data_9G0G
# 
_entry.id   9G0G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9G0G         pdb_00009g0g 10.2210/pdb9g0g/pdb 
WWPDB D_1292140026 ?            ?                   
# 
_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       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G0G 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8OGK 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rficner@gwdg.de 
_pdbx_contact_author.name_first         Ficner 
_pdbx_contact_author.name_last          Ralf 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0129-8112 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Neumann, P.' 1 0000-0003-0129-8112 
'Ficner, R.'  2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.F' 
_citation.journal_id_ASTM           ACSFEN 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2053-230X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            80 
_citation.language                  ? 
_citation.page_first                200 
_citation.page_last                 209 
_citation.title                     
'Crystallographic fragment screen of the c-di-AMP-synthesizing enzyme CdaA from Bacillus subtilis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2053230X24007039 
_citation.pdbx_database_id_PubMed   39177700 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Garbers, T.'     1 0000-0002-7130-3418 
primary 'Neumann, P.'     2 ?                   
primary 'Wollenhaupt, J.' 3 0000-0002-3418-5213 
primary 'Dickmanns, A.'   4 ?                   
primary 'Weiss, M.S.'     5 0000-0002-2362-7047 
primary 'Ficner, R.'      6 0000-0002-1739-6086 
# 
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 'Cyclic di-AMP synthase CdaA'                                              16810.199 2   2.7.7.85 ? ? 
'GP are part of the precission protease site' 
2 non-polymer syn '~{N}-[5-(2-azanyl-1,3-thiazol-4-yl)-4-methyl-1,3-thiazol-2-yl]ethanamide' 254.332   2   ?        ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                       78.133    15  ?        ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                    106.120   2   ?        ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                             35.453    6   ?        ? ? ? 
6 water       nat water                                                                      18.015    166 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'c-di-AMP synthase,Diadenylate cyclase,DAC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPTPVEEAQQKTIEAITKAINYMAKRRIGALLTIERDTGMGDYIETGIPLNAKVSSELLINIFIPNTPLHDGAVIMKNNE
IAAAACYLPLSESPFISKELGTRHRAAVGISEVTDSLTIIVSEETGGVSVAKNGDLHRELTEEALKEMLEAEFKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPTPVEEAQQKTIEAITKAINYMAKRRIGALLTIERDTGMGDYIETGIPLNAKVSSELLINIFIPNTPLHDGAVIMKNNE
IAAAACYLPLSESPFISKELGTRHRAAVGISEVTDSLTIIVSEETGGVSVAKNGDLHRELTEEALKEMLEAEFKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '~{N}-[5-(2-azanyl-1,3-thiazol-4-yl)-4-methyl-1,3-thiazol-2-yl]ethanamide' TJ9 
3 'DIMETHYL SULFOXIDE'                                                       DMS 
4 'DI(HYDROXYETHYL)ETHER'                                                    PEG 
5 'CHLORIDE ION'                                                             CL  
6 water                                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   THR n 
1 4   PRO n 
1 5   VAL n 
1 6   GLU n 
1 7   GLU n 
1 8   ALA n 
1 9   GLN n 
1 10  GLN n 
1 11  LYS n 
1 12  THR n 
1 13  ILE n 
1 14  GLU n 
1 15  ALA n 
1 16  ILE n 
1 17  THR n 
1 18  LYS n 
1 19  ALA n 
1 20  ILE n 
1 21  ASN n 
1 22  TYR n 
1 23  MET n 
1 24  ALA n 
1 25  LYS n 
1 26  ARG n 
1 27  ARG n 
1 28  ILE n 
1 29  GLY n 
1 30  ALA n 
1 31  LEU n 
1 32  LEU n 
1 33  THR n 
1 34  ILE n 
1 35  GLU n 
1 36  ARG n 
1 37  ASP n 
1 38  THR n 
1 39  GLY n 
1 40  MET n 
1 41  GLY n 
1 42  ASP n 
1 43  TYR n 
1 44  ILE n 
1 45  GLU n 
1 46  THR n 
1 47  GLY n 
1 48  ILE n 
1 49  PRO n 
1 50  LEU n 
1 51  ASN n 
1 52  ALA n 
1 53  LYS n 
1 54  VAL n 
1 55  SER n 
1 56  SER n 
1 57  GLU n 
1 58  LEU n 
1 59  LEU n 
1 60  ILE n 
1 61  ASN n 
1 62  ILE n 
1 63  PHE n 
1 64  ILE n 
1 65  PRO n 
1 66  ASN n 
1 67  THR n 
1 68  PRO n 
1 69  LEU n 
1 70  HIS n 
1 71  ASP n 
1 72  GLY n 
1 73  ALA n 
1 74  VAL n 
1 75  ILE n 
1 76  MET n 
1 77  LYS n 
1 78  ASN n 
1 79  ASN n 
1 80  GLU n 
1 81  ILE n 
1 82  ALA n 
1 83  ALA n 
1 84  ALA n 
1 85  ALA n 
1 86  CYS n 
1 87  TYR n 
1 88  LEU n 
1 89  PRO n 
1 90  LEU n 
1 91  SER n 
1 92  GLU n 
1 93  SER n 
1 94  PRO n 
1 95  PHE n 
1 96  ILE n 
1 97  SER n 
1 98  LYS n 
1 99  GLU n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ARG n 
1 104 HIS n 
1 105 ARG n 
1 106 ALA n 
1 107 ALA n 
1 108 VAL n 
1 109 GLY n 
1 110 ILE n 
1 111 SER n 
1 112 GLU n 
1 113 VAL n 
1 114 THR n 
1 115 ASP n 
1 116 SER n 
1 117 LEU n 
1 118 THR n 
1 119 ILE n 
1 120 ILE n 
1 121 VAL n 
1 122 SER n 
1 123 GLU n 
1 124 GLU n 
1 125 THR n 
1 126 GLY n 
1 127 GLY n 
1 128 VAL n 
1 129 SER n 
1 130 VAL n 
1 131 ALA n 
1 132 LYS n 
1 133 ASN n 
1 134 GLY n 
1 135 ASP n 
1 136 LEU n 
1 137 HIS n 
1 138 ARG n 
1 139 GLU n 
1 140 LEU n 
1 141 THR n 
1 142 GLU n 
1 143 GLU n 
1 144 ALA n 
1 145 LEU n 
1 146 LYS n 
1 147 GLU n 
1 148 MET n 
1 149 LEU n 
1 150 GLU n 
1 151 ALA n 
1 152 GLU n 
1 153 PHE n 
1 154 LYS n 
1 155 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   155 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cdaA, ybbP, BSU01750' 
_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      'Bacillus subtilis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1423 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
CL  non-polymer         . 'CHLORIDE ION'                                                             ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                   ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                       ? 'C2 H6 O S'      78.133  
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 
HOH non-polymer         . WATER                                                                      ? 'H2 O'           18.015  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                    ? 'C4 H10 O3'      106.120 
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 
TJ9 non-polymer         . '~{N}-[5-(2-azanyl-1,3-thiazol-4-yl)-4-methyl-1,3-thiazol-2-yl]ethanamide' ? 'C9 H10 N4 O S2' 254.332 
TYR 'L-peptide linking' y TYROSINE                                                                   ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   101 ?   ?   ?   A . n 
A 1 2   PRO 2   102 ?   ?   ?   A . n 
A 1 3   THR 3   103 103 THR THR A . n 
A 1 4   PRO 4   104 104 PRO PRO A . n 
A 1 5   VAL 5   105 105 VAL VAL A . n 
A 1 6   GLU 6   106 106 GLU GLU A . n 
A 1 7   GLU 7   107 107 GLU GLU A . n 
A 1 8   ALA 8   108 108 ALA ALA A . n 
A 1 9   GLN 9   109 109 GLN GLN A . n 
A 1 10  GLN 10  110 110 GLN GLN A . n 
A 1 11  LYS 11  111 111 LYS LYS A . n 
A 1 12  THR 12  112 112 THR THR A . n 
A 1 13  ILE 13  113 113 ILE ILE A . n 
A 1 14  GLU 14  114 114 GLU GLU A . n 
A 1 15  ALA 15  115 115 ALA ALA A . n 
A 1 16  ILE 16  116 116 ILE ILE A . n 
A 1 17  THR 17  117 117 THR THR A . n 
A 1 18  LYS 18  118 118 LYS LYS A . n 
A 1 19  ALA 19  119 119 ALA ALA A . n 
A 1 20  ILE 20  120 120 ILE ILE A . n 
A 1 21  ASN 21  121 121 ASN ASN A . n 
A 1 22  TYR 22  122 122 TYR TYR A . n 
A 1 23  MET 23  123 123 MET MET A . n 
A 1 24  ALA 24  124 124 ALA ALA A . n 
A 1 25  LYS 25  125 125 LYS LYS A . n 
A 1 26  ARG 26  126 126 ARG ARG A . n 
A 1 27  ARG 27  127 127 ARG ARG A . n 
A 1 28  ILE 28  128 128 ILE ILE A . n 
A 1 29  GLY 29  129 129 GLY GLY A . n 
A 1 30  ALA 30  130 130 ALA ALA A . n 
A 1 31  LEU 31  131 131 LEU LEU A . n 
A 1 32  LEU 32  132 132 LEU LEU A . n 
A 1 33  THR 33  133 133 THR THR A . n 
A 1 34  ILE 34  134 134 ILE ILE A . n 
A 1 35  GLU 35  135 135 GLU GLU A . n 
A 1 36  ARG 36  136 136 ARG ARG A . n 
A 1 37  ASP 37  137 137 ASP ASP A . n 
A 1 38  THR 38  138 138 THR THR A . n 
A 1 39  GLY 39  139 139 GLY GLY A . n 
A 1 40  MET 40  140 140 MET MET A . n 
A 1 41  GLY 41  141 141 GLY GLY A . n 
A 1 42  ASP 42  142 142 ASP ASP A . n 
A 1 43  TYR 43  143 143 TYR TYR A . n 
A 1 44  ILE 44  144 144 ILE ILE A . n 
A 1 45  GLU 45  145 145 GLU GLU A . n 
A 1 46  THR 46  146 146 THR THR A . n 
A 1 47  GLY 47  147 147 GLY GLY A . n 
A 1 48  ILE 48  148 148 ILE ILE A . n 
A 1 49  PRO 49  149 149 PRO PRO A . n 
A 1 50  LEU 50  150 150 LEU LEU A . n 
A 1 51  ASN 51  151 151 ASN ASN A . n 
A 1 52  ALA 52  152 152 ALA ALA A . n 
A 1 53  LYS 53  153 153 LYS LYS A . n 
A 1 54  VAL 54  154 154 VAL VAL A . n 
A 1 55  SER 55  155 155 SER SER A . n 
A 1 56  SER 56  156 156 SER SER A . n 
A 1 57  GLU 57  157 157 GLU GLU A . n 
A 1 58  LEU 58  158 158 LEU LEU A . n 
A 1 59  LEU 59  159 159 LEU LEU A . n 
A 1 60  ILE 60  160 160 ILE ILE A . n 
A 1 61  ASN 61  161 161 ASN ASN A . n 
A 1 62  ILE 62  162 162 ILE ILE A . n 
A 1 63  PHE 63  163 163 PHE PHE A . n 
A 1 64  ILE 64  164 164 ILE ILE A . n 
A 1 65  PRO 65  165 165 PRO PRO A . n 
A 1 66  ASN 66  166 166 ASN ASN A . n 
A 1 67  THR 67  167 167 THR THR A . n 
A 1 68  PRO 68  168 168 PRO PRO A . n 
A 1 69  LEU 69  169 169 LEU LEU A . n 
A 1 70  HIS 70  170 170 HIS HIS A . n 
A 1 71  ASP 71  171 171 ASP ASP A . n 
A 1 72  GLY 72  172 172 GLY GLY A . n 
A 1 73  ALA 73  173 173 ALA ALA A . n 
A 1 74  VAL 74  174 174 VAL VAL A . n 
A 1 75  ILE 75  175 175 ILE ILE A . n 
A 1 76  MET 76  176 176 MET MET A . n 
A 1 77  LYS 77  177 177 LYS LYS A . n 
A 1 78  ASN 78  178 178 ASN ASN A . n 
A 1 79  ASN 79  179 179 ASN ASN A . n 
A 1 80  GLU 80  180 180 GLU GLU A . n 
A 1 81  ILE 81  181 181 ILE ILE A . n 
A 1 82  ALA 82  182 182 ALA ALA A . n 
A 1 83  ALA 83  183 183 ALA ALA A . n 
A 1 84  ALA 84  184 184 ALA ALA A . n 
A 1 85  ALA 85  185 185 ALA ALA A . n 
A 1 86  CYS 86  186 186 CYS CYS A . n 
A 1 87  TYR 87  187 187 TYR TYR A . n 
A 1 88  LEU 88  188 188 LEU LEU A . n 
A 1 89  PRO 89  189 189 PRO PRO A . n 
A 1 90  LEU 90  190 190 LEU LEU A . n 
A 1 91  SER 91  191 191 SER SER A . n 
A 1 92  GLU 92  192 192 GLU GLU A . n 
A 1 93  SER 93  193 193 SER SER A . n 
A 1 94  PRO 94  194 194 PRO PRO A . n 
A 1 95  PHE 95  195 195 PHE PHE A . n 
A 1 96  ILE 96  196 196 ILE ILE A . n 
A 1 97  SER 97  197 197 SER SER A . n 
A 1 98  LYS 98  198 198 LYS LYS A . n 
A 1 99  GLU 99  199 199 GLU GLU A . n 
A 1 100 LEU 100 200 200 LEU LEU A . n 
A 1 101 GLY 101 201 201 GLY GLY A . n 
A 1 102 THR 102 202 202 THR THR A . n 
A 1 103 ARG 103 203 203 ARG ARG A . n 
A 1 104 HIS 104 204 204 HIS HIS A . n 
A 1 105 ARG 105 205 205 ARG ARG A . n 
A 1 106 ALA 106 206 206 ALA ALA A . n 
A 1 107 ALA 107 207 207 ALA ALA A . n 
A 1 108 VAL 108 208 208 VAL VAL A . n 
A 1 109 GLY 109 209 209 GLY GLY A . n 
A 1 110 ILE 110 210 210 ILE ILE A . n 
A 1 111 SER 111 211 211 SER SER A . n 
A 1 112 GLU 112 212 212 GLU GLU A . n 
A 1 113 VAL 113 213 213 VAL VAL A . n 
A 1 114 THR 114 214 214 THR THR A . n 
A 1 115 ASP 115 215 215 ASP ASP A . n 
A 1 116 SER 116 216 216 SER SER A . n 
A 1 117 LEU 117 217 217 LEU LEU A . n 
A 1 118 THR 118 218 218 THR THR A . n 
A 1 119 ILE 119 219 219 ILE ILE A . n 
A 1 120 ILE 120 220 220 ILE ILE A . n 
A 1 121 VAL 121 221 221 VAL VAL A . n 
A 1 122 SER 122 222 222 SER SER A . n 
A 1 123 GLU 123 223 223 GLU GLU A . n 
A 1 124 GLU 124 224 224 GLU GLU A . n 
A 1 125 THR 125 225 225 THR THR A . n 
A 1 126 GLY 126 226 226 GLY GLY A . n 
A 1 127 GLY 127 227 227 GLY GLY A . n 
A 1 128 VAL 128 228 228 VAL VAL A . n 
A 1 129 SER 129 229 229 SER SER A . n 
A 1 130 VAL 130 230 230 VAL VAL A . n 
A 1 131 ALA 131 231 231 ALA ALA A . n 
A 1 132 LYS 132 232 232 LYS LYS A . n 
A 1 133 ASN 133 233 233 ASN ASN A . n 
A 1 134 GLY 134 234 234 GLY GLY A . n 
A 1 135 ASP 135 235 235 ASP ASP A . n 
A 1 136 LEU 136 236 236 LEU LEU A . n 
A 1 137 HIS 137 237 237 HIS HIS A . n 
A 1 138 ARG 138 238 238 ARG ARG A . n 
A 1 139 GLU 139 239 239 GLU GLU A . n 
A 1 140 LEU 140 240 240 LEU LEU A . n 
A 1 141 THR 141 241 241 THR THR A . n 
A 1 142 GLU 142 242 242 GLU GLU A . n 
A 1 143 GLU 143 243 243 GLU GLU A . n 
A 1 144 ALA 144 244 244 ALA ALA A . n 
A 1 145 LEU 145 245 245 LEU LEU A . n 
A 1 146 LYS 146 246 246 LYS LYS A . n 
A 1 147 GLU 147 247 247 GLU GLU A . n 
A 1 148 MET 148 248 248 MET MET A . n 
A 1 149 LEU 149 249 249 LEU LEU A . n 
A 1 150 GLU 150 250 250 GLU GLU A . n 
A 1 151 ALA 151 251 251 ALA ALA A . n 
A 1 152 GLU 152 252 252 GLU GLU A . n 
A 1 153 PHE 153 253 253 PHE PHE A . n 
A 1 154 LYS 154 254 254 LYS LYS A . n 
A 1 155 LYS 155 255 ?   ?   ?   A . n 
B 1 1   GLY 1   101 ?   ?   ?   B . n 
B 1 2   PRO 2   102 102 PRO PRO B . n 
B 1 3   THR 3   103 103 THR THR B . n 
B 1 4   PRO 4   104 104 PRO PRO B . n 
B 1 5   VAL 5   105 105 VAL VAL B . n 
B 1 6   GLU 6   106 106 GLU GLU B . n 
B 1 7   GLU 7   107 107 GLU GLU B . n 
B 1 8   ALA 8   108 108 ALA ALA B . n 
B 1 9   GLN 9   109 109 GLN GLN B . n 
B 1 10  GLN 10  110 110 GLN GLN B . n 
B 1 11  LYS 11  111 111 LYS LYS B . n 
B 1 12  THR 12  112 112 THR THR B . n 
B 1 13  ILE 13  113 113 ILE ILE B . n 
B 1 14  GLU 14  114 114 GLU GLU B . n 
B 1 15  ALA 15  115 115 ALA ALA B . n 
B 1 16  ILE 16  116 116 ILE ILE B . n 
B 1 17  THR 17  117 117 THR THR B . n 
B 1 18  LYS 18  118 118 LYS LYS B . n 
B 1 19  ALA 19  119 119 ALA ALA B . n 
B 1 20  ILE 20  120 120 ILE ILE B . n 
B 1 21  ASN 21  121 121 ASN ASN B . n 
B 1 22  TYR 22  122 122 TYR TYR B . n 
B 1 23  MET 23  123 123 MET MET B . n 
B 1 24  ALA 24  124 124 ALA ALA B . n 
B 1 25  LYS 25  125 125 LYS LYS B . n 
B 1 26  ARG 26  126 126 ARG ARG B . n 
B 1 27  ARG 27  127 127 ARG ARG B . n 
B 1 28  ILE 28  128 128 ILE ILE B . n 
B 1 29  GLY 29  129 129 GLY GLY B . n 
B 1 30  ALA 30  130 130 ALA ALA B . n 
B 1 31  LEU 31  131 131 LEU LEU B . n 
B 1 32  LEU 32  132 132 LEU LEU B . n 
B 1 33  THR 33  133 133 THR THR B . n 
B 1 34  ILE 34  134 134 ILE ILE B . n 
B 1 35  GLU 35  135 135 GLU GLU B . n 
B 1 36  ARG 36  136 136 ARG ARG B . n 
B 1 37  ASP 37  137 137 ASP ASP B . n 
B 1 38  THR 38  138 138 THR THR B . n 
B 1 39  GLY 39  139 139 GLY GLY B . n 
B 1 40  MET 40  140 140 MET MET B . n 
B 1 41  GLY 41  141 141 GLY GLY B . n 
B 1 42  ASP 42  142 142 ASP ASP B . n 
B 1 43  TYR 43  143 143 TYR TYR B . n 
B 1 44  ILE 44  144 144 ILE ILE B . n 
B 1 45  GLU 45  145 145 GLU GLU B . n 
B 1 46  THR 46  146 146 THR THR B . n 
B 1 47  GLY 47  147 147 GLY GLY B . n 
B 1 48  ILE 48  148 148 ILE ILE B . n 
B 1 49  PRO 49  149 149 PRO PRO B . n 
B 1 50  LEU 50  150 150 LEU LEU B . n 
B 1 51  ASN 51  151 151 ASN ASN B . n 
B 1 52  ALA 52  152 152 ALA ALA B . n 
B 1 53  LYS 53  153 153 LYS LYS B . n 
B 1 54  VAL 54  154 154 VAL VAL B . n 
B 1 55  SER 55  155 155 SER SER B . n 
B 1 56  SER 56  156 156 SER SER B . n 
B 1 57  GLU 57  157 157 GLU GLU B . n 
B 1 58  LEU 58  158 158 LEU LEU B . n 
B 1 59  LEU 59  159 159 LEU LEU B . n 
B 1 60  ILE 60  160 160 ILE ILE B . n 
B 1 61  ASN 61  161 161 ASN ASN B . n 
B 1 62  ILE 62  162 162 ILE ILE B . n 
B 1 63  PHE 63  163 163 PHE PHE B . n 
B 1 64  ILE 64  164 164 ILE ILE B . n 
B 1 65  PRO 65  165 165 PRO PRO B . n 
B 1 66  ASN 66  166 166 ASN ASN B . n 
B 1 67  THR 67  167 167 THR THR B . n 
B 1 68  PRO 68  168 168 PRO PRO B . n 
B 1 69  LEU 69  169 169 LEU LEU B . n 
B 1 70  HIS 70  170 170 HIS HIS B . n 
B 1 71  ASP 71  171 171 ASP ASP B . n 
B 1 72  GLY 72  172 172 GLY GLY B . n 
B 1 73  ALA 73  173 173 ALA ALA B . n 
B 1 74  VAL 74  174 174 VAL VAL B . n 
B 1 75  ILE 75  175 175 ILE ILE B . n 
B 1 76  MET 76  176 176 MET MET B . n 
B 1 77  LYS 77  177 177 LYS LYS B . n 
B 1 78  ASN 78  178 178 ASN ASN B . n 
B 1 79  ASN 79  179 179 ASN ASN B . n 
B 1 80  GLU 80  180 180 GLU GLU B . n 
B 1 81  ILE 81  181 181 ILE ILE B . n 
B 1 82  ALA 82  182 182 ALA ALA B . n 
B 1 83  ALA 83  183 183 ALA ALA B . n 
B 1 84  ALA 84  184 184 ALA ALA B . n 
B 1 85  ALA 85  185 185 ALA ALA B . n 
B 1 86  CYS 86  186 186 CYS CYS B . n 
B 1 87  TYR 87  187 187 TYR TYR B . n 
B 1 88  LEU 88  188 188 LEU LEU B . n 
B 1 89  PRO 89  189 189 PRO PRO B . n 
B 1 90  LEU 90  190 190 LEU LEU B . n 
B 1 91  SER 91  191 191 SER SER B . n 
B 1 92  GLU 92  192 192 GLU GLU B . n 
B 1 93  SER 93  193 193 SER SER B . n 
B 1 94  PRO 94  194 194 PRO PRO B . n 
B 1 95  PHE 95  195 195 PHE PHE B . n 
B 1 96  ILE 96  196 196 ILE ILE B . n 
B 1 97  SER 97  197 197 SER SER B . n 
B 1 98  LYS 98  198 198 LYS LYS B . n 
B 1 99  GLU 99  199 199 GLU GLU B . n 
B 1 100 LEU 100 200 200 LEU LEU B . n 
B 1 101 GLY 101 201 201 GLY GLY B . n 
B 1 102 THR 102 202 202 THR THR B . n 
B 1 103 ARG 103 203 203 ARG ARG B . n 
B 1 104 HIS 104 204 204 HIS HIS B . n 
B 1 105 ARG 105 205 205 ARG ARG B . n 
B 1 106 ALA 106 206 206 ALA ALA B . n 
B 1 107 ALA 107 207 207 ALA ALA B . n 
B 1 108 VAL 108 208 208 VAL VAL B . n 
B 1 109 GLY 109 209 209 GLY GLY B . n 
B 1 110 ILE 110 210 210 ILE ILE B . n 
B 1 111 SER 111 211 211 SER SER B . n 
B 1 112 GLU 112 212 212 GLU GLU B . n 
B 1 113 VAL 113 213 213 VAL VAL B . n 
B 1 114 THR 114 214 214 THR THR B . n 
B 1 115 ASP 115 215 215 ASP ASP B . n 
B 1 116 SER 116 216 216 SER SER B . n 
B 1 117 LEU 117 217 217 LEU LEU B . n 
B 1 118 THR 118 218 218 THR THR B . n 
B 1 119 ILE 119 219 219 ILE ILE B . n 
B 1 120 ILE 120 220 220 ILE ILE B . n 
B 1 121 VAL 121 221 221 VAL VAL B . n 
B 1 122 SER 122 222 222 SER SER B . n 
B 1 123 GLU 123 223 223 GLU GLU B . n 
B 1 124 GLU 124 224 224 GLU GLU B . n 
B 1 125 THR 125 225 225 THR THR B . n 
B 1 126 GLY 126 226 226 GLY GLY B . n 
B 1 127 GLY 127 227 227 GLY GLY B . n 
B 1 128 VAL 128 228 228 VAL VAL B . n 
B 1 129 SER 129 229 229 SER SER B . n 
B 1 130 VAL 130 230 230 VAL VAL B . n 
B 1 131 ALA 131 231 231 ALA ALA B . n 
B 1 132 LYS 132 232 232 LYS LYS B . n 
B 1 133 ASN 133 233 233 ASN ASN B . n 
B 1 134 GLY 134 234 234 GLY GLY B . n 
B 1 135 ASP 135 235 235 ASP ASP B . n 
B 1 136 LEU 136 236 236 LEU LEU B . n 
B 1 137 HIS 137 237 237 HIS HIS B . n 
B 1 138 ARG 138 238 238 ARG ARG B . n 
B 1 139 GLU 139 239 239 GLU GLU B . n 
B 1 140 LEU 140 240 240 LEU LEU B . n 
B 1 141 THR 141 241 241 THR THR B . n 
B 1 142 GLU 142 242 242 GLU GLU B . n 
B 1 143 GLU 143 243 243 GLU GLU B . n 
B 1 144 ALA 144 244 244 ALA ALA B . n 
B 1 145 LEU 145 245 245 LEU LEU B . n 
B 1 146 LYS 146 246 246 LYS LYS B . n 
B 1 147 GLU 147 247 247 GLU GLU B . n 
B 1 148 MET 148 248 248 MET MET B . n 
B 1 149 LEU 149 249 249 LEU LEU B . n 
B 1 150 GLU 150 250 250 GLU GLU B . n 
B 1 151 ALA 151 251 251 ALA ALA B . n 
B 1 152 GLU 152 252 252 GLU GLU B . n 
B 1 153 PHE 153 253 253 PHE PHE B . n 
B 1 154 LYS 154 254 254 LYS LYS B . n 
B 1 155 LYS 155 255 255 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TJ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TJ9 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2 TJ9 1  301 301 TJ9 TJ9 A . 
D  3 DMS 1  302 502 DMS DMS A . 
E  3 DMS 1  303 503 DMS DMS A . 
F  3 DMS 1  304 504 DMS DMS A . 
G  3 DMS 1  305 505 DMS DMS A . 
H  3 DMS 1  306 506 DMS DMS A . 
I  3 DMS 1  307 507 DMS DMS A . 
J  3 DMS 1  308 508 DMS DMS A . 
K  3 DMS 1  309 509 DMS DMS A . 
L  4 PEG 1  310 510 PEG PEG A . 
M  3 DMS 1  311 511 DMS DMS A . 
N  5 CL  1  312 2   CL  CL  A . 
O  5 CL  1  313 3   CL  CL  A . 
P  5 CL  1  314 6   CL  CL  A . 
Q  2 TJ9 1  301 301 TJ9 TJ9 B . 
R  3 DMS 1  302 502 DMS DMS B . 
S  3 DMS 1  303 503 DMS DMS B . 
T  3 DMS 1  304 504 DMS DMS B . 
U  3 DMS 1  305 505 DMS DMS B . 
V  3 DMS 1  306 506 DMS DMS B . 
W  3 DMS 1  307 507 DMS DMS B . 
X  4 PEG 1  308 508 PEG PEG B . 
Y  5 CL  1  309 1   CL  CL  B . 
Z  5 CL  1  310 4   CL  CL  B . 
AA 5 CL  1  311 5   CL  CL  B . 
BA 6 HOH 1  401 157 HOH HOH A . 
BA 6 HOH 2  402 73  HOH HOH A . 
BA 6 HOH 3  403 118 HOH HOH A . 
BA 6 HOH 4  404 69  HOH HOH A . 
BA 6 HOH 5  405 189 HOH HOH A . 
BA 6 HOH 6  406 31  HOH HOH A . 
BA 6 HOH 7  407 113 HOH HOH A . 
BA 6 HOH 8  408 169 HOH HOH A . 
BA 6 HOH 9  409 49  HOH HOH A . 
BA 6 HOH 10 410 183 HOH HOH A . 
BA 6 HOH 11 411 67  HOH HOH A . 
BA 6 HOH 12 412 52  HOH HOH A . 
BA 6 HOH 13 413 144 HOH HOH A . 
BA 6 HOH 14 414 18  HOH HOH A . 
BA 6 HOH 15 415 186 HOH HOH A . 
BA 6 HOH 16 416 4   HOH HOH A . 
BA 6 HOH 17 417 8   HOH HOH A . 
BA 6 HOH 18 418 88  HOH HOH A . 
BA 6 HOH 19 419 32  HOH HOH A . 
BA 6 HOH 20 420 78  HOH HOH A . 
BA 6 HOH 21 421 66  HOH HOH A . 
BA 6 HOH 22 422 9   HOH HOH A . 
BA 6 HOH 23 423 156 HOH HOH A . 
BA 6 HOH 24 424 127 HOH HOH A . 
BA 6 HOH 25 425 148 HOH HOH A . 
BA 6 HOH 26 426 7   HOH HOH A . 
BA 6 HOH 27 427 89  HOH HOH A . 
BA 6 HOH 28 428 43  HOH HOH A . 
BA 6 HOH 29 429 134 HOH HOH A . 
BA 6 HOH 30 430 42  HOH HOH A . 
BA 6 HOH 31 431 82  HOH HOH A . 
BA 6 HOH 32 432 13  HOH HOH A . 
BA 6 HOH 33 433 86  HOH HOH A . 
BA 6 HOH 34 434 21  HOH HOH A . 
BA 6 HOH 35 435 17  HOH HOH A . 
BA 6 HOH 36 436 5   HOH HOH A . 
BA 6 HOH 37 437 26  HOH HOH A . 
BA 6 HOH 38 438 81  HOH HOH A . 
BA 6 HOH 39 439 64  HOH HOH A . 
BA 6 HOH 40 440 130 HOH HOH A . 
BA 6 HOH 41 441 143 HOH HOH A . 
BA 6 HOH 42 442 61  HOH HOH A . 
BA 6 HOH 43 443 99  HOH HOH A . 
BA 6 HOH 44 444 172 HOH HOH A . 
BA 6 HOH 45 445 114 HOH HOH A . 
BA 6 HOH 46 446 76  HOH HOH A . 
BA 6 HOH 47 447 181 HOH HOH A . 
BA 6 HOH 48 448 93  HOH HOH A . 
BA 6 HOH 49 449 84  HOH HOH A . 
BA 6 HOH 50 450 154 HOH HOH A . 
BA 6 HOH 51 451 28  HOH HOH A . 
BA 6 HOH 52 452 74  HOH HOH A . 
BA 6 HOH 53 453 80  HOH HOH A . 
BA 6 HOH 54 454 34  HOH HOH A . 
BA 6 HOH 55 455 40  HOH HOH A . 
BA 6 HOH 56 456 160 HOH HOH A . 
BA 6 HOH 57 457 133 HOH HOH A . 
BA 6 HOH 58 458 68  HOH HOH A . 
BA 6 HOH 59 459 35  HOH HOH A . 
BA 6 HOH 60 460 117 HOH HOH A . 
BA 6 HOH 61 461 171 HOH HOH A . 
BA 6 HOH 62 462 60  HOH HOH A . 
BA 6 HOH 63 463 125 HOH HOH A . 
BA 6 HOH 64 464 20  HOH HOH A . 
BA 6 HOH 65 465 101 HOH HOH A . 
BA 6 HOH 66 466 62  HOH HOH A . 
BA 6 HOH 67 467 146 HOH HOH A . 
BA 6 HOH 68 468 2   HOH HOH A . 
BA 6 HOH 69 469 174 HOH HOH A . 
BA 6 HOH 70 470 98  HOH HOH A . 
BA 6 HOH 71 471 79  HOH HOH A . 
BA 6 HOH 72 472 95  HOH HOH A . 
BA 6 HOH 73 473 179 HOH HOH A . 
BA 6 HOH 74 474 58  HOH HOH A . 
BA 6 HOH 75 475 190 HOH HOH A . 
BA 6 HOH 76 476 92  HOH HOH A . 
BA 6 HOH 77 477 180 HOH HOH A . 
BA 6 HOH 78 478 147 HOH HOH A . 
BA 6 HOH 79 479 166 HOH HOH A . 
BA 6 HOH 80 480 153 HOH HOH A . 
BA 6 HOH 81 481 152 HOH HOH A . 
BA 6 HOH 82 482 136 HOH HOH A . 
BA 6 HOH 83 483 100 HOH HOH A . 
BA 6 HOH 84 484 175 HOH HOH A . 
BA 6 HOH 85 485 139 HOH HOH A . 
CA 6 HOH 1  401 106 HOH HOH B . 
CA 6 HOH 2  402 150 HOH HOH B . 
CA 6 HOH 3  403 142 HOH HOH B . 
CA 6 HOH 4  404 129 HOH HOH B . 
CA 6 HOH 5  405 25  HOH HOH B . 
CA 6 HOH 6  406 6   HOH HOH B . 
CA 6 HOH 7  407 124 HOH HOH B . 
CA 6 HOH 8  408 11  HOH HOH B . 
CA 6 HOH 9  409 122 HOH HOH B . 
CA 6 HOH 10 410 85  HOH HOH B . 
CA 6 HOH 11 411 15  HOH HOH B . 
CA 6 HOH 12 412 141 HOH HOH B . 
CA 6 HOH 13 413 14  HOH HOH B . 
CA 6 HOH 14 414 47  HOH HOH B . 
CA 6 HOH 15 415 53  HOH HOH B . 
CA 6 HOH 16 416 29  HOH HOH B . 
CA 6 HOH 17 417 120 HOH HOH B . 
CA 6 HOH 18 418 105 HOH HOH B . 
CA 6 HOH 19 419 104 HOH HOH B . 
CA 6 HOH 20 420 24  HOH HOH B . 
CA 6 HOH 21 421 51  HOH HOH B . 
CA 6 HOH 22 422 33  HOH HOH B . 
CA 6 HOH 23 423 83  HOH HOH B . 
CA 6 HOH 24 424 30  HOH HOH B . 
CA 6 HOH 25 425 46  HOH HOH B . 
CA 6 HOH 26 426 10  HOH HOH B . 
CA 6 HOH 27 427 54  HOH HOH B . 
CA 6 HOH 28 428 55  HOH HOH B . 
CA 6 HOH 29 429 19  HOH HOH B . 
CA 6 HOH 30 430 45  HOH HOH B . 
CA 6 HOH 31 431 63  HOH HOH B . 
CA 6 HOH 32 432 3   HOH HOH B . 
CA 6 HOH 33 433 72  HOH HOH B . 
CA 6 HOH 34 434 132 HOH HOH B . 
CA 6 HOH 35 435 16  HOH HOH B . 
CA 6 HOH 36 436 167 HOH HOH B . 
CA 6 HOH 37 437 149 HOH HOH B . 
CA 6 HOH 38 438 119 HOH HOH B . 
CA 6 HOH 39 439 70  HOH HOH B . 
CA 6 HOH 40 440 90  HOH HOH B . 
CA 6 HOH 41 441 23  HOH HOH B . 
CA 6 HOH 42 442 56  HOH HOH B . 
CA 6 HOH 43 443 50  HOH HOH B . 
CA 6 HOH 44 444 27  HOH HOH B . 
CA 6 HOH 45 445 145 HOH HOH B . 
CA 6 HOH 46 446 59  HOH HOH B . 
CA 6 HOH 47 447 110 HOH HOH B . 
CA 6 HOH 48 448 65  HOH HOH B . 
CA 6 HOH 49 449 155 HOH HOH B . 
CA 6 HOH 50 450 37  HOH HOH B . 
CA 6 HOH 51 451 168 HOH HOH B . 
CA 6 HOH 52 452 12  HOH HOH B . 
CA 6 HOH 53 453 39  HOH HOH B . 
CA 6 HOH 54 454 22  HOH HOH B . 
CA 6 HOH 55 455 48  HOH HOH B . 
CA 6 HOH 56 456 173 HOH HOH B . 
CA 6 HOH 57 457 162 HOH HOH B . 
CA 6 HOH 58 458 77  HOH HOH B . 
CA 6 HOH 59 459 178 HOH HOH B . 
CA 6 HOH 60 460 128 HOH HOH B . 
CA 6 HOH 61 461 188 HOH HOH B . 
CA 6 HOH 62 462 161 HOH HOH B . 
CA 6 HOH 63 463 184 HOH HOH B . 
CA 6 HOH 64 464 57  HOH HOH B . 
CA 6 HOH 65 465 87  HOH HOH B . 
CA 6 HOH 66 466 116 HOH HOH B . 
CA 6 HOH 67 467 38  HOH HOH B . 
CA 6 HOH 68 468 151 HOH HOH B . 
CA 6 HOH 69 469 158 HOH HOH B . 
CA 6 HOH 70 470 94  HOH HOH B . 
CA 6 HOH 71 471 164 HOH HOH B . 
CA 6 HOH 72 472 138 HOH HOH B . 
CA 6 HOH 73 473 159 HOH HOH B . 
CA 6 HOH 74 474 163 HOH HOH B . 
CA 6 HOH 75 475 97  HOH HOH B . 
CA 6 HOH 76 476 187 HOH HOH B . 
CA 6 HOH 77 477 71  HOH HOH B . 
CA 6 HOH 78 478 41  HOH HOH B . 
CA 6 HOH 79 479 109 HOH HOH B . 
CA 6 HOH 80 480 165 HOH HOH B . 
CA 6 HOH 81 481 137 HOH HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.290 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G0G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.500 
_cell.length_a_esd                 ? 
_cell.length_b                     39.230 
_cell.length_b_esd                 ? 
_cell.length_c                     67.600 
_cell.length_c_esd                 ? 
_cell.volume                       313375.357 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9G0G 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   9G0G 
_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             2.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.65 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;100 mM HEPES pH 8.0,
200 mM MgCl2
30% (v/v) PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR scanner 300 mm plate' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    Graphite 
_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   1.5406 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5406 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          23.73 
_reflns.entry_id                                       9G0G 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               23.74 
_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                                     32367 
_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                           93.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.36 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.059 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_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_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.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_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 
1.70  1.8  ? ? ? ? ? ? 4800  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.679 ? ? 1 1 0.881 ? ? ? ? 0.614 ? ? ? ? ? ? ? ? ? 
1.80  1.9  ? ? ? ? ? ? 3955  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.335 ? ? 2 1 0.968 ? ? ? ? 0.305 ? ? ? ? ? ? ? ? ? 
1.90  2.1  ? ? ? ? ? ? 5893  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.157 ? ? 3 1 0.992 ? ? ? ? 0.143 ? ? ? ? ? ? ? ? ? 
2.10  8.0  ? ? ? ? ? ? 17366 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.048 ? ? 4 1 0.999 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? ? 
8.00  14.0 ? ? ? ? ? ? 285   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039 ? ? 5 1 0.999 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? ? 
14.00 17.0 ? ? ? ? ? ? 28    ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.056 ? ? 6 1 0.999 ? ? ? ? 0.043 ? ? ? ? ? ? ? ? ? 
17.00 50.0 ? ? ? ? ? ? 40    ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.853 ? ? 7 1 0.73  ? ? ? ? 2.386 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               34.04 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9G0G 
_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                            1.70 
_refine.ls_d_res_low                             21.54 
_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                     32313 
_refine.ls_number_reflns_R_free                  1619 
_refine.ls_number_reflns_R_work                  30694 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.83 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1751 
_refine.ls_R_factor_R_free                       0.2041 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1736 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.33 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             0.9000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.6000 
_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                 23.4688 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2237 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        21.54 
_refine_hist.number_atoms_solvent             166 
_refine_hist.number_atoms_total               2606 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2328 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         112 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0065  ? 2469 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7781  ? 3322 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0555  ? 388  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0078  ? 422  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.5622 ? 918  ? f_dihedral_angle_d ? ? 
# 
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_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 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.75  . . 127 2357 89.26 . . . . 0.3944 . . . . . . . . . . . 0.4522 
'X-RAY DIFFRACTION' 1.75 1.81  . . 130 2479 90.65 . . . . 0.2186 . . . . . . . . . . . 0.2893 
'X-RAY DIFFRACTION' 1.81 1.87  . . 131 2478 91.61 . . . . 0.2017 . . . . . . . . . . . 0.2370 
'X-RAY DIFFRACTION' 1.87 1.95  . . 130 2494 91.91 . . . . 0.1944 . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 1.95 2.03  . . 131 2495 92.76 . . . . 0.1716 . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 2.03 2.14  . . 134 2531 93.48 . . . . 0.1644 . . . . . . . . . . . 0.2126 
'X-RAY DIFFRACTION' 2.14 2.28  . . 134 2557 93.93 . . . . 0.1658 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 2.28 2.45  . . 137 2601 94.90 . . . . 0.1697 . . . . . . . . . . . 0.2347 
'X-RAY DIFFRACTION' 2.45 2.70  . . 137 2611 95.68 . . . . 0.1741 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 2.70 3.09  . . 139 2630 96.55 . . . . 0.1676 . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 3.09 3.88  . . 142 2697 97.66 . . . . 0.1567 . . . . . . . . . . . 0.1723 
'X-RAY DIFFRACTION' 3.89 21.54 . . 147 2764 97.39 . . . . 0.1700 . . . . . . . . . . . 0.1774 
# 
_struct.entry_id                     9G0G 
_struct.title                        'BsCdaA in complex with Compound 7' 
_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        9G0G 
_struct_keywords.text            'CdaA, Cyclic-di-AMP, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 3 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 4 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 6 ? 
CA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CDAA_BACSU 
_struct_ref.pdbx_db_accession          Q45589 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TPVEEAQQKTIEAITKAINYMAKRRIGALLTIERDTGMGDYIETGIPLNAKVSSELLINIFIPNTPLHDGAVIMKNNEIA
AAACYLPLSESPFISKELGTRHRAAVGISEVTDSLTIIVSEETGGVSVAKNGDLHRELTEEALKEMLEAEFKK
;
_struct_ref.pdbx_align_begin           103 
# 
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 9G0G A 3 ? 155 ? Q45589 103 ? 255 ? 103 255 
2 1 9G0G B 3 ? 155 ? Q45589 103 ? 255 ? 103 255 
# 
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 9G0G GLY A 1 ? UNP Q45589 ? ? 'expression tag' 101 1 
1 9G0G PRO A 2 ? UNP Q45589 ? ? 'expression tag' 102 2 
2 9G0G GLY B 1 ? UNP Q45589 ? ? 'expression tag' 101 3 
2 9G0G PRO B 2 ? UNP Q45589 ? ? 'expression tag' 102 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5630  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  14980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 THR A 3   ? ARG A 27  ? THR A 103 ARG A 127 1 ? 25 
HELX_P HELX_P2  AA2 MET A 40  ? GLU A 45  ? MET A 140 GLU A 145 1 ? 6  
HELX_P HELX_P3  AA3 SER A 55  ? ILE A 64  ? SER A 155 ILE A 164 1 ? 10 
HELX_P HELX_P4  AA4 GLY A 101 ? THR A 114 ? GLY A 201 THR A 214 1 ? 14 
HELX_P HELX_P5  AA5 THR A 141 ? LYS A 154 ? THR A 241 LYS A 254 1 ? 14 
HELX_P HELX_P6  AA6 THR B 3   ? ARG B 27  ? THR B 103 ARG B 127 1 ? 25 
HELX_P HELX_P7  AA7 MET B 40  ? GLU B 45  ? MET B 140 GLU B 145 1 ? 6  
HELX_P HELX_P8  AA8 SER B 55  ? ILE B 64  ? SER B 155 ILE B 164 1 ? 10 
HELX_P HELX_P9  AA9 GLY B 101 ? THR B 114 ? GLY B 201 THR B 214 1 ? 14 
HELX_P HELX_P10 AB1 THR B 141 ? LYS B 155 ? THR B 241 LYS B 255 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 48  ? LYS A 53  ? ILE A 148 LYS A 153 
AA1 2 GLU A 80  ? CYS A 86  ? GLU A 180 CYS A 186 
AA1 3 ALA A 73  ? LYS A 77  ? ALA A 173 LYS A 177 
AA1 4 ALA A 30  ? ILE A 34  ? ALA A 130 ILE A 134 
AA1 5 LEU A 117 ? VAL A 121 ? LEU A 217 VAL A 221 
AA1 6 VAL A 128 ? LYS A 132 ? VAL A 228 LYS A 232 
AA1 7 ASP A 135 ? HIS A 137 ? ASP A 235 HIS A 237 
AA2 1 ILE B 48  ? ALA B 52  ? ILE B 148 ALA B 152 
AA2 2 GLU B 80  ? CYS B 86  ? GLU B 180 CYS B 186 
AA2 3 ALA B 73  ? LYS B 77  ? ALA B 173 LYS B 177 
AA2 4 ALA B 30  ? ILE B 34  ? ALA B 130 ILE B 134 
AA2 5 LEU B 117 ? VAL B 121 ? LEU B 217 VAL B 221 
AA2 6 VAL B 128 ? LYS B 132 ? VAL B 228 LYS B 232 
AA2 7 ASP B 135 ? HIS B 137 ? ASP B 235 HIS B 237 
# 
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 ALA A 52  ? N ALA A 152 O ILE A 81  ? O ILE A 181 
AA1 2 3 O CYS A 86  ? O CYS A 186 N ALA A 73  ? N ALA A 173 
AA1 3 4 O VAL A 74  ? O VAL A 174 N THR A 33  ? N THR A 133 
AA1 4 5 N ILE A 34  ? N ILE A 134 O LEU A 117 ? O LEU A 217 
AA1 5 6 N ILE A 120 ? N ILE A 220 O SER A 129 ? O SER A 229 
AA1 6 7 N VAL A 130 ? N VAL A 230 O HIS A 137 ? O HIS A 237 
AA2 1 2 N ILE B 48  ? N ILE B 148 O ALA B 84  ? O ALA B 184 
AA2 2 3 O CYS B 86  ? O CYS B 186 N ALA B 73  ? N ALA B 173 
AA2 3 4 O VAL B 74  ? O VAL B 174 N THR B 33  ? N THR B 133 
AA2 4 5 N LEU B 32  ? N LEU B 132 O ILE B 119 ? O ILE B 219 
AA2 5 6 N ILE B 120 ? N ILE B 220 O SER B 129 ? O SER B 229 
AA2 6 7 N VAL B 130 ? N VAL B 230 O HIS B 137 ? O HIS B 237 
# 
_pdbx_entry_details.entry_id                   9G0G 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 136 ? ? -117.42 -118.42 
2 1 ARG B 136 ? ? -118.30 -122.32 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    CL 
_pdbx_struct_special_symmetry.auth_seq_id     309 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   Y 
_pdbx_struct_special_symmetry.label_comp_id   CL 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 19.842635659   -20.7457989678 16.3608593052 0.288671161661 ? -0.0102485006472 ? -0.035828353193   
? 0.192475541294 ? 0.0143786103703  ? 0.304808598798 ? 1.05872128075  ? -0.0663334073674 ? -0.690620619062    ? 0.791244992031 ? 
0.186850814637   ? 0.44490818022  ? 0.244770096583   ? 0.0499606338321 ? -0.546592511618    ? -0.134438879659  ? -0.031590973928  
? -0.0658434227487 ? 0.76086885035    ? 0.0981286164995  ? 0.00843622604024   ? 
2  'X-RAY DIFFRACTION' ? refined 14.0038909075  -8.61230339871 17.7703877735 0.219023922864 ? -0.0341488374708 ? 0.00559800599063  
? 0.180185072859 ? -0.0235169840949 ? 0.186589414415 ? 2.73232056993  ? 0.614632431329   ? -1.08289450183     ? 1.68498453492  ? 
-0.0260451731118 ? 0.347965204701 ? 0.116394069136   ? -0.1417522355   ? 0.145386750862     ? 0.116405019736   ? -0.0183648223957 
? 0.0142574578175  ? -0.0870516697673 ? 0.0635384528069  ? 0.00161842643321   ? 
3  'X-RAY DIFFRACTION' ? refined 23.3881400077  2.32624206096  8.08241296387 0.258080793605 ? -0.0293939871548 ? 0.00737168820549  
? 0.347028017995 ? 0.117818680019   ? 0.284561729755 ? 2.12267795562  ? 1.55159031221    ? -1.05778871276     ? 1.09916901622  ? 
-0.86705959209   ? 1.21378360038  ? 0.148348374565   ? 0.765635932438  ? 1.1804803764       ? -0.0979486014561 ? 0.230075403796   
? 0.527260670307   ? -0.129563798521  ? -0.196711308556  ? 0.159543167831     ? 
4  'X-RAY DIFFRACTION' ? refined 24.2459537488  -2.55091317111 13.2034111241 0.222327116022 ? -0.0479786960593 ? 0.0140572108885   
? 0.186178727967 ? 0.003362440876   ? 0.230493987963 ? 0.43506565115  ? -0.413783049398  ? -0.0512508358841   ? 0.422250230895 ? 
0.0645737399054  ? 0.219133137227 ? 0.0900231494397  ? 0.214175473994  ? 0.173325947695     ? -0.0750467001808 ? 0.0206751002001  
? -0.105770448954  ? -0.196534102266  ? 0.174205673371   ? 0.00763143004533   ? 
5  'X-RAY DIFFRACTION' ? refined 27.7087597398  -8.43939628321 7.23436387964 0.258062518155 ? -0.0275973862661 ? 0.010650745444    
? 0.295371028419 ? 0.00969206660016 ? 0.222833944767 ? 0.25380403596  ? -0.159635901563  ? -0.000302800641218 ? 0.483365147316 ? 
0.25410628349    ? 0.212025461695 ? 0.037179960528   ? 0.410251295596  ? 0.152178272775     ? -0.229211168324  ? -0.0331884271683 
? -0.143102976972  ? -0.156076915237  ? 0.200450851756   ? 2.09871489752e-07  ? 
6  'X-RAY DIFFRACTION' ? refined 29.7642763159  -17.6213190638 17.4350651078 0.316873673859 ? 0.0157300246129  ? -0.0303031446858  
? 0.406842453547 ? 0.073860743806   ? 0.342702109717 ? 0.180398158456 ? -0.0854572555378 ? -0.00498431610222  ? 0.140762740015 ? 
-0.173135929153  ? 0.205023500559 ? -0.17931604799   ? -0.550294646581 ? -0.211187696512    ? 0.503700988384   ? -0.0816837911112 
? -0.431199637016  ? 0.353687594549   ? 0.292253435228   ? 7.51648979462e-07  ? 
7  'X-RAY DIFFRACTION' ? refined -7.50346076135 -5.45404699603 21.3437247049 0.326569590233 ? 0.0142833970753  ? -0.00660017316211 
? 0.189730129353 ? 0.0135903917757  ? 0.332538657129 ? 0.630003832113 ? -0.359733601712  ? 0.24089602954      ? 0.485423415385 ? 
-0.0499043147686 ? 0.451726519502 ? -0.127150433617  ? 0.114468911298  ? 0.439525274866     ? -0.0475762870147 ? -0.0130024935435 
? -0.0236829192433 ? -0.798694185919  ? -0.258955487006  ? -0.025897495676    ? 
8  'X-RAY DIFFRACTION' ? refined -5.79472255369 -21.8104728052 23.4621543529 0.221119969662 ? -0.0264416132956 ? -0.0170209678077  
? 0.252494273273 ? 0.0175752153275  ? 0.200398867536 ? 1.57098516737  ? 0.242802112474   ? 0.171907227415     ? 0.537994509852 ? 
-0.070395461443  ? 0.313520110448 ? 0.0715785500312  ? -0.200368985831 ? -0.000155015531167 ? 0.0432574977222  ? 0.055121977643   
? 0.04560777597    ? -0.074058157648  ? -0.169584039608  ? -2.93075997214e-07 ? 
9  'X-RAY DIFFRACTION' ? refined 1.08154494445  -15.9703382501 18.7120637101 0.202694394684 ? -0.0254525528171 ? -0.00199464668771 
? 0.20437113269  ? 0.00516671307819 ? 0.193114986719 ? 1.79995179781  ? -0.100120220045  ? -0.381480398835    ? 1.73131424887  ? 
-0.99612092832   ? 0.533111980289 ? 0.0262227443109  ? 0.13020386876   ? 0.019556451005     ? 0.113631981268   ? 0.0546657810151  
? -0.0127122892074 ? 0.0627527858584  ? -0.0944444728671 ? 4.02145670333e-07  ? 
10 'X-RAY DIFFRACTION' ? refined -13.4392207697 -29.365334668  14.9019485073 0.227160363998 ? -0.0514494600389 ? -0.0525122067196  
? 0.406454404737 ? -0.0308014526829 ? 0.286183729531 ? 0.162866406365 ? -0.137687777439  ? -0.238619855103    ? 0.360760813976 ? 
0.244669146723   ? 0.142924786685 ? -0.146854662485  ? 1.41474100002   ? -0.514768416314    ? -0.165157520133  ? 0.294726414056   
? -0.0116261838492 ? -0.064819196498  ? 0.103149496289   ? 0.00318353132128   ? 
11 'X-RAY DIFFRACTION' ? refined -14.9512073635 -21.4130829674 16.9294006229 0.230094785125 ? -0.0171103629613 ? -0.00620040863549 
? 0.226156195653 ? 0.0257545476112  ? 0.214654952206 ? 1.57434477013  ? 0.182649161557   ? 0.771154474447     ? 1.02905829443  ? 
-0.509806176051  ? 0.505829229954 ? 0.0977493452169  ? 0.0186499360428 ? -0.0833109222092   ? 0.0126516614785  ? 0.00239634912292 
? 0.0948142351593  ? -0.0517917485476 ? -0.255778117127  ? 6.40029481534e-08  ? 
12 'X-RAY DIFFRACTION' ? refined -16.5096843974 -9.01942956349 24.3898966938 0.400513631876 ? -0.0169733958344 ? 0.116497177236    
? 0.411997402534 ? -0.0741874793302 ? 0.423596538392 ? 0.290299452172 ? 0.180968243674   ? 0.0601363974247    ? 0.427392288937 ? 
0.370054303244   ? 0.297759510476 ? -0.0586852902577 ? -0.653880016597 ? 0.410641392245     ? 0.585436186026   ? -0.0737912087973 
? 0.472850097074   ? -0.546491957528  ? -0.27681342269   ? -0.0404663529895   ? 
# 
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  A 1   A 103 ? A 24  A 126 ? ? 
;chain 'A' and (resid 103 through 126 )
;
2  'X-RAY DIFFRACTION' 2  A 25  A 127 ? A 81  A 183 ? ? 
;chain 'A' and (resid 127 through 183 )
;
3  'X-RAY DIFFRACTION' 3  A 82  A 184 ? A 99  A 201 ? ? 
;chain 'A' and (resid 184 through 201 )
;
4  'X-RAY DIFFRACTION' 4  A 100 A 202 ? A 119 A 221 ? ? 
;chain 'A' and (resid 202 through 221 )
;
5  'X-RAY DIFFRACTION' 5  A 120 A 222 ? A 139 A 241 ? ? 
;chain 'A' and (resid 222 through 241 )
;
6  'X-RAY DIFFRACTION' 6  A 140 A 242 ? A 152 A 254 ? ? 
;chain 'A' and (resid 242 through 254 )
;
7  'X-RAY DIFFRACTION' 7  M 1   B 102 ? M 25  B 126 ? ? 
;chain 'B' and (resid 102 through 126 )
;
8  'X-RAY DIFFRACTION' 8  M 26  B 127 ? M 45  B 146 ? ? 
;chain 'B' and (resid 127 through 146 )
;
9  'X-RAY DIFFRACTION' 9  M 46  B 147 ? M 82  B 183 ? ? 
;chain 'B' and (resid 147 through 183 )
;
10 'X-RAY DIFFRACTION' 10 M 83  B 184 ? M 100 B 201 ? ? 
;chain 'B' and (resid 184 through 201 )
;
11 'X-RAY DIFFRACTION' 11 M 101 B 202 ? M 140 B 241 ? ? 
;chain 'B' and (resid 202 through 241 )
;
12 'X-RAY DIFFRACTION' 12 M 141 B 242 ? M 154 B 255 ? ? 
;chain 'B' and (resid 242 through 255 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       485 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.38 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 A GLY 101 ? A GLY 1   
2 1 Y 1 A PRO 102 ? A PRO 2   
3 1 Y 1 A LYS 255 ? A LYS 155 
4 1 Y 1 B GLY 101 ? B GLY 1   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
DMS S    S  N N 89  
DMS O    O  N N 90  
DMS C1   C  N N 91  
DMS C2   C  N N 92  
DMS H11  H  N N 93  
DMS H12  H  N N 94  
DMS H13  H  N N 95  
DMS H21  H  N N 96  
DMS H22  H  N N 97  
DMS H23  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PEG C1   C  N N 261 
PEG O1   O  N N 262 
PEG C2   C  N N 263 
PEG O2   O  N N 264 
PEG C3   C  N N 265 
PEG C4   C  N N 266 
PEG O4   O  N N 267 
PEG H11  H  N N 268 
PEG H12  H  N N 269 
PEG HO1  H  N N 270 
PEG H21  H  N N 271 
PEG H22  H  N N 272 
PEG H31  H  N N 273 
PEG H32  H  N N 274 
PEG H41  H  N N 275 
PEG H42  H  N N 276 
PEG HO4  H  N N 277 
PHE N    N  N N 278 
PHE CA   C  N S 279 
PHE C    C  N N 280 
PHE O    O  N N 281 
PHE CB   C  N N 282 
PHE CG   C  Y N 283 
PHE CD1  C  Y N 284 
PHE CD2  C  Y N 285 
PHE CE1  C  Y N 286 
PHE CE2  C  Y N 287 
PHE CZ   C  Y N 288 
PHE OXT  O  N N 289 
PHE H    H  N N 290 
PHE H2   H  N N 291 
PHE HA   H  N N 292 
PHE HB2  H  N N 293 
PHE HB3  H  N N 294 
PHE HD1  H  N N 295 
PHE HD2  H  N N 296 
PHE HE1  H  N N 297 
PHE HE2  H  N N 298 
PHE HZ   H  N N 299 
PHE HXT  H  N N 300 
PRO N    N  N N 301 
PRO CA   C  N S 302 
PRO C    C  N N 303 
PRO O    O  N N 304 
PRO CB   C  N N 305 
PRO CG   C  N N 306 
PRO CD   C  N N 307 
PRO OXT  O  N N 308 
PRO H    H  N N 309 
PRO HA   H  N N 310 
PRO HB2  H  N N 311 
PRO HB3  H  N N 312 
PRO HG2  H  N N 313 
PRO HG3  H  N N 314 
PRO HD2  H  N N 315 
PRO HD3  H  N N 316 
PRO HXT  H  N N 317 
SER N    N  N N 318 
SER CA   C  N S 319 
SER C    C  N N 320 
SER O    O  N N 321 
SER CB   C  N N 322 
SER OG   O  N N 323 
SER OXT  O  N N 324 
SER H    H  N N 325 
SER H2   H  N N 326 
SER HA   H  N N 327 
SER HB2  H  N N 328 
SER HB3  H  N N 329 
SER HG   H  N N 330 
SER HXT  H  N N 331 
THR N    N  N N 332 
THR CA   C  N S 333 
THR C    C  N N 334 
THR O    O  N N 335 
THR CB   C  N R 336 
THR OG1  O  N N 337 
THR CG2  C  N N 338 
THR OXT  O  N N 339 
THR H    H  N N 340 
THR H2   H  N N 341 
THR HA   H  N N 342 
THR HB   H  N N 343 
THR HG1  H  N N 344 
THR HG21 H  N N 345 
THR HG22 H  N N 346 
THR HG23 H  N N 347 
THR HXT  H  N N 348 
TJ9 N1   N  Y N 349 
TJ9 N3   N  Y N 350 
TJ9 C4   C  Y N 351 
TJ9 C5   C  N N 352 
TJ9 C6   C  N N 353 
TJ9 C7   C  Y N 354 
TJ9 C8   C  Y N 355 
TJ9 C1   C  N N 356 
TJ9 C2   C  Y N 357 
TJ9 C3   C  Y N 358 
TJ9 C9   C  Y N 359 
TJ9 N2   N  N N 360 
TJ9 N4   N  N N 361 
TJ9 O1   O  N N 362 
TJ9 S1   S  Y N 363 
TJ9 S2   S  Y N 364 
TJ9 H1   H  N N 365 
TJ9 H2   H  N N 366 
TJ9 H3   H  N N 367 
TJ9 H4   H  N N 368 
TJ9 H5   H  N N 369 
TJ9 H6   H  N N 370 
TJ9 H7   H  N N 371 
TJ9 H8   H  N N 372 
TJ9 H9   H  N N 373 
TJ9 H10  H  N N 374 
TYR N    N  N N 375 
TYR CA   C  N S 376 
TYR C    C  N N 377 
TYR O    O  N N 378 
TYR CB   C  N N 379 
TYR CG   C  Y N 380 
TYR CD1  C  Y N 381 
TYR CD2  C  Y N 382 
TYR CE1  C  Y N 383 
TYR CE2  C  Y N 384 
TYR CZ   C  Y N 385 
TYR OH   O  N N 386 
TYR OXT  O  N N 387 
TYR H    H  N N 388 
TYR H2   H  N N 389 
TYR HA   H  N N 390 
TYR HB2  H  N N 391 
TYR HB3  H  N N 392 
TYR HD1  H  N N 393 
TYR HD2  H  N N 394 
TYR HE1  H  N N 395 
TYR HE2  H  N N 396 
TYR HH   H  N N 397 
TYR HXT  H  N N 398 
VAL N    N  N N 399 
VAL CA   C  N S 400 
VAL C    C  N N 401 
VAL O    O  N N 402 
VAL CB   C  N N 403 
VAL CG1  C  N N 404 
VAL CG2  C  N N 405 
VAL OXT  O  N N 406 
VAL H    H  N N 407 
VAL H2   H  N N 408 
VAL HA   H  N N 409 
VAL HB   H  N N 410 
VAL HG11 H  N N 411 
VAL HG12 H  N N 412 
VAL HG13 H  N N 413 
VAL HG21 H  N N 414 
VAL HG22 H  N N 415 
VAL HG23 H  N N 416 
VAL HXT  H  N N 417 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TJ9 N4  C9   sing N N 331 
TJ9 C1  C2   sing N N 332 
TJ9 N3  C9   doub Y N 333 
TJ9 N3  C7   sing Y N 334 
TJ9 C9  S2   sing Y N 335 
TJ9 C2  N1   sing Y N 336 
TJ9 C2  C3   doub Y N 337 
TJ9 C7  C3   sing N N 338 
TJ9 C7  C8   doub Y N 339 
TJ9 N1  C4   doub Y N 340 
TJ9 C3  S1   sing Y N 341 
TJ9 S2  C8   sing Y N 342 
TJ9 C4  S1   sing Y N 343 
TJ9 C4  N2   sing N N 344 
TJ9 N2  C5   sing N N 345 
TJ9 C5  O1   doub N N 346 
TJ9 C5  C6   sing N N 347 
TJ9 C6  H1   sing N N 348 
TJ9 C6  H2   sing N N 349 
TJ9 C6  H3   sing N N 350 
TJ9 C8  H4   sing N N 351 
TJ9 C1  H5   sing N N 352 
TJ9 C1  H6   sing N N 353 
TJ9 C1  H7   sing N N 354 
TJ9 N2  H8   sing N N 355 
TJ9 N4  H9   sing N N 356 
TJ9 N4  H10  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8OGM 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G0G 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008439 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000633 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025491 
_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]   0.014834 
_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 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A  1 3   ? 26.35700  -26.25700 32.65400 0.876 62.52310  ? 103 THR A N   1 
ATOM   2    C  CA  . THR A  1 3   ? 25.47400  -25.51700 33.55100 0.876 68.45247  ? 103 THR A CA  1 
ATOM   3    C  C   . THR A  1 3   ? 24.14600  -25.20400 32.85700 0.876 68.26790  ? 103 THR A C   1 
ATOM   4    O  O   . THR A  1 3   ? 24.07600  -25.21800 31.62700 0.876 64.91039  ? 103 THR A O   1 
ATOM   5    C  CB  . THR A  1 3   ? 26.12800  -24.20000 34.02900 0.876 69.38291  ? 103 THR A CB  1 
ATOM   6    O  OG1 . THR A  1 3   ? 26.05700  -23.22200 32.98400 0.876 68.20684  ? 103 THR A OG1 1 
ATOM   7    C  CG2 . THR A  1 3   ? 27.58500  -24.42800 34.41800 0.876 69.74555  ? 103 THR A CG2 1 
ATOM   8    N  N   . PRO A  1 4   ? 23.09400  -24.93100 33.64000 0.686 64.85677  ? 104 PRO A N   1 
ATOM   9    C  CA  . PRO A  1 4   ? 21.82000  -24.52500 33.01800 0.686 63.63808  ? 104 PRO A CA  1 
ATOM   10   C  C   . PRO A  1 4   ? 21.95200  -23.29300 32.14000 0.686 58.18857  ? 104 PRO A C   1 
ATOM   11   O  O   . PRO A  1 4   ? 21.43500  -23.28000 31.01400 0.686 50.60429  ? 104 PRO A O   1 
ATOM   12   C  CB  . PRO A  1 4   ? 20.90900  -24.27700 34.23000 0.686 57.27454  ? 104 PRO A CB  1 
ATOM   13   C  CG  . PRO A  1 4   ? 21.85000  -24.04600 35.37600 0.686 75.02755  ? 104 PRO A CG  1 
ATOM   14   C  CD  . PRO A  1 4   ? 22.99000  -24.97400 35.10800 0.686 70.67432  ? 104 PRO A CD  1 
ATOM   15   N  N   . VAL A  1 5   ? 22.63900  -22.25600 32.62900 0.865 55.50378  ? 105 VAL A N   1 
ATOM   16   C  CA  . VAL A  1 5   ? 22.87100  -21.05200 31.83000 0.865 64.49690  ? 105 VAL A CA  1 
ATOM   17   C  C   . VAL A  1 5   ? 23.53500  -21.41400 30.50600 0.865 66.00684  ? 105 VAL A C   1 
ATOM   18   O  O   . VAL A  1 5   ? 23.08500  -20.99700 29.43200 0.865 61.38993  ? 105 VAL A O   1 
ATOM   19   C  CB  . VAL A  1 5   ? 23.71400  -20.03300 32.62200 0.865 59.32472  ? 105 VAL A CB  1 
ATOM   20   C  CG1 . VAL A  1 5   ? 24.26800  -18.95800 31.69700 0.865 57.19376  ? 105 VAL A CG1 1 
ATOM   21   C  CG2 . VAL A  1 5   ? 22.89100  -19.40000 33.73400 0.865 62.89598  ? 105 VAL A CG2 1 
ATOM   22   N  N   . GLU A  1 6   ? 24.60800  -22.20900 30.56600 1.000 63.43378  ? 106 GLU A N   1 
ATOM   23   C  CA  . GLU A  1 6   ? 25.35300  -22.56100 29.36000 1.000 60.38795  ? 106 GLU A CA  1 
ATOM   24   C  C   . GLU A  1 6   ? 24.47000  -23.29400 28.35600 1.000 58.96624  ? 106 GLU A C   1 
ATOM   25   O  O   . GLU A  1 6   ? 24.47500  -22.97500 27.16100 1.000 52.60021  ? 106 GLU A O   1 
ATOM   26   C  CB  . GLU A  1 6   ? 26.57700  -23.40400 29.72700 1.000 69.74450  ? 106 GLU A CB  1 
ATOM   27   C  CG  . GLU A  1 6   ? 27.70100  -22.60000 30.37400 1.000 80.60964  ? 106 GLU A CG  1 
ATOM   28   C  CD  . GLU A  1 6   ? 28.80700  -23.46500 30.96400 1.000 89.22079  ? 106 GLU A CD  1 
ATOM   29   O  OE1 . GLU A  1 6   ? 28.68200  -24.71000 30.94400 1.000 82.31809  ? 106 GLU A OE1 1 
ATOM   30   O  OE2 . GLU A  1 6   ? 29.80400  -22.89200 31.45100 1.000 90.07932  ? 106 GLU A OE2 1 
ATOM   31   N  N   . GLU A  1 7   ? 23.70400  -24.28400 28.82300 1.000 55.08264  ? 107 GLU A N   1 
ATOM   32   C  CA  . GLU A  1 7   ? 22.80300  -25.00000 27.92600 1.000 60.17480  ? 107 GLU A CA  1 
ATOM   33   C  C   . GLU A  1 7   ? 21.76500  -24.05800 27.32800 1.000 54.79260  ? 107 GLU A C   1 
ATOM   34   O  O   . GLU A  1 7   ? 21.40800  -24.18400 26.15000 1.000 59.87607  ? 107 GLU A O   1 
ATOM   35   C  CB  . GLU A  1 7   ? 22.12400  -26.15300 28.66500 1.000 56.28762  ? 107 GLU A CB  1 
ATOM   36   C  CG  . GLU A  1 7   ? 21.34000  -27.08000 27.75100 1.000 76.84130  ? 107 GLU A CG  1 
ATOM   37   C  CD  . GLU A  1 7   ? 21.14700  -28.46500 28.34200 1.000 87.76939  ? 107 GLU A CD  1 
ATOM   38   O  OE1 . GLU A  1 7   ? 21.67500  -28.72000 29.44600 1.000 88.71981  ? 107 GLU A OE1 1 
ATOM   39   O  OE2 . GLU A  1 7   ? 20.47200  -29.29700 27.70000 1.000 91.01003  ? 107 GLU A OE2 1 
ATOM   40   N  N   . ALA A  1 8   ? 21.27600  -23.10300 28.12500 1.000 47.23669  ? 108 ALA A N   1 
ATOM   41   C  CA  . ALA A  1 8   ? 20.34300  -22.11300 27.59800 1.000 48.81242  ? 108 ALA A CA  1 
ATOM   42   C  C   . ALA A  1 8   ? 20.99800  -21.27600 26.50900 1.000 50.44111  ? 108 ALA A C   1 
ATOM   43   O  O   . ALA A  1 8   ? 20.38100  -20.99500 25.47500 1.000 40.82034  ? 108 ALA A O   1 
ATOM   44   C  CB  . ALA A  1 8   ? 19.82900  -21.21700 28.72600 1.000 49.71871  ? 108 ALA A CB  1 
ATOM   45   N  N   . GLN A  1 9   ? 22.25800  -20.88800 26.71700 1.000 41.10863  ? 109 GLN A N   1 
ATOM   46   C  CA  . GLN A  1 9   ? 22.96200  -20.07500 25.73100 1.000 45.48913  ? 109 GLN A CA  1 
ATOM   47   C  C   . GLN A  1 9   ? 23.11100  -20.81500 24.41100 1.000 37.08979  ? 109 GLN A C   1 
ATOM   48   O  O   . GLN A  1 9   ? 22.90300  -20.23800 23.33700 1.000 34.76778  ? 109 GLN A O   1 
ATOM   49   C  CB  . GLN A  1 9   ? 24.33700  -19.67800 26.26200 1.000 48.65640  ? 109 GLN A CB  1 
ATOM   50   C  CG  . GLN A  1 9   ? 24.31700  -18.68300 27.39400 1.000 54.37745  ? 109 GLN A CG  1 
ATOM   51   C  CD  . GLN A  1 9   ? 25.71600  -18.23900 27.77100 1.000 58.74964  ? 109 GLN A CD  1 
ATOM   52   O  OE1 . GLN A  1 9   ? 26.58700  -19.06200 28.06300 1.000 61.65393  ? 109 GLN A OE1 1 
ATOM   53   N  NE2 . GLN A  1 9   ? 25.94500  -16.93400 27.74500 1.000 63.10427  ? 109 GLN A NE2 1 
ATOM   54   N  N   . GLN A  1 10  ? 23.50600  -22.08900 24.47100 1.000 41.15809  ? 110 GLN A N   1 
ATOM   55   C  CA  . GLN A  1 10  ? 23.68800  -22.85800 23.24500 1.000 42.93168  ? 110 GLN A CA  1 
ATOM   56   C  C   . GLN A  1 10  ? 22.36100  -23.07900 22.53300 1.000 39.92275  ? 110 GLN A C   1 
ATOM   57   O  O   . GLN A  1 10  ? 22.30800  -23.07700 21.29600 1.000 36.67655  ? 110 GLN A O   1 
ATOM   58   C  CB  . GLN A  1 10  ? 24.37100  -24.18900 23.54700 1.000 49.06648  ? 110 GLN A CB  1 
ATOM   59   C  CG  . GLN A  1 10  ? 25.82400  -24.04300 23.96900 1.000 59.02202  ? 110 GLN A CG  1 
ATOM   60   C  CD  . GLN A  1 10  ? 26.66300  -23.31500 22.93000 1.000 76.68130  ? 110 GLN A CD  1 
ATOM   61   O  OE1 . GLN A  1 10  ? 26.62900  -23.64700 21.74000 1.000 66.87238  ? 110 GLN A OE1 1 
ATOM   62   N  NE2 . GLN A  1 10  ? 27.41600  -22.30900 23.37400 1.000 63.78296  ? 110 GLN A NE2 1 
ATOM   63   N  N   . LYS A  1 11  ? 21.27600  -23.26600 23.29300 1.000 33.03437  ? 111 LYS A N   1 
ATOM   64   C  CA  . LYS A  1 11  ? 19.96300  -23.35700 22.66300 1.000 36.29716  ? 111 LYS A CA  1 
ATOM   65   C  C   . LYS A  1 11  ? 19.62100  -22.06200 21.94000 1.000 29.79321  ? 111 LYS A C   1 
ATOM   66   O  O   . LYS A  1 11  ? 19.13000  -22.08700 20.80700 1.000 29.50086  ? 111 LYS A O   1 
ATOM   67   C  CB  . LYS A  1 11  ? 18.89700  -23.70200 23.70300 1.000 42.98818  ? 111 LYS A CB  1 
ATOM   68   C  CG  . LYS A  1 11  ? 18.90900  -25.17500 24.09500 1.000 52.89534  ? 111 LYS A CG  1 
ATOM   69   C  CD  . LYS A  1 11  ? 18.14900  -25.44000 25.38600 1.000 69.84357  ? 111 LYS A CD  1 
ATOM   70   C  CE  . LYS A  1 11  ? 18.30400  -26.89600 25.80700 1.000 80.24744  ? 111 LYS A CE  1 
ATOM   71   N  NZ  . LYS A  1 11  ? 17.76300  -27.16400 27.17100 1.000 88.87469  ? 111 LYS A NZ  1 
ATOM   72   N  N   . THR A  1 12  ? 19.90600  -20.91800 22.56900 1.000 27.77516  ? 112 THR A N   1 
ATOM   73   C  CA  . THR A  1 12  ? 19.65500  -19.63500 21.92200 1.000 28.50106  ? 112 THR A CA  1 
ATOM   74   C  C   . THR A  1 12  ? 20.50500  -19.47200 20.67000 1.000 27.66894  ? 112 THR A C   1 
ATOM   75   O  O   . THR A  1 12  ? 20.01700  -18.99800 19.63700 1.000 25.33900  ? 112 THR A O   1 
ATOM   76   C  CB  . THR A  1 12  ? 19.92600  -18.49100 22.89900 1.000 30.24324  ? 112 THR A CB  1 
ATOM   77   O  OG1 . THR A  1 12  ? 18.94700  -18.51400 23.94300 1.000 41.89267  ? 112 THR A OG1 1 
ATOM   78   C  CG2 . THR A  1 12  ? 19.88500  -17.14800 22.19800 1.000 27.65470  ? 112 THR A CG2 1 
ATOM   79   N  N   . ILE A  1 13  ? 21.78500  -19.84400 20.74000 1.000 22.75995  ? 113 ILE A N   1 
ATOM   80   C  CA  . ILE A  1 13  ? 22.63200  -19.75100 19.55100 1.000 23.67759  ? 113 ILE A CA  1 
ATOM   81   C  C   . ILE A  1 13  ? 22.08400  -20.64000 18.43900 1.000 27.82857  ? 113 ILE A C   1 
ATOM   82   O  O   . ILE A  1 13  ? 22.03700  -20.23700 17.26800 1.000 27.34689  ? 113 ILE A O   1 
ATOM   83   C  CB  . ILE A  1 13  ? 24.09400  -20.09900 19.89500 1.000 28.84560  ? 113 ILE A CB  1 
ATOM   84   C  CG1 . ILE A  1 13  ? 24.69700  -18.99900 20.78000 1.000 27.81663  ? 113 ILE A CG1 1 
ATOM   85   C  CG2 . ILE A  1 13  ? 24.90900  -20.29800 18.62400 1.000 32.04486  ? 113 ILE A CG2 1 
ATOM   86   C  CD1 . ILE A  1 13  ? 26.02300  -19.34800 21.39900 1.000 34.22203  ? 113 ILE A CD1 1 
ATOM   87   N  N   . GLU A  1 14  ? 21.64300  -21.85100 18.78300 1.000 25.50433  ? 114 GLU A N   1 
ATOM   88   C  CA  . GLU A  1 14  ? 21.11600  -22.74200 17.75400 1.000 28.23721  ? 114 GLU A CA  1 
ATOM   89   C  C   . GLU A  1 14  ? 19.84900  -22.17300 17.13300 1.000 30.42696  ? 114 GLU A C   1 
ATOM   90   O  O   . GLU A  1 14  ? 19.66400  -22.24500 15.91100 1.000 25.67061  ? 114 GLU A O   1 
ATOM   91   C  CB  . GLU A  1 14  ? 20.85700  -24.13400 18.32500 1.000 43.07179  ? 114 GLU A CB  1 
ATOM   92   C  CG  . GLU A  1 14  ? 20.97900  -25.22800 17.27500 1.000 55.62997  ? 114 GLU A CG  1 
ATOM   93   C  CD  . GLU A  1 14  ? 22.34500  -25.22200 16.60000 1.000 62.22559  ? 114 GLU A CD  1 
ATOM   94   O  OE1 . GLU A  1 14  ? 23.36900  -25.14400 17.32000 1.000 67.79477  ? 114 GLU A OE1 1 
ATOM   95   O  OE2 . GLU A  1 14  ? 22.39200  -25.27600 15.35100 1.000 64.15904  ? 114 GLU A OE2 1 
ATOM   96   N  N   . ALA A  1 15  ? 18.97700  -21.57300 17.95300 1.000 26.00417  ? 115 ALA A N   1 
ATOM   97   C  CA  . ALA A  1 15  ? 17.76400  -20.95000 17.42400 1.000 25.83568  ? 115 ALA A CA  1 
ATOM   98   C  C   . ALA A  1 15  ? 18.09700  -19.80500 16.47200 1.000 23.67589  ? 115 ALA A C   1 
ATOM   99   O  O   . ALA A  1 15  ? 17.50100  -19.69300 15.39300 1.000 22.64497  ? 115 ALA A O   1 
ATOM   100  C  CB  . ALA A  1 15  ? 16.88600  -20.44900 18.57700 1.000 26.48604  ? 115 ALA A CB  1 
ATOM   101  N  N   . ILE A  1 16  ? 19.04100  -18.94000 16.85600 1.000 20.06792  ? 116 ILE A N   1 
ATOM   102  C  CA  . ILE A  1 16  ? 19.42700  -17.83200 15.98500 1.000 20.38204  ? 116 ILE A CA  1 
ATOM   103  C  C   . ILE A  1 16  ? 19.99600  -18.35500 14.67900 1.000 24.78861  ? 116 ILE A C   1 
ATOM   104  O  O   . ILE A  1 16  ? 19.65200  -17.86600 13.59900 1.000 23.33779  ? 116 ILE A O   1 
ATOM   105  C  CB  . ILE A  1 16  ? 20.43800  -16.90600 16.68400 1.000 20.01517  ? 116 ILE A CB  1 
ATOM   106  C  CG1 . ILE A  1 16  ? 19.77600  -16.15500 17.84100 1.000 18.85691  ? 116 ILE A CG1 1 
ATOM   107  C  CG2 . ILE A  1 16  ? 21.02700  -15.90900 15.68700 1.000 21.75264  ? 116 ILE A CG2 1 
ATOM   108  C  CD1 . ILE A  1 16  ? 20.80500  -15.55600 18.81600 1.000 21.86442  ? 116 ILE A CD1 1 
ATOM   109  N  N   . THR A  1 17  ? 20.90600  -19.32900 14.75300 1.000 21.93496  ? 117 THR A N   1 
ATOM   110  C  CA  . THR A  1 17  ? 21.57400  -19.74300 13.52500 1.000 26.76573  ? 117 THR A CA  1 
ATOM   111  C  C   . THR A  1 17  ? 20.61300  -20.46100 12.58600 1.000 28.26334  ? 117 THR A C   1 
ATOM   112  O  O   . THR A  1 17  ? 20.71700  -20.30800 11.36200 1.000 26.23729  ? 117 THR A O   1 
ATOM   113  C  CB  . THR A  1 17  ? 22.79700  -20.61700 13.82900 1.000 32.65428  ? 117 THR A CB  1 
ATOM   114  O  OG1 . THR A  1 17  ? 22.39900  -21.79300 14.53800 1.000 32.43324  ? 117 THR A OG1 1 
ATOM   115  C  CG2 . THR A  1 17  ? 23.82700  -19.84500 14.66000 1.000 31.47582  ? 117 THR A CG2 1 
ATOM   116  N  N   . LYS A  1 18  ? 19.65200  -21.21600 13.13100 1.000 23.79275  ? 118 LYS A N   1 
ATOM   117  C  CA  . LYS A  1 18  ? 18.66900  -21.86700 12.26700 1.000 23.75786  ? 118 LYS A CA  1 
ATOM   118  C  C   . LYS A  1 18  ? 17.76200  -20.84300 11.59100 1.000 23.95896  ? 118 LYS A C   1 
ATOM   119  O  O   . LYS A  1 18  ? 17.43400  -20.98600 10.40500 1.000 24.25793  ? 118 LYS A O   1 
ATOM   120  C  CB  . LYS A  1 18  ? 17.85000  -22.87700 13.06800 1.000 26.96344  ? 118 LYS A CB  1 
ATOM   121  C  CG  . LYS A  1 18  ? 16.73600  -23.54300 12.30100 1.000 34.55251  ? 118 LYS A CG  1 
ATOM   122  C  CD  . LYS A  1 18  ? 16.36400  -24.86900 12.95600 1.000 59.50022  ? 118 LYS A CD  1 
ATOM   123  C  CE  . LYS A  1 18  ? 16.18700  -24.70000 14.45900 1.000 66.63269  ? 118 LYS A CE  1 
ATOM   124  N  NZ  . LYS A  1 18  ? 16.67100  -25.88000 15.23500 1.000 76.15031  ? 118 LYS A NZ  1 
ATOM   125  N  N   . ALA A  1 19  ? 17.35400  -19.80100 12.32400 1.000 21.10174  ? 119 ALA A N   1 
ATOM   126  C  CA  . ALA A  1 19  ? 16.50700  -18.76700 11.73100 1.000 21.61773  ? 119 ALA A CA  1 
ATOM   127  C  C   . ALA A  1 19  ? 17.26800  -17.97700 10.68300 1.000 21.03800  ? 119 ALA A C   1 
ATOM   128  O  O   . ALA A  1 19  ? 16.73400  -17.67800 9.61000  1.000 20.03375  ? 119 ALA A O   1 
ATOM   129  C  CB  . ALA A  1 19  ? 15.98300  -17.82000 12.80600 1.000 20.03038  ? 119 ALA A CB  1 
ATOM   130  N  N   . ILE A  1 20  ? 18.52000  -17.62800 10.97800 1.000 19.87915  ? 120 ILE A N   1 
ATOM   131  C  CA  . ILE A  1 20  ? 19.31200  -16.89100 9.99900  1.000 19.64692  ? 120 ILE A CA  1 
ATOM   132  C  C   . ILE A  1 20  ? 19.54900  -17.74600 8.76100  1.000 20.87908  ? 120 ILE A C   1 
ATOM   133  O  O   . ILE A  1 20  ? 19.50900  -17.24700 7.62900  1.000 23.53752  ? 120 ILE A O   1 
ATOM   134  C  CB  . ILE A  1 20  ? 20.63800  -16.41400 10.62300 1.000 20.34872  ? 120 ILE A CB  1 
ATOM   135  C  CG1 . ILE A  1 20  ? 20.37400  -15.38800 11.73400 1.000 22.30656  ? 120 ILE A CG1 1 
ATOM   136  C  CG2 . ILE A  1 20  ? 21.59300  -15.85500 9.52200  1.000 19.99791  ? 120 ILE A CG2 1 
ATOM   137  C  CD1 . ILE A  1 20  ? 19.84700  -14.04800 11.25200 1.000 22.87584  ? 120 ILE A CD1 1 
ATOM   138  N  N   . ASN A  1 21  ? 19.80300  -19.04600 8.94800  1.000 21.30756  ? 121 ASN A N   1 
ATOM   139  C  CA  . ASN A  1 21  ? 20.02000  -19.92200 7.79600  1.000 25.63285  ? 121 ASN A CA  1 
ATOM   140  C  C   . ASN A  1 21  ? 18.78700  -19.95300 6.91100  1.000 31.19517  ? 121 ASN A C   1 
ATOM   141  O  O   . ASN A  1 21  ? 18.88900  -19.84700 5.68400  1.000 28.62891  ? 121 ASN A O   1 
ATOM   142  C  CB  . ASN A  1 21  ? 20.37900  -21.33900 8.25300  1.000 33.60299  ? 121 ASN A CB  1 
ATOM   143  C  CG  . ASN A  1 21  ? 20.51900  -22.31600 7.08700  1.000 48.21653  ? 121 ASN A CG  1 
ATOM   144  O  OD1 . ASN A  1 21  ? 21.57700  -22.41000 6.46900  1.000 54.22851  ? 121 ASN A OD1 1 
ATOM   145  N  ND2 . ASN A  1 21  ? 19.45200  -23.05000 6.79000  1.000 45.18273  ? 121 ASN A ND2 1 
ATOM   146  N  N   . TYR A  1 22  ? 17.61100  -20.06700 7.52800  1.000 24.39001  ? 122 TYR A N   1 
ATOM   147  C  CA  . TYR A  1 22  ? 16.36200  -20.04600 6.77900  1.000 26.35812  ? 122 TYR A CA  1 
ATOM   148  C  C   . TYR A  1 22  ? 16.22200  -18.75600 5.98700  1.000 24.17274  ? 122 TYR A C   1 
ATOM   149  O  O   . TYR A  1 22  ? 15.93200  -18.77800 4.78400  1.000 27.27969  ? 122 TYR A O   1 
ATOM   150  C  CB  . TYR A  1 22  ? 15.18700  -20.21300 7.74500  1.000 26.67951  ? 122 TYR A CB  1 
ATOM   151  C  CG  . TYR A  1 22  ? 13.84000  -20.24900 7.07100  1.000 30.98437  ? 122 TYR A CG  1 
ATOM   152  C  CD1 . TYR A  1 22  ? 13.12400  -19.08100 6.83800  1.000 22.57302  ? 122 TYR A CD1 1 
ATOM   153  C  CD2 . TYR A  1 22  ? 13.28200  -21.45600 6.67200  1.000 49.20353  ? 122 TYR A CD2 1 
ATOM   154  C  CE1 . TYR A  1 22  ? 11.87200  -19.12500 6.20500  1.000 29.89395  ? 122 TYR A CE1 1 
ATOM   155  C  CE2 . TYR A  1 22  ? 12.05300  -21.50500 6.05500  1.000 44.49171  ? 122 TYR A CE2 1 
ATOM   156  C  CZ  . TYR A  1 22  ? 11.35400  -20.34100 5.82500  1.000 49.70691  ? 122 TYR A CZ  1 
ATOM   157  O  OH  . TYR A  1 22  ? 10.12800  -20.39400 5.20500  1.000 57.12440  ? 122 TYR A OH  1 
ATOM   158  N  N   . MET A  1 23  ? 16.41900  -17.61200 6.64600  1.000 20.47760  ? 123 MET A N   1 
ATOM   159  C  CA  . MET A  1 23  ? 16.20700  -16.33600 5.97200  1.000 22.10075  ? 123 MET A CA  1 
ATOM   160  C  C   . MET A  1 23  ? 17.26200  -16.07500 4.90500  1.000 21.43074  ? 123 MET A C   1 
ATOM   161  O  O   . MET A  1 23  ? 16.95900  -15.47200 3.86800  1.000 25.24105  ? 123 MET A O   1 
ATOM   162  C  CB  . MET A  1 23  ? 16.16300  -15.22000 7.00900  1.000 22.98577  ? 123 MET A CB  1 
ATOM   163  C  CG  . MET A  1 23  ? 14.94400  -15.39500 7.88700  1.000 20.14742  ? 123 MET A CG  1 
ATOM   164  S  SD  . MET A  1 23  ? 14.71900  -14.08300 9.06900  1.000 25.53394  ? 123 MET A SD  1 
ATOM   165  C  CE  . MET A  1 23  ? 16.13900  -14.33100 10.13300 1.000 23.56223  ? 123 MET A CE  1 
ATOM   166  N  N   . ALA A  1 24  ? 18.49000  -16.54300 5.12500  1.000 22.00639  ? 124 ALA A N   1 
ATOM   167  C  CA  . ALA A  1 24  ? 19.51900  -16.41100 4.10000  1.000 22.26544  ? 124 ALA A CA  1 
ATOM   168  C  C   . ALA A  1 24  ? 19.14400  -17.18900 2.84600  1.000 29.77059  ? 124 ALA A C   1 
ATOM   169  O  O   . ALA A  1 24  ? 19.30500  -16.68900 1.72200  1.000 25.69817  ? 124 ALA A O   1 
ATOM   170  C  CB  . ALA A  1 24  ? 20.86700  -16.89200 4.65100  1.000 24.44042  ? 124 ALA A CB  1 
ATOM   171  N  N   . LYS A  1 25  ? 18.63200  -18.41200 3.01800  1.000 23.13112  ? 125 LYS A N   1 
ATOM   172  C  CA  . LYS A  1 25  ? 18.26500  -19.23200 1.86200  1.000 24.75344  ? 125 LYS A CA  1 
ATOM   173  C  C   . LYS A  1 25  ? 17.12900  -18.60400 1.06100  1.000 25.50311  ? 125 LYS A C   1 
ATOM   174  O  O   . LYS A  1 25  ? 17.09900  -18.71000 -0.17000 1.000 28.71811  ? 125 LYS A O   1 
ATOM   175  C  CB  . LYS A  1 25  ? 17.86600  -20.63400 2.31600  1.000 29.06751  ? 125 LYS A CB  1 
ATOM   176  C  CG  . LYS A  1 25  ? 18.92300  -21.36700 3.12500  1.000 38.90132  ? 125 LYS A CG  1 
ATOM   177  C  CD  . LYS A  1 25  ? 19.73900  -22.34300 2.30700  1.000 64.07836  ? 125 LYS A CD  1 
ATOM   178  C  CE  . LYS A  1 25  ? 20.28100  -23.46700 3.19200  1.000 64.00947  ? 125 LYS A CE  1 
ATOM   179  N  NZ  . LYS A  1 25  ? 21.74500  -23.36400 3.45800  1.000 71.60639  ? 125 LYS A NZ  1 
ATOM   180  N  N   A ARG A  1 26  ? 16.18000  -17.96200 1.73800  0.503 26.23640  ? 126 ARG A N   1 
ATOM   181  N  N   B ARG A  1 26  ? 16.18000  -17.96100 1.73600  0.497 26.23695  ? 126 ARG A N   1 
ATOM   182  C  CA  A ARG A  1 26  ? 15.05300  -17.32500 1.06300  0.503 29.60134  ? 126 ARG A CA  1 
ATOM   183  C  CA  B ARG A  1 26  ? 15.05700  -17.32900 1.04900  0.497 29.59450  ? 126 ARG A CA  1 
ATOM   184  C  C   A ARG A  1 26  ? 15.32300  -15.87500 0.69200  0.503 29.45062  ? 126 ARG A C   1 
ATOM   185  C  C   B ARG A  1 26  ? 15.32700  -15.87700 0.68300  0.497 29.44793  ? 126 ARG A C   1 
ATOM   186  O  O   A ARG A  1 26  ? 14.47600  -15.25500 0.03400  0.503 28.32714  ? 126 ARG A O   1 
ATOM   187  O  O   B ARG A  1 26  ? 14.48300  -15.25800 0.02100  0.497 28.32564  ? 126 ARG A O   1 
ATOM   188  C  CB  A ARG A  1 26  ? 13.79300  -17.37400 1.93900  0.503 27.82375  ? 126 ARG A CB  1 
ATOM   189  C  CB  B ARG A  1 26  ? 13.78600  -17.38000 1.90900  0.497 27.79889  ? 126 ARG A CB  1 
ATOM   190  C  CG  A ARG A  1 26  ? 13.35500  -18.76000 2.38600  0.503 33.96504  ? 126 ARG A CG  1 
ATOM   191  C  CG  B ARG A  1 26  ? 13.58400  -18.65600 2.72000  0.497 37.01163  ? 126 ARG A CG  1 
ATOM   192  C  CD  A ARG A  1 26  ? 12.76400  -19.54300 1.24500  0.503 38.24780  ? 126 ARG A CD  1 
ATOM   193  C  CD  B ARG A  1 26  ? 12.84700  -19.71000 1.93400  0.497 34.95468  ? 126 ARG A CD  1 
ATOM   194  N  NE  A ARG A  1 26  ? 11.67900  -18.82100 0.59100  0.503 33.49522  ? 126 ARG A NE  1 
ATOM   195  N  NE  B ARG A  1 26  ? 12.42200  -20.84800 2.74400  0.497 36.13561  ? 126 ARG A NE  1 
ATOM   196  C  CZ  A ARG A  1 26  ? 10.40900  -19.20100 0.59900  0.503 35.21057  ? 126 ARG A CZ  1 
ATOM   197  C  CZ  B ARG A  1 26  ? 13.02900  -22.02800 2.75900  0.497 46.09273  ? 126 ARG A CZ  1 
ATOM   198  N  NH1 A ARG A  1 26  ? 10.02600  -20.32200 1.19100  0.503 44.30139  ? 126 ARG A NH1 1 
ATOM   199  N  NH1 B ARG A  1 26  ? 14.15200  -22.23700 2.09100  0.497 52.83884  ? 126 ARG A NH1 1 
ATOM   200  N  NH2 A ARG A  1 26  ? 9.50300   -18.44200 -0.00900 0.503 33.55277  ? 126 ARG A NH2 1 
ATOM   201  N  NH2 B ARG A  1 26  ? 12.48700  -23.02900 3.44700  0.497 33.75937  ? 126 ARG A NH2 1 
ATOM   202  N  N   . ARG A  1 27  ? 16.46500  -15.32300 1.10900  1.000 24.07973  ? 127 ARG A N   1 
ATOM   203  C  CA  . ARG A  1 27  ? 16.80100  -13.91200 0.90700  1.000 21.43727  ? 127 ARG A CA  1 
ATOM   204  C  C   . ARG A  1 27  ? 15.76700  -12.98300 1.54200  1.000 26.53726  ? 127 ARG A C   1 
ATOM   205  O  O   . ARG A  1 27  ? 15.34800  -11.99000 0.95100  1.000 24.46144  ? 127 ARG A O   1 
ATOM   206  C  CB  . ARG A  1 27  ? 16.99500  -13.60500 -0.58000 1.000 27.57108  ? 127 ARG A CB  1 
ATOM   207  C  CG  . ARG A  1 27  ? 17.97200  -14.58800 -1.17300 1.000 27.10164  ? 127 ARG A CG  1 
ATOM   208  C  CD  . ARG A  1 27  ? 18.25400  -14.36600 -2.63300 1.000 31.26789  ? 127 ARG A CD  1 
ATOM   209  N  NE  . ARG A  1 27  ? 19.08700  -15.46300 -3.10200 1.000 28.36724  ? 127 ARG A NE  1 
ATOM   210  C  CZ  . ARG A  1 27  ? 19.32200  -15.73400 -4.37500 1.000 28.70520  ? 127 ARG A CZ  1 
ATOM   211  N  NH1 . ARG A  1 27  ? 18.83600  -14.97100 -5.34500 1.000 31.21554  ? 127 ARG A NH1 1 
ATOM   212  N  NH2 . ARG A  1 27  ? 20.04800  -16.80800 -4.68600 1.000 33.09623  ? 127 ARG A NH2 1 
ATOM   213  N  N   . ILE A  1 28  ? 15.39200  -13.30300 2.78200  1.000 23.08638  ? 128 ILE A N   1 
ATOM   214  C  CA  . ILE A  1 28  ? 14.49400  -12.48300 3.58500  1.000 19.05863  ? 128 ILE A CA  1 
ATOM   215  C  C   . ILE A  1 28  ? 15.33800  -11.51200 4.40300  1.000 22.26019  ? 128 ILE A C   1 
ATOM   216  O  O   . ILE A  1 28  ? 16.19000  -11.94000 5.18800  1.000 21.63956  ? 128 ILE A O   1 
ATOM   217  C  CB  . ILE A  1 28  ? 13.63700  -13.36400 4.50600  1.000 22.00515  ? 128 ILE A CB  1 
ATOM   218  C  CG1 . ILE A  1 28  ? 12.65000  -14.21000 3.68800  1.000 22.28061  ? 128 ILE A CG1 1 
ATOM   219  C  CG2 . ILE A  1 28  ? 12.92400  -12.52000 5.56500  1.000 22.01976  ? 128 ILE A CG2 1 
ATOM   220  C  CD1 . ILE A  1 28  ? 12.09600  -15.39300 4.46300  1.000 31.14548  ? 128 ILE A CD1 1 
ATOM   221  N  N   . GLY A  1 29  ? 15.12100  -10.21300 4.21600  1.000 20.15724  ? 129 GLY A N   1 
ATOM   222  C  CA  . GLY A  1 29  ? 15.89600  -9.23700  4.96800  1.000 22.98740  ? 129 GLY A CA  1 
ATOM   223  C  C   . GLY A  1 29  ? 15.59900  -9.32800  6.45500  1.000 21.84139  ? 129 GLY A C   1 
ATOM   224  O  O   . GLY A  1 29  ? 14.45500  -9.53000  6.86700  1.000 23.24014  ? 129 GLY A O   1 
ATOM   225  N  N   . ALA A  1 30  ? 16.65100  -9.17300  7.27300  1.000 18.62557  ? 130 ALA A N   1 
ATOM   226  C  CA  . ALA A  1 30  ? 16.50700  -9.33800  8.71400  1.000 16.54180  ? 130 ALA A CA  1 
ATOM   227  C  C   . ALA A  1 30  ? 17.57100  -8.53200  9.44100  1.000 19.06009  ? 130 ALA A C   1 
ATOM   228  O  O   . ALA A  1 30  ? 18.65200  -8.27900  8.91900  1.000 18.64061  ? 130 ALA A O   1 
ATOM   229  C  CB  . ALA A  1 30  ? 16.60000  -10.80900 9.13200  1.000 18.26436  ? 130 ALA A CB  1 
ATOM   230  N  N   . LEU A  1 31  ? 17.25100  -8.15600  10.67200 1.000 19.79646  ? 131 LEU A N   1 
ATOM   231  C  CA  . LEU A  1 31  ? 18.11200  -7.27800  11.45300 1.000 20.69656  ? 131 LEU A CA  1 
ATOM   232  C  C   . LEU A  1 31  ? 17.89900  -7.66200  12.90700 1.000 18.24499  ? 131 LEU A C   1 
ATOM   233  O  O   . LEU A  1 31  ? 16.81200  -7.44400  13.44100 1.000 20.21151  ? 131 LEU A O   1 
ATOM   234  C  CB  . LEU A  1 31  ? 17.75800  -5.81500  11.20500 1.000 22.38164  ? 131 LEU A CB  1 
ATOM   235  C  CG  . LEU A  1 31  ? 18.50200  -4.70900  11.94700 1.000 20.31403  ? 131 LEU A CG  1 
ATOM   236  C  CD1 . LEU A  1 31  ? 19.98900  -4.69000  11.58300 1.000 22.33305  ? 131 LEU A CD1 1 
ATOM   237  C  CD2 . LEU A  1 31  ? 17.86900  -3.37800  11.59800 1.000 24.37911  ? 131 LEU A CD2 1 
ATOM   238  N  N   . LEU A  1 32  ? 18.93200  -8.21000  13.54400 1.000 18.08947  ? 132 LEU A N   1 
ATOM   239  C  CA  . LEU A  1 32  ? 18.82300  -8.80100  14.87500 1.000 16.99796  ? 132 LEU A CA  1 
ATOM   240  C  C   . LEU A  1 32  ? 19.98700  -8.30200  15.72400 1.000 16.59048  ? 132 LEU A C   1 
ATOM   241  O  O   . LEU A  1 32  ? 21.14100  -8.63800  15.44900 1.000 19.69073  ? 132 LEU A O   1 
ATOM   242  C  CB  . LEU A  1 32  ? 18.83000  -10.32300 14.76000 1.000 19.41868  ? 132 LEU A CB  1 
ATOM   243  C  CG  . LEU A  1 32  ? 18.73800  -11.15100 16.04000 1.000 24.69222  ? 132 LEU A CG  1 
ATOM   244  C  CD1 . LEU A  1 32  ? 17.57000  -10.70000 16.83900 1.000 29.97997  ? 132 LEU A CD1 1 
ATOM   245  C  CD2 . LEU A  1 32  ? 18.60100  -12.61200 15.68000 1.000 23.43522  ? 132 LEU A CD2 1 
ATOM   246  N  N   . THR A  1 33  ? 19.68600  -7.48800  16.73500 1.000 16.28021  ? 133 THR A N   1 
ATOM   247  C  CA  . THR A  1 33  ? 20.69500  -6.90300  17.61300 1.000 16.90086  ? 133 THR A CA  1 
ATOM   248  C  C   . THR A  1 33  ? 20.63000  -7.59700  18.96600 1.000 17.94191  ? 133 THR A C   1 
ATOM   249  O  O   . THR A  1 33  ? 19.54300  -7.74300  19.54100 1.000 21.70550  ? 133 THR A O   1 
ATOM   250  C  CB  . THR A  1 33  ? 20.46300  -5.39700  17.77900 1.000 19.98213  ? 133 THR A CB  1 
ATOM   251  O  OG1 . THR A  1 33  ? 20.62600  -4.73300  16.51300 1.000 21.06023  ? 133 THR A OG1 1 
ATOM   252  C  CG2 . THR A  1 33  ? 21.43500  -4.80100  18.82500 1.000 19.56460  ? 133 THR A CG2 1 
ATOM   253  N  N   . ILE A  1 34  ? 21.78600  -8.02800  19.46900 1.000 18.59663  ? 134 ILE A N   1 
ATOM   254  C  CA  . ILE A  1 34  ? 21.87600  -8.71600  20.75400 1.000 20.51837  ? 134 ILE A CA  1 
ATOM   255  C  C   . ILE A  1 34  ? 22.58700  -7.79900  21.73900 1.000 23.06331  ? 134 ILE A C   1 
ATOM   256  O  O   . ILE A  1 34  ? 23.76700  -7.47400  21.55200 1.000 22.22249  ? 134 ILE A O   1 
ATOM   257  C  CB  . ILE A  1 34  ? 22.61400  -10.05600 20.60700 1.000 22.87432  ? 134 ILE A CB  1 
ATOM   258  C  CG1 . ILE A  1 34  ? 21.97500  -10.89200 19.48700 1.000 26.00266  ? 134 ILE A CG1 1 
ATOM   259  C  CG2 . ILE A  1 34  ? 22.66300  -10.80700 21.93600 1.000 26.27185  ? 134 ILE A CG2 1 
ATOM   260  C  CD1 . ILE A  1 34  ? 22.77900  -12.10000 19.10300 1.000 27.91627  ? 134 ILE A CD1 1 
ATOM   261  N  N   . GLU A  1 35  ? 21.87300  -7.39200  22.79300 1.000 19.94030  ? 135 GLU A N   1 
ATOM   262  C  CA  . GLU A  1 35  ? 22.45300  -6.52100  23.81500 1.000 24.72109  ? 135 GLU A CA  1 
ATOM   263  C  C   . GLU A  1 35  ? 23.58800  -7.22400  24.55200 1.000 27.95011  ? 135 GLU A C   1 
ATOM   264  O  O   . GLU A  1 35  ? 23.51000  -8.41900  24.83700 1.000 28.58977  ? 135 GLU A O   1 
ATOM   265  C  CB  . GLU A  1 35  ? 21.37200  -6.10300  24.81700 1.000 26.14772  ? 135 GLU A CB  1 
ATOM   266  C  CG  . GLU A  1 35  ? 21.77100  -4.93400  25.69800 1.000 27.15079  ? 135 GLU A CG  1 
ATOM   267  C  CD  . GLU A  1 35  ? 20.75400  -4.65600  26.79800 1.000 42.02284  ? 135 GLU A CD  1 
ATOM   268  O  OE1 . GLU A  1 35  ? 20.68200  -5.45700  27.75500 1.000 41.14880  ? 135 GLU A OE1 1 
ATOM   269  O  OE2 . GLU A  1 35  ? 20.03100  -3.63900  26.69500 1.000 38.89641  ? 135 GLU A OE2 1 
ATOM   270  N  N   . ARG A  1 36  ? 24.65300  -6.47000  24.85800 1.000 26.83765  ? 136 ARG A N   1 
ATOM   271  C  CA  . ARG A  1 36  ? 25.77300  -6.98900  25.63900 1.000 30.49825  ? 136 ARG A CA  1 
ATOM   272  C  C   . ARG A  1 36  ? 25.82000  -6.16100  26.91200 1.000 33.27230  ? 136 ARG A C   1 
ATOM   273  O  O   . ARG A  1 36  ? 24.85000  -6.16300  27.66200 1.000 32.35949  ? 136 ARG A O   1 
ATOM   274  C  CB  . ARG A  1 36  ? 27.06500  -6.98800  24.83200 1.000 32.35277  ? 136 ARG A CB  1 
ATOM   275  C  CG  . ARG A  1 36  ? 28.25200  -7.71800  25.49900 1.000 41.09716  ? 136 ARG A CG  1 
ATOM   276  C  CD  . ARG A  1 36  ? 29.53300  -7.58700  24.66500 1.000 51.58638  ? 136 ARG A CD  1 
ATOM   277  N  NE  . ARG A  1 36  ? 30.67100  -8.26500  25.27700 1.000 66.81561  ? 136 ARG A NE  1 
ATOM   278  C  CZ  . ARG A  1 36  ? 30.86700  -9.57700  25.24800 1.000 63.56900  ? 136 ARG A CZ  1 
ATOM   279  N  NH1 . ARG A  1 36  ? 30.00900  -10.39200 24.65300 1.000 60.62300  ? 136 ARG A NH1 1 
ATOM   280  N  NH2 . ARG A  1 36  ? 31.94900  -10.08500 25.83400 1.000 53.23697  ? 136 ARG A NH2 1 
ATOM   281  N  N   . ASP A  1 37  ? 26.91200  -5.43400  27.16500 1.000 29.90463  ? 137 ASP A N   1 
ATOM   282  C  CA  . ASP A  1 37  ? 27.03400  -4.70000  28.41900 1.000 33.91216  ? 137 ASP A CA  1 
ATOM   283  C  C   . ASP A  1 37  ? 26.42800  -3.30800  28.35100 1.000 37.78122  ? 137 ASP A C   1 
ATOM   284  O  O   . ASP A  1 37  ? 26.01300  -2.77300  29.38500 1.000 35.88452  ? 137 ASP A O   1 
ATOM   285  C  CB  . ASP A  1 37  ? 28.50400  -4.60900  28.83300 1.000 34.43806  ? 137 ASP A CB  1 
ATOM   286  C  CG  . ASP A  1 37  ? 29.06000  -5.94400  29.28400 1.000 45.14410  ? 137 ASP A CG  1 
ATOM   287  O  OD1 . ASP A  1 37  ? 28.32400  -6.68600  29.96700 1.000 53.47499  ? 137 ASP A OD1 1 
ATOM   288  O  OD2 . ASP A  1 37  ? 30.22400  -6.25000  28.94700 1.000 60.66555  ? 137 ASP A OD2 1 
ATOM   289  N  N   . THR A  1 38  ? 26.36000  -2.71000  27.16400 1.000 30.40314  ? 138 THR A N   1 
ATOM   290  C  CA  . THR A  1 38  ? 25.75400  -1.39200  27.01900 1.000 34.83537  ? 138 THR A CA  1 
ATOM   291  C  C   . THR A  1 38  ? 24.24300  -1.56100  26.95000 1.000 35.12091  ? 138 THR A C   1 
ATOM   292  O  O   . THR A  1 38  ? 23.74300  -2.28800  26.09000 1.000 33.92645  ? 138 THR A O   1 
ATOM   293  C  CB  . THR A  1 38  ? 26.28000  -0.68800  25.76700 1.000 36.25527  ? 138 THR A CB  1 
ATOM   294  O  OG1 . THR A  1 38  ? 27.71000  -0.74800  25.75300 1.000 41.84623  ? 138 THR A OG1 1 
ATOM   295  C  CG2 . THR A  1 38  ? 25.84900  0.78700   25.75700 1.000 32.63019  ? 138 THR A CG2 1 
ATOM   296  N  N   . GLY A  1 39  ? 23.51600  -0.92000  27.86600 1.000 32.98044  ? 139 GLY A N   1 
ATOM   297  C  CA  . GLY A  1 39  ? 22.06700  -1.05200  27.86300 1.000 31.56191  ? 139 GLY A CA  1 
ATOM   298  C  C   . GLY A  1 39  ? 21.45100  -0.43700  26.61800 1.000 36.69782  ? 139 GLY A C   1 
ATOM   299  O  O   . GLY A  1 39  ? 21.87300  0.61800   26.14000 1.000 35.85153  ? 139 GLY A O   1 
ATOM   300  N  N   . MET A  1 40  ? 20.43300  -1.10600  26.08900 1.000 36.21762  ? 140 MET A N   1 
ATOM   301  C  CA  . MET A  1 40  ? 19.78100  -0.65300  24.87100 1.000 39.11680  ? 140 MET A CA  1 
ATOM   302  C  C   . MET A  1 40  ? 18.30600  -0.36600  25.08400 1.000 34.32213  ? 140 MET A C   1 
ATOM   303  O  O   . MET A  1 40  ? 17.52500  -0.38900  24.13200 1.000 32.81198  ? 140 MET A O   1 
ATOM   304  C  CB  . MET A  1 40  ? 19.97400  -1.67700  23.76300 1.000 38.38224  ? 140 MET A CB  1 
ATOM   305  C  CG  . MET A  1 40  ? 21.42600  -1.79700  23.44000 1.000 48.45323  ? 140 MET A CG  1 
ATOM   306  S  SD  . MET A  1 40  ? 21.69500  -2.44300  21.81800 1.000 39.74484  ? 140 MET A SD  1 
ATOM   307  C  CE  . MET A  1 40  ? 20.20800  -1.91300  20.97300 1.000 25.44213  ? 140 MET A CE  1 
ATOM   308  N  N   . GLY A  1 41  ? 17.92600  -0.06600  26.32600 1.000 31.84663  ? 141 GLY A N   1 
ATOM   309  C  CA  . GLY A  1 41  ? 16.52800  0.17800   26.63200 1.000 34.77904  ? 141 GLY A CA  1 
ATOM   310  C  C   . GLY A  1 41  ? 15.92300  1.31500   25.83200 1.000 32.47907  ? 141 GLY A C   1 
ATOM   311  O  O   . GLY A  1 41  ? 14.74500  1.26300   25.47200 1.000 35.97790  ? 141 GLY A O   1 
ATOM   312  N  N   . ASP A  1 42  ? 16.71600  2.35000   25.53400 1.000 33.64764  ? 142 ASP A N   1 
ATOM   313  C  CA  . ASP A  1 42  ? 16.19600  3.46800   24.75200 1.000 36.74352  ? 142 ASP A CA  1 
ATOM   314  C  C   . ASP A  1 42  ? 15.77600  3.02900   23.35600 1.000 32.71624  ? 142 ASP A C   1 
ATOM   315  O  O   . ASP A  1 42  ? 14.80400  3.56100   22.80400 1.000 33.48265  ? 142 ASP A O   1 
ATOM   316  C  CB  . ASP A  1 42  ? 17.23300  4.58700   24.65500 1.000 38.56763  ? 142 ASP A CB  1 
ATOM   317  C  CG  . ASP A  1 42  ? 17.46300  5.28900   25.98100 1.000 48.02791  ? 142 ASP A CG  1 
ATOM   318  O  OD1 . ASP A  1 42  ? 16.53000  5.31900   26.80800 1.000 51.93395  ? 142 ASP A OD1 1 
ATOM   319  O  OD2 . ASP A  1 42  ? 18.57700  5.81000   26.19000 1.000 50.29768  ? 142 ASP A OD2 1 
ATOM   320  N  N   . TYR A  1 43  ? 16.49000  2.07200   22.76600 1.000 27.15361  ? 143 TYR A N   1 
ATOM   321  C  CA  . TYR A  1 43  ? 16.09900  1.56700   21.45200 1.000 26.86844  ? 143 TYR A CA  1 
ATOM   322  C  C   . TYR A  1 43  ? 15.02700  0.49300   21.54400 1.000 24.60841  ? 143 TYR A C   1 
ATOM   323  O  O   . TYR A  1 43  ? 14.15300  0.42200   20.66600 1.000 27.55444  ? 143 TYR A O   1 
ATOM   324  C  CB  . TYR A  1 43  ? 17.31600  1.02700   20.70000 1.000 30.86377  ? 143 TYR A CB  1 
ATOM   325  C  CG  . TYR A  1 43  ? 18.38900  2.07700   20.59500 1.000 33.70581  ? 143 TYR A CG  1 
ATOM   326  C  CD1 . TYR A  1 43  ? 18.28600  3.10800   19.67600 1.000 35.43212  ? 143 TYR A CD1 1 
ATOM   327  C  CD2 . TYR A  1 43  ? 19.46600  2.07600   21.46800 1.000 35.57606  ? 143 TYR A CD2 1 
ATOM   328  C  CE1 . TYR A  1 43  ? 19.25600  4.09400   19.60200 1.000 42.11410  ? 143 TYR A CE1 1 
ATOM   329  C  CE2 . TYR A  1 43  ? 20.43300  3.05300   21.40400 1.000 38.19937  ? 143 TYR A CE2 1 
ATOM   330  C  CZ  . TYR A  1 43  ? 20.32500  4.06000   20.46900 1.000 38.68374  ? 143 TYR A CZ  1 
ATOM   331  O  OH  . TYR A  1 43  ? 21.30000  5.03400   20.41100 1.000 46.51401  ? 143 TYR A OH  1 
ATOM   332  N  N   . ILE A  1 44  ? 15.08100  -0.34700  22.57800 1.000 26.94163  ? 144 ILE A N   1 
ATOM   333  C  CA  . ILE A  1 44  ? 14.01800  -1.32200  22.80800 1.000 28.04737  ? 144 ILE A CA  1 
ATOM   334  C  C   . ILE A  1 44  ? 12.66900  -0.62000  22.91700 1.000 26.45494  ? 144 ILE A C   1 
ATOM   335  O  O   . ILE A  1 44  ? 11.65200  -1.10800  22.40800 1.000 25.03089  ? 144 ILE A O   1 
ATOM   336  C  CB  . ILE A  1 44  ? 14.32900  -2.16000  24.06200 1.000 29.64155  ? 144 ILE A CB  1 
ATOM   337  C  CG1 . ILE A  1 44  ? 15.56400  -3.03100  23.82800 1.000 27.83398  ? 144 ILE A CG1 1 
ATOM   338  C  CG2 . ILE A  1 44  ? 13.13100  -3.02000  24.45200 1.000 30.31287  ? 144 ILE A CG2 1 
ATOM   339  C  CD1 . ILE A  1 44  ? 16.02800  -3.81200  25.07800 1.000 27.67268  ? 144 ILE A CD1 1 
ATOM   340  N  N   . GLU A  1 45  ? 12.64800  0.55600   23.54400 1.000 29.03177  ? 145 GLU A N   1 
ATOM   341  C  CA  . GLU A  1 45  ? 11.39200  1.27000   23.75600 1.000 27.43782  ? 145 GLU A CA  1 
ATOM   342  C  C   . GLU A  1 45  ? 10.77800  1.79300   22.46200 1.000 30.86510  ? 145 GLU A C   1 
ATOM   343  O  O   . GLU A  1 45  ? 9.58700   2.11900   22.45400 1.000 35.80971  ? 145 GLU A O   1 
ATOM   344  C  CB  . GLU A  1 45  ? 11.61400  2.42700   24.73400 1.000 30.56295  ? 145 GLU A CB  1 
ATOM   345  C  CG  . GLU A  1 45  ? 11.65000  2.00000   26.19300 1.000 48.46408  ? 145 GLU A CG  1 
ATOM   346  C  CD  . GLU A  1 45  ? 12.06800  3.13200   27.12200 1.000 72.30239  ? 145 GLU A CD  1 
ATOM   347  O  OE1 . GLU A  1 45  ? 12.06800  4.30300   26.67700 1.000 64.66328  ? 145 GLU A OE1 1 
ATOM   348  O  OE2 . GLU A  1 45  ? 12.40900  2.84900   28.29400 1.000 70.77368  ? 145 GLU A OE2 1 
ATOM   349  N  N   . THR A  1 46  ? 11.53700  1.86000   21.36400 1.000 27.25627  ? 146 THR A N   1 
ATOM   350  C  CA  . THR A  1 46  ? 10.97800  2.36700   20.11400 1.000 26.78327  ? 146 THR A CA  1 
ATOM   351  C  C   . THR A  1 46  ? 10.18300  1.32600   19.33200 1.000 27.66583  ? 146 THR A C   1 
ATOM   352  O  O   . THR A  1 46  ? 9.50300   1.69500   18.37000 1.000 34.24100  ? 146 THR A O   1 
ATOM   353  C  CB  . THR A  1 46  ? 12.07700  2.91300   19.19800 1.000 29.76777  ? 146 THR A CB  1 
ATOM   354  O  OG1 . THR A  1 46  ? 12.89800  1.83100   18.74300 1.000 28.31248  ? 146 THR A OG1 1 
ATOM   355  C  CG2 . THR A  1 46  ? 12.93800  3.91300   19.94100 1.000 29.66798  ? 146 THR A CG2 1 
ATOM   356  N  N   . GLY A  1 47  ? 10.25800  0.04600   19.70000 1.000 28.18890  ? 147 GLY A N   1 
ATOM   357  C  CA  . GLY A  1 47  ? 9.60900   -1.01200  18.96500 1.000 26.47633  ? 147 GLY A CA  1 
ATOM   358  C  C   . GLY A  1 47  ? 8.36900   -1.54300  19.66100 1.000 25.23189  ? 147 GLY A C   1 
ATOM   359  O  O   . GLY A  1 47  ? 7.84200   -0.95300  20.60700 1.000 29.46150  ? 147 GLY A O   1 
ATOM   360  N  N   . ILE A  1 48  ? 7.90400   -2.68600  19.17200 1.000 24.21716  ? 148 ILE A N   1 
ATOM   361  C  CA  . ILE A  1 48  ? 6.74900   -3.37400  19.74000 1.000 24.61956  ? 148 ILE A CA  1 
ATOM   362  C  C   . ILE A  1 48  ? 7.25600   -4.30700  20.83800 1.000 20.86670  ? 148 ILE A C   1 
ATOM   363  O  O   . ILE A  1 48  ? 8.05700   -5.20600  20.53900 1.000 23.26676  ? 148 ILE A O   1 
ATOM   364  C  CB  . ILE A  1 48  ? 5.99300   -4.17200  18.67200 1.000 25.15660  ? 148 ILE A CB  1 
ATOM   365  C  CG1 . ILE A  1 48  ? 5.52300   -3.27300  17.51700 1.000 32.80115  ? 148 ILE A CG1 1 
ATOM   366  C  CG2 . ILE A  1 48  ? 4.82900   -4.94300  19.31200 1.000 25.30800  ? 148 ILE A CG2 1 
ATOM   367  C  CD1 . ILE A  1 48  ? 4.52700   -2.19700  17.91100 1.000 31.17183  ? 148 ILE A CD1 1 
ATOM   368  N  N   . PRO A  1 49  ? 6.80100   -4.15800  22.08600 1.000 23.31908  ? 149 PRO A N   1 
ATOM   369  C  CA  . PRO A  1 49  ? 7.26400   -5.05000  23.16300 1.000 29.29136  ? 149 PRO A CA  1 
ATOM   370  C  C   . PRO A  1 49  ? 6.82900   -6.49100  22.93200 1.000 26.00574  ? 149 PRO A C   1 
ATOM   371  O  O   . PRO A  1 49  ? 5.65700   -6.76600  22.65900 1.000 25.38693  ? 149 PRO A O   1 
ATOM   372  C  CB  . PRO A  1 49  ? 6.60300   -4.46800  24.42200 1.000 26.09555  ? 149 PRO A CB  1 
ATOM   373  C  CG  . PRO A  1 49  ? 6.18500   -3.07500  24.04100 1.000 32.74223  ? 149 PRO A CG  1 
ATOM   374  C  CD  . PRO A  1 49  ? 5.89800   -3.10400  22.57500 1.000 24.70227  ? 149 PRO A CD  1 
ATOM   375  N  N   . LEU A  1 50  ? 7.78100   -7.41400  23.05800 1.000 22.13909  ? 150 LEU A N   1 
ATOM   376  C  CA  . LEU A  1 50  ? 7.49700   -8.84500  22.99000 1.000 19.31037  ? 150 LEU A CA  1 
ATOM   377  C  C   . LEU A  1 50  ? 7.85300   -9.57200  24.27400 1.000 22.91684  ? 150 LEU A C   1 
ATOM   378  O  O   . LEU A  1 50  ? 7.03500   -10.34400 24.78800 1.000 22.17424  ? 150 LEU A O   1 
ATOM   379  C  CB  . LEU A  1 50  ? 8.25200   -9.49600  21.81600 1.000 20.04543  ? 150 LEU A CB  1 
ATOM   380  C  CG  . LEU A  1 50  ? 7.48800   -9.61400  20.50000 1.000 26.96591  ? 150 LEU A CG  1 
ATOM   381  C  CD1 . LEU A  1 50  ? 7.37400   -8.25500  19.86700 1.000 26.93884  ? 150 LEU A CD1 1 
ATOM   382  C  CD2 . LEU A  1 50  ? 8.20100   -10.59600 19.54800 1.000 29.36780  ? 150 LEU A CD2 1 
ATOM   383  N  N   . ASN A  1 51  ? 9.05500   -9.34400  24.80100 1.000 24.34646  ? 151 ASN A N   1 
ATOM   384  C  CA  . ASN A  1 51  ? 9.60100   -10.09900 25.92400 1.000 22.04753  ? 151 ASN A CA  1 
ATOM   385  C  C   . ASN A  1 51  ? 9.32600   -11.59200 25.76500 1.000 24.33462  ? 151 ASN A C   1 
ATOM   386  O  O   . ASN A  1 51  ? 8.79800   -12.25600 26.65900 1.000 24.65516  ? 151 ASN A O   1 
ATOM   387  C  CB  . ASN A  1 51  ? 9.06000   -9.56600  27.25300 1.000 25.63388  ? 151 ASN A CB  1 
ATOM   388  C  CG  . ASN A  1 51  ? 9.64300   -8.21400  27.61600 1.000 42.92367  ? 151 ASN A CG  1 
ATOM   389  O  OD1 . ASN A  1 51  ? 10.13600  -7.48300  26.76200 1.000 43.61846  ? 151 ASN A OD1 1 
ATOM   390  N  ND2 . ASN A  1 51  ? 9.60100   -7.88200  28.90000 1.000 66.21105  ? 151 ASN A ND2 1 
ATOM   391  N  N   . ALA A  1 52  ? 9.70500   -12.12400 24.60700 1.000 21.16025  ? 152 ALA A N   1 
ATOM   392  C  CA  . ALA A  1 52  ? 9.31900   -13.46100 24.17800 1.000 21.96843  ? 152 ALA A CA  1 
ATOM   393  C  C   . ALA A  1 52  ? 10.49200  -14.42600 24.29100 1.000 23.84257  ? 152 ALA A C   1 
ATOM   394  O  O   . ALA A  1 52  ? 11.65100  -14.03600 24.11800 1.000 22.59473  ? 152 ALA A O   1 
ATOM   395  C  CB  . ALA A  1 52  ? 8.81500   -13.45000 22.72700 1.000 21.47628  ? 152 ALA A CB  1 
ATOM   396  N  N   . LYS A  1 53  ? 10.17800  -15.69200 24.58000 1.000 19.96007  ? 153 LYS A N   1 
ATOM   397  C  CA  . LYS A  1 53  ? 11.17800  -16.75100 24.49900 1.000 21.86352  ? 153 LYS A CA  1 
ATOM   398  C  C   . LYS A  1 53  ? 11.74400  -16.82200 23.08800 1.000 28.18853  ? 153 LYS A C   1 
ATOM   399  O  O   . LYS A  1 53  ? 11.01900  -16.63700 22.10800 1.000 24.79656  ? 153 LYS A O   1 
ATOM   400  C  CB  . LYS A  1 53  ? 10.56400  -18.10200 24.87000 1.000 25.25001  ? 153 LYS A CB  1 
ATOM   401  C  CG  . LYS A  1 53  ? 11.58400  -19.24000 24.98000 1.000 48.73890  ? 153 LYS A CG  1 
ATOM   402  C  CD  . LYS A  1 53  ? 10.95900  -20.54900 25.46200 1.000 53.80892  ? 153 LYS A CD  1 
ATOM   403  C  CE  . LYS A  1 53  ? 11.96700  -21.69500 25.39800 1.000 57.18934  ? 153 LYS A CE  1 
ATOM   404  N  NZ  . LYS A  1 53  ? 11.37700  -22.99800 25.81200 1.000 60.94298  ? 153 LYS A NZ  1 
ATOM   405  N  N   . VAL A  1 54  ? 13.04300  -17.10100 22.98300 1.000 20.12616  ? 154 VAL A N   1 
ATOM   406  C  CA  . VAL A  1 54  ? 13.67500  -17.22100 21.66600 1.000 22.16649  ? 154 VAL A CA  1 
ATOM   407  C  C   . VAL A  1 54  ? 13.31800  -18.57500 21.07300 1.000 23.66381  ? 154 VAL A C   1 
ATOM   408  O  O   . VAL A  1 54  ? 13.41100  -19.60100 21.75100 1.000 26.14311  ? 154 VAL A O   1 
ATOM   409  C  CB  . VAL A  1 54  ? 15.20400  -17.06400 21.76900 1.000 25.83599  ? 154 VAL A CB  1 
ATOM   410  C  CG1 . VAL A  1 54  ? 15.83800  -17.19400 20.39400 1.000 29.09651  ? 154 VAL A CG1 1 
ATOM   411  C  CG2 . VAL A  1 54  ? 15.58400  -15.72300 22.37400 1.000 26.19239  ? 154 VAL A CG2 1 
ATOM   412  N  N   . SER A  1 55  ? 12.90700  -18.58100 19.80300 1.000 22.26196  ? 155 SER A N   1 
ATOM   413  C  CA  . SER A  1 55  ? 12.83200  -19.80700 19.02300 1.000 21.86752  ? 155 SER A CA  1 
ATOM   414  C  C   . SER A  1 55  ? 13.14600  -19.46200 17.57900 1.000 20.94840  ? 155 SER A C   1 
ATOM   415  O  O   . SER A  1 55  ? 12.96700  -18.32000 17.15300 1.000 18.89447  ? 155 SER A O   1 
ATOM   416  C  CB  . SER A  1 55  ? 11.46000  -20.48700 19.08500 1.000 22.86105  ? 155 SER A CB  1 
ATOM   417  O  OG  . SER A  1 55  ? 10.44000  -19.63000 18.59500 1.000 21.16286  ? 155 SER A OG  1 
ATOM   418  N  N   . SER A  1 56  ? 13.60300  -20.46200 16.82400 1.000 18.44671  ? 156 SER A N   1 
ATOM   419  C  CA  . SER A  1 56  ? 13.85500  -20.20100 15.41600 1.000 21.02075  ? 156 SER A CA  1 
ATOM   420  C  C   . SER A  1 56  ? 12.54800  -19.87500 14.71300 1.000 20.78586  ? 156 SER A C   1 
ATOM   421  O  O   . SER A  1 56  ? 12.49900  -18.96800 13.87500 1.000 20.00329  ? 156 SER A O   1 
ATOM   422  C  CB  . SER A  1 56  ? 14.56500  -21.38600 14.76300 1.000 24.88270  ? 156 SER A CB  1 
ATOM   423  O  OG  . SER A  1 56  ? 13.75300  -22.53500 14.76400 1.000 28.35791  ? 156 SER A OG  1 
ATOM   424  N  N   . GLU A  1 57  ? 11.46300  -20.53600 15.12700 1.000 21.14562  ? 157 GLU A N   1 
ATOM   425  C  CA  . GLU A  1 57  ? 10.15000  -20.30900 14.52200 1.000 23.16459  ? 157 GLU A CA  1 
ATOM   426  C  C   . GLU A  1 57  ? 9.67900   -18.86700 14.71400 1.000 23.35660  ? 157 GLU A C   1 
ATOM   427  O  O   . GLU A  1 57  ? 9.24000   -18.22000 13.75500 1.000 21.66646  ? 157 GLU A O   1 
ATOM   428  C  CB  . GLU A  1 57  ? 9.13300   -21.29500 15.10300 1.000 21.87366  ? 157 GLU A CB  1 
ATOM   429  C  CG  . GLU A  1 57  ? 9.36000   -22.75700 14.70800 1.000 22.66635  ? 157 GLU A CG  1 
ATOM   430  C  CD  . GLU A  1 57  ? 10.25500  -23.51200 15.67200 1.000 27.62530  ? 157 GLU A CD  1 
ATOM   431  O  OE1 . GLU A  1 57  ? 10.86700  -22.87300 16.55600 1.000 27.74499  ? 157 GLU A OE1 1 
ATOM   432  O  OE2 . GLU A  1 57  ? 10.35200  -24.75200 15.53800 1.000 29.28364  ? 157 GLU A OE2 1 
ATOM   433  N  N   . LEU A  1 58  ? 9.75100   -18.34000 15.94800 1.000 20.24799  ? 158 LEU A N   1 
ATOM   434  C  CA  . LEU A  1 58  ? 9.32600   -16.95700 16.15800 1.000 16.90336  ? 158 LEU A CA  1 
ATOM   435  C  C   . LEU A  1 58  ? 10.21000  -15.97300 15.39600 1.000 19.76550  ? 158 LEU A C   1 
ATOM   436  O  O   . LEU A  1 58  ? 9.70800   -15.00300 14.82100 1.000 18.44901  ? 158 LEU A O   1 
ATOM   437  C  CB  . LEU A  1 58  ? 9.31400   -16.59700 17.65200 1.000 17.62239  ? 158 LEU A CB  1 
ATOM   438  C  CG  . LEU A  1 58  ? 8.94200   -15.13700 17.96400 1.000 18.85726  ? 158 LEU A CG  1 
ATOM   439  C  CD1 . LEU A  1 58  ? 7.55200   -14.79000 17.41800 1.000 22.68248  ? 158 LEU A CD1 1 
ATOM   440  C  CD2 . LEU A  1 58  ? 8.98800   -14.87900 19.47500 1.000 21.90311  ? 158 LEU A CD2 1 
ATOM   441  N  N   . LEU A  1 59  ? 11.53100  -16.17200 15.41800 1.000 18.38191  ? 159 LEU A N   1 
ATOM   442  C  CA  . LEU A  1 59  ? 12.40600  -15.27400 14.67500 1.000 16.71480  ? 159 LEU A CA  1 
ATOM   443  C  C   . LEU A  1 59  ? 12.03000  -15.24600 13.19200 1.000 20.20069  ? 159 LEU A C   1 
ATOM   444  O  O   . LEU A  1 59  ? 11.93100  -14.17100 12.58700 1.000 20.48422  ? 159 LEU A O   1 
ATOM   445  C  CB  . LEU A  1 59  ? 13.86100  -15.69300 14.86400 1.000 18.64735  ? 159 LEU A CB  1 
ATOM   446  C  CG  . LEU A  1 59  ? 14.47200  -15.31900 16.21100 1.000 21.23940  ? 159 LEU A CG  1 
ATOM   447  C  CD1 . LEU A  1 59  ? 15.85800  -15.94600 16.35600 1.000 21.07512  ? 159 LEU A CD1 1 
ATOM   448  C  CD2 . LEU A  1 59  ? 14.53800  -13.80400 16.38400 1.000 17.50908  ? 159 LEU A CD2 1 
ATOM   449  N  N   . ILE A  1 60  ? 11.78600  -16.41300 12.60100 1.000 20.45279  ? 160 ILE A N   1 
ATOM   450  C  CA  . ILE A  1 60  ? 11.36000  -16.45400 11.20000 1.000 20.52324  ? 160 ILE A CA  1 
ATOM   451  C  C   . ILE A  1 60  ? 10.03200  -15.72500 11.01500 1.000 24.65844  ? 160 ILE A C   1 
ATOM   452  O  O   . ILE A  1 60  ? 9.88900   -14.89800 10.10800 1.000 24.17443  ? 160 ILE A O   1 
ATOM   453  C  CB  . ILE A  1 60  ? 11.28900  -17.90800 10.70400 1.000 19.44459  ? 160 ILE A CB  1 
ATOM   454  C  CG1 . ILE A  1 60  ? 12.70200  -18.50100 10.62300 1.000 21.78518  ? 160 ILE A CG1 1 
ATOM   455  C  CG2 . ILE A  1 60  ? 10.60500  -17.97600 9.33600  1.000 22.19632  ? 160 ILE A CG2 1 
ATOM   456  C  CD1 . ILE A  1 60  ? 12.70600  -20.00700 10.46100 1.000 24.92631  ? 160 ILE A CD1 1 
ATOM   457  N  N   . ASN A  1 61  ? 9.04100   -16.01300 11.86800 1.000 21.26641  ? 161 ASN A N   1 
ATOM   458  C  CA  . ASN A  1 61  ? 7.72800   -15.38700 11.69100 1.000 20.01337  ? 161 ASN A CA  1 
ATOM   459  C  C   . ASN A  1 61  ? 7.79400   -13.86400 11.80400 1.000 24.09573  ? 161 ASN A C   1 
ATOM   460  O  O   . ASN A  1 61  ? 7.04500   -13.15800 11.11600 1.000 23.90671  ? 161 ASN A O   1 
ATOM   461  C  CB  . ASN A  1 61  ? 6.72600   -15.96800 12.69800 1.000 18.83636  ? 161 ASN A CB  1 
ATOM   462  C  CG  . ASN A  1 61  ? 5.90200   -17.09600 12.10200 1.000 21.37158  ? 161 ASN A CG  1 
ATOM   463  O  OD1 . ASN A  1 61  ? 6.34800   -18.24600 11.99600 1.000 22.14935  ? 161 ASN A OD1 1 
ATOM   464  N  ND2 . ASN A  1 61  ? 4.68200   -16.76800 11.70900 1.000 19.80684  ? 161 ASN A ND2 1 
ATOM   465  N  N   . ILE A  1 62  ? 8.70300   -13.33600 12.63000 1.000 19.56811  ? 162 ILE A N   1 
ATOM   466  C  CA  . ILE A  1 62  ? 8.81700   -11.88400 12.77000 1.000 18.09571  ? 162 ILE A CA  1 
ATOM   467  C  C   . ILE A  1 62  ? 9.23500   -11.23100 11.45300 1.000 21.05618  ? 162 ILE A C   1 
ATOM   468  O  O   . ILE A  1 62  ? 8.75100   -10.14800 11.09900 1.000 19.95823  ? 162 ILE A O   1 
ATOM   469  C  CB  . ILE A  1 62  ? 9.81000   -11.53700 13.89500 1.000 17.08586  ? 162 ILE A CB  1 
ATOM   470  C  CG1 . ILE A  1 62  ? 9.19700   -11.86000 15.26300 1.000 18.27936  ? 162 ILE A CG1 1 
ATOM   471  C  CG2 . ILE A  1 62  ? 10.23600  -10.06200 13.80500 1.000 22.81206  ? 162 ILE A CG2 1 
ATOM   472  C  CD1 . ILE A  1 62  ? 10.23400  -11.78000 16.42900 1.000 17.19285  ? 162 ILE A CD1 1 
ATOM   473  N  N   . PHE A  1 63  ? 10.15300  -11.85000 10.72400 1.000 19.94389  ? 163 PHE A N   1 
ATOM   474  C  CA  . PHE A  1 63  ? 10.78000  -11.17000 9.59500  1.000 20.56594  ? 163 PHE A CA  1 
ATOM   475  C  C   . PHE A  1 63  ? 10.11700  -11.45000 8.25300  1.000 26.07836  ? 163 PHE A C   1 
ATOM   476  O  O   . PHE A  1 63  ? 10.62200  -10.98400 7.22200  1.000 26.67518  ? 163 PHE A O   1 
ATOM   477  C  CB  . PHE A  1 63  ? 12.26300  -11.53400 9.51500  1.000 18.60569  ? 163 PHE A CB  1 
ATOM   478  C  CG  . PHE A  1 63  ? 13.08800  -10.88700 10.59000 1.000 19.73236  ? 163 PHE A CG  1 
ATOM   479  C  CD1 . PHE A  1 63  ? 13.23200  -9.51000  10.63500 1.000 22.21917  ? 163 PHE A CD1 1 
ATOM   480  C  CD2 . PHE A  1 63  ? 13.72000  -11.66000 11.55000 1.000 20.53076  ? 163 PHE A CD2 1 
ATOM   481  C  CE1 . PHE A  1 63  ? 14.00200  -8.91000  11.63900 1.000 19.40368  ? 163 PHE A CE1 1 
ATOM   482  C  CE2 . PHE A  1 63  ? 14.50100  -11.07600 12.54000 1.000 21.00751  ? 163 PHE A CE2 1 
ATOM   483  C  CZ  . PHE A  1 63  ? 14.64300  -9.70600  12.58400 1.000 23.77928  ? 163 PHE A CZ  1 
ATOM   484  N  N   . ILE A  1 64  ? 9.00500   -12.17700 8.23500  1.000 21.33341  ? 164 ILE A N   1 
ATOM   485  C  CA  . ILE A  1 64  ? 8.33800   -12.42800 6.95200  1.000 22.43202  ? 164 ILE A CA  1 
ATOM   486  C  C   . ILE A  1 64  ? 8.01800   -11.09900 6.27300  1.000 22.69822  ? 164 ILE A C   1 
ATOM   487  O  O   . ILE A  1 64  ? 7.50600   -10.17000 6.92500  1.000 24.62936  ? 164 ILE A O   1 
ATOM   488  C  CB  . ILE A  1 64  ? 7.06600   -13.25900 7.16600  1.000 26.24473  ? 164 ILE A CB  1 
ATOM   489  C  CG1 . ILE A  1 64  ? 7.42500   -14.64700 7.71800  1.000 24.05280  ? 164 ILE A CG1 1 
ATOM   490  C  CG2 . ILE A  1 64  ? 6.27800   -13.36900 5.84600  1.000 25.70165  ? 164 ILE A CG2 1 
ATOM   491  C  CD1 . ILE A  1 64  ? 8.38000   -15.45200 6.80300  1.000 28.10786  ? 164 ILE A CD1 1 
ATOM   492  N  N   . PRO A  1 65  ? 8.30500   -10.94500 4.97600  1.000 26.60307  ? 165 PRO A N   1 
ATOM   493  C  CA  . PRO A  1 65  ? 8.06700   -9.65600  4.31200  1.000 25.96037  ? 165 PRO A CA  1 
ATOM   494  C  C   . PRO A  1 65  ? 6.59700   -9.26100  4.33400  1.000 24.60127  ? 165 PRO A C   1 
ATOM   495  O  O   . PRO A  1 65  ? 5.70100   -10.11200 4.32600  1.000 25.32361  ? 165 PRO A O   1 
ATOM   496  C  CB  . PRO A  1 65  ? 8.54700   -9.89800  2.87300  1.000 26.81978  ? 165 PRO A CB  1 
ATOM   497  C  CG  . PRO A  1 65  ? 9.43100   -11.08600 2.93400  1.000 34.04695  ? 165 PRO A CG  1 
ATOM   498  C  CD  . PRO A  1 65  ? 9.01900   -11.90900 4.12800  1.000 27.23915  ? 165 PRO A CD  1 
ATOM   499  N  N   . ASN A  1 66  ? 6.37100   -7.94200  4.35400  1.000 26.95415  ? 166 ASN A N   1 
ATOM   500  C  CA  . ASN A  1 66  ? 5.04000   -7.34700  4.22300  1.000 33.21752  ? 166 ASN A CA  1 
ATOM   501  C  C   . ASN A  1 66  ? 4.14200   -7.73400  5.39500  1.000 31.11293  ? 166 ASN A C   1 
ATOM   502  O  O   . ASN A  1 66  ? 2.94300   -7.96300  5.23300  1.000 35.86310  ? 166 ASN A O   1 
ATOM   503  C  CB  . ASN A  1 66  ? 4.39400   -7.72800  2.89200  1.000 32.34566  ? 166 ASN A CB  1 
ATOM   504  C  CG  . ASN A  1 66  ? 3.40300   -6.68300  2.40700  1.000 40.72949  ? 166 ASN A CG  1 
ATOM   505  O  OD1 . ASN A  1 66  ? 3.59200   -5.48600  2.63400  1.000 53.60595  ? 166 ASN A OD1 1 
ATOM   506  N  ND2 . ASN A  1 66  ? 2.35000   -7.12800  1.72500  1.000 46.24516  ? 166 ASN A ND2 1 
ATOM   507  N  N   . THR A  1 67  ? 4.73800   -7.82200  6.58000  1.000 23.51338  ? 167 THR A N   1 
ATOM   508  C  CA  . THR A  1 67  ? 4.04400   -8.08900  7.82600  1.000 22.25774  ? 167 THR A CA  1 
ATOM   509  C  C   . THR A  1 67  ? 4.29400   -6.94900  8.80700  1.000 25.30142  ? 167 THR A C   1 
ATOM   510  O  O   . THR A  1 67  ? 5.24800   -6.17300  8.64600  1.000 25.99708  ? 167 THR A O   1 
ATOM   511  C  CB  . THR A  1 67  ? 4.51600   -9.41100  8.44700  1.000 24.72313  ? 167 THR A CB  1 
ATOM   512  O  OG1 . THR A  1 67  ? 5.91600   -9.32700  8.73200  1.000 22.41862  ? 167 THR A OG1 1 
ATOM   513  C  CG2 . THR A  1 67  ? 4.25400   -10.57000 7.51500  1.000 30.03546  ? 167 THR A CG2 1 
ATOM   514  N  N   . PRO A  1 68  ? 3.46400   -6.82800  9.85200  1.000 25.08652  ? 168 PRO A N   1 
ATOM   515  C  CA  . PRO A  1 68  ? 3.63800   -5.70700  10.79100 1.000 26.43776  ? 168 PRO A CA  1 
ATOM   516  C  C   . PRO A  1 68  ? 5.01700   -5.61500  11.42300 1.000 25.64336  ? 168 PRO A C   1 
ATOM   517  O  O   . PRO A  1 68  ? 5.51500   -4.50000  11.60400 1.000 28.44925  ? 168 PRO A O   1 
ATOM   518  C  CB  . PRO A  1 68  ? 2.55100   -5.98000  11.83900 1.000 24.32739  ? 168 PRO A CB  1 
ATOM   519  C  CG  . PRO A  1 68  ? 1.45100   -6.60600  11.03000 1.000 28.84580  ? 168 PRO A CG  1 
ATOM   520  C  CD  . PRO A  1 68  ? 2.17600   -7.52000  10.07100 1.000 28.29984  ? 168 PRO A CD  1 
ATOM   521  N  N   . LEU A  1 69  ? 5.65700   -6.73800  11.75300 1.000 25.17074  ? 169 LEU A N   1 
ATOM   522  C  CA  . LEU A  1 69  ? 6.90400   -6.70300  12.51500 1.000 21.40570  ? 169 LEU A CA  1 
ATOM   523  C  C   . LEU A  1 69  ? 8.17000   -6.77000  11.66700 1.000 24.17685  ? 169 LEU A C   1 
ATOM   524  O  O   . LEU A  1 69  ? 9.26400   -6.72100  12.23600 1.000 27.89298  ? 169 LEU A O   1 
ATOM   525  C  CB  . LEU A  1 69  ? 6.95300   -7.85600  13.53900 1.000 20.28778  ? 169 LEU A CB  1 
ATOM   526  C  CG  . LEU A  1 69  ? 5.86900   -7.86700  14.61700 1.000 21.26506  ? 169 LEU A CG  1 
ATOM   527  C  CD1 . LEU A  1 69  ? 6.04200   -9.04100  15.59800 1.000 23.44649  ? 169 LEU A CD1 1 
ATOM   528  C  CD2 . LEU A  1 69  ? 5.90400   -6.54000  15.34300 1.000 24.53873  ? 169 LEU A CD2 1 
ATOM   529  N  N   . HIS A  1 70  ? 8.08200   -6.88000  10.34100 1.000 25.73264  ? 170 HIS A N   1 
ATOM   530  C  CA  . HIS A  1 70  ? 9.30600   -7.26200  9.63100  1.000 25.86257  ? 170 HIS A CA  1 
ATOM   531  C  C   . HIS A  1 70  ? 10.27800  -6.10000  9.44000  1.000 28.17501  ? 170 HIS A C   1 
ATOM   532  O  O   . HIS A  1 70  ? 11.48000  -6.33400  9.28400  1.000 29.93866  ? 170 HIS A O   1 
ATOM   533  C  CB  . HIS A  1 70  ? 8.98300   -7.87700  8.27600  1.000 26.86389  ? 170 HIS A CB  1 
ATOM   534  C  CG  . HIS A  1 70  ? 8.73900   -6.86900  7.19900  1.000 35.72399  ? 170 HIS A CG  1 
ATOM   535  N  ND1 . HIS A  1 70  ? 7.70100   -5.96200  7.25000  1.000 39.11544  ? 170 HIS A ND1 1 
ATOM   536  C  CD2 . HIS A  1 70  ? 9.39700   -6.62700  6.03900  1.000 37.04665  ? 170 HIS A CD2 1 
ATOM   537  C  CE1 . HIS A  1 70  ? 7.73100   -5.20300  6.16800  1.000 43.25718  ? 170 HIS A CE1 1 
ATOM   538  N  NE2 . HIS A  1 70  ? 8.74500   -5.59000  5.41400  1.000 33.82291  ? 170 HIS A NE2 1 
ATOM   539  N  N   . ASP A  1 71  ? 9.79500   -4.86200  9.44300  1.000 30.36126  ? 171 ASP A N   1 
ATOM   540  C  CA  . ASP A  1 71  ? 10.67400  -3.71500  9.27700  1.000 36.43379  ? 171 ASP A CA  1 
ATOM   541  C  C   . ASP A  1 71  ? 11.19300  -3.26000  10.63200 1.000 34.53547  ? 171 ASP A C   1 
ATOM   542  O  O   . ASP A  1 71  ? 10.43700  -3.16700  11.60000 1.000 38.88079  ? 171 ASP A O   1 
ATOM   543  C  CB  . ASP A  1 71  ? 9.94900   -2.56300  8.58500  1.000 39.71104  ? 171 ASP A CB  1 
ATOM   544  C  CG  . ASP A  1 71  ? 10.00800  -2.66100  7.07900  1.000 42.57566  ? 171 ASP A CG  1 
ATOM   545  O  OD1 . ASP A  1 71  ? 10.99500  -3.21900  6.54600  1.000 42.62473  ? 171 ASP A OD1 1 
ATOM   546  O  OD2 . ASP A  1 71  ? 9.06100   -2.17500  6.42900  1.000 45.87631  ? 171 ASP A OD2 1 
ATOM   547  N  N   . GLY A  1 72  ? 12.48100  -2.97400  10.69200 1.000 30.97485  ? 172 GLY A N   1 
ATOM   548  C  CA  . GLY A  1 72  ? 13.10700  -2.59300  11.93800 1.000 30.97744  ? 172 GLY A CA  1 
ATOM   549  C  C   . GLY A  1 72  ? 13.86300  -3.75400  12.55000 1.000 21.36297  ? 172 GLY A C   1 
ATOM   550  O  O   . GLY A  1 72  ? 13.93800  -4.86300  12.01100 1.000 24.10698  ? 172 GLY A O   1 
ATOM   551  N  N   . ALA A  1 73  ? 14.44100  -3.47600  13.70200 1.000 19.10784  ? 173 ALA A N   1 
ATOM   552  C  CA  . ALA A  1 73  ? 15.32700  -4.42700  14.34400 1.000 21.31886  ? 173 ALA A CA  1 
ATOM   553  C  C   . ALA A  1 73  ? 14.59100  -5.21600  15.40900 1.000 21.22785  ? 173 ALA A C   1 
ATOM   554  O  O   . ALA A  1 73  ? 13.78600  -4.66500  16.16800 1.000 22.30384  ? 173 ALA A O   1 
ATOM   555  C  CB  . ALA A  1 73  ? 16.52000  -3.70800  14.97800 1.000 20.17087  ? 173 ALA A CB  1 
ATOM   556  N  N   . VAL A  1 74  ? 14.89900  -6.49800  15.48500 1.000 18.28110  ? 174 VAL A N   1 
ATOM   557  C  CA  . VAL A  1 74  ? 14.64200  -7.25800  16.70300 1.000 18.50065  ? 174 VAL A CA  1 
ATOM   558  C  C   . VAL A  1 74  ? 15.80200  -6.99700  17.65600 1.000 19.84083  ? 174 VAL A C   1 
ATOM   559  O  O   . VAL A  1 74  ? 16.96400  -7.00800  17.23900 1.000 22.31190  ? 174 VAL A O   1 
ATOM   560  C  CB  . VAL A  1 74  ? 14.49300  -8.75100  16.38100 1.000 18.68938  ? 174 VAL A CB  1 
ATOM   561  C  CG1 . VAL A  1 74  ? 14.46100  -9.57400  17.65200 1.000 23.39266  ? 174 VAL A CG1 1 
ATOM   562  C  CG2 . VAL A  1 74  ? 13.18400  -8.99200  15.57800 1.000 22.11206  ? 174 VAL A CG2 1 
ATOM   563  N  N   . ILE A  1 75  ? 15.50200  -6.71300  18.92400 1.000 19.56759  ? 175 ILE A N   1 
ATOM   564  C  CA  . ILE A  1 75  ? 16.54700  -6.56700  19.93200 1.000 20.28838  ? 175 ILE A CA  1 
ATOM   565  C  C   . ILE A  1 75  ? 16.37000  -7.66200  20.97200 1.000 22.77511  ? 175 ILE A C   1 
ATOM   566  O  O   . ILE A  1 75  ? 15.29600  -7.79100  21.57200 1.000 22.25260  ? 175 ILE A O   1 
ATOM   567  C  CB  . ILE A  1 75  ? 16.53300  -5.17800  20.58500 1.000 17.83215  ? 175 ILE A CB  1 
ATOM   568  C  CG1 . ILE A  1 75  ? 16.78700  -4.11200  19.50900 1.000 19.12459  ? 175 ILE A CG1 1 
ATOM   569  C  CG2 . ILE A  1 75  ? 17.60200  -5.11400  21.66000 1.000 19.54363  ? 175 ILE A CG2 1 
ATOM   570  C  CD1 . ILE A  1 75  ? 16.59700  -2.66500  19.99000 1.000 21.41175  ? 175 ILE A CD1 1 
ATOM   571  N  N   . MET A  1 76  ? 17.43000  -8.43600  21.19200 1.000 19.89730  ? 176 MET A N   1 
ATOM   572  C  CA  . MET A  1 76  ? 17.45800  -9.49700  22.18400 1.000 23.03753  ? 176 MET A CA  1 
ATOM   573  C  C   . MET A  1 76  ? 18.21400  -9.02700  23.41300 1.000 27.37908  ? 176 MET A C   1 
ATOM   574  O  O   . MET A  1 76  ? 19.23300  -8.34400  23.29700 1.000 25.77296  ? 176 MET A O   1 
ATOM   575  C  CB  . MET A  1 76  ? 18.13700  -10.74300 21.61700 1.000 21.65159  ? 176 MET A CB  1 
ATOM   576  C  CG  . MET A  1 76  ? 17.30100  -11.45900 20.58400 1.000 29.55721  ? 176 MET A CG  1 
ATOM   577  S  SD  . MET A  1 76  ? 18.05800  -13.01100 20.06900 1.000 38.20365  ? 176 MET A SD  1 
ATOM   578  C  CE  . MET A  1 76  ? 18.96100  -13.47600 21.52900 1.000 26.78235  ? 176 MET A CE  1 
ATOM   579  N  N   . LYS A  1 77  ? 17.69800  -9.38800  24.58800 1.000 24.33517  ? 177 LYS A N   1 
ATOM   580  C  CA  . LYS A  1 77  ? 18.28900  -9.04000  25.87200 1.000 26.38462  ? 177 LYS A CA  1 
ATOM   581  C  C   . LYS A  1 77  ? 17.97100  -10.16700 26.84100 1.000 32.54930  ? 177 LYS A C   1 
ATOM   582  O  O   . LYS A  1 77  ? 16.83300  -10.64200 26.87000 1.000 32.19405  ? 177 LYS A O   1 
ATOM   583  C  CB  . LYS A  1 77  ? 17.71600  -7.71100  26.38700 1.000 31.70493  ? 177 LYS A CB  1 
ATOM   584  C  CG  . LYS A  1 77  ? 18.04800  -7.32600  27.81200 1.000 43.80871  ? 177 LYS A CG  1 
ATOM   585  C  CD  . LYS A  1 77  ? 17.19200  -6.12500  28.21600 1.000 40.22410  ? 177 LYS A CD  1 
ATOM   586  C  CE  . LYS A  1 77  ? 17.71800  -5.39900  29.43800 1.000 47.78428  ? 177 LYS A CE  1 
ATOM   587  N  NZ  . LYS A  1 77  ? 18.07800  -3.98500  29.09700 1.000 56.24553  ? 177 LYS A NZ  1 
ATOM   588  N  N   . ASN A  1 78  ? 18.96700  -10.59800 27.61800 1.000 33.56402  ? 178 ASN A N   1 
ATOM   589  C  CA  . ASN A  1 78  ? 18.74900  -11.58200 28.68400 1.000 36.97752  ? 178 ASN A CA  1 
ATOM   590  C  C   . ASN A  1 78  ? 18.12600  -12.87500 28.15900 1.000 34.92506  ? 178 ASN A C   1 
ATOM   591  O  O   . ASN A  1 78  ? 17.27100  -13.47100 28.81700 1.000 35.18000  ? 178 ASN A O   1 
ATOM   592  C  CB  . ASN A  1 78  ? 17.87300  -11.00200 29.79900 1.000 39.13278  ? 178 ASN A CB  1 
ATOM   593  C  CG  . ASN A  1 78  ? 18.50900  -9.81700  30.49200 1.000 44.58502  ? 178 ASN A CG  1 
ATOM   594  O  OD1 . ASN A  1 78  ? 19.72000  -9.77200  30.67800 1.000 41.84396  ? 178 ASN A OD1 1 
ATOM   595  N  ND2 . ASN A  1 78  ? 17.68700  -8.84700  30.87400 1.000 58.13593  ? 178 ASN A ND2 1 
ATOM   596  N  N   . ASN A  1 79  ? 18.53300  -13.29800 26.95600 1.000 32.11747  ? 179 ASN A N   1 
ATOM   597  C  CA  . ASN A  1 79  ? 18.08300  -14.55400 26.35200 1.000 29.01264  ? 179 ASN A CA  1 
ATOM   598  C  C   . ASN A  1 79  ? 16.60200  -14.51800 25.97000 1.000 32.49936  ? 179 ASN A C   1 
ATOM   599  O  O   . ASN A  1 79  ? 15.94800  -15.55900 25.89900 1.000 39.99268  ? 179 ASN A O   1 
ATOM   600  C  CB  . ASN A  1 79  ? 18.34900  -15.74600 27.27600 1.000 40.09641  ? 179 ASN A CB  1 
ATOM   601  C  CG  . ASN A  1 79  ? 18.89700  -16.94400 26.54200 1.000 49.18079  ? 179 ASN A CG  1 
ATOM   602  O  OD1 . ASN A  1 79  ? 19.79100  -16.81600 25.71100 1.000 51.15970  ? 179 ASN A OD1 1 
ATOM   603  N  ND2 . ASN A  1 79  ? 18.37000  -18.12300 26.85500 1.000 53.76362  ? 179 ASN A ND2 1 
ATOM   604  N  N   . GLU A  1 80  ? 16.05400  -13.32800 25.74100 1.000 27.94374  ? 180 GLU A N   1 
ATOM   605  C  CA  . GLU A  1 80  ? 14.69500  -13.18400 25.24700 1.000 24.65190  ? 180 GLU A CA  1 
ATOM   606  C  C   . GLU A  1 80  ? 14.67100  -12.18800 24.10100 1.000 25.74255  ? 180 GLU A C   1 
ATOM   607  O  O   . GLU A  1 80  ? 15.59200  -11.39200 23.91200 1.000 23.39278  ? 180 GLU A O   1 
ATOM   608  C  CB  . GLU A  1 80  ? 13.73300  -12.73500 26.35400 1.000 31.79075  ? 180 GLU A CB  1 
ATOM   609  C  CG  . GLU A  1 80  ? 13.36300  -13.85300 27.31400 1.000 36.56073  ? 180 GLU A CG  1 
ATOM   610  C  CD  . GLU A  1 80  ? 12.24200  -13.45900 28.24900 1.000 51.10528  ? 180 GLU A CD  1 
ATOM   611  O  OE1 . GLU A  1 80  ? 11.86900  -12.26400 28.27200 1.000 43.11446  ? 180 GLU A OE1 1 
ATOM   612  O  OE2 . GLU A  1 80  ? 11.73700  -14.35400 28.95500 1.000 58.21752  ? 180 GLU A OE2 1 
ATOM   613  N  N   . ILE A  1 81  ? 13.60200  -12.24700 23.31700 1.000 19.99885  ? 181 ILE A N   1 
ATOM   614  C  CA  . ILE A  1 81  ? 13.36800  -11.23200 22.29700 1.000 20.67355  ? 181 ILE A CA  1 
ATOM   615  C  C   . ILE A  1 81  ? 12.64100  -10.08800 22.99000 1.000 22.71913  ? 181 ILE A C   1 
ATOM   616  O  O   . ILE A  1 81  ? 11.46700  -10.21800 23.35200 1.000 22.28580  ? 181 ILE A O   1 
ATOM   617  C  CB  . ILE A  1 81  ? 12.55100  -11.78500 21.12400 1.000 20.89527  ? 181 ILE A CB  1 
ATOM   618  C  CG1 . ILE A  1 81  ? 13.36800  -12.83400 20.35600 1.000 24.40253  ? 181 ILE A CG1 1 
ATOM   619  C  CG2 . ILE A  1 81  ? 12.09400  -10.64300 20.22000 1.000 19.87296  ? 181 ILE A CG2 1 
ATOM   620  C  CD1 . ILE A  1 81  ? 12.51700  -13.79300 19.51500 1.000 25.01606  ? 181 ILE A CD1 1 
ATOM   621  N  N   . ALA A  1 82  ? 13.34800  -8.98100  23.22400 1.000 20.50349  ? 182 ALA A N   1 
ATOM   622  C  CA  . ALA A  1 82  ? 12.74700  -7.88900  23.98800 1.000 18.45370  ? 182 ALA A CA  1 
ATOM   623  C  C   . ALA A  1 82  ? 11.67200  -7.17600  23.16900 1.000 22.42126  ? 182 ALA A C   1 
ATOM   624  O  O   . ALA A  1 82  ? 10.56100  -6.94600  23.65400 1.000 23.42271  ? 182 ALA A O   1 
ATOM   625  C  CB  . ALA A  1 82  ? 13.81400  -6.89800  24.44900 1.000 24.63824  ? 182 ALA A CB  1 
ATOM   626  N  N   . ALA A  1 83  ? 11.99500  -6.81200  21.93100 1.000 20.60194  ? 183 ALA A N   1 
ATOM   627  C  CA  . ALA A  1 83  ? 11.07200  -6.04900  21.10000 1.000 20.57595  ? 183 ALA A CA  1 
ATOM   628  C  C   . ALA A  1 83  ? 11.40000  -6.27900  19.63100 1.000 22.56788  ? 183 ALA A C   1 
ATOM   629  O  O   . ALA A  1 83  ? 12.49000  -6.73400  19.27900 1.000 21.67394  ? 183 ALA A O   1 
ATOM   630  C  CB  . ALA A  1 83  ? 11.13400  -4.55800  21.43800 1.000 22.04578  ? 183 ALA A CB  1 
ATOM   631  N  N   . ALA A  1 84  ? 10.41900  -5.98800  18.77900 1.000 23.68152  ? 184 ALA A N   1 
ATOM   632  C  CA  . ALA A  1 84  ? 10.58600  -6.05600  17.34200 1.000 18.41696  ? 184 ALA A CA  1 
ATOM   633  C  C   . ALA A  1 84  ? 10.23400  -4.70400  16.73800 1.000 19.98887  ? 184 ALA A C   1 
ATOM   634  O  O   . ALA A  1 84  ? 9.62500   -3.85100  17.39200 1.000 26.07438  ? 184 ALA A O   1 
ATOM   635  C  CB  . ALA A  1 84  ? 9.71700   -7.17100  16.73900 1.000 20.62932  ? 184 ALA A CB  1 
ATOM   636  N  N   . ALA A  1 85  ? 10.62500  -4.52200  15.47000 1.000 19.80799  ? 185 ALA A N   1 
ATOM   637  C  CA  . ALA A  1 85  ? 10.34200  -3.29700  14.71500 1.000 23.86790  ? 185 ALA A CA  1 
ATOM   638  C  C   . ALA A  1 85  ? 10.92700  -2.06500  15.40700 1.000 28.22949  ? 185 ALA A C   1 
ATOM   639  O  O   . ALA A  1 85  ? 10.33800  -0.97700  15.39600 1.000 27.73549  ? 185 ALA A O   1 
ATOM   640  C  CB  . ALA A  1 85  ? 8.83600   -3.12500  14.46700 1.000 25.54085  ? 185 ALA A CB  1 
ATOM   641  N  N   . CYS A  1 86  ? 12.10900  -2.23200  15.99100 1.000 20.57480  ? 186 CYS A N   1 
ATOM   642  C  CA  . CYS A  1 86  ? 12.77800  -1.15500  16.70800 1.000 24.00508  ? 186 CYS A CA  1 
ATOM   643  C  C   . CYS A  1 86  ? 13.57100  -0.26700  15.76200 1.000 28.46812  ? 186 CYS A C   1 
ATOM   644  O  O   . CYS A  1 86  ? 14.07000  -0.71400  14.73100 1.000 24.45540  ? 186 CYS A O   1 
ATOM   645  C  CB  . CYS A  1 86  ? 13.73700  -1.71700  17.75200 1.000 24.92861  ? 186 CYS A CB  1 
ATOM   646  S  SG  . CYS A  1 86  ? 12.98900  -2.74100  19.02200 1.000 23.74198  ? 186 CYS A SG  1 
ATOM   647  N  N   . TYR A  1 87  ? 13.71900  0.99400   16.14700 1.000 27.14941  ? 187 TYR A N   1 
ATOM   648  C  CA  . TYR A  1 87  ? 14.58800  1.91100   15.42800 1.000 26.09718  ? 187 TYR A CA  1 
ATOM   649  C  C   . TYR A  1 87  ? 16.00700  1.79400   15.95800 1.000 27.86679  ? 187 TYR A C   1 
ATOM   650  O  O   . TYR A  1 87  ? 16.22400  1.59900   17.15700 1.000 28.34179  ? 187 TYR A O   1 
ATOM   651  C  CB  . TYR A  1 87  ? 14.09600  3.34900   15.56600 1.000 32.39414  ? 187 TYR A CB  1 
ATOM   652  C  CG  . TYR A  1 87  ? 12.80100  3.60100   14.82300 1.000 48.41726  ? 187 TYR A CG  1 
ATOM   653  C  CD1 . TYR A  1 87  ? 11.57400  3.24600   15.38000 1.000 50.91084  ? 187 TYR A CD1 1 
ATOM   654  C  CD2 . TYR A  1 87  ? 12.80400  4.17900   13.55600 1.000 60.17170  ? 187 TYR A CD2 1 
ATOM   655  C  CE1 . TYR A  1 87  ? 10.38700  3.47200   14.70100 1.000 57.83208  ? 187 TYR A CE1 1 
ATOM   656  C  CE2 . TYR A  1 87  ? 11.62300  4.41100   12.87000 1.000 62.43938  ? 187 TYR A CE2 1 
ATOM   657  C  CZ  . TYR A  1 87  ? 10.41900  4.05600   13.44800 1.000 61.24488  ? 187 TYR A CZ  1 
ATOM   658  O  OH  . TYR A  1 87  ? 9.24600   4.28100   12.76700 1.000 69.88387  ? 187 TYR A OH  1 
ATOM   659  N  N   . LEU A  1 88  ? 16.96600  1.90000   15.05200 1.000 24.27565  ? 188 LEU A N   1 
ATOM   660  C  CA  . LEU A  1 88  ? 18.37500  1.97500   15.39900 1.000 22.95633  ? 188 LEU A CA  1 
ATOM   661  C  C   . LEU A  1 88  ? 18.95900  3.21700   14.74900 1.000 29.88740  ? 188 LEU A C   1 
ATOM   662  O  O   . LEU A  1 88  ? 18.42900  3.69500   13.74200 1.000 33.16864  ? 188 LEU A O   1 
ATOM   663  C  CB  . LEU A  1 88  ? 19.13400  0.72400   14.92900 1.000 24.17566  ? 188 LEU A CB  1 
ATOM   664  C  CG  . LEU A  1 88  ? 18.74300  -0.63000  15.52900 1.000 23.43627  ? 188 LEU A CG  1 
ATOM   665  C  CD1 . LEU A  1 88  ? 19.56000  -1.73900  14.88800 1.000 22.04929  ? 188 LEU A CD1 1 
ATOM   666  C  CD2 . LEU A  1 88  ? 18.91000  -0.66700  17.03700 1.000 23.68727  ? 188 LEU A CD2 1 
ATOM   667  N  N   . PRO A  1 89  ? 20.03000  3.77800   15.31000 1.000 32.40303  ? 189 PRO A N   1 
ATOM   668  C  CA  . PRO A  1 89  ? 20.63400  4.96000   14.68800 1.000 33.50932  ? 189 PRO A CA  1 
ATOM   669  C  C   . PRO A  1 89  ? 21.38800  4.57500   13.42400 1.000 31.89134  ? 189 PRO A C   1 
ATOM   670  O  O   . PRO A  1 89  ? 22.08900  3.56200   13.38200 1.000 30.16941  ? 189 PRO A O   1 
ATOM   671  C  CB  . PRO A  1 89  ? 21.57800  5.48700   15.77500 1.000 34.14228  ? 189 PRO A CB  1 
ATOM   672  C  CG  . PRO A  1 89  ? 21.95800  4.26600   16.54400 1.000 33.24804  ? 189 PRO A CG  1 
ATOM   673  C  CD  . PRO A  1 89  ? 20.74800  3.36200   16.53000 1.000 27.92386  ? 189 PRO A CD  1 
ATOM   674  N  N   . LEU A  1 90  ? 21.22300  5.38200   12.37700 1.000 30.36141  ? 190 LEU A N   1 
ATOM   675  C  CA  . LEU A  1 90  ? 21.92200  5.12400   11.12400 1.000 30.27884  ? 190 LEU A CA  1 
ATOM   676  C  C   . LEU A  1 90  ? 23.35100  5.63300   11.20700 1.000 32.63147  ? 190 LEU A C   1 
ATOM   677  O  O   . LEU A  1 90  ? 23.58100  6.80100   11.52700 1.000 34.71312  ? 190 LEU A O   1 
ATOM   678  C  CB  . LEU A  1 90  ? 21.20800  5.79900   9.95500  1.000 35.62365  ? 190 LEU A CB  1 
ATOM   679  C  CG  . LEU A  1 90  ? 19.79200  5.30800   9.68900  1.000 41.52826  ? 190 LEU A CG  1 
ATOM   680  C  CD1 . LEU A  1 90  ? 19.28400  5.89400   8.38900  1.000 46.90461  ? 190 LEU A CD1 1 
ATOM   681  C  CD2 . LEU A  1 90  ? 19.77100  3.79300   9.65300  1.000 38.07290  ? 190 LEU A CD2 1 
ATOM   682  N  N   . SER A  1 91  ? 24.31200  4.76300   10.90600 1.000 30.55868  ? 191 SER A N   1 
ATOM   683  C  CA  . SER A  1 91  ? 25.69900  5.20400   10.84900 1.000 31.41953  ? 191 SER A CA  1 
ATOM   684  C  C   . SER A  1 91  ? 25.85400  6.33000   9.83900  1.000 33.83081  ? 191 SER A C   1 
ATOM   685  O  O   . SER A  1 91  ? 25.19700  6.34400   8.79400  1.000 32.31847  ? 191 SER A O   1 
ATOM   686  C  CB  . SER A  1 91  ? 26.61900  4.04900   10.46500 1.000 28.10414  ? 191 SER A CB  1 
ATOM   687  O  OG  . SER A  1 91  ? 27.93200  4.53800   10.23200 1.000 31.91336  ? 191 SER A OG  1 
ATOM   688  N  N   . GLU A  1 92  ? 26.73000  7.28100   10.15500 1.000 30.03748  ? 192 GLU A N   1 
ATOM   689  C  CA  . GLU A  1 92  ? 27.13000  8.30500   9.19800  1.000 33.00139  ? 192 GLU A CA  1 
ATOM   690  C  C   . GLU A  1 92  ? 28.49100  8.01600   8.58600  1.000 32.94716  ? 192 GLU A C   1 
ATOM   691  O  O   . GLU A  1 92  ? 29.06600  8.89100   7.92400  1.000 31.94876  ? 192 GLU A O   1 
ATOM   692  C  CB  . GLU A  1 92  ? 27.12100  9.68100   9.86200  1.000 44.76272  ? 192 GLU A CB  1 
ATOM   693  C  CG  . GLU A  1 92  ? 25.78800  10.39600  9.72300  1.000 53.05544  ? 192 GLU A CG  1 
ATOM   694  C  CD  . GLU A  1 92  ? 25.35500  11.08600  10.99800 1.000 72.97780  ? 192 GLU A CD  1 
ATOM   695  O  OE1 . GLU A  1 92  ? 26.23400  11.48500  11.79200 1.000 74.67549  ? 192 GLU A OE1 1 
ATOM   696  O  OE2 . GLU A  1 92  ? 24.12900  11.21700  11.21000 1.000 81.08201  ? 192 GLU A OE2 1 
ATOM   697  N  N   . SER A  1 93  ? 29.00500  6.81000   8.78400  1.000 29.19942  ? 193 SER A N   1 
ATOM   698  C  CA  . SER A  1 93  ? 30.31600  6.44200   8.26700  1.000 29.17301  ? 193 SER A CA  1 
ATOM   699  C  C   . SER A  1 93  ? 30.38200  6.63700   6.75500  1.000 31.51180  ? 193 SER A C   1 
ATOM   700  O  O   . SER A  1 93  ? 29.46600  6.21200   6.03600  1.000 37.90542  ? 193 SER A O   1 
ATOM   701  C  CB  . SER A  1 93  ? 30.62800  4.98700   8.61000  1.000 31.93936  ? 193 SER A CB  1 
ATOM   702  O  OG  . SER A  1 93  ? 31.86700  4.59400   8.04400  1.000 31.88536  ? 193 SER A OG  1 
ATOM   703  N  N   . PRO A  1 94  ? 31.44200  7.25200   6.22900  1.000 36.76405  ? 194 PRO A N   1 
ATOM   704  C  CA  . PRO A  1 94  ? 31.60000  7.30800   4.77400  1.000 37.15546  ? 194 PRO A CA  1 
ATOM   705  C  C   . PRO A  1 94  ? 32.18300  6.04100   4.16800  1.000 37.95648  ? 194 PRO A C   1 
ATOM   706  O  O   . PRO A  1 94  ? 32.41800  6.01500   2.95400  1.000 39.38115  ? 194 PRO A O   1 
ATOM   707  C  CB  . PRO A  1 94  ? 32.54600  8.50100   4.57800  1.000 36.83611  ? 194 PRO A CB  1 
ATOM   708  C  CG  . PRO A  1 94  ? 33.42000  8.46900   5.81100  1.000 31.61662  ? 194 PRO A CG  1 
ATOM   709  C  CD  . PRO A  1 94  ? 32.54200  7.93400   6.94100  1.000 31.39881  ? 194 PRO A CD  1 
ATOM   710  N  N   . PHE A  1 95  ? 32.41700  4.99400   4.96200  1.000 32.88549  ? 195 PHE A N   1 
ATOM   711  C  CA  . PHE A  1 95  ? 33.01800  3.76000   4.47200  1.000 40.85670  ? 195 PHE A CA  1 
ATOM   712  C  C   . PHE A  1 95  ? 32.01400  2.61800   4.35600  1.000 48.49520  ? 195 PHE A C   1 
ATOM   713  O  O   . PHE A  1 95  ? 32.42000  1.45500   4.28000  1.000 55.38150  ? 195 PHE A O   1 
ATOM   714  C  CB  . PHE A  1 95  ? 34.18300  3.33700   5.37200  1.000 36.76256  ? 195 PHE A CB  1 
ATOM   715  C  CG  . PHE A  1 95  ? 35.24400  4.38800   5.51200  1.000 30.35022  ? 195 PHE A CG  1 
ATOM   716  C  CD1 . PHE A  1 95  ? 36.12100  4.64800   4.47000  1.000 28.93987  ? 195 PHE A CD1 1 
ATOM   717  C  CD2 . PHE A  1 95  ? 35.34800  5.13700   6.67500  1.000 24.50835  ? 195 PHE A CD2 1 
ATOM   718  C  CE1 . PHE A  1 95  ? 37.09000  5.62300   4.58800  1.000 33.47287  ? 195 PHE A CE1 1 
ATOM   719  C  CE2 . PHE A  1 95  ? 36.31100  6.11500   6.79600  1.000 27.34563  ? 195 PHE A CE2 1 
ATOM   720  C  CZ  . PHE A  1 95  ? 37.18100  6.36100   5.75200  1.000 23.68971  ? 195 PHE A CZ  1 
ATOM   721  N  N   . ILE A  1 96  ? 30.71800  2.91000   4.34800  1.000 40.73263  ? 196 ILE A N   1 
ATOM   722  C  CA  . ILE A  1 96  ? 29.70200  1.88400   4.13800  1.000 40.38858  ? 196 ILE A CA  1 
ATOM   723  C  C   . ILE A  1 96  ? 29.32000  1.88300   2.66500  1.000 39.84458  ? 196 ILE A C   1 
ATOM   724  O  O   . ILE A  1 96  ? 28.92200  2.91800   2.11200  1.000 42.83241  ? 196 ILE A O   1 
ATOM   725  C  CB  . ILE A  1 96  ? 28.47100  2.10100   5.02500  1.000 39.74872  ? 196 ILE A CB  1 
ATOM   726  C  CG1 . ILE A  1 96  ? 28.87800  2.16700   6.49200  1.000 37.03238  ? 196 ILE A CG1 1 
ATOM   727  C  CG2 . ILE A  1 96  ? 27.47000  0.97100   4.81000  1.000 42.54964  ? 196 ILE A CG2 1 
ATOM   728  C  CD1 . ILE A  1 96  ? 27.71200  2.33000   7.40700  1.000 36.48084  ? 196 ILE A CD1 1 
ATOM   729  N  N   . SER A  1 97  ? 29.43100  0.71800   2.03700  1.000 39.74485  ? 197 SER A N   1 
ATOM   730  C  CA  . SER A  1 97  ? 29.19700  0.61400   0.60600  1.000 44.71900  ? 197 SER A CA  1 
ATOM   731  C  C   . SER A  1 97  ? 27.73800  0.89300   0.27200  1.000 49.69749  ? 197 SER A C   1 
ATOM   732  O  O   . SER A  1 97  ? 26.82800  0.48100   0.99900  1.000 41.67923  ? 197 SER A O   1 
ATOM   733  C  CB  . SER A  1 97  ? 29.59100  -0.77500  0.11000  1.000 48.08570  ? 197 SER A CB  1 
ATOM   734  O  OG  . SER A  1 97  ? 29.21400  -0.94500  -1.24700 1.000 45.75161  ? 197 SER A OG  1 
ATOM   735  N  N   . LYS A  1 98  ? 27.51600  1.59600   -0.84700 1.000 35.25333  ? 198 LYS A N   1 
ATOM   736  C  CA  . LYS A  1 98  ? 26.15100  1.79600   -1.32000 1.000 45.41966  ? 198 LYS A CA  1 
ATOM   737  C  C   . LYS A  1 98  ? 25.56200  0.53700   -1.92400 1.000 39.25404  ? 198 LYS A C   1 
ATOM   738  O  O   . LYS A  1 98  ? 24.40600  0.56000   -2.36000 1.000 45.30858  ? 198 LYS A O   1 
ATOM   739  C  CB  . LYS A  1 98  ? 26.08700  2.94400   -2.32900 1.000 48.19508  ? 198 LYS A CB  1 
ATOM   740  C  CG  . LYS A  1 98  ? 26.51700  4.28800   -1.75400 1.000 51.34161  ? 198 LYS A CG  1 
ATOM   741  C  CD  . LYS A  1 98  ? 26.04900  4.45400   -0.31300 1.000 66.56221  ? 198 LYS A CD  1 
ATOM   742  C  CE  . LYS A  1 98  ? 24.64900  5.03400   -0.23000 1.000 52.52762  ? 198 LYS A CE  1 
ATOM   743  N  NZ  . LYS A  1 98  ? 24.68300  6.51400   -0.34300 1.000 65.09797  ? 198 LYS A NZ  1 
ATOM   744  N  N   . GLU A  1 99  ? 26.33100  -0.55300  -1.96900 1.000 44.29557  ? 199 GLU A N   1 
ATOM   745  C  CA  . GLU A  1 99  ? 25.73800  -1.86100  -2.21200 1.000 51.53701  ? 199 GLU A CA  1 
ATOM   746  C  C   . GLU A  1 99  ? 24.80800  -2.26800  -1.08500 1.000 44.45122  ? 199 GLU A C   1 
ATOM   747  O  O   . GLU A  1 99  ? 23.90500  -3.08400  -1.30000 1.000 44.64255  ? 199 GLU A O   1 
ATOM   748  C  CB  . GLU A  1 99  ? 26.82800  -2.91800  -2.36800 1.000 48.83312  ? 199 GLU A CB  1 
ATOM   749  C  CG  . GLU A  1 99  ? 27.53500  -2.88700  -3.69800 1.000 57.17654  ? 199 GLU A CG  1 
ATOM   750  C  CD  . GLU A  1 99  ? 28.61100  -3.94400  -3.79400 1.000 63.96159  ? 199 GLU A CD  1 
ATOM   751  O  OE1 . GLU A  1 99  ? 28.75600  -4.73000  -2.83000 1.000 61.35630  ? 199 GLU A OE1 1 
ATOM   752  O  OE2 . GLU A  1 99  ? 29.31000  -3.98600  -4.82800 1.000 65.62316  ? 199 GLU A OE2 1 
ATOM   753  N  N   . LEU A  1 100 ? 25.01200  -1.72300  0.10600  1.000 32.91193  ? 200 LEU A N   1 
ATOM   754  C  CA  . LEU A  1 100 ? 24.30000  -2.15700  1.29600  1.000 39.26108  ? 200 LEU A CA  1 
ATOM   755  C  C   . LEU A  1 100 ? 23.08400  -1.27900  1.57300  1.000 42.06590  ? 200 LEU A C   1 
ATOM   756  O  O   . LEU A  1 100 ? 22.99100  -0.13600  1.12700  1.000 46.52646  ? 200 LEU A O   1 
ATOM   757  C  CB  . LEU A  1 100 ? 25.24200  -2.15100  2.49500  1.000 37.07634  ? 200 LEU A CB  1 
ATOM   758  C  CG  . LEU A  1 100 ? 26.37400  -3.14500  2.27400  1.000 42.90708  ? 200 LEU A CG  1 
ATOM   759  C  CD1 . LEU A  1 100 ? 27.45100  -2.93600  3.29200  1.000 39.19623  ? 200 LEU A CD1 1 
ATOM   760  C  CD2 . LEU A  1 100 ? 25.84400  -4.57400  2.31900  1.000 47.87930  ? 200 LEU A CD2 1 
ATOM   761  N  N   . GLY A  1 101 ? 22.15400  -1.83100  2.34900  1.000 39.08865  ? 201 GLY A N   1 
ATOM   762  C  CA  . GLY A  1 101 ? 20.89200  -1.18400  2.60600  1.000 45.68173  ? 201 GLY A CA  1 
ATOM   763  C  C   . GLY A  1 101 ? 20.85800  -0.44700  3.93600  1.000 38.34258  ? 201 GLY A C   1 
ATOM   764  O  O   . GLY A  1 101 ? 21.82700  -0.39000  4.69600  1.000 32.19340  ? 201 GLY A O   1 
ATOM   765  N  N   . THR A  1 102 ? 19.69000  0.14600   4.18900  1.000 31.09831  ? 202 THR A N   1 
ATOM   766  C  CA  . THR A  1 102 ? 19.42800  0.80100   5.46100  1.000 32.05888  ? 202 THR A CA  1 
ATOM   767  C  C   . THR A  1 102 ? 19.60900  -0.15600  6.63000  1.000 31.12222  ? 202 THR A C   1 
ATOM   768  O  O   . THR A  1 102 ? 20.06900  0.25900   7.69800  1.000 28.74381  ? 202 THR A O   1 
ATOM   769  C  CB  . THR A  1 102 ? 18.01000  1.37400   5.46200  1.000 34.20702  ? 202 THR A CB  1 
ATOM   770  O  OG1 . THR A  1 102 ? 17.82300  2.16900   4.28400  1.000 41.48054  ? 202 THR A OG1 1 
ATOM   771  C  CG2 . THR A  1 102 ? 17.78200  2.23000   6.69900  1.000 41.37275  ? 202 THR A CG2 1 
ATOM   772  N  N   . ARG A  1 103 ? 19.23800  -1.43100  6.45700  1.000 28.46356  ? 203 ARG A N   1 
ATOM   773  C  CA  . ARG A  1 103 ? 19.44900  -2.40200  7.52900  1.000 27.65810  ? 203 ARG A CA  1 
ATOM   774  C  C   . ARG A  1 103 ? 20.90600  -2.42500  7.95000  1.000 25.31187  ? 203 ARG A C   1 
ATOM   775  O  O   . ARG A  1 103 ? 21.21200  -2.42700  9.14900  1.000 23.77390  ? 203 ARG A O   1 
ATOM   776  C  CB  . ARG A  1 103 ? 19.01700  -3.80300  7.09500  1.000 32.26690  ? 203 ARG A CB  1 
ATOM   777  C  CG  . ARG A  1 103 ? 17.52300  -4.08600  7.22100  1.000 32.66794  ? 203 ARG A CG  1 
ATOM   778  C  CD  . ARG A  1 103 ? 17.22000  -5.51600  6.79400  1.000 26.80315  ? 203 ARG A CD  1 
ATOM   779  N  NE  . ARG A  1 103 ? 15.80200  -5.80600  6.94400  1.000 30.46121  ? 203 ARG A NE  1 
ATOM   780  C  CZ  . ARG A  1 103 ? 14.93600  -5.74200  5.94300  1.000 37.05107  ? 203 ARG A CZ  1 
ATOM   781  N  NH1 . ARG A  1 103 ? 15.33300  -5.48100  4.71300  1.000 36.21079  ? 203 ARG A NH1 1 
ATOM   782  N  NH2 . ARG A  1 103 ? 13.64400  -5.93800  6.18800  1.000 45.27548  ? 203 ARG A NH2 1 
ATOM   783  N  N   . HIS A  1 104 ? 21.81800  -2.43600  6.97500  1.000 24.37347  ? 204 HIS A N   1 
ATOM   784  C  CA  . HIS A  1 104 ? 23.24000  -2.48900  7.29500  1.000 26.18043  ? 204 HIS A CA  1 
ATOM   785  C  C   . HIS A  1 104 ? 23.72100  -1.19100  7.91700  1.000 22.60195  ? 204 HIS A C   1 
ATOM   786  O  O   . HIS A  1 104 ? 24.55900  -1.20900  8.82600  1.000 22.81552  ? 204 HIS A O   1 
ATOM   787  C  CB  . HIS A  1 104 ? 24.05500  -2.79900  6.04300  1.000 24.65482  ? 204 HIS A CB  1 
ATOM   788  C  CG  . HIS A  1 104 ? 23.74500  -4.13300  5.45000  1.000 25.09256  ? 204 HIS A CG  1 
ATOM   789  N  ND1 . HIS A  1 104 ? 22.78600  -4.30700  4.47600  1.000 26.55492  ? 204 HIS A ND1 1 
ATOM   790  C  CD2 . HIS A  1 104 ? 24.24800  -5.36100  5.70900  1.000 21.72963  ? 204 HIS A CD2 1 
ATOM   791  C  CE1 . HIS A  1 104 ? 22.71900  -5.58600  4.15200  1.000 28.89516  ? 204 HIS A CE1 1 
ATOM   792  N  NE2 . HIS A  1 104 ? 23.59300  -6.24900  4.88900  1.000 22.92520  ? 204 HIS A NE2 1 
ATOM   793  N  N   . ARG A  1 105 ? 23.23100  -0.05000  7.42300  1.000 24.39943  ? 205 ARG A N   1 
ATOM   794  C  CA  . ARG A  1 105 ? 23.63600  1.22100   8.01500  1.000 27.52704  ? 205 ARG A CA  1 
ATOM   795  C  C   . ARG A  1 105 ? 23.11600  1.36100   9.44200  1.000 23.52257  ? 205 ARG A C   1 
ATOM   796  O  O   . ARG A  1 105 ? 23.80600  1.93500   10.29300 1.000 25.47622  ? 205 ARG A O   1 
ATOM   797  C  CB  . ARG A  1 105 ? 23.16300  2.39400   7.15000  1.000 32.00835  ? 205 ARG A CB  1 
ATOM   798  C  CG  . ARG A  1 105 ? 23.67600  3.74500   7.63600  1.000 35.26465  ? 205 ARG A CG  1 
ATOM   799  C  CD  . ARG A  1 105 ? 23.44900  4.88000   6.63000  1.000 40.53772  ? 205 ARG A CD  1 
ATOM   800  N  NE  . ARG A  1 105 ? 24.30200  4.78000   5.44700  1.000 42.27308  ? 205 ARG A NE  1 
ATOM   801  C  CZ  . ARG A  1 105 ? 25.57100  5.17100   5.38500  1.000 51.04511  ? 205 ARG A CZ  1 
ATOM   802  N  NH1 . ARG A  1 105 ? 26.20200  5.65800   6.44300  1.000 43.90257  ? 205 ARG A NH1 1 
ATOM   803  N  NH2 . ARG A  1 105 ? 26.22700  5.06400   4.23100  1.000 49.65754  ? 205 ARG A NH2 1 
ATOM   804  N  N   . ALA A  1 106 ? 21.91800  0.83400   9.72900  1.000 22.77807  ? 206 ALA A N   1 
ATOM   805  C  CA  . ALA A  1 106 ? 21.41500  0.83900   11.10100 1.000 20.55421  ? 206 ALA A CA  1 
ATOM   806  C  C   . ALA A  1 106 ? 22.21500  -0.10100  11.98700 1.000 22.87385  ? 206 ALA A C   1 
ATOM   807  O  O   . ALA A  1 106 ? 22.48400  0.21100   13.15500 1.000 22.99898  ? 206 ALA A O   1 
ATOM   808  C  CB  . ALA A  1 106 ? 19.94000  0.43600   11.12400 1.000 26.41441  ? 206 ALA A CB  1 
ATOM   809  N  N   . ALA A  1 107 ? 22.58400  -1.26400  11.45800 1.000 20.29890  ? 207 ALA A N   1 
ATOM   810  C  CA  . ALA A  1 107 ? 23.39200  -2.20200  12.23100 1.000 18.48077  ? 207 ALA A CA  1 
ATOM   811  C  C   . ALA A  1 107 ? 24.74100  -1.60000  12.59300 1.000 22.18396  ? 207 ALA A C   1 
ATOM   812  O  O   . ALA A  1 107 ? 25.18200  -1.68700  13.73900 1.000 20.42096  ? 207 ALA A O   1 
ATOM   813  C  CB  . ALA A  1 107 ? 23.57100  -3.49700  11.44300 1.000 18.61212  ? 207 ALA A CB  1 
ATOM   814  N  N   . VAL A  1 108 ? 25.43300  -1.01000  11.61500 1.000 21.94153  ? 208 VAL A N   1 
ATOM   815  C  CA  . VAL A  1 108 ? 26.70200  -0.36500  11.92400 1.000 20.19550  ? 208 VAL A CA  1 
ATOM   816  C  C   . VAL A  1 108 ? 26.49600  0.77300   12.91400 1.000 24.35319  ? 208 VAL A C   1 
ATOM   817  O  O   . VAL A  1 108 ? 27.28500  0.94500   13.85100 1.000 24.63490  ? 208 VAL A O   1 
ATOM   818  C  CB  . VAL A  1 108 ? 27.37900  0.12800   10.63500 1.000 19.58708  ? 208 VAL A CB  1 
ATOM   819  C  CG1 . VAL A  1 108 ? 28.64000  0.90600   10.98100 1.000 25.39951  ? 208 VAL A CG1 1 
ATOM   820  C  CG2 . VAL A  1 108 ? 27.68600  -1.06200  9.73200  1.000 22.37238  ? 208 VAL A CG2 1 
ATOM   821  N  N   . GLY A  1 109 ? 25.41100  1.53700   12.74400 1.000 23.51758  ? 209 GLY A N   1 
ATOM   822  C  CA  . GLY A  1 109 ? 25.14600  2.66400   13.63200 1.000 25.49407  ? 209 GLY A CA  1 
ATOM   823  C  C   . GLY A  1 109 ? 24.99100  2.26900   15.08900 1.000 24.31566  ? 209 GLY A C   1 
ATOM   824  O  O   . GLY A  1 109 ? 25.57800  2.89500   15.97700 1.000 24.25657  ? 209 GLY A O   1 
ATOM   825  N  N   . ILE A  1 110 ? 24.19800  1.22900   15.36300 1.000 22.15173  ? 210 ILE A N   1 
ATOM   826  C  CA  . ILE A  1 110 ? 24.05900  0.81700   16.75800 1.000 24.19851  ? 210 ILE A CA  1 
ATOM   827  C  C   . ILE A  1 110 ? 25.37400  0.23900   17.26600 1.000 26.72321  ? 210 ILE A C   1 
ATOM   828  O  O   . ILE A  1 110 ? 25.70400  0.40300   18.44000 1.000 24.77990  ? 210 ILE A O   1 
ATOM   829  C  CB  . ILE A  1 110 ? 22.88000  -0.16200  16.96200 1.000 20.04356  ? 210 ILE A CB  1 
ATOM   830  C  CG1 . ILE A  1 110 ? 22.54200  -0.33300  18.46000 1.000 20.19293  ? 210 ILE A CG1 1 
ATOM   831  C  CG2 . ILE A  1 110 ? 23.18800  -1.54000  16.41300 1.000 18.34421  ? 210 ILE A CG2 1 
ATOM   832  C  CD1 . ILE A  1 110 ? 22.02300  0.92100   19.13800 1.000 22.40879  ? 210 ILE A CD1 1 
ATOM   833  N  N   . SER A  1 111 ? 26.16600  -0.40300  16.39500 1.000 20.12831  ? 211 SER A N   1 
ATOM   834  C  CA  . SER A  1 111 ? 27.44800  -0.95700  16.82300 1.000 22.89679  ? 211 SER A CA  1 
ATOM   835  C  C   . SER A  1 111 ? 28.48700  0.11900   17.12000 1.000 24.24133  ? 211 SER A C   1 
ATOM   836  O  O   . SER A  1 111 ? 29.51900  -0.18800  17.72900 1.000 23.72574  ? 211 SER A O   1 
ATOM   837  C  CB  . SER A  1 111 ? 28.00600  -1.91700  15.76000 1.000 21.22313  ? 211 SER A CB  1 
ATOM   838  O  OG  . SER A  1 111 ? 28.68200  -1.21000  14.72700 1.000 23.91156  ? 211 SER A OG  1 
ATOM   839  N  N   . GLU A  1 112 ? 28.25300  1.35800   16.68500 1.000 23.54522  ? 212 GLU A N   1 
ATOM   840  C  CA  . GLU A  1 112 ? 29.16000  2.46000   16.97400 1.000 27.26874  ? 212 GLU A CA  1 
ATOM   841  C  C   . GLU A  1 112 ? 28.98100  3.02300   18.37700 1.000 29.70598  ? 212 GLU A C   1 
ATOM   842  O  O   . GLU A  1 112 ? 29.91000  3.65300   18.89600 1.000 28.61688  ? 212 GLU A O   1 
ATOM   843  C  CB  . GLU A  1 112 ? 28.95700  3.59300   15.96500 1.000 26.51189  ? 212 GLU A CB  1 
ATOM   844  C  CG  . GLU A  1 112 ? 29.47900  3.29600   14.56400 1.000 26.46226  ? 212 GLU A CG  1 
ATOM   845  C  CD  . GLU A  1 112 ? 28.94000  4.26600   13.51800 1.000 27.34500  ? 212 GLU A CD  1 
ATOM   846  O  OE1 . GLU A  1 112 ? 28.09300  5.12200   13.86800 1.000 33.20873  ? 212 GLU A OE1 1 
ATOM   847  O  OE2 . GLU A  1 112 ? 29.35800  4.16800   12.34300 1.000 34.11268  ? 212 GLU A OE2 1 
ATOM   848  N  N   . VAL A  1 113 ? 27.80800  2.84300   18.98100 1.000 30.48871  ? 213 VAL A N   1 
ATOM   849  C  CA  . VAL A  1 113 ? 27.47700  3.47500   20.25100 1.000 30.15234  ? 213 VAL A CA  1 
ATOM   850  C  C   . VAL A  1 113 ? 27.14800  2.46700   21.33700 1.000 29.79083  ? 213 VAL A C   1 
ATOM   851  O  O   . VAL A  1 113 ? 26.78700  2.86600   22.45300 1.000 31.68269  ? 213 VAL A O   1 
ATOM   852  C  CB  . VAL A  1 113 ? 26.32600  4.48900   20.08500 1.000 29.74592  ? 213 VAL A CB  1 
ATOM   853  C  CG1 . VAL A  1 113 ? 26.73800  5.58000   19.10200 1.000 36.00199  ? 213 VAL A CG1 1 
ATOM   854  C  CG2 . VAL A  1 113 ? 25.03400  3.79100   19.62000 1.000 26.15330  ? 213 VAL A CG2 1 
ATOM   855  N  N   . THR A  1 114 ? 27.25500  1.17300   21.04300 1.000 22.38019  ? 214 THR A N   1 
ATOM   856  C  CA  . THR A  1 114 ? 27.05600  0.09900   22.00300 1.000 26.29306  ? 214 THR A CA  1 
ATOM   857  C  C   . THR A  1 114 ? 28.06400  -1.00300  21.71000 1.000 25.86338  ? 214 THR A C   1 
ATOM   858  O  O   . THR A  1 114 ? 28.67600  -1.04400  20.64100 1.000 26.58767  ? 214 THR A O   1 
ATOM   859  C  CB  . THR A  1 114 ? 25.64600  -0.49600  21.92000 1.000 23.20460  ? 214 THR A CB  1 
ATOM   860  O  OG1 . THR A  1 114 ? 25.54000  -1.25500  20.70700 1.000 26.75711  ? 214 THR A OG1 1 
ATOM   861  C  CG2 . THR A  1 114 ? 24.57500  0.58700   21.92000 1.000 25.67932  ? 214 THR A CG2 1 
ATOM   862  N  N   . ASP A  1 115 ? 28.21500  -1.92700  22.66000 1.000 22.51760  ? 215 ASP A N   1 
ATOM   863  C  CA  . ASP A  1 115 ? 29.00400  -3.12700  22.43200 1.000 25.11882  ? 215 ASP A CA  1 
ATOM   864  C  C   . ASP A  1 115 ? 28.16400  -4.29000  21.92800 1.000 24.00852  ? 215 ASP A C   1 
ATOM   865  O  O   . ASP A  1 115 ? 28.57800  -5.45000  22.07600 1.000 26.95566  ? 215 ASP A O   1 
ATOM   866  C  CB  . ASP A  1 115 ? 29.74600  -3.52800  23.71000 1.000 25.03064  ? 215 ASP A CB  1 
ATOM   867  C  CG  . ASP A  1 115 ? 28.80400  -3.91100  24.83900 1.000 32.63214  ? 215 ASP A CG  1 
ATOM   868  O  OD1 . ASP A  1 115 ? 27.59600  -3.58700  24.77200 1.000 29.21332  ? 215 ASP A OD1 1 
ATOM   869  O  OD2 . ASP A  1 115 ? 29.28100  -4.55200  25.79700 1.000 37.74838  ? 215 ASP A OD2 1 
ATOM   870  N  N   . SER A  1 116 ? 27.00300  -4.01100  21.33500 1.000 21.96654  ? 216 SER A N   1 
ATOM   871  C  CA  . SER A  1 116 ? 26.11400  -5.07900  20.92400 1.000 19.78743  ? 216 SER A CA  1 
ATOM   872  C  C   . SER A  1 116 ? 26.68700  -5.81500  19.71800 1.000 20.63240  ? 216 SER A C   1 
ATOM   873  O  O   . SER A  1 116 ? 27.63300  -5.36000  19.06100 1.000 23.20956  ? 216 SER A O   1 
ATOM   874  C  CB  . SER A  1 116 ? 24.72700  -4.53200  20.57400 1.000 21.47569  ? 216 SER A CB  1 
ATOM   875  O  OG  . SER A  1 116 ? 24.83000  -3.53900  19.56400 1.000 21.81073  ? 216 SER A OG  1 
ATOM   876  N  N   . LEU A  1 117 ? 26.09500  -6.96800  19.43800 1.000 19.75006  ? 217 LEU A N   1 
ATOM   877  C  CA  . LEU A  1 117 ? 26.32700  -7.70700  18.20800 1.000 19.17978  ? 217 LEU A CA  1 
ATOM   878  C  C   . LEU A  1 117 ? 25.04900  -7.66600  17.38000 1.000 17.88306  ? 217 LEU A C   1 
ATOM   879  O  O   . LEU A  1 117 ? 23.97000  -8.02000  17.87300 1.000 18.41546  ? 217 LEU A O   1 
ATOM   880  C  CB  . LEU A  1 117 ? 26.74400  -9.14800  18.51700 1.000 17.52777  ? 217 LEU A CB  1 
ATOM   881  C  CG  . LEU A  1 117 ? 27.19500  -9.97100  17.30500 1.000 21.14639  ? 217 LEU A CG  1 
ATOM   882  C  CD1 . LEU A  1 117 ? 28.16800  -11.04200 17.75600 1.000 30.39669  ? 217 LEU A CD1 1 
ATOM   883  C  CD2 . LEU A  1 117 ? 26.01700  -10.61200 16.54600 1.000 24.02133  ? 217 LEU A CD2 1 
ATOM   884  N  N   . THR A  1 118 ? 25.16400  -7.25200  16.11800 1.000 16.69862  ? 218 THR A N   1 
ATOM   885  C  CA  . THR A  1 118 ? 24.00400  -7.19500  15.23700 1.000 15.86728  ? 218 THR A CA  1 
ATOM   886  C  C   . THR A  1 118 ? 24.23700  -8.08700  14.02900 1.000 17.78496  ? 218 THR A C   1 
ATOM   887  O  O   . THR A  1 118 ? 25.29300  -8.01200  13.39500 1.000 20.35630  ? 218 THR A O   1 
ATOM   888  C  CB  . THR A  1 118 ? 23.72500  -5.76600  14.77800 1.000 17.82616  ? 218 THR A CB  1 
ATOM   889  O  OG1 . THR A  1 118 ? 23.47800  -4.95100  15.92500 1.000 20.90886  ? 218 THR A OG1 1 
ATOM   890  C  CG2 . THR A  1 118 ? 22.49200  -5.73400  13.86300 1.000 16.55865  ? 218 THR A CG2 1 
ATOM   891  N  N   . ILE A  1 119 ? 23.26200  -8.93700  13.73300 1.000 17.74671  ? 219 ILE A N   1 
ATOM   892  C  CA  . ILE A  1 119 ? 23.28000  -9.78800  12.54600 1.000 18.96580  ? 219 ILE A CA  1 
ATOM   893  C  C   . ILE A  1 119 ? 22.35500  -9.18300  11.50500 1.000 21.69504  ? 219 ILE A C   1 
ATOM   894  O  O   . ILE A  1 119 ? 21.25300  -8.72800  11.83700 1.000 19.71249  ? 219 ILE A O   1 
ATOM   895  C  CB  . ILE A  1 119 ? 22.83700  -11.21900 12.89600 1.000 18.74544  ? 219 ILE A CB  1 
ATOM   896  C  CG1 . ILE A  1 119 ? 23.69600  -11.78200 14.02200 1.000 21.26222  ? 219 ILE A CG1 1 
ATOM   897  C  CG2 . ILE A  1 119 ? 22.88700  -12.12300 11.65200 1.000 18.92570  ? 219 ILE A CG2 1 
ATOM   898  C  CD1 . ILE A  1 119 ? 23.05500  -13.01400 14.65500 1.000 22.31695  ? 219 ILE A CD1 1 
ATOM   899  N  N   . ILE A  1 120 ? 22.78600  -9.19000  10.23600 1.000 17.96620  ? 220 ILE A N   1 
ATOM   900  C  CA  . ILE A  1 120 ? 21.97900  -8.67400  9.13400  1.000 18.23215  ? 220 ILE A CA  1 
ATOM   901  C  C   . ILE A  1 120 ? 21.89900  -9.74400  8.05600  1.000 20.64101  ? 220 ILE A C   1 
ATOM   902  O  O   . ILE A  1 120 ? 22.91800  -10.34000 7.69200  1.000 19.84354  ? 220 ILE A O   1 
ATOM   903  C  CB  . ILE A  1 120 ? 22.54900  -7.37100  8.52900  1.000 18.14911  ? 220 ILE A CB  1 
ATOM   904  C  CG1 . ILE A  1 120 ? 23.01300  -6.39800  9.61400  1.000 21.10027  ? 220 ILE A CG1 1 
ATOM   905  C  CG2 . ILE A  1 120 ? 21.47600  -6.70100  7.63600  1.000 20.35829  ? 220 ILE A CG2 1 
ATOM   906  C  CD1 . ILE A  1 120 ? 24.50500  -6.57100  10.03300 1.000 21.21782  ? 220 ILE A CD1 1 
ATOM   907  N  N   . VAL A  1 121 ? 20.69300  -9.98900  7.54300  1.000 20.03725  ? 221 VAL A N   1 
ATOM   908  C  CA  . VAL A  1 121 ? 20.51000  -10.77600 6.32500  1.000 19.38260  ? 221 VAL A CA  1 
ATOM   909  C  C   . VAL A  1 121 ? 20.10600  -9.81400  5.21700  1.000 21.14152  ? 221 VAL A C   1 
ATOM   910  O  O   . VAL A  1 121 ? 19.15200  -9.04400  5.37300  1.000 19.29632  ? 221 VAL A O   1 
ATOM   911  C  CB  . VAL A  1 121 ? 19.46100  -11.89100 6.49900  1.000 20.71417  ? 221 VAL A CB  1 
ATOM   912  C  CG1 . VAL A  1 121 ? 19.36000  -12.75500 5.22300  1.000 25.17612  ? 221 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A  1 121 ? 19.78100  -12.76100 7.73100  1.000 20.90054  ? 221 VAL A CG2 1 
ATOM   914  N  N   . SER A  1 122 ? 20.84200  -9.84900  4.10100  1.000 20.22105  ? 222 SER A N   1 
ATOM   915  C  CA  . SER A  1 122 ? 20.52900  -9.00000  2.95600  1.000 22.20689  ? 222 SER A CA  1 
ATOM   916  C  C   . SER A  1 122 ? 19.28100  -9.48000  2.21400  1.000 24.34825  ? 222 SER A C   1 
ATOM   917  O  O   . SER A  1 122 ? 19.16600  -10.65700 1.86100  1.000 25.91593  ? 222 SER A O   1 
ATOM   918  C  CB  . SER A  1 122 ? 21.70800  -8.97200  1.97900  1.000 23.16637  ? 222 SER A CB  1 
ATOM   919  O  OG  . SER A  1 122 ? 21.30200  -8.38500  0.75200  1.000 25.20065  ? 222 SER A OG  1 
ATOM   920  N  N   . GLU A  1 123 ? 18.36600  -8.55000  1.92500  1.000 23.46327  ? 223 GLU A N   1 
ATOM   921  C  CA  . GLU A  1 123 ? 17.18300  -8.88500  1.13900  1.000 26.89158  ? 223 GLU A CA  1 
ATOM   922  C  C   . GLU A  1 123 ? 17.49600  -9.06200  -0.33900 1.000 29.98293  ? 223 GLU A C   1 
ATOM   923  O  O   . GLU A  1 123 ? 16.62400  -9.51500  -1.09400 1.000 31.71074  ? 223 GLU A O   1 
ATOM   924  C  CB  . GLU A  1 123 ? 16.10900  -7.80300  1.32300  1.000 29.19676  ? 223 GLU A CB  1 
ATOM   925  C  CG  . GLU A  1 123 ? 16.47500  -6.44300  0.71800  1.000 29.75080  ? 223 GLU A CG  1 
ATOM   926  C  CD  . GLU A  1 123 ? 15.35900  -5.40600  0.84600  1.000 46.19810  ? 223 GLU A CD  1 
ATOM   927  O  OE1 . GLU A  1 123 ? 14.65100  -5.39400  1.87700  1.000 42.12062  ? 223 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A  1 123 ? 15.19400  -4.60200  -0.09500 1.000 61.79541  ? 223 GLU A OE2 1 
ATOM   929  N  N   . GLU A  1 124 ? 18.71100  -8.71900  -0.76800 1.000 27.91287  ? 224 GLU A N   1 
ATOM   930  C  CA  . GLU A  1 124 ? 19.11800  -8.84600  -2.16000 1.000 30.90551  ? 224 GLU A CA  1 
ATOM   931  C  C   . GLU A  1 124 ? 19.83400  -10.15600 -2.44500 1.000 32.09811  ? 224 GLU A C   1 
ATOM   932  O  O   . GLU A  1 124 ? 19.57400  -10.79000 -3.47400 1.000 30.31155  ? 224 GLU A O   1 
ATOM   933  C  CB  . GLU A  1 124 ? 20.03200  -7.67900  -2.55500 1.000 35.52185  ? 224 GLU A CB  1 
ATOM   934  C  CG  . GLU A  1 124 ? 19.46400  -6.30300  -2.24700 1.000 43.31118  ? 224 GLU A CG  1 
ATOM   935  C  CD  . GLU A  1 124 ? 18.39500  -5.88000  -3.23700 1.000 61.04158  ? 224 GLU A CD  1 
ATOM   936  O  OE1 . GLU A  1 124 ? 18.62200  -6.03000  -4.45700 1.000 67.89924  ? 224 GLU A OE1 1 
ATOM   937  O  OE2 . GLU A  1 124 ? 17.32500  -5.40800  -2.79500 1.000 62.91823  ? 224 GLU A OE2 1 
ATOM   938  N  N   . THR A  1 125 ? 20.74200  -10.57200 -1.56300 1.000 26.61570  ? 225 THR A N   1 
ATOM   939  C  CA  . THR A  1 125 ? 21.58600  -11.73500 -1.80700 1.000 24.90670  ? 225 THR A CA  1 
ATOM   940  C  C   . THR A  1 125 ? 21.37800  -12.86600 -0.81700 1.000 24.70134  ? 225 THR A C   1 
ATOM   941  O  O   . THR A  1 125 ? 21.85900  -13.97800 -1.07100 1.000 25.62147  ? 225 THR A O   1 
ATOM   942  C  CB  . THR A  1 125 ? 23.07400  -11.35100 -1.75300 1.000 28.01312  ? 225 THR A CB  1 
ATOM   943  O  OG1 . THR A  1 125 ? 23.39300  -10.90500 -0.42900 1.000 28.41437  ? 225 THR A OG1 1 
ATOM   944  C  CG2 . THR A  1 125 ? 23.40600  -10.25700 -2.76600 1.000 25.26653  ? 225 THR A CG2 1 
ATOM   945  N  N   . GLY A  1 126 ? 20.71700  -12.61500 0.31200  1.000 23.26048  ? 226 GLY A N   1 
ATOM   946  C  CA  . GLY A  1 126 ? 20.77000  -13.57300 1.39300  1.000 23.95650  ? 226 GLY A CA  1 
ATOM   947  C  C   . GLY A  1 126 ? 22.09000  -13.60900 2.12800  1.000 25.27594  ? 226 GLY A C   1 
ATOM   948  O  O   . GLY A  1 126 ? 22.26200  -14.45100 3.01500  1.000 22.10695  ? 226 GLY A O   1 
ATOM   949  N  N   . GLY A  1 127 ? 23.02500  -12.71700 1.80000  1.000 23.61496  ? 227 GLY A N   1 
ATOM   950  C  CA  . GLY A  1 127 ? 24.29100  -12.68800 2.51500  1.000 23.22949  ? 227 GLY A CA  1 
ATOM   951  C  C   . GLY A  1 127 ? 24.09000  -12.29400 3.96900  1.000 25.03583  ? 227 GLY A C   1 
ATOM   952  O  O   . GLY A  1 127 ? 23.23800  -11.47100 4.30000  1.000 24.33165  ? 227 GLY A O   1 
ATOM   953  N  N   . VAL A  1 128 ? 24.88600  -12.89200 4.85200  1.000 20.23879  ? 228 VAL A N   1 
ATOM   954  C  CA  . VAL A  1 128 ? 24.78900  -12.64600 6.28400  1.000 19.19116  ? 228 VAL A CA  1 
ATOM   955  C  C   . VAL A  1 128 ? 26.00000  -11.82900 6.70500  1.000 22.26848  ? 228 VAL A C   1 
ATOM   956  O  O   . VAL A  1 128 ? 27.13200  -12.16000 6.34100  1.000 25.03636  ? 228 VAL A O   1 
ATOM   957  C  CB  . VAL A  1 128 ? 24.70700  -13.96200 7.07700  1.000 20.61073  ? 228 VAL A CB  1 
ATOM   958  C  CG1 . VAL A  1 128 ? 24.63800  -13.68200 8.60400  1.000 18.06456  ? 228 VAL A CG1 1 
ATOM   959  C  CG2 . VAL A  1 128 ? 23.51400  -14.80000 6.60300  1.000 22.64966  ? 228 VAL A CG2 1 
ATOM   960  N  N   . SER A  1 129 ? 25.76600  -10.76800 7.47500  1.000 19.25306  ? 229 SER A N   1 
ATOM   961  C  CA  . SER A  1 129 ? 26.84500  -9.93100  7.98100  1.000 19.98973  ? 229 SER A CA  1 
ATOM   962  C  C   . SER A  1 129 ? 26.60600  -9.66300  9.45300  1.000 18.66956  ? 229 SER A C   1 
ATOM   963  O  O   . SER A  1 129 ? 25.52000  -9.90800  9.97900  1.000 19.57951  ? 229 SER A O   1 
ATOM   964  C  CB  . SER A  1 129 ? 26.95400  -8.59300  7.24900  1.000 23.51453  ? 229 SER A CB  1 
ATOM   965  O  OG  . SER A  1 129 ? 25.68000  -8.00700  7.06900  1.000 28.01291  ? 229 SER A OG  1 
ATOM   966  N  N   . VAL A  1 130 ? 27.65200  -9.17800  10.11500 1.000 18.75205  ? 230 VAL A N   1 
ATOM   967  C  CA  . VAL A  1 130 ? 27.60200  -8.86200  11.53800 1.000 20.51030  ? 230 VAL A CA  1 
ATOM   968  C  C   . VAL A  1 130 ? 28.27100  -7.51500  11.75400 1.000 21.93051  ? 230 VAL A C   1 
ATOM   969  O  O   . VAL A  1 130 ? 29.35500  -7.26700  11.21800 1.000 21.68166  ? 230 VAL A O   1 
ATOM   970  C  CB  . VAL A  1 130 ? 28.28700  -9.94700  12.39600 1.000 21.51282  ? 230 VAL A CB  1 
ATOM   971  C  CG1 . VAL A  1 130 ? 28.65000  -9.38100  13.77400 1.000 19.56946  ? 230 VAL A CG1 1 
ATOM   972  C  CG2 . VAL A  1 130 ? 27.35500  -11.13800 12.54600 1.000 19.93537  ? 230 VAL A CG2 1 
ATOM   973  N  N   . ALA A  1 131 ? 27.62200  -6.64100  12.52500 1.000 20.48658  ? 231 ALA A N   1 
ATOM   974  C  CA  . ALA A  1 131 ? 28.18500  -5.35100  12.89800 1.000 20.19140  ? 231 ALA A CA  1 
ATOM   975  C  C   . ALA A  1 131 ? 28.60300  -5.41500  14.36000 1.000 21.12727  ? 231 ALA A C   1 
ATOM   976  O  O   . ALA A  1 131 ? 27.82600  -5.85600  15.21500 1.000 19.38273  ? 231 ALA A O   1 
ATOM   977  C  CB  . ALA A  1 131 ? 27.17800  -4.21400  12.67200 1.000 18.58980  ? 231 ALA A CB  1 
ATOM   978  N  N   . LYS A  1 132 ? 29.83900  -5.01200  14.62900 1.000 20.04162  ? 232 LYS A N   1 
ATOM   979  C  CA  . LYS A  1 132 ? 30.40500  -5.04700  15.97200 1.000 22.68775  ? 232 LYS A CA  1 
ATOM   980  C  C   . LYS A  1 132 ? 31.44400  -3.93900  16.03300 1.000 20.65568  ? 232 LYS A C   1 
ATOM   981  O  O   . LYS A  1 132 ? 32.29800  -3.86000  15.14700 1.000 19.32534  ? 232 LYS A O   1 
ATOM   982  C  CB  . LYS A  1 132 ? 31.03600  -6.41400  16.26200 1.000 23.51683  ? 232 LYS A CB  1 
ATOM   983  C  CG  . LYS A  1 132 ? 31.80500  -6.49300  17.57300 1.000 25.50139  ? 232 LYS A CG  1 
ATOM   984  C  CD  . LYS A  1 132 ? 30.83900  -6.57600  18.74600 1.000 24.98032  ? 232 LYS A CD  1 
ATOM   985  C  CE  . LYS A  1 132 ? 31.61800  -6.59300  20.06400 1.000 36.91313  ? 232 LYS A CE  1 
ATOM   986  N  NZ  . LYS A  1 132 ? 30.76400  -7.02400  21.20900 1.000 46.62452  ? 232 LYS A NZ  1 
ATOM   987  N  N   . ASN A  1 133 ? 31.33300  -3.05600  17.02700 1.000 21.74433  ? 233 ASN A N   1 
ATOM   988  C  CA  . ASN A  1 133 ? 32.32200  -1.99400  17.25300 1.000 23.48027  ? 233 ASN A CA  1 
ATOM   989  C  C   . ASN A  1 133 ? 32.52700  -1.11400  16.02300 1.000 26.35751  ? 233 ASN A C   1 
ATOM   990  O  O   . ASN A  1 133 ? 33.63400  -0.64200  15.75400 1.000 24.83039  ? 233 ASN A O   1 
ATOM   991  C  CB  . ASN A  1 133 ? 33.67000  -2.56900  17.70300 1.000 21.79774  ? 233 ASN A CB  1 
ATOM   992  C  CG  . ASN A  1 133 ? 33.62500  -3.15000  19.09600 1.000 28.23809  ? 233 ASN A CG  1 
ATOM   993  O  OD1 . ASN A  1 133 ? 32.82200  -2.73600  19.92200 1.000 28.61419  ? 233 ASN A OD1 1 
ATOM   994  N  ND2 . ASN A  1 133 ? 34.47500  -4.12800  19.35300 1.000 27.73816  ? 233 ASN A ND2 1 
ATOM   995  N  N   . GLY A  1 134 ? 31.46500  -0.90100  15.25300 1.000 25.23159  ? 234 GLY A N   1 
ATOM   996  C  CA  . GLY A  1 134 ? 31.54800  -0.03400  14.10000 1.000 22.02702  ? 234 GLY A CA  1 
ATOM   997  C  C   . GLY A  1 134 ? 32.03300  -0.69000  12.83100 1.000 27.12325  ? 234 GLY A C   1 
ATOM   998  O  O   . GLY A  1 134 ? 32.04200  -0.03800  11.78500 1.000 26.91568  ? 234 GLY A O   1 
ATOM   999  N  N   A ASP A  1 135 ? 32.43300  -1.95300  12.88000 0.462 25.62160  ? 235 ASP A N   1 
ATOM   1000 N  N   B ASP A  1 135 ? 32.45500  -1.94800  12.88900 0.538 25.65185  ? 235 ASP A N   1 
ATOM   1001 C  CA  A ASP A  1 135 ? 32.92200  -2.66300  11.71200 0.462 24.65860  ? 235 ASP A CA  1 
ATOM   1002 C  CA  B ASP A  1 135 ? 32.91900  -2.69200  11.72900 0.538 24.66120  ? 235 ASP A CA  1 
ATOM   1003 C  C   A ASP A  1 135 ? 31.86300  -3.65100  11.24600 0.462 25.12741  ? 235 ASP A C   1 
ATOM   1004 C  C   B ASP A  1 135 ? 31.81800  -3.61800  11.24200 0.538 25.15106  ? 235 ASP A C   1 
ATOM   1005 O  O   A ASP A  1 135 ? 31.12000  -4.21200  12.05600 0.462 21.39801  ? 235 ASP A O   1 
ATOM   1006 O  O   B ASP A  1 135 ? 31.02300  -4.12800  12.03400 0.538 21.42369  ? 235 ASP A O   1 
ATOM   1007 C  CB  A ASP A  1 135 ? 34.23400  -3.39500  12.02100 0.462 28.77068  ? 235 ASP A CB  1 
ATOM   1008 C  CB  B ASP A  1 135 ? 34.15800  -3.52600  12.06200 0.538 28.77304  ? 235 ASP A CB  1 
ATOM   1009 C  CG  A ASP A  1 135 ? 35.16500  -3.44400  10.82900 0.462 29.70480  ? 235 ASP A CG  1 
ATOM   1010 C  CG  B ASP A  1 135 ? 35.44800  -2.78700  11.80700 0.538 32.50928  ? 235 ASP A CG  1 
ATOM   1011 O  OD1 A ASP A  1 135 ? 34.73700  -3.02900  9.73300  0.462 36.18738  ? 235 ASP A OD1 1 
ATOM   1012 O  OD1 B ASP A  1 135 ? 35.40400  -1.65300  11.28400 0.538 36.66662  ? 235 ASP A OD1 1 
ATOM   1013 O  OD2 A ASP A  1 135 ? 36.32400  -3.88600  10.98700 0.462 30.69594  ? 235 ASP A OD2 1 
ATOM   1014 O  OD2 B ASP A  1 135 ? 36.51100  -3.35700  12.12600 0.538 28.50454  ? 235 ASP A OD2 1 
ATOM   1015 N  N   . LEU A  1 136 ? 31.79400  -3.84800  9.93200  1.000 22.80836  ? 236 LEU A N   1 
ATOM   1016 C  CA  . LEU A  1 136 ? 30.79600  -4.70800  9.30700  1.000 21.55360  ? 236 LEU A CA  1 
ATOM   1017 C  C   . LEU A  1 136 ? 31.51500  -5.86100  8.62900  1.000 25.99883  ? 236 LEU A C   1 
ATOM   1018 O  O   . LEU A  1 136 ? 32.34900  -5.64100  7.73800  1.000 27.72102  ? 236 LEU A O   1 
ATOM   1019 C  CB  . LEU A  1 136 ? 29.95500  -3.92200  8.30100  1.000 25.69923  ? 236 LEU A CB  1 
ATOM   1020 C  CG  . LEU A  1 136 ? 28.78900  -4.66200  7.63300  1.000 25.56304  ? 236 LEU A CG  1 
ATOM   1021 C  CD1 . LEU A  1 136 ? 27.66800  -4.99400  8.60700  1.000 20.97581  ? 236 LEU A CD1 1 
ATOM   1022 C  CD2 . LEU A  1 136 ? 28.26100  -3.81100  6.49900  1.000 27.42088  ? 236 LEU A CD2 1 
ATOM   1023 N  N   . HIS A  1 137 ? 31.20300  -7.08000  9.06500  1.000 23.07081  ? 237 HIS A N   1 
ATOM   1024 C  CA  . HIS A  1 137 ? 31.84100  -8.29900  8.57600  1.000 25.84063  ? 237 HIS A CA  1 
ATOM   1025 C  C   . HIS A  1 137 ? 30.89100  -8.99800  7.61300  1.000 23.19382  ? 237 HIS A C   1 
ATOM   1026 O  O   . HIS A  1 137 ? 29.86200  -9.53300  8.03000  1.000 22.33171  ? 237 HIS A O   1 
ATOM   1027 C  CB  . HIS A  1 137 ? 32.21200  -9.19400  9.75300  1.000 23.89624  ? 237 HIS A CB  1 
ATOM   1028 C  CG  . HIS A  1 137 ? 33.08800  -8.50900  10.75000 1.000 26.02661  ? 237 HIS A CG  1 
ATOM   1029 N  ND1 . HIS A  1 137 ? 34.44000  -8.33600  10.54600 1.000 29.85302  ? 237 HIS A ND1 1 
ATOM   1030 C  CD2 . HIS A  1 137 ? 32.80300  -7.90900  11.93000 1.000 24.09357  ? 237 HIS A CD2 1 
ATOM   1031 C  CE1 . HIS A  1 137 ? 34.95600  -7.68200  11.57200 1.000 30.15675  ? 237 HIS A CE1 1 
ATOM   1032 N  NE2 . HIS A  1 137 ? 33.98700  -7.41600  12.42900 1.000 24.45820  ? 237 HIS A NE2 1 
ATOM   1033 N  N   . ARG A  1 138 ? 31.23700  -9.00500  6.32800  1.000 22.61839  ? 238 ARG A N   1 
ATOM   1034 C  CA  . ARG A  1 138 ? 30.27400  -9.37800  5.29900  1.000 27.96033  ? 238 ARG A CA  1 
ATOM   1035 C  C   . ARG A  1 138 ? 30.45800  -10.82300 4.83000  1.000 28.23001  ? 238 ARG A C   1 
ATOM   1036 O  O   . ARG A  1 138 ? 31.50200  -11.44800 5.04400  1.000 27.85804  ? 238 ARG A O   1 
ATOM   1037 C  CB  . ARG A  1 138 ? 30.37300  -8.42300  4.10200  1.000 32.76532  ? 238 ARG A CB  1 
ATOM   1038 C  CG  . ARG A  1 138 ? 30.15200  -6.94900  4.45300  1.000 35.38192  ? 238 ARG A CG  1 
ATOM   1039 C  CD  . ARG A  1 138 ? 29.87800  -6.13300  3.21100  1.000 49.21288  ? 238 ARG A CD  1 
ATOM   1040 N  NE  . ARG A  1 138 ? 28.80100  -6.75200  2.44700  1.000 45.22935  ? 238 ARG A NE  1 
ATOM   1041 C  CZ  . ARG A  1 138 ? 28.55200  -6.53200  1.16500  1.000 60.38927  ? 238 ARG A CZ  1 
ATOM   1042 N  NH1 . ARG A  1 138 ? 29.27200  -5.67500  0.45700  1.000 59.49662  ? 238 ARG A NH1 1 
ATOM   1043 N  NH2 . ARG A  1 138 ? 27.56200  -7.19800  0.57500  1.000 52.30923  ? 238 ARG A NH2 1 
ATOM   1044 N  N   . GLU A  1 139 ? 29.40600  -11.33700 4.18400  1.000 26.22767  ? 239 GLU A N   1 
ATOM   1045 C  CA  . GLU A  1 139 ? 29.38100  -12.64800 3.52200  1.000 26.21464  ? 239 GLU A CA  1 
ATOM   1046 C  C   . GLU A  1 139 ? 29.86800  -13.76200 4.44400  1.000 26.37601  ? 239 GLU A C   1 
ATOM   1047 O  O   . GLU A  1 139 ? 30.72300  -14.57600 4.08600  1.000 33.22101  ? 239 GLU A O   1 
ATOM   1048 C  CB  . GLU A  1 139 ? 30.19400  -12.62300 2.22600  1.000 29.61122  ? 239 GLU A CB  1 
ATOM   1049 C  CG  . GLU A  1 139 ? 29.72900  -11.56100 1.25200  1.000 31.08114  ? 239 GLU A CG  1 
ATOM   1050 C  CD  . GLU A  1 139 ? 30.55900  -11.52600 -0.02100 1.000 38.48151  ? 239 GLU A CD  1 
ATOM   1051 O  OE1 . GLU A  1 139 ? 31.73900  -11.13600 0.04600  1.000 48.39172  ? 239 GLU A OE1 1 
ATOM   1052 O  OE2 . GLU A  1 139 ? 30.02600  -11.90100 -1.08100 1.000 45.66746  ? 239 GLU A OE2 1 
ATOM   1053 N  N   . LEU A  1 140 ? 29.30000  -13.80500 5.64200  1.000 23.45080  ? 240 LEU A N   1 
ATOM   1054 C  CA  . LEU A  1 140 ? 29.74100  -14.75500 6.64600  1.000 25.94769  ? 240 LEU A CA  1 
ATOM   1055 C  C   . LEU A  1 140 ? 29.26600  -16.16200 6.32300  1.000 26.59506  ? 240 LEU A C   1 
ATOM   1056 O  O   . LEU A  1 140 ? 28.15100  -16.36600 5.83600  1.000 29.62865  ? 240 LEU A O   1 
ATOM   1057 C  CB  . LEU A  1 140 ? 29.21900  -14.34200 8.02100  1.000 24.41445  ? 240 LEU A CB  1 
ATOM   1058 C  CG  . LEU A  1 140 ? 29.73800  -13.00300 8.54100  1.000 26.33516  ? 240 LEU A CG  1 
ATOM   1059 C  CD1 . LEU A  1 140 ? 28.98700  -12.63000 9.79600  1.000 20.41878  ? 240 LEU A CD1 1 
ATOM   1060 C  CD2 . LEU A  1 140 ? 31.23500  -13.08400 8.81600  1.000 29.41636  ? 240 LEU A CD2 1 
ATOM   1061 N  N   . THR A  1 141 ? 30.12600  -17.13600 6.60500  1.000 30.03190  ? 241 THR A N   1 
ATOM   1062 C  CA  . THR A  1 141 ? 29.72800  -18.53000 6.56700  1.000 29.58588  ? 241 THR A CA  1 
ATOM   1063 C  C   . THR A  1 141 ? 28.94900  -18.87000 7.82700  1.000 31.45520  ? 241 THR A C   1 
ATOM   1064 O  O   . THR A  1 141 ? 28.98400  -18.14000 8.82200  1.000 30.70053  ? 241 THR A O   1 
ATOM   1065 C  CB  . THR A  1 141 ? 30.95200  -19.43800 6.45700  1.000 34.78525  ? 241 THR A CB  1 
ATOM   1066 O  OG1 . THR A  1 141 ? 31.77600  -19.26800 7.62200  1.000 31.10417  ? 241 THR A OG1 1 
ATOM   1067 C  CG2 . THR A  1 141 ? 31.76100  -19.07800 5.22400  1.000 32.75587  ? 241 THR A CG2 1 
ATOM   1068 N  N   . GLU A  1 142 ? 28.25300  -20.00400 7.78600  1.000 30.21500  ? 242 GLU A N   1 
ATOM   1069 C  CA  . GLU A  1 142 ? 27.57600  -20.48800 8.98400  1.000 32.30740  ? 242 GLU A CA  1 
ATOM   1070 C  C   . GLU A  1 142 ? 28.57000  -20.70500 10.12000 1.000 38.97451  ? 242 GLU A C   1 
ATOM   1071 O  O   . GLU A  1 142 ? 28.29400  -20.35900 11.27500 1.000 30.26757  ? 242 GLU A O   1 
ATOM   1072 C  CB  . GLU A  1 142 ? 26.81200  -21.77900 8.67600  1.000 37.20438  ? 242 GLU A CB  1 
ATOM   1073 C  CG  . GLU A  1 142 ? 26.23900  -22.44200 9.92500  1.000 53.57930  ? 242 GLU A CG  1 
ATOM   1074 C  CD  . GLU A  1 142 ? 25.21200  -23.51700 9.62200  1.000 65.99350  ? 242 GLU A CD  1 
ATOM   1075 O  OE1 . GLU A  1 142 ? 25.24300  -24.08700 8.50900  1.000 70.46084  ? 242 GLU A OE1 1 
ATOM   1076 O  OE2 . GLU A  1 142 ? 24.36800  -23.78500 10.50600 1.000 58.68769  ? 242 GLU A OE2 1 
ATOM   1077 N  N   . GLU A  1 143 ? 29.74400  -21.25400 9.80200  1.000 33.59620  ? 243 GLU A N   1 
ATOM   1078 C  CA  . GLU A  1 143 ? 30.76200  -21.48700 10.82500 1.000 40.06835  ? 243 GLU A CA  1 
ATOM   1079 C  C   . GLU A  1 143 ? 31.22400  -20.18000 11.45800 1.000 32.86091  ? 243 GLU A C   1 
ATOM   1080 O  O   . GLU A  1 143 ? 31.40600  -20.10600 12.67800 1.000 34.34408  ? 243 GLU A O   1 
ATOM   1081 C  CB  . GLU A  1 143 ? 31.95100  -22.24000 10.22000 1.000 42.41521  ? 243 GLU A CB  1 
ATOM   1082 C  CG  . GLU A  1 143 ? 33.23800  -22.14500 11.03500 1.000 48.34041  ? 243 GLU A CG  1 
ATOM   1083 C  CD  . GLU A  1 143 ? 34.40400  -22.91200 10.41800 1.000 65.83275  ? 243 GLU A CD  1 
ATOM   1084 O  OE1 . GLU A  1 143 ? 34.83600  -22.56500 9.29500  1.000 56.41503  ? 243 GLU A OE1 1 
ATOM   1085 O  OE2 . GLU A  1 143 ? 34.89300  -23.86500 11.06400 1.000 65.94393  ? 243 GLU A OE2 1 
ATOM   1086 N  N   . ALA A  1 144 ? 31.42700  -19.13800 10.64500 1.000 32.17646  ? 244 ALA A N   1 
ATOM   1087 C  CA  . ALA A  1 144 ? 31.92800  -17.87500 11.18200 1.000 30.80191  ? 244 ALA A CA  1 
ATOM   1088 C  C   . ALA A  1 144 ? 30.89000  -17.20500 12.08000 1.000 30.36287  ? 244 ALA A C   1 
ATOM   1089 O  O   . ALA A  1 144 ? 31.23600  -16.66900 13.13800 1.000 26.67833  ? 244 ALA A O   1 
ATOM   1090 C  CB  . ALA A  1 144 ? 32.34700  -16.94100 10.04800 1.000 31.53105  ? 244 ALA A CB  1 
ATOM   1091 N  N   . LEU A  1 145 ? 29.61600  -17.22700 11.67700 1.000 25.43836  ? 245 LEU A N   1 
ATOM   1092 C  CA  . LEU A  1 145 ? 28.55200  -16.68000 12.52000 1.000 25.02795  ? 245 LEU A CA  1 
ATOM   1093 C  C   . LEU A  1 145 ? 28.47900  -17.39000 13.86900 1.000 25.49977  ? 245 LEU A C   1 
ATOM   1094 O  O   . LEU A  1 145 ? 28.35600  -16.74200 14.91700 1.000 26.93227  ? 245 LEU A O   1 
ATOM   1095 C  CB  . LEU A  1 145 ? 27.20700  -16.78700 11.79900 1.000 22.72613  ? 245 LEU A CB  1 
ATOM   1096 C  CG  . LEU A  1 145 ? 26.01400  -16.32300 12.63800 1.000 22.57075  ? 245 LEU A CG  1 
ATOM   1097 C  CD1 . LEU A  1 145 ? 26.17500  -14.85100 13.02600 1.000 27.30120  ? 245 LEU A CD1 1 
ATOM   1098 C  CD2 . LEU A  1 145 ? 24.69500  -16.55300 11.89600 1.000 22.75600  ? 245 LEU A CD2 1 
ATOM   1099 N  N   . LYS A  1 146 ? 28.55000  -18.72200 13.86400 1.000 27.98740  ? 246 LYS A N   1 
ATOM   1100 C  CA  . LYS A  1 146 ? 28.48600  -19.47000 15.11400 1.000 29.04792  ? 246 LYS A CA  1 
ATOM   1101 C  C   . LYS A  1 146 ? 29.67100  -19.13200 16.01100 1.000 32.12682  ? 246 LYS A C   1 
ATOM   1102 O  O   . LYS A  1 146 ? 29.51400  -18.98600 17.22700 1.000 30.32799  ? 246 LYS A O   1 
ATOM   1103 C  CB  . LYS A  1 146 ? 28.44800  -20.97000 14.82900 1.000 31.13768  ? 246 LYS A CB  1 
ATOM   1104 C  CG  . LYS A  1 146 ? 28.24500  -21.82900 16.07100 1.000 52.91076  ? 246 LYS A CG  1 
ATOM   1105 C  CD  . LYS A  1 146 ? 28.46300  -23.30700 15.76900 1.000 70.68239  ? 246 LYS A CD  1 
ATOM   1106 C  CE  . LYS A  1 146 ? 28.28100  -24.17100 17.01300 1.000 74.76992  ? 246 LYS A CE  1 
ATOM   1107 N  NZ  . LYS A  1 146 ? 26.87700  -24.14400 17.51900 1.000 59.71592  ? 246 LYS A NZ  1 
ATOM   1108 N  N   . GLU A  1 147 ? 30.86200  -18.99100 15.42700 1.000 27.76891  ? 247 GLU A N   1 
ATOM   1109 C  CA  . GLU A  1 147 ? 32.02900  -18.64300 16.23600 1.000 29.14355  ? 247 GLU A CA  1 
ATOM   1110 C  C   . GLU A  1 147 ? 31.87100  -17.26100 16.85100 1.000 32.44183  ? 247 GLU A C   1 
ATOM   1111 O  O   . GLU A  1 147 ? 32.24000  -17.04100 18.01500 1.000 30.34038  ? 247 GLU A O   1 
ATOM   1112 C  CB  . GLU A  1 147 ? 33.29700  -18.70100 15.39300 1.000 37.57176  ? 247 GLU A CB  1 
ATOM   1113 C  CG  . GLU A  1 147 ? 33.65000  -20.07800 14.89000 1.000 42.57962  ? 247 GLU A CG  1 
ATOM   1114 C  CD  . GLU A  1 147 ? 35.05100  -20.12700 14.32600 1.000 63.50977  ? 247 GLU A CD  1 
ATOM   1115 O  OE1 . GLU A  1 147 ? 35.72600  -19.07200 14.33100 1.000 51.96685  ? 247 GLU A OE1 1 
ATOM   1116 O  OE2 . GLU A  1 147 ? 35.47700  -21.21700 13.88300 1.000 75.32488  ? 247 GLU A OE2 1 
ATOM   1117 N  N   . MET A  1 148 ? 31.32300  -16.31800 16.07900 1.000 30.44908  ? 248 MET A N   1 
ATOM   1118 C  CA  . MET A  1 148 ? 31.05600  -14.97800 16.59100 1.000 26.94393  ? 248 MET A CA  1 
ATOM   1119 C  C   . MET A  1 148 ? 30.05900  -15.01200 17.74600 1.000 27.41572  ? 248 MET A C   1 
ATOM   1120 O  O   . MET A  1 148 ? 30.27200  -14.37100 18.78000 1.000 30.09825  ? 248 MET A O   1 
ATOM   1121 C  CB  . MET A  1 148 ? 30.54400  -14.07700 15.46500 1.000 28.41279  ? 248 MET A CB  1 
ATOM   1122 C  CG  . MET A  1 148 ? 31.62000  -13.70800 14.43400 1.000 28.50851  ? 248 MET A CG  1 
ATOM   1123 S  SD  . MET A  1 148 ? 30.91700  -12.66300 13.13700 1.000 29.51489  ? 248 MET A SD  1 
ATOM   1124 C  CE  . MET A  1 148 ? 32.38000  -12.20100 12.22700 1.000 25.23527  ? 248 MET A CE  1 
ATOM   1125 N  N   . LEU A  1 149 ? 28.95800  -15.75300 17.58700 1.000 26.90106  ? 249 LEU A N   1 
ATOM   1126 C  CA  . LEU A  1 149 ? 27.97800  -15.84100 18.66900 1.000 30.39859  ? 249 LEU A CA  1 
ATOM   1127 C  C   . LEU A  1 149 ? 28.56200  -16.53300 19.89300 1.000 32.72316  ? 249 LEU A C   1 
ATOM   1128 O  O   . LEU A  1 149 ? 28.26600  -16.14500 21.02900 1.000 32.46844  ? 249 LEU A O   1 
ATOM   1129 C  CB  . LEU A  1 149 ? 26.72000  -16.57000 18.19700 1.000 28.32393  ? 249 LEU A CB  1 
ATOM   1130 C  CG  . LEU A  1 149 ? 25.93700  -15.82600 17.11300 1.000 29.17576  ? 249 LEU A CG  1 
ATOM   1131 C  CD1 . LEU A  1 149 ? 24.82900  -16.70100 16.55300 1.000 29.37265  ? 249 LEU A CD1 1 
ATOM   1132 C  CD2 . LEU A  1 149 ? 25.36200  -14.53500 17.68000 1.000 32.51138  ? 249 LEU A CD2 1 
ATOM   1133 N  N   . GLU A  1 150 ? 29.38100  -17.56700 19.69000 1.000 30.16233  ? 250 GLU A N   1 
ATOM   1134 C  CA  . GLU A  1 150 ? 29.99500  -18.23800 20.83700 1.000 34.60324  ? 250 GLU A CA  1 
ATOM   1135 C  C   . GLU A  1 150 ? 30.98500  -17.32300 21.54100 1.000 35.37336  ? 250 GLU A C   1 
ATOM   1136 O  O   . GLU A  1 150 ? 31.04300  -17.29700 22.77700 1.000 36.51479  ? 250 GLU A O   1 
ATOM   1137 C  CB  . GLU A  1 150 ? 30.67700  -19.52900 20.39600 1.000 34.02792  ? 250 GLU A CB  1 
ATOM   1138 C  CG  . GLU A  1 150 ? 29.69900  -20.60800 19.98700 1.000 40.15326  ? 250 GLU A CG  1 
ATOM   1139 C  CD  . GLU A  1 150 ? 30.35700  -21.95400 19.79300 1.000 61.31127  ? 250 GLU A CD  1 
ATOM   1140 O  OE1 . GLU A  1 150 ? 31.60600  -22.01600 19.78300 1.000 67.22890  ? 250 GLU A OE1 1 
ATOM   1141 O  OE2 . GLU A  1 150 ? 29.62100  -22.95400 19.65500 1.000 69.19608  ? 250 GLU A OE2 1 
ATOM   1142 N  N   . ALA A  1 151 ? 31.77800  -16.57600 20.76900 1.000 38.06749  ? 251 ALA A N   1 
ATOM   1143 C  CA  . ALA A  1 151 ? 32.67100  -15.58400 21.35600 1.000 42.22787  ? 251 ALA A CA  1 
ATOM   1144 C  C   . ALA A  1 151 ? 31.88200  -14.54500 22.14000 1.000 44.04714  ? 251 ALA A C   1 
ATOM   1145 O  O   . ALA A  1 151 ? 32.30000  -14.11600 23.22300 1.000 47.79627  ? 251 ALA A O   1 
ATOM   1146 C  CB  . ALA A  1 151 ? 33.49200  -14.91300 20.25400 1.000 36.09104  ? 251 ALA A CB  1 
ATOM   1147 N  N   . GLU A  1 152 ? 30.72100  -14.15900 21.61700 1.000 41.68965  ? 252 GLU A N   1 
ATOM   1148 C  CA  . GLU A  1 152 ? 29.92300  -13.09500 22.21400 1.000 41.33652  ? 252 GLU A CA  1 
ATOM   1149 C  C   . GLU A  1 152 ? 29.21700  -13.56100 23.48400 1.000 51.28521  ? 252 GLU A C   1 
ATOM   1150 O  O   . GLU A  1 152 ? 29.11800  -12.80300 24.45700 1.000 52.76040  ? 252 GLU A O   1 
ATOM   1151 C  CB  . GLU A  1 152 ? 28.91500  -12.59700 21.18400 1.000 45.13762  ? 252 GLU A CB  1 
ATOM   1152 C  CG  . GLU A  1 152 ? 27.91600  -11.59600 21.69700 1.000 45.96378  ? 252 GLU A CG  1 
ATOM   1153 C  CD  . GLU A  1 152 ? 28.52600  -10.22900 21.87200 1.000 55.75429  ? 252 GLU A CD  1 
ATOM   1154 O  OE1 . GLU A  1 152 ? 29.56300  -9.95200  21.22200 1.000 47.73709  ? 252 GLU A OE1 1 
ATOM   1155 O  OE2 . GLU A  1 152 ? 27.97100  -9.43900  22.66800 1.000 70.06173  ? 252 GLU A OE2 1 
ATOM   1156 N  N   . PHE A  1 153 ? 28.70500  -14.79500 23.49300 1.000 43.31828  ? 253 PHE A N   1 
ATOM   1157 C  CA  . PHE A  1 153 ? 27.97300  -15.29800 24.65000 1.000 46.43802  ? 253 PHE A CA  1 
ATOM   1158 C  C   . PHE A  1 153 ? 28.88600  -15.80500 25.75800 1.000 53.81659  ? 253 PHE A C   1 
ATOM   1159 O  O   . PHE A  1 153 ? 28.39900  -16.06300 26.86300 1.000 63.37283  ? 253 PHE A O   1 
ATOM   1160 C  CB  . PHE A  1 153 ? 27.02100  -16.43000 24.24400 1.000 38.58826  ? 253 PHE A CB  1 
ATOM   1161 C  CG  . PHE A  1 153 ? 25.76600  -15.96700 23.53600 1.000 42.89817  ? 253 PHE A CG  1 
ATOM   1162 C  CD1 . PHE A  1 153 ? 25.82200  -15.03700 22.51000 1.000 49.52486  ? 253 PHE A CD1 1 
ATOM   1163 C  CD2 . PHE A  1 153 ? 24.53000  -16.49500 23.88300 1.000 53.35974  ? 253 PHE A CD2 1 
ATOM   1164 C  CE1 . PHE A  1 153 ? 24.67000  -14.63100 21.85500 1.000 50.87545  ? 253 PHE A CE1 1 
ATOM   1165 C  CE2 . PHE A  1 153 ? 23.37800  -16.09300 23.23200 1.000 58.92669  ? 253 PHE A CE2 1 
ATOM   1166 C  CZ  . PHE A  1 153 ? 23.45000  -15.16100 22.21300 1.000 41.78033  ? 253 PHE A CZ  1 
ATOM   1167 N  N   . LYS A  1 154 ? 30.18000  -15.96400 25.49400 1.000 57.92395  ? 254 LYS A N   1 
ATOM   1168 C  CA  . LYS A  1 154 ? 31.11600  -16.44500 26.50600 1.000 70.08002  ? 254 LYS A CA  1 
ATOM   1169 C  C   . LYS A  1 154 ? 31.44700  -15.34300 27.50800 1.000 73.20743  ? 254 LYS A C   1 
ATOM   1170 O  O   . LYS A  1 154 ? 30.59000  -14.53000 27.86000 1.000 67.54903  ? 254 LYS A O   1 
ATOM   1171 C  CB  . LYS A  1 154 ? 32.39900  -16.96200 25.85200 1.000 66.37803  ? 254 LYS A CB  1 
ATOM   1172 C  CG  . LYS A  1 154 ? 33.34600  -17.65400 26.81100 1.000 80.66306  ? 254 LYS A CG  1 
ATOM   1173 C  CD  . LYS A  1 154 ? 32.93400  -19.09500 27.08000 1.000 103.13621 ? 254 LYS A CD  1 
ATOM   1174 C  CE  . LYS A  1 154 ? 33.41300  -20.02500 25.97300 1.000 102.38432 ? 254 LYS A CE  1 
ATOM   1175 N  NZ  . LYS A  1 154 ? 33.90100  -21.32500 26.52200 1.000 105.02662 ? 254 LYS A NZ  1 
ATOM   1176 N  N   . PRO B  1 2   ? -10.69300 3.59600   35.71600 1.000 89.92653  ? 102 PRO B N   1 
ATOM   1177 C  CA  . PRO B  1 2   ? -9.89600  2.54600   35.08500 1.000 82.98780  ? 102 PRO B CA  1 
ATOM   1178 C  C   . PRO B  1 2   ? -8.58500  2.22900   35.80600 1.000 72.20797  ? 102 PRO B C   1 
ATOM   1179 O  O   . PRO B  1 2   ? -7.60000  2.95800   35.67300 1.000 70.27960  ? 102 PRO B O   1 
ATOM   1180 C  CB  . PRO B  1 2   ? -9.63500  3.12600   33.69400 1.000 88.01477  ? 102 PRO B CB  1 
ATOM   1181 C  CG  . PRO B  1 2   ? -10.88600 3.96600   33.40700 1.000 97.09961  ? 102 PRO B CG  1 
ATOM   1182 C  CD  . PRO B  1 2   ? -11.60400 4.20700   34.73400 1.000 95.83923  ? 102 PRO B CD  1 
ATOM   1183 N  N   . THR B  1 3   ? -8.59300  1.13500   36.56600 0.712 64.20379  ? 103 THR B N   1 
ATOM   1184 C  CA  . THR B  1 3   ? -7.38700  0.64300   37.20400 0.712 57.64849  ? 103 THR B CA  1 
ATOM   1185 C  C   . THR B  1 3   ? -6.40900  0.14400   36.14400 0.712 52.59035  ? 103 THR B C   1 
ATOM   1186 O  O   . THR B  1 3   ? -6.81100  -0.16800  35.02000 0.712 45.90977  ? 103 THR B O   1 
ATOM   1187 C  CB  . THR B  1 3   ? -7.72100  -0.49300  38.16900 0.712 55.20283  ? 103 THR B CB  1 
ATOM   1188 O  OG1 . THR B  1 3   ? -8.28500  -1.58200  37.43200 0.712 52.40269  ? 103 THR B OG1 1 
ATOM   1189 C  CG2 . THR B  1 3   ? -8.72000  -0.03500  39.21800 0.712 66.41068  ? 103 THR B CG2 1 
ATOM   1190 N  N   . PRO B  1 4   ? -5.11600  0.06800   36.47800 1.000 54.96961  ? 104 PRO B N   1 
ATOM   1191 C  CA  . PRO B  1 4   ? -4.14900  -0.51000  35.52700 1.000 48.79091  ? 104 PRO B CA  1 
ATOM   1192 C  C   . PRO B  1 4   ? -4.55200  -1.87900  35.00100 1.000 46.92693  ? 104 PRO B C   1 
ATOM   1193 O  O   . PRO B  1 4   ? -4.34200  -2.16200  33.81500 1.000 46.63538  ? 104 PRO B O   1 
ATOM   1194 C  CB  . PRO B  1 4   ? -2.85900  -0.57300  36.35400 1.000 47.35942  ? 104 PRO B CB  1 
ATOM   1195 C  CG  . PRO B  1 4   ? -2.99300  0.55500   37.31700 1.000 55.66117  ? 104 PRO B CG  1 
ATOM   1196 C  CD  . PRO B  1 4   ? -4.45200  0.61300   37.67600 1.000 53.16089  ? 104 PRO B CD  1 
ATOM   1197 N  N   . VAL B  1 5   ? -5.13300  -2.73800  35.84400 1.000 46.97751  ? 105 VAL B N   1 
ATOM   1198 C  CA  . VAL B  1 5   ? -5.52300  -4.06400  35.37200 1.000 48.77483  ? 105 VAL B CA  1 
ATOM   1199 C  C   . VAL B  1 5   ? -6.65800  -3.95200  34.35900 1.000 43.21654  ? 105 VAL B C   1 
ATOM   1200 O  O   . VAL B  1 5   ? -6.63100  -4.60700  33.31100 1.000 43.27263  ? 105 VAL B O   1 
ATOM   1201 C  CB  . VAL B  1 5   ? -5.88200  -4.99100  36.55400 1.000 44.81686  ? 105 VAL B CB  1 
ATOM   1202 C  CG1 . VAL B  1 5   ? -6.92100  -4.36100  37.46400 1.000 58.20216  ? 105 VAL B CG1 1 
ATOM   1203 C  CG2 . VAL B  1 5   ? -6.36800  -6.34600  36.05300 1.000 47.13087  ? 105 VAL B CG2 1 
ATOM   1204 N  N   . GLU B  1 6   ? -7.64900  -3.09400  34.63600 1.000 40.13390  ? 106 GLU B N   1 
ATOM   1205 C  CA  . GLU B  1 6   ? -8.75600  -2.88500  33.70100 1.000 44.48399  ? 106 GLU B CA  1 
ATOM   1206 C  C   . GLU B  1 6   ? -8.26300  -2.33100  32.37400 1.000 38.76832  ? 106 GLU B C   1 
ATOM   1207 O  O   . GLU B  1 6   ? -8.70500  -2.77100  31.30400 1.000 43.21197  ? 106 GLU B O   1 
ATOM   1208 C  CB  . GLU B  1 6   ? -9.78900  -1.92800  34.29600 1.000 56.95288  ? 106 GLU B CB  1 
ATOM   1209 C  CG  . GLU B  1 6   ? -10.61100 -2.48500  35.44100 1.000 60.26581  ? 106 GLU B CG  1 
ATOM   1210 C  CD  . GLU B  1 6   ? -11.50200 -1.42800  36.07300 1.000 71.41075  ? 106 GLU B CD  1 
ATOM   1211 O  OE1 . GLU B  1 6   ? -10.98500 -0.35100  36.44700 1.000 68.70808  ? 106 GLU B OE1 1 
ATOM   1212 O  OE2 . GLU B  1 6   ? -12.72200 -1.67000  36.18500 1.000 77.26264  ? 106 GLU B OE2 1 
ATOM   1213 N  N   . GLU B  1 7   ? -7.36600  -1.34300  32.42700 1.000 47.22105  ? 107 GLU B N   1 
ATOM   1214 C  CA  . GLU B  1 7   ? -6.80000  -0.78500  31.20400 1.000 44.05355  ? 107 GLU B CA  1 
ATOM   1215 C  C   . GLU B  1 7   ? -5.98100  -1.82600  30.46400 1.000 38.61237  ? 107 GLU B C   1 
ATOM   1216 O  O   . GLU B  1 7   ? -6.04400  -1.91000  29.23400 1.000 35.09754  ? 107 GLU B O   1 
ATOM   1217 C  CB  . GLU B  1 7   ? -5.94000  0.43400   31.53000 1.000 46.71477  ? 107 GLU B CB  1 
ATOM   1218 C  CG  . GLU B  1 7   ? -6.67300  1.51100   32.30200 1.000 55.41224  ? 107 GLU B CG  1 
ATOM   1219 C  CD  . GLU B  1 7   ? -5.83600  2.75800   32.47900 1.000 60.56084  ? 107 GLU B CD  1 
ATOM   1220 O  OE1 . GLU B  1 7   ? -4.67500  2.63700   32.91900 1.000 66.12973  ? 107 GLU B OE1 1 
ATOM   1221 O  OE2 . GLU B  1 7   ? -6.33400  3.85800   32.16100 1.000 72.58697  ? 107 GLU B OE2 1 
ATOM   1222 N  N   . ALA B  1 8   ? -5.21200  -2.63500  31.20200 1.000 33.10459  ? 108 ALA B N   1 
ATOM   1223 C  CA  . ALA B  1 8   ? -4.46900  -3.72100  30.57700 1.000 36.84821  ? 108 ALA B CA  1 
ATOM   1224 C  C   . ALA B  1 8   ? -5.40200  -4.67300  29.84600 1.000 30.28369  ? 108 ALA B C   1 
ATOM   1225 O  O   . ALA B  1 8   ? -5.11600  -5.08500  28.71400 1.000 31.34026  ? 108 ALA B O   1 
ATOM   1226 C  CB  . ALA B  1 8   ? -3.65300  -4.47800  31.62600 1.000 34.80101  ? 108 ALA B CB  1 
ATOM   1227 N  N   . GLN B  1 9   ? -6.52100  -5.04200  30.48200 1.000 32.79142  ? 109 GLN B N   1 
ATOM   1228 C  CA  . GLN B  1 9   ? -7.48500  -5.92000  29.82800 1.000 34.70916  ? 109 GLN B CA  1 
ATOM   1229 C  C   . GLN B  1 9   ? -8.03400  -5.27400  28.56700 1.000 35.33840  ? 109 GLN B C   1 
ATOM   1230 O  O   . GLN B  1 9   ? -8.14700  -5.92800  27.52400 1.000 30.42435  ? 109 GLN B O   1 
ATOM   1231 C  CB  . GLN B  1 9   ? -8.63600  -6.26600  30.77600 1.000 38.98250  ? 109 GLN B CB  1 
ATOM   1232 C  CG  . GLN B  1 9   ? -8.22400  -6.87900  32.11100 1.000 54.89458  ? 109 GLN B CG  1 
ATOM   1233 C  CD  . GLN B  1 9   ? -7.72700  -8.30700  31.98800 1.000 71.61561  ? 109 GLN B CD  1 
ATOM   1234 O  OE1 . GLN B  1 9   ? -7.99800  -8.97800  31.07000 1.000 74.99106  ? 109 GLN B OE1 1 
ATOM   1235 N  NE2 . GLN B  1 9   ? -7.00800  -8.74800  32.91900 1.000 66.83924  ? 109 GLN B NE2 1 
ATOM   1236 N  N   . GLN B  1 10  ? -8.37700  -3.98700  28.64400 1.000 34.02566  ? 110 GLN B N   1 
ATOM   1237 C  CA  . GLN B  1 10  ? -8.93800  -3.30800  27.48400 1.000 35.36105  ? 110 GLN B CA  1 
ATOM   1238 C  C   . GLN B  1 10  ? -7.93300  -3.24700  26.34200 1.000 34.53202  ? 110 GLN B C   1 
ATOM   1239 O  O   . GLN B  1 10  ? -8.30500  -3.43200  25.17800 1.000 33.47833  ? 110 GLN B O   1 
ATOM   1240 C  CB  . GLN B  1 10  ? -9.40800  -1.90600  27.86600 1.000 37.77079  ? 110 GLN B CB  1 
ATOM   1241 C  CG  . GLN B  1 10  ? -10.38000 -1.31300  26.86800 1.000 54.96410  ? 110 GLN B CG  1 
ATOM   1242 C  CD  . GLN B  1 10  ? -11.56700 -2.22600  26.59800 1.000 59.82658  ? 110 GLN B CD  1 
ATOM   1243 O  OE1 . GLN B  1 10  ? -12.00000 -2.38100  25.45200 1.000 64.14119  ? 110 GLN B OE1 1 
ATOM   1244 N  NE2 . GLN B  1 10  ? -12.10400 -2.83200  27.65600 1.000 57.46382  ? 110 GLN B NE2 1 
ATOM   1245 N  N   . LYS B  1 11  ? -6.65400  -3.00000  26.65400 1.000 35.69373  ? 111 LYS B N   1 
ATOM   1246 C  CA  . LYS B  1 11  ? -5.62700  -3.00700  25.61300 1.000 32.28153  ? 111 LYS B CA  1 
ATOM   1247 C  C   . LYS B  1 11  ? -5.50900  -4.38000  24.96900 1.000 28.90810  ? 111 LYS B C   1 
ATOM   1248 O  O   . LYS B  1 11  ? -5.33000  -4.49100  23.74900 1.000 27.55704  ? 111 LYS B O   1 
ATOM   1249 C  CB  . LYS B  1 11  ? -4.27300  -2.58500  26.18800 1.000 36.07587  ? 111 LYS B CB  1 
ATOM   1250 C  CG  . LYS B  1 11  ? -4.26300  -1.23200  26.88500 1.000 42.18616  ? 111 LYS B CG  1 
ATOM   1251 C  CD  . LYS B  1 11  ? -3.92600  -0.08800  25.94800 1.000 54.55424  ? 111 LYS B CD  1 
ATOM   1252 C  CE  . LYS B  1 11  ? -3.71000  1.19800   26.73100 1.000 61.19497  ? 111 LYS B CE  1 
ATOM   1253 N  NZ  . LYS B  1 11  ? -4.14000  2.38800   25.95700 1.000 58.55708  ? 111 LYS B NZ  1 
ATOM   1254 N  N   . THR B  1 12  ? -5.58300  -5.44100  25.77600 1.000 27.74452  ? 112 THR B N   1 
ATOM   1255 C  CA  . THR B  1 12  ? -5.54200  -6.78900  25.22000 1.000 28.75734  ? 112 THR B CA  1 
ATOM   1256 C  C   . THR B  1 12  ? -6.73400  -7.04000  24.30100 1.000 31.08131  ? 112 THR B C   1 
ATOM   1257 O  O   . THR B  1 12  ? -6.57900  -7.60300  23.21000 1.000 25.84749  ? 112 THR B O   1 
ATOM   1258 C  CB  . THR B  1 12  ? -5.49800  -7.82600  26.34400 1.000 32.82398  ? 112 THR B CB  1 
ATOM   1259 O  OG1 . THR B  1 12  ? -4.26800  -7.70100  27.07300 1.000 33.90748  ? 112 THR B OG1 1 
ATOM   1260 C  CG2 . THR B  1 12  ? -5.58800  -9.22700  25.76900 1.000 29.63021  ? 112 THR B CG2 1 
ATOM   1261 N  N   . ILE B  1 13  ? -7.93300  -6.62600  24.72100 1.000 23.36395  ? 113 ILE B N   1 
ATOM   1262 C  CA  . ILE B  1 13  ? -9.12000  -6.79700  23.87800 1.000 25.45204  ? 113 ILE B CA  1 
ATOM   1263 C  C   . ILE B  1 13  ? -8.95700  -6.04100  22.56500 1.000 28.31801  ? 113 ILE B C   1 
ATOM   1264 O  O   . ILE B  1 13  ? -9.26300  -6.56500  21.48600 1.000 26.47718  ? 113 ILE B O   1 
ATOM   1265 C  CB  . ILE B  1 13  ? -10.38600 -6.34500  24.62700 1.000 24.01125  ? 113 ILE B CB  1 
ATOM   1266 C  CG1 . ILE B  1 13  ? -10.68100 -7.28400  25.79600 1.000 32.50278  ? 113 ILE B CG1 1 
ATOM   1267 C  CG2 . ILE B  1 13  ? -11.58600 -6.29600  23.67900 1.000 29.27406  ? 113 ILE B CG2 1 
ATOM   1268 C  CD1 . ILE B  1 13  ? -11.86400 -6.82700  26.65100 1.000 38.58098  ? 113 ILE B CD1 1 
ATOM   1269 N  N   . GLU B  1 14  ? -8.49100  -4.79000  22.63300 1.000 25.68528  ? 114 GLU B N   1 
ATOM   1270 C  CA  . GLU B  1 14  ? -8.28400  -4.03200  21.39400 1.000 29.38606  ? 114 GLU B CA  1 
ATOM   1271 C  C   . GLU B  1 14  ? -7.25100  -4.71100  20.50500 1.000 27.26735  ? 114 GLU B C   1 
ATOM   1272 O  O   . GLU B  1 14  ? -7.39900  -4.74400  19.27800 1.000 29.10033  ? 114 GLU B O   1 
ATOM   1273 C  CB  . GLU B  1 14  ? -7.83400  -2.59800  21.68700 1.000 34.63532  ? 114 GLU B CB  1 
ATOM   1274 C  CG  . GLU B  1 14  ? -8.65100  -1.81400  22.71100 1.000 48.84915  ? 114 GLU B CG  1 
ATOM   1275 C  CD  . GLU B  1 14  ? -10.03000 -1.40100  22.23200 1.000 69.22401  ? 114 GLU B CD  1 
ATOM   1276 O  OE1 . GLU B  1 14  ? -10.36400 -1.63900  21.05200 1.000 70.85090  ? 114 GLU B OE1 1 
ATOM   1277 O  OE2 . GLU B  1 14  ? -10.78200 -0.82600  23.05000 1.000 76.34277  ? 114 GLU B OE2 1 
ATOM   1278 N  N   . ALA B  1 15  ? -6.18100  -5.23300  21.11100 1.000 25.39662  ? 115 ALA B N   1 
ATOM   1279 C  CA  . ALA B  1 15  ? -5.15200  -5.93200  20.35100 1.000 26.08048  ? 115 ALA B CA  1 
ATOM   1280 C  C   . ALA B  1 15  ? -5.72800  -7.13700  19.62500 1.000 25.48089  ? 115 ALA B C   1 
ATOM   1281 O  O   . ALA B  1 15  ? -5.42600  -7.36500  18.44900 1.000 26.20653  ? 115 ALA B O   1 
ATOM   1282 C  CB  . ALA B  1 15  ? -4.01600  -6.36500  21.27700 1.000 26.94218  ? 115 ALA B CB  1 
ATOM   1283 N  N   . ILE B  1 16  ? -6.56700  -7.91500  20.31200 1.000 23.25800  ? 116 ILE B N   1 
ATOM   1284 C  CA  . ILE B  1 16  ? -7.19800  -9.07400  19.68800 1.000 21.87523  ? 116 ILE B CA  1 
ATOM   1285 C  C   . ILE B  1 16  ? -8.10500  -8.63800  18.54400 1.000 21.56794  ? 116 ILE B C   1 
ATOM   1286 O  O   . ILE B  1 16  ? -8.03200  -9.17900  17.43100 1.000 22.68289  ? 116 ILE B O   1 
ATOM   1287 C  CB  . ILE B  1 16  ? -7.97500  -9.88500  20.73700 1.000 19.00221  ? 116 ILE B CB  1 
ATOM   1288 C  CG1 . ILE B  1 16  ? -7.00500  -10.51800 21.73400 1.000 23.33302  ? 116 ILE B CG1 1 
ATOM   1289 C  CG2 . ILE B  1 16  ? -8.83600  -10.95200 20.05900 1.000 19.95856  ? 116 ILE B CG2 1 
ATOM   1290 C  CD1 . ILE B  1 16  ? -7.72300  -11.06700 22.97400 1.000 25.37042  ? 116 ILE B CD1 1 
ATOM   1291 N  N   . THR B  1 17  ? -8.97300  -7.65400  18.79300 1.000 21.45985  ? 117 THR B N   1 
ATOM   1292 C  CA  . THR B  1 17  ? -9.97000  -7.31800  17.77900 1.000 22.36220  ? 117 THR B CA  1 
ATOM   1293 C  C   . THR B  1 17  ? -9.31400  -6.69300  16.55000 1.000 23.32082  ? 117 THR B C   1 
ATOM   1294 O  O   . THR B  1 17  ? -9.74100  -6.95400  15.41900 1.000 25.85392  ? 117 THR B O   1 
ATOM   1295 C  CB  . THR B  1 17  ? -11.05400 -6.39900  18.35300 1.000 32.06322  ? 117 THR B CB  1 
ATOM   1296 O  OG1 . THR B  1 17  ? -10.46600 -5.18100  18.82500 1.000 29.78916  ? 117 THR B OG1 1 
ATOM   1297 C  CG2 . THR B  1 17  ? -11.80400 -7.09400  19.50300 1.000 30.58002  ? 117 THR B CG2 1 
ATOM   1298 N  N   . LYS B  1 18  ? -8.25900  -5.89000  16.75200 1.000 25.57588  ? 118 LYS B N   1 
ATOM   1299 C  CA  . LYS B  1 18  ? -7.49200  -5.34500  15.63200 1.000 23.78505  ? 118 LYS B CA  1 
ATOM   1300 C  C   . LYS B  1 18  ? -6.87600  -6.45800  14.79400 1.000 23.24619  ? 118 LYS B C   1 
ATOM   1301 O  O   . LYS B  1 18  ? -6.91400  -6.41800  13.55400 1.000 24.18966  ? 118 LYS B O   1 
ATOM   1302 C  CB  . LYS B  1 18  ? -6.39300  -4.41000  16.16400 1.000 28.08924  ? 118 LYS B CB  1 
ATOM   1303 C  CG  . LYS B  1 18  ? -6.53700  -2.95300  15.75300 1.000 45.92210  ? 118 LYS B CG  1 
ATOM   1304 C  CD  . LYS B  1 18  ? -5.88200  -2.03300  16.77300 1.000 51.93912  ? 118 LYS B CD  1 
ATOM   1305 C  CE  . LYS B  1 18  ? -4.42600  -2.41100  17.01100 1.000 54.24096  ? 118 LYS B CE  1 
ATOM   1306 N  NZ  . LYS B  1 18  ? -3.79100  -1.58300  18.08300 1.000 65.21226  ? 118 LYS B NZ  1 
ATOM   1307 N  N   . ALA B  1 19  ? -6.27000  -7.44500  15.46100 1.000 21.24441  ? 119 ALA B N   1 
ATOM   1308 C  CA  . ALA B  1 19  ? -5.62700  -8.54800  14.75500 1.000 20.56161  ? 119 ALA B CA  1 
ATOM   1309 C  C   . ALA B  1 19  ? -6.64600  -9.39200  14.00400 1.000 24.95879  ? 119 ALA B C   1 
ATOM   1310 O  O   . ALA B  1 19  ? -6.44100  -9.73900  12.83300 1.000 21.31363  ? 119 ALA B O   1 
ATOM   1311 C  CB  . ALA B  1 19  ? -4.84700  -9.41400  15.74900 1.000 22.74137  ? 119 ALA B CB  1 
ATOM   1312 N  N   . ILE B  1 20  ? -7.74600  -9.74500  14.67200 1.000 23.16813  ? 120 ILE B N   1 
ATOM   1313 C  CA  . ILE B  1 20  ? -8.78600  -10.54900 14.03100 1.000 22.06011  ? 120 ILE B CA  1 
ATOM   1314 C  C   . ILE B  1 20  ? -9.36900  -9.81100  12.83000 1.000 24.73547  ? 120 ILE B C   1 
ATOM   1315 O  O   . ILE B  1 20  ? -9.61700  -10.41100 11.77600 1.000 24.17557  ? 120 ILE B O   1 
ATOM   1316 C  CB  . ILE B  1 20  ? -9.87600  -10.92600 15.05100 1.000 21.21666  ? 120 ILE B CB  1 
ATOM   1317 C  CG1 . ILE B  1 20  ? -9.32800  -11.89400 16.11800 1.000 26.21182  ? 120 ILE B CG1 1 
ATOM   1318 C  CG2 . ILE B  1 20  ? -11.12200 -11.48300 14.32400 1.000 23.67845  ? 120 ILE B CG2 1 
ATOM   1319 C  CD1 . ILE B  1 20  ? -8.82500  -13.23700 15.57100 1.000 20.49446  ? 120 ILE B CD1 1 
ATOM   1320 N  N   . ASN B  1 21  ? -9.59000  -8.49900  12.96400 1.000 21.48684  ? 121 ASN B N   1 
ATOM   1321 C  CA  . ASN B  1 21  ? -10.12300 -7.73000  11.83900 1.000 29.12814  ? 121 ASN B CA  1 
ATOM   1322 C  C   . ASN B  1 21  ? -9.15300  -7.73000  10.66700 1.000 29.86187  ? 121 ASN B C   1 
ATOM   1323 O  O   . ASN B  1 21  ? -9.55900  -7.90800  9.51300  1.000 28.72410  ? 121 ASN B O   1 
ATOM   1324 C  CB  . ASN B  1 21  ? -10.43800 -6.30000  12.27600 1.000 30.92837  ? 121 ASN B CB  1 
ATOM   1325 C  CG  . ASN B  1 21  ? -11.14100 -5.50200  11.19200 1.000 48.58400  ? 121 ASN B CG  1 
ATOM   1326 O  OD1 . ASN B  1 21  ? -12.14300 -5.94500  10.62900 1.000 59.33243  ? 121 ASN B OD1 1 
ATOM   1327 N  ND2 . ASN B  1 21  ? -10.61600 -4.32100  10.89200 1.000 46.74460  ? 121 ASN B ND2 1 
ATOM   1328 N  N   . TYR B  1 22  ? -7.86000  -7.53700  10.94500 1.000 22.99480  ? 122 TYR B N   1 
ATOM   1329 C  CA  . TYR B  1 22  ? -6.84900  -7.53800  9.88800  1.000 26.77292  ? 122 TYR B CA  1 
ATOM   1330 C  C   . TYR B  1 22  ? -6.83100  -8.87100  9.14500  1.000 25.45869  ? 122 TYR B C   1 
ATOM   1331 O  O   . TYR B  1 22  ? -6.79300  -8.91200  7.90900  1.000 25.63684  ? 122 TYR B O   1 
ATOM   1332 C  CB  . TYR B  1 22  ? -5.48200  -7.23900  10.51400 1.000 28.78454  ? 122 TYR B CB  1 
ATOM   1333 C  CG  . TYR B  1 22  ? -4.28400  -7.19000  9.57300  1.000 28.87055  ? 122 TYR B CG  1 
ATOM   1334 C  CD1 . TYR B  1 22  ? -3.68100  -8.35800  9.10500  1.000 24.62813  ? 122 TYR B CD1 1 
ATOM   1335 C  CD2 . TYR B  1 22  ? -3.71700  -5.97700  9.21800  1.000 35.76254  ? 122 TYR B CD2 1 
ATOM   1336 C  CE1 . TYR B  1 22  ? -2.56600  -8.30700  8.27300  1.000 30.09679  ? 122 TYR B CE1 1 
ATOM   1337 C  CE2 . TYR B  1 22  ? -2.60800  -5.91700  8.39000  1.000 39.69034  ? 122 TYR B CE2 1 
ATOM   1338 C  CZ  . TYR B  1 22  ? -2.03900  -7.08300  7.92200  1.000 38.60985  ? 122 TYR B CZ  1 
ATOM   1339 O  OH  . TYR B  1 22  ? -0.93800  -7.02100  7.10000  1.000 46.33479  ? 122 TYR B OH  1 
ATOM   1340 N  N   . MET B  1 23  ? -6.84700  -9.97800  9.89200  1.000 23.36410  ? 123 MET B N   1 
ATOM   1341 C  CA  . MET B  1 23  ? -6.78600  -11.30100 9.27900  1.000 19.17903  ? 123 MET B CA  1 
ATOM   1342 C  C   . MET B  1 23  ? -8.09000  -11.63700 8.55900  1.000 25.28994  ? 123 MET B C   1 
ATOM   1343 O  O   . MET B  1 23  ? -8.07600  -12.26300 7.48900  1.000 24.92587  ? 123 MET B O   1 
ATOM   1344 C  CB  . MET B  1 23  ? -6.46300  -12.33800 10.36200 1.000 19.88552  ? 123 MET B CB  1 
ATOM   1345 C  CG  . MET B  1 23  ? -5.07800  -12.12400 10.95800 1.000 25.16906  ? 123 MET B CG  1 
ATOM   1346 S  SD  . MET B  1 23  ? -4.55700  -13.41700 12.11100 1.000 22.39102  ? 123 MET B SD  1 
ATOM   1347 C  CE  . MET B  1 23  ? -5.60900  -13.05200 13.52500 1.000 21.52480  ? 123 MET B CE  1 
ATOM   1348 N  N   . ALA B  1 24  ? -9.22300  -11.22500 9.12500  1.000 21.31585  ? 124 ALA B N   1 
ATOM   1349 C  CA  . ALA B  1 24  ? -10.50800 -11.48300 8.48000  1.000 23.05783  ? 124 ALA B CA  1 
ATOM   1350 C  C   . ALA B  1 24  ? -10.56000 -10.84600 7.09700  1.000 25.94455  ? 124 ALA B C   1 
ATOM   1351 O  O   . ALA B  1 24  ? -10.98800 -11.48300 6.12600  1.000 23.77846  ? 124 ALA B O   1 
ATOM   1352 C  CB  . ALA B  1 24  ? -11.65300 -10.96400 9.35500  1.000 23.58073  ? 124 ALA B CB  1 
ATOM   1353 N  N   . LYS B  1 25  ? -10.09900 -9.59700  6.98900  1.000 22.78975  ? 125 LYS B N   1 
ATOM   1354 C  CA  . LYS B  1 25  ? -10.13800 -8.89300  5.71000  1.000 25.42789  ? 125 LYS B CA  1 
ATOM   1355 C  C   . LYS B  1 25  ? -9.29700  -9.59500  4.65900  1.000 26.24145  ? 125 LYS B C   1 
ATOM   1356 O  O   . LYS B  1 25  ? -9.56400  -9.45000  3.45700  1.000 28.61371  ? 125 LYS B O   1 
ATOM   1357 C  CB  . LYS B  1 25  ? -9.65000  -7.45400  5.86600  1.000 29.21026  ? 125 LYS B CB  1 
ATOM   1358 C  CG  . LYS B  1 25  ? -10.55600 -6.52400  6.65000  1.000 44.00755  ? 125 LYS B CG  1 
ATOM   1359 C  CD  . LYS B  1 25  ? -10.24000 -5.07400  6.28900  1.000 64.73275  ? 125 LYS B CD  1 
ATOM   1360 C  CE  . LYS B  1 25  ? -10.78000 -4.09000  7.31000  1.000 61.51473  ? 125 LYS B CE  1 
ATOM   1361 N  NZ  . LYS B  1 25  ? -9.70500  -3.63900  8.23300  1.000 56.65874  ? 125 LYS B NZ  1 
ATOM   1362 N  N   . ARG B  1 26  ? -8.27800  -10.34500 5.08500  1.000 24.59656  ? 126 ARG B N   1 
ATOM   1363 C  CA  . ARG B  1 26  ? -7.32300  -10.97200 4.18000  1.000 26.25242  ? 126 ARG B CA  1 
ATOM   1364 C  C   . ARG B  1 26  ? -7.51000  -12.48000 4.05300  1.000 28.63875  ? 126 ARG B C   1 
ATOM   1365 O  O   . ARG B  1 26  ? -6.70200  -13.13500 3.38500  1.000 27.17468  ? 126 ARG B O   1 
ATOM   1366 C  CB  . ARG B  1 26  ? -5.89800  -10.65800 4.64400  1.000 25.86526  ? 126 ARG B CB  1 
ATOM   1367 C  CG  . ARG B  1 26  ? -5.52400  -9.20000  4.44500  1.000 30.33091  ? 126 ARG B CG  1 
ATOM   1368 C  CD  . ARG B  1 26  ? -4.34500  -8.77100  5.30400  1.000 26.92454  ? 126 ARG B CD  1 
ATOM   1369 N  NE  . ARG B  1 26  ? -3.98200  -7.38000  5.05100  1.000 33.24410  ? 126 ARG B NE  1 
ATOM   1370 C  CZ  . ARG B  1 26  ? -4.59200  -6.33600  5.59800  1.000 41.44885  ? 126 ARG B CZ  1 
ATOM   1371 N  NH1 . ARG B  1 26  ? -5.61700  -6.48600  6.42100  1.000 34.51303  ? 126 ARG B NH1 1 
ATOM   1372 N  NH2 . ARG B  1 26  ? -4.16600  -5.10900  5.30800  1.000 37.83448  ? 126 ARG B NH2 1 
ATOM   1373 N  N   . ARG B  1 27  ? -8.54200  -13.04900 4.68100  1.000 23.35267  ? 127 ARG B N   1 
ATOM   1374 C  CA  . ARG B  1 27  ? -8.74900  -14.50300 4.69000  1.000 21.39996  ? 127 ARG B CA  1 
ATOM   1375 C  C   . ARG B  1 27  ? -7.54700  -15.24100 5.27300  1.000 26.35323  ? 127 ARG B C   1 
ATOM   1376 O  O   . ARG B  1 27  ? -7.19500  -16.34300 4.83800  1.000 30.77532  ? 127 ARG B O   1 
ATOM   1377 C  CB  . ARG B  1 27  ? -9.05900  -15.04300 3.29400  1.000 31.55911  ? 127 ARG B CB  1 
ATOM   1378 C  CG  . ARG B  1 27  ? -10.38300 -14.60900 2.75900  1.000 29.95573  ? 127 ARG B CG  1 
ATOM   1379 C  CD  . ARG B  1 27  ? -10.64200 -15.30700 1.44300  1.000 32.64443  ? 127 ARG B CD  1 
ATOM   1380 N  NE  . ARG B  1 27  ? -11.79500 -14.70400 0.80600  1.000 30.70299  ? 127 ARG B NE  1 
ATOM   1381 C  CZ  . ARG B  1 27  ? -11.77600 -13.51600 0.22000  1.000 31.05423  ? 127 ARG B CZ  1 
ATOM   1382 N  NH1 . ARG B  1 27  ? -10.65600 -12.82100 0.09700  1.000 35.40948  ? 127 ARG B NH1 1 
ATOM   1383 N  NH2 . ARG B  1 27  ? -12.91300 -12.99900 -0.22900 1.000 33.29656  ? 127 ARG B NH2 1 
ATOM   1384 N  N   . ILE B  1 28  ? -6.89800  -14.63400 6.25600  1.000 24.08078  ? 128 ILE B N   1 
ATOM   1385 C  CA  . ILE B  1 28  ? -5.81300  -15.29900 6.96600  1.000 23.20729  ? 128 ILE B CA  1 
ATOM   1386 C  C   . ILE B  1 28  ? -6.44100  -16.19400 8.03300  1.000 27.14484  ? 128 ILE B C   1 
ATOM   1387 O  O   . ILE B  1 28  ? -7.01800  -15.69400 9.00000  1.000 24.72257  ? 128 ILE B O   1 
ATOM   1388 C  CB  . ILE B  1 28  ? -4.85400  -14.28000 7.58300  1.000 22.19749  ? 128 ILE B CB  1 
ATOM   1389 C  CG1 . ILE B  1 28  ? -4.13000  -13.49100 6.47500  1.000 21.19183  ? 128 ILE B CG1 1 
ATOM   1390 C  CG2 . ILE B  1 28  ? -3.86200  -14.96400 8.51800  1.000 21.03705  ? 128 ILE B CG2 1 
ATOM   1391 C  CD1 . ILE B  1 28  ? -3.42600  -12.25600 7.02400  1.000 27.08452  ? 128 ILE B CD1 1 
ATOM   1392 N  N   . GLY B  1 29  ? -6.33400  -17.51000 7.85600  1.000 23.33203  ? 129 GLY B N   1 
ATOM   1393 C  CA  . GLY B  1 29  ? -6.91400  -18.42400 8.82700  1.000 19.61457  ? 129 GLY B CA  1 
ATOM   1394 C  C   . GLY B  1 29  ? -6.25700  -18.25900 10.18500 1.000 23.51321  ? 129 GLY B C   1 
ATOM   1395 O  O   . GLY B  1 29  ? -5.04000  -18.09300 10.29200 1.000 23.07318  ? 129 GLY B O   1 
ATOM   1396 N  N   . ALA B  1 30  ? -7.07800  -18.27900 11.23300 1.000 21.19202  ? 130 ALA B N   1 
ATOM   1397 C  CA  . ALA B  1 30  ? -6.53700  -18.07800 12.56900 1.000 18.96258  ? 130 ALA B CA  1 
ATOM   1398 C  C   . ALA B  1 30  ? -7.35200  -18.86000 13.58600 1.000 19.44015  ? 130 ALA B C   1 
ATOM   1399 O  O   . ALA B  1 30  ? -8.55400  -19.09300 13.42100 1.000 18.19326  ? 130 ALA B O   1 
ATOM   1400 C  CB  . ALA B  1 30  ? -6.49200  -16.59200 12.96300 1.000 18.27330  ? 130 ALA B CB  1 
ATOM   1401 N  N   . LEU B  1 31  ? -6.67200  -19.24500 14.65600 1.000 19.59310  ? 131 LEU B N   1 
ATOM   1402 C  CA  . LEU B  1 31  ? -7.25400  -20.06000 15.72000 1.000 18.82465  ? 131 LEU B CA  1 
ATOM   1403 C  C   . LEU B  1 31  ? -6.65300  -19.54700 17.01500 1.000 17.56177  ? 131 LEU B C   1 
ATOM   1404 O  O   . LEU B  1 31  ? -5.47700  -19.79700 17.28900 1.000 17.30771  ? 131 LEU B O   1 
ATOM   1405 C  CB  . LEU B  1 31  ? -6.93300  -21.54100 15.52800 1.000 19.70007  ? 131 LEU B CB  1 
ATOM   1406 C  CG  . LEU B  1 31  ? -7.45300  -22.52500 16.57100 1.000 23.37943  ? 131 LEU B CG  1 
ATOM   1407 C  CD1 . LEU B  1 31  ? -8.96300  -22.41400 16.65200 1.000 24.85678  ? 131 LEU B CD1 1 
ATOM   1408 C  CD2 . LEU B  1 31  ? -7.05400  -23.92800 16.17100 1.000 24.76021  ? 131 LEU B CD2 1 
ATOM   1409 N  N   . LEU B  1 32  ? -7.46000  -18.86100 17.82700 1.000 17.94031  ? 132 LEU B N   1 
ATOM   1410 C  CA  . LEU B  1 32  ? -6.95000  -18.14800 18.99900 1.000 17.93084  ? 132 LEU B CA  1 
ATOM   1411 C  C   . LEU B  1 32  ? -7.78700  -18.53600 20.20800 1.000 19.58182  ? 132 LEU B C   1 
ATOM   1412 O  O   . LEU B  1 32  ? -8.96600  -18.18000 20.28300 1.000 18.52491  ? 132 LEU B O   1 
ATOM   1413 C  CB  . LEU B  1 32  ? -6.99700  -16.64000 18.75700 1.000 19.27068  ? 132 LEU B CB  1 
ATOM   1414 C  CG  . LEU B  1 32  ? -6.51100  -15.74000 19.88800 1.000 21.02709  ? 132 LEU B CG  1 
ATOM   1415 C  CD1 . LEU B  1 32  ? -5.05600  -16.01100 20.14100 1.000 24.10517  ? 132 LEU B CD1 1 
ATOM   1416 C  CD2 . LEU B  1 32  ? -6.71500  -14.29800 19.43200 1.000 28.60844  ? 132 LEU B CD2 1 
ATOM   1417 N  N   . THR B  1 33  ? -7.18100  -19.26900 21.14300 1.000 18.04773  ? 133 THR B N   1 
ATOM   1418 C  CA  . THR B  1 33  ? -7.86200  -19.76600 22.33600 1.000 18.33700  ? 133 THR B CA  1 
ATOM   1419 C  C   . THR B  1 33  ? -7.41000  -18.95000 23.53800 1.000 18.61097  ? 133 THR B C   1 
ATOM   1420 O  O   . THR B  1 33  ? -6.20800  -18.82300 23.78600 1.000 18.95079  ? 133 THR B O   1 
ATOM   1421 C  CB  . THR B  1 33  ? -7.55400  -21.25200 22.54600 1.000 18.63478  ? 133 THR B CB  1 
ATOM   1422 O  OG1 . THR B  1 33  ? -8.13800  -22.01100 21.47100 1.000 20.80633  ? 133 THR B OG1 1 
ATOM   1423 C  CG2 . THR B  1 33  ? -8.12200  -21.73800 23.87800 1.000 21.07603  ? 133 THR B CG2 1 
ATOM   1424 N  N   . ILE B  1 34  ? -8.36500  -18.39000 24.27400 1.000 19.11854  ? 134 ILE B N   1 
ATOM   1425 C  CA  . ILE B  1 34  ? -8.07400  -17.53300 25.41900 1.000 19.53570  ? 134 ILE B CA  1 
ATOM   1426 C  C   . ILE B  1 34  ? -8.43400  -18.29700 26.68300 1.000 20.82148  ? 134 ILE B C   1 
ATOM   1427 O  O   . ILE B  1 34  ? -9.60800  -18.62000 26.89600 1.000 24.36990  ? 134 ILE B O   1 
ATOM   1428 C  CB  . ILE B  1 34  ? -8.84700  -16.20900 25.33800 1.000 23.73436  ? 134 ILE B CB  1 
ATOM   1429 C  CG1 . ILE B  1 34  ? -8.57700  -15.51700 23.99700 1.000 26.90929  ? 134 ILE B CG1 1 
ATOM   1430 C  CG2 . ILE B  1 34  ? -8.49300  -15.29300 26.51000 1.000 27.34594  ? 134 ILE B CG2 1 
ATOM   1431 C  CD1 . ILE B  1 34  ? -9.53000  -14.38100 23.71400 1.000 29.54165  ? 134 ILE B CD1 1 
ATOM   1432 N  N   . GLU B  1 35  ? -7.42600  -18.58300 27.52000 1.000 19.87768  ? 135 GLU B N   1 
ATOM   1433 C  CA  . GLU B  1 35  ? -7.66500  -19.26900 28.78800 1.000 22.80274  ? 135 GLU B CA  1 
ATOM   1434 C  C   . GLU B  1 35  ? -8.59800  -18.45200 29.67400 1.000 31.61786  ? 135 GLU B C   1 
ATOM   1435 O  O   . GLU B  1 35  ? -8.53800  -17.22000 29.70500 1.000 26.12925  ? 135 GLU B O   1 
ATOM   1436 C  CB  . GLU B  1 35  ? -6.33200  -19.51600 29.50700 1.000 24.89804  ? 135 GLU B CB  1 
ATOM   1437 C  CG  . GLU B  1 35  ? -6.40800  -20.53000 30.66200 1.000 27.76349  ? 135 GLU B CG  1 
ATOM   1438 C  CD  . GLU B  1 35  ? -5.05900  -20.68700 31.36700 1.000 33.49967  ? 135 GLU B CD  1 
ATOM   1439 O  OE1 . GLU B  1 35  ? -4.69500  -19.76800 32.11900 1.000 27.86954  ? 135 GLU B OE1 1 
ATOM   1440 O  OE2 . GLU B  1 35  ? -4.35900  -21.69900 31.13900 1.000 29.09806  ? 135 GLU B OE2 1 
ATOM   1441 N  N   . ARG B  1 36  ? -9.48900  -19.14800 30.39400 1.000 25.68844  ? 136 ARG B N   1 
ATOM   1442 C  CA  . ARG B  1 36  ? -10.38200 -18.49400 31.34100 1.000 28.44444  ? 136 ARG B CA  1 
ATOM   1443 C  C   . ARG B  1 36  ? -10.04000 -19.07800 32.70200 1.000 32.18538  ? 136 ARG B C   1 
ATOM   1444 O  O   . ARG B  1 36  ? -8.88100  -19.01600 33.10400 1.000 36.46577  ? 136 ARG B O   1 
ATOM   1445 C  CB  . ARG B  1 36  ? -11.83700 -18.63100 30.91200 1.000 29.17334  ? 136 ARG B CB  1 
ATOM   1446 C  CG  . ARG B  1 36  ? -12.10200 -18.01200 29.54700 1.000 40.78566  ? 136 ARG B CG  1 
ATOM   1447 C  CD  . ARG B  1 36  ? -12.47500 -16.53900 29.65400 1.000 57.83483  ? 136 ARG B CD  1 
ATOM   1448 N  NE  . ARG B  1 36  ? -13.92200 -16.35000 29.69900 1.000 62.03766  ? 136 ARG B NE  1 
ATOM   1449 C  CZ  . ARG B  1 36  ? -14.64700 -16.35600 30.81000 1.000 71.47577  ? 136 ARG B CZ  1 
ATOM   1450 N  NH1 . ARG B  1 36  ? -14.09100 -16.53300 31.99900 1.000 62.20171  ? 136 ARG B NH1 1 
ATOM   1451 N  NH2 . ARG B  1 36  ? -15.96100 -16.17200 30.72900 1.000 77.12989  ? 136 ARG B NH2 1 
ATOM   1452 N  N   . ASP B  1 37  ? -10.99700 -19.67800 33.40400 1.000 25.06065  ? 137 ASP B N   1 
ATOM   1453 C  CA  . ASP B  1 37  ? -10.64800 -20.24100 34.70400 1.000 29.60968  ? 137 ASP B CA  1 
ATOM   1454 C  C   . ASP B  1 37  ? -10.00100 -21.62200 34.58000 1.000 28.08159  ? 137 ASP B C   1 
ATOM   1455 O  O   . ASP B  1 37  ? -9.17900  -21.99000 35.42400 1.000 30.60524  ? 137 ASP B O   1 
ATOM   1456 C  CB  . ASP B  1 37  ? -11.88500 -20.30200 35.60600 1.000 30.09845  ? 137 ASP B CB  1 
ATOM   1457 C  CG  . ASP B  1 37  ? -12.49600 -18.92400 35.88300 1.000 31.48163  ? 137 ASP B CG  1 
ATOM   1458 O  OD1 . ASP B  1 37  ? -11.81600 -17.89900 35.70400 1.000 40.88898  ? 137 ASP B OD1 1 
ATOM   1459 O  OD2 . ASP B  1 37  ? -13.67200 -18.87300 36.30200 1.000 37.01052  ? 137 ASP B OD2 1 
ATOM   1460 N  N   . THR B  1 38  ? -10.33600 -22.39200 33.53900 1.000 29.34194  ? 138 THR B N   1 
ATOM   1461 C  CA  . THR B  1 38  ? -9.76500  -23.72500 33.36300 1.000 27.75043  ? 138 THR B CA  1 
ATOM   1462 C  C   . THR B  1 38  ? -8.34500  -23.62200 32.82200 1.000 29.13916  ? 138 THR B C   1 
ATOM   1463 O  O   . THR B  1 38  ? -8.13100  -23.06800 31.73900 1.000 26.61192  ? 138 THR B O   1 
ATOM   1464 C  CB  . THR B  1 38  ? -10.60900 -24.56100 32.40500 1.000 35.72790  ? 138 THR B CB  1 
ATOM   1465 O  OG1 . THR B  1 38  ? -11.97400 -24.56200 32.84100 1.000 38.60892  ? 138 THR B OG1 1 
ATOM   1466 C  CG2 . THR B  1 38  ? -10.07500 -25.99400 32.36000 1.000 33.38237  ? 138 THR B CG2 1 
ATOM   1467 N  N   . GLY B  1 39  ? -7.38200  -24.18900 33.54500 1.000 29.35788  ? 139 GLY B N   1 
ATOM   1468 C  CA  . GLY B  1 39  ? -6.00400  -24.12400 33.08900 1.000 26.75166  ? 139 GLY B CA  1 
ATOM   1469 C  C   . GLY B  1 39  ? -5.79100  -24.94700 31.83000 1.000 23.45449  ? 139 GLY B C   1 
ATOM   1470 O  O   . GLY B  1 39  ? -6.27600  -26.06800 31.69800 1.000 30.02557  ? 139 GLY B O   1 
ATOM   1471 N  N   . MET B  1 40  ? -5.03900  -24.39200 30.89700 1.000 22.04246  ? 140 MET B N   1 
ATOM   1472 C  CA  . MET B  1 40  ? -4.78600  -25.12800 29.66700 1.000 25.22693  ? 140 MET B CA  1 
ATOM   1473 C  C   . MET B  1 40  ? -3.31500  -25.44700 29.44700 1.000 24.06673  ? 140 MET B C   1 
ATOM   1474 O  O   . MET B  1 40  ? -2.87700  -25.62100 28.30600 1.000 21.81474  ? 140 MET B O   1 
ATOM   1475 C  CB  . MET B  1 40  ? -5.36000  -24.37600 28.48700 1.000 30.86236  ? 140 MET B CB  1 
ATOM   1476 C  CG  . MET B  1 40  ? -6.78800  -24.79300 28.32500 1.000 35.97879  ? 140 MET B CG  1 
ATOM   1477 S  SD  . MET B  1 40  ? -7.44500  -23.75300 27.10500 1.000 34.95661  ? 140 MET B SD  1 
ATOM   1478 C  CE  . MET B  1 40  ? -6.43300  -24.24700 25.70800 1.000 28.90883  ? 140 MET B CE  1 
ATOM   1479 N  N   . GLY B  1 41  ? -2.56000  -25.57600 30.53900 1.000 23.02413  ? 141 GLY B N   1 
ATOM   1480 C  CA  . GLY B  1 41  ? -1.14900  -25.90300 30.42100 1.000 29.26937  ? 141 GLY B CA  1 
ATOM   1481 C  C   . GLY B  1 41  ? -0.87700  -27.12000 29.55700 1.000 25.12453  ? 141 GLY B C   1 
ATOM   1482 O  O   . GLY B  1 41  ? 0.11500   -27.15700 28.82500 1.000 24.07355  ? 141 GLY B O   1 
ATOM   1483 N  N   . ASP B  1 42  ? -1.74500  -28.13900 29.64000 1.000 23.46536  ? 142 ASP B N   1 
ATOM   1484 C  CA  . ASP B  1 42  ? -1.51000  -29.37200 28.89500 1.000 28.36293  ? 142 ASP B CA  1 
ATOM   1485 C  C   . ASP B  1 42  ? -1.46300  -29.10000 27.39700 1.000 26.88886  ? 142 ASP B C   1 
ATOM   1486 O  O   . ASP B  1 42  ? -0.64300  -29.68200 26.67800 1.000 29.31551  ? 142 ASP B O   1 
ATOM   1487 C  CB  . ASP B  1 42  ? -2.59300  -30.41000 29.20000 1.000 31.83479  ? 142 ASP B CB  1 
ATOM   1488 C  CG  . ASP B  1 42  ? -2.51500  -30.94800 30.61800 1.000 36.17413  ? 142 ASP B CG  1 
ATOM   1489 O  OD1 . ASP B  1 42  ? -1.42300  -30.90500 31.21700 1.000 39.28689  ? 142 ASP B OD1 1 
ATOM   1490 O  OD2 . ASP B  1 42  ? -3.55400  -31.41600 31.12100 1.000 44.95461  ? 142 ASP B OD2 1 
ATOM   1491 N  N   . TYR B  1 43  ? -2.31600  -28.19700 26.91700 1.000 20.35237  ? 143 TYR B N   1 
ATOM   1492 C  CA  . TYR B  1 43  ? -2.32600  -27.86200 25.49500 1.000 22.59395  ? 143 TYR B CA  1 
ATOM   1493 C  C   . TYR B  1 43  ? -1.25300  -26.84000 25.14500 1.000 23.73396  ? 143 TYR B C   1 
ATOM   1494 O  O   . TYR B  1 43  ? -0.67400  -26.89300 24.05100 1.000 21.18210  ? 143 TYR B O   1 
ATOM   1495 C  CB  . TYR B  1 43  ? -3.70900  -27.34700 25.09200 1.000 23.51735  ? 143 TYR B CB  1 
ATOM   1496 C  CG  . TYR B  1 43  ? -4.76700  -28.32800 25.51100 1.000 25.90003  ? 143 TYR B CG  1 
ATOM   1497 C  CD1 . TYR B  1 43  ? -5.05800  -29.43600 24.72200 1.000 23.25275  ? 143 TYR B CD1 1 
ATOM   1498 C  CD2 . TYR B  1 43  ? -5.43400  -28.17900 26.71500 1.000 27.87614  ? 143 TYR B CD2 1 
ATOM   1499 C  CE1 . TYR B  1 43  ? -6.00000  -30.35900 25.12500 1.000 30.59668  ? 143 TYR B CE1 1 
ATOM   1500 C  CE2 . TYR B  1 43  ? -6.39000  -29.09100 27.11800 1.000 30.22590  ? 143 TYR B CE2 1 
ATOM   1501 C  CZ  . TYR B  1 43  ? -6.66000  -30.17900 26.32300 1.000 32.44826  ? 143 TYR B CZ  1 
ATOM   1502 O  OH  . TYR B  1 43  ? -7.60400  -31.09000 26.73300 1.000 39.05886  ? 143 TYR B OH  1 
ATOM   1503 N  N   . ILE B  1 44  ? -0.97000  -25.91000 26.05600 1.000 18.37441  ? 144 ILE B N   1 
ATOM   1504 C  CA  . ILE B  1 44  ? 0.10400   -24.94700 25.81600 1.000 21.99628  ? 144 ILE B CA  1 
ATOM   1505 C  C   . ILE B  1 44  ? 1.43200   -25.66800 25.60600 1.000 19.66569  ? 144 ILE B C   1 
ATOM   1506 O  O   . ILE B  1 44  ? 2.26400   -25.25000 24.78600 1.000 21.62102  ? 144 ILE B O   1 
ATOM   1507 C  CB  . ILE B  1 44  ? 0.17500   -23.94300 26.98500 1.000 19.78887  ? 144 ILE B CB  1 
ATOM   1508 C  CG1 . ILE B  1 44  ? -1.02400  -22.99400 26.92800 1.000 18.55456  ? 144 ILE B CG1 1 
ATOM   1509 C  CG2 . ILE B  1 44  ? 1.47700   -23.18000 26.98100 1.000 22.23965  ? 144 ILE B CG2 1 
ATOM   1510 C  CD1 . ILE B  1 44  ? -1.21800  -22.15600 28.22200 1.000 20.77041  ? 144 ILE B CD1 1 
ATOM   1511 N  N   . GLU B  1 45  ? 1.64400   -26.77100 26.32700 1.000 22.17163  ? 145 GLU B N   1 
ATOM   1512 C  CA  . GLU B  1 45  ? 2.92200   -27.46700 26.23400 1.000 24.16089  ? 145 GLU B CA  1 
ATOM   1513 C  C   . GLU B  1 45  ? 3.09600   -28.18900 24.90800 1.000 23.28186  ? 145 GLU B C   1 
ATOM   1514 O  O   . GLU B  1 45  ? 4.21900   -28.59700 24.59900 1.000 28.15603  ? 145 GLU B O   1 
ATOM   1515 C  CB  . GLU B  1 45  ? 3.08700   -28.47000 27.37800 1.000 27.60302  ? 145 GLU B CB  1 
ATOM   1516 C  CG  . GLU B  1 45  ? 3.21800   -27.83800 28.75300 1.000 42.06319  ? 145 GLU B CG  1 
ATOM   1517 C  CD  . GLU B  1 45  ? 4.47000   -26.99100 28.92500 1.000 58.01090  ? 145 GLU B CD  1 
ATOM   1518 O  OE1 . GLU B  1 45  ? 5.35100   -26.97800 28.03200 1.000 63.47081  ? 145 GLU B OE1 1 
ATOM   1519 O  OE2 . GLU B  1 45  ? 4.57100   -26.33700 29.98300 1.000 65.21030  ? 145 GLU B OE2 1 
ATOM   1520 N  N   . THR B  1 46  ? 2.03200   -28.35000 24.11800 1.000 21.23670  ? 146 THR B N   1 
ATOM   1521 C  CA  . THR B  1 46  ? 2.19600   -28.99800 22.81900 1.000 23.27502  ? 146 THR B CA  1 
ATOM   1522 C  C   . THR B  1 46  ? 2.68900   -28.04900 21.74000 1.000 24.64350  ? 146 THR B C   1 
ATOM   1523 O  O   . THR B  1 46  ? 3.02200   -28.50700 20.64300 1.000 26.10969  ? 146 THR B O   1 
ATOM   1524 C  CB  . THR B  1 46  ? 0.88500   -29.62100 22.33100 1.000 23.48982  ? 146 THR B CB  1 
ATOM   1525 O  OG1 . THR B  1 46  ? -0.04600  -28.58000 21.99500 1.000 24.86224  ? 146 THR B OG1 1 
ATOM   1526 C  CG2 . THR B  1 46  ? 0.28700   -30.56400 23.39900 1.000 23.41173  ? 146 THR B CG2 1 
ATOM   1527 N  N   . GLY B  1 47  ? 2.72200   -26.74600 21.99600 1.000 20.71992  ? 147 GLY B N   1 
ATOM   1528 C  CA  . GLY B  1 47  ? 3.08500   -25.78000 20.98400 1.000 18.25878  ? 147 GLY B CA  1 
ATOM   1529 C  C   . GLY B  1 47  ? 4.50800   -25.27300 21.14100 1.000 25.56605  ? 147 GLY B C   1 
ATOM   1530 O  O   . GLY B  1 47  ? 5.32800   -25.82200 21.88300 1.000 24.47496  ? 147 GLY B O   1 
ATOM   1531 N  N   . ILE B  1 48  ? 4.79400   -24.20100 20.41400 1.000 19.74069  ? 148 ILE B N   1 
ATOM   1532 C  CA  . ILE B  1 48  ? 6.06700   -23.49700 20.51600 1.000 22.20770  ? 148 ILE B CA  1 
ATOM   1533 C  C   . ILE B  1 48  ? 5.91200   -22.43700 21.60300 1.000 19.87387  ? 148 ILE B C   1 
ATOM   1534 O  O   . ILE B  1 48  ? 5.03800   -21.56700 21.47500 1.000 20.59087  ? 148 ILE B O   1 
ATOM   1535 C  CB  . ILE B  1 48  ? 6.46700   -22.84700 19.18700 1.000 19.99975  ? 148 ILE B CB  1 
ATOM   1536 C  CG1 . ILE B  1 48  ? 6.60100   -23.89800 18.07200 1.000 26.24816  ? 148 ILE B CG1 1 
ATOM   1537 C  CG2 . ILE B  1 48  ? 7.76700   -22.04000 19.36900 1.000 23.47057  ? 148 ILE B CG2 1 
ATOM   1538 C  CD1 . ILE B  1 48  ? 7.71700   -24.89700 18.32200 1.000 33.43753  ? 148 ILE B CD1 1 
ATOM   1539 N  N   . PRO B  1 49  ? 6.72700   -22.46000 22.65700 1.000 20.52034  ? 149 PRO B N   1 
ATOM   1540 C  CA  . PRO B  1 49  ? 6.56600   -21.47000 23.72700 1.000 20.44811  ? 149 PRO B CA  1 
ATOM   1541 C  C   . PRO B  1 49  ? 6.96700   -20.07300 23.28100 1.000 25.37796  ? 149 PRO B C   1 
ATOM   1542 O  O   . PRO B  1 49  ? 7.99400   -19.87400 22.62600 1.000 22.84568  ? 149 PRO B O   1 
ATOM   1543 C  CB  . PRO B  1 49  ? 7.49200   -21.99100 24.83400 1.000 22.30772  ? 149 PRO B CB  1 
ATOM   1544 C  CG  . PRO B  1 49  ? 8.46400   -22.86300 24.15100 1.000 29.23254  ? 149 PRO B CG  1 
ATOM   1545 C  CD  . PRO B  1 49  ? 7.77100   -23.45300 22.96300 1.000 24.88826  ? 149 PRO B CD  1 
ATOM   1546 N  N   . LEU B  1 50  ? 6.13100   -19.10100 23.64500 1.000 21.23740  ? 150 LEU B N   1 
ATOM   1547 C  CA  . LEU B  1 50  ? 6.38600   -17.68800 23.39900 1.000 20.57873  ? 150 LEU B CA  1 
ATOM   1548 C  C   . LEU B  1 50  ? 6.41600   -16.88800 24.68600 1.000 23.13914  ? 150 LEU B C   1 
ATOM   1549 O  O   . LEU B  1 50  ? 7.34500   -16.09400 24.89300 1.000 21.93518  ? 150 LEU B O   1 
ATOM   1550 C  CB  . LEU B  1 50  ? 5.32000   -17.09800 22.45300 1.000 20.87142  ? 150 LEU B CB  1 
ATOM   1551 C  CG  . LEU B  1 50  ? 5.62700   -17.11000 20.95400 1.000 27.16659  ? 150 LEU B CG  1 
ATOM   1552 C  CD1 . LEU B  1 50  ? 5.49000   -18.51400 20.39500 1.000 29.16202  ? 150 LEU B CD1 1 
ATOM   1553 C  CD2 . LEU B  1 50  ? 4.70900   -16.13600 20.22700 1.000 41.04240  ? 150 LEU B CD2 1 
ATOM   1554 N  N   . ASN B  1 51  ? 5.42700   -17.08900 25.56000 1.000 22.17178  ? 151 ASN B N   1 
ATOM   1555 C  CA  . ASN B  1 51  ? 5.29800   -16.35200 26.81000 1.000 20.73304  ? 151 ASN B CA  1 
ATOM   1556 C  C   . ASN B  1 51  ? 5.50500   -14.85900 26.58200 1.000 24.36214  ? 151 ASN B C   1 
ATOM   1557 O  O   . ASN B  1 51  ? 6.26300   -14.18700 27.28600 1.000 24.51869  ? 151 ASN B O   1 
ATOM   1558 C  CB  . ASN B  1 51  ? 6.26900   -16.90200 27.85900 1.000 24.20891  ? 151 ASN B CB  1 
ATOM   1559 C  CG  . ASN B  1 51  ? 6.02100   -18.36400 28.13700 1.000 32.19899  ? 151 ASN B CG  1 
ATOM   1560 O  OD1 . ASN B  1 51  ? 6.88700   -19.20300 27.90000 1.000 39.86577  ? 151 ASN B OD1 1 
ATOM   1561 N  ND2 . ASN B  1 51  ? 4.81600   -18.68300 28.61400 1.000 31.48760  ? 151 ASN B ND2 1 
ATOM   1562 N  N   . ALA B  1 52  ? 4.80700   -14.33500 25.58200 1.000 20.69863  ? 152 ALA B N   1 
ATOM   1563 C  CA  . ALA B  1 52  ? 5.08100   -13.00500 25.06800 1.000 22.87929  ? 152 ALA B CA  1 
ATOM   1564 C  C   . ALA B  1 52  ? 3.99100   -12.02900 25.48400 1.000 30.38013  ? 152 ALA B C   1 
ATOM   1565 O  O   . ALA B  1 52  ? 2.86700   -12.41600 25.82500 1.000 24.75090  ? 152 ALA B O   1 
ATOM   1566 C  CB  . ALA B  1 52  ? 5.20900   -13.02600 23.53800 1.000 21.80151  ? 152 ALA B CB  1 
ATOM   1567 N  N   . LYS B  1 53  ? 4.34900   -10.74900 25.46700 1.000 22.29632  ? 153 LYS B N   1 
ATOM   1568 C  CA  . LYS B  1 53  ? 3.35300   -9.70500  25.62600 1.000 21.96168  ? 153 LYS B CA  1 
ATOM   1569 C  C   . LYS B  1 53  ? 2.41200   -9.69600  24.42700 1.000 20.55730  ? 153 LYS B C   1 
ATOM   1570 O  O   . LYS B  1 53  ? 2.79600   -10.03200 23.30600 1.000 23.80562  ? 153 LYS B O   1 
ATOM   1571 C  CB  . LYS B  1 53  ? 4.01400   -8.33100  25.77200 1.000 22.14417  ? 153 LYS B CB  1 
ATOM   1572 C  CG  . LYS B  1 53  ? 4.84200   -8.17900  27.04100 1.000 30.31984  ? 153 LYS B CG  1 
ATOM   1573 C  CD  . LYS B  1 53  ? 5.22000   -6.74200  27.29900 1.000 38.00731  ? 153 LYS B CD  1 
ATOM   1574 C  CE  . LYS B  1 53  ? 6.00500   -6.63000  28.60400 1.000 48.49450  ? 153 LYS B CE  1 
ATOM   1575 N  NZ  . LYS B  1 53  ? 6.85300   -5.40200  28.65100 1.000 59.15326  ? 153 LYS B NZ  1 
ATOM   1576 N  N   . VAL B  1 54  ? 1.17800   -9.28900  24.67800 1.000 24.92347  ? 154 VAL B N   1 
ATOM   1577 C  CA  . VAL B  1 54  ? 0.15400   -9.23000  23.64100 1.000 23.78311  ? 154 VAL B CA  1 
ATOM   1578 C  C   . VAL B  1 54  ? 0.38800   -7.99800  22.77900 1.000 23.67427  ? 154 VAL B C   1 
ATOM   1579 O  O   . VAL B  1 54  ? 0.65000   -6.90400  23.29000 1.000 25.38294  ? 154 VAL B O   1 
ATOM   1580 C  CB  . VAL B  1 54  ? -1.25500  -9.19400  24.27100 1.000 23.34076  ? 154 VAL B CB  1 
ATOM   1581 C  CG1 . VAL B  1 54  ? -2.32300  -9.11800  23.17900 1.000 32.57168  ? 154 VAL B CG1 1 
ATOM   1582 C  CG2 . VAL B  1 54  ? -1.50400  -10.39400 25.15900 1.000 26.40773  ? 154 VAL B CG2 1 
ATOM   1583 N  N   . SER B  1 55  ? 0.30600   -8.17300  21.46200 1.000 21.58953  ? 155 SER B N   1 
ATOM   1584 C  CA  . SER B  1 55  ? 0.14900   -7.05300  20.54600 1.000 23.54928  ? 155 SER B CA  1 
ATOM   1585 C  C   . SER B  1 55  ? -0.62800  -7.54800  19.34200 1.000 22.39530  ? 155 SER B C   1 
ATOM   1586 O  O   . SER B  1 55  ? -0.60800  -8.74100  19.02700 1.000 24.51057  ? 155 SER B O   1 
ATOM   1587 C  CB  . SER B  1 55  ? 1.48800   -6.46500  20.08700 1.000 25.43026  ? 155 SER B CB  1 
ATOM   1588 O  OG  . SER B  1 55  ? 2.28700   -7.45600  19.46200 1.000 22.17890  ? 155 SER B OG  1 
ATOM   1589 N  N   . SER B  1 56  ? -1.31200  -6.62200  18.66900 1.000 21.11032  ? 156 SER B N   1 
ATOM   1590 C  CA  . SER B  1 56  ? -1.96700  -6.99400  17.42400 1.000 19.32936  ? 156 SER B CA  1 
ATOM   1591 C  C   . SER B  1 56  ? -0.93300  -7.40400  16.38800 1.000 22.93345  ? 156 SER B C   1 
ATOM   1592 O  O   . SER B  1 56  ? -1.15600  -8.34300  15.61500 1.000 21.53232  ? 156 SER B O   1 
ATOM   1593 C  CB  . SER B  1 56  ? -2.82800  -5.84000  16.91200 1.000 25.24405  ? 156 SER B CB  1 
ATOM   1594 O  OG  . SER B  1 56  ? -2.01900  -4.70000  16.68200 1.000 30.71435  ? 156 SER B OG  1 
ATOM   1595 N  N   . GLU B  1 57  ? 0.23600   -6.75300  16.41100 1.000 22.35986  ? 157 GLU B N   1 
ATOM   1596 C  CA  . GLU B  1 57  ? 1.27800   -7.04100  15.43400 1.000 22.44965  ? 157 GLU B CA  1 
ATOM   1597 C  C   . GLU B  1 57  ? 1.80500   -8.46400  15.58400 1.000 25.55596  ? 157 GLU B C   1 
ATOM   1598 O  O   . GLU B  1 57  ? 1.97000   -9.18400  14.59500 1.000 20.91376  ? 157 GLU B O   1 
ATOM   1599 C  CB  . GLU B  1 57  ? 2.41400   -6.02600  15.57900 1.000 22.93794  ? 157 GLU B CB  1 
ATOM   1600 C  CG  . GLU B  1 57  ? 2.02800   -4.62100  15.17700 1.000 27.99453  ? 157 GLU B CG  1 
ATOM   1601 C  CD  . GLU B  1 57  ? 1.45600   -3.78700  16.31200 1.000 33.50361  ? 157 GLU B CD  1 
ATOM   1602 O  OE1 . GLU B  1 57  ? 1.18400   -4.33100  17.40500 1.000 27.59481  ? 157 GLU B OE1 1 
ATOM   1603 O  OE2 . GLU B  1 57  ? 1.28500   -2.56800  16.10200 1.000 35.75020  ? 157 GLU B OE2 1 
ATOM   1604 N  N   . LEU B  1 58  ? 2.07500   -8.89600  16.81900 1.000 21.44899  ? 158 LEU B N   1 
ATOM   1605 C  CA  . LEU B  1 58  ? 2.56600   -10.25900 16.98800 1.000 18.85958  ? 158 LEU B CA  1 
ATOM   1606 C  C   . LEU B  1 58  ? 1.50600   -11.27600 16.58900 1.000 22.49767  ? 158 LEU B C   1 
ATOM   1607 O  O   . LEU B  1 58  ? 1.81300   -12.28000 15.93300 1.000 19.81992  ? 158 LEU B O   1 
ATOM   1608 C  CB  . LEU B  1 58  ? 3.02300   -10.48500 18.42600 1.000 21.02505  ? 158 LEU B CB  1 
ATOM   1609 C  CG  . LEU B  1 58  ? 3.48800   -11.89800 18.77500 1.000 22.39766  ? 158 LEU B CG  1 
ATOM   1610 C  CD1 . LEU B  1 58  ? 4.57800   -12.39700 17.84600 1.000 25.42691  ? 158 LEU B CD1 1 
ATOM   1611 C  CD2 . LEU B  1 58  ? 3.96500   -11.93500 20.23600 1.000 22.30667  ? 158 LEU B CD2 1 
ATOM   1612 N  N   . LEU B  1 59  ? 0.25100   -11.02800 16.96000 1.000 20.66179  ? 159 LEU B N   1 
ATOM   1613 C  CA  . LEU B  1 59  ? -0.82000  -11.95000 16.58800 1.000 23.33515  ? 159 LEU B CA  1 
ATOM   1614 C  C   . LEU B  1 59  ? -0.89400  -12.12100 15.07800 1.000 22.77716  ? 159 LEU B C   1 
ATOM   1615 O  O   . LEU B  1 59  ? -0.99800  -13.24500 14.57300 1.000 20.72782  ? 159 LEU B O   1 
ATOM   1616 C  CB  . LEU B  1 59  ? -2.15800  -11.45300 17.13100 1.000 20.99183  ? 159 LEU B CB  1 
ATOM   1617 C  CG  . LEU B  1 59  ? -2.36100  -11.65100 18.63700 1.000 23.01619  ? 159 LEU B CG  1 
ATOM   1618 C  CD1 . LEU B  1 59  ? -3.63600  -10.98900 19.11400 1.000 22.71927  ? 159 LEU B CD1 1 
ATOM   1619 C  CD2 . LEU B  1 59  ? -2.34000  -13.14200 19.00100 1.000 19.97050  ? 159 LEU B CD2 1 
ATOM   1620 N  N   . ILE B  1 60  ? -0.84800  -11.01000 14.34000 1.000 22.08639  ? 160 ILE B N   1 
ATOM   1621 C  CA  . ILE B  1 60  ? -0.87800  -11.08100 12.88300 1.000 21.34061  ? 160 ILE B CA  1 
ATOM   1622 C  C   . ILE B  1 60  ? 0.33300   -11.84000 12.35800 1.000 23.40542  ? 160 ILE B C   1 
ATOM   1623 O  O   . ILE B  1 60  ? 0.20900   -12.72700 11.50800 1.000 23.12902  ? 160 ILE B O   1 
ATOM   1624 C  CB  . ILE B  1 60  ? -0.96000  -9.66900  12.27400 1.000 23.18884  ? 160 ILE B CB  1 
ATOM   1625 C  CG1 . ILE B  1 60  ? -2.33600  -9.05200  12.55600 1.000 25.08325  ? 160 ILE B CG1 1 
ATOM   1626 C  CG2 . ILE B  1 60  ? -0.71800  -9.74300  10.77100 1.000 26.40810  ? 160 ILE B CG2 1 
ATOM   1627 C  CD1 . ILE B  1 60  ? -2.35700  -7.53600  12.46800 1.000 24.20538  ? 160 ILE B CD1 1 
ATOM   1628 N  N   . ASN B  1 61  ? 1.52600   -11.51700 12.87300 1.000 22.29643  ? 161 ASN B N   1 
ATOM   1629 C  CA  . ASN B  1 61  ? 2.72700   -12.14700 12.34600 1.000 18.28601  ? 161 ASN B CA  1 
ATOM   1630 C  C   . ASN B  1 61  ? 2.72200   -13.65900 12.56400 1.000 23.50227  ? 161 ASN B C   1 
ATOM   1631 O  O   . ASN B  1 61  ? 3.26200   -14.39900 11.73500 1.000 23.06985  ? 161 ASN B O   1 
ATOM   1632 C  CB  . ASN B  1 61  ? 3.97600   -11.49900 12.95700 1.000 20.44266  ? 161 ASN B CB  1 
ATOM   1633 C  CG  . ASN B  1 61  ? 4.56100   -10.40500 12.05000 1.000 19.13235  ? 161 ASN B CG  1 
ATOM   1634 O  OD1 . ASN B  1 61  ? 4.06000   -9.27800  12.00400 1.000 24.17762  ? 161 ASN B OD1 1 
ATOM   1635 N  ND2 . ASN B  1 61  ? 5.61500   -10.74300 11.32000 1.000 20.85372  ? 161 ASN B ND2 1 
ATOM   1636 N  N   . ILE B  1 62  ? 2.10000   -14.13400 13.64800 1.000 20.18888  ? 162 ILE B N   1 
ATOM   1637 C  CA  . ILE B  1 62  ? 2.05800   -15.57100 13.92700 1.000 17.38102  ? 162 ILE B CA  1 
ATOM   1638 C  C   . ILE B  1 62  ? 1.26200   -16.32000 12.86500 1.000 19.42607  ? 162 ILE B C   1 
ATOM   1639 O  O   . ILE B  1 62  ? 1.63100   -17.43100 12.45800 1.000 19.65228  ? 162 ILE B O   1 
ATOM   1640 C  CB  . ILE B  1 62  ? 1.47200   -15.81900 15.33600 1.000 20.05013  ? 162 ILE B CB  1 
ATOM   1641 C  CG1 . ILE B  1 62  ? 2.46600   -15.38700 16.40700 1.000 18.54864  ? 162 ILE B CG1 1 
ATOM   1642 C  CG2 . ILE B  1 62  ? 1.07500   -17.28500 15.50100 1.000 23.30953  ? 162 ILE B CG2 1 
ATOM   1643 C  CD1 . ILE B  1 62  ? 1.80700   -15.24400 17.80300 1.000 21.67152  ? 162 ILE B CD1 1 
ATOM   1644 N  N   . PHE B  1 63  ? 0.16800   -15.73400 12.38900 1.000 23.34258  ? 163 PHE B N   1 
ATOM   1645 C  CA  . PHE B  1 63  ? -0.76900  -16.46300 11.54800 1.000 20.06405  ? 163 PHE B CA  1 
ATOM   1646 C  C   . PHE B  1 63  ? -0.53700  -16.28300 10.05000 1.000 20.18643  ? 163 PHE B C   1 
ATOM   1647 O  O   . PHE B  1 63  ? -1.30100  -16.84400 9.26200  1.000 24.10416  ? 163 PHE B O   1 
ATOM   1648 C  CB  . PHE B  1 63  ? -2.20700  -16.05200 11.88500 1.000 21.31821  ? 163 PHE B CB  1 
ATOM   1649 C  CG  . PHE B  1 63  ? -2.68600  -16.58400 13.21500 1.000 19.68634  ? 163 PHE B CG  1 
ATOM   1650 C  CD1 . PHE B  1 63  ? -2.88700  -17.94400 13.39300 1.000 20.29217  ? 163 PHE B CD1 1 
ATOM   1651 C  CD2 . PHE B  1 63  ? -2.95100  -15.72100 14.27000 1.000 20.75580  ? 163 PHE B CD2 1 
ATOM   1652 C  CE1 . PHE B  1 63  ? -3.32400  -18.45200 14.61400 1.000 18.84173  ? 163 PHE B CE1 1 
ATOM   1653 C  CE2 . PHE B  1 63  ? -3.39500  -16.21300 15.50100 1.000 21.38399  ? 163 PHE B CE2 1 
ATOM   1654 C  CZ  . PHE B  1 63  ? -3.59400  -17.57900 15.66400 1.000 17.76662  ? 163 PHE B CZ  1 
ATOM   1655 N  N   . ILE B  1 64  ? 0.48700   -15.54000 9.64700  1.000 22.91240  ? 164 ILE B N   1 
ATOM   1656 C  CA  . ILE B  1 64  ? 0.78600   -15.36200 8.22500  1.000 23.10488  ? 164 ILE B CA  1 
ATOM   1657 C  C   . ILE B  1 64  ? 0.88200   -16.73000 7.55800  1.000 23.62108  ? 164 ILE B C   1 
ATOM   1658 O  O   . ILE B  1 64  ? 1.55100   -17.63800 8.06900  1.000 24.79719  ? 164 ILE B O   1 
ATOM   1659 C  CB  . ILE B  1 64  ? 2.07200   -14.55000 8.00800  1.000 25.47912  ? 164 ILE B CB  1 
ATOM   1660 C  CG1 . ILE B  1 64  ? 1.93300   -13.14500 8.59900  1.000 28.35155  ? 164 ILE B CG1 1 
ATOM   1661 C  CG2 . ILE B  1 64  ? 2.38100   -14.45600 6.49500  1.000 23.98886  ? 164 ILE B CG2 1 
ATOM   1662 C  CD1 . ILE B  1 64  ? 0.80200   -12.31900 7.97700  1.000 32.16471  ? 164 ILE B CD1 1 
ATOM   1663 N  N   . PRO B  1 65  ? 0.19300   -16.93700 6.43900  1.000 24.50792  ? 165 PRO B N   1 
ATOM   1664 C  CA  . PRO B  1 65  ? 0.18500   -18.26400 5.81300  1.000 28.92258  ? 165 PRO B CA  1 
ATOM   1665 C  C   . PRO B  1 65  ? 1.58300   -18.71500 5.41000  1.000 26.05189  ? 165 PRO B C   1 
ATOM   1666 O  O   . PRO B  1 65  ? 2.44600   -17.90500 5.06700  1.000 28.01853  ? 165 PRO B O   1 
ATOM   1667 C  CB  . PRO B  1 65  ? -0.71200  -18.06600 4.58800  1.000 26.92567  ? 165 PRO B CB  1 
ATOM   1668 C  CG  . PRO B  1 65  ? -1.59400  -16.88700 4.96800  1.000 32.17834  ? 165 PRO B CG  1 
ATOM   1669 C  CD  . PRO B  1 65  ? -0.71700  -15.98800 5.78100  1.000 27.91000  ? 165 PRO B CD  1 
ATOM   1670 N  N   . ASN B  1 66  ? 1.79500   -20.03300 5.46400  1.000 29.34827  ? 166 ASN B N   1 
ATOM   1671 C  CA  . ASN B  1 66  ? 3.01500   -20.70000 5.01300  1.000 30.71530  ? 166 ASN B CA  1 
ATOM   1672 C  C   . ASN B  1 66  ? 4.21000   -20.41100 5.91600  1.000 33.09705  ? 166 ASN B C   1 
ATOM   1673 O  O   . ASN B  1 66  ? 5.36200   -20.56900 5.49000  1.000 34.99548  ? 166 ASN B O   1 
ATOM   1674 C  CB  . ASN B  1 66  ? 3.36200   -20.33600 3.55900  1.000 31.39861  ? 166 ASN B CB  1 
ATOM   1675 C  CG  . ASN B  1 66  ? 2.18700   -20.50800 2.61000  1.000 56.20489  ? 166 ASN B CG  1 
ATOM   1676 O  OD1 . ASN B  1 66  ? 1.38300   -21.43200 2.75200  1.000 53.86004  ? 166 ASN B OD1 1 
ATOM   1677 N  ND2 . ASN B  1 66  ? 2.08300   -19.61200 1.63200  1.000 54.67888  ? 166 ASN B ND2 1 
ATOM   1678 N  N   . THR B  1 67  ? 3.96500   -19.98800 7.15300  1.000 24.31241  ? 167 THR B N   1 
ATOM   1679 C  CA  . THR B  1 67  ? 5.02700   -19.70000 8.10900  1.000 25.22001  ? 167 THR B CA  1 
ATOM   1680 C  C   . THR B  1 67  ? 5.12400   -20.78700 9.17100  1.000 26.56265  ? 167 THR B C   1 
ATOM   1681 O  O   . THR B  1 67  ? 4.18700   -21.56400 9.37300  1.000 26.51054  ? 167 THR B O   1 
ATOM   1682 C  CB  . THR B  1 67  ? 4.77300   -18.35200 8.80100  1.000 27.60641  ? 167 THR B CB  1 
ATOM   1683 O  OG1 . THR B  1 67  ? 3.51700   -18.41000 9.48600  1.000 24.97479  ? 167 THR B OG1 1 
ATOM   1684 C  CG2 . THR B  1 67  ? 4.74900   -17.22200 7.77500  1.000 29.08609  ? 167 THR B CG2 1 
ATOM   1685 N  N   . PRO B  1 68  ? 6.24800   -20.85700 9.89600  1.000 24.17729  ? 168 PRO B N   1 
ATOM   1686 C  CA  . PRO B  1 68  ? 6.38300   -21.90500 10.92300 1.000 25.02052  ? 168 PRO B CA  1 
ATOM   1687 C  C   . PRO B  1 68  ? 5.26300   -21.93000 11.97200 1.000 25.60822  ? 168 PRO B C   1 
ATOM   1688 O  O   . PRO B  1 68  ? 4.86000   -23.01900 12.39800 1.000 28.15042  ? 168 PRO B O   1 
ATOM   1689 C  CB  . PRO B  1 68  ? 7.75100   -21.58900 11.54800 1.000 22.34557  ? 168 PRO B CB  1 
ATOM   1690 C  CG  . PRO B  1 68  ? 8.53100   -20.92500 10.45000 1.000 31.54877  ? 168 PRO B CG  1 
ATOM   1691 C  CD  . PRO B  1 68  ? 7.53600   -20.18900 9.59900  1.000 23.86826  ? 168 PRO B CD  1 
ATOM   1692 N  N   . LEU B  1 69  ? 4.74300   -20.77800 12.39700 1.000 27.78991  ? 169 LEU B N   1 
ATOM   1693 C  CA  . LEU B  1 69  ? 3.81700   -20.73200 13.53100 1.000 25.00558  ? 169 LEU B CA  1 
ATOM   1694 C  C   . LEU B  1 69  ? 2.33900   -20.70500 13.14000 1.000 24.59156  ? 169 LEU B C   1 
ATOM   1695 O  O   . LEU B  1 69  ? 1.48700   -20.65900 14.03500 1.000 26.18169  ? 169 LEU B O   1 
ATOM   1696 C  CB  . LEU B  1 69  ? 4.10900   -19.50600 14.40200 1.000 22.58226  ? 169 LEU B CB  1 
ATOM   1697 C  CG  . LEU B  1 69  ? 5.46900   -19.46400 15.10900 1.000 23.22046  ? 169 LEU B CG  1 
ATOM   1698 C  CD1 . LEU B  1 69  ? 5.62600   -18.17000 15.91400 1.000 22.82835  ? 169 LEU B CD1 1 
ATOM   1699 C  CD2 . LEU B  1 69  ? 5.62200   -20.66300 16.00800 1.000 21.16788  ? 169 LEU B CD2 1 
ATOM   1700 N  N   . HIS B  1 70  ? 2.00200   -20.73600 11.85200 1.000 26.39315  ? 170 HIS B N   1 
ATOM   1701 C  CA  . HIS B  1 70  ? 0.64000   -20.36500 11.47700 1.000 23.29338  ? 170 HIS B CA  1 
ATOM   1702 C  C   . HIS B  1 70  ? -0.37200  -21.49800 11.63000 1.000 28.09441  ? 170 HIS B C   1 
ATOM   1703 O  O   . HIS B  1 70  ? -1.57400  -21.22100 11.72300 1.000 33.15651  ? 170 HIS B O   1 
ATOM   1704 C  CB  . HIS B  1 70  ? 0.60900   -19.80100 10.05300 1.000 25.83909  ? 170 HIS B CB  1 
ATOM   1705 C  CG  . HIS B  1 70  ? 0.44400   -20.83100 8.97300  1.000 32.13504  ? 170 HIS B CG  1 
ATOM   1706 N  ND1 . HIS B  1 70  ? 1.38000   -21.81400 8.72600  1.000 34.07551  ? 170 HIS B ND1 1 
ATOM   1707 C  CD2 . HIS B  1 70  ? -0.54600  -21.01900 8.06700  1.000 38.16952  ? 170 HIS B CD2 1 
ATOM   1708 C  CE1 . HIS B  1 70  ? 0.97000   -22.56700 7.71900  1.000 35.05117  ? 170 HIS B CE1 1 
ATOM   1709 N  NE2 . HIS B  1 70  ? -0.19200  -22.10000 7.29600  1.000 34.48795  ? 170 HIS B NE2 1 
ATOM   1710 N  N   . ASP B  1 71  ? 0.06500   -22.74700 11.68700 1.000 24.44287  ? 171 ASP B N   1 
ATOM   1711 C  CA  . ASP B  1 71  ? -0.85600  -23.86300 11.84200 1.000 34.44353  ? 171 ASP B CA  1 
ATOM   1712 C  C   . ASP B  1 71  ? -0.93000  -24.24600 13.31100 1.000 26.18770  ? 171 ASP B C   1 
ATOM   1713 O  O   . ASP B  1 71  ? 0.07000   -24.16300 14.02600 1.000 33.67219  ? 171 ASP B O   1 
ATOM   1714 C  CB  . ASP B  1 71  ? -0.42500  -25.06400 11.00100 1.000 39.54277  ? 171 ASP B CB  1 
ATOM   1715 C  CG  . ASP B  1 71  ? -0.90500  -24.96600 9.56500  1.000 43.04523  ? 171 ASP B CG  1 
ATOM   1716 O  OD1 . ASP B  1 71  ? -1.96200  -24.33800 9.32400  1.000 36.46591  ? 171 ASP B OD1 1 
ATOM   1717 O  OD2 . ASP B  1 71  ? -0.22100  -25.51200 8.67700  1.000 39.94559  ? 171 ASP B OD2 1 
ATOM   1718 N  N   . GLY B  1 72  ? -2.11300  -24.66200 13.75000 1.000 27.57096  ? 172 GLY B N   1 
ATOM   1719 C  CA  . GLY B  1 72  ? -2.34400  -24.91000 15.16000 1.000 23.37778  ? 172 GLY B CA  1 
ATOM   1720 C  C   . GLY B  1 72  ? -2.85900  -23.67400 15.86100 1.000 27.07912  ? 172 GLY B C   1 
ATOM   1721 O  O   . GLY B  1 72  ? -3.01900  -22.59400 15.28300 1.000 23.03666  ? 172 GLY B O   1 
ATOM   1722 N  N   . ALA B  1 73  ? -3.12300  -23.83100 17.15200 1.000 19.45617  ? 173 ALA B N   1 
ATOM   1723 C  CA  . ALA B  1 73  ? -3.72200  -22.75400 17.92900 1.000 22.51756  ? 173 ALA B CA  1 
ATOM   1724 C  C   . ALA B  1 73  ? -2.67200  -21.91200 18.63900 1.000 22.44173  ? 173 ALA B C   1 
ATOM   1725 O  O   . ALA B  1 73  ? -1.66300  -22.43300 19.13200 1.000 18.65813  ? 173 ALA B O   1 
ATOM   1726 C  CB  . ALA B  1 73  ? -4.70100  -23.31500 18.96800 1.000 21.30221  ? 173 ALA B CB  1 
ATOM   1727 N  N   . VAL B  1 74  ? -2.92100  -20.60500 18.69900 1.000 17.98665  ? 174 VAL B N   1 
ATOM   1728 C  CA  . VAL B  1 74  ? -2.29100  -19.73900 19.70300 1.000 16.80512  ? 174 VAL B CA  1 
ATOM   1729 C  C   . VAL B  1 74  ? -3.13800  -19.82300 20.95800 1.000 19.24941  ? 174 VAL B C   1 
ATOM   1730 O  O   . VAL B  1 74  ? -4.36700  -19.73100 20.88000 1.000 17.97986  ? 174 VAL B O   1 
ATOM   1731 C  CB  . VAL B  1 74  ? -2.21400  -18.28500 19.21300 1.000 18.69949  ? 174 VAL B CB  1 
ATOM   1732 C  CG1 . VAL B  1 74  ? -1.87400  -17.34600 20.37800 1.000 19.94990  ? 174 VAL B CG1 1 
ATOM   1733 C  CG2 . VAL B  1 74  ? -1.18300  -18.16500 18.10300 1.000 20.06669  ? 174 VAL B CG2 1 
ATOM   1734 N  N   . ILE B  1 75  ? -2.50200  -19.98800 22.11200 1.000 16.94663  ? 175 ILE B N   1 
ATOM   1735 C  CA  . ILE B  1 75  ? -3.20400  -19.97600 23.38500 1.000 17.24460  ? 175 ILE B CA  1 
ATOM   1736 C  C   . ILE B  1 75  ? -2.71600  -18.78100 24.18100 1.000 17.19149  ? 175 ILE B C   1 
ATOM   1737 O  O   . ILE B  1 75  ? -1.50300  -18.59300 24.34900 1.000 20.53707  ? 175 ILE B O   1 
ATOM   1738 C  CB  . ILE B  1 75  ? -3.00600  -21.27700 24.17100 1.000 17.52092  ? 175 ILE B CB  1 
ATOM   1739 C  CG1 . ILE B  1 75  ? -3.57000  -22.44700 23.36400 1.000 19.39297  ? 175 ILE B CG1 1 
ATOM   1740 C  CG2 . ILE B  1 75  ? -3.71600  -21.17300 25.54000 1.000 17.95622  ? 175 ILE B CG2 1 
ATOM   1741 C  CD1 . ILE B  1 75  ? -3.31500  -23.81100 23.98200 1.000 21.77790  ? 175 ILE B CD1 1 
ATOM   1742 N  N   . MET B  1 76  ? -3.66300  -17.97300 24.64900 1.000 17.45711  ? 176 MET B N   1 
ATOM   1743 C  CA  . MET B  1 76  ? -3.40100  -16.78400 25.44500 1.000 17.63782  ? 176 MET B CA  1 
ATOM   1744 C  C   . MET B  1 76  ? -3.76000  -17.02900 26.89500 1.000 22.41403  ? 176 MET B C   1 
ATOM   1745 O  O   . MET B  1 76  ? -4.68600  -17.78400 27.21000 1.000 23.50725  ? 176 MET B O   1 
ATOM   1746 C  CB  . MET B  1 76  ? -4.20000  -15.58000 24.95600 1.000 19.48375  ? 176 MET B CB  1 
ATOM   1747 C  CG  . MET B  1 76  ? -3.69200  -15.03300 23.65200 1.000 21.60144  ? 176 MET B CG  1 
ATOM   1748 S  SD  . MET B  1 76  ? -4.64100  -13.61600 23.08600 1.000 28.37392  ? 176 MET B SD  1 
ATOM   1749 C  CE  . MET B  1 76  ? -4.58800  -12.57700 24.54400 1.000 31.89381  ? 176 MET B CE  1 
ATOM   1750 N  N   . LYS B  1 77  ? -2.99600  -16.39000 27.76900 1.000 21.54661  ? 177 LYS B N   1 
ATOM   1751 C  CA  . LYS B  1 77  ? -3.35300  -16.26300 29.17200 1.000 25.46364  ? 177 LYS B CA  1 
ATOM   1752 C  C   . LYS B  1 77  ? -3.57800  -14.77600 29.45600 1.000 21.88319  ? 177 LYS B C   1 
ATOM   1753 O  O   . LYS B  1 77  ? -3.55100  -13.94600 28.54100 1.000 37.39164  ? 177 LYS B O   1 
ATOM   1754 C  CB  . LYS B  1 77  ? -2.27300  -16.91100 30.03600 1.000 24.20742  ? 177 LYS B CB  1 
ATOM   1755 C  CG  . LYS B  1 77  ? -2.19600  -18.41100 29.80000 1.000 22.16811  ? 177 LYS B CG  1 
ATOM   1756 C  CD  . LYS B  1 77  ? -1.06600  -19.08100 30.52300 1.000 27.31910  ? 177 LYS B CD  1 
ATOM   1757 C  CE  . LYS B  1 77  ? -1.22900  -18.90500 32.01400 1.000 25.17439  ? 177 LYS B CE  1 
ATOM   1758 N  NZ  . LYS B  1 77  ? -0.52500  -19.98700 32.75100 1.000 37.35631  ? 177 LYS B NZ  1 
ATOM   1759 N  N   . ASN B  1 78  ? -3.83100  -14.44200 30.71900 1.000 31.18359  ? 178 ASN B N   1 
ATOM   1760 C  CA  . ASN B  1 78  ? -4.05200  -13.03700 31.04100 1.000 34.94913  ? 178 ASN B CA  1 
ATOM   1761 C  C   . ASN B  1 78  ? -2.87400  -12.19300 30.57100 1.000 36.95486  ? 178 ASN B C   1 
ATOM   1762 O  O   . ASN B  1 78  ? -1.74800  -12.35600 31.05600 1.000 35.40260  ? 178 ASN B O   1 
ATOM   1763 C  CB  . ASN B  1 78  ? -4.28900  -12.82400 32.53700 1.000 37.79450  ? 178 ASN B CB  1 
ATOM   1764 C  CG  . ASN B  1 78  ? -4.74600  -11.40600 32.84700 1.000 57.25089  ? 178 ASN B CG  1 
ATOM   1765 O  OD1 . ASN B  1 78  ? -5.82700  -10.98600 32.42800 1.000 58.86137  ? 178 ASN B OD1 1 
ATOM   1766 N  ND2 . ASN B  1 78  ? -3.92200  -10.65800 33.56900 1.000 52.35669  ? 178 ASN B ND2 1 
ATOM   1767 N  N   . ASN B  1 79  ? -3.15100  -11.32000 29.59500 1.000 31.12308  ? 179 ASN B N   1 
ATOM   1768 C  CA  . ASN B  1 79  ? -2.19400  -10.37100 29.02200 1.000 35.30302  ? 179 ASN B CA  1 
ATOM   1769 C  C   . ASN B  1 79  ? -0.93500  -11.06300 28.50300 1.000 38.41224  ? 179 ASN B C   1 
ATOM   1770 O  O   . ASN B  1 79  ? 0.15800   -10.50000 28.54900 1.000 37.04128  ? 179 ASN B O   1 
ATOM   1771 C  CB  . ASN B  1 79  ? -1.83400  -9.27300  30.02600 1.000 48.08088  ? 179 ASN B CB  1 
ATOM   1772 C  CG  . ASN B  1 79  ? -3.04400  -8.45800  30.46000 1.000 49.69585  ? 179 ASN B CG  1 
ATOM   1773 O  OD1 . ASN B  1 79  ? -3.96400  -8.21200  29.67200 1.000 49.06126  ? 179 ASN B OD1 1 
ATOM   1774 N  ND2 . ASN B  1 79  ? -3.05700  -8.05100  31.72500 1.000 52.45480  ? 179 ASN B ND2 1 
ATOM   1775 N  N   . GLU B  1 80  ? -1.08400  -12.28200 27.98300 1.000 29.67656  ? 180 GLU B N   1 
ATOM   1776 C  CA  . GLU B  1 80  ? 0.06900   -13.05500 27.53100 1.000 21.75763  ? 180 GLU B CA  1 
ATOM   1777 C  C   . GLU B  1 80  ? -0.29300  -13.94400 26.34900 1.000 22.78731  ? 180 GLU B C   1 
ATOM   1778 O  O   . GLU B  1 80  ? -1.34200  -14.58500 26.35700 1.000 24.37738  ? 180 GLU B O   1 
ATOM   1779 C  CB  . GLU B  1 80  ? 0.59500   -13.93700 28.66800 1.000 26.69090  ? 180 GLU B CB  1 
ATOM   1780 C  CG  . GLU B  1 80  ? 1.74600   -14.84000 28.26700 1.000 26.27781  ? 180 GLU B CG  1 
ATOM   1781 C  CD  . GLU B  1 80  ? 2.22300   -15.69600 29.42600 1.000 43.48594  ? 180 GLU B CD  1 
ATOM   1782 O  OE1 . GLU B  1 80  ? 1.39300   -16.04900 30.28900 1.000 43.12428  ? 180 GLU B OE1 1 
ATOM   1783 O  OE2 . GLU B  1 80  ? 3.42800   -16.00300 29.48900 1.000 35.30990  ? 180 GLU B OE2 1 
ATOM   1784 N  N   . ILE B  1 81  ? 0.58000   -13.98000 25.34400 1.000 20.30557  ? 181 ILE B N   1 
ATOM   1785 C  CA  . ILE B  1 81  ? 0.54400   -15.01700 24.31200 1.000 17.34362  ? 181 ILE B CA  1 
ATOM   1786 C  C   . ILE B  1 81  ? 1.47100   -16.14200 24.77700 1.000 23.30949  ? 181 ILE B C   1 
ATOM   1787 O  O   . ILE B  1 81  ? 2.69800   -16.01600 24.71500 1.000 22.64792  ? 181 ILE B O   1 
ATOM   1788 C  CB  . ILE B  1 81  ? 0.96000   -14.46100 22.95100 1.000 21.67590  ? 181 ILE B CB  1 
ATOM   1789 C  CG1 . ILE B  1 81  ? -0.02400  -13.36400 22.50500 1.000 25.89202  ? 181 ILE B CG1 1 
ATOM   1790 C  CG2 . ILE B  1 81  ? 1.02800   -15.59000 21.93300 1.000 21.66594  ? 181 ILE B CG2 1 
ATOM   1791 C  CD1 . ILE B  1 81  ? 0.46900   -12.52300 21.29500 1.000 24.57131  ? 181 ILE B CD1 1 
ATOM   1792 N  N   . ALA B  1 82  ? 0.88700   -17.25200 25.26300 1.000 20.34832  ? 182 ALA B N   1 
ATOM   1793 C  CA  . ALA B  1 82  ? 1.68500   -18.30400 25.88700 1.000 18.44365  ? 182 ALA B CA  1 
ATOM   1794 C  C   . ALA B  1 82  ? 2.44200   -19.14800 24.86400 1.000 16.93339  ? 182 ALA B C   1 
ATOM   1795 O  O   . ALA B  1 82  ? 3.64100   -19.41900 25.03100 1.000 19.82996  ? 182 ALA B O   1 
ATOM   1796 C  CB  . ALA B  1 82  ? 0.80100   -19.20500 26.76200 1.000 22.50071  ? 182 ALA B CB  1 
ATOM   1797 N  N   . ALA B  1 83  ? 1.76100   -19.58900 23.80900 1.000 19.46636  ? 183 ALA B N   1 
ATOM   1798 C  CA  . ALA B  1 83  ? 2.37400   -20.50500 22.85900 1.000 16.62176  ? 183 ALA B CA  1 
ATOM   1799 C  C   . ALA B  1 83  ? 1.62200   -20.45100 21.53900 1.000 19.84684  ? 183 ALA B C   1 
ATOM   1800 O  O   . ALA B  1 83  ? 0.45300   -20.06300 21.48100 1.000 19.76576  ? 183 ALA B O   1 
ATOM   1801 C  CB  . ALA B  1 83  ? 2.38600   -21.93400 23.41100 1.000 22.69950  ? 183 ALA B CB  1 
ATOM   1802 N  N   . ALA B  1 84  ? 2.31500   -20.83700 20.46900 1.000 20.28574  ? 184 ALA B N   1 
ATOM   1803 C  CA  . ALA B  1 84  ? 1.68000   -20.93300 19.16300 1.000 17.87360  ? 184 ALA B CA  1 
ATOM   1804 C  C   . ALA B  1 84  ? 1.81400   -22.35600 18.63400 1.000 19.37208  ? 184 ALA B C   1 
ATOM   1805 O  O   . ALA B  1 84  ? 2.56900   -23.17500 19.15900 1.000 22.34467  ? 184 ALA B O   1 
ATOM   1806 C  CB  . ALA B  1 84  ? 2.28800   -19.92900 18.16900 1.000 21.53324  ? 184 ALA B CB  1 
ATOM   1807 N  N   . ALA B  1 85  ? 1.04900   -22.64500 17.58600 1.000 20.52467  ? 185 ALA B N   1 
ATOM   1808 C  CA  . ALA B  1 85  ? 1.07700   -23.94800 16.92000 1.000 27.50672  ? 185 ALA B CA  1 
ATOM   1809 C  C   . ALA B  1 85  ? 0.72700   -25.07400 17.89300 1.000 26.51508  ? 185 ALA B C   1 
ATOM   1810 O  O   . ALA B  1 85  ? 1.30300   -26.16200 17.85000 1.000 26.24224  ? 185 ALA B O   1 
ATOM   1811 C  CB  . ALA B  1 85  ? 2.43000   -24.19600 16.24200 1.000 30.53842  ? 185 ALA B CB  1 
ATOM   1812 N  N   . CYS B  1 86  ? -0.23000  -24.80400 18.77500 1.000 21.56149  ? 186 CYS B N   1 
ATOM   1813 C  CA  . CYS B  1 86  ? -0.66300  -25.77600 19.76700 1.000 20.78517  ? 186 CYS B CA  1 
ATOM   1814 C  C   . CYS B  1 86  ? -1.68000  -26.74600 19.19200 1.000 21.49678  ? 186 CYS B C   1 
ATOM   1815 O  O   . CYS B  1 86  ? -2.46300  -26.40500 18.30500 1.000 22.95453  ? 186 CYS B O   1 
ATOM   1816 C  CB  . CYS B  1 86  ? -1.28900  -25.07000 20.96300 1.000 19.05693  ? 186 CYS B CB  1 
ATOM   1817 S  SG  . CYS B  1 86  ? -0.10400  -24.02600 21.84700 1.000 20.01041  ? 186 CYS B SG  1 
ATOM   1818 N  N   . TYR B  1 87  ? -1.69900  -27.94800 19.75300 1.000 20.89666  ? 187 TYR B N   1 
ATOM   1819 C  CA  . TYR B  1 87  ? -2.72200  -28.93500 19.44400 1.000 23.47932  ? 187 TYR B CA  1 
ATOM   1820 C  C   . TYR B  1 87  ? -3.91900  -28.75100 20.37000 1.000 25.34876  ? 187 TYR B C   1 
ATOM   1821 O  O   . TYR B  1 87  ? -3.76300  -28.40400 21.54700 1.000 24.71672  ? 187 TYR B O   1 
ATOM   1822 C  CB  . TYR B  1 87  ? -2.15500  -30.35000 19.58500 1.000 32.12256  ? 187 TYR B CB  1 
ATOM   1823 C  CG  . TYR B  1 87  ? -1.20800  -30.75100 18.47500 1.000 43.07478  ? 187 TYR B CG  1 
ATOM   1824 C  CD1 . TYR B  1 87  ? 0.13000   -30.36200 18.49500 1.000 44.12256  ? 187 TYR B CD1 1 
ATOM   1825 C  CD2 . TYR B  1 87  ? -1.65000  -31.52200 17.40500 1.000 48.65377  ? 187 TYR B CD2 1 
ATOM   1826 C  CE1 . TYR B  1 87  ? 0.99900   -30.72800 17.47800 1.000 50.76698  ? 187 TYR B CE1 1 
ATOM   1827 C  CE2 . TYR B  1 87  ? -0.78800  -31.89300 16.38000 1.000 51.87377  ? 187 TYR B CE2 1 
ATOM   1828 C  CZ  . TYR B  1 87  ? 0.53200   -31.49600 16.42200 1.000 51.21720  ? 187 TYR B CZ  1 
ATOM   1829 O  OH  . TYR B  1 87  ? 1.38300   -31.86600 15.40400 1.000 62.37446  ? 187 TYR B OH  1 
ATOM   1830 N  N   . LEU B  1 88  ? -5.11400  -28.95900 19.82200 1.000 24.10586  ? 188 LEU B N   1 
ATOM   1831 C  CA  . LEU B  1 88  ? -6.37400  -28.95200 20.54400 1.000 25.29554  ? 188 LEU B CA  1 
ATOM   1832 C  C   . LEU B  1 88  ? -7.14200  -30.22600 20.22500 1.000 29.67833  ? 188 LEU B C   1 
ATOM   1833 O  O   . LEU B  1 88  ? -7.00000  -30.78400 19.13100 1.000 28.48654  ? 188 LEU B O   1 
ATOM   1834 C  CB  . LEU B  1 88  ? -7.23800  -27.73600 20.16800 1.000 20.54607  ? 188 LEU B CB  1 
ATOM   1835 C  CG  . LEU B  1 88  ? -6.66600  -26.33700 20.40500 1.000 18.65495  ? 188 LEU B CG  1 
ATOM   1836 C  CD1 . LEU B  1 88  ? -7.66900  -25.28700 19.95000 1.000 19.90630  ? 188 LEU B CD1 1 
ATOM   1837 C  CD2 . LEU B  1 88  ? -6.30300  -26.15300 21.90000 1.000 22.12464  ? 188 LEU B CD2 1 
ATOM   1838 N  N   . PRO B  1 89  ? -7.97600  -30.69600 21.14800 1.000 24.81864  ? 189 PRO B N   1 
ATOM   1839 C  CA  . PRO B  1 89  ? -8.80000  -31.86800 20.84600 1.000 31.02305  ? 189 PRO B CA  1 
ATOM   1840 C  C   . PRO B  1 89  ? -9.81700  -31.52000 19.77400 1.000 27.03143  ? 189 PRO B C   1 
ATOM   1841 O  O   . PRO B  1 89  ? -10.33300 -30.40100 19.73300 1.000 27.25969  ? 189 PRO B O   1 
ATOM   1842 C  CB  . PRO B  1 89  ? -9.47700  -32.18700 22.18400 1.000 30.90206  ? 189 PRO B CB  1 
ATOM   1843 C  CG  . PRO B  1 89  ? -9.47000  -30.90500 22.94000 1.000 35.81028  ? 189 PRO B CG  1 
ATOM   1844 C  CD  . PRO B  1 89  ? -8.30900  -30.08300 22.44700 1.000 23.71273  ? 189 PRO B CD  1 
ATOM   1845 N  N   . LEU B  1 90  ? -10.09400 -32.47700 18.89700 1.000 24.45661  ? 190 LEU B N   1 
ATOM   1846 C  CA  . LEU B  1 90  ? -11.05100 -32.24900 17.82200 1.000 29.11286  ? 190 LEU B CA  1 
ATOM   1847 C  C   . LEU B  1 90  ? -12.43800 -32.68400 18.27400 1.000 34.49987  ? 190 LEU B C   1 
ATOM   1848 O  O   . LEU B  1 90  ? -12.61500 -33.81100 18.74100 1.000 34.83963  ? 190 LEU B O   1 
ATOM   1849 C  CB  . LEU B  1 90  ? -10.64100 -33.00300 16.55800 1.000 34.85344  ? 190 LEU B CB  1 
ATOM   1850 C  CG  . LEU B  1 90  ? -9.28700  -32.61300 15.96200 1.000 39.68345  ? 190 LEU B CG  1 
ATOM   1851 C  CD1 . LEU B  1 90  ? -9.03900  -33.39300 14.68800 1.000 47.49141  ? 190 LEU B CD1 1 
ATOM   1852 C  CD2 . LEU B  1 90  ? -9.21700  -31.11700 15.70000 1.000 35.14581  ? 190 LEU B CD2 1 
ATOM   1853 N  N   . SER B  1 91  ? -13.41400 -31.78600 18.13900 1.000 27.88117  ? 191 SER B N   1 
ATOM   1854 C  CA  . SER B  1 91  ? -14.78000 -32.10800 18.53200 1.000 29.09121  ? 191 SER B CA  1 
ATOM   1855 C  C   . SER B  1 91  ? -15.35900 -33.19400 17.64000 1.000 32.02486  ? 191 SER B C   1 
ATOM   1856 O  O   . SER B  1 91  ? -15.08600 -33.25700 16.43700 1.000 31.06949  ? 191 SER B O   1 
ATOM   1857 C  CB  . SER B  1 91  ? -15.68000 -30.86900 18.46300 1.000 24.90218  ? 191 SER B CB  1 
ATOM   1858 O  OG  . SER B  1 91  ? -17.05100 -31.22400 18.68600 1.000 29.02478  ? 191 SER B OG  1 
ATOM   1859 N  N   . GLU B  1 92  ? -16.19500 -34.03900 18.24400 1.000 29.79518  ? 192 GLU B N   1 
ATOM   1860 C  CA  . GLU B  1 92  ? -16.99400 -35.01700 17.52200 1.000 35.36786  ? 192 GLU B CA  1 
ATOM   1861 C  C   . GLU B  1 92  ? -18.45500 -34.60200 17.40500 1.000 34.03243  ? 192 GLU B C   1 
ATOM   1862 O  O   . GLU B  1 92  ? -19.29500 -35.42600 17.02400 1.000 34.27200  ? 192 GLU B O   1 
ATOM   1863 C  CB  . GLU B  1 92  ? -16.88200 -36.38900 18.19400 1.000 42.89063  ? 192 GLU B CB  1 
ATOM   1864 C  CG  . GLU B  1 92  ? -15.85800 -37.30800 17.53900 1.000 58.37125  ? 192 GLU B CG  1 
ATOM   1865 C  CD  . GLU B  1 92  ? -15.03400 -38.08900 18.54600 1.000 73.19418  ? 192 GLU B CD  1 
ATOM   1866 O  OE1 . GLU B  1 92  ? -15.56600 -38.42200 19.62700 1.000 74.85238  ? 192 GLU B OE1 1 
ATOM   1867 O  OE2 . GLU B  1 92  ? -13.84700 -38.36200 18.25600 1.000 80.65736  ? 192 GLU B OE2 1 
ATOM   1868 N  N   . SER B  1 93  ? -18.76800 -33.34400 17.69900 1.000 28.15301  ? 193 SER B N   1 
ATOM   1869 C  CA  . SER B  1 93  ? -20.14800 -32.87300 17.67100 1.000 29.71878  ? 193 SER B CA  1 
ATOM   1870 C  C   . SER B  1 93  ? -20.77000 -33.09500 16.29400 1.000 33.77752  ? 193 SER B C   1 
ATOM   1871 O  O   . SER B  1 93  ? -20.14400 -32.79200 15.27200 1.000 29.60104  ? 193 SER B O   1 
ATOM   1872 C  CB  . SER B  1 93  ? -20.20900 -31.38400 18.01700 1.000 28.67761  ? 193 SER B CB  1 
ATOM   1873 O  OG  . SER B  1 93  ? -21.48600 -30.83500 17.69400 1.000 29.60998  ? 193 SER B OG  1 
ATOM   1874 N  N   . PRO B  1 94  ? -22.00700 -33.59100 16.22600 1.000 33.82802  ? 194 PRO B N   1 
ATOM   1875 C  CA  . PRO B  1 94  ? -22.69900 -33.67000 14.93500 1.000 33.40274  ? 194 PRO B CA  1 
ATOM   1876 C  C   . PRO B  1 94  ? -23.21900 -32.33200 14.43600 1.000 33.91942  ? 194 PRO B C   1 
ATOM   1877 O  O   . PRO B  1 94  ? -23.79500 -32.28800 13.34500 1.000 37.74104  ? 194 PRO B O   1 
ATOM   1878 C  CB  . PRO B  1 94  ? -23.85600 -34.63600 15.22700 1.000 34.42064  ? 194 PRO B CB  1 
ATOM   1879 C  CG  . PRO B  1 94  ? -24.18200 -34.38300 16.65600 1.000 29.29120  ? 194 PRO B CG  1 
ATOM   1880 C  CD  . PRO B  1 94  ? -22.85600 -34.06000 17.33900 1.000 28.67116  ? 194 PRO B CD  1 
ATOM   1881 N  N   . PHE B  1 95  ? -23.03000 -31.24600 15.19100 1.000 28.74676  ? 195 PHE B N   1 
ATOM   1882 C  CA  . PHE B  1 95  ? -23.49700 -29.92400 14.79300 1.000 27.39510  ? 195 PHE B CA  1 
ATOM   1883 C  C   . PHE B  1 95  ? -22.41900 -29.08200 14.14000 1.000 41.07671  ? 195 PHE B C   1 
ATOM   1884 O  O   . PHE B  1 95  ? -22.60500 -27.87200 13.98800 1.000 40.03481  ? 195 PHE B O   1 
ATOM   1885 C  CB  . PHE B  1 95  ? -24.06000 -29.16500 15.98600 1.000 30.27917  ? 195 PHE B CB  1 
ATOM   1886 C  CG  . PHE B  1 95  ? -25.25900 -29.80000 16.58100 1.000 30.26507  ? 195 PHE B CG  1 
ATOM   1887 C  CD1 . PHE B  1 95  ? -26.51200 -29.56100 16.04800 1.000 30.09589  ? 195 PHE B CD1 1 
ATOM   1888 C  CD2 . PHE B  1 95  ? -25.14200 -30.64900 17.66100 1.000 29.87377  ? 195 PHE B CD2 1 
ATOM   1889 C  CE1 . PHE B  1 95  ? -27.62600 -30.14400 16.59600 1.000 32.24101  ? 195 PHE B CE1 1 
ATOM   1890 C  CE2 . PHE B  1 95  ? -26.26000 -31.23800 18.21000 1.000 28.58614  ? 195 PHE B CE2 1 
ATOM   1891 C  CZ  . PHE B  1 95  ? -27.50100 -30.98700 17.67300 1.000 30.42761  ? 195 PHE B CZ  1 
ATOM   1892 N  N   . ILE B  1 96  ? -21.30300 -29.68000 13.75600 1.000 38.41916  ? 196 ILE B N   1 
ATOM   1893 C  CA  . ILE B  1 96  ? -20.22600 -28.94100 13.11600 1.000 41.93749  ? 196 ILE B CA  1 
ATOM   1894 C  C   . ILE B  1 96  ? -20.39800 -29.06800 11.61200 1.000 44.21893  ? 196 ILE B C   1 
ATOM   1895 O  O   . ILE B  1 96  ? -20.31300 -30.17000 11.05500 1.000 42.48101  ? 196 ILE B O   1 
ATOM   1896 C  CB  . ILE B  1 96  ? -18.85300 -29.44600 13.57800 1.000 38.94840  ? 196 ILE B CB  1 
ATOM   1897 C  CG1 . ILE B  1 96  ? -18.65600 -29.08700 15.05200 1.000 35.11107  ? 196 ILE B CG1 1 
ATOM   1898 C  CG2 . ILE B  1 96  ? -17.75300 -28.85600 12.71500 1.000 45.61297  ? 196 ILE B CG2 1 
ATOM   1899 C  CD1 . ILE B  1 96  ? -17.28300 -29.37600 15.56000 1.000 35.73330  ? 196 ILE B CD1 1 
ATOM   1900 N  N   . SER B  1 97  ? -20.65600 -27.93700 10.96200 1.000 39.93698  ? 197 SER B N   1 
ATOM   1901 C  CA  . SER B  1 97  ? -21.00200 -27.94700 9.55100  1.000 46.31247  ? 197 SER B CA  1 
ATOM   1902 C  C   . SER B  1 97  ? -19.91800 -28.62600 8.72200  1.000 45.81854  ? 197 SER B C   1 
ATOM   1903 O  O   . SER B  1 97  ? -18.71900 -28.51400 8.99900  1.000 42.96724  ? 197 SER B O   1 
ATOM   1904 C  CB  . SER B  1 97  ? -21.23500 -26.52400 9.04200  1.000 49.58922  ? 197 SER B CB  1 
ATOM   1905 O  OG  . SER B  1 97  ? -21.37800 -26.52300 7.63200  1.000 56.36427  ? 197 SER B OG  1 
ATOM   1906 N  N   . LYS B  1 98  ? -20.36600 -29.33600 7.68400  1.000 54.58632  ? 198 LYS B N   1 
ATOM   1907 C  CA  . LYS B  1 98  ? -19.45400 -30.08400 6.82900  1.000 61.81305  ? 198 LYS B CA  1 
ATOM   1908 C  C   . LYS B  1 98  ? -18.50800 -29.16700 6.06200  1.000 47.63013  ? 198 LYS B C   1 
ATOM   1909 O  O   . LYS B  1 98  ? -17.41200 -29.59200 5.68100  1.000 50.06473  ? 198 LYS B O   1 
ATOM   1910 C  CB  . LYS B  1 98  ? -20.25900 -30.96200 5.86500  1.000 65.76037  ? 198 LYS B CB  1 
ATOM   1911 C  CG  . LYS B  1 98  ? -21.54500 -30.30700 5.35800  1.000 61.34997  ? 198 LYS B CG  1 
ATOM   1912 C  CD  . LYS B  1 98  ? -22.33500 -31.22300 4.41600  1.000 70.17597  ? 198 LYS B CD  1 
ATOM   1913 C  CE  . LYS B  1 98  ? -23.51800 -30.48300 3.78700  1.000 82.82594  ? 198 LYS B CE  1 
ATOM   1914 N  NZ  . LYS B  1 98  ? -24.38100 -31.34300 2.91900  1.000 69.50039  ? 198 LYS B NZ  1 
ATOM   1915 N  N   . GLU B  1 99  ? -18.90800 -27.92100 5.81700  1.000 47.18103  ? 199 GLU B N   1 
ATOM   1916 C  CA  . GLU B  1 99  ? -18.05500 -26.99700 5.08500  1.000 49.09842  ? 199 GLU B CA  1 
ATOM   1917 C  C   . GLU B  1 99  ? -16.99100 -26.34900 5.96400  1.000 39.84045  ? 199 GLU B C   1 
ATOM   1918 O  O   . GLU B  1 99  ? -16.17600 -25.57600 5.45000  1.000 53.84630  ? 199 GLU B O   1 
ATOM   1919 C  CB  . GLU B  1 99  ? -18.89700 -25.90900 4.40500  1.000 70.41244  ? 199 GLU B CB  1 
ATOM   1920 C  CG  . GLU B  1 99  ? -19.71000 -25.02700 5.34700  1.000 71.34350  ? 199 GLU B CG  1 
ATOM   1921 C  CD  . GLU B  1 99  ? -19.82500 -23.58900 4.85100  1.000 87.73879  ? 199 GLU B CD  1 
ATOM   1922 O  OE1 . GLU B  1 99  ? -18.87900 -22.80000 5.08400  1.000 76.83685  ? 199 GLU B OE1 1 
ATOM   1923 O  OE2 . GLU B  1 99  ? -20.85400 -23.25200 4.21900  1.000 82.27248  ? 199 GLU B OE2 1 
ATOM   1924 N  N   . LEU B  1 100 ? -16.96400 -26.64400 7.26000  1.000 46.85034  ? 200 LEU B N   1 
ATOM   1925 C  CA  . LEU B  1 100 ? -16.00500 -26.00500 8.15100  1.000 42.09184  ? 200 LEU B CA  1 
ATOM   1926 C  C   . LEU B  1 100 ? -14.68500 -26.76900 8.18900  1.000 45.97640  ? 200 LEU B C   1 
ATOM   1927 O  O   . LEU B  1 100 ? -14.60800 -27.95000 7.84300  1.000 51.24699  ? 200 LEU B O   1 
ATOM   1928 C  CB  . LEU B  1 100 ? -16.58000 -25.87600 9.56300  1.000 33.13934  ? 200 LEU B CB  1 
ATOM   1929 C  CG  . LEU B  1 100 ? -17.72600 -24.86400 9.63600  1.000 37.61308  ? 200 LEU B CG  1 
ATOM   1930 C  CD1 . LEU B  1 100 ? -18.26400 -24.76400 11.05300 1.000 35.64024  ? 200 LEU B CD1 1 
ATOM   1931 C  CD2 . LEU B  1 100 ? -17.26100 -23.50000 9.13600  1.000 37.82655  ? 200 LEU B CD2 1 
ATOM   1932 N  N   . GLY B  1 101 ? -13.63900 -26.07400 8.64300  1.000 38.45239  ? 201 GLY B N   1 
ATOM   1933 C  CA  . GLY B  1 101 ? -12.30000 -26.61500 8.64900  1.000 43.54661  ? 201 GLY B CA  1 
ATOM   1934 C  C   . GLY B  1 101 ? -11.91200 -27.26800 9.96800  1.000 39.20996  ? 201 GLY B C   1 
ATOM   1935 O  O   . GLY B  1 101 ? -12.64600 -27.26300 10.95600 1.000 33.57050  ? 201 GLY B O   1 
ATOM   1936 N  N   . THR B  1 102 ? -10.70600 -27.84600 9.96000  1.000 33.22265  ? 202 THR B N   1 
ATOM   1937 C  CA  . THR B  1 102 ? -10.14200 -28.42000 11.17700 1.000 35.60568  ? 202 THR B CA  1 
ATOM   1938 C  C   . THR B  1 102 ? -10.02000 -27.37800 12.28200 1.000 29.35864  ? 202 THR B C   1 
ATOM   1939 O  O   . THR B  1 102 ? -10.20700 -27.70200 13.46600 1.000 27.42092  ? 202 THR B O   1 
ATOM   1940 C  CB  . THR B  1 102 ? -8.78000  -29.05400 10.86700 1.000 41.26538  ? 202 THR B CB  1 
ATOM   1941 O  OG1 . THR B  1 102 ? -8.97000  -30.17500 9.99500  1.000 50.74805  ? 202 THR B OG1 1 
ATOM   1942 C  CG2 . THR B  1 102 ? -8.08600  -29.52900 12.13400 1.000 40.25455  ? 202 THR B CG2 1 
ATOM   1943 N  N   . ARG B  1 103 ? -9.75300  -26.11700 11.92200 1.000 23.52081  ? 203 ARG B N   1 
ATOM   1944 C  CA  . ARG B  1 103 ? -9.67300  -25.07400 12.94900 1.000 26.05946  ? 203 ARG B CA  1 
ATOM   1945 C  C   . ARG B  1 103 ? -10.97200 -24.98000 13.74100 1.000 26.16765  ? 203 ARG B C   1 
ATOM   1946 O  O   . ARG B  1 103 ? -10.94700 -24.82100 14.96700 1.000 21.39708  ? 203 ARG B O   1 
ATOM   1947 C  CB  . ARG B  1 103 ? -9.33800  -23.72000 12.32500 1.000 26.84694  ? 203 ARG B CB  1 
ATOM   1948 C  CG  . ARG B  1 103 ? -7.87400  -23.51400 11.97300 1.000 33.56675  ? 203 ARG B CG  1 
ATOM   1949 C  CD  . ARG B  1 103 ? -7.65300  -22.10900 11.42000 1.000 35.97087  ? 203 ARG B CD  1 
ATOM   1950 N  NE  . ARG B  1 103 ? -6.27000  -21.89500 11.01600 1.000 35.77447  ? 203 ARG B NE  1 
ATOM   1951 C  CZ  . ARG B  1 103 ? -5.83800  -21.98000 9.76600  1.000 38.70488  ? 203 ARG B CZ  1 
ATOM   1952 N  NH1 . ARG B  1 103 ? -6.67100  -22.21600 8.76300  1.000 35.72146  ? 203 ARG B NH1 1 
ATOM   1953 N  NH2 . ARG B  1 103 ? -4.54000  -21.82300 9.51700  1.000 40.34899  ? 203 ARG B NH2 1 
ATOM   1954 N  N   . HIS B  1 104 ? -12.12200 -25.07000 13.05800 1.000 21.58531  ? 204 HIS B N   1 
ATOM   1955 C  CA  . HIS B  1 104 ? -13.39600 -24.98300 13.76800 1.000 21.37922  ? 204 HIS B CA  1 
ATOM   1956 C  C   . HIS B  1 104 ? -13.63400 -26.21500 14.62200 1.000 22.59201  ? 204 HIS B C   1 
ATOM   1957 O  O   . HIS B  1 104 ? -14.14900 -26.10900 15.74200 1.000 21.55677  ? 204 HIS B O   1 
ATOM   1958 C  CB  . HIS B  1 104 ? -14.54300 -24.78000 12.77500 1.000 20.89629  ? 204 HIS B CB  1 
ATOM   1959 C  CG  . HIS B  1 104 ? -14.39100 -23.54000 11.96400 1.000 20.59819  ? 204 HIS B CG  1 
ATOM   1960 N  ND1 . HIS B  1 104 ? -13.62200 -23.50400 10.82300 1.000 24.83308  ? 204 HIS B ND1 1 
ATOM   1961 C  CD2 . HIS B  1 104 ? -14.82600 -22.27200 12.16500 1.000 22.45934  ? 204 HIS B CD2 1 
ATOM   1962 C  CE1 . HIS B  1 104 ? -13.63200 -22.28100 10.32400 1.000 29.52905  ? 204 HIS B CE1 1 
ATOM   1963 N  NE2 . HIS B  1 104 ? -14.34600 -21.51100 11.12000 1.000 20.89596  ? 204 HIS B NE2 1 
ATOM   1964 N  N   . ARG B  1 105 ? -13.26700 -27.39200 14.11200 1.000 22.17054  ? 205 ARG B N   1 
ATOM   1965 C  CA  . ARG B  1 105 ? -13.43700 -28.61500 14.88900 1.000 23.49759  ? 205 ARG B CA  1 
ATOM   1966 C  C   . ARG B  1 105 ? -12.57500 -28.59000 16.14400 1.000 24.88331  ? 205 ARG B C   1 
ATOM   1967 O  O   . ARG B  1 105 ? -13.00600 -29.04100 17.21100 1.000 25.51957  ? 205 ARG B O   1 
ATOM   1968 C  CB  . ARG B  1 105 ? -13.09600 -29.83200 14.02700 1.000 29.82024  ? 205 ARG B CB  1 
ATOM   1969 C  CG  . ARG B  1 105 ? -13.52600 -31.14100 14.64600 1.000 41.94426  ? 205 ARG B CG  1 
ATOM   1970 C  CD  . ARG B  1 105 ? -13.53100 -32.27500 13.62900 1.000 44.41945  ? 205 ARG B CD  1 
ATOM   1971 N  NE  . ARG B  1 105 ? -14.56000 -32.11100 12.60800 1.000 54.50554  ? 205 ARG B NE  1 
ATOM   1972 C  CZ  . ARG B  1 105 ? -15.83300 -32.45900 12.75700 1.000 61.79099  ? 205 ARG B CZ  1 
ATOM   1973 N  NH1 . ARG B  1 105 ? -16.28700 -32.94900 13.90100 1.000 47.44852  ? 205 ARG B NH1 1 
ATOM   1974 N  NH2 . ARG B  1 105 ? -16.67100 -32.31200 11.73400 1.000 57.12407  ? 205 ARG B NH2 1 
ATOM   1975 N  N   . ALA B  1 106 ? -11.36000 -28.05100 16.03100 1.000 22.00924  ? 206 ALA B N   1 
ATOM   1976 C  CA  . ALA B  1 106 ? -10.47300 -27.92800 17.18900 1.000 21.13814  ? 206 ALA B CA  1 
ATOM   1977 C  C   . ALA B  1 106 ? -10.99600 -26.90200 18.18300 1.000 20.79090  ? 206 ALA B C   1 
ATOM   1978 O  O   . ALA B  1 106 ? -10.95300 -27.11900 19.40500 1.000 21.95071  ? 206 ALA B O   1 
ATOM   1979 C  CB  . ALA B  1 106 ? -9.07400  -27.54500 16.71100 1.000 24.69890  ? 206 ALA B CB  1 
ATOM   1980 N  N   . ALA B  1 107 ? -11.50900 -25.77800 17.68400 1.000 19.42800  ? 207 ALA B N   1 
ATOM   1981 C  CA  . ALA B  1 107 ? -12.02100 -24.75900 18.59300 1.000 20.50127  ? 207 ALA B CA  1 
ATOM   1982 C  C   . ALA B  1 107 ? -13.20900 -25.28200 19.38400 1.000 21.05412  ? 207 ALA B C   1 
ATOM   1983 O  O   . ALA B  1 107 ? -13.30000 -25.08700 20.59900 1.000 20.85523  ? 207 ALA B O   1 
ATOM   1984 C  CB  . ALA B  1 107 ? -12.40000 -23.51200 17.79800 1.000 22.06653  ? 207 ALA B CB  1 
ATOM   1985 N  N   . VAL B  1 108 ? -14.16200 -25.92800 18.70400 1.000 19.17912  ? 208 VAL B N   1 
ATOM   1986 C  CA  . VAL B  1 108 ? -15.27500 -26.50100 19.45400 1.000 20.06804  ? 208 VAL B CA  1 
ATOM   1987 C  C   . VAL B  1 108 ? -14.77000 -27.56900 20.41500 1.000 21.69020  ? 208 VAL B C   1 
ATOM   1988 O  O   . VAL B  1 108 ? -15.22800 -27.65400 21.55700 1.000 22.41597  ? 208 VAL B O   1 
ATOM   1989 C  CB  . VAL B  1 108 ? -16.35200 -27.05800 18.51200 1.000 22.76000  ? 208 VAL B CB  1 
ATOM   1990 C  CG1 . VAL B  1 108 ? -17.46200 -27.71700 19.35100 1.000 19.84596  ? 208 VAL B CG1 1 
ATOM   1991 C  CG2 . VAL B  1 108 ? -16.91400 -25.93500 17.65000 1.000 23.59332  ? 208 VAL B CG2 1 
ATOM   1992 N  N   . GLY B  1 109 ? -13.78600 -28.36200 19.98200 1.000 23.15058  ? 209 GLY B N   1 
ATOM   1993 C  CA  . GLY B  1 109 ? -13.23400 -29.39800 20.84800 1.000 21.30919  ? 209 GLY B CA  1 
ATOM   1994 C  C   . GLY B  1 109 ? -12.69100 -28.86900 22.16500 1.000 24.89156  ? 209 GLY B C   1 
ATOM   1995 O  O   . GLY B  1 109 ? -13.00100 -29.40100 23.23700 1.000 25.08416  ? 209 GLY B O   1 
ATOM   1996 N  N   . ILE B  1 110 ? -11.87100 -27.81400 22.11100 1.000 21.34094  ? 210 ILE B N   1 
ATOM   1997 C  CA  . ILE B  1 110 ? -11.31700 -27.28300 23.36500 1.000 21.48160  ? 210 ILE B CA  1 
ATOM   1998 C  C   . ILE B  1 110 ? -12.40900 -26.60800 24.18600 1.000 25.66473  ? 210 ILE B C   1 
ATOM   1999 O  O   . ILE B  1 110 ? -12.35000 -26.60200 25.42300 1.000 23.63405  ? 210 ILE B O   1 
ATOM   2000 C  CB  . ILE B  1 110 ? -10.13300 -26.33100 23.09300 1.000 19.09649  ? 210 ILE B CB  1 
ATOM   2001 C  CG1 . ILE B  1 110 ? -9.34100  -26.05400 24.38100 1.000 21.94381  ? 210 ILE B CG1 1 
ATOM   2002 C  CG2 . ILE B  1 110 ? -10.59900 -24.98100 22.53100 1.000 17.19017  ? 210 ILE B CG2 1 
ATOM   2003 C  CD1 . ILE B  1 110 ? -8.72700  -27.30300 25.01000 1.000 26.00194  ? 210 ILE B CD1 1 
ATOM   2004 N  N   . SER B  1 111 ? -13.44200 -26.07000 23.52700 1.000 20.91892  ? 211 SER B N   1 
ATOM   2005 C  CA  . SER B  1 111 ? -14.54400 -25.42700 24.24400 1.000 20.91192  ? 211 SER B CA  1 
ATOM   2006 C  C   . SER B  1 111 ? -15.41300 -26.43200 24.99400 1.000 23.44314  ? 211 SER B C   1 
ATOM   2007 O  O   . SER B  1 111 ? -16.14000 -26.04200 25.91500 1.000 25.03419  ? 211 SER B O   1 
ATOM   2008 C  CB  . SER B  1 111 ? -15.41500 -24.62600 23.26100 1.000 21.18672  ? 211 SER B CB  1 
ATOM   2009 O  OG  . SER B  1 111 ? -16.37000 -25.46200 22.62300 1.000 22.87233  ? 211 SER B OG  1 
ATOM   2010 N  N   . GLU B  1 112 ? -15.35100 -27.71100 24.62800 1.000 20.78166  ? 212 GLU B N   1 
ATOM   2011 C  CA  . GLU B  1 112 ? -16.14400 -28.73300 25.30200 1.000 22.62326  ? 212 GLU B CA  1 
ATOM   2012 C  C   . GLU B  1 112 ? -15.53100 -29.18000 26.61700 1.000 33.83369  ? 212 GLU B C   1 
ATOM   2013 O  O   . GLU B  1 112 ? -16.25200 -29.69300 27.48200 1.000 32.25974  ? 212 GLU B O   1 
ATOM   2014 C  CB  . GLU B  1 112 ? -16.33200 -29.94200 24.37400 1.000 30.03661  ? 212 GLU B CB  1 
ATOM   2015 C  CG  . GLU B  1 112 ? -17.23400 -29.65400 23.15400 1.000 27.21415  ? 212 GLU B CG  1 
ATOM   2016 C  CD  . GLU B  1 112 ? -17.13700 -30.71200 22.05600 1.000 29.61476  ? 212 GLU B CD  1 
ATOM   2017 O  OE1 . GLU B  1 112 ? -16.26500 -31.60400 22.14600 1.000 30.79597  ? 212 GLU B OE1 1 
ATOM   2018 O  OE2 . GLU B  1 112 ? -17.93500 -30.64100 21.09800 1.000 31.06911  ? 212 GLU B OE2 1 
ATOM   2019 N  N   . VAL B  1 113 ? -14.22600 -28.99100 26.79800 1.000 27.87538  ? 213 VAL B N   1 
ATOM   2020 C  CA  . VAL B  1 113 ? -13.52900 -29.50500 27.96800 1.000 29.51028  ? 213 VAL B CA  1 
ATOM   2021 C  C   . VAL B  1 113 ? -12.85300 -28.41400 28.78100 1.000 27.77928  ? 213 VAL B C   1 
ATOM   2022 O  O   . VAL B  1 113 ? -12.14600 -28.73000 29.74600 1.000 28.93785  ? 213 VAL B O   1 
ATOM   2023 C  CB  . VAL B  1 113 ? -12.50900 -30.59400 27.57300 1.000 30.58305  ? 213 VAL B CB  1 
ATOM   2024 C  CG1 . VAL B  1 113 ? -13.20700 -31.75400 26.87800 1.000 27.71233  ? 213 VAL B CG1 1 
ATOM   2025 C  CG2 . VAL B  1 113 ? -11.38200 -30.01000 26.71700 1.000 26.31550  ? 213 VAL B CG2 1 
ATOM   2026 N  N   . THR B  1 114 ? -13.03200 -27.14500 28.41100 1.000 25.29485  ? 214 THR B N   1 
ATOM   2027 C  CA  . THR B  1 114 ? -12.54900 -25.97800 29.15000 1.000 20.97825  ? 214 THR B CA  1 
ATOM   2028 C  C   . THR B  1 114 ? -13.61600 -24.89500 29.08500 1.000 28.36055  ? 214 THR B C   1 
ATOM   2029 O  O   . THR B  1 114 ? -14.52500 -24.94900 28.25900 1.000 27.68517  ? 214 THR B O   1 
ATOM   2030 C  CB  . THR B  1 114 ? -11.24800 -25.41100 28.56400 1.000 28.70828  ? 214 THR B CB  1 
ATOM   2031 O  OG1 . THR B  1 114 ? -11.51900 -24.86000 27.25700 1.000 24.23508  ? 214 THR B OG1 1 
ATOM   2032 C  CG2 . THR B  1 114 ? -10.18600 -26.48900 28.44300 1.000 28.36544  ? 214 THR B CG2 1 
ATOM   2033 N  N   . ASP B  1 115 ? -13.47700 -23.86500 29.92100 1.000 24.77631  ? 215 ASP B N   1 
ATOM   2034 C  CA  . ASP B  1 115 ? -14.32000 -22.68000 29.81000 1.000 23.54016  ? 215 ASP B CA  1 
ATOM   2035 C  C   . ASP B  1 115 ? -13.67400 -21.60000 28.95900 1.000 22.62693  ? 215 ASP B C   1 
ATOM   2036 O  O   . ASP B  1 115 ? -14.04900 -20.42500 29.07100 1.000 27.22023  ? 215 ASP B O   1 
ATOM   2037 C  CB  . ASP B  1 115 ? -14.65400 -22.12400 31.19800 1.000 29.37002  ? 215 ASP B CB  1 
ATOM   2038 C  CG  . ASP B  1 115 ? -13.44600 -21.51000 31.88000 1.000 30.86831  ? 215 ASP B CG  1 
ATOM   2039 O  OD1 . ASP B  1 115 ? -12.31400 -21.87600 31.50900 1.000 27.69526  ? 215 ASP B OD1 1 
ATOM   2040 O  OD2 . ASP B  1 115 ? -13.63100 -20.65700 32.77200 1.000 31.03543  ? 215 ASP B OD2 1 
ATOM   2041 N  N   . SER B  1 116 ? -12.69400 -21.97100 28.13700 1.000 22.00529  ? 216 SER B N   1 
ATOM   2042 C  CA  . SER B  1 116 ? -11.98400 -21.00600 27.31900 1.000 20.74128  ? 216 SER B CA  1 
ATOM   2043 C  C   . SER B  1 116 ? -12.90400 -20.42500 26.24900 1.000 22.44882  ? 216 SER B C   1 
ATOM   2044 O  O   . SER B  1 116 ? -13.96400 -20.97500 25.92400 1.000 24.73725  ? 216 SER B O   1 
ATOM   2045 C  CB  . SER B  1 116 ? -10.77700 -21.65200 26.62700 1.000 22.37261  ? 216 SER B CB  1 
ATOM   2046 O  OG  . SER B  1 116 ? -11.19100 -22.73500 25.79300 1.000 22.01567  ? 216 SER B OG  1 
ATOM   2047 N  N   . LEU B  1 117 ? -12.47200 -19.30000 25.69300 1.000 18.55102  ? 217 LEU B N   1 
ATOM   2048 C  CA  . LEU B  1 117 ? -13.12400 -18.68400 24.54900 1.000 20.60336  ? 217 LEU B CA  1 
ATOM   2049 C  C   . LEU B  1 117 ? -12.17400 -18.77900 23.36500 1.000 21.93826  ? 217 LEU B C   1 
ATOM   2050 O  O   . LEU B  1 117 ? -11.02900 -18.32400 23.44800 1.000 20.01129  ? 217 LEU B O   1 
ATOM   2051 C  CB  . LEU B  1 117 ? -13.49200 -17.22400 24.83800 1.000 21.52306  ? 217 LEU B CB  1 
ATOM   2052 C  CG  . LEU B  1 117 ? -14.19800 -16.45600 23.71000 1.000 26.92229  ? 217 LEU B CG  1 
ATOM   2053 C  CD1 . LEU B  1 117 ? -15.02900 -15.34400 24.28000 1.000 41.23672  ? 217 LEU B CD1 1 
ATOM   2054 C  CD2 . LEU B  1 117 ? -13.21100 -15.86300 22.71700 1.000 31.32980  ? 217 LEU B CD2 1 
ATOM   2055 N  N   . THR B  1 118 ? -12.64500 -19.34100 22.25600 1.000 17.65998  ? 218 THR B N   1 
ATOM   2056 C  CA  . THR B  1 118 ? -11.78000 -19.48300 21.09200 1.000 17.17038  ? 218 THR B CA  1 
ATOM   2057 C  C   . THR B  1 118 ? -12.36000 -18.69900 19.93300 1.000 21.02161  ? 218 THR B C   1 
ATOM   2058 O  O   . THR B  1 118 ? -13.56500 -18.76300 19.67900 1.000 19.56710  ? 218 THR B O   1 
ATOM   2059 C  CB  . THR B  1 118 ? -11.60100 -20.94600 20.70200 1.000 18.23901  ? 218 THR B CB  1 
ATOM   2060 O  OG1 . THR B  1 118 ? -10.99200 -21.63800 21.79500 1.000 18.79454  ? 218 THR B OG1 1 
ATOM   2061 C  CG2 . THR B  1 118 ? -10.68400 -21.05200 19.47000 1.000 18.21405  ? 218 THR B CG2 1 
ATOM   2062 N  N   . ILE B  1 119 ? -11.49700 -17.96200 19.23300 1.000 18.15865  ? 219 ILE B N   1 
ATOM   2063 C  CA  . ILE B  1 119 ? -11.88400 -17.20000 18.05500 1.000 18.62116  ? 219 ILE B CA  1 
ATOM   2064 C  C   . ILE B  1 119 ? -11.29500 -17.88900 16.83400 1.000 20.50011  ? 219 ILE B C   1 
ATOM   2065 O  O   . ILE B  1 119 ? -10.14800 -18.34300 16.86000 1.000 18.71672  ? 219 ILE B O   1 
ATOM   2066 C  CB  . ILE B  1 119 ? -11.38500 -15.74300 18.14000 1.000 19.00161  ? 219 ILE B CB  1 
ATOM   2067 C  CG1 . ILE B  1 119 ? -11.82300 -15.08900 19.44600 1.000 21.74396  ? 219 ILE B CG1 1 
ATOM   2068 C  CG2 . ILE B  1 119 ? -11.87600 -14.93100 16.95500 1.000 19.30771  ? 219 ILE B CG2 1 
ATOM   2069 C  CD1 . ILE B  1 119 ? -11.06500 -13.81900 19.74700 1.000 24.19000  ? 219 ILE B CD1 1 
ATOM   2070 N  N   . ILE B  1 120 ? -12.06800 -17.95500 15.75400 1.000 17.12629  ? 220 ILE B N   1 
ATOM   2071 C  CA  . ILE B  1 120 ? -11.60000 -18.60100 14.53000 1.000 17.09788  ? 220 ILE B CA  1 
ATOM   2072 C  C   . ILE B  1 120 ? -11.83800 -17.65200 13.37000 1.000 21.54241  ? 220 ILE B C   1 
ATOM   2073 O  O   . ILE B  1 120 ? -12.93100 -17.09500 13.24400 1.000 20.30245  ? 220 ILE B O   1 
ATOM   2074 C  CB  . ILE B  1 120 ? -12.31900 -19.93800 14.26300 1.000 17.27594  ? 220 ILE B CB  1 
ATOM   2075 C  CG1 . ILE B  1 120 ? -12.44100 -20.78500 15.53000 1.000 18.62610  ? 220 ILE B CG1 1 
ATOM   2076 C  CG2 . ILE B  1 120 ? -11.59700 -20.72800 13.18800 1.000 21.26692  ? 220 ILE B CG2 1 
ATOM   2077 C  CD1 . ILE B  1 120 ? -13.70700 -20.51500 16.39500 1.000 18.35511  ? 220 ILE B CD1 1 
ATOM   2078 N  N   . VAL B  1 121 ? -10.82400 -17.47100 12.52400 1.000 17.32841  ? 221 VAL B N   1 
ATOM   2079 C  CA  . VAL B  1 121 ? -10.97900 -16.79200 11.24400 1.000 19.99721  ? 221 VAL B CA  1 
ATOM   2080 C  C   . VAL B  1 121 ? -10.90500 -17.85200 10.15400 1.000 19.64005  ? 221 VAL B C   1 
ATOM   2081 O  O   . VAL B  1 121 ? -9.96000  -18.64500 10.11500 1.000 18.86784  ? 221 VAL B O   1 
ATOM   2082 C  CB  . VAL B  1 121 ? -9.90800  -15.70400 11.03200 1.000 17.69861  ? 221 VAL B CB  1 
ATOM   2083 C  CG1 . VAL B  1 121 ? -10.16700 -15.00800 9.68500  1.000 23.35561  ? 221 VAL B CG1 1 
ATOM   2084 C  CG2 . VAL B  1 121 ? -9.95800  -14.68900 12.15100 1.000 18.75446  ? 221 VAL B CG2 1 
ATOM   2085 N  N   . SER B  1 122 ? -11.90800 -17.86900 9.27000  1.000 18.43976  ? 222 SER B N   1 
ATOM   2086 C  CA  . SER B  1 122 ? -11.96100 -18.83400 8.18300  1.000 19.26113  ? 222 SER B CA  1 
ATOM   2087 C  C   . SER B  1 122 ? -11.03400 -18.40800 7.05200  1.000 21.35777  ? 222 SER B C   1 
ATOM   2088 O  O   . SER B  1 122 ? -11.10500 -17.27100 6.57600  1.000 23.09994  ? 222 SER B O   1 
ATOM   2089 C  CB  . SER B  1 122 ? -13.40100 -18.95000 7.66200  1.000 19.71699  ? 222 SER B CB  1 
ATOM   2090 O  OG  . SER B  1 122 ? -13.40900 -19.62400 6.41400  1.000 21.22214  ? 222 SER B OG  1 
ATOM   2091 N  N   . GLU B  1 123 ? -10.16000 -19.31600 6.61100  1.000 20.46093  ? 223 GLU B N   1 
ATOM   2092 C  CA  . GLU B  1 123 ? -9.35200  -18.97800 5.44500  1.000 20.78699  ? 223 GLU B CA  1 
ATOM   2093 C  C   . GLU B  1 123 ? -10.13200 -19.09500 4.14200  1.000 25.79096  ? 223 GLU B C   1 
ATOM   2094 O  O   . GLU B  1 123 ? -9.63100  -18.66600 3.09600  1.000 29.16265  ? 223 GLU B O   1 
ATOM   2095 C  CB  . GLU B  1 123 ? -8.09200  -19.84700 5.39400  1.000 28.13170  ? 223 GLU B CB  1 
ATOM   2096 C  CG  . GLU B  1 123 ? -8.35900  -21.30600 5.14100  1.000 35.98526  ? 223 GLU B CG  1 
ATOM   2097 C  CD  . GLU B  1 123 ? -7.10000  -22.14600 5.26300  1.000 43.50804  ? 223 GLU B CD  1 
ATOM   2098 O  OE1 . GLU B  1 123 ? -6.17200  -21.73500 5.99400  1.000 45.43307  ? 223 GLU B OE1 1 
ATOM   2099 O  OE2 . GLU B  1 123 ? -7.03900  -23.21000 4.62000  1.000 46.12233  ? 223 GLU B OE2 1 
ATOM   2100 N  N   . GLU B  1 124 ? -11.34000 -19.65100 4.17600  1.000 22.56878  ? 224 GLU B N   1 
ATOM   2101 C  CA  . GLU B  1 124 ? -12.16400 -19.68000 2.97200  1.000 22.81627  ? 224 GLU B CA  1 
ATOM   2102 C  C   . GLU B  1 124 ? -12.92100 -18.37100 2.78000  1.000 23.84310  ? 224 GLU B C   1 
ATOM   2103 O  O   . GLU B  1 124 ? -12.93200 -17.81400 1.67900  1.000 27.19403  ? 224 GLU B O   1 
ATOM   2104 C  CB  . GLU B  1 124 ? -13.13400 -20.86200 3.02100  1.000 25.09931  ? 224 GLU B CB  1 
ATOM   2105 C  CG  . GLU B  1 124 ? -13.82300 -21.13900 1.68200  1.000 35.77963  ? 224 GLU B CG  1 
ATOM   2106 C  CD  . GLU B  1 124 ? -14.84100 -22.26700 1.74600  1.000 61.70949  ? 224 GLU B CD  1 
ATOM   2107 O  OE1 . GLU B  1 124 ? -14.66800 -23.19100 2.57200  1.000 67.87647  ? 224 GLU B OE1 1 
ATOM   2108 O  OE2 . GLU B  1 124 ? -15.82000 -22.22600 0.96700  1.000 60.97554  ? 224 GLU B OE2 1 
ATOM   2109 N  N   . THR B  1 125 ? -13.55000 -17.85900 3.83600  1.000 23.73159  ? 225 THR B N   1 
ATOM   2110 C  CA  . THR B  1 125 ? -14.42800 -16.70400 3.71600  1.000 25.01147  ? 225 THR B CA  1 
ATOM   2111 C  C   . THR B  1 125 ? -13.94900 -15.47200 4.45400  1.000 26.63910  ? 225 THR B C   1 
ATOM   2112 O  O   . THR B  1 125 ? -14.49200 -14.39000 4.21800  1.000 23.94555  ? 225 THR B O   1 
ATOM   2113 C  CB  . THR B  1 125 ? -15.82500 -17.03100 4.26600  1.000 25.98523  ? 225 THR B CB  1 
ATOM   2114 O  OG1 . THR B  1 125 ? -15.70300 -17.33700 5.66200  1.000 22.49514  ? 225 THR B OG1 1 
ATOM   2115 C  CG2 . THR B  1 125 ? -16.44800 -18.21200 3.52900  1.000 25.17651  ? 225 THR B CG2 1 
ATOM   2116 N  N   . GLY B  1 126 ? -13.01300 -15.60800 5.38600  1.000 22.38473  ? 226 GLY B N   1 
ATOM   2117 C  CA  . GLY B  1 126 ? -12.71800 -14.52000 6.29200  1.000 19.84309  ? 226 GLY B CA  1 
ATOM   2118 C  C   . GLY B  1 126 ? -13.74500 -14.33200 7.37700  1.000 21.81994  ? 226 GLY B C   1 
ATOM   2119 O  O   . GLY B  1 126 ? -13.60400 -13.40300 8.18100  1.000 22.26387  ? 226 GLY B O   1 
ATOM   2120 N  N   . GLY B  1 127 ? -14.77600 -15.17800 7.42400  1.000 22.84085  ? 227 GLY B N   1 
ATOM   2121 C  CA  . GLY B  1 127 ? -15.76000 -15.08000 8.48900  1.000 19.61970  ? 227 GLY B CA  1 
ATOM   2122 C  C   . GLY B  1 127 ? -15.15800 -15.39900 9.84600  1.000 19.05832  ? 227 GLY B C   1 
ATOM   2123 O  O   . GLY B  1 127 ? -14.25600 -16.22700 9.98100  1.000 22.41612  ? 227 GLY B O   1 
ATOM   2124 N  N   . VAL B  1 128 ? -15.69100 -14.73600 10.86600 1.000 20.38416  ? 228 VAL B N   1 
ATOM   2125 C  CA  . VAL B  1 128 ? -15.18800 -14.83500 12.23500 1.000 22.32964  ? 228 VAL B CA  1 
ATOM   2126 C  C   . VAL B  1 128 ? -16.20400 -15.58100 13.09100 1.000 20.32533  ? 228 VAL B C   1 
ATOM   2127 O  O   . VAL B  1 128 ? -17.39800 -15.25400 13.07600 1.000 22.13905  ? 228 VAL B O   1 
ATOM   2128 C  CB  . VAL B  1 128 ? -14.89400 -13.44100 12.81300 1.000 22.89458  ? 228 VAL B CB  1 
ATOM   2129 C  CG1 . VAL B  1 128 ? -14.48400 -13.53900 14.29100 1.000 20.05268  ? 228 VAL B CG1 1 
ATOM   2130 C  CG2 . VAL B  1 128 ? -13.79900 -12.76400 11.99000 1.000 19.65043  ? 228 VAL B CG2 1 
ATOM   2131 N  N   . SER B  1 129 ? -15.73300 -16.57700 13.84300 1.000 18.42295  ? 229 SER B N   1 
ATOM   2132 C  CA  . SER B  1 129 ? -16.60800 -17.33300 14.73100 1.000 18.57989  ? 229 SER B CA  1 
ATOM   2133 C  C   . SER B  1 129 ? -15.96400 -17.47400 16.09400 1.000 19.18854  ? 229 SER B C   1 
ATOM   2134 O  O   . SER B  1 129 ? -14.76800 -17.24000 16.26200 1.000 20.38007  ? 229 SER B O   1 
ATOM   2135 C  CB  . SER B  1 129 ? -16.94500 -18.72000 14.18000 1.000 21.78772  ? 229 SER B CB  1 
ATOM   2136 O  OG  . SER B  1 129 ? -15.77400 -19.42800 13.83700 1.000 25.86698  ? 229 SER B OG  1 
ATOM   2137 N  N   . VAL B  1 130 ? -16.78900 -17.86000 17.07000 1.000 20.64252  ? 230 VAL B N   1 
ATOM   2138 C  CA  . VAL B  1 130 ? -16.33900 -18.04200 18.44700 1.000 18.70847  ? 230 VAL B CA  1 
ATOM   2139 C  C   . VAL B  1 130 ? -16.89300 -19.36500 18.96000 1.000 21.38010  ? 230 VAL B C   1 
ATOM   2140 O  O   . VAL B  1 130 ? -18.05700 -19.69900 18.70900 1.000 21.43961  ? 230 VAL B O   1 
ATOM   2141 C  CB  . VAL B  1 130 ? -16.77600 -16.86200 19.34900 1.000 21.95637  ? 230 VAL B CB  1 
ATOM   2142 C  CG1 . VAL B  1 130 ? -16.64200 -17.21800 20.82000 1.000 26.03674  ? 230 VAL B CG1 1 
ATOM   2143 C  CG2 . VAL B  1 130 ? -15.92600 -15.63000 19.04500 1.000 19.94102  ? 230 VAL B CG2 1 
ATOM   2144 N  N   . ALA B  1 131 ? -16.04900 -20.13500 19.64200 1.000 18.40512  ? 231 ALA B N   1 
ATOM   2145 C  CA  . ALA B  1 131 ? -16.45400 -21.36200 20.31400 1.000 20.43753  ? 231 ALA B CA  1 
ATOM   2146 C  C   . ALA B  1 131 ? -16.37100 -21.16300 21.82000 1.000 22.69146  ? 231 ALA B C   1 
ATOM   2147 O  O   . ALA B  1 131 ? -15.34200 -20.71300 22.34300 1.000 20.26447  ? 231 ALA B O   1 
ATOM   2148 C  CB  . ALA B  1 131 ? -15.58300 -22.55500 19.90300 1.000 19.72636  ? 231 ALA B CB  1 
ATOM   2149 N  N   . LYS B  1 132 ? -17.44300 -21.52000 22.51600 1.000 20.83111  ? 232 LYS B N   1 
ATOM   2150 C  CA  . LYS B  1 132 ? -17.49400 -21.40000 23.96700 1.000 19.95385  ? 232 LYS B CA  1 
ATOM   2151 C  C   . LYS B  1 132 ? -18.47000 -22.44000 24.48700 1.000 21.10164  ? 232 LYS B C   1 
ATOM   2152 O  O   . LYS B  1 132 ? -19.58800 -22.53900 23.97300 1.000 21.14391  ? 232 LYS B O   1 
ATOM   2153 C  CB  . LYS B  1 132 ? -17.93900 -19.99400 24.38600 1.000 26.60052  ? 232 LYS B CB  1 
ATOM   2154 C  CG  . LYS B  1 132 ? -18.23700 -19.83000 25.87800 1.000 33.55957  ? 232 LYS B CG  1 
ATOM   2155 C  CD  . LYS B  1 132 ? -17.00000 -19.44700 26.66400 1.000 35.66196  ? 232 LYS B CD  1 
ATOM   2156 C  CE  . LYS B  1 132 ? -17.35100 -19.25500 28.14000 1.000 40.05221  ? 232 LYS B CE  1 
ATOM   2157 N  NZ  . LYS B  1 132 ? -16.18400 -18.75900 28.92700 1.000 49.76358  ? 232 LYS B NZ  1 
ATOM   2158 N  N   . ASN B  1 133 ? -18.04000 -23.22500 25.48100 1.000 20.72086  ? 233 ASN B N   1 
ATOM   2159 C  CA  . ASN B  1 133 ? -18.92200 -24.17900 26.15500 1.000 27.65259  ? 233 ASN B CA  1 
ATOM   2160 C  C   . ASN B  1 133 ? -19.52900 -25.17900 25.18100 1.000 28.79622  ? 233 ASN B C   1 
ATOM   2161 O  O   . ASN B  1 133 ? -20.65500 -25.64100 25.37800 1.000 29.50123  ? 233 ASN B O   1 
ATOM   2162 C  CB  . ASN B  1 133 ? -20.03000 -23.45600 26.92400 1.000 28.15248  ? 233 ASN B CB  1 
ATOM   2163 C  CG  . ASN B  1 133 ? -19.48900 -22.60800 28.06300 1.000 33.07622  ? 233 ASN B CG  1 
ATOM   2164 O  OD1 . ASN B  1 133 ? -18.54100 -23.00000 28.74800 1.000 43.99312  ? 233 ASN B OD1 1 
ATOM   2165 N  ND2 . ASN B  1 133 ? -20.08200 -21.43500 28.26200 1.000 51.83522  ? 233 ASN B ND2 1 
ATOM   2166 N  N   . GLY B  1 134 ? -18.79900 -25.51900 24.12400 1.000 20.75543  ? 234 GLY B N   1 
ATOM   2167 C  CA  . GLY B  1 134 ? -19.30300 -26.45500 23.14700 1.000 22.62199  ? 234 GLY B CA  1 
ATOM   2168 C  C   . GLY B  1 134 ? -20.15200 -25.85900 22.04400 1.000 24.67165  ? 234 GLY B C   1 
ATOM   2169 O  O   . GLY B  1 134 ? -20.51100 -26.58300 21.11200 1.000 26.47340  ? 234 GLY B O   1 
ATOM   2170 N  N   . ASP B  1 135 ? -20.47100 -24.57100 22.10400 1.000 23.39524  ? 235 ASP B N   1 
ATOM   2171 C  CA  . ASP B  1 135 ? -21.26500 -23.91800 21.06700 1.000 24.89620  ? 235 ASP B CA  1 
ATOM   2172 C  C   . ASP B  1 135 ? -20.37300 -23.11700 20.12800 1.000 25.61661  ? 235 ASP B C   1 
ATOM   2173 O  O   . ASP B  1 135 ? -19.42000 -22.46700 20.56400 1.000 24.07759  ? 235 ASP B O   1 
ATOM   2174 C  CB  . ASP B  1 135 ? -22.30500 -22.98900 21.68500 1.000 24.64122  ? 235 ASP B CB  1 
ATOM   2175 C  CG  . ASP B  1 135 ? -23.31000 -23.72700 22.53600 1.000 31.30860  ? 235 ASP B CG  1 
ATOM   2176 O  OD1 . ASP B  1 135 ? -23.83300 -24.76300 22.07700 1.000 28.65504  ? 235 ASP B OD1 1 
ATOM   2177 O  OD2 . ASP B  1 135 ? -23.58500 -23.26400 23.65700 1.000 32.07848  ? 235 ASP B OD2 1 
ATOM   2178 N  N   . LEU B  1 136 ? -20.70400 -23.14700 18.83800 1.000 20.44203  ? 236 LEU B N   1 
ATOM   2179 C  CA  . LEU B  1 136 ? -20.01100 -22.35500 17.82700 1.000 20.18539  ? 236 LEU B CA  1 
ATOM   2180 C  C   . LEU B  1 136 ? -20.97400 -21.31100 17.27600 1.000 27.51768  ? 236 LEU B C   1 
ATOM   2181 O  O   . LEU B  1 136 ? -22.03300 -21.66200 16.73700 1.000 25.32369  ? 236 LEU B O   1 
ATOM   2182 C  CB  . LEU B  1 136 ? -19.48300 -23.24200 16.69700 1.000 23.22416  ? 236 LEU B CB  1 
ATOM   2183 C  CG  . LEU B  1 136 ? -18.65300 -22.57000 15.59500 1.000 22.62710  ? 236 LEU B CG  1 
ATOM   2184 C  CD1 . LEU B  1 136 ? -17.27800 -22.14700 16.12100 1.000 21.26993  ? 236 LEU B CD1 1 
ATOM   2185 C  CD2 . LEU B  1 136 ? -18.49000 -23.51800 14.43900 1.000 24.29127  ? 236 LEU B CD2 1 
ATOM   2186 N  N   . HIS B  1 137 ? -20.60600 -20.04100 17.41100 1.000 20.55850  ? 237 HIS B N   1 
ATOM   2187 C  CA  . HIS B  1 137 ? -21.37900 -18.91300 16.90400 1.000 24.18272  ? 237 HIS B CA  1 
ATOM   2188 C  C   . HIS B  1 137 ? -20.61300 -18.29500 15.74200 1.000 21.17838  ? 237 HIS B C   1 
ATOM   2189 O  O   . HIS B  1 137 ? -19.47900 -17.83700 15.91800 1.000 20.59357  ? 237 HIS B O   1 
ATOM   2190 C  CB  . HIS B  1 137 ? -21.61700 -17.88000 18.00400 1.000 33.70401  ? 237 HIS B CB  1 
ATOM   2191 C  CG  . HIS B  1 137 ? -22.11500 -18.47500 19.28600 1.000 33.22064  ? 237 HIS B CG  1 
ATOM   2192 N  ND1 . HIS B  1 137 ? -23.42300 -18.86900 19.46400 1.000 44.10815  ? 237 HIS B ND1 1 
ATOM   2193 C  CD2 . HIS B  1 137 ? -21.47300 -18.76400 20.44400 1.000 41.84722  ? 237 HIS B CD2 1 
ATOM   2194 C  CE1 . HIS B  1 137 ? -23.57100 -19.36300 20.68000 1.000 41.26852  ? 237 HIS B CE1 1 
ATOM   2195 N  NE2 . HIS B  1 137 ? -22.40200 -19.30500 21.29700 1.000 45.91210  ? 237 HIS B NE2 1 
ATOM   2196 N  N   . ARG B  1 138 ? -21.23100 -18.26700 14.56800 1.000 20.36364  ? 238 ARG B N   1 
ATOM   2197 C  CA  . ARG B  1 138 ? -20.50400 -17.92400 13.34900 1.000 21.21783  ? 238 ARG B CA  1 
ATOM   2198 C  C   . ARG B  1 138 ? -20.95200 -16.58700 12.76700 1.000 20.45948  ? 238 ARG B C   1 
ATOM   2199 O  O   . ARG B  1 138 ? -21.96100 -15.99400 13.17000 1.000 23.16470  ? 238 ARG B O   1 
ATOM   2200 C  CB  . ARG B  1 138 ? -20.65700 -19.03200 12.29600 1.000 25.07991  ? 238 ARG B CB  1 
ATOM   2201 C  CG  . ARG B  1 138 ? -20.06400 -20.36900 12.75500 1.000 28.70091  ? 238 ARG B CG  1 
ATOM   2202 C  CD  . ARG B  1 138 ? -19.69400 -21.27500 11.58800 1.000 32.32918  ? 238 ARG B CD  1 
ATOM   2203 N  NE  . ARG B  1 138 ? -20.83800 -21.45100 10.71200 1.000 29.45873  ? 238 ARG B NE  1 
ATOM   2204 C  CZ  . ARG B  1 138 ? -20.98900 -20.86300 9.53300  1.000 35.96680  ? 238 ARG B CZ  1 
ATOM   2205 N  NH1 . ARG B  1 138 ? -20.00200 -20.18900 8.96000  1.000 34.99037  ? 238 ARG B NH1 1 
ATOM   2206 N  NH2 . ARG B  1 138 ? -22.16700 -20.94100 8.92100  1.000 32.25353  ? 238 ARG B NH2 1 
ATOM   2207 N  N   . GLU B  1 139 ? -20.14100 -16.10900 11.81900 1.000 20.26154  ? 239 GLU B N   1 
ATOM   2208 C  CA  . GLU B  1 139 ? -20.41200 -14.89900 11.02600 1.000 23.79008  ? 239 GLU B CA  1 
ATOM   2209 C  C   . GLU B  1 139 ? -20.59500 -13.67400 11.91600 1.000 23.87546  ? 239 GLU B C   1 
ATOM   2210 O  O   . GLU B  1 139 ? -21.50600 -12.86300 11.72000 1.000 24.63381  ? 239 GLU B O   1 
ATOM   2211 C  CB  . GLU B  1 139 ? -21.63200 -15.06800 10.09800 1.000 22.87914  ? 239 GLU B CB  1 
ATOM   2212 C  CG  . GLU B  1 139 ? -21.63300 -16.31100 9.21000  1.000 21.25289  ? 239 GLU B CG  1 
ATOM   2213 C  CD  . GLU B  1 139 ? -20.57000 -16.28600 8.13600  1.000 25.31401  ? 239 GLU B CD  1 
ATOM   2214 O  OE1 . GLU B  1 139 ? -19.83200 -15.27800 8.03000  1.000 23.96841  ? 239 GLU B OE1 1 
ATOM   2215 O  OE2 . GLU B  1 139 ? -20.47100 -17.30200 7.41300  1.000 23.66845  ? 239 GLU B OE2 1 
ATOM   2216 N  N   . LEU B  1 140 ? -19.69800 -13.52000 12.88400 1.000 21.94417  ? 240 LEU B N   1 
ATOM   2217 C  CA  . LEU B  1 140 ? -19.79700 -12.41800 13.82700 1.000 27.63841  ? 240 LEU B CA  1 
ATOM   2218 C  C   . LEU B  1 140 ? -19.35600 -11.10400 13.19500 1.000 29.46840  ? 240 LEU B C   1 
ATOM   2219 O  O   . LEU B  1 140 ? -18.35300 -11.04800 12.48200 1.000 26.73925  ? 240 LEU B O   1 
ATOM   2220 C  CB  . LEU B  1 140 ? -18.92800 -12.70000 15.05200 1.000 23.29663  ? 240 LEU B CB  1 
ATOM   2221 C  CG  . LEU B  1 140 ? -19.21700 -14.02000 15.76900 1.000 28.41075  ? 240 LEU B CG  1 
ATOM   2222 C  CD1 . LEU B  1 140 ? -18.15200 -14.27100 16.81200 1.000 26.67898  ? 240 LEU B CD1 1 
ATOM   2223 C  CD2 . LEU B  1 140 ? -20.59400 -14.00400 16.41200 1.000 32.69304  ? 240 LEU B CD2 1 
ATOM   2224 N  N   . THR B  1 141 ? -20.09400 -10.03800 13.49300 1.000 29.05079  ? 241 THR B N   1 
ATOM   2225 C  CA  . THR B  1 141 ? -19.61000 -8.69400  13.21900 1.000 36.65342  ? 241 THR B CA  1 
ATOM   2226 C  C   . THR B  1 141 ? -18.50600 -8.33300  14.20700 1.000 33.83600  ? 241 THR B C   1 
ATOM   2227 O  O   . THR B  1 141 ? -18.33300 -8.97700  15.24800 1.000 29.77359  ? 241 THR B O   1 
ATOM   2228 C  CB  . THR B  1 141 ? -20.74600 -7.66800  13.32200 1.000 37.52321  ? 241 THR B CB  1 
ATOM   2229 O  OG1 . THR B  1 141 ? -21.28800 -7.68600  14.64800 1.000 35.49480  ? 241 THR B OG1 1 
ATOM   2230 C  CG2 . THR B  1 141 ? -21.84700 -7.98900  12.32900 1.000 42.30283  ? 241 THR B CG2 1 
ATOM   2231 N  N   . GLU B  1 142 ? -17.74300 -7.28900  13.87600 1.000 40.80194  ? 242 GLU B N   1 
ATOM   2232 C  CA  . GLU B  1 142 ? -16.73400 -6.85400  14.83200 1.000 42.22219  ? 242 GLU B CA  1 
ATOM   2233 C  C   . GLU B  1 142 ? -17.37800 -6.30800  16.10000 1.000 41.24197  ? 242 GLU B C   1 
ATOM   2234 O  O   . GLU B  1 142 ? -16.81900 -6.47200  17.19100 1.000 36.49930  ? 242 GLU B O   1 
ATOM   2235 C  CB  . GLU B  1 142 ? -15.78300 -5.83400  14.20200 1.000 56.32405  ? 242 GLU B CB  1 
ATOM   2236 C  CG  . GLU B  1 142 ? -16.36600 -4.49000  13.85900 1.000 63.35374  ? 242 GLU B CG  1 
ATOM   2237 C  CD  . GLU B  1 142 ? -15.43200 -3.66800  12.98300 1.000 81.17400  ? 242 GLU B CD  1 
ATOM   2238 O  OE1 . GLU B  1 142 ? -15.46700 -3.85100  11.74400 1.000 85.99028  ? 242 GLU B OE1 1 
ATOM   2239 O  OE2 . GLU B  1 142 ? -14.65400 -2.85500  13.53200 1.000 75.19343  ? 242 GLU B OE2 1 
ATOM   2240 N  N   . GLU B  1 143 ? -18.56200 -5.69500  15.98600 1.000 40.73796  ? 243 GLU B N   1 
ATOM   2241 C  CA  . GLU B  1 143 ? -19.31100 -5.30100  17.17600 1.000 48.89748  ? 243 GLU B CA  1 
ATOM   2242 C  C   . GLU B  1 143 ? -19.61200 -6.51100  18.05100 1.000 43.15386  ? 243 GLU B C   1 
ATOM   2243 O  O   . GLU B  1 143 ? -19.42900 -6.47200  19.27300 1.000 39.25568  ? 243 GLU B O   1 
ATOM   2244 C  CB  . GLU B  1 143 ? -20.61800 -4.59900  16.78700 1.000 54.73392  ? 243 GLU B CB  1 
ATOM   2245 C  CG  . GLU B  1 143 ? -20.46100 -3.31100  15.99700 1.000 58.21235  ? 243 GLU B CG  1 
ATOM   2246 C  CD  . GLU B  1 143 ? -20.15500 -3.55000  14.52700 1.000 66.30615  ? 243 GLU B CD  1 
ATOM   2247 O  OE1 . GLU B  1 143 ? -21.00000 -4.13900  13.81900 1.000 65.32908  ? 243 GLU B OE1 1 
ATOM   2248 O  OE2 . GLU B  1 143 ? -19.06200 -3.14900  14.08400 1.000 72.33790  ? 243 GLU B OE2 1 
ATOM   2249 N  N   . ALA B  1 144 ? -20.08200 -7.59800  17.43600 1.000 35.44594  ? 244 ALA B N   1 
ATOM   2250 C  CA  . ALA B  1 144 ? -20.43200 -8.79100  18.19800 1.000 32.69971  ? 244 ALA B CA  1 
ATOM   2251 C  C   . ALA B  1 144 ? -19.20700 -9.39500  18.87400 1.000 31.76025  ? 244 ALA B C   1 
ATOM   2252 O  O   . ALA B  1 144 ? -19.28300 -9.86100  20.01600 1.000 33.43901  ? 244 ALA B O   1 
ATOM   2253 C  CB  . ALA B  1 144 ? -21.09900 -9.81800  17.28500 1.000 34.67315  ? 244 ALA B CB  1 
ATOM   2254 N  N   . LEU B  1 145 ? -18.07000 -9.39800  18.18200 1.000 27.56037  ? 245 LEU B N   1 
ATOM   2255 C  CA  . LEU B  1 145 ? -16.87100 -9.99100  18.75600 1.000 31.10804  ? 245 LEU B CA  1 
ATOM   2256 C  C   . LEU B  1 145 ? -16.37400 -9.17400  19.94000 1.000 31.73033  ? 245 LEU B C   1 
ATOM   2257 O  O   . LEU B  1 145 ? -16.05100 -9.72600  20.99800 1.000 33.98431  ? 245 LEU B O   1 
ATOM   2258 C  CB  . LEU B  1 145 ? -15.78500 -10.10400 17.69300 1.000 30.10972  ? 245 LEU B CB  1 
ATOM   2259 C  CG  . LEU B  1 145 ? -14.43000 -10.56600 18.22600 1.000 28.09719  ? 245 LEU B CG  1 
ATOM   2260 C  CD1 . LEU B  1 145 ? -14.53100 -11.97100 18.80800 1.000 29.09443  ? 245 LEU B CD1 1 
ATOM   2261 C  CD2 . LEU B  1 145 ? -13.41300 -10.51300 17.10600 1.000 27.92103  ? 245 LEU B CD2 1 
ATOM   2262 N  N   . LYS B  1 146 ? -16.30500 -7.85300  19.77800 1.000 33.95010  ? 246 LYS B N   1 
ATOM   2263 C  CA  . LYS B  1 146 ? -15.81500 -7.01000  20.86300 1.000 35.66843  ? 246 LYS B CA  1 
ATOM   2264 C  C   . LYS B  1 146 ? -16.70600 -7.12400  22.09100 1.000 36.43500  ? 246 LYS B C   1 
ATOM   2265 O  O   . LYS B  1 146 ? -16.21100 -7.17300  23.22500 1.000 37.85880  ? 246 LYS B O   1 
ATOM   2266 C  CB  . LYS B  1 146 ? -15.71600 -5.55900  20.39700 1.000 37.90418  ? 246 LYS B CB  1 
ATOM   2267 C  CG  . LYS B  1 146 ? -14.79500 -4.69100  21.25500 1.000 43.49704  ? 246 LYS B CG  1 
ATOM   2268 C  CD  . LYS B  1 146 ? -14.23800 -3.52200  20.45200 1.000 56.87973  ? 246 LYS B CD  1 
ATOM   2269 C  CE  . LYS B  1 146 ? -13.45200 -2.55700  21.32500 1.000 57.89200  ? 246 LYS B CE  1 
ATOM   2270 N  NZ  . LYS B  1 146 ? -14.31600 -1.81900  22.28900 1.000 66.28536  ? 246 LYS B NZ  1 
ATOM   2271 N  N   . GLU B  1 147 ? -18.02600 -7.17400  21.89100 1.000 37.94760  ? 247 GLU B N   1 
ATOM   2272 C  CA  . GLU B  1 147 ? -18.92600 -7.29200  23.03500 1.000 39.03131  ? 247 GLU B CA  1 
ATOM   2273 C  C   . GLU B  1 147 ? -18.79700 -8.65600  23.70600 1.000 39.21266  ? 247 GLU B C   1 
ATOM   2274 O  O   . GLU B  1 147 ? -18.86600 -8.74900  24.93500 1.000 41.51813  ? 247 GLU B O   1 
ATOM   2275 C  CB  . GLU B  1 147 ? -20.36800 -7.02300  22.60300 1.000 45.59861  ? 247 GLU B CB  1 
ATOM   2276 C  CG  . GLU B  1 147 ? -20.61200 -5.57500  22.20200 1.000 61.85618  ? 247 GLU B CG  1 
ATOM   2277 C  CD  . GLU B  1 147 ? -22.00800 -5.33800  21.65000 1.000 77.41750  ? 247 GLU B CD  1 
ATOM   2278 O  OE1 . GLU B  1 147 ? -22.98800 -5.77800  22.29000 1.000 75.90034  ? 247 GLU B OE1 1 
ATOM   2279 O  OE2 . GLU B  1 147 ? -22.12100 -4.71600  20.57000 1.000 72.29849  ? 247 GLU B OE2 1 
ATOM   2280 N  N   . MET B  1 148 ? -18.58200 -9.72100  22.92500 1.000 34.64841  ? 248 MET B N   1 
ATOM   2281 C  CA  . MET B  1 148 ? -18.30800 -11.02600 23.52700 1.000 38.10563  ? 248 MET B CA  1 
ATOM   2282 C  C   . MET B  1 148 ? -17.06200 -10.97100 24.39900 1.000 35.98369  ? 248 MET B C   1 
ATOM   2283 O  O   . MET B  1 148 ? -17.07500 -11.41200 25.55400 1.000 39.18148  ? 248 MET B O   1 
ATOM   2284 C  CB  . MET B  1 148 ? -18.13700 -12.09500 22.44900 1.000 38.48404  ? 248 MET B CB  1 
ATOM   2285 C  CG  . MET B  1 148 ? -19.41300 -12.62500 21.85400 1.000 47.51345  ? 248 MET B CG  1 
ATOM   2286 S  SD  . MET B  1 148 ? -19.07900 -14.09200 20.85800 1.000 51.76352  ? 248 MET B SD  1 
ATOM   2287 C  CE  . MET B  1 148 ? -20.72400 -14.43500 20.22500 1.000 52.91535  ? 248 MET B CE  1 
ATOM   2288 N  N   . LEU B  1 149 ? -15.97100 -10.42500 23.85600 1.000 32.02252  ? 249 LEU B N   1 
ATOM   2289 C  CA  . LEU B  1 149 ? -14.72000 -10.34800 24.60400 1.000 31.43983  ? 249 LEU B CA  1 
ATOM   2290 C  C   . LEU B  1 149 ? -14.87500 -9.51300  25.86500 1.000 40.15039  ? 249 LEU B C   1 
ATOM   2291 O  O   . LEU B  1 149 ? -14.36100 -9.88200  26.92800 1.000 43.07953  ? 249 LEU B O   1 
ATOM   2292 C  CB  . LEU B  1 149 ? -13.61800 -9.76700  23.72200 1.000 29.36370  ? 249 LEU B CB  1 
ATOM   2293 C  CG  . LEU B  1 149 ? -13.13400 -10.69400 22.61400 1.000 31.21871  ? 249 LEU B CG  1 
ATOM   2294 C  CD1 . LEU B  1 149 ? -12.18400 -9.95700  21.71300 1.000 29.41089  ? 249 LEU B CD1 1 
ATOM   2295 C  CD2 . LEU B  1 149 ? -12.45100 -11.89900 23.23400 1.000 36.88391  ? 249 LEU B CD2 1 
ATOM   2296 N  N   . GLU B  1 150 ? -15.57200 -8.37800  25.76500 1.000 35.71330  ? 250 GLU B N   1 
ATOM   2297 C  CA  . GLU B  1 150 ? -15.77100 -7.53700  26.94200 1.000 40.09270  ? 250 GLU B CA  1 
ATOM   2298 C  C   . GLU B  1 150 ? -16.59100 -8.26400  27.99800 1.000 46.76006  ? 250 GLU B C   1 
ATOM   2299 O  O   . GLU B  1 150 ? -16.27300 -8.20100  29.19300 1.000 48.20463  ? 250 GLU B O   1 
ATOM   2300 C  CB  . GLU B  1 150 ? -16.42500 -6.21400  26.53700 1.000 37.59431  ? 250 GLU B CB  1 
ATOM   2301 C  CG  . GLU B  1 150 ? -15.40700 -5.23000  25.95800 1.000 39.37448  ? 250 GLU B CG  1 
ATOM   2302 C  CD  . GLU B  1 150 ? -16.02600 -4.08700  25.18500 1.000 60.66636  ? 250 GLU B CD  1 
ATOM   2303 O  OE1 . GLU B  1 150 ? -17.23600 -4.14300  24.88300 1.000 62.82456  ? 250 GLU B OE1 1 
ATOM   2304 O  OE2 . GLU B  1 150 ? -15.28800 -3.12900  24.87000 1.000 65.62003  ? 250 GLU B OE2 1 
ATOM   2305 N  N   . ALA B  1 151 ? -17.63400 -8.98000  27.57600 1.000 39.51095  ? 251 ALA B N   1 
ATOM   2306 C  CA  . ALA B  1 151 ? -18.42600 -9.75300  28.52600 1.000 47.32666  ? 251 ALA B CA  1 
ATOM   2307 C  C   . ALA B  1 151 ? -17.59500 -10.86200 29.15500 1.000 54.88111  ? 251 ALA B C   1 
ATOM   2308 O  O   . ALA B  1 151 ? -17.71400 -11.13600 30.35400 1.000 55.55314  ? 251 ALA B O   1 
ATOM   2309 C  CB  . ALA B  1 151 ? -19.65900 -10.33500 27.83500 1.000 42.76159  ? 251 ALA B CB  1 
ATOM   2310 N  N   . GLU B  1 152 ? -16.72900 -11.49600 28.37100 1.000 51.04334  ? 252 GLU B N   1 
ATOM   2311 C  CA  . GLU B  1 152 ? -16.00300 -12.65800 28.86600 1.000 61.81981  ? 252 GLU B CA  1 
ATOM   2312 C  C   . GLU B  1 152 ? -14.79700 -12.27600 29.71500 1.000 62.25392  ? 252 GLU B C   1 
ATOM   2313 O  O   . GLU B  1 152 ? -14.42100 -13.03500 30.61500 1.000 79.24581  ? 252 GLU B O   1 
ATOM   2314 C  CB  . GLU B  1 152 ? -15.57800 -13.53800 27.69100 1.000 57.12956  ? 252 GLU B CB  1 
ATOM   2315 C  CG  . GLU B  1 152 ? -16.76600 -14.11400 26.93400 1.000 58.07966  ? 252 GLU B CG  1 
ATOM   2316 C  CD  . GLU B  1 152 ? -17.57700 -15.08400 27.76600 1.000 74.89611  ? 252 GLU B CD  1 
ATOM   2317 O  OE1 . GLU B  1 152 ? -16.98500 -16.06100 28.27500 1.000 70.61766  ? 252 GLU B OE1 1 
ATOM   2318 O  OE2 . GLU B  1 152 ? -18.80100 -14.86500 27.91500 1.000 77.11179  ? 252 GLU B OE2 1 
ATOM   2319 N  N   . PHE B  1 153 ? -14.18700 -11.11600 29.46100 1.000 48.95836  ? 253 PHE B N   1 
ATOM   2320 C  CA  . PHE B  1 153 ? -13.00700 -10.72700 30.22600 1.000 55.48887  ? 253 PHE B CA  1 
ATOM   2321 C  C   . PHE B  1 153 ? -13.35800 -10.25800 31.63400 1.000 68.89957  ? 253 PHE B C   1 
ATOM   2322 O  O   . PHE B  1 153 ? -12.48200 -10.26700 32.50600 1.000 78.63874  ? 253 PHE B O   1 
ATOM   2323 C  CB  . PHE B  1 153 ? -12.23000 -9.63100  29.48900 1.000 61.84161  ? 253 PHE B CB  1 
ATOM   2324 C  CG  . PHE B  1 153 ? -11.09800 -10.14500 28.62200 1.000 66.34201  ? 253 PHE B CG  1 
ATOM   2325 C  CD1 . PHE B  1 153 ? -11.33000 -10.57800 27.32600 1.000 62.17301  ? 253 PHE B CD1 1 
ATOM   2326 C  CD2 . PHE B  1 153 ? -9.79600  -10.17000 29.10100 1.000 69.20656  ? 253 PHE B CD2 1 
ATOM   2327 C  CE1 . PHE B  1 153 ? -10.28300 -11.03500 26.52700 1.000 63.35953  ? 253 PHE B CE1 1 
ATOM   2328 C  CE2 . PHE B  1 153 ? -8.74500  -10.62400 28.31000 1.000 59.64574  ? 253 PHE B CE2 1 
ATOM   2329 C  CZ  . PHE B  1 153 ? -8.99000  -11.05500 27.02200 1.000 52.50416  ? 253 PHE B CZ  1 
ATOM   2330 N  N   . LYS B  1 154 ? -14.61300 -9.85700  31.87200 1.000 65.11649  ? 254 LYS B N   1 
ATOM   2331 C  CA  . LYS B  1 154 ? -15.03400 -9.38700  33.19100 1.000 80.94291  ? 254 LYS B CA  1 
ATOM   2332 C  C   . LYS B  1 154 ? -14.68800 -10.40200 34.27500 1.000 86.42201  ? 254 LYS B C   1 
ATOM   2333 O  O   . LYS B  1 154 ? -14.00400 -10.08000 35.25400 1.000 88.56088  ? 254 LYS B O   1 
ATOM   2334 C  CB  . LYS B  1 154 ? -16.53700 -9.09500  33.18000 1.000 67.17239  ? 254 LYS B CB  1 
ATOM   2335 C  CG  . LYS B  1 154 ? -16.92000 -7.81600  32.45300 1.000 72.58446  ? 254 LYS B CG  1 
ATOM   2336 C  CD  . LYS B  1 154 ? -18.23400 -7.96800  31.69600 1.000 71.62737  ? 254 LYS B CD  1 
ATOM   2337 C  CE  . LYS B  1 154 ? -19.34400 -8.51800  32.57500 1.000 79.15906  ? 254 LYS B CE  1 
ATOM   2338 N  NZ  . LYS B  1 154 ? -20.54500 -8.86600  31.76300 1.000 81.55534  ? 254 LYS B NZ  1 
ATOM   2339 N  N   . LYS B  1 155 ? -15.16200 -11.63500 34.10800 1.000 82.37955  ? 255 LYS B N   1 
ATOM   2340 C  CA  . LYS B  1 155 ? -14.75000 -12.76300 34.93800 1.000 87.92952  ? 255 LYS B CA  1 
ATOM   2341 C  C   . LYS B  1 155 ? -15.27600 -14.07100 34.35200 1.000 96.95686  ? 255 LYS B C   1 
ATOM   2342 O  O   . LYS B  1 155 ? -16.11400 -14.06800 33.44900 1.000 87.46350  ? 255 LYS B O   1 
ATOM   2343 C  CB  . LYS B  1 155 ? -15.23600 -12.60200 36.37900 1.000 76.88887  ? 255 LYS B CB  1 
ATOM   2344 C  CG  . LYS B  1 155 ? -14.11600 -12.69400 37.39900 1.000 66.54159  ? 255 LYS B CG  1 
ATOM   2345 C  CD  . LYS B  1 155 ? -13.26800 -13.94300 37.17000 1.000 76.63622  ? 255 LYS B CD  1 
ATOM   2346 C  CE  . LYS B  1 155 ? -13.96100 -15.18000 37.70800 1.000 66.46474  ? 255 LYS B CE  1 
ATOM   2347 N  NZ  . LYS B  1 155 ? -14.18400 -15.04200 39.18300 1.000 45.92147  ? 255 LYS B NZ  1 
HETATM 2348 N  N1  . TJ9 C  2 .   ? 16.41200  2.06300   12.20800 0.675 36.57238  ? 301 TJ9 A N1  1 
HETATM 2349 N  N3  . TJ9 C  2 .   ? 13.97700  0.35300   8.34400  0.675 54.39867  ? 301 TJ9 A N3  1 
HETATM 2350 C  C4  . TJ9 C  2 .   ? 16.26300  3.19000   11.52600 0.675 40.62752  ? 301 TJ9 A C4  1 
HETATM 2351 C  C5  . TJ9 C  2 .   ? 16.06800  5.75700   11.51200 0.675 51.22960  ? 301 TJ9 A C5  1 
HETATM 2352 C  C6  . TJ9 C  2 .   ? 16.51000  7.10900   11.99300 0.675 55.57644  ? 301 TJ9 A C6  1 
HETATM 2353 C  C7  . TJ9 C  2 .   ? 14.91400  -0.17300  9.34600  0.675 45.86909  ? 301 TJ9 A C7  1 
HETATM 2354 C  C8  . TJ9 C  2 .   ? 15.15700  -1.60600  9.07800  0.675 38.66242  ? 301 TJ9 A C8  1 
HETATM 2355 C  C1  . TJ9 C  2 .   ? 16.17900  -0.41200  12.39300 0.675 31.79983  ? 301 TJ9 A C1  1 
HETATM 2356 C  C2  . TJ9 C  2 .   ? 15.97800  0.81800   11.55400 0.675 34.08327  ? 301 TJ9 A C2  1 
HETATM 2357 C  C3  . TJ9 C  2 .   ? 15.43000  0.58600   10.33800 0.675 47.67697  ? 301 TJ9 A C3  1 
HETATM 2358 C  C9  . TJ9 C  2 .   ? 13.59500  -0.56300  7.47000  0.675 47.83215  ? 301 TJ9 A C9  1 
HETATM 2359 N  N2  . TJ9 C  2 .   ? 16.58200  4.51900   11.89300 0.675 40.79339  ? 301 TJ9 A N2  1 
HETATM 2360 N  N4  . TJ9 C  2 .   ? 12.72200  -0.35100  6.41700  0.675 54.55729  ? 301 TJ9 A N4  1 
HETATM 2361 O  O1  . TJ9 C  2 .   ? 15.13300  5.73700   10.67300 0.675 53.77346  ? 301 TJ9 A O1  1 
HETATM 2362 S  S1  . TJ9 C  2 .   ? 15.52200  2.70800   9.94900  0.675 51.18434  ? 301 TJ9 A S1  1 
HETATM 2363 S  S2  . TJ9 C  2 .   ? 14.36200  -2.18500  7.79900  0.675 51.96538  ? 301 TJ9 A S2  1 
HETATM 2364 S  S   . DMS D  3 .   ? 24.22300  -18.48100 6.54100  1.000 57.68019  ? 302 DMS A S   1 
HETATM 2365 O  O   . DMS D  3 .   ? 25.02000  -18.73000 5.29800  1.000 61.03925  ? 302 DMS A O   1 
HETATM 2366 C  C1  . DMS D  3 .   ? 25.36700  -17.84900 7.79700  1.000 37.76574  ? 302 DMS A C1  1 
HETATM 2367 C  C2  . DMS D  3 .   ? 23.70600  -20.06400 7.24700  1.000 55.80381  ? 302 DMS A C2  1 
HETATM 2368 S  S   . DMS E  3 .   ? 23.05000  -3.96800  31.68300 1.000 71.97392  ? 303 DMS A S   1 
HETATM 2369 O  O   . DMS E  3 .   ? 22.27000  -2.69800  31.56900 1.000 63.60904  ? 303 DMS A O   1 
HETATM 2370 C  C1  . DMS E  3 .   ? 23.22500  -4.67800  30.02500 1.000 47.57868  ? 303 DMS A C1  1 
HETATM 2371 C  C2  . DMS E  3 .   ? 22.01200  -5.23500  32.46300 1.000 66.82407  ? 303 DMS A C2  1 
HETATM 2372 S  S   . DMS F  3 .   ? 21.65000  -13.10600 24.71300 0.733 59.19235  ? 304 DMS A S   1 
HETATM 2373 O  O   . DMS F  3 .   ? 20.31800  -12.45100 24.90600 0.733 42.45383  ? 304 DMS A O   1 
HETATM 2374 C  C1  . DMS F  3 .   ? 21.83600  -14.44400 25.92500 0.733 54.41570  ? 304 DMS A C1  1 
HETATM 2375 C  C2  . DMS F  3 .   ? 22.95700  -12.00300 25.31800 0.733 45.79398  ? 304 DMS A C2  1 
HETATM 2376 S  S   . DMS G  3 .   ? 36.53800  -6.79000  17.60600 0.896 26.52336  ? 305 DMS A S   1 
HETATM 2377 O  O   . DMS G  3 .   ? 36.41700  -5.34100  17.94400 0.896 26.04191  ? 305 DMS A O   1 
HETATM 2378 C  C1  . DMS G  3 .   ? 38.26900  -7.32100  17.74600 0.896 26.71185  ? 305 DMS A C1  1 
HETATM 2379 C  C2  . DMS G  3 .   ? 35.86100  -7.65200  19.05100 0.896 26.44480  ? 305 DMS A C2  1 
HETATM 2380 S  S   . DMS H  3 .   ? 26.79100  -15.49300 -0.11400 0.928 72.81233  ? 306 DMS A S   1 
HETATM 2381 O  O   . DMS H  3 .   ? 27.60200  -14.32600 0.33700  0.928 52.51206  ? 306 DMS A O   1 
HETATM 2382 C  C1  . DMS H  3 .   ? 26.47500  -16.58000 1.30200  0.928 54.67706  ? 306 DMS A C1  1 
HETATM 2383 C  C2  . DMS H  3 .   ? 25.10600  -14.93900 -0.52000 0.928 36.80178  ? 306 DMS A C2  1 
HETATM 2384 S  S   . DMS I  3 .   ? 33.76200  -9.49400  22.82900 1.000 82.17571  ? 307 DMS A S   1 
HETATM 2385 O  O   . DMS I  3 .   ? 33.12100  -8.75000  21.70700 1.000 54.70278  ? 307 DMS A O   1 
HETATM 2386 C  C1  . DMS I  3 .   ? 35.53300  -9.14600  22.75600 1.000 58.65057  ? 307 DMS A C1  1 
HETATM 2387 C  C2  . DMS I  3 .   ? 33.78400  -11.26600 22.44000 1.000 64.66770  ? 307 DMS A C2  1 
HETATM 2388 S  S   . DMS J  3 .   ? 35.16100  -12.99600 9.74400  0.854 66.74626  ? 308 DMS A S   1 
HETATM 2389 O  O   . DMS J  3 .   ? 35.54600  -11.86200 8.84600  0.854 61.74210  ? 308 DMS A O   1 
HETATM 2390 C  C1  . DMS J  3 .   ? 36.62500  -13.58300 10.63600 0.854 52.55171  ? 308 DMS A C1  1 
HETATM 2391 C  C2  . DMS J  3 .   ? 34.87500  -14.48000 8.74400  0.854 54.60063  ? 308 DMS A C2  1 
HETATM 2392 S  S   . DMS K  3 .   ? 10.80600  1.15100   11.51600 0.798 73.25521  ? 309 DMS A S   1 
HETATM 2393 O  O   . DMS K  3 .   ? 12.11500  1.07900   12.23500 0.798 52.35747  ? 309 DMS A O   1 
HETATM 2394 C  C1  . DMS K  3 .   ? 9.67900   -0.09700  12.19400 0.798 50.13986  ? 309 DMS A C1  1 
HETATM 2395 C  C2  . DMS K  3 .   ? 10.98100  0.56100   9.81200  0.798 53.58730  ? 309 DMS A C2  1 
HETATM 2396 C  C1  . PEG L  4 .   ? 3.23000   -11.91700 1.72800  0.875 55.57703  ? 310 PEG A C1  1 
HETATM 2397 O  O1  . PEG L  4 .   ? 2.53600   -10.68000 1.73400  0.875 62.43256  ? 310 PEG A O1  1 
HETATM 2398 C  C2  . PEG L  4 .   ? 3.60300   -12.34700 3.11400  0.875 44.58738  ? 310 PEG A C2  1 
HETATM 2399 O  O2  . PEG L  4 .   ? 3.94300   -13.72800 3.10900  0.875 60.22513  ? 310 PEG A O2  1 
HETATM 2400 C  C3  . PEG L  4 .   ? 2.86400   -14.56700 2.71800  0.875 52.20379  ? 310 PEG A C3  1 
HETATM 2401 C  C4  . PEG L  4 .   ? 3.27700   -16.00500 2.81700  0.875 48.86172  ? 310 PEG A C4  1 
HETATM 2402 O  O4  . PEG L  4 .   ? 4.40300   -16.29600 2.00100  0.875 59.35630  ? 310 PEG A O4  1 
HETATM 2403 S  S   . DMS M  3 .   ? 14.08300  -10.99300 -4.58000 1.000 44.15034  ? 311 DMS A S   1 
HETATM 2404 O  O   . DMS M  3 .   ? 13.98900  -9.55800  -4.97700 1.000 47.72037  ? 311 DMS A O   1 
HETATM 2405 C  C1  . DMS M  3 .   ? 12.69400  -11.33500 -3.46700 1.000 30.74059  ? 311 DMS A C1  1 
HETATM 2406 C  C2  . DMS M  3 .   ? 15.44600  -11.19300 -3.38200 1.000 36.03434  ? 311 DMS A C2  1 
HETATM 2407 CL CL  . CL  N  5 .   ? 2.15200   -5.00900  7.00600  0.911 65.10816  ? 312 CL  A CL  1 
HETATM 2408 CL CL  . CL  O  5 .   ? 19.05100  -5.41400  3.08700  0.673 33.60874  ? 313 CL  A CL  1 
HETATM 2409 CL CL  . CL  P  5 .   ? 12.15900  -9.79800  1.19200  0.865 41.84014  ? 314 CL  A CL  1 
HETATM 2410 N  N1  . TJ9 Q  2 .   ? -5.41900  -29.28800 16.93500 0.780 28.97600  ? 301 TJ9 B N1  1 
HETATM 2411 N  N3  . TJ9 Q  2 .   ? -4.88300  -26.19100 13.20300 0.780 41.59855  ? 301 TJ9 B N3  1 
HETATM 2412 C  C4  . TJ9 Q  2 .   ? -5.37900  -30.51800 16.45400 0.780 29.03216  ? 301 TJ9 B C4  1 
HETATM 2413 C  C5  . TJ9 Q  2 .   ? -5.57300  -33.08100 16.72100 0.780 42.72196  ? 301 TJ9 B C5  1 
HETATM 2414 C  C6  . TJ9 Q  2 .   ? -5.82600  -34.28100 17.58800 0.780 47.10342  ? 301 TJ9 B C6  1 
HETATM 2415 C  C7  . TJ9 Q  2 .   ? -4.63800  -27.61400 13.48400 0.780 38.82172  ? 301 TJ9 B C7  1 
HETATM 2416 C  C8  . TJ9 Q  2 .   ? -4.05900  -28.25700 12.28900 0.780 44.07057  ? 301 TJ9 B C8  1 
HETATM 2417 C  C1  . TJ9 Q  2 .   ? -5.22300  -26.82600 16.65000 0.780 26.12633  ? 301 TJ9 B C1  1 
HETATM 2418 C  C2  . TJ9 Q  2 .   ? -5.16900  -28.18400 16.00700 0.780 29.69768  ? 301 TJ9 B C2  1 
HETATM 2419 C  C3  . TJ9 Q  2 .   ? -4.91100  -28.17400 14.68000 0.780 44.25421  ? 301 TJ9 B C3  1 
HETATM 2420 C  C9  . TJ9 Q  2 .   ? -4.54000  -25.84900 11.97400 0.780 37.16643  ? 301 TJ9 B C9  1 
HETATM 2421 N  N2  . TJ9 Q  2 .   ? -5.58400  -31.74700 17.12300 0.780 37.62850  ? 301 TJ9 B N2  1 
HETATM 2422 N  N4  . TJ9 Q  2 .   ? -4.65000  -24.58400 11.42900 0.780 45.95894  ? 301 TJ9 B N4  1 
HETATM 2423 O  O1  . TJ9 Q  2 .   ? -5.32900  -33.30300 15.50800 0.780 43.04517  ? 301 TJ9 B O1  1 
HETATM 2424 S  S1  . TJ9 Q  2 .   ? -5.02500  -30.32800 14.68500 0.780 43.64585  ? 301 TJ9 B S1  1 
HETATM 2425 S  S2  . TJ9 Q  2 .   ? -3.86600  -27.25700 11.03900 0.780 53.51465  ? 301 TJ9 B S2  1 
HETATM 2426 S  S   . DMS R  3 .   ? -14.79500 -9.29100  11.93300 0.815 63.01336  ? 302 DMS B S   1 
HETATM 2427 O  O   . DMS R  3 .   ? -15.55000 -9.81800  13.11400 0.815 47.84494  ? 302 DMS B O   1 
HETATM 2428 C  C1  . DMS R  3 .   ? -13.65900 -8.02700  12.53100 0.815 27.32728  ? 302 DMS B C1  1 
HETATM 2429 C  C2  . DMS R  3 .   ? -15.89800 -8.25500  10.92900 0.815 43.78042  ? 302 DMS B C2  1 
HETATM 2430 S  S   . DMS S  3 .   ? -0.29900  -28.52600 14.40700 0.926 60.31875  ? 303 DMS B S   1 
HETATM 2431 O  O   . DMS S  3 .   ? -0.97000  -28.24600 13.10600 0.926 50.00516  ? 303 DMS B O   1 
HETATM 2432 C  C1  . DMS S  3 .   ? -1.50500  -28.43700 15.75900 0.926 38.76443  ? 303 DMS B C1  1 
HETATM 2433 C  C2  . DMS S  3 .   ? 0.76400   -27.13500 14.85900 0.926 44.54628  ? 303 DMS B C2  1 
HETATM 2434 S  S   . DMS T  3 .   ? -1.05900  -3.77000  12.79400 0.761 57.71544  ? 304 DMS B S   1 
HETATM 2435 O  O   . DMS T  3 .   ? -1.93000  -3.59400  13.98900 0.761 44.75618  ? 304 DMS B O   1 
HETATM 2436 C  C1  . DMS T  3 .   ? -2.08700  -3.67500  11.30500 0.761 45.43553  ? 304 DMS B C1  1 
HETATM 2437 C  C2  . DMS T  3 .   ? -0.05700  -2.27500  12.55800 0.761 50.66008  ? 304 DMS B C2  1 
HETATM 2438 S  S   . DMS U  3 .   ? -10.58700 -21.97800 38.92000 0.760 46.52583  ? 305 DMS B S   1 
HETATM 2439 O  O   . DMS U  3 .   ? -12.05700 -22.21200 39.12800 0.760 31.76776  ? 305 DMS B O   1 
HETATM 2440 C  C1  . DMS U  3 .   ? -9.71700  -21.68300 40.48700 0.760 23.35750  ? 305 DMS B C1  1 
HETATM 2441 C  C2  . DMS U  3 .   ? -9.76400  -23.51700 38.44500 0.760 42.56097  ? 305 DMS B C2  1 
HETATM 2442 S  S   . DMS V  3 .   ? -15.97200 -27.35000 30.58200 0.813 61.94971  ? 306 DMS B S   1 
HETATM 2443 O  O   . DMS V  3 .   ? -16.11100 -26.38200 31.70900 0.813 48.12906  ? 306 DMS B O   1 
HETATM 2444 C  C1  . DMS V  3 .   ? -17.12800 -26.90600 29.25000 0.813 45.51525  ? 306 DMS B C1  1 
HETATM 2445 C  C2  . DMS V  3 .   ? -16.61200 -28.97600 31.06400 0.813 51.90511  ? 306 DMS B C2  1 
HETATM 2446 S  S   . DMS W  3 .   ? -8.13500  -10.54800 36.41300 0.892 73.30179  ? 307 DMS B S   1 
HETATM 2447 O  O   . DMS W  3 .   ? -7.64400  -9.62400  37.48400 0.892 49.35164  ? 307 DMS B O   1 
HETATM 2448 C  C1  . DMS W  3 .   ? -9.74900  -9.97300  35.81600 0.892 70.55408  ? 307 DMS B C1  1 
HETATM 2449 C  C2  . DMS W  3 .   ? -8.62500  -12.14400 37.12600 0.892 50.09647  ? 307 DMS B C2  1 
HETATM 2450 C  C1  . PEG X  4 .   ? -4.11200  5.45600   26.94000 0.932 51.91431  ? 308 PEG B C1  1 
HETATM 2451 O  O1  . PEG X  4 .   ? -4.13600  5.26500   28.34900 0.932 54.72968  ? 308 PEG B O1  1 
HETATM 2452 C  C2  . PEG X  4 .   ? -2.86400  6.15900   26.49100 0.932 44.39425  ? 308 PEG B C2  1 
HETATM 2453 O  O2  . PEG X  4 .   ? -2.66700  5.96900   25.09700 0.932 55.61522  ? 308 PEG B O2  1 
HETATM 2454 C  C3  . PEG X  4 .   ? -3.75300  6.43200   24.30800 0.932 57.18948  ? 308 PEG B C3  1 
HETATM 2455 C  C4  . PEG X  4 .   ? -3.44500  6.23700   22.85300 0.932 56.16507  ? 308 PEG B C4  1 
HETATM 2456 O  O4  . PEG X  4 .   ? -4.56500  6.53800   22.03300 0.932 50.52768  ? 308 PEG B O4  1 
HETATM 2457 CL CL  . CL  Y  5 .   ? -2.52700  -24.98000 33.70500 0.538 26.25007  ? 309 CL  B CL  1 
HETATM 2458 CL CL  . CL  Z  5 .   ? -10.33200 -22.30200 8.15600  0.892 41.93169  ? 310 CL  B CL  1 
HETATM 2459 CL CL  . CL  AA 5 .   ? -17.89800 -18.02700 10.30100 0.883 24.97065  ? 311 CL  B CL  1 
HETATM 2460 O  O   . HOH BA 6 .   ? 15.41200  -6.30600  -3.70900 1.000 50.05015  ? 401 HOH A O   1 
HETATM 2461 O  O   . HOH BA 6 .   ? 14.70900  3.35800   28.56400 1.000 46.98975  ? 402 HOH A O   1 
HETATM 2462 O  O   . HOH BA 6 .   ? 22.27300  -7.21200  28.32100 1.000 44.47592  ? 403 HOH A O   1 
HETATM 2463 O  O   . HOH BA 6 .   ? 35.28500  -4.71400  8.04500  1.000 47.74436  ? 404 HOH A O   1 
HETATM 2464 O  O   . HOH BA 6 .   ? 9.48500   -5.75200  3.04800  1.000 40.03411  ? 405 HOH A O   1 
HETATM 2465 O  O   . HOH BA 6 .   ? 33.55400  3.91600   9.74100  1.000 38.27483  ? 406 HOH A O   1 
HETATM 2466 O  O   . HOH BA 6 .   ? 12.43700  -9.84800  28.03500 1.000 44.81455  ? 407 HOH A O   1 
HETATM 2467 O  O   . HOH BA 6 .   ? 28.42900  -20.33800 24.59100 1.000 67.10825  ? 408 HOH A O   1 
HETATM 2468 O  O   . HOH BA 6 .   ? 14.47600  -17.61200 25.43100 1.000 31.04075  ? 409 HOH A O   1 
HETATM 2469 O  O   . HOH BA 6 .   ? 25.87900  -10.34000 0.07800  0.782 34.97996  ? 410 HOH A O   1 
HETATM 2470 O  O   . HOH BA 6 .   ? 31.77900  -5.26600  25.92500 1.000 37.30371  ? 411 HOH A O   1 
HETATM 2471 O  O   . HOH BA 6 .   ? 27.97400  7.37100   12.44100 1.000 39.14306  ? 412 HOH A O   1 
HETATM 2472 O  O   . HOH BA 6 .   ? 8.96500   -3.60000  3.71200  1.000 44.87415  ? 413 HOH A O   1 
HETATM 2473 O  O   . HOH BA 6 .   ? 12.07900  -8.86700  5.95700  1.000 30.15294  ? 414 HOH A O   1 
HETATM 2474 O  O   . HOH BA 6 .   ? 6.70900   -16.81800 3.15400  1.000 56.88754  ? 415 HOH A O   1 
HETATM 2475 O  O   . HOH BA 6 .   ? 25.75800  -4.08600  16.98600 1.000 20.43642  ? 416 HOH A O   1 
HETATM 2476 O  O   . HOH BA 6 .   ? 9.39800   -18.41000 20.71700 1.000 23.74209  ? 417 HOH A O   1 
HETATM 2477 O  O   . HOH BA 6 .   ? 23.56400  -16.69700 2.40800  1.000 47.51454  ? 418 HOH A O   1 
HETATM 2478 O  O   . HOH BA 6 .   ? 7.74400   -3.19400  10.92300 1.000 35.08255  ? 419 HOH A O   1 
HETATM 2479 O  O   . HOH BA 6 .   ? 34.40800  -19.76600 7.66600  1.000 49.36236  ? 420 HOH A O   1 
HETATM 2480 O  O   . HOH BA 6 .   ? 18.73600  -20.35800 -1.51800 1.000 43.14913  ? 421 HOH A O   1 
HETATM 2481 O  O   . HOH BA 6 .   ? 29.26400  -3.20000  18.85500 1.000 22.97952  ? 422 HOH A O   1 
HETATM 2482 O  O   . HOH BA 6 .   ? 22.21900  -16.59400 -0.44200 1.000 44.46154  ? 423 HOH A O   1 
HETATM 2483 O  O   . HOH BA 6 .   ? 37.67400  -5.83600  12.31200 1.000 41.61273  ? 424 HOH A O   1 
HETATM 2484 O  O   . HOH BA 6 .   ? 32.68200  -4.19400  5.45000  1.000 47.79565  ? 425 HOH A O   1 
HETATM 2485 O  O   . HOH BA 6 .   ? 11.66800  -6.33700  13.46800 1.000 23.93246  ? 426 HOH A O   1 
HETATM 2486 O  O   . HOH BA 6 .   ? 32.58400  -1.89000  22.50700 1.000 44.32686  ? 427 HOH A O   1 
HETATM 2487 O  O   . HOH BA 6 .   ? 26.61000  -15.02100 4.02500  1.000 24.49055  ? 428 HOH A O   1 
HETATM 2488 O  O   . HOH BA 6 .   ? 27.76500  7.68900   4.49000  1.000 47.84589  ? 429 HOH A O   1 
HETATM 2489 O  O   . HOH BA 6 .   ? 9.17400   -1.82500  23.31200 1.000 38.80471  ? 430 HOH A O   1 
HETATM 2490 O  O   . HOH BA 6 .   ? 33.71100  -11.56800 6.83200  1.000 50.31152  ? 431 HOH A O   1 
HETATM 2491 O  O   . HOH BA 6 .   ? 24.87200  -3.81300  24.09900 1.000 23.42137  ? 432 HOH A O   1 
HETATM 2492 O  O   . HOH BA 6 .   ? 31.064    0.211     -2.925   1.000 37.02570  ? 433 HOH A O   1 
HETATM 2493 O  O   . HOH BA 6 .   ? 31.71700  2.85900   11.76000 1.000 32.57136  ? 434 HOH A O   1 
HETATM 2494 O  O   . HOH BA 6 .   ? 34.20400  -5.88200  14.71600 1.000 24.93017  ? 435 HOH A O   1 
HETATM 2495 O  O   . HOH BA 6 .   ? 24.39200  -9.01000  4.81000  1.000 22.11874  ? 436 HOH A O   1 
HETATM 2496 O  O   . HOH BA 6 .   ? 14.45800  -5.95800  9.51600  1.000 31.81149  ? 437 HOH A O   1 
HETATM 2497 O  O   . HOH BA 6 .   ? 12.88100  -25.70100 16.18800 1.000 54.68021  ? 438 HOH A O   1 
HETATM 2498 O  O   . HOH BA 6 .   ? 28.71800  -3.30800  -7.46100 1.000 45.44165  ? 439 HOH A O   1 
HETATM 2499 O  O   . HOH BA 6 .   ? 17.40300  -23.31300 8.86900  1.000 40.72870  ? 440 HOH A O   1 
HETATM 2500 O  O   . HOH BA 6 .   ? 29.554    2.687     -2.454   1.000 35.02810  ? 441 HOH A O   1 
HETATM 2501 O  O   . HOH BA 6 .   ? 35.32600  -9.03600  7.96600  1.000 35.61142  ? 442 HOH A O   1 
HETATM 2502 O  O   . HOH BA 6 .   ? 11.78500  -24.32200 18.80100 1.000 42.15524  ? 443 HOH A O   1 
HETATM 2503 O  O   . HOH BA 6 .   ? 11.66000  -5.17600  27.34900 1.000 56.38254  ? 444 HOH A O   1 
HETATM 2504 O  O   . HOH BA 6 .   ? 13.59500  -16.48500 29.08900 1.000 57.64965  ? 445 HOH A O   1 
HETATM 2505 O  O   . HOH BA 6 .   ? 14.16400  -22.92600 18.12400 1.000 31.41909  ? 446 HOH A O   1 
HETATM 2506 O  O   . HOH BA 6 .   ? 22.25900  -5.70900  0.68900  1.000 46.00228  ? 447 HOH A O   1 
HETATM 2507 O  O   . HOH BA 6 .   ? 19.32600  -10.15000 -6.23900 1.000 43.90348  ? 448 HOH A O   1 
HETATM 2508 O  O   . HOH BA 6 .   ? 15.90200  -24.41200 17.55700 1.000 55.18190  ? 449 HOH A O   1 
HETATM 2509 O  O   . HOH BA 6 .   ? 23.23300  -19.53500 10.22000 1.000 36.22247  ? 450 HOH A O   1 
HETATM 2510 O  O   . HOH BA 6 .   ? 36.485    -4.237    14.858   1.000 27.77333  ? 451 HOH A O   1 
HETATM 2511 O  O   . HOH BA 6 .   ? 19.61200  7.77000   12.42200 1.000 40.58596  ? 452 HOH A O   1 
HETATM 2512 O  O   . HOH BA 6 .   ? 27.80700  -21.24500 5.16600  1.000 48.10463  ? 453 HOH A O   1 
HETATM 2513 O  O   . HOH BA 6 .   ? 13.45500  6.00800   23.70000 1.000 46.13906  ? 454 HOH A O   1 
HETATM 2514 O  O   . HOH BA 6 .   ? 21.62300  -9.37300  27.18700 1.000 46.13564  ? 455 HOH A O   1 
HETATM 2515 O  O   A HOH BA 6 .   ? 25.64700  5.88400   15.35500 0.556 28.45192  ? 456 HOH A O   1 
HETATM 2516 O  O   B HOH BA 6 .   ? 25.21600  7.44500   15.72000 0.444 37.52519  ? 456 HOH A O   1 
HETATM 2517 O  O   . HOH BA 6 .   ? 32.52700  4.17000   17.60800 1.000 47.53094  ? 457 HOH A O   1 
HETATM 2518 O  O   . HOH BA 6 .   ? 33.93200  -8.09000  5.46900  1.000 38.81349  ? 458 HOH A O   1 
HETATM 2519 O  O   . HOH BA 6 .   ? 25.92900  -10.27000 24.67100 1.000 43.14134  ? 459 HOH A O   1 
HETATM 2520 O  O   . HOH BA 6 .   ? 31.47600  0.46600   19.90300 1.000 40.01933  ? 460 HOH A O   1 
HETATM 2521 O  O   . HOH BA 6 .   ? 15.22900  -3.07400  28.70400 0.838 47.85883  ? 461 HOH A O   1 
HETATM 2522 O  O   . HOH BA 6 .   ? 24.54100  0.98800   29.97000 1.000 41.30659  ? 462 HOH A O   1 
HETATM 2523 O  O   . HOH BA 6 .   ? 12.38900  -23.57800 12.19200 1.000 43.78419  ? 463 HOH A O   1 
HETATM 2524 O  O   . HOH BA 6 .   ? 19.02400  0.13100   29.22900 1.000 37.82780  ? 464 HOH A O   1 
HETATM 2525 O  O   . HOH BA 6 .   ? 17.62300  -0.16700  1.87400  1.000 43.99649  ? 465 HOH A O   1 
HETATM 2526 O  O   . HOH BA 6 .   ? 33.05100  -16.06000 6.77800  1.000 40.29444  ? 466 HOH A O   1 
HETATM 2527 O  O   . HOH BA 6 .   ? 33.12000  -0.69400  8.29100  1.000 39.37761  ? 467 HOH A O   1 
HETATM 2528 O  O   . HOH BA 6 .   ? 26.85900  -9.72900  3.14200  1.000 17.89588  ? 468 HOH A O   1 
HETATM 2529 O  O   . HOH BA 6 .   ? 7.52600   0.43100   16.19600 1.000 45.12819  ? 469 HOH A O   1 
HETATM 2530 O  O   . HOH BA 6 .   ? 19.80800  -24.51100 9.65500  1.000 53.56613  ? 470 HOH A O   1 
HETATM 2531 O  O   . HOH BA 6 .   ? 27.93800  -1.52900  31.72100 1.000 62.08585  ? 471 HOH A O   1 
HETATM 2532 O  O   . HOH BA 6 .   ? 22.79300  3.09500   2.90900  1.000 53.27276  ? 472 HOH A O   1 
HETATM 2533 O  O   . HOH BA 6 .   ? 30.777    -9.789    -3.644   1.000 51.81513  ? 473 HOH A O   1 
HETATM 2534 O  O   . HOH BA 6 .   ? 17.00000  -12.15500 -5.89300 1.000 44.77741  ? 474 HOH A O   1 
HETATM 2535 O  O   . HOH BA 6 .   ? 4.26600   -3.46100  6.62600  1.000 56.53107  ? 475 HOH A O   1 
HETATM 2536 O  O   . HOH BA 6 .   ? 22.751    -19.001   -4.057   1.000 42.79815  ? 476 HOH A O   1 
HETATM 2537 O  O   . HOH BA 6 .   ? 24.24100  -6.86400  -0.84300 1.000 58.10391  ? 477 HOH A O   1 
HETATM 2538 O  O   . HOH BA 6 .   ? 31.60800  -2.06800  4.67900  1.000 47.99249  ? 478 HOH A O   1 
HETATM 2539 O  O   . HOH BA 6 .   ? 34.15300  1.17000   8.87500  1.000 41.91320  ? 479 HOH A O   1 
HETATM 2540 O  O   . HOH BA 6 .   ? 30.230    1.634     24.023   1.000 56.68493  ? 480 HOH A O   1 
HETATM 2541 O  O   . HOH BA 6 .   ? 31.335    1.717     21.973   1.000 57.61859  ? 481 HOH A O   1 
HETATM 2542 O  O   . HOH BA 6 .   ? 11.81300  -26.67800 19.09800 1.000 56.84894  ? 482 HOH A O   1 
HETATM 2543 O  O   . HOH BA 6 .   ? 11.02600  -23.80000 21.06500 1.000 41.32233  ? 483 HOH A O   1 
HETATM 2544 O  O   . HOH BA 6 .   ? 5.74300   0.38300   14.75500 1.000 55.81014  ? 484 HOH A O   1 
HETATM 2545 O  O   . HOH BA 6 .   ? 13.96400  -26.72200 20.94600 1.000 65.02306  ? 485 HOH A O   1 
HETATM 2546 O  O   . HOH CA 6 .   ? 0.43400   -8.72500  6.45000  1.000 49.23663  ? 401 HOH B O   1 
HETATM 2547 O  O   . HOH CA 6 .   ? -24.79300 -18.17400 17.77500 1.000 42.74771  ? 402 HOH B O   1 
HETATM 2548 O  O   . HOH CA 6 .   ? -1.35100  -22.89800 5.19200  1.000 42.72094  ? 403 HOH B O   1 
HETATM 2549 O  O   . HOH CA 6 .   ? -3.64100  -32.59500 33.39200 1.000 56.49504  ? 404 HOH B O   1 
HETATM 2550 O  O   . HOH CA 6 .   ? -3.19300  -18.78600 8.61600  1.000 29.87709  ? 405 HOH B O   1 
HETATM 2551 O  O   . HOH CA 6 .   ? 3.83100   -8.36200  21.33900 1.000 25.25045  ? 406 HOH B O   1 
HETATM 2552 O  O   . HOH CA 6 .   ? -0.43400  -24.86300 6.13800  1.000 44.22935  ? 407 HOH B O   1 
HETATM 2553 O  O   . HOH CA 6 .   ? -15.49300 -23.00100 26.63100 1.000 23.72241  ? 408 HOH B O   1 
HETATM 2554 O  O   . HOH CA 6 .   ? -22.35400 -30.43900 20.15400 1.000 27.65875  ? 409 HOH B O   1 
HETATM 2555 O  O   . HOH CA 6 .   ? -12.79100 -22.50100 23.52900 1.000 19.89181  ? 410 HOH B O   1 
HETATM 2556 O  O   . HOH CA 6 .   ? -17.75700 -18.07800 7.15900  1.000 27.32268  ? 411 HOH B O   1 
HETATM 2557 O  O   . HOH CA 6 .   ? -9.91300  -21.74200 30.03800 1.000 24.46739  ? 412 HOH B O   1 
HETATM 2558 O  O   . HOH CA 6 .   ? -19.42300 -12.68800 8.43700  1.000 27.26498  ? 413 HOH B O   1 
HETATM 2559 O  O   . HOH CA 6 .   ? -20.25600 -29.35600 21.30900 1.000 29.47333  ? 414 HOH B O   1 
HETATM 2560 O  O   . HOH CA 6 .   ? 2.39500   -25.27100 31.09500 1.000 32.89988  ? 415 HOH B O   1 
HETATM 2561 O  O   . HOH CA 6 .   ? -26.31500 -25.09600 23.02400 1.000 39.58572  ? 416 HOH B O   1 
HETATM 2562 O  O   . HOH CA 6 .   ? -0.92500  -1.24300  16.83800 1.000 56.81278  ? 417 HOH B O   1 
HETATM 2563 O  O   . HOH CA 6 .   ? -8.63200  -31.41600 29.20300 1.000 49.72496  ? 418 HOH B O   1 
HETATM 2564 O  O   . HOH CA 6 .   ? -12.97900 0.40400   38.10100 1.000 69.35692  ? 419 HOH B O   1 
HETATM 2565 O  O   . HOH CA 6 .   ? -16.84700 -34.01500 21.07100 1.000 36.64951  ? 420 HOH B O   1 
HETATM 2566 O  O   . HOH CA 6 .   ? -22.64100 -18.83000 6.76700  1.000 36.93909  ? 421 HOH B O   1 
HETATM 2567 O  O   . HOH CA 6 .   ? 1.08200   -31.74100 27.17500 1.000 41.13427  ? 422 HOH B O   1 
HETATM 2568 O  O   . HOH CA 6 .   ? 0.86500   -2.69000  19.56900 1.000 45.67593  ? 423 HOH B O   1 
HETATM 2569 O  O   . HOH CA 6 .   ? 4.88900   -24.45900 24.86900 1.000 29.75040  ? 424 HOH B O   1 
HETATM 2570 O  O   . HOH CA 6 .   ? -9.10100  -9.90900  0.78900  1.000 36.54299  ? 425 HOH B O   1 
HETATM 2571 O  O   . HOH CA 6 .   ? -0.51400  -21.01400 15.89600 1.000 22.56326  ? 426 HOH B O   1 
HETATM 2572 O  O   . HOH CA 6 .   ? 2.43500   -24.36600 12.52100 1.000 36.33839  ? 427 HOH B O   1 
HETATM 2573 O  O   . HOH CA 6 .   ? -0.10500  -14.36400 32.04600 1.000 35.38081  ? 428 HOH B O   1 
HETATM 2574 O  O   . HOH CA 6 .   ? -15.41300 -11.41700 8.99300  1.000 28.92650  ? 429 HOH B O   1 
HETATM 2575 O  O   . HOH CA 6 .   ? -17.45600 -12.53700 10.27800 1.000 22.66505  ? 430 HOH B O   1 
HETATM 2576 O  O   . HOH CA 6 .   ? -23.699   -19.422   13.832   1.000 32.81523  ? 431 HOH B O   1 
HETATM 2577 O  O   . HOH CA 6 .   ? -14.99300 -18.68900 11.16200 1.000 21.03714  ? 432 HOH B O   1 
HETATM 2578 O  O   . HOH CA 6 .   ? -13.98300 -22.35800 6.97000  1.000 43.87871  ? 433 HOH B O   1 
HETATM 2579 O  O   . HOH CA 6 .   ? -8.01600  -20.90400 37.78900 1.000 38.77452  ? 434 HOH B O   1 
HETATM 2580 O  O   . HOH CA 6 .   ? -4.23800  -21.38800 12.95000 1.000 28.01896  ? 435 HOH B O   1 
HETATM 2581 O  O   . HOH CA 6 .   ? -23.52100 -16.07900 15.56100 1.000 39.93916  ? 436 HOH B O   1 
HETATM 2582 O  O   . HOH CA 6 .   ? -12.58700 -7.30200  15.29500 1.000 40.21022  ? 437 HOH B O   1 
HETATM 2583 O  O   . HOH CA 6 .   ? -1.45200  -4.00200  19.85200 1.000 37.45689  ? 438 HOH B O   1 
HETATM 2584 O  O   . HOH CA 6 .   ? 0.69900   -7.94500  27.18400 1.000 33.70200  ? 439 HOH B O   1 
HETATM 2585 O  O   . HOH CA 6 .   ? -7.04200  -18.33600 1.85100  1.000 53.69864  ? 440 HOH B O   1 
HETATM 2586 O  O   . HOH CA 6 .   ? -1.76700  -22.62500 32.09800 1.000 31.26584  ? 441 HOH B O   1 
HETATM 2587 O  O   . HOH CA 6 .   ? 3.12400   -5.33400  23.27500 1.000 31.46140  ? 442 HOH B O   1 
HETATM 2588 O  O   . HOH CA 6 .   ? -4.57600  -28.15900 30.42900 1.000 37.29491  ? 443 HOH B O   1 
HETATM 2589 O  O   . HOH CA 6 .   ? -14.04400 -30.45100 10.23600 1.000 57.65706  ? 444 HOH B O   1 
HETATM 2590 O  O   A HOH CA 6 .   ? -13.44700 -32.32300 22.94500 0.614 27.16597  ? 445 HOH B O   1 
HETATM 2591 O  O   C HOH CA 6 .   ? -12.81400 -33.92400 22.89400 0.386 38.41120  ? 445 HOH B O   1 
HETATM 2592 O  O   . HOH CA 6 .   ? -8.79400  -35.16900 19.26800 1.000 39.18829  ? 446 HOH B O   1 
HETATM 2593 O  O   . HOH CA 6 .   ? -9.27400  -29.44200 30.34100 1.000 45.68075  ? 447 HOH B O   1 
HETATM 2594 O  O   . HOH CA 6 .   ? -21.18000 -10.79300 9.53700  1.000 48.25718  ? 448 HOH B O   1 
HETATM 2595 O  O   . HOH CA 6 .   ? 0.77900   -29.12600 32.32600 1.000 51.88242  ? 449 HOH B O   1 
HETATM 2596 O  O   . HOH CA 6 .   ? -5.02800  -18.04600 3.55200  1.000 45.89735  ? 450 HOH B O   1 
HETATM 2597 O  O   . HOH CA 6 .   ? -18.54300 -6.25300  11.11100 1.000 45.41547  ? 451 HOH B O   1 
HETATM 2598 O  O   . HOH CA 6 .   ? -9.41300  -27.74700 7.18200  1.000 48.87572  ? 452 HOH B O   1 
HETATM 2599 O  O   . HOH CA 6 .   ? -4.38300  -19.24300 6.12700  1.000 37.01128  ? 453 HOH B O   1 
HETATM 2600 O  O   . HOH CA 6 .   ? -7.59900  -13.00000 0.38300  1.000 44.52417  ? 454 HOH B O   1 
HETATM 2601 O  O   . HOH CA 6 .   ? -22.75800 -11.04200 14.74500 1.000 40.20552  ? 455 HOH B O   1 
HETATM 2602 O  O   . HOH CA 6 .   ? 9.45600   -3.94800  27.74100 1.000 55.71001  ? 456 HOH B O   1 
HETATM 2603 O  O   . HOH CA 6 .   ? 6.57200   -28.67900 21.77500 1.000 47.88240  ? 457 HOH B O   1 
HETATM 2604 O  O   . HOH CA 6 .   ? -3.738    -15.990   33.445   1.000 36.69312  ? 458 HOH B O   1 
HETATM 2605 O  O   . HOH CA 6 .   ? -1.55600  -5.03900  3.56800  1.000 61.44739  ? 459 HOH B O   1 
HETATM 2606 O  O   . HOH CA 6 .   ? -8.46400  -15.86100 33.64300 1.000 36.33198  ? 460 HOH B O   1 
HETATM 2607 O  O   . HOH CA 6 .   ? -18.11100 -35.56800 13.32600 1.000 53.19500  ? 461 HOH B O   1 
HETATM 2608 O  O   . HOH CA 6 .   ? 4.25100   -27.43000 17.27300 1.000 47.46231  ? 462 HOH B O   1 
HETATM 2609 O  O   . HOH CA 6 .   ? -4.37100  -2.53300  39.03100 1.000 52.11637  ? 463 HOH B O   1 
HETATM 2610 O  O   . HOH CA 6 .   ? -9.13300  -24.91100 8.93000  1.000 35.59991  ? 464 HOH B O   1 
HETATM 2611 O  O   . HOH CA 6 .   ? 1.19800   -0.23800  18.51100 1.000 60.00684  ? 465 HOH B O   1 
HETATM 2612 O  O   . HOH CA 6 .   ? -19.68300 -28.43900 27.00500 1.000 47.34182  ? 466 HOH B O   1 
HETATM 2613 O  O   . HOH CA 6 .   ? -6.14500  -23.01500 36.65500 1.000 32.47977  ? 467 HOH B O   1 
HETATM 2614 O  O   . HOH CA 6 .   ? -25.28200 -16.31600 14.24400 1.000 47.67999  ? 468 HOH B O   1 
HETATM 2615 O  O   . HOH CA 6 .   ? 4.58500   -24.35800 7.19500  1.000 54.22905  ? 469 HOH B O   1 
HETATM 2616 O  O   . HOH CA 6 .   ? -1.331    -28.440   33.795   1.000 49.37106  ? 470 HOH B O   1 
HETATM 2617 O  O   . HOH CA 6 .   ? -19.96400 -34.24100 20.98100 1.000 48.86832  ? 471 HOH B O   1 
HETATM 2618 O  O   . HOH CA 6 .   ? 4.07200   -25.17000 9.40600  1.000 55.38234  ? 472 HOH B O   1 
HETATM 2619 O  O   . HOH CA 6 .   ? 6.94900   -23.28500 7.30400  1.000 50.00284  ? 473 HOH B O   1 
HETATM 2620 O  O   . HOH CA 6 .   ? 8.34700   -27.69200 20.63400 1.000 53.46626  ? 474 HOH B O   1 
HETATM 2621 O  O   . HOH CA 6 .   ? 2.12000   -4.33800  26.08900 1.000 59.80953  ? 475 HOH B O   1 
HETATM 2622 O  O   . HOH CA 6 .   ? -4.72000  -31.84400 11.72000 1.000 59.11466  ? 476 HOH B O   1 
HETATM 2623 O  O   . HOH CA 6 .   ? -21.20800 -29.55400 24.13500 1.000 45.72954  ? 477 HOH B O   1 
HETATM 2624 O  O   . HOH CA 6 .   ? -6.67900  -9.82100  0.44900  1.000 49.16963  ? 478 HOH B O   1 
HETATM 2625 O  O   . HOH CA 6 .   ? 2.54200   -31.15000 29.06200 1.000 58.14181  ? 479 HOH B O   1 
HETATM 2626 O  O   . HOH CA 6 .   ? -22.26900 -33.49700 21.21500 1.000 53.53847  ? 480 HOH B O   1 
HETATM 2627 O  O   . HOH CA 6 .   ? 2.25300   -2.87200  21.95300 1.000 45.87241  ? 481 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . THR A 3   ? 0.82783 0.71333 0.83443 0.04227  -0.10274 0.17631  103 THR A N   
2    C CA  . THR A 3   ? 0.89761 0.80135 0.90192 0.02217  -0.09892 0.18470  103 THR A CA  
3    C C   . THR A 3   ? 0.89935 0.79162 0.90289 0.00258  -0.09286 0.17949  103 THR A C   
4    O O   . THR A 3   ? 0.85874 0.74141 0.86615 0.00531  -0.09025 0.16637  103 THR A O   
5    C CB  . THR A 3   ? 0.88841 0.84306 0.90476 0.02232  -0.09325 0.17975  103 THR A CB  
6    O OG1 . THR A 3   ? 0.86302 0.83706 0.89147 0.01855  -0.08379 0.16333  103 THR A OG1 
7    C CG2 . THR A 3   ? 0.88644 0.85633 0.90724 0.04417  -0.09897 0.18010  103 THR A CG2 
8    N N   . PRO A 4   ? 0.85715 0.75152 0.85559 -0.01680 -0.08992 0.18815  104 PRO A N   
9    C CA  . PRO A 4   ? 0.84262 0.73274 0.84260 -0.03529 -0.08258 0.18013  104 PRO A CA  
10   C C   . PRO A 4   ? 0.75936 0.67871 0.77283 -0.03787 -0.07552 0.16917  104 PRO A C   
11   O O   . PRO A 4   ? 0.66658 0.57430 0.68186 -0.04141 -0.07294 0.15912  104 PRO A O   
12   C CB  . PRO A 4   ? 0.75954 0.66128 0.75534 -0.05071 -0.07649 0.18232  104 PRO A CB  
13   C CG  . PRO A 4   ? 0.97718 0.90109 0.97243 -0.04296 -0.07916 0.19119  104 PRO A CG  
14   C CD  . PRO A 4   ? 0.92948 0.83493 0.92090 -0.02155 -0.08894 0.19646  104 PRO A CD  
15   N N   . VAL A 5   ? 0.70861 0.66851 0.73177 -0.03532 -0.07026 0.16684  105 VAL A N   
16   C CA  . VAL A 5   ? 0.80722 0.79878 0.84459 -0.03550 -0.06018 0.15234  105 VAL A CA  
17   C C   . VAL A 5   ? 0.82953 0.80893 0.86950 -0.01896 -0.06120 0.13877  105 VAL A C   
18   O O   . VAL A 5   ? 0.76965 0.74923 0.81366 -0.02314 -0.05543 0.12836  105 VAL A O   
19   C CB  . VAL A 5   ? 0.72357 0.75884 0.77166 -0.03238 -0.05488 0.15142  105 VAL A CB  
20   C CG1 . VAL A 5   ? 0.68155 0.74628 0.74527 -0.02674 -0.04457 0.13522  105 VAL A CG1 
21   C CG2 . VAL A 5   ? 0.76353 0.81530 0.81093 -0.05223 -0.05051 0.16163  105 VAL A CG2 
22   N N   . GLU A 6   ? 0.80143 0.76993 0.83883 0.00027  -0.06851 0.13902  106 GLU A N   
23   C CA  . GLU A 6   ? 0.76548 0.72317 0.80582 0.01715  -0.06901 0.12588  106 GLU A CA  
24   C C   . GLU A 6   ? 0.76258 0.68355 0.79432 0.01180  -0.07119 0.12192  106 GLU A C   
25   O O   . GLU A 6   ? 0.68019 0.60256 0.71582 0.01466  -0.06630 0.10849  106 GLU A O   
26   C CB  . GLU A 6   ? 0.88728 0.83654 0.92616 0.03790  -0.07714 0.12905  106 GLU A CB  
27   C CG  . GLU A 6   ? 1.00733 0.99740 1.05807 0.04737  -0.07444 0.12724  106 GLU A CG  
28   C CD  . GLU A 6   ? 1.11934 1.10252 1.16812 0.06643  -0.08389 0.13362  106 GLU A CD  
29   O OE1 . GLU A 6   ? 1.04824 0.99348 1.08599 0.07213  -0.09212 0.14099  106 GLU A OE1 
30   O OE2 . GLU A 6   ? 1.11570 1.13206 1.17484 0.07579  -0.08277 0.13115  106 GLU A OE2 
31   N N   . GLU A 7   ? 0.72831 0.61632 0.74827 0.00398  -0.07822 0.13322  107 GLU A N   
32   C CA  . GLU A 7   ? 0.80678 0.66027 0.81932 -0.00272 -0.08034 0.12894  107 GLU A CA  
33   C C   . GLU A 7   ? 0.73225 0.60056 0.74906 -0.01981 -0.07280 0.12244  107 GLU A C   
34   O O   . GLU A 7   ? 0.80118 0.65705 0.81679 -0.02017 -0.07172 0.11134  107 GLU A O   
35   C CB  . GLU A 7   ? 0.77341 0.59102 0.77425 -0.00971 -0.08781 0.14300  107 GLU A CB  
36   C CG  . GLU A 7   ? 1.04903 0.82772 1.04286 -0.01440 -0.09078 0.13756  107 GLU A CG  
37   C CD  . GLU A 7   ? 1.20424 0.94272 1.18788 -0.01289 -0.09817 0.14934  107 GLU A CD  
38   O OE1 . GLU A 7   ? 1.21549 0.95890 1.19657 -0.00641 -0.10016 0.16084  107 GLU A OE1 
39   O OE2 . GLU A 7   ? 1.25688 0.96569 1.23539 -0.01742 -0.09874 0.14336  107 GLU A OE2 
40   N N   . ALA A 8   ? 0.62578 0.52132 0.64767 -0.03387 -0.06735 0.12920  108 ALA A N   
41   C CA  . ALA A 8   ? 0.63788 0.55090 0.66587 -0.04927 -0.05919 0.12377  108 ALA A CA  
42   C C   . ALA A 8   ? 0.64757 0.58403 0.68493 -0.03898 -0.05171 0.10862  108 ALA A C   
43   O O   . ALA A 8   ? 0.52613 0.46064 0.56421 -0.04418 -0.04816 0.10005  108 ALA A O   
44   C CB  . ALA A 8   ? 0.63885 0.57825 0.67199 -0.06496 -0.05363 0.13385  108 ALA A CB  
45   N N   . GLN A 9   ? 0.51954 0.47826 0.56414 -0.02393 -0.04921 0.10511  109 GLN A N   
46   C CA  . GLN A 9   ? 0.56422 0.54558 0.61858 -0.01334 -0.04087 0.09086  109 GLN A CA  
47   C C   . GLN A 9   ? 0.46894 0.42357 0.51673 -0.00260 -0.04431 0.07984  109 GLN A C   
48   O O   . GLN A 9   ? 0.43578 0.39871 0.48653 -0.00288 -0.03768 0.06924  109 GLN A O   
49   C CB  . GLN A 9   ? 0.59257 0.59982 0.65634 0.00149  -0.03855 0.08905  109 GLN A CB  
50   C CG  . GLN A 9   ? 0.65045 0.69232 0.72332 -0.00835 -0.03246 0.09583  109 GLN A CG  
51   C CD  . GLN A 9   ? 0.69276 0.76280 0.77666 0.00685  -0.02969 0.09116  109 GLN A CD  
52   O OE1 . GLN A 9   ? 0.73457 0.79309 0.81491 0.02156  -0.03817 0.09318  109 GLN A OE1 
53   N NE2 . GLN A 9   ? 0.73064 0.83796 0.82907 0.00364  -0.01737 0.08455  109 GLN A NE2 
54   N N   . GLN A 10  ? 0.53406 0.45685 0.57291 0.00756  -0.05413 0.08215  110 GLN A N   
55   C CA  . GLN A 10  ? 0.56760 0.46353 0.60008 0.01785  -0.05721 0.07104  110 GLN A CA  
56   C C   . GLN A 10  ? 0.53839 0.41518 0.56332 0.00290  -0.05831 0.06845  110 GLN A C   
57   O O   . GLN A 10  ? 0.50006 0.37083 0.52265 0.00706  -0.05623 0.05594  110 GLN A O   
58   C CB  . GLN A 10  ? 0.65774 0.52305 0.68352 0.03134  -0.06672 0.07501  110 GLN A CB  
59   C CG  . GLN A 10  ? 0.77502 0.65856 0.80899 0.04984  -0.06619 0.07441  110 GLN A CG  
60   C CD  . GLN A 10  ? 0.98885 0.89301 1.03169 0.06239  -0.05798 0.05877  110 GLN A CD  
61   O OE1 . GLN A 10  ? 0.87185 0.75875 0.91025 0.06751  -0.05711 0.04747  110 GLN A OE1 
62   N NE2 . GLN A 10  ? 0.80885 0.75030 0.86431 0.06710  -0.05135 0.05761  110 GLN A NE2 
63   N N   . LYS A 11  ? 0.45544 0.32319 0.47652 -0.01463 -0.06149 0.07985  111 LYS A N   
64   C CA  . LYS A 11  ? 0.50288 0.35709 0.51916 -0.03023 -0.06209 0.07720  111 LYS A CA  
65   C C   . LYS A 11  ? 0.40751 0.29301 0.43149 -0.03578 -0.05245 0.06949  111 LYS A C   
66   O O   . LYS A 11  ? 0.40741 0.28569 0.42780 -0.03752 -0.05201 0.05964  111 LYS A O   
67   C CB  . LYS A 11  ? 0.59297 0.43461 0.60578 -0.04828 -0.06600 0.09134  111 LYS A CB  
68   C CG  . LYS A 11  ? 0.73524 0.53641 0.73813 -0.04492 -0.07551 0.09753  111 LYS A CG  
69   C CD  . LYS A 11  ? 0.95362 0.74634 0.95378 -0.05962 -0.07806 0.11389  111 LYS A CD  
70   C CE  . LYS A 11  ? 1.10181 0.85459 1.09264 -0.05380 -0.08628 0.12091  111 LYS A CE  
71   N NZ  . LYS A 11  ? 1.20997 0.96900 1.19786 -0.06150 -0.08312 0.13072  111 LYS A NZ  
72   N N   . THR A 12  ? 0.36656 0.28749 0.40128 -0.03803 -0.04426 0.07359  112 THR A N   
73   C CA  . THR A 12  ? 0.36254 0.31423 0.40614 -0.04217 -0.03341 0.06706  112 THR A CA  
74   C C   . THR A 12  ? 0.35050 0.30629 0.39450 -0.02515 -0.02945 0.05247  112 THR A C   
75   O O   . THR A 12  ? 0.31910 0.28093 0.36274 -0.02773 -0.02481 0.04468  112 THR A O   
76   C CB  . THR A 12  ? 0.36831 0.35627 0.42452 -0.04677 -0.02447 0.07365  112 THR A CB  
77   O OG1 . THR A 12  ? 0.51690 0.50246 0.57237 -0.06505 -0.02658 0.08655  112 THR A OG1 
78   C CG2 . THR A 12  ? 0.32113 0.34136 0.38827 -0.04774 -0.01143 0.06626  112 THR A CG2 
79   N N   . ILE A 13  ? 0.28887 0.24218 0.33372 -0.00732 -0.03095 0.04876  113 ILE A N   
80   C CA  . ILE A 13  ? 0.29985 0.25489 0.34489 0.00937  -0.02684 0.03461  113 ILE A CA  
81   C C   . ILE A 13  ? 0.36729 0.29073 0.39933 0.00959  -0.03322 0.02669  113 ILE A C   
82   O O   . ILE A 13  ? 0.35987 0.28896 0.39023 0.01353  -0.02803 0.01582  113 ILE A O   
83   C CB  . ILE A 13  ? 0.36364 0.31960 0.41277 0.02831  -0.02817 0.03254  113 ILE A CB  
84   C CG1 . ILE A 13  ? 0.33297 0.32710 0.39683 0.02875  -0.01976 0.03663  113 ILE A CG1 
85   C CG2 . ILE A 13  ? 0.40736 0.35589 0.45431 0.04558  -0.02558 0.01781  113 ILE A CG2 
86   C CD1 . ILE A 13  ? 0.41113 0.40897 0.48018 0.04476  -0.02269 0.03718  113 ILE A CD1 
87   N N   . GLU A 14  ? 0.35214 0.24218 0.37473 0.00507  -0.04407 0.03183  114 GLU A N   
88   C CA  . GLU A 14  ? 0.40081 0.26034 0.41173 0.00443  -0.05007 0.02320  114 GLU A CA  
89   C C   . GLU A 14  ? 0.42634 0.29419 0.43555 -0.01120 -0.04766 0.02084  114 GLU A C   
90   O O   . GLU A 14  ? 0.37021 0.23208 0.37308 -0.00805 -0.04726 0.00907  114 GLU A O   
91   C CB  . GLU A 14  ? 0.60385 0.42591 0.60676 0.00161  -0.06091 0.02972  114 GLU A CB  
92   C CG  . GLU A 14  ? 0.77738 0.56622 0.77009 0.00974  -0.06627 0.01789  114 GLU A CG  
93   C CD  . GLU A 14  ? 0.85921 0.65167 0.85341 0.03127  -0.06255 0.00716  114 GLU A CD  
94   O OE1 . GLU A 14  ? 0.92426 0.72624 0.92539 0.04269  -0.06135 0.01236  114 GLU A OE1 
95   O OE2 . GLU A 14  ? 0.88744 0.67430 0.87602 0.03671  -0.06071 -0.00665 114 GLU A OE2 
96   N N   . ALA A 15  ? 0.36333 0.24638 0.37834 -0.02785 -0.04576 0.03185  115 ALA A N   
97   C CA  . ALA A 15  ? 0.35731 0.25142 0.37290 -0.04275 -0.04299 0.03071  115 ALA A CA  
98   C C   . ALA A 15  ? 0.31856 0.24193 0.33909 -0.03539 -0.03240 0.02193  115 ALA A C   
99   O O   . ALA A 15  ? 0.30761 0.23001 0.32279 -0.03778 -0.03223 0.01397  115 ALA A O   
100  C CB  . ALA A 15  ? 0.35881 0.26579 0.38175 -0.06100 -0.04141 0.04476  115 ALA A CB  
101  N N   . ILE A 16  ? 0.26051 0.21059 0.29139 -0.02638 -0.02316 0.02321  116 ILE A N   
102  C CA  . ILE A 16  ? 0.25343 0.23092 0.29007 -0.01854 -0.01138 0.01525  116 ILE A CA  
103  C C   . ILE A 16  ? 0.31789 0.27965 0.34432 -0.00336 -0.01306 0.00116  116 ILE A C   
104  O O   . ILE A 16  ? 0.29778 0.26809 0.32085 -0.00246 -0.00834 -0.00619 116 ILE A O   
105  C CB  . ILE A 16  ? 0.23421 0.24127 0.28500 -0.01103 -0.00095 0.01802  116 ILE A CB  
106  C CG1 . ILE A 16  ? 0.20904 0.23696 0.27048 -0.02748 0.00331  0.03059  116 ILE A CG1 
107  C CG2 . ILE A 16  ? 0.24649 0.27718 0.30283 0.00032  0.01189  0.00820  116 ILE A CG2 
108  C CD1 . ILE A 16  ? 0.23500 0.28659 0.30915 -0.02130 0.01021  0.03402  116 ILE A CD1 
109  N N   . THR A 17  ? 0.29084 0.23029 0.31230 0.00943  -0.01920 -0.00271 117 THR A N   
110  C CA  . THR A 17  ? 0.35914 0.28568 0.37216 0.02495  -0.01894 -0.01681 117 THR A CA  
111  C C   . THR A 17  ? 0.39073 0.29349 0.38966 0.01802  -0.02665 -0.02350 117 THR A C   
112  O O   . THR A 17  ? 0.36709 0.27080 0.35901 0.02539  -0.02337 -0.03503 117 THR A O   
113  C CB  . THR A 17  ? 0.43992 0.34832 0.45247 0.04070  -0.02312 -0.01935 117 THR A CB  
114  O OG1 . THR A 17  ? 0.44899 0.32762 0.45570 0.03405  -0.03494 -0.01236 117 THR A OG1 
115  C CG2 . THR A 17  ? 0.41101 0.34662 0.43831 0.04883  -0.01529 -0.01472 117 THR A CG2 
116  N N   . LYS A 18  ? 0.34229 0.22469 0.33703 0.00352  -0.03645 -0.01676 118 LYS A N   
117  C CA  . LYS A 18  ? 0.35263 0.21449 0.33557 -0.00470 -0.04375 -0.02387 118 LYS A CA  
118  C C   . LYS A 18  ? 0.34659 0.23329 0.33046 -0.01381 -0.03839 -0.02525 118 LYS A C   
119  O O   . LYS A 18  ? 0.35544 0.23692 0.32934 -0.01194 -0.04000 -0.03622 118 LYS A O   
120  C CB  . LYS A 18  ? 0.40304 0.23807 0.38337 -0.01864 -0.05428 -0.01609 118 LYS A CB  
121  C CG  . LYS A 18  ? 0.50909 0.32418 0.47957 -0.02965 -0.06194 -0.02324 118 LYS A CG  
122  C CD  . LYS A 18  ? 0.83824 0.61745 0.80505 -0.03695 -0.07178 -0.01915 118 LYS A CD  
123  C CE  . LYS A 18  ? 0.92379 0.70821 0.89974 -0.04592 -0.07154 -0.00199 118 LYS A CE  
124  N NZ  . LYS A 18  ? 1.05551 0.80882 1.02903 -0.04134 -0.07752 0.00328  118 LYS A NZ  
125  N N   . ALA A 19  ? 0.29724 0.21155 0.29298 -0.02342 -0.03177 -0.01425 119 ALA A N   
126  C CA  . ALA A 19  ? 0.29448 0.23394 0.29296 -0.03147 -0.02561 -0.01409 119 ALA A CA  
127  C C   . ALA A 19  ? 0.28108 0.23971 0.27855 -0.01604 -0.01521 -0.02332 119 ALA A C   
128  O O   . ALA A 19  ? 0.26854 0.23349 0.25916 -0.01646 -0.01405 -0.02978 119 ALA A O   
129  C CB  . ALA A 19  ? 0.26127 0.22555 0.27424 -0.04461 -0.01935 -0.00015 119 ALA A CB  
130  N N   . ILE A 20  ? 0.26080 0.22938 0.26514 -0.00211 -0.00739 -0.02403 120 ILE A N   
131  C CA  . ILE A 20  ? 0.25227 0.23783 0.25639 0.01324  0.00374  -0.03301 120 ILE A CA  
132  C C   . ILE A 20  ? 0.28134 0.24324 0.26873 0.02358  -0.00204 -0.04709 120 ILE A C   
133  O O   . ILE A 20  ? 0.31373 0.28588 0.29471 0.02974  0.00381  -0.05478 120 ILE A O   
134  C CB  . ILE A 20  ? 0.25218 0.25232 0.26866 0.02574  0.01300  -0.03176 120 ILE A CB  
135  C CG1 . ILE A 20  ? 0.26198 0.29030 0.29527 0.01507  0.02085  -0.01934 120 ILE A CG1 
136  C CG2 . ILE A 20  ? 0.24434 0.25601 0.25947 0.04375  0.02431  -0.04309 120 ILE A CG2 
137  C CD1 . ILE A 20  ? 0.25664 0.31543 0.29711 0.01070  0.03372  -0.01750 120 ILE A CD1 
138  N N   . ASN A 21  ? 0.30001 0.22974 0.27984 0.02586  -0.01303 -0.05066 121 ASN A N   
139  C CA  . ASN A 21  ? 0.36809 0.27358 0.33226 0.03487  -0.01833 -0.06490 121 ASN A CA  
140  C C   . ASN A 21  ? 0.44265 0.34671 0.39592 0.02402  -0.02328 -0.06941 121 ASN A C   
141  O O   . ASN A 21  ? 0.41334 0.31876 0.35567 0.03207  -0.02075 -0.08065 121 ASN A O   
142  C CB  . ASN A 21  ? 0.48234 0.35238 0.44205 0.03711  -0.02899 -0.06660 121 ASN A CB  
143  C CG  . ASN A 21  ? 0.68177 0.52459 0.62565 0.04462  -0.03446 -0.08198 121 ASN A CG  
144  O OD1 . ASN A 21  ? 0.76024 0.59928 0.70091 0.06127  -0.02947 -0.09146 121 ASN A OD1 
145  N ND2 . ASN A 21  ? 0.65275 0.47665 0.58734 0.03198  -0.04434 -0.08508 121 ASN A ND2 
146  N N   . TYR A 22  ? 0.35587 0.25859 0.31224 0.00572  -0.03011 -0.06065 122 TYR A N   
147  C CA  . TYR A 22  ? 0.38284 0.28738 0.33127 -0.00596 -0.03533 -0.06408 122 TYR A CA  
148  C C   . TYR A 22  ? 0.34400 0.28112 0.29334 -0.00207 -0.02471 -0.06471 122 TYR A C   
149  O O   . TYR A 22  ? 0.38743 0.32489 0.32418 0.00141  -0.02605 -0.07477 122 TYR A O   
150  C CB  . TYR A 22  ? 0.38535 0.28725 0.34110 -0.02634 -0.04225 -0.05264 122 TYR A CB  
151  C CG  . TYR A 22  ? 0.44122 0.34508 0.39096 -0.03971 -0.04873 -0.05585 122 TYR A CG  
152  C CD1 . TYR A 22  ? 0.32225 0.25742 0.27800 -0.04606 -0.04250 -0.05012 122 TYR A CD1 
153  C CD2 . TYR A 22  ? 0.68519 0.56003 0.62428 -0.04599 -0.06085 -0.06481 122 TYR A CD2 
154  C CE1 . TYR A 22  ? 0.41552 0.35396 0.36635 -0.05798 -0.04927 -0.05306 122 TYR A CE1 
155  C CE2 . TYR A 22  ? 0.62600 0.50403 0.56045 -0.05841 -0.06738 -0.06876 122 TYR A CE2 
156  C CZ  . TYR A 22  ? 0.67935 0.58970 0.61959 -0.06415 -0.06203 -0.06269 122 TYR A CZ  
157  O OH  . TYR A 22  ? 0.77305 0.68809 0.70933 -0.07608 -0.06920 -0.06653 122 TYR A OH  
158  N N   . MET A 23  ? 0.28293 0.24807 0.24706 -0.00256 -0.01360 -0.05398 123 MET A N   
159  C CA  . MET A 23  ? 0.29210 0.28857 0.25906 0.00017  -0.00217 -0.05273 123 MET A CA  
160  C C   . MET A 23  ? 0.28506 0.28529 0.24392 0.01996  0.00647  -0.06384 123 MET A C   
161  O O   . MET A 23  ? 0.33079 0.34567 0.28259 0.02381  0.01155  -0.06782 123 MET A O   
162  C CB  . MET A 23  ? 0.28775 0.31155 0.27406 -0.00612 0.00847  -0.03888 123 MET A CB  
163  C CG  . MET A 23  ? 0.25036 0.27204 0.24311 -0.02669 0.00063  -0.02834 123 MET A CG  
164  S SD  . MET A 23  ? 0.30051 0.35428 0.31539 -0.03648 0.01316  -0.01254 123 MET A SD  
165  C CE  . MET A 23  ? 0.27500 0.32273 0.29753 -0.02666 0.01646  -0.01107 123 MET A CE  
166  N N   . ALA A 24  ? 0.29662 0.28345 0.25607 0.03291  0.00819  -0.06884 124 ALA A N   
167  C CA  . ALA A 24  ? 0.30250 0.28951 0.25398 0.05180  0.01614  -0.08043 124 ALA A CA  
168  C C   . ALA A 24  ? 0.41093 0.37869 0.34153 0.05425  0.00771  -0.09343 124 ALA A C   
169  O O   . ALA A 24  ? 0.35895 0.33731 0.28015 0.06384  0.01480  -0.10060 124 ALA A O   
170  C CB  . ALA A 24  ? 0.33233 0.30659 0.28970 0.06428  0.01799  -0.08331 124 ALA A CB  
171  N N   . LYS A 25  ? 0.33879 0.27830 0.26179 0.04549  -0.00696 -0.09681 125 LYS A N   
172  C CA  . LYS A 25  ? 0.37228 0.29241 0.27583 0.04663  -0.01549 -0.11064 125 LYS A CA  
173  C C   . LYS A 25  ? 0.37772 0.31719 0.27409 0.03862  -0.01621 -0.11058 125 LYS A C   
174  O O   . LYS A 25  ? 0.42443 0.36214 0.30458 0.04551  -0.01670 -0.12217 125 LYS A O   
175  C CB  . LYS A 25  ? 0.43934 0.32603 0.33907 0.03698  -0.03010 -0.11348 125 LYS A CB  
176  C CG  . LYS A 25  ? 0.56876 0.43428 0.47503 0.04487  -0.03073 -0.11258 125 LYS A CG  
177  C CD  . LYS A 25  ? 0.90092 0.73942 0.79435 0.05823  -0.03295 -0.12806 125 LYS A CD  
178  C CE  . LYS A 25  ? 0.90814 0.71714 0.80679 0.05955  -0.03926 -0.12621 125 LYS A CE  
179  N NZ  . LYS A 25  ? 1.00176 0.81114 0.90781 0.07727  -0.03107 -0.12658 125 LYS A NZ  
180  N N   A ARG A 26  ? 0.37689 0.33506 0.28491 0.02419  -0.01640 -0.09766 126 ARG A N   
181  N N   B ARG A 26  ? 0.37690 0.33509 0.28490 0.02421  -0.01639 -0.09767 126 ARG A N   
182  C CA  A ARG A 26  ? 0.41416 0.39277 0.31778 0.01620  -0.01722 -0.09586 126 ARG A CA  
183  C CA  B ARG A 26  ? 0.41418 0.39269 0.31759 0.01633  -0.01723 -0.09602 126 ARG A CA  
184  C C   A ARG A 26  ? 0.39919 0.41134 0.30845 0.02500  -0.00128 -0.08988 126 ARG A C   
185  C C   B ARG A 26  ? 0.39922 0.41131 0.30835 0.02510  -0.00128 -0.08998 126 ARG A C   
186  O O   A ARG A 26  ? 0.37994 0.41124 0.28512 0.02106  -0.00041 -0.08788 126 ARG A O   
187  O O   B ARG A 26  ? 0.38001 0.41123 0.28500 0.02122  -0.00040 -0.08803 126 ARG A O   
188  C CB  A ARG A 26  ? 0.38710 0.36875 0.30133 -0.00463 -0.02532 -0.08496 126 ARG A CB  
189  C CB  B ARG A 26  ? 0.38694 0.36852 0.30077 -0.00454 -0.02542 -0.08524 126 ARG A CB  
190  C CG  A ARG A 26  ? 0.47690 0.42609 0.38753 -0.01571 -0.04031 -0.08921 126 ARG A CG  
191  C CG  B ARG A 26  ? 0.51369 0.46389 0.42870 -0.01476 -0.03796 -0.08610 126 ARG A CG  
192  C CD  A ARG A 26  ? 0.54179 0.47688 0.43458 -0.01771 -0.05106 -0.10370 126 ARG A CD  
193  C CD  B ARG A 26  ? 0.49972 0.42874 0.39966 -0.02126 -0.05160 -0.09866 126 ARG A CD  
194  N NE  A ARG A 26  ? 0.47407 0.43403 0.36456 -0.02502 -0.05201 -0.10181 126 ARG A NE  
195  N NE  B ARG A 26  ? 0.52301 0.42377 0.42620 -0.03383 -0.06275 -0.09788 126 ARG A NE  
196  C CZ  A ARG A 26  ? 0.49644 0.45425 0.38714 -0.04156 -0.06318 -0.10189 126 ARG A CZ  
197  C CZ  B ARG A 26  ? 0.66220 0.53062 0.55850 -0.02877 -0.06828 -0.10688 126 ARG A CZ  
198  N NH1 A ARG A 26  ? 0.62013 0.55054 0.51258 -0.05312 -0.07400 -0.10440 126 ARG A NH1 
199  N NH1 B ARG A 26  ? 0.75363 0.61353 0.64048 -0.01133 -0.06375 -0.11715 126 ARG A NH1 
200  N NH2 A ARG A 26  ? 0.46711 0.45094 0.35681 -0.04633 -0.06314 -0.09934 126 ARG A NH2 
201  N NH2 B ARG A 26  ? 0.51329 0.35672 0.41270 -0.04143 -0.07793 -0.10554 126 ARG A NH2 
202  N N   . ARG A 27  ? 0.32298 0.35085 0.24109 -0.07804 0.02830  -0.06330 127 ARG A N   
203  C CA  . ARG A 27  ? 0.29448 0.31907 0.20097 -0.07364 0.02621  -0.04977 127 ARG A CA  
204  C C   . ARG A 27  ? 0.35873 0.38505 0.26451 -0.06547 0.01595  -0.03580 127 ARG A C   
205  O O   . ARG A 27  ? 0.33444 0.36738 0.22761 -0.06393 0.01208  -0.02436 127 ARG A O   
206  C CB  . ARG A 27  ? 0.37610 0.41090 0.26057 -0.08125 0.02994  -0.05029 127 ARG A CB  
207  C CG  . ARG A 27  ? 0.37003 0.40237 0.25734 -0.09041 0.04220  -0.06653 127 ARG A CG  
208  C CD  . ARG A 27  ? 0.42743 0.46960 0.29101 -0.09962 0.04796  -0.06915 127 ARG A CD  
209  N NE  . ARG A 27  ? 0.38938 0.42866 0.25979 -0.10939 0.06143  -0.08786 127 ARG A NE  
210  C CZ  . ARG A 27  ? 0.39669 0.44557 0.24840 -0.12114 0.06964  -0.09770 127 ARG A CZ  
211  N NH1 . ARG A 27  ? 0.43342 0.49680 0.25583 -0.12445 0.06466  -0.08878 127 ARG A NH1 
212  N NH2 . ARG A 27  ? 0.44976 0.49454 0.31320 -0.13023 0.08373  -0.11663 127 ARG A NH2 
213  N N   . ILE A 28  ? 0.31201 0.33195 0.23322 -0.06020 0.01265  -0.03606 128 ILE A N   
214  C CA  . ILE A 28  ? 0.26029 0.27892 0.18493 -0.05277 0.00539  -0.02500 128 ILE A CA  
215  C C   . ILE A 28  ? 0.30310 0.30813 0.23455 -0.04721 0.00792  -0.01859 128 ILE A C   
216  O O   . ILE A 28  ? 0.29469 0.29071 0.23681 -0.04665 0.01124  -0.02396 128 ILE A O   
217  C CB  . ILE A 28  ? 0.29353 0.31255 0.23001 -0.05108 0.00200  -0.02971 128 ILE A CB  
218  C CG1 . ILE A 28  ? 0.29350 0.32768 0.22538 -0.05685 -0.00086 -0.03658 128 ILE A CG1 
219  C CG2 . ILE A 28  ? 0.29340 0.30722 0.23603 -0.04364 -0.00270 -0.01999 128 ILE A CG2 
220  C CD1 . ILE A 28  ? 0.40114 0.43423 0.34801 -0.05693 -0.00029 -0.04491 128 ILE A CD1 
221  N N   . GLY A 29  ? 0.27796 0.28261 0.20531 -0.04344 0.00666  -0.00701 129 GLY A N   
222  C CA  . GLY A 29  ? 0.31510 0.30754 0.25078 -0.03923 0.01030  -0.00289 129 GLY A CA  
223  C C   . GLY A 29  ? 0.29881 0.28470 0.24636 -0.03554 0.00782  -0.00497 129 GLY A C   
224  O O   . GLY A 29  ? 0.31460 0.30436 0.26407 -0.03365 0.00321  -0.00332 129 GLY A O   
225  N N   . ALA A 30  ? 0.25844 0.23533 0.21392 -0.03505 0.01099  -0.00873 130 ALA A N   
226  C CA  . ALA A 30  ? 0.23073 0.20335 0.19444 -0.03300 0.00860  -0.01129 130 ALA A CA  
227  C C   . ALA A 30  ? 0.26274 0.22809 0.23337 -0.03263 0.01170  -0.01254 130 ALA A C   
228  O O   . ALA A 30  ? 0.25771 0.22052 0.23003 -0.03430 0.01579  -0.01393 130 ALA A O   
229  C CB  . ALA A 30  ? 0.25057 0.22543 0.21796 -0.03479 0.00665  -0.01783 130 ALA A CB  
230  N N   . LEU A 31  ? 0.27151 0.23423 0.24643 -0.03123 0.01022  -0.01317 131 LEU A N   
231  C CA  . LEU A 31  ? 0.28231 0.24029 0.26377 -0.03208 0.01296  -0.01602 131 LEU A CA  
232  C C   . LEU A 31  ? 0.25056 0.20980 0.23287 -0.03283 0.00916  -0.01974 131 LEU A C   
233  O O   . LEU A 31  ? 0.27627 0.23501 0.25667 -0.03162 0.00891  -0.01841 131 LEU A O   
234  C CB  . LEU A 31  ? 0.30385 0.25748 0.28907 -0.03044 0.01852  -0.01168 131 LEU A CB  
235  C CG  . LEU A 31  ? 0.27617 0.22473 0.27094 -0.03212 0.02369  -0.01627 131 LEU A CG  
236  C CD1 . LEU A 31  ? 0.30065 0.24803 0.29987 -0.03440 0.02593  -0.02004 131 LEU A CD1 
237  C CD2 . LEU A 31  ? 0.32666 0.27064 0.32899 -0.02974 0.03087  -0.01031 131 LEU A CD2 
238  N N   . LEU A 32  ? 0.24661 0.20828 0.23242 -0.03497 0.00645  -0.02359 132 LEU A N   
239  C CA  . LEU A 32  ? 0.23185 0.19763 0.21637 -0.03599 0.00166  -0.02499 132 LEU A CA  
240  C C   . LEU A 32  ? 0.22416 0.19289 0.21331 -0.03944 0.00028  -0.02950 132 LEU A C   
241  O O   . LEU A 32  ? 0.26004 0.23124 0.25688 -0.04038 -0.00106 -0.03017 132 LEU A O   
242  C CB  . LEU A 32  ? 0.26056 0.23035 0.24691 -0.03491 -0.00191 -0.02245 132 LEU A CB  
243  C CG  . LEU A 32  ? 0.32567 0.30069 0.31182 -0.03513 -0.00670 -0.02048 132 LEU A CG  
244  C CD1 . LEU A 32  ? 0.39608 0.36961 0.37341 -0.03505 -0.00613 -0.02063 132 LEU A CD1 
245  C CD2 . LEU A 32  ? 0.30690 0.28403 0.29950 -0.03333 -0.00731 -0.01723 132 LEU A CD2 
246  N N   . THR A 33  ? 0.22119 0.19039 0.20699 -0.04204 0.00117  -0.03356 133 THR A N   
247  C CA  . THR A 33  ? 0.22619 0.20061 0.21536 -0.04696 -0.00028 -0.04004 133 THR A CA  
248  C C   . THR A 33  ? 0.23873 0.22277 0.22022 -0.04960 -0.00732 -0.03967 133 THR A C   
249  O O   . THR A 33  ? 0.28983 0.27281 0.26207 -0.04938 -0.00650 -0.03865 133 THR A O   
250  C CB  . THR A 33  ? 0.26604 0.23513 0.25805 -0.04976 0.00773  -0.04701 133 THR A CB  
251  O OG1 . THR A 33  ? 0.27958 0.24067 0.27994 -0.04690 0.01447  -0.04476 133 THR A OG1 
252  C CG2 . THR A 33  ? 0.25720 0.23397 0.25220 -0.05674 0.00632  -0.05674 133 THR A CG2 
253  N N   . ILE A 34  ? 0.24211 0.23626 0.22822 -0.05207 -0.01413 -0.03946 134 ILE A N   
254  C CA  . ILE A 34  ? 0.26475 0.27123 0.24362 -0.05468 -0.02214 -0.03636 134 ILE A CA  
255  C C   . ILE A 34  ? 0.29450 0.31093 0.27087 -0.06245 -0.02453 -0.04556 134 ILE A C   
256  O O   . ILE A 34  ? 0.27829 0.29981 0.26625 -0.06471 -0.02684 -0.04908 134 ILE A O   
257  C CB  . ILE A 34  ? 0.28887 0.30241 0.27784 -0.05133 -0.02911 -0.02644 134 ILE A CB  
258  C CG1 . ILE A 34  ? 0.33025 0.33375 0.32398 -0.04521 -0.02460 -0.02100 134 ILE A CG1 
259  C CG2 . ILE A 34  ? 0.32946 0.35709 0.31166 -0.05317 -0.03766 -0.01947 134 ILE A CG2 
260  C CD1 . ILE A 34  ? 0.34780 0.35543 0.35746 -0.04240 -0.02757 -0.01371 134 ILE A CD1 
261  N N   . GLU A 35  ? 0.25864 0.27842 0.22059 -0.06735 -0.02330 -0.05060 135 GLU A N   
262  C CA  . GLU A 35  ? 0.31695 0.34809 0.27425 -0.07681 -0.02478 -0.06200 135 GLU A CA  
263  C C   . GLU A 35  ? 0.35099 0.40212 0.30886 -0.07984 -0.03806 -0.05681 135 GLU A C   
264  O O   . GLU A 35  ? 0.35800 0.41571 0.31258 -0.07595 -0.04546 -0.04359 135 GLU A O   
265  C CB  . GLU A 35  ? 0.34079 0.37180 0.28091 -0.08220 -0.01964 -0.06851 135 GLU A CB  
266  C CG  . GLU A 35  ? 0.35195 0.39135 0.28830 -0.09358 -0.01635 -0.08522 135 GLU A CG  
267  C CD  . GLU A 35  ? 0.54594 0.58685 0.46388 -0.10038 -0.01070 -0.09236 135 GLU A CD  
268  O OE1 . GLU A 35  ? 0.53621 0.59039 0.43687 -0.10310 -0.01889 -0.08628 135 GLU A OE1 
269  O OE2 . GLU A 35  ? 0.50897 0.53771 0.43120 -0.10297 0.00281  -0.10332 135 GLU A OE2 
270  N N   . ARG A 36  ? 0.33108 0.39274 0.29589 -0.08681 -0.04082 -0.06674 136 ARG A N   
271  C CA  . ARG A 36  ? 0.36918 0.45352 0.33609 -0.09090 -0.05470 -0.06236 136 ARG A CA  
272  C C   . ARG A 36  ? 0.40433 0.50407 0.35579 -0.10329 -0.05645 -0.07608 136 ARG A C   
273  O O   . ARG A 36  ? 0.39946 0.49944 0.33061 -0.10659 -0.05357 -0.07766 136 ARG A O   
274  C CB  . ARG A 36  ? 0.38400 0.46982 0.37544 -0.08850 -0.05759 -0.06154 136 ARG A CB  
275  C CG  . ARG A 36  ? 0.48382 0.59373 0.48395 -0.09065 -0.07314 -0.05288 136 ARG A CG  
276  C CD  . ARG A 36  ? 0.60745 0.71717 0.63543 -0.08886 -0.07381 -0.05432 136 ARG A CD  
277  N NE  . ARG A 36  ? 0.78802 0.92164 0.82903 -0.09053 -0.08883 -0.04505 136 ARG A NE  
278  C CZ  . ARG A 36  ? 0.74169 0.88099 0.79266 -0.08365 -0.09605 -0.02632 136 ARG A CZ  
279  N NH1 . ARG A 36  ? 0.71070 0.83366 0.75904 -0.07536 -0.08943 -0.01658 136 ARG A NH1 
280  N NH2 . ARG A 36  ? 0.59781 0.76069 0.66426 -0.08535 -0.10994 -0.01704 136 ARG A NH2 
281  N N   . ASP A 37  ? 0.35412 0.46684 0.31528 -0.11107 -0.06004 -0.08753 137 ASP A N   
282  C CA  . ASP A 37  ? 0.40380 0.53482 0.34989 -0.12481 -0.06236 -0.10250 137 ASP A CA  
283  C C   . ASP A 37  ? 0.45760 0.57449 0.40343 -0.13129 -0.04537 -0.12338 137 ASP A C   
284  O O   . ASP A 37  ? 0.43632 0.56231 0.36482 -0.14236 -0.04226 -0.13645 137 ASP A O   
285  C CB  . ASP A 37  ? 0.39831 0.55401 0.35617 -0.13159 -0.07534 -0.10596 137 ASP A CB  
286  C CG  . ASP A 37  ? 0.52751 0.70358 0.48418 -0.12765 -0.09333 -0.08484 137 ASP A CG  
287  O OD1 . ASP A 37  ? 0.63820 0.81971 0.57389 -0.12664 -0.09749 -0.07347 137 ASP A OD1 
288  O OD2 . ASP A 37  ? 0.71325 0.89942 0.69234 -0.12530 -0.10230 -0.07886 137 ASP A OD2 
289  N N   . THR A 38  ? 0.36482 0.46010 0.33027 -0.12502 -0.03336 -0.12640 138 THR A N   
290  C CA  . THR A 38  ? 0.42408 0.50458 0.39492 -0.12966 -0.01570 -0.14331 138 THR A CA  
291  C C   . THR A 38  ? 0.43734 0.50161 0.39548 -0.12464 -0.00683 -0.13775 138 THR A C   
292  O O   . THR A 38  ? 0.42584 0.47727 0.38594 -0.11301 -0.00748 -0.12200 138 THR A O   
293  C CB  . THR A 38  ? 0.43829 0.50315 0.43609 -0.12436 -0.00628 -0.14574 138 THR A CB  
294  O OG1 . THR A 38  ? 0.49959 0.57919 0.51119 -0.12740 -0.01569 -0.14812 138 THR A OG1 
295  C CG2 . THR A 38  ? 0.39262 0.44564 0.40154 -0.13061 0.01245  -0.16389 138 THR A CG2 
296  N N   . GLY A 39  ? 0.41379 0.47957 0.35974 -0.13409 0.00176  -0.15147 139 GLY A N   
297  C CA  . GLY A 39  ? 0.40397 0.45477 0.34047 -0.12987 0.01091  -0.14691 139 GLY A CA  
298  C C   . GLY A 39  ? 0.47005 0.49681 0.42749 -0.12083 0.02455  -0.14406 139 GLY A C   
299  O O   . GLY A 39  ? 0.45480 0.47488 0.43252 -0.12285 0.03442  -0.15397 139 GLY A O   
300  N N   . MET A 40  ? 0.46932 0.48407 0.42272 -0.11090 0.02514  -0.12968 140 MET A N   
301  C CA  . MET A 40  ? 0.50664 0.50179 0.47784 -0.10174 0.03547  -0.12352 140 MET A CA  
302  C C   . MET A 40  ? 0.45022 0.43395 0.41991 -0.10095 0.04683  -0.12432 140 MET A C   
303  O O   . MET A 40  ? 0.43212 0.40273 0.41186 -0.09166 0.05118  -0.11370 140 MET A O   
304  C CB  . MET A 40  ? 0.49788 0.48959 0.47088 -0.09011 0.02587  -0.10545 140 MET A CB  
305  C CG  . MET A 40  ? 0.62003 0.62028 0.60070 -0.09078 0.01799  -0.10562 140 MET A CG  
306  S SD  . MET A 40  ? 0.50939 0.50005 0.50068 -0.07878 0.01494  -0.08988 140 MET A SD  
307  C CE  . MET A 40  ? 0.33254 0.30531 0.32884 -0.07210 0.02716  -0.08439 140 MET A CE  
308  N N   . GLY A 41  ? 0.42081 0.41049 0.37873 -0.11135 0.05204  -0.13733 141 GLY A N   
309  C CA  . GLY A 41  ? 0.46158 0.44053 0.41933 -0.11150 0.06399  -0.13917 141 GLY A CA  
310  C C   . GLY A 41  ? 0.42876 0.39076 0.41454 -0.10774 0.08026  -0.14117 141 GLY A C   
311  O O   . GLY A 41  ? 0.47448 0.42530 0.46722 -0.10136 0.08639  -0.13317 141 GLY A O   
312  N N   . ASP A 42  ? 0.43776 0.39831 0.44239 -0.11136 0.08758  -0.15075 142 ASP A N   
313  C CA  . ASP A 42  ? 0.47212 0.41696 0.50701 -0.10717 0.10396  -0.15020 142 ASP A CA  
314  C C   . ASP A 42  ? 0.42134 0.35742 0.46431 -0.09244 0.09859  -0.12800 142 ASP A C   
315  O O   . ASP A 42  ? 0.42861 0.35313 0.49045 -0.08672 0.10899  -0.12097 142 ASP A O   
316  C CB  . ASP A 42  ? 0.48836 0.43365 0.54338 -0.11343 0.11288  -0.16358 142 ASP A CB  
317  C CG  . ASP A 42  ? 0.60452 0.56271 0.65761 -0.12572 0.12088  -0.18217 142 ASP A CG  
318  O OD1 . ASP A 42  ? 0.65616 0.61491 0.70218 -0.13010 0.12769  -0.18697 142 ASP A OD1 
319  O OD2 . ASP A 42  ? 0.62748 0.59671 0.68690 -0.13056 0.12044  -0.19068 142 ASP A OD2 
320  N N   . TYR A 43  ? 0.35298 0.29548 0.38325 -0.08672 0.08284  -0.11690 143 TYR A N   
321  C CA  . TYR A 43  ? 0.35006 0.28649 0.38433 -0.07450 0.07742  -0.09770 143 TYR A CA  
322  C C   . TYR A 43  ? 0.32612 0.26309 0.34580 -0.06969 0.07026  -0.08798 143 TYR A C   
323  O O   . TYR A 43  ? 0.36275 0.29325 0.39094 -0.06155 0.07141  -0.07556 143 TYR A O   
324  C CB  . TYR A 43  ? 0.40031 0.34212 0.43026 -0.07114 0.06638  -0.09154 143 TYR A CB  
325  C CG  . TYR A 43  ? 0.43106 0.37213 0.47747 -0.07583 0.07401  -0.10135 143 TYR A CG  
326  C CD1 . TYR A 43  ? 0.44874 0.37904 0.51847 -0.07157 0.08614  -0.09677 143 TYR A CD1 
327  C CD2 . TYR A 43  ? 0.45306 0.40524 0.49343 -0.08494 0.06967  -0.11507 143 TYR A CD2 
328  C CE1 . TYR A 43  ? 0.52791 0.45659 0.61564 -0.07598 0.09508  -0.10627 143 TYR A CE1 
329  C CE2 . TYR A 43  ? 0.48048 0.43257 0.53835 -0.08999 0.07734  -0.12585 143 TYR A CE2 
330  C CZ  . TYR A 43  ? 0.48279 0.42210 0.56492 -0.08542 0.09084  -0.12188 143 TYR A CZ  
331  O OH  . TYR A 43  ? 0.57557 0.51405 0.67771 -0.09048 0.10000  -0.13293 143 TYR A OH  
332  N N   . ILE A 44  ? 0.35974 0.30547 0.35845 -0.07468 0.06278  -0.09269 144 ILE A N   
333  C CA  . ILE A 44  ? 0.37779 0.32321 0.36468 -0.07098 0.05848  -0.08494 144 ILE A CA  
334  C C   . ILE A 44  ? 0.35646 0.29161 0.35710 -0.07043 0.07188  -0.08648 144 ILE A C   
335  O O   . ILE A 44  ? 0.33872 0.26969 0.34265 -0.06335 0.07045  -0.07572 144 ILE A O   
336  C CB  . ILE A 44  ? 0.40198 0.35876 0.36550 -0.07764 0.05092  -0.08999 144 ILE A CB  
337  C CG1 . ILE A 44  ? 0.37847 0.34585 0.33325 -0.07598 0.03651  -0.08409 144 ILE A CG1 
338  C CG2 . ILE A 44  ? 0.41446 0.36917 0.36812 -0.07486 0.05031  -0.08367 144 ILE A CG2 
339  C CD1 . ILE A 44  ? 0.37860 0.36036 0.31248 -0.08245 0.02777  -0.08635 144 ILE A CD1 
340  N N   . GLU A 45  ? 0.38654 0.31785 0.39869 -0.07816 0.08586  -0.10037 145 GLU A N   
341  C CA  . GLU A 45  ? 0.36396 0.28515 0.39340 -0.07858 0.10090  -0.10311 145 GLU A CA  
342  C C   . GLU A 45  ? 0.40151 0.31394 0.45728 -0.06837 0.10515  -0.08899 145 GLU A C   
343  O O   . GLU A 45  ? 0.46112 0.36643 0.53305 -0.06585 0.11429  -0.08573 145 GLU A O   
344  C CB  . GLU A 45  ? 0.40122 0.32066 0.43937 -0.09065 0.11684  -0.12353 145 GLU A CB  
345  C CG  . GLU A 45  ? 0.63373 0.56166 0.64602 -0.10211 0.11645  -0.13769 145 GLU A CG  
346  C CD  . GLU A 45  ? 0.93309 0.86254 0.95153 -0.11628 0.13134  -0.16088 145 GLU A CD  
347  O OE1 . GLU A 45  ? 0.82923 0.74989 0.87779 -0.11632 0.14556  -0.16574 145 GLU A OE1 
348  O OE2 . GLU A 45  ? 0.91818 0.85898 0.91192 -0.12764 0.12902  -0.17384 145 GLU A OE2 
349  N N   . THR A 46  ? 0.35371 0.26745 0.41445 -0.06249 0.09867  -0.07953 146 THR A N   
350  C CA  . THR A 46  ? 0.34208 0.25010 0.42546 -0.05318 0.10190  -0.06413 146 THR A CA  
351  C C   . THR A 46  ? 0.35477 0.26632 0.43009 -0.04454 0.08979  -0.04815 146 THR A C   
352  O O   . THR A 46  ? 0.43283 0.34234 0.52584 -0.03732 0.09142  -0.03447 146 THR A O   
353  C CB  . THR A 46  ? 0.37715 0.28516 0.46873 -0.05079 0.10149  -0.05983 146 THR A CB  
354  O OG1 . THR A 46  ? 0.36365 0.27949 0.43260 -0.04863 0.08569  -0.05512 146 THR A OG1 
355  C CG2 . THR A 46  ? 0.37336 0.27906 0.47483 -0.05994 0.11331  -0.07718 146 THR A CG2 
356  N N   . GLY A 47  ? 0.36742 0.28537 0.41826 -0.04531 0.07792  -0.04907 147 GLY A N   
357  C CA  . GLY A 47  ? 0.34665 0.26880 0.39053 -0.03839 0.06698  -0.03661 147 GLY A CA  
358  C C   . GLY A 47  ? 0.33178 0.25260 0.37432 -0.03864 0.06874  -0.03770 147 GLY A C   
359  O O   . GLY A 47  ? 0.38473 0.29995 0.43472 -0.04348 0.08025  -0.04658 147 GLY A O   
360  N N   . ILE A 48  ? 0.32007 0.24601 0.35405 -0.03396 0.05833  -0.02955 148 ILE A N   
361  C CA  . ILE A 48  ? 0.32579 0.25100 0.35865 -0.03356 0.05905  -0.02970 148 ILE A CA  
362  C C   . ILE A 48  ? 0.28504 0.21286 0.29494 -0.03876 0.05563  -0.03749 148 ILE A C   
363  O O   . ILE A 48  ? 0.31791 0.25193 0.31420 -0.03767 0.04532  -0.03467 148 ILE A O   
364  C CB  . ILE A 48  ? 0.32932 0.26016 0.36635 -0.02667 0.04996  -0.01809 148 ILE A CB  
365  C CG1 . ILE A 48  ? 0.41869 0.35066 0.47695 -0.02137 0.05115  -0.00726 148 ILE A CG1 
366  C CG2 . ILE A 48  ? 0.33137 0.26123 0.36899 -0.02653 0.05138  -0.01933 148 ILE A CG2 
367  C CD1 . ILE A 48  ? 0.39195 0.31699 0.47545 -0.02104 0.06381  -0.00680 148 ILE A CD1 
368  N N   . PRO A 49  ? 0.31872 0.24271 0.32459 -0.04448 0.06433  -0.04630 149 PRO A N   
369  C CA  . PRO A 49  ? 0.40059 0.32921 0.38314 -0.04949 0.06059  -0.05116 149 PRO A CA  
370  C C   . PRO A 49  ? 0.35994 0.29219 0.33597 -0.04443 0.05206  -0.04250 149 PRO A C   
371  O O   . PRO A 49  ? 0.34948 0.27842 0.33669 -0.04051 0.05456  -0.03840 149 PRO A O   
372  C CB  . PRO A 49  ? 0.36223 0.28546 0.34382 -0.05688 0.07414  -0.06197 149 PRO A CB  
373  C CG  . PRO A 49  ? 0.44075 0.35617 0.44713 -0.05700 0.08589  -0.06557 149 PRO A CG  
374  C CD  . PRO A 49  ? 0.33312 0.24882 0.35663 -0.04725 0.07918  -0.05214 149 PRO A CD  
375  N N   . LEU A 50  ? 0.31362 0.25308 0.27449 -0.04473 0.04265  -0.03991 150 LEU A N   
376  C CA  . LEU A 50  ? 0.27817 0.22101 0.23453 -0.04087 0.03646  -0.03265 150 LEU A CA  
377  C C   . LEU A 50  ? 0.32831 0.27561 0.26682 -0.04520 0.03574  -0.03304 150 LEU A C   
378  O O   . LEU A 50  ? 0.32013 0.26577 0.25662 -0.04425 0.03874  -0.02999 150 LEU A O   
379  C CB  . LEU A 50  ? 0.28471 0.23273 0.24420 -0.03618 0.02648  -0.02639 150 LEU A CB  
380  C CG  . LEU A 50  ? 0.36779 0.31504 0.34176 -0.03060 0.02466  -0.02178 150 LEU A CG  
381  C CD1 . LEU A 50  ? 0.36504 0.30913 0.34938 -0.03011 0.02826  -0.02260 150 LEU A CD1 
382  C CD2 . LEU A 50  ? 0.39636 0.34966 0.36982 -0.02788 0.01625  -0.01758 150 LEU A CD2 
383  N N   . ASN A 51  ? 0.34823 0.30230 0.27452 -0.05002 0.03171  -0.03590 151 ASN A N   
384  C CA  . ASN A 51  ? 0.32209 0.28476 0.23086 -0.05385 0.02784  -0.03304 151 ASN A CA  
385  C C   . ASN A 51  ? 0.34961 0.31400 0.26099 -0.04783 0.02349  -0.02153 151 ASN A C   
386  O O   . ASN A 51  ? 0.35618 0.32139 0.25921 -0.04886 0.02667  -0.01757 151 ASN A O   
387  C CB  . ASN A 51  ? 0.37237 0.33425 0.26735 -0.06186 0.03707  -0.04096 151 ASN A CB  
388  C CG  . ASN A 51  ? 0.59204 0.55557 0.48329 -0.07004 0.04124  -0.05400 151 ASN A CG  
389  O OD1 . ASN A 51  ? 0.59741 0.55865 0.50124 -0.06842 0.04013  -0.05715 151 ASN A OD1 
390  N ND2 . ASN A 51  ? 0.89126 0.85934 0.76511 -0.07959 0.04692  -0.06217 151 ASN A ND2 
391  N N   . ALA A 52  ? 0.30505 0.26995 0.22900 -0.04200 0.01743  -0.01655 152 ALA A N   
392  C CA  . ALA A 52  ? 0.31222 0.27702 0.24546 -0.03633 0.01573  -0.00835 152 ALA A CA  
393  C C   . ALA A 52  ? 0.33311 0.30670 0.26610 -0.03514 0.00824  -0.00017 152 ALA A C   
394  O O   . ALA A 52  ? 0.31608 0.29514 0.24728 -0.03691 0.00248  -0.00124 152 ALA A O   
395  C CB  . ALA A 52  ? 0.30210 0.26246 0.25144 -0.03170 0.01550  -0.00984 152 ALA A CB  
396  N N   . LYS A 53  ? 0.28182 0.25664 0.21994 -0.03194 0.00924  0.00847  153 LYS A N   
397  C CA  . LYS A 53  ? 0.30075 0.28292 0.24704 -0.02935 0.00373  0.01797  153 LYS A CA  
398  C C   . LYS A 53  ? 0.37629 0.35728 0.33747 -0.02688 0.00087  0.01445  153 LYS A C   
399  O O   . LYS A 53  ? 0.33297 0.30786 0.30132 -0.02539 0.00389  0.00820  153 LYS A O   
400  C CB  . LYS A 53  ? 0.34081 0.32221 0.29637 -0.02558 0.00821  0.02756  153 LYS A CB  
401  C CG  . LYS A 53  ? 0.63156 0.62096 0.59934 -0.02269 0.00420  0.03992  153 LYS A CG  
402  C CD  . LYS A 53  ? 0.69233 0.68058 0.67158 -0.01883 0.01057  0.05085  153 LYS A CD  
403  C CE  . LYS A 53  ? 0.72615 0.72149 0.72529 -0.01516 0.00821  0.06372  153 LYS A CE  
404  N NZ  . LYS A 53  ? 0.76894 0.76243 0.78419 -0.01090 0.01625  0.07524  153 LYS A NZ  
405  N N   . VAL A 54  ? 0.27022 0.25818 0.23631 -0.02685 -0.00493 0.01880  154 VAL A N   
406  C CA  . VAL A 54  ? 0.29186 0.27858 0.27179 -0.02533 -0.00618 0.01509  154 VAL A CA  
407  C C   . VAL A 54  ? 0.30512 0.28999 0.30401 -0.02172 -0.00178 0.01842  154 VAL A C   
408  O O   . VAL A 54  ? 0.33260 0.32079 0.33992 -0.01963 -0.00053 0.02821  154 VAL A O   
409  C CB  . VAL A 54  ? 0.33499 0.32942 0.31725 -0.02681 -0.01262 0.01796  154 VAL A CB  
410  C CG1 . VAL A 54  ? 0.37239 0.36430 0.36884 -0.02582 -0.01186 0.01337  154 VAL A CG1 
411  C CG2 . VAL A 54  ? 0.34414 0.34147 0.30959 -0.03153 -0.01617 0.01253  154 VAL A CG2 
412  N N   . SER A 55  ? 0.28627 0.26685 0.29273 -0.02144 0.00107  0.01036  155 SER A N   
413  C CA  . SER A 55  ? 0.27469 0.25499 0.30118 -0.01995 0.00576  0.00971  155 SER A CA  
414  C C   . SER A 55  ? 0.26239 0.24214 0.29141 -0.02204 0.00575  0.00024  155 SER A C   
415  O O   . SER A 55  ? 0.24125 0.21964 0.25701 -0.02348 0.00302  -0.00467 155 SER A O   
416  C CB  . SER A 55  ? 0.28614 0.26324 0.31924 -0.01856 0.01172  0.00852  155 SER A CB  
417  O OG  . SER A 55  ? 0.26880 0.24316 0.29213 -0.01972 0.01135  0.00076  155 SER A OG  
418  N N   . SER A 56  ? 0.22427 0.20521 0.27141 -0.02255 0.01002  -0.00207 156 SER A N   
419  C CA  . SER A 56  ? 0.25672 0.23802 0.30396 -0.02576 0.01116  -0.01188 156 SER A CA  
420  C C   . SER A 56  ? 0.25622 0.23782 0.29573 -0.02714 0.01152  -0.01909 156 SER A C   
421  O O   . SER A 56  ? 0.24980 0.23259 0.27765 -0.02906 0.00873  -0.02352 156 SER A O   
422  C CB  . SER A 56  ? 0.29779 0.28025 0.36739 -0.02735 0.01784  -0.01499 156 SER A CB  
423  O OG  . SER A 56  ? 0.33643 0.31885 0.42219 -0.02713 0.02462  -0.01694 156 SER A OG  
424  N N   . GLU A 57  ? 0.25860 0.23980 0.30504 -0.02582 0.01459  -0.01870 157 GLU A N   
425  C CA  . GLU A 57  ? 0.28460 0.26798 0.32756 -0.02707 0.01431  -0.02501 157 GLU A CA  
426  C C   . GLU A 57  ? 0.29335 0.27541 0.31868 -0.02591 0.00867  -0.02247 157 GLU A C   
427  O O   . GLU A 57  ? 0.27262 0.25863 0.29198 -0.02756 0.00581  -0.02638 157 GLU A O   
428  C CB  . GLU A 57  ? 0.26403 0.24634 0.32072 -0.02555 0.01960  -0.02451 157 GLU A CB  
429  C CG  . GLU A 57  ? 0.26584 0.24974 0.34564 -0.02732 0.02762  -0.02918 157 GLU A CG  
430  C CD  . GLU A 57  ? 0.32564 0.30596 0.41804 -0.02412 0.03154  -0.01898 157 GLU A CD  
431  O OE1 . GLU A 57  ? 0.33184 0.31050 0.41184 -0.02147 0.02632  -0.00917 157 GLU A OE1 
432  O OE2 . GLU A 57  ? 0.33863 0.31896 0.45506 -0.02458 0.04008  -0.02064 157 GLU A OE2 
433  N N   . LEU A 58  ? 0.25802 0.23547 0.27584 -0.02353 0.00761  -0.01572 158 LEU A N   
434  C CA  . LEU A 58  ? 0.22064 0.19588 0.22573 -0.02312 0.00478  -0.01477 158 LEU A CA  
435  C C   . LEU A 58  ? 0.25917 0.23543 0.25640 -0.02449 0.00147  -0.01596 158 LEU A C   
436  O O   . LEU A 58  ? 0.24377 0.22067 0.23654 -0.02445 -0.00004 -0.01647 158 LEU A O   
437  C CB  . LEU A 58  ? 0.23368 0.20453 0.23136 -0.02218 0.00584  -0.00980 158 LEU A CB  
438  C CG  . LEU A 58  ? 0.25375 0.22127 0.24147 -0.02276 0.00556  -0.01065 158 LEU A CG  
439  C CD1 . LEU A 58  ? 0.30032 0.26750 0.29401 -0.02165 0.00701  -0.01257 158 LEU A CD1 
440  C CD2 . LEU A 58  ? 0.29632 0.26086 0.27504 -0.02387 0.00785  -0.00824 158 LEU A CD2 
441  N N   . LEU A 59  ? 0.24149 0.21797 0.23897 -0.02541 0.00079  -0.01524 159 LEU A N   
442  C CA  . LEU A 59  ? 0.22224 0.19892 0.21393 -0.02682 -0.00098 -0.01669 159 LEU A CA  
443  C C   . LEU A 59  ? 0.26509 0.24590 0.25655 -0.02843 -0.00090 -0.02062 159 LEU A C   
444  O O   . LEU A 59  ? 0.27088 0.25213 0.25530 -0.02849 -0.00230 -0.01947 159 LEU A O   
445  C CB  . LEU A 59  ? 0.24499 0.22211 0.24141 -0.02772 -0.00116 -0.01581 159 LEU A CB  
446  C CG  . LEU A 59  ? 0.27929 0.25587 0.27184 -0.02732 -0.00365 -0.01142 159 LEU A CG  
447  C CD1 . LEU A 59  ? 0.27295 0.25267 0.27514 -0.02784 -0.00483 -0.00897 159 LEU A CD1 
448  C CD2 . LEU A 59  ? 0.23639 0.21047 0.21841 -0.02838 -0.00462 -0.01311 159 LEU A CD2 
449  N N   . ILE A 60  ? 0.26418 0.24907 0.26386 -0.03020 0.00123  -0.02510 160 ILE A N   
450  C CA  . ILE A 60  ? 0.26357 0.25552 0.26069 -0.03340 0.00084  -0.03018 160 ILE A CA  
451  C C   . ILE A 60  ? 0.31618 0.31197 0.30876 -0.03194 -0.00294 -0.02742 160 ILE A C   
452  O O   . ILE A 60  ? 0.31101 0.31174 0.29576 -0.03278 -0.00581 -0.02538 160 ILE A O   
453  C CB  . ILE A 60  ? 0.24446 0.24076 0.25358 -0.03694 0.00532  -0.03816 160 ILE A CB  
454  C CG1 . ILE A 60  ? 0.27259 0.26571 0.28944 -0.03871 0.01007  -0.04042 160 ILE A CG1 
455  C CG2 . ILE A 60  ? 0.27736 0.28426 0.28175 -0.04174 0.00410  -0.04500 160 ILE A CG2 
456  C CD1 . ILE A 60  ? 0.30555 0.30039 0.34115 -0.04147 0.01721  -0.04738 160 ILE A CD1 
457  N N   . ASN A 61  ? 0.27167 0.26564 0.27071 -0.02958 -0.00257 -0.02612 161 ASN A N   
458  C CA  . ASN A 61  ? 0.25425 0.25232 0.25385 -0.02812 -0.00559 -0.02345 161 ASN A CA  
459  C C   . ASN A 61  ? 0.30931 0.30385 0.30236 -0.02561 -0.00724 -0.01634 161 ASN A C   
460  O O   . ASN A 61  ? 0.30464 0.30544 0.29827 -0.02487 -0.01047 -0.01227 161 ASN A O   
461  C CB  . ASN A 61  ? 0.23717 0.23190 0.24663 -0.02610 -0.00295 -0.02371 161 ASN A CB  
462  C CG  . ASN A 61  ? 0.26287 0.26594 0.28320 -0.02863 -0.00247 -0.03046 161 ASN A CG  
463  O OD1 . ASN A 61  ? 0.27028 0.27392 0.29738 -0.03101 0.00142  -0.03627 161 ASN A OD1 
464  N ND2 . ASN A 61  ? 0.23909 0.24937 0.26412 -0.02838 -0.00590 -0.02995 161 ASN A ND2 
465  N N   . ILE A 62  ? 0.25629 0.24214 0.24507 -0.02459 -0.00487 -0.01456 162 ILE A N   
466  C CA  . ILE A 62  ? 0.23997 0.22169 0.22590 -0.02296 -0.00421 -0.00967 162 ILE A CA  
467  C C   . ILE A 62  ? 0.27718 0.26417 0.25869 -0.02363 -0.00629 -0.00644 162 ILE A C   
468  O O   . ILE A 62  ? 0.26207 0.25018 0.24608 -0.02162 -0.00649 0.00011  162 ILE A O   
469  C CB  . ILE A 62  ? 0.23112 0.20473 0.21333 -0.02340 -0.00129 -0.01091 162 ILE A CB  
470  C CG1 . ILE A 62  ? 0.24712 0.21643 0.23098 -0.02296 0.00128  -0.01192 162 ILE A CG1 
471  C CG2 . ILE A 62  ? 0.30526 0.27503 0.28647 -0.02303 0.00090  -0.00831 162 ILE A CG2 
472  C CD1 . ILE A 62  ? 0.23672 0.20225 0.21428 -0.02480 0.00248  -0.01345 162 ILE A CD1 
473  N N   . PHE A 63  ? 0.26383 0.25389 0.24006 -0.02649 -0.00675 -0.01018 163 PHE A N   
474  C CA  . PHE A 63  ? 0.27284 0.26618 0.24239 -0.02768 -0.00698 -0.00707 163 PHE A CA  
475  C C   . PHE A 63  ? 0.33985 0.34622 0.30479 -0.03004 -0.01086 -0.00601 163 PHE A C   
476  O O   . PHE A 63  ? 0.34867 0.35946 0.30540 -0.03179 -0.01087 -0.00288 163 PHE A O   
477  C CB  . PHE A 63  ? 0.25043 0.23956 0.21694 -0.03022 -0.00394 -0.01196 163 PHE A CB  
478  C CG  . PHE A 63  ? 0.26691 0.24667 0.23616 -0.02866 -0.00147 -0.01144 163 PHE A CG  
479  C CD1 . PHE A 63  ? 0.29970 0.27532 0.26921 -0.02696 0.00066  -0.00664 163 PHE A CD1 
480  C CD2 . PHE A 63  ? 0.27682 0.25335 0.24990 -0.02931 -0.00108 -0.01553 163 PHE A CD2 
481  C CE1 . PHE A 63  ? 0.26535 0.23395 0.23796 -0.02704 0.00333  -0.00874 163 PHE A CE1 
482  C CE2 . PHE A 63  ? 0.28419 0.25550 0.25849 -0.02909 -0.00017 -0.01565 163 PHE A CE2 
483  C CZ  . PHE A 63  ? 0.32081 0.28835 0.29435 -0.02852 0.00208  -0.01365 163 PHE A CZ  
484  N N   . ILE A 64  ? 0.27572 0.28941 0.24544 -0.03068 -0.01401 -0.00860 164 ILE A N   
485  C CA  . ILE A 64  ? 0.28597 0.31557 0.25077 -0.03417 -0.01896 -0.00851 164 ILE A CA  
486  C C   . ILE A 64  ? 0.28856 0.32410 0.24977 -0.03156 -0.02246 0.00460  164 ILE A C   
487  O O   . ILE A 64  ? 0.31175 0.34161 0.28245 -0.02627 -0.02202 0.01302  164 ILE A O   
488  C CB  . ILE A 64  ? 0.32859 0.36554 0.30305 -0.03482 -0.02201 -0.01296 164 ILE A CB  
489  C CG1 . ILE A 64  ? 0.30063 0.33227 0.28099 -0.03748 -0.01701 -0.02479 164 ILE A CG1 
490  C CG2 . ILE A 64  ? 0.31661 0.37371 0.28622 -0.03905 -0.02897 -0.01236 164 ILE A CG2 
491  C CD1 . ILE A 64  ? 0.35268 0.38872 0.32656 -0.04406 -0.01379 -0.03427 164 ILE A CD1 
492  N N   . PRO A 65  ? 0.33833 0.38534 0.28712 -0.03529 -0.02488 0.00733  165 PRO A N   
493  C CA  . PRO A 65  ? 0.32892 0.38208 0.27537 -0.03215 -0.02767 0.02297  165 PRO A CA  
494  C C   . PRO A 65  ? 0.30421 0.36792 0.26260 -0.02855 -0.03447 0.03271  165 PRO A C   
495  O O   . PRO A 65  ? 0.30873 0.38220 0.27126 -0.03095 -0.03937 0.02641  165 PRO A O   
496  C CB  . PRO A 65  ? 0.34143 0.40833 0.26927 -0.03865 -0.02948 0.02225  165 PRO A CB  
497  C CG  . PRO A 65  ? 0.43659 0.49797 0.35906 -0.04462 -0.02408 0.00520  165 PRO A CG  
498  C CD  . PRO A 65  ? 0.34829 0.40136 0.28531 -0.04280 -0.02304 -0.00374 165 PRO A CD  
499  N N   . ASN A 66  ? 0.33180 0.39339 0.29895 -0.02274 -0.03378 0.04829  166 ASN A N   
500  C CA  . ASN A 66  ? 0.40233 0.47507 0.38471 -0.01854 -0.03975 0.06157  166 ASN A CA  
501  C C   . ASN A 66  ? 0.37229 0.43774 0.37212 -0.01617 -0.03851 0.05495  166 ASN A C   
502  O O   . ASN A 66  ? 0.42460 0.50285 0.43518 -0.01566 -0.04513 0.05815  166 ASN A O   
503  C CB  . ASN A 66  ? 0.38593 0.48479 0.35827 -0.02287 -0.05080 0.06667  166 ASN A CB  
504  C CG  . ASN A 66  ? 0.48268 0.59561 0.46924 -0.01759 -0.05722 0.08824  166 ASN A CG  
505  O OD1 . ASN A 66  ? 0.64488 0.74833 0.64358 -0.01128 -0.05158 0.10212  166 ASN A OD1 
506  N ND2 . ASN A 66  ? 0.54428 0.68093 0.53189 -0.02035 -0.06874 0.09135  166 ASN A ND2 
507  N N   . THR A 67  ? 0.28172 0.32757 0.28411 -0.01520 -0.03002 0.04568  167 THR A N   
508  C CA  . THR A 67  ? 0.26439 0.30053 0.28077 -0.01324 -0.02636 0.03965  167 THR A CA  
509  C C   . THR A 67  ? 0.30469 0.32431 0.33234 -0.00926 -0.01710 0.04339  167 THR A C   
510  O O   . THR A 67  ? 0.31705 0.33042 0.34030 -0.00871 -0.01280 0.04691  167 THR A O   
511  C CB  . THR A 67  ? 0.30066 0.33040 0.30830 -0.01716 -0.02429 0.02389  167 THR A CB  
512  O OG1 . THR A 67  ? 0.27891 0.29738 0.27552 -0.01843 -0.01908 0.01935  167 THR A OG1 
513  C CG2 . THR A 67  ? 0.36523 0.41052 0.36546 -0.02217 -0.03092 0.01737  167 THR A CG2 
514  N N   . PRO A 68  ? 0.29935 0.31144 0.34239 -0.00724 -0.01256 0.04129  168 PRO A N   
515  C CA  . PRO A 68  ? 0.31746 0.31471 0.37234 -0.00502 -0.00211 0.04263  168 PRO A CA  
516  C C   . PRO A 68  ? 0.31594 0.30084 0.35756 -0.00775 0.00383  0.03371  168 PRO A C   
517  O O   . PRO A 68  ? 0.35173 0.32903 0.40018 -0.00678 0.01094  0.03675  168 PRO A O   
518  C CB  . PRO A 68  ? 0.28793 0.27990 0.35650 -0.00450 0.00198  0.03764  168 PRO A CB  
519  C CG  . PRO A 68  ? 0.33751 0.34558 0.41292 -0.00350 -0.00750 0.04273  168 PRO A CG  
520  C CD  . PRO A 68  ? 0.33415 0.35278 0.38833 -0.00696 -0.01602 0.03919  168 PRO A CD  
521  N N   . LEU A 69  ? 0.31570 0.29921 0.34146 -0.01119 0.00146  0.02322  169 LEU A N   
522  C CA  . LEU A 69  ? 0.27463 0.24814 0.29055 -0.01384 0.00614  0.01518  169 LEU A CA  
523  C C   . LEU A 69  ? 0.31285 0.28887 0.31689 -0.01538 0.00365  0.01536  169 LEU A C   
524  O O   . LEU A 69  ? 0.36412 0.33337 0.36231 -0.01757 0.00676  0.00920  169 LEU A O   
525  C CB  . LEU A 69  ? 0.26404 0.23417 0.27263 -0.01629 0.00602  0.00556  169 LEU A CB  
526  C CG  . LEU A 69  ? 0.27510 0.24025 0.29262 -0.01585 0.01075  0.00324  169 LEU A CG  
527  C CD1 . LEU A 69  ? 0.30665 0.26913 0.31508 -0.01816 0.01096  -0.00403 169 LEU A CD1 
528  C CD2 . LEU A 69  ? 0.31679 0.27297 0.34260 -0.01625 0.01972  0.00270  169 LEU A CD2 
529  N N   . HIS A 70  ? 0.33039 0.31682 0.33051 -0.01495 -0.00166 0.02189  170 HIS A N   
530  C CA  . HIS A 70  ? 0.33587 0.32399 0.32280 -0.01777 -0.00286 0.01890  170 HIS A CA  
531  C C   . HIS A 70  ? 0.36686 0.34850 0.35517 -0.01702 0.00280  0.02301  170 HIS A C   
532  O O   . HIS A 70  ? 0.39279 0.37147 0.37327 -0.01955 0.00428  0.01794  170 HIS A O   
533  C CB  . HIS A 70  ? 0.34656 0.34889 0.32526 -0.01957 -0.00938 0.02189  170 HIS A CB  
534  C CG  . HIS A 70  ? 0.45591 0.46603 0.43541 -0.01753 -0.01075 0.03532  170 HIS A CG  
535  N ND1 . HIS A 70  ? 0.49306 0.50585 0.48729 -0.01305 -0.01110 0.04683  170 HIS A ND1 
536  C CD2 . HIS A 70  ? 0.47428 0.49057 0.44276 -0.01930 -0.01126 0.04043  170 HIS A CD2 
537  C CE1 . HIS A 70  ? 0.54316 0.56431 0.53611 -0.01158 -0.01254 0.06013  170 HIS A CE1 
538  N NE2 . HIS A 70  ? 0.42868 0.45220 0.40423 -0.01555 -0.01269 0.05638  170 HIS A NE2 
539  N N   . ASP A 71  ? 0.39105 0.37024 0.39230 -0.01361 0.00704  0.03209  171 ASP A N   
540  C CA  . ASP A 71  ? 0.46847 0.44082 0.47503 -0.01283 0.01431  0.03593  171 ASP A CA  
541  C C   . ASP A 71  ? 0.44604 0.40629 0.45986 -0.01453 0.02168  0.02585  171 ASP A C   
542  O O   . ASP A 71  ? 0.49960 0.45625 0.52144 -0.01442 0.02404  0.02222  171 ASP A O   
543  C CB  . ASP A 71  ? 0.50398 0.47987 0.52498 -0.00826 0.01693  0.05191  171 ASP A CB  
544  C CG  . ASP A 71  ? 0.53968 0.52804 0.54996 -0.00776 0.01136  0.06337  171 ASP A CG  
545  O OD1 . ASP A 71  ? 0.54542 0.53490 0.53922 -0.01133 0.01016  0.05794  171 ASP A OD1 
546  O OD2 . ASP A 71  ? 0.57540 0.57338 0.59431 -0.00417 0.00839  0.07816  171 ASP A OD2 
547  N N   . GLY A 72  ? 0.40364 0.35864 0.41462 -0.01683 0.02558  0.02070  172 GLY A N   
548  C CA  . GLY A 72  ? 0.40479 0.35161 0.42060 -0.02000 0.03123  0.00962  172 GLY A CA  
549  C C   . GLY A 72  ? 0.28686 0.23541 0.28943 -0.02371 0.02543  -0.00062 172 GLY A C   
550  O O   . GLY A 72  ? 0.32316 0.27737 0.31542 -0.02372 0.01873  0.00004  172 GLY A O   
551  N N   . ALA A 73  ? 0.25894 0.20353 0.26354 -0.02737 0.02860  -0.01019 173 ALA A N   
552  C CA  . ALA A 73  ? 0.28909 0.23674 0.28419 -0.03076 0.02310  -0.01774 173 ALA A CA  
553  C C   . ALA A 73  ? 0.28928 0.23914 0.27814 -0.03185 0.01953  -0.02098 173 ALA A C   
554  O O   . ALA A 73  ? 0.30267 0.24944 0.29534 -0.03273 0.02420  -0.02330 173 ALA A O   
555  C CB  . ALA A 73  ? 0.27363 0.21919 0.27359 -0.03504 0.02702  -0.02600 173 ALA A CB  
556  N N   . VAL A 74  ? 0.25295 0.20765 0.23400 -0.03205 0.01273  -0.02117 174 VAL A N   
557  C CA  . VAL A 74  ? 0.25688 0.21418 0.23188 -0.03393 0.00978  -0.02425 174 VAL A CA  
558  C C   . VAL A 74  ? 0.27363 0.23371 0.24652 -0.03865 0.00887  -0.03054 174 VAL A C   
559  O O   . VAL A 74  ? 0.30322 0.26533 0.27920 -0.03944 0.00691  -0.03134 174 VAL A O   
560  C CB  . VAL A 74  ? 0.25888 0.22050 0.23073 -0.03188 0.00413  -0.02059 174 VAL A CB  
561  C CG1 . VAL A 74  ? 0.31905 0.28393 0.28584 -0.03349 0.00140  -0.02143 174 VAL A CG1 
562  C CG2 . VAL A 74  ? 0.30163 0.26294 0.27559 -0.02855 0.00458  -0.01633 174 VAL A CG2 
563  N N   . ILE A 75  ? 0.27146 0.23258 0.23945 -0.04253 0.01064  -0.03565 175 ILE A N   
564  C CA  . ILE A 75  ? 0.27982 0.24761 0.24344 -0.04829 0.00797  -0.04191 175 ILE A CA  
565  C C   . ILE A 75  ? 0.31253 0.28760 0.26522 -0.04955 0.00211  -0.03909 175 ILE A C   
566  O O   . ILE A 75  ? 0.30869 0.28149 0.25532 -0.04985 0.00527  -0.03901 175 ILE A O   
567  C CB  . ILE A 75  ? 0.24866 0.21398 0.21490 -0.05407 0.01599  -0.05220 175 ILE A CB  
568  C CG1 . ILE A 75  ? 0.26271 0.22062 0.24331 -0.05197 0.02278  -0.05261 175 ILE A CG1 
569  C CG2 . ILE A 75  ? 0.26892 0.24479 0.22885 -0.06141 0.01165  -0.05980 175 ILE A CG2 
570  C CD1 . ILE A 75  ? 0.29021 0.24314 0.28020 -0.05686 0.03420  -0.06241 175 ILE A CD1 
571  N N   . MET A 76  ? 0.27331 0.25726 0.22543 -0.05015 -0.00575 -0.03581 176 MET A N   
572  C CA  . MET A 76  ? 0.31279 0.30572 0.25680 -0.05095 -0.01191 -0.03012 176 MET A CA  
573  C C   . MET A 76  ? 0.36684 0.37132 0.30211 -0.05855 -0.01566 -0.03555 176 MET A C   
574  O O   . MET A 76  ? 0.34328 0.35179 0.28419 -0.06198 -0.01719 -0.04154 176 MET A O   
575  C CB  . MET A 76  ? 0.29078 0.28766 0.24422 -0.04637 -0.01794 -0.02091 176 MET A CB  
576  C CG  . MET A 76  ? 0.39154 0.38022 0.35128 -0.04054 -0.01457 -0.01661 176 MET A CG  
577  S SD  . MET A 76  ? 0.49482 0.48806 0.46869 -0.03667 -0.01868 -0.00793 176 MET A SD  
578  C CE  . MET A 76  ? 0.34613 0.35357 0.31791 -0.03933 -0.02673 -0.00106 176 MET A CE  
579  N N   . LYS A 77  ? 0.33093 0.34158 0.25211 -0.06179 -0.01681 -0.03386 177 LYS A N   
580  C CA  . LYS A 77  ? 0.35643 0.38139 0.26468 -0.07047 -0.02109 -0.03884 177 LYS A CA  
581  C C   . LYS A 77  ? 0.43556 0.46990 0.33127 -0.07017 -0.02629 -0.02757 177 LYS A C   
582  O O   . LYS A 77  ? 0.43512 0.46089 0.32722 -0.06660 -0.02075 -0.02337 177 LYS A O   
583  C CB  . LYS A 77  ? 0.42787 0.44819 0.32859 -0.07813 -0.01115 -0.05424 177 LYS A CB  
584  C CG  . LYS A 77  ? 0.58202 0.61744 0.46508 -0.08935 -0.01323 -0.06254 177 LYS A CG  
585  C CD  . LYS A 77  ? 0.54090 0.56761 0.41983 -0.09642 0.00078  -0.07853 177 LYS A CD  
586  C CE  . LYS A 77  ? 0.63645 0.67820 0.50094 -0.11026 0.00107  -0.09316 177 LYS A CE  
587  N NZ  . LYS A 77  ? 0.74054 0.77673 0.61981 -0.11578 0.01050  -0.11044 177 LYS A NZ  
588  N N   . ASN A 78  ? 0.44397 0.49657 0.33474 -0.07370 -0.03683 -0.02162 178 ASN A N   
589  C CA  . ASN A 78  ? 0.48768 0.55218 0.36511 -0.07426 -0.04207 -0.00896 178 ASN A CA  
590  C C   . ASN A 78  ? 0.46095 0.51666 0.34938 -0.06419 -0.04028 0.00574  178 ASN A C   
591  O O   . ASN A 78  ? 0.46786 0.52302 0.34580 -0.06345 -0.03713 0.01268  178 ASN A O   
592  C CB  . ASN A 78  ? 0.52251 0.58846 0.37589 -0.08267 -0.03553 -0.01770 178 ASN A CB  
593  C CG  . ASN A 78  ? 0.59147 0.66923 0.43333 -0.09470 -0.03666 -0.03364 178 ASN A CG  
594  O OD1 . ASN A 78  ? 0.55028 0.64445 0.39515 -0.09804 -0.04732 -0.03263 178 ASN A OD1 
595  N ND2 . ASN A 78  ? 0.76930 0.83904 0.60056 -0.10173 -0.02482 -0.04932 178 ASN A ND2 
596  N N   . ASN A 79  ? 0.42054 0.46900 0.33078 -0.05712 -0.04085 0.00925  179 ASN A N   
597  C CA  . ASN A 79  ? 0.37875 0.42002 0.30358 -0.04862 -0.03847 0.02086  179 ASN A CA  
598  C C   . ASN A 79  ? 0.42923 0.45464 0.35096 -0.04599 -0.02812 0.01608  179 ASN A C   
599  O O   . ASN A 79  ? 0.52321 0.54467 0.45166 -0.04096 -0.02498 0.02478  179 ASN A O   
600  C CB  . ASN A 79  ? 0.51454 0.56919 0.43975 -0.04679 -0.04442 0.03852  179 ASN A CB  
601  C CG  . ASN A 79  ? 0.62073 0.67502 0.57289 -0.03929 -0.04583 0.05054  179 ASN A CG  
602  O OD1 . ASN A 79  ? 0.64059 0.69442 0.60882 -0.03817 -0.04809 0.04733  179 ASN A OD1 
603  N ND2 . ASN A 79  ? 0.67651 0.73060 0.63567 -0.03447 -0.04297 0.06408  179 ASN A ND2 
604  N N   . GLU A 80  ? 0.37681 0.39364 0.29129 -0.04938 -0.02224 0.00264  180 GLU A N   
605  C CA  . GLU A 80  ? 0.33928 0.34210 0.25527 -0.04661 -0.01319 -0.00168 180 GLU A CA  
606  C C   . GLU A 80  ? 0.35331 0.34704 0.27774 -0.04590 -0.00973 -0.01124 180 GLU A C   
607  O O   . GLU A 80  ? 0.32215 0.31890 0.24778 -0.04896 -0.01212 -0.01692 180 GLU A O   
608  C CB  . GLU A 80  ? 0.43578 0.43720 0.33492 -0.05158 -0.00698 -0.00607 180 GLU A CB  
609  C CG  . GLU A 80  ? 0.49690 0.50396 0.38828 -0.05067 -0.00753 0.00550  180 GLU A CG  
610  C CD  . GLU A 80  ? 0.68771 0.69045 0.56361 -0.05531 0.00130  0.00036  180 GLU A CD  
611  O OE1 . GLU A 80  ? 0.58988 0.58677 0.46151 -0.06020 0.00755  -0.01298 180 GLU A OE1 
612  O OE2 . GLU A 80  ? 0.77907 0.78379 0.64914 -0.05406 0.00326  0.00991  180 GLU A OE2 
613  N N   . ILE A 81  ? 0.28162 0.26513 0.21311 -0.04180 -0.00409 -0.01216 181 ILE A N   
614  C CA  . ILE A 81  ? 0.29042 0.26627 0.22881 -0.04100 -0.00028 -0.01885 181 ILE A CA  
615  C C   . ILE A 81  ? 0.31998 0.29131 0.25193 -0.04543 0.00705  -0.02679 181 ILE A C   
616  O O   . ILE A 81  ? 0.31653 0.28303 0.24721 -0.04484 0.01254  -0.02666 181 ILE A O   
617  C CB  . ILE A 81  ? 0.29147 0.26172 0.24074 -0.03536 0.00130  -0.01572 181 ILE A CB  
618  C CG1 . ILE A 81  ? 0.33176 0.30600 0.28943 -0.03250 -0.00361 -0.01085 181 ILE A CG1 
619  C CG2 . ILE A 81  ? 0.27871 0.24283 0.23355 -0.03461 0.00529  -0.02004 181 ILE A CG2 
620  C CD1 . ILE A 81  ? 0.33719 0.30913 0.30418 -0.02863 -0.00190 -0.00855 181 ILE A CD1 
621  N N   . ALA A 82  ? 0.29207 0.26492 0.22205 -0.05047 0.00841  -0.03460 182 ALA A N   
622  C CA  . ALA A 82  ? 0.26875 0.23764 0.19477 -0.05623 0.01744  -0.04423 182 ALA A CA  
623  C C   . ALA A 82  ? 0.31803 0.27566 0.25821 -0.05246 0.02567  -0.04519 182 ALA A C   
624  O O   . ALA A 82  ? 0.33224 0.28439 0.27333 -0.05355 0.03349  -0.04775 182 ALA A O   
625  C CB  . ALA A 82  ? 0.34619 0.32054 0.26941 -0.06355 0.01783  -0.05410 182 ALA A CB  
626  N N   . ALA A 83  ? 0.29193 0.24682 0.24403 -0.04814 0.02424  -0.04231 183 ALA A N   
627  C CA  . ALA A 83  ? 0.28930 0.23630 0.25619 -0.04439 0.03081  -0.04062 183 ALA A CA  
628  C C   . ALA A 83  ? 0.31188 0.25980 0.28580 -0.03855 0.02523  -0.03285 183 ALA A C   
629  O O   . ALA A 83  ? 0.30048 0.25295 0.27008 -0.03852 0.01897  -0.03172 183 ALA A O   
630  C CB  . ALA A 83  ? 0.30665 0.24861 0.28238 -0.04902 0.04122  -0.04931 183 ALA A CB  
631  N N   . ALA A 84  ? 0.30822 0.30440 0.28717 -0.04200 0.00540  -0.07431 184 ALA A N   
632  C CA  . ALA A 84  ? 0.23447 0.25938 0.20592 -0.03990 -0.00907 -0.04614 184 ALA A CA  
633  C C   . ALA A 84  ? 0.23026 0.26742 0.26180 -0.03136 0.00076  -0.01332 184 ALA A C   
634  O O   . ALA A 84  ? 0.29518 0.32035 0.37518 -0.02623 0.01828  -0.01110 184 ALA A O   
635  C CB  . ALA A 84  ? 0.26369 0.31399 0.20614 -0.04441 -0.02812 -0.03750 184 ALA A CB  
636  N N   . ALA A 85  ? 0.22086 0.28211 0.24964 -0.03041 -0.00974 0.01266  185 ALA A N   
637  C CA  . ALA A 85  ? 0.24808 0.32635 0.33244 -0.02278 -0.00344 0.04911  185 ALA A CA  
638  C C   . ALA A 85  ? 0.29978 0.34862 0.42419 -0.01696 0.02022  0.04161  185 ALA A C   
639  O O   . ALA A 85  ? 0.27309 0.32300 0.45773 -0.00902 0.03466  0.06319  185 ALA A O   
640  C CB  . ALA A 85  ? 0.24738 0.35063 0.37243 -0.01894 -0.00559 0.07694  185 ALA A CB  
641  N N   . CYS A 86  ? 0.22230 0.24540 0.31405 -0.02165 0.02490  0.01194  186 CYS A N   
642  C CA  . CYS A 86  ? 0.26591 0.25964 0.38654 -0.02002 0.04720  0.00026  186 CYS A CA  
643  C C   . CYS A 86  ? 0.31332 0.31589 0.45245 -0.01610 0.04869  0.02370  186 CYS A C   
644  O O   . CYS A 86  ? 0.26478 0.28972 0.37469 -0.01777 0.03136  0.03676  186 CYS A O   
645  C CB  . CYS A 86  ? 0.30132 0.26751 0.37834 -0.02903 0.05041  -0.03974 186 CYS A CB  
646  S SG  . CYS A 86  ? 0.29930 0.25138 0.35141 -0.03581 0.04992  -0.07119 186 CYS A SG  
647  N N   . TYR A 87  ? 0.28729 0.27031 0.47395 -0.01204 0.07101  0.02718  187 TYR A N   
648  C CA  . TYR A 87  ? 0.26726 0.25266 0.47166 -0.00924 0.07540  0.04508  187 TYR A CA  
649  C C   . TYR A 87  ? 0.31014 0.27275 0.47592 -0.01736 0.07887  0.01519  187 TYR A C   
650  O O   . TYR A 87  ? 0.32996 0.26594 0.48096 -0.02430 0.08939  -0.01736 187 TYR A O   
651  C CB  . TYR A 87  ? 0.32699 0.30085 0.60299 -0.00125 0.09950  0.06404  187 TYR A CB  
652  C CG  . TYR A 87  ? 0.50475 0.50801 0.82688 0.00813  0.09507  0.10308  187 TYR A CG  
653  C CD1 . TYR A 87  ? 0.53043 0.53505 0.86890 0.01034  0.09797  0.10050  187 TYR A CD1 
654  C CD2 . TYR A 87  ? 0.63474 0.66721 0.98431 0.01383  0.08716  0.14418  187 TYR A CD2 
655  C CE1 . TYR A 87  ? 0.59319 0.62818 0.97598 0.01847  0.09334  0.13871  187 TYR A CE1 
656  C CE2 . TYR A 87  ? 0.63830 0.70217 1.03195 0.02109  0.08194  0.18337  187 TYR A CE2 
657  C CZ  . TYR A 87  ? 0.61694 0.68237 1.02772 0.02360  0.08506  0.18088  187 TYR A CZ  
658  O OH  . TYR A 87  ? 0.69964 0.79952 1.15610 0.03038  0.07932  0.22211  187 TYR A OH  
659  N N   . LEU A 88  ? 0.26578 0.24136 0.41523 -0.01758 0.06953  0.02751  188 LEU A N   
660  C CA  . LEU A 88  ? 0.26435 0.22244 0.38545 -0.02426 0.07354  0.00602  188 LEU A CA  
661  C C   . LEU A 88  ? 0.34034 0.29894 0.49631 -0.02047 0.08333  0.02806  188 LEU A C   
662  O O   . LEU A 88  ? 0.36383 0.34494 0.55149 -0.01312 0.07902  0.06258  188 LEU A O   
663  C CB  . LEU A 88  ? 0.29517 0.26839 0.35501 -0.02896 0.05197  -0.00356 188 LEU A CB  
664  C CG  . LEU A 88  ? 0.29991 0.27194 0.31862 -0.03347 0.04114  -0.02662 188 LEU A CG  
665  C CD1 . LEU A 88  ? 0.29541 0.28199 0.26037 -0.03684 0.02294  -0.03163 188 LEU A CD1 
666  C CD2 . LEU A 88  ? 0.31484 0.25679 0.32838 -0.04040 0.05471  -0.05976 188 LEU A CD2 
667  N N   . PRO A 89  ? 0.38117 0.31665 0.53335 -0.02636 0.09654  0.01026  189 PRO A N   
668  C CA  . PRO A 89  ? 0.38480 0.31972 0.56869 -0.02344 0.10613  0.03066  189 PRO A CA  
669  C C   . PRO A 89  ? 0.36443 0.32772 0.51957 -0.02240 0.08585  0.04875  189 PRO A C   
670  O O   . PRO A 89  ? 0.35771 0.32739 0.46120 -0.02763 0.07160  0.03241  189 PRO A O   
671  C CB  . PRO A 89  ? 0.40555 0.30749 0.58421 -0.03349 0.12501  0.00119  189 PRO A CB  
672  C CG  . PRO A 89  ? 0.41356 0.31156 0.53816 -0.04234 0.11438  -0.03031 189 PRO A CG  
673  C CD  . PRO A 89  ? 0.34380 0.25474 0.46245 -0.03746 0.10279  -0.02783 189 PRO A CD  
674  N N   . LEU A 90  ? 0.32739 0.30840 0.51780 -0.01592 0.08536  0.08365  190 LEU A N   
675  C CA  . LEU A 90  ? 0.32530 0.33419 0.49097 -0.01655 0.06770  0.10239  190 LEU A CA  
676  C C   . LEU A 90  ? 0.36380 0.35869 0.51736 -0.02137 0.07494  0.09133  190 LEU A C   
677  O O   . LEU A 90  ? 0.38392 0.35962 0.57540 -0.02062 0.09383  0.09468  190 LEU A O   
678  C CB  . LEU A 90  ? 0.36959 0.40648 0.57747 -0.00975 0.06313  0.14636  190 LEU A CB  
679  C CG  . LEU A 90  ? 0.43268 0.49144 0.65376 -0.00601 0.05332  0.16380  190 LEU A CG  
680  C CD1 . LEU A 90  ? 0.47727 0.57128 0.73361 -0.00208 0.04489  0.21063  190 LEU A CD1 
681  C CD2 . LEU A 90  ? 0.40531 0.47579 0.56549 -0.01238 0.03421  0.14447  190 LEU A CD2 
682  N N   . SER A 91  ? 0.35155 0.35598 0.45357 -0.02660 0.06104  0.07868  191 SER A N   
683  C CA  . SER A 91  ? 0.36900 0.36580 0.45900 -0.03112 0.06577  0.07187  191 SER A CA  
684  C C   . SER A 91  ? 0.38324 0.39257 0.50961 -0.02724 0.06899  0.10487  191 SER A C   
685  O O   . SER A 91  ? 0.35048 0.38697 0.49050 -0.02286 0.05815  0.13492  191 SER A O   
686  C CB  . SER A 91  ? 0.34124 0.35200 0.37459 -0.03548 0.04951  0.05939  191 SER A CB  
687  O OG  . SER A 91  ? 0.39261 0.40130 0.41865 -0.03902 0.05315  0.05859  191 SER A OG  
688  N N   . GLU A 92  ? 0.33624 0.32696 0.47808 -0.03027 0.08378  0.10008  192 GLU A N   
689  C CA  . GLU A 92  ? 0.36064 0.36237 0.53089 -0.02785 0.08637  0.12914  192 GLU A CA  
690  C C   . GLU A 92  ? 0.36863 0.38294 0.50027 -0.03314 0.07630  0.12616  192 GLU A C   
691  O O   . GLU A 92  ? 0.34790 0.36782 0.49819 -0.03314 0.07983  0.14526  192 GLU A O   
692  C CB  . GLU A 92  ? 0.50311 0.47519 0.72249 -0.02767 0.11189  0.12930  192 GLU A CB  
693  C CG  . GLU A 92  ? 0.58866 0.56083 0.86637 -0.01851 0.12157  0.15495  192 GLU A CG  
694  C CD  . GLU A 92  ? 0.84251 0.77630 1.15402 -0.01974 0.14843  0.13558  192 GLU A CD  
695  O OE1 . GLU A 92  ? 0.87688 0.78544 1.17501 -0.02762 0.16110  0.10843  192 GLU A OE1 
696  O OE2 . GLU A 92  ? 0.93442 0.86794 1.27839 -0.01141 0.15319  0.14310  192 GLU A OE2 
697  N N   . SER A 93  ? 0.33665 0.35566 0.41713 -0.03730 0.06465  0.10367  193 SER A N   
698  C CA  . SER A 93  ? 0.34469 0.37507 0.38868 -0.04181 0.05661  0.09904  193 SER A CA  
699  C C   . SER A 93  ? 0.36311 0.42428 0.40992 -0.03999 0.04517  0.13101  193 SER A C   
700  O O   . SER A 93  ? 0.43671 0.51962 0.48390 -0.03758 0.03369  0.14877  193 SER A O   
701  C CB  . SER A 93  ? 0.39566 0.42913 0.38876 -0.04459 0.04564  0.07415  193 SER A CB  
702  O OG  . SER A 93  ? 0.40159 0.44747 0.36244 -0.04783 0.03901  0.07156  193 SER A OG  
703  N N   . PRO A 94  ? 0.42793 0.49378 0.47515 -0.04275 0.04739  0.13949  194 PRO A N   
704  C CA  . PRO A 94  ? 0.42388 0.52138 0.46648 -0.04339 0.03526  0.16779  194 PRO A CA  
705  C C   . PRO A 94  ? 0.44551 0.56227 0.43440 -0.04766 0.02101  0.15774  194 PRO A C   
706  O O   . PRO A 94  ? 0.45807 0.60132 0.43691 -0.05088 0.01168  0.17802  194 PRO A O   
707  C CB  . PRO A 94  ? 0.41444 0.50575 0.47941 -0.04517 0.04542  0.17803  194 PRO A CB  
708  C CG  . PRO A 94  ? 0.36252 0.42529 0.41347 -0.04894 0.05701  0.14514  194 PRO A CG  
709  C CD  . PRO A 94  ? 0.36609 0.40983 0.41709 -0.04724 0.06112  0.12385  194 PRO A CD  
710  N N   . PHE A 95  ? 0.39666 0.50105 0.35179 -0.04849 0.02005  0.12771  195 PHE A N   
711  C CA  . PHE A 95  ? 0.50918 0.62758 0.41561 -0.05181 0.01000  0.11605  195 PHE A CA  
712  C C   . PHE A 95  ? 0.61050 0.73742 0.49467 -0.05187 0.00012  0.11124  195 PHE A C   
713  O O   . PHE A 95  ? 0.70867 0.82603 0.56955 -0.04878 -0.00445 0.08445  195 PHE A O   
714  C CB  . PHE A 95  ? 0.47074 0.57175 0.35432 -0.05310 0.01613  0.08773  195 PHE A CB  
715  C CG  . PHE A 95  ? 0.38620 0.47994 0.28704 -0.05520 0.02555  0.09069  195 PHE A CG  
716  C CD1 . PHE A 95  ? 0.36491 0.47692 0.25775 -0.05762 0.02261  0.10502  195 PHE A CD1 
717  C CD2 . PHE A 95  ? 0.31269 0.38143 0.23708 -0.05644 0.03814  0.07891  195 PHE A CD2 
718  C CE1 . PHE A 95  ? 0.41918 0.52501 0.32763 -0.06016 0.03111  0.10820  195 PHE A CE1 
719  C CE2 . PHE A 95  ? 0.34609 0.40797 0.28495 -0.06037 0.04742  0.08133  195 PHE A CE2 
720  C CZ  . PHE A 95  ? 0.29604 0.37661 0.22745 -0.06168 0.04347  0.09647  195 PHE A CZ  
721  N N   . ILE A 96  ? 0.50210 0.63271 0.41284 -0.04953 -0.00198 0.12600  196 ILE A N   
722  C CA  . ILE A 96  ? 0.50040 0.63957 0.39461 -0.04996 -0.01204 0.12135  196 ILE A CA  
723  C C   . ILE A 96  ? 0.48252 0.64471 0.38668 -0.05207 -0.02167 0.13654  196 ILE A C   
724  O O   . ILE A 96  ? 0.50383 0.68339 0.44021 -0.05264 -0.02264 0.16710  196 ILE A O   
725  C CB  . ILE A 96  ? 0.48714 0.61553 0.40761 -0.04613 -0.00830 0.12322  196 ILE A CB  
726  C CG1 . ILE A 96  ? 0.46259 0.55779 0.38669 -0.04327 0.00394  0.09411  196 ILE A CG1 
727  C CG2 . ILE A 96  ? 0.52644 0.66648 0.42378 -0.04843 -0.01943 0.11948  196 ILE A CG2 
728  C CD1 . ILE A 96  ? 0.45171 0.53187 0.40253 -0.03957 0.00955  0.08942  196 ILE A CD1 
729  N N   . SER A 97  ? 0.48967 0.64910 0.37135 -0.05341 -0.02623 0.11577  197 SER A N   
730  C CA  . SER A 97  ? 0.54436 0.72478 0.42999 -0.05933 -0.03247 0.12674  197 SER A CA  
731  C C   . SER A 97  ? 0.59261 0.79512 0.50055 -0.06287 -0.03912 0.14892  197 SER A C   
732  O O   . SER A 97  ? 0.49325 0.68905 0.40132 -0.06055 -0.03987 0.14414  197 SER A O   
733  C CB  . SER A 97  ? 0.60056 0.76643 0.46005 -0.05956 -0.03174 0.10124  197 SER A CB  
734  O OG  . SER A 97  ? 0.56343 0.75049 0.42443 -0.06809 -0.03684 0.11173  197 SER A OG  
735  N N   . LYS A 98  ? 0.39332 0.62375 0.32239 -0.06877 -0.04412 0.17390  198 LYS A N   
736  C CA  . LYS A 98  ? 0.50548 0.76111 0.45915 -0.07321 -0.05092 0.19597  198 LYS A CA  
737  C C   . LYS A 98  ? 0.43397 0.69274 0.36477 -0.08108 -0.05497 0.18027  198 LYS A C   
738  O O   . LYS A 98  ? 0.49747 0.77892 0.44513 -0.08698 -0.06081 0.19664  198 LYS A O   
739  C CB  . LYS A 98  ? 0.51899 0.80532 0.50688 -0.07746 -0.05490 0.22850  198 LYS A CB  
740  C CG  . LYS A 98  ? 0.54993 0.83009 0.57073 -0.06808 -0.04865 0.24822  198 LYS A CG  
741  C CD  . LYS A 98  ? 0.74650 1.00271 0.77985 -0.05780 -0.04121 0.24704  198 LYS A CD  
742  C CE  . LYS A 98  ? 0.54811 0.81949 0.62821 -0.05388 -0.04238 0.27424  198 LYS A CE  
743  N NZ  . LYS A 98  ? 0.68789 0.96339 0.82214 -0.04673 -0.03544 0.30360  198 LYS A NZ  
744  N N   . GLU A 99  ? 0.51678 0.75246 0.41379 -0.08068 -0.05086 0.15078  199 GLU A N   
745  C CA  . GLU A 99  ? 0.61769 0.84519 0.49530 -0.08426 -0.05145 0.13358  199 GLU A CA  
746  C C   . GLU A 99  ? 0.53230 0.74584 0.41080 -0.07823 -0.05107 0.12578  199 GLU A C   
747  O O   . GLU A 99  ? 0.53606 0.75145 0.40871 -0.08236 -0.05335 0.12109  199 GLU A O   
748  C CB  . GLU A 99  ? 0.59875 0.80649 0.45020 -0.08377 -0.04568 0.10850  199 GLU A CB  
749  C CG  . GLU A 99  ? 0.69930 0.92703 0.54612 -0.09478 -0.04677 0.11472  199 GLU A CG  
750  C CD  . GLU A 99  ? 0.79693 1.01058 0.62274 -0.09582 -0.04052 0.09320  199 GLU A CD  
751  O OE1 . GLU A 99  ? 0.77456 0.96456 0.59214 -0.08803 -0.03584 0.07495  199 GLU A OE1 
752  O OE2 . GLU A 99  ? 0.81575 1.04255 0.63508 -0.10443 -0.04019 0.09566  199 GLU A OE2 
753  N N   . LEU A 100 ? 0.38836 0.58853 0.27361 -0.06953 -0.04793 0.12455  200 LEU A N   
754  C CA  . LEU A 100 ? 0.47523 0.65875 0.35776 -0.06373 -0.04664 0.11339  200 LEU A CA  
755  C C   . LEU A 100 ? 0.49280 0.69918 0.40634 -0.06467 -0.05125 0.14140  200 LEU A C   
756  O O   . LEU A 100 ? 0.53167 0.76080 0.47532 -0.06572 -0.05330 0.17078  200 LEU A O   
757  C CB  . LEU A 100 ? 0.46061 0.61622 0.33190 -0.05514 -0.03980 0.09478  200 LEU A CB  
758  C CG  . LEU A 100 ? 0.55010 0.68130 0.39887 -0.05104 -0.03492 0.06972  200 LEU A CG  
759  C CD1 . LEU A 100 ? 0.51170 0.62220 0.35538 -0.04416 -0.02875 0.05654  200 LEU A CD1 
760  C CD2 . LEU A 100 ? 0.61893 0.74283 0.45744 -0.05266 -0.03493 0.05411  200 LEU A CD2 
761  N N   . GLY A 101 ? 0.45877 0.65673 0.36969 -0.06246 -0.05192 0.13333  201 GLY A N   
762  C CA  . GLY A 101 ? 0.52483 0.74295 0.46792 -0.06208 -0.05577 0.15978  201 GLY A CA  
763  C C   . GLY A 101 ? 0.43041 0.63553 0.39091 -0.05287 -0.05057 0.16792  201 GLY A C   
764  O O   . GLY A 101 ? 0.36550 0.54842 0.30927 -0.04931 -0.04418 0.15262  201 GLY A O   
765  N N   . THR A 102 ? 0.42148 0.38445 0.37567 -0.01739 0.03183  0.04899  202 THR A N   
766  C CA  . THR A 102 ? 0.43648 0.38682 0.39479 -0.02250 0.03211  0.04889  202 THR A CA  
767  C C   . THR A 102 ? 0.42125 0.37395 0.38730 -0.02437 0.02644  0.04083  202 THR A C   
768  O O   . THR A 102 ? 0.39134 0.33811 0.36268 -0.03023 0.02748  0.03909  202 THR A O   
769  C CB  . THR A 102 ? 0.46946 0.40817 0.42208 -0.01854 0.03131  0.05331  202 THR A CB  
770  O OG1 . THR A 102 ? 0.56471 0.50215 0.50921 -0.01567 0.03633  0.06074  202 THR A OG1 
771  C CG2 . THR A 102 ? 0.56377 0.48862 0.51958 -0.02376 0.03261  0.05421  202 THR A CG2 
772  N N   . ARG A 103 ? 0.38455 0.34555 0.35139 -0.01915 0.02039  0.03578  203 ARG A N   
773  C CA  . ARG A 103 ? 0.37104 0.33473 0.34511 -0.02045 0.01536  0.02832  203 ARG A CA  
774  C C   . ARG A 103 ? 0.33748 0.30705 0.31721 -0.02668 0.01764  0.02505  203 ARG A C   
775  O O   . ARG A 103 ? 0.31761 0.28289 0.30281 -0.03069 0.01648  0.02139  203 ARG A O   
776  C CB  . ARG A 103 ? 0.42596 0.39943 0.40060 -0.01407 0.00918  0.02347  203 ARG A CB  
777  C CG  . ARG A 103 ? 0.43361 0.40078 0.40685 -0.00854 0.00483  0.02380  203 ARG A CG  
778  C CD  . ARG A 103 ? 0.35510 0.33272 0.33058 -0.00273 -0.00134 0.01829  203 ARG A CD  
779  N NE  . ARG A 103 ? 0.40324 0.37513 0.37903 0.00228  -0.00551 0.01830  203 ARG A NE  
780  C CZ  . ARG A 103 ? 0.48808 0.46081 0.45888 0.00808  -0.00678 0.02099  203 ARG A CZ  
781  N NH1 . ARG A 103 ? 0.47735 0.45669 0.44181 0.01022  -0.00443 0.02372  203 ARG A NH1 
782  N NH2 . ARG A 103 ? 0.59371 0.56058 0.56597 0.01208  -0.01042 0.02094  203 ARG A NH2 
783  N N   . HIS A 104 ? 0.32269 0.30223 0.30116 -0.02724 0.02092  0.02628  204 HIS A N   
784  C CA  . HIS A 104 ? 0.34127 0.32765 0.32581 -0.03304 0.02314  0.02305  204 HIS A CA  
785  C C   . HIS A 104 ? 0.29819 0.27501 0.28557 -0.04018 0.02846  0.02625  204 HIS A C   
786  O O   . HIS A 104 ? 0.29836 0.27586 0.29267 -0.04538 0.02820  0.02185  204 HIS A O   
787  C CB  . HIS A 104 ? 0.31830 0.31778 0.30070 -0.03144 0.02576  0.02412  204 HIS A CB  
788  C CG  . HIS A 104 ? 0.32099 0.33099 0.30142 -0.02466 0.02018  0.01992  204 HIS A CG  
789  N ND1 . HIS A 104 ? 0.34169 0.35233 0.31495 -0.01763 0.01863  0.02283  204 HIS A ND1 
790  C CD2 . HIS A 104 ? 0.27354 0.29360 0.25848 -0.02362 0.01552  0.01274  204 HIS A CD2 
791  C CE1 . HIS A 104 ? 0.36776 0.38848 0.34165 -0.01270 0.01313  0.01740  204 HIS A CE1 
792  N NE2 . HIS A 104 ? 0.28794 0.31433 0.26879 -0.01625 0.01128  0.01138  204 HIS A NE2 
793  N N   . ARG A 105 ? 0.32560 0.29359 0.30788 -0.04038 0.03328  0.03372  205 ARG A N   
794  C CA  . ARG A 105 ? 0.36750 0.32547 0.35294 -0.04716 0.03829  0.03678  205 ARG A CA  
795  C C   . ARG A 105 ? 0.31935 0.26643 0.30798 -0.04905 0.03469  0.03341  205 ARG A C   
796  O O   . ARG A 105 ? 0.34356 0.28633 0.33809 -0.05516 0.03633  0.03154  205 ARG A O   
797  C CB  . ARG A 105 ? 0.42900 0.37935 0.40782 -0.04640 0.04434  0.04584  205 ARG A CB  
798  C CG  . ARG A 105 ? 0.47223 0.41268 0.45499 -0.05367 0.05020  0.04934  205 ARG A CG  
799  C CD  . ARG A 105 ? 0.54293 0.47765 0.51966 -0.05317 0.05741  0.05875  205 ARG A CD  
800  N NE  . ARG A 105 ? 0.56148 0.50745 0.53726 -0.05264 0.06220  0.06169  205 ARG A NE  
801  C CZ  . ARG A 105 ? 0.66870 0.61928 0.65151 -0.05878 0.06735  0.06195  205 ARG A CZ  
802  N NH1 . ARG A 105 ? 0.57685 0.52245 0.56879 -0.06617 0.06792  0.05871  205 ARG A NH1 
803  N NH2 . ARG A 105 ? 0.64839 0.60909 0.62928 -0.05721 0.07199  0.06541  205 ARG A NH2 
804  N N   . ALA A 106 ? 0.31250 0.25528 0.29768 -0.04369 0.02975  0.03242  206 ALA A N   
805  C CA  . ALA A 106 ? 0.28657 0.21985 0.27455 -0.04460 0.02623  0.02907  206 ALA A CA  
806  C C   . ALA A 106 ? 0.31127 0.25171 0.30613 -0.04638 0.02228  0.02094  206 ALA A C   
807  O O   . ALA A 106 ? 0.31359 0.24771 0.31256 -0.04994 0.02154  0.01789  206 ALA A O   
808  C CB  . ALA A 106 ? 0.36411 0.29208 0.34744 -0.03810 0.02224  0.03022  206 ALA A CB  
809  N N   . ALA A 107 ? 0.27397 0.22746 0.26984 -0.04346 0.01950  0.01717  207 ALA A N   
810  C CA  . ALA A 107 ? 0.24635 0.20740 0.24843 -0.04477 0.01589  0.00950  207 ALA A CA  
811  C C   . ALA A 107 ? 0.29063 0.25386 0.29840 -0.05181 0.01930  0.00773  207 ALA A C   
812  O O   . ALA A 107 ? 0.26739 0.22845 0.28006 -0.05448 0.01723  0.00267  207 ALA A O   
813  C CB  . ALA A 107 ? 0.24351 0.21838 0.24528 -0.04031 0.01277  0.00631  207 ALA A CB  
814  N N   . VAL A 108 ? 0.28605 0.25406 0.29357 -0.05462 0.02457  0.01171  208 VAL A N   
815  C CA  . VAL A 108 ? 0.26107 0.23096 0.27531 -0.06167 0.02823  0.01034  208 VAL A CA  
816  C C   . VAL A 108 ? 0.31780 0.27348 0.33404 -0.06594 0.02971  0.01150  208 VAL A C   
817  O O   . VAL A 108 ? 0.31930 0.27446 0.34226 -0.07047 0.02895  0.00661  208 VAL A O   
818  C CB  . VAL A 108 ? 0.25132 0.22800 0.26489 -0.06354 0.03447  0.01556  208 VAL A CB  
819  C CG1 . VAL A 108 ? 0.32186 0.29941 0.34379 -0.07134 0.03874  0.01456  208 VAL A CG1 
820  C CG2 . VAL A 108 ? 0.28225 0.27378 0.29402 -0.05908 0.03251  0.01342  208 VAL A CG2 
821  N N   . GLY A 109 ? 0.31308 0.25708 0.32340 -0.06412 0.03141  0.01758  209 GLY A N   
822  C CA  . GLY A 109 ? 0.34244 0.27225 0.35397 -0.06776 0.03290  0.01906  209 GLY A CA  
823  C C   . GLY A 109 ? 0.32816 0.25322 0.34251 -0.06738 0.02754  0.01252  209 GLY A C   
824  O O   . GLY A 109 ? 0.32736 0.24736 0.34691 -0.07214 0.02799  0.00966  209 GLY A O   
825  N N   . ILE A 110 ? 0.30131 0.22784 0.31251 -0.06145 0.02245  0.01000  210 ILE A N   
826  C CA  . ILE A 110 ? 0.32795 0.25004 0.34145 -0.06045 0.01779  0.00413  210 ILE A CA  
827  C C   . ILE A 110 ? 0.35426 0.28632 0.37477 -0.06346 0.01597  -0.00324 210 ILE A C   
828  O O   . ILE A 110 ? 0.33003 0.25757 0.35392 -0.06522 0.01394  -0.00790 210 ILE A O   
829  C CB  . ILE A 110 ? 0.27710 0.19800 0.28647 -0.05335 0.01325  0.00353  210 ILE A CB  
830  C CG1 . ILE A 110 ? 0.28128 0.19418 0.29178 -0.05186 0.00958  -0.00076 210 ILE A CG1 
831  C CG2 . ILE A 110 ? 0.25048 0.18544 0.26107 -0.05006 0.01031  -0.00015 210 ILE A CG2 
832  C CD1 . ILE A 110 ? 0.31507 0.21283 0.32353 -0.05372 0.01149  0.00244  210 ILE A CD1 
833  N N   . SER A 111 ? 0.26547 0.21120 0.28812 -0.06394 0.01671  -0.00448 211 SER A N   
834  C CA  . SER A 111 ? 0.29484 0.25080 0.32433 -0.06674 0.01508  -0.01148 211 SER A CA  
835  C C   . SER A 111 ? 0.31035 0.26437 0.34635 -0.07404 0.01861  -0.01224 211 SER A C   
836  O O   . SER A 111 ? 0.29952 0.25998 0.34197 -0.07668 0.01680  -0.01875 211 SER A O   
837  C CB  . SER A 111 ? 0.26841 0.23967 0.29831 -0.06507 0.01510  -0.01237 211 SER A CB  
838  O OG  . SER A 111 ? 0.30048 0.27620 0.33186 -0.06912 0.02077  -0.00801 211 SER A OG  
839  N N   . GLU A 112 ? 0.30471 0.25028 0.33962 -0.07728 0.02361  -0.00587 212 GLU A N   
840  C CA  . GLU A 112 ? 0.35057 0.29293 0.39258 -0.08442 0.02720  -0.00628 212 GLU A CA  
841  C C   . GLU A 112 ? 0.38468 0.31538 0.42863 -0.08579 0.02445  -0.01007 212 GLU A C   
842  O O   . GLU A 112 ? 0.36848 0.29866 0.42018 -0.09134 0.02539  -0.01358 212 GLU A O   
843  C CB  . GLU A 112 ? 0.34340 0.28040 0.38353 -0.08714 0.03400  0.00240  212 GLU A CB  
844  C CG  . GLU A 112 ? 0.33884 0.28789 0.37872 -0.08715 0.03810  0.00614  212 GLU A CG  
845  C CD  . GLU A 112 ? 0.35385 0.29645 0.38868 -0.08732 0.04440  0.01573  212 GLU A CD  
846  O OE1 . GLU A 112 ? 0.43393 0.36265 0.46519 -0.08725 0.04528  0.01946  212 GLU A OE1 
847  O OE2 . GLU A 112 ? 0.43691 0.38830 0.47092 -0.08710 0.04855  0.01963  212 GLU A OE2 
848  N N   . VAL A 113 ? 0.39989 0.32124 0.43730 -0.08075 0.02121  -0.00939 213 VAL A N   
849  C CA  . VAL A 113 ? 0.39976 0.30854 0.43736 -0.08117 0.01906  -0.01185 213 VAL A CA  
850  C C   . VAL A 113 ? 0.39574 0.30480 0.43137 -0.07584 0.01292  -0.01792 213 VAL A C   
851  O O   . VAL A 113 ? 0.42349 0.32222 0.45808 -0.07481 0.01068  -0.02014 213 VAL A O   
852  C CB  . VAL A 113 ? 0.40147 0.29577 0.43296 -0.08033 0.02185  -0.00445 213 VAL A CB  
853  C CG1 . VAL A 113 ? 0.48032 0.37338 0.51422 -0.08581 0.02841  0.00155  213 VAL A CG1 
854  C CG2 . VAL A 113 ? 0.35914 0.25239 0.38218 -0.07341 0.02041  -0.00027 213 VAL A CG2 
855  N N   . THR A 114 ? 0.29836 0.21869 0.33330 -0.07210 0.01030  -0.02053 214 THR A N   
856  C CA  . THR A 114 ? 0.34773 0.26980 0.38149 -0.06694 0.00491  -0.02627 214 THR A CA  
857  C C   . THR A 114 ? 0.33563 0.27340 0.37366 -0.06692 0.00309  -0.03156 214 THR A C   
858  O O   . THR A 114 ? 0.34086 0.28803 0.38132 -0.06976 0.00592  -0.02979 214 THR A O   
859  C CB  . THR A 114 ? 0.31260 0.22977 0.33930 -0.06023 0.00329  -0.02253 214 THR A CB  
860  O OG1 . THR A 114 ? 0.35464 0.28193 0.38008 -0.05842 0.00402  -0.02003 214 THR A OG1 
861  C CG2 . THR A 114 ? 0.35033 0.25314 0.37223 -0.06006 0.00575  -0.01604 214 THR A CG2 
862  N N   . ASP A 115 ? 0.29217 0.23273 0.33066 -0.06318 -0.00153 -0.03787 215 ASP A N   
863  C CA  . ASP A 115 ? 0.31935 0.27425 0.36080 -0.06185 -0.00379 -0.04285 215 ASP A CA  
864  C C   . ASP A 115 ? 0.30547 0.26430 0.34244 -0.05573 -0.00558 -0.04101 215 ASP A C   
865  O O   . ASP A 115 ? 0.33920 0.30738 0.37761 -0.05284 -0.00862 -0.04586 215 ASP A O   
866  C CB  . ASP A 115 ? 0.31650 0.27326 0.36129 -0.06102 -0.00779 -0.05112 215 ASP A CB  
867  C CG  . ASP A 115 ? 0.41763 0.36484 0.45740 -0.05479 -0.01114 -0.05227 215 ASP A CG  
868  O OD1 . ASP A 115 ? 0.37942 0.31650 0.41405 -0.05227 -0.01007 -0.04665 215 ASP A OD1 
869  O OD2 . ASP A 115 ? 0.48108 0.43115 0.52204 -0.05210 -0.01472 -0.05875 215 ASP A OD2 
870  N N   . SER A 116 ? 0.28356 0.23555 0.31552 -0.05361 -0.00389 -0.03436 216 SER A N   
871  C CA  . SER A 116 ? 0.25616 0.21094 0.28474 -0.04763 -0.00599 -0.03295 216 SER A CA  
872  C C   . SER A 116 ? 0.26164 0.23060 0.29169 -0.04779 -0.00556 -0.03332 216 SER A C   
873  O O   . SER A 116 ? 0.29114 0.26675 0.32397 -0.05254 -0.00270 -0.03302 216 SER A O   
874  C CB  . SER A 116 ? 0.28285 0.22693 0.30620 -0.04532 -0.00443 -0.02594 216 SER A CB  
875  O OG  . SER A 116 ? 0.28771 0.23099 0.31001 -0.04937 -0.00006 -0.02054 216 SER A OG  
876  N N   . LEU A 117 ? 0.24948 0.22296 0.27797 -0.04234 -0.00837 -0.03399 217 LEU A N   
877  C CA  . LEU A 117 ? 0.23825 0.22374 0.26675 -0.04102 -0.00840 -0.03363 217 LEU A CA  
878  C C   . LEU A 117 ? 0.22480 0.20597 0.24870 -0.03736 -0.00793 -0.02777 217 LEU A C   
879  O O   . LEU A 117 ? 0.23443 0.20849 0.25679 -0.03303 -0.01020 -0.02705 217 LEU A O   
880  C CB  . LEU A 117 ? 0.21322 0.20837 0.24438 -0.03745 -0.01252 -0.03999 217 LEU A CB  
881  C CG  . LEU A 117 ? 0.25429 0.26321 0.28596 -0.03620 -0.01294 -0.04086 217 LEU A CG  
882  C CD1 . LEU A 117 ? 0.36672 0.38590 0.40231 -0.03534 -0.01591 -0.04805 217 LEU A CD1 
883  C CD2 . LEU A 117 ? 0.29180 0.30053 0.32037 -0.03069 -0.01467 -0.03796 217 LEU A CD2 
884  N N   . THR A 118 ? 0.20898 0.19467 0.23082 -0.03874 -0.00495 -0.02360 218 THR A N   
885  C CA  . THR A 118 ? 0.20105 0.18361 0.21822 -0.03491 -0.00467 -0.01830 218 THR A CA  
886  C C   . THR A 118 ? 0.22122 0.21676 0.23776 -0.03196 -0.00582 -0.01920 218 THR A C   
887  O O   . THR A 118 ? 0.25036 0.25516 0.26793 -0.03479 -0.00360 -0.01985 218 THR A O   
888  C CB  . THR A 118 ? 0.22984 0.20404 0.24343 -0.03806 0.00014  -0.01148 218 THR A CB  
889  O OG1 . THR A 118 ? 0.27285 0.23464 0.28696 -0.04047 0.00084  -0.01099 218 THR A OG1 
890  C CG2 . THR A 118 ? 0.21653 0.18776 0.22486 -0.03339 0.00007  -0.00623 218 THR A CG2 
891  N N   . ILE A 119 ? 0.22089 0.21719 0.23621 -0.02617 -0.00933 -0.01946 219 ILE A N   
892  C CA  . ILE A 119 ? 0.23294 0.24053 0.24714 -0.02234 -0.01107 -0.02032 219 ILE A CA  
893  C C   . ILE A 119 ? 0.27055 0.27451 0.27925 -0.01986 -0.00942 -0.01412 219 ILE A C   
894  O O   . ILE A 119 ? 0.24962 0.24280 0.25657 -0.01833 -0.00961 -0.01083 219 ILE A O   
895  C CB  . ILE A 119 ? 0.22774 0.23922 0.24529 -0.01726 -0.01657 -0.02552 219 ILE A CB  
896  C CG1 . ILE A 119 ? 0.25723 0.27111 0.27953 -0.01916 -0.01807 -0.03139 219 ILE A CG1 
897  C CG2 . ILE A 119 ? 0.22633 0.24978 0.24298 -0.01309 -0.01885 -0.02708 219 ILE A CG2 
898  C CD1 . ILE A 119 ? 0.26958 0.28307 0.29529 -0.01420 -0.02275 -0.03540 219 ILE A CD1 
899  N N   . ILE A 120 ? 0.22131 0.23438 0.22695 -0.01895 -0.00780 -0.01248 220 ILE A N   
900  C CA  . ILE A 120 ? 0.22739 0.23839 0.22696 -0.01571 -0.00632 -0.00680 220 ILE A CA  
901  C C   . ILE A 120 ? 0.25441 0.27719 0.25267 -0.00996 -0.00979 -0.00937 220 ILE A C   
902  O O   . ILE A 120 ? 0.24005 0.27413 0.23979 -0.01046 -0.01000 -0.01284 220 ILE A O   
903  C CB  . ILE A 120 ? 0.22827 0.23744 0.22387 -0.01983 0.00024  -0.00079 220 ILE A CB  
904  C CG1 . ILE A 120 ? 0.26770 0.26773 0.26628 -0.02653 0.00361  0.00018  220 ILE A CG1 
905  C CG2 . ILE A 120 ? 0.26049 0.26388 0.24915 -0.01604 0.00177  0.00571  220 ILE A CG2 
906  C CD1 . ILE A 120 ? 0.26475 0.27259 0.26884 -0.03169 0.00490  -0.00424 220 ILE A CD1 
907  N N   . VAL A 121 ? 0.24843 0.26875 0.24414 -0.00431 -0.01271 -0.00795 221 VAL A N   
908  C CA  . VAL A 121 ? 0.23757 0.26816 0.23072 0.00170  -0.01573 -0.00950 221 VAL A CA  
909  C C   . VAL A 121 ? 0.26321 0.29169 0.24839 0.00375  -0.01222 -0.00280 221 VAL A C   
910  O O   . VAL A 121 ? 0.24422 0.26207 0.22689 0.00423  -0.01114 0.00167  221 VAL A O   
911  C CB  . VAL A 121 ? 0.25306 0.28379 0.25019 0.00728  -0.02233 -0.01379 221 VAL A CB  
912  C CG1 . VAL A 121 ? 0.30646 0.34867 0.30145 0.01366  -0.02603 -0.01639 221 VAL A CG1 
913  C CG2 . VAL A 121 ? 0.25283 0.28360 0.25770 0.00534  -0.02512 -0.01960 221 VAL A CG2 
914  N N   . SER A 122 ? 0.27864 0.29830 0.19138 0.00141  -0.01264 -0.00062 222 SER A N   
915  C CA  . SER A 122 ? 0.30793 0.32749 0.20834 0.00218  -0.01212 0.00771  222 SER A CA  
916  C C   . SER A 122 ? 0.33825 0.35756 0.22932 0.00910  -0.01708 0.00332  222 SER A C   
917  O O   . SER A 122 ? 0.35574 0.38355 0.24540 0.01376  -0.01757 -0.00507 222 SER A O   
918  C CB  . SER A 122 ? 0.31772 0.34997 0.21252 0.00064  -0.00514 0.01224  222 SER A CB  
919  O OG  . SER A 122 ? 0.34801 0.38083 0.22867 0.00291  -0.00487 0.01886  222 SER A OG  
920  N N   . GLU A 123 ? 0.33237 0.34223 0.21690 0.00990  -0.02080 0.00903  223 GLU A N   
921  C CA  . GLU A 123 ? 0.37899 0.38857 0.25420 0.01659  -0.02577 0.00542  223 GLU A CA  
922  C C   . GLU A 123 ? 0.41905 0.43960 0.28056 0.02007  -0.02286 0.00795  223 GLU A C   
923  O O   . GLU A 123 ? 0.44295 0.46561 0.29630 0.02634  -0.02677 0.00377  223 GLU A O   
924  C CB  . GLU A 123 ? 0.41361 0.40930 0.28643 0.01652  -0.03102 0.01058  223 GLU A CB  
925  C CG  . GLU A 123 ? 0.42468 0.41661 0.28911 0.01320  -0.02846 0.02325  223 GLU A CG  
926  C CD  . GLU A 123 ? 0.63856 0.61672 0.50004 0.01379  -0.03419 0.02795  223 GLU A CD  
927  O OE1 . GLU A 123 ? 0.58681 0.55591 0.45768 0.01328  -0.03860 0.02374  223 GLU A OE1 
928  O OE2 . GLU A 123 ? 0.84077 0.81700 0.69018 0.01489  -0.03421 0.03585  223 GLU A OE2 
929  N N   . GLU A 124 ? 0.39136 0.41891 0.25028 0.01624  -0.01607 0.01442  224 GLU A N   
930  C CA  . GLU A 124 ? 0.43025 0.46822 0.27580 0.01908  -0.01234 0.01742  224 GLU A CA  
931  C C   . GLU A 124 ? 0.43984 0.49242 0.28732 0.02133  -0.00889 0.00930  224 GLU A C   
932  O O   . GLU A 124 ? 0.41785 0.47853 0.25532 0.02702  -0.00941 0.00585  224 GLU A O   
933  C CB  . GLU A 124 ? 0.49052 0.52777 0.33138 0.01353  -0.00622 0.02959  224 GLU A CB  
934  C CG  . GLU A 124 ? 0.59454 0.61713 0.43396 0.01059  -0.00900 0.03848  224 GLU A CG  
935  C CD  . GLU A 124 ? 0.82573 0.84348 0.65009 0.01610  -0.01352 0.04170  224 GLU A CD  
936  O OE1 . GLU A 124 ? 0.91440 0.93994 0.72552 0.01937  -0.01074 0.04399  224 GLU A OE1 
937  O OE2 . GLU A 124 ? 0.85293 0.85909 0.67859 0.01739  -0.01995 0.04169  224 GLU A OE2 
938  N N   . THR A 125 ? 0.36504 0.42116 0.22507 0.01719  -0.00557 0.00605  225 THR A N   
939  C CA  . THR A 125 ? 0.33789 0.40807 0.20038 0.01867  -0.00167 -0.00091 225 THR A CA  
940  C C   . THR A 125 ? 0.33134 0.40167 0.20552 0.02031  -0.00481 -0.01218 225 THR A C   
941  O O   . THR A 125 ? 0.33884 0.42042 0.21424 0.02293  -0.00287 -0.01946 225 THR A O   
942  C CB  . THR A 125 ? 0.37358 0.45037 0.24043 0.01253  0.00610  0.00464  225 THR A CB  
943  O OG1 . THR A 125 ? 0.37688 0.44549 0.25725 0.00692  0.00579  0.00568  225 THR A OG1 
944  C CG2 . THR A 125 ? 0.34259 0.41970 0.19772 0.01045  0.01049  0.01611  225 THR A CG2 
945  N N   . GLY A 126 ? 0.31435 0.37239 0.19705 0.01875  -0.00930 -0.01376 226 GLY A N   
946  C CA  . GLY A 126 ? 0.31945 0.37676 0.21403 0.01893  -0.01087 -0.02311 226 GLY A CA  
947  C C   . GLY A 126 ? 0.33158 0.39259 0.23620 0.01368  -0.00605 -0.02251 226 GLY A C   
948  O O   . GLY A 126 ? 0.28838 0.34926 0.20232 0.01398  -0.00700 -0.03030 226 GLY A O   
949  N N   . GLY A 127 ? 0.31006 0.37401 0.21319 0.00891  -0.00091 -0.01362 227 GLY A N   
950  C CA  . GLY A 127 ? 0.30047 0.36797 0.21417 0.00376  0.00349  -0.01318 227 GLY A CA  
951  C C   . GLY A 127 ? 0.32386 0.37858 0.24881 0.00029  0.00029  -0.01364 227 GLY A C   
952  O O   . GLY A 127 ? 0.31936 0.36192 0.24322 -0.00065 -0.00340 -0.00937 227 GLY A O   
953  N N   . VAL A 128 ? 0.25865 0.31601 0.19432 -0.00142 0.00158  -0.01907 228 VAL A N   
954  C CA  . VAL A 128 ? 0.24570 0.29146 0.19201 -0.00429 -0.00133 -0.02050 228 VAL A CA  
955  C C   . VAL A 128 ? 0.28180 0.32867 0.23564 -0.01072 0.00293  -0.01445 228 VAL A C   
956  O O   . VAL A 128 ? 0.31214 0.37091 0.26822 -0.01197 0.00783  -0.01518 228 VAL A O   
957  C CB  . VAL A 128 ? 0.26142 0.30755 0.21415 -0.00094 -0.00376 -0.03175 228 VAL A CB  
958  C CG1 . VAL A 128 ? 0.23001 0.26333 0.19303 -0.00385 -0.00660 -0.03302 228 VAL A CG1 
959  C CG2 . VAL A 128 ? 0.28966 0.33538 0.23555 0.00536  -0.00764 -0.03812 228 VAL A CG2 
960  N N   . SER A 129 ? 0.24619 0.28087 0.20447 -0.01478 0.00105  -0.00884 229 SER A N   
961  C CA  . SER A 129 ? 0.25284 0.28720 0.21948 -0.02105 0.00451  -0.00335 229 SER A CA  
962  C C   . SER A 129 ? 0.23718 0.25863 0.21354 -0.02307 0.00042  -0.00529 229 SER A C   
963  O O   . SER A 129 ? 0.25232 0.26399 0.22763 -0.02017 -0.00469 -0.00900 229 SER A O   
964  C CB  . SER A 129 ? 0.29980 0.33261 0.26104 -0.02503 0.00750  0.00813  229 SER A CB  
965  O OG  . SER A 129 ? 0.36285 0.38490 0.31662 -0.02330 0.00314  0.01186  229 SER A OG  
966  N N   . VAL A 130 ? 0.23487 0.25666 0.22097 -0.02801 0.00283  -0.00310 230 VAL A N   
967  C CA  . VAL A 130 ? 0.25783 0.26791 0.25356 -0.03025 -0.00067 -0.00466 230 VAL A CA  
968  C C   . VAL A 130 ? 0.27502 0.28185 0.27639 -0.03676 0.00174  0.00412  230 VAL A C   
969  O O   . VAL A 130 ? 0.26771 0.28468 0.27141 -0.03992 0.00709  0.00746  230 VAL A O   
970  C CB  . VAL A 130 ? 0.26653 0.28029 0.27056 -0.02865 -0.00114 -0.01409 230 VAL A CB  
971  C CG1 . VAL A 130 ? 0.24169 0.24544 0.25642 -0.03228 -0.00327 -0.01383 230 VAL A CG1 
972  C CG2 . VAL A 130 ? 0.24881 0.26013 0.24851 -0.02255 -0.00492 -0.02273 230 VAL A CG2 
973  N N   . ALA A 131 ? 0.26061 0.25338 0.26441 -0.03882 -0.00202 0.00776  231 ALA A N   
974  C CA  . ALA A 131 ? 0.25632 0.24421 0.26665 -0.04498 -0.00050 0.01550  231 ALA A CA  
975  C C   . ALA A 131 ? 0.26641 0.24772 0.28861 -0.04658 -0.00317 0.01084  231 ALA A C   
976  O O   . ALA A 131 ? 0.24725 0.21917 0.27003 -0.04361 -0.00807 0.00541  231 ALA A O   
977  C CB  . ALA A 131 ? 0.24182 0.21838 0.24612 -0.04626 -0.00288 0.02358  231 ALA A CB  
978  N N   . LYS A 132 ? 0.24784 0.23429 0.27935 -0.05107 0.00018  0.01260  232 LYS A N   
979  C CA  . LYS A 132 ? 0.27914 0.26060 0.32229 -0.05260 -0.00215 0.00815  232 LYS A CA  
980  C C   . LYS A 132 ? 0.24976 0.23340 0.30166 -0.05910 0.00139  0.01471  232 LYS A C   
981  O O   . LYS A 132 ? 0.22879 0.22450 0.28098 -0.06134 0.00706  0.01760  232 LYS A O   
982  C CB  . LYS A 132 ? 0.28564 0.27573 0.33216 -0.04898 -0.00192 -0.00182 232 LYS A CB  
983  C CG  . LYS A 132 ? 0.30802 0.29454 0.36638 -0.05030 -0.00398 -0.00666 232 LYS A CG  
984  C CD  . LYS A 132 ? 0.30675 0.27753 0.36487 -0.04793 -0.01014 -0.01012 232 LYS A CD  
985  C CE  . LYS A 132 ? 0.45565 0.42211 0.52477 -0.04904 -0.01240 -0.01462 232 LYS A CE  
986  N NZ  . LYS A 132 ? 0.58373 0.53628 0.65151 -0.04551 -0.01793 -0.02006 232 LYS A NZ  
987  N N   . ASN A 133 ? 0.26519 0.23708 0.32392 -0.06219 -0.00172 0.01726  233 ASN A N   
988  C CA  . ASN A 133 ? 0.28348 0.25632 0.35235 -0.06849 0.00107  0.02269  233 ASN A CA  
989  C C   . ASN A 133 ? 0.31967 0.29785 0.38395 -0.07240 0.00661  0.03242  233 ASN A C   
990  O O   . ASN A 133 ? 0.29531 0.28132 0.36682 -0.07703 0.01160  0.03560  233 ASN A O   
991  C CB  . ASN A 133 ? 0.25515 0.23796 0.33511 -0.06934 0.00311  0.01642  233 ASN A CB  
992  C CG  . ASN A 133 ? 0.33720 0.31247 0.42326 -0.06654 -0.00247 0.00810  233 ASN A CG  
993  O OD1 . ASN A 133 ? 0.34673 0.30811 0.43238 -0.06610 -0.00730 0.00866  233 ASN A OD1 
994  N ND2 . ASN A 133 ? 0.32618 0.31035 0.41740 -0.06440 -0.00181 0.00025  233 ASN A ND2 
995  N N   . GLY A 134 ? 0.31087 0.28483 0.36298 -0.07043 0.00589  0.03705  234 GLY A N   
996  C CA  . GLY A 134 ? 0.27132 0.24834 0.31726 -0.07365 0.01072  0.04671  234 GLY A CA  
997  C C   . GLY A 134 ? 0.33325 0.32509 0.37222 -0.07213 0.01647  0.04654  234 GLY A C   
998  O O   . GLY A 134 ? 0.33223 0.32646 0.36399 -0.07420 0.02072  0.05460  234 GLY A O   
999  N N   A ASP A 135 ? 0.31052 0.31203 0.35095 -0.06846 0.01678  0.03769  235 ASP A N   
1000 N N   B ASP A 135 ? 0.31080 0.31240 0.35146 -0.06854 0.01683  0.03768  235 ASP A N   
1001 C CA  A ASP A 135 ? 0.29548 0.31170 0.32974 -0.06667 0.02211  0.03658  235 ASP A CA  
1002 C CA  B ASP A 135 ? 0.29547 0.31173 0.32981 -0.06656 0.02201  0.03632  235 ASP A CA  
1003 C C   A ASP A 135 ? 0.30532 0.32174 0.32766 -0.05981 0.01884  0.03181  235 ASP A C   
1004 C C   B ASP A 135 ? 0.30589 0.32181 0.32793 -0.05981 0.01872  0.03206  235 ASP A C   
1005 O O   A ASP A 135 ? 0.26044 0.26925 0.28333 -0.05613 0.01300  0.02562  235 ASP A O   
1006 O O   B ASP A 135 ? 0.26134 0.26912 0.28354 -0.05618 0.01278  0.02628  235 ASP A O   
1007 C CB  A ASP A 135 ? 0.33985 0.36833 0.38498 -0.06750 0.02520  0.02974  235 ASP A CB  
1008 C CB  B ASP A 135 ? 0.34007 0.36840 0.38477 -0.06679 0.02464  0.02877  235 ASP A CB  
1009 C CG  A ASP A 135 ? 0.34738 0.39079 0.39048 -0.06950 0.03316  0.03271  235 ASP A CG  
1010 C CG  B ASP A 135 ? 0.38181 0.41793 0.43546 -0.07314 0.03117  0.03360  235 ASP A CG  
1011 O OD1 A ASP A 135 ? 0.43304 0.47722 0.46469 -0.06953 0.03612  0.03965  235 ASP A OD1 
1012 O OD1 B ASP A 135 ? 0.43657 0.46912 0.48748 -0.07744 0.03432  0.04322  235 ASP A OD1 
1013 O OD2 A ASP A 135 ? 0.35311 0.40730 0.40590 -0.07095 0.03646  0.02808  235 ASP A OD2 
1014 O OD2 B ASP A 135 ? 0.32454 0.37036 0.38814 -0.07376 0.03322  0.02756  235 ASP A OD2 
1015 N N   . LEU A 136 ? 0.27671 0.30167 0.28824 -0.05811 0.02278  0.03470  236 LEU A N   
1016 C CA  . LEU A 136 ? 0.26444 0.29053 0.26397 -0.05165 0.02008  0.03083  236 LEU A CA  
1017 C C   . LEU A 136 ? 0.31593 0.35794 0.31397 -0.04883 0.02405  0.02473  236 LEU A C   
1018 O O   . LEU A 136 ? 0.33484 0.38728 0.33116 -0.05129 0.03056  0.02887  236 LEU A O   
1019 C CB  . LEU A 136 ? 0.32288 0.34422 0.30935 -0.05125 0.02042  0.03947  236 LEU A CB  
1020 C CG  . LEU A 136 ? 0.32544 0.34659 0.29925 -0.04447 0.01687  0.03600  236 LEU A CG  
1021 C CD1 . LEU A 136 ? 0.27063 0.28005 0.24631 -0.04113 0.00930  0.03033  236 LEU A CD1 
1022 C CD2 . LEU A 136 ? 0.35407 0.37275 0.31505 -0.04456 0.01845  0.04533  236 LEU A CD2 
1023 N N   . HIS A 137 ? 0.27804 0.32164 0.27690 -0.04377 0.02034  0.01490  237 HIS A N   
1024 C CA  . HIS A 137 ? 0.30846 0.36644 0.30692 -0.04051 0.02315  0.00763  237 HIS A CA  
1025 C C   . HIS A 137 ? 0.27847 0.33928 0.26351 -0.03456 0.02173  0.00548  237 HIS A C   
1026 O O   . HIS A 137 ? 0.27096 0.32431 0.25324 -0.03030 0.01610  0.00047  237 HIS A O   
1027 C CB  . HIS A 137 ? 0.28048 0.33803 0.28944 -0.03891 0.01999  -0.00208 237 HIS A CB  
1028 C CG  . HIS A 137 ? 0.30422 0.35830 0.32637 -0.04424 0.02054  -0.00054 237 HIS A CG  
1029 N ND1 . HIS A 137 ? 0.34636 0.41150 0.37642 -0.04815 0.02614  0.00045  237 HIS A ND1 
1030 C CD2 . HIS A 137 ? 0.28187 0.32276 0.31081 -0.04635 0.01625  0.00025  237 HIS A CD2 
1031 C CE1 . HIS A 137 ? 0.34840 0.40743 0.38999 -0.05232 0.02499  0.00144  237 HIS A CE1 
1032 N NE2 . HIS A 137 ? 0.28140 0.32565 0.32225 -0.05124 0.01896  0.00137  237 HIS A NE2 
1033 N N   . ARG A 138 ? 0.27032 0.34193 0.24714 -0.03420 0.02691  0.00900  238 ARG A N   
1034 C CA  . ARG A 138 ? 0.34222 0.41521 0.30493 -0.02897 0.02553  0.00901  238 ARG A CA  
1035 C C   . ARG A 138 ? 0.34237 0.42770 0.30254 -0.02360 0.02613  -0.00029 238 ARG A C   
1036 O O   . ARG A 138 ? 0.33178 0.42689 0.29982 -0.02439 0.02915  -0.00532 238 ARG A O   
1037 C CB  . ARG A 138 ? 0.40563 0.48105 0.35825 -0.03124 0.03038  0.01935  238 ARG A CB  
1038 C CG  . ARG A 138 ? 0.44248 0.50540 0.39648 -0.03644 0.02993  0.02918  238 ARG A CG  
1039 C CD  . ARG A 138 ? 0.62220 0.68494 0.56273 -0.03684 0.03316  0.03878  238 ARG A CD  
1040 N NE  . ARG A 138 ? 0.57600 0.63905 0.50346 -0.03001 0.02950  0.03583  238 ARG A NE  
1041 C CZ  . ARG A 138 ? 0.77155 0.83816 0.68480 -0.02782 0.03200  0.04099  238 ARG A CZ  
1042 N NH1 . ARG A 138 ? 0.76061 0.83018 0.66981 -0.03207 0.03862  0.05006  238 ARG A NH1 
1043 N NH2 . ARG A 138 ? 0.67254 0.73966 0.57532 -0.02112 0.02783  0.03678  238 ARG A NH2 
1044 N N   . GLU A 139 ? 0.32088 0.40549 0.27017 -0.01797 0.02293  -0.00274 239 GLU A N   
1045 C CA  . GLU A 139 ? 0.31860 0.41449 0.26294 -0.01223 0.02320  -0.01085 239 GLU A CA  
1046 C C   . GLU A 139 ? 0.31595 0.41523 0.27099 -0.01078 0.02171  -0.02112 239 GLU A C   
1047 O O   . GLU A 139 ? 0.39768 0.50986 0.35470 -0.00953 0.02519  -0.02608 239 GLU A O   
1048 C CB  . GLU A 139 ? 0.35928 0.46918 0.29663 -0.01265 0.03011  -0.00719 239 GLU A CB  
1049 C CG  . GLU A 139 ? 0.38317 0.48945 0.30833 -0.01362 0.03182  0.00309  239 GLU A CG  
1050 C CD  . GLU A 139 ? 0.47499 0.59459 0.39254 -0.01413 0.03923  0.00696  239 GLU A CD  
1051 O OE1 . GLU A 139 ? 0.59617 0.72176 0.52074 -0.01934 0.04527  0.01018  239 GLU A OE1 
1052 O OE2 . GLU A 139 ? 0.56877 0.69289 0.47349 -0.00920 0.03902  0.00647  239 GLU A OE2 
1053 N N   . LEU A 140 ? 0.28076 0.36794 0.24232 -0.01073 0.01644  -0.02442 240 LEU A N   
1054 C CA  . LEU A 140 ? 0.30884 0.39674 0.28031 -0.00956 0.01472  -0.03348 240 LEU A CA  
1055 C C   . LEU A 140 ? 0.31663 0.41000 0.28385 -0.00300 0.01255  -0.04305 240 LEU A C   
1056 O O   . LEU A 140 ? 0.35900 0.44896 0.31779 0.00092  0.00950  -0.04397 240 LEU A O   
1057 C CB  . LEU A 140 ? 0.29231 0.36451 0.27082 -0.01133 0.00985  -0.03377 240 LEU A CB  
1058 C CG  . LEU A 140 ? 0.31661 0.38261 0.30139 -0.01788 0.01141  -0.02541 240 LEU A CG  
1059 C CD1 . LEU A 140 ? 0.24551 0.29526 0.23505 -0.01865 0.00598  -0.02592 240 LEU A CD1 
1060 C CD2 . LEU A 140 ? 0.34921 0.42460 0.34389 -0.02128 0.01574  -0.02663 240 LEU A CD2 
1061 N N   . THR A 141 ? 0.35521 0.45710 0.32877 -0.00173 0.01398  -0.05047 241 THR A N   
1062 C CA  . THR A 141 ? 0.34901 0.45433 0.32079 0.00426  0.01145  -0.06053 241 THR A CA  
1063 C C   . THR A 141 ? 0.37584 0.46700 0.35231 0.00570  0.00584  -0.06561 241 THR A C   
1064 O O   . THR A 141 ? 0.36777 0.44829 0.35042 0.00200  0.00432  -0.06237 241 THR A O   
1065 C CB  . THR A 141 ? 0.40853 0.52751 0.38563 0.00514  0.01487  -0.06669 241 THR A CB  
1066 O OG1 . THR A 141 ? 0.35934 0.47449 0.34798 0.00171  0.01475  -0.06783 241 THR A OG1 
1067 C CG2 . THR A 141 ? 0.37957 0.51268 0.35233 0.00340  0.02107  -0.06160 241 THR A CG2 
1068 N N   . GLU A 142 ? 0.32178 0.34976 0.47649 0.00351  0.07251  0.05061  242 GLU A N   
1069 C CA  . GLU A 142 ? 0.36293 0.37959 0.48501 0.00290  0.07282  0.05559  242 GLU A CA  
1070 C C   . GLU A 142 ? 0.44620 0.47181 0.56284 0.01229  0.05780  0.06797  242 GLU A C   
1071 O O   . GLU A 142 ? 0.34176 0.37128 0.43699 0.01035  0.04899  0.06760  242 GLU A O   
1072 C CB  . GLU A 142 ? 0.43808 0.42898 0.54654 0.00360  0.09084  0.06162  242 GLU A CB  
1073 C CG  . GLU A 142 ? 0.66046 0.63900 0.73630 0.00472  0.09132  0.06935  242 GLU A CG  
1074 C CD  . GLU A 142 ? 0.83147 0.78461 0.89137 0.00236  0.10974  0.07206  242 GLU A CD  
1075 O OE1 . GLU A 142 ? 0.88630 0.82946 0.96143 0.00362  0.12160  0.07283  242 GLU A OE1 
1076 O OE2 . GLU A 142 ? 0.75159 0.69478 0.78350 -0.00081 0.11224  0.07341  242 GLU A OE2 
1077 N N   . GLU A 143 ? 0.37030 0.39976 0.50645 0.02259  0.05453  0.07897  243 GLU A N   
1078 C CA  . GLU A 143 ? 0.45027 0.48888 0.58327 0.03203  0.04022  0.09142  243 GLU A CA  
1079 C C   . GLU A 143 ? 0.34988 0.41194 0.48674 0.02921  0.02169  0.08464  243 GLU A C   
1080 O O   . GLU A 143 ? 0.37279 0.43988 0.49225 0.03167  0.01041  0.08971  243 GLU A O   
1081 C CB  . GLU A 143 ? 0.47188 0.51143 0.62828 0.04326  0.04064  0.10355  243 GLU A CB  
1082 C CG  . GLU A 143 ? 0.53928 0.59528 0.70216 0.05252  0.02315  0.11414  243 GLU A CG  
1083 C CD  . GLU A 143 ? 0.75282 0.80957 0.93895 0.06388  0.02414  0.12654  243 GLU A CD  
1084 O OE1 . GLU A 143 ? 0.62211 0.68606 0.83534 0.06379  0.02645  0.12193  243 GLU A OE1 
1085 O OE2 . GLU A 143 ? 0.75937 0.80961 0.93659 0.07310  0.02265  0.14112  243 GLU A OE2 
1086 N N   . ALA A 144 ? 0.32878 0.40540 0.48838 0.02410  0.01819  0.07322  244 ALA A N   
1087 C CA  . ALA A 144 ? 0.30188 0.40117 0.46728 0.02149  0.00025  0.06670  244 ALA A CA  
1088 C C   . ALA A 144 ? 0.30568 0.40420 0.44377 0.01247  -0.00281 0.05720  244 ALA A C   
1089 O O   . ALA A 144 ? 0.25837 0.36884 0.38644 0.01337  -0.01792 0.05818  244 ALA A O   
1090 C CB  . ALA A 144 ? 0.29576 0.40998 0.49229 0.01794  -0.00179 0.05667  244 ALA A CB  
1091 N N   . LEU A 145 ? 0.25211 0.33670 0.37773 0.00382  0.01133  0.04807  245 LEU A N   
1092 C CA  . LEU A 145 ? 0.25692 0.33898 0.35505 -0.00454 0.01004  0.03963  245 LEU A CA  
1093 C C   . LEU A 145 ? 0.27489 0.34916 0.34482 0.00065  0.00590  0.05082  245 LEU A C   
1094 O O   . LEU A 145 ? 0.29576 0.37852 0.34902 -0.00168 -0.00576 0.04785  245 LEU A O   
1095 C CB  . LEU A 145 ? 0.23577 0.30207 0.32565 -0.01371 0.02780  0.03001  245 LEU A CB  
1096 C CG  . LEU A 145 ? 0.24523 0.30693 0.30542 -0.02225 0.02844  0.02190  245 LEU A CG  
1097 C CD1 . LEU A 145 ? 0.29717 0.37945 0.36071 -0.02776 0.01332  0.01049  245 LEU A CD1 
1098 C CD2 . LEU A 145 ? 0.25574 0.30079 0.30809 -0.03079 0.04698  0.01382  245 LEU A CD2 
1099 N N   . LYS A 146 ? 0.31380 0.37176 0.37783 0.00778  0.01535  0.06375  246 LYS A N   
1100 C CA  . LYS A 146 ? 0.33872 0.38856 0.37641 0.01314  0.01225  0.07519  246 LYS A CA  
1101 C C   . LYS A 146 ? 0.37045 0.43815 0.41207 0.02047  -0.00722 0.08244  246 LYS A C   
1102 O O   . LYS A 146 ? 0.35444 0.42453 0.37335 0.02077  -0.01607 0.08469  246 LYS A O   
1103 C CB  . LYS A 146 ? 0.37312 0.40266 0.40731 0.01995  0.02603  0.08806  246 LYS A CB  
1104 C CG  . LYS A 146 ? 0.66199 0.68076 0.66762 0.02502  0.02511  0.09990  246 LYS A CG  
1105 C CD  . LYS A 146 ? 0.89278 0.89370 0.89913 0.03334  0.03669  0.11405  246 LYS A CD  
1106 C CE  . LYS A 146 ? 0.95738 0.94784 0.93570 0.03862  0.03570  0.12627  246 LYS A CE  
1107 N NZ  . LYS A 146 ? 0.78046 0.75850 0.72998 0.03016  0.04367  0.12000  246 LYS A NZ  
1108 N N   . GLU A 147 ? 0.30135 0.38205 0.37169 0.02638  -0.01421 0.08615  247 GLU A N   
1109 C CA  . GLU A 147 ? 0.31095 0.40960 0.38677 0.03320  -0.03313 0.09308  247 GLU A CA  
1110 C C   . GLU A 147 ? 0.34918 0.46444 0.41902 0.02593  -0.04718 0.08112  247 GLU A C   
1111 O O   . GLU A 147 ? 0.32435 0.44802 0.38042 0.02888  -0.06104 0.08550  247 GLU A O   
1112 C CB  . GLU A 147 ? 0.40275 0.51261 0.51220 0.04029  -0.03724 0.09856  247 GLU A CB  
1113 C CG  . GLU A 147 ? 0.46891 0.56400 0.58492 0.04919  -0.02566 0.11204  247 GLU A CG  
1114 C CD  . GLU A 147 ? 0.71925 0.82776 0.86608 0.05778  -0.03292 0.11958  247 GLU A CD  
1115 O OE1 . GLU A 147 ? 0.56064 0.69014 0.72373 0.05640  -0.04707 0.11413  247 GLU A OE1 
1116 O OE2 . GLU A 147 ? 0.86974 0.96779 1.02447 0.06594  -0.02452 0.13105  247 GLU A OE2 
1117 N N   . MET A 148 ? 0.31900 0.43900 0.39892 0.01643  -0.04378 0.06594  248 MET A N   
1118 C CA  . MET A 148 ? 0.27192 0.40624 0.34558 0.00865  -0.05569 0.05332  248 MET A CA  
1119 C C   . MET A 148 ? 0.29293 0.41813 0.33061 0.00472  -0.05534 0.05166  248 MET A C   
1120 O O   . MET A 148 ? 0.32725 0.46363 0.35272 0.00448  -0.07008 0.05039  248 MET A O   
1121 C CB  . MET A 148 ? 0.28352 0.42203 0.37400 -0.00087 -0.04945 0.03767  248 MET A CB  
1122 C CG  . MET A 148 ? 0.26767 0.42059 0.39493 0.00220  -0.05392 0.03727  248 MET A CG  
1123 S SD  . MET A 148 ? 0.27315 0.43010 0.41818 -0.00935 -0.04569 0.01865  248 MET A SD  
1124 C CE  . MET A 148 ? 0.19850 0.37546 0.38486 -0.00406 -0.05514 0.02049  248 MET A CE  
1125 N N   . LEU A 149 ? 0.29902 0.40387 0.31923 0.00158  -0.03863 0.05168  249 LEU A N   
1126 C CA  . LEU A 149 ? 0.35791 0.45343 0.34367 -0.00192 -0.03736 0.05074  249 LEU A CA  
1127 C C   . LEU A 149 ? 0.39301 0.48794 0.36238 0.00734  -0.04647 0.06529  249 LEU A C   
1128 O O   . LEU A 149 ? 0.39634 0.49468 0.34263 0.00583  -0.05531 0.06394  249 LEU A O   
1129 C CB  . LEU A 149 ? 0.34356 0.41711 0.31551 -0.00679 -0.01710 0.04887  249 LEU A CB  
1130 C CG  . LEU A 149 ? 0.35069 0.42404 0.33381 -0.01723 -0.00770 0.03332  249 LEU A CG  
1131 C CD1 . LEU A 149 ? 0.36414 0.41526 0.33662 -0.02086 0.01273  0.03348  249 LEU A CD1 
1132 C CD2 . LEU A 149 ? 0.39354 0.47763 0.36412 -0.02586 -0.01641 0.01982  249 LEU A CD2 
1133 N N   . GLU A 150 ? 0.35837 0.44883 0.33883 0.01711  -0.04429 0.07938  250 GLU A N   
1134 C CA  . GLU A 150 ? 0.41935 0.50993 0.38548 0.02637  -0.05317 0.09380  250 GLU A CA  
1135 C C   . GLU A 150 ? 0.41945 0.53241 0.39217 0.02889  -0.07449 0.09331  250 GLU A C   
1136 O O   . GLU A 150 ? 0.43999 0.55597 0.39144 0.03143  -0.08460 0.09790  250 GLU A O   
1137 C CB  . GLU A 150 ? 0.41122 0.49230 0.38938 0.03634  -0.04582 0.10884  250 GLU A CB  
1138 C CG  . GLU A 150 ? 0.50105 0.55795 0.46664 0.03509  -0.02577 0.11199  250 GLU A CG  
1139 C CD  . GLU A 150 ? 0.77029 0.81665 0.74261 0.04575  -0.01959 0.12826  250 GLU A CD  
1140 O OE1 . GLU A 150 ? 0.83502 0.89351 0.82586 0.05395  -0.02985 0.13638  250 GLU A OE1 
1141 O OE2 . GLU A 150 ? 0.88145 0.90726 0.84043 0.04594  -0.00444 0.13306  250 GLU A OE2 
1142 N N   . ALA A 151 ? 0.43848 0.56729 0.44063 0.02831  -0.08162 0.08800  251 ALA A N   
1143 C CA  . ALA A 151 ? 0.48125 0.63205 0.49116 0.02938  -0.10202 0.08583  251 ALA A CA  
1144 C C   . ALA A 151 ? 0.50989 0.66555 0.49815 0.02075  -0.10910 0.07349  251 ALA A C   
1145 O O   . ALA A 151 ? 0.55761 0.72408 0.53435 0.02288  -0.12470 0.07552  251 ALA A O   
1146 C CB  . ALA A 151 ? 0.38659 0.55234 0.43236 0.02874  -0.10627 0.08056  251 ALA A CB  
1147 N N   . GLU A 152 ? 0.48499 0.63227 0.46676 0.01112  -0.09750 0.06089  252 GLU A N   
1148 C CA  . GLU A 152 ? 0.48510 0.63706 0.44843 0.00224  -0.10305 0.04774  252 GLU A CA  
1149 C C   . GLU A 152 ? 0.62679 0.76797 0.55384 0.00318  -0.10257 0.05264  252 GLU A C   
1150 O O   . GLU A 152 ? 0.64806 0.79793 0.55866 0.00079  -0.11498 0.04789  252 GLU A O   
1151 C CB  . GLU A 152 ? 0.53327 0.67934 0.50242 -0.00798 -0.08975 0.03344  252 GLU A CB  
1152 C CG  . GLU A 152 ? 0.54990 0.69777 0.49875 -0.01761 -0.09212 0.01964  252 GLU A CG  
1153 C CD  . GLU A 152 ? 0.66277 0.83204 0.62360 -0.02074 -0.10967 0.01025  252 GLU A CD  
1154 O OE1 . GLU A 152 ? 0.54714 0.72934 0.53731 -0.01771 -0.11652 0.01138  252 GLU A OE1 
1155 O OE2 . GLU A 152 ? 0.84944 1.02245 0.79015 -0.02610 -0.11664 0.00192  252 GLU A OE2 
1156 N N   . PHE A 153 ? 0.53664 0.65874 0.45052 0.00655  -0.08830 0.06200  253 PHE A N   
1157 C CA  . PHE A 153 ? 0.59140 0.70219 0.47084 0.00739  -0.08636 0.06702  253 PHE A CA  
1158 C C   . PHE A 153 ? 0.68603 0.80206 0.55670 0.01749  -0.09917 0.08124  253 PHE A C   
1159 O O   . PHE A 153 ? 0.81865 0.92872 0.66051 0.01852  -0.10094 0.08511  253 PHE A O   
1160 C CB  . PHE A 153 ? 0.50345 0.59124 0.37149 0.00671  -0.06582 0.07155  253 PHE A CB  
1161 C CG  . PHE A 153 ? 0.56200 0.64167 0.42627 -0.00434 -0.05265 0.05748  253 PHE A CG  
1162 C CD1 . PHE A 153 ? 0.63489 0.72422 0.52260 -0.01080 -0.05264 0.04480  253 PHE A CD1 
1163 C CD2 . PHE A 153 ? 0.70920 0.77143 0.54679 -0.00812 -0.03990 0.05744  253 PHE A CD2 
1164 C CE1 . PHE A 153 ? 0.65559 0.73753 0.53992 -0.02081 -0.04032 0.03221  253 PHE A CE1 
1165 C CE2 . PHE A 153 ? 0.78328 0.83816 0.61751 -0.01819 -0.02766 0.04500  253 PHE A CE2 
1166 C CZ  . PHE A 153 ? 0.55502 0.61977 0.41267 -0.02452 -0.02784 0.03234  253 PHE A CZ  
1167 N N   . LYS A 154 ? 0.72646 0.85346 0.62092 0.02503  -0.10787 0.08932  254 LYS A N   
1168 C CA  . LYS A 154 ? 0.88057 1.01354 0.76861 0.03491  -0.12038 0.10327  254 LYS A CA  
1169 C C   . LYS A 154 ? 0.91743 1.06779 0.79633 0.03313  -0.13993 0.09761  254 LYS A C   
1170 O O   . LYS A 154 ? 0.85110 1.00199 0.71346 0.02499  -0.14110 0.08557  254 LYS A O   
1171 C CB  . LYS A 154 ? 0.82170 0.96112 0.73924 0.04353  -0.12306 0.11379  254 LYS A CB  
1172 C CG  . LYS A 154 ? 1.00332 1.14667 0.91485 0.05451  -0.13353 0.12998  254 LYS A CG  
1173 C CD  . LYS A 154 ? 1.30046 1.42347 1.19477 0.06037  -0.12012 0.14305  254 LYS A CD  
1174 C CE  . LYS A 154 ? 1.28578 1.40079 1.20356 0.06590  -0.10849 0.15127  254 LYS A CE  
1175 N NZ  . LYS A 154 ? 1.32490 1.43099 1.23464 0.07682  -0.10650 0.16946  254 LYS A NZ  
1176 N N   . PRO B 2   ? 1.28715 0.94572 1.18393 0.14338  -0.05962 -0.09496 102 PRO B N   
1177 C CA  . PRO B 2   ? 1.19221 0.86060 1.10035 0.12821  -0.05500 -0.09090 102 PRO B CA  
1178 C C   . PRO B 2   ? 1.05476 0.72047 0.96835 0.11106  -0.05397 -0.09377 102 PRO B C   
1179 O O   . PRO B 2   ? 1.03970 0.68086 0.94974 0.09913  -0.05841 -0.09055 102 PRO B O   
1180 C CB  . PRO B 2   ? 1.26527 0.91032 1.16857 0.12302  -0.05914 -0.08094 102 PRO B CB  
1181 C CG  . PRO B 2   ? 1.38552 1.02511 1.27871 0.14192  -0.06267 -0.08010 102 PRO B CG  
1182 C CD  . PRO B 2   ? 1.36702 1.01754 1.25689 0.15493  -0.06259 -0.08954 102 PRO B CD  
1183 N N   . THR B 3   ? 0.94093 0.63438 0.86415 0.10974  -0.04757 -0.09924 103 THR B N   
1184 C CA  . THR B 3   ? 0.85479 0.55086 0.78473 0.09328  -0.04541 -0.10154 103 THR B CA  
1185 C C   . THR B 3   ? 0.78934 0.48159 0.72727 0.07467  -0.04410 -0.09424 103 THR B C   
1186 O O   . THR B 3   ? 0.70298 0.39812 0.64326 0.07617  -0.04340 -0.08872 103 THR B O   
1187 C CB  . THR B 3   ? 0.80990 0.53893 0.74862 0.09670  -0.03825 -0.10790 103 THR B CB  
1188 O OG1 . THR B 3   ? 0.76228 0.51704 0.71174 0.09878  -0.03244 -0.10571 103 THR B OG1 
1189 C CG2 . THR B 3   ? 0.95216 0.68755 0.88360 0.11407  -0.03892 -0.11361 103 THR B CG2 
1190 N N   . PRO B 4   ? 0.81958 0.50691 0.76211 0.05685  -0.04347 -0.09346 104 PRO B N   
1191 C CA  . PRO B 4   ? 0.73736 0.42699 0.68948 0.03734  -0.04077 -0.08574 104 PRO B CA  
1192 C C   . PRO B 4   ? 0.70098 0.41746 0.66457 0.03638  -0.03536 -0.08561 104 PRO B C   
1193 O O   . PRO B 4   ? 0.69605 0.41139 0.66449 0.02767  -0.03515 -0.07781 104 PRO B O   
1194 C CB  . PRO B 4   ? 0.71707 0.40842 0.67395 0.02186  -0.03849 -0.08735 104 PRO B CB  
1195 C CG  . PRO B 4   ? 0.83171 0.50530 0.77787 0.03177  -0.04386 -0.09277 104 PRO B CG  
1196 C CD  . PRO B 4   ? 0.80054 0.47979 0.73955 0.05361  -0.04528 -0.09853 104 PRO B CD  
1197 N N   . VAL B 5   ? 0.69099 0.43359 0.66036 0.04503  -0.03083 -0.09368 105 VAL B N   
1198 C CA  . VAL B 5   ? 0.69671 0.47473 0.68178 0.04310  -0.02367 -0.09248 105 VAL B CA  
1199 C C   . VAL B 5   ? 0.62314 0.41143 0.60746 0.05487  -0.02224 -0.08584 105 VAL B C   
1200 O O   . VAL B 5   ? 0.61373 0.42192 0.60851 0.04597  -0.01749 -0.07721 105 VAL B O   
1201 C CB  . VAL B 5   ? 0.63439 0.44115 0.62729 0.04947  -0.01815 -0.10179 105 VAL B CB  
1202 C CG1 . VAL B 5   ? 0.80861 0.61310 0.78971 0.07022  -0.01950 -0.10722 105 VAL B CG1 
1203 C CG2 . VAL B 5   ? 0.64295 0.49392 0.65389 0.04636  -0.00865 -0.09736 105 VAL B CG2 
1204 N N   . GLU B 6   ? 0.59314 0.36713 0.56463 0.07520  -0.02678 -0.08988 106 GLU B N   
1205 C CA  . GLU B 6   ? 0.64642 0.42776 0.61601 0.08771  -0.02636 -0.08403 106 GLU B CA  
1206 C C   . GLU B 6   ? 0.58199 0.34347 0.54755 0.07728  -0.02958 -0.07267 106 GLU B C   
1207 O O   . GLU B 6   ? 0.62969 0.41018 0.60199 0.07646  -0.02587 -0.06470 106 GLU B O   
1208 C CB  . GLU B 6   ? 0.81482 0.57944 0.76969 0.11118  -0.03172 -0.09087 106 GLU B CB  
1209 C CG  . GLU B 6   ? 0.84498 0.63959 0.80526 0.12260  -0.02620 -0.09816 106 GLU B CG  
1210 C CD  . GLU B 6   ? 0.99343 0.77856 0.94129 0.13781  -0.02980 -0.10017 106 GLU B CD  
1211 O OE1 . GLU B 6   ? 0.97349 0.72798 0.90913 0.13588  -0.03641 -0.10147 106 GLU B OE1 
1212 O OE2 . GLU B 6   ? 1.05825 0.86775 1.00963 0.15070  -0.02614 -0.10012 106 GLU B OE2 
1213 N N   . GLU B 7   ? 0.70561 0.42852 0.66006 0.06973  -0.03671 -0.07172 107 GLU B N   
1214 C CA  . GLU B 7   ? 0.67357 0.37611 0.62416 0.05870  -0.03959 -0.06019 107 GLU B CA  
1215 C C   . GLU B 7   ? 0.59172 0.31780 0.55757 0.03820  -0.03276 -0.05249 107 GLU B C   
1216 O O   . GLU B 7   ? 0.54471 0.27621 0.51263 0.03366  -0.03095 -0.04217 107 GLU B O   
1217 C CB  . GLU B 7   ? 0.72681 0.38387 0.66426 0.05366  -0.04859 -0.06115 107 GLU B CB  
1218 C CG  . GLU B 7   ? 0.84533 0.48927 0.77081 0.07102  -0.05316 -0.06715 107 GLU B CG  
1219 C CD  . GLU B 7   ? 0.92195 0.53830 0.84079 0.06271  -0.05832 -0.06430 107 GLU B CD  
1220 O OE1 . GLU B 7   ? 0.99008 0.60690 0.91565 0.04658  -0.05668 -0.06465 107 GLU B OE1 
1221 O OE2 . GLU B 7   ? 1.08470 0.68071 0.99256 0.07252  -0.06372 -0.06162 107 GLU B OE2 
1222 N N   . ALA B 8   ? 0.51365 0.25423 0.48995 0.02618  -0.02899 -0.05753 108 ALA B N   
1223 C CA  . ALA B 8   ? 0.54751 0.31338 0.53918 0.00758  -0.02218 -0.05128 108 ALA B CA  
1224 C C   . ALA B 8   ? 0.44834 0.25176 0.45053 0.01337  -0.01545 -0.04750 108 ALA B C   
1225 O O   . ALA B 8   ? 0.45591 0.27048 0.46439 0.00312  -0.01231 -0.03813 108 ALA B O   
1226 C CB  . ALA B 8   ? 0.51453 0.29211 0.51565 -0.00329 -0.01929 -0.05881 108 ALA B CB  
1227 N N   . GLN B 9   ? 0.47252 0.29632 0.47708 0.02989  -0.01324 -0.05472 109 GLN B N   
1228 C CA  . GLN B 9   ? 0.48133 0.34074 0.49673 0.03642  -0.00752 -0.05163 109 GLN B CA  
1229 C C   . GLN B 9   ? 0.49541 0.34434 0.50295 0.04277  -0.01044 -0.04271 109 GLN B C   
1230 O O   . GLN B 9   ? 0.42321 0.29335 0.43943 0.03741  -0.00659 -0.03546 109 GLN B O   
1231 C CB  . GLN B 9   ? 0.52765 0.40747 0.54603 0.05442  -0.00529 -0.06069 109 GLN B CB  
1232 C CG  . GLN B 9   ? 0.72338 0.61414 0.74823 0.05089  -0.00234 -0.06990 109 GLN B CG  
1233 C CD  . GLN B 9   ? 0.91735 0.84237 0.96134 0.03585  0.00520  -0.06822 109 GLN B CD  
1234 O OE1 . GLN B 9   ? 0.94929 0.89670 1.00333 0.03231  0.00894  -0.06215 109 GLN B OE1 
1235 N NE2 . GLN B 9   ? 0.85427 0.78252 0.90279 0.02757  0.00695  -0.07389 109 GLN B NE2 
1236 N N   . GLN B 10  ? 0.49541 0.31128 0.48613 0.05453  -0.01756 -0.04325 110 GLN B N   
1237 C CA  . GLN B 10  ? 0.51914 0.32330 0.50112 0.06187  -0.02077 -0.03482 110 GLN B CA  
1238 C C   . GLN B 10  ? 0.51183 0.30610 0.49413 0.04391  -0.02055 -0.02344 110 GLN B C   
1239 O O   . GLN B 10  ? 0.49423 0.29969 0.47810 0.04468  -0.01895 -0.01519 110 GLN B O   
1240 C CB  . GLN B 10  ? 0.56788 0.33587 0.53137 0.07734  -0.02895 -0.03797 110 GLN B CB  
1241 C CG  . GLN B 10  ? 0.79021 0.55278 0.74539 0.09101  -0.03183 -0.03160 110 GLN B CG  
1242 C CD  . GLN B 10  ? 0.83481 0.63711 0.80121 0.10239  -0.02647 -0.03276 110 GLN B CD  
1243 O OE1 . GLN B 10  ? 0.88528 0.69837 0.85342 0.10400  -0.02550 -0.02491 110 GLN B OE1 
1244 N NE2 . GLN B 10  ? 0.79491 0.61930 0.76915 0.11052  -0.02310 -0.04245 110 GLN B NE2 
1245 N N   . LYS B 11  ? 0.53368 0.30780 0.51473 0.02780  -0.02211 -0.02280 111 LYS B N   
1246 C CA  . LYS B 11  ? 0.49227 0.25924 0.47504 0.00970  -0.02106 -0.01175 111 LYS B CA  
1247 C C   . LYS B 11  ? 0.43088 0.23739 0.43011 -0.00012 -0.01307 -0.00806 111 LYS B C   
1248 O O   . LYS B 11  ? 0.41203 0.22302 0.41200 -0.00643 -0.01141 0.00208  111 LYS B O   
1249 C CB  . LYS B 11  ? 0.54953 0.29081 0.53038 -0.00605 -0.02389 -0.01275 111 LYS B CB  
1250 C CG  . LYS B 11  ? 0.64583 0.34604 0.61101 0.00216  -0.03263 -0.01711 111 LYS B CG  
1251 C CD  . LYS B 11  ? 0.81790 0.48393 0.77098 -0.00092 -0.03811 -0.00639 111 LYS B CD  
1252 C CE  . LYS B 11  ? 0.92063 0.54454 0.85996 0.00423  -0.04729 -0.01135 111 LYS B CE  
1253 N NZ  . LYS B 11  ? 0.90160 0.49671 0.82659 0.01312  -0.05322 -0.00366 111 LYS B NZ  
1254 N N   . THR B 12  ? 0.40219 0.23740 0.41458 -0.00157 -0.00816 -0.01614 112 THR B N   
1255 C CA  . THR B 12  ? 0.39676 0.27034 0.42555 -0.00986 -0.00099 -0.01354 112 THR B CA  
1256 C C   . THR B 12  ? 0.41910 0.31254 0.44931 0.00303  0.00023  -0.00964 112 THR B C   
1257 O O   . THR B 12  ? 0.34530 0.25516 0.38162 -0.00426 0.00330  -0.00210 112 THR B O   
1258 C CB  . THR B 12  ? 0.43524 0.33449 0.47743 -0.01206 0.00354  -0.02326 112 THR B CB  
1259 O OG1 . THR B 12  ? 0.45440 0.33744 0.49649 -0.02619 0.00261  -0.02614 112 THR B OG1 
1260 C CG2 . THR B 12  ? 0.37563 0.31500 0.43518 -0.01887 0.01040  -0.02097 112 THR B CG2 
1261 N N   . ILE B 13  ? 0.32355 0.21606 0.34811 0.02261  -0.00235 -0.01485 113 ILE B N   
1262 C CA  . ILE B 13  ? 0.34362 0.25402 0.36942 0.03601  -0.00191 -0.01155 113 ILE B CA  
1263 C C   . ILE B 13  ? 0.39036 0.28076 0.40483 0.03435  -0.00527 -0.00041 113 ILE B C   
1264 O O   . ILE B 13  ? 0.35879 0.26880 0.37843 0.03380  -0.00300 0.00582  113 ILE B O   
1265 C CB  . ILE B 13  ? 0.32747 0.23684 0.34801 0.05774  -0.00457 -0.01917 113 ILE B CB  
1266 C CG1 . ILE B 13  ? 0.42146 0.35809 0.45541 0.06017  0.00011  -0.02902 113 ILE B CG1 
1267 C CG2 . ILE B 13  ? 0.39025 0.31223 0.40979 0.07217  -0.00551 -0.01499 113 ILE B CG2 
1268 C CD1 . ILE B 13  ? 0.50052 0.43619 0.52919 0.08152  -0.00202 -0.03686 113 ILE B CD1 
1269 N N   . GLU B 14  ? 0.37544 0.22631 0.37416 0.03397  -0.01098 0.00233  114 GLU B N   
1270 C CA  . GLU B 14  ? 0.43291 0.26318 0.42045 0.03185  -0.01404 0.01388  114 GLU B CA  
1271 C C   . GLU B 14  ? 0.39948 0.24161 0.39494 0.01246  -0.00945 0.02234  114 GLU B C   
1272 O O   . GLU B 14  ? 0.42169 0.26913 0.41487 0.01227  -0.00882 0.03145  114 GLU B O   
1273 C CB  . GLU B 14  ? 0.52024 0.30484 0.49090 0.03270  -0.02102 0.01554  114 GLU B CB  
1274 C CG  . GLU B 14  ? 0.70915 0.47652 0.67037 0.05062  -0.02632 0.00624  114 GLU B CG  
1275 C CD  . GLU B 14  ? 0.96883 0.73863 0.92274 0.07138  -0.02909 0.00702  114 GLU B CD  
1276 O OE1 . GLU B 14  ? 0.98491 0.76728 0.93982 0.07224  -0.02756 0.01525  114 GLU B OE1 
1277 O OE2 . GLU B 14  ? 1.06494 0.82397 1.01177 0.08737  -0.03300 -0.00087 114 GLU B OE2 
1278 N N   . ALA B 15  ? 0.37162 0.21749 0.37584 -0.00365 -0.00639 0.01944  115 ALA B N   
1279 C CA  . ALA B 15  ? 0.37320 0.23185 0.38588 -0.02230 -0.00171 0.02670  115 ALA B CA  
1280 C C   . ALA B 15  ? 0.34815 0.24673 0.37327 -0.02050 0.00341  0.02777  115 ALA B C   
1281 O O   . ALA B 15  ? 0.35491 0.26051 0.38031 -0.02712 0.00531  0.03690  115 ALA B O   
1282 C CB  . ALA B 15  ? 0.38120 0.23998 0.40250 -0.03814 0.00059  0.02157  115 ALA B CB  
1283 N N   . ILE B 16  ? 0.30766 0.23277 0.34326 -0.01131 0.00554  0.01855  116 ILE B N   
1284 C CA  . ILE B 16  ? 0.27300 0.23641 0.32175 -0.00873 0.00970  0.01870  116 ILE B CA  
1285 C C   . ILE B 16  ? 0.27225 0.23464 0.31259 0.00392  0.00691  0.02535  116 ILE B C   
1286 O O   . ILE B 16  ? 0.27954 0.25852 0.32379 -0.00053 0.00901  0.03188  116 ILE B O   
1287 C CB  . ILE B 16  ? 0.22362 0.21321 0.28516 -0.00043 0.01212  0.00774  116 ILE B CB  
1288 C CG1 . ILE B 16  ? 0.27322 0.26868 0.34465 -0.01456 0.01562  0.00199  116 ILE B CG1 
1289 C CG2 . ILE B 16  ? 0.21881 0.24599 0.29353 0.00512  0.01512  0.00792  116 ILE B CG2 
1290 C CD1 . ILE B 16  ? 0.28976 0.30370 0.37050 -0.00532 0.01745  -0.00883 116 ILE B CD1 
1291 N N   . THR B 17  ? 0.28140 0.22433 0.30965 0.02037  0.00192  0.02362  117 THR B N   
1292 C CA  . THR B 17  ? 0.29437 0.23954 0.31576 0.03425  -0.00083 0.02881  117 THR B CA  
1293 C C   . THR B 17  ? 0.31717 0.24223 0.32669 0.02689  -0.00242 0.04117  117 THR B C   
1294 O O   . THR B 17  ? 0.34479 0.28353 0.35401 0.03073  -0.00216 0.04723  117 THR B O   
1295 C CB  . THR B 17  ? 0.42605 0.35500 0.43721 0.05411  -0.00590 0.02389  117 THR B CB  
1296 O OG1 . THR B 17  ? 0.41571 0.30432 0.41183 0.05244  -0.01031 0.02493  117 THR B OG1 
1297 C CG2 . THR B 17  ? 0.39501 0.34813 0.41876 0.06266  -0.00357 0.01229  117 THR B CG2 
1298 N N   . LYS B 18  ? 0.35944 0.25272 0.35961 0.01606  -0.00405 0.04519  118 LYS B N   
1299 C CA  . LYS B 18  ? 0.34619 0.22101 0.33652 0.00677  -0.00466 0.05778  118 LYS B CA  
1300 C C   . LYS B 18  ? 0.32621 0.22919 0.32784 -0.00672 0.00113  0.06265  118 LYS B C   
1301 O O   . LYS B 18  ? 0.33893 0.24486 0.33531 -0.00646 0.00140  0.07202  118 LYS B O   
1302 C CB  . LYS B 18  ? 0.41569 0.25400 0.39757 -0.00433 -0.00706 0.06015  118 LYS B CB  
1303 C CG  . LYS B 18  ? 0.66076 0.46037 0.62370 0.00313  -0.01332 0.06752  118 LYS B CG  
1304 C CD  . LYS B 18  ? 0.75065 0.51569 0.70711 -0.00147 -0.01746 0.06408  118 LYS B CD  
1305 C CE  . LYS B 18  ? 0.77744 0.54128 0.74219 -0.02349 -0.01386 0.06596  118 LYS B CE  
1306 N NZ  . LYS B 18  ? 0.92870 0.66046 0.88861 -0.02802 -0.01837 0.06127  118 LYS B NZ  
1307 N N   . ALA B 19  ? 0.28914 0.21229 0.30575 -0.01853 0.00568  0.05643  119 ALA B N   
1308 C CA  . ALA B 19  ? 0.26768 0.21779 0.29578 -0.03174 0.01110  0.06004  119 ALA B CA  
1309 C C   . ALA B 19  ? 0.31012 0.29285 0.34535 -0.02151 0.01219  0.05923  119 ALA B C   
1310 O O   . ALA B 19  ? 0.26037 0.25430 0.29515 -0.02547 0.01385  0.06683  119 ALA B O   
1311 C CB  . ALA B 19  ? 0.28565 0.24996 0.32846 -0.04506 0.01517  0.05241  119 ALA B CB  
1312 N N   . ILE B 20  ? 0.27971 0.27860 0.32198 -0.00821 0.01123  0.04996  120 ILE B N   
1313 C CA  . ILE B 20  ? 0.25237 0.28275 0.30306 0.00212  0.01165  0.04841  120 ILE B CA  
1314 C C   . ILE B 20  ? 0.29482 0.31380 0.33122 0.01294  0.00777  0.05700  120 ILE B C   
1315 O O   . ILE B 20  ? 0.27970 0.31936 0.31950 0.01404  0.00858  0.06095  120 ILE B O   
1316 C CB  . ILE B 20  ? 0.23285 0.27987 0.29341 0.01494  0.01118  0.03738  120 ILE B CB  
1317 C CG1 . ILE B 20  ? 0.28474 0.34967 0.36152 0.00390  0.01577  0.02934  120 ILE B CG1 
1318 C CG2 . ILE B 20  ? 0.25278 0.32708 0.31981 0.02861  0.01003  0.03662  120 ILE B CG2 
1319 C CD1 . ILE B 20  ? 0.19662 0.29308 0.28900 -0.00855 0.02035  0.03012  120 ILE B CD1 
1320 N N   . ASN B 21  ? 0.27032 0.25588 0.29021 0.02134  0.00318  0.05993  121 ASN B N   
1321 C CA  . ASN B 21  ? 0.37640 0.34879 0.38154 0.03187  -0.00075 0.06862  121 ASN B CA  
1322 C C   . ASN B 21  ? 0.38916 0.35697 0.38848 0.01921  0.00136  0.08026  121 ASN B C   
1323 O O   . ASN B 21  ? 0.37209 0.35134 0.36796 0.02468  0.00074  0.08615  121 ASN B O   
1324 C CB  . ASN B 21  ? 0.41719 0.35220 0.40574 0.04213  -0.00621 0.06954  121 ASN B CB  
1325 C CG  . ASN B 21  ? 0.65017 0.57218 0.62362 0.05529  -0.01072 0.07772  121 ASN B CG  
1326 O OD1 . ASN B 21  ? 0.77766 0.72199 0.75471 0.06729  -0.01171 0.07644  121 ASN B OD1 
1327 N ND2 . ASN B 21  ? 0.64455 0.53021 0.60132 0.05306  -0.01370 0.08631  121 ASN B ND2 
1328 N N   . TYR B 22  ? 0.30790 0.25961 0.30619 0.00240  0.00387  0.08374  122 TYR B N   
1329 C CA  . TYR B 22  ? 0.35869 0.30640 0.35217 -0.01065 0.00660  0.09520  122 TYR B CA  
1330 C C   . TYR B 22  ? 0.32517 0.31094 0.33120 -0.01503 0.01077  0.09488  122 TYR B C   
1331 O O   . TYR B 22  ? 0.32784 0.31872 0.32752 -0.01434 0.01116  0.10360  122 TYR B O   
1332 C CB  . TYR B 22  ? 0.39058 0.31843 0.38467 -0.02844 0.00882  0.09699  122 TYR B CB  
1333 C CG  . TYR B 22  ? 0.39491 0.31691 0.38512 -0.04386 0.01227  0.10900  122 TYR B CG  
1334 C CD1 . TYR B 22  ? 0.32740 0.27878 0.32957 -0.05525 0.01775  0.10961  122 TYR B CD1 
1335 C CD2 . TYR B 22  ? 0.49892 0.38570 0.47420 -0.04747 0.01010  0.11957  122 TYR B CD2 
1336 C CE1 . TYR B 22  ? 0.39939 0.34608 0.39807 -0.06910 0.02129  0.12061  122 TYR B CE1 
1337 C CE2 . TYR B 22  ? 0.55128 0.43312 0.52365 -0.06175 0.01372  0.13112  122 TYR B CE2 
1338 C CZ  . TYR B 22  ? 0.52359 0.43589 0.50752 -0.07231 0.01947  0.13154  122 TYR B CZ  
1339 O OH  . TYR B 22  ? 0.62361 0.53288 0.60402 -0.08360 0.02371  0.13908  122 TYR B OH  
1340 N N   . MET B 23  ? 0.28377 0.29641 0.30754 -0.01943 0.01376  0.08483  123 MET B N   
1341 C CA  . MET B 23  ? 0.21426 0.26302 0.25144 -0.02434 0.01737  0.08349  123 MET B CA  
1342 C C   . MET B 23  ? 0.28454 0.35371 0.32266 -0.00786 0.01441  0.08202  123 MET B C   
1343 O O   . MET B 23  ? 0.27281 0.36142 0.31284 -0.00881 0.01545  0.08606  123 MET B O   
1344 C CB  . MET B 23  ? 0.21000 0.27963 0.26593 -0.03329 0.02096  0.07310  123 MET B CB  
1345 C CG  . MET B 23  ? 0.28260 0.33507 0.33864 -0.05085 0.02394  0.07479  123 MET B CG  
1346 S SD  . MET B 23  ? 0.23168 0.30975 0.30933 -0.06280 0.02848  0.06367  123 MET B SD  
1347 C CE  . MET B 23  ? 0.22221 0.29394 0.30169 -0.04878 0.02531  0.05267  123 MET B CE  
1348 N N   . ALA B 24  ? 0.23593 0.30123 0.27274 0.00768  0.01052  0.07613  124 ALA B N   
1349 C CA  . ALA B 24  ? 0.25133 0.33527 0.28949 0.02403  0.00719  0.07454  124 ALA B CA  
1350 C C   . ALA B 24  ? 0.29743 0.36931 0.31904 0.02909  0.00467  0.08577  124 ALA B C   
1351 O O   . ALA B 24  ? 0.26139 0.35596 0.28613 0.03370  0.00404  0.08728  124 ALA B O   
1352 C CB  . ALA B 24  ? 0.26027 0.33776 0.29793 0.04003  0.00345  0.06727  124 ALA B CB  
1353 N N   . LYS B 25  ? 0.27532 0.31133 0.27925 0.02804  0.00306  0.09389  125 LYS B N   
1354 C CA  . LYS B 25  ? 0.31918 0.34095 0.30601 0.03317  0.00073  0.10555  125 LYS B CA  
1355 C C   . LYS B 25  ? 0.32365 0.36128 0.31212 0.02143  0.00476  0.11257  125 LYS B C   
1356 O O   . LYS B 25  ? 0.35629 0.39614 0.33476 0.02792  0.00315  0.12022  125 LYS B O   
1357 C CB  . LYS B 25  ? 0.38718 0.36646 0.35622 0.03176  -0.00132 0.11339  125 LYS B CB  
1358 C CG  . LYS B 25  ? 0.58380 0.54227 0.54601 0.04641  -0.00656 0.10846  125 LYS B CG  
1359 C CD  . LYS B 25  ? 0.86683 0.78440 0.80832 0.04809  -0.00988 0.11914  125 LYS B CD  
1360 C CE  . LYS B 25  ? 0.83700 0.72825 0.77203 0.05826  -0.01465 0.11368  125 LYS B CE  
1361 N NZ  . LYS B 25  ? 0.78350 0.65084 0.71844 0.04426  -0.01332 0.11309  125 LYS B NZ  
1362 N N   . ARG B 26  ? 0.29518 0.34383 0.29554 0.00467  0.00991  0.11012  126 ARG B N   
1363 C CA  . ARG B 26  ? 0.31129 0.37310 0.31308 -0.00795 0.01425  0.11681  126 ARG B CA  
1364 C C   . ARG B 26  ? 0.32196 0.42410 0.34208 -0.01016 0.01637  0.10885  126 ARG B C   
1365 O O   . ARG B 26  ? 0.29775 0.41384 0.32092 -0.02085 0.02010  0.11281  126 ARG B O   
1366 C CB  . ARG B 26  ? 0.31296 0.35589 0.31391 -0.02639 0.01849  0.12128  126 ARG B CB  
1367 C CG  . ARG B 26  ? 0.38901 0.39234 0.37108 -0.02644 0.01660  0.13206  126 ARG B CG  
1368 C CD  . ARG B 26  ? 0.35261 0.33415 0.33625 -0.04238 0.01914  0.13317  126 ARG B CD  
1369 N NE  . ARG B 26  ? 0.45113 0.39455 0.41744 -0.04277 0.01692  0.14410  126 ARG B NE  
1370 C CZ  . ARG B 26  ? 0.56715 0.48363 0.52408 -0.03242 0.01168  0.14270  126 ARG B CZ  
1371 N NH1 . ARG B 26  ? 0.47512 0.39866 0.43756 -0.02018 0.00838  0.13109  126 ARG B NH1 
1372 N NH2 . ARG B 26  ? 0.53801 0.41969 0.47983 -0.03420 0.00968  0.15339  126 ARG B NH2 
1373 N N   . ARG B 27  ? 0.29550 0.32353 0.26827 -0.02508 -0.02371 0.07707  127 ARG B N   
1374 C CA  . ARG B 27  ? 0.27093 0.30464 0.23753 -0.02798 -0.02601 0.07015  127 ARG B CA  
1375 C C   . ARG B 27  ? 0.33736 0.36443 0.29951 -0.02982 -0.02352 0.05912  127 ARG B C   
1376 O O   . ARG B 27  ? 0.39397 0.42548 0.34987 -0.03391 -0.02507 0.05315  127 ARG B O   
1377 C CB  . ARG B 27  ? 0.39792 0.44411 0.35707 -0.03293 -0.03000 0.07347  127 ARG B CB  
1378 C CG  . ARG B 27  ? 0.37329 0.42805 0.33684 -0.03164 -0.03372 0.08399  127 ARG B CG  
1379 C CD  . ARG B 27  ? 0.40577 0.47400 0.36057 -0.03724 -0.03800 0.08543  127 ARG B CD  
1380 N NE  . ARG B 27  ? 0.37684 0.45392 0.33581 -0.03638 -0.04185 0.09735  127 ARG B NE  
1381 C CZ  . ARG B 27  ? 0.37994 0.45835 0.34164 -0.03578 -0.04188 0.10819  127 ARG B CZ  
1382 N NH1 . ARG B 27  ? 0.43778 0.50999 0.39762 -0.03648 -0.03828 0.10864  127 ARG B NH1 
1383 N NH2 . ARG B 27  ? 0.40371 0.48984 0.37156 -0.03443 -0.04581 0.11946  127 ARG B NH2 
1384 N N   . ILE B 28  ? 0.31067 0.32732 0.27697 -0.02685 -0.01982 0.05604  128 ILE B N   
1385 C CA  . ILE B 28  ? 0.30261 0.31294 0.26622 -0.02815 -0.01782 0.04624  128 ILE B CA  
1386 C C   . ILE B 28  ? 0.35142 0.36209 0.31787 -0.02656 -0.01900 0.04197  128 ILE B C   
1387 O O   . ILE B 28  ? 0.31970 0.32752 0.29212 -0.02237 -0.01768 0.04331  128 ILE B O   
1388 C CB  . ILE B 28  ? 0.29219 0.29215 0.25907 -0.02608 -0.01383 0.04472  128 ILE B CB  
1389 C CG1 . ILE B 28  ? 0.28015 0.28048 0.24456 -0.02855 -0.01275 0.04948  128 ILE B CG1 
1390 C CG2 . ILE B 28  ? 0.28001 0.27386 0.24544 -0.02690 -0.01226 0.03506  128 ILE B CG2 
1391 C CD1 . ILE B 28  ? 0.35612 0.34628 0.32669 -0.02604 -0.00933 0.05019  128 ILE B CD1 
1392 N N   . GLY B 29  ? 0.30292 0.31768 0.26592 -0.03002 -0.02142 0.03683  129 GLY B N   
1393 C CA  . GLY B 29  ? 0.25429 0.27011 0.22086 -0.02919 -0.02298 0.03400  129 GLY B CA  
1394 C C   . GLY B 29  ? 0.30550 0.31328 0.27461 -0.02700 -0.02007 0.02952  129 GLY B C   
1395 O O   . GLY B 29  ? 0.30272 0.30425 0.26970 -0.02808 -0.01799 0.02500  129 GLY B O   
1396 N N   . ALA B 30  ? 0.27416 0.28317 0.24786 -0.02404 -0.01989 0.03089  130 ALA B N   
1397 C CA  . ALA B 30  ? 0.24726 0.25060 0.22263 -0.02212 -0.01722 0.02677  130 ALA B CA  
1398 C C   . ALA B 30  ? 0.25047 0.25900 0.22917 -0.02149 -0.01853 0.02707  130 ALA B C   
1399 O O   . ALA B 30  ? 0.23133 0.24697 0.21296 -0.02071 -0.02031 0.03168  130 ALA B O   
1400 C CB  . ALA B 30  ? 0.23937 0.23751 0.21742 -0.01791 -0.01339 0.02809  130 ALA B CB  
1401 N N   . LEU B 31  ? 0.25341 0.25906 0.23198 -0.02205 -0.01772 0.02265  131 LEU B N   
1402 C CA  . LEU B 31  ? 0.24088 0.25208 0.22230 -0.02229 -0.01898 0.02330  131 LEU B CA  
1403 C C   . LEU B 31  ? 0.22620 0.23416 0.20691 -0.02055 -0.01588 0.01967  131 LEU B C   
1404 O O   . LEU B 31  ? 0.22540 0.22818 0.20404 -0.02261 -0.01603 0.01535  131 LEU B O   
1405 C CB  . LEU B 31  ? 0.25103 0.26401 0.23347 -0.02683 -0.02318 0.02193  131 LEU B CB  
1406 C CG  . LEU B 31  ? 0.29422 0.31322 0.28087 -0.02805 -0.02529 0.02393  131 LEU B CG  
1407 C CD1 . LEU B 31  ? 0.30904 0.33647 0.29894 -0.02604 -0.02543 0.02967  131 LEU B CD1 
1408 C CD2 . LEU B 31  ? 0.31055 0.32969 0.30054 -0.03256 -0.02986 0.02242  131 LEU B CD2 
1409 N N   . LEU B 32  ? 0.22899 0.24085 0.21181 -0.01689 -0.01316 0.02098  132 LEU B N   
1410 C CA  . LEU B 32  ? 0.22999 0.23953 0.21177 -0.01486 -0.00969 0.01643  132 LEU B CA  
1411 C C   . LEU B 32  ? 0.24712 0.26645 0.23045 -0.01410 -0.00905 0.01776  132 LEU B C   
1412 O O   . LEU B 32  ? 0.23042 0.25607 0.21738 -0.01115 -0.00754 0.02082  132 LEU B O   
1413 C CB  . LEU B 32  ? 0.24805 0.25238 0.23177 -0.01067 -0.00596 0.01506  132 LEU B CB  
1414 C CG  . LEU B 32  ? 0.27121 0.27274 0.25498 -0.00824 -0.00218 0.00897  132 LEU B CG  
1415 C CD1 . LEU B 32  ? 0.31375 0.30894 0.29320 -0.01146 -0.00303 0.00421  132 LEU B CD1 
1416 C CD2 . LEU B 32  ? 0.36740 0.36341 0.35618 -0.00407 0.00081  0.00863  132 LEU B CD2 
1417 N N   . THR B 33  ? 0.22773 0.24919 0.20881 -0.01690 -0.01025 0.01600  133 THR B N   
1418 C CA  . THR B 33  ? 0.22751 0.25992 0.20930 -0.01726 -0.00996 0.01813  133 THR B CA  
1419 C C   . THR B 33  ? 0.23171 0.26514 0.21027 -0.01545 -0.00614 0.01240  133 THR B C   
1420 O O   . THR B 33  ? 0.23924 0.26628 0.21452 -0.01699 -0.00646 0.00791  133 THR B O   
1421 C CB  . THR B 33  ? 0.22989 0.26559 0.21256 -0.02228 -0.01479 0.02158  133 THR B CB  
1422 O OG1 . THR B 33  ? 0.25591 0.29201 0.24262 -0.02385 -0.01828 0.02600  133 THR B OG1 
1423 C CG2 . THR B 33  ? 0.25661 0.30452 0.23966 -0.02331 -0.01452 0.02473  133 THR B CG2 
1424 N N   . ILE B 34  ? 0.23483 0.27685 0.21475 -0.01225 -0.00247 0.01197  134 ILE B N   
1425 C CA  . ILE B 34  ? 0.24016 0.28476 0.21735 -0.01022 0.00166  0.00512  134 ILE B CA  
1426 C C   . ILE B 34  ? 0.25261 0.31134 0.22718 -0.01266 0.00148  0.00729  134 ILE B C   
1427 O O   . ILE B 34  ? 0.29294 0.36250 0.27051 -0.01191 0.00232  0.01199  134 ILE B O   
1428 C CB  . ILE B 34  ? 0.29185 0.33625 0.27369 -0.00441 0.00660  0.00153  134 ILE B CB  
1429 C CG1 . ILE B 34  ? 0.33514 0.36671 0.32058 -0.00251 0.00608  0.00193  134 ILE B CG1 
1430 C CG2 . ILE B 34  ? 0.33749 0.38427 0.31727 -0.00233 0.01097  -0.00753 134 ILE B CG2 
1431 C CD1 . ILE B 34  ? 0.36588 0.39764 0.35892 0.00307  0.00971  0.00133  134 ILE B CD1 
1432 N N   . GLU B 35  ? 0.24214 0.30165 0.21147 -0.01583 0.00023  0.00450  135 GLU B N   
1433 C CA  . GLU B 35  ? 0.27535 0.34954 0.24151 -0.01875 -0.00018 0.00725  135 GLU B CA  
1434 C C   . GLU B 35  ? 0.38326 0.46936 0.34871 -0.01515 0.00567  0.00315  135 GLU B C   
1435 O O   . GLU B 35  ? 0.31513 0.39665 0.28101 -0.01091 0.01000  -0.00523 135 GLU B O   
1436 C CB  . GLU B 35  ? 0.30425 0.37679 0.26497 -0.02248 -0.00255 0.00434  135 GLU B CB  
1437 C CG  . GLU B 35  ? 0.33649 0.42393 0.29447 -0.02711 -0.00506 0.01029  135 GLU B CG  
1438 C CD  . GLU B 35  ? 0.41122 0.49730 0.36431 -0.03070 -0.00778 0.00757  135 GLU B CD  
1439 O OE1 . GLU B 35  ? 0.34091 0.42951 0.28850 -0.02934 -0.00441 -0.00065 135 GLU B OE1 
1440 O OE2 . GLU B 35  ? 0.35587 0.43811 0.31161 -0.03474 -0.01336 0.01311  135 GLU B OE2 
1441 N N   . ARG B 36  ? 0.30283 0.40484 0.26837 -0.01688 0.00590  0.00906  136 ARG B N   
1442 C CA  . ARG B 36  ? 0.33324 0.44956 0.29795 -0.01395 0.01180  0.00503  136 ARG B CA  
1443 C C   . ARG B 36  ? 0.37814 0.50915 0.33560 -0.01856 0.01115  0.00631  136 ARG B C   
1444 O O   . ARG B 36  ? 0.43568 0.56235 0.38751 -0.02095 0.00930  0.00228  136 ARG B O   
1445 C CB  . ARG B 36  ? 0.33766 0.46113 0.30966 -0.01143 0.01349  0.01076  136 ARG B CB  
1446 C CG  . ARG B 36  ? 0.48716 0.59652 0.46598 -0.00721 0.01349  0.01002  136 ARG B CG  
1447 C CD  . ARG B 36  ? 0.70240 0.81026 0.68480 -0.00086 0.01969  0.00079  136 ARG B CD  
1448 N NE  . ARG B 36  ? 0.74947 0.86859 0.73910 0.00267  0.02319  0.00333  136 ARG B NE  
1449 C CZ  . ARG B 36  ? 0.86336 1.00006 0.85233 0.00315  0.02749  0.00177  136 ARG B CZ  
1450 N NH1 . ARG B 36  ? 0.74564 0.89163 0.72611 0.00012  0.02872  -0.00215 136 ARG B NH1 
1451 N NH2 . ARG B 36  ? 0.92908 1.07535 0.92615 0.00660  0.03065  0.00428  136 ARG B NH2 
1452 N N   . ASP B 37  ? 0.28184 0.43078 0.23957 -0.02029 0.01224  0.01268  137 ASP B N   
1453 C CA  . ASP B 37  ? 0.33672 0.50116 0.28715 -0.02528 0.01130  0.01515  137 ASP B CA  
1454 C C   . ASP B 37  ? 0.31781 0.47996 0.26920 -0.03159 0.00349  0.02617  137 ASP B C   
1455 O O   . ASP B 37  ? 0.34981 0.51773 0.29532 -0.03592 0.00090  0.02729  137 ASP B O   
1456 C CB  . ASP B 37  ? 0.33557 0.52238 0.28565 -0.02508 0.01602  0.01774  137 ASP B CB  
1457 C CG  . ASP B 37  ? 0.35164 0.54256 0.30195 -0.01870 0.02419  0.00542  137 ASP B CG  
1458 O OD1 . ASP B 37  ? 0.47527 0.65414 0.42419 -0.01534 0.02613  -0.00578 137 ASP B OD1 
1459 O OD2 . ASP B 37  ? 0.41546 0.62224 0.36854 -0.01709 0.02872  0.00692  137 ASP B OD2 
1460 N N   . THR B 38  ? 0.33379 0.48775 0.29332 -0.03228 -0.00059 0.03405  138 THR B N   
1461 C CA  . THR B 38  ? 0.31337 0.46443 0.27659 -0.03795 -0.00808 0.04380  138 THR B CA  
1462 C C   . THR B 38  ? 0.33722 0.47081 0.29913 -0.03849 -0.01153 0.03876  138 THR B C   
1463 O O   . THR B 38  ? 0.30961 0.42786 0.27366 -0.03500 -0.01077 0.03323  138 THR B O   
1464 C CB  . THR B 38  ? 0.41200 0.56025 0.38525 -0.03847 -0.01123 0.05227  138 THR B CB  
1465 O OG1 . THR B 38  ? 0.44242 0.60670 0.41784 -0.03753 -0.00758 0.05660  138 THR B OG1 
1466 C CG2 . THR B 38  ? 0.38077 0.52767 0.35994 -0.04455 -0.01900 0.06214  138 THR B CG2 
1467 N N   . GLY B 39  ? 0.33991 0.47652 0.29904 -0.04312 -0.01556 0.04150  139 GLY B N   
1468 C CA  . GLY B 39  ? 0.31214 0.43335 0.27096 -0.04381 -0.01881 0.03689  139 GLY B CA  
1469 C C   . GLY B 39  ? 0.27180 0.37937 0.23999 -0.04469 -0.02368 0.04112  139 GLY B C   
1470 O O   . GLY B 39  ? 0.35106 0.46301 0.32676 -0.04775 -0.02777 0.05061  139 GLY B O   
1471 N N   . MET B 40  ? 0.25929 0.35069 0.22753 -0.04222 -0.02325 0.03374  140 MET B N   
1472 C CA  . MET B 40  ? 0.30092 0.38032 0.27727 -0.04309 -0.02738 0.03615  140 MET B CA  
1473 C C   . MET B 40  ? 0.28912 0.35801 0.26730 -0.04538 -0.03125 0.03361  140 MET B C   
1474 O O   . MET B 40  ? 0.26316 0.31980 0.24590 -0.04483 -0.03276 0.03113  140 MET B O   
1475 C CB  . MET B 40  ? 0.37507 0.44572 0.35185 -0.03852 -0.02386 0.03146  140 MET B CB  
1476 C CG  . MET B 40  ? 0.43549 0.51493 0.41661 -0.03807 -0.02353 0.03793  140 MET B CG  
1477 S SD  . MET B 40  ? 0.42535 0.49650 0.40634 -0.03263 -0.01940 0.03278  140 MET B SD  
1478 C CE  . MET B 40  ? 0.35282 0.40803 0.33755 -0.03425 -0.02370 0.03073  140 MET B CE  
1479 N N   . GLY B 41  ? 0.27494 0.34986 0.25002 -0.04823 -0.03306 0.03453  141 GLY B N   
1480 C CA  . GLY B 41  ? 0.35597 0.42213 0.33400 -0.05051 -0.03703 0.03265  141 GLY B CA  
1481 C C   . GLY B 41  ? 0.30191 0.36088 0.29183 -0.05285 -0.04248 0.03741  141 GLY B C   
1482 O O   . GLY B 41  ? 0.29134 0.33853 0.28482 -0.05274 -0.04385 0.03269  141 GLY B O   
1483 N N   . ASP B 42  ? 0.27600 0.34245 0.27314 -0.05514 -0.04560 0.04644  142 ASP B N   
1484 C CA  . ASP B 42  ? 0.33565 0.39590 0.34611 -0.05766 -0.05125 0.05051  142 ASP B CA  
1485 C C   . ASP B 42  ? 0.32078 0.36797 0.33290 -0.05474 -0.04941 0.04307  142 ASP B C   
1486 O O   . ASP B 42  ? 0.35189 0.38998 0.37198 -0.05590 -0.05255 0.04055  142 ASP B O   
1487 C CB  . ASP B 42  ? 0.37346 0.44405 0.39206 -0.06046 -0.05457 0.06125  142 ASP B CB  
1488 C CG  . ASP B 42  ? 0.42353 0.50787 0.44305 -0.06463 -0.05783 0.07083  142 ASP B CG  
1489 O OD1 . ASP B 42  ? 0.46361 0.54747 0.48164 -0.06631 -0.05987 0.07011  142 ASP B OD1 
1490 O OD2 . ASP B 42  ? 0.52991 0.62633 0.55183 -0.06647 -0.05848 0.07953  142 ASP B OD2 
1491 N N   . TYR B 43  ? 0.24047 0.28741 0.24542 -0.05101 -0.04426 0.03942  143 TYR B N   
1492 C CA  . TYR B 43  ? 0.27226 0.30863 0.27758 -0.04852 -0.04250 0.03330  143 TYR B CA  
1493 C C   . TYR B 43  ? 0.29206 0.31878 0.29094 -0.04632 -0.03923 0.02462  143 TYR B C   
1494 O O   . TYR B 43  ? 0.26197 0.27936 0.26349 -0.04603 -0.03952 0.01996  143 TYR B O   
1495 C CB  . TYR B 43  ? 0.28365 0.32429 0.28561 -0.04563 -0.03904 0.03438  143 TYR B CB  
1496 C CG  . TYR B 43  ? 0.30808 0.35917 0.31683 -0.04806 -0.04213 0.04333  143 TYR B CG  
1497 C CD1 . TYR B 43  ? 0.27175 0.32070 0.29105 -0.05043 -0.04675 0.04629  143 TYR B CD1 
1498 C CD2 . TYR B 43  ? 0.33002 0.39379 0.33536 -0.04836 -0.04054 0.04859  143 TYR B CD2 
1499 C CE1 . TYR B 43  ? 0.35902 0.41737 0.38615 -0.05306 -0.04999 0.05500  143 TYR B CE1 
1500 C CE2 . TYR B 43  ? 0.35396 0.42828 0.36620 -0.05102 -0.04334 0.05775  143 TYR B CE2 
1501 C CZ  . TYR B 43  ? 0.37941 0.45048 0.40299 -0.05341 -0.04824 0.06126  143 TYR B CZ  
1502 O OH  . TYR B 43  ? 0.45694 0.53833 0.48879 -0.05637 -0.05131 0.07081  143 TYR B OH  
1503 N N   . ILE B 44  ? 0.22593 0.25545 0.21676 -0.04499 -0.03608 0.02209  144 ILE B N   
1504 C CA  . ILE B 44  ? 0.27641 0.29687 0.26248 -0.04335 -0.03340 0.01417  144 ILE B CA  
1505 C C   . ILE B 44  ? 0.24687 0.26094 0.23939 -0.04626 -0.03745 0.01290  144 ILE B C   
1506 O O   . ILE B 44  ? 0.27481 0.27933 0.26735 -0.04537 -0.03606 0.00694  144 ILE B O   
1507 C CB  . ILE B 44  ? 0.24943 0.27529 0.22716 -0.04203 -0.03007 0.01135  144 ILE B CB  
1508 C CG1 . ILE B 44  ? 0.23423 0.26370 0.20706 -0.03803 -0.02493 0.00996  144 ILE B CG1 
1509 C CG2 . ILE B 44  ? 0.28419 0.30165 0.25916 -0.04167 -0.02888 0.00411  144 ILE B CG2 
1510 C CD1 . ILE B 44  ? 0.26174 0.29993 0.22751 -0.03683 -0.02155 0.00704  144 ILE B CD1 
1511 N N   . GLU B 45  ? 0.27449 0.29426 0.27367 -0.04985 -0.04256 0.01896  145 GLU B N   
1512 C CA  . GLU B 45  ? 0.29879 0.31315 0.30607 -0.05245 -0.04671 0.01804  145 GLU B CA  
1513 C C   . GLU B 45  ? 0.28721 0.29374 0.30365 -0.05273 -0.04836 0.01576  145 GLU B C   
1514 O O   . GLU B 45  ? 0.34858 0.34918 0.37203 -0.05405 -0.05055 0.01266  145 GLU B O   
1515 C CB  . GLU B 45  ? 0.33732 0.36041 0.35107 -0.05635 -0.05234 0.02634  145 GLU B CB  
1516 C CG  . GLU B 45  ? 0.52051 0.55260 0.52511 -0.05703 -0.05138 0.02775  145 GLU B CG  
1517 C CD  . GLU B 45  ? 0.72604 0.75223 0.72588 -0.05642 -0.04990 0.02030  145 GLU B CD  
1518 O OE1 . GLU B 45  ? 0.79717 0.81255 0.80189 -0.05583 -0.04994 0.01500  145 GLU B OE1 
1519 O OE2 . GLU B 45  ? 0.81766 0.85101 0.80902 -0.05677 -0.04865 0.01950  145 GLU B OE2 
1520 N N   . THR B 46  ? 0.26098 0.26807 0.27785 -0.05158 -0.04734 0.01667  146 THR B N   
1521 C CA  . THR B 46  ? 0.28632 0.28708 0.31095 -0.05205 -0.04873 0.01312  146 THR B CA  
1522 C C   . THR B 46  ? 0.30841 0.30140 0.32653 -0.04967 -0.04410 0.00501  146 THR B C   
1523 O O   . THR B 46  ? 0.32673 0.31520 0.35012 -0.05028 -0.04471 0.00071  146 THR B O   
1524 C CB  . THR B 46  ? 0.28635 0.29142 0.31474 -0.05236 -0.05018 0.01713  146 THR B CB  
1525 O OG1 . THR B 46  ? 0.30670 0.31342 0.32453 -0.04923 -0.04540 0.01630  146 THR B OG1 
1526 C CG2 . THR B 46  ? 0.28001 0.29389 0.31564 -0.05507 -0.05472 0.02660  146 THR B CG2 
1527 N N   . GLY B 47  ? 0.27664 0.22589 0.28474 -0.03411 -0.00903 -0.00221 147 GLY B N   
1528 C CA  . GLY B 47  ? 0.24561 0.19957 0.24858 -0.03374 -0.00939 -0.00706 147 GLY B CA  
1529 C C   . GLY B 47  ? 0.33821 0.29116 0.34203 -0.03037 -0.01069 -0.00551 147 GLY B C   
1530 O O   . GLY B 47  ? 0.32396 0.27253 0.33345 -0.02882 -0.01171 -0.00130 147 GLY B O   
1531 N N   . ILE B 48  ? 0.26389 0.22208 0.26408 -0.02935 -0.01088 -0.00768 148 ILE B N   
1532 C CA  . ILE B 48  ? 0.29403 0.25267 0.29709 -0.02646 -0.01271 -0.00528 148 ILE B CA  
1533 C C   . ILE B 48  ? 0.26679 0.22554 0.26279 -0.02612 -0.01676 -0.00141 148 ILE B C   
1534 O O   . ILE B 48  ? 0.27682 0.23922 0.26631 -0.02666 -0.01585 -0.00239 148 ILE B O   
1535 C CB  . ILE B 48  ? 0.26372 0.22815 0.26804 -0.02503 -0.01015 -0.00855 148 ILE B CB  
1536 C CG1 . ILE B 48  ? 0.34264 0.30505 0.34962 -0.02519 -0.00533 -0.01403 148 ILE B CG1 
1537 C CG2 . ILE B 48  ? 0.30515 0.27063 0.31600 -0.02208 -0.01235 -0.00434 148 ILE B CG2 
1538 C CD1 . ILE B 48  ? 0.43266 0.38773 0.45009 -0.02309 -0.00326 -0.01227 148 ILE B CD1 
1539 N N   . PRO B 49  ? 0.27608 0.23073 0.27287 -0.02537 -0.02115 0.00300  149 PRO B N   
1540 C CA  . PRO B 49  ? 0.27937 0.23186 0.26570 -0.02550 -0.02526 0.00490  149 PRO B CA  
1541 C C   . PRO B 49  ? 0.34071 0.29606 0.32748 -0.02492 -0.02668 0.00313  149 PRO B C   
1542 O O   . PRO B 49  ? 0.30416 0.26235 0.30153 -0.02396 -0.02771 0.00379  149 PRO B O   
1543 C CB  . PRO B 49  ? 0.30390 0.25220 0.29149 -0.02553 -0.03097 0.01020  149 PRO B CB  
1544 C CG  . PRO B 49  ? 0.38583 0.33561 0.38927 -0.02469 -0.02980 0.01196  149 PRO B CG  
1545 C CD  . PRO B 49  ? 0.32906 0.28057 0.33601 -0.02460 -0.02253 0.00685  149 PRO B CD  
1546 N N   . LEU B 50  ? 0.29187 0.24628 0.26878 -0.02509 -0.02569 0.00170  150 LEU B N   
1547 C CA  . LEU B 50  ? 0.28273 0.23847 0.26070 -0.02461 -0.02652 0.00037  150 LEU B CA  
1548 C C   . LEU B 50  ? 0.32200 0.26919 0.28799 -0.02531 -0.03067 -0.00034 150 LEU B C   
1549 O O   . LEU B 50  ? 0.30646 0.25123 0.27575 -0.02610 -0.03618 -0.00081 150 LEU B O   
1550 C CB  . LEU B 50  ? 0.28377 0.24641 0.26284 -0.02393 -0.01997 -0.00086 150 LEU B CB  
1551 C CG  . LEU B 50  ? 0.35656 0.32884 0.34681 -0.02304 -0.01721 -0.00098 150 LEU B CG  
1552 C CD1 . LEU B 50  ? 0.38091 0.35464 0.37247 -0.02383 -0.01549 -0.00230 150 LEU B CD1 
1553 C CD2 . LEU B 50  ? 0.52932 0.50939 0.52072 -0.02247 -0.01254 -0.00028 150 LEU B CD2 
1554 N N   . ASN B 51  ? 0.31612 0.25815 0.26816 -0.02506 -0.02806 -0.00041 151 ASN B N   
1555 C CA  . ASN B 51  ? 0.30667 0.23873 0.24237 -0.02518 -0.03028 -0.00221 151 ASN B CA  
1556 C C   . ASN B 51  ? 0.35286 0.28245 0.29034 -0.02536 -0.03041 -0.00595 151 ASN B C   
1557 O O   . ASN B 51  ? 0.35930 0.28125 0.29104 -0.02710 -0.03717 -0.00863 151 ASN B O   
1558 C CB  . ASN B 51  ? 0.35464 0.28150 0.28369 -0.02684 -0.03925 -0.00039 151 ASN B CB  
1559 C CG  . ASN B 51  ? 0.45484 0.38417 0.38440 -0.02618 -0.03797 0.00455  151 ASN B CG  
1560 O OD1 . ASN B 51  ? 0.54669 0.47991 0.48812 -0.02697 -0.04191 0.00802  151 ASN B OD1 
1561 N ND2 . ASN B 51  ? 0.45002 0.37718 0.36919 -0.02438 -0.03142 0.00580  151 ASN B ND2 
1562 N N   . ALA B 52  ? 0.30116 0.23760 0.24770 -0.02389 -0.02323 -0.00571 152 ALA B N   
1563 C CA  . ALA B 52  ? 0.32554 0.26291 0.28085 -0.02363 -0.02235 -0.00736 152 ALA B CA  
1564 C C   . ALA B 52  ? 0.42536 0.35663 0.37231 -0.02195 -0.01478 -0.00907 152 ALA B C   
1565 O O   . ALA B 52  ? 0.35737 0.28754 0.29550 -0.02039 -0.00840 -0.00743 152 ALA B O   
1566 C CB  . ALA B 52  ? 0.30111 0.25240 0.27484 -0.02264 -0.01937 -0.00420 152 ALA B CB  
1567 N N   . LYS B 53  ? 0.32284 0.24967 0.27464 -0.02209 -0.01494 -0.01176 153 LYS B N   
1568 C CA  . LYS B 53  ? 0.32110 0.24299 0.27035 -0.01986 -0.00568 -0.01265 153 LYS B CA  
1569 C C   . LYS B 53  ? 0.29336 0.23034 0.25738 -0.01765 0.00277  -0.00600 153 LYS B C   
1570 O O   . LYS B 53  ? 0.32533 0.27573 0.30345 -0.01808 0.00071  -0.00245 153 LYS B O   
1571 C CB  . LYS B 53  ? 0.32420 0.23790 0.27928 -0.02081 -0.00767 -0.01702 153 LYS B CB  
1572 C CG  . LYS B 53  ? 0.43888 0.33612 0.37702 -0.02404 -0.01707 -0.02452 153 LYS B CG  
1573 C CD  . LYS B 53  ? 0.53877 0.42460 0.48073 -0.02539 -0.01771 -0.03036 153 LYS B CD  
1574 C CE  . LYS B 53  ? 0.68400 0.55278 0.60579 -0.02975 -0.02881 -0.03877 153 LYS B CE  
1575 N NZ  . LYS B 53  ? 0.81832 0.67845 0.75079 -0.03328 -0.03487 -0.04419 153 LYS B NZ  
1576 N N   . VAL B 54  ? 0.35067 0.28533 0.31098 -0.01520 0.01245  -0.00386 154 VAL B N   
1577 C CA  . VAL B 54  ? 0.32653 0.27613 0.30099 -0.01363 0.01993  0.00391  154 VAL B CA  
1578 C C   . VAL B 54  ? 0.31667 0.27325 0.30960 -0.01256 0.02294  0.00663  154 VAL B C   
1579 O O   . VAL B 54  ? 0.34184 0.28730 0.33530 -0.01166 0.02531  0.00304  154 VAL B O   
1580 C CB  . VAL B 54  ? 0.32482 0.26992 0.29210 -0.01100 0.02992  0.00744  154 VAL B CB  
1581 C CG1 . VAL B 54  ? 0.43018 0.39263 0.41477 -0.01021 0.03620  0.01718  154 VAL B CG1 
1582 C CG2 . VAL B 54  ? 0.37133 0.31008 0.32196 -0.01140 0.02781  0.00626  154 VAL B CG2 
1583 N N   . SER B 55  ? 0.27918 0.25396 0.28716 -0.01272 0.02288  0.01298  155 SER B N   
1584 C CA  . SER B 55  ? 0.29394 0.27959 0.32123 -0.01079 0.02829  0.01933  155 SER B CA  
1585 C C   . SER B 55  ? 0.26969 0.27558 0.30566 -0.01107 0.03002  0.02782  155 SER B C   
1586 O O   . SER B 55  ? 0.29724 0.30812 0.32593 -0.01335 0.02479  0.02654  155 SER B O   
1587 C CB  . SER B 55  ? 0.31349 0.30054 0.35221 -0.01091 0.02330  0.01775  155 SER B CB  
1588 O OG  . SER B 55  ? 0.27009 0.26487 0.30773 -0.01239 0.01600  0.01713  155 SER B OG  
1589 N N   . SER B 56  ? 0.24422 0.26164 0.29623 -0.00904 0.03714  0.03664  156 SER B N   
1590 C CA  . SER B 56  ? 0.21175 0.25049 0.27219 -0.00999 0.03707  0.04544  156 SER B CA  
1591 C C   . SER B 56  ? 0.25349 0.30238 0.31549 -0.01083 0.03043  0.04420  156 SER B C   
1592 O O   . SER B 56  ? 0.23385 0.29348 0.29080 -0.01316 0.02639  0.04509  156 SER B O   
1593 C CB  . SER B 56  ? 0.27632 0.32698 0.35586 -0.00742 0.04588  0.05708  156 SER B CB  
1594 O OG  . SER B 56  ? 0.34121 0.39144 0.43435 -0.00473 0.04842  0.05814  156 SER B OG  
1595 N N   . GLU B 57  ? 0.24572 0.28971 0.31414 -0.00903 0.02928  0.04159  157 GLU B N   
1596 C CA  . GLU B 57  ? 0.24248 0.29587 0.31464 -0.00851 0.02500  0.04199  157 GLU B CA  
1597 C C   . GLU B 57  ? 0.28921 0.33643 0.34537 -0.01101 0.01811  0.03405  157 GLU B C   
1598 O O   . GLU B 57  ? 0.22788 0.28565 0.28110 -0.01144 0.01615  0.03486  157 GLU B O   
1599 C CB  . GLU B 57  ? 0.24593 0.29403 0.33158 -0.00612 0.02527  0.04189  157 GLU B CB  
1600 C CG  . GLU B 57  ? 0.30035 0.35691 0.40641 -0.00315 0.03283  0.05105  157 GLU B CG  
1601 C CD  . GLU B 57  ? 0.37480 0.41593 0.48225 -0.00305 0.03780  0.04836  157 GLU B CD  
1602 O OE1 . GLU B 57  ? 0.31117 0.33636 0.40095 -0.00514 0.03577  0.04003  157 GLU B OE1 
1603 O OE2 . GLU B 57  ? 0.39572 0.44039 0.52223 -0.00044 0.04463  0.05492  157 GLU B OE2 
1604 N N   . LEU B 58  ? 0.24665 0.27646 0.29185 -0.01255 0.01476  0.02642  158 LEU B N   
1605 C CA  . LEU B 58  ? 0.21970 0.24417 0.25270 -0.01463 0.00899  0.02038  158 LEU B CA  
1606 C C   . LEU B 58  ? 0.26630 0.29731 0.29120 -0.01706 0.00915  0.02087  158 LEU B C   
1607 O O   . LEU B 58  ? 0.23268 0.26747 0.25291 -0.01834 0.00622  0.01830  158 LEU B O   
1608 C CB  . LEU B 58  ? 0.25641 0.26269 0.27975 -0.01580 0.00508  0.01392  158 LEU B CB  
1609 C CG  . LEU B 58  ? 0.27931 0.27956 0.29214 -0.01774 -0.00030 0.00918  158 LEU B CG  
1610 C CD1 . LEU B 58  ? 0.31345 0.31990 0.33275 -0.01689 -0.00267 0.00936  158 LEU B CD1 
1611 C CD2 . LEU B 58  ? 0.28660 0.27068 0.29027 -0.01875 -0.00465 0.00466  158 LEU B CD2 
1612 N N   . LEU B 59  ? 0.24291 0.27486 0.26728 -0.01776 0.01286  0.02435  159 LEU B N   
1613 C CA  . LEU B 59  ? 0.27586 0.31487 0.29590 -0.02082 0.01209  0.02607  159 LEU B CA  
1614 C C   . LEU B 59  ? 0.26179 0.31800 0.28564 -0.02199 0.01060  0.02935  159 LEU B C   
1615 O O   . LEU B 59  ? 0.23759 0.29602 0.25395 -0.02515 0.00653  0.02559  159 LEU B O   
1616 C CB  . LEU B 59  ? 0.24472 0.28439 0.26848 -0.02061 0.01755  0.03228  159 LEU B CB  
1617 C CG  . LEU B 59  ? 0.27930 0.30158 0.29364 -0.01977 0.01948  0.02865  159 LEU B CG  
1618 C CD1 . LEU B 59  ? 0.27365 0.29630 0.29328 -0.01804 0.02754  0.03595  159 LEU B CD1 
1619 C CD2 . LEU B 59  ? 0.24607 0.26264 0.25008 -0.02262 0.01438  0.02385  159 LEU B CD2 
1620 N N   . ILE B 60  ? 0.24527 0.31352 0.28039 -0.01946 0.01405  0.03637  160 ILE B N   
1621 C CA  . ILE B 60  ? 0.22941 0.31527 0.26617 -0.01999 0.01286  0.04046  160 ILE B CA  
1622 C C   . ILE B 60  ? 0.25945 0.34192 0.28793 -0.01928 0.00983  0.03327  160 ILE B C   
1623 O O   . ILE B 60  ? 0.25722 0.34534 0.27624 -0.02179 0.00688  0.03024  160 ILE B O   
1624 C CB  . ILE B 60  ? 0.24288 0.34266 0.29553 -0.01642 0.01809  0.05112  160 ILE B CB  
1625 C CG1 . ILE B 60  ? 0.26155 0.36770 0.32380 -0.01729 0.02202  0.06008  160 ILE B CG1 
1626 C CG2 . ILE B 60  ? 0.27797 0.39569 0.32973 -0.01595 0.01686  0.05525  160 ILE B CG2 
1627 C CD1 . ILE B 60  ? 0.24190 0.35467 0.32312 -0.01291 0.02933  0.06978  160 ILE B CD1 
1628 N N   . ASN B 61  ? 0.24751 0.31988 0.27977 -0.01600 0.01061  0.03039  161 ASN B N   
1629 C CA  . ASN B 61  ? 0.19883 0.26889 0.22707 -0.01429 0.00936  0.02589  161 ASN B CA  
1630 C C   . ASN B 61  ? 0.27270 0.33300 0.28728 -0.01765 0.00566  0.01711  161 ASN B C   
1631 O O   . ASN B 61  ? 0.26883 0.33066 0.27706 -0.01712 0.00577  0.01348  161 ASN B O   
1632 C CB  . ASN B 61  ? 0.22560 0.28707 0.26406 -0.01082 0.00987  0.02610  161 ASN B CB  
1633 C CG  . ASN B 61  ? 0.19996 0.27404 0.25295 -0.00622 0.01407  0.03432  161 ASN B CG  
1634 O OD1 . ASN B 61  ? 0.25768 0.33900 0.32195 -0.00507 0.01716  0.04122  161 ASN B OD1 
1635 N ND2 . ASN B 61  ? 0.22044 0.29724 0.27467 -0.00306 0.01526  0.03453  161 ASN B ND2 
1636 N N   . ILE B 62  ? 0.23557 0.28562 0.24589 -0.02070 0.00337  0.01401  162 ILE B N   
1637 C CA  . ILE B 62  ? 0.20633 0.24708 0.20699 -0.02383 0.00030  0.00683  162 ILE B CA  
1638 C C   . ILE B 62  ? 0.23178 0.28107 0.22525 -0.02760 -0.00118 0.00487  162 ILE B C   
1639 O O   . ILE B 62  ? 0.23886 0.28294 0.22490 -0.02906 -0.00240 -0.00204 162 ILE B O   
1640 C CB  . ILE B 62  ? 0.24443 0.27415 0.24324 -0.02565 -0.00104 0.00610  162 ILE B CB  
1641 C CG1 . ILE B 62  ? 0.22842 0.24687 0.22948 -0.02296 -0.00162 0.00533  162 ILE B CG1 
1642 C CG2 . ILE B 62  ? 0.29003 0.31356 0.28207 -0.02940 -0.00367 0.00097  162 ILE B CG2 
1643 C CD1 . ILE B 62  ? 0.27254 0.28142 0.26946 -0.02370 -0.00160 0.00589  162 ILE B CD1 
1644 N N   . PHE B 63  ? 0.27621 0.33845 0.27225 -0.02953 -0.00127 0.01094  163 PHE B N   
1645 C CA  . PHE B 63  ? 0.23426 0.30447 0.22361 -0.03486 -0.00500 0.00946  163 PHE B CA  
1646 C C   . PHE B 63  ? 0.23332 0.31696 0.21671 -0.03440 -0.00507 0.01007  163 PHE B C   
1647 O O   . PHE B 63  ? 0.28309 0.37403 0.25873 -0.03960 -0.00947 0.00831  163 PHE B O   
1648 C CB  . PHE B 63  ? 0.24511 0.32317 0.24172 -0.03808 -0.00605 0.01735  163 PHE B CB  
1649 C CG  . PHE B 63  ? 0.22808 0.29326 0.22665 -0.03945 -0.00613 0.01612  163 PHE B CG  
1650 C CD1 . PHE B 63  ? 0.24039 0.29715 0.23347 -0.04373 -0.01001 0.00936  163 PHE B CD1 
1651 C CD2 . PHE B 63  ? 0.24055 0.30175 0.24632 -0.03620 -0.00165 0.02190  163 PHE B CD2 
1652 C CE1 . PHE B 63  ? 0.22463 0.27080 0.22047 -0.04433 -0.00942 0.00984  163 PHE B CE1 
1653 C CE2 . PHE B 63  ? 0.25257 0.30213 0.25779 -0.03666 -0.00079 0.02139  163 PHE B CE2 
1654 C CZ  . PHE B 63  ? 0.21032 0.25349 0.21124 -0.04057 -0.00470 0.01625  163 PHE B CZ  
1655 N N   . ILE B 64  ? 0.26561 0.35272 0.25224 -0.02853 -0.00062 0.01276  164 ILE B N   
1656 C CA  . ILE B 64  ? 0.26604 0.36613 0.24572 -0.02680 0.00071  0.01428  164 ILE B CA  
1657 C C   . ILE B 64  ? 0.28070 0.37420 0.24259 -0.03035 -0.00196 0.00300  164 ILE B C   
1658 O O   . ILE B 64  ? 0.30214 0.37922 0.26082 -0.02994 -0.00103 -0.00552 164 ILE B O   
1659 C CB  . ILE B 64  ? 0.29296 0.39458 0.28054 -0.01909 0.00693  0.01850  164 ILE B CB  
1660 C CG1 . ILE B 64  ? 0.32125 0.42869 0.32729 -0.01622 0.00945  0.02889  164 ILE B CG1 
1661 C CG2 . ILE B 64  ? 0.27267 0.38792 0.25088 -0.01640 0.00958  0.02062  164 ILE B CG2 
1662 C CD1 . ILE B 64  ? 0.36130 0.48801 0.37280 -0.01774 0.00924  0.03933  164 ILE B CD1 
1663 N N   . PRO B 65  ? 0.29189 0.39730 0.24201 -0.03435 -0.00558 0.00256  165 PRO B N   
1664 C CA  . PRO B 65  ? 0.35686 0.45374 0.28833 -0.03883 -0.00866 -0.01009 165 PRO B CA  
1665 C C   . PRO B 65  ? 0.32694 0.41298 0.24994 -0.03263 -0.00147 -0.01730 165 PRO B C   
1666 O O   . PRO B 65  ? 0.34820 0.44052 0.27585 -0.02523 0.00496  -0.01084 165 PRO B O   
1667 C CB  . PRO B 65  ? 0.32929 0.44441 0.24936 -0.04354 -0.01411 -0.00699 165 PRO B CB  
1668 C CG  . PRO B 65  ? 0.38440 0.51574 0.32249 -0.04398 -0.01578 0.00796  165 PRO B CG  
1669 C CD  . PRO B 65  ? 0.32643 0.45335 0.28068 -0.03586 -0.00787 0.01394  165 PRO B CD  
1670 N N   . ASN B 66  ? 0.37762 0.44702 0.29047 -0.03551 -0.00192 -0.02996 166 ASN B N   
1671 C CA  . ASN B 66  ? 0.40210 0.45906 0.30588 -0.03022 0.00574  -0.03800 166 ASN B CA  
1672 C C   . ASN B 66  ? 0.42936 0.47793 0.35025 -0.02290 0.01222  -0.03331 166 ASN B C   
1673 O O   . ASN B 66  ? 0.45581 0.49898 0.37488 -0.01627 0.02028  -0.03466 166 ASN B O   
1674 C CB  . ASN B 66  ? 0.41261 0.48055 0.29985 -0.02626 0.01013  -0.03746 166 ASN B CB  
1675 C CG  . ASN B 66  ? 0.72921 0.80816 0.59816 -0.03408 0.00198  -0.04083 166 ASN B CG  
1676 O OD1 . ASN B 66  ? 0.70434 0.77538 0.56672 -0.04268 -0.00542 -0.04994 166 ASN B OD1 
1677 N ND2 . ASN B 66  ? 0.70580 0.80397 0.56778 -0.03139 0.00277  -0.03250 166 ASN B ND2 
1678 N N   . THR B 67  ? 0.31305 0.36040 0.25031 -0.02398 0.00889  -0.02742 167 THR B N   
1679 C CA  . THR B 67  ? 0.32190 0.36154 0.27480 -0.01863 0.01250  -0.02300 167 THR B CA  
1680 C C   . THR B 67  ? 0.34320 0.36615 0.29991 -0.02140 0.01064  -0.02889 167 THR B C   
1681 O O   . THR B 67  ? 0.34586 0.36440 0.29703 -0.02770 0.00607  -0.03452 167 THR B O   
1682 C CB  . THR B 67  ? 0.34417 0.39334 0.31141 -0.01747 0.01033  -0.01227 167 THR B CB  
1683 O OG1 . THR B 67  ? 0.31053 0.36026 0.27813 -0.02362 0.00432  -0.01216 167 THR B OG1 
1684 C CG2 . THR B 67  ? 0.35685 0.42358 0.32471 -0.01395 0.01313  -0.00429 167 THR B CG2 
1685 N N   . PRO B 68  ? 0.31201 0.32634 0.28027 -0.01694 0.01372  -0.02635 168 PRO B N   
1686 C CA  . PRO B 68  ? 0.32588 0.32584 0.29894 -0.01918 0.01213  -0.03011 168 PRO B CA  
1687 C C   . PRO B 68  ? 0.33291 0.33221 0.30787 -0.02473 0.00539  -0.02893 168 PRO B C   
1688 O O   . PRO B 68  ? 0.36853 0.35859 0.34247 -0.02846 0.00382  -0.03388 168 PRO B O   
1689 C CB  . PRO B 68  ? 0.28851 0.28450 0.27602 -0.01349 0.01487  -0.02370 168 PRO B CB  
1690 C CG  . PRO B 68  ? 0.40230 0.40620 0.39021 -0.00757 0.02107  -0.02034 168 PRO B CG  
1691 C CD  . PRO B 68  ? 0.30406 0.32140 0.28142 -0.00953 0.01952  -0.02006 168 PRO B CD  
1692 N N   . LEU B 69  ? 0.35629 0.36457 0.33503 -0.02494 0.00245  -0.02209 169 LEU B N   
1693 C CA  . LEU B 69  ? 0.32089 0.32704 0.30217 -0.02851 -0.00186 -0.01967 169 LEU B CA  
1694 C C   . LEU B 69  ? 0.31465 0.32886 0.29086 -0.03367 -0.00480 -0.01975 169 LEU B C   
1695 O O   . LEU B 69  ? 0.33415 0.34719 0.31344 -0.03606 -0.00706 -0.01655 169 LEU B O   
1696 C CB  . LEU B 69  ? 0.28705 0.29526 0.27571 -0.02561 -0.00253 -0.01249 169 LEU B CB  
1697 C CG  . LEU B 69  ? 0.29529 0.29562 0.29136 -0.02198 -0.00241 -0.01072 169 LEU B CG  
1698 C CD1 . LEU B 69  ? 0.28805 0.28978 0.28955 -0.02048 -0.00438 -0.00519 169 LEU B CD1 
1699 C CD2 . LEU B 69  ? 0.27309 0.26191 0.26928 -0.02362 -0.00406 -0.01317 169 LEU B CD2 
1700 N N   . HIS B 70  ? 0.33716 0.35987 0.30579 -0.03544 -0.00490 -0.02247 170 HIS B N   
1701 C CA  . HIS B 70  ? 0.29448 0.32901 0.26155 -0.04015 -0.00873 -0.01900 170 HIS B CA  
1702 C C   . HIS B 70  ? 0.35753 0.38723 0.32270 -0.04712 -0.01338 -0.02361 170 HIS B C   
1703 O O   . HIS B 70  ? 0.41753 0.45568 0.38659 -0.05116 -0.01693 -0.01826 170 HIS B O   
1704 C CB  . HIS B 70  ? 0.32447 0.37306 0.28424 -0.03969 -0.00831 -0.01792 170 HIS B CB  
1705 C CG  . HIS B 70  ? 0.40949 0.45644 0.35506 -0.04399 -0.01057 -0.02743 170 HIS B CG  
1706 N ND1 . HIS B 70  ? 0.44096 0.47430 0.37945 -0.04227 -0.00701 -0.03709 170 HIS B ND1 
1707 C CD2 . HIS B 70  ? 0.48561 0.54227 0.42238 -0.05022 -0.01615 -0.02897 170 HIS B CD2 
1708 C CE1 . HIS B 70  ? 0.45825 0.49115 0.38238 -0.04714 -0.00969 -0.04569 170 HIS B CE1 
1709 N NE2 . HIS B 70  ? 0.44694 0.49435 0.36910 -0.05245 -0.01620 -0.04108 170 HIS B NE2 
1710 N N   . ASP B 71  ? 0.31670 0.33319 0.27883 -0.04854 -0.01306 -0.03224 171 ASP B N   
1711 C CA  . ASP B 71  ? 0.44483 0.45575 0.40812 -0.05538 -0.01746 -0.03661 171 ASP B CA  
1712 C C   . ASP B 71  ? 0.33969 0.34139 0.31393 -0.05428 -0.01646 -0.03258 171 ASP B C   
1713 O O   . ASP B 71  ? 0.43594 0.43042 0.41303 -0.04897 -0.01265 -0.03131 171 ASP B O   
1714 C CB  . ASP B 71  ? 0.51584 0.51652 0.47008 -0.05801 -0.01711 -0.04901 171 ASP B CB  
1715 C CG  . ASP B 71  ? 0.56177 0.57168 0.50208 -0.06242 -0.02095 -0.05400 171 ASP B CG  
1716 O OD1 . ASP B 71  ? 0.47325 0.49748 0.41482 -0.06649 -0.02657 -0.04754 171 ASP B OD1 
1717 O OD2 . ASP B 71  ? 0.52898 0.53199 0.45678 -0.06163 -0.01803 -0.06384 171 ASP B OD2 
1718 N N   . GLY B 72  ? 0.35466 0.35747 0.33544 -0.05932 -0.02013 -0.02959 172 GLY B N   
1719 C CA  . GLY B 72  ? 0.30053 0.29690 0.29081 -0.05767 -0.01852 -0.02361 172 GLY B CA  
1720 C C   . GLY B 72  ? 0.34377 0.34817 0.33695 -0.05453 -0.01686 -0.01324 172 GLY B C   
1721 O O   . GLY B 72  ? 0.28981 0.30502 0.28045 -0.05352 -0.01674 -0.00995 172 GLY B O   
1722 N N   . ALA B 73  ? 0.24735 0.24592 0.24597 -0.05250 -0.01469 -0.00762 173 ALA B N   
1723 C CA  . ALA B 73  ? 0.28401 0.28727 0.28428 -0.04932 -0.01166 0.00157  173 ALA B CA  
1724 C C   . ALA B 73  ? 0.28685 0.28486 0.28097 -0.04315 -0.00846 0.00201  173 ALA B C   
1725 O O   . ALA B 73  ? 0.24280 0.23162 0.23450 -0.04111 -0.00856 -0.00142 173 ALA B O   
1726 C CB  . ALA B 73  ? 0.26719 0.26713 0.27507 -0.04999 -0.01009 0.00836  173 ALA B CB  
1727 N N   . VAL B 74  ? 0.22876 0.23268 0.22197 -0.04052 -0.00588 0.00678  174 VAL B N   
1728 C CA  . VAL B 74  ? 0.21773 0.21489 0.20590 -0.03545 -0.00290 0.00837  174 VAL B CA  
1729 C C   . VAL B 74  ? 0.25082 0.24248 0.23809 -0.03391 0.00073  0.01417  174 VAL B C   
1730 O O   . VAL B 74  ? 0.23065 0.22842 0.22408 -0.03520 0.00320  0.02023  174 VAL B O   
1731 C CB  . VAL B 74  ? 0.23897 0.24340 0.22812 -0.03322 -0.00068 0.01063  174 VAL B CB  
1732 C CG1 . VAL B 74  ? 0.25943 0.25508 0.24349 -0.02895 0.00258  0.01205  174 VAL B CG1 
1733 C CG2 . VAL B 74  ? 0.25466 0.26374 0.24404 -0.03322 -0.00319 0.00595  174 VAL B CG2 
1734 N N   . ILE B 75  ? 0.22770 0.20862 0.20758 -0.03101 0.00120  0.01344  175 ILE B N   
1735 C CA  . ILE B 75  ? 0.23506 0.20985 0.21030 -0.02830 0.00577  0.01906  175 ILE B CA  
1736 C C   . ILE B 75  ? 0.24056 0.20824 0.20439 -0.02426 0.00817  0.01809  175 ILE B C   
1737 O O   . ILE B 75  ? 0.28648 0.24917 0.24466 -0.02380 0.00385  0.01319  175 ILE B O   
1738 C CB  . ILE B 75  ? 0.24097 0.20920 0.21555 -0.02844 0.00432  0.02003  175 ILE B CB  
1739 C CG1 . ILE B 75  ? 0.25853 0.23217 0.24614 -0.03308 0.00215  0.02011  175 ILE B CG1 
1740 C CG2 . ILE B 75  ? 0.25089 0.21313 0.21823 -0.02446 0.01021  0.02692  175 ILE B CG2 
1741 C CD1 . ILE B 75  ? 0.28947 0.25704 0.28096 -0.03350 0.00106  0.02117  175 ILE B CD1 
1742 N N   . MET B 76  ? 0.24495 0.21176 0.20659 -0.02154 0.01515  0.02292  176 MET B N   
1743 C CA  . MET B 76  ? 0.25417 0.21194 0.20405 -0.01778 0.01893  0.02122  176 MET B CA  
1744 C C   . MET B 76  ? 0.32302 0.26977 0.25884 -0.01420 0.02355  0.02390  176 MET B C   
1745 O O   . MET B 76  ? 0.33493 0.28365 0.27459 -0.01337 0.02769  0.03061  176 MET B O   
1746 C CB  . MET B 76  ? 0.27343 0.23640 0.23046 -0.01625 0.02579  0.02479  176 MET B CB  
1747 C CG  . MET B 76  ? 0.29325 0.26645 0.26106 -0.01860 0.02188  0.02252  176 MET B CG  
1748 S SD  . MET B 76  ? 0.37244 0.35366 0.35198 -0.01650 0.03040  0.02918  176 MET B SD  
1749 C CE  . MET B 76  ? 0.42816 0.39069 0.39296 -0.01128 0.03831  0.02645  176 MET B CE  
1750 N N   . LYS B 77  ? 0.32133 0.25655 0.24080 -0.01224 0.02239  0.01883  177 LYS B N   
1751 C CA  . LYS B 77  ? 0.38119 0.30436 0.28195 -0.00804 0.02810  0.02033  177 LYS B CA  
1752 C C   . LYS B 77  ? 0.34160 0.25609 0.23377 -0.00513 0.03496  0.01696  177 LYS B C   
1753 O O   . LYS B 77  ? 0.53210 0.45201 0.43660 -0.00634 0.03553  0.01545  177 LYS B O   
1754 C CB  . LYS B 77  ? 0.37229 0.28858 0.25891 -0.00889 0.01989  0.01715  177 LYS B CB  
1755 C CG  . LYS B 77  ? 0.34006 0.26415 0.23807 -0.01094 0.01574  0.02187  177 LYS B CG  
1756 C CD  . LYS B 77  ? 0.40970 0.32961 0.29869 -0.01193 0.00742  0.02069  177 LYS B CD  
1757 C CE  . LYS B 77  ? 0.39401 0.30337 0.25914 -0.00806 0.01049  0.02260  177 LYS B CE  
1758 N NZ  . LYS B 77  ? 0.54968 0.45926 0.41042 -0.00850 0.00410  0.02669  177 LYS B NZ  
1759 N N   . ASN B 78  ? 0.47103 0.37176 0.34204 -0.00097 0.04104  0.01610  178 ASN B N   
1760 C CA  . ASN B 78  ? 0.52552 0.41501 0.38738 0.00196  0.04878  0.01162  178 ASN B CA  
1761 C C   . ASN B 78  ? 0.55100 0.43814 0.41498 -0.00193 0.03985  0.00241  178 ASN B C   
1762 O O   . ASN B 78  ? 0.53744 0.41847 0.38923 -0.00474 0.02932  -0.00392 178 ASN B O   
1763 C CB  . ASN B 78  ? 0.57698 0.44901 0.41003 0.00676  0.05558  0.00943  178 ASN B CB  
1764 C CG  . ASN B 78  ? 0.83067 0.68926 0.65535 0.01062  0.06693  0.00504  178 ASN B CG  
1765 O OD1 . ASN B 78  ? 0.84482 0.70759 0.68405 0.01414  0.07921  0.01205  178 ASN B OD1 
1766 N ND2 . ASN B 78  ? 0.78145 0.62372 0.58415 0.00963  0.06271  -0.00632 178 ASN B ND2 
1767 N N   . ASN B 79  ? 0.46891 0.36256 0.35107 -0.00212 0.04391  0.00341  179 ASN B N   
1768 C CA  . ASN B 79  ? 0.51956 0.41253 0.40926 -0.00493 0.03794  -0.00311 179 ASN B CA  
1769 C C   . ASN B 79  ? 0.55428 0.45502 0.45019 -0.00977 0.02375  -0.00561 179 ASN B C   
1770 O O   . ASN B 79  ? 0.53906 0.43457 0.43377 -0.01229 0.01604  -0.01196 179 ASN B O   
1771 C CB  . ASN B 79  ? 0.69449 0.56727 0.56509 -0.00371 0.04002  -0.01227 179 ASN B CB  
1772 C CG  . ASN B 79  ? 0.71957 0.58298 0.58567 0.00194  0.05646  -0.01016 179 ASN B CG  
1773 O OD1 . ASN B 79  ? 0.70112 0.57555 0.58743 0.00417  0.06553  -0.00167 179 ASN B OD1 
1774 N ND2 . ASN B 79  ? 0.77031 0.61330 0.60943 0.00438  0.06062  -0.01734 179 ASN B ND2 
1775 N N   . GLU B 80  ? 0.43674 0.34966 0.34118 -0.01111 0.02069  -0.00028 180 GLU B N   
1776 C CA  . GLU B 80  ? 0.33241 0.25148 0.24280 -0.01480 0.00932  -0.00199 180 GLU B CA  
1777 C C   . GLU B 80  ? 0.33451 0.26919 0.26211 -0.01621 0.00921  0.00315  180 GLU B C   
1778 O O   . GLU B 80  ? 0.35269 0.29146 0.28208 -0.01531 0.01440  0.00837  180 GLU B O   
1779 C CB  . GLU B 80  ? 0.40315 0.31417 0.29681 -0.01539 0.00328  -0.00322 180 GLU B CB  
1780 C CG  . GLU B 80  ? 0.39299 0.31032 0.29512 -0.01864 -0.00708 -0.00317 180 GLU B CG  
1781 C CD  . GLU B 80  ? 0.61788 0.52887 0.50552 -0.01903 -0.01275 -0.00219 180 GLU B CD  
1782 O OE1 . GLU B 80  ? 0.61935 0.52550 0.49368 -0.01639 -0.00719 0.00072  180 GLU B OE1 
1783 O OE2 . GLU B 80  ? 0.51319 0.42475 0.40367 -0.02166 -0.02240 -0.00304 180 GLU B OE2 
1784 N N   . ILE B 81  ? 0.29625 0.23902 0.23625 -0.01845 0.00336  0.00167  181 ILE B N   
1785 C CA  . ILE B 81  ? 0.25103 0.20552 0.20243 -0.02036 0.00130  0.00401  181 ILE B CA  
1786 C C   . ILE B 81  ? 0.32931 0.27967 0.27667 -0.02176 -0.00562 0.00234  181 ILE B C   
1787 O O   . ILE B 81  ? 0.32068 0.26943 0.27041 -0.02258 -0.01170 -0.00015 181 ILE B O   
1788 C CB  . ILE B 81  ? 0.29762 0.26293 0.26303 -0.02100 0.00052  0.00397  181 ILE B CB  
1789 C CG1 . ILE B 81  ? 0.34691 0.31808 0.31879 -0.01945 0.00780  0.00782  181 ILE B CG1 
1790 C CG2 . ILE B 81  ? 0.29199 0.26667 0.26455 -0.02306 -0.00182 0.00440  181 ILE B CG2 
1791 C CD1 . ILE B 81  ? 0.32210 0.30386 0.30764 -0.01917 0.00768  0.00909  181 ILE B CD1 
1792 N N   . ALA B 82  ? 0.29339 0.24257 0.23718 -0.02190 -0.00441 0.00510  182 ALA B N   
1793 C CA  . ALA B 82  ? 0.27170 0.21663 0.21245 -0.02265 -0.00986 0.00531  182 ALA B CA  
1794 C C   . ALA B 82  ? 0.24609 0.19722 0.20009 -0.02456 -0.01333 0.00415  182 ALA B C   
1795 O O   . ALA B 82  ? 0.28278 0.23163 0.23904 -0.02492 -0.01872 0.00359  182 ALA B O   
1796 C CB  . ALA B 82  ? 0.32605 0.26799 0.26088 -0.02156 -0.00635 0.01000  182 ALA B CB  
1797 N N   . ALA B 83  ? 0.27276 0.23137 0.23550 -0.02586 -0.01023 0.00403  183 ALA B N   
1798 C CA  . ALA B 83  ? 0.23237 0.19450 0.20468 -0.02742 -0.01204 0.00172  183 ALA B CA  
1799 C C   . ALA B 83  ? 0.26842 0.23944 0.24622 -0.02920 -0.00942 0.00001  183 ALA B C   
1800 O O   . ALA B 83  ? 0.26625 0.24144 0.24331 -0.02985 -0.00658 0.00250  183 ALA B O   
1801 C CB  . ALA B 83  ? 0.31001 0.26772 0.28475 -0.02819 -0.01266 0.00352  183 ALA B CB  
1802 N N   . ALA B 84  ? 0.26788 0.26737 0.23551 -0.04318 -0.00441 0.07380  184 ALA B N   
1803 C CA  . ALA B 84  ? 0.22370 0.27298 0.18244 -0.05349 -0.00356 0.06811  184 ALA B CA  
1804 C C   . ALA B 84  ? 0.22634 0.30124 0.20847 -0.05429 -0.00499 0.02918  184 ALA B C   
1805 O O   . ALA B 84  ? 0.26202 0.32149 0.26549 -0.04829 -0.00554 0.00617  184 ALA B O   
1806 C CB  . ALA B 84  ? 0.26362 0.35400 0.20054 -0.06548 0.00292  0.07716  184 ALA B CB  
1807 N N   . ALA B 85  ? 0.22925 0.34351 0.20708 -0.06160 -0.00567 0.02208  185 ALA B N   
1808 C CA  . ALA B 85  ? 0.30075 0.44557 0.29881 -0.06394 -0.00667 -0.01423 185 ALA B CA  
1809 C C   . ALA B 85  ? 0.29282 0.39842 0.31621 -0.05220 -0.01153 -0.02919 185 ALA B C   
1810 O O   . ALA B 85  ? 0.27959 0.39235 0.32515 -0.05031 -0.01147 -0.06102 185 ALA B O   
1811 C CB  . ALA B 85  ? 0.32535 0.50545 0.32951 -0.07080 -0.00152 -0.03968 185 ALA B CB  
1812 N N   . CYS B 86  ? 0.24534 0.30879 0.26511 -0.04422 -0.01550 -0.00582 186 CYS B N   
1813 C CA  . CYS B 86  ? 0.24217 0.26390 0.28367 -0.03251 -0.01982 -0.01613 186 CYS B CA  
1814 C C   . CYS B 86  ? 0.24052 0.28273 0.29353 -0.03403 -0.02266 -0.03364 186 CYS B C   
1815 O O   . CYS B 86  ? 0.25265 0.32742 0.29210 -0.04185 -0.02298 -0.02533 186 CYS B O   
1816 C CB  . CYS B 86  ? 0.24153 0.20847 0.27408 -0.02335 -0.02260 0.01668  186 CYS B CB  
1817 S SG  . CYS B 86  ? 0.26769 0.20256 0.29005 -0.01949 -0.01974 0.03627  186 CYS B SG  
1818 N N   . TYR B 87  ? 0.23178 0.25234 0.30985 -0.02589 -0.02479 -0.05712 187 TYR B N   
1819 C CA  . TYR B 87  ? 0.25677 0.28668 0.34866 -0.02519 -0.02761 -0.07319 187 TYR B CA  
1820 C C   . TYR B 87  ? 0.29654 0.28041 0.38619 -0.01655 -0.03157 -0.04958 187 TYR B C   
1821 O O   . TYR B 87  ? 0.30545 0.23924 0.39444 -0.00714 -0.03252 -0.03278 187 TYR B O   
1822 C CB  . TYR B 87  ? 0.35699 0.38604 0.47748 -0.02067 -0.02732 -0.11088 187 TYR B CB  
1823 C CG  . TYR B 87  ? 0.47641 0.55831 0.60192 -0.03036 -0.02372 -0.13890 187 TYR B CG  
1824 C CD1 . TYR B 87  ? 0.48882 0.57625 0.61138 -0.03229 -0.02029 -0.14256 187 TYR B CD1 
1825 C CD2 . TYR B 87  ? 0.52956 0.65596 0.66311 -0.03765 -0.02365 -0.16211 187 TYR B CD2 
1826 C CE1 . TYR B 87  ? 0.55537 0.69085 0.68269 -0.04131 -0.01671 -0.16833 187 TYR B CE1 
1827 C CE2 . TYR B 87  ? 0.55273 0.72754 0.69069 -0.04667 -0.02021 -0.18787 187 TYR B CE2 
1828 C CZ  . TYR B 87  ? 0.54411 0.72299 0.67892 -0.04849 -0.01667 -0.19079 187 TYR B CZ  
1829 O OH  . TYR B 87  ? 0.66987 0.89281 0.80726 -0.05527 -0.01127 -0.21155 187 TYR B OH  
1830 N N   . LEU B 88  ? 0.27543 0.27697 0.36351 -0.01990 -0.03383 -0.04810 188 LEU B N   
1831 C CA  . LEU B 88  ? 0.30280 0.26689 0.39143 -0.01269 -0.03753 -0.03020 188 LEU B CA  
1832 C C   . LEU B 88  ? 0.34731 0.32322 0.45711 -0.01174 -0.03930 -0.05661 188 LEU B C   
1833 O O   . LEU B 88  ? 0.31392 0.33885 0.42959 -0.01997 -0.03811 -0.08085 188 LEU B O   
1834 C CB  . LEU B 88  ? 0.24808 0.22223 0.31034 -0.01828 -0.03868 0.00344  188 LEU B CB  
1835 C CG  . LEU B 88  ? 0.23538 0.19985 0.27358 -0.02021 -0.03665 0.03379  188 LEU B CG  
1836 C CD1 . LEU B 88  ? 0.25508 0.23223 0.26904 -0.02570 -0.03793 0.06425  188 LEU B CD1 
1837 C CD2 . LEU B 88  ? 0.29864 0.20054 0.34146 -0.00823 -0.03728 0.04759  188 LEU B CD2 
1838 N N   . PRO B 89  ? 0.29652 0.22864 0.41784 -0.00200 -0.04187 -0.05246 189 PRO B N   
1839 C CA  . PRO B 89  ? 0.36496 0.30768 0.50610 -0.00126 -0.04321 -0.07621 189 PRO B CA  
1840 C C   . PRO B 89  ? 0.30454 0.28918 0.43335 -0.01071 -0.04484 -0.06884 189 PRO B C   
1841 O O   . PRO B 89  ? 0.31556 0.29806 0.42213 -0.01326 -0.04616 -0.03783 189 PRO B O   
1842 C CB  . PRO B 89  ? 0.37868 0.28899 0.50647 0.00966  -0.03793 -0.05314 189 PRO B CB  
1843 C CG  . PRO B 89  ? 0.45757 0.35029 0.55277 0.01061  -0.03361 -0.02050 189 PRO B CG  
1844 C CD  . PRO B 89  ? 0.30286 0.19352 0.40459 0.00700  -0.03863 -0.02045 189 PRO B CD  
1845 N N   . LEU B 90  ? 0.25425 0.27756 0.39743 -0.01582 -0.04475 -0.09760 190 LEU B N   
1846 C CA  . LEU B 90  ? 0.30230 0.36848 0.43538 -0.02467 -0.04659 -0.09402 190 LEU B CA  
1847 C C   . LEU B 90  ? 0.37561 0.41663 0.51860 -0.01893 -0.04972 -0.08960 190 LEU B C   
1848 O O   . LEU B 90  ? 0.37851 0.39957 0.54567 -0.01254 -0.04946 -0.11152 190 LEU B O   
1849 C CB  . LEU B 90  ? 0.35245 0.47719 0.49464 -0.03396 -0.04490 -0.12710 190 LEU B CB  
1850 C CG  . LEU B 90  ? 0.40646 0.56216 0.53917 -0.04092 -0.04139 -0.13386 190 LEU B CG  
1851 C CD1 . LEU B 90  ? 0.48294 0.69665 0.62487 -0.05018 -0.03993 -0.16632 190 LEU B CD1 
1852 C CD2 . LEU B 90  ? 0.35633 0.52087 0.45819 -0.04622 -0.04117 -0.10036 190 LEU B CD2 
1853 N N   . SER B 91  ? 0.29778 0.33941 0.42216 -0.02115 -0.05240 -0.06129 191 SER B N   
1854 C CA  . SER B 91  ? 0.31791 0.33701 0.45042 -0.01626 -0.05539 -0.05526 191 SER B CA  
1855 C C   . SER B 91  ? 0.33608 0.39443 0.48629 -0.02092 -0.05604 -0.08598 191 SER B C   
1856 O O   . SER B 91  ? 0.30717 0.42044 0.45289 -0.03068 -0.05553 -0.10065 191 SER B O   
1857 C CB  . SER B 91  ? 0.27392 0.29061 0.38164 -0.01858 -0.05820 -0.01865 191 SER B CB  
1858 O OG  . SER B 91  ? 0.32816 0.33012 0.44453 -0.01505 -0.06118 -0.01534 191 SER B OG  
1859 N N   . GLU B 92  ? 0.31088 0.34009 0.48110 -0.01380 -0.05700 -0.09523 192 GLU B N   
1860 C CA  . GLU B 92  ? 0.36543 0.42562 0.55277 -0.01726 -0.05793 -0.12063 192 GLU B CA  
1861 C C   . GLU B 92  ? 0.35119 0.41084 0.53105 -0.01792 -0.06169 -0.10148 192 GLU B C   
1862 O O   . GLU B 92  ? 0.34362 0.41888 0.53968 -0.01891 -0.06271 -0.12013 192 GLU B O   
1863 C CB  . GLU B 92  ? 0.46005 0.49186 0.67774 -0.00930 -0.05563 -0.14908 192 GLU B CB  
1864 C CG  . GLU B 92  ? 0.64202 0.70859 0.86723 -0.01036 -0.04883 -0.17602 192 GLU B CG  
1865 C CD  . GLU B 92  ? 0.83741 0.87545 1.06818 0.00255  -0.04064 -0.16911 192 GLU B CD  
1866 O OE1 . GLU B 92  ? 0.86952 0.87730 1.09723 0.00990  -0.03902 -0.14736 192 GLU B OE1 
1867 O OE2 . GLU B 92  ? 0.92540 0.98095 1.15826 0.00145  -0.03695 -0.18093 192 GLU B OE2 
1868 N N   . SER B 93  ? 0.29012 0.33348 0.44608 -0.01760 -0.06368 -0.06523 193 SER B N   
1869 C CA  . SER B 93  ? 0.31405 0.35315 0.46198 -0.01759 -0.06738 -0.04451 193 SER B CA  
1870 C C   . SER B 93  ? 0.34553 0.44551 0.49236 -0.02721 -0.06960 -0.05907 193 SER B C   
1871 O O   . SER B 93  ? 0.28085 0.42850 0.41535 -0.03593 -0.06908 -0.06515 193 SER B O   
1872 C CB  . SER B 93  ? 0.31650 0.33734 0.43578 -0.01745 -0.06880 -0.00358 193 SER B CB  
1873 O OG  . SER B 93  ? 0.32886 0.35909 0.43710 -0.01975 -0.07262 0.01561  193 SER B OG  
1874 N N   . PRO B 94  ? 0.34212 0.44221 0.50098 -0.02589 -0.07208 -0.06441 194 PRO B N   
1875 C CA  . PRO B 94  ? 0.31888 0.47599 0.47428 -0.03472 -0.07493 -0.07453 194 PRO B CA  
1876 C C   . PRO B 94  ? 0.32915 0.50491 0.45472 -0.03965 -0.07842 -0.04219 194 PRO B C   
1877 O O   . PRO B 94  ? 0.36351 0.58721 0.48327 -0.04682 -0.08119 -0.04805 194 PRO B O   
1878 C CB  . PRO B 94  ? 0.32860 0.47089 0.50833 -0.03018 -0.07614 -0.08941 194 PRO B CB  
1879 C CG  . PRO B 94  ? 0.28526 0.36041 0.46726 -0.01973 -0.07564 -0.06724 194 PRO B CG  
1880 C CD  . PRO B 94  ? 0.28890 0.33611 0.46436 -0.01612 -0.07234 -0.06038 194 PRO B CD  
1881 N N   . PHE B 95  ? 0.28203 0.42180 0.38842 -0.03593 -0.07832 -0.00858 195 PHE B N   
1882 C CA  . PHE B 95  ? 0.27001 0.42366 0.34722 -0.04007 -0.08117 0.02412  195 PHE B CA  
1883 C C   . PHE B 95  ? 0.44098 0.62497 0.49478 -0.04701 -0.07916 0.03261  195 PHE B C   
1884 O O   . PHE B 95  ? 0.43540 0.62271 0.46303 -0.04946 -0.08044 0.06311  195 PHE B O   
1885 C CB  . PHE B 95  ? 0.32831 0.42482 0.39734 -0.03217 -0.08224 0.05815  195 PHE B CB  
1886 C CG  . PHE B 95  ? 0.33149 0.39888 0.41956 -0.02589 -0.08432 0.05494  195 PHE B CG  
1887 C CD1 . PHE B 95  ? 0.32419 0.41202 0.40729 -0.02863 -0.08858 0.06336  195 PHE B CD1 
1888 C CD2 . PHE B 95  ? 0.33468 0.35460 0.44579 -0.01712 -0.08189 0.04292  195 PHE B CD2 
1889 C CE1 . PHE B 95  ? 0.35424 0.41520 0.45557 -0.02300 -0.09020 0.06005  195 PHE B CE1 
1890 C CE2 . PHE B 95  ? 0.32169 0.31402 0.45044 -0.01138 -0.08321 0.03981  195 PHE B CE2 
1891 C CZ  . PHE B 95  ? 0.33957 0.35273 0.46381 -0.01451 -0.08728 0.04814  195 PHE B CZ  
1892 N N   . ILE B 96  ? 0.39720 0.60285 0.45970 -0.05023 -0.07577 0.00669  196 ILE B N   
1893 C CA  . ILE B 96  ? 0.43881 0.67406 0.48056 -0.05708 -0.07321 0.01236  196 ILE B CA  
1894 C C   . ILE B 96  ? 0.44779 0.74950 0.48283 -0.06715 -0.07452 -0.00363 196 ILE B C   
1895 O O   . ILE B 96  ? 0.40988 0.73949 0.46471 -0.06975 -0.07414 -0.03732 196 ILE B O   
1896 C CB  . ILE B 96  ? 0.40200 0.62196 0.45590 -0.05480 -0.06861 -0.00539 196 ILE B CB  
1897 C CG1 . ILE B 96  ? 0.37488 0.52929 0.42989 -0.04489 -0.06759 0.01583  196 ILE B CG1 
1898 C CG2 . ILE B 96  ? 0.47928 0.73900 0.51481 -0.06326 -0.06563 -0.00612 196 ILE B CG2 
1899 C CD1 . ILE B 96  ? 0.38588 0.52290 0.44893 -0.04218 -0.06344 0.00354  196 ILE B CD1 
1900 N N   . SER B 97  ? 0.39471 0.72118 0.40152 -0.07259 -0.07600 0.02077  197 SER B N   
1901 C CA  . SER B 97  ? 0.45815 0.84583 0.45568 -0.08145 -0.07798 0.00976  197 SER B CA  
1902 C C   . SER B 97  ? 0.43575 0.86425 0.44090 -0.08795 -0.07445 -0.02225 197 SER B C   
1903 O O   . SER B 97  ? 0.40337 0.82207 0.40711 -0.08816 -0.07002 -0.02484 197 SER B O   
1904 C CB  . SER B 97  ? 0.50610 0.90836 0.46970 -0.08543 -0.07813 0.04275  197 SER B CB  
1905 O OG  . SER B 97  ? 0.57940 1.02659 0.53560 -0.09120 -0.07316 0.03040  197 SER B OG  
1906 N N   . LYS B 98  ? 0.53094 0.99921 0.54388 -0.09189 -0.07426 -0.04619 198 LYS B N   
1907 C CA  . LYS B 98  ? 0.61027 1.10744 0.63091 -0.09555 -0.06726 -0.07646 198 LYS B CA  
1908 C C   . LYS B 98  ? 0.43099 0.95219 0.42654 -0.10141 -0.06104 -0.06533 198 LYS B C   
1909 O O   . LYS B 98  ? 0.45517 0.99111 0.45596 -0.10405 -0.05529 -0.08499 198 LYS B O   
1910 C CB  . LYS B 98  ? 0.64750 1.17237 0.67873 -0.09631 -0.06576 -0.09890 198 LYS B CB  
1911 C CG  . LYS B 98  ? 0.59257 1.13013 0.60832 -0.09714 -0.06920 -0.07929 198 LYS B CG  
1912 C CD  . LYS B 98  ? 0.69117 1.25654 0.71866 -0.09780 -0.06799 -0.10273 198 LYS B CD  
1913 C CE  . LYS B 98  ? 0.85164 1.43334 0.86203 -0.09907 -0.07064 -0.08330 198 LYS B CE  
1914 N NZ  . LYS B 98  ? 0.67036 1.27814 0.69220 -0.09942 -0.07032 -0.10473 198 LYS B NZ  
1915 N N   . GLU B 99  ? 0.43315 0.95636 0.40315 -0.10302 -0.06076 -0.03415 199 GLU B N   
1916 C CA  . GLU B 99  ? 0.45753 1.00073 0.40725 -0.10829 -0.05330 -0.02253 199 GLU B CA  
1917 C C   . GLU B 99  ? 0.35218 0.86730 0.29428 -0.10733 -0.05195 -0.00727 199 GLU B C   
1918 O O   . GLU B 99  ? 0.52972 1.05743 0.45876 -0.11144 -0.04522 0.00177  199 GLU B O   
1919 C CB  . GLU B 99  ? 0.73018 1.28315 0.66202 -0.10971 -0.05120 0.00326  199 GLU B CB  
1920 C CG  . GLU B 99  ? 0.75861 1.26917 0.68295 -0.10405 -0.05460 0.03551  199 GLU B CG  
1921 C CD  . GLU B 99  ? 0.97154 1.47909 0.88305 -0.10511 -0.04905 0.06188  199 GLU B CD  
1922 O OE1 . GLU B 99  ? 0.84003 1.33234 0.74708 -0.10536 -0.04478 0.07327  199 GLU B OE1 
1923 O OE2 . GLU B 99  ? 0.89918 1.41830 0.80850 -0.10516 -0.04963 0.06865  199 GLU B OE2 
1924 N N   . LEU B 100 ? 0.45004 0.92744 0.40262 -0.10196 -0.05811 -0.00453 200 LEU B N   
1925 C CA  . LEU B 100 ? 0.40240 0.85017 0.34673 -0.10028 -0.05718 0.01199  200 LEU B CA  
1926 C C   . LEU B 100 ? 0.44327 0.90068 0.40294 -0.10253 -0.05463 -0.01675 200 LEU B C   
1927 O O   . LEU B 100 ? 0.49663 0.97155 0.47897 -0.10321 -0.05436 -0.04984 200 LEU B O   
1928 C CB  . LEU B 100 ? 0.30588 0.69669 0.25658 -0.09105 -0.06141 0.03193  200 LEU B CB  
1929 C CG  . LEU B 100 ? 0.37367 0.74912 0.30634 -0.08876 -0.06267 0.06545  200 LEU B CG  
1930 C CD1 . LEU B 100 ? 0.36572 0.68438 0.30406 -0.07968 -0.06697 0.08548  200 LEU B CD1 
1931 C CD2 . LEU B 100 ? 0.38242 0.75488 0.29994 -0.09050 -0.05216 0.08559  200 LEU B CD2 
1932 N N   . GLY B 101 ? 0.35790 0.79631 0.30681 -0.10212 -0.05029 -0.00321 201 GLY B N   
1933 C CA  . GLY B 101 ? 0.41650 0.86019 0.37788 -0.10366 -0.04562 -0.02704 201 GLY B CA  
1934 C C   . GLY B 101 ? 0.37121 0.76228 0.35631 -0.09391 -0.04525 -0.03472 201 GLY B C   
1935 O O   . GLY B 101 ? 0.31249 0.65920 0.30384 -0.08559 -0.04825 -0.02010 201 GLY B O   
1936 N N   . THR B 102 ? 0.42784 0.40969 0.42478 -0.02143 -0.03460 -0.02083 202 THR B N   
1937 C CA  . THR B 102 ? 0.45683 0.43088 0.46515 -0.02605 -0.03637 -0.01869 202 THR B CA  
1938 C C   . THR B 102 ? 0.37936 0.35126 0.38488 -0.02706 -0.03065 -0.00947 202 THR B C   
1939 O O   . THR B 102 ? 0.35331 0.32249 0.36608 -0.03211 -0.03300 -0.00469 202 THR B O   
1940 C CB  . THR B 102 ? 0.52907 0.49663 0.54219 -0.02480 -0.03607 -0.02605 202 THR B CB  
1941 O OG1 . THR B 102 ? 0.64753 0.61589 0.66477 -0.02398 -0.04277 -0.03609 202 THR B OG1 
1942 C CG2 . THR B 102 ? 0.51505 0.47404 0.54040 -0.03001 -0.03802 -0.02241 202 THR B CG2 
1943 N N   . ARG B 103 ? 0.30842 0.28188 0.30339 -0.02253 -0.02381 -0.00665 203 ARG B N   
1944 C CA  . ARG B 103 ? 0.34272 0.31283 0.33459 -0.02282 -0.01935 0.00096  203 ARG B CA  
1945 C C   . ARG B 103 ? 0.34187 0.31693 0.33545 -0.02506 -0.02085 0.00580  203 ARG B C   
1946 O O   . ARG B 103 ? 0.28205 0.25360 0.27734 -0.02800 -0.01988 0.01027  203 ARG B O   
1947 C CB  . ARG B 103 ? 0.35550 0.32705 0.33751 -0.01750 -0.01357 0.00358  203 ARG B CB  
1948 C CG  . ARG B 103 ? 0.44261 0.40906 0.42370 -0.01582 -0.01037 0.00254  203 ARG B CG  
1949 C CD  . ARG B 103 ? 0.47495 0.44400 0.44778 -0.01141 -0.00584 0.00746  203 ARG B CD  
1950 N NE  . ARG B 103 ? 0.47324 0.43975 0.44628 -0.00993 -0.00272 0.00796  203 ARG B NE  
1951 C CZ  . ARG B 103 ? 0.50893 0.48315 0.47853 -0.00692 -0.00061 0.00495  203 ARG B CZ  
1952 N NH1 . ARG B 103 ? 0.46981 0.45359 0.43386 -0.00523 -0.00187 0.00098  203 ARG B NH1 
1953 N NH2 . ARG B 103 ? 0.52946 0.50252 0.50111 -0.00572 0.00280  0.00629  203 ARG B NH2 
1954 N N   . HIS B 104 ? 0.28101 0.26506 0.27408 -0.02376 -0.02318 0.00529  204 HIS B N   
1955 C CA  . HIS B 104 ? 0.27494 0.26590 0.27147 -0.02548 -0.02407 0.01060  204 HIS B CA  
1956 C C   . HIS B 104 ? 0.28660 0.27769 0.29411 -0.03214 -0.02976 0.01178  204 HIS B C   
1957 O O   . HIS B 104 ? 0.27151 0.26584 0.28171 -0.03486 -0.02855 0.01755  204 HIS B O   
1958 C CB  . HIS B 104 ? 0.26609 0.26673 0.26115 -0.02280 -0.02593 0.01079  204 HIS B CB  
1959 C CG  . HIS B 104 ? 0.26507 0.26687 0.25069 -0.01712 -0.02131 0.01139  204 HIS B CG  
1960 N ND1 . HIS B 104 ? 0.32130 0.32159 0.30065 -0.01487 -0.02116 0.00686  204 HIS B ND1 
1961 C CD2 . HIS B 104 ? 0.28894 0.29331 0.27111 -0.01332 -0.01682 0.01630  204 HIS B CD2 
1962 C CE1 . HIS B 104 ? 0.38217 0.38496 0.35484 -0.01074 -0.01737 0.01027  204 HIS B CE1 
1963 N NE2 . HIS B 104 ? 0.27156 0.27588 0.24651 -0.00962 -0.01515 0.01577  204 HIS B NE2 
1964 N N   . ARG B 105 ? 0.27996 0.26811 0.29431 -0.03483 -0.03629 0.00643  205 ARG B N   
1965 C CA  . ARG B 105 ? 0.29257 0.28030 0.31993 -0.04185 -0.04349 0.00831  205 ARG B CA  
1966 C C   . ARG B 105 ? 0.31174 0.29259 0.34112 -0.04578 -0.04137 0.01209  205 ARG B C   
1967 O O   . ARG B 105 ? 0.31634 0.30056 0.35273 -0.05170 -0.04417 0.01836  205 ARG B O   
1968 C CB  . ARG B 105 ? 0.37138 0.35522 0.40644 -0.04303 -0.05167 0.00032  205 ARG B CB  
1969 C CG  . ARG B 105 ? 0.51929 0.50394 0.57047 -0.05046 -0.06171 0.00294  205 ARG B CG  
1970 C CD  . ARG B 105 ? 0.54912 0.53075 0.60786 -0.05047 -0.07135 -0.00589 205 ARG B CD  
1971 N NE  . ARG B 105 ? 0.67641 0.66497 0.72959 -0.04730 -0.07352 -0.00794 205 ARG B NE  
1972 C CZ  . ARG B 105 ? 0.76354 0.76017 0.82406 -0.05089 -0.07983 -0.00182 205 ARG B CZ  
1973 N NH1 . ARG B 105 ? 0.57633 0.57702 0.64948 -0.05767 -0.08374 0.00735  205 ARG B NH1 
1974 N NH2 . ARG B 105 ? 0.70447 0.70612 0.75987 -0.04804 -0.08253 -0.00407 205 ARG B NH2 
1975 N N   . ALA B 106 ? 0.28032 0.25230 0.30363 -0.04296 -0.03671 0.00922  206 ALA B N   
1976 C CA  . ALA B 106 ? 0.27161 0.23573 0.29581 -0.04676 -0.03516 0.01313  206 ALA B CA  
1977 C C   . ALA B 106 ? 0.26908 0.23622 0.28466 -0.04640 -0.02960 0.01962  206 ALA B C   
1978 O O   . ALA B 106 ? 0.28336 0.24954 0.30112 -0.05200 -0.03069 0.02479  206 ALA B O   
1979 C CB  . ALA B 106 ? 0.32101 0.27565 0.34178 -0.04337 -0.03180 0.00911  206 ALA B CB  
1980 N N   . ALA B 107 ? 0.25371 0.22490 0.25957 -0.03986 -0.02393 0.01931  207 ALA B N   
1981 C CA  . ALA B 107 ? 0.26904 0.24267 0.26724 -0.03817 -0.01860 0.02381  207 ALA B CA  
1982 C C   . ALA B 107 ? 0.27048 0.25540 0.27407 -0.04223 -0.02022 0.02863  207 ALA B C   
1983 O O   . ALA B 107 ? 0.26861 0.25448 0.26930 -0.04503 -0.01806 0.03274  207 ALA B O   
1984 C CB  . ALA B 107 ? 0.29076 0.26687 0.28080 -0.03022 -0.01358 0.02252  207 ALA B CB  
1985 N N   . VAL B 108 ? 0.24100 0.23554 0.25218 -0.04266 -0.02415 0.02863  208 VAL B N   
1986 C CA  . VAL B 108 ? 0.24562 0.25247 0.26440 -0.04723 -0.02632 0.03487  208 VAL B CA  
1987 C C   . VAL B 108 ? 0.26435 0.26866 0.29112 -0.05620 -0.03185 0.03856  208 VAL B C   
1988 O O   . VAL B 108 ? 0.27073 0.28262 0.29836 -0.06046 -0.03066 0.04514  208 VAL B O   
1989 C CB  . VAL B 108 ? 0.27363 0.29030 0.30085 -0.04679 -0.03128 0.03505  208 VAL B CB  
1990 C CG1 . VAL B 108 ? 0.22861 0.25926 0.26619 -0.05242 -0.03415 0.04340  208 VAL B CG1 
1991 C CG2 . VAL B 108 ? 0.28549 0.30567 0.30528 -0.03866 -0.02611 0.03301  208 VAL B CG2 
1992 N N   . GLY B 109 ? 0.28422 0.27834 0.31706 -0.05907 -0.03779 0.03453  209 GLY B N   
1993 C CA  . GLY B 109 ? 0.25871 0.24933 0.30162 -0.06797 -0.04437 0.03840  209 GLY B CA  
1994 C C   . GLY B 109 ? 0.30792 0.29490 0.34295 -0.07109 -0.04011 0.04311  209 GLY B C   
1995 O O   . GLY B 109 ? 0.30660 0.30003 0.34646 -0.07859 -0.04301 0.05061  209 GLY B O   
1996 N N   . ILE B 110 ? 0.27044 0.24732 0.29309 -0.06582 -0.03383 0.03933  210 ILE B N   
1997 C CA  . ILE B 110 ? 0.27694 0.24848 0.29079 -0.06883 -0.03084 0.04316  210 ILE B CA  
1998 C C   . ILE B 110 ? 0.32892 0.31238 0.33384 -0.06729 -0.02486 0.04707  210 ILE B C   
1999 O O   . ILE B 110 ? 0.30424 0.28937 0.30438 -0.07248 -0.02425 0.05201  210 ILE B O   
2000 C CB  . ILE B 110 ? 0.25479 0.21162 0.25917 -0.06387 -0.02705 0.03872  210 ILE B CB  
2001 C CG1 . ILE B 110 ? 0.29600 0.24407 0.29369 -0.06899 -0.02718 0.04272  210 ILE B CG1 
2002 C CG2 . ILE B 110 ? 0.23400 0.19246 0.22669 -0.05413 -0.01955 0.03518  210 ILE B CG2 
2003 C CD1 . ILE B 110 ? 0.34434 0.28927 0.35434 -0.07945 -0.03542 0.04748  210 ILE B CD1 
2004 N N   . SER B 111 ? 0.26629 0.25919 0.26935 -0.06035 -0.02053 0.04512  211 SER B N   
2005 C CA  . SER B 111 ? 0.26399 0.26983 0.26073 -0.05765 -0.01415 0.04824  211 SER B CA  
2006 C C   . SER B 111 ? 0.28754 0.30926 0.29393 -0.06542 -0.01745 0.05646  211 SER B C   
2007 O O   . SER B 111 ? 0.30564 0.33913 0.30641 -0.06511 -0.01191 0.06031  211 SER B O   
2008 C CB  . SER B 111 ? 0.26588 0.27777 0.26135 -0.04835 -0.00959 0.04472  211 SER B CB  
2009 O OG  . SER B 111 ? 0.27898 0.30293 0.28714 -0.05023 -0.01394 0.04752  211 SER B OG  
2010 N N   . GLU B 112 ? 0.24847 0.27133 0.26981 -0.07227 -0.02657 0.05931  212 GLU B N   
2011 C CA  . GLU B 112 ? 0.26271 0.30085 0.29602 -0.08073 -0.03159 0.06879  212 GLU B CA  
2012 C C   . GLU B 112 ? 0.40549 0.44253 0.43751 -0.09010 -0.03416 0.07523  212 GLU B C   
2013 O O   . GLU B 112 ? 0.37857 0.43146 0.41570 -0.09671 -0.03538 0.08466  212 GLU B O   
2014 C CB  . GLU B 112 ? 0.35045 0.38897 0.40183 -0.08454 -0.04226 0.06922  212 GLU B CB  
2015 C CG  . GLU B 112 ? 0.31214 0.35607 0.36580 -0.07709 -0.04113 0.06525  212 GLU B CG  
2016 C CD  . GLU B 112 ? 0.33975 0.37839 0.40709 -0.07923 -0.05196 0.06185  212 GLU B CD  
2017 O OE1 . GLU B 112 ? 0.35519 0.38422 0.43069 -0.08510 -0.05976 0.06090  212 GLU B OE1 
2018 O OE2 . GLU B 112 ? 0.35556 0.39931 0.42561 -0.07486 -0.05304 0.05976  212 GLU B OE2 
2019 N N   . VAL B 113 ? 0.33788 0.35766 0.36359 -0.09127 -0.03524 0.07139  213 VAL B N   
2020 C CA  . VAL B 113 ? 0.35953 0.37629 0.38544 -0.10132 -0.03968 0.07795  213 VAL B CA  
2021 C C   . VAL B 113 ? 0.34727 0.35485 0.35337 -0.09889 -0.03288 0.07536  213 VAL B C   
2022 O O   . VAL B 113 ? 0.36428 0.36701 0.36822 -0.10723 -0.03676 0.08036  213 VAL B O   
2023 C CB  . VAL B 113 ? 0.37206 0.37618 0.41378 -0.10786 -0.05074 0.07784  213 VAL B CB  
2024 C CG1 . VAL B 113 ? 0.32618 0.33873 0.38804 -0.11100 -0.05932 0.08027  213 VAL B CG1 
2025 C CG2 . VAL B 113 ? 0.32603 0.31128 0.36256 -0.10080 -0.04871 0.06787  213 VAL B CG2 
2026 N N   . THR B 114 ? 0.32150 0.32573 0.31386 -0.08806 -0.02400 0.06792  214 THR B N   
2027 C CA  . THR B 114 ? 0.27616 0.27169 0.24922 -0.08428 -0.01777 0.06445  214 THR B CA  
2028 C C   . THR B 114 ? 0.36963 0.37526 0.33268 -0.07406 -0.00797 0.06029  214 THR B C   
2029 O O   . THR B 114 ? 0.35491 0.37077 0.32623 -0.06921 -0.00620 0.05947  214 THR B O   
2030 C CB  . THR B 114 ? 0.38258 0.35644 0.35177 -0.08054 -0.01912 0.05810  214 THR B CB  
2031 O OG1 . THR B 114 ? 0.32565 0.29812 0.29705 -0.07077 -0.01582 0.05160  214 THR B OG1 
2032 C CG2 . THR B 114 ? 0.37710 0.34113 0.35953 -0.08914 -0.02848 0.06124  214 THR B CG2 
2033 N N   . ASP B 115 ? 0.33146 0.33294 0.27699 -0.07030 -0.00212 0.05704  215 ASP B N   
2034 C CA  . ASP B 115 ? 0.31687 0.32413 0.25342 -0.05898 0.00689  0.05109  215 ASP B CA  
2035 C C   . ASP B 115 ? 0.31277 0.30239 0.24456 -0.05005 0.00787  0.04303  215 ASP B C   
2036 O O   . ASP B 115 ? 0.37454 0.36308 0.29663 -0.04094 0.01397  0.03731  215 ASP B O   
2037 C CB  . ASP B 115 ? 0.39391 0.40793 0.31409 -0.05864 0.01291  0.05080  215 ASP B CB  
2038 C CG  . ASP B 115 ? 0.42483 0.41865 0.32938 -0.06003 0.01076  0.04703  215 ASP B CG  
2039 O OD1 . ASP B 115 ? 0.38836 0.36616 0.29778 -0.06502 0.00346  0.04825  215 ASP B OD1 
2040 O OD2 . ASP B 115 ? 0.43248 0.42640 0.32033 -0.05585 0.01616  0.04260  215 ASP B OD2 
2041 N N   . SER B 116 ? 0.30686 0.28319 0.24604 -0.05249 0.00177  0.04273  216 SER B N   
2042 C CA  . SER B 116 ? 0.29712 0.25807 0.23288 -0.04525 0.00209  0.03702  216 SER B CA  
2043 C C   . SER B 116 ? 0.31457 0.28348 0.25490 -0.03600 0.00617  0.03373  216 SER B C   
2044 O O   . SER B 116 ? 0.33537 0.32016 0.28436 -0.03604 0.00730  0.03607  216 SER B O   
2045 C CB  . SER B 116 ? 0.31900 0.26763 0.26342 -0.05000 -0.00458 0.03814  216 SER B CB  
2046 O OG  . SER B 116 ? 0.30645 0.26459 0.26545 -0.05270 -0.00767 0.03998  216 SER B OG  
2047 N N   . LEU B 117 ? 0.27059 0.22818 0.20608 -0.02861 0.00741  0.02926  217 LEU B N   
2048 C CA  . LEU B 117 ? 0.29327 0.25577 0.23380 -0.02054 0.00970  0.02694  217 LEU B CA  
2049 C C   . LEU B 117 ? 0.31168 0.26448 0.25739 -0.02080 0.00551  0.02678  217 LEU B C   
2050 O O   . LEU B 117 ? 0.29372 0.23175 0.23486 -0.02119 0.00337  0.02622  217 LEU B O   
2051 C CB  . LEU B 117 ? 0.30879 0.26791 0.24108 -0.01132 0.01419  0.02253  217 LEU B CB  
2052 C CG  . LEU B 117 ? 0.37342 0.33748 0.31202 -0.00298 0.01589  0.02101  217 LEU B CG  
2053 C CD1 . LEU B 117 ? 0.55505 0.52251 0.48925 0.00546  0.02102  0.01702  217 LEU B CD1 
2054 C CD2 . LEU B 117 ? 0.43338 0.38413 0.37288 -0.00091 0.01206  0.02076  217 LEU B CD2 
2055 N N   . THR B 118 ? 0.25147 0.21305 0.20648 -0.02044 0.00427  0.02739  218 THR B N   
2056 C CA  . THR B 118 ? 0.24622 0.20108 0.20510 -0.02036 0.00114  0.02664  218 THR B CA  
2057 C C   . THR B 118 ? 0.29285 0.25280 0.25307 -0.01321 0.00276  0.02559  218 THR B C   
2058 O O   . THR B 118 ? 0.26902 0.24132 0.23312 -0.01098 0.00419  0.02601  218 THR B O   
2059 C CB  . THR B 118 ? 0.25541 0.21417 0.22342 -0.02691 -0.00324 0.02737  218 THR B CB  
2060 O OG1 . THR B 118 ? 0.26412 0.21755 0.23244 -0.03422 -0.00577 0.02949  218 THR B OG1 
2061 C CG2 . THR B 118 ? 0.25605 0.20906 0.22693 -0.02565 -0.00531 0.02528  218 THR B CG2 
2062 N N   . ILE B 119 ? 0.26027 0.21141 0.21826 -0.01016 0.00207  0.02533  219 ILE B N   
2063 C CA  . ILE B 119 ? 0.26413 0.21979 0.22359 -0.00443 0.00254  0.02569  219 ILE B CA  
2064 C C   . ILE B 119 ? 0.28619 0.24375 0.24897 -0.00654 0.00018  0.02546  219 ILE B C   
2065 O O   . ILE B 119 ? 0.26606 0.21609 0.22900 -0.00990 -0.00118 0.02519  219 ILE B O   
2066 C CB  . ILE B 119 ? 0.27372 0.21945 0.22881 0.00071  0.00294  0.02665  219 ILE B CB  
2067 C CG1 . ILE B 119 ? 0.31141 0.25312 0.26164 0.00322  0.00507  0.02485  219 ILE B CG1 
2068 C CG2 . ILE B 119 ? 0.27456 0.22631 0.23273 0.00596  0.00257  0.02847  219 ILE B CG2 
2069 C CD1 . ILE B 119 ? 0.34862 0.27614 0.29435 0.00693  0.00346  0.02499  219 ILE B CD1 
2070 N N   . ILE B 120 ? 0.23913 0.20701 0.20458 -0.00436 -0.00036 0.02540  220 ILE B N   
2071 C CA  . ILE B 120 ? 0.23734 0.20836 0.20394 -0.00570 -0.00237 0.02393  220 ILE B CA  
2072 C C   . ILE B 120 ? 0.29259 0.26872 0.25720 -0.00114 -0.00220 0.02629  220 ILE B C   
2073 O O   . ILE B 120 ? 0.27417 0.25686 0.24037 0.00179  -0.00212 0.02809  220 ILE B O   
2074 C CB  . ILE B 120 ? 0.23522 0.21446 0.20673 -0.00930 -0.00523 0.02113  220 ILE B CB  
2075 C CG1 . ILE B 120 ? 0.25167 0.22887 0.22717 -0.01426 -0.00619 0.02101  220 ILE B CG1 
2076 C CG2 . ILE B 120 ? 0.28556 0.26521 0.25728 -0.01064 -0.00744 0.01735  220 ILE B CG2 
2077 C CD1 . ILE B 120 ? 0.24525 0.22979 0.22238 -0.01353 -0.00444 0.02374  220 ILE B CD1 
2078 N N   . VAL B 121 ? 0.24065 0.21494 0.20281 -0.00075 -0.00223 0.02703  221 VAL B N   
2079 C CA  . VAL B 121 ? 0.27269 0.25442 0.23270 0.00210  -0.00277 0.02999  221 VAL B CA  
2080 C C   . VAL B 121 ? 0.26621 0.25568 0.22434 0.00022  -0.00397 0.02579  221 VAL B C   
2081 O O   . VAL B 121 ? 0.25756 0.24371 0.21562 -0.00179 -0.00335 0.02208  221 VAL B O   
2082 C CB  . VAL B 121 ? 0.24591 0.22217 0.20439 0.00397  -0.00203 0.03522  221 VAL B CB  
2083 C CG1 . VAL B 121 ? 0.31477 0.30107 0.27157 0.00606  -0.00324 0.03982  221 VAL B CG1 
2084 C CG2 . VAL B 121 ? 0.26204 0.22845 0.22210 0.00606  -0.00213 0.03790  221 VAL B CG2 
2085 N N   . SER B 122 ? 0.24806 0.24753 0.20504 0.00102  -0.00614 0.02602  222 SER B N   
2086 C CA  . SER B 122 ? 0.25724 0.26385 0.21074 -0.00043 -0.00824 0.02109  222 SER B CA  
2087 C C   . SER B 122 ? 0.28454 0.29556 0.23140 0.00100  -0.00650 0.02259  222 SER B C   
2088 O O   . SER B 122 ? 0.30588 0.32090 0.25092 0.00283  -0.00628 0.02956  222 SER B O   
2089 C CB  . SER B 122 ? 0.25978 0.27522 0.21416 -0.00059 -0.01216 0.02172  222 SER B CB  
2090 O OG  . SER B 122 ? 0.27859 0.30084 0.22692 -0.00150 -0.01491 0.01742  222 SER B OG  
2091 N N   . GLU B 123 ? 0.27398 0.28524 0.21820 0.00022  -0.00539 0.01641  223 GLU B N   
2092 C CA  . GLU B 123 ? 0.27789 0.29683 0.21509 0.00179  -0.00294 0.01773  223 GLU B CA  
2093 C C   . GLU B 123 ? 0.34000 0.37088 0.26906 0.00195  -0.00575 0.01631  223 GLU B C   
2094 O O   . GLU B 123 ? 0.38212 0.42219 0.30374 0.00297  -0.00387 0.01897  223 GLU B O   
2095 C CB  . GLU B 123 ? 0.37157 0.38792 0.30939 0.00186  0.00016  0.01131  223 GLU B CB  
2096 C CG  . GLU B 123 ? 0.47096 0.48753 0.40878 0.00096  -0.00262 0.00005  223 GLU B CG  
2097 C CD  . GLU B 123 ? 0.56622 0.57866 0.50823 0.00148  0.00018  -0.00647 223 GLU B CD  
2098 O OE1 . GLU B 123 ? 0.59084 0.59678 0.53862 0.00123  0.00336  -0.00169 223 GLU B OE1 
2099 O OE2 . GLU B 123 ? 0.59898 0.61430 0.53916 0.00228  -0.00131 -0.01653 223 GLU B OE2 
2100 N N   . GLU B 124 ? 0.29849 0.33022 0.22880 0.00056  -0.01055 0.01306  224 GLU B N   
2101 C CA  . GLU B 124 ? 0.30070 0.34287 0.22334 0.00011  -0.01453 0.01281  224 GLU B CA  
2102 C C   . GLU B 124 ? 0.31158 0.35880 0.23555 0.00044  -0.01608 0.02367  224 GLU B C   
2103 O O   . GLU B 124 ? 0.35327 0.41024 0.26974 0.00034  -0.01702 0.02809  224 GLU B O   
2104 C CB  . GLU B 124 ? 0.32931 0.37019 0.25416 -0.00194 -0.02044 0.00548  224 GLU B CB  
2105 C CG  . GLU B 124 ? 0.46468 0.51502 0.37976 -0.00282 -0.02564 0.00297  224 GLU B CG  
2106 C CD  . GLU B 124 ? 0.79255 0.84070 0.71143 -0.00526 -0.03321 -0.00313 224 GLU B CD  
2107 O OE1 . GLU B 124 ? 0.87063 0.91082 0.79755 -0.00617 -0.03413 -0.00878 224 GLU B OE1 
2108 O OE2 . GLU B 124 ? 0.78249 0.83701 0.69728 -0.00678 -0.03912 -0.00133 224 GLU B OE2 
2109 N N   . THR B 125 ? 0.30884 0.35018 0.24267 0.00089  -0.01648 0.02814  225 THR B N   
2110 C CA  . THR B 125 ? 0.32224 0.36776 0.26032 0.00179  -0.01880 0.03722  225 THR B CA  
2111 C C   . THR B 125 ? 0.34286 0.38233 0.28697 0.00422  -0.01597 0.04416  225 THR B C   
2112 O O   . THR B 125 ? 0.30618 0.34908 0.25456 0.00543  -0.01830 0.05201  225 THR B O   
2113 C CB  . THR B 125 ? 0.33182 0.37743 0.27808 0.00123  -0.02230 0.03678  225 THR B CB  
2114 O OG1 . THR B 125 ? 0.28830 0.32492 0.24150 0.00182  -0.01924 0.03391  225 THR B OG1 
2115 C CG2 . THR B 125 ? 0.32129 0.37207 0.26323 -0.00161 -0.02733 0.03090  225 THR B CG2 
2116 N N   . GLY B 126 ? 0.29167 0.32138 0.23747 0.00485  -0.01206 0.04151  226 GLY B N   
2117 C CA  . GLY B 126 ? 0.26017 0.28163 0.21215 0.00714  -0.01067 0.04677  226 GLY B CA  
2118 C C   . GLY B 126 ? 0.28414 0.30115 0.24377 0.00881  -0.01107 0.04604  226 GLY B C   
2119 O O   . GLY B 126 ? 0.29073 0.30025 0.25495 0.01144  -0.01026 0.04900  226 GLY B O   
2120 N N   . GLY B 127 ? 0.29487 0.31670 0.25628 0.00753  -0.01251 0.04224  227 GLY B N   
2121 C CA  . GLY B 127 ? 0.25202 0.27222 0.22122 0.00915  -0.01186 0.04190  227 GLY B CA  
2122 C C   . GLY B 127 ? 0.24820 0.25829 0.21764 0.00888  -0.00824 0.03801  227 GLY B C   
2123 O O   . GLY B 127 ? 0.29360 0.29908 0.25903 0.00602  -0.00731 0.03403  227 GLY B O   
2124 N N   . VAL B 128 ? 0.26434 0.27135 0.23882 0.01197  -0.00637 0.03903  228 VAL B N   
2125 C CA  . VAL B 128 ? 0.29253 0.29001 0.26588 0.01187  -0.00319 0.03601  228 VAL B CA  
2126 C C   . VAL B 128 ? 0.26387 0.26691 0.24148 0.01075  -0.00174 0.03384  228 VAL B C   
2127 O O   . VAL B 128 ? 0.28193 0.29340 0.26586 0.01347  -0.00161 0.03583  228 VAL B O   
2128 C CB  . VAL B 128 ? 0.30227 0.29123 0.27638 0.01659  -0.00224 0.03809  228 VAL B CB  
2129 C CG1 . VAL B 128 ? 0.27052 0.24972 0.24167 0.01637  0.00062  0.03444  228 VAL B CG1 
2130 C CG2 . VAL B 128 ? 0.26367 0.24788 0.23508 0.01663  -0.00447 0.04204  228 VAL B CG2 
2131 N N   . SER B 129 ? 0.24172 0.24097 0.21730 0.00649  -0.00093 0.03074  229 SER B N   
2132 C CA  . SER B 129 ? 0.24009 0.24570 0.22016 0.00436  0.00012  0.03019  229 SER B CA  
2133 C C   . SER B 129 ? 0.25178 0.24919 0.22811 0.00245  0.00277  0.02848  229 SER B C   
2134 O O   . SER B 129 ? 0.27251 0.25844 0.24340 0.00169  0.00274  0.02733  229 SER B O   
2135 C CB  . SER B 129 ? 0.27718 0.28966 0.26099 -0.00089 -0.00401 0.02941  229 SER B CB  
2136 O OG  . SER B 129 ? 0.33265 0.33765 0.31253 -0.00448 -0.00609 0.02618  229 SER B OG  
2137 N N   . VAL B 130 ? 0.26678 0.27121 0.24633 0.00134  0.00487  0.02914  230 VAL B N   
2138 C CA  . VAL B 130 ? 0.24557 0.24460 0.22067 -0.00121 0.00726  0.02817  230 VAL B CA  
2139 C C   . VAL B 130 ? 0.27428 0.28294 0.25512 -0.00762 0.00576  0.03029  230 VAL B C   
2140 O O   . VAL B 130 ? 0.26802 0.28997 0.25662 -0.00739 0.00539  0.03294  230 VAL B O   
2141 C CB  . VAL B 130 ? 0.28810 0.28653 0.25962 0.00506  0.01235  0.02706  230 VAL B CB  
2142 C CG1 . VAL B 130 ? 0.34181 0.33940 0.30807 0.00178  0.01504  0.02639  230 VAL B CG1 
2143 C CG2 . VAL B 130 ? 0.26886 0.25376 0.23505 0.00988  0.01184  0.02530  230 VAL B CG2 
2144 N N   . ALA B 131 ? 0.23953 0.24160 0.21818 -0.01384 0.00391  0.03011  231 ALA B N   
2145 C CA  . ALA B 131 ? 0.26046 0.27074 0.24533 -0.02095 0.00152  0.03335  231 ALA B CA  
2146 C C   . ALA B 131 ? 0.29111 0.30121 0.26985 -0.02276 0.00536  0.03474  231 ALA B C   
2147 O O   . ALA B 131 ? 0.26764 0.26464 0.23768 -0.02301 0.00606  0.03258  231 ALA B O   
2148 C CB  . ALA B 131 ? 0.25208 0.25587 0.24156 -0.02769 -0.00510 0.03259  231 ALA B CB  
2149 N N   . LYS B 132 ? 0.26102 0.28628 0.24419 -0.02439 0.00751  0.03884  232 LYS B N   
2150 C CA  . LYS B 132 ? 0.25107 0.27973 0.22736 -0.02642 0.01167  0.04050  232 LYS B CA  
2151 C C   . LYS B 132 ? 0.25617 0.30339 0.24221 -0.03252 0.01063  0.04772  232 LYS B C   
2152 O O   . LYS B 132 ? 0.24894 0.30990 0.24453 -0.03002 0.01128  0.05048  232 LYS B O   
2153 C CB  . LYS B 132 ? 0.33784 0.36735 0.30551 -0.01698 0.01946  0.03648  232 LYS B CB  
2154 C CG  . LYS B 132 ? 0.42636 0.46311 0.38565 -0.01773 0.02503  0.03719  232 LYS B CG  
2155 C CD  . LYS B 132 ? 0.46349 0.48287 0.40863 -0.01974 0.02419  0.03363  232 LYS B CD  
2156 C CE  . LYS B 132 ? 0.51998 0.54748 0.45434 -0.02030 0.02982  0.03363  232 LYS B CE  
2157 N NZ  . LYS B 132 ? 0.65419 0.66347 0.57314 -0.02184 0.02835  0.02964  232 LYS B NZ  
2158 N N   . ASN B 133 ? 0.25151 0.29941 0.23638 -0.04111 0.00815  0.05188  233 ASN B N   
2159 C CA  . ASN B 133 ? 0.32986 0.39682 0.32399 -0.04795 0.00695  0.06060  233 ASN B CA  
2160 C C   . ASN B 133 ? 0.33608 0.41056 0.34748 -0.05139 -0.00044 0.06482  233 ASN B C   
2161 O O   . ASN B 133 ? 0.33532 0.42857 0.35702 -0.05348 -0.00039 0.07204  233 ASN B O   
2162 C CB  . ASN B 133 ? 0.33182 0.41611 0.32173 -0.04234 0.01659  0.06212  233 ASN B CB  
2163 C CG  . ASN B 133 ? 0.40229 0.48027 0.37418 -0.03988 0.02302  0.05772  233 ASN B CG  
2164 O OD1 . ASN B 133 ? 0.54598 0.61461 0.51095 -0.04708 0.01945  0.05882  233 ASN B OD1 
2165 N ND2 . ASN B 133 ? 0.64083 0.72314 0.60553 -0.02962 0.03181  0.05241  233 ASN B ND2 
2166 N N   . GLY B 134 ? 0.23779 0.29823 0.25259 -0.05189 -0.00701 0.06040  234 GLY B N   
2167 C CA  . GLY B 134 ? 0.25501 0.32012 0.28440 -0.05473 -0.01501 0.06257  234 GLY B CA  
2168 C C   . GLY B 134 ? 0.27859 0.34856 0.31027 -0.04700 -0.01311 0.06011  234 GLY B C   
2169 O O   . GLY B 134 ? 0.29743 0.36910 0.33935 -0.04900 -0.02056 0.06073  234 GLY B O   
2170 N N   . ASP B 135 ? 0.26481 0.33631 0.28779 -0.03841 -0.00433 0.05720  235 ASP B N   
2171 C CA  . ASP B 135 ? 0.28131 0.35726 0.30738 -0.03124 -0.00293 0.05568  235 ASP B CA  
2172 C C   . ASP B 135 ? 0.29896 0.35864 0.31571 -0.02572 -0.00258 0.04794  235 ASP B C   
2173 O O   . ASP B 135 ? 0.28705 0.33487 0.29292 -0.02366 0.00105  0.04384  235 ASP B O   
2174 C CB  . ASP B 135 ? 0.27349 0.36333 0.29943 -0.02479 0.00601  0.05809  235 ASP B CB  
2175 C CG  . ASP B 135 ? 0.34777 0.45772 0.38409 -0.02971 0.00664  0.06712  235 ASP B CG  
2176 O OD1 . ASP B 135 ? 0.30723 0.42469 0.35684 -0.03561 -0.00118 0.07301  235 ASP B OD1 
2177 O OD2 . ASP B 135 ? 0.35626 0.47504 0.38754 -0.02765 0.01467  0.06846  235 ASP B OD2 
2178 N N   . LEU B 136 ? 0.23191 0.29181 0.25298 -0.02364 -0.00676 0.04672  236 LEU B N   
2179 C CA  . LEU B 136 ? 0.23517 0.28347 0.24832 -0.01851 -0.00642 0.04106  236 LEU B CA  
2180 C C   . LEU B 136 ? 0.32481 0.38066 0.34007 -0.01137 -0.00319 0.04243  236 LEU B C   
2181 O O   . LEU B 136 ? 0.29013 0.35715 0.31491 -0.01197 -0.00653 0.04632  236 LEU B O   
2182 C CB  . LEU B 136 ? 0.27519 0.31730 0.28993 -0.02214 -0.01428 0.03792  236 LEU B CB  
2183 C CG  . LEU B 136 ? 0.27386 0.30593 0.27994 -0.01787 -0.01403 0.03273  236 LEU B CG  
2184 C CD1 . LEU B 136 ? 0.26398 0.28282 0.26136 -0.01739 -0.01051 0.02957  236 LEU B CD1 
2185 C CD2 . LEU B 136 ? 0.29467 0.32536 0.30293 -0.02079 -0.02148 0.02945  236 LEU B CD2 
2186 N N   . HIS B 137 ? 0.24134 0.29063 0.24915 -0.00491 0.00224  0.03970  237 HIS B N   
2187 C CA  . HIS B 137 ? 0.28456 0.33887 0.29541 0.00234  0.00478  0.04072  237 HIS B CA  
2188 C C   . HIS B 137 ? 0.25191 0.29585 0.25692 0.00463  0.00200  0.03816  237 HIS B C   
2189 O O   . HIS B 137 ? 0.25156 0.28302 0.24788 0.00551  0.00335  0.03492  237 HIS B O   
2190 C CB  . HIS B 137 ? 0.40558 0.46089 0.41413 0.00847  0.01243  0.03955  237 HIS B CB  
2191 C CG  . HIS B 137 ? 0.39537 0.46078 0.40609 0.00574  0.01635  0.04172  237 HIS B CG  
2192 N ND1 . HIS B 137 ? 0.52330 0.60684 0.54577 0.00550  0.01757  0.04723  237 HIS B ND1 
2193 C CD2 . HIS B 137 ? 0.50869 0.56975 0.51156 0.00248  0.01894  0.04021  237 HIS B CD2 
2194 C CE1 . HIS B 137 ? 0.48509 0.57625 0.50668 0.00236  0.02131  0.04920  237 HIS B CE1 
2195 N NE2 . HIS B 137 ? 0.55263 0.63009 0.56173 0.00034  0.02206  0.04483  237 HIS B NE2 
2196 N N   . ARG B 138 ? 0.23800 0.28784 0.24789 0.00523  -0.00217 0.04046  238 ARG B N   
2197 C CA  . ARG B 138 ? 0.25323 0.29601 0.25694 0.00569  -0.00563 0.03896  238 ARG B CA  
2198 C C   . ARG B 138 ? 0.24205 0.28686 0.24845 0.01169  -0.00502 0.04183  238 ARG B C   
2199 O O   . ARG B 138 ? 0.27097 0.32327 0.28592 0.01586  -0.00255 0.04454  238 ARG B O   
2200 C CB  . ARG B 138 ? 0.30064 0.34712 0.30516 0.00059  -0.01251 0.03863  238 ARG B CB  
2201 C CG  . ARG B 138 ? 0.34820 0.39067 0.35164 -0.00537 -0.01473 0.03526  238 ARG B CG  
2202 C CD  . ARG B 138 ? 0.39582 0.43634 0.39620 -0.00891 -0.02140 0.03162  238 ARG B CD  
2203 N NE  . ARG B 138 ? 0.35457 0.40454 0.36019 -0.00942 -0.02682 0.03459  238 ARG B NE  
2204 C CZ  . ARG B 138 ? 0.43778 0.48978 0.43901 -0.00731 -0.02899 0.03530  238 ARG B CZ  
2205 N NH1 . ARG B 138 ? 0.43071 0.47673 0.42203 -0.00494 -0.02660 0.03303  238 ARG B NH1 
2206 N NH2 . ARG B 138 ? 0.38561 0.44666 0.39321 -0.00806 -0.03408 0.03949  238 ARG B NH2 
2207 N N   . GLU B 139 ? 0.24382 0.28233 0.24370 0.01207  -0.00735 0.04153  239 GLU B N   
2208 C CA  . GLU B 139 ? 0.28704 0.32718 0.28970 0.01623  -0.00895 0.04557  239 GLU B CA  
2209 C C   . GLU B 139 ? 0.28771 0.32426 0.29518 0.02271  -0.00483 0.04595  239 GLU B C   
2210 O O   . GLU B 139 ? 0.29215 0.33462 0.30921 0.02701  -0.00549 0.04946  239 GLU B O   
2211 C CB  . GLU B 139 ? 0.26891 0.32106 0.27933 0.01529  -0.01371 0.05014  239 GLU B CB  
2212 C CG  . GLU B 139 ? 0.24866 0.30436 0.25450 0.00923  -0.01906 0.04883  239 GLU B CG  
2213 C CD  . GLU B 139 ? 0.30551 0.35652 0.29979 0.00736  -0.02150 0.04720  239 GLU B CD  
2214 O OE1 . GLU B 139 ? 0.29132 0.33716 0.28221 0.01014  -0.01950 0.04881  239 GLU B OE1 
2215 O OE2 . GLU B 139 ? 0.28580 0.33871 0.27478 0.00318  -0.02562 0.04422  239 GLU B OE2 
2216 N N   . LEU B 140 ? 0.26886 0.29494 0.26999 0.02353  -0.00120 0.04202  240 LEU B N   
2217 C CA  . LEU B 140 ? 0.34186 0.36267 0.34561 0.02988  0.00230  0.04047  240 LEU B CA  
2218 C C   . LEU B 140 ? 0.36673 0.38072 0.37221 0.03373  -0.00101 0.04329  240 LEU B C   
2219 O O   . LEU B 140 ? 0.33605 0.34433 0.33559 0.03079  -0.00408 0.04521  240 LEU B O   
2220 C CB  . LEU B 140 ? 0.29315 0.30391 0.28811 0.02865  0.00596  0.03555  240 LEU B CB  
2221 C CG  . LEU B 140 ? 0.35630 0.37330 0.34988 0.02368  0.00839  0.03392  240 LEU B CG  
2222 C CD1 . LEU B 140 ? 0.34129 0.34695 0.32543 0.02113  0.01038  0.03028  240 LEU B CD1 
2223 C CD2 . LEU B 140 ? 0.40338 0.43330 0.40551 0.02700  0.01225  0.03464  240 LEU B CD2 
2224 N N   . THR B 141 ? 0.35796 0.37307 0.37277 0.04047  -0.00049 0.04376  241 THR B N   
2225 C CA  . THR B 141 ? 0.45623 0.46218 0.47426 0.04465  -0.00423 0.04588  241 THR B CA  
2226 C C   . THR B 141 ? 0.42859 0.41904 0.43799 0.04591  -0.00273 0.04107  241 THR B C   
2227 O O   . THR B 141 ? 0.38046 0.36829 0.38251 0.04479  0.00197  0.03565  241 THR B O   
2228 C CB  . THR B 141 ? 0.46077 0.47146 0.49348 0.05215  -0.00474 0.04680  241 THR B CB  
2229 O OG1 . THR B 141 ? 0.43463 0.44589 0.46812 0.05721  0.00181  0.03987  241 THR B OG1 
2230 C CG2 . THR B 141 ? 0.51302 0.53876 0.55554 0.05036  -0.00726 0.05280  241 THR B CG2 
2231 N N   . GLU B 142 ? 0.45411 0.41005 0.68613 0.00115  0.03357  -0.02091 242 GLU B N   
2232 C CA  . GLU B 142 ? 0.48947 0.42999 0.68479 -0.00698 0.03112  -0.02927 242 GLU B CA  
2233 C C   . GLU B 142 ? 0.48239 0.42193 0.66268 0.00342  0.04533  -0.04659 242 GLU B C   
2234 O O   . GLU B 142 ? 0.43089 0.37261 0.58331 -0.00269 0.05024  -0.05106 242 GLU B O   
2235 C CB  . GLU B 142 ? 0.68327 0.59038 0.86641 -0.01319 0.01362  -0.03246 242 GLU B CB  
2236 C CG  . GLU B 142 ? 0.77889 0.66024 0.96802 -0.00090 0.01027  -0.04574 242 GLU B CG  
2237 C CD  . GLU B 142 ? 1.01732 0.86782 1.19910 -0.00859 -0.00815 -0.04493 242 GLU B CD  
2238 O OE1 . GLU B 142 ? 1.07139 0.92074 1.27511 -0.01060 -0.01753 -0.03375 242 GLU B OE1 
2239 O OE2 . GLU B 142 ? 0.95854 0.78615 1.11231 -0.01306 -0.01311 -0.05541 242 GLU B OE2 
2240 N N   . GLU B 143 ? 0.47061 0.40793 0.66932 0.01904  0.05226  -0.05646 243 GLU B N   
2241 C CA  . GLU B 143 ? 0.57619 0.51707 0.76462 0.02948  0.06764  -0.07260 243 GLU B CA  
2242 C C   . GLU B 143 ? 0.49388 0.46667 0.67910 0.02682  0.08308  -0.06729 243 GLU B C   
2243 O O   . GLU B 143 ? 0.45258 0.42706 0.61190 0.02520  0.09198  -0.07622 243 GLU B O   
2244 C CB  . GLU B 143 ? 0.64266 0.57997 0.85701 0.04694  0.07266  -0.08248 243 GLU B CB  
2245 C CG  . GLU B 143 ? 0.69679 0.60101 0.91401 0.05153  0.05846  -0.08952 243 GLU B CG  
2246 C CD  . GLU B 143 ? 0.79389 0.69365 1.03179 0.04633  0.04365  -0.07415 243 GLU B CD  
2247 O OE1 . GLU B 143 ? 0.76506 0.68321 1.03394 0.05245  0.04693  -0.06578 243 GLU B OE1 
2248 O OE2 . GLU B 143 ? 0.88254 0.76050 1.10547 0.03581  0.02886  -0.07072 243 GLU B OE2 
2249 N N   . ALA B 144 ? 0.37920 0.37729 0.59030 0.02621  0.08648  -0.05272 244 ALA B N   
2250 C CA  . ALA B 144 ? 0.33452 0.36333 0.54459 0.02385  0.10137  -0.04682 244 ALA B CA  
2251 C C   . ALA B 144 ? 0.33216 0.36299 0.51160 0.00834  0.09808  -0.04024 244 ALA B C   
2252 O O   . ALA B 144 ? 0.35504 0.39914 0.51635 0.00673  0.11042  -0.04370 244 ALA B O   
2253 C CB  . ALA B 144 ? 0.33955 0.39347 0.58441 0.02548  0.10389  -0.03169 244 ALA B CB  
2254 N N   . LEU B 145 ? 0.28540 0.30312 0.45865 -0.00333 0.08140  -0.03093 245 LEU B N   
2255 C CA  . LEU B 145 ? 0.33876 0.35857 0.48463 -0.01819 0.07699  -0.02440 245 LEU B CA  
2256 C C   . LEU B 145 ? 0.36456 0.36640 0.47465 -0.01899 0.07902  -0.04014 245 LEU B C   
2257 O O   . LEU B 145 ? 0.39715 0.40967 0.48443 -0.02460 0.08646  -0.04049 245 LEU B O   
2258 C CB  . LEU B 145 ? 0.32864 0.33769 0.47771 -0.03017 0.05837  -0.01219 245 LEU B CB  
2259 C CG  . LEU B 145 ? 0.31334 0.32071 0.43351 -0.04573 0.05133  -0.00697 245 LEU B CG  
2260 C CD1 . LEU B 145 ? 0.31615 0.35387 0.43543 -0.05077 0.06159  0.00401  245 LEU B CD1 
2261 C CD2 . LEU B 145 ? 0.31376 0.30814 0.43896 -0.05665 0.03270  0.00284  245 LEU B CD2 
2262 N N   . LYS B 146 ? 0.40383 0.37788 0.50824 -0.01347 0.07228  -0.05329 246 LYS B N   
2263 C CA  . LYS B 146 ? 0.44291 0.39857 0.51375 -0.01418 0.07360  -0.06888 246 LYS B CA  
2264 C C   . LYS B 146 ? 0.45050 0.42069 0.51318 -0.00562 0.09280  -0.07965 246 LYS B C   
2265 O O   . LYS B 146 ? 0.47874 0.44850 0.51122 -0.01080 0.09760  -0.08566 246 LYS B O   
2266 C CB  . LYS B 146 ? 0.48229 0.40586 0.55203 -0.00851 0.06363  -0.08118 246 LYS B CB  
2267 C CG  . LYS B 146 ? 0.57301 0.47316 0.60651 -0.01366 0.05911  -0.09424 246 LYS B CG  
2268 C CD  . LYS B 146 ? 0.75369 0.62147 0.78601 -0.01444 0.04327  -0.09946 246 LYS B CD  
2269 C CE  . LYS B 146 ? 0.78596 0.62985 0.78382 -0.01784 0.03999  -0.11442 246 LYS B CE  
2270 N NZ  . LYS B 146 ? 0.89596 0.73618 0.88640 -0.00503 0.05332  -0.13258 246 LYS B NZ  
2271 N N   . GLU B 147 ? 0.45641 0.43984 0.54559 0.00732  0.10409  -0.08249 247 GLU B N   
2272 C CA  . GLU B 147 ? 0.46731 0.46549 0.55022 0.01538  0.12316  -0.09324 247 GLU B CA  
2273 C C   . GLU B 147 ? 0.46360 0.48895 0.53735 0.00700  0.13270  -0.08216 247 GLU B C   
2274 O O   . GLU B 147 ? 0.49873 0.52969 0.54907 0.00656  0.14427  -0.09038 247 GLU B O   
2275 C CB  . GLU B 147 ? 0.53698 0.54320 0.65236 0.03118  0.13248  -0.09918 247 GLU B CB  
2276 C CG  . GLU B 147 ? 0.75042 0.72884 0.87099 0.04126  0.12547  -0.11358 247 GLU B CG  
2277 C CD  . GLU B 147 ? 0.93335 0.91956 1.08860 0.05691  0.13274  -0.11841 247 GLU B CD  
2278 O OE1 . GLU B 147 ? 0.90427 0.91213 1.06747 0.06410  0.14984  -0.12322 247 GLU B OE1 
2279 O OE2 . GLU B 147 ? 0.86733 0.83789 1.04180 0.06185  0.12119  -0.11748 247 GLU B OE2 
2280 N N   . MET B 148 ? 0.39460 0.43637 0.48551 -0.00010 0.12774  -0.06352 248 MET B N   
2281 C CA  . MET B 148 ? 0.43410 0.49941 0.51433 -0.00945 0.13467  -0.05194 248 MET B CA  
2282 C C   . MET B 148 ? 0.42410 0.47785 0.46527 -0.02124 0.12878  -0.05398 248 MET B C   
2283 O O   . MET B 148 ? 0.46848 0.53270 0.48753 -0.02377 0.13984  -0.05706 248 MET B O   
2284 C CB  . MET B 148 ? 0.42523 0.50693 0.53005 -0.01600 0.12768  -0.03160 248 MET B CB  
2285 C CG  . MET B 148 ? 0.52029 0.62366 0.66135 -0.00634 0.13775  -0.02648 248 MET B CG  
2286 S SD  . MET B 148 ? 0.55906 0.68515 0.72256 -0.01656 0.13133  -0.00182 248 MET B SD  
2287 C CE  . MET B 148 ? 0.55211 0.70034 0.75810 -0.00248 0.14425  -0.00032 248 MET B CE  
2288 N N   . LEU B 149 ? 0.38429 0.41612 0.41630 -0.02873 0.11123  -0.05251 249 LEU B N   
2289 C CA  . LEU B 149 ? 0.39280 0.41290 0.38887 -0.04027 0.10404  -0.05448 249 LEU B CA  
2290 C C   . LEU B 149 ? 0.51625 0.52475 0.48453 -0.03513 0.11317  -0.07336 249 LEU B C   
2291 O O   . LEU B 149 ? 0.56163 0.57426 0.50094 -0.04192 0.11731  -0.07486 249 LEU B O   
2292 C CB  . LEU B 149 ? 0.37489 0.37197 0.36882 -0.04803 0.08396  -0.05159 249 LEU B CB  
2293 C CG  . LEU B 149 ? 0.38804 0.39614 0.40199 -0.05708 0.07319  -0.03218 249 LEU B CG  
2294 C CD1 . LEU B 149 ? 0.37355 0.35703 0.38690 -0.06334 0.05451  -0.03177 249 LEU B CD1 
2295 C CD2 . LEU B 149 ? 0.45934 0.48538 0.45670 -0.06877 0.07442  -0.02105 249 LEU B CD2 
2296 N N   . GLU B 150 ? 0.46230 0.45588 0.43876 -0.02318 0.11607  -0.08808 250 GLU B N   
2297 C CA  . GLU B 150 ? 0.52972 0.51225 0.48138 -0.01771 0.12511  -0.10701 250 GLU B CA  
2298 C C   . GLU B 150 ? 0.60804 0.61455 0.55408 -0.01419 0.14476  -0.10922 250 GLU B C   
2299 O O   . GLU B 150 ? 0.63722 0.64211 0.55223 -0.01763 0.15107  -0.11739 250 GLU B O   
2300 C CB  . GLU B 150 ? 0.50016 0.46288 0.46538 -0.00494 0.12418  -0.12181 250 GLU B CB  
2301 C CG  . GLU B 150 ? 0.53608 0.46835 0.49163 -0.00981 0.10584  -0.12519 250 GLU B CG  
2302 C CD  . GLU B 150 ? 0.80526 0.71854 0.78124 0.00190  0.10165  -0.13474 250 GLU B CD  
2303 O OE1 . GLU B 150 ? 0.81972 0.74482 0.82251 0.01370  0.11106  -0.13634 250 GLU B OE1 
2304 O OE2 . GLU B 150 ? 0.88070 0.76676 0.84581 -0.00084 0.08858  -0.14071 250 GLU B OE2 
2305 N N   . ALA B 151 ? 0.49899 0.52804 0.47421 -0.00786 0.15462  -0.10187 251 ALA B N   
2306 C CA  . ALA B 151 ? 0.59136 0.64441 0.56243 -0.00535 0.17367  -0.10292 251 ALA B CA  
2307 C C   . ALA B 151 ? 0.69077 0.75634 0.63812 -0.01896 0.17341  -0.09082 251 ALA B C   
2308 O O   . ALA B 151 ? 0.70461 0.77801 0.62815 -0.02052 0.18553  -0.09651 251 ALA B O   
2309 C CB  . ALA B 151 ? 0.51357 0.58844 0.52274 0.00346  0.18310  -0.09644 251 ALA B CB  
2310 N N   . GLU B 152 ? 0.63991 0.70686 0.59264 -0.02910 0.15938  -0.07442 252 GLU B N   
2311 C CA  . GLU B 152 ? 0.77784 0.85876 0.71227 -0.04155 0.15876  -0.06142 252 GLU B CA  
2312 C C   . GLU B 152 ? 0.80230 0.86596 0.69711 -0.05079 0.15084  -0.06742 252 GLU B C   
2313 O O   . GLU B 152 ? 1.02193 1.09591 0.89314 -0.05830 0.15562  -0.06317 252 GLU B O   
2314 C CB  . GLU B 152 ? 0.70746 0.79832 0.66488 -0.04871 0.14723  -0.04161 252 GLU B CB  
2315 C CG  . GLU B 152 ? 0.69984 0.81155 0.69537 -0.04060 0.15615  -0.03408 252 GLU B CG  
2316 C CD  . GLU B 152 ? 0.90488 1.04224 0.89860 -0.03898 0.17490  -0.03141 252 GLU B CD  
2317 O OE1 . GLU B 152 ? 0.85278 1.00125 0.82912 -0.04933 0.17511  -0.02103 252 GLU B OE1 
2318 O OE2 . GLU B 152 ? 0.92479 1.07086 0.93424 -0.02748 0.18930  -0.03996 252 GLU B OE2 
2319 N N   . PHE B 153 ? 0.64544 0.68278 0.53198 -0.05044 0.13886  -0.07735 253 PHE B N   
2320 C CA  . PHE B 153 ? 0.74602 0.76661 0.59569 -0.05938 0.13063  -0.08340 253 PHE B CA  
2321 C C   . PHE B 153 ? 0.92614 0.94382 0.74791 -0.05506 0.14428  -0.09976 253 PHE B C   
2322 O O   . PHE B 153 ? 1.06286 1.07372 0.85133 -0.06323 0.14108  -0.10284 253 PHE B O   
2323 C CB  . PHE B 153 ? 0.83565 0.82867 0.68538 -0.06089 0.11358  -0.08898 253 PHE B CB  
2324 C CG  . PHE B 153 ? 0.89212 0.88277 0.74580 -0.07308 0.09593  -0.07392 253 PHE B CG  
2325 C CD1 . PHE B 153 ? 0.82555 0.82399 0.71275 -0.07279 0.08982  -0.06073 253 PHE B CD1 
2326 C CD2 . PHE B 153 ? 0.94167 0.92214 0.76572 -0.08487 0.08531  -0.07365 253 PHE B CD2 
2327 C CE1 . PHE B 153 ? 0.83998 0.83636 0.73103 -0.08436 0.07378  -0.04757 253 PHE B CE1 
2328 C CE2 . PHE B 153 ? 0.81985 0.79834 0.64807 -0.09622 0.06910  -0.06081 253 PHE B CE2 
2329 C CZ  . PHE B 153 ? 0.71556 0.70204 0.57732 -0.09609 0.06350  -0.04784 253 PHE B CZ  
2330 N N   . LYS B 154 ? 0.87211 0.89512 0.70690 -0.04254 0.15928  -0.11052 254 LYS B N   
2331 C CA  . LYS B 154 ? 1.08144 1.10245 0.89158 -0.03796 0.17335  -0.12701 254 LYS B CA  
2332 C C   . LYS B 154 ? 1.15500 1.19118 0.93747 -0.04701 0.18066  -0.12092 254 LYS B C   
2333 O O   . LYS B 154 ? 1.19721 1.22261 0.94509 -0.05227 0.17959  -0.12916 254 LYS B O   
2334 C CB  . LYS B 154 ? 0.89579 0.92661 0.72984 -0.02369 0.18957  -0.13638 254 LYS B CB  
2335 C CG  . LYS B 154 ? 0.96449 0.97572 0.81766 -0.01311 0.18410  -0.14826 254 LYS B CG  
2336 C CD  . LYS B 154 ? 0.93441 0.96008 0.82703 -0.00143 0.19274  -0.14650 254 LYS B CD  
2337 C CE  . LYS B 154 ? 1.02184 1.07038 0.91546 0.00422  0.21442  -0.15135 254 LYS B CE  
2338 N NZ  . LYS B 154 ? 1.03312 1.09884 0.96677 0.01404  0.22193  -0.14690 254 LYS B NZ  
2339 N N   . LYS B 155 ? 1.09062 1.15158 0.88785 -0.04890 0.18803  -0.10644 255 LYS B N   
2340 C CA  . LYS B 155 ? 1.16370 1.23958 0.93764 -0.05879 0.19247  -0.09668 255 LYS B CA  
2341 C C   . LYS B 155 ? 1.26088 1.36250 1.06054 -0.06021 0.19742  -0.07865 255 LYS B C   
2342 O O   . LYS B 155 ? 1.12641 1.23585 0.96096 -0.05230 0.20038  -0.07589 255 LYS B O   
2343 C CB  . LYS B 155 ? 1.03206 1.11096 0.77840 -0.05617 0.20927  -0.11027 255 LYS B CB  
2344 C CG  . LYS B 155 ? 0.91814 0.98798 0.62216 -0.06688 0.20373  -0.11173 255 LYS B CG  
2345 C CD  . LYS B 155 ? 1.04387 1.12471 0.74325 -0.07909 0.19417  -0.09155 255 LYS B CD  
2346 C CE  . LYS B 155 ? 0.90459 1.00687 0.61390 -0.07572 0.20203  -0.07816 255 LYS B CE  
2347 N NZ  . LYS B 155 ? 0.65387 0.75330 0.33764 -0.07202 0.20983  -0.08677 255 LYS B NZ  
# 
