . THR I 5 41  ? 3.240   95.450  18.717 1.000 267.500 0 41  THR III CG2 1 ? 12 
ATOM 10512 N N   . GLY I 5 42  ? 5.923   98.557  20.938 1.000 281.168 0 42  GLY III N   1 ? 12 
ATOM 10513 C CA  . GLY I 5 42  ? 6.173   99.708  21.773 1.000 286.409 0 42  GLY III CA  1 ? 12 
ATOM 10514 C C   . GLY I 5 42  ? 5.041   99.987  22.721 1.000 300.025 0 42  GLY III C   1 ? 12 
ATOM 10515 O O   . GLY I 5 42  ? 4.935   101.097 23.252 1.000 309.509 0 42  GLY III O   1 ? 12 
ATOM 10516 N N   . GLU I 5 43  ? 4.166   98.999  22.926 1.000 293.243 0 43  GLU III N   1 ? 12 
ATOM 10517 C CA  . GLU I 5 43  ? 2.955   99.201  23.702 1.000 289.620 0 43  GLU III CA  1 ? 12 
ATOM 10518 C C   . GLU I 5 43  ? 3.265   99.432  25.172 1.000 285.318 0 43  GLU III C   1 ? 12 
ATOM 10519 O O   . GLU I 5 43  ? 2.426   99.977  25.894 1.000 308.732 0 43  GLU III O   1 ? 12 
ATOM 10520 C CB  . GLU I 5 43  ? 2.060   97.970  23.553 1.000 292.942 0 43  GLU III CB  1 ? 12 
ATOM 10521 C CG  . GLU I 5 43  ? 2.635   96.756  24.297 1.000 289.299 0 43  GLU III CG  1 ? 12 
ATOM 10522 C CD  . GLU I 5 43  ? 1.988   95.441  23.914 1.000 293.118 0 43  GLU III CD  1 ? 12 
ATOM 10523 O OE1 . GLU I 5 43  ? 1.958   95.122  22.707 1.000 293.046 0 43  GLU III OE1 1 ? 12 
ATOM 10524 O OE2 . GLU I 5 43  ? 1.518   94.724  24.823 1.000 294.827 0 43  GLU III OE2 1 ? 12 
ATOM 10525 N N   . LYS I 5 44  ? 4.452   99.024  25.627 1.000 267.177 0 44  LYS III N   1 ? 12 
ATOM 10526 C CA  . LYS I 5 44  ? 4.916   99.289  26.980 1.000 260.264 0 44  LYS III CA  1 ? 12 
ATOM 10527 C C   . LYS I 5 44  ? 5.626   100.629 27.121 1.000 249.913 0 44  LYS III C   1 ? 12 
ATOM 10528 O O   . LYS I 5 44  ? 6.015   100.994 28.237 1.000 243.151 0 44  LYS III O   1 ? 12 
ATOM 10529 C CB  . LYS I 5 44  ? 5.884   98.181  27.410 1.000 255.436 0 44  LYS III CB  1 ? 12 
ATOM 10530 C CG  . LYS I 5 44  ? 5.322   96.768  27.363 1.000 260.407 0 44  LYS III CG  1 ? 12 
ATOM 10531 C CD  . LYS I 5 44  ? 4.232   96.516  28.378 1.000 266.950 0 44  LYS III CD  1 ? 12 
ATOM 10532 C CE  . LYS I 5 44  ? 3.552   95.195  28.072 1.000 267.823 0 44  LYS III CE  1 ? 12 
ATOM 10533 N NZ  . LYS I 5 44  ? 2.266   95.049  28.797 1.000 282.089 0 44  LYS III NZ  1 ? 12 
ATOM 10534 N N   . GLY I 5 45  ? 5.798   101.375 26.036 1.000 244.044 0 45  GLY III N   1 ? 12 
ATOM 10535 C CA  . GLY I 5 45  ? 6.420   102.677 26.113 1.000 240.805 0 45  GLY III CA  1 ? 12 
ATOM 10536 C C   . GLY I 5 45  ? 7.852   102.681 25.627 1.000 246.299 0 45  GLY III C   1 ? 12 
ATOM 10537 O O   . GLY I 5 45  ? 8.472   103.753 25.592 1.000 244.604 0 45  GLY III O   1 ? 12 
ATOM 10538 N N   . PHE I 5 46  ? 8.380   101.518 25.233 1.000 247.451 0 46  PHE III N   1 ? 12 
ATOM 10539 C CA  . PHE I 5 46  ? 9.707   101.405 24.666 1.000 241.115 0 46  PHE III CA  1 ? 12 
ATOM 10540 C C   . PHE I 5 46  ? 9.697   100.211 23.707 1.000 235.960 0 46  PHE III C   1 ? 12 
ATOM 10541 O O   . PHE I 5 46  ? 9.107   99.174  24.061 1.000 240.445 0 46  PHE III O   1 ? 12 
ATOM 10542 C CB  . PHE I 5 46  ? 10.699  101.244 25.859 1.000 234.102 0 46  PHE III CB  1 ? 12 
ATOM 10543 C CG  . PHE I 5 46  ? 10.349  100.076 26.818 1.000 233.741 0 46  PHE III CG  1 ? 12 
ATOM 10544 C CD1 . PHE I 5 46  ? 10.807  98.782  26.611 1.000 225.692 0 46  PHE III CD1 1 ? 12 
ATOM 10545 C CD2 . PHE I 5 46  ? 9.517   100.303 27.922 1.000 241.315 0 46  PHE III CD2 1 ? 12 
ATOM 10546 C CE1 . PHE I 5 46  ? 10.467  97.744  27.491 1.000 218.003 0 46  PHE III CE1 1 ? 12 
ATOM 10547 C CE2 . PHE I 5 46  ? 9.171   99.268  28.796 1.000 238.586 0 46  PHE III CE2 1 ? 12 
ATOM 10548 C CZ  . PHE I 5 46  ? 9.649   97.991  28.578 1.000 226.106 0 46  PHE III CZ  1 ? 12 
ATOM 10549 N N   . GLY I 5 47  ? 10.720  100.143 22.856 1.000 227.995 0 47  GLY III N   1 ? 12 
ATOM 10550 C CA  . GLY I 5 47  ? 10.756  99.082  21.871 1.000 220.636 0 47  GLY III CA  1 ? 12 
ATOM 10551 C C   . GLY I 5 47  ? 11.791  99.234  20.773 1.000 207.737 0 47  GLY III C   1 ? 12 
ATOM 10552 O O   . GLY I 5 47  ? 12.736  100.012 20.919 1.000 200.232 0 47  GLY III O   1 ? 12 
ATOM 10553 N N   . TYR I 5 48  ? 11.620  98.462  19.688 1.000 199.019 0 48  TYR III N   1 ? 12 
ATOM 10554 C CA  . TYR I 5 48  ? 12.706  98.280  18.725 1.000 191.579 0 48  TYR III CA  1 ? 12 
ATOM 10555 C C   . TYR I 5 48  ? 12.878  99.398  17.711 1.000 196.434 0 48  TYR III C   1 ? 12 
ATOM 10556 O O   . TYR I 5 48  ? 13.949  99.487  17.104 1.000 197.341 0 48  TYR III O   1 ? 12 
ATOM 10557 C CB  . TYR I 5 48  ? 12.547  96.946  17.980 1.000 187.657 0 48  TYR III CB  1 ? 12 
ATOM 10558 C CG  . TYR I 5 48  ? 12.741  95.710  18.831 1.000 182.313 0 48  TYR III CG  1 ? 12 
ATOM 10559 C CD1 . TYR I 5 48  ? 13.801  95.618  19.724 1.000 176.256 0 48  TYR III CD1 1 ? 12 
ATOM 10560 C CD2 . TYR I 5 48  ? 11.924  94.600  18.671 1.000 190.379 0 48  TYR III CD2 1 ? 12 
ATOM 10561 C CE1 . TYR I 5 48  ? 13.998  94.480  20.493 1.000 177.986 0 48  TYR III CE1 1 ? 12 
ATOM 10562 C CE2 . TYR I 5 48  ? 12.118  93.457  19.423 1.000 190.438 0 48  TYR III CE2 1 ? 12 
ATOM 10563 C CZ  . TYR I 5 48  ? 13.158  93.401  20.332 1.000 183.789 0 48  TYR III CZ  1 ? 12 
ATOM 10564 O OH  . TYR I 5 48  ? 13.353  92.262  21.081 1.000 194.000 0 48  TYR III OH  1 ? 12 
ATOM 10565 N N   . LYS I 5 49  ? 11.865  100.231 17.476 1.000 201.804 0 49  LYS III N   1 ? 12 
ATOM 10566 C CA  . LYS I 5 49  ? 11.976  101.246 16.430 1.000 202.575 0 49  LYS III CA  1 ? 12 
ATOM 10567 C C   . LYS I 5 49  ? 13.153  102.176 16.724 1.000 199.402 0 49  LYS III C   1 ? 12 
ATOM 10568 O O   . LYS I 5 49  ? 13.271  102.720 17.825 1.000 198.114 0 49  LYS III O   1 ? 12 
ATOM 10569 C CB  . LYS I 5 49  ? 10.666  102.008 16.233 1.000 207.361 0 49  LYS III CB  1 ? 12 
ATOM 10570 C CG  . LYS I 5 49  ? 9.413   101.195 16.516 1.000 220.219 0 49  LYS III CG  1 ? 12 
ATOM 10571 C CD  . LYS I 5 49  ? 8.190   102.077 16.385 1.000 231.782 0 49  LYS III CD  1 ? 12 
ATOM 10572 C CE  . LYS I 5 49  ? 7.450   101.744 15.099 1.000 239.898 0 49  LYS III CE  1 ? 12 
ATOM 10573 N NZ  . LYS I 5 49  ? 6.211   102.547 14.904 1.000 246.483 0 49  LYS III NZ  1 ? 12 
ATOM 10574 N N   . GLY I 5 50  ? 14.042  102.339 15.743 1.000 201.225 0 50  GLY III N   1 ? 12 
ATOM 10575 C CA  . GLY I 5 50  ? 15.217  103.164 15.925 1.000 204.685 0 50  GLY III CA  1 ? 12 
ATOM 10576 C C   . GLY I 5 50  ? 16.446  102.433 16.435 1.000 206.590 0 50  GLY III C   1 ? 12 
ATOM 10577 O O   . GLY I 5 50  ? 17.502  103.065 16.579 1.000 204.491 0 50  GLY III O   1 ? 12 
ATOM 10578 N N   . SER I 5 51  ? 16.350  101.132 16.709 1.000 210.459 0 51  SER III N   1 ? 12 
ATOM 10579 C CA  . SER I 5 51  ? 17.461  100.382 17.270 1.000 205.772 0 51  SER III CA  1 ? 12 
ATOM 10580 C C   . SER I 5 51  ? 18.347  99.930  16.119 1.000 198.489 0 51  SER III C   1 ? 12 
ATOM 10581 O O   . SER I 5 51  ? 17.952  99.981  14.950 1.000 195.022 0 51  SER III O   1 ? 12 
ATOM 10582 C CB  . SER I 5 51  ? 16.976  99.166  18.060 1.000 210.424 0 51  SER III CB  1 ? 12 
ATOM 10583 O OG  . SER I 5 51  ? 16.014  98.425  17.331 1.000 202.364 0 51  SER III OG  1 ? 12 
ATOM 10584 N N   . CYS I 5 52  ? 19.551  99.475  16.446 1.000 191.958 0 52  CYS III N   1 ? 12 
ATOM 10585 C CA  . CYS I 5 52  ? 20.505  99.110  15.413 1.000 182.137 0 52  CYS III CA  1 ? 12 
ATOM 10586 C C   . CYS I 5 52  ? 20.771  97.613  15.403 1.000 172.310 0 52  CYS III C   1 ? 12 
ATOM 10587 O O   . CYS I 5 52  ? 20.503  96.900  16.373 1.000 171.889 0 52  CYS III O   1 ? 12 
ATOM 10588 C CB  . CYS I 5 52  ? 21.835  99.849  15.632 1.000 174.107 0 52  CYS III CB  1 ? 12 
ATOM 10589 S SG  . CYS I 5 52  ? 21.864  101.596 15.169 1.000 194.042 0 52  CYS III SG  1 ? 12 
ATOM 10590 N N   . PHE I 5 53  ? 21.312  97.146  14.278 1.000 161.461 0 53  PHE III N   1 ? 12 
ATOM 10591 C CA  . PHE I 5 53  ? 21.922  95.825  14.199 1.000 149.924 0 53  PHE III CA  1 ? 12 
ATOM 10592 C C   . PHE I 5 53  ? 23.398  95.989  14.521 1.000 153.889 0 53  PHE III C   1 ? 12 
ATOM 10593 O O   . PHE I 5 53  ? 24.160  96.543  13.722 1.000 160.859 0 53  PHE III O   1 ? 12 
ATOM 10594 C CB  . PHE I 5 53  ? 21.710  95.180  12.832 1.000 145.395 0 53  PHE III CB  1 ? 12 
ATOM 10595 C CG  . PHE I 5 53  ? 20.342  94.590  12.655 1.000 145.910 0 53  PHE III CG  1 ? 12 
ATOM 10596 C CD1 . PHE I 5 53  ? 19.276  95.386  12.278 1.000 147.546 0 53  PHE III CD1 1 ? 12 
ATOM 10597 C CD2 . PHE I 5 53  ? 20.117  93.241  12.888 1.000 138.713 0 53  PHE III CD2 1 ? 12 
ATOM 10598 C CE1 . PHE I 5 53  ? 18.014  94.851  12.122 1.000 139.540 0 53  PHE III CE1 1 ? 12 
ATOM 10599 C CE2 . PHE I 5 53  ? 18.854  92.700  12.737 1.000 134.594 0 53  PHE III CE2 1 ? 12 
ATOM 10600 C CZ  . PHE I 5 53  ? 17.802  93.507  12.353 1.000 137.334 0 53  PHE III CZ  1 ? 12 
ATOM 10601 N N   . HIS I 5 54  ? 23.797  95.517  15.695 1.000 149.647 0 54  HIS III N   1 ? 12 
ATOM 10602 C CA  . HIS I 5 54  ? 25.146  95.755  16.183 1.000 148.586 0 54  HIS III CA  1 ? 12 
ATOM 10603 C C   . HIS I 5 54  ? 26.128  94.681  15.734 1.000 144.997 0 54  HIS III C   1 ? 12 
ATOM 10604 O O   . HIS I 5 54  ? 27.323  94.966  15.592 1.000 142.098 0 54  HIS III O   1 ? 12 
ATOM 10605 C CB  . HIS I 5 54  ? 25.113  95.890  17.712 1.000 157.521 0 54  HIS III CB  1 ? 12 
ATOM 10606 C CG  . HIS I 5 54  ? 24.717  94.636  18.430 1.000 157.650 0 54  HIS III CG  1 ? 12 
ATOM 10607 N ND1 . HIS I 5 54  ? 23.400  94.286  18.637 1.000 157.322 0 54  HIS III ND1 1 ? 12 
ATOM 10608 C CD2 . HIS I 5 54  ? 25.461  93.668  19.015 1.000 156.225 0 54  HIS III CD2 1 ? 12 
ATOM 10609 C CE1 . HIS I 5 54  ? 23.349  93.146  19.303 1.000 161.542 0 54  HIS III CE1 1 ? 12 
ATOM 10610 N NE2 . HIS I 5 54  ? 24.586  92.750  19.545 1.000 156.819 0 54  HIS III NE2 1 ? 12 
ATOM 10611 N N   . ARG I 5 55  ? 25.654  93.461  15.491 1.000 144.885 0 55  ARG III N   1 ? 12 
ATOM 10612 C CA  . ARG I 5 55  ? 26.483  92.385  14.955 1.000 135.068 0 55  ARG III CA  1 ? 12 
ATOM 10613 C C   . ARG I 5 55  ? 25.803  91.796  13.729 1.000 127.279 0 55  ARG III C   1 ? 12 
ATOM 10614 O O   . ARG I 5 55  ? 24.747  91.164  13.844 1.000 125.363 0 55  ARG III O   1 ? 12 
ATOM 10615 C CB  . ARG I 5 55  ? 26.749  91.295  15.993 1.000 131.508 0 55  ARG III CB  1 ? 12 
ATOM 10616 C CG  . ARG I 5 55  ? 28.042  91.477  16.769 1.000 127.385 0 55  ARG III CG  1 ? 12 
ATOM 10617 C CD  . ARG I 5 55  ? 28.191  90.412  17.842 1.000 133.409 0 55  ARG III CD  1 ? 12 
ATOM 10618 N NE  . ARG I 5 55  ? 28.354  89.083  17.263 1.000 125.602 0 55  ARG III NE  1 ? 12 
ATOM 10619 C CZ  . ARG I 5 55  ? 28.458  87.964  17.968 1.000 132.373 0 55  ARG III CZ  1 ? 12 
ATOM 10620 N NH1 . ARG I 5 55  ? 28.411  87.971  19.290 1.000 152.949 0 55  ARG III NH1 1 ? 12 
ATOM 10621 N NH2 . ARG I 5 55  ? 28.615  86.808  17.330 1.000 134.931 0 55  ARG III NH2 1 ? 12 
ATOM 10622 N N   . ILE I 5 56  ? 26.401  91.994  12.559 1.000 124.202 0 56  ILE III N   1 ? 12 
ATOM 10623 C CA  . ILE I 5 56  ? 25.995  91.273  11.365 1.000 124.048 0 56  ILE III CA  1 ? 12 
ATOM 10624 C C   . ILE I 5 56  ? 27.203  90.480  10.901 1.000 126.489 0 56  ILE III C   1 ? 12 
ATOM 10625 O O   . ILE I 5 56  ? 28.237  91.058  10.538 1.000 132.524 0 56  ILE III O   1 ? 12 
ATOM 10626 C CB  . ILE I 5 56  ? 25.504  92.220  10.260 1.000 126.436 0 56  ILE III CB  1 ? 12 
ATOM 10627 C CG1 . ILE I 5 56  ? 24.262  92.980  10.722 1.000 129.484 0 56  ILE III CG1 1 ? 12 
ATOM 10628 C CG2 . ILE I 5 56  ? 25.221  91.447  8.991  1.000 131.669 0 56  ILE III CG2 1 ? 12 
ATOM 10629 C CD1 . ILE I 5 56  ? 23.689  93.882  9.658  1.000 129.877 0 56  ILE III CD1 1 ? 12 
ATOM 10630 N N   . ILE I 5 57  ? 27.068  89.160  10.916 1.000 126.231 0 57  ILE III N   1 ? 12 
ATOM 10631 C CA  . ILE I 5 57  ? 28.124  88.240  10.512 1.000 122.680 0 57  ILE III CA  1 ? 12 
ATOM 10632 C C   . ILE I 5 57  ? 27.640  87.392  9.344  1.000 115.059 0 57  ILE III C   1 ? 12 
ATOM 10633 O O   . ILE I 5 57  ? 26.760  86.541  9.536  1.000 108.960 0 57  ILE III O   1 ? 12 
ATOM 10634 C CB  . ILE I 5 57  ? 28.584  87.371  11.691 1.000 123.253 0 57  ILE III CB  1 ? 12 
ATOM 10635 C CG1 . ILE I 5 57  ? 29.082  88.260  12.828 1.000 120.513 0 57  ILE III CG1 1 ? 12 
ATOM 10636 C CG2 . ILE I 5 57  ? 29.676  86.424  11.257 1.000 126.835 0 57  ILE III CG2 1 ? 12 
ATOM 10637 C CD1 . ILE I 5 57  ? 29.383  87.511  14.094 1.000 132.671 0 57  ILE III CD1 1 ? 12 
ATOM 10638 N N   . PRO I 5 58  ? 28.152  87.592  8.134  1.000 115.950 0 58  PRO III N   1 ? 12 
ATOM 10639 C CA  . PRO I 5 58  ? 27.626  86.842  6.987  1.000 119.280 0 58  PRO III CA  1 ? 12 
ATOM 10640 C C   . PRO I 5 58  ? 27.838  85.346  7.176  1.000 120.059 0 58  PRO III C   1 ? 12 
ATOM 10641 O O   . PRO I 5 58  ? 28.893  84.899  7.630  1.000 123.339 0 58  PRO III O   1 ? 12 
ATOM 10642 C CB  . PRO I 5 58  ? 28.441  87.385  5.806  1.000 124.928 0 58  PRO III CB  1 ? 12 
ATOM 10643 C CG  . PRO I 5 58  ? 29.681  87.963  6.438  1.000 124.685 0 58  PRO III CG  1 ? 12 
ATOM 10644 C CD  . PRO I 5 58  ? 29.221  88.524  7.742  1.000 120.865 0 58  PRO III CD  1 ? 12 
ATOM 10645 N N   . GLY I 5 59  ? 26.820  84.570  6.810  1.000 121.860 0 59  GLY III N   1 ? 12 
ATOM 10646 C CA  . GLY I 5 59  ? 26.872  83.134  6.966  1.000 125.489 0 59  GLY III CA  1 ? 12 
ATOM 10647 C C   . GLY I 5 59  ? 26.572  82.652  8.368  1.000 125.786 0 59  GLY III C   1 ? 12 
ATOM 10648 O O   . GLY I 5 59  ? 26.680  81.446  8.628  1.000 124.642 0 59  GLY III O   1 ? 12 
ATOM 10649 N N   . PHE I 5 60  ? 26.199  83.555  9.275  1.000 121.659 0 60  PHE III N   1 ? 12 
ATOM 10650 C CA  . PHE I 5 60  ? 25.960  83.221  10.674 1.000 129.716 0 60  PHE III CA  1 ? 12 
ATOM 10651 C C   . PHE I 5 60  ? 24.602  83.736  11.129 1.000 130.240 0 60  PHE III C   1 ? 12 
ATOM 10652 O O   . PHE I 5 60  ? 23.637  82.968  11.213 1.000 138.025 0 60  PHE III O   1 ? 12 
ATOM 10653 C CB  . PHE I 5 60  ? 27.072  83.801  11.554 1.000 138.412 0 60  PHE III CB  1 ? 12 
ATOM 10654 C CG  . PHE I 5 60  ? 26.998  83.373  12.996 1.000 139.322 0 60  PHE III CG  1 ? 12 
ATOM 10655 C CD1 . PHE I 5 60  ? 26.441  82.154  13.346 1.000 147.304 0 60  PHE III CD1 1 ? 12 
ATOM 10656 C CD2 . PHE I 5 60  ? 27.515  84.178  13.998 1.000 137.353 0 60  PHE III CD2 1 ? 12 
ATOM 10657 C CE1 . PHE I 5 60  ? 26.379  81.758  14.666 1.000 152.899 0 60  PHE III CE1 1 ? 12 
ATOM 10658 C CE2 . PHE I 5 60  ? 27.460  83.783  15.320 1.000 152.846 0 60  PHE III CE2 1 ? 12 
ATOM 10659 C CZ  . PHE I 5 60  ? 26.891  82.572  15.654 1.000 159.396 0 60  PHE III CZ  1 ? 12 
ATOM 10660 N N   . MET I 5 61  ? 24.522  85.029  11.427 1.000 126.979 0 61  MET III N   1 ? 12 
ATOM 10661 C CA  . MET I 5 61  ? 23.303  85.612  11.971 1.000 125.468 0 61  MET III CA  1 ? 12 
ATOM 10662 C C   . MET I 5 61  ? 23.388  87.128  11.860 1.000 122.791 0 61  MET III C   1 ? 12 
ATOM 10663 O O   . MET I 5 61  ? 24.450  87.696  11.592 1.000 122.328 0 61  MET III O   1 ? 12 
ATOM 10664 C CB  . MET I 5 61  ? 23.084  85.186  13.425 1.000 133.536 0 61  MET III CB  1 ? 12 
ATOM 10665 C CG  . MET I 5 61  ? 24.259  85.484  14.339 1.000 134.441 0 61  MET III CG  1 ? 12 
ATOM 10666 S SD  . MET I 5 61  ? 24.141  87.119  15.087 1.000 146.712 0 61  MET III SD  1 ? 12 
ATOM 10667 C CE  . MET I 5 61  ? 25.859  87.438  15.467 1.000 139.749 0 61  MET III CE  1 ? 12 
ATOM 10668 N N   . CYS I 5 62  ? 22.243  87.774  12.079 1.000 125.210 0 62  CYS III N   1 ? 12 
ATOM 10669 C CA  . CYS I 5 62  ? 22.138  89.222  12.205 1.000 128.239 0 62  CYS III CA  1 ? 12 
ATOM 10670 C C   . CYS I 5 62  ? 21.498  89.531  13.546 1.000 130.805 0 62  CYS III C   1 ? 12 
ATOM 10671 O O   . CYS I 5 62  ? 20.426  89.004  13.860 1.000 135.149 0 62  CYS III O   1 ? 12 
ATOM 10672 C CB  . CYS I 5 62  ? 21.300  89.831  11.083 1.000 133.821 0 62  CYS III CB  1 ? 12 
ATOM 10673 S SG  . CYS I 5 62  ? 21.977  89.584  9.440  1.000 145.187 0 62  CYS III SG  1 ? 12 
ATOM 10674 N N   . GLN I 5 63  ? 22.134  90.406  14.318 1.000 130.892 0 63  GLN III N   1 ? 12 
ATOM 10675 C CA  . GLN I 5 63  ? 21.726  90.650  15.691 1.000 131.310 0 63  GLN III CA  1 ? 12 
ATOM 10676 C C   . GLN I 5 63  ? 21.493  92.135  15.925 1.000 136.548 0 63  GLN III C   1 ? 12 
ATOM 10677 O O   . GLN I 5 63  ? 22.237  92.980  15.421 1.000 137.425 0 63  GLN III O   1 ? 12 
ATOM 10678 C CB  . GLN I 5 63  ? 22.794  90.115  16.660 1.000 138.006 0 63  GLN III CB  1 ? 12 
ATOM 10679 C CG  . GLN I 5 63  ? 22.339  89.947  18.099 1.000 144.806 0 63  GLN III CG  1 ? 12 
ATOM 10680 C CD  . GLN I 5 63  ? 23.489  89.640  19.050 1.000 140.278 0 63  GLN III CD  1 ? 12 
ATOM 10681 O OE1 . GLN I 5 63  ? 24.608  89.348  18.625 1.000 127.897 0 63  GLN III OE1 1 ? 12 
ATOM 10682 N NE2 . GLN I 5 63  ? 23.216  89.723  20.346 1.000 144.523 0 63  GLN III NE2 1 ? 12 
ATOM 10683 N N   . GLY I 5 64  ? 20.467  92.434  16.705 1.000 143.917 0 64  GLY III N   1 ? 12 
ATOM 10684 C CA  . GLY I 5 64  ? 20.103  93.794  17.024 1.000 155.096 0 64  GLY III CA  1 ? 12 
ATOM 10685 C C   . GLY I 5 64  ? 19.237  93.807  18.261 1.000 162.280 0 64  GLY III C   1 ? 12 
ATOM 10686 O O   . GLY I 5 64  ? 19.173  92.827  19.005 1.000 160.338 0 64  GLY III O   1 ? 12 
ATOM 10687 N N   . GLY I 5 65  ? 18.563  94.931  18.489 1.000 171.932 0 65  GLY III N   1 ? 12 
ATOM 10688 C CA  . GLY I 5 65  ? 17.627  94.997  19.591 1.000 178.532 0 65  GLY III CA  1 ? 12 
ATOM 10689 C C   . GLY I 5 65  ? 18.139  95.617  20.870 1.000 169.590 0 65  GLY III C   1 ? 12 
ATOM 10690 O O   . GLY I 5 65  ? 17.390  95.661  21.854 1.000 162.622 0 65  GLY III O   1 ? 12 
ATOM 10691 N N   . ASP I 5 66  ? 19.384  96.094  20.902 1.000 162.069 0 66  ASP III N   1 ? 12 
ATOM 10692 C CA  . ASP I 5 66  ? 19.915  96.735  22.107 1.000 171.363 0 66  ASP III CA  1 ? 12 
ATOM 10693 C C   . ASP I 5 66  ? 19.588  98.224  22.105 1.000 176.149 0 66  ASP III C   1 ? 12 
ATOM 10694 O O   . ASP I 5 66  ? 20.361  99.076  21.665 1.000 173.052 0 66  ASP III O   1 ? 12 
ATOM 10695 C CB  . ASP I 5 66  ? 21.417  96.498  22.207 1.000 177.682 0 66  ASP III CB  1 ? 12 
ATOM 10696 C CG  . ASP I 5 66  ? 22.045  97.149  23.439 1.000 188.672 0 66  ASP III CG  1 ? 12 
ATOM 10697 O OD1 . ASP I 5 66  ? 21.333  97.827  24.209 1.000 196.626 0 66  ASP III OD1 1 ? 12 
ATOM 10698 O OD2 . ASP I 5 66  ? 23.269  96.984  23.637 1.000 189.014 0 66  ASP III OD2 1 ? 12 
ATOM 10699 N N   . PHE I 5 67  ? 18.379  98.522  22.579 1.000 179.910 0 67  PHE III N   1 ? 12 
ATOM 10700 C CA  . PHE I 5 67  ? 17.842  99.875  22.602 1.000 181.265 0 67  PHE III CA  1 ? 12 
ATOM 10701 C C   . PHE I 5 67  ? 18.173  100.618 23.890 1.000 182.984 0 67  PHE III C   1 ? 12 
ATOM 10702 O O   . PHE I 5 67  ? 17.754  101.770 24.052 1.000 187.521 0 67  PHE III O   1 ? 12 
ATOM 10703 C CB  . PHE I 5 67  ? 16.333  99.866  22.324 1.000 187.208 0 67  PHE III CB  1 ? 12 
ATOM 10704 C CG  . PHE I 5 67  ? 15.527  98.951  23.209 1.000 193.841 0 67  PHE III CG  1 ? 12 
ATOM 10705 C CD1 . PHE I 5 67  ? 15.059  99.364  24.447 1.000 202.481 0 67  PHE III CD1 1 ? 12 
ATOM 10706 C CD2 . PHE I 5 67  ? 15.210  97.677  22.774 1.000 195.591 0 67  PHE III CD2 1 ? 12 
ATOM 10707 C CE1 . PHE I 5 67  ? 14.305  98.514  25.234 1.000 215.907 0 67  PHE III CE1 1 ? 12 
ATOM 10708 C CE2 . PHE I 5 67  ? 14.460  96.826  23.554 1.000 204.147 0 67  PHE III CE2 1 ? 12 
ATOM 10709 C CZ  . PHE I 5 67  ? 14.008  97.243  24.789 1.000 212.540 0 67  PHE III CZ  1 ? 12 
ATOM 10710 N N   . THR I 5 68  ? 18.946  100.006 24.795 1.000 178.960 0 68  THR III N   1 ? 12 
ATOM 10711 C CA  . THR I 5 68  ? 19.357  100.678 26.019 1.000 181.640 0 68  THR III CA  1 ? 12 
ATOM 10712 C C   . THR I 5 68  ? 20.821  101.091 26.003 1.000 184.264 0 68  THR III C   1 ? 12 
ATOM 10713 O O   . THR I 5 68  ? 21.162  102.113 26.606 1.000 195.077 0 68  THR III O   1 ? 12 
ATOM 10714 C CB  . THR I 5 68  ? 19.105  99.766  27.236 1.000 183.219 0 68  THR III CB  1 ? 12 
ATOM 10715 O OG1 . THR I 5 68  ? 19.939  98.600  27.146 1.000 181.474 0 68  THR III OG1 1 ? 12 
ATOM 10716 C CG2 . THR I 5 68  ? 17.635  99.351  27.342 1.000 187.383 0 68  THR III CG2 1 ? 12 
ATOM 10717 N N   . ARG I 5 69  ? 21.695  100.352 25.309 1.000 183.411 0 69  ARG III N   1 ? 12 
ATOM 10718 C CA  . ARG I 5 69  ? 23.107  100.702 25.264 1.000 184.309 0 69  ARG III CA  1 ? 12 
ATOM 10719 C C   . ARG I 5 69  ? 23.644  100.731 23.841 1.000 187.492 0 69  ARG III C   1 ? 12 
ATOM 10720 O O   . ARG I 5 69  ? 24.754  101.230 23.629 1.000 192.567 0 69  ARG III O   1 ? 12 
ATOM 10721 C CB  . ARG I 5 69  ? 23.944  99.714  26.094 1.000 182.645 0 69  ARG III CB  1 ? 12 
ATOM 10722 C CG  . ARG I 5 69  ? 23.635  99.687  27.594 1.000 191.230 0 69  ARG III CG  1 ? 12 
ATOM 10723 C CD  . ARG I 5 69  ? 24.046  100.965 28.308 1.000 200.257 0 69  ARG III CD  1 ? 12 
ATOM 10724 N NE  . ARG I 5 69  ? 23.648  100.969 29.713 1.000 205.587 0 69  ARG III NE  1 ? 12 
ATOM 10725 C CZ  . ARG I 5 69  ? 22.530  101.524 30.162 1.000 207.001 0 69  ARG III CZ  1 ? 12 
ATOM 10726 N NH1 . ARG I 5 69  ? 21.683  102.125 29.343 1.000 206.676 0 69  ARG III NH1 1 ? 12 
ATOM 10727 N NH2 . ARG I 5 69  ? 22.261  101.491 31.465 1.000 210.353 0 69  ARG III NH2 1 ? 12 
ATOM 10728 N N   . HIS I 5 70  ? 22.897  100.209 22.869 1.000 191.199 0 70  HIS III N   1 ? 12 
ATOM 10729 C CA  . HIS I 5 70  ? 23.128  100.363 21.432 1.000 189.484 0 70  HIS III CA  1 ? 12 
ATOM 10730 C C   . HIS I 5 70  ? 24.426  99.721  20.931 1.000 185.410 0 70  HIS III C   1 ? 12 
ATOM 10731 O O   . HIS I 5 70  ? 24.905  100.063 19.846 1.000 189.639 0 70  HIS III O   1 ? 12 
ATOM 10732 C CB  . HIS I 5 70  ? 23.004  101.828 21.012 1.000 192.498 0 70  HIS III CB  1 ? 12 
ATOM 10733 C CG  . HIS I 5 70  ? 21.615  102.176 20.573 1.000 196.594 0 70  HIS III CG  1 ? 12 
ATOM 10734 N ND1 . HIS I 5 70  ? 20.740  102.896 21.357 1.000 198.153 0 70  HIS III ND1 1 ? 12 
ATOM 10735 C CD2 . HIS I 5 70  ? 20.925  101.834 19.459 1.000 196.682 0 70  HIS III CD2 1 ? 12 
ATOM 10736 C CE1 . HIS I 5 70  ? 19.584  103.017 20.728 1.000 201.893 0 70  HIS III CE1 1 ? 12 
ATOM 10737 N NE2 . HIS I 5 70  ? 19.670  102.380 19.573 1.000 200.360 0 70  HIS III NE2 1 ? 12 
ATOM 10738 N N   . ASN I 5 71  ? 25.014  98.785  21.676 1.000 171.697 0 71  ASN III N   1 ? 12 
ATOM 10739 C CA  . ASN I 5 71  ? 26.312  98.243  21.292 1.000 165.296 0 71  ASN III CA  1 ? 12 
ATOM 10740 C C   . ASN I 5 71  ? 26.477  96.767  21.619 1.000 162.383 0 71  ASN III C   1 ? 12 
ATOM 10741 O O   . ASN I 5 71  ? 27.569  96.227  21.412 1.000 170.321 0 71  ASN III O   1 ? 12 
ATOM 10742 C CB  . ASN I 5 71  ? 27.460  99.024  21.961 1.000 169.571 0 71  ASN III CB  1 ? 12 
ATOM 10743 C CG  . ASN I 5 71  ? 27.451  98.902  23.474 1.000 169.557 0 71  ASN III CG  1 ? 12 
ATOM 10744 O OD1 . ASN I 5 71  ? 28.320  98.254  24.059 1.000 163.759 0 71  ASN III OD1 1 ? 12 
ATOM 10745 N ND2 . ASN I 5 71  ? 26.481  99.535  24.115 1.000 176.281 0 71  ASN III ND2 1 ? 12 
ATOM 10746 N N   . GLY I 5 72  ? 25.440  96.095  22.105 1.000 159.610 0 72  GLY III N   1 ? 12 
ATOM 10747 C CA  . GLY I 5 72  ? 25.527  94.695  22.456 1.000 162.342 0 72  GLY III CA  1 ? 12 
ATOM 10748 C C   . GLY I 5 72  ? 25.673  94.465  23.940 1.000 171.426 0 72  GLY III C   1 ? 12 
ATOM 10749 O O   . GLY I 5 72  ? 25.727  93.307  24.377 1.000 172.830 0 72  GLY III O   1 ? 12 
ATOM 10750 N N   . THR I 5 73  ? 25.748  95.535  24.725 1.000 171.711 0 73  THR III N   1 ? 12 
ATOM 10751 C CA  . THR I 5 73  ? 25.952  95.428  26.161 1.000 171.245 0 73  THR III CA  1 ? 12 
ATOM 10752 C C   . THR I 5 73  ? 24.710  94.796  26.757 1.000 180.041 0 73  THR III C   1 ? 12 
ATOM 10753 O O   . THR I 5 73  ? 24.686  93.587  27.033 1.000 187.736 0 73  THR III O   1 ? 12 
ATOM 10754 C CB  . THR I 5 73  ? 26.247  96.805  26.768 1.000 167.944 0 73  THR III CB  1 ? 12 
ATOM 10755 O OG1 . THR I 5 73  ? 27.502  97.287  26.267 1.000 160.151 0 73  THR III OG1 1 ? 12 
ATOM 10756 C CG2 . THR I 5 73  ? 26.335  96.745  28.296 1.000 178.131 0 73  THR III CG2 1 ? 12 
ATOM 10757 N N   . GLY I 5 74  ? 23.739  95.617  27.101 1.000 180.876 0 74  GLY III N   1 ? 12 
ATOM 10758 C CA  . GLY I 5 74  ? 22.585  95.043  27.733 1.000 192.374 0 74  GLY III CA  1 ? 12 
ATOM 10759 C C   . GLY I 5 74  ? 21.292  95.366  27.015 1.000 202.119 0 74  GLY III C   1 ? 12 
ATOM 10760 O O   . GLY I 5 74  ? 21.111  96.501  26.560 1.000 196.712 0 74  GLY III O   1 ? 12 
ATOM 10761 N N   . GLY I 5 75  ? 20.356  94.422  27.006 1.000 203.065 0 75  GLY III N   1 ? 12 
ATOM 10762 C CA  . GLY I 5 75  ? 19.096  94.501  26.299 1.000 201.737 0 75  GLY III CA  1 ? 12 
ATOM 10763 C C   . GLY I 5 75  ? 18.112  94.505  27.449 1.000 216.238 0 75  GLY III C   1 ? 12 
ATOM 10764 O O   . GLY I 5 75  ? 18.531  94.181  28.563 1.000 222.799 0 75  GLY III O   1 ? 12 
ATOM 10765 N N   . LYS I 5 76  ? 16.863  94.893  27.269 1.000 219.852 0 76  LYS III N   1 ? 12 
ATOM 10766 C CA  . LYS I 5 76  ? 15.944  94.727  28.378 1.000 219.216 0 76  LYS III CA  1 ? 12 
ATOM 10767 C C   . LYS I 5 76  ? 14.663  94.018  27.971 1.000 212.043 0 76  LYS III C   1 ? 12 
ATOM 10768 O O   . LYS I 5 76  ? 14.136  94.204  26.881 1.000 223.462 0 76  LYS III O   1 ? 12 
ATOM 10769 C CB  . LYS I 5 76  ? 15.562  96.132  28.876 1.000 219.928 0 76  LYS III CB  1 ? 12 
ATOM 10770 C CG  . LYS I 5 76  ? 14.416  96.247  29.845 1.000 233.392 0 76  LYS III CG  1 ? 12 
ATOM 10771 C CD  . LYS I 5 76  ? 14.195  97.713  30.220 1.000 235.963 0 76  LYS III CD  1 ? 12 
ATOM 10772 C CE  . LYS I 5 76  ? 13.089  97.914  31.255 1.000 247.372 0 76  LYS III CE  1 ? 12 
ATOM 10773 N NZ  . LYS I 5 76  ? 13.158  96.990  32.402 1.000 255.781 0 76  LYS III NZ  1 ? 12 
ATOM 10774 N N   . SER I 5 77  ? 14.126  93.272  28.924 1.000 219.254 0 77  SER III N   1 ? 12 
ATOM 10775 C CA  . SER I 5 77  ? 12.861  92.578  28.815 1.000 223.030 0 77  SER III CA  1 ? 12 
ATOM 10776 C C   . SER I 5 77  ? 11.723  93.459  29.303 1.000 233.593 0 77  SER III C   1 ? 12 
ATOM 10777 O O   . SER I 5 77  ? 11.930  94.513  29.904 1.000 245.090 0 77  SER III O   1 ? 12 
ATOM 10778 C CB  . SER I 5 77  ? 12.909  91.279  29.609 1.000 226.172 0 77  SER III CB  1 ? 12 
ATOM 10779 O OG  . SER I 5 77  ? 11.603  90.833  29.878 1.000 230.185 0 77  SER III OG  1 ? 12 
ATOM 10780 N N   . ILE I 5 78  ? 10.500  92.990  29.071 1.000 232.114 0 78  ILE III N   1 ? 12 
ATOM 10781 C CA  . ILE I 5 78  ? 9.332   93.674  29.612 1.000 237.220 0 78  ILE III CA  1 ? 12 
ATOM 10782 C C   . ILE I 5 78  ? 9.188   93.395  31.098 1.000 244.205 0 78  ILE III C   1 ? 12 
ATOM 10783 O O   . ILE I 5 78  ? 8.314   93.977  31.752 1.000 260.035 0 78  ILE III O   1 ? 12 
ATOM 10784 C CB  . ILE I 5 78  ? 8.038   93.335  28.853 1.000 236.782 0 78  ILE III CB  1 ? 12 
ATOM 10785 C CG1 . ILE I 5 78  ? 7.682   91.855  29.007 1.000 237.162 0 78  ILE III CG1 1 ? 12 
ATOM 10786 C CG2 . ILE I 5 78  ? 8.130   93.833  27.411 1.000 236.297 0 78  ILE III CG2 1 ? 12 
ATOM 10787 C CD1 . ILE I 5 78  ? 6.278   91.530  28.563 1.000 242.157 0 78  ILE III CD1 1 ? 12 
ATOM 10788 N N   . TYR I 5 79  ? 10.019  92.515  31.647 1.000 239.894 0 79  TYR III N   1 ? 12 
ATOM 10789 C CA  . TYR I 5 79  ? 9.971   92.138  33.049 1.000 237.814 0 79  TYR III CA  1 ? 12 
ATOM 10790 C C   . TYR I 5 79  ? 11.076  92.831  33.836 1.000 235.226 0 79  TYR III C   1 ? 12 
ATOM 10791 O O   . TYR I 5 79  ? 11.244  92.556  35.030 1.000 238.823 0 79  TYR III O   1 ? 12 
ATOM 10792 C CB  . TYR I 5 79  ? 10.103  90.613  33.169 1.000 236.563 0 79  TYR III CB  1 ? 12 
ATOM 10793 C CG  . TYR I 5 79  ? 9.172   89.858  32.232 1.000 241.373 0 79  TYR III CG  1 ? 12 
ATOM 10794 C CD1 . TYR I 5 79  ? 7.789   89.960  32.327 1.000 251.817 0 79  TYR III CD1 1 ? 12 
ATOM 10795 C CD2 . TYR I 5 79  ? 9.696   89.088  31.200 1.000 244.919 0 79  TYR III CD2 1 ? 12 
ATOM 10796 C CE1 . TYR I 5 79  ? 6.957   89.273  31.434 1.000 254.116 0 79  TYR III CE1 1 ? 12 
ATOM 10797 C CE2 . TYR I 5 79  ? 8.885   88.414  30.306 1.000 241.358 0 79  TYR III CE2 1 ? 12 
ATOM 10798 C CZ  . TYR I 5 79  ? 7.520   88.504  30.424 1.000 246.896 0 79  TYR III CZ  1 ? 12 
ATOM 10799 O OH  . TYR I 5 79  ? 6.724   87.824  29.526 1.000 248.308 0 79  TYR III OH  1 ? 12 
ATOM 10800 N N   . GLY I 5 80  ? 11.892  93.639  33.160 1.000 243.657 0 80  GLY III N   1 ? 12 
ATOM 10801 C CA  . GLY I 5 80  ? 13.071  94.242  33.750 1.000 250.106 0 80  GLY III CA  1 ? 12 
ATOM 10802 C C   . GLY I 5 80  ? 14.268  93.415  33.362 1.000 255.335 0 80  GLY III C   1 ? 12 
ATOM 10803 O O   . GLY I 5 80  ? 15.057  93.072  34.250 1.000 250.988 0 80  GLY III O   1 ? 12 
ATOM 10804 N N   . GLU I 5 81  ? 14.459  93.156  32.062 1.000 269.639 0 81  GLU III N   1 ? 12 
ATOM 10805 C CA  . GLU I 5 81  ? 15.551  92.257  31.662 1.000 255.970 0 81  GLU III CA  1 ? 12 
ATOM 10806 C C   . GLU I 5 81  ? 15.129  91.057  32.487 1.000 257.171 0 81  GLU III C   1 ? 12 
ATOM 10807 O O   . GLU I 5 81  ? 13.938  90.719  32.490 1.000 280.553 0 81  GLU III O   1 ? 12 
ATOM 10808 C CB  . GLU I 5 81  ? 16.919  92.839  31.979 1.000 249.136 0 81  GLU III CB  1 ? 12 
ATOM 10809 C CG  . GLU I 5 81  ? 18.042  92.533  31.009 1.000 251.220 0 81  GLU III CG  1 ? 12 
ATOM 10810 C CD  . GLU I 5 81  ? 18.691  91.181  31.238 1.000 253.189 0 81  GLU III CD  1 ? 12 
ATOM 10811 O OE1 . GLU I 5 81  ? 18.625  90.670  32.376 1.000 258.631 0 81  GLU III OE1 1 ? 12 
ATOM 10812 O OE2 . GLU I 5 81  ? 19.312  90.653  30.289 1.000 252.784 0 81  GLU III OE2 1 ? 12 
ATOM 10813 N N   . LYS I 5 82  ? 16.042  90.326  33.099 1.000 240.968 0 82  LYS III N   1 ? 12 
ATOM 10814 C CA  . LYS I 5 82  ? 15.576  89.219  33.903 1.000 237.268 0 82  LYS III CA  1 ? 12 
ATOM 10815 C C   . LYS I 5 82  ? 14.639  88.188  33.259 1.000 238.475 0 82  LYS III C   1 ? 12 
ATOM 10816 O O   . LYS I 5 82  ? 13.938  87.530  34.028 1.000 250.672 0 82  LYS III O   1 ? 12 
ATOM 10817 C CB  . LYS I 5 82  ? 14.794  89.870  35.064 1.000 239.869 0 82  LYS III CB  1 ? 12 
ATOM 10818 C CG  . LYS I 5 82  ? 14.679  89.315  36.467 1.000 236.021 0 82  LYS III CG  1 ? 12 
ATOM 10819 C CD  . LYS I 5 82  ? 15.929  88.960  37.197 1.000 232.095 0 82  LYS III CD  1 ? 12 
ATOM 10820 C CE  . LYS I 5 82  ? 15.525  88.495  38.606 1.000 232.669 0 82  LYS III CE  1 ? 12 
ATOM 10821 N NZ  . LYS I 5 82  ? 14.734  87.240  38.591 1.000 237.804 0 82  LYS III NZ  1 ? 12 
ATOM 10822 N N   . PHE I 5 83  ? 14.544  87.869  31.953 1.000 237.262 0 83  PHE III N   1 ? 12 
ATOM 10823 C CA  . PHE I 5 83  ? 13.668  86.699  31.930 1.000 241.865 0 83  PHE III CA  1 ? 12 
ATOM 10824 C C   . PHE I 5 83  ? 14.393  85.413  31.563 1.000 234.039 0 83  PHE III C   1 ? 12 
ATOM 10825 O O   . PHE I 5 83  ? 15.481  85.392  30.980 1.000 229.397 0 83  PHE III O   1 ? 12 
ATOM 10826 C CB  . PHE I 5 83  ? 12.437  86.892  30.998 1.000 233.589 0 83  PHE III CB  1 ? 12 
ATOM 10827 C CG  . PHE I 5 83  ? 12.709  86.961  29.483 1.000 227.191 0 83  PHE III CG  1 ? 12 
ATOM 10828 C CD1 . PHE I 5 83  ? 13.384  85.963  28.778 1.000 228.833 0 83  PHE III CD1 1 ? 12 
ATOM 10829 C CD2 . PHE I 5 83  ? 12.180  88.006  28.760 1.000 229.733 0 83  PHE III CD2 1 ? 12 
ATOM 10830 C CE1 . PHE I 5 83  ? 13.557  86.060  27.391 1.000 236.266 0 83  PHE III CE1 1 ? 12 
ATOM 10831 C CE2 . PHE I 5 83  ? 12.362  88.102  27.398 1.000 240.175 0 83  PHE III CE2 1 ? 12 
ATOM 10832 C CZ  . PHE I 5 83  ? 13.056  87.140  26.707 1.000 242.908 0 83  PHE III CZ  1 ? 12 
ATOM 10833 N N   . GLU I 5 84  ? 13.723  84.331  31.926 1.000 241.586 0 84  GLU III N   1 ? 12 
ATOM 10834 C CA  . GLU I 5 84  ? 14.216  82.968  31.883 1.000 242.756 0 84  GLU III CA  1 ? 12 
ATOM 10835 C C   . GLU I 5 84  ? 14.264  82.394  30.468 1.000 249.230 0 84  GLU III C   1 ? 12 
ATOM 10836 O O   . GLU I 5 84  ? 13.631  82.897  29.536 1.000 251.178 0 84  GLU III O   1 ? 12 
ATOM 10837 C CB  . GLU I 5 84  ? 13.425  82.127  32.881 1.000 252.242 0 84  GLU III CB  1 ? 12 
ATOM 10838 C CG  . GLU I 5 84  ? 12.014  81.826  32.539 1.000 259.926 0 84  GLU III CG  1 ? 12 
ATOM 10839 C CD  . GLU I 5 84  ? 11.391  80.958  33.602 1.000 263.435 0 84  GLU III CD  1 ? 12 
ATOM 10840 O OE1 . GLU I 5 84  ? 11.970  80.884  34.709 1.000 258.656 0 84  GLU III OE1 1 ? 12 
ATOM 10841 O OE2 . GLU I 5 84  ? 10.329  80.361  33.342 1.000 263.513 0 84  GLU III OE2 1 ? 12 
ATOM 10842 N N   . ASP I 5 85  ? 15.053  81.334  30.315 1.000 248.603 0 85  ASP III N   1 ? 12 
ATOM 10843 C CA  . ASP I 5 85  ? 14.999  80.512  29.112 1.000 254.814 0 85  ASP III CA  1 ? 12 
ATOM 10844 C C   . ASP I 5 85  ? 13.692  79.734  29.144 1.000 259.508 0 85  ASP III C   1 ? 12 
ATOM 10845 O O   . ASP I 5 85  ? 13.482  78.913  30.042 1.000 257.840 0 85  ASP III O   1 ? 12 
ATOM 10846 C CB  . ASP I 5 85  ? 16.193  79.562  29.025 1.000 247.752 0 85  ASP III CB  1 ? 12 
ATOM 10847 C CG  . ASP I 5 85  ? 17.512  80.288  28.888 1.000 235.866 0 85  ASP III CG  1 ? 12 
ATOM 10848 O OD1 . ASP I 5 85  ? 17.573  81.237  28.082 1.000 225.325 0 85  ASP III OD1 1 ? 12 
ATOM 10849 O OD2 . ASP I 5 85  ? 18.478  79.935  29.596 1.000 234.405 0 85  ASP III OD2 1 ? 12 
ATOM 10850 N N   . GLU I 5 86  ? 12.795  80.008  28.196 1.000 259.952 0 86  GLU III N   1 ? 12 
ATOM 10851 C CA  . GLU I 5 86  ? 11.449  79.452  28.290 1.000 265.216 0 86  GLU III CA  1 ? 12 
ATOM 10852 C C   . GLU I 5 86  ? 11.515  77.953  28.047 1.000 274.826 0 86  GLU III C   1 ? 12 
ATOM 10853 O O   . GLU I 5 86  ? 11.004  77.166  28.852 1.000 283.765 0 86  GLU III O   1 ? 12 
ATOM 10854 C CB  . GLU I 5 86  ? 10.463  80.156  27.357 1.000 254.835 0 86  GLU III CB  1 ? 12 
ATOM 10855 C CG  . GLU I 5 86  ? 9.032   79.648  27.582 1.000 253.354 0 86  GLU III CG  1 ? 12 
ATOM 10856 C CD  . GLU I 5 86  ? 7.975   80.478  26.886 1.000 255.011 0 86  GLU III CD  1 ? 12 
ATOM 10857 O OE1 . GLU I 5 86  ? 8.341   81.351  26.077 1.000 252.590 0 86  GLU III OE1 1 ? 12 
ATOM 10858 O OE2 . GLU I 5 86  ? 6.774   80.268  27.167 1.000 262.967 0 86  GLU III OE2 1 ? 12 
ATOM 10859 N N   . ASN I 5 87  ? 12.199  77.544  26.980 1.000 274.596 0 87  ASN III N   1 ? 12 
ATOM 10860 C CA  . ASN I 5 87  ? 12.454  76.136  26.704 1.000 274.285 0 87  ASN III CA  1 ? 12 
ATOM 10861 C C   . ASN I 5 87  ? 13.546  76.065  25.647 1.000 273.830 0 87  ASN III C   1 ? 12 
ATOM 10862 O O   . ASN I 5 87  ? 13.917  77.067  25.033 1.000 279.473 0 87  ASN III O   1 ? 12 
ATOM 10863 C CB  . ASN I 5 87  ? 11.228  75.417  26.105 1.000 271.990 0 87  ASN III CB  1 ? 12 
ATOM 10864 C CG  . ASN I 5 87  ? 10.021  75.399  27.010 1.000 277.260 0 87  ASN III CG  1 ? 12 
ATOM 10865 O OD1 . ASN I 5 87  ? 8.986   75.983  26.682 1.000 279.289 0 87  ASN III OD1 1 ? 12 
ATOM 10866 N ND2 . ASN I 5 87  ? 10.134  74.723  28.144 1.000 286.601 0 87  ASN III ND2 1 ? 12 
ATOM 10867 N N   . PHE I 5 88  ? 14.058  74.846  25.454 1.000 264.105 0 88  PHE III N   1 ? 12 
ATOM 10868 C CA  . PHE I 5 88  ? 15.053  74.520  24.438 1.000 260.554 0 88  PHE III CA  1 ? 12 
ATOM 10869 C C   . PHE I 5 88  ? 14.562  73.378  23.560 1.000 262.220 0 88  PHE III C   1 ? 12 
ATOM 10870 O O   . PHE I 5 88  ? 15.370  72.715  22.901 1.000 274.035 0 88  PHE III O   1 ? 12 
ATOM 10871 C CB  . PHE I 5 88  ? 16.420  74.172  25.044 1.000 258.655 0 88  PHE III CB  1 ? 12 
ATOM 10872 C CG  . PHE I 5 88  ? 17.078  75.300  25.804 1.000 254.603 0 88  PHE III CG  1 ? 12 
ATOM 10873 C CD1 . PHE I 5 88  ? 17.200  76.559  25.236 1.000 252.923 0 88  PHE III CD1 1 ? 12 
ATOM 10874 C CD2 . PHE I 5 88  ? 17.616  75.091  27.066 1.000 256.056 0 88  PHE III CD2 1 ? 12 
ATOM 10875 C CE1 . PHE I 5 88  ? 17.826  77.590  25.919 1.000 249.873 0 88  PHE III CE1 1 ? 12 
ATOM 10876 C CE2 . PHE I 5 88  ? 18.238  76.122  27.755 1.000 251.495 0 88  PHE III CE2 1 ? 12 
ATOM 10877 C CZ  . PHE I 5 88  ? 18.342  77.372  27.180 1.000 246.871 0 88  PHE III CZ  1 ? 12 
ATOM 10878 N N   . ILE I 5 89  ? 13.253  73.125  23.565 1.000 258.273 0 89  ILE III N   1 ? 12 
ATOM 10879 C CA  . ILE I 5 89  ? 12.696  72.036  22.772 1.000 251.014 0 89  ILE III CA  1 ? 12 
ATOM 10880 C C   . ILE I 5 89  ? 12.967  72.270  21.293 1.000 252.774 0 89  ILE III C   1 ? 12 
ATOM 10881 O O   . ILE I 5 89  ? 13.358  71.350  20.564 1.000 259.389 0 89  ILE III O   1 ? 12 
ATOM 10882 C CB  . ILE I 5 89  ? 11.195  71.871  23.070 1.000 253.360 0 89  ILE III CB  1 ? 12 
ATOM 10883 C CG1 . ILE I 5 89  ? 10.973  71.769  24.583 1.000 259.254 0 89  ILE III CG1 1 ? 12 
ATOM 10884 C CG2 . ILE I 5 89  ? 10.651  70.637  22.373 1.000 257.541 0 89  ILE III CG2 1 ? 12 
ATOM 10885 C CD1 . ILE I 5 89  ? 9.546   71.465  24.981 1.000 262.286 0 89  ILE III CD1 1 ? 12 
ATOM 10886 N N   . LEU I 5 90  ? 12.773  73.502  20.832 1.000 248.721 0 90  LEU III N   1 ? 12 
ATOM 10887 C CA  . LEU I 5 90  ? 12.952  73.822  19.424 1.000 238.377 0 90  LEU III CA  1 ? 12 
ATOM 10888 C C   . LEU I 5 90  ? 14.430  73.818  19.055 1.000 234.048 0 90  LEU III C   1 ? 12 
ATOM 10889 O O   . LEU I 5 90  ? 15.306  74.093  19.879 1.000 235.398 0 90  LEU III O   1 ? 12 
ATOM 10890 C CB  . LEU I 5 90  ? 12.346  75.190  19.108 1.000 222.516 0 90  LEU III CB  1 ? 12 
ATOM 10891 C CG  . LEU I 5 90  ? 10.820  75.289  19.119 1.000 220.592 0 90  LEU III CG  1 ? 12 
ATOM 10892 C CD1 . LEU I 5 90  ? 10.374  76.686  18.725 1.000 212.084 0 90  LEU III CD1 1 ? 12 
ATOM 10893 C CD2 . LEU I 5 90  ? 10.204  74.249  18.197 1.000 219.123 0 90  LEU III CD2 1 ? 12 
ATOM 10894 N N   . LYS I 5 91  ? 14.701  73.502  17.794 1.000 238.570 0 91  LYS III N   1 ? 12 
ATOM 10895 C CA  . LYS I 5 91  ? 16.063  73.387  17.305 1.000 243.989 0 91  LYS III CA  1 ? 12 
ATOM 10896 C C   . LYS I 5 91  ? 16.282  74.391  16.178 1.000 252.049 0 91  LYS III C   1 ? 12 
ATOM 10897 O O   . LYS I 5 91  ? 15.351  74.742  15.447 1.000 261.681 0 91  LYS III O   1 ? 12 
ATOM 10898 C CB  . LYS I 5 91  ? 16.339  71.953  16.823 1.000 243.172 0 91  LYS III CB  1 ? 12 
ATOM 10899 C CG  . LYS I 5 91  ? 17.614  71.312  17.363 1.000 239.230 0 91  LYS III CG  1 ? 12 
ATOM 10900 C CD  . LYS I 5 91  ? 17.425  70.781  18.780 1.000 237.146 0 91  LYS III CD  1 ? 12 
ATOM 10901 C CE  . LYS I 5 91  ? 18.649  70.010  19.248 1.000 233.773 0 91  LYS III CE  1 ? 12 
ATOM 10902 N NZ  . LYS I 5 91  ? 18.417  69.352  20.562 1.000 228.556 0 91  LYS III NZ  1 ? 12 
ATOM 10903 N N   . HIS I 5 92  ? 17.523  74.870  16.073 1.000 258.578 0 92  HIS III N   1 ? 12 
ATOM 10904 C CA  . HIS I 5 92  ? 17.986  75.800  15.037 1.000 251.254 0 92  HIS III CA  1 ? 12 
ATOM 10905 C C   . HIS I 5 92  ? 18.244  75.039  13.740 1.000 252.624 0 92  HIS III C   1 ? 12 
ATOM 10906 O O   . HIS I 5 92  ? 19.361  74.598  13.464 1.000 256.266 0 92  HIS III O   1 ? 12 
ATOM 10907 C CB  . HIS I 5 92  ? 19.228  76.552  15.498 1.000 239.661 0 92  HIS III CB  1 ? 12 
ATOM 10908 C CG  . HIS I 5 92  ? 19.004  77.397  16.712 1.000 231.569 0 92  HIS III CG  1 ? 12 
ATOM 10909 N ND1 . HIS I 5 92  ? 19.049  76.888  17.992 1.000 231.690 0 92  HIS III ND1 1 ? 12 
ATOM 10910 C CD2 . HIS I 5 92  ? 18.715  78.713  16.841 1.000 218.846 0 92  HIS III CD2 1 ? 12 
ATOM 10911 C CE1 . HIS I 5 92  ? 18.812  77.857  18.858 1.000 224.274 0 92  HIS III CE1 1 ? 12 
ATOM 10912 N NE2 . HIS I 5 92  ? 18.604  78.975  18.185 1.000 214.565 0 92  HIS III NE2 1 ? 12 
ATOM 10913 N N   . THR I 5 93  ? 17.202  74.902  12.920 1.000 237.531 0 93  THR III N   1 ? 12 
ATOM 10914 C CA  . THR I 5 93  ? 17.214  73.989  11.782 1.000 234.693 0 93  THR III CA  1 ? 12 
ATOM 10915 C C   . THR I 5 93  ? 17.662  74.629  10.471 1.000 223.599 0 93  THR III C   1 ? 12 
ATOM 10916 O O   . THR I 5 93  ? 17.873  73.901  9.497  1.000 215.719 0 93  THR III O   1 ? 12 
ATOM 10917 C CB  . THR I 5 93  ? 15.820  73.374  11.571 1.000 244.882 0 93  THR III CB  1 ? 12 
ATOM 10918 O OG1 . THR I 5 93  ? 14.956  74.332  10.943 1.000 248.835 0 93  THR III OG1 1 ? 12 
ATOM 10919 C CG2 . THR I 5 93  ? 15.211  72.892  12.886 1.000 244.465 0 93  THR III CG2 1 ? 12 
ATOM 10920 N N   . GLY I 5 94  ? 17.826  75.949  10.406 1.000 215.514 0 94  GLY III N   1 ? 12 
ATOM 10921 C CA  . GLY I 5 94  ? 18.196  76.570  9.154  1.000 196.435 0 94  GLY III CA  1 ? 12 
ATOM 10922 C C   . GLY I 5 94  ? 17.989  78.070  9.087  1.000 192.071 0 94  GLY III C   1 ? 12 
ATOM 10923 O O   . GLY I 5 94  ? 17.701  78.732  10.090 1.000 196.707 0 94  GLY III O   1 ? 12 
ATOM 10924 N N   . PRO I 5 95  ? 18.154  78.636  7.889  1.000 185.716 0 95  PRO III N   1 ? 12 
ATOM 10925 C CA  . PRO I 5 95  ? 17.922  80.075  7.708  1.000 182.181 0 95  PRO III CA  1 ? 12 
ATOM 10926 C C   . PRO I 5 95  ? 16.503  80.473  8.076  1.000 189.886 0 95  PRO III C   1 ? 12 
ATOM 10927 O O   . PRO I 5 95  ? 15.541  79.743  7.829  1.000 197.952 0 95  PRO III O   1 ? 12 
ATOM 10928 C CB  . PRO I 5 95  ? 18.200  80.302  6.217  1.000 177.591 0 95  PRO III CB  1 ? 12 
ATOM 10929 C CG  . PRO I 5 95  ? 18.985  79.121  5.778  1.000 181.132 0 95  PRO III CG  1 ? 12 
ATOM 10930 C CD  . PRO I 5 95  ? 18.565  77.976  6.639  1.000 184.205 0 95  PRO III CD  1 ? 12 
ATOM 10931 N N   . GLY I 5 96  ? 16.388  81.654  8.670  1.000 184.439 0 96  GLY III N   1 ? 12 
ATOM 10932 C CA  . GLY I 5 96  ? 15.112  82.244  8.983  1.000 182.539 0 96  GLY III CA  1 ? 12 
ATOM 10933 C C   . GLY I 5 96  ? 14.703  82.026  10.418 1.000 190.595 0 96  GLY III C   1 ? 12 
ATOM 10934 O O   . GLY I 5 96  ? 13.769  82.685  10.891 1.000 205.809 0 96  GLY III O   1 ? 12 
ATOM 10935 N N   . ILE I 5 97  ? 15.389  81.121  11.121 1.000 187.323 0 97  ILE III N   1 ? 12 
ATOM 10936 C CA  . ILE I 5 97  ? 15.111  80.885  12.529 1.000 186.681 0 97  ILE III CA  1 ? 12 
ATOM 10937 C C   . ILE I 5 97  ? 15.389  82.152  13.321 1.000 179.859 0 97  ILE III C   1 ? 12 
ATOM 10938 O O   . ILE I 5 97  ? 16.442  82.784  13.172 1.000 163.750 0 97  ILE III O   1 ? 12 
ATOM 10939 C CB  . ILE I 5 97  ? 15.948  79.703  13.044 1.000 184.394 0 97  ILE III CB  1 ? 12 
ATOM 10940 C CG1 . ILE I 5 97  ? 15.487  78.396  12.397 1.000 190.223 0 97  ILE III CG1 1 ? 12 
ATOM 10941 C CG2 . ILE I 5 97  ? 15.882  79.605  14.561 1.000 189.434 0 97  ILE III CG2 1 ? 12 
ATOM 10942 C CD1 . ILE I 5 97  ? 14.016  78.109  12.585 1.000 194.330 0 97  ILE III CD1 1 ? 12 
ATOM 10943 N N   . LEU I 5 98  ? 14.442  82.525  14.174 1.000 188.131 0 98  LEU III N   1 ? 12 
ATOM 10944 C CA  . LEU I 5 98  ? 14.566  83.686  15.043 1.000 182.902 0 98  LEU III CA  1 ? 12 
ATOM 10945 C C   . LEU I 5 98  ? 14.725  83.188  16.470 1.000 184.632 0 98  LEU III C   1 ? 12 
ATOM 10946 O O   . LEU I 5 98  ? 13.884  82.428  16.964 1.000 192.812 0 98  LEU III O   1 ? 12 
ATOM 10947 C CB  . LEU I 5 98  ? 13.351  84.608  14.919 1.000 187.667 0 98  LEU III CB  1 ? 12 
ATOM 10948 C CG  . LEU I 5 98  ? 13.536  86.049  15.405 1.000 179.344 0 98  LEU III CG  1 ? 12 
ATOM 10949 C CD1 . LEU I 5 98  ? 14.939  86.544  15.110 1.000 172.666 0 98  LEU III CD1 1 ? 12 
ATOM 10950 C CD2 . LEU I 5 98  ? 12.501  86.981  14.785 1.000 194.635 0 98  LEU III CD2 1 ? 12 
ATOM 10951 N N   . SER I 5 99  ? 15.799  83.612  17.127 1.000 180.460 0 99  SER III N   1 ? 12 
ATOM 10952 C CA  . SER I 5 99  ? 16.113  83.125  18.457 1.000 180.066 0 99  SER III CA  1 ? 12 
ATOM 10953 C C   . SER I 5 99  ? 16.676  84.266  19.290 1.000 175.660 0 99  SER III C   1 ? 12 
ATOM 10954 O O   . SER I 5 99  ? 17.238  85.228  18.760 1.000 165.621 0 99  SER III O   1 ? 12 
ATOM 10955 C CB  . SER I 5 99  ? 17.100  81.950  18.404 1.000 178.193 0 99  SER III CB  1 ? 12 
ATOM 10956 O OG  . SER I 5 99  ? 17.566  81.609  19.697 1.000 188.719 0 99  SER III OG  1 ? 12 
ATOM 10957 N N   . MET I 5 100 ? 16.510  84.149  20.602 1.000 180.463 0 100 MET III N   1 ? 12 
ATOM 10958 C CA  . MET I 5 100 ? 16.974  85.173  21.526 1.000 174.367 0 100 MET III CA  1 ? 12 
ATOM 10959 C C   . MET I 5 100 ? 18.482  85.088  21.729 1.000 165.795 0 100 MET III C   1 ? 12 
ATOM 10960 O O   . MET I 5 100 ? 19.068  84.005  21.714 1.000 163.100 0 100 MET III O   1 ? 12 
ATOM 10961 C CB  . MET I 5 100 ? 16.273  85.013  22.873 1.000 175.071 0 100 MET III CB  1 ? 12 
ATOM 10962 C CG  . MET I 5 100 ? 14.930  85.688  22.965 1.000 176.569 0 100 MET III CG  1 ? 12 
ATOM 10963 S SD  . MET I 5 100 ? 15.039  87.480  22.820 1.000 171.302 0 100 MET III SD  1 ? 12 
ATOM 10964 C CE  . MET I 5 100 ? 16.180  87.880  24.147 1.000 184.479 0 100 MET III CE  1 ? 12 
ATOM 10965 N N   . ALA I 5 101 ? 19.115  86.243  21.912 1.000 162.568 0 101 ALA III N   1 ? 12 
ATOM 10966 C CA  . ALA I 5 101 ? 20.511  86.250  22.311 1.000 162.655 0 101 ALA III CA  1 ? 12 
ATOM 10967 C C   . ALA I 5 101 ? 20.585  86.074  23.818 1.000 165.090 0 101 ALA III C   1 ? 12 
ATOM 10968 O O   . ALA I 5 101 ? 19.649  86.420  24.550 1.000 171.365 0 101 ALA III O   1 ? 12 
ATOM 10969 C CB  . ALA I 5 101 ? 21.225  87.538  21.881 1.000 158.594 0 101 ALA III CB  1 ? 12 
ATOM 10970 N N   . ASN I 5 102 ? 21.698  85.510  24.280 1.000 165.238 0 102 ASN III N   1 ? 12 
ATOM 10971 C CA  . ASN I 5 102 ? 21.903  85.367  25.713 1.000 171.508 0 102 ASN III CA  1 ? 12 
ATOM 10972 C C   . ASN I 5 102 ? 23.377  85.224  26.052 1.000 178.980 0 102 ASN III C   1 ? 12 
ATOM 10973 O O   . ASN I 5 102 ? 24.087  84.415  25.445 1.000 184.265 0 102 ASN III O   1 ? 12 
ATOM 10974 C CB  . ASN I 5 102 ? 21.135  84.162  26.236 1.000 182.068 0 102 ASN III CB  1 ? 12 
ATOM 10975 C CG  . ASN I 5 102 ? 21.682  82.841  25.704 1.000 181.266 0 102 ASN III CG  1 ? 12 
ATOM 10976 O OD1 . ASN I 5 102 ? 21.183  82.309  24.713 1.000 184.562 0 102 ASN III OD1 1 ? 12 
ATOM 10977 N ND2 . ASN I 5 102 ? 22.670  82.283  26.391 1.000 183.918 0 102 ASN III ND2 1 ? 12 
ATOM 10978 N N   . ALA I 5 103 ? 23.837  86.053  26.992 1.000 182.391 0 103 ALA III N   1 ? 12 
ATOM 10979 C CA  . ALA I 5 103 ? 25.238  86.047  27.391 1.000 181.962 0 103 ALA III CA  1 ? 12 
ATOM 10980 C C   . ALA I 5 103 ? 25.578  84.741  28.097 1.000 187.780 0 103 ALA III C   1 ? 12 
ATOM 10981 O O   . ALA I 5 103 ? 26.740  84.317  28.111 1.000 187.251 0 103 ALA III O   1 ? 12 
ATOM 10982 C CB  . ALA I 5 103 ? 25.527  87.242  28.296 1.000 169.377 0 103 ALA III CB  1 ? 12 
ATOM 10983 N N   . GLY I 5 104 ? 24.568  84.100  28.680 1.000 196.753 0 104 GLY III N   1 ? 12 
ATOM 10984 C CA  . GLY I 5 104 ? 24.714  82.921  29.500 1.000 204.342 0 104 GLY III CA  1 ? 12 
ATOM 10985 C C   . GLY I 5 104 ? 23.341  82.314  29.704 1.000 212.369 0 104 GLY III C   1 ? 12 
ATOM 10986 O O   . GLY I 5 104 ? 22.337  82.884  29.266 1.000 214.002 0 104 GLY III O   1 ? 12 
ATOM 10987 N N   . PRO I 5 105 ? 23.256  81.145  30.339 1.000 213.674 0 105 PRO III N   1 ? 12 
ATOM 10988 C CA  . PRO I 5 105 ? 21.931  80.589  30.646 1.000 210.083 0 105 PRO III CA  1 ? 12 
ATOM 10989 C C   . PRO I 5 105 ? 21.088  81.593  31.419 1.000 211.623 0 105 PRO III C   1 ? 12 
ATOM 10990 O O   . PRO I 5 105 ? 21.543  82.211  32.387 1.000 215.678 0 105 PRO III O   1 ? 12 
ATOM 10991 C CB  . PRO I 5 105 ? 22.236  79.331  31.467 1.000 212.617 0 105 PRO III CB  1 ? 12 
ATOM 10992 C CG  . PRO I 5 105 ? 23.707  79.170  31.486 1.000 218.647 0 105 PRO III CG  1 ? 12 
ATOM 10993 C CD  . PRO I 5 105 ? 24.357  80.406  30.978 1.000 216.849 0 105 PRO III CD  1 ? 12 
ATOM 10994 N N   . ASN I 5 106 ? 19.844  81.745  30.976 1.000 217.631 0 106 ASN III N   1 ? 12 
ATOM 10995 C CA  . ASN I 5 106 ? 18.825  82.563  31.630 1.000 221.044 0 106 ASN III CA  1 ? 12 
ATOM 10996 C C   . ASN I 5 106 ? 19.277  84.016  31.791 1.000 212.277 0 106 ASN III C   1 ? 12 
ATOM 10997 O O   . ASN I 5 106 ? 19.127  84.623  32.852 1.000 205.288 0 106 ASN III O   1 ? 12 
ATOM 10998 C CB  . ASN I 5 106 ? 18.413  81.975  32.980 1.000 221.843 0 106 ASN III CB  1 ? 12 
ATOM 10999 C CG  . ASN I 5 106 ? 17.979  80.537  32.877 1.000 229.970 0 106 ASN III CG  1 ? 12 
ATOM 11000 O OD1 . ASN I 5 106 ? 17.107  80.194  32.076 1.000 241.089 0 106 ASN III OD1 1 ? 12 
ATOM 11001 N ND2 . ASN I 5 106 ? 18.578  79.681  33.693 1.000 223.892 0 106 ASN III ND2 1 ? 12 
ATOM 11002 N N   . THR I 5 107 ? 19.844  84.574  30.718 1.000 208.311 0 107 THR III N   1 ? 12 
ATOM 11003 C CA  . THR I 5 107 ? 20.294  85.961  30.693 1.000 199.973 0 107 THR III CA  1 ? 12 
ATOM 11004 C C   . THR I 5 107 ? 19.768  86.610  29.422 1.000 201.952 0 107 THR III C   1 ? 12 
ATOM 11005 O O   . THR I 5 107 ? 20.416  87.482  28.840 1.000 202.554 0 107 THR III O   1 ? 12 
ATOM 11006 C CB  . THR I 5 107 ? 21.816  86.064  30.761 1.000 194.150 0 107 THR III CB  1 ? 12 
ATOM 11007 O OG1 . THR I 5 107 ? 22.387  85.396  29.628 1.000 187.071 0 107 THR III OG1 1 ? 12 
ATOM 11008 C CG2 . THR I 5 107 ? 22.338  85.439  32.042 1.000 209.289 0 107 THR III CG2 1 ? 12 
ATOM 11009 N N   . ASN I 5 108 ? 18.589  86.158  28.995 1.000 203.548 0 108 ASN III N   1 ? 12 
ATOM 11010 C CA  . ASN I 5 108 ? 17.878  86.703  27.850 1.000 196.960 0 108 ASN III CA  1 ? 12 
ATOM 11011 C C   . ASN I 5 108 ? 17.366  88.112  28.115 1.000 200.733 0 108 ASN III C   1 ? 12 
ATOM 11012 O O   . ASN I 5 108 ? 16.865  88.408  29.199 1.000 213.588 0 108 ASN III O   1 ? 12 
ATOM 11013 C CB  . ASN I 5 108 ? 16.718  85.768  27.499 1.000 193.811 0 108 ASN III CB  1 ? 12 
ATOM 11014 C CG  . ASN I 5 108 ? 17.175  84.348  27.203 1.000 195.658 0 108 ASN III CG  1 ? 12 
ATOM 11015 O OD1 . ASN I 5 108 ? 17.797  84.098  26.169 1.000 199.779 0 108 ASN III OD1 1 ? 12 
ATOM 11016 N ND2 . ASN I 5 108 ? 16.941  83.427  28.143 1.000 198.917 0 108 ASN III ND2 1 ? 12 
ATOM 11017 N N   . GLY I 5 109 ? 17.503  88.989  27.122 1.000 196.996 0 109 GLY III N   1 ? 12 
ATOM 11018 C CA  . GLY I 5 109 ? 16.951  90.320  27.304 1.000 197.178 0 109 GLY III CA  1 ? 12 
ATOM 11019 C C   . GLY I 5 109 ? 16.046  90.781  26.178 1.000 200.137 0 109 GLY III C   1 ? 12 
ATOM 11020 O O   . GLY I 5 109 ? 14.934  90.264  26.026 1.000 200.810 0 109 GLY III O   1 ? 12 
ATOM 11021 N N   . SER I 5 110 ? 16.507  91.751  25.383 1.000 198.774 0 110 SER III N   1 ? 12 
ATOM 11022 C CA  . SER I 5 110 ? 15.785  92.260  24.218 1.000 187.592 0 110 SER III CA  1 ? 12 
ATOM 11023 C C   . SER I 5 110 ? 16.602  92.133  22.942 1.000 187.954 0 110 SER III C   1 ? 12 
ATOM 11024 O O   . SER I 5 110 ? 16.400  92.896  21.995 1.000 189.620 0 110 SER III O   1 ? 12 
ATOM 11025 C CB  . SER I 5 110 ? 15.384  93.718  24.406 1.000 191.001 0 110 SER III CB  1 ? 12 
ATOM 11026 O OG  . SER I 5 110 ? 16.511  94.544  24.638 1.000 196.931 0 110 SER III OG  1 ? 12 
ATOM 11027 N N   . GLN I 5 111 ? 17.529  91.189  22.894 1.000 182.117 0 111 GLN III N   1 ? 12 
ATOM 11028 C CA  . GLN I 5 111 ? 18.384  91.044  21.730 1.000 167.334 0 111 GLN III CA  1 ? 12 
ATOM 11029 C C   . GLN I 5 111 ? 18.105  89.721  21.038 1.000 164.192 0 111 GLN III C   1 ? 12 
ATOM 11030 O O   . GLN I 5 111 ? 17.999  88.674  21.683 1.000 163.702 0 111 GLN III O   1 ? 12 
ATOM 11031 C CB  . GLN I 5 111 ? 19.856  91.157  22.129 1.000 159.566 0 111 GLN III CB  1 ? 12 
ATOM 11032 C CG  . GLN I 5 111 ? 20.215  92.554  22.623 1.000 161.850 0 111 GLN III CG  1 ? 12 
ATOM 11033 C CD  . GLN I 5 111 ? 21.688  92.723  22.920 1.000 158.952 0 111 GLN III CD  1 ? 12 
ATOM 11034 O OE1 . GLN I 5 111 ? 22.529  92.019  22.364 1.000 153.154 0 111 GLN III OE1 1 ? 12 
ATOM 11035 N NE2 . GLN I 5 111 ? 22.008  93.652  23.813 1.000 165.751 0 111 GLN III NE2 1 ? 12 
ATOM 11036 N N   . PHE I 5 112 ? 18.002  89.787  19.717 1.000 160.028 0 112 PHE III N   1 ? 12 
ATOM 11037 C CA  . PHE I 5 112 ? 17.603  88.664  18.891 1.000 157.362 0 112 PHE III CA  1 ? 12 
ATOM 11038 C C   . PHE I 5 112 ? 18.616  88.502  17.772 1.000 156.450 0 112 PHE III C   1 ? 12 
ATOM 11039 O O   . PHE I 5 112 ? 19.251  89.470  17.346 1.000 150.745 0 112 PHE III O   1 ? 12 
ATOM 11040 C CB  . PHE I 5 112 ? 16.199  88.875  18.294 1.000 160.133 0 112 PHE III CB  1 ? 12 
ATOM 11041 C CG  . PHE I 5 112 ? 16.081  90.114  17.437 1.000 161.081 0 112 PHE III CG  1 ? 12 
ATOM 11042 C CD1 . PHE I 5 112 ? 15.992  91.373  18.011 1.000 164.185 0 112 PHE III CD1 1 ? 12 
ATOM 11043 C CD2 . PHE I 5 112 ? 16.054  90.015  16.055 1.000 157.842 0 112 PHE III CD2 1 ? 12 
ATOM 11044 C CE1 . PHE I 5 112 ? 15.887  92.507  17.226 1.000 164.609 0 112 PHE III CE1 1 ? 12 
ATOM 11045 C CE2 . PHE I 5 112 ? 15.946  91.147  15.265 1.000 159.230 0 112 PHE III CE2 1 ? 12 
ATOM 11046 C CZ  . PHE I 5 112 ? 15.863  92.394  15.853 1.000 154.398 0 112 PHE III CZ  1 ? 12 
ATOM 11047 N N   . PHE I 5 113 ? 18.764  87.271  17.295 1.000 155.976 0 113 PHE III N   1 ? 12 
ATOM 11048 C CA  . PHE I 5 113 ? 19.607  86.994  16.144 1.000 148.186 0 113 PHE III CA  1 ? 12 
ATOM 11049 C C   . PHE I 5 113 ? 18.813  86.173  15.141 1.000 155.048 0 113 PHE III C   1 ? 12 
ATOM 11050 O O   . PHE I 5 113 ? 18.125  85.218  15.515 1.000 165.534 0 113 PHE III O   1 ? 12 
ATOM 11051 C CB  . PHE I 5 113 ? 20.907  86.292  16.571 1.000 140.925 0 113 PHE III CB  1 ? 12 
ATOM 11052 C CG  . PHE I 5 113 ? 20.729  84.863  17.014 1.000 148.675 0 113 PHE III CG  1 ? 12 
ATOM 11053 C CD1 . PHE I 5 113 ? 20.398  84.564  18.326 1.000 162.883 0 113 PHE III CD1 1 ? 12 
ATOM 11054 C CD2 . PHE I 5 113 ? 20.949  83.818  16.133 1.000 152.689 0 113 PHE III CD2 1 ? 12 
ATOM 11055 C CE1 . PHE I 5 113 ? 20.259  83.250  18.740 1.000 168.448 0 113 PHE III CE1 1 ? 12 
ATOM 11056 C CE2 . PHE I 5 113 ? 20.808  82.505  16.542 1.000 157.466 0 113 PHE III CE2 1 ? 12 
ATOM 11057 C CZ  . PHE I 5 113 ? 20.465  82.220  17.844 1.000 162.096 0 113 PHE III CZ  1 ? 12 
ATOM 11058 N N   . ILE I 5 114 ? 18.898  86.563  13.875 1.000 151.637 0 114 ILE III N   1 ? 12 
ATOM 11059 C CA  . ILE I 5 114 ? 18.195  85.897  12.787 1.000 149.513 0 114 ILE III CA  1 ? 12 
ATOM 11060 C C   . ILE I 5 114 ? 19.218  85.025  12.081 1.000 153.021 0 114 ILE III C   1 ? 12 
ATOM 11061 O O   . ILE I 5 114 ? 20.181  85.537  11.500 1.000 152.001 0 114 ILE III O   1 ? 12 
ATOM 11062 C CB  . ILE I 5 114 ? 17.569  86.904  11.814 1.000 143.599 0 114 ILE III CB  1 ? 12 
ATOM 11063 C CG1 . ILE I 5 114 ? 16.954  88.070  12.581 1.000 142.036 0 114 ILE III CG1 1 ? 12 
ATOM 11064 C CG2 . ILE I 5 114 ? 16.528  86.218  10.940 1.000 153.984 0 114 ILE III CG2 1 ? 12 
ATOM 11065 C CD1 . ILE I 5 114 ? 16.672  89.269  11.713 1.000 141.379 0 114 ILE III CD1 1 ? 12 
ATOM 11066 N N   . CYS I 5 115 ? 19.030  83.711  12.134 1.000 155.670 0 115 CYS III N   1 ? 12 
ATOM 11067 C CA  . CYS I 5 115 ? 19.997  82.822  11.511 1.000 156.382 0 115 CYS III CA  1 ? 12 
ATOM 11068 C C   . CYS I 5 115 ? 19.944  82.943  9.995  1.000 153.829 0 115 CYS III C   1 ? 12 
ATOM 11069 O O   . CYS I 5 115 ? 18.869  83.048  9.397  1.000 158.271 0 115 CYS III O   1 ? 12 
ATOM 11070 C CB  . CYS I 5 115 ? 19.728  81.366  11.894 1.000 162.873 0 115 CYS III CB  1 ? 12 
ATOM 11071 S SG  . CYS I 5 115 ? 19.897  80.963  13.632 1.000 183.487 0 115 CYS III SG  1 ? 12 
ATOM 11072 N N   . THR I 5 116 ? 21.120  82.928  9.372  1.000 147.559 0 116 THR III N   1 ? 12 
ATOM 11073 C CA  . THR I 5 116 ? 21.216  82.925  7.921  1.000 146.047 0 116 THR III CA  1 ? 12 
ATOM 11074 C C   . THR I 5 116 ? 21.867  81.635  7.456  1.000 148.531 0 116 THR III C   1 ? 12 
ATOM 11075 O O   . THR I 5 116 ? 22.251  81.514  6.286  1.000 151.672 0 116 THR III O   1 ? 12 
ATOM 11076 C CB  . THR I 5 116 ? 22.014  84.132  7.423  1.000 136.557 0 116 THR III CB  1 ? 12 
ATOM 11077 O OG1 . THR I 5 116 ? 23.309  84.131  8.034  1.000 142.611 0 116 THR III OG1 1 ? 12 
ATOM 11078 C CG2 . THR I 5 116 ? 21.294  85.426  7.776  1.000 129.702 0 116 THR III CG2 1 ? 12 
ATOM 11079 N N   . ALA I 5 117 ? 22.018  80.684  8.369  1.000 148.197 0 117 ALA III N   1 ? 12 
ATOM 11080 C CA  . ALA I 5 117 ? 22.524  79.352  8.097  1.000 159.318 0 117 ALA III CA  1 ? 12 
ATOM 11081 C C   . ALA I 5 117 ? 21.999  78.440  9.196  1.000 173.008 0 117 ALA III C   1 ? 12 
ATOM 11082 O O   . ALA I 5 117 ? 21.439  78.898  10.195 1.000 173.964 0 117 ALA III O   1 ? 12 
ATOM 11083 C CB  . ALA I 5 117 ? 24.052  79.332  8.025  1.000 159.346 0 117 ALA III CB  1 ? 12 
ATOM 11084 N N   . LYS I 5 118 ? 22.175  77.139  8.993  1.000 185.396 0 118 LYS III N   1 ? 12 
ATOM 11085 C CA  . LYS I 5 118 ? 21.874  76.171  10.040 1.000 194.479 0 118 LYS III CA  1 ? 12 
ATOM 11086 C C   . LYS I 5 118 ? 22.976  76.314  11.092 1.000 200.751 0 118 LYS III C   1 ? 12 
ATOM 11087 O O   . LYS I 5 118 ? 24.166  76.282  10.758 1.000 196.048 0 118 LYS III O   1 ? 12 
ATOM 11088 C CB  . LYS I 5 118 ? 21.760  74.767  9.451  1.000 197.884 0 118 LYS III CB  1 ? 12 
ATOM 11089 C CG  . LYS I 5 118 ? 21.431  73.659  10.437 1.000 206.635 0 118 LYS III CG  1 ? 12 
ATOM 11090 C CD  . LYS I 5 118 ? 21.258  72.348  9.662  1.000 200.437 0 118 LYS III CD  1 ? 12 
ATOM 11091 C CE  . LYS I 5 118 ? 20.895  71.147  10.540 1.000 202.649 0 118 LYS III CE  1 ? 12 
ATOM 11092 N NZ  . LYS I 5 118 ? 22.080  70.454  11.115 1.000 206.939 0 118 LYS III NZ  1 ? 12 
ATOM 11093 N N   . THR I 5 119 ? 22.593  76.463  12.368 1.000 206.063 0 119 THR III N   1 ? 12 
ATOM 11094 C CA  . THR I 5 119 ? 23.541  76.756  13.455 1.000 203.935 0 119 THR III CA  1 ? 12 
ATOM 11095 C C   . THR I 5 119 ? 23.403  75.775  14.623 1.000 216.965 0 119 THR III C   1 ? 12 
ATOM 11096 O O   . THR I 5 119 ? 22.964  76.139  15.717 1.000 220.377 0 119 THR III O   1 ? 12 
ATOM 11097 C CB  . THR I 5 119 ? 23.341  78.196  13.949 1.000 191.559 0 119 THR III CB  1 ? 12 
ATOM 11098 O OG1 . THR I 5 119 ? 21.987  78.364  14.392 1.000 190.062 0 119 THR III OG1 1 ? 12 
ATOM 11099 C CG2 . THR I 5 119 ? 23.617  79.197  12.838 1.000 185.006 0 119 THR III CG2 1 ? 12 
ATOM 11100 N N   . GLU I 5 120 ? 23.771  74.515  14.377 1.000 228.450 0 120 GLU III N   1 ? 12 
ATOM 11101 C CA  . GLU I 5 120 ? 23.438  73.449  15.313 1.000 239.222 0 120 GLU III CA  1 ? 12 
ATOM 11102 C C   . GLU I 5 120 ? 24.167  73.597  16.644 1.000 235.508 0 120 GLU III C   1 ? 12 
ATOM 11103 O O   . GLU I 5 120 ? 23.681  73.101  17.665 1.000 240.906 0 120 GLU III O   1 ? 12 
ATOM 11104 C CB  . GLU I 5 120 ? 23.829  72.106  14.704 1.000 254.871 0 120 GLU III CB  1 ? 12 
ATOM 11105 C CG  . GLU I 5 120 ? 23.558  72.010  13.224 1.000 261.547 0 120 GLU III CG  1 ? 12 
ATOM 11106 C CD  . GLU I 5 120 ? 24.706  72.573  12.393 1.000 261.240 0 120 GLU III CD  1 ? 12 
ATOM 11107 O OE1 . GLU I 5 120 ? 25.610  73.206  12.980 1.000 259.365 0 120 GLU III OE1 1 ? 12 
ATOM 11108 O OE2 . GLU I 5 120 ? 24.703  72.395  11.157 1.000 263.885 0 120 GLU III OE2 1 ? 12 
ATOM 11109 N N   . TRP I 5 121 ? 25.329  74.261  16.665 1.000 213.919 0 121 TRP III N   1 ? 12 
ATOM 11110 C CA  . TRP I 5 121 ? 26.044  74.415  17.928 1.000 207.683 0 121 TRP III CA  1 ? 12 
ATOM 11111 C C   . TRP I 5 121 ? 25.327  75.334  18.906 1.000 204.027 0 121 TRP III C   1 ? 12 
ATOM 11112 O O   . TRP I 5 121 ? 25.685  75.350  20.089 1.000 209.530 0 121 TRP III O   1 ? 12 
ATOM 11113 C CB  . TRP I 5 121 ? 27.465  74.913  17.659 1.000 205.901 0 121 TRP III CB  1 ? 12 
ATOM 11114 C CG  . TRP I 5 121 ? 27.503  76.253  17.017 1.000 200.537 0 121 TRP III CG  1 ? 12 
ATOM 11115 C CD1 . TRP I 5 121 ? 27.555  77.466  17.637 1.000 192.474 0 121 TRP III CD1 1 ? 12 
ATOM 11116 C CD2 . TRP I 5 121 ? 27.430  76.519  15.614 1.000 200.842 0 121 TRP III CD2 1 ? 12 
ATOM 11117 N NE1 . TRP I 5 121 ? 27.553  78.474  16.701 1.000 186.884 0 121 TRP III NE1 1 ? 12 
ATOM 11118 C CE2 . TRP I 5 121 ? 27.472  77.917  15.451 1.000 189.160 0 121 TRP III CE2 1 ? 12 
ATOM 11119 C CE3 . TRP I 5 121 ? 27.345  75.709  14.477 1.000 204.711 0 121 TRP III CE3 1 ? 12 
ATOM 11120 C CZ2 . TRP I 5 121 ? 27.433  78.522  14.198 1.000 184.801 0 121 TRP III CZ2 1 ? 12 
ATOM 11121 C CZ3 . TRP I 5 121 ? 27.305  76.311  13.235 1.000 202.381 0 121 TRP III CZ3 1 ? 12 
ATOM 11122 C CH2 . TRP I 5 121 ? 27.349  77.704  13.104 1.000 193.810 0 121 TRP III CH2 1 ? 12 
ATOM 11123 N N   . LEU I 5 122 ? 24.336  76.097  18.447 1.000 216.203 0 122 LEU III N   1 ? 12 
ATOM 11124 C CA  . LEU I 5 122 ? 23.537  76.930  19.331 1.000 218.267 0 122 LEU III CA  1 ? 12 
ATOM 11125 C C   . LEU I 5 122 ? 22.339  76.179  19.886 1.000 232.484 0 122 LEU III C   1 ? 12 
ATOM 11126 O O   . LEU I 5 122 ? 21.656  76.698  20.776 1.000 239.641 0 122 LEU III O   1 ? 12 
ATOM 11127 C CB  . LEU I 5 122 ? 23.089  78.211  18.617 1.000 207.537 0 122 LEU III CB  1 ? 12 
ATOM 11128 C CG  . LEU I 5 122 ? 24.250  79.060  18.089 1.000 201.220 0 122 LEU III CG  1 ? 12 
ATOM 11129 C CD1 . LEU I 5 122 ? 23.748  80.266  17.311 1.000 191.612 0 122 LEU III CD1 1 ? 12 
ATOM 11130 C CD2 . LEU I 5 122 ? 25.164  79.490  19.231 1.000 197.142 0 122 LEU III CD2 1 ? 12 
ATOM 11131 N N   . ASP I 5 123 ? 22.062  74.984  19.360 1.000 242.547 0 123 ASP III N   1 ? 12 
ATOM 11132 C CA  . ASP I 5 123 ? 20.922  74.198  19.806 1.000 253.837 0 123 ASP III CA  1 ? 12 
ATOM 11133 C C   . ASP I 5 123 ? 21.074  73.893  21.288 1.000 256.371 0 123 ASP III C   1 ? 12 
ATOM 11134 O O   . ASP I 5 123 ? 22.140  73.463  21.736 1.000 258.275 0 123 ASP III O   1 ? 12 
ATOM 11135 C CB  . ASP I 5 123 ? 20.839  72.900  19.006 1.000 263.146 0 123 ASP III CB  1 ? 12 
ATOM 11136 C CG  . ASP I 5 123 ? 20.436  73.132  17.569 1.000 262.024 0 123 ASP III CG  1 ? 12 
ATOM 11137 O OD1 . ASP I 5 123 ? 19.973  74.247  17.267 1.000 261.731 0 123 ASP III OD1 1 ? 12 
ATOM 11138 O OD2 . ASP I 5 123 ? 20.610  72.217  16.737 1.000 260.339 0 123 ASP III OD2 1 ? 12 
ATOM 11139 N N   . GLY I 5 124 ? 20.009  74.114  22.050 1.000 244.878 0 124 GLY III N   1 ? 12 
ATOM 11140 C CA  . GLY I 5 124 ? 20.052  73.805  23.460 1.000 236.448 0 124 GLY III CA  1 ? 12 
ATOM 11141 C C   . GLY I 5 124 ? 20.660  74.897  24.308 1.000 226.091 0 124 GLY III C   1 ? 12 
ATOM 11142 O O   . GLY I 5 124 ? 20.708  74.754  25.536 1.000 230.168 0 124 GLY III O   1 ? 12 
ATOM 11143 N N   . LYS I 5 125 ? 21.122  75.979  23.689 1.000 219.957 0 125 LYS III N   1 ? 12 
ATOM 11144 C CA  . LYS I 5 125 ? 21.731  77.116  24.362 1.000 207.272 0 125 LYS III CA  1 ? 12 
ATOM 11145 C C   . LYS I 5 125 ? 20.960  78.408  24.145 1.000 202.691 0 125 LYS III C   1 ? 12 
ATOM 11146 O O   . LYS I 5 125 ? 20.964  79.268  25.028 1.000 204.441 0 125 LYS III O   1 ? 12 
ATOM 11147 C CB  . LYS I 5 125 ? 23.188  77.272  23.897 1.000 196.562 0 125 LYS III CB  1 ? 12 
ATOM 11148 C CG  . LYS I 5 125 ? 23.947  75.948  23.978 1.000 194.956 0 125 LYS III CG  1 ? 12 
ATOM 11149 C CD  . LYS I 5 125 ? 25.414  76.053  23.605 1.000 190.350 0 125 LYS III CD  1 ? 12 
ATOM 11150 C CE  . LYS I 5 125 ? 26.096  74.702  23.792 1.000 184.576 0 125 LYS III CE  1 ? 12 
ATOM 11151 N NZ  . LYS I 5 125 ? 27.560  74.811  24.043 1.000 171.725 0 125 LYS III NZ  1 ? 12 
ATOM 11152 N N   . HIS I 5 126 ? 20.312  78.568  22.992 1.000 209.855 0 126 HIS III N   1 ? 12 
ATOM 11153 C CA  . HIS I 5 126 ? 19.530  79.750  22.663 1.000 206.361 0 126 HIS III CA  1 ? 12 
ATOM 11154 C C   . HIS I 5 126 ? 18.105  79.309  22.351 1.000 208.437 0 126 HIS III C   1 ? 12 
ATOM 11155 O O   . HIS I 5 126 ? 17.870  78.171  21.933 1.000 211.397 0 126 HIS III O   1 ? 12 
ATOM 11156 C CB  . HIS I 5 126 ? 20.117  80.519  21.467 1.000 206.556 0 126 HIS III CB  1 ? 12 
ATOM 11157 C CG  . HIS I 5 126 ? 21.479  81.094  21.715 1.000 205.274 0 126 HIS III CG  1 ? 12 
ATOM 11158 N ND1 . HIS I 5 126 ? 21.671  82.397  22.122 1.000 202.140 0 126 HIS III ND1 1 ? 12 
ATOM 11159 C CD2 . HIS I 5 126 ? 22.714  80.551  21.598 1.000 203.560 0 126 HIS III CD2 1 ? 12 
ATOM 11160 C CE1 . HIS I 5 126 ? 22.965  82.629  22.254 1.000 196.807 0 126 HIS III CE1 1 ? 12 
ATOM 11161 N NE2 . HIS I 5 126 ? 23.620  81.526  21.942 1.000 193.551 0 126 HIS III NE2 1 ? 12 
ATOM 11162 N N   . VAL I 5 127 ? 17.153  80.216  22.548 1.000 210.176 0 127 VAL III N   1 ? 12 
ATOM 11163 C CA  . VAL I 5 127 ? 15.732  79.879  22.540 1.000 215.790 0 127 VAL III CA  1 ? 12 
ATOM 11164 C C   . VAL I 5 127 ? 15.116  80.335  21.225 1.000 212.710 0 127 VAL III C   1 ? 12 
ATOM 11165 O O   . VAL I 5 127 ? 15.101  81.533  20.921 1.000 215.558 0 127 VAL III O   1 ? 12 
ATOM 11166 C CB  . VAL I 5 127 ? 14.996  80.513  23.731 1.000 222.592 0 127 VAL III CB  1 ? 12 
ATOM 11167 C CG1 . VAL I 5 127 ? 13.503  80.246  23.631 1.000 233.532 0 127 VAL III CG1 1 ? 12 
ATOM 11168 C CG2 . VAL I 5 127 ? 15.546  79.985  25.041 1.000 233.959 0 127 VAL III CG2 1 ? 12 
ATOM 11169 N N   . VAL I 5 128 ? 14.575  79.388  20.465 1.000 219.198 0 128 VAL III N   1 ? 12 
ATOM 11170 C CA  . VAL I 5 128 ? 13.932  79.694  19.191 1.000 201.925 0 128 VAL III CA  1 ? 12 
ATOM 11171 C C   . VAL I 5 128 ? 12.506  80.147  19.471 1.000 192.577 0 128 VAL III C   1 ? 12 
ATOM 11172 O O   . VAL I 5 128 ? 11.704  79.391  20.029 1.000 195.173 0 128 VAL III O   1 ? 12 
ATOM 11173 C CB  . VAL I 5 128 ? 13.945  78.476  18.256 1.000 199.813 0 128 VAL III CB  1 ? 12 
ATOM 11174 C CG1 . VAL I 5 128 ? 13.239  78.804  16.951 1.000 202.260 0 128 VAL III CG1 1 ? 12 
ATOM 11175 C CG2 . VAL I 5 128 ? 15.370  78.013  17.999 1.000 213.514 0 128 VAL III CG2 1 ? 12 
ATOM 11176 N N   . PHE I 5 129 ? 12.181  81.383  19.084 1.000 188.205 0 129 PHE III N   1 ? 12 
ATOM 11177 C CA  . PHE I 5 129 ? 10.852  81.919  19.339 1.000 193.872 0 129 PHE III CA  1 ? 12 
ATOM 11178 C C   . PHE I 5 129 ? 10.116  82.362  18.082 1.000 211.040 0 129 PHE III C   1 ? 12 
ATOM 11179 O O   . PHE I 5 129 ? 8.970   82.814  18.186 1.000 219.563 0 129 PHE III O   1 ? 12 
ATOM 11180 C CB  . PHE I 5 129 ? 10.927  83.105  20.317 1.000 196.813 0 129 PHE III CB  1 ? 12 
ATOM 11181 C CG  . PHE I 5 129 ? 11.623  84.325  19.762 1.000 188.984 0 129 PHE III CG  1 ? 12 
ATOM 11182 C CD1 . PHE I 5 129 ? 10.898  85.323  19.127 1.000 193.833 0 129 PHE III CD1 1 ? 12 
ATOM 11183 C CD2 . PHE I 5 129 ? 12.994  84.487  19.897 1.000 184.695 0 129 PHE III CD2 1 ? 12 
ATOM 11184 C CE1 . PHE I 5 129 ? 11.524  86.448  18.621 1.000 200.592 0 129 PHE III CE1 1 ? 12 
ATOM 11185 C CE2 . PHE I 5 129 ? 13.627  85.615  19.394 1.000 192.816 0 129 PHE III CE2 1 ? 12 
ATOM 11186 C CZ  . PHE I 5 129 ? 12.890  86.595  18.758 1.000 204.377 0 129 PHE III CZ  1 ? 12 
ATOM 11187 N N   . GLY I 5 130 ? 10.721  82.239  16.907 1.000 230.537 0 130 GLY III N   1 ? 12 
ATOM 11188 C CA  . GLY I 5 130 ? 10.031  82.631  15.693 1.000 240.624 0 130 GLY III CA  1 ? 12 
ATOM 11189 C C   . GLY I 5 130 ? 10.772  82.148  14.467 1.000 234.506 0 130 GLY III C   1 ? 12 
ATOM 11190 O O   . GLY I 5 130 ? 11.801  81.473  14.558 1.000 235.795 0 130 GLY III O   1 ? 12 
ATOM 11191 N N   . LYS I 5 131 ? 10.216  82.493  13.307 1.000 222.465 0 131 LYS III N   1 ? 12 
ATOM 11192 C CA  . LYS I 5 131 ? 10.850  82.172  12.039 1.000 217.277 0 131 LYS III CA  1 ? 12 
ATOM 11193 C C   . LYS I 5 131 ? 10.419  83.243  11.045 1.000 222.037 0 131 LYS III C   1 ? 12 
ATOM 11194 O O   . LYS I 5 131 ? 9.283   83.721  11.074 1.000 229.495 0 131 LYS III O   1 ? 12 
ATOM 11195 C CB  . LYS I 5 131 ? 10.490  80.758  11.549 1.000 220.799 0 131 LYS III CB  1 ? 12 
ATOM 11196 C CG  . LYS I 5 131 ? 10.845  80.476  10.085 1.000 213.979 0 131 LYS III CG  1 ? 12 
ATOM 11197 C CD  . LYS I 5 131 ? 10.710  79.002  9.720  1.000 206.898 0 131 LYS III CD  1 ? 12 
ATOM 11198 C CE  . LYS I 5 131 ? 11.679  78.611  8.613  1.000 194.943 0 131 LYS III CE  1 ? 12 
ATOM 11199 N NZ  . LYS I 5 131 ? 11.891  79.705  7.626  1.000 196.864 0 131 LYS III NZ  1 ? 12 
ATOM 11200 N N   . VAL I 5 132 ? 11.338  83.573  10.137 1.000 222.425 0 132 VAL III N   1 ? 12 
ATOM 11201 C CA  . VAL I 5 132 ? 11.058  84.413  8.974  1.000 217.216 0 132 VAL III CA  1 ? 12 
ATOM 11202 C C   . VAL I 5 132 ? 10.007  83.803  8.059  1.000 211.862 0 132 VAL III C   1 ? 12 
ATOM 11203 O O   . VAL I 5 132 ? 10.089  82.627  7.683  1.000 208.092 0 132 VAL III O   1 ? 12 
ATOM 11204 C CB  . VAL I 5 132 ? 12.357  84.700  8.211  1.000 214.989 0 132 VAL III CB  1 ? 12 
ATOM 11205 C CG1 . VAL I 5 132 ? 12.054  85.474  6.939  1.000 209.439 0 132 VAL III CG1 1 ? 12 
ATOM 11206 C CG2 . VAL I 5 132 ? 13.318  85.476  9.099  1.000 218.358 0 132 VAL III CG2 1 ? 12 
ATOM 11207 N N   . LYS I 5 133 ? 9.002   84.605  7.703  1.000 222.255 0 133 LYS III N   1 ? 12 
ATOM 11208 C CA  . LYS I 5 133 ? 7.939   84.167  6.808  1.000 228.963 0 133 LYS III CA  1 ? 12 
ATOM 11209 C C   . LYS I 5 133 ? 8.167   84.661  5.385  1.000 227.385 0 133 LYS III C   1 ? 12 
ATOM 11210 O O   . LYS I 5 133 ? 8.186   83.866  4.441  1.000 216.714 0 133 LYS III O   1 ? 12 
ATOM 11211 C CB  . LYS I 5 133 ? 6.613   84.777  7.297  1.000 235.526 0 133 LYS III CB  1 ? 12 
ATOM 11212 C CG  . LYS I 5 133 ? 5.315   83.992  7.229  1.000 226.400 0 133 LYS III CG  1 ? 12 
ATOM 11213 C CD  . LYS I 5 133 ? 5.200   82.837  8.186  1.000 240.654 0 133 LYS III CD  1 ? 12 
ATOM 11214 C CE  . LYS I 5 133 ? 3.932   82.058  7.865  1.000 239.088 0 133 LYS III CE  1 ? 12 
ATOM 11215 N NZ  . LYS I 5 133 ? 2.732   82.959  7.937  1.000 241.489 0 133 LYS III NZ  1 ? 12 
ATOM 11216 N N   . GLU I 5 134 ? 8.360   85.967  5.222  1.000 231.519 0 134 GLU III N   1 ? 12 
ATOM 11217 C CA  . GLU I 5 134 ? 8.716   86.614  3.965  1.000 236.197 0 134 GLU III CA  1 ? 12 
ATOM 11218 C C   . GLU I 5 134 ? 9.863   87.598  4.151  1.000 237.246 0 134 GLU III C   1 ? 12 
ATOM 11219 O O   . GLU I 5 134 ? 10.087  88.131  5.243  1.000 237.959 0 134 GLU III O   1 ? 12 
ATOM 11220 C CB  . GLU I 5 134 ? 7.515   87.233  3.245  1.000 242.598 0 134 GLU III CB  1 ? 12 
ATOM 11221 C CG  . GLU I 5 134 ? 6.486   86.164  2.896  1.000 248.198 0 134 GLU III CG  1 ? 12 
ATOM 11222 C CD  . GLU I 5 134 ? 5.058   86.633  2.905  1.000 258.390 0 134 GLU III CD  1 ? 12 
ATOM 11223 O OE1 . GLU I 5 134 ? 4.671   87.394  3.816  1.000 263.563 0 134 GLU III OE1 1 ? 12 
ATOM 11224 O OE2 . GLU I 5 134 ? 4.316   86.225  1.986  1.000 261.075 0 134 GLU III OE2 1 ? 12 
ATOM 11225 N N   . GLY I 5 135 ? 10.588  87.819  3.060  1.000 235.500 0 135 GLY III N   1 ? 12 
ATOM 11226 C CA  . GLY I 5 135 ? 11.680  88.768  3.037  1.000 213.358 0 135 GLY III CA  1 ? 12 
ATOM 11227 C C   . GLY I 5 135 ? 13.016  88.282  3.532  1.000 196.675 0 135 GLY III C   1 ? 12 
ATOM 11228 O O   . GLY I 5 135 ? 13.833  89.090  3.988  1.000 190.124 0 135 GLY III O   1 ? 12 
ATOM 11229 N N   . MET I 5 136 ? 13.267  86.976  3.444  1.000 184.814 0 136 MET III N   1 ? 12 
ATOM 11230 C CA  . MET I 5 136 ? 14.596  86.462  3.739  1.000 177.860 0 136 MET III CA  1 ? 12 
ATOM 11231 C C   . MET I 5 136 ? 15.626  87.101  2.822  1.000 173.945 0 136 MET III C   1 ? 12 
ATOM 11232 O O   . MET I 5 136 ? 16.792  87.250  3.205  1.000 181.845 0 136 MET III O   1 ? 12 
ATOM 11233 C CB  . MET I 5 136 ? 14.627  84.939  3.588  1.000 182.024 0 136 MET III CB  1 ? 12 
ATOM 11234 C CG  . MET I 5 136 ? 14.652  84.168  4.906  1.000 192.234 0 136 MET III CG  1 ? 12 
ATOM 11235 S SD  . MET I 5 136 ? 16.055  84.586  5.965  1.000 185.272 0 136 MET III SD  1 ? 12 
ATOM 11236 C CE  . MET I 5 136 ? 17.411  84.010  4.945  1.000 179.425 0 136 MET III CE  1 ? 12 
ATOM 11237 N N   . ASN I 5 137 ? 15.214  87.468  1.601  1.000 177.669 0 137 ASN III N   1 ? 12 
ATOM 11238 C CA  . ASN I 5 137 ? 16.123  88.135  0.677  1.000 176.575 0 137 ASN III CA  1 ? 12 
ATOM 11239 C C   . ASN I 5 137 ? 16.598  89.481  1.221  1.000 171.495 0 137 ASN III C   1 ? 12 
ATOM 11240 O O   . ASN I 5 137 ? 17.707  89.921  0.894  1.000 171.854 0 137 ASN III O   1 ? 12 
ATOM 11241 C CB  . ASN I 5 137 ? 15.425  88.327  -0.676 1.000 178.963 0 137 ASN III CB  1 ? 12 
ATOM 11242 C CG  . ASN I 5 137 ? 14.782  87.047  -1.200 1.000 178.777 0 137 ASN III CG  1 ? 12 
ATOM 11243 O OD1 . ASN I 5 137 ? 13.682  87.080  -1.754 1.000 189.611 0 137 ASN III OD1 1 ? 12 
ATOM 11244 N ND2 . ASN I 5 137 ? 15.446  85.917  -0.997 1.000 172.318 0 137 ASN III ND2 1 ? 12 
ATOM 11245 N N   . ILE I 5 138 ? 15.776  90.158  2.031  1.000 158.030 0 138 ILE III N   1 ? 12 
ATOM 11246 C CA  . ILE I 5 138 ? 16.209  91.412  2.648  1.000 152.916 0 138 ILE III CA  1 ? 12 
ATOM 11247 C C   . ILE I 5 138 ? 17.193  91.130  3.777  1.000 154.874 0 138 ILE III C   1 ? 12 
ATOM 11248 O O   . ILE I 5 138 ? 18.183  91.851  3.956  1.000 151.691 0 138 ILE III O   1 ? 12 
ATOM 11249 C CB  . ILE I 5 138 ? 15.020  92.264  3.126  1.000 156.538 0 138 ILE III CB  1 ? 12 
ATOM 11250 C CG1 . ILE I 5 138 ? 14.127  92.660  1.953  1.000 171.512 0 138 ILE III CG1 1 ? 12 
ATOM 11251 C CG2 . ILE I 5 138 ? 15.514  93.516  3.820  1.000 168.123 0 138 ILE III CG2 1 ? 12 
ATOM 11252 C CD1 . ILE I 5 138 ? 13.006  91.723  1.695  1.000 199.171 0 138 ILE III CD1 1 ? 12 
ATOM 11253 N N   . VAL I 5 139 ? 16.937  90.073  4.555  1.000 151.954 0 139 VAL III N   1 ? 12 
ATOM 11254 C CA  . VAL I 5 139 ? 17.894  89.648  5.572  1.000 150.128 0 139 VAL III CA  1 ? 12 
ATOM 11255 C C   . VAL I 5 139 ? 19.227  89.312  4.926  1.000 153.684 0 139 VAL III C   1 ? 12 
ATOM 11256 O O   . VAL I 5 139 ? 20.293  89.648  5.459  1.000 169.697 0 139 VAL III O   1 ? 12 
ATOM 11257 C CB  . VAL I 5 139 ? 17.334  88.446  6.359  1.000 153.852 0 139 VAL III CB  1 ? 12 
ATOM 11258 C CG1 . VAL I 5 139 ? 18.379  87.894  7.310  1.000 170.273 0 139 VAL III CG1 1 ? 12 
ATOM 11259 C CG2 . VAL I 5 139 ? 16.090  88.844  7.129  1.000 162.959 0 139 VAL III CG2 1 ? 12 
ATOM 11260 N N   . GLU I 5 140 ? 19.194  88.646  3.771  1.000 152.096 0 140 GLU III N   1 ? 12 
ATOM 11261 C CA  . GLU I 5 140 ? 20.437  88.344  3.073  1.000 146.995 0 140 GLU III CA  1 ? 12 
ATOM 11262 C C   . GLU I 5 140 ? 21.118  89.633  2.633  1.000 141.908 0 140 GLU III C   1 ? 12 
ATOM 11263 O O   . GLU I 5 140 ? 22.329  89.790  2.810  1.000 144.097 0 140 GLU III O   1 ? 12 
ATOM 11264 C CB  . GLU I 5 140 ? 20.198  87.407  1.885  1.000 153.703 0 140 GLU III CB  1 ? 12 
ATOM 11265 C CG  . GLU I 5 140 ? 19.791  85.977  2.270  1.000 161.385 0 140 GLU III CG  1 ? 12 
ATOM 11266 C CD  . GLU I 5 140 ? 19.288  85.159  1.085  1.000 171.814 0 140 GLU III CD  1 ? 12 
ATOM 11267 O OE1 . GLU I 5 140 ? 19.115  85.732  -0.012 1.000 165.467 0 140 GLU III OE1 1 ? 12 
ATOM 11268 O OE2 . GLU I 5 140 ? 19.092  83.934  1.245  1.000 176.461 0 140 GLU III OE2 1 ? 12 
ATOM 11269 N N   . ALA I 5 141 ? 20.320  90.624  2.225  1.000 142.917 0 141 ALA III N   1 ? 12 
ATOM 11270 C CA  . ALA I 5 141 ? 20.843  91.926  1.813  1.000 146.437 0 141 ALA III CA  1 ? 12 
ATOM 11271 C C   . ALA I 5 141 ? 21.540  92.624  2.970  1.000 147.062 0 141 ALA III C   1 ? 12 
ATOM 11272 O O   . ALA I 5 141 ? 22.540  93.323  2.769  1.000 146.335 0 141 ALA III O   1 ? 12 
ATOM 11273 C CB  . ALA I 5 141 ? 19.723  92.799  1.246  1.000 153.470 0 141 ALA III CB  1 ? 12 
ATOM 11274 N N   . MET I 5 142 ? 21.033  92.445  4.186  1.000 151.721 0 142 MET III N   1 ? 12 
ATOM 11275 C CA  . MET I 5 142 ? 21.676  93.047  5.348  1.000 154.773 0 142 MET III CA  1 ? 12 
ATOM 11276 C C   . MET I 5 142 ? 23.098  92.515  5.500  1.000 147.422 0 142 MET III C   1 ? 12 
ATOM 11277 O O   . MET I 5 142 ? 24.006  93.261  5.886  1.000 148.340 0 142 MET III O   1 ? 12 
ATOM 11278 C CB  . MET I 5 142 ? 20.850  92.773  6.599  1.000 156.335 0 142 MET III CB  1 ? 12 
ATOM 11279 C CG  . MET I 5 142 ? 19.543  93.533  6.653  1.000 152.370 0 142 MET III CG  1 ? 12 
ATOM 11280 S SD  . MET I 5 142 ? 18.505  92.849  7.943  1.000 153.285 0 142 MET III SD  1 ? 12 
ATOM 11281 C CE  . MET I 5 142 ? 19.585  93.040  9.354  1.000 147.635 0 142 MET III CE  1 ? 12 
ATOM 11282 N N   . GLU I 5 143 ? 23.311  91.230  5.191  1.000 144.126 0 143 GLU III N   1 ? 12 
ATOM 11283 C CA  . GLU I 5 143 ? 24.608  90.587  5.400  1.000 141.643 0 143 GLU III CA  1 ? 12 
ATOM 11284 C C   . GLU I 5 143 ? 25.729  91.346  4.703  1.000 137.872 0 143 GLU III C   1 ? 12 
ATOM 11285 O O   . GLU I 5 143 ? 26.876  91.323  5.168  1.000 138.585 0 143 GLU III O   1 ? 12 
ATOM 11286 C CB  . GLU I 5 143 ? 24.604  89.149  4.878  1.000 140.608 0 143 GLU III CB  1 ? 12 
ATOM 11287 C CG  . GLU I 5 143 ? 23.697  88.185  5.593  1.000 144.707 0 143 GLU III CG  1 ? 12 
ATOM 11288 C CD  . GLU I 5 143 ? 23.838  86.773  5.049  1.000 142.514 0 143 GLU III CD  1 ? 12 
ATOM 11289 O OE1 . GLU I 5 143 ? 23.619  86.567  3.836  1.000 149.538 0 143 GLU III OE1 1 ? 12 
ATOM 11290 O OE2 . GLU I 5 143 ? 24.207  85.873  5.829  1.000 137.910 0 143 GLU III OE2 1 ? 12 
ATOM 11291 N N   . ARG I 5 144 ? 25.416  92.034  3.601  1.000 142.032 0 144 ARG III N   1 ? 12 
ATOM 11292 C CA  . ARG I 5 144 ? 26.430  92.634  2.753  1.000 149.859 0 144 ARG III CA  1 ? 12 
ATOM 11293 C C   . ARG I 5 144 ? 27.068  93.845  3.386  1.000 146.072 0 144 ARG III C   1 ? 12 
ATOM 11294 O O   . ARG I 5 144 ? 28.122  94.288  2.918  1.000 157.676 0 144 ARG III O   1 ? 12 
ATOM 11295 C CB  . ARG I 5 144 ? 25.725  93.196  1.517  1.000 160.255 0 144 ARG III CB  1 ? 12 
ATOM 11296 C CG  . ARG I 5 144 ? 25.192  92.266  0.469  1.000 181.531 0 144 ARG III CG  1 ? 12 
ATOM 11297 C CD  . ARG I 5 144 ? 24.206  91.251  1.016  1.000 200.348 0 144 ARG III CD  1 ? 12 
ATOM 11298 N NE  . ARG I 5 144 ? 23.289  90.703  0.022  1.000 198.490 0 144 ARG III NE  1 ? 12 
ATOM 11299 C CZ  . ARG I 5 144 ? 22.869  89.444  0.014  1.000 190.815 0 144 ARG III CZ  1 ? 12 
ATOM 11300 N NH1 . ARG I 5 144 ? 23.272  88.574  0.927  1.000 167.450 0 144 ARG III NH1 1 ? 12 
ATOM 11301 N NH2 . ARG I 5 144 ? 22.052  89.040  -0.950 1.000 219.533 0 144 ARG III NH2 1 ? 12 
ATOM 11302 N N   . PHE I 5 145 ? 26.458  94.386  4.429  1.000 139.487 0 145 PHE III N   1 ? 12 
ATOM 11303 C CA  . PHE I 5 145 ? 27.017  95.508  5.148  1.000 141.824 0 145 PHE III CA  1 ? 12 
ATOM 11304 C C   . PHE I 5 145 ? 27.777  95.047  6.380  1.000 143.742 0 145 PHE III C   1 ? 12 
ATOM 11305 O O   . PHE I 5 145 ? 28.324  95.877  7.110  1.000 157.946 0 145 PHE III O   1 ? 12 
ATOM 11306 C CB  . PHE I 5 145 ? 25.860  96.422  5.542  1.000 149.363 0 145 PHE III CB  1 ? 12 
ATOM 11307 C CG  . PHE I 5 145 ? 25.117  96.975  4.356  1.000 144.359 0 145 PHE III CG  1 ? 12 
ATOM 11308 C CD1 . PHE I 5 145 ? 25.651  97.977  3.568  1.000 145.967 0 145 PHE III CD1 1 ? 12 
ATOM 11309 C CD2 . PHE I 5 145 ? 23.885  96.438  4.004  1.000 137.229 0 145 PHE III CD2 1 ? 12 
ATOM 11310 C CE1 . PHE I 5 145 ? 24.958  98.455  2.470  1.000 144.691 0 145 PHE III CE1 1 ? 12 
ATOM 11311 C CE2 . PHE I 5 145 ? 23.189  96.909  2.910  1.000 144.493 0 145 PHE III CE2 1 ? 12 
ATOM 11312 C CZ  . PHE I 5 145 ? 23.727  97.919  2.141  1.000 149.059 0 145 PHE III CZ  1 ? 12 
ATOM 11313 N N   . GLY I 5 146 ? 27.837  93.735  6.602  1.000 140.259 0 146 GLY III N   1 ? 12 
ATOM 11314 C CA  . GLY I 5 146 ? 28.579  93.154  7.697  1.000 136.530 0 146 GLY III CA  1 ? 12 
ATOM 11315 C C   . GLY I 5 146 ? 30.011  92.795  7.383  1.000 135.161 0 146 GLY III C   1 ? 12 
ATOM 11316 O O   . GLY I 5 146 ? 30.554  93.091  6.318  1.000 136.795 0 146 GLY III O   1 ? 12 
ATOM 11317 N N   . SER I 5 147 ? 30.630  92.142  8.362  1.000 136.784 0 147 SER III N   1 ? 12 
ATOM 11318 C CA  . SER I 5 147 ? 32.016  91.711  8.283  1.000 138.864 0 147 SER III CA  1 ? 12 
ATOM 11319 C C   . SER I 5 147 ? 32.203  90.555  9.255  1.000 137.714 0 147 SER III C   1 ? 12 
ATOM 11320 O O   . SER I 5 147 ? 31.317  90.232  10.050 1.000 138.045 0 147 SER III O   1 ? 12 
ATOM 11321 C CB  . SER I 5 147 ? 32.986  92.854  8.603  1.000 147.677 0 147 SER III CB  1 ? 12 
ATOM 11322 O OG  . SER I 5 147 ? 32.914  93.216  9.972  1.000 144.287 0 147 SER III OG  1 ? 12 
ATOM 11323 N N   . ARG I 5 148 ? 33.375  89.930  9.167  1.000 135.766 0 148 ARG III N   1 ? 12 
ATOM 11324 C CA  . ARG I 5 148 ? 33.689  88.766  9.989  1.000 135.211 0 148 ARG III CA  1 ? 12 
ATOM 11325 C C   . ARG I 5 148 ? 33.613  89.068  11.483 1.000 135.129 0 148 ARG III C   1 ? 12 
ATOM 11326 O O   . ARG I 5 148 ? 33.211  88.204  12.271 1.000 132.905 0 148 ARG III O   1 ? 12 
ATOM 11327 C CB  . ARG I 5 148 ? 35.063  88.201  9.653  1.000 138.574 0 148 ARG III CB  1 ? 12 
ATOM 11328 C CG  . ARG I 5 148 ? 35.153  87.533  8.311  1.000 141.321 0 148 ARG III CG  1 ? 12 
ATOM 11329 C CD  . ARG I 5 148 ? 36.478  87.867  7.676  1.000 155.057 0 148 ARG III CD  1 ? 12 
ATOM 11330 N NE  . ARG I 5 148 ? 37.567  87.294  8.451  1.000 175.146 0 148 ARG III NE  1 ? 12 
ATOM 11331 C CZ  . ARG I 5 148 ? 38.837  87.674  8.368  1.000 185.005 0 148 ARG III CZ  1 ? 12 
ATOM 11332 N NH1 . ARG I 5 148 ? 39.203  88.656  7.561  1.000 191.039 0 148 ARG III NH1 1 ? 12 
ATOM 11333 N NH2 . ARG I 5 148 ? 39.747  87.103  9.154  1.000 178.303 0 148 ARG III NH2 1 ? 12 
ATOM 11334 N N   . ASN I 5 149 ? 33.988  90.277  11.893 1.000 137.663 0 149 ASN III N   1 ? 12 
ATOM 11335 C CA  . ASN I 5 149 ? 33.965  90.643  13.302 1.000 139.637 0 149 ASN III CA  1 ? 12 
ATOM 11336 C C   . ASN I 5 149 ? 32.654  91.250  13.757 1.000 141.293 0 149 ASN III C   1 ? 12 
ATOM 11337 O O   . ASN I 5 149 ? 32.549  91.639  14.924 1.000 158.417 0 149 ASN III O   1 ? 12 
ATOM 11338 C CB  . ASN I 5 149 ? 35.034  91.702  13.574 1.000 145.777 0 149 ASN III CB  1 ? 12 
ATOM 11339 C CG  . ASN I 5 149 ? 36.288  91.470  12.786 1.000 176.278 0 149 ASN III CG  1 ? 12 
ATOM 11340 O OD1 . ASN I 5 149 ? 36.273  91.565  11.559 1.000 179.636 0 149 ASN III OD1 1 ? 12 
ATOM 11341 N ND2 . ASN I 5 149 ? 37.395  91.218  13.475 1.000 200.287 0 149 ASN III ND2 1 ? 12 
ATOM 11342 N N   . GLY I 5 150 ? 31.662  91.365  12.884 1.000 139.403 0 150 GLY III N   1 ? 12 
ATOM 11343 C CA  . GLY I 5 150 ? 30.344  91.778  13.302 1.000 139.059 0 150 GLY III CA  1 ? 12 
ATOM 11344 C C   . GLY I 5 150 ? 30.117  93.254  13.088 1.000 139.297 0 150 GLY III C   1 ? 12 
ATOM 11345 O O   . GLY I 5 150 ? 28.978  93.725  13.202 1.000 142.787 0 150 GLY III O   1 ? 12 
ATOM 11346 N N   . LYS I 5 151 ? 31.184  93.986  12.784 1.000 144.355 0 151 LYS III N   1 ? 12 
ATOM 11347 C CA  . LYS I 5 151 ? 31.094  95.413  12.551 1.000 150.743 0 151 LYS III CA  1 ? 12 
ATOM 11348 C C   . LYS I 5 151 ? 30.359  95.678  11.253 1.000 157.643 0 151 LYS III C   1 ? 12 
ATOM 11349 O O   . LYS I 5 151 ? 30.579  94.995  10.250 1.000 159.282 0 151 LYS III O   1 ? 12 
ATOM 11350 C CB  . LYS I 5 151 ? 32.504  95.985  12.421 1.000 156.858 0 151 LYS III CB  1 ? 12 
ATOM 11351 C CG  . LYS I 5 151 ? 32.592  97.461  12.111 1.000 163.457 0 151 LYS III CG  1 ? 12 
ATOM 11352 C CD  . LYS I 5 151 ? 34.047  97.894  12.007 1.000 170.031 0 151 LYS III CD  1 ? 12 
ATOM 11353 C CE  . LYS I 5 151 ? 34.904  97.369  13.140 1.000 183.586 0 151 LYS III CE  1 ? 12 
ATOM 11354 N NZ  . LYS I 5 151 ? 36.321  97.783  12.982 1.000 193.952 0 151 LYS III NZ  1 ? 12 
ATOM 11355 N N   . THR I 5 152 ? 29.478  96.666  11.264 1.000 166.233 0 152 THR III N   1 ? 12 
ATOM 11356 C CA  . THR I 5 152 ? 28.712  96.950  10.068 1.000 167.654 0 152 THR III CA  1 ? 12 
ATOM 11357 C C   . THR I 5 152 ? 29.412  98.080  9.333  1.000 175.646 0 152 THR III C   1 ? 12 
ATOM 11358 O O   . THR I 5 152 ? 29.972  98.984  9.961  1.000 188.098 0 152 THR III O   1 ? 12 
ATOM 11359 C CB  . THR I 5 152 ? 27.272  97.337  10.405 1.000 164.688 0 152 THR III CB  1 ? 12 
ATOM 11360 O OG1 . THR I 5 152 ? 27.274  98.499  11.243 1.000 173.488 0 152 THR III OG1 1 ? 12 
ATOM 11361 C CG2 . THR I 5 152 ? 26.577  96.197  11.130 1.000 161.797 0 152 THR III CG2 1 ? 12 
ATOM 11362 N N   . SER I 5 153 ? 29.390  98.025  8.006  1.000 168.142 0 153 SER III N   1 ? 12 
ATOM 11363 C CA  . SER I 5 153 ? 30.053  99.056  7.226  1.000 163.215 0 153 SER III CA  1 ? 12 
ATOM 11364 C C   . SER I 5 153 ? 29.152  100.259 7.022  1.000 164.067 0 153 SER III C   1 ? 12 
ATOM 11365 O O   . SER I 5 153 ? 29.641  101.344 6.688  1.000 166.036 0 153 SER III O   1 ? 12 
ATOM 11366 C CB  . SER I 5 153 ? 30.505  98.503  5.869  1.000 166.381 0 153 SER III CB  1 ? 12 
ATOM 11367 O OG  . SER I 5 153 ? 29.415  97.971  5.137  1.000 156.462 0 153 SER III OG  1 ? 12 
ATOM 11368 N N   . LYS I 5 154 ? 27.852  100.079 7.247  1.000 162.708 0 154 LYS III N   1 ? 12 
ATOM 11369 C CA  . LYS I 5 154 ? 26.860  101.139 7.208  1.000 166.927 0 154 LYS III CA  1 ? 12 
ATOM 11370 C C   . LYS I 5 154 ? 25.902  100.911 8.373  1.000 166.331 0 154 LYS III C   1 ? 12 
ATOM 11371 O O   . LYS I 5 154 ? 25.820  99.808  8.919  1.000 164.645 0 154 LYS III O   1 ? 12 
ATOM 11372 C CB  . LYS I 5 154 ? 26.105  101.137 5.871  1.000 167.400 0 154 LYS III CB  1 ? 12 
ATOM 11373 C CG  . LYS I 5 154 ? 26.935  101.576 4.654  1.000 166.872 0 154 LYS III CG  1 ? 12 
ATOM 11374 C CD  . LYS I 5 154 ? 27.482  102.993 4.731  1.000 174.336 0 154 LYS III CD  1 ? 12 
ATOM 11375 C CE  . LYS I 5 154 ? 28.616  103.174 3.721  1.000 164.338 0 154 LYS III CE  1 ? 12 
ATOM 11376 N NZ  . LYS I 5 154 ? 29.815  102.353 4.043  1.000 161.576 0 154 LYS III NZ  1 ? 12 
ATOM 11377 N N   . LYS I 5 155 ? 25.175  101.955 8.765  1.000 162.300 0 155 LYS III N   1 ? 12 
ATOM 11378 C CA  . LYS I 5 155 ? 24.264  101.849 9.902  1.000 160.394 0 155 LYS III CA  1 ? 12 
ATOM 11379 C C   . LYS I 5 155 ? 22.939  101.222 9.473  1.000 162.129 0 155 LYS III C   1 ? 12 
ATOM 11380 O O   . LYS I 5 155 ? 22.257  101.741 8.582  1.000 178.777 0 155 LYS III O   1 ? 12 
ATOM 11381 C CB  . LYS I 5 155 ? 24.020  103.219 10.530 1.000 174.285 0 155 LYS III CB  1 ? 12 
ATOM 11382 C CG  . LYS I 5 155 ? 22.899  103.208 11.561 1.000 183.887 0 155 LYS III CG  1 ? 12 
ATOM 11383 C CD  . LYS I 5 155 ? 22.757  104.536 12.281 1.000 192.001 0 155 LYS III CD  1 ? 12 
ATOM 11384 C CE  . LYS I 5 155 ? 24.020  104.904 13.034 1.000 202.259 0 155 LYS III CE  1 ? 12 
ATOM 11385 N NZ  . LYS I 5 155 ? 23.822  106.106 13.878 1.000 207.068 0 155 LYS III NZ  1 ? 12 
ATOM 11386 N N   . ILE I 5 156 ? 22.585  100.103 10.106 1.000 155.402 0 156 ILE III N   1 ? 12 
ATOM 11387 C CA  . ILE I 5 156 ? 21.355  99.364  9.827  1.000 157.752 0 156 ILE III CA  1 ? 12 
ATOM 11388 C C   . ILE I 5 156 ? 20.342  99.654  10.930 1.000 163.178 0 156 ILE III C   1 ? 12 
ATOM 11389 O O   . ILE I 5 156 ? 20.582  99.329  12.098 1.000 163.596 0 156 ILE III O   1 ? 12 
ATOM 11390 C CB  . ILE I 5 156 ? 21.624  97.855  9.720  1.000 149.622 0 156 ILE III CB  1 ? 12 
ATOM 11391 C CG1 . ILE I 5 156 ? 22.876  97.599  8.881  1.000 152.626 0 156 ILE III CG1 1 ? 12 
ATOM 11392 C CG2 . ILE I 5 156 ? 20.415  97.133  9.137  1.000 151.094 0 156 ILE III CG2 1 ? 12 
ATOM 11393 C CD1 . ILE I 5 156 ? 22.712  97.951  7.426  1.000 152.376 0 156 ILE III CD1 1 ? 12 
ATOM 11394 N N   . THR I 5 157 ? 19.211  100.264 10.567 1.000 169.489 0 157 THR III N   1 ? 12 
ATOM 11395 C CA  . THR I 5 157 ? 18.213  100.725 11.527 1.000 176.237 0 157 THR III CA  1 ? 12 
ATOM 11396 C C   . THR I 5 157 ? 16.864  100.062 11.265 1.000 184.527 0 157 THR III C   1 ? 12 
ATOM 11397 O O   . THR I 5 157 ? 16.492  99.832  10.109 1.000 196.393 0 157 THR III O   1 ? 12 
ATOM 11398 C CB  . THR I 5 157 ? 18.053  102.250 11.461 1.000 179.241 0 157 THR III CB  1 ? 12 
ATOM 11399 O OG1 . THR I 5 157 ? 19.341  102.865 11.330 1.000 175.336 0 157 THR III OG1 1 ? 12 
ATOM 11400 C CG2 . THR I 5 157 ? 17.368  102.774 12.721 1.000 186.110 0 157 THR III CG2 1 ? 12 
ATOM 11401 N N   . ILE I 5 158 ? 16.139  99.749  12.342 1.000 180.858 0 158 ILE III N   1 ? 12 
ATOM 11402 C CA  . ILE I 5 158 ? 14.773  99.229  12.259 1.000 181.232 0 158 ILE III CA  1 ? 12 
ATOM 11403 C C   . ILE I 5 158 ? 13.814  100.418 12.315 1.000 191.303 0 158 ILE III C   1 ? 12 
ATOM 11404 O O   . ILE I 5 158 ? 13.555  100.985 13.378 1.000 201.202 0 158 ILE III O   1 ? 12 
ATOM 11405 C CB  . ILE I 5 158 ? 14.478  98.201  13.352 1.000 176.643 0 158 ILE III CB  1 ? 12 
ATOM 11406 C CG1 . ILE I 5 158 ? 15.593  97.163  13.429 1.000 179.447 0 158 ILE III CG1 1 ? 12 
ATOM 11407 C CG2 . ILE I 5 158 ? 13.196  97.468  13.042 1.000 175.969 0 158 ILE III CG2 1 ? 12 
ATOM 11408 C CD1 . ILE I 5 158 ? 15.539  96.318  14.683 1.000 190.081 0 158 ILE III CD1 1 ? 12 
ATOM 11409 N N   . ALA I 5 159 ? 13.290  100.792 11.146 1.000 202.248 0 159 ALA III N   1 ? 12 
ATOM 11410 C CA  . ALA I 5 159 ? 12.458  101.981 10.973 1.000 204.734 0 159 ALA III CA  1 ? 12 
ATOM 11411 C C   . ALA I 5 159 ? 11.038  101.826 11.519 1.000 222.864 0 159 ALA III C   1 ? 12 
ATOM 11412 O O   . ALA I 5 159 ? 10.472  102.798 12.034 1.000 226.584 0 159 ALA III O   1 ? 12 
ATOM 11413 C CB  . ALA I 5 159 ? 12.406  102.362 9.494  1.000 212.927 0 159 ALA III CB  1 ? 12 
ATOM 11414 N N   . ASP I 5 160 ? 10.459  100.628 11.449 1.000 238.371 0 160 ASP III N   1 ? 12 
ATOM 11415 C CA  . ASP I 5 160 ? 9.116   100.385 11.968 1.000 253.189 0 160 ASP III CA  1 ? 12 
ATOM 11416 C C   . ASP I 5 160 ? 8.969   98.937  12.409 1.000 259.687 0 160 ASP III C   1 ? 12 
ATOM 11417 O O   . ASP I 5 160 ? 9.689   98.048  11.947 1.000 259.525 0 160 ASP III O   1 ? 12 
ATOM 11418 C CB  . ASP I 5 160 ? 8.033   100.726 10.936 1.000 266.192 0 160 ASP III CB  1 ? 12 
ATOM 11419 C CG  . ASP I 5 160 ? 7.787   102.210 10.829 1.000 280.544 0 160 ASP III CG  1 ? 12 
ATOM 11420 O OD1 . ASP I 5 160 ? 7.490   102.830 11.872 1.000 285.685 0 160 ASP III OD1 1 ? 12 
ATOM 11421 O OD2 . ASP I 5 160 ? 7.896   102.755 9.711  1.000 285.191 0 160 ASP III OD2 1 ? 12 
ATOM 11422 N N   . CYS I 5 161 ? 7.986   98.711  13.283 1.000 279.031 0 161 CYS III N   1 ? 12 
ATOM 11423 C CA  . CYS I 5 161 ? 7.669   97.372  13.762 1.000 284.124 0 161 CYS III CA  1 ? 12 
ATOM 11424 C C   . CYS I 5 161 ? 6.216   97.362  14.218 1.000 285.229 0 161 CYS III C   1 ? 12 
ATOM 11425 O O   . CYS I 5 161 ? 5.619   98.408  14.485 1.000 284.642 0 161 CYS III O   1 ? 12 
ATOM 11426 C CB  . CYS I 5 161 ? 8.558   96.965  14.949 1.000 289.746 0 161 CYS III CB  1 ? 12 
ATOM 11427 S SG  . CYS I 5 161 ? 10.333  97.335  14.927 1.000 374.045 0 161 CYS III SG  1 ? 12 
ATOM 11428 N N   . GLY I 5 162 ? 5.661   96.158  14.313 1.000 277.559 0 162 GLY III N   1 ? 12 
ATOM 11429 C CA  . GLY I 5 162 ? 4.273   96.006  14.696 1.000 282.098 0 162 GLY III CA  1 ? 12 
ATOM 11430 C C   . GLY I 5 162 ? 3.823   94.564  14.553 1.000 279.728 0 162 GLY III C   1 ? 12 
ATOM 11431 O O   . GLY I 5 162 ? 4.632   93.644  14.426 1.000 269.362 0 162 GLY III O   1 ? 12 
ATOM 11432 N N   . GLN I 5 163 ? 2.505   94.398  14.582 1.000 291.758 0 163 GLN III N   1 ? 12 
ATOM 11433 C CA  . GLN I 5 163 ? 1.830   93.107  14.512 1.000 296.205 0 163 GLN III CA  1 ? 12 
ATOM 11434 C C   . GLN I 5 163 ? 1.254   93.003  13.110 1.000 310.990 0 163 GLN III C   1 ? 12 
ATOM 11435 O O   . GLN I 5 163 ? 0.566   93.917  12.644 1.000 298.728 0 163 GLN III O   1 ? 12 
ATOM 11436 C CB  . GLN I 5 163 ? 0.719   92.971  15.557 1.000 274.529 0 163 GLN III CB  1 ? 12 
ATOM 11437 C CG  . GLN I 5 163 ? -0.028  91.622  15.512 1.000 271.620 0 163 GLN III CG  1 ? 12 
ATOM 11438 C CD  . GLN I 5 163 ? 0.720   90.456  16.108 1.000 268.426 0 163 GLN III CD  1 ? 12 
ATOM 11439 O OE1 . GLN I 5 163 ? 0.569   89.319  15.661 1.000 274.010 0 163 GLN III OE1 1 ? 12 
ATOM 11440 N NE2 . GLN I 5 163 ? 1.503   90.721  17.139 1.000 258.264 0 163 GLN III NE2 1 ? 12 
ATOM 11441 N N   . LEU I 5 164 ? 1.534   91.881  12.452 1.000 319.632 0 164 LEU III N   1 ? 12 
ATOM 11442 C CA  . LEU I 5 164 ? 0.947   91.585  11.160 1.000 336.830 0 164 LEU III CA  1 ? 12 
ATOM 11443 C C   . LEU I 5 164 ? -0.334  90.786  11.306 1.000 355.296 0 164 LEU III C   1 ? 12 
ATOM 11444 O O   . LEU I 5 164 ? -0.427  89.850  12.106 1.000 360.410 0 164 LEU III O   1 ? 12 
ATOM 11445 C CB  . LEU I 5 164 ? 1.953   90.783  10.327 1.000 331.219 0 164 LEU III CB  1 ? 12 
ATOM 11446 C CG  . LEU I 5 164 ? 1.697   90.448  8.861  1.000 331.070 0 164 LEU III CG  1 ? 12 
ATOM 11447 C CD1 . LEU I 5 164 ? 1.739   91.702  8.023  1.000 325.552 0 164 LEU III CD1 1 ? 12 
ATOM 11448 C CD2 . LEU I 5 164 ? 2.718   89.428  8.371  1.000 312.544 0 164 LEU III CD2 1 ? 12 
ATOM 11449 N N   . GLU I 5 165 ? -1.319  91.187  10.513 1.000 368.169 0 165 GLU III N   1 ? 12 
ATOM 11450 C CA  . GLU I 5 165 ? -2.652  90.627  10.468 1.000 380.396 0 165 GLU III CA  1 ? 12 
ATOM 11451 C C   . GLU I 5 165 ? -2.795  89.613  9.340  1.000 394.663 0 165 GLU III C   1 ? 12 
ATOM 11452 O O   . GLU I 5 165 ? -3.325  89.934  8.276  1.000 412.751 0 165 GLU III O   1 ? 12 
ATOM 11453 C CB  . GLU I 5 165 ? -3.658  91.772  10.322 1.000 382.671 0 165 GLU III CB  1 ? 12 
ATOM 11454 C CG  . GLU I 5 165 ? -3.309  92.990  11.196 1.000 371.484 0 165 GLU III CG  1 ? 12 
ATOM 11455 C CD  . GLU I 5 165 ? -2.375  93.988  10.519 1.000 364.600 0 165 GLU III CD  1 ? 12 
ATOM 11456 O OE1 . GLU I 5 165 ? -2.148  93.866  9.298  1.000 372.157 0 165 GLU III OE1 1 ? 12 
ATOM 11457 O OE2 . GLU I 5 165 ? -1.859  94.888  11.218 1.000 356.577 0 165 GLU III OE2 1 ? 12 
ATOM 11458 O OXT . GLU I 5 165 ? -2.377  88.461  9.458  1.000 403.343 0 165 GLU III OXT 1 ? 12 
# 
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   . PRO A 1   ? 1.068 1.426 1.149 -0.048 0.105  0.024  1   PRO BBB N   
2     C CA  . PRO A 1   ? 1.053 1.413 1.135 -0.052 0.101  0.020  1   PRO BBB CA  
3     C C   . PRO A 1   ? 1.094 1.455 1.173 -0.050 0.104  0.022  1   PRO BBB C   
4     O O   . PRO A 1   ? 1.212 1.575 1.292 -0.046 0.109  0.026  1   PRO BBB O   
5     C CB  A PRO A 1   ? 1.114 1.480 1.205 -0.054 0.093  0.021  1   PRO BBB CB  
6     C CG  A PRO A 1   ? 1.103 1.474 1.201 -0.051 0.093  0.027  1   PRO BBB CG  
7     C CD  A PRO A 1   ? 1.120 1.485 1.209 -0.048 0.100  0.027  1   PRO BBB CD  
8     N N   . ILE A 2   ? 1.004 1.367 1.082 -0.052 0.101  0.019  2   ILE BBB N   
9     C CA  . ILE A 2   ? 0.994 1.362 1.070 -0.050 0.104  0.022  2   ILE BBB CA  
10    C C   . ILE A 2   ? 1.089 1.462 1.174 -0.051 0.099  0.029  2   ILE BBB C   
11    O O   . ILE A 2   ? 1.146 1.518 1.234 -0.053 0.093  0.027  2   ILE BBB O   
12    C CB  . ILE A 2   ? 0.924 1.290 0.990 -0.050 0.104  0.014  2   ILE BBB CB  
13    C CG1 . ILE A 2   ? 0.921 1.280 0.980 -0.051 0.108  0.007  2   ILE BBB CG1 
14    C CG2 . ILE A 2   ? 1.087 1.459 1.149 -0.046 0.107  0.017  2   ILE BBB CG2 
15    C CD1 . ILE A 2   ? 0.981 1.335 1.036 -0.047 0.115  0.009  2   ILE BBB CD1 
16    N N   . VAL A 3   ? 1.084 1.463 1.174 -0.049 0.102  0.038  3   VAL BBB N   
17    C CA  . VAL A 3   ? 1.137 1.522 1.238 -0.051 0.099  0.047  3   VAL BBB CA  
18    C C   . VAL A 3   ? 1.198 1.589 1.294 -0.048 0.105  0.054  3   VAL BBB C   
19    O O   . VAL A 3   ? 1.244 1.637 1.331 -0.043 0.111  0.051  3   VAL BBB O   
20    C CB  . VAL A 3   ? 1.262 1.651 1.376 -0.054 0.097  0.053  3   VAL BBB CB  
21    C CG1 . VAL A 3   ? 1.422 1.821 1.539 -0.050 0.104  0.060  3   VAL BBB CG1 
22    C CG2 . VAL A 3   ? 1.339 1.727 1.465 -0.059 0.091  0.058  3   VAL BBB CG2 
23    N N   . GLN A 4   ? 1.229 1.623 1.333 -0.050 0.103  0.063  4   GLN BBB N   
24    C CA  A GLN A 4   ? 1.407 1.812 1.508 -0.046 0.109  0.072  4   GLN BBB CA  
25    C C   . GLN A 4   ? 1.402 1.817 1.516 -0.048 0.113  0.083  4   GLN BBB C   
26    O O   . GLN A 4   ? 1.316 1.731 1.445 -0.054 0.108  0.086  4   GLN BBB O   
27    C CB  . GLN A 4   ? 1.548 1.953 1.646 -0.045 0.108  0.078  4   GLN BBB CB  
28    C CG  . GLN A 4   ? 1.585 1.981 1.693 -0.051 0.101  0.082  4   GLN BBB CG  
29    C CD  . GLN A 4   ? 1.745 2.129 1.846 -0.050 0.094  0.071  4   GLN BBB CD  
30    O OE1 . GLN A 4   ? 1.828 2.214 1.917 -0.046 0.094  0.066  4   GLN BBB OE1 
31    N NE2 . GLN A 4   ? 1.811 2.187 1.921 -0.055 0.087  0.068  4   GLN BBB NE2 
32    N N   . ASN A 5   ? 1.514 1.941 1.623 -0.042 0.121  0.088  5   ASN BBB N   
33    C CA  . ASN A 5   ? 1.593 2.036 1.714 -0.042 0.126  0.099  5   ASN BBB CA  
34    C C   . ASN A 5   ? 1.792 2.242 1.920 -0.046 0.127  0.113  5   ASN BBB C   
35    O O   . ASN A 5   ? 1.884 2.324 2.009 -0.048 0.123  0.114  5   ASN BBB O   
36    C CB  . ASN A 5   ? 1.612 2.064 1.724 -0.033 0.134  0.096  5   ASN BBB CB  
37    C CG  . ASN A 5   ? 1.703 2.160 1.799 -0.025 0.139  0.097  5   ASN BBB CG  
38    O OD1 . ASN A 5   ? 1.833 2.287 1.924 -0.027 0.137  0.098  5   ASN BBB OD1 
39    N ND2 . ASN A 5   ? 1.745 2.211 1.833 -0.016 0.146  0.094  5   ASN BBB ND2 
40    N N   . LEU A 6   ? 1.813 2.281 1.950 -0.045 0.134  0.125  6   LEU BBB N   
41    C CA  . LEU A 6   ? 1.757 2.232 1.902 -0.050 0.136  0.141  6   LEU BBB CA  
42    C C   . LEU A 6   ? 1.842 2.320 1.969 -0.042 0.141  0.144  6   LEU BBB C   
43    O O   . LEU A 6   ? 1.959 2.435 2.088 -0.045 0.141  0.155  6   LEU BBB O   
44    C CB  . LEU A 6   ? 1.906 2.405 2.067 -0.052 0.143  0.154  6   LEU BBB CB  
45    C CG  . LEU A 6   ? 2.131 2.651 2.284 -0.041 0.153  0.157  6   LEU BBB CG  
46    C CD1 . LEU A 6   ? 2.274 2.806 2.419 -0.037 0.161  0.169  6   LEU BBB CD1 
47    C CD2 . LEU A 6   ? 2.306 2.846 2.478 -0.044 0.157  0.164  6   LEU BBB CD2 
48    N N   . GLN A 7   ? 2.053 2.534 2.163 -0.031 0.145  0.134  7   GLN BBB N   
49    C CA  . GLN A 7   ? 2.138 2.622 2.229 -0.023 0.148  0.133  7   GLN BBB CA  
50    C C   . GLN A 7   ? 2.129 2.596 2.212 -0.024 0.140  0.125  7   GLN BBB C   
51    O O   . GLN A 7   ? 2.232 2.702 2.300 -0.018 0.141  0.125  7   GLN BBB O   
52    C CB  . GLN A 7   ? 2.135 2.629 2.213 -0.012 0.154  0.123  7   GLN BBB CB  
53    C CG  . GLN A 7   ? 2.204 2.703 2.261 -0.002 0.156  0.119  7   GLN BBB CG  
54    C CD  . GLN A 7   ? 2.290 2.810 2.344 0.003  0.164  0.135  7   GLN BBB CD  
55    O OE1 . GLN A 7   ? 2.404 2.938 2.471 0.001  0.170  0.148  7   GLN BBB OE1 
56    N NE2 . GLN A 7   ? 2.243 2.768 2.281 0.010  0.165  0.135  7   GLN BBB NE2 
57    N N   . GLY A 8   ? 1.926 2.377 2.017 -0.031 0.132  0.117  8   GLY BBB N   
58    C CA  . GLY A 8   ? 1.841 2.278 1.923 -0.031 0.125  0.107  8   GLY BBB CA  
59    C C   . GLY A 8   ? 1.858 2.291 1.928 -0.027 0.124  0.090  8   GLY BBB C   
60    O O   . GLY A 8   ? 1.997 2.420 2.062 -0.029 0.118  0.080  8   GLY BBB O   
61    N N   . GLN A 9   ? 1.808 2.249 1.873 -0.022 0.130  0.086  9   GLN BBB N   
62    C CA  . GLN A 9   ? 1.794 2.229 1.847 -0.019 0.130  0.070  9   GLN BBB CA  
63    C C   . GLN A 9   ? 1.696 2.117 1.755 -0.025 0.125  0.062  9   GLN BBB C   
64    O O   . GLN A 9   ? 1.711 2.131 1.783 -0.029 0.124  0.067  9   GLN BBB O   
65    C CB  . GLN A 9   ? 1.832 2.276 1.878 -0.011 0.138  0.068  9   GLN BBB CB  
66    C CG  . GLN A 9   ? 2.002 2.438 2.035 -0.007 0.138  0.052  9   GLN BBB CG  
67    C CD  . GLN A 9   ? 2.114 2.556 2.142 0.001  0.146  0.051  9   GLN BBB CD  
68    O OE1 . GLN A 9   ? 2.058 2.514 2.092 0.005  0.151  0.063  9   GLN BBB OE1 
69    N NE2 . GLN A 9   ? 2.175 2.607 2.193 0.005  0.147  0.036  9   GLN BBB NE2 
70    N N   . MET A 10  ? 1.448 1.860 1.499 -0.026 0.122  0.048  10  MET BBB N   
71    C CA  . MET A 10  ? 1.210 1.611 1.266 -0.031 0.118  0.041  10  MET BBB CA  
72    C C   . MET A 10  ? 1.242 1.638 1.295 -0.029 0.122  0.035  10  MET BBB C   
73    O O   . MET A 10  ? 1.300 1.694 1.341 -0.025 0.126  0.027  10  MET BBB O   
74    C CB  . MET A 10  ? 1.231 1.626 1.280 -0.034 0.112  0.030  10  MET BBB CB  
75    C CG  . MET A 10  ? 1.404 1.802 1.455 -0.034 0.107  0.035  10  MET BBB CG  
76    S SD  . MET A 10  ? 1.459 1.850 1.526 -0.040 0.102  0.044  10  MET BBB SD  
77    C CE  . MET A 10  ? 1.401 1.784 1.470 -0.045 0.097  0.031  10  MET BBB CE  
78    N N   . VAL A 11  ? 1.258 1.652 1.320 -0.031 0.123  0.040  11  VAL BBB N   
79    C CA  . VAL A 11  ? 1.230 1.620 1.291 -0.028 0.127  0.037  11  VAL BBB CA  
80    C C   . VAL A 11  ? 1.131 1.512 1.197 -0.032 0.123  0.034  11  VAL BBB C   
81    O O   . VAL A 11  ? 1.066 1.447 1.141 -0.038 0.118  0.036  11  VAL BBB O   
82    C CB  . VAL A 11  ? 1.288 1.690 1.355 -0.022 0.132  0.047  11  VAL BBB CB  
83    C CG1 . VAL A 11  ? 1.457 1.871 1.518 -0.017 0.137  0.052  11  VAL BBB CG1 
84    C CG2 . VAL A 11  ? 1.280 1.689 1.364 -0.027 0.129  0.057  11  VAL BBB CG2 
85    N N   . HIS A 12  ? 1.102 1.472 1.162 -0.030 0.127  0.029  12  HIS BBB N   
86    C CA  . HIS A 12  ? 1.021 1.384 1.085 -0.033 0.125  0.027  12  HIS BBB CA  
87    C C   . HIS A 12  ? 1.036 1.407 1.110 -0.030 0.125  0.036  12  HIS BBB C   
88    O O   . HIS A 12  ? 1.155 1.535 1.231 -0.024 0.129  0.042  12  HIS BBB O   
89    C CB  . HIS A 12  ? 1.001 1.349 1.055 -0.031 0.129  0.020  12  HIS BBB CB  
90    C CG  . HIS A 12  ? 0.999 1.339 1.055 -0.033 0.128  0.020  12  HIS BBB CG  
91    N ND1 . HIS A 12  ? 1.048 1.385 1.105 -0.027 0.131  0.026  12  HIS BBB ND1 
92    C CD2 . HIS A 12  ? 1.085 1.419 1.140 -0.040 0.124  0.017  12  HIS BBB CD2 
93    C CE1 . HIS A 12  ? 1.194 1.525 1.251 -0.030 0.129  0.026  12  HIS BBB CE1 
94    N NE2 . HIS A 12  ? 1.194 1.523 1.250 -0.038 0.125  0.020  12  HIS BBB NE2 
95    N N   . GLN A 13  ? 0.981 1.352 1.062 -0.034 0.120  0.037  13  GLN BBB N   
96    C CA  . GLN A 13  ? 1.055 1.435 1.147 -0.032 0.118  0.044  13  GLN BBB CA  
97    C C   . GLN A 13  ? 1.057 1.430 1.146 -0.032 0.116  0.041  13  GLN BBB C   
98    O O   . GLN A 13  ? 1.035 1.400 1.120 -0.037 0.113  0.036  13  GLN BBB O   
99    C CB  . GLN A 13  ? 1.091 1.483 1.196 -0.038 0.112  0.049  13  GLN BBB CB  
100   C CG  . GLN A 13  ? 1.304 1.708 1.422 -0.037 0.110  0.055  13  GLN BBB CG  
101   C CD  . GLN A 13  ? 1.438 1.853 1.571 -0.044 0.105  0.061  13  GLN BBB CD  
102   O OE1 . GLN A 13  ? 1.374 1.783 1.506 -0.048 0.102  0.060  13  GLN BBB OE1 
103   N NE2 . GLN A 13  ? 1.711 2.141 1.857 -0.044 0.104  0.067  13  GLN BBB NE2 
104   N N   . CYS A 14  ? 1.085 1.461 1.176 -0.026 0.118  0.046  14  CYS BBB N   
105   C CA  . CYS A 14  ? 1.047 1.417 1.135 -0.025 0.117  0.045  14  CYS BBB CA  
106   C C   . CYS A 14  ? 1.079 1.456 1.174 -0.031 0.109  0.043  14  CYS BBB C   
107   O O   . CYS A 14  ? 1.125 1.514 1.232 -0.034 0.104  0.045  14  CYS BBB O   
108   C CB  . CYS A 14  ? 1.144 1.518 1.232 -0.016 0.121  0.050  14  CYS BBB CB  
109   S SG  . CYS A 14  ? 1.554 1.915 1.631 -0.006 0.131  0.050  14  CYS BBB SG  
110   N N   . ILE A 15  ? 1.093 1.462 1.181 -0.032 0.108  0.040  15  ILE BBB N   
111   C CA  . ILE A 15  ? 1.019 1.395 1.112 -0.035 0.101  0.037  15  ILE BBB CA  
112   C C   . ILE A 15  ? 1.035 1.425 1.137 -0.031 0.097  0.042  15  ILE BBB C   
113   O O   . ILE A 15  ? 1.037 1.428 1.136 -0.024 0.101  0.047  15  ILE BBB O   
114   C CB  . ILE A 15  ? 0.935 1.303 1.018 -0.036 0.102  0.034  15  ILE BBB CB  
115   C CG1 . ILE A 15  ? 0.921 1.297 1.008 -0.039 0.094  0.030  15  ILE BBB CG1 
116   C CG2 . ILE A 15  ? 0.949 1.309 1.024 -0.030 0.108  0.039  15  ILE BBB CG2 
117   C CD1 . ILE A 15  ? 1.028 1.399 1.106 -0.041 0.095  0.026  15  ILE BBB CD1 
118   N N   . SER A 16  ? 1.001 1.402 1.113 -0.035 0.089  0.040  16  SER BBB N   
119   C CA  . SER A 16  ? 1.035 1.452 1.159 -0.032 0.084  0.044  16  SER BBB CA  
120   C C   . SER A 16  ? 1.000 1.422 1.119 -0.027 0.081  0.042  16  SER BBB C   
121   O O   . SER A 16  ? 0.988 1.404 1.099 -0.028 0.079  0.038  16  SER BBB O   
122   C CB  . SER A 16  ? 1.049 1.475 1.187 -0.040 0.076  0.042  16  SER BBB CB  
123   O OG  . SER A 16  ? 1.228 1.670 1.379 -0.039 0.071  0.044  16  SER BBB OG  
124   N N   . PRO A 17  ? 1.025 1.461 1.149 -0.021 0.080  0.047  17  PRO BBB N   
125   C CA  . PRO A 17  ? 1.023 1.467 1.143 -0.015 0.076  0.046  17  PRO BBB CA  
126   C C   . PRO A 17  ? 1.110 1.563 1.236 -0.020 0.065  0.038  17  PRO BBB C   
127   O O   . PRO A 17  ? 1.224 1.677 1.340 -0.017 0.063  0.035  17  PRO BBB O   
128   C CB  . PRO A 17  ? 1.035 1.497 1.163 -0.008 0.075  0.052  17  PRO BBB CB  
129   C CG  . PRO A 17  ? 1.042 1.498 1.171 -0.007 0.084  0.058  17  PRO BBB CG  
130   C CD  . PRO A 17  ? 1.110 1.554 1.241 -0.017 0.084  0.054  17  PRO BBB CD  
131   N N   . ARG A 18  ? 1.099 1.556 1.239 -0.028 0.059  0.034  18  ARG BBB N   
132   C CA  . ARG A 18  ? 1.054 1.514 1.199 -0.033 0.049  0.025  18  ARG BBB CA  
133   C C   . ARG A 18  ? 1.047 1.494 1.180 -0.034 0.049  0.019  18  ARG BBB C   
134   O O   . ARG A 18  ? 1.173 1.624 1.301 -0.032 0.044  0.013  18  ARG BBB O   
135   C CB  . ARG A 18  ? 1.106 1.569 1.268 -0.042 0.043  0.024  18  ARG BBB CB  
136   C CG  . ARG A 18  ? 1.242 1.715 1.415 -0.046 0.030  0.015  18  ARG BBB CG  
137   C CD  . ARG A 18  ? 1.434 1.910 1.627 -0.055 0.026  0.017  18  ARG BBB CD  
138   N NE  . ARG A 18  ? 1.620 2.107 1.821 -0.055 0.033  0.027  18  ARG BBB NE  
139   C CZ  . ARG A 18  ? 1.684 2.175 1.900 -0.062 0.034  0.032  18  ARG BBB CZ  
140   N NH1 . ARG A 18  ? 1.674 2.156 1.900 -0.072 0.029  0.030  18  ARG BBB NH1 
141   N NH2 . ARG A 18  ? 1.665 2.169 1.887 -0.060 0.041  0.042  18  ARG BBB NH2 
142   N N   . THR A 19  ? 1.075 1.507 1.203 -0.038 0.056  0.021  19  THR BBB N   
143   C CA  . THR A 19  ? 1.070 1.492 1.187 -0.039 0.056  0.015  19  THR BBB CA  
144   C C   . THR A 19  ? 1.066 1.489 1.170 -0.033 0.061  0.016  19  THR BBB C   
145   O O   . THR A 19  ? 1.160 1.586 1.258 -0.032 0.057  0.010  19  THR BBB O   
146   C CB  . THR A 19  ? 1.079 1.488 1.195 -0.044 0.062  0.017  19  THR BBB CB  
147   O OG1 . THR A 19  ? 1.128 1.531 1.234 -0.044 0.064  0.012  19  THR BBB OG1 
148   C CG2 . THR A 19  ? 1.189 1.594 1.302 -0.042 0.071  0.025  19  THR BBB CG2 
149   N N   . LEU A 20  ? 0.984 1.404 1.082 -0.029 0.069  0.024  20  LEU BBB N   
150   C CA  . LEU A 20  ? 0.986 1.404 1.071 -0.024 0.075  0.028  20  LEU BBB CA  
151   C C   . LEU A 20  ? 1.050 1.484 1.134 -0.018 0.068  0.025  20  LEU BBB C   
152   O O   . LEU A 20  ? 1.026 1.462 1.101 -0.016 0.068  0.023  20  LEU BBB O   
153   C CB  . LEU A 20  ? 0.974 1.385 1.054 -0.019 0.084  0.037  20  LEU BBB CB  
154   C CG  . LEU A 20  ? 1.063 1.457 1.140 -0.023 0.092  0.039  20  LEU BBB CG  
155   C CD1 . LEU A 20  ? 1.072 1.461 1.147 -0.016 0.098  0.047  20  LEU BBB CD1 
156   C CD2 . LEU A 20  ? 1.065 1.447 1.131 -0.027 0.097  0.037  20  LEU BBB CD2 
157   N N   . ASN A 21  ? 1.104 1.550 1.196 -0.015 0.062  0.026  21  ASN BBB N   
158   C CA  . ASN A 21  ? 1.114 1.578 1.205 -0.008 0.054  0.022  21  ASN BBB CA  
159   C C   . ASN A 21  ? 1.090 1.558 1.183 -0.012 0.046  0.011  21  ASN BBB C   
160   O O   . ASN A 21  ? 1.174 1.651 1.258 -0.007 0.043  0.007  21  ASN BBB O   
161   C CB  . ASN A 21  ? 1.154 1.634 1.257 -0.006 0.049  0.024  21  ASN BBB CB  
162   C CG  . ASN A 21  ? 1.286 1.785 1.386 0.002  0.041  0.020  21  ASN BBB CG  
163   O OD1 . ASN A 21  ? 1.488 1.990 1.575 0.009  0.043  0.022  21  ASN BBB OD1 
164   N ND2 . ASN A 21  ? 1.422 1.938 1.537 0.001  0.031  0.015  21  ASN BBB ND2 
165   N N   . ALA A 22  ? 1.021 1.482 1.124 -0.020 0.041  0.005  22  ALA BBB N   
166   C CA  . ALA A 22  ? 0.983 1.444 1.088 -0.023 0.033  -0.007 22  ALA BBB CA  
167   C C   . ALA A 22  ? 0.986 1.443 1.077 -0.020 0.038  -0.009 22  ALA BBB C   
168   O O   . ALA A 22  ? 1.041 1.508 1.127 -0.016 0.032  -0.017 22  ALA BBB O   
169   C CB  . ALA A 22  ? 0.955 1.405 1.072 -0.031 0.030  -0.010 22  ALA BBB CB  
170   N N   . TRP A 23  ? 0.953 1.399 1.038 -0.023 0.048  -0.002 23  TRP BBB N   
171   C CA  . TRP A 23  ? 0.969 1.413 1.043 -0.023 0.053  -0.003 23  TRP BBB CA  
172   C C   . TRP A 23  ? 1.000 1.455 1.062 -0.016 0.056  0.001  23  TRP BBB C   
173   O O   . TRP A 23  ? 1.027 1.492 1.084 -0.012 0.054  -0.005 23  TRP BBB O   
174   C CB  . TRP A 23  ? 0.913 1.342 0.985 -0.029 0.063  0.003  23  TRP BBB CB  
175   C CG  . TRP A 23  ? 0.903 1.332 0.966 -0.030 0.070  0.003  23  TRP BBB CG  
176   C CD1 . TRP A 23  ? 0.916 1.338 0.970 -0.031 0.080  0.011  23  TRP BBB CD1 
177   C CD2 . TRP A 23  ? 0.894 1.329 0.955 -0.031 0.066  -0.006 23  TRP BBB CD2 
178   N NE1 . TRP A 23  ? 0.917 1.344 0.967 -0.034 0.083  0.008  23  TRP BBB NE1 
179   C CE2 . TRP A 23  ? 0.902 1.338 0.955 -0.033 0.075  -0.002 23  TRP BBB CE2 
180   C CE3 . TRP A 23  ? 0.886 1.326 0.951 -0.029 0.057  -0.016 23  TRP BBB CE3 
181   C CZ2 . TRP A 23  ? 0.901 1.345 0.950 -0.033 0.075  -0.008 23  TRP BBB CZ2 
182   C CZ3 . TRP A 23  ? 0.887 1.334 0.948 -0.028 0.056  -0.023 23  TRP BBB CZ3 
183   C CH2 . TRP A 23  ? 0.894 1.345 0.947 -0.030 0.066  -0.019 23  TRP BBB CH2 
184   N N   . VAL A 24  ? 1.027 1.482 1.086 -0.012 0.061  0.011  24  VAL BBB N   
185   C CA  . VAL A 24  ? 0.999 1.465 1.048 -0.004 0.064  0.016  24  VAL BBB CA  
186   C C   . VAL A 24  ? 1.069 1.555 1.117 0.003  0.053  0.007  24  VAL BBB C   
187   O O   . VAL A 24  ? 1.175 1.672 1.212 0.008  0.054  0.007  24  VAL BBB O   
188   C CB  . VAL A 24  ? 1.006 1.468 1.052 0.001  0.070  0.028  24  VAL BBB CB  
189   C CG1 . VAL A 24  ? 1.127 1.604 1.163 0.012  0.070  0.034  24  VAL BBB CG1 
190   C CG2 . VAL A 24  ? 1.011 1.453 1.053 -0.003 0.082  0.037  24  VAL BBB CG2 
191   N N   . LYS A 25  ? 1.074 1.564 1.134 0.002  0.043  -0.000 25  LYS BBB N   
192   C CA  . LYS A 25  ? 1.186 1.694 1.247 0.008  0.031  -0.010 25  LYS BBB CA  
193   C C   . LYS A 25  ? 1.204 1.713 1.262 0.007  0.026  -0.023 25  LYS BBB C   
194   O O   . LYS A 25  ? 1.358 1.884 1.408 0.015  0.022  -0.029 25  LYS BBB O   
195   C CB  . LYS A 25  ? 1.182 1.693 1.258 0.005  0.022  -0.015 25  LYS BBB CB  
196   C CG  . LYS A 25  ? 1.211 1.741 1.288 0.013  0.018  -0.012 25  LYS BBB CG  
197   C CD  . LYS A 25  ? 1.417 1.966 1.485 0.021  0.009  -0.022 25  LYS BBB CD  
198   C CE  . LYS A 25  ? 1.492 2.063 1.562 0.030  0.002  -0.021 25  LYS BBB CE  
199   N NZ  . LYS A 25  ? 1.506 2.098 1.569 0.038  -0.008 -0.033 25  LYS BBB NZ  
200   N N   . VAL A 26  ? 1.051 1.546 1.115 -0.001 0.026  -0.027 26  VAL BBB N   
201   C CA  . VAL A 26  ? 1.070 1.566 1.132 -0.000 0.021  -0.038 26  VAL BBB CA  
202   C C   . VAL A 26  ? 1.131 1.637 1.179 0.005  0.029  -0.036 26  VAL BBB C   
203   O O   . VAL A 26  ? 1.215 1.733 1.257 0.011  0.024  -0.045 26  VAL BBB O   
204   C CB  . VAL A 26  ? 0.973 1.452 1.045 -0.009 0.021  -0.041 26  VAL BBB CB  
205   C CG1 . VAL A 26  ? 0.991 1.459 1.059 -0.014 0.033  -0.032 26  VAL BBB CG1 
206   C CG2 . VAL A 26  ? 0.981 1.460 1.052 -0.006 0.013  -0.055 26  VAL BBB CG2 
207   N N   . VAL A 27  ? 1.074 1.574 1.116 0.002  0.041  -0.023 27  VAL BBB N   
208   C CA  . VAL A 27  ? 1.083 1.592 1.113 0.005  0.050  -0.018 27  VAL BBB CA  
209   C C   . VAL A 27  ? 1.211 1.740 1.231 0.016  0.048  -0.016 27  VAL BBB C   
210   O O   . VAL A 27  ? 1.318 1.863 1.328 0.022  0.048  -0.019 27  VAL BBB O   
211   C CB  . VAL A 27  ? 1.004 1.499 1.032 -0.001 0.063  -0.004 27  VAL BBB CB  
212   C CG1 . VAL A 27  ? 1.103 1.608 1.119 0.001  0.073  0.003  27  VAL BBB CG1 
213   C CG2 . VAL A 27  ? 0.987 1.467 1.023 -0.011 0.065  -0.007 27  VAL BBB CG2 
214   N N   . GLU A 28  ? 1.255 1.786 1.276 0.020  0.046  -0.011 28  GLU BBB N   
215   C CA  . GLU A 28  ? 1.316 1.868 1.327 0.032  0.043  -0.009 28  GLU BBB CA  
216   C C   . GLU A 28  ? 1.264 1.833 1.274 0.038  0.030  -0.026 28  GLU BBB C   
217   O O   . GLU A 28  ? 1.316 1.904 1.313 0.048  0.029  -0.028 28  GLU BBB O   
218   C CB  . GLU A 28  ? 1.409 1.961 1.424 0.035  0.041  -0.002 28  GLU BBB CB  
219   C CG  . GLU A 28  ? 1.625 2.164 1.634 0.034  0.054  0.016  28  GLU BBB CG  
220   C CD  . GLU A 28  ? 1.709 2.250 1.722 0.039  0.052  0.023  28  GLU BBB CD  
221   O OE1 . GLU A 28  ? 1.561 2.113 1.583 0.041  0.041  0.013  28  GLU BBB OE1 
222   O OE2 . GLU A 28  ? 1.834 2.364 1.841 0.041  0.062  0.037  28  GLU BBB OE2 
223   N N   . GLU A 29  ? 1.295 1.856 1.318 0.033  0.019  -0.039 29  GLU BBB N   
224   C CA  . GLU A 29  ? 1.369 1.943 1.393 0.039  0.006  -0.057 29  GLU BBB CA  
225   C C   . GLU A 29  ? 1.378 1.952 1.396 0.041  0.005  -0.067 29  GLU BBB C   
226   O O   . GLU A 29  ? 1.502 2.094 1.512 0.051  -0.002 -0.078 29  GLU BBB O   
227   C CB  . GLU A 29  ? 1.459 2.023 1.499 0.033  -0.006 -0.066 29  GLU BBB CB  
228   C CG  . GLU A 29  ? 1.615 2.184 1.662 0.033  -0.009 -0.061 29  GLU BBB CG  
229   C CD  . GLU A 29  ? 1.876 2.431 1.942 0.023  -0.017 -0.066 29  GLU BBB CD  
230   O OE1 . GLU A 29  ? 1.851 2.394 1.925 0.018  -0.023 -0.077 29  GLU BBB OE1 
231   O OE2 . GLU A 29  ? 1.874 2.431 1.949 0.020  -0.016 -0.058 29  GLU BBB OE2 
232   N N   . LYS A 30  ? 1.232 1.791 1.256 0.032  0.011  -0.064 30  LYS BBB N   
233   C CA  . LYS A 30  ? 1.189 1.748 1.210 0.034  0.010  -0.074 30  LYS BBB CA  
234   C C   . LYS A 30  ? 1.206 1.772 1.218 0.034  0.023  -0.064 30  LYS BBB C   
235   O O   . LYS A 30  ? 1.154 1.727 1.163 0.036  0.023  -0.072 30  LYS BBB O   
236   C CB  . LYS A 30  ? 1.172 1.709 1.207 0.025  0.006  -0.079 30  LYS BBB CB  
237   C CG  . LYS A 30  ? 1.242 1.770 1.289 0.023  -0.008 -0.088 30  LYS BBB CG  
238   C CD  . LYS A 30  ? 1.361 1.901 1.404 0.033  -0.021 -0.106 30  LYS BBB CD  
239   C CE  . LYS A 30  ? 1.572 2.097 1.630 0.028  -0.034 -0.117 30  LYS BBB CE  
240   N NZ  . LYS A 30  ? 1.612 2.116 1.677 0.023  -0.036 -0.122 30  LYS BBB NZ  
241   N N   . ALA A 31  ? 1.241 1.805 1.249 0.030  0.035  -0.048 31  ALA BBB N   
242   C CA  . ALA A 31  ? 1.230 1.799 1.232 0.027  0.048  -0.037 31  ALA BBB CA  
243   C C   . ALA A 31  ? 1.244 1.802 1.253 0.018  0.051  -0.041 31  ALA BBB C   
244   O O   . ALA A 31  ? 1.288 1.826 1.307 0.010  0.049  -0.041 31  ALA BBB O   
245   C CB  . ALA A 31  ? 1.222 1.818 1.210 0.037  0.051  -0.037 31  ALA BBB CB  
246   N N   . PHE A 32  ? 1.168 1.741 1.172 0.021  0.054  -0.045 32  PHE BBB N   
247   C CA  . PHE A 32  ? 1.105 1.673 1.116 0.015  0.056  -0.049 32  PHE BBB CA  
248   C C   . PHE A 32  ? 1.094 1.672 1.105 0.024  0.045  -0.066 32  PHE BBB C   
249   O O   . PHE A 32  ? 1.177 1.766 1.187 0.025  0.048  -0.071 32  PHE BBB O   
250   C CB  . PHE A 32  ? 1.139 1.716 1.147 0.008  0.069  -0.039 32  PHE BBB CB  
251   C CG  . PHE A 32  ? 1.165 1.725 1.175 -0.001 0.079  -0.024 32  PHE BBB CG  
252   C CD1 . PHE A 32  ? 1.108 1.647 1.127 -0.011 0.080  -0.022 32  PHE BBB CD1 
253   C CD2 . PHE A 32  ? 1.239 1.805 1.240 0.001  0.086  -0.011 32  PHE BBB CD2 
254   C CE1 . PHE A 32  ? 1.128 1.650 1.147 -0.019 0.089  -0.010 32  PHE BBB CE1 
255   C CE2 . PHE A 32  ? 1.237 1.785 1.238 -0.007 0.095  0.003  32  PHE BBB CE2 
256   C CZ  . PHE A 32  ? 1.201 1.727 1.212 -0.017 0.096  0.003  32  PHE BBB CZ  
257   N N   . SER A 33  ? 1.046 1.619 1.058 0.030  0.033  -0.077 33  SER BBB N   
258   C CA  . SER A 33  ? 1.088 1.661 1.102 0.037  0.022  -0.093 33  SER BBB CA  
259   C C   . SER A 33  ? 1.126 1.679 1.150 0.030  0.021  -0.095 33  SER BBB C   
260   O O   . SER A 33  ? 1.249 1.784 1.280 0.019  0.025  -0.085 33  SER BBB O   
261   C CB  . SER A 33  ? 1.125 1.693 1.140 0.043  0.008  -0.104 33  SER BBB CB  
262   O OG  . SER A 33  ? 1.358 1.945 1.363 0.051  0.008  -0.103 33  SER BBB OG  
263   N N   . PRO A 34  ? 1.140 1.697 1.165 0.036  0.016  -0.106 34  PRO BBB N   
264   C CA  . PRO A 34  ? 1.157 1.698 1.189 0.030  0.017  -0.106 34  PRO BBB CA  
265   C C   . PRO A 34  ? 1.251 1.765 1.293 0.023  0.011  -0.104 34  PRO BBB C   
266   O O   . PRO A 34  ? 1.255 1.756 1.303 0.014  0.015  -0.097 34  PRO BBB O   
267   C CB  . PRO A 34  ? 1.231 1.780 1.260 0.042  0.009  -0.121 34  PRO BBB CB  
268   C CG  . PRO A 34  ? 1.266 1.825 1.288 0.053  0.001  -0.131 34  PRO BBB CG  
269   C CD  . PRO A 34  ? 1.272 1.846 1.288 0.050  0.009  -0.120 34  PRO BBB CD  
270   N N   . GLU A 35  ? 1.355 1.861 1.399 0.026  0.001  -0.110 35  GLU BBB N   
271   C CA  . GLU A 35  ? 1.323 1.805 1.377 0.018  -0.004 -0.108 35  GLU BBB CA  
272   C C   . GLU A 35  ? 1.251 1.727 1.310 0.007  0.005  -0.093 35  GLU BBB C   
273   O O   . GLU A 35  ? 1.282 1.740 1.350 0.000  0.002  -0.089 35  GLU BBB O   
274   C CB  . GLU A 35  ? 1.377 1.858 1.433 0.023  -0.016 -0.118 35  GLU BBB CB  
275   C CG  . GLU A 35  ? 1.506 2.002 1.557 0.023  -0.012 -0.112 35  GLU BBB CG  
276   C CD  . GLU A 35  ? 1.602 2.111 1.648 0.033  -0.022 -0.124 35  GLU BBB CD  
277   O OE1 . GLU A 35  ? 1.808 2.310 1.862 0.031  -0.032 -0.130 35  GLU BBB OE1 
278   O OE2 . GLU A 35  ? 1.569 2.098 1.603 0.043  -0.021 -0.130 35  GLU BBB OE2 
279   N N   . VAL A 36  ? 1.143 1.632 1.195 0.006  0.015  -0.083 36  VAL BBB N   
280   C CA  . VAL A 36  ? 1.054 1.535 1.110 -0.003 0.023  -0.070 36  VAL BBB CA  
281   C C   . VAL A 36  ? 1.037 1.506 1.097 -0.011 0.029  -0.064 36  VAL BBB C   
282   O O   . VAL A 36  ? 1.133 1.589 1.199 -0.018 0.032  -0.056 36  VAL BBB O   
283   C CB  A VAL A 36  ? 0.946 1.442 0.993 -0.002 0.032  -0.061 36  VAL BBB CB  
284   C CG1 A VAL A 36  ? 0.935 1.420 0.983 -0.011 0.043  -0.047 36  VAL BBB CG1 
285   C CG2 A VAL A 36  ? 1.012 1.517 1.055 0.005  0.026  -0.063 36  VAL BBB CG2 
286   N N   . ILE A 37  ? 0.980 1.455 1.037 -0.009 0.031  -0.069 37  ILE BBB N   
287   C CA  . ILE A 37  ? 0.934 1.401 0.995 -0.015 0.036  -0.065 37  ILE BBB CA  
288   C C   . ILE A 37  ? 0.942 1.390 1.011 -0.018 0.030  -0.066 37  ILE BBB C   
289   O O   . ILE A 37  ? 0.971 1.409 1.044 -0.025 0.035  -0.058 37  ILE BBB O   
290   C CB  . ILE A 37  ? 0.949 1.432 1.007 -0.012 0.037  -0.071 37  ILE BBB CB  
291   C CG1 . ILE A 37  ? 0.922 1.426 0.973 -0.010 0.045  -0.069 37  ILE BBB CG1 
292   C CG2 . ILE A 37  ? 1.021 1.499 1.082 -0.018 0.042  -0.068 37  ILE BBB CG2 
293   C CD1 . ILE A 37  ? 0.953 1.475 1.001 -0.008 0.048  -0.073 37  ILE BBB CD1 
294   N N   . PRO A 38  ? 0.910 1.351 0.982 -0.013 0.019  -0.074 38  PRO BBB N   
295   C CA  A PRO A 38  ? 0.910 1.331 0.991 -0.017 0.014  -0.072 38  PRO BBB CA  
296   C C   . PRO A 38  ? 0.930 1.345 1.015 -0.024 0.018  -0.062 38  PRO BBB C   
297   O O   . PRO A 38  ? 1.004 1.410 1.094 -0.030 0.022  -0.054 38  PRO BBB O   
298   C CB  A PRO A 38  ? 0.924 1.340 1.007 -0.010 0.002  -0.083 38  PRO BBB CB  
299   C CG  A PRO A 38  ? 0.967 1.399 1.042 -0.001 0.001  -0.093 38  PRO BBB CG  
300   C CD  A PRO A 38  ? 0.998 1.447 1.067 -0.003 0.012  -0.086 38  PRO BBB CD  
301   N N   . MET A 39  ? 0.931 1.354 1.015 -0.023 0.017  -0.062 39  MET BBB N   
302   C CA  . MET A 39  ? 0.892 1.312 0.982 -0.028 0.019  -0.053 39  MET BBB CA  
303   C C   . MET A 39  ? 0.897 1.314 0.985 -0.033 0.031  -0.042 39  MET BBB C   
304   O O   . MET A 39  ? 0.942 1.351 1.036 -0.038 0.033  -0.035 39  MET BBB O   
305   C CB  . MET A 39  ? 0.912 1.345 0.999 -0.023 0.016  -0.056 39  MET BBB CB  
306   C CG  . MET A 39  ? 0.917 1.348 1.011 -0.027 0.016  -0.049 39  MET BBB CG  
307   S SD  . MET A 39  ? 1.045 1.463 1.155 -0.032 0.006  -0.052 39  MET BBB SD  
308   C CE  . MET A 39  ? 0.968 1.393 1.078 -0.026 -0.008 -0.068 39  MET BBB CE  
309   N N   . PHE A 40  ? 0.926 1.352 1.005 -0.032 0.038  -0.041 40  PHE BBB N   
310   C CA  . PHE A 40  ? 0.859 1.281 0.936 -0.038 0.049  -0.032 40  PHE BBB CA  
311   C C   . PHE A 40  ? 0.924 1.335 1.005 -0.042 0.050  -0.031 40  PHE BBB C   
312   O O   . PHE A 40  ? 1.002 1.405 1.085 -0.046 0.055  -0.024 40  PHE BBB O   
313   C CB  . PHE A 40  ? 0.851 1.283 0.919 -0.038 0.056  -0.033 40  PHE BBB CB  
314   C CG  . PHE A 40  ? 0.850 1.277 0.916 -0.044 0.066  -0.026 40  PHE BBB CG  
315   C CD1 . PHE A 40  ? 0.853 1.274 0.917 -0.046 0.072  -0.017 40  PHE BBB CD1 
316   C CD2 . PHE A 40  ? 0.885 1.313 0.951 -0.048 0.068  -0.029 40  PHE BBB CD2 
317   C CE1 . PHE A 40  ? 0.862 1.276 0.924 -0.052 0.081  -0.012 40  PHE BBB CE1 
318   C CE2 . PHE A 40  ? 0.851 1.274 0.916 -0.055 0.077  -0.024 40  PHE BBB CE2 
319   C CZ  . PHE A 40  ? 0.861 1.275 0.924 -0.057 0.083  -0.016 40  PHE BBB CZ  
320   N N   . SER A 41  ? 1.010 1.421 1.092 -0.040 0.045  -0.038 41  SER BBB N   
321   C CA  . SER A 41  ? 1.031 1.434 1.116 -0.043 0.045  -0.036 41  SER BBB CA  
322   C C   . SER A 41  ? 1.028 1.419 1.120 -0.045 0.043  -0.031 41  SER BBB C   
323   O O   . SER A 41  ? 1.055 1.440 1.148 -0.049 0.047  -0.025 41  SER BBB O   
324   C CB  . SER A 41  ? 1.076 1.481 1.159 -0.038 0.040  -0.045 41  SER BBB CB  
325   O OG  . SER A 41  ? 1.378 1.777 1.462 -0.039 0.040  -0.042 41  SER BBB OG  
326   N N   . ALA A 42  ? 0.994 1.383 1.092 -0.044 0.035  -0.033 42  ALA BBB N   
327   C CA  . ALA A 42  ? 0.953 1.332 1.060 -0.047 0.033  -0.027 42  ALA BBB CA  
328   C C   . ALA A 42  ? 0.913 1.295 1.022 -0.051 0.040  -0.019 42  ALA BBB C   
329   O O   . ALA A 42  ? 0.909 1.286 1.022 -0.054 0.043  -0.011 42  ALA BBB O   
330   C CB  . ALA A 42  ? 0.887 1.264 1.002 -0.046 0.022  -0.034 42  ALA BBB CB  
331   N N   . LEU A 43  ? 0.881 1.272 0.986 -0.048 0.042  -0.019 43  LEU BBB N   
332   C CA  . LEU A 43  ? 0.869 1.262 0.974 -0.050 0.048  -0.011 43  LEU BBB CA  
333   C C   . LEU A 43  ? 0.921 1.309 1.020 -0.052 0.058  -0.006 43  LEU BBB C   
334   O O   . LEU A 43  ? 0.949 1.335 1.049 -0.052 0.063  0.001  43  LEU BBB O   
335   C CB  . LEU A 43  ? 0.890 1.292 0.989 -0.045 0.048  -0.012 43  LEU BBB CB  
336   C CG  . LEU A 43  ? 0.871 1.281 0.977 -0.043 0.039  -0.018 43  LEU BBB CG  
337   C CD1 . LEU A 43  ? 0.873 1.295 0.971 -0.037 0.039  -0.019 43  LEU BBB CD1 
338   C CD2 . LEU A 43  ? 0.924 1.333 1.042 -0.046 0.036  -0.013 43  LEU BBB CD2 
339   N N   . SER A 44  ? 0.940 1.326 1.032 -0.052 0.060  -0.010 44  SER BBB N   
340   C CA  . SER A 44  ? 0.982 1.364 1.069 -0.055 0.069  -0.007 44  SER BBB CA  
341   C C   . SER A 44  ? 0.994 1.371 1.084 -0.057 0.068  -0.006 44  SER BBB C   
342   O O   . SER A 44  ? 1.031 1.407 1.116 -0.058 0.073  -0.007 44  SER BBB O   
343   C CB  . SER A 44  ? 0.966 1.352 1.046 -0.056 0.072  -0.011 44  SER BBB CB  
344   O OG  . SER A 44  ? 1.042 1.434 1.123 -0.055 0.067  -0.018 44  SER BBB OG  
345   N N   . CYS A 45  ? 0.984 1.359 1.082 -0.056 0.062  -0.004 45  CYS BBB N   
346   C CA  . CYS A 45  ? 0.946 1.316 1.045 -0.057 0.062  -0.002 45  CYS BBB CA  
347   C C   . CYS A 45  ? 0.984 1.352 1.080 -0.058 0.070  0.004  45  CYS BBB C   
348   O O   . CYS A 45  ? 1.124 1.493 1.223 -0.058 0.073  0.010  45  CYS BBB O   
349   C CB  . CYS A 45  ? 1.053 1.419 1.162 -0.058 0.056  0.001  45  CYS BBB CB  
350   S SG  . CYS A 45  ? 1.472 1.832 1.584 -0.058 0.055  0.007  45  CYS BBB SG  
351   N N   . GLY A 46  ? 1.032 1.400 1.122 -0.058 0.073  0.003  46  GLY BBB N   
352   C CA  . GLY A 46  ? 1.033 1.400 1.119 -0.058 0.080  0.007  46  GLY BBB CA  
353   C C   . GLY A 46  ? 0.946 1.311 1.027 -0.059 0.087  0.005  46  GLY BBB C   
354   O O   . GLY A 46  ? 1.008 1.370 1.085 -0.058 0.093  0.007  46  GLY BBB O   
355   N N   . ALA A 47  ? 0.904 1.270 0.984 -0.060 0.086  0.001  47  ALA BBB N   
356   C CA  . ALA A 47  ? 1.019 1.381 1.094 -0.061 0.092  0.002  47  ALA BBB CA  
357   C C   . ALA A 47  ? 0.922 1.279 0.989 -0.064 0.098  -0.003 47  ALA BBB C   
358   O O   . ALA A 47  ? 0.867 1.228 0.932 -0.066 0.096  -0.009 47  ALA BBB O   
359   C CB  . ALA A 47  ? 1.076 1.441 1.150 -0.061 0.090  -0.000 47  ALA BBB CB  
360   N N   . THR A 48  ? 0.950 1.298 1.013 -0.063 0.104  -0.001 48  THR BBB N   
361   C CA  . THR A 48  ? 0.930 1.272 0.986 -0.067 0.109  -0.006 48  THR BBB CA  
362   C C   . THR A 48  ? 0.946 1.287 1.001 -0.072 0.110  -0.008 48  THR BBB C   
363   O O   . THR A 48  ? 1.023 1.367 1.081 -0.070 0.109  -0.004 48  THR BBB O   
364   C CB  . THR A 48  ? 0.974 1.305 1.026 -0.064 0.115  -0.004 48  THR BBB CB  
365   O OG1 . THR A 48  ? 1.002 1.327 1.055 -0.061 0.118  0.003  48  THR BBB OG1 
366   C CG2 . THR A 48  ? 1.018 1.354 1.072 -0.058 0.115  -0.001 48  THR BBB CG2 
367   N N   . PRO A 49  ? 0.932 1.270 0.984 -0.078 0.114  -0.015 49  PRO BBB N   
368   C CA  . PRO A 49  ? 0.947 1.283 0.999 -0.083 0.117  -0.015 49  PRO BBB CA  
369   C C   . PRO A 49  ? 1.066 1.390 1.115 -0.081 0.122  -0.006 49  PRO BBB C   
370   O O   . PRO A 49  ? 1.185 1.513 1.234 -0.081 0.123  -0.002 49  PRO BBB O   
371   C CB  . PRO A 49  ? 0.955 1.287 1.005 -0.091 0.120  -0.023 49  PRO BBB CB  
372   C CG  . PRO A 49  ? 0.947 1.289 0.998 -0.090 0.115  -0.029 49  PRO BBB CG  
373   C CD  . PRO A 49  ? 0.956 1.297 1.006 -0.081 0.113  -0.023 49  PRO BBB CD  
374   N N   . GLN A 50  ? 0.990 1.301 1.036 -0.076 0.125  -0.004 50  GLN BBB N   
375   C CA  . GLN A 50  ? 1.092 1.392 1.134 -0.071 0.130  0.005  50  GLN BBB CA  
376   C C   . GLN A 50  ? 1.133 1.446 1.179 -0.065 0.125  0.011  50  GLN BBB C   
377   O O   . GLN A 50  ? 1.142 1.454 1.187 -0.064 0.127  0.017  50  GLN BBB O   
378   C CB  . GLN A 50  ? 1.049 1.337 1.088 -0.065 0.133  0.006  50  GLN BBB CB  
379   C CG  . GLN A 50  ? 1.245 1.520 1.280 -0.059 0.138  0.014  50  GLN BBB CG  
380   C CD  . GLN A 50  ? 1.368 1.636 1.400 -0.050 0.140  0.015  50  GLN BBB CD  
381   O OE1 . GLN A 50  ? 1.347 1.627 1.383 -0.045 0.137  0.016  50  GLN BBB OE1 
382   N NE2 . GLN A 50  ? 1.535 1.781 1.560 -0.049 0.146  0.015  50  GLN BBB NE2 
383   N N   . ASP A 51  ? 1.203 1.528 1.255 -0.062 0.119  0.010  51  ASP BBB N   
384   C CA  . ASP A 51  ? 1.156 1.492 1.213 -0.058 0.114  0.014  51  ASP BBB CA  
385   C C   . ASP A 51  ? 1.092 1.437 1.149 -0.060 0.111  0.012  51  ASP BBB C   
386   O O   . ASP A 51  ? 1.108 1.459 1.165 -0.056 0.109  0.016  51  ASP BBB O   
387   C CB  . ASP A 51  ? 1.198 1.542 1.261 -0.056 0.108  0.013  51  ASP BBB CB  
388   C CG  . ASP A 51  ? 1.330 1.670 1.394 -0.052 0.111  0.017  51  ASP BBB CG  
389   O OD1 . ASP A 51  ? 1.423 1.756 1.484 -0.047 0.116  0.022  51  ASP BBB OD1 
390   O OD2 . ASP A 51  ? 1.262 1.605 1.329 -0.052 0.109  0.015  51  ASP BBB OD2 
391   N N   . LEU A 52  ? 1.002 1.352 1.059 -0.066 0.109  0.005  52  LEU BBB N   
392   C CA  . LEU A 52  ? 0.975 1.336 1.032 -0.068 0.107  0.003  52  LEU BBB CA  
393   C C   . LEU A 52  ? 1.008 1.365 1.060 -0.069 0.114  0.009  52  LEU BBB C   
394   O O   . LEU A 52  ? 1.020 1.386 1.070 -0.065 0.112  0.011  52  LEU BBB O   
395   C CB  . LEU A 52  ? 0.906 1.276 0.965 -0.073 0.105  -0.005 52  LEU BBB CB  
396   C CG  . LEU A 52  ? 0.890 1.266 0.953 -0.071 0.098  -0.011 52  LEU BBB CG  
397   C CD1 . LEU A 52  ? 1.037 1.404 1.100 -0.071 0.099  -0.011 52  LEU BBB CD1 
398   C CD2 . LEU A 52  ? 0.888 1.275 0.951 -0.074 0.096  -0.018 52  LEU BBB CD2 
399   N N   . ASN A 53  ? 0.959 1.302 1.007 -0.073 0.121  0.011  53  ASN BBB N   
400   C CA  . ASN A 53  ? 0.998 1.333 1.041 -0.074 0.128  0.018  53  ASN BBB CA  
401   C C   . ASN A 53  ? 1.039 1.371 1.078 -0.065 0.128  0.027  53  ASN BBB C   
402   O O   . ASN A 53  ? 1.015 1.352 1.050 -0.062 0.130  0.033  53  ASN BBB O   
403   C CB  . ASN A 53  ? 1.024 1.339 1.064 -0.081 0.135  0.018  53  ASN BBB CB  
404   C CG  . ASN A 53  ? 1.034 1.355 1.077 -0.092 0.136  0.009  53  ASN BBB CG  
405   O OD1 . ASN A 53  ? 1.111 1.448 1.156 -0.095 0.134  0.007  53  ASN BBB OD1 
406   N ND2 . ASN A 53  ? 1.137 1.445 1.180 -0.097 0.138  0.004  53  ASN BBB ND2 
407   N N   . THR A 54  ? 1.060 1.387 1.101 -0.059 0.126  0.028  54  THR BBB N   
408   C CA  . THR A 54  ? 1.018 1.348 1.058 -0.050 0.125  0.035  54  THR BBB CA  
409   C C   . THR A 54  ? 0.982 1.332 1.024 -0.046 0.118  0.034  54  THR BBB C   
410   O O   . THR A 54  ? 1.058 1.412 1.096 -0.040 0.119  0.041  54  THR BBB O   
411   C CB  . THR A 54  ? 0.990 1.318 1.034 -0.045 0.123  0.035  54  THR BBB CB  
412   O OG1 . THR A 54  ? 1.085 1.393 1.125 -0.046 0.130  0.035  54  THR BBB OG1 
413   C CG2 . THR A 54  ? 0.988 1.323 1.034 -0.035 0.120  0.041  54  THR BBB CG2 
414   N N   . MET A 55  ? 0.945 1.306 0.993 -0.048 0.110  0.026  55  MET BBB N   
415   C CA  . MET A 55  ? 0.943 1.321 0.994 -0.044 0.103  0.024  55  MET BBB CA  
416   C C   . MET A 55  ? 1.000 1.386 1.044 -0.044 0.106  0.025  55  MET BBB C   
417   O O   . MET A 55  ? 0.992 1.388 1.032 -0.038 0.103  0.028  55  MET BBB O   
418   C CB  . MET A 55  ? 0.914 1.299 0.972 -0.047 0.095  0.014  55  MET BBB CB  
419   C CG  . MET A 55  ? 0.922 1.304 0.988 -0.046 0.091  0.014  55  MET BBB CG  
420   S SD  . MET A 55  ? 1.065 1.451 1.138 -0.050 0.083  0.005  55  MET BBB SD  
421   C CE  . MET A 55  ? 0.976 1.375 1.052 -0.045 0.073  0.000  55  MET BBB CE  
422   N N   . LEU A 56  ? 1.022 1.405 1.064 -0.052 0.111  0.024  56  LEU BBB N   
423   C CA  . LEU A 56  ? 0.993 1.384 1.029 -0.053 0.115  0.026  56  LEU BBB CA  
424   C C   . LEU A 56  ? 1.008 1.392 1.037 -0.050 0.123  0.038  56  LEU BBB C   
425   O O   . LEU A 56  ? 1.016 1.411 1.039 -0.045 0.124  0.043  56  LEU BBB O   
426   C CB  . LEU A 56  ? 0.989 1.380 1.028 -0.063 0.119  0.022  56  LEU BBB CB  
427   C CG  . LEU A 56  ? 0.957 1.358 1.001 -0.065 0.112  0.010  56  LEU BBB CG  
428   C CD1 . LEU A 56  ? 0.952 1.356 0.999 -0.074 0.117  0.006  56  LEU BBB CD1 
429   C CD2 . LEU A 56  ? 0.950 1.370 0.995 -0.057 0.104  0.005  56  LEU BBB CD2 
430   N N   . ASN A 57  ? 1.013 1.376 1.041 -0.051 0.129  0.044  57  ASN BBB N   
431   C CA  . ASN A 57  ? 1.049 1.400 1.068 -0.048 0.137  0.056  57  ASN BBB CA  
432   C C   . ASN A 57  ? 1.050 1.409 1.065 -0.035 0.133  0.062  57  ASN BBB C   
433   O O   . ASN A 57  ? 1.090 1.446 1.097 -0.030 0.138  0.073  57  ASN BBB O   
434   C CB  . ASN A 57  ? 1.079 1.404 1.097 -0.052 0.143  0.058  57  ASN BBB CB  
435   C CG  . ASN A 57  ? 1.193 1.510 1.214 -0.065 0.149  0.055  57  ASN BBB CG  
436   O OD1 . ASN A 57  ? 1.257 1.589 1.280 -0.071 0.147  0.050  57  ASN BBB OD1 
437   N ND2 . ASN A 57  ? 1.282 1.574 1.300 -0.069 0.155  0.057  57  ASN BBB ND2 
438   N N   . THR A 58  ? 1.025 1.394 1.047 -0.030 0.124  0.056  58  THR BBB N   
439   C CA  . THR A 58  ? 1.048 1.428 1.068 -0.019 0.119  0.060  58  THR BBB CA  
440   C C   . THR A 58  ? 1.109 1.511 1.125 -0.014 0.115  0.059  58  THR BBB C   
441   O O   . THR A 58  ? 1.187 1.599 1.200 -0.003 0.111  0.064  58  THR BBB O   
442   C CB  . THR A 58  ? 1.033 1.418 1.063 -0.017 0.111  0.054  58  THR BBB CB  
443   O OG1 . THR A 58  ? 0.991 1.384 1.029 -0.023 0.104  0.043  58  THR BBB OG1 
444   C CG2 . THR A 58  ? 1.053 1.419 1.086 -0.018 0.116  0.057  58  THR BBB CG2 
445   N N   . VAL A 59  ? 1.099 1.509 1.115 -0.019 0.114  0.054  59  VAL BBB N   
446   C CA  . VAL A 59  ? 1.062 1.493 1.072 -0.014 0.111  0.052  59  VAL BBB CA  
447   C C   . VAL A 59  ? 1.107 1.538 1.106 -0.010 0.120  0.066  59  VAL BBB C   
448   O O   . VAL A 59  ? 1.150 1.566 1.145 -0.017 0.130  0.073  59  VAL BBB O   
449   C CB  . VAL A 59  ? 1.038 1.479 1.051 -0.020 0.109  0.042  59  VAL BBB CB  
450   C CG1 . VAL A 59  ? 1.095 1.559 1.101 -0.013 0.105  0.040  59  VAL BBB CG1 
451   C CG2 . VAL A 59  ? 1.031 1.471 1.055 -0.023 0.099  0.030  59  VAL BBB CG2 
452   N N   . GLY A 60  ? 1.133 1.578 1.125 0.002  0.117  0.071  60  GLY BBB N   
453   C CA  . GLY A 60  ? 1.296 1.741 1.275 0.008  0.126  0.086  60  GLY BBB CA  
454   C C   . GLY A 60  ? 1.277 1.738 1.248 0.008  0.130  0.089  60  GLY BBB C   
455   O O   . GLY A 60  ? 1.275 1.728 1.239 0.005  0.141  0.102  60  GLY BBB O   
456   N N   . GLY A 61  ? 1.180 1.666 1.152 0.011  0.121  0.077  61  GLY BBB N   
457   C CA  . GLY A 61  ? 1.304 1.810 1.267 0.013  0.125  0.079  61  GLY BBB CA  
458   C C   . GLY A 61  ? 1.278 1.783 1.248 0.001  0.128  0.072  61  GLY BBB C   
459   O O   . GLY A 61  ? 1.275 1.761 1.255 -0.010 0.130  0.069  61  GLY BBB O   
460   N N   . HIS A 62  ? 1.313 1.843 1.280 0.003  0.129  0.069  62  HIS BBB N   
461   C CA  . HIS A 62  ? 1.288 1.825 1.262 -0.006 0.129  0.059  62  HIS BBB CA  
462   C C   . HIS A 62  ? 1.301 1.819 1.280 -0.021 0.140  0.066  62  HIS BBB C   
463   O O   . HIS A 62  ? 1.398 1.911 1.387 -0.030 0.138  0.057  62  HIS BBB O   
464   C CB  . HIS A 62  ? 1.288 1.825 1.271 -0.005 0.116  0.041  62  HIS BBB CB  
465   C CG  . HIS A 62  ? 1.289 1.843 1.269 0.008  0.104  0.031  62  HIS BBB CG  
466   N ND1 . HIS A 62  ? 1.388 1.969 1.360 0.017  0.101  0.025  62  HIS BBB ND1 
467   C CD2 . HIS A 62  ? 1.270 1.817 1.253 0.013  0.094  0.025  62  HIS BBB CD2 
468   C CE1 . HIS A 62  ? 1.421 2.010 1.391 0.027  0.089  0.015  62  HIS BBB CE1 
469   N NE2 . HIS A 62  ? 1.309 1.879 1.287 0.024  0.084  0.015  62  HIS BBB NE2 
470   N N   . GLN A 63  ? 1.237 1.743 1.210 -0.023 0.151  0.083  63  GLN BBB N   
471   C CA  . GLN A 63  ? 1.272 1.755 1.251 -0.038 0.161  0.090  63  GLN BBB CA  
472   C C   . GLN A 63  ? 1.317 1.816 1.302 -0.049 0.167  0.088  63  GLN BBB C   
473   O O   . GLN A 63  ? 1.371 1.855 1.365 -0.063 0.171  0.086  63  GLN BBB O   
474   C CB  . GLN A 63  ? 1.328 1.791 1.299 -0.038 0.171  0.109  63  GLN BBB CB  
475   C CG  . GLN A 63  ? 1.397 1.841 1.366 -0.029 0.167  0.111  63  GLN BBB CG  
476   C CD  . GLN A 63  ? 1.418 1.841 1.397 -0.036 0.162  0.100  63  GLN BBB CD  
477   O OE1 . GLN A 63  ? 1.465 1.866 1.449 -0.048 0.169  0.102  63  GLN BBB OE1 
478   N NE2 . GLN A 63  ? 1.398 1.827 1.381 -0.030 0.150  0.088  63  GLN BBB NE2 
479   N N   . ALA A 64  ? 1.285 1.814 1.264 -0.043 0.167  0.087  64  ALA BBB N   
480   C CA  . ALA A 64  ? 1.267 1.817 1.253 -0.052 0.171  0.082  64  ALA BBB CA  
481   C C   . ALA A 64  ? 1.240 1.791 1.238 -0.056 0.162  0.064  64  ALA BBB C   
482   O O   . ALA A 64  ? 1.305 1.853 1.313 -0.069 0.165  0.061  64  ALA BBB O   
483   C CB  . ALA A 64  ? 1.348 1.934 1.326 -0.041 0.172  0.084  64  ALA BBB CB  
484   N N   . ALA A 65  ? 1.231 1.784 1.228 -0.045 0.149  0.051  65  ALA BBB N   
485   C CA  . ALA A 65  ? 1.213 1.764 1.220 -0.047 0.140  0.035  65  ALA BBB CA  
486   C C   . ALA A 65  ? 1.197 1.719 1.212 -0.059 0.142  0.036  65  ALA BBB C   
487   O O   . ALA A 65  ? 1.243 1.765 1.266 -0.067 0.141  0.028  65  ALA BBB O   
488   C CB  . ALA A 65  ? 1.209 1.764 1.214 -0.034 0.126  0.024  65  ALA BBB CB  
489   N N   . MET A 66  ? 1.133 1.631 1.144 -0.058 0.144  0.045  66  MET BBB N   
490   C CA  . MET A 66  ? 1.152 1.623 1.169 -0.068 0.146  0.045  66  MET BBB CA  
491   C C   . MET A 66  ? 1.247 1.713 1.269 -0.083 0.156  0.050  66  MET BBB C   
492   O O   . MET A 66  ? 1.383 1.839 1.413 -0.092 0.155  0.042  66  MET BBB O   
493   C CB  . MET A 66  ? 1.222 1.671 1.233 -0.062 0.148  0.055  66  MET BBB CB  
494   C CG  . MET A 66  ? 1.200 1.657 1.207 -0.048 0.138  0.052  66  MET BBB CG  
495   S SD  . MET A 66  ? 1.107 1.559 1.123 -0.047 0.126  0.036  66  MET BBB SD  
496   C CE  . MET A 66  ? 1.205 1.628 1.226 -0.058 0.131  0.039  66  MET BBB CE  
497   N N   . GLN A 67  ? 1.207 1.682 1.225 -0.086 0.166  0.061  67  GLN BBB N   
498   C CA  . GLN A 67  ? 1.238 1.711 1.263 -0.102 0.176  0.066  67  GLN BBB CA  
499   C C   . GLN A 67  ? 1.250 1.747 1.285 -0.108 0.173  0.053  67  GLN BBB C   
500   O O   . GLN A 67  ? 1.279 1.770 1.323 -0.121 0.175  0.049  67  GLN BBB O   
501   C CB  . GLN A 67  ? 1.370 1.848 1.388 -0.104 0.187  0.083  67  GLN BBB CB  
502   C CG  . GLN A 67  ? 1.511 1.975 1.536 -0.122 0.199  0.091  67  GLN BBB CG  
503   C CD  . GLN A 67  ? 1.648 2.071 1.670 -0.126 0.202  0.097  67  GLN BBB CD  
504   O OE1 . GLN A 67  ? 1.642 2.051 1.655 -0.114 0.200  0.103  67  GLN BBB OE1 
505   N NE2 . GLN A 67  ? 1.748 2.154 1.780 -0.142 0.206  0.094  67  GLN BBB NE2 
506   N N   . MET A 68  ? 1.254 1.779 1.286 -0.097 0.166  0.046  68  MET BBB N   
507   C CA  . MET A 68  ? 1.251 1.799 1.292 -0.100 0.162  0.033  68  MET BBB CA  
508   C C   . MET A 68  ? 1.240 1.773 1.288 -0.101 0.153  0.020  68  MET BBB C   
509   O O   . MET A 68  ? 1.334 1.874 1.391 -0.110 0.153  0.013  68  MET BBB O   
510   C CB  . MET A 68  ? 1.333 1.910 1.369 -0.085 0.155  0.026  68  MET BBB CB  
511   C CG  . MET A 68  ? 1.370 1.973 1.400 -0.082 0.163  0.035  68  MET BBB CG  
512   S SD  . MET A 68  ? 1.623 2.263 1.648 -0.065 0.154  0.023  68  MET BBB SD  
513   C CE  . MET A 68  ? 1.471 2.096 1.485 -0.048 0.144  0.021  68  MET BBB CE  
514   N N   . LEU A 69  ? 1.155 1.669 1.198 -0.093 0.146  0.019  69  LEU BBB N   
515   C CA  . LEU A 69  ? 1.091 1.590 1.139 -0.094 0.139  0.009  69  LEU BBB CA  
516   C C   . LEU A 69  ? 1.150 1.630 1.204 -0.108 0.145  0.011  69  LEU BBB C   
517   O O   . LEU A 69  ? 1.257 1.737 1.317 -0.113 0.141  0.001  69  LEU BBB O   
518   C CB  . LEU A 69  ? 1.048 1.531 1.091 -0.083 0.132  0.009  69  LEU BBB CB  
519   C CG  . LEU A 69  ? 1.021 1.489 1.068 -0.082 0.124  0.001  69  LEU BBB CG  
520   C CD1 . LEU A 69  ? 1.038 1.523 1.091 -0.081 0.117  -0.011 69  LEU BBB CD1 
521   C CD2 . LEU A 69  ? 0.995 1.453 1.038 -0.072 0.118  0.002  69  LEU BBB CD2 
522   N N   . LYS A 70  ? 1.163 1.625 1.213 -0.114 0.154  0.023  70  LYS BBB N   
523   C CA  . LYS A 70  ? 1.212 1.653 1.266 -0.128 0.160  0.023  70  LYS BBB CA  
524   C C   . LYS A 70  ? 1.289 1.749 1.354 -0.141 0.163  0.018  70  LYS BBB C   
525   O O   . LYS A 70  ? 1.375 1.828 1.447 -0.149 0.161  0.009  70  LYS BBB O   
526   C CB  . LYS A 70  ? 1.204 1.622 1.253 -0.131 0.169  0.038  70  LYS BBB CB  
527   C CG  . LYS A 70  ? 1.235 1.636 1.275 -0.118 0.167  0.044  70  LYS BBB CG  
528   C CD  . LYS A 70  ? 1.373 1.761 1.414 -0.113 0.158  0.035  70  LYS BBB CD  
529   C CE  . LYS A 70  ? 1.340 1.719 1.373 -0.099 0.155  0.040  70  LYS BBB CE  
530   N NZ  . LYS A 70  ? 1.251 1.624 1.287 -0.094 0.146  0.032  70  LYS BBB NZ  
531   N N   . GLU A 71  ? 1.344 1.830 1.410 -0.141 0.167  0.022  71  GLU BBB N   
532   C CA  . GLU A 71  ? 1.370 1.881 1.447 -0.153 0.170  0.016  71  GLU BBB CA  
533   C C   . GLU A 71  ? 1.346 1.872 1.429 -0.149 0.160  0.001  71  GLU BBB C   
534   O O   . GLU A 71  ? 1.436 1.968 1.528 -0.160 0.159  -0.007 71  GLU BBB O   
535   C CB  . GLU A 71  ? 1.475 2.014 1.551 -0.151 0.176  0.024  71  GLU BBB CB  
536   C CG  . GLU A 71  ? 1.619 2.146 1.691 -0.159 0.188  0.042  71  GLU BBB CG  
537   C CD  . GLU A 71  ? 1.837 2.398 1.911 -0.160 0.195  0.050  71  GLU BBB CD  
538   O OE1 . GLU A 71  ? 1.888 2.479 1.960 -0.148 0.190  0.043  71  GLU BBB OE1 
539   O OE2 . GLU A 71  ? 1.914 2.472 1.990 -0.172 0.207  0.063  71  GLU BBB OE2 
540   N N   . THR A 72  ? 1.231 1.764 1.307 -0.133 0.151  -0.005 72  THR BBB N   
541   C CA  . THR A 72  ? 1.193 1.738 1.274 -0.127 0.141  -0.018 72  THR BBB CA  
542   C C   . THR A 72  ? 1.205 1.727 1.288 -0.132 0.137  -0.024 72  THR BBB C   
543   O O   . THR A 72  ? 1.325 1.858 1.415 -0.136 0.134  -0.034 72  THR BBB O   
544   C CB  . THR A 72  ? 1.127 1.680 1.202 -0.110 0.132  -0.022 72  THR BBB CB  
545   O OG1 . THR A 72  ? 1.231 1.809 1.303 -0.105 0.135  -0.019 72  THR BBB OG1 
546   C CG2 . THR A 72  ? 1.140 1.701 1.218 -0.104 0.122  -0.035 72  THR BBB CG2 
547   N N   . ILE A 73  ? 1.153 1.646 1.230 -0.130 0.138  -0.018 73  ILE BBB N   
548   C CA  . ILE A 73  ? 1.173 1.645 1.251 -0.134 0.135  -0.023 73  ILE BBB CA  
549   C C   . ILE A 73  ? 1.300 1.770 1.385 -0.150 0.141  -0.026 73  ILE BBB C   
550   O O   . ILE A 73  ? 1.394 1.866 1.484 -0.153 0.137  -0.036 73  ILE BBB O   
551   C CB  . ILE A 73  ? 1.146 1.589 1.216 -0.129 0.137  -0.015 73  ILE BBB CB  
552   C CG1 . ILE A 73  ? 1.106 1.551 1.171 -0.114 0.129  -0.015 73  ILE BBB CG1 
553   C CG2 . ILE A 73  ? 1.206 1.626 1.277 -0.134 0.137  -0.019 73  ILE BBB CG2 
554   C CD1 . ILE A 73  ? 1.054 1.477 1.112 -0.108 0.131  -0.007 73  ILE BBB CD1 
555   N N   . ASN A 74  ? 1.305 1.772 1.392 -0.160 0.150  -0.018 74  ASN BBB N   
556   C CA  . ASN A 74  ? 1.302 1.766 1.397 -0.177 0.156  -0.021 74  ASN BBB CA  
557   C C   . ASN A 74  ? 1.353 1.851 1.460 -0.183 0.153  -0.031 74  ASN BBB C   
558   O O   . ASN A 74  ? 1.406 1.904 1.520 -0.193 0.151  -0.041 74  ASN BBB O   
559   C CB  . ASN A 74  ? 1.410 1.864 1.505 -0.187 0.167  -0.007 74  ASN BBB CB  
560   C CG  . ASN A 74  ? 1.530 1.947 1.615 -0.183 0.170  0.002  74  ASN BBB CG  
561   O OD1 . ASN A 74  ? 1.612 2.017 1.690 -0.171 0.164  -0.000 74  ASN BBB OD1 
562   N ND2 . ASN A 74  ? 1.646 2.047 1.731 -0.192 0.180  0.013  74  ASN BBB ND2 
563   N N   . GLU A 75  ? 1.510 2.037 1.617 -0.176 0.151  -0.031 75  GLU BBB N   
564   C CA  . GLU A 75  ? 1.575 2.137 1.693 -0.178 0.147  -0.041 75  GLU BBB CA  
565   C C   . GLU A 75  ? 1.528 2.090 1.645 -0.171 0.137  -0.054 75  GLU BBB C   
566   O O   . GLU A 75  ? 1.611 2.187 1.736 -0.179 0.135  -0.063 75  GLU BBB O   
567   C CB  . GLU A 75  ? 1.667 2.259 1.783 -0.168 0.147  -0.038 75  GLU BBB CB  
568   C CG  . GLU A 75  ? 1.911 2.541 2.036 -0.166 0.142  -0.049 75  GLU BBB CG  
569   C CD  . GLU A 75  ? 2.098 2.759 2.222 -0.156 0.143  -0.047 75  GLU BBB CD  
570   O OE1 . GLU A 75  ? 2.066 2.717 2.179 -0.145 0.144  -0.040 75  GLU BBB OE1 
571   O OE2 . GLU A 75  ? 2.150 2.846 2.283 -0.158 0.144  -0.052 75  GLU BBB OE2 
572   N N   . GLU A 76  ? 1.385 1.931 1.492 -0.156 0.131  -0.053 76  GLU BBB N   
573   C CA  . GLU A 76  ? 1.347 1.891 1.452 -0.149 0.122  -0.062 76  GLU BBB CA  
574   C C   . GLU A 76  ? 1.363 1.887 1.469 -0.158 0.122  -0.067 76  GLU BBB C   
575   O O   . GLU A 76  ? 1.401 1.934 1.509 -0.157 0.116  -0.077 76  GLU BBB O   
576   C CB  . GLU A 76  ? 1.274 1.805 1.370 -0.132 0.116  -0.059 76  GLU BBB CB  
577   C CG  . GLU A 76  ? 1.291 1.843 1.386 -0.121 0.113  -0.059 76  GLU BBB CG  
578   C CD  . GLU A 76  ? 1.366 1.948 1.467 -0.117 0.107  -0.069 76  GLU BBB CD  
579   O OE1 . GLU A 76  ? 1.367 1.948 1.469 -0.116 0.102  -0.076 76  GLU BBB OE1 
580   O OE2 . GLU A 76  ? 1.425 2.033 1.528 -0.114 0.108  -0.070 76  GLU BBB OE2 
581   N N   . ALA A 77  ? 1.405 1.903 1.509 -0.165 0.129  -0.060 77  ALA BBB N   
582   C CA  . ALA A 77  ? 1.476 1.953 1.579 -0.174 0.130  -0.065 77  ALA BBB CA  
583   C C   . ALA A 77  ? 1.577 2.071 1.692 -0.189 0.131  -0.075 77  ALA BBB C   
584   O O   . ALA A 77  ? 1.650 2.143 1.766 -0.191 0.126  -0.085 77  ALA BBB O   
585   C CB  . ALA A 77  ? 1.461 1.905 1.559 -0.178 0.137  -0.055 77  ALA BBB CB  
586   N N   . ALA A 78  ? 1.572 2.084 1.695 -0.199 0.136  -0.071 78  ALA BBB N   
587   C CA  . ALA A 78  ? 1.623 2.155 1.759 -0.215 0.137  -0.081 78  ALA BBB CA  
588   C C   . ALA A 78  ? 1.669 2.233 1.809 -0.208 0.128  -0.093 78  ALA BBB C   
589   O O   . ALA A 78  ? 1.869 2.439 2.015 -0.216 0.124  -0.105 78  ALA BBB O   
590   C CB  . ALA A 78  ? 1.699 2.248 1.845 -0.227 0.146  -0.073 78  ALA BBB CB  
591   N N   . GLU A 79  ? 1.616 2.199 1.753 -0.193 0.123  -0.091 79  GLU BBB N   
592   C CA  . GLU A 79  ? 1.649 2.260 1.789 -0.184 0.114  -0.102 79  GLU BBB CA  
593   C C   . GLU A 79  ? 1.645 2.238 1.776 -0.176 0.107  -0.108 79  GLU BBB C   
594   O O   . GLU A 79  ? 1.725 2.337 1.860 -0.176 0.101  -0.119 79  GLU BBB O   
595   C CB  . GLU A 79  ? 1.693 2.324 1.830 -0.168 0.111  -0.099 79  GLU BBB CB  
596   C CG  . GLU A 79  ? 1.862 2.532 2.010 -0.173 0.114  -0.101 79  GLU BBB CG  
597   C CD  . GLU A 79  ? 2.010 2.679 2.164 -0.189 0.125  -0.092 79  GLU BBB CD  
598   O OE1 . GLU A 79  ? 2.096 2.733 2.244 -0.192 0.130  -0.082 79  GLU BBB OE1 
599   O OE2 . GLU A 79  ? 2.035 2.736 2.202 -0.199 0.128  -0.094 79  GLU BBB OE2 
600   N N   . TRP A 80  ? 1.516 2.076 1.636 -0.170 0.108  -0.101 80  TRP BBB N   
601   C CA  . TRP A 80  ? 1.462 2.006 1.574 -0.164 0.103  -0.106 80  TRP BBB CA  
602   C C   . TRP A 80  ? 1.583 2.124 1.700 -0.177 0.104  -0.116 80  TRP BBB C   
603   O O   . TRP A 80  ? 1.726 2.278 1.842 -0.174 0.098  -0.126 80  TRP BBB O   
604   C CB  . TRP A 80  ? 1.376 1.887 1.478 -0.156 0.106  -0.096 80  TRP BBB CB  
605   C CG  . TRP A 80  ? 1.273 1.767 1.366 -0.150 0.102  -0.100 80  TRP BBB CG  
606   C CD1 . TRP A 80  ? 1.247 1.721 1.338 -0.157 0.105  -0.103 80  TRP BBB CD1 
607   C CD2 . TRP A 80  ? 1.187 1.685 1.274 -0.136 0.095  -0.100 80  TRP BBB CD2 
608   N NE1 . TRP A 80  ? 1.201 1.669 1.284 -0.147 0.100  -0.106 80  TRP BBB NE1 
609   C CE2 . TRP A 80  ? 1.163 1.646 1.244 -0.135 0.094  -0.103 80  TRP BBB CE2 
610   C CE3 . TRP A 80  ? 1.145 1.658 1.231 -0.123 0.089  -0.098 80  TRP BBB CE3 
611   C CZ2 . TRP A 80  ? 1.165 1.647 1.238 -0.122 0.089  -0.103 80  TRP BBB CZ2 
612   C CZ3 . TRP A 80  ? 1.131 1.641 1.210 -0.111 0.084  -0.098 80  TRP BBB CZ3 
613   C CH2 . TRP A 80  ? 1.168 1.663 1.240 -0.111 0.084  -0.099 80  TRP BBB CH2 
614   N N   . ASP A 81  ? 1.753 2.278 1.874 -0.193 0.112  -0.113 81  ASP BBB N   
615   C CA  . ASP A 81  ? 1.846 2.364 1.972 -0.207 0.112  -0.124 81  ASP BBB CA  
616   C C   . ASP A 81  ? 1.822 2.378 1.961 -0.215 0.108  -0.137 81  ASP BBB C   
617   O O   . ASP A 81  ? 1.905 2.466 2.045 -0.219 0.103  -0.150 81  ASP BBB O   
618   C CB  . ASP A 81  ? 1.915 2.409 2.045 -0.222 0.122  -0.118 81  ASP BBB CB  
619   C CG  . ASP A 81  ? 2.008 2.464 2.126 -0.214 0.126  -0.107 81  ASP BBB CG  
620   O OD1 . ASP A 81  ? 2.125 2.571 2.232 -0.200 0.121  -0.108 81  ASP BBB OD1 
621   O OD2 . ASP A 81  ? 2.041 2.477 2.159 -0.222 0.134  -0.098 81  ASP BBB OD2 
622   N N   . ARG A 82  ? 1.634 2.218 1.781 -0.217 0.109  -0.133 82  ARG BBB N   
623   C CA  . ARG A 82  ? 1.634 2.259 1.795 -0.224 0.105  -0.144 82  ARG BBB CA  
624   C C   . ARG A 82  ? 1.603 2.249 1.758 -0.208 0.095  -0.153 82  ARG BBB C   
625   O O   . ARG A 82  ? 1.652 2.320 1.813 -0.213 0.089  -0.166 82  ARG BBB O   
626   C CB  . ARG A 82  ? 1.709 2.361 1.880 -0.227 0.110  -0.138 82  ARG BBB CB  
627   C CG  . ARG A 82  ? 1.824 2.524 2.006 -0.226 0.104  -0.147 82  ARG BBB CG  
628   C CD  . ARG A 82  ? 1.862 2.589 2.052 -0.227 0.110  -0.139 82  ARG BBB CD  
629   N NE  . ARG A 82  ? 1.973 2.745 2.170 -0.218 0.104  -0.147 82  ARG BBB NE  
630   C CZ  . ARG A 82  ? 1.933 2.716 2.122 -0.196 0.098  -0.145 82  ARG BBB CZ  
631   N NH1 . ARG A 82  ? 1.842 2.594 2.015 -0.182 0.098  -0.136 82  ARG BBB NH1 
632   N NH2 . ARG A 82  ? 1.940 2.764 2.136 -0.188 0.093  -0.152 82  ARG BBB NH2 
633   N N   . LEU A 83  ? 1.549 2.187 1.692 -0.188 0.091  -0.146 83  LEU BBB N   
634   C CA  . LEU A 83  ? 1.543 2.198 1.680 -0.172 0.082  -0.151 83  LEU BBB CA  
635   C C   . LEU A 83  ? 1.522 2.155 1.648 -0.167 0.078  -0.155 83  LEU BBB C   
636   O O   . LEU A 83  ? 1.598 2.248 1.719 -0.157 0.071  -0.162 83  LEU BBB O   
637   C CB  A LEU A 83  ? 1.535 2.193 1.666 -0.154 0.080  -0.142 83  LEU BBB CB  
638   C CG  A LEU A 83  ? 1.747 2.434 1.889 -0.157 0.083  -0.141 83  LEU BBB CG  
639   C CD1 A LEU A 83  ? 1.798 2.482 1.933 -0.141 0.082  -0.132 83  LEU BBB CD1 
640   C CD2 A LEU A 83  ? 1.858 2.587 2.010 -0.159 0.078  -0.152 83  LEU BBB CD2 
641   N N   . HIS A 84  ? 1.489 2.087 1.609 -0.172 0.084  -0.151 84  HIS BBB N   
642   C CA  . HIS A 84  ? 1.432 2.009 1.541 -0.167 0.081  -0.154 84  HIS BBB CA  
643   C C   . HIS A 84  ? 1.492 2.044 1.603 -0.183 0.088  -0.157 84  HIS BBB C   
644   O O   . HIS A 84  ? 1.572 2.092 1.677 -0.182 0.093  -0.148 84  HIS BBB O   
645   C CB  . HIS A 84  ? 1.380 1.935 1.476 -0.150 0.082  -0.141 84  HIS BBB CB  
646   C CG  . HIS A 84  ? 1.437 2.010 1.531 -0.135 0.076  -0.137 84  HIS BBB CG  
647   N ND1 . HIS A 84  ? 1.506 2.083 1.603 -0.132 0.078  -0.128 84  HIS BBB ND1 
648   C CD2 . HIS A 84  ? 1.481 2.068 1.569 -0.122 0.069  -0.139 84  HIS BBB CD2 
649   C CE1 . HIS A 84  ? 1.496 2.087 1.590 -0.117 0.072  -0.127 84  HIS BBB CE1 
650   N NE2 . HIS A 84  ? 1.541 2.137 1.629 -0.111 0.066  -0.133 84  HIS BBB NE2 
651   N N   . PRO A 85  ? 1.509 2.075 1.630 -0.198 0.086  -0.170 85  PRO BBB N   
652   C CA  . PRO A 85  ? 1.507 2.047 1.631 -0.214 0.092  -0.174 85  PRO BBB CA  
653   C C   . PRO A 85  ? 1.510 2.025 1.620 -0.206 0.090  -0.180 85  PRO BBB C   
654   O O   . PRO A 85  ? 1.527 2.053 1.628 -0.193 0.083  -0.184 85  PRO BBB O   
655   C CB  . PRO A 85  ? 1.504 2.070 1.643 -0.231 0.089  -0.189 85  PRO BBB CB  
656   C CG  . PRO A 85  ? 1.556 2.165 1.702 -0.224 0.084  -0.189 85  PRO BBB CG  
657   C CD  . PRO A 85  ? 1.562 2.169 1.693 -0.201 0.080  -0.182 85  PRO BBB CD  
658   N N   . VAL A 86  ? 1.546 2.027 1.654 -0.215 0.095  -0.179 86  VAL BBB N   
659   C CA  . VAL A 86  ? 1.631 2.086 1.726 -0.208 0.095  -0.184 86  VAL BBB CA  
660   C C   . VAL A 86  ? 1.704 2.166 1.801 -0.217 0.089  -0.204 86  VAL BBB C   
661   O O   . VAL A 86  ? 1.760 2.221 1.870 -0.236 0.091  -0.213 86  VAL BBB O   
662   C CB  . VAL A 86  ? 1.648 2.062 1.738 -0.210 0.103  -0.174 86  VAL BBB CB  
663   C CG1 . VAL A 86  ? 1.725 2.114 1.802 -0.203 0.103  -0.180 86  VAL BBB CG1 
664   C CG2 . VAL A 86  ? 1.662 2.073 1.750 -0.200 0.107  -0.155 86  VAL BBB CG2 
665   N N   . HIS A 87  ? 1.759 2.229 1.844 -0.204 0.083  -0.212 87  HIS BBB N   
666   C CA  . HIS A 87  ? 1.749 2.227 1.833 -0.209 0.077  -0.232 87  HIS BBB CA  
667   C C   . HIS A 87  ? 1.840 2.278 1.918 -0.213 0.081  -0.238 87  HIS BBB C   
668   O O   . HIS A 87  ? 1.971 2.386 2.036 -0.200 0.084  -0.229 87  HIS BBB O   
669   C CB  . HIS A 87  ? 1.633 2.136 1.706 -0.190 0.069  -0.237 87  HIS BBB CB  
670   C CG  . HIS A 87  ? 1.587 2.128 1.666 -0.185 0.064  -0.232 87  HIS BBB CG  
671   N ND1 . HIS A 87  ? 1.659 2.235 1.750 -0.194 0.058  -0.246 87  HIS BBB ND1 
672   C CD2 . HIS A 87  ? 1.673 2.223 1.749 -0.171 0.065  -0.217 87  HIS BBB CD2 
673   C CE1 . HIS A 87  ? 1.739 2.344 1.832 -0.185 0.055  -0.238 87  HIS BBB CE1 
674   N NE2 . HIS A 87  ? 1.781 2.368 1.865 -0.171 0.059  -0.221 87  HIS BBB NE2 
675   N N   . ALA A 88  ? 1.867 2.298 1.954 -0.232 0.080  -0.253 88  ALA BBB N   
676   C CA  . ALA A 88  ? 1.960 2.349 2.042 -0.237 0.085  -0.258 88  ALA BBB CA  
677   C C   . ALA A 88  ? 2.029 2.416 2.098 -0.229 0.078  -0.277 88  ALA BBB C   
678   O O   . ALA A 88  ? 2.151 2.570 2.222 -0.229 0.069  -0.292 88  ALA BBB O   
679   C CB  . ALA A 88  ? 2.071 2.445 2.170 -0.262 0.088  -0.263 88  ALA BBB CB  
680   N N   . GLY A 89  ? 2.096 2.447 2.153 -0.221 0.082  -0.276 89  GLY BBB N   
681   C CA  . GLY A 89  ? 2.144 2.489 2.186 -0.213 0.077  -0.294 89  GLY BBB CA  
682   C C   . GLY A 89  ? 2.171 2.482 2.198 -0.197 0.083  -0.287 89  GLY BBB C   
683   O O   . GLY A 89  ? 2.245 2.539 2.270 -0.191 0.090  -0.267 89  GLY BBB O   
684   N N   . PRO A 90  ? 2.145 2.446 2.159 -0.190 0.079  -0.305 90  PRO BBB N   
685   C CA  . PRO A 90  ? 2.143 2.416 2.140 -0.173 0.084  -0.299 90  PRO BBB CA  
686   C C   . PRO A 90  ? 2.034 2.330 2.021 -0.152 0.085  -0.283 90  PRO BBB C   
687   O O   . PRO A 90  ? 1.968 2.301 1.953 -0.146 0.079  -0.285 90  PRO BBB O   
688   C CB  . PRO A 90  ? 2.203 2.469 2.190 -0.170 0.078  -0.325 90  PRO BBB CB  
689   C CG  . PRO A 90  ? 2.265 2.547 2.266 -0.190 0.071  -0.344 90  PRO BBB CG  
690   C CD  . PRO A 90  ? 2.162 2.480 2.176 -0.196 0.069  -0.331 90  PRO BBB CD  
691   N N   . ILE A 91  ? 2.032 2.307 2.013 -0.141 0.093  -0.266 91  ILE BBB N   
692   C CA  . ILE A 91  ? 2.004 2.299 1.977 -0.123 0.094  -0.249 91  ILE BBB CA  
693   C C   . ILE A 91  ? 2.045 2.346 2.001 -0.105 0.092  -0.258 91  ILE BBB C   
694   O O   . ILE A 91  ? 2.096 2.370 2.042 -0.099 0.095  -0.266 91  ILE BBB O   
695   C CB  . ILE A 91  ? 2.070 2.345 2.046 -0.119 0.103  -0.226 91  ILE BBB CB  
696   C CG1 . ILE A 91  ? 2.057 2.331 2.049 -0.135 0.105  -0.217 91  ILE BBB CG1 
697   C CG2 . ILE A 91  ? 2.002 2.296 1.971 -0.102 0.104  -0.210 91  ILE BBB CG2 
698   C CD1 . ILE A 91  ? 2.069 2.309 2.068 -0.150 0.109  -0.221 91  ILE BBB CD1 
699   N N   . ALA A 92  ? 2.179 2.514 2.129 -0.095 0.088  -0.257 92  ALA BBB N   
700   C CA  . ALA A 92  ? 2.230 2.579 2.162 -0.076 0.086  -0.262 92  ALA BBB CA  
701   C C   . ALA A 92  ? 2.233 2.572 2.157 -0.060 0.094  -0.244 92  ALA BBB C   
702   O O   . ALA A 92  ? 2.286 2.625 2.218 -0.060 0.098  -0.223 92  ALA BBB O   
703   C CB  . ALA A 92  ? 2.235 2.625 2.165 -0.071 0.080  -0.262 92  ALA BBB CB  
704   N N   . PRO A 93  ? 2.154 2.484 2.064 -0.047 0.096  -0.252 93  PRO BBB N   
705   C CA  . PRO A 93  ? 2.162 2.485 2.065 -0.031 0.104  -0.235 93  PRO BBB CA  
706   C C   . PRO A 93  ? 2.173 2.525 2.077 -0.024 0.105  -0.215 93  PRO BBB C   
707   O O   . PRO A 93  ? 2.181 2.562 2.079 -0.018 0.100  -0.217 93  PRO BBB O   
708   C CB  . PRO A 93  ? 2.254 2.576 2.139 -0.017 0.104  -0.251 93  PRO BBB CB  
709   C CG  . PRO A 93  ? 2.304 2.640 2.185 -0.023 0.095  -0.275 93  PRO BBB CG  
710   C CD  . PRO A 93  ? 2.206 2.535 2.105 -0.045 0.091  -0.278 93  PRO BBB CD  
711   N N   . GLY A 94  ? 2.155 2.498 2.068 -0.024 0.111  -0.194 94  GLY BBB N   
712   C CA  . GLY A 94  ? 2.120 2.482 2.037 -0.019 0.113  -0.173 94  GLY BBB CA  
713   C C   . GLY A 94  ? 2.051 2.426 1.980 -0.030 0.108  -0.168 94  GLY BBB C   
714   O O   . GLY A 94  ? 2.072 2.464 2.003 -0.025 0.107  -0.153 94  GLY BBB O   
715   N N   . GLN A 95  ? 1.986 2.352 1.923 -0.045 0.104  -0.180 95  GLN BBB N   
716   C CA  . GLN A 95  ? 1.853 2.232 1.802 -0.056 0.099  -0.177 95  GLN BBB CA  
717   C C   . GLN A 95  ? 1.758 2.113 1.719 -0.067 0.104  -0.168 95  GLN BBB C   
718   O O   . GLN A 95  ? 1.763 2.092 1.723 -0.069 0.109  -0.171 95  GLN BBB O   
719   C CB  . GLN A 95  ? 1.945 2.337 1.896 -0.066 0.092  -0.196 95  GLN BBB CB  
720   C CG  . GLN A 95  ? 2.109 2.527 2.048 -0.056 0.086  -0.207 95  GLN BBB CG  
721   C CD  . GLN A 95  ? 2.051 2.494 1.986 -0.044 0.085  -0.191 95  GLN BBB CD  
722   O OE1 . GLN A 95  ? 2.009 2.464 1.954 -0.049 0.083  -0.183 95  GLN BBB OE1 
723   N NE2 . GLN A 95  ? 2.079 2.530 2.000 -0.028 0.088  -0.186 95  GLN BBB NE2 
724   N N   . MET A 96  ? 1.666 2.031 1.638 -0.073 0.103  -0.156 96  MET BBB N   
725   C CA  . MET A 96  ? 1.602 1.948 1.585 -0.082 0.107  -0.147 96  MET BBB CA  
726   C C   . MET A 96  ? 1.547 1.896 1.540 -0.098 0.104  -0.157 96  MET BBB C   
727   O O   . MET A 96  ? 1.591 1.963 1.585 -0.101 0.098  -0.166 96  MET BBB O   
728   C CB  . MET A 96  ? 1.529 1.880 1.515 -0.075 0.109  -0.128 96  MET BBB CB  
729   C CG  . MET A 96  ? 1.561 1.896 1.556 -0.082 0.113  -0.117 96  MET BBB CG  
730   S SD  . MET A 96  ? 1.704 2.049 1.702 -0.072 0.113  -0.097 96  MET BBB SD  
731   C CE  . MET A 96  ? 1.447 1.820 1.441 -0.064 0.108  -0.098 96  MET BBB CE  
732   N N   . ARG A 97  ? 1.418 1.746 1.418 -0.109 0.108  -0.153 97  ARG BBB N   
733   C CA  . ARG A 97  ? 1.366 1.700 1.378 -0.125 0.106  -0.160 97  ARG BBB CA  
734   C C   . ARG A 97  ? 1.355 1.710 1.376 -0.126 0.104  -0.149 97  ARG BBB C   
735   O O   . ARG A 97  ? 1.305 1.664 1.324 -0.116 0.105  -0.135 97  ARG BBB O   
736   C CB  . ARG A 97  ? 1.455 1.758 1.471 -0.136 0.112  -0.160 97  ARG BBB CB  
737   C CG  . ARG A 97  ? 1.522 1.810 1.541 -0.134 0.118  -0.141 97  ARG BBB CG  
738   C CD  . ARG A 97  ? 1.595 1.850 1.615 -0.142 0.124  -0.142 97  ARG BBB CD  
739   N NE  . ARG A 97  ? 1.579 1.821 1.601 -0.139 0.130  -0.124 97  ARG BBB NE  
740   C CZ  . ARG A 97  ? 1.539 1.788 1.570 -0.147 0.132  -0.115 97  ARG BBB CZ  
741   N NH1 . ARG A 97  ? 1.539 1.808 1.579 -0.159 0.129  -0.121 97  ARG BBB NH1 
742   N NH2 . ARG A 97  ? 1.495 1.732 1.525 -0.142 0.137  -0.099 97  ARG BBB NH2 
743   N N   . GLU A 98  ? 1.483 1.851 1.514 -0.139 0.101  -0.156 98  GLU BBB N   
744   C CA  . GLU A 98  ? 1.470 1.860 1.509 -0.140 0.099  -0.148 98  GLU BBB CA  
745   C C   . GLU A 98  ? 1.473 1.848 1.519 -0.146 0.105  -0.136 98  GLU BBB C   
746   O O   . GLU A 98  ? 1.524 1.880 1.574 -0.157 0.110  -0.138 98  GLU BBB O   
747   C CB  . GLU A 98  ? 1.547 1.962 1.595 -0.150 0.094  -0.161 98  GLU BBB CB  
748   C CG  . GLU A 98  ? 1.612 2.044 1.653 -0.145 0.087  -0.175 98  GLU BBB CG  
749   C CD  . GLU A 98  ? 1.722 2.184 1.773 -0.155 0.081  -0.188 98  GLU BBB CD  
750   O OE1 . GLU A 98  ? 1.718 2.186 1.782 -0.167 0.083  -0.186 98  GLU BBB OE1 
751   O OE2 . GLU A 98  ? 1.849 2.329 1.895 -0.150 0.075  -0.200 98  GLU BBB OE2 
752   N N   . PRO A 99  ? 1.403 1.786 1.451 -0.139 0.105  -0.122 99  PRO BBB N   
753   C CA  . PRO A 99  ? 1.346 1.718 1.399 -0.142 0.111  -0.110 99  PRO BBB CA  
754   C C   . PRO A 99  ? 1.380 1.766 1.444 -0.156 0.111  -0.113 99  PRO BBB C   
755   O O   . PRO A 99  ? 1.356 1.769 1.425 -0.156 0.106  -0.119 99  PRO BBB O   
756   C CB  . PRO A 99  ? 1.253 1.631 1.303 -0.129 0.109  -0.099 99  PRO BBB CB  
757   C CG  . PRO A 99  ? 1.221 1.622 1.270 -0.123 0.102  -0.104 99  PRO BBB CG  
758   C CD  . PRO A 99  ? 1.358 1.759 1.402 -0.125 0.100  -0.118 99  PRO BBB CD  
759   N N   . ARG A 100 ? 1.393 1.761 1.461 -0.165 0.118  -0.109 100 ARG BBB N   
760   C CA  . ARG A 100 ? 1.392 1.773 1.470 -0.177 0.120  -0.107 100 ARG BBB CA  
761   C C   . ARG A 100 ? 1.376 1.764 1.455 -0.170 0.122  -0.093 100 ARG BBB C   
762   O O   . ARG A 100 ? 1.384 1.763 1.456 -0.158 0.121  -0.085 100 ARG BBB O   
763   C CB  . ARG A 100 ? 1.445 1.803 1.527 -0.192 0.127  -0.107 100 ARG BBB CB  
764   C CG  . ARG A 100 ? 1.550 1.892 1.630 -0.198 0.126  -0.121 100 ARG BBB CG  
765   C CD  . ARG A 100 ? 1.648 1.953 1.726 -0.205 0.134  -0.116 100 ARG BBB CD  
766   N NE  . ARG A 100 ? 1.846 2.135 1.925 -0.216 0.133  -0.131 100 ARG BBB NE  
767   C CZ  . ARG A 100 ? 2.030 2.312 2.119 -0.235 0.137  -0.135 100 ARG BBB CZ  
768   N NH1 . ARG A 100 ? 1.971 2.261 2.069 -0.244 0.142  -0.124 100 ARG BBB NH1 
769   N NH2 . ARG A 100 ? 2.198 2.465 2.288 -0.244 0.135  -0.150 100 ARG BBB NH2 
770   N N   . GLY A 101 ? 1.395 1.800 1.483 -0.179 0.124  -0.091 101 GLY BBB N   
771   C CA  . GLY A 101 ? 1.318 1.730 1.406 -0.172 0.125  -0.079 101 GLY BBB CA  
772   C C   . GLY A 101 ? 1.255 1.639 1.336 -0.167 0.131  -0.068 101 GLY BBB C   
773   O O   . GLY A 101 ? 1.244 1.626 1.320 -0.155 0.129  -0.060 101 GLY BBB O   
774   N N   . SER A 102 ? 1.198 1.558 1.278 -0.177 0.137  -0.066 102 SER BBB N   
775   C CA  . SER A 102 ? 1.212 1.544 1.285 -0.173 0.143  -0.055 102 SER BBB CA  
776   C C   . SER A 102 ? 1.215 1.532 1.280 -0.159 0.140  -0.056 102 SER BBB C   
777   O O   . SER A 102 ? 1.267 1.569 1.326 -0.151 0.143  -0.045 102 SER BBB O   
778   C CB  . SER A 102 ? 1.284 1.592 1.359 -0.187 0.150  -0.056 102 SER BBB CB  
779   O OG  . SER A 102 ? 1.608 1.933 1.693 -0.200 0.153  -0.055 102 SER BBB OG  
780   N N   . ASP A 103 ? 1.281 1.604 1.344 -0.157 0.134  -0.067 103 ASP BBB N   
781   C CA  . ASP A 103 ? 1.234 1.548 1.289 -0.144 0.132  -0.066 103 ASP BBB CA  
782   C C   . ASP A 103 ? 1.169 1.499 1.223 -0.132 0.128  -0.058 103 ASP BBB C   
783   O O   . ASP A 103 ? 1.190 1.510 1.240 -0.122 0.128  -0.051 103 ASP BBB O   
784   C CB  . ASP A 103 ? 1.264 1.581 1.316 -0.143 0.128  -0.079 103 ASP BBB CB  
785   C CG  . ASP A 103 ? 1.321 1.619 1.373 -0.153 0.131  -0.088 103 ASP BBB CG  
786   O OD1 . ASP A 103 ? 1.311 1.583 1.359 -0.155 0.137  -0.083 103 ASP BBB OD1 
787   O OD2 . ASP A 103 ? 1.398 1.708 1.452 -0.161 0.127  -0.101 103 ASP BBB OD2 
788   N N   . ILE A 104 ? 1.073 1.427 1.133 -0.134 0.123  -0.061 104 ILE BBB N   
789   C CA  . ILE A 104 ? 1.038 1.405 1.098 -0.123 0.118  -0.055 104 ILE BBB CA  
790   C C   . ILE A 104 ? 1.019 1.379 1.078 -0.120 0.122  -0.044 104 ILE BBB C   
791   O O   . ILE A 104 ? 1.024 1.382 1.081 -0.111 0.119  -0.038 104 ILE BBB O   
792   C CB  . ILE A 104 ? 1.054 1.448 1.120 -0.125 0.113  -0.062 104 ILE BBB CB  
793   C CG1 . ILE A 104 ? 1.046 1.447 1.110 -0.124 0.108  -0.072 104 ILE BBB CG1 
794   C CG2 . ILE A 104 ? 1.027 1.432 1.093 -0.115 0.109  -0.056 104 ILE BBB CG2 
795   C CD1 . ILE A 104 ? 1.093 1.519 1.159 -0.118 0.101  -0.075 104 ILE BBB CD1 
796   N N   . ALA A 105 ? 1.024 1.381 1.086 -0.129 0.127  -0.041 105 ALA BBB N   
797   C CA  . ALA A 105 ? 1.021 1.372 1.080 -0.125 0.131  -0.030 105 ALA BBB CA  
798   C C   . ALA A 105 ? 1.034 1.361 1.087 -0.120 0.135  -0.022 105 ALA BBB C   
799   O O   . ALA A 105 ? 1.049 1.371 1.100 -0.116 0.138  -0.013 105 ALA BBB O   
800   C CB  . ALA A 105 ? 1.075 1.432 1.139 -0.135 0.136  -0.027 105 ALA BBB CB  
801   N N   . GLY A 106 ? 1.048 1.360 1.098 -0.119 0.135  -0.027 106 GLY BBB N   
802   C CA  . GLY A 106 ? 1.074 1.364 1.118 -0.112 0.139  -0.021 106 GLY BBB CA  
803   C C   . GLY A 106 ? 1.126 1.395 1.167 -0.118 0.147  -0.015 106 GLY BBB C   
804   O O   . GLY A 106 ? 1.278 1.530 1.314 -0.110 0.150  -0.008 106 GLY BBB O   
805   N N   . THR A 107 ? 1.152 1.420 1.197 -0.130 0.150  -0.018 107 THR BBB N   
806   C CA  . THR A 107 ? 1.209 1.455 1.252 -0.137 0.158  -0.011 107 THR BBB CA  
807   C C   . THR A 107 ? 1.244 1.464 1.284 -0.141 0.161  -0.019 107 THR BBB C   
808   O O   . THR A 107 ? 1.272 1.465 1.306 -0.139 0.167  -0.012 107 THR BBB O   
809   C CB  . THR A 107 ? 1.271 1.531 1.321 -0.149 0.161  -0.010 107 THR BBB CB  
810   O OG1 . THR A 107 ? 1.539 1.813 1.596 -0.160 0.158  -0.023 107 THR BBB OG1 
811   C CG2 . THR A 107 ? 1.212 1.495 1.262 -0.143 0.159  -0.002 107 THR BBB CG2 
812   N N   . THR A 108 ? 1.244 1.471 1.287 -0.147 0.157  -0.033 108 THR BBB N   
813   C CA  . THR A 108 ? 1.320 1.525 1.360 -0.151 0.158  -0.043 108 THR BBB CA  
814   C C   . THR A 108 ? 1.326 1.535 1.361 -0.141 0.153  -0.052 108 THR BBB C   
815   O O   . THR A 108 ? 1.426 1.621 1.458 -0.143 0.153  -0.063 108 THR BBB O   
816   C CB  . THR A 108 ? 1.371 1.582 1.420 -0.169 0.158  -0.054 108 THR BBB CB  
817   O OG1 . THR A 108 ? 1.645 1.838 1.690 -0.172 0.157  -0.068 108 THR BBB OG1 
818   C CG2 . THR A 108 ? 1.279 1.526 1.335 -0.171 0.151  -0.061 108 THR BBB CG2 
819   N N   . SER A 109 ? 1.219 1.445 1.253 -0.129 0.149  -0.047 109 SER BBB N   
820   C CA  . SER A 109 ? 1.190 1.421 1.219 -0.119 0.145  -0.053 109 SER BBB CA  
821   C C   . SER A 109 ? 1.193 1.414 1.217 -0.105 0.147  -0.043 109 SER BBB C   
822   O O   . SER A 109 ? 1.228 1.448 1.252 -0.101 0.149  -0.031 109 SER BBB O   
823   C CB  . SER A 109 ? 1.156 1.417 1.189 -0.117 0.138  -0.055 109 SER BBB CB  
824   O OG  . SER A 109 ? 1.104 1.376 1.141 -0.112 0.137  -0.044 109 SER BBB OG  
825   N N   . THR A 110 ? 1.269 1.484 1.286 -0.096 0.147  -0.048 110 THR BBB N   
826   C CA  . THR A 110 ? 1.213 1.423 1.226 -0.082 0.149  -0.039 110 THR BBB CA  
827   C C   . THR A 110 ? 1.150 1.386 1.167 -0.075 0.144  -0.035 110 THR BBB C   
828   O O   . THR A 110 ? 1.153 1.407 1.173 -0.079 0.139  -0.041 110 THR BBB O   
829   C CB  . THR A 110 ? 1.297 1.490 1.301 -0.075 0.151  -0.047 110 THR BBB CB  
830   O OG1 . THR A 110 ? 1.292 1.499 1.294 -0.074 0.147  -0.057 110 THR BBB OG1 
831   C CG2 . THR A 110 ? 1.414 1.578 1.415 -0.083 0.155  -0.053 110 THR BBB CG2 
832   N N   . LEU A 111 ? 1.115 1.352 1.131 -0.065 0.145  -0.025 111 LEU BBB N   
833   C CA  . LEU A 111 ? 1.075 1.334 1.095 -0.059 0.141  -0.020 111 LEU BBB CA  
834   C C   . LEU A 111 ? 1.121 1.389 1.138 -0.056 0.139  -0.028 111 LEU BBB C   
835   O O   . LEU A 111 ? 1.121 1.406 1.141 -0.058 0.134  -0.028 111 LEU BBB O   
836   C CB  . LEU A 111 ? 1.065 1.324 1.086 -0.049 0.142  -0.009 111 LEU BBB CB  
837   C CG  . LEU A 111 ? 1.032 1.313 1.060 -0.043 0.139  -0.004 111 LEU BBB CG  
838   C CD1 . LEU A 111 ? 0.993 1.288 1.028 -0.050 0.133  -0.003 111 LEU BBB CD1 
839   C CD2 . LEU A 111 ? 1.139 1.422 1.169 -0.034 0.140  0.006  111 LEU BBB CD2 
840   N N   . GLN A 112 ? 1.168 1.422 1.177 -0.052 0.142  -0.035 112 GLN BBB N   
841   C CA  . GLN A 112 ? 1.214 1.479 1.219 -0.048 0.141  -0.042 112 GLN BBB CA  
842   C C   . GLN A 112 ? 1.223 1.497 1.228 -0.057 0.136  -0.052 112 GLN BBB C   
843   O O   . GLN A 112 ? 1.247 1.540 1.252 -0.054 0.132  -0.053 112 GLN BBB O   
844   C CB  . GLN A 112 ? 1.353 1.601 1.348 -0.041 0.145  -0.050 112 GLN BBB CB  
845   C CG  . GLN A 112 ? 1.620 1.882 1.608 -0.032 0.145  -0.055 112 GLN BBB CG  
846   C CD  . GLN A 112 ? 1.808 2.054 1.785 -0.029 0.147  -0.069 112 GLN BBB CD  
847   O OE1 . GLN A 112 ? 1.814 2.048 1.790 -0.039 0.145  -0.080 112 GLN BBB OE1 
848   N NE2 . GLN A 112 ? 1.921 2.169 1.891 -0.016 0.150  -0.069 112 GLN BBB NE2 
849   N N   . GLU A 113 ? 1.251 1.515 1.258 -0.068 0.136  -0.059 113 GLU BBB N   
850   C CA  . GLU A 113 ? 1.206 1.483 1.215 -0.077 0.131  -0.068 113 GLU BBB CA  
851   C C   . GLU A 113 ? 1.178 1.476 1.195 -0.078 0.127  -0.060 113 GLU BBB C   
852   O O   . GLU A 113 ? 1.148 1.463 1.165 -0.078 0.122  -0.065 113 GLU BBB O   
853   C CB  . GLU A 113 ? 1.192 1.455 1.204 -0.090 0.133  -0.074 113 GLU BBB CB  
854   C CG  . GLU A 113 ? 1.248 1.488 1.253 -0.091 0.136  -0.085 113 GLU BBB CG  
855   C CD  . GLU A 113 ? 1.324 1.546 1.333 -0.105 0.139  -0.090 113 GLU BBB CD  
856   O OE1 . GLU A 113 ? 1.331 1.550 1.346 -0.109 0.141  -0.079 113 GLU BBB OE1 
857   O OE2 . GLU A 113 ? 1.490 1.704 1.497 -0.112 0.138  -0.104 113 GLU BBB OE2 
858   N N   . GLN A 114 ? 1.119 1.415 1.142 -0.078 0.128  -0.049 114 GLN BBB N   
859   C CA  . GLN A 114 ? 1.049 1.361 1.078 -0.078 0.123  -0.043 114 GLN BBB CA  
860   C C   . GLN A 114 ? 1.074 1.399 1.102 -0.069 0.120  -0.039 114 GLN BBB C   
861   O O   . GLN A 114 ? 1.131 1.471 1.162 -0.069 0.115  -0.039 114 GLN BBB O   
862   C CB  . GLN A 114 ? 1.028 1.334 1.061 -0.077 0.125  -0.033 114 GLN BBB CB  
863   C CG  . GLN A 114 ? 1.085 1.383 1.120 -0.086 0.128  -0.035 114 GLN BBB CG  
864   C CD  . GLN A 114 ? 1.043 1.333 1.079 -0.084 0.131  -0.024 114 GLN BBB CD  
865   O OE1 . GLN A 114 ? 1.070 1.366 1.108 -0.077 0.129  -0.017 114 GLN BBB OE1 
866   N NE2 . GLN A 114 ? 1.056 1.331 1.090 -0.090 0.136  -0.024 114 GLN BBB NE2 
867   N N   . ILE A 115 ? 1.113 1.432 1.138 -0.061 0.124  -0.033 115 ILE BBB N   
868   C CA  . ILE A 115 ? 1.109 1.441 1.133 -0.053 0.122  -0.028 115 ILE BBB CA  
869   C C   . ILE A 115 ? 1.143 1.484 1.161 -0.052 0.120  -0.036 115 ILE BBB C   
870   O O   . ILE A 115 ? 1.156 1.512 1.176 -0.050 0.117  -0.033 115 ILE BBB O   
871   C CB  . ILE A 115 ? 1.071 1.398 1.094 -0.045 0.127  -0.021 115 ILE BBB CB  
872   C CG1 . ILE A 115 ? 1.034 1.357 1.065 -0.045 0.128  -0.012 115 ILE BBB CG1 
873   C CG2 . ILE A 115 ? 1.117 1.458 1.139 -0.038 0.127  -0.016 115 ILE BBB CG2 
874   C CD1 . ILE A 115 ? 1.029 1.346 1.058 -0.037 0.133  -0.006 115 ILE BBB CD1 
875   N N   . GLY A 116 ? 1.210 1.544 1.221 -0.054 0.122  -0.048 116 GLY BBB N   
876   C CA  . GLY A 116 ? 1.263 1.608 1.268 -0.053 0.120  -0.057 116 GLY BBB CA  
877   C C   . GLY A 116 ? 1.225 1.584 1.233 -0.058 0.113  -0.060 116 GLY BBB C   
878   O O   . GLY A 116 ? 1.228 1.602 1.233 -0.052 0.110  -0.059 116 GLY BBB O   
879   N N   . TRP A 117 ? 1.113 1.470 1.129 -0.067 0.112  -0.062 117 TRP BBB N   
880   C CA  . TRP A 117 ? 1.042 1.415 1.062 -0.070 0.106  -0.065 117 TRP BBB CA  
881   C C   . TRP A 117 ? 1.025 1.406 1.048 -0.064 0.103  -0.053 117 TRP BBB C   
882   O O   . TRP A 117 ? 1.096 1.491 1.117 -0.060 0.099  -0.054 117 TRP BBB O   
883   C CB  . TRP A 117 ? 1.038 1.407 1.065 -0.081 0.106  -0.069 117 TRP BBB CB  
884   C CG  . TRP A 117 ? 1.081 1.442 1.105 -0.089 0.108  -0.081 117 TRP BBB CG  
885   C CD1 . TRP A 117 ? 1.236 1.603 1.255 -0.090 0.106  -0.093 117 TRP BBB CD1 
886   C CD2 . TRP A 117 ? 1.149 1.494 1.177 -0.098 0.113  -0.082 117 TRP BBB CD2 
887   N NE1 . TRP A 117 ? 1.338 1.693 1.359 -0.100 0.109  -0.103 117 TRP BBB NE1 
888   C CE2 . TRP A 117 ? 1.206 1.546 1.231 -0.105 0.113  -0.095 117 TRP BBB CE2 
889   C CE3 . TRP A 117 ? 1.197 1.531 1.230 -0.101 0.116  -0.073 117 TRP BBB CE3 
890   C CZ2 . TRP A 117 ? 1.211 1.534 1.240 -0.116 0.118  -0.099 117 TRP BBB CZ2 
891   C CZ3 . TRP A 117 ? 1.197 1.515 1.231 -0.110 0.121  -0.075 117 TRP BBB CZ3 
892   C CH2 . TRP A 117 ? 1.189 1.500 1.222 -0.118 0.122  -0.087 117 TRP BBB CH2 
893   N N   . MET A 118 ? 1.001 1.373 1.029 -0.063 0.105  -0.043 118 MET BBB N   
894   C CA  . MET A 118 ? 1.002 1.381 1.036 -0.059 0.101  -0.033 118 MET BBB CA  
895   C C   . MET A 118 ? 1.183 1.568 1.213 -0.051 0.101  -0.027 118 MET BBB C   
896   O O   . MET A 118 ? 1.311 1.703 1.343 -0.048 0.097  -0.021 118 MET BBB O   
897   C CB  . MET A 118 ? 1.022 1.391 1.062 -0.060 0.103  -0.025 118 MET BBB CB  
898   C CG  . MET A 118 ? 1.042 1.408 1.086 -0.067 0.102  -0.030 118 MET BBB CG  
899   S SD  . MET A 118 ? 0.956 1.311 1.004 -0.067 0.105  -0.021 118 MET BBB SD  
900   C CE  . MET A 118 ? 0.983 1.346 1.039 -0.063 0.099  -0.013 118 MET BBB CE  
901   N N   . THR A 119 ? 1.193 1.576 1.216 -0.047 0.106  -0.027 119 THR BBB N   
902   C CA  . THR A 119 ? 1.159 1.550 1.178 -0.039 0.107  -0.020 119 THR BBB CA  
903   C C   . THR A 119 ? 1.288 1.690 1.296 -0.035 0.106  -0.027 119 THR BBB C   
904   O O   . THR A 119 ? 1.441 1.851 1.443 -0.028 0.108  -0.022 119 THR BBB O   
905   C CB  . THR A 119 ? 1.120 1.506 1.139 -0.035 0.114  -0.014 119 THR BBB CB  
906   O OG1 . THR A 119 ? 1.186 1.564 1.197 -0.035 0.117  -0.024 119 THR BBB OG1 
907   C CG2 . THR A 119 ? 1.197 1.575 1.226 -0.039 0.114  -0.006 119 THR BBB CG2 
908   N N   . HIS A 120 ? 1.372 1.777 1.378 -0.040 0.103  -0.040 120 HIS BBB N   
909   C CA  . HIS A 120 ? 1.439 1.857 1.435 -0.036 0.101  -0.049 120 HIS BBB CA  
910   C C   . HIS A 120 ? 1.550 1.982 1.545 -0.029 0.096  -0.042 120 HIS BBB C   
911   O O   . HIS A 120 ? 1.569 1.999 1.572 -0.030 0.094  -0.032 120 HIS BBB O   
912   C CB  . HIS A 120 ? 1.519 1.938 1.516 -0.044 0.098  -0.065 120 HIS BBB CB  
913   C CG  . HIS A 120 ? 1.669 2.100 1.655 -0.041 0.096  -0.078 120 HIS BBB CG  
914   N ND1 . HIS A 120 ? 1.769 2.219 1.754 -0.039 0.090  -0.084 120 HIS BBB ND1 
915   C CD2 . HIS A 120 ? 1.770 2.198 1.747 -0.038 0.099  -0.086 120 HIS BBB CD2 
916   C CE1 . HIS A 120 ? 1.912 2.371 1.887 -0.036 0.088  -0.095 120 HIS BBB CE1 
917   N NE2 . HIS A 120 ? 1.945 2.391 1.915 -0.035 0.094  -0.098 120 HIS BBB NE2 
918   N N   . ASN A 121 ? 1.692 2.138 1.676 -0.023 0.095  -0.046 121 ASN BBB N   
919   C CA  . ASN A 121 ? 1.765 2.225 1.746 -0.016 0.090  -0.040 121 ASN BBB CA  
920   C C   . ASN A 121 ? 1.882 2.359 1.857 -0.015 0.085  -0.055 121 ASN BBB C   
921   O O   . ASN A 121 ? 1.926 2.412 1.890 -0.011 0.085  -0.063 121 ASN BBB O   
922   C CB  . ASN A 121 ? 1.781 2.248 1.754 -0.005 0.094  -0.027 121 ASN BBB CB  
923   C CG  . ASN A 121 ? 1.741 2.218 1.711 0.002  0.090  -0.017 121 ASN BBB CG  
924   O OD1 . ASN A 121 ? 1.689 2.162 1.667 -0.000 0.085  -0.013 121 ASN BBB OD1 
925   N ND2 . ASN A 121 ? 1.820 2.311 1.778 0.012  0.091  -0.012 121 ASN BBB ND2 
926   N N   . PRO A 122 ? 1.998 2.480 1.979 -0.019 0.079  -0.059 122 PRO BBB N   
927   C CA  . PRO A 122 ? 1.900 2.372 1.892 -0.023 0.077  -0.051 122 PRO BBB CA  
928   C C   . PRO A 122 ? 1.844 2.301 1.846 -0.034 0.081  -0.054 122 PRO BBB C   
929   O O   . PRO A 122 ? 1.904 2.359 1.906 -0.040 0.083  -0.066 122 PRO BBB O   
930   C CB  . PRO A 122 ? 2.013 2.502 2.007 -0.022 0.070  -0.059 122 PRO BBB CB  
931   C CG  . PRO A 122 ? 2.062 2.570 2.045 -0.015 0.068  -0.067 122 PRO BBB CG  
932   C CD  . PRO A 122 ? 2.059 2.560 2.036 -0.018 0.073  -0.073 122 PRO BBB CD  
933   N N   . PRO A 123 ? 1.629 2.074 1.638 -0.035 0.081  -0.044 123 PRO BBB N   
934   C CA  . PRO A 123 ? 1.429 1.860 1.446 -0.044 0.085  -0.045 123 PRO BBB CA  
935   C C   . PRO A 123 ? 1.368 1.803 1.391 -0.051 0.082  -0.056 123 PRO BBB C   
936   O O   . PRO A 123 ? 1.443 1.890 1.468 -0.050 0.077  -0.058 123 PRO BBB O   
937   C CB  . PRO A 123 ? 1.336 1.757 1.360 -0.042 0.085  -0.032 123 PRO BBB CB  
938   C CG  . PRO A 123 ? 1.425 1.855 1.447 -0.035 0.079  -0.027 123 PRO BBB CG  
939   C CD  . PRO A 123 ? 1.608 2.051 1.620 -0.029 0.079  -0.031 123 PRO BBB CD  
940   N N   . ILE A 124 ? 1.215 1.641 1.240 -0.060 0.086  -0.062 124 ILE BBB N   
941   C CA  . ILE A 124 ? 1.197 1.625 1.228 -0.069 0.086  -0.069 124 ILE BBB CA  
942   C C   . ILE A 124 ? 1.155 1.570 1.193 -0.071 0.088  -0.060 124 ILE BBB C   
943   O O   . ILE A 124 ? 1.217 1.618 1.254 -0.074 0.094  -0.058 124 ILE BBB O   
944   C CB  . ILE A 124 ? 1.175 1.602 1.205 -0.077 0.089  -0.081 124 ILE BBB CB  
945   C CG1 . ILE A 124 ? 1.257 1.698 1.280 -0.074 0.085  -0.090 124 ILE BBB CG1 
946   C CG2 . ILE A 124 ? 1.142 1.572 1.180 -0.088 0.089  -0.087 124 ILE BBB CG2 
947   C CD1 . ILE A 124 ? 1.353 1.788 1.373 -0.080 0.088  -0.102 124 ILE BBB CD1 
948   N N   . PRO A 125 ? 1.071 1.491 1.114 -0.069 0.085  -0.056 125 PRO BBB N   
949   C CA  . PRO A 125 ? 1.027 1.436 1.075 -0.069 0.086  -0.047 125 PRO BBB CA  
950   C C   . PRO A 125 ? 1.010 1.415 1.061 -0.076 0.089  -0.050 125 PRO BBB C   
951   O O   . PRO A 125 ? 1.085 1.497 1.141 -0.077 0.086  -0.050 125 PRO BBB O   
952   C CB  . PRO A 125 ? 1.069 1.486 1.120 -0.062 0.079  -0.044 125 PRO BBB CB  
953   C CG  . PRO A 125 ? 1.028 1.461 1.077 -0.062 0.076  -0.053 125 PRO BBB CG  
954   C CD  . PRO A 125 ? 1.051 1.489 1.096 -0.066 0.078  -0.060 125 PRO BBB CD  
955   N N   . VAL A 126 ? 0.965 1.360 1.015 -0.082 0.095  -0.051 126 VAL BBB N   
956   C CA  . VAL A 126 ? 0.961 1.351 1.014 -0.089 0.099  -0.052 126 VAL BBB CA  
957   C C   . VAL A 126 ? 0.975 1.361 1.031 -0.087 0.098  -0.044 126 VAL BBB C   
958   O O   . VAL A 126 ? 1.071 1.462 1.130 -0.090 0.100  -0.044 126 VAL BBB O   
959   C CB  . VAL A 126 ? 0.959 1.334 1.009 -0.095 0.105  -0.054 126 VAL BBB CB  
960   C CG1 . VAL A 126 ? 0.985 1.366 1.032 -0.099 0.104  -0.066 126 VAL BBB CG1 
961   C CG2 . VAL A 126 ? 0.947 1.308 0.992 -0.088 0.107  -0.047 126 VAL BBB CG2 
962   N N   . GLY A 127 ? 0.937 1.316 0.992 -0.080 0.097  -0.036 127 GLY BBB N   
963   C CA  . GLY A 127 ? 0.992 1.370 1.052 -0.077 0.096  -0.030 127 GLY BBB CA  
964   C C   . GLY A 127 ? 0.990 1.380 1.053 -0.075 0.089  -0.032 127 GLY BBB C   
965   O O   . GLY A 127 ? 0.984 1.377 1.049 -0.075 0.089  -0.032 127 GLY BBB O   
966   N N   . GLU A 128 ? 0.919 1.317 0.982 -0.071 0.084  -0.035 128 GLU BBB N   
967   C CA  . GLU A 128 ? 0.915 1.322 0.980 -0.067 0.078  -0.038 128 GLU BBB CA  
968   C C   . GLU A 128 ? 0.953 1.374 1.019 -0.071 0.079  -0.045 128 GLU BBB C   
969   O O   . GLU A 128 ? 1.005 1.435 1.074 -0.069 0.076  -0.047 128 GLU BBB O   
970   C CB  . GLU A 128 ? 0.992 1.403 1.057 -0.061 0.073  -0.038 128 GLU BBB CB  
971   C CG  . GLU A 128 ? 1.183 1.582 1.248 -0.057 0.072  -0.030 128 GLU BBB CG  
972   C CD  . GLU A 128 ? 1.276 1.669 1.347 -0.056 0.069  -0.025 128 GLU BBB CD  
973   O OE1 . GLU A 128 ? 1.213 1.611 1.285 -0.055 0.066  -0.030 128 GLU BBB OE1 
974   O OE2 . GLU A 128 ? 1.539 1.923 1.612 -0.056 0.070  -0.018 128 GLU BBB OE2 
975   N N   . ILE A 129 ? 0.996 1.421 1.061 -0.077 0.083  -0.050 129 ILE BBB N   
976   C CA  . ILE A 129 ? 0.971 1.412 1.039 -0.083 0.085  -0.056 129 ILE BBB CA  
977   C C   . ILE A 129 ? 0.981 1.418 1.050 -0.088 0.090  -0.052 129 ILE BBB C   
978   O O   . ILE A 129 ? 1.040 1.492 1.112 -0.088 0.089  -0.054 129 ILE BBB O   
979   C CB  . ILE A 129 ? 0.954 1.399 1.022 -0.091 0.087  -0.063 129 ILE BBB CB  
980   C CG1 . ILE A 129 ? 0.956 1.408 1.021 -0.084 0.082  -0.067 129 ILE BBB CG1 
981   C CG2 . ILE A 129 ? 1.073 1.534 1.145 -0.099 0.090  -0.069 129 ILE BBB CG2 
982   C CD1 . ILE A 129 ? 0.977 1.430 1.039 -0.089 0.084  -0.073 129 ILE BBB CD1 
983   N N   . TYR A 130 ? 0.950 1.370 1.017 -0.091 0.095  -0.047 130 TYR BBB N   
984   C CA  . TYR A 130 ? 0.934 1.350 1.001 -0.094 0.100  -0.041 130 TYR BBB CA  
985   C C   . TYR A 130 ? 0.956 1.378 1.023 -0.086 0.096  -0.038 130 TYR BBB C   
986   O O   . TYR A 130 ? 0.998 1.428 1.065 -0.087 0.097  -0.037 130 TYR BBB O   
987   C CB  . TYR A 130 ? 0.927 1.321 0.990 -0.096 0.105  -0.035 130 TYR BBB CB  
988   C CG  . TYR A 130 ? 0.938 1.326 1.000 -0.099 0.112  -0.029 130 TYR BBB CG  
989   C CD1 . TYR A 130 ? 0.951 1.351 1.015 -0.105 0.115  -0.030 130 TYR BBB CD1 
990   C CD2 . TYR A 130 ? 0.941 1.312 0.999 -0.096 0.115  -0.021 130 TYR BBB CD2 
991   C CE1 . TYR A 130 ? 0.964 1.358 1.026 -0.109 0.121  -0.022 130 TYR BBB CE1 
992   C CE2 . TYR A 130 ? 0.957 1.322 1.012 -0.098 0.121  -0.014 130 TYR BBB CE2 
993   C CZ  . TYR A 130 ? 0.966 1.342 1.024 -0.104 0.124  -0.014 130 TYR BBB CZ  
994   O OH  . TYR A 130 ? 1.017 1.386 1.071 -0.106 0.131  -0.005 130 TYR BBB OH  
995   N N   . LYS A 131 ? 0.927 1.344 0.994 -0.079 0.090  -0.037 131 LYS BBB N   
996   C CA  . LYS A 131 ? 0.936 1.356 1.004 -0.072 0.084  -0.035 131 LYS BBB CA  
997   C C   . LYS A 131 ? 0.942 1.380 1.011 -0.069 0.080  -0.042 131 LYS BBB C   
998   O O   . LYS A 131 ? 0.950 1.396 1.018 -0.065 0.079  -0.043 131 LYS BBB O   
999   C CB  . LYS A 131 ? 0.945 1.356 1.015 -0.066 0.079  -0.033 131 LYS BBB CB  
1000  C CG  . LYS A 131 ? 0.994 1.405 1.066 -0.060 0.073  -0.032 131 LYS BBB CG  
1001  C CD  . LYS A 131 ? 0.967 1.369 1.042 -0.056 0.067  -0.030 131 LYS BBB CD  
1002  C CE  . LYS A 131 ? 1.150 1.555 1.226 -0.052 0.061  -0.035 131 LYS BBB CE  
1003  N NZ  . LYS A 131 ? 1.153 1.547 1.232 -0.051 0.057  -0.030 131 LYS BBB NZ  
1004  N N   . ARG A 132 ? 1.056 1.503 1.126 -0.069 0.079  -0.048 132 ARG BBB N   
1005  C CA  . ARG A 132 ? 1.080 1.547 1.152 -0.066 0.076  -0.055 132 ARG BBB CA  
1006  C C   . ARG A 132 ? 1.070 1.551 1.143 -0.072 0.082  -0.055 132 ARG BBB C   
1007  O O   . ARG A 132 ? 1.103 1.598 1.176 -0.067 0.080  -0.057 132 ARG BBB O   
1008  C CB  . ARG A 132 ? 1.189 1.667 1.263 -0.068 0.074  -0.061 132 ARG BBB CB  
1009  C CG  . ARG A 132 ? 1.341 1.841 1.416 -0.063 0.071  -0.068 132 ARG BBB CG  
1010  C CD  . ARG A 132 ? 1.479 1.995 1.557 -0.066 0.071  -0.074 132 ARG BBB CD  
1011  N NE  . ARG A 132 ? 1.763 2.268 1.839 -0.064 0.068  -0.074 132 ARG BBB NE  
1012  C CZ  . ARG A 132 ? 1.764 2.276 1.841 -0.070 0.069  -0.078 132 ARG BBB CZ  
1013  N NH1 . ARG A 132 ? 1.724 2.253 1.806 -0.079 0.074  -0.083 132 ARG BBB NH1 
1014  N NH2 . ARG A 132 ? 1.691 2.194 1.763 -0.067 0.067  -0.076 132 ARG BBB NH2 
1015  N N   . TRP A 133 ? 0.941 1.417 1.014 -0.082 0.090  -0.052 133 TRP BBB N   
1016  C CA  . TRP A 133 ? 0.953 1.440 1.028 -0.089 0.097  -0.049 133 TRP BBB CA  
1017  C C   . TRP A 133 ? 0.945 1.428 1.015 -0.085 0.098  -0.043 133 TRP BBB C   
1018  O O   . TRP A 133 ? 0.993 1.493 1.063 -0.083 0.100  -0.042 133 TRP BBB O   
1019  C CB  . TRP A 133 ? 0.965 1.442 1.041 -0.102 0.104  -0.047 133 TRP BBB CB  
1020  C CG  . TRP A 133 ? 0.988 1.469 1.067 -0.107 0.103  -0.055 133 TRP BBB CG  
1021  C CD1 . TRP A 133 ? 1.074 1.572 1.156 -0.102 0.096  -0.063 133 TRP BBB CD1 
1022  C CD2 . TRP A 133 ? 1.024 1.493 1.105 -0.118 0.107  -0.056 133 TRP BBB CD2 
1023  N NE1 . TRP A 133 ? 1.109 1.609 1.194 -0.109 0.096  -0.069 133 TRP BBB NE1 
1024  C CE2 . TRP A 133 ? 1.075 1.556 1.158 -0.119 0.103  -0.065 133 TRP BBB CE2 
1025  C CE3 . TRP A 133 ? 1.046 1.494 1.124 -0.125 0.115  -0.050 133 TRP BBB CE3 
1026  C CZ2 . TRP A 133 ? 1.118 1.593 1.203 -0.128 0.105  -0.070 133 TRP BBB CZ2 
1027  C CZ3 . TRP A 133 ? 1.039 1.478 1.119 -0.134 0.117  -0.056 133 TRP BBB CZ3 
1028  C CH2 . TRP A 133 ? 1.057 1.510 1.140 -0.136 0.112  -0.066 133 TRP BBB CH2 
1029  N N   . ILE A 134 ? 0.911 1.375 0.979 -0.082 0.097  -0.037 134 ILE BBB N   
1030  C CA  . ILE A 134 ? 0.902 1.363 0.966 -0.077 0.098  -0.031 134 ILE BBB CA  
1031  C C   . ILE A 134 ? 0.897 1.372 0.959 -0.066 0.090  -0.037 134 ILE BBB C   
1032  O O   . ILE A 134 ? 0.901 1.389 0.960 -0.063 0.092  -0.035 134 ILE BBB O   
1033  C CB  . ILE A 134 ? 0.892 1.331 0.953 -0.075 0.098  -0.025 134 ILE BBB CB  
1034  C CG1 . ILE A 134 ? 0.895 1.320 0.955 -0.084 0.106  -0.020 134 ILE BBB CG1 
1035  C CG2 . ILE A 134 ? 0.897 1.337 0.955 -0.068 0.096  -0.020 134 ILE BBB CG2 
1036  C CD1 . ILE A 134 ? 0.885 1.291 0.944 -0.082 0.107  -0.015 134 ILE BBB CD1 
1037  N N   . ILE A 135 ? 0.904 1.378 0.969 -0.061 0.082  -0.043 135 ILE BBB N   
1038  C CA  . ILE A 135 ? 0.902 1.386 0.966 -0.050 0.074  -0.049 135 ILE BBB CA  
1039  C C   . ILE A 135 ? 0.953 1.461 1.016 -0.049 0.076  -0.055 135 ILE BBB C   
1040  O O   . ILE A 135 ? 1.051 1.573 1.112 -0.041 0.073  -0.058 135 ILE BBB O   
1041  C CB  . ILE A 135 ? 0.888 1.362 0.955 -0.045 0.066  -0.054 135 ILE BBB CB  
1042  C CG1 . ILE A 135 ? 0.883 1.337 0.951 -0.046 0.063  -0.048 135 ILE BBB CG1 
1043  C CG2 . ILE A 135 ? 0.887 1.371 0.953 -0.035 0.057  -0.063 135 ILE BBB CG2 
1044  C CD1 . ILE A 135 ? 0.939 1.381 1.011 -0.044 0.058  -0.049 135 ILE BBB CD1 
1045  N N   . LEU A 136 ? 0.983 1.501 1.051 -0.055 0.080  -0.057 136 LEU BBB N   
1046  C CA  . LEU A 136 ? 1.020 1.565 1.089 -0.055 0.083  -0.061 136 LEU BBB CA  
1047  C C   . LEU A 136 ? 0.994 1.548 1.060 -0.058 0.090  -0.054 136 LEU BBB C   
1048  O O   . LEU A 136 ? 1.035 1.611 1.099 -0.051 0.090  -0.057 136 LEU BBB O   
1049  C CB  . LEU A 136 ? 1.027 1.581 1.102 -0.065 0.086  -0.063 136 LEU BBB CB  
1050  C CG  . LEU A 136 ? 1.171 1.755 1.249 -0.068 0.091  -0.065 136 LEU BBB CG  
1051  C CD1 . LEU A 136 ? 1.165 1.771 1.241 -0.053 0.085  -0.073 136 LEU BBB CD1 
1052  C CD2 . LEU A 136 ? 1.193 1.786 1.279 -0.078 0.094  -0.069 136 LEU BBB CD2 
1053  N N   . GLY A 137 ? 0.961 1.499 1.025 -0.067 0.097  -0.044 137 GLY BBB N   
1054  C CA  . GLY A 137 ? 1.002 1.546 1.062 -0.069 0.105  -0.036 137 GLY BBB CA  
1055  C C   . GLY A 137 ? 1.032 1.578 1.085 -0.056 0.100  -0.036 137 GLY BBB C   
1056  O O   . GLY A 137 ? 1.066 1.630 1.114 -0.053 0.103  -0.033 137 GLY BBB O   
1057  N N   . LEU A 138 ? 1.048 1.576 1.100 -0.051 0.092  -0.038 138 LEU BBB N   
1058  C CA  . LEU A 138 ? 0.973 1.504 1.020 -0.040 0.086  -0.039 138 LEU BBB CA  
1059  C C   . LEU A 138 ? 0.974 1.525 1.018 -0.029 0.079  -0.050 138 LEU BBB C   
1060  O O   . LEU A 138 ? 1.069 1.633 1.107 -0.021 0.078  -0.051 138 LEU BBB O   
1061  C CB  . LEU A 138 ? 0.935 1.443 0.983 -0.037 0.078  -0.040 138 LEU BBB CB  
1062  C CG  . LEU A 138 ? 0.924 1.413 0.972 -0.045 0.084  -0.030 138 LEU BBB CG  
1063  C CD1 . LEU A 138 ? 0.896 1.367 0.948 -0.043 0.077  -0.031 138 LEU BBB CD1 
1064  C CD2 . LEU A 138 ? 0.943 1.436 0.984 -0.042 0.090  -0.021 138 LEU BBB CD2 
1065  N N   . ASN A 139 ? 0.965 1.520 1.014 -0.028 0.075  -0.058 139 ASN BBB N   
1066  C CA  . ASN A 139 ? 1.015 1.591 1.063 -0.017 0.070  -0.069 139 ASN BBB CA  
1067  C C   . ASN A 139 ? 1.115 1.719 1.159 -0.016 0.077  -0.066 139 ASN BBB C   
1068  O O   . ASN A 139 ? 1.244 1.864 1.282 -0.005 0.074  -0.072 139 ASN BBB O   
1069  C CB  . ASN A 139 ? 1.163 1.739 1.216 -0.016 0.065  -0.076 139 ASN BBB CB  
1070  C CG  . ASN A 139 ? 1.172 1.723 1.228 -0.014 0.056  -0.079 139 ASN BBB CG  
1071  O OD1 . ASN A 139 ? 1.226 1.773 1.280 -0.003 0.047  -0.087 139 ASN BBB OD1 
1072  N ND2 . ASN A 139 ? 1.211 1.745 1.271 -0.023 0.059  -0.073 139 ASN BBB ND2 
1073  N N   . LYS A 140 ? 1.107 1.718 1.155 -0.029 0.088  -0.058 140 LYS BBB N   
1074  C CA  . LYS A 140 ? 1.139 1.778 1.185 -0.029 0.097  -0.053 140 LYS BBB CA  
1075  C C   . LYS A 140 ? 1.178 1.818 1.214 -0.023 0.099  -0.047 140 LYS BBB C   
1076  O O   . LYS A 140 ? 1.423 2.089 1.453 -0.015 0.100  -0.048 140 LYS BBB O   
1077  C CB  . LYS A 140 ? 1.152 1.793 1.204 -0.046 0.108  -0.044 140 LYS BBB CB  
1078  C CG  . LYS A 140 ? 1.242 1.891 1.304 -0.052 0.107  -0.051 140 LYS BBB CG  
1079  C CD  . LYS A 140 ? 1.283 1.922 1.352 -0.070 0.116  -0.043 140 LYS BBB CD  
1080  C CE  . LYS A 140 ? 1.368 2.029 1.447 -0.078 0.119  -0.048 140 LYS BBB CE  
1081  N NZ  . LYS A 140 ? 1.339 2.002 1.421 -0.071 0.109  -0.060 140 LYS BBB NZ  
1082  N N   . ILE A 141 ? 1.117 1.732 1.151 -0.027 0.099  -0.039 141 ILE BBB N   
1083  C CA  . ILE A 141 ? 1.088 1.704 1.111 -0.021 0.100  -0.033 141 ILE BBB CA  
1084  C C   . ILE A 141 ? 1.145 1.771 1.162 -0.004 0.089  -0.044 141 ILE BBB C   
1085  O O   . ILE A 141 ? 1.321 1.968 1.330 0.004  0.091  -0.043 141 ILE BBB O   
1086  C CB  . ILE A 141 ? 1.112 1.699 1.135 -0.027 0.102  -0.023 141 ILE BBB CB  
1087  C CG1 . ILE A 141 ? 1.104 1.683 1.131 -0.042 0.114  -0.012 141 ILE BBB CG1 
1088  C CG2 . ILE A 141 ? 1.143 1.732 1.156 -0.018 0.101  -0.017 141 ILE BBB CG2 
1089  C CD1 . ILE A 141 ? 1.198 1.747 1.228 -0.048 0.114  -0.006 141 ILE BBB CD1 
1090  N N   . VAL A 142 ? 1.096 1.708 1.117 0.000  0.077  -0.056 142 VAL BBB N   
1091  C CA  . VAL A 142 ? 1.153 1.772 1.169 0.015  0.066  -0.068 142 VAL BBB CA  
1092  C C   . VAL A 142 ? 1.341 1.992 1.353 0.024  0.067  -0.075 142 VAL BBB C   
1093  O O   . VAL A 142 ? 1.452 2.118 1.454 0.037  0.063  -0.081 142 VAL BBB O   
1094  C CB  . VAL A 142 ? 1.005 1.602 1.028 0.017  0.054  -0.079 142 VAL BBB CB  
1095  C CG1 . VAL A 142 ? 0.978 1.548 1.006 0.008  0.054  -0.071 142 VAL BBB CG1 
1096  C CG2 . VAL A 142 ? 1.124 1.723 1.153 0.016  0.053  -0.085 142 VAL BBB CG2 
1097  N N   . ARG A 143 ? 1.300 1.963 1.317 0.020  0.072  -0.076 143 ARG BBB N   
1098  C CA  . ARG A 143 ? 1.337 2.034 1.351 0.029  0.074  -0.082 143 ARG BBB CA  
1099  C C   . ARG A 143 ? 1.374 2.093 1.379 0.030  0.085  -0.072 143 ARG BBB C   
1100  O O   . ARG A 143 ? 1.519 2.264 1.515 0.043  0.083  -0.078 143 ARG BBB O   
1101  C CB  . ARG A 143 ? 1.488 2.196 1.511 0.022  0.079  -0.083 143 ARG BBB CB  
1102  C CG  . ARG A 143 ? 1.724 2.405 1.754 0.018  0.072  -0.088 143 ARG BBB CG  
1103  C CD  . ARG A 143 ? 1.871 2.563 1.911 0.009  0.077  -0.087 143 ARG BBB CD  
1104  N NE  . ARG A 143 ? 2.034 2.758 2.075 0.018  0.077  -0.096 143 ARG BBB NE  
1105  C CZ  . ARG A 143 ? 2.185 2.924 2.235 0.012  0.080  -0.097 143 ARG BBB CZ  
1106  N NH1 . ARG A 143 ? 2.274 2.999 2.332 -0.003 0.084  -0.090 143 ARG BBB NH1 
1107  N NH2 . ARG A 143 ? 2.248 3.020 2.299 0.023  0.079  -0.105 143 ARG BBB NH2 
1108  N N   . MET A 144 ? 1.368 2.080 1.375 0.016  0.096  -0.055 144 MET BBB N   
1109  C CA  . MET A 144 ? 1.395 2.127 1.394 0.015  0.107  -0.042 144 MET BBB CA  
1110  C C   . MET A 144 ? 1.426 2.159 1.413 0.028  0.101  -0.044 144 MET BBB C   
1111  O O   . MET A 144 ? 1.660 2.421 1.636 0.038  0.105  -0.041 144 MET BBB O   
1112  C CB  . MET A 144 ? 1.400 2.116 1.404 -0.003 0.119  -0.025 144 MET BBB CB  
1113  C CG  . MET A 144 ? 1.454 2.165 1.472 -0.017 0.123  -0.025 144 MET BBB CG  
1114  S SD  . MET A 144 ? 1.793 2.536 1.818 -0.011 0.119  -0.040 144 MET BBB SD  
1115  C CE  . MET A 144 ? 1.573 2.310 1.613 -0.031 0.125  -0.037 144 MET BBB CE  
1116  N N   . TYR A 145 ? 1.320 2.025 1.307 0.030  0.091  -0.048 145 TYR BBB N   
1117  C CA  . TYR A 145 ? 1.350 2.055 1.326 0.041  0.085  -0.050 145 TYR BBB CA  
1118  C C   . TYR A 145 ? 1.381 2.096 1.353 0.057  0.071  -0.069 145 TYR BBB C   
1119  O O   . TYR A 145 ? 1.470 2.185 1.434 0.067  0.063  -0.074 145 TYR BBB O   
1120  C CB  . TYR A 145 ? 1.331 2.005 1.311 0.034  0.082  -0.044 145 TYR BBB CB  
1121  C CG  . TYR A 145 ? 1.375 2.038 1.355 0.023  0.094  -0.024 145 TYR BBB CG  
1122  C CD1 . TYR A 145 ? 1.322 1.989 1.307 0.011  0.107  -0.014 145 TYR BBB CD1 
1123  C CD2 . TYR A 145 ? 1.446 2.095 1.422 0.024  0.093  -0.016 145 TYR BBB CD2 
1124  C CE1 . TYR A 145 ? 1.343 1.996 1.328 0.000  0.118  0.004  145 TYR BBB CE1 
1125  C CE2 . TYR A 145 ? 1.454 2.091 1.429 0.016  0.104  0.002  145 TYR BBB CE2 
1126  C CZ  . TYR A 145 ? 1.420 2.056 1.398 0.004  0.117  0.012  145 TYR BBB CZ  
1127  O OH  . TYR A 145 ? 1.340 1.961 1.317 -0.005 0.127  0.029  145 TYR BBB OH  
1128  N N   . SER A 146 ? 1.232 1.784 1.676 0.083  0.248  -0.139 146 SER BBB N   
1129  C CA  . SER A 146 ? 1.264 1.826 1.664 0.100  0.223  -0.130 146 SER BBB CA  
1130  C C   . SER A 146 ? 1.363 1.913 1.742 0.119  0.222  -0.104 146 SER BBB C   
1131  O O   . SER A 146 ? 1.506 2.057 1.888 0.114  0.240  -0.098 146 SER BBB O   
1132  C CB  . SER A 146 ? 1.301 1.891 1.678 0.091  0.219  -0.146 146 SER BBB CB  
1133  O OG  . SER A 146 ? 1.300 1.898 1.637 0.108  0.198  -0.138 146 SER BBB OG  
1134  N N   . PRO A 147 ? 1.386 1.920 1.743 0.140  0.201  -0.088 147 PRO BBB N   
1135  C CA  . PRO A 147 ? 1.503 2.016 1.831 0.159  0.199  -0.062 147 PRO BBB CA  
1136  C C   . PRO A 147 ? 1.469 1.993 1.752 0.166  0.199  -0.055 147 PRO BBB C   
1137  O O   . PRO A 147 ? 1.496 1.999 1.754 0.176  0.210  -0.035 147 PRO BBB O   
1138  C CB  . PRO A 147 ? 1.547 2.042 1.868 0.179  0.171  -0.053 147 PRO BBB CB  
1139  C CG  . PRO A 147 ? 1.429 1.944 1.759 0.173  0.157  -0.075 147 PRO BBB CG  
1140  C CD  . PRO A 147 ? 1.358 1.890 1.718 0.147  0.179  -0.096 147 PRO BBB CD  
1141  N N   . THR A 148 ? 1.506 2.058 1.777 0.162  0.189  -0.071 148 THR BBB N   
1142  C CA  . THR A 148 ? 1.524 2.087 1.756 0.171  0.186  -0.066 148 THR BBB CA  
1143  C C   . THR A 148 ? 1.514 2.111 1.760 0.156  0.192  -0.086 148 THR BBB C   
1144  O O   . THR A 148 ? 1.575 2.185 1.837 0.145  0.184  -0.104 148 THR BBB O   
1145  C CB  . THR A 148 ? 1.535 2.091 1.727 0.190  0.159  -0.061 148 THR BBB CB  
1146  O OG1 . THR A 148 ? 1.693 2.265 1.898 0.185  0.143  -0.079 148 THR BBB OG1 
1147  C CG2 . THR A 148 ? 1.526 2.048 1.702 0.207  0.146  -0.042 148 THR BBB CG2 
1148  N N   . SER A 149 ? 1.548 2.156 1.787 0.156  0.205  -0.084 149 SER BBB N   
1149  C CA  . SER A 149 ? 1.540 2.184 1.792 0.147  0.203  -0.102 149 SER BBB CA  
1150  C C   . SER A 149 ? 1.481 2.132 1.698 0.161  0.180  -0.103 149 SER BBB C   
1151  O O   . SER A 149 ? 1.564 2.198 1.746 0.177  0.173  -0.089 149 SER BBB O   
1152  C CB  . SER A 149 ? 1.586 2.241 1.856 0.142  0.227  -0.103 149 SER BBB CB  
1153  O OG  . SER A 149 ? 1.561 2.251 1.840 0.141  0.218  -0.118 149 SER BBB OG  
1154  N N   . ILE A 150 ? 1.292 1.967 1.516 0.155  0.167  -0.121 150 ILE BBB N   
1155  C CA  A ILE A 150 ? 1.311 1.991 1.504 0.168  0.147  -0.122 150 ILE BBB CA  
1156  C C   . ILE A 150 ? 1.380 2.065 1.553 0.181  0.150  -0.113 150 ILE BBB C   
1157  O O   . ILE A 150 ? 1.339 2.016 1.480 0.195  0.138  -0.108 150 ILE BBB O   
1158  C CB  A ILE A 150 ? 1.266 1.965 1.465 0.160  0.135  -0.141 150 ILE BBB CB  
1159  C CG1 A ILE A 150 ? 1.237 1.933 1.403 0.173  0.117  -0.141 150 ILE BBB CG1 
1160  C CG2 A ILE A 150 ? 1.285 2.015 1.511 0.153  0.140  -0.151 150 ILE BBB CG2 
1161  C CD1 A ILE A 150 ? 1.270 1.939 1.420 0.178  0.112  -0.137 150 ILE BBB CD1 
1162  N N   . LEU A 151 ? 1.360 2.057 1.555 0.176  0.170  -0.113 151 LEU BBB N   
1163  C CA  . LEU A 151 ? 1.409 2.106 1.589 0.187  0.181  -0.105 151 LEU BBB CA  
1164  C C   . LEU A 151 ? 1.451 2.112 1.586 0.199  0.185  -0.086 151 LEU BBB C   
1165  O O   . LEU A 151 ? 1.549 2.203 1.655 0.211  0.190  -0.080 151 LEU BBB O   
1166  C CB  . LEU A 151 ? 1.391 2.105 1.613 0.176  0.207  -0.111 151 LEU BBB CB  
1167  C CG  . LEU A 151 ? 1.380 2.133 1.647 0.165  0.197  -0.133 151 LEU BBB CG  
1168  C CD1 . LEU A 151 ? 1.548 2.314 1.869 0.148  0.222  -0.142 151 LEU BBB CD1 
1169  C CD2 . LEU A 151 ? 1.414 2.191 1.682 0.176  0.186  -0.140 151 LEU BBB CD2 
1170  N N   . ASP A 152 ? 1.458 2.093 1.584 0.199  0.183  -0.076 152 ASP BBB N   
1171  C CA  . ASP A 152 ? 1.524 2.123 1.605 0.213  0.181  -0.057 152 ASP BBB CA  
1172  C C   . ASP A 152 ? 1.499 2.090 1.555 0.225  0.151  -0.059 152 ASP BBB C   
1173  O O   . ASP A 152 ? 1.523 2.086 1.542 0.238  0.141  -0.047 152 ASP BBB O   
1174  C CB  . ASP A 152 ? 1.609 2.180 1.698 0.209  0.194  -0.044 152 ASP BBB CB  
1175  C CG  . ASP A 152 ? 1.760 2.329 1.868 0.199  0.230  -0.041 152 ASP BBB CG  
1176  O OD1 . ASP A 152 ? 1.813 2.404 1.934 0.195  0.244  -0.050 152 ASP BBB OD1 
1177  O OD2 . ASP A 152 ? 1.944 2.488 2.060 0.196  0.246  -0.029 152 ASP BBB OD2 
1178  N N   . ILE A 153 ? 1.504 2.118 1.580 0.220  0.136  -0.075 153 ILE BBB N   
1179  C CA  . ILE A 153 ? 1.412 2.021 1.471 0.229  0.112  -0.080 153 ILE BBB CA  
1180  C C   . ILE A 153 ? 1.423 2.038 1.453 0.239  0.109  -0.082 153 ILE BBB C   
1181  O O   . ILE A 153 ? 1.402 2.040 1.444 0.236  0.111  -0.092 153 ILE BBB O   
1182  C CB  . ILE A 153 ? 1.186 1.806 1.275 0.219  0.104  -0.095 153 ILE BBB CB  
1183  C CG1 . ILE A 153 ? 1.201 1.815 1.323 0.206  0.112  -0.095 153 ILE BBB CG1 
1184  C CG2 . ILE A 153 ? 1.140 1.751 1.217 0.227  0.084  -0.102 153 ILE BBB CG2 
1185  C CD1 . ILE A 153 ? 1.320 1.907 1.439 0.215  0.104  -0.084 153 ILE BBB CD1 
1186  N N   . ARG A 154 ? 1.403 1.997 1.393 0.253  0.103  -0.074 154 ARG BBB N   
1187  C CA  . ARG A 154 ? 1.396 1.992 1.355 0.263  0.102  -0.077 154 ARG BBB CA  
1188  C C   . ARG A 154 ? 1.373 1.954 1.308 0.274  0.078  -0.081 154 ARG BBB C   
1189  O O   . ARG A 154 ? 1.434 1.994 1.357 0.279  0.065  -0.075 154 ARG BBB O   
1190  C CB  . ARG A 154 ? 1.591 2.171 1.518 0.267  0.124  -0.064 154 ARG BBB CB  
1191  C CG  . ARG A 154 ? 1.806 2.396 1.719 0.272  0.136  -0.070 154 ARG BBB CG  
1192  C CD  . ARG A 154 ? 1.959 2.536 1.858 0.270  0.168  -0.060 154 ARG BBB CD  
1193  N NE  . ARG A 154 ? 2.019 2.606 1.960 0.257  0.186  -0.057 154 ARG BBB NE  
1194  C CZ  . ARG A 154 ? 2.053 2.674 2.047 0.247  0.198  -0.068 154 ARG BBB CZ  
1195  N NH1 . ARG A 154 ? 2.016 2.663 2.028 0.249  0.193  -0.080 154 ARG BBB NH1 
1196  N NH2 . ARG A 154 ? 2.117 2.744 2.148 0.234  0.213  -0.067 154 ARG BBB NH2 
1197  N N   . GLN A 155 ? 1.330 1.921 1.260 0.278  0.072  -0.093 155 GLN BBB N   
1198  C CA  . GLN A 155 ? 1.407 1.986 1.323 0.286  0.050  -0.102 155 GLN BBB CA  
1199  C C   . GLN A 155 ? 1.555 2.110 1.420 0.299  0.044  -0.095 155 GLN BBB C   
1200  O O   . GLN A 155 ? 1.776 2.326 1.609 0.302  0.060  -0.089 155 GLN BBB O   
1201  C CB  . GLN A 155 ? 1.409 2.001 1.333 0.287  0.050  -0.116 155 GLN BBB CB  
1202  C CG  . GLN A 155 ? 1.490 2.074 1.414 0.293  0.031  -0.129 155 GLN BBB CG  
1203  C CD  . GLN A 155 ? 1.508 2.098 1.435 0.294  0.036  -0.142 155 GLN BBB CD  
1204  O OE1 . GLN A 155 ? 1.563 2.164 1.486 0.295  0.050  -0.138 155 GLN BBB OE1 
1205  N NE2 . GLN A 155 ? 1.510 2.093 1.450 0.295  0.024  -0.156 155 GLN BBB NE2 
1206  N N   . GLY A 156 ? 1.762 2.301 1.619 0.306  0.020  -0.096 156 GLY BBB N   
1207  C CA  . GLY A 156 ? 1.941 2.453 1.741 0.320  0.007  -0.091 156 GLY BBB CA  
1208  C C   . GLY A 156 ? 2.031 2.544 1.808 0.325  0.002  -0.106 156 GLY BBB C   
1209  O O   . GLY A 156 ? 2.039 2.573 1.851 0.320  0.003  -0.121 156 GLY BBB O   
1210  N N   . PRO A 157 ? 2.007 2.496 1.721 0.336  0.000  -0.102 157 PRO BBB N   
1211  C CA  A PRO A 157 ? 1.938 2.426 1.628 0.340  -0.000 -0.118 157 PRO BBB CA  
1212  C C   . PRO A 157 ? 1.966 2.462 1.682 0.343  -0.030 -0.140 157 PRO BBB C   
1213  O O   . PRO A 157 ? 1.881 2.389 1.613 0.341  -0.025 -0.157 157 PRO BBB O   
1214  C CB  A PRO A 157 ? 2.059 2.511 1.668 0.350  0.002  -0.109 157 PRO BBB CB  
1215  C CG  A PRO A 157 ? 2.075 2.509 1.667 0.350  0.014  -0.085 157 PRO BBB CG  
1216  C CD  A PRO A 157 ? 2.014 2.469 1.671 0.344  0.002  -0.083 157 PRO BBB CD  
1217  N N   . LYS A 158 ? 2.178 2.667 1.904 0.348  -0.060 -0.141 158 LYS BBB N   
1218  C CA  . LYS A 158 ? 2.290 2.787 2.053 0.350  -0.089 -0.164 158 LYS BBB CA  
1219  C C   . LYS A 158 ? 2.243 2.761 2.083 0.340  -0.089 -0.170 158 LYS BBB C   
1220  O O   . LYS A 158 ? 2.334 2.858 2.216 0.340  -0.110 -0.189 158 LYS BBB O   
1221  C CB  . LYS A 158 ? 2.578 3.053 2.305 0.365  -0.128 -0.166 158 LYS BBB CB  
1222  C CG  . LYS A 158 ? 2.777 3.246 2.522 0.368  -0.142 -0.149 158 LYS BBB CG  
1223  C CD  . LYS A 158 ? 3.035 3.468 2.707 0.386  -0.167 -0.135 158 LYS BBB CD  
1224  C CE  . LYS A 158 ? 3.098 3.519 2.779 0.388  -0.166 -0.109 158 LYS BBB CE  
1225  N NZ  . LYS A 158 ? 3.077 3.502 2.762 0.375  -0.120 -0.091 158 LYS BBB NZ  
1226  N N   . GLU A 159 ? 2.032 2.559 1.894 0.330  -0.064 -0.155 159 GLU BBB N   
1227  C CA  . GLU A 159 ? 1.827 2.368 1.754 0.319  -0.061 -0.160 159 GLU BBB CA  
1228  C C   . GLU A 159 ? 1.675 2.229 1.634 0.310  -0.046 -0.177 159 GLU BBB C   
1229  O O   . GLU A 159 ? 1.652 2.212 1.593 0.307  -0.025 -0.173 159 GLU BBB O   
1230  C CB  . GLU A 159 ? 1.783 2.327 1.717 0.311  -0.042 -0.140 159 GLU BBB CB  
1231  C CG  . GLU A 159 ? 1.741 2.294 1.736 0.299  -0.037 -0.146 159 GLU BBB CG  
1232  C CD  . GLU A 159 ? 1.723 2.280 1.727 0.290  -0.018 -0.130 159 GLU BBB CD  
1233  O OE1 . GLU A 159 ? 1.725 2.282 1.696 0.290  -0.003 -0.116 159 GLU BBB OE1 
1234  O OE2 . GLU A 159 ? 1.687 2.245 1.735 0.281  -0.017 -0.132 159 GLU BBB OE2 
1235  N N   . PRO A 160 ? 1.501 2.058 1.509 0.306  -0.056 -0.197 160 PRO BBB N   
1236  C CA  . PRO A 160 ? 1.397 1.958 1.433 0.297  -0.036 -0.210 160 PRO BBB CA  
1237  C C   . PRO A 160 ? 1.426 1.992 1.463 0.287  -0.010 -0.196 160 PRO BBB C   
1238  O O   . PRO A 160 ? 1.574 2.142 1.624 0.281  -0.008 -0.185 160 PRO BBB O   
1239  C CB  . PRO A 160 ? 1.370 1.929 1.465 0.292  -0.047 -0.231 160 PRO BBB CB  
1240  C CG  . PRO A 160 ? 1.503 2.061 1.595 0.304  -0.081 -0.235 160 PRO BBB CG  
1241  C CD  . PRO A 160 ? 1.574 2.127 1.615 0.311  -0.084 -0.208 160 PRO BBB CD  
1242  N N   . PHE A 161 ? 1.358 1.925 1.382 0.285  0.008  -0.197 161 PHE BBB N   
1243  C CA  . PHE A 161 ? 1.292 1.864 1.313 0.277  0.026  -0.186 161 PHE BBB CA  
1244  C C   . PHE A 161 ? 1.241 1.808 1.297 0.265  0.033  -0.190 161 PHE BBB C   
1245  O O   . PHE A 161 ? 1.198 1.771 1.254 0.258  0.040  -0.179 161 PHE BBB O   
1246  C CB  . PHE A 161 ? 1.310 1.879 1.317 0.280  0.040  -0.189 161 PHE BBB CB  
1247  C CG  . PHE A 161 ? 1.338 1.914 1.335 0.277  0.053  -0.177 161 PHE BBB CG  
1248  C CD1 . PHE A 161 ? 1.371 1.962 1.363 0.274  0.052  -0.164 161 PHE BBB CD1 
1249  C CD2 . PHE A 161 ? 1.340 1.905 1.333 0.276  0.065  -0.180 161 PHE BBB CD2 
1250  C CE1 . PHE A 161 ? 1.320 1.920 1.309 0.271  0.060  -0.156 161 PHE BBB CE1 
1251  C CE2 . PHE A 161 ? 1.310 1.880 1.291 0.275  0.070  -0.170 161 PHE BBB CE2 
1252  C CZ  . PHE A 161 ? 1.293 1.885 1.276 0.272  0.066  -0.160 161 PHE BBB CZ  
1253  N N   . ARG A 162 ? 1.238 1.793 1.326 0.261  0.034  -0.207 162 ARG BBB N   
1254  C CA  . ARG A 162 ? 1.215 1.760 1.338 0.248  0.045  -0.213 162 ARG BBB CA  
1255  C C   . ARG A 162 ? 1.176 1.729 1.318 0.245  0.036  -0.205 162 ARG BBB C   
1256  O O   . ARG A 162 ? 1.258 1.808 1.410 0.233  0.049  -0.201 162 ARG BBB O   
1257  C CB  . ARG A 162 ? 1.256 1.786 1.419 0.244  0.050  -0.237 162 ARG BBB CB  
1258  C CG  . ARG A 162 ? 1.262 1.776 1.462 0.229  0.070  -0.247 162 ARG BBB CG  
1259  C CD  . ARG A 162 ? 1.314 1.816 1.566 0.226  0.073  -0.272 162 ARG BBB CD  
1260  N NE  . ARG A 162 ? 1.520 2.013 1.754 0.231  0.080  -0.280 162 ARG BBB NE  
1261  C CZ  . ARG A 162 ? 1.601 2.085 1.875 0.230  0.086  -0.304 162 ARG BBB CZ  
1262  N NH1 . ARG A 162 ? 1.441 1.924 1.782 0.223  0.084  -0.324 162 ARG BBB NH1 
1263  N NH2 . ARG A 162 ? 1.580 2.053 1.832 0.234  0.095  -0.309 162 ARG BBB NH2 
1264  N N   . ASP A 163 ? 1.185 1.744 1.328 0.255  0.013  -0.202 163 ASP BBB N   
1265  C CA  . ASP A 163 ? 1.210 1.772 1.370 0.255  0.004  -0.192 163 ASP BBB CA  
1266  C C   . ASP A 163 ? 1.241 1.810 1.369 0.252  0.014  -0.171 163 ASP BBB C   
1267  O O   . ASP A 163 ? 1.283 1.851 1.430 0.244  0.021  -0.165 163 ASP BBB O   
1268  C CB  . ASP A 163 ? 1.345 1.906 1.505 0.270  -0.026 -0.192 163 ASP BBB CB  
1269  C CG  . ASP A 163 ? 1.434 1.993 1.642 0.271  -0.041 -0.217 163 ASP BBB CG  
1270  O OD1 . ASP A 163 ? 1.534 2.088 1.788 0.259  -0.024 -0.232 163 ASP BBB OD1 
1271  O OD2 . ASP A 163 ? 1.338 1.897 1.534 0.285  -0.067 -0.223 163 ASP BBB OD2 
1272  N N   . TYR A 164 ? 1.207 1.782 1.292 0.259  0.017  -0.163 164 TYR BBB N   
1273  C CA  . TYR A 164 ? 1.174 1.757 1.237 0.256  0.029  -0.147 164 TYR BBB CA  
1274  C C   . TYR A 164 ? 1.175 1.764 1.253 0.242  0.046  -0.150 164 TYR BBB C   
1275  O O   . TYR A 164 ? 1.207 1.801 1.294 0.233  0.054  -0.143 164 TYR BBB O   
1276  C CB  . TYR A 164 ? 1.183 1.773 1.206 0.266  0.030  -0.142 164 TYR BBB CB  
1277  C CG  . TYR A 164 ? 1.207 1.810 1.219 0.262  0.046  -0.133 164 TYR BBB CG  
1278  C CD1 . TYR A 164 ? 1.237 1.844 1.251 0.257  0.054  -0.121 164 TYR BBB CD1 
1279  C CD2 . TYR A 164 ? 1.187 1.799 1.191 0.263  0.052  -0.137 164 TYR BBB CD2 
1280  C CE1 . TYR A 164 ? 1.165 1.790 1.181 0.253  0.068  -0.116 164 TYR BBB CE1 
1281  C CE2 . TYR A 164 ? 1.138 1.766 1.141 0.261  0.063  -0.131 164 TYR BBB CE2 
1282  C CZ  . TYR A 164 ? 1.136 1.772 1.147 0.255  0.070  -0.122 164 TYR BBB CZ  
1283  O OH  . TYR A 164 ? 1.127 1.783 1.147 0.252  0.080  -0.120 164 TYR BBB OH  
1284  N N   . VAL A 165 ? 1.130 1.713 1.208 0.238  0.052  -0.161 165 VAL BBB N   
1285  C CA  . VAL A 165 ? 1.088 1.670 1.168 0.226  0.066  -0.164 165 VAL BBB CA  
1286  C C   . VAL A 165 ? 1.080 1.652 1.191 0.213  0.074  -0.170 165 VAL BBB C   
1287  O O   . VAL A 165 ? 1.044 1.620 1.157 0.202  0.083  -0.168 165 VAL BBB O   
1288  C CB  . VAL A 165 ? 1.113 1.681 1.179 0.228  0.073  -0.174 165 VAL BBB CB  
1289  C CG1 . VAL A 165 ? 1.281 1.838 1.335 0.217  0.086  -0.176 165 VAL BBB CG1 
1290  C CG2 . VAL A 165 ? 1.135 1.711 1.172 0.241  0.068  -0.168 165 VAL BBB CG2 
1291  N N   . ASP A 166 ? 1.238 1.799 1.380 0.213  0.069  -0.178 166 ASP BBB N   
1292  C CA  . ASP A 166 ? 1.286 1.839 1.467 0.202  0.076  -0.183 166 ASP BBB CA  
1293  C C   . ASP A 166 ? 1.298 1.863 1.483 0.200  0.075  -0.169 166 ASP BBB C   
1294  O O   . ASP A 166 ? 1.372 1.934 1.571 0.186  0.089  -0.171 166 ASP BBB O   
1295  C CB  . ASP A 166 ? 1.308 1.854 1.532 0.207  0.066  -0.194 166 ASP BBB CB  
1296  C CG  . ASP A 166 ? 1.383 1.911 1.623 0.200  0.079  -0.214 166 ASP BBB CG  
1297  O OD1 . ASP A 166 ? 1.428 1.941 1.665 0.186  0.103  -0.220 166 ASP BBB OD1 
1298  O OD2 . ASP A 166 ? 1.393 1.921 1.650 0.209  0.068  -0.224 166 ASP BBB OD2 
1299  N N   . ARG A 167 ? 1.143 1.716 1.312 0.213  0.061  -0.156 167 ARG BBB N   
1300  C CA  . ARG A 167 ? 1.113 1.690 1.282 0.212  0.064  -0.141 167 ARG BBB CA  
1301  C C   . ARG A 167 ? 1.070 1.660 1.225 0.202  0.079  -0.139 167 ARG BBB C   
1302  O O   . ARG A 167 ? 1.071 1.663 1.243 0.191  0.090  -0.136 167 ARG BBB O   
1303  C CB  . ARG A 167 ? 1.142 1.717 1.285 0.229  0.049  -0.126 167 ARG BBB CB  
1304  C CG  . ARG A 167 ? 1.207 1.770 1.367 0.240  0.028  -0.128 167 ARG BBB CG  
1305  C CD  . ARG A 167 ? 1.298 1.852 1.423 0.257  0.014  -0.111 167 ARG BBB CD  
1306  N NE  . ARG A 167 ? 1.272 1.829 1.347 0.264  0.015  -0.107 167 ARG BBB NE  
1307  C CZ  . ARG A 167 ? 1.271 1.829 1.315 0.264  0.029  -0.093 167 ARG BBB CZ  
1308  N NH1 . ARG A 167 ? 1.315 1.869 1.369 0.257  0.045  -0.081 167 ARG BBB NH1 
1309  N NH2 . ARG A 167 ? 1.283 1.844 1.288 0.270  0.032  -0.092 167 ARG BBB NH2 
1310  N N   . PHE A 168 ? 1.037 1.637 1.164 0.206  0.078  -0.141 168 PHE BBB N   
1311  C CA  . PHE A 168 ? 1.056 1.673 1.174 0.199  0.086  -0.140 168 PHE BBB CA  
1312  C C   . PHE A 168 ? 1.052 1.665 1.184 0.182  0.096  -0.151 168 PHE BBB C   
1313  O O   . PHE A 168 ? 1.072 1.694 1.219 0.172  0.104  -0.151 168 PHE BBB O   
1314  C CB  . PHE A 168 ? 1.056 1.680 1.145 0.209  0.081  -0.141 168 PHE BBB CB  
1315  C CG  . PHE A 168 ? 1.049 1.695 1.134 0.206  0.084  -0.141 168 PHE BBB CG  
1316  C CD1 . PHE A 168 ? 1.055 1.702 1.136 0.198  0.084  -0.150 168 PHE BBB CD1 
1317  C CD2 . PHE A 168 ? 1.131 1.792 1.214 0.213  0.087  -0.132 168 PHE BBB CD2 
1318  C CE1 . PHE A 168 ? 1.041 1.710 1.123 0.198  0.081  -0.152 168 PHE BBB CE1 
1319  C CE2 . PHE A 168 ? 1.091 1.775 1.183 0.211  0.089  -0.135 168 PHE BBB CE2 
1320  C CZ  . PHE A 168 ? 1.042 1.732 1.135 0.204  0.083  -0.145 168 PHE BBB CZ  
1321  N N   . TYR A 169 ? 1.026 1.622 1.155 0.178  0.098  -0.162 169 TYR BBB N   
1322  C CA  . TYR A 169 ? 1.030 1.615 1.161 0.162  0.110  -0.174 169 TYR BBB CA  
1323  C C   . TYR A 169 ? 1.014 1.590 1.182 0.149  0.121  -0.179 169 TYR BBB C   
1324  O O   . TYR A 169 ? 1.042 1.613 1.213 0.133  0.133  -0.188 169 TYR BBB O   
1325  C CB  . TYR A 169 ? 1.092 1.653 1.202 0.161  0.114  -0.184 169 TYR BBB CB  
1326  C CG  . TYR A 169 ? 1.177 1.743 1.247 0.171  0.106  -0.181 169 TYR BBB CG  
1327  C CD1 . TYR A 169 ? 1.154 1.740 1.209 0.171  0.099  -0.178 169 TYR BBB CD1 
1328  C CD2 . TYR A 169 ? 1.230 1.780 1.283 0.181  0.106  -0.183 169 TYR BBB CD2 
1329  C CE1 . TYR A 169 ? 1.080 1.670 1.103 0.182  0.089  -0.176 169 TYR BBB CE1 
1330  C CE2 . TYR A 169 ? 1.151 1.701 1.168 0.191  0.099  -0.179 169 TYR BBB CE2 
1331  C CZ  . TYR A 169 ? 1.109 1.679 1.111 0.193  0.089  -0.174 169 TYR BBB CZ  
1332  O OH  . TYR A 169 ? 1.164 1.734 1.135 0.206  0.081  -0.170 169 TYR BBB OH  
1333  N N   . LYS A 170 ? 1.001 1.572 1.197 0.155  0.118  -0.173 170 LYS BBB N   
1334  C CA  . LYS A 170 ? 0.964 1.528 1.201 0.146  0.128  -0.174 170 LYS BBB CA  
1335  C C   . LYS A 170 ? 1.179 1.757 1.420 0.140  0.134  -0.167 170 LYS BBB C   
1336  O O   . LYS A 170 ? 1.261 1.835 1.523 0.124  0.149  -0.175 170 LYS BBB O   
1337  C CB  . LYS A 170 ? 0.969 1.526 1.233 0.159  0.116  -0.168 170 LYS BBB CB  
1338  C CG  . LYS A 170 ? 1.128 1.676 1.438 0.153  0.124  -0.166 170 LYS BBB CG  
1339  C CD  . LYS A 170 ? 1.371 1.903 1.716 0.137  0.142  -0.185 170 LYS BBB CD  
1340  C CE  . LYS A 170 ? 1.414 1.936 1.816 0.136  0.146  -0.183 170 LYS BBB CE  
1341  N NZ  . LYS A 170 ? 1.291 1.809 1.724 0.153  0.125  -0.182 170 LYS BBB NZ  
1342  N N   . THR A 171 ? 1.220 1.813 1.443 0.151  0.125  -0.153 171 THR BBB N   
1343  C CA  . THR A 171 ? 1.161 1.768 1.392 0.145  0.135  -0.147 171 THR BBB CA  
1344  C C   . THR A 171 ? 1.209 1.831 1.435 0.131  0.141  -0.162 171 THR BBB C   
1345  O O   . THR A 171 ? 1.264 1.890 1.513 0.116  0.154  -0.168 171 THR BBB O   
1346  C CB  . THR A 171 ? 1.115 1.732 1.325 0.160  0.129  -0.131 171 THR BBB CB  
1347  O OG1 . THR A 171 ? 1.029 1.628 1.235 0.175  0.120  -0.118 171 THR BBB OG1 
1348  C CG2 . THR A 171 ? 1.368 1.996 1.591 0.153  0.144  -0.127 171 THR BBB CG2 
1349  N N   . LEU A 172 ? 1.169 1.796 1.363 0.135  0.130  -0.167 172 LEU BBB N   
1350  C CA  . LEU A 172 ? 1.275 1.913 1.457 0.125  0.129  -0.181 172 LEU BBB CA  
1351  C C   . LEU A 172 ? 1.370 1.990 1.560 0.106  0.141  -0.197 172 LEU BBB C   
1352  O O   . LEU A 172 ? 1.557 2.185 1.753 0.092  0.144  -0.209 172 LEU BBB O   
1353  C CB  . LEU A 172 ? 1.230 1.869 1.374 0.136  0.114  -0.182 172 LEU BBB CB  
1354  C CG  . LEU A 172 ? 1.443 2.111 1.580 0.145  0.102  -0.180 172 LEU BBB CG  
1355  C CD1 . LEU A 172 ? 1.576 2.237 1.676 0.158  0.089  -0.178 172 LEU BBB CD1 
1356  C CD2 . LEU A 172 ? 1.647 2.333 1.798 0.131  0.101  -0.193 172 LEU BBB CD2 
1357  N N   . ARG A 173 ? 1.206 1.799 1.399 0.105  0.148  -0.199 173 ARG BBB N   
1358  C CA  . ARG A 173 ? 1.217 1.787 1.418 0.087  0.164  -0.215 173 ARG BBB CA  
1359  C C   . ARG A 173 ? 1.287 1.861 1.531 0.073  0.179  -0.217 173 ARG BBB C   
1360  O O   . ARG A 173 ? 1.626 2.193 1.872 0.055  0.191  -0.234 173 ARG BBB O   
1361  C CB  . ARG A 173 ? 1.238 1.779 1.445 0.088  0.173  -0.218 173 ARG BBB CB  
1362  C CG  . ARG A 173 ? 1.350 1.863 1.558 0.068  0.195  -0.237 173 ARG BBB CG  
1363  C CD  . ARG A 173 ? 1.307 1.787 1.501 0.066  0.207  -0.246 173 ARG BBB CD  
1364  N NE  . ARG A 173 ? 1.341 1.802 1.588 0.059  0.226  -0.254 173 ARG BBB NE  
1365  C CZ  . ARG A 173 ? 1.359 1.790 1.613 0.056  0.242  -0.264 173 ARG BBB CZ  
1366  N NH1 . ARG A 173 ? 1.328 1.742 1.533 0.060  0.242  -0.266 173 ARG BBB NH1 
1367  N NH2 . ARG A 173 ? 1.336 1.755 1.650 0.049  0.259  -0.273 173 ARG BBB NH2 
1368  N N   . ALA A 174 ? 1.146 1.729 1.421 0.082  0.179  -0.202 174 ALA BBB N   
1369  C CA  . ALA A 174 ? 1.354 1.935 1.670 0.071  0.195  -0.202 174 ALA BBB CA  
1370  C C   . ALA A 174 ? 1.542 2.145 1.858 0.059  0.199  -0.211 174 ALA BBB C   
1371  O O   . ALA A 174 ? 1.761 2.362 2.104 0.041  0.215  -0.223 174 ALA BBB O   
1372  C CB  . ALA A 174 ? 1.290 1.869 1.629 0.086  0.193  -0.181 174 ALA BBB CB  
1373  N N   . GLU A 175 ? 1.468 2.095 1.761 0.069  0.183  -0.206 175 GLU BBB N   
1374  C CA  . GLU A 175 ? 1.585 2.238 1.887 0.060  0.183  -0.217 175 GLU BBB CA  
1375  C C   . GLU A 175 ? 1.767 2.417 2.048 0.045  0.179  -0.240 175 GLU BBB C   
1376  O O   . GLU A 175 ? 1.648 2.310 1.896 0.050  0.159  -0.246 175 GLU BBB O   
1377  C CB  . GLU A 175 ? 1.681 2.358 1.965 0.076  0.167  -0.207 175 GLU BBB CB  
1378  C CG  . GLU A 175 ? 1.747 2.422 2.039 0.092  0.172  -0.183 175 GLU BBB CG  
1379  C CD  . GLU A 175 ? 1.902 2.584 2.230 0.086  0.191  -0.179 175 GLU BBB CD  
1380  O OE1 . GLU A 175 ? 2.095 2.801 2.446 0.074  0.196  -0.193 175 GLU BBB OE1 
1381  O OE2 . GLU A 175 ? 1.747 2.409 2.080 0.093  0.202  -0.161 175 GLU BBB OE2 
1382  N N   . GLN A 176 ? 2.135 2.766 2.433 0.026  0.197  -0.254 176 GLN BBB N   
1383  C CA  . GLN A 176 ? 2.362 2.984 2.637 0.008  0.197  -0.279 176 GLN BBB CA  
1384  C C   . GLN A 176 ? 2.485 3.087 2.700 0.016  0.183  -0.281 176 GLN BBB C   
1385  O O   . GLN A 176 ? 2.868 3.474 3.042 0.014  0.167  -0.293 176 GLN BBB O   
1386  C CB  . GLN A 176 ? 2.579 3.231 2.864 -0.002 0.188  -0.296 176 GLN BBB CB  
1387  C CG  . GLN A 176 ? 2.660 3.300 2.944 -0.027 0.198  -0.325 176 GLN BBB CG  
1388  C CD  . GLN A 176 ? 2.819 3.450 3.038 -0.029 0.176  -0.342 176 GLN BBB CD  
1389  O OE1 . GLN A 176 ? 2.964 3.615 3.156 -0.014 0.148  -0.338 176 GLN BBB OE1 
1390  N NE2 . GLN A 176 ? 2.788 3.384 2.977 -0.046 0.190  -0.360 176 GLN BBB NE2 
1391  N N   . ALA A 177 ? 2.011 2.588 2.221 0.025  0.191  -0.269 177 ALA BBB N   
1392  C CA  . ALA A 177 ? 2.001 2.549 2.163 0.030  0.189  -0.270 177 ALA BBB CA  
1393  C C   . ALA A 177 ? 2.223 2.780 2.334 0.045  0.164  -0.265 177 ALA BBB C   
1394  O O   . ALA A 177 ? 2.623 3.213 2.736 0.050  0.145  -0.265 177 ALA BBB O   
1395  C CB  . ALA A 177 ? 2.054 2.567 2.193 0.009  0.208  -0.292 177 ALA BBB CB  
1396  N N   . SER A 178 ? 2.121 2.650 2.194 0.053  0.164  -0.261 178 SER BBB N   
1397  C CA  . SER A 178 ? 2.404 2.935 2.426 0.069  0.143  -0.255 178 SER BBB CA  
1398  C C   . SER A 178 ? 2.799 3.326 2.773 0.063  0.129  -0.269 178 SER BBB C   
1399  O O   . SER A 178 ? 3.066 3.568 3.021 0.045  0.142  -0.285 178 SER BBB O   
1400  C CB  . SER A 178 ? 2.206 2.699 2.198 0.077  0.154  -0.250 178 SER BBB CB  
1401  O OG  . SER A 178 ? 1.941 2.446 1.974 0.088  0.155  -0.237 178 SER BBB OG  
1402  N N   . GLN A 179 ? 2.998 3.548 2.951 0.079  0.101  -0.263 179 GLN BBB N   
1403  C CA  . GLN A 179 ? 3.232 3.778 3.133 0.079  0.079  -0.274 179 GLN BBB CA  
1404  C C   . GLN A 179 ? 3.487 4.045 3.363 0.104  0.053  -0.260 179 GLN BBB C   
1405  O O   . GLN A 179 ? 3.381 3.948 3.277 0.118  0.056  -0.244 179 GLN BBB O   
1406  C CB  . GLN A 179 ? 3.232 3.815 3.167 0.066  0.066  -0.291 179 GLN BBB CB  
1407  C CG  . GLN A 179 ? 3.312 3.875 3.251 0.040  0.087  -0.311 179 GLN BBB CG  
1408  C CD  . GLN A 179 ? 3.359 3.944 3.376 0.028  0.110  -0.312 179 GLN BBB CD  
1409  O OE1 . GLN A 179 ? 3.473 4.093 3.540 0.038  0.107  -0.298 179 GLN BBB OE1 
1410  N NE2 . GLN A 179 ? 3.405 3.967 3.431 0.006  0.135  -0.327 179 GLN BBB NE2 
1411  N N   . GLU A 180 ? 3.774 4.331 3.604 0.110  0.025  -0.267 180 GLU BBB N   
1412  C CA  . GLU A 180 ? 3.850 4.423 3.663 0.134  -0.005 -0.256 180 GLU BBB CA  
1413  C C   . GLU A 180 ? 3.818 4.455 3.707 0.141  -0.019 -0.255 180 GLU BBB C   
1414  O O   . GLU A 180 ? 3.807 4.462 3.706 0.161  -0.032 -0.243 180 GLU BBB O   
1415  C CB  . GLU A 180 ? 3.881 4.431 3.621 0.140  -0.034 -0.265 180 GLU BBB CB  
1416  C CG  . GLU A 180 ? 3.746 4.227 3.400 0.146  -0.019 -0.255 180 GLU BBB CG  
1417  C CD  . GLU A 180 ? 3.664 4.139 3.314 0.170  -0.019 -0.233 180 GLU BBB CD  
1418  O OE1 . GLU A 180 ? 3.607 4.126 3.294 0.187  -0.044 -0.226 180 GLU BBB OE1 
1419  O OE2 . GLU A 180 ? 3.668 4.093 3.279 0.170  0.007  -0.224 180 GLU BBB OE2 
1420  N N   . VAL A 181 ? 3.618 4.284 3.559 0.123  -0.013 -0.270 181 VAL BBB N   
1421  C CA  . VAL A 181 ? 3.295 4.015 3.310 0.125  -0.018 -0.271 181 VAL BBB CA  
1422  C C   . VAL A 181 ? 3.186 3.909 3.230 0.134  0.003  -0.250 181 VAL BBB C   
1423  O O   . VAL A 181 ? 2.916 3.669 2.991 0.149  -0.004 -0.242 181 VAL BBB O   
1424  C CB  . VAL A 181 ? 3.122 3.863 3.186 0.101  -0.007 -0.291 181 VAL BBB CB  
1425  C CG1 . VAL A 181 ? 2.931 3.719 3.074 0.102  -0.000 -0.290 181 VAL BBB CG1 
1426  C CG2 . VAL A 181 ? 2.983 3.725 3.020 0.093  -0.032 -0.315 181 VAL BBB CG2 
1427  N N   . LYS A 182 ? 3.254 3.944 3.287 0.126  0.029  -0.243 182 LYS BBB N   
1428  C CA  . LYS A 182 ? 3.066 3.754 3.118 0.135  0.046  -0.225 182 LYS BBB CA  
1429  C C   . LYS A 182 ? 3.135 3.816 3.157 0.157  0.034  -0.212 182 LYS BBB C   
1430  O O   . LYS A 182 ? 3.383 4.062 3.415 0.166  0.044  -0.199 182 LYS BBB O   
1431  C CB  . LYS A 182 ? 2.795 3.447 2.840 0.124  0.070  -0.223 182 LYS BBB CB  
1432  C CG  . LYS A 182 ? 2.710 3.359 2.782 0.102  0.086  -0.236 182 LYS BBB CG  
1433  C CD  . LYS A 182 ? 2.538 3.224 2.665 0.097  0.088  -0.238 182 LYS BBB CD  
1434  C CE  . LYS A 182 ? 2.372 3.048 2.535 0.082  0.113  -0.239 182 LYS BBB CE  
1435  N NZ  . LYS A 182 ? 2.707 3.375 2.872 0.060  0.119  -0.261 182 LYS BBB NZ  
1436  N N   . ASN A 183 ? 3.055 3.730 3.038 0.168  0.012  -0.215 183 ASN BBB N   
1437  C CA  . ASN A 183 ? 2.897 3.560 2.849 0.189  0.004  -0.202 183 ASN BBB CA  
1438  C C   . ASN A 183 ? 2.738 3.443 2.723 0.205  -0.015 -0.198 183 ASN BBB C   
1439  O O   . ASN A 183 ? 2.787 3.491 2.771 0.221  -0.013 -0.186 183 ASN BBB O   
1440  C CB  . ASN A 183 ? 2.927 3.548 2.809 0.193  -0.006 -0.203 183 ASN BBB CB  
1441  C CG  . ASN A 183 ? 2.941 3.513 2.790 0.180  0.020  -0.205 183 ASN BBB CG  
1442  O OD1 . ASN A 183 ? 3.156 3.709 2.987 0.163  0.027  -0.217 183 ASN BBB OD1 
1443  N ND2 . ASN A 183 ? 2.735 3.284 2.579 0.187  0.037  -0.194 183 ASN BBB ND2 
1444  N N   . ALA A 184 ? 2.806 3.546 2.823 0.201  -0.032 -0.211 184 ALA BBB N   
1445  C CA  . ALA A 184 ? 2.606 3.389 2.670 0.214  -0.045 -0.211 184 ALA BBB CA  
1446  C C   . ALA A 184 ? 2.637 3.436 2.745 0.213  -0.019 -0.202 184 ALA BBB C   
1447  O O   . ALA A 184 ? 2.411 3.221 2.533 0.228  -0.018 -0.193 184 ALA BBB O   
1448  C CB  . ALA A 184 ? 2.293 3.113 2.396 0.207  -0.065 -0.231 184 ALA BBB CB  
1449  N N   . ALA A 185 ? 2.492 3.287 2.619 0.195  0.003  -0.204 185 ALA BBB N   
1450  C CA  . ALA A 185 ? 2.347 3.146 2.501 0.194  0.028  -0.194 185 ALA BBB CA  
1451  C C   . ALA A 185 ? 2.179 2.948 2.297 0.205  0.035  -0.179 185 ALA BBB C   
1452  O O   . ALA A 185 ? 1.988 2.761 2.117 0.212  0.048  -0.169 185 ALA BBB O   
1453  C CB  . ALA A 185 ? 2.297 3.093 2.475 0.174  0.047  -0.198 185 ALA BBB CB  
1454  N N   . THR A 186 ? 2.183 2.919 2.257 0.205  0.032  -0.178 186 THR BBB N   
1455  C CA  . THR A 186 ? 2.103 2.810 2.151 0.212  0.041  -0.168 186 THR BBB CA  
1456  C C   . THR A 186 ? 2.036 2.747 2.072 0.232  0.034  -0.160 186 THR BBB C   
1457  O O   . THR A 186 ? 1.864 2.574 1.906 0.239  0.044  -0.153 186 THR BBB O   
1458  C CB  . THR A 186 ? 2.227 2.896 2.237 0.205  0.043  -0.172 186 THR BBB CB  
1459  O OG1 . THR A 186 ? 2.489 3.154 2.513 0.186  0.052  -0.180 186 THR BBB OG1 
1460  C CG2 . THR A 186 ? 2.166 2.808 2.162 0.211  0.054  -0.166 186 THR BBB CG2 
1461  N N   . GLU A 187 ? 2.173 2.886 2.193 0.243  0.016  -0.162 187 GLU BBB N   
1462  C CA  . GLU A 187 ? 2.167 2.884 2.181 0.263  0.009  -0.155 187 GLU BBB CA  
1463  C C   . GLU A 187 ? 2.101 2.852 2.158 0.270  0.015  -0.153 187 GLU BBB C   
1464  O O   . GLU A 187 ? 2.222 2.975 2.279 0.286  0.014  -0.148 187 GLU BBB O   
1465  C CB  . GLU A 187 ? 2.272 2.991 2.269 0.274  -0.016 -0.158 187 GLU BBB CB  
1466  C CG  . GLU A 187 ? 2.325 3.082 2.358 0.268  -0.032 -0.169 187 GLU BBB CG  
1467  C CD  . GLU A 187 ? 2.526 3.272 2.524 0.272  -0.059 -0.175 187 GLU BBB CD  
1468  O OE1 . GLU A 187 ? 2.637 3.342 2.578 0.281  -0.062 -0.167 187 GLU BBB OE1 
1469  O OE2 . GLU A 187 ? 2.691 3.467 2.717 0.266  -0.076 -0.188 187 GLU BBB OE2 
1470  N N   . THR A 188 ? 1.909 2.678 1.999 0.258  0.026  -0.156 188 THR BBB N   
1471  C CA  . THR A 188 ? 1.822 2.619 1.953 0.260  0.038  -0.156 188 THR BBB CA  
1472  C C   . THR A 188 ? 1.552 2.333 1.675 0.254  0.060  -0.148 188 THR BBB C   
1473  O O   . THR A 188 ? 1.446 2.215 1.553 0.264  0.068  -0.142 188 THR BBB O   
1474  C CB  . THR A 188 ? 1.874 2.708 2.056 0.253  0.034  -0.167 188 THR BBB CB  
1475  O OG1 . THR A 188 ? 1.944 2.795 2.163 0.253  0.056  -0.166 188 THR BBB OG1 
1476  C CG2 . THR A 188 ? 1.927 2.761 2.114 0.234  0.032  -0.176 188 THR BBB CG2 
1477  N N   . LEU A 189 ? 1.395 2.172 1.527 0.239  0.068  -0.149 189 LEU BBB N   
1478  C CA  . LEU A 189 ? 1.386 2.150 1.515 0.234  0.087  -0.141 189 LEU BBB CA  
1479  C C   . LEU A 189 ? 1.425 2.158 1.514 0.241  0.085  -0.134 189 LEU BBB C   
1480  O O   . LEU A 189 ? 1.505 2.226 1.581 0.245  0.095  -0.127 189 LEU BBB O   
1481  C CB  . LEU A 189 ? 1.296 2.060 1.444 0.217  0.094  -0.144 189 LEU BBB CB  
1482  C CG  . LEU A 189 ? 1.348 2.103 1.506 0.211  0.116  -0.136 189 LEU BBB CG  
1483  C CD1 . LEU A 189 ? 1.477 2.249 1.659 0.214  0.133  -0.135 189 LEU BBB CD1 
1484  C CD2 . LEU A 189 ? 1.256 2.010 1.437 0.194  0.120  -0.141 189 LEU BBB CD2 
1485  N N   . LEU A 190 ? 1.333 2.051 1.403 0.241  0.073  -0.138 190 LEU BBB N   
1486  C CA  . LEU A 190 ? 1.226 1.918 1.271 0.246  0.072  -0.135 190 LEU BBB CA  
1487  C C   . LEU A 190 ? 1.266 1.957 1.296 0.261  0.074  -0.132 190 LEU BBB C   
1488  O O   . LEU A 190 ? 1.416 2.091 1.430 0.265  0.076  -0.129 190 LEU BBB O   
1489  C CB  . LEU A 190 ? 1.198 1.871 1.227 0.244  0.065  -0.141 190 LEU BBB CB  
1490  C CG  . LEU A 190 ? 1.108 1.754 1.124 0.246  0.067  -0.143 190 LEU BBB CG  
1491  C CD1 . LEU A 190 ? 1.168 1.806 1.199 0.236  0.070  -0.144 190 LEU BBB CD1 
1492  C CD2 . LEU A 190 ? 1.122 1.746 1.119 0.246  0.066  -0.149 190 LEU BBB CD2 
1493  N N   . VAL A 191 ? 1.214 1.921 1.250 0.270  0.072  -0.133 191 VAL BBB N   
1494  C CA  . VAL A 191 ? 1.169 1.875 1.196 0.283  0.077  -0.131 191 VAL BBB CA  
1495  C C   . VAL A 191 ? 1.230 1.945 1.265 0.283  0.092  -0.127 191 VAL BBB C   
1496  O O   . VAL A 191 ? 1.252 1.953 1.265 0.289  0.100  -0.125 191 VAL BBB O   
1497  C CB  . VAL A 191 ? 1.180 1.899 1.216 0.294  0.069  -0.134 191 VAL BBB CB  
1498  C CG1 . VAL A 191 ? 1.198 1.916 1.229 0.307  0.078  -0.133 191 VAL BBB CG1 
1499  C CG2 . VAL A 191 ? 1.182 1.881 1.196 0.295  0.058  -0.135 191 VAL BBB CG2 
1500  N N   . GLN A 192 ? 1.230 1.967 1.297 0.275  0.099  -0.128 192 GLN BBB N   
1501  C CA  . GLN A 192 ? 1.320 2.061 1.396 0.274  0.120  -0.124 192 GLN BBB CA  
1502  C C   . GLN A 192 ? 1.357 2.070 1.400 0.271  0.129  -0.115 192 GLN BBB C   
1503  O O   . GLN A 192 ? 1.505 2.204 1.527 0.275  0.145  -0.111 192 GLN BBB O   
1504  C CB  . GLN A 192 ? 1.372 2.139 1.495 0.264  0.127  -0.129 192 GLN BBB CB  
1505  C CG  . GLN A 192 ? 1.721 2.493 1.864 0.261  0.155  -0.128 192 GLN BBB CG  
1506  C CD  . GLN A 192 ? 1.939 2.740 2.138 0.248  0.161  -0.136 192 GLN BBB CD  
1507  O OE1 . GLN A 192 ? 2.078 2.908 2.314 0.248  0.145  -0.147 192 GLN BBB OE1 
1508  N NE2 . GLN A 192 ? 2.084 2.873 2.288 0.238  0.186  -0.131 192 GLN BBB NE2 
1509  N N   . ASN A 193 ? 1.318 2.019 1.354 0.264  0.117  -0.114 193 ASN BBB N   
1510  C CA  . ASN A 193 ? 1.346 2.020 1.355 0.263  0.119  -0.105 193 ASN BBB CA  
1511  C C   . ASN A 193 ? 1.344 1.997 1.319 0.272  0.104  -0.107 193 ASN BBB C   
1512  O O   . ASN A 193 ? 1.372 2.004 1.325 0.274  0.099  -0.101 193 ASN BBB O   
1513  C CB  . ASN A 193 ? 1.491 2.165 1.521 0.251  0.116  -0.104 193 ASN BBB CB  
1514  C CG  . ASN A 193 ? 1.566 2.255 1.628 0.240  0.134  -0.103 193 ASN BBB CG  
1515  O OD1 . ASN A 193 ? 1.486 2.190 1.562 0.242  0.148  -0.105 193 ASN BBB OD1 
1516  N ND2 . ASN A 193 ? 1.630 2.315 1.709 0.229  0.136  -0.101 193 ASN BBB ND2 
1517  N N   . ALA A 194 ? 1.325 1.984 1.298 0.279  0.097  -0.115 194 ALA BBB N   
1518  C CA  . ALA A 194 ? 1.391 2.031 1.338 0.287  0.086  -0.120 194 ALA BBB CA  
1519  C C   . ALA A 194 ? 1.584 2.210 1.495 0.296  0.094  -0.117 194 ALA BBB C   
1520  O O   . ALA A 194 ? 1.638 2.268 1.546 0.296  0.112  -0.111 194 ALA BBB O   
1521  C CB  . ALA A 194 ? 1.444 2.089 1.398 0.291  0.081  -0.129 194 ALA BBB CB  
1522  N N   . ASN A 195 ? 1.748 2.355 1.632 0.302  0.080  -0.122 195 ASN BBB N   
1523  C CA  . ASN A 195 ? 1.796 2.383 1.635 0.310  0.085  -0.121 195 ASN BBB CA  
1524  C C   . ASN A 195 ? 1.780 2.374 1.617 0.316  0.099  -0.128 195 ASN BBB C   
1525  O O   . ASN A 195 ? 1.679 2.291 1.547 0.315  0.099  -0.134 195 ASN BBB O   
1526  C CB  . ASN A 195 ? 1.843 2.411 1.658 0.316  0.061  -0.128 195 ASN BBB CB  
1527  C CG  . ASN A 195 ? 1.838 2.409 1.667 0.318  0.051  -0.145 195 ASN BBB CG  
1528  O OD1 . ASN A 195 ? 1.853 2.432 1.718 0.313  0.044  -0.151 195 ASN BBB OD1 
1529  N ND2 . ASN A 195 ? 1.913 2.474 1.713 0.325  0.053  -0.155 195 ASN BBB ND2 
1530  N N   . PRO A 196 ? 1.764 2.342 1.562 0.321  0.112  -0.128 196 PRO BBB N   
1531  C CA  A PRO A 196 ? 1.706 2.290 1.508 0.326  0.131  -0.135 196 PRO BBB CA  
1532  C C   . PRO A 196 ? 1.673 2.265 1.494 0.330  0.121  -0.148 196 PRO BBB C   
1533  O O   . PRO A 196 ? 1.655 2.266 1.511 0.332  0.128  -0.148 196 PRO BBB O   
1534  C CB  A PRO A 196 ? 1.798 2.351 1.540 0.331  0.142  -0.136 196 PRO BBB CB  
1535  C CG  A PRO A 196 ? 1.858 2.390 1.565 0.329  0.133  -0.124 196 PRO BBB CG  
1536  C CD  A PRO A 196 ? 1.816 2.366 1.566 0.323  0.117  -0.118 196 PRO BBB CD  
1537  N N   . ASP A 197 ? 1.646 2.221 1.443 0.333  0.105  -0.158 197 ASP BBB N   
1538  C CA  . ASP A 197 ? 1.642 2.217 1.453 0.338  0.102  -0.172 197 ASP BBB CA  
1539  C C   . ASP A 197 ? 1.670 2.259 1.523 0.334  0.095  -0.171 197 ASP BBB C   
1540  O O   . ASP A 197 ? 1.809 2.403 1.681 0.339  0.103  -0.175 197 ASP BBB O   
1541  C CB  . ASP A 197 ? 1.703 2.258 1.485 0.340  0.086  -0.188 197 ASP BBB CB  
1542  C CG  . ASP A 197 ? 2.009 2.545 1.741 0.345  0.095  -0.192 197 ASP BBB CG  
1543  O OD1 . ASP A 197 ? 2.167 2.699 1.896 0.349  0.110  -0.203 197 ASP BBB OD1 
1544  O OD2 . ASP A 197 ? 2.211 2.732 1.904 0.345  0.089  -0.185 197 ASP BBB OD2 
1545  N N   . CYS A 198 ? 1.662 2.254 1.527 0.327  0.082  -0.166 198 CYS BBB N   
1546  C CA  . CYS A 198 ? 1.525 2.125 1.422 0.322  0.078  -0.165 198 CYS BBB CA  
1547  C C   . CYS A 198 ? 1.435 2.054 1.350 0.323  0.088  -0.155 198 CYS BBB C   
1548  O O   . CYS A 198 ? 1.383 2.004 1.313 0.325  0.088  -0.155 198 CYS BBB O   
1549  C CB  . CYS A 198 ? 1.600 2.197 1.507 0.313  0.065  -0.163 198 CYS BBB CB  
1550  S SG  . CYS A 198 ? 1.894 2.474 1.800 0.313  0.047  -0.180 198 CYS BBB SG  
1551  N N   . LYS A 199 ? 1.433 2.065 1.349 0.322  0.097  -0.146 199 LYS BBB N   
1552  C CA  . LYS A 199 ? 1.403 2.057 1.347 0.323  0.104  -0.140 199 LYS BBB CA  
1553  C C   . LYS A 199 ? 1.419 2.076 1.372 0.334  0.110  -0.145 199 LYS BBB C   
1554  O O   . LYS A 199 ? 1.465 2.133 1.439 0.338  0.104  -0.142 199 LYS BBB O   
1555  C CB  . LYS A 199 ? 1.404 2.069 1.352 0.319  0.117  -0.134 199 LYS BBB CB  
1556  C CG  . LYS A 199 ? 1.429 2.122 1.418 0.318  0.122  -0.132 199 LYS BBB CG  
1557  C CD  . LYS A 199 ? 1.489 2.190 1.489 0.314  0.143  -0.129 199 LYS BBB CD  
1558  C CE  . LYS A 199 ? 1.480 2.171 1.468 0.303  0.145  -0.122 199 LYS BBB CE  
1559  N NZ  . LYS A 199 ? 1.441 2.143 1.452 0.297  0.169  -0.119 199 LYS BBB NZ  
1560  N N   . THR A 200 ? 1.449 2.094 1.383 0.340  0.121  -0.151 200 THR BBB N   
1561  C CA  . THR A 200 ? 1.488 2.132 1.432 0.352  0.129  -0.155 200 THR BBB CA  
1562  C C   . THR A 200 ? 1.501 2.133 1.447 0.355  0.118  -0.158 200 THR BBB C   
1563  O O   . THR A 200 ? 1.525 2.161 1.489 0.365  0.119  -0.154 200 THR BBB O   
1564  C CB  . THR A 200 ? 1.503 2.129 1.419 0.355  0.143  -0.165 200 THR BBB CB  
1565  O OG1 . THR A 200 ? 1.519 2.124 1.411 0.353  0.132  -0.174 200 THR BBB OG1 
1566  C CG2 . THR A 200 ? 1.664 2.290 1.561 0.350  0.155  -0.162 200 THR BBB CG2 
1567  N N   . ILE A 201 ? 1.505 2.120 1.435 0.348  0.110  -0.163 201 ILE BBB N   
1568  C CA  . ILE A 201 ? 1.428 2.025 1.360 0.350  0.106  -0.166 201 ILE BBB CA  
1569  C C   . ILE A 201 ? 1.460 2.064 1.402 0.349  0.098  -0.155 201 ILE BBB C   
1570  O O   . ILE A 201 ? 1.537 2.131 1.479 0.357  0.099  -0.152 201 ILE BBB O   
1571  C CB  . ILE A 201 ? 1.360 1.940 1.283 0.341  0.100  -0.177 201 ILE BBB CB  
1572  C CG1 . ILE A 201 ? 1.492 2.061 1.401 0.344  0.104  -0.191 201 ILE BBB CG1 
1573  C CG2 . ILE A 201 ? 1.368 1.926 1.296 0.339  0.101  -0.180 201 ILE BBB CG2 
1574  C CD1 . ILE A 201 ? 1.500 2.060 1.406 0.335  0.091  -0.203 201 ILE BBB CD1 
1575  N N   . LEU A 202 ? 1.462 2.082 1.410 0.339  0.090  -0.150 202 LEU BBB N   
1576  C CA  . LEU A 202 ? 1.392 2.017 1.346 0.336  0.081  -0.144 202 LEU BBB CA  
1577  C C   . LEU A 202 ? 1.422 2.066 1.392 0.348  0.078  -0.137 202 LEU BBB C   
1578  O O   . LEU A 202 ? 1.385 2.022 1.350 0.354  0.069  -0.133 202 LEU BBB O   
1579  C CB  . LEU A 202 ? 1.255 1.894 1.217 0.322  0.076  -0.142 202 LEU BBB CB  
1580  C CG  . LEU A 202 ? 1.243 1.865 1.197 0.311  0.075  -0.147 202 LEU BBB CG  
1581  C CD1 . LEU A 202 ? 1.253 1.889 1.218 0.300  0.071  -0.143 202 LEU BBB CD1 
1582  C CD2 . LEU A 202 ? 1.241 1.838 1.187 0.309  0.075  -0.152 202 LEU BBB CD2 
1583  N N   . LYS A 203 ? 1.408 2.075 1.398 0.352  0.085  -0.138 203 LYS BBB N   
1584  C CA  . LYS A 203 ? 1.416 2.103 1.433 0.364  0.082  -0.135 203 LYS BBB CA  
1585  C C   . LYS A 203 ? 1.452 2.121 1.462 0.381  0.083  -0.133 203 LYS BBB C   
1586  O O   . LYS A 203 ? 1.495 2.170 1.516 0.392  0.070  -0.128 203 LYS BBB O   
1587  C CB  . LYS A 203 ? 1.414 2.124 1.457 0.364  0.097  -0.138 203 LYS BBB CB  
1588  C CG  . LYS A 203 ? 1.396 2.127 1.455 0.350  0.097  -0.137 203 LYS BBB CG  
1589  C CD  . LYS A 203 ? 1.511 2.274 1.618 0.353  0.105  -0.140 203 LYS BBB CD  
1590  C CE  . LYS A 203 ? 1.453 2.212 1.558 0.351  0.133  -0.142 203 LYS BBB CE  
1591  N NZ  . LYS A 203 ? 1.463 2.250 1.616 0.346  0.146  -0.146 203 LYS BBB NZ  
1592  N N   . ALA A 204 ? 1.415 2.060 1.407 0.382  0.096  -0.138 204 ALA BBB N   
1593  C CA  . ALA A 204 ? 1.602 2.226 1.589 0.397  0.101  -0.137 204 ALA BBB CA  
1594  C C   . ALA A 204 ? 1.682 2.277 1.644 0.399  0.092  -0.131 204 ALA BBB C   
1595  O O   . ALA A 204 ? 1.764 2.341 1.720 0.415  0.092  -0.125 204 ALA BBB O   
1596  C CB  . ALA A 204 ? 1.668 2.273 1.643 0.396  0.119  -0.148 204 ALA BBB CB  
1597  N N   . LEU A 205 ? 1.674 2.263 1.619 0.384  0.086  -0.132 205 LEU BBB N   
1598  C CA  . LEU A 205 ? 1.614 2.169 1.530 0.384  0.082  -0.127 205 LEU BBB CA  
1599  C C   . LEU A 205 ? 1.658 2.218 1.569 0.396  0.064  -0.116 205 LEU BBB C   
1600  O O   . LEU A 205 ? 1.732 2.257 1.611 0.404  0.062  -0.108 205 LEU BBB O   
1601  C CB  . LEU A 205 ? 1.479 2.029 1.386 0.364  0.082  -0.133 205 LEU BBB CB  
1602  C CG  . LEU A 205 ? 1.557 2.062 1.440 0.358  0.096  -0.137 205 LEU BBB CG  
1603  C CD1 . LEU A 205 ? 1.596 2.081 1.482 0.366  0.112  -0.145 205 LEU BBB CD1 
1604  C CD2 . LEU A 205 ? 1.559 2.067 1.449 0.339  0.097  -0.147 205 LEU BBB CD2 
1605  N N   . GLY A 206 ? 1.628 2.229 1.568 0.398  0.050  -0.115 206 GLY BBB N   
1606  C CA  . GLY A 206 ? 1.726 2.339 1.670 0.410  0.027  -0.108 206 GLY BBB CA  
1607  C C   . GLY A 206 ? 1.876 2.492 1.804 0.397  0.011  -0.108 206 GLY BBB C   
1608  O O   . GLY A 206 ? 1.972 2.579 1.887 0.378  0.020  -0.114 206 GLY BBB O   
1609  N N   . PRO A 207 ? 1.920 2.546 1.847 0.408  -0.015 -0.104 207 PRO BBB N   
1610  C CA  . PRO A 207 ? 1.936 2.565 1.846 0.396  -0.032 -0.108 207 PRO BBB CA  
1611  C C   . PRO A 207 ? 2.023 2.596 1.865 0.392  -0.028 -0.103 207 PRO BBB C   
1612  O O   . PRO A 207 ? 2.073 2.604 1.880 0.405  -0.020 -0.094 207 PRO BBB O   
1613  C CB  . PRO A 207 ? 1.930 2.589 1.864 0.413  -0.065 -0.107 207 PRO BBB CB  
1614  C CG  . PRO A 207 ? 1.896 2.540 1.830 0.438  -0.066 -0.097 207 PRO BBB CG  
1615  C CD  . PRO A 207 ? 1.830 2.466 1.776 0.433  -0.032 -0.098 207 PRO BBB CD  
1616  N N   . GLY A 208 ? 2.048 2.619 1.875 0.373  -0.030 -0.109 208 GLY BBB N   
1617  C CA  . GLY A 208 ? 2.068 2.585 1.832 0.367  -0.023 -0.107 208 GLY BBB CA  
1618  C C   . GLY A 208 ? 2.015 2.496 1.766 0.355  0.011  -0.109 208 GLY BBB C   
1619  O O   . GLY A 208 ? 2.113 2.540 1.812 0.352  0.024  -0.106 208 GLY BBB O   
1620  N N   . ALA A 209 ? 1.783 2.289 1.578 0.348  0.025  -0.114 209 ALA BBB N   
1621  C CA  . ALA A 209 ? 1.706 2.184 1.499 0.337  0.052  -0.120 209 ALA BBB CA  
1622  C C   . ALA A 209 ? 1.677 2.142 1.462 0.315  0.061  -0.128 209 ALA BBB C   
1623  O O   . ALA A 209 ? 1.749 2.244 1.554 0.304  0.051  -0.133 209 ALA BBB O   
1624  C CB  . ALA A 209 ? 1.685 2.194 1.523 0.337  0.059  -0.125 209 ALA BBB CB  
1625  N N   . THR A 210 ? 1.606 2.021 1.364 0.309  0.083  -0.132 210 THR BBB N   
1626  C CA  . THR A 210 ? 1.516 1.913 1.272 0.288  0.098  -0.142 210 THR BBB CA  
1627  C C   . THR A 210 ? 1.457 1.882 1.268 0.277  0.105  -0.152 210 THR BBB C   
1628  O O   . THR A 210 ? 1.565 2.008 1.401 0.285  0.103  -0.152 210 THR BBB O   
1629  C CB  . THR A 210 ? 1.621 1.952 1.335 0.286  0.125  -0.143 210 THR BBB CB  
1630  O OG1 . THR A 210 ? 1.918 2.217 1.573 0.302  0.118  -0.129 210 THR BBB OG1 
1631  C CG2 . THR A 210 ? 1.744 2.048 1.448 0.264  0.143  -0.153 210 THR BBB CG2 
1632  N N   . LEU A 211 ? 1.375 1.799 1.201 0.259  0.112  -0.161 211 LEU BBB N   
1633  C CA  . LEU A 211 ? 1.328 1.774 1.204 0.250  0.115  -0.169 211 LEU BBB CA  
1634  C C   . LEU A 211 ? 1.440 1.864 1.329 0.253  0.131  -0.178 211 LEU BBB C   
1635  O O   . LEU A 211 ? 1.533 1.979 1.453 0.257  0.125  -0.182 211 LEU BBB O   
1636  C CB  . LEU A 211 ? 1.313 1.758 1.208 0.232  0.121  -0.178 211 LEU BBB CB  
1637  C CG  . LEU A 211 ? 1.256 1.745 1.179 0.228  0.105  -0.174 211 LEU BBB CG  
1638  C CD1 . LEU A 211 ? 1.269 1.780 1.172 0.236  0.088  -0.165 211 LEU BBB CD1 
1639  C CD2 . LEU A 211 ? 1.297 1.781 1.240 0.210  0.114  -0.182 211 LEU BBB CD2 
1640  N N   . GLU A 212 ? 1.620 1.996 1.484 0.250  0.153  -0.182 212 GLU BBB N   
1641  C CA  . GLU A 212 ? 1.633 1.984 1.514 0.251  0.172  -0.192 212 GLU BBB CA  
1642  C C   . GLU A 212 ? 1.642 2.010 1.523 0.269  0.162  -0.187 212 GLU BBB C   
1643  O O   . GLU A 212 ? 1.684 2.063 1.600 0.269  0.163  -0.198 212 GLU BBB O   
1644  C CB  . GLU A 212 ? 1.693 1.983 1.536 0.247  0.202  -0.194 212 GLU BBB CB  
1645  C CG  . GLU A 212 ? 1.849 2.115 1.659 0.235  0.210  -0.192 212 GLU BBB CG  
1646  C CD  . GLU A 212 ? 2.134 2.329 1.900 0.229  0.246  -0.195 212 GLU BBB CD  
1647  O OE1 . GLU A 212 ? 2.068 2.235 1.851 0.230  0.270  -0.204 212 GLU BBB OE1 
1648  O OE2 . GLU A 212 ? 2.246 2.410 1.957 0.225  0.251  -0.189 212 GLU BBB OE2 
1649  N N   . GLU A 213 ? 1.584 1.952 1.428 0.283  0.152  -0.171 213 GLU BBB N   
1650  C CA  . GLU A 213 ? 1.524 1.907 1.373 0.299  0.146  -0.167 213 GLU BBB CA  
1651  C C   . GLU A 213 ? 1.373 1.805 1.256 0.301  0.128  -0.170 213 GLU BBB C   
1652  O O   . GLU A 213 ? 1.390 1.830 1.292 0.306  0.130  -0.177 213 GLU BBB O   
1653  C CB  . GLU A 213 ? 1.622 1.998 1.432 0.316  0.137  -0.150 213 GLU BBB CB  
1654  C CG  . GLU A 213 ? 1.843 2.161 1.606 0.322  0.154  -0.143 213 GLU BBB CG  
1655  C CD  . GLU A 213 ? 2.020 2.335 1.742 0.340  0.135  -0.125 213 GLU BBB CD  
1656  O OE1 . GLU A 213 ? 1.912 2.271 1.646 0.341  0.109  -0.121 213 GLU BBB OE1 
1657  O OE2 . GLU A 213 ? 2.214 2.482 1.892 0.352  0.145  -0.115 213 GLU BBB OE2 
1658  N N   . MET A 214 ? 1.310 1.775 1.200 0.296  0.112  -0.164 214 MET BBB N   
1659  C CA  . MET A 214 ? 1.308 1.812 1.224 0.297  0.099  -0.165 214 MET BBB CA  
1660  C C   . MET A 214 ? 1.297 1.801 1.239 0.288  0.101  -0.179 214 MET BBB C   
1661  O O   . MET A 214 ? 1.448 1.966 1.400 0.294  0.096  -0.183 214 MET BBB O   
1662  C CB  A MET A 214 ? 1.307 1.841 1.226 0.294  0.085  -0.156 214 MET BBB CB  
1663  C CG  A MET A 214 ? 1.427 1.954 1.342 0.280  0.085  -0.157 214 MET BBB CG  
1664  S SD  A MET A 214 ? 1.477 2.044 1.402 0.279  0.069  -0.149 214 MET BBB SD  
1665  C CE  A MET A 214 ? 1.375 1.973 1.329 0.280  0.067  -0.148 214 MET BBB CE  
1666  N N   . MET A 215 ? 1.285 1.773 1.240 0.275  0.108  -0.187 215 MET BBB N   
1667  C CA  . MET A 215 ? 1.300 1.790 1.289 0.268  0.106  -0.201 215 MET BBB CA  
1668  C C   . MET A 215 ? 1.331 1.806 1.331 0.273  0.113  -0.215 215 MET BBB C   
1669  O O   . MET A 215 ? 1.492 1.980 1.513 0.275  0.102  -0.226 215 MET BBB O   
1670  C CB  . MET A 215 ? 1.325 1.800 1.334 0.253  0.115  -0.208 215 MET BBB CB  
1671  C CG  . MET A 215 ? 1.388 1.880 1.394 0.246  0.107  -0.198 215 MET BBB CG  
1672  S SD  . MET A 215 ? 1.497 1.994 1.551 0.233  0.104  -0.209 215 MET BBB SD  
1673  C CE  . MET A 215 ? 1.559 2.014 1.631 0.222  0.131  -0.227 215 MET BBB CE  
1674  N N   . THR A 216 ? 1.331 1.775 1.315 0.275  0.133  -0.217 216 THR BBB N   
1675  C CA  . THR A 216 ? 1.359 1.787 1.355 0.280  0.144  -0.231 216 THR BBB CA  
1676  C C   . THR A 216 ? 1.448 1.898 1.434 0.293  0.131  -0.227 216 THR BBB C   
1677  O O   . THR A 216 ? 1.578 2.033 1.583 0.294  0.127  -0.243 216 THR BBB O   
1678  C CB  . THR A 216 ? 1.386 1.770 1.359 0.281  0.171  -0.228 216 THR BBB CB  
1679  O OG1 . THR A 216 ? 1.454 1.811 1.432 0.267  0.187  -0.233 216 THR BBB OG1 
1680  C CG2 . THR A 216 ? 1.515 1.880 1.507 0.284  0.187  -0.245 216 THR BBB CG2 
1681  N N   . ALA A 217 ? 1.479 1.941 1.436 0.303  0.126  -0.209 217 ALA BBB N   
1682  C CA  . ALA A 217 ? 1.429 1.910 1.378 0.315  0.120  -0.205 217 ALA BBB CA  
1683  C C   . ALA A 217 ? 1.397 1.904 1.356 0.313  0.104  -0.212 217 ALA BBB C   
1684  O O   . ALA A 217 ? 1.472 1.982 1.429 0.319  0.103  -0.221 217 ALA BBB O   
1685  C CB  . ALA A 217 ? 1.349 1.843 1.278 0.324  0.115  -0.185 217 ALA BBB CB  
1686  N N   . CYS A 218 ? 1.347 1.869 1.313 0.305  0.091  -0.208 218 CYS BBB N   
1687  C CA  . CYS A 218 ? 1.398 1.938 1.364 0.305  0.075  -0.210 218 CYS BBB CA  
1688  C C   . CYS A 218 ? 1.570 2.103 1.559 0.300  0.065  -0.229 218 CYS BBB C   
1689  O O   . CYS A 218 ? 1.996 2.540 1.982 0.301  0.047  -0.229 218 CYS BBB O   
1690  C CB  . CYS A 218 ? 1.335 1.893 1.297 0.302  0.068  -0.194 218 CYS BBB CB  
1691  S SG  . CYS A 218 ? 1.421 1.997 1.365 0.309  0.073  -0.177 218 CYS BBB SG  
1692  N N   . GLN A 219 ? 1.535 2.049 1.549 0.295  0.075  -0.244 219 GLN BBB N   
1693  C CA  . GLN A 219 ? 1.464 1.976 1.513 0.290  0.065  -0.266 219 GLN BBB CA  
1694  C C   . GLN A 219 ? 1.476 1.988 1.519 0.298  0.055  -0.284 219 GLN BBB C   
1695  O O   . GLN A 219 ? 1.473 1.997 1.486 0.305  0.040  -0.279 219 GLN BBB O   
1696  C CB  . GLN A 219 ? 1.446 1.935 1.529 0.280  0.085  -0.279 219 GLN BBB CB  
1697  C CG  . GLN A 219 ? 1.534 2.002 1.621 0.282  0.104  -0.293 219 GLN BBB CG  
1698  C CD  . GLN A 219 ? 1.613 2.053 1.737 0.272  0.128  -0.310 219 GLN BBB CD  
1699  O OE1 . GLN A 219 ? 1.695 2.133 1.852 0.261  0.128  -0.317 219 GLN BBB OE1 
1700  N NE2 . GLN A 219 ? 1.660 2.073 1.780 0.273  0.153  -0.317 219 GLN BBB NE2 
1701  N N   . PRO B 1   ? 0.904 1.308 1.057 0.060  0.065  -0.157 1   PRO CCC N   
1702  C CA  . PRO B 1   ? 0.771 1.179 0.926 0.057  0.066  -0.157 1   PRO CCC CA  
1703  C C   . PRO B 1   ? 0.848 1.241 0.990 0.059  0.075  -0.159 1   PRO CCC C   
1704  O O   . PRO B 1   ? 0.948 1.327 1.080 0.064  0.081  -0.160 1   PRO CCC O   
1705  C CB  A PRO B 1   ? 0.900 1.330 1.076 0.058  0.066  -0.150 1   PRO CCC CB  
1706  C CG  A PRO B 1   ? 1.015 1.449 1.198 0.066  0.067  -0.147 1   PRO CCC CG  
1707  C CD  A PRO B 1   ? 0.946 1.364 1.114 0.064  0.064  -0.151 1   PRO CCC CD  
1708  N N   . ILE B 2   ? 0.872 1.266 1.011 0.055  0.077  -0.158 2   ILE CCC N   
1709  C CA  . ILE B 2   ? 0.967 1.346 1.091 0.056  0.086  -0.159 2   ILE CCC CA  
1710  C C   . ILE B 2   ? 0.971 1.369 1.111 0.057  0.097  -0.153 2   ILE CCC C   
1711  O O   . ILE B 2   ? 0.929 1.341 1.081 0.049  0.093  -0.150 2   ILE CCC O   
1712  C CB  . ILE B 2   ? 0.857 1.220 0.960 0.051  0.081  -0.163 2   ILE CCC CB  
1713  C CG1 . ILE B 2   ? 0.788 1.142 0.881 0.051  0.069  -0.170 2   ILE CCC CG1 
1714  C CG2 . ILE B 2   ? 1.089 1.432 1.171 0.053  0.091  -0.164 2   ILE CCC CG2 
1715  C CD1 . ILE B 2   ? 0.818 1.160 0.901 0.055  0.072  -0.174 2   ILE CCC CD1 
1716  N N   . VAL B 3   ? 0.973 1.370 1.113 0.065  0.110  -0.152 3   VAL CCC N   
1717  C CA  . VAL B 3   ? 1.108 1.529 1.268 0.067  0.121  -0.146 3   VAL CCC CA  
1718  C C   . VAL B 3   ? 1.239 1.649 1.383 0.070  0.137  -0.147 3   VAL CCC C   
1719  O O   . VAL B 3   ? 1.336 1.716 1.452 0.072  0.139  -0.151 3   VAL CCC O   
1720  C CB  . VAL B 3   ? 1.176 1.616 1.357 0.079  0.123  -0.143 3   VAL CCC CB  
1721  C CG1 . VAL B 3   ? 1.241 1.694 1.437 0.076  0.108  -0.142 3   VAL CCC CG1 
1722  C CG2 . VAL B 3   ? 1.129 1.543 1.290 0.092  0.127  -0.147 3   VAL CCC CG2 
1723  N N   . GLN B 4   ? 1.230 1.667 1.393 0.068  0.149  -0.142 4   GLN CCC N   
1724  C CA  A GLN B 4   ? 1.374 1.806 1.524 0.067  0.166  -0.141 4   GLN CCC CA  
1725  C C   . GLN B 4   ? 1.533 1.952 1.670 0.084  0.179  -0.144 4   GLN CCC C   
1726  O O   . GLN B 4   ? 1.773 2.174 1.886 0.084  0.192  -0.145 4   GLN CCC O   
1727  C CB  . GLN B 4   ? 1.438 1.909 1.618 0.058  0.175  -0.135 4   GLN CCC CB  
1728  C CG  . GLN B 4   ? 1.502 1.967 1.673 0.037  0.172  -0.132 4   GLN CCC CG  
1729  C CD  . GLN B 4   ? 1.587 2.026 1.726 0.032  0.187  -0.133 4   GLN CCC CD  
1730  O OE1 . GLN B 4   ? 1.432 1.869 1.563 0.043  0.203  -0.134 4   GLN CCC OE1 
1731  N NE2 . GLN B 4   ? 1.724 2.140 1.840 0.016  0.181  -0.131 4   GLN CCC NE2 
1732  N N   . ASN B 5   ? 1.488 1.911 1.635 0.099  0.177  -0.145 5   ASN CCC N   
1733  C CA  . ASN B 5   ? 1.619 2.031 1.754 0.117  0.190  -0.148 5   ASN CCC CA  
1734  C C   . ASN B 5   ? 1.799 2.243 1.952 0.124  0.210  -0.144 5   ASN CCC C   
1735  O O   . ASN B 5   ? 1.874 2.351 2.052 0.112  0.214  -0.140 5   ASN CCC O   
1736  C CB  . ASN B 5   ? 1.614 1.978 1.704 0.118  0.192  -0.154 5   ASN CCC CB  
1737  C CG  . ASN B 5   ? 1.718 2.058 1.789 0.136  0.198  -0.158 5   ASN CCC CG  
1738  O OD1 . ASN B 5   ? 1.840 2.198 1.929 0.152  0.204  -0.156 5   ASN CCC OD1 
1739  N ND2 . ASN B 5   ? 1.731 2.027 1.762 0.135  0.196  -0.164 5   ASN CCC ND2 
1740  N N   . LEU B 6   ? 1.955 2.390 2.097 0.144  0.224  -0.147 6   LEU CCC N   
1741  C CA  . LEU B 6   ? 1.852 2.320 2.012 0.152  0.246  -0.145 6   LEU CCC CA  
1742  C C   . LEU B 6   ? 1.816 2.267 1.948 0.142  0.261  -0.146 6   LEU CCC C   
1743  O O   . LEU B 6   ? 1.919 2.403 2.069 0.135  0.276  -0.142 6   LEU CCC O   
1744  C CB  . LEU B 6   ? 1.928 2.393 2.085 0.181  0.255  -0.148 6   LEU CCC CB  
1745  C CG  . LEU B 6   ? 1.993 2.464 2.167 0.191  0.238  -0.147 6   LEU CCC CG  
1746  C CD1 . LEU B 6   ? 2.035 2.488 2.196 0.221  0.244  -0.150 6   LEU CCC CD1 
1747  C CD2 . LEU B 6   ? 1.830 2.358 2.055 0.185  0.232  -0.141 6   LEU CCC CD2 
1748  N N   . GLN B 7   ? 1.807 2.206 1.894 0.140  0.257  -0.151 7   GLN CCC N   
1749  C CA  . GLN B 7   ? 1.893 2.266 1.946 0.128  0.264  -0.152 7   GLN CCC CA  
1750  C C   . GLN B 7   ? 1.904 2.273 1.958 0.105  0.247  -0.149 7   GLN CCC C   
1751  O O   . GLN B 7   ? 1.912 2.295 1.989 0.100  0.230  -0.148 7   GLN CCC O   
1752  C CB  . GLN B 7   ? 1.990 2.310 1.994 0.138  0.265  -0.159 7   GLN CCC CB  
1753  C CG  . GLN B 7   ? 2.132 2.447 2.131 0.163  0.277  -0.163 7   GLN CCC CG  
1754  C CD  . GLN B 7   ? 2.339 2.600 2.284 0.171  0.282  -0.170 7   GLN CCC CD  
1755  O OE1 . GLN B 7   ? 2.340 2.570 2.252 0.158  0.278  -0.172 7   GLN CCC OE1 
1756  N NE2 . GLN B 7   ? 2.454 2.700 2.387 0.193  0.290  -0.174 7   GLN CCC NE2 
1757  N N   . GLY B 8   ? 1.924 2.269 1.947 0.093  0.252  -0.148 8   GLY CCC N   
1758  C CA  . GLY B 8   ? 1.885 2.223 1.905 0.073  0.237  -0.146 8   GLY CCC CA  
1759  C C   . GLY B 8   ? 1.865 2.178 1.873 0.073  0.213  -0.151 8   GLY CCC C   
1760  O O   . GLY B 8   ? 1.849 2.161 1.860 0.060  0.199  -0.149 8   GLY CCC O   
1761  N N   . GLN B 9   ? 1.917 2.209 1.910 0.085  0.207  -0.157 9   GLN CCC N   
1762  C CA  . GLN B 9   ? 1.871 2.138 1.849 0.082  0.186  -0.162 9   GLN CCC CA  
1763  C C   . GLN B 9   ? 1.774 2.067 1.787 0.079  0.171  -0.161 9   GLN CCC C   
1764  O O   . GLN B 9   ? 1.721 2.042 1.764 0.086  0.175  -0.158 9   GLN CCC O   
1765  C CB  . GLN B 9   ? 1.842 2.079 1.794 0.094  0.185  -0.169 9   GLN CCC CB  
1766  C CG  . GLN B 9   ? 2.005 2.216 1.922 0.101  0.201  -0.172 9   GLN CCC CG  
1767  C CD  . GLN B 9   ? 2.178 2.367 2.078 0.116  0.206  -0.177 9   GLN CCC CD  
1768  O OE1 . GLN B 9   ? 2.318 2.503 2.207 0.127  0.225  -0.177 9   GLN CCC OE1 
1769  N NE2 . GLN B 9   ? 2.125 2.303 2.025 0.115  0.189  -0.182 9   GLN CCC NE2 
1770  N N   . MET B 10  ? 1.574 1.858 1.580 0.070  0.153  -0.163 10  MET CCC N   
1771  C CA  . MET B 10  ? 1.303 1.607 1.336 0.066  0.138  -0.162 10  MET CCC CA  
1772  C C   . MET B 10  ? 1.250 1.543 1.279 0.073  0.129  -0.168 10  MET CCC C   
1773  O O   . MET B 10  ? 1.217 1.486 1.222 0.072  0.121  -0.174 10  MET CCC O   
1774  C CB  . MET B 10  ? 1.226 1.524 1.251 0.056  0.125  -0.162 10  MET CCC CB  
1775  C CG  . MET B 10  ? 1.378 1.681 1.403 0.047  0.134  -0.156 10  MET CCC CG  
1776  S SD  . MET B 10  ? 1.359 1.708 1.430 0.043  0.140  -0.149 10  MET CCC SD  
1777  C CE  . MET B 10  ? 1.311 1.669 1.398 0.038  0.119  -0.150 10  MET CCC CE  
1778  N N   . VAL B 11  ? 1.171 1.483 1.225 0.078  0.129  -0.165 11  VAL CCC N   
1779  C CA  . VAL B 11  ? 1.125 1.424 1.173 0.081  0.123  -0.169 11  VAL CCC CA  
1780  C C   . VAL B 11  ? 1.107 1.426 1.179 0.078  0.112  -0.167 11  VAL CCC C   
1781  O O   . VAL B 11  ? 1.134 1.479 1.230 0.076  0.111  -0.162 11  VAL CCC O   
1782  C CB  . VAL B 11  ? 1.214 1.502 1.255 0.095  0.135  -0.169 11  VAL CCC CB  
1783  C CG1 . VAL B 11  ? 1.408 1.675 1.423 0.100  0.148  -0.172 11  VAL CCC CG1 
1784  C CG2 . VAL B 11  ? 1.216 1.534 1.288 0.103  0.142  -0.162 11  VAL CCC CG2 
1785  N N   . HIS B 12  ? 1.030 1.337 1.094 0.075  0.103  -0.172 12  HIS CCC N   
1786  C CA  . HIS B 12  ? 0.950 1.271 1.031 0.071  0.094  -0.170 12  HIS CCC CA  
1787  C C   . HIS B 12  ? 1.070 1.395 1.161 0.080  0.100  -0.165 12  HIS CCC C   
1788  O O   . HIS B 12  ? 1.123 1.429 1.200 0.089  0.108  -0.165 12  HIS CCC O   
1789  C CB  . HIS B 12  ? 1.010 1.319 1.079 0.063  0.085  -0.177 12  HIS CCC CB  
1790  C CG  . HIS B 12  ? 0.966 1.288 1.048 0.058  0.078  -0.175 12  HIS CCC CG  
1791  N ND1 . HIS B 12  ? 1.012 1.356 1.109 0.053  0.069  -0.175 12  HIS CCC ND1 
1792  C CD2 . HIS B 12  ? 0.973 1.287 1.053 0.057  0.078  -0.173 12  HIS CCC CD2 
1793  C CE1 . HIS B 12  ? 1.034 1.385 1.138 0.050  0.066  -0.174 12  HIS CCC CE1 
1794  N NE2 . HIS B 12  ? 1.105 1.438 1.199 0.051  0.071  -0.172 12  HIS CCC NE2 
1795  N N   . GLN B 13  ? 1.106 1.452 1.218 0.079  0.094  -0.160 13  GLN CCC N   
1796  C CA  . GLN B 13  ? 1.111 1.462 1.232 0.088  0.096  -0.155 13  GLN CCC CA  
1797  C C   . GLN B 13  ? 1.068 1.424 1.193 0.082  0.086  -0.154 13  GLN CCC C   
1798  O O   . GLN B 13  ? 1.001 1.372 1.136 0.073  0.079  -0.155 13  GLN CCC O   
1799  C CB  . GLN B 13  ? 1.151 1.529 1.295 0.097  0.101  -0.149 13  GLN CCC CB  
1800  C CG  . GLN B 13  ? 1.413 1.790 1.560 0.114  0.108  -0.146 13  GLN CCC CG  
1801  C CD  . GLN B 13  ? 1.516 1.927 1.689 0.121  0.115  -0.142 13  GLN CCC CD  
1802  O OE1 . GLN B 13  ? 1.474 1.910 1.666 0.111  0.111  -0.140 13  GLN CCC OE1 
1803  N NE2 . GLN B 13  ? 1.619 2.030 1.793 0.139  0.125  -0.141 13  GLN CCC NE2 
1804  N N   . CYS B 14  ? 1.239 1.579 1.355 0.086  0.086  -0.152 14  CYS CCC N   
1805  C CA  . CYS B 14  ? 1.287 1.628 1.403 0.080  0.078  -0.150 14  CYS CCC CA  
1806  C C   . CYS B 14  ? 1.299 1.669 1.438 0.082  0.073  -0.145 14  CYS CCC C   
1807  O O   . CYS B 14  ? 1.362 1.747 1.515 0.093  0.075  -0.141 14  CYS CCC O   
1808  C CB  . CYS B 14  ? 1.353 1.665 1.449 0.084  0.081  -0.148 14  CYS CCC CB  
1809  S SG  . CYS B 14  ? 1.656 1.932 1.723 0.076  0.085  -0.155 14  CYS CCC SG  
1810  N N   . ILE B 15  ? 1.177 1.556 1.318 0.073  0.065  -0.146 15  ILE CCC N   
1811  C CA  . ILE B 15  ? 1.059 1.459 1.216 0.075  0.059  -0.141 15  ILE CCC CA  
1812  C C   . ILE B 15  ? 1.018 1.412 1.173 0.087  0.058  -0.135 15  ILE CCC C   
1813  O O   . ILE B 15  ? 0.949 1.318 1.085 0.089  0.061  -0.133 15  ILE CCC O   
1814  C CB  . ILE B 15  ? 1.002 1.408 1.156 0.065  0.052  -0.144 15  ILE CCC CB  
1815  C CG1 . ILE B 15  ? 0.958 1.383 1.125 0.066  0.044  -0.140 15  ILE CCC CG1 
1816  C CG2 . ILE B 15  ? 1.052 1.439 1.189 0.060  0.053  -0.143 15  ILE CCC CG2 
1817  C CD1 . ILE B 15  ? 1.005 1.437 1.169 0.058  0.038  -0.144 15  ILE CCC CD1 
1818  N N   . SER B 16  ? 0.936 1.353 1.111 0.095  0.054  -0.130 16  SER CCC N   
1819  C CA  . SER B 16  ? 1.009 1.423 1.184 0.110  0.053  -0.125 16  SER CCC CA  
1820  C C   . SER B 16  ? 0.932 1.339 1.096 0.110  0.044  -0.120 16  SER CCC C   
1821  O O   . SER B 16  ? 0.934 1.353 1.102 0.100  0.037  -0.121 16  SER CCC O   
1822  C CB  . SER B 16  ? 1.066 1.513 1.269 0.120  0.053  -0.122 16  SER CCC CB  
1823  O OG  . SER B 16  ? 1.287 1.736 1.492 0.138  0.049  -0.117 16  SER CCC OG  
1824  N N   . PRO B 17  ? 1.011 1.398 1.160 0.122  0.044  -0.116 17  PRO CCC N   
1825  C CA  . PRO B 17  ? 0.998 1.376 1.133 0.124  0.035  -0.111 17  PRO CCC CA  
1826  C C   . PRO B 17  ? 0.992 1.402 1.149 0.127  0.023  -0.108 17  PRO CCC C   
1827  O O   . PRO B 17  ? 1.051 1.460 1.199 0.121  0.015  -0.107 17  PRO CCC O   
1828  C CB  . PRO B 17  ? 0.974 1.321 1.087 0.140  0.036  -0.106 17  PRO CCC CB  
1829  C CG  . PRO B 17  ? 0.914 1.241 1.018 0.140  0.048  -0.110 17  PRO CCC CG  
1830  C CD  . PRO B 17  ? 0.949 1.309 1.081 0.135  0.052  -0.115 17  PRO CCC CD  
1831  N N   . ARG B 18  ? 1.003 1.444 1.189 0.136  0.022  -0.108 18  ARG CCC N   
1832  C CA  . ARG B 18  ? 0.998 1.472 1.207 0.136  0.010  -0.106 18  ARG CCC CA  
1833  C C   . ARG B 18  ? 0.939 1.424 1.152 0.117  0.006  -0.110 18  ARG CCC C   
1834  O O   . ARG B 18  ? 1.052 1.542 1.262 0.114  -0.006 -0.109 18  ARG CCC O   
1835  C CB  . ARG B 18  ? 1.097 1.606 1.338 0.147  0.012  -0.106 18  ARG CCC CB  
1836  C CG  . ARG B 18  ? 1.269 1.801 1.525 0.162  -0.001 -0.101 18  ARG CCC CG  
1837  C CD  . ARG B 18  ? 1.458 2.018 1.741 0.180  0.004  -0.100 18  ARG CCC CD  
1838  N NE  . ARG B 18  ? 1.630 2.214 1.928 0.198  -0.010 -0.096 18  ARG CCC NE  
1839  C CZ  . ARG B 18  ? 1.748 2.307 2.024 0.219  -0.016 -0.092 18  ARG CCC CZ  
1840  N NH1 . ARG B 18  ? 1.711 2.219 1.948 0.223  -0.008 -0.091 18  ARG CCC NH1 
1841  N NH2 . ARG B 18  ? 1.807 2.391 2.097 0.235  -0.031 -0.089 18  ARG CCC NH2 
1842  N N   . THR B 19  ? 0.876 1.361 1.093 0.106  0.015  -0.116 19  THR CCC N   
1843  C CA  . THR B 19  ? 0.908 1.398 1.124 0.091  0.011  -0.120 19  THR CCC CA  
1844  C C   . THR B 19  ? 0.922 1.392 1.114 0.085  0.007  -0.121 19  THR CCC C   
1845  O O   . THR B 19  ? 0.953 1.429 1.142 0.080  -0.002 -0.122 19  THR CCC O   
1846  C CB  . THR B 19  ? 0.926 1.417 1.148 0.083  0.020  -0.125 19  THR CCC CB  
1847  O OG1 . THR B 19  ? 0.946 1.440 1.165 0.070  0.015  -0.129 19  THR CCC OG1 
1848  C CG2 . THR B 19  ? 1.026 1.493 1.230 0.084  0.031  -0.127 19  THR CCC CG2 
1849  N N   . LEU B 20  ? 0.913 1.358 1.085 0.085  0.016  -0.121 20  LEU CCC N   
1850  C CA  . LEU B 20  ? 0.932 1.361 1.082 0.078  0.015  -0.123 20  LEU CCC CA  
1851  C C   . LEU B 20  ? 1.034 1.461 1.174 0.083  0.005  -0.118 20  LEU CCC C   
1852  O O   . LEU B 20  ? 1.124 1.554 1.256 0.077  0.001  -0.120 20  LEU CCC O   
1853  C CB  . LEU B 20  ? 0.904 1.309 1.035 0.076  0.026  -0.123 20  LEU CCC CB  
1854  C CG  . LEU B 20  ? 1.018 1.421 1.153 0.068  0.034  -0.129 20  LEU CCC CG  
1855  C CD1 . LEU B 20  ? 0.979 1.355 1.096 0.068  0.042  -0.128 20  LEU CCC CD1 
1856  C CD2 . LEU B 20  ? 1.005 1.417 1.138 0.057  0.034  -0.135 20  LEU CCC CD2 
1857  N N   . ASN B 21  ? 1.091 1.513 1.229 0.096  0.002  -0.111 21  ASN CCC N   
1858  C CA  . ASN B 21  ? 1.132 1.549 1.257 0.102  -0.009 -0.106 21  ASN CCC CA  
1859  C C   . ASN B 21  ? 1.119 1.563 1.262 0.099  -0.022 -0.108 21  ASN CCC C   
1860  O O   . ASN B 21  ? 1.203 1.641 1.330 0.096  -0.030 -0.108 21  ASN CCC O   
1861  C CB  . ASN B 21  ? 1.171 1.578 1.292 0.119  -0.012 -0.099 21  ASN CCC CB  
1862  C CG  . ASN B 21  ? 1.292 1.688 1.393 0.127  -0.024 -0.093 21  ASN CCC CG  
1863  O OD1 . ASN B 21  ? 1.403 1.787 1.484 0.119  -0.027 -0.094 21  ASN CCC OD1 
1864  N ND2 . ASN B 21  ? 1.402 1.801 1.508 0.146  -0.033 -0.088 21  ASN CCC ND2 
1865  N N   . ALA B 22  ? 0.972 1.442 1.144 0.099  -0.023 -0.110 22  ALA CCC N   
1866  C CA  . ALA B 22  ? 0.959 1.453 1.147 0.093  -0.035 -0.112 22  ALA CCC CA  
1867  C C   . ALA B 22  ? 0.947 1.432 1.121 0.080  -0.036 -0.118 22  ALA CCC C   
1868  O O   . ALA B 22  ? 0.995 1.482 1.161 0.077  -0.048 -0.118 22  ALA CCC O   
1869  C CB  . ALA B 22  ? 0.984 1.505 1.204 0.091  -0.032 -0.113 22  ALA CCC CB  
1870  N N   . TRP B 23  ? 0.860 1.335 1.028 0.074  -0.024 -0.122 23  TRP CCC N   
1871  C CA  . TRP B 23  ? 0.839 1.308 0.994 0.065  -0.025 -0.129 23  TRP CCC CA  
1872  C C   . TRP B 23  ? 0.926 1.380 1.055 0.066  -0.027 -0.128 23  TRP CCC C   
1873  O O   . TRP B 23  ? 0.953 1.404 1.069 0.063  -0.035 -0.131 23  TRP CCC O   
1874  C CB  . TRP B 23  ? 0.787 1.251 0.943 0.060  -0.013 -0.134 23  TRP CCC CB  
1875  C CG  . TRP B 23  ? 0.763 1.223 0.905 0.055  -0.012 -0.141 23  TRP CCC CG  
1876  C CD1 . TRP B 23  ? 0.810 1.263 0.941 0.053  -0.004 -0.145 23  TRP CCC CD1 
1877  C CD2 . TRP B 23  ? 0.775 1.236 0.914 0.052  -0.021 -0.145 23  TRP CCC CD2 
1878  N NE1 . TRP B 23  ? 0.831 1.284 0.953 0.052  -0.006 -0.151 23  TRP CCC NE1 
1879  C CE2 . TRP B 23  ? 0.757 1.212 0.881 0.051  -0.017 -0.152 23  TRP CCC CE2 
1880  C CE3 . TRP B 23  ? 0.874 1.341 1.021 0.048  -0.032 -0.145 23  TRP CCC CE3 
1881  C CZ2 . TRP B 23  ? 0.769 1.219 0.882 0.050  -0.024 -0.158 23  TRP CCC CZ2 
1882  C CZ3 . TRP B 23  ? 0.845 1.305 0.980 0.044  -0.039 -0.151 23  TRP CCC CZ3 
1883  C CH2 . TRP B 23  ? 0.794 1.243 0.910 0.047  -0.035 -0.157 23  TRP CCC CH2 
1884  N N   . VAL B 24  ? 0.928 1.367 1.043 0.070  -0.019 -0.124 24  VAL CCC N   
1885  C CA  . VAL B 24  ? 0.956 1.378 1.042 0.070  -0.019 -0.122 24  VAL CCC CA  
1886  C C   . VAL B 24  ? 1.014 1.436 1.092 0.075  -0.034 -0.119 24  VAL CCC C   
1887  O O   . VAL B 24  ? 1.106 1.521 1.163 0.073  -0.038 -0.121 24  VAL CCC O   
1888  C CB  . VAL B 24  ? 0.983 1.386 1.055 0.071  -0.009 -0.117 24  VAL CCC CB  
1889  C CG1 . VAL B 24  ? 1.115 1.497 1.154 0.072  -0.010 -0.112 24  VAL CCC CG1 
1890  C CG2 . VAL B 24  ? 1.052 1.453 1.125 0.062  0.006  -0.122 24  VAL CCC CG2 
1891  N N   . LYS B 25  ? 1.030 1.462 1.124 0.083  -0.044 -0.114 25  LYS CCC N   
1892  C CA  . LYS B 25  ? 1.055 1.489 1.142 0.088  -0.061 -0.110 25  LYS CCC CA  
1893  C C   . LYS B 25  ? 1.066 1.512 1.159 0.081  -0.072 -0.116 25  LYS CCC C   
1894  O O   . LYS B 25  ? 1.194 1.632 1.266 0.081  -0.083 -0.116 25  LYS CCC O   
1895  C CB  . LYS B 25  ? 1.092 1.539 1.198 0.100  -0.068 -0.104 25  LYS CCC CB  
1896  C CG  . LYS B 25  ? 1.152 1.578 1.244 0.111  -0.061 -0.098 25  LYS CCC CG  
1897  C CD  . LYS B 25  ? 1.353 1.745 1.402 0.110  -0.059 -0.095 25  LYS CCC CD  
1898  C CE  . LYS B 25  ? 1.500 1.863 1.528 0.117  -0.049 -0.088 25  LYS CCC CE  
1899  N NZ  . LYS B 25  ? 1.641 1.971 1.626 0.113  -0.045 -0.085 25  LYS CCC NZ  
1900  N N   . VAL B 26  ? 0.986 1.450 1.104 0.073  -0.070 -0.121 26  VAL CCC N   
1901  C CA  . VAL B 26  ? 1.002 1.472 1.121 0.065  -0.081 -0.126 26  VAL CCC CA  
1902  C C   . VAL B 26  ? 1.122 1.571 1.210 0.062  -0.079 -0.132 26  VAL CCC C   
1903  O O   . VAL B 26  ? 1.299 1.740 1.370 0.059  -0.091 -0.135 26  VAL CCC O   
1904  C CB  . VAL B 26  ? 0.928 1.414 1.074 0.056  -0.077 -0.130 26  VAL CCC CB  
1905  C CG1 . VAL B 26  ? 1.086 1.596 1.262 0.060  -0.078 -0.124 26  VAL CCC CG1 
1906  C CG2 . VAL B 26  ? 0.971 1.448 1.113 0.054  -0.061 -0.134 26  VAL CCC CG2 
1907  N N   . VAL B 27  ? 1.070 1.510 1.149 0.063  -0.063 -0.134 27  VAL CCC N   
1908  C CA  . VAL B 27  ? 1.136 1.561 1.187 0.062  -0.058 -0.140 27  VAL CCC CA  
1909  C C   . VAL B 27  ? 1.218 1.628 1.240 0.067  -0.064 -0.136 27  VAL CCC C   
1910  O O   . VAL B 27  ? 1.235 1.634 1.233 0.067  -0.069 -0.140 27  VAL CCC O   
1911  C CB  . VAL B 27  ? 1.043 1.469 1.096 0.061  -0.040 -0.143 27  VAL CCC CB  
1912  C CG1 . VAL B 27  ? 1.123 1.541 1.151 0.061  -0.034 -0.148 27  VAL CCC CG1 
1913  C CG2 . VAL B 27  ? 0.945 1.382 1.021 0.057  -0.038 -0.147 27  VAL CCC CG2 
1914  N N   . GLU B 28  ? 1.237 1.643 1.257 0.071  -0.062 -0.128 28  GLU CCC N   
1915  C CA  . GLU B 28  ? 1.271 1.658 1.259 0.076  -0.067 -0.123 28  GLU CCC CA  
1916  C C   . GLU B 28  ? 1.326 1.714 1.308 0.078  -0.089 -0.123 28  GLU CCC C   
1917  O O   . GLU B 28  ? 1.564 1.935 1.514 0.080  -0.095 -0.124 28  GLU CCC O   
1918  C CB  . GLU B 28  ? 1.323 1.701 1.308 0.082  -0.063 -0.113 28  GLU CCC CB  
1919  C CG  . GLU B 28  ? 1.499 1.865 1.474 0.078  -0.043 -0.112 28  GLU CCC CG  
1920  C CD  . GLU B 28  ? 1.686 2.035 1.651 0.084  -0.040 -0.103 28  GLU CCC CD  
1921  O OE1 . GLU B 28  ? 1.761 2.111 1.732 0.094  -0.054 -0.098 28  GLU CCC OE1 
1922  O OE2 . GLU B 28  ? 1.769 2.103 1.721 0.078  -0.025 -0.101 28  GLU CCC OE2 
1923  N N   . GLU B 29  ? 1.315 1.723 1.328 0.078  -0.100 -0.122 29  GLU CCC N   
1924  C CA  . GLU B 29  ? 1.364 1.776 1.374 0.078  -0.123 -0.122 29  GLU CCC CA  
1925  C C   . GLU B 29  ? 1.359 1.771 1.365 0.068  -0.131 -0.131 29  GLU CCC C   
1926  O O   . GLU B 29  ? 1.596 1.995 1.578 0.067  -0.146 -0.133 29  GLU CCC O   
1927  C CB  . GLU B 29  ? 1.451 1.891 1.499 0.080  -0.132 -0.118 29  GLU CCC CB  
1928  C CG  . GLU B 29  ? 1.686 2.125 1.736 0.094  -0.130 -0.109 29  GLU CCC CG  
1929  C CD  . GLU B 29  ? 1.783 2.254 1.876 0.097  -0.132 -0.107 29  GLU CCC CD  
1930  O OE1 . GLU B 29  ? 1.710 2.208 1.831 0.088  -0.140 -0.110 29  GLU CCC OE1 
1931  O OE2 . GLU B 29  ? 1.782 2.252 1.880 0.109  -0.125 -0.101 29  GLU CCC OE2 
1932  N N   . LYS B 30  ? 1.198 1.617 1.221 0.061  -0.121 -0.136 30  LYS CCC N   
1933  C CA  . LYS B 30  ? 1.257 1.670 1.274 0.052  -0.129 -0.144 30  LYS CCC CA  
1934  C C   . LYS B 30  ? 1.263 1.657 1.256 0.053  -0.117 -0.152 30  LYS CCC C   
1935  O O   . LYS B 30  ? 1.280 1.661 1.259 0.049  -0.124 -0.159 30  LYS CCC O   
1936  C CB  . LYS B 30  ? 1.287 1.722 1.341 0.043  -0.131 -0.144 30  LYS CCC CB  
1937  C CG  . LYS B 30  ? 1.358 1.818 1.439 0.041  -0.144 -0.138 30  LYS CCC CG  
1938  C CD  . LYS B 30  ? 1.502 1.984 1.616 0.028  -0.148 -0.139 30  LYS CCC CD  
1939  C CE  . LYS B 30  ? 1.618 2.127 1.755 0.024  -0.167 -0.136 30  LYS CCC CE  
1940  N NZ  . LYS B 30  ? 1.647 2.177 1.811 0.007  -0.171 -0.138 30  LYS CCC NZ  
1941  N N   . ALA B 31  ? 1.424 1.816 1.411 0.060  -0.099 -0.151 31  ALA CCC N   
1942  C CA  . ALA B 31  ? 1.456 1.839 1.427 0.062  -0.086 -0.158 31  ALA CCC CA  
1943  C C   . ALA B 31  ? 1.469 1.855 1.455 0.058  -0.085 -0.165 31  ALA CCC C   
1944  O O   . ALA B 31  ? 1.500 1.901 1.515 0.054  -0.081 -0.162 31  ALA CCC O   
1945  C CB  . ALA B 31  ? 1.523 1.885 1.455 0.067  -0.091 -0.163 31  ALA CCC CB  
1946  N N   . PHE B 32  ? 1.294 1.664 1.257 0.060  -0.090 -0.173 32  PHE CCC N   
1947  C CA  . PHE B 32  ? 1.243 1.606 1.210 0.057  -0.091 -0.179 32  PHE CCC CA  
1948  C C   . PHE B 32  ? 1.245 1.590 1.198 0.049  -0.110 -0.182 32  PHE CCC C   
1949  O O   . PHE B 32  ? 1.302 1.625 1.234 0.050  -0.114 -0.190 32  PHE CCC O   
1950  C CB  . PHE B 32  ? 1.221 1.579 1.172 0.067  -0.080 -0.188 32  PHE CCC CB  
1951  C CG  . PHE B 32  ? 1.184 1.563 1.154 0.071  -0.062 -0.186 32  PHE CCC CG  
1952  C CD1 . PHE B 32  ? 1.215 1.607 1.212 0.068  -0.056 -0.184 32  PHE CCC CD1 
1953  C CD2 . PHE B 32  ? 1.257 1.641 1.215 0.076  -0.051 -0.185 32  PHE CCC CD2 
1954  C CE1 . PHE B 32  ? 1.323 1.733 1.336 0.069  -0.041 -0.183 32  PHE CCC CE1 
1955  C CE2 . PHE B 32  ? 1.314 1.717 1.289 0.075  -0.036 -0.183 32  PHE CCC CE2 
1956  C CZ  . PHE B 32  ? 1.367 1.783 1.370 0.072  -0.031 -0.182 32  PHE CCC CZ  
1957  N N   . SER B 33  ? 1.224 1.577 1.188 0.040  -0.123 -0.176 33  SER CCC N   
1958  C CA  . SER B 33  ? 1.295 1.639 1.257 0.027  -0.141 -0.177 33  SER CCC CA  
1959  C C   . SER B 33  ? 1.241 1.591 1.226 0.018  -0.137 -0.177 33  SER CCC C   
1960  O O   . SER B 33  ? 1.308 1.678 1.320 0.020  -0.123 -0.173 33  SER CCC O   
1961  C CB  . SER B 33  ? 1.435 1.797 1.412 0.021  -0.154 -0.170 33  SER CCC CB  
1962  O OG  . SER B 33  ? 1.619 1.970 1.569 0.030  -0.160 -0.170 33  SER CCC OG  
1963  N N   . PRO B 34  ? 1.188 1.517 1.158 0.007  -0.148 -0.182 34  PRO CCC N   
1964  C CA  . PRO B 34  ? 1.216 1.540 1.197 -0.002 -0.142 -0.182 34  PRO CCC CA  
1965  C C   . PRO B 34  ? 1.152 1.511 1.177 -0.011 -0.136 -0.174 34  PRO CCC C   
1966  O O   . PRO B 34  ? 1.175 1.537 1.212 -0.011 -0.124 -0.173 34  PRO CCC O   
1967  C CB  . PRO B 34  ? 1.336 1.630 1.291 -0.017 -0.159 -0.187 34  PRO CCC CB  
1968  C CG  . PRO B 34  ? 1.319 1.612 1.263 -0.019 -0.175 -0.187 34  PRO CCC CG  
1969  C CD  . PRO B 34  ? 1.259 1.560 1.196 0.001  -0.166 -0.187 34  PRO CCC CD  
1970  N N   . GLU B 35  ? 1.249 1.636 1.299 -0.017 -0.143 -0.168 35  GLU CCC N   
1971  C CA  . GLU B 35  ? 1.215 1.637 1.307 -0.023 -0.137 -0.161 35  GLU CCC CA  
1972  C C   . GLU B 35  ? 1.129 1.567 1.238 -0.008 -0.118 -0.157 35  GLU CCC C   
1973  O O   . GLU B 35  ? 1.134 1.595 1.273 -0.011 -0.110 -0.152 35  GLU CCC O   
1974  C CB  . GLU B 35  ? 1.312 1.763 1.426 -0.028 -0.150 -0.156 35  GLU CCC CB  
1975  C CG  . GLU B 35  ? 1.350 1.810 1.462 -0.012 -0.152 -0.153 35  GLU CCC CG  
1976  C CD  . GLU B 35  ? 1.426 1.858 1.498 -0.009 -0.166 -0.158 35  GLU CCC CD  
1977  O OE1 . GLU B 35  ? 1.459 1.861 1.503 -0.015 -0.170 -0.165 35  GLU CCC OE1 
1978  O OE2 . GLU B 35  ? 1.430 1.868 1.498 0.000  -0.173 -0.155 35  GLU CCC OE2 
1979  N N   . VAL B 36  ? 1.027 1.451 1.115 0.006  -0.112 -0.160 36  VAL CCC N   
1980  C CA  . VAL B 36  ? 0.994 1.430 1.096 0.017  -0.095 -0.157 36  VAL CCC CA  
1981  C C   . VAL B 36  ? 0.998 1.429 1.104 0.015  -0.084 -0.160 36  VAL CCC C   
1982  O O   . VAL B 36  ? 0.981 1.426 1.107 0.018  -0.071 -0.156 36  VAL CCC O   
1983  C CB  A VAL B 36  ? 0.998 1.422 1.076 0.030  -0.091 -0.160 36  VAL CCC CB  
1984  C CG1 A VAL B 36  ? 1.074 1.505 1.160 0.038  -0.073 -0.159 36  VAL CCC CG1 
1985  C CG2 A VAL B 36  ? 1.023 1.453 1.098 0.033  -0.100 -0.155 36  VAL CCC CG2 
1986  N N   . ILE B 37  ? 0.974 1.381 1.059 0.011  -0.088 -0.166 37  ILE CCC N   
1987  C CA  . ILE B 37  ? 0.948 1.346 1.032 0.010  -0.079 -0.168 37  ILE CCC CA  
1988  C C   . ILE B 37  ? 0.942 1.356 1.052 -0.001 -0.074 -0.162 37  ILE CCC C   
1989  O O   . ILE B 37  ? 0.925 1.346 1.047 0.004  -0.062 -0.161 37  ILE CCC O   
1990  C CB  . ILE B 37  ? 0.969 1.332 1.018 0.010  -0.087 -0.176 37  ILE CCC CB  
1991  C CG1 . ILE B 37  ? 0.988 1.339 1.012 0.024  -0.089 -0.182 37  ILE CCC CG1 
1992  C CG2 . ILE B 37  ? 1.016 1.365 1.059 0.012  -0.079 -0.178 37  ILE CCC CG2 
1993  C CD1 . ILE B 37  ? 1.119 1.435 1.108 0.029  -0.095 -0.191 37  ILE CCC CD1 
1994  N N   . PRO B 38  ? 0.961 1.382 1.081 -0.016 -0.083 -0.159 38  PRO CCC N   
1995  C CA  A PRO B 38  ? 0.957 1.401 1.107 -0.025 -0.075 -0.153 38  PRO CCC CA  
1996  C C   . PRO B 38  ? 0.939 1.413 1.117 -0.014 -0.065 -0.148 38  PRO CCC C   
1997  O O   . PRO B 38  ? 0.977 1.459 1.169 -0.014 -0.052 -0.146 38  PRO CCC O   
1998  C CB  A PRO B 38  ? 0.985 1.441 1.146 -0.043 -0.088 -0.151 38  PRO CCC CB  
1999  C CG  A PRO B 38  ? 1.020 1.450 1.150 -0.043 -0.104 -0.156 38  PRO CCC CG  
2000  C CD  A PRO B 38  ? 1.004 1.405 1.104 -0.028 -0.099 -0.162 38  PRO CCC CD  
2001  N N   . MET B 39  ? 0.944 1.430 1.127 -0.005 -0.070 -0.146 39  MET CCC N   
2002  C CA  . MET B 39  ? 0.942 1.449 1.145 0.006  -0.061 -0.141 39  MET CCC CA  
2003  C C   . MET B 39  ? 0.917 1.412 1.113 0.016  -0.046 -0.143 39  MET CCC C   
2004  O O   . MET B 39  ? 0.956 1.463 1.168 0.020  -0.035 -0.140 39  MET CCC O   
2005  C CB  . MET B 39  ? 0.966 1.478 1.166 0.015  -0.070 -0.139 39  MET CCC CB  
2006  C CG  . MET B 39  ? 0.980 1.510 1.198 0.028  -0.063 -0.134 39  MET CCC CG  
2007  S SD  . MET B 39  ? 1.015 1.584 1.272 0.026  -0.067 -0.128 39  MET CCC SD  
2008  C CE  . MET B 39  ? 1.308 1.884 1.560 0.024  -0.090 -0.127 39  MET CCC CE  
2009  N N   . PHE B 40  ? 0.898 1.371 1.069 0.019  -0.047 -0.149 40  PHE CCC N   
2010  C CA  . PHE B 40  ? 0.886 1.351 1.050 0.026  -0.035 -0.152 40  PHE CCC CA  
2011  C C   . PHE B 40  ? 0.885 1.348 1.055 0.021  -0.027 -0.152 40  PHE CCC C   
2012  O O   . PHE B 40  ? 0.895 1.362 1.074 0.026  -0.016 -0.150 40  PHE CCC O   
2013  C CB  . PHE B 40  ? 0.909 1.355 1.048 0.031  -0.038 -0.159 40  PHE CCC CB  
2014  C CG  . PHE B 40  ? 0.866 1.308 1.000 0.037  -0.028 -0.163 40  PHE CCC CG  
2015  C CD1 . PHE B 40  ? 0.858 1.308 0.997 0.042  -0.019 -0.162 40  PHE CCC CD1 
2016  C CD2 . PHE B 40  ? 0.858 1.286 0.980 0.037  -0.028 -0.168 40  PHE CCC CD2 
2017  C CE1 . PHE B 40  ? 0.850 1.299 0.986 0.046  -0.011 -0.166 40  PHE CCC CE1 
2018  C CE2 . PHE B 40  ? 0.848 1.275 0.968 0.043  -0.021 -0.173 40  PHE CCC CE2 
2019  C CZ  . PHE B 40  ? 0.843 1.283 0.972 0.047  -0.013 -0.172 40  PHE CCC CZ  
2020  N N   . SER B 41  ? 0.886 1.338 1.049 0.011  -0.033 -0.153 41  SER CCC N   
2021  C CA  . SER B 41  ? 0.895 1.341 1.058 0.006  -0.025 -0.153 41  SER CCC CA  
2022  C C   . SER B 41  ? 0.934 1.404 1.125 0.003  -0.015 -0.147 41  SER CCC C   
2023  O O   . SER B 41  ? 1.011 1.479 1.203 0.006  -0.004 -0.146 41  SER CCC O   
2024  C CB  . SER B 41  ? 0.922 1.348 1.068 -0.007 -0.033 -0.154 41  SER CCC CB  
2025  O OG  . SER B 41  ? 1.146 1.564 1.291 -0.015 -0.025 -0.153 41  SER CCC OG  
2026  N N   . ALA B 42  ? 0.913 1.406 1.125 -0.000 -0.020 -0.142 42  ALA CCC N   
2027  C CA  . ALA B 42  ? 0.902 1.423 1.142 0.001  -0.011 -0.137 42  ALA CCC CA  
2028  C C   . ALA B 42  ? 0.877 1.402 1.122 0.017  -0.002 -0.136 42  ALA CCC C   
2029  O O   . ALA B 42  ? 0.925 1.455 1.178 0.021  0.010  -0.134 42  ALA CCC O   
2030  C CB  . ALA B 42  ? 0.931 1.480 1.194 -0.005 -0.020 -0.133 42  ALA CCC CB  
2031  N N   . LEU B 43  ? 0.859 1.378 1.095 0.025  -0.008 -0.137 43  LEU CCC N   
2032  C CA  . LEU B 43  ? 0.869 1.385 1.103 0.038  -0.001 -0.135 43  LEU CCC CA  
2033  C C   . LEU B 43  ? 0.862 1.360 1.082 0.040  0.009  -0.140 43  LEU CCC C   
2034  O O   . LEU B 43  ? 0.935 1.430 1.156 0.047  0.018  -0.139 43  LEU CCC O   
2035  C CB  . LEU B 43  ? 0.883 1.394 1.107 0.044  -0.009 -0.135 43  LEU CCC CB  
2036  C CG  . LEU B 43  ? 0.902 1.432 1.140 0.047  -0.019 -0.130 43  LEU CCC CG  
2037  C CD1 . LEU B 43  ? 0.910 1.427 1.128 0.052  -0.027 -0.130 43  LEU CCC CD1 
2038  C CD2 . LEU B 43  ? 0.913 1.460 1.171 0.057  -0.013 -0.125 43  LEU CCC CD2 
2039  N N   . SER B 44  ? 0.845 1.328 1.050 0.033  0.007  -0.144 44  SER CCC N   
2040  C CA  . SER B 44  ? 0.834 1.301 1.025 0.036  0.014  -0.149 44  SER CCC CA  
2041  C C   . SER B 44  ? 0.849 1.311 1.039 0.031  0.020  -0.149 44  SER CCC C   
2042  O O   . SER B 44  ? 0.887 1.332 1.061 0.031  0.021  -0.154 44  SER CCC O   
2043  C CB  . SER B 44  ? 0.820 1.274 0.993 0.036  0.007  -0.155 44  SER CCC CB  
2044  O OG  . SER B 44  ? 0.824 1.271 0.989 0.029  -0.001 -0.157 44  SER CCC OG  
2045  N N   . CYS B 45  ? 0.892 1.368 1.098 0.027  0.024  -0.144 45  CYS CCC N   
2046  C CA  . CYS B 45  ? 0.898 1.371 1.103 0.021  0.033  -0.143 45  CYS CCC CA  
2047  C C   . CYS B 45  ? 0.900 1.361 1.096 0.029  0.044  -0.145 45  CYS CCC C   
2048  O O   . CYS B 45  ? 0.867 1.335 1.071 0.038  0.049  -0.144 45  CYS CCC O   
2049  C CB  . CYS B 45  ? 0.894 1.393 1.124 0.016  0.038  -0.137 45  CYS CCC CB  
2050  S SG  . CYS B 45  ? 1.148 1.645 1.376 0.005  0.051  -0.135 45  CYS CCC SG  
2051  N N   . GLY B 46  ? 0.934 1.374 1.110 0.026  0.046  -0.149 46  GLY CCC N   
2052  C CA  . GLY B 46  ? 0.883 1.309 1.046 0.033  0.054  -0.151 46  GLY CCC CA  
2053  C C   . GLY B 46  ? 0.864 1.284 1.021 0.040  0.049  -0.156 46  GLY CCC C   
2054  O O   . GLY B 46  ? 0.871 1.281 1.019 0.044  0.055  -0.159 46  GLY CCC O   
2055  N N   . ALA B 47  ? 0.910 1.336 1.069 0.040  0.040  -0.158 47  ALA CCC N   
2056  C CA  . ALA B 47  ? 0.875 1.299 1.030 0.044  0.038  -0.162 47  ALA CCC CA  
2057  C C   . ALA B 47  ? 0.874 1.285 1.013 0.045  0.035  -0.169 47  ALA CCC C   
2058  O O   . ALA B 47  ? 0.847 1.249 0.975 0.044  0.031  -0.172 47  ALA CCC O   
2059  C CB  . ALA B 47  ? 0.843 1.276 1.003 0.043  0.029  -0.163 47  ALA CCC CB  
2060  N N   . THR B 48  ? 0.862 1.271 0.999 0.046  0.038  -0.172 48  THR CCC N   
2061  C CA  . THR B 48  ? 0.858 1.262 0.984 0.047  0.033  -0.180 48  THR CCC CA  
2062  C C   . THR B 48  ? 0.911 1.329 1.042 0.047  0.026  -0.184 48  THR CCC C   
2063  O O   . THR B 48  ? 1.051 1.479 1.191 0.046  0.026  -0.180 48  THR CCC O   
2064  C CB  . THR B 48  ? 0.862 1.261 0.985 0.045  0.038  -0.182 48  THR CCC CB  
2065  O OG1 . THR B 48  ? 0.847 1.252 0.978 0.043  0.041  -0.180 48  THR CCC OG1 
2066  C CG2 . THR B 48  ? 0.884 1.268 1.000 0.047  0.047  -0.179 48  THR CCC CG2 
2067  N N   . PRO B 49  ? 0.864 1.285 0.988 0.050  0.019  -0.192 49  PRO CCC N   
2068  C CA  . PRO B 49  ? 0.832 1.271 0.963 0.051  0.015  -0.196 49  PRO CCC CA  
2069  C C   . PRO B 49  ? 0.849 1.300 0.990 0.045  0.021  -0.194 49  PRO CCC C   
2070  O O   . PRO B 49  ? 0.907 1.368 1.051 0.045  0.020  -0.193 49  PRO CCC O   
2071  C CB  . PRO B 49  ? 0.842 1.285 0.967 0.056  0.008  -0.206 49  PRO CCC CB  
2072  C CG  . PRO B 49  ? 0.857 1.278 0.966 0.059  0.005  -0.205 49  PRO CCC CG  
2073  C CD  . PRO B 49  ? 0.858 1.267 0.968 0.053  0.015  -0.196 49  PRO CCC CD  
2074  N N   . GLN B 50  ? 0.854 1.299 0.994 0.039  0.026  -0.194 50  GLN CCC N   
2075  C CA  . GLN B 50  ? 0.884 1.332 1.028 0.032  0.032  -0.191 50  GLN CCC CA  
2076  C C   . GLN B 50  ? 0.897 1.341 1.043 0.034  0.035  -0.182 50  GLN CCC C   
2077  O O   . GLN B 50  ? 0.940 1.390 1.086 0.031  0.037  -0.180 50  GLN CCC O   
2078  C CB  . GLN B 50  ? 0.921 1.353 1.058 0.026  0.037  -0.191 50  GLN CCC CB  
2079  C CG  . GLN B 50  ? 1.047 1.477 1.182 0.017  0.043  -0.189 50  GLN CCC CG  
2080  C CD  . GLN B 50  ? 1.103 1.510 1.226 0.011  0.047  -0.189 50  GLN CCC CD  
2081  O OE1 . GLN B 50  ? 1.134 1.522 1.250 0.018  0.051  -0.184 50  GLN CCC OE1 
2082  N NE2 . GLN B 50  ? 1.243 1.651 1.362 -0.001 0.048  -0.194 50  GLN CCC NE2 
2083  N N   . ASP B 51  ? 0.942 1.375 1.087 0.039  0.036  -0.177 51  ASP CCC N   
2084  C CA  . ASP B 51  ? 0.874 1.307 1.024 0.041  0.037  -0.169 51  ASP CCC CA  
2085  C C   . ASP B 51  ? 0.845 1.289 0.998 0.043  0.031  -0.169 51  ASP CCC C   
2086  O O   . ASP B 51  ? 0.885 1.332 1.038 0.043  0.030  -0.165 51  ASP CCC O   
2087  C CB  . ASP B 51  ? 0.897 1.324 1.051 0.046  0.040  -0.165 51  ASP CCC CB  
2088  C CG  . ASP B 51  ? 1.013 1.426 1.161 0.047  0.048  -0.164 51  ASP CCC CG  
2089  O OD1 . ASP B 51  ? 1.114 1.518 1.255 0.045  0.051  -0.164 51  ASP CCC OD1 
2090  O OD2 . ASP B 51  ? 0.997 1.404 1.144 0.049  0.051  -0.164 51  ASP CCC OD2 
2091  N N   . LEU B 52  ? 0.818 1.266 0.969 0.044  0.025  -0.174 52  LEU CCC N   
2092  C CA  . LEU B 52  ? 0.816 1.270 0.965 0.047  0.018  -0.176 52  LEU CCC CA  
2093  C C   . LEU B 52  ? 0.839 1.303 0.986 0.046  0.020  -0.179 52  LEU CCC C   
2094  O O   . LEU B 52  ? 0.943 1.409 1.086 0.046  0.018  -0.176 52  LEU CCC O   
2095  C CB  . LEU B 52  ? 0.800 1.249 0.941 0.050  0.011  -0.181 52  LEU CCC CB  
2096  C CG  . LEU B 52  ? 0.797 1.234 0.937 0.048  0.011  -0.177 52  LEU CCC CG  
2097  C CD1 . LEU B 52  ? 0.859 1.284 0.985 0.052  0.005  -0.183 52  LEU CCC CD1 
2098  C CD2 . LEU B 52  ? 0.801 1.239 0.944 0.046  0.006  -0.172 52  LEU CCC CD2 
2099  N N   . ASN B 53  ? 0.832 1.303 0.980 0.043  0.023  -0.184 53  ASN CCC N   
2100  C CA  . ASN B 53  ? 0.830 1.315 0.978 0.040  0.027  -0.187 53  ASN CCC CA  
2101  C C   . ASN B 53  ? 0.852 1.330 0.996 0.034  0.033  -0.179 53  ASN CCC C   
2102  O O   . ASN B 53  ? 0.870 1.354 1.009 0.033  0.035  -0.179 53  ASN CCC O   
2103  C CB  . ASN B 53  ? 0.831 1.328 0.983 0.036  0.029  -0.195 53  ASN CCC CB  
2104  C CG  . ASN B 53  ? 0.822 1.330 0.976 0.045  0.022  -0.203 53  ASN CCC CG  
2105  O OD1 . ASN B 53  ? 0.823 1.332 0.972 0.053  0.017  -0.205 53  ASN CCC OD1 
2106  N ND2 . ASN B 53  ? 0.819 1.331 0.976 0.044  0.020  -0.209 53  ASN CCC ND2 
2107  N N   . THR B 54  ? 0.886 1.349 1.029 0.031  0.037  -0.174 54  THR CCC N   
2108  C CA  . THR B 54  ? 0.933 1.383 1.069 0.029  0.041  -0.166 54  THR CCC CA  
2109  C C   . THR B 54  ? 0.924 1.373 1.057 0.035  0.035  -0.161 54  THR CCC C   
2110  O O   . THR B 54  ? 0.960 1.406 1.083 0.033  0.037  -0.157 54  THR CCC O   
2111  C CB  . THR B 54  ? 1.009 1.441 1.143 0.030  0.044  -0.162 54  THR CCC CB  
2112  O OG1 . THR B 54  ? 1.139 1.572 1.282 0.037  0.040  -0.161 54  THR CCC OG1 
2113  C CG2 . THR B 54  ? 1.081 1.508 1.212 0.021  0.049  -0.167 54  THR CCC CG2 
2114  N N   . MET B 55  ? 0.880 1.331 1.020 0.041  0.029  -0.160 55  MET CCC N   
2115  C CA  . MET B 55  ? 0.890 1.342 1.029 0.045  0.021  -0.156 55  MET CCC CA  
2116  C C   . MET B 55  ? 0.898 1.355 1.026 0.045  0.019  -0.159 55  MET CCC C   
2117  O O   . MET B 55  ? 0.941 1.394 1.060 0.046  0.017  -0.155 55  MET CCC O   
2118  C CB  . MET B 55  ? 0.877 1.332 1.026 0.048  0.015  -0.156 55  MET CCC CB  
2119  C CG  . MET B 55  ? 0.909 1.363 1.069 0.049  0.018  -0.151 55  MET CCC CG  
2120  S SD  . MET B 55  ? 1.017 1.477 1.188 0.048  0.013  -0.152 55  MET CCC SD  
2121  C CE  . MET B 55  ? 0.935 1.403 1.110 0.048  0.002  -0.147 55  MET CCC CE  
2122  N N   . LEU B 56  ? 0.874 1.340 1.002 0.045  0.019  -0.167 56  LEU CCC N   
2123  C CA  . LEU B 56  ? 0.876 1.349 0.995 0.047  0.018  -0.172 56  LEU CCC CA  
2124  C C   . LEU B 56  ? 0.905 1.381 1.016 0.042  0.027  -0.171 56  LEU CCC C   
2125  O O   . LEU B 56  ? 0.939 1.415 1.037 0.043  0.028  -0.170 56  LEU CCC O   
2126  C CB  . LEU B 56  ? 0.850 1.331 0.970 0.052  0.015  -0.182 56  LEU CCC CB  
2127  C CG  . LEU B 56  ? 0.832 1.304 0.952 0.056  0.006  -0.183 56  LEU CCC CG  
2128  C CD1 . LEU B 56  ? 0.829 1.305 0.946 0.063  0.003  -0.193 56  LEU CCC CD1 
2129  C CD2 . LEU B 56  ? 0.840 1.301 0.951 0.057  -0.003 -0.180 56  LEU CCC CD2 
2130  N N   . ASN B 57  ? 0.907 1.387 1.024 0.035  0.035  -0.171 57  ASN CCC N   
2131  C CA  . ASN B 57  ? 0.943 1.426 1.053 0.025  0.046  -0.170 57  ASN CCC CA  
2132  C C   . ASN B 57  ? 0.980 1.441 1.073 0.023  0.048  -0.160 57  ASN CCC C   
2133  O O   . ASN B 57  ? 1.019 1.478 1.098 0.016  0.055  -0.158 57  ASN CCC O   
2134  C CB  . ASN B 57  ? 0.950 1.439 1.069 0.016  0.052  -0.174 57  ASN CCC CB  
2135  C CG  . ASN B 57  ? 0.980 1.495 1.113 0.018  0.051  -0.185 57  ASN CCC CG  
2136  O OD1 . ASN B 57  ? 1.047 1.572 1.180 0.028  0.046  -0.190 57  ASN CCC OD1 
2137  N ND2 . ASN B 57  ? 1.086 1.611 1.228 0.009  0.056  -0.189 57  ASN CCC ND2 
2138  N N   . THR B 58  ? 0.987 1.433 1.081 0.029  0.041  -0.154 58  THR CCC N   
2139  C CA  . THR B 58  ? 1.040 1.464 1.116 0.029  0.041  -0.144 58  THR CCC CA  
2140  C C   . THR B 58  ? 1.050 1.472 1.112 0.035  0.035  -0.142 58  THR CCC C   
2141  O O   . THR B 58  ? 1.072 1.476 1.115 0.036  0.034  -0.134 58  THR CCC O   
2142  C CB  . THR B 58  ? 1.057 1.470 1.141 0.037  0.036  -0.138 58  THR CCC CB  
2143  O OG1 . THR B 58  ? 1.028 1.453 1.127 0.044  0.026  -0.140 58  THR CCC OG1 
2144  C CG2 . THR B 58  ? 1.068 1.474 1.157 0.032  0.043  -0.140 58  THR CCC CG2 
2145  N N   . VAL B 59  ? 1.035 1.472 1.102 0.039  0.030  -0.148 59  VAL CCC N   
2146  C CA  . VAL B 59  ? 1.057 1.490 1.107 0.043  0.024  -0.148 59  VAL CCC CA  
2147  C C   . VAL B 59  ? 1.169 1.602 1.200 0.037  0.036  -0.148 59  VAL CCC C   
2148  O O   . VAL B 59  ? 1.264 1.714 1.302 0.032  0.045  -0.156 59  VAL CCC O   
2149  C CB  . VAL B 59  ? 1.002 1.445 1.057 0.049  0.015  -0.155 59  VAL CCC CB  
2150  C CG1 . VAL B 59  ? 1.030 1.465 1.063 0.053  0.008  -0.155 59  VAL CCC CG1 
2151  C CG2 . VAL B 59  ? 0.971 1.415 1.045 0.051  0.005  -0.154 59  VAL CCC CG2 
2152  N N   . GLY B 60  ? 1.344 1.757 1.350 0.037  0.035  -0.141 60  GLY CCC N   
2153  C CA  . GLY B 60  ? 1.419 1.829 1.403 0.029  0.048  -0.140 60  GLY CCC CA  
2154  C C   . GLY B 60  ? 1.428 1.846 1.397 0.033  0.050  -0.146 60  GLY CCC C   
2155  O O   . GLY B 60  ? 1.436 1.869 1.402 0.027  0.063  -0.151 60  GLY CCC O   
2156  N N   . GLY B 61  ? 1.383 1.792 1.342 0.043  0.035  -0.146 61  GLY CCC N   
2157  C CA  . GLY B 61  ? 1.395 1.805 1.334 0.049  0.035  -0.152 61  GLY CCC CA  
2158  C C   . GLY B 61  ? 1.249 1.678 1.206 0.056  0.030  -0.163 61  GLY CCC C   
2159  O O   . GLY B 61  ? 1.222 1.667 1.206 0.054  0.032  -0.167 61  GLY CCC O   
2160  N N   . HIS B 62  ? 1.275 1.697 1.211 0.064  0.025  -0.168 62  HIS CCC N   
2161  C CA  . HIS B 62  ? 1.196 1.626 1.140 0.073  0.017  -0.178 62  HIS CCC CA  
2162  C C   . HIS B 62  ? 1.142 1.599 1.108 0.074  0.029  -0.187 62  HIS CCC C   
2163  O O   . HIS B 62  ? 1.174 1.637 1.156 0.078  0.022  -0.192 62  HIS CCC O   
2164  C CB  . HIS B 62  ? 1.191 1.612 1.149 0.073  -0.001 -0.176 62  HIS CCC CB  
2165  C CG  . HIS B 62  ? 1.217 1.618 1.160 0.072  -0.015 -0.169 62  HIS CCC CG  
2166  N ND1 . HIS B 62  ? 1.281 1.664 1.194 0.077  -0.024 -0.171 62  HIS CCC ND1 
2167  C CD2 . HIS B 62  ? 1.223 1.619 1.176 0.068  -0.021 -0.159 62  HIS CCC CD2 
2168  C CE1 . HIS B 62  ? 1.426 1.797 1.334 0.075  -0.038 -0.164 62  HIS CCC CE1 
2169  N NE2 . HIS B 62  ? 1.316 1.697 1.250 0.071  -0.036 -0.156 62  HIS CCC NE2 
2170  N N   . GLN B 63  ? 1.128 1.601 1.092 0.069  0.046  -0.187 63  GLN CCC N   
2171  C CA  . GLN B 63  ? 1.094 1.599 1.083 0.067  0.057  -0.195 63  GLN CCC CA  
2172  C C   . GLN B 63  ? 1.124 1.643 1.112 0.083  0.056  -0.207 63  GLN CCC C   
2173  O O   . GLN B 63  ? 1.182 1.724 1.193 0.086  0.058  -0.215 63  GLN CCC O   
2174  C CB  . GLN B 63  ? 1.080 1.601 1.069 0.055  0.076  -0.192 63  GLN CCC CB  
2175  C CG  . GLN B 63  ? 1.155 1.661 1.148 0.040  0.078  -0.180 63  GLN CCC CG  
2176  C CD  . GLN B 63  ? 1.209 1.720 1.231 0.037  0.071  -0.180 63  GLN CCC CD  
2177  O OE1 . GLN B 63  ? 1.284 1.821 1.327 0.033  0.078  -0.187 63  GLN CCC OE1 
2178  N NE2 . GLN B 63  ? 1.268 1.756 1.290 0.039  0.058  -0.174 63  GLN CCC NE2 
2179  N N   . ALA B 64  ? 1.157 1.659 1.116 0.093  0.051  -0.211 64  ALA CCC N   
2180  C CA  . ALA B 64  ? 1.254 1.759 1.206 0.111  0.047  -0.223 64  ALA CCC CA  
2181  C C   . ALA B 64  ? 1.228 1.720 1.191 0.115  0.030  -0.225 64  ALA CCC C   
2182  O O   . ALA B 64  ? 1.226 1.733 1.203 0.125  0.029  -0.233 64  ALA CCC O   
2183  C CB  . ALA B 64  ? 1.343 1.825 1.256 0.120  0.043  -0.225 64  ALA CCC CB  
2184  N N   . ALA B 65  ? 1.157 1.623 1.116 0.108  0.017  -0.216 65  ALA CCC N   
2185  C CA  . ALA B 65  ? 1.140 1.592 1.109 0.108  0.003  -0.217 65  ALA CCC CA  
2186  C C   . ALA B 65  ? 1.162 1.636 1.163 0.103  0.008  -0.216 65  ALA CCC C   
2187  O O   . ALA B 65  ? 1.238 1.713 1.246 0.110  0.002  -0.222 65  ALA CCC O   
2188  C CB  . ALA B 65  ? 1.133 1.561 1.096 0.099  -0.010 -0.208 65  ALA CCC CB  
2189  N N   . MET B 66  ? 1.145 1.634 1.162 0.092  0.018  -0.209 66  MET CCC N   
2190  C CA  . MET B 66  ? 1.122 1.629 1.166 0.085  0.023  -0.209 66  MET CCC CA  
2191  C C   . MET B 66  ? 1.058 1.592 1.113 0.094  0.029  -0.220 66  MET CCC C   
2192  O O   . MET B 66  ? 1.097 1.638 1.168 0.097  0.025  -0.224 66  MET CCC O   
2193  C CB  . MET B 66  ? 1.096 1.608 1.149 0.071  0.033  -0.200 66  MET CCC CB  
2194  C CG  . MET B 66  ? 1.029 1.516 1.073 0.065  0.026  -0.189 66  MET CCC CG  
2195  S SD  . MET B 66  ? 0.946 1.418 1.000 0.066  0.010  -0.186 66  MET CCC SD  
2196  C CE  . MET B 66  ? 1.098 1.585 1.178 0.062  0.016  -0.188 66  MET CCC CE  
2197  N N   . GLN B 67  ? 1.066 1.619 1.114 0.099  0.039  -0.225 67  GLN CCC N   
2198  C CA  . GLN B 67  ? 1.133 1.719 1.195 0.110  0.045  -0.237 67  GLN CCC CA  
2199  C C   . GLN B 67  ? 1.154 1.726 1.203 0.130  0.032  -0.246 67  GLN CCC C   
2200  O O   . GLN B 67  ? 1.192 1.781 1.255 0.140  0.029  -0.253 67  GLN CCC O   
2201  C CB  . GLN B 67  ? 1.130 1.741 1.186 0.111  0.061  -0.240 67  GLN CCC CB  
2202  C CG  . GLN B 67  ? 1.157 1.815 1.237 0.118  0.070  -0.252 67  GLN CCC CG  
2203  C CD  . GLN B 67  ? 1.250 1.934 1.358 0.098  0.079  -0.248 67  GLN CCC CD  
2204  O OE1 . GLN B 67  ? 1.185 1.857 1.289 0.078  0.086  -0.238 67  GLN CCC OE1 
2205  N NE2 . GLN B 67  ? 1.429 2.148 1.563 0.102  0.078  -0.257 67  GLN CCC NE2 
2206  N N   . MET B 68  ? 1.133 1.672 1.153 0.137  0.024  -0.245 68  MET CCC N   
2207  C CA  . MET B 68  ? 1.182 1.697 1.184 0.153  0.010  -0.252 68  MET CCC CA  
2208  C C   . MET B 68  ? 1.153 1.653 1.167 0.148  -0.001 -0.248 68  MET CCC C   
2209  O O   . MET B 68  ? 1.248 1.743 1.259 0.161  -0.008 -0.256 68  MET CCC O   
2210  C CB  . MET B 68  ? 1.242 1.721 1.210 0.156  0.002  -0.251 68  MET CCC CB  
2211  C CG  . MET B 68  ? 1.404 1.856 1.343 0.176  -0.009 -0.261 68  MET CCC CG  
2212  S SD  . MET B 68  ? 1.442 1.843 1.337 0.175  -0.022 -0.259 68  MET CCC SD  
2213  C CE  . MET B 68  ? 1.351 1.764 1.252 0.157  -0.013 -0.248 68  MET CCC CE  
2214  N N   . LEU B 69  ? 1.108 1.600 1.133 0.130  -0.002 -0.237 69  LEU CCC N   
2215  C CA  . LEU B 69  ? 1.158 1.639 1.194 0.123  -0.009 -0.233 69  LEU CCC CA  
2216  C C   . LEU B 69  ? 1.181 1.687 1.239 0.127  -0.005 -0.238 69  LEU CCC C   
2217  O O   . LEU B 69  ? 1.207 1.702 1.264 0.132  -0.013 -0.241 69  LEU CCC O   
2218  C CB  . LEU B 69  ? 1.120 1.594 1.167 0.105  -0.008 -0.221 69  LEU CCC CB  
2219  C CG  . LEU B 69  ? 1.043 1.506 1.101 0.097  -0.013 -0.216 69  LEU CCC CG  
2220  C CD1 . LEU B 69  ? 1.081 1.515 1.121 0.103  -0.025 -0.218 69  LEU CCC CD1 
2221  C CD2 . LEU B 69  ? 1.007 1.467 1.075 0.083  -0.011 -0.205 69  LEU CCC CD2 
2222  N N   . LYS B 70  ? 1.120 1.661 1.196 0.122  0.008  -0.240 70  LYS CCC N   
2223  C CA  . LYS B 70  ? 1.071 1.642 1.170 0.124  0.010  -0.245 70  LYS CCC CA  
2224  C C   . LYS B 70  ? 1.095 1.672 1.187 0.146  0.003  -0.257 70  LYS CCC C   
2225  O O   . LYS B 70  ? 1.171 1.750 1.270 0.152  -0.004 -0.261 70  LYS CCC O   
2226  C CB  . LYS B 70  ? 1.063 1.670 1.181 0.113  0.025  -0.246 70  LYS CCC CB  
2227  C CG  . LYS B 70  ? 1.119 1.719 1.242 0.092  0.032  -0.234 70  LYS CCC CG  
2228  C CD  . LYS B 70  ? 1.338 1.928 1.473 0.083  0.028  -0.230 70  LYS CCC CD  
2229  C CE  . LYS B 70  ? 1.354 1.932 1.491 0.066  0.034  -0.219 70  LYS CCC CE  
2230  N NZ  . LYS B 70  ? 1.224 1.790 1.369 0.059  0.031  -0.215 70  LYS CCC NZ  
2231  N N   . GLU B 71  ? 1.129 1.706 1.204 0.160  0.004  -0.264 71  GLU CCC N   
2232  C CA  . GLU B 71  ? 1.201 1.778 1.264 0.186  -0.003 -0.276 71  GLU CCC CA  
2233  C C   . GLU B 71  ? 1.196 1.729 1.237 0.193  -0.019 -0.275 71  GLU CCC C   
2234  O O   . GLU B 71  ? 1.230 1.765 1.270 0.208  -0.027 -0.282 71  GLU CCC O   
2235  C CB  . GLU B 71  ? 1.410 1.987 1.453 0.199  0.002  -0.281 71  GLU CCC CB  
2236  C CG  . GLU B 71  ? 1.545 2.174 1.611 0.196  0.019  -0.285 71  GLU CCC CG  
2237  C CD  . GLU B 71  ? 1.619 2.255 1.665 0.214  0.026  -0.293 71  GLU CCC CD  
2238  O OE1 . GLU B 71  ? 1.638 2.230 1.648 0.222  0.018  -0.293 71  GLU CCC OE1 
2239  O OE2 . GLU B 71  ? 1.569 2.252 1.633 0.219  0.039  -0.300 71  GLU CCC OE2 
2240  N N   . THR B 72  ? 1.191 1.684 1.213 0.181  -0.025 -0.266 72  THR CCC N   
2241  C CA  . THR B 72  ? 1.266 1.715 1.266 0.184  -0.038 -0.264 72  THR CCC CA  
2242  C C   . THR B 72  ? 1.200 1.655 1.218 0.176  -0.040 -0.261 72  THR CCC C   
2243  O O   . THR B 72  ? 1.245 1.678 1.248 0.187  -0.050 -0.265 72  THR CCC O   
2244  C CB  . THR B 72  ? 1.304 1.718 1.287 0.169  -0.043 -0.256 72  THR CCC CB  
2245  O OG1 . THR B 72  ? 1.369 1.772 1.329 0.178  -0.043 -0.260 72  THR CCC OG1 
2246  C CG2 . THR B 72  ? 1.273 1.644 1.235 0.166  -0.055 -0.253 72  THR CCC CG2 
2247  N N   . ILE B 73  ? 1.124 1.601 1.169 0.158  -0.031 -0.254 73  ILE CCC N   
2248  C CA  . ILE B 73  ? 1.111 1.593 1.171 0.151  -0.032 -0.251 73  ILE CCC CA  
2249  C C   . ILE B 73  ? 1.172 1.677 1.239 0.168  -0.036 -0.262 73  ILE CCC C   
2250  O O   . ILE B 73  ? 1.220 1.710 1.280 0.173  -0.044 -0.263 73  ILE CCC O   
2251  C CB  . ILE B 73  ? 1.038 1.540 1.123 0.131  -0.021 -0.244 73  ILE CCC CB  
2252  C CG1 . ILE B 73  ? 1.015 1.492 1.093 0.117  -0.020 -0.233 73  ILE CCC CG1 
2253  C CG2 . ILE B 73  ? 1.019 1.532 1.120 0.126  -0.021 -0.243 73  ILE CCC CG2 
2254  C CD1 . ILE B 73  ? 0.977 1.471 1.074 0.101  -0.010 -0.225 73  ILE CCC CD1 
2255  N N   . ASN B 74  ? 1.196 1.741 1.278 0.176  -0.030 -0.270 74  ASN CCC N   
2256  C CA  . ASN B 74  ? 1.210 1.787 1.305 0.192  -0.033 -0.281 74  ASN CCC CA  
2257  C C   . ASN B 74  ? 1.307 1.857 1.373 0.218  -0.048 -0.288 74  ASN CCC C   
2258  O O   . ASN B 74  ? 1.397 1.951 1.464 0.231  -0.057 -0.294 74  ASN CCC O   
2259  C CB  . ASN B 74  ? 1.234 1.863 1.353 0.195  -0.022 -0.287 74  ASN CCC CB  
2260  C CG  . ASN B 74  ? 1.234 1.890 1.379 0.169  -0.009 -0.281 74  ASN CCC CG  
2261  O OD1 . ASN B 74  ? 1.255 1.899 1.407 0.154  -0.011 -0.274 74  ASN CCC OD1 
2262  N ND2 . ASN B 74  ? 1.228 1.917 1.386 0.164  0.004  -0.283 74  ASN CCC ND2 
2263  N N   . GLU B 75  ? 1.551 2.068 1.588 0.227  -0.050 -0.289 75  GLU CCC N   
2264  C CA  . GLU B 75  ? 1.661 2.141 1.663 0.251  -0.064 -0.295 75  GLU CCC CA  
2265  C C   . GLU B 75  ? 1.629 2.066 1.612 0.244  -0.074 -0.288 75  GLU CCC C   
2266  O O   . GLU B 75  ? 1.699 2.120 1.666 0.262  -0.086 -0.294 75  GLU CCC O   
2267  C CB  . GLU B 75  ? 1.865 2.311 1.836 0.256  -0.065 -0.295 75  GLU CCC CB  
2268  C CG  . GLU B 75  ? 2.115 2.498 2.040 0.266  -0.079 -0.295 75  GLU CCC CG  
2269  C CD  . GLU B 75  ? 2.322 2.674 2.215 0.273  -0.081 -0.298 75  GLU CCC CD  
2270  O OE1 . GLU B 75  ? 2.387 2.770 2.290 0.280  -0.072 -0.303 75  GLU CCC OE1 
2271  O OE2 . GLU B 75  ? 2.429 2.723 2.284 0.269  -0.091 -0.294 75  GLU CCC OE2 
2272  N N   . GLU B 76  ? 1.442 1.859 1.427 0.218  -0.070 -0.277 76  GLU CCC N   
2273  C CA  . GLU B 76  ? 1.440 1.818 1.408 0.209  -0.077 -0.270 76  GLU CCC CA  
2274  C C   . GLU B 76  ? 1.381 1.783 1.369 0.209  -0.077 -0.271 76  GLU CCC C   
2275  O O   . GLU B 76  ? 1.413 1.784 1.379 0.215  -0.087 -0.271 76  GLU CCC O   
2276  C CB  . GLU B 76  ? 1.317 1.678 1.288 0.183  -0.070 -0.257 76  GLU CCC CB  
2277  C CG  . GLU B 76  ? 1.361 1.691 1.307 0.182  -0.073 -0.256 76  GLU CCC CG  
2278  C CD  . GLU B 76  ? 1.551 1.828 1.452 0.194  -0.087 -0.259 76  GLU CCC CD  
2279  O OE1 . GLU B 76  ? 1.557 1.810 1.446 0.191  -0.091 -0.256 76  GLU CCC OE1 
2280  O OE2 . GLU B 76  ? 1.801 2.057 1.677 0.206  -0.092 -0.265 76  GLU CCC OE2 
2281  N N   . ALA B 77  ? 1.289 1.740 1.314 0.202  -0.068 -0.273 77  ALA CCC N   
2282  C CA  . ALA B 77  ? 1.242 1.717 1.285 0.201  -0.070 -0.275 77  ALA CCC CA  
2283  C C   . ALA B 77  ? 1.320 1.802 1.354 0.228  -0.083 -0.287 77  ALA CCC C   
2284  O O   . ALA B 77  ? 1.426 1.896 1.451 0.232  -0.092 -0.288 77  ALA CCC O   
2285  C CB  . ALA B 77  ? 1.188 1.713 1.270 0.186  -0.058 -0.275 77  ALA CCC CB  
2286  N N   . ALA B 78  ? 1.359 1.861 1.393 0.248  -0.085 -0.296 78  ALA CCC N   
2287  C CA  . ALA B 78  ? 1.397 1.908 1.422 0.278  -0.098 -0.308 78  ALA CCC CA  
2288  C C   . ALA B 78  ? 1.469 1.916 1.446 0.292  -0.113 -0.306 78  ALA CCC C   
2289  O O   . ALA B 78  ? 1.583 2.025 1.550 0.308  -0.126 -0.311 78  ALA CCC O   
2290  C CB  . ALA B 78  ? 1.397 1.940 1.430 0.298  -0.095 -0.318 78  ALA CCC CB  
2291  N N   . GLU B 79  ? 1.474 1.870 1.419 0.285  -0.111 -0.299 79  GLU CCC N   
2292  C CA  . GLU B 79  ? 1.585 1.915 1.482 0.292  -0.124 -0.296 79  GLU CCC CA  
2293  C C   . GLU B 79  ? 1.591 1.900 1.482 0.276  -0.126 -0.288 79  GLU CCC C   
2294  O O   . GLU B 79  ? 1.682 1.951 1.539 0.289  -0.138 -0.289 79  GLU CCC O   
2295  C CB  . GLU B 79  ? 1.608 1.891 1.476 0.282  -0.121 -0.290 79  GLU CCC CB  
2296  C CG  . GLU B 79  ? 1.810 2.018 1.622 0.286  -0.133 -0.286 79  GLU CCC CG  
2297  C CD  . GLU B 79  ? 1.983 2.165 1.758 0.322  -0.149 -0.297 79  GLU CCC CD  
2298  O OE1 . GLU B 79  ? 2.020 2.246 1.816 0.346  -0.152 -0.308 79  GLU CCC OE1 
2299  O OE2 . GLU B 79  ? 2.081 2.195 1.804 0.326  -0.158 -0.295 79  GLU CCC OE2 
2300  N N   . TRP B 80  ? 1.514 1.846 1.436 0.249  -0.113 -0.280 80  TRP CCC N   
2301  C CA  . TRP B 80  ? 1.537 1.855 1.456 0.235  -0.113 -0.274 80  TRP CCC CA  
2302  C C   . TRP B 80  ? 1.577 1.914 1.499 0.254  -0.125 -0.283 80  TRP CCC C   
2303  O O   . TRP B 80  ? 1.675 1.976 1.567 0.259  -0.134 -0.281 80  TRP CCC O   
2304  C CB  . TRP B 80  ? 1.490 1.835 1.444 0.207  -0.098 -0.266 80  TRP CCC CB  
2305  C CG  . TRP B 80  ? 1.417 1.748 1.367 0.196  -0.097 -0.260 80  TRP CCC CG  
2306  C CD1 . TRP B 80  ? 1.370 1.731 1.338 0.196  -0.099 -0.265 80  TRP CCC CD1 
2307  C CD2 . TRP B 80  ? 1.431 1.715 1.353 0.183  -0.094 -0.251 80  TRP CCC CD2 
2308  N NE1 . TRP B 80  ? 1.360 1.692 1.312 0.185  -0.097 -0.258 80  TRP CCC NE1 
2309  C CE2 . TRP B 80  ? 1.408 1.694 1.332 0.177  -0.094 -0.249 80  TRP CCC CE2 
2310  C CE3 . TRP B 80  ? 1.448 1.689 1.343 0.173  -0.092 -0.243 80  TRP CCC CE3 
2311  C CZ2 . TRP B 80  ? 1.456 1.705 1.357 0.164  -0.089 -0.241 80  TRP CCC CZ2 
2312  C CZ3 . TRP B 80  ? 1.446 1.654 1.322 0.159  -0.087 -0.234 80  TRP CCC CZ3 
2313  C CH2 . TRP B 80  ? 1.470 1.682 1.349 0.155  -0.085 -0.233 80  TRP CCC CH2 
2314  N N   . ASP B 81  ? 1.554 1.951 1.513 0.262  -0.124 -0.292 81  ASP CCC N   
2315  C CA  . ASP B 81  ? 1.577 2.000 1.545 0.278  -0.136 -0.301 81  ASP CCC CA  
2316  C C   . ASP B 81  ? 1.654 2.044 1.582 0.310  -0.154 -0.308 81  ASP CCC C   
2317  O O   . ASP B 81  ? 1.756 2.134 1.669 0.321  -0.168 -0.311 81  ASP CCC O   
2318  C CB  . ASP B 81  ? 1.514 2.011 1.530 0.281  -0.131 -0.310 81  ASP CCC CB  
2319  C CG  . ASP B 81  ? 1.485 2.014 1.538 0.250  -0.115 -0.304 81  ASP CCC CG  
2320  O OD1 . ASP B 81  ? 1.613 2.113 1.657 0.230  -0.110 -0.295 81  ASP CCC OD1 
2321  O OD2 . ASP B 81  ? 1.418 1.998 1.505 0.246  -0.106 -0.309 81  ASP CCC OD2 
2322  N N   . ARG B 82  ? 1.609 1.981 1.518 0.327  -0.156 -0.311 82  ARG CCC N   
2323  C CA  . ARG B 82  ? 1.701 2.033 1.566 0.359  -0.174 -0.318 82  ARG CCC CA  
2324  C C   . ARG B 82  ? 1.769 2.023 1.580 0.354  -0.182 -0.308 82  ARG CCC C   
2325  O O   . ARG B 82  ? 1.907 2.134 1.686 0.377  -0.198 -0.313 82  ARG CCC O   
2326  C CB  . ARG B 82  ? 1.720 2.044 1.573 0.376  -0.173 -0.323 82  ARG CCC CB  
2327  C CG  . ARG B 82  ? 1.869 2.124 1.660 0.403  -0.188 -0.325 82  ARG CCC CG  
2328  C CD  . ARG B 82  ? 1.934 2.173 1.707 0.417  -0.186 -0.330 82  ARG CCC CD  
2329  N NE  . ARG B 82  ? 2.193 2.356 1.901 0.441  -0.202 -0.331 82  ARG CCC NE  
2330  C CZ  . ARG B 82  ? 2.210 2.300 1.871 0.424  -0.202 -0.322 82  ARG CCC CZ  
2331  N NH1 . ARG B 82  ? 2.089 2.176 1.765 0.386  -0.187 -0.310 82  ARG CCC NH1 
2332  N NH2 . ARG B 82  ? 2.309 2.327 1.907 0.446  -0.217 -0.324 82  ARG CCC NH2 
2333  N N   . LEU B 83  ? 1.743 1.962 1.543 0.325  -0.169 -0.296 83  LEU CCC N   
2334  C CA  . LEU B 83  ? 1.836 1.982 1.585 0.317  -0.174 -0.286 83  LEU CCC CA  
2335  C C   . LEU B 83  ? 1.869 2.016 1.622 0.301  -0.171 -0.280 83  LEU CCC C   
2336  O O   . LEU B 83  ? 1.944 2.035 1.652 0.300  -0.178 -0.275 83  LEU CCC O   
2337  C CB  A LEU B 83  ? 1.822 1.932 1.556 0.293  -0.162 -0.276 83  LEU CCC CB  
2338  C CG  A LEU B 83  ? 1.876 1.969 1.591 0.310  -0.167 -0.282 83  LEU CCC CG  
2339  C CD1 A LEU B 83  ? 1.864 1.934 1.574 0.284  -0.156 -0.273 83  LEU CCC CD1 
2340  C CD2 A LEU B 83  ? 2.061 2.093 1.716 0.339  -0.186 -0.287 83  LEU CCC CD2 
2341  N N   . HIS B 84  ? 1.835 2.040 1.638 0.287  -0.162 -0.282 84  HIS CCC N   
2342  C CA  . HIS B 84  ? 1.835 2.044 1.644 0.271  -0.159 -0.277 84  HIS CCC CA  
2343  C C   . HIS B 84  ? 1.782 2.058 1.636 0.279  -0.163 -0.287 84  HIS CCC C   
2344  O O   . HIS B 84  ? 1.744 2.063 1.640 0.259  -0.150 -0.286 84  HIS CCC O   
2345  C CB  . HIS B 84  ? 1.761 1.963 1.583 0.238  -0.139 -0.265 84  HIS CCC CB  
2346  C CG  . HIS B 84  ? 1.851 1.998 1.638 0.227  -0.134 -0.255 84  HIS CCC CG  
2347  N ND1 . HIS B 84  ? 1.815 1.963 1.609 0.221  -0.128 -0.253 84  HIS CCC ND1 
2348  C CD2 . HIS B 84  ? 2.049 2.138 1.791 0.219  -0.135 -0.247 84  HIS CCC CD2 
2349  C CE1 . HIS B 84  ? 1.927 2.022 1.685 0.209  -0.126 -0.244 84  HIS CCC CE1 
2350  N NE2 . HIS B 84  ? 2.156 2.214 1.882 0.207  -0.129 -0.240 84  HIS CCC NE2 
2351  N N   . PRO B 85  ? 1.762 2.047 1.606 0.307  -0.182 -0.298 85  PRO CCC N   
2352  C CA  . PRO B 85  ? 1.701 2.054 1.590 0.313  -0.187 -0.309 85  PRO CCC CA  
2353  C C   . PRO B 85  ? 1.733 2.088 1.628 0.293  -0.185 -0.305 85  PRO CCC C   
2354  O O   . PRO B 85  ? 1.751 2.053 1.608 0.285  -0.185 -0.297 85  PRO CCC O   
2355  C CB  . PRO B 85  ? 1.666 2.020 1.536 0.350  -0.209 -0.320 85  PRO CCC CB  
2356  C CG  . PRO B 85  ? 1.856 2.141 1.672 0.365  -0.214 -0.316 85  PRO CCC CG  
2357  C CD  . PRO B 85  ? 1.785 2.019 1.578 0.335  -0.200 -0.301 85  PRO CCC CD  
2358  N N   . VAL B 86  ? 1.710 2.127 1.651 0.285  -0.183 -0.312 86  VAL CCC N   
2359  C CA  . VAL B 86  ? 1.691 2.114 1.640 0.265  -0.181 -0.310 86  VAL CCC CA  
2360  C C   . VAL B 86  ? 1.824 2.245 1.756 0.284  -0.204 -0.319 86  VAL CCC C   
2361  O O   . VAL B 86  ? 1.841 2.305 1.792 0.306  -0.219 -0.331 86  VAL CCC O   
2362  C CB  . VAL B 86  ? 1.600 2.084 1.604 0.244  -0.169 -0.313 86  VAL CCC CB  
2363  C CG1 . VAL B 86  ? 1.581 2.068 1.589 0.225  -0.169 -0.312 86  VAL CCC CG1 
2364  C CG2 . VAL B 86  ? 1.703 2.183 1.719 0.226  -0.148 -0.303 86  VAL CCC CG2 
2365  N N   . HIS B 87  ? 1.900 2.273 1.794 0.278  -0.207 -0.313 87  HIS CCC N   
2366  C CA  . HIS B 87  ? 1.884 2.248 1.755 0.295  -0.230 -0.320 87  HIS CCC CA  
2367  C C   . HIS B 87  ? 1.892 2.314 1.804 0.281  -0.234 -0.329 87  HIS CCC C   
2368  O O   . HIS B 87  ? 1.985 2.406 1.909 0.253  -0.219 -0.323 87  HIS CCC O   
2369  C CB  . HIS B 87  ? 1.902 2.191 1.714 0.291  -0.230 -0.311 87  HIS CCC CB  
2370  C CG  . HIS B 87  ? 1.910 2.139 1.674 0.306  -0.232 -0.304 87  HIS CCC CG  
2371  N ND1 . HIS B 87  ? 1.929 2.086 1.635 0.303  -0.231 -0.295 87  HIS CCC ND1 
2372  C CD2 . HIS B 87  ? 2.037 2.264 1.799 0.322  -0.233 -0.305 87  HIS CCC CD2 
2373  C CE1 . HIS B 87  ? 2.105 2.218 1.775 0.316  -0.233 -0.290 87  HIS CCC CE1 
2374  N NE2 . HIS B 87  ? 2.233 2.386 1.936 0.329  -0.235 -0.297 87  HIS CCC NE2 
2375  N N   . ALA B 88  ? 1.970 2.440 1.904 0.300  -0.254 -0.342 88  ALA CCC N   
2376  C CA  . ALA B 88  ? 1.912 2.444 1.891 0.285  -0.257 -0.351 88  ALA CCC CA  
2377  C C   . ALA B 88  ? 1.978 2.486 1.929 0.284  -0.275 -0.354 88  ALA CCC C   
2378  O O   . ALA B 88  ? 2.137 2.604 2.042 0.308  -0.293 -0.355 88  ALA CCC O   
2379  C CB  . ALA B 88  ? 1.944 2.551 1.969 0.303  -0.269 -0.365 88  ALA CCC CB  
2380  N N   . GLY B 89  ? 1.973 2.502 1.945 0.257  -0.270 -0.355 89  GLY CCC N   
2381  C CA  . GLY B 89  ? 2.040 2.550 1.987 0.254  -0.286 -0.360 89  GLY CCC CA  
2382  C C   . GLY B 89  ? 2.048 2.562 2.009 0.219  -0.273 -0.358 89  GLY CCC C   
2383  O O   . GLY B 89  ? 2.035 2.557 2.019 0.197  -0.250 -0.351 89  GLY CCC O   
2384  N N   . PRO B 90  ? 1.960 2.466 1.904 0.214  -0.290 -0.364 90  PRO CCC N   
2385  C CA  . PRO B 90  ? 1.952 2.448 1.898 0.182  -0.278 -0.362 90  PRO CCC CA  
2386  C C   . PRO B 90  ? 1.927 2.354 1.832 0.173  -0.256 -0.347 90  PRO CCC C   
2387  O O   . PRO B 90  ? 1.891 2.264 1.749 0.190  -0.258 -0.341 90  PRO CCC O   
2388  C CB  . PRO B 90  ? 2.070 2.565 1.996 0.184  -0.305 -0.373 90  PRO CCC CB  
2389  C CG  . PRO B 90  ? 2.067 2.600 2.005 0.214  -0.331 -0.383 90  PRO CCC CG  
2390  C CD  . PRO B 90  ? 1.906 2.416 1.831 0.237  -0.321 -0.375 90  PRO CCC CD  
2391  N N   . ILE B 91  ? 1.905 2.332 1.827 0.147  -0.234 -0.342 91  ILE CCC N   
2392  C CA  . ILE B 91  ? 1.922 2.293 1.814 0.139  -0.211 -0.328 91  ILE CCC CA  
2393  C C   . ILE B 91  ? 2.001 2.324 1.849 0.131  -0.213 -0.328 91  ILE CCC C   
2394  O O   . ILE B 91  ? 2.086 2.423 1.943 0.115  -0.220 -0.336 91  ILE CCC O   
2395  C CB  . ILE B 91  ? 1.904 2.294 1.830 0.119  -0.186 -0.321 91  ILE CCC CB  
2396  C CG1 . ILE B 91  ? 1.940 2.279 1.839 0.118  -0.164 -0.307 91  ILE CCC CG1 
2397  C CG2 . ILE B 91  ? 1.951 2.362 1.899 0.094  -0.183 -0.326 91  ILE CCC CG2 
2398  C CD1 . ILE B 91  ? 1.889 2.203 1.765 0.139  -0.165 -0.301 91  ILE CCC CD1 
2399  N N   . ALA B 92  ? 2.110 2.376 1.910 0.141  -0.208 -0.320 92  ALA CCC N   
2400  C CA  . ALA B 92  ? 2.171 2.383 1.922 0.136  -0.206 -0.318 92  ALA CCC CA  
2401  C C   . ALA B 92  ? 2.179 2.378 1.935 0.114  -0.181 -0.312 92  ALA CCC C   
2402  O O   . ALA B 92  ? 2.264 2.468 2.041 0.108  -0.160 -0.303 92  ALA CCC O   
2403  C CB  . ALA B 92  ? 2.228 2.384 1.926 0.152  -0.204 -0.310 92  ALA CCC CB  
2404  N N   . PRO B 93  ? 2.148 2.328 1.884 0.102  -0.185 -0.318 93  PRO CCC N   
2405  C CA  . PRO B 93  ? 2.141 2.303 1.877 0.084  -0.163 -0.313 93  PRO CCC CA  
2406  C C   . PRO B 93  ? 2.162 2.289 1.880 0.088  -0.137 -0.300 93  PRO CCC C   
2407  O O   . PRO B 93  ? 2.223 2.308 1.897 0.099  -0.134 -0.295 93  PRO CCC O   
2408  C CB  . PRO B 93  ? 2.135 2.264 1.831 0.078  -0.175 -0.322 93  PRO CCC CB  
2409  C CG  . PRO B 93  ? 2.286 2.405 1.952 0.096  -0.200 -0.327 93  PRO CCC CG  
2410  C CD  . PRO B 93  ? 2.217 2.386 1.924 0.107  -0.211 -0.329 93  PRO CCC CD  
2411  N N   . GLY B 94  ? 2.055 2.202 1.807 0.078  -0.118 -0.293 94  GLY CCC N   
2412  C CA  . GLY B 94  ? 2.010 2.138 1.759 0.078  -0.092 -0.281 94  GLY CCC CA  
2413  C C   . GLY B 94  ? 1.971 2.107 1.729 0.089  -0.089 -0.273 94  GLY CCC C   
2414  O O   . GLY B 94  ? 1.983 2.098 1.731 0.090  -0.069 -0.263 94  GLY CCC O   
2415  N N   . GLN B 95  ? 1.965 2.131 1.742 0.098  -0.107 -0.278 95  GLN CCC N   
2416  C CA  . GLN B 95  ? 1.922 2.090 1.703 0.109  -0.105 -0.272 95  GLN CCC CA  
2417  C C   . GLN B 95  ? 1.808 2.025 1.641 0.103  -0.100 -0.271 95  GLN CCC C   
2418  O O   . GLN B 95  ? 1.793 2.045 1.656 0.095  -0.107 -0.279 95  GLN CCC O   
2419  C CB  . GLN B 95  ? 1.955 2.117 1.714 0.127  -0.128 -0.277 95  GLN CCC CB  
2420  C CG  . GLN B 95  ? 2.097 2.210 1.800 0.135  -0.137 -0.278 95  GLN CCC CG  
2421  C CD  . GLN B 95  ? 2.110 2.176 1.777 0.132  -0.115 -0.266 95  GLN CCC CD  
2422  O OE1 . GLN B 95  ? 2.141 2.197 1.805 0.136  -0.108 -0.258 95  GLN CCC OE1 
2423  N NE2 . GLN B 95  ? 2.128 2.165 1.769 0.124  -0.105 -0.265 95  GLN CCC NE2 
2424  N N   . MET B 96  ? 1.757 1.974 1.600 0.106  -0.089 -0.263 96  MET CCC N   
2425  C CA  . MET B 96  ? 1.631 1.890 1.518 0.102  -0.084 -0.262 96  MET CCC CA  
2426  C C   . MET B 96  ? 1.550 1.840 1.452 0.115  -0.103 -0.270 96  MET CCC C   
2427  O O   . MET B 96  ? 1.569 1.841 1.445 0.131  -0.117 -0.273 96  MET CCC O   
2428  C CB  . MET B 96  ? 1.638 1.884 1.527 0.099  -0.066 -0.250 96  MET CCC CB  
2429  C CG  . MET B 96  ? 1.660 1.889 1.545 0.087  -0.047 -0.244 96  MET CCC CG  
2430  S SD  . MET B 96  ? 1.950 2.174 1.845 0.083  -0.026 -0.231 96  MET CCC SD  
2431  C CE  . MET B 96  ? 1.760 1.961 1.628 0.094  -0.035 -0.228 96  MET CCC CE  
2432  N N   . ARG B 97  ? 1.493 1.829 1.437 0.110  -0.102 -0.274 97  ARG CCC N   
2433  C CA  . ARG B 97  ? 1.485 1.854 1.446 0.124  -0.117 -0.281 97  ARG CCC CA  
2434  C C   . ARG B 97  ? 1.486 1.844 1.443 0.134  -0.110 -0.274 97  ARG CCC C   
2435  O O   . ARG B 97  ? 1.505 1.839 1.455 0.125  -0.094 -0.264 97  ARG CCC O   
2436  C CB  . ARG B 97  ? 1.482 1.907 1.487 0.115  -0.119 -0.289 97  ARG CCC CB  
2437  C CG  . ARG B 97  ? 1.610 2.081 1.643 0.128  -0.129 -0.297 97  ARG CCC CG  
2438  C CD  . ARG B 97  ? 1.639 2.162 1.715 0.112  -0.122 -0.301 97  ARG CCC CD  
2439  N NE  . ARG B 97  ? 1.398 1.916 1.486 0.094  -0.101 -0.292 97  ARG CCC NE  
2440  C CZ  . ARG B 97  ? 1.283 1.804 1.380 0.097  -0.090 -0.286 97  ARG CCC CZ  
2441  N NH1 . ARG B 97  ? 1.348 1.876 1.444 0.116  -0.097 -0.288 97  ARG CCC NH1 
2442  N NH2 . ARG B 97  ? 1.221 1.738 1.328 0.080  -0.073 -0.278 97  ARG CCC NH2 
2443  N N   . GLU B 98  ? 1.610 1.983 1.570 0.152  -0.123 -0.280 98  GLU CCC N   
2444  C CA  . GLU B 98  ? 1.612 1.968 1.563 0.160  -0.118 -0.274 98  GLU CCC CA  
2445  C C   . GLU B 98  ? 1.579 1.974 1.569 0.153  -0.107 -0.273 98  GLU CCC C   
2446  O O   . GLU B 98  ? 1.638 2.080 1.659 0.154  -0.112 -0.282 98  GLU CCC O   
2447  C CB  . GLU B 98  ? 1.749 2.092 1.675 0.185  -0.137 -0.280 98  GLU CCC CB  
2448  C CG  . GLU B 98  ? 1.859 2.161 1.743 0.192  -0.148 -0.280 98  GLU CCC CG  
2449  C CD  . GLU B 98  ? 1.996 2.277 1.848 0.219  -0.168 -0.285 98  GLU CCC CD  
2450  O OE1 . GLU B 98  ? 2.045 2.339 1.905 0.233  -0.172 -0.288 98  GLU CCC OE1 
2451  O OE2 . GLU B 98  ? 2.070 2.316 1.883 0.227  -0.180 -0.286 98  GLU CCC OE2 
2452  N N   . PRO B 99  ? 1.533 1.910 1.521 0.145  -0.093 -0.263 99  PRO CCC N   
2453  C CA  . PRO B 99  ? 1.361 1.771 1.382 0.138  -0.083 -0.262 99  PRO CCC CA  
2454  C C   . PRO B 99  ? 1.338 1.765 1.363 0.157  -0.092 -0.269 99  PRO CCC C   
2455  O O   . PRO B 99  ? 1.305 1.700 1.300 0.171  -0.100 -0.268 99  PRO CCC O   
2456  C CB  . PRO B 99  ? 1.259 1.640 1.271 0.126  -0.068 -0.250 99  PRO CCC CB  
2457  C CG  . PRO B 99  ? 1.347 1.681 1.319 0.132  -0.073 -0.246 99  PRO CCC CG  
2458  C CD  . PRO B 99  ? 1.521 1.849 1.478 0.140  -0.085 -0.253 99  PRO CCC CD  
2459  N N   . ARG B 100 ? 1.366 1.841 1.424 0.156  -0.090 -0.275 100 ARG CCC N   
2460  C CA  . ARG B 100 ? 1.368 1.863 1.433 0.173  -0.095 -0.281 100 ARG CCC CA  
2461  C C   . ARG B 100 ? 1.380 1.867 1.449 0.165  -0.082 -0.273 100 ARG CCC C   
2462  O O   . ARG B 100 ? 1.383 1.854 1.452 0.147  -0.070 -0.263 100 ARG CCC O   
2463  C CB  . ARG B 100 ? 1.387 1.943 1.489 0.175  -0.097 -0.291 100 ARG CCC CB  
2464  C CG  . ARG B 100 ? 1.489 2.065 1.598 0.175  -0.108 -0.299 100 ARG CCC CG  
2465  C CD  . ARG B 100 ? 1.558 2.198 1.710 0.168  -0.106 -0.308 100 ARG CCC CD  
2466  N NE  . ARG B 100 ? 1.780 2.452 1.942 0.178  -0.123 -0.319 100 ARG CCC NE  
2467  C CZ  . ARG B 100 ? 1.902 2.600 2.069 0.204  -0.137 -0.330 100 ARG CCC CZ  
2468  N NH1 . ARG B 100 ? 1.871 2.564 2.029 0.224  -0.136 -0.330 100 ARG CCC NH1 
2469  N NH2 . ARG B 100 ? 1.940 2.670 2.118 0.211  -0.153 -0.340 100 ARG CCC NH2 
2470  N N   . GLY B 101 ? 1.328 1.824 1.395 0.181  -0.085 -0.278 101 GLY CCC N   
2471  C CA  . GLY B 101 ? 1.200 1.690 1.269 0.175  -0.075 -0.272 101 GLY CCC CA  
2472  C C   . GLY B 101 ? 1.096 1.615 1.195 0.154  -0.060 -0.267 101 GLY CCC C   
2473  O O   . GLY B 101 ? 1.070 1.572 1.167 0.139  -0.050 -0.258 101 GLY CCC O   
2474  N N   . SER B 102 ? 1.081 1.645 1.207 0.151  -0.059 -0.275 102 SER CCC N   
2475  C CA  . SER B 102 ? 1.061 1.652 1.213 0.131  -0.045 -0.271 102 SER CCC CA  
2476  C C   . SER B 102 ? 1.043 1.612 1.192 0.112  -0.040 -0.263 102 SER CCC C   
2477  O O   . SER B 102 ? 1.062 1.635 1.221 0.095  -0.028 -0.257 102 SER CCC O   
2478  C CB  . SER B 102 ? 1.098 1.743 1.278 0.131  -0.047 -0.282 102 SER CCC CB  
2479  O OG  . SER B 102 ? 1.152 1.810 1.348 0.108  -0.038 -0.279 102 SER CCC OG  
2480  N N   . ASP B 103 ? 1.100 1.644 1.232 0.115  -0.048 -0.263 103 ASP CCC N   
2481  C CA  . ASP B 103 ? 1.082 1.601 1.206 0.099  -0.042 -0.256 103 ASP CCC CA  
2482  C C   . ASP B 103 ? 1.058 1.544 1.169 0.095  -0.034 -0.245 103 ASP CCC C   
2483  O O   . ASP B 103 ? 1.072 1.552 1.189 0.081  -0.024 -0.237 103 ASP CCC O   
2484  C CB  . ASP B 103 ? 1.113 1.614 1.220 0.104  -0.053 -0.259 103 ASP CCC CB  
2485  C CG  . ASP B 103 ? 1.108 1.645 1.232 0.105  -0.062 -0.270 103 ASP CCC CG  
2486  O OD1 . ASP B 103 ? 1.094 1.658 1.240 0.090  -0.055 -0.272 103 ASP CCC OD1 
2487  O OD2 . ASP B 103 ? 1.151 1.688 1.264 0.121  -0.076 -0.278 103 ASP CCC OD2 
2488  N N   . ILE B 104 ? 0.984 1.450 1.077 0.107  -0.039 -0.244 104 ILE CCC N   
2489  C CA  . ILE B 104 ? 0.964 1.404 1.047 0.102  -0.033 -0.234 104 ILE CCC CA  
2490  C C   . ILE B 104 ? 0.953 1.411 1.054 0.093  -0.024 -0.230 104 ILE CCC C   
2491  O O   . ILE B 104 ? 0.889 1.336 0.992 0.083  -0.016 -0.221 104 ILE CCC O   
2492  C CB  . ILE B 104 ? 0.997 1.410 1.054 0.115  -0.043 -0.235 104 ILE CCC CB  
2493  C CG1 . ILE B 104 ? 1.041 1.427 1.074 0.120  -0.050 -0.236 104 ILE CCC CG1 
2494  C CG2 . ILE B 104 ? 0.998 1.391 1.049 0.107  -0.037 -0.226 104 ILE CCC CG2 
2495  C CD1 . ILE B 104 ? 1.176 1.524 1.177 0.129  -0.058 -0.235 104 ILE CCC CD1 
2496  N N   . ALA B 105 ? 0.917 1.403 1.030 0.099  -0.025 -0.236 105 ALA CCC N   
2497  C CA  . ALA B 105 ? 0.888 1.389 1.015 0.091  -0.016 -0.233 105 ALA CCC CA  
2498  C C   . ALA B 105 ? 0.889 1.404 1.031 0.076  -0.006 -0.229 105 ALA CCC C   
2499  O O   . ALA B 105 ? 0.891 1.416 1.041 0.069  0.001  -0.225 105 ALA CCC O   
2500  C CB  . ALA B 105 ? 0.907 1.434 1.039 0.102  -0.018 -0.241 105 ALA CCC CB  
2501  N N   . GLY B 106 ? 0.954 1.466 1.098 0.070  -0.007 -0.230 106 GLY CCC N   
2502  C CA  . GLY B 106 ? 0.979 1.496 1.133 0.055  0.002  -0.227 106 GLY CCC CA  
2503  C C   . GLY B 106 ? 1.032 1.581 1.202 0.047  0.005  -0.233 106 GLY CCC C   
2504  O O   . GLY B 106 ? 1.112 1.659 1.286 0.033  0.013  -0.229 106 GLY CCC O   
2505  N N   . THR B 107 ? 0.998 1.576 1.177 0.056  -0.000 -0.242 107 THR CCC N   
2506  C CA  . THR B 107 ? 0.986 1.602 1.184 0.048  0.004  -0.248 107 THR CCC CA  
2507  C C   . THR B 107 ? 1.013 1.647 1.222 0.039  -0.000 -0.255 107 THR CCC C   
2508  O O   . THR B 107 ? 1.080 1.732 1.301 0.022  0.007  -0.256 107 THR CCC O   
2509  C CB  . THR B 107 ? 1.023 1.668 1.228 0.063  0.002  -0.255 107 THR CCC CB  
2510  O OG1 . THR B 107 ? 1.153 1.798 1.353 0.081  -0.012 -0.262 107 THR CCC OG1 
2511  C CG2 . THR B 107 ? 1.017 1.644 1.210 0.069  0.006  -0.248 107 THR CCC CG2 
2512  N N   . THR B 108 ? 1.093 1.719 1.294 0.050  -0.013 -0.260 108 THR CCC N   
2513  C CA  . THR B 108 ? 1.150 1.792 1.359 0.045  -0.021 -0.268 108 THR CCC CA  
2514  C C   . THR B 108 ? 1.166 1.768 1.354 0.041  -0.025 -0.264 108 THR CCC C   
2515  O O   . THR B 108 ? 1.288 1.896 1.476 0.039  -0.034 -0.271 108 THR CCC O   
2516  C CB  . THR B 108 ? 1.205 1.877 1.422 0.063  -0.034 -0.279 108 THR CCC CB  
2517  O OG1 . THR B 108 ? 1.180 1.823 1.376 0.084  -0.042 -0.278 108 THR CCC OG1 
2518  C CG2 . THR B 108 ? 1.283 2.004 1.525 0.065  -0.028 -0.285 108 THR CCC CG2 
2519  N N   . SER B 109 ? 1.032 1.595 1.202 0.041  -0.018 -0.254 109 SER CCC N   
2520  C CA  . SER B 109 ? 1.001 1.527 1.151 0.039  -0.019 -0.251 109 SER CCC CA  
2521  C C   . SER B 109 ? 0.975 1.483 1.122 0.023  -0.007 -0.243 109 SER CCC C   
2522  O O   . SER B 109 ? 1.013 1.526 1.168 0.017  0.003  -0.238 109 SER CCC O   
2523  C CB  . SER B 109 ? 0.977 1.474 1.108 0.053  -0.021 -0.245 109 SER CCC CB  
2524  O OG  . SER B 109 ? 0.981 1.473 1.115 0.053  -0.012 -0.237 109 SER CCC OG  
2525  N N   . THR B 110 ? 1.004 1.487 1.136 0.017  -0.008 -0.243 110 THR CCC N   
2526  C CA  . THR B 110 ? 1.032 1.490 1.155 0.006  0.003  -0.237 110 THR CCC CA  
2527  C C   . THR B 110 ? 1.055 1.482 1.163 0.015  0.010  -0.228 110 THR CCC C   
2528  O O   . THR B 110 ? 1.107 1.527 1.208 0.027  0.006  -0.228 110 THR CCC O   
2529  C CB  . THR B 110 ? 1.124 1.569 1.235 -0.006 -0.001 -0.243 110 THR CCC CB  
2530  O OG1 . THR B 110 ? 1.162 1.585 1.254 0.005  -0.007 -0.245 110 THR CCC OG1 
2531  C CG2 . THR B 110 ? 1.285 1.766 1.414 -0.017 -0.009 -0.252 110 THR CCC CG2 
2532  N N   . LEU B 111 ? 1.027 1.435 1.130 0.010  0.020  -0.221 111 LEU CCC N   
2533  C CA  . LEU B 111 ? 0.999 1.384 1.093 0.019  0.028  -0.213 111 LEU CCC CA  
2534  C C   . LEU B 111 ? 1.098 1.461 1.172 0.024  0.025  -0.215 111 LEU CCC C   
2535  O O   . LEU B 111 ? 1.126 1.481 1.194 0.033  0.027  -0.211 111 LEU CCC O   
2536  C CB  . LEU B 111 ? 1.005 1.373 1.095 0.014  0.038  -0.206 111 LEU CCC CB  
2537  C CG  . LEU B 111 ? 1.052 1.400 1.134 0.024  0.046  -0.198 111 LEU CCC CG  
2538  C CD1 . LEU B 111 ? 0.936 1.300 1.031 0.032  0.045  -0.194 111 LEU CCC CD1 
2539  C CD2 . LEU B 111 ? 1.241 1.572 1.317 0.023  0.055  -0.193 111 LEU CCC CD2 
2540  N N   . GLN B 112 ? 1.141 1.493 1.202 0.018  0.021  -0.222 112 GLN CCC N   
2541  C CA  . GLN B 112 ? 1.133 1.460 1.171 0.023  0.019  -0.225 112 GLN CCC CA  
2542  C C   . GLN B 112 ? 1.106 1.441 1.141 0.032  0.009  -0.228 112 GLN CCC C   
2543  O O   . GLN B 112 ? 1.109 1.424 1.127 0.040  0.012  -0.225 112 GLN CCC O   
2544  C CB  . GLN B 112 ? 1.383 1.696 1.406 0.013  0.014  -0.232 112 GLN CCC CB  
2545  C CG  . GLN B 112 ? 1.695 1.972 1.696 0.012  0.025  -0.229 112 GLN CCC CG  
2546  C CD  . GLN B 112 ? 1.880 2.156 1.891 0.008  0.035  -0.222 112 GLN CCC CD  
2547  O OE1 . GLN B 112 ? 1.965 2.258 1.990 -0.003 0.033  -0.223 112 GLN CCC OE1 
2548  N NE2 . GLN B 112 ? 1.813 2.070 1.817 0.018  0.047  -0.215 112 GLN CCC NE2 
2549  N N   . GLU B 113 ? 1.089 1.452 1.139 0.032  -0.002 -0.234 113 GLU CCC N   
2550  C CA  . GLU B 113 ? 1.107 1.476 1.153 0.044  -0.012 -0.237 113 GLU CCC CA  
2551  C C   . GLU B 113 ? 1.074 1.437 1.120 0.051  -0.005 -0.228 113 GLU CCC C   
2552  O O   . GLU B 113 ? 1.148 1.492 1.175 0.059  -0.008 -0.227 113 GLU CCC O   
2553  C CB  . GLU B 113 ? 1.133 1.537 1.197 0.045  -0.024 -0.245 113 GLU CCC CB  
2554  C CG  . GLU B 113 ? 1.220 1.634 1.284 0.037  -0.034 -0.255 113 GLU CCC CG  
2555  C CD  . GLU B 113 ? 1.237 1.696 1.327 0.037  -0.044 -0.263 113 GLU CCC CD  
2556  O OE1 . GLU B 113 ? 1.219 1.702 1.331 0.026  -0.037 -0.262 113 GLU CCC OE1 
2557  O OE2 . GLU B 113 ? 1.297 1.768 1.384 0.048  -0.059 -0.271 113 GLU CCC OE2 
2558  N N   . GLN B 114 ? 1.038 1.415 1.104 0.048  0.003  -0.223 114 GLN CCC N   
2559  C CA  . GLN B 114 ? 0.998 1.370 1.065 0.052  0.008  -0.215 114 GLN CCC CA  
2560  C C   . GLN B 114 ? 1.022 1.368 1.074 0.053  0.017  -0.208 114 GLN CCC C   
2561  O O   . GLN B 114 ? 1.013 1.348 1.055 0.057  0.018  -0.205 114 GLN CCC O   
2562  C CB  . GLN B 114 ? 0.919 1.310 1.008 0.048  0.014  -0.210 114 GLN CCC CB  
2563  C CG  . GLN B 114 ? 0.910 1.329 1.013 0.048  0.006  -0.216 114 GLN CCC CG  
2564  C CD  . GLN B 114 ? 0.908 1.342 1.027 0.041  0.013  -0.212 114 GLN CCC CD  
2565  O OE1 . GLN B 114 ? 0.955 1.380 1.076 0.040  0.021  -0.204 114 GLN CCC OE1 
2566  N NE2 . GLN B 114 ? 0.883 1.342 1.015 0.038  0.011  -0.218 114 GLN CCC NE2 
2567  N N   . ILE B 115 ? 1.052 1.388 1.101 0.049  0.026  -0.207 115 ILE CCC N   
2568  C CA  . ILE B 115 ? 1.027 1.341 1.061 0.051  0.037  -0.201 115 ILE CCC CA  
2569  C C   . ILE B 115 ? 1.246 1.538 1.252 0.054  0.032  -0.205 115 ILE CCC C   
2570  O O   . ILE B 115 ? 1.349 1.627 1.344 0.057  0.039  -0.200 115 ILE CCC O   
2571  C CB  . ILE B 115 ? 0.966 1.270 0.998 0.048  0.046  -0.201 115 ILE CCC CB  
2572  C CG1 . ILE B 115 ? 0.934 1.253 0.987 0.046  0.051  -0.195 115 ILE CCC CG1 
2573  C CG2 . ILE B 115 ? 0.999 1.280 1.012 0.053  0.058  -0.197 115 ILE CCC CG2 
2574  C CD1 . ILE B 115 ? 0.989 1.296 1.038 0.044  0.057  -0.196 115 ILE CCC CD1 
2575  N N   . GLY B 116 ? 1.460 1.750 1.456 0.055  0.021  -0.213 116 GLY CCC N   
2576  C CA  . GLY B 116 ? 1.567 1.833 1.533 0.060  0.014  -0.217 116 GLY CCC CA  
2577  C C   . GLY B 116 ? 1.593 1.854 1.551 0.066  0.009  -0.214 116 GLY CCC C   
2578  O O   . GLY B 116 ? 1.732 1.966 1.663 0.068  0.013  -0.211 116 GLY CCC O   
2579  N N   . TRP B 117 ? 1.260 1.543 1.236 0.068  0.001  -0.215 117 TRP CCC N   
2580  C CA  . TRP B 117 ? 1.241 1.513 1.204 0.074  -0.004 -0.213 117 TRP CCC CA  
2581  C C   . TRP B 117 ? 1.283 1.544 1.245 0.068  0.009  -0.203 117 TRP CCC C   
2582  O O   . TRP B 117 ? 1.379 1.614 1.315 0.068  0.011  -0.199 117 TRP CCC O   
2583  C CB  . TRP B 117 ? 1.221 1.519 1.204 0.078  -0.015 -0.217 117 TRP CCC CB  
2584  C CG  . TRP B 117 ? 1.226 1.539 1.210 0.085  -0.030 -0.228 117 TRP CCC CG  
2585  C CD1 . TRP B 117 ? 1.414 1.712 1.375 0.093  -0.041 -0.234 117 TRP CCC CD1 
2586  C CD2 . TRP B 117 ? 1.175 1.526 1.189 0.085  -0.035 -0.234 117 TRP CCC CD2 
2587  N NE1 . TRP B 117 ? 1.417 1.743 1.393 0.098  -0.054 -0.244 117 TRP CCC NE1 
2588  C CE2 . TRP B 117 ? 1.253 1.613 1.262 0.092  -0.049 -0.244 117 TRP CCC CE2 
2589  C CE3 . TRP B 117 ? 1.204 1.581 1.245 0.079  -0.028 -0.232 117 TRP CCC CE3 
2590  C CZ2 . TRP B 117 ? 1.234 1.634 1.269 0.092  -0.056 -0.252 117 TRP CCC CZ2 
2591  C CZ3 . TRP B 117 ? 1.147 1.559 1.210 0.079  -0.034 -0.240 117 TRP CCC CZ3 
2592  C CH2 . TRP B 117 ? 1.124 1.549 1.186 0.085  -0.047 -0.250 117 TRP CCC CH2 
2593  N N   . MET B 118 ? 1.226 1.507 1.215 0.062  0.020  -0.198 118 MET CCC N   
2594  C CA  . MET B 118 ? 1.243 1.523 1.238 0.056  0.032  -0.189 118 MET CCC CA  
2595  C C   . MET B 118 ? 1.322 1.582 1.299 0.053  0.045  -0.185 118 MET CCC C   
2596  O O   . MET B 118 ? 1.378 1.631 1.351 0.048  0.054  -0.178 118 MET CCC O   
2597  C CB  . MET B 118 ? 1.219 1.526 1.247 0.052  0.037  -0.186 118 MET CCC CB  
2598  C CG  . MET B 118 ? 1.200 1.525 1.242 0.054  0.026  -0.188 118 MET CCC CG  
2599  S SD  . MET B 118 ? 1.127 1.480 1.201 0.051  0.030  -0.185 118 MET CCC SD  
2600  C CE  . MET B 118 ? 1.287 1.643 1.371 0.045  0.041  -0.175 118 MET CCC CE  
2601  N N   . THR B 119 ? 1.302 1.552 1.268 0.056  0.048  -0.189 119 THR CCC N   
2602  C CA  . THR B 119 ? 1.345 1.576 1.292 0.055  0.062  -0.185 119 THR CCC CA  
2603  C C   . THR B 119 ? 1.468 1.665 1.374 0.058  0.057  -0.188 119 THR CCC C   
2604  O O   . THR B 119 ? 1.612 1.790 1.496 0.059  0.069  -0.187 119 THR CCC O   
2605  C CB  . THR B 119 ? 1.348 1.583 1.302 0.058  0.070  -0.187 119 THR CCC CB  
2606  O OG1 . THR B 119 ? 1.359 1.587 1.303 0.060  0.058  -0.196 119 THR CCC OG1 
2607  C CG2 . THR B 119 ? 1.304 1.568 1.294 0.056  0.075  -0.183 119 THR CCC CG2 
2608  N N   . HIS B 120 ? 1.577 1.766 1.470 0.062  0.041  -0.192 120 HIS CCC N   
2609  C CA  . HIS B 120 ? 1.690 1.845 1.541 0.067  0.033  -0.195 120 HIS CCC CA  
2610  C C   . HIS B 120 ? 1.817 1.947 1.644 0.061  0.045  -0.187 120 HIS CCC C   
2611  O O   . HIS B 120 ? 1.839 1.983 1.686 0.053  0.054  -0.180 120 HIS CCC O   
2612  C CB  . HIS B 120 ? 1.763 1.919 1.609 0.075  0.011  -0.202 120 HIS CCC CB  
2613  C CG  . HIS B 120 ? 1.851 1.974 1.655 0.083  -0.000 -0.207 120 HIS CCC CG  
2614  N ND1 . HIS B 120 ? 1.961 2.052 1.730 0.088  -0.008 -0.205 120 HIS CCC ND1 
2615  C CD2 . HIS B 120 ? 1.953 2.066 1.739 0.087  -0.007 -0.214 120 HIS CCC CD2 
2616  C CE1 . HIS B 120 ? 2.158 2.223 1.891 0.096  -0.019 -0.210 120 HIS CCC CE1 
2617  N NE2 . HIS B 120 ? 2.220 2.299 1.964 0.096  -0.019 -0.216 120 HIS CCC NE2 
2618  N N   . ASN B 121 ? 1.990 2.083 1.774 0.064  0.044  -0.187 121 ASN CCC N   
2619  C CA  . ASN B 121 ? 2.110 2.173 1.862 0.057  0.053  -0.179 121 ASN CCC CA  
2620  C C   . ASN B 121 ? 2.270 2.296 1.980 0.066  0.034  -0.182 121 ASN CCC C   
2621  O O   . ASN B 121 ? 2.421 2.421 2.097 0.073  0.027  -0.187 121 ASN CCC O   
2622  C CB  . ASN B 121 ? 2.159 2.206 1.891 0.053  0.074  -0.175 121 ASN CCC CB  
2623  C CG  . ASN B 121 ? 2.256 2.277 1.960 0.042  0.087  -0.165 121 ASN CCC CG  
2624  O OD1 . ASN B 121 ? 2.235 2.266 1.955 0.032  0.088  -0.160 121 ASN CCC OD1 
2625  N ND2 . ASN B 121 ? 2.417 2.404 2.078 0.042  0.098  -0.163 121 ASN CCC ND2 
2626  N N   . PRO B 122 ? 2.306 2.326 2.014 0.065  0.024  -0.180 122 PRO CCC N   
2627  C CA  . PRO B 122 ? 2.111 2.157 1.854 0.056  0.029  -0.175 122 PRO CCC CA  
2628  C C   . PRO B 122 ? 1.964 2.056 1.755 0.061  0.022  -0.181 122 PRO CCC C   
2629  O O   . PRO B 122 ? 2.002 2.101 1.795 0.073  0.007  -0.190 122 PRO CCC O   
2630  C CB  . PRO B 122 ? 2.242 2.252 1.951 0.057  0.017  -0.173 122 PRO CCC CB  
2631  C CG  . PRO B 122 ? 2.453 2.415 2.106 0.064  0.013  -0.174 122 PRO CCC CG  
2632  C CD  . PRO B 122 ? 2.450 2.428 2.111 0.074  0.008  -0.182 122 PRO CCC CD  
2633  N N   . PRO B 123 ? 1.771 1.891 1.598 0.051  0.032  -0.176 123 PRO CCC N   
2634  C CA  . PRO B 123 ? 1.622 1.783 1.491 0.054  0.027  -0.181 123 PRO CCC CA  
2635  C C   . PRO B 123 ? 1.590 1.754 1.461 0.062  0.009  -0.186 123 PRO CCC C   
2636  O O   . PRO B 123 ? 1.683 1.824 1.534 0.061  0.004  -0.183 123 PRO CCC O   
2637  C CB  . PRO B 123 ? 1.571 1.756 1.472 0.042  0.042  -0.173 123 PRO CCC CB  
2638  C CG  . PRO B 123 ? 1.754 1.915 1.632 0.031  0.050  -0.166 123 PRO CCC CG  
2639  C CD  . PRO B 123 ? 1.818 1.938 1.649 0.035  0.048  -0.167 123 PRO CCC CD  
2640  N N   . ILE B 124 ? 1.463 1.653 1.355 0.071  -0.001 -0.194 124 ILE CCC N   
2641  C CA  . ILE B 124 ? 1.403 1.606 1.305 0.080  -0.015 -0.199 124 ILE CCC CA  
2642  C C   . ILE B 124 ? 1.274 1.512 1.216 0.073  -0.008 -0.197 124 ILE CCC C   
2643  O O   . ILE B 124 ? 1.228 1.494 1.196 0.073  -0.006 -0.200 124 ILE CCC O   
2644  C CB  . ILE B 124 ? 1.432 1.644 1.332 0.093  -0.030 -0.210 124 ILE CCC CB  
2645  C CG1 . ILE B 124 ? 1.529 1.704 1.387 0.101  -0.038 -0.212 124 ILE CCC CG1 
2646  C CG2 . ILE B 124 ? 1.375 1.605 1.286 0.104  -0.043 -0.216 124 ILE CCC CG2 
2647  C CD1 . ILE B 124 ? 1.609 1.796 1.466 0.112  -0.051 -0.222 124 ILE CCC CD1 
2648  N N   . PRO B 125 ? 1.225 1.461 1.171 0.066  -0.006 -0.192 125 PRO CCC N   
2649  C CA  . PRO B 125 ? 1.118 1.384 1.099 0.059  0.001  -0.188 125 PRO CCC CA  
2650  C C   . PRO B 125 ? 1.104 1.395 1.104 0.066  -0.007 -0.194 125 PRO CCC C   
2651  O O   . PRO B 125 ? 1.165 1.457 1.167 0.065  -0.012 -0.193 125 PRO CCC O   
2652  C CB  . PRO B 125 ? 1.118 1.368 1.090 0.048  0.005  -0.181 125 PRO CCC CB  
2653  C CG  . PRO B 125 ? 1.161 1.376 1.096 0.054  -0.007 -0.183 125 PRO CCC CG  
2654  C CD  . PRO B 125 ? 1.274 1.477 1.190 0.066  -0.012 -0.190 125 PRO CCC CD  
2655  N N   . VAL B 126 ? 1.074 1.385 1.087 0.071  -0.009 -0.200 126 VAL CCC N   
2656  C CA  . VAL B 126 ? 1.049 1.385 1.078 0.077  -0.016 -0.206 126 VAL CCC CA  
2657  C C   . VAL B 126 ? 1.011 1.365 1.063 0.070  -0.009 -0.201 126 VAL CCC C   
2658  O O   . VAL B 126 ? 1.110 1.476 1.167 0.074  -0.015 -0.204 126 VAL CCC O   
2659  C CB  . VAL B 126 ? 0.922 1.278 0.963 0.080  -0.018 -0.213 126 VAL CCC CB  
2660  C CG1 . VAL B 126 ? 1.051 1.392 1.069 0.090  -0.028 -0.219 126 VAL CCC CG1 
2661  C CG2 . VAL B 126 ? 0.883 1.244 0.936 0.070  -0.006 -0.208 126 VAL CCC CG2 
2662  N N   . GLY B 127 ? 1.024 1.381 1.087 0.061  0.002  -0.193 127 GLY CCC N   
2663  C CA  . GLY B 127 ? 1.003 1.375 1.085 0.055  0.006  -0.188 127 GLY CCC CA  
2664  C C   . GLY B 127 ? 1.034 1.397 1.109 0.052  0.001  -0.185 127 GLY CCC C   
2665  O O   . GLY B 127 ? 1.027 1.401 1.111 0.053  -0.003 -0.186 127 GLY CCC O   
2666  N N   . GLU B 128 ? 1.069 1.409 1.127 0.048  0.001  -0.182 128 GLU CCC N   
2667  C CA  . GLU B 128 ? 1.082 1.408 1.130 0.042  -0.004 -0.180 128 GLU CCC CA  
2668  C C   . GLU B 128 ? 1.141 1.455 1.171 0.052  -0.017 -0.187 128 GLU CCC C   
2669  O O   . GLU B 128 ? 1.232 1.544 1.260 0.050  -0.022 -0.186 128 GLU CCC O   
2670  C CB  . GLU B 128 ? 1.194 1.495 1.223 0.033  0.000  -0.175 128 GLU CCC CB  
2671  C CG  . GLU B 128 ? 1.330 1.648 1.380 0.024  0.014  -0.167 128 GLU CCC CG  
2672  C CD  . GLU B 128 ? 1.415 1.762 1.495 0.018  0.016  -0.163 128 GLU CCC CD  
2673  O OE1 . GLU B 128 ? 1.549 1.894 1.629 0.010  0.011  -0.161 128 GLU CCC OE1 
2674  O OE2 . GLU B 128 ? 1.296 1.665 1.397 0.023  0.022  -0.163 128 GLU CCC OE2 
2675  N N   . ILE B 129 ? 1.166 1.473 1.182 0.065  -0.022 -0.194 129 ILE CCC N   
2676  C CA  . ILE B 129 ? 1.164 1.462 1.163 0.078  -0.034 -0.201 129 ILE CCC CA  
2677  C C   . ILE B 129 ? 1.085 1.413 1.105 0.083  -0.034 -0.205 129 ILE CCC C   
2678  O O   . ILE B 129 ? 1.175 1.496 1.186 0.087  -0.040 -0.208 129 ILE CCC O   
2679  C CB  . ILE B 129 ? 1.166 1.456 1.149 0.092  -0.040 -0.209 129 ILE CCC CB  
2680  C CG1 . ILE B 129 ? 1.250 1.503 1.204 0.088  -0.040 -0.204 129 ILE CCC CG1 
2681  C CG2 . ILE B 129 ? 1.243 1.530 1.212 0.110  -0.052 -0.218 129 ILE CCC CG2 
2682  C CD1 . ILE B 129 ? 1.267 1.515 1.210 0.099  -0.045 -0.210 129 ILE CCC CD1 
2683  N N   . TYR B 130 ? 1.326 1.684 1.372 0.081  -0.027 -0.205 130 TYR CCC N   
2684  C CA  . TYR B 130 ? 1.066 1.450 1.129 0.083  -0.025 -0.207 130 TYR CCC CA  
2685  C C   . TYR B 130 ? 1.099 1.481 1.166 0.074  -0.024 -0.201 130 TYR CCC C   
2686  O O   . TYR B 130 ? 1.317 1.706 1.382 0.079  -0.027 -0.205 130 TYR CCC O   
2687  C CB  . TYR B 130 ? 0.964 1.373 1.050 0.078  -0.016 -0.207 130 TYR CCC CB  
2688  C CG  . TYR B 130 ? 0.911 1.348 1.012 0.079  -0.014 -0.210 130 TYR CCC CG  
2689  C CD1 . TYR B 130 ? 0.940 1.385 1.035 0.090  -0.019 -0.217 130 TYR CCC CD1 
2690  C CD2 . TYR B 130 ? 0.854 1.306 0.971 0.070  -0.005 -0.206 130 TYR CCC CD2 
2691  C CE1 . TYR B 130 ? 0.906 1.376 1.013 0.090  -0.014 -0.219 130 TYR CCC CE1 
2692  C CE2 . TYR B 130 ? 0.795 1.269 0.923 0.069  -0.001 -0.208 130 TYR CCC CE2 
2693  C CZ  . TYR B 130 ? 0.815 1.299 0.939 0.078  -0.005 -0.215 130 TYR CCC CZ  
2694  O OH  . TYR B 130 ? 0.966 1.473 1.099 0.076  0.001  -0.217 130 TYR CCC OH  
2695  N N   . LYS B 131 ? 0.974 1.350 1.046 0.063  -0.019 -0.193 131 LYS CCC N   
2696  C CA  . LYS B 131 ? 0.969 1.346 1.046 0.055  -0.021 -0.188 131 LYS CCC CA  
2697  C C   . LYS B 131 ? 1.112 1.466 1.166 0.056  -0.031 -0.191 131 LYS CCC C   
2698  O O   . LYS B 131 ? 1.161 1.518 1.214 0.055  -0.035 -0.191 131 LYS CCC O   
2699  C CB  . LYS B 131 ? 0.983 1.361 1.072 0.043  -0.014 -0.179 131 LYS CCC CB  
2700  C CG  . LYS B 131 ? 0.986 1.377 1.090 0.035  -0.015 -0.174 131 LYS CCC CG  
2701  C CD  . LYS B 131 ? 0.870 1.272 0.992 0.025  -0.007 -0.166 131 LYS CCC CD  
2702  C CE  . LYS B 131 ? 0.972 1.357 1.083 0.017  -0.005 -0.164 131 LYS CCC CE  
2703  N NZ  . LYS B 131 ? 1.026 1.425 1.155 0.013  0.007  -0.158 131 LYS CCC NZ  
2704  N N   . ARG B 132 ? 1.116 1.444 1.147 0.059  -0.036 -0.194 132 ARG CCC N   
2705  C CA  . ARG B 132 ? 1.186 1.483 1.186 0.063  -0.047 -0.198 132 ARG CCC CA  
2706  C C   . ARG B 132 ? 1.151 1.457 1.147 0.079  -0.052 -0.206 132 ARG CCC C   
2707  O O   . ARG B 132 ? 1.179 1.473 1.161 0.079  -0.058 -0.208 132 ARG CCC O   
2708  C CB  . ARG B 132 ? 1.248 1.512 1.220 0.067  -0.051 -0.199 132 ARG CCC CB  
2709  C CG  . ARG B 132 ? 1.451 1.703 1.424 0.050  -0.045 -0.191 132 ARG CCC CG  
2710  C CD  . ARG B 132 ? 1.713 1.925 1.650 0.052  -0.048 -0.191 132 ARG CCC CD  
2711  N NE  . ARG B 132 ? 1.965 2.173 1.906 0.035  -0.038 -0.183 132 ARG CCC NE  
2712  C CZ  . ARG B 132 ? 2.003 2.187 1.922 0.036  -0.036 -0.182 132 ARG CCC CZ  
2713  N NH1 . ARG B 132 ? 2.004 2.164 1.895 0.054  -0.045 -0.188 132 ARG CCC NH1 
2714  N NH2 . ARG B 132 ? 2.103 2.288 2.028 0.021  -0.025 -0.174 132 ARG CCC NH2 
2715  N N   . TRP B 133 ? 1.135 1.462 1.141 0.091  -0.048 -0.212 133 TRP CCC N   
2716  C CA  . TRP B 133 ? 1.094 1.435 1.098 0.106  -0.051 -0.220 133 TRP CCC CA  
2717  C C   . TRP B 133 ? 1.048 1.410 1.067 0.099  -0.046 -0.217 133 TRP CCC C   
2718  O O   . TRP B 133 ? 1.065 1.421 1.070 0.106  -0.050 -0.221 133 TRP CCC O   
2719  C CB  . TRP B 133 ? 1.035 1.404 1.054 0.117  -0.047 -0.226 133 TRP CCC CB  
2720  C CG  . TRP B 133 ? 1.142 1.493 1.145 0.127  -0.054 -0.230 133 TRP CCC CG  
2721  C CD1 . TRP B 133 ? 1.241 1.551 1.212 0.129  -0.062 -0.230 133 TRP CCC CD1 
2722  C CD2 . TRP B 133 ? 1.121 1.494 1.136 0.134  -0.053 -0.235 133 TRP CCC CD2 
2723  N NE1 . TRP B 133 ? 1.228 1.531 1.189 0.140  -0.067 -0.234 133 TRP CCC NE1 
2724  C CE2 . TRP B 133 ? 1.153 1.496 1.142 0.143  -0.062 -0.237 133 TRP CCC CE2 
2725  C CE3 . TRP B 133 ? 1.087 1.500 1.131 0.133  -0.046 -0.238 133 TRP CCC CE3 
2726  C CZ2 . TRP B 133 ? 1.142 1.496 1.135 0.152  -0.066 -0.243 133 TRP CCC CZ2 
2727  C CZ3 . TRP B 133 ? 1.055 1.481 1.104 0.140  -0.049 -0.244 133 TRP CCC CZ3 
2728  C CH2 . TRP B 133 ? 1.117 1.515 1.142 0.150  -0.060 -0.246 133 TRP CCC CH2 
2729  N N   . ILE B 134 ? 1.577 1.957 1.620 0.087  -0.038 -0.209 134 ILE CCC N   
2730  C CA  . ILE B 134 ? 1.047 1.444 1.102 0.081  -0.034 -0.206 134 ILE CCC CA  
2731  C C   . ILE B 134 ? 1.133 1.509 1.173 0.076  -0.042 -0.203 134 ILE CCC C   
2732  O O   . ILE B 134 ? 1.071 1.448 1.103 0.079  -0.045 -0.205 134 ILE CCC O   
2733  C CB  . ILE B 134 ? 0.933 1.347 1.013 0.071  -0.025 -0.198 134 ILE CCC CB  
2734  C CG1 . ILE B 134 ? 0.881 1.315 0.973 0.075  -0.017 -0.202 134 ILE CCC CG1 
2735  C CG2 . ILE B 134 ? 0.901 1.325 0.987 0.066  -0.023 -0.193 134 ILE CCC CG2 
2736  C CD1 . ILE B 134 ? 0.817 1.259 0.927 0.066  -0.009 -0.195 134 ILE CCC CD1 
2737  N N   . ILE B 135 ? 1.071 1.428 1.106 0.066  -0.047 -0.198 135 ILE CCC N   
2738  C CA  . ILE B 135 ? 1.034 1.372 1.056 0.057  -0.056 -0.196 135 ILE CCC CA  
2739  C C   . ILE B 135 ? 1.168 1.478 1.155 0.067  -0.065 -0.204 135 ILE CCC C   
2740  O O   . ILE B 135 ? 1.249 1.551 1.224 0.066  -0.072 -0.206 135 ILE CCC O   
2741  C CB  . ILE B 135 ? 0.971 1.298 0.996 0.041  -0.056 -0.189 135 ILE CCC CB  
2742  C CG1 . ILE B 135 ? 0.889 1.245 0.947 0.033  -0.048 -0.181 135 ILE CCC CG1 
2743  C CG2 . ILE B 135 ? 1.076 1.379 1.083 0.030  -0.067 -0.189 135 ILE CCC CG2 
2744  C CD1 . ILE B 135 ? 1.027 1.381 1.094 0.020  -0.044 -0.175 135 ILE CCC CD1 
2745  N N   . LEU B 136 ? 1.129 1.424 1.099 0.080  -0.067 -0.211 136 LEU CCC N   
2746  C CA  . LEU B 136 ? 1.227 1.497 1.164 0.095  -0.075 -0.220 136 LEU CCC CA  
2747  C C   . LEU B 136 ? 1.209 1.501 1.150 0.106  -0.072 -0.225 136 LEU CCC C   
2748  O O   . LEU B 136 ? 1.251 1.523 1.167 0.111  -0.079 -0.229 136 LEU CCC O   
2749  C CB  . LEU B 136 ? 1.283 1.542 1.207 0.112  -0.076 -0.227 136 LEU CCC CB  
2750  C CG  . LEU B 136 ? 1.451 1.671 1.353 0.103  -0.082 -0.223 136 LEU CCC CG  
2751  C CD1 . LEU B 136 ? 1.480 1.692 1.369 0.121  -0.084 -0.229 136 LEU CCC CD1 
2752  C CD2 . LEU B 136 ? 1.537 1.711 1.401 0.098  -0.094 -0.224 136 LEU CCC CD2 
2753  N N   . GLY B 137 ? 1.157 1.488 1.127 0.109  -0.061 -0.224 137 GLY CCC N   
2754  C CA  . GLY B 137 ? 1.104 1.456 1.077 0.116  -0.055 -0.228 137 GLY CCC CA  
2755  C C   . GLY B 137 ? 1.096 1.445 1.067 0.104  -0.057 -0.222 137 GLY CCC C   
2756  O O   . GLY B 137 ? 1.258 1.600 1.209 0.112  -0.059 -0.226 137 GLY CCC O   
2757  N N   . LEU B 138 ? 1.131 1.484 1.120 0.088  -0.057 -0.212 138 LEU CCC N   
2758  C CA  . LEU B 138 ? 1.042 1.395 1.032 0.078  -0.061 -0.206 138 LEU CCC CA  
2759  C C   . LEU B 138 ? 1.147 1.467 1.106 0.076  -0.075 -0.209 138 LEU CCC C   
2760  O O   . LEU B 138 ? 1.189 1.504 1.134 0.076  -0.080 -0.210 138 LEU CCC O   
2761  C CB  . LEU B 138 ? 0.888 1.255 0.905 0.064  -0.059 -0.196 138 LEU CCC CB  
2762  C CG  . LEU B 138 ? 0.828 1.223 0.870 0.065  -0.046 -0.192 138 LEU CCC CG  
2763  C CD1 . LEU B 138 ? 0.812 1.217 0.879 0.054  -0.044 -0.183 138 LEU CCC CD1 
2764  C CD2 . LEU B 138 ? 0.823 1.230 0.862 0.069  -0.041 -0.192 138 LEU CCC CD2 
2765  N N   . ASN B 139 ? 1.272 1.566 1.217 0.073  -0.082 -0.212 139 ASN CCC N   
2766  C CA  . ASN B 139 ? 1.350 1.605 1.260 0.070  -0.096 -0.215 139 ASN CCC CA  
2767  C C   . ASN B 139 ? 1.461 1.703 1.341 0.088  -0.098 -0.225 139 ASN CCC C   
2768  O O   . ASN B 139 ? 1.627 1.848 1.483 0.085  -0.108 -0.227 139 ASN CCC O   
2769  C CB  . ASN B 139 ? 1.388 1.611 1.281 0.066  -0.102 -0.217 139 ASN CCC CB  
2770  C CG  . ASN B 139 ? 1.478 1.710 1.395 0.045  -0.101 -0.207 139 ASN CCC CG  
2771  O OD1 . ASN B 139 ? 1.390 1.657 1.342 0.039  -0.092 -0.200 139 ASN CCC OD1 
2772  N ND2 . ASN B 139 ? 1.744 1.942 1.640 0.033  -0.109 -0.207 139 ASN CCC ND2 
2773  N N   . LYS B 140 ? 1.400 1.653 1.279 0.107  -0.090 -0.232 140 LYS CCC N   
2774  C CA  . LYS B 140 ? 1.464 1.709 1.316 0.126  -0.089 -0.241 140 LYS CCC CA  
2775  C C   . LYS B 140 ? 1.429 1.694 1.286 0.123  -0.084 -0.239 140 LYS CCC C   
2776  O O   . LYS B 140 ? 1.642 1.886 1.468 0.128  -0.090 -0.243 140 LYS CCC O   
2777  C CB  . LYS B 140 ? 1.455 1.721 1.315 0.147  -0.079 -0.249 140 LYS CCC CB  
2778  C CG  . LYS B 140 ? 1.569 1.810 1.412 0.157  -0.086 -0.254 140 LYS CCC CG  
2779  C CD  . LYS B 140 ? 1.587 1.857 1.441 0.180  -0.077 -0.263 140 LYS CCC CD  
2780  C CE  . LYS B 140 ? 1.623 1.864 1.453 0.197  -0.086 -0.270 140 LYS CCC CE  
2781  N NZ  . LYS B 140 ? 1.683 1.962 1.532 0.218  -0.078 -0.278 140 LYS CCC NZ  
2782  N N   . ILE B 141 ? 1.307 1.607 1.199 0.114  -0.074 -0.230 141 ILE CCC N   
2783  C CA  . ILE B 141 ? 1.311 1.627 1.205 0.111  -0.070 -0.227 141 ILE CCC CA  
2784  C C   . ILE B 141 ? 1.462 1.756 1.340 0.099  -0.084 -0.222 141 ILE CCC C   
2785  O O   . ILE B 141 ? 1.532 1.816 1.386 0.103  -0.086 -0.225 141 ILE CCC O   
2786  C CB  . ILE B 141 ? 1.211 1.563 1.143 0.104  -0.057 -0.219 141 ILE CCC CB  
2787  C CG1 . ILE B 141 ? 1.156 1.533 1.101 0.115  -0.043 -0.224 141 ILE CCC CG1 
2788  C CG2 . ILE B 141 ? 1.269 1.629 1.198 0.099  -0.054 -0.213 141 ILE CCC CG2 
2789  C CD1 . ILE B 141 ? 1.256 1.660 1.235 0.106  -0.033 -0.218 141 ILE CCC CD1 
2790  N N   . VAL B 142 ? 1.489 1.776 1.380 0.083  -0.093 -0.216 142 VAL CCC N   
2791  C CA  . VAL B 142 ? 1.477 1.748 1.357 0.071  -0.109 -0.213 142 VAL CCC CA  
2792  C C   . VAL B 142 ? 1.475 1.706 1.309 0.077  -0.120 -0.222 142 VAL CCC C   
2793  O O   . VAL B 142 ? 1.590 1.808 1.403 0.074  -0.130 -0.223 142 VAL CCC O   
2794  C CB  . VAL B 142 ? 1.398 1.674 1.303 0.052  -0.116 -0.206 142 VAL CCC CB  
2795  C CG1 . VAL B 142 ? 1.334 1.645 1.279 0.050  -0.103 -0.198 142 VAL CCC CG1 
2796  C CG2 . VAL B 142 ? 1.471 1.716 1.358 0.048  -0.122 -0.210 142 VAL CCC CG2 
2797  N N   . ARG B 143 ? 1.557 1.764 1.371 0.086  -0.121 -0.230 143 ARG CCC N   
2798  C CA  . ARG B 143 ? 1.688 1.851 1.453 0.094  -0.132 -0.240 143 ARG CCC CA  
2799  C C   . ARG B 143 ? 1.731 1.898 1.474 0.112  -0.125 -0.246 143 ARG CCC C   
2800  O O   . ARG B 143 ? 1.870 2.009 1.578 0.113  -0.135 -0.250 143 ARG CCC O   
2801  C CB  . ARG B 143 ? 1.763 1.897 1.508 0.104  -0.134 -0.247 143 ARG CCC CB  
2802  C CG  . ARG B 143 ? 1.992 2.072 1.680 0.112  -0.147 -0.257 143 ARG CCC CG  
2803  C CD  . ARG B 143 ? 2.186 2.227 1.848 0.120  -0.151 -0.263 143 ARG CCC CD  
2804  N NE  . ARG B 143 ? 2.232 2.295 1.904 0.146  -0.138 -0.268 143 ARG CCC NE  
2805  C CZ  . ARG B 143 ? 2.211 2.297 1.913 0.146  -0.130 -0.265 143 ARG CCC CZ  
2806  N NH1 . ARG B 143 ? 2.149 2.237 1.874 0.123  -0.133 -0.255 143 ARG CCC NH1 
2807  N NH2 . ARG B 143 ? 2.205 2.313 1.915 0.170  -0.120 -0.271 143 ARG CCC NH2 
2808  N N   . MET B 144 ? 1.651 1.852 1.415 0.126  -0.107 -0.247 144 MET CCC N   
2809  C CA  . MET B 144 ? 1.644 1.851 1.388 0.142  -0.097 -0.253 144 MET CCC CA  
2810  C C   . MET B 144 ? 1.660 1.872 1.400 0.132  -0.100 -0.246 144 MET CCC C   
2811  O O   . MET B 144 ? 1.825 2.019 1.528 0.141  -0.101 -0.252 144 MET CCC O   
2812  C CB  . MET B 144 ? 1.622 1.872 1.395 0.153  -0.077 -0.254 144 MET CCC CB  
2813  C CG  . MET B 144 ? 1.683 1.937 1.467 0.164  -0.074 -0.260 144 MET CCC CG  
2814  S SD  . MET B 144 ? 2.106 2.347 1.856 0.196  -0.071 -0.276 144 MET CCC SD  
2815  C CE  . MET B 144 ? 2.003 2.232 1.761 0.202  -0.078 -0.278 144 MET CCC CE  
2816  N N   . TYR B 145 ? 1.593 1.825 1.366 0.115  -0.101 -0.235 145 TYR CCC N   
2817  C CA  . TYR B 145 ? 1.628 1.867 1.400 0.107  -0.104 -0.227 145 TYR CCC CA  
2818  C C   . TYR B 145 ? 1.657 1.869 1.411 0.094  -0.127 -0.226 145 TYR CCC C   
2819  O O   . TYR B 145 ? 1.714 1.932 1.468 0.087  -0.133 -0.219 145 TYR CCC O   
2820  C CB  . TYR B 145 ? 1.563 1.839 1.379 0.098  -0.095 -0.216 145 TYR CCC CB  
2821  C CG  . TYR B 145 ? 1.517 1.820 1.347 0.107  -0.073 -0.217 145 TYR CCC CG  
2822  C CD1 . TYR B 145 ? 1.471 1.774 1.284 0.123  -0.062 -0.227 145 TYR CCC CD1 
2823  C CD2 . TYR B 145 ? 1.516 1.846 1.376 0.100  -0.063 -0.208 145 TYR CCC CD2 
2824  C CE1 . TYR B 145 ? 1.420 1.754 1.250 0.129  -0.043 -0.228 145 TYR CCC CE1 
2825  C CE2 . TYR B 145 ? 1.511 1.865 1.383 0.105  -0.043 -0.208 145 TYR CCC CE2 
2826  C CZ  . TYR B 145 ? 1.442 1.802 1.301 0.118  -0.033 -0.219 145 TYR CCC CZ  
2827  O OH  . TYR B 145 ? 1.369 1.758 1.244 0.121  -0.014 -0.220 145 TYR CCC OH  
2828  N N   . SER B 146 ? 1.444 1.594 1.729 0.036  -0.144 -0.348 146 SER CCC N   
2829  C CA  . SER B 146 ? 1.491 1.638 1.734 0.034  -0.137 -0.340 146 SER CCC CA  
2830  C C   . SER B 146 ? 1.611 1.789 1.849 0.014  -0.116 -0.333 146 SER CCC C   
2831  O O   . SER B 146 ? 1.660 1.864 1.914 0.013  -0.105 -0.350 146 SER CCC O   
2832  C CB  . SER B 146 ? 1.492 1.628 1.714 0.050  -0.142 -0.357 146 SER CCC CB  
2833  O OG  . SER B 146 ? 1.608 1.742 1.793 0.047  -0.136 -0.350 146 SER CCC OG  
2834  N N   . PRO B 147 ? 1.657 1.836 1.873 -0.001 -0.112 -0.310 147 PRO CCC N   
2835  C CA  . PRO B 147 ? 1.710 1.923 1.918 -0.025 -0.093 -0.302 147 PRO CCC CA  
2836  C C   . PRO B 147 ? 1.720 1.951 1.901 -0.023 -0.078 -0.316 147 PRO CCC C   
2837  O O   . PRO B 147 ? 1.813 2.082 1.994 -0.039 -0.059 -0.321 147 PRO CCC O   
2838  C CB  . PRO B 147 ? 1.728 1.926 1.920 -0.042 -0.101 -0.270 147 PRO CCC CB  
2839  C CG  . PRO B 147 ? 1.622 1.784 1.802 -0.022 -0.119 -0.270 147 PRO CCC CG  
2840  C CD  . PRO B 147 ? 1.637 1.789 1.838 0.001  -0.127 -0.293 147 PRO CCC CD  
2841  N N   . THR B 148 ? 1.697 1.905 1.855 -0.005 -0.085 -0.324 148 THR CCC N   
2842  C CA  . THR B 148 ? 1.681 1.902 1.813 -0.003 -0.075 -0.335 148 THR CCC CA  
2843  C C   . THR B 148 ? 1.675 1.877 1.809 0.020  -0.087 -0.357 148 THR CCC C   
2844  O O   . THR B 148 ? 1.767 1.939 1.898 0.031  -0.103 -0.352 148 THR CCC O   
2845  C CB  . THR B 148 ? 1.726 1.937 1.818 -0.013 -0.075 -0.314 148 THR CCC CB  
2846  O OG1 . THR B 148 ? 1.881 2.056 1.963 0.000  -0.092 -0.305 148 THR CCC OG1 
2847  C CG2 . THR B 148 ? 1.734 1.957 1.821 -0.039 -0.069 -0.288 148 THR CCC CG2 
2848  N N   . SER B 149 ? 1.620 1.842 1.760 0.025  -0.081 -0.381 149 SER CCC N   
2849  C CA  . SER B 149 ? 1.680 1.880 1.818 0.043  -0.097 -0.398 149 SER CCC CA  
2850  C C   . SER B 149 ? 1.679 1.862 1.777 0.043  -0.101 -0.386 149 SER CCC C   
2851  O O   . SER B 149 ? 1.769 1.967 1.844 0.031  -0.088 -0.375 149 SER CCC O   
2852  C CB  . SER B 149 ? 1.778 2.004 1.945 0.050  -0.094 -0.432 149 SER CCC CB  
2853  O OG  . SER B 149 ? 1.795 1.997 1.954 0.065  -0.113 -0.444 149 SER CCC OG  
2854  N N   . ILE B 150 ? 1.602 1.753 1.688 0.055  -0.120 -0.385 150 ILE CCC N   
2855  C CA  A ILE B 150 ? 1.688 1.823 1.739 0.054  -0.125 -0.375 150 ILE CCC CA  
2856  C C   . ILE B 150 ? 1.765 1.919 1.810 0.053  -0.117 -0.389 150 ILE CCC C   
2857  O O   . ILE B 150 ? 1.743 1.895 1.758 0.047  -0.113 -0.378 150 ILE CCC O   
2858  C CB  A ILE B 150 ? 1.601 1.705 1.644 0.063  -0.147 -0.374 150 ILE CCC CB  
2859  C CG1 A ILE B 150 ? 1.781 1.872 1.829 0.065  -0.154 -0.366 150 ILE CCC CG1 
2860  C CG2 A ILE B 150 ? 1.730 1.821 1.740 0.061  -0.153 -0.363 150 ILE CCC CG2 
2861  C CD1 A ILE B 150 ? 1.885 1.952 1.927 0.071  -0.176 -0.368 150 ILE CCC CD1 
2862  N N   . LEU B 151 ? 1.775 1.948 1.850 0.059  -0.116 -0.417 151 LEU CCC N   
2863  C CA  . LEU B 151 ? 1.770 1.967 1.844 0.060  -0.110 -0.438 151 LEU CCC CA  
2864  C C   . LEU B 151 ? 1.768 1.996 1.818 0.042  -0.085 -0.427 151 LEU CCC C   
2865  O O   . LEU B 151 ? 1.849 2.090 1.880 0.039  -0.079 -0.435 151 LEU CCC O   
2866  C CB  . LEU B 151 ? 1.849 2.071 1.970 0.070  -0.112 -0.476 151 LEU CCC CB  
2867  C CG  . LEU B 151 ? 1.846 2.034 1.993 0.087  -0.142 -0.488 151 LEU CCC CG  
2868  C CD1 . LEU B 151 ? 1.944 2.159 2.146 0.098  -0.146 -0.529 151 LEU CCC CD1 
2869  C CD2 . LEU B 151 ? 1.838 1.988 1.961 0.093  -0.167 -0.481 151 LEU CCC CD2 
2870  N N   . ASP B 152 ? 1.871 2.108 1.922 0.028  -0.073 -0.407 152 ASP CCC N   
2871  C CA  . ASP B 152 ? 1.930 2.191 1.957 0.007  -0.054 -0.390 152 ASP CCC CA  
2872  C C   . ASP B 152 ? 1.862 2.093 1.856 0.000  -0.061 -0.355 152 ASP CCC C   
2873  O O   . ASP B 152 ? 1.926 2.169 1.899 -0.019 -0.052 -0.336 152 ASP CCC O   
2874  C CB  . ASP B 152 ? 2.080 2.372 2.131 -0.008 -0.039 -0.388 152 ASP CCC CB  
2875  C CG  . ASP B 152 ? 2.268 2.605 2.353 -0.005 -0.027 -0.425 152 ASP CCC CG  
2876  O OD1 . ASP B 152 ? 2.348 2.689 2.440 0.010  -0.032 -0.454 152 ASP CCC OD1 
2877  O OD2 . ASP B 152 ? 2.406 2.775 2.515 -0.018 -0.013 -0.426 152 ASP CCC OD2 
2878  N N   . ILE B 153 ? 1.778 1.972 1.769 0.014  -0.079 -0.348 153 ILE CCC N   
2879  C CA  . ILE B 153 ? 1.736 1.906 1.702 0.010  -0.087 -0.323 153 ILE CCC CA  
2880  C C   . ILE B 153 ? 1.738 1.902 1.675 0.011  -0.090 -0.324 153 ILE CCC C   
2881  O O   . ILE B 153 ? 1.786 1.935 1.723 0.023  -0.101 -0.335 153 ILE CCC O   
2882  C CB  . ILE B 153 ? 1.710 1.853 1.687 0.021  -0.101 -0.317 153 ILE CCC CB  
2883  C CG1 . ILE B 153 ? 1.743 1.891 1.751 0.021  -0.100 -0.319 153 ILE CCC CG1 
2884  C CG2 . ILE B 153 ? 1.615 1.741 1.574 0.018  -0.108 -0.297 153 ILE CCC CG2 
2885  C CD1 . ILE B 153 ? 1.780 1.937 1.791 0.005  -0.094 -0.300 153 ILE CCC CD1 
2886  N N   . ARG B 154 ? 1.627 1.803 1.541 -0.003 -0.082 -0.311 154 ARG CCC N   
2887  C CA  . ARG B 154 ? 1.679 1.851 1.565 -0.004 -0.085 -0.312 154 ARG CCC CA  
2888  C C   . ARG B 154 ? 1.689 1.847 1.553 -0.015 -0.090 -0.284 154 ARG CCC C   
2889  O O   . ARG B 154 ? 1.714 1.877 1.578 -0.029 -0.087 -0.266 154 ARG CCC O   
2890  C CB  . ARG B 154 ? 1.832 2.037 1.709 -0.010 -0.071 -0.332 154 ARG CCC CB  
2891  C CG  . ARG B 154 ? 1.866 2.088 1.774 0.003  -0.069 -0.365 154 ARG CCC CG  
2892  C CD  . ARG B 154 ? 1.964 2.223 1.869 0.000  -0.058 -0.393 154 ARG CCC CD  
2893  N NE  . ARG B 154 ? 2.007 2.289 1.952 0.011  -0.055 -0.427 154 ARG CCC NE  
2894  C CZ  . ARG B 154 ? 2.071 2.391 2.034 0.001  -0.036 -0.437 154 ARG CCC CZ  
2895  N NH1 . ARG B 154 ? 2.088 2.427 2.032 -0.023 -0.020 -0.413 154 ARG CCC NH1 
2896  N NH2 . ARG B 154 ? 2.199 2.541 2.205 0.014  -0.036 -0.472 154 ARG CCC NH2 
2897  N N   . GLN B 155 ? 1.686 1.825 1.534 -0.009 -0.101 -0.279 155 GLN CCC N   
2898  C CA  . GLN B 155 ? 1.742 1.866 1.576 -0.017 -0.110 -0.256 155 GLN CCC CA  
2899  C C   . GLN B 155 ? 1.786 1.922 1.594 -0.036 -0.105 -0.244 155 GLN CCC C   
2900  O O   . GLN B 155 ? 1.801 1.954 1.589 -0.039 -0.098 -0.256 155 GLN CCC O   
2901  C CB  . GLN B 155 ? 1.745 1.851 1.572 -0.008 -0.122 -0.256 155 GLN CCC CB  
2902  C CG  . GLN B 155 ? 1.762 1.854 1.587 -0.012 -0.133 -0.237 155 GLN CCC CG  
2903  C CD  . GLN B 155 ? 1.683 1.763 1.501 -0.006 -0.143 -0.238 155 GLN CCC CD  
2904  O OE1 . GLN B 155 ? 1.779 1.859 1.589 -0.000 -0.143 -0.250 155 GLN CCC OE1 
2905  N NE2 . GLN B 155 ? 1.581 1.653 1.408 -0.006 -0.153 -0.227 155 GLN CCC NE2 
2906  N N   . GLY B 156 ? 1.866 1.995 1.675 -0.049 -0.112 -0.220 156 GLY CCC N   
2907  C CA  . GLY B 156 ? 1.929 2.064 1.709 -0.071 -0.113 -0.202 156 GLY CCC CA  
2908  C C   . GLY B 156 ? 1.975 2.096 1.730 -0.071 -0.125 -0.195 156 GLY CCC C   
2909  O O   . GLY B 156 ? 2.004 2.106 1.771 -0.055 -0.135 -0.200 156 GLY CCC O   
2910  N N   . PRO B 157 ? 2.005 2.135 1.724 -0.091 -0.124 -0.185 157 PRO CCC N   
2911  C CA  A PRO B 157 ? 2.086 2.203 1.780 -0.090 -0.136 -0.181 157 PRO CCC CA  
2912  C C   . PRO B 157 ? 2.099 2.184 1.807 -0.087 -0.160 -0.161 157 PRO CCC C   
2913  O O   . PRO B 157 ? 2.184 2.255 1.895 -0.074 -0.170 -0.167 157 PRO CCC O   
2914  C CB  A PRO B 157 ? 2.177 2.316 1.828 -0.116 -0.129 -0.173 157 PRO CCC CB  
2915  C CG  A PRO B 157 ? 2.154 2.302 1.810 -0.137 -0.126 -0.153 157 PRO CCC CG  
2916  C CD  A PRO B 157 ? 2.017 2.168 1.717 -0.118 -0.117 -0.168 157 PRO CCC CD  
2917  N N   . LYS B 158 ? 2.121 2.193 1.841 -0.099 -0.173 -0.139 158 LYS CCC N   
2918  C CA  . LYS B 158 ? 2.212 2.256 1.956 -0.094 -0.200 -0.124 158 LYS CCC CA  
2919  C C   . LYS B 158 ? 2.199 2.237 1.992 -0.075 -0.202 -0.135 158 LYS CCC C   
2920  O O   . LYS B 158 ? 2.292 2.311 2.113 -0.070 -0.224 -0.128 158 LYS CCC O   
2921  C CB  . LYS B 158 ? 2.354 2.382 2.085 -0.120 -0.221 -0.092 158 LYS CCC CB  
2922  C CG  . LYS B 158 ? 2.437 2.483 2.153 -0.144 -0.210 -0.079 158 LYS CCC CG  
2923  C CD  . LYS B 158 ? 2.555 2.583 2.247 -0.175 -0.235 -0.042 158 LYS CCC CD  
2924  C CE  . LYS B 158 ? 2.528 2.579 2.200 -0.205 -0.223 -0.025 158 LYS CCC CE  
2925  N NZ  . LYS B 158 ? 2.574 2.606 2.219 -0.241 -0.251 0.016  158 LYS CCC NZ  
2926  N N   . GLU B 159 ? 2.007 2.062 1.810 -0.064 -0.181 -0.154 159 GLU CCC N   
2927  C CA  . GLU B 159 ? 1.765 1.817 1.608 -0.048 -0.183 -0.165 159 GLU CCC CA  
2928  C C   . GLU B 159 ? 1.702 1.751 1.559 -0.030 -0.186 -0.181 159 GLU CCC C   
2929  O O   . GLU B 159 ? 1.661 1.718 1.500 -0.025 -0.175 -0.193 159 GLU CCC O   
2930  C CB  . GLU B 159 ? 1.734 1.804 1.581 -0.045 -0.162 -0.179 159 GLU CCC CB  
2931  C CG  . GLU B 159 ? 1.757 1.825 1.641 -0.031 -0.164 -0.190 159 GLU CCC CG  
2932  C CD  . GLU B 159 ? 1.702 1.785 1.592 -0.028 -0.147 -0.203 159 GLU CCC CD  
2933  O OE1 . GLU B 159 ? 1.627 1.725 1.496 -0.032 -0.133 -0.211 159 GLU CCC OE1 
2934  O OE2 . GLU B 159 ? 1.747 1.829 1.666 -0.021 -0.150 -0.208 159 GLU CCC OE2 
2935  N N   . PRO B 160 ? 1.653 1.695 1.544 -0.021 -0.201 -0.183 160 PRO CCC N   
2936  C CA  . PRO B 160 ? 1.661 1.711 1.568 -0.007 -0.200 -0.200 160 PRO CCC CA  
2937  C C   . PRO B 160 ? 1.623 1.687 1.527 0.001  -0.182 -0.216 160 PRO CCC C   
2938  O O   . PRO B 160 ? 1.748 1.814 1.659 0.003  -0.175 -0.220 160 PRO CCC O   
2939  C CB  . PRO B 160 ? 1.696 1.743 1.646 0.001  -0.218 -0.205 160 PRO CCC CB  
2940  C CG  . PRO B 160 ? 1.691 1.717 1.643 -0.012 -0.237 -0.183 160 PRO CCC CG  
2941  C CD  . PRO B 160 ? 1.663 1.691 1.581 -0.026 -0.222 -0.170 160 PRO CCC CD  
2942  N N   . PHE B 161 ? 1.511 1.581 1.404 0.005  -0.177 -0.225 161 PHE CCC N   
2943  C CA  . PHE B 161 ? 1.416 1.494 1.303 0.010  -0.165 -0.237 161 PHE CCC CA  
2944  C C   . PHE B 161 ? 1.462 1.548 1.374 0.017  -0.164 -0.247 161 PHE CCC C   
2945  O O   . PHE B 161 ? 1.430 1.518 1.340 0.020  -0.156 -0.253 161 PHE CCC O   
2946  C CB  . PHE B 161 ? 1.345 1.426 1.220 0.010  -0.166 -0.240 161 PHE CCC CB  
2947  C CG  . PHE B 161 ? 1.321 1.403 1.185 0.011  -0.161 -0.247 161 PHE CCC CG  
2948  C CD1 . PHE B 161 ? 1.380 1.455 1.230 0.012  -0.157 -0.250 161 PHE CCC CD1 
2949  C CD2 . PHE B 161 ? 1.315 1.408 1.183 0.011  -0.161 -0.253 161 PHE CCC CD2 
2950  C CE1 . PHE B 161 ? 1.314 1.385 1.159 0.013  -0.158 -0.257 161 PHE CCC CE1 
2951  C CE2 . PHE B 161 ? 1.276 1.366 1.133 0.008  -0.162 -0.255 161 PHE CCC CE2 
2952  C CZ  . PHE B 161 ? 1.278 1.354 1.125 0.011  -0.162 -0.257 161 PHE CCC CZ  
2953  N N   . ARG B 162 ? 1.534 1.628 1.473 0.022  -0.172 -0.252 162 ARG CCC N   
2954  C CA  . ARG B 162 ? 1.567 1.673 1.531 0.029  -0.171 -0.266 162 ARG CCC CA  
2955  C C   . ARG B 162 ? 1.538 1.634 1.510 0.030  -0.171 -0.263 162 ARG CCC C   
2956  O O   . ARG B 162 ? 1.640 1.742 1.617 0.034  -0.165 -0.272 162 ARG CCC O   
2957  C CB  . ARG B 162 ? 1.657 1.775 1.658 0.036  -0.183 -0.278 162 ARG CCC CB  
2958  C CG  . ARG B 162 ? 1.858 1.995 1.863 0.035  -0.183 -0.286 162 ARG CCC CG  
2959  C CD  . ARG B 162 ? 1.805 1.965 1.856 0.044  -0.192 -0.308 162 ARG CCC CD  
2960  N NE  . ARG B 162 ? 1.899 2.042 1.983 0.050  -0.212 -0.306 162 ARG CCC NE  
2961  C CZ  . ARG B 162 ? 1.938 2.076 2.047 0.057  -0.219 -0.313 162 ARG CCC CZ  
2962  N NH1 . ARG B 162 ? 1.883 2.033 1.986 0.060  -0.206 -0.324 162 ARG CCC NH1 
2963  N NH2 . ARG B 162 ? 2.029 2.146 2.169 0.060  -0.243 -0.307 162 ARG CCC NH2 
2964  N N   . ASP B 163 ? 1.483 1.565 1.455 0.023  -0.177 -0.247 163 ASP CCC N   
2965  C CA  . ASP B 163 ? 1.502 1.578 1.484 0.020  -0.177 -0.241 163 ASP CCC CA  
2966  C C   . ASP B 163 ? 1.510 1.589 1.470 0.017  -0.161 -0.243 163 ASP CCC C   
2967  O O   . ASP B 163 ? 1.566 1.648 1.539 0.019  -0.158 -0.248 163 ASP CCC O   
2968  C CB  . ASP B 163 ? 1.607 1.668 1.589 0.007  -0.190 -0.221 163 ASP CCC CB  
2969  C CG  . ASP B 163 ? 1.758 1.811 1.774 0.012  -0.213 -0.221 163 ASP CCC CG  
2970  O OD1 . ASP B 163 ? 1.829 1.892 1.875 0.025  -0.218 -0.240 163 ASP CCC OD1 
2971  O OD2 . ASP B 163 ? 1.760 1.798 1.771 0.002  -0.228 -0.203 163 ASP CCC OD2 
2972  N N   . TYR B 164 ? 1.460 1.541 1.390 0.012  -0.153 -0.241 164 TYR CCC N   
2973  C CA  . TYR B 164 ? 1.427 1.513 1.344 0.013  -0.142 -0.248 164 TYR CCC CA  
2974  C C   . TYR B 164 ? 1.449 1.537 1.375 0.023  -0.141 -0.263 164 TYR CCC C   
2975  O O   . TYR B 164 ? 1.486 1.576 1.421 0.026  -0.137 -0.270 164 TYR CCC O   
2976  C CB  . TYR B 164 ? 1.410 1.496 1.298 0.008  -0.138 -0.248 164 TYR CCC CB  
2977  C CG  . TYR B 164 ? 1.385 1.474 1.266 0.014  -0.132 -0.262 164 TYR CCC CG  
2978  C CD1 . TYR B 164 ? 1.470 1.569 1.359 0.014  -0.124 -0.271 164 TYR CCC CD1 
2979  C CD2 . TYR B 164 ? 1.422 1.504 1.291 0.018  -0.138 -0.267 164 TYR CCC CD2 
2980  C CE1 . TYR B 164 ? 1.496 1.596 1.386 0.020  -0.124 -0.288 164 TYR CCC CE1 
2981  C CE2 . TYR B 164 ? 1.424 1.504 1.291 0.022  -0.140 -0.279 164 TYR CCC CE2 
2982  C CZ  . TYR B 164 ? 1.446 1.534 1.325 0.025  -0.134 -0.291 164 TYR CCC CZ  
2983  O OH  . TYR B 164 ? 1.479 1.563 1.362 0.031  -0.140 -0.307 164 TYR CCC OH  
2984  N N   . VAL B 165 ? 1.401 1.490 1.324 0.026  -0.146 -0.266 165 VAL CCC N   
2985  C CA  . VAL B 165 ? 1.344 1.436 1.268 0.031  -0.147 -0.277 165 VAL CCC CA  
2986  C C   . VAL B 165 ? 1.307 1.404 1.256 0.037  -0.148 -0.284 165 VAL CCC C   
2987  O O   . VAL B 165 ? 1.351 1.447 1.302 0.040  -0.149 -0.292 165 VAL CCC O   
2988  C CB  . VAL B 165 ? 1.308 1.407 1.221 0.028  -0.150 -0.277 165 VAL CCC CB  
2989  C CG1 . VAL B 165 ? 1.377 1.483 1.286 0.028  -0.151 -0.285 165 VAL CCC CG1 
2990  C CG2 . VAL B 165 ? 1.294 1.386 1.185 0.023  -0.151 -0.270 165 VAL CCC CG2 
2991  N N   . ASP B 166 ? 1.286 1.386 1.257 0.038  -0.153 -0.283 166 ASP CCC N   
2992  C CA  . ASP B 166 ? 1.298 1.400 1.298 0.044  -0.158 -0.291 166 ASP CCC CA  
2993  C C   . ASP B 166 ? 1.363 1.457 1.367 0.043  -0.155 -0.288 166 ASP CCC C   
2994  O O   . ASP B 166 ? 1.458 1.554 1.475 0.048  -0.156 -0.298 166 ASP CCC O   
2995  C CB  . ASP B 166 ? 1.336 1.437 1.363 0.046  -0.170 -0.289 166 ASP CCC CB  
2996  C CG  . ASP B 166 ? 1.430 1.547 1.471 0.052  -0.175 -0.304 166 ASP CCC CG  
2997  O OD1 . ASP B 166 ? 1.468 1.601 1.496 0.054  -0.168 -0.316 166 ASP CCC OD1 
2998  O OD2 . ASP B 166 ? 1.487 1.603 1.551 0.054  -0.187 -0.303 166 ASP CCC OD2 
2999  N N   . ARG B 167 ? 1.346 1.436 1.341 0.034  -0.150 -0.275 167 ARG CCC N   
3000  C CA  . ARG B 167 ? 1.337 1.429 1.340 0.030  -0.144 -0.274 167 ARG CCC CA  
3001  C C   . ARG B 167 ? 1.340 1.433 1.334 0.036  -0.138 -0.287 167 ARG CCC C   
3002  O O   . ARG B 167 ? 1.314 1.409 1.326 0.039  -0.138 -0.295 167 ARG CCC O   
3003  C CB  . ARG B 167 ? 1.399 1.494 1.389 0.016  -0.137 -0.260 167 ARG CCC CB  
3004  C CG  . ARG B 167 ? 1.508 1.596 1.508 0.007  -0.148 -0.242 167 ARG CCC CG  
3005  C CD  . ARG B 167 ? 1.566 1.660 1.550 -0.013 -0.141 -0.225 167 ARG CCC CD  
3006  N NE  . ARG B 167 ? 1.594 1.695 1.544 -0.016 -0.131 -0.227 167 ARG CCC NE  
3007  C CZ  . ARG B 167 ? 1.640 1.760 1.578 -0.020 -0.116 -0.236 167 ARG CCC CZ  
3008  N NH1 . ARG B 167 ? 1.673 1.807 1.628 -0.022 -0.107 -0.245 167 ARG CCC NH1 
3009  N NH2 . ARG B 167 ? 1.683 1.808 1.593 -0.022 -0.110 -0.240 167 ARG CCC NH2 
3010  N N   . PHE B 168 ? 1.281 1.372 1.252 0.037  -0.138 -0.290 168 PHE CCC N   
3011  C CA  . PHE B 168 ? 1.325 1.412 1.289 0.041  -0.140 -0.300 168 PHE CCC CA  
3012  C C   . PHE B 168 ? 1.362 1.445 1.336 0.048  -0.148 -0.309 168 PHE CCC C   
3013  O O   . PHE B 168 ? 1.451 1.532 1.439 0.052  -0.150 -0.317 168 PHE CCC O   
3014  C CB  . PHE B 168 ? 1.269 1.352 1.208 0.039  -0.143 -0.298 168 PHE CCC CB  
3015  C CG  . PHE B 168 ? 1.327 1.400 1.259 0.042  -0.151 -0.307 168 PHE CCC CG  
3016  C CD1 . PHE B 168 ? 1.393 1.469 1.333 0.044  -0.148 -0.317 168 PHE CCC CD1 
3017  C CD2 . PHE B 168 ? 1.408 1.471 1.328 0.041  -0.163 -0.306 168 PHE CCC CD2 
3018  C CE1 . PHE B 168 ? 1.446 1.512 1.389 0.049  -0.162 -0.328 168 PHE CCC CE1 
3019  C CE2 . PHE B 168 ? 1.469 1.518 1.386 0.042  -0.177 -0.311 168 PHE CCC CE2 
3020  C CZ  . PHE B 168 ? 1.449 1.496 1.380 0.048  -0.178 -0.323 168 PHE CCC CZ  
3021  N N   . TYR B 169 ? 1.316 1.401 1.285 0.048  -0.152 -0.308 169 TYR CCC N   
3022  C CA  . TYR B 169 ? 1.337 1.422 1.309 0.052  -0.160 -0.317 169 TYR CCC CA  
3023  C C   . TYR B 169 ? 1.344 1.432 1.346 0.058  -0.161 -0.324 169 TYR CCC C   
3024  O O   . TYR B 169 ? 1.325 1.411 1.331 0.062  -0.168 -0.333 169 TYR CCC O   
3025  C CB  . TYR B 169 ? 1.350 1.447 1.306 0.048  -0.161 -0.318 169 TYR CCC CB  
3026  C CG  . TYR B 169 ? 1.297 1.389 1.223 0.039  -0.165 -0.310 169 TYR CCC CG  
3027  C CD1 . TYR B 169 ? 1.374 1.455 1.284 0.035  -0.176 -0.310 169 TYR CCC CD1 
3028  C CD2 . TYR B 169 ? 1.286 1.382 1.201 0.035  -0.161 -0.302 169 TYR CCC CD2 
3029  C CE1 . TYR B 169 ? 1.388 1.460 1.272 0.025  -0.184 -0.301 169 TYR CCC CE1 
3030  C CE2 . TYR B 169 ? 1.315 1.404 1.205 0.026  -0.166 -0.295 169 TYR CCC CE2 
3031  C CZ  . TYR B 169 ? 1.360 1.437 1.235 0.021  -0.179 -0.294 169 TYR CCC CZ  
3032  O OH  . TYR B 169 ? 1.460 1.527 1.314 0.010  -0.189 -0.284 169 TYR CCC OH  
3033  N N   . LYS B 170 ? 1.306 1.397 1.327 0.058  -0.158 -0.319 170 LYS CCC N   
3034  C CA  . LYS B 170 ? 1.321 1.411 1.374 0.061  -0.162 -0.322 170 LYS CCC CA  
3035  C C   . LYS B 170 ? 1.424 1.511 1.487 0.061  -0.159 -0.325 170 LYS CCC C   
3036  O O   . LYS B 170 ? 1.467 1.552 1.548 0.066  -0.166 -0.334 170 LYS CCC O   
3037  C CB  . LYS B 170 ? 1.312 1.402 1.384 0.057  -0.163 -0.312 170 LYS CCC CB  
3038  C CG  . LYS B 170 ? 1.331 1.418 1.440 0.060  -0.172 -0.315 170 LYS CCC CG  
3039  C CD  . LYS B 170 ? 1.381 1.463 1.514 0.056  -0.183 -0.305 170 LYS CCC CD  
3040  C CE  . LYS B 170 ? 1.395 1.472 1.567 0.061  -0.197 -0.311 170 LYS CCC CE  
3041  N NZ  . LYS B 170 ? 1.583 1.649 1.784 0.054  -0.213 -0.298 170 LYS CCC NZ  
3042  N N   . THR B 171 ? 1.394 1.484 1.447 0.055  -0.150 -0.320 171 THR CCC N   
3043  C CA  . THR B 171 ? 1.426 1.520 1.493 0.056  -0.147 -0.328 171 THR CCC CA  
3044  C C   . THR B 171 ? 1.480 1.563 1.543 0.064  -0.158 -0.340 171 THR CCC C   
3045  O O   . THR B 171 ? 1.620 1.701 1.706 0.069  -0.164 -0.350 171 THR CCC O   
3046  C CB  . THR B 171 ? 1.425 1.529 1.481 0.048  -0.135 -0.326 171 THR CCC CB  
3047  O OG1 . THR B 171 ? 1.398 1.511 1.453 0.037  -0.127 -0.310 171 THR CCC OG1 
3048  C CG2 . THR B 171 ? 1.580 1.696 1.658 0.050  -0.131 -0.340 171 THR CCC CG2 
3049  N N   . LEU B 172 ? 1.437 1.511 1.471 0.064  -0.164 -0.338 172 LEU CCC N   
3050  C CA  . LEU B 172 ? 1.517 1.577 1.542 0.067  -0.180 -0.345 172 LEU CCC CA  
3051  C C   . LEU B 172 ? 1.599 1.657 1.634 0.071  -0.189 -0.351 172 LEU CCC C   
3052  O O   . LEU B 172 ? 1.783 1.830 1.826 0.075  -0.202 -0.359 172 LEU CCC O   
3053  C CB  . LEU B 172 ? 1.581 1.634 1.570 0.061  -0.186 -0.337 172 LEU CCC CB  
3054  C CG  . LEU B 172 ? 1.747 1.789 1.724 0.059  -0.195 -0.336 172 LEU CCC CG  
3055  C CD1 . LEU B 172 ? 1.825 1.863 1.768 0.049  -0.200 -0.324 172 LEU CCC CD1 
3056  C CD2 . LEU B 172 ? 1.915 1.939 1.904 0.063  -0.215 -0.346 172 LEU CCC CD2 
3057  N N   . ARG B 173 ? 1.534 1.602 1.572 0.071  -0.184 -0.349 173 ARG CCC N   
3058  C CA  . ARG B 173 ? 1.452 1.521 1.501 0.076  -0.192 -0.358 173 ARG CCC CA  
3059  C C   . ARG B 173 ? 1.480 1.545 1.565 0.082  -0.196 -0.365 173 ARG CCC C   
3060  O O   . ARG B 173 ? 1.587 1.644 1.678 0.086  -0.209 -0.374 173 ARG CCC O   
3061  C CB  . ARG B 173 ? 1.348 1.431 1.402 0.077  -0.188 -0.360 173 ARG CCC CB  
3062  C CG  . ARG B 173 ? 1.275 1.364 1.337 0.083  -0.198 -0.375 173 ARG CCC CG  
3063  C CD  . ARG B 173 ? 1.267 1.372 1.345 0.087  -0.196 -0.382 173 ARG CCC CD  
3064  N NE  . ARG B 173 ? 1.306 1.424 1.387 0.093  -0.204 -0.403 173 ARG CCC NE  
3065  C CZ  . ARG B 173 ? 1.320 1.454 1.423 0.100  -0.207 -0.418 173 ARG CCC CZ  
3066  N NH1 . ARG B 173 ? 1.294 1.430 1.420 0.102  -0.206 -0.414 173 ARG CCC NH1 
3067  N NH2 . ARG B 173 ? 1.349 1.501 1.454 0.105  -0.214 -0.441 173 ARG CCC NH2 
3068  N N   . ALA B 174 ? 1.437 1.508 1.545 0.080  -0.186 -0.360 174 ALA CCC N   
3069  C CA  . ALA B 174 ? 1.519 1.592 1.665 0.082  -0.188 -0.366 174 ALA CCC CA  
3070  C C   . ALA B 174 ? 1.675 1.741 1.825 0.085  -0.194 -0.376 174 ALA CCC C   
3071  O O   . ALA B 174 ? 1.796 1.857 1.971 0.091  -0.205 -0.386 174 ALA CCC O   
3072  C CB  . ALA B 174 ? 1.393 1.478 1.559 0.073  -0.175 -0.355 174 ALA CCC CB  
3073  N N   . GLU B 175 ? 1.696 1.762 1.827 0.083  -0.190 -0.374 175 GLU CCC N   
3074  C CA  . GLU B 175 ? 1.799 1.857 1.937 0.087  -0.200 -0.386 175 GLU CCC CA  
3075  C C   . GLU B 175 ? 1.845 1.881 1.966 0.091  -0.224 -0.388 175 GLU CCC C   
3076  O O   . GLU B 175 ? 1.961 1.984 2.098 0.096  -0.241 -0.399 175 GLU CCC O   
3077  C CB  . GLU B 175 ? 1.881 1.944 2.004 0.084  -0.193 -0.385 175 GLU CCC CB  
3078  C CG  . GLU B 175 ? 1.840 1.929 1.976 0.078  -0.170 -0.383 175 GLU CCC CG  
3079  C CD  . GLU B 175 ? 1.979 2.087 2.154 0.080  -0.165 -0.402 175 GLU CCC CD  
3080  O OE1 . GLU B 175 ? 2.155 2.255 2.346 0.089  -0.180 -0.419 175 GLU CCC OE1 
3081  O OE2 . GLU B 175 ? 1.962 2.096 2.155 0.071  -0.148 -0.400 175 GLU CCC OE2 
3082  N N   . GLN B 176 ? 1.872 1.904 1.961 0.087  -0.225 -0.379 176 GLN CCC N   
3083  C CA  . GLN B 176 ? 2.109 2.127 2.173 0.085  -0.244 -0.379 176 GLN CCC CA  
3084  C C   . GLN B 176 ? 2.463 2.460 2.508 0.080  -0.265 -0.376 176 GLN CCC C   
3085  O O   . GLN B 176 ? 2.531 2.524 2.536 0.070  -0.268 -0.364 176 GLN CCC O   
3086  C CB  . GLN B 176 ? 2.076 2.089 2.165 0.091  -0.256 -0.390 176 GLN CCC CB  
3087  C CG  . GLN B 176 ? 1.890 1.919 2.003 0.096  -0.244 -0.394 176 GLN CCC CG  
3088  C CD  . GLN B 176 ? 1.862 1.887 2.013 0.103  -0.255 -0.405 176 GLN CCC CD  
3089  O OE1 . GLN B 176 ? 2.003 2.015 2.169 0.107  -0.269 -0.412 176 GLN CCC OE1 
3090  N NE2 . GLN B 176 ? 1.830 1.864 2.003 0.107  -0.250 -0.409 176 GLN CCC NE2 
3091  N N   . ALA B 177 ? 2.955 2.938 3.027 0.087  -0.280 -0.386 177 ALA CCC N   
3092  C CA  . ALA B 177 ? 3.110 3.069 3.170 0.084  -0.304 -0.383 177 ALA CCC CA  
3093  C C   . ALA B 177 ? 3.301 3.241 3.315 0.070  -0.326 -0.368 177 ALA CCC C   
3094  O O   . ALA B 177 ? 3.635 3.568 3.644 0.069  -0.339 -0.370 177 ALA CCC O   
3095  C CB  . ALA B 177 ? 3.023 2.989 3.074 0.081  -0.292 -0.379 177 ALA CCC CB  
3096  N N   . SER B 178 ? 2.848 2.783 2.826 0.058  -0.329 -0.353 178 SER CCC N   
3097  C CA  . SER B 178 ? 2.768 2.691 2.698 0.040  -0.348 -0.336 178 SER CCC CA  
3098  C C   . SER B 178 ? 2.756 2.694 2.651 0.026  -0.332 -0.321 178 SER CCC C   
3099  O O   . SER B 178 ? 2.795 2.748 2.704 0.033  -0.310 -0.324 178 SER CCC O   
3100  C CB  . SER B 178 ? 2.652 2.535 2.580 0.034  -0.390 -0.331 178 SER CCC CB  
3101  O OG  . SER B 178 ? 2.527 2.395 2.443 0.025  -0.403 -0.319 178 SER CCC OG  
3102  N N   . GLN B 179 ? 2.760 2.695 2.609 0.005  -0.346 -0.305 179 GLN CCC N   
3103  C CA  . GLN B 179 ? 2.838 2.788 2.653 -0.012 -0.334 -0.289 179 GLN CCC CA  
3104  C C   . GLN B 179 ? 2.875 2.797 2.691 -0.017 -0.354 -0.278 179 GLN CCC C   
3105  O O   . GLN B 179 ? 2.950 2.884 2.762 -0.019 -0.339 -0.273 179 GLN CCC O   
3106  C CB  . GLN B 179 ? 2.951 2.915 2.716 -0.037 -0.340 -0.277 179 GLN CCC CB  
3107  C CG  . GLN B 179 ? 2.973 2.980 2.735 -0.033 -0.311 -0.291 179 GLN CCC CG  
3108  C CD  . GLN B 179 ? 2.930 2.967 2.710 -0.024 -0.279 -0.298 179 GLN CCC CD  
3109  O OE1 . GLN B 179 ? 2.909 2.946 2.677 -0.033 -0.276 -0.286 179 GLN CCC OE1 
3110  N NE2 . GLN B 179 ? 2.926 2.983 2.735 -0.007 -0.260 -0.318 179 GLN CCC NE2 
3111  N N   . GLU B 180 ? 2.790 2.674 2.613 -0.018 -0.392 -0.274 180 GLU CCC N   
3112  C CA  . GLU B 180 ? 2.777 2.631 2.613 -0.018 -0.416 -0.269 180 GLU CCC CA  
3113  C C   . GLU B 180 ? 2.702 2.569 2.582 0.006  -0.393 -0.291 180 GLU CCC C   
3114  O O   . GLU B 180 ? 2.873 2.740 2.753 0.005  -0.391 -0.288 180 GLU CCC O   
3115  C CB  . GLU B 180 ? 2.748 2.558 2.595 -0.020 -0.464 -0.267 180 GLU CCC CB  
3116  C CG  . GLU B 180 ? 2.755 2.544 2.549 -0.053 -0.496 -0.236 180 GLU CCC CG  
3117  C CD  . GLU B 180 ? 2.829 2.567 2.634 -0.057 -0.552 -0.230 180 GLU CCC CD  
3118  O OE1 . GLU B 180 ? 2.770 2.494 2.629 -0.031 -0.563 -0.255 180 GLU CCC OE1 
3119  O OE2 . GLU B 180 ? 3.006 2.719 2.769 -0.087 -0.586 -0.200 180 GLU CCC OE2 
3120  N N   . VAL B 181 ? 2.741 2.621 2.658 0.026  -0.379 -0.313 181 VAL CCC N   
3121  C CA  . VAL B 181 ? 2.556 2.455 2.511 0.044  -0.354 -0.333 181 VAL CCC CA  
3122  C C   . VAL B 181 ? 2.491 2.419 2.426 0.040  -0.319 -0.326 181 VAL CCC C   
3123  O O   . VAL B 181 ? 2.414 2.350 2.357 0.045  -0.309 -0.330 181 VAL CCC O   
3124  C CB  . VAL B 181 ? 2.501 2.412 2.497 0.061  -0.345 -0.354 181 VAL CCC CB  
3125  C CG1 . VAL B 181 ? 2.378 2.318 2.405 0.073  -0.314 -0.371 181 VAL CCC CG1 
3126  C CG2 . VAL B 181 ? 2.274 2.155 2.300 0.068  -0.383 -0.366 181 VAL CCC CG2 
3127  N N   . LYS B 182 ? 2.284 2.232 2.196 0.033  -0.302 -0.317 182 LYS CCC N   
3128  C CA  . LYS B 182 ? 2.294 2.269 2.193 0.030  -0.273 -0.312 182 LYS CCC CA  
3129  C C   . LYS B 182 ? 2.385 2.355 2.256 0.016  -0.278 -0.296 182 LYS CCC C   
3130  O O   . LYS B 182 ? 2.397 2.383 2.268 0.018  -0.259 -0.295 182 LYS CCC O   
3131  C CB  . LYS B 182 ? 2.222 2.219 2.106 0.025  -0.260 -0.310 182 LYS CCC CB  
3132  C CG  . LYS B 182 ? 2.116 2.123 2.030 0.038  -0.250 -0.325 182 LYS CCC CG  
3133  C CD  . LYS B 182 ? 2.145 2.173 2.046 0.034  -0.241 -0.327 182 LYS CCC CD  
3134  C CE  . LYS B 182 ? 2.084 2.120 2.018 0.048  -0.234 -0.341 182 LYS CCC CE  
3135  N NZ  . LYS B 182 ? 1.960 2.018 1.885 0.046  -0.227 -0.348 182 LYS CCC NZ  
3136  N N   . ASN B 183 ? 2.479 2.425 2.329 0.002  -0.307 -0.283 183 ASN CCC N   
3137  C CA  . ASN B 183 ? 2.496 2.438 2.321 -0.013 -0.313 -0.267 183 ASN CCC CA  
3138  C C   . ASN B 183 ? 2.464 2.381 2.310 -0.005 -0.332 -0.272 183 ASN CCC C   
3139  O O   . ASN B 183 ? 2.435 2.354 2.274 -0.009 -0.328 -0.266 183 ASN CCC O   
3140  C CB  . ASN B 183 ? 2.596 2.530 2.380 -0.040 -0.334 -0.244 183 ASN CCC CB  
3141  C CG  . ASN B 183 ? 2.832 2.728 2.617 -0.046 -0.374 -0.239 183 ASN CCC CG  
3142  O OD1 . ASN B 183 ? 3.054 2.919 2.862 -0.038 -0.400 -0.243 183 ASN CCC OD1 
3143  N ND2 . ASN B 183 ? 2.940 2.837 2.699 -0.060 -0.384 -0.230 183 ASN CCC ND2 
3144  N N   . ALA B 184 ? 2.547 2.441 2.422 0.006  -0.355 -0.285 184 ALA CCC N   
3145  C CA  . ALA B 184 ? 2.424 2.302 2.330 0.020  -0.370 -0.301 184 ALA CCC CA  
3146  C C   . ALA B 184 ? 2.280 2.189 2.206 0.035  -0.335 -0.319 184 ALA CCC C   
3147  O O   . ALA B 184 ? 2.232 2.142 2.162 0.038  -0.334 -0.324 184 ALA CCC O   
3148  C CB  . ALA B 184 ? 2.398 2.251 2.338 0.031  -0.400 -0.317 184 ALA CCC CB  
3149  N N   . ALA B 185 ? 2.146 2.080 2.083 0.043  -0.308 -0.329 185 ALA CCC N   
3150  C CA  . ALA B 185 ? 2.105 2.068 2.058 0.054  -0.277 -0.342 185 ALA CCC CA  
3151  C C   . ALA B 185 ? 2.034 2.010 1.960 0.046  -0.258 -0.328 185 ALA CCC C   
3152  O O   . ALA B 185 ? 2.033 2.022 1.966 0.051  -0.245 -0.337 185 ALA CCC O   
3153  C CB  . ALA B 185 ? 2.011 1.993 1.980 0.060  -0.256 -0.349 185 ALA CCC CB  
3154  N N   . THR B 186 ? 2.044 2.021 1.942 0.032  -0.256 -0.309 186 THR CCC N   
3155  C CA  . THR B 186 ? 2.066 2.058 1.944 0.025  -0.240 -0.297 186 THR CCC CA  
3156  C C   . THR B 186 ? 2.176 2.152 2.046 0.021  -0.256 -0.293 186 THR CCC C   
3157  O O   . THR B 186 ? 2.022 2.007 1.893 0.025  -0.244 -0.297 186 THR CCC O   
3158  C CB  . THR B 186 ? 2.091 2.095 1.946 0.013  -0.234 -0.283 186 THR CCC CB  
3159  O OG1 . THR B 186 ? 2.237 2.258 2.081 0.008  -0.219 -0.276 186 THR CCC OG1 
3160  C CG2 . THR B 186 ? 2.202 2.190 2.035 -0.003 -0.258 -0.270 186 THR CCC CG2 
3161  N N   . GLU B 187 ? 2.385 2.335 2.247 0.012  -0.286 -0.285 187 GLU CCC N   
3162  C CA  . GLU B 187 ? 2.380 2.309 2.240 0.008  -0.309 -0.281 187 GLU CCC CA  
3163  C C   . GLU B 187 ? 2.293 2.221 2.181 0.026  -0.310 -0.306 187 GLU CCC C   
3164  O O   . GLU B 187 ? 2.321 2.234 2.213 0.026  -0.328 -0.309 187 GLU CCC O   
3165  C CB  . GLU B 187 ? 2.450 2.346 2.305 -0.003 -0.347 -0.270 187 GLU CCC CB  
3166  C CG  . GLU B 187 ? 2.535 2.403 2.384 -0.015 -0.379 -0.257 187 GLU CCC CG  
3167  C CD  . GLU B 187 ? 2.622 2.463 2.449 -0.038 -0.413 -0.232 187 GLU CCC CD  
3168  O OE1 . GLU B 187 ? 2.628 2.477 2.440 -0.046 -0.407 -0.226 187 GLU CCC OE1 
3169  O OE2 . GLU B 187 ? 2.664 2.475 2.488 -0.051 -0.448 -0.219 187 GLU CCC OE2 
3170  N N   . THR B 188 ? 2.202 2.150 2.112 0.040  -0.290 -0.326 188 THR CCC N   
3171  C CA  . THR B 188 ? 2.140 2.097 2.079 0.056  -0.289 -0.355 188 THR CCC CA  
3172  C C   . THR B 188 ? 2.116 2.107 2.051 0.059  -0.253 -0.361 188 THR CCC C   
3173  O O   . THR B 188 ? 2.203 2.201 2.125 0.057  -0.245 -0.360 188 THR CCC O   
3174  C CB  . THR B 188 ? 2.131 2.081 2.105 0.068  -0.303 -0.377 188 THR CCC CB  
3175  O OG1 . THR B 188 ? 2.288 2.249 2.262 0.066  -0.288 -0.370 188 THR CCC OG1 
3176  C CG2 . THR B 188 ? 2.143 2.054 2.127 0.066  -0.348 -0.374 188 THR CCC CG2 
3177  N N   . LEU B 189 ? 2.007 2.017 1.953 0.062  -0.233 -0.365 189 LEU CCC N   
3178  C CA  . LEU B 189 ? 1.954 1.996 1.902 0.062  -0.203 -0.371 189 LEU CCC CA  
3179  C C   . LEU B 189 ? 1.940 1.988 1.858 0.052  -0.187 -0.349 189 LEU CCC C   
3180  O O   . LEU B 189 ? 1.981 2.048 1.892 0.050  -0.171 -0.351 189 LEU CCC O   
3181  C CB  . LEU B 189 ? 1.880 1.936 1.850 0.066  -0.192 -0.379 189 LEU CCC CB  
3182  C CG  . LEU B 189 ? 1.912 1.964 1.918 0.077  -0.208 -0.404 189 LEU CCC CG  
3183  C CD1 . LEU B 189 ? 1.871 1.933 1.898 0.079  -0.200 -0.407 189 LEU CCC CD1 
3184  C CD2 . LEU B 189 ? 1.894 1.969 1.921 0.085  -0.203 -0.434 189 LEU CCC CD2 
3185  N N   . LEU B 190 ? 1.876 1.912 1.779 0.045  -0.192 -0.329 190 LEU CCC N   
3186  C CA  . LEU B 190 ? 1.816 1.860 1.700 0.038  -0.179 -0.312 190 LEU CCC CA  
3187  C C   . LEU B 190 ? 1.820 1.863 1.688 0.035  -0.181 -0.310 190 LEU CCC C   
3188  O O   . LEU B 190 ? 1.857 1.913 1.717 0.031  -0.168 -0.304 190 LEU CCC O   
3189  C CB  . LEU B 190 ? 1.766 1.805 1.639 0.031  -0.185 -0.297 190 LEU CCC CB  
3190  C CG  . LEU B 190 ? 1.623 1.674 1.487 0.025  -0.173 -0.285 190 LEU CCC CG  
3191  C CD1 . LEU B 190 ? 1.619 1.683 1.499 0.029  -0.160 -0.287 190 LEU CCC CD1 
3192  C CD2 . LEU B 190 ? 1.517 1.569 1.370 0.017  -0.180 -0.276 190 LEU CCC CD2 
3193  N N   . VAL B 191 ? 1.833 1.860 1.699 0.036  -0.200 -0.314 191 VAL CCC N   
3194  C CA  . VAL B 191 ? 1.886 1.911 1.740 0.034  -0.203 -0.314 191 VAL CCC CA  
3195  C C   . VAL B 191 ? 1.967 2.009 1.827 0.041  -0.194 -0.335 191 VAL CCC C   
3196  O O   . VAL B 191 ? 1.958 2.012 1.803 0.037  -0.183 -0.333 191 VAL CCC O   
3197  C CB  . VAL B 191 ? 1.925 1.925 1.775 0.031  -0.230 -0.310 191 VAL CCC CB  
3198  C CG1 . VAL B 191 ? 1.937 1.936 1.778 0.030  -0.235 -0.312 191 VAL CCC CG1 
3199  C CG2 . VAL B 191 ? 1.850 1.844 1.688 0.019  -0.235 -0.288 191 VAL CCC CG2 
3200  N N   . GLN B 192 ? 2.041 2.086 1.925 0.050  -0.199 -0.359 192 GLN CCC N   
3201  C CA  . GLN B 192 ? 2.100 2.170 1.993 0.056  -0.188 -0.385 192 GLN CCC CA  
3202  C C   . GLN B 192 ? 1.982 2.082 1.865 0.048  -0.160 -0.380 192 GLN CCC C   
3203  O O   . GLN B 192 ? 2.032 2.155 1.903 0.045  -0.148 -0.390 192 GLN CCC O   
3204  C CB  . GLN B 192 ? 2.279 2.351 2.207 0.069  -0.201 -0.415 192 GLN CCC CB  
3205  C CG  . GLN B 192 ? 2.574 2.617 2.518 0.077  -0.236 -0.426 192 GLN CCC CG  
3206  C CD  . GLN B 192 ? 2.820 2.826 2.755 0.070  -0.258 -0.399 192 GLN CCC CD  
3207  O OE1 . GLN B 192 ? 2.938 2.930 2.848 0.060  -0.262 -0.375 192 GLN CCC OE1 
3208  N NE2 . GLN B 192 ? 2.947 2.940 2.904 0.074  -0.273 -0.404 192 GLN CCC NE2 
3209  N N   . ASN B 193 ? 1.863 1.964 1.750 0.044  -0.151 -0.364 193 ASN CCC N   
3210  C CA  . ASN B 193 ? 1.869 1.992 1.749 0.034  -0.129 -0.355 193 ASN CCC CA  
3211  C C   . ASN B 193 ? 1.871 1.988 1.726 0.024  -0.126 -0.328 193 ASN CCC C   
3212  O O   . ASN B 193 ? 1.848 1.977 1.697 0.014  -0.114 -0.316 193 ASN CCC O   
3213  C CB  . ASN B 193 ? 1.885 2.011 1.789 0.036  -0.124 -0.355 193 ASN CCC CB  
3214  C CG  . ASN B 193 ? 1.981 2.123 1.915 0.045  -0.124 -0.384 193 ASN CCC CG  
3215  O OD1 . ASN B 193 ? 2.000 2.150 1.942 0.052  -0.130 -0.408 193 ASN CCC OD1 
3216  N ND2 . ASN B 193 ? 2.085 2.235 2.042 0.045  -0.118 -0.386 193 ASN CCC ND2 
3217  N N   . ALA B 194 ? 1.893 1.989 1.736 0.025  -0.139 -0.319 194 ALA CCC N   
3218  C CA  . ALA B 194 ? 1.840 1.930 1.664 0.017  -0.139 -0.298 194 ALA CCC CA  
3219  C C   . ALA B 194 ? 1.871 1.974 1.673 0.010  -0.133 -0.299 194 ALA CCC C   
3220  O O   . ALA B 194 ? 1.978 2.096 1.778 0.011  -0.129 -0.319 194 ALA CCC O   
3221  C CB  . ALA B 194 ? 1.842 1.912 1.662 0.020  -0.155 -0.291 194 ALA CCC CB  
3222  N N   . ASN B 195 ? 1.950 2.048 1.737 0.001  -0.134 -0.279 195 ASN CCC N   
3223  C CA  . ASN B 195 ? 1.997 2.105 1.758 -0.010 -0.131 -0.275 195 ASN CCC CA  
3224  C C   . ASN B 195 ? 1.989 2.088 1.737 -0.005 -0.142 -0.285 195 ASN CCC C   
3225  O O   . ASN B 195 ? 1.938 2.021 1.698 0.004  -0.153 -0.287 195 ASN CCC O   
3226  C CB  . ASN B 195 ? 2.017 2.114 1.772 -0.020 -0.137 -0.249 195 ASN CCC CB  
3227  C CG  . ASN B 195 ? 2.191 2.299 1.918 -0.038 -0.134 -0.237 195 ASN CCC CG  
3228  O OD1 . ASN B 195 ? 2.349 2.480 2.064 -0.046 -0.120 -0.246 195 ASN CCC OD1 
3229  N ND2 . ASN B 195 ? 2.283 2.375 1.999 -0.045 -0.148 -0.217 195 ASN CCC ND2 
3230  N N   . PRO B 196 ? 1.980 2.091 1.703 -0.012 -0.140 -0.291 196 PRO CCC N   
3231  C CA  A PRO B 196 ? 1.920 2.023 1.637 -0.004 -0.153 -0.306 196 PRO CCC CA  
3232  C C   . PRO B 196 ? 1.969 2.048 1.679 -0.005 -0.168 -0.286 196 PRO CCC C   
3233  O O   . PRO B 196 ? 2.021 2.085 1.738 0.002  -0.182 -0.292 196 PRO CCC O   
3234  C CB  A PRO B 196 ? 1.919 2.048 1.609 -0.012 -0.144 -0.321 196 PRO CCC CB  
3235  C CG  A PRO B 196 ? 1.967 2.122 1.653 -0.024 -0.125 -0.317 196 PRO CCC CG  
3236  C CD  A PRO B 196 ? 1.989 2.125 1.689 -0.027 -0.127 -0.290 196 PRO CCC CD  
3237  N N   . ASP B 197 ? 1.982 2.057 1.685 -0.015 -0.168 -0.263 197 ASP CCC N   
3238  C CA  . ASP B 197 ? 1.991 2.047 1.697 -0.015 -0.183 -0.248 197 ASP CCC CA  
3239  C C   . ASP B 197 ? 1.937 1.984 1.670 -0.008 -0.186 -0.246 197 ASP CCC C   
3240  O O   . ASP B 197 ? 1.834 1.872 1.573 -0.006 -0.198 -0.245 197 ASP CCC O   
3241  C CB  . ASP B 197 ? 1.980 2.032 1.678 -0.026 -0.186 -0.226 197 ASP CCC CB  
3242  C CG  . ASP B 197 ? 2.046 2.103 1.708 -0.039 -0.188 -0.222 197 ASP CCC CG  
3243  O OD1 . ASP B 197 ? 2.102 2.167 1.746 -0.037 -0.186 -0.239 197 ASP CCC OD1 
3244  O OD2 . ASP B 197 ? 2.032 2.084 1.684 -0.052 -0.194 -0.202 197 ASP CCC OD2 
3245  N N   . CYS B 198 ? 1.878 1.931 1.628 -0.005 -0.177 -0.247 198 CYS CCC N   
3246  C CA  . CYS B 198 ? 1.722 1.772 1.494 0.000  -0.179 -0.247 198 CYS CCC CA  
3247  C C   . CYS B 198 ? 1.734 1.778 1.507 0.005  -0.185 -0.260 198 CYS CCC C   
3248  O O   . CYS B 198 ? 1.725 1.762 1.505 0.004  -0.194 -0.257 198 CYS CCC O   
3249  C CB  . CYS B 198 ? 1.651 1.709 1.439 0.001  -0.169 -0.245 198 CYS CCC CB  
3250  S SG  . CYS B 198 ? 1.604 1.663 1.409 -0.002 -0.172 -0.231 198 CYS CCC SG  
3251  N N   . LYS B 199 ? 1.794 1.843 1.563 0.010  -0.181 -0.277 199 LYS CCC N   
3252  C CA  . LYS B 199 ? 1.857 1.898 1.635 0.017  -0.192 -0.293 199 LYS CCC CA  
3253  C C   . LYS B 199 ? 1.926 1.951 1.699 0.016  -0.211 -0.291 199 LYS CCC C   
3254  O O   . LYS B 199 ? 1.921 1.931 1.704 0.016  -0.227 -0.290 199 LYS CCC O   
3255  C CB  . LYS B 199 ? 1.885 1.942 1.665 0.022  -0.184 -0.317 199 LYS CCC CB  
3256  C CG  . LYS B 199 ? 2.045 2.096 1.844 0.033  -0.197 -0.340 199 LYS CCC CG  
3257  C CD  . LYS B 199 ? 2.053 2.130 1.856 0.038  -0.186 -0.368 199 LYS CCC CD  
3258  C CE  . LYS B 199 ? 1.851 1.951 1.659 0.034  -0.164 -0.367 199 LYS CCC CE  
3259  N NZ  . LYS B 199 ? 1.823 1.954 1.644 0.038  -0.153 -0.398 199 LYS CCC NZ  
3260  N N   . THR B 200 ? 1.964 1.991 1.721 0.013  -0.212 -0.289 200 THR CCC N   
3261  C CA  . THR B 200 ? 1.905 1.916 1.658 0.011  -0.231 -0.287 200 THR CCC CA  
3262  C C   . THR B 200 ? 1.937 1.940 1.699 0.003  -0.238 -0.266 200 THR CCC C   
3263  O O   . THR B 200 ? 1.915 1.904 1.684 -0.000 -0.256 -0.263 200 THR CCC O   
3264  C CB  . THR B 200 ? 1.859 1.874 1.591 0.008  -0.231 -0.286 200 THR CCC CB  
3265  O OG1 . THR B 200 ? 1.764 1.786 1.491 0.001  -0.221 -0.267 200 THR CCC OG1 
3266  C CG2 . THR B 200 ? 1.965 1.995 1.685 0.013  -0.223 -0.309 200 THR CCC CG2 
3267  N N   . ILE B 201 ? 1.928 1.943 1.692 -0.001 -0.225 -0.253 201 ILE CCC N   
3268  C CA  . ILE B 201 ? 1.802 1.821 1.578 -0.009 -0.227 -0.239 201 ILE CCC CA  
3269  C C   . ILE B 201 ? 1.764 1.780 1.548 -0.012 -0.229 -0.239 201 ILE CCC C   
3270  O O   . ILE B 201 ? 1.834 1.847 1.620 -0.022 -0.240 -0.230 201 ILE CCC O   
3271  C CB  . ILE B 201 ? 1.685 1.718 1.468 -0.010 -0.214 -0.232 201 ILE CCC CB  
3272  C CG1 . ILE B 201 ? 1.914 1.945 1.690 -0.011 -0.219 -0.228 201 ILE CCC CG1 
3273  C CG2 . ILE B 201 ? 1.555 1.603 1.355 -0.017 -0.212 -0.226 201 ILE CCC CG2 
3274  C CD1 . ILE B 201 ? 2.013 2.052 1.799 -0.010 -0.212 -0.222 201 ILE CCC CD1 
3275  N N   . LEU B 202 ? 1.769 1.787 1.555 -0.005 -0.221 -0.247 202 LEU CCC N   
3276  C CA  . LEU B 202 ? 1.780 1.794 1.572 -0.008 -0.226 -0.246 202 LEU CCC CA  
3277  C C   . LEU B 202 ? 1.951 1.942 1.743 -0.010 -0.250 -0.249 202 LEU CCC C   
3278  O O   . LEU B 202 ? 2.038 2.021 1.830 -0.021 -0.263 -0.237 202 LEU CCC O   
3279  C CB  . LEU B 202 ? 1.765 1.784 1.564 0.001  -0.214 -0.257 202 LEU CCC CB  
3280  C CG  . LEU B 202 ? 1.693 1.731 1.498 0.002  -0.196 -0.253 202 LEU CCC CG  
3281  C CD1 . LEU B 202 ? 1.726 1.767 1.539 0.010  -0.186 -0.264 202 LEU CCC CD1 
3282  C CD2 . LEU B 202 ? 1.716 1.765 1.525 -0.006 -0.194 -0.244 202 LEU CCC CD2 
3283  N N   . LYS B 203 ? 2.038 2.020 1.832 0.000  -0.258 -0.264 203 LYS CCC N   
3284  C CA  . LYS B 203 ? 2.078 2.037 1.878 0.001  -0.285 -0.270 203 LYS CCC CA  
3285  C C   . LYS B 203 ? 2.096 2.044 1.891 -0.014 -0.302 -0.252 203 LYS CCC C   
3286  O O   . LYS B 203 ? 2.146 2.074 1.946 -0.023 -0.327 -0.243 203 LYS CCC O   
3287  C CB  . LYS B 203 ? 2.203 2.161 2.007 0.015  -0.288 -0.296 203 LYS CCC CB  
3288  C CG  . LYS B 203 ? 2.247 2.216 2.064 0.027  -0.278 -0.318 203 LYS CCC CG  
3289  C CD  . LYS B 203 ? 2.461 2.444 2.280 0.039  -0.274 -0.348 203 LYS CCC CD  
3290  C CE  . LYS B 203 ? 2.648 2.645 2.489 0.051  -0.268 -0.373 203 LYS CCC CE  
3291  N NZ  . LYS B 203 ? 2.793 2.765 2.659 0.055  -0.295 -0.377 203 LYS CCC NZ  
3292  N N   . ALA B 204 ? 2.025 1.986 1.812 -0.017 -0.290 -0.244 204 ALA CCC N   
3293  C CA  . ALA B 204 ? 1.992 1.949 1.778 -0.031 -0.304 -0.228 204 ALA CCC CA  
3294  C C   . ALA B 204 ? 2.031 1.999 1.816 -0.050 -0.302 -0.208 204 ALA CCC C   
3295  O O   . ALA B 204 ? 2.103 2.066 1.889 -0.067 -0.317 -0.193 204 ALA CCC O   
3296  C CB  . ALA B 204 ? 1.921 1.890 1.702 -0.029 -0.293 -0.227 204 ALA CCC CB  
3297  N N   . LEU B 205 ? 1.996 1.982 1.781 -0.050 -0.283 -0.208 205 LEU CCC N   
3298  C CA  . LEU B 205 ? 1.981 1.984 1.762 -0.069 -0.279 -0.193 205 LEU CCC CA  
3299  C C   . LEU B 205 ? 2.109 2.089 1.884 -0.084 -0.305 -0.180 205 LEU CCC C   
3300  O O   . LEU B 205 ? 2.167 2.159 1.934 -0.108 -0.310 -0.162 205 LEU CCC O   
3301  C CB  . LEU B 205 ? 1.902 1.928 1.686 -0.063 -0.256 -0.199 205 LEU CCC CB  
3302  C CG  . LEU B 205 ? 1.840 1.890 1.633 -0.054 -0.235 -0.206 205 LEU CCC CG  
3303  C CD1 . LEU B 205 ? 1.808 1.877 1.607 -0.048 -0.217 -0.214 205 LEU CCC CD1 
3304  C CD2 . LEU B 205 ? 1.801 1.872 1.599 -0.069 -0.234 -0.198 205 LEU CCC CD2 
3305  N N   . GLY B 206 ? 2.255 2.205 2.035 -0.072 -0.324 -0.190 206 GLY CCC N   
3306  C CA  . GLY B 206 ? 2.296 2.217 2.075 -0.085 -0.357 -0.178 206 GLY CCC CA  
3307  C C   . GLY B 206 ? 2.365 2.285 2.138 -0.089 -0.356 -0.176 206 GLY CCC C   
3308  O O   . GLY B 206 ? 2.449 2.393 2.222 -0.079 -0.329 -0.185 206 GLY CCC O   
3309  N N   . PRO B 207 ? 2.305 2.196 2.076 -0.102 -0.390 -0.163 207 PRO CCC N   
3310  C CA  . PRO B 207 ? 2.255 2.140 2.020 -0.107 -0.395 -0.159 207 PRO CCC CA  
3311  C C   . PRO B 207 ? 2.245 2.163 1.984 -0.132 -0.377 -0.139 207 PRO CCC C   
3312  O O   . PRO B 207 ? 2.283 2.221 2.010 -0.154 -0.371 -0.123 207 PRO CCC O   
3313  C CB  . PRO B 207 ? 2.339 2.177 2.110 -0.117 -0.445 -0.148 207 PRO CCC CB  
3314  C CG  . PRO B 207 ? 2.310 2.140 2.079 -0.134 -0.462 -0.131 207 PRO CCC CG  
3315  C CD  . PRO B 207 ? 2.324 2.182 2.100 -0.117 -0.429 -0.148 207 PRO CCC CD  
3316  N N   . GLY B 208 ? 2.190 2.117 1.923 -0.129 -0.367 -0.144 208 GLY CCC N   
3317  C CA  . GLY B 208 ? 2.220 2.180 1.928 -0.153 -0.350 -0.131 208 GLY CCC CA  
3318  C C   . GLY B 208 ? 2.073 2.083 1.785 -0.146 -0.309 -0.144 208 GLY CCC C   
3319  O O   . GLY B 208 ? 2.102 2.149 1.798 -0.166 -0.294 -0.136 208 GLY CCC O   
3320  N N   . ALA B 209 ? 1.992 2.004 1.726 -0.118 -0.293 -0.163 209 ALA CCC N   
3321  C CA  . ALA B 209 ? 1.957 2.009 1.700 -0.110 -0.260 -0.176 209 ALA CCC CA  
3322  C C   . ALA B 209 ? 1.893 1.965 1.636 -0.104 -0.243 -0.187 209 ALA CCC C   
3323  O O   . ALA B 209 ? 1.939 1.990 1.685 -0.091 -0.250 -0.194 209 ALA CCC O   
3324  C CB  . ALA B 209 ? 2.006 2.049 1.768 -0.085 -0.252 -0.191 209 ALA CCC CB  
3325  N N   . THR B 210 ? 1.805 1.920 1.546 -0.113 -0.223 -0.192 210 THR CCC N   
3326  C CA  . THR B 210 ? 1.739 1.877 1.483 -0.106 -0.208 -0.206 210 THR CCC CA  
3327  C C   . THR B 210 ? 1.698 1.834 1.470 -0.077 -0.194 -0.224 210 THR CCC C   
3328  O O   . THR B 210 ? 1.760 1.889 1.546 -0.066 -0.191 -0.226 210 THR CCC O   
3329  C CB  . THR B 210 ? 1.745 1.937 1.485 -0.123 -0.191 -0.211 210 THR CCC CB  
3330  O OG1 . THR B 210 ? 1.859 2.059 1.575 -0.155 -0.201 -0.190 210 THR CCC OG1 
3331  C CG2 . THR B 210 ? 1.833 2.046 1.566 -0.124 -0.183 -0.222 210 THR CCC CG2 
3332  N N   . LEU B 211 ? 1.681 1.821 1.460 -0.066 -0.187 -0.237 211 LEU CCC N   
3333  C CA  . LEU B 211 ? 1.549 1.689 1.355 -0.043 -0.176 -0.252 211 LEU CCC CA  
3334  C C   . LEU B 211 ? 1.614 1.785 1.438 -0.041 -0.162 -0.260 211 LEU CCC C   
3335  O O   . LEU B 211 ? 1.652 1.814 1.493 -0.028 -0.160 -0.263 211 LEU CCC O   
3336  C CB  . LEU B 211 ? 1.602 1.743 1.414 -0.034 -0.173 -0.263 211 LEU CCC CB  
3337  C CG  . LEU B 211 ? 1.495 1.633 1.334 -0.013 -0.164 -0.276 211 LEU CCC CG  
3338  C CD1 . LEU B 211 ? 1.534 1.697 1.397 -0.007 -0.154 -0.287 211 LEU CCC CD1 
3339  C CD2 . LEU B 211 ? 1.431 1.538 1.274 -0.003 -0.169 -0.271 211 LEU CCC CD2 
3340  N N   . GLU B 212 ? 1.759 1.968 1.580 -0.055 -0.155 -0.266 212 GLU CCC N   
3341  C CA  . GLU B 212 ? 1.812 2.057 1.657 -0.053 -0.145 -0.278 212 GLU CCC CA  
3342  C C   . GLU B 212 ? 1.831 2.064 1.680 -0.055 -0.150 -0.267 212 GLU CCC C   
3343  O O   . GLU B 212 ? 1.847 2.082 1.721 -0.042 -0.148 -0.275 212 GLU CCC O   
3344  C CB  . GLU B 212 ? 1.905 2.199 1.741 -0.074 -0.136 -0.286 212 GLU CCC CB  
3345  C CG  . GLU B 212 ? 2.068 2.383 1.902 -0.072 -0.130 -0.302 212 GLU CCC CG  
3346  C CD  . GLU B 212 ? 2.240 2.614 2.065 -0.094 -0.118 -0.314 212 GLU CCC CD  
3347  O OE1 . GLU B 212 ? 2.129 2.537 1.962 -0.106 -0.111 -0.316 212 GLU CCC OE1 
3348  O OE2 . GLU B 212 ? 2.454 2.844 2.261 -0.101 -0.116 -0.320 212 GLU CCC OE2 
3349  N N   . GLU B 213 ? 1.747 1.963 1.570 -0.071 -0.160 -0.248 213 GLU CCC N   
3350  C CA  . GLU B 213 ? 1.599 1.803 1.425 -0.073 -0.167 -0.239 213 GLU CCC CA  
3351  C C   . GLU B 213 ? 1.530 1.697 1.362 -0.053 -0.172 -0.238 213 GLU CCC C   
3352  O O   . GLU B 213 ? 1.620 1.788 1.466 -0.047 -0.173 -0.240 213 GLU CCC O   
3353  C CB  . GLU B 213 ? 1.628 1.817 1.428 -0.094 -0.181 -0.218 213 GLU CCC CB  
3354  C CG  . GLU B 213 ? 1.754 1.983 1.544 -0.122 -0.177 -0.212 213 GLU CCC CG  
3355  C CD  . GLU B 213 ? 1.884 2.088 1.644 -0.146 -0.198 -0.187 213 GLU CCC CD  
3356  O OE1 . GLU B 213 ? 1.936 2.104 1.681 -0.143 -0.212 -0.180 213 GLU CCC OE1 
3357  O OE2 . GLU B 213 ? 1.948 2.170 1.705 -0.168 -0.201 -0.175 213 GLU CCC OE2 
3358  N N   . MET B 214 ? 1.488 1.627 1.312 -0.044 -0.177 -0.237 214 MET CCC N   
3359  C CA  . MET B 214 ? 1.498 1.613 1.326 -0.028 -0.179 -0.239 214 MET CCC CA  
3360  C C   . MET B 214 ? 1.470 1.596 1.320 -0.017 -0.169 -0.248 214 MET CCC C   
3361  O O   . MET B 214 ? 1.663 1.778 1.516 -0.011 -0.172 -0.246 214 MET CCC O   
3362  C CB  A MET B 214 ? 1.545 1.634 1.364 -0.022 -0.184 -0.240 214 MET CCC CB  
3363  C CG  A MET B 214 ? 1.723 1.816 1.540 -0.024 -0.183 -0.243 214 MET CCC CG  
3364  S SD  A MET B 214 ? 1.843 1.904 1.657 -0.015 -0.195 -0.247 214 MET CCC SD  
3365  C CE  A MET B 214 ? 1.663 1.701 1.463 -0.025 -0.216 -0.237 214 MET CCC CE  
3366  N N   . MET B 215 ? 1.310 1.456 1.176 -0.013 -0.162 -0.259 215 MET CCC N   
3367  C CA  . MET B 215 ? 1.282 1.434 1.174 -0.002 -0.160 -0.267 215 MET CCC CA  
3368  C C   . MET B 215 ? 1.310 1.478 1.220 -0.003 -0.163 -0.270 215 MET CCC C   
3369  O O   . MET B 215 ? 1.405 1.562 1.330 0.004  -0.169 -0.268 215 MET CCC O   
3370  C CB  . MET B 215 ? 1.425 1.596 1.335 0.003  -0.154 -0.281 215 MET CCC CB  
3371  C CG  . MET B 215 ? 1.463 1.616 1.363 0.008  -0.153 -0.280 215 MET CCC CG  
3372  S SD  . MET B 215 ? 1.351 1.525 1.276 0.016  -0.149 -0.299 215 MET CCC SD  
3373  C CE  . MET B 215 ? 1.624 1.792 1.585 0.028  -0.156 -0.302 215 MET CCC CE  
3374  N N   . THR B 216 ? 1.367 1.562 1.278 -0.014 -0.160 -0.273 216 THR CCC N   
3375  C CA  . THR B 216 ? 1.402 1.614 1.333 -0.016 -0.163 -0.277 216 THR CCC CA  
3376  C C   . THR B 216 ? 1.395 1.577 1.311 -0.017 -0.174 -0.261 216 THR CCC C   
3377  O O   . THR B 216 ? 1.434 1.611 1.368 -0.011 -0.182 -0.262 216 THR CCC O   
3378  C CB  . THR B 216 ? 1.404 1.657 1.337 -0.032 -0.156 -0.283 216 THR CCC CB  
3379  O OG1 . THR B 216 ? 1.493 1.779 1.437 -0.032 -0.146 -0.301 216 THR CCC OG1 
3380  C CG2 . THR B 216 ? 1.419 1.696 1.380 -0.034 -0.159 -0.291 216 THR CCC CG2 
3381  N N   . ALA B 217 ? 1.397 1.559 1.282 -0.025 -0.176 -0.248 217 ALA CCC N   
3382  C CA  . ALA B 217 ? 1.386 1.522 1.255 -0.026 -0.187 -0.237 217 ALA CCC CA  
3383  C C   . ALA B 217 ? 1.402 1.514 1.268 -0.015 -0.190 -0.235 217 ALA CCC C   
3384  O O   . ALA B 217 ? 1.531 1.632 1.394 -0.014 -0.199 -0.230 217 ALA CCC O   
3385  C CB  . ALA B 217 ? 1.339 1.455 1.181 -0.033 -0.192 -0.228 217 ALA CCC CB  
3386  N N   . CYS B 218 ? 1.296 1.403 1.162 -0.008 -0.184 -0.238 218 CYS CCC N   
3387  C CA  . CYS B 218 ? 1.320 1.409 1.179 -0.002 -0.186 -0.234 218 CYS CCC CA  
3388  C C   . CYS B 218 ? 1.383 1.476 1.268 0.002  -0.191 -0.235 218 CYS CCC C   
3389  O O   . CYS B 218 ? 1.537 1.616 1.416 0.003  -0.193 -0.229 218 CYS CCC O   
3390  C CB  . CYS B 218 ? 1.389 1.471 1.238 0.001  -0.178 -0.237 218 CYS CCC CB  
3391  S SG  . CYS B 218 ? 1.506 1.573 1.329 -0.002 -0.181 -0.237 218 CYS CCC SG  
3392  N N   . GLN B 219 ? 1.312 1.424 1.226 0.004  -0.194 -0.244 219 GLN CCC N   
3393  C CA  . GLN B 219 ? 1.461 1.575 1.407 0.010  -0.205 -0.247 219 GLN CCC CA  
3394  C C   . GLN B 219 ? 1.742 1.836 1.685 0.007  -0.222 -0.235 219 GLN CCC C   
3395  O O   . GLN B 219 ? 1.799 1.887 1.769 0.011  -0.238 -0.235 219 GLN CCC O   
3396  C CB  . GLN B 219 ? 1.450 1.596 1.434 0.013  -0.205 -0.266 219 GLN CCC CB  
3397  C CG  . GLN B 219 ? 1.643 1.818 1.638 0.015  -0.191 -0.282 219 GLN CCC CG  
3398  C CD  . GLN B 219 ? 1.608 1.824 1.636 0.014  -0.189 -0.303 219 GLN CCC CD  
3399  O OE1 . GLN B 219 ? 1.441 1.663 1.481 0.012  -0.196 -0.303 219 GLN CCC OE1 
3400  N NE2 . GLN B 219 ? 1.646 1.894 1.688 0.016  -0.178 -0.322 219 GLN CCC NE2 
3416  N N   . PRO C 1   ? 1.170 1.208 1.117 0.013  0.152  0.108  1   PRO AAA N   
3417  C CA  . PRO C 1   ? 1.079 1.107 1.017 0.014  0.152  0.108  1   PRO AAA CA  
3418  C C   . PRO C 1   ? 1.149 1.163 1.082 0.014  0.154  0.112  1   PRO AAA C   
3419  O O   . PRO C 1   ? 1.272 1.284 1.210 0.012  0.155  0.115  1   PRO AAA O   
3420  C CB  A PRO C 1   ? 1.233 1.264 1.175 0.015  0.147  0.100  1   PRO AAA CB  
3421  C CG  A PRO C 1   ? 1.277 1.315 1.230 0.013  0.144  0.096  1   PRO AAA CG  
3422  C CD  A PRO C 1   ? 1.264 1.310 1.219 0.012  0.147  0.100  1   PRO AAA CD  
3423  N N   . ILE C 2   ? 1.227 1.232 1.150 0.014  0.153  0.113  2   ILE AAA N   
3424  C CA  . ILE C 2   ? 1.103 1.096 1.019 0.012  0.154  0.117  2   ILE AAA CA  
3425  C C   . ILE C 2   ? 1.075 1.066 0.997 0.011  0.148  0.115  2   ILE AAA C   
3426  O O   . ILE C 2   ? 1.030 1.026 0.951 0.012  0.145  0.112  2   ILE AAA O   
3427  C CB  . ILE C 2   ? 1.030 1.014 0.930 0.011  0.158  0.121  2   ILE AAA CB  
3428  C CG1 . ILE C 2   ? 1.025 1.010 0.921 0.014  0.164  0.123  2   ILE AAA CG1 
3429  C CG2 . ILE C 2   ? 1.154 1.127 1.047 0.009  0.158  0.125  2   ILE AAA CG2 
3430  C CD1 . ILE C 2   ? 1.049 1.035 0.950 0.015  0.169  0.127  2   ILE AAA CD1 
3431  N N   . VAL C 3   ? 1.119 1.105 1.047 0.010  0.146  0.117  3   VAL AAA N   
3432  C CA  . VAL C 3   ? 1.210 1.192 1.144 0.011  0.140  0.116  3   VAL AAA CA  
3433  C C   . VAL C 3   ? 1.320 1.290 1.248 0.008  0.140  0.123  3   VAL AAA C   
3434  O O   . VAL C 3   ? 1.430 1.397 1.352 0.005  0.144  0.128  3   VAL AAA O   
3435  C CB  . VAL C 3   ? 1.253 1.236 1.199 0.012  0.137  0.110  3   VAL AAA CB  
3436  C CG1 . VAL C 3   ? 1.318 1.314 1.268 0.014  0.137  0.102  3   VAL AAA CG1 
3437  C CG2 . VAL C 3   ? 1.233 1.213 1.184 0.008  0.138  0.114  3   VAL AAA CG2 
3438  N N   . GLN C 4   ? 1.434 1.401 1.366 0.009  0.134  0.124  4   GLN AAA N   
3439  C CA  . GLN C 4   ? 1.586 1.544 1.516 0.006  0.132  0.132  4   GLN AAA CA  
3440  C C   . GLN C 4   ? 1.623 1.575 1.564 0.005  0.130  0.133  4   GLN AAA C   
3441  O O   . GLN C 4   ? 1.625 1.577 1.578 0.009  0.127  0.126  4   GLN AAA O   
3442  C CB  . GLN C 4   ? 1.707 1.665 1.637 0.008  0.127  0.134  4   GLN AAA CB  
3443  C CG  . GLN C 4   ? 1.886 1.835 1.811 0.004  0.124  0.144  4   GLN AAA CG  
3444  C CD  . GLN C 4   ? 1.942 1.894 1.863 0.004  0.120  0.149  4   GLN AAA CD  
3445  O OE1 . GLN C 4   ? 1.967 1.927 1.886 0.006  0.119  0.145  4   GLN AAA OE1 
3446  N NE2 . GLN C 4   ? 2.112 2.058 2.031 0.001  0.116  0.158  4   GLN AAA NE2 
3447  N N   . ASN C 5   ? 1.710 1.656 1.648 0.001  0.132  0.140  5   ASN AAA N   
3448  C CA  . ASN C 5   ? 1.825 1.765 1.774 -0.002 0.129  0.142  5   ASN AAA CA  
3449  C C   . ASN C 5   ? 1.993 1.922 1.944 -0.002 0.123  0.149  5   ASN AAA C   
3450  O O   . ASN C 5   ? 2.111 2.040 2.058 0.001  0.120  0.150  5   ASN AAA O   
3451  C CB  . ASN C 5   ? 1.814 1.757 1.760 -0.007 0.134  0.148  5   ASN AAA CB  
3452  C CG  . ASN C 5   ? 1.798 1.738 1.733 -0.011 0.137  0.157  5   ASN AAA CG  
3453  O OD1 . ASN C 5   ? 1.947 1.879 1.883 -0.014 0.133  0.165  5   ASN AAA OD1 
3454  N ND2 . ASN C 5   ? 1.833 1.778 1.755 -0.011 0.144  0.158  5   ASN AAA ND2 
3455  N N   . LEU C 6   ? 2.046 1.966 2.005 -0.006 0.120  0.153  6   LEU AAA N   
3456  C CA  . LEU C 6   ? 1.998 1.906 1.961 -0.006 0.113  0.160  6   LEU AAA CA  
3457  C C   . LEU C 6   ? 1.949 1.858 1.901 -0.009 0.114  0.171  6   LEU AAA C   
3458  O O   . LEU C 6   ? 2.056 1.960 2.008 -0.007 0.109  0.176  6   LEU AAA O   
3459  C CB  . LEU C 6   ? 2.067 1.963 2.039 -0.010 0.109  0.163  6   LEU AAA CB  
3460  C CG  . LEU C 6   ? 2.118 2.006 2.101 -0.006 0.106  0.151  6   LEU AAA CG  
3461  C CD1 . LEU C 6   ? 2.112 2.000 2.099 0.004  0.103  0.145  6   LEU AAA CD1 
3462  C CD2 . LEU C 6   ? 2.105 2.004 2.088 -0.007 0.110  0.142  6   LEU AAA CD2 
3463  N N   . GLN C 7   ? 1.924 1.839 1.865 -0.015 0.120  0.175  7   GLN AAA N   
3464  C CA  . GLN C 7   ? 1.962 1.879 1.888 -0.017 0.122  0.182  7   GLN AAA CA  
3465  C C   . GLN C 7   ? 2.079 2.003 1.996 -0.013 0.124  0.175  7   GLN AAA C   
3466  O O   . GLN C 7   ? 2.111 2.040 2.033 -0.009 0.126  0.165  7   GLN AAA O   
3467  C CB  . GLN C 7   ? 1.941 1.861 1.857 -0.024 0.129  0.189  7   GLN AAA CB  
3468  C CG  . GLN C 7   ? 1.983 1.898 1.908 -0.029 0.126  0.198  7   GLN AAA CG  
3469  C CD  . GLN C 7   ? 2.025 1.946 1.940 -0.036 0.133  0.205  7   GLN AAA CD  
3470  O OE1 . GLN C 7   ? 2.077 2.005 1.978 -0.035 0.140  0.203  7   GLN AAA OE1 
3471  N NE2 . GLN C 7   ? 2.000 1.919 1.922 -0.042 0.131  0.214  7   GLN AAA NE2 
3472  N N   . GLY C 8   ? 2.397 2.322 2.300 -0.016 0.124  0.180  8   GLY AAA N   
3473  C CA  . GLY C 8   ? 2.358 2.288 2.252 -0.014 0.125  0.174  8   GLY AAA CA  
3474  C C   . GLY C 8   ? 2.275 2.209 2.161 -0.013 0.133  0.166  8   GLY AAA C   
3475  O O   . GLY C 8   ? 2.291 2.228 2.173 -0.011 0.133  0.161  8   GLY AAA O   
3476  N N   . GLN C 9   ? 2.054 1.987 1.940 -0.014 0.139  0.167  9   GLN AAA N   
3477  C CA  . GLN C 9   ? 1.943 1.879 1.820 -0.012 0.148  0.162  9   GLN AAA CA  
3478  C C   . GLN C 9   ? 1.790 1.732 1.679 -0.007 0.148  0.154  9   GLN AAA C   
3479  O O   . GLN C 9   ? 1.731 1.676 1.636 -0.006 0.144  0.152  9   GLN AAA O   
3480  C CB  . GLN C 9   ? 1.916 1.853 1.789 -0.015 0.155  0.167  9   GLN AAA CB  
3481  C CG  . GLN C 9   ? 1.985 1.925 1.851 -0.011 0.164  0.163  9   GLN AAA CG  
3482  C CD  . GLN C 9   ? 2.101 2.047 1.971 -0.013 0.171  0.169  9   GLN AAA CD  
3483  O OE1 . GLN C 9   ? 2.136 2.082 2.011 -0.017 0.168  0.176  9   GLN AAA OE1 
3484  N NE2 . GLN C 9   ? 2.112 2.063 1.980 -0.008 0.179  0.167  9   GLN AAA NE2 
3485  N N   . MET C 10  ? 1.621 1.565 1.501 -0.005 0.152  0.149  10  MET AAA N   
3486  C CA  . MET C 10  ? 1.490 1.441 1.378 -0.001 0.153  0.142  10  MET AAA CA  
3487  C C   . MET C 10  ? 1.438 1.394 1.329 0.001  0.159  0.142  10  MET AAA C   
3488  O O   . MET C 10  ? 1.459 1.412 1.339 0.001  0.167  0.144  10  MET AAA O   
3489  C CB  . MET C 10  ? 1.463 1.414 1.340 -0.001 0.153  0.138  10  MET AAA CB  
3490  C CG  . MET C 10  ? 1.574 1.524 1.450 -0.002 0.145  0.139  10  MET AAA CG  
3491  S SD  . MET C 10  ? 1.799 1.756 1.672 -0.002 0.143  0.134  10  MET AAA SD  
3492  C CE  . MET C 10  ? 1.709 1.654 1.557 -0.006 0.148  0.135  10  MET AAA CE  
3493  N N   . VAL C 11  ? 1.352 1.315 1.259 0.002  0.157  0.139  11  VAL AAA N   
3494  C CA  . VAL C 11  ? 1.327 1.299 1.241 0.003  0.162  0.140  11  VAL AAA CA  
3495  C C   . VAL C 11  ? 1.320 1.301 1.242 0.005  0.161  0.134  11  VAL AAA C   
3496  O O   . VAL C 11  ? 1.360 1.342 1.287 0.006  0.155  0.129  11  VAL AAA O   
3497  C CB  . VAL C 11  ? 1.406 1.379 1.330 -0.002 0.161  0.145  11  VAL AAA CB  
3498  C CG1 . VAL C 11  ? 1.561 1.526 1.476 -0.005 0.163  0.153  11  VAL AAA CG1 
3499  C CG2 . VAL C 11  ? 1.425 1.396 1.362 -0.003 0.152  0.141  11  VAL AAA CG2 
3500  N N   . HIS C 12  ? 1.310 1.299 1.235 0.007  0.166  0.136  12  HIS AAA N   
3501  C CA  . HIS C 12  ? 1.228 1.229 1.161 0.009  0.165  0.131  12  HIS AAA CA  
3502  C C   . HIS C 12  ? 1.305 1.312 1.253 0.005  0.160  0.129  12  HIS AAA C   
3503  O O   . HIS C 12  ? 1.483 1.490 1.437 0.001  0.159  0.134  12  HIS AAA O   
3504  C CB  . HIS C 12  ? 1.266 1.275 1.198 0.013  0.173  0.135  12  HIS AAA CB  
3505  C CG  . HIS C 12  ? 1.242 1.264 1.182 0.015  0.172  0.133  12  HIS AAA CG  
3506  N ND1 . HIS C 12  ? 1.338 1.375 1.292 0.013  0.171  0.135  12  HIS AAA ND1 
3507  C CD2 . HIS C 12  ? 1.256 1.281 1.193 0.018  0.171  0.130  12  HIS AAA CD2 
3508  C CE1 . HIS C 12  ? 1.414 1.461 1.372 0.014  0.169  0.133  12  HIS AAA CE1 
3509  N NE2 . HIS C 12  ? 1.331 1.372 1.279 0.018  0.170  0.130  12  HIS AAA NE2 
3510  N N   . GLN C 13  ? 1.190 1.204 1.143 0.006  0.156  0.123  13  GLN AAA N   
3511  C CA  . GLN C 13  ? 1.203 1.222 1.167 0.002  0.150  0.118  13  GLN AAA CA  
3512  C C   . GLN C 13  ? 1.210 1.245 1.179 0.003  0.150  0.115  13  GLN AAA C   
3513  O O   . GLN C 13  ? 1.183 1.222 1.146 0.007  0.152  0.114  13  GLN AAA O   
3514  C CB  . GLN C 13  ? 1.226 1.236 1.192 0.002  0.144  0.111  13  GLN AAA CB  
3515  C CG  . GLN C 13  ? 1.425 1.430 1.400 -0.003 0.139  0.109  13  GLN AAA CG  
3516  C CD  . GLN C 13  ? 1.593 1.584 1.568 -0.001 0.133  0.103  13  GLN AAA CD  
3517  O OE1 . GLN C 13  ? 1.652 1.644 1.623 0.005  0.134  0.099  13  GLN AAA OE1 
3518  N NE2 . GLN C 13  ? 1.744 1.724 1.725 -0.004 0.129  0.103  13  GLN AAA NE2 
3519  N N   . CYS C 14  ? 1.292 1.336 1.271 -0.002 0.148  0.116  14  CYS AAA N   
3520  C CA  . CYS C 14  ? 1.301 1.361 1.283 -0.003 0.147  0.114  14  CYS AAA CA  
3521  C C   . CYS C 14  ? 1.264 1.324 1.243 -0.001 0.143  0.104  14  CYS AAA C   
3522  O O   . CYS C 14  ? 1.306 1.355 1.285 -0.002 0.139  0.097  14  CYS AAA O   
3523  C CB  . CYS C 14  ? 1.383 1.452 1.376 -0.010 0.143  0.115  14  CYS AAA CB  
3524  S SG  . CYS C 14  ? 1.507 1.583 1.506 -0.013 0.148  0.129  14  CYS AAA SG  
3525  N N   . ILE C 15  ? 1.202 1.276 1.180 0.001  0.144  0.103  15  ILE AAA N   
3526  C CA  . ILE C 15  ? 1.201 1.279 1.176 0.002  0.140  0.094  15  ILE AAA CA  
3527  C C   . ILE C 15  ? 1.197 1.277 1.178 -0.004 0.134  0.086  15  ILE AAA C   
3528  O O   . ILE C 15  ? 1.217 1.304 1.204 -0.010 0.133  0.090  15  ILE AAA O   
3529  C CB  . ILE C 15  ? 1.173 1.267 1.146 0.004  0.142  0.097  15  ILE AAA CB  
3530  C CG1 . ILE C 15  ? 1.093 1.194 1.062 0.004  0.139  0.088  15  ILE AAA CG1 
3531  C CG2 . ILE C 15  ? 1.222 1.332 1.202 0.000  0.142  0.103  15  ILE AAA CG2 
3532  C CD1 . ILE C 15  ? 1.198 1.289 1.160 0.009  0.141  0.087  15  ILE AAA CD1 
3533  N N   . SER C 16  ? 1.171 1.243 1.149 -0.003 0.131  0.076  16  SER AAA N   
3534  C CA  . SER C 16  ? 1.207 1.275 1.189 -0.009 0.126  0.068  16  SER AAA CA  
3535  C C   . SER C 16  ? 1.137 1.222 1.118 -0.013 0.123  0.062  16  SER AAA C   
3536  O O   . SER C 16  ? 1.211 1.309 1.188 -0.009 0.125  0.061  16  SER AAA O   
3537  C CB  . SER C 16  ? 1.218 1.269 1.198 -0.005 0.124  0.059  16  SER AAA CB  
3538  O OG  . SER C 16  ? 1.324 1.369 1.304 -0.009 0.119  0.049  16  SER AAA OG  
3539  N N   . PRO C 17  ? 1.080 1.165 1.063 -0.021 0.118  0.059  17  PRO AAA N   
3540  C CA  . PRO C 17  ? 1.151 1.252 1.132 -0.026 0.115  0.052  17  PRO AAA CA  
3541  C C   . PRO C 17  ? 1.179 1.278 1.153 -0.021 0.114  0.038  17  PRO AAA C   
3542  O O   . PRO C 17  ? 1.133 1.249 1.102 -0.021 0.114  0.035  17  PRO AAA O   
3543  C CB  . PRO C 17  ? 1.205 1.301 1.189 -0.037 0.109  0.050  17  PRO AAA CB  
3544  C CG  . PRO C 17  ? 1.249 1.338 1.241 -0.038 0.111  0.063  17  PRO AAA CG  
3545  C CD  . PRO C 17  ? 1.243 1.319 1.233 -0.028 0.116  0.064  17  PRO AAA CD  
3546  N N   . ARG C 18  ? 1.177 1.255 1.149 -0.016 0.114  0.031  18  ARG AAA N   
3547  C CA  . ARG C 18  ? 1.160 1.237 1.126 -0.010 0.115  0.018  18  ARG AAA CA  
3548  C C   . ARG C 18  ? 1.121 1.213 1.084 -0.003 0.120  0.022  18  ARG AAA C   
3549  O O   . ARG C 18  ? 1.199 1.305 1.156 -0.002 0.120  0.014  18  ARG AAA O   
3550  C CB  . ARG C 18  ? 1.217 1.269 1.185 -0.004 0.114  0.012  18  ARG AAA CB  
3551  C CG  . ARG C 18  ? 1.361 1.393 1.326 -0.009 0.109  0.002  18  ARG AAA CG  
3552  C CD  . ARG C 18  ? 1.479 1.491 1.445 0.000  0.110  -0.007 18  ARG AAA CD  
3553  N NE  . ARG C 18  ? 1.701 1.690 1.664 -0.003 0.105  -0.019 18  ARG AAA NE  
3554  C CZ  . ARG C 18  ? 1.813 1.801 1.768 -0.001 0.105  -0.035 18  ARG AAA CZ  
3555  N NH1 . ARG C 18  ? 1.782 1.792 1.731 0.004  0.109  -0.040 18  ARG AAA NH1 
3556  N NH2 . ARG C 18  ? 1.839 1.801 1.790 -0.003 0.101  -0.046 18  ARG AAA NH2 
3557  N N   . THR C 19  ? 1.083 1.173 1.049 0.001  0.123  0.033  19  THR AAA N   
3558  C CA  . THR C 19  ? 1.083 1.187 1.046 0.006  0.127  0.037  19  THR AAA CA  
3559  C C   . THR C 19  ? 1.092 1.218 1.053 0.001  0.127  0.041  19  THR AAA C   
3560  O O   . THR C 19  ? 1.164 1.305 1.121 0.003  0.128  0.038  19  THR AAA O   
3561  C CB  . THR C 19  ? 1.143 1.237 1.108 0.009  0.130  0.048  19  THR AAA CB  
3562  O OG1 . THR C 19  ? 1.228 1.332 1.189 0.013  0.132  0.051  19  THR AAA OG1 
3563  C CG2 . THR C 19  ? 1.298 1.391 1.265 0.005  0.131  0.059  19  THR AAA CG2 
3564  N N   . LEU C 20  ? 1.039 1.168 1.003 -0.004 0.126  0.049  20  LEU AAA N   
3565  C CA  . LEU C 20  ? 1.072 1.222 1.035 -0.007 0.126  0.055  20  LEU AAA CA  
3566  C C   . LEU C 20  ? 1.125 1.290 1.083 -0.011 0.122  0.045  20  LEU AAA C   
3567  O O   . LEU C 20  ? 1.128 1.311 1.083 -0.010 0.123  0.046  20  LEU AAA O   
3568  C CB  . LEU C 20  ? 1.058 1.212 1.029 -0.012 0.125  0.065  20  LEU AAA CB  
3569  C CG  . LEU C 20  ? 1.172 1.316 1.146 -0.008 0.129  0.077  20  LEU AAA CG  
3570  C CD1 . LEU C 20  ? 1.163 1.310 1.146 -0.013 0.128  0.084  20  LEU AAA CD1 
3571  C CD2 . LEU C 20  ? 1.153 1.307 1.124 -0.004 0.133  0.086  20  LEU AAA CD2 
3572  N N   . ASN C 21  ? 1.159 1.316 1.117 -0.015 0.119  0.034  21  ASN AAA N   
3573  C CA  . ASN C 21  ? 1.121 1.291 1.072 -0.019 0.116  0.022  21  ASN AAA CA  
3574  C C   . ASN C 21  ? 1.103 1.276 1.047 -0.012 0.119  0.014  21  ASN AAA C   
3575  O O   . ASN C 21  ? 1.182 1.375 1.120 -0.013 0.119  0.011  21  ASN AAA O   
3576  C CB  . ASN C 21  ? 1.193 1.348 1.142 -0.025 0.111  0.011  21  ASN AAA CB  
3577  C CG  . ASN C 21  ? 1.325 1.491 1.265 -0.031 0.108  -0.002 21  ASN AAA CG  
3578  O OD1 . ASN C 21  ? 1.412 1.601 1.347 -0.032 0.108  0.000  21  ASN AAA OD1 
3579  N ND2 . ASN C 21  ? 1.394 1.543 1.329 -0.035 0.104  -0.015 21  ASN AAA ND2 
3580  N N   . ALA C 22  ? 1.082 1.239 1.028 -0.004 0.122  0.011  22  ALA AAA N   
3581  C CA  . ALA C 22  ? 1.101 1.263 1.043 0.003  0.125  0.004  22  ALA AAA CA  
3582  C C   . ALA C 22  ? 1.078 1.262 1.018 0.004  0.128  0.014  22  ALA AAA C   
3583  O O   . ALA C 22  ? 1.106 1.307 1.040 0.005  0.129  0.008  22  ALA AAA O   
3584  C CB  . ALA C 22  ? 1.075 1.218 1.022 0.011  0.127  0.004  22  ALA AAA CB  
3585  N N   . TRP C 23  ? 1.016 1.198 0.960 0.003  0.129  0.028  23  TRP AAA N   
3586  C CA  . TRP C 23  ? 1.005 1.203 0.946 0.003  0.130  0.038  23  TRP AAA CA  
3587  C C   . TRP C 23  ? 1.032 1.252 0.969 -0.003 0.128  0.039  23  TRP AAA C   
3588  O O   . TRP C 23  ? 1.149 1.388 1.081 -0.003 0.129  0.040  23  TRP AAA O   
3589  C CB  . TRP C 23  ? 0.976 1.165 0.922 0.003  0.132  0.052  23  TRP AAA CB  
3590  C CG  . TRP C 23  ? 0.976 1.177 0.918 0.003  0.133  0.063  23  TRP AAA CG  
3591  C CD1 . TRP C 23  ? 1.025 1.231 0.968 0.000  0.133  0.074  23  TRP AAA CD1 
3592  C CD2 . TRP C 23  ? 0.978 1.189 0.915 0.004  0.135  0.064  23  TRP AAA CD2 
3593  N NE1 . TRP C 23  ? 1.050 1.264 0.988 -0.000 0.134  0.082  23  TRP AAA NE1 
3594  C CE2 . TRP C 23  ? 1.014 1.233 0.949 0.001  0.135  0.076  23  TRP AAA CE2 
3595  C CE3 . TRP C 23  ? 1.015 1.230 0.951 0.008  0.136  0.056  23  TRP AAA CE3 
3596  C CZ2 . TRP C 23  ? 1.028 1.257 0.958 0.000  0.136  0.081  23  TRP AAA CZ2 
3597  C CZ3 . TRP C 23  ? 1.085 1.313 1.017 0.007  0.137  0.061  23  TRP AAA CZ3 
3598  C CH2 . TRP C 23  ? 1.071 1.306 1.000 0.002  0.137  0.073  23  TRP AAA CH2 
3599  N N   . VAL C 24  ? 1.061 1.282 1.001 -0.009 0.125  0.041  24  VAL AAA N   
3600  C CA  . VAL C 24  ? 1.074 1.318 1.011 -0.015 0.122  0.043  24  VAL AAA CA  
3601  C C   . VAL C 24  ? 1.121 1.377 1.049 -0.017 0.122  0.029  24  VAL AAA C   
3602  O O   . VAL C 24  ? 1.249 1.528 1.171 -0.019 0.121  0.031  24  VAL AAA O   
3603  C CB  . VAL C 24  ? 1.095 1.338 1.038 -0.022 0.118  0.047  24  VAL AAA CB  
3604  C CG1 . VAL C 24  ? 1.262 1.528 1.199 -0.030 0.114  0.045  24  VAL AAA CG1 
3605  C CG2 . VAL C 24  ? 1.089 1.328 1.040 -0.020 0.120  0.063  24  VAL AAA CG2 
3606  N N   . LYS C 25  ? 1.130 1.372 1.056 -0.014 0.122  0.014  25  LYS AAA N   
3607  C CA  . LYS C 25  ? 1.209 1.461 1.125 -0.015 0.122  -0.001 25  LYS AAA CA  
3608  C C   . LYS C 25  ? 1.245 1.511 1.158 -0.008 0.127  -0.003 25  LYS AAA C   
3609  O O   . LYS C 25  ? 1.342 1.629 1.246 -0.010 0.127  -0.008 25  LYS AAA O   
3610  C CB  . LYS C 25  ? 1.292 1.521 1.206 -0.013 0.120  -0.017 25  LYS AAA CB  
3611  C CG  . LYS C 25  ? 1.429 1.653 1.342 -0.024 0.114  -0.019 25  LYS AAA CG  
3612  C CD  . LYS C 25  ? 1.565 1.764 1.475 -0.023 0.113  -0.035 25  LYS AAA CD  
3613  C CE  . LYS C 25  ? 1.657 1.854 1.564 -0.036 0.106  -0.037 25  LYS AAA CE  
3614  N NZ  . LYS C 25  ? 1.763 1.931 1.667 -0.037 0.103  -0.051 25  LYS AAA NZ  
3615  N N   . VAL C 26  ? 1.201 1.455 1.119 -0.001 0.130  0.001  26  VAL AAA N   
3616  C CA  . VAL C 26  ? 1.149 1.418 1.065 0.005  0.134  0.000  26  VAL AAA CA  
3617  C C   . VAL C 26  ? 1.162 1.456 1.075 -0.000 0.134  0.012  26  VAL AAA C   
3618  O O   . VAL C 26  ? 1.356 1.672 1.263 0.000  0.136  0.009  26  VAL AAA O   
3619  C CB  . VAL C 26  ? 1.125 1.379 1.049 0.013  0.137  0.004  26  VAL AAA CB  
3620  C CG1 . VAL C 26  ? 1.186 1.417 1.113 0.018  0.137  -0.007 26  VAL AAA CG1 
3621  C CG2 . VAL C 26  ? 1.147 1.391 1.076 0.010  0.136  0.021  26  VAL AAA CG2 
3622  N N   . VAL C 27  ? 1.118 1.409 1.035 -0.005 0.132  0.027  27  VAL AAA N   
3623  C CA  . VAL C 27  ? 1.197 1.509 1.110 -0.010 0.131  0.039  27  VAL AAA CA  
3624  C C   . VAL C 27  ? 1.334 1.669 1.240 -0.017 0.128  0.034  27  VAL AAA C   
3625  O O   . VAL C 27  ? 1.338 1.696 1.238 -0.020 0.129  0.037  27  VAL AAA O   
3626  C CB  . VAL C 27  ? 1.145 1.446 1.064 -0.012 0.129  0.055  27  VAL AAA CB  
3627  C CG1 . VAL C 27  ? 1.208 1.530 1.125 -0.017 0.127  0.068  27  VAL AAA CG1 
3628  C CG2 . VAL C 27  ? 1.149 1.430 1.073 -0.007 0.132  0.060  27  VAL AAA CG2 
3629  N N   . GLU C 28  ? 1.389 1.718 1.294 -0.020 0.125  0.026  28  GLU AAA N   
3630  C CA  . GLU C 28  ? 1.429 1.779 1.325 -0.028 0.122  0.020  28  GLU AAA CA  
3631  C C   . GLU C 28  ? 1.476 1.838 1.362 -0.025 0.125  0.004  28  GLU AAA C   
3632  O O   . GLU C 28  ? 1.669 2.057 1.545 -0.030 0.125  0.004  28  GLU AAA O   
3633  C CB  . GLU C 28  ? 1.518 1.855 1.414 -0.033 0.117  0.013  28  GLU AAA CB  
3634  C CG  . GLU C 28  ? 1.701 2.039 1.606 -0.038 0.113  0.030  28  GLU AAA CG  
3635  C CD  . GLU C 28  ? 1.881 2.211 1.788 -0.044 0.108  0.024  28  GLU AAA CD  
3636  O OE1 . GLU C 28  ? 1.895 2.215 1.794 -0.046 0.107  0.007  28  GLU AAA OE1 
3637  O OE2 . GLU C 28  ? 1.881 2.215 1.795 -0.049 0.104  0.038  28  GLU AAA OE2 
3638  N N   . GLU C 29  ? 1.506 1.850 1.392 -0.016 0.129  -0.008 29  GLU AAA N   
3639  C CA  . GLU C 29  ? 1.533 1.889 1.411 -0.012 0.133  -0.025 29  GLU AAA CA  
3640  C C   . GLU C 29  ? 1.489 1.863 1.367 -0.006 0.139  -0.019 29  GLU AAA C   
3641  O O   . GLU C 29  ? 1.639 2.037 1.509 -0.006 0.142  -0.027 29  GLU AAA O   
3642  C CB  . GLU C 29  ? 1.633 1.962 1.511 -0.004 0.135  -0.041 29  GLU AAA CB  
3643  C CG  . GLU C 29  ? 1.819 2.132 1.693 -0.012 0.130  -0.050 29  GLU AAA CG  
3644  C CD  . GLU C 29  ? 2.043 2.323 1.922 -0.005 0.130  -0.060 29  GLU AAA CD  
3645  O OE1 . GLU C 29  ? 2.091 2.359 1.977 0.005  0.134  -0.059 29  GLU AAA OE1 
3646  O OE2 . GLU C 29  ? 2.159 2.424 2.034 -0.012 0.125  -0.068 29  GLU AAA OE2 
3647  N N   . LYS C 30  ? 1.319 1.684 1.208 -0.003 0.140  -0.007 30  LYS AAA N   
3648  C CA  . LYS C 30  ? 1.317 1.698 1.208 0.001  0.144  -0.001 30  LYS AAA CA  
3649  C C   . LYS C 30  ? 1.280 1.674 1.172 -0.006 0.142  0.019  30  LYS AAA C   
3650  O O   . LYS C 30  ? 1.342 1.753 1.234 -0.005 0.145  0.025  30  LYS AAA O   
3651  C CB  . LYS C 30  ? 1.308 1.669 1.208 0.011  0.147  -0.003 30  LYS AAA CB  
3652  C CG  . LYS C 30  ? 1.475 1.836 1.373 0.021  0.152  -0.022 30  LYS AAA CG  
3653  C CD  . LYS C 30  ? 1.571 1.921 1.479 0.031  0.155  -0.022 30  LYS AAA CD  
3654  C CE  . LYS C 30  ? 1.621 1.983 1.527 0.042  0.161  -0.037 30  LYS AAA CE  
3655  N NZ  . LYS C 30  ? 1.741 2.083 1.642 0.047  0.162  -0.056 30  LYS AAA NZ  
3656  N N   . ALA C 31  ? 1.235 1.622 1.128 -0.012 0.137  0.030  31  ALA AAA N   
3657  C CA  . ALA C 31  ? 1.249 1.643 1.144 -0.018 0.135  0.049  31  ALA AAA CA  
3658  C C   . ALA C 31  ? 1.240 1.622 1.141 -0.015 0.137  0.058  31  ALA AAA C   
3659  O O   . ALA C 31  ? 1.297 1.654 1.203 -0.010 0.137  0.057  31  ALA AAA O   
3660  C CB  . ALA C 31  ? 1.341 1.767 1.228 -0.024 0.135  0.054  31  ALA AAA CB  
3661  N N   . PHE C 32  ? 1.199 1.600 1.097 -0.019 0.137  0.069  32  PHE AAA N   
3662  C CA  . PHE C 32  ? 1.238 1.631 1.139 -0.018 0.138  0.078  32  PHE AAA CA  
3663  C C   . PHE C 32  ? 1.241 1.655 1.143 -0.016 0.142  0.074  32  PHE AAA C   
3664  O O   . PHE C 32  ? 1.358 1.784 1.259 -0.020 0.142  0.085  32  PHE AAA O   
3665  C CB  . PHE C 32  ? 1.299 1.691 1.198 -0.025 0.135  0.097  32  PHE AAA CB  
3666  C CG  . PHE C 32  ? 1.272 1.642 1.174 -0.025 0.132  0.103  32  PHE AAA CG  
3667  C CD1 . PHE C 32  ? 1.237 1.577 1.143 -0.021 0.133  0.105  32  PHE AAA CD1 
3668  C CD2 . PHE C 32  ? 1.353 1.732 1.253 -0.029 0.129  0.108  32  PHE AAA CD2 
3669  C CE1 . PHE C 32  ? 1.220 1.541 1.129 -0.021 0.131  0.111  32  PHE AAA CE1 
3670  C CE2 . PHE C 32  ? 1.348 1.709 1.252 -0.028 0.127  0.114  32  PHE AAA CE2 
3671  C CZ  . PHE C 32  ? 1.261 1.593 1.169 -0.023 0.129  0.116  32  PHE AAA CZ  
3672  N N   . SER C 33  ? 1.205 1.624 1.107 -0.008 0.146  0.057  33  SER AAA N   
3673  C CA  . SER C 33  ? 1.272 1.706 1.176 -0.003 0.150  0.052  33  SER AAA CA  
3674  C C   . SER C 33  ? 1.266 1.681 1.179 0.000  0.150  0.058  33  SER AAA C   
3675  O O   . SER C 33  ? 1.359 1.743 1.274 0.002  0.147  0.058  33  SER AAA O   
3676  C CB  . SER C 33  ? 1.366 1.805 1.270 0.006  0.154  0.031  33  SER AAA CB  
3677  O OG  . SER C 33  ? 1.530 1.987 1.424 0.003  0.155  0.025  33  SER AAA OG  
3678  N N   . PRO C 34  ? 1.252 1.683 1.168 0.001  0.152  0.063  34  PRO AAA N   
3679  C CA  . PRO C 34  ? 1.201 1.615 1.124 0.001  0.150  0.071  34  PRO AAA CA  
3680  C C   . PRO C 34  ? 1.160 1.546 1.088 0.010  0.150  0.062  34  PRO AAA C   
3681  O O   . PRO C 34  ? 1.161 1.523 1.091 0.008  0.147  0.069  34  PRO AAA O   
3682  C CB  . PRO C 34  ? 1.295 1.739 1.221 0.001  0.152  0.075  34  PRO AAA CB  
3683  C CG  . PRO C 34  ? 1.376 1.848 1.300 0.006  0.157  0.063  34  PRO AAA CG  
3684  C CD  . PRO C 34  ? 1.350 1.818 1.265 0.001  0.156  0.061  34  PRO AAA CD  
3685  N N   . GLU C 35  ? 1.232 1.620 1.163 0.019  0.153  0.047  35  GLU AAA N   
3686  C CA  . GLU C 35  ? 1.239 1.601 1.176 0.028  0.153  0.038  35  GLU AAA CA  
3687  C C   . GLU C 35  ? 1.222 1.554 1.157 0.025  0.150  0.040  35  GLU AAA C   
3688  O O   . GLU C 35  ? 1.230 1.538 1.170 0.030  0.149  0.036  35  GLU AAA O   
3689  C CB  . GLU C 35  ? 1.277 1.648 1.216 0.039  0.158  0.021  35  GLU AAA CB  
3690  C CG  . GLU C 35  ? 1.329 1.699 1.259 0.037  0.158  0.010  35  GLU AAA CG  
3691  C CD  . GLU C 35  ? 1.456 1.861 1.379 0.032  0.161  0.010  35  GLU AAA CD  
3692  O OE1 . GLU C 35  ? 1.518 1.943 1.442 0.028  0.161  0.023  35  GLU AAA OE1 
3693  O OE2 . GLU C 35  ? 1.570 1.981 1.484 0.033  0.162  -0.002 35  GLU AAA OE2 
3694  N N   . VAL C 36  ? 1.228 1.560 1.157 0.016  0.147  0.045  36  VAL AAA N   
3695  C CA  . VAL C 36  ? 1.117 1.424 1.045 0.014  0.144  0.048  36  VAL AAA CA  
3696  C C   . VAL C 36  ? 1.063 1.349 0.993 0.012  0.143  0.059  36  VAL AAA C   
3697  O O   . VAL C 36  ? 1.202 1.464 1.135 0.013  0.142  0.059  36  VAL AAA O   
3698  C CB  A VAL C 36  ? 1.106 1.422 1.028 0.006  0.143  0.052  36  VAL AAA CB  
3699  C CG1 A VAL C 36  ? 1.119 1.413 1.041 0.003  0.140  0.061  36  VAL AAA CG1 
3700  C CG2 A VAL C 36  ? 1.192 1.517 1.110 0.008  0.143  0.038  36  VAL AAA CG2 
3701  N N   . ILE C 37  ? 1.041 1.337 0.970 0.008  0.142  0.070  37  ILE AAA N   
3702  C CA  . ILE C 37  ? 1.035 1.310 0.964 0.005  0.140  0.080  37  ILE AAA CA  
3703  C C   . ILE C 37  ? 1.080 1.339 1.014 0.012  0.141  0.074  37  ILE AAA C   
3704  O O   . ILE C 37  ? 1.143 1.377 1.077 0.012  0.140  0.077  37  ILE AAA O   
3705  C CB  . ILE C 37  ? 1.035 1.324 0.960 -0.002 0.139  0.091  37  ILE AAA CB  
3706  C CG1 . ILE C 37  ? 1.092 1.395 1.011 -0.009 0.138  0.098  37  ILE AAA CG1 
3707  C CG2 . ILE C 37  ? 1.022 1.288 0.944 -0.006 0.137  0.100  37  ILE AAA CG2 
3708  C CD1 . ILE C 37  ? 1.209 1.539 1.127 -0.015 0.138  0.105  37  ILE AAA CD1 
3709  N N   . PRO C 38  ? 1.027 1.298 0.967 0.019  0.143  0.067  38  PRO AAA N   
3710  C CA  A PRO C 38  ? 1.025 1.279 0.972 0.026  0.142  0.062  38  PRO AAA CA  
3711  C C   . PRO C 38  ? 1.013 1.245 0.960 0.029  0.142  0.055  38  PRO AAA C   
3712  O O   . PRO C 38  ? 1.084 1.294 1.033 0.029  0.140  0.058  38  PRO AAA O   
3713  C CB  A PRO C 38  ? 1.055 1.331 1.009 0.035  0.145  0.053  38  PRO AAA CB  
3714  C CG  A PRO C 38  ? 1.086 1.392 1.037 0.030  0.147  0.059  38  PRO AAA CG  
3715  C CD  A PRO C 38  ? 1.053 1.355 0.996 0.018  0.144  0.069  38  PRO AAA CD  
3716  N N   . MET C 39  ? 1.023 1.261 0.969 0.029  0.143  0.046  39  MET AAA N   
3717  C CA  . MET C 39  ? 1.015 1.234 0.961 0.031  0.142  0.039  39  MET AAA CA  
3718  C C   . MET C 39  ? 1.070 1.270 1.014 0.025  0.140  0.048  39  MET AAA C   
3719  O O   . MET C 39  ? 1.075 1.255 1.023 0.026  0.139  0.048  39  MET AAA O   
3720  C CB  . MET C 39  ? 1.064 1.297 1.007 0.030  0.143  0.029  39  MET AAA CB  
3721  C CG  . MET C 39  ? 1.067 1.281 1.010 0.030  0.141  0.021  39  MET AAA CG  
3722  S SD  . MET C 39  ? 1.127 1.324 1.077 0.040  0.142  0.010  39  MET AAA SD  
3723  C CE  . MET C 39  ? 1.222 1.442 1.170 0.047  0.146  -0.004 39  MET AAA CE  
3724  N N   . PHE C 40  ? 1.018 1.226 0.957 0.019  0.140  0.058  40  PHE AAA N   
3725  C CA  . PHE C 40  ? 1.020 1.211 0.957 0.015  0.139  0.067  40  PHE AAA CA  
3726  C C   . PHE C 40  ? 1.095 1.267 1.032 0.016  0.139  0.072  40  PHE AAA C   
3727  O O   . PHE C 40  ? 1.222 1.376 1.161 0.016  0.139  0.074  40  PHE AAA O   
3728  C CB  . PHE C 40  ? 1.016 1.218 0.947 0.009  0.139  0.077  40  PHE AAA CB  
3729  C CG  . PHE C 40  ? 1.070 1.253 0.998 0.007  0.139  0.087  40  PHE AAA CG  
3730  C CD1 . PHE C 40  ? 1.049 1.227 0.979 0.007  0.139  0.088  40  PHE AAA CD1 
3731  C CD2 . PHE C 40  ? 1.085 1.257 1.007 0.004  0.139  0.095  40  PHE AAA CD2 
3732  C CE1 . PHE C 40  ? 1.050 1.212 0.978 0.006  0.140  0.096  40  PHE AAA CE1 
3733  C CE2 . PHE C 40  ? 1.115 1.268 1.033 0.003  0.140  0.103  40  PHE AAA CE2 
3734  C CZ  . PHE C 40  ? 1.113 1.262 1.034 0.005  0.141  0.104  40  PHE AAA CZ  
3735  N N   . SER C 41  ? 1.059 1.237 0.996 0.016  0.139  0.075  41  SER AAA N   
3736  C CA  . SER C 41  ? 1.128 1.290 1.064 0.016  0.138  0.080  41  SER AAA CA  
3737  C C   . SER C 41  ? 1.108 1.256 1.050 0.022  0.138  0.074  41  SER AAA C   
3738  O O   . SER C 41  ? 1.230 1.359 1.171 0.021  0.137  0.078  41  SER AAA O   
3739  C CB  . SER C 41  ? 1.128 1.303 1.063 0.015  0.137  0.084  41  SER AAA CB  
3740  O OG  . SER C 41  ? 1.303 1.464 1.236 0.013  0.135  0.090  41  SER AAA OG  
3741  N N   . ALA C 42  ? 1.073 1.230 1.022 0.028  0.138  0.064  42  ALA AAA N   
3742  C CA  . ALA C 42  ? 1.067 1.208 1.022 0.033  0.137  0.058  42  ALA AAA CA  
3743  C C   . ALA C 42  ? 1.128 1.253 1.082 0.031  0.137  0.057  42  ALA AAA C   
3744  O O   . ALA C 42  ? 1.209 1.315 1.165 0.031  0.136  0.059  42  ALA AAA O   
3745  C CB  . ALA C 42  ? 1.056 1.208 1.017 0.041  0.138  0.047  42  ALA AAA CB  
3746  N N   . LEU C 43  ? 1.081 1.215 1.033 0.028  0.137  0.054  43  LEU AAA N   
3747  C CA  . LEU C 43  ? 1.066 1.189 1.018 0.024  0.137  0.054  43  LEU AAA CA  
3748  C C   . LEU C 43  ? 1.127 1.239 1.077 0.021  0.138  0.065  43  LEU AAA C   
3749  O O   . LEU C 43  ? 1.191 1.292 1.143 0.019  0.137  0.066  43  LEU AAA O   
3750  C CB  . LEU C 43  ? 1.039 1.178 0.990 0.021  0.136  0.049  43  LEU AAA CB  
3751  C CG  . LEU C 43  ? 1.012 1.158 0.964 0.024  0.136  0.036  43  LEU AAA CG  
3752  C CD1 . LEU C 43  ? 1.027 1.191 0.975 0.020  0.135  0.032  43  LEU AAA CD1 
3753  C CD2 . LEU C 43  ? 1.015 1.141 0.971 0.026  0.134  0.029  43  LEU AAA CD2 
3754  N N   . SER C 44  ? 1.117 1.231 1.061 0.019  0.139  0.073  44  SER AAA N   
3755  C CA  . SER C 44  ? 1.095 1.196 1.034 0.017  0.140  0.082  44  SER AAA CA  
3756  C C   . SER C 44  ? 1.187 1.273 1.123 0.018  0.140  0.086  44  SER AAA C   
3757  O O   . SER C 44  ? 1.301 1.377 1.230 0.015  0.142  0.093  44  SER AAA O   
3758  C CB  . SER C 44  ? 1.067 1.176 0.999 0.014  0.141  0.088  44  SER AAA CB  
3759  O OG  . SER C 44  ? 1.069 1.186 0.998 0.013  0.140  0.089  44  SER AAA OG  
3760  N N   . CYS C 45  ? 1.159 1.242 1.101 0.021  0.138  0.081  45  CYS AAA N   
3761  C CA  . CYS C 45  ? 1.149 1.220 1.090 0.021  0.137  0.085  45  CYS AAA CA  
3762  C C   . CYS C 45  ? 1.181 1.234 1.117 0.019  0.139  0.090  45  CYS AAA C   
3763  O O   . CYS C 45  ? 1.184 1.233 1.126 0.019  0.139  0.088  45  CYS AAA O   
3764  C CB  . CYS C 45  ? 1.203 1.272 1.153 0.026  0.135  0.079  45  CYS AAA CB  
3765  S SG  . CYS C 45  ? 1.472 1.528 1.421 0.027  0.132  0.085  45  CYS AAA SG  
3766  N N   . GLY C 46  ? 1.130 1.175 1.058 0.016  0.140  0.097  46  GLY AAA N   
3767  C CA  . GLY C 46  ? 1.161 1.191 1.084 0.015  0.143  0.102  46  GLY AAA CA  
3768  C C   . GLY C 46  ? 1.160 1.190 1.081 0.014  0.147  0.104  46  GLY AAA C   
3769  O O   . GLY C 46  ? 1.216 1.236 1.133 0.014  0.150  0.108  46  GLY AAA O   
3770  N N   . ALA C 47  ? 1.142 1.184 1.063 0.015  0.147  0.103  47  ALA AAA N   
3771  C CA  . ALA C 47  ? 1.174 1.219 1.096 0.015  0.150  0.105  47  ALA AAA CA  
3772  C C   . ALA C 47  ? 1.139 1.171 1.050 0.015  0.155  0.112  47  ALA AAA C   
3773  O O   . ALA C 47  ? 1.105 1.129 1.005 0.014  0.155  0.114  47  ALA AAA O   
3774  C CB  . ALA C 47  ? 1.179 1.241 1.103 0.015  0.149  0.103  47  ALA AAA CB  
3775  N N   . THR C 48  ? 1.142 1.172 1.055 0.018  0.159  0.115  48  THR AAA N   
3776  C CA  . THR C 48  ? 1.131 1.151 1.034 0.020  0.165  0.121  48  THR AAA CA  
3777  C C   . THR C 48  ? 1.075 1.103 0.978 0.021  0.164  0.123  48  THR AAA C   
3778  O O   . THR C 48  ? 1.121 1.165 1.032 0.020  0.161  0.121  48  THR AAA O   
3779  C CB  . THR C 48  ? 1.173 1.191 1.081 0.024  0.170  0.125  48  THR AAA CB  
3780  O OG1 . THR C 48  ? 1.219 1.255 1.141 0.024  0.169  0.125  48  THR AAA OG1 
3781  C CG2 . THR C 48  ? 1.212 1.224 1.121 0.022  0.169  0.124  48  THR AAA CG2 
3782  N N   . PRO C 49  ? 1.050 1.066 0.943 0.023  0.168  0.128  49  PRO AAA N   
3783  C CA  . PRO C 49  ? 1.148 1.172 1.042 0.025  0.168  0.132  49  PRO AAA CA  
3784  C C   . PRO C 49  ? 1.226 1.268 1.134 0.028  0.169  0.134  49  PRO AAA C   
3785  O O   . PRO C 49  ? 1.387 1.445 1.300 0.026  0.165  0.135  49  PRO AAA O   
3786  C CB  . PRO C 49  ? 1.074 1.076 0.954 0.028  0.173  0.137  49  PRO AAA CB  
3787  C CG  . PRO C 49  ? 1.081 1.066 0.948 0.024  0.173  0.133  49  PRO AAA CG  
3788  C CD  . PRO C 49  ? 1.112 1.105 0.989 0.023  0.172  0.129  49  PRO AAA CD  
3789  N N   . GLN C 50  ? 1.192 1.235 1.107 0.031  0.173  0.136  50  GLN AAA N   
3790  C CA  . GLN C 50  ? 1.234 1.297 1.164 0.033  0.172  0.139  50  GLN AAA CA  
3791  C C   . GLN C 50  ? 1.192 1.271 1.129 0.027  0.165  0.132  50  GLN AAA C   
3792  O O   . GLN C 50  ? 1.270 1.366 1.214 0.025  0.162  0.134  50  GLN AAA O   
3793  C CB  . GLN C 50  ? 1.216 1.278 1.152 0.036  0.177  0.141  50  GLN AAA CB  
3794  C CG  . GLN C 50  ? 1.249 1.332 1.200 0.033  0.174  0.142  50  GLN AAA CG  
3795  C CD  . GLN C 50  ? 1.311 1.395 1.268 0.034  0.178  0.145  50  GLN AAA CD  
3796  O OE1 . GLN C 50  ? 1.320 1.396 1.274 0.040  0.185  0.150  50  GLN AAA OE1 
3797  N NE2 . GLN C 50  ? 1.377 1.469 1.343 0.027  0.173  0.141  50  GLN AAA NE2 
3798  N N   . ASP C 51  ? 1.161 1.234 1.097 0.023  0.162  0.125  51  ASP AAA N   
3799  C CA  . ASP C 51  ? 1.183 1.268 1.125 0.019  0.157  0.118  51  ASP AAA CA  
3800  C C   . ASP C 51  ? 1.193 1.288 1.132 0.017  0.153  0.116  51  ASP AAA C   
3801  O O   . ASP C 51  ? 1.163 1.275 1.108 0.015  0.150  0.112  51  ASP AAA O   
3802  C CB  . ASP C 51  ? 1.232 1.305 1.173 0.017  0.155  0.112  51  ASP AAA CB  
3803  C CG  . ASP C 51  ? 1.375 1.441 1.321 0.017  0.157  0.114  51  ASP AAA CG  
3804  O OD1 . ASP C 51  ? 1.533 1.608 1.486 0.017  0.158  0.118  51  ASP AAA OD1 
3805  O OD2 . ASP C 51  ? 1.330 1.382 1.271 0.017  0.157  0.113  51  ASP AAA OD2 
3806  N N   . LEU C 52  ? 1.139 1.226 1.069 0.018  0.154  0.118  52  LEU AAA N   
3807  C CA  . LEU C 52  ? 1.113 1.211 1.039 0.015  0.152  0.118  52  LEU AAA CA  
3808  C C   . LEU C 52  ? 1.118 1.230 1.048 0.016  0.152  0.124  52  LEU AAA C   
3809  O O   . LEU C 52  ? 1.225 1.356 1.159 0.013  0.148  0.122  52  LEU AAA O   
3810  C CB  . LEU C 52  ? 1.058 1.142 0.972 0.014  0.152  0.121  52  LEU AAA CB  
3811  C CG  . LEU C 52  ? 1.043 1.118 0.954 0.012  0.151  0.116  52  LEU AAA CG  
3812  C CD1 . LEU C 52  ? 1.070 1.129 0.968 0.010  0.152  0.120  52  LEU AAA CD1 
3813  C CD2 . LEU C 52  ? 1.071 1.162 0.987 0.011  0.147  0.109  52  LEU AAA CD2 
3814  N N   . ASN C 53  ? 1.111 1.216 1.041 0.020  0.156  0.132  53  ASN AAA N   
3815  C CA  . ASN C 53  ? 1.107 1.226 1.042 0.021  0.155  0.139  53  ASN AAA CA  
3816  C C   . ASN C 53  ? 1.083 1.222 1.030 0.019  0.152  0.136  53  ASN AAA C   
3817  O O   . ASN C 53  ? 1.084 1.243 1.035 0.017  0.149  0.138  53  ASN AAA O   
3818  C CB  . ASN C 53  ? 1.170 1.276 1.105 0.028  0.161  0.148  53  ASN AAA CB  
3819  C CG  . ASN C 53  ? 1.224 1.309 1.145 0.030  0.164  0.152  53  ASN AAA CG  
3820  O OD1 . ASN C 53  ? 1.214 1.301 1.129 0.026  0.160  0.153  53  ASN AAA OD1 
3821  N ND2 . ASN C 53  ? 1.335 1.400 1.251 0.036  0.170  0.155  53  ASN AAA ND2 
3822  N N   . THR C 54  ? 1.064 1.199 1.016 0.019  0.153  0.132  54  THR AAA N   
3823  C CA  . THR C 54  ? 1.100 1.252 1.062 0.014  0.149  0.127  54  THR AAA CA  
3824  C C   . THR C 54  ? 1.081 1.245 1.040 0.009  0.144  0.118  54  THR AAA C   
3825  O O   . THR C 54  ? 1.131 1.315 1.094 0.006  0.140  0.119  54  THR AAA O   
3826  C CB  . THR C 54  ? 1.142 1.284 1.108 0.014  0.150  0.123  54  THR AAA CB  
3827  O OG1 . THR C 54  ? 1.308 1.445 1.278 0.018  0.155  0.132  54  THR AAA OG1 
3828  C CG2 . THR C 54  ? 1.092 1.247 1.066 0.007  0.145  0.117  54  THR AAA CG2 
3829  N N   . MET C 55  ? 1.093 1.248 1.046 0.009  0.143  0.111  55  MET AAA N   
3830  C CA  . MET C 55  ? 1.091 1.258 1.042 0.006  0.140  0.102  55  MET AAA CA  
3831  C C   . MET C 55  ? 1.040 1.225 0.988 0.004  0.138  0.107  55  MET AAA C   
3832  O O   . MET C 55  ? 1.047 1.251 0.996 0.000  0.135  0.103  55  MET AAA O   
3833  C CB  . MET C 55  ? 1.064 1.220 1.010 0.007  0.140  0.096  55  MET AAA CB  
3834  C CG  . MET C 55  ? 1.137 1.278 1.086 0.009  0.140  0.090  55  MET AAA CG  
3835  S SD  . MET C 55  ? 1.206 1.335 1.150 0.011  0.141  0.086  55  MET AAA SD  
3836  C CE  . MET C 55  ? 1.124 1.272 1.069 0.011  0.138  0.074  55  MET AAA CE  
3837  N N   . LEU C 56  ? 1.026 1.205 0.969 0.006  0.141  0.117  56  LEU AAA N   
3838  C CA  . LEU C 56  ? 1.039 1.234 0.980 0.004  0.139  0.123  56  LEU AAA CA  
3839  C C   . LEU C 56  ? 1.099 1.309 1.046 0.003  0.137  0.130  56  LEU AAA C   
3840  O O   . LEU C 56  ? 1.149 1.380 1.096 -0.001 0.134  0.132  56  LEU AAA O   
3841  C CB  . LEU C 56  ? 1.017 1.197 0.951 0.006  0.142  0.132  56  LEU AAA CB  
3842  C CG  . LEU C 56  ? 0.990 1.158 0.916 0.005  0.142  0.127  56  LEU AAA CG  
3843  C CD1 . LEU C 56  ? 0.989 1.141 0.907 0.005  0.144  0.137  56  LEU AAA CD1 
3844  C CD2 . LEU C 56  ? 1.025 1.212 0.950 0.001  0.139  0.120  56  LEU AAA CD2 
3845  N N   . ASN C 57  ? 1.085 1.288 1.039 0.007  0.140  0.136  57  ASN AAA N   
3846  C CA  . ASN C 57  ? 1.073 1.293 1.036 0.007  0.138  0.145  57  ASN AAA CA  
3847  C C   . ASN C 57  ? 1.034 1.273 1.001 0.000  0.133  0.137  57  ASN AAA C   
3848  O O   . ASN C 57  ? 1.039 1.299 1.011 -0.003 0.130  0.144  57  ASN AAA O   
3849  C CB  . ASN C 57  ? 1.056 1.264 1.024 0.014  0.143  0.153  57  ASN AAA CB  
3850  C CG  . ASN C 57  ? 1.197 1.390 1.161 0.020  0.148  0.163  57  ASN AAA CG  
3851  O OD1 . ASN C 57  ? 1.210 1.398 1.164 0.019  0.147  0.163  57  ASN AAA OD1 
3852  N ND2 . ASN C 57  ? 1.400 1.584 1.368 0.028  0.153  0.170  57  ASN AAA ND2 
3853  N N   . THR C 58  ? 1.009 1.241 0.975 -0.002 0.132  0.124  58  THR AAA N   
3854  C CA  . THR C 58  ? 1.029 1.274 0.997 -0.009 0.127  0.116  58  THR AAA CA  
3855  C C   . THR C 58  ? 1.137 1.400 1.098 -0.014 0.124  0.110  58  THR AAA C   
3856  O O   . THR C 58  ? 1.204 1.481 1.164 -0.021 0.119  0.103  58  THR AAA O   
3857  C CB  . THR C 58  ? 1.069 1.298 1.037 -0.010 0.127  0.104  58  THR AAA CB  
3858  O OG1 . THR C 58  ? 1.131 1.347 1.092 -0.007 0.130  0.096  58  THR AAA OG1 
3859  C CG2 . THR C 58  ? 1.104 1.321 1.081 -0.008 0.130  0.111  58  THR AAA CG2 
3860  N N   . VAL C 59  ? 1.161 1.425 1.115 -0.012 0.125  0.112  59  VAL AAA N   
3861  C CA  . VAL C 59  ? 1.162 1.446 1.109 -0.017 0.123  0.109  59  VAL AAA CA  
3862  C C   . VAL C 59  ? 1.283 1.590 1.233 -0.020 0.119  0.120  59  VAL AAA C   
3863  O O   . VAL C 59  ? 1.337 1.642 1.291 -0.017 0.121  0.135  59  VAL AAA O   
3864  C CB  . VAL C 59  ? 1.096 1.377 1.037 -0.014 0.125  0.110  59  VAL AAA CB  
3865  C CG1 . VAL C 59  ? 1.237 1.542 1.170 -0.019 0.123  0.107  59  VAL AAA CG1 
3866  C CG2 . VAL C 59  ? 1.160 1.421 1.098 -0.010 0.128  0.099  59  VAL AAA CG2 
3867  N N   . GLY C 60  ? 1.486 1.813 1.434 -0.028 0.114  0.114  60  GLY AAA N   
3868  C CA  . GLY C 60  ? 1.552 1.903 1.503 -0.032 0.110  0.125  60  GLY AAA CA  
3869  C C   . GLY C 60  ? 1.587 1.957 1.531 -0.035 0.109  0.132  60  GLY AAA C   
3870  O O   . GLY C 60  ? 1.729 2.109 1.677 -0.034 0.107  0.148  60  GLY AAA O   
3871  N N   . GLY C 61  ? 1.343 1.717 1.276 -0.037 0.109  0.121  61  GLY AAA N   
3872  C CA  . GLY C 61  ? 1.406 1.801 1.332 -0.040 0.108  0.127  61  GLY AAA CA  
3873  C C   . GLY C 61  ? 1.323 1.705 1.248 -0.035 0.112  0.135  61  GLY AAA C   
3874  O O   . GLY C 61  ? 1.293 1.651 1.223 -0.029 0.115  0.138  61  GLY AAA O   
3875  N N   . HIS C 62  ? 1.319 1.718 1.236 -0.039 0.112  0.137  62  HIS AAA N   
3876  C CA  . HIS C 62  ? 1.280 1.669 1.193 -0.037 0.115  0.143  62  HIS AAA CA  
3877  C C   . HIS C 62  ? 1.275 1.643 1.194 -0.032 0.116  0.159  62  HIS AAA C   
3878  O O   . HIS C 62  ? 1.271 1.618 1.189 -0.029 0.119  0.160  62  HIS AAA O   
3879  C CB  . HIS C 62  ? 1.272 1.646 1.183 -0.033 0.119  0.128  62  HIS AAA CB  
3880  C CG  . HIS C 62  ? 1.239 1.629 1.145 -0.035 0.119  0.111  62  HIS AAA CG  
3881  N ND1 . HIS C 62  ? 1.341 1.756 1.238 -0.040 0.119  0.108  62  HIS AAA ND1 
3882  C CD2 . HIS C 62  ? 1.219 1.601 1.126 -0.033 0.120  0.095  62  HIS AAA CD2 
3883  C CE1 . HIS C 62  ? 1.369 1.792 1.262 -0.040 0.121  0.091  62  HIS AAA CE1 
3884  N NE2 . HIS C 62  ? 1.218 1.619 1.116 -0.036 0.121  0.082  62  HIS AAA NE2 
3885  N N   . GLN C 63  ? 1.252 1.628 1.177 -0.032 0.113  0.171  63  GLN AAA N   
3886  C CA  . GLN C 63  ? 1.294 1.649 1.224 -0.026 0.114  0.186  63  GLN AAA CA  
3887  C C   . GLN C 63  ? 1.303 1.651 1.227 -0.027 0.114  0.198  63  GLN AAA C   
3888  O O   . GLN C 63  ? 1.390 1.713 1.316 -0.021 0.117  0.206  63  GLN AAA O   
3889  C CB  . GLN C 63  ? 1.257 1.625 1.197 -0.025 0.111  0.196  63  GLN AAA CB  
3890  C CG  . GLN C 63  ? 1.236 1.603 1.183 -0.024 0.111  0.186  63  GLN AAA CG  
3891  C CD  . GLN C 63  ? 1.166 1.503 1.116 -0.016 0.117  0.181  63  GLN AAA CD  
3892  O OE1 . GLN C 63  ? 1.159 1.475 1.109 -0.010 0.120  0.189  63  GLN AAA OE1 
3893  N NE2 . GLN C 63  ? 1.260 1.594 1.213 -0.017 0.117  0.167  63  GLN AAA NE2 
3894  N N   . ALA C 64  ? 1.280 1.649 1.197 -0.034 0.112  0.200  64  ALA AAA N   
3895  C CA  . ALA C 64  ? 1.342 1.704 1.253 -0.037 0.112  0.210  64  ALA AAA CA  
3896  C C   . ALA C 64  ? 1.387 1.725 1.294 -0.035 0.116  0.202  64  ALA AAA C   
3897  O O   . ALA C 64  ? 1.401 1.714 1.306 -0.033 0.117  0.210  64  ALA AAA O   
3898  C CB  . ALA C 64  ? 1.339 1.734 1.243 -0.047 0.108  0.213  64  ALA AAA CB  
3899  N N   . ALA C 65  ? 1.328 1.672 1.234 -0.035 0.118  0.185  65  ALA AAA N   
3900  C CA  . ALA C 65  ? 1.301 1.624 1.204 -0.033 0.121  0.178  65  ALA AAA CA  
3901  C C   . ALA C 65  ? 1.319 1.610 1.226 -0.026 0.124  0.178  65  ALA AAA C   
3902  O O   . ALA C 65  ? 1.410 1.678 1.313 -0.025 0.125  0.182  65  ALA AAA O   
3903  C CB  . ALA C 65  ? 1.307 1.643 1.211 -0.033 0.123  0.160  65  ALA AAA CB  
3904  N N   . MET C 66  ? 1.246 1.536 1.161 -0.021 0.124  0.176  66  MET AAA N   
3905  C CA  . MET C 66  ? 1.227 1.489 1.146 -0.014 0.128  0.177  66  MET AAA CA  
3906  C C   . MET C 66  ? 1.319 1.562 1.235 -0.011 0.128  0.192  66  MET AAA C   
3907  O O   . MET C 66  ? 1.444 1.658 1.356 -0.007 0.132  0.192  66  MET AAA O   
3908  C CB  . MET C 66  ? 1.204 1.473 1.132 -0.010 0.127  0.173  66  MET AAA CB  
3909  C CG  . MET C 66  ? 1.235 1.520 1.164 -0.013 0.126  0.158  66  MET AAA CG  
3910  S SD  . MET C 66  ? 1.210 1.477 1.135 -0.012 0.129  0.143  66  MET AAA SD  
3911  C CE  . MET C 66  ? 1.287 1.522 1.216 -0.004 0.133  0.147  66  MET AAA CE  
3912  N N   . GLN C 67  ? 1.305 1.562 1.222 -0.013 0.125  0.204  67  GLN AAA N   
3913  C CA  . GLN C 67  ? 1.376 1.613 1.290 -0.010 0.125  0.219  67  GLN AAA CA  
3914  C C   . GLN C 67  ? 1.408 1.628 1.310 -0.016 0.125  0.221  67  GLN AAA C   
3915  O O   . GLN C 67  ? 1.452 1.641 1.348 -0.012 0.127  0.226  67  GLN AAA O   
3916  C CB  . GLN C 67  ? 1.318 1.575 1.235 -0.011 0.121  0.234  67  GLN AAA CB  
3917  C CG  . GLN C 67  ? 1.390 1.626 1.306 -0.006 0.122  0.250  67  GLN AAA CG  
3918  C CD  . GLN C 67  ? 1.513 1.734 1.438 0.006  0.126  0.254  67  GLN AAA CD  
3919  O OE1 . GLN C 67  ? 1.547 1.782 1.482 0.009  0.127  0.248  67  GLN AAA OE1 
3920  N NE2 . GLN C 67  ? 1.597 1.788 1.519 0.013  0.129  0.264  67  GLN AAA NE2 
3921  N N   . MET C 68  ? 1.363 1.603 1.261 -0.024 0.123  0.216  68  MET AAA N   
3922  C CA  . MET C 68  ? 1.438 1.667 1.326 -0.031 0.122  0.217  68  MET AAA CA  
3923  C C   . MET C 68  ? 1.427 1.630 1.313 -0.027 0.126  0.206  68  MET AAA C   
3924  O O   . MET C 68  ? 1.492 1.669 1.368 -0.030 0.126  0.210  68  MET AAA O   
3925  C CB  . MET C 68  ? 1.448 1.708 1.334 -0.040 0.120  0.213  68  MET AAA CB  
3926  C CG  . MET C 68  ? 1.437 1.721 1.322 -0.046 0.115  0.225  68  MET AAA CG  
3927  S SD  . MET C 68  ? 1.566 1.884 1.446 -0.057 0.114  0.222  68  MET AAA SD  
3928  C CE  . MET C 68  ? 1.595 1.940 1.482 -0.052 0.116  0.203  68  MET AAA CE  
3929  N N   . LEU C 69  ? 1.347 1.555 1.239 -0.023 0.128  0.193  69  LEU AAA N   
3930  C CA  . LEU C 69  ? 1.290 1.476 1.180 -0.019 0.131  0.184  69  LEU AAA CA  
3931  C C   . LEU C 69  ? 1.401 1.554 1.288 -0.013 0.134  0.190  69  LEU AAA C   
3932  O O   . LEU C 69  ? 1.498 1.626 1.376 -0.014 0.136  0.188  69  LEU AAA O   
3933  C CB  . LEU C 69  ? 1.243 1.441 1.142 -0.015 0.133  0.171  69  LEU AAA CB  
3934  C CG  . LEU C 69  ? 1.352 1.530 1.249 -0.012 0.136  0.162  69  LEU AAA CG  
3935  C CD1 . LEU C 69  ? 1.405 1.577 1.294 -0.018 0.135  0.161  69  LEU AAA CD1 
3936  C CD2 . LEU C 69  ? 1.310 1.501 1.216 -0.009 0.136  0.149  69  LEU AAA CD2 
3937  N N   . LYS C 70  ? 1.463 1.616 1.356 -0.007 0.136  0.197  70  LYS AAA N   
3938  C CA  . LYS C 70  ? 1.492 1.615 1.381 0.001  0.140  0.202  70  LYS AAA CA  
3939  C C   . LYS C 70  ? 1.525 1.623 1.401 -0.003 0.139  0.211  70  LYS AAA C   
3940  O O   . LYS C 70  ? 1.622 1.688 1.489 0.001  0.142  0.209  70  LYS AAA O   
3941  C CB  . LYS C 70  ? 1.510 1.643 1.410 0.009  0.141  0.211  70  LYS AAA CB  
3942  C CG  . LYS C 70  ? 1.542 1.699 1.455 0.012  0.141  0.204  70  LYS AAA CG  
3943  C CD  . LYS C 70  ? 1.726 1.872 1.640 0.014  0.145  0.191  70  LYS AAA CD  
3944  C CE  . LYS C 70  ? 1.566 1.737 1.492 0.014  0.143  0.184  70  LYS AAA CE  
3945  N NZ  . LYS C 70  ? 1.465 1.625 1.392 0.015  0.146  0.172  70  LYS AAA NZ  
3946  N N   . GLU C 71  ? 1.551 1.663 1.425 -0.010 0.134  0.220  71  GLU AAA N   
3947  C CA  . GLU C 71  ? 1.565 1.653 1.426 -0.016 0.132  0.228  71  GLU AAA CA  
3948  C C   . GLU C 71  ? 1.516 1.589 1.366 -0.023 0.131  0.220  71  GLU AAA C   
3949  O O   . GLU C 71  ? 1.609 1.649 1.446 -0.024 0.132  0.223  71  GLU AAA O   
3950  C CB  . GLU C 71  ? 1.647 1.759 1.508 -0.025 0.126  0.239  71  GLU AAA CB  
3951  C CG  . GLU C 71  ? 1.780 1.901 1.649 -0.019 0.125  0.252  71  GLU AAA CG  
3952  C CD  . GLU C 71  ? 2.158 2.296 2.024 -0.029 0.119  0.265  71  GLU AAA CD  
3953  O OE1 . GLU C 71  ? 2.154 2.310 2.015 -0.040 0.116  0.263  71  GLU AAA OE1 
3954  O OE2 . GLU C 71  ? 2.371 2.505 2.239 -0.025 0.117  0.279  71  GLU AAA OE2 
3955  N N   . THR C 72  ? 1.477 1.575 1.331 -0.028 0.130  0.211  72  THR AAA N   
3956  C CA  . THR C 72  ? 1.513 1.601 1.360 -0.035 0.129  0.205  72  THR AAA CA  
3957  C C   . THR C 72  ? 1.526 1.584 1.368 -0.028 0.134  0.197  72  THR AAA C   
3958  O O   . THR C 72  ? 1.625 1.657 1.454 -0.033 0.133  0.197  72  THR AAA O   
3959  C CB  . THR C 72  ? 1.457 1.578 1.312 -0.039 0.128  0.196  72  THR AAA CB  
3960  O OG1 . THR C 72  ? 1.558 1.706 1.414 -0.046 0.124  0.203  72  THR AAA OG1 
3961  C CG2 . THR C 72  ? 1.432 1.545 1.280 -0.045 0.127  0.191  72  THR AAA CG2 
3962  N N   . ILE C 73  ? 1.452 1.514 1.304 -0.018 0.138  0.191  73  ILE AAA N   
3963  C CA  . ILE C 73  ? 1.435 1.472 1.283 -0.011 0.143  0.185  73  ILE AAA CA  
3964  C C   . ILE C 73  ? 1.521 1.522 1.356 -0.008 0.145  0.192  73  ILE AAA C   
3965  O O   . ILE C 73  ? 1.644 1.617 1.466 -0.009 0.147  0.188  73  ILE AAA O   
3966  C CB  . ILE C 73  ? 1.394 1.445 1.256 -0.001 0.147  0.180  73  ILE AAA CB  
3967  C CG1 . ILE C 73  ? 1.349 1.426 1.220 -0.004 0.144  0.170  73  ILE AAA CG1 
3968  C CG2 . ILE C 73  ? 1.417 1.442 1.275 0.007  0.153  0.177  73  ILE AAA CG2 
3969  C CD1 . ILE C 73  ? 1.335 1.429 1.220 0.002  0.146  0.166  73  ILE AAA CD1 
3970  N N   . ASN C 74  ? 1.538 1.539 1.376 -0.004 0.146  0.202  74  ASN AAA N   
3971  C CA  . ASN C 74  ? 1.655 1.620 1.481 0.001  0.149  0.208  74  ASN AAA CA  
3972  C C   . ASN C 74  ? 1.690 1.631 1.498 -0.010 0.144  0.211  74  ASN AAA C   
3973  O O   . ASN C 74  ? 1.731 1.635 1.523 -0.009 0.147  0.209  74  ASN AAA O   
3974  C CB  . ASN C 74  ? 1.761 1.734 1.596 0.008  0.149  0.220  74  ASN AAA CB  
3975  C CG  . ASN C 74  ? 1.940 1.930 1.791 0.020  0.153  0.219  74  ASN AAA CG  
3976  O OD1 . ASN C 74  ? 2.037 2.024 1.890 0.026  0.158  0.210  74  ASN AAA OD1 
3977  N ND2 . ASN C 74  ? 1.947 1.958 1.809 0.024  0.151  0.229  74  ASN AAA ND2 
3978  N N   . GLU C 75  ? 1.805 1.767 1.614 -0.023 0.138  0.214  75  GLU AAA N   
3979  C CA  . GLU C 75  ? 1.877 1.822 1.669 -0.036 0.133  0.217  75  GLU AAA CA  
3980  C C   . GLU C 75  ? 1.869 1.800 1.652 -0.040 0.134  0.206  75  GLU AAA C   
3981  O O   . GLU C 75  ? 1.925 1.822 1.690 -0.046 0.133  0.207  75  GLU AAA O   
3982  C CB  . GLU C 75  ? 1.908 1.888 1.707 -0.048 0.126  0.222  75  GLU AAA CB  
3983  C CG  . GLU C 75  ? 2.067 2.043 1.854 -0.064 0.120  0.223  75  GLU AAA CG  
3984  C CD  . GLU C 75  ? 2.096 2.109 1.890 -0.074 0.115  0.231  75  GLU AAA CD  
3985  O OE1 . GLU C 75  ? 2.034 2.070 1.839 -0.070 0.115  0.235  75  GLU AAA OE1 
3986  O OE2 . GLU C 75  ? 2.174 2.192 1.962 -0.088 0.110  0.233  75  GLU AAA OE2 
3987  N N   . GLU C 76  ? 1.710 1.664 1.504 -0.037 0.135  0.197  76  GLU AAA N   
3988  C CA  . GLU C 76  ? 1.660 1.604 1.447 -0.040 0.136  0.188  76  GLU AAA CA  
3989  C C   . GLU C 76  ? 1.676 1.584 1.452 -0.032 0.142  0.183  76  GLU AAA C   
3990  O O   . GLU C 76  ? 1.734 1.620 1.495 -0.037 0.141  0.179  76  GLU AAA O   
3991  C CB  . GLU C 76  ? 1.575 1.552 1.378 -0.038 0.136  0.180  76  GLU AAA CB  
3992  C CG  . GLU C 76  ? 1.639 1.650 1.450 -0.047 0.130  0.183  76  GLU AAA CG  
3993  C CD  . GLU C 76  ? 1.825 1.831 1.624 -0.061 0.125  0.186  76  GLU AAA CD  
3994  O OE1 . GLU C 76  ? 1.927 1.913 1.716 -0.064 0.125  0.182  76  GLU AAA OE1 
3995  O OE2 . GLU C 76  ? 2.007 2.029 1.807 -0.070 0.120  0.194  76  GLU AAA OE2 
3996  N N   . ALA C 77  ? 1.627 1.534 1.411 -0.018 0.148  0.184  77  ALA AAA N   
3997  C CA  . ALA C 77  ? 1.643 1.518 1.417 -0.009 0.155  0.181  77  ALA AAA CA  
3998  C C   . ALA C 77  ? 1.760 1.594 1.511 -0.013 0.155  0.184  77  ALA AAA C   
3999  O O   . ALA C 77  ? 1.865 1.671 1.600 -0.012 0.158  0.178  77  ALA AAA O   
4000  C CB  . ALA C 77  ? 1.644 1.529 1.433 0.006  0.161  0.183  77  ALA AAA CB  
4001  N N   . ALA C 78  ? 1.769 1.599 1.519 -0.017 0.151  0.194  78  ALA AAA N   
4002  C CA  . ALA C 78  ? 1.905 1.693 1.633 -0.021 0.150  0.197  78  ALA AAA CA  
4003  C C   . ALA C 78  ? 1.957 1.731 1.666 -0.037 0.145  0.193  78  ALA AAA C   
4004  O O   . ALA C 78  ? 2.056 1.790 1.742 -0.039 0.147  0.188  78  ALA AAA O   
4005  C CB  . ALA C 78  ? 2.003 1.792 1.733 -0.024 0.146  0.210  78  ALA AAA CB  
4006  N N   . GLU C 79  ? 1.967 1.772 1.684 -0.049 0.138  0.193  79  GLU AAA N   
4007  C CA  . GLU C 79  ? 2.057 1.854 1.759 -0.065 0.132  0.190  79  GLU AAA CA  
4008  C C   . GLU C 79  ? 2.004 1.790 1.699 -0.062 0.136  0.179  79  GLU AAA C   
4009  O O   . GLU C 79  ? 2.068 1.827 1.742 -0.072 0.134  0.176  79  GLU AAA O   
4010  C CB  . GLU C 79  ? 2.123 1.963 1.840 -0.076 0.125  0.194  79  GLU AAA CB  
4011  C CG  . GLU C 79  ? 2.193 2.033 1.898 -0.094 0.117  0.193  79  GLU AAA CG  
4012  C CD  . GLU C 79  ? 2.293 2.099 1.975 -0.108 0.112  0.200  79  GLU AAA CD  
4013  O OE1 . GLU C 79  ? 2.307 2.077 1.976 -0.104 0.114  0.202  79  GLU AAA OE1 
4014  O OE2 . GLU C 79  ? 2.387 2.202 2.063 -0.125 0.104  0.203  79  GLU AAA OE2 
4015  N N   . TRP C 80  ? 1.846 1.652 1.558 -0.049 0.142  0.174  80  TRP AAA N   
4016  C CA  . TRP C 80  ? 1.838 1.631 1.542 -0.045 0.147  0.165  80  TRP AAA CA  
4017  C C   . TRP C 80  ? 1.871 1.619 1.552 -0.040 0.153  0.162  80  TRP AAA C   
4018  O O   . TRP C 80  ? 1.992 1.717 1.653 -0.046 0.152  0.156  80  TRP AAA O   
4019  C CB  . TRP C 80  ? 1.779 1.599 1.504 -0.031 0.152  0.161  80  TRP AAA CB  
4020  C CG  . TRP C 80  ? 1.681 1.489 1.399 -0.027 0.157  0.153  80  TRP AAA CG  
4021  C CD1 . TRP C 80  ? 1.707 1.493 1.419 -0.015 0.166  0.149  80  TRP AAA CD1 
4022  C CD2 . TRP C 80  ? 1.658 1.473 1.373 -0.034 0.154  0.148  80  TRP AAA CD2 
4023  N NE1 . TRP C 80  ? 1.740 1.521 1.445 -0.015 0.169  0.143  80  TRP AAA NE1 
4024  C CE2 . TRP C 80  ? 1.718 1.516 1.425 -0.026 0.161  0.142  80  TRP AAA CE2 
4025  C CE3 . TRP C 80  ? 1.674 1.512 1.395 -0.045 0.146  0.148  80  TRP AAA CE3 
4026  C CZ2 . TRP C 80  ? 1.723 1.524 1.426 -0.031 0.160  0.137  80  TRP AAA CZ2 
4027  C CZ3 . TRP C 80  ? 1.736 1.576 1.453 -0.049 0.145  0.144  80  TRP AAA CZ3 
4028  C CH2 . TRP C 80  ? 1.696 1.518 1.405 -0.042 0.151  0.138  80  TRP AAA CH2 
4029  N N   . ASP C 81  ? 1.825 1.561 1.509 -0.028 0.158  0.165  81  ASP AAA N   
4030  C CA  . ASP C 81  ? 1.869 1.561 1.532 -0.020 0.165  0.162  81  ASP AAA CA  
4031  C C   . ASP C 81  ? 1.945 1.600 1.580 -0.035 0.160  0.162  81  ASP AAA C   
4032  O O   . ASP C 81  ? 2.059 1.678 1.670 -0.035 0.163  0.155  81  ASP AAA O   
4033  C CB  . ASP C 81  ? 1.861 1.549 1.535 -0.004 0.172  0.168  81  ASP AAA CB  
4034  C CG  . ASP C 81  ? 1.840 1.560 1.538 0.011  0.179  0.167  81  ASP AAA CG  
4035  O OD1 . ASP C 81  ? 1.895 1.628 1.596 0.011  0.180  0.160  81  ASP AAA OD1 
4036  O OD2 . ASP C 81  ? 1.763 1.494 1.476 0.022  0.181  0.174  81  ASP AAA OD2 
4037  N N   . ARG C 82  ? 1.866 1.529 1.503 -0.047 0.151  0.171  82  ARG AAA N   
4038  C CA  . ARG C 82  ? 1.949 1.579 1.561 -0.064 0.144  0.172  82  ARG AAA CA  
4039  C C   . ARG C 82  ? 2.013 1.641 1.610 -0.080 0.138  0.166  82  ARG AAA C   
4040  O O   . ARG C 82  ? 2.173 1.762 1.742 -0.088 0.137  0.161  82  ARG AAA O   
4041  C CB  . ARG C 82  ? 2.062 1.709 1.683 -0.075 0.135  0.185  82  ARG AAA CB  
4042  C CG  . ARG C 82  ? 2.245 1.852 1.840 -0.090 0.128  0.189  82  ARG AAA CG  
4043  C CD  . ARG C 82  ? 2.297 1.926 1.902 -0.103 0.119  0.202  82  ARG AAA CD  
4044  N NE  . ARG C 82  ? 2.277 1.949 1.894 -0.116 0.112  0.204  82  ARG AAA NE  
4045  C CZ  . ARG C 82  ? 2.351 2.019 1.954 -0.135 0.105  0.202  82  ARG AAA CZ  
4046  N NH1 . ARG C 82  ? 2.439 2.061 2.013 -0.144 0.102  0.199  82  ARG AAA NH1 
4047  N NH2 . ARG C 82  ? 2.340 2.053 1.959 -0.144 0.099  0.204  82  ARG AAA NH2 
4048  N N   . LEU C 83  ? 1.937 1.606 1.551 -0.083 0.135  0.165  83  LEU AAA N   
4049  C CA  . LEU C 83  ? 1.998 1.668 1.600 -0.097 0.130  0.160  83  LEU AAA CA  
4050  C C   . LEU C 83  ? 2.009 1.667 1.602 -0.089 0.137  0.150  83  LEU AAA C   
4051  O O   . LEU C 83  ? 2.116 1.763 1.692 -0.100 0.133  0.145  83  LEU AAA O   
4052  C CB  A LEU C 83  ? 1.961 1.679 1.585 -0.105 0.122  0.165  83  LEU AAA CB  
4053  C CG  A LEU C 83  ? 2.143 1.871 1.771 -0.117 0.115  0.175  83  LEU AAA CG  
4054  C CD1 A LEU C 83  ? 2.110 1.889 1.762 -0.121 0.110  0.180  83  LEU AAA CD1 
4055  C CD2 A LEU C 83  ? 2.255 1.949 1.854 -0.137 0.107  0.178  83  LEU AAA CD2 
4056  N N   . HIS C 84  ? 1.983 1.647 1.590 -0.070 0.147  0.146  84  HIS AAA N   
4057  C CA  . HIS C 84  ? 1.991 1.647 1.592 -0.060 0.155  0.138  84  HIS AAA CA  
4058  C C   . HIS C 84  ? 2.010 1.646 1.610 -0.042 0.166  0.136  84  HIS AAA C   
4059  O O   . HIS C 84  ? 1.989 1.647 1.611 -0.027 0.172  0.137  84  HIS AAA O   
4060  C CB  . HIS C 84  ? 1.888 1.585 1.513 -0.056 0.154  0.137  84  HIS AAA CB  
4061  C CG  . HIS C 84  ? 1.880 1.603 1.510 -0.072 0.144  0.140  84  HIS AAA CG  
4062  N ND1 . HIS C 84  ? 1.893 1.648 1.544 -0.076 0.138  0.146  84  HIS AAA ND1 
4063  C CD2 . HIS C 84  ? 1.983 1.705 1.602 -0.084 0.138  0.137  84  HIS AAA CD2 
4064  C CE1 . HIS C 84  ? 1.978 1.752 1.631 -0.089 0.130  0.148  84  HIS AAA CE1 
4065  N NE2 . HIS C 84  ? 2.091 1.845 1.724 -0.094 0.129  0.143  84  HIS AAA NE2 
4066  N N   . PRO C 85  ? 2.021 1.613 1.596 -0.042 0.169  0.134  85  PRO AAA N   
4067  C CA  . PRO C 85  ? 2.070 1.640 1.643 -0.023 0.180  0.133  85  PRO AAA CA  
4068  C C   . PRO C 85  ? 2.174 1.744 1.744 -0.012 0.190  0.124  85  PRO AAA C   
4069  O O   . PRO C 85  ? 2.141 1.710 1.698 -0.022 0.188  0.118  85  PRO AAA O   
4070  C CB  . PRO C 85  ? 2.140 1.661 1.684 -0.028 0.180  0.131  85  PRO AAA CB  
4071  C CG  . PRO C 85  ? 2.164 1.684 1.698 -0.052 0.166  0.135  85  PRO AAA CG  
4072  C CD  . PRO C 85  ? 2.096 1.654 1.642 -0.060 0.161  0.133  85  PRO AAA CD  
4073  N N   . VAL C 86  ? 2.380 1.949 1.960 0.008  0.201  0.124  86  VAL AAA N   
4074  C CA  . VAL C 86  ? 2.414 1.987 1.993 0.019  0.212  0.117  86  VAL AAA CA  
4075  C C   . VAL C 86  ? 2.474 1.999 2.019 0.023  0.220  0.108  86  VAL AAA C   
4076  O O   . VAL C 86  ? 2.551 2.043 2.083 0.030  0.224  0.108  86  VAL AAA O   
4077  C CB  . VAL C 86  ? 2.398 1.996 2.005 0.039  0.220  0.123  86  VAL AAA CB  
4078  C CG1 . VAL C 86  ? 2.353 1.954 1.959 0.051  0.232  0.117  86  VAL AAA CG1 
4079  C CG2 . VAL C 86  ? 2.336 1.980 1.974 0.034  0.212  0.130  86  VAL AAA CG2 
4080  N N   . HIS C 87  ? 2.392 1.914 1.922 0.017  0.221  0.100  87  HIS AAA N   
4081  C CA  . HIS C 87  ? 2.404 1.884 1.899 0.019  0.229  0.090  87  HIS AAA CA  
4082  C C   . HIS C 87  ? 2.375 1.854 1.876 0.043  0.245  0.088  87  HIS AAA C   
4083  O O   . HIS C 87  ? 2.334 1.848 1.856 0.050  0.250  0.090  87  HIS AAA O   
4084  C CB  . HIS C 87  ? 2.496 1.976 1.972 0.004  0.225  0.083  87  HIS AAA CB  
4085  C CG  . HIS C 87  ? 2.544 2.025 2.012 -0.020 0.209  0.086  87  HIS AAA CG  
4086  N ND1 . HIS C 87  ? 2.695 2.135 2.128 -0.035 0.204  0.080  87  HIS AAA ND1 
4087  C CD2 . HIS C 87  ? 2.612 2.130 2.103 -0.031 0.198  0.093  87  HIS AAA CD2 
4088  C CE1 . HIS C 87  ? 2.799 2.254 2.235 -0.054 0.190  0.085  87  HIS AAA CE1 
4089  N NE2 . HIS C 87  ? 2.790 2.292 2.261 -0.052 0.186  0.093  87  HIS AAA NE2 
4090  N N   . ALA C 88  ? 2.379 1.821 1.864 0.055  0.254  0.085  88  ALA AAA N   
4091  C CA  . ALA C 88  ? 2.370 1.815 1.865 0.080  0.270  0.085  88  ALA AAA CA  
4092  C C   . ALA C 88  ? 2.484 1.908 1.953 0.085  0.281  0.073  88  ALA AAA C   
4093  O O   . ALA C 88  ? 2.609 1.997 2.042 0.074  0.280  0.063  88  ALA AAA O   
4094  C CB  . ALA C 88  ? 2.408 1.826 1.903 0.093  0.274  0.089  88  ALA AAA CB  
4095  N N   . GLY C 89  ? 2.426 1.875 1.911 0.102  0.293  0.074  89  GLY AAA N   
4096  C CA  . GLY C 89  ? 2.360 1.794 1.822 0.111  0.307  0.064  89  GLY AAA CA  
4097  C C   . GLY C 89  ? 2.288 1.766 1.778 0.124  0.316  0.069  89  GLY AAA C   
4098  O O   . GLY C 89  ? 2.315 1.834 1.840 0.123  0.310  0.080  89  GLY AAA O   
4099  N N   . PRO C 90  ? 2.316 1.784 1.789 0.135  0.331  0.062  90  PRO AAA N   
4100  C CA  . PRO C 90  ? 2.286 1.796 1.782 0.145  0.339  0.067  90  PRO AAA CA  
4101  C C   . PRO C 90  ? 2.269 1.810 1.774 0.126  0.328  0.069  90  PRO AAA C   
4102  O O   . PRO C 90  ? 2.321 1.844 1.800 0.109  0.321  0.062  90  PRO AAA O   
4103  C CB  . PRO C 90  ? 2.415 1.902 1.885 0.159  0.357  0.056  90  PRO AAA CB  
4104  C CG  . PRO C 90  ? 2.537 1.969 1.962 0.149  0.354  0.044  90  PRO AAA CG  
4105  C CD  . PRO C 90  ? 2.446 1.864 1.878 0.141  0.341  0.048  90  PRO AAA CD  
4106  N N   . ILE C 91  ? 2.248 1.834 1.787 0.129  0.327  0.079  91  ILE AAA N   
4107  C CA  . ILE C 91  ? 2.235 1.852 1.787 0.113  0.317  0.082  91  ILE AAA CA  
4108  C C   . ILE C 91  ? 2.331 1.955 1.870 0.113  0.326  0.079  91  ILE AAA C   
4109  O O   . ILE C 91  ? 2.413 2.049 1.959 0.129  0.340  0.080  91  ILE AAA O   
4110  C CB  . ILE C 91  ? 2.232 1.890 1.826 0.113  0.310  0.094  91  ILE AAA CB  
4111  C CG1 . ILE C 91  ? 2.121 1.795 1.721 0.093  0.294  0.096  91  ILE AAA CG1 
4112  C CG2 . ILE C 91  ? 2.313 2.005 1.931 0.127  0.320  0.101  91  ILE AAA CG2 
4113  C CD1 . ILE C 91  ? 2.124 1.772 1.706 0.079  0.282  0.092  91  ILE AAA CD1 
4114  N N   . ALA C 92  ? 2.387 2.005 1.907 0.096  0.318  0.074  92  ALA AAA N   
4115  C CA  . ALA C 92  ? 2.479 2.106 1.987 0.092  0.323  0.072  92  ALA AAA CA  
4116  C C   . ALA C 92  ? 2.495 2.168 2.036 0.092  0.322  0.082  92  ALA AAA C   
4117  O O   . ALA C 92  ? 2.548 2.243 2.115 0.085  0.310  0.090  92  ALA AAA O   
4118  C CB  . ALA C 92  ? 2.495 2.104 1.975 0.071  0.312  0.066  92  ALA AAA CB  
4119  N N   . PRO C 93  ? 2.544 2.231 2.083 0.101  0.335  0.083  93  PRO AAA N   
4120  C CA  . PRO C 93  ? 2.521 2.250 2.091 0.100  0.334  0.094  93  PRO AAA CA  
4121  C C   . PRO C 93  ? 2.463 2.205 2.040 0.081  0.318  0.098  93  PRO AAA C   
4122  O O   . PRO C 93  ? 2.497 2.225 2.050 0.068  0.312  0.094  93  PRO AAA O   
4123  C CB  . PRO C 93  ? 2.605 2.338 2.159 0.108  0.350  0.092  93  PRO AAA CB  
4124  C CG  . PRO C 93  ? 2.677 2.369 2.188 0.106  0.355  0.079  93  PRO AAA CG  
4125  C CD  . PRO C 93  ? 2.645 2.308 2.151 0.109  0.350  0.074  93  PRO AAA CD  
4126  N N   . GLY C 94  ? 2.324 2.093 1.936 0.080  0.310  0.107  94  GLY AAA N   
4127  C CA  . GLY C 94  ? 2.260 2.047 1.889 0.065  0.295  0.112  94  GLY AAA CA  
4128  C C   . GLY C 94  ? 2.235 2.005 1.858 0.055  0.281  0.109  94  GLY AAA C   
4129  O O   . GLY C 94  ? 2.245 2.026 1.876 0.042  0.269  0.112  94  GLY AAA O   
4130  N N   . GLN C 95  ? 2.193 1.938 1.802 0.060  0.283  0.103  95  GLN AAA N   
4131  C CA  . GLN C 95  ? 2.116 1.848 1.722 0.049  0.270  0.101  95  GLN AAA CA  
4132  C C   . GLN C 95  ? 2.073 1.818 1.706 0.056  0.268  0.106  95  GLN AAA C   
4133  O O   . GLN C 95  ? 2.106 1.856 1.750 0.071  0.278  0.108  95  GLN AAA O   
4134  C CB  . GLN C 95  ? 2.168 1.861 1.739 0.046  0.272  0.092  95  GLN AAA CB  
4135  C CG  . GLN C 95  ? 2.253 1.928 1.790 0.038  0.275  0.086  95  GLN AAA CG  
4136  C CD  . GLN C 95  ? 2.262 1.952 1.801 0.022  0.262  0.089  95  GLN AAA CD  
4137  O OE1 . GLN C 95  ? 2.203 1.901 1.755 0.012  0.249  0.093  95  GLN AAA OE1 
4138  N NE2 . GLN C 95  ? 2.405 2.099 1.931 0.018  0.266  0.089  95  GLN AAA NE2 
4139  N N   . MET C 96  ? 2.051 1.804 1.696 0.047  0.255  0.108  96  MET AAA N   
4140  C CA  . MET C 96  ? 1.951 1.716 1.619 0.051  0.251  0.112  96  MET AAA CA  
4141  C C   . MET C 96  ? 1.920 1.658 1.574 0.054  0.251  0.109  96  MET AAA C   
4142  O O   . MET C 96  ? 2.010 1.719 1.635 0.048  0.251  0.103  96  MET AAA O   
4143  C CB  . MET C 96  ? 1.915 1.703 1.603 0.040  0.238  0.116  96  MET AAA CB  
4144  C CG  . MET C 96  ? 1.888 1.692 1.599 0.043  0.233  0.120  96  MET AAA CG  
4145  S SD  . MET C 96  ? 1.953 1.791 1.693 0.038  0.225  0.125  96  MET AAA SD  
4146  C CE  . MET C 96  ? 1.848 1.678 1.570 0.025  0.218  0.122  96  MET AAA CE  
4147  N N   . ARG C 97  ? 1.745 1.493 1.418 0.063  0.253  0.114  97  ARG AAA N   
4148  C CA  . ARG C 97  ? 1.771 1.493 1.432 0.065  0.252  0.112  97  ARG AAA CA  
4149  C C   . ARG C 97  ? 1.783 1.509 1.447 0.050  0.238  0.114  97  ARG AAA C   
4150  O O   . ARG C 97  ? 1.790 1.540 1.469 0.042  0.229  0.116  97  ARG AAA O   
4151  C CB  . ARG C 97  ? 1.784 1.514 1.463 0.080  0.258  0.118  97  ARG AAA CB  
4152  C CG  . ARG C 97  ? 1.778 1.542 1.489 0.080  0.251  0.126  97  ARG AAA CG  
4153  C CD  . ARG C 97  ? 1.834 1.609 1.562 0.097  0.260  0.132  97  ARG AAA CD  
4154  N NE  . ARG C 97  ? 1.828 1.637 1.586 0.096  0.253  0.140  97  ARG AAA NE  
4155  C CZ  . ARG C 97  ? 1.808 1.619 1.572 0.092  0.245  0.143  97  ARG AAA CZ  
4156  N NH1 . ARG C 97  ? 1.806 1.589 1.551 0.087  0.242  0.141  97  ARG AAA NH1 
4157  N NH2 . ARG C 97  ? 1.715 1.558 1.504 0.091  0.240  0.149  97  ARG AAA NH2 
4158  N N   . GLU C 98  ? 1.874 1.574 1.522 0.047  0.235  0.113  98  GLU AAA N   
4159  C CA  . GLU C 98  ? 1.896 1.600 1.547 0.033  0.222  0.115  98  GLU AAA CA  
4160  C C   . GLU C 98  ? 1.840 1.569 1.518 0.038  0.218  0.122  98  GLU AAA C   
4161  O O   . GLU C 98  ? 1.885 1.609 1.569 0.050  0.224  0.125  98  GLU AAA O   
4162  C CB  . GLU C 98  ? 2.015 1.682 1.637 0.025  0.219  0.111  98  GLU AAA CB  
4163  C CG  . GLU C 98  ? 2.129 1.778 1.724 0.012  0.215  0.105  98  GLU AAA CG  
4164  C CD  . GLU C 98  ? 2.330 1.934 1.890 0.011  0.220  0.098  98  GLU AAA CD  
4165  O OE1 . GLU C 98  ? 2.381 1.968 1.934 0.025  0.232  0.094  98  GLU AAA OE1 
4166  O OE2 . GLU C 98  ? 2.396 1.981 1.937 -0.005 0.211  0.096  98  GLU AAA OE2 
4167  N N   . PRO C 99  ? 1.766 1.522 1.461 0.029  0.208  0.125  99  PRO AAA N   
4168  C CA  . PRO C 99  ? 1.621 1.401 1.341 0.032  0.205  0.131  99  PRO AAA CA  
4169  C C   . PRO C 99  ? 1.674 1.440 1.386 0.029  0.201  0.135  99  PRO AAA C   
4170  O O   . PRO C 99  ? 1.719 1.471 1.416 0.016  0.194  0.133  99  PRO AAA O   
4171  C CB  . PRO C 99  ? 1.575 1.385 1.310 0.023  0.196  0.131  99  PRO AAA CB  
4172  C CG  . PRO C 99  ? 1.673 1.471 1.392 0.014  0.195  0.126  99  PRO AAA CG  
4173  C CD  . PRO C 99  ? 1.777 1.539 1.467 0.014  0.199  0.123  99  PRO AAA CD  
4174  N N   . ARG C 100 ? 1.665 1.437 1.390 0.039  0.204  0.141  100 ARG AAA N   
4175  C CA  . ARG C 100 ? 1.661 1.426 1.385 0.036  0.199  0.146  100 ARG AAA CA  
4176  C C   . ARG C 100 ? 1.602 1.402 1.347 0.029  0.191  0.151  100 ARG AAA C   
4177  O O   . ARG C 100 ? 1.613 1.440 1.374 0.028  0.189  0.149  100 ARG AAA O   
4178  C CB  . ARG C 100 ? 1.729 1.483 1.456 0.051  0.207  0.151  100 ARG AAA CB  
4179  C CG  . ARG C 100 ? 1.863 1.587 1.573 0.062  0.218  0.146  100 ARG AAA CG  
4180  C CD  . ARG C 100 ? 1.961 1.677 1.677 0.079  0.226  0.152  100 ARG AAA CD  
4181  N NE  . ARG C 100 ? 2.214 1.912 1.924 0.076  0.221  0.158  100 ARG AAA NE  
4182  C CZ  . ARG C 100 ? 2.386 2.044 2.075 0.081  0.226  0.158  100 ARG AAA CZ  
4183  N NH1 . ARG C 100 ? 2.446 2.077 2.118 0.091  0.236  0.151  100 ARG AAA NH1 
4184  N NH2 . ARG C 100 ? 2.375 2.018 2.060 0.077  0.220  0.165  100 ARG AAA NH2 
4185  N N   . GLY C 101 ? 1.584 1.381 1.327 0.024  0.185  0.157  101 GLY AAA N   
4186  C CA  . GLY C 101 ? 1.558 1.389 1.319 0.018  0.178  0.161  101 GLY AAA CA  
4187  C C   . GLY C 101 ? 1.510 1.371 1.296 0.028  0.181  0.164  101 GLY AAA C   
4188  O O   . GLY C 101 ? 1.420 1.310 1.220 0.025  0.177  0.161  101 GLY AAA O   
4189  N N   . SER C 102 ? 1.522 1.376 1.312 0.041  0.188  0.168  102 SER AAA N   
4190  C CA  . SER C 102 ? 1.536 1.418 1.348 0.051  0.191  0.171  102 SER AAA CA  
4191  C C   . SER C 102 ? 1.495 1.389 1.314 0.053  0.194  0.165  102 SER AAA C   
4192  O O   . SER C 102 ? 1.479 1.402 1.318 0.055  0.194  0.166  102 SER AAA O   
4193  C CB  . SER C 102 ? 1.521 1.390 1.334 0.065  0.198  0.178  102 SER AAA CB  
4194  O OG  . SER C 102 ? 1.595 1.434 1.393 0.072  0.206  0.174  102 SER AAA OG  
4195  N N   . ASP C 103 ? 1.493 1.366 1.297 0.052  0.198  0.158  103 ASP AAA N   
4196  C CA  . ASP C 103 ? 1.433 1.318 1.243 0.052  0.200  0.153  103 ASP AAA CA  
4197  C C   . ASP C 103 ? 1.391 1.297 1.210 0.041  0.192  0.149  103 ASP AAA C   
4198  O O   . ASP C 103 ? 1.425 1.352 1.258 0.042  0.191  0.148  103 ASP AAA O   
4199  C CB  . ASP C 103 ? 1.445 1.301 1.234 0.053  0.206  0.147  103 ASP AAA CB  
4200  C CG  . ASP C 103 ? 1.505 1.342 1.288 0.067  0.217  0.150  103 ASP AAA CG  
4201  O OD1 . ASP C 103 ? 1.461 1.316 1.261 0.077  0.222  0.155  103 ASP AAA OD1 
4202  O OD2 . ASP C 103 ? 1.575 1.379 1.335 0.067  0.220  0.147  103 ASP AAA OD2 
4203  N N   . ILE C 104 ? 1.365 1.265 1.174 0.031  0.185  0.148  104 ILE AAA N   
4204  C CA  . ILE C 104 ? 1.291 1.212 1.108 0.022  0.177  0.145  104 ILE AAA CA  
4205  C C   . ILE C 104 ? 1.227 1.177 1.064 0.024  0.174  0.147  104 ILE AAA C   
4206  O O   . ILE C 104 ? 1.156 1.127 1.005 0.022  0.171  0.144  104 ILE AAA O   
4207  C CB  . ILE C 104 ? 1.341 1.250 1.143 0.011  0.171  0.145  104 ILE AAA CB  
4208  C CG1 . ILE C 104 ? 1.437 1.319 1.219 0.007  0.173  0.141  104 ILE AAA CG1 
4209  C CG2 . ILE C 104 ? 1.321 1.257 1.135 0.003  0.164  0.143  104 ILE AAA CG2 
4210  C CD1 . ILE C 104 ? 1.523 1.401 1.293 -0.006 0.165  0.141  104 ILE AAA CD1 
4211  N N   . ALA C 105 ? 1.261 1.215 1.101 0.027  0.175  0.154  105 ALA AAA N   
4212  C CA  . ALA C 105 ? 1.282 1.264 1.139 0.028  0.172  0.157  105 ALA AAA CA  
4213  C C   . ALA C 105 ? 1.280 1.277 1.153 0.036  0.176  0.157  105 ALA AAA C   
4214  O O   . ALA C 105 ? 1.305 1.326 1.191 0.036  0.173  0.160  105 ALA AAA O   
4215  C CB  . ALA C 105 ? 1.360 1.341 1.216 0.029  0.170  0.165  105 ALA AAA CB  
4216  N N   . GLY C 106 ? 1.289 1.272 1.159 0.042  0.182  0.156  106 GLY AAA N   
4217  C CA  . GLY C 106 ? 1.330 1.328 1.214 0.048  0.186  0.157  106 GLY AAA CA  
4218  C C   . GLY C 106 ? 1.342 1.349 1.236 0.057  0.190  0.165  106 GLY AAA C   
4219  O O   . GLY C 106 ? 1.430 1.456 1.338 0.060  0.191  0.168  106 GLY AAA O   
4220  N N   . THR C 107 ? 1.288 1.279 1.172 0.061  0.191  0.171  107 THR AAA N   
4221  C CA  . THR C 107 ? 1.317 1.315 1.211 0.070  0.195  0.181  107 THR AAA CA  
4222  C C   . THR C 107 ? 1.400 1.381 1.290 0.083  0.205  0.183  107 THR AAA C   
4223  O O   . THR C 107 ? 1.488 1.485 1.392 0.092  0.210  0.190  107 THR AAA O   
4224  C CB  . THR C 107 ? 1.371 1.359 1.257 0.069  0.191  0.187  107 THR AAA CB  
4225  O OG1 . THR C 107 ? 1.444 1.396 1.308 0.068  0.194  0.184  107 THR AAA OG1 
4226  C CG2 . THR C 107 ? 1.350 1.357 1.239 0.057  0.182  0.185  107 THR AAA CG2 
4227  N N   . THR C 108 ? 1.423 1.374 1.294 0.083  0.209  0.177  108 THR AAA N   
4228  C CA  . THR C 108 ? 1.456 1.388 1.319 0.094  0.220  0.177  108 THR AAA CA  
4229  C C   . THR C 108 ? 1.467 1.394 1.323 0.092  0.224  0.169  108 THR AAA C   
4230  O O   . THR C 108 ? 1.547 1.455 1.392 0.100  0.233  0.168  108 THR AAA O   
4231  C CB  . THR C 108 ? 1.493 1.388 1.335 0.098  0.223  0.177  108 THR AAA CB  
4232  O OG1 . THR C 108 ? 1.524 1.403 1.349 0.084  0.217  0.170  108 THR AAA OG1 
4233  C CG2 . THR C 108 ? 1.567 1.466 1.416 0.102  0.221  0.187  108 THR AAA CG2 
4234  N N   . SER C 109 ? 1.356 1.298 1.218 0.081  0.217  0.164  109 SER AAA N   
4235  C CA  . SER C 109 ? 1.405 1.343 1.261 0.078  0.220  0.158  109 SER AAA CA  
4236  C C   . SER C 109 ? 1.418 1.386 1.295 0.078  0.219  0.160  109 SER AAA C   
4237  O O   . SER C 109 ? 1.424 1.416 1.319 0.076  0.214  0.164  109 SER AAA O   
4238  C CB  . SER C 109 ? 1.408 1.337 1.253 0.065  0.212  0.151  109 SER AAA CB  
4239  O OG  . SER C 109 ? 1.326 1.277 1.185 0.058  0.203  0.151  109 SER AAA OG  
4240  N N   . THR C 110 ? 1.406 1.372 1.282 0.080  0.225  0.159  110 THR AAA N   
4241  C CA  . THR C 110 ? 1.378 1.369 1.271 0.078  0.225  0.161  110 THR AAA CA  
4242  C C   . THR C 110 ? 1.331 1.323 1.223 0.066  0.216  0.155  110 THR AAA C   
4243  O O   . THR C 110 ? 1.412 1.386 1.289 0.060  0.214  0.149  110 THR AAA O   
4244  C CB  . THR C 110 ? 1.520 1.510 1.412 0.086  0.235  0.164  110 THR AAA CB  
4245  O OG1 . THR C 110 ? 1.692 1.674 1.581 0.099  0.244  0.168  110 THR AAA OG1 
4246  C CG2 . THR C 110 ? 1.543 1.562 1.456 0.084  0.235  0.169  110 THR AAA CG2 
4247  N N   . LEU C 111 ? 1.245 1.259 1.154 0.061  0.212  0.156  111 LEU AAA N   
4248  C CA  . LEU C 111 ? 1.305 1.318 1.215 0.051  0.205  0.150  111 LEU AAA CA  
4249  C C   . LEU C 111 ? 1.484 1.479 1.378 0.050  0.209  0.148  111 LEU AAA C   
4250  O O   . LEU C 111 ? 1.540 1.523 1.424 0.044  0.204  0.143  111 LEU AAA O   
4251  C CB  . LEU C 111 ? 1.271 1.307 1.199 0.047  0.201  0.152  111 LEU AAA CB  
4252  C CG  . LEU C 111 ? 1.206 1.239 1.135 0.038  0.194  0.147  111 LEU AAA CG  
4253  C CD1 . LEU C 111 ? 1.187 1.213 1.110 0.034  0.187  0.140  111 LEU AAA CD1 
4254  C CD2 . LEU C 111 ? 1.314 1.366 1.261 0.033  0.190  0.148  111 LEU AAA CD2 
4255  N N   . GLN C 112 ? 1.601 1.593 1.492 0.056  0.218  0.152  112 GLN AAA N   
4256  C CA  . GLN C 112 ? 1.640 1.618 1.516 0.055  0.222  0.150  112 GLN AAA CA  
4257  C C   . GLN C 112 ? 1.661 1.612 1.513 0.054  0.223  0.145  112 GLN AAA C   
4258  O O   . GLN C 112 ? 1.711 1.650 1.551 0.047  0.219  0.141  112 GLN AAA O   
4259  C CB  . GLN C 112 ? 1.751 1.734 1.628 0.062  0.233  0.155  112 GLN AAA CB  
4260  C CG  . GLN C 112 ? 1.997 1.972 1.867 0.074  0.243  0.157  112 GLN AAA CG  
4261  C CD  . GLN C 112 ? 2.271 2.235 2.125 0.080  0.255  0.157  112 GLN AAA CD  
4262  O OE1 . GLN C 112 ? 2.397 2.368 2.253 0.076  0.256  0.158  112 GLN AAA OE1 
4263  N NE2 . GLN C 112 ? 2.332 2.278 2.172 0.090  0.263  0.155  112 GLN AAA NE2 
4264  N N   . GLU C 113 ? 1.530 1.472 1.376 0.061  0.226  0.145  113 GLU AAA N   
4265  C CA  . GLU C 113 ? 1.467 1.384 1.292 0.058  0.225  0.140  113 GLU AAA CA  
4266  C C   . GLU C 113 ? 1.443 1.361 1.268 0.048  0.213  0.137  113 GLU AAA C   
4267  O O   . GLU C 113 ? 1.487 1.389 1.295 0.041  0.210  0.133  113 GLU AAA O   
4268  C CB  . GLU C 113 ? 1.483 1.390 1.303 0.067  0.230  0.142  113 GLU AAA CB  
4269  C CG  . GLU C 113 ? 1.671 1.572 1.487 0.080  0.242  0.145  113 GLU AAA CG  
4270  C CD  . GLU C 113 ? 1.702 1.595 1.518 0.090  0.247  0.148  113 GLU AAA CD  
4271  O OE1 . GLU C 113 ? 1.586 1.477 1.404 0.086  0.239  0.149  113 GLU AAA OE1 
4272  O OE2 . GLU C 113 ? 1.820 1.707 1.632 0.102  0.258  0.150  113 GLU AAA OE2 
4273  N N   . GLN C 114 ? 1.433 1.371 1.277 0.046  0.207  0.138  114 GLN AAA N   
4274  C CA  . GLN C 114 ? 1.347 1.289 1.192 0.037  0.197  0.135  114 GLN AAA CA  
4275  C C   . GLN C 114 ? 1.324 1.266 1.168 0.031  0.194  0.132  114 GLN AAA C   
4276  O O   . GLN C 114 ? 1.381 1.314 1.215 0.025  0.189  0.130  114 GLN AAA O   
4277  C CB  . GLN C 114 ? 1.268 1.234 1.134 0.037  0.192  0.136  114 GLN AAA CB  
4278  C CG  . GLN C 114 ? 1.232 1.199 1.098 0.042  0.194  0.140  114 GLN AAA CG  
4279  C CD  . GLN C 114 ? 1.189 1.181 1.075 0.042  0.190  0.142  114 GLN AAA CD  
4280  O OE1 . GLN C 114 ? 1.162 1.168 1.058 0.037  0.185  0.138  114 GLN AAA OE1 
4281  N NE2 . GLN C 114 ? 1.183 1.180 1.073 0.049  0.193  0.147  114 GLN AAA NE2 
4282  N N   . ILE C 115 ? 1.330 1.282 1.184 0.032  0.196  0.134  115 ILE AAA N   
4283  C CA  . ILE C 115 ? 1.276 1.226 1.129 0.027  0.193  0.134  115 ILE AAA CA  
4284  C C   . ILE C 115 ? 1.346 1.276 1.177 0.025  0.196  0.133  115 ILE AAA C   
4285  O O   . ILE C 115 ? 1.324 1.250 1.149 0.018  0.191  0.132  115 ILE AAA O   
4286  C CB  . ILE C 115 ? 1.171 1.135 1.040 0.028  0.195  0.137  115 ILE AAA CB  
4287  C CG1 . ILE C 115 ? 1.149 1.131 1.037 0.027  0.190  0.137  115 ILE AAA CG1 
4288  C CG2 . ILE C 115 ? 1.228 1.187 1.093 0.023  0.193  0.138  115 ILE AAA CG2 
4289  C CD1 . ILE C 115 ? 1.219 1.216 1.122 0.028  0.192  0.141  115 ILE AAA CD1 
4290  N N   . GLY C 116 ? 1.373 1.292 1.193 0.031  0.205  0.134  116 GLY AAA N   
4291  C CA  . GLY C 116 ? 1.473 1.371 1.268 0.028  0.209  0.132  116 GLY AAA CA  
4292  C C   . GLY C 116 ? 1.446 1.331 1.227 0.021  0.202  0.128  116 GLY AAA C   
4293  O O   . GLY C 116 ? 1.560 1.437 1.328 0.014  0.198  0.127  116 GLY AAA O   
4294  N N   . TRP C 117 ? 1.374 1.258 1.157 0.022  0.199  0.127  117 TRP AAA N   
4295  C CA  . TRP C 117 ? 1.360 1.233 1.130 0.014  0.192  0.125  117 TRP AAA CA  
4296  C C   . TRP C 117 ? 1.401 1.289 1.182 0.006  0.183  0.126  117 TRP AAA C   
4297  O O   . TRP C 117 ? 1.452 1.333 1.220 -0.002 0.178  0.125  117 TRP AAA O   
4298  C CB  . TRP C 117 ? 1.362 1.234 1.134 0.016  0.192  0.126  117 TRP AAA CB  
4299  C CG  . TRP C 117 ? 1.355 1.206 1.113 0.023  0.200  0.126  117 TRP AAA CG  
4300  C CD1 . TRP C 117 ? 1.470 1.296 1.204 0.023  0.206  0.123  117 TRP AAA CD1 
4301  C CD2 . TRP C 117 ? 1.377 1.231 1.144 0.033  0.205  0.128  117 TRP AAA CD2 
4302  N NE1 . TRP C 117 ? 1.527 1.338 1.253 0.032  0.214  0.123  117 TRP AAA NE1 
4303  C CE2 . TRP C 117 ? 1.413 1.241 1.161 0.039  0.214  0.127  117 TRP AAA CE2 
4304  C CE3 . TRP C 117 ? 1.460 1.336 1.248 0.036  0.203  0.132  117 TRP AAA CE3 
4305  C CZ2 . TRP C 117 ? 1.461 1.285 1.212 0.049  0.220  0.130  117 TRP AAA CZ2 
4306  C CZ3 . TRP C 117 ? 1.505 1.378 1.296 0.046  0.208  0.136  117 TRP AAA CZ3 
4307  C CH2 . TRP C 117 ? 1.481 1.328 1.254 0.053  0.217  0.135  117 TRP AAA CH2 
4308  N N   . MET C 118 ? 1.335 1.244 1.138 0.009  0.180  0.126  118 MET AAA N   
4309  C CA  . MET C 118 ? 1.340 1.262 1.154 0.004  0.171  0.126  118 MET AAA CA  
4310  C C   . MET C 118 ? 1.372 1.292 1.184 0.001  0.169  0.127  118 MET AAA C   
4311  O O   . MET C 118 ? 1.459 1.384 1.273 -0.004 0.162  0.128  118 MET AAA O   
4312  C CB  . MET C 118 ? 1.372 1.314 1.209 0.008  0.170  0.125  118 MET AAA CB  
4313  C CG  . MET C 118 ? 1.357 1.306 1.198 0.010  0.169  0.125  118 MET AAA CG  
4314  S SD  . MET C 118 ? 1.506 1.477 1.370 0.014  0.168  0.124  118 MET AAA SD  
4315  C CE  . MET C 118 ? 1.450 1.433 1.324 0.011  0.160  0.120  118 MET AAA CE  
4316  N N   . THR C 119 ? 1.410 1.325 1.218 0.003  0.176  0.129  119 THR AAA N   
4317  C CA  . THR C 119 ? 1.482 1.395 1.287 -0.001 0.174  0.132  119 THR AAA CA  
4318  C C   . THR C 119 ? 1.537 1.433 1.317 -0.005 0.177  0.132  119 THR AAA C   
4319  O O   . THR C 119 ? 1.524 1.418 1.299 -0.008 0.176  0.135  119 THR AAA O   
4320  C CB  . THR C 119 ? 1.395 1.317 1.214 0.003  0.178  0.134  119 THR AAA CB  
4321  O OG1 . THR C 119 ? 1.412 1.328 1.224 0.009  0.187  0.135  119 THR AAA OG1 
4322  C CG2 . THR C 119 ? 1.353 1.291 1.195 0.006  0.174  0.133  119 THR AAA CG2 
4323  N N   . HIS C 120 ? 1.674 1.556 1.437 -0.006 0.179  0.129  120 HIS AAA N   
4324  C CA  . HIS C 120 ? 1.773 1.636 1.509 -0.011 0.182  0.128  120 HIS AAA CA  
4325  C C   . HIS C 120 ? 1.882 1.744 1.610 -0.021 0.172  0.130  120 HIS AAA C   
4326  O O   . HIS C 120 ? 1.840 1.717 1.584 -0.024 0.164  0.132  120 HIS AAA O   
4327  C CB  . HIS C 120 ? 1.912 1.755 1.630 -0.009 0.187  0.124  120 HIS AAA CB  
4328  C CG  . HIS C 120 ? 2.066 1.886 1.755 -0.011 0.193  0.121  120 HIS AAA CG  
4329  N ND1 . HIS C 120 ? 2.192 1.995 1.857 -0.021 0.188  0.119  120 HIS AAA ND1 
4330  C CD2 . HIS C 120 ? 2.169 1.981 1.847 -0.006 0.203  0.120  120 HIS AAA CD2 
4331  C CE1 . HIS C 120 ? 2.366 2.150 2.007 -0.022 0.195  0.115  120 HIS AAA CE1 
4332  N NE2 . HIS C 120 ? 2.438 2.228 2.086 -0.012 0.204  0.116  120 HIS AAA NE2 
4333  N N   . ASN C 121 ? 2.124 1.973 1.829 -0.028 0.173  0.130  121 ASN AAA N   
4334  C CA  . ASN C 121 ? 2.182 2.029 1.876 -0.039 0.163  0.132  121 ASN AAA CA  
4335  C C   . ASN C 121 ? 2.310 2.135 1.974 -0.046 0.165  0.128  121 ASN AAA C   
4336  O O   . ASN C 121 ? 2.319 2.127 1.960 -0.047 0.171  0.125  121 ASN AAA O   
4337  C CB  . ASN C 121 ? 2.209 2.063 1.903 -0.043 0.161  0.137  121 ASN AAA CB  
4338  C CG  . ASN C 121 ? 2.270 2.129 1.958 -0.054 0.150  0.142  121 ASN AAA CG  
4339  O OD1 . ASN C 121 ? 2.221 2.089 1.919 -0.056 0.142  0.143  121 ASN AAA OD1 
4340  N ND2 . ASN C 121 ? 2.447 2.301 2.118 -0.061 0.148  0.145  121 ASN AAA ND2 
4341  N N   . PRO C 122 ? 2.402 2.223 2.062 -0.052 0.159  0.127  122 PRO AAA N   
4342  C CA  . PRO C 122 ? 2.315 2.155 1.998 -0.051 0.152  0.129  122 PRO AAA CA  
4343  C C   . PRO C 122 ? 2.238 2.085 1.940 -0.040 0.158  0.127  122 PRO AAA C   
4344  O O   . PRO C 122 ? 2.337 2.169 2.030 -0.034 0.166  0.124  122 PRO AAA O   
4345  C CB  . PRO C 122 ? 2.401 2.232 2.067 -0.063 0.145  0.129  122 PRO AAA CB  
4346  C CG  . PRO C 122 ? 2.554 2.360 2.188 -0.071 0.147  0.126  122 PRO AAA CG  
4347  C CD  . PRO C 122 ? 2.483 2.279 2.112 -0.061 0.159  0.123  122 PRO AAA CD  
4348  N N   . PRO C 123 ? 1.987 1.856 1.714 -0.037 0.153  0.129  123 PRO AAA N   
4349  C CA  . PRO C 123 ? 1.800 1.678 1.545 -0.027 0.157  0.128  123 PRO AAA CA  
4350  C C   . PRO C 123 ? 1.734 1.606 1.474 -0.028 0.157  0.126  123 PRO AAA C   
4351  O O   . PRO C 123 ? 1.840 1.712 1.573 -0.037 0.151  0.128  123 PRO AAA O   
4352  C CB  . PRO C 123 ? 1.762 1.664 1.532 -0.025 0.151  0.130  123 PRO AAA CB  
4353  C CG  . PRO C 123 ? 1.872 1.780 1.638 -0.034 0.143  0.133  123 PRO AAA CG  
4354  C CD  . PRO C 123 ? 1.987 1.875 1.727 -0.041 0.144  0.133  123 PRO AAA CD  
4355  N N   . ILE C 124 ? 1.594 1.461 1.338 -0.020 0.165  0.125  124 ILE AAA N   
4356  C CA  . ILE C 124 ? 1.484 1.348 1.227 -0.019 0.165  0.125  124 ILE AAA CA  
4357  C C   . ILE C 124 ? 1.378 1.267 1.147 -0.013 0.163  0.126  124 ILE AAA C   
4358  O O   . ILE C 124 ? 1.393 1.287 1.173 -0.004 0.169  0.125  124 ILE AAA O   
4359  C CB  . ILE C 124 ? 1.516 1.357 1.244 -0.013 0.173  0.123  124 ILE AAA CB  
4360  C CG1 . ILE C 124 ? 1.658 1.472 1.357 -0.019 0.175  0.120  124 ILE AAA CG1 
4361  C CG2 . ILE C 124 ? 1.460 1.296 1.187 -0.013 0.172  0.124  124 ILE AAA CG2 
4362  C CD1 . ILE C 124 ? 1.691 1.501 1.386 -0.013 0.183  0.119  124 ILE AAA CD1 
4363  N N   . PRO C 125 ? 1.348 1.255 1.127 -0.018 0.156  0.127  125 PRO AAA N   
4364  C CA  . PRO C 125 ? 1.233 1.164 1.036 -0.013 0.154  0.126  125 PRO AAA CA  
4365  C C   . PRO C 125 ? 1.267 1.204 1.077 -0.009 0.156  0.127  125 PRO AAA C   
4366  O O   . PRO C 125 ? 1.303 1.253 1.118 -0.012 0.152  0.128  125 PRO AAA O   
4367  C CB  . PRO C 125 ? 1.182 1.128 0.990 -0.019 0.146  0.127  125 PRO AAA CB  
4368  C CG  . PRO C 125 ? 1.289 1.223 1.079 -0.029 0.143  0.130  125 PRO AAA CG  
4369  C CD  . PRO C 125 ? 1.369 1.274 1.138 -0.029 0.149  0.129  125 PRO AAA CD  
4370  N N   . VAL C 126 ? 1.251 1.179 1.060 -0.001 0.163  0.127  126 VAL AAA N   
4371  C CA  . VAL C 126 ? 1.232 1.164 1.046 0.003  0.166  0.129  126 VAL AAA CA  
4372  C C   . VAL C 126 ? 1.218 1.177 1.052 0.004  0.162  0.129  126 VAL AAA C   
4373  O O   . VAL C 126 ? 1.293 1.262 1.131 0.004  0.160  0.131  126 VAL AAA O   
4374  C CB  . VAL C 126 ? 1.229 1.149 1.040 0.012  0.174  0.131  126 VAL AAA CB  
4375  C CG1 . VAL C 126 ? 1.338 1.229 1.127 0.011  0.178  0.130  126 VAL AAA CG1 
4376  C CG2 . VAL C 126 ? 1.213 1.144 1.037 0.016  0.177  0.129  126 VAL AAA CG2 
4377  N N   . GLY C 127 ? 1.199 1.171 1.045 0.006  0.161  0.126  127 GLY AAA N   
4378  C CA  . GLY C 127 ? 1.193 1.188 1.057 0.007  0.157  0.123  127 GLY AAA CA  
4379  C C   . GLY C 127 ? 1.241 1.248 1.105 0.001  0.151  0.123  127 GLY AAA C   
4380  O O   . GLY C 127 ? 1.228 1.251 1.098 0.001  0.150  0.123  127 GLY AAA O   
4381  N N   . GLU C 128 ? 1.140 1.141 0.996 -0.004 0.148  0.123  128 GLU AAA N   
4382  C CA  . GLU C 128 ? 1.144 1.160 1.002 -0.009 0.143  0.123  128 GLU AAA CA  
4383  C C   . GLU C 128 ? 1.199 1.213 1.048 -0.014 0.142  0.128  128 GLU AAA C   
4384  O O   . GLU C 128 ? 1.287 1.320 1.141 -0.017 0.139  0.129  128 GLU AAA O   
4385  C CB  . GLU C 128 ? 1.155 1.166 1.007 -0.014 0.139  0.124  128 GLU AAA CB  
4386  C CG  . GLU C 128 ? 1.281 1.298 1.145 -0.009 0.139  0.121  128 GLU AAA CG  
4387  C CD  . GLU C 128 ? 1.255 1.293 1.136 -0.004 0.138  0.116  128 GLU AAA CD  
4388  O OE1 . GLU C 128 ? 1.173 1.229 1.059 -0.005 0.135  0.116  128 GLU AAA OE1 
4389  O OE2 . GLU C 128 ? 1.344 1.382 1.234 0.002  0.140  0.113  128 GLU AAA OE2 
4390  N N   . ILE C 129 ? 1.207 1.197 1.040 -0.016 0.145  0.131  129 ILE AAA N   
4391  C CA  . ILE C 129 ? 1.251 1.234 1.074 -0.021 0.144  0.136  129 ILE AAA CA  
4392  C C   . ILE C 129 ? 1.220 1.218 1.054 -0.016 0.145  0.137  129 ILE AAA C   
4393  O O   . ILE C 129 ? 1.288 1.299 1.123 -0.021 0.142  0.141  129 ILE AAA O   
4394  C CB  . ILE C 129 ? 1.354 1.305 1.158 -0.022 0.147  0.137  129 ILE AAA CB  
4395  C CG1 . ILE C 129 ? 1.364 1.302 1.155 -0.029 0.145  0.136  129 ILE AAA CG1 
4396  C CG2 . ILE C 129 ? 1.413 1.353 1.206 -0.027 0.146  0.143  129 ILE AAA CG2 
4397  C CD1 . ILE C 129 ? 1.392 1.297 1.163 -0.027 0.150  0.135  129 ILE AAA CD1 
4398  N N   . TYR C 130 ? 1.179 1.178 1.021 -0.008 0.150  0.136  130 TYR AAA N   
4399  C CA  . TYR C 130 ? 1.158 1.172 1.010 -0.004 0.151  0.138  130 TYR AAA CA  
4400  C C   . TYR C 130 ? 1.159 1.203 1.025 -0.006 0.147  0.135  130 TYR AAA C   
4401  O O   . TYR C 130 ? 1.256 1.314 1.124 -0.007 0.145  0.138  130 TYR AAA O   
4402  C CB  . TYR C 130 ? 1.150 1.162 1.010 0.005  0.156  0.137  130 TYR AAA CB  
4403  C CG  . TYR C 130 ? 1.104 1.129 0.973 0.009  0.157  0.141  130 TYR AAA CG  
4404  C CD1 . TYR C 130 ? 1.110 1.137 0.974 0.006  0.155  0.147  130 TYR AAA CD1 
4405  C CD2 . TYR C 130 ? 1.136 1.172 1.017 0.015  0.159  0.139  130 TYR AAA CD2 
4406  C CE1 . TYR C 130 ? 1.190 1.231 1.063 0.010  0.155  0.152  130 TYR AAA CE1 
4407  C CE2 . TYR C 130 ? 1.150 1.201 1.040 0.018  0.159  0.144  130 TYR AAA CE2 
4408  C CZ  . TYR C 130 ? 1.215 1.268 1.101 0.015  0.157  0.150  130 TYR AAA CZ  
4409  O OH  . TYR C 130 ? 1.396 1.465 1.290 0.018  0.157  0.156  130 TYR AAA OH  
4410  N N   . LYS C 131 ? 1.141 1.192 1.013 -0.005 0.145  0.128  131 LYS AAA N   
4411  C CA  . LYS C 131 ? 1.158 1.235 1.040 -0.005 0.142  0.124  131 LYS AAA CA  
4412  C C   . LYS C 131 ? 1.106 1.195 0.984 -0.012 0.139  0.128  131 LYS AAA C   
4413  O O   . LYS C 131 ? 1.110 1.221 0.994 -0.013 0.137  0.127  131 LYS AAA O   
4414  C CB  . LYS C 131 ? 1.031 1.111 0.921 -0.003 0.141  0.118  131 LYS AAA CB  
4415  C CG  . LYS C 131 ? 1.032 1.135 0.934 0.000  0.140  0.111  131 LYS AAA CG  
4416  C CD  . LYS C 131 ? 1.015 1.119 0.923 0.003  0.138  0.106  131 LYS AAA CD  
4417  C CE  . LYS C 131 ? 1.037 1.123 0.946 0.006  0.140  0.104  131 LYS AAA CE  
4418  N NZ  . LYS C 131 ? 1.055 1.145 0.973 0.010  0.138  0.099  131 LYS AAA NZ  
4419  N N   . ARG C 132 ? 1.179 1.254 1.046 -0.018 0.137  0.132  132 ARG AAA N   
4420  C CA  . ARG C 132 ? 1.255 1.341 1.118 -0.027 0.133  0.137  132 ARG AAA CA  
4421  C C   . ARG C 132 ? 1.244 1.332 1.103 -0.029 0.133  0.143  132 ARG AAA C   
4422  O O   . ARG C 132 ? 1.277 1.390 1.141 -0.033 0.131  0.146  132 ARG AAA O   
4423  C CB  . ARG C 132 ? 1.398 1.466 1.248 -0.035 0.130  0.141  132 ARG AAA CB  
4424  C CG  . ARG C 132 ? 1.609 1.690 1.454 -0.045 0.125  0.147  132 ARG AAA CG  
4425  C CD  . ARG C 132 ? 1.732 1.791 1.561 -0.055 0.122  0.152  132 ARG AAA CD  
4426  N NE  . ARG C 132 ? 1.897 1.950 1.727 -0.052 0.122  0.147  132 ARG AAA NE  
4427  C CZ  . ARG C 132 ? 2.005 2.030 1.825 -0.050 0.125  0.145  132 ARG AAA CZ  
4428  N NH1 . ARG C 132 ? 1.875 1.875 1.683 -0.049 0.128  0.146  132 ARG AAA NH1 
4429  N NH2 . ARG C 132 ? 2.021 2.045 1.843 -0.047 0.124  0.142  132 ARG AAA NH2 
4430  N N   . TRP C 133 ? 1.176 1.243 1.028 -0.027 0.136  0.147  133 TRP AAA N   
4431  C CA  . TRP C 133 ? 1.229 1.297 1.079 -0.028 0.136  0.154  133 TRP AAA CA  
4432  C C   . TRP C 133 ? 1.186 1.283 1.050 -0.024 0.136  0.152  133 TRP AAA C   
4433  O O   . TRP C 133 ? 1.253 1.366 1.117 -0.029 0.134  0.158  133 TRP AAA O   
4434  C CB  . TRP C 133 ? 1.243 1.283 1.085 -0.023 0.140  0.157  133 TRP AAA CB  
4435  C CG  . TRP C 133 ? 1.332 1.339 1.158 -0.027 0.140  0.158  133 TRP AAA CG  
4436  C CD1 . TRP C 133 ? 1.410 1.412 1.226 -0.036 0.136  0.158  133 TRP AAA CD1 
4437  C CD2 . TRP C 133 ? 1.351 1.329 1.167 -0.021 0.145  0.159  133 TRP AAA CD2 
4438  N NE1 . TRP C 133 ? 1.430 1.399 1.230 -0.038 0.138  0.158  133 TRP AAA NE1 
4439  C CE2 . TRP C 133 ? 1.398 1.351 1.197 -0.028 0.144  0.158  133 TRP AAA CE2 
4440  C CE3 . TRP C 133 ? 1.333 1.304 1.154 -0.010 0.150  0.160  133 TRP AAA CE3 
4441  C CZ2 . TRP C 133 ? 1.417 1.336 1.201 -0.024 0.149  0.158  133 TRP AAA CZ2 
4442  C CZ3 . TRP C 133 ? 1.351 1.291 1.159 -0.006 0.156  0.161  133 TRP AAA CZ3 
4443  C CH2 . TRP C 133 ? 1.416 1.329 1.205 -0.012 0.155  0.159  133 TRP AAA CH2 
4444  N N   . ILE C 134 ? 1.150 1.253 1.023 -0.017 0.138  0.144  134 ILE AAA N   
4445  C CA  . ILE C 134 ? 1.047 1.175 0.931 -0.014 0.138  0.141  134 ILE AAA CA  
4446  C C   . ILE C 134 ? 1.138 1.293 1.026 -0.018 0.136  0.138  134 ILE AAA C   
4447  O O   . ILE C 134 ? 1.219 1.396 1.110 -0.020 0.134  0.140  134 ILE AAA O   
4448  C CB  . ILE C 134 ? 1.033 1.160 0.926 -0.007 0.141  0.133  134 ILE AAA CB  
4449  C CG1 . ILE C 134 ? 1.080 1.188 0.972 -0.002 0.144  0.138  134 ILE AAA CG1 
4450  C CG2 . ILE C 134 ? 1.129 1.283 1.032 -0.005 0.140  0.128  134 ILE AAA CG2 
4451  C CD1 . ILE C 134 ? 1.045 1.146 0.943 0.004  0.147  0.132  134 ILE AAA CD1 
4452  N N   . ILE C 135 ? 1.187 1.342 1.075 -0.019 0.135  0.134  135 ILE AAA N   
4453  C CA  . ILE C 135 ? 1.121 1.303 1.013 -0.022 0.133  0.131  135 ILE AAA CA  
4454  C C   . ILE C 135 ? 1.176 1.370 1.063 -0.031 0.130  0.141  135 ILE AAA C   
4455  O O   . ILE C 135 ? 1.284 1.505 1.174 -0.033 0.130  0.141  135 ILE AAA O   
4456  C CB  . ILE C 135 ? 1.030 1.210 0.926 -0.020 0.133  0.126  135 ILE AAA CB  
4457  C CG1 . ILE C 135 ? 1.008 1.184 0.912 -0.011 0.135  0.116  135 ILE AAA CG1 
4458  C CG2 . ILE C 135 ? 1.120 1.327 1.020 -0.023 0.131  0.127  135 ILE AAA CG2 
4459  C CD1 . ILE C 135 ? 1.202 1.369 1.109 -0.008 0.134  0.112  135 ILE AAA CD1 
4460  N N   . LEU C 136 ? 1.194 1.365 1.069 -0.037 0.129  0.150  136 LEU AAA N   
4461  C CA  . LEU C 136 ? 1.243 1.421 1.111 -0.047 0.125  0.160  136 LEU AAA CA  
4462  C C   . LEU C 136 ? 1.327 1.520 1.198 -0.046 0.126  0.164  136 LEU AAA C   
4463  O O   . LEU C 136 ? 1.457 1.674 1.329 -0.052 0.124  0.169  136 LEU AAA O   
4464  C CB  . LEU C 136 ? 1.210 1.357 1.064 -0.054 0.123  0.168  136 LEU AAA CB  
4465  C CG  . LEU C 136 ? 1.421 1.559 1.270 -0.061 0.121  0.168  136 LEU AAA CG  
4466  C CD1 . LEU C 136 ? 1.572 1.740 1.423 -0.070 0.117  0.174  136 LEU AAA CD1 
4467  C CD2 . LEU C 136 ? 1.423 1.558 1.277 -0.054 0.122  0.159  136 LEU AAA CD2 
4468  N N   . GLY C 137 ? 1.360 1.538 1.232 -0.039 0.128  0.163  137 GLY AAA N   
4469  C CA  . GLY C 137 ? 1.388 1.582 1.264 -0.038 0.128  0.167  137 GLY AAA CA  
4470  C C   . GLY C 137 ? 1.388 1.616 1.273 -0.037 0.129  0.160  137 GLY AAA C   
4471  O O   . GLY C 137 ? 1.440 1.690 1.324 -0.041 0.127  0.165  137 GLY AAA O   
4472  N N   . LEU C 138 ? 1.351 1.582 1.243 -0.030 0.131  0.147  138 LEU AAA N   
4473  C CA  . LEU C 138 ? 1.259 1.519 1.157 -0.028 0.132  0.138  138 LEU AAA CA  
4474  C C   . LEU C 138 ? 1.327 1.613 1.223 -0.033 0.131  0.139  138 LEU AAA C   
4475  O O   . LEU C 138 ? 1.425 1.738 1.323 -0.034 0.131  0.137  138 LEU AAA O   
4476  C CB  . LEU C 138 ? 1.059 1.311 0.963 -0.020 0.134  0.125  138 LEU AAA CB  
4477  C CG  . LEU C 138 ? 1.041 1.274 0.948 -0.015 0.135  0.122  138 LEU AAA CG  
4478  C CD1 . LEU C 138 ? 1.018 1.241 0.930 -0.009 0.136  0.111  138 LEU AAA CD1 
4479  C CD2 . LEU C 138 ? 1.169 1.419 1.078 -0.015 0.134  0.122  138 LEU AAA CD2 
4480  N N   . ASN C 139 ? 1.376 1.656 1.271 -0.037 0.130  0.143  139 ASN AAA N   
4481  C CA  . ASN C 139 ? 1.411 1.719 1.306 -0.043 0.129  0.147  139 ASN AAA CA  
4482  C C   . ASN C 139 ? 1.488 1.813 1.378 -0.052 0.127  0.157  139 ASN AAA C   
4483  O O   . ASN C 139 ? 1.645 2.003 1.537 -0.054 0.128  0.156  139 ASN AAA O   
4484  C CB  . ASN C 139 ? 1.451 1.748 1.343 -0.048 0.127  0.152  139 ASN AAA CB  
4485  C CG  . ASN C 139 ? 1.494 1.785 1.393 -0.040 0.129  0.141  139 ASN AAA CG  
4486  O OD1 . ASN C 139 ? 1.463 1.742 1.366 -0.031 0.131  0.132  139 ASN AAA OD1 
4487  N ND2 . ASN C 139 ? 1.627 1.925 1.528 -0.044 0.127  0.144  139 ASN AAA ND2 
4488  N N   . LYS C 140 ? 1.363 1.666 1.246 -0.056 0.124  0.168  140 LYS AAA N   
4489  C CA  . LYS C 140 ? 1.492 1.810 1.371 -0.064 0.122  0.180  140 LYS AAA CA  
4490  C C   . LYS C 140 ? 1.419 1.760 1.301 -0.060 0.123  0.175  140 LYS AAA C   
4491  O O   . LYS C 140 ? 1.521 1.892 1.402 -0.066 0.123  0.180  140 LYS AAA O   
4492  C CB  . LYS C 140 ? 1.583 1.869 1.453 -0.067 0.119  0.192  140 LYS AAA CB  
4493  C CG  . LYS C 140 ? 1.719 1.981 1.582 -0.075 0.116  0.200  140 LYS AAA CG  
4494  C CD  . LYS C 140 ? 1.767 1.990 1.622 -0.074 0.116  0.207  140 LYS AAA CD  
4495  C CE  . LYS C 140 ? 1.827 2.025 1.670 -0.084 0.112  0.216  140 LYS AAA CE  
4496  N NZ  . LYS C 140 ? 1.915 2.072 1.749 -0.081 0.112  0.220  140 LYS AAA NZ  
4497  N N   . ILE C 141 ? 1.351 1.682 1.237 -0.051 0.125  0.166  141 ILE AAA N   
4498  C CA  . ILE C 141 ? 1.377 1.729 1.266 -0.048 0.126  0.161  141 ILE AAA CA  
4499  C C   . ILE C 141 ? 1.452 1.835 1.342 -0.047 0.129  0.149  141 ILE AAA C   
4500  O O   . ILE C 141 ? 1.650 2.062 1.539 -0.051 0.129  0.150  141 ILE AAA O   
4501  C CB  . ILE C 141 ? 1.334 1.665 1.227 -0.040 0.127  0.153  141 ILE AAA CB  
4502  C CG1 . ILE C 141 ? 1.309 1.615 1.200 -0.040 0.126  0.166  141 ILE AAA CG1 
4503  C CG2 . ILE C 141 ? 1.339 1.693 1.235 -0.038 0.127  0.145  141 ILE AAA CG2 
4504  C CD1 . ILE C 141 ? 1.328 1.610 1.224 -0.032 0.127  0.160  141 ILE AAA CD1 
4505  N N   . VAL C 142 ? 1.415 1.794 1.310 -0.042 0.131  0.139  142 VAL AAA N   
4506  C CA  . VAL C 142 ? 1.368 1.776 1.265 -0.039 0.135  0.128  142 VAL AAA CA  
4507  C C   . VAL C 142 ? 1.445 1.884 1.339 -0.047 0.134  0.137  142 VAL AAA C   
4508  O O   . VAL C 142 ? 1.507 1.976 1.399 -0.047 0.137  0.132  142 VAL AAA O   
4509  C CB  . VAL C 142 ? 1.266 1.663 1.170 -0.032 0.137  0.118  142 VAL AAA CB  
4510  C CG1 . VAL C 142 ? 1.298 1.725 1.205 -0.028 0.141  0.110  142 VAL AAA CG1 
4511  C CG2 . VAL C 142 ? 1.310 1.683 1.217 -0.023 0.138  0.107  142 VAL AAA CG2 
4512  N N   . ARG C 143 ? 1.431 1.862 1.323 -0.055 0.131  0.151  143 ARG AAA N   
4513  C CA  . ARG C 143 ? 1.542 2.002 1.431 -0.065 0.130  0.162  143 ARG AAA CA  
4514  C C   . ARG C 143 ? 1.597 2.072 1.479 -0.071 0.128  0.170  143 ARG AAA C   
4515  O O   . ARG C 143 ? 1.729 2.240 1.610 -0.075 0.130  0.172  143 ARG AAA O   
4516  C CB  . ARG C 143 ? 1.686 2.127 1.573 -0.073 0.127  0.175  143 ARG AAA CB  
4517  C CG  . ARG C 143 ? 1.874 2.341 1.758 -0.085 0.125  0.188  143 ARG AAA CG  
4518  C CD  . ARG C 143 ? 2.103 2.547 1.986 -0.091 0.121  0.195  143 ARG AAA CD  
4519  N NE  . ARG C 143 ? 2.098 2.499 1.974 -0.094 0.117  0.202  143 ARG AAA NE  
4520  C CZ  . ARG C 143 ? 2.254 2.628 2.125 -0.100 0.114  0.208  143 ARG AAA CZ  
4521  N NH1 . ARG C 143 ? 2.407 2.795 2.281 -0.105 0.113  0.209  143 ARG AAA NH1 
4522  N NH2 . ARG C 143 ? 2.222 2.557 2.086 -0.100 0.111  0.212  143 ARG AAA NH2 
4523  N N   . MET C 144 ? 1.656 2.107 1.536 -0.071 0.125  0.176  144 MET AAA N   
4524  C CA  . MET C 144 ? 1.721 2.187 1.596 -0.077 0.123  0.186  144 MET AAA CA  
4525  C C   . MET C 144 ? 1.778 2.273 1.653 -0.073 0.126  0.173  144 MET AAA C   
4526  O O   . MET C 144 ? 1.875 2.400 1.745 -0.079 0.125  0.179  144 MET AAA O   
4527  C CB  . MET C 144 ? 1.789 2.224 1.663 -0.076 0.119  0.194  144 MET AAA CB  
4528  C CG  . MET C 144 ? 1.916 2.326 1.787 -0.082 0.116  0.209  144 MET AAA CG  
4529  S SD  . MET C 144 ? 2.113 2.482 1.983 -0.077 0.114  0.217  144 MET AAA SD  
4530  C CE  . MET C 144 ? 2.026 2.368 1.889 -0.086 0.111  0.230  144 MET AAA CE  
4531  N N   . TYR C 145 ? 1.659 2.145 1.538 -0.063 0.129  0.156  145 TYR AAA N   
4532  C CA  . TYR C 145 ? 1.735 2.242 1.613 -0.059 0.132  0.141  145 TYR AAA CA  
4533  C C   . TYR C 145 ? 1.763 2.298 1.640 -0.056 0.137  0.130  145 TYR AAA C   
4534  O O   . TYR C 145 ? 1.767 2.317 1.641 -0.051 0.140  0.115  145 TYR AAA O   
4535  C CB  . TYR C 145 ? 1.765 2.246 1.647 -0.050 0.132  0.128  145 TYR AAA CB  
4536  C CG  . TYR C 145 ? 1.731 2.192 1.613 -0.051 0.128  0.136  145 TYR AAA CG  
4537  C CD1 . TYR C 145 ? 1.721 2.168 1.603 -0.056 0.124  0.154  145 TYR AAA CD1 
4538  C CD2 . TYR C 145 ? 1.750 2.207 1.634 -0.047 0.127  0.126  145 TYR AAA CD2 
4539  C CE1 . TYR C 145 ? 1.775 2.206 1.659 -0.055 0.121  0.162  145 TYR AAA CE1 
4540  C CE2 . TYR C 145 ? 1.814 2.257 1.700 -0.048 0.124  0.134  145 TYR AAA CE2 
4541  C CZ  . TYR C 145 ? 1.864 2.295 1.751 -0.051 0.121  0.152  145 TYR AAA CZ  
4542  O OH  . TYR C 145 ? 1.869 2.288 1.760 -0.049 0.118  0.161  145 TYR AAA OH  
4543  N N   . SER C 146 ? 1.468 2.502 1.931 -0.053 0.278  0.265  146 SER AAA N   
4544  C CA  . SER C 146 ? 1.516 2.500 1.935 -0.083 0.270  0.256  146 SER AAA CA  
4545  C C   . SER C 146 ? 1.470 2.490 1.884 -0.084 0.242  0.267  146 SER AAA C   
4546  O O   . SER C 146 ? 1.342 2.358 1.753 -0.052 0.231  0.288  146 SER AAA O   
4547  C CB  . SER C 146 ? 1.457 2.350 1.832 -0.069 0.278  0.255  146 SER AAA CB  
4548  O OG  . SER C 146 ? 1.411 2.264 1.753 -0.094 0.272  0.249  146 SER AAA OG  
4549  N N   . PRO C 147 ? 1.433 2.483 1.842 -0.119 0.230  0.253  147 PRO AAA N   
4550  C CA  . PRO C 147 ? 1.467 2.560 1.864 -0.116 0.201  0.263  147 PRO AAA CA  
4551  C C   . PRO C 147 ? 1.587 2.620 1.930 -0.107 0.197  0.277  147 PRO AAA C   
4552  O O   . PRO C 147 ? 1.858 2.918 2.185 -0.090 0.178  0.296  147 PRO AAA O   
4553  C CB  . PRO C 147 ? 1.432 2.566 1.835 -0.159 0.192  0.236  147 PRO AAA CB  
4554  C CG  . PRO C 147 ? 1.512 2.641 1.951 -0.180 0.218  0.219  147 PRO AAA CG  
4555  C CD  . PRO C 147 ? 1.476 2.527 1.891 -0.158 0.242  0.229  147 PRO AAA CD  
4556  N N   . THR C 148 ? 1.560 2.518 1.877 -0.115 0.216  0.272  148 THR AAA N   
4557  C CA  . THR C 148 ? 1.612 2.519 1.887 -0.113 0.216  0.285  148 THR AAA CA  
4558  C C   . THR C 148 ? 1.633 2.469 1.908 -0.100 0.232  0.291  148 THR AAA C   
4559  O O   . THR C 148 ? 1.592 2.403 1.877 -0.105 0.244  0.275  148 THR AAA O   
4560  C CB  . THR C 148 ? 1.622 2.519 1.865 -0.145 0.219  0.266  148 THR AAA CB  
4561  O OG1 . THR C 148 ? 1.589 2.546 1.842 -0.166 0.206  0.246  148 THR AAA OG1 
4562  C CG2 . THR C 148 ? 1.750 2.628 1.952 -0.138 0.216  0.285  148 THR AAA CG2 
4563  N N   . SER C 149 ? 1.762 2.564 2.024 -0.083 0.231  0.315  149 SER AAA N   
4564  C CA  . SER C 149 ? 1.775 2.506 2.040 -0.078 0.242  0.317  149 SER AAA CA  
4565  C C   . SER C 149 ? 1.720 2.422 1.967 -0.106 0.251  0.304  149 SER AAA C   
4566  O O   . SER C 149 ? 1.706 2.427 1.930 -0.120 0.251  0.307  149 SER AAA O   
4567  C CB  . SER C 149 ? 1.785 2.485 2.051 -0.054 0.241  0.348  149 SER AAA CB  
4568  O OG  . SER C 149 ? 1.732 2.365 2.003 -0.061 0.250  0.348  149 SER AAA OG  
4569  N N   . ILE C 150 ? 1.596 2.252 1.850 -0.110 0.258  0.290  150 ILE AAA N   
4570  C CA  A ILE C 150 ? 1.536 2.169 1.782 -0.132 0.266  0.278  150 ILE AAA CA  
4571  C C   . ILE C 150 ? 1.694 2.318 1.933 -0.137 0.271  0.298  150 ILE AAA C   
4572  O O   . ILE C 150 ? 1.684 2.313 1.907 -0.153 0.280  0.293  150 ILE AAA O   
4573  C CB  A ILE C 150 ? 1.469 2.056 1.726 -0.130 0.266  0.262  150 ILE AAA CB  
4574  C CG1 A ILE C 150 ? 1.492 2.064 1.745 -0.148 0.273  0.252  150 ILE AAA CG1 
4575  C CG2 A ILE C 150 ? 1.491 2.039 1.767 -0.115 0.260  0.274  150 ILE AAA CG2 
4576  C CD1 A ILE C 150 ? 1.489 2.023 1.751 -0.145 0.267  0.237  150 ILE AAA CD1 
4577  N N   . LEU C 151 ? 1.708 2.315 1.957 -0.122 0.270  0.324  151 LEU AAA N   
4578  C CA  . LEU C 151 ? 1.630 2.223 1.875 -0.125 0.281  0.350  151 LEU AAA CA  
4579  C C   . LEU C 151 ? 1.635 2.269 1.841 -0.128 0.285  0.359  151 LEU AAA C   
4580  O O   . LEU C 151 ? 1.759 2.386 1.953 -0.134 0.300  0.374  151 LEU AAA O   
4581  C CB  . LEU C 151 ? 1.658 2.222 1.920 -0.105 0.280  0.379  151 LEU AAA CB  
4582  C CG  . LEU C 151 ? 1.738 2.255 2.033 -0.099 0.273  0.366  151 LEU AAA CG  
4583  C CD1 . LEU C 151 ? 1.878 2.358 2.188 -0.079 0.276  0.396  151 LEU AAA CD1 
4584  C CD2 . LEU C 151 ? 1.746 2.233 2.065 -0.120 0.275  0.346  151 LEU AAA CD2 
4585  N N   . ASP C 152 ? 1.689 2.368 1.876 -0.124 0.271  0.349  152 ASP AAA N   
4586  C CA  . ASP C 152 ? 1.656 2.378 1.802 -0.127 0.267  0.350  152 ASP AAA CA  
4587  C C   . ASP C 152 ? 1.540 2.275 1.669 -0.151 0.269  0.315  152 ASP AAA C   
4588  O O   . ASP C 152 ? 1.517 2.285 1.608 -0.156 0.263  0.307  152 ASP AAA O   
4589  C CB  . ASP C 152 ? 1.738 2.508 1.878 -0.108 0.246  0.359  152 ASP AAA CB  
4590  C CG  . ASP C 152 ? 1.847 2.601 1.991 -0.078 0.246  0.400  152 ASP AAA CG  
4591  O OD1 . ASP C 152 ? 1.775 2.494 1.904 -0.076 0.263  0.426  152 ASP AAA OD1 
4592  O OD2 . ASP C 152 ? 1.995 2.770 2.159 -0.057 0.232  0.408  152 ASP AAA OD2 
4593  N N   . ILE C 153 ? 1.517 2.226 1.669 -0.165 0.276  0.293  153 ILE AAA N   
4594  C CA  . ILE C 153 ? 1.596 2.305 1.733 -0.186 0.283  0.264  153 ILE AAA CA  
4595  C C   . ILE C 153 ? 1.623 2.304 1.745 -0.190 0.303  0.269  153 ILE AAA C   
4596  O O   . ILE C 153 ? 1.603 2.251 1.753 -0.189 0.313  0.273  153 ILE AAA O   
4597  C CB  . ILE C 153 ? 1.655 2.348 1.818 -0.193 0.284  0.243  153 ILE AAA CB  
4598  C CG1 . ILE C 153 ? 1.641 2.366 1.826 -0.185 0.270  0.243  153 ILE AAA CG1 
4599  C CG2 . ILE C 153 ? 1.622 2.308 1.768 -0.213 0.294  0.217  153 ILE AAA CG2 
4600  C CD1 . ILE C 153 ? 1.609 2.388 1.785 -0.196 0.258  0.232  153 ILE AAA CD1 
4601  N N   . ARG C 154 ? 1.677 2.372 1.755 -0.193 0.309  0.267  154 ARG AAA N   
4602  C CA  . ARG C 154 ? 1.758 2.432 1.819 -0.193 0.333  0.273  154 ARG AAA CA  
4603  C C   . ARG C 154 ? 1.735 2.410 1.753 -0.205 0.339  0.242  154 ARG AAA C   
4604  O O   . ARG C 154 ? 1.786 2.488 1.773 -0.211 0.322  0.225  154 ARG AAA O   
4605  C CB  . ARG C 154 ? 1.840 2.520 1.879 -0.177 0.342  0.309  154 ARG AAA CB  
4606  C CG  . ARG C 154 ? 1.913 2.592 1.985 -0.164 0.332  0.339  154 ARG AAA CG  
4607  C CD  . ARG C 154 ? 1.954 2.630 2.006 -0.147 0.347  0.380  154 ARG AAA CD  
4608  N NE  . ARG C 154 ? 2.175 2.820 2.267 -0.151 0.373  0.400  154 ARG AAA NE  
4609  C CZ  . ARG C 154 ? 2.314 2.955 2.393 -0.155 0.401  0.404  154 ARG AAA CZ  
4610  N NH1 . ARG C 154 ? 2.406 3.064 2.425 -0.154 0.408  0.387  154 ARG AAA NH1 
4611  N NH2 . ARG C 154 ? 2.336 2.957 2.468 -0.160 0.424  0.423  154 ARG AAA NH2 
4612  N N   . GLN C 155 ? 1.787 2.434 1.808 -0.209 0.362  0.233  155 GLN AAA N   
4613  C CA  . GLN C 155 ? 1.885 2.519 1.868 -0.219 0.371  0.201  155 GLN AAA CA  
4614  C C   . GLN C 155 ? 2.047 2.695 1.965 -0.213 0.377  0.199  155 GLN AAA C   
4615  O O   . GLN C 155 ? 2.197 2.847 2.100 -0.197 0.395  0.226  155 GLN AAA O   
4616  C CB  . GLN C 155 ? 1.950 2.551 1.955 -0.216 0.395  0.196  155 GLN AAA CB  
4617  C CG  . GLN C 155 ? 2.052 2.627 2.022 -0.225 0.407  0.161  155 GLN AAA CG  
4618  C CD  . GLN C 155 ? 2.105 2.648 2.094 -0.216 0.433  0.161  155 GLN AAA CD  
4619  O OE1 . GLN C 155 ? 2.099 2.650 2.128 -0.203 0.443  0.186  155 GLN AAA OE1 
4620  N NE2 . GLN C 155 ? 2.024 2.534 1.990 -0.221 0.444  0.132  155 GLN AAA NE2 
4621  N N   . GLY C 156 ? 2.242 2.897 2.118 -0.225 0.362  0.165  156 GLY AAA N   
4622  C CA  . GLY C 156 ? 2.523 3.187 2.325 -0.220 0.364  0.153  156 GLY AAA CA  
4623  C C   . GLY C 156 ? 2.666 3.291 2.439 -0.213 0.400  0.142  156 GLY AAA C   
4624  O O   . GLY C 156 ? 2.839 3.433 2.651 -0.217 0.417  0.135  156 GLY AAA O   
4625  N N   . PRO C 157 ? 2.703 3.331 2.406 -0.198 0.413  0.143  157 PRO AAA N   
4626  C CA  A PRO C 157 ? 2.677 3.269 2.350 -0.187 0.452  0.131  157 PRO AAA CA  
4627  C C   . PRO C 157 ? 2.707 3.260 2.364 -0.204 0.451  0.080  157 PRO AAA C   
4628  O O   . PRO C 157 ? 2.631 3.147 2.300 -0.197 0.482  0.073  157 PRO AAA O   
4629  C CB  A PRO C 157 ? 2.767 3.373 2.354 -0.165 0.464  0.140  157 PRO AAA CB  
4630  C CG  A PRO C 157 ? 2.717 3.367 2.301 -0.161 0.435  0.170  157 PRO AAA CG  
4631  C CD  A PRO C 157 ? 2.624 3.288 2.268 -0.184 0.397  0.158  157 PRO AAA CD  
4632  N N   . LYS C 158 ? 2.734 3.295 2.369 -0.226 0.417  0.045  158 LYS AAA N   
4633  C CA  . LYS C 158 ? 2.831 3.347 2.454 -0.246 0.419  -0.003 158 LYS AAA CA  
4634  C C   . LYS C 158 ? 2.769 3.275 2.467 -0.270 0.407  -0.007 158 LYS AAA C   
4635  O O   . LYS C 158 ? 2.872 3.341 2.567 -0.291 0.406  -0.044 158 LYS AAA O   
4636  C CB  . LYS C 158 ? 3.026 3.553 2.580 -0.261 0.389  -0.047 158 LYS AAA CB  
4637  C CG  . LYS C 158 ? 3.080 3.669 2.664 -0.278 0.343  -0.039 158 LYS AAA CG  
4638  C CD  . LYS C 158 ? 3.179 3.821 2.731 -0.252 0.330  -0.002 158 LYS AAA CD  
4639  C CE  . LYS C 158 ? 3.124 3.829 2.715 -0.264 0.285  0.007  158 LYS AAA CE  
4640  N NZ  . LYS C 158 ? 3.239 3.991 2.792 -0.235 0.272  0.045  158 LYS AAA NZ  
4641  N N   . GLU C 159 ? 2.540 3.076 2.300 -0.265 0.399  0.031  159 GLU AAA N   
4642  C CA  . GLU C 159 ? 2.212 2.741 2.034 -0.283 0.389  0.029  159 GLU AAA CA  
4643  C C   . GLU C 159 ? 2.085 2.566 1.937 -0.274 0.418  0.036  159 GLU AAA C   
4644  O O   . GLU C 159 ? 2.028 2.511 1.898 -0.251 0.435  0.065  159 GLU AAA O   
4645  C CB  . GLU C 159 ? 2.100 2.678 1.968 -0.280 0.367  0.062  159 GLU AAA CB  
4646  C CG  . GLU C 159 ? 2.000 2.575 1.924 -0.296 0.358  0.061  159 GLU AAA CG  
4647  C CD  . GLU C 159 ? 1.897 2.516 1.861 -0.288 0.339  0.090  159 GLU AAA CD  
4648  O OE1 . GLU C 159 ? 1.972 2.612 1.930 -0.269 0.337  0.117  159 GLU AAA OE1 
4649  O OE2 . GLU C 159 ? 1.769 2.400 1.771 -0.301 0.328  0.086  159 GLU AAA OE2 
4650  N N   . PRO C 160 ? 2.055 2.493 1.916 -0.290 0.425  0.011  160 PRO AAA N   
4651  C CA  . PRO C 160 ? 2.062 2.457 1.953 -0.277 0.449  0.023  160 PRO AAA CA  
4652  C C   . PRO C 160 ? 1.998 2.421 1.943 -0.265 0.439  0.059  160 PRO AAA C   
4653  O O   . PRO C 160 ? 2.044 2.502 2.011 -0.276 0.417  0.067  160 PRO AAA O   
4654  C CB  . PRO C 160 ? 2.120 2.468 2.011 -0.301 0.453  -0.006 160 PRO AAA CB  
4655  C CG  . PRO C 160 ? 2.176 2.528 2.024 -0.325 0.439  -0.044 160 PRO AAA CG  
4656  C CD  . PRO C 160 ? 2.126 2.549 1.968 -0.321 0.412  -0.029 160 PRO AAA CD  
4657  N N   . PHE C 161 ? 1.819 2.230 1.786 -0.241 0.456  0.079  161 PHE AAA N   
4658  C CA  . PHE C 161 ? 1.675 2.109 1.690 -0.231 0.444  0.109  161 PHE AAA CA  
4659  C C   . PHE C 161 ? 1.589 2.015 1.623 -0.242 0.431  0.106  161 PHE AAA C   
4660  O O   . PHE C 161 ? 1.532 1.988 1.591 -0.243 0.412  0.121  161 PHE AAA O   
4661  C CB  . PHE C 161 ? 1.680 2.100 1.721 -0.206 0.461  0.124  161 PHE AAA CB  
4662  C CG  . PHE C 161 ? 1.615 2.063 1.707 -0.196 0.444  0.149  161 PHE AAA CG  
4663  C CD1 . PHE C 161 ? 1.631 2.115 1.737 -0.202 0.427  0.164  161 PHE AAA CD1 
4664  C CD2 . PHE C 161 ? 1.525 1.958 1.646 -0.179 0.445  0.157  161 PHE AAA CD2 
4665  C CE1 . PHE C 161 ? 1.528 2.028 1.680 -0.194 0.411  0.182  161 PHE AAA CE1 
4666  C CE2 . PHE C 161 ? 1.470 1.927 1.634 -0.171 0.425  0.174  161 PHE AAA CE2 
4667  C CZ  . PHE C 161 ? 1.465 1.952 1.645 -0.180 0.409  0.184  161 PHE AAA CZ  
4668  N N   . ARG C 162 ? 1.623 2.006 1.644 -0.251 0.444  0.089  162 ARG AAA N   
4669  C CA  . ARG C 162 ? 1.558 1.930 1.595 -0.263 0.439  0.090  162 ARG AAA CA  
4670  C C   . ARG C 162 ? 1.505 1.922 1.552 -0.284 0.418  0.085  162 ARG AAA C   
4671  O O   . ARG C 162 ? 1.474 1.910 1.545 -0.282 0.408  0.099  162 ARG AAA O   
4672  C CB  . ARG C 162 ? 1.565 1.877 1.585 -0.273 0.461  0.072  162 ARG AAA CB  
4673  C CG  . ARG C 162 ? 1.490 1.785 1.526 -0.282 0.465  0.079  162 ARG AAA CG  
4674  C CD  . ARG C 162 ? 1.554 1.791 1.576 -0.303 0.488  0.059  162 ARG AAA CD  
4675  N NE  . ARG C 162 ? 1.616 1.796 1.614 -0.283 0.509  0.055  162 ARG AAA NE  
4676  C CZ  . ARG C 162 ? 1.728 1.840 1.708 -0.293 0.534  0.038  162 ARG AAA CZ  
4677  N NH1 . ARG C 162 ? 1.751 1.843 1.739 -0.329 0.539  0.022  162 ARG AAA NH1 
4678  N NH2 . ARG C 162 ? 1.837 1.900 1.796 -0.267 0.554  0.037  162 ARG AAA NH2 
4679  N N   . ASP C 163 ? 1.555 1.992 1.581 -0.302 0.410  0.066  163 ASP AAA N   
4680  C CA  . ASP C 163 ? 1.589 2.078 1.629 -0.320 0.387  0.062  163 ASP AAA CA  
4681  C C   . ASP C 163 ? 1.518 2.054 1.576 -0.301 0.369  0.089  163 ASP AAA C   
4682  O O   . ASP C 163 ? 1.536 2.107 1.621 -0.305 0.355  0.097  163 ASP AAA O   
4683  C CB  . ASP C 163 ? 1.656 2.158 1.664 -0.340 0.377  0.032  163 ASP AAA CB  
4684  C CG  . ASP C 163 ? 1.833 2.282 1.827 -0.364 0.393  -0.000 163 ASP AAA CG  
4685  O OD1 . ASP C 163 ? 1.965 2.381 1.985 -0.372 0.408  0.003  163 ASP AAA OD1 
4686  O OD2 . ASP C 163 ? 1.945 2.382 1.899 -0.374 0.391  -0.029 163 ASP AAA OD2 
4687  N N   . TYR C 164 ? 1.472 2.008 1.518 -0.281 0.373  0.104  164 TYR AAA N   
4688  C CA  . TYR C 164 ? 1.421 1.988 1.487 -0.265 0.359  0.131  164 TYR AAA CA  
4689  C C   . TYR C 164 ? 1.372 1.929 1.473 -0.254 0.357  0.145  164 TYR AAA C   
4690  O O   . TYR C 164 ? 1.329 1.911 1.451 -0.249 0.343  0.156  164 TYR AAA O   
4691  C CB  . TYR C 164 ? 1.456 2.020 1.508 -0.249 0.370  0.145  164 TYR AAA CB  
4692  C CG  . TYR C 164 ? 1.389 1.964 1.475 -0.233 0.365  0.174  164 TYR AAA CG  
4693  C CD1 . TYR C 164 ? 1.442 2.046 1.538 -0.229 0.347  0.190  164 TYR AAA CD1 
4694  C CD2 . TYR C 164 ? 1.372 1.927 1.482 -0.221 0.377  0.184  164 TYR AAA CD2 
4695  C CE1 . TYR C 164 ? 1.512 2.116 1.639 -0.216 0.344  0.214  164 TYR AAA CE1 
4696  C CE2 . TYR C 164 ? 1.344 1.907 1.490 -0.212 0.370  0.206  164 TYR AAA CE2 
4697  C CZ  . TYR C 164 ? 1.456 2.039 1.610 -0.210 0.355  0.220  164 TYR AAA CZ  
4698  O OH  . TYR C 164 ? 1.537 2.118 1.728 -0.203 0.349  0.240  164 TYR AAA OH  
4699  N N   . VAL C 165 ? 1.344 1.862 1.447 -0.247 0.372  0.143  165 VAL AAA N   
4700  C CA  . VAL C 165 ? 1.290 1.795 1.415 -0.234 0.368  0.154  165 VAL AAA CA  
4701  C C   . VAL C 165 ? 1.269 1.781 1.399 -0.243 0.366  0.149  165 VAL AAA C   
4702  O O   . VAL C 165 ? 1.208 1.731 1.353 -0.231 0.356  0.159  165 VAL AAA O   
4703  C CB  . VAL C 165 ? 1.319 1.785 1.440 -0.221 0.382  0.153  165 VAL AAA CB  
4704  C CG1 . VAL C 165 ? 1.378 1.832 1.510 -0.205 0.374  0.162  165 VAL AAA CG1 
4705  C CG2 . VAL C 165 ? 1.390 1.861 1.520 -0.210 0.385  0.161  165 VAL AAA CG2 
4706  N N   . ASP C 166 ? 1.259 1.764 1.379 -0.264 0.376  0.133  166 ASP AAA N   
4707  C CA  . ASP C 166 ? 1.274 1.797 1.411 -0.277 0.377  0.130  166 ASP AAA CA  
4708  C C   . ASP C 166 ? 1.303 1.881 1.460 -0.274 0.357  0.138  166 ASP AAA C   
4709  O O   . ASP C 166 ? 1.350 1.944 1.527 -0.265 0.356  0.147  166 ASP AAA O   
4710  C CB  . ASP C 166 ? 1.304 1.817 1.437 -0.308 0.389  0.108  166 ASP AAA CB  
4711  C CG  . ASP C 166 ? 1.343 1.793 1.462 -0.309 0.415  0.105  166 ASP AAA CG  
4712  O OD1 . ASP C 166 ? 1.307 1.729 1.420 -0.286 0.424  0.122  166 ASP AAA OD1 
4713  O OD2 . ASP C 166 ? 1.415 1.840 1.526 -0.333 0.426  0.085  166 ASP AAA OD2 
4714  N N   . ARG C 167 ? 1.275 1.883 1.426 -0.278 0.342  0.135  167 ARG AAA N   
4715  C CA  . ARG C 167 ? 1.257 1.915 1.425 -0.271 0.323  0.147  167 ARG AAA CA  
4716  C C   . ARG C 167 ? 1.211 1.860 1.389 -0.243 0.318  0.168  167 ARG AAA C   
4717  O O   . ARG C 167 ? 1.243 1.917 1.441 -0.232 0.310  0.177  167 ARG AAA O   
4718  C CB  . ARG C 167 ? 1.309 1.996 1.456 -0.276 0.309  0.143  167 ARG AAA CB  
4719  C CG  . ARG C 167 ? 1.373 2.078 1.513 -0.305 0.305  0.116  167 ARG AAA CG  
4720  C CD  . ARG C 167 ? 1.471 2.216 1.585 -0.306 0.284  0.111  167 ARG AAA CD  
4721  N NE  . ARG C 167 ? 1.578 2.296 1.651 -0.290 0.292  0.121  167 ARG AAA NE  
4722  C CZ  . ARG C 167 ? 1.619 2.354 1.684 -0.267 0.284  0.148  167 ARG AAA CZ  
4723  N NH1 . ARG C 167 ? 1.611 2.385 1.701 -0.255 0.267  0.166  167 ARG AAA NH1 
4724  N NH2 . ARG C 167 ? 1.598 2.310 1.631 -0.256 0.297  0.158  167 ARG AAA NH2 
4725  N N   . PHE C 168 ? 1.134 1.747 1.301 -0.233 0.323  0.173  168 PHE AAA N   
4726  C CA  . PHE C 168 ? 1.181 1.783 1.361 -0.213 0.316  0.188  168 PHE AAA CA  
4727  C C   . PHE C 168 ? 1.265 1.854 1.454 -0.200 0.316  0.187  168 PHE AAA C   
4728  O O   . PHE C 168 ? 1.331 1.930 1.533 -0.186 0.306  0.195  168 PHE AAA O   
4729  C CB  . PHE C 168 ? 1.216 1.787 1.393 -0.208 0.321  0.191  168 PHE AAA CB  
4730  C CG  . PHE C 168 ? 1.337 1.898 1.537 -0.194 0.311  0.204  168 PHE AAA CG  
4731  C CD1 . PHE C 168 ? 1.365 1.901 1.571 -0.182 0.304  0.199  168 PHE AAA CD1 
4732  C CD2 . PHE C 168 ? 1.385 1.956 1.596 -0.191 0.307  0.221  168 PHE AAA CD2 
4733  C CE1 . PHE C 168 ? 1.389 1.913 1.618 -0.172 0.291  0.204  168 PHE AAA CE1 
4734  C CE2 . PHE C 168 ? 1.413 1.969 1.652 -0.182 0.298  0.231  168 PHE AAA CE2 
4735  C CZ  . PHE C 168 ? 1.397 1.929 1.647 -0.174 0.288  0.220  168 PHE AAA CZ  
4736  N N   . TYR C 169 ? 1.278 1.840 1.455 -0.202 0.328  0.179  169 TYR AAA N   
4737  C CA  . TYR C 169 ? 1.266 1.814 1.440 -0.186 0.331  0.180  169 TYR AAA CA  
4738  C C   . TYR C 169 ? 1.297 1.877 1.483 -0.189 0.338  0.180  169 TYR AAA C   
4739  O O   . TYR C 169 ? 1.311 1.887 1.495 -0.169 0.339  0.183  169 TYR AAA O   
4740  C CB  . TYR C 169 ? 1.306 1.815 1.458 -0.182 0.344  0.176  169 TYR AAA CB  
4741  C CG  . TYR C 169 ? 1.336 1.820 1.484 -0.168 0.332  0.176  169 TYR AAA CG  
4742  C CD1 . TYR C 169 ? 1.454 1.927 1.602 -0.148 0.315  0.176  169 TYR AAA CD1 
4743  C CD2 . TYR C 169 ? 1.278 1.752 1.426 -0.176 0.338  0.175  169 TYR AAA CD2 
4744  C CE1 . TYR C 169 ? 1.472 1.931 1.628 -0.139 0.300  0.175  169 TYR AAA CE1 
4745  C CE2 . TYR C 169 ? 1.380 1.841 1.537 -0.163 0.328  0.177  169 TYR AAA CE2 
4746  C CZ  . TYR C 169 ? 1.426 1.883 1.591 -0.147 0.307  0.177  169 TYR AAA CZ  
4747  O OH  . TYR C 169 ? 1.525 1.978 1.710 -0.138 0.293  0.177  169 TYR AAA OH  
4748  N N   . LYS C 170 ? 1.268 1.880 1.467 -0.212 0.342  0.175  170 LYS AAA N   
4749  C CA  . LYS C 170 ? 1.238 1.896 1.464 -0.215 0.345  0.177  170 LYS AAA CA  
4750  C C   . LYS C 170 ? 1.320 2.007 1.561 -0.194 0.328  0.188  170 LYS AAA C   
4751  O O   . LYS C 170 ? 1.345 2.048 1.601 -0.176 0.333  0.193  170 LYS AAA O   
4752  C CB  . LYS C 170 ? 1.180 1.874 1.424 -0.247 0.346  0.166  170 LYS AAA CB  
4753  C CG  . LYS C 170 ? 1.296 2.047 1.582 -0.253 0.349  0.167  170 LYS AAA CG  
4754  C CD  . LYS C 170 ? 1.469 2.249 1.779 -0.291 0.352  0.151  170 LYS AAA CD  
4755  C CE  . LYS C 170 ? 1.556 2.395 1.921 -0.299 0.360  0.155  170 LYS AAA CE  
4756  N NZ  . LYS C 170 ? 1.651 2.514 2.051 -0.342 0.366  0.137  170 LYS AAA NZ  
4757  N N   . THR C 171 ? 1.283 1.974 1.520 -0.193 0.311  0.193  171 THR AAA N   
4758  C CA  . THR C 171 ? 1.204 1.911 1.453 -0.170 0.296  0.207  171 THR AAA CA  
4759  C C   . THR C 171 ? 1.199 1.862 1.441 -0.146 0.297  0.209  171 THR AAA C   
4760  O O   . THR C 171 ? 1.263 1.934 1.516 -0.123 0.295  0.215  171 THR AAA O   
4761  C CB  . THR C 171 ? 1.187 1.898 1.427 -0.174 0.283  0.216  171 THR AAA CB  
4762  O OG1 . THR C 171 ? 1.234 1.986 1.472 -0.194 0.279  0.209  171 THR AAA OG1 
4763  C CG2 . THR C 171 ? 1.400 2.119 1.652 -0.149 0.272  0.235  171 THR AAA CG2 
4764  N N   . LEU C 172 ? 1.193 1.810 1.416 -0.148 0.299  0.203  172 LEU AAA N   
4765  C CA  . LEU C 172 ? 1.270 1.846 1.483 -0.127 0.294  0.199  172 LEU AAA CA  
4766  C C   . LEU C 172 ? 1.401 1.978 1.604 -0.111 0.307  0.193  172 LEU AAA C   
4767  O O   . LEU C 172 ? 1.538 2.097 1.735 -0.086 0.303  0.190  172 LEU AAA O   
4768  C CB  . LEU C 172 ? 1.381 1.920 1.580 -0.133 0.290  0.192  172 LEU AAA CB  
4769  C CG  . LEU C 172 ? 1.542 2.043 1.739 -0.116 0.274  0.185  172 LEU AAA CG  
4770  C CD1 . LEU C 172 ? 1.676 2.173 1.900 -0.116 0.262  0.195  172 LEU AAA CD1 
4771  C CD2 . LEU C 172 ? 1.655 2.136 1.846 -0.122 0.271  0.178  172 LEU AAA CD2 
4772  N N   . ARG C 173 ? 1.350 1.944 1.550 -0.124 0.325  0.191  173 ARG AAA N   
4773  C CA  . ARG C 173 ? 1.264 1.862 1.456 -0.111 0.345  0.190  173 ARG AAA CA  
4774  C C   . ARG C 173 ? 1.347 1.988 1.568 -0.096 0.347  0.197  173 ARG AAA C   
4775  O O   . ARG C 173 ? 1.471 2.102 1.680 -0.069 0.357  0.196  173 ARG AAA O   
4776  C CB  . ARG C 173 ? 1.164 1.771 1.357 -0.134 0.368  0.191  173 ARG AAA CB  
4777  C CG  . ARG C 173 ? 1.330 1.934 1.511 -0.120 0.396  0.195  173 ARG AAA CG  
4778  C CD  . ARG C 173 ? 1.168 1.778 1.359 -0.147 0.422  0.199  173 ARG AAA CD  
4779  N NE  . ARG C 173 ? 1.210 1.804 1.379 -0.129 0.454  0.208  173 ARG AAA NE  
4780  C CZ  . ARG C 173 ? 1.262 1.856 1.441 -0.148 0.486  0.217  173 ARG AAA CZ  
4781  N NH1 . ARG C 173 ? 1.241 1.848 1.453 -0.187 0.489  0.212  173 ARG AAA NH1 
4782  N NH2 . ARG C 173 ? 1.366 1.942 1.518 -0.127 0.519  0.229  173 ARG AAA NH2 
4783  N N   . ALA C 174 ? 1.358 2.046 1.613 -0.110 0.337  0.203  174 ALA AAA N   
4784  C CA  . ALA C 174 ? 1.397 2.134 1.686 -0.093 0.337  0.212  174 ALA AAA CA  
4785  C C   . ALA C 174 ? 1.568 2.272 1.846 -0.059 0.326  0.215  174 ALA AAA C   
4786  O O   . ALA C 174 ? 1.792 2.508 2.080 -0.031 0.335  0.218  174 ALA AAA O   
4787  C CB  . ALA C 174 ? 1.187 1.985 1.510 -0.113 0.323  0.218  174 ALA AAA CB  
4788  N N   . GLU C 175 ? 1.531 2.193 1.792 -0.062 0.308  0.215  175 GLU AAA N   
4789  C CA  . GLU C 175 ? 1.691 2.314 1.947 -0.034 0.297  0.216  175 GLU AAA CA  
4790  C C   . GLU C 175 ? 1.922 2.497 2.144 -0.015 0.305  0.199  175 GLU AAA C   
4791  O O   . GLU C 175 ? 1.907 2.459 2.104 -0.027 0.307  0.188  175 GLU AAA O   
4792  C CB  . GLU C 175 ? 1.787 2.378 2.043 -0.046 0.279  0.222  175 GLU AAA CB  
4793  C CG  . GLU C 175 ? 1.903 2.538 2.178 -0.058 0.273  0.241  175 GLU AAA CG  
4794  C CD  . GLU C 175 ? 2.036 2.639 2.312 -0.063 0.262  0.254  175 GLU AAA CD  
4795  O OE1 . GLU C 175 ? 2.107 2.655 2.378 -0.062 0.258  0.245  175 GLU AAA OE1 
4796  O OE2 . GLU C 175 ? 1.945 2.578 2.226 -0.066 0.257  0.273  175 GLU AAA OE2 
4797  N N   . GLN C 176 ? 2.361 2.921 2.580 0.019  0.309  0.196  176 GLN AAA N   
4798  C CA  . GLN C 176 ? 2.581 3.089 2.757 0.043  0.313  0.175  176 GLN AAA CA  
4799  C C   . GLN C 176 ? 2.681 3.203 2.831 0.040  0.336  0.171  176 GLN AAA C   
4800  O O   . GLN C 176 ? 2.993 3.472 3.095 0.058  0.338  0.156  176 GLN AAA O   
4801  C CB  . GLN C 176 ? 2.758 3.202 2.912 0.037  0.288  0.159  176 GLN AAA CB  
4802  C CG  . GLN C 176 ? 2.821 3.234 3.000 0.039  0.269  0.163  176 GLN AAA CG  
4803  C CD  . GLN C 176 ? 2.899 3.280 3.071 0.077  0.273  0.155  176 GLN AAA CD  
4804  O OE1 . GLN C 176 ? 3.033 3.380 3.164 0.101  0.277  0.132  176 GLN AAA OE1 
4805  N NE2 . GLN C 176 ? 2.847 3.235 3.052 0.085  0.272  0.174  176 GLN AAA NE2 
4806  N N   . ALA C 177 ? 2.506 3.086 2.686 0.019  0.352  0.186  177 ALA AAA N   
4807  C CA  . ALA C 177 ? 2.497 3.093 2.663 0.015  0.381  0.188  177 ALA AAA CA  
4808  C C   . ALA C 177 ? 2.823 3.364 2.935 0.012  0.377  0.177  177 ALA AAA C   
4809  O O   . ALA C 177 ? 3.015 3.533 3.083 0.032  0.396  0.174  177 ALA AAA O   
4810  C CB  . ALA C 177 ? 2.279 2.890 2.440 0.049  0.409  0.190  177 ALA AAA CB  
4811  N N   . SER C 178 ? 2.735 3.257 2.850 -0.010 0.352  0.173  178 SER AAA N   
4812  C CA  . SER C 178 ? 2.762 3.239 2.837 -0.013 0.341  0.164  178 SER AAA CA  
4813  C C   . SER C 178 ? 3.251 3.682 3.286 0.020  0.326  0.145  178 SER AAA C   
4814  O O   . SER C 178 ? 3.784 4.204 3.835 0.029  0.309  0.138  178 SER AAA O   
4815  C CB  . SER C 178 ? 2.517 2.995 2.569 -0.020 0.368  0.172  178 SER AAA CB  
4816  O OG  . SER C 178 ? 2.369 2.810 2.389 -0.022 0.354  0.167  178 SER AAA OG  
4817  N N   . GLN C 179 ? 3.469 3.869 3.446 0.040  0.331  0.137  179 GLN AAA N   
4818  C CA  . GLN C 179 ? 3.505 3.860 3.431 0.075  0.317  0.115  179 GLN AAA CA  
4819  C C   . GLN C 179 ? 3.566 3.893 3.512 0.072  0.279  0.096  179 GLN AAA C   
4820  O O   . GLN C 179 ? 3.693 3.993 3.623 0.097  0.273  0.079  179 GLN AAA O   
4821  C CB  . GLN C 179 ? 3.342 3.706 3.250 0.105  0.347  0.117  179 GLN AAA CB  
4822  C CG  . GLN C 179 ? 3.209 3.604 3.107 0.106  0.391  0.139  179 GLN AAA CG  
4823  C CD  . GLN C 179 ? 3.272 3.633 3.101 0.120  0.398  0.140  179 GLN AAA CD  
4824  O OE1 . GLN C 179 ? 3.156 3.531 2.990 0.102  0.420  0.160  179 GLN AAA OE1 
4825  N NE2 . GLN C 179 ? 3.405 3.719 3.166 0.153  0.378  0.117  179 GLN AAA NE2 
4826  N N   . GLU C 180 ? 3.395 3.727 3.380 0.043  0.257  0.098  180 GLU AAA N   
4827  C CA  . GLU C 180 ? 3.280 3.587 3.295 0.035  0.224  0.084  180 GLU AAA CA  
4828  C C   . GLU C 180 ? 3.139 3.433 3.155 0.021  0.195  0.073  180 GLU AAA C   
4829  O O   . GLU C 180 ? 3.100 3.394 3.078 0.029  0.196  0.071  180 GLU AAA O   
4830  C CB  . GLU C 180 ? 3.289 3.624 3.366 0.012  0.231  0.105  180 GLU AAA CB  
4831  C CG  . GLU C 180 ? 3.310 3.613 3.413 0.017  0.213  0.097  180 GLU AAA CG  
4832  C CD  . GLU C 180 ? 3.439 3.709 3.507 0.052  0.219  0.080  180 GLU AAA CD  
4833  O OE1 . GLU C 180 ? 3.436 3.734 3.488 0.071  0.246  0.090  180 GLU AAA OE1 
4834  O OE2 . GLU C 180 ? 3.510 3.728 3.571 0.062  0.196  0.056  180 GLU AAA OE2 
4835  N N   . VAL C 181 ? 3.066 3.350 3.131 0.002  0.171  0.067  181 VAL AAA N   
4836  C CA  . VAL C 181 ? 2.972 3.254 3.056 -0.013 0.143  0.058  181 VAL AAA CA  
4837  C C   . VAL C 181 ? 3.007 3.328 3.105 -0.030 0.161  0.081  181 VAL AAA C   
4838  O O   . VAL C 181 ? 2.993 3.318 3.074 -0.025 0.151  0.077  181 VAL AAA O   
4839  C CB  . VAL C 181 ? 2.789 3.057 2.935 -0.035 0.120  0.051  181 VAL AAA CB  
4840  C CG1 . VAL C 181 ? 2.741 2.959 2.867 -0.019 0.092  0.016  181 VAL AAA CG1 
4841  C CG2 . VAL C 181 ? 2.572 2.853 2.758 -0.048 0.144  0.077  181 VAL AAA CG2 
4842  N N   . LYS C 182 ? 2.914 3.262 3.043 -0.048 0.185  0.105  182 LYS AAA N   
4843  C CA  . LYS C 182 ? 2.744 3.123 2.883 -0.064 0.205  0.124  182 LYS AAA CA  
4844  C C   . LYS C 182 ? 2.729 3.115 2.901 -0.078 0.189  0.124  182 LYS AAA C   
4845  O O   . LYS C 182 ? 2.651 3.051 2.819 -0.083 0.202  0.133  182 LYS AAA O   
4846  C CB  . LYS C 182 ? 2.685 3.065 2.773 -0.049 0.225  0.127  182 LYS AAA CB  
4847  C CG  . LYS C 182 ? 2.362 2.768 2.458 -0.067 0.255  0.146  182 LYS AAA CG  
4848  C CD  . LYS C 182 ? 2.271 2.699 2.375 -0.071 0.274  0.154  182 LYS AAA CD  
4849  C CE  . LYS C 182 ? 2.192 2.642 2.295 -0.086 0.302  0.166  182 LYS AAA CE  
4850  N NZ  . LYS C 182 ? 2.050 2.482 2.111 -0.072 0.320  0.167  182 LYS AAA NZ  
4851  N N   . ASN C 183 ? 2.709 3.084 2.918 -0.084 0.163  0.112  183 ASN AAA N   
4852  C CA  . ASN C 183 ? 2.637 3.027 2.887 -0.096 0.146  0.111  183 ASN AAA CA  
4853  C C   . ASN C 183 ? 2.435 2.833 2.755 -0.120 0.142  0.119  183 ASN AAA C   
4854  O O   . ASN C 183 ? 2.381 2.806 2.742 -0.135 0.151  0.133  183 ASN AAA O   
4855  C CB  . ASN C 183 ? 2.923 3.296 3.153 -0.078 0.111  0.084  183 ASN AAA CB  
4856  C CG  . ASN C 183 ? 3.099 3.468 3.263 -0.052 0.117  0.083  183 ASN AAA CG  
4857  O OD1 . ASN C 183 ? 3.095 3.479 3.250 -0.054 0.143  0.103  183 ASN AAA OD1 
4858  N ND2 . ASN C 183 ? 3.294 3.637 3.405 -0.027 0.095  0.061  183 ASN AAA ND2 
4859  N N   . ALA C 184 ? 2.441 2.813 2.776 -0.123 0.132  0.112  184 ALA AAA N   
4860  C CA  . ALA C 184 ? 2.424 2.795 2.824 -0.146 0.133  0.125  184 ALA AAA CA  
4861  C C   . ALA C 184 ? 2.429 2.824 2.838 -0.157 0.168  0.158  184 ALA AAA C   
4862  O O   . ALA C 184 ? 2.353 2.770 2.808 -0.175 0.179  0.176  184 ALA AAA O   
4863  C CB  . ALA C 184 ? 2.418 2.744 2.825 -0.144 0.118  0.111  184 ALA AAA CB  
4864  N N   . ALA C 185 ? 2.459 2.855 2.824 -0.146 0.185  0.167  185 ALA AAA N   
4865  C CA  . ALA C 185 ? 2.278 2.701 2.643 -0.154 0.212  0.195  185 ALA AAA CA  
4866  C C   . ALA C 185 ? 2.216 2.670 2.576 -0.162 0.226  0.200  185 ALA AAA C   
4867  O O   . ALA C 185 ? 2.119 2.592 2.493 -0.173 0.245  0.220  185 ALA AAA O   
4868  C CB  . ALA C 185 ? 2.095 2.520 2.419 -0.139 0.222  0.199  185 ALA AAA CB  
4869  N N   . THR C 186 ? 2.314 2.768 2.649 -0.153 0.220  0.184  186 THR AAA N   
4870  C CA  . THR C 186 ? 2.262 2.735 2.587 -0.156 0.235  0.187  186 THR AAA CA  
4871  C C   . THR C 186 ? 2.295 2.784 2.671 -0.166 0.236  0.195  186 THR AAA C   
4872  O O   . THR C 186 ? 2.087 2.595 2.470 -0.174 0.259  0.209  186 THR AAA O   
4873  C CB  . THR C 186 ? 2.311 2.773 2.597 -0.139 0.229  0.172  186 THR AAA CB  
4874  O OG1 . THR C 186 ? 2.258 2.709 2.503 -0.130 0.234  0.168  186 THR AAA OG1 
4875  C CG2 . THR C 186 ? 2.134 2.606 2.407 -0.141 0.248  0.177  186 THR AAA CG2 
4876  N N   . GLU C 187 ? 2.578 3.063 2.994 -0.166 0.210  0.183  187 GLU AAA N   
4877  C CA  . GLU C 187 ? 2.667 3.176 3.148 -0.177 0.209  0.190  187 GLU AAA CA  
4878  C C   . GLU C 187 ? 2.552 3.072 3.074 -0.196 0.232  0.215  187 GLU AAA C   
4879  O O   . GLU C 187 ? 2.531 3.076 3.112 -0.206 0.241  0.226  187 GLU AAA O   
4880  C CB  . GLU C 187 ? 2.876 3.379 3.400 -0.179 0.171  0.170  187 GLU AAA CB  
4881  C CG  . GLU C 187 ? 3.146 3.642 3.634 -0.157 0.143  0.146  187 GLU AAA CG  
4882  C CD  . GLU C 187 ? 3.330 3.843 3.789 -0.141 0.158  0.152  187 GLU AAA CD  
4883  O OE1 . GLU C 187 ? 3.447 3.992 3.955 -0.145 0.166  0.162  187 GLU AAA OE1 
4884  O OE2 . GLU C 187 ? 3.385 3.877 3.775 -0.124 0.164  0.148  187 GLU AAA OE2 
4885  N N   . THR C 188 ? 2.296 2.800 2.787 -0.197 0.244  0.227  188 THR AAA N   
4886  C CA  . THR C 188 ? 2.205 2.710 2.721 -0.209 0.264  0.254  188 THR AAA CA  
4887  C C   . THR C 188 ? 2.117 2.635 2.583 -0.205 0.291  0.272  188 THR AAA C   
4888  O O   . THR C 188 ? 2.055 2.596 2.523 -0.209 0.316  0.287  188 THR AAA O   
4889  C CB  . THR C 188 ? 2.278 2.749 2.812 -0.212 0.249  0.254  188 THR AAA CB  
4890  O OG1 . THR C 188 ? 2.351 2.801 2.832 -0.196 0.233  0.235  188 THR AAA OG1 
4891  C CG2 . THR C 188 ? 2.246 2.708 2.850 -0.226 0.226  0.242  188 THR AAA CG2 
4892  N N   . LEU C 189 ? 2.014 2.520 2.435 -0.196 0.286  0.269  189 LEU AAA N   
4893  C CA  . LEU C 189 ? 2.001 2.521 2.378 -0.193 0.302  0.285  189 LEU AAA CA  
4894  C C   . LEU C 189 ? 1.966 2.507 2.305 -0.193 0.316  0.275  189 LEU AAA C   
4895  O O   . LEU C 189 ? 2.028 2.585 2.338 -0.194 0.333  0.287  189 LEU AAA O   
4896  C CB  . LEU C 189 ? 1.900 2.410 2.250 -0.181 0.289  0.280  189 LEU AAA CB  
4897  C CG  . LEU C 189 ? 1.903 2.385 2.277 -0.176 0.280  0.292  189 LEU AAA CG  
4898  C CD1 . LEU C 189 ? 1.796 2.279 2.139 -0.159 0.271  0.287  189 LEU AAA CD1 
4899  C CD2 . LEU C 189 ? 1.955 2.437 2.347 -0.181 0.298  0.326  189 LEU AAA CD2 
4900  N N   . LEU C 190 ? 1.809 2.346 2.140 -0.190 0.308  0.252  190 LEU AAA N   
4901  C CA  . LEU C 190 ? 1.708 2.253 2.003 -0.192 0.323  0.243  190 LEU AAA CA  
4902  C C   . LEU C 190 ? 1.758 2.316 2.063 -0.195 0.346  0.254  190 LEU AAA C   
4903  O O   . LEU C 190 ? 1.873 2.438 2.139 -0.196 0.363  0.253  190 LEU AAA O   
4904  C CB  . LEU C 190 ? 1.665 2.196 1.952 -0.185 0.315  0.223  190 LEU AAA CB  
4905  C CG  . LEU C 190 ? 1.539 2.064 1.788 -0.185 0.329  0.210  190 LEU AAA CG  
4906  C CD1 . LEU C 190 ? 1.375 1.879 1.617 -0.174 0.319  0.197  190 LEU AAA CD1 
4907  C CD2 . LEU C 190 ? 1.586 2.114 1.832 -0.187 0.351  0.211  190 LEU AAA CD2 
4908  N N   . VAL C 191 ? 1.879 2.441 2.237 -0.196 0.348  0.264  191 VAL AAA N   
4909  C CA  . VAL C 191 ? 1.788 2.368 2.164 -0.197 0.375  0.279  191 VAL AAA CA  
4910  C C   . VAL C 191 ? 1.867 2.455 2.230 -0.200 0.394  0.305  191 VAL AAA C   
4911  O O   . VAL C 191 ? 1.747 2.345 2.074 -0.197 0.419  0.312  191 VAL AAA O   
4912  C CB  . VAL C 191 ? 1.583 2.175 2.032 -0.198 0.372  0.282  191 VAL AAA CB  
4913  C CG1 . VAL C 191 ? 1.455 2.039 1.904 -0.188 0.351  0.258  191 VAL AAA CG1 
4914  C CG2 . VAL C 191 ? 1.840 2.430 2.347 -0.209 0.358  0.295  191 VAL AAA CG2 
4915  N N   . GLN C 192 ? 1.930 2.509 2.315 -0.204 0.382  0.321  192 GLN AAA N   
4916  C CA  . GLN C 192 ? 2.101 2.684 2.474 -0.204 0.401  0.352  192 GLN AAA CA  
4917  C C   . GLN C 192 ? 2.105 2.695 2.399 -0.195 0.404  0.351  192 GLN AAA C   
4918  O O   . GLN C 192 ? 2.316 2.917 2.578 -0.190 0.426  0.372  192 GLN AAA O   
4919  C CB  . GLN C 192 ? 2.187 2.748 2.597 -0.208 0.386  0.367  192 GLN AAA CB  
4920  C CG  . GLN C 192 ? 2.438 2.996 2.919 -0.219 0.404  0.394  192 GLN AAA CG  
4921  C CD  . GLN C 192 ? 2.568 3.136 3.118 -0.230 0.394  0.375  192 GLN AAA CD  
4922  O OE1 . GLN C 192 ? 2.632 3.187 3.197 -0.231 0.361  0.348  192 GLN AAA OE1 
4923  N NE2 . GLN C 192 ? 2.665 3.259 3.255 -0.235 0.422  0.390  192 GLN AAA NE2 
4924  N N   . ASN C 193 ? 1.981 2.569 2.245 -0.194 0.381  0.326  193 ASN AAA N   
4925  C CA  . ASN C 193 ? 1.961 2.564 2.163 -0.190 0.377  0.318  193 ASN AAA CA  
4926  C C   . ASN C 193 ? 1.946 2.554 2.108 -0.194 0.389  0.295  193 ASN AAA C   
4927  O O   . ASN C 193 ? 1.844 2.465 1.956 -0.195 0.383  0.282  193 ASN AAA O   
4928  C CB  . ASN C 193 ? 2.020 2.623 2.220 -0.189 0.350  0.306  193 ASN AAA CB  
4929  C CG  . ASN C 193 ? 2.094 2.690 2.316 -0.180 0.340  0.330  193 ASN AAA CG  
4930  O OD1 . ASN C 193 ? 2.095 2.694 2.306 -0.173 0.351  0.360  193 ASN AAA OD1 
4931  N ND2 . ASN C 193 ? 2.052 2.634 2.300 -0.177 0.322  0.319  193 ASN AAA ND2 
4932  N N   . ALA C 194 ? 2.097 2.696 2.283 -0.195 0.404  0.287  194 ALA AAA N   
4933  C CA  . ALA C 194 ? 2.171 2.765 2.321 -0.195 0.421  0.266  194 ALA AAA CA  
4934  C C   . ALA C 194 ? 2.357 2.962 2.461 -0.188 0.445  0.279  194 ALA AAA C   
4935  O O   . ALA C 194 ? 2.459 3.076 2.568 -0.182 0.454  0.310  194 ALA AAA O   
4936  C CB  . ALA C 194 ? 2.171 2.755 2.364 -0.191 0.432  0.261  194 ALA AAA CB  
4937  N N   . ASN C 195 ? 2.416 3.013 2.470 -0.187 0.457  0.254  195 ASN AAA N   
4938  C CA  . ASN C 195 ? 2.621 3.225 2.616 -0.177 0.480  0.260  195 ASN AAA CA  
4939  C C   . ASN C 195 ? 2.736 3.344 2.761 -0.165 0.518  0.284  195 ASN AAA C   
4940  O O   . ASN C 195 ? 2.728 3.334 2.820 -0.166 0.523  0.287  195 ASN AAA O   
4941  C CB  . ASN C 195 ? 2.735 3.321 2.669 -0.182 0.479  0.218  195 ASN AAA CB  
4942  C CG  . ASN C 195 ? 3.035 3.614 2.908 -0.168 0.511  0.211  195 ASN AAA CG  
4943  O OD1 . ASN C 195 ? 3.335 3.928 3.150 -0.160 0.514  0.220  195 ASN AAA OD1 
4944  N ND2 . ASN C 195 ? 3.071 3.624 2.952 -0.162 0.535  0.194  195 ASN AAA ND2 
4945  N N   . PRO C 196 ? 2.778 3.396 2.757 -0.152 0.545  0.302  196 PRO AAA N   
4946  C CA  A PRO C 196 ? 2.775 3.403 2.795 -0.141 0.586  0.333  196 PRO AAA CA  
4947  C C   . PRO C 196 ? 2.790 3.412 2.836 -0.133 0.610  0.316  196 PRO AAA C   
4948  O O   . PRO C 196 ? 2.753 3.390 2.882 -0.133 0.624  0.334  196 PRO AAA O   
4949  C CB  A PRO C 196 ? 2.721 3.357 2.665 -0.125 0.612  0.355  196 PRO AAA CB  
4950  C CG  A PRO C 196 ? 2.639 3.276 2.518 -0.129 0.575  0.343  196 PRO AAA CG  
4951  C CD  A PRO C 196 ? 2.761 3.390 2.673 -0.148 0.533  0.313  196 PRO AAA CD  
4952  N N   . ASP C 197 ? 2.867 3.466 2.847 -0.126 0.616  0.280  197 ASP AAA N   
4953  C CA  . ASP C 197 ? 2.936 3.522 2.938 -0.114 0.640  0.263  197 ASP AAA CA  
4954  C C   . ASP C 197 ? 2.809 3.389 2.885 -0.123 0.614  0.254  197 ASP AAA C   
4955  O O   . ASP C 197 ? 2.978 3.569 3.118 -0.112 0.630  0.262  197 ASP AAA O   
4956  C CB  . ASP C 197 ? 3.117 3.668 3.027 -0.106 0.650  0.223  197 ASP AAA CB  
4957  C CG  . ASP C 197 ? 3.397 3.954 3.232 -0.087 0.685  0.231  197 ASP AAA CG  
4958  O OD1 . ASP C 197 ? 3.516 4.096 3.327 -0.089 0.681  0.258  197 ASP AAA OD1 
4959  O OD2 . ASP C 197 ? 3.565 4.101 3.360 -0.068 0.719  0.211  197 ASP AAA OD2 
4960  N N   . CYS C 198 ? 2.604 3.171 2.671 -0.141 0.574  0.239  198 CYS AAA N   
4961  C CA  . CYS C 198 ? 2.442 3.002 2.567 -0.147 0.549  0.232  198 CYS AAA CA  
4962  C C   . CYS C 198 ? 2.298 2.888 2.507 -0.151 0.538  0.262  198 CYS AAA C   
4963  O O   . CYS C 198 ? 2.131 2.725 2.399 -0.146 0.531  0.261  198 CYS AAA O   
4964  C CB  . CYS C 198 ? 2.413 2.953 2.504 -0.164 0.515  0.210  198 CYS AAA CB  
4965  S SG  . CYS C 198 ? 2.351 2.844 2.377 -0.166 0.521  0.167  198 CYS AAA SG  
4966  N N   . LYS C 199 ? 2.222 2.831 2.437 -0.158 0.536  0.286  199 LYS AAA N   
4967  C CA  . LYS C 199 ? 2.210 2.838 2.506 -0.166 0.526  0.311  199 LYS AAA CA  
4968  C C   . LYS C 199 ? 2.296 2.950 2.665 -0.158 0.551  0.325  199 LYS AAA C   
4969  O O   . LYS C 199 ? 2.201 2.868 2.646 -0.163 0.531  0.327  199 LYS AAA O   
4970  C CB  . LYS C 199 ? 2.182 2.818 2.467 -0.172 0.530  0.340  199 LYS AAA CB  
4971  C CG  . LYS C 199 ? 2.071 2.714 2.436 -0.184 0.515  0.363  199 LYS AAA CG  
4972  C CD  . LYS C 199 ? 2.086 2.729 2.436 -0.186 0.529  0.397  199 LYS AAA CD  
4973  C CE  . LYS C 199 ? 2.151 2.779 2.431 -0.184 0.503  0.389  199 LYS AAA CE  
4974  N NZ  . LYS C 199 ? 2.168 2.791 2.447 -0.184 0.507  0.425  199 LYS AAA NZ  
4975  N N   . THR C 200 ? 2.396 3.061 2.745 -0.144 0.593  0.335  200 THR AAA N   
4976  C CA  . THR C 200 ? 2.285 2.982 2.708 -0.133 0.622  0.349  200 THR AAA CA  
4977  C C   . THR C 200 ? 2.228 2.922 2.682 -0.122 0.604  0.325  200 THR AAA C   
4978  O O   . THR C 200 ? 2.169 2.895 2.714 -0.121 0.598  0.334  200 THR AAA O   
4979  C CB  . THR C 200 ? 2.413 3.116 2.789 -0.114 0.675  0.359  200 THR AAA CB  
4980  O OG1 . THR C 200 ? 2.435 3.103 2.729 -0.099 0.679  0.325  200 THR AAA OG1 
4981  C CG2 . THR C 200 ? 2.485 3.187 2.811 -0.120 0.690  0.385  200 THR AAA CG2 
4982  N N   . ILE C 201 ? 2.298 2.951 2.678 -0.115 0.595  0.295  201 ILE AAA N   
4983  C CA  . ILE C 201 ? 2.204 2.845 2.603 -0.102 0.580  0.276  201 ILE AAA CA  
4984  C C   . ILE C 201 ? 2.118 2.766 2.567 -0.114 0.534  0.275  201 ILE AAA C   
4985  O O   . ILE C 201 ? 2.083 2.751 2.595 -0.103 0.521  0.276  201 ILE AAA O   
4986  C CB  . ILE C 201 ? 2.135 2.723 2.443 -0.096 0.584  0.246  201 ILE AAA CB  
4987  C CG1 . ILE C 201 ? 2.468 3.044 2.724 -0.079 0.629  0.240  201 ILE AAA CG1 
4988  C CG2 . ILE C 201 ? 2.077 2.642 2.397 -0.084 0.566  0.231  201 ILE AAA CG2 
4989  C CD1 . ILE C 201 ? 2.379 2.899 2.538 -0.083 0.629  0.206  201 ILE AAA CD1 
4990  N N   . LEU C 202 ? 2.074 2.706 2.494 -0.134 0.508  0.272  202 LEU AAA N   
4991  C CA  . LEU C 202 ? 2.080 2.712 2.535 -0.142 0.466  0.267  202 LEU AAA CA  
4992  C C   . LEU C 202 ? 2.206 2.877 2.756 -0.150 0.456  0.285  202 LEU AAA C   
4993  O O   . LEU C 202 ? 2.114 2.796 2.711 -0.147 0.425  0.277  202 LEU AAA O   
4994  C CB  . LEU C 202 ? 1.973 2.581 2.377 -0.158 0.446  0.261  202 LEU AAA CB  
4995  C CG  . LEU C 202 ? 2.009 2.581 2.332 -0.158 0.448  0.240  202 LEU AAA CG  
4996  C CD1 . LEU C 202 ? 2.017 2.582 2.308 -0.173 0.429  0.239  202 LEU AAA CD1 
4997  C CD2 . LEU C 202 ? 1.932 2.481 2.250 -0.146 0.435  0.224  202 LEU AAA CD2 
4998  N N   . LYS C 203 ? 2.208 2.901 2.786 -0.160 0.482  0.309  203 LYS AAA N   
4999  C CA  . LYS C 203 ? 1.957 2.689 2.637 -0.172 0.479  0.328  203 LYS AAA CA  
5000  C C   . LYS C 203 ? 2.009 2.782 2.763 -0.157 0.483  0.327  203 LYS AAA C   
5001  O O   . LYS C 203 ? 2.024 2.826 2.863 -0.165 0.454  0.326  203 LYS AAA O   
5002  C CB  . LYS C 203 ? 2.002 2.744 2.688 -0.181 0.518  0.360  203 LYS AAA CB  
5003  C CG  . LYS C 203 ? 1.949 2.661 2.592 -0.197 0.506  0.368  203 LYS AAA CG  
5004  C CD  . LYS C 203 ? 2.168 2.887 2.801 -0.199 0.549  0.404  203 LYS AAA CD  
5005  C CE  . LYS C 203 ? 2.130 2.879 2.871 -0.215 0.566  0.434  203 LYS AAA CE  
5006  N NZ  . LYS C 203 ? 2.166 2.898 2.962 -0.237 0.526  0.429  203 LYS AAA NZ  
5007  N N   . ALA C 204 ? 2.030 2.804 2.751 -0.134 0.516  0.326  204 ALA AAA N   
5008  C CA  . ALA C 204 ? 2.192 3.007 2.977 -0.111 0.527  0.327  204 ALA AAA CA  
5009  C C   . ALA C 204 ? 2.159 2.966 2.949 -0.097 0.484  0.305  204 ALA AAA C   
5010  O O   . ALA C 204 ? 2.318 3.168 3.181 -0.080 0.477  0.308  204 ALA AAA O   
5011  C CB  . ALA C 204 ? 2.358 3.162 3.090 -0.086 0.577  0.328  204 ALA AAA CB  
5012  N N   . LEU C 205 ? 2.133 2.891 2.849 -0.101 0.454  0.286  205 LEU AAA N   
5013  C CA  . LEU C 205 ? 2.092 2.838 2.800 -0.084 0.418  0.270  205 LEU AAA CA  
5014  C C   . LEU C 205 ? 2.067 2.856 2.863 -0.089 0.374  0.268  205 LEU AAA C   
5015  O O   . LEU C 205 ? 2.034 2.834 2.842 -0.066 0.348  0.260  205 LEU AAA O   
5016  C CB  . LEU C 205 ? 2.189 2.875 2.803 -0.090 0.401  0.253  205 LEU AAA CB  
5017  C CG  . LEU C 205 ? 2.307 2.946 2.834 -0.083 0.434  0.246  205 LEU AAA CG  
5018  C CD1 . LEU C 205 ? 2.431 3.023 2.886 -0.093 0.415  0.232  205 LEU AAA CD1 
5019  C CD2 . LEU C 205 ? 2.292 2.924 2.817 -0.050 0.452  0.244  205 LEU AAA CD2 
5020  N N   . GLY C 206 ? 2.146 2.958 3.000 -0.118 0.362  0.274  206 GLY AAA N   
5021  C CA  . GLY C 206 ? 2.268 3.120 3.207 -0.124 0.316  0.266  206 GLY AAA CA  
5022  C C   . GLY C 206 ? 2.375 3.189 3.268 -0.131 0.268  0.244  206 GLY AAA C   
5023  O O   . GLY C 206 ? 2.393 3.152 3.194 -0.131 0.272  0.237  206 GLY AAA O   
5024  N N   . PRO C 207 ? 2.497 3.341 3.455 -0.135 0.220  0.229  207 PRO AAA N   
5025  C CA  . PRO C 207 ? 2.482 3.286 3.390 -0.138 0.175  0.205  207 PRO AAA CA  
5026  C C   . PRO C 207 ? 2.516 3.291 3.335 -0.103 0.162  0.194  207 PRO AAA C   
5027  O O   . PRO C 207 ? 2.657 3.452 3.479 -0.075 0.171  0.202  207 PRO AAA O   
5028  C CB  . PRO C 207 ? 2.519 3.370 3.527 -0.151 0.127  0.190  207 PRO AAA CB  
5029  C CG  . PRO C 207 ? 2.595 3.517 3.688 -0.137 0.138  0.204  207 PRO AAA CG  
5030  C CD  . PRO C 207 ? 2.608 3.525 3.683 -0.134 0.204  0.232  207 PRO AAA CD  
5031  N N   . GLY C 208 ? 2.547 3.270 3.287 -0.103 0.146  0.180  208 GLY AAA N   
5032  C CA  . GLY C 208 ? 2.534 3.224 3.188 -0.072 0.136  0.172  208 GLY AAA CA  
5033  C C   . GLY C 208 ? 2.493 3.151 3.084 -0.064 0.184  0.188  208 GLY AAA C   
5034  O O   . GLY C 208 ? 2.723 3.405 3.346 -0.056 0.213  0.202  208 GLY AAA O   
5035  N N   . ALA C 209 ? 2.310 2.919 2.823 -0.068 0.198  0.185  209 ALA AAA N   
5036  C CA  . ALA C 209 ? 2.251 2.834 2.715 -0.062 0.241  0.196  209 ALA AAA CA  
5037  C C   . ALA C 209 ? 2.303 2.835 2.680 -0.052 0.242  0.190  209 ALA AAA C   
5038  O O   . ALA C 209 ? 2.466 2.982 2.817 -0.065 0.231  0.182  209 ALA AAA O   
5039  C CB  . ALA C 209 ? 2.046 2.631 2.519 -0.088 0.274  0.204  209 ALA AAA CB  
5040  N N   . THR C 210 ? 2.209 2.715 2.545 -0.030 0.261  0.196  210 THR AAA N   
5041  C CA  . THR C 210 ? 2.093 2.552 2.354 -0.025 0.269  0.195  210 THR AAA CA  
5042  C C   . THR C 210 ? 1.982 2.422 2.222 -0.053 0.303  0.195  210 THR AAA C   
5043  O O   . THR C 210 ? 2.037 2.492 2.304 -0.065 0.323  0.197  210 THR AAA O   
5044  C CB  . THR C 210 ? 2.114 2.544 2.337 0.009  0.276  0.204  210 THR AAA CB  
5045  O OG1 . THR C 210 ? 2.300 2.765 2.559 0.035  0.242  0.205  210 THR AAA OG1 
5046  C CG2 . THR C 210 ? 1.974 2.361 2.124 0.017  0.278  0.205  210 THR AAA CG2 
5047  N N   . LEU C 211 ? 1.836 2.248 2.028 -0.061 0.309  0.191  211 LEU AAA N   
5048  C CA  . LEU C 211 ? 1.770 2.172 1.947 -0.087 0.337  0.189  211 LEU AAA CA  
5049  C C   . LEU C 211 ? 1.840 2.213 2.001 -0.082 0.368  0.191  211 LEU AAA C   
5050  O O   . LEU C 211 ? 1.949 2.326 2.116 -0.098 0.388  0.187  211 LEU AAA O   
5051  C CB  . LEU C 211 ? 1.771 2.156 1.911 -0.097 0.339  0.186  211 LEU AAA CB  
5052  C CG  . LEU C 211 ? 1.717 2.103 1.849 -0.126 0.360  0.181  211 LEU AAA CG  
5053  C CD1 . LEU C 211 ? 1.489 1.884 1.611 -0.135 0.352  0.179  211 LEU AAA CD1 
5054  C CD2 . LEU C 211 ? 1.795 2.145 1.900 -0.132 0.389  0.179  211 LEU AAA CD2 
5055  N N   . GLU C 212 ? 1.862 2.203 1.997 -0.057 0.374  0.198  212 GLU AAA N   
5056  C CA  . GLU C 212 ? 1.960 2.262 2.078 -0.046 0.404  0.201  212 GLU AAA CA  
5057  C C   . GLU C 212 ? 2.083 2.407 2.239 -0.038 0.412  0.201  212 GLU AAA C   
5058  O O   . GLU C 212 ? 2.171 2.472 2.316 -0.046 0.442  0.194  212 GLU AAA O   
5059  C CB  . GLU C 212 ? 2.058 2.326 2.146 -0.011 0.402  0.216  212 GLU AAA CB  
5060  C CG  . GLU C 212 ? 2.233 2.486 2.282 -0.006 0.390  0.221  212 GLU AAA CG  
5061  C CD  . GLU C 212 ? 2.342 2.556 2.350 0.033  0.394  0.240  212 GLU AAA CD  
5062  O OE1 . GLU C 212 ? 2.350 2.529 2.352 0.049  0.417  0.249  212 GLU AAA OE1 
5063  O OE2 . GLU C 212 ? 2.363 2.578 2.341 0.051  0.374  0.246  212 GLU AAA OE2 
5064  N N   . GLU C 213 ? 2.157 2.528 2.362 -0.022 0.388  0.207  213 GLU AAA N   
5065  C CA  . GLU C 213 ? 2.092 2.493 2.344 -0.012 0.400  0.210  213 GLU AAA CA  
5066  C C   . GLU C 213 ? 2.046 2.467 2.311 -0.041 0.417  0.203  213 GLU AAA C   
5067  O O   . GLU C 213 ? 2.187 2.602 2.452 -0.037 0.447  0.201  213 GLU AAA O   
5068  C CB  . GLU C 213 ? 2.151 2.607 2.465 0.006  0.366  0.218  213 GLU AAA CB  
5069  C CG  . GLU C 213 ? 2.320 2.768 2.625 0.045  0.348  0.226  213 GLU AAA CG  
5070  C CD  . GLU C 213 ? 2.431 2.938 2.793 0.055  0.303  0.226  213 GLU AAA CD  
5071  O OE1 . GLU C 213 ? 2.391 2.939 2.804 0.029  0.289  0.220  213 GLU AAA OE1 
5072  O OE2 . GLU C 213 ? 2.572 3.083 2.931 0.090  0.280  0.233  213 GLU AAA OE2 
5073  N N   . MET C 214 ? 1.784 2.227 2.056 -0.066 0.399  0.200  214 MET AAA N   
5074  C CA  . MET C 214 ? 1.771 2.231 2.045 -0.090 0.414  0.198  214 MET AAA CA  
5075  C C   . MET C 214 ? 1.800 2.221 2.017 -0.103 0.441  0.185  214 MET AAA C   
5076  O O   . MET C 214 ? 2.017 2.442 2.227 -0.108 0.464  0.182  214 MET AAA O   
5077  C CB  A MET C 214 ? 1.655 2.143 1.951 -0.109 0.388  0.201  214 MET AAA CB  
5078  C CG  A MET C 214 ? 1.770 2.239 2.035 -0.116 0.367  0.195  214 MET AAA CG  
5079  S SD  A MET C 214 ? 1.757 2.260 2.062 -0.131 0.340  0.200  214 MET AAA SD  
5080  C CE  A MET C 214 ? 1.869 2.374 2.146 -0.154 0.359  0.201  214 MET AAA CE  
5081  N N   . MET C 215 ? 1.725 2.108 1.901 -0.110 0.439  0.177  215 MET AAA N   
5082  C CA  . MET C 215 ? 1.789 2.136 1.918 -0.128 0.461  0.160  215 MET AAA CA  
5083  C C   . MET C 215 ? 1.959 2.268 2.072 -0.112 0.491  0.153  215 MET AAA C   
5084  O O   . MET C 215 ? 2.158 2.450 2.241 -0.125 0.510  0.136  215 MET AAA O   
5085  C CB  . MET C 215 ? 1.815 2.133 1.917 -0.142 0.456  0.155  215 MET AAA CB  
5086  C CG  . MET C 215 ? 1.683 2.032 1.792 -0.159 0.432  0.158  215 MET AAA CG  
5087  S SD  . MET C 215 ? 1.649 1.965 1.730 -0.175 0.439  0.152  215 MET AAA SD  
5088  C CE  . MET C 215 ? 1.755 2.045 1.811 -0.202 0.462  0.128  215 MET AAA CE  
5089  N N   . THR C 216 ? 1.995 2.289 2.123 -0.082 0.494  0.164  216 THR AAA N   
5090  C CA  . THR C 216 ? 2.197 2.454 2.314 -0.059 0.525  0.160  216 THR AAA CA  
5091  C C   . THR C 216 ? 2.318 2.614 2.459 -0.053 0.540  0.160  216 THR AAA C   
5092  O O   . THR C 216 ? 2.452 2.717 2.561 -0.051 0.570  0.144  216 THR AAA O   
5093  C CB  . THR C 216 ? 2.210 2.454 2.344 -0.022 0.521  0.178  216 THR AAA CB  
5094  O OG1 . THR C 216 ? 2.252 2.456 2.354 -0.026 0.512  0.182  216 THR AAA OG1 
5095  C CG2 . THR C 216 ? 2.347 2.549 2.471 0.007  0.555  0.176  216 THR AAA CG2 
5096  N N   . ALA C 217 ? 2.263 2.622 2.458 -0.049 0.522  0.176  217 ALA AAA N   
5097  C CA  . ALA C 217 ? 2.203 2.605 2.431 -0.043 0.540  0.183  217 ALA AAA CA  
5098  C C   . ALA C 217 ? 2.168 2.562 2.348 -0.066 0.557  0.168  217 ALA AAA C   
5099  O O   . ALA C 217 ? 2.376 2.769 2.543 -0.054 0.589  0.164  217 ALA AAA O   
5100  C CB  . ALA C 217 ? 2.008 2.476 2.307 -0.046 0.514  0.202  217 ALA AAA CB  
5101  N N   . CYS C 218 ? 2.037 2.427 2.189 -0.095 0.537  0.160  218 CYS AAA N   
5102  C CA  . CYS C 218 ? 2.121 2.513 2.227 -0.117 0.542  0.148  218 CYS AAA CA  
5103  C C   . CYS C 218 ? 2.244 2.579 2.286 -0.129 0.553  0.117  218 CYS AAA C   
5104  O O   . CYS C 218 ? 2.382 2.718 2.382 -0.150 0.550  0.101  218 CYS AAA O   
5105  C CB  . CYS C 218 ? 2.041 2.466 2.159 -0.140 0.512  0.157  218 CYS AAA CB  
5106  S SG  . CYS C 218 ? 1.944 2.429 2.130 -0.135 0.504  0.189  218 CYS AAA SG  
5107  N N   . GLN C 219 ? 2.304 2.587 2.338 -0.116 0.566  0.109  219 GLN AAA N   
5108  C CA  . GLN C 219 ? 2.392 2.612 2.372 -0.129 0.580  0.078  219 GLN AAA CA  
5109  C C   . GLN C 219 ? 2.551 2.751 2.490 -0.118 0.610  0.059  219 GLN AAA C   
5110  O O   . GLN C 219 ? 2.732 2.932 2.625 -0.138 0.608  0.036  219 GLN AAA O   
5111  C CB  . GLN C 219 ? 2.361 2.523 2.345 -0.113 0.591  0.081  219 GLN AAA CB  
5112  C CG  . GLN C 219 ? 2.408 2.553 2.399 -0.128 0.572  0.088  219 GLN AAA CG  
5113  C CD  . GLN C 219 ? 2.387 2.479 2.381 -0.099 0.588  0.100  219 GLN AAA CD  
5114  O OE1 . GLN C 219 ? 2.393 2.464 2.389 -0.067 0.610  0.102  219 GLN AAA OE1 
5115  N NE2 . GLN C 219 ? 2.244 2.316 2.238 -0.105 0.578  0.111  219 GLN AAA NE2 
5116  N N   . ASP D 1   ? 1.939 2.165 1.552 -0.326 -0.272 0.061  1   ASP FFF N   
5117  C CA  . ASP D 1   ? 1.892 2.072 1.554 -0.303 -0.277 0.061  1   ASP FFF CA  
5118  C C   . ASP D 1   ? 1.773 1.949 1.429 -0.307 -0.294 0.041  1   ASP FFF C   
5119  O O   . ASP D 1   ? 1.788 2.009 1.440 -0.299 -0.302 0.057  1   ASP FFF O   
5120  C CB  . ASP D 1   ? 1.830 1.946 1.522 -0.303 -0.266 0.044  1   ASP FFF CB  
5121  C CG  . ASP D 1   ? 1.928 2.006 1.674 -0.278 -0.266 0.058  1   ASP FFF CG  
5122  O OD1 . ASP D 1   ? 1.981 2.077 1.738 -0.259 -0.269 0.081  1   ASP FFF OD1 
5123  O OD2 . ASP D 1   ? 1.987 2.017 1.765 -0.279 -0.263 0.045  1   ASP FFF OD2 
5124  N N   . VAL D 2   ? 1.705 1.831 1.362 -0.318 -0.297 0.010  2   VAL FFF N   
5125  C CA  . VAL D 2   ? 1.713 1.827 1.361 -0.323 -0.310 -0.010 2   VAL FFF CA  
5126  C C   . VAL D 2   ? 1.677 1.789 1.285 -0.354 -0.309 -0.036 2   VAL FFF C   
5127  O O   . VAL D 2   ? 1.595 1.668 1.201 -0.363 -0.299 -0.052 2   VAL FFF O   
5128  C CB  . VAL D 2   ? 1.763 1.816 1.444 -0.307 -0.317 -0.023 2   VAL FFF CB  
5129  C CG1 . VAL D 2   ? 1.684 1.727 1.348 -0.311 -0.329 -0.041 2   VAL FFF CG1 
5130  C CG2 . VAL D 2   ? 1.919 1.964 1.636 -0.279 -0.316 -0.000 2   VAL FFF CG2 
5131  N N   . GLN D 3   ? 1.726 1.878 1.304 -0.371 -0.318 -0.039 3   GLN FFF N   
5132  C CA  . GLN D 3   ? 1.779 1.927 1.315 -0.405 -0.316 -0.064 3   GLN FFF CA  
5133  C C   . GLN D 3   ? 1.760 1.888 1.292 -0.411 -0.325 -0.080 3   GLN FFF C   
5134  O O   . GLN D 3   ? 1.679 1.836 1.223 -0.399 -0.335 -0.068 3   GLN FFF O   
5135  C CB  . GLN D 3   ? 1.752 1.969 1.251 -0.429 -0.318 -0.055 3   GLN FFF CB  
5136  C CG  . GLN D 3   ? 1.760 1.998 1.253 -0.425 -0.308 -0.037 3   GLN FFF CG  
5137  C CD  . GLN D 3   ? 1.857 2.042 1.330 -0.437 -0.290 -0.060 3   GLN FFF CD  
5138  O OE1 . GLN D 3   ? 1.816 1.969 1.258 -0.462 -0.285 -0.089 3   GLN FFF OE1 
5139  N NE2 . GLN D 3   ? 1.942 2.116 1.435 -0.418 -0.276 -0.044 3   GLN FFF NE2 
5140  N N   . LEU D 4   ? 1.762 1.839 1.275 -0.428 -0.319 -0.107 4   LEU FFF N   
5141  C CA  . LEU D 4   ? 1.970 2.022 1.473 -0.437 -0.325 -0.122 4   LEU FFF CA  
5142  C C   . LEU D 4   ? 2.181 2.228 1.639 -0.476 -0.317 -0.143 4   LEU FFF C   
5143  O O   . LEU D 4   ? 2.240 2.266 1.677 -0.489 -0.304 -0.155 4   LEU FFF O   
5144  C CB  . LEU D 4   ? 1.990 1.974 1.516 -0.417 -0.324 -0.133 4   LEU FFF CB  
5145  C CG  . LEU D 4   ? 1.964 1.935 1.532 -0.383 -0.333 -0.121 4   LEU FFF CG  
5146  C CD1 . LEU D 4   ? 1.938 1.846 1.524 -0.372 -0.335 -0.134 4   LEU FFF CD1 
5147  C CD2 . LEU D 4   ? 1.959 1.958 1.528 -0.372 -0.345 -0.110 4   LEU FFF CD2 
5148  N N   . GLN D 5   ? 2.417 2.479 1.858 -0.494 -0.323 -0.148 5   GLN FFF N   
5149  C CA  . GLN D 5   ? 2.562 2.609 1.960 -0.535 -0.316 -0.170 5   GLN FFF CA  
5150  C C   . GLN D 5   ? 2.574 2.595 1.969 -0.541 -0.318 -0.177 5   GLN FFF C   
5151  O O   . GLN D 5   ? 2.495 2.560 1.904 -0.536 -0.329 -0.162 5   GLN FFF O   
5152  C CB  . GLN D 5   ? 2.656 2.776 2.028 -0.567 -0.322 -0.164 5   GLN FFF CB  
5153  C CG  . GLN D 5   ? 2.965 3.065 2.287 -0.615 -0.315 -0.191 5   GLN FFF CG  
5154  C CD  . GLN D 5   ? 3.089 3.107 2.386 -0.618 -0.293 -0.216 5   GLN FFF CD  
5155  O OE1 . GLN D 5   ? 3.177 3.197 2.463 -0.615 -0.285 -0.216 5   GLN FFF OE1 
5156  N NE2 . GLN D 5   ? 3.085 3.032 2.374 -0.623 -0.282 -0.234 5   GLN FFF NE2 
5157  N N   . GLU D 6   ? 2.596 2.546 1.973 -0.551 -0.305 -0.198 6   GLU FFF N   
5158  C CA  . GLU D 6   ? 2.537 2.462 1.905 -0.560 -0.305 -0.202 6   GLU FFF CA  
5159  C C   . GLU D 6   ? 2.547 2.502 1.881 -0.608 -0.303 -0.211 6   GLU FFF C   
5160  O O   . GLU D 6   ? 2.595 2.568 1.902 -0.637 -0.300 -0.222 6   GLU FFF O   
5161  C CB  . GLU D 6   ? 2.589 2.426 1.950 -0.552 -0.291 -0.218 6   GLU FFF CB  
5162  C CG  . GLU D 6   ? 2.545 2.352 1.943 -0.511 -0.294 -0.211 6   GLU FFF CG  
5163  C CD  . GLU D 6   ? 2.565 2.361 1.967 -0.506 -0.283 -0.216 6   GLU FFF CD  
5164  O OE1 . GLU D 6   ? 2.663 2.497 2.044 -0.528 -0.280 -0.218 6   GLU FFF OE1 
5165  O OE2 . GLU D 6   ? 2.555 2.309 1.981 -0.482 -0.278 -0.216 6   GLU FFF OE2 
5166  N N   . SER D 7   ? 2.463 2.423 1.796 -0.618 -0.306 -0.208 7   SER FFF N   
5167  C CA  . SER D 7   ? 2.537 2.520 1.842 -0.669 -0.303 -0.217 7   SER FFF CA  
5168  C C   . SER D 7   ? 2.610 2.575 1.917 -0.672 -0.300 -0.211 7   SER FFF C   
5169  O O   . SER D 7   ? 2.690 2.639 2.020 -0.634 -0.303 -0.198 7   SER FFF O   
5170  C CB  . SER D 7   ? 2.572 2.657 1.883 -0.687 -0.319 -0.202 7   SER FFF CB  
5171  O OG  . SER D 7   ? 2.462 2.607 1.811 -0.658 -0.330 -0.174 7   SER FFF OG  
5172  N N   . GLY D 8   ? 2.691 2.660 1.974 -0.720 -0.295 -0.221 8   GLY FFF N   
5173  C CA  . GLY D 8   ? 2.876 2.828 2.158 -0.731 -0.288 -0.216 8   GLY FFF CA  
5174  C C   . GLY D 8   ? 3.027 2.872 2.281 -0.738 -0.267 -0.234 8   GLY FFF C   
5175  O O   . GLY D 8   ? 3.050 2.871 2.300 -0.747 -0.259 -0.228 8   GLY FFF O   
5176  N N   . GLY D 9   ? 3.114 2.897 2.351 -0.731 -0.257 -0.253 9   GLY FFF N   
5177  C CA  . GLY D 9   ? 3.198 2.878 2.412 -0.732 -0.234 -0.268 9   GLY FFF CA  
5178  C C   . GLY D 9   ? 3.358 2.991 2.527 -0.788 -0.216 -0.293 9   GLY FFF C   
5179  O O   . GLY D 9   ? 3.439 3.113 2.587 -0.830 -0.221 -0.307 9   GLY FFF O   
5180  N N   . GLY D 10  ? 3.431 2.974 2.583 -0.787 -0.194 -0.299 10  GLY FFF N   
5181  C CA  . GLY D 10  ? 3.577 3.056 2.685 -0.839 -0.171 -0.324 10  GLY FFF CA  
5182  C C   . GLY D 10  ? 3.679 3.060 2.778 -0.825 -0.147 -0.320 10  GLY FFF C   
5183  O O   . GLY D 10  ? 3.678 3.034 2.801 -0.772 -0.147 -0.302 10  GLY FFF O   
5184  N N   . LEU D 11  ? 3.702 3.027 2.765 -0.873 -0.126 -0.336 11  LEU FFF N   
5185  C CA  . LEU D 11  ? 3.789 3.008 2.836 -0.867 -0.097 -0.335 11  LEU FFF CA  
5186  C C   . LEU D 11  ? 3.864 3.100 2.918 -0.889 -0.098 -0.315 11  LEU FFF C   
5187  O O   . LEU D 11  ? 3.953 3.238 2.999 -0.943 -0.105 -0.322 11  LEU FFF O   
5188  C CB  . LEU D 11  ? 3.829 2.949 2.825 -0.905 -0.065 -0.369 11  LEU FFF CB  
5189  C CG  . LEU D 11  ? 3.811 2.874 2.781 -0.894 -0.046 -0.395 11  LEU FFF CG  
5190  C CD1 . LEU D 11  ? 3.752 2.877 2.699 -0.931 -0.062 -0.421 11  LEU FFF CD1 
5191  C CD2 . LEU D 11  ? 3.853 2.781 2.781 -0.908 -0.004 -0.414 11  LEU FFF CD2 
5192  N N   . VAL D 12  ? 3.912 3.111 2.982 -0.848 -0.090 -0.289 12  VAL FFF N   
5193  C CA  . VAL D 12  ? 3.851 3.064 2.928 -0.860 -0.089 -0.265 12  VAL FFF CA  
5194  C C   . VAL D 12  ? 3.909 3.011 2.970 -0.834 -0.060 -0.253 12  VAL FFF C   
5195  O O   . VAL D 12  ? 3.981 3.027 3.042 -0.793 -0.052 -0.255 12  VAL FFF O   
5196  C CB  . VAL D 12  ? 3.723 3.036 2.837 -0.823 -0.118 -0.236 12  VAL FFF CB  
5197  C CG1 . VAL D 12  ? 3.673 2.992 2.792 -0.824 -0.111 -0.208 12  VAL FFF CG1 
5198  C CG2 . VAL D 12  ? 3.712 3.135 2.844 -0.847 -0.143 -0.243 12  VAL FFF CG2 
5199  N N   . GLN D 13  ? 3.956 3.028 3.007 -0.859 -0.043 -0.239 13  GLN FFF N   
5200  C CA  . GLN D 13  ? 4.093 3.066 3.130 -0.833 -0.016 -0.221 13  GLN FFF CA  
5201  C C   . GLN D 13  ? 4.113 3.112 3.173 -0.770 -0.031 -0.184 13  GLN FFF C   
5202  O O   . GLN D 13  ? 4.170 3.264 3.255 -0.752 -0.060 -0.171 13  GLN FFF O   
5203  C CB  . GLN D 13  ? 4.166 3.085 3.179 -0.889 0.012  -0.221 13  GLN FFF CB  
5204  C CG  . GLN D 13  ? 4.211 3.074 3.191 -0.947 0.030  -0.263 13  GLN FFF CG  
5205  C CD  . GLN D 13  ? 4.412 3.181 3.360 -0.997 0.066  -0.268 13  GLN FFF CD  
5206  O OE1 . GLN D 13  ? 4.479 3.239 3.434 -0.997 0.076  -0.238 13  GLN FFF OE1 
5207  N NE2 . GLN D 13  ? 4.535 3.225 3.446 -1.039 0.088  -0.306 13  GLN FFF NE2 
5208  N N   . ALA D 14  ? 4.157 3.069 3.208 -0.735 -0.011 -0.167 14  ALA FFF N   
5209  C CA  . ALA D 14  ? 4.055 2.977 3.119 -0.677 -0.023 -0.131 14  ALA FFF CA  
5210  C C   . ALA D 14  ? 4.061 3.036 3.123 -0.688 -0.029 -0.106 14  ALA FFF C   
5211  O O   . ALA D 14  ? 4.114 3.079 3.163 -0.737 -0.010 -0.106 14  ALA FFF O   
5212  C CB  . ALA D 14  ? 4.039 2.853 3.088 -0.647 0.006  -0.114 14  ALA FFF CB  
5213  N N   . GLY D 15  ? 3.945 2.977 3.021 -0.641 -0.055 -0.085 15  GLY FFF N   
5214  C CA  . GLY D 15  ? 3.871 2.963 2.947 -0.635 -0.065 -0.061 15  GLY FFF CA  
5215  C C   . GLY D 15  ? 3.787 2.981 2.881 -0.661 -0.084 -0.073 15  GLY FFF C   
5216  O O   . GLY D 15  ? 3.764 3.015 2.860 -0.653 -0.090 -0.053 15  GLY FFF O   
5217  N N   . GLY D 16  ? 3.863 3.083 2.971 -0.689 -0.091 -0.103 16  GLY FFF N   
5218  C CA  . GLY D 16  ? 3.839 3.159 2.968 -0.712 -0.110 -0.112 16  GLY FFF CA  
5219  C C   . GLY D 16  ? 3.796 3.177 2.945 -0.664 -0.140 -0.110 16  GLY FFF C   
5220  O O   . GLY D 16  ? 3.709 3.060 2.856 -0.616 -0.149 -0.102 16  GLY FFF O   
5221  N N   . SER D 17  ? 3.824 3.295 2.994 -0.679 -0.156 -0.116 17  SER FFF N   
5222  C CA  . SER D 17  ? 3.756 3.287 2.947 -0.640 -0.182 -0.116 17  SER FFF CA  
5223  C C   . SER D 17  ? 3.642 3.226 2.852 -0.665 -0.194 -0.137 17  SER FFF C   
5224  O O   . SER D 17  ? 3.704 3.303 2.911 -0.717 -0.185 -0.148 17  SER FFF O   
5225  C CB  . SER D 17  ? 3.863 3.457 3.060 -0.619 -0.188 -0.093 17  SER FFF CB  
5226  O OG  . SER D 17  ? 4.014 3.663 3.219 -0.661 -0.177 -0.085 17  SER FFF OG  
5227  N N   . LEU D 18  ? 3.409 3.020 2.636 -0.632 -0.214 -0.143 18  LEU FFF N   
5228  C CA  . LEU D 18  ? 3.186 2.848 2.429 -0.651 -0.225 -0.159 18  LEU FFF CA  
5229  C C   . LEU D 18  ? 3.070 2.782 2.337 -0.608 -0.247 -0.153 18  LEU FFF C   
5230  O O   . LEU D 18  ? 3.118 2.801 2.385 -0.565 -0.255 -0.146 18  LEU FFF O   
5231  C CB  . LEU D 18  ? 3.110 2.711 2.340 -0.669 -0.216 -0.183 18  LEU FFF CB  
5232  C CG  . LEU D 18  ? 2.987 2.641 2.222 -0.698 -0.225 -0.200 18  LEU FFF CG  
5233  C CD1 . LEU D 18  ? 3.003 2.721 2.238 -0.748 -0.224 -0.197 18  LEU FFF CD1 
5234  C CD2 . LEU D 18  ? 3.002 2.587 2.215 -0.715 -0.211 -0.225 18  LEU FFF CD2 
5235  N N   . ARG D 19  ? 2.928 2.716 2.214 -0.621 -0.258 -0.155 19  ARG FFF N   
5236  C CA  . ARG D 19  ? 2.792 2.626 2.102 -0.583 -0.276 -0.149 19  ARG FFF CA  
5237  C C   . ARG D 19  ? 2.694 2.549 2.014 -0.593 -0.284 -0.162 19  ARG FFF C   
5238  O O   . ARG D 19  ? 2.737 2.646 2.060 -0.629 -0.284 -0.165 19  ARG FFF O   
5239  C CB  . ARG D 19  ? 2.779 2.694 2.105 -0.577 -0.279 -0.128 19  ARG FFF CB  
5240  C CG  . ARG D 19  ? 2.645 2.611 1.997 -0.541 -0.294 -0.120 19  ARG FFF CG  
5241  C CD  . ARG D 19  ? 2.660 2.692 2.024 -0.529 -0.290 -0.098 19  ARG FFF CD  
5242  N NE  . ARG D 19  ? 2.664 2.715 2.041 -0.482 -0.298 -0.090 19  ARG FFF NE  
5243  C CZ  . ARG D 19  ? 2.676 2.689 2.039 -0.445 -0.298 -0.087 19  ARG FFF CZ  
5244  N NH1 . ARG D 19  ? 2.759 2.718 2.093 -0.446 -0.290 -0.088 19  ARG FFF NH1 
5245  N NH2 . ARG D 19  ? 2.540 2.568 1.913 -0.406 -0.304 -0.083 19  ARG FFF NH2 
5246  N N   . LEU D 20  ? 2.681 2.498 2.008 -0.563 -0.290 -0.170 20  LEU FFF N   
5247  C CA  . LEU D 20  ? 2.596 2.431 1.933 -0.566 -0.296 -0.180 20  LEU FFF CA  
5248  C C   . LEU D 20  ? 2.576 2.477 1.942 -0.538 -0.311 -0.166 20  LEU FFF C   
5249  O O   . LEU D 20  ? 2.626 2.528 2.002 -0.505 -0.318 -0.154 20  LEU FFF O   
5250  C CB  . LEU D 20  ? 2.562 2.326 1.898 -0.548 -0.292 -0.192 20  LEU FFF CB  
5251  C CG  . LEU D 20  ? 2.667 2.353 1.978 -0.563 -0.274 -0.203 20  LEU FFF CG  
5252  C CD1 . LEU D 20  ? 2.615 2.241 1.934 -0.538 -0.269 -0.210 20  LEU FFF CD1 
5253  C CD2 . LEU D 20  ? 2.886 2.570 2.170 -0.615 -0.259 -0.217 20  LEU FFF CD2 
5254  N N   . SER D 21  ? 2.514 2.466 1.888 -0.552 -0.316 -0.166 21  SER FFF N   
5255  C CA  . SER D 21  ? 2.473 2.486 1.875 -0.525 -0.328 -0.149 21  SER FFF CA  
5256  C C   . SER D 21  ? 2.423 2.441 1.833 -0.522 -0.331 -0.155 21  SER FFF C   
5257  O O   . SER D 21  ? 2.466 2.485 1.858 -0.554 -0.326 -0.167 21  SER FFF O   
5258  C CB  . SER D 21  ? 2.500 2.600 1.911 -0.542 -0.330 -0.132 21  SER FFF CB  
5259  O OG  . SER D 21  ? 2.643 2.741 2.048 -0.545 -0.323 -0.125 21  SER FFF OG  
5260  N N   . CYS D 22  ? 2.256 2.276 1.691 -0.484 -0.338 -0.145 22  CYS FFF N   
5261  C CA  . CYS D 22  ? 2.218 2.238 1.666 -0.474 -0.340 -0.146 22  CYS FFF CA  
5262  C C   . CYS D 22  ? 2.084 2.172 1.555 -0.456 -0.347 -0.124 22  CYS FFF C   
5263  O O   . CYS D 22  ? 2.091 2.181 1.582 -0.423 -0.352 -0.112 22  CYS FFF O   
5264  C CB  . CYS D 22  ? 2.421 2.374 1.883 -0.446 -0.341 -0.154 22  CYS FFF CB  
5265  S SG  . CYS D 22  ? 2.510 2.462 1.997 -0.430 -0.341 -0.150 22  CYS FFF SG  
5266  N N   . ALA D 23  ? 2.063 2.205 1.529 -0.477 -0.348 -0.118 23  ALA FFF N   
5267  C CA  . ALA D 23  ? 1.903 2.116 1.392 -0.461 -0.353 -0.092 23  ALA FFF CA  
5268  C C   . ALA D 23  ? 1.795 1.985 1.301 -0.436 -0.352 -0.088 23  ALA FFF C   
5269  O O   . ALA D 23  ? 1.816 1.974 1.310 -0.449 -0.347 -0.102 23  ALA FFF O   
5270  C CB  . ALA D 23  ? 2.157 2.447 1.632 -0.497 -0.357 -0.084 23  ALA FFF CB  
5271  N N   . ALA D 24  ? 1.741 1.948 1.276 -0.400 -0.354 -0.067 24  ALA FFF N   
5272  C CA  . ALA D 24  ? 1.714 1.897 1.270 -0.375 -0.352 -0.059 24  ALA FFF CA  
5273  C C   . ALA D 24  ? 1.701 1.952 1.274 -0.360 -0.352 -0.028 24  ALA FFF C   
5274  O O   . ALA D 24  ? 1.708 2.015 1.289 -0.352 -0.354 -0.010 24  ALA FFF O   
5275  C CB  . ALA D 24  ? 1.748 1.871 1.324 -0.344 -0.354 -0.065 24  ALA FFF CB  
5276  N N   . SER D 25  ? 1.641 1.891 1.222 -0.356 -0.348 -0.020 25  SER FFF N   
5277  C CA  . SER D 25  ? 1.776 2.082 1.375 -0.335 -0.346 0.014  25  SER FFF CA  
5278  C C   . SER D 25  ? 1.963 2.239 1.595 -0.294 -0.342 0.027  25  SER FFF C   
5279  O O   . SER D 25  ? 2.104 2.309 1.745 -0.283 -0.342 0.009  25  SER FFF O   
5280  C CB  . SER D 25  ? 1.792 2.105 1.385 -0.344 -0.341 0.020  25  SER FFF CB  
5281  O OG  . SER D 25  ? 1.899 2.223 1.520 -0.312 -0.335 0.050  25  SER FFF OG  
5282  N N   . GLY D 26  ? 2.222 2.552 1.871 -0.270 -0.339 0.061  26  GLY FFF N   
5283  C CA  . GLY D 26  ? 2.252 2.551 1.927 -0.231 -0.332 0.073  26  GLY FFF CA  
5284  C C   . GLY D 26  ? 2.227 2.506 1.895 -0.224 -0.334 0.058  26  GLY FFF C   
5285  O O   . GLY D 26  ? 2.305 2.615 1.955 -0.247 -0.340 0.048  26  GLY FFF O   
5286  N N   . SER D 27  ? 1.998 2.221 1.679 -0.192 -0.328 0.056  27  SER FFF N   
5287  C CA  . SER D 27  ? 2.029 2.221 1.698 -0.179 -0.327 0.041  27  SER FFF CA  
5288  C C   . SER D 27  ? 2.082 2.198 1.736 -0.195 -0.337 0.005  27  SER FFF C   
5289  O O   . SER D 27  ? 2.159 2.225 1.824 -0.197 -0.341 -0.005 27  SER FFF O   
5290  C CB  . SER D 27  ? 2.094 2.262 1.779 -0.136 -0.314 0.057  27  SER FFF CB  
5291  O OG  . SER D 27  ? 2.223 2.361 1.889 -0.123 -0.311 0.042  27  SER FFF OG  
5292  N N   . ILE D 28  ? 1.999 2.109 1.629 -0.207 -0.342 -0.013 28  ILE FFF N   
5293  C CA  . ILE D 28  ? 1.848 1.893 1.462 -0.222 -0.352 -0.043 28  ILE FFF CA  
5294  C C   . ILE D 28  ? 1.867 1.842 1.482 -0.197 -0.355 -0.056 28  ILE FFF C   
5295  O O   . ILE D 28  ? 1.964 1.885 1.578 -0.206 -0.367 -0.077 28  ILE FFF O   
5296  C CB  . ILE D 28  ? 1.767 1.828 1.355 -0.241 -0.354 -0.054 28  ILE FFF CB  
5297  C CG1 . ILE D 28  ? 1.722 1.733 1.297 -0.264 -0.364 -0.079 28  ILE FFF CG1 
5298  C CG2 . ILE D 28  ? 1.956 2.002 1.527 -0.218 -0.349 -0.055 28  ILE FFF CG2 
5299  C CD1 . ILE D 28  ? 1.878 1.898 1.426 -0.287 -0.363 -0.088 28  ILE FFF CD1 
5300  N N   . SER D 29  ? 1.881 1.854 1.498 -0.167 -0.345 -0.044 29  SER FFF N   
5301  C CA  . SER D 29  ? 1.950 1.851 1.561 -0.145 -0.347 -0.060 29  SER FFF CA  
5302  C C   . SER D 29  ? 1.951 1.811 1.590 -0.146 -0.352 -0.062 29  SER FFF C   
5303  O O   . SER D 29  ? 2.080 1.875 1.716 -0.137 -0.358 -0.079 29  SER FFF O   
5304  C CB  . SER D 29  ? 1.959 1.863 1.562 -0.111 -0.330 -0.046 29  SER FFF CB  
5305  O OG  . SER D 29  ? 2.029 1.980 1.661 -0.095 -0.315 -0.014 29  SER FFF OG  
5306  N N   . ARG D 30  ? 1.885 1.784 1.549 -0.158 -0.348 -0.044 30  ARG FFF N   
5307  C CA  . ARG D 30  ? 1.944 1.810 1.639 -0.159 -0.350 -0.042 30  ARG FFF CA  
5308  C C   . ARG D 30  ? 1.871 1.702 1.572 -0.183 -0.366 -0.066 30  ARG FFF C   
5309  O O   . ARG D 30  ? 1.828 1.617 1.555 -0.184 -0.370 -0.071 30  ARG FFF O   
5310  C CB  . ARG D 30  ? 2.039 1.962 1.754 -0.163 -0.339 -0.014 30  ARG FFF CB  
5311  C CG  . ARG D 30  ? 2.157 2.136 1.875 -0.141 -0.324 0.019  30  ARG FFF CG  
5312  C CD  . ARG D 30  ? 2.253 2.282 1.988 -0.150 -0.318 0.045  30  ARG FFF CD  
5313  N NE  . ARG D 30  ? 2.217 2.268 1.938 -0.184 -0.327 0.029  30  ARG FFF NE  
5314  C CZ  . ARG D 30  ? 2.125 2.207 1.850 -0.200 -0.324 0.040  30  ARG FFF CZ  
5315  N NH1 . ARG D 30  ? 2.242 2.344 1.987 -0.186 -0.313 0.070  30  ARG FFF NH1 
5316  N NH2 . ARG D 30  ? 1.937 2.027 1.644 -0.231 -0.330 0.022  30  ARG FFF NH2 
5317  N N   . PHE D 31  ? 1.867 1.715 1.549 -0.203 -0.373 -0.078 31  PHE FFF N   
5318  C CA  . PHE D 31  ? 1.809 1.627 1.498 -0.222 -0.386 -0.097 31  PHE FFF CA  
5319  C C   . PHE D 31  ? 1.789 1.549 1.472 -0.215 -0.403 -0.118 31  PHE FFF C   
5320  O O   . PHE D 31  ? 1.842 1.588 1.494 -0.203 -0.405 -0.126 31  PHE FFF O   
5321  C CB  . PHE D 31  ? 1.820 1.667 1.486 -0.242 -0.386 -0.102 31  PHE FFF CB  
5322  C CG  . PHE D 31  ? 1.815 1.719 1.482 -0.254 -0.372 -0.085 31  PHE FFF CG  
5323  C CD1 . PHE D 31  ? 1.782 1.694 1.475 -0.257 -0.365 -0.073 31  PHE FFF CD1 
5324  C CD2 . PHE D 31  ? 1.847 1.797 1.488 -0.263 -0.368 -0.079 31  PHE FFF CD2 
5325  C CE1 . PHE D 31  ? 1.793 1.759 1.479 -0.268 -0.354 -0.057 31  PHE FFF CE1 
5326  C CE2 . PHE D 31  ? 1.832 1.837 1.470 -0.276 -0.359 -0.064 31  PHE FFF CE2 
5327  C CZ  . PHE D 31  ? 1.789 1.802 1.446 -0.279 -0.353 -0.054 31  PHE FFF CZ  
5328  N N   . ASN D 32  ? 1.756 1.484 1.466 -0.225 -0.415 -0.128 32  ASN FFF N   
5329  C CA  . ASN D 32  ? 1.687 1.365 1.390 -0.223 -0.435 -0.148 32  ASN FFF CA  
5330  C C   . ASN D 32  ? 1.656 1.330 1.338 -0.233 -0.450 -0.162 32  ASN FFF C   
5331  O O   . ASN D 32  ? 1.663 1.302 1.325 -0.229 -0.468 -0.178 32  ASN FFF O   
5332  C CB  . ASN D 32  ? 1.620 1.270 1.370 -0.229 -0.445 -0.150 32  ASN FFF CB  
5333  C CG  . ASN D 32  ? 1.651 1.293 1.422 -0.219 -0.429 -0.136 32  ASN FFF CG  
5334  O OD1 . ASN D 32  ? 1.668 1.305 1.413 -0.201 -0.419 -0.131 32  ASN FFF OD1 
5335  N ND2 . ASN D 32  ? 1.681 1.322 1.499 -0.228 -0.426 -0.125 32  ASN FFF ND2 
5336  N N   . ALA D 33  ? 1.721 1.426 1.403 -0.245 -0.442 -0.156 33  ALA FFF N   
5337  C CA  . ALA D 33  ? 1.751 1.449 1.412 -0.252 -0.451 -0.165 33  ALA FFF CA  
5338  C C   . ALA D 33  ? 1.766 1.497 1.417 -0.265 -0.433 -0.157 33  ALA FFF C   
5339  O O   . ALA D 33  ? 1.820 1.574 1.494 -0.272 -0.419 -0.148 33  ALA FFF O   
5340  C CB  . ALA D 33  ? 1.749 1.422 1.439 -0.257 -0.470 -0.173 33  ALA FFF CB  
5341  N N   . MET D 34  ? 1.776 1.509 1.392 -0.270 -0.431 -0.162 34  MET FFF N   
5342  C CA  . MET D 34  ? 1.782 1.536 1.385 -0.287 -0.416 -0.159 34  MET FFF CA  
5343  C C   . MET D 34  ? 1.807 1.535 1.389 -0.291 -0.421 -0.166 34  MET FFF C   
5344  O O   . MET D 34  ? 1.850 1.553 1.418 -0.280 -0.437 -0.171 34  MET FFF O   
5345  C CB  . MET D 34  ? 1.806 1.602 1.386 -0.293 -0.402 -0.150 34  MET FFF CB  
5346  C CG  . MET D 34  ? 1.917 1.742 1.513 -0.281 -0.398 -0.138 34  MET FFF CG  
5347  S SD  . MET D 34  ? 2.059 1.946 1.633 -0.290 -0.383 -0.124 34  MET FFF SD  
5348  C CE  . MET D 34  ? 2.044 1.950 1.613 -0.322 -0.374 -0.127 34  MET FFF CE  
5349  N N   . GLY D 35  ? 1.810 1.539 1.384 -0.308 -0.407 -0.167 35  GLY FFF N   
5350  C CA  . GLY D 35  ? 1.934 1.635 1.489 -0.312 -0.407 -0.171 35  GLY FFF CA  
5351  C C   . GLY D 35  ? 1.984 1.682 1.528 -0.332 -0.385 -0.173 35  GLY FFF C   
5352  O O   . GLY D 35  ? 2.015 1.740 1.560 -0.347 -0.372 -0.173 35  GLY FFF O   
5353  N N   . TRP D 36  ? 2.136 1.799 1.668 -0.333 -0.382 -0.175 36  TRP FFF N   
5354  C CA  . TRP D 36  ? 2.151 1.796 1.663 -0.353 -0.359 -0.179 36  TRP FFF CA  
5355  C C   . TRP D 36  ? 2.297 1.901 1.829 -0.342 -0.355 -0.178 36  TRP FFF C   
5356  O O   . TRP D 36  ? 2.386 1.972 1.926 -0.323 -0.371 -0.172 36  TRP FFF O   
5357  C CB  . TRP D 36  ? 2.163 1.802 1.634 -0.366 -0.354 -0.179 36  TRP FFF CB  
5358  C CG  . TRP D 36  ? 2.189 1.876 1.644 -0.381 -0.352 -0.177 36  TRP FFF CG  
5359  C CD1 . TRP D 36  ? 2.215 1.927 1.663 -0.369 -0.364 -0.171 36  TRP FFF CD1 
5360  C CD2 . TRP D 36  ? 2.272 1.989 1.713 -0.410 -0.338 -0.181 36  TRP FFF CD2 
5361  N NE1 . TRP D 36  ? 2.266 2.026 1.705 -0.385 -0.357 -0.167 36  TRP FFF NE1 
5362  C CE2 . TRP D 36  ? 2.275 2.042 1.710 -0.413 -0.343 -0.173 36  TRP FFF CE2 
5363  C CE3 . TRP D 36  ? 2.338 2.044 1.769 -0.435 -0.321 -0.191 36  TRP FFF CE3 
5364  C CZ2 . TRP D 36  ? 2.282 2.097 1.707 -0.440 -0.336 -0.172 36  TRP FFF CZ2 
5365  C CZ3 . TRP D 36  ? 2.319 2.067 1.733 -0.464 -0.314 -0.194 36  TRP FFF CZ3 
5366  C CH2 . TRP D 36  ? 2.297 2.103 1.711 -0.467 -0.323 -0.183 36  TRP FFF CH2 
5367  N N   . TRP D 37  ? 2.415 2.007 1.953 -0.352 -0.333 -0.183 37  TRP FFF N   
5368  C CA  . TRP D 37  ? 2.549 2.100 2.104 -0.341 -0.320 -0.181 37  TRP FFF CA  
5369  C C   . TRP D 37  ? 2.775 2.292 2.292 -0.363 -0.290 -0.191 37  TRP FFF C   
5370  O O   . TRP D 37  ? 2.891 2.424 2.375 -0.390 -0.281 -0.201 37  TRP FFF O   
5371  C CB  . TRP D 37  ? 2.489 2.052 2.091 -0.329 -0.318 -0.178 37  TRP FFF CB  
5372  C CG  . TRP D 37  ? 2.477 2.061 2.123 -0.308 -0.347 -0.167 37  TRP FFF CG  
5373  C CD1 . TRP D 37  ? 2.505 2.119 2.155 -0.307 -0.370 -0.167 37  TRP FFF CD1 
5374  C CD2 . TRP D 37  ? 2.488 2.066 2.184 -0.287 -0.356 -0.156 37  TRP FFF CD2 
5375  N NE1 . TRP D 37  ? 2.581 2.201 2.273 -0.290 -0.394 -0.160 37  TRP FFF NE1 
5376  C CE2 . TRP D 37  ? 2.592 2.196 2.316 -0.278 -0.387 -0.153 37  TRP FFF CE2 
5377  C CE3 . TRP D 37  ? 2.496 2.050 2.217 -0.274 -0.339 -0.149 37  TRP FFF CE3 
5378  C CZ2 . TRP D 37  ? 2.727 2.338 2.503 -0.262 -0.406 -0.142 37  TRP FFF CZ2 
5379  C CZ3 . TRP D 37  ? 2.576 2.143 2.353 -0.254 -0.357 -0.134 37  TRP FFF CZ3 
5380  C CH2 . TRP D 37  ? 2.748 2.345 2.553 -0.250 -0.392 -0.132 37  TRP FFF CH2 
5381  N N   . ARG D 38  ? 2.856 2.323 2.375 -0.353 -0.273 -0.188 38  ARG FFF N   
5382  C CA  . ARG D 38  ? 2.907 2.329 2.388 -0.374 -0.241 -0.200 38  ARG FFF CA  
5383  C C   . ARG D 38  ? 2.965 2.342 2.466 -0.356 -0.215 -0.198 38  ARG FFF C   
5384  O O   . ARG D 38  ? 3.016 2.394 2.562 -0.325 -0.224 -0.182 38  ARG FFF O   
5385  C CB  . ARG D 38  ? 2.948 2.336 2.390 -0.384 -0.237 -0.198 38  ARG FFF CB  
5386  C CG  . ARG D 38  ? 2.970 2.323 2.428 -0.354 -0.241 -0.180 38  ARG FFF CG  
5387  C CD  . ARG D 38  ? 3.050 2.370 2.466 -0.368 -0.234 -0.176 38  ARG FFF CD  
5388  N NE  . ARG D 38  ? 3.087 2.371 2.511 -0.339 -0.236 -0.155 38  ARG FFF NE  
5389  C CZ  . ARG D 38  ? 3.188 2.448 2.581 -0.341 -0.235 -0.144 38  ARG FFF CZ  
5390  N NH1 . ARG D 38  ? 3.255 2.523 2.610 -0.372 -0.231 -0.153 38  ARG FFF NH1 
5391  N NH2 . ARG D 38  ? 3.232 2.462 2.634 -0.311 -0.238 -0.122 38  ARG FFF NH2 
5392  N N   . GLN D 39  ? 3.018 2.357 2.485 -0.377 -0.181 -0.215 39  GLN FFF N   
5393  C CA  . GLN D 39  ? 3.096 2.380 2.570 -0.362 -0.147 -0.217 39  GLN FFF CA  
5394  C C   . GLN D 39  ? 3.258 2.473 2.674 -0.387 -0.113 -0.234 39  GLN FFF C   
5395  O O   . GLN D 39  ? 3.292 2.509 2.661 -0.426 -0.107 -0.256 39  GLN FFF O   
5396  C CB  . GLN D 39  ? 3.064 2.368 2.557 -0.359 -0.132 -0.224 39  GLN FFF CB  
5397  C CG  . GLN D 39  ? 3.128 2.379 2.637 -0.335 -0.095 -0.221 39  GLN FFF CG  
5398  C CD  . GLN D 39  ? 3.095 2.363 2.624 -0.328 -0.076 -0.225 39  GLN FFF CD  
5399  O OE1 . GLN D 39  ? 2.970 2.294 2.507 -0.339 -0.093 -0.226 39  GLN FFF OE1 
5400  N NE2 . GLN D 39  ? 3.163 2.382 2.699 -0.309 -0.036 -0.225 39  GLN FFF NE2 
5401  N N   . ALA D 40  ? 3.528 2.682 2.948 -0.366 -0.093 -0.224 40  ALA FFF N   
5402  C CA  . ALA D 40  ? 3.659 2.732 3.026 -0.387 -0.056 -0.240 40  ALA FFF CA  
5403  C C   . ALA D 40  ? 3.784 2.806 3.147 -0.376 -0.013 -0.252 40  ALA FFF C   
5404  O O   . ALA D 40  ? 3.912 2.956 3.327 -0.341 -0.012 -0.237 40  ALA FFF O   
5405  C CB  . ALA D 40  ? 3.635 2.660 3.003 -0.368 -0.053 -0.219 40  ALA FFF CB  
5406  N N   . PRO D 41  ? 3.731 2.687 3.034 -0.408 0.023  -0.279 41  PRO FFF N   
5407  C CA  . PRO D 41  ? 3.723 2.624 3.013 -0.397 0.067  -0.294 41  PRO FFF CA  
5408  C C   . PRO D 41  ? 3.703 2.563 3.041 -0.344 0.091  -0.268 41  PRO FFF C   
5409  O O   . PRO D 41  ? 3.765 2.568 3.098 -0.332 0.103  -0.255 41  PRO FFF O   
5410  C CB  . PRO D 41  ? 3.845 2.669 3.053 -0.444 0.098  -0.329 41  PRO FFF CB  
5411  C CG  . PRO D 41  ? 3.765 2.645 2.949 -0.488 0.061  -0.337 41  PRO FFF CG  
5412  C CD  . PRO D 41  ? 3.732 2.666 2.972 -0.460 0.022  -0.302 41  PRO FFF CD  
5413  N N   . GLY D 42  ? 3.767 2.658 3.154 -0.312 0.098  -0.257 42  GLY FFF N   
5414  C CA  . GLY D 42  ? 3.682 2.551 3.126 -0.259 0.120  -0.229 42  GLY FFF CA  
5415  C C   . GLY D 42  ? 3.612 2.548 3.132 -0.225 0.077  -0.190 42  GLY FFF C   
5416  O O   . GLY D 42  ? 3.458 2.402 3.040 -0.180 0.087  -0.162 42  GLY FFF O   
5417  N N   . LYS D 43  ? 3.597 2.583 3.112 -0.244 0.030  -0.187 43  LYS FFF N   
5418  C CA  . LYS D 43  ? 3.523 2.569 3.096 -0.218 -0.014 -0.155 43  LYS FFF CA  
5419  C C   . LYS D 43  ? 3.353 2.487 2.964 -0.224 -0.051 -0.155 43  LYS FFF C   
5420  O O   . LYS D 43  ? 3.414 2.567 2.991 -0.257 -0.052 -0.180 43  LYS FFF O   
5421  C CB  . LYS D 43  ? 3.524 2.558 3.063 -0.233 -0.038 -0.150 43  LYS FFF CB  
5422  C CG  . LYS D 43  ? 3.554 2.545 3.109 -0.198 -0.029 -0.120 43  LYS FFF CG  
5423  C CD  . LYS D 43  ? 3.525 2.506 3.043 -0.212 -0.051 -0.113 43  LYS FFF CD  
5424  C CE  . LYS D 43  ? 3.361 2.425 2.891 -0.223 -0.104 -0.111 43  LYS FFF CE  
5425  N NZ  . LYS D 43  ? 3.378 2.430 2.863 -0.242 -0.118 -0.109 43  LYS FFF NZ  
5426  N N   . GLU D 44  ? 3.135 2.323 2.814 -0.194 -0.081 -0.128 44  GLU FFF N   
5427  C CA  . GLU D 44  ? 2.999 2.264 2.717 -0.199 -0.114 -0.127 44  GLU FFF CA  
5428  C C   . GLU D 44  ? 2.946 2.246 2.634 -0.226 -0.155 -0.136 44  GLU FFF C   
5429  O O   . GLU D 44  ? 3.018 2.299 2.677 -0.229 -0.169 -0.132 44  GLU FFF O   
5430  C CB  . GLU D 44  ? 2.998 2.307 2.801 -0.162 -0.133 -0.096 44  GLU FFF CB  
5431  C CG  . GLU D 44  ? 3.019 2.303 2.860 -0.134 -0.088 -0.085 44  GLU FFF CG  
5432  C CD  . GLU D 44  ? 2.958 2.304 2.894 -0.103 -0.104 -0.055 44  GLU FFF CD  
5433  O OE1 . GLU D 44  ? 2.815 2.225 2.784 -0.112 -0.148 -0.051 44  GLU FFF OE1 
5434  O OE2 . GLU D 44  ? 3.036 2.368 3.014 -0.071 -0.072 -0.036 44  GLU FFF OE2 
5435  N N   . ARG D 45  ? 2.932 2.281 2.626 -0.243 -0.171 -0.147 45  ARG FFF N   
5436  C CA  . ARG D 45  ? 2.903 2.290 2.575 -0.263 -0.207 -0.154 45  ARG FFF CA  
5437  C C   . ARG D 45  ? 2.933 2.341 2.627 -0.247 -0.246 -0.136 45  ARG FFF C   
5438  O O   . ARG D 45  ? 2.954 2.390 2.705 -0.223 -0.265 -0.119 45  ARG FFF O   
5439  C CB  . ARG D 45  ? 2.783 2.222 2.475 -0.274 -0.217 -0.160 45  ARG FFF CB  
5440  C CG  . ARG D 45  ? 2.829 2.255 2.475 -0.300 -0.187 -0.181 45  ARG FFF CG  
5441  C CD  . ARG D 45  ? 2.773 2.231 2.449 -0.298 -0.177 -0.180 45  ARG FFF CD  
5442  N NE  . ARG D 45  ? 2.661 2.173 2.345 -0.309 -0.206 -0.179 45  ARG FFF NE  
5443  C CZ  . ARG D 45  ? 2.648 2.178 2.287 -0.335 -0.205 -0.193 45  ARG FFF CZ  
5444  N NH1 . ARG D 45  ? 2.757 2.256 2.339 -0.358 -0.179 -0.211 45  ARG FFF NH1 
5445  N NH2 . ARG D 45  ? 2.547 2.123 2.198 -0.339 -0.230 -0.187 45  ARG FFF NH2 
5446  N N   . GLU D 46  ? 3.124 2.522 2.771 -0.261 -0.259 -0.141 46  GLU FFF N   
5447  C CA  . GLU D 46  ? 3.048 2.461 2.699 -0.247 -0.294 -0.127 46  GLU FFF CA  
5448  C C   . GLU D 46  ? 2.884 2.335 2.513 -0.265 -0.321 -0.138 46  GLU FFF C   
5449  O O   . GLU D 46  ? 2.868 2.322 2.461 -0.290 -0.308 -0.154 46  GLU FFF O   
5450  C CB  . GLU D 46  ? 3.193 2.558 2.807 -0.243 -0.283 -0.119 46  GLU FFF CB  
5451  C CG  . GLU D 46  ? 3.286 2.656 2.926 -0.212 -0.309 -0.093 46  GLU FFF CG  
5452  C CD  . GLU D 46  ? 3.382 2.703 2.981 -0.206 -0.297 -0.081 46  GLU FFF CD  
5453  O OE1 . GLU D 46  ? 3.424 2.709 2.975 -0.230 -0.271 -0.094 46  GLU FFF OE1 
5454  O OE2 . GLU D 46  ? 3.360 2.682 2.977 -0.179 -0.314 -0.056 46  GLU FFF OE2 
5455  N N   . PHE D 47  ? 2.677 2.158 2.328 -0.252 -0.357 -0.130 47  PHE FFF N   
5456  C CA  . PHE D 47  ? 2.581 2.094 2.214 -0.262 -0.381 -0.139 47  PHE FFF CA  
5457  C C   . PHE D 47  ? 2.558 2.056 2.135 -0.269 -0.385 -0.139 47  PHE FFF C   
5458  O O   . PHE D 47  ? 2.705 2.180 2.269 -0.255 -0.390 -0.127 47  PHE FFF O   
5459  C CB  . PHE D 47  ? 2.606 2.148 2.280 -0.247 -0.417 -0.132 47  PHE FFF CB  
5460  C CG  . PHE D 47  ? 2.564 2.123 2.210 -0.252 -0.443 -0.140 47  PHE FFF CG  
5461  C CD1 . PHE D 47  ? 2.504 2.087 2.150 -0.264 -0.442 -0.151 47  PHE FFF CD1 
5462  C CD2 . PHE D 47  ? 2.602 2.152 2.220 -0.241 -0.466 -0.135 47  PHE FFF CD2 
5463  C CE1 . PHE D 47  ? 2.403 1.996 2.023 -0.264 -0.461 -0.158 47  PHE FFF CE1 
5464  C CE2 . PHE D 47  ? 2.516 2.077 2.104 -0.243 -0.485 -0.144 47  PHE FFF CE2 
5465  C CZ  . PHE D 47  ? 2.411 1.991 2.001 -0.253 -0.482 -0.156 47  PHE FFF CZ  
5466  N N   . VAL D 48  ? 2.425 1.940 1.971 -0.288 -0.381 -0.151 48  VAL FFF N   
5467  C CA  . VAL D 48  ? 2.412 1.918 1.908 -0.297 -0.379 -0.150 48  VAL FFF CA  
5468  C C   . VAL D 48  ? 2.393 1.928 1.876 -0.290 -0.405 -0.152 48  VAL FFF C   
5469  O O   . VAL D 48  ? 2.453 1.977 1.912 -0.278 -0.419 -0.145 48  VAL FFF O   
5470  C CB  . VAL D 48  ? 2.409 1.913 1.876 -0.326 -0.351 -0.160 48  VAL FFF CB  
5471  C CG1 . VAL D 48  ? 2.451 1.951 1.874 -0.337 -0.347 -0.157 48  VAL FFF CG1 
5472  C CG2 . VAL D 48  ? 2.563 2.027 2.034 -0.333 -0.323 -0.163 48  VAL FFF CG2 
5473  N N   . ALA D 49  ? 2.306 1.874 1.801 -0.297 -0.408 -0.160 49  ALA FFF N   
5474  C CA  . ALA D 49  ? 2.235 1.823 1.713 -0.289 -0.426 -0.163 49  ALA FFF CA  
5475  C C   . ALA D 49  ? 2.159 1.772 1.671 -0.285 -0.437 -0.168 49  ALA FFF C   
5476  O O   . ALA D 49  ? 2.182 1.807 1.722 -0.294 -0.426 -0.170 49  ALA FFF O   
5477  C CB  . ALA D 49  ? 2.190 1.793 1.629 -0.303 -0.411 -0.163 49  ALA FFF CB  
5478  N N   . ARG D 50  ? 2.150 1.767 1.654 -0.272 -0.458 -0.171 50  ARG FFF N   
5479  C CA  . ARG D 50  ? 2.045 1.676 1.577 -0.268 -0.468 -0.177 50  ARG FFF CA  
5480  C C   . ARG D 50  ? 2.024 1.658 1.522 -0.258 -0.474 -0.181 50  ARG FFF C   
5481  O O   . ARG D 50  ? 2.163 1.780 1.623 -0.250 -0.483 -0.183 50  ARG FFF O   
5482  C CB  . ARG D 50  ? 2.061 1.681 1.633 -0.260 -0.490 -0.178 50  ARG FFF CB  
5483  C CG  . ARG D 50  ? 2.291 1.891 1.845 -0.248 -0.519 -0.181 50  ARG FFF CG  
5484  C CD  . ARG D 50  ? 2.276 1.876 1.881 -0.247 -0.542 -0.182 50  ARG FFF CD  
5485  N NE  . ARG D 50  ? 2.376 1.966 1.976 -0.239 -0.570 -0.180 50  ARG FFF NE  
5486  C CZ  . ARG D 50  ? 2.474 2.071 2.122 -0.237 -0.584 -0.171 50  ARG FFF CZ  
5487  N NH1 . ARG D 50  ? 2.538 2.151 2.244 -0.242 -0.571 -0.165 50  ARG FFF NH1 
5488  N NH2 . ARG D 50  ? 2.598 2.191 2.238 -0.229 -0.613 -0.166 50  ARG FFF NH2 
5489  N N   . ILE D 51  ? 1.893 1.548 1.404 -0.258 -0.467 -0.182 51  ILE FFF N   
5490  C CA  . ILE D 51  ? 1.917 1.569 1.404 -0.244 -0.470 -0.186 51  ILE FFF CA  
5491  C C   . ILE D 51  ? 1.890 1.540 1.415 -0.240 -0.476 -0.189 51  ILE FFF C   
5492  O O   . ILE D 51  ? 2.034 1.710 1.587 -0.246 -0.462 -0.181 51  ILE FFF O   
5493  C CB  . ILE D 51  ? 1.943 1.626 1.405 -0.244 -0.449 -0.179 51  ILE FFF CB  
5494  C CG1 . ILE D 51  ? 2.130 1.810 1.554 -0.250 -0.442 -0.175 51  ILE FFF CG1 
5495  C CG2 . ILE D 51  ? 1.913 1.591 1.355 -0.224 -0.448 -0.182 51  ILE FFF CG2 
5496  C CD1 . ILE D 51  ? 2.282 1.990 1.677 -0.246 -0.424 -0.167 51  ILE FFF CD1 
5497  N N   . VAL D 52  ? 1.909 1.529 1.431 -0.231 -0.497 -0.201 52  VAL FFF N   
5498  C CA  . VAL D 52  ? 1.903 1.511 1.456 -0.228 -0.503 -0.205 52  VAL FFF CA  
5499  C C   . VAL D 52  ? 1.958 1.549 1.476 -0.211 -0.497 -0.211 52  VAL FFF C   
5500  O O   . VAL D 52  ? 2.059 1.633 1.528 -0.202 -0.500 -0.220 52  VAL FFF O   
5501  C CB  . VAL D 52  ? 1.923 1.505 1.501 -0.234 -0.531 -0.215 52  VAL FFF CB  
5502  C CG1 . VAL D 52  ? 1.921 1.490 1.537 -0.236 -0.535 -0.218 52  VAL FFF CG1 
5503  C CG2 . VAL D 52  ? 1.883 1.483 1.496 -0.245 -0.533 -0.205 52  VAL FFF CG2 
5504  N N   . LYS D 53  ? 1.892 1.487 1.435 -0.206 -0.484 -0.205 53  LYS FFF N   
5505  C CA  . LYS D 53  ? 1.991 1.573 1.506 -0.186 -0.470 -0.207 53  LYS FFF CA  
5506  C C   . LYS D 53  ? 2.164 1.690 1.641 -0.178 -0.487 -0.230 53  LYS FFF C   
5507  O O   . LYS D 53  ? 2.212 1.705 1.708 -0.188 -0.508 -0.243 53  LYS FFF O   
5508  C CB  . LYS D 53  ? 1.954 1.545 1.508 -0.181 -0.454 -0.194 53  LYS FFF CB  
5509  C CG  . LYS D 53  ? 1.969 1.618 1.534 -0.178 -0.429 -0.169 53  LYS FFF CG  
5510  C CD  . LYS D 53  ? 1.912 1.563 1.492 -0.158 -0.410 -0.155 53  LYS FFF CD  
5511  C CE  . LYS D 53  ? 1.903 1.538 1.529 -0.165 -0.413 -0.150 53  LYS FFF CE  
5512  N NZ  . LYS D 53  ? 1.958 1.594 1.599 -0.144 -0.392 -0.131 53  LYS FFF NZ  
5513  N N   . GLY D 54  ? 2.361 1.879 1.785 -0.162 -0.477 -0.234 54  GLY FFF N   
5514  C CA  . GLY D 54  ? 2.453 1.917 1.824 -0.152 -0.490 -0.258 54  GLY FFF CA  
5515  C C   . GLY D 54  ? 2.439 1.893 1.775 -0.161 -0.515 -0.268 54  GLY FFF C   
5516  O O   . GLY D 54  ? 2.642 2.055 1.924 -0.154 -0.527 -0.288 54  GLY FFF O   
5517  N N   . PHE D 55  ? 2.198 1.687 1.561 -0.176 -0.522 -0.256 55  PHE FFF N   
5518  C CA  . PHE D 55  ? 2.233 1.714 1.571 -0.183 -0.546 -0.261 55  PHE FFF CA  
5519  C C   . PHE D 55  ? 2.208 1.717 1.517 -0.179 -0.528 -0.246 55  PHE FFF C   
5520  O O   . PHE D 55  ? 2.151 1.695 1.474 -0.178 -0.501 -0.231 55  PHE FFF O   
5521  C CB  . PHE D 55  ? 2.245 1.739 1.639 -0.201 -0.568 -0.257 55  PHE FFF CB  
5522  C CG  . PHE D 55  ? 2.204 1.672 1.628 -0.210 -0.591 -0.271 55  PHE FFF CG  
5523  C CD1 . PHE D 55  ? 2.400 1.837 1.796 -0.214 -0.624 -0.289 55  PHE FFF CD1 
5524  C CD2 . PHE D 55  ? 2.121 1.596 1.599 -0.216 -0.580 -0.266 55  PHE FFF CD2 
5525  C CE1 . PHE D 55  ? 2.516 1.930 1.942 -0.227 -0.647 -0.304 55  PHE FFF CE1 
5526  C CE2 . PHE D 55  ? 2.144 1.595 1.654 -0.227 -0.599 -0.278 55  PHE FFF CE2 
5527  C CZ  . PHE D 55  ? 2.398 1.817 1.882 -0.234 -0.633 -0.298 55  PHE FFF CZ  
5528  N N   . ASP D 56  ? 2.328 1.824 1.597 -0.178 -0.544 -0.249 56  ASP FFF N   
5529  C CA  . ASP D 56  ? 2.385 1.901 1.628 -0.177 -0.528 -0.233 56  ASP FFF CA  
5530  C C   . ASP D 56  ? 2.351 1.896 1.645 -0.194 -0.523 -0.217 56  ASP FFF C   
5531  O O   . ASP D 56  ? 2.224 1.768 1.564 -0.203 -0.539 -0.219 56  ASP FFF O   
5532  C CB  . ASP D 56  ? 2.584 2.073 1.767 -0.169 -0.546 -0.238 56  ASP FFF CB  
5533  C CG  . ASP D 56  ? 2.789 2.255 1.905 -0.151 -0.535 -0.249 56  ASP FFF CG  
5534  O OD1 . ASP D 56  ? 2.849 2.301 1.966 -0.143 -0.527 -0.262 56  ASP FFF OD1 
5535  O OD2 . ASP D 56  ? 2.911 2.371 1.972 -0.142 -0.531 -0.244 56  ASP FFF OD2 
5536  N N   . PRO D 57  ? 2.522 2.090 1.808 -0.199 -0.500 -0.202 57  PRO FFF N   
5537  C CA  . PRO D 57  ? 2.447 2.031 1.770 -0.216 -0.494 -0.191 57  PRO FFF CA  
5538  C C   . PRO D 57  ? 2.484 2.045 1.805 -0.215 -0.514 -0.188 57  PRO FFF C   
5539  O O   . PRO D 57  ? 2.600 2.143 1.876 -0.205 -0.525 -0.187 57  PRO FFF O   
5540  C CB  . PRO D 57  ? 2.407 2.014 1.710 -0.223 -0.465 -0.178 57  PRO FFF CB  
5541  C CG  . PRO D 57  ? 2.392 2.015 1.678 -0.211 -0.452 -0.181 57  PRO FFF CG  
5542  C CD  . PRO D 57  ? 2.536 2.121 1.788 -0.192 -0.473 -0.195 57  PRO FFF CD  
5543  N N   . VAL D 58  ? 2.234 1.801 1.607 -0.225 -0.519 -0.185 58  VAL FFF N   
5544  C CA  . VAL D 58  ? 2.252 1.806 1.638 -0.223 -0.534 -0.177 58  VAL FFF CA  
5545  C C   . VAL D 58  ? 2.282 1.840 1.684 -0.234 -0.508 -0.164 58  VAL FFF C   
5546  O O   . VAL D 58  ? 2.338 1.911 1.766 -0.247 -0.489 -0.166 58  VAL FFF O   
5547  C CB  . VAL D 58  ? 2.255 1.811 1.691 -0.223 -0.559 -0.182 58  VAL FFF CB  
5548  C CG1 . VAL D 58  ? 2.341 1.893 1.800 -0.219 -0.573 -0.169 58  VAL FFF CG1 
5549  C CG2 . VAL D 58  ? 2.512 2.057 1.928 -0.217 -0.585 -0.198 58  VAL FFF CG2 
5550  N N   . LEU D 59  ? 2.429 1.968 1.810 -0.229 -0.507 -0.152 59  LEU FFF N   
5551  C CA  . LEU D 59  ? 2.510 2.038 1.896 -0.240 -0.481 -0.141 59  LEU FFF CA  
5552  C C   . LEU D 59  ? 2.640 2.151 2.052 -0.229 -0.490 -0.129 59  LEU FFF C   
5553  O O   . LEU D 59  ? 2.746 2.255 2.157 -0.213 -0.520 -0.124 59  LEU FFF O   
5554  C CB  . LEU D 59  ? 2.561 2.078 1.894 -0.243 -0.463 -0.133 59  LEU FFF CB  
5555  C CG  . LEU D 59  ? 2.513 2.055 1.825 -0.253 -0.449 -0.141 59  LEU FFF CG  
5556  C CD1 . LEU D 59  ? 2.587 2.120 1.849 -0.252 -0.436 -0.130 59  LEU FFF CD1 
5557  C CD2 . LEU D 59  ? 2.560 2.123 1.900 -0.276 -0.426 -0.145 59  LEU FFF CD2 
5558  N N   . ALA D 60  ? 2.645 2.144 2.081 -0.236 -0.466 -0.123 60  ALA FFF N   
5559  C CA  . ALA D 60  ? 2.723 2.203 2.185 -0.222 -0.469 -0.107 60  ALA FFF CA  
5560  C C   . ALA D 60  ? 2.885 2.340 2.305 -0.209 -0.471 -0.089 60  ALA FFF C   
5561  O O   . ALA D 60  ? 3.012 2.456 2.383 -0.217 -0.459 -0.089 60  ALA FFF O   
5562  C CB  . ALA D 60  ? 2.657 2.121 2.146 -0.232 -0.436 -0.107 60  ALA FFF CB  
5563  N N   . ASP D 61  ? 2.943 2.391 2.385 -0.188 -0.486 -0.071 61  ASP FFF N   
5564  C CA  . ASP D 61  ? 2.904 2.329 2.305 -0.172 -0.491 -0.049 61  ASP FFF CA  
5565  C C   . ASP D 61  ? 2.950 2.333 2.327 -0.179 -0.450 -0.037 61  ASP FFF C   
5566  O O   . ASP D 61  ? 3.042 2.405 2.369 -0.176 -0.445 -0.025 61  ASP FFF O   
5567  C CB  . ASP D 61  ? 2.841 2.279 2.278 -0.147 -0.519 -0.028 61  ASP FFF CB  
5568  C CG  . ASP D 61  ? 3.058 2.528 2.484 -0.141 -0.567 -0.035 61  ASP FFF CG  
5569  O OD1 . ASP D 61  ? 3.085 2.562 2.479 -0.154 -0.574 -0.057 61  ASP FFF OD1 
5570  O OD2 . ASP D 61  ? 3.139 2.625 2.584 -0.123 -0.597 -0.017 61  ASP FFF OD2 
5571  N N   . SER D 62  ? 2.968 2.332 2.376 -0.189 -0.420 -0.042 62  SER FFF N   
5572  C CA  . SER D 62  ? 3.057 2.372 2.440 -0.199 -0.380 -0.034 62  SER FFF CA  
5573  C C   . SER D 62  ? 3.038 2.351 2.377 -0.229 -0.363 -0.050 62  SER FFF C   
5574  O O   . SER D 62  ? 3.108 2.381 2.421 -0.243 -0.331 -0.045 62  SER FFF O   
5575  C CB  . SER D 62  ? 3.024 2.316 2.446 -0.203 -0.351 -0.040 62  SER FFF CB  
5576  O OG  . SER D 62  ? 3.210 2.512 2.682 -0.174 -0.366 -0.024 62  SER FFF OG  
5577  N N   . VAL D 63  ? 2.983 2.340 2.317 -0.238 -0.381 -0.066 63  VAL FFF N   
5578  C CA  . VAL D 63  ? 3.014 2.385 2.319 -0.266 -0.366 -0.080 63  VAL FFF CA  
5579  C C   . VAL D 63  ? 3.140 2.540 2.414 -0.257 -0.389 -0.079 63  VAL FFF C   
5580  O O   . VAL D 63  ? 3.125 2.543 2.375 -0.273 -0.377 -0.085 63  VAL FFF O   
5581  C CB  . VAL D 63  ? 2.897 2.294 2.231 -0.288 -0.358 -0.102 63  VAL FFF CB  
5582  C CG1 . VAL D 63  ? 2.800 2.161 2.153 -0.297 -0.331 -0.105 63  VAL FFF CG1 
5583  C CG2 . VAL D 63  ? 2.869 2.305 2.235 -0.275 -0.387 -0.111 63  VAL FFF CG2 
5584  N N   . LYS D 64  ? 3.268 2.675 2.543 -0.230 -0.420 -0.072 64  LYS FFF N   
5585  C CA  . LYS D 64  ? 3.284 2.716 2.531 -0.221 -0.444 -0.079 64  LYS FFF CA  
5586  C C   . LYS D 64  ? 3.365 2.792 2.557 -0.226 -0.427 -0.071 64  LYS FFF C   
5587  O O   . LYS D 64  ? 3.321 2.774 2.494 -0.230 -0.427 -0.082 64  LYS FFF O   
5588  C CB  . LYS D 64  ? 3.324 2.755 2.570 -0.195 -0.480 -0.070 64  LYS FFF CB  
5589  C CG  . LYS D 64  ? 3.358 2.811 2.592 -0.186 -0.514 -0.085 64  LYS FFF CG  
5590  C CD  . LYS D 64  ? 3.349 2.823 2.641 -0.190 -0.531 -0.099 64  LYS FFF CD  
5591  C CE  . LYS D 64  ? 3.328 2.814 2.614 -0.178 -0.572 -0.108 64  LYS FFF CE  
5592  N NZ  . LYS D 64  ? 3.279 2.784 2.630 -0.182 -0.590 -0.117 64  LYS FFF NZ  
5593  N N   . GLY D 65  ? 3.614 3.008 2.782 -0.224 -0.411 -0.050 65  GLY FFF N   
5594  C CA  . GLY D 65  ? 3.650 3.038 2.768 -0.229 -0.391 -0.038 65  GLY FFF CA  
5595  C C   . GLY D 65  ? 3.649 3.048 2.772 -0.261 -0.359 -0.045 65  GLY FFF C   
5596  O O   . GLY D 65  ? 3.816 3.229 2.906 -0.268 -0.346 -0.039 65  GLY FFF O   
5597  N N   . ARG D 66  ? 3.357 2.755 2.520 -0.282 -0.347 -0.058 66  ARG FFF N   
5598  C CA  . ARG D 66  ? 3.285 2.687 2.450 -0.318 -0.317 -0.062 66  ARG FFF CA  
5599  C C   . ARG D 66  ? 3.176 2.628 2.368 -0.338 -0.318 -0.083 66  ARG FFF C   
5600  O O   . ARG D 66  ? 3.189 2.665 2.375 -0.364 -0.300 -0.083 66  ARG FFF O   
5601  C CB  . ARG D 66  ? 3.313 2.665 2.491 -0.332 -0.295 -0.059 66  ARG FFF CB  
5602  C CG  . ARG D 66  ? 3.339 2.640 2.499 -0.307 -0.294 -0.035 66  ARG FFF CG  
5603  C CD  . ARG D 66  ? 3.298 2.541 2.470 -0.316 -0.269 -0.031 66  ARG FFF CD  
5604  N NE  . ARG D 66  ? 3.282 2.524 2.496 -0.312 -0.274 -0.046 66  ARG FFF NE  
5605  C CZ  . ARG D 66  ? 3.327 2.556 2.556 -0.339 -0.253 -0.065 66  ARG FFF CZ  
5606  N NH1 . ARG D 66  ? 3.380 2.594 2.588 -0.377 -0.227 -0.073 66  ARG FFF NH1 
5607  N NH2 . ARG D 66  ? 3.283 2.514 2.548 -0.329 -0.258 -0.076 66  ARG FFF NH2 
5608  N N   . PHE D 67  ? 3.008 2.477 2.231 -0.326 -0.338 -0.097 67  PHE FFF N   
5609  C CA  . PHE D 67  ? 2.871 2.385 2.120 -0.342 -0.338 -0.113 67  PHE FFF CA  
5610  C C   . PHE D 67  ? 2.781 2.335 2.028 -0.324 -0.356 -0.116 67  PHE FFF C   
5611  O O   . PHE D 67  ? 2.876 2.417 2.105 -0.297 -0.375 -0.113 67  PHE FFF O   
5612  C CB  . PHE D 67  ? 2.906 2.413 2.193 -0.345 -0.342 -0.125 67  PHE FFF CB  
5613  C CG  . PHE D 67  ? 3.112 2.579 2.400 -0.367 -0.318 -0.127 67  PHE FFF CG  
5614  C CD1 . PHE D 67  ? 3.233 2.668 2.491 -0.384 -0.296 -0.117 67  PHE FFF CD1 
5615  C CD2 . PHE D 67  ? 3.102 2.559 2.419 -0.372 -0.314 -0.138 67  PHE FFF CD2 
5616  C CE1 . PHE D 67  ? 3.306 2.695 2.562 -0.405 -0.272 -0.121 67  PHE FFF CE1 
5617  C CE2 . PHE D 67  ? 3.140 2.553 2.452 -0.391 -0.288 -0.143 67  PHE FFF CE2 
5618  C CZ  . PHE D 67  ? 3.268 2.644 2.548 -0.408 -0.267 -0.135 67  PHE FFF CZ  
5619  N N   . THR D 68  ? 2.659 2.260 1.920 -0.338 -0.350 -0.123 68  THR FFF N   
5620  C CA  . THR D 68  ? 2.595 2.230 1.859 -0.319 -0.363 -0.127 68  THR FFF CA  
5621  C C   . THR D 68  ? 2.457 2.129 1.758 -0.331 -0.363 -0.136 68  THR FFF C   
5622  O O   . THR D 68  ? 2.476 2.168 1.789 -0.359 -0.349 -0.136 68  THR FFF O   
5623  C CB  . THR D 68  ? 2.601 2.265 1.837 -0.318 -0.349 -0.116 68  THR FFF CB  
5624  O OG1 . THR D 68  ? 2.763 2.392 1.962 -0.311 -0.345 -0.105 68  THR FFF OG1 
5625  C CG2 . THR D 68  ? 2.568 2.255 1.801 -0.292 -0.359 -0.120 68  THR FFF CG2 
5626  N N   . ILE D 69  ? 2.373 2.054 1.690 -0.310 -0.380 -0.143 69  ILE FFF N   
5627  C CA  . ILE D 69  ? 2.235 1.950 1.586 -0.315 -0.381 -0.148 69  ILE FFF CA  
5628  C C   . ILE D 69  ? 2.227 1.975 1.575 -0.297 -0.381 -0.144 69  ILE FFF C   
5629  O O   . ILE D 69  ? 2.288 2.015 1.614 -0.273 -0.390 -0.147 69  ILE FFF O   
5630  C CB  . ILE D 69  ? 2.151 1.842 1.532 -0.306 -0.397 -0.157 69  ILE FFF CB  
5631  C CG1 . ILE D 69  ? 2.169 1.893 1.583 -0.309 -0.396 -0.159 69  ILE FFF CG1 
5632  C CG2 . ILE D 69  ? 2.224 1.883 1.594 -0.281 -0.418 -0.161 69  ILE FFF CG2 
5633  C CD1 . ILE D 69  ? 2.148 1.852 1.595 -0.306 -0.406 -0.165 69  ILE FFF CD1 
5634  N N   . SER D 70  ? 2.202 2.003 1.569 -0.308 -0.370 -0.138 70  SER FFF N   
5635  C CA  . SER D 70  ? 2.249 2.085 1.618 -0.289 -0.365 -0.130 70  SER FFF CA  
5636  C C   . SER D 70  ? 2.187 2.066 1.592 -0.293 -0.363 -0.125 70  SER FFF C   
5637  O O   . SER D 70  ? 2.118 2.010 1.539 -0.317 -0.363 -0.127 70  SER FFF O   
5638  C CB  . SER D 70  ? 2.373 2.245 1.723 -0.294 -0.347 -0.116 70  SER FFF CB  
5639  O OG  . SER D 70  ? 2.502 2.408 1.862 -0.329 -0.337 -0.110 70  SER FFF OG  
5640  N N   . ILE D 71  ? 2.221 2.119 1.634 -0.267 -0.361 -0.119 71  ILE FFF N   
5641  C CA  . ILE D 71  ? 2.176 2.116 1.622 -0.265 -0.358 -0.109 71  ILE FFF CA  
5642  C C   . ILE D 71  ? 2.246 2.245 1.696 -0.251 -0.343 -0.089 71  ILE FFF C   
5643  O O   . ILE D 71  ? 2.358 2.342 1.789 -0.225 -0.336 -0.088 71  ILE FFF O   
5644  C CB  . ILE D 71  ? 1.998 1.900 1.460 -0.243 -0.369 -0.117 71  ILE FFF CB  
5645  C CG1 . ILE D 71  ? 1.976 1.836 1.447 -0.259 -0.383 -0.132 71  ILE FFF CG1 
5646  C CG2 . ILE D 71  ? 1.967 1.912 1.459 -0.233 -0.362 -0.101 71  ILE FFF CG2 
5647  C CD1 . ILE D 71  ? 1.928 1.759 1.423 -0.245 -0.394 -0.138 71  ILE FFF CD1 
5648  N N   . ASP D 72  ? 2.148 2.215 1.622 -0.268 -0.337 -0.073 72  ASP FFF N   
5649  C CA  . ASP D 72  ? 2.211 2.350 1.701 -0.256 -0.323 -0.048 72  ASP FFF CA  
5650  C C   . ASP D 72  ? 2.235 2.404 1.757 -0.241 -0.324 -0.034 72  ASP FFF C   
5651  O O   . ASP D 72  ? 2.293 2.497 1.831 -0.265 -0.330 -0.030 72  ASP FFF O   
5652  C CB  . ASP D 72  ? 2.330 2.534 1.825 -0.292 -0.317 -0.037 72  ASP FFF CB  
5653  C CG  . ASP D 72  ? 2.467 2.756 1.984 -0.279 -0.303 -0.007 72  ASP FFF CG  
5654  O OD1 . ASP D 72  ? 2.470 2.768 2.002 -0.240 -0.296 0.006  72  ASP FFF OD1 
5655  O OD2 . ASP D 72  ? 2.551 2.899 2.075 -0.308 -0.299 0.004  72  ASP FFF OD2 
5656  N N   . SER D 73  ? 2.325 2.475 1.852 -0.202 -0.317 -0.028 73  SER FFF N   
5657  C CA  . SER D 73  ? 2.366 2.539 1.924 -0.185 -0.315 -0.012 73  SER FFF CA  
5658  C C   . SER D 73  ? 2.452 2.726 2.038 -0.184 -0.305 0.022  73  SER FFF C   
5659  O O   . SER D 73  ? 2.583 2.892 2.193 -0.181 -0.307 0.039  73  SER FFF O   
5660  C CB  . SER D 73  ? 2.342 2.456 1.895 -0.143 -0.308 -0.016 73  SER FFF CB  
5661  O OG  . SER D 73  ? 2.246 2.374 1.829 -0.126 -0.304 0.002  73  SER FFF OG  
5662  N N   . ALA D 74  ? 2.493 2.815 2.075 -0.188 -0.295 0.033  74  ALA FFF N   
5663  C CA  . ALA D 74  ? 2.503 2.933 2.118 -0.191 -0.289 0.068  74  ALA FFF CA  
5664  C C   . ALA D 74  ? 2.483 2.965 2.107 -0.237 -0.305 0.069  74  ALA FFF C   
5665  O O   . ALA D 74  ? 2.390 2.936 2.040 -0.235 -0.309 0.093  74  ALA FFF O   
5666  C CB  . ALA D 74  ? 2.501 2.973 2.114 -0.190 -0.274 0.079  74  ALA FFF CB  
5667  N N   . GLU D 75  ? 2.534 2.984 2.132 -0.277 -0.315 0.044  75  GLU FFF N   
5668  C CA  . GLU D 75  ? 2.501 2.985 2.098 -0.323 -0.329 0.038  75  GLU FFF CA  
5669  C C   . GLU D 75  ? 2.395 2.816 1.981 -0.328 -0.338 0.018  75  GLU FFF C   
5670  O O   . GLU D 75  ? 2.573 3.010 2.149 -0.364 -0.347 0.010  75  GLU FFF O   
5671  C CB  . GLU D 75  ? 2.528 3.006 2.102 -0.366 -0.330 0.021  75  GLU FFF CB  
5672  C CG  . GLU D 75  ? 2.650 3.204 2.240 -0.372 -0.320 0.044  75  GLU FFF CG  
5673  C CD  . GLU D 75  ? 2.757 3.422 2.373 -0.402 -0.329 0.067  75  GLU FFF CD  
5674  O OE1 . GLU D 75  ? 2.744 3.414 2.351 -0.433 -0.343 0.056  75  GLU FFF OE1 
5675  O OE2 . GLU D 75  ? 2.891 3.641 2.538 -0.394 -0.321 0.096  75  GLU FFF OE2 
5676  N N   . ASN D 76  ? 2.215 2.565 1.800 -0.294 -0.336 0.009  76  ASN FFF N   
5677  C CA  . ASN D 76  ? 2.046 2.338 1.627 -0.296 -0.343 -0.007 76  ASN FFF CA  
5678  C C   . ASN D 76  ? 1.981 2.228 1.537 -0.333 -0.349 -0.035 76  ASN FFF C   
5679  O O   . ASN D 76  ? 2.001 2.244 1.555 -0.353 -0.353 -0.043 76  ASN FFF O   
5680  C CB  . ASN D 76  ? 2.039 2.382 1.640 -0.295 -0.345 0.014  76  ASN FFF CB  
5681  C CG  . ASN D 76  ? 2.041 2.371 1.665 -0.251 -0.338 0.032  76  ASN FFF CG  
5682  O OD1 . ASN D 76  ? 2.031 2.296 1.653 -0.225 -0.334 0.021  76  ASN FFF OD1 
5683  N ND2 . ASN D 76  ? 2.204 2.595 1.849 -0.243 -0.336 0.061  76  ASN FFF ND2 
5684  N N   . THR D 77  ? 2.052 2.263 1.588 -0.339 -0.348 -0.050 77  THR FFF N   
5685  C CA  . THR D 77  ? 2.104 2.275 1.617 -0.373 -0.350 -0.072 77  THR FFF CA  
5686  C C   . THR D 77  ? 2.177 2.267 1.675 -0.357 -0.352 -0.090 77  THR FFF C   
5687  O O   . THR D 77  ? 2.160 2.235 1.655 -0.329 -0.351 -0.086 77  THR FFF O   
5688  C CB  . THR D 77  ? 2.102 2.320 1.603 -0.409 -0.346 -0.069 77  THR FFF CB  
5689  O OG1 . THR D 77  ? 2.205 2.376 1.681 -0.442 -0.346 -0.092 77  THR FFF OG1 
5690  C CG2 . THR D 77  ? 2.165 2.393 1.663 -0.395 -0.339 -0.060 77  THR FFF CG2 
5691  N N   . LEU D 78  ? 2.168 2.208 1.654 -0.375 -0.355 -0.109 78  LEU FFF N   
5692  C CA  . LEU D 78  ? 2.156 2.125 1.629 -0.364 -0.359 -0.123 78  LEU FFF CA  
5693  C C   . LEU D 78  ? 2.296 2.246 1.744 -0.392 -0.352 -0.131 78  LEU FFF C   
5694  O O   . LEU D 78  ? 2.347 2.293 1.789 -0.420 -0.347 -0.140 78  LEU FFF O   
5695  C CB  . LEU D 78  ? 2.062 1.987 1.552 -0.356 -0.365 -0.134 78  LEU FFF CB  
5696  C CG  . LEU D 78  ? 2.046 1.905 1.527 -0.351 -0.371 -0.147 78  LEU FFF CG  
5697  C CD1 . LEU D 78  ? 2.078 1.910 1.558 -0.321 -0.383 -0.148 78  LEU FFF CD1 
5698  C CD2 . LEU D 78  ? 2.033 1.866 1.533 -0.355 -0.371 -0.155 78  LEU FFF CD2 
5699  N N   . ALA D 79  ? 2.307 2.242 1.737 -0.384 -0.350 -0.129 79  ALA FFF N   
5700  C CA  . ALA D 79  ? 2.291 2.210 1.697 -0.410 -0.340 -0.132 79  ALA FFF CA  
5701  C C   . ALA D 79  ? 2.321 2.167 1.711 -0.400 -0.344 -0.142 79  ALA FFF C   
5702  O O   . ALA D 79  ? 2.390 2.209 1.779 -0.369 -0.354 -0.142 79  ALA FFF O   
5703  C CB  . ALA D 79  ? 2.263 2.224 1.661 -0.410 -0.332 -0.117 79  ALA FFF CB  
5704  N N   . LEU D 80  ? 2.414 2.227 1.791 -0.425 -0.334 -0.149 80  LEU FFF N   
5705  C CA  . LEU D 80  ? 2.591 2.339 1.951 -0.416 -0.334 -0.153 80  LEU FFF CA  
5706  C C   . LEU D 80  ? 2.839 2.580 2.173 -0.443 -0.317 -0.148 80  LEU FFF C   
5707  O O   . LEU D 80  ? 2.931 2.670 2.261 -0.478 -0.305 -0.155 80  LEU FFF O   
5708  C CB  . LEU D 80  ? 2.475 2.179 1.847 -0.417 -0.333 -0.164 80  LEU FFF CB  
5709  C CG  . LEU D 80  ? 2.540 2.179 1.899 -0.407 -0.331 -0.163 80  LEU FFF CG  
5710  C CD1 . LEU D 80  ? 2.559 2.186 1.925 -0.370 -0.352 -0.158 80  LEU FFF CD1 
5711  C CD2 . LEU D 80  ? 2.476 2.077 1.844 -0.417 -0.320 -0.173 80  LEU FFF CD2 
5712  N N   . GLN D 81  ? 2.980 2.716 2.296 -0.429 -0.316 -0.137 81  GLN FFF N   
5713  C CA  . GLN D 81  ? 3.084 2.812 2.378 -0.454 -0.298 -0.128 81  GLN FFF CA  
5714  C C   . GLN D 81  ? 3.144 2.797 2.418 -0.450 -0.292 -0.129 81  GLN FFF C   
5715  O O   . GLN D 81  ? 3.142 2.766 2.398 -0.423 -0.297 -0.119 81  GLN FFF O   
5716  C CB  . GLN D 81  ? 3.109 2.874 2.392 -0.439 -0.296 -0.113 81  GLN FFF CB  
5717  C CG  . GLN D 81  ? 3.222 2.981 2.484 -0.462 -0.276 -0.100 81  GLN FFF CG  
5718  C CD  . GLN D 81  ? 3.350 3.163 2.627 -0.507 -0.264 -0.099 81  GLN FFF CD  
5719  O OE1 . GLN D 81  ? 3.422 3.307 2.717 -0.507 -0.264 -0.088 81  GLN FFF OE1 
5720  N NE2 . GLN D 81  ? 3.493 3.272 2.764 -0.544 -0.255 -0.109 81  GLN FFF NE2 
5721  N N   . MET D 82  ? 3.138 2.757 2.413 -0.476 -0.281 -0.140 82  MET FFF N   
5722  C CA  . MET D 82  ? 3.235 2.780 2.493 -0.474 -0.269 -0.138 82  MET FFF CA  
5723  C C   . MET D 82  ? 3.427 2.957 2.658 -0.493 -0.251 -0.124 82  MET FFF C   
5724  O O   . MET D 82  ? 3.592 3.149 2.820 -0.531 -0.238 -0.127 82  MET FFF O   
5725  C CB  . MET D 82  ? 3.217 2.729 2.480 -0.497 -0.257 -0.155 82  MET FFF CB  
5726  C CG  . MET D 82  ? 3.159 2.685 2.450 -0.478 -0.271 -0.166 82  MET FFF CG  
5727  S SD  . MET D 82  ? 3.228 2.722 2.520 -0.504 -0.253 -0.187 82  MET FFF SD  
5728  C CE  . MET D 82  ? 3.335 2.736 2.602 -0.509 -0.227 -0.185 82  MET FFF CE  
5729  N N   . ASN D 83  A 3.418 2.909 2.630 -0.466 -0.251 -0.109 82  ASN FFF N   
5730  C CA  . ASN D 83  A 3.385 2.856 2.570 -0.480 -0.231 -0.092 82  ASN FFF CA  
5731  C C   . ASN D 83  A 3.460 2.852 2.627 -0.466 -0.221 -0.081 82  ASN FFF C   
5732  O O   . ASN D 83  A 3.476 2.841 2.653 -0.436 -0.235 -0.082 82  ASN FFF O   
5733  C CB  . ASN D 83  A 3.277 2.791 2.449 -0.457 -0.239 -0.075 82  ASN FFF CB  
5734  C CG  . ASN D 83  A 3.208 2.801 2.401 -0.465 -0.247 -0.081 82  ASN FFF CG  
5735  O OD1 . ASN D 83  A 3.201 2.830 2.408 -0.503 -0.236 -0.086 82  ASN FFF OD1 
5736  N ND2 . ASN D 83  A 3.210 2.830 2.403 -0.429 -0.265 -0.080 82  ASN FFF ND2 
5737  N N   . ARG D 84  B 3.507 2.864 2.652 -0.487 -0.196 -0.067 82  ARG FFF N   
5738  C CA  . ARG D 84  B 3.636 2.913 2.762 -0.471 -0.183 -0.051 82  ARG FFF CA  
5739  C C   . ARG D 84  B 3.606 2.833 2.748 -0.470 -0.177 -0.067 82  ARG FFF C   
5740  O O   . ARG D 84  B 3.566 2.759 2.714 -0.434 -0.185 -0.058 82  ARG FFF O   
5741  C CB  . ARG D 84  B 3.663 2.938 2.771 -0.424 -0.200 -0.029 82  ARG FFF CB  
5742  C CG  . ARG D 84  B 3.774 2.980 2.856 -0.412 -0.181 -0.002 82  ARG FFF CG  
5743  C CD  . ARG D 84  B 3.815 3.018 2.880 -0.363 -0.203 0.019  82  ARG FFF CD  
5744  N NE  . ARG D 84  B 3.871 3.123 2.911 -0.357 -0.212 0.027  82  ARG FFF NE  
5745  C CZ  . ARG D 84  B 3.932 3.205 2.953 -0.320 -0.239 0.034  82  ARG FFF CZ  
5746  N NH1 . ARG D 84  B 3.985 3.242 3.012 -0.287 -0.263 0.037  82  ARG FFF NH1 
5747  N NH2 . ARG D 84  B 3.927 3.238 2.920 -0.316 -0.239 0.040  82  ARG FFF NH2 
5748  N N   . LEU D 85  C 3.724 2.951 2.873 -0.511 -0.164 -0.090 82  LEU FFF N   
5749  C CA  . LEU D 85  C 3.758 2.947 2.921 -0.512 -0.157 -0.110 82  LEU FFF CA  
5750  C C   . LEU D 85  C 3.827 2.922 2.977 -0.502 -0.131 -0.099 82  LEU FFF C   
5751  O O   . LEU D 85  C 4.012 3.060 3.136 -0.518 -0.107 -0.085 82  LEU FFF O   
5752  C CB  . LEU D 85  C 3.781 2.988 2.941 -0.565 -0.146 -0.136 82  LEU FFF CB  
5753  C CG  . LEU D 85  C 3.678 2.976 2.859 -0.576 -0.169 -0.150 82  LEU FFF CG  
5754  C CD1 . LEU D 85  C 3.738 3.049 2.909 -0.633 -0.156 -0.172 82  LEU FFF CD1 
5755  C CD2 . LEU D 85  C 3.559 2.873 2.765 -0.542 -0.188 -0.157 82  LEU FFF CD2 
5756  N N   . LYS D 86  ? 3.654 2.720 2.822 -0.473 -0.132 -0.103 83  LYS FFF N   
5757  C CA  . LYS D 86  ? 3.687 2.669 2.853 -0.452 -0.108 -0.092 83  LYS FFF CA  
5758  C C   . LYS D 86  ? 3.719 2.659 2.889 -0.468 -0.086 -0.119 83  LYS FFF C   
5759  O O   . LYS D 86  ? 3.714 2.701 2.896 -0.485 -0.097 -0.143 83  LYS FFF O   
5760  C CB  . LYS D 86  ? 3.615 2.608 2.803 -0.395 -0.131 -0.065 83  LYS FFF CB  
5761  C CG  . LYS D 86  ? 3.554 2.576 2.722 -0.381 -0.149 -0.040 83  LYS FFF CG  
5762  C CD  . LYS D 86  ? 3.438 2.459 2.616 -0.329 -0.170 -0.010 83  LYS FFF CD  
5763  C CE  . LYS D 86  ? 3.346 2.415 2.502 -0.318 -0.196 0.006  83  LYS FFF CE  
5764  N NZ  . LYS D 86  ? 3.280 2.355 2.439 -0.270 -0.222 0.032  83  LYS FFF NZ  
5765  N N   . PRO D 87  ? 3.775 2.624 2.935 -0.461 -0.051 -0.113 84  PRO FFF N   
5766  C CA  . PRO D 87  ? 3.789 2.591 2.949 -0.470 -0.025 -0.139 84  PRO FFF CA  
5767  C C   . PRO D 87  ? 3.726 2.571 2.928 -0.435 -0.044 -0.144 84  PRO FFF C   
5768  O O   . PRO D 87  ? 3.679 2.523 2.879 -0.453 -0.033 -0.172 84  PRO FFF O   
5769  C CB  . PRO D 87  ? 3.786 2.481 2.931 -0.453 0.014  -0.123 84  PRO FFF CB  
5770  C CG  . PRO D 87  ? 3.813 2.494 2.933 -0.467 0.017  -0.101 84  PRO FFF CG  
5771  C CD  . PRO D 87  ? 3.824 2.603 2.962 -0.450 -0.028 -0.085 84  PRO FFF CD  
5772  N N   . GLU D 88  ? 3.699 2.580 2.935 -0.387 -0.071 -0.116 85  GLU FFF N   
5773  C CA  . GLU D 88  ? 3.681 2.610 2.962 -0.358 -0.090 -0.119 85  GLU FFF CA  
5774  C C   . GLU D 88  ? 3.697 2.705 2.984 -0.383 -0.116 -0.142 85  GLU FFF C   
5775  O O   . GLU D 88  ? 3.633 2.675 2.954 -0.368 -0.127 -0.150 85  GLU FFF O   
5776  C CB  . GLU D 88  ? 3.629 2.588 2.947 -0.307 -0.119 -0.086 85  GLU FFF CB  
5777  C CG  . GLU D 88  ? 3.645 2.537 2.967 -0.273 -0.096 -0.056 85  GLU FFF CG  
5778  C CD  . GLU D 88  ? 3.674 2.523 2.954 -0.282 -0.085 -0.038 85  GLU FFF CD  
5779  O OE1 . GLU D 88  ? 3.684 2.575 2.941 -0.304 -0.106 -0.041 85  GLU FFF OE1 
5780  O OE2 . GLU D 88  ? 3.597 2.370 2.868 -0.265 -0.053 -0.019 85  GLU FFF OE2 
5781  N N   . ASP D 89  ? 3.879 2.916 3.138 -0.419 -0.124 -0.152 86  ASP FFF N   
5782  C CA  . ASP D 89  ? 3.792 2.904 3.058 -0.440 -0.147 -0.170 86  ASP FFF CA  
5783  C C   . ASP D 89  ? 3.769 2.870 3.020 -0.475 -0.126 -0.200 86  ASP FFF C   
5784  O O   . ASP D 89  ? 3.674 2.839 2.932 -0.492 -0.143 -0.213 86  ASP FFF O   
5785  C CB  . ASP D 89  ? 3.809 2.965 3.055 -0.464 -0.162 -0.166 86  ASP FFF CB  
5786  C CG  . ASP D 89  ? 3.729 2.907 2.983 -0.430 -0.186 -0.139 86  ASP FFF CG  
5787  O OD1 . ASP D 89  ? 3.724 2.890 3.001 -0.390 -0.196 -0.124 86  ASP FFF OD1 
5788  O OD2 . ASP D 89  ? 3.629 2.838 2.865 -0.443 -0.194 -0.132 86  ASP FFF OD2 
5789  N N   . THR D 90  ? 3.797 2.818 3.024 -0.489 -0.089 -0.212 87  THR FFF N   
5790  C CA  . THR D 90  ? 3.768 2.778 2.973 -0.522 -0.071 -0.244 87  THR FFF CA  
5791  C C   . THR D 90  ? 3.666 2.717 2.909 -0.492 -0.082 -0.245 87  THR FFF C   
5792  O O   . THR D 90  ? 3.648 2.670 2.920 -0.452 -0.073 -0.232 87  THR FFF O   
5793  C CB  . THR D 90  ? 3.786 2.690 2.955 -0.536 -0.026 -0.257 87  THR FFF CB  
5794  O OG1 . THR D 90  ? 3.704 2.566 2.841 -0.564 -0.014 -0.253 87  THR FFF OG1 
5795  C CG2 . THR D 90  ? 3.819 2.708 2.956 -0.572 -0.007 -0.294 87  THR FFF CG2 
5796  N N   . ALA D 91  ? 3.571 2.689 2.815 -0.513 -0.100 -0.259 88  ALA FFF N   
5797  C CA  . ALA D 91  ? 3.456 2.617 2.735 -0.488 -0.111 -0.259 88  ALA FFF CA  
5798  C C   . ALA D 91  ? 3.386 2.617 2.655 -0.519 -0.128 -0.274 88  ALA FFF C   
5799  O O   . ALA D 91  ? 3.420 2.677 2.662 -0.555 -0.136 -0.280 88  ALA FFF O   
5800  C CB  . ALA D 91  ? 3.429 2.629 2.761 -0.442 -0.140 -0.231 88  ALA FFF CB  
5801  N N   . VAL D 92  ? 3.283 2.546 2.575 -0.505 -0.131 -0.276 89  VAL FFF N   
5802  C CA  . VAL D 92  ? 3.147 2.486 2.441 -0.521 -0.151 -0.281 89  VAL FFF CA  
5803  C C   . VAL D 92  ? 3.110 2.511 2.452 -0.490 -0.186 -0.258 89  VAL FFF C   
5804  O O   . VAL D 92  ? 3.122 2.516 2.505 -0.453 -0.191 -0.244 89  VAL FFF O   
5805  C CB  . VAL D 92  ? 3.105 2.443 2.396 -0.521 -0.134 -0.294 89  VAL FFF CB  
5806  C CG1 . VAL D 92  ? 3.021 2.432 2.301 -0.544 -0.151 -0.299 89  VAL FFF CG1 
5807  C CG2 . VAL D 92  ? 3.232 2.489 2.473 -0.542 -0.094 -0.318 89  VAL FFF CG2 
5808  N N   . TYR D 93  ? 3.050 2.512 2.388 -0.507 -0.208 -0.254 90  TYR FFF N   
5809  C CA  . TYR D 93  ? 2.919 2.430 2.292 -0.480 -0.238 -0.235 90  TYR FFF CA  
5810  C C   . TYR D 93  ? 2.768 2.341 2.160 -0.478 -0.251 -0.233 90  TYR FFF C   
5811  O O   . TYR D 93  ? 2.803 2.410 2.171 -0.508 -0.248 -0.242 90  TYR FFF O   
5812  C CB  . TYR D 93  ? 2.947 2.476 2.303 -0.492 -0.250 -0.228 90  TYR FFF CB  
5813  C CG  . TYR D 93  ? 3.042 2.514 2.387 -0.483 -0.241 -0.222 90  TYR FFF CG  
5814  C CD1 . TYR D 93  ? 3.183 2.593 2.497 -0.506 -0.214 -0.232 90  TYR FFF CD1 
5815  C CD2 . TYR D 93  ? 3.019 2.494 2.381 -0.453 -0.260 -0.204 90  TYR FFF CD2 
5816  C CE1 . TYR D 93  ? 3.291 2.645 2.595 -0.495 -0.205 -0.223 90  TYR FFF CE1 
5817  C CE2 . TYR D 93  ? 3.174 2.599 2.523 -0.443 -0.253 -0.195 90  TYR FFF CE2 
5818  C CZ  . TYR D 93  ? 3.299 2.665 2.622 -0.463 -0.225 -0.202 90  TYR FFF CZ  
5819  O OH  . TYR D 93  ? 3.496 2.810 2.806 -0.451 -0.215 -0.189 90  TYR FFF OH  
5820  N N   . TYR D 94  ? 2.641 2.231 2.075 -0.446 -0.266 -0.221 91  TYR FFF N   
5821  C CA  . TYR D 94  ? 2.521 2.163 1.978 -0.440 -0.276 -0.215 91  TYR FFF CA  
5822  C C   . TYR D 94  ? 2.402 2.082 1.885 -0.419 -0.303 -0.201 91  TYR FFF C   
5823  O O   . TYR D 94  ? 2.387 2.045 1.888 -0.397 -0.315 -0.195 91  TYR FFF O   
5824  C CB  . TYR D 94  ? 2.550 2.175 2.040 -0.421 -0.266 -0.214 91  TYR FFF CB  
5825  C CG  . TYR D 94  ? 2.743 2.319 2.210 -0.432 -0.235 -0.228 91  TYR FFF CG  
5826  C CD1 . TYR D 94  ? 2.848 2.366 2.317 -0.420 -0.223 -0.228 91  TYR FFF CD1 
5827  C CD2 . TYR D 94  ? 2.834 2.418 2.276 -0.451 -0.217 -0.239 91  TYR FFF CD2 
5828  C CE1 . TYR D 94  ? 2.979 2.445 2.426 -0.426 -0.190 -0.241 91  TYR FFF CE1 
5829  C CE2 . TYR D 94  ? 2.898 2.429 2.313 -0.460 -0.185 -0.254 91  TYR FFF CE2 
5830  C CZ  . TYR D 94  ? 2.994 2.464 2.413 -0.447 -0.170 -0.256 91  TYR FFF CZ  
5831  O OH  . TYR D 94  ? 3.058 2.467 2.449 -0.452 -0.134 -0.271 91  TYR FFF OH  
5832  N N   . CYS D 95  ? 2.244 1.978 1.728 -0.425 -0.311 -0.195 92  CYS FFF N   
5833  C CA  . CYS D 95  ? 2.186 1.947 1.696 -0.401 -0.331 -0.182 92  CYS FFF CA  
5834  C C   . CYS D 95  ? 2.052 1.825 1.599 -0.385 -0.333 -0.175 92  CYS FFF C   
5835  O O   . CYS D 95  ? 2.025 1.808 1.570 -0.396 -0.319 -0.177 92  CYS FFF O   
5836  C CB  . CYS D 95  ? 2.262 2.077 1.758 -0.410 -0.338 -0.174 92  CYS FFF CB  
5837  S SG  . CYS D 95  ? 2.726 2.596 2.207 -0.437 -0.328 -0.172 92  CYS FFF SG  
5838  N N   . PHE D 96  ? 2.000 1.769 1.578 -0.361 -0.350 -0.168 93  PHE FFF N   
5839  C CA  . PHE D 96  ? 1.904 1.685 1.520 -0.348 -0.353 -0.160 93  PHE FFF CA  
5840  C C   . PHE D 96  ? 1.820 1.619 1.448 -0.332 -0.368 -0.151 93  PHE FFF C   
5841  O O   . PHE D 96  ? 1.858 1.648 1.471 -0.324 -0.380 -0.154 93  PHE FFF O   
5842  C CB  . PHE D 96  ? 1.928 1.674 1.581 -0.335 -0.355 -0.161 93  PHE FFF CB  
5843  C CG  . PHE D 96  ? 1.944 1.667 1.609 -0.320 -0.377 -0.162 93  PHE FFF CG  
5844  C CD1 . PHE D 96  ? 1.868 1.595 1.558 -0.306 -0.396 -0.158 93  PHE FFF CD1 
5845  C CD2 . PHE D 96  ? 1.956 1.651 1.604 -0.319 -0.380 -0.168 93  PHE FFF CD2 
5846  C CE1 . PHE D 96  ? 1.788 1.493 1.481 -0.295 -0.418 -0.162 93  PHE FFF CE1 
5847  C CE2 . PHE D 96  ? 1.981 1.658 1.633 -0.305 -0.402 -0.168 93  PHE FFF CE2 
5848  C CZ  . PHE D 96  ? 1.859 1.543 1.532 -0.294 -0.422 -0.166 93  PHE FFF CZ  
5849  N N   . ALA D 97  ? 1.727 1.549 1.378 -0.325 -0.366 -0.140 94  ALA FFF N   
5850  C CA  . ALA D 97  ? 1.673 1.502 1.338 -0.307 -0.377 -0.131 94  ALA FFF CA  
5851  C C   . ALA D 97  ? 1.683 1.500 1.393 -0.298 -0.377 -0.124 94  ALA FFF C   
5852  O O   . ALA D 97  ? 1.815 1.643 1.538 -0.305 -0.363 -0.118 94  ALA FFF O   
5853  C CB  . ALA D 97  ? 1.689 1.566 1.337 -0.308 -0.370 -0.118 94  ALA FFF CB  
5854  N N   . ALA D 98  ? 1.578 1.371 1.308 -0.284 -0.392 -0.125 95  ALA FFF N   
5855  C CA  . ALA D 98  ? 1.630 1.411 1.407 -0.280 -0.392 -0.118 95  ALA FFF CA  
5856  C C   . ALA D 98  ? 1.667 1.451 1.455 -0.267 -0.390 -0.106 95  ALA FFF C   
5857  O O   . ALA D 98  ? 1.686 1.448 1.464 -0.255 -0.402 -0.112 95  ALA FFF O   
5858  C CB  . ALA D 98  ? 1.576 1.323 1.380 -0.279 -0.411 -0.130 95  ALA FFF CB  
5859  N N   . LEU D 99  ? 1.700 1.508 1.506 -0.267 -0.373 -0.087 96  LEU FFF N   
5860  C CA  . LEU D 99  ? 1.748 1.553 1.574 -0.253 -0.368 -0.071 96  LEU FFF CA  
5861  C C   . LEU D 99  ? 1.921 1.727 1.788 -0.260 -0.357 -0.058 96  LEU FFF C   
5862  O O   . LEU D 99  ? 2.135 1.973 1.993 -0.268 -0.342 -0.050 96  LEU FFF O   
5863  C CB  . LEU D 99  ? 1.769 1.614 1.567 -0.243 -0.357 -0.053 96  LEU FFF CB  
5864  C CG  . LEU D 99  ? 1.936 1.769 1.741 -0.220 -0.352 -0.038 96  LEU FFF CG  
5865  C CD1 . LEU D 99  ? 2.052 1.926 1.824 -0.209 -0.348 -0.029 96  LEU FFF CD1 
5866  C CD2 . LEU D 99  ? 2.058 1.895 1.895 -0.212 -0.337 -0.012 96  LEU FFF CD2 
5867  N N   . ASP D 100 ? 1.973 1.746 1.882 -0.258 -0.362 -0.057 97  ASP FFF N   
5868  C CA  . ASP D 100 ? 2.075 1.851 2.031 -0.264 -0.349 -0.042 97  ASP FFF CA  
5869  C C   . ASP D 100 ? 1.855 1.655 1.810 -0.275 -0.337 -0.043 97  ASP FFF C   
5870  O O   . ASP D 100 ? 1.817 1.638 1.785 -0.277 -0.316 -0.025 97  ASP FFF O   
5871  C CB  . ASP D 100 ? 2.288 2.079 2.252 -0.254 -0.328 -0.013 97  ASP FFF CB  
5872  C CG  . ASP D 100 ? 2.522 2.360 2.440 -0.248 -0.315 0.000  97  ASP FFF CG  
5873  O OD1 . ASP D 100 ? 2.465 2.336 2.370 -0.257 -0.302 0.007  97  ASP FFF OD1 
5874  O OD2 . ASP D 100 ? 2.810 2.652 2.707 -0.234 -0.318 0.006  97  ASP FFF OD2 
5875  N N   . THR D 101 ? 1.786 1.583 1.719 -0.281 -0.348 -0.063 98  THR FFF N   
5876  C CA  . THR D 101 ? 1.720 1.522 1.652 -0.290 -0.341 -0.071 98  THR FFF CA  
5877  C C   . THR D 101 ? 1.642 1.467 1.516 -0.295 -0.330 -0.075 98  THR FFF C   
5878  O O   . THR D 101 ? 1.640 1.469 1.477 -0.294 -0.340 -0.082 98  THR FFF O   
5879  C CB  . THR D 101 ? 1.857 1.667 1.830 -0.293 -0.320 -0.058 98  THR FFF CB  
5880  O OG1 . THR D 101 ? 1.882 1.687 1.851 -0.297 -0.316 -0.071 98  THR FFF OG1 
5881  C CG2 . THR D 101 ? 1.896 1.735 1.848 -0.294 -0.293 -0.041 98  THR FFF CG2 
5882  N N   . ALA D 104 ? 1.752 1.536 1.639 -0.302 -0.336 -0.104 101 ALA FFF N   
5883  C CA  . ALA D 104 ? 1.809 1.598 1.640 -0.306 -0.342 -0.113 101 ALA FFF CA  
5884  C C   . ALA D 104 ? 1.870 1.681 1.658 -0.318 -0.319 -0.113 101 ALA FFF C   
5885  O O   . ALA D 104 ? 2.035 1.849 1.830 -0.322 -0.298 -0.109 101 ALA FFF O   
5886  C CB  . ALA D 104 ? 1.924 1.688 1.739 -0.305 -0.357 -0.128 101 ALA FFF CB  
5887  N N   . TYR D 105 ? 1.858 1.683 1.600 -0.325 -0.324 -0.118 102 TYR FFF N   
5888  C CA  . TYR D 105 ? 1.843 1.693 1.539 -0.342 -0.309 -0.120 102 TYR FFF CA  
5889  C C   . TYR D 105 ? 1.929 1.761 1.587 -0.356 -0.310 -0.138 102 TYR FFF C   
5890  O O   . TYR D 105 ? 1.969 1.786 1.626 -0.350 -0.326 -0.144 102 TYR FFF O   
5891  C CB  . TYR D 105 ? 1.722 1.617 1.402 -0.342 -0.313 -0.106 102 TYR FFF CB  
5892  C CG  . TYR D 105 ? 1.678 1.589 1.393 -0.327 -0.311 -0.084 102 TYR FFF CG  
5893  C CD1 . TYR D 105 ? 1.786 1.699 1.518 -0.328 -0.293 -0.075 102 TYR FFF CD1 
5894  C CD2 . TYR D 105 ? 1.632 1.551 1.360 -0.311 -0.323 -0.072 102 TYR FFF CD2 
5895  C CE1 . TYR D 105 ? 1.792 1.717 1.556 -0.315 -0.288 -0.052 102 TYR FFF CE1 
5896  C CE2 . TYR D 105 ? 1.664 1.591 1.424 -0.297 -0.318 -0.051 102 TYR FFF CE2 
5897  C CZ  . TYR D 105 ? 1.672 1.602 1.451 -0.300 -0.301 -0.040 102 TYR FFF CZ  
5898  O OH  . TYR D 105 ? 1.556 1.490 1.366 -0.287 -0.294 -0.016 102 TYR FFF OH  
5899  N N   . TRP D 106 ? 1.935 1.765 1.558 -0.375 -0.291 -0.148 103 TRP FFF N   
5900  C CA  . TRP D 106 ? 2.034 1.838 1.620 -0.391 -0.286 -0.166 103 TRP FFF CA  
5901  C C   . TRP D 106 ? 2.097 1.932 1.631 -0.419 -0.280 -0.172 103 TRP FFF C   
5902  O O   . TRP D 106 ? 2.043 1.910 1.564 -0.427 -0.272 -0.166 103 TRP FFF O   
5903  C CB  . TRP D 106 ? 2.086 1.843 1.677 -0.389 -0.267 -0.176 103 TRP FFF CB  
5904  C CG  . TRP D 106 ? 2.060 1.794 1.705 -0.364 -0.277 -0.169 103 TRP FFF CG  
5905  C CD1 . TRP D 106 ? 2.053 1.795 1.749 -0.348 -0.277 -0.156 103 TRP FFF CD1 
5906  C CD2 . TRP D 106 ? 2.095 1.797 1.747 -0.355 -0.289 -0.173 103 TRP FFF CD2 
5907  N NE1 . TRP D 106 ? 2.057 1.779 1.794 -0.331 -0.292 -0.153 103 TRP FFF NE1 
5908  C CE2 . TRP D 106 ? 2.053 1.751 1.762 -0.334 -0.300 -0.162 103 TRP FFF CE2 
5909  C CE3 . TRP D 106 ? 2.183 1.863 1.800 -0.363 -0.293 -0.182 103 TRP FFF CE3 
5910  C CZ2 . TRP D 106 ? 2.057 1.733 1.786 -0.320 -0.316 -0.161 103 TRP FFF CZ2 
5911  C CZ3 . TRP D 106 ? 2.191 1.845 1.826 -0.347 -0.306 -0.179 103 TRP FFF CZ3 
5912  C CH2 . TRP D 106 ? 2.114 1.767 1.803 -0.326 -0.319 -0.169 103 TRP FFF CH2 
5913  N N   . GLY D 107 ? 2.225 2.052 1.729 -0.435 -0.285 -0.183 104 GLY FFF N   
5914  C CA  . GLY D 107 ? 2.249 2.095 1.704 -0.469 -0.278 -0.194 104 GLY FFF CA  
5915  C C   . GLY D 107 ? 2.355 2.152 1.775 -0.488 -0.254 -0.215 104 GLY FFF C   
5916  O O   . GLY D 107 ? 2.299 2.050 1.737 -0.472 -0.239 -0.219 104 GLY FFF O   
5917  N N   . GLN D 108 ? 2.431 2.240 1.800 -0.525 -0.248 -0.229 105 GLN FFF N   
5918  C CA  . GLN D 108 ? 2.492 2.247 1.819 -0.546 -0.223 -0.253 105 GLN FFF CA  
5919  C C   . GLN D 108 ? 2.416 2.107 1.730 -0.553 -0.214 -0.268 105 GLN FFF C   
5920  O O   . GLN D 108 ? 2.432 2.061 1.721 -0.560 -0.188 -0.286 105 GLN FFF O   
5921  C CB  . GLN D 108 ? 2.566 2.357 1.837 -0.589 -0.222 -0.266 105 GLN FFF CB  
5922  C CG  . GLN D 108 ? 2.698 2.551 1.964 -0.589 -0.227 -0.253 105 GLN FFF CG  
5923  C CD  . GLN D 108 ? 2.866 2.693 2.141 -0.566 -0.206 -0.251 105 GLN FFF CD  
5924  O OE1 . GLN D 108 ? 2.945 2.761 2.274 -0.530 -0.205 -0.235 105 GLN FFF OE1 
5925  N NE2 . GLN D 108 ? 2.934 2.751 2.155 -0.589 -0.187 -0.268 105 GLN FFF NE2 
5926  N N   . GLY D 109 ? 2.524 2.227 1.853 -0.551 -0.231 -0.259 106 GLY FFF N   
5927  C CA  . GLY D 109 ? 2.636 2.281 1.958 -0.552 -0.224 -0.266 106 GLY FFF CA  
5928  C C   . GLY D 109 ? 2.663 2.309 1.940 -0.596 -0.222 -0.280 106 GLY FFF C   
5929  O O   . GLY D 109 ? 2.699 2.380 1.944 -0.630 -0.222 -0.290 106 GLY FFF O   
5930  N N   . THR D 110 ? 2.684 2.297 1.961 -0.596 -0.222 -0.278 107 THR FFF N   
5931  C CA  . THR D 110 ? 2.881 2.482 2.118 -0.640 -0.216 -0.291 107 THR FFF CA  
5932  C C   . THR D 110 ? 3.088 2.597 2.310 -0.638 -0.193 -0.299 107 THR FFF C   
5933  O O   . THR D 110 ? 3.068 2.550 2.320 -0.600 -0.195 -0.284 107 THR FFF O   
5934  C CB  . THR D 110 ? 2.795 2.464 2.046 -0.647 -0.238 -0.274 107 THR FFF CB  
5935  O OG1 . THR D 110 ? 2.893 2.559 2.110 -0.696 -0.232 -0.285 107 THR FFF OG1 
5936  C CG2 . THR D 110 ? 2.860 2.517 2.144 -0.609 -0.247 -0.254 107 THR FFF CG2 
5937  N N   . GLN D 111 ? 3.301 2.762 2.476 -0.678 -0.171 -0.322 108 GLN FFF N   
5938  C CA  . GLN D 111 ? 3.480 2.843 2.638 -0.675 -0.144 -0.330 108 GLN FFF CA  
5939  C C   . GLN D 111 ? 3.540 2.896 2.698 -0.685 -0.149 -0.318 108 GLN FFF C   
5940  O O   . GLN D 111 ? 3.593 2.992 2.736 -0.725 -0.159 -0.321 108 GLN FFF O   
5941  C CB  . GLN D 111 ? 3.645 2.947 2.747 -0.715 -0.115 -0.363 108 GLN FFF CB  
5942  C CG  . GLN D 111 ? 3.690 2.883 2.765 -0.719 -0.082 -0.373 108 GLN FFF CG  
5943  C CD  . GLN D 111 ? 3.653 2.784 2.749 -0.670 -0.059 -0.367 108 GLN FFF CD  
5944  O OE1 . GLN D 111 ? 3.587 2.716 2.680 -0.658 -0.048 -0.377 108 GLN FFF OE1 
5945  N NE2 . GLN D 111 ? 3.696 2.782 2.815 -0.639 -0.052 -0.348 108 GLN FFF NE2 
5946  N N   . VAL D 112 ? 3.567 2.875 2.745 -0.649 -0.143 -0.301 109 VAL FFF N   
5947  C CA  . VAL D 112 ? 3.593 2.883 2.767 -0.655 -0.143 -0.287 109 VAL FFF CA  
5948  C C   . VAL D 112 ? 3.739 2.922 2.893 -0.649 -0.111 -0.290 109 VAL FFF C   
5949  O O   . VAL D 112 ? 3.840 2.985 3.014 -0.607 -0.102 -0.283 109 VAL FFF O   
5950  C CB  . VAL D 112 ? 3.463 2.804 2.676 -0.615 -0.170 -0.259 109 VAL FFF CB  
5951  C CG1 . VAL D 112 ? 3.446 2.753 2.649 -0.614 -0.164 -0.243 109 VAL FFF CG1 
5952  C CG2 . VAL D 112 ? 3.394 2.833 2.621 -0.626 -0.196 -0.255 109 VAL FFF CG2 
5953  N N   . THR D 113 ? 3.811 2.949 2.930 -0.690 -0.092 -0.299 110 THR FFF N   
5954  C CA  . THR D 113 ? 3.825 2.852 2.919 -0.690 -0.056 -0.304 110 THR FFF CA  
5955  C C   . THR D 113 ? 3.822 2.835 2.909 -0.704 -0.054 -0.285 110 THR FFF C   
5956  O O   . THR D 113 ? 3.838 2.885 2.909 -0.752 -0.059 -0.292 110 THR FFF O   
5957  C CB  . THR D 113 ? 3.901 2.867 2.946 -0.735 -0.027 -0.340 110 THR FFF CB  
5958  O OG1 . THR D 113 ? 3.978 2.986 3.026 -0.732 -0.035 -0.357 110 THR FFF OG1 
5959  C CG2 . THR D 113 ? 3.956 2.798 2.981 -0.720 0.016  -0.344 110 THR FFF CG2 
5960  N N   . VAL D 114 ? 3.825 2.793 2.926 -0.662 -0.047 -0.259 111 VAL FFF N   
5961  C CA  . VAL D 114 ? 3.858 2.806 2.950 -0.669 -0.041 -0.237 111 VAL FFF CA  
5962  C C   . VAL D 114 ? 3.951 2.779 3.015 -0.672 -0.000 -0.236 111 VAL FFF C   
5963  O O   . VAL D 114 ? 3.917 2.690 2.992 -0.627 0.014  -0.226 111 VAL FFF O   
5964  C CB  . VAL D 114 ? 3.787 2.785 2.911 -0.619 -0.068 -0.203 111 VAL FFF CB  
5965  C CG1 . VAL D 114 ? 3.847 2.840 2.957 -0.632 -0.063 -0.181 111 VAL FFF CG1 
5966  C CG2 . VAL D 114 ? 3.762 2.865 2.914 -0.610 -0.104 -0.206 111 VAL FFF CG2 
5967  N N   . SER D 115 ? 4.022 2.812 3.054 -0.725 0.020  -0.246 112 SER FFF N   
5968  C CA  . SER D 115 ? 4.103 2.784 3.109 -0.732 0.057  -0.236 112 SER FFF CA  
5969  C C   . SER D 115 ? 4.188 2.850 3.161 -0.807 0.072  -0.256 112 SER FFF C   
5970  O O   . SER D 115 ? 4.251 2.894 3.218 -0.823 0.083  -0.235 112 SER FFF O   
5971  C CB  . SER D 115 ? 4.176 2.752 3.169 -0.707 0.092  -0.247 112 SER FFF CB  
5972  O OG  . SER D 115 ? 4.236 2.729 3.225 -0.679 0.119  -0.217 112 SER FFF OG  
5973  N N   . ASP E 1   ? 3.322 2.674 2.418 0.489  -0.012 -0.300 1   ASP EEE N   
5974  C CA  . ASP E 1   ? 3.377 2.819 2.522 0.502  0.051  -0.291 1   ASP EEE CA  
5975  C C   . ASP E 1   ? 3.404 2.916 2.619 0.489  0.071  -0.286 1   ASP EEE C   
5976  O O   . ASP E 1   ? 3.449 2.923 2.649 0.478  0.045  -0.289 1   ASP EEE O   
5977  C CB  . ASP E 1   ? 3.389 2.766 2.432 0.543  0.094  -0.284 1   ASP EEE CB  
5978  C CG  . ASP E 1   ? 3.302 2.770 2.408 0.555  0.151  -0.272 1   ASP EEE CG  
5979  O OD1 . ASP E 1   ? 3.266 2.824 2.465 0.535  0.149  -0.273 1   ASP EEE OD1 
5980  O OD2 . ASP E 1   ? 3.414 2.862 2.477 0.585  0.197  -0.260 1   ASP EEE OD2 
5981  N N   . VAL E 2   ? 3.301 2.908 2.588 0.489  0.114  -0.278 2   VAL EEE N   
5982  C CA  . VAL E 2   ? 3.141 2.810 2.487 0.479  0.134  -0.273 2   VAL EEE CA  
5983  C C   . VAL E 2   ? 3.111 2.764 2.412 0.508  0.178  -0.262 2   VAL EEE C   
5984  O O   . VAL E 2   ? 3.118 2.793 2.420 0.528  0.212  -0.254 2   VAL EEE O   
5985  C CB  . VAL E 2   ? 2.954 2.732 2.409 0.459  0.147  -0.271 2   VAL EEE CB  
5986  C CG1 . VAL E 2   ? 2.999 2.826 2.499 0.450  0.167  -0.265 2   VAL EEE CG1 
5987  C CG2 . VAL E 2   ? 2.830 2.625 2.337 0.433  0.109  -0.278 2   VAL EEE CG2 
5988  N N   . GLN E 3   ? 2.943 2.560 2.211 0.511  0.177  -0.261 3   GLN EEE N   
5989  C CA  . GLN E 3   ? 3.000 2.597 2.227 0.540  0.218  -0.250 3   GLN EEE CA  
5990  C C   . GLN E 3   ? 2.909 2.569 2.199 0.528  0.231  -0.245 3   GLN EEE C   
5991  O O   . GLN E 3   ? 2.842 2.506 2.154 0.504  0.205  -0.251 3   GLN EEE O   
5992  C CB  . GLN E 3   ? 3.167 2.643 2.275 0.562  0.206  -0.253 3   GLN EEE CB  
5993  C CG  . GLN E 3   ? 3.269 2.667 2.297 0.578  0.194  -0.258 3   GLN EEE CG  
5994  C CD  . GLN E 3   ? 3.395 2.674 2.321 0.579  0.149  -0.269 3   GLN EEE CD  
5995  O OE1 . GLN E 3   ? 3.389 2.665 2.338 0.553  0.111  -0.276 3   GLN EEE OE1 
5996  N NE2 . GLN E 3   ? 3.502 2.673 2.311 0.610  0.153  -0.269 3   GLN EEE NE2 
5997  N N   . LEU E 4   ? 2.911 2.616 2.233 0.544  0.270  -0.231 4   LEU EEE N   
5998  C CA  . LEU E 4   ? 2.956 2.710 2.327 0.535  0.281  -0.225 4   LEU EEE CA  
5999  C C   . LEU E 4   ? 3.081 2.807 2.418 0.566  0.315  -0.210 4   LEU EEE C   
6000  O O   . LEU E 4   ? 3.095 2.805 2.413 0.594  0.344  -0.198 4   LEU EEE O   
6001  C CB  . LEU E 4   ? 2.891 2.739 2.354 0.518  0.288  -0.221 4   LEU EEE CB  
6002  C CG  . LEU E 4   ? 2.767 2.651 2.275 0.488  0.261  -0.233 4   LEU EEE CG  
6003  C CD1 . LEU E 4   ? 2.518 2.404 2.026 0.490  0.255  -0.237 4   LEU EEE CD1 
6004  C CD2 . LEU E 4   ? 2.710 2.665 2.290 0.469  0.266  -0.230 4   LEU EEE CD2 
6005  N N   . GLN E 5   ? 3.145 2.864 2.479 0.562  0.315  -0.209 5   GLN EEE N   
6006  C CA  . GLN E 5   ? 3.127 2.828 2.444 0.591  0.347  -0.192 5   GLN EEE CA  
6007  C C   . GLN E 5   ? 3.146 2.892 2.514 0.575  0.344  -0.189 5   GLN EEE C   
6008  O O   . GLN E 5   ? 3.160 2.889 2.513 0.556  0.320  -0.200 5   GLN EEE O   
6009  C CB  . GLN E 5   ? 3.191 2.789 2.403 0.617  0.352  -0.194 5   GLN EEE CB  
6010  C CG  . GLN E 5   ? 3.348 2.906 2.519 0.657  0.394  -0.178 5   GLN EEE CG  
6011  C CD  . GLN E 5   ? 3.361 2.957 2.583 0.681  0.436  -0.153 5   GLN EEE CD  
6012  O OE1 . GLN E 5   ? 3.301 2.956 2.590 0.665  0.430  -0.149 5   GLN EEE OE1 
6013  N NE2 . GLN E 5   ? 3.559 3.119 2.751 0.719  0.479  -0.135 5   GLN EEE NE2 
6014  N N   . GLU E 6   ? 3.189 2.988 2.617 0.584  0.366  -0.172 6   GLU EEE N   
6015  C CA  . GLU E 6   ? 3.232 3.064 2.702 0.575  0.365  -0.166 6   GLU EEE CA  
6016  C C   . GLU E 6   ? 3.292 3.075 2.720 0.599  0.381  -0.156 6   GLU EEE C   
6017  O O   . GLU E 6   ? 3.414 3.144 2.791 0.629  0.404  -0.149 6   GLU EEE O   
6018  C CB  . GLU E 6   ? 3.224 3.125 2.776 0.575  0.374  -0.150 6   GLU EEE CB  
6019  C CG  . GLU E 6   ? 3.267 3.174 2.836 0.602  0.402  -0.133 6   GLU EEE CG  
6020  C CD  . GLU E 6   ? 3.215 3.141 2.792 0.591  0.394  -0.142 6   GLU EEE CD  
6021  O OE1 . GLU E 6   ? 3.276 3.155 2.790 0.592  0.387  -0.157 6   GLU EEE OE1 
6022  O OE2 . GLU E 6   ? 3.092 3.075 2.734 0.582  0.392  -0.135 6   GLU EEE OE2 
6023  N N   . SER E 7   ? 3.257 3.053 2.703 0.587  0.372  -0.156 7   SER EEE N   
6024  C CA  . SER E 7   ? 3.274 3.031 2.691 0.607  0.385  -0.146 7   SER EEE CA  
6025  C C   . SER E 7   ? 3.323 3.114 2.782 0.588  0.371  -0.144 7   SER EEE C   
6026  O O   . SER E 7   ? 3.328 3.159 2.821 0.560  0.350  -0.152 7   SER EEE O   
6027  C CB  . SER E 7   ? 3.332 3.006 2.656 0.613  0.378  -0.159 7   SER EEE CB  
6028  O OG  . SER E 7   ? 3.128 2.799 2.442 0.580  0.345  -0.177 7   SER EEE OG  
6029  N N   . GLY E 8   ? 3.349 3.116 2.798 0.606  0.382  -0.132 8   GLY EEE N   
6030  C CA  . GLY E 8   ? 3.287 3.076 2.767 0.592  0.368  -0.128 8   GLY EEE CA  
6031  C C   . GLY E 8   ? 3.285 3.121 2.842 0.601  0.373  -0.106 8   GLY EEE C   
6032  O O   . GLY E 8   ? 3.206 3.053 2.785 0.590  0.357  -0.103 8   GLY EEE O   
6033  N N   . GLY E 9   ? 3.412 3.274 3.013 0.620  0.394  -0.090 9   GLY EEE N   
6034  C CA  . GLY E 9   ? 3.460 3.367 3.147 0.627  0.394  -0.065 9   GLY EEE CA  
6035  C C   . GLY E 9   ? 3.646 3.533 3.348 0.658  0.418  -0.041 9   GLY EEE C   
6036  O O   . GLY E 9   ? 3.755 3.592 3.399 0.682  0.445  -0.042 9   GLY EEE O   
6037  N N   . GLY E 10  ? 3.564 3.484 3.344 0.659  0.407  -0.019 10  GLY EEE N   
6038  C CA  . GLY E 10  ? 3.704 3.611 3.516 0.689  0.429  0.007  10  GLY EEE CA  
6039  C C   . GLY E 10  ? 3.705 3.652 3.610 0.681  0.402  0.029  10  GLY EEE C   
6040  O O   . GLY E 10  ? 3.794 3.780 3.748 0.659  0.372  0.029  10  GLY EEE O   
6041  N N   . LEU E 11  ? 3.748 3.678 3.674 0.701  0.410  0.048  11  LEU EEE N   
6042  C CA  . LEU E 11  ? 3.660 3.619 3.680 0.699  0.383  0.074  11  LEU EEE CA  
6043  C C   . LEU E 11  ? 3.694 3.619 3.657 0.679  0.348  0.055  11  LEU EEE C   
6044  O O   . LEU E 11  ? 3.708 3.588 3.600 0.689  0.365  0.044  11  LEU EEE O   
6045  C CB  . LEU E 11  ? 3.615 3.581 3.713 0.738  0.421  0.114  11  LEU EEE CB  
6046  C CG  . LEU E 11  ? 3.528 3.524 3.746 0.743  0.398  0.150  11  LEU EEE CG  
6047  C CD1 . LEU E 11  ? 3.525 3.563 3.814 0.714  0.347  0.156  11  LEU EEE CD1 
6048  C CD2 . LEU E 11  ? 3.536 3.550 3.848 0.785  0.449  0.194  11  LEU EEE CD2 
6049  N N   . VAL E 12  ? 3.682 3.621 3.672 0.652  0.300  0.053  12  VAL EEE N   
6050  C CA  . VAL E 12  ? 3.822 3.726 3.754 0.631  0.264  0.035  12  VAL EEE CA  
6051  C C   . VAL E 12  ? 3.982 3.897 3.986 0.622  0.218  0.057  12  VAL EEE C   
6052  O O   . VAL E 12  ? 4.020 3.973 4.113 0.623  0.206  0.079  12  VAL EEE O   
6053  C CB  . VAL E 12  ? 3.834 3.722 3.680 0.601  0.251  0.000  12  VAL EEE CB  
6054  C CG1 . VAL E 12  ? 3.739 3.611 3.518 0.607  0.288  -0.020 12  VAL EEE CG1 
6055  C CG2 . VAL E 12  ? 3.829 3.751 3.714 0.583  0.229  0.000  12  VAL EEE CG2 
6056  N N   . GLN E 13  ? 4.086 3.962 4.052 0.612  0.190  0.051  13  GLN EEE N   
6057  C CA  . GLN E 13  ? 4.055 3.928 4.074 0.601  0.137  0.068  13  GLN EEE CA  
6058  C C   . GLN E 13  ? 4.010 3.870 3.983 0.571  0.100  0.048  13  GLN EEE C   
6059  O O   . GLN E 13  ? 4.002 3.851 3.895 0.556  0.115  0.019  13  GLN EEE O   
6060  C CB  . GLN E 13  ? 4.017 3.845 4.007 0.603  0.116  0.071  13  GLN EEE CB  
6061  C CG  . GLN E 13  ? 4.045 3.819 3.911 0.581  0.105  0.037  13  GLN EEE CG  
6062  C CD  . GLN E 13  ? 4.040 3.811 3.829 0.580  0.149  0.010  13  GLN EEE CD  
6063  O OE1 . GLN E 13  ? 3.983 3.777 3.794 0.600  0.190  0.015  13  GLN EEE OE1 
6064  N NE2 . GLN E 13  ? 4.118 3.850 3.815 0.558  0.141  -0.017 13  GLN EEE NE2 
6065  N N   . ALA E 14  ? 3.932 3.792 3.963 0.562  0.050  0.067  14  ALA EEE N   
6066  C CA  . ALA E 14  ? 3.873 3.705 3.856 0.536  0.007  0.052  14  ALA EEE CA  
6067  C C   . ALA E 14  ? 3.969 3.736 3.827 0.520  -0.002 0.023  14  ALA EEE C   
6068  O O   . ALA E 14  ? 4.209 3.943 4.037 0.525  -0.004 0.023  14  ALA EEE O   
6069  C CB  . ALA E 14  ? 3.834 3.661 3.897 0.531  -0.054 0.080  14  ALA EEE CB  
6070  N N   . GLY E 15  ? 3.851 3.600 3.639 0.501  -0.005 -0.000 15  GLY EEE N   
6071  C CA  . GLY E 15  ? 3.874 3.562 3.545 0.487  -0.005 -0.025 15  GLY EEE CA  
6072  C C   . GLY E 15  ? 3.938 3.634 3.558 0.488  0.046  -0.046 15  GLY EEE C   
6073  O O   . GLY E 15  ? 3.973 3.623 3.505 0.476  0.052  -0.065 15  GLY EEE O   
6074  N N   . GLY E 16  ? 4.031 3.777 3.700 0.503  0.083  -0.041 16  GLY EEE N   
6075  C CA  . GLY E 16  ? 3.983 3.727 3.603 0.505  0.124  -0.059 16  GLY EEE CA  
6076  C C   . GLY E 16  ? 3.843 3.604 3.433 0.491  0.143  -0.079 16  GLY EEE C   
6077  O O   . GLY E 16  ? 3.849 3.618 3.447 0.481  0.127  -0.080 16  GLY EEE O   
6078  N N   . SER E 17  ? 3.715 3.476 3.270 0.491  0.175  -0.094 17  SER EEE N   
6079  C CA  . SER E 17  ? 3.521 3.299 3.056 0.478  0.193  -0.111 17  SER EEE CA  
6080  C C   . SER E 17  ? 3.471 3.277 3.025 0.491  0.222  -0.113 17  SER EEE C   
6081  O O   . SER E 17  ? 3.519 3.315 3.073 0.507  0.234  -0.107 17  SER EEE O   
6082  C CB  . SER E 17  ? 3.499 3.238 2.963 0.459  0.198  -0.128 17  SER EEE CB  
6083  O OG  . SER E 17  ? 3.479 3.188 2.909 0.463  0.207  -0.131 17  SER EEE OG  
6084  N N   . LEU E 18  ? 3.446 3.279 3.008 0.484  0.233  -0.123 18  LEU EEE N   
6085  C CA  . LEU E 18  ? 3.328 3.178 2.897 0.495  0.257  -0.126 18  LEU EEE CA  
6086  C C   . LEU E 18  ? 3.300 3.165 2.857 0.477  0.262  -0.142 18  LEU EEE C   
6087  O O   . LEU E 18  ? 3.348 3.224 2.912 0.464  0.251  -0.146 18  LEU EEE O   
6088  C CB  . LEU E 18  ? 3.245 3.129 2.876 0.517  0.264  -0.107 18  LEU EEE CB  
6089  C CG  . LEU E 18  ? 3.274 3.157 2.902 0.538  0.293  -0.104 18  LEU EEE CG  
6090  C CD1 . LEU E 18  ? 3.304 3.141 2.878 0.546  0.302  -0.110 18  LEU EEE CD1 
6091  C CD2 . LEU E 18  ? 3.238 3.149 2.934 0.563  0.304  -0.079 18  LEU EEE CD2 
6092  N N   . ARG E 19  ? 3.224 3.083 2.762 0.480  0.277  -0.152 19  ARG EEE N   
6093  C CA  . ARG E 19  ? 3.115 2.989 2.650 0.465  0.281  -0.165 19  ARG EEE CA  
6094  C C   . ARG E 19  ? 3.139 3.025 2.686 0.481  0.293  -0.164 19  ARG EEE C   
6095  O O   . ARG E 19  ? 3.323 3.178 2.839 0.494  0.301  -0.165 19  ARG EEE O   
6096  C CB  . ARG E 19  ? 3.044 2.887 2.540 0.448  0.281  -0.178 19  ARG EEE CB  
6097  C CG  . ARG E 19  ? 3.011 2.868 2.515 0.427  0.283  -0.188 19  ARG EEE CG  
6098  C CD  . ARG E 19  ? 2.996 2.822 2.474 0.411  0.283  -0.194 19  ARG EEE CD  
6099  N NE  . ARG E 19  ? 3.053 2.891 2.547 0.391  0.289  -0.199 19  ARG EEE NE  
6100  C CZ  . ARG E 19  ? 3.030 2.860 2.515 0.381  0.296  -0.197 19  ARG EEE CZ  
6101  N NH1 . ARG E 19  ? 3.091 2.898 2.548 0.387  0.292  -0.191 19  ARG EEE NH1 
6102  N NH2 . ARG E 19  ? 2.919 2.759 2.422 0.367  0.307  -0.199 19  ARG EEE NH2 
6103  N N   . LEU E 20  ? 3.043 2.965 2.627 0.482  0.294  -0.161 20  LEU EEE N   
6104  C CA  . LEU E 20  ? 2.993 2.919 2.580 0.497  0.307  -0.160 20  LEU EEE CA  
6105  C C   . LEU E 20  ? 3.059 2.979 2.624 0.481  0.302  -0.178 20  LEU EEE C   
6106  O O   . LEU E 20  ? 3.231 3.167 2.807 0.459  0.294  -0.186 20  LEU EEE O   
6107  C CB  . LEU E 20  ? 2.898 2.866 2.539 0.507  0.311  -0.147 20  LEU EEE CB  
6108  C CG  . LEU E 20  ? 2.914 2.896 2.597 0.517  0.306  -0.127 20  LEU EEE CG  
6109  C CD1 . LEU E 20  ? 2.786 2.809 2.531 0.524  0.306  -0.112 20  LEU EEE CD1 
6110  C CD2 . LEU E 20  ? 3.109 3.063 2.780 0.541  0.321  -0.115 20  LEU EEE CD2 
6111  N N   . SER E 21  ? 3.052 2.945 2.587 0.492  0.308  -0.182 21  SER EEE N   
6112  C CA  . SER E 21  ? 3.127 3.009 2.646 0.475  0.297  -0.196 21  SER EEE CA  
6113  C C   . SER E 21  ? 3.248 3.121 2.755 0.490  0.301  -0.198 21  SER EEE C   
6114  O O   . SER E 21  ? 3.379 3.222 2.856 0.516  0.315  -0.190 21  SER EEE O   
6115  C CB  . SER E 21  ? 3.138 2.972 2.615 0.467  0.286  -0.204 21  SER EEE CB  
6116  O OG  . SER E 21  ? 3.033 2.871 2.517 0.453  0.284  -0.202 21  SER EEE OG  
6117  N N   . CYS E 22  ? 3.521 3.416 3.048 0.475  0.292  -0.206 22  CYS EEE N   
6118  C CA  . CYS E 22  ? 3.532 3.419 3.048 0.486  0.293  -0.209 22  CYS EEE CA  
6119  C C   . CYS E 22  ? 3.489 3.342 2.979 0.470  0.269  -0.222 22  CYS EEE C   
6120  O O   . CYS E 22  ? 3.432 3.312 2.960 0.445  0.256  -0.228 22  CYS EEE O   
6121  C CB  . CYS E 22  ? 3.593 3.537 3.162 0.482  0.298  -0.205 22  CYS EEE CB  
6122  S SG  . CYS E 22  ? 3.744 3.681 3.302 0.492  0.299  -0.209 22  CYS EEE SG  
6123  N N   . ALA E 23  ? 3.287 3.074 2.714 0.485  0.263  -0.225 23  ALA EEE N   
6124  C CA  . ALA E 23  ? 3.150 2.891 2.547 0.471  0.233  -0.236 23  ALA EEE CA  
6125  C C   . ALA E 23  ? 3.071 2.812 2.469 0.472  0.224  -0.241 23  ALA EEE C   
6126  O O   . ALA E 23  ? 3.075 2.804 2.445 0.497  0.242  -0.236 23  ALA EEE O   
6127  C CB  . ALA E 23  ? 3.177 2.831 2.491 0.486  0.224  -0.238 23  ALA EEE CB  
6128  N N   . ALA E 24  ? 3.005 2.757 2.436 0.447  0.196  -0.249 24  ALA EEE N   
6129  C CA  . ALA E 24  ? 2.893 2.648 2.332 0.444  0.182  -0.254 24  ALA EEE CA  
6130  C C   . ALA E 24  ? 2.937 2.624 2.340 0.433  0.139  -0.262 24  ALA EEE C   
6131  O O   . ALA E 24  ? 3.063 2.735 2.479 0.415  0.118  -0.262 24  ALA EEE O   
6132  C CB  . ALA E 24  ? 2.814 2.650 2.340 0.424  0.186  -0.254 24  ALA EEE CB  
6133  N N   . SER E 25  ? 2.887 2.528 2.244 0.445  0.124  -0.267 25  SER EEE N   
6134  C CA  . SER E 25  ? 2.849 2.423 2.177 0.431  0.074  -0.274 25  SER EEE CA  
6135  C C   . SER E 25  ? 2.783 2.416 2.209 0.400  0.050  -0.274 25  SER EEE C   
6136  O O   . SER E 25  ? 2.781 2.493 2.274 0.395  0.073  -0.272 25  SER EEE O   
6137  C CB  . SER E 25  ? 2.891 2.381 2.125 0.455  0.061  -0.279 25  SER EEE CB  
6138  O OG  . SER E 25  ? 2.844 2.382 2.108 0.461  0.079  -0.278 25  SER EEE OG  
6139  N N   . GLY E 26  ? 2.839 2.428 2.273 0.379  0.003  -0.276 26  GLY EEE N   
6140  C CA  . GLY E 26  ? 2.968 2.613 2.507 0.349  -0.017 -0.272 26  GLY EEE CA  
6141  C C   . GLY E 26  ? 3.048 2.771 2.671 0.334  0.015  -0.264 26  GLY EEE C   
6142  O O   . GLY E 26  ? 3.019 2.742 2.616 0.341  0.039  -0.262 26  GLY EEE O   
6143  N N   . SER E 27  ? 2.914 2.700 2.635 0.313  0.014  -0.258 27  SER EEE N   
6144  C CA  . SER E 27  ? 2.851 2.706 2.653 0.299  0.046  -0.249 27  SER EEE CA  
6145  C C   . SER E 27  ? 2.773 2.693 2.588 0.311  0.093  -0.250 27  SER EEE C   
6146  O O   . SER E 27  ? 2.836 2.775 2.654 0.318  0.094  -0.255 27  SER EEE O   
6147  C CB  . SER E 27  ? 2.823 2.704 2.728 0.272  0.025  -0.239 27  SER EEE CB  
6148  O OG  . SER E 27  ? 2.914 2.735 2.818 0.258  -0.025 -0.235 27  SER EEE OG  
6149  N N   . ILE E 28  ? 2.713 2.662 2.534 0.312  0.128  -0.245 28  ILE EEE N   
6150  C CA  . ILE E 28  ? 2.604 2.601 2.427 0.324  0.165  -0.246 28  ILE EEE CA  
6151  C C   . ILE E 28  ? 2.617 2.668 2.517 0.311  0.177  -0.242 28  ILE EEE C   
6152  O O   . ILE E 28  ? 2.627 2.711 2.529 0.320  0.195  -0.244 28  ILE EEE O   
6153  C CB  . ILE E 28  ? 2.508 2.510 2.308 0.329  0.193  -0.242 28  ILE EEE CB  
6154  C CG1 . ILE E 28  ? 2.536 2.502 2.261 0.351  0.194  -0.245 28  ILE EEE CG1 
6155  C CG2 . ILE E 28  ? 2.504 2.556 2.333 0.330  0.226  -0.238 28  ILE EEE CG2 
6156  C CD1 . ILE E 28  ? 2.588 2.552 2.293 0.355  0.215  -0.241 28  ILE EEE CD1 
6157  N N   . SER E 29  ? 2.617 2.674 2.583 0.292  0.166  -0.234 29  SER EEE N   
6158  C CA  . SER E 29  ? 2.476 2.581 2.518 0.283  0.183  -0.227 29  SER EEE CA  
6159  C C   . SER E 29  ? 2.433 2.549 2.488 0.286  0.164  -0.233 29  SER EEE C   
6160  O O   . SER E 29  ? 2.305 2.462 2.416 0.282  0.179  -0.229 29  SER EEE O   
6161  C CB  . SER E 29  ? 2.450 2.558 2.572 0.262  0.178  -0.213 29  SER EEE CB  
6162  O OG  . SER E 29  ? 2.470 2.623 2.670 0.256  0.199  -0.203 29  SER EEE OG  
6163  N N   . ARG E 30  ? 2.706 2.781 2.706 0.294  0.132  -0.243 30  ARG EEE N   
6164  C CA  . ARG E 30  ? 2.715 2.794 2.719 0.298  0.112  -0.249 30  ARG EEE CA  
6165  C C   . ARG E 30  ? 2.662 2.768 2.632 0.316  0.141  -0.255 30  ARG EEE C   
6166  O O   . ARG E 30  ? 2.588 2.717 2.579 0.318  0.137  -0.258 30  ARG EEE O   
6167  C CB  . ARG E 30  ? 2.810 2.819 2.747 0.304  0.070  -0.256 30  ARG EEE CB  
6168  C CG  . ARG E 30  ? 2.870 2.832 2.823 0.287  0.029  -0.252 30  ARG EEE CG  
6169  C CD  . ARG E 30  ? 2.949 2.827 2.816 0.297  -0.014 -0.261 30  ARG EEE CD  
6170  N NE  . ARG E 30  ? 2.990 2.844 2.760 0.324  0.011  -0.269 30  ARG EEE NE  
6171  C CZ  . ARG E 30  ? 3.116 2.893 2.790 0.341  -0.009 -0.276 30  ARG EEE CZ  
6172  N NH1 . ARG E 30  ? 3.207 2.913 2.852 0.335  -0.061 -0.279 30  ARG EEE NH1 
6173  N NH2 . ARG E 30  ? 3.075 2.840 2.677 0.367  0.025  -0.278 30  ARG EEE NH2 
6174  N N   . PHE E 31  ? 2.561 2.667 2.484 0.328  0.166  -0.255 31  PHE EEE N   
6175  C CA  . PHE E 31  ? 2.437 2.568 2.335 0.344  0.189  -0.258 31  PHE EEE CA  
6176  C C   . PHE E 31  ? 2.240 2.420 2.188 0.338  0.213  -0.254 31  PHE EEE C   
6177  O O   . PHE E 31  ? 2.175 2.366 2.155 0.328  0.228  -0.248 31  PHE EEE O   
6178  C CB  . PHE E 31  ? 2.572 2.685 2.417 0.357  0.204  -0.256 31  PHE EEE CB  
6179  C CG  . PHE E 31  ? 2.584 2.639 2.369 0.368  0.186  -0.259 31  PHE EEE CG  
6180  C CD1 . PHE E 31  ? 2.593 2.619 2.345 0.378  0.169  -0.263 31  PHE EEE CD1 
6181  C CD2 . PHE E 31  ? 2.637 2.660 2.394 0.367  0.185  -0.256 31  PHE EEE CD2 
6182  C CE1 . PHE E 31  ? 2.724 2.684 2.408 0.390  0.154  -0.266 31  PHE EEE CE1 
6183  C CE2 . PHE E 31  ? 2.761 2.722 2.455 0.378  0.168  -0.259 31  PHE EEE CE2 
6184  C CZ  . PHE E 31  ? 2.827 2.753 2.481 0.391  0.153  -0.264 31  PHE EEE CZ  
6185  N N   . ASN E 32  ? 2.136 2.342 2.086 0.346  0.220  -0.257 32  ASN EEE N   
6186  C CA  . ASN E 32  ? 1.923 2.164 1.907 0.343  0.242  -0.254 32  ASN EEE CA  
6187  C C   . ASN E 32  ? 1.855 2.100 1.807 0.351  0.263  -0.251 32  ASN EEE C   
6188  O O   . ASN E 32  ? 1.828 2.086 1.792 0.349  0.282  -0.248 32  ASN EEE O   
6189  C CB  . ASN E 32  ? 1.767 2.033 1.773 0.345  0.237  -0.258 32  ASN EEE CB  
6190  C CG  . ASN E 32  ? 1.747 2.009 1.792 0.336  0.212  -0.260 32  ASN EEE CG  
6191  O OD1 . ASN E 32  ? 1.753 2.016 1.845 0.323  0.208  -0.254 32  ASN EEE OD1 
6192  N ND2 . ASN E 32  ? 1.765 2.021 1.794 0.342  0.193  -0.266 32  ASN EEE ND2 
6193  N N   . ALA E 33  ? 1.961 2.189 1.869 0.362  0.260  -0.251 33  ALA EEE N   
6194  C CA  . ALA E 33  ? 1.943 2.171 1.827 0.369  0.273  -0.246 33  ALA EEE CA  
6195  C C   . ALA E 33  ? 2.082 2.286 1.930 0.380  0.268  -0.243 33  ALA EEE C   
6196  O O   . ALA E 33  ? 2.238 2.431 2.072 0.389  0.259  -0.245 33  ALA EEE O   
6197  C CB  . ALA E 33  ? 1.819 2.068 1.706 0.376  0.276  -0.245 33  ALA EEE CB  
6198  N N   . MET E 34  ? 2.171 2.362 1.998 0.382  0.276  -0.238 34  MET EEE N   
6199  C CA  . MET E 34  ? 2.263 2.434 2.061 0.395  0.275  -0.233 34  MET EEE CA  
6200  C C   . MET E 34  ? 2.248 2.422 2.040 0.400  0.280  -0.225 34  MET EEE C   
6201  O O   . MET E 34  ? 2.279 2.456 2.073 0.392  0.284  -0.225 34  MET EEE O   
6202  C CB  . MET E 34  ? 2.440 2.578 2.217 0.390  0.271  -0.235 34  MET EEE CB  
6203  C CG  . MET E 34  ? 2.643 2.760 2.412 0.390  0.257  -0.241 34  MET EEE CG  
6204  S SD  . MET E 34  ? 2.823 2.917 2.602 0.371  0.246  -0.244 34  MET EEE SD  
6205  C CE  . MET E 34  ? 2.704 2.838 2.541 0.355  0.259  -0.243 34  MET EEE CE  
6206  N N   . GLY E 35  ? 2.366 2.532 2.146 0.414  0.281  -0.216 35  GLY EEE N   
6207  C CA  . GLY E 35  ? 2.447 2.614 2.228 0.419  0.279  -0.206 35  GLY EEE CA  
6208  C C   . GLY E 35  ? 2.538 2.698 2.319 0.436  0.282  -0.194 35  GLY EEE C   
6209  O O   . GLY E 35  ? 2.635 2.782 2.403 0.447  0.290  -0.194 35  GLY EEE O   
6210  N N   . TRP E 36  ? 2.352 2.517 2.149 0.440  0.276  -0.181 36  TRP EEE N   
6211  C CA  . TRP E 36  ? 2.312 2.474 2.123 0.457  0.279  -0.165 36  TRP EEE CA  
6212  C C   . TRP E 36  ? 2.258 2.445 2.117 0.462  0.269  -0.148 36  TRP EEE C   
6213  O O   . TRP E 36  ? 2.287 2.476 2.152 0.451  0.250  -0.148 36  TRP EEE O   
6214  C CB  . TRP E 36  ? 2.330 2.463 2.116 0.456  0.275  -0.163 36  TRP EEE CB  
6215  C CG  . TRP E 36  ? 2.519 2.624 2.265 0.455  0.285  -0.173 36  TRP EEE CG  
6216  C CD1 . TRP E 36  ? 2.570 2.657 2.287 0.440  0.284  -0.187 36  TRP EEE CD1 
6217  C CD2 . TRP E 36  ? 2.655 2.739 2.385 0.473  0.298  -0.168 36  TRP EEE CD2 
6218  N NE1 . TRP E 36  ? 2.642 2.701 2.330 0.444  0.289  -0.191 36  TRP EEE NE1 
6219  C CE2 . TRP E 36  ? 2.756 2.808 2.443 0.465  0.298  -0.180 36  TRP EEE CE2 
6220  C CE3 . TRP E 36  ? 2.739 2.824 2.485 0.497  0.312  -0.151 36  TRP EEE CE3 
6221  C CZ2 . TRP E 36  ? 2.918 2.934 2.570 0.479  0.306  -0.180 36  TRP EEE CZ2 
6222  C CZ3 . TRP E 36  ? 2.863 2.912 2.572 0.513  0.327  -0.150 36  TRP EEE CZ3 
6223  C CH2 . TRP E 36  ? 2.945 2.957 2.603 0.504  0.322  -0.165 36  TRP EEE CH2 
6224  N N   . TRP E 37  ? 2.251 2.451 2.143 0.480  0.281  -0.131 37  TRP EEE N   
6225  C CA  . TRP E 37  ? 2.254 2.479 2.208 0.488  0.274  -0.108 37  TRP EEE CA  
6226  C C   . TRP E 37  ? 2.445 2.664 2.424 0.508  0.288  -0.086 37  TRP EEE C   
6227  O O   . TRP E 37  ? 2.573 2.767 2.513 0.519  0.307  -0.091 37  TRP EEE O   
6228  C CB  . TRP E 37  ? 2.207 2.459 2.192 0.495  0.284  -0.103 37  TRP EEE CB  
6229  C CG  . TRP E 37  ? 2.056 2.322 2.039 0.478  0.268  -0.115 37  TRP EEE CG  
6230  C CD1 . TRP E 37  ? 2.030 2.287 1.970 0.464  0.266  -0.139 37  TRP EEE CD1 
6231  C CD2 . TRP E 37  ? 2.115 2.407 2.148 0.474  0.252  -0.103 37  TRP EEE CD2 
6232  N NE1 . TRP E 37  ? 2.126 2.401 2.081 0.454  0.252  -0.143 37  TRP EEE NE1 
6233  C CE2 . TRP E 37  ? 2.159 2.453 2.166 0.459  0.242  -0.122 37  TRP EEE CE2 
6234  C CE3 . TRP E 37  ? 2.188 2.501 2.290 0.482  0.244  -0.075 37  TRP EEE CE3 
6235  C CZ2 . TRP E 37  ? 2.176 2.488 2.214 0.452  0.223  -0.117 37  TRP EEE CZ2 
6236  C CZ3 . TRP E 37  ? 2.173 2.506 2.312 0.474  0.223  -0.069 37  TRP EEE CZ3 
6237  C CH2 . TRP E 37  ? 2.159 2.489 2.260 0.459  0.213  -0.091 37  TRP EEE CH2 
6238  N N   . ARG E 38  ? 2.445 2.684 2.491 0.513  0.276  -0.061 38  ARG EEE N   
6239  C CA  . ARG E 38  ? 2.607 2.845 2.692 0.535  0.293  -0.036 38  ARG EEE CA  
6240  C C   . ARG E 38  ? 2.739 3.012 2.917 0.547  0.296  -0.004 38  ARG EEE C   
6241  O O   . ARG E 38  ? 2.764 3.058 2.980 0.532  0.268  0.000  38  ARG EEE O   
6242  C CB  . ARG E 38  ? 2.583 2.801 2.666 0.530  0.270  -0.031 38  ARG EEE CB  
6243  C CG  . ARG E 38  ? 2.524 2.752 2.654 0.514  0.226  -0.020 38  ARG EEE CG  
6244  C CD  . ARG E 38  ? 2.523 2.722 2.643 0.509  0.199  -0.016 38  ARG EEE CD  
6245  N NE  . ARG E 38  ? 2.485 2.681 2.643 0.495  0.151  -0.004 38  ARG EEE NE  
6246  C CZ  . ARG E 38  ? 2.553 2.714 2.690 0.486  0.115  -0.003 38  ARG EEE CZ  
6247  N NH1 . ARG E 38  ? 2.666 2.795 2.748 0.487  0.123  -0.015 38  ARG EEE NH1 
6248  N NH2 . ARG E 38  ? 2.500 2.649 2.666 0.474  0.066  0.009  38  ARG EEE NH2 
6249  N N   . GLN E 39  ? 2.896 3.172 3.112 0.573  0.331  0.021  39  GLN EEE N   
6250  C CA  . GLN E 39  ? 2.860 3.172 3.181 0.587  0.339  0.058  39  GLN EEE CA  
6251  C C   . GLN E 39  ? 2.917 3.225 3.287 0.612  0.362  0.089  39  GLN EEE C   
6252  O O   . GLN E 39  ? 2.867 3.146 3.188 0.634  0.403  0.086  39  GLN EEE O   
6253  C CB  . GLN E 39  ? 2.810 3.134 3.135 0.599  0.373  0.062  39  GLN EEE CB  
6254  C CG  . GLN E 39  ? 2.802 3.166 3.242 0.610  0.380  0.103  39  GLN EEE CG  
6255  C CD  . GLN E 39  ? 2.662 3.033 3.097 0.622  0.414  0.105  39  GLN EEE CD  
6256  O OE1 . GLN E 39  ? 2.587 2.925 2.936 0.633  0.445  0.085  39  GLN EEE OE1 
6257  N NE2 . GLN E 39  ? 2.649 3.059 3.175 0.617  0.405  0.130  39  GLN EEE NE2 
6258  N N   . ALA E 40  ? 3.162 3.494 3.628 0.608  0.336  0.118  40  ALA EEE N   
6259  C CA  . ALA E 40  ? 3.303 3.640 3.843 0.632  0.354  0.154  40  ALA EEE CA  
6260  C C   . ALA E 40  ? 3.409 3.783 4.062 0.653  0.387  0.197  40  ALA EEE C   
6261  O O   . ALA E 40  ? 3.586 3.988 4.281 0.642  0.374  0.202  40  ALA EEE O   
6262  C CB  . ALA E 40  ? 3.318 3.655 3.905 0.614  0.298  0.163  40  ALA EEE CB  
6263  N N   . PRO E 41  ? 3.127 3.499 3.831 0.686  0.434  0.229  41  PRO EEE N   
6264  C CA  . PRO E 41  ? 3.080 3.487 3.899 0.710  0.473  0.275  41  PRO EEE CA  
6265  C C   . PRO E 41  ? 3.071 3.524 4.019 0.686  0.416  0.302  41  PRO EEE C   
6266  O O   . PRO E 41  ? 3.133 3.590 4.136 0.676  0.372  0.315  41  PRO EEE O   
6267  C CB  . PRO E 41  ? 3.027 3.419 3.877 0.748  0.526  0.305  41  PRO EEE CB  
6268  C CG  . PRO E 41  ? 3.035 3.371 3.740 0.749  0.533  0.264  41  PRO EEE CG  
6269  C CD  . PRO E 41  ? 3.015 3.350 3.665 0.707  0.462  0.225  41  PRO EEE CD  
6270  N N   . GLY E 42  ? 3.044 3.526 4.039 0.679  0.413  0.312  42  GLY EEE N   
6271  C CA  . GLY E 42  ? 2.962 3.481 4.074 0.656  0.356  0.337  42  GLY EEE CA  
6272  C C   . GLY E 42  ? 2.909 3.413 3.951 0.617  0.284  0.299  42  GLY EEE C   
6273  O O   . GLY E 42  ? 2.711 3.236 3.828 0.596  0.233  0.314  42  GLY EEE O   
6274  N N   . LYS E 43  ? 3.026 3.491 3.928 0.607  0.278  0.251  43  LYS EEE N   
6275  C CA  . LYS E 43  ? 3.109 3.553 3.937 0.573  0.219  0.215  43  LYS EEE CA  
6276  C C   . LYS E 43  ? 3.229 3.670 3.973 0.570  0.244  0.184  43  LYS EEE C   
6277  O O   . LYS E 43  ? 3.308 3.744 4.005 0.591  0.301  0.176  43  LYS EEE O   
6278  C CB  . LYS E 43  ? 3.041 3.442 3.774 0.565  0.198  0.186  43  LYS EEE CB  
6279  C CG  . LYS E 43  ? 2.860 3.237 3.595 0.539  0.124  0.183  43  LYS EEE CG  
6280  C CD  . LYS E 43  ? 2.773 3.169 3.646 0.541  0.090  0.230  43  LYS EEE CD  
6281  C CE  . LYS E 43  ? 2.746 3.103 3.601 0.514  0.008  0.224  43  LYS EEE CE  
6282  N NZ  . LYS E 43  ? 2.880 3.246 3.866 0.516  -0.034 0.269  43  LYS EEE NZ  
6283  N N   . GLU E 44  ? 3.243 3.684 3.965 0.544  0.200  0.166  44  GLU EEE N   
6284  C CA  . GLU E 44  ? 3.153 3.593 3.802 0.540  0.220  0.137  44  GLU EEE CA  
6285  C C   . GLU E 44  ? 3.204 3.607 3.724 0.535  0.230  0.093  44  GLU EEE C   
6286  O O   . GLU E 44  ? 3.391 3.767 3.871 0.526  0.205  0.081  44  GLU EEE O   
6287  C CB  . GLU E 44  ? 3.086 3.535 3.759 0.517  0.172  0.136  44  GLU EEE CB  
6288  C CG  . GLU E 44  ? 3.063 3.532 3.728 0.519  0.198  0.129  44  GLU EEE CG  
6289  C CD  . GLU E 44  ? 3.103 3.550 3.647 0.515  0.217  0.085  44  GLU EEE CD  
6290  O OE1 . GLU E 44  ? 3.227 3.645 3.696 0.499  0.190  0.056  44  GLU EEE OE1 
6291  O OE2 . GLU E 44  ? 3.071 3.525 3.595 0.529  0.261  0.081  44  GLU EEE OE2 
6292  N N   . ARG E 45  ? 3.184 3.583 3.640 0.541  0.266  0.072  45  ARG EEE N   
6293  C CA  . ARG E 45  ? 3.124 3.490 3.468 0.533  0.270  0.032  45  ARG EEE CA  
6294  C C   . ARG E 45  ? 3.101 3.451 3.407 0.506  0.221  0.011  45  ARG EEE C   
6295  O O   . ARG E 45  ? 3.171 3.531 3.488 0.492  0.196  0.008  45  ARG EEE O   
6296  C CB  . ARG E 45  ? 3.073 3.438 3.366 0.538  0.300  0.013  45  ARG EEE CB  
6297  C CG  . ARG E 45  ? 2.944 3.279 3.165 0.555  0.339  -0.001 45  ARG EEE CG  
6298  C CD  . ARG E 45  ? 2.790 3.121 2.972 0.559  0.360  -0.015 45  ARG EEE CD  
6299  N NE  . ARG E 45  ? 2.617 2.907 2.723 0.576  0.391  -0.029 45  ARG EEE NE  
6300  C CZ  . ARG E 45  ? 2.450 2.722 2.510 0.583  0.409  -0.040 45  ARG EEE CZ  
6301  N NH1 . ARG E 45  ? 2.297 2.593 2.383 0.576  0.403  -0.039 45  ARG EEE NH1 
6302  N NH2 . ARG E 45  ? 2.437 2.660 2.420 0.597  0.430  -0.052 45  ARG EEE NH2 
6303  N N   . GLU E 46  ? 2.820 3.140 3.074 0.500  0.210  -0.003 46  GLU EEE N   
6304  C CA  . GLU E 46  ? 2.573 2.866 2.781 0.478  0.169  -0.021 46  GLU EEE CA  
6305  C C   . GLU E 46  ? 2.349 2.616 2.462 0.470  0.184  -0.056 46  GLU EEE C   
6306  O O   . GLU E 46  ? 2.277 2.535 2.360 0.480  0.212  -0.063 46  GLU EEE O   
6307  C CB  . GLU E 46  ? 2.624 2.897 2.859 0.474  0.132  -0.004 46  GLU EEE CB  
6308  C CG  . GLU E 46  ? 2.597 2.823 2.761 0.455  0.094  -0.024 46  GLU EEE CG  
6309  C CD  . GLU E 46  ? 2.546 2.742 2.730 0.452  0.054  -0.007 46  GLU EEE CD  
6310  O OE1 . GLU E 46  ? 2.415 2.637 2.692 0.462  0.045  0.025  46  GLU EEE OE1 
6311  O OE2 . GLU E 46  ? 2.489 2.635 2.598 0.442  0.032  -0.023 46  GLU EEE OE2 
6312  N N   . PHE E 47  ? 2.200 2.453 2.270 0.454  0.165  -0.075 47  PHE EEE N   
6313  C CA  . PHE E 47  ? 2.163 2.395 2.158 0.446  0.180  -0.103 47  PHE EEE CA  
6314  C C   . PHE E 47  ? 2.127 2.318 2.075 0.440  0.169  -0.109 47  PHE EEE C   
6315  O O   . PHE E 47  ? 2.160 2.326 2.106 0.435  0.137  -0.101 47  PHE EEE O   
6316  C CB  . PHE E 47  ? 2.221 2.450 2.191 0.433  0.170  -0.118 47  PHE EEE CB  
6317  C CG  . PHE E 47  ? 2.161 2.363 2.063 0.423  0.179  -0.142 47  PHE EEE CG  
6318  C CD1 . PHE E 47  ? 2.107 2.320 1.991 0.424  0.208  -0.158 47  PHE EEE CD1 
6319  C CD2 . PHE E 47  ? 2.129 2.287 1.983 0.414  0.159  -0.148 47  PHE EEE CD2 
6320  C CE1 . PHE E 47  ? 1.994 2.185 1.830 0.414  0.217  -0.175 47  PHE EEE CE1 
6321  C CE2 . PHE E 47  ? 2.125 2.257 1.922 0.408  0.175  -0.166 47  PHE EEE CE2 
6322  C CZ  . PHE E 47  ? 2.063 2.216 1.858 0.407  0.205  -0.178 47  PHE EEE CZ  
6323  N N   . VAL E 48  ? 2.168 2.348 2.075 0.442  0.194  -0.123 48  VAL EEE N   
6324  C CA  . VAL E 48  ? 2.190 2.332 2.052 0.438  0.188  -0.128 48  VAL EEE CA  
6325  C C   . VAL E 48  ? 2.215 2.330 2.014 0.425  0.197  -0.150 48  VAL EEE C   
6326  O O   . VAL E 48  ? 2.162 2.240 1.921 0.417  0.182  -0.154 48  VAL EEE O   
6327  C CB  . VAL E 48  ? 2.089 2.232 1.958 0.451  0.208  -0.122 48  VAL EEE CB  
6328  C CG1 . VAL E 48  ? 2.278 2.380 2.100 0.447  0.202  -0.127 48  VAL EEE CG1 
6329  C CG2 . VAL E 48  ? 2.254 2.421 2.191 0.467  0.206  -0.096 48  VAL EEE CG2 
6330  N N   . ALA E 49  ? 2.145 2.276 1.936 0.424  0.222  -0.163 49  ALA EEE N   
6331  C CA  . ALA E 49  ? 1.996 2.108 1.745 0.413  0.234  -0.180 49  ALA EEE CA  
6332  C C   . ALA E 49  ? 1.915 2.054 1.679 0.410  0.250  -0.190 49  ALA EEE C   
6333  O O   . ALA E 49  ? 2.004 2.168 1.795 0.417  0.255  -0.188 49  ALA EEE O   
6334  C CB  . ALA E 49  ? 2.050 2.135 1.768 0.412  0.245  -0.183 49  ALA EEE CB  
6335  N N   . ARG E 50  ? 1.924 2.053 1.667 0.399  0.258  -0.201 50  ARG EEE N   
6336  C CA  . ARG E 50  ? 1.884 2.037 1.645 0.395  0.270  -0.210 50  ARG EEE CA  
6337  C C   . ARG E 50  ? 1.966 2.100 1.708 0.385  0.287  -0.217 50  ARG EEE C   
6338  O O   . ARG E 50  ? 2.138 2.240 1.847 0.382  0.292  -0.216 50  ARG EEE O   
6339  C CB  . ARG E 50  ? 1.824 1.996 1.603 0.395  0.264  -0.211 50  ARG EEE CB  
6340  C CG  . ARG E 50  ? 1.929 2.076 1.679 0.390  0.262  -0.213 50  ARG EEE CG  
6341  C CD  . ARG E 50  ? 1.792 1.964 1.565 0.391  0.256  -0.215 50  ARG EEE CD  
6342  N NE  . ARG E 50  ? 1.706 1.848 1.446 0.389  0.253  -0.217 50  ARG EEE NE  
6343  C CZ  . ARG E 50  ? 1.822 1.944 1.546 0.391  0.228  -0.211 50  ARG EEE CZ  
6344  N NH1 . ARG E 50  ? 1.837 1.972 1.589 0.395  0.205  -0.199 50  ARG EEE NH1 
6345  N NH2 . ARG E 50  ? 2.013 2.097 1.694 0.391  0.226  -0.214 50  ARG EEE NH2 
6346  N N   . ILE E 51  ? 1.878 2.027 1.642 0.380  0.296  -0.223 51  ILE EEE N   
6347  C CA  . ILE E 51  ? 1.857 2.000 1.627 0.369  0.313  -0.227 51  ILE EEE CA  
6348  C C   . ILE E 51  ? 1.853 2.025 1.664 0.365  0.313  -0.232 51  ILE EEE C   
6349  O O   . ILE E 51  ? 1.992 2.176 1.819 0.367  0.301  -0.234 51  ILE EEE O   
6350  C CB  . ILE E 51  ? 1.897 2.019 1.660 0.364  0.317  -0.225 51  ILE EEE CB  
6351  C CG1 . ILE E 51  ? 1.907 2.031 1.698 0.352  0.334  -0.225 51  ILE EEE CG1 
6352  C CG2 . ILE E 51  ? 2.150 2.276 1.915 0.370  0.303  -0.226 51  ILE EEE CG2 
6353  C CD1 . ILE E 51  ? 2.059 2.162 1.833 0.350  0.358  -0.221 51  ILE EEE CD1 
6354  N N   . VAL E 52  ? 1.772 1.950 1.594 0.362  0.326  -0.232 52  VAL EEE N   
6355  C CA  . VAL E 52  ? 1.703 1.908 1.568 0.358  0.327  -0.236 52  VAL EEE CA  
6356  C C   . VAL E 52  ? 1.737 1.939 1.634 0.348  0.347  -0.232 52  VAL EEE C   
6357  O O   . VAL E 52  ? 1.772 1.949 1.650 0.347  0.369  -0.226 52  VAL EEE O   
6358  C CB  . VAL E 52  ? 1.587 1.802 1.450 0.363  0.329  -0.237 52  VAL EEE CB  
6359  C CG1 . VAL E 52  ? 1.524 1.768 1.433 0.359  0.328  -0.241 52  VAL EEE CG1 
6360  C CG2 . VAL E 52  ? 1.574 1.791 1.415 0.372  0.309  -0.237 52  VAL EEE CG2 
6361  N N   . LYS E 53  ? 1.771 1.993 1.717 0.340  0.337  -0.233 53  LYS EEE N   
6362  C CA  . LYS E 53  ? 1.753 1.976 1.748 0.329  0.349  -0.226 53  LYS EEE CA  
6363  C C   . LYS E 53  ? 1.866 2.089 1.878 0.330  0.385  -0.218 53  LYS EEE C   
6364  O O   . LYS E 53  ? 1.920 2.158 1.942 0.336  0.391  -0.220 53  LYS EEE O   
6365  C CB  . LYS E 53  ? 1.703 1.946 1.752 0.321  0.325  -0.228 53  LYS EEE CB  
6366  C CG  . LYS E 53  ? 1.784 2.009 1.832 0.314  0.298  -0.229 53  LYS EEE CG  
6367  C CD  . LYS E 53  ? 1.830 2.065 1.946 0.301  0.278  -0.225 53  LYS EEE CD  
6368  C CE  . LYS E 53  ? 1.872 2.122 1.995 0.306  0.256  -0.233 53  LYS EEE CE  
6369  N NZ  . LYS E 53  ? 1.870 2.121 2.054 0.293  0.227  -0.230 53  LYS EEE NZ  
6370  N N   . GLY E 54  ? 2.051 2.251 2.061 0.327  0.410  -0.208 54  GLY EEE N   
6371  C CA  . GLY E 54  ? 2.134 2.321 2.149 0.332  0.452  -0.197 54  GLY EEE CA  
6372  C C   . GLY E 54  ? 2.167 2.313 2.097 0.345  0.469  -0.200 54  GLY EEE C   
6373  O O   . GLY E 54  ? 2.263 2.381 2.177 0.352  0.508  -0.191 54  GLY EEE O   
6374  N N   . PHE E 55  ? 2.005 2.142 1.880 0.350  0.441  -0.210 55  PHE EEE N   
6375  C CA  . PHE E 55  ? 1.990 2.085 1.786 0.361  0.445  -0.212 55  PHE EEE CA  
6376  C C   . PHE E 55  ? 2.101 2.161 1.846 0.361  0.438  -0.211 55  PHE EEE C   
6377  O O   . PHE E 55  ? 2.084 2.159 1.852 0.354  0.424  -0.212 55  PHE EEE O   
6378  C CB  . PHE E 55  ? 1.863 1.975 1.647 0.366  0.416  -0.221 55  PHE EEE CB  
6379  C CG  . PHE E 55  ? 1.823 1.958 1.643 0.369  0.425  -0.223 55  PHE EEE CG  
6380  C CD1 . PHE E 55  ? 1.980 2.082 1.763 0.379  0.449  -0.220 55  PHE EEE CD1 
6381  C CD2 . PHE E 55  ? 1.850 2.035 1.736 0.362  0.410  -0.226 55  PHE EEE CD2 
6382  C CE1 . PHE E 55  ? 2.046 2.170 1.863 0.382  0.459  -0.221 55  PHE EEE CE1 
6383  C CE2 . PHE E 55  ? 1.871 2.079 1.793 0.364  0.416  -0.227 55  PHE EEE CE2 
6384  C CZ  . PHE E 55  ? 1.954 2.134 1.845 0.374  0.442  -0.224 55  PHE EEE CZ  
6385  N N   . ASP E 56  ? 2.168 2.174 1.837 0.370  0.444  -0.210 56  ASP EEE N   
6386  C CA  . ASP E 56  ? 2.194 2.163 1.812 0.371  0.432  -0.209 56  ASP EEE CA  
6387  C C   . ASP E 56  ? 2.133 2.126 1.755 0.371  0.390  -0.215 56  ASP EEE C   
6388  O O   . ASP E 56  ? 2.168 2.190 1.810 0.373  0.371  -0.219 56  ASP EEE O   
6389  C CB  . ASP E 56  ? 2.378 2.272 1.906 0.381  0.445  -0.206 56  ASP EEE CB  
6390  C CG  . ASP E 56  ? 2.531 2.388 2.044 0.383  0.494  -0.196 56  ASP EEE CG  
6391  O OD1 . ASP E 56  ? 2.415 2.312 2.002 0.376  0.517  -0.191 56  ASP EEE OD1 
6392  O OD2 . ASP E 56  ? 2.800 2.582 2.227 0.393  0.508  -0.193 56  ASP EEE OD2 
6393  N N   . PRO E 57  ? 2.173 2.153 1.778 0.369  0.376  -0.214 57  PRO EEE N   
6394  C CA  . PRO E 57  ? 2.162 2.160 1.773 0.373  0.342  -0.215 57  PRO EEE CA  
6395  C C   . PRO E 57  ? 2.202 2.169 1.769 0.380  0.320  -0.213 57  PRO EEE C   
6396  O O   . PRO E 57  ? 2.367 2.275 1.871 0.383  0.325  -0.211 57  PRO EEE O   
6397  C CB  . PRO E 57  ? 2.196 2.178 1.793 0.371  0.339  -0.212 57  PRO EEE CB  
6398  C CG  . PRO E 57  ? 2.189 2.170 1.804 0.363  0.367  -0.211 57  PRO EEE CG  
6399  C CD  . PRO E 57  ? 2.165 2.128 1.768 0.364  0.394  -0.209 57  PRO EEE CD  
6400  N N   . VAL E 58  ? 2.021 2.021 1.619 0.383  0.295  -0.213 58  VAL EEE N   
6401  C CA  . VAL E 58  ? 2.114 2.091 1.688 0.388  0.265  -0.208 58  VAL EEE CA  
6402  C C   . VAL E 58  ? 2.144 2.138 1.745 0.391  0.239  -0.200 58  VAL EEE C   
6403  O O   . VAL E 58  ? 2.236 2.277 1.887 0.392  0.243  -0.199 58  VAL EEE O   
6404  C CB  . VAL E 58  ? 2.107 2.109 1.705 0.389  0.258  -0.211 58  VAL EEE CB  
6405  C CG1 . VAL E 58  ? 2.183 2.161 1.764 0.392  0.220  -0.204 58  VAL EEE CG1 
6406  C CG2 . VAL E 58  ? 2.208 2.190 1.779 0.388  0.287  -0.217 58  VAL EEE CG2 
6407  N N   . LEU E 59  ? 2.177 2.127 1.743 0.393  0.213  -0.193 59  LEU EEE N   
6408  C CA  . LEU E 59  ? 2.216 2.179 1.814 0.398  0.189  -0.181 59  LEU EEE CA  
6409  C C   . LEU E 59  ? 2.316 2.265 1.923 0.399  0.149  -0.170 59  LEU EEE C   
6410  O O   . LEU E 59  ? 2.425 2.330 1.984 0.397  0.136  -0.174 59  LEU EEE O   
6411  C CB  . LEU E 59  ? 2.266 2.186 1.824 0.398  0.188  -0.179 59  LEU EEE CB  
6412  C CG  . LEU E 59  ? 2.273 2.198 1.822 0.395  0.220  -0.186 59  LEU EEE CG  
6413  C CD1 . LEU E 59  ? 2.436 2.298 1.922 0.394  0.219  -0.185 59  LEU EEE CD1 
6414  C CD2 . LEU E 59  ? 2.368 2.340 1.972 0.400  0.223  -0.182 59  LEU EEE CD2 
6415  N N   . ALA E 60  ? 2.370 2.355 2.041 0.404  0.131  -0.156 60  ALA EEE N   
6416  C CA  . ALA E 60  ? 2.482 2.455 2.176 0.404  0.088  -0.141 60  ALA EEE CA  
6417  C C   . ALA E 60  ? 2.832 2.733 2.471 0.402  0.053  -0.136 60  ALA EEE C   
6418  O O   . ALA E 60  ? 3.184 3.055 2.783 0.403  0.064  -0.139 60  ALA EEE O   
6419  C CB  . ALA E 60  ? 2.313 2.343 2.100 0.411  0.082  -0.122 60  ALA EEE CB  
6420  N N   . ASP E 61  ? 2.875 2.741 2.507 0.399  0.009  -0.127 61  ASP EEE N   
6421  C CA  . ASP E 61  ? 3.006 2.789 2.575 0.397  -0.034 -0.122 61  ASP EEE CA  
6422  C C   . ASP E 61  ? 3.112 2.904 2.733 0.399  -0.057 -0.103 61  ASP EEE C   
6423  O O   . ASP E 61  ? 3.267 2.995 2.828 0.399  -0.075 -0.103 61  ASP EEE O   
6424  C CB  . ASP E 61  ? 3.054 2.788 2.598 0.392  -0.082 -0.117 61  ASP EEE CB  
6425  C CG  . ASP E 61  ? 3.122 2.821 2.586 0.392  -0.058 -0.136 61  ASP EEE CG  
6426  O OD1 . ASP E 61  ? 3.063 2.788 2.511 0.394  -0.004 -0.151 61  ASP EEE OD1 
6427  O OD2 . ASP E 61  ? 3.298 2.937 2.715 0.390  -0.096 -0.135 61  ASP EEE OD2 
6428  N N   . SER E 62  ? 3.094 2.960 2.823 0.404  -0.055 -0.086 62  SER EEE N   
6429  C CA  . SER E 62  ? 2.958 2.836 2.748 0.410  -0.072 -0.065 62  SER EEE CA  
6430  C C   . SER E 62  ? 2.911 2.791 2.673 0.416  -0.035 -0.074 62  SER EEE C   
6431  O O   . SER E 62  ? 3.047 2.932 2.851 0.422  -0.047 -0.058 62  SER EEE O   
6432  C CB  . SER E 62  ? 2.836 2.793 2.750 0.417  -0.068 -0.043 62  SER EEE CB  
6433  O OG  . SER E 62  ? 2.873 2.834 2.819 0.410  -0.099 -0.034 62  SER EEE OG  
6434  N N   . VAL E 63  ? 2.903 2.781 2.604 0.414  0.008  -0.097 63  VAL EEE N   
6435  C CA  . VAL E 63  ? 2.890 2.773 2.570 0.418  0.043  -0.105 63  VAL EEE CA  
6436  C C   . VAL E 63  ? 2.944 2.767 2.522 0.411  0.057  -0.125 63  VAL EEE C   
6437  O O   . VAL E 63  ? 2.960 2.770 2.504 0.412  0.082  -0.132 63  VAL EEE O   
6438  C CB  . VAL E 63  ? 2.765 2.716 2.494 0.425  0.088  -0.109 63  VAL EEE CB  
6439  C CG1 . VAL E 63  ? 2.768 2.772 2.595 0.435  0.081  -0.087 63  VAL EEE CG1 
6440  C CG2 . VAL E 63  ? 2.685 2.650 2.388 0.418  0.112  -0.128 63  VAL EEE CG2 
6441  N N   . LYS E 64  ? 2.787 2.570 2.314 0.406  0.044  -0.132 64  LYS EEE N   
6442  C CA  . LYS E 64  ? 2.807 2.540 2.244 0.402  0.070  -0.149 64  LYS EEE CA  
6443  C C   . LYS E 64  ? 2.890 2.556 2.254 0.402  0.070  -0.151 64  LYS EEE C   
6444  O O   . LYS E 64  ? 2.889 2.544 2.214 0.401  0.110  -0.161 64  LYS EEE O   
6445  C CB  . LYS E 64  ? 2.809 2.496 2.198 0.399  0.050  -0.152 64  LYS EEE CB  
6446  C CG  . LYS E 64  ? 2.761 2.388 2.054 0.400  0.081  -0.167 64  LYS EEE CG  
6447  C CD  . LYS E 64  ? 2.880 2.440 2.108 0.401  0.054  -0.168 64  LYS EEE CD  
6448  C CE  . LYS E 64  ? 3.011 2.502 2.205 0.400  -0.010 -0.157 64  LYS EEE CE  
6449  N NZ  . LYS E 64  ? 3.052 2.463 2.169 0.402  -0.040 -0.159 64  LYS EEE NZ  
6450  N N   . GLY E 65  ? 2.987 2.605 2.335 0.403  0.023  -0.139 65  GLY EEE N   
6451  C CA  . GLY E 65  ? 3.090 2.637 2.362 0.404  0.021  -0.141 65  GLY EEE CA  
6452  C C   . GLY E 65  ? 3.109 2.696 2.419 0.406  0.045  -0.139 65  GLY EEE C   
6453  O O   . GLY E 65  ? 3.118 2.656 2.363 0.406  0.060  -0.144 65  GLY EEE O   
6454  N N   . ARG E 66  ? 3.058 2.726 2.466 0.410  0.051  -0.131 66  ARG EEE N   
6455  C CA  . ARG E 66  ? 3.064 2.761 2.508 0.415  0.064  -0.126 66  ARG EEE CA  
6456  C C   . ARG E 66  ? 3.022 2.779 2.499 0.417  0.112  -0.136 66  ARG EEE C   
6457  O O   . ARG E 66  ? 3.129 2.885 2.597 0.419  0.131  -0.138 66  ARG EEE O   
6458  C CB  . ARG E 66  ? 3.102 2.827 2.627 0.423  0.029  -0.105 66  ARG EEE CB  
6459  C CG  . ARG E 66  ? 3.152 2.817 2.655 0.420  -0.028 -0.093 66  ARG EEE CG  
6460  C CD  . ARG E 66  ? 3.194 2.896 2.799 0.426  -0.065 -0.068 66  ARG EEE CD  
6461  N NE  . ARG E 66  ? 3.104 2.876 2.789 0.428  -0.052 -0.062 66  ARG EEE NE  
6462  C CZ  . ARG E 66  ? 3.155 2.998 2.931 0.439  -0.028 -0.049 66  ARG EEE CZ  
6463  N NH1 . ARG E 66  ? 3.301 3.156 3.103 0.450  -0.013 -0.040 66  ARG EEE NH1 
6464  N NH2 . ARG E 66  ? 3.078 2.976 2.916 0.441  -0.016 -0.044 66  ARG EEE NH2 
6465  N N   . PHE E 67  ? 2.918 2.720 2.428 0.415  0.128  -0.141 67  PHE EEE N   
6466  C CA  . PHE E 67  ? 2.844 2.696 2.384 0.416  0.166  -0.149 67  PHE EEE CA  
6467  C C   . PHE E 67  ? 2.762 2.600 2.257 0.406  0.194  -0.165 67  PHE EEE C   
6468  O O   . PHE E 67  ? 2.780 2.584 2.233 0.401  0.189  -0.169 67  PHE EEE O   
6469  C CB  . PHE E 67  ? 2.773 2.687 2.386 0.423  0.167  -0.143 67  PHE EEE CB  
6470  C CG  . PHE E 67  ? 2.881 2.819 2.556 0.435  0.152  -0.124 67  PHE EEE CG  
6471  C CD1 . PHE E 67  ? 3.078 2.985 2.748 0.440  0.131  -0.112 67  PHE EEE CD1 
6472  C CD2 . PHE E 67  ? 2.818 2.808 2.557 0.445  0.162  -0.115 67  PHE EEE CD2 
6473  C CE1 . PHE E 67  ? 3.072 3.005 2.811 0.453  0.121  -0.091 67  PHE EEE CE1 
6474  C CE2 . PHE E 67  ? 2.890 2.903 2.694 0.459  0.156  -0.094 67  PHE EEE CE2 
6475  C CZ  . PHE E 67  ? 3.019 3.005 2.827 0.464  0.136  -0.080 67  PHE EEE CZ  
6476  N N   . THR E 68  ? 2.765 2.626 2.271 0.404  0.222  -0.172 68  THR EEE N   
6477  C CA  . THR E 68  ? 2.724 2.585 2.213 0.395  0.250  -0.183 68  THR EEE CA  
6478  C C   . THR E 68  ? 2.750 2.663 2.289 0.395  0.265  -0.188 68  THR EEE C   
6479  O O   . THR E 68  ? 2.777 2.704 2.335 0.402  0.263  -0.185 68  THR EEE O   
6480  C CB  . THR E 68  ? 2.725 2.540 2.164 0.389  0.266  -0.185 68  THR EEE CB  
6481  O OG1 . THR E 68  ? 2.843 2.601 2.228 0.392  0.247  -0.180 68  THR EEE OG1 
6482  C CG2 . THR E 68  ? 2.677 2.487 2.105 0.380  0.296  -0.191 68  THR EEE CG2 
6483  N N   . ILE E 69  ? 2.731 2.664 2.284 0.388  0.279  -0.195 69  ILE EEE N   
6484  C CA  . ILE E 69  ? 2.556 2.528 2.150 0.387  0.289  -0.200 69  ILE EEE CA  
6485  C C   . ILE E 69  ? 2.466 2.432 2.059 0.375  0.310  -0.205 69  ILE EEE C   
6486  O O   . ILE E 69  ? 2.494 2.444 2.072 0.369  0.324  -0.205 69  ILE EEE O   
6487  C CB  . ILE E 69  ? 2.420 2.429 2.048 0.390  0.283  -0.201 69  ILE EEE CB  
6488  C CG1 . ILE E 69  ? 2.289 2.329 1.949 0.388  0.291  -0.207 69  ILE EEE CG1 
6489  C CG2 . ILE E 69  ? 2.434 2.432 2.046 0.385  0.288  -0.203 69  ILE EEE CG2 
6490  C CD1 . ILE E 69  ? 2.175 2.251 1.868 0.394  0.285  -0.207 69  ILE EEE CD1 
6491  N N   . SER E 70  ? 2.387 2.360 1.995 0.372  0.311  -0.207 70  SER EEE N   
6492  C CA  . SER E 70  ? 2.473 2.442 2.096 0.359  0.326  -0.209 70  SER EEE CA  
6493  C C   . SER E 70  ? 2.467 2.456 2.122 0.357  0.316  -0.214 70  SER EEE C   
6494  O O   . SER E 70  ? 2.550 2.545 2.200 0.368  0.303  -0.215 70  SER EEE O   
6495  C CB  . SER E 70  ? 2.602 2.532 2.195 0.354  0.332  -0.205 70  SER EEE CB  
6496  O OG  . SER E 70  ? 2.716 2.616 2.265 0.359  0.335  -0.201 70  SER EEE OG  
6497  N N   . ILE E 71  ? 2.467 2.464 2.155 0.343  0.322  -0.214 71  ILE EEE N   
6498  C CA  . ILE E 71  ? 2.525 2.531 2.241 0.339  0.306  -0.218 71  ILE EEE CA  
6499  C C   . ILE E 71  ? 2.689 2.673 2.420 0.325  0.304  -0.214 71  ILE EEE C   
6500  O O   . ILE E 71  ? 2.634 2.619 2.390 0.313  0.322  -0.206 71  ILE EEE O   
6501  C CB  . ILE E 71  ? 2.459 2.499 2.218 0.335  0.306  -0.220 71  ILE EEE CB  
6502  C CG1 . ILE E 71  ? 2.490 2.549 2.236 0.350  0.303  -0.224 71  ILE EEE CG1 
6503  C CG2 . ILE E 71  ? 2.440 2.477 2.227 0.328  0.285  -0.223 71  ILE EEE CG2 
6504  C CD1 . ILE E 71  ? 2.572 2.659 2.352 0.349  0.295  -0.229 71  ILE EEE CD1 
6505  N N   . ASP E 72  ? 2.875 2.835 2.589 0.326  0.282  -0.217 72  ASP EEE N   
6506  C CA  . ASP E 72  ? 2.897 2.830 2.625 0.311  0.270  -0.213 72  ASP EEE CA  
6507  C C   . ASP E 72  ? 2.950 2.883 2.706 0.306  0.243  -0.216 72  ASP EEE C   
6508  O O   . ASP E 72  ? 2.908 2.818 2.624 0.317  0.222  -0.224 72  ASP EEE O   
6509  C CB  . ASP E 72  ? 2.840 2.732 2.514 0.318  0.262  -0.213 72  ASP EEE CB  
6510  C CG  . ASP E 72  ? 2.902 2.762 2.590 0.302  0.247  -0.208 72  ASP EEE CG  
6511  O OD1 . ASP E 72  ? 2.934 2.810 2.683 0.284  0.247  -0.201 72  ASP EEE OD1 
6512  O OD2 . ASP E 72  ? 2.938 2.758 2.580 0.307  0.236  -0.209 72  ASP EEE OD2 
6513  N N   . SER E 73  ? 2.915 2.870 2.738 0.289  0.243  -0.210 73  SER EEE N   
6514  C CA  . SER E 73  ? 2.943 2.896 2.799 0.281  0.211  -0.212 73  SER EEE CA  
6515  C C   . SER E 73  ? 3.041 2.942 2.881 0.272  0.176  -0.211 73  SER EEE C   
6516  O O   . SER E 73  ? 3.105 2.980 2.938 0.271  0.139  -0.216 73  SER EEE O   
6517  C CB  . SER E 73  ? 2.896 2.889 2.840 0.266  0.221  -0.203 73  SER EEE CB  
6518  O OG  . SER E 73  ? 2.936 2.928 2.926 0.250  0.237  -0.188 73  SER EEE OG  
6519  N N   . ALA E 74  ? 3.107 2.987 2.937 0.266  0.184  -0.205 74  ALA EEE N   
6520  C CA  . ALA E 74  ? 3.199 3.024 3.007 0.258  0.150  -0.203 74  ALA EEE CA  
6521  C C   . ALA E 74  ? 3.342 3.118 3.058 0.279  0.129  -0.217 74  ALA EEE C   
6522  O O   . ALA E 74  ? 3.469 3.194 3.160 0.277  0.088  -0.221 74  ALA EEE O   
6523  C CB  . ALA E 74  ? 3.198 3.014 3.010 0.250  0.168  -0.193 74  ALA EEE CB  
6524  N N   . GLU E 75  ? 3.349 3.132 3.012 0.301  0.156  -0.222 75  GLU EEE N   
6525  C CA  . GLU E 75  ? 3.410 3.149 2.990 0.325  0.148  -0.231 75  GLU EEE CA  
6526  C C   . GLU E 75  ? 3.346 3.099 2.913 0.341  0.148  -0.237 75  GLU EEE C   
6527  O O   . GLU E 75  ? 3.374 3.089 2.874 0.364  0.148  -0.242 75  GLU EEE O   
6528  C CB  . GLU E 75  ? 3.300 3.046 2.844 0.341  0.178  -0.229 75  GLU EEE CB  
6529  C CG  . GLU E 75  ? 3.273 2.971 2.775 0.341  0.172  -0.226 75  GLU EEE CG  
6530  C CD  . GLU E 75  ? 3.348 2.974 2.777 0.356  0.147  -0.232 75  GLU EEE CD  
6531  O OE1 . GLU E 75  ? 3.442 3.057 2.836 0.377  0.149  -0.237 75  GLU EEE OE1 
6532  O OE2 . GLU E 75  ? 3.315 2.891 2.717 0.349  0.128  -0.231 75  GLU EEE OE2 
6533  N N   . ASN E 76  ? 3.164 2.966 2.792 0.330  0.153  -0.237 76  ASN EEE N   
6534  C CA  . ASN E 76  ? 3.050 2.868 2.670 0.344  0.153  -0.242 76  ASN EEE CA  
6535  C C   . ASN E 76  ? 3.071 2.902 2.652 0.369  0.182  -0.243 76  ASN EEE C   
6536  O O   . ASN E 76  ? 2.948 2.756 2.485 0.389  0.182  -0.246 76  ASN EEE O   
6537  C CB  . ASN E 76  ? 3.038 2.795 2.616 0.348  0.116  -0.249 76  ASN EEE CB  
6538  C CG  . ASN E 76  ? 3.056 2.811 2.693 0.322  0.081  -0.246 76  ASN EEE CG  
6539  O OD1 . ASN E 76  ? 3.045 2.829 2.749 0.301  0.084  -0.238 76  ASN EEE OD1 
6540  N ND2 . ASN E 76  ? 3.082 2.797 2.697 0.324  0.047  -0.252 76  ASN EEE ND2 
6541  N N   . THR E 77  ? 3.207 3.071 2.806 0.368  0.208  -0.237 77  THR EEE N   
6542  C CA  . THR E 77  ? 3.146 3.021 2.719 0.389  0.230  -0.234 77  THR EEE CA  
6543  C C   . THR E 77  ? 3.002 2.932 2.617 0.384  0.249  -0.231 77  THR EEE C   
6544  O O   . THR E 77  ? 2.762 2.713 2.414 0.366  0.253  -0.230 77  THR EEE O   
6545  C CB  . THR E 77  ? 3.087 2.924 2.615 0.398  0.234  -0.231 77  THR EEE CB  
6546  O OG1 . THR E 77  ? 2.962 2.804 2.470 0.422  0.252  -0.225 77  THR EEE OG1 
6547  C CG2 . THR E 77  ? 3.012 2.863 2.565 0.381  0.241  -0.227 77  THR EEE CG2 
6548  N N   . LEU E 78  ? 2.926 2.875 2.536 0.402  0.262  -0.227 78  LEU EEE N   
6549  C CA  . LEU E 78  ? 2.798 2.787 2.438 0.399  0.274  -0.223 78  LEU EEE CA  
6550  C C   . LEU E 78  ? 2.772 2.751 2.391 0.410  0.281  -0.215 78  LEU EEE C   
6551  O O   . LEU E 78  ? 2.940 2.910 2.545 0.430  0.285  -0.209 78  LEU EEE O   
6552  C CB  . LEU E 78  ? 2.723 2.745 2.385 0.407  0.276  -0.223 78  LEU EEE CB  
6553  C CG  . LEU E 78  ? 2.608 2.667 2.303 0.398  0.282  -0.222 78  LEU EEE CG  
6554  C CD1 . LEU E 78  ? 2.552 2.639 2.268 0.406  0.281  -0.222 78  LEU EEE CD1 
6555  C CD2 . LEU E 78  ? 2.608 2.666 2.295 0.401  0.287  -0.214 78  LEU EEE CD2 
6556  N N   . ALA E 79  ? 2.705 2.681 2.323 0.400  0.285  -0.213 79  ALA EEE N   
6557  C CA  . ALA E 79  ? 2.743 2.701 2.340 0.408  0.287  -0.206 79  ALA EEE CA  
6558  C C   . ALA E 79  ? 2.769 2.747 2.380 0.410  0.287  -0.200 79  ALA EEE C   
6559  O O   . ALA E 79  ? 2.844 2.835 2.466 0.399  0.289  -0.203 79  ALA EEE O   
6560  C CB  . ALA E 79  ? 2.747 2.675 2.321 0.396  0.288  -0.207 79  ALA EEE CB  
6561  N N   . LEU E 80  ? 2.823 2.800 2.435 0.425  0.283  -0.190 80  LEU EEE N   
6562  C CA  . LEU E 80  ? 2.909 2.893 2.531 0.426  0.274  -0.182 80  LEU EEE CA  
6563  C C   . LEU E 80  ? 3.104 3.057 2.703 0.431  0.268  -0.175 80  LEU EEE C   
6564  O O   . LEU E 80  ? 3.295 3.246 2.903 0.447  0.268  -0.166 80  LEU EEE O   
6565  C CB  . LEU E 80  ? 2.859 2.875 2.522 0.439  0.269  -0.172 80  LEU EEE CB  
6566  C CG  . LEU E 80  ? 2.879 2.901 2.563 0.441  0.252  -0.161 80  LEU EEE CG  
6567  C CD1 . LEU E 80  ? 2.866 2.892 2.544 0.427  0.245  -0.168 80  LEU EEE CD1 
6568  C CD2 . LEU E 80  ? 2.816 2.868 2.552 0.458  0.251  -0.145 80  LEU EEE CD2 
6569  N N   . GLN E 81  ? 3.100 3.025 2.668 0.420  0.264  -0.178 81  GLN EEE N   
6570  C CA  . GLN E 81  ? 3.137 3.027 2.678 0.423  0.256  -0.171 81  GLN EEE CA  
6571  C C   . GLN E 81  ? 3.195 3.080 2.746 0.428  0.233  -0.160 81  GLN EEE C   
6572  O O   . GLN E 81  ? 3.205 3.082 2.743 0.420  0.224  -0.162 81  GLN EEE O   
6573  C CB  . GLN E 81  ? 3.142 2.995 2.638 0.409  0.264  -0.178 81  GLN EEE CB  
6574  C CG  . GLN E 81  ? 3.167 2.977 2.627 0.412  0.254  -0.172 81  GLN EEE CG  
6575  C CD  . GLN E 81  ? 3.117 2.920 2.574 0.420  0.258  -0.171 81  GLN EEE CD  
6576  O OE1 . GLN E 81  ? 2.991 2.795 2.445 0.415  0.270  -0.178 81  GLN EEE OE1 
6577  N NE2 . GLN E 81  ? 3.289 3.079 2.748 0.433  0.244  -0.160 81  GLN EEE NE2 
6578  N N   . MET E 82  ? 3.293 3.181 2.868 0.442  0.223  -0.147 82  MET EEE N   
6579  C CA  . MET E 82  ? 3.372 3.259 2.975 0.448  0.195  -0.131 82  MET EEE CA  
6580  C C   . MET E 82  ? 3.544 3.391 3.125 0.451  0.179  -0.123 82  MET EEE C   
6581  O O   . MET E 82  ? 3.808 3.657 3.403 0.464  0.188  -0.116 82  MET EEE O   
6582  C CB  . MET E 82  ? 3.244 3.177 2.918 0.463  0.197  -0.116 82  MET EEE CB  
6583  C CG  . MET E 82  ? 3.108 3.076 2.797 0.465  0.222  -0.125 82  MET EEE CG  
6584  S SD  . MET E 82  ? 3.031 3.040 2.791 0.488  0.235  -0.105 82  MET EEE SD  
6585  C CE  . MET E 82  ? 3.195 3.179 2.946 0.507  0.248  -0.095 82  MET EEE CE  
6586  N N   . ASN E 83  A 3.437 3.240 2.974 0.441  0.156  -0.125 82  ASN EEE N   
6587  C CA  . ASN E 83  A 3.436 3.192 2.946 0.443  0.134  -0.117 82  ASN EEE CA  
6588  C C   . ASN E 83  A 3.469 3.218 3.016 0.446  0.091  -0.099 82  ASN EEE C   
6589  O O   . ASN E 83  A 3.489 3.259 3.065 0.444  0.078  -0.096 82  ASN EEE O   
6590  C CB  . ASN E 83  A 3.359 3.055 2.782 0.430  0.138  -0.130 82  ASN EEE CB  
6591  C CG  . ASN E 83  A 3.265 2.967 2.663 0.425  0.176  -0.143 82  ASN EEE CG  
6592  O OD1 . ASN E 83  A 3.212 2.957 2.641 0.424  0.198  -0.150 82  ASN EEE OD1 
6593  N ND2 . ASN E 83  A 3.200 2.856 2.546 0.421  0.181  -0.147 82  ASN EEE ND2 
6594  N N   . ARG E 84  B 3.534 3.252 3.081 0.452  0.066  -0.087 82  ARG EEE N   
6595  C CA  . ARG E 84  B 3.571 3.276 3.160 0.454  0.017  -0.067 82  ARG EEE CA  
6596  C C   . ARG E 84  B 3.473 3.245 3.169 0.464  0.017  -0.048 82  ARG EEE C   
6597  O O   . ARG E 84  B 3.332 3.109 3.061 0.459  -0.015 -0.039 82  ARG EEE O   
6598  C CB  . ARG E 84  B 3.540 3.184 3.062 0.441  -0.018 -0.073 82  ARG EEE CB  
6599  C CG  . ARG E 84  B 3.524 3.091 2.933 0.433  -0.014 -0.089 82  ARG EEE CG  
6600  C CD  . ARG E 84  B 3.430 2.990 2.780 0.424  0.021  -0.109 82  ARG EEE CD  
6601  N NE  . ARG E 84  B 3.475 2.947 2.715 0.418  0.016  -0.119 82  ARG EEE NE  
6602  C CZ  . ARG E 84  B 3.554 2.963 2.737 0.414  -0.015 -0.119 82  ARG EEE CZ  
6603  N NH1 . ARG E 84  B 3.479 2.910 2.712 0.414  -0.048 -0.110 82  ARG EEE NH1 
6604  N NH2 . ARG E 84  B 3.694 3.013 2.765 0.412  -0.013 -0.127 82  ARG EEE NH2 
6605  N N   . LEU E 85  C 3.587 3.408 3.333 0.479  0.054  -0.043 82  LEU EEE N   
6606  C CA  . LEU E 85  C 3.447 3.329 3.285 0.490  0.066  -0.026 82  LEU EEE CA  
6607  C C   . LEU E 85  C 3.599 3.488 3.525 0.497  0.026  0.005  82  LEU EEE C   
6608  O O   . LEU E 85  C 3.831 3.692 3.763 0.501  0.004  0.017  82  LEU EEE O   
6609  C CB  . LEU E 85  C 3.285 3.198 3.140 0.509  0.116  -0.026 82  LEU EEE CB  
6610  C CG  . LEU E 85  C 3.179 3.097 2.974 0.503  0.152  -0.052 82  LEU EEE CG  
6611  C CD1 . LEU E 85  C 3.125 3.053 2.921 0.522  0.192  -0.051 82  LEU EEE CD1 
6612  C CD2 . LEU E 85  C 3.099 3.052 2.919 0.497  0.155  -0.056 82  LEU EEE CD2 
6613  N N   . LYS E 86  ? 3.408 3.336 3.408 0.497  0.015  0.021  83  LYS EEE N   
6614  C CA  . LYS E 86  ? 3.396 3.336 3.496 0.501  -0.027 0.054  83  LYS EEE CA  
6615  C C   . LYS E 86  ? 3.380 3.388 3.595 0.521  0.006  0.081  83  LYS EEE C   
6616  O O   . LYS E 86  ? 3.369 3.410 3.575 0.529  0.054  0.071  83  LYS EEE O   
6617  C CB  . LYS E 86  ? 3.293 3.205 3.382 0.482  -0.082 0.054  83  LYS EEE CB  
6618  C CG  . LYS E 86  ? 3.235 3.070 3.196 0.465  -0.107 0.027  83  LYS EEE CG  
6619  C CD  . LYS E 86  ? 3.163 2.952 3.109 0.450  -0.169 0.031  83  LYS EEE CD  
6620  C CE  . LYS E 86  ? 3.190 2.902 2.992 0.437  -0.175 0.001  83  LYS EEE CE  
6621  N NZ  . LYS E 86  ? 3.305 2.956 3.071 0.424  -0.234 0.003  83  LYS EEE NZ  
6622  N N   . PRO E 87  ? 3.373 3.400 3.700 0.531  -0.017 0.119  84  PRO EEE N   
6623  C CA  . PRO E 87  ? 3.280 3.370 3.725 0.552  0.018  0.150  84  PRO EEE CA  
6624  C C   . PRO E 87  ? 3.173 3.297 3.648 0.543  0.018  0.149  84  PRO EEE C   
6625  O O   . PRO E 87  ? 3.196 3.364 3.713 0.560  0.068  0.158  84  PRO EEE O   
6626  C CB  . PRO E 87  ? 3.386 3.483 3.951 0.559  -0.020 0.192  84  PRO EEE CB  
6627  C CG  . PRO E 87  ? 3.471 3.509 3.964 0.551  -0.056 0.179  84  PRO EEE CG  
6628  C CD  . PRO E 87  ? 3.423 3.412 3.776 0.528  -0.071 0.137  84  PRO EEE CD  
6629  N N   . GLU E 88  ? 3.119 3.216 3.567 0.519  -0.037 0.140  85  GLU EEE N   
6630  C CA  . GLU E 88  ? 3.077 3.203 3.546 0.511  -0.037 0.138  85  GLU EEE CA  
6631  C C   . GLU E 88  ? 3.107 3.243 3.487 0.512  0.016  0.104  85  GLU EEE C   
6632  O O   . GLU E 88  ? 3.055 3.224 3.459 0.510  0.031  0.103  85  GLU EEE O   
6633  C CB  . GLU E 88  ? 3.008 3.089 3.444 0.486  -0.108 0.131  85  GLU EEE CB  
6634  C CG  . GLU E 88  ? 3.035 3.099 3.560 0.481  -0.175 0.166  85  GLU EEE CG  
6635  C CD  . GLU E 88  ? 3.126 3.130 3.602 0.457  -0.249 0.159  85  GLU EEE CD  
6636  O OE1 . GLU E 88  ? 3.137 3.093 3.480 0.446  -0.247 0.122  85  GLU EEE OE1 
6637  O OE2 . GLU E 88  ? 3.234 3.232 3.802 0.451  -0.310 0.191  85  GLU EEE OE2 
6638  N N   . ASP E 89  ? 3.289 3.395 3.572 0.513  0.042  0.077  86  ASP EEE N   
6639  C CA  . ASP E 89  ? 3.224 3.335 3.428 0.514  0.089  0.046  86  ASP EEE CA  
6640  C C   . ASP E 89  ? 3.157 3.303 3.396 0.539  0.147  0.056  86  ASP EEE C   
6641  O O   . ASP E 89  ? 3.098 3.246 3.278 0.540  0.182  0.034  86  ASP EEE O   
6642  C CB  . ASP E 89  ? 3.289 3.349 3.379 0.503  0.088  0.016  86  ASP EEE CB  
6643  C CG  . ASP E 89  ? 3.449 3.463 3.481 0.481  0.041  0.002  86  ASP EEE CG  
6644  O OD1 . ASP E 89  ? 3.740 3.732 3.806 0.476  -0.007 0.020  86  ASP EEE OD1 
6645  O OD2 . ASP E 89  ? 3.390 3.385 3.341 0.469  0.053  -0.026 86  ASP EEE OD2 
6646  N N   . THR E 90  ? 3.224 3.390 3.554 0.559  0.157  0.091  87  THR EEE N   
6647  C CA  . THR E 90  ? 3.176 3.365 3.534 0.588  0.216  0.104  87  THR EEE CA  
6648  C C   . THR E 90  ? 3.092 3.313 3.470 0.591  0.243  0.104  87  THR EEE C   
6649  O O   . THR E 90  ? 2.943 3.196 3.404 0.586  0.222  0.126  87  THR EEE O   
6650  C CB  . THR E 90  ? 3.181 3.387 3.649 0.610  0.221  0.147  87  THR EEE CB  
6651  O OG1 . THR E 90  ? 3.355 3.528 3.801 0.607  0.195  0.146  87  THR EEE OG1 
6652  C CG2 . THR E 90  ? 3.265 3.484 3.756 0.645  0.290  0.164  87  THR EEE CG2 
6653  N N   . ALA E 91  ? 3.166 3.375 3.468 0.600  0.285  0.082  88  ALA EEE N   
6654  C CA  . ALA E 91  ? 3.152 3.381 3.450 0.605  0.312  0.077  88  ALA EEE CA  
6655  C C   . ALA E 91  ? 3.197 3.393 3.397 0.616  0.352  0.053  88  ALA EEE C   
6656  O O   . ALA E 91  ? 3.330 3.490 3.463 0.616  0.352  0.036  88  ALA EEE O   
6657  C CB  . ALA E 91  ? 3.056 3.297 3.340 0.576  0.275  0.059  88  ALA EEE CB  
6658  N N   . VAL E 92  ? 3.086 3.289 3.276 0.627  0.383  0.051  89  VAL EEE N   
6659  C CA  . VAL E 92  ? 3.004 3.171 3.095 0.633  0.409  0.024  89  VAL EEE CA  
6660  C C   . VAL E 92  ? 2.933 3.103 2.974 0.602  0.379  -0.009 89  VAL EEE C   
6661  O O   . VAL E 92  ? 2.907 3.109 2.989 0.590  0.364  -0.006 89  VAL EEE O   
6662  C CB  . VAL E 92  ? 2.947 3.108 3.044 0.662  0.457  0.041  89  VAL EEE CB  
6663  C CG1 . VAL E 92  ? 2.997 3.113 2.986 0.665  0.472  0.011  89  VAL EEE CG1 
6664  C CG2 . VAL E 92  ? 3.036 3.186 3.175 0.697  0.496  0.074  89  VAL EEE CG2 
6665  N N   . TYR E 93  ? 2.792 2.927 2.749 0.591  0.373  -0.037 90  TYR EEE N   
6666  C CA  . TYR E 93  ? 2.716 2.852 2.631 0.563  0.348  -0.066 90  TYR EEE CA  
6667  C C   . TYR E 93  ? 2.723 2.839 2.582 0.566  0.365  -0.084 90  TYR EEE C   
6668  O O   . TYR E 93  ? 2.801 2.875 2.607 0.582  0.386  -0.088 90  TYR EEE O   
6669  C CB  . TYR E 93  ? 2.775 2.887 2.648 0.545  0.327  -0.082 90  TYR EEE CB  
6670  C CG  . TYR E 93  ? 2.840 2.963 2.754 0.535  0.298  -0.070 90  TYR EEE CG  
6671  C CD1 . TYR E 93  ? 2.964 3.091 2.929 0.552  0.299  -0.044 90  TYR EEE CD1 
6672  C CD2 . TYR E 93  ? 2.835 2.960 2.736 0.511  0.268  -0.083 90  TYR EEE CD2 
6673  C CE1 . TYR E 93  ? 2.964 3.094 2.965 0.541  0.265  -0.032 90  TYR EEE CE1 
6674  C CE2 . TYR E 93  ? 2.829 2.950 2.753 0.502  0.238  -0.073 90  TYR EEE CE2 
6675  C CZ  . TYR E 93  ? 2.874 2.997 2.849 0.517  0.233  -0.048 90  TYR EEE CZ  
6676  O OH  . TYR E 93  ? 2.843 2.954 2.840 0.507  0.195  -0.037 90  TYR EEE OH  
6677  N N   . TYR E 94  ? 2.687 2.825 2.551 0.551  0.354  -0.096 91  TYR EEE N   
6678  C CA  . TYR E 94  ? 2.748 2.869 2.566 0.551  0.363  -0.112 91  TYR EEE CA  
6679  C C   . TYR E 94  ? 2.705 2.828 2.497 0.523  0.339  -0.137 91  TYR EEE C   
6680  O O   . TYR E 94  ? 2.668 2.819 2.490 0.505  0.320  -0.140 91  TYR EEE O   
6681  C CB  . TYR E 94  ? 2.755 2.902 2.613 0.561  0.376  -0.100 91  TYR EEE CB  
6682  C CG  . TYR E 94  ? 2.841 2.999 2.751 0.588  0.402  -0.068 91  TYR EEE CG  
6683  C CD1 . TYR E 94  ? 2.867 3.064 2.857 0.583  0.389  -0.046 91  TYR EEE CD1 
6684  C CD2 . TYR E 94  ? 2.878 3.002 2.759 0.618  0.439  -0.056 91  TYR EEE CD2 
6685  C CE1 . TYR E 94  ? 2.833 3.045 2.889 0.607  0.412  -0.013 91  TYR EEE CE1 
6686  C CE2 . TYR E 94  ? 2.888 3.022 2.826 0.644  0.470  -0.023 91  TYR EEE CE2 
6687  C CZ  . TYR E 94  ? 2.811 2.994 2.845 0.638  0.456  -0.000 91  TYR EEE CZ  
6688  O OH  . TYR E 94  ? 2.742 2.941 2.850 0.663  0.486  0.037  91  TYR EEE OH  
6689  N N   . CYS E 95  ? 2.946 3.034 2.682 0.520  0.339  -0.155 92  CYS EEE N   
6690  C CA  . CYS E 95  ? 2.871 2.965 2.596 0.496  0.321  -0.175 92  CYS EEE CA  
6691  C C   . CYS E 95  ? 2.764 2.866 2.490 0.497  0.321  -0.181 92  CYS EEE C   
6692  O O   . CYS E 95  ? 2.836 2.916 2.541 0.516  0.335  -0.175 92  CYS EEE O   
6693  C CB  . CYS E 95  ? 2.988 3.042 2.665 0.488  0.313  -0.189 92  CYS EEE CB  
6694  S SG  . CYS E 95  ? 3.422 3.411 3.033 0.513  0.325  -0.188 92  CYS EEE SG  
6695  N N   . PHE E 96  ? 2.479 2.607 2.225 0.476  0.306  -0.192 93  PHE EEE N   
6696  C CA  . PHE E 96  ? 2.385 2.520 2.133 0.473  0.301  -0.201 93  PHE EEE CA  
6697  C C   . PHE E 96  ? 2.411 2.543 2.155 0.451  0.284  -0.217 93  PHE EEE C   
6698  O O   . PHE E 96  ? 2.489 2.630 2.244 0.436  0.280  -0.220 93  PHE EEE O   
6699  C CB  . PHE E 96  ? 2.294 2.472 2.088 0.472  0.302  -0.193 93  PHE EEE CB  
6700  C CG  . PHE E 96  ? 2.184 2.391 2.006 0.453  0.290  -0.197 93  PHE EEE CG  
6701  C CD1 . PHE E 96  ? 2.132 2.349 1.958 0.437  0.281  -0.211 93  PHE EEE CD1 
6702  C CD2 . PHE E 96  ? 2.151 2.368 1.992 0.453  0.287  -0.186 93  PHE EEE CD2 
6703  C CE1 . PHE E 96  ? 2.074 2.307 1.916 0.423  0.275  -0.213 93  PHE EEE CE1 
6704  C CE2 . PHE E 96  ? 2.171 2.398 2.020 0.438  0.275  -0.190 93  PHE EEE CE2 
6705  C CZ  . PHE E 96  ? 2.114 2.347 1.960 0.424  0.272  -0.204 93  PHE EEE CZ  
6706  N N   . ALA E 97  ? 2.326 2.443 2.056 0.449  0.275  -0.226 94  ALA EEE N   
6707  C CA  . ALA E 97  ? 2.190 2.309 1.934 0.428  0.258  -0.238 94  ALA EEE CA  
6708  C C   . ALA E 97  ? 2.116 2.253 1.879 0.426  0.251  -0.243 94  ALA EEE C   
6709  O O   . ALA E 97  ? 2.162 2.282 1.900 0.441  0.253  -0.241 94  ALA EEE O   
6710  C CB  . ALA E 97  ? 2.198 2.267 1.905 0.425  0.242  -0.245 94  ALA EEE CB  
6711  N N   . ALA E 98  ? 2.099 2.266 1.902 0.408  0.244  -0.248 95  ALA EEE N   
6712  C CA  . ALA E 98  ? 1.996 2.181 1.818 0.407  0.236  -0.252 95  ALA EEE CA  
6713  C C   . ALA E 98  ? 2.055 2.226 1.891 0.393  0.215  -0.261 95  ALA EEE C   
6714  O O   . ALA E 98  ? 2.004 2.193 1.879 0.377  0.213  -0.262 95  ALA EEE O   
6715  C CB  . ALA E 98  ? 1.644 1.874 1.505 0.401  0.246  -0.250 95  ALA EEE CB  
6716  N N   . LEU E 99  ? 2.207 2.343 2.012 0.400  0.198  -0.265 96  LEU EEE N   
6717  C CA  . LEU E 99  ? 2.333 2.450 2.151 0.389  0.168  -0.272 96  LEU EEE CA  
6718  C C   . LEU E 99  ? 2.566 2.673 2.360 0.401  0.165  -0.274 96  LEU EEE C   
6719  O O   . LEU E 99  ? 2.760 2.835 2.498 0.421  0.176  -0.271 96  LEU EEE O   
6720  C CB  . LEU E 99  ? 2.554 2.611 2.337 0.385  0.143  -0.274 96  LEU EEE CB  
6721  C CG  . LEU E 99  ? 2.421 2.475 2.252 0.365  0.110  -0.277 96  LEU EEE CG  
6722  C CD1 . LEU E 99  ? 2.243 2.359 2.157 0.348  0.125  -0.272 96  LEU EEE CD1 
6723  C CD2 . LEU E 99  ? 2.615 2.605 2.415 0.358  0.076  -0.279 96  LEU EEE CD2 
6724  N N   . ASP E 100 ? 2.615 2.742 2.446 0.392  0.150  -0.278 97  ASP EEE N   
6725  C CA  . ASP E 100 ? 2.704 2.815 2.508 0.403  0.143  -0.281 97  ASP EEE CA  
6726  C C   . ASP E 100 ? 2.562 2.690 2.345 0.422  0.174  -0.274 97  ASP EEE C   
6727  O O   . ASP E 100 ? 2.542 2.716 2.362 0.420  0.185  -0.272 97  ASP EEE O   
6728  C CB  . ASP E 100 ? 2.952 2.983 2.690 0.410  0.112  -0.286 97  ASP EEE CB  
6729  C CG  . ASP E 100 ? 3.181 3.155 2.851 0.423  0.118  -0.284 97  ASP EEE CG  
6730  O OD1 . ASP E 100 ? 3.177 3.129 2.795 0.446  0.144  -0.278 97  ASP EEE OD1 
6731  O OD2 . ASP E 100 ? 3.505 3.454 3.176 0.411  0.098  -0.286 97  ASP EEE OD2 
6732  N N   . THR E 101 ? 2.435 2.525 2.163 0.440  0.189  -0.267 98  THR EEE N   
6733  C CA  . THR E 101 ? 2.297 2.412 2.027 0.456  0.221  -0.255 98  THR EEE CA  
6734  C C   . THR E 101 ? 2.221 2.350 1.961 0.456  0.237  -0.248 98  THR EEE C   
6735  O O   . THR E 101 ? 2.295 2.420 2.042 0.443  0.227  -0.254 98  THR EEE O   
6736  C CB  . THR E 101 ? 2.414 2.476 2.081 0.482  0.234  -0.249 98  THR EEE CB  
6737  O OG1 . THR E 101 ? 2.124 2.220 1.815 0.496  0.265  -0.233 98  THR EEE OG1 
6738  C CG2 . THR E 101 ? 2.628 2.620 2.226 0.495  0.235  -0.249 98  THR EEE CG2 
6739  N N   . ALA E 102 ? 1.836 1.983 1.584 0.470  0.262  -0.234 101 ALA EEE N   
6740  C CA  . ALA E 102 ? 1.786 1.940 1.541 0.473  0.275  -0.226 101 ALA EEE CA  
6741  C C   . ALA E 102 ? 2.106 2.207 1.806 0.495  0.290  -0.219 101 ALA EEE C   
6742  O O   . ALA E 102 ? 2.246 2.322 1.919 0.516  0.307  -0.209 101 ALA EEE O   
6743  C CB  . ALA E 102 ? 1.620 1.825 1.426 0.474  0.288  -0.213 101 ALA EEE CB  
6744  N N   . TYR E 103 ? 2.145 2.222 1.824 0.491  0.285  -0.222 102 TYR EEE N   
6745  C CA  . TYR E 103 ? 2.302 2.323 1.924 0.512  0.300  -0.216 102 TYR EEE CA  
6746  C C   . TYR E 103 ? 2.385 2.429 2.033 0.516  0.316  -0.204 102 TYR EEE C   
6747  O O   . TYR E 103 ? 2.374 2.455 2.060 0.497  0.305  -0.207 102 TYR EEE O   
6748  C CB  . TYR E 103 ? 2.350 2.308 1.913 0.507  0.276  -0.230 102 TYR EEE CB  
6749  C CG  . TYR E 103 ? 2.489 2.412 2.022 0.502  0.250  -0.242 102 TYR EEE CG  
6750  C CD1 . TYR E 103 ? 2.688 2.541 2.145 0.526  0.256  -0.240 102 TYR EEE CD1 
6751  C CD2 . TYR E 103 ? 2.351 2.301 1.926 0.475  0.221  -0.253 102 TYR EEE CD2 
6752  C CE1 . TYR E 103 ? 2.792 2.601 2.213 0.522  0.227  -0.251 102 TYR EEE CE1 
6753  C CE2 . TYR E 103 ? 2.479 2.394 2.032 0.470  0.192  -0.263 102 TYR EEE CE2 
6754  C CZ  . TYR E 103 ? 2.717 2.560 2.190 0.493  0.192  -0.263 102 TYR EEE CZ  
6755  O OH  . TYR E 103 ? 2.836 2.636 2.281 0.488  0.159  -0.272 102 TYR EEE OH  
6756  N N   . TRP E 104 ? 2.501 2.519 2.126 0.543  0.343  -0.188 103 TRP EEE N   
6757  C CA  . TRP E 104 ? 2.651 2.686 2.303 0.550  0.359  -0.173 103 TRP EEE CA  
6758  C C   . TRP E 104 ? 2.837 2.806 2.423 0.571  0.373  -0.170 103 TRP EEE C   
6759  O O   . TRP E 104 ? 2.764 2.671 2.282 0.590  0.381  -0.172 103 TRP EEE O   
6760  C CB  . TRP E 104 ? 2.640 2.716 2.351 0.565  0.382  -0.149 103 TRP EEE CB  
6761  C CG  . TRP E 104 ? 2.418 2.556 2.194 0.545  0.366  -0.150 103 TRP EEE CG  
6762  C CD1 . TRP E 104 ? 2.364 2.518 2.151 0.539  0.360  -0.155 103 TRP EEE CD1 
6763  C CD2 . TRP E 104 ? 2.384 2.568 2.219 0.531  0.354  -0.143 103 TRP EEE CD2 
6764  N NE1 . TRP E 104 ? 2.298 2.505 2.145 0.522  0.346  -0.152 103 TRP EEE NE1 
6765  C CE2 . TRP E 104 ? 2.354 2.576 2.227 0.517  0.341  -0.145 103 TRP EEE CE2 
6766  C CE3 . TRP E 104 ? 2.413 2.601 2.265 0.529  0.351  -0.135 103 TRP EEE CE3 
6767  C CZ2 . TRP E 104 ? 2.345 2.604 2.267 0.502  0.323  -0.140 103 TRP EEE CZ2 
6768  C CZ3 . TRP E 104 ? 2.465 2.690 2.366 0.514  0.332  -0.130 103 TRP EEE CZ3 
6769  C CH2 . TRP E 104 ? 2.328 2.585 2.260 0.501  0.318  -0.133 103 TRP EEE CH2 
6770  N N   . GLY E 105 ? 3.017 2.993 2.616 0.569  0.374  -0.165 104 GLY EEE N   
6771  C CA  . GLY E 105 ? 3.063 2.984 2.612 0.593  0.393  -0.157 104 GLY EEE CA  
6772  C C   . GLY E 105 ? 3.181 3.110 2.758 0.624  0.432  -0.129 104 GLY EEE C   
6773  O O   . GLY E 105 ? 3.062 3.041 2.704 0.625  0.442  -0.115 104 GLY EEE O   
6774  N N   . GLN E 106 ? 3.459 3.334 2.989 0.650  0.456  -0.120 105 GLN EEE N   
6775  C CA  . GLN E 106 ? 3.610 3.486 3.170 0.683  0.500  -0.089 105 GLN EEE CA  
6776  C C   . GLN E 106 ? 3.565 3.498 3.212 0.679  0.501  -0.071 105 GLN EEE C   
6777  O O   . GLN E 106 ? 3.659 3.615 3.367 0.700  0.531  -0.041 105 GLN EEE O   
6778  C CB  . GLN E 106 ? 3.804 3.588 3.268 0.718  0.529  -0.085 105 GLN EEE CB  
6779  C CG  . GLN E 106 ? 3.898 3.610 3.269 0.732  0.536  -0.095 105 GLN EEE CG  
6780  C CD  . GLN E 106 ? 3.953 3.615 3.246 0.709  0.490  -0.128 105 GLN EEE CD  
6781  O OE1 . GLN E 106 ? 3.901 3.580 3.207 0.685  0.460  -0.141 105 GLN EEE OE1 
6782  N NE2 . GLN E 106 ? 4.072 3.672 3.289 0.716  0.483  -0.139 105 GLN EEE NE2 
6783  N N   . GLY E 107 ? 3.425 3.375 3.080 0.653  0.468  -0.085 106 GLY EEE N   
6784  C CA  . GLY E 107 ? 3.338 3.336 3.068 0.645  0.460  -0.070 106 GLY EEE CA  
6785  C C   . GLY E 107 ? 3.327 3.288 3.030 0.660  0.470  -0.064 106 GLY EEE C   
6786  O O   . GLY E 107 ? 3.349 3.249 2.985 0.685  0.495  -0.063 106 GLY EEE O   
6787  N N   . THR E 108 ? 3.252 3.244 3.001 0.644  0.448  -0.061 107 THR EEE N   
6788  C CA  . THR E 108 ? 3.233 3.200 2.973 0.656  0.454  -0.052 107 THR EEE CA  
6789  C C   . THR E 108 ? 3.227 3.242 3.064 0.657  0.448  -0.025 107 THR EEE C   
6790  O O   . THR E 108 ? 3.117 3.176 3.005 0.633  0.418  -0.027 107 THR EEE O   
6791  C CB  . THR E 108 ? 3.207 3.145 2.885 0.633  0.427  -0.078 107 THR EEE CB  
6792  O OG1 . THR E 108 ? 3.331 3.238 2.993 0.648  0.435  -0.069 107 THR EEE OG1 
6793  C CG2 . THR E 108 ? 3.066 3.045 2.777 0.598  0.390  -0.090 107 THR EEE CG2 
6794  N N   . GLN E 109 ? 3.335 3.336 3.196 0.685  0.475  -0.001 108 GLN EEE N   
6795  C CA  . GLN E 109 ? 3.324 3.369 3.290 0.689  0.468  0.030  108 GLN EEE CA  
6796  C C   . GLN E 109 ? 3.375 3.418 3.340 0.668  0.430  0.021  108 GLN EEE C   
6797  O O   . GLN E 109 ? 3.471 3.470 3.367 0.671  0.432  0.008  108 GLN EEE O   
6798  C CB  . GLN E 109 ? 3.264 3.295 3.267 0.730  0.517  0.064  108 GLN EEE CB  
6799  C CG  . GLN E 109 ? 3.250 3.322 3.369 0.735  0.507  0.099  108 GLN EEE CG  
6800  C CD  . GLN E 109 ? 3.139 3.271 3.371 0.730  0.499  0.125  108 GLN EEE CD  
6801  O OE1 . GLN E 109 ? 3.105 3.245 3.359 0.750  0.537  0.140  108 GLN EEE OE1 
6802  N NE2 . GLN E 109 ? 3.141 3.309 3.438 0.703  0.448  0.129  108 GLN EEE NE2 
6803  N N   . VAL E 110 ? 3.321 3.404 3.354 0.647  0.393  0.029  109 VAL EEE N   
6804  C CA  . VAL E 110 ? 3.413 3.488 3.445 0.629  0.355  0.025  109 VAL EEE CA  
6805  C C   . VAL E 110 ? 3.452 3.556 3.592 0.637  0.340  0.061  109 VAL EEE C   
6806  O O   . VAL E 110 ? 3.291 3.434 3.510 0.633  0.327  0.079  109 VAL EEE O   
6807  C CB  . VAL E 110 ? 3.410 3.487 3.404 0.594  0.315  -0.002 109 VAL EEE CB  
6808  C CG1 . VAL E 110 ? 3.381 3.445 3.380 0.578  0.275  -0.001 109 VAL EEE CG1 
6809  C CG2 . VAL E 110 ? 3.470 3.517 3.368 0.584  0.326  -0.035 109 VAL EEE CG2 
6810  N N   . THR E 111 ? 3.686 3.770 3.834 0.649  0.340  0.073  110 THR EEE N   
6811  C CA  . THR E 111 ? 3.685 3.790 3.941 0.661  0.328  0.111  110 THR EEE CA  
6812  C C   . THR E 111 ? 3.778 3.857 4.013 0.645  0.284  0.105  110 THR EEE C   
6813  O O   . THR E 111 ? 3.841 3.881 3.998 0.648  0.294  0.087  110 THR EEE O   
6814  C CB  . THR E 111 ? 3.599 3.702 3.895 0.702  0.384  0.140  110 THR EEE CB  
6815  O OG1 . THR E 111 ? 3.616 3.719 3.882 0.718  0.430  0.137  110 THR EEE OG1 
6816  C CG2 . THR E 111 ? 3.517 3.661 3.959 0.715  0.377  0.187  110 THR EEE CG2 
6817  N N   . VAL E 112 ? 3.920 4.013 4.214 0.626  0.233  0.116  111 VAL EEE N   
6818  C CA  . VAL E 112 ? 3.862 3.919 4.130 0.613  0.189  0.112  111 VAL EEE CA  
6819  C C   . VAL E 112 ? 3.829 3.902 4.214 0.627  0.169  0.153  111 VAL EEE C   
6820  O O   . VAL E 112 ? 3.856 3.907 4.242 0.641  0.176  0.163  111 VAL EEE O   
6821  C CB  . VAL E 112 ? 3.807 3.843 4.021 0.580  0.138  0.088  111 VAL EEE CB  
6822  C CG1 . VAL E 112 ? 3.805 3.806 4.028 0.569  0.084  0.098  111 VAL EEE CG1 
6823  C CG2 . VAL E 112 ? 3.769 3.776 3.859 0.566  0.156  0.048  111 VAL EEE CG2 
6824  N N   . VAL F 1   ? 3.073 4.123 4.844 -0.114 0.628  -0.624 2   VAL DDD N   
6825  C CA  . VAL F 1   ? 3.015 4.052 4.810 -0.094 0.607  -0.603 2   VAL DDD CA  
6826  C C   . VAL F 1   ? 3.119 4.187 4.901 -0.106 0.613  -0.594 2   VAL DDD C   
6827  O O   . VAL F 1   ? 3.485 4.553 5.210 -0.127 0.617  -0.575 2   VAL DDD O   
6828  C CB  . VAL F 1   ? 2.739 3.729 4.503 -0.085 0.583  -0.563 2   VAL DDD CB  
6829  C CG1 . VAL F 1   ? 2.732 3.710 4.520 -0.065 0.561  -0.541 2   VAL DDD CG1 
6830  C CG2 . VAL F 1   ? 2.547 3.504 4.322 -0.076 0.575  -0.571 2   VAL DDD CG2 
6831  N N   . GLN F 2   ? 2.984 4.077 4.818 -0.094 0.612  -0.609 3   GLN DDD N   
6832  C CA  . GLN F 2   ? 2.725 3.851 4.555 -0.106 0.618  -0.606 3   GLN DDD CA  
6833  C C   . GLN F 2   ? 2.654 3.763 4.506 -0.085 0.594  -0.581 3   GLN DDD C   
6834  O O   . GLN F 2   ? 2.733 3.810 4.614 -0.059 0.575  -0.573 3   GLN DDD O   
6835  C CB  . GLN F 2   ? 2.622 3.807 4.493 -0.116 0.642  -0.651 3   GLN DDD CB  
6836  C CG  . GLN F 2   ? 2.533 3.740 4.375 -0.143 0.667  -0.674 3   GLN DDD CG  
6837  C CD  . GLN F 2   ? 2.459 3.666 4.227 -0.177 0.673  -0.650 3   GLN DDD CD  
6838  O OE1 . GLN F 2   ? 2.492 3.709 4.243 -0.189 0.669  -0.633 3   GLN DDD OE1 
6839  N NE2 . GLN F 2   ? 2.399 3.590 4.121 -0.193 0.681  -0.647 3   GLN DDD NE2 
6840  N N   . LEU F 3   ? 2.561 3.688 4.395 -0.098 0.594  -0.567 4   LEU DDD N   
6841  C CA  . LEU F 3   ? 2.512 3.628 4.363 -0.082 0.574  -0.544 4   LEU DDD CA  
6842  C C   . LEU F 3   ? 2.632 3.800 4.518 -0.090 0.585  -0.565 4   LEU DDD C   
6843  O O   . LEU F 3   ? 2.734 3.940 4.601 -0.118 0.606  -0.583 4   LEU DDD O   
6844  C CB  . LEU F 3   ? 2.425 3.511 4.212 -0.092 0.561  -0.502 4   LEU DDD CB  
6845  C CG  . LEU F 3   ? 2.543 3.582 4.295 -0.082 0.546  -0.477 4   LEU DDD CG  
6846  C CD1 . LEU F 3   ? 2.710 3.732 4.401 -0.092 0.535  -0.444 4   LEU DDD CD1 
6847  C CD2 . LEU F 3   ? 2.564 3.575 4.356 -0.053 0.524  -0.467 4   LEU DDD CD2 
6848  N N   . GLN F 4   ? 2.625 3.796 4.562 -0.066 0.570  -0.565 5   GLN DDD N   
6849  C CA  . GLN F 4   ? 2.694 3.917 4.666 -0.072 0.578  -0.583 5   GLN DDD CA  
6850  C C   . GLN F 4   ? 2.738 3.945 4.727 -0.055 0.554  -0.557 5   GLN DDD C   
6851  O O   . GLN F 4   ? 2.725 3.903 4.750 -0.024 0.535  -0.550 5   GLN DDD O   
6852  C CB  . GLN F 4   ? 2.664 3.933 4.706 -0.059 0.591  -0.633 5   GLN DDD CB  
6853  C CG  . GLN F 4   ? 2.716 4.051 4.795 -0.068 0.602  -0.656 5   GLN DDD CG  
6854  C CD  . GLN F 4   ? 2.697 4.058 4.717 -0.112 0.620  -0.648 5   GLN DDD CD  
6855  O OE1 . GLN F 4   ? 2.731 4.090 4.725 -0.125 0.611  -0.622 5   GLN DDD OE1 
6856  N NE2 . GLN F 4   ? 2.654 4.036 4.648 -0.137 0.643  -0.668 5   GLN DDD NE2 
6857  N N   . GLU F 5   ? 2.800 4.023 4.761 -0.075 0.555  -0.540 6   GLU DDD N   
6858  C CA  . GLU F 5   ? 2.881 4.095 4.862 -0.060 0.534  -0.519 6   GLU DDD CA  
6859  C C   . GLU F 5   ? 2.881 4.152 4.940 -0.048 0.540  -0.554 6   GLU DDD C   
6860  O O   . GLU F 5   ? 2.864 4.189 4.948 -0.059 0.562  -0.593 6   GLU DDD O   
6861  C CB  . GLU F 5   ? 3.003 4.210 4.922 -0.087 0.532  -0.489 6   GLU DDD CB  
6862  C CG  . GLU F 5   ? 3.150 4.367 5.087 -0.083 0.518  -0.475 6   GLU DDD CG  
6863  C CD  . GLU F 5   ? 3.211 4.375 5.141 -0.058 0.490  -0.439 6   GLU DDD CD  
6864  O OE1 . GLU F 5   ? 3.294 4.412 5.166 -0.062 0.480  -0.409 6   GLU DDD OE1 
6865  O OE2 . GLU F 5   ? 3.176 4.347 5.160 -0.036 0.476  -0.440 6   GLU DDD OE2 
6866  N N   . SER F 6   ? 2.891 4.151 4.987 -0.023 0.518  -0.542 7   SER DDD N   
6867  C CA  . SER F 6   ? 2.729 4.043 4.900 -0.008 0.519  -0.573 7   SER DDD CA  
6868  C C   . SER F 6   ? 2.642 3.935 4.836 0.013  0.492  -0.547 7   SER DDD C   
6869  O O   . SER F 6   ? 2.708 3.947 4.858 0.014  0.474  -0.506 7   SER DDD O   
6870  C CB  . SER F 6   ? 2.678 4.004 4.910 0.019  0.522  -0.613 7   SER DDD CB  
6871  O OG  . SER F 6   ? 2.755 4.016 4.994 0.049  0.497  -0.594 7   SER DDD OG  
6872  N N   . GLY F 7   ? 2.592 3.937 4.850 0.025  0.491  -0.573 8   GLY DDD N   
6873  C CA  . GLY F 7   ? 2.552 3.884 4.838 0.045  0.465  -0.552 8   GLY DDD CA  
6874  C C   . GLY F 7   ? 2.636 3.991 4.902 0.024  0.464  -0.532 8   GLY DDD C   
6875  O O   . GLY F 7   ? 2.573 3.915 4.864 0.042  0.442  -0.515 8   GLY DDD O   
6876  N N   . GLY F 8   ? 2.711 4.096 4.932 -0.014 0.485  -0.533 9   GLY DDD N   
6877  C CA  . GLY F 8   ? 2.821 4.224 5.017 -0.037 0.482  -0.514 9   GLY DDD CA  
6878  C C   . GLY F 8   ? 2.867 4.353 5.120 -0.044 0.492  -0.547 9   GLY DDD C   
6879  O O   . GLY F 8   ? 2.850 4.396 5.156 -0.038 0.508  -0.592 9   GLY DDD O   
6880  N N   . GLY F 9   ? 3.102 4.593 5.342 -0.056 0.482  -0.524 10  GLY DDD N   
6881  C CA  . GLY F 9   ? 3.458 5.031 5.747 -0.065 0.490  -0.551 10  GLY DDD CA  
6882  C C   . GLY F 9   ? 3.711 5.272 5.976 -0.077 0.473  -0.517 10  GLY DDD C   
6883  O O   . GLY F 9   ? 4.096 5.590 6.293 -0.088 0.461  -0.474 10  GLY DDD O   
6884  N N   . LEU F 10  ? 3.473 5.101 5.797 -0.074 0.473  -0.538 11  LEU DDD N   
6885  C CA  . LEU F 10  ? 3.277 4.913 5.585 -0.091 0.461  -0.514 11  LEU DDD CA  
6886  C C   . LEU F 10  ? 3.406 5.028 5.772 -0.050 0.433  -0.504 11  LEU DDD C   
6887  O O   . LEU F 10  ? 3.374 5.037 5.820 -0.017 0.430  -0.537 11  LEU DDD O   
6888  C CB  . LEU F 10  ? 2.866 4.600 5.190 -0.127 0.483  -0.547 11  LEU DDD CB  
6889  C CG  . LEU F 10  ? 2.704 4.436 4.940 -0.185 0.499  -0.532 11  LEU DDD CG  
6890  C CD1 . LEU F 10  ? 2.780 4.431 4.943 -0.196 0.477  -0.477 11  LEU DDD CD1 
6891  C CD2 . LEU F 10  ? 2.695 4.410 4.895 -0.197 0.518  -0.543 11  LEU DDD CD2 
6892  N N   . VAL F 11  ? 3.590 5.153 5.914 -0.052 0.412  -0.458 12  VAL DDD N   
6893  C CA  . VAL F 11  ? 3.564 5.105 5.932 -0.017 0.384  -0.443 12  VAL DDD CA  
6894  C C   . VAL F 11  ? 3.529 5.062 5.859 -0.041 0.373  -0.410 12  VAL DDD C   
6895  O O   . VAL F 11  ? 3.694 5.206 5.947 -0.078 0.380  -0.388 12  VAL DDD O   
6896  C CB  . VAL F 11  ? 3.562 5.017 5.921 0.017  0.362  -0.417 12  VAL DDD CB  
6897  C CG1 . VAL F 11  ? 3.540 4.997 5.934 0.040  0.371  -0.448 12  VAL DDD CG1 
6898  C CG2 . VAL F 11  ? 3.552 4.937 5.818 -0.004 0.359  -0.374 12  VAL DDD CG2 
6899  N N   . GLN F 12  ? 3.260 4.808 5.641 -0.019 0.353  -0.406 13  GLN DDD N   
6900  C CA  . GLN F 12  ? 3.095 4.629 5.444 -0.036 0.338  -0.373 13  GLN DDD CA  
6901  C C   . GLN F 12  ? 3.105 4.543 5.404 -0.023 0.314  -0.325 13  GLN DDD C   
6902  O O   . GLN F 12  ? 3.168 4.557 5.473 0.006  0.304  -0.318 13  GLN DDD O   
6903  C CB  . GLN F 12  ? 2.925 4.518 5.351 -0.018 0.327  -0.390 13  GLN DDD CB  
6904  C CG  . GLN F 12  ? 2.821 4.434 5.223 -0.048 0.321  -0.369 13  GLN DDD CG  
6905  C CD  . GLN F 12  ? 2.780 4.348 5.196 -0.022 0.290  -0.337 13  GLN DDD CD  
6906  O OE1 . GLN F 12  ? 2.793 4.348 5.267 0.020  0.273  -0.344 13  GLN DDD OE1 
6907  N NE2 . GLN F 12  ? 2.737 4.282 5.102 -0.047 0.280  -0.304 13  GLN DDD NE2 
6908  N N   . ALA F 13  ? 3.016 4.432 5.262 -0.047 0.305  -0.293 14  ALA DDD N   
6909  C CA  . ALA F 13  ? 2.958 4.293 5.159 -0.035 0.281  -0.249 14  ALA DDD CA  
6910  C C   . ALA F 13  ? 2.974 4.296 5.238 0.006  0.257  -0.244 14  ALA DDD C   
6911  O O   . ALA F 13  ? 2.919 4.293 5.252 0.019  0.252  -0.264 14  ALA DDD O   
6912  C CB  . ALA F 13  ? 2.824 4.147 4.968 -0.067 0.274  -0.222 14  ALA DDD CB  
6913  N N   . GLY F 14  ? 3.009 4.260 5.247 0.025  0.240  -0.217 15  GLY DDD N   
6914  C CA  . GLY F 14  ? 2.976 4.201 5.261 0.060  0.215  -0.208 15  GLY DDD CA  
6915  C C   . GLY F 14  ? 2.997 4.234 5.343 0.090  0.216  -0.237 15  GLY DDD C   
6916  O O   . GLY F 14  ? 2.978 4.186 5.359 0.119  0.193  -0.229 15  GLY DDD O   
6917  N N   . GLY F 15  ? 3.051 4.327 5.408 0.082  0.241  -0.271 16  GLY DDD N   
6918  C CA  . GLY F 15  ? 3.014 4.303 5.427 0.109  0.244  -0.303 16  GLY DDD CA  
6919  C C   . GLY F 15  ? 2.955 4.180 5.332 0.118  0.241  -0.290 16  GLY DDD C   
6920  O O   . GLY F 15  ? 2.952 4.123 5.266 0.108  0.234  -0.255 16  GLY DDD O   
6921  N N   . SER F 16  ? 2.925 4.155 5.345 0.139  0.244  -0.319 17  SER DDD N   
6922  C CA  . SER F 16  ? 2.815 3.989 5.204 0.147  0.242  -0.310 17  SER DDD CA  
6923  C C   . SER F 16  ? 2.705 3.915 5.107 0.143  0.269  -0.350 17  SER DDD C   
6924  O O   . SER F 16  ? 2.580 3.853 5.035 0.146  0.281  -0.388 17  SER DDD O   
6925  C CB  . SER F 16  ? 2.768 3.894 5.190 0.179  0.211  -0.300 17  SER DDD CB  
6926  O OG  . SER F 16  ? 2.796 3.880 5.189 0.178  0.188  -0.259 17  SER DDD OG  
6927  N N   . LEU F 17  ? 2.708 3.879 5.063 0.135  0.278  -0.342 18  LEU DDD N   
6928  C CA  . LEU F 17  ? 2.679 3.877 5.039 0.129  0.303  -0.376 18  LEU DDD CA  
6929  C C   . LEU F 17  ? 2.841 3.979 5.162 0.133  0.301  -0.364 18  LEU DDD C   
6930  O O   . LEU F 17  ? 2.952 4.038 5.228 0.131  0.286  -0.326 18  LEU DDD O   
6931  C CB  . LEU F 17  ? 2.534 3.778 4.857 0.093  0.332  -0.386 18  LEU DDD CB  
6932  C CG  . LEU F 17  ? 2.360 3.650 4.704 0.087  0.359  -0.429 18  LEU DDD CG  
6933  C CD1 . LEU F 17  ? 2.263 3.609 4.695 0.112  0.356  -0.470 18  LEU DDD CD1 
6934  C CD2 . LEU F 17  ? 2.346 3.676 4.644 0.046  0.386  -0.435 18  LEU DDD CD2 
6935  N N   . ARG F 18  ? 2.760 3.910 5.104 0.141  0.314  -0.396 19  ARG DDD N   
6936  C CA  . ARG F 18  ? 2.673 3.774 4.983 0.143  0.314  -0.388 19  ARG DDD CA  
6937  C C   . ARG F 18  ? 2.673 3.803 4.961 0.123  0.345  -0.414 19  ARG DDD C   
6938  O O   . ARG F 18  ? 2.658 3.836 4.991 0.127  0.360  -0.455 19  ARG DDD O   
6939  C CB  . ARG F 18  ? 2.610 3.679 4.966 0.174  0.292  -0.400 19  ARG DDD CB  
6940  C CG  . ARG F 18  ? 2.530 3.555 4.850 0.171  0.296  -0.396 19  ARG DDD CG  
6941  C CD  . ARG F 18  ? 2.423 3.436 4.793 0.196  0.286  -0.426 19  ARG DDD CD  
6942  N NE  . ARG F 18  ? 2.435 3.433 4.857 0.224  0.255  -0.425 19  ARG DDD NE  
6943  C CZ  . ARG F 18  ? 2.449 3.383 4.866 0.238  0.224  -0.403 19  ARG DDD CZ  
6944  N NH1 . ARG F 18  ? 2.397 3.281 4.763 0.226  0.221  -0.381 19  ARG DDD NH1 
6945  N NH2 . ARG F 18  ? 2.498 3.420 4.961 0.262  0.194  -0.402 19  ARG DDD NH2 
6946  N N   . LEU F 19  ? 2.737 3.842 4.954 0.100  0.355  -0.391 20  LEU DDD N   
6947  C CA  . LEU F 19  ? 2.835 3.961 5.025 0.080  0.383  -0.412 20  LEU DDD CA  
6948  C C   . LEU F 19  ? 2.983 4.075 5.170 0.091  0.383  -0.420 20  LEU DDD C   
6949  O O   . LEU F 19  ? 3.190 4.229 5.361 0.103  0.362  -0.395 20  LEU DDD O   
6950  C CB  . LEU F 19  ? 2.821 3.935 4.934 0.050  0.391  -0.384 20  LEU DDD CB  
6951  C CG  . LEU F 19  ? 2.741 3.895 4.836 0.024  0.402  -0.384 20  LEU DDD CG  
6952  C CD1 . LEU F 19  ? 2.851 3.972 4.861 0.000  0.403  -0.353 20  LEU DDD CD1 
6953  C CD2 . LEU F 19  ? 2.594 3.812 4.713 0.007  0.429  -0.424 20  LEU DDD CD2 
6954  N N   . SER F 20  ? 2.949 4.073 5.149 0.084  0.406  -0.456 21  SER DDD N   
6955  C CA  . SER F 20  ? 2.967 4.063 5.165 0.092  0.409  -0.469 21  SER DDD CA  
6956  C C   . SER F 20  ? 3.003 4.120 5.163 0.067  0.438  -0.486 21  SER DDD C   
6957  O O   . SER F 20  ? 3.181 4.353 5.355 0.052  0.460  -0.515 21  SER DDD O   
6958  C CB  . SER F 20  ? 2.921 4.025 5.192 0.122  0.399  -0.503 21  SER DDD CB  
6959  O OG  . SER F 20  ? 2.816 3.876 5.106 0.145  0.366  -0.479 21  SER DDD OG  
6960  N N   . CYS F 21  ? 2.962 4.038 5.079 0.062  0.437  -0.472 22  CYS DDD N   
6961  C CA  . CYS F 21  ? 2.848 3.931 4.920 0.039  0.461  -0.481 22  CYS DDD CA  
6962  C C   . CYS F 21  ? 2.701 3.771 4.787 0.047  0.466  -0.505 22  CYS DDD C   
6963  O O   . CYS F 21  ? 2.745 3.766 4.821 0.059  0.449  -0.488 22  CYS DDD O   
6964  C CB  . CYS F 21  ? 2.994 4.042 4.991 0.023  0.456  -0.442 22  CYS DDD CB  
6965  S SG  . CYS F 21  ? 3.299 4.357 5.264 0.008  0.451  -0.416 22  CYS DDD SG  
6966  N N   . ALA F 22  ? 2.657 3.770 4.764 0.039  0.490  -0.544 23  ALA DDD N   
6967  C CA  . ALA F 22  ? 2.577 3.679 4.697 0.046  0.496  -0.570 23  ALA DDD CA  
6968  C C   . ALA F 22  ? 2.560 3.649 4.617 0.021  0.512  -0.561 23  ALA DDD C   
6969  O O   . ALA F 22  ? 2.553 3.667 4.569 -0.006 0.530  -0.558 23  ALA DDD O   
6970  C CB  . ALA F 22  ? 2.472 3.629 4.655 0.055  0.512  -0.621 23  ALA DDD CB  
6971  N N   . ALA F 23  ? 2.652 3.696 4.701 0.031  0.502  -0.556 24  ALA DDD N   
6972  C CA  . ALA F 23  ? 2.770 3.791 4.766 0.015  0.510  -0.547 24  ALA DDD CA  
6973  C C   . ALA F 23  ? 3.048 4.066 5.070 0.021  0.518  -0.582 24  ALA DDD C   
6974  O O   . ALA F 23  ? 3.011 4.016 5.084 0.046  0.504  -0.601 24  ALA DDD O   
6975  C CB  . ALA F 23  ? 2.788 3.755 4.747 0.019  0.486  -0.505 24  ALA DDD CB  
6976  N N   . SER F 24  ? 3.333 4.359 5.317 -0.000 0.539  -0.592 25  SER DDD N   
6977  C CA  . SER F 24  ? 3.379 4.394 5.381 0.005  0.544  -0.621 25  SER DDD CA  
6978  C C   . SER F 24  ? 3.406 4.359 5.386 0.013  0.521  -0.595 25  SER DDD C   
6979  O O   . SER F 24  ? 3.328 4.258 5.264 0.006  0.509  -0.556 25  SER DDD O   
6980  C CB  . SER F 24  ? 3.345 4.390 5.314 -0.022 0.573  -0.640 25  SER DDD CB  
6981  O OG  . SER F 24  ? 3.347 4.366 5.314 -0.019 0.574  -0.656 25  SER DDD OG  
6982  N N   . GLY F 25  ? 3.345 4.273 5.352 0.027  0.513  -0.618 26  GLY DDD N   
6983  C CA  . GLY F 25  ? 3.474 4.342 5.463 0.033  0.488  -0.595 26  GLY DDD CA  
6984  C C   . GLY F 25  ? 3.606 4.446 5.616 0.053  0.458  -0.569 26  GLY DDD C   
6985  O O   . GLY F 25  ? 3.510 4.374 5.560 0.067  0.456  -0.577 26  GLY DDD O   
6986  N N   . SER F 26  ? 3.935 4.725 5.914 0.050  0.436  -0.537 27  SER DDD N   
6987  C CA  . SER F 26  ? 4.315 5.073 6.304 0.064  0.406  -0.508 27  SER DDD CA  
6988  C C   . SER F 26  ? 4.506 5.278 6.455 0.051  0.406  -0.469 27  SER DDD C   
6989  O O   . SER F 26  ? 4.887 5.666 6.785 0.031  0.417  -0.454 27  SER DDD O   
6990  C CB  . SER F 26  ? 4.467 5.162 6.443 0.065  0.379  -0.495 27  SER DDD CB  
6991  O OG  . SER F 26  ? 4.632 5.296 6.614 0.076  0.349  -0.466 27  SER DDD OG  
6992  N N   . ILE F 27  ? 4.339 5.117 6.312 0.064  0.392  -0.456 28  ILE DDD N   
6993  C CA  . ILE F 27  ? 3.834 4.625 5.772 0.055  0.392  -0.422 28  ILE DDD CA  
6994  C C   . ILE F 27  ? 3.623 4.377 5.521 0.048  0.370  -0.385 28  ILE DDD C   
6995  O O   . ILE F 27  ? 3.551 4.316 5.406 0.037  0.372  -0.360 28  ILE DDD O   
6996  C CB  . ILE F 27  ? 3.659 4.471 5.634 0.069  0.386  -0.421 28  ILE DDD CB  
6997  C CG1 . ILE F 27  ? 3.394 4.232 5.331 0.056  0.395  -0.398 28  ILE DDD CG1 
6998  C CG2 . ILE F 27  ? 3.598 4.372 5.600 0.087  0.353  -0.404 28  ILE DDD CG2 
6999  C CD1 . ILE F 27  ? 3.347 4.221 5.256 0.038  0.424  -0.413 28  ILE DDD CD1 
7000  N N   . SER F 28  ? 3.489 4.198 5.398 0.054  0.347  -0.382 29  SER DDD N   
7001  C CA  . SER F 28  ? 3.309 3.985 5.179 0.044  0.326  -0.349 29  SER DDD CA  
7002  C C   . SER F 28  ? 3.258 3.942 5.074 0.021  0.339  -0.342 29  SER DDD C   
7003  O O   . SER F 28  ? 3.078 3.750 4.857 0.009  0.326  -0.314 29  SER DDD O   
7004  C CB  . SER F 28  ? 3.145 3.767 5.037 0.052  0.297  -0.349 29  SER DDD CB  
7005  O OG  . SER F 28  ? 3.241 3.847 5.144 0.052  0.303  -0.378 29  SER DDD OG  
7006  N N   . ARG F 29  ? 3.340 4.049 5.152 0.015  0.366  -0.367 30  ARG DDD N   
7007  C CA  . ARG F 29  ? 3.264 3.983 5.027 -0.006 0.379  -0.363 30  ARG DDD CA  
7008  C C   . ARG F 29  ? 3.160 3.914 4.883 -0.014 0.389  -0.344 30  ARG DDD C   
7009  O O   . ARG F 29  ? 2.983 3.743 4.660 -0.028 0.391  -0.331 30  ARG DDD O   
7010  C CB  . ARG F 29  ? 3.409 4.143 5.185 -0.009 0.404  -0.399 30  ARG DDD CB  
7011  C CG  . ARG F 29  ? 3.563 4.267 5.382 0.003  0.396  -0.427 30  ARG DDD CG  
7012  C CD  . ARG F 29  ? 3.561 4.287 5.386 -0.003 0.423  -0.463 30  ARG DDD CD  
7013  N NE  . ARG F 29  ? 3.519 4.295 5.345 -0.005 0.446  -0.470 30  ARG DDD NE  
7014  C CZ  . ARG F 29  ? 3.406 4.215 5.232 -0.014 0.473  -0.498 30  ARG DDD CZ  
7015  N NH1 . ARG F 29  ? 3.309 4.109 5.138 -0.019 0.482  -0.524 30  ARG DDD NH1 
7016  N NH2 . ARG F 29  ? 3.254 4.104 5.075 -0.020 0.490  -0.500 30  ARG DDD NH2 
7017  N N   . PHE F 30  ? 3.295 4.068 5.035 -0.003 0.392  -0.342 31  PHE DDD N   
7018  C CA  . PHE F 30  ? 3.272 4.071 4.976 -0.007 0.397  -0.325 31  PHE DDD CA  
7019  C C   . PHE F 30  ? 3.211 3.999 4.890 -0.007 0.375  -0.291 31  PHE DDD C   
7020  O O   . PHE F 30  ? 3.152 3.916 4.853 0.000  0.354  -0.280 31  PHE DDD O   
7021  C CB  . PHE F 30  ? 3.330 4.151 5.060 0.001  0.406  -0.334 31  PHE DDD CB  
7022  C CG  . PHE F 30  ? 3.376 4.218 5.126 -0.004 0.430  -0.368 31  PHE DDD CG  
7023  C CD1 . PHE F 30  ? 3.545 4.381 5.347 0.005  0.432  -0.395 31  PHE DDD CD1 
7024  C CD2 . PHE F 30  ? 3.386 4.253 5.101 -0.019 0.450  -0.374 31  PHE DDD CD2 
7025  C CE1 . PHE F 30  ? 3.626 4.488 5.446 0.000  0.455  -0.428 31  PHE DDD CE1 
7026  C CE2 . PHE F 30  ? 3.484 4.373 5.213 -0.028 0.473  -0.405 31  PHE DDD CE2 
7027  C CZ  . PHE F 30  ? 3.553 4.443 5.336 -0.018 0.477  -0.433 31  PHE DDD CZ  
7028  N N   . ASN F 31  ? 2.963 3.770 4.594 -0.014 0.378  -0.277 32  ASN DDD N   
7029  C CA  . ASN F 31  ? 2.654 3.460 4.256 -0.014 0.359  -0.249 32  ASN DDD CA  
7030  C C   . ASN F 31  ? 2.553 3.364 4.161 -0.002 0.348  -0.233 32  ASN DDD C   
7031  O O   . ASN F 31  ? 2.393 3.200 3.988 0.001  0.330  -0.211 32  ASN DDD O   
7032  C CB  . ASN F 31  ? 2.358 3.187 3.907 -0.024 0.365  -0.244 32  ASN DDD CB  
7033  C CG  . ASN F 31  ? 2.316 3.144 3.853 -0.039 0.374  -0.256 32  ASN DDD CG  
7034  O OD1 . ASN F 31  ? 2.569 3.373 4.134 -0.043 0.373  -0.267 32  ASN DDD OD1 
7035  N ND2 . ASN F 31  ? 2.063 2.915 3.557 -0.048 0.382  -0.256 32  ASN DDD ND2 
7036  N N   . ALA F 32  ? 2.652 3.471 4.277 0.005  0.359  -0.244 33  ALA DDD N   
7037  C CA  . ALA F 32  ? 2.761 3.582 4.391 0.015  0.349  -0.230 33  ALA DDD CA  
7038  C C   . ALA F 32  ? 2.988 3.817 4.650 0.017  0.363  -0.250 33  ALA DDD C   
7039  O O   . ALA F 32  ? 3.366 4.209 5.024 0.008  0.383  -0.270 33  ALA DDD O   
7040  C CB  . ALA F 32  ? 2.671 3.505 4.249 0.014  0.345  -0.214 33  ALA DDD CB  
7041  N N   . MET F 33  ? 2.899 3.725 4.594 0.027  0.354  -0.244 34  MET DDD N   
7042  C CA  . MET F 33  ? 2.756 3.598 4.479 0.028  0.366  -0.261 34  MET DDD CA  
7043  C C   . MET F 33  ? 2.516 3.359 4.236 0.034  0.354  -0.243 34  MET DDD C   
7044  O O   . MET F 33  ? 2.361 3.189 4.073 0.041  0.334  -0.219 34  MET DDD O   
7045  C CB  . MET F 33  ? 2.905 3.746 4.690 0.035  0.370  -0.286 34  MET DDD CB  
7046  C CG  . MET F 33  ? 3.090 3.921 4.883 0.032  0.377  -0.305 34  MET DDD CG  
7047  S SD  . MET F 33  ? 3.242 4.039 5.014 0.031  0.357  -0.284 34  MET DDD SD  
7048  C CE  . MET F 33  ? 3.165 3.933 4.990 0.048  0.331  -0.279 34  MET DDD CE  
7049  N N   . GLY F 34  ? 2.714 3.576 4.441 0.028  0.366  -0.253 35  GLY DDD N   
7050  C CA  . GLY F 34  ? 2.711 3.572 4.433 0.032  0.354  -0.237 35  GLY DDD CA  
7051  C C   . GLY F 34  ? 2.922 3.807 4.651 0.021  0.369  -0.252 35  GLY DDD C   
7052  O O   . GLY F 34  ? 3.036 3.942 4.783 0.012  0.389  -0.278 35  GLY DDD O   
7053  N N   . TRP F 35  ? 2.963 3.845 4.675 0.020  0.359  -0.234 36  TRP DDD N   
7054  C CA  . TRP F 35  ? 3.079 3.982 4.796 0.007  0.368  -0.243 36  TRP DDD CA  
7055  C C   . TRP F 35  ? 3.083 3.972 4.736 -0.005 0.361  -0.224 36  TRP DDD C   
7056  O O   . TRP F 35  ? 3.068 3.933 4.693 0.005  0.342  -0.200 36  TRP DDD O   
7057  C CB  . TRP F 35  ? 3.226 4.140 5.000 0.018  0.359  -0.244 36  TRP DDD CB  
7058  C CG  . TRP F 35  ? 3.493 4.427 5.334 0.028  0.366  -0.270 36  TRP DDD CG  
7059  C CD1 . TRP F 35  ? 3.610 4.529 5.492 0.048  0.353  -0.269 36  TRP DDD CD1 
7060  C CD2 . TRP F 35  ? 3.695 4.670 5.574 0.019  0.385  -0.301 36  TRP DDD CD2 
7061  N NE1 . TRP F 35  ? 3.764 4.707 5.705 0.055  0.361  -0.299 36  TRP DDD NE1 
7062  C CE2 . TRP F 35  ? 3.831 4.812 5.774 0.039  0.382  -0.321 36  TRP DDD CE2 
7063  C CE3 . TRP F 35  ? 3.801 4.808 5.663 -0.004 0.404  -0.316 36  TRP DDD CE3 
7064  C CZ2 . TRP F 35  ? 4.048 5.071 6.042 0.039  0.398  -0.357 36  TRP DDD CZ2 
7065  C CZ3 . TRP F 35  ? 4.018 5.071 5.931 -0.008 0.422  -0.351 36  TRP DDD CZ3 
7066  C CH2 . TRP F 35  ? 4.112 5.174 6.091 0.015  0.419  -0.373 36  TRP DDD CH2 
7067  N N   . TRP F 36  ? 2.936 3.840 4.564 -0.027 0.377  -0.237 37  TRP DDD N   
7068  C CA  . TRP F 36  ? 2.915 3.804 4.483 -0.043 0.370  -0.222 37  TRP DDD CA  
7069  C C   . TRP F 36  ? 3.060 3.977 4.645 -0.064 0.381  -0.235 37  TRP DDD C   
7070  O O   . TRP F 36  ? 3.209 4.164 4.848 -0.068 0.398  -0.260 37  TRP DDD O   
7071  C CB  . TRP F 36  ? 2.850 3.721 4.351 -0.056 0.373  -0.221 37  TRP DDD CB  
7072  C CG  . TRP F 36  ? 2.783 3.623 4.243 -0.039 0.356  -0.202 37  TRP DDD CG  
7073  C CD1 . TRP F 36  ? 2.784 3.623 4.262 -0.021 0.353  -0.201 37  TRP DDD CD1 
7074  C CD2 . TRP F 36  ? 2.703 3.512 4.092 -0.040 0.339  -0.184 37  TRP DDD CD2 
7075  N NE1 . TRP F 36  ? 2.697 3.513 4.123 -0.010 0.336  -0.184 37  TRP DDD NE1 
7076  C CE2 . TRP F 36  ? 2.580 3.376 3.953 -0.020 0.326  -0.174 37  TRP DDD CE2 
7077  C CE3 . TRP F 36  ? 2.675 3.464 4.013 -0.057 0.331  -0.176 37  TRP DDD CE3 
7078  C CZ2 . TRP F 36  ? 2.378 3.146 3.688 -0.011 0.306  -0.159 37  TRP DDD CZ2 
7079  C CZ3 . TRP F 36  ? 2.525 3.278 3.797 -0.049 0.309  -0.159 37  TRP DDD CZ3 
7080  C CH2 . TRP F 36  ? 2.354 3.098 3.615 -0.024 0.297  -0.152 37  TRP DDD CH2 
7081  N N   . ARG F 37  ? 3.085 3.985 4.624 -0.078 0.370  -0.219 38  ARG DDD N   
7082  C CA  . ARG F 37  ? 3.016 3.942 4.556 -0.104 0.379  -0.228 38  ARG DDD CA  
7083  C C   . ARG F 37  ? 3.036 3.931 4.493 -0.129 0.371  -0.213 38  ARG DDD C   
7084  O O   . ARG F 37  ? 3.280 4.130 4.683 -0.119 0.351  -0.192 38  ARG DDD O   
7085  C CB  . ARG F 37  ? 2.922 3.861 4.509 -0.094 0.370  -0.221 38  ARG DDD CB  
7086  C CG  . ARG F 37  ? 2.741 3.638 4.290 -0.082 0.343  -0.190 38  ARG DDD CG  
7087  C CD  . ARG F 37  ? 2.601 3.513 4.199 -0.073 0.334  -0.184 38  ARG DDD CD  
7088  N NE  . ARG F 37  ? 2.454 3.328 4.015 -0.064 0.310  -0.154 38  ARG DDD NE  
7089  C CZ  . ARG F 37  ? 2.431 3.307 4.026 -0.051 0.297  -0.143 38  ARG DDD CZ  
7090  N NH1 . ARG F 37  ? 2.528 3.443 4.197 -0.044 0.304  -0.158 38  ARG DDD NH1 
7091  N NH2 . ARG F 37  ? 2.302 3.142 3.857 -0.044 0.275  -0.117 38  ARG DDD NH2 
7092  N N   . GLN F 38  ? 2.899 3.818 4.342 -0.163 0.385  -0.226 39  GLN DDD N   
7093  C CA  . GLN F 38  ? 2.762 3.648 4.123 -0.192 0.374  -0.211 39  GLN DDD CA  
7094  C C   . GLN F 38  ? 2.839 3.758 4.212 -0.221 0.381  -0.217 39  GLN DDD C   
7095  O O   . GLN F 38  ? 2.841 3.816 4.259 -0.239 0.404  -0.244 39  GLN DDD O   
7096  C CB  . GLN F 38  ? 2.614 3.489 3.921 -0.215 0.384  -0.220 39  GLN DDD CB  
7097  C CG  . GLN F 38  ? 2.546 3.372 3.758 -0.241 0.365  -0.200 39  GLN DDD CG  
7098  C CD  . GLN F 38  ? 2.418 3.229 3.574 -0.263 0.371  -0.207 39  GLN DDD CD  
7099  O OE1 . GLN F 38  ? 2.364 3.199 3.549 -0.255 0.389  -0.225 39  GLN DDD OE1 
7100  N NE2 . GLN F 38  ? 2.419 3.186 3.490 -0.291 0.355  -0.193 39  GLN DDD NE2 
7101  N N   . ALA F 39  ? 3.122 4.008 4.456 -0.228 0.359  -0.193 40  ALA DDD N   
7102  C CA  . ALA F 39  ? 3.099 4.002 4.425 -0.258 0.358  -0.191 40  ALA DDD CA  
7103  C C   . ALA F 39  ? 3.096 3.966 4.329 -0.300 0.351  -0.182 40  ALA DDD C   
7104  O O   . ALA F 39  ? 3.412 4.226 4.578 -0.298 0.336  -0.168 40  ALA DDD O   
7105  C CB  . ALA F 39  ? 3.054 3.933 4.389 -0.236 0.335  -0.168 40  ALA DDD CB  
7106  N N   . PRO F 40  ? 2.688 3.593 3.916 -0.341 0.361  -0.190 41  PRO DDD N   
7107  C CA  . PRO F 40  ? 2.645 3.515 3.779 -0.389 0.353  -0.180 41  PRO DDD CA  
7108  C C   . PRO F 40  ? 2.651 3.437 3.709 -0.379 0.317  -0.146 41  PRO DDD C   
7109  O O   . PRO F 40  ? 2.653 3.429 3.725 -0.367 0.302  -0.132 41  PRO DDD O   
7110  C CB  . PRO F 40  ? 2.602 3.534 3.759 -0.430 0.369  -0.194 41  PRO DDD CB  
7111  C CG  . PRO F 40  ? 2.554 3.566 3.820 -0.407 0.395  -0.224 41  PRO DDD CG  
7112  C CD  . PRO F 40  ? 2.564 3.548 3.873 -0.349 0.383  -0.214 41  PRO DDD CD  
7113  N N   . GLY F 41  ? 2.740 3.464 3.719 -0.383 0.301  -0.135 42  GLY DDD N   
7114  C CA  . GLY F 41  ? 2.606 3.248 3.510 -0.371 0.265  -0.106 42  GLY DDD CA  
7115  C C   . GLY F 41  ? 2.788 3.408 3.720 -0.314 0.252  -0.099 42  GLY DDD C   
7116  O O   . GLY F 41  ? 2.795 3.363 3.673 -0.297 0.234  -0.090 42  GLY DDD O   
7117  N N   . LYS F 42  ? 2.687 3.347 3.701 -0.284 0.261  -0.102 43  LYS DDD N   
7118  C CA  . LYS F 42  ? 2.705 3.346 3.742 -0.234 0.248  -0.094 43  LYS DDD CA  
7119  C C   . LYS F 42  ? 2.748 3.398 3.794 -0.219 0.260  -0.108 43  LYS DDD C   
7120  O O   . LYS F 42  ? 2.764 3.455 3.836 -0.238 0.286  -0.128 43  LYS DDD O   
7121  C CB  . LYS F 42  ? 2.622 3.304 3.745 -0.209 0.254  -0.096 43  LYS DDD CB  
7122  C CG  . LYS F 42  ? 2.526 3.196 3.639 -0.219 0.239  -0.080 43  LYS DDD CG  
7123  C CD  . LYS F 42  ? 2.453 3.047 3.485 -0.207 0.205  -0.056 43  LYS DDD CD  
7124  C CE  . LYS F 42  ? 2.405 2.972 3.405 -0.223 0.186  -0.038 43  LYS DDD CE  
7125  N NZ  . LYS F 42  ? 2.376 2.995 3.455 -0.218 0.197  -0.041 43  LYS DDD NZ  
7126  N N   . GLU F 43  ? 2.759 3.372 3.783 -0.184 0.241  -0.097 44  GLU DDD N   
7127  C CA  . GLU F 43  ? 2.786 3.403 3.812 -0.168 0.249  -0.107 44  GLU DDD CA  
7128  C C   . GLU F 43  ? 2.851 3.524 3.969 -0.148 0.273  -0.123 44  GLU DDD C   
7129  O O   . GLU F 43  ? 2.944 3.640 4.119 -0.133 0.274  -0.120 44  GLU DDD O   
7130  C CB  . GLU F 43  ? 2.707 3.272 3.679 -0.137 0.220  -0.092 44  GLU DDD CB  
7131  C CG  . GLU F 43  ? 2.695 3.196 3.572 -0.155 0.191  -0.077 44  GLU DDD CG  
7132  C CD  . GLU F 43  ? 2.793 3.272 3.609 -0.186 0.194  -0.083 44  GLU DDD CD  
7133  O OE1 . GLU F 43  ? 2.948 3.441 3.769 -0.177 0.204  -0.095 44  GLU DDD OE1 
7134  O OE2 . GLU F 43  ? 2.717 3.167 3.478 -0.222 0.185  -0.076 44  GLU DDD OE2 
7135  N N   . ARG F 44  ? 2.818 3.512 3.949 -0.148 0.291  -0.140 45  ARG DDD N   
7136  C CA  . ARG F 44  ? 2.773 3.512 3.983 -0.129 0.310  -0.155 45  ARG DDD CA  
7137  C C   . ARG F 44  ? 2.824 3.554 4.061 -0.092 0.295  -0.141 45  ARG DDD C   
7138  O O   . ARG F 44  ? 2.897 3.595 4.092 -0.073 0.276  -0.129 45  ARG DDD O   
7139  C CB  . ARG F 44  ? 2.665 3.415 3.869 -0.133 0.326  -0.171 45  ARG DDD CB  
7140  C CG  . ARG F 44  ? 2.639 3.443 3.915 -0.141 0.356  -0.197 45  ARG DDD CG  
7141  C CD  . ARG F 44  ? 2.550 3.365 3.825 -0.141 0.371  -0.213 45  ARG DDD CD  
7142  N NE  . ARG F 44  ? 2.516 3.315 3.724 -0.171 0.374  -0.215 45  ARG DDD NE  
7143  C CZ  . ARG F 44  ? 2.470 3.271 3.660 -0.178 0.384  -0.227 45  ARG DDD CZ  
7144  N NH1 . ARG F 44  ? 2.477 3.297 3.709 -0.157 0.394  -0.237 45  ARG DDD NH1 
7145  N NH2 . ARG F 44  ? 2.445 3.228 3.570 -0.207 0.384  -0.228 45  ARG DDD NH2 
7146  N N   . GLU F 45  ? 3.017 3.778 4.325 -0.082 0.302  -0.145 46  GLU DDD N   
7147  C CA  . GLU F 45  ? 2.944 3.701 4.285 -0.051 0.288  -0.133 46  GLU DDD CA  
7148  C C   . GLU F 45  ? 2.872 3.659 4.278 -0.035 0.302  -0.146 46  GLU DDD C   
7149  O O   . GLU F 45  ? 2.900 3.720 4.352 -0.046 0.323  -0.166 46  GLU DDD O   
7150  C CB  . GLU F 45  ? 2.936 3.694 4.297 -0.051 0.278  -0.121 46  GLU DDD CB  
7151  C CG  . GLU F 45  ? 2.967 3.698 4.315 -0.026 0.253  -0.099 46  GLU DDD CG  
7152  C CD  . GLU F 45  ? 2.966 3.716 4.371 -0.002 0.254  -0.099 46  GLU DDD CD  
7153  O OE1 . GLU F 45  ? 3.066 3.845 4.535 -0.003 0.265  -0.108 46  GLU DDD OE1 
7154  O OE2 . GLU F 45  ? 2.932 3.668 4.317 0.017  0.242  -0.090 46  GLU DDD OE2 
7155  N N   . PHE F 46  ? 2.720 3.497 4.128 -0.011 0.290  -0.135 47  PHE DDD N   
7156  C CA  . PHE F 46  ? 2.576 3.373 4.037 0.003  0.298  -0.144 47  PHE DDD CA  
7157  C C   . PHE F 46  ? 2.499 3.310 4.023 0.011  0.295  -0.142 47  PHE DDD C   
7158  O O   . PHE F 46  ? 2.558 3.356 4.077 0.018  0.278  -0.125 47  PHE DDD O   
7159  C CB  . PHE F 46  ? 2.542 3.325 3.975 0.021  0.285  -0.133 47  PHE DDD CB  
7160  C CG  . PHE F 46  ? 2.669 3.465 4.150 0.034  0.286  -0.134 47  PHE DDD CG  
7161  C CD1 . PHE F 46  ? 2.934 3.744 4.438 0.031  0.302  -0.151 47  PHE DDD CD1 
7162  C CD2 . PHE F 46  ? 2.729 3.521 4.232 0.048  0.269  -0.118 47  PHE DDD CD2 
7163  C CE1 . PHE F 46  ? 3.054 3.870 4.599 0.040  0.299  -0.151 47  PHE DDD CE1 
7164  C CE2 . PHE F 46  ? 2.846 3.645 4.388 0.056  0.267  -0.118 47  PHE DDD CE2 
7165  C CZ  . PHE F 46  ? 3.007 3.816 4.569 0.052  0.281  -0.134 47  PHE DDD CZ  
7166  N N   . VAL F 47  ? 2.500 3.335 4.083 0.012  0.309  -0.160 48  VAL DDD N   
7167  C CA  . VAL F 47  ? 2.439 3.288 4.086 0.021  0.305  -0.161 48  VAL DDD CA  
7168  C C   . VAL F 47  ? 2.357 3.199 4.039 0.040  0.296  -0.157 48  VAL DDD C   
7169  O O   . VAL F 47  ? 2.252 3.083 3.947 0.051  0.278  -0.139 48  VAL DDD O   
7170  C CB  . VAL F 47  ? 2.539 3.422 4.231 0.009  0.325  -0.187 48  VAL DDD CB  
7171  C CG1 . VAL F 47  ? 2.540 3.439 4.300 0.022  0.318  -0.191 48  VAL DDD CG1 
7172  C CG2 . VAL F 47  ? 2.596 3.486 4.248 -0.015 0.333  -0.190 48  VAL DDD CG2 
7173  N N   . ALA F 48  ? 2.390 3.238 4.084 0.040  0.307  -0.172 49  ALA DDD N   
7174  C CA  . ALA F 48  ? 2.383 3.221 4.109 0.054  0.297  -0.168 49  ALA DDD CA  
7175  C C   . ALA F 48  ? 2.382 3.214 4.085 0.052  0.304  -0.173 49  ALA DDD C   
7176  O O   . ALA F 48  ? 2.524 3.366 4.203 0.041  0.320  -0.188 49  ALA DDD O   
7177  C CB  . ALA F 48  ? 2.409 3.259 4.204 0.061  0.300  -0.186 49  ALA DDD CB  
7178  N N   . ARG F 49  ? 2.182 2.999 3.889 0.060  0.289  -0.161 50  ARG DDD N   
7179  C CA  . ARG F 49  ? 2.215 3.029 3.902 0.057  0.293  -0.163 50  ARG DDD CA  
7180  C C   . ARG F 49  ? 2.140 2.939 3.860 0.063  0.280  -0.159 50  ARG DDD C   
7181  O O   . ARG F 49  ? 2.053 2.841 3.790 0.070  0.261  -0.143 50  ARG DDD O   
7182  C CB  . ARG F 49  ? 2.350 3.163 3.976 0.056  0.287  -0.148 50  ARG DDD CB  
7183  C CG  . ARG F 49  ? 2.321 3.127 3.932 0.063  0.266  -0.125 50  ARG DDD CG  
7184  C CD  . ARG F 49  ? 2.023 2.836 3.576 0.062  0.264  -0.119 50  ARG DDD CD  
7185  N NE  . ARG F 49  ? 1.812 2.624 3.341 0.070  0.245  -0.099 50  ARG DDD NE  
7186  C CZ  . ARG F 49  ? 1.934 2.751 3.416 0.076  0.239  -0.094 50  ARG DDD CZ  
7187  N NH1 . ARG F 49  ? 1.910 2.727 3.361 0.073  0.249  -0.106 50  ARG DDD NH1 
7188  N NH2 . ARG F 49  ? 2.065 2.884 3.528 0.084  0.221  -0.078 50  ARG DDD NH2 
7189  N N   . ILE F 50  ? 2.131 2.927 3.857 0.058  0.288  -0.173 51  ILE DDD N   
7190  C CA  . ILE F 50  ? 2.118 2.894 3.861 0.059  0.275  -0.169 51  ILE DDD CA  
7191  C C   . ILE F 50  ? 2.262 3.041 3.965 0.047  0.282  -0.171 51  ILE DDD C   
7192  O O   . ILE F 50  ? 2.391 3.180 4.091 0.042  0.302  -0.191 51  ILE DDD O   
7193  C CB  . ILE F 50  ? 2.137 2.902 3.937 0.066  0.275  -0.188 51  ILE DDD CB  
7194  C CG1 . ILE F 50  ? 2.069 2.802 3.882 0.066  0.255  -0.181 51  ILE DDD CG1 
7195  C CG2 . ILE F 50  ? 2.338 3.120 4.145 0.061  0.299  -0.218 51  ILE DDD CG2 
7196  C CD1 . ILE F 50  ? 1.926 2.641 3.739 0.069  0.228  -0.153 51  ILE DDD CD1 
7197  N N   . VAL F 51  ? 2.262 3.037 3.936 0.043  0.268  -0.151 52  VAL DDD N   
7198  C CA  . VAL F 51  ? 2.162 2.943 3.802 0.031  0.273  -0.153 52  VAL DDD CA  
7199  C C   . VAL F 51  ? 2.214 2.972 3.868 0.022  0.260  -0.150 52  VAL DDD C   
7200  O O   . VAL F 51  ? 2.276 3.014 3.946 0.024  0.240  -0.134 52  VAL DDD O   
7201  C CB  . VAL F 51  ? 1.888 2.690 3.479 0.029  0.267  -0.136 52  VAL DDD CB  
7202  C CG1 . VAL F 51  ? 1.804 2.622 3.360 0.017  0.274  -0.140 52  VAL DDD CG1 
7203  C CG2 . VAL F 51  ? 1.881 2.696 3.456 0.038  0.274  -0.138 52  VAL DDD CG2 
7204  N N   . LYS F 52  ? 2.253 3.009 3.899 0.012  0.271  -0.164 53  LYS DDD N   
7205  C CA  . LYS F 52  ? 2.268 2.994 3.925 0.002  0.260  -0.164 53  LYS DDD CA  
7206  C C   . LYS F 52  ? 2.268 2.988 3.897 -0.011 0.238  -0.139 53  LYS DDD C   
7207  O O   . LYS F 52  ? 2.188 2.938 3.776 -0.020 0.241  -0.130 53  LYS DDD O   
7208  C CB  . LYS F 52  ? 2.265 2.994 3.909 -0.009 0.277  -0.184 53  LYS DDD CB  
7209  C CG  . LYS F 52  ? 2.325 3.041 4.011 0.001  0.290  -0.212 53  LYS DDD CG  
7210  C CD  . LYS F 52  ? 2.384 3.082 4.066 -0.011 0.295  -0.228 53  LYS DDD CD  
7211  C CE  . LYS F 52  ? 2.479 3.206 4.121 -0.024 0.315  -0.235 53  LYS DDD CE  
7212  N NZ  . LYS F 52  ? 2.636 3.349 4.284 -0.032 0.326  -0.258 53  LYS DDD NZ  
7213  N N   . GLY F 53  ? 2.456 3.141 4.108 -0.011 0.216  -0.128 54  GLY DDD N   
7214  C CA  . GLY F 53  ? 2.431 3.107 4.059 -0.027 0.193  -0.103 54  GLY DDD CA  
7215  C C   . GLY F 53  ? 2.426 3.117 4.051 -0.020 0.182  -0.083 54  GLY DDD C   
7216  O O   . GLY F 53  ? 2.503 3.187 4.112 -0.033 0.161  -0.061 54  GLY DDD O   
7217  N N   . PHE F 54  ? 2.253 2.965 3.890 -0.001 0.194  -0.089 55  PHE DDD N   
7218  C CA  . PHE F 54  ? 2.087 2.815 3.717 0.006  0.185  -0.071 55  PHE DDD CA  
7219  C C   . PHE F 54  ? 2.057 2.763 3.733 0.023  0.178  -0.073 55  PHE DDD C   
7220  O O   . PHE F 54  ? 2.072 2.763 3.784 0.032  0.186  -0.092 55  PHE DDD O   
7221  C CB  . PHE F 54  ? 1.968 2.735 3.566 0.013  0.201  -0.076 55  PHE DDD CB  
7222  C CG  . PHE F 54  ? 1.870 2.667 3.422 -0.001 0.204  -0.074 55  PHE DDD CG  
7223  C CD1 . PHE F 54  ? 1.882 2.700 3.405 -0.009 0.190  -0.056 55  PHE DDD CD1 
7224  C CD2 . PHE F 54  ? 1.855 2.662 3.393 -0.006 0.222  -0.091 55  PHE DDD CD2 
7225  C CE1 . PHE F 54  ? 1.777 2.631 3.260 -0.021 0.194  -0.057 55  PHE DDD CE1 
7226  C CE2 . PHE F 54  ? 1.788 2.627 3.286 -0.018 0.225  -0.090 55  PHE DDD CE2 
7227  C CZ  . PHE F 54  ? 1.795 2.658 3.265 -0.025 0.211  -0.074 55  PHE DDD CZ  
7228  N N   . ASP F 55  ? 1.892 2.600 3.568 0.027  0.163  -0.054 56  ASP DDD N   
7229  C CA  . ASP F 55  ? 1.895 2.589 3.614 0.043  0.157  -0.055 56  ASP DDD CA  
7230  C C   . ASP F 55  ? 1.843 2.561 3.567 0.056  0.179  -0.071 56  ASP DDD C   
7231  O O   . ASP F 55  ? 1.862 2.605 3.549 0.053  0.192  -0.073 56  ASP DDD O   
7232  C CB  . ASP F 55  ? 1.947 2.635 3.662 0.042  0.134  -0.029 56  ASP DDD CB  
7233  C CG  . ASP F 55  ? 2.006 2.671 3.707 0.024  0.112  -0.012 56  ASP DDD CG  
7234  O OD1 . ASP F 55  ? 2.011 2.648 3.726 0.018  0.107  -0.020 56  ASP DDD OD1 
7235  O OD2 . ASP F 55  ? 2.031 2.707 3.705 0.014  0.098  0.009  56  ASP DDD OD2 
7236  N N   . PRO F 56  ? 1.884 2.596 3.652 0.068  0.181  -0.083 57  PRO DDD N   
7237  C CA  . PRO F 56  ? 1.906 2.641 3.676 0.075  0.201  -0.096 57  PRO DDD CA  
7238  C C   . PRO F 56  ? 1.923 2.672 3.666 0.078  0.196  -0.079 57  PRO DDD C   
7239  O O   . PRO F 56  ? 1.917 2.657 3.666 0.081  0.178  -0.060 57  PRO DDD O   
7240  C CB  . PRO F 56  ? 1.963 2.692 3.791 0.086  0.202  -0.113 57  PRO DDD CB  
7241  C CG  . PRO F 56  ? 1.927 2.626 3.780 0.090  0.176  -0.100 57  PRO DDD CG  
7242  C CD  . PRO F 56  ? 1.894 2.578 3.712 0.076  0.167  -0.088 57  PRO DDD CD  
7243  N N   . VAL F 57  ? 1.940 2.706 3.649 0.076  0.213  -0.086 58  VAL DDD N   
7244  C CA  . VAL F 57  ? 2.048 2.824 3.727 0.080  0.210  -0.075 58  VAL DDD CA  
7245  C C   . VAL F 57  ? 2.163 2.947 3.855 0.080  0.225  -0.090 58  VAL DDD C   
7246  O O   . VAL F 57  ? 2.163 2.954 3.860 0.076  0.244  -0.111 58  VAL DDD O   
7247  C CB  . VAL F 57  ? 2.117 2.905 3.739 0.077  0.211  -0.070 58  VAL DDD CB  
7248  C CG1 . VAL F 57  ? 2.068 2.858 3.656 0.083  0.206  -0.061 58  VAL DDD CG1 
7249  C CG2 . VAL F 57  ? 2.137 2.925 3.746 0.073  0.196  -0.055 58  VAL DDD CG2 
7250  N N   . LEU F 58  ? 2.314 3.097 4.009 0.084  0.217  -0.081 59  LEU DDD N   
7251  C CA  . LEU F 58  ? 2.376 3.168 4.081 0.081  0.228  -0.091 59  LEU DDD CA  
7252  C C   . LEU F 58  ? 2.479 3.267 4.132 0.080  0.222  -0.078 59  LEU DDD C   
7253  O O   . LEU F 58  ? 2.588 3.367 4.213 0.086  0.207  -0.060 59  LEU DDD O   
7254  C CB  . LEU F 58  ? 2.365 3.160 4.128 0.086  0.223  -0.094 59  LEU DDD CB  
7255  C CG  . LEU F 58  ? 2.294 3.090 4.110 0.091  0.226  -0.111 59  LEU DDD CG  
7256  C CD1 . LEU F 58  ? 2.253 3.028 4.091 0.099  0.203  -0.095 59  LEU DDD CD1 
7257  C CD2 . LEU F 58  ? 2.582 3.399 4.445 0.092  0.237  -0.133 59  LEU DDD CD2 
7258  N N   . ALA F 59  ? 2.429 3.221 4.064 0.071  0.234  -0.087 60  ALA DDD N   
7259  C CA  . ALA F 59  ? 2.424 3.203 4.005 0.071  0.224  -0.074 60  ALA DDD CA  
7260  C C   . ALA F 59  ? 2.527 3.299 4.119 0.076  0.206  -0.055 60  ALA DDD C   
7261  O O   . ALA F 59  ? 2.600 3.379 4.243 0.077  0.205  -0.056 60  ALA DDD O   
7262  C CB  . ALA F 59  ? 2.342 3.122 3.897 0.056  0.237  -0.085 60  ALA DDD CB  
7263  N N   . ASP F 60  ? 2.469 3.225 4.011 0.081  0.192  -0.041 61  ASP DDD N   
7264  C CA  . ASP F 60  ? 2.549 3.296 4.091 0.087  0.173  -0.022 61  ASP DDD CA  
7265  C C   . ASP F 60  ? 2.706 3.453 4.267 0.078  0.174  -0.021 61  ASP DDD C   
7266  O O   . ASP F 60  ? 2.940 3.688 4.531 0.082  0.162  -0.009 61  ASP DDD O   
7267  C CB  . ASP F 60  ? 2.402 3.134 3.882 0.095  0.158  -0.011 61  ASP DDD CB  
7268  C CG  . ASP F 60  ? 2.298 3.040 3.768 0.105  0.154  -0.010 61  ASP DDD CG  
7269  O OD1 . ASP F 60  ? 2.389 3.144 3.893 0.102  0.164  -0.017 61  ASP DDD OD1 
7270  O OD2 . ASP F 60  ? 2.136 2.874 3.562 0.114  0.141  -0.003 61  ASP DDD OD2 
7271  N N   . SER F 61  ? 2.685 3.433 4.230 0.064  0.186  -0.032 62  SER DDD N   
7272  C CA  . SER F 61  ? 2.586 3.340 4.150 0.053  0.186  -0.030 62  SER DDD CA  
7273  C C   . SER F 61  ? 2.654 3.436 4.294 0.054  0.194  -0.041 62  SER DDD C   
7274  O O   . SER F 61  ? 2.687 3.481 4.353 0.047  0.193  -0.041 62  SER DDD O   
7275  C CB  . SER F 61  ? 2.426 3.176 3.951 0.033  0.196  -0.040 62  SER DDD CB  
7276  O OG  . SER F 61  ? 2.454 3.223 3.992 0.025  0.217  -0.061 62  SER DDD OG  
7277  N N   . VAL F 62  ? 2.802 3.594 4.478 0.063  0.201  -0.052 63  VAL DDD N   
7278  C CA  . VAL F 62  ? 2.839 3.653 4.585 0.067  0.207  -0.066 63  VAL DDD CA  
7279  C C   . VAL F 62  ? 2.962 3.766 4.736 0.082  0.195  -0.058 63  VAL DDD C   
7280  O O   . VAL F 62  ? 2.927 3.740 4.758 0.089  0.193  -0.067 63  VAL DDD O   
7281  C CB  . VAL F 62  ? 2.820 3.657 4.582 0.057  0.231  -0.094 63  VAL DDD CB  
7282  C CG1 . VAL F 62  ? 2.836 3.685 4.568 0.037  0.242  -0.101 63  VAL DDD CG1 
7283  C CG2 . VAL F 62  ? 2.697 3.525 4.434 0.060  0.239  -0.100 63  VAL DDD CG2 
7284  N N   . LYS F 63  ? 3.219 4.004 4.950 0.086  0.185  -0.043 64  LYS DDD N   
7285  C CA  . LYS F 63  ? 3.172 3.948 4.915 0.094  0.176  -0.037 64  LYS DDD CA  
7286  C C   . LYS F 63  ? 3.242 4.012 5.032 0.102  0.158  -0.027 64  LYS DDD C   
7287  O O   . LYS F 63  ? 3.544 4.309 5.369 0.106  0.154  -0.032 64  LYS DDD O   
7288  C CB  . LYS F 63  ? 2.875 3.640 4.562 0.096  0.167  -0.022 64  LYS DDD CB  
7289  C CG  . LYS F 63  ? 2.644 3.403 4.336 0.099  0.155  -0.012 64  LYS DDD CG  
7290  C CD  . LYS F 63  ? 2.547 3.310 4.256 0.097  0.168  -0.029 64  LYS DDD CD  
7291  C CE  . LYS F 63  ? 2.401 3.155 4.119 0.096  0.154  -0.019 64  LYS DDD CE  
7292  N NZ  . LYS F 63  ? 2.263 3.015 3.998 0.092  0.164  -0.035 64  LYS DDD NZ  
7293  N N   . GLY F 64  ? 3.034 3.803 4.825 0.102  0.145  -0.012 65  GLY DDD N   
7294  C CA  . GLY F 64  ? 2.833 3.595 4.664 0.109  0.126  0.001  65  GLY DDD CA  
7295  C C   . GLY F 64  ? 2.705 3.480 4.601 0.114  0.129  -0.016 65  GLY DDD C   
7296  O O   . GLY F 64  ? 2.724 3.489 4.658 0.122  0.111  -0.009 65  GLY DDD O   
7297  N N   . ARG F 65  ? 2.901 3.699 4.810 0.110  0.149  -0.039 66  ARG DDD N   
7298  C CA  . ARG F 65  ? 2.977 3.798 4.946 0.115  0.153  -0.058 66  ARG DDD CA  
7299  C C   . ARG F 65  ? 3.196 4.031 5.202 0.120  0.168  -0.088 66  ARG DDD C   
7300  O O   . ARG F 65  ? 3.183 4.031 5.249 0.131  0.163  -0.103 66  ARG DDD O   
7301  C CB  . ARG F 65  ? 2.941 3.787 4.902 0.103  0.163  -0.062 66  ARG DDD CB  
7302  C CG  . ARG F 65  ? 3.014 3.867 4.922 0.086  0.182  -0.068 66  ARG DDD CG  
7303  C CD  . ARG F 65  ? 2.761 3.639 4.674 0.073  0.188  -0.073 66  ARG DDD CD  
7304  N NE  . ARG F 65  ? 2.757 3.638 4.616 0.053  0.203  -0.077 66  ARG DDD NE  
7305  C CZ  . ARG F 65  ? 2.922 3.836 4.791 0.037  0.223  -0.100 66  ARG DDD CZ  
7306  N NH1 . ARG F 65  ? 3.010 3.964 4.946 0.042  0.231  -0.124 66  ARG DDD NH1 
7307  N NH2 . ARG F 65  ? 2.920 3.828 4.731 0.016  0.233  -0.100 66  ARG DDD NH2 
7308  N N   . PHE F 66  ? 3.399 4.231 5.373 0.113  0.184  -0.097 67  PHE DDD N   
7309  C CA  . PHE F 66  ? 3.457 4.302 5.460 0.116  0.200  -0.126 67  PHE DDD CA  
7310  C C   . PHE F 66  ? 3.410 4.226 5.414 0.124  0.190  -0.123 67  PHE DDD C   
7311  O O   . PHE F 66  ? 3.425 4.215 5.394 0.121  0.176  -0.098 67  PHE DDD O   
7312  C CB  . PHE F 66  ? 3.471 4.333 5.435 0.100  0.226  -0.140 67  PHE DDD CB  
7313  C CG  . PHE F 66  ? 3.594 4.487 5.555 0.087  0.239  -0.150 67  PHE DDD CG  
7314  C CD1 . PHE F 66  ? 3.667 4.574 5.658 0.090  0.229  -0.144 67  PHE DDD CD1 
7315  C CD2 . PHE F 66  ? 3.605 4.514 5.533 0.070  0.261  -0.163 67  PHE DDD CD2 
7316  C CE1 . PHE F 66  ? 3.702 4.639 5.687 0.074  0.241  -0.152 67  PHE DDD CE1 
7317  C CE2 . PHE F 66  ? 3.706 4.641 5.625 0.053  0.272  -0.171 67  PHE DDD CE2 
7318  C CZ  . PHE F 66  ? 3.731 4.682 5.679 0.054  0.262  -0.166 67  PHE DDD CZ  
7319  N N   . THR F 67  ? 3.167 3.987 5.212 0.132  0.196  -0.149 68  THR DDD N   
7320  C CA  . THR F 67  ? 3.045 3.836 5.089 0.136  0.188  -0.150 68  THR DDD CA  
7321  C C   . THR F 67  ? 3.040 3.847 5.093 0.134  0.211  -0.181 68  THR DDD C   
7322  O O   . THR F 67  ? 2.996 3.836 5.085 0.137  0.226  -0.208 68  THR DDD O   
7323  C CB  . THR F 67  ? 2.932 3.699 5.024 0.152  0.161  -0.148 68  THR DDD CB  
7324  O OG1 . THR F 67  ? 2.983 3.744 5.077 0.155  0.142  -0.123 68  THR DDD OG1 
7325  C CG2 . THR F 67  ? 2.771 3.497 4.846 0.151  0.147  -0.138 68  THR DDD CG2 
7326  N N   . ILE F 68  ? 2.950 3.738 4.969 0.127  0.215  -0.178 69  ILE DDD N   
7327  C CA  . ILE F 68  ? 2.853 3.649 4.870 0.123  0.236  -0.204 69  ILE DDD CA  
7328  C C   . ILE F 68  ? 2.790 3.554 4.822 0.129  0.224  -0.210 69  ILE DDD C   
7329  O O   . ILE F 68  ? 2.896 3.627 4.902 0.125  0.204  -0.185 69  ILE DDD O   
7330  C CB  . ILE F 68  ? 2.764 3.569 4.719 0.105  0.253  -0.195 69  ILE DDD CB  
7331  C CG1 . ILE F 68  ? 2.735 3.547 4.680 0.098  0.274  -0.219 69  ILE DDD CG1 
7332  C CG2 . ILE F 68  ? 2.633 3.413 4.541 0.101  0.236  -0.163 69  ILE DDD CG2 
7333  C CD1 . ILE F 68  ? 2.681 3.505 4.568 0.083  0.290  -0.213 69  ILE DDD CD1 
7334  N N   . SER F 69  ? 2.683 3.454 4.752 0.137  0.233  -0.243 70  SER DDD N   
7335  C CA  . SER F 69  ? 2.580 3.313 4.657 0.142  0.220  -0.248 70  SER DDD CA  
7336  C C   . SER F 69  ? 2.702 3.450 4.783 0.139  0.244  -0.281 70  SER DDD C   
7337  O O   . SER F 69  ? 2.698 3.488 4.793 0.137  0.268  -0.304 70  SER DDD O   
7338  C CB  . SER F 69  ? 2.441 3.151 4.575 0.164  0.193  -0.256 70  SER DDD CB  
7339  O OG  . SER F 69  ? 2.532 3.280 4.720 0.179  0.203  -0.287 70  SER DDD OG  
7340  N N   . ILE F 70  ? 2.806 3.520 4.871 0.135  0.238  -0.282 71  ILE DDD N   
7341  C CA  . ILE F 70  ? 2.930 3.654 4.997 0.131  0.259  -0.313 71  ILE DDD CA  
7342  C C   . ILE F 70  ? 3.018 3.703 5.114 0.144  0.242  -0.332 71  ILE DDD C   
7343  O O   . ILE F 70  ? 3.120 3.756 5.200 0.142  0.216  -0.311 71  ILE DDD O   
7344  C CB  . ILE F 70  ? 2.993 3.723 4.999 0.108  0.277  -0.302 71  ILE DDD CB  
7345  C CG1 . ILE F 70  ? 2.977 3.749 4.958 0.099  0.297  -0.295 71  ILE DDD CG1 
7346  C CG2 . ILE F 70  ? 3.006 3.737 5.013 0.104  0.295  -0.331 71  ILE DDD CG2 
7347  C CD1 . ILE F 70  ? 2.988 3.762 4.909 0.081  0.307  -0.279 71  ILE DDD CD1 
7348  N N   . ASP F 71  ? 3.033 3.741 5.170 0.156  0.257  -0.372 72  ASP DDD N   
7349  C CA  . ASP F 71  ? 3.044 3.720 5.212 0.171  0.245  -0.399 72  ASP DDD CA  
7350  C C   . ASP F 71  ? 3.122 3.814 5.270 0.158  0.273  -0.423 72  ASP DDD C   
7351  O O   . ASP F 71  ? 3.178 3.922 5.343 0.157  0.301  -0.451 72  ASP DDD O   
7352  C CB  . ASP F 71  ? 3.006 3.694 5.245 0.201  0.234  -0.431 72  ASP DDD CB  
7353  C CG  . ASP F 71  ? 3.042 3.686 5.305 0.217  0.216  -0.458 72  ASP DDD CG  
7354  O OD1 . ASP F 71  ? 2.974 3.561 5.198 0.206  0.199  -0.438 72  ASP DDD OD1 
7355  O OD2 . ASP F 71  ? 3.103 3.767 5.421 0.241  0.217  -0.498 72  ASP DDD OD2 
7356  N N   . SER F 72  ? 3.173 3.823 5.282 0.145  0.266  -0.413 73  SER DDD N   
7357  C CA  . SER F 72  ? 3.174 3.840 5.263 0.131  0.293  -0.435 73  SER DDD CA  
7358  C C   . SER F 72  ? 3.173 3.847 5.314 0.151  0.298  -0.482 73  SER DDD C   
7359  O O   . SER F 72  ? 3.213 3.916 5.350 0.143  0.325  -0.509 73  SER DDD O   
7360  C CB  . SER F 72  ? 3.183 3.804 5.220 0.112  0.283  -0.415 73  SER DDD CB  
7361  O OG  . SER F 72  ? 3.153 3.714 5.206 0.123  0.253  -0.419 73  SER DDD OG  
7362  N N   . ALA F 73  ? 3.058 3.705 5.246 0.178  0.271  -0.494 74  ALA DDD N   
7363  C CA  . ALA F 73  ? 3.198 3.855 5.442 0.202  0.272  -0.543 74  ALA DDD CA  
7364  C C   . ALA F 73  ? 3.333 4.073 5.611 0.205  0.305  -0.573 74  ALA DDD C   
7365  O O   . ALA F 73  ? 3.516 4.286 5.809 0.205  0.328  -0.612 74  ALA DDD O   
7366  C CB  . ALA F 73  ? 3.160 3.774 5.449 0.233  0.232  -0.546 74  ALA DDD CB  
7367  N N   . GLU F 74  ? 3.514 4.291 5.801 0.203  0.309  -0.557 75  GLU DDD N   
7368  C CA  . GLU F 74  ? 3.537 4.392 5.850 0.200  0.340  -0.585 75  GLU DDD CA  
7369  C C   . GLU F 74  ? 3.475 4.364 5.734 0.166  0.373  -0.571 75  GLU DDD C   
7370  O O   . GLU F 74  ? 3.688 4.638 5.959 0.158  0.398  -0.593 75  GLU DDD O   
7371  C CB  . GLU F 74  ? 3.521 4.410 5.866 0.210  0.333  -0.577 75  GLU DDD CB  
7372  C CG  . GLU F 74  ? 3.493 4.379 5.903 0.244  0.305  -0.592 75  GLU DDD CG  
7373  C CD  . GLU F 74  ? 3.453 4.267 5.854 0.255  0.265  -0.555 75  GLU DDD CD  
7374  O OE1 . GLU F 74  ? 3.432 4.240 5.805 0.243  0.258  -0.515 75  GLU DDD OE1 
7375  O OE2 . GLU F 74  ? 3.463 4.228 5.887 0.277  0.238  -0.569 75  GLU DDD OE2 
7376  N N   . ASN F 75  ? 3.170 4.021 5.368 0.147  0.371  -0.538 76  ASN DDD N   
7377  C CA  . ASN F 75  ? 3.050 3.928 5.193 0.117  0.397  -0.523 76  ASN DDD CA  
7378  C C   . ASN F 75  ? 2.859 3.776 4.999 0.110  0.404  -0.509 76  ASN DDD C   
7379  O O   . ASN F 75  ? 2.707 3.669 4.832 0.092  0.430  -0.519 76  ASN DDD O   
7380  C CB  . ASN F 75  ? 3.051 3.963 5.194 0.105  0.427  -0.560 76  ASN DDD CB  
7381  C CG  . ASN F 75  ? 3.201 4.075 5.350 0.113  0.421  -0.580 76  ASN DDD CG  
7382  O OD1 . ASN F 75  ? 3.255 4.072 5.391 0.120  0.395  -0.558 76  ASN DDD OD1 
7383  N ND2 . ASN F 75  ? 3.230 4.136 5.395 0.110  0.444  -0.620 76  ASN DDD ND2 
7384  N N   . THR F 76  ? 2.930 3.828 5.083 0.123  0.380  -0.483 77  THR DDD N   
7385  C CA  . THR F 76  ? 2.823 3.755 4.979 0.118  0.383  -0.471 77  THR DDD CA  
7386  C C   . THR F 76  ? 2.804 3.701 4.921 0.114  0.363  -0.424 77  THR DDD C   
7387  O O   . THR F 76  ? 2.796 3.645 4.903 0.121  0.340  -0.404 77  THR DDD O   
7388  C CB  . THR F 76  ? 2.766 3.726 4.992 0.141  0.375  -0.496 77  THR DDD CB  
7389  O OG1 . THR F 76  ? 2.812 3.725 5.069 0.166  0.342  -0.490 77  THR DDD OG1 
7390  C CG2 . THR F 76  ? 2.755 3.766 5.021 0.144  0.398  -0.546 77  THR DDD CG2 
7391  N N   . LEU F 77  ? 2.700 3.622 4.793 0.101  0.371  -0.408 78  LEU DDD N   
7392  C CA  . LEU F 77  ? 2.714 3.612 4.772 0.098  0.353  -0.367 78  LEU DDD CA  
7393  C C   . LEU F 77  ? 2.808 3.728 4.906 0.109  0.345  -0.367 78  LEU DDD C   
7394  O O   . LEU F 77  ? 3.030 3.994 5.136 0.099  0.362  -0.382 78  LEU DDD O   
7395  C CB  . LEU F 77  ? 2.771 3.675 4.762 0.075  0.368  -0.348 78  LEU DDD CB  
7396  C CG  . LEU F 77  ? 2.793 3.683 4.746 0.072  0.354  -0.311 78  LEU DDD CG  
7397  C CD1 . LEU F 77  ? 2.628 3.481 4.593 0.086  0.326  -0.290 78  LEU DDD CD1 
7398  C CD2 . LEU F 77  ? 2.764 3.647 4.648 0.055  0.362  -0.295 78  LEU DDD CD2 
7399  N N   . ALA F 78  ? 2.789 3.679 4.911 0.126  0.317  -0.350 79  ALA DDD N   
7400  C CA  . ALA F 78  ? 2.759 3.667 4.926 0.140  0.305  -0.352 79  ALA DDD CA  
7401  C C   . ALA F 78  ? 2.697 3.594 4.830 0.132  0.292  -0.313 79  ALA DDD C   
7402  O O   . ALA F 78  ? 2.638 3.499 4.770 0.141  0.267  -0.288 79  ALA DDD O   
7403  C CB  . ALA F 78  ? 2.669 3.552 4.890 0.166  0.280  -0.363 79  ALA DDD CB  
7404  N N   . LEU F 79  ? 2.728 3.654 4.829 0.114  0.310  -0.309 80  LEU DDD N   
7405  C CA  . LEU F 79  ? 2.729 3.651 4.803 0.108  0.299  -0.278 80  LEU DDD CA  
7406  C C   . LEU F 79  ? 2.809 3.754 4.937 0.120  0.289  -0.285 80  LEU DDD C   
7407  O O   . LEU F 79  ? 2.910 3.901 5.064 0.115  0.305  -0.309 80  LEU DDD O   
7408  C CB  . LEU F 79  ? 2.772 3.712 4.792 0.085  0.319  -0.274 80  LEU DDD CB  
7409  C CG  . LEU F 79  ? 2.761 3.697 4.746 0.076  0.310  -0.246 80  LEU DDD CG  
7410  C CD1 . LEU F 79  ? 2.825 3.720 4.760 0.078  0.294  -0.213 80  LEU DDD CD1 
7411  C CD2 . LEU F 79  ? 2.805 3.768 4.754 0.052  0.331  -0.254 80  LEU DDD CD2 
7412  N N   . GLN F 80  ? 2.914 3.829 5.057 0.135  0.261  -0.263 81  GLN DDD N   
7413  C CA  . GLN F 80  ? 3.173 4.106 5.364 0.147  0.247  -0.265 81  GLN DDD CA  
7414  C C   . GLN F 80  ? 3.444 4.381 5.599 0.133  0.245  -0.237 81  GLN DDD C   
7415  O O   . GLN F 80  ? 3.560 4.462 5.670 0.129  0.232  -0.205 81  GLN DDD O   
7416  C CB  . GLN F 80  ? 3.042 3.938 5.270 0.170  0.217  -0.257 81  GLN DDD CB  
7417  C CG  . GLN F 80  ? 2.934 3.848 5.211 0.183  0.200  -0.256 81  GLN DDD CG  
7418  C CD  . GLN F 80  ? 2.789 3.750 5.133 0.198  0.208  -0.299 81  GLN DDD CD  
7419  O OE1 . GLN F 80  ? 2.710 3.667 5.083 0.212  0.209  -0.326 81  GLN DDD OE1 
7420  N NE2 . GLN F 80  ? 2.761 3.769 5.128 0.195  0.213  -0.306 81  GLN DDD NE2 
7421  N N   . ARG F 81  ? 3.480 4.462 5.653 0.125  0.257  -0.251 82  ARG DDD N   
7422  C CA  . ARG F 81  ? 3.391 4.378 5.527 0.109  0.255  -0.228 82  ARG DDD CA  
7423  C C   . ARG F 81  ? 3.475 4.469 5.656 0.123  0.234  -0.220 82  ARG DDD C   
7424  O O   . ARG F 81  ? 3.490 4.527 5.726 0.129  0.238  -0.245 82  ARG DDD O   
7425  C CB  . ARG F 81  ? 3.162 4.193 5.282 0.086  0.282  -0.247 82  ARG DDD CB  
7426  C CG  . ARG F 81  ? 3.024 4.073 5.148 0.081  0.305  -0.278 82  ARG DDD CG  
7427  C CD  . ARG F 81  ? 2.961 4.038 5.042 0.051  0.329  -0.286 82  ARG DDD CD  
7428  N NE  . ARG F 81  ? 3.057 4.095 5.062 0.036  0.323  -0.253 82  ARG DDD NE  
7429  C CZ  . ARG F 81  ? 3.230 4.275 5.182 0.009  0.336  -0.251 82  ARG DDD CZ  
7430  N NH1 . ARG F 81  ? 3.317 4.410 5.281 -0.011 0.358  -0.278 82  ARG DDD NH1 
7431  N NH2 . ARG F 81  ? 3.237 4.242 5.121 0.001  0.326  -0.221 82  ARG DDD NH2 
7432  N N   . ASN F 82  A 3.514 4.469 5.673 0.128  0.211  -0.186 82  ASN DDD N   
7433  C CA  . ASN F 82  A 3.468 4.427 5.666 0.139  0.190  -0.176 82  ASN DDD CA  
7434  C C   . ASN F 82  A 3.433 4.395 5.589 0.122  0.189  -0.152 82  ASN DDD C   
7435  O O   . ASN F 82  A 3.535 4.480 5.628 0.106  0.197  -0.137 82  ASN DDD O   
7436  C CB  . ASN F 82  A 3.343 4.254 5.549 0.156  0.161  -0.155 82  ASN DDD CB  
7437  C CG  . ASN F 82  A 3.327 4.224 5.567 0.173  0.158  -0.176 82  ASN DDD CG  
7438  O OD1 . ASN F 82  A 3.269 4.145 5.475 0.167  0.167  -0.176 82  ASN DDD OD1 
7439  N ND2 . ASN F 82  A 3.326 4.233 5.630 0.193  0.144  -0.194 82  ASN DDD ND2 
7440  N N   . ARG F 83  B 3.133 4.115 5.325 0.126  0.176  -0.149 82  ARG DDD N   
7441  C CA  . ARG F 83  B 2.928 3.911 5.083 0.110  0.172  -0.126 82  ARG DDD CA  
7442  C C   . ARG F 83  B 2.924 3.930 5.035 0.084  0.197  -0.135 82  ARG DDD C   
7443  O O   . ARG F 83  B 2.970 3.950 5.016 0.068  0.197  -0.113 82  ARG DDD O   
7444  C CB  . ARG F 83  B 2.833 3.764 4.941 0.112  0.152  -0.089 82  ARG DDD CB  
7445  C CG  . ARG F 83  B 2.645 3.551 4.791 0.133  0.126  -0.077 82  ARG DDD CG  
7446  C CD  . ARG F 83  B 2.518 3.377 4.612 0.132  0.110  -0.046 82  ARG DDD CD  
7447  N NE  . ARG F 83  B 2.318 3.157 4.436 0.142  0.082  -0.025 82  ARG DDD NE  
7448  C CZ  . ARG F 83  B 2.237 3.070 4.339 0.137  0.068  -0.002 82  ARG DDD CZ  
7449  N NH1 . ARG F 83  B 2.294 3.138 4.357 0.122  0.079  0.004  82  ARG DDD NH1 
7450  N NH2 . ARG F 83  B 2.161 2.974 4.285 0.146  0.042  0.016  82  ARG DDD NH2 
7451  N N   . LEU F 84  C 2.915 3.968 5.059 0.078  0.218  -0.169 82  LEU DDD N   
7452  C CA  . LEU F 84  C 2.936 4.008 5.035 0.050  0.242  -0.180 82  LEU DDD CA  
7453  C C   . LEU F 84  C 2.925 4.007 4.986 0.025  0.242  -0.165 82  LEU DDD C   
7454  O O   . LEU F 84  C 2.948 4.053 5.042 0.025  0.232  -0.163 82  LEU DDD O   
7455  C CB  . LEU F 84  C 2.900 4.027 5.047 0.048  0.264  -0.221 82  LEU DDD CB  
7456  C CG  . LEU F 84  C 2.944 4.057 5.103 0.063  0.272  -0.238 82  LEU DDD CG  
7457  C CD1 . LEU F 84  C 2.801 3.973 5.016 0.065  0.292  -0.282 82  LEU DDD CD1 
7458  C CD2 . LEU F 84  C 3.092 4.171 5.175 0.045  0.282  -0.224 82  LEU DDD CD2 
7459  N N   . LYS F 85  ? 2.874 3.934 4.862 0.001  0.251  -0.156 83  LYS DDD N   
7460  C CA  . LYS F 85  ? 2.747 3.802 4.678 -0.027 0.251  -0.140 83  LYS DDD CA  
7461  C C   . LYS F 85  ? 2.665 3.750 4.567 -0.059 0.274  -0.161 83  LYS DDD C   
7462  O O   . LYS F 85  ? 2.745 3.844 4.656 -0.059 0.291  -0.182 83  LYS DDD O   
7463  C CB  . LYS F 85  ? 2.685 3.675 4.545 -0.025 0.233  -0.107 83  LYS DDD CB  
7464  C CG  . LYS F 85  ? 2.598 3.565 4.466 -0.010 0.209  -0.081 83  LYS DDD CG  
7465  C CD  . LYS F 85  ? 2.577 3.514 4.463 0.019  0.195  -0.070 83  LYS DDD CD  
7466  C CE  . LYS F 85  ? 2.488 3.418 4.403 0.033  0.172  -0.051 83  LYS DDD CE  
7467  N NZ  . LYS F 85  ? 2.652 3.555 4.585 0.057  0.157  -0.039 83  LYS DDD NZ  
7468  N N   . PRO F 86  ? 2.601 3.695 4.465 -0.090 0.275  -0.154 84  PRO DDD N   
7469  C CA  . PRO F 86  ? 2.572 3.687 4.394 -0.128 0.295  -0.168 84  PRO DDD CA  
7470  C C   . PRO F 86  ? 2.673 3.738 4.422 -0.135 0.297  -0.159 84  PRO DDD C   
7471  O O   . PRO F 86  ? 2.773 3.860 4.507 -0.157 0.317  -0.179 84  PRO DDD O   
7472  C CB  . PRO F 86  ? 2.357 3.476 4.144 -0.158 0.286  -0.153 84  PRO DDD CB  
7473  C CG  . PRO F 86  ? 2.308 3.445 4.157 -0.135 0.272  -0.148 84  PRO DDD CG  
7474  C CD  . PRO F 86  ? 2.422 3.516 4.288 -0.094 0.258  -0.135 84  PRO DDD CD  
7475  N N   . GLU F 87  ? 2.564 3.566 4.268 -0.118 0.278  -0.131 85  GLU DDD N   
7476  C CA  . GLU F 87  ? 2.612 3.565 4.247 -0.120 0.276  -0.123 85  GLU DDD CA  
7477  C C   . GLU F 87  ? 2.913 3.879 4.575 -0.107 0.293  -0.143 85  GLU DDD C   
7478  O O   . GLU F 87  ? 2.951 3.886 4.558 -0.113 0.295  -0.141 85  GLU DDD O   
7479  C CB  . GLU F 87  ? 2.443 3.336 4.038 -0.098 0.251  -0.092 85  GLU DDD CB  
7480  C CG  . GLU F 87  ? 2.348 3.212 3.893 -0.114 0.232  -0.070 85  GLU DDD CG  
7481  C CD  . GLU F 87  ? 2.283 3.155 3.874 -0.096 0.218  -0.057 85  GLU DDD CD  
7482  O OE1 . GLU F 87  ? 2.232 3.112 3.877 -0.067 0.216  -0.059 85  GLU DDD OE1 
7483  O OE2 . GLU F 87  ? 2.282 3.149 3.852 -0.113 0.208  -0.045 85  GLU DDD OE2 
7484  N N   . ASP F 88  ? 3.301 4.309 5.042 -0.089 0.302  -0.164 86  ASP DDD N   
7485  C CA  . ASP F 88  ? 3.532 4.550 5.295 -0.078 0.318  -0.185 86  ASP DDD CA  
7486  C C   . ASP F 88  ? 3.523 4.580 5.278 -0.108 0.343  -0.212 86  ASP DDD C   
7487  O O   . ASP F 88  ? 3.611 4.677 5.377 -0.104 0.357  -0.231 86  ASP DDD O   
7488  C CB  . ASP F 88  ? 3.846 4.887 5.693 -0.047 0.316  -0.199 86  ASP DDD CB  
7489  C CG  . ASP F 88  ? 3.933 4.933 5.784 -0.020 0.292  -0.172 86  ASP DDD CG  
7490  O OD1 . ASP F 88  ? 3.839 4.793 5.634 -0.016 0.282  -0.151 86  ASP DDD OD1 
7491  O OD2 . ASP F 88  ? 4.091 5.105 6.000 -0.002 0.282  -0.173 86  ASP DDD OD2 
7492  N N   . THR F 89  ? 3.334 4.418 5.071 -0.140 0.348  -0.215 87  THR DDD N   
7493  C CA  . THR F 89  ? 3.296 4.420 5.019 -0.175 0.372  -0.240 87  THR DDD CA  
7494  C C   . THR F 89  ? 3.340 4.419 4.986 -0.189 0.374  -0.231 87  THR DDD C   
7495  O O   . THR F 89  ? 3.395 4.419 4.967 -0.198 0.357  -0.204 87  THR DDD O   
7496  C CB  . THR F 89  ? 3.225 4.379 4.929 -0.212 0.373  -0.239 87  THR DDD CB  
7497  O OG1 . THR F 89  ? 3.181 4.380 4.958 -0.197 0.370  -0.248 87  THR DDD OG1 
7498  C CG2 . THR F 89  ? 3.155 4.354 4.839 -0.253 0.398  -0.264 87  THR DDD CG2 
7499  N N   . ALA F 90  ? 3.374 4.477 5.038 -0.189 0.394  -0.256 88  ALA DDD N   
7500  C CA  . ALA F 90  ? 3.360 4.427 4.961 -0.200 0.398  -0.253 88  ALA DDD CA  
7501  C C   . ALA F 90  ? 3.296 4.409 4.941 -0.201 0.424  -0.288 88  ALA DDD C   
7502  O O   . ALA F 90  ? 3.493 4.656 5.217 -0.185 0.434  -0.312 88  ALA DDD O   
7503  C CB  . ALA F 90  ? 3.382 4.385 4.950 -0.170 0.378  -0.227 88  ALA DDD CB  
7504  N N   . VAL F 91  ? 3.102 4.197 4.695 -0.218 0.433  -0.291 89  VAL DDD N   
7505  C CA  . VAL F 91  ? 3.001 4.128 4.631 -0.212 0.454  -0.321 89  VAL DDD CA  
7506  C C   . VAL F 91  ? 2.981 4.064 4.617 -0.174 0.443  -0.308 89  VAL DDD C   
7507  O O   . VAL F 91  ? 2.946 3.974 4.520 -0.171 0.426  -0.282 89  VAL DDD O   
7508  C CB  . VAL F 91  ? 2.841 3.975 4.414 -0.252 0.471  -0.332 89  VAL DDD CB  
7509  C CG1 . VAL F 91  ? 2.845 4.004 4.451 -0.243 0.491  -0.360 89  VAL DDD CG1 
7510  C CG2 . VAL F 91  ? 2.790 3.973 4.357 -0.293 0.484  -0.346 89  VAL DDD CG2 
7511  N N   . TYR F 92  ? 2.836 3.944 4.544 -0.147 0.450  -0.328 90  TYR DDD N   
7512  C CA  . TYR F 92  ? 2.823 3.893 4.541 -0.114 0.437  -0.316 90  TYR DDD CA  
7513  C C   . TYR F 92  ? 2.871 3.945 4.592 -0.112 0.453  -0.336 90  TYR DDD C   
7514  O O   . TYR F 92  ? 2.947 4.065 4.716 -0.115 0.472  -0.369 90  TYR DDD O   
7515  C CB  . TYR F 92  ? 2.887 3.968 4.680 -0.082 0.427  -0.319 90  TYR DDD CB  
7516  C CG  . TYR F 92  ? 2.966 4.029 4.758 -0.074 0.405  -0.293 90  TYR DDD CG  
7517  C CD1 . TYR F 92  ? 3.112 4.204 4.908 -0.093 0.407  -0.295 90  TYR DDD CD1 
7518  C CD2 . TYR F 92  ? 2.920 3.939 4.707 -0.048 0.383  -0.267 90  TYR DDD CD2 
7519  C CE1 . TYR F 92  ? 3.220 4.296 5.016 -0.085 0.387  -0.272 90  TYR DDD CE1 
7520  C CE2 . TYR F 92  ? 2.970 3.974 4.757 -0.041 0.364  -0.244 90  TYR DDD CE2 
7521  C CZ  . TYR F 92  ? 3.187 4.218 4.978 -0.058 0.366  -0.246 90  TYR DDD CZ  
7522  O OH  . TYR F 92  ? 3.437 4.452 5.227 -0.052 0.346  -0.223 90  TYR DDD OH  
7523  N N   . TYR F 93  ? 2.828 3.858 4.505 -0.103 0.444  -0.318 91  TYR DDD N   
7524  C CA  . TYR F 93  ? 2.934 3.964 4.610 -0.101 0.457  -0.334 91  TYR DDD CA  
7525  C C   . TYR F 93  ? 2.979 3.978 4.675 -0.069 0.441  -0.320 91  TYR DDD C   
7526  O O   . TYR F 93  ? 2.940 3.905 4.607 -0.058 0.420  -0.291 91  TYR DDD O   
7527  C CB  . TYR F 93  ? 2.860 3.869 4.459 -0.125 0.462  -0.327 91  TYR DDD CB  
7528  C CG  . TYR F 93  ? 2.835 3.860 4.393 -0.162 0.471  -0.332 91  TYR DDD CG  
7529  C CD1 . TYR F 93  ? 2.808 3.807 4.316 -0.174 0.454  -0.307 91  TYR DDD CD1 
7530  C CD2 . TYR F 93  ? 2.935 3.999 4.497 -0.188 0.496  -0.361 91  TYR DDD CD2 
7531  C CE1 . TYR F 93  ? 2.869 3.878 4.331 -0.212 0.461  -0.310 91  TYR DDD CE1 
7532  C CE2 . TYR F 93  ? 3.047 4.126 4.566 -0.227 0.505  -0.365 91  TYR DDD CE2 
7533  C CZ  . TYR F 93  ? 3.013 4.062 4.480 -0.240 0.486  -0.338 91  TYR DDD CZ  
7534  O OH  . TYR F 93  ? 3.072 4.132 4.490 -0.283 0.492  -0.340 91  TYR DDD OH  
7535  N N   . CYS F 94  ? 3.098 4.109 4.841 -0.056 0.449  -0.341 92  CYS DDD N   
7536  C CA  . CYS F 94  ? 3.086 4.067 4.838 -0.033 0.436  -0.330 92  CYS DDD CA  
7537  C C   . CYS F 94  ? 3.035 4.001 4.745 -0.040 0.443  -0.331 92  CYS DDD C   
7538  O O   . CYS F 94  ? 2.966 3.951 4.660 -0.059 0.463  -0.350 92  CYS DDD O   
7539  C CB  . CYS F 94  ? 3.167 4.162 4.994 -0.013 0.436  -0.350 92  CYS DDD CB  
7540  S SG  . CYS F 94  ? 3.266 4.306 5.133 -0.023 0.464  -0.396 92  CYS DDD SG  
7541  N N   . PHE F 95  ? 3.114 4.049 4.805 -0.026 0.428  -0.310 93  PHE DDD N   
7542  C CA  . PHE F 95  ? 3.027 3.952 4.684 -0.030 0.433  -0.311 93  PHE DDD CA  
7543  C C   . PHE F 95  ? 2.921 3.830 4.604 -0.013 0.424  -0.309 93  PHE DDD C   
7544  O O   . PHE F 95  ? 2.897 3.791 4.604 0.002  0.406  -0.294 93  PHE DDD O   
7545  C CB  . PHE F 95  ? 3.080 3.984 4.665 -0.036 0.422  -0.287 93  PHE DDD CB  
7546  C CG  . PHE F 95  ? 3.256 4.137 4.831 -0.018 0.398  -0.259 93  PHE DDD CG  
7547  C CD1 . PHE F 95  ? 3.465 4.340 5.043 -0.012 0.384  -0.243 93  PHE DDD CD1 
7548  C CD2 . PHE F 95  ? 3.215 4.084 4.774 -0.008 0.390  -0.250 93  PHE DDD CD2 
7549  C CE1 . PHE F 95  ? 3.629 4.485 5.195 0.004  0.363  -0.219 93  PHE DDD CE1 
7550  C CE2 . PHE F 95  ? 3.324 4.178 4.872 0.006  0.368  -0.226 93  PHE DDD CE2 
7551  C CZ  . PHE F 95  ? 3.467 4.315 5.019 0.012  0.355  -0.211 93  PHE DDD CZ  
7552  N N   . ALA F 96  ? 2.858 3.767 4.532 -0.019 0.435  -0.322 94  ALA DDD N   
7553  C CA  . ALA F 96  ? 2.805 3.696 4.493 -0.009 0.426  -0.319 94  ALA DDD CA  
7554  C C   . ALA F 96  ? 2.745 3.631 4.378 -0.019 0.431  -0.313 94  ALA DDD C   
7555  O O   . ALA F 96  ? 2.829 3.729 4.437 -0.034 0.447  -0.327 94  ALA DDD O   
7556  C CB  . ALA F 96  ? 2.822 3.718 4.565 -0.004 0.435  -0.347 94  ALA DDD CB  
7557  N N   . ALA F 97  ? 2.665 3.534 4.282 -0.012 0.415  -0.295 95  ALA DDD N   
7558  C CA  . ALA F 97  ? 2.577 3.447 4.144 -0.020 0.416  -0.287 95  ALA DDD CA  
7559  C C   . ALA F 97  ? 2.595 3.458 4.169 -0.023 0.418  -0.295 95  ALA DDD C   
7560  O O   . ALA F 97  ? 2.782 3.631 4.374 -0.017 0.403  -0.285 95  ALA DDD O   
7561  C CB  . ALA F 97  ? 2.846 3.709 4.380 -0.011 0.395  -0.259 95  ALA DDD CB  
7562  N N   . LEU F 98  ? 2.510 3.384 4.067 -0.036 0.435  -0.313 96  LEU DDD N   
7563  C CA  . LEU F 98  ? 2.365 3.233 3.915 -0.044 0.438  -0.318 96  LEU DDD CA  
7564  C C   . LEU F 98  ? 2.274 3.158 3.771 -0.055 0.446  -0.318 96  LEU DDD C   
7565  O O   . LEU F 98  ? 2.064 2.958 3.549 -0.063 0.461  -0.330 96  LEU DDD O   
7566  C CB  . LEU F 98  ? 2.381 3.243 3.973 -0.047 0.450  -0.345 96  LEU DDD CB  
7567  C CG  . LEU F 98  ? 2.329 3.172 3.920 -0.051 0.442  -0.344 96  LEU DDD CG  
7568  C CD1 . LEU F 98  ? 2.467 3.291 4.106 -0.047 0.445  -0.367 96  LEU DDD CD1 
7569  C CD2 . LEU F 98  ? 2.055 2.909 3.600 -0.067 0.451  -0.344 96  LEU DDD CD2 
7570  N N   . ASP F 99  ? 2.222 3.109 3.686 -0.056 0.436  -0.303 97  ASP DDD N   
7571  C CA  . ASP F 99  ? 2.076 2.979 3.491 -0.065 0.441  -0.304 97  ASP DDD CA  
7572  C C   . ASP F 99  ? 2.078 2.987 3.487 -0.079 0.463  -0.326 97  ASP DDD C   
7573  O O   . ASP F 99  ? 2.096 3.008 3.506 -0.091 0.476  -0.341 97  ASP DDD O   
7574  C CB  . ASP F 99  ? 1.844 2.753 3.244 -0.072 0.436  -0.299 97  ASP DDD CB  
7575  C CG  . ASP F 99  ? 1.541 2.472 2.888 -0.074 0.432  -0.292 97  ASP DDD CG  
7576  O OD1 . ASP F 99  ? 1.498 2.433 2.819 -0.066 0.428  -0.287 97  ASP DDD OD1 
7577  O OD2 . ASP F 99  ? 1.480 2.423 2.810 -0.083 0.432  -0.292 97  ASP DDD OD2 
7578  N N   . THR F 100 ? 2.019 2.930 3.423 -0.079 0.468  -0.329 98  THR DDD N   
7579  C CA  . THR F 100 ? 1.971 2.891 3.356 -0.095 0.486  -0.346 98  THR DDD CA  
7580  C C   . THR F 100 ? 2.071 3.000 3.435 -0.110 0.499  -0.359 98  THR DDD C   
7581  O O   . THR F 100 ? 1.981 2.912 3.371 -0.119 0.515  -0.380 98  THR DDD O   
7582  C CB  . THR F 100 ? 1.836 2.753 3.173 -0.095 0.476  -0.332 98  THR DDD CB  
7583  O OG1 . THR F 100 ? 1.593 2.501 2.947 -0.083 0.465  -0.320 98  THR DDD OG1 
7584  C CG2 . THR F 100 ? 1.881 2.804 3.194 -0.116 0.493  -0.348 98  THR DDD CG2 
7585  N N   . ALA F 103 ? 1.660 2.552 3.027 -0.070 0.446  -0.299 101 ALA DDD N   
7586  C CA  . ALA F 103 ? 1.876 2.765 3.275 -0.065 0.442  -0.295 101 ALA DDD CA  
7587  C C   . ALA F 103 ? 2.470 3.376 3.898 -0.083 0.464  -0.319 101 ALA DDD C   
7588  O O   . ALA F 103 ? 2.647 3.558 4.043 -0.103 0.476  -0.329 101 ALA DDD O   
7589  C CB  . ALA F 103 ? 1.693 2.566 3.051 -0.060 0.423  -0.274 101 ALA DDD CB  
7590  N N   . TYR F 104 ? 2.482 3.397 3.970 -0.075 0.468  -0.328 102 TYR DDD N   
7591  C CA  . TYR F 104 ? 2.434 3.373 3.960 -0.088 0.487  -0.354 102 TYR DDD CA  
7592  C C   . TYR F 104 ? 2.504 3.449 4.053 -0.085 0.480  -0.348 102 TYR DDD C   
7593  O O   . TYR F 104 ? 2.546 3.476 4.109 -0.066 0.462  -0.329 102 TYR DDD O   
7594  C CB  . TYR F 104 ? 2.543 3.492 4.126 -0.079 0.497  -0.376 102 TYR DDD CB  
7595  C CG  . TYR F 104 ? 2.791 3.735 4.355 -0.084 0.504  -0.384 102 TYR DDD CG  
7596  C CD1 . TYR F 104 ? 2.851 3.803 4.369 -0.104 0.517  -0.390 102 TYR DDD CD1 
7597  C CD2 . TYR F 104 ? 3.074 4.005 4.667 -0.070 0.498  -0.385 102 TYR DDD CD2 
7598  C CE1 . TYR F 104 ? 2.882 3.831 4.383 -0.110 0.524  -0.397 102 TYR DDD CE1 
7599  C CE2 . TYR F 104 ? 3.005 3.932 4.579 -0.078 0.505  -0.392 102 TYR DDD CE2 
7600  C CZ  . TYR F 104 ? 2.804 3.743 4.334 -0.096 0.518  -0.399 102 TYR DDD CZ  
7601  O OH  . TYR F 104 ? 2.507 3.444 4.019 -0.104 0.525  -0.406 102 TYR DDD OH  
7602  N N   . TRP F 105 ? 2.580 3.549 4.132 -0.105 0.496  -0.365 103 TRP DDD N   
7603  C CA  . TRP F 105 ? 2.679 3.662 4.250 -0.109 0.493  -0.363 103 TRP DDD CA  
7604  C C   . TRP F 105 ? 2.714 3.739 4.345 -0.115 0.513  -0.396 103 TRP DDD C   
7605  O O   . TRP F 105 ? 2.710 3.758 4.350 -0.127 0.533  -0.423 103 TRP DDD O   
7606  C CB  . TRP F 105 ? 2.664 3.636 4.169 -0.132 0.489  -0.349 103 TRP DDD CB  
7607  C CG  . TRP F 105 ? 2.693 3.624 4.141 -0.122 0.465  -0.317 103 TRP DDD CG  
7608  C CD1 . TRP F 105 ? 2.699 3.607 4.080 -0.131 0.459  -0.307 103 TRP DDD CD1 
7609  C CD2 . TRP F 105 ? 2.706 3.616 4.156 -0.102 0.442  -0.293 103 TRP DDD CD2 
7610  N NE1 . TRP F 105 ? 2.742 3.618 4.087 -0.114 0.434  -0.280 103 TRP DDD NE1 
7611  C CE2 . TRP F 105 ? 2.738 3.615 4.124 -0.097 0.424  -0.271 103 TRP DDD CE2 
7612  C CE3 . TRP F 105 ? 2.675 3.591 4.176 -0.086 0.435  -0.288 103 TRP DDD CE3 
7613  C CZ2 . TRP F 105 ? 2.714 3.566 4.084 -0.078 0.400  -0.246 103 TRP DDD CZ2 
7614  C CZ3 . TRP F 105 ? 2.646 3.536 4.131 -0.069 0.411  -0.261 103 TRP DDD CZ3 
7615  C CH2 . TRP F 105 ? 2.700 3.560 4.121 -0.066 0.394  -0.241 103 TRP DDD CH2 
7616  N N   . GLY F 106 ? 2.771 3.811 4.445 -0.105 0.507  -0.396 104 GLY DDD N   
7617  C CA  . GLY F 106 ? 2.777 3.865 4.504 -0.113 0.524  -0.428 104 GLY DDD CA  
7618  C C   . GLY F 106 ? 2.800 3.916 4.491 -0.149 0.537  -0.434 104 GLY DDD C   
7619  O O   . GLY F 106 ? 2.873 3.963 4.496 -0.167 0.530  -0.412 104 GLY DDD O   
7620  N N   . GLN F 107 ? 2.725 3.896 4.464 -0.159 0.555  -0.466 105 GLN DDD N   
7621  C CA  . GLN F 107 ? 2.820 4.024 4.527 -0.198 0.568  -0.474 105 GLN DDD CA  
7622  C C   . GLN F 107 ? 2.960 4.165 4.660 -0.205 0.555  -0.455 105 GLN DDD C   
7623  O O   . GLN F 107 ? 2.928 4.143 4.579 -0.240 0.560  -0.450 105 GLN DDD O   
7624  C CB  . GLN F 107 ? 2.769 4.041 4.531 -0.208 0.595  -0.521 105 GLN DDD CB  
7625  C CG  . GLN F 107 ? 2.703 3.988 4.450 -0.223 0.615  -0.544 105 GLN DDD CG  
7626  C CD  . GLN F 107 ? 2.666 3.936 4.329 -0.263 0.620  -0.529 105 GLN DDD CD  
7627  O OE1 . GLN F 107 ? 2.742 4.028 4.373 -0.294 0.621  -0.523 105 GLN DDD OE1 
7628  N NE2 . GLN F 107 ? 2.546 3.782 4.169 -0.265 0.621  -0.522 105 GLN DDD NE2 
7629  N N   . GLY F 108 ? 3.230 4.425 4.974 -0.174 0.538  -0.444 106 GLY DDD N   
7630  C CA  . GLY F 108 ? 3.432 4.620 5.171 -0.174 0.521  -0.422 106 GLY DDD CA  
7631  C C   . GLY F 108 ? 3.650 4.899 5.458 -0.173 0.530  -0.448 106 GLY DDD C   
7632  O O   . GLY F 108 ? 3.956 5.263 5.802 -0.184 0.552  -0.485 106 GLY DDD O   
7633  N N   . THR F 109 ? 3.681 4.922 5.507 -0.160 0.512  -0.429 107 THR DDD N   
7634  C CA  . THR F 109 ? 3.665 4.966 5.551 -0.161 0.518  -0.451 107 THR DDD CA  
7635  C C   . THR F 109 ? 3.629 4.923 5.483 -0.179 0.504  -0.425 107 THR DDD C   
7636  O O   . THR F 109 ? 3.834 5.071 5.655 -0.165 0.481  -0.389 107 THR DDD O   
7637  C CB  . THR F 109 ? 3.580 4.892 5.549 -0.119 0.509  -0.465 107 THR DDD CB  
7638  O OG1 . THR F 109 ? 3.545 4.858 5.540 -0.103 0.519  -0.490 107 THR DDD OG1 
7639  C CG2 . THR F 109 ? 3.476 4.861 5.506 -0.123 0.518  -0.495 107 THR DDD CG2 
7640  N N   . GLN F 110 ? 3.245 4.599 5.110 -0.208 0.517  -0.443 108 GLN DDD N   
7641  C CA  . GLN F 110 ? 3.012 4.354 4.839 -0.228 0.503  -0.416 108 GLN DDD CA  
7642  C C   . GLN F 110 ? 3.029 4.385 4.928 -0.193 0.489  -0.416 108 GLN DDD C   
7643  O O   . GLN F 110 ? 2.968 4.382 4.945 -0.177 0.499  -0.450 108 GLN DDD O   
7644  C CB  . GLN F 110 ? 2.778 4.177 4.582 -0.278 0.521  -0.433 108 GLN DDD CB  
7645  C CG  . GLN F 110 ? 2.767 4.159 4.541 -0.299 0.506  -0.408 108 GLN DDD CG  
7646  C CD  . GLN F 110 ? 2.721 4.033 4.395 -0.318 0.487  -0.367 108 GLN DDD CD  
7647  O OE1 . GLN F 110 ? 2.666 3.961 4.274 -0.350 0.494  -0.365 108 GLN DDD OE1 
7648  N NE2 . GLN F 110 ? 2.809 4.071 4.469 -0.298 0.462  -0.335 108 GLN DDD NE2 
7649  N N   . VAL F 111 ? 3.115 4.417 4.989 -0.180 0.464  -0.379 109 VAL DDD N   
7650  C CA  . VAL F 111 ? 3.172 4.481 5.105 -0.150 0.447  -0.373 109 VAL DDD CA  
7651  C C   . VAL F 111 ? 3.264 4.568 5.165 -0.171 0.434  -0.349 109 VAL DDD C   
7652  O O   . VAL F 111 ? 3.348 4.598 5.172 -0.187 0.423  -0.318 109 VAL DDD O   
7653  C CB  . VAL F 111 ? 3.060 4.308 5.003 -0.109 0.426  -0.351 109 VAL DDD CB  
7654  C CG1 . VAL F 111 ? 3.043 4.287 5.029 -0.084 0.405  -0.337 109 VAL DDD CG1 
7655  C CG2 . VAL F 111 ? 2.925 4.185 4.915 -0.086 0.437  -0.379 109 VAL DDD CG2 
7656  N N   . THR F 112 ? 3.329 4.693 5.287 -0.172 0.437  -0.366 110 THR DDD N   
7657  C CA  . THR F 112 ? 3.292 4.667 5.228 -0.196 0.428  -0.349 110 THR DDD CA  
7658  C C   . THR F 112 ? 3.352 4.742 5.360 -0.162 0.411  -0.348 110 THR DDD C   
7659  O O   . THR F 112 ? 3.548 4.999 5.637 -0.143 0.420  -0.382 110 THR DDD O   
7660  C CB  . THR F 112 ? 3.256 4.703 5.185 -0.243 0.450  -0.375 110 THR DDD CB  
7661  O OG1 . THR F 112 ? 3.267 4.712 5.149 -0.269 0.468  -0.386 110 THR DDD OG1 
7662  C CG2 . THR F 112 ? 3.185 4.619 5.057 -0.277 0.438  -0.348 110 THR DDD CG2 
7663  N N   . VAL F 113 ? 3.227 4.564 5.207 -0.152 0.387  -0.311 111 VAL DDD N   
7664  C CA  . VAL F 113 ? 3.142 4.487 5.183 -0.122 0.369  -0.305 111 VAL DDD CA  
7665  C C   . VAL F 113 ? 3.102 4.468 5.126 -0.149 0.362  -0.292 111 VAL DDD C   
7666  O O   . VAL F 113 ? 3.120 4.432 5.072 -0.166 0.349  -0.258 111 VAL DDD O   
7667  C CB  . VAL F 113 ? 3.042 4.312 5.070 -0.088 0.345  -0.273 111 VAL DDD CB  
7668  C CG1 . VAL F 113 ? 3.045 4.324 5.143 -0.055 0.326  -0.271 111 VAL DDD CG1 
7669  C CG2 . VAL F 113 ? 3.044 4.285 5.068 -0.071 0.351  -0.281 111 VAL DDD CG2 
7670  N N   . SER F 114 ? 3.012 4.456 5.102 -0.151 0.370  -0.320 112 SER DDD N   
7671  C CA  . SER F 114 ? 2.807 4.283 4.896 -0.173 0.363  -0.311 112 SER DDD CA  
7672  C C   . SER F 114 ? 2.767 4.334 4.954 -0.158 0.369  -0.349 112 SER DDD C   
7673  O O   . SER F 114 ? 2.758 4.386 4.989 -0.158 0.390  -0.389 112 SER DDD O   
7674  C CB  . SER F 114 ? 2.519 4.004 4.533 -0.229 0.375  -0.306 112 SER DDD CB  
7675  O OG  . SER F 114 ? 2.276 3.805 4.297 -0.254 0.372  -0.304 112 SER DDD OG  
7676  N N   . MET G 1   ? 5.085 3.585 2.871 1.415  0.600  0.351  1   MET GGG N   
7677  C CA  . MET G 1   ? 5.081 3.777 2.948 1.456  0.576  0.359  1   MET GGG CA  
7678  C C   . MET G 1   ? 5.127 3.921 3.106 1.406  0.548  0.345  1   MET GGG C   
7679  O O   . MET G 1   ? 5.202 3.915 3.203 1.340  0.545  0.329  1   MET GGG O   
7680  C CB  . MET G 1   ? 4.978 3.772 2.914 1.437  0.553  0.359  1   MET GGG CB  
7681  C CG  . MET G 1   ? 4.902 3.912 2.972 1.424  0.515  0.356  1   MET GGG CG  
7682  S SD  . MET G 1   ? 4.836 3.923 3.013 1.351  0.482  0.344  1   MET GGG SD  
7683  C CE  . MET G 1   ? 4.453 3.765 2.776 1.322  0.441  0.336  1   MET GGG CE  
7684  N N   . VAL G 2   ? 5.273 4.237 3.317 1.439  0.528  0.350  2   VAL GGG N   
7685  C CA  . VAL G 2   ? 5.089 4.145 3.233 1.394  0.502  0.337  2   VAL GGG CA  
7686  C C   . VAL G 2   ? 4.931 3.992 3.183 1.290  0.474  0.315  2   VAL GGG C   
7687  O O   . VAL G 2   ? 4.990 4.020 3.282 1.239  0.466  0.301  2   VAL GGG O   
7688  C CB  . VAL G 2   ? 4.984 4.239 3.187 1.435  0.483  0.346  2   VAL GGG CB  
7689  C CG1 . VAL G 2   ? 5.073 4.325 3.179 1.532  0.510  0.365  2   VAL GGG CG1 
7690  C CG2 . VAL G 2   ? 4.909 4.266 3.147 1.443  0.469  0.352  2   VAL GGG CG2 
7691  N N   . ASN G 3   ? 4.914 4.012 3.211 1.259  0.459  0.312  3   ASN GGG N   
7692  C CA  . ASN G 3   ? 4.639 3.742 3.031 1.166  0.433  0.293  3   ASN GGG CA  
7693  C C   . ASN G 3   ? 4.727 3.665 3.061 1.132  0.451  0.288  3   ASN GGG C   
7694  O O   . ASN G 3   ? 4.658 3.576 2.976 1.129  0.452  0.291  3   ASN GGG O   
7695  C CB  . ASN G 3   ? 4.376 3.621 2.855 1.148  0.405  0.292  3   ASN GGG CB  
7696  C CG  . ASN G 3   ? 4.251 3.660 2.819 1.140  0.378  0.288  3   ASN GGG CG  
7697  O OD1 . ASN G 3   ? 4.307 3.721 2.892 1.131  0.376  0.282  3   ASN GGG OD1 
7698  N ND2 . ASN G 3   ? 4.090 3.634 2.713 1.141  0.359  0.290  3   ASN GGG ND2 
7699  N N   . PRO G 4   ? 4.685 3.506 2.983 1.104  0.465  0.280  4   PRO GGG N   
7700  C CA  . PRO G 4   ? 4.682 3.347 2.916 1.068  0.484  0.275  4   PRO GGG CA  
7701  C C   . PRO G 4   ? 4.630 3.315 2.956 0.983  0.458  0.260  4   PRO GGG C   
7702  O O   . PRO G 4   ? 4.672 3.480 3.113 0.948  0.425  0.252  4   PRO GGG O   
7703  C CB  . PRO G 4   ? 4.737 3.295 2.912 1.064  0.504  0.271  4   PRO GGG CB  
7704  C CG  . PRO G 4   ? 4.769 3.448 3.035 1.058  0.482  0.266  4   PRO GGG CG  
7705  C CD  . PRO G 4   ? 4.646 3.494 2.999 1.073  0.454  0.270  4   PRO GGG CD  
7706  N N   . THR G 5   ? 4.601 3.158 2.869 0.950  0.474  0.256  5   THR GGG N   
7707  C CA  . THR G 5   ? 4.462 3.016 2.797 0.872  0.454  0.243  5   THR GGG CA  
7708  C C   . THR G 5   ? 4.395 2.834 2.701 0.816  0.467  0.231  5   THR GGG C   
7709  O O   . THR G 5   ? 4.503 2.821 2.700 0.837  0.498  0.235  5   THR GGG O   
7710  C CB  . THR G 5   ? 4.452 2.983 2.753 0.880  0.458  0.249  5   THR GGG CB  
7711  O OG1 . THR G 5   ? 4.616 3.001 2.775 0.917  0.497  0.258  5   THR GGG OG1 
7712  C CG2 . THR G 5   ? 4.436 3.102 2.781 0.929  0.443  0.259  5   THR GGG CG2 
7713  N N   . VAL G 6   ? 4.189 2.669 2.591 0.743  0.442  0.217  6   VAL GGG N   
7714  C CA  . VAL G 6   ? 4.055 2.462 2.455 0.683  0.447  0.205  6   VAL GGG CA  
7715  C C   . VAL G 6   ? 4.031 2.419 2.464 0.616  0.436  0.197  6   VAL GGG C   
7716  O O   . VAL G 6   ? 3.935 2.397 2.430 0.607  0.415  0.197  6   VAL GGG O   
7717  C CB  . VAL G 6   ? 3.875 2.366 2.367 0.664  0.428  0.197  6   VAL GGG CB  
7718  C CG1 . VAL G 6   ? 3.847 2.269 2.334 0.607  0.435  0.186  6   VAL GGG CG1 
7719  C CG2 . VAL G 6   ? 3.863 2.384 2.326 0.730  0.436  0.206  6   VAL GGG CG2 
7720  N N   . PHE G 7   ? 4.064 2.355 2.452 0.568  0.452  0.189  7   PHE GGG N   
7721  C CA  . PHE G 7   ? 4.050 2.303 2.443 0.505  0.448  0.181  7   PHE GGG CA  
7722  C C   . PHE G 7   ? 3.934 2.223 2.406 0.438  0.432  0.168  7   PHE GGG C   
7723  O O   . PHE G 7   ? 3.932 2.196 2.390 0.433  0.442  0.165  7   PHE GGG O   
7724  C CB  . PHE G 7   ? 4.192 2.286 2.437 0.508  0.486  0.184  7   PHE GGG CB  
7725  C CG  . PHE G 7   ? 4.146 2.173 2.369 0.432  0.492  0.173  7   PHE GGG CG  
7726  C CD1 . PHE G 7   ? 4.228 2.210 2.436 0.385  0.502  0.164  7   PHE GGG CD1 
7727  C CD2 . PHE G 7   ? 4.079 2.073 2.274 0.413  0.493  0.174  7   PHE GGG CD2 
7728  C CE1 . PHE G 7   ? 4.233 2.158 2.415 0.313  0.508  0.154  7   PHE GGG CE1 
7729  C CE2 . PHE G 7   ? 4.185 2.117 2.352 0.341  0.500  0.164  7   PHE GGG CE2 
7730  C CZ  . PHE G 7   ? 4.218 2.119 2.378 0.291  0.507  0.154  7   PHE GGG CZ  
7731  N N   . PHE G 8   ? 3.752 2.104 2.307 0.390  0.407  0.162  8   PHE GGG N   
7732  C CA  . PHE G 8   ? 3.606 1.990 2.228 0.327  0.394  0.152  8   PHE GGG CA  
7733  C C   . PHE G 8   ? 3.532 1.895 2.154 0.271  0.390  0.147  8   PHE GGG C   
7734  O O   . PHE G 8   ? 3.423 1.829 2.080 0.275  0.375  0.150  8   PHE GGG O   
7735  C CB  . PHE G 8   ? 3.457 1.970 2.206 0.324  0.362  0.149  8   PHE GGG CB  
7736  C CG  . PHE G 8   ? 3.510 2.056 2.279 0.355  0.362  0.150  8   PHE GGG CG  
7737  C CD1 . PHE G 8   ? 3.653 2.189 2.375 0.417  0.373  0.158  8   PHE GGG CD1 
7738  C CD2 . PHE G 8   ? 3.300 1.895 2.139 0.324  0.349  0.143  8   PHE GGG CD2 
7739  C CE1 . PHE G 8   ? 3.633 2.204 2.376 0.443  0.372  0.158  8   PHE GGG CE1 
7740  C CE2 . PHE G 8   ? 3.155 1.779 2.014 0.350  0.349  0.142  8   PHE GGG CE2 
7741  C CZ  . PHE G 8   ? 3.371 1.982 2.181 0.408  0.360  0.150  8   PHE GGG CZ  
7742  N N   . ASP G 9   ? 3.624 1.929 2.210 0.218  0.403  0.140  9   ASP GGG N   
7743  C CA  . ASP G 9   ? 3.628 1.939 2.235 0.154  0.395  0.133  9   ASP GGG CA  
7744  C C   . ASP G 9   ? 3.448 1.857 2.163 0.113  0.371  0.127  9   ASP GGG C   
7745  O O   . ASP G 9   ? 3.528 1.932 2.243 0.098  0.379  0.122  9   ASP GGG O   
7746  C CB  . ASP G 9   ? 3.869 2.055 2.357 0.117  0.426  0.129  9   ASP GGG CB  
7747  C CG  . ASP G 9   ? 3.935 2.119 2.426 0.057  0.421  0.124  9   ASP GGG CG  
7748  O OD1 . ASP G 9   ? 3.975 2.263 2.570 0.037  0.391  0.123  9   ASP GGG OD1 
7749  O OD2 . ASP G 9   ? 4.045 2.120 2.427 0.030  0.447  0.121  9   ASP GGG OD2 
7750  N N   . ILE G 10  ? 3.214 1.712 2.018 0.097  0.344  0.127  10  ILE GGG N   
7751  C CA  . ILE G 10  ? 2.872 1.468 1.780 0.069  0.321  0.123  10  ILE GGG CA  
7752  C C   . ILE G 10  ? 2.842 1.440 1.752 0.004  0.320  0.118  10  ILE GGG C   
7753  O O   . ILE G 10  ? 3.011 1.575 1.883 -0.015 0.323  0.118  10  ILE GGG O   
7754  C CB  . ILE G 10  ? 2.839 1.532 1.842 0.095  0.292  0.127  10  ILE GGG CB  
7755  C CG1 . ILE G 10  ? 2.836 1.531 1.831 0.154  0.294  0.132  10  ILE GGG CG1 
7756  C CG2 . ILE G 10  ? 2.746 1.527 1.844 0.071  0.272  0.124  10  ILE GGG CG2 
7757  C CD1 . ILE G 10  ? 2.883 1.582 1.883 0.168  0.301  0.130  10  ILE GGG CD1 
7758  N N   . ALA G 11  ? 2.818 1.459 1.769 -0.029 0.316  0.113  11  ALA GGG N   
7759  C CA  . ALA G 11  ? 2.858 1.525 1.822 -0.091 0.313  0.109  11  ALA GGG CA  
7760  C C   . ALA G 11  ? 2.722 1.507 1.798 -0.099 0.287  0.110  11  ALA GGG C   
7761  O O   . ALA G 11  ? 2.711 1.538 1.838 -0.068 0.279  0.111  11  ALA GGG O   
7762  C CB  . ALA G 11  ? 3.061 1.660 1.946 -0.132 0.339  0.102  11  ALA GGG CB  
7763  N N   . VAL G 12  ? 2.707 1.545 1.817 -0.141 0.276  0.109  12  VAL GGG N   
7764  C CA  . VAL G 12  ? 2.679 1.626 1.886 -0.149 0.253  0.112  12  VAL GGG CA  
7765  C C   . VAL G 12  ? 2.853 1.831 2.055 -0.207 0.259  0.107  12  VAL GGG C   
7766  O O   . VAL G 12  ? 3.014 1.985 2.187 -0.249 0.261  0.106  12  VAL GGG O   
7767  C CB  . VAL G 12  ? 2.524 1.524 1.787 -0.138 0.230  0.117  12  VAL GGG CB  
7768  C CG1 . VAL G 12  ? 2.402 1.509 1.755 -0.145 0.210  0.120  12  VAL GGG CG1 
7769  C CG2 . VAL G 12  ? 2.633 1.612 1.901 -0.085 0.224  0.120  12  VAL GGG CG2 
7770  N N   . ASP G 13  ? 2.794 1.815 2.027 -0.211 0.261  0.106  13  ASP GGG N   
7771  C CA  . ASP G 13  ? 2.850 1.904 2.074 -0.266 0.269  0.102  13  ASP GGG CA  
7772  C C   . ASP G 13  ? 2.989 1.950 2.107 -0.313 0.294  0.095  13  ASP GGG C   
7773  O O   . ASP G 13  ? 3.048 2.035 2.149 -0.370 0.297  0.091  13  ASP GGG O   
7774  C CB  . ASP G 13  ? 2.800 1.966 2.096 -0.289 0.249  0.107  13  ASP GGG CB  
7775  C CG  . ASP G 13  ? 2.780 2.039 2.166 -0.256 0.232  0.113  13  ASP GGG CG  
7776  O OD1 . ASP G 13  ? 2.811 2.049 2.203 -0.221 0.237  0.112  13  ASP GGG OD1 
7777  O OD2 . ASP G 13  ? 2.812 2.164 2.258 -0.264 0.216  0.118  13  ASP GGG OD2 
7778  N N   . GLY G 14  ? 3.040 1.891 2.081 -0.288 0.313  0.093  14  GLY GGG N   
7779  C CA  . GLY G 14  ? 3.180 1.924 2.107 -0.327 0.339  0.086  14  GLY GGG CA  
7780  C C   . GLY G 14  ? 3.237 1.937 2.124 -0.337 0.338  0.087  14  GLY GGG C   
7781  O O   . GLY G 14  ? 3.426 2.025 2.207 -0.368 0.362  0.082  14  GLY GGG O   
7782  N N   . GLU G 15  ? 3.221 1.987 2.183 -0.309 0.313  0.094  15  GLU GGG N   
7783  C CA  . GLU G 15  ? 3.190 1.923 2.121 -0.318 0.310  0.095  15  GLU GGG CA  
7784  C C   . GLU G 15  ? 3.177 1.837 2.073 -0.258 0.315  0.099  15  GLU GGG C   
7785  O O   . GLU G 15  ? 3.201 1.902 2.158 -0.205 0.302  0.105  15  GLU GGG O   
7786  C CB  . GLU G 15  ? 3.095 1.940 2.122 -0.324 0.281  0.100  15  GLU GGG CB  
7787  C CG  . GLU G 15  ? 3.203 2.141 2.273 -0.377 0.274  0.098  15  GLU GGG CG  
7788  C CD  . GLU G 15  ? 3.348 2.346 2.450 -0.406 0.257  0.100  15  GLU GGG CD  
7789  O OE1 . GLU G 15  ? 3.446 2.378 2.495 -0.410 0.262  0.099  15  GLU GGG OE1 
7790  O OE2 . GLU G 15  ? 3.312 2.423 2.490 -0.421 0.239  0.104  15  GLU GGG OE2 
7791  N N   . PRO G 16  ? 3.201 1.756 1.998 -0.263 0.335  0.098  16  PRO GGG N   
7792  C CA  . PRO G 16  ? 3.190 1.679 1.948 -0.201 0.342  0.104  16  PRO GGG CA  
7793  C C   . PRO G 16  ? 3.124 1.693 1.971 -0.162 0.314  0.111  16  PRO GGG C   
7794  O O   . PRO G 16  ? 3.246 1.871 2.140 -0.187 0.296  0.111  16  PRO GGG O   
7795  C CB  . PRO G 16  ? 3.380 1.748 2.015 -0.224 0.367  0.101  16  PRO GGG CB  
7796  C CG  . PRO G 16  ? 3.351 1.753 1.992 -0.298 0.362  0.095  16  PRO GGG CG  
7797  C CD  . PRO G 16  ? 3.321 1.813 2.033 -0.326 0.352  0.092  16  PRO GGG CD  
7798  N N   . LEU G 17  ? 3.104 1.678 1.972 -0.101 0.310  0.116  17  LEU GGG N   
7799  C CA  . LEU G 17  ? 2.996 1.646 1.946 -0.064 0.284  0.122  17  LEU GGG CA  
7800  C C   . LEU G 17  ? 2.990 1.590 1.893 -0.013 0.292  0.128  17  LEU GGG C   
7801  O O   . LEU G 17  ? 3.082 1.710 2.010 -0.004 0.278  0.131  17  LEU GGG O   
7802  C CB  . LEU G 17  ? 2.850 1.586 1.890 -0.042 0.267  0.123  17  LEU GGG CB  
7803  C CG  . LEU G 17  ? 2.667 1.472 1.780 -0.006 0.243  0.128  17  LEU GGG CG  
7804  C CD1 . LEU G 17  ? 2.581 1.438 1.742 -0.038 0.225  0.129  17  LEU GGG CD1 
7805  C CD2 . LEU G 17  ? 2.604 1.477 1.790 0.017  0.230  0.128  17  LEU GGG CD2 
7806  N N   . GLY G 18  ? 3.092 1.635 1.937 0.027  0.310  0.129  18  GLY GGG N   
7807  C CA  . GLY G 18  ? 3.189 1.694 1.988 0.077  0.318  0.136  18  GLY GGG CA  
7808  C C   . GLY G 18  ? 3.347 1.815 2.102 0.129  0.334  0.140  18  GLY GGG C   
7809  O O   . GLY G 18  ? 3.379 1.850 2.142 0.127  0.339  0.137  18  GLY GGG O   
7810  N N   . ARG G 19  ? 3.414 1.852 2.121 0.179  0.342  0.147  19  ARG GGG N   
7811  C CA  . ARG G 19  ? 3.583 1.981 2.233 0.237  0.361  0.153  19  ARG GGG CA  
7812  C C   . ARG G 19  ? 3.428 1.922 2.147 0.286  0.341  0.160  19  ARG GGG C   
7813  O O   . ARG G 19  ? 3.367 1.902 2.114 0.294  0.327  0.163  19  ARG GGG O   
7814  C CB  . ARG G 19  ? 3.758 2.031 2.274 0.258  0.393  0.158  19  ARG GGG CB  
7815  C CG  . ARG G 19  ? 3.837 2.026 2.263 0.291  0.422  0.161  19  ARG GGG CG  
7816  C CD  . ARG G 19  ? 3.914 2.151 2.353 0.365  0.419  0.170  19  ARG GGG CD  
7817  N NE  . ARG G 19  ? 3.975 2.201 2.370 0.413  0.425  0.180  19  ARG GGG NE  
7818  C CZ  . ARG G 19  ? 4.062 2.329 2.453 0.481  0.426  0.190  19  ARG GGG CZ  
7819  N NH1 . ARG G 19  ? 4.100 2.417 2.524 0.509  0.422  0.191  19  ARG GGG NH1 
7820  N NH2 . ARG G 19  ? 4.189 2.451 2.541 0.523  0.432  0.200  19  ARG GGG NH2 
7821  N N   . VAL G 20  ? 3.412 1.942 2.155 0.316  0.339  0.160  20  VAL GGG N   
7822  C CA  . VAL G 20  ? 3.333 1.961 2.142 0.356  0.320  0.165  20  VAL GGG CA  
7823  C C   . VAL G 20  ? 3.487 2.081 2.222 0.420  0.341  0.173  20  VAL GGG C   
7824  O O   . VAL G 20  ? 3.539 2.068 2.216 0.431  0.362  0.173  20  VAL GGG O   
7825  C CB  . VAL G 20  ? 3.250 1.962 2.156 0.337  0.299  0.159  20  VAL GGG CB  
7826  C CG1 . VAL G 20  ? 3.248 2.063 2.222 0.366  0.278  0.162  20  VAL GGG CG1 
7827  C CG2 . VAL G 20  ? 3.143 1.873 2.105 0.276  0.285  0.151  20  VAL GGG CG2 
7828  N N   . SER G 21  ? 3.477 2.119 2.215 0.464  0.336  0.182  21  SER GGG N   
7829  C CA  . SER G 21  ? 3.575 2.202 2.246 0.532  0.354  0.192  21  SER GGG CA  
7830  C C   . SER G 21  ? 3.399 2.129 2.141 0.553  0.337  0.191  21  SER GGG C   
7831  O O   . SER G 21  ? 3.232 2.061 2.069 0.532  0.310  0.187  21  SER GGG O   
7832  C CB  . SER G 21  ? 3.739 2.372 2.372 0.572  0.358  0.202  21  SER GGG CB  
7833  O OG  . SER G 21  ? 3.939 2.495 2.528 0.542  0.367  0.200  21  SER GGG OG  
7834  N N   . PHE G 22  ? 3.609 2.309 2.297 0.595  0.356  0.196  22  PHE GGG N   
7835  C CA  . PHE G 22  ? 3.654 2.443 2.397 0.615  0.343  0.195  22  PHE GGG CA  
7836  C C   . PHE G 22  ? 3.916 2.715 2.594 0.690  0.359  0.208  22  PHE GGG C   
7837  O O   . PHE G 22  ? 4.144 2.843 2.717 0.725  0.389  0.216  22  PHE GGG O   
7838  C CB  . PHE G 22  ? 3.678 2.422 2.421 0.590  0.350  0.188  22  PHE GGG CB  
7839  C CG  . PHE G 22  ? 3.535 2.320 2.370 0.527  0.327  0.176  22  PHE GGG CG  
7840  C CD1 . PHE G 22  ? 3.458 2.196 2.296 0.476  0.327  0.170  22  PHE GGG CD1 
7841  C CD2 . PHE G 22  ? 3.375 2.243 2.287 0.519  0.309  0.171  22  PHE GGG CD2 
7842  C CE1 . PHE G 22  ? 3.340 2.118 2.258 0.423  0.307  0.161  22  PHE GGG CE1 
7843  C CE2 . PHE G 22  ? 3.253 2.152 2.242 0.466  0.291  0.161  22  PHE GGG CE2 
7844  C CZ  . PHE G 22  ? 3.267 2.124 2.260 0.421  0.290  0.157  22  PHE GGG CZ  
7845  N N   . GLU G 23  ? 4.098 3.019 2.834 0.715  0.341  0.211  23  GLU GGG N   
7846  C CA  . GLU G 23  ? 4.396 3.352 3.082 0.788  0.354  0.224  23  GLU GGG CA  
7847  C C   . GLU G 23  ? 4.436 3.482 3.183 0.789  0.340  0.219  23  GLU GGG C   
7848  O O   . GLU G 23  ? 4.519 3.651 3.360 0.747  0.313  0.210  23  GLU GGG O   
7849  C CB  . GLU G 23  ? 4.564 3.596 3.254 0.821  0.347  0.233  23  GLU GGG CB  
7850  C CG  . GLU G 23  ? 4.731 3.827 3.380 0.898  0.357  0.247  23  GLU GGG CG  
7851  C CD  . GLU G 23  ? 4.750 4.004 3.489 0.893  0.330  0.244  23  GLU GGG CD  
7852  O OE1 . GLU G 23  ? 4.695 3.999 3.524 0.831  0.305  0.232  23  GLU GGG OE1 
7853  O OE2 . GLU G 23  ? 4.889 4.217 3.606 0.950  0.335  0.255  23  GLU GGG OE2 
7854  N N   . LEU G 24  ? 4.292 3.313 2.980 0.838  0.358  0.226  24  LEU GGG N   
7855  C CA  . LEU G 24  ? 4.058 3.158 2.791 0.843  0.347  0.223  24  LEU GGG CA  
7856  C C   . LEU G 24  ? 4.034 3.238 2.755 0.907  0.347  0.235  24  LEU GGG C   
7857  O O   . LEU G 24  ? 4.391 3.559 3.026 0.971  0.370  0.249  24  LEU GGG O   
7858  C CB  . LEU G 24  ? 3.948 2.951 2.629 0.847  0.368  0.221  24  LEU GGG CB  
7859  C CG  . LEU G 24  ? 3.942 2.841 2.623 0.787  0.373  0.210  24  LEU GGG CG  
7860  C CD1 . LEU G 24  ? 3.931 2.746 2.555 0.798  0.394  0.209  24  LEU GGG CD1 
7861  C CD2 . LEU G 24  ? 3.814 2.782 2.607 0.722  0.343  0.196  24  LEU GGG CD2 
7862  N N   . PHE G 25  ? 3.876 3.210 2.681 0.889  0.322  0.229  25  PHE GGG N   
7863  C CA  . PHE G 25  ? 3.871 3.331 2.678 0.940  0.317  0.239  25  PHE GGG CA  
7864  C C   . PHE G 25  ? 3.947 3.412 2.720 0.980  0.329  0.243  25  PHE GGG C   
7865  O O   . PHE G 25  ? 3.873 3.435 2.700 0.968  0.313  0.237  25  PHE GGG O   
7866  C CB  . PHE G 25  ? 3.688 3.285 2.590 0.899  0.286  0.231  25  PHE GGG CB  
7867  C CG  . PHE G 25  ? 3.670 3.267 2.601 0.865  0.275  0.228  25  PHE GGG CG  
7868  C CD1 . PHE G 25  ? 3.790 3.438 2.691 0.907  0.279  0.240  25  PHE GGG CD1 
7869  C CD2 . PHE G 25  ? 3.471 3.030 2.459 0.796  0.260  0.215  25  PHE GGG CD2 
7870  C CE1 . PHE G 25  ? 3.749 3.402 2.676 0.879  0.269  0.239  25  PHE GGG CE1 
7871  C CE2 . PHE G 25  ? 3.472 3.036 2.485 0.769  0.250  0.213  25  PHE GGG CE2 
7872  C CZ  . PHE G 25  ? 3.568 3.177 2.550 0.809  0.254  0.225  25  PHE GGG CZ  
7873  N N   . ALA G 26  ? 4.130 3.482 2.805 1.027  0.359  0.253  26  ALA GGG N   
7874  C CA  . ALA G 26  ? 4.180 3.506 2.804 1.069  0.376  0.258  26  ALA GGG CA  
7875  C C   . ALA G 26  ? 4.216 3.673 2.834 1.132  0.374  0.270  26  ALA GGG C   
7876  O O   . ALA G 26  ? 4.118 3.592 2.717 1.161  0.380  0.273  26  ALA GGG O   
7877  C CB  . ALA G 26  ? 4.170 3.333 2.678 1.105  0.411  0.266  26  ALA GGG CB  
7878  N N   . ASP G 27  ? 4.313 3.866 2.943 1.154  0.365  0.278  27  ASP GGG N   
7879  C CA  . ASP G 27  ? 4.504 4.203 3.135 1.210  0.361  0.290  27  ASP GGG CA  
7880  C C   . ASP G 27  ? 4.507 4.337 3.231 1.165  0.333  0.278  27  ASP GGG C   
7881  O O   . ASP G 27  ? 4.694 4.633 3.415 1.206  0.331  0.285  27  ASP GGG O   
7882  C CB  . ASP G 27  ? 4.545 4.320 3.173 1.236  0.358  0.301  27  ASP GGG CB  
7883  C CG  . ASP G 27  ? 4.404 4.237 3.128 1.158  0.328  0.286  27  ASP GGG CG  
7884  O OD1 . ASP G 27  ? 4.384 4.136 3.148 1.090  0.320  0.270  27  ASP GGG OD1 
7885  O OD2 . ASP G 27  ? 4.358 4.320 3.117 1.163  0.314  0.290  27  ASP GGG OD2 
7886  N N   . LYS G 28  ? 4.487 4.309 3.291 1.083  0.312  0.259  28  LYS GGG N   
7887  C CA  . LYS G 28  ? 4.200 4.117 3.082 1.034  0.288  0.246  28  LYS GGG CA  
7888  C C   . LYS G 28  ? 4.108 3.933 2.995 1.005  0.292  0.235  28  LYS GGG C   
7889  O O   . LYS G 28  ? 4.057 3.946 2.969 1.000  0.285  0.230  28  LYS GGG O   
7890  C CB  . LYS G 28  ? 3.988 3.965 2.954 0.963  0.261  0.232  28  LYS GGG CB  
7891  C CG  . LYS G 28  ? 4.000 4.072 2.970 0.981  0.255  0.241  28  LYS GGG CG  
7892  C CD  . LYS G 28  ? 3.933 4.161 2.899 1.025  0.251  0.250  28  LYS GGG CD  
7893  C CE  . LYS G 28  ? 3.797 4.151 2.794 1.018  0.237  0.253  28  LYS GGG CE  
7894  N NZ  . LYS G 28  ? 3.815 4.099 2.770 1.046  0.250  0.263  28  LYS GGG NZ  
7895  N N   . VAL G 29  ? 3.933 3.615 2.796 0.984  0.304  0.231  29  VAL GGG N   
7896  C CA  . VAL G 29  ? 3.753 3.354 2.628 0.949  0.307  0.220  29  VAL GGG CA  
7897  C C   . VAL G 29  ? 3.819 3.269 2.605 0.980  0.337  0.227  29  VAL GGG C   
7898  O O   . VAL G 29  ? 3.845 3.195 2.621 0.947  0.343  0.222  29  VAL GGG O   
7899  C CB  . VAL G 29  ? 3.567 3.164 2.525 0.867  0.285  0.203  29  VAL GGG CB  
7900  C CG1 . VAL G 29  ? 3.473 2.956 2.430 0.832  0.293  0.194  29  VAL GGG CG1 
7901  C CG2 . VAL G 29  ? 3.472 3.197 2.503 0.836  0.260  0.194  29  VAL GGG CG2 
7902  N N   . PRO G 30  ? 3.838 3.268 2.547 1.047  0.359  0.240  30  PRO GGG N   
7903  C CA  . PRO G 30  ? 3.917 3.192 2.527 1.076  0.391  0.247  30  PRO GGG CA  
7904  C C   . PRO G 30  ? 3.914 3.090 2.531 1.029  0.396  0.234  30  PRO GGG C   
7905  O O   . PRO G 30  ? 4.004 3.053 2.574 1.011  0.413  0.232  30  PRO GGG O   
7906  C CB  . PRO G 30  ? 3.948 3.244 2.478 1.164  0.411  0.264  30  PRO GGG CB  
7907  C CG  . PRO G 30  ? 3.911 3.374 2.511 1.167  0.387  0.262  30  PRO GGG CG  
7908  C CD  . PRO G 30  ? 3.858 3.409 2.555 1.106  0.358  0.251  30  PRO GGG CD  
7909  N N   . LYS G 31  ? 3.868 3.102 2.539 1.008  0.382  0.225  31  LYS GGG N   
7910  C CA  . LYS G 31  ? 3.854 3.000 2.528 0.970  0.389  0.215  31  LYS GGG CA  
7911  C C   . LYS G 31  ? 3.849 2.939 2.569 0.899  0.380  0.202  31  LYS GGG C   
7912  O O   . LYS G 31  ? 3.920 2.894 2.599 0.879  0.397  0.199  31  LYS GGG O   
7913  C CB  . LYS G 31  ? 3.783 3.014 2.515 0.958  0.373  0.208  31  LYS GGG CB  
7914  C CG  . LYS G 31  ? 3.836 3.141 2.530 1.026  0.380  0.220  31  LYS GGG CG  
7915  C CD  . LYS G 31  ? 3.760 3.170 2.523 1.005  0.359  0.211  31  LYS GGG CD  
7916  C CE  . LYS G 31  ? 3.785 3.122 2.534 0.993  0.370  0.204  31  LYS GGG CE  
7917  N NZ  . LYS G 31  ? 3.613 3.052 2.415 0.983  0.353  0.198  31  LYS GGG NZ  
7918  N N   . THR G 32  ? 3.754 2.927 2.556 0.860  0.354  0.196  32  THR GGG N   
7919  C CA  . THR G 32  ? 3.663 2.794 2.512 0.795  0.344  0.185  32  THR GGG CA  
7920  C C   . THR G 32  ? 3.717 2.759 2.507 0.800  0.359  0.191  32  THR GGG C   
7921  O O   . THR G 32  ? 3.738 2.693 2.519 0.760  0.366  0.185  32  THR GGG O   
7922  C CB  . THR G 32  ? 3.540 2.777 2.486 0.754  0.313  0.177  32  THR GGG CB  
7923  O OG1 . THR G 32  ? 3.500 2.815 2.489 0.750  0.300  0.171  32  THR GGG OG1 
7924  C CG2 . THR G 32  ? 3.479 2.671 2.471 0.691  0.304  0.166  32  THR GGG CG2 
7925  N N   . ALA G 33  ? 3.727 2.793 2.474 0.848  0.365  0.203  33  ALA GGG N   
7926  C CA  . ALA G 33  ? 3.857 2.832 2.536 0.858  0.383  0.209  33  ALA GGG CA  
7927  C C   . ALA G 33  ? 4.069 2.902 2.649 0.873  0.415  0.212  33  ALA GGG C   
7928  O O   . ALA G 33  ? 4.057 2.790 2.602 0.839  0.427  0.208  33  ALA GGG O   
7929  C CB  . ALA G 33  ? 3.915 2.945 2.558 0.917  0.387  0.223  33  ALA GGG CB  
7930  N N   . GLU G 34  ? 4.121 2.946 2.652 0.921  0.431  0.218  34  GLU GGG N   
7931  C CA  . GLU G 34  ? 4.323 3.007 2.750 0.936  0.463  0.221  34  GLU GGG CA  
7932  C C   . GLU G 34  ? 4.310 2.937 2.772 0.865  0.460  0.206  34  GLU GGG C   
7933  O O   . GLU G 34  ? 4.454 2.958 2.848 0.844  0.482  0.204  34  GLU GGG O   
7934  C CB  . GLU G 34  ? 4.292 2.989 2.669 1.001  0.478  0.231  34  GLU GGG CB  
7935  C CG  . GLU G 34  ? 4.516 3.102 2.752 1.068  0.515  0.246  34  GLU GGG CG  
7936  C CD  . GLU G 34  ? 4.607 3.222 2.809 1.115  0.518  0.259  34  GLU GGG CD  
7937  O OE1 . GLU G 34  ? 4.595 3.353 2.873 1.127  0.493  0.261  34  GLU GGG OE1 
7938  O OE2 . GLU G 34  ? 4.688 3.182 2.784 1.139  0.546  0.267  34  GLU GGG OE2 
7939  N N   . ASN G 35  ? 4.340 3.059 2.906 0.828  0.434  0.196  35  ASN GGG N   
7940  C CA  . ASN G 35  ? 4.321 3.009 2.934 0.762  0.428  0.182  35  ASN GGG CA  
7941  C C   . ASN G 35  ? 4.264 2.906 2.886 0.712  0.425  0.177  35  ASN GGG C   
7942  O O   . ASN G 35  ? 4.306 2.855 2.890 0.677  0.441  0.172  35  ASN GGG O   
7943  C CB  . ASN G 35  ? 4.284 3.087 3.007 0.737  0.399  0.174  35  ASN GGG CB  
7944  C CG  . ASN G 35  ? 4.316 3.097 3.090 0.675  0.392  0.161  35  ASN GGG CG  
7945  O OD1 . ASN G 35  ? 4.338 3.027 3.071 0.647  0.408  0.158  35  ASN GGG OD1 
7946  N ND2 . ASN G 35  ? 4.286 3.154 3.146 0.654  0.370  0.154  35  ASN GGG ND2 
7947  N N   . PHE G 36  ? 4.122 2.835 2.795 0.707  0.406  0.179  36  PHE GGG N   
7948  C CA  . PHE G 36  ? 4.107 2.789 2.794 0.662  0.401  0.174  36  PHE GGG CA  
7949  C C   . PHE G 36  ? 4.165 2.722 2.737 0.676  0.431  0.181  36  PHE GGG C   
7950  O O   . PHE G 36  ? 4.132 2.617 2.686 0.628  0.438  0.174  36  PHE GGG O   
7951  C CB  . PHE G 36  ? 4.021 2.805 2.777 0.661  0.375  0.176  36  PHE GGG CB  
7952  C CG  . PHE G 36  ? 3.808 2.586 2.604 0.609  0.363  0.170  36  PHE GGG CG  
7953  C CD1 . PHE G 36  ? 3.575 2.406 2.464 0.557  0.340  0.160  36  PHE GGG CD1 
7954  C CD2 . PHE G 36  ? 3.880 2.598 2.619 0.613  0.375  0.175  36  PHE GGG CD2 
7955  C CE1 . PHE G 36  ? 3.505 2.335 2.430 0.512  0.329  0.155  36  PHE GGG CE1 
7956  C CE2 . PHE G 36  ? 3.783 2.499 2.559 0.565  0.363  0.170  36  PHE GGG CE2 
7957  C CZ  . PHE G 36  ? 3.577 2.353 2.448 0.514  0.339  0.160  36  PHE GGG CZ  
7958  N N   . ARG G 37  ? 4.273 2.802 2.763 0.742  0.450  0.193  37  ARG GGG N   
7959  C CA  . ARG G 37  ? 4.384 2.781 2.751 0.762  0.482  0.200  37  ARG GGG CA  
7960  C C   . ARG G 37  ? 4.441 2.717 2.740 0.731  0.506  0.193  37  ARG GGG C   
7961  O O   . ARG G 37  ? 4.354 2.535 2.601 0.691  0.521  0.189  37  ARG GGG O   
7962  C CB  . ARG G 37  ? 4.336 2.727 2.622 0.847  0.500  0.216  37  ARG GGG CB  
7963  C CG  . ARG G 37  ? 4.283 2.514 2.418 0.878  0.541  0.224  37  ARG GGG CG  
7964  C CD  . ARG G 37  ? 4.372 2.601 2.429 0.969  0.560  0.240  37  ARG GGG CD  
7965  N NE  . ARG G 37  ? 4.613 2.681 2.525 0.995  0.602  0.245  37  ARG GGG NE  
7966  C CZ  . ARG G 37  ? 4.725 2.744 2.601 0.999  0.616  0.243  37  ARG GGG CZ  
7967  N NH1 . ARG G 37  ? 4.661 2.778 2.639 0.977  0.592  0.235  37  ARG GGG NH1 
7968  N NH2 . ARG G 37  ? 4.823 2.685 2.555 1.025  0.656  0.248  37  ARG GGG NH2 
7969  N N   . ALA G 38  ? 4.552 2.831 2.849 0.746  0.512  0.192  38  ALA GGG N   
7970  C CA  . ALA G 38  ? 4.844 3.006 3.069 0.719  0.537  0.187  38  ALA GGG CA  
7971  C C   . ALA G 38  ? 4.774 2.943 3.067 0.635  0.524  0.172  38  ALA GGG C   
7972  O O   . ALA G 38  ? 4.972 3.035 3.197 0.595  0.545  0.167  38  ALA GGG O   
7973  C CB  . ALA G 38  ? 5.181 3.353 3.393 0.756  0.545  0.189  38  ALA GGG CB  
7974  N N   . LEU G 39  ? 4.404 2.696 2.825 0.607  0.490  0.166  39  LEU GGG N   
7975  C CA  . LEU G 39  ? 4.186 2.495 2.674 0.533  0.476  0.154  39  LEU GGG CA  
7976  C C   . LEU G 39  ? 4.075 2.343 2.540 0.499  0.478  0.153  39  LEU GGG C   
7977  O O   . LEU G 39  ? 4.034 2.271 2.505 0.438  0.480  0.144  39  LEU GGG O   
7978  C CB  . LEU G 39  ? 4.056 2.499 2.677 0.518  0.441  0.149  39  LEU GGG CB  
7979  C CG  . LEU G 39  ? 3.927 2.413 2.580 0.536  0.437  0.147  39  LEU GGG CG  
7980  C CD1 . LEU G 39  ? 3.709 2.319 2.483 0.522  0.404  0.143  39  LEU GGG CD1 
7981  C CD2 . LEU G 39  ? 3.989 2.408 2.611 0.503  0.455  0.140  39  LEU GGG CD2 
7982  N N   . SER G 40  ? 4.077 2.349 2.517 0.536  0.477  0.161  40  SER GGG N   
7983  C CA  . SER G 40  ? 4.104 2.334 2.518 0.507  0.480  0.161  40  SER GGG CA  
7984  C C   . SER G 40  ? 4.288 2.365 2.564 0.499  0.517  0.162  40  SER GGG C   
7985  O O   . SER G 40  ? 4.391 2.418 2.642 0.450  0.522  0.156  40  SER GGG O   
7986  C CB  . SER G 40  ? 4.106 2.394 2.537 0.550  0.467  0.170  40  SER GGG CB  
7987  O OG  . SER G 40  ? 4.062 2.486 2.616 0.546  0.433  0.168  40  SER GGG OG  
7988  N N   . THR G 41  ? 4.360 2.358 2.538 0.548  0.544  0.168  41  THR GGG N   
7989  C CA  . THR G 41  ? 4.440 2.279 2.475 0.539  0.583  0.169  41  THR GGG CA  
7990  C C   . THR G 41  ? 4.491 2.271 2.501 0.486  0.597  0.158  41  THR GGG C   
7991  O O   . THR G 41  ? 4.583 2.242 2.493 0.448  0.623  0.153  41  THR GGG O   
7992  C CB  . THR G 41  ? 4.630 2.393 2.549 0.622  0.611  0.183  41  THR GGG CB  
7993  O OG1 . THR G 41  ? 4.747 2.544 2.682 0.659  0.611  0.185  41  THR GGG OG1 
7994  C CG2 . THR G 41  ? 4.584 2.415 2.526 0.677  0.598  0.194  41  THR GGG CG2 
7995  N N   . GLY G 42  ? 4.451 2.317 2.550 0.481  0.579  0.154  42  GLY GGG N   
7996  C CA  . GLY G 42  ? 4.465 2.294 2.554 0.435  0.590  0.144  42  GLY GGG CA  
7997  C C   . GLY G 42  ? 4.532 2.237 2.489 0.470  0.627  0.148  42  GLY GGG C   
7998  O O   . GLY G 42  ? 4.616 2.253 2.527 0.429  0.645  0.141  42  GLY GGG O   
7999  N N   . GLU G 43  ? 4.576 2.252 2.470 0.549  0.639  0.162  43  GLU GGG N   
8000  C CA  . GLU G 43  ? 4.744 2.287 2.493 0.594  0.678  0.169  43  GLU GGG CA  
8001  C C   . GLU G 43  ? 4.707 2.266 2.471 0.606  0.681  0.167  43  GLU GGG C   
8002  O O   . GLU G 43  ? 4.798 2.231 2.439 0.621  0.716  0.169  43  GLU GGG O   
8003  C CB  . GLU G 43  ? 4.840 2.377 2.534 0.682  0.686  0.185  43  GLU GGG CB  
8004  C CG  . GLU G 43  ? 4.789 2.474 2.588 0.737  0.658  0.192  43  GLU GGG CG  
8005  C CD  . GLU G 43  ? 4.851 2.570 2.626 0.814  0.657  0.208  43  GLU GGG CD  
8006  O OE1 . GLU G 43  ? 5.044 2.669 2.693 0.879  0.689  0.220  43  GLU GGG OE1 
8007  O OE2 . GLU G 43  ? 4.750 2.592 2.631 0.811  0.626  0.208  43  GLU GGG OE2 
8008  N N   . LYS G 44  ? 4.571 2.271 2.473 0.599  0.648  0.163  44  LYS GGG N   
8009  C CA  . LYS G 44  ? 4.599 2.319 2.523 0.604  0.649  0.160  44  LYS GGG CA  
8010  C C   . LYS G 44  ? 4.626 2.328 2.575 0.524  0.650  0.145  44  LYS GGG C   
8011  O O   . LYS G 44  ? 4.590 2.302 2.553 0.523  0.653  0.142  44  LYS GGG O   
8012  C CB  . LYS G 44  ? 4.444 2.322 2.499 0.635  0.613  0.162  44  LYS GGG CB  
8013  C CG  . LYS G 44  ? 4.333 2.256 2.376 0.714  0.609  0.176  44  LYS GGG CG  
8014  C CD  . LYS G 44  ? 4.429 2.272 2.356 0.785  0.639  0.188  44  LYS GGG CD  
8015  C CE  . LYS G 44  ? 4.394 2.279 2.298 0.860  0.637  0.203  44  LYS GGG CE  
8016  N NZ  . LYS G 44  ? 4.554 2.336 2.317 0.935  0.673  0.217  44  LYS GGG NZ  
8017  N N   . GLY G 45  ? 4.646 2.330 2.602 0.458  0.648  0.137  45  GLY GGG N   
8018  C CA  . GLY G 45  ? 4.690 2.365 2.665 0.381  0.651  0.124  45  GLY GGG CA  
8019  C C   . GLY G 45  ? 4.663 2.483 2.793 0.339  0.612  0.117  45  GLY GGG C   
8020  O O   . GLY G 45  ? 4.615 2.453 2.778 0.276  0.610  0.107  45  GLY GGG O   
8021  N N   . PHE G 46  ? 4.699 2.626 2.922 0.375  0.583  0.123  46  PHE GGG N   
8022  C CA  . PHE G 46  ? 4.542 2.603 2.905 0.345  0.547  0.118  46  PHE GGG CA  
8023  C C   . PHE G 46  ? 4.416 2.538 2.824 0.377  0.526  0.125  46  PHE GGG C   
8024  O O   . PHE G 46  ? 4.475 2.599 2.857 0.440  0.528  0.134  46  PHE GGG O   
8025  C CB  . PHE G 46  ? 4.444 2.589 2.889 0.359  0.531  0.116  46  PHE GGG CB  
8026  C CG  . PHE G 46  ? 4.424 2.580 2.852 0.433  0.532  0.125  46  PHE GGG CG  
8027  C CD1 . PHE G 46  ? 4.537 2.608 2.872 0.466  0.560  0.128  46  PHE GGG CD1 
8028  C CD2 . PHE G 46  ? 4.309 2.566 2.815 0.469  0.506  0.130  46  PHE GGG CD2 
8029  C CE1 . PHE G 46  ? 4.561 2.654 2.883 0.535  0.560  0.137  46  PHE GGG CE1 
8030  C CE2 . PHE G 46  ? 4.247 2.528 2.739 0.533  0.506  0.138  46  PHE GGG CE2 
8031  C CZ  . PHE G 46  ? 4.360 2.563 2.763 0.568  0.532  0.142  46  PHE GGG CZ  
8032  N N   . GLY G 47  ? 4.206 2.381 2.678 0.335  0.506  0.121  47  GLY GGG N   
8033  C CA  . GLY G 47  ? 4.154 2.383 2.665 0.360  0.488  0.127  47  GLY GGG CA  
8034  C C   . GLY G 47  ? 3.925 2.226 2.524 0.309  0.463  0.122  47  GLY GGG C   
8035  O O   . GLY G 47  ? 3.821 2.161 2.475 0.262  0.454  0.114  47  GLY GGG O   
8036  N N   . TYR G 48  ? 3.816 2.135 2.423 0.322  0.453  0.126  48  TYR GGG N   
8037  C CA  . TYR G 48  ? 3.521 1.924 2.220 0.287  0.426  0.123  48  TYR GGG CA  
8038  C C   . TYR G 48  ? 3.478 1.839 2.152 0.224  0.433  0.118  48  TYR GGG C   
8039  O O   . TYR G 48  ? 3.386 1.820 2.141 0.188  0.411  0.114  48  TYR GGG O   
8040  C CB  . TYR G 48  ? 3.445 1.893 2.169 0.324  0.410  0.130  48  TYR GGG CB  
8041  C CG  . TYR G 48  ? 3.395 1.917 2.168 0.374  0.396  0.135  48  TYR GGG CG  
8042  C CD1 . TYR G 48  ? 3.237 1.833 2.091 0.364  0.380  0.130  48  TYR GGG CD1 
8043  C CD2 . TYR G 48  ? 3.498 2.026 2.240 0.428  0.398  0.143  48  TYR GGG CD2 
8044  C CE1 . TYR G 48  ? 3.174 1.838 2.070 0.404  0.367  0.132  48  TYR GGG CE1 
8045  C CE2 . TYR G 48  ? 3.442 2.050 2.231 0.469  0.384  0.147  48  TYR GGG CE2 
8046  C CZ  . TYR G 48  ? 3.249 1.923 2.114 0.454  0.368  0.141  48  TYR GGG CZ  
8047  O OH  . TYR G 48  ? 3.290 2.041 2.196 0.489  0.355  0.143  48  TYR GGG OH  
8048  N N   . LYS G 49  ? 3.588 1.833 2.148 0.211  0.463  0.117  49  LYS GGG N   
8049  C CA  . LYS G 49  ? 3.599 1.806 2.130 0.147  0.470  0.111  49  LYS GGG CA  
8050  C C   . LYS G 49  ? 3.572 1.849 2.178 0.092  0.457  0.103  49  LYS GGG C   
8051  O O   . LYS G 49  ? 3.754 2.025 2.356 0.089  0.466  0.099  49  LYS GGG O   
8052  C CB  . LYS G 49  ? 3.758 1.817 2.141 0.136  0.508  0.109  49  LYS GGG CB  
8053  C CG  . LYS G 49  ? 3.981 1.959 2.273 0.203  0.527  0.119  49  LYS GGG CG  
8054  C CD  . LYS G 49  ? 4.201 2.062 2.378 0.183  0.551  0.119  49  LYS GGG CD  
8055  C CE  . LYS G 49  ? 4.337 2.117 2.418 0.255  0.571  0.130  49  LYS GGG CE  
8056  N NZ  . LYS G 49  ? 4.372 2.024 2.328 0.237  0.598  0.130  49  LYS GGG NZ  
8057  N N   . GLY G 50  ? 3.568 1.915 2.242 0.053  0.437  0.100  50  GLY GGG N   
8058  C CA  . GLY G 50  ? 3.494 1.920 2.243 0.006  0.425  0.095  50  GLY GGG CA  
8059  C C   . GLY G 50  ? 3.391 1.932 2.258 0.031  0.396  0.097  50  GLY GGG C   
8060  O O   . GLY G 50  ? 3.347 1.960 2.280 -0.001 0.385  0.094  50  GLY GGG O   
8061  N N   . SER G 51  ? 3.531 2.094 2.425 0.087  0.385  0.103  51  SER GGG N   
8062  C CA  . SER G 51  ? 3.428 2.090 2.424 0.107  0.360  0.104  51  SER GGG CA  
8063  C C   . SER G 51  ? 3.298 2.036 2.369 0.093  0.335  0.106  51  SER GGG C   
8064  O O   . SER G 51  ? 3.347 2.062 2.393 0.078  0.335  0.107  51  SER GGG O   
8065  C CB  . SER G 51  ? 3.443 2.103 2.434 0.167  0.359  0.108  51  SER GGG CB  
8066  O OG  . SER G 51  ? 3.363 2.114 2.446 0.185  0.333  0.110  51  SER GGG OG  
8067  N N   . CYS G 52  ? 3.078 1.901 2.237 0.098  0.314  0.106  52  CYS GGG N   
8068  C CA  . CYS G 52  ? 2.913 1.807 2.142 0.085  0.291  0.108  52  CYS GGG CA  
8069  C C   . CYS G 52  ? 2.739 1.676 2.015 0.125  0.273  0.111  52  CYS GGG C   
8070  O O   . CYS G 52  ? 2.695 1.628 1.966 0.160  0.275  0.112  52  CYS GGG O   
8071  C CB  . CYS G 52  ? 2.871 1.830 2.162 0.056  0.282  0.106  52  CYS GGG CB  
8072  S SG  . CYS G 52  ? 3.362 2.300 2.612 -0.004 0.299  0.102  52  CYS GGG SG  
8073  N N   . PHE G 53  ? 2.583 1.563 1.902 0.118  0.255  0.114  53  PHE GGG N   
8074  C CA  . PHE G 53  ? 2.431 1.465 1.806 0.143  0.235  0.116  53  PHE GGG CA  
8075  C C   . PHE G 53  ? 2.395 1.490 1.837 0.131  0.222  0.115  53  PHE GGG C   
8076  O O   . PHE G 53  ? 2.356 1.483 1.829 0.104  0.214  0.117  53  PHE GGG O   
8077  C CB  . PHE G 53  ? 2.367 1.408 1.745 0.143  0.224  0.119  53  PHE GGG CB  
8078  C CG  . PHE G 53  ? 2.433 1.427 1.752 0.171  0.234  0.121  53  PHE GGG CG  
8079  C CD1 . PHE G 53  ? 2.419 1.437 1.749 0.207  0.227  0.123  53  PHE GGG CD1 
8080  C CD2 . PHE G 53  ? 2.536 1.460 1.783 0.161  0.253  0.121  53  PHE GGG CD2 
8081  C CE1 . PHE G 53  ? 2.485 1.470 1.760 0.237  0.237  0.126  53  PHE GGG CE1 
8082  C CE2 . PHE G 53  ? 2.533 1.409 1.718 0.192  0.264  0.125  53  PHE GGG CE2 
8083  C CZ  . PHE G 53  ? 2.422 1.333 1.623 0.233  0.256  0.128  53  PHE GGG CZ  
8084  N N   . HIS G 54  ? 2.408 1.519 1.870 0.151  0.222  0.114  54  HIS GGG N   
8085  C CA  . HIS G 54  ? 2.304 1.463 1.819 0.145  0.214  0.113  54  HIS GGG CA  
8086  C C   . HIS G 54  ? 2.185 1.391 1.752 0.156  0.195  0.115  54  HIS GGG C   
8087  O O   . HIS G 54  ? 2.088 1.333 1.696 0.148  0.187  0.117  54  HIS GGG O   
8088  C CB  . HIS G 54  ? 2.356 1.502 1.860 0.159  0.225  0.110  54  HIS GGG CB  
8089  C CG  . HIS G 54  ? 2.411 1.550 1.907 0.193  0.223  0.109  54  HIS GGG CG  
8090  N ND1 . HIS G 54  ? 2.522 1.619 1.966 0.212  0.234  0.109  54  HIS GGG ND1 
8091  C CD2 . HIS G 54  ? 2.392 1.563 1.922 0.210  0.213  0.108  54  HIS GGG CD2 
8092  C CE1 . HIS G 54  ? 2.515 1.629 1.966 0.239  0.228  0.108  54  HIS GGG CE1 
8093  N NE2 . HIS G 54  ? 2.422 1.579 1.924 0.236  0.216  0.107  54  HIS GGG NE2 
8094  N N   . ARG G 55  ? 2.156 1.358 1.716 0.175  0.188  0.115  55  ARG GGG N   
8095  C CA  . ARG G 55  ? 2.012 1.251 1.611 0.181  0.171  0.116  55  ARG GGG CA  
8096  C C   . ARG G 55  ? 2.029 1.265 1.618 0.179  0.164  0.118  55  ARG GGG C   
8097  O O   . ARG G 55  ? 1.992 1.211 1.549 0.195  0.167  0.117  55  ARG GGG O   
8098  C CB  . ARG G 55  ? 1.894 1.140 1.496 0.204  0.169  0.113  55  ARG GGG CB  
8099  C CG  . ARG G 55  ? 1.789 1.064 1.429 0.204  0.158  0.112  55  ARG GGG CG  
8100  C CD  . ARG G 55  ? 1.768 1.045 1.402 0.221  0.158  0.107  55  ARG GGG CD  
8101  N NE  . ARG G 55  ? 1.737 1.033 1.389 0.220  0.146  0.106  55  ARG GGG NE  
8102  C CZ  . ARG G 55  ? 1.965 1.271 1.607 0.228  0.142  0.101  55  ARG GGG CZ  
8103  N NH1 . ARG G 55  ? 2.047 1.351 1.665 0.242  0.150  0.099  55  ARG GGG NH1 
8104  N NH2 . ARG G 55  ? 2.049 1.367 1.701 0.220  0.133  0.099  55  ARG GGG NH2 
8105  N N   . ILE G 56  ? 2.019 1.274 1.632 0.161  0.154  0.121  56  ILE GGG N   
8106  C CA  . ILE G 56  ? 1.984 1.243 1.595 0.159  0.144  0.123  56  ILE GGG CA  
8107  C C   . ILE G 56  ? 1.875 1.168 1.526 0.157  0.129  0.124  56  ILE GGG C   
8108  O O   . ILE G 56  ? 1.864 1.176 1.543 0.146  0.124  0.127  56  ILE GGG O   
8109  C CB  . ILE G 56  ? 1.972 1.214 1.564 0.138  0.148  0.125  56  ILE GGG CB  
8110  C CG1 . ILE G 56  ? 2.058 1.251 1.596 0.139  0.167  0.124  56  ILE GGG CG1 
8111  C CG2 . ILE G 56  ? 1.938 1.186 1.531 0.136  0.138  0.127  56  ILE GGG CG2 
8112  C CD1 . ILE G 56  ? 2.041 1.206 1.549 0.114  0.173  0.125  56  ILE GGG CD1 
8113  N N   . ILE G 57  ? 1.873 1.175 1.524 0.169  0.121  0.122  57  ILE GGG N   
8114  C CA  . ILE G 57  ? 1.889 1.213 1.566 0.166  0.108  0.122  57  ILE GGG CA  
8115  C C   . ILE G 57  ? 1.865 1.198 1.538 0.161  0.100  0.123  57  ILE GGG C   
8116  O O   . ILE G 57  ? 1.832 1.168 1.485 0.171  0.100  0.121  57  ILE GGG O   
8117  C CB  . ILE G 57  ? 1.898 1.229 1.578 0.177  0.108  0.117  57  ILE GGG CB  
8118  C CG1 . ILE G 57  ? 1.858 1.180 1.542 0.182  0.117  0.117  57  ILE GGG CG1 
8119  C CG2 . ILE G 57  ? 1.875 1.216 1.569 0.170  0.097  0.117  57  ILE GGG CG2 
8120  C CD1 . ILE G 57  ? 1.921 1.244 1.600 0.194  0.119  0.111  57  ILE GGG CD1 
8121  N N   . PRO G 58  ? 1.860 1.199 1.548 0.147  0.092  0.127  58  PRO GGG N   
8122  C CA  . PRO G 58  ? 1.845 1.189 1.527 0.142  0.084  0.128  58  PRO GGG CA  
8123  C C   . PRO G 58  ? 1.894 1.255 1.576 0.146  0.077  0.124  58  PRO GGG C   
8124  O O   . PRO G 58  ? 1.847 1.212 1.541 0.144  0.073  0.122  58  PRO GGG O   
8125  C CB  . PRO G 58  ? 1.861 1.211 1.563 0.127  0.077  0.133  58  PRO GGG CB  
8126  C CG  . PRO G 58  ? 1.922 1.278 1.645 0.128  0.077  0.134  58  PRO GGG CG  
8127  C CD  . PRO G 58  ? 1.915 1.262 1.628 0.137  0.089  0.131  58  PRO GGG CD  
8128  N N   . GLY G 59  ? 1.901 1.272 1.565 0.151  0.076  0.124  59  GLY GGG N   
8129  C CA  . GLY G 59  ? 1.896 1.293 1.558 0.151  0.069  0.120  59  GLY GGG CA  
8130  C C   . GLY G 59  ? 1.897 1.306 1.547 0.164  0.075  0.115  59  GLY GGG C   
8131  O O   . GLY G 59  ? 1.900 1.337 1.548 0.160  0.070  0.110  59  GLY GGG O   
8132  N N   . PHE G 60  ? 1.933 1.324 1.575 0.178  0.085  0.115  60  PHE GGG N   
8133  C CA  . PHE G 60  ? 1.931 1.332 1.562 0.192  0.092  0.111  60  PHE GGG CA  
8134  C C   . PHE G 60  ? 1.950 1.339 1.551 0.214  0.104  0.114  60  PHE GGG C   
8135  O O   . PHE G 60  ? 2.004 1.417 1.585 0.230  0.105  0.115  60  PHE GGG O   
8136  C CB  . PHE G 60  ? 2.013 1.397 1.658 0.187  0.094  0.109  60  PHE GGG CB  
8137  C CG  . PHE G 60  ? 2.074 1.469 1.709 0.197  0.099  0.104  60  PHE GGG CG  
8138  C CD1 . PHE G 60  ? 2.122 1.554 1.744 0.200  0.095  0.100  60  PHE GGG CD1 
8139  C CD2 . PHE G 60  ? 2.044 1.419 1.682 0.203  0.106  0.102  60  PHE GGG CD2 
8140  C CE1 . PHE G 60  ? 2.225 1.672 1.837 0.207  0.098  0.095  60  PHE GGG CE1 
8141  C CE2 . PHE G 60  ? 2.116 1.500 1.743 0.211  0.110  0.097  60  PHE GGG CE2 
8142  C CZ  . PHE G 60  ? 2.208 1.629 1.823 0.213  0.106  0.093  60  PHE GGG CZ  
8143  N N   . MET G 61  ? 1.972 1.325 1.567 0.216  0.114  0.116  61  MET GGG N   
8144  C CA  . MET G 61  ? 2.072 1.400 1.630 0.237  0.128  0.118  61  MET GGG CA  
8145  C C   . MET G 61  ? 2.112 1.397 1.663 0.226  0.138  0.120  61  MET GGG C   
8146  O O   . MET G 61  ? 2.086 1.372 1.668 0.207  0.133  0.119  61  MET GGG O   
8147  C CB  . MET G 61  ? 2.130 1.471 1.676 0.256  0.134  0.115  61  MET GGG CB  
8148  C CG  . MET G 61  ? 2.135 1.475 1.707 0.246  0.132  0.110  61  MET GGG CG  
8149  S SD  . MET G 61  ? 2.211 1.506 1.771 0.247  0.148  0.111  61  MET GGG SD  
8150  C CE  . MET G 61  ? 2.167 1.470 1.771 0.228  0.140  0.109  61  MET GGG CE  
8151  N N   . CYS G 62  ? 2.172 1.420 1.680 0.240  0.153  0.122  62  CYS GGG N   
8152  C CA  . CYS G 62  ? 2.205 1.409 1.695 0.228  0.166  0.122  62  CYS GGG CA  
8153  C C   . CYS G 62  ? 2.249 1.427 1.704 0.249  0.181  0.121  62  CYS GGG C   
8154  O O   . CYS G 62  ? 2.272 1.442 1.689 0.277  0.188  0.123  62  CYS GGG O   
8155  C CB  . CYS G 62  ? 2.243 1.409 1.698 0.218  0.173  0.126  62  CYS GGG CB  
8156  S SG  . CYS G 62  ? 2.235 1.429 1.725 0.194  0.156  0.128  62  CYS GGG SG  
8157  N N   . GLN G 63  ? 2.243 1.412 1.709 0.238  0.186  0.119  63  GLN GGG N   
8158  C CA  . GLN G 63  ? 2.265 1.414 1.704 0.257  0.199  0.117  63  GLN GGG CA  
8159  C C   . GLN G 63  ? 2.346 1.445 1.754 0.242  0.216  0.117  63  GLN GGG C   
8160  O O   . GLN G 63  ? 2.328 1.430 1.758 0.212  0.214  0.116  63  GLN GGG O   
8161  C CB  . GLN G 63  ? 2.249 1.437 1.731 0.259  0.191  0.113  63  GLN GGG CB  
8162  C CG  . GLN G 63  ? 2.253 1.429 1.711 0.282  0.202  0.111  63  GLN GGG CG  
8163  C CD  . GLN G 63  ? 2.239 1.447 1.736 0.280  0.194  0.107  63  GLN GGG CD  
8164  O OE1 . GLN G 63  ? 2.084 1.323 1.621 0.266  0.180  0.106  63  GLN GGG OE1 
8165  N NE2 . GLN G 63  ? 2.312 1.508 1.792 0.295  0.204  0.105  63  GLN GGG NE2 
8166  N N   . GLY G 64  ? 2.495 1.549 1.848 0.262  0.234  0.117  64  GLY GGG N   
8167  C CA  . GLY G 64  ? 2.636 1.634 1.946 0.246  0.253  0.116  64  GLY GGG CA  
8168  C C   . GLY G 64  ? 2.643 1.604 1.904 0.276  0.270  0.116  64  GLY GGG C   
8169  O O   . GLY G 64  ? 2.572 1.565 1.847 0.304  0.264  0.116  64  GLY GGG O   
8170  N N   . GLY G 65  ? 2.842 1.734 2.041 0.266  0.291  0.115  65  GLY GGG N   
8171  C CA  . GLY G 65  ? 2.939 1.785 2.080 0.297  0.310  0.116  65  GLY GGG CA  
8172  C C   . GLY G 65  ? 2.964 1.809 2.117 0.288  0.316  0.112  65  GLY GGG C   
8173  O O   . GLY G 65  ? 3.055 1.862 2.160 0.314  0.332  0.113  65  GLY GGG O   
8174  N N   . ASP G 66  ? 2.778 1.665 1.990 0.255  0.306  0.108  66  ASP GGG N   
8175  C CA  . ASP G 66  ? 2.865 1.752 2.087 0.247  0.313  0.105  66  ASP GGG CA  
8176  C C   . ASP G 66  ? 3.013 1.840 2.181 0.214  0.334  0.102  66  ASP GGG C   
8177  O O   . ASP G 66  ? 2.984 1.833 2.180 0.175  0.331  0.100  66  ASP GGG O   
8178  C CB  . ASP G 66  ? 2.781 1.742 2.087 0.232  0.294  0.103  66  ASP GGG CB  
8179  C CG  . ASP G 66  ? 2.830 1.796 2.148 0.225  0.301  0.100  66  ASP GGG CG  
8180  O OD1 . ASP G 66  ? 2.923 1.837 2.187 0.228  0.321  0.098  66  ASP GGG OD1 
8181  O OD2 . ASP G 66  ? 2.824 1.845 2.203 0.218  0.289  0.099  66  ASP GGG OD2 
8182  N N   . PHE G 67  ? 3.129 1.879 2.215 0.231  0.356  0.103  67  PHE GGG N   
8183  C CA  . PHE G 67  ? 3.175 1.850 2.189 0.200  0.380  0.101  67  PHE GGG CA  
8184  C C   . PHE G 67  ? 3.219 1.885 2.228 0.189  0.392  0.096  67  PHE GGG C   
8185  O O   . PHE G 67  ? 3.354 1.957 2.300 0.160  0.413  0.093  67  PHE GGG O   
8186  C CB  . PHE G 67  ? 3.265 1.847 2.178 0.224  0.401  0.104  67  PHE GGG CB  
8187  C CG  . PHE G 67  ? 3.366 1.928 2.247 0.281  0.408  0.109  67  PHE GGG CG  
8188  C CD1 . PHE G 67  ? 3.580 2.090 2.408 0.293  0.428  0.107  67  PHE GGG CD1 
8189  C CD2 . PHE G 67  ? 3.336 1.935 2.234 0.322  0.394  0.114  67  PHE GGG CD2 
8190  C CE1 . PHE G 67  ? 3.725 2.223 2.522 0.348  0.434  0.112  67  PHE GGG CE1 
8191  C CE2 . PHE G 67  ? 3.441 2.034 2.310 0.375  0.400  0.119  67  PHE GGG CE2 
8192  C CZ  . PHE G 67  ? 3.673 2.217 2.492 0.389  0.420  0.118  67  PHE GGG CZ  
8193  N N   . THR G 68  ? 3.242 1.967 2.312 0.209  0.379  0.096  68  THR GGG N   
8194  C CA  . THR G 68  ? 3.291 2.012 2.360 0.199  0.390  0.092  68  THR GGG CA  
8195  C C   . THR G 68  ? 3.164 1.962 2.313 0.169  0.376  0.090  68  THR GGG C   
8196  O O   . THR G 68  ? 3.192 1.985 2.333 0.142  0.388  0.086  68  THR GGG O   
8197  C CB  . THR G 68  ? 3.346 2.069 2.414 0.246  0.390  0.094  68  THR GGG CB  
8198  O OG1 . THR G 68  ? 3.563 2.244 2.577 0.285  0.396  0.098  68  THR GGG OG1 
8199  C CG2 . THR G 68  ? 3.438 2.122 2.470 0.240  0.410  0.090  68  THR GGG CG2 
8200  N N   . ARG G 69  ? 3.052 1.921 2.273 0.173  0.352  0.092  69  ARG GGG N   
8201  C CA  . ARG G 69  ? 2.982 1.924 2.276 0.152  0.340  0.092  69  ARG GGG CA  
8202  C C   . ARG G 69  ? 2.950 1.938 2.285 0.131  0.324  0.094  69  ARG GGG C   
8203  O O   . ARG G 69  ? 2.924 1.971 2.309 0.111  0.316  0.095  69  ARG GGG O   
8204  C CB  . ARG G 69  ? 2.963 1.950 2.309 0.183  0.327  0.092  69  ARG GGG CB  
8205  C CG  . ARG G 69  ? 3.097 2.050 2.410 0.201  0.343  0.089  69  ARG GGG CG  
8206  C CD  . ARG G 69  ? 3.203 2.154 2.508 0.170  0.357  0.087  69  ARG GGG CD  
8207  N NE  . ARG G 69  ? 3.330 2.210 2.564 0.172  0.380  0.084  69  ARG GGG NE  
8208  C CZ  . ARG G 69  ? 3.303 2.162 2.520 0.204  0.386  0.083  69  ARG GGG CZ  
8209  N NH1 . ARG G 69  ? 3.263 2.169 2.532 0.232  0.371  0.084  69  ARG GGG NH1 
8210  N NH2 . ARG G 69  ? 3.294 2.082 2.439 0.205  0.409  0.081  69  ARG GGG NH2 
8211  N N   . HIS G 70  ? 2.969 1.932 2.281 0.137  0.320  0.096  70  HIS GGG N   
8212  C CA  . HIS G 70  ? 2.856 1.848 2.192 0.112  0.308  0.098  70  HIS GGG CA  
8213  C C   . HIS G 70  ? 2.777 1.847 2.193 0.120  0.285  0.101  70  HIS GGG C   
8214  O O   . HIS G 70  ? 2.733 1.842 2.179 0.097  0.275  0.103  70  HIS GGG O   
8215  C CB  . HIS G 70  ? 2.928 1.908 2.235 0.064  0.321  0.096  70  HIS GGG CB  
8216  C CG  . HIS G 70  ? 3.054 1.941 2.269 0.054  0.342  0.093  70  HIS GGG CG  
8217  N ND1 . HIS G 70  ? 3.226 2.054 2.377 0.039  0.366  0.089  70  HIS GGG ND1 
8218  C CD2 . HIS G 70  ? 3.081 1.921 2.252 0.060  0.344  0.095  70  HIS GGG CD2 
8219  C CE1 . HIS G 70  ? 3.290 2.031 2.356 0.036  0.383  0.089  70  HIS GGG CE1 
8220  N NE2 . HIS G 70  ? 3.325 2.073 2.402 0.050  0.370  0.092  70  HIS GGG NE2 
8221  N N   . ASN G 71  ? 2.704 1.796 2.152 0.152  0.276  0.101  71  ASN GGG N   
8222  C CA  . ASN G 71  ? 2.494 1.647 2.006 0.160  0.258  0.104  71  ASN GGG CA  
8223  C C   . ASN G 71  ? 2.349 1.506 1.874 0.192  0.247  0.103  71  ASN GGG C   
8224  O O   . ASN G 71  ? 2.305 1.502 1.874 0.200  0.233  0.105  71  ASN GGG O   
8225  C CB  . ASN G 71  ? 2.534 1.723 2.079 0.155  0.261  0.104  71  ASN GGG CB  
8226  C CG  . ASN G 71  ? 2.570 1.735 2.097 0.176  0.271  0.100  71  ASN GGG CG  
8227  O OD1 . ASN G 71  ? 2.667 1.782 2.147 0.188  0.280  0.098  71  ASN GGG OD1 
8228  N ND2 . ASN G 71  ? 2.432 1.631 1.992 0.182  0.270  0.101  71  ASN GGG ND2 
8229  N N   . GLY G 72  ? 2.354 1.473 1.837 0.212  0.253  0.102  72  GLY GGG N   
8230  C CA  . GLY G 72  ? 2.353 1.483 1.843 0.239  0.243  0.101  72  GLY GGG CA  
8231  C C   . GLY G 72  ? 2.456 1.581 1.937 0.261  0.249  0.098  72  GLY GGG C   
8232  O O   . GLY G 72  ? 2.478 1.617 1.961 0.282  0.242  0.097  72  GLY GGG O   
8233  N N   . THR G 73  ? 2.509 1.617 1.980 0.254  0.263  0.097  73  THR GGG N   
8234  C CA  . THR G 73  ? 2.398 1.500 1.862 0.273  0.269  0.094  73  THR GGG CA  
8235  C C   . THR G 73  ? 2.425 1.475 1.827 0.286  0.288  0.093  73  THR GGG C   
8236  O O   . THR G 73  ? 2.468 1.511 1.859 0.306  0.294  0.091  73  THR GGG O   
8237  C CB  . THR G 73  ? 2.388 1.511 1.884 0.260  0.271  0.093  73  THR GGG CB  
8238  O OG1 . THR G 73  ? 2.456 1.621 2.000 0.249  0.257  0.095  73  THR GGG OG1 
8239  C CG2 . THR G 73  ? 2.433 1.561 1.934 0.281  0.272  0.090  73  THR GGG CG2 
8240  N N   . GLY G 74  ? 2.535 1.545 1.893 0.279  0.297  0.095  74  GLY GGG N   
8241  C CA  . GLY G 74  ? 2.752 1.700 2.041 0.291  0.318  0.095  74  GLY GGG CA  
8242  C C   . GLY G 74  ? 2.731 1.648 1.971 0.318  0.322  0.099  74  GLY GGG C   
8243  O O   . GLY G 74  ? 2.479 1.437 1.743 0.336  0.307  0.101  74  GLY GGG O   
8244  N N   . GLY G 75  ? 2.854 1.700 2.019 0.323  0.344  0.101  75  GLY GGG N   
8245  C CA  . GLY G 75  ? 3.001 1.814 2.109 0.358  0.351  0.106  75  GLY GGG CA  
8246  C C   . GLY G 75  ? 3.047 1.836 2.110 0.398  0.363  0.108  75  GLY GGG C   
8247  O O   . GLY G 75  ? 2.939 1.751 2.028 0.401  0.362  0.104  75  GLY GGG O   
8248  N N   . LYS G 76  ? 3.159 1.903 2.152 0.432  0.377  0.114  76  LYS GGG N   
8249  C CA  . LYS G 76  ? 3.229 1.955 2.174 0.479  0.389  0.118  76  LYS GGG CA  
8250  C C   . LYS G 76  ? 3.357 2.072 2.250 0.522  0.394  0.126  76  LYS GGG C   
8251  O O   . LYS G 76  ? 3.474 2.155 2.338 0.513  0.398  0.129  76  LYS GGG O   
8252  C CB  . LYS G 76  ? 3.341 1.980 2.217 0.472  0.416  0.116  76  LYS GGG CB  
8253  C CG  . LYS G 76  ? 3.644 2.231 2.438 0.523  0.437  0.122  76  LYS GGG CG  
8254  C CD  . LYS G 76  ? 3.776 2.271 2.503 0.507  0.463  0.119  76  LYS GGG CD  
8255  C CE  . LYS G 76  ? 3.889 2.308 2.566 0.468  0.478  0.118  76  LYS GGG CE  
8256  N NZ  . LYS G 76  ? 4.093 2.411 2.686 0.451  0.508  0.115  76  LYS GGG NZ  
8257  N N   . SER G 77  ? 3.470 2.217 2.349 0.569  0.394  0.131  77  SER GGG N   
8258  C CA  . SER G 77  ? 3.696 2.448 2.524 0.621  0.399  0.141  77  SER GGG CA  
8259  C C   . SER G 77  ? 3.961 2.607 2.677 0.655  0.432  0.148  77  SER GGG C   
8260  O O   . SER G 77  ? 4.238 2.811 2.919 0.635  0.449  0.144  77  SER GGG O   
8261  C CB  . SER G 77  ? 3.743 2.593 2.613 0.653  0.383  0.143  77  SER GGG CB  
8262  O OG  . SER G 77  ? 3.999 2.847 2.869 0.660  0.389  0.139  77  SER GGG OG  
8263  N N   . ILE G 78  ? 4.115 2.750 2.770 0.708  0.442  0.159  78  ILE GGG N   
8264  C CA  . ILE G 78  ? 4.035 2.563 2.573 0.746  0.475  0.166  78  ILE GGG CA  
8265  C C   . ILE G 78  ? 4.259 2.803 2.789 0.776  0.480  0.167  78  ILE GGG C   
8266  O O   . ILE G 78  ? 4.403 2.858 2.838 0.808  0.508  0.173  78  ILE GGG O   
8267  C CB  . ILE G 78  ? 3.783 2.291 2.249 0.802  0.487  0.180  78  ILE GGG CB  
8268  C CG1 . ILE G 78  ? 3.809 2.438 2.315 0.852  0.470  0.187  78  ILE GGG CG1 
8269  C CG2 . ILE G 78  ? 3.986 2.479 2.464 0.769  0.481  0.178  78  ILE GGG CG2 
8270  C CD1 . ILE G 78  ? 3.800 2.443 2.257 0.906  0.475  0.200  78  ILE GGG CD1 
8271  N N   . TYR G 79  ? 4.078 2.731 2.701 0.766  0.454  0.162  79  TYR GGG N   
8272  C CA  . TYR G 79  ? 4.069 2.762 2.708 0.785  0.452  0.160  79  TYR GGG CA  
8273  C C   . TYR G 79  ? 4.119 2.800 2.815 0.724  0.446  0.148  79  TYR GGG C   
8274  O O   . TYR G 79  ? 4.335 3.031 3.086 0.676  0.432  0.141  79  TYR GGG O   
8275  C CB  . TYR G 79  ? 4.031 2.856 2.738 0.805  0.427  0.162  79  TYR GGG CB  
8276  C CG  . TYR G 79  ? 4.153 3.020 2.830 0.852  0.426  0.173  79  TYR GGG CG  
8277  C CD1 . TYR G 79  ? 4.377 3.200 2.957 0.918  0.449  0.187  79  TYR GGG CD1 
8278  C CD2 . TYR G 79  ? 4.121 3.072 2.864 0.833  0.402  0.172  79  TYR GGG CD2 
8279  C CE1 . TYR G 79  ? 4.379 3.248 2.932 0.965  0.449  0.199  79  TYR GGG CE1 
8280  C CE2 . TYR G 79  ? 4.126 3.121 2.843 0.876  0.401  0.182  79  TYR GGG CE2 
8281  C CZ  . TYR G 79  ? 4.223 3.182 2.847 0.942  0.425  0.196  79  TYR GGG CZ  
8282  O OH  . TYR G 79  ? 4.260 3.271 2.861 0.987  0.424  0.208  79  TYR GGG OH  
8283  N N   . GLY G 80  ? 4.085 2.741 2.765 0.728  0.456  0.145  80  GLY GGG N   
8284  C CA  . GLY G 80  ? 3.898 2.536 2.621 0.674  0.454  0.134  80  GLY GGG CA  
8285  C C   . GLY G 80  ? 3.688 2.423 2.522 0.636  0.423  0.126  80  GLY GGG C   
8286  O O   . GLY G 80  ? 3.612 2.425 2.493 0.649  0.407  0.125  80  GLY GGG O   
8287  N N   . GLU G 81  ? 3.580 2.308 2.449 0.590  0.416  0.121  81  GLU GGG N   
8288  C CA  . GLU G 81  ? 3.456 2.263 2.421 0.555  0.389  0.115  81  GLU GGG CA  
8289  C C   . GLU G 81  ? 3.475 2.368 2.483 0.572  0.367  0.117  81  GLU GGG C   
8290  O O   . GLU G 81  ? 3.532 2.430 2.535 0.574  0.363  0.121  81  GLU GGG O   
8291  C CB  . GLU G 81  ? 3.424 2.259 2.439 0.535  0.383  0.108  81  GLU GGG CB  
8292  C CG  . GLU G 81  ? 3.409 2.258 2.485 0.485  0.373  0.101  81  GLU GGG CG  
8293  C CD  . GLU G 81  ? 3.376 2.240 2.487 0.470  0.373  0.095  81  GLU GGG CD  
8294  O OE1 . GLU G 81  ? 3.361 2.208 2.441 0.494  0.383  0.095  81  GLU GGG OE1 
8295  O OE2 . GLU G 81  ? 3.317 2.211 2.486 0.437  0.361  0.091  81  GLU GGG OE2 
8296  N N   . LYS G 82  ? 3.473 2.435 2.522 0.582  0.354  0.114  82  LYS GGG N   
8297  C CA  . LYS G 82  ? 3.467 2.516 2.557 0.589  0.332  0.115  82  LYS GGG CA  
8298  C C   . LYS G 82  ? 3.579 2.645 2.620 0.636  0.338  0.125  82  LYS GGG C   
8299  O O   . LYS G 82  ? 3.768 2.783 2.738 0.674  0.358  0.132  82  LYS GGG O   
8300  C CB  . LYS G 82  ? 3.413 2.526 2.542 0.590  0.320  0.109  82  LYS GGG CB  
8301  C CG  . LYS G 82  ? 3.454 2.530 2.582 0.581  0.331  0.104  82  LYS GGG CG  
8302  C CD  . LYS G 82  ? 3.406 2.470 2.586 0.535  0.324  0.097  82  LYS GGG CD  
8303  C CE  . LYS G 82  ? 3.411 2.443 2.587 0.529  0.335  0.093  82  LYS GGG CE  
8304  N NZ  . LYS G 82  ? 3.386 2.408 2.608 0.488  0.331  0.087  82  LYS GGG NZ  
8305  N N   . PHE G 83  ? 3.760 2.897 2.835 0.635  0.320  0.125  83  PHE GGG N   
8306  C CA  . PHE G 83  ? 3.854 3.035 2.893 0.681  0.321  0.135  83  PHE GGG CA  
8307  C C   . PHE G 83  ? 3.751 3.043 2.848 0.670  0.297  0.131  83  PHE GGG C   
8308  O O   . PHE G 83  ? 3.682 3.001 2.839 0.626  0.280  0.123  83  PHE GGG O   
8309  C CB  . PHE G 83  ? 3.939 3.069 2.938 0.690  0.331  0.142  83  PHE GGG CB  
8310  C CG  . PHE G 83  ? 4.003 3.200 2.994 0.721  0.323  0.150  83  PHE GGG CG  
8311  C CD1 . PHE G 83  ? 4.155 3.394 3.102 0.777  0.330  0.160  83  PHE GGG CD1 
8312  C CD2 . PHE G 83  ? 3.944 3.166 2.972 0.695  0.309  0.149  83  PHE GGG CD2 
8313  C CE1 . PHE G 83  ? 4.197 3.508 3.139 0.805  0.324  0.168  83  PHE GGG CE1 
8314  C CE2 . PHE G 83  ? 4.016 3.302 3.038 0.720  0.303  0.156  83  PHE GGG CE2 
8315  C CZ  . PHE G 83  ? 4.112 3.446 3.092 0.776  0.310  0.165  83  PHE GGG CZ  
8316  N N   . GLU G 84  ? 3.617 2.977 2.691 0.712  0.296  0.138  84  GLU GGG N   
8317  C CA  . GLU G 84  ? 3.436 2.908 2.557 0.699  0.275  0.133  84  GLU GGG CA  
8318  C C   . GLU G 84  ? 3.390 2.904 2.538 0.682  0.261  0.134  84  GLU GGG C   
8319  O O   . GLU G 84  ? 3.433 2.902 2.553 0.696  0.270  0.141  84  GLU GGG O   
8320  C CB  . GLU G 84  ? 3.384 2.929 2.474 0.745  0.278  0.140  84  GLU GGG CB  
8321  C CG  . GLU G 84  ? 3.457 3.027 2.495 0.801  0.287  0.154  84  GLU GGG CG  
8322  C CD  . GLU G 84  ? 3.430 3.088 2.445 0.845  0.288  0.160  84  GLU GGG CD  
8323  O OE1 . GLU G 84  ? 3.433 3.100 2.459 0.834  0.287  0.154  84  GLU GGG OE1 
8324  O OE2 . GLU G 84  ? 3.369 3.086 2.352 0.890  0.291  0.172  84  GLU GGG OE2 
8325  N N   . ASP G 85  ? 3.253 2.851 2.453 0.650  0.240  0.126  85  ASP GGG N   
8326  C CA  . ASP G 85  ? 3.206 2.861 2.424 0.640  0.228  0.128  85  ASP GGG CA  
8327  C C   . ASP G 85  ? 3.223 2.950 2.402 0.693  0.232  0.140  85  ASP GGG C   
8328  O O   . ASP G 85  ? 3.215 3.027 2.394 0.706  0.227  0.140  85  ASP GGG O   
8329  C CB  . ASP G 85  ? 3.189 2.906 2.465 0.588  0.206  0.116  85  ASP GGG CB  
8330  C CG  . ASP G 85  ? 3.189 2.835 2.501 0.542  0.203  0.107  85  ASP GGG CG  
8331  O OD1 . ASP G 85  ? 3.224 2.784 2.520 0.548  0.216  0.109  85  ASP GGG OD1 
8332  O OD2 . ASP G 85  ? 3.143 2.821 2.493 0.500  0.188  0.098  85  ASP GGG OD2 
8333  N N   . GLU G 86  ? 3.297 2.995 2.440 0.725  0.243  0.151  86  GLU GGG N   
8334  C CA  . GLU G 86  ? 3.327 3.080 2.420 0.787  0.252  0.165  86  GLU GGG CA  
8335  C C   . GLU G 86  ? 3.379 3.272 2.503 0.782  0.233  0.165  86  GLU GGG C   
8336  O O   . GLU G 86  ? 3.380 3.364 2.490 0.813  0.233  0.169  86  GLU GGG O   
8337  C CB  . GLU G 86  ? 3.401 3.075 2.437 0.824  0.270  0.177  86  GLU GGG CB  
8338  C CG  . GLU G 86  ? 3.401 3.121 2.374 0.898  0.284  0.193  86  GLU GGG CG  
8339  C CD  . GLU G 86  ? 3.485 3.103 2.383 0.941  0.308  0.206  86  GLU GGG CD  
8340  O OE1 . GLU G 86  ? 3.588 3.112 2.489 0.907  0.311  0.201  86  GLU GGG OE1 
8341  O OE2 . GLU G 86  ? 3.555 3.188 2.387 1.009  0.324  0.221  86  GLU GGG OE2 
8342  N N   . ASN G 87  ? 3.353 3.269 2.518 0.741  0.219  0.159  87  ASN GGG N   
8343  C CA  . ASN G 87  ? 3.283 3.329 2.481 0.724  0.201  0.157  87  ASN GGG CA  
8344  C C   . ASN G 87  ? 3.336 3.369 2.582 0.666  0.186  0.147  87  ASN GGG C   
8345  O O   . ASN G 87  ? 3.393 3.323 2.644 0.647  0.190  0.145  87  ASN GGG O   
8346  C CB  . ASN G 87  ? 3.266 3.389 2.423 0.784  0.207  0.173  87  ASN GGG CB  
8347  C CG  . ASN G 87  ? 3.357 3.412 2.485 0.809  0.218  0.183  87  ASN GGG CG  
8348  O OD1 . ASN G 87  ? 3.365 3.396 2.525 0.768  0.209  0.177  87  ASN GGG OD1 
8349  N ND2 . ASN G 87  ? 3.458 3.475 2.518 0.877  0.240  0.198  87  ASN GGG ND2 
8350  N N   . PHE G 88  ? 3.293 3.433 2.570 0.636  0.168  0.142  88  PHE GGG N   
8351  C CA  . PHE G 88  ? 3.243 3.384 2.560 0.582  0.154  0.134  88  PHE GGG CA  
8352  C C   . PHE G 88  ? 3.217 3.454 2.533 0.595  0.148  0.141  88  PHE GGG C   
8353  O O   . PHE G 88  ? 3.142 3.427 2.490 0.548  0.133  0.133  88  PHE GGG O   
8354  C CB  . PHE G 88  ? 3.210 3.379 2.566 0.520  0.139  0.117  88  PHE GGG CB  
8355  C CG  . PHE G 88  ? 3.274 3.352 2.636 0.503  0.144  0.110  88  PHE GGG CG  
8356  C CD1 . PHE G 88  ? 3.221 3.184 2.577 0.514  0.155  0.113  88  PHE GGG CD1 
8357  C CD2 . PHE G 88  ? 3.268 3.377 2.641 0.474  0.138  0.099  88  PHE GGG CD2 
8358  C CE1 . PHE G 88  ? 3.115 3.003 2.478 0.499  0.160  0.106  88  PHE GGG CE1 
8359  C CE2 . PHE G 88  ? 3.152 3.179 2.531 0.461  0.143  0.093  88  PHE GGG CE2 
8360  C CZ  . PHE G 88  ? 3.070 2.990 2.445 0.474  0.154  0.097  88  PHE GGG CZ  
8361  N N   . ILE G 89  ? 3.245 3.509 2.518 0.659  0.160  0.156  89  ILE GGG N   
8362  C CA  . ILE G 89  ? 3.215 3.572 2.482 0.679  0.156  0.165  89  ILE GGG CA  
8363  C C   . ILE G 89  ? 3.144 3.444 2.430 0.650  0.151  0.163  89  ILE GGG C   
8364  O O   . ILE G 89  ? 3.074 3.449 2.388 0.618  0.138  0.159  89  ILE GGG O   
8365  C CB  . ILE G 89  ? 3.209 3.581 2.416 0.763  0.175  0.184  89  ILE GGG CB  
8366  C CG1 . ILE G 89  ? 3.256 3.674 2.441 0.796  0.181  0.187  89  ILE GGG CG1 
8367  C CG2 . ILE G 89  ? 3.165 3.647 2.366 0.788  0.171  0.194  89  ILE GGG CG2 
8368  C CD1 . ILE G 89  ? 3.281 3.696 2.399 0.884  0.203  0.207  89  ILE GGG CD1 
8369  N N   . LEU G 90  ? 3.156 3.325 2.427 0.656  0.163  0.165  90  LEU GGG N   
8370  C CA  . LEU G 90  ? 3.036 3.144 2.320 0.632  0.160  0.164  90  LEU GGG CA  
8371  C C   . LEU G 90  ? 2.946 3.037 2.285 0.560  0.143  0.148  90  LEU GGG C   
8372  O O   . LEU G 90  ? 2.959 3.035 2.317 0.531  0.139  0.138  90  LEU GGG O   
8373  C CB  . LEU G 90  ? 2.965 2.940 2.209 0.660  0.178  0.170  90  LEU GGG CB  
8374  C CG  . LEU G 90  ? 2.934 2.901 2.122 0.720  0.194  0.186  90  LEU GGG CG  
8375  C CD1 . LEU G 90  ? 2.970 2.794 2.110 0.738  0.214  0.191  90  LEU GGG CD1 
8376  C CD2 . LEU G 90  ? 2.719 2.742 1.927 0.705  0.183  0.188  90  LEU GGG CD2 
8377  N N   . LYS G 91  ? 2.869 2.961 2.228 0.533  0.134  0.147  91  LYS GGG N   
8378  C CA  . LYS G 91  ? 2.810 2.887 2.213 0.469  0.119  0.134  91  LYS GGG CA  
8379  C C   . LYS G 91  ? 2.931 2.904 2.340 0.455  0.121  0.134  91  LYS GGG C   
8380  O O   . LYS G 91  ? 2.953 2.891 2.335 0.488  0.131  0.144  91  LYS GGG O   
8381  C CB  . LYS G 91  ? 2.758 2.942 2.181 0.440  0.104  0.130  91  LYS GGG CB  
8382  C CG  . LYS G 91  ? 2.648 2.852 2.103 0.377  0.090  0.115  91  LYS GGG CG  
8383  C CD  . LYS G 91  ? 2.570 2.847 2.021 0.374  0.089  0.109  91  LYS GGG CD  
8384  C CE  . LYS G 91  ? 2.539 2.850 2.010 0.309  0.075  0.094  91  LYS GGG CE  
8385  N NZ  . LYS G 91  ? 2.646 3.048 2.108 0.302  0.073  0.089  91  LYS GGG NZ  
8386  N N   . HIS G 92  ? 3.097 3.021 2.538 0.408  0.113  0.124  92  HIS GGG N   
8387  C CA  . HIS G 92  ? 3.121 2.962 2.576 0.386  0.112  0.123  92  HIS GGG CA  
8388  C C   . HIS G 92  ? 3.157 3.042 2.629 0.364  0.101  0.123  92  HIS GGG C   
8389  O O   . HIS G 92  ? 3.121 3.023 2.620 0.320  0.088  0.114  92  HIS GGG O   
8390  C CB  . HIS G 92  ? 3.080 2.864 2.562 0.350  0.109  0.113  92  HIS GGG CB  
8391  C CG  . HIS G 92  ? 3.111 2.852 2.579 0.368  0.120  0.113  92  HIS GGG CG  
8392  N ND1 . HIS G 92  ? 3.195 2.981 2.659 0.374  0.120  0.109  92  HIS GGG ND1 
8393  C CD2 . HIS G 92  ? 3.058 2.717 2.514 0.381  0.132  0.116  92  HIS GGG CD2 
8394  C CE1 . HIS G 92  ? 3.159 2.889 2.609 0.391  0.132  0.110  92  HIS GGG CE1 
8395  N NE2 . HIS G 92  ? 3.087 2.741 2.532 0.395  0.139  0.114  92  HIS GGG NE2 
8396  N N   . THR G 93  ? 3.095 2.993 2.544 0.396  0.106  0.133  93  THR GGG N   
8397  C CA  . THR G 93  ? 2.978 2.937 2.437 0.382  0.096  0.134  93  THR GGG CA  
8398  C C   . THR G 93  ? 2.828 2.727 2.303 0.356  0.092  0.133  93  THR GGG C   
8399  O O   . THR G 93  ? 2.762 2.707 2.250 0.336  0.082  0.132  93  THR GGG O   
8400  C CB  . THR G 93  ? 3.079 3.096 2.503 0.433  0.105  0.146  93  THR GGG CB  
8401  O OG1 . THR G 93  ? 3.146 3.081 2.539 0.465  0.118  0.155  93  THR GGG OG1 
8402  C CG2 . THR G 93  ? 3.067 3.143 2.471 0.468  0.112  0.149  93  THR GGG CG2 
8403  N N   . GLY G 94  ? 2.689 2.493 2.162 0.354  0.098  0.134  94  GLY GGG N   
8404  C CA  . GLY G 94  ? 2.614 2.366 2.100 0.332  0.094  0.134  94  GLY GGG CA  
8405  C C   . GLY G 94  ? 2.564 2.221 2.034 0.340  0.105  0.137  94  GLY GGG C   
8406  O O   . GLY G 94  ? 2.607 2.230 2.059 0.358  0.116  0.138  94  GLY GGG O   
8407  N N   . PRO G 95  ? 2.462 2.075 1.937 0.324  0.103  0.139  95  PRO GGG N   
8408  C CA  . PRO G 95  ? 2.397 1.924 1.854 0.327  0.114  0.141  95  PRO GGG CA  
8409  C C   . PRO G 95  ? 2.575 2.075 1.975 0.372  0.133  0.149  95  PRO GGG C   
8410  O O   . PRO G 95  ? 2.783 2.320 2.156 0.403  0.137  0.156  95  PRO GGG O   
8411  C CB  . PRO G 95  ? 2.294 1.799 1.762 0.304  0.107  0.143  95  PRO GGG CB  
8412  C CG  . PRO G 95  ? 2.346 1.914 1.849 0.281  0.091  0.138  95  PRO GGG CG  
8413  C CD  . PRO G 95  ? 2.444 2.084 1.940 0.300  0.090  0.138  95  PRO GGG CD  
8414  N N   . GLY G 96  ? 2.541 1.973 1.918 0.377  0.146  0.149  96  GLY GGG N   
8415  C CA  . GLY G 96  ? 2.544 1.927 1.855 0.417  0.167  0.157  96  GLY GGG CA  
8416  C C   . GLY G 96  ? 2.560 1.965 1.853 0.449  0.175  0.158  96  GLY GGG C   
8417  O O   . GLY G 96  ? 2.785 2.136 2.019 0.482  0.195  0.163  96  GLY GGG O   
8418  N N   . ILE G 97  ? 2.529 2.007 1.865 0.438  0.162  0.152  97  ILE GGG N   
8419  C CA  . ILE G 97  ? 2.563 2.068 1.887 0.463  0.168  0.152  97  ILE GGG CA  
8420  C C   . ILE G 97  ? 2.578 2.008 1.890 0.457  0.179  0.149  97  ILE GGG C   
8421  O O   . ILE G 97  ? 2.468 1.867 1.814 0.419  0.172  0.142  97  ILE GGG O   
8422  C CB  . ILE G 97  ? 2.561 2.155 1.933 0.442  0.150  0.145  97  ILE GGG CB  
8423  C CG1 . ILE G 97  ? 2.640 2.325 2.008 0.461  0.144  0.150  97  ILE GGG CG1 
8424  C CG2 . ILE G 97  ? 2.592 2.195 1.965 0.449  0.153  0.141  97  ILE GGG CG2 
8425  C CD1 . ILE G 97  ? 2.754 2.483 2.083 0.512  0.155  0.157  97  ILE GGG CD1 
8426  N N   . LEU G 98  ? 2.610 2.011 1.871 0.496  0.197  0.154  98  LEU GGG N   
8427  C CA  . LEU G 98  ? 2.684 2.014 1.925 0.494  0.210  0.152  98  LEU GGG CA  
8428  C C   . LEU G 98  ? 2.749 2.124 2.001 0.507  0.208  0.149  98  LEU GGG C   
8429  O O   . LEU G 98  ? 2.862 2.285 2.088 0.547  0.213  0.155  98  LEU GGG O   
8430  C CB  . LEU G 98  ? 2.784 2.029 1.945 0.526  0.234  0.160  98  LEU GGG CB  
8431  C CG  . LEU G 98  ? 2.833 1.993 1.964 0.518  0.251  0.157  98  LEU GGG CG  
8432  C CD1 . LEU G 98  ? 2.747 1.888 1.928 0.463  0.240  0.148  98  LEU GGG CD1 
8433  C CD2 . LEU G 98  ? 2.987 2.054 2.027 0.546  0.277  0.165  98  LEU GGG CD2 
8434  N N   . SER G 99  ? 2.709 2.073 1.998 0.476  0.203  0.140  99  SER GGG N   
8435  C CA  . SER G 99  ? 2.768 2.174 2.071 0.483  0.200  0.136  99  SER GGG CA  
8436  C C   . SER G 99  ? 2.748 2.095 2.054 0.468  0.208  0.131  99  SER GGG C   
8437  O O   . SER G 99  ? 2.607 1.902 1.925 0.440  0.209  0.129  99  SER GGG O   
8438  C CB  . SER G 99  ? 2.812 2.300 2.171 0.456  0.179  0.129  99  SER GGG CB  
8439  O OG  . SER G 99  ? 3.005 2.520 2.379 0.452  0.176  0.123  99  SER GGG OG  
8440  N N   . MET G 100 ? 2.814 2.175 2.107 0.489  0.213  0.130  100 MET GGG N   
8441  C CA  . MET G 100 ? 2.685 1.998 1.979 0.479  0.222  0.126  100 MET GGG CA  
8442  C C   . MET G 100 ? 2.618 1.957 1.972 0.440  0.207  0.117  100 MET GGG C   
8443  O O   . MET G 100 ? 2.575 1.978 1.961 0.428  0.191  0.113  100 MET GGG O   
8444  C CB  . MET G 100 ? 2.687 2.006 1.942 0.517  0.234  0.129  100 MET GGG CB  
8445  C CG  . MET G 100 ? 2.749 2.007 1.929 0.557  0.256  0.138  100 MET GGG CG  
8446  S SD  . MET G 100 ? 2.649 1.790 1.795 0.537  0.275  0.137  100 MET GGG SD  
8447  C CE  . MET G 100 ? 2.815 1.961 1.999 0.516  0.272  0.128  100 MET GGG CE  
8448  N N   . ALA G 101 ? 2.585 1.873 1.948 0.419  0.212  0.113  101 ALA GGG N   
8449  C CA  . ALA G 101 ? 2.626 1.928 2.036 0.391  0.202  0.106  101 ALA GGG CA  
8450  C C   . ALA G 101 ? 2.760 2.075 2.161 0.407  0.207  0.103  101 ALA GGG C   
8451  O O   . ALA G 101 ? 2.928 2.223 2.287 0.437  0.221  0.107  101 ALA GGG O   
8452  C CB  . ALA G 101 ? 2.544 1.797 1.969 0.365  0.207  0.105  101 ALA GGG CB  
8453  N N   . ASN G 102 ? 2.746 2.092 2.183 0.388  0.197  0.096  102 ASN GGG N   
8454  C CA  . ASN G 102 ? 2.779 2.135 2.209 0.399  0.201  0.092  102 ASN GGG CA  
8455  C C   . ASN G 102 ? 2.699 2.059 2.165 0.371  0.193  0.085  102 ASN GGG C   
8456  O O   . ASN G 102 ? 2.657 2.046 2.147 0.349  0.180  0.081  102 ASN GGG O   
8457  C CB  . ASN G 102 ? 2.964 2.382 2.377 0.420  0.197  0.093  102 ASN GGG CB  
8458  C CG  . ASN G 102 ? 3.083 2.561 2.524 0.396  0.180  0.088  102 ASN GGG CG  
8459  O OD1 . ASN G 102 ? 3.272 2.772 2.719 0.391  0.172  0.091  102 ASN GGG OD1 
8460  N ND2 . ASN G 102 ? 3.077 2.580 2.531 0.380  0.174  0.080  102 ASN GGG ND2 
8461  N N   . ALA G 103 ? 2.783 2.110 2.246 0.373  0.203  0.083  103 ALA GGG N   
8462  C CA  . ALA G 103 ? 2.764 2.087 2.255 0.352  0.198  0.077  103 ALA GGG CA  
8463  C C   . ALA G 103 ? 2.802 2.168 2.291 0.349  0.191  0.071  103 ALA GGG C   
8464  O O   . ALA G 103 ? 2.787 2.154 2.293 0.328  0.184  0.065  103 ALA GGG O   
8465  C CB  . ALA G 103 ? 2.669 1.950 2.155 0.358  0.212  0.077  103 ALA GGG CB  
8466  N N   . GLY G 104 ? 2.889 2.289 2.353 0.371  0.193  0.072  104 GLY GGG N   
8467  C CA  . GLY G 104 ? 2.941 2.390 2.397 0.370  0.187  0.066  104 GLY GGG CA  
8468  C C   . GLY G 104 ? 3.025 2.521 2.454 0.400  0.189  0.071  104 GLY GGG C   
8469  O O   . GLY G 104 ? 3.032 2.508 2.443 0.423  0.196  0.080  104 GLY GGG O   
8470  N N   . PRO G 105 ? 2.933 2.492 2.354 0.400  0.183  0.067  105 PRO GGG N   
8471  C CA  . PRO G 105 ? 2.903 2.517 2.296 0.435  0.185  0.074  105 PRO GGG CA  
8472  C C   . PRO G 105 ? 3.003 2.571 2.365 0.474  0.203  0.081  105 PRO GGG C   
8473  O O   . PRO G 105 ? 3.100 2.627 2.459 0.474  0.210  0.078  105 PRO GGG O   
8474  C CB  . PRO G 105 ? 2.893 2.580 2.285 0.421  0.177  0.066  105 PRO GGG CB  
8475  C CG  . PRO G 105 ? 2.875 2.538 2.289 0.376  0.170  0.056  105 PRO GGG CG  
8476  C CD  . PRO G 105 ? 2.930 2.509 2.361 0.369  0.175  0.057  105 PRO GGG CD  
8477  N N   . ASN G 106 ? 2.979 2.549 2.311 0.509  0.210  0.091  106 ASN GGG N   
8478  C CA  . ASN G 106 ? 3.164 2.688 2.452 0.551  0.229  0.099  106 ASN GGG CA  
8479  C C   . ASN G 106 ? 3.184 2.613 2.471 0.540  0.240  0.098  106 ASN GGG C   
8480  O O   . ASN G 106 ? 3.258 2.650 2.522 0.555  0.253  0.098  106 ASN GGG O   
8481  C CB  . ASN G 106 ? 3.218 2.787 2.483 0.579  0.232  0.100  106 ASN GGG CB  
8482  C CG  . ASN G 106 ? 3.333 3.010 2.598 0.588  0.221  0.101  106 ASN GGG CG  
8483  O OD1 . ASN G 106 ? 3.345 3.054 2.595 0.610  0.220  0.110  106 ASN GGG OD1 
8484  N ND2 . ASN G 106 ? 3.489 3.225 2.769 0.570  0.211  0.093  106 ASN GGG ND2 
8485  N N   . THR G 107 ? 3.071 2.466 2.383 0.511  0.236  0.097  107 THR GGG N   
8486  C CA  . THR G 107 ? 3.024 2.341 2.338 0.496  0.246  0.096  107 THR GGG CA  
8487  C C   . THR G 107 ? 3.038 2.316 2.339 0.494  0.251  0.101  107 THR GGG C   
8488  O O   . THR G 107 ? 3.038 2.278 2.359 0.467  0.251  0.099  107 THR GGG O   
8489  C CB  . THR G 107 ? 2.929 2.246 2.292 0.458  0.237  0.087  107 THR GGG CB  
8490  O OG1 . THR G 107 ? 2.963 2.314 2.359 0.433  0.221  0.085  107 THR GGG OG1 
8491  C CG2 . THR G 107 ? 2.916 2.262 2.284 0.459  0.234  0.081  107 THR GGG CG2 
8492  N N   . ASN G 108 ? 3.144 2.436 2.409 0.524  0.255  0.109  108 ASN GGG N   
8493  C CA  . ASN G 108 ? 3.025 2.274 2.266 0.527  0.261  0.115  108 ASN GGG CA  
8494  C C   . ASN G 108 ? 3.036 2.194 2.230 0.533  0.283  0.117  108 ASN GGG C   
8495  O O   . ASN G 108 ? 3.248 2.380 2.401 0.559  0.298  0.119  108 ASN GGG O   
8496  C CB  . ASN G 108 ? 3.040 2.328 2.247 0.564  0.262  0.123  108 ASN GGG CB  
8497  C CG  . ASN G 108 ? 2.967 2.349 2.219 0.552  0.241  0.120  108 ASN GGG CG  
8498  O OD1 . ASN G 108 ? 2.926 2.334 2.229 0.515  0.226  0.111  108 ASN GGG OD1 
8499  N ND2 . ASN G 108 ? 3.088 2.523 2.317 0.584  0.240  0.127  108 ASN GGG ND2 
8500  N N   . GLY G 109 ? 2.851 1.960 2.045 0.507  0.286  0.117  109 GLY GGG N   
8501  C CA  . GLY G 109 ? 2.842 1.865 1.984 0.507  0.308  0.119  109 GLY GGG CA  
8502  C C   . GLY G 109 ? 2.873 1.843 1.967 0.508  0.319  0.124  109 GLY GGG C   
8503  O O   . GLY G 109 ? 3.012 1.974 2.056 0.547  0.327  0.132  109 GLY GGG O   
8504  N N   . SER G 110 ? 2.768 1.702 1.875 0.469  0.320  0.121  110 SER GGG N   
8505  C CA  . SER G 110 ? 2.841 1.722 1.904 0.462  0.329  0.125  110 SER GGG CA  
8506  C C   . SER G 110 ? 2.803 1.722 1.925 0.427  0.310  0.123  110 SER GGG C   
8507  O O   . SER G 110 ? 2.848 1.723 1.947 0.403  0.316  0.123  110 SER GGG O   
8508  C CB  . SER G 110 ? 2.928 1.716 1.929 0.446  0.353  0.124  110 SER GGG CB  
8509  O OG  . SER G 110 ? 2.877 1.675 1.927 0.399  0.347  0.117  110 SER GGG OG  
8510  N N   . GLN G 111 ? 2.673 1.671 1.865 0.420  0.288  0.120  111 GLN GGG N   
8511  C CA  . GLN G 111 ? 2.560 1.592 1.806 0.388  0.270  0.118  111 GLN GGG CA  
8512  C C   . GLN G 111 ? 2.533 1.618 1.793 0.404  0.256  0.121  111 GLN GGG C   
8513  O O   . GLN G 111 ? 2.507 1.642 1.777 0.428  0.249  0.121  111 GLN GGG O   
8514  C CB  . GLN G 111 ? 2.483 1.552 1.794 0.360  0.257  0.112  111 GLN GGG CB  
8515  C CG  . GLN G 111 ? 2.595 1.621 1.896 0.339  0.270  0.109  111 GLN GGG CG  
8516  C CD  . GLN G 111 ? 2.564 1.629 1.928 0.315  0.259  0.105  111 GLN GGG CD  
8517  O OE1 . GLN G 111 ? 2.470 1.585 1.881 0.312  0.241  0.103  111 GLN GGG OE1 
8518  N NE2 . GLN G 111 ? 2.597 1.638 1.957 0.299  0.270  0.102  111 GLN GGG NE2 
8519  N N   . PHE G 112 ? 2.476 1.554 1.739 0.389  0.251  0.123  112 PHE GGG N   
8520  C CA  . PHE G 112 ? 2.461 1.581 1.730 0.403  0.240  0.127  112 PHE GGG CA  
8521  C C   . PHE G 112 ? 2.391 1.541 1.715 0.367  0.222  0.124  112 PHE GGG C   
8522  O O   . PHE G 112 ? 2.345 1.469 1.686 0.336  0.222  0.121  112 PHE GGG O   
8523  C CB  . PHE G 112 ? 2.607 1.676 1.806 0.427  0.256  0.134  112 PHE GGG CB  
8524  C CG  . PHE G 112 ? 2.663 1.657 1.831 0.400  0.268  0.134  112 PHE GGG CG  
8525  C CD1 . PHE G 112 ? 2.739 1.667 1.867 0.392  0.287  0.132  112 PHE GGG CD1 
8526  C CD2 . PHE G 112 ? 2.669 1.662 1.848 0.379  0.261  0.135  112 PHE GGG CD2 
8527  C CE1 . PHE G 112 ? 2.828 1.693 1.925 0.360  0.298  0.130  112 PHE GGG CE1 
8528  C CE2 . PHE G 112 ? 2.746 1.677 1.896 0.350  0.271  0.134  112 PHE GGG CE2 
8529  C CZ  . PHE G 112 ? 2.789 1.656 1.896 0.339  0.290  0.131  112 PHE GGG CZ  
8530  N N   . PHE G 113 ? 2.366 1.575 1.718 0.371  0.207  0.124  113 PHE GGG N   
8531  C CA  . PHE G 113 ? 2.290 1.523 1.686 0.342  0.191  0.123  113 PHE GGG CA  
8532  C C   . PHE G 113 ? 2.395 1.649 1.775 0.355  0.187  0.128  113 PHE GGG C   
8533  O O   . PHE G 113 ? 2.495 1.789 1.860 0.384  0.186  0.130  113 PHE GGG O   
8534  C CB  . PHE G 113 ? 2.179 1.462 1.631 0.323  0.175  0.117  113 PHE GGG CB  
8535  C CG  . PHE G 113 ? 2.153 1.495 1.611 0.338  0.166  0.115  113 PHE GGG CG  
8536  C CD1 . PHE G 113 ? 2.209 1.598 1.683 0.332  0.153  0.116  113 PHE GGG CD1 
8537  C CD2 . PHE G 113 ? 2.236 1.593 1.685 0.355  0.171  0.113  113 PHE GGG CD2 
8538  C CE1 . PHE G 113 ? 2.288 1.739 1.766 0.341  0.146  0.113  113 PHE GGG CE1 
8539  C CE2 . PHE G 113 ? 2.317 1.737 1.772 0.364  0.163  0.111  113 PHE GGG CE2 
8540  C CZ  . PHE G 113 ? 2.313 1.782 1.782 0.356  0.151  0.111  113 PHE GGG CZ  
8541  N N   . ILE G 114 ? 2.425 1.658 1.808 0.335  0.184  0.129  114 ILE GGG N   
8542  C CA  . ILE G 114 ? 2.331 1.580 1.701 0.345  0.180  0.134  114 ILE GGG CA  
8543  C C   . ILE G 114 ? 2.248 1.548 1.675 0.318  0.159  0.131  114 ILE GGG C   
8544  O O   . ILE G 114 ? 2.190 1.477 1.646 0.287  0.152  0.128  114 ILE GGG O   
8545  C CB  . ILE G 114 ? 2.279 1.460 1.604 0.341  0.193  0.138  114 ILE GGG CB  
8546  C CG1 . ILE G 114 ? 2.442 1.556 1.711 0.355  0.215  0.139  114 ILE GGG CG1 
8547  C CG2 . ILE G 114 ? 2.366 1.559 1.663 0.363  0.194  0.144  114 ILE GGG CG2 
8548  C CD1 . ILE G 114 ? 2.530 1.569 1.756 0.336  0.228  0.141  114 ILE GGG CD1 
8549  N N   . CYS G 115 ? 2.186 1.548 1.625 0.329  0.150  0.131  115 CYS GGG N   
8550  C CA  . CYS G 115 ? 2.154 1.561 1.637 0.303  0.131  0.127  115 CYS GGG CA  
8551  C C   . CYS G 115 ? 2.178 1.573 1.664 0.289  0.126  0.130  115 CYS GGG C   
8552  O O   . CYS G 115 ? 2.270 1.648 1.719 0.308  0.134  0.136  115 CYS GGG O   
8553  C CB  . CYS G 115 ? 2.222 1.702 1.709 0.314  0.124  0.125  115 CYS GGG CB  
8554  S SG  . CYS G 115 ? 2.313 1.822 1.801 0.326  0.126  0.121  115 CYS GGG SG  
8555  N N   . THR G 116 ? 2.145 1.545 1.670 0.257  0.113  0.127  116 THR GGG N   
8556  C CA  . THR G 116 ? 2.171 1.567 1.704 0.241  0.106  0.129  116 THR GGG CA  
8557  C C   . THR G 116 ? 2.192 1.639 1.753 0.226  0.091  0.126  116 THR GGG C   
8558  O O   . THR G 116 ? 2.239 1.687 1.814 0.208  0.082  0.128  116 THR GGG O   
8559  C CB  . THR G 116 ? 2.062 1.418 1.612 0.217  0.106  0.129  116 THR GGG CB  
8560  O OG1 . THR G 116 ? 1.970 1.336 1.555 0.201  0.099  0.125  116 THR GGG OG1 
8561  C CG2 . THR G 116 ? 2.153 1.456 1.669 0.225  0.122  0.132  116 THR GGG CG2 
8562  N N   . ALA G 117 ? 2.187 1.676 1.754 0.230  0.088  0.122  117 ALA GGG N   
8563  C CA  . ALA G 117 ? 2.240 1.782 1.823 0.214  0.076  0.118  117 ALA GGG CA  
8564  C C   . ALA G 117 ? 2.344 1.935 1.914 0.230  0.078  0.115  117 ALA GGG C   
8565  O O   . ALA G 117 ? 2.347 1.927 1.899 0.254  0.089  0.117  117 ALA GGG O   
8566  C CB  . ALA G 117 ? 2.153 1.679 1.763 0.183  0.067  0.112  117 ALA GGG CB  
8567  N N   . LYS G 118 ? 2.442 2.092 2.018 0.215  0.069  0.111  118 LYS GGG N   
8568  C CA  . LYS G 118 ? 2.540 2.250 2.107 0.223  0.069  0.108  118 LYS GGG CA  
8569  C C   . LYS G 118 ? 2.524 2.208 2.101 0.205  0.069  0.100  118 LYS GGG C   
8570  O O   . LYS G 118 ? 2.459 2.114 2.051 0.175  0.063  0.095  118 LYS GGG O   
8571  C CB  . LYS G 118 ? 2.642 2.427 2.210 0.206  0.060  0.105  118 LYS GGG CB  
8572  C CG  . LYS G 118 ? 2.670 2.529 2.227 0.210  0.060  0.101  118 LYS GGG CG  
8573  C CD  . LYS G 118 ? 2.718 2.662 2.275 0.191  0.051  0.099  118 LYS GGG CD  
8574  C CE  . LYS G 118 ? 2.821 2.851 2.367 0.193  0.050  0.095  118 LYS GGG CE  
8575  N NZ  . LYS G 118 ? 2.827 2.952 2.372 0.168  0.041  0.091  118 LYS GGG NZ  
8576  N N   . THR G 119 ? 2.556 2.249 2.122 0.225  0.077  0.100  119 THR GGG N   
8577  C CA  . THR G 119 ? 2.546 2.208 2.118 0.214  0.079  0.093  119 THR GGG CA  
8578  C C   . THR G 119 ? 2.648 2.370 2.208 0.214  0.078  0.088  119 THR GGG C   
8579  O O   . THR G 119 ? 2.720 2.446 2.268 0.237  0.086  0.089  119 THR GGG O   
8580  C CB  . THR G 119 ? 2.514 2.118 2.081 0.238  0.091  0.098  119 THR GGG CB  
8581  O OG1 . THR G 119 ? 2.527 2.150 2.067 0.275  0.100  0.104  119 THR GGG OG1 
8582  C CG2 . THR G 119 ? 2.505 2.054 2.082 0.232  0.091  0.103  119 THR GGG CG2 
8583  N N   . GLU G 120 ? 2.674 2.445 2.236 0.183  0.069  0.081  120 GLU GGG N   
8584  C CA  . GLU G 120 ? 2.784 2.633 2.333 0.178  0.066  0.076  120 GLU GGG CA  
8585  C C   . GLU G 120 ? 2.844 2.673 2.388 0.169  0.070  0.069  120 GLU GGG C   
8586  O O   . GLU G 120 ? 2.980 2.867 2.512 0.176  0.071  0.066  120 GLU GGG O   
8587  C CB  . GLU G 120 ? 2.858 2.748 2.408 0.135  0.056  0.069  120 GLU GGG CB  
8588  C CG  . GLU G 120 ? 3.016 2.906 2.574 0.136  0.051  0.075  120 GLU GGG CG  
8589  C CD  . GLU G 120 ? 3.075 2.944 2.636 0.090  0.043  0.069  120 GLU GGG CD  
8590  O OE1 . GLU G 120 ? 3.118 2.992 2.667 0.054  0.041  0.058  120 GLU GGG OE1 
8591  O OE2 . GLU G 120 ? 3.081 2.919 2.652 0.090  0.041  0.074  120 GLU GGG OE2 
8592  N N   . TRP G 121 ? 2.722 2.475 2.275 0.153  0.072  0.066  121 TRP GGG N   
8593  C CA  . TRP G 121 ? 2.644 2.369 2.190 0.146  0.076  0.059  121 TRP GGG CA  
8594  C C   . TRP G 121 ? 2.651 2.366 2.194 0.184  0.086  0.064  121 TRP GGG C   
8595  O O   . TRP G 121 ? 2.685 2.392 2.220 0.181  0.090  0.058  121 TRP GGG O   
8596  C CB  . TRP G 121 ? 2.606 2.253 2.157 0.123  0.077  0.056  121 TRP GGG CB  
8597  C CG  . TRP G 121 ? 2.580 2.174 2.150 0.143  0.080  0.064  121 TRP GGG CG  
8598  C CD1 . TRP G 121 ? 2.506 2.056 2.084 0.165  0.088  0.069  121 TRP GGG CD1 
8599  C CD2 . TRP G 121 ? 2.591 2.175 2.173 0.138  0.075  0.070  121 TRP GGG CD2 
8600  N NE1 . TRP G 121 ? 2.420 1.936 2.013 0.172  0.088  0.076  121 TRP GGG NE1 
8601  C CE2 . TRP G 121 ? 2.470 2.005 2.066 0.157  0.080  0.077  121 TRP GGG CE2 
8602  C CE3 . TRP G 121 ? 2.601 2.217 2.182 0.119  0.066  0.069  121 TRP GGG CE3 
8603  C CZ2 . TRP G 121 ? 2.439 1.955 2.048 0.156  0.076  0.083  121 TRP GGG CZ2 
8604  C CZ3 . TRP G 121 ? 2.501 2.094 2.095 0.120  0.063  0.075  121 TRP GGG CZ3 
8605  C CH2 . TRP G 121 ? 2.447 1.991 2.055 0.139  0.068  0.082  121 TRP GGG CH2 
8606  N N   . LEU G 122 ? 2.662 2.371 2.205 0.218  0.091  0.073  122 LEU GGG N   
8607  C CA  . LEU G 122 ? 2.729 2.425 2.261 0.255  0.102  0.078  122 LEU GGG CA  
8608  C C   . LEU G 122 ? 2.803 2.575 2.315 0.280  0.104  0.081  122 LEU GGG C   
8609  O O   . LEU G 122 ? 2.815 2.581 2.310 0.312  0.114  0.085  122 LEU GGG O   
8610  C CB  . LEU G 122 ? 2.686 2.326 2.218 0.278  0.110  0.087  122 LEU GGG CB  
8611  C CG  . LEU G 122 ? 2.574 2.150 2.128 0.256  0.108  0.086  122 LEU GGG CG  
8612  C CD1 . LEU G 122 ? 2.423 1.953 1.974 0.271  0.115  0.094  122 LEU GGG CD1 
8613  C CD2 . LEU G 122 ? 2.622 2.163 2.182 0.248  0.113  0.081  122 LEU GGG CD2 
8614  N N   . ASP G 123 ? 2.914 2.760 2.425 0.267  0.095  0.080  123 ASP GGG N   
8615  C CA  . ASP G 123 ? 3.001 2.936 2.494 0.292  0.096  0.083  123 ASP GGG CA  
8616  C C   . ASP G 123 ? 3.023 2.984 2.507 0.290  0.098  0.077  123 ASP GGG C   
8617  O O   . ASP G 123 ? 3.052 3.005 2.543 0.250  0.093  0.066  123 ASP GGG O   
8618  C CB  . ASP G 123 ? 3.065 3.083 2.562 0.269  0.085  0.081  123 ASP GGG CB  
8619  C CG  . ASP G 123 ? 3.123 3.127 2.624 0.281  0.084  0.089  123 ASP GGG CG  
8620  O OD1 . ASP G 123 ? 3.158 3.098 2.652 0.312  0.093  0.098  123 ASP GGG OD1 
8621  O OD2 . ASP G 123 ? 3.082 3.136 2.590 0.256  0.074  0.087  123 ASP GGG OD2 
8622  N N   . GLY G 124 ? 3.125 3.114 2.589 0.334  0.107  0.084  124 GLY GGG N   
8623  C CA  . GLY G 124 ? 3.121 3.143 2.574 0.338  0.109  0.079  124 GLY GGG CA  
8624  C C   . GLY G 124 ? 3.046 2.981 2.498 0.341  0.118  0.077  124 GLY GGG C   
8625  O O   . GLY G 124 ? 3.102 3.059 2.544 0.346  0.121  0.073  124 GLY GGG O   
8626  N N   . LYS G 125 ? 2.918 2.763 2.382 0.338  0.122  0.078  125 LYS GGG N   
8627  C CA  . LYS G 125 ? 2.773 2.539 2.239 0.341  0.131  0.076  125 LYS GGG CA  
8628  C C   . LYS G 125 ? 2.819 2.523 2.272 0.377  0.144  0.086  125 LYS GGG C   
8629  O O   . LYS G 125 ? 2.833 2.495 2.274 0.393  0.154  0.087  125 LYS GGG O   
8630  C CB  . LYS G 125 ? 2.609 2.321 2.098 0.299  0.125  0.068  125 LYS GGG CB  
8631  C CG  . LYS G 125 ? 2.537 2.290 2.028 0.258  0.115  0.058  125 LYS GGG CG  
8632  C CD  . LYS G 125 ? 2.440 2.125 1.944 0.225  0.113  0.051  125 LYS GGG CD  
8633  C CE  . LYS G 125 ? 2.397 2.107 1.890 0.181  0.106  0.040  125 LYS GGG CE  
8634  N NZ  . LYS G 125 ? 2.395 2.035 1.892 0.153  0.105  0.036  125 LYS GGG NZ  
8635  N N   . HIS G 126 ? 2.884 2.579 2.333 0.387  0.144  0.093  126 HIS GGG N   
8636  C CA  . HIS G 126 ? 2.970 2.600 2.397 0.416  0.158  0.102  126 HIS GGG CA  
8637  C C   . HIS G 126 ? 3.190 2.860 2.584 0.455  0.163  0.112  126 HIS GGG C   
8638  O O   . HIS G 126 ? 3.201 2.946 2.602 0.452  0.153  0.112  126 HIS GGG O   
8639  C CB  . HIS G 126 ? 2.823 2.394 2.270 0.391  0.155  0.102  126 HIS GGG CB  
8640  C CG  . HIS G 126 ? 2.661 2.193 2.138 0.359  0.152  0.094  126 HIS GGG CG  
8641  N ND1 . HIS G 126 ? 2.671 2.139 2.144 0.362  0.163  0.095  126 HIS GGG ND1 
8642  C CD2 . HIS G 126 ? 2.528 2.073 2.033 0.325  0.140  0.087  126 HIS GGG CD2 
8643  C CE1 . HIS G 126 ? 2.664 2.114 2.166 0.334  0.157  0.089  126 HIS GGG CE1 
8644  N NE2 . HIS G 126 ? 2.611 2.103 2.129 0.313  0.145  0.084  126 HIS GGG NE2 
8645  N N   . VAL G 127 ? 3.433 3.051 2.787 0.493  0.180  0.120  127 VAL GGG N   
8646  C CA  . VAL G 127 ? 3.509 3.159 2.819 0.542  0.189  0.131  127 VAL GGG CA  
8647  C C   . VAL G 127 ? 3.445 3.050 2.734 0.553  0.195  0.138  127 VAL GGG C   
8648  O O   . VAL G 127 ? 3.542 3.057 2.812 0.550  0.207  0.140  127 VAL GGG O   
8649  C CB  . VAL G 127 ? 3.588 3.205 2.853 0.583  0.207  0.136  127 VAL GGG CB  
8650  C CG1 . VAL G 127 ? 3.724 3.365 2.934 0.641  0.219  0.149  127 VAL GGG CG1 
8651  C CG2 . VAL G 127 ? 3.574 3.241 2.858 0.574  0.200  0.128  127 VAL GGG CG2 
8652  N N   . VAL G 128 ? 3.239 2.910 2.527 0.563  0.188  0.143  128 VAL GGG N   
8653  C CA  . VAL G 128 ? 3.123 2.759 2.388 0.575  0.194  0.151  128 VAL GGG CA  
8654  C C   . VAL G 128 ? 3.097 2.702 2.291 0.636  0.215  0.163  128 VAL GGG C   
8655  O O   . VAL G 128 ? 3.124 2.800 2.296 0.677  0.218  0.170  128 VAL GGG O   
8656  C CB  . VAL G 128 ? 3.102 2.825 2.396 0.561  0.177  0.150  128 VAL GGG CB  
8657  C CG1 . VAL G 128 ? 3.144 2.826 2.418 0.570  0.183  0.157  128 VAL GGG CG1 
8658  C CG2 . VAL G 128 ? 3.094 2.847 2.449 0.503  0.158  0.138  128 VAL GGG CG2 
8659  N N   . PHE G 129 ? 2.898 2.396 2.051 0.643  0.232  0.167  129 PHE GGG N   
8660  C CA  . PHE G 129 ? 2.959 2.403 2.030 0.700  0.256  0.179  129 PHE GGG CA  
8661  C C   . PHE G 129 ? 3.078 2.457 2.101 0.715  0.269  0.187  129 PHE GGG C   
8662  O O   . PHE G 129 ? 3.321 2.643 2.265 0.764  0.292  0.197  129 PHE GGG O   
8663  C CB  . PHE G 129 ? 3.078 2.436 2.118 0.703  0.272  0.177  129 PHE GGG CB  
8664  C CG  . PHE G 129 ? 3.049 2.312 2.097 0.657  0.275  0.169  129 PHE GGG CG  
8665  C CD1 . PHE G 129 ? 2.969 2.247 2.086 0.604  0.259  0.158  129 PHE GGG CD1 
8666  C CD2 . PHE G 129 ? 3.165 2.325 2.146 0.667  0.296  0.175  129 PHE GGG CD2 
8667  C CE1 . PHE G 129 ? 2.984 2.189 2.110 0.564  0.262  0.152  129 PHE GGG CE1 
8668  C CE2 . PHE G 129 ? 3.134 2.218 2.122 0.622  0.299  0.168  129 PHE GGG CE2 
8669  C CZ  . PHE G 129 ? 3.055 2.167 2.118 0.571  0.281  0.157  129 PHE GGG CZ  
8670  N N   . GLY G 130 ? 3.027 2.405 2.088 0.675  0.256  0.182  130 GLY GGG N   
8671  C CA  . GLY G 130 ? 3.177 2.491 2.189 0.688  0.268  0.189  130 GLY GGG CA  
8672  C C   . GLY G 130 ? 3.113 2.460 2.180 0.645  0.249  0.185  130 GLY GGG C   
8673  O O   . GLY G 130 ? 3.022 2.440 2.161 0.608  0.227  0.176  130 GLY GGG O   
8674  N N   . LYS G 131 ? 3.244 2.534 2.270 0.652  0.259  0.190  131 LYS GGG N   
8675  C CA  . LYS G 131 ? 3.109 2.416 2.179 0.613  0.243  0.186  131 LYS GGG CA  
8676  C C   . LYS G 131 ? 3.190 2.390 2.207 0.606  0.258  0.189  131 LYS GGG C   
8677  O O   . LYS G 131 ? 3.326 2.454 2.259 0.646  0.282  0.198  131 LYS GGG O   
8678  C CB  . LYS G 131 ? 3.102 2.506 2.186 0.635  0.232  0.192  131 LYS GGG CB  
8679  C CG  . LYS G 131 ? 3.007 2.527 2.167 0.609  0.207  0.185  131 LYS GGG CG  
8680  C CD  . LYS G 131 ? 2.930 2.531 2.096 0.623  0.199  0.192  131 LYS GGG CD  
8681  C CE  . LYS G 131 ? 2.770 2.484 2.004 0.591  0.176  0.184  131 LYS GGG CE  
8682  N NZ  . LYS G 131 ? 2.704 2.497 1.943 0.610  0.174  0.184  131 LYS GGG NZ  
8683  N N   . VAL G 132 ? 3.152 2.341 2.216 0.554  0.244  0.182  132 VAL GGG N   
8684  C CA  . VAL G 132 ? 3.199 2.308 2.227 0.537  0.253  0.183  132 VAL GGG CA  
8685  C C   . VAL G 132 ? 3.212 2.338 2.201 0.574  0.258  0.193  132 VAL GGG C   
8686  O O   . VAL G 132 ? 3.204 2.425 2.239 0.579  0.241  0.194  132 VAL GGG O   
8687  C CB  . VAL G 132 ? 3.108 2.227 2.204 0.476  0.233  0.174  132 VAL GGG CB  
8688  C CG1 . VAL G 132 ? 3.188 2.238 2.249 0.458  0.241  0.175  132 VAL GGG CG1 
8689  C CG2 . VAL G 132 ? 3.084 2.178 2.207 0.445  0.233  0.166  132 VAL GGG CG2 
8690  N N   . LYS G 133 ? 3.372 2.404 2.271 0.600  0.283  0.200  133 LYS GGG N   
8691  C CA  . LYS G 133 ? 3.307 2.342 2.158 0.641  0.291  0.211  133 LYS GGG CA  
8692  C C   . LYS G 133 ? 3.564 2.555 2.414 0.605  0.288  0.209  133 LYS GGG C   
8693  O O   . LYS G 133 ? 3.599 2.652 2.479 0.606  0.275  0.212  133 LYS GGG O   
8694  C CB  . LYS G 133 ? 3.571 2.519 2.308 0.699  0.324  0.222  133 LYS GGG CB  
8695  C CG  . LYS G 133 ? 3.771 2.786 2.488 0.764  0.330  0.232  133 LYS GGG CG  
8696  C CD  . LYS G 133 ? 3.606 2.767 2.395 0.772  0.307  0.234  133 LYS GGG CD  
8697  C CE  . LYS G 133 ? 3.742 2.967 2.493 0.844  0.317  0.247  133 LYS GGG CE  
8698  N NZ  . LYS G 133 ? 3.780 3.158 2.595 0.853  0.296  0.249  133 LYS GGG NZ  
8699  N N   . GLU G 134 ? 3.600 2.490 2.417 0.570  0.299  0.204  134 GLU GGG N   
8700  C CA  . GLU G 134 ? 3.761 2.611 2.581 0.528  0.295  0.200  134 GLU GGG CA  
8701  C C   . GLU G 134 ? 3.666 2.498 2.535 0.465  0.284  0.189  134 GLU GGG C   
8702  O O   . GLU G 134 ? 3.527 2.334 2.392 0.458  0.291  0.184  134 GLU GGG O   
8703  C CB  . GLU G 134 ? 3.988 2.719 2.694 0.548  0.324  0.207  134 GLU GGG CB  
8704  C CG  . GLU G 134 ? 4.156 2.861 2.855 0.521  0.320  0.207  134 GLU GGG CG  
8705  C CD  . GLU G 134 ? 4.299 3.112 3.064 0.531  0.298  0.210  134 GLU GGG CD  
8706  O OE1 . GLU G 134 ? 4.412 3.299 3.186 0.579  0.295  0.217  134 GLU GGG OE1 
8707  O OE2 . GLU G 134 ? 4.479 3.298 3.278 0.491  0.284  0.206  134 GLU GGG OE2 
8708  N N   . GLY G 135 ? 3.562 2.409 2.476 0.421  0.268  0.184  135 GLY GGG N   
8709  C CA  . GLY G 135 ? 3.371 2.207 2.329 0.363  0.259  0.174  135 GLY GGG CA  
8710  C C   . GLY G 135 ? 3.156 2.082 2.213 0.343  0.234  0.168  135 GLY GGG C   
8711  O O   . GLY G 135 ? 3.067 1.983 2.150 0.309  0.232  0.162  135 GLY GGG O   
8712  N N   . MET G 136 ? 3.056 2.069 2.163 0.361  0.217  0.170  136 MET GGG N   
8713  C CA  . MET G 136 ? 2.794 1.884 1.989 0.336  0.194  0.164  136 MET GGG CA  
8714  C C   . MET G 136 ? 2.597 1.685 1.836 0.286  0.181  0.159  136 MET GGG C   
8715  O O   . MET G 136 ? 2.574 1.692 1.868 0.260  0.168  0.154  136 MET GGG O   
8716  C CB  . MET G 136 ? 2.802 1.981 2.034 0.357  0.180  0.166  136 MET GGG CB  
8717  C CG  . MET G 136 ? 2.880 2.111 2.131 0.378  0.177  0.165  136 MET GGG CG  
8718  S SD  . MET G 136 ? 2.778 2.031 2.098 0.338  0.163  0.155  136 MET GGG SD  
8719  C CE  . MET G 136 ? 2.725 2.036 2.112 0.302  0.138  0.151  136 MET GGG CE  
8720  N N   . ASN G 137 ? 2.610 1.663 1.822 0.275  0.184  0.162  137 ASN GGG N   
8721  C CA  . ASN G 137 ? 2.593 1.645 1.842 0.228  0.172  0.158  137 ASN GGG CA  
8722  C C   . ASN G 137 ? 2.600 1.609 1.840 0.200  0.180  0.153  137 ASN GGG C   
8723  O O   . ASN G 137 ? 2.645 1.679 1.934 0.165  0.168  0.150  137 ASN GGG O   
8724  C CB  . ASN G 137 ? 2.697 1.712 1.906 0.223  0.176  0.162  137 ASN GGG CB  
8725  C CG  . ASN G 137 ? 2.732 1.790 1.944 0.253  0.170  0.167  137 ASN GGG CG  
8726  O OD1 . ASN G 137 ? 2.636 1.767 1.908 0.251  0.152  0.166  137 ASN GGG OD1 
8727  N ND2 . ASN G 137 ? 2.823 1.832 1.963 0.281  0.188  0.173  137 ASN GGG ND2 
8728  N N   . ILE G 138 ? 2.621 1.566 1.794 0.216  0.203  0.154  138 ILE GGG N   
8729  C CA  . ILE G 138 ? 2.764 1.670 1.925 0.188  0.212  0.149  138 ILE GGG CA  
8730  C C   . ILE G 138 ? 2.793 1.753 2.013 0.190  0.202  0.146  138 ILE GGG C   
8731  O O   . ILE G 138 ? 2.793 1.765 2.046 0.159  0.198  0.141  138 ILE GGG O   
8732  C CB  . ILE G 138 ? 2.895 1.706 1.956 0.203  0.242  0.151  138 ILE GGG CB  
8733  C CG1 . ILE G 138 ? 3.059 1.808 2.056 0.197  0.253  0.153  138 ILE GGG CG1 
8734  C CG2 . ILE G 138 ? 2.878 1.652 1.925 0.168  0.252  0.145  138 ILE GGG CG2 
8735  C CD1 . ILE G 138 ? 2.965 1.718 1.987 0.142  0.243  0.149  138 ILE GGG CD1 
8736  N N   . VAL G 139 ? 2.820 1.815 2.051 0.228  0.200  0.148  139 VAL GGG N   
8737  C CA  . VAL G 139 ? 2.738 1.786 2.025 0.230  0.189  0.144  139 VAL GGG CA  
8738  C C   . VAL G 139 ? 2.637 1.743 1.998 0.201  0.166  0.141  139 VAL GGG C   
8739  O O   . VAL G 139 ? 2.590 1.717 1.992 0.183  0.160  0.138  139 VAL GGG O   
8740  C CB  . VAL G 139 ? 2.760 1.845 2.044 0.273  0.189  0.147  139 VAL GGG CB  
8741  C CG1 . VAL G 139 ? 2.602 1.744 1.944 0.270  0.176  0.142  139 VAL GGG CG1 
8742  C CG2 . VAL G 139 ? 2.925 1.952 2.131 0.307  0.212  0.150  139 VAL GGG CG2 
8743  N N   . GLU G 140 ? 2.608 1.736 1.983 0.197  0.155  0.144  140 GLU GGG N   
8744  C CA  . GLU G 140 ? 2.480 1.655 1.917 0.171  0.136  0.142  140 GLU GGG CA  
8745  C C   . GLU G 140 ? 2.368 1.523 1.814 0.136  0.136  0.141  140 GLU GGG C   
8746  O O   . GLU G 140 ? 2.285 1.476 1.781 0.120  0.125  0.140  140 GLU GGG O   
8747  C CB  . GLU G 140 ? 2.525 1.724 1.971 0.172  0.125  0.145  140 GLU GGG CB  
8748  C CG  . GLU G 140 ? 2.607 1.849 2.058 0.200  0.119  0.146  140 GLU GGG CG  
8749  C CD  . GLU G 140 ? 2.554 1.813 2.001 0.202  0.113  0.150  140 GLU GGG CD  
8750  O OE1 . GLU G 140 ? 2.409 1.635 1.841 0.186  0.114  0.152  140 GLU GGG OE1 
8751  O OE2 . GLU G 140 ? 2.578 1.885 2.036 0.218  0.106  0.150  140 GLU GGG OE2 
8752  N N   . ALA G 141 ? 2.416 1.515 1.809 0.125  0.151  0.142  141 ALA GGG N   
8753  C CA  . ALA G 141 ? 2.428 1.517 1.826 0.087  0.153  0.140  141 ALA GGG CA  
8754  C C   . ALA G 141 ? 2.429 1.535 1.853 0.078  0.154  0.137  141 ALA GGG C   
8755  O O   . ALA G 141 ? 2.398 1.536 1.860 0.052  0.146  0.137  141 ALA GGG O   
8756  C CB  . ALA G 141 ? 2.498 1.515 1.822 0.073  0.171  0.140  141 ALA GGG CB  
8757  N N   . MET G 142 ? 2.391 1.479 1.795 0.101  0.165  0.136  142 MET GGG N   
8758  C CA  . MET G 142 ? 2.322 1.426 1.751 0.095  0.167  0.133  142 MET GGG CA  
8759  C C   . MET G 142 ? 2.187 1.356 1.687 0.095  0.148  0.133  142 MET GGG C   
8760  O O   . MET G 142 ? 2.177 1.369 1.706 0.079  0.147  0.132  142 MET GGG O   
8761  C CB  . MET G 142 ? 2.326 1.399 1.718 0.125  0.181  0.131  142 MET GGG CB  
8762  C CG  . MET G 142 ? 2.444 1.443 1.758 0.122  0.204  0.131  142 MET GGG CG  
8763  S SD  . MET G 142 ? 2.516 1.482 1.783 0.169  0.219  0.132  142 MET GGG SD  
8764  C CE  . MET G 142 ? 2.518 1.527 1.838 0.167  0.213  0.128  142 MET GGG CE  
8765  N N   . GLU G 143 ? 2.074 1.273 1.600 0.114  0.135  0.134  143 GLU GGG N   
8766  C CA  . GLU G 143 ? 2.161 1.407 1.741 0.117  0.121  0.134  143 GLU GGG CA  
8767  C C   . GLU G 143 ? 2.093 1.368 1.712 0.094  0.112  0.136  143 GLU GGG C   
8768  O O   . GLU G 143 ? 2.184 1.486 1.836 0.097  0.106  0.136  143 GLU GGG O   
8769  C CB  . GLU G 143 ? 2.134 1.403 1.726 0.132  0.110  0.134  143 GLU GGG CB  
8770  C CG  . GLU G 143 ? 2.309 1.589 1.910 0.120  0.099  0.137  143 GLU GGG CG  
8771  C CD  . GLU G 143 ? 2.314 1.618 1.921 0.135  0.090  0.136  143 GLU GGG CD  
8772  O OE1 . GLU G 143 ? 2.016 1.332 1.622 0.151  0.092  0.133  143 GLU GGG OE1 
8773  O OE2 . GLU G 143 ? 2.407 1.720 2.017 0.128  0.082  0.138  143 GLU GGG OE2 
8774  N N   . ARG G 144 ? 1.972 1.245 1.585 0.072  0.110  0.139  144 ARG GGG N   
8775  C CA  . ARG G 144 ? 2.048 1.361 1.702 0.056  0.099  0.142  144 ARG GGG CA  
8776  C C   . ARG G 144 ? 2.094 1.421 1.756 0.043  0.106  0.143  144 ARG GGG C   
8777  O O   . ARG G 144 ? 2.163 1.532 1.861 0.039  0.099  0.147  144 ARG GGG O   
8778  C CB  . ARG G 144 ? 2.026 1.343 1.675 0.032  0.095  0.145  144 ARG GGG CB  
8779  C CG  . ARG G 144 ? 2.086 1.451 1.777 0.021  0.082  0.151  144 ARG GGG CG  
8780  C CD  . ARG G 144 ? 2.095 1.443 1.756 -0.004 0.087  0.151  144 ARG GGG CD  
8781  N NE  . ARG G 144 ? 2.630 1.948 2.268 0.000  0.085  0.150  144 ARG GGG NE  
8782  C CZ  . ARG G 144 ? 2.945 2.227 2.539 -0.018 0.094  0.148  144 ARG GGG CZ  
8783  N NH1 . ARG G 144 ? 2.832 2.105 2.405 -0.044 0.105  0.147  144 ARG GGG NH1 
8784  N NH2 . ARG G 144 ? 2.959 2.212 2.527 -0.013 0.093  0.149  144 ARG GGG NH2 
8785  N N   . PHE G 145 ? 2.026 1.320 1.653 0.041  0.122  0.139  145 PHE GGG N   
8786  C CA  . PHE G 145 ? 2.087 1.400 1.722 0.026  0.129  0.139  145 PHE GGG CA  
8787  C C   . PHE G 145 ? 2.081 1.406 1.738 0.051  0.130  0.137  145 PHE GGG C   
8788  O O   . PHE G 145 ? 2.089 1.431 1.755 0.045  0.136  0.137  145 PHE GGG O   
8789  C CB  . PHE G 145 ? 2.195 1.459 1.774 0.007  0.147  0.134  145 PHE GGG CB  
8790  C CG  . PHE G 145 ? 2.238 1.483 1.786 -0.022 0.149  0.135  145 PHE GGG CG  
8791  C CD1 . PHE G 145 ? 2.269 1.556 1.836 -0.054 0.144  0.137  145 PHE GGG CD1 
8792  C CD2 . PHE G 145 ? 2.245 1.434 1.745 -0.013 0.155  0.133  145 PHE GGG CD2 
8793  C CE1 . PHE G 145 ? 2.372 1.639 1.906 -0.083 0.146  0.137  145 PHE GGG CE1 
8794  C CE2 . PHE G 145 ? 2.307 1.471 1.774 -0.038 0.158  0.134  145 PHE GGG CE2 
8795  C CZ  . PHE G 145 ? 2.365 1.567 1.849 -0.075 0.153  0.135  145 PHE GGG CZ  
8796  N N   . GLY G 146 ? 2.065 1.383 1.729 0.076  0.123  0.137  146 GLY GGG N   
8797  C CA  . GLY G 146 ? 1.924 1.252 1.607 0.098  0.122  0.135  146 GLY GGG CA  
8798  C C   . GLY G 146 ? 1.854 1.220 1.578 0.102  0.110  0.140  146 GLY GGG C   
8799  O O   . GLY G 146 ? 1.793 1.183 1.533 0.089  0.102  0.144  146 GLY GGG O   
8800  N N   . SER G 147 ? 1.928 1.296 1.664 0.121  0.108  0.138  147 SER GGG N   
8801  C CA  . SER G 147 ? 1.924 1.314 1.687 0.130  0.099  0.143  147 SER GGG CA  
8802  C C   . SER G 147 ? 1.970 1.343 1.728 0.147  0.098  0.138  147 SER GGG C   
8803  O O   . SER G 147 ? 1.966 1.321 1.705 0.152  0.104  0.132  147 SER GGG O   
8804  C CB  . SER G 147 ? 1.986 1.408 1.769 0.130  0.104  0.148  147 SER GGG CB  
8805  O OG  . SER G 147 ? 2.004 1.418 1.783 0.140  0.114  0.145  147 SER GGG OG  
8806  N N   . ARG G 148 ? 2.029 1.407 1.799 0.155  0.092  0.141  148 ARG GGG N   
8807  C CA  . ARG G 148 ? 2.046 1.404 1.804 0.165  0.091  0.136  148 ARG GGG CA  
8808  C C   . ARG G 148 ? 2.021 1.370 1.772 0.176  0.101  0.132  148 ARG GGG C   
8809  O O   . ARG G 148 ? 1.993 1.328 1.728 0.179  0.103  0.125  148 ARG GGG O   
8810  C CB  . ARG G 148 ? 2.128 1.481 1.889 0.172  0.086  0.141  148 ARG GGG CB  
8811  C CG  . ARG G 148 ? 2.346 1.700 2.107 0.161  0.076  0.143  148 ARG GGG CG  
8812  C CD  . ARG G 148 ? 2.654 2.004 2.403 0.149  0.072  0.136  148 ARG GGG CD  
8813  N NE  . ARG G 148 ? 3.048 2.392 2.789 0.140  0.063  0.136  148 ARG GGG NE  
8814  C CZ  . ARG G 148 ? 3.063 2.405 2.789 0.132  0.060  0.129  148 ARG GGG CZ  
8815  N NH1 . ARG G 148 ? 2.900 2.247 2.617 0.136  0.065  0.123  148 ARG GGG NH1 
8816  N NH2 . ARG G 148 ? 3.103 2.440 2.822 0.122  0.052  0.129  148 ARG GGG NH2 
8817  N N   . ASN G 149 ? 2.015 1.377 1.778 0.180  0.109  0.136  149 ASN GGG N   
8818  C CA  . ASN G 149 ? 1.952 1.307 1.709 0.190  0.119  0.132  149 ASN GGG CA  
8819  C C   . ASN G 149 ? 1.914 1.264 1.659 0.184  0.126  0.128  149 ASN GGG C   
8820  O O   . ASN G 149 ? 2.007 1.349 1.745 0.191  0.136  0.125  149 ASN GGG O   
8821  C CB  . ASN G 149 ? 2.037 1.410 1.810 0.201  0.124  0.139  149 ASN GGG CB  
8822  C CG  . ASN G 149 ? 2.110 1.518 1.899 0.189  0.126  0.144  149 ASN GGG CG  
8823  O OD1 . ASN G 149 ? 2.118 1.539 1.913 0.175  0.119  0.147  149 ASN GGG OD1 
8824  N ND2 . ASN G 149 ? 2.185 1.612 1.982 0.191  0.135  0.146  149 ASN GGG ND2 
8825  N N   . GLY G 150 ? 1.849 1.199 1.587 0.170  0.124  0.129  150 GLY GGG N   
8826  C CA  . GLY G 150 ? 1.995 1.326 1.707 0.166  0.133  0.125  150 GLY GGG CA  
8827  C C   . GLY G 150 ? 2.064 1.399 1.773 0.151  0.142  0.127  150 GLY GGG C   
8828  O O   . GLY G 150 ? 2.064 1.373 1.741 0.144  0.151  0.125  150 GLY GGG O   
8829  N N   . LYS G 151 ? 2.055 1.421 1.789 0.145  0.141  0.132  151 LYS GGG N   
8830  C CA  . LYS G 151 ? 2.107 1.488 1.839 0.125  0.150  0.134  151 LYS GGG CA  
8831  C C   . LYS G 151 ? 2.063 1.444 1.784 0.102  0.146  0.136  151 LYS GGG C   
8832  O O   . LYS G 151 ? 2.027 1.420 1.763 0.103  0.134  0.139  151 LYS GGG O   
8833  C CB  . LYS G 151 ? 2.133 1.561 1.896 0.128  0.149  0.140  151 LYS GGG CB  
8834  C CG  . LYS G 151 ? 2.289 1.712 2.057 0.150  0.156  0.138  151 LYS GGG CG  
8835  C CD  . LYS G 151 ? 2.401 1.785 2.137 0.149  0.168  0.131  151 LYS GGG CD  
8836  C CE  . LYS G 151 ? 2.328 1.696 2.065 0.174  0.170  0.128  151 LYS GGG CE  
8837  N NZ  . LYS G 151 ? 2.470 1.804 2.177 0.177  0.181  0.122  151 LYS GGG NZ  
8838  N N   . THR G 152 ? 2.045 1.406 1.735 0.081  0.158  0.133  152 THR GGG N   
8839  C CA  . THR G 152 ? 2.043 1.395 1.715 0.057  0.156  0.134  152 THR GGG CA  
8840  C C   . THR G 152 ? 2.081 1.483 1.773 0.029  0.154  0.138  152 THR GGG C   
8841  O O   . THR G 152 ? 2.224 1.654 1.924 0.020  0.161  0.138  152 THR GGG O   
8842  C CB  . THR G 152 ? 2.122 1.414 1.736 0.047  0.171  0.128  152 THR GGG CB  
8843  O OG1 . THR G 152 ? 2.252 1.537 1.847 0.032  0.186  0.126  152 THR GGG OG1 
8844  C CG2 . THR G 152 ? 2.106 1.359 1.700 0.078  0.172  0.126  152 THR GGG CG2 
8845  N N   . SER G 153 ? 2.036 1.454 1.735 0.016  0.144  0.141  153 SER GGG N   
8846  C CA  . SER G 153 ? 2.041 1.515 1.759 -0.011 0.141  0.146  153 SER GGG CA  
8847  C C   . SER G 153 ? 2.063 1.519 1.739 -0.052 0.153  0.142  153 SER GGG C   
8848  O O   . SER G 153 ? 2.047 1.557 1.734 -0.081 0.154  0.144  153 SER GGG O   
8849  C CB  . SER G 153 ? 2.087 1.587 1.829 -0.007 0.125  0.152  153 SER GGG CB  
8850  O OG  . SER G 153 ? 2.139 1.589 1.851 -0.013 0.123  0.148  153 SER GGG OG  
8851  N N   . LYS G 154 ? 2.089 1.471 1.712 -0.056 0.164  0.135  154 LYS GGG N   
8852  C CA  . LYS G 154 ? 2.236 1.577 1.801 -0.094 0.181  0.130  154 LYS GGG CA  
8853  C C   . LYS G 154 ? 2.322 1.591 1.841 -0.078 0.197  0.124  154 LYS GGG C   
8854  O O   . LYS G 154 ? 2.247 1.499 1.777 -0.039 0.193  0.125  154 LYS GGG O   
8855  C CB  . LYS G 154 ? 2.276 1.585 1.809 -0.114 0.179  0.129  154 LYS GGG CB  
8856  C CG  . LYS G 154 ? 2.289 1.667 1.860 -0.136 0.164  0.135  154 LYS GGG CG  
8857  C CD  . LYS G 154 ? 2.377 1.809 1.949 -0.181 0.170  0.134  154 LYS GGG CD  
8858  C CE  . LYS G 154 ? 2.291 1.814 1.916 -0.189 0.153  0.142  154 LYS GGG CE  
8859  N NZ  . LYS G 154 ? 2.279 1.855 1.966 -0.145 0.139  0.150  154 LYS GGG NZ  
8860  N N   . LYS G 155 ? 2.514 1.741 1.977 -0.108 0.216  0.119  155 LYS GGG N   
8861  C CA  . LYS G 155 ? 2.602 1.758 2.014 -0.091 0.234  0.114  155 LYS GGG CA  
8862  C C   . LYS G 155 ? 2.596 1.671 1.949 -0.075 0.241  0.113  155 LYS GGG C   
8863  O O   . LYS G 155 ? 2.682 1.716 1.985 -0.103 0.249  0.112  155 LYS GGG O   
8864  C CB  . LYS G 155 ? 2.793 1.927 2.160 -0.130 0.254  0.109  155 LYS GGG CB  
8865  C CG  . LYS G 155 ? 2.861 2.083 2.280 -0.151 0.249  0.111  155 LYS GGG CG  
8866  C CD  . LYS G 155 ? 3.026 2.221 2.390 -0.196 0.271  0.104  155 LYS GGG CD  
8867  C CE  . LYS G 155 ? 3.096 2.379 2.510 -0.208 0.269  0.106  155 LYS GGG CE  
8868  N NZ  . LYS G 155 ? 3.159 2.427 2.519 -0.262 0.289  0.099  155 LYS GGG NZ  
8869  N N   . ILE G 156 ? 2.521 1.575 1.877 -0.030 0.239  0.115  156 ILE GGG N   
8870  C CA  . ILE G 156 ? 2.565 1.554 1.869 -0.005 0.245  0.115  156 ILE GGG CA  
8871  C C   . ILE G 156 ? 2.652 1.568 1.887 0.007  0.269  0.112  156 ILE GGG C   
8872  O O   . ILE G 156 ? 2.677 1.604 1.929 0.032  0.270  0.111  156 ILE GGG O   
8873  C CB  . ILE G 156 ? 2.489 1.512 1.839 0.037  0.228  0.119  156 ILE GGG CB  
8874  C CG1 . ILE G 156 ? 2.445 1.537 1.861 0.025  0.206  0.122  156 ILE GGG CG1 
8875  C CG2 . ILE G 156 ? 2.481 1.447 1.776 0.063  0.235  0.120  156 ILE GGG CG2 
8876  C CD1 . ILE G 156 ? 2.366 1.445 1.760 -0.005 0.205  0.123  156 ILE GGG CD1 
8877  N N   . THR G 157 ? 2.728 1.563 1.878 -0.011 0.289  0.110  157 THR GGG N   
8878  C CA  . THR G 157 ? 2.792 1.545 1.862 -0.005 0.315  0.107  157 THR GGG CA  
8879  C C   . THR G 157 ? 2.837 1.509 1.831 0.030  0.328  0.110  157 THR GGG C   
8880  O O   . THR G 157 ? 2.953 1.612 1.932 0.026  0.324  0.113  157 THR GGG O   
8881  C CB  . THR G 157 ? 2.889 1.603 1.906 -0.062 0.333  0.101  157 THR GGG CB  
8882  O OG1 . THR G 157 ? 2.963 1.665 1.957 -0.097 0.331  0.101  157 THR GGG OG1 
8883  C CG2 . THR G 157 ? 2.858 1.654 1.943 -0.089 0.324  0.099  157 THR GGG CG2 
8884  N N   . ILE G 158 ? 2.920 1.542 1.866 0.066  0.343  0.111  158 ILE GGG N   
8885  C CA  . ILE G 158 ? 3.096 1.635 1.956 0.104  0.361  0.116  158 ILE GGG CA  
8886  C C   . ILE G 158 ? 3.394 1.823 2.144 0.072  0.392  0.112  158 ILE GGG C   
8887  O O   . ILE G 158 ? 3.575 1.952 2.275 0.071  0.411  0.109  158 ILE GGG O   
8888  C CB  . ILE G 158 ? 3.034 1.578 1.894 0.162  0.363  0.120  158 ILE GGG CB  
8889  C CG1 . ILE G 158 ? 2.997 1.653 1.967 0.179  0.333  0.121  158 ILE GGG CG1 
8890  C CG2 . ILE G 158 ? 3.042 1.520 1.821 0.208  0.378  0.127  158 ILE GGG CG2 
8891  C CD1 . ILE G 158 ? 3.121 1.797 2.101 0.226  0.333  0.123  158 ILE GGG CD1 
8892  N N   . ALA G 159 ? 3.519 1.906 2.225 0.043  0.397  0.111  159 ALA GGG N   
8893  C CA  . ALA G 159 ? 3.623 1.905 2.222 0.000  0.425  0.106  159 ALA GGG CA  
8894  C C   . ALA G 159 ? 3.821 1.979 2.298 0.041  0.456  0.110  159 ALA GGG C   
8895  O O   . ALA G 159 ? 3.895 1.960 2.279 0.017  0.484  0.105  159 ALA GGG O   
8896  C CB  . ALA G 159 ? 3.635 1.914 2.225 -0.043 0.420  0.104  159 ALA GGG CB  
8897  N N   . ASP G 160 ? 3.962 2.118 2.432 0.104  0.453  0.119  160 ASP GGG N   
8898  C CA  . ASP G 160 ? 4.158 2.204 2.512 0.154  0.483  0.124  160 ASP GGG CA  
8899  C C   . ASP G 160 ? 4.112 2.218 2.509 0.229  0.470  0.134  160 ASP GGG C   
8900  O O   . ASP G 160 ? 3.957 2.166 2.452 0.238  0.441  0.136  160 ASP GGG O   
8901  C CB  . ASP G 160 ? 4.363 2.296 2.603 0.143  0.506  0.126  160 ASP GGG CB  
8902  C CG  . ASP G 160 ? 4.600 2.389 2.693 0.179  0.545  0.130  160 ASP GGG CG  
8903  O OD1 . ASP G 160 ? 4.691 2.469 2.771 0.206  0.555  0.131  160 ASP GGG OD1 
8904  O OD2 . ASP G 160 ? 4.759 2.443 2.744 0.183  0.568  0.133  160 ASP GGG OD2 
8905  N N   . CYS G 161 ? 4.286 2.322 2.602 0.281  0.493  0.140  161 CYS GGG N   
8906  C CA  . CYS G 161 ? 4.324 2.406 2.657 0.356  0.487  0.150  161 CYS GGG CA  
8907  C C   . CYS G 161 ? 4.512 2.473 2.707 0.407  0.523  0.158  161 CYS GGG C   
8908  O O   . CYS G 161 ? 4.673 2.519 2.771 0.382  0.552  0.154  161 CYS GGG O   
8909  C CB  . CYS G 161 ? 4.302 2.502 2.750 0.363  0.461  0.148  161 CYS GGG CB  
8910  S SG  . CYS G 161 ? 4.432 2.611 2.883 0.323  0.470  0.138  161 CYS GGG SG  
8911  N N   . GLY G 162 ? 4.563 2.549 2.746 0.480  0.523  0.169  162 GLY GGG N   
8912  C CA  . GLY G 162 ? 4.713 2.593 2.765 0.541  0.558  0.179  162 GLY GGG CA  
8913  C C   . GLY G 162 ? 4.741 2.685 2.802 0.619  0.551  0.193  162 GLY GGG C   
8914  O O   . GLY G 162 ? 4.526 2.601 2.700 0.622  0.519  0.193  162 GLY GGG O   
8915  N N   . GLN G 163 ? 4.854 2.702 2.789 0.682  0.583  0.205  163 GLN GGG N   
8916  C CA  . GLN G 163 ? 4.995 2.907 2.927 0.764  0.580  0.220  163 GLN GGG CA  
8917  C C   . GLN G 163 ? 5.116 2.979 2.978 0.793  0.592  0.229  163 GLN GGG C   
8918  O O   . GLN G 163 ? 5.353 3.066 3.082 0.796  0.626  0.232  163 GLN GGG O   
8919  C CB  . GLN G 163 ? 5.050 2.908 2.893 0.832  0.606  0.230  163 GLN GGG CB  
8920  C CG  . GLN G 163 ? 5.095 3.024 2.925 0.925  0.607  0.247  163 GLN GGG CG  
8921  C CD  . GLN G 163 ? 4.970 3.084 2.943 0.933  0.568  0.247  163 GLN GGG CD  
8922  O OE1 . GLN G 163 ? 4.962 3.155 2.937 1.001  0.565  0.259  163 GLN GGG OE1 
8923  N NE2 . GLN G 163 ? 4.997 3.182 3.085 0.866  0.541  0.232  163 GLN GGG NE2 
8924  N N   . LEU G 164 ? 4.949 2.938 2.899 0.812  0.565  0.234  164 LEU GGG N   
8925  C CA  . LEU G 164 ? 4.967 2.954 2.875 0.854  0.571  0.245  164 LEU GGG CA  
8926  C C   . LEU G 164 ? 5.044 3.079 2.915 0.951  0.580  0.262  164 LEU GGG C   
8927  O O   . LEU G 164 ? 5.021 3.119 2.927 0.976  0.574  0.264  164 LEU GGG O   
8928  C CB  . LEU G 164 ? 4.764 2.864 2.794 0.809  0.535  0.239  164 LEU GGG CB  
8929  C CG  . LEU G 164 ? 4.612 2.652 2.658 0.721  0.530  0.224  164 LEU GGG CG  
8930  C CD1 . LEU G 164 ? 4.317 2.472 2.487 0.677  0.494  0.218  164 LEU GGG CD1 
8931  C CD2 . LEU G 164 ? 4.729 2.603 2.629 0.719  0.566  0.227  164 LEU GGG CD2 
8932  N N   . GLU G 165 ? 5.108 3.119 2.908 1.006  0.595  0.276  165 GLU GGG N   
8933  C CA  . GLU G 165 ? 5.233 3.305 2.999 1.102  0.603  0.294  165 GLU GGG CA  
8934  C C   . GLU G 165 ? 5.187 3.453 3.085 1.111  0.566  0.296  165 GLU GGG C   
8935  O O   . GLU G 165 ? 5.151 3.534 3.106 1.144  0.552  0.300  165 GLU GGG O   
8936  C CB  . GLU G 165 ? 5.357 3.303 2.965 1.170  0.643  0.311  165 GLU GGG CB  
8937  C CG  . GLU G 165 ? 5.340 3.292 2.948 1.165  0.638  0.314  165 GLU GGG CG  
8938  C CD  . GLU G 165 ? 5.303 3.160 2.910 1.074  0.637  0.298  165 GLU GGG CD  
8939  O OE1 . GLU G 165 ? 5.379 3.110 2.922 1.034  0.656  0.289  165 GLU GGG OE1 
8940  O OE2 . GLU G 165 ? 5.200 3.116 2.874 1.041  0.616  0.294  165 GLU GGG OE2 
8941  O OXT . GLU G 165 ? 5.279 3.593 3.231 1.082  0.548  0.293  165 GLU GGG OXT 
8942  N N   . ASN H 3   ? 5.361 3.405 2.264 -1.350 0.249  -0.146 3   ASN HHH N   
8943  C CA  . ASN H 3   ? 5.184 3.388 2.282 -1.293 0.242  -0.145 3   ASN HHH CA  
8944  C C   . ASN H 3   ? 5.192 3.533 2.354 -1.371 0.255  -0.154 3   ASN HHH C   
8945  O O   . ASN H 3   ? 5.273 3.566 2.383 -1.391 0.261  -0.149 3   ASN HHH O   
8946  C CB  . ASN H 3   ? 5.161 3.257 2.228 -1.210 0.234  -0.129 3   ASN HHH CB  
8947  C CG  . ASN H 3   ? 5.123 3.172 2.216 -1.106 0.218  -0.123 3   ASN HHH CG  
8948  O OD1 . ASN H 3   ? 5.254 3.298 2.337 -1.101 0.213  -0.129 3   ASN HHH OD1 
8949  N ND2 . ASN H 3   ? 5.039 3.058 2.162 -1.023 0.209  -0.113 3   ASN HHH ND2 
8950  N N   . PRO H 4   ? 5.030 3.542 2.301 -1.413 0.258  -0.169 4   PRO HHH N   
8951  C CA  . PRO H 4   ? 5.012 3.673 2.347 -1.484 0.269  -0.181 4   PRO HHH CA  
8952  C C   . PRO H 4   ? 4.975 3.772 2.485 -1.420 0.262  -0.177 4   PRO HHH C   
8953  O O   . PRO H 4   ? 5.051 3.833 2.637 -1.327 0.250  -0.165 4   PRO HHH O   
8954  C CB  . PRO H 4   ? 4.902 3.702 2.301 -1.528 0.271  -0.198 4   PRO HHH CB  
8955  C CG  . PRO H 4   ? 4.871 3.658 2.329 -1.447 0.257  -0.194 4   PRO HHH CG  
8956  C CD  . PRO H 4   ? 4.936 3.541 2.314 -1.372 0.248  -0.176 4   PRO HHH CD  
8957  N N   . THR H 5   ? 5.051 3.984 2.620 -1.474 0.270  -0.188 5   THR HHH N   
8958  C CA  . THR H 5   ? 4.827 3.895 2.554 -1.423 0.266  -0.185 5   THR HHH CA  
8959  C C   . THR H 5   ? 4.590 3.877 2.464 -1.438 0.265  -0.203 5   THR HHH C   
8960  O O   . THR H 5   ? 4.758 4.110 2.592 -1.520 0.274  -0.220 5   THR HHH O   
8961  C CB  . THR H 5   ? 5.000 4.031 2.662 -1.462 0.275  -0.182 5   THR HHH CB  
8962  O OG1 . THR H 5   ? 5.254 4.067 2.735 -1.473 0.278  -0.170 5   THR HHH OG1 
8963  C CG2 . THR H 5   ? 4.819 3.937 2.622 -1.388 0.269  -0.172 5   THR HHH CG2 
8964  N N   . VAL H 6   ? 4.392 3.793 2.434 -1.359 0.254  -0.200 6   VAL HHH N   
8965  C CA  . VAL H 6   ? 4.091 3.692 2.276 -1.356 0.250  -0.216 6   VAL HHH CA  
8966  C C   . VAL H 6   ? 3.933 3.641 2.249 -1.305 0.247  -0.211 6   VAL HHH C   
8967  O O   . VAL H 6   ? 3.875 3.514 2.218 -1.241 0.242  -0.193 6   VAL HHH O   
8968  C CB  . VAL H 6   ? 3.864 3.489 2.119 -1.307 0.239  -0.219 6   VAL HHH CB  
8969  C CG1 . VAL H 6   ? 3.709 3.529 2.126 -1.279 0.232  -0.233 6   VAL HHH CG1 
8970  C CG2 . VAL H 6   ? 3.916 3.466 2.048 -1.367 0.244  -0.227 6   VAL HHH CG2 
8971  N N   . PHE H 7   ? 3.647 3.526 2.041 -1.331 0.249  -0.228 7   PHE HHH N   
8972  C CA  . PHE H 7   ? 3.501 3.488 2.005 -1.291 0.246  -0.226 7   PHE HHH CA  
8973  C C   . PHE H 7   ? 3.329 3.484 1.979 -1.249 0.237  -0.238 7   PHE HHH C   
8974  O O   . PHE H 7   ? 3.375 3.613 2.031 -1.282 0.236  -0.257 7   PHE HHH O   
8975  C CB  . PHE H 7   ? 3.742 3.771 2.183 -1.363 0.258  -0.235 7   PHE HHH CB  
8976  C CG  . PHE H 7   ? 3.906 4.107 2.373 -1.421 0.262  -0.262 7   PHE HHH CG  
8977  C CD1 . PHE H 7   ? 3.900 4.278 2.495 -1.385 0.256  -0.272 7   PHE HHH CD1 
8978  C CD2 . PHE H 7   ? 4.159 4.345 2.517 -1.512 0.272  -0.277 7   PHE HHH CD2 
8979  C CE1 . PHE H 7   ? 3.968 4.513 2.585 -1.434 0.259  -0.299 7   PHE HHH CE1 
8980  C CE2 . PHE H 7   ? 4.197 4.554 2.579 -1.568 0.276  -0.303 7   PHE HHH CE2 
8981  C CZ  . PHE H 7   ? 4.060 4.601 2.573 -1.527 0.269  -0.315 7   PHE HHH CZ  
8982  N N   . PHE H 8   ? 3.051 3.251 1.814 -1.174 0.229  -0.228 8   PHE HHH N   
8983  C CA  . PHE H 8   ? 2.959 3.308 1.855 -1.128 0.219  -0.239 8   PHE HHH CA  
8984  C C   . PHE H 8   ? 2.789 3.229 1.746 -1.107 0.221  -0.237 8   PHE HHH C   
8985  O O   . PHE H 8   ? 2.819 3.187 1.777 -1.076 0.223  -0.218 8   PHE HHH O   
8986  C CB  . PHE H 8   ? 2.964 3.273 1.944 -1.048 0.207  -0.227 8   PHE HHH CB  
8987  C CG  . PHE H 8   ? 3.034 3.296 1.987 -1.054 0.202  -0.233 8   PHE HHH CG  
8988  C CD1 . PHE H 8   ? 3.345 3.522 2.174 -1.117 0.209  -0.237 8   PHE HHH CD1 
8989  C CD2 . PHE H 8   ? 2.798 3.095 1.848 -0.994 0.189  -0.235 8   PHE HHH CD2 
8990  C CE1 . PHE H 8   ? 3.467 3.600 2.270 -1.118 0.204  -0.242 8   PHE HHH CE1 
8991  C CE2 . PHE H 8   ? 2.862 3.121 1.892 -0.996 0.183  -0.241 8   PHE HHH CE2 
8992  C CZ  . PHE H 8   ? 3.174 3.352 2.081 -1.056 0.191  -0.244 8   PHE HHH CZ  
8993  N N   . ASP H 9   ? 2.777 3.378 1.785 -1.120 0.219  -0.258 9   ASP HHH N   
8994  C CA  . ASP H 9   ? 2.711 3.418 1.796 -1.081 0.217  -0.259 9   ASP HHH CA  
8995  C C   . ASP H 9   ? 2.539 3.313 1.745 -1.001 0.203  -0.260 9   ASP HHH C   
8996  O O   . ASP H 9   ? 2.483 3.344 1.724 -0.997 0.196  -0.278 9   ASP HHH O   
8997  C CB  . ASP H 9   ? 2.921 3.771 1.982 -1.139 0.222  -0.284 9   ASP HHH CB  
8998  C CG  . ASP H 9   ? 3.083 3.877 2.039 -1.208 0.236  -0.282 9   ASP HHH CG  
8999  O OD1 . ASP H 9   ? 3.174 3.811 2.046 -1.232 0.242  -0.266 9   ASP HHH OD1 
9000  O OD2 . ASP H 9   ? 3.079 3.986 2.033 -1.237 0.240  -0.297 9   ASP HHH OD2 
9001  N N   . ILE H 10  ? 2.398 3.130 1.660 -0.938 0.200  -0.239 10  ILE HHH N   
9002  C CA  . ILE H 10  ? 2.057 2.815 1.421 -0.861 0.188  -0.235 10  ILE HHH CA  
9003  C C   . ILE H 10  ? 1.936 2.818 1.359 -0.828 0.185  -0.243 10  ILE HHH C   
9004  O O   . ILE H 10  ? 1.986 2.884 1.385 -0.840 0.192  -0.238 10  ILE HHH O   
9005  C CB  . ILE H 10  ? 1.984 2.613 1.369 -0.816 0.189  -0.207 10  ILE HHH CB  
9006  C CG1 . ILE H 10  ? 2.078 2.587 1.393 -0.846 0.191  -0.201 10  ILE HHH CG1 
9007  C CG2 . ILE H 10  ? 2.057 2.709 1.541 -0.746 0.177  -0.204 10  ILE HHH CG2 
9008  C CD1 . ILE H 10  ? 2.348 2.878 1.680 -0.847 0.182  -0.216 10  ILE HHH CD1 
9009  N N   . ALA H 11  ? 1.852 2.819 1.346 -0.782 0.173  -0.256 11  ALA HHH N   
9010  C CA  . ALA H 11  ? 1.800 2.876 1.347 -0.737 0.167  -0.263 11  ALA HHH CA  
9011  C C   . ALA H 11  ? 1.697 2.740 1.321 -0.659 0.157  -0.252 11  ALA HHH C   
9012  O O   . ALA H 11  ? 1.822 2.809 1.470 -0.644 0.150  -0.250 11  ALA HHH O   
9013  C CB  . ALA H 11  ? 2.038 3.273 1.584 -0.757 0.162  -0.296 11  ALA HHH CB  
9014  N N   . VAL H 12  ? 1.717 2.795 1.376 -0.610 0.155  -0.245 12  VAL HHH N   
9015  C CA  . VAL H 12  ? 1.819 2.862 1.543 -0.538 0.146  -0.234 12  VAL HHH CA  
9016  C C   . VAL H 12  ? 1.895 3.056 1.648 -0.490 0.135  -0.252 12  VAL HHH C   
9017  O O   . VAL H 12  ? 2.033 3.255 1.776 -0.479 0.138  -0.253 12  VAL HHH O   
9018  C CB  . VAL H 12  ? 1.771 2.711 1.502 -0.515 0.154  -0.203 12  VAL HHH CB  
9019  C CG1 . VAL H 12  ? 1.708 2.614 1.498 -0.447 0.147  -0.192 12  VAL HHH CG1 
9020  C CG2 . VAL H 12  ? 1.833 2.657 1.532 -0.553 0.163  -0.186 12  VAL HHH CG2 
9021  N N   . ASP H 13  ? 1.918 3.109 1.706 -0.456 0.122  -0.267 13  ASP HHH N   
9022  C CA  . ASP H 13  ? 2.037 3.345 1.846 -0.407 0.109  -0.289 13  ASP HHH CA  
9023  C C   . ASP H 13  ? 2.174 3.627 1.949 -0.440 0.112  -0.312 13  ASP HHH C   
9024  O O   . ASP H 13  ? 2.228 3.771 2.007 -0.399 0.106  -0.322 13  ASP HHH O   
9025  C CB  . ASP H 13  ? 2.064 3.328 1.900 -0.336 0.105  -0.272 13  ASP HHH CB  
9026  C CG  . ASP H 13  ? 2.201 3.529 2.060 -0.268 0.087  -0.291 13  ASP HHH CG  
9027  O OD1 . ASP H 13  ? 2.411 3.877 2.259 -0.257 0.080  -0.317 13  ASP HHH OD1 
9028  O OD2 . ASP H 13  ? 2.127 3.368 2.014 -0.225 0.080  -0.281 13  ASP HHH OD2 
9029  N N   . GLY H 14  ? 2.176 3.652 1.912 -0.515 0.120  -0.322 14  GLY HHH N   
9030  C CA  . GLY H 14  ? 2.121 3.731 1.819 -0.562 0.125  -0.345 14  GLY HHH CA  
9031  C C   . GLY H 14  ? 2.127 3.723 1.788 -0.595 0.138  -0.332 14  GLY HHH C   
9032  O O   . GLY H 14  ? 2.213 3.922 1.839 -0.642 0.144  -0.352 14  GLY HHH O   
9033  N N   . GLU H 15  ? 2.055 3.520 1.721 -0.575 0.144  -0.301 15  GLU HHH N   
9034  C CA  . GLU H 15  ? 1.998 3.439 1.629 -0.602 0.157  -0.287 15  GLU HHH CA  
9035  C C   . GLU H 15  ? 1.954 3.280 1.533 -0.670 0.170  -0.272 15  GLU HHH C   
9036  O O   . GLU H 15  ? 2.050 3.255 1.640 -0.662 0.169  -0.255 15  GLU HHH O   
9037  C CB  . GLU H 15  ? 1.932 3.307 1.597 -0.533 0.156  -0.262 15  GLU HHH CB  
9038  C CG  . GLU H 15  ? 1.945 3.410 1.651 -0.457 0.142  -0.275 15  GLU HHH CG  
9039  C CD  . GLU H 15  ? 1.918 3.320 1.644 -0.393 0.142  -0.251 15  GLU HHH CD  
9040  O OE1 . GLU H 15  ? 1.888 3.237 1.594 -0.412 0.154  -0.231 15  GLU HHH OE1 
9041  O OE2 . GLU H 15  ? 1.941 3.346 1.699 -0.324 0.131  -0.251 15  GLU HHH OE2 
9042  N N   . PRO H 16  ? 1.956 3.314 1.475 -0.736 0.180  -0.280 16  PRO HHH N   
9043  C CA  . PRO H 16  ? 2.019 3.260 1.471 -0.802 0.191  -0.269 16  PRO HHH CA  
9044  C C   . PRO H 16  ? 2.087 3.176 1.541 -0.774 0.197  -0.235 16  PRO HHH C   
9045  O O   . PRO H 16  ? 2.082 3.169 1.564 -0.729 0.197  -0.221 16  PRO HHH O   
9046  C CB  . PRO H 16  ? 2.113 3.431 1.500 -0.872 0.201  -0.285 16  PRO HHH CB  
9047  C CG  . PRO H 16  ? 2.084 3.523 1.511 -0.825 0.196  -0.293 16  PRO HHH CG  
9048  C CD  . PRO H 16  ? 2.094 3.593 1.595 -0.752 0.182  -0.301 16  PRO HHH CD  
9049  N N   . LEU H 17  ? 2.128 3.093 1.550 -0.799 0.201  -0.222 17  LEU HHH N   
9050  C CA  . LEU H 17  ? 2.176 3.001 1.599 -0.771 0.205  -0.192 17  LEU HHH CA  
9051  C C   . LEU H 17  ? 2.156 2.880 1.486 -0.828 0.216  -0.183 17  LEU HHH C   
9052  O O   . LEU H 17  ? 2.195 2.866 1.505 -0.821 0.224  -0.166 17  LEU HHH O   
9053  C CB  . LEU H 17  ? 2.189 2.947 1.662 -0.730 0.197  -0.183 17  LEU HHH CB  
9054  C CG  . LEU H 17  ? 2.031 2.657 1.508 -0.702 0.202  -0.154 17  LEU HHH CG  
9055  C CD1 . LEU H 17  ? 2.015 2.658 1.535 -0.655 0.204  -0.138 17  LEU HHH CD1 
9056  C CD2 . LEU H 17  ? 2.089 2.656 1.609 -0.671 0.195  -0.148 17  LEU HHH CD2 
9057  N N   . GLY H 18  ? 2.194 2.881 1.462 -0.883 0.218  -0.193 18  GLY HHH N   
9058  C CA  . GLY H 18  ? 2.306 2.885 1.472 -0.936 0.228  -0.186 18  GLY HHH CA  
9059  C C   . GLY H 18  ? 2.401 2.921 1.504 -0.982 0.228  -0.195 18  GLY HHH C   
9060  O O   . GLY H 18  ? 2.319 2.884 1.464 -0.971 0.220  -0.206 18  GLY HHH O   
9061  N N   . ARG H 19  ? 2.531 2.941 1.525 -1.033 0.237  -0.189 19  ARG HHH N   
9062  C CA  . ARG H 19  ? 2.770 3.106 1.678 -1.085 0.239  -0.196 19  ARG HHH CA  
9063  C C   . ARG H 19  ? 2.805 2.973 1.668 -1.057 0.238  -0.175 19  ARG HHH C   
9064  O O   . ARG H 19  ? 2.818 2.900 1.639 -1.046 0.244  -0.158 19  ARG HHH O   
9065  C CB  . ARG H 19  ? 2.983 3.323 1.778 -1.176 0.250  -0.211 19  ARG HHH CB  
9066  C CG  . ARG H 19  ? 3.107 3.374 1.803 -1.238 0.253  -0.221 19  ARG HHH CG  
9067  C CD  . ARG H 19  ? 3.244 3.340 1.796 -1.283 0.262  -0.209 19  ARG HHH CD  
9068  N NE  . ARG H 19  ? 3.387 3.507 1.873 -1.343 0.272  -0.217 19  ARG HHH NE  
9069  C CZ  . ARG H 19  ? 3.520 3.501 1.885 -1.377 0.279  -0.207 19  ARG HHH CZ  
9070  N NH1 . ARG H 19  ? 3.636 3.443 1.927 -1.355 0.278  -0.190 19  ARG HHH NH1 
9071  N NH2 . ARG H 19  ? 3.501 3.518 1.814 -1.433 0.288  -0.217 19  ARG HHH NH2 
9072  N N   . VAL H 20  ? 2.974 3.102 1.844 -1.042 0.232  -0.176 20  VAL HHH N   
9073  C CA  . VAL H 20  ? 3.039 3.023 1.872 -1.009 0.230  -0.158 20  VAL HHH CA  
9074  C C   . VAL H 20  ? 3.294 3.187 2.004 -1.066 0.233  -0.166 20  VAL HHH C   
9075  O O   . VAL H 20  ? 3.357 3.308 2.073 -1.095 0.230  -0.183 20  VAL HHH O   
9076  C CB  . VAL H 20  ? 2.755 2.761 1.699 -0.937 0.219  -0.153 20  VAL HHH CB  
9077  C CG1 . VAL H 20  ? 2.832 2.702 1.729 -0.908 0.215  -0.140 20  VAL HHH CG1 
9078  C CG2 . VAL H 20  ? 2.686 2.759 1.736 -0.882 0.217  -0.142 20  VAL HHH CG2 
9079  N N   . SER H 21  ? 3.379 3.127 1.972 -1.082 0.238  -0.155 21  SER HHH N   
9080  C CA  . SER H 21  ? 3.578 3.212 2.036 -1.133 0.241  -0.160 21  SER HHH CA  
9081  C C   . SER H 21  ? 3.567 3.089 2.010 -1.077 0.233  -0.148 21  SER HHH C   
9082  O O   . SER H 21  ? 3.513 2.987 1.991 -1.013 0.229  -0.131 21  SER HHH O   
9083  C CB  . SER H 21  ? 3.842 3.371 2.155 -1.191 0.252  -0.157 21  SER HHH CB  
9084  O OG  . SER H 21  ? 3.964 3.373 2.241 -1.141 0.251  -0.137 21  SER HHH OG  
9085  N N   . PHE H 22  ? 3.606 3.090 1.995 -1.101 0.231  -0.157 22  PHE HHH N   
9086  C CA  . PHE H 22  ? 3.702 3.069 2.050 -1.056 0.223  -0.148 22  PHE HHH CA  
9087  C C   . PHE H 22  ? 3.947 3.176 2.118 -1.116 0.229  -0.151 22  PHE HHH C   
9088  O O   . PHE H 22  ? 4.023 3.288 2.141 -1.193 0.237  -0.166 22  PHE HHH O   
9089  C CB  . PHE H 22  ? 3.631 3.072 2.084 -1.015 0.212  -0.156 22  PHE HHH CB  
9090  C CG  . PHE H 22  ? 3.500 3.093 2.123 -0.973 0.206  -0.158 22  PHE HHH CG  
9091  C CD1 . PHE H 22  ? 3.406 3.134 2.086 -1.009 0.210  -0.171 22  PHE HHH CD1 
9092  C CD2 . PHE H 22  ? 3.462 3.061 2.181 -0.896 0.197  -0.149 22  PHE HHH CD2 
9093  C CE1 . PHE H 22  ? 3.268 3.121 2.090 -0.966 0.204  -0.173 22  PHE HHH CE1 
9094  C CE2 . PHE H 22  ? 3.319 3.041 2.181 -0.860 0.192  -0.150 22  PHE HHH CE2 
9095  C CZ  . PHE H 22  ? 3.231 3.074 2.141 -0.893 0.195  -0.162 22  PHE HHH CZ  
9096  N N   . GLU H 23  ? 4.242 3.314 2.317 -1.080 0.226  -0.139 23  GLU HHH N   
9097  C CA  . GLU H 23  ? 4.548 3.461 2.444 -1.122 0.230  -0.139 23  GLU HHH CA  
9098  C C   . GLU H 23  ? 4.525 3.426 2.455 -1.070 0.218  -0.141 23  GLU HHH C   
9099  O O   . GLU H 23  ? 4.526 3.452 2.553 -0.989 0.208  -0.134 23  GLU HHH O   
9100  C CB  . GLU H 23  ? 4.818 3.564 2.578 -1.109 0.232  -0.125 23  GLU HHH CB  
9101  C CG  . GLU H 23  ? 5.206 3.771 2.763 -1.156 0.237  -0.126 23  GLU HHH CG  
9102  C CD  . GLU H 23  ? 5.493 4.053 2.956 -1.261 0.251  -0.135 23  GLU HHH CD  
9103  O OE1 . GLU H 23  ? 5.480 4.172 3.041 -1.281 0.256  -0.139 23  GLU HHH OE1 
9104  O OE2 . GLU H 23  ? 5.881 4.304 3.170 -1.324 0.258  -0.137 23  GLU HHH OE2 
9105  N N   . LEU H 24  ? 4.577 3.442 2.427 -1.117 0.220  -0.151 24  LEU HHH N   
9106  C CA  . LEU H 24  ? 4.473 3.330 2.352 -1.070 0.209  -0.154 24  LEU HHH CA  
9107  C C   . LEU H 24  ? 4.708 3.370 2.417 -1.056 0.206  -0.147 24  LEU HHH C   
9108  O O   . LEU H 24  ? 5.068 3.609 2.610 -1.121 0.215  -0.147 24  LEU HHH O   
9109  C CB  . LEU H 24  ? 4.427 3.397 2.350 -1.124 0.211  -0.172 24  LEU HHH CB  
9110  C CG  . LEU H 24  ? 4.230 3.402 2.308 -1.144 0.212  -0.183 24  LEU HHH CG  
9111  C CD1 . LEU H 24  ? 4.219 3.474 2.308 -1.191 0.213  -0.201 24  LEU HHH CD1 
9112  C CD2 . LEU H 24  ? 4.025 3.294 2.273 -1.061 0.201  -0.179 24  LEU HHH CD2 
9113  N N   . PHE H 25  ? 4.488 3.123 2.239 -0.968 0.192  -0.142 25  PHE HHH N   
9114  C CA  . PHE H 25  ? 4.697 3.154 2.303 -0.925 0.186  -0.134 25  PHE HHH CA  
9115  C C   . PHE H 25  ? 5.017 3.429 2.556 -0.941 0.183  -0.143 25  PHE HHH C   
9116  O O   . PHE H 25  ? 5.211 3.629 2.792 -0.876 0.170  -0.146 25  PHE HHH O   
9117  C CB  . PHE H 25  ? 4.496 2.951 2.174 -0.823 0.174  -0.126 25  PHE HHH CB  
9118  C CG  . PHE H 25  ? 4.468 2.925 2.167 -0.807 0.179  -0.115 25  PHE HHH CG  
9119  C CD1 . PHE H 25  ? 4.311 2.924 2.173 -0.809 0.182  -0.115 25  PHE HHH CD1 
9120  C CD2 . PHE H 25  ? 4.623 2.914 2.166 -0.790 0.180  -0.104 25  PHE HHH CD2 
9121  C CE1 . PHE H 25  ? 4.221 2.829 2.094 -0.794 0.186  -0.104 25  PHE HHH CE1 
9122  C CE2 . PHE H 25  ? 4.493 2.780 2.047 -0.774 0.184  -0.094 25  PHE HHH CE2 
9123  C CZ  . PHE H 25  ? 4.286 2.735 2.009 -0.778 0.188  -0.094 25  PHE HHH CZ  
9124  N N   . ALA H 26  ? 5.125 3.499 2.557 -1.034 0.195  -0.149 26  ALA HHH N   
9125  C CA  . ALA H 26  ? 5.079 3.414 2.431 -1.074 0.196  -0.157 26  ALA HHH CA  
9126  C C   . ALA H 26  ? 5.216 3.349 2.396 -1.032 0.190  -0.149 26  ALA HHH C   
9127  O O   . ALA H 26  ? 5.271 3.362 2.392 -1.039 0.187  -0.155 26  ALA HHH O   
9128  C CB  . ALA H 26  ? 5.036 3.377 2.304 -1.191 0.214  -0.164 26  ALA HHH CB  
9129  N N   . ASP H 27  ? 5.265 3.269 2.356 -0.988 0.187  -0.137 27  ASP HHH N   
9130  C CA  . ASP H 27  ? 5.425 3.233 2.347 -0.935 0.179  -0.130 27  ASP HHH CA  
9131  C C   . ASP H 27  ? 5.350 3.203 2.362 -0.835 0.161  -0.133 27  ASP HHH C   
9132  O O   . ASP H 27  ? 5.591 3.305 2.470 -0.797 0.154  -0.132 27  ASP HHH O   
9133  C CB  . ASP H 27  ? 5.416 3.100 2.242 -0.903 0.180  -0.117 27  ASP HHH CB  
9134  C CG  . ASP H 27  ? 5.190 3.000 2.193 -0.825 0.171  -0.114 27  ASP HHH CG  
9135  O OD1 . ASP H 27  ? 5.122 3.124 2.316 -0.839 0.173  -0.120 27  ASP HHH OD1 
9136  O OD2 . ASP H 27  ? 5.139 2.854 2.082 -0.753 0.164  -0.105 27  ASP HHH OD2 
9137  N N   . LYS H 28  ? 5.196 3.232 2.422 -0.790 0.154  -0.138 28  LYS HHH N   
9138  C CA  . LYS H 28  ? 5.104 3.198 2.423 -0.706 0.137  -0.144 28  LYS HHH CA  
9139  C C   . LYS H 28  ? 5.063 3.296 2.499 -0.735 0.135  -0.158 28  LYS HHH C   
9140  O O   . LYS H 28  ? 4.965 3.182 2.390 -0.695 0.124  -0.165 28  LYS HHH O   
9141  C CB  . LYS H 28  ? 4.884 3.076 2.352 -0.626 0.128  -0.141 28  LYS HHH CB  
9142  C CG  . LYS H 28  ? 4.897 2.961 2.257 -0.581 0.127  -0.129 28  LYS HHH CG  
9143  C CD  . LYS H 28  ? 5.035 2.926 2.220 -0.526 0.117  -0.128 28  LYS HHH CD  
9144  C CE  . LYS H 28  ? 5.068 2.842 2.153 -0.463 0.113  -0.118 28  LYS HHH CE  
9145  N NZ  . LYS H 28  ? 5.143 2.800 2.093 -0.530 0.127  -0.108 28  LYS HHH NZ  
9146  N N   . VAL H 29  ? 5.127 3.496 2.671 -0.799 0.145  -0.163 29  VAL HHH N   
9147  C CA  . VAL H 29  ? 4.996 3.507 2.657 -0.824 0.143  -0.178 29  VAL HHH CA  
9148  C C   . VAL H 29  ? 4.998 3.544 2.620 -0.930 0.159  -0.182 29  VAL HHH C   
9149  O O   . VAL H 29  ? 4.904 3.595 2.652 -0.960 0.164  -0.187 29  VAL HHH O   
9150  C CB  . VAL H 29  ? 4.787 3.476 2.669 -0.771 0.133  -0.183 29  VAL HHH CB  
9151  C CG1 . VAL H 29  ? 4.759 3.433 2.680 -0.677 0.116  -0.184 29  VAL HHH CG1 
9152  C CG2 . VAL H 29  ? 4.813 3.546 2.759 -0.772 0.140  -0.174 29  VAL HHH CG2 
9153  N N   . PRO H 30  ? 5.020 3.440 2.467 -0.989 0.168  -0.182 30  PRO HHH N   
9154  C CA  . PRO H 30  ? 5.007 3.466 2.411 -1.098 0.185  -0.188 30  PRO HHH CA  
9155  C C   . PRO H 30  ? 4.864 3.514 2.413 -1.124 0.185  -0.205 30  PRO HHH C   
9156  O O   . PRO H 30  ? 4.792 3.562 2.405 -1.184 0.195  -0.212 30  PRO HHH O   
9157  C CB  . PRO H 30  ? 5.292 3.557 2.467 -1.147 0.194  -0.184 30  PRO HHH CB  
9158  C CG  . PRO H 30  ? 5.328 3.497 2.462 -1.059 0.178  -0.180 30  PRO HHH CG  
9159  C CD  . PRO H 30  ? 5.141 3.367 2.407 -0.962 0.164  -0.176 30  PRO HHH CD  
9160  N N   . LYS H 31  ? 4.813 3.497 2.413 -1.079 0.173  -0.212 31  LYS HHH N   
9161  C CA  . LYS H 31  ? 4.657 3.519 2.392 -1.099 0.171  -0.229 31  LYS HHH CA  
9162  C C   . LYS H 31  ? 4.534 3.565 2.461 -1.070 0.166  -0.233 31  LYS HHH C   
9163  O O   . LYS H 31  ? 4.537 3.710 2.542 -1.118 0.172  -0.245 31  LYS HHH O   
9164  C CB  . LYS H 31  ? 4.510 3.376 2.274 -1.044 0.156  -0.237 31  LYS HHH CB  
9165  C CG  . LYS H 31  ? 4.647 3.381 2.237 -1.082 0.162  -0.236 31  LYS HHH CG  
9166  C CD  . LYS H 31  ? 4.663 3.390 2.286 -1.009 0.144  -0.242 31  LYS HHH CD  
9167  C CE  . LYS H 31  ? 4.468 3.394 2.277 -0.995 0.136  -0.260 31  LYS HHH CE  
9168  N NZ  . LYS H 31  ? 4.368 3.293 2.201 -0.936 0.120  -0.268 31  LYS HHH NZ  
9169  N N   . THR H 32  ? 4.478 3.499 2.478 -0.992 0.155  -0.224 32  THR HHH N   
9170  C CA  . THR H 32  ? 4.234 3.403 2.409 -0.963 0.151  -0.227 32  THR HHH CA  
9171  C C   . THR H 32  ? 4.171 3.363 2.330 -1.017 0.165  -0.222 32  THR HHH C   
9172  O O   . THR H 32  ? 4.030 3.368 2.303 -1.035 0.167  -0.230 32  THR HHH O   
9173  C CB  . THR H 32  ? 4.212 3.362 2.463 -0.871 0.138  -0.219 32  THR HHH CB  
9174  O OG1 . THR H 32  ? 4.252 3.379 2.507 -0.822 0.124  -0.225 32  THR HHH OG1 
9175  C CG2 . THR H 32  ? 4.007 3.308 2.438 -0.841 0.133  -0.222 32  THR HHH CG2 
9176  N N   . ALA H 33  ? 4.296 3.341 2.309 -1.042 0.174  -0.209 33  ALA HHH N   
9177  C CA  . ALA H 33  ? 4.334 3.394 2.317 -1.100 0.188  -0.205 33  ALA HHH CA  
9178  C C   . ALA H 33  ? 4.385 3.533 2.349 -1.192 0.200  -0.220 33  ALA HHH C   
9179  O O   . ALA H 33  ? 4.312 3.590 2.358 -1.222 0.205  -0.227 33  ALA HHH O   
9180  C CB  . ALA H 33  ? 4.539 3.409 2.350 -1.112 0.195  -0.191 33  ALA HHH CB  
9181  N N   . GLU H 34  ? 4.517 3.600 2.370 -1.236 0.204  -0.226 34  GLU HHH N   
9182  C CA  . GLU H 34  ? 4.549 3.719 2.373 -1.329 0.217  -0.241 34  GLU HHH CA  
9183  C C   . GLU H 34  ? 4.377 3.759 2.381 -1.311 0.209  -0.258 34  GLU HHH C   
9184  O O   . GLU H 34  ? 4.411 3.924 2.455 -1.367 0.218  -0.271 34  GLU HHH O   
9185  C CB  . GLU H 34  ? 4.653 3.707 2.322 -1.377 0.222  -0.243 34  GLU HHH CB  
9186  C CG  . GLU H 34  ? 4.652 3.806 2.294 -1.475 0.236  -0.260 34  GLU HHH CG  
9187  C CD  . GLU H 34  ? 4.666 3.828 2.241 -1.561 0.253  -0.261 34  GLU HHH CD  
9188  O OE1 . GLU H 34  ? 4.835 3.823 2.256 -1.590 0.261  -0.248 34  GLU HHH OE1 
9189  O OE2 . GLU H 34  ? 4.589 3.932 2.264 -1.596 0.258  -0.277 34  GLU HHH OE2 
9190  N N   . ASN H 35  ? 4.222 3.639 2.330 -1.231 0.193  -0.259 35  ASN HHH N   
9191  C CA  . ASN H 35  ? 4.069 3.672 2.347 -1.202 0.184  -0.274 35  ASN HHH CA  
9192  C C   . ASN H 35  ? 3.918 3.624 2.297 -1.194 0.186  -0.274 35  ASN HHH C   
9193  O O   . ASN H 35  ? 3.820 3.676 2.266 -1.226 0.189  -0.288 35  ASN HHH O   
9194  C CB  . ASN H 35  ? 4.078 3.679 2.446 -1.113 0.165  -0.274 35  ASN HHH CB  
9195  C CG  . ASN H 35  ? 3.998 3.776 2.531 -1.081 0.155  -0.290 35  ASN HHH CG  
9196  O OD1 . ASN H 35  ? 4.207 4.083 2.752 -1.120 0.157  -0.307 35  ASN HHH OD1 
9197  N ND2 . ASN H 35  ? 3.795 3.612 2.451 -1.009 0.143  -0.285 35  ASN HHH ND2 
9198  N N   . PHE H 36  ? 4.164 3.794 2.551 -1.148 0.183  -0.257 36  PHE HHH N   
9199  C CA  . PHE H 36  ? 4.117 3.834 2.593 -1.138 0.185  -0.254 36  PHE HHH CA  
9200  C C   . PHE H 36  ? 4.176 3.919 2.573 -1.225 0.201  -0.259 36  PHE HHH C   
9201  O O   . PHE H 36  ? 4.123 4.008 2.602 -1.240 0.204  -0.269 36  PHE HHH O   
9202  C CB  . PHE H 36  ? 4.145 3.762 2.626 -1.077 0.181  -0.234 36  PHE HHH CB  
9203  C CG  . PHE H 36  ? 3.929 3.638 2.522 -1.048 0.180  -0.229 36  PHE HHH CG  
9204  C CD1 . PHE H 36  ? 3.984 3.686 2.530 -1.090 0.192  -0.224 36  PHE HHH CD1 
9205  C CD2 . PHE H 36  ? 3.717 3.512 2.458 -0.980 0.168  -0.230 36  PHE HHH CD2 
9206  C CE1 . PHE H 36  ? 3.799 3.582 2.444 -1.062 0.192  -0.219 36  PHE HHH CE1 
9207  C CE2 . PHE H 36  ? 3.583 3.451 2.417 -0.954 0.169  -0.225 36  PHE HHH CE2 
9208  C CZ  . PHE H 36  ? 3.557 3.420 2.344 -0.993 0.180  -0.219 36  PHE HHH CZ  
9209  N N   . ARG H 37  ? 4.152 3.757 2.384 -1.284 0.213  -0.253 37  ARG HHH N   
9210  C CA  . ARG H 37  ? 4.209 3.832 2.354 -1.377 0.229  -0.260 37  ARG HHH CA  
9211  C C   . ARG H 37  ? 4.165 3.956 2.355 -1.432 0.233  -0.283 37  ARG HHH C   
9212  O O   . ARG H 37  ? 4.075 3.995 2.309 -1.469 0.240  -0.294 37  ARG HHH O   
9213  C CB  . ARG H 37  ? 4.454 3.886 2.400 -1.434 0.240  -0.251 37  ARG HHH CB  
9214  C CG  . ARG H 37  ? 4.601 4.041 2.458 -1.529 0.257  -0.256 37  ARG HHH CG  
9215  C CD  . ARG H 37  ? 4.754 4.034 2.407 -1.612 0.271  -0.255 37  ARG HHH CD  
9216  N NE  . ARG H 37  ? 4.786 4.166 2.399 -1.719 0.286  -0.272 37  ARG HHH NE  
9217  C CZ  . ARG H 37  ? 4.772 4.280 2.413 -1.766 0.291  -0.291 37  ARG HHH CZ  
9218  N NH1 . ARG H 37  ? 4.528 4.083 2.244 -1.715 0.279  -0.295 37  ARG HHH NH1 
9219  N NH2 . ARG H 37  ? 4.979 4.581 2.576 -1.867 0.306  -0.308 37  ARG HHH NH2 
9220  N N   . ALA H 38  ? 4.306 4.103 2.483 -1.436 0.230  -0.292 38  ALA HHH N   
9221  C CA  . ALA H 38  ? 4.311 4.267 2.519 -1.491 0.235  -0.315 38  ALA HHH CA  
9222  C C   . ALA H 38  ? 3.996 4.145 2.384 -1.436 0.223  -0.328 38  ALA HHH C   
9223  O O   . ALA H 38  ? 4.035 4.342 2.462 -1.478 0.229  -0.347 38  ALA HHH O   
9224  C CB  . ALA H 38  ? 4.526 4.438 2.678 -1.502 0.233  -0.321 38  ALA HHH CB  
9225  N N   . LEU H 39  ? 3.817 3.955 2.311 -1.341 0.207  -0.319 39  LEU HHH N   
9226  C CA  . LEU H 39  ? 3.407 3.704 2.059 -1.285 0.196  -0.328 39  LEU HHH CA  
9227  C C   . LEU H 39  ? 3.335 3.682 2.008 -1.298 0.203  -0.325 39  LEU HHH C   
9228  O O   . LEU H 39  ? 3.104 3.608 1.872 -1.285 0.200  -0.339 39  LEU HHH O   
9229  C CB  . LEU H 39  ? 3.328 3.587 2.076 -1.189 0.179  -0.318 39  LEU HHH CB  
9230  C CG  . LEU H 39  ? 3.387 3.629 2.141 -1.166 0.170  -0.325 39  LEU HHH CG  
9231  C CD1 . LEU H 39  ? 3.231 3.427 2.071 -1.075 0.154  -0.315 39  LEU HHH CD1 
9232  C CD2 . LEU H 39  ? 3.499 3.906 2.312 -1.183 0.166  -0.350 39  LEU HHH CD2 
9233  N N   . SER H 40  ? 3.562 3.775 2.142 -1.321 0.212  -0.307 40  SER HHH N   
9234  C CA  . SER H 40  ? 3.604 3.848 2.190 -1.335 0.219  -0.303 40  SER HHH CA  
9235  C C   . SER H 40  ? 3.803 4.139 2.327 -1.430 0.233  -0.321 40  SER HHH C   
9236  O O   . SER H 40  ? 3.984 4.427 2.556 -1.438 0.236  -0.328 40  SER HHH O   
9237  C CB  . SER H 40  ? 3.676 3.740 2.177 -1.326 0.223  -0.279 40  SER HHH CB  
9238  O OG  . SER H 40  ? 3.603 3.606 2.175 -1.236 0.210  -0.264 40  SER HHH OG  
9239  N N   . THR H 41  ? 3.910 4.210 2.326 -1.503 0.243  -0.330 41  THR HHH N   
9240  C CA  . THR H 41  ? 3.848 4.243 2.200 -1.602 0.258  -0.349 41  THR HHH CA  
9241  C C   . THR H 41  ? 3.829 4.432 2.271 -1.608 0.254  -0.376 41  THR HHH C   
9242  O O   . THR H 41  ? 3.908 4.652 2.349 -1.668 0.263  -0.396 41  THR HHH O   
9243  C CB  . THR H 41  ? 4.128 4.372 2.302 -1.689 0.272  -0.345 41  THR HHH CB  
9244  O OG1 . THR H 41  ? 4.084 4.123 2.171 -1.669 0.273  -0.321 41  THR HHH OG1 
9245  C CG2 . THR H 41  ? 4.290 4.612 2.381 -1.802 0.290  -0.364 41  THR HHH CG2 
9246  N N   . GLY H 42  ? 3.733 4.363 2.253 -1.545 0.240  -0.378 42  GLY HHH N   
9247  C CA  . GLY H 42  ? 3.657 4.473 2.262 -1.538 0.234  -0.403 42  GLY HHH CA  
9248  C C   . GLY H 42  ? 3.831 4.691 2.346 -1.629 0.247  -0.421 42  GLY HHH C   
9249  O O   . GLY H 42  ? 3.825 4.867 2.398 -1.641 0.245  -0.446 42  GLY HHH O   
9250  N N   . GLU H 43  ? 4.118 4.813 2.486 -1.695 0.260  -0.409 43  GLU HHH N   
9251  C CA  . GLU H 43  ? 4.296 5.016 2.556 -1.797 0.275  -0.424 43  GLU HHH CA  
9252  C C   . GLU H 43  ? 4.294 5.071 2.587 -1.778 0.268  -0.436 43  GLU HHH C   
9253  O O   . GLU H 43  ? 4.522 5.388 2.764 -1.855 0.280  -0.455 43  GLU HHH O   
9254  C CB  . GLU H 43  ? 4.503 5.002 2.584 -1.864 0.290  -0.406 43  GLU HHH CB  
9255  C CG  . GLU H 43  ? 4.467 4.765 2.531 -1.785 0.278  -0.379 43  GLU HHH CG  
9256  C CD  . GLU H 43  ? 4.690 4.765 2.579 -1.837 0.291  -0.359 43  GLU HHH CD  
9257  O OE1 . GLU H 43  ? 4.929 5.000 2.713 -1.935 0.308  -0.366 43  GLU HHH OE1 
9258  O OE2 . GLU H 43  ? 4.702 4.607 2.554 -1.778 0.282  -0.339 43  GLU HHH OE2 
9259  N N   . LYS H 44  ? 3.981 4.713 2.358 -1.679 0.250  -0.426 44  LYS HHH N   
9260  C CA  . LYS H 44  ? 3.859 4.650 2.277 -1.653 0.241  -0.438 44  LYS HHH CA  
9261  C C   . LYS H 44  ? 3.673 4.690 2.237 -1.607 0.229  -0.462 44  LYS HHH C   
9262  O O   . LYS H 44  ? 3.647 4.731 2.249 -1.586 0.222  -0.476 44  LYS HHH O   
9263  C CB  . LYS H 44  ? 3.816 4.458 2.259 -1.566 0.226  -0.418 44  LYS HHH CB  
9264  C CG  . LYS H 44  ? 3.910 4.320 2.213 -1.588 0.233  -0.393 44  LYS HHH CG  
9265  C CD  . LYS H 44  ? 4.092 4.404 2.236 -1.671 0.248  -0.394 44  LYS HHH CD  
9266  C CE  . LYS H 44  ? 4.179 4.261 2.185 -1.686 0.255  -0.369 44  LYS HHH CE  
9267  N NZ  . LYS H 44  ? 4.533 4.494 2.352 -1.784 0.274  -0.366 44  LYS HHH NZ  
9268  N N   . GLY H 45  ? 3.690 4.822 2.330 -1.589 0.227  -0.469 45  GLY HHH N   
9269  C CA  . GLY H 45  ? 3.581 4.923 2.345 -1.543 0.215  -0.493 45  GLY HHH CA  
9270  C C   . GLY H 45  ? 3.472 4.805 2.362 -1.428 0.195  -0.484 45  GLY HHH C   
9271  O O   . GLY H 45  ? 3.321 4.808 2.314 -1.374 0.182  -0.502 45  GLY HHH O   
9272  N N   . PHE H 46  ? 3.567 4.720 2.443 -1.388 0.190  -0.457 46  PHE HHH N   
9273  C CA  . PHE H 46  ? 3.491 4.610 2.473 -1.288 0.173  -0.445 46  PHE HHH CA  
9274  C C   . PHE H 46  ? 3.436 4.378 2.369 -1.281 0.178  -0.416 46  PHE HHH C   
9275  O O   . PHE H 46  ? 3.530 4.325 2.358 -1.320 0.186  -0.403 46  PHE HHH O   
9276  C CB  . PHE H 46  ? 3.449 4.550 2.484 -1.228 0.157  -0.448 46  PHE HHH CB  
9277  C CG  . PHE H 46  ? 3.569 4.525 2.506 -1.259 0.162  -0.438 46  PHE HHH CG  
9278  C CD1 . PHE H 46  ? 3.593 4.373 2.503 -1.225 0.159  -0.414 46  PHE HHH CD1 
9279  C CD2 . PHE H 46  ? 3.774 4.773 2.642 -1.323 0.171  -0.453 46  PHE HHH CD2 
9280  C CE1 . PHE H 46  ? 3.721 4.367 2.534 -1.248 0.163  -0.405 46  PHE HHH CE1 
9281  C CE2 . PHE H 46  ? 3.908 4.767 2.677 -1.350 0.176  -0.443 46  PHE HHH CE2 
9282  C CZ  . PHE H 46  ? 3.856 4.537 2.596 -1.310 0.171  -0.419 46  PHE HHH CZ  
9283  N N   . GLY H 47  ? 3.268 4.224 2.271 -1.232 0.173  -0.407 47  GLY HHH N   
9284  C CA  . GLY H 47  ? 3.170 3.976 2.134 -1.223 0.177  -0.381 47  GLY HHH CA  
9285  C C   . GLY H 47  ? 3.040 3.877 2.109 -1.150 0.168  -0.372 47  GLY HHH C   
9286  O O   . GLY H 47  ? 2.991 3.933 2.163 -1.093 0.155  -0.384 47  GLY HHH O   
9287  N N   . TYR H 48  ? 3.065 3.804 2.099 -1.152 0.175  -0.352 48  TYR HHH N   
9288  C CA  . TYR H 48  ? 2.870 3.606 1.995 -1.080 0.167  -0.339 48  TYR HHH CA  
9289  C C   . TYR H 48  ? 2.755 3.634 1.938 -1.074 0.167  -0.350 48  TYR HHH C   
9290  O O   . TYR H 48  ? 2.617 3.520 1.888 -1.007 0.158  -0.343 48  TYR HHH O   
9291  C CB  . TYR H 48  ? 2.866 3.441 1.936 -1.075 0.173  -0.312 48  TYR HHH CB  
9292  C CG  . TYR H 48  ? 2.879 3.314 1.908 -1.056 0.168  -0.300 48  TYR HHH CG  
9293  C CD1 . TYR H 48  ? 2.699 3.149 1.805 -1.000 0.154  -0.305 48  TYR HHH CD1 
9294  C CD2 . TYR H 48  ? 3.086 3.372 1.997 -1.090 0.178  -0.286 48  TYR HHH CD2 
9295  C CE1 . TYR H 48  ? 2.874 3.206 1.945 -0.979 0.149  -0.296 48  TYR HHH CE1 
9296  C CE2 . TYR H 48  ? 3.176 3.339 2.048 -1.065 0.173  -0.276 48  TYR HHH CE2 
9297  C CZ  . TYR H 48  ? 3.078 3.270 2.033 -1.009 0.158  -0.282 48  TYR HHH CZ  
9298  O OH  . TYR H 48  ? 3.266 3.345 2.183 -0.982 0.152  -0.274 48  TYR HHH OH  
9299  N N   . LYS H 49  ? 2.705 3.680 1.838 -1.142 0.177  -0.367 49  LYS HHH N   
9300  C CA  . LYS H 49  ? 2.596 3.712 1.778 -1.134 0.178  -0.378 49  LYS HHH CA  
9301  C C   . LYS H 49  ? 2.499 3.739 1.793 -1.061 0.161  -0.393 49  LYS HHH C   
9302  O O   . LYS H 49  ? 2.563 3.871 1.875 -1.058 0.155  -0.411 49  LYS HHH O   
9303  C CB  . LYS H 49  ? 2.689 3.909 1.801 -1.222 0.191  -0.399 49  LYS HHH CB  
9304  C CG  . LYS H 49  ? 2.847 3.958 1.847 -1.295 0.207  -0.386 49  LYS HHH CG  
9305  C CD  . LYS H 49  ? 3.111 4.335 2.042 -1.390 0.221  -0.410 49  LYS HHH CD  
9306  C CE  . LYS H 49  ? 3.390 4.502 2.202 -1.466 0.237  -0.399 49  LYS HHH CE  
9307  N NZ  . LYS H 49  ? 3.549 4.770 2.288 -1.568 0.251  -0.423 49  LYS HHH NZ  
9308  N N   . GLY H 50  ? 2.406 3.666 1.768 -0.999 0.155  -0.385 50  GLY HHH N   
9309  C CA  . GLY H 50  ? 2.280 3.637 1.739 -0.924 0.139  -0.396 50  GLY HHH CA  
9310  C C   . GLY H 50  ? 2.329 3.590 1.848 -0.854 0.126  -0.382 50  GLY HHH C   
9311  O O   . GLY H 50  ? 2.280 3.604 1.872 -0.789 0.113  -0.390 50  GLY HHH O   
9312  N N   . SER H 51  ? 2.479 3.593 1.966 -0.863 0.130  -0.362 51  SER HHH N   
9313  C CA  . SER H 51  ? 2.448 3.485 1.994 -0.801 0.118  -0.352 51  SER HHH CA  
9314  C C   . SER H 51  ? 2.318 3.296 1.907 -0.753 0.118  -0.330 51  SER HHH C   
9315  O O   . SER H 51  ? 2.349 3.323 1.913 -0.771 0.128  -0.320 51  SER HHH O   
9316  C CB  . SER H 51  ? 2.582 3.497 2.077 -0.826 0.120  -0.343 51  SER HHH CB  
9317  O OG  . SER H 51  ? 2.628 3.430 2.064 -0.851 0.132  -0.320 51  SER HHH OG  
9318  N N   . CYS H 52  ? 2.173 3.107 1.829 -0.693 0.106  -0.323 52  CYS HHH N   
9319  C CA  . CYS H 52  ? 2.005 2.889 1.705 -0.647 0.106  -0.303 52  CYS HHH CA  
9320  C C   . CYS H 52  ? 1.932 2.680 1.629 -0.638 0.108  -0.282 52  CYS HHH C   
9321  O O   . CYS H 52  ? 1.871 2.570 1.547 -0.651 0.105  -0.285 52  CYS HHH O   
9322  C CB  . CYS H 52  ? 1.971 2.915 1.747 -0.583 0.092  -0.312 52  CYS HHH CB  
9323  S SG  . CYS H 52  ? 1.993 2.884 1.822 -0.541 0.077  -0.317 52  CYS HHH SG  
9324  N N   . PHE H 53  ? 1.831 2.523 1.547 -0.614 0.113  -0.260 53  PHE HHH N   
9325  C CA  . PHE H 53  ? 1.697 2.282 1.431 -0.590 0.113  -0.242 53  PHE HHH CA  
9326  C C   . PHE H 53  ? 1.641 2.234 1.459 -0.534 0.101  -0.243 53  PHE HHH C   
9327  O O   . PHE H 53  ? 1.614 2.228 1.470 -0.503 0.101  -0.237 53  PHE HHH O   
9328  C CB  . PHE H 53  ? 1.747 2.267 1.454 -0.596 0.126  -0.219 53  PHE HHH CB  
9329  C CG  . PHE H 53  ? 1.819 2.284 1.434 -0.648 0.136  -0.214 53  PHE HHH CG  
9330  C CD1 . PHE H 53  ? 1.993 2.508 1.550 -0.695 0.144  -0.223 53  PHE HHH CD1 
9331  C CD2 . PHE H 53  ? 1.817 2.179 1.398 -0.648 0.137  -0.203 53  PHE HHH CD2 
9332  C CE1 . PHE H 53  ? 2.094 2.544 1.555 -0.746 0.153  -0.219 53  PHE HHH CE1 
9333  C CE2 . PHE H 53  ? 1.915 2.211 1.399 -0.691 0.146  -0.199 53  PHE HHH CE2 
9334  C CZ  . PHE H 53  ? 2.016 2.350 1.437 -0.743 0.154  -0.206 53  PHE HHH CZ  
9335  N N   . HIS H 54  ? 1.612 2.185 1.451 -0.523 0.091  -0.253 54  HIS HHH N   
9336  C CA  . HIS H 54  ? 1.474 2.053 1.383 -0.477 0.078  -0.259 54  HIS HHH CA  
9337  C C   . HIS H 54  ? 1.399 1.894 1.344 -0.453 0.080  -0.241 54  HIS HHH C   
9338  O O   . HIS H 54  ? 1.344 1.835 1.343 -0.418 0.074  -0.239 54  HIS HHH O   
9339  C CB  . HIS H 54  ? 1.582 2.195 1.497 -0.478 0.066  -0.282 54  HIS HHH CB  
9340  C CG  . HIS H 54  ? 1.700 2.250 1.585 -0.498 0.066  -0.281 54  HIS HHH CG  
9341  N ND1 . HIS H 54  ? 1.682 2.222 1.494 -0.544 0.074  -0.282 54  HIS HHH ND1 
9342  C CD2 . HIS H 54  ? 1.680 2.173 1.594 -0.479 0.059  -0.280 54  HIS HHH CD2 
9343  C CE1 . HIS H 54  ? 1.694 2.168 1.486 -0.546 0.071  -0.281 54  HIS HHH CE1 
9344  N NE2 . HIS H 54  ? 1.645 2.097 1.502 -0.507 0.062  -0.280 54  HIS HHH NE2 
9345  N N   . ARG H 55  ? 1.412 1.840 1.322 -0.472 0.088  -0.227 55  ARG HHH N   
9346  C CA  . ARG H 55  ? 1.468 1.827 1.408 -0.452 0.091  -0.210 55  ARG HHH CA  
9347  C C   . ARG H 55  ? 1.467 1.784 1.367 -0.465 0.106  -0.189 55  ARG HHH C   
9348  O O   . ARG H 55  ? 1.432 1.715 1.267 -0.492 0.112  -0.186 55  ARG HHH O   
9349  C CB  . ARG H 55  ? 1.428 1.748 1.365 -0.452 0.084  -0.218 55  ARG HHH CB  
9350  C CG  . ARG H 55  ? 1.338 1.631 1.340 -0.422 0.078  -0.215 55  ARG HHH CG  
9351  C CD  . ARG H 55  ? 1.431 1.704 1.431 -0.420 0.069  -0.228 55  ARG HHH CD  
9352  N NE  . ARG H 55  ? 1.517 1.773 1.579 -0.396 0.063  -0.228 55  ARG HHH NE  
9353  C CZ  . ARG H 55  ? 1.480 1.697 1.545 -0.388 0.067  -0.218 55  ARG HHH CZ  
9354  N NH1 . ARG H 55  ? 1.412 1.592 1.417 -0.398 0.076  -0.206 55  ARG HHH NH1 
9355  N NH2 . ARG H 55  ? 1.535 1.751 1.661 -0.371 0.062  -0.221 55  ARG HHH NH2 
9356  N N   . ILE H 56  ? 1.466 1.782 1.400 -0.446 0.112  -0.174 56  ILE HHH N   
9357  C CA  . ILE H 56  ? 1.522 1.795 1.430 -0.451 0.125  -0.152 56  ILE HHH CA  
9358  C C   . ILE H 56  ? 1.517 1.755 1.480 -0.423 0.128  -0.137 56  ILE HHH C   
9359  O O   . ILE H 56  ? 1.497 1.753 1.510 -0.401 0.125  -0.136 56  ILE HHH O   
9360  C CB  . ILE H 56  ? 1.546 1.858 1.433 -0.460 0.133  -0.146 56  ILE HHH CB  
9361  C CG1 . ILE H 56  ? 1.442 1.796 1.270 -0.496 0.133  -0.162 56  ILE HHH CG1 
9362  C CG2 . ILE H 56  ? 1.592 1.857 1.456 -0.461 0.147  -0.123 56  ILE HHH CG2 
9363  C CD1 . ILE H 56  ? 1.589 1.992 1.392 -0.508 0.140  -0.159 56  ILE HHH CD1 
9364  N N   . ILE H 57  ? 1.515 1.702 1.464 -0.422 0.132  -0.128 57  ILE HHH N   
9365  C CA  . ILE H 57  ? 1.518 1.680 1.516 -0.401 0.136  -0.116 57  ILE HHH CA  
9366  C C   . ILE H 57  ? 1.508 1.636 1.472 -0.402 0.150  -0.094 57  ILE HHH C   
9367  O O   . ILE H 57  ? 1.501 1.593 1.411 -0.410 0.152  -0.093 57  ILE HHH O   
9368  C CB  . ILE H 57  ? 1.477 1.624 1.497 -0.393 0.127  -0.126 57  ILE HHH CB  
9369  C CG1 . ILE H 57  ? 1.501 1.681 1.550 -0.391 0.112  -0.148 57  ILE HHH CG1 
9370  C CG2 . ILE H 57  ? 1.475 1.609 1.547 -0.376 0.132  -0.115 57  ILE HHH CG2 
9371  C CD1 . ILE H 57  ? 1.495 1.667 1.567 -0.383 0.102  -0.162 57  ILE HHH CD1 
9372  N N   . PRO H 58  ? 1.503 1.636 1.491 -0.393 0.159  -0.078 58  PRO HHH N   
9373  C CA  . PRO H 58  ? 1.485 1.588 1.437 -0.394 0.173  -0.058 58  PRO HHH CA  
9374  C C   . PRO H 58  ? 1.531 1.601 1.486 -0.382 0.176  -0.052 58  PRO HHH C   
9375  O O   . PRO H 58  ? 1.537 1.615 1.547 -0.370 0.172  -0.056 58  PRO HHH O   
9376  C CB  . PRO H 58  ? 1.540 1.659 1.531 -0.382 0.181  -0.043 58  PRO HHH CB  
9377  C CG  . PRO H 58  ? 1.488 1.626 1.540 -0.370 0.172  -0.054 58  PRO HHH CG  
9378  C CD  . PRO H 58  ? 1.543 1.702 1.582 -0.380 0.158  -0.077 58  PRO HHH CD  
9379  N N   . GLY H 59  ? 1.601 1.633 1.490 -0.386 0.181  -0.045 59  GLY HHH N   
9380  C CA  . GLY H 59  ? 1.643 1.646 1.522 -0.369 0.183  -0.040 59  GLY HHH CA  
9381  C C   . GLY H 59  ? 1.692 1.681 1.549 -0.367 0.171  -0.058 59  GLY HHH C   
9382  O O   . GLY H 59  ? 1.740 1.712 1.589 -0.347 0.170  -0.058 59  GLY HHH O   
9383  N N   . PHE H 60  ? 1.687 1.688 1.533 -0.384 0.161  -0.074 60  PHE HHH N   
9384  C CA  . PHE H 60  ? 1.698 1.687 1.523 -0.383 0.149  -0.092 60  PHE HHH CA  
9385  C C   . PHE H 60  ? 1.765 1.726 1.505 -0.410 0.147  -0.100 60  PHE HHH C   
9386  O O   . PHE H 60  ? 1.800 1.702 1.456 -0.412 0.149  -0.097 60  PHE HHH O   
9387  C CB  . PHE H 60  ? 1.679 1.716 1.585 -0.378 0.139  -0.107 60  PHE HHH CB  
9388  C CG  . PHE H 60  ? 1.733 1.764 1.629 -0.372 0.126  -0.125 60  PHE HHH CG  
9389  C CD1 . PHE H 60  ? 1.858 1.845 1.696 -0.358 0.125  -0.125 60  PHE HHH CD1 
9390  C CD2 . PHE H 60  ? 1.631 1.697 1.568 -0.377 0.115  -0.143 60  PHE HHH CD2 
9391  C CE1 . PHE H 60  ? 1.819 1.799 1.643 -0.350 0.113  -0.142 60  PHE HHH CE1 
9392  C CE2 . PHE H 60  ? 1.629 1.690 1.556 -0.371 0.103  -0.160 60  PHE HHH CE2 
9393  C CZ  . PHE H 60  ? 1.726 1.745 1.597 -0.357 0.102  -0.160 60  PHE HHH CZ  
9394  N N   . MET H 61  ? 1.758 1.760 1.514 -0.431 0.143  -0.111 61  MET HHH N   
9395  C CA  . MET H 61  ? 1.797 1.786 1.477 -0.463 0.141  -0.121 61  MET HHH CA  
9396  C C   . MET H 61  ? 1.728 1.784 1.439 -0.483 0.139  -0.130 61  MET HHH C   
9397  O O   . MET H 61  ? 1.617 1.722 1.407 -0.465 0.136  -0.131 61  MET HHH O   
9398  C CB  . MET H 61  ? 1.863 1.829 1.517 -0.461 0.130  -0.136 61  MET HHH CB  
9399  C CG  . MET H 61  ? 1.848 1.867 1.588 -0.444 0.118  -0.151 61  MET HHH CG  
9400  S SD  . MET H 61  ? 2.053 2.121 1.789 -0.471 0.110  -0.172 61  MET HHH SD  
9401  C CE  . MET H 61  ? 1.845 1.985 1.696 -0.449 0.103  -0.178 61  MET HHH CE  
9402  N N   . CYS H 62  ? 1.856 1.913 1.497 -0.519 0.141  -0.138 62  CYS HHH N   
9403  C CA  . CYS H 62  ? 1.815 1.947 1.472 -0.539 0.138  -0.151 62  CYS HHH CA  
9404  C C   . CYS H 62  ? 1.887 2.020 1.494 -0.567 0.132  -0.169 62  CYS HHH C   
9405  O O   . CYS H 62  ? 1.972 2.043 1.489 -0.593 0.137  -0.168 62  CYS HHH O   
9406  C CB  . CYS H 62  ? 1.777 1.931 1.398 -0.564 0.149  -0.144 62  CYS HHH CB  
9407  S SG  . CYS H 62  ? 1.846 1.984 1.503 -0.536 0.159  -0.120 62  CYS HHH SG  
9408  N N   . GLN H 63  ? 1.840 2.037 1.498 -0.561 0.122  -0.187 63  GLN HHH N   
9409  C CA  . GLN H 63  ? 1.814 2.018 1.433 -0.584 0.115  -0.204 63  GLN HHH CA  
9410  C C   . GLN H 63  ? 1.777 2.078 1.413 -0.603 0.112  -0.222 63  GLN HHH C   
9411  O O   . GLN H 63  ? 1.674 2.040 1.377 -0.580 0.109  -0.224 63  GLN HHH O   
9412  C CB  . GLN H 63  ? 1.850 2.032 1.508 -0.553 0.104  -0.211 63  GLN HHH CB  
9413  C CG  . GLN H 63  ? 1.851 2.104 1.593 -0.531 0.091  -0.227 63  GLN HHH CG  
9414  C CD  . GLN H 63  ? 1.912 2.143 1.671 -0.512 0.079  -0.238 63  GLN HHH CD  
9415  O OE1 . GLN H 63  ? 1.896 2.060 1.619 -0.506 0.080  -0.232 63  GLN HHH OE1 
9416  N NE2 . GLN H 63  ? 1.929 2.216 1.741 -0.499 0.068  -0.256 63  GLN HHH NE2 
9417  N N   . GLY H 64  ? 1.950 2.261 1.520 -0.644 0.113  -0.234 64  GLY HHH N   
9418  C CA  . GLY H 64  ? 2.038 2.450 1.613 -0.667 0.111  -0.253 64  GLY HHH CA  
9419  C C   . GLY H 64  ? 2.150 2.561 1.665 -0.703 0.109  -0.268 64  GLY HHH C   
9420  O O   . GLY H 64  ? 2.199 2.534 1.685 -0.697 0.106  -0.266 64  GLY HHH O   
9421  N N   . GLY H 65  ? 2.240 2.741 1.736 -0.739 0.112  -0.285 65  GLY HHH N   
9422  C CA  . GLY H 65  ? 2.325 2.828 1.755 -0.781 0.113  -0.299 65  GLY HHH CA  
9423  C C   . GLY H 65  ? 2.227 2.805 1.709 -0.762 0.099  -0.320 65  GLY HHH C   
9424  O O   . GLY H 65  ? 2.318 2.898 1.746 -0.796 0.100  -0.331 65  GLY HHH O   
9425  N N   . ASP H 66  ? 2.092 2.725 1.671 -0.708 0.088  -0.325 66  ASP HHH N   
9426  C CA  . ASP H 66  ? 2.161 2.865 1.786 -0.685 0.074  -0.347 66  ASP HHH CA  
9427  C C   . ASP H 66  ? 2.318 3.158 1.951 -0.702 0.074  -0.367 66  ASP HHH C   
9428  O O   . ASP H 66  ? 2.214 3.125 1.910 -0.664 0.067  -0.373 66  ASP HHH O   
9429  C CB  . ASP H 66  ? 2.151 2.841 1.866 -0.621 0.060  -0.346 66  ASP HHH CB  
9430  C CG  . ASP H 66  ? 2.219 2.976 1.980 -0.594 0.044  -0.369 66  ASP HHH CG  
9431  O OD1 . ASP H 66  ? 2.368 3.194 2.097 -0.623 0.044  -0.387 66  ASP HHH OD1 
9432  O OD2 . ASP H 66  ? 2.238 2.979 2.066 -0.546 0.032  -0.370 66  ASP HHH OD2 
9433  N N   . PHE H 67  ? 2.609 3.483 2.171 -0.760 0.082  -0.377 67  PHE HHH N   
9434  C CA  . PHE H 67  ? 2.578 3.591 2.133 -0.789 0.085  -0.398 67  PHE HHH CA  
9435  C C   . PHE H 67  ? 2.529 3.634 2.119 -0.769 0.072  -0.423 67  PHE HHH C   
9436  O O   . PHE H 67  ? 2.548 3.782 2.132 -0.791 0.074  -0.444 67  PHE HHH O   
9437  C CB  . PHE H 67  ? 2.627 3.635 2.080 -0.871 0.103  -0.397 67  PHE HHH CB  
9438  C CG  . PHE H 67  ? 2.802 3.709 2.174 -0.912 0.108  -0.392 67  PHE HHH CG  
9439  C CD1 . PHE H 67  ? 2.915 3.871 2.261 -0.938 0.106  -0.411 67  PHE HHH CD1 
9440  C CD2 . PHE H 67  ? 2.932 3.691 2.247 -0.921 0.115  -0.369 67  PHE HHH CD2 
9441  C CE1 . PHE H 67  ? 3.190 4.043 2.453 -0.973 0.112  -0.405 67  PHE HHH CE1 
9442  C CE2 . PHE H 67  ? 3.101 3.758 2.332 -0.953 0.120  -0.364 67  PHE HHH CE2 
9443  C CZ  . PHE H 67  ? 3.239 3.940 2.441 -0.979 0.118  -0.381 67  PHE HHH CZ  
9444  N N   . THR H 68  ? 2.474 3.526 2.102 -0.727 0.059  -0.424 68  THR HHH N   
9445  C CA  . THR H 68  ? 2.497 3.641 2.160 -0.705 0.046  -0.449 68  THR HHH CA  
9446  C C   . THR H 68  ? 2.419 3.596 2.172 -0.629 0.029  -0.456 68  THR HHH C   
9447  O O   . THR H 68  ? 2.505 3.791 2.287 -0.605 0.018  -0.479 68  THR HHH O   
9448  C CB  . THR H 68  ? 2.545 3.619 2.179 -0.715 0.042  -0.451 68  THR HHH CB  
9449  O OG1 . THR H 68  ? 2.644 3.630 2.186 -0.775 0.058  -0.436 68  THR HHH OG1 
9450  C CG2 . THR H 68  ? 2.548 3.729 2.188 -0.717 0.034  -0.478 68  THR HHH CG2 
9451  N N   . ARG H 69  ? 2.205 3.289 1.997 -0.591 0.025  -0.437 69  ARG HHH N   
9452  C CA  . ARG H 69  ? 2.120 3.218 1.986 -0.524 0.010  -0.442 69  ARG HHH CA  
9453  C C   . ARG H 69  ? 2.152 3.213 2.041 -0.503 0.015  -0.423 69  ARG HHH C   
9454  O O   . ARG H 69  ? 2.199 3.270 2.140 -0.449 0.004  -0.426 69  ARG HHH O   
9455  C CB  . ARG H 69  ? 2.143 3.173 2.047 -0.490 -0.004 -0.445 69  ARG HHH CB  
9456  C CG  . ARG H 69  ? 2.309 3.390 2.195 -0.502 -0.011 -0.468 69  ARG HHH CG  
9457  C CD  . ARG H 69  ? 2.338 3.376 2.270 -0.459 -0.029 -0.477 69  ARG HHH CD  
9458  N NE  . ARG H 69  ? 2.417 3.493 2.407 -0.402 -0.043 -0.488 69  ARG HHH NE  
9459  C CZ  . ARG H 69  ? 2.339 3.349 2.372 -0.364 -0.048 -0.476 69  ARG HHH CZ  
9460  N NH1 . ARG H 69  ? 2.247 3.158 2.283 -0.375 -0.040 -0.453 69  ARG HHH NH1 
9461  N NH2 . ARG H 69  ? 2.383 3.425 2.452 -0.314 -0.061 -0.488 69  ARG HHH NH2 
9462  N N   . HIS H 70  ? 2.159 3.168 2.007 -0.542 0.031  -0.403 70  HIS HHH N   
9463  C CA  . HIS H 70  ? 2.073 3.062 1.932 -0.529 0.038  -0.385 70  HIS HHH CA  
9464  C C   . HIS H 70  ? 1.976 2.874 1.887 -0.483 0.033  -0.368 70  HIS HHH C   
9465  O O   . HIS H 70  ? 2.029 2.921 1.962 -0.458 0.035  -0.357 70  HIS HHH O   
9466  C CB  . HIS H 70  ? 2.069 3.178 1.940 -0.513 0.036  -0.399 70  HIS HHH CB  
9467  C CG  . HIS H 70  ? 2.133 3.317 1.946 -0.571 0.049  -0.405 70  HIS HHH CG  
9468  N ND1 . HIS H 70  ? 2.249 3.463 2.011 -0.625 0.055  -0.417 70  HIS HHH ND1 
9469  C CD2 . HIS H 70  ? 2.203 3.435 1.996 -0.587 0.059  -0.401 70  HIS HHH CD2 
9470  C CE1 . HIS H 70  ? 2.315 3.593 2.028 -0.675 0.067  -0.421 70  HIS HHH CE1 
9471  N NE2 . HIS H 70  ? 2.342 3.636 2.075 -0.653 0.070  -0.412 70  HIS HHH NE2 
9472  N N   . ASN H 71  ? 1.735 2.563 1.663 -0.473 0.026  -0.367 71  ASN HHH N   
9473  C CA  . ASN H 71  ? 1.617 2.373 1.599 -0.432 0.020  -0.355 71  ASN HHH CA  
9474  C C   . ASN H 71  ? 1.580 2.243 1.557 -0.442 0.022  -0.345 71  ASN HHH C   
9475  O O   . ASN H 71  ? 1.707 2.317 1.730 -0.413 0.016  -0.338 71  ASN HHH O   
9476  C CB  . ASN H 71  ? 1.730 2.520 1.763 -0.385 0.002  -0.374 71  ASN HHH CB  
9477  C CG  . ASN H 71  ? 1.905 2.717 1.936 -0.388 -0.009 -0.396 71  ASN HHH CG  
9478  O OD1 . ASN H 71  ? 1.972 2.767 1.964 -0.424 -0.004 -0.395 71  ASN HHH OD1 
9479  N ND2 . ASN H 71  ? 1.976 2.822 2.043 -0.348 -0.026 -0.414 71  ASN HHH ND2 
9480  N N   . GLY H 72  ? 1.559 2.200 1.478 -0.481 0.028  -0.343 72  GLY HHH N   
9481  C CA  . GLY H 72  ? 1.614 2.169 1.521 -0.484 0.029  -0.335 72  GLY HHH CA  
9482  C C   . GLY H 72  ? 1.694 2.252 1.600 -0.481 0.017  -0.353 72  GLY HHH C   
9483  O O   . GLY H 72  ? 1.753 2.245 1.645 -0.479 0.016  -0.348 72  GLY HHH O   
9484  N N   . THR H 73  ? 1.757 2.392 1.676 -0.476 0.008  -0.374 73  THR HHH N   
9485  C CA  . THR H 73  ? 1.765 2.416 1.687 -0.470 -0.005 -0.394 73  THR HHH CA  
9486  C C   . THR H 73  ? 1.843 2.526 1.692 -0.515 0.002  -0.402 73  THR HHH C   
9487  O O   . THR H 73  ? 1.999 2.683 1.832 -0.518 -0.005 -0.416 73  THR HHH O   
9488  C CB  . THR H 73  ? 1.761 2.476 1.745 -0.431 -0.020 -0.413 73  THR HHH CB  
9489  O OG1 . THR H 73  ? 1.721 2.387 1.764 -0.394 -0.027 -0.406 73  THR HHH OG1 
9490  C CG2 . THR H 73  ? 1.980 2.734 1.963 -0.426 -0.033 -0.437 73  THR HHH CG2 
9491  N N   . GLY H 74  ? 1.934 2.632 1.731 -0.553 0.017  -0.393 74  GLY HHH N   
9492  C CA  . GLY H 74  ? 2.030 2.765 1.753 -0.604 0.025  -0.401 74  GLY HHH CA  
9493  C C   . GLY H 74  ? 2.093 2.744 1.728 -0.650 0.041  -0.383 74  GLY HHH C   
9494  O O   . GLY H 74  ? 2.017 2.569 1.642 -0.636 0.043  -0.366 74  GLY HHH O   
9495  N N   . GLY H 75  ? 2.303 2.994 1.869 -0.704 0.053  -0.387 75  GLY HHH N   
9496  C CA  . GLY H 75  ? 2.499 3.110 1.961 -0.758 0.069  -0.374 75  GLY HHH CA  
9497  C C   . GLY H 75  ? 2.807 3.390 2.194 -0.792 0.070  -0.383 75  GLY HHH C   
9498  O O   . GLY H 75  ? 2.819 3.422 2.239 -0.765 0.057  -0.396 75  GLY HHH O   
9499  N N   . LYS H 76  ? 3.049 3.577 2.326 -0.853 0.085  -0.375 76  LYS HHH N   
9500  C CA  . LYS H 76  ? 3.209 3.687 2.399 -0.887 0.088  -0.380 76  LYS HHH CA  
9501  C C   . LYS H 76  ? 3.411 3.768 2.469 -0.940 0.104  -0.363 76  LYS HHH C   
9502  O O   . LYS H 76  ? 3.534 3.889 2.562 -0.972 0.116  -0.355 76  LYS HHH O   
9503  C CB  . LYS H 76  ? 3.199 3.809 2.392 -0.923 0.089  -0.403 76  LYS HHH CB  
9504  C CG  . LYS H 76  ? 3.372 3.956 2.466 -0.975 0.096  -0.410 76  LYS HHH CG  
9505  C CD  . LYS H 76  ? 3.257 3.997 2.373 -1.006 0.098  -0.434 76  LYS HHH CD  
9506  C CE  . LYS H 76  ? 3.116 3.954 2.248 -1.037 0.107  -0.438 76  LYS HHH CE  
9507  N NZ  . LYS H 76  ? 3.093 4.091 2.230 -1.075 0.111  -0.463 76  LYS HHH NZ  
9508  N N   . SER H 77  ? 3.622 3.875 2.596 -0.947 0.104  -0.360 77  SER HHH N   
9509  C CA  . SER H 77  ? 3.715 3.839 2.544 -0.998 0.118  -0.345 77  SER HHH CA  
9510  C C   . SER H 77  ? 3.915 4.081 2.656 -1.080 0.131  -0.357 77  SER HHH C   
9511  O O   . SER H 77  ? 4.254 4.548 3.050 -1.088 0.128  -0.377 77  SER HHH O   
9512  C CB  . SER H 77  ? 3.783 3.764 2.549 -0.962 0.111  -0.335 77  SER HHH CB  
9513  O OG  . SER H 77  ? 4.209 4.184 2.925 -0.978 0.109  -0.346 77  SER HHH OG  
9514  N N   . ILE H 78  ? 4.036 4.093 2.635 -1.142 0.147  -0.346 78  ILE HHH N   
9515  C CA  . ILE H 78  ? 4.081 4.172 2.588 -1.226 0.161  -0.358 78  ILE HHH CA  
9516  C C   . ILE H 78  ? 4.231 4.272 2.684 -1.223 0.156  -0.363 78  ILE HHH C   
9517  O O   . ILE H 78  ? 4.352 4.434 2.739 -1.289 0.167  -0.375 78  ILE HHH O   
9518  C CB  . ILE H 78  ? 3.844 3.836 2.210 -1.303 0.181  -0.346 78  ILE HHH CB  
9519  C CG1 . ILE H 78  ? 3.952 3.733 2.195 -1.287 0.181  -0.325 78  ILE HHH CG1 
9520  C CG2 . ILE H 78  ? 3.756 3.816 2.187 -1.303 0.184  -0.343 78  ILE HHH CG2 
9521  C CD1 . ILE H 78  ? 4.095 3.755 2.167 -1.370 0.200  -0.316 78  ILE HHH CD1 
9522  N N   . TYR H 79  ? 4.184 4.144 2.663 -1.150 0.142  -0.356 79  TYR HHH N   
9523  C CA  . TYR H 79  ? 4.236 4.141 2.666 -1.135 0.135  -0.361 79  TYR HHH CA  
9524  C C   . TYR H 79  ? 4.271 4.304 2.849 -1.074 0.116  -0.378 79  TYR HHH C   
9525  O O   . TYR H 79  ? 4.078 4.078 2.720 -0.999 0.100  -0.375 79  TYR HHH O   
9526  C CB  . TYR H 79  ? 4.307 4.026 2.643 -1.098 0.131  -0.342 79  TYR HHH CB  
9527  C CG  . TYR H 79  ? 4.481 4.059 2.669 -1.149 0.147  -0.324 79  TYR HHH CG  
9528  C CD1 . TYR H 79  ? 4.715 4.244 2.759 -1.239 0.166  -0.325 79  TYR HHH CD1 
9529  C CD2 . TYR H 79  ? 4.306 3.798 2.493 -1.108 0.145  -0.308 79  TYR HHH CD2 
9530  C CE1 . TYR H 79  ? 4.889 4.276 2.786 -1.289 0.180  -0.309 79  TYR HHH CE1 
9531  C CE2 . TYR H 79  ? 4.398 3.755 2.443 -1.152 0.159  -0.293 79  TYR HHH CE2 
9532  C CZ  . TYR H 79  ? 4.747 4.047 2.645 -1.242 0.176  -0.294 79  TYR HHH CZ  
9533  O OH  . TYR H 79  ? 4.852 4.007 2.600 -1.289 0.189  -0.279 79  TYR HHH OH  
9542  C CB  . GLU H 81  ? 3.181 3.657 2.394 -0.812 0.048  -0.424 81  GLU HHH CB  
9543  C CG  . GLU H 81  ? 3.207 3.827 2.446 -0.838 0.049  -0.446 81  GLU HHH CG  
9544  C CD  . GLU H 81  ? 3.152 3.866 2.509 -0.778 0.029  -0.464 81  GLU HHH CD  
9545  O OE1 . GLU H 81  ? 3.017 3.701 2.450 -0.722 0.018  -0.459 81  GLU HHH OE1 
9546  O OE2 . GLU H 81  ? 3.134 3.950 2.503 -0.788 0.026  -0.485 81  GLU HHH OE2 
9547  N N   . LYS H 82  ? 3.428 3.577 2.456 -0.808 0.060  -0.378 82  LYS HHH N   
9548  C CA  . LYS H 82  ? 3.252 3.300 2.278 -0.765 0.056  -0.362 82  LYS HHH CA  
9549  C C   . LYS H 82  ? 3.350 3.257 2.233 -0.779 0.062  -0.352 82  LYS HHH C   
9550  O O   . LYS H 82  ? 3.429 3.318 2.240 -0.805 0.063  -0.360 82  LYS HHH O   
9551  C CB  . LYS H 82  ? 3.080 3.162 2.225 -0.693 0.037  -0.369 82  LYS HHH CB  
9552  C CG  . LYS H 82  ? 2.978 3.157 2.251 -0.668 0.032  -0.373 82  LYS HHH CG  
9553  C CD  . LYS H 82  ? 2.836 3.023 2.208 -0.603 0.015  -0.378 82  LYS HHH CD  
9554  C CE  . LYS H 82  ? 2.678 2.947 2.168 -0.579 0.011  -0.380 82  LYS HHH CE  
9555  N NZ  . LYS H 82  ? 2.726 2.974 2.208 -0.594 0.024  -0.361 82  LYS HHH NZ  
9556  N N   . PHE H 83  ? 3.204 3.006 2.042 -0.758 0.064  -0.334 83  PHE HHH N   
9557  C CA  . PHE H 83  ? 3.342 2.997 2.045 -0.753 0.066  -0.324 83  PHE HHH CA  
9558  C C   . PHE H 83  ? 3.374 2.963 2.101 -0.684 0.056  -0.314 83  PHE HHH C   
9559  O O   . PHE H 83  ? 3.387 3.034 2.224 -0.651 0.052  -0.311 83  PHE HHH O   
9560  C CB  . PHE H 83  ? 3.522 3.086 2.079 -0.821 0.085  -0.311 83  PHE HHH CB  
9561  C CG  . PHE H 83  ? 3.513 3.058 2.079 -0.825 0.093  -0.296 83  PHE HHH CG  
9562  C CD1 . PHE H 83  ? 3.410 3.073 2.069 -0.849 0.099  -0.299 83  PHE HHH CD1 
9563  C CD2 . PHE H 83  ? 3.581 2.989 2.056 -0.803 0.096  -0.279 83  PHE HHH CD2 
9564  C CE1 . PHE H 83  ? 3.282 2.930 1.949 -0.853 0.106  -0.286 83  PHE HHH CE1 
9565  C CE2 . PHE H 83  ? 3.435 2.828 1.918 -0.807 0.103  -0.266 83  PHE HHH CE2 
9566  C CZ  . PHE H 83  ? 3.346 2.859 1.926 -0.833 0.109  -0.269 83  PHE HHH CZ  
9567  N N   . GLU H 84  ? 3.483 2.950 2.097 -0.663 0.053  -0.309 84  GLU HHH N   
9568  C CA  . GLU H 84  ? 3.539 2.945 2.157 -0.592 0.042  -0.304 84  GLU HHH CA  
9569  C C   . GLU H 84  ? 3.592 2.937 2.179 -0.588 0.051  -0.285 84  GLU HHH C   
9570  O O   . GLU H 84  ? 3.611 2.928 2.138 -0.643 0.066  -0.276 84  GLU HHH O   
9571  C CB  . GLU H 84  ? 3.701 2.994 2.194 -0.569 0.036  -0.305 84  GLU HHH CB  
9572  C CG  . GLU H 84  ? 3.717 3.077 2.261 -0.554 0.024  -0.324 84  GLU HHH CG  
9573  C CD  . GLU H 84  ? 3.880 3.162 2.364 -0.493 0.010  -0.328 84  GLU HHH CD  
9574  O OE1 . GLU H 84  ? 4.071 3.273 2.507 -0.448 0.007  -0.319 84  GLU HHH OE1 
9575  O OE2 . GLU H 84  ? 3.814 3.120 2.297 -0.485 0.001  -0.342 84  GLU HHH OE2 
9576  N N   . ASP H 85  ? 3.540 2.869 2.169 -0.522 0.041  -0.282 85  ASP HHH N   
9577  C CA  . ASP H 85  ? 3.674 2.930 2.256 -0.507 0.047  -0.265 85  ASP HHH CA  
9578  C C   . ASP H 85  ? 3.929 3.019 2.316 -0.518 0.054  -0.254 85  ASP HHH C   
9579  O O   . ASP H 85  ? 4.004 3.017 2.313 -0.478 0.044  -0.258 85  ASP HHH O   
9580  C CB  . ASP H 85  ? 3.622 2.910 2.294 -0.431 0.035  -0.267 85  ASP HHH CB  
9581  C CG  . ASP H 85  ? 3.400 2.836 2.255 -0.421 0.030  -0.276 85  ASP HHH CG  
9582  O OD1 . ASP H 85  ? 3.346 2.841 2.257 -0.461 0.039  -0.271 85  ASP HHH OD1 
9583  O OD2 . ASP H 85  ? 3.260 2.750 2.199 -0.373 0.016  -0.288 85  ASP HHH OD2 
9584  N N   . GLU H 86  ? 4.033 3.067 2.339 -0.574 0.070  -0.242 86  GLU HHH N   
9585  C CA  . GLU H 86  ? 4.274 3.143 2.380 -0.604 0.078  -0.232 86  GLU HHH CA  
9586  C C   . GLU H 86  ? 4.367 3.122 2.395 -0.534 0.071  -0.222 86  GLU HHH C   
9587  O O   . GLU H 86  ? 4.602 3.238 2.499 -0.507 0.065  -0.222 86  GLU HHH O   
9588  C CB  . GLU H 86  ? 4.306 3.156 2.353 -0.686 0.097  -0.223 86  GLU HHH CB  
9589  C CG  . GLU H 86  ? 4.504 3.176 2.332 -0.730 0.107  -0.214 86  GLU HHH CG  
9590  C CD  . GLU H 86  ? 4.579 3.246 2.348 -0.825 0.126  -0.210 86  GLU HHH CD  
9591  O OE1 . GLU H 86  ? 4.529 3.326 2.422 -0.849 0.131  -0.213 86  GLU HHH OE1 
9592  O OE2 . GLU H 86  ? 4.672 3.204 2.264 -0.878 0.137  -0.205 86  GLU HHH OE2 
9593  N N   . ASN H 87  ? 4.217 3.013 2.326 -0.500 0.071  -0.215 87  ASN HHH N   
9594  C CA  . ASN H 87  ? 4.290 3.008 2.349 -0.424 0.062  -0.209 87  ASN HHH CA  
9595  C C   . ASN H 87  ? 4.157 2.984 2.367 -0.394 0.062  -0.206 87  ASN HHH C   
9596  O O   . ASN H 87  ? 4.129 3.058 2.448 -0.436 0.069  -0.205 87  ASN HHH O   
9597  C CB  . ASN H 87  ? 4.517 3.057 2.380 -0.439 0.071  -0.194 87  ASN HHH CB  
9598  C CG  . ASN H 87  ? 4.830 3.230 2.513 -0.467 0.073  -0.195 87  ASN HHH CG  
9599  O OD1 . ASN H 87  ? 5.151 3.498 2.778 -0.413 0.061  -0.201 87  ASN HHH OD1 
9600  N ND2 . ASN H 87  ? 4.906 3.244 2.491 -0.553 0.089  -0.189 87  ASN HHH ND2 
9601  N N   . PHE H 88  ? 4.028 2.828 2.234 -0.318 0.052  -0.204 88  PHE HHH N   
9602  C CA  . PHE H 88  ? 3.863 2.746 2.186 -0.281 0.052  -0.199 88  PHE HHH CA  
9603  C C   . PHE H 88  ? 3.920 2.690 2.128 -0.243 0.054  -0.186 88  PHE HHH C   
9604  O O   . PHE H 88  ? 3.868 2.688 2.145 -0.187 0.050  -0.185 88  PHE HHH O   
9605  C CB  . PHE H 88  ? 3.739 2.737 2.201 -0.220 0.037  -0.213 88  PHE HHH CB  
9606  C CG  . PHE H 88  ? 3.645 2.770 2.245 -0.250 0.034  -0.227 88  PHE HHH CG  
9607  C CD1 . PHE H 88  ? 3.686 2.837 2.300 -0.321 0.043  -0.226 88  PHE HHH CD1 
9608  C CD2 . PHE H 88  ? 3.562 2.785 2.278 -0.204 0.020  -0.242 88  PHE HHH CD2 
9609  C CE1 . PHE H 88  ? 3.668 2.934 2.404 -0.342 0.039  -0.239 88  PHE HHH CE1 
9610  C CE2 . PHE H 88  ? 3.611 2.941 2.447 -0.229 0.016  -0.255 88  PHE HHH CE2 
9611  C CZ  . PHE H 88  ? 3.648 2.998 2.492 -0.295 0.025  -0.253 88  PHE HHH CZ  
9612  N N   . ILE H 89  ? 4.173 2.790 2.201 -0.272 0.061  -0.177 89  ILE HHH N   
9613  C CA  . ILE H 89  ? 4.405 2.897 2.304 -0.231 0.062  -0.166 89  ILE HHH CA  
9614  C C   . ILE H 89  ? 4.396 2.954 2.384 -0.234 0.070  -0.155 89  ILE HHH C   
9615  O O   . ILE H 89  ? 4.448 3.008 2.446 -0.170 0.066  -0.152 89  ILE HHH O   
9616  C CB  . ILE H 89  ? 4.579 2.888 2.265 -0.277 0.070  -0.158 89  ILE HHH CB  
9617  C CG1 . ILE H 89  ? 4.613 2.883 2.235 -0.299 0.065  -0.168 89  ILE HHH CG1 
9618  C CG2 . ILE H 89  ? 4.628 2.786 2.154 -0.215 0.065  -0.150 89  ILE HHH CG2 
9619  C CD1 . ILE H 89  ? 4.725 2.821 2.141 -0.358 0.075  -0.161 89  ILE HHH CD1 
9620  N N   . LEU H 90  ? 4.485 3.101 2.536 -0.307 0.083  -0.151 90  LEU HHH N   
9621  C CA  . LEU H 90  ? 4.411 3.084 2.537 -0.315 0.093  -0.140 90  LEU HHH CA  
9622  C C   . LEU H 90  ? 4.327 3.161 2.648 -0.275 0.087  -0.144 90  LEU HHH C   
9623  O O   . LEU H 90  ? 4.438 3.366 2.863 -0.271 0.080  -0.157 90  LEU HHH O   
9624  C CB  . LEU H 90  ? 4.244 2.934 2.372 -0.404 0.107  -0.135 90  LEU HHH CB  
9625  C CG  . LEU H 90  ? 4.335 2.866 2.267 -0.456 0.116  -0.130 90  LEU HHH CG  
9626  C CD1 . LEU H 90  ? 4.190 2.762 2.140 -0.542 0.130  -0.126 90  LEU HHH CD1 
9627  C CD2 . LEU H 90  ? 4.484 2.871 2.274 -0.410 0.114  -0.119 90  LEU HHH CD2 
9628  N N   . LYS H 91  ? 4.087 2.949 2.453 -0.249 0.092  -0.134 91  LYS HHH N   
9629  C CA  . LYS H 91  ? 3.898 2.900 2.434 -0.213 0.089  -0.136 91  LYS HHH CA  
9630  C C   . LYS H 91  ? 3.820 2.894 2.448 -0.255 0.102  -0.125 91  LYS HHH C   
9631  O O   . LYS H 91  ? 3.907 2.914 2.455 -0.290 0.113  -0.114 91  LYS HHH O   
9632  C CB  . LYS H 91  ? 3.856 2.840 2.370 -0.133 0.082  -0.135 91  LYS HHH CB  
9633  C CG  . LYS H 91  ? 3.721 2.816 2.353 -0.083 0.070  -0.150 91  LYS HHH CG  
9634  C CD  . LYS H 91  ? 3.699 2.785 2.301 -0.003 0.063  -0.152 91  LYS HHH CD  
9635  C CE  . LYS H 91  ? 3.582 2.781 2.293 0.043  0.050  -0.169 91  LYS HHH CE  
9636  N NZ  . LYS H 91  ? 3.553 2.779 2.259 0.118  0.044  -0.172 91  LYS HHH NZ  
9637  N N   . HIS H 92  ? 3.653 2.861 2.444 -0.251 0.101  -0.129 92  HIS HHH N   
9638  C CA  . HIS H 92  ? 3.444 2.731 2.335 -0.282 0.113  -0.119 92  HIS HHH CA  
9639  C C   . HIS H 92  ? 3.430 2.709 2.321 -0.248 0.119  -0.105 92  HIS HHH C   
9640  O O   . HIS H 92  ? 3.297 2.654 2.287 -0.209 0.117  -0.105 92  HIS HHH O   
9641  C CB  . HIS H 92  ? 3.196 2.613 2.248 -0.285 0.109  -0.128 92  HIS HHH CB  
9642  C CG  . HIS H 92  ? 3.098 2.535 2.160 -0.320 0.103  -0.142 92  HIS HHH CG  
9643  N ND1 . HIS H 92  ? 3.119 2.539 2.155 -0.297 0.090  -0.157 92  HIS HHH ND1 
9644  C CD2 . HIS H 92  ? 2.934 2.410 2.025 -0.373 0.107  -0.145 92  HIS HHH CD2 
9645  C CE1 . HIS H 92  ? 2.972 2.418 2.023 -0.336 0.088  -0.167 92  HIS HHH CE1 
9646  N NE2 . HIS H 92  ? 2.846 2.329 1.930 -0.382 0.098  -0.161 92  HIS HHH NE2 
9647  N N   . THR H 93  ? 3.532 2.717 2.309 -0.264 0.127  -0.094 93  THR HHH N   
9648  C CA  . THR H 93  ? 3.571 2.722 2.312 -0.225 0.132  -0.082 93  THR HHH CA  
9649  C C   . THR H 93  ? 3.361 2.580 2.188 -0.245 0.144  -0.068 93  THR HHH C   
9650  O O   . THR H 93  ? 3.396 2.606 2.214 -0.210 0.149  -0.058 93  THR HHH O   
9651  C CB  . THR H 93  ? 3.821 2.816 2.375 -0.227 0.133  -0.077 93  THR HHH CB  
9652  O OG1 . THR H 93  ? 3.965 2.918 2.463 -0.300 0.141  -0.075 93  THR HHH OG1 
9653  C CG2 . THR H 93  ? 3.883 2.798 2.338 -0.186 0.120  -0.088 93  THR HHH CG2 
9654  N N   . GLY H 94  ? 3.185 2.470 2.088 -0.297 0.150  -0.069 94  GLY HHH N   
9655  C CA  . GLY H 94  ? 3.016 2.359 1.990 -0.314 0.162  -0.056 94  GLY HHH CA  
9656  C C   . GLY H 94  ? 2.931 2.321 1.944 -0.374 0.167  -0.058 94  GLY HHH C   
9657  O O   . GLY H 94  ? 2.955 2.352 1.962 -0.403 0.161  -0.071 94  GLY HHH O   
9658  N N   . PRO H 95  ? 2.875 2.306 1.931 -0.391 0.177  -0.047 95  PRO HHH N   
9659  C CA  . PRO H 95  ? 2.732 2.214 1.819 -0.443 0.182  -0.050 95  PRO HHH CA  
9660  C C   . PRO H 95  ? 2.785 2.193 1.748 -0.492 0.183  -0.057 95  PRO HHH C   
9661  O O   . PRO H 95  ? 2.857 2.161 1.698 -0.493 0.185  -0.053 95  PRO HHH O   
9662  C CB  . PRO H 95  ? 2.668 2.183 1.794 -0.442 0.193  -0.035 95  PRO HHH CB  
9663  C CG  . PRO H 95  ? 2.784 2.296 1.943 -0.387 0.194  -0.024 95  PRO HHH CG  
9664  C CD  . PRO H 95  ? 2.917 2.352 1.992 -0.359 0.185  -0.031 95  PRO HHH CD  
9665  N N   . GLY H 96  ? 2.894 2.357 1.886 -0.534 0.181  -0.069 96  GLY HHH N   
9666  C CA  . GLY H 96  ? 3.012 2.428 1.898 -0.591 0.184  -0.077 96  GLY HHH CA  
9667  C C   . GLY H 96  ? 3.071 2.438 1.897 -0.599 0.176  -0.090 96  GLY HHH C   
9668  O O   . GLY H 96  ? 3.155 2.499 1.906 -0.654 0.178  -0.099 96  GLY HHH O   
9669  N N   . ILE H 97  ? 2.998 2.353 1.854 -0.548 0.166  -0.091 97  ILE HHH N   
9670  C CA  . ILE H 97  ? 3.051 2.366 1.857 -0.548 0.157  -0.104 97  ILE HHH CA  
9671  C C   . ILE H 97  ? 3.010 2.419 1.887 -0.585 0.155  -0.118 97  ILE HHH C   
9672  O O   . ILE H 97  ? 2.738 2.254 1.744 -0.573 0.153  -0.120 97  ILE HHH O   
9673  C CB  . ILE H 97  ? 3.021 2.330 1.867 -0.481 0.147  -0.105 97  ILE HHH CB  
9674  C CG1 . ILE H 97  ? 3.176 2.378 1.920 -0.443 0.148  -0.094 97  ILE HHH CG1 
9675  C CG2 . ILE H 97  ? 3.111 2.412 1.941 -0.479 0.136  -0.120 97  ILE HHH CG2 
9676  C CD1 . ILE H 97  ? 3.425 2.489 1.992 -0.470 0.149  -0.094 97  ILE HHH CD1 
9677  N N   . LEU H 98  ? 3.238 2.602 2.023 -0.629 0.155  -0.128 98  LEU HHH N   
9678  C CA  . LEU H 98  ? 3.159 2.609 1.995 -0.665 0.152  -0.143 98  LEU HHH CA  
9679  C C   . LEU H 98  ? 3.073 2.495 1.891 -0.645 0.141  -0.154 98  LEU HHH C   
9680  O O   . LEU H 98  ? 3.269 2.577 1.961 -0.648 0.141  -0.153 98  LEU HHH O   
9681  C CB  . LEU H 98  ? 3.275 2.716 2.024 -0.740 0.163  -0.148 98  LEU HHH CB  
9682  C CG  . LEU H 98  ? 3.206 2.771 2.029 -0.775 0.162  -0.164 98  LEU HHH CG  
9683  C CD1 . LEU H 98  ? 2.939 2.623 1.918 -0.737 0.157  -0.164 98  LEU HHH CD1 
9684  C CD2 . LEU H 98  ? 3.431 3.010 2.180 -0.850 0.174  -0.169 98  LEU HHH CD2 
9685  N N   . SER H 99  ? 2.906 2.425 1.844 -0.622 0.132  -0.164 99  SER HHH N   
9686  C CA  . SER H 99  ? 2.990 2.496 1.928 -0.597 0.121  -0.176 99  SER HHH CA  
9687  C C   . SER H 99  ? 2.927 2.544 1.958 -0.613 0.115  -0.192 99  SER HHH C   
9688  O O   . SER H 99  ? 2.741 2.453 1.868 -0.618 0.117  -0.193 99  SER HHH O   
9689  C CB  . SER H 99  ? 2.953 2.448 1.943 -0.528 0.112  -0.172 99  SER HHH CB  
9690  O OG  . SER H 99  ? 3.115 2.633 2.140 -0.502 0.099  -0.186 99  SER HHH OG  
9691  N N   . MET H 100 ? 2.974 2.576 1.972 -0.616 0.107  -0.204 100 MET HHH N   
9692  C CA  . MET H 100 ? 2.798 2.500 1.873 -0.629 0.101  -0.221 100 MET HHH CA  
9693  C C   . MET H 100 ? 2.659 2.433 1.869 -0.576 0.088  -0.228 100 MET HHH C   
9694  O O   . MET H 100 ? 2.658 2.395 1.880 -0.530 0.082  -0.224 100 MET HHH O   
9695  C CB  . MET H 100 ? 2.852 2.512 1.841 -0.652 0.098  -0.233 100 MET HHH CB  
9696  C CG  . MET H 100 ? 2.973 2.569 1.828 -0.717 0.111  -0.229 100 MET HHH CG  
9697  S SD  . MET H 100 ? 2.947 2.673 1.847 -0.779 0.117  -0.243 100 MET HHH SD  
9698  C CE  . MET H 100 ? 2.831 2.655 1.835 -0.748 0.102  -0.263 100 MET HHH CE  
9699  N N   . ALA H 101 ? 2.565 2.443 1.870 -0.583 0.085  -0.238 101 ALA HHH N   
9700  C CA  . ALA H 101 ? 2.518 2.460 1.939 -0.541 0.072  -0.248 101 ALA HHH CA  
9701  C C   . ALA H 101 ? 2.666 2.608 2.072 -0.535 0.061  -0.265 101 ALA HHH C   
9702  O O   . ALA H 101 ? 2.867 2.790 2.193 -0.571 0.064  -0.271 101 ALA HHH O   
9703  C CB  . ALA H 101 ? 2.328 2.370 1.848 -0.543 0.072  -0.253 101 ALA HHH CB  
9704  N N   . ASN H 102 ? 2.706 2.668 2.186 -0.492 0.049  -0.273 102 ASN HHH N   
9705  C CA  . ASN H 102 ? 2.763 2.734 2.241 -0.482 0.036  -0.291 102 ASN HHH CA  
9706  C C   . ASN H 102 ? 2.669 2.699 2.263 -0.442 0.023  -0.302 102 ASN HHH C   
9707  O O   . ASN H 102 ? 2.686 2.706 2.323 -0.411 0.022  -0.295 102 ASN HHH O   
9708  C CB  . ASN H 102 ? 3.004 2.879 2.377 -0.471 0.035  -0.288 102 ASN HHH CB  
9709  C CG  . ASN H 102 ? 3.081 2.899 2.441 -0.436 0.037  -0.273 102 ASN HHH CG  
9710  O OD1 . ASN H 102 ? 3.195 2.987 2.532 -0.448 0.049  -0.257 102 ASN HHH OD1 
9711  N ND2 . ASN H 102 ? 3.033 2.835 2.403 -0.392 0.026  -0.280 102 ASN HHH ND2 
9712  N N   . ALA H 103 ? 2.618 2.711 2.260 -0.445 0.013  -0.321 103 ALA HHH N   
9713  C CA  . ALA H 103 ? 2.622 2.768 2.368 -0.412 -0.000 -0.334 103 ALA HHH CA  
9714  C C   . ALA H 103 ? 2.637 2.749 2.381 -0.378 -0.010 -0.340 103 ALA HHH C   
9715  O O   . ALA H 103 ? 2.550 2.692 2.376 -0.351 -0.018 -0.347 103 ALA HHH O   
9716  C CB  . ALA H 103 ? 2.526 2.738 2.306 -0.421 -0.010 -0.354 103 ALA HHH CB  
9717  N N   . GLY H 104 ? 2.806 2.855 2.452 -0.381 -0.009 -0.338 104 GLY HHH N   
9718  C CA  . GLY H 104 ? 2.774 2.790 2.398 -0.345 -0.019 -0.346 104 GLY HHH CA  
9719  C C   . GLY H 104 ? 2.909 2.832 2.398 -0.353 -0.013 -0.336 104 GLY HHH C   
9720  O O   . GLY H 104 ? 2.996 2.882 2.411 -0.391 -0.000 -0.325 104 GLY HHH O   
9721  N N   . PRO H 105 ? 2.648 2.526 2.093 -0.315 -0.021 -0.341 105 PRO HHH N   
9722  C CA  . PRO H 105 ? 2.797 2.571 2.097 -0.318 -0.017 -0.333 105 PRO HHH CA  
9723  C C   . PRO H 105 ? 2.892 2.651 2.124 -0.363 -0.013 -0.337 105 PRO HHH C   
9724  O O   . PRO H 105 ? 2.946 2.765 2.227 -0.366 -0.022 -0.354 105 PRO HHH O   
9725  C CB  . PRO H 105 ? 2.796 2.551 2.083 -0.262 -0.031 -0.344 105 PRO HHH CB  
9726  C CG  . PRO H 105 ? 2.654 2.506 2.083 -0.235 -0.041 -0.357 105 PRO HHH CG  
9727  C CD  . PRO H 105 ? 2.525 2.450 2.049 -0.271 -0.037 -0.357 105 PRO HHH CD  
9728  N N   . ASN H 106 ? 2.986 2.664 2.100 -0.399 0.001  -0.322 106 ASN HHH N   
9729  C CA  . ASN H 106 ? 3.096 2.745 2.120 -0.449 0.007  -0.325 106 ASN HHH CA  
9730  C C   . ASN H 106 ? 2.980 2.740 2.092 -0.485 0.008  -0.336 106 ASN HHH C   
9731  O O   . ASN H 106 ? 2.956 2.747 2.057 -0.503 0.004  -0.349 106 ASN HHH O   
9732  C CB  . ASN H 106 ? 3.196 2.790 2.142 -0.427 -0.003 -0.335 106 ASN HHH CB  
9733  C CG  . ASN H 106 ? 3.391 2.878 2.245 -0.381 -0.006 -0.326 106 ASN HHH CG  
9734  O OD1 . ASN H 106 ? 3.624 3.016 2.374 -0.394 0.005  -0.310 106 ASN HHH OD1 
9735  N ND2 . ASN H 106 ? 3.317 2.821 2.207 -0.324 -0.022 -0.339 106 ASN HHH ND2 
9736  N N   . THR H 107 ? 3.018 2.840 2.214 -0.494 0.014  -0.330 107 THR HHH N   
9737  C CA  . THR H 107 ? 2.968 2.895 2.246 -0.521 0.015  -0.339 107 THR HHH CA  
9738  C C   . THR H 107 ? 2.918 2.852 2.177 -0.561 0.031  -0.325 107 THR HHH C   
9739  O O   . THR H 107 ? 2.848 2.865 2.195 -0.565 0.031  -0.328 107 THR HHH O   
9740  C CB  . THR H 107 ? 2.937 2.949 2.358 -0.480 0.001  -0.351 107 THR HHH CB  
9741  O OG1 . THR H 107 ? 2.997 2.994 2.463 -0.454 0.004  -0.337 107 THR HHH OG1 
9742  C CG2 . THR H 107 ? 2.986 3.001 2.427 -0.444 -0.015 -0.367 107 THR HHH CG2 
9743  N N   . ASN H 108 ? 2.971 2.811 2.108 -0.591 0.043  -0.311 108 ASN HHH N   
9744  C CA  . ASN H 108 ? 2.914 2.753 2.016 -0.635 0.058  -0.299 108 ASN HHH CA  
9745  C C   . ASN H 108 ? 2.921 2.843 2.023 -0.688 0.064  -0.311 108 ASN HHH C   
9746  O O   . ASN H 108 ? 3.098 3.022 2.150 -0.712 0.063  -0.322 108 ASN HHH O   
9747  C CB  . ASN H 108 ? 3.045 2.750 2.000 -0.656 0.069  -0.284 108 ASN HHH CB  
9748  C CG  . ASN H 108 ? 3.071 2.698 2.017 -0.598 0.063  -0.273 108 ASN HHH CG  
9749  O OD1 . ASN H 108 ? 3.038 2.684 2.048 -0.573 0.064  -0.264 108 ASN HHH OD1 
9750  N ND2 . ASN H 108 ? 3.204 2.750 2.072 -0.573 0.056  -0.276 108 ASN HHH ND2 
9751  N N   . GLY H 109 ? 2.689 2.685 1.847 -0.706 0.071  -0.309 109 GLY HHH N   
9752  C CA  . GLY H 109 ? 2.825 2.909 1.978 -0.755 0.077  -0.321 109 GLY HHH CA  
9753  C C   . GLY H 109 ? 2.921 3.004 2.021 -0.805 0.093  -0.311 109 GLY HHH C   
9754  O O   . GLY H 109 ? 3.090 3.078 2.070 -0.845 0.104  -0.301 109 GLY HHH O   
9755  N N   . SER H 110 ? 2.816 3.000 2.000 -0.802 0.094  -0.314 110 SER HHH N   
9756  C CA  . SER H 110 ? 2.816 3.013 1.963 -0.844 0.108  -0.306 110 SER HHH CA  
9757  C C   . SER H 110 ? 2.606 2.812 1.831 -0.803 0.107  -0.294 110 SER HHH C   
9758  O O   . SER H 110 ? 2.559 2.823 1.799 -0.823 0.115  -0.292 110 SER HHH O   
9759  C CB  . SER H 110 ? 3.004 3.326 2.159 -0.889 0.113  -0.324 110 SER HHH CB  
9760  O OG  . SER H 110 ? 3.014 3.450 2.287 -0.846 0.100  -0.338 110 SER HHH OG  
9761  N N   . GLN H 111 ? 2.511 2.668 1.788 -0.747 0.098  -0.285 111 GLN HHH N   
9762  C CA  . GLN H 111 ? 2.350 2.518 1.704 -0.709 0.098  -0.273 111 GLN HHH CA  
9763  C C   . GLN H 111 ? 2.388 2.440 1.686 -0.696 0.103  -0.253 111 GLN HHH C   
9764  O O   . GLN H 111 ? 2.437 2.409 1.688 -0.680 0.099  -0.251 111 GLN HHH O   
9765  C CB  . GLN H 111 ? 2.273 2.496 1.744 -0.654 0.083  -0.281 111 GLN HHH CB  
9766  C CG  . GLN H 111 ? 2.240 2.580 1.770 -0.657 0.076  -0.301 111 GLN HHH CG  
9767  C CD  . GLN H 111 ? 2.041 2.423 1.680 -0.604 0.062  -0.308 111 GLN HHH CD  
9768  O OE1 . GLN H 111 ? 2.003 2.472 1.692 -0.594 0.054  -0.324 111 GLN HHH OE1 
9769  N NE2 . GLN H 111 ? 1.909 2.228 1.579 -0.568 0.058  -0.297 111 GLN HHH NE2 
9770  N N   . PHE H 112 ? 2.396 2.444 1.696 -0.700 0.112  -0.239 112 PHE HHH N   
9771  C CA  . PHE H 112 ? 2.370 2.317 1.612 -0.692 0.119  -0.220 112 PHE HHH CA  
9772  C C   . PHE H 112 ? 2.224 2.202 1.557 -0.652 0.120  -0.208 112 PHE HHH C   
9773  O O   . PHE H 112 ? 2.052 2.121 1.465 -0.648 0.119  -0.213 112 PHE HHH O   
9774  C CB  . PHE H 112 ? 2.475 2.376 1.603 -0.749 0.133  -0.214 112 PHE HHH CB  
9775  C CG  . PHE H 112 ? 2.489 2.487 1.649 -0.781 0.140  -0.219 112 PHE HHH CG  
9776  C CD1 . PHE H 112 ? 2.500 2.595 1.677 -0.813 0.139  -0.238 112 PHE HHH CD1 
9777  C CD2 . PHE H 112 ? 2.557 2.556 1.732 -0.775 0.148  -0.205 112 PHE HHH CD2 
9778  C CE1 . PHE H 112 ? 2.521 2.716 1.728 -0.838 0.144  -0.244 112 PHE HHH CE1 
9779  C CE2 . PHE H 112 ? 2.582 2.674 1.786 -0.801 0.153  -0.210 112 PHE HHH CE2 
9780  C CZ  . PHE H 112 ? 2.469 2.662 1.689 -0.831 0.151  -0.230 112 PHE HHH CZ  
9781  N N   . PHE H 113 ? 2.283 2.186 1.601 -0.622 0.121  -0.193 113 PHE HHH N   
9782  C CA  . PHE H 113 ? 2.224 2.149 1.615 -0.590 0.124  -0.179 113 PHE HHH CA  
9783  C C   . PHE H 113 ? 2.275 2.121 1.588 -0.597 0.135  -0.162 113 PHE HHH C   
9784  O O   . PHE H 113 ? 2.447 2.200 1.668 -0.597 0.136  -0.158 113 PHE HHH O   
9785  C CB  . PHE H 113 ? 2.224 2.159 1.702 -0.539 0.115  -0.180 113 PHE HHH CB  
9786  C CG  . PHE H 113 ? 2.307 2.162 1.732 -0.514 0.110  -0.178 113 PHE HHH CG  
9787  C CD1 . PHE H 113 ? 2.314 2.109 1.708 -0.491 0.116  -0.162 113 PHE HHH CD1 
9788  C CD2 . PHE H 113 ? 2.438 2.282 1.843 -0.510 0.100  -0.193 113 PHE HHH CD2 
9789  C CE1 . PHE H 113 ? 2.427 2.156 1.770 -0.461 0.110  -0.163 113 PHE HHH CE1 
9790  C CE2 . PHE H 113 ? 2.540 2.314 1.894 -0.482 0.095  -0.192 113 PHE HHH CE2 
9791  C CZ  . PHE H 113 ? 2.504 2.221 1.826 -0.456 0.099  -0.178 113 PHE HHH CZ  
9792  N N   . ILE H 114 ? 2.230 2.110 1.573 -0.602 0.144  -0.152 114 ILE HHH N   
9793  C CA  . ILE H 114 ? 2.288 2.101 1.563 -0.608 0.154  -0.135 114 ILE HHH CA  
9794  C C   . ILE H 114 ? 2.254 2.063 1.597 -0.557 0.154  -0.121 114 ILE HHH C   
9795  O O   . ILE H 114 ? 2.143 2.020 1.580 -0.540 0.155  -0.118 114 ILE HHH O   
9796  C CB  . ILE H 114 ? 2.239 2.097 1.500 -0.647 0.164  -0.134 114 ILE HHH CB  
9797  C CG1 . ILE H 114 ? 2.200 2.111 1.435 -0.695 0.162  -0.153 114 ILE HHH CG1 
9798  C CG2 . ILE H 114 ? 2.223 1.995 1.382 -0.665 0.174  -0.121 114 ILE HHH CG2 
9799  C CD1 . ILE H 114 ? 2.087 2.083 1.341 -0.724 0.169  -0.157 114 ILE HHH CD1 
9800  N N   . CYS H 115 ? 2.325 2.053 1.615 -0.531 0.153  -0.114 115 CYS HHH N   
9801  C CA  . CYS H 115 ? 2.289 2.019 1.639 -0.484 0.154  -0.103 115 CYS HHH CA  
9802  C C   . CYS H 115 ? 2.289 2.022 1.643 -0.485 0.165  -0.086 115 CYS HHH C   
9803  O O   . CYS H 115 ? 2.427 2.113 1.695 -0.512 0.173  -0.080 115 CYS HHH O   
9804  C CB  . CYS H 115 ? 2.399 2.049 1.682 -0.452 0.149  -0.101 115 CYS HHH CB  
9805  S SG  . CYS H 115 ? 2.434 2.077 1.713 -0.439 0.134  -0.120 115 CYS HHH SG  
9806  N N   . THR H 116 ? 2.157 1.944 1.610 -0.456 0.167  -0.078 116 THR HHH N   
9807  C CA  . THR H 116 ? 2.156 1.945 1.618 -0.450 0.179  -0.060 116 THR HHH CA  
9808  C C   . THR H 116 ? 2.185 1.954 1.669 -0.407 0.180  -0.049 116 THR HHH C   
9809  O O   . THR H 116 ? 2.166 1.946 1.676 -0.394 0.190  -0.034 116 THR HHH O   
9810  C CB  . THR H 116 ? 2.032 1.903 1.585 -0.456 0.181  -0.058 116 THR HHH CB  
9811  O OG1 . THR H 116 ? 1.850 1.767 1.497 -0.432 0.174  -0.064 116 THR HHH OG1 
9812  C CG2 . THR H 116 ? 2.064 1.968 1.593 -0.495 0.180  -0.071 116 THR HHH CG2 
9813  N N   . ALA H 117 ? 2.346 2.090 1.817 -0.384 0.172  -0.058 117 ALA HHH N   
9814  C CA  . ALA H 117 ? 2.439 2.171 1.921 -0.340 0.172  -0.052 117 ALA HHH CA  
9815  C C   . ALA H 117 ? 2.613 2.290 2.023 -0.322 0.161  -0.064 117 ALA HHH C   
9816  O O   . ALA H 117 ? 2.679 2.333 2.046 -0.345 0.154  -0.076 117 ALA HHH O   
9817  C CB  . ALA H 117 ? 2.374 2.186 1.980 -0.322 0.172  -0.051 117 ALA HHH CB  
9818  N N   . LYS H 118 ? 2.608 2.267 2.002 -0.279 0.160  -0.061 118 LYS HHH N   
9819  C CA  . LYS H 118 ? 2.694 2.311 2.030 -0.249 0.149  -0.073 118 LYS HHH CA  
9820  C C   . LYS H 118 ? 2.709 2.402 2.145 -0.244 0.139  -0.088 118 LYS HHH C   
9821  O O   . LYS H 118 ? 2.612 2.383 2.156 -0.236 0.142  -0.087 118 LYS HHH O   
9822  C CB  . LYS H 118 ? 2.731 2.319 2.025 -0.199 0.149  -0.067 118 LYS HHH CB  
9823  C CG  . LYS H 118 ? 2.822 2.369 2.050 -0.158 0.137  -0.080 118 LYS HHH CG  
9824  C CD  . LYS H 118 ? 2.839 2.362 2.018 -0.103 0.137  -0.075 118 LYS HHH CD  
9825  C CE  . LYS H 118 ? 3.007 2.487 2.111 -0.054 0.123  -0.089 118 LYS HHH CE  
9826  N NZ  . LYS H 118 ? 3.028 2.491 2.081 0.007  0.122  -0.086 118 LYS HHH NZ  
9827  N N   . THR H 119 ? 2.796 2.462 2.192 -0.250 0.128  -0.103 119 THR HHH N   
9828  C CA  . THR H 119 ? 2.712 2.445 2.195 -0.250 0.118  -0.120 119 THR HHH CA  
9829  C C   . THR H 119 ? 2.837 2.546 2.277 -0.214 0.105  -0.135 119 THR HHH C   
9830  O O   . THR H 119 ? 2.919 2.600 2.317 -0.226 0.096  -0.147 119 THR HHH O   
9831  C CB  . THR H 119 ? 2.593 2.339 2.088 -0.296 0.117  -0.126 119 THR HHH CB  
9832  O OG1 . THR H 119 ? 2.583 2.247 1.956 -0.316 0.116  -0.128 119 THR HHH OG1 
9833  C CG2 . THR H 119 ? 2.506 2.289 2.052 -0.325 0.128  -0.114 119 THR HHH CG2 
9834  N N   . GLU H 120 ? 2.953 2.676 2.400 -0.168 0.103  -0.135 120 GLU HHH N   
9835  C CA  . GLU H 120 ? 3.042 2.731 2.423 -0.124 0.091  -0.148 120 GLU HHH CA  
9836  C C   . GLU H 120 ? 2.924 2.672 2.373 -0.123 0.078  -0.168 120 GLU HHH C   
9837  O O   . GLU H 120 ? 3.043 2.752 2.427 -0.099 0.066  -0.181 120 GLU HHH O   
9838  C CB  . GLU H 120 ? 3.177 2.894 2.567 -0.071 0.091  -0.145 120 GLU HHH CB  
9839  C CG  . GLU H 120 ? 3.328 3.027 2.701 -0.073 0.106  -0.125 120 GLU HHH CG  
9840  C CD  . GLU H 120 ? 3.246 3.040 2.751 -0.098 0.116  -0.117 120 GLU HHH CD  
9841  O OE1 . GLU H 120 ? 3.163 3.041 2.771 -0.099 0.112  -0.129 120 GLU HHH OE1 
9842  O OE2 . GLU H 120 ? 3.261 3.039 2.761 -0.116 0.129  -0.099 120 GLU HHH OE2 
9843  N N   . TRP H 121 ? 2.609 2.445 2.184 -0.146 0.079  -0.172 121 TRP HHH N   
9844  C CA  . TRP H 121 ? 2.483 2.374 2.124 -0.147 0.067  -0.193 121 TRP HHH CA  
9845  C C   . TRP H 121 ? 2.505 2.352 2.095 -0.176 0.061  -0.200 121 TRP HHH C   
9846  O O   . TRP H 121 ? 2.500 2.377 2.121 -0.171 0.048  -0.218 121 TRP HHH O   
9847  C CB  . TRP H 121 ? 2.355 2.339 2.132 -0.166 0.070  -0.194 121 TRP HHH CB  
9848  C CG  . TRP H 121 ? 2.301 2.283 2.106 -0.209 0.081  -0.181 121 TRP HHH CG  
9849  C CD1 . TRP H 121 ? 2.219 2.209 2.048 -0.241 0.078  -0.187 121 TRP HHH CD1 
9850  C CD2 . TRP H 121 ? 2.395 2.372 2.207 -0.219 0.096  -0.160 121 TRP HHH CD2 
9851  N NE1 . TRP H 121 ? 2.206 2.198 2.054 -0.269 0.089  -0.171 121 TRP HHH NE1 
9852  C CE2 . TRP H 121 ? 2.290 2.272 2.128 -0.257 0.101  -0.154 121 TRP HHH CE2 
9853  C CE3 . TRP H 121 ? 2.549 2.521 2.345 -0.197 0.106  -0.146 121 TRP HHH CE3 
9854  C CZ2 . TRP H 121 ? 2.276 2.257 2.125 -0.273 0.114  -0.135 121 TRP HHH CZ2 
9855  C CZ3 . TRP H 121 ? 2.568 2.536 2.376 -0.216 0.120  -0.126 121 TRP HHH CZ3 
9856  C CH2 . TRP H 121 ? 2.405 2.376 2.238 -0.253 0.124  -0.121 121 TRP HHH CH2 
9857  N N   . LEU H 122 ? 2.724 2.507 2.239 -0.208 0.069  -0.188 122 LEU HHH N   
9858  C CA  . LEU H 122 ? 2.771 2.513 2.226 -0.238 0.065  -0.195 122 LEU HHH CA  
9859  C C   . LEU H 122 ? 2.998 2.643 2.316 -0.219 0.060  -0.197 122 LEU HHH C   
9860  O O   . LEU H 122 ? 3.068 2.674 2.326 -0.241 0.056  -0.205 122 LEU HHH O   
9861  C CB  . LEU H 122 ? 2.722 2.454 2.164 -0.288 0.077  -0.183 122 LEU HHH CB  
9862  C CG  . LEU H 122 ? 2.542 2.359 2.105 -0.306 0.082  -0.180 122 LEU HHH CG  
9863  C CD1 . LEU H 122 ? 2.442 2.250 1.980 -0.349 0.093  -0.169 122 LEU HHH CD1 
9864  C CD2 . LEU H 122 ? 2.476 2.359 2.125 -0.307 0.070  -0.199 122 LEU HHH CD2 
9865  N N   . ASP H 123 ? 3.131 2.733 2.393 -0.176 0.060  -0.191 123 ASP HHH N   
9866  C CA  . ASP H 123 ? 3.386 2.881 2.503 -0.150 0.055  -0.192 123 ASP HHH CA  
9867  C C   . ASP H 123 ? 3.394 2.900 2.509 -0.127 0.040  -0.212 123 ASP HHH C   
9868  O O   . ASP H 123 ? 3.369 2.966 2.586 -0.099 0.031  -0.225 123 ASP HHH O   
9869  C CB  . ASP H 123 ? 3.615 3.081 2.689 -0.096 0.056  -0.184 123 ASP HHH CB  
9870  C CG  . ASP H 123 ? 3.749 3.178 2.792 -0.117 0.071  -0.164 123 ASP HHH CG  
9871  O OD1 . ASP H 123 ? 3.785 3.192 2.813 -0.173 0.080  -0.156 123 ASP HHH OD1 
9872  O OD2 . ASP H 123 ? 3.815 3.247 2.853 -0.077 0.073  -0.157 123 ASP HHH OD2 
9873  N N   . GLY H 124 ? 3.474 2.889 2.471 -0.141 0.037  -0.214 124 GLY HHH N   
9874  C CA  . GLY H 124 ? 3.483 2.898 2.463 -0.118 0.022  -0.232 124 GLY HHH CA  
9875  C C   . GLY H 124 ? 3.351 2.844 2.424 -0.156 0.019  -0.245 124 GLY HHH C   
9876  O O   . GLY H 124 ? 3.451 2.951 2.517 -0.140 0.006  -0.261 124 GLY HHH O   
9877  N N   . LYS H 125 ? 3.214 2.768 2.374 -0.202 0.028  -0.239 125 LYS HHH N   
9878  C CA  . LYS H 125 ? 3.070 2.700 2.319 -0.237 0.025  -0.250 125 LYS HHH CA  
9879  C C   . LYS H 125 ? 3.121 2.730 2.329 -0.298 0.035  -0.244 125 LYS HHH C   
9880  O O   . LYS H 125 ? 3.061 2.700 2.284 -0.323 0.031  -0.255 125 LYS HHH O   
9881  C CB  . LYS H 125 ? 2.859 2.601 2.263 -0.230 0.024  -0.254 125 LYS HHH CB  
9882  C CG  . LYS H 125 ? 2.747 2.530 2.203 -0.177 0.015  -0.262 125 LYS HHH CG  
9883  C CD  . LYS H 125 ? 2.553 2.439 2.156 -0.181 0.015  -0.267 125 LYS HHH CD  
9884  C CE  . LYS H 125 ? 2.426 2.359 2.076 -0.135 0.009  -0.274 125 LYS HHH CE  
9885  N NZ  . LYS H 125 ? 2.394 2.412 2.171 -0.147 0.014  -0.273 125 LYS HHH NZ  
9886  N N   . HIS H 126 ? 3.236 2.799 2.392 -0.322 0.049  -0.226 126 HIS HHH N   
9887  C CA  . HIS H 126 ? 3.230 2.782 2.346 -0.382 0.060  -0.221 126 HIS HHH CA  
9888  C C   . HIS H 126 ? 3.335 2.762 2.290 -0.401 0.068  -0.209 126 HIS HHH C   
9889  O O   . HIS H 126 ? 3.396 2.746 2.280 -0.363 0.067  -0.201 126 HIS HHH O   
9890  C CB  . HIS H 126 ? 3.127 2.751 2.337 -0.401 0.069  -0.211 126 HIS HHH CB  
9891  C CG  . HIS H 126 ? 3.011 2.745 2.366 -0.390 0.062  -0.222 126 HIS HHH CG  
9892  N ND1 . HIS H 126 ? 2.891 2.691 2.298 -0.422 0.061  -0.232 126 HIS HHH ND1 
9893  C CD2 . HIS H 126 ? 2.935 2.722 2.389 -0.352 0.056  -0.225 126 HIS HHH CD2 
9894  C CE1 . HIS H 126 ? 2.755 2.633 2.281 -0.401 0.053  -0.240 126 HIS HHH CE1 
9895  N NE2 . HIS H 126 ? 2.766 2.637 2.323 -0.363 0.051  -0.235 126 HIS HHH NE2 
9896  N N   . VAL H 127 ? 3.229 2.635 2.121 -0.460 0.076  -0.209 127 VAL HHH N   
9897  C CA  . VAL H 127 ? 3.374 2.653 2.097 -0.491 0.084  -0.202 127 VAL HHH CA  
9898  C C   . VAL H 127 ? 3.337 2.597 2.030 -0.527 0.098  -0.187 127 VAL HHH C   
9899  O O   . VAL H 127 ? 3.251 2.585 1.996 -0.575 0.106  -0.189 127 VAL HHH O   
9900  C CB  . VAL H 127 ? 3.444 2.714 2.108 -0.541 0.085  -0.212 127 VAL HHH CB  
9901  C CG1 . VAL H 127 ? 3.693 2.816 2.169 -0.574 0.093  -0.205 127 VAL HHH CG1 
9902  C CG2 . VAL H 127 ? 3.460 2.773 2.177 -0.506 0.070  -0.228 127 VAL HHH CG2 
9903  N N   . VAL H 128 ? 3.584 2.743 2.185 -0.505 0.102  -0.174 128 VAL HHH N   
9904  C CA  . VAL H 128 ? 3.595 2.723 2.155 -0.535 0.115  -0.161 128 VAL HHH CA  
9905  C C   . VAL H 128 ? 3.742 2.771 2.149 -0.602 0.125  -0.159 128 VAL HHH C   
9906  O O   . VAL H 128 ? 3.809 2.710 2.074 -0.595 0.122  -0.158 128 VAL HHH O   
9907  C CB  . VAL H 128 ? 3.632 2.696 2.160 -0.479 0.114  -0.148 128 VAL HHH CB  
9908  C CG1 . VAL H 128 ? 3.661 2.693 2.147 -0.511 0.127  -0.135 128 VAL HHH CG1 
9909  C CG2 . VAL H 128 ? 3.447 2.616 2.127 -0.421 0.106  -0.151 128 VAL HHH CG2 
9910  N N   . PHE H 129 ? 3.633 2.723 2.063 -0.666 0.135  -0.161 129 PHE HHH N   
9911  C CA  . PHE H 129 ? 3.739 2.755 2.031 -0.740 0.146  -0.162 129 PHE HHH CA  
9912  C C   . PHE H 129 ? 3.869 2.870 2.117 -0.789 0.160  -0.153 129 PHE HHH C   
9913  O O   . PHE H 129 ? 4.033 2.977 2.165 -0.859 0.170  -0.156 129 PHE HHH O   
9914  C CB  . PHE H 129 ? 3.688 2.796 2.023 -0.788 0.146  -0.178 129 PHE HHH CB  
9915  C CG  . PHE H 129 ? 3.491 2.761 1.973 -0.806 0.149  -0.184 129 PHE HHH CG  
9916  C CD1 . PHE H 129 ? 3.337 2.718 1.975 -0.755 0.138  -0.190 129 PHE HHH CD1 
9917  C CD2 . PHE H 129 ? 3.496 2.807 1.954 -0.875 0.161  -0.186 129 PHE HHH CD2 
9918  C CE1 . PHE H 129 ? 3.214 2.731 1.974 -0.768 0.139  -0.195 129 PHE HHH CE1 
9919  C CE2 . PHE H 129 ? 3.371 2.831 1.956 -0.885 0.162  -0.193 129 PHE HHH CE2 
9920  C CZ  . PHE H 129 ? 3.246 2.804 1.979 -0.829 0.151  -0.197 129 PHE HHH CZ  
9921  N N   . GLY H 130 ? 3.965 3.015 2.298 -0.759 0.161  -0.144 130 GLY HHH N   
9922  C CA  . GLY H 130 ? 3.962 2.999 2.249 -0.805 0.174  -0.137 130 GLY HHH CA  
9923  C C   . GLY H 130 ? 3.834 2.897 2.195 -0.757 0.174  -0.124 130 GLY HHH C   
9924  O O   . GLY H 130 ? 3.757 2.848 2.202 -0.689 0.165  -0.120 130 GLY HHH O   
9925  N N   . LYS H 131 ? 3.758 2.817 2.085 -0.797 0.185  -0.119 131 LYS HHH N   
9926  C CA  . LYS H 131 ? 3.601 2.689 1.991 -0.761 0.188  -0.106 131 LYS HHH CA  
9927  C C   . LYS H 131 ? 3.570 2.729 1.978 -0.820 0.199  -0.108 131 LYS HHH C   
9928  O O   . LYS H 131 ? 3.626 2.754 1.938 -0.890 0.206  -0.115 131 LYS HHH O   
9929  C CB  . LYS H 131 ? 3.695 2.633 1.961 -0.728 0.188  -0.094 131 LYS HHH CB  
9930  C CG  . LYS H 131 ? 3.553 2.497 1.849 -0.699 0.193  -0.080 131 LYS HHH CG  
9931  C CD  . LYS H 131 ? 3.384 2.439 1.844 -0.637 0.188  -0.075 131 LYS HHH CD  
9932  C CE  . LYS H 131 ? 3.336 2.387 1.810 -0.611 0.194  -0.060 131 LYS HHH CE  
9933  N NZ  . LYS H 131 ? 3.236 2.306 1.684 -0.669 0.205  -0.059 131 LYS HHH NZ  
9934  N N   . VAL H 132 ? 3.486 2.743 2.018 -0.790 0.200  -0.101 132 VAL HHH N   
9935  C CA  . VAL H 132 ? 3.396 2.719 1.950 -0.828 0.209  -0.101 132 VAL HHH CA  
9936  C C   . VAL H 132 ? 3.600 2.809 2.020 -0.854 0.217  -0.092 132 VAL HHH C   
9937  O O   . VAL H 132 ? 3.668 2.784 2.043 -0.809 0.216  -0.079 132 VAL HHH O   
9938  C CB  . VAL H 132 ? 3.079 2.511 1.784 -0.779 0.208  -0.093 132 VAL HHH CB  
9939  C CG1 . VAL H 132 ? 3.154 2.646 1.872 -0.812 0.217  -0.091 132 VAL HHH CG1 
9940  C CG2 . VAL H 132 ? 2.950 2.494 1.781 -0.760 0.199  -0.103 132 VAL HHH CG2 
9941  N N   . LYS H 133 ? 3.580 2.799 1.933 -0.929 0.226  -0.101 133 LYS HHH N   
9942  C CA  . LYS H 133 ? 3.673 2.790 1.895 -0.966 0.235  -0.096 133 LYS HHH CA  
9943  C C   . LYS H 133 ? 3.578 2.787 1.870 -0.970 0.241  -0.092 133 LYS HHH C   
9944  O O   . LYS H 133 ? 3.535 2.682 1.794 -0.945 0.244  -0.079 133 LYS HHH O   
9945  C CB  . LYS H 133 ? 3.887 2.940 1.968 -1.054 0.242  -0.108 133 LYS HHH CB  
9946  C CG  . LYS H 133 ? 4.094 3.017 2.024 -1.091 0.250  -0.103 133 LYS HHH CG  
9947  C CD  . LYS H 133 ? 4.216 3.061 1.991 -1.185 0.258  -0.115 133 LYS HHH CD  
9948  C CE  . LYS H 133 ? 4.490 3.176 2.103 -1.210 0.264  -0.108 133 LYS HHH CE  
9949  N NZ  . LYS H 133 ? 4.698 3.286 2.141 -1.309 0.274  -0.119 133 LYS HHH NZ  
9950  N N   . GLU H 134 ? 3.653 3.011 2.040 -0.999 0.243  -0.104 134 GLU HHH N   
9951  C CA  . GLU H 134 ? 3.623 3.083 2.089 -0.995 0.247  -0.101 134 GLU HHH CA  
9952  C C   . GLU H 134 ? 3.381 2.991 2.010 -0.955 0.241  -0.105 134 GLU HHH C   
9953  O O   . GLU H 134 ? 3.282 2.944 1.956 -0.958 0.235  -0.116 134 GLU HHH O   
9954  C CB  . GLU H 134 ? 3.892 3.389 2.287 -1.080 0.256  -0.116 134 GLU HHH CB  
9955  C CG  . GLU H 134 ? 4.201 3.721 2.593 -1.086 0.263  -0.110 134 GLU HHH CG  
9956  C CD  . GLU H 134 ? 4.205 3.881 2.749 -1.046 0.261  -0.110 134 GLU HHH CD  
9957  O OE1 . GLU H 134 ? 4.255 4.062 2.860 -1.071 0.260  -0.127 134 GLU HHH OE1 
9958  O OE2 . GLU H 134 ? 4.263 3.930 2.861 -0.988 0.260  -0.093 134 GLU HHH OE2 
9959  N N   . GLY H 135 ? 3.203 2.875 1.916 -0.917 0.243  -0.095 135 GLY HHH N   
9960  C CA  . GLY H 135 ? 2.989 2.791 1.846 -0.878 0.238  -0.096 135 GLY HHH CA  
9961  C C   . GLY H 135 ? 2.850 2.645 1.796 -0.810 0.230  -0.085 135 GLY HHH C   
9962  O O   . GLY H 135 ? 2.727 2.616 1.774 -0.787 0.224  -0.092 135 GLY HHH O   
9963  N N   . MET H 136 ? 2.829 2.516 1.737 -0.775 0.230  -0.071 136 MET HHH N   
9964  C CA  . MET H 136 ? 2.603 2.303 1.607 -0.711 0.223  -0.062 136 MET HHH CA  
9965  C C   . MET H 136 ? 2.529 2.317 1.643 -0.677 0.226  -0.052 136 MET HHH C   
9966  O O   . MET H 136 ? 2.564 2.406 1.778 -0.640 0.220  -0.051 136 MET HHH O   
9967  C CB  . MET H 136 ? 2.598 2.182 1.542 -0.676 0.223  -0.049 136 MET HHH CB  
9968  C CG  . MET H 136 ? 2.613 2.152 1.547 -0.656 0.213  -0.055 136 MET HHH CG  
9969  S SD  . MET H 136 ? 2.392 2.031 1.480 -0.612 0.204  -0.059 136 MET HHH SD  
9970  C CE  . MET H 136 ? 2.594 2.245 1.757 -0.556 0.209  -0.039 136 MET HHH CE  
9971  N N   . ASN H 137 ? 2.532 2.330 1.623 -0.690 0.234  -0.046 137 ASN HHH N   
9972  C CA  . ASN H 137 ? 2.495 2.372 1.676 -0.661 0.237  -0.037 137 ASN HHH CA  
9973  C C   . ASN H 137 ? 2.372 2.364 1.628 -0.668 0.232  -0.051 137 ASN HHH C   
9974  O O   . ASN H 137 ? 2.275 2.328 1.623 -0.630 0.231  -0.045 137 ASN HHH O   
9975  C CB  . ASN H 137 ? 2.596 2.456 1.723 -0.676 0.246  -0.028 137 ASN HHH CB  
9976  C CG  . ASN H 137 ? 2.740 2.476 1.759 -0.682 0.250  -0.020 137 ASN HHH CG  
9977  O OD1 . ASN H 137 ? 2.991 2.680 1.907 -0.730 0.253  -0.028 137 ASN HHH OD1 
9978  N ND2 . ASN H 137 ? 2.692 2.374 1.730 -0.633 0.249  -0.005 137 ASN HHH ND2 
9979  N N   . ILE H 138 ? 2.332 2.355 1.546 -0.716 0.229  -0.071 138 ILE HHH N   
9980  C CA  . ILE H 138 ? 2.281 2.418 1.558 -0.722 0.223  -0.088 138 ILE HHH CA  
9981  C C   . ILE H 138 ? 2.304 2.450 1.652 -0.687 0.213  -0.091 138 ILE HHH C   
9982  O O   . ILE H 138 ? 2.217 2.441 1.649 -0.658 0.208  -0.096 138 ILE HHH O   
9983  C CB  . ILE H 138 ? 2.304 2.475 1.507 -0.788 0.224  -0.109 138 ILE HHH CB  
9984  C CG1 . ILE H 138 ? 2.481 2.651 1.616 -0.825 0.234  -0.108 138 ILE HHH CG1 
9985  C CG2 . ILE H 138 ? 2.221 2.520 1.487 -0.791 0.217  -0.130 138 ILE HHH CG2 
9986  C CD1 . ILE H 138 ? 2.599 2.780 1.641 -0.901 0.238  -0.128 138 ILE HHH CD1 
9987  N N   . VAL H 139 ? 2.329 2.391 1.639 -0.687 0.211  -0.089 139 VAL HHH N   
9988  C CA  . VAL H 139 ? 2.224 2.286 1.601 -0.652 0.201  -0.091 139 VAL HHH CA  
9989  C C   . VAL H 139 ? 2.211 2.284 1.676 -0.598 0.201  -0.076 139 VAL HHH C   
9990  O O   . VAL H 139 ? 2.213 2.333 1.759 -0.571 0.194  -0.080 139 VAL HHH O   
9991  C CB  . VAL H 139 ? 2.223 2.187 1.531 -0.658 0.199  -0.091 139 VAL HHH CB  
9992  C CG1 . VAL H 139 ? 2.212 2.176 1.590 -0.618 0.189  -0.093 139 VAL HHH CG1 
9993  C CG2 . VAL H 139 ? 2.388 2.338 1.605 -0.715 0.199  -0.107 139 VAL HHH CG2 
9994  N N   . GLU H 140 ? 2.139 2.165 1.586 -0.584 0.210  -0.057 140 GLU HHH N   
9995  C CA  . GLU H 140 ? 2.110 2.146 1.634 -0.539 0.213  -0.040 140 GLU HHH CA  
9996  C C   . GLU H 140 ? 2.061 2.181 1.652 -0.526 0.212  -0.042 140 GLU HHH C   
9997  O O   . GLU H 140 ? 2.125 2.265 1.792 -0.493 0.210  -0.037 140 GLU HHH O   
9998  C CB  . GLU H 140 ? 2.232 2.208 1.715 -0.528 0.223  -0.021 140 GLU HHH CB  
9999  C CG  . GLU H 140 ? 2.248 2.244 1.804 -0.490 0.229  -0.003 140 GLU HHH CG  
10000 C CD  . GLU H 140 ? 2.234 2.190 1.823 -0.457 0.229  0.008  140 GLU HHH CD  
10001 O OE1 . GLU H 140 ? 2.631 2.528 2.165 -0.458 0.227  0.006  140 GLU HHH OE1 
10002 O OE2 . GLU H 140 ? 1.854 1.838 1.518 -0.430 0.232  0.018  140 GLU HHH OE2 
10003 N N   . ALA H 141 ? 1.999 2.169 1.558 -0.553 0.214  -0.051 141 ALA HHH N   
10004 C CA  . ALA H 141 ? 1.991 2.247 1.606 -0.536 0.212  -0.055 141 ALA HHH CA  
10005 C C   . ALA H 141 ? 2.059 2.364 1.728 -0.524 0.200  -0.071 141 ALA HHH C   
10006 O O   . ALA H 141 ? 2.120 2.461 1.850 -0.489 0.196  -0.070 141 ALA HHH O   
10007 C CB  . ALA H 141 ? 1.911 2.223 1.475 -0.570 0.215  -0.065 141 ALA HHH CB  
10008 N N   . MET H 142 ? 2.040 2.340 1.679 -0.551 0.194  -0.087 142 MET HHH N   
10009 C CA  . MET H 142 ? 1.926 2.271 1.612 -0.540 0.182  -0.104 142 MET HHH CA  
10010 C C   . MET H 142 ? 1.837 2.145 1.590 -0.499 0.177  -0.095 142 MET HHH C   
10011 O O   . MET H 142 ? 1.791 2.140 1.600 -0.474 0.169  -0.103 142 MET HHH O   
10012 C CB  . MET H 142 ? 1.944 2.279 1.579 -0.578 0.178  -0.121 142 MET HHH CB  
10013 C CG  . MET H 142 ? 2.147 2.536 1.722 -0.626 0.180  -0.137 142 MET HHH CG  
10014 S SD  . MET H 142 ? 2.278 2.614 1.772 -0.675 0.179  -0.149 142 MET HHH SD  
10015 C CE  . MET H 142 ? 1.911 2.274 1.474 -0.646 0.165  -0.162 142 MET HHH CE  
10016 N N   . GLU H 143 ? 1.910 2.143 1.656 -0.492 0.183  -0.079 143 GLU HHH N   
10017 C CA  . GLU H 143 ? 2.007 2.213 1.814 -0.461 0.178  -0.074 143 GLU HHH CA  
10018 C C   . GLU H 143 ? 1.981 2.215 1.856 -0.428 0.178  -0.067 143 GLU HHH C   
10019 O O   . GLU H 143 ? 2.103 2.335 2.029 -0.409 0.171  -0.071 143 GLU HHH O   
10020 C CB  . GLU H 143 ? 2.041 2.176 1.827 -0.456 0.185  -0.059 143 GLU HHH CB  
10021 C CG  . GLU H 143 ? 2.226 2.338 2.021 -0.439 0.197  -0.037 143 GLU HHH CG  
10022 C CD  . GLU H 143 ? 2.334 2.383 2.099 -0.433 0.201  -0.027 143 GLU HHH CD  
10023 O OE1 . GLU H 143 ? 2.118 2.140 1.857 -0.439 0.194  -0.037 143 GLU HHH OE1 
10024 O OE2 . GLU H 143 ? 2.498 2.527 2.264 -0.419 0.212  -0.008 143 GLU HHH OE2 
10025 N N   . ARG H 144 ? 1.736 1.989 1.606 -0.421 0.186  -0.056 144 ARG HHH N   
10026 C CA  . ARG H 144 ? 1.840 2.100 1.762 -0.387 0.187  -0.046 144 ARG HHH CA  
10027 C C   . ARG H 144 ? 1.783 2.096 1.731 -0.372 0.174  -0.064 144 ARG HHH C   
10028 O O   . ARG H 144 ? 1.825 2.133 1.811 -0.343 0.172  -0.059 144 ARG HHH O   
10029 C CB  . ARG H 144 ? 1.907 2.172 1.815 -0.379 0.198  -0.029 144 ARG HHH CB  
10030 C CG  . ARG H 144 ? 2.087 2.331 2.035 -0.347 0.203  -0.011 144 ARG HHH CG  
10031 C CD  . ARG H 144 ? 2.211 2.400 2.196 -0.340 0.208  0.002  144 ARG HHH CD  
10032 N NE  . ARG H 144 ? 2.239 2.396 2.196 -0.353 0.219  0.017  144 ARG HHH NE  
10033 C CZ  . ARG H 144 ? 2.354 2.476 2.322 -0.355 0.222  0.022  144 ARG HHH CZ  
10034 N NH1 . ARG H 144 ? 2.354 2.471 2.365 -0.352 0.214  0.013  144 ARG HHH NH1 
10035 N NH2 . ARG H 144 ? 2.333 2.428 2.268 -0.360 0.232  0.034  144 ARG HHH NH2 
10036 N N   . PHE H 145 ? 1.758 2.120 1.681 -0.392 0.166  -0.085 145 PHE HHH N   
10037 C CA  . PHE H 145 ? 1.691 2.109 1.638 -0.373 0.153  -0.104 145 PHE HHH CA  
10038 C C   . PHE H 145 ? 1.718 2.116 1.696 -0.371 0.143  -0.116 145 PHE HHH C   
10039 O O   . PHE H 145 ? 1.806 2.241 1.804 -0.353 0.131  -0.133 145 PHE HHH O   
10040 C CB  . PHE H 145 ? 1.665 2.162 1.572 -0.398 0.150  -0.124 145 PHE HHH CB  
10041 C CG  . PHE H 145 ? 1.600 2.135 1.473 -0.404 0.159  -0.118 145 PHE HHH CG  
10042 C CD1 . PHE H 145 ? 1.601 2.177 1.491 -0.368 0.157  -0.117 145 PHE HHH CD1 
10043 C CD2 . PHE H 145 ? 1.646 2.174 1.465 -0.447 0.168  -0.116 145 PHE HHH CD2 
10044 C CE1 . PHE H 145 ? 1.636 2.255 1.495 -0.373 0.164  -0.113 145 PHE HHH CE1 
10045 C CE2 . PHE H 145 ? 1.641 2.206 1.428 -0.456 0.175  -0.113 145 PHE HHH CE2 
10046 C CZ  . PHE H 145 ? 1.655 2.271 1.465 -0.419 0.173  -0.112 145 PHE HHH CZ  
10047 N N   . GLY H 146 ? 1.640 1.979 1.619 -0.384 0.147  -0.107 146 GLY HHH N   
10048 C CA  . GLY H 146 ? 1.491 1.806 1.501 -0.380 0.138  -0.116 146 GLY HHH CA  
10049 C C   . GLY H 146 ? 1.449 1.724 1.510 -0.354 0.139  -0.105 146 GLY HHH C   
10050 O O   . GLY H 146 ? 1.429 1.694 1.499 -0.338 0.147  -0.089 146 GLY HHH O   
10051 N N   . SER H 147 ? 1.637 1.889 1.729 -0.353 0.132  -0.112 147 SER HHH N   
10052 C CA  . SER H 147 ? 1.700 1.916 1.839 -0.336 0.133  -0.104 147 SER HHH CA  
10053 C C   . SER H 147 ? 1.745 1.939 1.908 -0.345 0.129  -0.110 147 SER HHH C   
10054 O O   . SER H 147 ? 1.768 1.971 1.907 -0.358 0.124  -0.122 147 SER HHH O   
10055 C CB  . SER H 147 ? 1.810 2.036 1.972 -0.313 0.123  -0.114 147 SER HHH CB  
10056 O OG  . SER H 147 ? 1.815 2.065 1.985 -0.312 0.107  -0.139 147 SER HHH OG  
10057 N N   . ARG H 148 ? 1.589 1.754 1.793 -0.338 0.133  -0.102 148 ARG HHH N   
10058 C CA  . ARG H 148 ? 1.533 1.687 1.764 -0.345 0.129  -0.109 148 ARG HHH CA  
10059 C C   . ARG H 148 ? 1.613 1.786 1.852 -0.345 0.112  -0.135 148 ARG HHH C   
10060 O O   . ARG H 148 ? 1.628 1.804 1.865 -0.351 0.108  -0.144 148 ARG HHH O   
10061 C CB  . ARG H 148 ? 1.708 1.837 1.984 -0.344 0.136  -0.099 148 ARG HHH CB  
10062 C CG  . ARG H 148 ? 1.939 2.053 2.207 -0.347 0.154  -0.073 148 ARG HHH CG  
10063 C CD  . ARG H 148 ? 2.127 2.223 2.437 -0.352 0.163  -0.064 148 ARG HHH CD  
10064 N NE  . ARG H 148 ? 2.394 2.466 2.724 -0.350 0.160  -0.066 148 ARG HHH NE  
10065 C CZ  . ARG H 148 ? 2.565 2.610 2.880 -0.342 0.167  -0.050 148 ARG HHH CZ  
10066 N NH1 . ARG H 148 ? 2.602 2.649 2.888 -0.336 0.179  -0.032 148 ARG HHH NH1 
10067 N NH2 . ARG H 148 ? 2.529 2.539 2.853 -0.337 0.163  -0.054 148 ARG HHH NH2 
10068 N N   . ASN H 149 ? 1.648 1.835 1.890 -0.334 0.102  -0.147 149 ASN HHH N   
10069 C CA  . ASN H 149 ? 1.491 1.701 1.741 -0.332 0.086  -0.173 149 ASN HHH CA  
10070 C C   . ASN H 149 ? 1.398 1.645 1.603 -0.340 0.081  -0.183 149 ASN HHH C   
10071 O O   . ASN H 149 ? 1.474 1.746 1.680 -0.340 0.068  -0.204 149 ASN HHH O   
10072 C CB  . ASN H 149 ? 1.610 1.819 1.880 -0.313 0.075  -0.183 149 ASN HHH CB  
10073 C CG  . ASN H 149 ? 2.048 2.210 2.341 -0.307 0.082  -0.169 149 ASN HHH CG  
10074 O OD1 . ASN H 149 ? 2.223 2.372 2.503 -0.304 0.095  -0.148 149 ASN HHH OD1 
10075 N ND2 . ASN H 149 ? 2.266 2.403 2.593 -0.306 0.074  -0.179 149 ASN HHH ND2 
10076 N N   . GLY H 150 ? 1.454 1.707 1.619 -0.351 0.093  -0.170 150 GLY HHH N   
10077 C CA  . GLY H 150 ? 1.498 1.781 1.613 -0.369 0.091  -0.179 150 GLY HHH CA  
10078 C C   . GLY H 150 ? 1.518 1.854 1.618 -0.365 0.088  -0.187 150 GLY HHH C   
10079 O O   . GLY H 150 ? 1.432 1.801 1.487 -0.386 0.091  -0.192 150 GLY HHH O   
10080 N N   . LYS H 151 ? 1.514 1.857 1.646 -0.338 0.084  -0.188 151 LYS HHH N   
10081 C CA  . LYS H 151 ? 1.553 1.951 1.671 -0.324 0.079  -0.197 151 LYS HHH CA  
10082 C C   . LYS H 151 ? 1.605 2.018 1.691 -0.332 0.092  -0.181 151 LYS HHH C   
10083 O O   . LYS H 151 ? 1.767 2.136 1.856 -0.332 0.104  -0.159 151 LYS HHH O   
10084 C CB  . LYS H 151 ? 1.594 1.976 1.743 -0.287 0.071  -0.199 151 LYS HHH CB  
10085 C CG  . LYS H 151 ? 1.810 2.228 1.969 -0.267 0.053  -0.225 151 LYS HHH CG  
10086 C CD  . LYS H 151 ? 1.921 2.299 2.098 -0.230 0.047  -0.223 151 LYS HHH CD  
10087 C CE  . LYS H 151 ? 2.093 2.496 2.273 -0.201 0.028  -0.249 151 LYS HHH CE  
10088 N NZ  . LYS H 151 ? 2.184 2.530 2.368 -0.164 0.023  -0.245 151 LYS HHH NZ  
10089 N N   . THR H 152 ? 1.690 2.172 1.743 -0.341 0.090  -0.194 152 THR HHH N   
10090 C CA  . THR H 152 ? 1.700 2.206 1.720 -0.352 0.102  -0.183 152 THR HHH CA  
10091 C C   . THR H 152 ? 1.744 2.284 1.777 -0.312 0.098  -0.184 152 THR HHH C   
10092 O O   . THR H 152 ? 1.885 2.460 1.932 -0.286 0.084  -0.202 152 THR HHH O   
10093 C CB  . THR H 152 ? 1.690 2.256 1.661 -0.390 0.104  -0.196 152 THR HHH CB  
10094 O OG1 . THR H 152 ? 1.802 2.448 1.778 -0.381 0.091  -0.222 152 THR HHH OG1 
10095 C CG2 . THR H 152 ? 1.609 2.126 1.555 -0.425 0.108  -0.194 152 THR HHH CG2 
10096 N N   . SER H 153 ? 1.777 2.303 1.798 -0.305 0.109  -0.165 153 SER HHH N   
10097 C CA  . SER H 153 ? 1.777 2.325 1.802 -0.263 0.105  -0.164 153 SER HHH CA  
10098 C C   . SER H 153 ? 1.979 2.632 1.975 -0.261 0.101  -0.181 153 SER HHH C   
10099 O O   . SER H 153 ? 1.980 2.670 1.975 -0.218 0.093  -0.189 153 SER HHH O   
10100 C CB  . SER H 153 ? 1.765 2.254 1.791 -0.253 0.119  -0.135 153 SER HHH CB  
10101 O OG  . SER H 153 ? 1.707 2.206 1.704 -0.285 0.132  -0.124 153 SER HHH OG  
10102 N N   . LYS H 154 ? 2.029 2.729 1.996 -0.305 0.106  -0.189 154 LYS HHH N   
10103 C CA  . LYS H 154 ? 2.024 2.834 1.962 -0.316 0.104  -0.210 154 LYS HHH CA  
10104 C C   . LYS H 154 ? 2.031 2.873 1.950 -0.364 0.102  -0.227 154 LYS HHH C   
10105 O O   . LYS H 154 ? 2.031 2.800 1.949 -0.390 0.106  -0.218 154 LYS HHH O   
10106 C CB  . LYS H 154 ? 2.067 2.898 1.973 -0.332 0.117  -0.197 154 LYS HHH CB  
10107 C CG  . LYS H 154 ? 2.004 2.782 1.924 -0.291 0.122  -0.174 154 LYS HHH CG  
10108 C CD  . LYS H 154 ? 2.041 2.867 1.969 -0.233 0.111  -0.184 154 LYS HHH CD  
10109 C CE  . LYS H 154 ? 2.078 2.862 2.001 -0.202 0.119  -0.160 154 LYS HHH CE  
10110 N NZ  . LYS H 154 ? 2.082 2.746 2.025 -0.210 0.129  -0.132 154 LYS HHH NZ  
10111 N N   . LYS H 155 ? 1.830 2.782 1.731 -0.375 0.097  -0.252 155 LYS HHH N   
10112 C CA  . LYS H 155 ? 1.837 2.819 1.714 -0.423 0.096  -0.268 155 LYS HHH CA  
10113 C C   . LYS H 155 ? 1.843 2.811 1.667 -0.483 0.111  -0.259 155 LYS HHH C   
10114 O O   . LYS H 155 ? 1.931 2.966 1.728 -0.499 0.117  -0.263 155 LYS HHH O   
10115 C CB  . LYS H 155 ? 1.814 2.927 1.690 -0.415 0.085  -0.299 155 LYS HHH CB  
10120 N N   . ILE H 156 ? 1.825 2.702 1.629 -0.516 0.117  -0.248 156 ILE HHH N   
10121 C CA  . ILE H 156 ? 1.835 2.671 1.577 -0.571 0.131  -0.239 156 ILE HHH CA  
10122 C C   . ILE H 156 ? 1.922 2.798 1.619 -0.623 0.130  -0.259 156 ILE HHH C   
10123 O O   . ILE H 156 ? 2.034 2.869 1.734 -0.626 0.125  -0.263 156 ILE HHH O   
10124 C CB  . ILE H 156 ? 1.746 2.452 1.486 -0.567 0.137  -0.213 156 ILE HHH CB  
10125 C CG1 . ILE H 156 ? 1.719 2.389 1.520 -0.511 0.135  -0.197 156 ILE HHH CG1 
10126 C CG2 . ILE H 156 ? 1.740 2.398 1.414 -0.609 0.151  -0.200 156 ILE HHH CG2 
10127 C CD1 . ILE H 156 ? 1.641 2.350 1.443 -0.494 0.140  -0.189 156 ILE HHH CD1 
10128 N N   . THR H 157 ? 1.948 2.907 1.599 -0.667 0.137  -0.272 157 THR HHH N   
10129 C CA  . THR H 157 ? 2.014 3.034 1.621 -0.720 0.137  -0.295 157 THR HHH CA  
10130 C C   . THR H 157 ? 2.082 3.062 1.600 -0.793 0.152  -0.291 157 THR HHH C   
10131 O O   . THR H 157 ? 2.088 3.060 1.583 -0.804 0.161  -0.280 157 THR HHH O   
10132 C CB  . THR H 157 ? 2.062 3.244 1.695 -0.708 0.130  -0.322 157 THR HHH CB  
10133 O OG1 . THR H 157 ? 2.013 3.215 1.718 -0.635 0.115  -0.326 157 THR HHH OG1 
10134 C CG2 . THR H 157 ? 2.282 3.539 1.874 -0.764 0.131  -0.346 157 THR HHH CG2 
10135 N N   . ILE H 158 ? 2.153 3.102 1.616 -0.842 0.155  -0.298 158 ILE HHH N   
10136 C CA  . ILE H 158 ? 2.262 3.170 1.624 -0.920 0.169  -0.298 158 ILE HHH CA  
10137 C C   . ILE H 158 ? 2.369 3.426 1.709 -0.970 0.172  -0.325 158 ILE HHH C   
10138 O O   . ILE H 158 ? 2.476 3.594 1.809 -0.991 0.169  -0.345 158 ILE HHH O   
10139 C CB  . ILE H 158 ? 2.237 3.025 1.540 -0.947 0.171  -0.291 158 ILE HHH CB  
10140 C CG1 . ILE H 158 ? 2.207 2.895 1.563 -0.882 0.162  -0.273 158 ILE HHH CG1 
10141 C CG2 . ILE H 158 ? 2.405 3.098 1.594 -1.013 0.185  -0.282 158 ILE HHH CG2 
10142 C CD1 . ILE H 158 ? 2.332 2.926 1.646 -0.893 0.160  -0.271 158 ILE HHH CD1 
10143 N N   . ALA H 159 ? 2.345 3.468 1.672 -0.987 0.179  -0.328 159 ALA HHH N   
10144 C CA  . ALA H 159 ? 2.331 3.616 1.643 -1.031 0.182  -0.357 159 ALA HHH CA  
10145 C C   . ALA H 159 ? 2.582 3.851 1.792 -1.129 0.194  -0.367 159 ALA HHH C   
10146 O O   . ALA H 159 ? 2.830 4.225 2.029 -1.170 0.195  -0.393 159 ALA HHH O   
10147 C CB  . ALA H 159 ? 2.310 3.671 1.637 -1.021 0.185  -0.358 159 ALA HHH CB  
10148 N N   . ASP H 160 ? 2.835 3.949 1.964 -1.168 0.205  -0.347 160 ASP HHH N   
10149 C CA  . ASP H 160 ? 3.053 4.116 2.067 -1.261 0.217  -0.354 160 ASP HHH CA  
10150 C C   . ASP H 160 ? 3.085 3.939 2.030 -1.263 0.221  -0.327 160 ASP HHH C   
10151 O O   . ASP H 160 ? 2.957 3.720 1.933 -1.206 0.217  -0.305 160 ASP HHH O   
10152 C CB  . ASP H 160 ? 3.256 4.398 2.208 -1.337 0.230  -0.368 160 ASP HHH CB  
10153 C CG  . ASP H 160 ? 3.500 4.589 2.449 -1.317 0.233  -0.351 160 ASP HHH CG  
10154 O OD1 . ASP H 160 ? 3.688 4.845 2.730 -1.245 0.225  -0.347 160 ASP HHH OD1 
10155 O OD2 . ASP H 160 ? 3.716 4.690 2.565 -1.373 0.245  -0.340 160 ASP HHH OD2 
10156 N N   . CYS H 161 ? 3.244 4.027 2.090 -1.329 0.229  -0.331 161 CYS HHH N   
10157 C CA  . CYS H 161 ? 3.331 3.915 2.085 -1.339 0.233  -0.310 161 CYS HHH CA  
10158 C C   . CYS H 161 ? 3.521 4.059 2.140 -1.439 0.246  -0.321 161 CYS HHH C   
10159 O O   . CYS H 161 ? 3.636 4.302 2.248 -1.493 0.250  -0.344 161 CYS HHH O   
10160 C CB  . CYS H 161 ? 3.301 3.818 2.111 -1.268 0.220  -0.300 161 CYS HHH CB  
10161 S SG  . CYS H 161 ? 3.586 4.231 2.463 -1.258 0.210  -0.323 161 CYS HHH SG  
10162 N N   . GLY H 162 ? 3.579 3.931 2.082 -1.463 0.252  -0.303 162 GLY HHH N   
10163 C CA  . GLY H 162 ? 3.803 4.084 2.159 -1.560 0.266  -0.310 162 GLY HHH CA  
10164 C C   . GLY H 162 ? 3.953 4.011 2.174 -1.573 0.271  -0.289 162 GLY HHH C   
10165 O O   . GLY H 162 ? 3.836 3.793 2.084 -1.499 0.263  -0.268 162 GLY HHH O   
10166 N N   . GLN H 163 ? 4.182 4.166 2.254 -1.670 0.285  -0.295 163 GLN HHH N   
10167 C CA  . GLN H 163 ? 4.483 4.244 2.393 -1.697 0.292  -0.278 163 GLN HHH CA  
10168 C C   . GLN H 163 ? 4.675 4.405 2.508 -1.754 0.303  -0.278 163 GLN HHH C   
10169 O O   . GLN H 163 ? 4.768 4.619 2.589 -1.832 0.313  -0.298 163 GLN HHH O   
10170 C CB  . GLN H 163 ? 4.590 4.271 2.367 -1.773 0.301  -0.285 163 GLN HHH CB  
10171 C CG  . GLN H 163 ? 4.788 4.220 2.374 -1.803 0.307  -0.269 163 GLN HHH CG  
10172 C CD  . GLN H 163 ? 4.786 4.073 2.381 -1.700 0.294  -0.246 163 GLN HHH CD  
10173 O OE1 . GLN H 163 ? 4.885 4.010 2.381 -1.689 0.295  -0.230 163 GLN HHH OE1 
10174 N NE2 . GLN H 163 ? 4.654 4.000 2.365 -1.624 0.281  -0.245 163 GLN HHH NE2 
10175 N N   . LEU H 164 ? 4.836 4.413 2.622 -1.709 0.300  -0.257 164 LEU HHH N   
10176 C CA  . LEU H 164 ? 5.169 4.663 2.856 -1.752 0.309  -0.252 164 LEU HHH CA  
10177 C C   . LEU H 164 ? 5.484 5.031 3.075 -1.877 0.325  -0.273 164 LEU HHH C   
10178 O O   . LEU H 164 ? 5.792 5.243 3.243 -1.953 0.335  -0.278 164 LEU HHH O   
10179 C CB  . LEU H 164 ? 5.310 4.555 2.854 -1.731 0.309  -0.230 164 LEU HHH CB  
10180 C CG  . LEU H 164 ? 5.561 4.686 2.967 -1.785 0.319  -0.226 164 LEU HHH CG  
10181 C CD1 . LEU H 164 ? 5.373 4.574 2.885 -1.729 0.314  -0.219 164 LEU HHH CD1 
10182 C CD2 . LEU H 164 ? 5.761 4.628 2.991 -1.777 0.319  -0.209 164 LEU HHH CD2 
10183 N N   . GLU H 165 ? 5.605 5.307 3.267 -1.898 0.329  -0.286 165 GLU HHH N   
10184 C CA  . GLU H 165 ? 5.783 5.564 3.368 -2.016 0.343  -0.309 165 GLU HHH CA  
10185 C C   . GLU H 165 ? 6.008 5.645 3.452 -2.069 0.353  -0.303 165 GLU HHH C   
10186 O O   . GLU H 165 ? 6.114 5.817 3.498 -2.164 0.365  -0.322 165 GLU HHH O   
10187 C CB  . GLU H 165 ? 5.641 5.687 3.381 -2.009 0.341  -0.331 165 GLU HHH CB  
10188 C CG  . GLU H 165 ? 5.481 5.591 3.364 -1.902 0.328  -0.319 165 GLU HHH CG  
10189 C CD  . GLU H 165 ? 5.573 5.607 3.398 -1.913 0.333  -0.310 165 GLU HHH CD  
10190 O OE1 . GLU H 165 ? 5.715 5.761 3.441 -2.011 0.345  -0.326 165 GLU HHH OE1 
10191 O OE2 . GLU H 165 ? 5.520 5.483 3.395 -1.825 0.324  -0.288 165 GLU HHH OE2 
10192 O OXT . GLU H 165 ? 6.183 5.637 3.568 -2.017 0.348  -0.280 165 GLU HHH OXT 
10193 N N   . MET I 1   ? 3.689 6.871 3.210 -0.352 -0.071 -0.331 1   MET III N   
10194 C CA  . MET I 1   ? 3.751 7.084 3.276 -0.377 -0.069 -0.334 1   MET III CA  
10195 C C   . MET I 1   ? 3.800 7.187 3.383 -0.284 -0.076 -0.327 1   MET III C   
10196 O O   . MET I 1   ? 3.703 7.220 3.297 -0.289 -0.077 -0.326 1   MET III O   
10197 C CB  . MET I 1   ? 3.713 7.244 3.229 -0.423 -0.063 -0.340 1   MET III CB  
10198 C CG  . MET I 1   ? 3.713 7.368 3.202 -0.503 -0.059 -0.343 1   MET III CG  
10199 S SD  . MET I 1   ? 3.702 7.645 3.212 -0.522 -0.056 -0.347 1   MET III SD  
10200 C CE  . MET I 1   ? 3.586 7.483 3.047 -0.585 -0.046 -0.355 1   MET III CE  
10201 N N   . VAL I 2   ? 4.062 7.344 3.676 -0.201 -0.082 -0.321 2   VAL III N   
10202 C CA  . VAL I 2   ? 3.979 7.293 3.639 -0.106 -0.088 -0.315 2   VAL III CA  
10203 C C   . VAL I 2   ? 3.896 7.022 3.561 -0.077 -0.092 -0.310 2   VAL III C   
10204 O O   . VAL I 2   ? 4.150 7.126 3.802 -0.085 -0.093 -0.309 2   VAL III O   
10205 C CB  . VAL I 2   ? 3.970 7.350 3.657 -0.027 -0.089 -0.313 2   VAL III CB  
10206 C CG1 . VAL I 2   ? 4.016 7.261 3.687 -0.028 -0.090 -0.314 2   VAL III CG1 
10207 C CG2 . VAL I 2   ? 3.833 7.213 3.554 0.073  -0.095 -0.306 2   VAL III CG2 
10208 N N   . ASN I 3   ? 3.480 6.618 3.162 -0.044 -0.094 -0.307 3   ASN III N   
10209 C CA  . ASN I 3   ? 3.048 6.025 2.739 -0.011 -0.097 -0.302 3   ASN III CA  
10210 C C   . ASN I 3   ? 2.940 5.961 2.662 0.075  -0.102 -0.297 3   ASN III C   
10211 O O   . ASN I 3   ? 2.832 5.897 2.555 0.073  -0.102 -0.296 3   ASN III O   
10212 C CB  . ASN I 3   ? 2.709 5.613 2.369 -0.084 -0.090 -0.305 3   ASN III CB  
10213 C CG  . ASN I 3   ? 2.701 5.482 2.324 -0.150 -0.084 -0.308 3   ASN III CG  
10214 O OD1 . ASN I 3   ? 2.923 5.643 2.551 -0.134 -0.087 -0.306 3   ASN III OD1 
10215 N ND2 . ASN I 3   ? 2.583 5.323 2.164 -0.225 -0.075 -0.312 3   ASN III ND2 
10216 N N   . PRO I 4   ? 2.839 5.845 2.580 0.152  -0.107 -0.293 4   PRO III N   
10217 C CA  . PRO I 4   ? 2.807 5.849 2.567 0.238  -0.111 -0.288 4   PRO III CA  
10218 C C   . PRO I 4   ? 2.952 5.845 2.716 0.263  -0.113 -0.284 4   PRO III C   
10219 O O   . PRO I 4   ? 2.988 5.747 2.746 0.222  -0.110 -0.285 4   PRO III O   
10220 C CB  . PRO I 4   ? 2.739 5.788 2.504 0.303  -0.112 -0.286 4   PRO III CB  
10221 C CG  . PRO I 4   ? 2.817 5.761 2.572 0.259  -0.112 -0.289 4   PRO III CG  
10222 C CD  . PRO I 4   ? 2.909 5.862 2.647 0.161  -0.107 -0.294 4   PRO III CD  
10223 N N   . THR I 5   ? 3.106 6.024 2.877 0.332  -0.116 -0.279 5   THR III N   
10224 C CA  . THR I 5   ? 3.061 5.854 2.834 0.360  -0.117 -0.276 5   THR III CA  
10225 C C   . THR I 5   ? 2.952 5.691 2.725 0.451  -0.121 -0.271 5   THR III C   
10226 O O   . THR I 5   ? 3.084 5.919 2.853 0.506  -0.123 -0.269 5   THR III O   
10227 C CB  . THR I 5   ? 3.191 6.049 2.960 0.347  -0.117 -0.275 5   THR III CB  
10228 O OG1 . THR I 5   ? 3.464 6.503 3.235 0.371  -0.121 -0.273 5   THR III OG1 
10229 C CG2 . THR I 5   ? 3.197 6.030 2.954 0.254  -0.110 -0.280 5   THR III CG2 
10230 N N   . VAL I 6   ? 2.724 5.307 2.497 0.465  -0.121 -0.269 6   VAL III N   
10231 C CA  . VAL I 6   ? 2.612 5.117 2.374 0.541  -0.124 -0.265 6   VAL III CA  
10232 C C   . VAL I 6   ? 2.581 4.986 2.340 0.556  -0.123 -0.262 6   VAL III C   
10233 O O   . VAL I 6   ? 2.398 4.742 2.169 0.503  -0.119 -0.264 6   VAL III O   
10234 C CB  . VAL I 6   ? 2.533 4.940 2.295 0.540  -0.127 -0.265 6   VAL III CB  
10235 C CG1 . VAL I 6   ? 2.644 4.929 2.391 0.599  -0.129 -0.261 6   VAL III CG1 
10236 C CG2 . VAL I 6   ? 2.675 5.182 2.432 0.545  -0.127 -0.267 6   VAL III CG2 
10237 N N   . PHE I 7   ? 2.573 4.958 2.312 0.628  -0.125 -0.258 7   PHE III N   
10238 C CA  . PHE I 7   ? 2.499 4.799 2.228 0.647  -0.124 -0.256 7   PHE III CA  
10239 C C   . PHE I 7   ? 2.476 4.643 2.183 0.697  -0.125 -0.253 7   PHE III C   
10240 O O   . PHE I 7   ? 2.594 4.766 2.279 0.745  -0.127 -0.251 7   PHE III O   
10241 C CB  . PHE I 7   ? 2.776 5.181 2.489 0.682  -0.125 -0.253 7   PHE III CB  
10242 C CG  . PHE I 7   ? 3.101 5.579 2.788 0.762  -0.129 -0.248 7   PHE III CG  
10243 C CD1 . PHE I 7   ? 3.176 5.564 2.826 0.832  -0.129 -0.244 7   PHE III CD1 
10244 C CD2 . PHE I 7   ? 3.348 5.986 3.045 0.766  -0.130 -0.248 7   PHE III CD2 
10245 C CE1 . PHE I 7   ? 3.410 5.857 3.028 0.910  -0.130 -0.239 7   PHE III CE1 
10246 C CE2 . PHE I 7   ? 3.537 6.247 3.212 0.844  -0.131 -0.243 7   PHE III CE2 
10247 C CZ  . PHE I 7   ? 3.591 6.201 3.224 0.919  -0.130 -0.238 7   PHE III CZ  
10248 N N   . PHE I 8   ? 2.336 4.385 2.045 0.683  -0.122 -0.252 8   PHE III N   
10249 C CA  . PHE I 8   ? 2.384 4.301 2.070 0.719  -0.123 -0.250 8   PHE III CA  
10250 C C   . PHE I 8   ? 2.188 4.056 1.851 0.744  -0.119 -0.248 8   PHE III C   
10251 O O   . PHE I 8   ? 2.163 4.030 1.845 0.704  -0.113 -0.250 8   PHE III O   
10252 C CB  . PHE I 8   ? 2.411 4.218 2.125 0.674  -0.122 -0.250 8   PHE III CB  
10253 C CG  . PHE I 8   ? 2.371 4.185 2.096 0.659  -0.128 -0.250 8   PHE III CG  
10254 C CD1 . PHE I 8   ? 2.890 4.796 2.600 0.684  -0.131 -0.251 8   PHE III CD1 
10255 C CD2 . PHE I 8   ? 2.070 3.794 1.821 0.622  -0.131 -0.247 8   PHE III CD2 
10256 C CE1 . PHE I 8   ? 3.226 5.131 2.942 0.668  -0.136 -0.251 8   PHE III CE1 
10257 C CE2 . PHE I 8   ? 2.197 3.920 1.954 0.608  -0.138 -0.246 8   PHE III CE2 
10258 C CZ  . PHE I 8   ? 2.714 4.523 2.451 0.629  -0.140 -0.249 8   PHE III CZ  
10259 N N   . ASP I 9   ? 2.233 4.054 1.848 0.808  -0.120 -0.245 9   ASP III N   
10260 C CA  . ASP I 9   ? 2.241 3.979 1.824 0.830  -0.116 -0.243 9   ASP III CA  
10261 C C   . ASP I 9   ? 2.148 3.736 1.722 0.821  -0.114 -0.243 9   ASP III C   
10262 O O   . ASP I 9   ? 2.181 3.714 1.725 0.850  -0.118 -0.242 9   ASP III O   
10263 C CB  . ASP I 9   ? 2.427 4.194 1.951 0.908  -0.118 -0.239 9   ASP III CB  
10264 C CG  . ASP I 9   ? 2.327 4.237 1.858 0.917  -0.121 -0.237 9   ASP III CG  
10265 O OD1 . ASP I 9   ? 2.343 4.374 1.909 0.894  -0.124 -0.238 9   ASP III OD1 
10266 O OD2 . ASP I 9   ? 2.327 4.229 1.826 0.945  -0.121 -0.233 9   ASP III OD2 
10267 N N   . ILE I 10  ? 2.015 3.539 1.612 0.780  -0.107 -0.245 10  ILE III N   
10268 C CA  . ILE I 10  ? 1.923 3.323 1.528 0.758  -0.105 -0.244 10  ILE III CA  
10269 C C   . ILE I 10  ? 1.944 3.252 1.495 0.790  -0.100 -0.243 10  ILE III C   
10270 O O   . ILE I 10  ? 2.198 3.526 1.730 0.802  -0.095 -0.244 10  ILE III O   
10271 C CB  . ILE I 10  ? 1.812 3.202 1.479 0.692  -0.098 -0.246 10  ILE III CB  
10272 C CG1 . ILE I 10  ? 1.846 3.321 1.554 0.660  -0.102 -0.247 10  ILE III CG1 
10273 C CG2 . ILE I 10  ? 1.784 3.062 1.466 0.672  -0.096 -0.243 10  ILE III CG2 
10274 C CD1 . ILE I 10  ? 2.023 3.481 1.734 0.666  -0.112 -0.244 10  ILE III CD1 
10275 N N   . ALA I 11  ? 1.915 3.117 1.435 0.800  -0.101 -0.241 11  ALA III N   
10276 C CA  . ALA I 11  ? 1.985 3.083 1.448 0.821  -0.096 -0.241 11  ALA III CA  
10277 C C   . ALA I 11  ? 1.982 2.983 1.469 0.777  -0.092 -0.240 11  ALA III C   
10278 O O   . ALA I 11  ? 1.898 2.895 1.427 0.748  -0.098 -0.239 11  ALA III O   
10279 C CB  . ALA I 11  ? 2.263 3.317 1.640 0.885  -0.100 -0.239 11  ALA III CB  
10280 N N   . VAL I 12  ? 2.166 3.092 1.628 0.773  -0.082 -0.241 12  VAL III N   
10281 C CA  . VAL I 12  ? 2.300 3.140 1.784 0.732  -0.077 -0.241 12  VAL III CA  
10282 C C   . VAL I 12  ? 2.622 3.348 2.017 0.756  -0.074 -0.241 12  VAL III C   
10283 O O   . VAL I 12  ? 2.906 3.602 2.251 0.778  -0.067 -0.242 12  VAL III O   
10284 C CB  . VAL I 12  ? 2.097 2.950 1.637 0.690  -0.063 -0.243 12  VAL III CB  
10285 C CG1 . VAL I 12  ? 2.126 2.897 1.688 0.653  -0.055 -0.242 12  VAL III CG1 
10286 C CG2 . VAL I 12  ? 1.935 2.884 1.548 0.663  -0.063 -0.244 12  VAL III CG2 
10287 N N   . ASP I 13  ? 2.804 3.464 2.177 0.749  -0.081 -0.238 13  ASP III N   
10288 C CA  . ASP I 13  ? 2.953 3.496 2.228 0.770  -0.080 -0.238 13  ASP III CA  
10289 C C   . ASP I 13  ? 3.114 3.648 2.298 0.837  -0.080 -0.239 13  ASP III C   
10290 O O   . ASP I 13  ? 3.335 3.779 2.437 0.857  -0.073 -0.240 13  ASP III O   
10291 C CB  . ASP I 13  ? 2.924 3.390 2.197 0.733  -0.068 -0.239 13  ASP III CB  
10292 C CG  . ASP I 13  ? 2.881 3.324 2.211 0.677  -0.071 -0.236 13  ASP III CG  
10293 O OD1 . ASP I 13  ? 2.856 3.367 2.259 0.659  -0.080 -0.232 13  ASP III OD1 
10294 O OD2 . ASP I 13  ? 2.955 3.312 2.254 0.651  -0.065 -0.235 13  ASP III OD2 
10295 N N   . GLY I 14  ? 2.952 3.579 2.148 0.872  -0.086 -0.238 14  GLY III N   
10296 C CA  . GLY I 14  ? 2.933 3.574 2.054 0.941  -0.086 -0.237 14  GLY III CA  
10297 C C   . GLY I 14  ? 3.000 3.706 2.134 0.955  -0.082 -0.237 14  GLY III C   
10298 O O   . GLY I 14  ? 3.155 3.889 2.232 1.015  -0.083 -0.235 14  GLY III O   
10299 N N   . GLU I 15  ? 2.840 3.572 2.044 0.902  -0.076 -0.240 15  GLU III N   
10300 C CA  . GLU I 15  ? 2.661 3.454 1.877 0.908  -0.071 -0.240 15  GLU III CA  
10301 C C   . GLU I 15  ? 2.482 3.416 1.778 0.890  -0.076 -0.241 15  GLU III C   
10302 O O   . GLU I 15  ? 2.507 3.467 1.878 0.841  -0.076 -0.243 15  GLU III O   
10303 C CB  . GLU I 15  ? 2.669 3.396 1.901 0.861  -0.058 -0.244 15  GLU III CB  
10304 C CG  . GLU I 15  ? 2.841 3.427 2.009 0.856  -0.053 -0.244 15  GLU III CG  
10305 C CD  . GLU I 15  ? 2.918 3.449 2.101 0.811  -0.038 -0.248 15  GLU III CD  
10306 O OE1 . GLU I 15  ? 2.937 3.525 2.157 0.797  -0.031 -0.250 15  GLU III OE1 
10307 O OE2 . GLU I 15  ? 3.035 3.462 2.185 0.790  -0.032 -0.249 15  GLU III OE2 
10308 N N   . PRO I 16  ? 2.400 3.427 1.683 0.927  -0.080 -0.239 16  PRO III N   
10309 C CA  . PRO I 16  ? 2.305 3.470 1.658 0.904  -0.085 -0.239 16  PRO III CA  
10310 C C   . PRO I 16  ? 2.237 3.414 1.654 0.838  -0.076 -0.244 16  PRO III C   
10311 O O   . PRO I 16  ? 2.367 3.486 1.767 0.824  -0.066 -0.245 16  PRO III O   
10312 C CB  . PRO I 16  ? 2.457 3.711 1.771 0.958  -0.091 -0.235 16  PRO III CB  
10313 C CG  . PRO I 16  ? 2.649 3.804 1.883 0.995  -0.087 -0.232 16  PRO III CG  
10314 C CD  . PRO I 16  ? 2.550 3.562 1.749 0.990  -0.082 -0.234 16  PRO III CD  
10315 N N   . LEU I 17  ? 2.089 3.336 1.574 0.797  -0.077 -0.246 17  LEU III N   
10316 C CA  . LEU I 17  ? 1.998 3.253 1.543 0.735  -0.067 -0.250 17  LEU III CA  
10317 C C   . LEU I 17  ? 1.967 3.345 1.538 0.716  -0.069 -0.251 17  LEU III C   
10318 O O   . LEU I 17  ? 2.041 3.434 1.616 0.688  -0.061 -0.253 17  LEU III O   
10319 C CB  . LEU I 17  ? 1.936 3.150 1.534 0.697  -0.065 -0.250 17  LEU III CB  
10320 C CG  . LEU I 17  ? 1.826 3.041 1.484 0.637  -0.053 -0.253 17  LEU III CG  
10321 C CD1 . LEU I 17  ? 1.786 2.925 1.434 0.622  -0.037 -0.255 17  LEU III CD1 
10322 C CD2 . LEU I 17  ? 1.818 3.009 1.527 0.609  -0.055 -0.250 17  LEU III CD2 
10323 N N   . GLY I 18  ? 1.933 3.400 1.518 0.726  -0.080 -0.249 18  GLY III N   
10324 C CA  . GLY I 18  ? 1.928 3.521 1.534 0.705  -0.083 -0.250 18  GLY III CA  
10325 C C   . GLY I 18  ? 1.930 3.602 1.558 0.708  -0.092 -0.250 18  GLY III C   
10326 O O   . GLY I 18  ? 1.925 3.548 1.554 0.724  -0.096 -0.249 18  GLY III O   
10327 N N   . ARG I 19  ? 1.958 3.753 1.599 0.689  -0.095 -0.251 19  ARG III N   
10328 C CA  . ARG I 19  ? 2.035 3.925 1.693 0.690  -0.103 -0.250 19  ARG III CA  
10329 C C   . ARG I 19  ? 2.050 3.970 1.750 0.617  -0.098 -0.255 19  ARG III C   
10330 O O   . ARG I 19  ? 1.906 3.852 1.610 0.575  -0.092 -0.257 19  ARG III O   
10331 C CB  . ARG I 19  ? 2.103 4.128 1.739 0.732  -0.112 -0.246 19  ARG III CB  
10332 C CG  . ARG I 19  ? 2.135 4.268 1.786 0.738  -0.118 -0.246 19  ARG III CG  
10333 C CD  . ARG I 19  ? 2.162 4.422 1.840 0.680  -0.118 -0.249 19  ARG III CD  
10334 N NE  . ARG I 19  ? 2.306 4.667 1.968 0.692  -0.123 -0.245 19  ARG III NE  
10335 C CZ  . ARG I 19  ? 2.333 4.810 2.009 0.641  -0.124 -0.247 19  ARG III CZ  
10336 N NH1 . ARG I 19  ? 2.337 4.841 2.038 0.575  -0.120 -0.253 19  ARG III NH1 
10337 N NH2 . ARG I 19  ? 2.375 4.941 2.033 0.655  -0.130 -0.242 19  ARG III NH2 
10338 N N   . VAL I 20  ? 2.209 4.116 1.932 0.601  -0.100 -0.256 20  VAL III N   
10339 C CA  . VAL I 20  ? 2.174 4.087 1.929 0.533  -0.095 -0.259 20  VAL III CA  
10340 C C   . VAL I 20  ? 2.134 4.166 1.893 0.523  -0.102 -0.260 20  VAL III C   
10341 O O   . VAL I 20  ? 1.963 4.010 1.719 0.557  -0.110 -0.258 20  VAL III O   
10342 C CB  . VAL I 20  ? 2.154 3.948 1.932 0.517  -0.092 -0.258 20  VAL III CB  
10343 C CG1 . VAL I 20  ? 2.180 3.962 1.983 0.450  -0.084 -0.260 20  VAL III CG1 
10344 C CG2 . VAL I 20  ? 2.093 3.778 1.866 0.538  -0.086 -0.256 20  VAL III CG2 
10345 N N   . SER I 21  ? 2.114 4.228 1.875 0.473  -0.099 -0.263 21  SER III N   
10346 C CA  . SER I 21  ? 2.211 4.443 1.975 0.450  -0.104 -0.265 21  SER III CA  
10347 C C   . SER I 21  ? 2.097 4.284 1.876 0.383  -0.098 -0.269 21  SER III C   
10348 O O   . SER I 21  ? 2.009 4.127 1.788 0.338  -0.088 -0.271 21  SER III O   
10349 C CB  . SER I 21  ? 2.423 4.790 2.173 0.435  -0.105 -0.266 21  SER III CB  
10350 O OG  . SER I 21  ? 2.368 4.697 2.110 0.386  -0.097 -0.269 21  SER III OG  
10351 N N   . PHE I 22  ? 2.211 4.431 1.996 0.379  -0.103 -0.269 22  PHE III N   
10352 C CA  . PHE I 22  ? 2.342 4.530 2.131 0.316  -0.099 -0.271 22  PHE III CA  
10353 C C   . PHE I 22  ? 2.449 4.763 2.230 0.295  -0.103 -0.274 22  PHE III C   
10354 O O   . PHE I 22  ? 2.452 4.849 2.233 0.342  -0.110 -0.273 22  PHE III O   
10355 C CB  . PHE I 22  ? 2.402 4.461 2.209 0.324  -0.101 -0.267 22  PHE III CB  
10356 C CG  . PHE I 22  ? 2.719 4.761 2.529 0.387  -0.110 -0.264 22  PHE III CG  
10357 C CD1 . PHE I 22  ? 3.349 5.464 3.152 0.402  -0.118 -0.264 22  PHE III CD1 
10358 C CD2 . PHE I 22  ? 2.389 4.338 2.203 0.428  -0.111 -0.260 22  PHE III CD2 
10359 C CE1 . PHE I 22  ? 3.512 5.601 3.308 0.459  -0.125 -0.261 22  PHE III CE1 
10360 C CE2 . PHE I 22  ? 2.651 4.574 2.457 0.481  -0.119 -0.257 22  PHE III CE2 
10361 C CZ  . PHE I 22  ? 3.399 5.389 3.194 0.498  -0.126 -0.257 22  PHE III CZ  
10362 N N   . GLU I 23  ? 2.500 4.827 2.270 0.223  -0.097 -0.278 23  GLU III N   
10363 C CA  . GLU I 23  ? 2.623 5.060 2.381 0.186  -0.099 -0.282 23  GLU III CA  
10364 C C   . GLU I 23  ? 2.620 4.979 2.379 0.169  -0.101 -0.281 23  GLU III C   
10365 O O   . GLU I 23  ? 2.712 4.946 2.472 0.145  -0.097 -0.279 23  GLU III O   
10366 C CB  . GLU I 23  ? 2.756 5.252 2.487 0.111  -0.091 -0.287 23  GLU III CB  
10367 C CG  . GLU I 23  ? 2.911 5.515 2.625 0.059  -0.092 -0.292 23  GLU III CG  
10368 C CD  . GLU I 23  ? 2.991 5.650 2.670 -0.022 -0.084 -0.297 23  GLU III CD  
10369 O OE1 . GLU I 23  ? 2.922 5.485 2.583 -0.052 -0.075 -0.298 23  GLU III OE1 
10370 O OE2 . GLU I 23  ? 3.205 6.001 2.870 -0.058 -0.086 -0.300 23  GLU III OE2 
10371 N N   . LEU I 24  ? 2.703 5.139 2.462 0.182  -0.107 -0.282 24  LEU III N   
10372 C CA  . LEU I 24  ? 2.558 4.928 2.314 0.166  -0.110 -0.281 24  LEU III CA  
10373 C C   . LEU I 24  ? 2.762 5.200 2.491 0.094  -0.106 -0.286 24  LEU III C   
10374 O O   . LEU I 24  ? 2.917 5.498 2.638 0.083  -0.104 -0.290 24  LEU III O   
10375 C CB  . LEU I 24  ? 2.286 4.678 2.052 0.230  -0.118 -0.278 24  LEU III CB  
10376 C CG  . LEU I 24  ? 2.122 4.455 1.902 0.306  -0.123 -0.273 24  LEU III CG  
10377 C CD1 . LEU I 24  ? 2.166 4.518 1.940 0.358  -0.129 -0.272 24  LEU III CD1 
10378 C CD2 . LEU I 24  ? 2.245 4.425 2.038 0.302  -0.124 -0.268 24  LEU III CD2 
10379 N N   . PHE I 25  ? 2.584 4.916 2.297 0.046  -0.104 -0.285 25  PHE III N   
10380 C CA  . PHE I 25  ? 2.776 5.133 2.450 -0.033 -0.097 -0.290 25  PHE III CA  
10381 C C   . PHE I 25  ? 2.937 5.337 2.603 -0.037 -0.103 -0.291 25  PHE III C   
10382 O O   . PHE I 25  ? 3.162 5.472 2.809 -0.065 -0.105 -0.289 25  PHE III O   
10383 C CB  . PHE I 25  ? 2.718 4.929 2.370 -0.078 -0.090 -0.287 25  PHE III CB  
10384 C CG  . PHE I 25  ? 2.613 4.783 2.268 -0.078 -0.082 -0.288 25  PHE III CG  
10385 C CD1 . PHE I 25  ? 2.637 4.919 2.285 -0.091 -0.077 -0.293 25  PHE III CD1 
10386 C CD2 . PHE I 25  ? 2.522 4.549 2.189 -0.065 -0.077 -0.282 25  PHE III CD2 
10387 C CE1 . PHE I 25  ? 2.580 4.822 2.226 -0.093 -0.069 -0.294 25  PHE III CE1 
10388 C CE2 . PHE I 25  ? 2.488 4.478 2.156 -0.065 -0.067 -0.283 25  PHE III CE2 
10389 C CZ  . PHE I 25  ? 2.567 4.659 2.221 -0.080 -0.063 -0.289 25  PHE III CZ  
10390 N N   . ALA I 26  ? 2.995 5.535 2.673 -0.005 -0.105 -0.294 26  ALA III N   
10391 C CA  . ALA I 26  ? 2.910 5.504 2.581 0.001  -0.108 -0.296 26  ALA III CA  
10392 C C   . ALA I 26  ? 3.065 5.694 2.696 -0.084 -0.102 -0.302 26  ALA III C   
10393 O O   . ALA I 26  ? 2.925 5.559 2.541 -0.093 -0.104 -0.303 26  ALA III O   
10394 C CB  . ALA I 26  ? 2.873 5.617 2.565 0.059  -0.108 -0.298 26  ALA III CB  
10395 N N   . ASP I 27  ? 3.303 5.950 2.907 -0.149 -0.094 -0.306 27  ASP III N   
10396 C CA  . ASP I 27  ? 3.378 6.042 2.930 -0.237 -0.087 -0.312 27  ASP III CA  
10397 C C   . ASP I 27  ? 3.324 5.817 2.845 -0.267 -0.089 -0.307 27  ASP III C   
10398 O O   . ASP I 27  ? 3.554 6.047 3.031 -0.324 -0.086 -0.311 27  ASP III O   
10399 C CB  . ASP I 27  ? 3.567 6.275 3.089 -0.301 -0.078 -0.317 27  ASP III CB  
10400 C CG  . ASP I 27  ? 3.544 6.103 3.060 -0.303 -0.074 -0.313 27  ASP III CG  
10401 O OD1 . ASP I 27  ? 3.469 5.947 3.026 -0.234 -0.081 -0.306 27  ASP III OD1 
10402 O OD2 . ASP I 27  ? 3.618 6.137 3.084 -0.375 -0.064 -0.316 27  ASP III OD2 
10403 N N   . LYS I 28  ? 3.139 5.493 2.681 -0.228 -0.093 -0.299 28  LYS III N   
10404 C CA  . LYS I 28  ? 3.125 5.322 2.645 -0.243 -0.097 -0.293 28  LYS III CA  
10405 C C   . LYS I 28  ? 3.034 5.184 2.589 -0.180 -0.111 -0.285 28  LYS III C   
10406 O O   . LYS I 28  ? 2.985 5.065 2.515 -0.199 -0.117 -0.281 28  LYS III O   
10407 C CB  . LYS I 28  ? 3.029 5.096 2.543 -0.252 -0.091 -0.288 28  LYS III CB  
10408 C CG  . LYS I 28  ? 2.909 4.995 2.373 -0.324 -0.075 -0.295 28  LYS III CG  
10409 C CD  . LYS I 28  ? 2.807 4.908 2.202 -0.402 -0.070 -0.301 28  LYS III CD  
10410 C CE  . LYS I 28  ? 2.862 5.013 2.201 -0.480 -0.055 -0.310 28  LYS III CE  
10411 N NZ  . LYS I 28  ? 2.866 4.892 2.179 -0.495 -0.044 -0.308 28  LYS III NZ  
10412 N N   . VAL I 29  ? 2.854 5.035 2.458 -0.108 -0.117 -0.282 29  VAL III N   
10413 C CA  . VAL I 29  ? 2.730 4.859 2.360 -0.050 -0.130 -0.275 29  VAL III CA  
10414 C C   . VAL I 29  ? 2.706 4.952 2.359 0.007  -0.131 -0.280 29  VAL III C   
10415 O O   . VAL I 29  ? 2.607 4.838 2.292 0.067  -0.134 -0.276 29  VAL III O   
10416 C CB  . VAL I 29  ? 2.554 4.548 2.212 -0.017 -0.137 -0.265 29  VAL III CB  
10417 C CG1 . VAL I 29  ? 2.513 4.383 2.146 -0.061 -0.139 -0.258 29  VAL III CG1 
10418 C CG2 . VAL I 29  ? 2.647 4.652 2.327 -0.002 -0.128 -0.267 29  VAL III CG2 
10419 N N   . PRO I 30  ? 2.787 5.148 2.422 -0.006 -0.127 -0.287 30  PRO III N   
10420 C CA  . PRO I 30  ? 2.783 5.257 2.439 0.056  -0.126 -0.290 30  PRO III CA  
10421 C C   . PRO I 30  ? 2.713 5.113 2.379 0.121  -0.135 -0.284 30  PRO III C   
10422 O O   . PRO I 30  ? 2.632 5.056 2.316 0.187  -0.135 -0.283 30  PRO III O   
10423 C CB  . PRO I 30  ? 2.918 5.527 2.550 0.017  -0.117 -0.298 30  PRO III CB  
10424 C CG  . PRO I 30  ? 2.994 5.524 2.588 -0.056 -0.118 -0.298 30  PRO III CG  
10425 C CD  . PRO I 30  ? 2.922 5.319 2.515 -0.079 -0.122 -0.292 30  PRO III CD  
10426 N N   . LYS I 31  ? 2.714 5.020 2.361 0.101  -0.144 -0.280 31  LYS III N   
10427 C CA  . LYS I 31  ? 2.615 4.849 2.265 0.155  -0.154 -0.274 31  LYS III CA  
10428 C C   . LYS I 31  ? 2.577 4.719 2.254 0.200  -0.161 -0.267 31  LYS III C   
10429 O O   . LYS I 31  ? 2.648 4.783 2.330 0.261  -0.163 -0.266 31  LYS III O   
10430 C CB  . LYS I 31  ? 2.609 4.753 2.234 0.117  -0.164 -0.269 31  LYS III CB  
10431 C CG  . LYS I 31  ? 2.621 4.694 2.238 0.162  -0.175 -0.264 31  LYS III CG  
10432 C CD  . LYS I 31  ? 2.720 4.730 2.305 0.120  -0.184 -0.260 31  LYS III CD  
10433 C CE  . LYS I 31  ? 2.752 4.693 2.325 0.159  -0.196 -0.254 31  LYS III CE  
10434 N NZ  . LYS I 31  ? 2.949 4.772 2.546 0.181  -0.212 -0.242 31  LYS III NZ  
10435 N N   . THR I 32  ? 2.628 4.697 2.320 0.170  -0.163 -0.262 32  THR III N   
10436 C CA  . THR I 32  ? 2.425 4.409 2.146 0.208  -0.168 -0.255 32  THR III CA  
10437 C C   . THR I 32  ? 2.429 4.489 2.164 0.249  -0.159 -0.260 32  THR III C   
10438 O O   . THR I 32  ? 2.400 4.423 2.145 0.303  -0.162 -0.257 32  THR III O   
10439 C CB  . THR I 32  ? 2.308 4.199 2.040 0.167  -0.170 -0.248 32  THR III CB  
10440 O OG1 . THR I 32  ? 2.385 4.211 2.099 0.131  -0.179 -0.242 32  THR III OG1 
10441 C CG2 . THR I 32  ? 2.245 4.049 2.010 0.205  -0.175 -0.240 32  THR III CG2 
10442 N N   . ALA I 33  ? 2.416 4.582 2.147 0.221  -0.148 -0.267 33  ALA III N   
10443 C CA  . ALA I 33  ? 2.432 4.687 2.173 0.258  -0.141 -0.271 33  ALA III CA  
10444 C C   . ALA I 33  ? 2.568 4.887 2.302 0.324  -0.141 -0.273 33  ALA III C   
10445 O O   . ALA I 33  ? 2.573 4.888 2.312 0.381  -0.140 -0.271 33  ALA III O   
10446 C CB  . ALA I 33  ? 2.479 4.848 2.213 0.207  -0.131 -0.278 33  ALA III CB  
10447 N N   . GLU I 34  ? 2.672 5.045 2.387 0.317  -0.139 -0.276 34  GLU III N   
10448 C CA  . GLU I 34  ? 2.791 5.228 2.493 0.381  -0.136 -0.278 34  GLU III CA  
10449 C C   . GLU I 34  ? 2.856 5.173 2.547 0.439  -0.143 -0.273 34  GLU III C   
10450 O O   . GLU I 34  ? 3.123 5.466 2.803 0.505  -0.138 -0.273 34  GLU III O   
10451 C CB  . GLU I 34  ? 2.845 5.351 2.526 0.357  -0.131 -0.283 34  GLU III CB  
10452 C CG  . GLU I 34  ? 3.010 5.573 2.671 0.424  -0.124 -0.286 34  GLU III CG  
10453 C CD  . GLU I 34  ? 3.172 5.872 2.844 0.473  -0.114 -0.288 34  GLU III CD  
10454 O OE1 . GLU I 34  ? 3.309 6.140 2.997 0.436  -0.108 -0.292 34  GLU III OE1 
10455 O OE2 . GLU I 34  ? 3.259 5.935 2.920 0.548  -0.112 -0.285 34  GLU III OE2 
10456 N N   . ASN I 35  ? 2.769 4.956 2.460 0.414  -0.154 -0.267 35  ASN III N   
10457 C CA  . ASN I 35  ? 2.732 4.804 2.412 0.460  -0.162 -0.261 35  ASN III CA  
10458 C C   . ASN I 35  ? 2.653 4.704 2.346 0.499  -0.160 -0.259 35  ASN III C   
10459 O O   . ASN I 35  ? 2.636 4.670 2.306 0.560  -0.157 -0.259 35  ASN III O   
10460 C CB  . ASN I 35  ? 2.721 4.667 2.408 0.423  -0.176 -0.253 35  ASN III CB  
10461 C CG  . ASN I 35  ? 2.713 4.550 2.386 0.464  -0.185 -0.247 35  ASN III CG  
10462 O OD1 . ASN I 35  ? 2.728 4.576 2.371 0.518  -0.180 -0.250 35  ASN III OD1 
10463 N ND2 . ASN I 35  ? 2.771 4.505 2.464 0.441  -0.197 -0.238 35  ASN III ND2 
10464 N N   . PHE I 36  ? 2.665 4.711 2.388 0.464  -0.159 -0.258 36  PHE III N   
10465 C CA  . PHE I 36  ? 2.615 4.637 2.349 0.493  -0.156 -0.257 36  PHE III CA  
10466 C C   . PHE I 36  ? 2.638 4.769 2.358 0.543  -0.147 -0.261 36  PHE III C   
10467 O O   . PHE I 36  ? 2.632 4.730 2.338 0.597  -0.146 -0.259 36  PHE III O   
10468 C CB  . PHE I 36  ? 2.537 4.541 2.301 0.441  -0.154 -0.256 36  PHE III CB  
10469 C CG  . PHE I 36  ? 2.477 4.427 2.255 0.463  -0.152 -0.253 36  PHE III CG  
10470 C CD1 . PHE I 36  ? 2.308 4.135 2.099 0.461  -0.158 -0.246 36  PHE III CD1 
10471 C CD2 . PHE I 36  ? 2.612 4.635 2.386 0.485  -0.144 -0.257 36  PHE III CD2 
10472 C CE1 . PHE I 36  ? 2.312 4.090 2.113 0.479  -0.154 -0.245 36  PHE III CE1 
10473 C CE2 . PHE I 36  ? 2.611 4.580 2.393 0.504  -0.142 -0.255 36  PHE III CE2 
10474 C CZ  . PHE I 36  ? 2.427 4.271 2.220 0.500  -0.146 -0.249 36  PHE III CZ  
10475 N N   . ARG I 37  ? 2.609 4.873 2.331 0.525  -0.141 -0.266 37  ARG III N   
10476 C CA  . ARG I 37  ? 2.621 5.004 2.334 0.576  -0.133 -0.268 37  ARG III CA  
10477 C C   . ARG I 37  ? 2.721 5.079 2.399 0.651  -0.131 -0.267 37  ARG III C   
10478 O O   . ARG I 37  ? 2.632 4.988 2.294 0.712  -0.128 -0.265 37  ARG III O   
10479 C CB  . ARG I 37  ? 2.636 5.175 2.357 0.540  -0.127 -0.274 37  ARG III CB  
10480 C CG  . ARG I 37  ? 2.541 5.224 2.263 0.585  -0.120 -0.274 37  ARG III CG  
10481 C CD  . ARG I 37  ? 2.598 5.367 2.301 0.633  -0.113 -0.276 37  ARG III CD  
10482 N NE  . ARG I 37  ? 2.613 5.490 2.325 0.577  -0.109 -0.281 37  ARG III NE  
10483 C CZ  . ARG I 37  ? 2.671 5.635 2.369 0.601  -0.100 -0.284 37  ARG III CZ  
10484 N NH1 . ARG I 37  ? 2.781 5.742 2.455 0.684  -0.094 -0.282 37  ARG III NH1 
10485 N NH2 . ARG I 37  ? 2.729 5.782 2.433 0.539  -0.096 -0.290 37  ARG III NH2 
10486 N N   . ALA I 38  ? 2.914 5.244 2.573 0.647  -0.132 -0.268 38  ALA III N   
10487 C CA  . ALA I 38  ? 3.025 5.326 2.640 0.717  -0.127 -0.268 38  ALA III CA  
10488 C C   . ALA I 38  ? 2.962 5.109 2.553 0.748  -0.134 -0.263 38  ALA III C   
10489 O O   . ALA I 38  ? 3.192 5.313 2.742 0.817  -0.128 -0.262 38  ALA III O   
10490 C CB  . ALA I 38  ? 3.199 5.499 2.794 0.700  -0.126 -0.271 38  ALA III CB  
10491 N N   . LEU I 39  ? 2.809 4.850 2.421 0.699  -0.145 -0.260 39  LEU III N   
10492 C CA  . LEU I 39  ? 2.596 4.502 2.190 0.722  -0.150 -0.255 39  LEU III CA  
10493 C C   . LEU I 39  ? 2.630 4.549 2.228 0.755  -0.146 -0.254 39  LEU III C   
10494 O O   . LEU I 39  ? 2.556 4.387 2.117 0.797  -0.145 -0.251 39  LEU III O   
10495 C CB  . LEU I 39  ? 2.372 4.182 1.997 0.662  -0.163 -0.250 39  LEU III CB  
10496 C CG  . LEU I 39  ? 2.346 4.108 1.963 0.629  -0.172 -0.248 39  LEU III CG  
10497 C CD1 . LEU I 39  ? 2.274 3.959 1.931 0.574  -0.185 -0.241 39  LEU III CD1 
10498 C CD2 . LEU I 39  ? 2.416 4.098 1.975 0.671  -0.174 -0.247 39  LEU III CD2 
10499 N N   . SER I 40  ? 2.636 4.658 2.269 0.732  -0.142 -0.256 40  SER III N   
10500 C CA  . SER I 40  ? 2.578 4.619 2.213 0.760  -0.138 -0.255 40  SER III CA  
10501 C C   . SER I 40  ? 2.737 4.854 2.335 0.835  -0.130 -0.255 40  SER III C   
10502 O O   . SER I 40  ? 2.766 4.849 2.341 0.880  -0.128 -0.252 40  SER III O   
10503 C CB  . SER I 40  ? 2.442 4.563 2.123 0.704  -0.137 -0.257 40  SER III CB  
10504 O OG  . SER I 40  ? 2.498 4.533 2.208 0.644  -0.142 -0.255 40  SER III OG  
10505 N N   . THR I 41  ? 2.822 5.040 2.412 0.853  -0.125 -0.257 41  THR III N   
10506 C CA  . THR I 41  ? 2.750 5.052 2.306 0.930  -0.116 -0.256 41  THR III CA  
10507 C C   . THR I 41  ? 2.964 5.168 2.456 0.993  -0.111 -0.255 41  THR III C   
10508 O O   . THR I 41  ? 3.062 5.287 2.510 1.070  -0.103 -0.253 41  THR III O   
10509 C CB  . THR I 41  ? 2.748 5.228 2.330 0.919  -0.110 -0.259 41  THR III CB  
10510 O OG1 . THR I 41  ? 2.845 5.310 2.422 0.891  -0.109 -0.264 41  THR III OG1 
10511 C CG2 . THR I 41  ? 2.652 5.226 2.286 0.851  -0.114 -0.261 41  THR III CG2 
10512 N N   . GLY I 42  ? 3.037 5.131 2.515 0.962  -0.116 -0.257 42  GLY III N   
10513 C CA  . GLY I 42  ? 3.161 5.152 2.569 1.013  -0.111 -0.257 42  GLY III CA  
10514 C C   . GLY I 42  ? 3.312 5.393 2.694 1.054  -0.098 -0.260 42  GLY III C   
10515 O O   . GLY I 42  ? 3.477 5.493 2.790 1.115  -0.089 -0.260 42  GLY III O   
10516 N N   . GLU I 43  ? 3.160 5.391 2.592 1.020  -0.096 -0.263 43  GLU III N   
10517 C CA  . GLU I 43  ? 3.081 5.427 2.496 1.059  -0.082 -0.266 43  GLU III CA  
10518 C C   . GLU I 43  ? 3.068 5.331 2.442 1.053  -0.078 -0.270 43  GLU III C   
10519 O O   . GLU I 43  ? 3.360 5.674 2.696 1.103  -0.062 -0.272 43  GLU III O   
10520 C CB  . GLU I 43  ? 3.042 5.565 2.523 1.008  -0.081 -0.269 43  GLU III CB  
10521 C CG  . GLU I 43  ? 2.996 5.488 2.508 0.915  -0.091 -0.273 43  GLU III CG  
10522 C CD  . GLU I 43  ? 2.978 5.612 2.548 0.849  -0.093 -0.275 43  GLU III CD  
10523 O OE1 . GLU I 43  ? 2.953 5.628 2.553 0.837  -0.097 -0.273 43  GLU III OE1 
10524 O OE2 . GLU I 43  ? 2.975 5.674 2.553 0.807  -0.089 -0.280 43  GLU III OE2 
10525 N N   . LYS I 44  ? 2.879 5.016 2.256 0.993  -0.092 -0.269 44  LYS III N   
10526 C CA  . LYS I 44  ? 2.840 4.877 2.172 0.982  -0.093 -0.271 44  LYS III CA  
10527 C C   . LYS I 44  ? 2.788 4.666 2.041 1.033  -0.091 -0.269 44  LYS III C   
10528 O O   . LYS I 44  ? 2.750 4.535 1.953 1.028  -0.091 -0.270 44  LYS III O   
10529 C CB  . LYS I 44  ? 2.784 4.765 2.157 0.892  -0.111 -0.270 44  LYS III CB  
10530 C CG  . LYS I 44  ? 2.782 4.893 2.220 0.831  -0.113 -0.273 44  LYS III CG  
10531 C CD  . LYS I 44  ? 2.833 5.050 2.260 0.831  -0.100 -0.279 44  LYS III CD  
10532 C CE  . LYS I 44  ? 2.778 5.135 2.263 0.773  -0.100 -0.282 44  LYS III CE  
10533 N NZ  . LYS I 44  ? 2.915 5.410 2.393 0.782  -0.084 -0.288 44  LYS III NZ  
10534 N N   . GLY I 45  ? 2.733 4.572 1.967 1.078  -0.089 -0.265 45  GLY III N   
10535 C CA  . GLY I 45  ? 2.772 4.456 1.921 1.126  -0.086 -0.263 45  GLY III CA  
10536 C C   . GLY I 45  ? 2.884 4.434 2.040 1.081  -0.103 -0.259 45  GLY III C   
10537 O O   . GLY I 45  ? 2.933 4.346 2.015 1.110  -0.102 -0.257 45  GLY III O   
10538 N N   . PHE I 46  ? 2.859 4.446 2.097 1.010  -0.118 -0.257 46  PHE III N   
10539 C CA  . PHE I 46  ? 2.807 4.289 2.065 0.968  -0.133 -0.253 46  PHE III CA  
10540 C C   . PHE I 46  ? 2.681 4.256 2.028 0.922  -0.139 -0.252 46  PHE III C   
10541 O O   . PHE I 46  ? 2.686 4.368 2.082 0.888  -0.139 -0.254 46  PHE III O   
10542 C CB  . PHE I 46  ? 2.757 4.136 2.002 0.917  -0.146 -0.250 46  PHE III CB  
10543 C CG  . PHE I 46  ? 2.710 4.170 2.001 0.867  -0.151 -0.252 46  PHE III CG  
10544 C CD1 . PHE I 46  ? 2.569 4.068 1.938 0.800  -0.164 -0.249 46  PHE III CD1 
10545 C CD2 . PHE I 46  ? 2.809 4.303 2.057 0.889  -0.141 -0.257 46  PHE III CD2 
10546 C CE1 . PHE I 46  ? 2.441 4.002 1.840 0.756  -0.168 -0.250 46  PHE III CE1 
10547 C CE2 . PHE I 46  ? 2.739 4.304 2.023 0.843  -0.145 -0.259 46  PHE III CE2 
10548 C CZ  . PHE I 46  ? 2.546 4.142 1.903 0.775  -0.159 -0.255 46  PHE III CZ  
10549 N N   . GLY I 47  ? 2.596 4.100 1.967 0.897  -0.147 -0.248 47  GLY III N   
10550 C CA  . GLY I 47  ? 2.454 4.030 1.899 0.857  -0.150 -0.247 47  GLY III CA  
10551 C C   . GLY I 47  ? 2.313 3.809 1.772 0.844  -0.154 -0.243 47  GLY III C   
10552 O O   . GLY I 47  ? 2.271 3.645 1.692 0.849  -0.159 -0.240 47  GLY III O   
10553 N N   . TYR I 48  ? 2.162 3.727 1.673 0.823  -0.152 -0.244 48  TYR III N   
10554 C CA  . TYR I 48  ? 2.081 3.577 1.621 0.794  -0.156 -0.241 48  TYR III CA  
10555 C C   . TYR I 48  ? 2.178 3.613 1.672 0.840  -0.150 -0.240 48  TYR III C   
10556 O O   . TYR I 48  ? 2.214 3.566 1.718 0.819  -0.152 -0.237 48  TYR III O   
10557 C CB  . TYR I 48  ? 1.982 3.559 1.589 0.747  -0.155 -0.242 48  TYR III CB  
10558 C CG  . TYR I 48  ? 1.891 3.493 1.543 0.689  -0.161 -0.241 48  TYR III CG  
10559 C CD1 . TYR I 48  ? 1.843 3.355 1.499 0.661  -0.172 -0.236 48  TYR III CD1 
10560 C CD2 . TYR I 48  ? 1.946 3.656 1.632 0.658  -0.157 -0.244 48  TYR III CD2 
10561 C CE1 . TYR I 48  ? 1.847 3.376 1.539 0.610  -0.179 -0.234 48  TYR III CE1 
10562 C CE2 . TYR I 48  ? 1.933 3.653 1.649 0.604  -0.163 -0.243 48  TYR III CE2 
10563 C CZ  . TYR I 48  ? 1.879 3.506 1.598 0.583  -0.173 -0.238 48  TYR III CZ  
10564 O OH  . TYR I 48  ? 1.998 3.631 1.743 0.532  -0.180 -0.235 48  TYR III OH  
10565 N N   . LYS I 49  ? 2.249 3.725 1.693 0.904  -0.141 -0.242 49  LYS III N   
10566 C CA  . LYS I 49  ? 2.294 3.713 1.690 0.949  -0.136 -0.241 49  LYS III CA  
10567 C C   . LYS I 49  ? 2.324 3.585 1.667 0.949  -0.138 -0.238 49  LYS III C   
10568 O O   . LYS I 49  ? 2.343 3.546 1.639 0.960  -0.140 -0.238 49  LYS III O   
10569 C CB  . LYS I 49  ? 2.348 3.836 1.694 1.024  -0.127 -0.241 49  LYS III CB  
10570 C CG  . LYS I 49  ? 2.441 4.095 1.831 1.024  -0.125 -0.243 49  LYS III CG  
10571 C CD  . LYS I 49  ? 2.582 4.303 1.921 1.106  -0.116 -0.241 49  LYS III CD  
10572 C CE  . LYS I 49  ? 2.637 4.471 2.007 1.117  -0.116 -0.239 49  LYS III CE  
10573 N NZ  . LYS I 49  ? 2.707 4.625 2.034 1.200  -0.108 -0.235 49  LYS III NZ  
10574 N N   . GLY I 50  ? 2.370 3.559 1.717 0.932  -0.138 -0.237 50  GLY III N   
10575 C CA  . GLY I 50  ? 2.477 3.523 1.777 0.922  -0.141 -0.235 50  GLY III CA  
10576 C C   . GLY I 50  ? 2.495 3.502 1.852 0.853  -0.151 -0.232 50  GLY III C   
10577 O O   . GLY I 50  ? 2.516 3.412 1.841 0.836  -0.155 -0.229 50  GLY III O   
10578 N N   . SER I 51  ? 2.489 3.581 1.926 0.811  -0.156 -0.231 51  SER III N   
10579 C CA  . SER I 51  ? 2.422 3.483 1.914 0.752  -0.167 -0.226 51  SER III CA  
10580 C C   . SER I 51  ? 2.319 3.361 1.861 0.720  -0.163 -0.224 51  SER III C   
10581 O O   . SER I 51  ? 2.267 3.335 1.808 0.738  -0.153 -0.228 51  SER III O   
10582 C CB  . SER I 51  ? 2.432 3.583 1.980 0.723  -0.173 -0.226 51  SER III CB  
10583 O OG  . SER I 51  ? 2.284 3.540 1.865 0.727  -0.164 -0.230 51  SER III OG  
10584 N N   . CYS I 52  ? 2.237 3.235 1.822 0.673  -0.171 -0.218 52  CYS III N   
10585 C CA  . CYS I 52  ? 2.105 3.079 1.736 0.645  -0.165 -0.216 52  CYS III CA  
10586 C C   . CYS I 52  ? 1.933 2.965 1.649 0.603  -0.166 -0.213 52  CYS III C   
10587 O O   . CYS I 52  ? 1.906 2.979 1.646 0.587  -0.175 -0.210 52  CYS III O   
10588 C CB  . CYS I 52  ? 2.043 2.916 1.656 0.626  -0.171 -0.210 52  CYS III CB  
10589 S SG  . CYS I 52  ? 2.365 3.137 1.871 0.665  -0.165 -0.214 52  CYS III SG  
10590 N N   . PHE I 53  ? 1.783 2.813 1.539 0.585  -0.155 -0.213 53  PHE III N   
10591 C CA  . PHE I 53  ? 1.604 2.658 1.434 0.544  -0.153 -0.208 53  PHE III CA  
10592 C C   . PHE I 53  ? 1.667 2.656 1.525 0.519  -0.160 -0.198 53  PHE III C   
10593 O O   . PHE I 53  ? 1.772 2.713 1.627 0.518  -0.152 -0.198 53  PHE III O   
10594 C CB  . PHE I 53  ? 1.528 2.613 1.383 0.538  -0.135 -0.213 53  PHE III CB  
10595 C CG  . PHE I 53  ? 1.509 2.678 1.356 0.546  -0.131 -0.220 53  PHE III CG  
10596 C CD1 . PHE I 53  ? 1.537 2.737 1.332 0.585  -0.129 -0.227 53  PHE III CD1 
10597 C CD2 . PHE I 53  ? 1.388 2.606 1.276 0.514  -0.130 -0.219 53  PHE III CD2 
10598 C CE1 . PHE I 53  ? 1.407 2.697 1.198 0.590  -0.126 -0.232 53  PHE III CE1 
10599 C CE2 . PHE I 53  ? 1.313 2.611 1.190 0.514  -0.126 -0.226 53  PHE III CE2 
10600 C CZ  . PHE I 53  ? 1.348 2.690 1.180 0.551  -0.125 -0.232 53  PHE III CZ  
10601 N N   . HIS I 54  ? 1.603 2.595 1.488 0.498  -0.175 -0.190 54  HIS III N   
10602 C CA  . HIS I 54  ? 1.599 2.540 1.507 0.475  -0.186 -0.179 54  HIS III CA  
10603 C C   . HIS I 54  ? 1.524 2.476 1.510 0.447  -0.180 -0.171 54  HIS III C   
10604 O O   . HIS I 54  ? 1.490 2.407 1.502 0.431  -0.182 -0.163 54  HIS III O   
10605 C CB  . HIS I 54  ? 1.721 2.654 1.610 0.468  -0.208 -0.172 54  HIS III CB  
10606 C CG  . HIS I 54  ? 1.692 2.679 1.619 0.453  -0.214 -0.169 54  HIS III CG  
10607 N ND1 . HIS I 54  ? 1.678 2.717 1.582 0.467  -0.211 -0.177 54  HIS III ND1 
10608 C CD2 . HIS I 54  ? 1.653 2.647 1.636 0.425  -0.225 -0.157 54  HIS III CD2 
10609 C CE1 . HIS I 54  ? 1.710 2.780 1.648 0.444  -0.218 -0.172 54  HIS III CE1 
10610 N NE2 . HIS I 54  ? 1.644 2.685 1.629 0.420  -0.226 -0.159 54  HIS III NE2 
10611 N N   . ARG I 55  ? 1.495 2.494 1.516 0.439  -0.171 -0.172 55  ARG III N   
10612 C CA  . ARG I 55  ? 1.347 2.351 1.434 0.419  -0.160 -0.166 55  ARG III CA  
10613 C C   . ARG I 55  ? 1.241 2.269 1.326 0.422  -0.137 -0.177 55  ARG III C   
10614 O O   . ARG I 55  ? 1.208 2.278 1.278 0.422  -0.136 -0.183 55  ARG III O   
10615 C CB  . ARG I 55  ? 1.284 2.304 1.409 0.399  -0.173 -0.154 55  ARG III CB  
10616 C CG  . ARG I 55  ? 1.228 2.223 1.388 0.386  -0.191 -0.138 55  ARG III CG  
10617 C CD  . ARG I 55  ? 1.289 2.301 1.479 0.371  -0.205 -0.126 55  ARG III CD  
10618 N NE  . ARG I 55  ? 1.173 2.196 1.404 0.364  -0.189 -0.123 55  ARG III NE  
10619 C CZ  . ARG I 55  ? 1.249 2.278 1.502 0.353  -0.196 -0.113 55  ARG III CZ  
10620 N NH1 . ARG I 55  ? 1.513 2.544 1.755 0.345  -0.221 -0.104 55  ARG III NH1 
10621 N NH2 . ARG I 55  ? 1.273 2.300 1.553 0.349  -0.177 -0.112 55  ARG III NH2 
10622 N N   . ILE I 56  ? 1.205 2.209 1.304 0.423  -0.120 -0.179 56  ILE III N   
10623 C CA  . ILE I 56  ? 1.196 2.216 1.301 0.419  -0.097 -0.187 56  ILE III CA  
10624 C C   . ILE I 56  ? 1.215 2.213 1.379 0.402  -0.082 -0.179 56  ILE III C   
10625 O O   . ILE I 56  ? 1.295 2.261 1.479 0.401  -0.077 -0.175 56  ILE III O   
10626 C CB  . ILE I 56  ? 1.245 2.255 1.304 0.438  -0.085 -0.198 56  ILE III CB  
10627 C CG1 . ILE I 56  ? 1.295 2.331 1.294 0.463  -0.098 -0.205 56  ILE III CG1 
10628 C CG2 . ILE I 56  ? 1.306 2.327 1.370 0.429  -0.062 -0.206 56  ILE III CG2 
10629 C CD1 . ILE I 56  ? 1.319 2.348 1.268 0.487  -0.089 -0.214 56  ILE III CD1 
10630 N N   . ILE I 57  ? 1.199 2.211 1.386 0.388  -0.073 -0.177 57  ILE III N   
10631 C CA  . ILE I 57  ? 1.144 2.135 1.383 0.377  -0.056 -0.169 57  ILE III CA  
10632 C C   . ILE I 57  ? 1.053 2.041 1.279 0.368  -0.029 -0.179 57  ILE III C   
10633 O O   . ILE I 57  ? 0.977 1.983 1.180 0.357  -0.028 -0.183 57  ILE III O   
10634 C CB  . ILE I 57  ? 1.138 2.133 1.413 0.368  -0.071 -0.154 57  ILE III CB  
10635 C CG1 . ILE I 57  ? 1.100 2.096 1.383 0.373  -0.099 -0.144 57  ILE III CG1 
10636 C CG2 . ILE I 57  ? 1.173 2.146 1.500 0.364  -0.052 -0.144 57  ILE III CG2 
10637 C CD1 . ILE I 57  ? 1.243 2.246 1.551 0.365  -0.119 -0.129 57  ILE III CD1 
10638 N N   . PRO I 58  ? 1.070 2.033 1.303 0.370  -0.006 -0.183 58  PRO III N   
10639 C CA  . PRO I 58  ? 1.122 2.078 1.332 0.359  0.020  -0.194 58  PRO III CA  
10640 C C   . PRO I 58  ? 1.131 2.072 1.359 0.344  0.033  -0.188 58  PRO III C   
10641 O O   . PRO I 58  ? 1.163 2.085 1.439 0.348  0.035  -0.175 58  PRO III O   
10642 C CB  . PRO I 58  ? 1.200 2.124 1.422 0.364  0.042  -0.197 58  PRO III CB  
10643 C CG  . PRO I 58  ? 1.184 2.099 1.455 0.371  0.031  -0.184 58  PRO III CG  
10644 C CD  . PRO I 58  ? 1.132 2.071 1.389 0.377  -0.002 -0.180 58  PRO III CD  
10645 N N   . GLY I 59  ? 1.165 2.114 1.351 0.327  0.043  -0.198 59  GLY III N   
10646 C CA  . GLY I 59  ? 1.220 2.144 1.404 0.310  0.056  -0.194 59  GLY III CA  
10647 C C   . GLY I 59  ? 1.218 2.159 1.402 0.305  0.033  -0.186 59  GLY III C   
10648 O O   . GLY I 59  ? 1.216 2.126 1.393 0.291  0.042  -0.181 59  GLY III O   
10649 N N   . PHE I 60  ? 1.153 2.134 1.336 0.315  0.004  -0.184 60  PHE III N   
10650 C CA  . PHE I 60  ? 1.249 2.246 1.433 0.310  -0.020 -0.176 60  PHE III CA  
10651 C C   . PHE I 60  ? 1.252 2.304 1.392 0.305  -0.037 -0.186 60  PHE III C   
10652 O O   . PHE I 60  ? 1.357 2.429 1.459 0.283  -0.034 -0.192 60  PHE III O   
10653 C CB  . PHE I 60  ? 1.346 2.334 1.579 0.328  -0.039 -0.160 60  PHE III CB  
10654 C CG  . PHE I 60  ? 1.354 2.350 1.589 0.322  -0.063 -0.150 60  PHE III CG  
10655 C CD1 . PHE I 60  ? 1.468 2.454 1.675 0.302  -0.059 -0.150 60  PHE III CD1 
10656 C CD2 . PHE I 60  ? 1.318 2.324 1.577 0.334  -0.090 -0.139 60  PHE III CD2 
10657 C CE1 . PHE I 60  ? 1.540 2.527 1.743 0.296  -0.081 -0.140 60  PHE III CE1 
10658 C CE2 . PHE I 60  ? 1.514 2.523 1.771 0.327  -0.112 -0.129 60  PHE III CE2 
10659 C CZ  . PHE I 60  ? 1.609 2.609 1.839 0.309  -0.108 -0.129 60  PHE III CZ  
10660 N N   . MET I 61  ? 1.203 2.279 1.344 0.327  -0.055 -0.187 61  MET III N   
10661 C CA  . MET I 61  ? 1.179 2.308 1.281 0.331  -0.071 -0.194 61  MET III CA  
10662 C C   . MET I 61  ? 1.145 2.279 1.241 0.360  -0.081 -0.196 61  MET III C   
10663 O O   . MET I 61  ? 1.143 2.238 1.266 0.371  -0.079 -0.191 61  MET III O   
10664 C CB  . MET I 61  ? 1.277 2.420 1.377 0.321  -0.091 -0.187 61  MET III CB  
10665 C CG  . MET I 61  ? 1.287 2.395 1.426 0.331  -0.108 -0.172 61  MET III CG  
10666 S SD  . MET I 61  ? 1.443 2.565 1.566 0.356  -0.132 -0.172 61  MET III SD  
10667 C CE  . MET I 61  ? 1.353 2.427 1.530 0.360  -0.142 -0.155 61  MET III CE  
10668 N N   . CYS I 62  ? 1.173 2.355 1.229 0.372  -0.091 -0.205 62  CYS III N   
10669 C CA  . CYS I 62  ? 1.219 2.401 1.253 0.404  -0.102 -0.206 62  CYS III CA  
10670 C C   . CYS I 62  ? 1.248 2.461 1.261 0.411  -0.122 -0.205 62  CYS III C   
10671 O O   . CYS I 62  ? 1.291 2.560 1.284 0.402  -0.123 -0.210 62  CYS III O   
10672 C CB  . CYS I 62  ? 1.292 2.502 1.290 0.421  -0.091 -0.217 62  CYS III CB  
10673 S SG  . CYS I 62  ? 1.445 2.615 1.457 0.412  -0.066 -0.221 62  CYS III SG  
10674 N N   . GLN I 63  ? 1.261 2.439 1.273 0.426  -0.137 -0.198 63  GLN III N   
10675 C CA  . GLN I 63  ? 1.268 2.461 1.260 0.430  -0.156 -0.195 63  GLN III CA  
10676 C C   . GLN I 63  ? 1.355 2.532 1.302 0.463  -0.164 -0.198 63  GLN III C   
10677 O O   . GLN I 63  ? 1.385 2.511 1.326 0.475  -0.162 -0.197 63  GLN III O   
10678 C CB  . GLN I 63  ? 1.353 2.509 1.382 0.408  -0.170 -0.182 63  GLN III CB  
10679 C CG  . GLN I 63  ? 1.439 2.612 1.451 0.401  -0.188 -0.178 63  GLN III CG  
10680 C CD  . GLN I 63  ? 1.385 2.517 1.429 0.384  -0.205 -0.163 63  GLN III CD  
10681 O OE1 . GLN I 63  ? 1.224 2.324 1.312 0.376  -0.201 -0.154 63  GLN III OE1 
10682 N NE2 . GLN I 63  ? 1.444 2.580 1.467 0.380  -0.223 -0.159 63  GLN III NE2 
10683 N N   . GLY I 64  ? 1.448 2.664 1.357 0.478  -0.172 -0.203 64  GLY III N   
10684 C CA  . GLY I 64  ? 1.613 2.812 1.468 0.515  -0.177 -0.206 64  GLY III CA  
10685 C C   . GLY I 64  ? 1.701 2.937 1.527 0.521  -0.187 -0.208 64  GLY III C   
10686 O O   . GLY I 64  ? 1.660 2.921 1.511 0.492  -0.193 -0.204 64  GLY III O   
10687 N N   . GLY I 65  ? 1.843 3.078 1.612 0.561  -0.187 -0.213 65  GLY III N   
10688 C CA  . GLY I 65  ? 1.922 3.201 1.660 0.572  -0.193 -0.216 65  GLY III CA  
10689 C C   . GLY I 65  ? 1.841 3.056 1.547 0.572  -0.207 -0.210 65  GLY III C   
10690 O O   . GLY I 65  ? 1.752 2.998 1.430 0.580  -0.210 -0.213 65  GLY III O   
10691 N N   . ASP I 66  ? 1.773 2.903 1.482 0.561  -0.215 -0.203 66  ASP III N   
10692 C CA  . ASP I 66  ? 1.925 2.990 1.596 0.556  -0.230 -0.197 66  ASP III CA  
10693 C C   . ASP I 66  ? 2.031 3.043 1.619 0.599  -0.224 -0.203 66  ASP III C   
10694 O O   . ASP I 66  ? 2.025 2.962 1.588 0.604  -0.224 -0.201 66  ASP III O   
10695 C CB  . ASP I 66  ? 2.010 3.018 1.723 0.518  -0.243 -0.185 66  ASP III CB  
10696 C CG  . ASP I 66  ? 2.184 3.125 1.859 0.505  -0.261 -0.178 66  ASP III CG  
10697 O OD1 . ASP I 66  ? 2.311 3.239 1.920 0.527  -0.261 -0.183 66  ASP III OD1 
10698 O OD2 . ASP I 66  ? 2.190 3.093 1.899 0.473  -0.274 -0.166 66  ASP III OD2 
10699 N N   . PHE I 67  ? 2.079 3.133 1.623 0.633  -0.218 -0.210 67  PHE III N   
10700 C CA  . PHE I 67  ? 2.140 3.150 1.597 0.685  -0.209 -0.216 67  PHE III CA  
10701 C C   . PHE I 67  ? 2.210 3.140 1.603 0.683  -0.219 -0.213 67  PHE III C   
10702 O O   . PHE I 67  ? 2.313 3.191 1.621 0.726  -0.210 -0.218 67  PHE III O   
10703 C CB  . PHE I 67  ? 2.189 3.294 1.631 0.730  -0.194 -0.224 67  PHE III CB  
10704 C CG  . PHE I 67  ? 2.234 3.429 1.703 0.714  -0.196 -0.226 67  PHE III CG  
10705 C CD1 . PHE I 67  ? 2.364 3.548 1.781 0.729  -0.197 -0.228 67  PHE III CD1 
10706 C CD2 . PHE I 67  ? 2.202 3.488 1.741 0.683  -0.195 -0.227 67  PHE III CD2 
10707 C CE1 . PHE I 67  ? 2.499 3.766 1.939 0.712  -0.198 -0.231 67  PHE III CE1 
10708 C CE2 . PHE I 67  ? 2.278 3.643 1.835 0.664  -0.196 -0.229 67  PHE III CE2 
10709 C CZ  . PHE I 67  ? 2.402 3.761 1.912 0.678  -0.198 -0.231 67  PHE III CZ  
10710 N N   . THR I 68  ? 2.154 3.066 1.579 0.634  -0.236 -0.205 68  THR III N   
10711 C CA  . THR I 68  ? 2.236 3.067 1.599 0.624  -0.247 -0.202 68  THR III CA  
10712 C C   . THR I 68  ? 2.300 3.040 1.661 0.588  -0.262 -0.192 68  THR III C   
10713 O O   . THR I 68  ? 2.494 3.143 1.775 0.590  -0.266 -0.191 68  THR III O   
10714 C CB  . THR I 68  ? 2.232 3.109 1.621 0.595  -0.259 -0.199 68  THR III CB  
10715 O OG1 . THR I 68  ? 2.172 3.076 1.647 0.546  -0.273 -0.189 68  THR III OG1 
10716 C CG2 . THR I 68  ? 2.252 3.227 1.640 0.625  -0.244 -0.208 68  THR III CG2 
10717 N N   . ARG I 69  ? 2.255 3.016 1.698 0.555  -0.268 -0.185 69  ARG III N   
10718 C CA  . ARG I 69  ? 2.287 2.978 1.737 0.519  -0.281 -0.175 69  ARG III CA  
10719 C C   . ARG I 69  ? 2.314 3.006 1.804 0.520  -0.271 -0.175 69  ARG III C   
10720 O O   . ARG I 69  ? 2.400 3.032 1.885 0.495  -0.277 -0.169 69  ARG III O   
10721 C CB  . ARG I 69  ? 2.237 2.949 1.754 0.469  -0.304 -0.161 69  ARG III CB  
10722 C CG  . ARG I 69  ? 2.363 3.063 1.839 0.458  -0.318 -0.158 69  ARG III CG  
10723 C CD  . ARG I 69  ? 2.543 3.142 1.924 0.453  -0.326 -0.157 69  ARG III CD  
10724 N NE  . ARG I 69  ? 2.631 3.215 1.965 0.445  -0.337 -0.157 69  ARG III NE  
10725 C CZ  . ARG I 69  ? 2.679 3.251 1.936 0.483  -0.322 -0.168 69  ARG III CZ  
10726 N NH1 . ARG I 69  ? 2.686 3.262 1.905 0.534  -0.298 -0.181 69  ARG III NH1 
10727 N NH2 . ARG I 69  ? 2.741 3.296 1.956 0.471  -0.332 -0.167 69  ARG III NH2 
10728 N N   . HIS I 70  ? 2.327 3.085 1.852 0.544  -0.254 -0.182 70  HIS III N   
10729 C CA  . HIS I 70  ? 2.300 3.056 1.844 0.555  -0.240 -0.186 70  HIS III CA  
10730 C C   . HIS I 70  ? 2.222 2.978 1.845 0.513  -0.245 -0.176 70  HIS III C   
10731 O O   . HIS I 70  ? 2.282 3.014 1.910 0.514  -0.235 -0.178 70  HIS III O   
10732 C CB  . HIS I 70  ? 2.397 3.072 1.846 0.588  -0.230 -0.192 70  HIS III CB  
10733 C CG  . HIS I 70  ? 2.453 3.162 1.855 0.644  -0.214 -0.203 70  HIS III CG  
10734 N ND1 . HIS I 70  ? 2.506 3.195 1.828 0.682  -0.211 -0.208 70  HIS III ND1 
10735 C CD2 . HIS I 70  ? 2.424 3.196 1.854 0.669  -0.200 -0.209 70  HIS III CD2 
10736 C CE1 . HIS I 70  ? 2.541 3.284 1.846 0.731  -0.197 -0.215 70  HIS III CE1 
10737 N NE2 . HIS I 70  ? 2.483 3.278 1.852 0.722  -0.191 -0.216 70  HIS III NE2 
10738 N N   . ASN I 71  ? 2.018 2.803 1.703 0.477  -0.261 -0.165 71  ASN III N   
10739 C CA  . ASN I 71  ? 1.913 2.698 1.670 0.442  -0.266 -0.154 71  ASN III CA  
10740 C C   . ASN I 71  ? 1.828 2.675 1.667 0.420  -0.273 -0.145 71  ASN III C   
10741 O O   . ASN I 71  ? 1.905 2.757 1.809 0.394  -0.277 -0.134 71  ASN III O   
10742 C CB  . ASN I 71  ? 1.996 2.716 1.730 0.412  -0.284 -0.143 71  ASN III CB  
10743 C CG  . ASN I 71  ? 2.004 2.718 1.720 0.395  -0.306 -0.136 71  ASN III CG  
10744 O OD1 . ASN I 71  ? 1.907 2.638 1.678 0.362  -0.324 -0.121 71  ASN III OD1 
10745 N ND2 . ASN I 71  ? 2.125 2.813 1.760 0.419  -0.305 -0.145 71  ASN III ND2 
10746 N N   . GLY I 72  ? 1.778 2.672 1.615 0.430  -0.272 -0.150 72  GLY III N   
10747 C CA  . GLY I 72  ? 1.776 2.717 1.675 0.408  -0.278 -0.142 72  GLY III CA  
10748 C C   . GLY I 72  ? 1.897 2.830 1.787 0.389  -0.301 -0.133 72  GLY III C   
10749 O O   . GLY I 72  ? 1.890 2.855 1.822 0.371  -0.308 -0.125 72  GLY III O   
10750 N N   . THR I 73  ? 1.937 2.822 1.765 0.390  -0.313 -0.132 73  THR III N   
10751 C CA  . THR I 73  ? 1.942 2.811 1.753 0.369  -0.336 -0.123 73  THR III CA  
10752 C C   . THR I 73  ? 2.045 2.958 1.838 0.378  -0.332 -0.130 73  THR III C   
10753 O O   . THR I 73  ? 2.115 3.065 1.953 0.360  -0.337 -0.124 73  THR III O   
10754 C CB  . THR I 73  ? 1.949 2.748 1.685 0.368  -0.346 -0.123 73  THR III CB  
10755 O OG1 . THR I 73  ? 1.854 2.618 1.612 0.349  -0.352 -0.114 73  THR III OG1 
10756 C CG2 . THR I 73  ? 2.094 2.873 1.801 0.345  -0.370 -0.114 73  THR III CG2 
10757 N N   . GLY I 74  ? 2.083 2.986 1.803 0.403  -0.325 -0.143 74  GLY III N   
10758 C CA  . GLY I 74  ? 2.218 3.170 1.921 0.409  -0.321 -0.150 74  GLY III CA  
10759 C C   . GLY I 74  ? 2.336 3.333 2.010 0.448  -0.297 -0.166 74  GLY III C   
10760 O O   . GLY I 74  ? 2.295 3.259 1.920 0.480  -0.288 -0.173 74  GLY III O   
10761 N N   . GLY I 75  ? 2.317 3.387 2.011 0.446  -0.289 -0.172 75  GLY III N   
10762 C CA  . GLY I 75  ? 2.283 3.420 1.962 0.477  -0.268 -0.186 75  GLY III CA  
10763 C C   . GLY I 75  ? 2.471 3.639 2.106 0.482  -0.268 -0.192 75  GLY III C   
10764 O O   . GLY I 75  ? 2.566 3.704 2.196 0.454  -0.285 -0.184 75  GLY III O   
10765 N N   . LYS I 76  ? 2.508 3.735 2.110 0.517  -0.252 -0.204 76  LYS III N   
10766 C CA  . LYS I 76  ? 2.498 3.765 2.066 0.517  -0.251 -0.209 76  LYS III CA  
10767 C C   . LYS I 76  ? 2.362 3.746 1.949 0.521  -0.235 -0.218 76  LYS III C   
10768 O O   . LYS I 76  ? 2.487 3.920 2.083 0.547  -0.221 -0.224 76  LYS III O   
10769 C CB  . LYS I 76  ? 2.547 3.773 2.037 0.562  -0.244 -0.214 76  LYS III CB  
10770 C CG  . LYS I 76  ? 2.716 3.991 2.161 0.579  -0.235 -0.222 76  LYS III CG  
10771 C CD  . LYS I 76  ? 2.797 4.010 2.158 0.629  -0.227 -0.226 76  LYS III CD  
10772 C CE  . LYS I 76  ? 2.945 4.200 2.254 0.651  -0.215 -0.234 76  LYS III CE  
10773 N NZ  . LYS I 76  ? 3.043 4.309 2.366 0.600  -0.227 -0.231 76  LYS III NZ  
10774 N N   . SER I 77  ? 2.441 3.866 2.024 0.493  -0.237 -0.220 77  SER III N   
10775 C CA  . SER I 77  ? 2.448 3.987 2.039 0.488  -0.223 -0.229 77  SER III CA  
10776 C C   . SER I 77  ? 2.582 4.172 2.121 0.533  -0.209 -0.238 77  SER III C   
10777 O O   . SER I 77  ? 2.766 4.291 2.255 0.565  -0.211 -0.237 77  SER III O   
10778 C CB  . SER I 77  ? 2.479 4.029 2.086 0.430  -0.232 -0.225 77  SER III CB  
10779 O OG  . SER I 77  ? 2.499 4.153 2.094 0.424  -0.219 -0.235 77  SER III OG  
10780 N N   . ILE I 78  ? 2.520 4.230 2.069 0.535  -0.195 -0.246 78  ILE III N   
10781 C CA  . ILE I 78  ? 2.577 4.355 2.082 0.577  -0.180 -0.255 78  ILE III CA  
10782 C C   . ILE I 78  ? 2.680 4.444 2.154 0.550  -0.183 -0.255 78  ILE III C   
10783 O O   . ILE I 78  ? 2.880 4.687 2.312 0.584  -0.170 -0.262 78  ILE III O   
10784 C CB  . ILE I 78  ? 2.514 4.441 2.042 0.590  -0.163 -0.262 78  ILE III CB  
10785 C CG1 . ILE I 78  ? 2.484 4.482 2.045 0.522  -0.165 -0.264 78  ILE III CG1 
10786 C CG2 . ILE I 78  ? 2.499 4.434 2.045 0.626  -0.159 -0.261 78  ILE III CG2 
10787 C CD1 . ILE I 78  ? 2.490 4.647 2.064 0.526  -0.148 -0.272 78  ILE III CD1 
10788 N N   . TYR I 79  ? 2.640 4.343 2.131 0.493  -0.201 -0.248 79  TYR III N   
10789 C CA  . TYR I 79  ? 2.632 4.312 2.092 0.460  -0.207 -0.248 79  TYR III CA  
10790 C C   . TYR I 79  ? 2.655 4.203 2.080 0.463  -0.224 -0.239 79  TYR III C   
10791 O O   . TYR I 79  ? 2.723 4.232 2.120 0.433  -0.234 -0.236 79  TYR III O   
10792 C CB  . TYR I 79  ? 2.597 4.299 2.093 0.392  -0.216 -0.244 79  TYR III CB  
10793 C CG  . TYR I 79  ? 2.607 4.428 2.136 0.379  -0.201 -0.252 79  TYR III CG  
10794 C CD1 . TYR I 79  ? 2.703 4.648 2.218 0.395  -0.182 -0.263 79  TYR III CD1 
10795 C CD2 . TYR I 79  ? 2.640 4.452 2.214 0.353  -0.205 -0.247 79  TYR III CD2 
10796 C CE1 . TYR I 79  ? 2.683 4.743 2.229 0.377  -0.170 -0.269 79  TYR III CE1 
10797 C CE2 . TYR I 79  ? 2.553 4.466 2.151 0.336  -0.192 -0.254 79  TYR III CE2 
10798 C CZ  . TYR I 79  ? 2.586 4.625 2.170 0.346  -0.176 -0.264 79  TYR III CZ  
10799 O OH  . TYR I 79  ? 2.561 4.706 2.167 0.324  -0.165 -0.270 79  TYR III OH  
10800 N N   . GLY I 80  ? 2.785 4.261 2.212 0.491  -0.230 -0.234 80  GLY III N   
10801 C CA  . GLY I 80  ? 2.917 4.269 2.317 0.484  -0.248 -0.225 80  GLY III CA  
10802 C C   . GLY I 80  ? 2.979 4.287 2.436 0.440  -0.269 -0.212 80  GLY III C   
10803 O O   . GLY I 80  ? 2.946 4.191 2.399 0.404  -0.289 -0.202 80  GLY III O   
10804 N N   . GLU I 81  ? 3.134 4.470 2.641 0.446  -0.263 -0.211 81  GLU III N   
10805 C CA  . GLU I 81  ? 2.953 4.254 2.518 0.407  -0.279 -0.199 81  GLU III CA  
10806 C C   . GLU I 81  ? 2.955 4.293 2.524 0.364  -0.283 -0.199 81  GLU III C   
10807 O O   . GLU I 81  ? 3.226 4.649 2.785 0.366  -0.267 -0.210 81  GLU III O   
10808 C CB  . GLU I 81  ? 2.903 4.100 2.463 0.401  -0.299 -0.187 81  GLU III CB  
10809 C CG  . GLU I 81  ? 2.920 4.087 2.539 0.389  -0.307 -0.177 81  GLU III CG  
10810 C CD  . GLU I 81  ? 2.929 4.093 2.598 0.344  -0.321 -0.165 81  GLU III CD  
10811 O OE1 . GLU I 81  ? 3.008 4.162 2.657 0.318  -0.333 -0.160 81  GLU III OE1 
10812 O OE2 . GLU I 81  ? 2.906 4.070 2.628 0.337  -0.319 -0.159 81  GLU III OE2 
10813 N N   . LYS I 82  ? 2.762 4.045 2.348 0.324  -0.304 -0.185 82  LYS III N   
10814 C CA  . LYS I 82  ? 2.709 4.020 2.287 0.284  -0.307 -0.185 82  LYS III CA  
10815 C C   . LYS I 82  ? 2.688 4.086 2.287 0.266  -0.289 -0.194 82  LYS III C   
10816 O O   . LYS I 82  ? 2.840 4.271 2.413 0.238  -0.286 -0.198 82  LYS III O   
10817 C CB  . LYS I 82  ? 2.760 4.080 2.274 0.295  -0.303 -0.193 82  LYS III CB  
10818 C CG  . LYS I 82  ? 2.730 4.029 2.208 0.258  -0.314 -0.189 82  LYS III CG  
10819 C CD  . LYS I 82  ? 2.709 3.918 2.192 0.226  -0.344 -0.171 82  LYS III CD  
10820 C CE  . LYS I 82  ? 2.736 3.935 2.170 0.193  -0.351 -0.170 82  LYS III CE  
10821 N NZ  . LYS I 82  ? 2.779 4.038 2.218 0.160  -0.340 -0.176 82  LYS III NZ  
10822 N N   . PHE I 83  ? 2.647 4.083 2.284 0.272  -0.277 -0.198 83  PHE III N   
10823 C CA  . PHE I 83  ? 2.684 4.186 2.319 0.235  -0.266 -0.204 83  PHE III CA  
10824 C C   . PHE I 83  ? 2.589 4.050 2.254 0.195  -0.272 -0.194 83  PHE III C   
10825 O O   . PHE I 83  ? 2.538 3.940 2.238 0.202  -0.280 -0.184 83  PHE III O   
10826 C CB  . PHE I 83  ? 2.542 4.153 2.180 0.254  -0.242 -0.219 83  PHE III CB  
10827 C CG  . PHE I 83  ? 2.444 4.066 2.122 0.271  -0.234 -0.220 83  PHE III CG  
10828 C CD1 . PHE I 83  ? 2.466 4.052 2.176 0.241  -0.235 -0.214 83  PHE III CD1 
10829 C CD2 . PHE I 83  ? 2.461 4.131 2.137 0.320  -0.223 -0.228 83  PHE III CD2 
10830 C CE1 . PHE I 83  ? 2.546 4.144 2.287 0.256  -0.225 -0.215 83  PHE III CE1 
10831 C CE2 . PHE I 83  ? 2.579 4.260 2.286 0.335  -0.215 -0.229 83  PHE III CE2 
10832 C CZ  . PHE I 83  ? 2.615 4.260 2.354 0.302  -0.216 -0.223 83  PHE III CZ  
10833 N N   . GLU I 84  ? 2.681 4.174 2.324 0.153  -0.266 -0.198 84  GLU III N   
10834 C CA  . GLU I 84  ? 2.710 4.156 2.358 0.109  -0.271 -0.190 84  GLU III CA  
10835 C C   . GLU I 84  ? 2.777 4.238 2.455 0.104  -0.256 -0.192 84  GLU III C   
10836 O O   . GLU I 84  ? 2.774 4.305 2.465 0.125  -0.241 -0.204 84  GLU III O   
10837 C CB  . GLU I 84  ? 2.839 4.306 2.439 0.064  -0.269 -0.194 84  GLU III CB  
10838 C CG  . GLU I 84  ? 2.908 4.481 2.487 0.044  -0.248 -0.211 84  GLU III CG  
10839 C CD  . GLU I 84  ? 2.967 4.548 2.495 -0.007 -0.248 -0.214 84  GLU III CD  
10840 O OE1 . GLU I 84  ? 2.937 4.446 2.444 -0.016 -0.265 -0.203 84  GLU III OE1 
10841 O OE2 . GLU I 84  ? 2.949 4.608 2.455 -0.041 -0.231 -0.226 84  GLU III OE2 
10842 N N   . ASP I 85  ? 2.789 4.181 2.475 0.077  -0.260 -0.181 85  ASP III N   
10843 C CA  . ASP I 85  ? 2.862 4.259 2.560 0.060  -0.243 -0.185 85  ASP III CA  
10844 C C   . ASP I 85  ? 2.914 4.379 2.567 0.016  -0.228 -0.198 85  ASP III C   
10845 O O   . ASP I 85  ? 2.915 4.355 2.527 -0.023 -0.232 -0.196 85  ASP III O   
10846 C CB  . ASP I 85  ? 2.802 4.099 2.512 0.047  -0.250 -0.169 85  ASP III CB  
10847 C CG  . ASP I 85  ? 2.652 3.896 2.413 0.087  -0.264 -0.154 85  ASP III CG  
10848 O OD1 . ASP I 85  ? 2.498 3.772 2.290 0.121  -0.258 -0.160 85  ASP III OD1 
10849 O OD2 . ASP I 85  ? 2.655 3.828 2.423 0.085  -0.282 -0.137 85  ASP III OD2 
10850 N N   . GLU I 86  ? 2.888 4.442 2.547 0.020  -0.210 -0.212 86  GLU III N   
10851 C CA  . GLU I 86  ? 2.939 4.581 2.557 -0.021 -0.197 -0.225 86  GLU III CA  
10852 C C   . GLU I 86  ? 3.090 4.680 2.673 -0.080 -0.189 -0.224 86  GLU III C   
10853 O O   . GLU I 86  ? 3.219 4.809 2.754 -0.127 -0.188 -0.226 86  GLU III O   
10854 C CB  . GLU I 86  ? 2.763 4.522 2.397 -0.000 -0.183 -0.239 86  GLU III CB  
10855 C CG  . GLU I 86  ? 2.721 4.589 2.316 -0.044 -0.170 -0.251 86  GLU III CG  
10856 C CD  . GLU I 86  ? 2.691 4.694 2.304 -0.016 -0.159 -0.262 86  GLU III CD  
10857 O OE1 . GLU I 86  ? 2.649 4.651 2.298 0.035  -0.160 -0.261 86  GLU III OE1 
10858 O OE2 . GLU I 86  ? 2.763 4.876 2.352 -0.043 -0.150 -0.272 86  GLU III OE2 
10859 N N   . ASN I 87  ? 3.099 4.634 2.701 -0.077 -0.181 -0.220 87  ASN III N   
10860 C CA  . ASN I 87  ? 3.133 4.593 2.696 -0.125 -0.172 -0.216 87  ASN III CA  
10861 C C   . ASN I 87  ? 3.139 4.526 2.739 -0.098 -0.167 -0.208 87  ASN III C   
10862 O O   . ASN I 87  ? 3.186 4.595 2.838 -0.051 -0.169 -0.208 87  ASN III O   
10863 C CB  . ASN I 87  ? 3.095 4.628 2.612 -0.180 -0.152 -0.231 87  ASN III CB  
10864 C CG  . ASN I 87  ? 3.144 4.768 2.623 -0.214 -0.153 -0.241 87  ASN III CG  
10865 O OD1 . ASN I 87  ? 3.124 4.874 2.614 -0.210 -0.146 -0.253 87  ASN III OD1 
10866 N ND2 . ASN I 87  ? 3.296 4.861 2.732 -0.246 -0.160 -0.236 87  ASN III ND2 
10867 N N   . PHE I 88  ? 3.058 4.351 2.625 -0.129 -0.159 -0.202 88  PHE III N   
10868 C CA  . PHE I 88  ? 3.031 4.247 2.622 -0.111 -0.149 -0.194 88  PHE III CA  
10869 C C   . PHE I 88  ? 3.078 4.272 2.613 -0.161 -0.125 -0.203 88  PHE III C   
10870 O O   . PHE I 88  ? 3.260 4.362 2.790 -0.159 -0.113 -0.196 88  PHE III O   
10871 C CB  . PHE I 88  ? 3.039 4.143 2.646 -0.088 -0.162 -0.174 88  PHE III CB  
10872 C CG  . PHE I 88  ? 2.965 4.081 2.628 -0.041 -0.187 -0.164 88  PHE III CG  
10873 C CD1 . PHE I 88  ? 2.906 4.079 2.625 0.001  -0.189 -0.168 88  PHE III CD1 
10874 C CD2 . PHE I 88  ? 3.004 4.068 2.657 -0.041 -0.208 -0.149 88  PHE III CD2 
10875 C CE1 . PHE I 88  ? 2.854 4.027 2.613 0.039  -0.210 -0.159 88  PHE III CE1 
10876 C CE2 . PHE I 88  ? 2.928 4.000 2.627 -0.003 -0.231 -0.139 88  PHE III CE2 
10877 C CZ  . PHE I 88  ? 2.835 3.960 2.585 0.036  -0.231 -0.145 88  PHE III CZ  
10878 N N   . ILE I 89  ? 3.017 4.291 2.505 -0.209 -0.117 -0.218 89  ILE III N   
10879 C CA  . ILE I 89  ? 2.953 4.208 2.376 -0.267 -0.094 -0.227 89  ILE III CA  
10880 C C   . ILE I 89  ? 2.965 4.222 2.417 -0.248 -0.079 -0.231 89  ILE III C   
10881 O O   . ILE I 89  ? 3.091 4.260 2.505 -0.270 -0.061 -0.230 89  ILE III O   
10882 C CB  . ILE I 89  ? 2.961 4.327 2.338 -0.322 -0.091 -0.242 89  ILE III CB  
10883 C CG1 . ILE I 89  ? 3.044 4.410 2.396 -0.336 -0.106 -0.238 89  ILE III CG1 
10884 C CG2 . ILE I 89  ? 3.052 4.386 2.347 -0.393 -0.069 -0.251 89  ILE III CG2 
10885 C CD1 . ILE I 89  ? 3.066 4.534 2.366 -0.397 -0.100 -0.252 89  ILE III CD1 
10886 N N   . LEU I 90  ? 2.862 4.212 2.376 -0.205 -0.085 -0.235 90  LEU III N   
10887 C CA  . LEU I 90  ? 2.719 4.079 2.259 -0.187 -0.072 -0.240 90  LEU III CA  
10888 C C   . LEU I 90  ? 2.689 3.937 2.267 -0.144 -0.069 -0.227 90  LEU III C   
10889 O O   . LEU I 90  ? 2.711 3.910 2.323 -0.110 -0.084 -0.214 90  LEU III O   
10890 C CB  . LEU I 90  ? 2.460 3.945 2.050 -0.148 -0.080 -0.246 90  LEU III CB  
10891 C CG  . LEU I 90  ? 2.400 4.020 1.962 -0.183 -0.079 -0.260 90  LEU III CG  
10892 C CD1 . LEU I 90  ? 2.239 3.968 1.852 -0.131 -0.086 -0.264 90  LEU III CD1 
10893 C CD2 . LEU I 90  ? 2.400 4.023 1.903 -0.247 -0.059 -0.269 90  LEU III CD2 
10894 N N   . LYS I 91  ? 2.761 3.971 2.333 -0.149 -0.049 -0.230 91  LYS III N   
10895 C CA  . LYS I 91  ? 2.852 3.961 2.457 -0.112 -0.041 -0.219 91  LYS III CA  
10896 C C   . LYS I 91  ? 2.923 4.073 2.580 -0.074 -0.036 -0.223 91  LYS III C   
10897 O O   . LYS I 91  ? 3.021 4.254 2.667 -0.089 -0.030 -0.236 91  LYS III O   
10898 C CB  . LYS I 91  ? 2.901 3.900 2.439 -0.152 -0.017 -0.218 91  LYS III CB  
10899 C CG  . LYS I 91  ? 2.890 3.766 2.433 -0.128 -0.016 -0.200 91  LYS III CG  
10900 C CD  . LYS I 91  ? 2.884 3.737 2.390 -0.149 -0.033 -0.193 91  LYS III CD  
10901 C CE  . LYS I 91  ? 2.885 3.612 2.386 -0.127 -0.032 -0.174 91  LYS III CE  
10902 N NZ  . LYS I 91  ? 2.848 3.539 2.297 -0.154 -0.046 -0.167 91  LYS III NZ  
10903 N N   . HIS I 92  ? 3.004 4.101 2.719 -0.025 -0.039 -0.212 92  HIS III N   
10904 C CA  . HIS I 92  ? 2.889 4.003 2.654 0.014  -0.033 -0.214 92  HIS III CA  
10905 C C   . HIS I 92  ? 2.936 3.989 2.673 -0.005 -0.003 -0.218 92  HIS III C   
10906 O O   . HIS I 92  ? 3.007 3.970 2.760 0.013  0.009  -0.209 92  HIS III O   
10907 C CB  . HIS I 92  ? 2.730 3.813 2.563 0.066  -0.047 -0.199 92  HIS III CB  
10908 C CG  . HIS I 92  ? 2.602 3.738 2.458 0.085  -0.075 -0.195 92  HIS III CG  
10909 N ND1 . HIS I 92  ? 2.617 3.730 2.456 0.072  -0.090 -0.187 92  HIS III ND1 
10910 C CD2 . HIS I 92  ? 2.409 3.613 2.293 0.115  -0.090 -0.199 92  HIS III CD2 
10911 C CE1 . HIS I 92  ? 2.499 3.665 2.358 0.092  -0.112 -0.186 92  HIS III CE1 
10912 N NE2 . HIS I 92  ? 2.349 3.570 2.234 0.119  -0.112 -0.193 92  HIS III NE2 
10913 N N   . THR I 93  ? 2.742 3.847 2.437 -0.040 0.008  -0.232 93  THR III N   
10914 C CA  . THR I 93  ? 2.743 3.787 2.388 -0.073 0.037  -0.239 93  THR III CA  
10915 C C   . THR I 93  ? 2.593 3.634 2.269 -0.046 0.050  -0.242 93  THR III C   
10916 O O   . THR I 93  ? 2.528 3.503 2.166 -0.068 0.076  -0.246 93  THR III O   
10917 C CB  . THR I 93  ? 2.878 3.977 2.449 -0.138 0.042  -0.252 93  THR III CB  
10918 O OG1 . THR I 93  ? 2.883 4.099 2.473 -0.132 0.034  -0.261 93  THR III OG1 
10919 C CG2 . THR I 93  ? 2.876 3.998 2.415 -0.168 0.027  -0.250 93  THR III CG2 
10920 N N   . GLY I 94  ? 2.450 3.551 2.188 -0.000 0.035  -0.241 94  GLY III N   
10921 C CA  . GLY I 94  ? 2.202 3.300 1.962 0.022  0.048  -0.245 94  GLY III CA  
10922 C C   . GLY I 94  ? 2.104 3.283 1.911 0.064  0.029  -0.246 94  GLY III C   
10923 O O   . GLY I 94  ? 2.137 3.371 1.966 0.084  0.006  -0.243 94  GLY III O   
10924 N N   . PRO I 95  ? 2.021 3.200 1.836 0.079  0.041  -0.251 95  PRO III N   
10925 C CA  . PRO I 95  ? 1.943 3.190 1.789 0.119  0.025  -0.253 95  PRO III CA  
10926 C C   . PRO I 95  ? 2.011 3.370 1.834 0.111  0.007  -0.259 95  PRO III C   
10927 O O   . PRO I 95  ? 2.115 3.515 1.892 0.067  0.013  -0.266 95  PRO III O   
10928 C CB  . PRO I 95  ? 1.896 3.115 1.736 0.123  0.045  -0.258 95  PRO III CB  
10929 C CG  . PRO I 95  ? 1.979 3.100 1.803 0.098  0.071  -0.257 95  PRO III CG  
10930 C CD  . PRO I 95  ? 2.033 3.144 1.822 0.060  0.070  -0.255 95  PRO III CD  
10931 N N   . GLY I 96  ? 1.916 3.324 1.768 0.153  -0.013 -0.256 96  GLY III N   
10932 C CA  . GLY I 96  ? 1.861 3.379 1.696 0.159  -0.028 -0.261 96  GLY III CA  
10933 C C   . GLY I 96  ? 1.952 3.504 1.786 0.152  -0.044 -0.258 96  GLY III C   
10934 O O   . GLY I 96  ? 2.116 3.759 1.946 0.168  -0.057 -0.260 96  GLY III O   
10935 N N   . ILE I 97  ? 1.933 3.414 1.771 0.130  -0.041 -0.252 97  ILE III N   
10936 C CA  . ILE I 97  ? 1.920 3.420 1.754 0.121  -0.056 -0.248 97  ILE III CA  
10937 C C   . ILE I 97  ? 1.817 3.333 1.684 0.172  -0.075 -0.243 97  ILE III C   
10938 O O   . ILE I 97  ? 1.622 3.078 1.522 0.206  -0.077 -0.237 97  ILE III O   
10939 C CB  . ILE I 97  ? 1.924 3.329 1.753 0.093  -0.049 -0.241 97  ILE III CB  
10940 C CG1 . ILE I 97  ? 2.022 3.407 1.798 0.037  -0.029 -0.248 97  ILE III CG1 
10941 C CG2 . ILE I 97  ? 1.986 3.396 1.815 0.091  -0.067 -0.235 97  ILE III CG2 
10942 C CD1 . ILE I 97  ? 2.055 3.540 1.788 -0.004 -0.033 -0.257 97  ILE III CD1 
10943 N N   . LEU I 98  ? 1.900 3.495 1.754 0.177  -0.088 -0.246 98  LEU III N   
10944 C CA  . LEU I 98  ? 1.823 3.431 1.695 0.222  -0.105 -0.242 98  LEU III CA  
10945 C C   . LEU I 98  ? 1.854 3.439 1.722 0.205  -0.117 -0.236 98  LEU III C   
10946 O O   . LEU I 98  ? 1.951 3.583 1.791 0.168  -0.116 -0.240 98  LEU III O   
10947 C CB  . LEU I 98  ? 1.853 3.568 1.709 0.249  -0.110 -0.249 98  LEU III CB  
10948 C CG  . LEU I 98  ? 1.746 3.458 1.611 0.307  -0.122 -0.246 98  LEU III CG  
10949 C CD1 . LEU I 98  ? 1.687 3.296 1.577 0.329  -0.123 -0.239 98  LEU III CD1 
10950 C CD2 . LEU I 98  ? 1.915 3.717 1.763 0.343  -0.121 -0.252 98  LEU III CD2 
10951 N N   . SER I 99  ? 1.816 3.331 1.710 0.228  -0.128 -0.226 99  SER III N   
10952 C CA  . SER I 99  ? 1.823 3.305 1.714 0.212  -0.141 -0.218 99  SER III CA  
10953 C C   . SER I 99  ? 1.769 3.228 1.677 0.251  -0.158 -0.212 99  SER III C   
10954 O O   . SER I 99  ? 1.644 3.080 1.570 0.285  -0.159 -0.210 99  SER III O   
10955 C CB  . SER I 99  ? 1.825 3.220 1.726 0.184  -0.135 -0.209 99  SER III CB  
10956 O OG  . SER I 99  ? 1.971 3.326 1.873 0.176  -0.150 -0.199 99  SER III OG  
10957 N N   . MET I 100 ? 1.834 3.295 1.727 0.242  -0.172 -0.208 100 MET III N   
10958 C CA  . MET I 100 ? 1.764 3.200 1.661 0.272  -0.189 -0.202 100 MET III CA  
10959 C C   . MET I 100 ? 1.674 3.020 1.605 0.274  -0.199 -0.187 100 MET III C   
10960 O O   . MET I 100 ? 1.649 2.954 1.595 0.249  -0.197 -0.179 100 MET III O   
10961 C CB  . MET I 100 ? 1.773 3.239 1.639 0.257  -0.200 -0.203 100 MET III CB  
10962 C CG  . MET I 100 ? 1.771 3.329 1.608 0.275  -0.195 -0.215 100 MET III CG  
10963 S SD  . MET I 100 ? 1.708 3.261 1.540 0.338  -0.199 -0.217 100 MET III SD  
10964 C CE  . MET I 100 ? 1.905 3.367 1.737 0.340  -0.220 -0.204 100 MET III CE  
10965 N N   . ALA I 101 ? 1.639 2.957 1.581 0.305  -0.210 -0.182 101 ALA III N   
10966 C CA  . ALA I 101 ? 1.653 2.901 1.627 0.305  -0.223 -0.167 101 ALA III CA  
10967 C C   . ALA I 101 ? 1.694 2.926 1.652 0.291  -0.244 -0.158 101 ALA III C   
10968 O O   . ALA I 101 ? 1.774 3.043 1.694 0.293  -0.248 -0.166 101 ALA III O   
10969 C CB  . ALA I 101 ? 1.607 2.826 1.593 0.336  -0.226 -0.165 101 ALA III CB  
10970 N N   . ASN I 102 ? 1.704 2.884 1.691 0.278  -0.256 -0.142 102 ASN III N   
10971 C CA  . ASN I 102 ? 1.796 2.954 1.767 0.265  -0.279 -0.132 102 ASN III CA  
10972 C C   . ASN I 102 ? 1.894 2.999 1.907 0.263  -0.296 -0.111 102 ASN III C   
10973 O O   . ASN I 102 ? 1.956 3.039 2.006 0.259  -0.288 -0.103 102 ASN III O   
10974 C CB  . ASN I 102 ? 1.934 3.107 1.877 0.234  -0.276 -0.134 102 ASN III CB  
10975 C CG  . ASN I 102 ? 1.927 3.067 1.893 0.216  -0.266 -0.126 102 ASN III CG  
10976 O OD1 . ASN I 102 ? 1.964 3.123 1.925 0.208  -0.244 -0.136 102 ASN III OD1 
10977 N ND2 . ASN I 102 ? 1.972 3.061 1.955 0.209  -0.283 -0.108 102 ASN III ND2 
10978 N N   . ALA I 103 ? 1.947 3.032 1.951 0.268  -0.318 -0.103 103 ALA III N   
10979 C CA  . ALA I 103 ? 1.942 2.987 1.985 0.265  -0.338 -0.082 103 ALA III CA  
10980 C C   . ALA I 103 ? 2.019 3.044 2.072 0.244  -0.349 -0.067 103 ALA III C   
10981 O O   . ALA I 103 ? 2.005 3.006 2.103 0.245  -0.360 -0.048 103 ALA III O   
10982 C CB  . ALA I 103 ? 1.796 2.824 1.815 0.267  -0.360 -0.078 103 ALA III CB  
10983 N N   . GLY I 104 ? 2.144 3.179 2.152 0.227  -0.347 -0.075 104 GLY III N   
10984 C CA  . GLY I 104 ? 2.253 3.261 2.250 0.205  -0.359 -0.062 104 GLY III CA  
10985 C C   . GLY I 104 ? 2.364 3.397 2.308 0.185  -0.345 -0.078 104 GLY III C   
10986 O O   . GLY I 104 ? 2.377 3.455 2.299 0.190  -0.329 -0.097 104 GLY III O   
10987 N N   . PRO I 105 ? 2.399 3.402 2.318 0.160  -0.350 -0.070 105 PRO III N   
10988 C CA  . PRO I 105 ? 2.364 3.393 2.225 0.133  -0.338 -0.085 105 PRO III CA  
10989 C C   . PRO I 105 ? 2.381 3.452 2.208 0.134  -0.345 -0.097 105 PRO III C   
10990 O O   . PRO I 105 ? 2.442 3.491 2.263 0.138  -0.368 -0.088 105 PRO III O   
10991 C CB  . PRO I 105 ? 2.423 3.397 2.259 0.107  -0.350 -0.070 105 PRO III CB  
10992 C CG  . PRO I 105 ? 2.499 3.424 2.384 0.126  -0.366 -0.046 105 PRO III CG  
10993 C CD  . PRO I 105 ? 2.451 3.400 2.388 0.156  -0.370 -0.045 105 PRO III CD  
10994 N N   . ASN I 106 ? 2.446 3.577 2.246 0.130  -0.324 -0.118 106 ASN III N   
10995 C CA  . ASN I 106 ? 2.486 3.666 2.247 0.133  -0.324 -0.131 106 ASN III CA  
10996 C C   . ASN I 106 ? 2.373 3.546 2.146 0.167  -0.335 -0.130 106 ASN III C   
10997 O O   . ASN I 106 ? 2.298 3.463 2.039 0.168  -0.348 -0.129 106 ASN III O   
10998 C CB  . ASN I 106 ? 2.517 3.683 2.229 0.100  -0.335 -0.128 106 ASN III CB  
10999 C CG  . ASN I 106 ? 2.630 3.790 2.318 0.061  -0.325 -0.130 106 ASN III CG  
11000 O OD1 . ASN I 106 ? 2.756 3.969 2.435 0.050  -0.302 -0.145 106 ASN III OD1 
11001 N ND2 . ASN I 106 ? 2.581 3.675 2.251 0.039  -0.341 -0.114 106 ASN III ND2 
11002 N N   . THR I 107 ? 2.310 3.481 2.124 0.194  -0.328 -0.129 107 THR III N   
11003 C CA  . THR I 107 ? 2.207 3.365 2.026 0.225  -0.335 -0.129 107 THR III CA  
11004 C C   . THR I 107 ? 2.215 3.415 2.043 0.253  -0.313 -0.144 107 THR III C   
11005 O O   . THR I 107 ? 2.223 3.402 2.071 0.277  -0.314 -0.141 107 THR III O   
11006 C CB  . THR I 107 ? 2.140 3.238 2.000 0.226  -0.355 -0.109 107 THR III CB  
11007 O OG1 . THR I 107 ? 2.035 3.129 1.944 0.228  -0.343 -0.105 107 THR III OG1 
11008 C CG2 . THR I 107 ? 2.348 3.407 2.197 0.201  -0.380 -0.092 107 THR III CG2 
11009 N N   . ASN I 108 ? 2.219 3.483 2.032 0.247  -0.294 -0.158 108 ASN III N   
11010 C CA  . ASN I 108 ? 2.117 3.435 1.932 0.272  -0.274 -0.172 108 ASN III CA  
11011 C C   . ASN I 108 ? 2.170 3.505 1.951 0.310  -0.273 -0.180 108 ASN III C   
11012 O O   . ASN I 108 ? 2.344 3.686 2.086 0.309  -0.279 -0.182 108 ASN III O   
11013 C CB  . ASN I 108 ? 2.058 3.446 1.860 0.249  -0.257 -0.183 108 ASN III CB  
11014 C CG  . ASN I 108 ? 2.086 3.442 1.906 0.212  -0.254 -0.176 108 ASN III CG  
11015 O OD1 . ASN I 108 ? 2.135 3.468 1.988 0.216  -0.246 -0.173 108 ASN III OD1 
11016 N ND2 . ASN I 108 ? 2.139 3.486 1.933 0.176  -0.261 -0.173 108 ASN III ND2 
11017 N N   . GLY I 109 ? 2.120 3.454 1.910 0.343  -0.264 -0.184 109 GLY III N   
11018 C CA  . GLY I 109 ? 2.133 3.477 1.882 0.383  -0.260 -0.192 109 GLY III CA  
11019 C C   . GLY I 109 ? 2.151 3.559 1.894 0.415  -0.240 -0.204 109 GLY III C   
11020 O O   . GLY I 109 ? 2.133 3.625 1.872 0.410  -0.229 -0.213 109 GLY III O   
11021 N N   . SER I 110 ? 2.146 3.518 1.888 0.448  -0.237 -0.204 110 SER III N   
11022 C CA  . SER I 110 ? 1.990 3.412 1.726 0.482  -0.220 -0.214 110 SER III CA  
11023 C C   . SER I 110 ? 1.993 3.382 1.766 0.478  -0.216 -0.210 110 SER III C   
11024 O O   . SER I 110 ? 2.017 3.411 1.777 0.511  -0.206 -0.215 110 SER III O   
11025 C CB  . SER I 110 ? 2.057 3.463 1.737 0.534  -0.217 -0.218 110 SER III CB  
11026 O OG  . SER I 110 ? 2.172 3.475 1.835 0.539  -0.228 -0.211 110 SER III OG  
11027 N N   . GLN I 111 ? 1.916 3.271 1.733 0.440  -0.222 -0.202 111 GLN III N   
11028 C CA  . GLN I 111 ? 1.728 3.049 1.581 0.436  -0.216 -0.198 111 GLN III CA  
11029 C C   . GLN I 111 ? 1.664 3.026 1.549 0.406  -0.204 -0.201 111 GLN III C   
11030 O O   . GLN I 111 ? 1.651 3.025 1.544 0.373  -0.208 -0.198 111 GLN III O   
11031 C CB  . GLN I 111 ? 1.648 2.888 1.527 0.423  -0.230 -0.185 111 GLN III CB  
11032 C CG  . GLN I 111 ? 1.708 2.895 1.547 0.448  -0.239 -0.183 111 GLN III CG  
11033 C CD  . GLN I 111 ? 1.686 2.803 1.550 0.431  -0.254 -0.170 111 GLN III CD  
11034 O OE1 . GLN I 111 ? 1.598 2.706 1.516 0.412  -0.252 -0.162 111 GLN III OE1 
11035 N NE2 . GLN I 111 ? 1.801 2.871 1.626 0.436  -0.268 -0.166 111 GLN III NE2 
11036 N N   . PHE I 112 ? 1.603 2.980 1.498 0.416  -0.190 -0.206 112 PHE III N   
11037 C CA  . PHE I 112 ? 1.551 2.966 1.462 0.389  -0.176 -0.210 112 PHE III CA  
11038 C C   . PHE I 112 ? 1.546 2.909 1.489 0.385  -0.166 -0.207 112 PHE III C   
11039 O O   . PHE I 112 ? 1.486 2.809 1.432 0.410  -0.167 -0.205 112 PHE III O   
11040 C CB  . PHE I 112 ? 1.565 3.071 1.449 0.402  -0.165 -0.222 112 PHE III CB  
11041 C CG  . PHE I 112 ? 1.582 3.088 1.450 0.447  -0.160 -0.226 112 PHE III CG  
11042 C CD1 . PHE I 112 ? 1.638 3.126 1.474 0.488  -0.168 -0.226 112 PHE III CD1 
11043 C CD2 . PHE I 112 ? 1.536 3.050 1.412 0.448  -0.147 -0.230 112 PHE III CD2 
11044 C CE1 . PHE I 112 ? 1.655 3.132 1.467 0.530  -0.163 -0.229 112 PHE III CE1 
11045 C CE2 . PHE I 112 ? 1.562 3.071 1.417 0.489  -0.143 -0.233 112 PHE III CE2 
11046 C CZ  . PHE I 112 ? 1.519 3.007 1.341 0.531  -0.151 -0.232 112 PHE III CZ  
11047 N N   . PHE I 113 ? 1.534 2.895 1.497 0.352  -0.156 -0.206 113 PHE III N   
11048 C CA  . PHE I 113 ? 1.441 2.758 1.432 0.348  -0.141 -0.204 113 PHE III CA  
11049 C C   . PHE I 113 ? 1.519 2.876 1.496 0.326  -0.123 -0.213 113 PHE III C   
11050 O O   . PHE I 113 ? 1.647 3.036 1.607 0.296  -0.122 -0.216 113 PHE III O   
11051 C CB  . PHE I 113 ? 1.359 2.609 1.387 0.332  -0.145 -0.191 113 PHE III CB  
11052 C CG  . PHE I 113 ? 1.459 2.707 1.484 0.297  -0.142 -0.188 113 PHE III CG  
11053 C CD1 . PHE I 113 ? 1.640 2.899 1.650 0.284  -0.159 -0.184 113 PHE III CD1 
11054 C CD2 . PHE I 113 ? 1.515 2.739 1.547 0.275  -0.123 -0.189 113 PHE III CD2 
11055 C CE1 . PHE I 113 ? 1.718 2.965 1.717 0.250  -0.156 -0.181 113 PHE III CE1 
11056 C CE2 . PHE I 113 ? 1.586 2.794 1.603 0.243  -0.119 -0.186 113 PHE III CE2 
11057 C CZ  . PHE I 113 ? 1.647 2.865 1.647 0.230  -0.136 -0.182 113 PHE III CZ  
11058 N N   . ILE I 114 ? 1.477 2.830 1.455 0.338  -0.110 -0.218 114 ILE III N   
11059 C CA  . ILE I 114 ? 1.445 2.831 1.405 0.317  -0.093 -0.227 114 ILE III CA  
11060 C C   . ILE I 114 ? 1.505 2.821 1.488 0.296  -0.076 -0.223 114 ILE III C   
11061 O O   . ILE I 114 ? 1.500 2.767 1.508 0.314  -0.070 -0.220 114 ILE III O   
11062 C CB  . ILE I 114 ? 1.363 2.791 1.303 0.346  -0.089 -0.235 114 ILE III CB  
11063 C CG1 . ILE I 114 ? 1.335 2.805 1.257 0.383  -0.105 -0.235 114 ILE III CG1 
11064 C CG2 . ILE I 114 ? 1.482 2.972 1.397 0.319  -0.077 -0.243 114 ILE III CG2 
11065 C CD1 . ILE I 114 ? 1.329 2.812 1.231 0.424  -0.103 -0.239 114 ILE III CD1 
11066 N N   . CYS I 115 ? 1.545 2.854 1.516 0.258  -0.066 -0.224 115 CYS III N   
11067 C CA  . CYS I 115 ? 1.573 2.808 1.560 0.242  -0.048 -0.219 115 CYS III CA  
11068 C C   . CYS I 115 ? 1.546 2.775 1.523 0.241  -0.027 -0.228 115 CYS III C   
11069 O O   . CYS I 115 ? 1.594 2.882 1.538 0.231  -0.024 -0.237 115 CYS III O   
11070 C CB  . CYS I 115 ? 1.670 2.887 1.631 0.200  -0.040 -0.219 115 CYS III CB  
11071 S SG  . CYS I 115 ? 1.933 3.139 1.900 0.195  -0.062 -0.208 115 CYS III SG  
11072 N N   . THR I 116 ? 1.479 2.642 1.486 0.252  -0.013 -0.223 116 THR III N   
11073 C CA  . THR I 116 ? 1.470 2.613 1.466 0.248  0.010  -0.230 116 THR III CA  
11074 C C   . THR I 116 ? 1.525 2.599 1.519 0.223  0.035  -0.228 116 THR III C   
11075 O O   . THR I 116 ? 1.579 2.616 1.568 0.220  0.058  -0.232 116 THR III O   
11076 C CB  . THR I 116 ? 1.347 2.470 1.372 0.282  0.009  -0.228 116 THR III CB  
11077 O OG1 . THR I 116 ? 1.424 2.498 1.497 0.295  0.006  -0.216 116 THR III OG1 
11078 C CG2 . THR I 116 ? 1.246 2.425 1.257 0.309  -0.012 -0.231 116 THR III CG2 
11079 N N   . ALA I 117 ? 1.530 2.580 1.521 0.207  0.032  -0.221 117 ALA III N   
11080 C CA  . ALA I 117 ? 1.700 2.677 1.676 0.185  0.055  -0.218 117 ALA III CA  
11081 C C   . ALA I 117 ? 1.883 2.862 1.829 0.159  0.044  -0.214 117 ALA III C   
11082 O O   . ALA I 117 ? 1.875 2.909 1.825 0.162  0.019  -0.213 117 ALA III O   
11083 C CB  . ALA I 117 ? 1.703 2.618 1.734 0.213  0.066  -0.206 117 ALA III CB  
11084 N N   . LYS I 118 ? 2.074 2.985 1.985 0.132  0.066  -0.213 118 LYS III N   
11085 C CA  . LYS I 118 ? 2.207 3.098 2.084 0.108  0.058  -0.208 118 LYS III CA  
11086 C C   . LYS I 118 ? 2.278 3.140 2.210 0.142  0.042  -0.191 118 LYS III C   
11087 O O   . LYS I 118 ? 2.221 3.033 2.195 0.170  0.054  -0.181 118 LYS III O   
11088 C CB  . LYS I 118 ? 2.299 3.111 2.109 0.070  0.087  -0.213 118 LYS III CB  
11089 C CG  . LYS I 118 ? 2.439 3.214 2.198 0.039  0.083  -0.208 118 LYS III CG  
11090 C CD  . LYS I 118 ? 2.416 3.105 2.094 -0.002 0.116  -0.214 118 LYS III CD  
11091 C CE  . LYS I 118 ? 2.486 3.120 2.094 -0.039 0.116  -0.211 118 LYS III CE  
11092 N NZ  . LYS I 118 ? 2.570 3.104 2.189 -0.009 0.122  -0.193 118 LYS III NZ  
11093 N N   . THR I 119 ? 2.333 3.231 2.266 0.139  0.015  -0.186 119 THR III N   
11094 C CA  . THR I 119 ? 2.293 3.178 2.277 0.170  -0.007 -0.168 119 THR III CA  
11095 C C   . THR I 119 ? 2.481 3.331 2.431 0.150  -0.017 -0.160 119 THR III C   
11096 O O   . THR I 119 ? 2.511 3.403 2.460 0.146  -0.043 -0.157 119 THR III O   
11097 C CB  . THR I 119 ? 2.100 3.058 2.121 0.192  -0.033 -0.169 119 THR III CB  
11098 O OG1 . THR I 119 ? 2.074 3.096 2.052 0.169  -0.045 -0.181 119 THR III OG1 
11099 C CG2 . THR I 119 ? 2.000 2.978 2.051 0.215  -0.023 -0.176 119 THR III CG2 
11100 N N   . GLU I 120 ? 2.666 3.434 2.581 0.137  0.004  -0.155 120 GLU III N   
11101 C CA  . GLU I 120 ? 2.835 3.560 2.694 0.109  -0.001 -0.149 120 GLU III CA  
11102 C C   . GLU I 120 ? 2.777 3.495 2.676 0.135  -0.029 -0.130 120 GLU III C   
11103 O O   . GLU I 120 ? 2.862 3.571 2.719 0.112  -0.044 -0.127 120 GLU III O   
11104 C CB  . GLU I 120 ? 3.085 3.705 2.894 0.097  0.031  -0.147 120 GLU III CB  
11105 C CG  . GLU I 120 ? 3.181 3.791 2.965 0.083  0.062  -0.162 120 GLU III CG  
11106 C CD  . GLU I 120 ? 3.158 3.756 3.012 0.129  0.075  -0.156 120 GLU III CD  
11107 O OE1 . GLU I 120 ? 3.103 3.722 3.030 0.169  0.057  -0.141 120 GLU III OE1 
11108 O OE2 . GLU I 120 ? 3.207 3.779 3.041 0.121  0.104  -0.166 120 GLU III OE2 
11109 N N   . TRP I 121 ? 2.477 3.199 2.452 0.178  -0.037 -0.116 121 TRP III N   
11110 C CA  . TRP I 121 ? 2.387 3.106 2.398 0.199  -0.066 -0.097 121 TRP III CA  
11111 C C   . TRP I 121 ? 2.316 3.107 2.329 0.190  -0.098 -0.101 121 TRP III C   
11112 O O   . TRP I 121 ? 2.384 3.170 2.408 0.196  -0.123 -0.087 121 TRP III O   
11113 C CB  . TRP I 121 ? 2.338 3.054 2.431 0.243  -0.067 -0.081 121 TRP III CB  
11114 C CG  . TRP I 121 ? 2.234 3.013 2.373 0.257  -0.070 -0.091 121 TRP III CG  
11115 C CD1 . TRP I 121 ? 2.100 2.937 2.275 0.267  -0.097 -0.089 121 TRP III CD1 
11116 C CD2 . TRP I 121 ? 2.235 3.018 2.378 0.259  -0.042 -0.104 121 TRP III CD2 
11117 N NE1 . TRP I 121 ? 2.010 2.882 2.209 0.278  -0.088 -0.100 121 TRP III NE1 
11118 C CE2 . TRP I 121 ? 2.054 2.897 2.237 0.273  -0.055 -0.110 121 TRP III CE2 
11119 C CE3 . TRP I 121 ? 2.311 3.046 2.421 0.249  -0.006 -0.113 121 TRP III CE3 
11120 C CZ2 . TRP I 121 ? 1.990 2.848 2.183 0.278  -0.035 -0.122 121 TRP III CZ2 
11121 C CZ3 . TRP I 121 ? 2.271 3.025 2.394 0.253  0.013  -0.126 121 TRP III CZ3 
11122 C CH2 . TRP I 121 ? 2.128 2.944 2.293 0.268  -0.002 -0.130 121 TRP III CH2 
11123 N N   . LEU I 122 ? 2.454 3.308 2.453 0.177  -0.096 -0.120 122 LEU III N   
11124 C CA  . LEU I 122 ? 2.460 3.381 2.452 0.170  -0.120 -0.126 122 LEU III CA  
11125 C C   . LEU I 122 ? 2.661 3.591 2.582 0.128  -0.120 -0.135 122 LEU III C   
11126 O O   . LEU I 122 ? 2.739 3.719 2.647 0.120  -0.140 -0.139 122 LEU III O   
11127 C CB  . LEU I 122 ? 2.295 3.283 2.307 0.184  -0.119 -0.140 122 LEU III CB  
11128 C CG  . LEU I 122 ? 2.196 3.176 2.273 0.221  -0.119 -0.132 122 LEU III CG  
11129 C CD1 . LEU I 122 ? 2.055 3.088 2.138 0.234  -0.116 -0.146 122 LEU III CD1 
11130 C CD2 . LEU I 122 ? 2.135 3.105 2.250 0.240  -0.147 -0.114 122 LEU III CD2 
11131 N N   . ASP I 123 ? 2.822 3.702 2.692 0.099  -0.097 -0.140 123 ASP III N   
11132 C CA  . ASP I 123 ? 2.988 3.874 2.783 0.050  -0.095 -0.149 123 ASP III CA  
11133 C C   . ASP I 123 ? 3.033 3.895 2.813 0.045  -0.119 -0.136 123 ASP III C   
11134 O O   . ASP I 123 ? 3.073 3.867 2.872 0.066  -0.126 -0.118 123 ASP III O   
11135 C CB  . ASP I 123 ? 3.150 3.963 2.886 0.020  -0.065 -0.153 123 ASP III CB  
11136 C CG  . ASP I 123 ? 3.126 3.969 2.861 0.013  -0.042 -0.169 123 ASP III CG  
11137 O OD1 . ASP I 123 ? 3.082 4.012 2.851 0.027  -0.050 -0.178 123 ASP III OD1 
11138 O OD2 . ASP I 123 ? 3.141 3.915 2.836 -0.004 -0.015 -0.171 123 ASP III OD2 
11139 N N   . GLY I 124 ? 2.878 3.800 2.626 0.018  -0.131 -0.146 124 GLY III N   
11140 C CA  . GLY I 124 ? 2.787 3.685 2.512 0.008  -0.152 -0.135 124 GLY III CA  
11141 C C   . GLY I 124 ? 2.628 3.553 2.409 0.045  -0.181 -0.124 124 GLY III C   
11142 O O   . GLY I 124 ? 2.691 3.600 2.454 0.037  -0.201 -0.115 124 GLY III O   
11143 N N   . LYS I 125 ? 2.518 3.479 2.360 0.082  -0.182 -0.125 125 LYS III N   
11144 C CA  . LYS I 125 ? 2.334 3.317 2.225 0.115  -0.207 -0.116 125 LYS III CA  
11145 C C   . LYS I 125 ? 2.245 3.311 2.146 0.128  -0.209 -0.131 125 LYS III C   
11146 O O   . LYS I 125 ? 2.257 3.346 2.165 0.141  -0.230 -0.128 125 LYS III O   
11147 C CB  . LYS I 125 ? 2.192 3.132 2.145 0.150  -0.208 -0.099 125 LYS III CB  
11148 C CG  . LYS I 125 ? 2.202 3.060 2.145 0.146  -0.202 -0.083 125 LYS III CG  
11149 C CD  . LYS I 125 ? 2.132 2.958 2.142 0.184  -0.203 -0.065 125 LYS III CD  
11150 C CE  . LYS I 125 ? 2.092 2.837 2.084 0.185  -0.197 -0.048 125 LYS III CE  
11151 N NZ  . LYS I 125 ? 1.914 2.639 1.972 0.222  -0.211 -0.023 125 LYS III NZ  
11152 N N   . HIS I 126 ? 2.324 3.430 2.220 0.125  -0.188 -0.147 126 HIS III N   
11153 C CA  . HIS I 126 ? 2.252 3.436 2.153 0.142  -0.187 -0.160 126 HIS III CA  
11154 C C   . HIS I 126 ? 2.273 3.520 2.126 0.109  -0.173 -0.177 126 HIS III C   
11155 O O   . HIS I 126 ? 2.330 3.552 2.151 0.075  -0.157 -0.180 126 HIS III O   
11156 C CB  . HIS I 126 ? 2.240 3.424 2.184 0.174  -0.177 -0.162 126 HIS III CB  
11157 C CG  . HIS I 126 ? 2.223 3.361 2.216 0.204  -0.191 -0.147 126 HIS III CG  
11158 N ND1 . HIS I 126 ? 2.171 3.329 2.180 0.230  -0.207 -0.145 126 HIS III ND1 
11159 C CD2 . HIS I 126 ? 2.210 3.287 2.237 0.210  -0.191 -0.131 126 HIS III CD2 
11160 C CE1 . HIS I 126 ? 2.104 3.218 2.156 0.246  -0.218 -0.130 126 HIS III CE1 
11161 N NE2 . HIS I 126 ? 2.072 3.142 2.140 0.236  -0.208 -0.121 126 HIS III NE2 
11162 N N   . VAL I 127 ? 2.271 3.599 2.115 0.120  -0.177 -0.188 127 VAL III N   
11163 C CA  . VAL I 127 ? 2.330 3.738 2.131 0.088  -0.168 -0.202 127 VAL III CA  
11164 C C   . VAL I 127 ? 2.268 3.739 2.075 0.099  -0.152 -0.214 127 VAL III C   
11165 O O   . VAL I 127 ? 2.284 3.790 2.116 0.141  -0.156 -0.217 127 VAL III O   
11166 C CB  . VAL I 127 ? 2.403 3.868 2.186 0.094  -0.181 -0.206 127 VAL III CB  
11167 C CG1 . VAL I 127 ? 2.521 4.086 2.267 0.065  -0.170 -0.221 127 VAL III CG1 
11168 C CG2 . VAL I 127 ? 2.573 3.973 2.342 0.078  -0.198 -0.194 127 VAL III CG2 
11169 N N   . VAL I 128 ? 2.355 3.840 2.134 0.060  -0.135 -0.222 128 VAL III N   
11170 C CA  . VAL I 128 ? 2.115 3.663 1.894 0.063  -0.121 -0.232 128 VAL III CA  
11171 C C   . VAL I 128 ? 1.962 3.634 1.721 0.058  -0.123 -0.243 128 VAL III C   
11172 O O   . VAL I 128 ? 1.994 3.706 1.716 0.013  -0.121 -0.248 128 VAL III O   
11173 C CB  . VAL I 128 ? 2.111 3.619 1.861 0.018  -0.101 -0.236 128 VAL III CB  
11174 C CG1 . VAL I 128 ? 2.120 3.698 1.867 0.017  -0.089 -0.246 128 VAL III CG1 
11175 C CG2 . VAL I 128 ? 2.318 3.705 2.089 0.028  -0.096 -0.224 128 VAL III CG2 
11176 N N   . PHE I 129 ? 1.878 3.613 1.660 0.105  -0.126 -0.246 129 PHE III N   
11177 C CA  . PHE I 129 ? 1.913 3.773 1.680 0.111  -0.128 -0.255 129 PHE III CA  
11178 C C   . PHE I 129 ? 2.101 4.046 1.872 0.125  -0.119 -0.262 129 PHE III C   
11179 O O   . PHE I 129 ? 2.173 4.234 1.935 0.135  -0.120 -0.268 129 PHE III O   
11180 C CB  . PHE I 129 ? 1.943 3.812 1.723 0.163  -0.142 -0.252 129 PHE III CB  
11181 C CG  . PHE I 129 ? 1.848 3.679 1.655 0.222  -0.145 -0.248 129 PHE III CG  
11182 C CD1 . PHE I 129 ? 1.883 3.792 1.690 0.263  -0.142 -0.253 129 PHE III CD1 
11183 C CD2 . PHE I 129 ? 1.823 3.542 1.652 0.236  -0.152 -0.238 129 PHE III CD2 
11184 C CE1 . PHE I 129 ? 1.979 3.843 1.800 0.315  -0.145 -0.250 129 PHE III CE1 
11185 C CE2 . PHE I 129 ? 1.931 3.615 1.780 0.284  -0.155 -0.235 129 PHE III CE2 
11186 C CZ  . PHE I 129 ? 2.059 3.808 1.898 0.322  -0.151 -0.241 129 PHE III CZ  
11187 N N   . GLY I 130 ? 2.362 4.254 2.143 0.126  -0.110 -0.261 130 GLY III N   
11188 C CA  . GLY I 130 ? 2.465 4.434 2.244 0.136  -0.103 -0.267 130 GLY III CA  
11189 C C   . GLY I 130 ? 2.412 4.305 2.193 0.120  -0.091 -0.266 130 GLY III C   
11190 O O   . GLY I 130 ? 2.463 4.248 2.249 0.103  -0.086 -0.261 130 GLY III O   
11191 N N   . LYS I 131 ? 2.241 4.194 2.018 0.128  -0.085 -0.271 131 LYS III N   
11192 C CA  . LYS I 131 ? 2.198 4.084 1.973 0.116  -0.072 -0.272 131 LYS III CA  
11193 C C   . LYS I 131 ? 2.235 4.183 2.018 0.158  -0.074 -0.273 131 LYS III C   
11194 O O   . LYS I 131 ? 2.293 4.360 2.067 0.171  -0.080 -0.276 131 LYS III O   
11195 C CB  . LYS I 131 ? 2.258 4.138 1.993 0.044  -0.058 -0.277 131 LYS III CB  
11196 C CG  . LYS I 131 ? 2.191 4.025 1.914 0.029  -0.042 -0.280 131 LYS III CG  
11197 C CD  . LYS I 131 ? 2.131 3.924 1.805 -0.044 -0.025 -0.284 131 LYS III CD  
11198 C CE  . LYS I 131 ? 2.020 3.701 1.687 -0.049 -0.006 -0.284 131 LYS III CE  
11199 N NZ  . LYS I 131 ? 2.030 3.726 1.724 -0.002 -0.007 -0.284 131 LYS III NZ  
11200 N N   . VAL I 132 ? 2.263 4.130 2.058 0.179  -0.066 -0.271 132 VAL III N   
11201 C CA  . VAL I 132 ? 2.186 4.089 1.979 0.210  -0.065 -0.273 132 VAL III CA  
11202 C C   . VAL I 132 ? 2.100 4.088 1.861 0.168  -0.059 -0.279 132 VAL III C   
11203 O O   . VAL I 132 ? 2.072 4.025 1.810 0.109  -0.046 -0.282 132 VAL III O   
11204 C CB  . VAL I 132 ? 2.192 3.977 2.000 0.229  -0.055 -0.270 132 VAL III CB  
11205 C CG1 . VAL I 132 ? 2.116 3.930 1.912 0.255  -0.053 -0.272 132 VAL III CG1 
11206 C CG2 . VAL I 132 ? 2.247 3.965 2.085 0.272  -0.064 -0.263 132 VAL III CG2 
11207 N N   . LYS I 133 ? 2.196 4.297 1.952 0.197  -0.068 -0.279 133 LYS III N   
11208 C CA  . LYS I 133 ? 2.257 4.458 1.985 0.160  -0.066 -0.283 133 LYS III CA  
11209 C C   . LYS I 133 ? 2.248 4.424 1.967 0.179  -0.061 -0.283 133 LYS III C   
11210 O O   . LYS I 133 ? 2.129 4.282 1.823 0.129  -0.049 -0.287 133 LYS III O   
11211 C CB  . LYS I 133 ? 2.286 4.646 2.017 0.187  -0.080 -0.282 133 LYS III CB  
11212 C CG  . LYS I 133 ? 2.132 4.629 1.841 0.131  -0.081 -0.286 133 LYS III CG  
11213 C CD  . LYS I 133 ? 2.319 4.810 2.015 0.067  -0.077 -0.290 133 LYS III CD  
11214 C CE  . LYS I 133 ? 2.264 4.889 1.930 0.002  -0.077 -0.294 133 LYS III CE  
11215 N NZ  . LYS I 133 ? 2.231 5.030 1.914 0.046  -0.090 -0.290 133 LYS III NZ  
11216 N N   . GLU I 134 ? 2.298 4.468 2.031 0.249  -0.069 -0.278 134 GLU III N   
11217 C CA  . GLU I 134 ? 2.374 4.504 2.097 0.276  -0.065 -0.277 134 GLU III CA  
11218 C C   . GLU I 134 ? 2.419 4.436 2.159 0.331  -0.064 -0.273 134 GLU III C   
11219 O O   . GLU I 134 ? 2.426 4.431 2.184 0.365  -0.072 -0.270 134 GLU III O   
11220 C CB  . GLU I 134 ? 2.419 4.676 2.123 0.300  -0.076 -0.274 134 GLU III CB  
11221 C CG  . GLU I 134 ? 2.461 4.825 2.145 0.232  -0.075 -0.278 134 GLU III CG  
11222 C CD  . GLU I 134 ? 2.533 5.071 2.213 0.254  -0.091 -0.274 134 GLU III CD  
11223 O OE1 . GLU I 134 ? 2.573 5.169 2.272 0.307  -0.101 -0.270 134 GLU III OE1 
11224 O OE2 . GLU I 134 ? 2.548 5.167 2.205 0.217  -0.093 -0.274 134 GLU III OE2 
11225 N N   . GLY I 135 ? 2.426 4.363 2.158 0.335  -0.054 -0.274 135 GLY III N   
11226 C CA  . GLY I 135 ? 2.177 4.010 1.920 0.380  -0.052 -0.271 135 GLY III CA  
11227 C C   . GLY I 135 ? 1.995 3.712 1.766 0.361  -0.042 -0.271 135 GLY III C   
11228 O O   . GLY I 135 ? 1.929 3.580 1.715 0.398  -0.045 -0.267 135 GLY III O   
11229 N N   . MET I 136 ? 1.852 3.542 1.627 0.305  -0.029 -0.274 136 MET III N   
11230 C CA  . MET I 136 ? 1.792 3.371 1.594 0.290  -0.016 -0.272 136 MET III CA  
11231 C C   . MET I 136 ? 1.770 3.262 1.577 0.312  -0.005 -0.272 136 MET III C   
11232 O O   . MET I 136 ? 1.887 3.298 1.724 0.324  -0.001 -0.268 136 MET III O   
11233 C CB  . MET I 136 ? 1.856 3.413 1.647 0.228  -0.001 -0.276 136 MET III CB  
11234 C CG  . MET I 136 ? 1.981 3.538 1.785 0.207  -0.006 -0.273 136 MET III CG  
11235 S SD  . MET I 136 ? 1.906 3.375 1.759 0.241  -0.012 -0.264 136 MET III SD  
11236 C CE  . MET I 136 ? 1.867 3.219 1.731 0.226  0.015  -0.264 136 MET III CE  
11237 N N   . ASN I 137 ? 1.821 3.331 1.599 0.317  -0.000 -0.275 137 ASN III N   
11238 C CA  . ASN I 137 ? 1.835 3.263 1.611 0.336  0.011  -0.275 137 ASN III CA  
11239 C C   . ASN I 137 ? 1.777 3.176 1.563 0.390  -0.001 -0.270 137 ASN III C   
11240 O O   . ASN I 137 ? 1.806 3.120 1.604 0.401  0.009  -0.269 137 ASN III O   
11241 C CB  . ASN I 137 ? 1.868 3.330 1.602 0.332  0.015  -0.279 137 ASN III CB  
11242 C CG  . ASN I 137 ? 1.861 3.359 1.572 0.274  0.026  -0.284 137 ASN III CG  
11243 O OD1 . ASN I 137 ? 1.981 3.563 1.660 0.265  0.017  -0.286 137 ASN III OD1 
11244 N ND2 . ASN I 137 ? 1.795 3.233 1.519 0.233  0.043  -0.286 137 ASN III ND2 
11245 N N   . ILE I 138 ? 1.586 3.054 1.364 0.423  -0.021 -0.267 138 ILE III N   
11246 C CA  . ILE I 138 ? 1.534 2.965 1.311 0.472  -0.032 -0.263 138 ILE III CA  
11247 C C   . ILE I 138 ? 1.564 2.940 1.380 0.462  -0.034 -0.259 138 ILE III C   
11248 O O   . ILE I 138 ? 1.545 2.848 1.370 0.480  -0.034 -0.256 138 ILE III O   
11249 C CB  . ILE I 138 ? 1.562 3.076 1.309 0.516  -0.051 -0.261 138 ILE III CB  
11250 C CG1 . ILE I 138 ? 1.747 3.314 1.455 0.533  -0.051 -0.262 138 ILE III CG1 
11251 C CG2 . ILE I 138 ? 1.732 3.190 1.467 0.563  -0.060 -0.257 138 ILE III CG2 
11252 C CD1 . ILE I 138 ? 2.062 3.737 1.768 0.500  -0.053 -0.264 138 ILE III CD1 
11253 N N   . VAL I 139 ? 1.507 2.920 1.346 0.431  -0.036 -0.259 139 VAL III N   
11254 C CA  . VAL I 139 ? 1.489 2.850 1.365 0.418  -0.037 -0.254 139 VAL III CA  
11255 C C   . VAL I 139 ? 1.554 2.828 1.457 0.401  -0.019 -0.252 139 VAL III C   
11256 O O   . VAL I 139 ? 1.767 2.984 1.697 0.410  -0.022 -0.246 139 VAL III O   
11257 C CB  . VAL I 139 ? 1.516 2.927 1.402 0.382  -0.040 -0.254 139 VAL III CB  
11258 C CG1 . VAL I 139 ? 1.731 3.083 1.655 0.368  -0.041 -0.247 139 VAL III CG1 
11259 C CG2 . VAL I 139 ? 1.608 3.111 1.473 0.400  -0.057 -0.255 139 VAL III CG2 
11260 N N   . GLU I 140 ? 1.541 2.804 1.434 0.375  -0.000 -0.257 140 GLU III N   
11261 C CA  . GLU I 140 ? 1.496 2.678 1.412 0.362  0.021  -0.256 140 GLU III CA  
11262 C C   . GLU I 140 ? 1.448 2.584 1.360 0.394  0.020  -0.255 140 GLU III C   
11263 O O   . GLU I 140 ? 1.484 2.561 1.430 0.395  0.026  -0.250 140 GLU III O   
11264 C CB  . GLU I 140 ? 1.590 2.765 1.485 0.328  0.043  -0.263 140 GLU III CB  
11265 C CG  . GLU I 140 ? 1.682 2.875 1.575 0.288  0.049  -0.264 140 GLU III CG  
11266 C CD  . GLU I 140 ? 1.827 3.020 1.681 0.252  0.068  -0.272 140 GLU III CD  
11267 O OE1 . GLU I 140 ? 1.755 2.948 1.584 0.259  0.074  -0.277 140 GLU III OE1 
11268 O OE2 . GLU I 140 ? 1.892 3.079 1.734 0.213  0.078  -0.274 140 GLU III OE2 
11269 N N   . ALA I 141 ? 1.465 2.631 1.335 0.421  0.011  -0.258 141 ALA III N   
11270 C CA  . ALA I 141 ? 1.533 2.648 1.383 0.452  0.010  -0.257 141 ALA III CA  
11271 C C   . ALA I 141 ? 1.545 2.629 1.413 0.470  -0.004 -0.251 141 ALA III C   
11272 O O   . ALA I 141 ? 1.556 2.576 1.428 0.476  0.001  -0.249 141 ALA III O   
11273 C CB  . ALA I 141 ? 1.627 2.783 1.421 0.483  0.001  -0.261 141 ALA III CB  
11274 N N   . MET I 142 ? 1.586 2.715 1.463 0.475  -0.021 -0.247 142 MET III N   
11275 C CA  . MET I 142 ? 1.631 2.729 1.521 0.488  -0.036 -0.241 142 MET III CA  
11276 C C   . MET I 142 ? 1.537 2.583 1.482 0.462  -0.026 -0.235 142 MET III C   
11277 O O   . MET I 142 ? 1.562 2.560 1.514 0.469  -0.032 -0.230 142 MET III O   
11278 C CB  . MET I 142 ? 1.630 2.788 1.521 0.492  -0.053 -0.239 142 MET III CB  
11279 C CG  . MET I 142 ? 1.579 2.792 1.419 0.528  -0.064 -0.243 142 MET III CG  
11280 S SD  . MET I 142 ? 1.559 2.858 1.407 0.521  -0.078 -0.242 142 MET III SD  
11281 C CE  . MET I 142 ? 1.499 2.738 1.373 0.517  -0.091 -0.234 142 MET III CE  
11282 N N   . GLU I 143 ? 1.481 2.534 1.460 0.432  -0.012 -0.235 143 GLU III N   
11283 C CA  . GLU I 143 ? 1.445 2.458 1.479 0.413  -0.003 -0.227 143 GLU III CA  
11284 C C   . GLU I 143 ? 1.413 2.369 1.456 0.417  0.009  -0.226 143 GLU III C   
11285 O O   . GLU I 143 ? 1.416 2.346 1.503 0.410  0.009  -0.217 143 GLU III O   
11286 C CB  . GLU I 143 ? 1.424 2.440 1.478 0.385  0.018  -0.229 143 GLU III CB  
11287 C CG  . GLU I 143 ? 1.463 2.526 1.509 0.370  0.009  -0.230 143 GLU III CG  
11288 C CD  . GLU I 143 ? 1.439 2.483 1.493 0.340  0.032  -0.231 143 GLU III CD  
11289 O OE1 . GLU I 143 ? 1.539 2.573 1.570 0.330  0.052  -0.239 143 GLU III OE1 
11290 O OE2 . GLU I 143 ? 1.375 2.409 1.455 0.328  0.031  -0.224 143 GLU III OE2 
11291 N N   . ARG I 144 ? 1.485 2.425 1.486 0.427  0.019  -0.234 144 ARG III N   
11292 C CA  . ARG I 144 ? 1.601 2.487 1.606 0.425  0.035  -0.235 144 ARG III CA  
11293 C C   . ARG I 144 ? 1.568 2.420 1.563 0.437  0.020  -0.229 144 ARG III C   
11294 O O   . ARG I 144 ? 1.725 2.533 1.733 0.428  0.032  -0.228 144 ARG III O   
11295 C CB  . ARG I 144 ? 1.756 2.631 1.702 0.435  0.044  -0.245 144 ARG III CB  
11296 C CG  . ARG I 144 ? 2.023 2.915 1.960 0.419  0.064  -0.252 144 ARG III CG  
11297 C CD  . ARG I 144 ? 2.239 3.192 2.181 0.409  0.055  -0.252 144 ARG III CD  
11298 N NE  . ARG I 144 ? 2.218 3.198 2.126 0.397  0.066  -0.260 144 ARG III NE  
11299 C CZ  . ARG I 144 ? 2.110 3.116 2.025 0.369  0.074  -0.262 144 ARG III CZ  
11300 N NH1 . ARG I 144 ? 1.800 2.806 1.756 0.355  0.073  -0.257 144 ARG III NH1 
11301 N NH2 . ARG I 144 ? 2.479 3.507 2.356 0.353  0.083  -0.269 144 ARG III NH2 
11302 N N   . PHE I 145 ? 1.486 2.357 1.456 0.455  -0.004 -0.227 145 PHE III N   
11303 C CA  . PHE I 145 ? 1.535 2.368 1.486 0.463  -0.019 -0.222 145 PHE III CA  
11304 C C   . PHE I 145 ? 1.537 2.381 1.543 0.447  -0.032 -0.211 145 PHE III C   
11305 O O   . PHE I 145 ? 1.731 2.546 1.725 0.447  -0.047 -0.205 145 PHE III O   
11306 C CB  . PHE I 145 ? 1.652 2.491 1.532 0.496  -0.036 -0.226 145 PHE III CB  
11307 C CG  . PHE I 145 ? 1.611 2.440 1.433 0.517  -0.026 -0.235 145 PHE III CG  
11308 C CD1 . PHE I 145 ? 1.669 2.430 1.447 0.521  -0.017 -0.237 145 PHE III CD1 
11309 C CD2 . PHE I 145 ? 1.505 2.395 1.314 0.529  -0.025 -0.240 145 PHE III CD2 
11310 C CE1 . PHE I 145 ? 1.675 2.425 1.397 0.542  -0.009 -0.244 145 PHE III CE1 
11311 C CE2 . PHE I 145 ? 1.615 2.503 1.372 0.548  -0.018 -0.246 145 PHE III CE2 
11312 C CZ  . PHE I 145 ? 1.712 2.527 1.425 0.556  -0.010 -0.248 145 PHE III CZ  
11313 N N   . GLY I 146 ? 1.462 2.344 1.523 0.432  -0.028 -0.207 146 GLY III N   
11314 C CA  . GLY I 146 ? 1.393 2.286 1.508 0.418  -0.040 -0.195 146 GLY III CA  
11315 C C   . GLY I 146 ? 1.361 2.237 1.538 0.400  -0.026 -0.186 146 GLY III C   
11316 O O   . GLY I 146 ? 1.390 2.240 1.568 0.396  -0.006 -0.190 146 GLY III O   
11317 N N   . SER I 147 ? 1.357 2.253 1.587 0.391  -0.038 -0.173 147 SER III N   
11318 C CA  . SER I 147 ? 1.361 2.255 1.659 0.378  -0.028 -0.161 147 SER III CA  
11319 C C   . SER I 147 ? 1.321 2.244 1.667 0.375  -0.039 -0.149 147 SER III C   
11320 O O   . SER I 147 ? 1.328 2.266 1.650 0.378  -0.055 -0.150 147 SER III O   
11321 C CB  . SER I 147 ? 1.477 2.354 1.779 0.369  -0.040 -0.155 147 SER III CB  
11322 O OG  . SER I 147 ? 1.435 2.320 1.727 0.367  -0.071 -0.146 147 SER III OG  
11323 N N   . ARG I 148 ? 1.272 2.202 1.685 0.370  -0.028 -0.136 148 ARG III N   
11324 C CA  . ARG I 148 ? 1.243 2.193 1.702 0.370  -0.035 -0.122 148 ARG III CA  
11325 C C   . ARG I 148 ? 1.238 2.204 1.693 0.367  -0.072 -0.111 148 ARG III C   
11326 O O   . ARG I 148 ? 1.206 2.181 1.663 0.368  -0.083 -0.106 148 ARG III O   
11327 C CB  . ARG I 148 ? 1.258 2.216 1.790 0.372  -0.018 -0.108 148 ARG III CB  
11328 C CG  . ARG I 148 ? 1.298 2.236 1.836 0.376  0.021  -0.117 148 ARG III CG  
11329 C CD  . ARG I 148 ? 1.451 2.397 2.043 0.375  0.039  -0.110 148 ARG III CD  
11330 N NE  . ARG I 148 ? 1.670 2.650 2.335 0.381  0.030  -0.088 148 ARG III NE  
11331 C CZ  . ARG I 148 ? 1.765 2.775 2.489 0.378  0.034  -0.076 148 ARG III CZ  
11332 N NH1 . ARG I 148 ? 1.846 2.851 2.562 0.365  0.046  -0.085 148 ARG III NH1 
11333 N NH2 . ARG I 148 ? 1.644 2.695 2.436 0.386  0.022  -0.053 148 ARG III NH2 
11334 N N   . ASN I 149 ? 1.275 2.238 1.717 0.360  -0.090 -0.109 149 ASN III N   
11335 C CA  . ASN I 149 ? 1.301 2.272 1.733 0.354  -0.125 -0.099 149 ASN III CA  
11336 C C   . ASN I 149 ? 1.351 2.310 1.707 0.360  -0.138 -0.112 149 ASN III C   
11337 O O   . ASN I 149 ? 1.575 2.533 1.911 0.355  -0.165 -0.106 149 ASN III O   
11338 C CB  . ASN I 149 ? 1.375 2.344 1.820 0.338  -0.138 -0.090 149 ASN III CB  
11339 C CG  . ASN I 149 ? 1.733 2.719 2.246 0.333  -0.118 -0.081 149 ASN III CG  
11340 O OD1 . ASN I 149 ? 1.783 2.753 2.290 0.337  -0.090 -0.093 149 ASN III OD1 
11341 N ND2 . ASN I 149 ? 2.005 3.025 2.580 0.323  -0.133 -0.061 149 ASN III ND2 
11342 N N   . GLY I 150 ? 1.345 2.294 1.657 0.371  -0.121 -0.129 150 GLY III N   
11343 C CA  . GLY I 150 ? 1.362 2.313 1.608 0.382  -0.131 -0.140 150 GLY III CA  
11344 C C   . GLY I 150 ? 1.396 2.315 1.582 0.391  -0.135 -0.149 150 GLY III C   
11345 O O   . GLY I 150 ? 1.460 2.379 1.586 0.407  -0.139 -0.159 150 GLY III O   
11346 N N   . LYS I 151 ? 1.465 2.357 1.663 0.380  -0.134 -0.144 151 LYS III N   
11347 C CA  . LYS I 151 ? 1.583 2.430 1.714 0.385  -0.136 -0.151 151 LYS III CA  
11348 C C   . LYS I 151 ? 1.689 2.522 1.780 0.403  -0.113 -0.167 151 LYS III C   
11349 O O   . LYS I 151 ? 1.693 2.538 1.821 0.400  -0.091 -0.169 151 LYS III O   
11350 C CB  . LYS I 151 ? 1.660 2.484 1.817 0.361  -0.136 -0.142 151 LYS III CB  
11351 C CG  . LYS I 151 ? 1.788 2.552 1.870 0.360  -0.136 -0.149 151 LYS III CG  
11352 C CD  . LYS I 151 ? 1.864 2.617 1.979 0.327  -0.136 -0.139 151 LYS III CD  
11353 C CE  . LYS I 151 ? 2.001 2.794 2.180 0.306  -0.158 -0.121 151 LYS III CE  
11354 N NZ  . LYS I 151 ? 2.120 2.915 2.335 0.272  -0.158 -0.111 151 LYS III NZ  
11355 N N   . THR I 152 ? 1.833 2.638 1.845 0.424  -0.118 -0.176 152 THR III N   
11356 C CA  . THR I 152 ? 1.868 2.664 1.838 0.445  -0.099 -0.189 152 THR III CA  
11357 C C   . THR I 152 ? 2.003 2.736 1.934 0.440  -0.091 -0.191 152 THR III C   
11358 O O   . THR I 152 ? 2.186 2.876 2.085 0.431  -0.103 -0.187 152 THR III O   
11359 C CB  . THR I 152 ? 1.847 2.658 1.753 0.477  -0.108 -0.197 152 THR III CB  
11360 O OG1 . THR I 152 ? 1.995 2.759 1.838 0.487  -0.124 -0.195 152 THR III OG1 
11361 C CG2 . THR I 152 ? 1.777 2.652 1.718 0.475  -0.115 -0.195 152 THR III CG2 
11362 N N   . SER I 153 ? 1.912 2.636 1.840 0.443  -0.068 -0.199 153 SER III N   
11363 C CA  . SER I 153 ? 1.885 2.545 1.771 0.436  -0.058 -0.202 153 SER III CA  
11364 C C   . SER I 153 ? 1.947 2.557 1.730 0.467  -0.061 -0.210 153 SER III C   
11365 O O   . SER I 153 ? 2.015 2.554 1.740 0.462  -0.058 -0.212 153 SER III O   
11366 C CB  . SER I 153 ? 1.911 2.576 1.835 0.424  -0.031 -0.206 153 SER III CB  
11367 O OG  . SER I 153 ? 1.781 2.473 1.691 0.444  -0.020 -0.215 153 SER III OG  
11368 N N   . LYS I 154 ? 1.927 2.572 1.683 0.499  -0.068 -0.215 154 LYS III N   
11369 C CA  . LYS I 154 ? 2.024 2.634 1.684 0.538  -0.073 -0.221 154 LYS III CA  
11370 C C   . LYS I 154 ? 2.003 2.660 1.657 0.560  -0.090 -0.219 154 LYS III C   
11371 O O   . LYS I 154 ? 1.937 2.660 1.659 0.545  -0.095 -0.216 154 LYS III O   
11372 C CB  . LYS I 154 ? 2.037 2.656 1.668 0.561  -0.057 -0.229 154 LYS III CB  
11373 C CG  . LYS I 154 ? 2.056 2.614 1.671 0.543  -0.039 -0.232 154 LYS III CG  
11374 C CD  . LYS I 154 ? 2.211 2.670 1.743 0.545  -0.041 -0.232 154 LYS III CD  
11375 C CE  . LYS I 154 ? 2.097 2.508 1.639 0.510  -0.022 -0.234 154 LYS III CE  
11376 N NZ  . LYS I 154 ? 2.018 2.464 1.658 0.466  -0.019 -0.227 154 LYS III NZ  
11377 N N   . LYS I 155 ? 1.992 2.614 1.561 0.596  -0.098 -0.222 155 LYS III N   
11378 C CA  . LYS I 155 ? 1.958 2.622 1.514 0.619  -0.112 -0.221 155 LYS III CA  
11379 C C   . LYS I 155 ? 1.948 2.697 1.515 0.648  -0.108 -0.226 155 LYS III C   
11380 O O   . LYS I 155 ? 2.177 2.922 1.694 0.681  -0.099 -0.231 155 LYS III O   
11381 C CB  . LYS I 155 ? 2.194 2.780 1.648 0.649  -0.119 -0.222 155 LYS III CB  
11382 C CG  . LYS I 155 ? 2.308 2.940 1.739 0.683  -0.129 -0.222 155 LYS III CG  
11383 C CD  . LYS I 155 ? 2.475 3.019 1.801 0.711  -0.134 -0.223 155 LYS III CD  
11384 C CE  . LYS I 155 ? 2.633 3.101 1.951 0.668  -0.144 -0.217 155 LYS III CE  
11385 N NZ  . LYS I 155 ? 2.760 3.139 1.969 0.691  -0.149 -0.218 155 LYS III NZ  
11386 N N   . ILE I 156 ? 1.816 2.644 1.445 0.633  -0.114 -0.224 156 ILE III N   
11387 C CA  . ILE I 156 ? 1.809 2.730 1.455 0.648  -0.111 -0.228 156 ILE III CA  
11388 C C   . ILE I 156 ? 1.877 2.836 1.487 0.679  -0.122 -0.228 156 ILE III C   
11389 O O   . ILE I 156 ? 1.873 2.837 1.506 0.662  -0.133 -0.225 156 ILE III O   
11390 C CB  . ILE I 156 ? 1.659 2.637 1.389 0.607  -0.107 -0.227 156 ILE III CB  
11391 C CG1 . ILE I 156 ? 1.700 2.630 1.469 0.575  -0.094 -0.225 156 ILE III CG1 
11392 C CG2 . ILE I 156 ? 1.646 2.712 1.383 0.614  -0.101 -0.232 156 ILE III CG2 
11393 C CD1 . ILE I 156 ? 1.712 2.625 1.452 0.587  -0.079 -0.231 156 ILE III CD1 
11394 N N   . THR I 157 ? 1.965 2.953 1.521 0.726  -0.120 -0.232 157 THR III N   
11395 C CA  . THR I 157 ? 2.054 3.075 1.567 0.765  -0.127 -0.233 157 THR III CA  
11396 C C   . THR I 157 ? 2.112 3.255 1.644 0.782  -0.125 -0.236 157 THR III C   
11397 O O   . THR I 157 ? 2.247 3.428 1.787 0.786  -0.118 -0.238 157 THR III O   
11398 C CB  . THR I 157 ? 2.152 3.092 1.567 0.817  -0.125 -0.233 157 THR III CB  
11399 O OG1 . THR I 157 ? 2.148 2.973 1.541 0.794  -0.124 -0.231 157 THR III OG1 
11400 C CG2 . THR I 157 ? 2.253 3.198 1.621 0.851  -0.132 -0.233 157 THR III CG2 
11401 N N   . ILE I 158 ? 2.042 3.249 1.581 0.788  -0.132 -0.236 158 ILE III N   
11402 C CA  . ILE I 158 ? 2.001 3.334 1.552 0.805  -0.130 -0.239 158 ILE III CA  
11403 C C   . ILE I 158 ? 2.149 3.493 1.627 0.876  -0.129 -0.239 158 ILE III C   
11404 O O   . ILE I 158 ? 2.292 3.620 1.733 0.903  -0.132 -0.238 158 ILE III O   
11405 C CB  . ILE I 158 ? 1.905 3.306 1.501 0.771  -0.136 -0.239 158 ILE III CB  
11406 C CG1 . ILE I 158 ? 1.932 3.296 1.590 0.708  -0.138 -0.237 158 ILE III CG1 
11407 C CG2 . ILE I 158 ? 1.844 3.380 1.462 0.771  -0.133 -0.242 158 ILE III CG2 
11408 C CD1 . ILE I 158 ? 2.045 3.443 1.734 0.676  -0.146 -0.235 158 ILE III CD1 
11409 N N   . ALA I 159 ? 2.287 3.656 1.741 0.908  -0.123 -0.239 159 ALA III N   
11410 C CA  . ALA I 159 ? 2.343 3.713 1.723 0.983  -0.120 -0.237 159 ALA III CA  
11411 C C   . ALA I 159 ? 2.528 4.031 1.909 1.018  -0.121 -0.237 159 ALA III C   
11412 O O   . ALA I 159 ? 2.600 4.090 1.919 1.081  -0.119 -0.235 159 ALA III O   
11413 C CB  . ALA I 159 ? 2.460 3.815 1.815 1.002  -0.116 -0.236 159 ALA III CB  
11414 N N   . ASP I 160 ? 2.661 4.288 2.109 0.980  -0.123 -0.238 160 ASP III N   
11415 C CA  . ASP I 160 ? 2.798 4.567 2.255 1.005  -0.124 -0.238 160 ASP III CA  
11416 C C   . ASP I 160 ? 2.828 4.684 2.356 0.936  -0.126 -0.242 160 ASP III C   
11417 O O   . ASP I 160 ? 2.820 4.649 2.391 0.875  -0.127 -0.244 160 ASP III O   
11418 C CB  . ASP I 160 ? 2.936 4.802 2.376 1.053  -0.122 -0.235 160 ASP III CB  
11419 C CG  . ASP I 160 ? 3.166 4.971 2.523 1.139  -0.118 -0.230 160 ASP III CG  
11420 O OD1 . ASP I 160 ? 3.249 5.038 2.568 1.180  -0.115 -0.230 160 ASP III OD1 
11421 O OD2 . ASP I 160 ? 3.249 5.014 2.573 1.165  -0.118 -0.226 160 ASP III OD2 
11422 N N   . CYS I 161 ? 3.035 4.997 2.570 0.947  -0.126 -0.243 161 CYS III N   
11423 C CA  . CYS I 161 ? 3.051 5.103 2.642 0.884  -0.128 -0.247 161 CYS III CA  
11424 C C   . CYS I 161 ? 3.014 5.220 2.603 0.914  -0.126 -0.247 161 CYS III C   
11425 O O   . CYS I 161 ? 3.015 5.239 2.561 0.985  -0.122 -0.244 161 CYS III O   
11426 C CB  . CYS I 161 ? 3.146 5.114 2.750 0.842  -0.132 -0.248 161 CYS III CB  
11427 S SG  . CYS I 161 ? 4.278 6.059 3.875 0.823  -0.135 -0.246 161 CYS III SG  
11428 N N   . GLY I 162 ? 2.865 5.181 2.499 0.857  -0.126 -0.250 162 GLY III N   
11429 C CA  . GLY I 162 ? 2.866 5.346 2.506 0.874  -0.124 -0.250 162 GLY III CA  
11430 C C   . GLY I 162 ? 2.786 5.371 2.471 0.794  -0.125 -0.254 162 GLY III C   
11431 O O   . GLY I 162 ? 2.671 5.186 2.378 0.728  -0.127 -0.257 162 GLY III O   
11432 N N   . GLN I 163 ? 2.879 5.633 2.574 0.804  -0.123 -0.254 163 GLN III N   
11433 C CA  . GLN I 163 ? 2.884 5.760 2.611 0.730  -0.123 -0.258 163 GLN III CA  
11434 C C   . GLN I 163 ? 3.038 6.006 2.772 0.729  -0.126 -0.254 163 GLN III C   
11435 O O   . GLN I 163 ? 2.863 5.904 2.583 0.799  -0.127 -0.248 163 GLN III O   
11436 C CB  . GLN I 163 ? 2.561 5.576 2.293 0.735  -0.118 -0.260 163 GLN III CB  
11437 C CG  . GLN I 163 ? 2.472 5.618 2.230 0.651  -0.118 -0.264 163 GLN III CG  
11438 C CD  . GLN I 163 ? 2.460 5.516 2.224 0.566  -0.118 -0.271 163 GLN III CD  
11439 O OE1 . GLN I 163 ? 2.515 5.608 2.288 0.490  -0.118 -0.274 163 GLN III OE1 
11440 N NE2 . GLN I 163 ? 2.374 5.311 2.128 0.578  -0.117 -0.272 163 GLN III NE2 
11441 N N   . LEU I 164 ? 3.145 6.104 2.895 0.650  -0.127 -0.257 164 LEU III N   
11442 C CA  . LEU I 164 ? 3.331 6.382 3.085 0.632  -0.130 -0.255 164 LEU III CA  
11443 C C   . LEU I 164 ? 3.496 6.737 3.267 0.587  -0.131 -0.256 164 LEU III C   
11444 O O   . LEU I 164 ? 3.552 6.811 3.331 0.524  -0.127 -0.262 164 LEU III O   
11445 C CB  . LEU I 164 ? 3.299 6.232 3.054 0.568  -0.129 -0.258 164 LEU III CB  
11446 C CG  . LEU I 164 ? 3.284 6.260 3.035 0.541  -0.131 -0.256 164 LEU III CG  
11447 C CD1 . LEU I 164 ? 3.227 6.183 2.960 0.621  -0.136 -0.249 164 LEU III CD1 
11448 C CD2 . LEU I 164 ? 3.091 5.943 2.842 0.467  -0.125 -0.262 164 LEU III CD2 
11449 N N   . GLU I 165 ? 3.612 6.993 3.383 0.620  -0.136 -0.249 165 GLU III N   
11450 C CA  . GLU I 165 ? 3.693 7.280 3.480 0.587  -0.138 -0.248 165 GLU III CA  
11451 C C   . GLU I 165 ? 3.861 7.487 3.647 0.505  -0.142 -0.250 165 GLU III C   
11452 O O   . GLU I 165 ? 4.063 7.773 3.846 0.525  -0.150 -0.242 165 GLU III O   
11453 C CB  . GLU I 165 ? 3.675 7.401 3.464 0.682  -0.142 -0.238 165 GLU III CB  
11454 C CG  . GLU I 165 ? 3.567 7.208 3.340 0.776  -0.136 -0.236 165 GLU III CG  
11455 C CD  . GLU I 165 ? 3.544 7.023 3.287 0.838  -0.139 -0.231 165 GLU III CD  
11456 O OE1 . GLU I 165 ? 3.648 7.106 3.386 0.821  -0.145 -0.228 165 GLU III OE1 
11457 O OE2 . GLU I 165 ? 3.486 6.857 3.206 0.900  -0.134 -0.231 165 GLU III OE2 
11458 O OXT . GLU I 165 ? 3.992 7.560 3.773 0.417  -0.137 -0.258 165 GLU III OXT 
# 
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   PRO 1   1   1   PRO PRO BBB . n 
A 1 2   ILE 2   2   2   ILE ILE BBB . n 
A 1 3   VAL 3   3   3   VAL VAL BBB . n 
A 1 4   GLN 4   4   4   GLN GLN BBB . n 
A 1 5   ASN 5   5   5   ASN ASN BBB . n 
A 1 6   LEU 6   6   6   LEU LEU BBB . n 
A 1 7   GLN 7   7   7   GLN GLN BBB . n 
A 1 8   GLY 8   8   8   GLY GLY BBB . n 
A 1 9   GLN 9   9   9   GLN GLN BBB . n 
A 1 10  MET 10  10  10  MET MET BBB . n 
A 1 11  VAL 11  11  11  VAL VAL BBB . n 
A 1 12  HIS 12  12  12  HIS HIS BBB . n 
A 1 13  GLN 13  13  13  GLN GLN BBB . n 
A 1 14  CYS 14  14  14  CYS CYS BBB . n 
A 1 15  ILE 15  15  15  ILE ILE BBB . n 
A 1 16  SER 16  16  16  SER SER BBB . n 
A 1 17  PRO 17  17  17  PRO PRO BBB . n 
A 1 18  ARG 18  18  18  ARG ARG BBB . n 
A 1 19  THR 19  19  19  THR THR BBB . n 
A 1 20  LEU 20  20  20  LEU LEU BBB . n 
A 1 21  ASN 21  21  21  ASN ASN BBB . n 
A 1 22  ALA 22  22  22  ALA ALA BBB . n 
A 1 23  TRP 23  23  23  TRP TRP BBB . n 
A 1 24  VAL 24  24  24  VAL VAL BBB . n 
A 1 25  LYS 25  25  25  LYS LYS BBB . n 
A 1 26  VAL 26  26  26  VAL VAL BBB . n 
A 1 27  VAL 27  27  27  VAL VAL BBB . n 
A 1 28  GLU 28  28  28  GLU GLU BBB . n 
A 1 29  GLU 29  29  29  GLU GLU BBB . n 
A 1 30  LYS 30  30  30  LYS LYS BBB . n 
A 1 31  ALA 31  31  31  ALA ALA BBB . n 
A 1 32  PHE 32  32  32  PHE PHE BBB . n 
A 1 33  SER 33  33  33  SER SER BBB . n 
A 1 34  PRO 34  34  34  PRO PRO BBB . n 
A 1 35  GLU 35  35  35  GLU GLU BBB . n 
A 1 36  VAL 36  36  36  VAL VAL BBB . n 
A 1 37  ILE 37  37  37  ILE ILE BBB . n 
A 1 38  PRO 38  38  38  PRO PRO BBB . n 
A 1 39  MET 39  39  39  MET MET BBB . n 
A 1 40  PHE 40  40  40  PHE PHE BBB . n 
A 1 41  SER 41  41  41  SER SER BBB . n 
A 1 42  ALA 42  42  42  ALA ALA BBB . n 
A 1 43  LEU 43  43  43  LEU LEU BBB . n 
A 1 44  SER 44  44  44  SER SER BBB . n 
A 1 45  CYS 45  45  45  CYS CYS BBB . n 
A 1 46  GLY 46  46  46  GLY GLY BBB . n 
A 1 47  ALA 47  47  47  ALA ALA BBB . n 
A 1 48  THR 48  48  48  THR THR BBB . n 
A 1 49  PRO 49  49  49  PRO PRO BBB . n 
A 1 50  GLN 50  50  50  GLN GLN BBB . n 
A 1 51  ASP 51  51  51  ASP ASP BBB . n 
A 1 52  LEU 52  52  52  LEU LEU BBB . n 
A 1 53  ASN 53  53  53  ASN ASN BBB . n 
A 1 54  THR 54  54  54  THR THR BBB . n 
A 1 55  MET 55  55  55  MET MET BBB . n 
A 1 56  LEU 56  56  56  LEU LEU BBB . n 
A 1 57  ASN 57  57  57  ASN ASN BBB . n 
A 1 58  THR 58  58  58  THR THR BBB . n 
A 1 59  VAL 59  59  59  VAL VAL BBB . n 
A 1 60  GLY 60  60  60  GLY GLY BBB . n 
A 1 61  GLY 61  61  61  GLY GLY BBB . n 
A 1 62  HIS 62  62  62  HIS HIS BBB . n 
A 1 63  GLN 63  63  63  GLN GLN BBB . n 
A 1 64  ALA 64  64  64  ALA ALA BBB . n 
A 1 65  ALA 65  65  65  ALA ALA BBB . n 
A 1 66  MET 66  66  66  MET MET BBB . n 
A 1 67  GLN 67  67  67  GLN GLN BBB . n 
A 1 68  MET 68  68  68  MET MET BBB . n 
A 1 69  LEU 69  69  69  LEU LEU BBB . n 
A 1 70  LYS 70  70  70  LYS LYS BBB . n 
A 1 71  GLU 71  71  71  GLU GLU BBB . n 
A 1 72  THR 72  72  72  THR THR BBB . n 
A 1 73  ILE 73  73  73  ILE ILE BBB . n 
A 1 74  ASN 74  74  74  ASN ASN BBB . n 
A 1 75  GLU 75  75  75  GLU GLU BBB . n 
A 1 76  GLU 76  76  76  GLU GLU BBB . n 
A 1 77  ALA 77  77  77  ALA ALA BBB . n 
A 1 78  ALA 78  78  78  ALA ALA BBB . n 
A 1 79  GLU 79  79  79  GLU GLU BBB . n 
A 1 80  TRP 80  80  80  TRP TRP BBB . n 
A 1 81  ASP 81  81  81  ASP ASP BBB . n 
A 1 82  ARG 82  82  82  ARG ARG BBB . n 
A 1 83  LEU 83  83  83  LEU LEU BBB . n 
A 1 84  HIS 84  84  84  HIS HIS BBB . n 
A 1 85  PRO 85  85  85  PRO PRO BBB . n 
A 1 86  VAL 86  86  86  VAL VAL BBB . n 
A 1 87  HIS 87  87  87  HIS HIS BBB . n 
A 1 88  ALA 88  88  88  ALA ALA BBB . n 
A 1 89  GLY 89  89  89  GLY GLY BBB . n 
A 1 90  PRO 90  90  90  PRO PRO BBB . n 
A 1 91  ILE 91  91  91  ILE ILE BBB . n 
A 1 92  ALA 92  92  92  ALA ALA BBB . n 
A 1 93  PRO 93  93  93  PRO PRO BBB . n 
A 1 94  GLY 94  94  94  GLY GLY BBB . n 
A 1 95  GLN 95  95  95  GLN GLN BBB . n 
A 1 96  MET 96  96  96  MET MET BBB . n 
A 1 97  ARG 97  97  97  ARG ARG BBB . n 
A 1 98  GLU 98  98  98  GLU GLU BBB . n 
A 1 99  PRO 99  99  99  PRO PRO BBB . n 
A 1 100 ARG 100 100 100 ARG ARG BBB . n 
A 1 101 GLY 101 101 101 GLY GLY BBB . n 
A 1 102 SER 102 102 102 SER SER BBB . n 
A 1 103 ASP 103 103 103 ASP ASP BBB . n 
A 1 104 ILE 104 104 104 ILE ILE BBB . n 
A 1 105 ALA 105 105 105 ALA ALA BBB . n 
A 1 106 GLY 106 106 106 GLY GLY BBB . n 
A 1 107 THR 107 107 107 THR THR BBB . n 
A 1 108 THR 108 108 108 THR THR BBB . n 
A 1 109 SER 109 109 109 SER SER BBB . n 
A 1 110 THR 110 110 110 THR THR BBB . n 
A 1 111 LEU 111 111 111 LEU LEU BBB . n 
A 1 112 GLN 112 112 112 GLN GLN BBB . n 
A 1 113 GLU 113 113 113 GLU GLU BBB . n 
A 1 114 GLN 114 114 114 GLN GLN BBB . n 
A 1 115 ILE 115 115 115 ILE ILE BBB . n 
A 1 116 GLY 116 116 116 GLY GLY BBB . n 
A 1 117 TRP 117 117 117 TRP TRP BBB . n 
A 1 118 MET 118 118 118 MET MET BBB . n 
A 1 119 THR 119 119 119 THR THR BBB . n 
A 1 120 HIS 120 120 120 HIS HIS BBB . n 
A 1 121 ASN 121 121 121 ASN ASN BBB . n 
A 1 122 PRO 122 122 122 PRO PRO BBB . n 
A 1 123 PRO 123 123 123 PRO PRO BBB . n 
A 1 124 ILE 124 124 124 ILE ILE BBB . n 
A 1 125 PRO 125 125 125 PRO PRO BBB . n 
A 1 126 VAL 126 126 126 VAL VAL BBB . n 
A 1 127 GLY 127 127 127 GLY GLY BBB . n 
A 1 128 GLU 128 128 128 GLU GLU BBB . n 
A 1 129 ILE 129 129 129 ILE ILE BBB . n 
A 1 130 TYR 130 130 130 TYR TYR BBB . n 
A 1 131 LYS 131 131 131 LYS LYS BBB . n 
A 1 132 ARG 132 132 132 ARG ARG BBB . n 
A 1 133 TRP 133 133 133 TRP TRP BBB . n 
A 1 134 ILE 134 134 134 ILE ILE BBB . n 
A 1 135 ILE 135 135 135 ILE ILE BBB . n 
A 1 136 LEU 136 136 136 LEU LEU BBB . n 
A 1 137 GLY 137 137 137 GLY GLY BBB . n 
A 1 138 LEU 138 138 138 LEU LEU BBB . n 
A 1 139 ASN 139 139 139 ASN ASN BBB . n 
A 1 140 LYS 140 140 140 LYS LYS BBB . n 
A 1 141 ILE 141 141 141 ILE ILE BBB . n 
A 1 142 VAL 142 142 142 VAL VAL BBB . n 
A 1 143 ARG 143 143 143 ARG ARG BBB . n 
A 1 144 MET 144 144 144 MET MET BBB . n 
A 1 145 TYR 145 145 145 TYR TYR BBB . n 
A 1 146 SER 146 146 146 SER SER BBB . n 
A 1 147 PRO 147 147 147 PRO PRO BBB . n 
A 1 148 THR 148 148 148 THR THR BBB . n 
A 1 149 SER 149 149 149 SER SER BBB . n 
A 1 150 ILE 150 150 150 ILE ILE BBB . n 
A 1 151 LEU 151 151 151 LEU LEU BBB . n 
A 1 152 ASP 152 152 152 ASP ASP BBB . n 
A 1 153 ILE 153 153 153 ILE ILE BBB . n 
A 1 154 ARG 154 154 154 ARG ARG BBB . n 
A 1 155 GLN 155 155 155 GLN GLN BBB . n 
A 1 156 GLY 156 156 156 GLY GLY BBB . n 
A 1 157 PRO 157 157 157 PRO PRO BBB . n 
A 1 158 LYS 158 158 158 LYS LYS BBB . n 
A 1 159 GLU 159 159 159 GLU GLU BBB . n 
A 1 160 PRO 160 160 160 PRO PRO BBB . n 
A 1 161 PHE 161 161 161 PHE PHE BBB . n 
A 1 162 ARG 162 162 162 ARG ARG BBB . n 
A 1 163 ASP 163 163 163 ASP ASP BBB . n 
A 1 164 TYR 164 164 164 TYR TYR BBB . n 
A 1 165 VAL 165 165 165 VAL VAL BBB . n 
A 1 166 ASP 166 166 166 ASP ASP BBB . n 
A 1 167 ARG 167 167 167 ARG ARG BBB . n 
A 1 168 PHE 168 168 168 PHE PHE BBB . n 
A 1 169 TYR 169 169 169 TYR TYR BBB . n 
A 1 170 LYS 170 170 170 LYS LYS BBB . n 
A 1 171 THR 171 171 171 THR THR BBB . n 
A 1 172 LEU 172 172 172 LEU LEU BBB . n 
A 1 173 ARG 173 173 173 ARG ARG BBB . n 
A 1 174 ALA 174 174 174 ALA ALA BBB . n 
A 1 175 GLU 175 175 175 GLU GLU BBB . n 
A 1 176 GLN 176 176 176 GLN GLN BBB . n 
A 1 177 ALA 177 177 177 ALA ALA BBB . n 
A 1 178 SER 178 178 178 SER SER BBB . n 
A 1 179 GLN 179 179 179 GLN GLN BBB . n 
A 1 180 GLU 180 180 180 GLU GLU BBB . n 
A 1 181 VAL 181 181 181 VAL VAL BBB . n 
A 1 182 LYS 182 182 182 LYS LYS BBB . n 
A 1 183 ASN 183 183 183 ASN ASN BBB . n 
A 1 184 ALA 184 184 184 ALA ALA BBB . n 
A 1 185 ALA 185 185 185 ALA ALA BBB . n 
A 1 186 THR 186 186 186 THR THR BBB . n 
A 1 187 GLU 187 187 187 GLU GLU BBB . n 
A 1 188 THR 188 188 188 THR THR BBB . n 
A 1 189 LEU 189 189 189 LEU LEU BBB . n 
A 1 190 LEU 190 190 190 LEU LEU BBB . n 
A 1 191 VAL 191 191 191 VAL VAL BBB . n 
A 1 192 GLN 192 192 192 GLN GLN BBB . n 
A 1 193 ASN 193 193 193 ASN ASN BBB . n 
A 1 194 ALA 194 194 194 ALA ALA BBB . n 
A 1 195 ASN 195 195 195 ASN ASN BBB . n 
A 1 196 PRO 196 196 196 PRO PRO BBB . n 
A 1 197 ASP 197 197 197 ASP ASP BBB . n 
A 1 198 CYS 198 198 198 CYS CYS BBB . n 
A 1 199 LYS 199 199 199 LYS LYS BBB . n 
A 1 200 THR 200 200 200 THR THR BBB . n 
A 1 201 ILE 201 201 201 ILE ILE BBB . n 
A 1 202 LEU 202 202 202 LEU LEU BBB . n 
A 1 203 LYS 203 203 203 LYS LYS BBB . n 
A 1 204 ALA 204 204 204 ALA ALA BBB . n 
A 1 205 LEU 205 205 205 LEU LEU BBB . n 
A 1 206 GLY 206 206 206 GLY GLY BBB . n 
A 1 207 PRO 207 207 207 PRO PRO BBB . n 
A 1 208 GLY 208 208 208 GLY GLY BBB . n 
A 1 209 ALA 209 209 209 ALA ALA BBB . n 
A 1 210 THR 210 210 210 THR THR BBB . n 
A 1 211 LEU 211 211 211 LEU LEU BBB . n 
A 1 212 GLU 212 212 212 GLU GLU BBB . n 
A 1 213 GLU 213 213 213 GLU GLU BBB . n 
A 1 214 MET 214 214 214 MET MET BBB . n 
A 1 215 MET 215 215 215 MET MET BBB . n 
A 1 216 THR 216 216 216 THR THR BBB . n 
A 1 217 ALA 217 217 217 ALA ALA BBB . n 
A 1 218 CYS 218 218 218 CYS CYS BBB . n 
A 1 219 GLN 219 219 219 GLN GLN BBB . n 
A 1 220 GLY 220 220 ?   ?   ?   BBB . n 
A 1 221 VAL 221 221 ?   ?   ?   BBB . n 
A 1 222 GLY 222 222 ?   ?   ?   BBB . n 
B 1 1   PRO 1   1   1   PRO PRO CCC . n 
B 1 2   ILE 2   2   2   ILE ILE CCC . n 
B 1 3   VAL 3   3   3   VAL VAL CCC . n 
B 1 4   GLN 4   4   4   GLN GLN CCC . n 
B 1 5   ASN 5   5   5   ASN ASN CCC . n 
B 1 6   LEU 6   6   6   LEU LEU CCC . n 
B 1 7   GLN 7   7   7   GLN GLN CCC . n 
B 1 8   GLY 8   8   8   GLY GLY CCC . n 
B 1 9   GLN 9   9   9   GLN GLN CCC . n 
B 1 10  MET 10  10  10  MET MET CCC . n 
B 1 11  VAL 11  11  11  VAL VAL CCC . n 
B 1 12  HIS 12  12  12  HIS HIS CCC . n 
B 1 13  GLN 13  13  13  GLN GLN CCC . n 
B 1 14  CYS 14  14  14  CYS CYS CCC . n 
B 1 15  ILE 15  15  15  ILE ILE CCC . n 
B 1 16  SER 16  16  16  SER SER CCC . n 
B 1 17  PRO 17  17  17  PRO PRO CCC . n 
B 1 18  ARG 18  18  18  ARG ARG CCC . n 
B 1 19  THR 19  19  19  THR THR CCC . n 
B 1 20  LEU 20  20  20  LEU LEU CCC . n 
B 1 21  ASN 21  21  21  ASN ASN CCC . n 
B 1 22  ALA 22  22  22  ALA ALA CCC . n 
B 1 23  TRP 23  23  23  TRP TRP CCC . n 
B 1 24  VAL 24  24  24  VAL VAL CCC . n 
B 1 25  LYS 25  25  25  LYS LYS CCC . n 
B 1 26  VAL 26  26  26  VAL VAL CCC . n 
B 1 27  VAL 27  27  27  VAL VAL CCC . n 
B 1 28  GLU 28  28  28  GLU GLU CCC . n 
B 1 29  GLU 29  29  29  GLU GLU CCC . n 
B 1 30  LYS 30  30  30  LYS LYS CCC . n 
B 1 31  ALA 31  31  31  ALA ALA CCC . n 
B 1 32  PHE 32  32  32  PHE PHE CCC . n 
B 1 33  SER 33  33  33  SER SER CCC . n 
B 1 34  PRO 34  34  34  PRO PRO CCC . n 
B 1 35  GLU 35  35  35  GLU GLU CCC . n 
B 1 36  VAL 36  36  36  VAL VAL CCC . n 
B 1 37  ILE 37  37  37  ILE ILE CCC . n 
B 1 38  PRO 38  38  38  PRO PRO CCC . n 
B 1 39  MET 39  39  39  MET MET CCC . n 
B 1 40  PHE 40  40  40  PHE PHE CCC . n 
B 1 41  SER 41  41  41  SER SER CCC . n 
B 1 42  ALA 42  42  42  ALA ALA CCC . n 
B 1 43  LEU 43  43  43  LEU LEU CCC . n 
B 1 44  SER 44  44  44  SER SER CCC . n 
B 1 45  CYS 45  45  45  CYS CYS CCC . n 
B 1 46  GLY 46  46  46  GLY GLY CCC . n 
B 1 47  ALA 47  47  47  ALA ALA CCC . n 
B 1 48  THR 48  48  48  THR THR CCC . n 
B 1 49  PRO 49  49  49  PRO PRO CCC . n 
B 1 50  GLN 50  50  50  GLN GLN CCC . n 
B 1 51  ASP 51  51  51  ASP ASP CCC . n 
B 1 52  LEU 52  52  52  LEU LEU CCC . n 
B 1 53  ASN 53  53  53  ASN ASN CCC . n 
B 1 54  THR 54  54  54  THR THR CCC . n 
B 1 55  MET 55  55  55  MET MET CCC . n 
B 1 56  LEU 56  56  56  LEU LEU CCC . n 
B 1 57  ASN 57  57  57  ASN ASN CCC . n 
B 1 58  THR 58  58  58  THR THR CCC . n 
B 1 59  VAL 59  59  59  VAL VAL CCC . n 
B 1 60  GLY 60  60  60  GLY GLY CCC . n 
B 1 61  GLY 61  61  61  GLY GLY CCC . n 
B 1 62  HIS 62  62  62  HIS HIS CCC . n 
B 1 63  GLN 63  63  63  GLN GLN CCC . n 
B 1 64  ALA 64  64  64  ALA ALA CCC . n 
B 1 65  ALA 65  65  65  ALA ALA CCC . n 
B 1 66  MET 66  66  66  MET MET CCC . n 
B 1 67  GLN 67  67  67  GLN GLN CCC . n 
B 1 68  MET 68  68  68  MET MET CCC . n 
B 1 69  LEU 69  69  69  LEU LEU CCC . n 
B 1 70  LYS 70  70  70  LYS LYS CCC . n 
B 1 71  GLU 71  71  71  GLU GLU CCC . n 
B 1 72  THR 72  72  72  THR THR CCC . n 
B 1 73  ILE 73  73  73  ILE ILE CCC . n 
B 1 74  ASN 74  74  74  ASN ASN CCC . n 
B 1 75  GLU 75  75  75  GLU GLU CCC . n 
B 1 76  GLU 76  76  76  GLU GLU CCC . n 
B 1 77  ALA 77  77  77  ALA ALA CCC . n 
B 1 78  ALA 78  78  78  ALA ALA CCC . n 
B 1 79  GLU 79  79  79  GLU GLU CCC . n 
B 1 80  TRP 80  80  80  TRP TRP CCC . n 
B 1 81  ASP 81  81  81  ASP ASP CCC . n 
B 1 82  ARG 82  82  82  ARG ARG CCC . n 
B 1 83  LEU 83  83  83  LEU LEU CCC . n 
B 1 84  HIS 84  84  84  HIS HIS CCC . n 
B 1 85  PRO 85  85  85  PRO PRO CCC . n 
B 1 86  VAL 86  86  86  VAL VAL CCC . n 
B 1 87  HIS 87  87  87  HIS HIS CCC . n 
B 1 88  ALA 88  88  88  ALA ALA CCC . n 
B 1 89  GLY 89  89  89  GLY GLY CCC . n 
B 1 90  PRO 90  90  90  PRO PRO CCC . n 
B 1 91  ILE 91  91  91  ILE ILE CCC . n 
B 1 92  ALA 92  92  92  ALA ALA CCC . n 
B 1 93  PRO 93  93  93  PRO PRO CCC . n 
B 1 94  GLY 94  94  94  GLY GLY CCC . n 
B 1 95  GLN 95  95  95  GLN GLN CCC . n 
B 1 96  MET 96  96  96  MET MET CCC . n 
B 1 97  ARG 97  97  97  ARG ARG CCC . n 
B 1 98  GLU 98  98  98  GLU GLU CCC . n 
B 1 99  PRO 99  99  99  PRO PRO CCC . n 
B 1 100 ARG 100 100 100 ARG ARG CCC . n 
B 1 101 GLY 101 101 101 GLY GLY CCC . n 
B 1 102 SER 102 102 102 SER SER CCC . n 
B 1 103 ASP 103 103 103 ASP ASP CCC . n 
B 1 104 ILE 104 104 104 ILE ILE CCC . n 
B 1 105 ALA 105 105 105 ALA ALA CCC . n 
B 1 106 GLY 106 106 106 GLY GLY CCC . n 
B 1 107 THR 107 107 107 THR THR CCC . n 
B 1 108 THR 108 108 108 THR THR CCC . n 
B 1 109 SER 109 109 109 SER SER CCC . n 
B 1 110 THR 110 110 110 THR THR CCC . n 
B 1 111 LEU 111 111 111 LEU LEU CCC . n 
B 1 112 GLN 112 112 112 GLN GLN CCC . n 
B 1 113 GLU 113 113 113 GLU GLU CCC . n 
B 1 114 GLN 114 114 114 GLN GLN CCC . n 
B 1 115 ILE 115 115 115 ILE ILE CCC . n 
B 1 116 GLY 116 116 116 GLY GLY CCC . n 
B 1 117 TRP 117 117 117 TRP TRP CCC . n 
B 1 118 MET 118 118 118 MET MET CCC . n 
B 1 119 THR 119 119 119 THR THR CCC . n 
B 1 120 HIS 120 120 120 HIS HIS CCC . n 
B 1 121 ASN 121 121 121 ASN ASN CCC . n 
B 1 122 PRO 122 122 122 PRO PRO CCC . n 
B 1 123 PRO 123 123 123 PRO PRO CCC . n 
B 1 124 ILE 124 124 124 ILE ILE CCC . n 
B 1 125 PRO 125 125 125 PRO PRO CCC . n 
B 1 126 VAL 126 126 126 VAL VAL CCC . n 
B 1 127 GLY 127 127 127 GLY GLY CCC . n 
B 1 128 GLU 128 128 128 GLU GLU CCC . n 
B 1 129 ILE 129 129 129 ILE ILE CCC . n 
B 1 130 TYR 130 130 130 TYR TYR CCC . n 
B 1 131 LYS 131 131 131 LYS LYS CCC . n 
B 1 132 ARG 132 132 132 ARG ARG CCC . n 
B 1 133 TRP 133 133 133 TRP TRP CCC . n 
B 1 134 ILE 134 134 134 ILE ILE CCC . n 
B 1 135 ILE 135 135 135 ILE ILE CCC . n 
B 1 136 LEU 136 136 136 LEU LEU CCC . n 
B 1 137 GLY 137 137 137 GLY GLY CCC . n 
B 1 138 LEU 138 138 138 LEU LEU CCC . n 
B 1 139 ASN 139 139 139 ASN ASN CCC . n 
B 1 140 LYS 140 140 140 LYS LYS CCC . n 
B 1 141 ILE 141 141 141 ILE ILE CCC . n 
B 1 142 VAL 142 142 142 VAL VAL CCC . n 
B 1 143 ARG 143 143 143 ARG ARG CCC . n 
B 1 144 MET 144 144 144 MET MET CCC . n 
B 1 145 TYR 145 145 145 TYR TYR CCC . n 
B 1 146 SER 146 146 146 SER SER CCC . n 
B 1 147 PRO 147 147 147 PRO PRO CCC . n 
B 1 148 THR 148 148 148 THR THR CCC . n 
B 1 149 SER 149 149 149 SER SER CCC . n 
B 1 150 ILE 150 150 150 ILE ILE CCC . n 
B 1 151 LEU 151 151 151 LEU LEU CCC . n 
B 1 152 ASP 152 152 152 ASP ASP CCC . n 
B 1 153 ILE 153 153 153 ILE ILE CCC . n 
B 1 154 ARG 154 154 154 ARG ARG CCC . n 
B 1 155 GLN 155 155 155 GLN GLN CCC . n 
B 1 156 GLY 156 156 156 GLY GLY CCC . n 
B 1 157 PRO 157 157 157 PRO PRO CCC . n 
B 1 158 LYS 158 158 158 LYS LYS CCC . n 
B 1 159 GLU 159 159 159 GLU GLU CCC . n 
B 1 160 PRO 160 160 160 PRO PRO CCC . n 
B 1 161 PHE 161 161 161 PHE PHE CCC . n 
B 1 162 ARG 162 162 162 ARG ARG CCC . n 
B 1 163 ASP 163 163 163 ASP ASP CCC . n 
B 1 164 TYR 164 164 164 TYR TYR CCC . n 
B 1 165 VAL 165 165 165 VAL VAL CCC . n 
B 1 166 ASP 166 166 166 ASP ASP CCC . n 
B 1 167 ARG 167 167 167 ARG ARG CCC . n 
B 1 168 PHE 168 168 168 PHE PHE CCC . n 
B 1 169 TYR 169 169 169 TYR TYR CCC . n 
B 1 170 LYS 170 170 170 LYS LYS CCC . n 
B 1 171 THR 171 171 171 THR THR CCC . n 
B 1 172 LEU 172 172 172 LEU LEU CCC . n 
B 1 173 ARG 173 173 173 ARG ARG CCC . n 
B 1 174 ALA 174 174 174 ALA ALA CCC . n 
B 1 175 GLU 175 175 175 GLU GLU CCC . n 
B 1 176 GLN 176 176 176 GLN GLN CCC . n 
B 1 177 ALA 177 177 177 ALA ALA CCC . n 
B 1 178 SER 178 178 178 SER SER CCC . n 
B 1 179 GLN 179 179 179 GLN GLN CCC . n 
B 1 180 GLU 180 180 180 GLU GLU CCC . n 
B 1 181 VAL 181 181 181 VAL VAL CCC . n 
B 1 182 LYS 182 182 182 LYS LYS CCC . n 
B 1 183 ASN 183 183 183 ASN ASN CCC . n 
B 1 184 ALA 184 184 184 ALA ALA CCC . n 
B 1 185 ALA 185 185 185 ALA ALA CCC . n 
B 1 186 THR 186 186 186 THR THR CCC . n 
B 1 187 GLU 187 187 187 GLU GLU CCC . n 
B 1 188 THR 188 188 188 THR THR CCC . n 
B 1 189 LEU 189 189 189 LEU LEU CCC . n 
B 1 190 LEU 190 190 190 LEU LEU CCC . n 
B 1 191 VAL 191 191 191 VAL VAL CCC . n 
B 1 192 GLN 192 192 192 GLN GLN CCC . n 
B 1 193 ASN 193 193 193 ASN ASN CCC . n 
B 1 194 ALA 194 194 194 ALA ALA CCC . n 
B 1 195 ASN 195 195 195 ASN ASN CCC . n 
B 1 196 PRO 196 196 196 PRO PRO CCC . n 
B 1 197 ASP 197 197 197 ASP ASP CCC . n 
B 1 198 CYS 198 198 198 CYS CYS CCC . n 
B 1 199 LYS 199 199 199 LYS LYS CCC . n 
B 1 200 THR 200 200 200 THR THR CCC . n 
B 1 201 ILE 201 201 201 ILE ILE CCC . n 
B 1 202 LEU 202 202 202 LEU LEU CCC . n 
B 1 203 LYS 203 203 203 LYS LYS CCC . n 
B 1 204 ALA 204 204 204 ALA ALA CCC . n 
B 1 205 LEU 205 205 205 LEU LEU CCC . n 
B 1 206 GLY 206 206 206 GLY GLY CCC . n 
B 1 207 PRO 207 207 207 PRO PRO CCC . n 
B 1 208 GLY 208 208 208 GLY GLY CCC . n 
B 1 209 ALA 209 209 209 ALA ALA CCC . n 
B 1 210 THR 210 210 210 THR THR CCC . n 
B 1 211 LEU 211 211 211 LEU LEU CCC . n 
B 1 212 GLU 212 212 212 GLU GLU CCC . n 
B 1 213 GLU 213 213 213 GLU GLU CCC . n 
B 1 214 MET 214 214 214 MET MET CCC . n 
B 1 215 MET 215 215 215 MET MET CCC . n 
B 1 216 THR 216 216 216 THR THR CCC . n 
B 1 217 ALA 217 217 217 ALA ALA CCC . n 
B 1 218 CYS 218 218 218 CYS CYS CCC . n 
B 1 219 GLN 219 219 219 GLN GLN CCC . n 
B 1 220 GLY 220 220 220 GLY GLY CCC . n 
B 1 221 VAL 221 221 221 VAL VAL CCC . n 
B 1 222 GLY 222 222 222 GLY GLY CCC . n 
C 1 1   PRO 1   1   1   PRO PRO AAA . n 
C 1 2   ILE 2   2   2   ILE ILE AAA . n 
C 1 3   VAL 3   3   3   VAL VAL AAA . n 
C 1 4   GLN 4   4   4   GLN GLN AAA . n 
C 1 5   ASN 5   5   5   ASN ASN AAA . n 
C 1 6   LEU 6   6   6   LEU LEU AAA . n 
C 1 7   GLN 7   7   7   GLN GLN AAA . n 
C 1 8   GLY 8   8   8   GLY GLY AAA . n 
C 1 9   GLN 9   9   9   GLN GLN AAA . n 
C 1 10  MET 10  10  10  MET MET AAA . n 
C 1 11  VAL 11  11  11  VAL VAL AAA . n 
C 1 12  HIS 12  12  12  HIS HIS AAA . n 
C 1 13  GLN 13  13  13  GLN GLN AAA . n 
C 1 14  CYS 14  14  14  CYS CYS AAA . n 
C 1 15  ILE 15  15  15  ILE ILE AAA . n 
C 1 16  SER 16  16  16  SER SER AAA . n 
C 1 17  PRO 17  17  17  PRO PRO AAA . n 
C 1 18  ARG 18  18  18  ARG ARG AAA . n 
C 1 19  THR 19  19  19  THR THR AAA . n 
C 1 20  LEU 20  20  20  LEU LEU AAA . n 
C 1 21  ASN 21  21  21  ASN ASN AAA . n 
C 1 22  ALA 22  22  22  ALA ALA AAA . n 
C 1 23  TRP 23  23  23  TRP TRP AAA . n 
C 1 24  VAL 24  24  24  VAL VAL AAA . n 
C 1 25  LYS 25  25  25  LYS LYS AAA . n 
C 1 26  VAL 26  26  26  VAL VAL AAA . n 
C 1 27  VAL 27  27  27  VAL VAL AAA . n 
C 1 28  GLU 28  28  28  GLU GLU AAA . n 
C 1 29  GLU 29  29  29  GLU GLU AAA . n 
C 1 30  LYS 30  30  30  LYS LYS AAA . n 
C 1 31  ALA 31  31  31  ALA ALA AAA . n 
C 1 32  PHE 32  32  32  PHE PHE AAA . n 
C 1 33  SER 33  33  33  SER SER AAA . n 
C 1 34  PRO 34  34  34  PRO PRO AAA . n 
C 1 35  GLU 35  35  35  GLU GLU AAA . n 
C 1 36  VAL 36  36  36  VAL VAL AAA . n 
C 1 37  ILE 37  37  37  ILE ILE AAA . n 
C 1 38  PRO 38  38  38  PRO PRO AAA . n 
C 1 39  MET 39  39  39  MET MET AAA . n 
C 1 40  PHE 40  40  40  PHE PHE AAA . n 
C 1 41  SER 41  41  41  SER SER AAA . n 
C 1 42  ALA 42  42  42  ALA ALA AAA . n 
C 1 43  LEU 43  43  43  LEU LEU AAA . n 
C 1 44  SER 44  44  44  SER SER AAA . n 
C 1 45  CYS 45  45  45  CYS CYS AAA . n 
C 1 46  GLY 46  46  46  GLY GLY AAA . n 
C 1 47  ALA 47  47  47  ALA ALA AAA . n 
C 1 48  THR 48  48  48  THR THR AAA . n 
C 1 49  PRO 49  49  49  PRO PRO AAA . n 
C 1 50  GLN 50  50  50  GLN GLN AAA . n 
C 1 51  ASP 51  51  51  ASP ASP AAA . n 
C 1 52  LEU 52  52  52  LEU LEU AAA . n 
C 1 53  ASN 53  53  53  ASN ASN AAA . n 
C 1 54  THR 54  54  54  THR THR AAA . n 
C 1 55  MET 55  55  55  MET MET AAA . n 
C 1 56  LEU 56  56  56  LEU LEU AAA . n 
C 1 57  ASN 57  57  57  ASN ASN AAA . n 
C 1 58  THR 58  58  58  THR THR AAA . n 
C 1 59  VAL 59  59  59  VAL VAL AAA . n 
C 1 60  GLY 60  60  60  GLY GLY AAA . n 
C 1 61  GLY 61  61  61  GLY GLY AAA . n 
C 1 62  HIS 62  62  62  HIS HIS AAA . n 
C 1 63  GLN 63  63  63  GLN GLN AAA . n 
C 1 64  ALA 64  64  64  ALA ALA AAA . n 
C 1 65  ALA 65  65  65  ALA ALA AAA . n 
C 1 66  MET 66  66  66  MET MET AAA . n 
C 1 67  GLN 67  67  67  GLN GLN AAA . n 
C 1 68  MET 68  68  68  MET MET AAA . n 
C 1 69  LEU 69  69  69  LEU LEU AAA . n 
C 1 70  LYS 70  70  70  LYS LYS AAA . n 
C 1 71  GLU 71  71  71  GLU GLU AAA . n 
C 1 72  THR 72  72  72  THR THR AAA . n 
C 1 73  ILE 73  73  73  ILE ILE AAA . n 
C 1 74  ASN 74  74  74  ASN ASN AAA . n 
C 1 75  GLU 75  75  75  GLU GLU AAA . n 
C 1 76  GLU 76  76  76  GLU GLU AAA . n 
C 1 77  ALA 77  77  77  ALA ALA AAA . n 
C 1 78  ALA 78  78  78  ALA ALA AAA . n 
C 1 79  GLU 79  79  79  GLU GLU AAA . n 
C 1 80  TRP 80  80  80  TRP TRP AAA . n 
C 1 81  ASP 81  81  81  ASP ASP AAA . n 
C 1 82  ARG 82  82  82  ARG ARG AAA . n 
C 1 83  LEU 83  83  83  LEU LEU AAA . n 
C 1 84  HIS 84  84  84  HIS HIS AAA . n 
C 1 85  PRO 85  85  85  PRO PRO AAA . n 
C 1 86  VAL 86  86  86  VAL VAL AAA . n 
C 1 87  HIS 87  87  87  HIS HIS AAA . n 
C 1 88  ALA 88  88  88  ALA ALA AAA . n 
C 1 89  GLY 89  89  89  GLY GLY AAA . n 
C 1 90  PRO 90  90  90  PRO PRO AAA . n 
C 1 91  ILE 91  91  91  ILE ILE AAA . n 
C 1 92  ALA 92  92  92  ALA ALA AAA . n 
C 1 93  PRO 93  93  93  PRO PRO AAA . n 
C 1 94  GLY 94  94  94  GLY GLY AAA . n 
C 1 95  GLN 95  95  95  GLN GLN AAA . n 
C 1 96  MET 96  96  96  MET MET AAA . n 
C 1 97  ARG 97  97  97  ARG ARG AAA . n 
C 1 98  GLU 98  98  98  GLU GLU AAA . n 
C 1 99  PRO 99  99  99  PRO PRO AAA . n 
C 1 100 ARG 100 100 100 ARG ARG AAA . n 
C 1 101 GLY 101 101 101 GLY GLY AAA . n 
C 1 102 SER 102 102 102 SER SER AAA . n 
C 1 103 ASP 103 103 103 ASP ASP AAA . n 
C 1 104 ILE 104 104 104 ILE ILE AAA . n 
C 1 105 ALA 105 105 105 ALA ALA AAA . n 
C 1 106 GLY 106 106 106 GLY GLY AAA . n 
C 1 107 THR 107 107 107 THR THR AAA . n 
C 1 108 THR 108 108 108 THR THR AAA . n 
C 1 109 SER 109 109 109 SER SER AAA . n 
C 1 110 THR 110 110 110 THR THR AAA . n 
C 1 111 LEU 111 111 111 LEU LEU AAA . n 
C 1 112 GLN 112 112 112 GLN GLN AAA . n 
C 1 113 GLU 113 113 113 GLU GLU AAA . n 
C 1 114 GLN 114 114 114 GLN GLN AAA . n 
C 1 115 ILE 115 115 115 ILE ILE AAA . n 
C 1 116 GLY 116 116 116 GLY GLY AAA . n 
C 1 117 TRP 117 117 117 TRP TRP AAA . n 
C 1 118 MET 118 118 118 MET MET AAA . n 
C 1 119 THR 119 119 119 THR THR AAA . n 
C 1 120 HIS 120 120 120 HIS HIS AAA . n 
C 1 121 ASN 121 121 121 ASN ASN AAA . n 
C 1 122 PRO 122 122 122 PRO PRO AAA . n 
C 1 123 PRO 123 123 123 PRO PRO AAA . n 
C 1 124 ILE 124 124 124 ILE ILE AAA . n 
C 1 125 PRO 125 125 125 PRO PRO AAA . n 
C 1 126 VAL 126 126 126 VAL VAL AAA . n 
C 1 127 GLY 127 127 127 GLY GLY AAA . n 
C 1 128 GLU 128 128 128 GLU GLU AAA . n 
C 1 129 ILE 129 129 129 ILE ILE AAA . n 
C 1 130 TYR 130 130 130 TYR TYR AAA . n 
C 1 131 LYS 131 131 131 LYS LYS AAA . n 
C 1 132 ARG 132 132 132 ARG ARG AAA . n 
C 1 133 TRP 133 133 133 TRP TRP AAA . n 
C 1 134 ILE 134 134 134 ILE ILE AAA . n 
C 1 135 ILE 135 135 135 ILE ILE AAA . n 
C 1 136 LEU 136 136 136 LEU LEU AAA . n 
C 1 137 GLY 137 137 137 GLY GLY AAA . n 
C 1 138 LEU 138 138 138 LEU LEU AAA . n 
C 1 139 ASN 139 139 139 ASN ASN AAA . n 
C 1 140 LYS 140 140 140 LYS LYS AAA . n 
C 1 141 ILE 141 141 141 ILE ILE AAA . n 
C 1 142 VAL 142 142 142 VAL VAL AAA . n 
C 1 143 ARG 143 143 143 ARG ARG AAA . n 
C 1 144 MET 144 144 144 MET MET AAA . n 
C 1 145 TYR 145 145 145 TYR TYR AAA . n 
C 1 146 SER 146 146 146 SER SER AAA . n 
C 1 147 PRO 147 147 147 PRO PRO AAA . n 
C 1 148 THR 148 148 148 THR THR AAA . n 
C 1 149 SER 149 149 149 SER SER AAA . n 
C 1 150 ILE 150 150 150 ILE ILE AAA . n 
C 1 151 LEU 151 151 151 LEU LEU AAA . n 
C 1 152 ASP 152 152 152 ASP ASP AAA . n 
C 1 153 ILE 153 153 153 ILE ILE AAA . n 
C 1 154 ARG 154 154 154 ARG ARG AAA . n 
C 1 155 GLN 155 155 155 GLN GLN AAA . n 
C 1 156 GLY 156 156 156 GLY GLY AAA . n 
C 1 157 PRO 157 157 157 PRO PRO AAA . n 
C 1 158 LYS 158 158 158 LYS LYS AAA . n 
C 1 159 GLU 159 159 159 GLU GLU AAA . n 
C 1 160 PRO 160 160 160 PRO PRO AAA . n 
C 1 161 PHE 161 161 161 PHE PHE AAA . n 
C 1 162 ARG 162 162 162 ARG ARG AAA . n 
C 1 163 ASP 163 163 163 ASP ASP AAA . n 
C 1 164 TYR 164 164 164 TYR TYR AAA . n 
C 1 165 VAL 165 165 165 VAL VAL AAA . n 
C 1 166 ASP 166 166 166 ASP ASP AAA . n 
C 1 167 ARG 167 167 167 ARG ARG AAA . n 
C 1 168 PHE 168 168 168 PHE PHE AAA . n 
C 1 169 TYR 169 169 169 TYR TYR AAA . n 
C 1 170 LYS 170 170 170 LYS LYS AAA . n 
C 1 171 THR 171 171 171 THR THR AAA . n 
C 1 172 LEU 172 172 172 LEU LEU AAA . n 
C 1 173 ARG 173 173 173 ARG ARG AAA . n 
C 1 174 ALA 174 174 174 ALA ALA AAA . n 
C 1 175 GLU 175 175 175 GLU GLU AAA . n 
C 1 176 GLN 176 176 176 GLN GLN AAA . n 
C 1 177 ALA 177 177 177 ALA ALA AAA . n 
C 1 178 SER 178 178 178 SER SER AAA . n 
C 1 179 GLN 179 179 179 GLN GLN AAA . n 
C 1 180 GLU 180 180 180 GLU GLU AAA . n 
C 1 181 VAL 181 181 181 VAL VAL AAA . n 
C 1 182 LYS 182 182 182 LYS LYS AAA . n 
C 1 183 ASN 183 183 183 ASN ASN AAA . n 
C 1 184 ALA 184 184 184 ALA ALA AAA . n 
C 1 185 ALA 185 185 185 ALA ALA AAA . n 
C 1 186 THR 186 186 186 THR THR AAA . n 
C 1 187 GLU 187 187 187 GLU GLU AAA . n 
C 1 188 THR 188 188 188 THR THR AAA . n 
C 1 189 LEU 189 189 189 LEU LEU AAA . n 
C 1 190 LEU 190 190 190 LEU LEU AAA . n 
C 1 191 VAL 191 191 191 VAL VAL AAA . n 
C 1 192 GLN 192 192 192 GLN GLN AAA . n 
C 1 193 ASN 193 193 193 ASN ASN AAA . n 
C 1 194 ALA 194 194 194 ALA ALA AAA . n 
C 1 195 ASN 195 195 195 ASN ASN AAA . n 
C 1 196 PRO 196 196 196 PRO PRO AAA . n 
C 1 197 ASP 197 197 197 ASP ASP AAA . n 
C 1 198 CYS 198 198 198 CYS CYS AAA . n 
C 1 199 LYS 199 199 199 LYS LYS AAA . n 
C 1 200 THR 200 200 200 THR THR AAA . n 
C 1 201 ILE 201 201 201 ILE ILE AAA . n 
C 1 202 LEU 202 202 202 LEU LEU AAA . n 
C 1 203 LYS 203 203 203 LYS LYS AAA . n 
C 1 204 ALA 204 204 204 ALA ALA AAA . n 
C 1 205 LEU 205 205 205 LEU LEU AAA . n 
C 1 206 GLY 206 206 206 GLY GLY AAA . n 
C 1 207 PRO 207 207 207 PRO PRO AAA . n 
C 1 208 GLY 208 208 208 GLY GLY AAA . n 
C 1 209 ALA 209 209 209 ALA ALA AAA . n 
C 1 210 THR 210 210 210 THR THR AAA . n 
C 1 211 LEU 211 211 211 LEU LEU AAA . n 
C 1 212 GLU 212 212 212 GLU GLU AAA . n 
C 1 213 GLU 213 213 213 GLU GLU AAA . n 
C 1 214 MET 214 214 214 MET MET AAA . n 
C 1 215 MET 215 215 215 MET MET AAA . n 
C 1 216 THR 216 216 216 THR THR AAA . n 
C 1 217 ALA 217 217 217 ALA ALA AAA . n 
C 1 218 CYS 218 218 218 CYS CYS AAA . n 
C 1 219 GLN 219 219 219 GLN GLN AAA . n 
C 1 220 GLY 220 220 ?   ?   ?   AAA . n 
C 1 221 VAL 221 221 ?   ?   ?   AAA . n 
C 1 222 GLY 222 222 ?   ?   ?   AAA . n 
D 2 1   ASP 1   1   1   ASP ASP FFF . n 
D 2 2   VAL 2   2   2   VAL VAL FFF . n 
D 2 3   GLN 3   3   3   GLN GLN FFF . n 
D 2 4   LEU 4   4   4   LEU LEU FFF . n 
D 2 5   GLN 5   5   5   GLN GLN FFF . n 
D 2 6   GLU 6   6   6   GLU GLU FFF . n 
D 2 7   SER 7   7   7   SER SER FFF . n 
D 2 8   GLY 8   8   8   GLY GLY FFF . n 
D 2 9   GLY 9   9   9   GLY GLY FFF . n 
D 2 10  GLY 10  10  10  GLY GLY FFF . n 
D 2 11  LEU 11  11  11  LEU LEU FFF . n 
D 2 12  VAL 12  12  12  VAL VAL FFF . n 
D 2 13  GLN 13  13  13  GLN GLN FFF . n 
D 2 14  ALA 14  14  14  ALA ALA FFF . n 
D 2 15  GLY 15  15  15  GLY GLY FFF . n 
D 2 16  GLY 16  16  16  GLY GLY FFF . n 
D 2 17  SER 17  17  17  SER SER FFF . n 
D 2 18  LEU 18  18  18  LEU LEU FFF . n 
D 2 19  ARG 19  19  19  ARG ARG FFF . n 
D 2 20  LEU 20  20  20  LEU LEU FFF . n 
D 2 21  SER 21  21  21  SER SER FFF . n 
D 2 22  CYS 22  22  22  CYS CYS FFF . n 
D 2 23  ALA 23  23  23  ALA ALA FFF . n 
D 2 24  ALA 24  24  24  ALA ALA FFF . n 
D 2 25  SER 25  25  25  SER SER FFF . n 
D 2 26  GLY 26  26  26  GLY GLY FFF . n 
D 2 27  SER 27  27  27  SER SER FFF . n 
D 2 28  ILE 28  28  28  ILE ILE FFF . n 
D 2 29  SER 29  29  29  SER SER FFF . n 
D 2 30  ARG 30  30  30  ARG ARG FFF . n 
D 2 31  PHE 31  31  31  PHE PHE FFF . n 
D 2 32  ASN 32  32  32  ASN ASN FFF . n 
D 2 33  ALA 33  33  33  ALA ALA FFF . n 
D 2 34  MET 34  34  34  MET MET FFF . n 
D 2 35  GLY 35  35  35  GLY GLY FFF . n 
D 2 36  TRP 36  36  36  TRP TRP FFF . n 
D 2 37  TRP 37  37  37  TRP TRP FFF . n 
D 2 38  ARG 38  38  38  ARG ARG FFF . n 
D 2 39  GLN 39  39  39  GLN GLN FFF . n 
D 2 40  ALA 40  40  40  ALA ALA FFF . n 
D 2 41  PRO 41  41  41  PRO PRO FFF . n 
D 2 42  GLY 42  42  42  GLY GLY FFF . n 
D 2 43  LYS 43  43  43  LYS LYS FFF . n 
D 2 44  GLU 44  44  44  GLU GLU FFF . n 
D 2 45  ARG 45  45  45  ARG ARG FFF . n 
D 2 46  GLU 46  46  46  GLU GLU FFF . n 
D 2 47  PHE 47  47  47  PHE PHE FFF . n 
D 2 48  VAL 48  48  48  VAL VAL FFF . n 
D 2 49  ALA 49  49  49  ALA ALA FFF . n 
D 2 50  ARG 50  50  50  ARG ARG FFF . n 
D 2 51  ILE 51  51  51  ILE ILE FFF . n 
D 2 52  VAL 52  52  52  VAL VAL FFF . n 
D 2 53  LYS 53  53  53  LYS LYS FFF . n 
D 2 54  GLY 54  54  54  GLY GLY FFF . n 
D 2 55  PHE 55  55  55  PHE PHE FFF . n 
D 2 56  ASP 56  56  56  ASP ASP FFF . n 
D 2 57  PRO 57  57  57  PRO PRO FFF . n 
D 2 58  VAL 58  58  58  VAL VAL FFF . n 
D 2 59  LEU 59  59  59  LEU LEU FFF . n 
D 2 60  ALA 60  60  60  ALA ALA FFF . n 
D 2 61  ASP 61  61  61  ASP ASP FFF . n 
D 2 62  SER 62  62  62  SER SER FFF . n 
D 2 63  VAL 63  63  63  VAL VAL FFF . n 
D 2 64  LYS 64  64  64  LYS LYS FFF . n 
D 2 65  GLY 65  65  65  GLY GLY FFF . n 
D 2 66  ARG 66  66  66  ARG ARG FFF . n 
D 2 67  PHE 67  67  67  PHE PHE FFF . n 
D 2 68  THR 68  68  68  THR THR FFF . n 
D 2 69  ILE 69  69  69  ILE ILE FFF . n 
D 2 70  SER 70  70  70  SER SER FFF . n 
D 2 71  ILE 71  71  71  ILE ILE FFF . n 
D 2 72  ASP 72  72  72  ASP ASP FFF . n 
D 2 73  SER 73  73  73  SER SER FFF . n 
D 2 74  ALA 74  74  74  ALA ALA FFF . n 
D 2 75  GLU 75  75  75  GLU GLU FFF . n 
D 2 76  ASN 76  76  76  ASN ASN FFF . n 
D 2 77  THR 77  77  77  THR THR FFF . n 
D 2 78  LEU 78  78  78  LEU LEU FFF . n 
D 2 79  ALA 79  79  79  ALA ALA FFF . n 
D 2 80  LEU 80  80  80  LEU LEU FFF . n 
D 2 81  GLN 81  81  81  GLN GLN FFF . n 
D 2 82  MET 82  82  82  MET MET FFF . n 
D 2 83  ASN 83  82  82  ASN ASN FFF A n 
D 2 84  ARG 84  82  82  ARG ARG FFF B n 
D 2 85  LEU 85  82  82  LEU LEU FFF C n 
D 2 86  LYS 86  83  83  LYS LYS FFF . n 
D 2 87  PRO 87  84  84  PRO PRO FFF . n 
D 2 88  GLU 88  85  85  GLU GLU FFF . n 
D 2 89  ASP 89  86  86  ASP ASP FFF . n 
D 2 90  THR 90  87  87  THR THR FFF . n 
D 2 91  ALA 91  88  88  ALA ALA FFF . n 
D 2 92  VAL 92  89  89  VAL VAL FFF . n 
D 2 93  TYR 93  90  90  TYR TYR FFF . n 
D 2 94  TYR 94  91  91  TYR TYR FFF . n 
D 2 95  CYS 95  92  92  CYS CYS FFF . n 
D 2 96  PHE 96  93  93  PHE PHE FFF . n 
D 2 97  ALA 97  94  94  ALA ALA FFF . n 
D 2 98  ALA 98  95  95  ALA ALA FFF . n 
D 2 99  LEU 99  96  96  LEU LEU FFF . n 
D 2 100 ASP 100 97  97  ASP ASP FFF . n 
D 2 101 THR 101 98  98  THR THR FFF . n 
D 2 102 UNK 102 99  ?   ?   ?   FFF . n 
D 2 103 UNK 103 100 ?   ?   ?   FFF . n 
D 2 104 ALA 104 101 101 ALA ALA FFF . n 
D 2 105 TYR 105 102 102 TYR TYR FFF . n 
D 2 106 TRP 106 103 103 TRP TRP FFF . n 
D 2 107 GLY 107 104 104 GLY GLY FFF . n 
D 2 108 GLN 108 105 105 GLN GLN FFF . n 
D 2 109 GLY 109 106 106 GLY GLY FFF . n 
D 2 110 THR 110 107 107 THR THR FFF . n 
D 2 111 GLN 111 108 108 GLN GLN FFF . n 
D 2 112 VAL 112 109 109 VAL VAL FFF . n 
D 2 113 THR 113 110 110 THR THR FFF . n 
D 2 114 VAL 114 111 111 VAL VAL FFF . n 
D 2 115 SER 115 112 112 SER SER FFF . n 
E 3 1   ASP 1   1   1   ASP ASP EEE . n 
E 3 2   VAL 2   2   2   VAL VAL EEE . n 
E 3 3   GLN 3   3   3   GLN GLN EEE . n 
E 3 4   LEU 4   4   4   LEU LEU EEE . n 
E 3 5   GLN 5   5   5   GLN GLN EEE . n 
E 3 6   GLU 6   6   6   GLU GLU EEE . n 
E 3 7   SER 7   7   7   SER SER EEE . n 
E 3 8   GLY 8   8   8   GLY GLY EEE . n 
E 3 9   GLY 9   9   9   GLY GLY EEE . n 
E 3 10  GLY 10  10  10  GLY GLY EEE . n 
E 3 11  LEU 11  11  11  LEU LEU EEE . n 
E 3 12  VAL 12  12  12  VAL VAL EEE . n 
E 3 13  GLN 13  13  13  GLN GLN EEE . n 
E 3 14  ALA 14  14  14  ALA ALA EEE . n 
E 3 15  GLY 15  15  15  GLY GLY EEE . n 
E 3 16  GLY 16  16  16  GLY GLY EEE . n 
E 3 17  SER 17  17  17  SER SER EEE . n 
E 3 18  LEU 18  18  18  LEU LEU EEE . n 
E 3 19  ARG 19  19  19  ARG ARG EEE . n 
E 3 20  LEU 20  20  20  LEU LEU EEE . n 
E 3 21  SER 21  21  21  SER SER EEE . n 
E 3 22  CYS 22  22  22  CYS CYS EEE . n 
E 3 23  ALA 23  23  23  ALA ALA EEE . n 
E 3 24  ALA 24  24  24  ALA ALA EEE . n 
E 3 25  SER 25  25  25  SER SER EEE . n 
E 3 26  GLY 26  26  26  GLY GLY EEE . n 
E 3 27  SER 27  27  27  SER SER EEE . n 
E 3 28  ILE 28  28  28  ILE ILE EEE . n 
E 3 29  SER 29  29  29  SER SER EEE . n 
E 3 30  ARG 30  30  30  ARG ARG EEE . n 
E 3 31  PHE 31  31  31  PHE PHE EEE . n 
E 3 32  ASN 32  32  32  ASN ASN EEE . n 
E 3 33  ALA 33  33  33  ALA ALA EEE . n 
E 3 34  MET 34  34  34  MET MET EEE . n 
E 3 35  GLY 35  35  35  GLY GLY EEE . n 
E 3 36  TRP 36  36  36  TRP TRP EEE . n 
E 3 37  TRP 37  37  37  TRP TRP EEE . n 
E 3 38  ARG 38  38  38  ARG ARG EEE . n 
E 3 39  GLN 39  39  39  GLN GLN EEE . n 
E 3 40  ALA 40  40  40  ALA ALA EEE . n 
E 3 41  PRO 41  41  41  PRO PRO EEE . n 
E 3 42  GLY 42  42  42  GLY GLY EEE . n 
E 3 43  LYS 43  43  43  LYS LYS EEE . n 
E 3 44  GLU 44  44  44  GLU GLU EEE . n 
E 3 45  ARG 45  45  45  ARG ARG EEE . n 
E 3 46  GLU 46  46  46  GLU GLU EEE . n 
E 3 47  PHE 47  47  47  PHE PHE EEE . n 
E 3 48  VAL 48  48  48  VAL VAL EEE . n 
E 3 49  ALA 49  49  49  ALA ALA EEE . n 
E 3 50  ARG 50  50  50  ARG ARG EEE . n 
E 3 51  ILE 51  51  51  ILE ILE EEE . n 
E 3 52  VAL 52  52  52  VAL VAL EEE . n 
E 3 53  LYS 53  53  53  LYS LYS EEE . n 
E 3 54  GLY 54  54  54  GLY GLY EEE . n 
E 3 55  PHE 55  55  55  PHE PHE EEE . n 
E 3 56  ASP 56  56  56  ASP ASP EEE . n 
E 3 57  PRO 57  57  57  PRO PRO EEE . n 
E 3 58  VAL 58  58  58  VAL VAL EEE . n 
E 3 59  LEU 59  59  59  LEU LEU EEE . n 
E 3 60  ALA 60  60  60  ALA ALA EEE . n 
E 3 61  ASP 61  61  61  ASP ASP EEE . n 
E 3 62  SER 62  62  62  SER SER EEE . n 
E 3 63  VAL 63  63  63  VAL VAL EEE . n 
E 3 64  LYS 64  64  64  LYS LYS EEE . n 
E 3 65  GLY 65  65  65  GLY GLY EEE . n 
E 3 66  ARG 66  66  66  ARG ARG EEE . n 
E 3 67  PHE 67  67  67  PHE PHE EEE . n 
E 3 68  THR 68  68  68  THR THR EEE . n 
E 3 69  ILE 69  69  69  ILE ILE EEE . n 
E 3 70  SER 70  70  70  SER SER EEE . n 
E 3 71  ILE 71  71  71  ILE ILE EEE . n 
E 3 72  ASP 72  72  72  ASP ASP EEE . n 
E 3 73  SER 73  73  73  SER SER EEE . n 
E 3 74  ALA 74  74  74  ALA ALA EEE . n 
E 3 75  GLU 75  75  75  GLU GLU EEE . n 
E 3 76  ASN 76  76  76  ASN ASN EEE . n 
E 3 77  THR 77  77  77  THR THR EEE . n 
E 3 78  LEU 78  78  78  LEU LEU EEE . n 
E 3 79  ALA 79  79  79  ALA ALA EEE . n 
E 3 80  LEU 80  80  80  LEU LEU EEE . n 
E 3 81  GLN 81  81  81  GLN GLN EEE . n 
E 3 82  MET 82  82  82  MET MET EEE . n 
E 3 83  ASN 83  82  82  ASN ASN EEE A n 
E 3 84  ARG 84  82  82  ARG ARG EEE B n 
E 3 85  LEU 85  82  82  LEU LEU EEE C n 
E 3 86  LYS 86  83  83  LYS LYS EEE . n 
E 3 87  PRO 87  84  84  PRO PRO EEE . n 
E 3 88  GLU 88  85  85  GLU GLU EEE . n 
E 3 89  ASP 89  86  86  ASP ASP EEE . n 
E 3 90  THR 90  87  87  THR THR EEE . n 
E 3 91  ALA 91  88  88  ALA ALA EEE . n 
E 3 92  VAL 92  89  89  VAL VAL EEE . n 
E 3 93  TYR 93  90  90  TYR TYR EEE . n 
E 3 94  TYR 94  91  91  TYR TYR EEE . n 
E 3 95  CYS 95  92  92  CYS CYS EEE . n 
E 3 96  PHE 96  93  93  PHE PHE EEE . n 
E 3 97  ALA 97  94  94  ALA ALA EEE . n 
E 3 98  ALA 98  95  95  ALA ALA EEE . n 
E 3 99  LEU 99  96  96  LEU LEU EEE . n 
E 3 100 ASP 100 97  97  ASP ASP EEE . n 
E 3 101 THR 101 98  98  THR THR EEE . n 
E 3 102 ALA 102 101 101 ALA ALA EEE . n 
E 3 103 TYR 103 102 102 TYR TYR EEE . n 
E 3 104 TRP 104 103 103 TRP TRP EEE . n 
E 3 105 GLY 105 104 104 GLY GLY EEE . n 
E 3 106 GLN 106 105 105 GLN GLN EEE . n 
E 3 107 GLY 107 106 106 GLY GLY EEE . n 
E 3 108 THR 108 107 107 THR THR EEE . n 
E 3 109 GLN 109 108 108 GLN GLN EEE . n 
E 3 110 VAL 110 109 109 VAL VAL EEE . n 
E 3 111 THR 111 110 110 THR THR EEE . n 
E 3 112 VAL 112 111 111 VAL VAL EEE . n 
F 4 1   VAL 1   2   2   VAL VAL DDD . n 
F 4 2   GLN 2   3   3   GLN GLN DDD . n 
F 4 3   LEU 3   4   4   LEU LEU DDD . n 
F 4 4   GLN 4   5   5   GLN GLN DDD . n 
F 4 5   GLU 5   6   6   GLU GLU DDD . n 
F 4 6   SER 6   7   7   SER SER DDD . n 
F 4 7   GLY 7   8   8   GLY GLY DDD . n 
F 4 8   GLY 8   9   9   GLY GLY DDD . n 
F 4 9   GLY 9   10  10  GLY GLY DDD . n 
F 4 10  LEU 10  11  11  LEU LEU DDD . n 
F 4 11  VAL 11  12  12  VAL VAL DDD . n 
F 4 12  GLN 12  13  13  GLN GLN DDD . n 
F 4 13  ALA 13  14  14  ALA ALA DDD . n 
F 4 14  GLY 14  15  15  GLY GLY DDD . n 
F 4 15  GLY 15  16  16  GLY GLY DDD . n 
F 4 16  SER 16  17  17  SER SER DDD . n 
F 4 17  LEU 17  18  18  LEU LEU DDD . n 
F 4 18  ARG 18  19  19  ARG ARG DDD . n 
F 4 19  LEU 19  20  20  LEU LEU DDD . n 
F 4 20  SER 20  21  21  SER SER DDD . n 
F 4 21  CYS 21  22  22  CYS CYS DDD . n 
F 4 22  ALA 22  23  23  ALA ALA DDD . n 
F 4 23  ALA 23  24  24  ALA ALA DDD . n 
F 4 24  SER 24  25  25  SER SER DDD . n 
F 4 25  GLY 25  26  26  GLY GLY DDD . n 
F 4 26  SER 26  27  27  SER SER DDD . n 
F 4 27  ILE 27  28  28  ILE ILE DDD . n 
F 4 28  SER 28  29  29  SER SER DDD . n 
F 4 29  ARG 29  30  30  ARG ARG DDD . n 
F 4 30  PHE 30  31  31  PHE PHE DDD . n 
F 4 31  ASN 31  32  32  ASN ASN DDD . n 
F 4 32  ALA 32  33  33  ALA ALA DDD . n 
F 4 33  MET 33  34  34  MET MET DDD . n 
F 4 34  GLY 34  35  35  GLY GLY DDD . n 
F 4 35  TRP 35  36  36  TRP TRP DDD . n 
F 4 36  TRP 36  37  37  TRP TRP DDD . n 
F 4 37  ARG 37  38  38  ARG ARG DDD . n 
F 4 38  GLN 38  39  39  GLN GLN DDD . n 
F 4 39  ALA 39  40  40  ALA ALA DDD . n 
F 4 40  PRO 40  41  41  PRO PRO DDD . n 
F 4 41  GLY 41  42  42  GLY GLY DDD . n 
F 4 42  LYS 42  43  43  LYS LYS DDD . n 
F 4 43  GLU 43  44  44  GLU GLU DDD . n 
F 4 44  ARG 44  45  45  ARG ARG DDD . n 
F 4 45  GLU 45  46  46  GLU GLU DDD . n 
F 4 46  PHE 46  47  47  PHE PHE DDD . n 
F 4 47  VAL 47  48  48  VAL VAL DDD . n 
F 4 48  ALA 48  49  49  ALA ALA DDD . n 
F 4 49  ARG 49  50  50  ARG ARG DDD . n 
F 4 50  ILE 50  51  51  ILE ILE DDD . n 
F 4 51  VAL 51  52  52  VAL VAL DDD . n 
F 4 52  LYS 52  53  53  LYS LYS DDD . n 
F 4 53  GLY 53  54  54  GLY GLY DDD . n 
F 4 54  PHE 54  55  55  PHE PHE DDD . n 
F 4 55  ASP 55  56  56  ASP ASP DDD . n 
F 4 56  PRO 56  57  57  PRO PRO DDD . n 
F 4 57  VAL 57  58  58  VAL VAL DDD . n 
F 4 58  LEU 58  59  59  LEU LEU DDD . n 
F 4 59  ALA 59  60  60  ALA ALA DDD . n 
F 4 60  ASP 60  61  61  ASP ASP DDD . n 
F 4 61  SER 61  62  62  SER SER DDD . n 
F 4 62  VAL 62  63  63  VAL VAL DDD . n 
F 4 63  LYS 63  64  64  LYS LYS DDD . n 
F 4 64  GLY 64  65  65  GLY GLY DDD . n 
F 4 65  ARG 65  66  66  ARG ARG DDD . n 
F 4 66  PHE 66  67  67  PHE PHE DDD . n 
F 4 67  THR 67  68  68  THR THR DDD . n 
F 4 68  ILE 68  69  69  ILE ILE DDD . n 
F 4 69  SER 69  70  70  SER SER DDD . n 
F 4 70  ILE 70  71  71  ILE ILE DDD . n 
F 4 71  ASP 71  72  72  ASP ASP DDD . n 
F 4 72  SER 72  73  73  SER SER DDD . n 
F 4 73  ALA 73  74  74  ALA ALA DDD . n 
F 4 74  GLU 74  75  75  GLU GLU DDD . n 
F 4 75  ASN 75  76  76  ASN ASN DDD . n 
F 4 76  THR 76  77  77  THR THR DDD . n 
F 4 77  LEU 77  78  78  LEU LEU DDD . n 
F 4 78  ALA 78  79  79  ALA ALA DDD . n 
F 4 79  LEU 79  80  80  LEU LEU DDD . n 
F 4 80  GLN 80  81  81  GLN GLN DDD . n 
F 4 81  ARG 81  82  82  ARG ARG DDD . n 
F 4 82  ASN 82  82  82  ASN ASN DDD A n 
F 4 83  ARG 83  82  82  ARG ARG DDD B n 
F 4 84  LEU 84  82  82  LEU LEU DDD C n 
F 4 85  LYS 85  83  83  LYS LYS DDD . n 
F 4 86  PRO 86  84  84  PRO PRO DDD . n 
F 4 87  GLU 87  85  85  GLU GLU DDD . n 
F 4 88  ASP 88  86  86  ASP ASP DDD . n 
F 4 89  THR 89  87  87  THR THR DDD . n 
F 4 90  ALA 90  88  88  ALA ALA DDD . n 
F 4 91  VAL 91  89  89  VAL VAL DDD . n 
F 4 92  TYR 92  90  90  TYR TYR DDD . n 
F 4 93  TYR 93  91  91  TYR TYR DDD . n 
F 4 94  CYS 94  92  92  CYS CYS DDD . n 
F 4 95  PHE 95  93  93  PHE PHE DDD . n 
F 4 96  ALA 96  94  94  ALA ALA DDD . n 
F 4 97  ALA 97  95  95  ALA ALA DDD . n 
F 4 98  LEU 98  96  96  LEU LEU DDD . n 
F 4 99  ASP 99  97  97  ASP ASP DDD . n 
F 4 100 THR 100 98  98  THR THR DDD . n 
F 4 101 UNK 101 99  ?   ?   ?   DDD . n 
F 4 102 UNK 102 100 ?   ?   ?   DDD . n 
F 4 103 ALA 103 101 101 ALA ALA DDD . n 
F 4 104 TYR 104 102 102 TYR TYR DDD . n 
F 4 105 TRP 105 103 103 TRP TRP DDD . n 
F 4 106 GLY 106 104 104 GLY GLY DDD . n 
F 4 107 GLN 107 105 105 GLN GLN DDD . n 
F 4 108 GLY 108 106 106 GLY GLY DDD . n 
F 4 109 THR 109 107 107 THR THR DDD . n 
F 4 110 GLN 110 108 108 GLN GLN DDD . n 
F 4 111 VAL 111 109 109 VAL VAL DDD . n 
F 4 112 THR 112 110 110 THR THR DDD . n 
F 4 113 VAL 113 111 111 VAL VAL DDD . n 
F 4 114 SER 114 112 112 SER SER DDD . n 
G 5 1   MET 1   1   1   MET MET GGG . n 
G 5 2   VAL 2   2   2   VAL VAL GGG . n 
G 5 3   ASN 3   3   3   ASN ASN GGG . n 
G 5 4   PRO 4   4   4   PRO PRO GGG . n 
G 5 5   THR 5   5   5   THR THR GGG . n 
G 5 6   VAL 6   6   6   VAL VAL GGG . n 
G 5 7   PHE 7   7   7   PHE PHE GGG . n 
G 5 8   PHE 8   8   8   PHE PHE GGG . n 
G 5 9   ASP 9   9   9   ASP ASP GGG . n 
G 5 10  ILE 10  10  10  ILE ILE GGG . n 
G 5 11  ALA 11  11  11  ALA ALA GGG . n 
G 5 12  VAL 12  12  12  VAL VAL GGG . n 
G 5 13  ASP 13  13  13  ASP ASP GGG . n 
G 5 14  GLY 14  14  14  GLY GLY GGG . n 
G 5 15  GLU 15  15  15  GLU GLU GGG . n 
G 5 16  PRO 16  16  16  PRO PRO GGG . n 
G 5 17  LEU 17  17  17  LEU LEU GGG . n 
G 5 18  GLY 18  18  18  GLY GLY GGG . n 
G 5 19  ARG 19  19  19  ARG ARG GGG . n 
G 5 20  VAL 20  20  20  VAL VAL GGG . n 
G 5 21  SER 21  21  21  SER SER GGG . n 
G 5 22  PHE 22  22  22  PHE PHE GGG . n 
G 5 23  GLU 23  23  23  GLU GLU GGG . n 
G 5 24  LEU 24  24  24  LEU LEU GGG . n 
G 5 25  PHE 25  25  25  PHE PHE GGG . n 
G 5 26  ALA 26  26  26  ALA ALA GGG . n 
G 5 27  ASP 27  27  27  ASP ASP GGG . n 
G 5 28  LYS 28  28  28  LYS LYS GGG . n 
G 5 29  VAL 29  29  29  VAL VAL GGG . n 
G 5 30  PRO 30  30  30  PRO PRO GGG . n 
G 5 31  LYS 31  31  31  LYS LYS GGG . n 
G 5 32  THR 32  32  32  THR THR GGG . n 
G 5 33  ALA 33  33  33  ALA ALA GGG . n 
G 5 34  GLU 34  34  34  GLU GLU GGG . n 
G 5 35  ASN 35  35  35  ASN ASN GGG . n 
G 5 36  PHE 36  36  36  PHE PHE GGG . n 
G 5 37  ARG 37  37  37  ARG ARG GGG . n 
G 5 38  ALA 38  38  38  ALA ALA GGG . n 
G 5 39  LEU 39  39  39  LEU LEU GGG . n 
G 5 40  SER 40  40  40  SER SER GGG . n 
G 5 41  THR 41  41  41  THR THR GGG . n 
G 5 42  GLY 42  42  42  GLY GLY GGG . n 
G 5 43  GLU 43  43  43  GLU GLU GGG . n 
G 5 44  LYS 44  44  44  LYS LYS GGG . n 
G 5 45  GLY 45  45  45  GLY GLY GGG . n 
G 5 46  PHE 46  46  46  PHE PHE GGG . n 
G 5 47  GLY 47  47  47  GLY GLY GGG . n 
G 5 48  TYR 48  48  48  TYR TYR GGG . n 
G 5 49  LYS 49  49  49  LYS LYS GGG . n 
G 5 50  GLY 50  50  50  GLY GLY GGG . n 
G 5 51  SER 51  51  51  SER SER GGG . n 
G 5 52  CYS 52  52  52  CYS CYS GGG . n 
G 5 53  PHE 53  53  53  PHE PHE GGG . n 
G 5 54  HIS 54  54  54  HIS HIS GGG . n 
G 5 55  ARG 55  55  55  ARG ARG GGG . n 
G 5 56  ILE 56  56  56  ILE ILE GGG . n 
G 5 57  ILE 57  57  57  ILE ILE GGG . n 
G 5 58  PRO 58  58  58  PRO PRO GGG . n 
G 5 59  GLY 59  59  59  GLY GLY GGG . n 
G 5 60  PHE 60  60  60  PHE PHE GGG . n 
G 5 61  MET 61  61  61  MET MET GGG . n 
G 5 62  CYS 62  62  62  CYS CYS GGG . n 
G 5 63  GLN 63  63  63  GLN GLN GGG . n 
G 5 64  GLY 64  64  64  GLY GLY GGG . n 
G 5 65  GLY 65  65  65  GLY GLY GGG . n 
G 5 66  ASP 66  66  66  ASP ASP GGG . n 
G 5 67  PHE 67  67  67  PHE PHE GGG . n 
G 5 68  THR 68  68  68  THR THR GGG . n 
G 5 69  ARG 69  69  69  ARG ARG GGG . n 
G 5 70  HIS 70  70  70  HIS HIS GGG . n 
G 5 71  ASN 71  71  71  ASN ASN GGG . n 
G 5 72  GLY 72  72  72  GLY GLY GGG . n 
G 5 73  THR 73  73  73  THR THR GGG . n 
G 5 74  GLY 74  74  74  GLY GLY GGG . n 
G 5 75  GLY 75  75  75  GLY GLY GGG . n 
G 5 76  LYS 76  76  76  LYS LYS GGG . n 
G 5 77  SER 77  77  77  SER SER GGG . n 
G 5 78  ILE 78  78  78  ILE ILE GGG . n 
G 5 79  TYR 79  79  79  TYR TYR GGG . n 
G 5 80  GLY 80  80  80  GLY GLY GGG . n 
G 5 81  GLU 81  81  81  GLU GLU GGG . n 
G 5 82  LYS 82  82  82  LYS LYS GGG . n 
G 5 83  PHE 83  83  83  PHE PHE GGG . n 
G 5 84  GLU 84  84  84  GLU GLU GGG . n 
G 5 85  ASP 85  85  85  ASP ASP GGG . n 
G 5 86  GLU 86  86  86  GLU GLU GGG . n 
G 5 87  ASN 87  87  87  ASN ASN GGG . n 
G 5 88  PHE 88  88  88  PHE PHE GGG . n 
G 5 89  ILE 89  89  89  ILE ILE GGG . n 
G 5 90  LEU 90  90  90  LEU LEU GGG . n 
G 5 91  LYS 91  91  91  LYS LYS GGG . n 
G 5 92  HIS 92  92  92  HIS HIS GGG . n 
G 5 93  THR 93  93  93  THR THR GGG . n 
G 5 94  GLY 94  94  94  GLY GLY GGG . n 
G 5 95  PRO 95  95  95  PRO PRO GGG . n 
G 5 96  GLY 96  96  96  GLY GLY GGG . n 
G 5 97  ILE 97  97  97  ILE ILE GGG . n 
G 5 98  LEU 98  98  98  LEU LEU GGG . n 
G 5 99  SER 99  99  99  SER SER GGG . n 
G 5 100 MET 100 100 100 MET MET GGG . n 
G 5 101 ALA 101 101 101 ALA ALA GGG . n 
G 5 102 ASN 102 102 102 ASN ASN GGG . n 
G 5 103 ALA 103 103 103 ALA ALA GGG . n 
G 5 104 GLY 104 104 104 GLY GLY GGG . n 
G 5 105 PRO 105 105 105 PRO PRO GGG . n 
G 5 106 ASN 106 106 106 ASN ASN GGG . n 
G 5 107 THR 107 107 107 THR THR GGG . n 
G 5 108 ASN 108 108 108 ASN ASN GGG . n 
G 5 109 GLY 109 109 109 GLY GLY GGG . n 
G 5 110 SER 110 110 110 SER SER GGG . n 
G 5 111 GLN 111 111 111 GLN GLN GGG . n 
G 5 112 PHE 112 112 112 PHE PHE GGG . n 
G 5 113 PHE 113 113 113 PHE PHE GGG . n 
G 5 114 ILE 114 114 114 ILE ILE GGG . n 
G 5 115 CYS 115 115 115 CYS CYS GGG . n 
G 5 116 THR 116 116 116 THR THR GGG . n 
G 5 117 ALA 117 117 117 ALA ALA GGG . n 
G 5 118 LYS 118 118 118 LYS LYS GGG . n 
G 5 119 THR 119 119 119 THR THR GGG . n 
G 5 120 GLU 120 120 120 GLU GLU GGG . n 
G 5 121 TRP 121 121 121 TRP TRP GGG . n 
G 5 122 LEU 122 122 122 LEU LEU GGG . n 
G 5 123 ASP 123 123 123 ASP ASP GGG . n 
G 5 124 GLY 124 124 124 GLY GLY GGG . n 
G 5 125 LYS 125 125 125 LYS LYS GGG . n 
G 5 126 HIS 126 126 126 HIS HIS GGG . n 
G 5 127 VAL 127 127 127 VAL VAL GGG . n 
G 5 128 VAL 128 128 128 VAL VAL GGG . n 
G 5 129 PHE 129 129 129 PHE PHE GGG . n 
G 5 130 GLY 130 130 130 GLY GLY GGG . n 
G 5 131 LYS 131 131 131 LYS LYS GGG . n 
G 5 132 VAL 132 132 132 VAL VAL GGG . n 
G 5 133 LYS 133 133 133 LYS LYS GGG . n 
G 5 134 GLU 134 134 134 GLU GLU GGG . n 
G 5 135 GLY 135 135 135 GLY GLY GGG . n 
G 5 136 MET 136 136 136 MET MET GGG . n 
G 5 137 ASN 137 137 137 ASN ASN GGG . n 
G 5 138 ILE 138 138 138 ILE ILE GGG . n 
G 5 139 VAL 139 139 139 VAL VAL GGG . n 
G 5 140 GLU 140 140 140 GLU GLU GGG . n 
G 5 141 ALA 141 141 141 ALA ALA GGG . n 
G 5 142 MET 142 142 142 MET MET GGG . n 
G 5 143 GLU 143 143 143 GLU GLU GGG . n 
G 5 144 ARG 144 144 144 ARG ARG GGG . n 
G 5 145 PHE 145 145 145 PHE PHE GGG . n 
G 5 146 GLY 146 146 146 GLY GLY GGG . n 
G 5 147 SER 147 147 147 SER SER GGG . n 
G 5 148 ARG 148 148 148 ARG ARG GGG . n 
G 5 149 ASN 149 149 149 ASN ASN GGG . n 
G 5 150 GLY 150 150 150 GLY GLY GGG . n 
G 5 151 LYS 151 151 151 LYS LYS GGG . n 
G 5 152 THR 152 152 152 THR THR GGG . n 
G 5 153 SER 153 153 153 SER SER GGG . n 
G 5 154 LYS 154 154 154 LYS LYS GGG . n 
G 5 155 LYS 155 155 155 LYS LYS GGG . n 
G 5 156 ILE 156 156 156 ILE ILE GGG . n 
G 5 157 THR 157 157 157 THR THR GGG . n 
G 5 158 ILE 158 158 158 ILE ILE GGG . n 
G 5 159 ALA 159 159 159 ALA ALA GGG . n 
G 5 160 ASP 160 160 160 ASP ASP GGG . n 
G 5 161 CYS 161 161 161 CYS CYS GGG . n 
G 5 162 GLY 162 162 162 GLY GLY GGG . n 
G 5 163 GLN 163 163 163 GLN GLN GGG . n 
G 5 164 LEU 164 164 164 LEU LEU GGG . n 
G 5 165 GLU 165 165 165 GLU GLU GGG . n 
H 5 1   MET 1   1   ?   ?   ?   HHH . n 
H 5 2   VAL 2   2   ?   ?   ?   HHH . n 
H 5 3   ASN 3   3   3   ASN ASN HHH . n 
H 5 4   PRO 4   4   4   PRO PRO HHH . n 
H 5 5   THR 5   5   5   THR THR HHH . n 
H 5 6   VAL 6   6   6   VAL VAL HHH . n 
H 5 7   PHE 7   7   7   PHE PHE HHH . n 
H 5 8   PHE 8   8   8   PHE PHE HHH . n 
H 5 9   ASP 9   9   9   ASP ASP HHH . n 
H 5 10  ILE 10  10  10  ILE ILE HHH . n 
H 5 11  ALA 11  11  11  ALA ALA HHH . n 
H 5 12  VAL 12  12  12  VAL VAL HHH . n 
H 5 13  ASP 13  13  13  ASP ASP HHH . n 
H 5 14  GLY 14  14  14  GLY GLY HHH . n 
H 5 15  GLU 15  15  15  GLU GLU HHH . n 
H 5 16  PRO 16  16  16  PRO PRO HHH . n 
H 5 17  LEU 17  17  17  LEU LEU HHH . n 
H 5 18  GLY 18  18  18  GLY GLY HHH . n 
H 5 19  ARG 19  19  19  ARG ARG HHH . n 
H 5 20  VAL 20  20  20  VAL VAL HHH . n 
H 5 21  SER 21  21  21  SER SER HHH . n 
H 5 22  PHE 22  22  22  PHE PHE HHH . n 
H 5 23  GLU 23  23  23  GLU GLU HHH . n 
H 5 24  LEU 24  24  24  LEU LEU HHH . n 
H 5 25  PHE 25  25  25  PHE PHE HHH . n 
H 5 26  ALA 26  26  26  ALA ALA HHH . n 
H 5 27  ASP 27  27  27  ASP ASP HHH . n 
H 5 28  LYS 28  28  28  LYS LYS HHH . n 
H 5 29  VAL 29  29  29  VAL VAL HHH . n 
H 5 30  PRO 30  30  30  PRO PRO HHH . n 
H 5 31  LYS 31  31  31  LYS LYS HHH . n 
H 5 32  THR 32  32  32  THR THR HHH . n 
H 5 33  ALA 33  33  33  ALA ALA HHH . n 
H 5 34  GLU 34  34  34  GLU GLU HHH . n 
H 5 35  ASN 35  35  35  ASN ASN HHH . n 
H 5 36  PHE 36  36  36  PHE PHE HHH . n 
H 5 37  ARG 37  37  37  ARG ARG HHH . n 
H 5 38  ALA 38  38  38  ALA ALA HHH . n 
H 5 39  LEU 39  39  39  LEU LEU HHH . n 
H 5 40  SER 40  40  40  SER SER HHH . n 
H 5 41  THR 41  41  41  THR THR HHH . n 
H 5 42  GLY 42  42  42  GLY GLY HHH . n 
H 5 43  GLU 43  43  43  GLU GLU HHH . n 
H 5 44  LYS 44  44  44  LYS LYS HHH . n 
H 5 45  GLY 45  45  45  GLY GLY HHH . n 
H 5 46  PHE 46  46  46  PHE PHE HHH . n 
H 5 47  GLY 47  47  47  GLY GLY HHH . n 
H 5 48  TYR 48  48  48  TYR TYR HHH . n 
H 5 49  LYS 49  49  49  LYS LYS HHH . n 
H 5 50  GLY 50  50  50  GLY GLY HHH . n 
H 5 51  SER 51  51  51  SER SER HHH . n 
H 5 52  CYS 52  52  52  CYS CYS HHH . n 
H 5 53  PHE 53  53  53  PHE PHE HHH . n 
H 5 54  HIS 54  54  54  HIS HIS HHH . n 
H 5 55  ARG 55  55  55  ARG ARG HHH . n 
H 5 56  ILE 56  56  56  ILE ILE HHH . n 
H 5 57  ILE 57  57  57  ILE ILE HHH . n 
H 5 58  PRO 58  58  58  PRO PRO HHH . n 
H 5 59  GLY 59  59  59  GLY GLY HHH . n 
H 5 60  PHE 60  60  60  PHE PHE HHH . n 
H 5 61  MET 61  61  61  MET MET HHH . n 
H 5 62  CYS 62  62  62  CYS CYS HHH . n 
H 5 63  GLN 63  63  63  GLN GLN HHH . n 
H 5 64  GLY 64  64  64  GLY GLY HHH . n 
H 5 65  GLY 65  65  65  GLY GLY HHH . n 
H 5 66  ASP 66  66  66  ASP ASP HHH . n 
H 5 67  PHE 67  67  67  PHE PHE HHH . n 
H 5 68  THR 68  68  68  THR THR HHH . n 
H 5 69  ARG 69  69  69  ARG ARG HHH . n 
H 5 70  HIS 70  70  70  HIS HIS HHH . n 
H 5 71  ASN 71  71  71  ASN ASN HHH . n 
H 5 72  GLY 72  72  72  GLY GLY HHH . n 
H 5 73  THR 73  73  73  THR THR HHH . n 
H 5 74  GLY 74  74  74  GLY GLY HHH . n 
H 5 75  GLY 75  75  75  GLY GLY HHH . n 
H 5 76  LYS 76  76  76  LYS LYS HHH . n 
H 5 77  SER 77  77  77  SER SER HHH . n 
H 5 78  ILE 78  78  78  ILE ILE HHH . n 
H 5 79  TYR 79  79  79  TYR TYR HHH . n 
H 5 80  GLY 80  80  80  GLY GLY HHH . n 
H 5 81  GLU 81  81  81  GLU GLU HHH . n 
H 5 82  LYS 82  82  82  LYS LYS HHH . n 
H 5 83  PHE 83  83  83  PHE PHE HHH . n 
H 5 84  GLU 84  84  84  GLU GLU HHH . n 
H 5 85  ASP 85  85  85  ASP ASP HHH . n 
H 5 86  GLU 86  86  86  GLU GLU HHH . n 
H 5 87  ASN 87  87  87  ASN ASN HHH . n 
H 5 88  PHE 88  88  88  PHE PHE HHH . n 
H 5 89  ILE 89  89  89  ILE ILE HHH . n 
H 5 90  LEU 90  90  90  LEU LEU HHH . n 
H 5 91  LYS 91  91  91  LYS LYS HHH . n 
H 5 92  HIS 92  92  92  HIS HIS HHH . n 
H 5 93  THR 93  93  93  THR THR HHH . n 
H 5 94  GLY 94  94  94  GLY GLY HHH . n 
H 5 95  PRO 95  95  95  PRO PRO HHH . n 
H 5 96  GLY 96  96  96  GLY GLY HHH . n 
H 5 97  ILE 97  97  97  ILE ILE HHH . n 
H 5 98  LEU 98  98  98  LEU LEU HHH . n 
H 5 99  SER 99  99  99  SER SER HHH . n 
H 5 100 MET 100 100 100 MET MET HHH . n 
H 5 101 ALA 101 101 101 ALA ALA HHH . n 
H 5 102 ASN 102 102 102 ASN ASN HHH . n 
H 5 103 ALA 103 103 103 ALA ALA HHH . n 
H 5 104 GLY 104 104 104 GLY GLY HHH . n 
H 5 105 PRO 105 105 105 PRO PRO HHH . n 
H 5 106 ASN 106 106 106 ASN ASN HHH . n 
H 5 107 THR 107 107 107 THR THR HHH . n 
H 5 108 ASN 108 108 108 ASN ASN HHH . n 
H 5 109 GLY 109 109 109 GLY GLY HHH . n 
H 5 110 SER 110 110 110 SER SER HHH . n 
H 5 111 GLN 111 111 111 GLN GLN HHH . n 
H 5 112 PHE 112 112 112 PHE PHE HHH . n 
H 5 113 PHE 113 113 113 PHE PHE HHH . n 
H 5 114 ILE 114 114 114 ILE ILE HHH . n 
H 5 115 CYS 115 115 115 CYS CYS HHH . n 
H 5 116 THR 116 116 116 THR THR HHH . n 
H 5 117 ALA 117 117 117 ALA ALA HHH . n 
H 5 118 LYS 118 118 118 LYS LYS HHH . n 
H 5 119 THR 119 119 119 THR THR HHH . n 
H 5 120 GLU 120 120 120 GLU GLU HHH . n 
H 5 121 TRP 121 121 121 TRP TRP HHH . n 
H 5 122 LEU 122 122 122 LEU LEU HHH . n 
H 5 123 ASP 123 123 123 ASP ASP HHH . n 
H 5 124 GLY 124 124 124 GLY GLY HHH . n 
H 5 125 LYS 125 125 125 LYS LYS HHH . n 
H 5 126 HIS 126 126 126 HIS HIS HHH . n 
H 5 127 VAL 127 127 127 VAL VAL HHH . n 
H 5 128 VAL 128 128 128 VAL VAL HHH . n 
H 5 129 PHE 129 129 129 PHE PHE HHH . n 
H 5 130 GLY 130 130 130 GLY GLY HHH . n 
H 5 131 LYS 131 131 131 LYS LYS HHH . n 
H 5 132 VAL 132 132 132 VAL VAL HHH . n 
H 5 133 LYS 133 133 133 LYS LYS HHH . n 
H 5 134 GLU 134 134 134 GLU GLU HHH . n 
H 5 135 GLY 135 135 135 GLY GLY HHH . n 
H 5 136 MET 136 136 136 MET MET HHH . n 
H 5 137 ASN 137 137 137 ASN ASN HHH . n 
H 5 138 ILE 138 138 138 ILE ILE HHH . n 
H 5 139 VAL 139 139 139 VAL VAL HHH . n 
H 5 140 GLU 140 140 140 GLU GLU HHH . n 
H 5 141 ALA 141 141 141 ALA ALA HHH . n 
H 5 142 MET 142 142 142 MET MET HHH . n 
H 5 143 GLU 143 143 143 GLU GLU HHH . n 
H 5 144 ARG 144 144 144 ARG ARG HHH . n 
H 5 145 PHE 145 145 145 PHE PHE HHH . n 
H 5 146 GLY 146 146 146 GLY GLY HHH . n 
H 5 147 SER 147 147 147 SER SER HHH . n 
H 5 148 ARG 148 148 148 ARG ARG HHH . n 
H 5 149 ASN 149 149 149 ASN ASN HHH . n 
H 5 150 GLY 150 150 150 GLY GLY HHH . n 
H 5 151 LYS 151 151 151 LYS LYS HHH . n 
H 5 152 THR 152 152 152 THR THR HHH . n 
H 5 153 SER 153 153 153 SER SER HHH . n 
H 5 154 LYS 154 154 154 LYS LYS HHH . n 
H 5 155 LYS 155 155 155 LYS LYS HHH . n 
H 5 156 ILE 156 156 156 ILE ILE HHH . n 
H 5 157 THR 157 157 157 THR THR HHH . n 
H 5 158 ILE 158 158 158 ILE ILE HHH . n 
H 5 159 ALA 159 159 159 ALA ALA HHH . n 
H 5 160 ASP 160 160 160 ASP ASP HHH . n 
H 5 161 CYS 161 161 161 CYS CYS HHH . n 
H 5 162 GLY 162 162 162 GLY GLY HHH . n 
H 5 163 GLN 163 163 163 GLN GLN HHH . n 
H 5 164 LEU 164 164 164 LEU LEU HHH . n 
H 5 165 GLU 165 165 165 GLU GLU HHH . n 
I 5 1   MET 1   1   1   MET MET III . n 
I 5 2   VAL 2   2   2   VAL VAL III . n 
I 5 3   ASN 3   3   3   ASN ASN III . n 
I 5 4   PRO 4   4   4   PRO PRO III . n 
I 5 5   THR 5   5   5   THR THR III . n 
I 5 6   VAL 6   6   6   VAL VAL III . n 
I 5 7   PHE 7   7   7   PHE PHE III . n 
I 5 8   PHE 8   8   8   PHE PHE III . n 
I 5 9   ASP 9   9   9   ASP ASP III . n 
I 5 10  ILE 10  10  10  ILE ILE III . n 
I 5 11  ALA 11  11  11  ALA ALA III . n 
I 5 12  VAL 12  12  12  VAL VAL III . n 
I 5 13  ASP 13  13  13  ASP ASP III . n 
I 5 14  GLY 14  14  14  GLY GLY III . n 
I 5 15  GLU 15  15  15  GLU GLU III . n 
I 5 16  PRO 16  16  16  PRO PRO III . n 
I 5 17  LEU 17  17  17  LEU LEU III . n 
I 5 18  GLY 18  18  18  GLY GLY III . n 
I 5 19  ARG 19  19  19  ARG ARG III . n 
I 5 20  VAL 20  20  20  VAL VAL III . n 
I 5 21  SER 21  21  21  SER SER III . n 
I 5 22  PHE 22  22  22  PHE PHE III . n 
I 5 23  GLU 23  23  23  GLU GLU III . n 
I 5 24  LEU 24  24  24  LEU LEU III . n 
I 5 25  PHE 25  25  25  PHE PHE III . n 
I 5 26  ALA 26  26  26  ALA ALA III . n 
I 5 27  ASP 27  27  27  ASP ASP III . n 
I 5 28  LYS 28  28  28  LYS LYS III . n 
I 5 29  VAL 29  29  29  VAL VAL III . n 
I 5 30  PRO 30  30  30  PRO PRO III . n 
I 5 31  LYS 31  31  31  LYS LYS III . n 
I 5 32  THR 32  32  32  THR THR III . n 
I 5 33  ALA 33  33  33  ALA ALA III . n 
I 5 34  GLU 34  34  34  GLU GLU III . n 
I 5 35  ASN 35  35  35  ASN ASN III . n 
I 5 36  PHE 36  36  36  PHE PHE III . n 
I 5 37  ARG 37  37  37  ARG ARG III . n 
I 5 38  ALA 38  38  38  ALA ALA III . n 
I 5 39  LEU 39  39  39  LEU LEU III . n 
I 5 40  SER 40  40  40  SER SER III . n 
I 5 41  THR 41  41  41  THR THR III . n 
I 5 42  GLY 42  42  42  GLY GLY III . n 
I 5 43  GLU 43  43  43  GLU GLU III . n 
I 5 44  LYS 44  44  44  LYS LYS III . n 
I 5 45  GLY 45  45  45  GLY GLY III . n 
I 5 46  PHE 46  46  46  PHE PHE III . n 
I 5 47  GLY 47  47  47  GLY GLY III . n 
I 5 48  TYR 48  48  48  TYR TYR III . n 
I 5 49  LYS 49  49  49  LYS LYS III . n 
I 5 50  GLY 50  50  50  GLY GLY III . n 
I 5 51  SER 51  51  51  SER SER III . n 
I 5 52  CYS 52  52  52  CYS CYS III . n 
I 5 53  PHE 53  53  53  PHE PHE III . n 
I 5 54  HIS 54  54  54  HIS HIS III . n 
I 5 55  ARG 55  55  55  ARG ARG III . n 
I 5 56  ILE 56  56  56  ILE ILE III . n 
I 5 57  ILE 57  57  57  ILE ILE III . n 
I 5 58  PRO 58  58  58  PRO PRO III . n 
I 5 59  GLY 59  59  59  GLY GLY III . n 
I 5 60  PHE 60  60  60  PHE PHE III . n 
I 5 61  MET 61  61  61  MET MET III . n 
I 5 62  CYS 62  62  62  CYS CYS III . n 
I 5 63  GLN 63  63  63  GLN GLN III . n 
I 5 64  GLY 64  64  64  GLY GLY III . n 
I 5 65  GLY 65  65  65  GLY GLY III . n 
I 5 66  ASP 66  66  66  ASP ASP III . n 
I 5 67  PHE 67  67  67  PHE PHE III . n 
I 5 68  THR 68  68  68  THR THR III . n 
I 5 69  ARG 69  69  69  ARG ARG III . n 
I 5 70  HIS 70  70  70  HIS HIS III . n 
I 5 71  ASN 71  71  71  ASN ASN III . n 
I 5 72  GLY 72  72  72  GLY GLY III . n 
I 5 73  THR 73  73  73  THR THR III . n 
I 5 74  GLY 74  74  74  GLY GLY III . n 
I 5 75  GLY 75  75  75  GLY GLY III . n 
I 5 76  LYS 76  76  76  LYS LYS III . n 
I 5 77  SER 77  77  77  SER SER III . n 
I 5 78  ILE 78  78  78  ILE ILE III . n 
I 5 79  TYR 79  79  79  TYR TYR III . n 
I 5 80  GLY 80  80  80  GLY GLY III . n 
I 5 81  GLU 81  81  81  GLU GLU III . n 
I 5 82  LYS 82  82  82  LYS LYS III . n 
I 5 83  PHE 83  83  83  PHE PHE III . n 
I 5 84  GLU 84  84  84  GLU GLU III . n 
I 5 85  ASP 85  85  85  ASP ASP III . n 
I 5 86  GLU 86  86  86  GLU GLU III . n 
I 5 87  ASN 87  87  87  ASN ASN III . n 
I 5 88  PHE 88  88  88  PHE PHE III . n 
I 5 89  ILE 89  89  89  ILE ILE III . n 
I 5 90  LEU 90  90  90  LEU LEU III . n 
I 5 91  LYS 91  91  91  LYS LYS III . n 
I 5 92  HIS 92  92  92  HIS HIS III . n 
I 5 93  THR 93  93  93  THR THR III . n 
I 5 94  GLY 94  94  94  GLY GLY III . n 
I 5 95  PRO 95  95  95  PRO PRO III . n 
I 5 96  GLY 96  96  96  GLY GLY III . n 
I 5 97  ILE 97  97  97  ILE ILE III . n 
I 5 98  LEU 98  98  98  LEU LEU III . n 
I 5 99  SER 99  99  99  SER SER III . n 
I 5 100 MET 100 100 100 MET MET III . n 
I 5 101 ALA 101 101 101 ALA ALA III . n 
I 5 102 ASN 102 102 102 ASN ASN III . n 
I 5 103 ALA 103 103 103 ALA ALA III . n 
I 5 104 GLY 104 104 104 GLY GLY III . n 
I 5 105 PRO 105 105 105 PRO PRO III . n 
I 5 106 ASN 106 106 106 ASN ASN III . n 
I 5 107 THR 107 107 107 THR THR III . n 
I 5 108 ASN 108 108 108 ASN ASN III . n 
I 5 109 GLY 109 109 109 GLY GLY III . n 
I 5 110 SER 110 110 110 SER SER III . n 
I 5 111 GLN 111 111 111 GLN GLN III . n 
I 5 112 PHE 112 112 112 PHE PHE III . n 
I 5 113 PHE 113 113 113 PHE PHE III . n 
I 5 114 ILE 114 114 114 ILE ILE III . n 
I 5 115 CYS 115 115 115 CYS CYS III . n 
I 5 116 THR 116 116 116 THR THR III . n 
I 5 117 ALA 117 117 117 ALA ALA III . n 
I 5 118 LYS 118 118 118 LYS LYS III . n 
I 5 119 THR 119 119 119 THR THR III . n 
I 5 120 GLU 120 120 120 GLU GLU III . n 
I 5 121 TRP 121 121 121 TRP TRP III . n 
I 5 122 LEU 122 122 122 LEU LEU III . n 
I 5 123 ASP 123 123 123 ASP ASP III . n 
I 5 124 GLY 124 124 124 GLY GLY III . n 
I 5 125 LYS 125 125 125 LYS LYS III . n 
I 5 126 HIS 126 126 126 HIS HIS III . n 
I 5 127 VAL 127 127 127 VAL VAL III . n 
I 5 128 VAL 128 128 128 VAL VAL III . n 
I 5 129 PHE 129 129 129 PHE PHE III . n 
I 5 130 GLY 130 130 130 GLY GLY III . n 
I 5 131 LYS 131 131 131 LYS LYS III . n 
I 5 132 VAL 132 132 132 VAL VAL III . n 
I 5 133 LYS 133 133 133 LYS LYS III . n 
I 5 134 GLU 134 134 134 GLU GLU III . n 
I 5 135 GLY 135 135 135 GLY GLY III . n 
I 5 136 MET 136 136 136 MET MET III . n 
I 5 137 ASN 137 137 137 ASN ASN III . n 
I 5 138 ILE 138 138 138 ILE ILE III . n 
I 5 139 VAL 139 139 139 VAL VAL III . n 
I 5 140 GLU 140 140 140 GLU GLU III . n 
I 5 141 ALA 141 141 141 ALA ALA III . n 
I 5 142 MET 142 142 142 MET MET III . n 
I 5 143 GLU 143 143 143 GLU GLU III . n 
I 5 144 ARG 144 144 144 ARG ARG III . n 
I 5 145 PHE 145 145 145 PHE PHE III . n 
I 5 146 GLY 146 146 146 GLY GLY III . n 
I 5 147 SER 147 147 147 SER SER III . n 
I 5 148 ARG 148 148 148 ARG ARG III . n 
I 5 149 ASN 149 149 149 ASN ASN III . n 
I 5 150 GLY 150 150 150 GLY GLY III . n 
I 5 151 LYS 151 151 151 LYS LYS III . n 
I 5 152 THR 152 152 152 THR THR III . n 
I 5 153 SER 153 153 153 SER SER III . n 
I 5 154 LYS 154 154 154 LYS LYS III . n 
I 5 155 LYS 155 155 155 LYS LYS III . n 
I 5 156 ILE 156 156 156 ILE ILE III . n 
I 5 157 THR 157 157 157 THR THR III . n 
I 5 158 ILE 158 158 158 ILE ILE III . n 
I 5 159 ALA 159 159 159 ALA ALA III . n 
I 5 160 ASP 160 160 160 ASP ASP III . n 
I 5 161 CYS 161 161 161 CYS CYS III . n 
I 5 162 GLY 162 162 162 GLY GLY III . n 
I 5 163 GLN 163 163 163 GLN GLN III . n 
I 5 164 LEU 164 164 164 LEU LEU III . n 
I 5 165 GLU 165 165 165 GLU GLU III . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   octadecameric 
_pdbx_struct_assembly.oligomeric_count     18 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I 
1 2 A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000  
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_665 -x+1,-y+1,z -1.0000000000 0.0000000000 0.0000000000 127.9500000000 0.0000000000 -1.0000000000 
0.0000000000 137.8500000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2022-06-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_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 60.4320 43.3660  40.9131 0.9030 ? 0.0111  ? 0.1545  ? 0.9536 ? 0.1276  ? 0.7936 ? 1.4098 ? 0.3393 
? 0.1451  ? 0.8341 ? -0.6304 ? 1.8346 ? -0.0074 ? -0.2698 ? -0.0101 ? -0.1570 ? -0.0435 ? -0.1071 ? 0.2185  ? -0.0337 ? 0.0508  ? 
2  'X-RAY DIFFRACTION' ? refined 32.4843 48.1463  64.1631 0.5118 ? -0.1969 ? 0.3364  ? 1.0475 ? 0.2043  ? 0.7177 ? 5.6617 ? 
-2.1672 ? -1.1706 ? 6.2437 ? -0.4013 ? 5.3937 ? 0.2974  ? -0.5725 ? -0.2704 ? 0.2240  ? -0.0331 ? 0.4526  ? -0.2357 ? 0.1626  ? 
-0.2642 ? 
3  'X-RAY DIFFRACTION' ? refined 40.1297 59.2030  40.7232 0.7431 ? -0.0833 ? 0.1050  ? 1.1193 ? -0.0193 ? 0.8033 ? 1.8410 ? 
-0.6134 ? 0.0649  ? 0.7290 ? 0.0388  ? 1.8666 ? -0.1220 ? -0.0986 ? -0.1561 ? 0.0014  ? -0.0701 ? 0.0222  ? 0.2198  ? -0.2256 ? 
0.1921  ? 
4  'X-RAY DIFFRACTION' ? refined 29.8497 85.8785  63.7466 0.5978 ? 0.2369  ? 0.0699  ? 1.2374 ? -0.1424 ? 0.6289 ? 2.6273 ? 
-0.2054 ? -1.4432 ? 6.1251 ? 1.5714  ? 1.4695 ? -0.1617 ? -0.0945 ? -0.2665 ? 0.0143  ? 0.1742  ? -0.0268 ? -0.1322 ? -0.4466 ? 
-0.0126 ? 
5  'X-RAY DIFFRACTION' ? refined 43.6382 84.8106  40.8524 0.6628 ? 0.0594  ? 0.0002  ? 1.0938 ? -0.1927 ? 0.7814 ? 0.7386 ? 
-0.1799 ? 0.2806  ? 2.2961 ? 0.3064  ? 3.6956 ? -0.1131 ? -0.1154 ? -0.0342 ? -0.1018 ? -0.1097 ? -0.0400 ? -0.2559 ? -0.2015 ? 
0.2228  ? 
6  'X-RAY DIFFRACTION' ? refined 62.2030 105.9532 65.3111 0.8365 ? 0.0304  ? -0.1556 ? 0.9034 ? -0.2883 ? 0.7206 ? 4.6239 ? 1.5236 
? 2.9599  ? 2.9046 ? 1.3521  ? 2.1049 ? -0.1291 ? -0.1379 ? -0.0106 ? 0.0602  ? -0.1504 ? 0.2852  ? -0.2236 ? 0.0160  ? 0.2796  ? 
7  'X-RAY DIFFRACTION' ? refined 83.1609 122.4489 68.8116 1.1008 ? -0.3990 ? -0.3393 ? 0.7812 ? -0.1821 ? 0.5447 ? 3.9545 ? 
-0.0358 ? -1.6229 ? 3.9301 ? -1.7157 ? 4.6786 ? 0.4710  ? -0.2270 ? 0.2698  ? -0.1320 ? -0.2764 ? 0.4698  ? -0.7578 ? 0.7475  ? 
-0.1945 ? 
8  'X-RAY DIFFRACTION' ? refined 21.8870 111.2147 62.6929 0.8612 ? 0.4630  ? 0.2873  ? 0.9588 ? -0.1665 ? 0.6070 ? 0.3638 ? 
-1.1898 ? 0.6918  ? 7.9137 ? -2.1785 ? 1.5775 ? -0.1173 ? -0.0421 ? -0.0116 ? 0.0230  ? 0.4348  ? 0.5758  ? -0.6496 ? -0.1686 ? 
-0.3175 ? 
9  'X-RAY DIFFRACTION' ? refined 6.8473  54.6685  64.7761 0.0837 ? 0.0267  ? 0.3711  ? 1.0360 ? -0.2812 ? 1.9492 ? 1.5557 ? 1.1853 
? 1.7414  ? 0.9418 ? 1.1018  ? 3.8958 ? 0.2134  ? -0.6812 ? 1.0244  ? 0.1959  ? -0.4498 ? 0.9800  ? 0.0020  ? -0.6666 ? 0.2364  ? 
10 'X-RAY DIFFRACTION' ? refined 70.8979 16.9916  16.6553 1.4895 ? 0.4144  ? 0.2596  ? 0.5170 ? 0.1382  ? 0.6603 ? 0.4065 ? 0.0682 
? -1.4085 ? 0.4532 ? -0.3223 ? 6.5672 ? -0.5694 ? -0.2050 ? 0.0631  ? 0.1221  ? 0.1730  ? 0.2610  ? 1.5978  ? 0.8416  ? 0.3964  ? 
11 'X-RAY DIFFRACTION' ? refined 23.3661 36.7977  16.4156 1.1923 ? -0.7679 ? 0.1468  ? 1.1464 ? -0.2017 ? 0.3455 ? 1.0471 ? 
-0.6267 ? 0.1381  ? 0.7541 ? 1.2489  ? 7.7742 ? -0.0611 ? -0.2382 ? 0.5632  ? 0.2240  ? -0.2180 ? -0.3258 ? 2.0937  ? -1.5630 ? 
0.2790  ? 
12 'X-RAY DIFFRACTION' ? refined 15.6758 89.0308  16.6355 0.4196 ? 0.4145  ? -0.1486 ? 1.9671 ? -0.2302 ? 0.3009 ? 0.5410 ? 1.0530 
? -0.8460 ? 2.4411 ? -0.5910 ? 7.1270 ? -0.0211 ? -0.0141 ? -0.1553 ? 0.1261  ? -0.1566 ? -0.5305 ? -0.2159 ? -1.9763 ? 0.1777  ? 
# 
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  ? ? AAA 1   ? ? ? AAA 145 ? ALL ? 
2  'X-RAY DIFFRACTION' 2  ? ? AAA 146 ? ? ? AAA 219 ? ALL ? 
3  'X-RAY DIFFRACTION' 3  ? ? BBB 1   ? ? ? BBB 145 ? ALL ? 
4  'X-RAY DIFFRACTION' 4  ? ? BBB 146 ? ? ? BBB 219 ? ALL ? 
5  'X-RAY DIFFRACTION' 5  ? ? CCC 1   ? ? ? CCC 145 ? ALL ? 
6  'X-RAY DIFFRACTION' 6  ? ? CCC 146 ? ? ? CCC 219 ? ALL ? 
7  'X-RAY DIFFRACTION' 7  ? ? FFF 1   ? ? ? FFF 112 ? ALL ? 
8  'X-RAY DIFFRACTION' 8  ? ? EEE 1   ? ? ? EEE 111 ? ALL ? 
9  'X-RAY DIFFRACTION' 9  ? ? DDD 2   ? ? ? DDD 112 ? ALL ? 
10 'X-RAY DIFFRACTION' 10 ? ? GGG 1   ? ? ? GGG 165 ? ALL ? 
11 'X-RAY DIFFRACTION' 11 ? ? HHH 3   ? ? ? HHH 165 ? ALL ? 
12 'X-RAY DIFFRACTION' 12 ? ? III 1   ? ? ? III 165 ? 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   ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O BBB LYS 182 ? ? OG1 BBB THR 186 ? ? 2.05 
2 1 O AAA GLY 208 ? ? NH2 DDD ARG 50  ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA DDD GLU 75  ? ? CB DDD GLU 75  ? ? CG DDD GLU 75  ? ? 127.21 113.40 13.81  2.20 N 
2 1 CB GGG ARG 144 ? ? CG GGG ARG 144 ? ? CD GGG ARG 144 ? ? 86.52  111.60 -25.08 2.60 N 
3 1 C  III LYS 82  ? ? N  III PHE 83  ? ? CA III PHE 83  ? ? 104.30 121.70 -17.40 2.50 Y 
# 
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 ALA BBB 31  ? ? 51.58   -123.07 
2  1 ALA BBB 177 ? ? 53.82   165.87  
3  1 GLU BBB 187 ? ? -54.62  -3.68   
4  1 THR BBB 188 ? ? -119.18 -74.21  
5  1 ASN CCC 5   ? ? 62.35   -178.50 
6  1 ALA CCC 31  ? ? 51.90   -123.19 
7  1 GLN CCC 176 ? ? 55.21   -66.31  
8  1 ALA CCC 177 ? ? 53.98   -120.20 
9  1 GLU CCC 187 ? ? -52.44  -5.37   
10 1 THR CCC 188 ? ? -121.41 -79.18  
11 1 ALA AAA 31  ? ? 51.96   -122.75 
12 1 GLN AAA 176 ? ? 53.77   17.80   
13 1 SER AAA 178 ? ? 66.23   -130.87 
14 1 GLU AAA 180 ? ? -129.11 -163.21 
15 1 ASN AAA 183 ? ? -133.08 -41.32  
16 1 GLU AAA 187 ? ? -57.38  -5.25   
17 1 THR AAA 188 ? ? -121.39 -77.19  
18 1 ASP EEE 97  ? ? 49.71   -73.46  
19 1 ASP DDD 97  ? ? -24.41  74.73   
20 1 LEU GGG 17  ? ? -121.41 -54.50  
21 1 PHE GGG 60  ? ? -128.54 -79.25  
22 1 GLU GGG 81  ? ? 59.63   -99.32  
23 1 PHE HHH 60  ? ? -129.06 -79.97  
24 1 TYR HHH 79  ? ? -104.62 77.12   
25 1 GLU HHH 81  ? ? -133.58 -42.19  
26 1 LEU HHH 164 ? ? -16.64  110.17  
27 1 PHE III 60  ? ? -128.56 -79.10  
28 1 THR III 73  ? ? -67.30  -88.17  
29 1 GLU III 81  ? ? 56.47   -140.34 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             PHE 
_pdbx_validate_main_chain_plane.auth_asym_id             III 
_pdbx_validate_main_chain_plane.auth_seq_id              46 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -14.41 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 HHH GLU 81  ? N  ? H GLU 81  N  
2 1 Y 0 HHH GLU 81  ? CA ? H GLU 81  CA 
3 1 Y 0 HHH GLU 81  ? C  ? H GLU 81  C  
4 1 Y 0 HHH GLU 81  ? O  ? H GLU 81  O  
5 1 Y 0 HHH LYS 155 ? CG ? H LYS 155 CG 
6 1 Y 0 HHH LYS 155 ? CD ? H LYS 155 CD 
7 1 Y 0 HHH LYS 155 ? CE ? H LYS 155 CE 
8 1 Y 0 HHH LYS 155 ? NZ ? H LYS 155 NZ 
# 
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 BBB GLY 220 ? A GLY 220 
2  1 Y 1 BBB VAL 221 ? A VAL 221 
3  1 Y 1 BBB GLY 222 ? A GLY 222 
4  1 Y 1 AAA GLY 220 ? C GLY 220 
5  1 Y 1 AAA VAL 221 ? C VAL 221 
6  1 Y 1 AAA GLY 222 ? C GLY 222 
7  1 Y 1 FFF UNK 99  ? D UNK 102 
8  1 Y 1 FFF UNK 100 ? D UNK 103 
9  1 Y 1 DDD UNK 99  ? F UNK 101 
10 1 Y 1 DDD UNK 100 ? F UNK 102 
11 1 Y 1 HHH MET 1   ? H MET 1   
12 1 Y 1 HHH VAL 2   ? H VAL 2   
13 1 Y 0 HHH GLY 80  ? H GLY 80  
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' P50GM082251 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                               'United States' 
'F32 GM131426 01A1' 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                ? 
# 
